data_7HD1
# 
_entry.id   7HD1 
# 
_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   7HD1         pdb_00007hd1 10.2210/pdb7hd1/pdb 
WWPDB D_1001407319 ?            ?                   
# 
_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                        7HD1 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                       18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn '[(2S)-4,4-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' 246.308   1   ? ? ? ? 
3 water       nat water                                                                            18.015    427 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '[(2S)-4,4-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' A1A6Z 
3 water                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A6Z non-polymer         . '[(2S)-4,4-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' ? 'C13 H18 N4 O'   
246.308 
ALA   'L-peptide linking' y ALANINE                                                                          ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                         ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                       ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                  ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                         ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                            ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A6Z 1   201 201  A1A6Z LA1 A . 
D 3 HOH   1   301 192  HOH   HOH A . 
D 3 HOH   2   302 493  HOH   HOH A . 
D 3 HOH   3   303 109  HOH   HOH A . 
D 3 HOH   4   304 292  HOH   HOH A . 
D 3 HOH   5   305 393  HOH   HOH A . 
D 3 HOH   6   306 196  HOH   HOH A . 
D 3 HOH   7   307 26   HOH   HOH A . 
D 3 HOH   8   308 136  HOH   HOH A . 
D 3 HOH   9   309 964  HOH   HOH A . 
D 3 HOH   10  310 132  HOH   HOH A . 
D 3 HOH   11  311 625  HOH   HOH A . 
D 3 HOH   12  312 209  HOH   HOH A . 
D 3 HOH   13  313 461  HOH   HOH A . 
D 3 HOH   14  314 1309 HOH   HOH A . 
D 3 HOH   15  315 1300 HOH   HOH A . 
D 3 HOH   16  316 3    HOH   HOH A . 
D 3 HOH   17  317 153  HOH   HOH A . 
D 3 HOH   18  318 1295 HOH   HOH A . 
D 3 HOH   19  319 247  HOH   HOH A . 
D 3 HOH   20  320 1283 HOH   HOH A . 
D 3 HOH   21  321 124  HOH   HOH A . 
D 3 HOH   22  322 76   HOH   HOH A . 
D 3 HOH   23  323 1290 HOH   HOH A . 
D 3 HOH   24  324 661  HOH   HOH A . 
D 3 HOH   25  325 199  HOH   HOH A . 
D 3 HOH   26  326 229  HOH   HOH A . 
D 3 HOH   27  327 105  HOH   HOH A . 
D 3 HOH   28  328 57   HOH   HOH A . 
D 3 HOH   29  329 241  HOH   HOH A . 
D 3 HOH   30  330 151  HOH   HOH A . 
D 3 HOH   31  331 21   HOH   HOH A . 
D 3 HOH   32  332 36   HOH   HOH A . 
D 3 HOH   33  333 381  HOH   HOH A . 
D 3 HOH   34  334 337  HOH   HOH A . 
D 3 HOH   35  335 165  HOH   HOH A . 
D 3 HOH   36  336 630  HOH   HOH A . 
D 3 HOH   37  337 140  HOH   HOH A . 
D 3 HOH   38  338 225  HOH   HOH A . 
D 3 HOH   39  339 236  HOH   HOH A . 
D 3 HOH   40  340 396  HOH   HOH A . 
D 3 HOH   41  341 164  HOH   HOH A . 
D 3 HOH   42  342 1301 HOH   HOH A . 
D 3 HOH   43  343 42   HOH   HOH A . 
D 3 HOH   44  344 469  HOH   HOH A . 
D 3 HOH   45  345 15   HOH   HOH A . 
D 3 HOH   46  346 20   HOH   HOH A . 
D 3 HOH   47  347 169  HOH   HOH A . 
D 3 HOH   48  348 18   HOH   HOH A . 
D 3 HOH   49  349 366  HOH   HOH A . 
D 3 HOH   50  350 218  HOH   HOH A . 
D 3 HOH   51  351 12   HOH   HOH A . 
D 3 HOH   52  352 212  HOH   HOH A . 
D 3 HOH   53  353 93   HOH   HOH A . 
D 3 HOH   54  354 320  HOH   HOH A . 
D 3 HOH   55  355 5    HOH   HOH A . 
D 3 HOH   56  356 6    HOH   HOH A . 
D 3 HOH   57  357 92   HOH   HOH A . 
D 3 HOH   58  358 281  HOH   HOH A . 
D 3 HOH   59  359 354  HOH   HOH A . 
D 3 HOH   60  360 56   HOH   HOH A . 
D 3 HOH   61  361 13   HOH   HOH A . 
D 3 HOH   62  362 19   HOH   HOH A . 
D 3 HOH   63  363 33   HOH   HOH A . 
D 3 HOH   64  364 2    HOH   HOH A . 
D 3 HOH   65  365 86   HOH   HOH A . 
D 3 HOH   66  366 66   HOH   HOH A . 
D 3 HOH   67  367 155  HOH   HOH A . 
D 3 HOH   68  368 186  HOH   HOH A . 
D 3 HOH   69  369 3    HOH   HOH A . 
D 3 HOH   70  370 96   HOH   HOH A . 
D 3 HOH   71  371 278  HOH   HOH A . 
D 3 HOH   72  372 162  HOH   HOH A . 
D 3 HOH   73  373 939  HOH   HOH A . 
D 3 HOH   74  374 102  HOH   HOH A . 
D 3 HOH   75  375 49   HOH   HOH A . 
D 3 HOH   76  376 138  HOH   HOH A . 
D 3 HOH   77  377 45   HOH   HOH A . 
D 3 HOH   78  378 17   HOH   HOH A . 
D 3 HOH   79  379 46   HOH   HOH A . 
D 3 HOH   80  380 78   HOH   HOH A . 
D 3 HOH   81  381 1310 HOH   HOH A . 
D 3 HOH   82  382 134  HOH   HOH A . 
D 3 HOH   83  383 409  HOH   HOH A . 
D 3 HOH   84  384 159  HOH   HOH A . 
D 3 HOH   85  385 74   HOH   HOH A . 
D 3 HOH   86  386 9    HOH   HOH A . 
D 3 HOH   87  387 405  HOH   HOH A . 
D 3 HOH   88  388 83   HOH   HOH A . 
D 3 HOH   89  389 662  HOH   HOH A . 
D 3 HOH   90  390 139  HOH   HOH A . 
D 3 HOH   91  391 35   HOH   HOH A . 
D 3 HOH   92  392 4    HOH   HOH A . 
D 3 HOH   93  393 148  HOH   HOH A . 
D 3 HOH   94  394 6    HOH   HOH A . 
D 3 HOH   95  395 67   HOH   HOH A . 
D 3 HOH   96  396 27   HOH   HOH A . 
D 3 HOH   97  397 85   HOH   HOH A . 
D 3 HOH   98  398 24   HOH   HOH A . 
D 3 HOH   99  399 195  HOH   HOH A . 
D 3 HOH   100 400 952  HOH   HOH A . 
D 3 HOH   101 401 2    HOH   HOH A . 
D 3 HOH   102 402 1313 HOH   HOH A . 
D 3 HOH   103 403 68   HOH   HOH A . 
D 3 HOH   104 404 39   HOH   HOH A . 
D 3 HOH   105 405 1068 HOH   HOH A . 
D 3 HOH   106 406 1289 HOH   HOH A . 
D 3 HOH   107 407 58   HOH   HOH A . 
D 3 HOH   108 408 154  HOH   HOH A . 
D 3 HOH   109 409 116  HOH   HOH A . 
D 3 HOH   110 410 8    HOH   HOH A . 
D 3 HOH   111 411 51   HOH   HOH A . 
D 3 HOH   112 412 944  HOH   HOH A . 
D 3 HOH   113 413 12   HOH   HOH A . 
D 3 HOH   114 414 1308 HOH   HOH A . 
D 3 HOH   115 415 303  HOH   HOH A . 
D 3 HOH   116 416 34   HOH   HOH A . 
D 3 HOH   117 417 582  HOH   HOH A . 
D 3 HOH   118 418 1315 HOH   HOH A . 
D 3 HOH   119 419 1094 HOH   HOH A . 
D 3 HOH   120 420 70   HOH   HOH A . 
D 3 HOH   121 421 1222 HOH   HOH A . 
D 3 HOH   122 422 123  HOH   HOH A . 
D 3 HOH   123 423 53   HOH   HOH A . 
D 3 HOH   124 424 156  HOH   HOH A . 
D 3 HOH   125 425 122  HOH   HOH A . 
D 3 HOH   126 426 296  HOH   HOH A . 
D 3 HOH   127 427 1275 HOH   HOH A . 
D 3 HOH   128 428 397  HOH   HOH A . 
D 3 HOH   129 429 115  HOH   HOH A . 
D 3 HOH   130 430 121  HOH   HOH A . 
D 3 HOH   131 431 1296 HOH   HOH A . 
D 3 HOH   132 432 125  HOH   HOH A . 
D 3 HOH   133 433 7    HOH   HOH A . 
D 3 HOH   134 434 25   HOH   HOH A . 
D 3 HOH   135 435 95   HOH   HOH A . 
D 3 HOH   136 436 16   HOH   HOH A . 
D 3 HOH   137 437 333  HOH   HOH A . 
D 3 HOH   138 438 1134 HOH   HOH A . 
D 3 HOH   139 439 16   HOH   HOH A . 
D 3 HOH   140 440 1238 HOH   HOH A . 
D 3 HOH   141 441 4    HOH   HOH A . 
D 3 HOH   142 442 73   HOH   HOH A . 
D 3 HOH   143 443 1    HOH   HOH A . 
D 3 HOH   144 444 351  HOH   HOH A . 
D 3 HOH   145 445 80   HOH   HOH A . 
D 3 HOH   146 446 1279 HOH   HOH A . 
D 3 HOH   147 447 1189 HOH   HOH A . 
D 3 HOH   148 448 71   HOH   HOH A . 
D 3 HOH   149 449 576  HOH   HOH A . 
D 3 HOH   150 450 94   HOH   HOH A . 
D 3 HOH   151 451 104  HOH   HOH A . 
D 3 HOH   152 452 40   HOH   HOH A . 
D 3 HOH   153 453 79   HOH   HOH A . 
D 3 HOH   154 454 188  HOH   HOH A . 
D 3 HOH   155 455 8    HOH   HOH A . 
D 3 HOH   156 456 97   HOH   HOH A . 
D 3 HOH   157 457 10   HOH   HOH A . 
D 3 HOH   158 458 330  HOH   HOH A . 
D 3 HOH   159 459 1286 HOH   HOH A . 
D 3 HOH   160 460 163  HOH   HOH A . 
D 3 HOH   161 461 107  HOH   HOH A . 
D 3 HOH   162 462 509  HOH   HOH A . 
D 3 HOH   163 463 726  HOH   HOH A . 
D 3 HOH   164 464 1119 HOH   HOH A . 
D 3 HOH   165 465 756  HOH   HOH A . 
D 3 HOH   166 466 408  HOH   HOH A . 
D 3 HOH   167 467 5    HOH   HOH A . 
D 3 HOH   168 468 319  HOH   HOH A . 
D 3 HOH   169 469 361  HOH   HOH A . 
D 3 HOH   170 470 1276 HOH   HOH A . 
D 3 HOH   171 471 342  HOH   HOH A . 
D 3 HOH   172 472 801  HOH   HOH A . 
D 3 HOH   173 473 556  HOH   HOH A . 
D 3 HOH   174 474 63   HOH   HOH A . 
D 3 HOH   175 475 126  HOH   HOH A . 
D 3 HOH   176 476 370  HOH   HOH A . 
D 3 HOH   177 477 250  HOH   HOH A . 
D 3 HOH   178 478 1307 HOH   HOH A . 
D 3 HOH   179 479 280  HOH   HOH A . 
D 3 HOH   180 480 224  HOH   HOH A . 
D 3 HOH   181 481 1287 HOH   HOH A . 
D 3 HOH   182 482 135  HOH   HOH A . 
D 3 HOH   183 483 521  HOH   HOH A . 
D 3 HOH   184 484 1306 HOH   HOH A . 
D 3 HOH   185 485 711  HOH   HOH A . 
D 3 HOH   186 486 674  HOH   HOH A . 
D 3 HOH   187 487 919  HOH   HOH A . 
D 3 HOH   188 488 695  HOH   HOH A . 
D 3 HOH   189 489 202  HOH   HOH A . 
D 3 HOH   190 490 318  HOH   HOH A . 
D 3 HOH   191 491 326  HOH   HOH A . 
D 3 HOH   192 492 267  HOH   HOH A . 
D 3 HOH   193 493 1314 HOH   HOH A . 
D 3 HOH   194 494 1299 HOH   HOH A . 
D 3 HOH   195 495 331  HOH   HOH A . 
D 3 HOH   196 496 309  HOH   HOH A . 
D 3 HOH   197 497 315  HOH   HOH A . 
D 3 HOH   198 498 941  HOH   HOH A . 
D 3 HOH   199 499 805  HOH   HOH A . 
D 3 HOH   200 500 1284 HOH   HOH A . 
D 3 HOH   201 501 263  HOH   HOH A . 
D 3 HOH   202 502 356  HOH   HOH A . 
D 3 HOH   203 503 208  HOH   HOH A . 
D 3 HOH   204 504 981  HOH   HOH A . 
D 3 HOH   205 505 152  HOH   HOH A . 
D 3 HOH   206 506 1071 HOH   HOH A . 
D 3 HOH   207 507 11   HOH   HOH A . 
D 3 HOH   208 508 350  HOH   HOH A . 
D 3 HOH   209 509 7    HOH   HOH A . 
D 3 HOH   210 510 14   HOH   HOH A . 
D 3 HOH   211 511 180  HOH   HOH A . 
D 3 HOH   212 512 363  HOH   HOH A . 
D 3 HOH   213 513 371  HOH   HOH A . 
D 3 HOH   214 514 313  HOH   HOH A . 
D 3 HOH   215 515 17   HOH   HOH A . 
D 3 HOH   216 516 19   HOH   HOH A . 
D 3 HOH   217 517 185  HOH   HOH A . 
D 3 HOH   218 518 429  HOH   HOH A . 
D 3 HOH   219 519 772  HOH   HOH A . 
D 3 HOH   220 520 376  HOH   HOH A . 
D 3 HOH   221 521 1074 HOH   HOH A . 
D 3 HOH   222 522 1292 HOH   HOH A . 
D 3 HOH   223 523 346  HOH   HOH A . 
D 3 HOH   224 524 18   HOH   HOH A . 
D 3 HOH   225 525 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 240  HOH   HOH B . 
E 3 HOH   3   203 549  HOH   HOH B . 
E 3 HOH   4   204 900  HOH   HOH B . 
E 3 HOH   5   205 1249 HOH   HOH B . 
E 3 HOH   6   206 364  HOH   HOH B . 
E 3 HOH   7   207 398  HOH   HOH B . 
E 3 HOH   8   208 232  HOH   HOH B . 
E 3 HOH   9   209 205  HOH   HOH B . 
E 3 HOH   10  210 120  HOH   HOH B . 
E 3 HOH   11  211 654  HOH   HOH B . 
E 3 HOH   12  212 444  HOH   HOH B . 
E 3 HOH   13  213 264  HOH   HOH B . 
E 3 HOH   14  214 50   HOH   HOH B . 
E 3 HOH   15  215 353  HOH   HOH B . 
E 3 HOH   16  216 758  HOH   HOH B . 
E 3 HOH   17  217 75   HOH   HOH B . 
E 3 HOH   18  218 358  HOH   HOH B . 
E 3 HOH   19  219 332  HOH   HOH B . 
E 3 HOH   20  220 172  HOH   HOH B . 
E 3 HOH   21  221 15   HOH   HOH B . 
E 3 HOH   22  222 452  HOH   HOH B . 
E 3 HOH   23  223 531  HOH   HOH B . 
E 3 HOH   24  224 54   HOH   HOH B . 
E 3 HOH   25  225 166  HOH   HOH B . 
E 3 HOH   26  226 82   HOH   HOH B . 
E 3 HOH   27  227 743  HOH   HOH B . 
E 3 HOH   28  228 131  HOH   HOH B . 
E 3 HOH   29  229 60   HOH   HOH B . 
E 3 HOH   30  230 1278 HOH   HOH B . 
E 3 HOH   31  231 127  HOH   HOH B . 
E 3 HOH   32  232 128  HOH   HOH B . 
E 3 HOH   33  233 81   HOH   HOH B . 
E 3 HOH   34  234 103  HOH   HOH B . 
E 3 HOH   35  235 110  HOH   HOH B . 
E 3 HOH   36  236 276  HOH   HOH B . 
E 3 HOH   37  237 343  HOH   HOH B . 
E 3 HOH   38  238 41   HOH   HOH B . 
E 3 HOH   39  239 1312 HOH   HOH B . 
E 3 HOH   40  240 181  HOH   HOH B . 
E 3 HOH   41  241 391  HOH   HOH B . 
E 3 HOH   42  242 325  HOH   HOH B . 
E 3 HOH   43  243 133  HOH   HOH B . 
E 3 HOH   44  244 282  HOH   HOH B . 
E 3 HOH   45  245 30   HOH   HOH B . 
E 3 HOH   46  246 272  HOH   HOH B . 
E 3 HOH   47  247 69   HOH   HOH B . 
E 3 HOH   48  248 300  HOH   HOH B . 
E 3 HOH   49  249 1    HOH   HOH B . 
E 3 HOH   50  250 14   HOH   HOH B . 
E 3 HOH   51  251 129  HOH   HOH B . 
E 3 HOH   52  252 72   HOH   HOH B . 
E 3 HOH   53  253 62   HOH   HOH B . 
E 3 HOH   54  254 52   HOH   HOH B . 
E 3 HOH   55  255 723  HOH   HOH B . 
E 3 HOH   56  256 150  HOH   HOH B . 
E 3 HOH   57  257 77   HOH   HOH B . 
E 3 HOH   58  258 31   HOH   HOH B . 
E 3 HOH   59  259 47   HOH   HOH B . 
E 3 HOH   60  260 231  HOH   HOH B . 
E 3 HOH   61  261 9    HOH   HOH B . 
E 3 HOH   62  262 144  HOH   HOH B . 
E 3 HOH   63  263 271  HOH   HOH B . 
E 3 HOH   64  264 1106 HOH   HOH B . 
E 3 HOH   65  265 10   HOH   HOH B . 
E 3 HOH   66  266 243  HOH   HOH B . 
E 3 HOH   67  267 61   HOH   HOH B . 
E 3 HOH   68  268 1285 HOH   HOH B . 
E 3 HOH   69  269 1140 HOH   HOH B . 
E 3 HOH   70  270 59   HOH   HOH B . 
E 3 HOH   71  271 242  HOH   HOH B . 
E 3 HOH   72  272 20   HOH   HOH B . 
E 3 HOH   73  273 114  HOH   HOH B . 
E 3 HOH   74  274 84   HOH   HOH B . 
E 3 HOH   75  275 221  HOH   HOH B . 
E 3 HOH   76  276 143  HOH   HOH B . 
E 3 HOH   77  277 11   HOH   HOH B . 
E 3 HOH   78  278 117  HOH   HOH B . 
E 3 HOH   79  279 302  HOH   HOH B . 
E 3 HOH   80  280 1305 HOH   HOH B . 
E 3 HOH   81  281 287  HOH   HOH B . 
E 3 HOH   82  282 347  HOH   HOH B . 
E 3 HOH   83  283 88   HOH   HOH B . 
E 3 HOH   84  284 1277 HOH   HOH B . 
E 3 HOH   85  285 175  HOH   HOH B . 
E 3 HOH   86  286 22   HOH   HOH B . 
E 3 HOH   87  287 43   HOH   HOH B . 
E 3 HOH   88  288 1066 HOH   HOH B . 
E 3 HOH   89  289 252  HOH   HOH B . 
E 3 HOH   90  290 220  HOH   HOH B . 
E 3 HOH   91  291 106  HOH   HOH B . 
E 3 HOH   92  292 89   HOH   HOH B . 
E 3 HOH   93  293 235  HOH   HOH B . 
E 3 HOH   94  294 13   HOH   HOH B . 
E 3 HOH   95  295 147  HOH   HOH B . 
E 3 HOH   96  296 316  HOH   HOH B . 
E 3 HOH   97  297 416  HOH   HOH B . 
E 3 HOH   98  298 207  HOH   HOH B . 
E 3 HOH   99  299 137  HOH   HOH B . 
E 3 HOH   100 300 216  HOH   HOH B . 
E 3 HOH   101 301 99   HOH   HOH B . 
E 3 HOH   102 302 311  HOH   HOH B . 
E 3 HOH   103 303 112  HOH   HOH B . 
E 3 HOH   104 304 445  HOH   HOH B . 
E 3 HOH   105 305 387  HOH   HOH B . 
E 3 HOH   106 306 299  HOH   HOH B . 
E 3 HOH   107 307 160  HOH   HOH B . 
E 3 HOH   108 308 297  HOH   HOH B . 
E 3 HOH   109 309 38   HOH   HOH B . 
E 3 HOH   110 310 37   HOH   HOH B . 
E 3 HOH   111 311 32   HOH   HOH B . 
E 3 HOH   112 312 142  HOH   HOH B . 
E 3 HOH   113 313 635  HOH   HOH B . 
E 3 HOH   114 314 170  HOH   HOH B . 
E 3 HOH   115 315 101  HOH   HOH B . 
E 3 HOH   116 316 215  HOH   HOH B . 
E 3 HOH   117 317 23   HOH   HOH B . 
E 3 HOH   118 318 91   HOH   HOH B . 
E 3 HOH   119 319 141  HOH   HOH B . 
E 3 HOH   120 320 1294 HOH   HOH B . 
E 3 HOH   121 321 197  HOH   HOH B . 
E 3 HOH   122 322 48   HOH   HOH B . 
E 3 HOH   123 323 118  HOH   HOH B . 
E 3 HOH   124 324 1291 HOH   HOH B . 
E 3 HOH   125 325 44   HOH   HOH B . 
E 3 HOH   126 326 334  HOH   HOH B . 
E 3 HOH   127 327 704  HOH   HOH B . 
E 3 HOH   128 328 177  HOH   HOH B . 
E 3 HOH   129 329 717  HOH   HOH B . 
E 3 HOH   130 330 100  HOH   HOH B . 
E 3 HOH   131 331 28   HOH   HOH B . 
E 3 HOH   132 332 1274 HOH   HOH B . 
E 3 HOH   133 333 29   HOH   HOH B . 
E 3 HOH   134 334 55   HOH   HOH B . 
E 3 HOH   135 335 98   HOH   HOH B . 
E 3 HOH   136 336 182  HOH   HOH B . 
E 3 HOH   137 337 339  HOH   HOH B . 
E 3 HOH   138 338 1126 HOH   HOH B . 
E 3 HOH   139 339 1293 HOH   HOH B . 
E 3 HOH   140 340 161  HOH   HOH B . 
E 3 HOH   141 341 234  HOH   HOH B . 
E 3 HOH   142 342 341  HOH   HOH B . 
E 3 HOH   143 343 65   HOH   HOH B . 
E 3 HOH   144 344 362  HOH   HOH B . 
E 3 HOH   145 345 619  HOH   HOH B . 
E 3 HOH   146 346 87   HOH   HOH B . 
E 3 HOH   147 347 90   HOH   HOH B . 
E 3 HOH   148 348 463  HOH   HOH B . 
E 3 HOH   149 349 1280 HOH   HOH B . 
E 3 HOH   150 350 191  HOH   HOH B . 
E 3 HOH   151 351 960  HOH   HOH B . 
E 3 HOH   152 352 178  HOH   HOH B . 
E 3 HOH   153 353 335  HOH   HOH B . 
E 3 HOH   154 354 1046 HOH   HOH B . 
E 3 HOH   155 355 1304 HOH   HOH B . 
E 3 HOH   156 356 203  HOH   HOH B . 
E 3 HOH   157 357 623  HOH   HOH B . 
E 3 HOH   158 358 304  HOH   HOH B . 
E 3 HOH   159 359 1077 HOH   HOH B . 
E 3 HOH   160 360 290  HOH   HOH B . 
E 3 HOH   161 361 541  HOH   HOH B . 
E 3 HOH   162 362 718  HOH   HOH B . 
E 3 HOH   163 363 389  HOH   HOH B . 
E 3 HOH   164 364 283  HOH   HOH B . 
E 3 HOH   165 365 1072 HOH   HOH B . 
E 3 HOH   166 366 479  HOH   HOH B . 
E 3 HOH   167 367 615  HOH   HOH B . 
E 3 HOH   168 368 291  HOH   HOH B . 
E 3 HOH   169 369 340  HOH   HOH B . 
E 3 HOH   170 370 373  HOH   HOH B . 
E 3 HOH   171 371 898  HOH   HOH B . 
E 3 HOH   172 372 1316 HOH   HOH B . 
E 3 HOH   173 373 667  HOH   HOH B . 
E 3 HOH   174 374 190  HOH   HOH B . 
E 3 HOH   175 375 310  HOH   HOH B . 
E 3 HOH   176 376 1303 HOH   HOH B . 
E 3 HOH   177 377 431  HOH   HOH B . 
E 3 HOH   178 378 1173 HOH   HOH B . 
E 3 HOH   179 379 418  HOH   HOH B . 
E 3 HOH   180 380 183  HOH   HOH B . 
E 3 HOH   181 381 149  HOH   HOH B . 
E 3 HOH   182 382 1000 HOH   HOH B . 
E 3 HOH   183 383 1311 HOH   HOH B . 
E 3 HOH   184 384 1163 HOH   HOH B . 
E 3 HOH   185 385 424  HOH   HOH B . 
E 3 HOH   186 386 491  HOH   HOH B . 
E 3 HOH   187 387 176  HOH   HOH B . 
E 3 HOH   188 388 265  HOH   HOH B . 
E 3 HOH   189 389 470  HOH   HOH B . 
E 3 HOH   190 390 248  HOH   HOH B . 
E 3 HOH   191 391 1298 HOH   HOH B . 
E 3 HOH   192 392 184  HOH   HOH B . 
E 3 HOH   193 393 360  HOH   HOH B . 
E 3 HOH   194 394 410  HOH   HOH B . 
E 3 HOH   195 395 355  HOH   HOH B . 
E 3 HOH   196 396 314  HOH   HOH B . 
E 3 HOH   197 397 274  HOH   HOH B . 
E 3 HOH   198 398 566  HOH   HOH B . 
E 3 HOH   199 399 157  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 HOH   201 401 792  HOH   HOH B . 
E 3 HOH   202 402 558  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           7HD1 
_cell.length_a           88.833 
_cell.length_b           88.833 
_cell.length_c           39.402 
_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                         7HD1 
_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          7HD1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.56 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HD1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.420 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   174493 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.100 
_reflns.pdbx_Rmerge_I_obs            0.046 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.400 
_reflns.B_iso_Wilson_estimate        11.800 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.050 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1082342 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.980 1.000  ? 26284 7620 ? 1.218 ? ? ? 3.400 ? 0.600  ? ? ? ? ? ? 88.100 1.430 0.728 0.462 
1 2 5.370 44.420 ? 8047  1161 ? 0.029 ? ? ? 6.900 ? 49.900 ? ? ? ? ? ? 99.800 0.031 0.012 0.999 
# 
_refine.entry_id                                 7HD1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             44.4200 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.9900 
_refine.ls_number_reflns_obs                     174307 
_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                          0.1475 
_refine.ls_R_factor_R_work                       0.1469 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1588 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  8418 
_refine.ls_number_reflns_R_work                  165889 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.1511 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1300 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                87.580 
_refine.B_iso_min                                7.740 
_refine.pdbx_overall_phase_error                 18.5500 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9800 
_refine_hist.d_res_low                        44.4200 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             427 
_refine_hist.number_atoms_total               3005 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.44 
_refine_hist.pdbx_B_iso_mean_solvent          31.64 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9800 0.9900  30 84.0000  4647 . 0.4635 0.4530 . 251 0.0000 4898 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 93.0000  5171 . 0.4045 0.4051 . 262 0.0000 5433 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 96.0000  5264 . 0.3527 0.3033 . 269 0.0000 5533 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 98.0000  5518 . 0.2934 0.2840 . 240 0.0000 5758 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5521 . 0.2589 0.2549 . 316 0.0000 5837 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5562 . 0.2242 0.2436 . 292 0.0000 5854 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5565 . 0.2075 0.2246 . 315 0.0000 5880 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5542 . 0.1948 0.2152 . 251 0.0000 5793 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5542 . 0.1716 0.2169 . 278 0.0000 5820 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5593 . 0.1646 0.1932 . 292 0.0000 5885 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5579 . 0.1551 0.1599 . 252 0.0000 5831 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5564 . 0.1437 0.1795 . 273 0.0000 5837 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5586 . 0.1342 0.1605 . 293 0.0000 5879 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5485 . 0.1276 0.1502 . 308 0.0000 5793 . 'X-RAY DIFFRACTION' 
1.2100 1.2400  30 100.0000 5662 . 0.1215 0.1462 . 237 0.0000 5899 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 5545 . 0.1239 0.1369 . 291 0.0000 5836 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5562 . 0.1228 0.1359 . 274 0.0000 5836 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5530 . 0.1266 0.1427 . 309 0.0000 5839 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5612 . 0.1260 0.1493 . 292 0.0000 5904 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5610 . 0.1280 0.1469 . 245 0.0000 5855 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5565 . 0.1275 0.1505 . 301 0.0000 5866 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5578 . 0.1194 0.1277 . 263 0.0000 5841 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5575 . 0.1200 0.1340 . 311 0.0000 5886 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5617 . 0.1228 0.1357 . 271 0.0000 5888 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5604 . 0.1330 0.1478 . 266 0.0000 5870 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5593 . 0.1362 0.1407 . 302 0.0000 5895 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5615 . 0.1390 0.1382 . 286 0.0000 5901 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5608 . 0.1390 0.1403 . 306 0.0000 5914 . 'X-RAY DIFFRACTION' 
2.4200 3.0500  30 100.0000 5674 . 0.1492 0.1691 . 290 0.0000 5964 . 'X-RAY DIFFRACTION' 
3.0500 44.4200 30 100.0000 5800 . 0.1510 0.1643 . 282 0.0000 6082 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HD1 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003704' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HD1 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HD1 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HD1 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 7HD1 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HD1 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HD1 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HD1 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O VAL A 151 ? O VAL A 151 
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                   7HD1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    223 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    321 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.15 -131.06 
2 1 HIS A 86  ? ? 55.10 -132.37 
3 1 SER A 128 ? B 71.54 -2.59   
4 1 HIS B 86  ? ? 57.26 -127.45 
# 
_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 522 ? 5.91 . 
2 1 O ? A HOH 523 ? 5.92 . 
3 1 O B A HOH 524 ? 6.17 . 
4 1 O ? A HOH 525 ? 7.61 . 
5 1 O ? B HOH 402 ? 6.61 . 
# 
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 
A1A6Z N2   N Y N 1   
A1A6Z C3   C N N 2   
A1A6Z C6   C N N 3   
A1A6Z C9   C Y N 4   
A1A6Z C12  C Y N 5   
A1A6Z C1   C N N 6   
A1A6Z C10  C Y N 7   
A1A6Z C11  C Y N 8   
A1A6Z C13  C N N 9   
A1A6Z C2   C N N 10  
A1A6Z C4   C N N 11  
A1A6Z C5   C N S 12  
A1A6Z C7   C Y N 13  
A1A6Z C8   C Y N 14  
A1A6Z N1   N N N 15  
A1A6Z N3   N Y N 16  
A1A6Z N4   N Y N 17  
A1A6Z O1   O N N 18  
A1A6Z H6   H N N 19  
A1A6Z H7   H N N 20  
A1A6Z H5   H N N 21  
A1A6Z H11  H N N 22  
A1A6Z H10  H N N 23  
A1A6Z H15  H N N 24  
A1A6Z H2   H N N 25  
A1A6Z H4   H N N 26  
A1A6Z H3   H N N 27  
A1A6Z H14  H N N 28  
A1A6Z H18  H N N 29  
A1A6Z H17  H N N 30  
A1A6Z H9   H N N 31  
A1A6Z H8   H N N 32  
A1A6Z H1   H N N 33  
A1A6Z H13  H N N 34  
A1A6Z H16  H N N 35  
A1A6Z H12  H N N 36  
ALA   N    N N N 37  
ALA   CA   C N S 38  
ALA   C    C N N 39  
ALA   O    O N N 40  
ALA   CB   C N N 41  
ALA   OXT  O N N 42  
ALA   H    H N N 43  
ALA   H2   H N N 44  
ALA   HA   H N N 45  
ALA   HB1  H N N 46  
ALA   HB2  H N N 47  
ALA   HB3  H N N 48  
ALA   HXT  H N N 49  
ARG   N    N N N 50  
ARG   CA   C N S 51  
ARG   C    C N N 52  
ARG   O    O N N 53  
ARG   CB   C N N 54  
ARG   CG   C N N 55  
ARG   CD   C N N 56  
ARG   NE   N N N 57  
ARG   CZ   C N N 58  
ARG   NH1  N N N 59  
ARG   NH2  N N N 60  
ARG   OXT  O N N 61  
ARG   H    H N N 62  
ARG   H2   H N N 63  
ARG   HA   H N N 64  
ARG   HB2  H N N 65  
ARG   HB3  H N N 66  
ARG   HG2  H N N 67  
ARG   HG3  H N N 68  
ARG   HD2  H N N 69  
ARG   HD3  H N N 70  
ARG   HE   H N N 71  
ARG   HH11 H N N 72  
ARG   HH12 H N N 73  
ARG   HH21 H N N 74  
ARG   HH22 H N N 75  
ARG   HXT  H N N 76  
ASN   N    N N N 77  
ASN   CA   C N S 78  
ASN   C    C N N 79  
ASN   O    O N N 80  
ASN   CB   C N N 81  
ASN   CG   C N N 82  
ASN   OD1  O N N 83  
ASN   ND2  N N N 84  
ASN   OXT  O N N 85  
ASN   H    H N N 86  
ASN   H2   H N N 87  
ASN   HA   H N N 88  
ASN   HB2  H N N 89  
ASN   HB3  H N N 90  
ASN   HD21 H N N 91  
ASN   HD22 H N N 92  
ASN   HXT  H N N 93  
ASP   N    N N N 94  
ASP   CA   C N S 95  
ASP   C    C N N 96  
ASP   O    O N N 97  
ASP   CB   C N N 98  
ASP   CG   C N N 99  
ASP   OD1  O N N 100 
ASP   OD2  O N N 101 
ASP   OXT  O N N 102 
ASP   H    H N N 103 
ASP   H2   H N N 104 
ASP   HA   H N N 105 
ASP   HB2  H N N 106 
ASP   HB3  H N N 107 
ASP   HD2  H N N 108 
ASP   HXT  H N N 109 
CYS   N    N N N 110 
CYS   CA   C N R 111 
CYS   C    C N N 112 
CYS   O    O N N 113 
CYS   CB   C N N 114 
CYS   SG   S N N 115 
CYS   OXT  O N N 116 
CYS   H    H N N 117 
CYS   H2   H N N 118 
CYS   HA   H N N 119 
CYS   HB2  H N N 120 
CYS   HB3  H N N 121 
CYS   HG   H N N 122 
CYS   HXT  H N N 123 
GLN   N    N N N 124 
GLN   CA   C N S 125 
GLN   C    C N N 126 
GLN   O    O N N 127 
GLN   CB   C N N 128 
GLN   CG   C N N 129 
GLN   CD   C N N 130 
GLN   OE1  O N N 131 
GLN   NE2  N N N 132 
GLN   OXT  O N N 133 
GLN   H    H N N 134 
GLN   H2   H N N 135 
GLN   HA   H N N 136 
GLN   HB2  H N N 137 
GLN   HB3  H N N 138 
GLN   HG2  H N N 139 
GLN   HG3  H N N 140 
GLN   HE21 H N N 141 
GLN   HE22 H N N 142 
GLN   HXT  H N N 143 
GLU   N    N N N 144 
GLU   CA   C N S 145 
GLU   C    C N N 146 
GLU   O    O N N 147 
GLU   CB   C N N 148 
GLU   CG   C N N 149 
GLU   CD   C N N 150 
GLU   OE1  O N N 151 
GLU   OE2  O N N 152 
GLU   OXT  O N N 153 
GLU   H    H N N 154 
GLU   H2   H N N 155 
GLU   HA   H N N 156 
GLU   HB2  H N N 157 
GLU   HB3  H N N 158 
GLU   HG2  H N N 159 
GLU   HG3  H N N 160 
GLU   HE2  H N N 161 
GLU   HXT  H N N 162 
GLY   N    N N N 163 
GLY   CA   C N N 164 
GLY   C    C N N 165 
GLY   O    O N N 166 
GLY   OXT  O N N 167 
GLY   H    H N N 168 
GLY   H2   H N N 169 
GLY   HA2  H N N 170 
GLY   HA3  H N N 171 
GLY   HXT  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
THR   N    N N N 340 
THR   CA   C N S 341 
THR   C    C N N 342 
THR   O    O N N 343 
THR   CB   C N R 344 
THR   OG1  O N N 345 
THR   CG2  C N N 346 
THR   OXT  O N N 347 
THR   H    H N N 348 
THR   H2   H N N 349 
THR   HA   H N N 350 
THR   HB   H N N 351 
THR   HG1  H N N 352 
THR   HG21 H N N 353 
THR   HG22 H N N 354 
THR   HG23 H N N 355 
THR   HXT  H N N 356 
TYR   N    N N N 357 
TYR   CA   C N S 358 
TYR   C    C N N 359 
TYR   O    O N N 360 
TYR   CB   C N N 361 
TYR   CG   C Y N 362 
TYR   CD1  C Y N 363 
TYR   CD2  C Y N 364 
TYR   CE1  C Y N 365 
TYR   CE2  C Y N 366 
TYR   CZ   C Y N 367 
TYR   OH   O N N 368 
TYR   OXT  O N N 369 
TYR   H    H N N 370 
TYR   H2   H N N 371 
TYR   HA   H N N 372 
TYR   HB2  H N N 373 
TYR   HB3  H N N 374 
TYR   HD1  H N N 375 
TYR   HD2  H N N 376 
TYR   HE1  H N N 377 
TYR   HE2  H N N 378 
TYR   HH   H N N 379 
TYR   HXT  H N N 380 
VAL   N    N N N 381 
VAL   CA   C N S 382 
VAL   C    C N N 383 
VAL   O    O N N 384 
VAL   CB   C N N 385 
VAL   CG1  C N N 386 
VAL   CG2  C N N 387 
VAL   OXT  O N N 388 
VAL   H    H N N 389 
VAL   H2   H N N 390 
VAL   HA   H N N 391 
VAL   HB   H N N 392 
VAL   HG11 H N N 393 
VAL   HG12 H N N 394 
VAL   HG13 H N N 395 
VAL   HG21 H N N 396 
VAL   HG22 H N N 397 
VAL   HG23 H N N 398 
VAL   HXT  H N N 399 
# 
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 
A1A6Z C1  C2   sing N N 1   
A1A6Z C4  C2   sing N N 2   
A1A6Z C4  C5   sing N N 3   
A1A6Z C2  C3   sing N N 4   
A1A6Z C2  C13  sing N N 5   
A1A6Z O1  C6   sing N N 6   
A1A6Z C6  C5   sing N N 7   
A1A6Z C13 N1   sing N N 8   
A1A6Z C5  N1   sing N N 9   
A1A6Z N1  C7   sing N N 10  
A1A6Z C7  N2   doub Y N 11  
A1A6Z C7  C10  sing Y N 12  
A1A6Z C11 C10  sing Y N 13  
A1A6Z C11 C12  doub Y N 14  
A1A6Z N2  C8   sing Y N 15  
A1A6Z C10 C9   doub Y N 16  
A1A6Z C12 N4   sing Y N 17  
A1A6Z C8  N3   doub Y N 18  
A1A6Z C9  N4   sing Y N 19  
A1A6Z C9  N3   sing Y N 20  
A1A6Z C3  H6   sing N N 21  
A1A6Z C3  H7   sing N N 22  
A1A6Z C3  H5   sing N N 23  
A1A6Z C6  H11  sing N N 24  
A1A6Z C6  H10  sing N N 25  
A1A6Z C12 H15  sing N N 26  
A1A6Z C1  H2   sing N N 27  
A1A6Z C1  H4   sing N N 28  
A1A6Z C1  H3   sing N N 29  
A1A6Z C11 H14  sing N N 30  
A1A6Z C13 H18  sing N N 31  
A1A6Z C13 H17  sing N N 32  
A1A6Z C4  H9   sing N N 33  
A1A6Z C4  H8   sing N N 34  
A1A6Z C5  H1   sing N N 35  
A1A6Z C8  H13  sing N N 36  
A1A6Z N4  H16  sing N N 37  
A1A6Z O1  H12  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TYR   N   CA   sing N N 344 
TYR   N   H    sing N N 345 
TYR   N   H2   sing N N 346 
TYR   CA  C    sing N N 347 
TYR   CA  CB   sing N N 348 
TYR   CA  HA   sing N N 349 
TYR   C   O    doub N N 350 
TYR   C   OXT  sing N N 351 
TYR   CB  CG   sing N N 352 
TYR   CB  HB2  sing N N 353 
TYR   CB  HB3  sing N N 354 
TYR   CG  CD1  doub Y N 355 
TYR   CG  CD2  sing Y N 356 
TYR   CD1 CE1  sing Y N 357 
TYR   CD1 HD1  sing N N 358 
TYR   CD2 CE2  doub Y N 359 
TYR   CD2 HD2  sing N N 360 
TYR   CE1 CZ   doub Y N 361 
TYR   CE1 HE1  sing N N 362 
TYR   CE2 CZ   sing Y N 363 
TYR   CE2 HE2  sing N N 364 
TYR   CZ  OH   sing N N 365 
TYR   OH  HH   sing N N 366 
TYR   OXT HXT  sing N N 367 
VAL   N   CA   sing N N 368 
VAL   N   H    sing N N 369 
VAL   N   H2   sing N N 370 
VAL   CA  C    sing N N 371 
VAL   CA  CB   sing N N 372 
VAL   CA  HA   sing N N 373 
VAL   C   O    doub N N 374 
VAL   C   OXT  sing N N 375 
VAL   CB  CG1  sing N N 376 
VAL   CB  CG2  sing N N 377 
VAL   CB  HB   sing N N 378 
VAL   CG1 HG11 sing N N 379 
VAL   CG1 HG12 sing N N 380 
VAL   CG1 HG13 sing N N 381 
VAL   CG2 HG21 sing N N 382 
VAL   CG2 HG22 sing N N 383 
VAL   CG2 HG23 sing N N 384 
VAL   OXT HXT  sing N N 385 
# 
_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                    7HD1 
_atom_sites.fract_transf_matrix[1][1]   0.011257 
_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]   0.011257 
_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]   0.025379 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.720 -16.245 22.232  0.34 55.62 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.803 -15.563 22.390  0.66 57.80 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.744 -15.174 22.384  0.34 55.21 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.776 -14.549 22.590  0.66 57.18 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.394 -13.824 22.100  0.34 53.32 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.345 -13.163 22.299  0.66 54.83 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.498 -13.547 22.571  0.34 53.82 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.403 -12.799 22.813  0.66 55.39 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.097 -15.200 23.785  0.34 56.31 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.182 -14.627 24.010  0.66 58.42 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.067 -14.087 23.920  0.34 56.65 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.099 -13.575 24.190  0.66 58.83 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.459 -16.556 24.053  0.34 56.64 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.629 -16.020 24.281  0.66 58.83 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.038 -15.300 21.735  0.34 66.41 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 18.053 -14.708 21.966  0.66 68.77 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.783 -15.056 24.454  0.34 67.72 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.881 -14.453 24.659  0.66 70.26 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.554 -14.230 24.731  0.34 68.13 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.623 -13.750 25.016  0.66 70.74 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.526 -13.234 23.967  0.34 68.13 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.512 -12.698 24.226  0.66 70.74 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.478 -14.106 23.149  0.34 68.13 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.486 -13.623 23.439  0.66 70.74 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.002 -16.526 24.908  0.34 68.12 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.197 -16.025 25.150  0.66 70.75 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.825 -16.752 23.345  0.34 68.12 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.986 -16.245 23.591  0.66 70.75 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.153 -17.234 24.073  0.34 68.12 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.359 -16.659 24.273  0.66 70.75 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.707 -12.989 21.322  0.34 50.56 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.639 -12.396 21.471  0.66 51.37 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.155 -11.634 21.029  0.34 47.49 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.048 -11.047 21.099  0.66 47.54 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 18.006 -10.661 21.274  0.34 44.65 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.907 -10.076 21.387  0.66 44.31 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.892 -11.056 21.632  0.34 44.84 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.838 -10.463 21.869  0.66 44.44 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.723 -11.516 19.607  0.34 47.00 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.508 -10.981 19.636  0.66 46.72 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.732 -11.939 18.541  0.34 46.48 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.460 -11.487 18.670  0.66 45.85 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.580 -11.506 18.537  0.34 46.33 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.316 -11.031 18.680  0.66 45.58 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.180 -12.794 17.627  0.34 46.35 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.844 -12.443 17.831  0.66 45.56 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.961 -13.194 20.946  0.34 60.82 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.899 -12.645 21.108  0.66 61.79 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.867 -11.407 21.642  0.34 57.14 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.800 -10.792 21.647  0.66 57.20 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.969 -10.591 19.441  0.34 56.56 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.709 -10.058 19.408  0.66 56.21 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.505 -12.084 19.531  0.34 56.56 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.303 -11.527 19.528  0.66 56.21 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.661 -13.064 16.997  0.34 55.77 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.287 -12.764 17.260  0.66 54.83 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.992 -13.077 17.665  0.34 55.77 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.652 -12.740 17.857  0.66 54.83 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.284 -9.373  21.077  0.34 41.37 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.139 -8.798  21.086  0.66 40.73 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.361 -8.305  21.436  0.34 37.96 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.216 -7.730  21.450  0.66 37.04 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.502 -7.832  20.267  0.34 34.19 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.328 -7.279  20.294  0.66 32.44 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.812 -6.816  20.395  0.34 34.21 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.608 -6.284  20.433  0.66 32.01 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.125 -7.124  22.040  0.34 38.32 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.980 -6.537  22.031  0.66 38.00 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.151 -6.680  21.170  0.34 38.48 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.768 -5.901  21.043  0.66 38.57 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 19.016 -9.092  20.725  0.34 49.80 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.836 -8.526  20.660  0.66 49.02 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.763 -8.639  22.122  0.34 45.70 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.632 -8.059  22.146  0.66 44.60 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.504 -6.394  22.195  0.34 46.14 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.343 -5.898  22.387  0.66 45.75 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.521 -7.403  22.881  0.34 46.14 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.562 -6.852  22.743  0.66 45.75 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.560 -6.032  21.517  0.34 46.32 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.328 -6.442  20.729  0.66 46.43 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.529 -8.532  19.135  0.34 30.29 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.358 -7.978  19.162  0.66 28.12 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.634 -8.195  18.035  0.34 26.38 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.420 -7.683  18.087  0.66 24.10 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.206 -8.587  18.394  0.34 25.24 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.004 -8.028  18.536  0.66 23.99 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.947 -9.724  18.801  0.34 25.49 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.775 -9.054  19.182  0.66 24.98 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.070 -8.912  16.758  0.34 23.82 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.783 -8.484  16.836  0.66 21.23 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.336 -8.366  16.155  0.34 21.67 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.082 -8.062  16.195  0.66 19.13 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.324 -7.182  15.436  0.34 20.64 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.164 -6.881  15.475  0.66 18.33 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.535 -9.044  16.298  0.34 21.01 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.216 -8.854  16.299  0.66 19.28 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.488 -6.680  14.878  0.34 20.23 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.353 -6.492  14.882  0.66 18.00 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.701 -8.548  15.741  0.34 20.70 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.406 -8.470  15.706  0.66 19.30 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.676 -7.365  15.030  0.34 20.36 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.472 -7.290  14.997  0.66 18.64 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.057 -9.193  18.979  0.34 36.49 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.905 -8.622  18.994  0.66 33.90 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.663 -7.239  17.877  0.34 31.80 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.456 -6.737  17.875  0.66 29.07 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.219 -9.849  16.961  0.34 28.73 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.863 -9.419  17.075  0.66 25.63 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.367 -8.826  16.097  0.34 28.73 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.080 -8.370  16.179  0.66 25.63 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.528 -6.715  15.330  0.34 24.92 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.413 -6.335  15.393  0.66 22.14 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.558 -9.842  16.776  0.34 25.37 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.174 -9.650  16.778  0.66 23.29 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.471 -5.882  14.398  0.34 24.43 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.399 -5.691  14.402  0.66 21.75 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.501 -9.011  15.845  0.34 24.99 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.158 -9.007  15.787  0.66 23.31 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.459 -7.029  14.655  0.34 24.58 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.271 -7.027  14.600  0.66 22.52 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.276 -7.646  18.233  0.34 23.92 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.049 -7.165  18.191  0.66 23.45 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.900 -7.815  18.681  0.34 22.89 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.691 -7.259  18.709  0.66 23.77 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.928 -7.530  17.543  0.34 21.20 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.678 -7.232  17.574  0.66 21.71 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.156 -6.633  16.727  0.34 21.46 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.776 -6.414  16.656  0.66 21.58 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.600 -6.869  19.855  0.34 23.37 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.400 -6.099  19.669  0.66 25.88 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.217 -6.870  20.169  0.34 24.12 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.537 -6.508  20.711  0.66 28.12 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.429 -6.887  17.859  0.34 28.86 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.172 -6.506  17.649  0.66 28.29 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.767 -8.726  18.984  0.34 27.62 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.588 -8.088  19.194  0.66 28.67 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.099 -7.162  20.636  0.34 28.20 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.238 -5.780  20.043  0.66 31.21 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.877 -5.968  19.613  0.34 28.20 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 10.965 -5.386  19.177  0.66 31.21 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.071 -6.338  20.804  0.34 29.09 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.402 -5.874  21.240  0.66 33.89 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.844  -8.306  17.497  0.34 19.72 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.693  -8.122  17.653  0.66 20.70 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.741  -8.034  16.595  0.34 18.23 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.574  -8.070  16.737  0.66 19.78 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.904  -8.524  15.174  0.34 17.11 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.838  -8.585  15.346  0.66 18.65 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.165  -8.074  14.292  0.34 17.40 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.036  -8.321  14.444  0.66 18.76 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.726  -8.995  17.991  0.34 23.81 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.660  -8.758  18.229  0.66 25.00 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.937  -8.438  16.969  0.34 22.03 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.846  -8.594  17.101  0.66 23.88 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.597  -7.078  16.556  0.34 22.03 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.274  -7.152  16.656  0.66 23.88 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.840  -9.434  14.917  0.34 15.63 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.923  -9.324  15.133  0.66 17.40 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.076 -9.936  13.572  0.34 14.31 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.201 -9.848  13.805  0.66 16.06 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.204  -11.153 13.284  0.34 14.09 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.362  -11.089 13.526  0.66 15.56 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.815  -11.900 14.187  0.34 14.88 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.094  -11.900 14.419  0.66 16.80 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.546 -10.326 13.388  0.34 13.81 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.687 -10.172 13.641  0.66 15.81 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.491 -9.148  13.268  0.34 13.81 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.526 -8.945  13.354  0.66 15.68 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.823 -8.386  14.379  0.34 14.18 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.804 -8.030  14.357  0.66 16.34 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.049 -8.798  12.043  0.34 13.80 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.008 -8.688  12.076  0.66 15.08 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.679 -7.307  14.277  0.34 14.32 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.550 -6.900  14.104  0.66 16.14 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.906 -7.719  11.931  0.34 14.13 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.758 -7.558  11.811  0.66 15.23 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.214 -6.979  13.052  0.34 14.51 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.017 -6.666  12.828  0.66 15.23 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 15.067 -5.908  12.948  0.34 15.03 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.757 -5.541  12.566  0.66 15.38 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.354 -9.779  15.511  0.34 18.90 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.505 -9.539  15.737  0.66 21.03 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.859  -9.250  12.924  0.34 17.33 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.969  -9.175  13.153  0.66 19.43 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.831 -10.860 14.146  0.34 16.72 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 12.018 -10.582 14.454  0.66 19.13 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.619 -10.844 12.573  0.34 16.72 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.787 -10.784 12.895  0.66 19.13 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.456 -8.602  15.205  0.34 17.16 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.478 -8.187  15.217  0.66 19.76 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.841 -9.297  11.285  0.34 16.71 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.827 -9.287  11.388  0.66 18.25 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.889 -6.802  15.029  0.34 17.33 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.730 -6.299  14.787  0.66 19.52 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.277 -7.495  11.105  0.34 17.11 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.081 -7.398  10.952  0.66 18.43 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.173 -5.546  13.699  0.34 18.18 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.858 -5.094  13.266  0.66 18.61 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.902  -11.343 12.003  0.34 13.85 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.951  -11.222 12.271  0.66 15.10 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.302  -12.573 11.512  0.34 13.58 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.328  -12.434 11.760  0.66 15.32 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.421  -13.520 11.106  0.34 12.50 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.425  -13.389 11.306  0.66 14.73 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.448 -13.089 10.579  0.34 11.96 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.291 -13.012 10.512  0.66 14.40 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.432  -12.269 10.294  0.34 14.67 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.451  -12.072 10.562  0.66 15.99 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.703  -13.464 9.684   0.34 15.95 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.840  -13.221 9.758   0.66 17.25 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.606  -13.937 10.622  0.34 16.30 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.805  -13.964 10.579  0.66 17.84 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.143  -13.115 8.318   0.34 16.76 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.229  -12.701 8.461   0.66 18.13 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 9.042  -10.761 11.383  0.34 16.77 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 9.026  -10.595 11.680  0.66 18.27 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.760  -12.987 12.201  0.34 16.44 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.782  -12.848 12.450  0.66 18.53 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.759  -11.621 10.553  0.34 17.75 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.717  -11.522 10.877  0.66 19.34 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.996  -11.889 9.602   0.34 17.75 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.993  -11.551 9.946   0.66 19.34 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.331  -14.194 9.566   0.34 19.29 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.540  -13.848 9.521   0.66 20.86 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.149  -14.690 10.218  0.34 19.72 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.525  -14.756 10.093  0.66 21.56 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 6.005  -14.205 11.465  0.34 19.72 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.196  -14.218 11.429  0.66 21.56 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.982  -13.210 10.769  0.34 19.72 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.044  -13.382 10.729  0.66 21.56 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.687  -13.890 7.958   0.34 20.26 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.881  -13.456 7.958   0.66 21.90 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.523  -12.376 8.413   0.34 20.26 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.512  -12.087 8.675   0.66 21.90 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.876  -12.861 7.734   0.34 20.26 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.915  -12.250 7.947   0.66 21.90 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.221  -14.811 11.348  0.34 12.46 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.386  -14.619 11.804  0.66 14.92 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.237 -15.817 11.071  0.34 12.99 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.336 -15.634 11.373  0.66 14.54 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.929  -16.425 9.710   0.34 13.48 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.933  -16.152 9.995   0.66 13.98 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.917  -17.113 9.548   0.34 13.93 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.781  -16.557 9.789   0.66 14.93 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.239 -16.871 12.176  0.34 13.01 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.357 -16.770 12.396  0.66 14.64 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.350 -17.904 12.092  0.34 13.02 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.350 -17.888 12.120  0.66 15.08 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.408 -18.744 13.367  0.34 13.34 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.432 -18.812 13.336  0.66 15.67 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.443 -19.859 13.271  0.34 13.44 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.461 -19.930 13.182  0.66 15.59 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.813 -19.327 13.043  0.34 13.58 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.836 -19.404 12.981  0.66 15.63 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.486  -15.138 11.670  0.34 15.10 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.815  -14.878 12.398  0.66 18.06 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.107 -15.398 11.032  0.34 15.73 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.220 -15.236 11.317  0.66 17.59 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.328 -16.415 13.028  0.34 15.76 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.570 -16.392 13.267  0.66 17.72 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.395  -17.347 12.150  0.34 15.76 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.469  -17.162 12.428  0.66 17.72 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.184 -18.495 11.343  0.34 15.78 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 11.054 -18.403 11.353  0.66 18.24 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.202 -17.452 11.985  0.34 15.78 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.229 -17.508 11.957  0.66 18.24 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.644 -18.172 14.116  0.34 16.16 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.671 -18.283 14.113  0.66 18.95 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.539 -19.149 13.522  0.34 16.16 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.562 -19.222 13.471  0.66 18.95 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.449 -20.360 14.100  0.34 16.28 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.464 -20.469 13.986  0.66 18.86 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.217 -20.438 12.528  0.34 16.28 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.232 -20.469 12.413  0.66 18.86 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.383 -19.996 12.917  0.34 16.45 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.412 -20.076 12.908  0.66 18.91 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.820 -18.802 12.321  0.34 16.45 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.868 -18.914 12.235  0.66 18.91 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.077 -18.849 13.746  0.34 16.45 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 14.072 -18.891 13.669  0.66 18.91 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.788 -16.164 8.725   0.34 13.34 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.879 -16.155 9.053   0.66 14.19 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.604 -16.784 7.420   0.34 13.44 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.624 -16.681 7.713   0.66 14.99 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.230 -18.164 7.356   0.34 13.59 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.182 -18.085 7.494   0.66 14.55 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.648 -19.080 6.764   0.34 13.67 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.512 -18.925 6.887   0.66 14.91 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.197 -15.914 6.314   0.34 13.24 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.180 -15.747 6.635   0.66 16.21 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.512 -14.565 6.127   0.34 14.26 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.506 -14.393 6.421   0.66 17.74 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.274 -13.720 5.121   0.34 14.98 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.099 -13.706 5.191   0.66 19.02 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.066  -14.758 5.697   0.34 14.57 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.995  -14.544 6.296   0.66 18.10 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.474 -15.647 8.785   0.34 16.16 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.679 -15.857 9.177   0.66 17.17 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.655  -16.888 7.253   0.34 16.28 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.668  -16.738 7.593   0.66 18.14 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.130 -15.750 6.523   0.34 16.04 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.108 -15.564 6.853   0.66 19.60 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.134 -16.402 5.477   0.34 16.04 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.140 -16.219 5.793   0.66 19.60 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.512 -14.098 6.974   0.34 17.27 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.687 -13.831 7.187   0.66 21.44 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.817 -12.871 5.017   0.34 18.12 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.652 -12.856 5.053   0.66 22.97 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.175 -13.573 5.451   0.34 18.12 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.050 -13.555 5.337   0.66 22.97 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.304 -14.187 4.272   0.34 18.12 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.975 -14.274 4.414   0.66 22.97 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.680  -13.894 5.502   0.34 17.64 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.620  -13.705 5.987   0.66 21.87 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 9.048  -15.314 4.905   0.34 17.64 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.799  -15.250 5.661   0.66 21.87 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.571  -15.189 6.413   0.34 17.64 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.630  -14.770 7.166   0.66 21.87 ?  12  LEU   A HD23 1 
ATOM   319  N N    . THR   A 1 13  ? 12.413 -18.331 7.941   1.00 13.84 ?  13  THR   A N    1 
ATOM   320  C CA   . THR   A 1 13  ? 13.101 -19.610 7.862   1.00 14.01 ?  13  THR   A CA   1 
ATOM   321  C C    . THR   A 1 13  ? 13.867 -19.819 9.161   1.00 13.91 ?  13  THR   A C    1 
ATOM   322  O O    . THR   A 1 13  ? 13.763 -19.033 10.108  1.00 14.02 ?  13  THR   A O    1 
ATOM   323  C CB   . THR   A 1 13  ? 14.091 -19.660 6.690   1.00 14.81 ?  13  THR   A CB   1 
ATOM   324  O OG1  . THR   A 1 13  ? 15.136 -18.717 6.931   1.00 14.92 ?  13  THR   A OG1  1 
ATOM   325  C CG2  . THR   A 1 13  ? 13.434 -19.366 5.349   1.00 15.61 ?  13  THR   A CG2  1 
ATOM   326  H H    A THR   A 1 13  ? 12.842 -17.721 8.370   0.34 16.76 ?  13  THR   A H    1 
ATOM   327  H H    B THR   A 1 13  ? 12.901 -17.728 8.312   0.66 16.76 ?  13  THR   A H    1 
ATOM   328  H HA   . THR   A 1 13  ? 12.460 -20.329 7.756   1.00 16.96 ?  13  THR   A HA   1 
ATOM   329  H HB   . THR   A 1 13  ? 14.481 -20.548 6.635   1.00 17.92 ?  13  THR   A HB   1 
ATOM   330  H HG1  . THR   A 1 13  ? 15.836 -19.117 7.179   1.00 18.06 ?  13  THR   A HG1  1 
ATOM   331  H HG21 . THR   A 1 13  ? 14.086 -19.480 4.631   1.00 18.88 ?  13  THR   A HG21 1 
ATOM   332  H HG22 . THR   A 1 13  ? 12.701 -19.980 5.200   1.00 18.88 ?  13  THR   A HG22 1 
ATOM   333  H HG23 . THR   A 1 13  ? 13.105 -18.459 5.330   1.00 18.88 ?  13  THR   A HG23 1 
ATOM   334  N N    A ASP   A 1 14  ? 14.703 -20.857 9.182   0.34 13.77 ?  14  ASP   A N    1 
ATOM   335  N N    B ASP   A 1 14  ? 14.660 -20.890 9.190   0.66 14.69 ?  14  ASP   A N    1 
ATOM   336  C CA   A ASP   A 1 14  ? 15.508 -21.132 10.365  0.34 13.51 ?  14  ASP   A CA   1 
ATOM   337  C CA   B ASP   A 1 14  ? 15.508 -21.155 10.341  0.66 15.64 ?  14  ASP   A CA   1 
ATOM   338  C C    A ASP   A 1 14  ? 16.372 -19.940 10.773  0.34 12.66 ?  14  ASP   A C    1 
ATOM   339  C C    B ASP   A 1 14  ? 16.317 -19.921 10.733  0.66 14.70 ?  14  ASP   A C    1 
ATOM   340  O O    A ASP   A 1 14  ? 16.684 -19.786 11.959  0.34 13.01 ?  14  ASP   A O    1 
ATOM   341  O O    B ASP   A 1 14  ? 16.483 -19.631 11.923  0.66 15.92 ?  14  ASP   A O    1 
ATOM   342  C CB   A ASP   A 1 14  ? 16.398 -22.343 10.115  0.34 15.10 ?  14  ASP   A CB   1 
ATOM   343  C CB   B ASP   A 1 14  ? 16.440 -22.321 10.017  0.66 19.05 ?  14  ASP   A CB   1 
ATOM   344  C CG   A ASP   A 1 14  ? 17.314 -22.621 11.271  0.34 17.37 ?  14  ASP   A CG   1 
ATOM   345  C CG   B ASP   A 1 14  ? 17.330 -22.684 11.181  0.66 23.09 ?  14  ASP   A CG   1 
ATOM   346  O OD1  A ASP   A 1 14  ? 16.835 -23.203 12.271  0.34 18.33 ?  14  ASP   A OD1  1 
ATOM   347  O OD1  B ASP   A 1 14  ? 16.801 -22.784 12.308  0.66 24.83 ?  14  ASP   A OD1  1 
ATOM   348  O OD2  A ASP   A 1 14  ? 18.500 -22.249 11.182  0.34 18.77 -1 14  ASP   A OD2  1 
ATOM   349  O OD2  B ASP   A 1 14  ? 18.545 -22.879 10.974  0.66 24.55 -1 14  ASP   A OD2  1 
ATOM   350  H H    A ASP   A 1 14  ? 14.824 -21.403 8.533   0.34 16.67 ?  14  ASP   A H    1 
ATOM   351  H H    B ASP   A 1 14  ? 14.738 -21.458 8.552   0.66 17.78 ?  14  ASP   A H    1 
ATOM   352  H HA   A ASP   A 1 14  ? 14.923 -21.342 11.105  0.34 16.37 ?  14  ASP   A HA   1 
ATOM   353  H HA   B ASP   A 1 14  ? 14.954 -21.412 11.096  0.66 18.92 ?  14  ASP   A HA   1 
ATOM   354  H HB2  A ASP   A 1 14  ? 15.840 -23.131 9.997   0.34 18.27 ?  14  ASP   A HB2  1 
ATOM   355  H HB2  B ASP   A 1 14  ? 15.896 -23.103 9.780   0.66 23.02 ?  14  ASP   A HB2  1 
ATOM   356  H HB3  A ASP   A 1 14  ? 16.934 -22.196 9.321   0.34 18.27 ?  14  ASP   A HB3  1 
ATOM   357  H HB3  B ASP   A 1 14  ? 17.003 -22.085 9.266   0.66 23.02 ?  14  ASP   A HB3  1 
ATOM   358  N N    A ASN   A 1 15  ? 16.782 -19.093 9.820   0.34 12.30 ?  15  ASN   A N    1 
ATOM   359  N N    B ASN   A 1 15  ? 16.804 -19.159 9.745   0.66 13.82 ?  15  ASN   A N    1 
ATOM   360  C CA   A ASN   A 1 15  ? 17.729 -18.020 10.113  0.34 12.53 ?  15  ASN   A CA   1 
ATOM   361  C CA   B ASN   A 1 15  ? 17.795 -18.117 9.991   0.66 13.75 ?  15  ASN   A CA   1 
ATOM   362  C C    A ASN   A 1 15  ? 17.328 -16.644 9.605   0.34 12.33 ?  15  ASN   A C    1 
ATOM   363  C C    B ASN   A 1 15  ? 17.436 -16.740 9.448   0.66 13.90 ?  15  ASN   A C    1 
ATOM   364  O O    A ASN   A 1 15  ? 17.999 -15.670 9.963   0.34 12.31 ?  15  ASN   A O    1 
ATOM   365  O O    B ASN   A 1 15  ? 18.251 -15.821 9.582   0.66 14.31 ?  15  ASN   A O    1 
ATOM   366  C CB   A ASN   A 1 15  ? 19.126 -18.347 9.556   0.34 12.83 ?  15  ASN   A CB   1 
ATOM   367  C CB   B ASN   A 1 15  ? 19.158 -18.535 9.416   0.66 13.57 ?  15  ASN   A CB   1 
ATOM   368  C CG   A ASN   A 1 15  ? 19.124 -18.545 8.050   0.34 13.13 ?  15  ASN   A CG   1 
ATOM   369  C CG   B ASN   A 1 15  ? 19.157 -18.584 7.901   0.66 14.01 ?  15  ASN   A CG   1 
ATOM   370  O OD1  A ASN   A 1 15  ? 18.378 -19.373 7.522   0.34 13.60 ?  15  ASN   A OD1  1 
ATOM   371  O OD1  B ASN   A 1 15  ? 18.488 -19.425 7.292   0.66 14.83 ?  15  ASN   A OD1  1 
ATOM   372  N ND2  A ASN   A 1 15  ? 19.955 -17.772 7.348   0.34 13.36 ?  15  ASN   A ND2  1 
ATOM   373  N ND2  B ASN   A 1 15  ? 19.908 -17.679 7.281   0.66 14.46 ?  15  ASN   A ND2  1 
ATOM   374  H H    A ASN   A 1 15  ? 16.518 -19.116 9.006   0.34 14.91 ?  15  ASN   A H    1 
ATOM   375  H H    B ASN   A 1 15  ? 16.569 -19.232 8.929   0.66 16.73 ?  15  ASN   A H    1 
ATOM   376  H HA   A ASN   A 1 15  ? 17.820 -17.948 11.076  0.34 15.19 ?  15  ASN   A HA   1 
ATOM   377  H HA   B ASN   A 1 15  ? 17.908 -18.017 10.949  0.66 16.65 ?  15  ASN   A HA   1 
ATOM   378  H HB2  A ASN   A 1 15  ? 19.731 -17.610 9.764   0.34 15.55 ?  15  ASN   A HB2  1 
ATOM   379  H HB2  B ASN   A 1 15  ? 19.833 -17.890 9.701   0.66 16.44 ?  15  ASN   A HB2  1 
ATOM   380  H HB3  A ASN   A 1 15  ? 19.450 -19.160 9.971   0.34 15.55 ?  15  ASN   A HB3  1 
ATOM   381  H HB3  B ASN   A 1 15  ? 19.390 -19.417 9.752   0.66 16.44 ?  15  ASN   A HB3  1 
ATOM   382  H HD21 A ASN   A 1 15  ? 19.993 -17.843 6.490   0.34 16.19 ?  15  ASN   A HD21 1 
ATOM   383  H HD21 B ASN   A 1 15  ? 19.936 -17.665 6.424   0.66 17.50 ?  15  ASN   A HD21 1 
ATOM   384  H HD22 A ASN   A 1 15  ? 20.457 -17.197 7.749   0.34 16.19 ?  15  ASN   A HD22 1 
ATOM   385  H HD22 B ASN   A 1 15  ? 20.360 -17.104 7.737   0.66 17.50 ?  15  ASN   A HD22 1 
ATOM   386  N N    A VAL   A 1 16  ? 16.274 -16.523 8.798   0.34 12.34 ?  16  VAL   A N    1 
ATOM   387  N N    B VAL   A 1 16  ? 16.258 -16.556 8.852   0.66 14.09 ?  16  VAL   A N    1 
ATOM   388  C CA   A VAL   A 1 16  ? 15.866 -15.255 8.199   0.34 12.30 ?  16  VAL   A CA   1 
ATOM   389  C CA   B VAL   A 1 16  ? 15.860 -15.269 8.287   0.66 13.73 ?  16  VAL   A CA   1 
ATOM   390  C C    A VAL   A 1 16  ? 14.589 -14.767 8.867   0.34 12.20 ?  16  VAL   A C    1 
ATOM   391  C C    B VAL   A 1 16  ? 14.594 -14.780 8.980   0.66 13.42 ?  16  VAL   A C    1 
ATOM   392  O O    A VAL   A 1 16  ? 13.592 -15.497 8.940   0.34 12.44 ?  16  VAL   A O    1 
ATOM   393  O O    B VAL   A 1 16  ? 13.611 -15.522 9.107   0.66 14.04 ?  16  VAL   A O    1 
ATOM   394  C CB   A VAL   A 1 16  ? 15.683 -15.371 6.676   0.34 12.75 ?  16  VAL   A CB   1 
ATOM   395  C CB   B VAL   A 1 16  ? 15.669 -15.332 6.761   0.66 14.23 ?  16  VAL   A CB   1 
ATOM   396  C CG1  A VAL   A 1 16  ? 15.257 -14.027 6.082   0.34 13.20 ?  16  VAL   A CG1  1 
ATOM   397  C CG1  B VAL   A 1 16  ? 15.225 -13.972 6.218   0.66 14.98 ?  16  VAL   A CG1  1 
ATOM   398  C CG2  A VAL   A 1 16  ? 16.966 -15.862 6.024   0.34 13.26 ?  16  VAL   A CG2  1 
ATOM   399  C CG2  B VAL   A 1 16  ? 16.948 -15.795 6.073   0.66 15.23 ?  16  VAL   A CG2  1 
ATOM   400  H H    A VAL   A 1 16  ? 15.770 -17.180 8.582   0.34 14.95 ?  16  VAL   A H    1 
ATOM   401  H H    B VAL   A 1 16  ? 15.664 -17.174 8.769   0.66 17.06 ?  16  VAL   A H    1 
ATOM   402  H HA   A VAL   A 1 16  ? 16.551 -14.592 8.364   0.34 14.91 ?  16  VAL   A HA   1 
ATOM   403  H HA   B VAL   A 1 16  ? 16.566 -14.625 8.467   0.66 16.63 ?  16  VAL   A HA   1 
ATOM   404  H HB   A VAL   A 1 16  ? 14.983 -16.015 6.488   0.34 15.45 ?  16  VAL   A HB   1 
ATOM   405  H HB   B VAL   A 1 16  ? 14.976 -15.973 6.561   0.66 17.22 ?  16  VAL   A HB   1 
ATOM   406  H HG11 A VAL   A 1 16  ? 15.333 -14.072 5.116   0.34 15.99 ?  16  VAL   A HG11 1 
ATOM   407  H HG11 B VAL   A 1 16  ? 15.300 -13.982 5.251   0.66 18.12 ?  16  VAL   A HG11 1 
ATOM   408  H HG12 A VAL   A 1 16  ? 14.338 -13.843 6.332   0.34 15.99 ?  16  VAL   A HG12 1 
ATOM   409  H HG12 B VAL   A 1 16  ? 14.305 -13.813 6.476   0.66 18.12 ?  16  VAL   A HG12 1 
ATOM   410  H HG13 A VAL   A 1 16  ? 15.840 -13.331 6.426   0.34 15.99 ?  16  VAL   A HG13 1 
ATOM   411  H HG13 B VAL   A 1 16  ? 15.799 -13.281 6.585   0.66 18.12 ?  16  VAL   A HG13 1 
ATOM   412  H HG21 A VAL   A 1 16  ? 16.849 -15.867 5.062   0.34 16.07 ?  16  VAL   A HG21 1 
ATOM   413  H HG21 B VAL   A 1 16  ? 16.815 -15.773 5.112   0.66 18.42 ?  16  VAL   A HG21 1 
ATOM   414  H HG22 A VAL   A 1 16  ? 17.691 -15.264 6.266   0.34 16.07 ?  16  VAL   A HG22 1 
ATOM   415  H HG22 B VAL   A 1 16  ? 17.676 -15.202 6.318   0.66 18.42 ?  16  VAL   A HG22 1 
ATOM   416  H HG23 A VAL   A 1 16  ? 17.157 -16.758 6.341   0.34 16.07 ?  16  VAL   A HG23 1 
ATOM   417  H HG23 B VAL   A 1 16  ? 17.151 -16.700 6.357   0.66 18.42 ?  16  VAL   A HG23 1 
ATOM   418  N N    A TYR   A 1 17  ? 14.621 -13.516 9.320   0.34 12.09 ?  17  TYR   A N    1 
ATOM   419  N N    B TYR   A 1 17  ? 14.622 -13.511 9.385   0.66 13.08 ?  17  TYR   A N    1 
ATOM   420  C CA   A TYR   A 1 17  ? 13.516 -12.830 9.970   0.34 11.93 ?  17  TYR   A CA   1 
ATOM   421  C CA   B TYR   A 1 17  ? 13.550 -12.823 10.088  0.66 12.65 ?  17  TYR   A CA   1 
ATOM   422  C C    A TYR   A 1 17  ? 13.244 -11.526 9.224   0.34 11.69 ?  17  TYR   A C    1 
ATOM   423  C C    B TYR   A 1 17  ? 13.273 -11.512 9.362   0.66 13.02 ?  17  TYR   A C    1 
ATOM   424  O O    A TYR   A 1 17  ? 14.073 -11.058 8.435   0.34 11.11 ?  17  TYR   A O    1 
ATOM   425  O O    B TYR   A 1 17  ? 14.203 -10.890 8.837   0.66 12.73 ?  17  TYR   A O    1 
ATOM   426  C CB   A TYR   A 1 17  ? 13.872 -12.532 11.431  0.34 12.77 ?  17  TYR   A CB   1 
ATOM   427  C CB   B TYR   A 1 17  ? 13.990 -12.536 11.528  0.66 13.35 ?  17  TYR   A CB   1 
ATOM   428  C CG   A TYR   A 1 17  ? 14.069 -13.777 12.270  0.34 13.63 ?  17  TYR   A CG   1 
ATOM   429  C CG   B TYR   A 1 17  ? 14.218 -13.789 12.342  0.66 14.16 ?  17  TYR   A CG   1 
ATOM   430  C CD1  A TYR   A 1 17  ? 15.254 -14.507 12.222  0.34 14.03 ?  17  TYR   A CD1  1 
ATOM   431  C CD1  B TYR   A 1 17  ? 15.411 -14.500 12.265  0.66 14.83 ?  17  TYR   A CD1  1 
ATOM   432  C CD2  A TYR   A 1 17  ? 13.058 -14.232 13.103  0.34 13.77 ?  17  TYR   A CD2  1 
ATOM   433  C CD2  B TYR   A 1 17  ? 13.222 -14.278 13.176  0.66 14.63 ?  17  TYR   A CD2  1 
ATOM   434  C CE1  A TYR   A 1 17  ? 15.420 -15.663 12.986  0.34 14.29 ?  17  TYR   A CE1  1 
ATOM   435  C CE1  B TYR   A 1 17  ? 15.604 -15.666 13.002  0.66 15.99 ?  17  TYR   A CE1  1 
ATOM   436  C CE2  A TYR   A 1 17  ? 13.215 -15.380 13.867  0.34 14.30 ?  17  TYR   A CE2  1 
ATOM   437  C CE2  B TYR   A 1 17  ? 13.407 -15.440 13.917  0.66 15.72 ?  17  TYR   A CE2  1 
ATOM   438  C CZ   A TYR   A 1 17  ? 14.395 -16.091 13.810  0.34 14.48 ?  17  TYR   A CZ   1 
ATOM   439  C CZ   B TYR   A 1 17  ? 14.601 -16.128 13.830  0.66 16.60 ?  17  TYR   A CZ   1 
ATOM   440  O OH   A TYR   A 1 17  ? 14.542 -17.232 14.573  0.34 14.89 ?  17  TYR   A OH   1 
ATOM   441  O OH   B TYR   A 1 17  ? 14.791 -17.281 14.565  0.66 18.01 ?  17  TYR   A OH   1 
ATOM   442  H H    A TYR   A 1 17  ? 15.319 -13.018 9.254   0.34 14.65 ?  17  TYR   A H    1 
ATOM   443  H H    B TYR   A 1 17  ? 15.299 -12.991 9.236   0.66 15.85 ?  17  TYR   A H    1 
ATOM   444  H HA   A TYR   A 1 17  ? 12.722 -13.392 9.940   0.34 14.46 ?  17  TYR   A HA   1 
ATOM   445  H HA   B TYR   A 1 17  ? 12.749 -13.368 10.094  0.66 15.34 ?  17  TYR   A HA   1 
ATOM   446  H HB2  A TYR   A 1 17  ? 14.694 -12.023 11.451  0.34 15.47 ?  17  TYR   A HB2  1 
ATOM   447  H HB2  B TYR   A 1 17  ? 14.819 -12.040 11.512  0.66 16.17 ?  17  TYR   A HB2  1 
ATOM   448  H HB3  A TYR   A 1 17  ? 13.154 -12.018 11.824  0.34 15.47 ?  17  TYR   A HB3  1 
ATOM   449  H HB3  B TYR   A 1 17  ? 13.299 -12.020 11.967  0.66 16.17 ?  17  TYR   A HB3  1 
ATOM   450  H HD1  A TYR   A 1 17  ? 15.943 -14.222 11.666  0.34 16.98 ?  17  TYR   A HD1  1 
ATOM   451  H HD1  B TYR   A 1 17  ? 16.087 -14.193 11.707  0.66 17.95 ?  17  TYR   A HD1  1 
ATOM   452  H HD2  A TYR   A 1 17  ? 12.254 -13.766 13.149  0.34 16.67 ?  17  TYR   A HD2  1 
ATOM   453  H HD2  B TYR   A 1 17  ? 12.412 -13.824 13.239  0.66 17.71 ?  17  TYR   A HD2  1 
ATOM   454  H HE1  A TYR   A 1 17  ? 16.221 -16.136 12.947  0.34 17.30 ?  17  TYR   A HE1  1 
ATOM   455  H HE1  B TYR   A 1 17  ? 16.410 -16.127 12.944  0.66 19.33 ?  17  TYR   A HE1  1 
ATOM   456  H HE2  A TYR   A 1 17  ? 12.528 -15.667 14.423  0.34 17.31 ?  17  TYR   A HE2  1 
ATOM   457  H HE2  B TYR   A 1 17  ? 12.728 -15.750 14.475  0.66 19.02 ?  17  TYR   A HE2  1 
ATOM   458  H HH   A TYR   A 1 17  ? 13.812 -17.420 14.932  0.34 18.02 ?  17  TYR   A HH   1 
ATOM   459  H HH   B TYR   A 1 17  ? 15.555 -17.591 14.413  0.66 21.76 ?  17  TYR   A HH   1 
ATOM   460  N N    A ILE   A 1 18  ? 12.085 -10.912 9.491   0.34 11.84 ?  18  ILE   A N    1 
ATOM   461  N N    B ILE   A 1 18  ? 12.005 -11.083 9.326   0.66 13.50 ?  18  ILE   A N    1 
ATOM   462  C CA   A ILE   A 1 18  ? 11.671 -9.718  8.755   0.34 11.79 ?  18  ILE   A CA   1 
ATOM   463  C CA   B ILE   A 1 18  ? 11.620 -9.911  8.541   0.66 13.94 ?  18  ILE   A CA   1 
ATOM   464  C C    A ILE   A 1 18  ? 10.720 -8.878  9.600   0.34 11.89 ?  18  ILE   A C    1 
ATOM   465  C C    B ILE   A 1 18  ? 10.620 -9.048  9.302   0.66 14.81 ?  18  ILE   A C    1 
ATOM   466  O O    A ILE   A 1 18  ? 9.932  -9.403  10.391  0.34 12.16 ?  18  ILE   A O    1 
ATOM   467  O O    B ILE   A 1 18  ? 9.798  -9.550  10.073  0.66 14.95 ?  18  ILE   A O    1 
ATOM   468  C CB   A ILE   A 1 18  ? 11.070 -10.096 7.379   0.34 12.33 ?  18  ILE   A CB   1 
ATOM   469  C CB   B ILE   A 1 18  ? 11.074 -10.348 7.165   0.66 14.27 ?  18  ILE   A CB   1 
ATOM   470  C CG1  A ILE   A 1 18  ? 10.944 -8.869  6.473   0.34 13.59 ?  18  ILE   A CG1  1 
ATOM   471  C CG1  B ILE   A 1 18  ? 10.994 -9.173  6.196   0.66 14.39 ?  18  ILE   A CG1  1 
ATOM   472  C CG2  A ILE   A 1 18  ? 9.733  -10.811 7.537   0.34 13.02 ?  18  ILE   A CG2  1 
ATOM   473  C CG2  B ILE   A 1 18  ? 9.727  -11.041 7.324   0.66 14.88 ?  18  ILE   A CG2  1 
ATOM   474  C CD1  A ILE   A 1 18  ? 10.626 -9.218  5.030   0.34 14.87 ?  18  ILE   A CD1  1 
ATOM   475  C CD1  B ILE   A 1 18  ? 10.809 -9.619  4.767   0.66 15.70 ?  18  ILE   A CD1  1 
ATOM   476  H H    A ILE   A 1 18  ? 11.537 -11.163 10.103  0.34 14.36 ?  18  ILE   A H    1 
ATOM   477  H H    B ILE   A 1 18  ? 11.351 -11.473 9.736   0.66 16.36 ?  18  ILE   A H    1 
ATOM   478  H HA   A ILE   A 1 18  ? 12.458 -9.180  8.590   0.34 14.30 ?  18  ILE   A HA   1 
ATOM   479  H HA   B ILE   A 1 18  ? 12.416 -9.382  8.381   0.66 16.88 ?  18  ILE   A HA   1 
ATOM   480  H HB   A ILE   A 1 18  ? 11.684 -10.707 6.959   0.34 14.95 ?  18  ILE   A HB   1 
ATOM   481  H HB   B ILE   A 1 18  ? 11.691 -10.996 6.790   0.66 17.28 ?  18  ILE   A HB   1 
ATOM   482  H HG12 A ILE   A 1 18  ? 10.231 -8.301  6.802   0.34 16.46 ?  18  ILE   A HG12 1 
ATOM   483  H HG12 B ILE   A 1 18  ? 10.237 -8.614  6.433   0.66 17.42 ?  18  ILE   A HG12 1 
ATOM   484  H HG13 A ILE   A 1 18  ? 11.784 -8.383  6.480   0.34 16.46 ?  18  ILE   A HG13 1 
ATOM   485  H HG13 B ILE   A 1 18  ? 11.815 -8.661  6.243   0.66 17.42 ?  18  ILE   A HG13 1 
ATOM   486  H HG21 A ILE   A 1 18  ? 9.471  -11.173 6.674   0.34 15.78 ?  18  ILE   A HG21 1 
ATOM   487  H HG21 B ILE   A 1 18  ? 9.494  -11.469 6.487   0.66 18.01 ?  18  ILE   A HG21 1 
ATOM   488  H HG22 A ILE   A 1 18  ? 9.836  -11.530 8.178   0.34 15.78 ?  18  ILE   A HG22 1 
ATOM   489  H HG22 B ILE   A 1 18  ? 9.796  -11.701 8.029   0.66 18.01 ?  18  ILE   A HG22 1 
ATOM   490  H HG23 A ILE   A 1 18  ? 9.067  -10.180 7.848   0.34 15.78 ?  18  ILE   A HG23 1 
ATOM   491  H HG23 B ILE   A 1 18  ? 9.058  -10.377 7.554   0.66 18.01 ?  18  ILE   A HG23 1 
ATOM   492  H HD11 A ILE   A 1 18  ? 10.644 -8.409  4.494   0.34 17.99 ?  18  ILE   A HD11 1 
ATOM   493  H HD11 B ILE   A 1 18  ? 10.819 -8.838  4.191   0.66 19.00 ?  18  ILE   A HD11 1 
ATOM   494  H HD12 A ILE   A 1 18  ? 11.292 -9.845  4.701   0.34 17.99 ?  18  ILE   A HD12 1 
ATOM   495  H HD12 B ILE   A 1 18  ? 11.532 -10.216 4.530   0.66 19.00 ?  18  ILE   A HD12 1 
ATOM   496  H HD13 A ILE   A 1 18  ? 9.745  -9.622  4.986   0.34 17.99 ?  18  ILE   A HD13 1 
ATOM   497  H HD13 B ILE   A 1 18  ? 9.958  -10.077 4.689   0.66 19.00 ?  18  ILE   A HD13 1 
ATOM   498  N N    A LYS   A 1 19  ? 10.788 -7.556  9.409   0.34 11.97 ?  19  LYS   A N    1 
ATOM   499  N N    B LYS   A 1 19  ? 10.674 -7.738  9.052   0.66 14.51 ?  19  LYS   A N    1 
ATOM   500  C CA   A LYS   A 1 19  ? 10.002 -6.608  10.188  0.34 12.51 ?  19  LYS   A CA   1 
ATOM   501  C CA   B LYS   A 1 19  ? 9.817  -6.776  9.733   0.66 14.55 ?  19  LYS   A CA   1 
ATOM   502  C C    A LYS   A 1 19  ? 9.813  -5.336  9.374   0.34 12.27 ?  19  LYS   A C    1 
ATOM   503  C C    B LYS   A 1 19  ? 9.624  -5.561  8.836   0.66 13.58 ?  19  LYS   A C    1 
ATOM   504  O O    A LYS   A 1 19  ? 10.729 -4.907  8.671   0.34 12.40 ?  19  LYS   A O    1 
ATOM   505  O O    B LYS   A 1 19  ? 10.541 -5.169  8.110   0.66 12.80 ?  19  LYS   A O    1 
ATOM   506  C CB   A LYS   A 1 19  ? 10.735 -6.278  11.494  0.34 13.01 ?  19  LYS   A CB   1 
ATOM   507  C CB   B LYS   A 1 19  ? 10.477 -6.325  11.044  0.66 14.95 ?  19  LYS   A CB   1 
ATOM   508  C CG   A LYS   A 1 19  ? 10.045 -5.299  12.420  0.34 13.73 ?  19  LYS   A CG   1 
ATOM   509  C CG   B LYS   A 1 19  ? 9.661  -5.377  11.917  0.66 15.87 ?  19  LYS   A CG   1 
ATOM   510  C CD   A LYS   A 1 19  ? 10.960 -4.987  13.593  0.34 14.12 ?  19  LYS   A CD   1 
ATOM   511  C CD   B LYS   A 1 19  ? 10.470 -5.016  13.160  0.66 16.64 ?  19  LYS   A CD   1 
ATOM   512  C CE   A LYS   A 1 19  ? 10.282 -4.115  14.623  0.34 14.80 ?  19  LYS   A CE   1 
ATOM   513  C CE   B LYS   A 1 19  ? 9.712  -4.127  14.128  0.66 17.32 ?  19  LYS   A CE   1 
ATOM   514  N NZ   A LYS   A 1 19  ? 11.159 -3.895  15.805  0.34 14.87 ?  19  LYS   A NZ   1 
ATOM   515  N NZ   B LYS   A 1 19  ? 10.582 -3.738  15.277  0.66 17.67 ?  19  LYS   A NZ   1 
ATOM   516  H H    A LYS   A 1 19  ? 11.297 -7.172  8.822   0.34 14.52 ?  19  LYS   A H    1 
ATOM   517  H H    B LYS   A 1 19  ? 11.210 -7.388  8.480   0.66 17.56 ?  19  LYS   A H    1 
ATOM   518  H HA   A LYS   A 1 19  ? 9.133  -6.980  10.398  0.34 15.16 ?  19  LYS   A HA   1 
ATOM   519  H HA   B LYS   A 1 19  ? 8.954  -7.192  9.931   0.66 17.61 ?  19  LYS   A HA   1 
ATOM   520  H HB2  A LYS   A 1 19  ? 10.853 -7.102  11.992  0.34 15.76 ?  19  LYS   A HB2  1 
ATOM   521  H HB2  B LYS   A 1 19  ? 10.669 -7.115  11.579  0.66 18.09 ?  19  LYS   A HB2  1 
ATOM   522  H HB3  A LYS   A 1 19  ? 11.602 -5.905  11.276  0.34 15.76 ?  19  LYS   A HB3  1 
ATOM   523  H HB3  B LYS   A 1 19  ? 11.305 -5.880  10.822  0.66 18.09 ?  19  LYS   A HB3  1 
ATOM   524  H HG2  A LYS   A 1 19  ? 9.859  -4.473  11.947  0.34 16.63 ?  19  LYS   A HG2  1 
ATOM   525  H HG2  B LYS   A 1 19  ? 9.469  -4.561  11.426  0.66 19.19 ?  19  LYS   A HG2  1 
ATOM   526  H HG3  A LYS   A 1 19  ? 9.227  -5.692  12.761  0.34 16.63 ?  19  LYS   A HG3  1 
ATOM   527  H HG3  B LYS   A 1 19  ? 8.839  -5.808  12.198  0.66 19.19 ?  19  LYS   A HG3  1 
ATOM   528  H HD2  A LYS   A 1 19  ? 11.222 -5.819  14.020  0.34 17.10 ?  19  LYS   A HD2  1 
ATOM   529  H HD2  B LYS   A 1 19  ? 10.709 -5.832  13.627  0.66 20.11 ?  19  LYS   A HD2  1 
ATOM   530  H HD3  A LYS   A 1 19  ? 11.747 -4.521  13.265  0.34 17.10 ?  19  LYS   A HD3  1 
ATOM   531  H HD3  B LYS   A 1 19  ? 11.273 -4.544  12.887  0.66 20.11 ?  19  LYS   A HD3  1 
ATOM   532  H HE2  A LYS   A 1 19  ? 10.083 -3.253  14.227  0.34 17.91 ?  19  LYS   A HE2  1 
ATOM   533  H HE2  B LYS   A 1 19  ? 9.429  -3.320  13.671  0.66 20.93 ?  19  LYS   A HE2  1 
ATOM   534  H HE3  A LYS   A 1 19  ? 9.470  -4.548  14.921  0.34 17.91 ?  19  LYS   A HE3  1 
ATOM   535  H HE3  B LYS   A 1 19  ? 8.944  -4.608  14.474  0.66 20.93 ?  19  LYS   A HE3  1 
ATOM   536  H HZ1  A LYS   A 1 19  ? 10.735 -3.398  16.408  0.34 17.99 ?  19  LYS   A HZ1  1 
ATOM   537  H HZ1  B LYS   A 1 19  ? 10.130 -3.219  15.839  0.66 21.36 ?  19  LYS   A HZ1  1 
ATOM   538  H HZ2  A LYS   A 1 19  ? 11.375 -4.677  16.172  0.34 17.99 ?  19  LYS   A HZ2  1 
ATOM   539  H HZ2  B LYS   A 1 19  ? 10.855 -4.467  15.710  0.66 21.36 ?  19  LYS   A HZ2  1 
ATOM   540  H HZ3  A LYS   A 1 19  ? 11.905 -3.478  15.557  0.34 17.99 ?  19  LYS   A HZ3  1 
ATOM   541  H HZ3  B LYS   A 1 19  ? 11.295 -3.295  14.980  0.66 21.36 ?  19  LYS   A HZ3  1 
ATOM   542  N N    A ASN   A 1 20  ? 8.623  -4.740  9.462   0.34 12.32 ?  20  ASN   A N    1 
ATOM   543  N N    B ASN   A 1 20  ? 8.430  -4.974  8.886   0.66 13.95 ?  20  ASN   A N    1 
ATOM   544  C CA   A ASN   A 1 20  ? 8.390  -3.425  8.866   0.34 12.51 ?  20  ASN   A CA   1 
ATOM   545  C CA   B ASN   A 1 20  ? 8.182  -3.692  8.230   0.66 14.45 ?  20  ASN   A CA   1 
ATOM   546  C C    A ASN   A 1 20  ? 8.980  -2.392  9.814   0.34 12.95 ?  20  ASN   A C    1 
ATOM   547  C C    B ASN   A 1 20  ? 8.740  -2.606  9.144   0.66 14.45 ?  20  ASN   A C    1 
ATOM   548  O O    A ASN   A 1 20  ? 8.419  -2.114  10.876  0.34 13.49 ?  20  ASN   A O    1 
ATOM   549  O O    B ASN   A 1 20  ? 8.128  -2.260  10.157  0.66 16.31 ?  20  ASN   A O    1 
ATOM   550  C CB   A ASN   A 1 20  ? 6.901  -3.190  8.629   0.34 12.62 ?  20  ASN   A CB   1 
ATOM   551  C CB   B ASN   A 1 20  ? 6.686  -3.511  7.983   0.66 15.74 ?  20  ASN   A CB   1 
ATOM   552  C CG   A ASN   A 1 20  ? 6.579  -1.748  8.256   0.34 13.37 ?  20  ASN   A CG   1 
ATOM   553  C CG   B ASN   A 1 20  ? 6.331  -2.118  7.480   0.66 17.10 ?  20  ASN   A CG   1 
ATOM   554  O OD1  A ASN   A 1 20  ? 5.653  -1.149  8.804   0.34 14.92 ?  20  ASN   A OD1  1 
ATOM   555  O OD1  B ASN   A 1 20  ? 5.289  -1.561  7.844   0.66 18.64 ?  20  ASN   A OD1  1 
ATOM   556  N ND2  A ASN   A 1 20  ? 7.346  -1.184  7.327   0.34 13.54 ?  20  ASN   A ND2  1 
ATOM   557  N ND2  B ASN   A 1 20  ? 7.187  -1.555  6.634   0.66 17.10 ?  20  ASN   A ND2  1 
ATOM   558  H H    A ASN   A 1 20  ? 7.934  -5.070  9.857   0.34 14.94 ?  20  ASN   A H    1 
ATOM   559  H H    B ASN   A 1 20  ? 7.740  -5.320  9.285   0.66 16.90 ?  20  ASN   A H    1 
ATOM   560  H HA   A ASN   A 1 20  ? 8.855  -3.367  8.020   0.34 15.16 ?  20  ASN   A HA   1 
ATOM   561  H HA   B ASN   A 1 20  ? 8.646  -3.678  7.377   0.66 17.49 ?  20  ASN   A HA   1 
ATOM   562  H HB2  A ASN   A 1 20  ? 6.610  -3.761  7.903   0.34 15.30 ?  20  ASN   A HB2  1 
ATOM   563  H HB2  B ASN   A 1 20  ? 6.392  -4.154  7.313   0.66 19.04 ?  20  ASN   A HB2  1 
ATOM   564  H HB3  A ASN   A 1 20  ? 6.415  -3.401  9.438   0.34 15.30 ?  20  ASN   A HB3  1 
ATOM   565  H HB3  B ASN   A 1 20  ? 6.208  -3.673  8.813   0.66 19.04 ?  20  ASN   A HB3  1 
ATOM   566  H HD21 A ASN   A 1 20  ? 7.198  -0.371  7.084   0.34 16.40 ?  20  ASN   A HD21 1 
ATOM   567  H HD21 B ASN   A 1 20  ? 7.026  -0.772  6.329   0.66 20.67 ?  20  ASN   A HD21 1 
ATOM   568  H HD22 A ASN   A 1 20  ? 7.986  -1.630  6.965   0.34 16.40 ?  20  ASN   A HD22 1 
ATOM   569  H HD22 B ASN   A 1 20  ? 7.901  -1.975  6.393   0.66 20.67 ?  20  ASN   A HD22 1 
ATOM   570  N N    A ALA   A 1 21  ? 10.136 -1.842  9.452   0.34 12.49 ?  21  ALA   A N    1 
ATOM   571  N N    B ALA   A 1 21  ? 9.923  -2.087  8.808   0.66 13.82 ?  21  ALA   A N    1 
ATOM   572  C CA   A ALA   A 1 21  ? 10.813 -0.911  10.341  0.34 12.90 ?  21  ALA   A CA   1 
ATOM   573  C CA   B ALA   A 1 21  ? 10.592 -1.117  9.667   0.66 14.11 ?  21  ALA   A CA   1 
ATOM   574  C C    A ALA   A 1 21  ? 11.863 -0.139  9.562   0.34 13.23 ?  21  ALA   A C    1 
ATOM   575  C C    B ALA   A 1 21  ? 11.654 -0.368  8.876   0.66 12.80 ?  21  ALA   A C    1 
ATOM   576  O O    A ALA   A 1 21  ? 12.401 -0.629  8.566   0.34 13.51 ?  21  ALA   A O    1 
ATOM   577  O O    B ALA   A 1 21  ? 12.142 -0.852  7.853   0.66 12.82 ?  21  ALA   A O    1 
ATOM   578  C CB   A ALA   A 1 21  ? 11.471 -1.645  11.513  0.34 13.63 ?  21  ALA   A CB   1 
ATOM   579  C CB   B ALA   A 1 21  ? 11.247 -1.801  10.869  0.66 15.98 ?  21  ALA   A CB   1 
ATOM   580  H H    A ALA   A 1 21  ? 10.550 -1.986  8.705   0.34 15.13 ?  21  ALA   A H    1 
ATOM   581  H H    B ALA   A 1 21  ? 10.346 -2.286  8.085   0.66 16.73 ?  21  ALA   A H    1 
ATOM   582  H HA   A ALA   A 1 21  ? 10.175 -0.271  10.693  0.34 15.63 ?  21  ALA   A HA   1 
ATOM   583  H HA   B ALA   A 1 21  ? 9.931  -0.484  9.992   0.66 17.09 ?  21  ALA   A HA   1 
ATOM   584  H HB1  A ALA   A 1 21  ? 11.878 -0.995  12.104  0.34 16.50 ?  21  ALA   A HB1  1 
ATOM   585  H HB1  B ALA   A 1 21  ? 11.675 -1.124  11.413  0.66 19.33 ?  21  ALA   A HB1  1 
ATOM   586  H HB2  A ALA   A 1 21  ? 10.788 -2.145  11.988  0.34 16.50 ?  21  ALA   A HB2  1 
ATOM   587  H HB2  B ALA   A 1 21  ? 10.561 -2.256  11.385  0.66 19.33 ?  21  ALA   A HB2  1 
ATOM   588  H HB3  A ALA   A 1 21  ? 12.144 -2.251  11.168  0.34 16.50 ?  21  ALA   A HB3  1 
ATOM   589  H HB3  B ALA   A 1 21  ? 11.900 -2.438  10.550  0.66 19.33 ?  21  ALA   A HB3  1 
ATOM   590  N N    A ASP   A 1 22  ? 12.124 1.082   10.026  0.34 14.18 ?  22  ASP   A N    1 
ATOM   591  N N    B ASP   A 1 22  ? 12.001 0.820   9.381   0.66 12.31 ?  22  ASP   A N    1 
ATOM   592  C CA   A ASP   A 1 22  ? 13.231 1.890   9.537   0.34 14.75 ?  22  ASP   A CA   1 
ATOM   593  C CA   B ASP   A 1 22  ? 13.110 1.618   8.871   0.66 11.58 ?  22  ASP   A CA   1 
ATOM   594  C C    A ASP   A 1 22  ? 14.532 1.338   10.110  0.34 14.34 ?  22  ASP   A C    1 
ATOM   595  C C    B ASP   A 1 22  ? 14.401 1.114   9.513   0.66 10.84 ?  22  ASP   A C    1 
ATOM   596  O O    A ASP   A 1 22  ? 14.699 1.276   11.333  0.34 14.64 ?  22  ASP   A O    1 
ATOM   597  O O    B ASP   A 1 22  ? 14.536 1.138   10.740  0.66 12.00 ?  22  ASP   A O    1 
ATOM   598  C CB   A ASP   A 1 22  ? 13.023 3.332   9.997   0.34 15.72 ?  22  ASP   A CB   1 
ATOM   599  C CB   B ASP   A 1 22  ? 12.858 3.079   9.251   0.66 12.63 ?  22  ASP   A CB   1 
ATOM   600  C CG   A ASP   A 1 22  ? 14.040 4.289   9.403   0.34 15.87 ?  22  ASP   A CG   1 
ATOM   601  C CG   B ASP   A 1 22  ? 13.878 4.043   8.664   0.66 13.64 ?  22  ASP   A CG   1 
ATOM   602  O OD1  A ASP   A 1 22  ? 15.027 3.824   8.795   0.34 15.93 ?  22  ASP   A OD1  1 
ATOM   603  O OD1  B ASP   A 1 22  ? 15.029 3.637   8.382   0.66 12.88 ?  22  ASP   A OD1  1 
ATOM   604  O OD2  A ASP   A 1 22  ? 13.843 5.514   9.538   0.34 16.09 -1 22  ASP   A OD2  1 
ATOM   605  O OD2  B ASP   A 1 22  ? 13.513 5.227   8.496   0.66 15.98 -1 22  ASP   A OD2  1 
ATOM   606  H H    A ASP   A 1 22  ? 11.660 1.474   10.626  0.34 17.17 ?  22  ASP   A H    1 
ATOM   607  H H    B ASP   A 1 22  ? 11.588 1.185   10.048  0.66 14.92 ?  22  ASP   A H    1 
ATOM   608  H HA   A ASP   A 1 22  ? 13.271 1.875   8.565   0.34 17.85 ?  22  ASP   A HA   1 
ATOM   609  H HA   B ASP   A 1 22  ? 13.162 1.534   7.907   0.66 14.04 ?  22  ASP   A HA   1 
ATOM   610  H HB2  A ASP   A 1 22  ? 12.134 3.628   9.730   0.34 19.02 ?  22  ASP   A HB2  1 
ATOM   611  H HB2  B ASP   A 1 22  ? 11.979 3.339   8.936   0.66 15.31 ?  22  ASP   A HB2  1 
ATOM   612  H HB3  A ASP   A 1 22  ? 13.092 3.367   10.970  0.34 19.02 ?  22  ASP   A HB3  1 
ATOM   613  H HB3  B ASP   A 1 22  ? 12.896 3.157   10.220  0.66 15.31 ?  22  ASP   A HB3  1 
ATOM   614  N N    A ILE   A 1 23  ? 15.450 0.929   9.229   0.34 13.74 ?  23  ILE   A N    1 
ATOM   615  N N    B ILE   A 1 23  ? 15.345 0.644   8.689   0.66 11.06 ?  23  ILE   A N    1 
ATOM   616  C CA   A ILE   A 1 23  ? 16.714 0.361   9.688   0.34 13.11 ?  23  ILE   A CA   1 
ATOM   617  C CA   B ILE   A 1 23  ? 16.589 0.084   9.215   0.66 11.25 ?  23  ILE   A CA   1 
ATOM   618  C C    A ILE   A 1 23  ? 17.462 1.344   10.576  0.34 12.90 ?  23  ILE   A C    1 
ATOM   619  C C    B ILE   A 1 23  ? 17.304 1.076   10.124  0.66 11.50 ?  23  ILE   A C    1 
ATOM   620  O O    A ILE   A 1 23  ? 18.185 0.937   11.494  0.34 12.93 ?  23  ILE   A O    1 
ATOM   621  O O    B ILE   A 1 23  ? 17.979 0.672   11.081  0.66 11.78 ?  23  ILE   A O    1 
ATOM   622  C CB   A ILE   A 1 23  ? 17.559 -0.126  8.488   0.34 12.91 ?  23  ILE   A CB   1 
ATOM   623  C CB   B ILE   A 1 23  ? 17.501 -0.446  8.082   0.66 11.41 ?  23  ILE   A CB   1 
ATOM   624  C CG1  A ILE   A 1 23  ? 18.743 -0.973  8.968   0.34 13.06 ?  23  ILE   A CG1  1 
ATOM   625  C CG1  B ILE   A 1 23  ? 18.545 -1.402  8.666   0.66 12.09 ?  23  ILE   A CG1  1 
ATOM   626  C CG2  A ILE   A 1 23  ? 18.019 1.052   7.628   0.34 12.84 ?  23  ILE   A CG2  1 
ATOM   627  C CG2  B ILE   A 1 23  ? 18.173 0.699   7.318   0.66 11.72 ?  23  ILE   A CG2  1 
ATOM   628  C CD1  A ILE   A 1 23  ? 19.453 -1.712  7.849   0.34 13.33 ?  23  ILE   A CD1  1 
ATOM   629  C CD1  B ILE   A 1 23  ? 19.472 -2.008  7.635   0.66 12.47 ?  23  ILE   A CD1  1 
ATOM   630  H H    A ILE   A 1 23  ? 15.364 0.968   8.376   0.34 16.64 ?  23  ILE   A H    1 
ATOM   631  H H    B ILE   A 1 23  ? 15.279 0.617   7.842   0.66 13.43 ?  23  ILE   A H    1 
ATOM   632  H HA   A ILE   A 1 23  ? 16.522 -0.414  10.230  0.34 15.88 ?  23  ILE   A HA   1 
ATOM   633  H HA   B ILE   A 1 23  ? 16.352 -0.685  9.758   0.66 13.65 ?  23  ILE   A HA   1 
ATOM   634  H HB   A ILE   A 1 23  ? 16.996 -0.690  7.939   0.34 15.64 ?  23  ILE   A HB   1 
ATOM   635  H HB   B ILE   A 1 23  ? 16.953 -0.952  7.457   0.66 13.85 ?  23  ILE   A HB   1 
ATOM   636  H HG12 A ILE   A 1 23  ? 19.392 -0.398  9.399   0.34 15.83 ?  23  ILE   A HG12 1 
ATOM   637  H HG12 B ILE   A 1 23  ? 19.091 -0.922  9.306   0.66 14.66 ?  23  ILE   A HG12 1 
ATOM   638  H HG13 A ILE   A 1 23  ? 18.419 -1.636  9.599   0.34 15.83 ?  23  ILE   A HG13 1 
ATOM   639  H HG13 B ILE   A 1 23  ? 18.088 -2.137  9.114   0.66 14.66 ?  23  ILE   A HG13 1 
ATOM   640  H HG21 A ILE   A 1 23  ? 18.417 0.710   6.810   0.34 15.56 ?  23  ILE   A HG21 1 
ATOM   641  H HG21 B ILE   A 1 23  ? 18.559 0.346   6.498   0.66 14.21 ?  23  ILE   A HG21 1 
ATOM   642  H HG22 A ILE   A 1 23  ? 17.250 1.603   7.412   0.34 15.56 ?  23  ILE   A HG22 1 
ATOM   643  H HG22 B ILE   A 1 23  ? 17.505 1.366   7.107   0.66 14.21 ?  23  ILE   A HG22 1 
ATOM   644  H HG23 A ILE   A 1 23  ? 18.672 1.572   8.120   0.34 15.56 ?  23  ILE   A HG23 1 
ATOM   645  H HG23 B ILE   A 1 23  ? 18.867 1.082   7.873   0.66 14.21 ?  23  ILE   A HG23 1 
ATOM   646  H HD11 A ILE   A 1 23  ? 20.151 -2.268  8.230   0.34 16.15 ?  23  ILE   A HD11 1 
ATOM   647  H HD11 B ILE   A 1 23  ? 20.014 -2.692  8.061   0.66 15.11 ?  23  ILE   A HD11 1 
ATOM   648  H HD12 A ILE   A 1 23  ? 18.810 -2.267  7.379   0.34 16.15 ?  23  ILE   A HD12 1 
ATOM   649  H HD12 B ILE   A 1 23  ? 18.939 -2.403  6.928   0.66 15.11 ?  23  ILE   A HD12 1 
ATOM   650  H HD13 A ILE   A 1 23  ? 19.840 -1.066  7.239   0.34 16.15 ?  23  ILE   A HD13 1 
ATOM   651  H HD13 B ILE   A 1 23  ? 20.040 -1.311  7.276   0.66 15.11 ?  23  ILE   A HD13 1 
ATOM   652  N N    A VAL   A 1 24  ? 17.291 2.646   10.337  0.34 13.41 ?  24  VAL   A N    1 
ATOM   653  N N    B VAL   A 1 24  ? 17.179 2.377   9.850   0.66 11.98 ?  24  VAL   A N    1 
ATOM   654  C CA   A VAL   A 1 24  ? 17.948 3.649   11.171  0.34 14.22 ?  24  VAL   A CA   1 
ATOM   655  C CA   B VAL   A 1 24  ? 17.843 3.371   10.688  0.66 12.93 ?  24  VAL   A CA   1 
ATOM   656  C C    A VAL   A 1 24  ? 17.437 3.563   12.604  0.34 14.97 ?  24  VAL   A C    1 
ATOM   657  C C    B VAL   A 1 24  ? 17.241 3.381   12.087  0.66 13.61 ?  24  VAL   A C    1 
ATOM   658  O O    A VAL   A 1 24  ? 18.219 3.504   13.562  0.34 14.91 ?  24  VAL   A O    1 
ATOM   659  O O    B VAL   A 1 24  ? 17.963 3.441   13.090  0.66 14.75 ?  24  VAL   A O    1 
ATOM   660  C CB   A VAL   A 1 24  ? 17.744 5.053   10.575  0.34 13.95 ?  24  VAL   A CB   1 
ATOM   661  C CB   B VAL   A 1 24  ? 17.791 4.759   10.027  0.66 13.52 ?  24  VAL   A CB   1 
ATOM   662  C CG1  A VAL   A 1 24  ? 18.191 6.123   11.560  0.34 13.74 ?  24  VAL   A CG1  1 
ATOM   663  C CG1  B VAL   A 1 24  ? 18.530 5.778   10.878  0.66 14.96 ?  24  VAL   A CG1  1 
ATOM   664  C CG2  A VAL   A 1 24  ? 18.497 5.183   9.259   0.34 14.12 ?  24  VAL   A CG2  1 
ATOM   665  C CG2  B VAL   A 1 24  ? 18.374 4.701   8.628   0.66 14.13 ?  24  VAL   A CG2  1 
ATOM   666  H H    A VAL   A 1 24  ? 16.806 2.973   9.705   0.34 16.24 ?  24  VAL   A H    1 
ATOM   667  H H    B VAL   A 1 24  ? 16.718 2.701   9.198   0.66 14.53 ?  24  VAL   A H    1 
ATOM   668  H HA   A VAL   A 1 24  ? 18.901 3.475   11.185  0.34 17.22 ?  24  VAL   A HA   1 
ATOM   669  H HA   B VAL   A 1 24  ? 18.772 3.123   10.776  0.66 15.67 ?  24  VAL   A HA   1 
ATOM   670  H HB   A VAL   A 1 24  ? 16.802 5.192   10.392  0.34 16.90 ?  24  VAL   A HB   1 
ATOM   671  H HB   B VAL   A 1 24  ? 16.866 5.043   9.954   0.66 16.37 ?  24  VAL   A HB   1 
ATOM   672  H HG11 A VAL   A 1 24  ? 18.325 6.957   11.082  0.34 16.65 ?  24  VAL   A HG11 1 
ATOM   673  H HG11 B VAL   A 1 24  ? 18.630 6.596   10.372  0.66 18.10 ?  24  VAL   A HG11 1 
ATOM   674  H HG12 A VAL   A 1 24  ? 17.505 6.239   12.236  0.34 16.65 ?  24  VAL   A HG12 1 
ATOM   675  H HG12 B VAL   A 1 24  ? 18.016 5.947   11.684  0.66 18.10 ?  24  VAL   A HG12 1 
ATOM   676  H HG13 A VAL   A 1 24  ? 19.023 5.844   11.973  0.34 16.65 ?  24  VAL   A HG13 1 
ATOM   677  H HG13 B VAL   A 1 24  ? 19.401 5.420   11.109  0.66 18.10 ?  24  VAL   A HG13 1 
ATOM   678  H HG21 A VAL   A 1 24  ? 18.248 6.016   8.829   0.34 17.10 ?  24  VAL   A HG21 1 
ATOM   679  H HG21 B VAL   A 1 24  ? 18.478 5.601   8.291   0.66 17.11 ?  24  VAL   A HG21 1 
ATOM   680  H HG22 A VAL   A 1 24  ? 19.452 5.179   9.438   0.34 17.10 ?  24  VAL   A HG22 1 
ATOM   681  H HG22 B VAL   A 1 24  ? 19.239 4.259   8.668   0.66 17.11 ?  24  VAL   A HG22 1 
ATOM   682  H HG23 A VAL   A 1 24  ? 18.265 4.435   8.686   0.34 17.10 ?  24  VAL   A HG23 1 
ATOM   683  H HG23 B VAL   A 1 24  ? 17.775 4.196   8.057   0.66 17.11 ?  24  VAL   A HG23 1 
ATOM   684  N N    A GLU   A 1 25  ? 16.113 3.563   12.773  0.34 15.85 ?  25  GLU   A N    1 
ATOM   685  N N    B GLU   A 1 25  ? 15.909 3.329   12.181  0.66 14.52 ?  25  GLU   A N    1 
ATOM   686  C CA   A GLU   A 1 25  ? 15.541 3.481   14.113  0.34 17.36 ?  25  GLU   A CA   1 
ATOM   687  C CA   B GLU   A 1 25  ? 15.258 3.284   13.488  0.66 15.22 ?  25  GLU   A CA   1 
ATOM   688  C C    A GLU   A 1 25  ? 15.752 2.105   14.733  0.34 16.61 ?  25  GLU   A C    1 
ATOM   689  C C    B GLU   A 1 25  ? 15.560 1.980   14.209  0.66 14.92 ?  25  GLU   A C    1 
ATOM   690  O O    A GLU   A 1 25  ? 15.923 1.999   15.953  0.34 16.40 ?  25  GLU   A O    1 
ATOM   691  O O    B GLU   A 1 25  ? 15.788 1.974   15.424  0.66 15.86 ?  25  GLU   A O    1 
ATOM   692  C CB   A GLU   A 1 25  ? 14.058 3.855   14.078  0.34 19.27 ?  25  GLU   A CB   1 
ATOM   693  C CB   B GLU   A 1 25  ? 13.750 3.490   13.336  0.66 16.73 ?  25  GLU   A CB   1 
ATOM   694  C CG   A GLU   A 1 25  ? 13.808 5.302   13.674  0.34 21.01 ?  25  GLU   A CG   1 
ATOM   695  C CG   B GLU   A 1 25  ? 13.380 4.883   12.861  0.66 20.61 ?  25  GLU   A CG   1 
ATOM   696  C CD   A GLU   A 1 25  ? 14.582 6.288   14.530  0.34 22.34 ?  25  GLU   A CD   1 
ATOM   697  C CD   B GLU   A 1 25  ? 13.965 5.972   13.738  0.66 23.87 ?  25  GLU   A CD   1 
ATOM   698  O OE1  A GLU   A 1 25  ? 14.678 6.067   15.756  0.34 22.75 ?  25  GLU   A OE1  1 
ATOM   699  O OE1  B GLU   A 1 25  ? 13.973 5.802   14.977  0.66 25.34 ?  25  GLU   A OE1  1 
ATOM   700  O OE2  A GLU   A 1 25  ? 15.113 7.271   13.972  0.34 23.07 -1 25  GLU   A OE2  1 
ATOM   701  O OE2  B GLU   A 1 25  ? 14.431 6.989   13.187  0.66 25.12 -1 25  GLU   A OE2  1 
ATOM   702  H H    A GLU   A 1 25  ? 15.537 3.616   12.135  0.34 19.17 ?  25  GLU   A H    1 
ATOM   703  H H    B GLU   A 1 25  ? 15.366 3.327   11.513  0.66 17.57 ?  25  GLU   A H    1 
ATOM   704  H HA   A GLU   A 1 25  ? 15.996 4.121   14.679  0.34 20.98 ?  25  GLU   A HA   1 
ATOM   705  H HA   B GLU   A 1 25  ? 15.608 3.998   14.039  0.66 18.41 ?  25  GLU   A HA   1 
ATOM   706  H HB2  A GLU   A 1 25  ? 13.603 3.289   13.435  0.34 23.28 ?  25  GLU   A HB2  1 
ATOM   707  H HB2  B GLU   A 1 25  ? 13.407 2.855   12.687  0.66 20.22 ?  25  GLU   A HB2  1 
ATOM   708  H HB3  A GLU   A 1 25  ? 13.678 3.725   14.960  0.34 23.28 ?  25  GLU   A HB3  1 
ATOM   709  H HB3  B GLU   A 1 25  ? 13.322 3.347   14.195  0.66 20.22 ?  25  GLU   A HB3  1 
ATOM   710  H HG2  A GLU   A 1 25  ? 14.089 5.428   12.755  0.34 25.37 ?  25  GLU   A HG2  1 
ATOM   711  H HG2  B GLU   A 1 25  ? 13.718 5.009   11.961  0.66 24.89 ?  25  GLU   A HG2  1 
ATOM   712  H HG3  A GLU   A 1 25  ? 12.862 5.497   13.764  0.34 25.37 ?  25  GLU   A HG3  1 
ATOM   713  H HG3  B GLU   A 1 25  ? 12.417 4.978   12.875  0.66 24.89 ?  25  GLU   A HG3  1 
ATOM   714  N N    A GLU   A 1 26  ? 15.752 1.046   13.920  0.34 16.08 ?  26  GLU   A N    1 
ATOM   715  N N    B GLU   A 1 26  ? 15.567 0.864   13.479  0.66 14.63 ?  26  GLU   A N    1 
ATOM   716  C CA   A GLU   A 1 26  ? 16.081 -0.279  14.439  0.34 16.27 ?  26  GLU   A CA   1 
ATOM   717  C CA   B GLU   A 1 26  ? 15.934 -0.407  14.092  0.66 15.00 ?  26  GLU   A CA   1 
ATOM   718  C C    A GLU   A 1 26  ? 17.500 -0.307  14.991  0.34 16.34 ?  26  GLU   A C    1 
ATOM   719  C C    B GLU   A 1 26  ? 17.345 -0.346  14.663  0.66 13.98 ?  26  GLU   A C    1 
ATOM   720  O O    A GLU   A 1 26  ? 17.742 -0.805  16.097  0.34 16.68 ?  26  GLU   A O    1 
ATOM   721  O O    B GLU   A 1 26  ? 17.593 -0.812  15.781  0.66 14.77 ?  26  GLU   A O    1 
ATOM   722  C CB   A GLU   A 1 26  ? 15.925 -1.332  13.340  0.34 16.64 ?  26  GLU   A CB   1 
ATOM   723  C CB   B GLU   A 1 26  ? 15.822 -1.542  13.071  0.66 16.37 ?  26  GLU   A CB   1 
ATOM   724  C CG   A GLU   A 1 26  ? 14.508 -1.818  13.120  0.34 17.60 ?  26  GLU   A CG   1 
ATOM   725  C CG   B GLU   A 1 26  ? 14.404 -1.962  12.750  0.66 17.88 ?  26  GLU   A CG   1 
ATOM   726  C CD   A GLU   A 1 26  ? 13.978 -2.638  14.286  0.34 18.19 ?  26  GLU   A CD   1 
ATOM   727  C CD   B GLU   A 1 26  ? 13.700 -2.578  13.939  0.66 18.87 ?  26  GLU   A CD   1 
ATOM   728  O OE1  A GLU   A 1 26  ? 14.364 -3.821  14.425  0.34 18.61 ?  26  GLU   A OE1  1 
ATOM   729  O OE1  B GLU   A 1 26  ? 14.241 -3.549  14.513  0.66 19.71 ?  26  GLU   A OE1  1 
ATOM   730  O OE2  A GLU   A 1 26  ? 13.181 -2.090  15.069  0.34 18.22 -1 26  GLU   A OE2  1 
ATOM   731  O OE2  B GLU   A 1 26  ? 12.619 -2.080  14.307  0.66 18.41 -1 26  GLU   A OE2  1 
ATOM   732  H H    A GLU   A 1 26  ? 15.573 1.073   13.079  0.34 19.45 ?  26  GLU   A H    1 
ATOM   733  H H    B GLU   A 1 26  ? 15.370 0.817   12.641  0.66 17.71 ?  26  GLU   A H    1 
ATOM   734  H HA   A GLU   A 1 26  ? 15.474 -0.497  15.159  0.34 19.68 ?  26  GLU   A HA   1 
ATOM   735  H HA   B GLU   A 1 26  ? 15.323 -0.597  14.818  0.66 18.15 ?  26  GLU   A HA   1 
ATOM   736  H HB2  A GLU   A 1 26  ? 16.240 -0.955  12.503  0.34 20.12 ?  26  GLU   A HB2  1 
ATOM   737  H HB2  B GLU   A 1 26  ? 16.237 -1.259  12.240  0.66 19.80 ?  26  GLU   A HB2  1 
ATOM   738  H HB3  A GLU   A 1 26  ? 16.466 -2.102  13.573  0.34 20.12 ?  26  GLU   A HB3  1 
ATOM   739  H HB3  B GLU   A 1 26  ? 16.287 -2.321  13.417  0.66 19.80 ?  26  GLU   A HB3  1 
ATOM   740  H HG2  A GLU   A 1 26  ? 13.934 -1.046  12.990  0.34 21.27 ?  26  GLU   A HG2  1 
ATOM   741  H HG2  B GLU   A 1 26  ? 13.898 -1.184  12.469  0.66 21.61 ?  26  GLU   A HG2  1 
ATOM   742  H HG3  A GLU   A 1 26  ? 14.489 -2.382  12.333  0.34 21.27 ?  26  GLU   A HG3  1 
ATOM   743  H HG3  B GLU   A 1 26  ? 14.418 -2.623  12.041  0.66 21.61 ?  26  GLU   A HG3  1 
ATOM   744  N N    A ALA   A 1 27  ? 18.458 0.227   14.230  0.34 16.44 ?  27  ALA   A N    1 
ATOM   745  N N    B ALA   A 1 27  ? 18.287 0.228   13.914  0.66 12.80 ?  27  ALA   A N    1 
ATOM   746  C CA   A ALA   A 1 27  ? 19.850 0.178   14.663  0.34 17.07 ?  27  ALA   A CA   1 
ATOM   747  C CA   B ALA   A 1 27  ? 19.662 0.301   14.397  0.66 13.03 ?  27  ALA   A CA   1 
ATOM   748  C C    A ALA   A 1 27  ? 20.057 0.976   15.944  0.34 18.52 ?  27  ALA   A C    1 
ATOM   749  C C    B ALA   A 1 27  ? 19.765 1.169   15.646  0.66 13.79 ?  27  ALA   A C    1 
ATOM   750  O O    A ALA   A 1 27  ? 20.743 0.517   16.865  0.34 18.59 ?  27  ALA   A O    1 
ATOM   751  O O    B ALA   A 1 27  ? 20.413 0.787   16.628  0.66 14.09 ?  27  ALA   A O    1 
ATOM   752  C CB   A ALA   A 1 27  ? 20.770 0.680   13.548  0.34 16.71 ?  27  ALA   A CB   1 
ATOM   753  C CB   B ALA   A 1 27  ? 20.585 0.817   13.291  0.66 13.14 ?  27  ALA   A CB   1 
ATOM   754  H H    A ALA   A 1 27  ? 18.330 0.622   13.476  0.34 19.88 ?  27  ALA   A H    1 
ATOM   755  H H    B ALA   A 1 27  ? 18.153 0.574   13.135  0.66 15.51 ?  27  ALA   A H    1 
ATOM   756  H HA   A ALA   A 1 27  ? 20.089 -0.741  14.847  0.34 20.64 ?  27  ALA   A HA   1 
ATOM   757  H HA   B ALA   A 1 27  ? 19.953 -0.589  14.632  0.66 15.79 ?  27  ALA   A HA   1 
ATOM   758  H HB1  A ALA   A 1 27  ? 21.692 0.639   13.852  0.34 20.21 ?  27  ALA   A HB1  1 
ATOM   759  H HB1  B ALA   A 1 27  ? 21.491 0.859   13.632  0.66 15.92 ?  27  ALA   A HB1  1 
ATOM   760  H HB2  A ALA   A 1 27  ? 20.659 0.114   12.765  0.34 20.21 ?  27  ALA   A HB2  1 
ATOM   761  H HB2  B ALA   A 1 27  ? 20.544 0.210   12.534  0.66 15.92 ?  27  ALA   A HB2  1 
ATOM   762  H HB3  A ALA   A 1 27  ? 20.537 1.595   13.328  0.34 20.21 ?  27  ALA   A HB3  1 
ATOM   763  H HB3  B ALA   A 1 27  ? 20.293 1.702   13.018  0.66 15.92 ?  27  ALA   A HB3  1 
ATOM   764  N N    A LYS   A 1 28  ? 19.465 2.170   16.028  0.34 20.34 ?  28  LYS   A N    1 
ATOM   765  N N    B LYS   A 1 28  ? 19.125 2.343   15.633  0.66 15.15 ?  28  LYS   A N    1 
ATOM   766  C CA   A LYS   A 1 28  ? 19.626 2.982   17.229  0.34 22.46 ?  28  LYS   A CA   1 
ATOM   767  C CA   B LYS   A 1 28  ? 19.193 3.226   16.794  0.66 18.14 ?  28  LYS   A CA   1 
ATOM   768  C C    A LYS   A 1 28  ? 19.048 2.289   18.457  0.34 23.35 ?  28  LYS   A C    1 
ATOM   769  C C    B LYS   A 1 28  ? 18.644 2.552   18.044  0.66 19.09 ?  28  LYS   A C    1 
ATOM   770  O O    A LYS   A 1 28  ? 19.566 2.459   19.566  0.34 23.78 ?  28  LYS   A O    1 
ATOM   771  O O    B LYS   A 1 28  ? 19.179 2.740   19.143  0.66 20.32 ?  28  LYS   A O    1 
ATOM   772  C CB   A LYS   A 1 28  ? 18.999 4.364   17.027  0.34 23.87 ?  28  LYS   A CB   1 
ATOM   773  C CB   B LYS   A 1 28  ? 18.449 4.534   16.518  0.66 21.10 ?  28  LYS   A CB   1 
ATOM   774  C CG   A LYS   A 1 28  ? 19.829 5.285   16.143  0.34 25.21 ?  28  LYS   A CG   1 
ATOM   775  C CG   B LYS   A 1 28  ? 19.232 5.497   15.651  0.66 24.33 ?  28  LYS   A CG   1 
ATOM   776  C CD   A LYS   A 1 28  ? 19.327 6.720   16.178  0.34 26.44 ?  28  LYS   A CD   1 
ATOM   777  C CD   B LYS   A 1 28  ? 18.683 6.911   15.717  0.66 27.73 ?  28  LYS   A CD   1 
ATOM   778  C CE   A LYS   A 1 28  ? 18.011 6.873   15.437  0.34 27.24 ?  28  LYS   A CE   1 
ATOM   779  C CE   B LYS   A 1 28  ? 17.537 7.110   14.748  0.66 30.04 ?  28  LYS   A CE   1 
ATOM   780  N NZ   A LYS   A 1 28  ? 17.603 8.302   15.346  0.34 27.87 ?  28  LYS   A NZ   1 
ATOM   781  N NZ   B LYS   A 1 28  ? 17.154 8.546   14.647  0.66 31.12 ?  28  LYS   A NZ   1 
ATOM   782  H H    A LYS   A 1 28  ? 18.976 2.523   15.415  0.34 24.56 ?  28  LYS   A H    1 
ATOM   783  H H    B LYS   A 1 28  ? 18.653 2.649   14.979  0.66 18.33 ?  28  LYS   A H    1 
ATOM   784  H HA   A LYS   A 1 28  ? 20.572 3.115   17.388  0.34 27.10 ?  28  LYS   A HA   1 
ATOM   785  H HA   B LYS   A 1 28  ? 20.115 3.448   16.970  0.66 21.91 ?  28  LYS   A HA   1 
ATOM   786  H HB2  A LYS   A 1 28  ? 18.130 4.261   16.609  0.34 28.80 ?  28  LYS   A HB2  1 
ATOM   787  H HB2  B LYS   A 1 28  ? 17.616 4.340   16.061  0.66 25.47 ?  28  LYS   A HB2  1 
ATOM   788  H HB3  A LYS   A 1 28  ? 18.901 4.796   17.890  0.34 28.80 ?  28  LYS   A HB3  1 
ATOM   789  H HB3  B LYS   A 1 28  ? 18.265 4.980   17.361  0.66 25.47 ?  28  LYS   A HB3  1 
ATOM   790  H HG2  A LYS   A 1 28  ? 20.748 5.281   16.451  0.34 30.40 ?  28  LYS   A HG2  1 
ATOM   791  H HG2  B LYS   A 1 28  ? 20.152 5.517   15.951  0.66 29.35 ?  28  LYS   A HG2  1 
ATOM   792  H HG3  A LYS   A 1 28  ? 19.782 4.974   15.225  0.34 30.40 ?  28  LYS   A HG3  1 
ATOM   793  H HG3  B LYS   A 1 28  ? 19.186 5.201   14.729  0.66 29.35 ?  28  LYS   A HG3  1 
ATOM   794  H HD2  A LYS   A 1 28  ? 19.187 6.988   17.100  0.34 31.88 ?  28  LYS   A HD2  1 
ATOM   795  H HD2  B LYS   A 1 28  ? 18.358 7.090   16.615  0.66 33.42 ?  28  LYS   A HD2  1 
ATOM   796  H HD3  A LYS   A 1 28  ? 19.981 7.299   15.756  0.34 31.88 ?  28  LYS   A HD3  1 
ATOM   797  H HD3  B LYS   A 1 28  ? 19.388 7.538   15.488  0.66 33.42 ?  28  LYS   A HD3  1 
ATOM   798  H HE2  A LYS   A 1 28  ? 18.108 6.526   14.536  0.34 32.84 ?  28  LYS   A HE2  1 
ATOM   799  H HE2  B LYS   A 1 28  ? 17.806 6.805   13.867  0.66 36.19 ?  28  LYS   A HE2  1 
ATOM   800  H HE3  A LYS   A 1 28  ? 17.318 6.388   15.911  0.34 32.84 ?  28  LYS   A HE3  1 
ATOM   801  H HE3  B LYS   A 1 28  ? 16.766 6.610   15.057  0.66 36.19 ?  28  LYS   A HE3  1 
ATOM   802  H HZ1  A LYS   A 1 28  ? 16.831 8.372   14.909  0.34 33.59 ?  28  LYS   A HZ1  1 
ATOM   803  H HZ1  B LYS   A 1 28  ? 16.483 8.642   14.073  0.66 37.50 ?  28  LYS   A HZ1  1 
ATOM   804  H HZ2  A LYS   A 1 28  ? 17.504 8.643   16.162  0.34 33.59 ?  28  LYS   A HZ2  1 
ATOM   805  H HZ2  B LYS   A 1 28  ? 16.902 8.850   15.444  0.66 37.50 ?  28  LYS   A HZ2  1 
ATOM   806  H HZ3  A LYS   A 1 28  ? 18.224 8.769   14.911  0.34 33.59 ?  28  LYS   A HZ3  1 
ATOM   807  H HZ3  B LYS   A 1 28  ? 17.849 9.026   14.362  0.66 37.50 ?  28  LYS   A HZ3  1 
ATOM   808  N N    A LYS   A 1 29  ? 17.989 1.497   18.281  0.34 24.11 ?  29  LYS   A N    1 
ATOM   809  N N    B LYS   A 1 29  ? 17.577 1.765   17.899  0.66 19.33 ?  29  LYS   A N    1 
ATOM   810  C CA   A LYS   A 1 29  ? 17.380 0.801   19.409  0.34 25.09 ?  29  LYS   A CA   1 
ATOM   811  C CA   B LYS   A 1 29  ? 16.948 1.132   19.054  0.66 20.49 ?  29  LYS   A CA   1 
ATOM   812  C C    A LYS   A 1 29  ? 18.182 -0.437  19.798  0.34 23.74 ?  29  LYS   A C    1 
ATOM   813  C C    B LYS   A 1 29  ? 17.744 -0.079  19.525  0.66 19.16 ?  29  LYS   A C    1 
ATOM   814  O O    A LYS   A 1 29  ? 18.508 -0.633  20.974  0.34 24.20 ?  29  LYS   A O    1 
ATOM   815  O O    B LYS   A 1 29  ? 17.967 -0.253  20.728  0.66 20.52 ?  29  LYS   A O    1 
ATOM   816  C CB   A LYS   A 1 29  ? 15.943 0.411   19.057  0.34 27.27 ?  29  LYS   A CB   1 
ATOM   817  C CB   B LYS   A 1 29  ? 15.519 0.717   18.697  0.66 23.26 ?  29  LYS   A CB   1 
ATOM   818  C CG   A LYS   A 1 29  ? 15.195 -0.311  20.169  0.34 29.45 ?  29  LYS   A CG   1 
ATOM   819  C CG   B LYS   A 1 29  ? 14.788 -0.035  19.801  0.66 26.91 ?  29  LYS   A CG   1 
ATOM   820  C CD   A LYS   A 1 29  ? 14.848 0.628   21.312  0.34 31.42 ?  29  LYS   A CD   1 
ATOM   821  C CD   B LYS   A 1 29  ? 14.537 0.856   21.002  0.66 30.35 ?  29  LYS   A CD   1 
ATOM   822  C CE   A LYS   A 1 29  ? 13.975 -0.065  22.346  0.34 32.75 ?  29  LYS   A CE   1 
ATOM   823  C CE   B LYS   A 1 29  ? 13.789 0.114   22.097  0.66 32.75 ?  29  LYS   A CE   1 
ATOM   824  N NZ   A LYS   A 1 29  ? 13.500 0.877   23.398  0.34 33.60 ?  29  LYS   A NZ   1 
ATOM   825  N NZ   B LYS   A 1 29  ? 13.483 1.005   23.246  0.66 34.22 ?  29  LYS   A NZ   1 
ATOM   826  H H    A LYS   A 1 29  ? 17.610 1.351   17.522  0.34 29.08 ?  29  LYS   A H    1 
ATOM   827  H H    B LYS   A 1 29  ? 17.197 1.585   17.148  0.66 23.34 ?  29  LYS   A H    1 
ATOM   828  H HA   A LYS   A 1 29  ? 17.351 1.400   20.172  0.34 30.26 ?  29  LYS   A HA   1 
ATOM   829  H HA   B LYS   A 1 29  ? 16.902 1.769   19.785  0.66 24.74 ?  29  LYS   A HA   1 
ATOM   830  H HB2  A LYS   A 1 29  ? 15.445 1.217   18.844  0.34 32.88 ?  29  LYS   A HB2  1 
ATOM   831  H HB2  B LYS   A 1 29  ? 15.000 1.513   18.498  0.66 28.06 ?  29  LYS   A HB2  1 
ATOM   832  H HB3  A LYS   A 1 29  ? 15.961 -0.175  18.285  0.34 32.88 ?  29  LYS   A HB3  1 
ATOM   833  H HB3  B LYS   A 1 29  ? 15.544 0.140   17.919  0.66 28.06 ?  29  LYS   A HB3  1 
ATOM   834  H HG2  A LYS   A 1 29  ? 14.369 -0.669  19.812  0.34 35.49 ?  29  LYS   A HG2  1 
ATOM   835  H HG2  B LYS   A 1 29  ? 13.929 -0.336  19.466  0.66 32.44 ?  29  LYS   A HG2  1 
ATOM   836  H HG3  A LYS   A 1 29  ? 15.744 -1.030  20.522  0.34 35.49 ?  29  LYS   A HG3  1 
ATOM   837  H HG3  B LYS   A 1 29  ? 15.315 -0.798  20.090  0.66 32.44 ?  29  LYS   A HG3  1 
ATOM   838  H HD2  A LYS   A 1 29  ? 15.664 0.921   21.749  0.34 37.86 ?  29  LYS   A HD2  1 
ATOM   839  H HD2  B LYS   A 1 29  ? 15.385 1.155   21.364  0.66 36.57 ?  29  LYS   A HD2  1 
ATOM   840  H HD3  A LYS   A 1 29  ? 14.361 1.392   20.963  0.34 37.86 ?  29  LYS   A HD3  1 
ATOM   841  H HD3  B LYS   A 1 29  ? 14.001 1.617   20.729  0.66 36.57 ?  29  LYS   A HD3  1 
ATOM   842  H HE2  A LYS   A 1 29  ? 13.197 -0.442  21.905  0.34 39.46 ?  29  LYS   A HE2  1 
ATOM   843  H HE2  B LYS   A 1 29  ? 12.953 -0.224  21.740  0.66 39.45 ?  29  LYS   A HE2  1 
ATOM   844  H HE3  A LYS   A 1 29  ? 14.487 -0.767  22.777  0.34 39.46 ?  29  LYS   A HE3  1 
ATOM   845  H HE3  B LYS   A 1 29  ? 14.338 -0.620  22.417  0.66 39.45 ?  29  LYS   A HE3  1 
ATOM   846  H HZ1  A LYS   A 1 29  ? 12.993 0.444   23.987  0.34 40.47 ?  29  LYS   A HZ1  1 
ATOM   847  H HZ1  B LYS   A 1 29  ? 13.046 0.551   23.875  0.66 41.22 ?  29  LYS   A HZ1  1 
ATOM   848  H HZ2  A LYS   A 1 29  ? 14.196 1.234   23.823  0.34 40.47 ?  29  LYS   A HZ2  1 
ATOM   849  H HZ2  B LYS   A 1 29  ? 14.238 1.325   23.592  0.66 41.22 ?  29  LYS   A HZ2  1 
ATOM   850  H HZ3  A LYS   A 1 29  ? 13.021 1.530   23.028  0.34 40.47 ?  29  LYS   A HZ3  1 
ATOM   851  H HZ3  B LYS   A 1 29  ? 12.977 1.686   22.976  0.66 41.22 ?  29  LYS   A HZ3  1 
ATOM   852  N N    A VAL   A 1 30  ? 18.507 -1.282  18.820  0.34 22.17 ?  30  VAL   A N    1 
ATOM   853  N N    B VAL   A 1 30  ? 18.166 -0.929  18.591  0.66 17.68 ?  30  VAL   A N    1 
ATOM   854  C CA   A VAL   A 1 30  ? 19.158 -2.555  19.115  0.34 21.11 ?  30  VAL   A CA   1 
ATOM   855  C CA   B VAL   A 1 30  ? 18.803 -2.193  18.946  0.66 16.91 ?  30  VAL   A CA   1 
ATOM   856  C C    A VAL   A 1 30  ? 20.660 -2.384  19.320  0.34 19.85 ?  30  VAL   A C    1 
ATOM   857  C C    B VAL   A 1 30  ? 20.310 -2.049  19.171  0.66 16.14 ?  30  VAL   A C    1 
ATOM   858  O O    A VAL   A 1 30  ? 21.267 -3.103  20.122  0.34 19.89 ?  30  VAL   A O    1 
ATOM   859  O O    B VAL   A 1 30  ? 20.879 -2.754  20.010  0.66 16.93 ?  30  VAL   A O    1 
ATOM   860  C CB   A VAL   A 1 30  ? 18.857 -3.559  17.988  0.34 21.29 ?  30  VAL   A CB   1 
ATOM   861  C CB   B VAL   A 1 30  ? 18.496 -3.238  17.856  0.66 17.49 ?  30  VAL   A CB   1 
ATOM   862  C CG1  A VAL   A 1 30  ? 19.619 -4.860  18.206  0.34 21.38 ?  30  VAL   A CG1  1 
ATOM   863  C CG1  B VAL   A 1 30  ? 19.242 -4.536  18.123  0.66 18.16 ?  30  VAL   A CG1  1 
ATOM   864  C CG2  A VAL   A 1 30  ? 17.362 -3.816  17.894  0.34 21.55 ?  30  VAL   A CG2  1 
ATOM   865  C CG2  B VAL   A 1 30  ? 16.992 -3.488  17.761  0.66 18.15 ?  30  VAL   A CG2  1 
ATOM   866  H H    A VAL   A 1 30  ? 18.361 -1.140  17.986  0.34 26.75 ?  30  VAL   A H    1 
ATOM   867  H H    B VAL   A 1 30  ? 18.087 -0.796  17.740  0.66 21.37 ?  30  VAL   A H    1 
ATOM   868  H HA   A VAL   A 1 30  ? 18.777 -2.910  19.934  0.34 25.48 ?  30  VAL   A HA   1 
ATOM   869  H HA   B VAL   A 1 30  ? 18.398 -2.511  19.769  0.66 20.44 ?  30  VAL   A HA   1 
ATOM   870  H HB   A VAL   A 1 30  ? 19.151 -3.180  17.144  0.34 25.70 ?  30  VAL   A HB   1 
ATOM   871  H HB   B VAL   A 1 30  ? 18.791 -2.895  16.998  0.66 21.14 ?  30  VAL   A HB   1 
ATOM   872  H HG11 A VAL   A 1 30  ? 19.254 -5.539  17.617  0.34 25.80 ?  30  VAL   A HG11 1 
ATOM   873  H HG11 B VAL   A 1 30  ? 18.812 -5.256  17.633  0.66 21.95 ?  30  VAL   A HG11 1 
ATOM   874  H HG12 A VAL   A 1 30  ? 20.557 -4.719  18.004  0.34 25.80 ?  30  VAL   A HG12 1 
ATOM   875  H HG12 B VAL   A 1 30  ? 20.160 -4.439  17.829  0.66 21.95 ?  30  VAL   A HG12 1 
ATOM   876  H HG13 A VAL   A 1 30  ? 19.515 -5.135  19.130  0.34 25.80 ?  30  VAL   A HG13 1 
ATOM   877  H HG13 B VAL   A 1 30  ? 19.215 -4.723  19.073  0.66 21.95 ?  30  VAL   A HG13 1 
ATOM   878  H HG21 A VAL   A 1 30  ? 17.201 -4.487  17.214  0.34 26.02 ?  30  VAL   A HG21 1 
ATOM   879  H HG21 B VAL   A 1 30  ? 16.827 -4.178  17.098  0.66 21.93 ?  30  VAL   A HG21 1 
ATOM   880  H HG22 A VAL   A 1 30  ? 17.043 -4.130  18.754  0.34 26.02 ?  30  VAL   A HG22 1 
ATOM   881  H HG22 B VAL   A 1 30  ? 16.665 -3.779  18.627  0.66 21.93 ?  30  VAL   A HG22 1 
ATOM   882  H HG23 A VAL   A 1 30  ? 16.914 -2.989  17.656  0.34 26.02 ?  30  VAL   A HG23 1 
ATOM   883  H HG23 B VAL   A 1 30  ? 16.549 -2.666  17.499  0.66 21.93 ?  30  VAL   A HG23 1 
ATOM   884  N N    A LYS   A 1 31  ? 21.279 -1.447  18.612  0.34 18.97 ?  31  LYS   A N    1 
ATOM   885  N N    B LYS   A 1 31  ? 20.964 -1.144  18.450  0.66 15.76 ?  31  LYS   A N    1 
ATOM   886  C CA   A LYS   A 1 31  ? 22.731 -1.326  18.550  0.34 19.15 ?  31  LYS   A CA   1 
ATOM   887  C CA   B LYS   A 1 31  ? 22.418 -1.038  18.432  0.66 16.39 ?  31  LYS   A CA   1 
ATOM   888  C C    A LYS   A 1 31  ? 23.366 -2.677  18.205  0.34 16.74 ?  31  LYS   A C    1 
ATOM   889  C C    B LYS   A 1 31  ? 23.057 -2.410  18.191  0.66 14.73 ?  31  LYS   A C    1 
ATOM   890  O O    A LYS   A 1 31  ? 24.160 -3.214  18.984  0.34 16.29 ?  31  LYS   A O    1 
ATOM   891  O O    B LYS   A 1 31  ? 23.822 -2.905  19.025  0.66 15.88 ?  31  LYS   A O    1 
ATOM   892  C CB   A LYS   A 1 31  ? 23.315 -0.763  19.838  0.34 22.15 ?  31  LYS   A CB   1 
ATOM   893  C CB   B LYS   A 1 31  ? 22.957 -0.391  19.701  0.66 20.06 ?  31  LYS   A CB   1 
ATOM   894  C CG   A LYS   A 1 31  ? 22.628 0.493   20.346  0.34 25.13 ?  31  LYS   A CG   1 
ATOM   895  C CG   B LYS   A 1 31  ? 22.226 0.883   20.105  0.66 25.09 ?  31  LYS   A CG   1 
ATOM   896  C CD   A LYS   A 1 31  ? 23.641 1.508   20.848  0.34 27.54 ?  31  LYS   A CD   1 
ATOM   897  C CD   B LYS   A 1 31  ? 23.192 1.957   20.582  0.66 29.13 ?  31  LYS   A CD   1 
ATOM   898  C CE   A LYS   A 1 31  ? 22.987 2.565   21.721  0.34 29.17 ?  31  LYS   A CE   1 
ATOM   899  C CE   B LYS   A 1 31  ? 22.481 3.028   21.393  0.66 32.09 ?  31  LYS   A CE   1 
ATOM   900  N NZ   A LYS   A 1 31  ? 21.832 3.223   21.050  0.34 29.98 ?  31  LYS   A NZ   1 
ATOM   901  N NZ   B LYS   A 1 31  ? 21.221 3.494   20.751  0.66 33.74 ?  31  LYS   A NZ   1 
ATOM   902  H H    A LYS   A 1 31  ? 20.865 -0.861  18.146  0.34 22.91 ?  31  LYS   A H    1 
ATOM   903  H H    B LYS   A 1 31  ? 20.562 -0.552  17.960  0.66 19.06 ?  31  LYS   A H    1 
ATOM   904  H HA   A LYS   A 1 31  ? 22.946 -0.709  17.843  0.34 23.13 ?  31  LYS   A HA   1 
ATOM   905  H HA   B LYS   A 1 31  ? 22.655 -0.462  17.694  0.66 19.82 ?  31  LYS   A HA   1 
ATOM   906  H HB2  A LYS   A 1 31  ? 23.251 -1.438  20.527  0.34 26.73 ?  31  LYS   A HB2  1 
ATOM   907  H HB2  B LYS   A 1 31  ? 22.880 -1.017  20.433  0.66 24.22 ?  31  LYS   A HB2  1 
ATOM   908  H HB3  A LYS   A 1 31  ? 24.248 -0.542  19.683  0.34 26.73 ?  31  LYS   A HB3  1 
ATOM   909  H HB3  B LYS   A 1 31  ? 23.887 -0.160  19.556  0.66 24.22 ?  31  LYS   A HB3  1 
ATOM   910  H HG2  A LYS   A 1 31  ? 22.123 0.898   19.624  0.34 30.30 ?  31  LYS   A HG2  1 
ATOM   911  H HG2  B LYS   A 1 31  ? 21.739 1.234   19.343  0.66 30.26 ?  31  LYS   A HG2  1 
ATOM   912  H HG3  A LYS   A 1 31  ? 22.039 0.263   21.082  0.34 30.30 ?  31  LYS   A HG3  1 
ATOM   913  H HG3  B LYS   A 1 31  ? 21.613 0.686   20.832  0.66 30.26 ?  31  LYS   A HG3  1 
ATOM   914  H HD2  A LYS   A 1 31  ? 24.315 1.053   21.375  0.34 33.20 ?  31  LYS   A HD2  1 
ATOM   915  H HD2  B LYS   A 1 31  ? 23.871 1.550   21.143  0.66 35.10 ?  31  LYS   A HD2  1 
ATOM   916  H HD3  A LYS   A 1 31  ? 24.050 1.952   20.088  0.34 33.20 ?  31  LYS   A HD3  1 
ATOM   917  H HD3  B LYS   A 1 31  ? 23.604 2.382   19.813  0.66 35.10 ?  31  LYS   A HD3  1 
ATOM   918  H HE2  A LYS   A 1 31  ? 22.665 2.148   22.535  0.34 35.16 ?  31  LYS   A HE2  1 
ATOM   919  H HE2  B LYS   A 1 31  ? 22.263 2.668   22.265  0.66 38.66 ?  31  LYS   A HE2  1 
ATOM   920  H HE3  A LYS   A 1 31  ? 23.641 3.249   21.932  0.34 35.16 ?  31  LYS   A HE3  1 
ATOM   921  H HE3  B LYS   A 1 31  ? 23.069 3.792   21.489  0.66 38.66 ?  31  LYS   A HE3  1 
ATOM   922  H HZ1  A LYS   A 1 31  ? 21.496 3.857   21.577  0.34 36.13 ?  31  LYS   A HZ1  1 
ATOM   923  H HZ1  B LYS   A 1 31  ? 20.873 4.167   21.218  0.66 40.64 ?  31  LYS   A HZ1  1 
ATOM   924  H HZ2  A LYS   A 1 31  ? 22.095 3.593   20.285  0.34 36.13 ?  31  LYS   A HZ2  1 
ATOM   925  H HZ2  B LYS   A 1 31  ? 21.388 3.773   19.923  0.66 40.64 ?  31  LYS   A HZ2  1 
ATOM   926  H HZ3  A LYS   A 1 31  ? 21.197 2.623   20.878  0.34 36.13 ?  31  LYS   A HZ3  1 
ATOM   927  H HZ3  B LYS   A 1 31  ? 20.630 2.829   20.718  0.66 40.64 ?  31  LYS   A HZ3  1 
ATOM   928  N N    A PRO   A 1 32  ? 23.041 -3.243  17.046  0.34 15.69 ?  32  PRO   A N    1 
ATOM   929  N N    B PRO   A 1 32  ? 22.771 -3.032  17.051  0.66 13.95 ?  32  PRO   A N    1 
ATOM   930  C CA   A PRO   A 1 32  ? 23.519 -4.589  16.718  0.34 15.39 ?  32  PRO   A CA   1 
ATOM   931  C CA   B PRO   A 1 32  ? 23.268 -4.384  16.790  0.66 14.19 ?  32  PRO   A CA   1 
ATOM   932  C C    A PRO   A 1 32  ? 25.022 -4.608  16.491  0.34 14.77 ?  32  PRO   A C    1 
ATOM   933  C C    B PRO   A 1 32  ? 24.776 -4.395  16.594  0.66 14.24 ?  32  PRO   A C    1 
ATOM   934  O O    A PRO   A 1 32  ? 25.675 -3.580  16.299  0.34 14.26 ?  32  PRO   A O    1 
ATOM   935  O O    B PRO   A 1 32  ? 25.424 -3.370  16.376  0.66 15.00 ?  32  PRO   A O    1 
ATOM   936  C CB   A PRO   A 1 32  ? 22.775 -4.909  15.421  0.34 15.90 ?  32  PRO   A CB   1 
ATOM   937  C CB   B PRO   A 1 32  ? 22.557 -4.753  15.488  0.66 15.07 ?  32  PRO   A CB   1 
ATOM   938  C CG   A PRO   A 1 32  ? 22.595 -3.576  14.775  0.34 15.86 ?  32  PRO   A CG   1 
ATOM   939  C CG   B PRO   A 1 32  ? 22.398 -3.440  14.783  0.66 14.90 ?  32  PRO   A CG   1 
ATOM   940  C CD   A PRO   A 1 32  ? 22.321 -2.627  15.916  0.34 15.58 ?  32  PRO   A CD   1 
ATOM   941  C CD   B PRO   A 1 32  ? 22.064 -2.470  15.883  0.66 14.01 ?  32  PRO   A CD   1 
ATOM   942  H HA   A PRO   A 1 32  ? 23.266 -5.223  17.410  0.34 18.62 ?  32  PRO   A HA   1 
ATOM   943  H HA   B PRO   A 1 32  ? 23.003 -4.992  17.499  0.66 17.18 ?  32  PRO   A HA   1 
ATOM   944  H HB2  A PRO   A 1 32  ? 23.317 -5.494  14.869  0.34 19.23 ?  32  PRO   A HB2  1 
ATOM   945  H HB2  B PRO   A 1 32  ? 23.110 -5.358  14.973  0.66 18.24 ?  32  PRO   A HB2  1 
ATOM   946  H HB3  A PRO   A 1 32  ? 21.918 -5.318  15.621  0.34 19.23 ?  32  PRO   A HB3  1 
ATOM   947  H HB3  B PRO   A 1 32  ? 21.690 -5.149  15.678  0.66 18.24 ?  32  PRO   A HB3  1 
ATOM   948  H HG2  A PRO   A 1 32  ? 23.409 -3.328  14.308  0.34 19.18 ?  32  PRO   A HG2  1 
ATOM   949  H HG2  B PRO   A 1 32  ? 23.230 -3.198  14.349  0.66 18.04 ?  32  PRO   A HG2  1 
ATOM   950  H HG3  A PRO   A 1 32  ? 21.844 -3.608  14.162  0.34 19.18 ?  32  PRO   A HG3  1 
ATOM   951  H HG3  B PRO   A 1 32  ? 21.675 -3.499  14.137  0.66 18.04 ?  32  PRO   A HG3  1 
ATOM   952  H HD2  A PRO   A 1 32  ? 22.684 -1.750  15.715  0.34 18.84 ?  32  PRO   A HD2  1 
ATOM   953  H HD2  B PRO   A 1 32  ? 22.406 -1.587  15.663  0.66 16.97 ?  32  PRO   A HD2  1 
ATOM   954  H HD3  A PRO   A 1 32  ? 21.368 -2.587  16.095  0.34 18.84 ?  32  PRO   A HD3  1 
ATOM   955  H HD3  B PRO   A 1 32  ? 21.102 -2.448  16.029  0.66 16.97 ?  32  PRO   A HD3  1 
ATOM   956  N N    A THR   A 1 33  ? 25.573 -5.823  16.493  0.34 14.59 ?  33  THR   A N    1 
ATOM   957  N N    B THR   A 1 33  ? 25.328 -5.604  16.635  0.66 14.33 ?  33  THR   A N    1 
ATOM   958  C CA   A THR   A 1 33  ? 26.985 -5.980  16.168  0.34 14.50 ?  33  THR   A CA   1 
ATOM   959  C CA   B THR   A 1 33  ? 26.745 -5.773  16.343  0.66 14.67 ?  33  THR   A CA   1 
ATOM   960  C C    A THR   A 1 33  ? 27.275 -5.550  14.733  0.34 13.33 ?  33  THR   A C    1 
ATOM   961  C C    B THR   A 1 33  ? 27.070 -5.332  14.921  0.66 13.34 ?  33  THR   A C    1 
ATOM   962  O O    A THR   A 1 33  ? 28.347 -4.998  14.456  0.34 13.12 ?  33  THR   A O    1 
ATOM   963  O O    B THR   A 1 33  ? 28.083 -4.659  14.689  0.66 12.92 ?  33  THR   A O    1 
ATOM   964  C CB   A THR   A 1 33  ? 27.415 -7.433  16.394  0.34 15.86 ?  33  THR   A CB   1 
ATOM   965  C CB   B THR   A 1 33  ? 27.137 -7.234  16.556  0.66 16.49 ?  33  THR   A CB   1 
ATOM   966  O OG1  A THR   A 1 33  ? 27.183 -7.802  17.759  0.34 16.54 ?  33  THR   A OG1  1 
ATOM   967  O OG1  B THR   A 1 33  ? 26.801 -7.627  17.891  0.66 18.19 ?  33  THR   A OG1  1 
ATOM   968  C CG2  A THR   A 1 33  ? 28.894 -7.621  16.081  0.34 16.24 ?  33  THR   A CG2  1 
ATOM   969  C CG2  B THR   A 1 33  ? 28.628 -7.432  16.330  0.66 17.23 ?  33  THR   A CG2  1 
ATOM   970  H H    A THR   A 1 33  ? 25.154 -6.553  16.674  0.34 17.66 ?  33  THR   A H    1 
ATOM   971  H H    B THR   A 1 33  ? 24.905 -6.325  16.822  0.66 17.34 ?  33  THR   A H    1 
ATOM   972  H HA   A THR   A 1 33  ? 27.505 -5.421  16.769  0.34 17.55 ?  33  THR   A HA   1 
ATOM   973  H HA   B THR   A 1 33  ? 27.260 -5.223  16.953  0.66 17.75 ?  33  THR   A HA   1 
ATOM   974  H HB   A THR   A 1 33  ? 26.899 -8.017  15.815  0.34 19.18 ?  33  THR   A HB   1 
ATOM   975  H HB   B THR   A 1 33  ? 26.653 -7.791  15.925  0.66 19.94 ?  33  THR   A HB   1 
ATOM   976  H HG1  A THR   A 1 33  ? 27.622 -7.301  18.273  0.34 20.00 ?  33  THR   A HG1  1 
ATOM   977  H HG1  B THR   A 1 33  ? 27.215 -7.145  18.444  0.66 21.98 ?  33  THR   A HG1  1 
ATOM   978  H HG21 A THR   A 1 33  ? 29.186 -8.496  16.386  0.34 19.64 ?  33  THR   A HG21 1 
ATOM   979  H HG21 B THR   A 1 33  ? 28.889 -8.319  16.618  0.66 20.83 ?  33  THR   A HG21 1 
ATOM   980  H HG22 A THR   A 1 33  ? 29.044 -7.554  15.127  0.34 19.64 ?  33  THR   A HG22 1 
ATOM   981  H HG22 B THR   A 1 33  ? 28.839 -7.332  15.388  0.66 20.83 ?  33  THR   A HG22 1 
ATOM   982  H HG23 A THR   A 1 33  ? 29.416 -6.941  16.535  0.34 19.64 ?  33  THR   A HG23 1 
ATOM   983  H HG23 B THR   A 1 33  ? 29.129 -6.775  16.837  0.66 20.83 ?  33  THR   A HG23 1 
ATOM   984  N N    A VAL   A 1 34  ? 26.336 -5.787  13.814  0.34 12.40 ?  34  VAL   A N    1 
ATOM   985  N N    B VAL   A 1 34  ? 26.226 -5.704  13.957  0.66 12.79 ?  34  VAL   A N    1 
ATOM   986  C CA   A VAL   A 1 34  ? 26.523 -5.460  12.403  0.34 11.78 ?  34  VAL   A CA   1 
ATOM   987  C CA   B VAL   A 1 34  ? 26.447 -5.388  12.551  0.66 12.11 ?  34  VAL   A CA   1 
ATOM   988  C C    A VAL   A 1 34  ? 25.218 -4.921  11.829  0.34 11.26 ?  34  VAL   A C    1 
ATOM   989  C C    B VAL   A 1 34  ? 25.158 -4.854  11.949  0.66 11.42 ?  34  VAL   A C    1 
ATOM   990  O O    A VAL   A 1 34  ? 24.205 -5.629  11.816  0.34 10.95 ?  34  VAL   A O    1 
ATOM   991  O O    B VAL   A 1 34  ? 24.109 -5.502  12.036  0.66 12.43 ?  34  VAL   A O    1 
ATOM   992  C CB   A VAL   A 1 34  ? 26.981 -6.677  11.577  0.34 11.87 ?  34  VAL   A CB   1 
ATOM   993  C CB   B VAL   A 1 34  ? 26.932 -6.609  11.744  0.66 13.00 ?  34  VAL   A CB   1 
ATOM   994  C CG1  A VAL   A 1 34  ? 27.139 -6.289  10.117  0.34 12.46 ?  34  VAL   A CG1  1 
ATOM   995  C CG1  B VAL   A 1 34  ? 27.168 -6.217  10.289  0.66 13.23 ?  34  VAL   A CG1  1 
ATOM   996  C CG2  A VAL   A 1 34  ? 28.276 -7.270  12.130  0.34 12.47 ?  34  VAL   A CG2  1 
ATOM   997  C CG2  B VAL   A 1 34  ? 28.190 -7.212  12.363  0.66 14.40 ?  34  VAL   A CG2  1 
ATOM   998  H H    A VAL   A 1 34  ? 25.575 -6.150  13.995  0.34 15.03 ?  34  VAL   A H    1 
ATOM   999  H H    B VAL   A 1 34  ? 25.503 -6.153  14.100  0.66 15.50 ?  34  VAL   A H    1 
ATOM   1000 H HA   A VAL   A 1 34  ? 27.197 -4.769  12.330  0.34 14.28 ?  34  VAL   A HA   1 
ATOM   1001 H HA   B VAL   A 1 34  ? 27.116 -4.693  12.482  0.66 14.69 ?  34  VAL   A HA   1 
ATOM   1002 H HB   A VAL   A 1 34  ? 26.296 -7.362  11.635  0.34 14.40 ?  34  VAL   A HB   1 
ATOM   1003 H HB   B VAL   A 1 34  ? 26.241 -7.288  11.759  0.66 15.76 ?  34  VAL   A HB   1 
ATOM   1004 H HG11 A VAL   A 1 34  ? 27.644 -6.980  9.665   0.34 15.10 ?  34  VAL   A HG11 1 
ATOM   1005 H HG11 B VAL   A 1 34  ? 27.671 -6.923  9.851   0.66 16.03 ?  34  VAL   A HG11 1 
ATOM   1006 H HG12 A VAL   A 1 34  ? 26.262 -6.202  9.716   0.34 15.10 ?  34  VAL   A HG12 1 
ATOM   1007 H HG12 B VAL   A 1 34  ? 26.315 -6.098  9.846   0.66 16.03 ?  34  VAL   A HG12 1 
ATOM   1008 H HG13 A VAL   A 1 34  ? 27.615 -5.444  10.067  0.34 15.10 ?  34  VAL   A HG13 1 
ATOM   1009 H HG13 B VAL   A 1 34  ? 27.676 -5.390  10.262  0.66 16.03 ?  34  VAL   A HG13 1 
ATOM   1010 H HG21 A VAL   A 1 34  ? 28.562 -7.994  11.549  0.34 15.11 ?  34  VAL   A HG21 1 
ATOM   1011 H HG21 B VAL   A 1 34  ? 28.501 -7.938  11.800  0.66 17.43 ?  34  VAL   A HG21 1 
ATOM   1012 H HG22 A VAL   A 1 34  ? 28.956 -6.579  12.155  0.34 15.11 ?  34  VAL   A HG22 1 
ATOM   1013 H HG22 B VAL   A 1 34  ? 28.872 -6.525  12.425  0.66 17.43 ?  34  VAL   A HG22 1 
ATOM   1014 H HG23 A VAL   A 1 34  ? 28.116 -7.609  13.025  0.34 15.11 ?  34  VAL   A HG23 1 
ATOM   1015 H HG23 B VAL   A 1 34  ? 27.977 -7.547  13.248  0.66 17.43 ?  34  VAL   A HG23 1 
ATOM   1016 N N    . VAL   A 1 35  ? 25.250 -3.685  11.321  1.00 11.33 ?  35  VAL   A N    1 
ATOM   1017 C CA   . VAL   A 1 35  ? 24.214 -3.172  10.436  1.00 10.94 ?  35  VAL   A CA   1 
ATOM   1018 C C    . VAL   A 1 35  ? 24.777 -3.182  9.021   1.00 10.22 ?  35  VAL   A C    1 
ATOM   1019 O O    . VAL   A 1 35  ? 25.925 -2.778  8.793   1.00 11.26 ?  35  VAL   A O    1 
ATOM   1020 C CB   . VAL   A 1 35  ? 23.680 -1.777  10.840  1.00 11.48 ?  35  VAL   A CB   1 
ATOM   1021 C CG1  . VAL   A 1 35  ? 24.740 -0.681  10.722  1.00 12.12 ?  35  VAL   A CG1  1 
ATOM   1022 C CG2  . VAL   A 1 35  ? 22.449 -1.422  10.002  1.00 12.25 ?  35  VAL   A CG2  1 
ATOM   1023 H H    A VAL   A 1 35  ? 25.880 -3.121  11.472  0.34 13.74 ?  35  VAL   A H    1 
ATOM   1024 H H    B VAL   A 1 35  ? 25.924 -3.159  11.396  0.66 13.74 ?  35  VAL   A H    1 
ATOM   1025 H HA   . VAL   A 1 35  ? 23.461 -3.782  10.454  1.00 13.28 ?  35  VAL   A HA   1 
ATOM   1026 H HB   . VAL   A 1 35  ? 23.398 -1.808  11.765  1.00 13.93 ?  35  VAL   A HB   1 
ATOM   1027 H HG11 . VAL   A 1 35  ? 24.382 0.150   11.078  1.00 14.69 ?  35  VAL   A HG11 1 
ATOM   1028 H HG12 . VAL   A 1 35  ? 25.526 -0.943  11.226  1.00 14.69 ?  35  VAL   A HG12 1 
ATOM   1029 H HG13 . VAL   A 1 35  ? 24.975 -0.560  9.786   1.00 14.69 ?  35  VAL   A HG13 1 
ATOM   1030 H HG21 . VAL   A 1 35  ? 22.091 -0.574  10.304  1.00 14.85 ?  35  VAL   A HG21 1 
ATOM   1031 H HG22 . VAL   A 1 35  ? 22.710 -1.353  9.066   1.00 14.85 ?  35  VAL   A HG22 1 
ATOM   1032 H HG23 . VAL   A 1 35  ? 21.784 -2.120  10.106  1.00 14.85 ?  35  VAL   A HG23 1 
ATOM   1033 N N    . VAL   A 1 36  ? 23.972 -3.644  8.073   1.00 9.92  ?  36  VAL   A N    1 
ATOM   1034 C CA   . VAL   A 1 36  ? 24.357 -3.663  6.671   1.00 9.77  ?  36  VAL   A CA   1 
ATOM   1035 C C    . VAL   A 1 36  ? 23.896 -2.383  5.989   1.00 9.93  ?  36  VAL   A C    1 
ATOM   1036 O O    . VAL   A 1 36  ? 22.730 -1.982  6.119   1.00 10.78 ?  36  VAL   A O    1 
ATOM   1037 C CB   . VAL   A 1 36  ? 23.769 -4.891  5.961   1.00 10.03 ?  36  VAL   A CB   1 
ATOM   1038 C CG1  . VAL   A 1 36  ? 24.039 -4.827  4.477   1.00 10.56 ?  36  VAL   A CG1  1 
ATOM   1039 C CG2  . VAL   A 1 36  ? 24.313 -6.169  6.561   1.00 10.61 ?  36  VAL   A CG2  1 
ATOM   1040 H H    . VAL   A 1 36  ? 23.178 -3.945  8.225   1.00 12.06 ?  36  VAL   A H    1 
ATOM   1041 H HA   . VAL   A 1 36  ? 25.328 -3.713  6.612   1.00 11.88 ?  36  VAL   A HA   1 
ATOM   1042 H HB   . VAL   A 1 36  ? 22.807 -4.886  6.092   1.00 12.19 ?  36  VAL   A HB   1 
ATOM   1043 H HG11 . VAL   A 1 36  ? 23.911 -5.713  4.099   1.00 12.82 ?  36  VAL   A HG11 1 
ATOM   1044 H HG12 . VAL   A 1 36  ? 23.423 -4.203  4.065   1.00 12.82 ?  36  VAL   A HG12 1 
ATOM   1045 H HG13 . VAL   A 1 36  ? 24.954 -4.540  4.334   1.00 12.82 ?  36  VAL   A HG13 1 
ATOM   1046 H HG21 . VAL   A 1 36  ? 23.926 -6.926  6.089   1.00 12.88 ?  36  VAL   A HG21 1 
ATOM   1047 H HG22 . VAL   A 1 36  ? 25.275 -6.178  6.472   1.00 12.88 ?  36  VAL   A HG22 1 
ATOM   1048 H HG23 . VAL   A 1 36  ? 24.064 -6.211  7.501   1.00 12.88 ?  36  VAL   A HG23 1 
ATOM   1049 N N    A ASN   A 1 37  ? 24.817 -1.733  5.286   0.34 9.64  ?  37  ASN   A N    1 
ATOM   1050 N N    B ASN   A 1 37  ? 24.805 -1.754  5.237   0.66 9.18  ?  37  ASN   A N    1 
ATOM   1051 C CA   A ASN   A 1 37  ? 24.493 -0.589  4.455   0.34 9.62  ?  37  ASN   A CA   1 
ATOM   1052 C CA   B ASN   A 1 37  ? 24.461 -0.664  4.335   0.66 9.12  ?  37  ASN   A CA   1 
ATOM   1053 C C    A ASN   A 1 37  ? 24.326 -1.040  3.014   0.34 9.31  ?  37  ASN   A C    1 
ATOM   1054 C C    B ASN   A 1 37  ? 24.372 -1.178  2.903   0.66 8.91  ?  37  ASN   A C    1 
ATOM   1055 O O    A ASN   A 1 37  ? 25.093 -1.875  2.522   0.34 9.54  ?  37  ASN   A O    1 
ATOM   1056 O O    B ASN   A 1 37  ? 25.206 -1.980  2.464   0.66 9.96  ?  37  ASN   A O    1 
ATOM   1057 C CB   A ASN   A 1 37  ? 25.601 0.458   4.520   0.34 9.61  ?  37  ASN   A CB   1 
ATOM   1058 C CB   B ASN   A 1 37  ? 25.508 0.449   4.415   0.66 9.28  ?  37  ASN   A CB   1 
ATOM   1059 C CG   A ASN   A 1 37  ? 25.242 1.706   3.772   0.34 9.18  ?  37  ASN   A CG   1 
ATOM   1060 C CG   B ASN   A 1 37  ? 25.193 1.613   3.493   0.66 9.29  ?  37  ASN   A CG   1 
ATOM   1061 O OD1  A ASN   A 1 37  ? 24.061 2.042   3.659   0.34 9.13  ?  37  ASN   A OD1  1 
ATOM   1062 O OD1  B ASN   A 1 37  ? 24.020 1.907   3.224   0.66 9.32  ?  37  ASN   A OD1  1 
ATOM   1063 N ND2  A ASN   A 1 37  ? 26.245 2.401   3.249   0.34 9.37  ?  37  ASN   A ND2  1 
ATOM   1064 N ND2  B ASN   A 1 37  ? 26.232 2.271   2.998   0.66 9.48  ?  37  ASN   A ND2  1 
ATOM   1065 H H    A ASN   A 1 37  ? 25.653 -1.945  5.277   0.34 11.72 ?  37  ASN   A H    1 
ATOM   1066 H H    B ASN   A 1 37  ? 25.645 -1.954  5.239   0.66 11.16 ?  37  ASN   A H    1 
ATOM   1067 H HA   A ASN   A 1 37  ? 23.666 -0.187  4.756   0.34 11.70 ?  37  ASN   A HA   1 
ATOM   1068 H HA   B ASN   A 1 37  ? 23.603 -0.298  4.590   0.66 11.10 ?  37  ASN   A HA   1 
ATOM   1069 H HB2  A ASN   A 1 37  ? 25.750 0.702   5.444   0.34 11.69 ?  37  ASN   A HB2  1 
ATOM   1070 H HB2  B ASN   A 1 37  ? 25.548 0.782   5.327   0.66 11.29 ?  37  ASN   A HB2  1 
ATOM   1071 H HB3  A ASN   A 1 37  ? 26.416 0.091   4.134   0.34 11.69 ?  37  ASN   A HB3  1 
ATOM   1072 H HB3  B ASN   A 1 37  ? 26.374 0.086   4.160   0.66 11.29 ?  37  ASN   A HB3  1 
ATOM   1073 H HD21 A ASN   A 1 37  ? 26.088 3.122   2.809   0.34 11.40 ?  37  ASN   A HD21 1 
ATOM   1074 H HD21 B ASN   A 1 37  ? 26.103 2.932   2.471   0.66 11.53 ?  37  ASN   A HD21 1 
ATOM   1075 H HD22 A ASN   A 1 37  ? 27.053 2.136   3.349   0.34 11.40 ?  37  ASN   A HD22 1 
ATOM   1076 H HD22 B ASN   A 1 37  ? 27.026 2.032   3.205   0.66 11.53 ?  37  ASN   A HD22 1 
ATOM   1077 N N    A ALA   A 1 38  ? 23.317 -0.487  2.343   0.34 9.60  ?  38  ALA   A N    1 
ATOM   1078 N N    B ALA   A 1 38  ? 23.344 -0.718  2.184   0.66 9.22  ?  38  ALA   A N    1 
ATOM   1079 C CA   A ALA   A 1 38  ? 23.127 -0.679  0.906   0.34 9.26  ?  38  ALA   A CA   1 
ATOM   1080 C CA   B ALA   A 1 38  ? 23.208 -0.957  0.747   0.66 10.10 ?  38  ALA   A CA   1 
ATOM   1081 C C    A ALA   A 1 38  ? 24.035 0.311   0.183   0.34 9.38  ?  38  ALA   A C    1 
ATOM   1082 C C    B ALA   A 1 38  ? 24.004 0.118   0.011   0.66 10.26 ?  38  ALA   A C    1 
ATOM   1083 O O    A ALA   A 1 38  ? 23.634 1.425   -0.154  0.34 9.11  ?  38  ALA   A O    1 
ATOM   1084 O O    B ALA   A 1 38  ? 23.485 1.161   -0.400  0.66 10.41 ?  38  ALA   A O    1 
ATOM   1085 C CB   A ALA   A 1 38  ? 21.662 -0.481  0.532   0.34 9.25  ?  38  ALA   A CB   1 
ATOM   1086 C CB   B ALA   A 1 38  ? 21.740 -0.957  0.338   0.66 10.59 ?  38  ALA   A CB   1 
ATOM   1087 H H    A ALA   A 1 38  ? 22.717 0.013   2.706   0.34 11.68 ?  38  ALA   A H    1 
ATOM   1088 H H    B ALA   A 1 38  ? 22.709 -0.248  2.522   0.66 11.22 ?  38  ALA   A H    1 
ATOM   1089 H HA   A ALA   A 1 38  ? 23.392 -1.570  0.654   0.34 11.27 ?  38  ALA   A HA   1 
ATOM   1090 H HA   B ALA   A 1 38  ? 23.587 -1.824  0.535   0.66 12.28 ?  38  ALA   A HA   1 
ATOM   1091 H HB1  A ALA   A 1 38  ? 21.550 -0.639  -0.418  0.34 11.26 ?  38  ALA   A HB1  1 
ATOM   1092 H HB1  B ALA   A 1 38  ? 21.684 -1.121  -0.619  0.66 12.86 ?  38  ALA   A HB1  1 
ATOM   1093 H HB2  A ALA   A 1 38  ? 21.120 -1.109  1.037   0.34 11.26 ?  38  ALA   A HB2  1 
ATOM   1094 H HB2  B ALA   A 1 38  ? 21.274 -1.658  0.819   0.66 12.86 ?  38  ALA   A HB2  1 
ATOM   1095 H HB3  A ALA   A 1 38  ? 21.396 0.428   0.747   0.34 11.26 ?  38  ALA   A HB3  1 
ATOM   1096 H HB3  B ALA   A 1 38  ? 21.352 -0.095  0.548   0.66 12.86 ?  38  ALA   A HB3  1 
ATOM   1097 N N    A ALA   A 1 39  ? 25.280 -0.102  -0.052  0.34 9.61  ?  39  ALA   A N    1 
ATOM   1098 N N    B ALA   A 1 39  ? 25.301 -0.144  -0.143  0.66 11.05 ?  39  ALA   A N    1 
ATOM   1099 C CA   A ALA   A 1 39  ? 26.355 0.773   -0.501  0.34 8.92  ?  39  ALA   A CA   1 
ATOM   1100 C CA   B ALA   A 1 39  ? 26.242 0.846   -0.634  0.66 10.43 ?  39  ALA   A CA   1 
ATOM   1101 C C    A ALA   A 1 39  ? 26.554 0.713   -2.012  0.34 9.52  ?  39  ALA   A C    1 
ATOM   1102 C C    B ALA   A 1 39  ? 26.366 0.789   -2.154  0.66 10.15 ?  39  ALA   A C    1 
ATOM   1103 O O    A ALA   A 1 39  ? 26.097 -0.211  -2.691  0.34 9.73  ?  39  ALA   A O    1 
ATOM   1104 O O    B ALA   A 1 39  ? 25.902 -0.148  -2.812  0.66 11.13 ?  39  ALA   A O    1 
ATOM   1105 C CB   A ALA   A 1 39  ? 27.664 0.387   0.193   0.34 9.10  ?  39  ALA   A CB   1 
ATOM   1106 C CB   B ALA   A 1 39  ? 27.603 0.637   0.025   0.66 11.32 ?  39  ALA   A CB   1 
ATOM   1107 H H    A ALA   A 1 39  ? 25.533 -0.918  0.056   0.34 11.68 ?  39  ALA   A H    1 
ATOM   1108 H H    B ALA   A 1 39  ? 25.664 -0.910  0.039   0.66 13.41 ?  39  ALA   A H    1 
ATOM   1109 H HA   A ALA   A 1 39  ? 26.142 1.688   -0.264  0.34 10.86 ?  39  ALA   A HA   1 
ATOM   1110 H HA   B ALA   A 1 39  ? 25.918 1.727   -0.382  0.66 12.67 ?  39  ALA   A HA   1 
ATOM   1111 H HB1  A ALA   A 1 39  ? 28.370 0.977   -0.116  0.34 11.07 ?  39  ALA   A HB1  1 
ATOM   1112 H HB1  B ALA   A 1 39  ? 28.215 1.310   -0.310  0.66 13.74 ?  39  ALA   A HB1  1 
ATOM   1113 H HB2  A ALA   A 1 39  ? 27.550 0.484   1.152   0.34 11.07 ?  39  ALA   A HB2  1 
ATOM   1114 H HB2  B ALA   A 1 39  ? 27.508 0.731   0.989   0.66 13.74 ?  39  ALA   A HB2  1 
ATOM   1115 H HB3  A ALA   A 1 39  ? 27.880 -0.531  -0.026  0.34 11.07 ?  39  ALA   A HB3  1 
ATOM   1116 H HB3  B ALA   A 1 39  ? 27.926 -0.247  -0.191  0.66 13.74 ?  39  ALA   A HB3  1 
ATOM   1117 N N    A ASN   A 1 40  ? 27.271 1.716   -2.529  0.34 9.90  ?  40  ASN   A N    1 
ATOM   1118 N N    B ASN   A 1 40  ? 26.995 1.823   -2.712  0.66 9.76  ?  40  ASN   A N    1 
ATOM   1119 C CA   A ASN   A 1 40  ? 27.836 1.685   -3.874  0.34 10.03 ?  40  ASN   A CA   1 
ATOM   1120 C CA   B ASN   A 1 40  ? 27.549 1.759   -4.057  0.66 9.69  ?  40  ASN   A CA   1 
ATOM   1121 C C    A ASN   A 1 40  ? 29.359 1.591   -3.789  0.34 9.70  ?  40  ASN   A C    1 
ATOM   1122 C C    B ASN   A 1 40  ? 29.070 1.608   -3.972  0.66 9.39  ?  40  ASN   A C    1 
ATOM   1123 O O    A ASN   A 1 40  ? 29.951 1.716   -2.713  0.34 9.99  ?  40  ASN   A O    1 
ATOM   1124 O O    B ASN   A 1 40  ? 29.663 1.700   -2.896  0.66 9.42  ?  40  ASN   A O    1 
ATOM   1125 C CB   A ASN   A 1 40  ? 27.371 2.881   -4.724  0.34 10.83 ?  40  ASN   A CB   1 
ATOM   1126 C CB   B ASN   A 1 40  ? 27.129 2.968   -4.904  0.66 10.34 ?  40  ASN   A CB   1 
ATOM   1127 C CG   A ASN   A 1 40  ? 27.729 4.222   -4.117  0.34 11.77 ?  40  ASN   A CG   1 
ATOM   1128 C CG   B ASN   A 1 40  ? 27.503 4.284   -4.276  0.66 10.93 ?  40  ASN   A CG   1 
ATOM   1129 O OD1  A ASN   A 1 40  ? 28.880 4.467   -3.760  0.34 11.42 ?  40  ASN   A OD1  1 
ATOM   1130 O OD1  B ASN   A 1 40  ? 28.679 4.557   -4.038  0.66 11.34 ?  40  ASN   A OD1  1 
ATOM   1131 N ND2  A ASN   A 1 40  ? 26.737 5.105   -4.007  0.34 12.83 ?  40  ASN   A ND2  1 
ATOM   1132 N ND2  B ASN   A 1 40  ? 26.502 5.119   -4.017  0.66 11.85 ?  40  ASN   A ND2  1 
ATOM   1133 H H    A ASN   A 1 40  ? 27.456 2.445   -2.106  0.34 12.03 ?  40  ASN   A H    1 
ATOM   1134 H H    B ASN   A 1 40  ? 27.111 2.580   -2.323  0.66 11.86 ?  40  ASN   A H    1 
ATOM   1135 H HA   A ASN   A 1 40  ? 27.525 0.887   -4.320  0.34 12.19 ?  40  ASN   A HA   1 
ATOM   1136 H HA   B ASN   A 1 40  ? 27.199 0.961   -4.492  0.66 11.78 ?  40  ASN   A HA   1 
ATOM   1137 H HB2  A ASN   A 1 40  ? 27.788 2.829   -5.606  0.34 13.14 ?  40  ASN   A HB2  1 
ATOM   1138 H HB2  B ASN   A 1 40  ? 27.563 2.908   -5.768  0.66 12.55 ?  40  ASN   A HB2  1 
ATOM   1139 H HB3  A ASN   A 1 40  ? 26.409 2.848   -4.820  0.34 13.14 ?  40  ASN   A HB3  1 
ATOM   1140 H HB3  B ASN   A 1 40  ? 26.163 2.950   -5.018  0.66 12.55 ?  40  ASN   A HB3  1 
ATOM   1141 H HD21 A ASN   A 1 40  ? 26.887 5.890   -3.683  0.34 15.55 ?  40  ASN   A HD21 1 
ATOM   1142 H HD21 B ASN   A 1 40  ? 26.666 5.888   -3.664  0.66 14.37 ?  40  ASN   A HD21 1 
ATOM   1143 H HD22 A ASN   A 1 40  ? 25.944 4.894   -4.262  0.34 15.55 ?  40  ASN   A HD22 1 
ATOM   1144 H HD22 B ASN   A 1 40  ? 25.695 4.897   -4.206  0.66 14.37 ?  40  ASN   A HD22 1 
ATOM   1145 N N    A VAL   A 1 41  ? 29.992 1.348   -4.944  0.34 9.63  ?  41  VAL   A N    1 
ATOM   1146 N N    B VAL   A 1 41  ? 29.698 1.358   -5.124  0.66 10.11 ?  41  VAL   A N    1 
ATOM   1147 C CA   A VAL   A 1 41  ? 31.419 1.022   -4.948  0.34 9.94  ?  41  VAL   A CA   1 
ATOM   1148 C CA   B VAL   A 1 41  ? 31.124 1.033   -5.140  0.66 10.63 ?  41  VAL   A CA   1 
ATOM   1149 C C    A VAL   A 1 41  ? 32.254 2.176   -4.412  0.34 9.81  ?  41  VAL   A C    1 
ATOM   1150 C C    B VAL   A 1 41  ? 31.994 2.187   -4.657  0.66 10.19 ?  41  VAL   A C    1 
ATOM   1151 O O    A VAL   A 1 41  ? 33.324 1.956   -3.829  0.34 9.63  ?  41  VAL   A O    1 
ATOM   1152 O O    B VAL   A 1 41  ? 33.161 1.971   -4.302  0.66 10.17 ?  41  VAL   A O    1 
ATOM   1153 C CB   A VAL   A 1 41  ? 31.908 0.543   -6.336  0.34 9.64  ?  41  VAL   A CB   1 
ATOM   1154 C CB   B VAL   A 1 41  ? 31.600 0.557   -6.533  0.66 12.03 ?  41  VAL   A CB   1 
ATOM   1155 C CG1  A VAL   A 1 41  ? 31.246 -0.776  -6.721  0.34 9.41  ?  41  VAL   A CG1  1 
ATOM   1156 C CG1  B VAL   A 1 41  ? 30.837 -0.681  -6.983  0.66 13.14 ?  41  VAL   A CG1  1 
ATOM   1157 C CG2  A VAL   A 1 41  ? 31.674 1.597   -7.407  0.34 10.44 ?  41  VAL   A CG2  1 
ATOM   1158 C CG2  B VAL   A 1 41  ? 31.494 1.670   -7.563  0.66 13.38 ?  41  VAL   A CG2  1 
ATOM   1159 H H    A VAL   A 1 41  ? 29.632 1.370   -5.722  0.34 11.70 ?  41  VAL   A H    1 
ATOM   1160 H H    B VAL   A 1 41  ? 29.316 1.352   -5.893  0.66 12.28 ?  41  VAL   A H    1 
ATOM   1161 H HA   A VAL   A 1 41  ? 31.570 0.287   -4.342  0.34 12.08 ?  41  VAL   A HA   1 
ATOM   1162 H HA   B VAL   A 1 41  ? 31.263 0.290   -4.531  0.66 12.91 ?  41  VAL   A HA   1 
ATOM   1163 H HB   A VAL   A 1 41  ? 32.868 0.379   -6.295  0.34 11.72 ?  41  VAL   A HB   1 
ATOM   1164 H HB   B VAL   A 1 41  ? 32.536 0.314   -6.466  0.66 14.58 ?  41  VAL   A HB   1 
ATOM   1165 H HG11 A VAL   A 1 41  ? 31.608 -1.080  -7.570  0.34 11.45 ?  41  VAL   A HG11 1 
ATOM   1166 H HG11 B VAL   A 1 41  ? 31.129 -0.923  -7.876  0.66 15.92 ?  41  VAL   A HG11 1 
ATOM   1167 H HG12 A VAL   A 1 41  ? 31.424 -1.435  -6.032  0.34 11.45 ?  41  VAL   A HG12 1 
ATOM   1168 H HG12 B VAL   A 1 41  ? 31.017 -1.404  -6.366  0.66 15.92 ?  41  VAL   A HG12 1 
ATOM   1169 H HG13 A VAL   A 1 41  ? 30.289 -0.635  -6.804  0.34 11.45 ?  41  VAL   A HG13 1 
ATOM   1170 H HG13 B VAL   A 1 41  ? 29.887 -0.482  -6.991  0.66 15.92 ?  41  VAL   A HG13 1 
ATOM   1171 H HG21 A VAL   A 1 41  ? 31.988 1.258   -8.262  0.34 12.67 ?  41  VAL   A HG21 1 
ATOM   1172 H HG21 B VAL   A 1 41  ? 31.686 1.301   -8.440  0.66 16.21 ?  41  VAL   A HG21 1 
ATOM   1173 H HG22 A VAL   A 1 41  ? 30.725 1.789   -7.460  0.34 12.67 ?  41  VAL   A HG22 1 
ATOM   1174 H HG22 B VAL   A 1 41  ? 30.599 2.034   -7.543  0.66 16.21 ?  41  VAL   A HG22 1 
ATOM   1175 H HG23 A VAL   A 1 41  ? 32.162 2.401   -7.173  0.34 12.67 ?  41  VAL   A HG23 1 
ATOM   1176 H HG23 B VAL   A 1 41  ? 32.141 2.361   -7.348  0.66 16.21 ?  41  VAL   A HG23 1 
ATOM   1177 N N    A TYR   A 1 42  ? 31.790 3.410   -4.588  0.34 10.02 ?  42  TYR   A N    1 
ATOM   1178 N N    B TYR   A 1 42  ? 31.472 3.415   -4.669  0.66 10.28 ?  42  TYR   A N    1 
ATOM   1179 C CA   A TYR   A 1 42  ? 32.520 4.588   -4.139  0.34 9.85  ?  42  TYR   A CA   1 
ATOM   1180 C CA   B TYR   A 1 42  ? 32.219 4.602   -4.258  0.66 10.09 ?  42  TYR   A CA   1 
ATOM   1181 C C    A TYR   A 1 42  ? 32.190 4.960   -2.704  0.34 9.76  ?  42  TYR   A C    1 
ATOM   1182 C C    B TYR   A 1 42  ? 31.987 4.978   -2.803  0.66 10.38 ?  42  TYR   A C    1 
ATOM   1183 O O    A TYR   A 1 42  ? 32.763 5.922   -2.178  0.34 10.15 ?  42  TYR   A O    1 
ATOM   1184 O O    B TYR   A 1 42  ? 32.553 5.978   -2.342  0.66 10.88 ?  42  TYR   A O    1 
ATOM   1185 C CB   A TYR   A 1 42  ? 32.226 5.781   -5.061  0.34 10.27 ?  42  TYR   A CB   1 
ATOM   1186 C CB   B TYR   A 1 42  ? 31.858 5.796   -5.157  0.66 10.32 ?  42  TYR   A CB   1 
ATOM   1187 C CG   A TYR   A 1 42  ? 32.407 5.449   -6.523  0.34 10.10 ?  42  TYR   A CG   1 
ATOM   1188 C CG   B TYR   A 1 42  ? 32.002 5.502   -6.630  0.66 10.83 ?  42  TYR   A CG   1 
ATOM   1189 C CD1  A TYR   A 1 42  ? 33.673 5.253   -7.052  0.34 10.50 ?  42  TYR   A CD1  1 
ATOM   1190 C CD1  B TYR   A 1 42  ? 33.250 5.290   -7.195  0.66 11.34 ?  42  TYR   A CD1  1 
ATOM   1191 C CD2  A TYR   A 1 42  ? 31.314 5.310   -7.371  0.34 10.21 ?  42  TYR   A CD2  1 
ATOM   1192 C CD2  B TYR   A 1 42  ? 30.889 5.423   -7.457  0.66 12.35 ?  42  TYR   A CD2  1 
ATOM   1193 C CE1  A TYR   A 1 42  ? 33.850 4.931   -8.382  0.34 10.39 ?  42  TYR   A CE1  1 
ATOM   1194 C CE1  B TYR   A 1 42  ? 33.389 5.002   -8.541  0.66 11.53 ?  42  TYR   A CE1  1 
ATOM   1195 C CE2  A TYR   A 1 42  ? 31.482 4.996   -8.710  0.34 10.32 ?  42  TYR   A CE2  1 
ATOM   1196 C CE2  B TYR   A 1 42  ? 31.019 5.155   -8.807  0.66 13.25 ?  42  TYR   A CE2  1 
ATOM   1197 C CZ   A TYR   A 1 42  ? 32.753 4.807   -9.208  0.34 10.47 ?  42  TYR   A CZ   1 
ATOM   1198 C CZ   B TYR   A 1 42  ? 32.267 4.937   -9.344  0.66 12.50 ?  42  TYR   A CZ   1 
ATOM   1199 O OH   A TYR   A 1 42  ? 32.943 4.488   -10.532 0.34 11.44 ?  42  TYR   A OH   1 
ATOM   1200 O OH   B TYR   A 1 42  ? 32.390 4.670   -10.689 0.66 13.95 ?  42  TYR   A OH   1 
ATOM   1201 H H    A TYR   A 1 42  ? 31.038 3.595   -4.955  0.34 12.18 ?  42  TYR   A H    1 
ATOM   1202 H H    B TYR   A 1 42  ? 30.670 3.591   -4.933  0.66 12.49 ?  42  TYR   A H    1 
ATOM   1203 H HA   A TYR   A 1 42  ? 33.475 4.410   -4.191  0.34 11.97 ?  42  TYR   A HA   1 
ATOM   1204 H HA   B TYR   A 1 42  ? 33.161 4.432   -4.368  0.66 12.26 ?  42  TYR   A HA   1 
ATOM   1205 H HB2  A TYR   A 1 42  ? 31.310 6.065   -4.928  0.34 12.47 ?  42  TYR   A HB2  1 
ATOM   1206 H HB2  B TYR   A 1 42  ? 30.935 6.050   -4.992  0.66 12.54 ?  42  TYR   A HB2  1 
ATOM   1207 H HB3  A TYR   A 1 42  ? 32.833 6.510   -4.839  0.34 12.47 ?  42  TYR   A HB3  1 
ATOM   1208 H HB3  B TYR   A 1 42  ? 32.445 6.539   -4.941  0.66 12.54 ?  42  TYR   A HB3  1 
ATOM   1209 H HD1  A TYR   A 1 42  ? 34.420 5.335   -6.502  0.34 12.75 ?  42  TYR   A HD1  1 
ATOM   1210 H HD1  B TYR   A 1 42  ? 34.008 5.324   -6.657  0.66 13.76 ?  42  TYR   A HD1  1 
ATOM   1211 H HD2  A TYR   A 1 42  ? 30.458 5.441   -7.036  0.34 12.41 ?  42  TYR   A HD2  1 
ATOM   1212 H HD2  B TYR   A 1 42  ? 30.042 5.572   -7.099  0.66 14.97 ?  42  TYR   A HD2  1 
ATOM   1213 H HE1  A TYR   A 1 42  ? 34.710 4.806   -8.723  0.34 12.62 ?  42  TYR   A HE1  1 
ATOM   1214 H HE1  B TYR   A 1 42  ? 34.233 4.860   -8.902  0.66 13.98 ?  42  TYR   A HE1  1 
ATOM   1215 H HE2  A TYR   A 1 42  ? 30.744 4.909   -9.270  0.34 12.54 ?  42  TYR   A HE2  1 
ATOM   1216 H HE2  B TYR   A 1 42  ? 30.261 5.109   -9.349  0.66 16.05 ?  42  TYR   A HE2  1 
ATOM   1217 H HH   A TYR   A 1 42  ? 32.206 4.440   -10.931 0.34 13.88 ?  42  TYR   A HH   1 
ATOM   1218 H HH   B TYR   A 1 42  ? 33.199 4.564   -10.886 0.66 16.89 ?  42  TYR   A HH   1 
ATOM   1219 N N    A LEU   A 1 43  ? 31.279 4.228   -2.067  0.34 9.47  ?  43  LEU   A N    1 
ATOM   1220 N N    B LEU   A 1 43  ? 31.162 4.216   -2.083  0.66 10.27 ?  43  LEU   A N    1 
ATOM   1221 C CA   A LEU   A 1 43  ? 30.830 4.541   -0.714  0.34 9.48  ?  43  LEU   A CA   1 
ATOM   1222 C CA   B LEU   A 1 43  ? 30.711 4.575   -0.738  0.66 9.89  ?  43  LEU   A CA   1 
ATOM   1223 C C    A LEU   A 1 43  ? 30.355 5.989   -0.607  0.34 10.09 ?  43  LEU   A C    1 
ATOM   1224 C C    B LEU   A 1 43  ? 30.230 6.024   -0.667  0.66 9.92  ?  43  LEU   A C    1 
ATOM   1225 O O    A LEU   A 1 43  ? 30.624 6.684   0.374   0.34 10.54 ?  43  LEU   A O    1 
ATOM   1226 O O    B LEU   A 1 43  ? 30.468 6.730   0.315   0.66 10.76 ?  43  LEU   A O    1 
ATOM   1227 C CB   A LEU   A 1 43  ? 31.897 4.218   0.333   0.34 10.00 ?  43  LEU   A CB   1 
ATOM   1228 C CB   B LEU   A 1 43  ? 31.750 4.273   0.341   0.66 10.01 ?  43  LEU   A CB   1 
ATOM   1229 C CG   A LEU   A 1 43  ? 32.373 2.767   0.418   0.34 10.61 ?  43  LEU   A CG   1 
ATOM   1230 C CG   B LEU   A 1 43  ? 32.255 2.832   0.433   0.66 10.37 ?  43  LEU   A CG   1 
ATOM   1231 C CD1  A LEU   A 1 43  ? 33.453 2.648   1.479   0.34 11.02 ?  43  LEU   A CD1  1 
ATOM   1232 C CD1  B LEU   A 1 43  ? 33.283 2.726   1.548   0.66 11.17 ?  43  LEU   A CD1  1 
ATOM   1233 C CD2  A LEU   A 1 43  ? 31.225 1.817   0.712   0.34 10.78 ?  43  LEU   A CD2  1 
ATOM   1234 C CD2  B LEU   A 1 43  ? 31.128 1.823   0.620   0.66 10.87 ?  43  LEU   A CD2  1 
ATOM   1235 H H    A LEU   A 1 43  ? 30.899 3.534   -2.405  0.34 11.51 ?  43  LEU   A H    1 
ATOM   1236 H H    B LEU   A 1 43  ? 30.845 3.468   -2.356  0.66 12.48 ?  43  LEU   A H    1 
ATOM   1237 H HA   A LEU   A 1 43  ? 30.065 3.978   -0.521  0.34 11.52 ?  43  LEU   A HA   1 
ATOM   1238 H HA   B LEU   A 1 43  ? 29.937 4.020   -0.538  0.66 12.03 ?  43  LEU   A HA   1 
ATOM   1239 H HB2  A LEU   A 1 43  ? 32.674 4.765   0.156   0.34 12.15 ?  43  LEU   A HB2  1 
ATOM   1240 H HB2  B LEU   A 1 43  ? 32.514 4.842   0.189   0.66 12.17 ?  43  LEU   A HB2  1 
ATOM   1241 H HB3  A LEU   A 1 43  ? 31.533 4.443   1.204   0.34 12.15 ?  43  LEU   A HB3  1 
ATOM   1242 H HB3  B LEU   A 1 43  ? 31.352 4.493   1.203   0.66 12.17 ?  43  LEU   A HB3  1 
ATOM   1243 H HG   A LEU   A 1 43  ? 32.765 2.509   -0.432  0.34 12.88 ?  43  LEU   A HG   1 
ATOM   1244 H HG   B LEU   A 1 43  ? 32.705 2.615   -0.396  0.66 12.59 ?  43  LEU   A HG   1 
ATOM   1245 H HD11 A LEU   A 1 43  ? 33.752 1.726   1.526   0.34 13.38 ?  43  LEU   A HD11 1 
ATOM   1246 H HD11 B LEU   A 1 43  ? 33.602 1.811   1.598   0.66 13.56 ?  43  LEU   A HD11 1 
ATOM   1247 H HD12 A LEU   A 1 43  ? 34.195 3.225   1.239   0.34 13.38 ?  43  LEU   A HD12 1 
ATOM   1248 H HD12 B LEU   A 1 43  ? 34.023 3.323   1.352   0.66 13.56 ?  43  LEU   A HD12 1 
ATOM   1249 H HD13 A LEU   A 1 43  ? 33.084 2.921   2.334   0.34 13.38 ?  43  LEU   A HD13 1 
ATOM   1250 H HD13 B LEU   A 1 43  ? 32.868 2.978   2.387   0.66 13.56 ?  43  LEU   A HD13 1 
ATOM   1251 H HD21 A LEU   A 1 43  ? 31.581 0.928   0.866   0.34 13.09 ?  43  LEU   A HD21 1 
ATOM   1252 H HD21 B LEU   A 1 43  ? 31.515 0.942   0.747   0.66 13.19 ?  43  LEU   A HD21 1 
ATOM   1253 H HD22 A LEU   A 1 43  ? 30.755 2.128   1.500   0.34 13.09 ?  43  LEU   A HD22 1 
ATOM   1254 H HD22 B LEU   A 1 43  ? 30.606 2.072   1.395   0.66 13.19 ?  43  LEU   A HD22 1 
ATOM   1255 H HD23 A LEU   A 1 43  ? 30.625 1.806   -0.050  0.34 13.09 ?  43  LEU   A HD23 1 
ATOM   1256 H HD23 B LEU   A 1 43  ? 30.570 1.827   -0.174  0.66 13.19 ?  43  LEU   A HD23 1 
ATOM   1257 N N    A LYS   A 1 44  ? 29.637 6.447   -1.634  0.34 10.77 ?  44  LYS   A N    1 
ATOM   1258 N N    B LYS   A 1 44  ? 29.521 6.459   -1.709  0.66 9.94  ?  44  LYS   A N    1 
ATOM   1259 C CA   A LYS   A 1 44  ? 29.007 7.764   -1.628  0.34 11.52 ?  44  LYS   A CA   1 
ATOM   1260 C CA   B LYS   A 1 44  ? 28.862 7.765   -1.722  0.66 9.94  ?  44  LYS   A CA   1 
ATOM   1261 C C    A LYS   A 1 44  ? 27.564 7.583   -1.173  0.34 10.57 ?  44  LYS   A C    1 
ATOM   1262 C C    B LYS   A 1 44  ? 27.447 7.569   -1.199  0.66 9.49  ?  44  LYS   A C    1 
ATOM   1263 O O    A LYS   A 1 44  ? 26.723 7.082   -1.928  0.34 11.38 ?  44  LYS   A O    1 
ATOM   1264 O O    B LYS   A 1 44  ? 26.574 7.045   -1.898  0.66 10.61 ?  44  LYS   A O    1 
ATOM   1265 C CB   A LYS   A 1 44  ? 29.081 8.410   -3.008  0.34 13.56 ?  44  LYS   A CB   1 
ATOM   1266 C CB   B LYS   A 1 44  ? 28.875 8.362   -3.125  0.66 12.15 ?  44  LYS   A CB   1 
ATOM   1267 C CG   A LYS   A 1 44  ? 30.486 8.784   -3.445  0.34 16.05 ?  44  LYS   A CG   1 
ATOM   1268 C CG   B LYS   A 1 44  ? 30.227 8.896   -3.551  0.66 15.73 ?  44  LYS   A CG   1 
ATOM   1269 C CD   A LYS   A 1 44  ? 31.165 9.709   -2.447  0.34 19.33 ?  44  LYS   A CD   1 
ATOM   1270 C CD   B LYS   A 1 44  ? 30.823 9.834   -2.502  0.66 20.59 ?  44  LYS   A CD   1 
ATOM   1271 C CE   A LYS   A 1 44  ? 32.501 10.199  -2.967  0.34 21.61 ?  44  LYS   A CE   1 
ATOM   1272 C CE   B LYS   A 1 44  ? 32.172 10.364  -2.934  0.66 23.39 ?  44  LYS   A CE   1 
ATOM   1273 N NZ   A LYS   A 1 44  ? 33.243 10.953  -1.926  0.34 22.87 ?  44  LYS   A NZ   1 
ATOM   1274 N NZ   B LYS   A 1 44  ? 33.007 10.757  -1.764  0.66 24.74 ?  44  LYS   A NZ   1 
ATOM   1275 H H    A LYS   A 1 44  ? 29.502 6.004   -2.363  0.34 13.08 ?  44  LYS   A H    1 
ATOM   1276 H H    B LYS   A 1 44  ? 29.403 6.012   -2.434  0.66 12.08 ?  44  LYS   A H    1 
ATOM   1277 H HA   A LYS   A 1 44  ? 29.454 8.335   -0.983  0.34 13.98 ?  44  LYS   A HA   1 
ATOM   1278 H HA   B LYS   A 1 44  ? 29.306 8.363   -1.102  0.66 12.08 ?  44  LYS   A HA   1 
ATOM   1279 H HB2  A LYS   A 1 44  ? 28.724 7.789   -3.660  0.34 16.42 ?  44  LYS   A HB2  1 
ATOM   1280 H HB2  B LYS   A 1 44  ? 28.615 7.675   -3.759  0.66 14.73 ?  44  LYS   A HB2  1 
ATOM   1281 H HB3  A LYS   A 1 44  ? 28.549 9.220   -3.000  0.34 16.42 ?  44  LYS   A HB3  1 
ATOM   1282 H HB3  B LYS   A 1 44  ? 28.240 9.097   -3.161  0.66 14.73 ?  44  LYS   A HB3  1 
ATOM   1283 H HG2  A LYS   A 1 44  ? 31.018 7.979   -3.527  0.34 19.41 ?  44  LYS   A HG2  1 
ATOM   1284 H HG2  B LYS   A 1 44  ? 30.838 8.160   -3.685  0.66 19.03 ?  44  LYS   A HG2  1 
ATOM   1285 H HG3  A LYS   A 1 44  ? 30.438 9.243   -4.300  0.34 19.41 ?  44  LYS   A HG3  1 
ATOM   1286 H HG3  B LYS   A 1 44  ? 30.125 9.403   -4.379  0.66 19.03 ?  44  LYS   A HG3  1 
ATOM   1287 H HD2  A LYS   A 1 44  ? 30.592 10.476  -2.283  0.34 23.35 ?  44  LYS   A HD2  1 
ATOM   1288 H HD2  B LYS   A 1 44  ? 30.219 10.579  -2.355  0.66 24.86 ?  44  LYS   A HD2  1 
ATOM   1289 H HD3  A LYS   A 1 44  ? 31.323 9.225   -1.620  0.34 23.35 ?  44  LYS   A HD3  1 
ATOM   1290 H HD3  B LYS   A 1 44  ? 30.966 9.346   -1.675  0.66 24.86 ?  44  LYS   A HD3  1 
ATOM   1291 H HE2  A LYS   A 1 44  ? 33.036 9.436   -3.235  0.34 26.08 ?  44  LYS   A HE2  1 
ATOM   1292 H HE2  B LYS   A 1 44  ? 32.646 9.670   -3.422  0.66 28.22 ?  44  LYS   A HE2  1 
ATOM   1293 H HE3  A LYS   A 1 44  ? 32.349 10.786  -3.724  0.34 26.08 ?  44  LYS   A HE3  1 
ATOM   1294 H HE3  B LYS   A 1 44  ? 32.046 11.142  -3.493  0.66 28.22 ?  44  LYS   A HE3  1 
ATOM   1295 H HZ1  A LYS   A 1 44  ? 34.038 11.195  -2.238  0.34 27.59 ?  44  LYS   A HZ1  1 
ATOM   1296 H HZ1  B LYS   A 1 44  ? 33.794 11.066  -2.043  0.66 29.84 ?  44  LYS   A HZ1  1 
ATOM   1297 H HZ2  A LYS   A 1 44  ? 32.786 11.683  -1.697  0.34 27.59 ?  44  LYS   A HZ2  1 
ATOM   1298 H HZ2  B LYS   A 1 44  ? 32.595 11.396  -1.299  0.66 29.84 ?  44  LYS   A HZ2  1 
ATOM   1299 H HZ3  A LYS   A 1 44  ? 33.355 10.444  -1.205  0.34 27.59 ?  44  LYS   A HZ3  1 
ATOM   1300 H HZ3  B LYS   A 1 44  ? 33.142 10.056  -1.234  0.66 29.84 ?  44  LYS   A HZ3  1 
ATOM   1301 N N    A HIS   A 1 45  ? 27.285 7.986   0.062   0.34 9.83  ?  45  HIS   A N    1 
ATOM   1302 N N    B HIS   A 1 45  ? 27.225 7.966   0.053   0.66 9.79  ?  45  HIS   A N    1 
ATOM   1303 C CA   A HIS   A 1 45  ? 26.043 7.617   0.737   0.34 9.39  ?  45  HIS   A CA   1 
ATOM   1304 C CA   B HIS   A 1 45  ? 25.986 7.649   0.763   0.66 10.45 ?  45  HIS   A CA   1 
ATOM   1305 C C    A HIS   A 1 45  ? 25.002 8.729   0.583   0.34 9.42  ?  45  HIS   A C    1 
ATOM   1306 C C    B HIS   A 1 45  ? 24.977 8.779   0.564   0.66 10.84 ?  45  HIS   A C    1 
ATOM   1307 O O    A HIS   A 1 45  ? 24.618 9.413   1.533   0.34 10.31 ?  45  HIS   A O    1 
ATOM   1308 O O    B HIS   A 1 45  ? 24.780 9.642   1.422   0.66 12.73 ?  45  HIS   A O    1 
ATOM   1309 C CB   A HIS   A 1 45  ? 26.332 7.289   2.197   0.34 8.97  ?  45  HIS   A CB   1 
ATOM   1310 C CB   B HIS   A 1 45  ? 26.276 7.442   2.239   0.66 10.25 ?  45  HIS   A CB   1 
ATOM   1311 C CG   A HIS   A 1 45  ? 27.452 6.312   2.381   0.34 8.35  ?  45  HIS   A CG   1 
ATOM   1312 C CG   B HIS   A 1 45  ? 27.391 6.487   2.506   0.66 9.86  ?  45  HIS   A CG   1 
ATOM   1313 N ND1  A HIS   A 1 45  ? 27.442 5.050   1.823   0.34 7.74  ?  45  HIS   A ND1  1 
ATOM   1314 N ND1  B HIS   A 1 45  ? 27.396 5.191   2.034   0.66 10.63 ?  45  HIS   A ND1  1 
ATOM   1315 C CD2  A HIS   A 1 45  ? 28.619 6.417   3.060   0.34 9.06  ?  45  HIS   A CD2  1 
ATOM   1316 C CD2  B HIS   A 1 45  ? 28.543 6.648   3.196   0.66 9.45  ?  45  HIS   A CD2  1 
ATOM   1317 C CE1  A HIS   A 1 45  ? 28.556 4.419   2.159   0.34 8.93  ?  45  HIS   A CE1  1 
ATOM   1318 C CE1  B HIS   A 1 45  ? 28.509 4.597   2.428   0.66 9.34  ?  45  HIS   A CE1  1 
ATOM   1319 N NE2  A HIS   A 1 45  ? 29.288 5.227   2.906   0.34 9.57  ?  45  HIS   A NE2  1 
ATOM   1320 N NE2  B HIS   A 1 45  ? 29.223 5.459   3.131   0.66 9.28  ?  45  HIS   A NE2  1 
ATOM   1321 H H    A HIS   A 1 45  ? 27.805 8.481   0.542   0.34 11.95 ?  45  HIS   A H    1 
ATOM   1322 H H    B HIS   A 1 45  ? 27.783 8.426   0.521   0.66 11.90 ?  45  HIS   A H    1 
ATOM   1323 H HA   A HIS   A 1 45  ? 25.684 6.822   0.321   0.34 11.42 ?  45  HIS   A HA   1 
ATOM   1324 H HA   B HIS   A 1 45  ? 25.608 6.828   0.403   0.66 12.69 ?  45  HIS   A HA   1 
ATOM   1325 H HB2  A HIS   A 1 45  ? 26.571 8.100   2.668   0.34 10.92 ?  45  HIS   A HB2  1 
ATOM   1326 H HB2  B HIS   A 1 45  ? 26.510 8.294   2.633   0.66 12.45 ?  45  HIS   A HB2  1 
ATOM   1327 H HB3  A HIS   A 1 45  ? 25.535 6.899   2.597   0.34 10.92 ?  45  HIS   A HB3  1 
ATOM   1328 H HB3  B HIS   A 1 45  ? 25.473 7.093   2.666   0.66 12.45 ?  45  HIS   A HB3  1 
ATOM   1329 H HD2  A HIS   A 1 45  ? 28.918 7.154   3.538   0.34 11.02 ?  45  HIS   A HD2  1 
ATOM   1330 H HD2  B HIS   A 1 45  ? 28.825 7.423   3.621   0.66 11.49 ?  45  HIS   A HD2  1 
ATOM   1331 H HE1  A HIS   A 1 45  ? 28.791 3.545   1.920   0.34 10.87 ?  45  HIS   A HE1  1 
ATOM   1332 H HE1  B HIS   A 1 45  ? 28.743 3.717   2.244   0.66 11.35 ?  45  HIS   A HE1  1 
ATOM   1333 H HE2  A HIS   A 1 45  ? 30.063 5.036   3.245   0.34 11.63 ?  45  HIS   A HE2  1 
ATOM   1334 H HE2  B HIS   A 1 45  ? 29.987 5.298   3.488   0.66 11.28 ?  45  HIS   A HE2  1 
ATOM   1335 N N    A GLY   A 1 46  ? 24.533 8.885   -0.655  0.34 9.73  ?  46  GLY   A N    1 
ATOM   1336 N N    B GLY   A 1 46  ? 24.313 8.764   -0.587  0.66 10.97 ?  46  GLY   A N    1 
ATOM   1337 C CA   A GLY   A 1 46  ? 23.714 10.027  -1.026  0.34 10.31 ?  46  GLY   A CA   1 
ATOM   1338 C CA   B GLY   A 1 46  ? 23.481 9.896   -0.950  0.66 11.99 ?  46  GLY   A CA   1 
ATOM   1339 C C    A GLY   A 1 46  ? 22.216 9.894   -0.814  0.34 10.54 ?  46  GLY   A C    1 
ATOM   1340 C C    B GLY   A 1 46  ? 22.029 9.795   -0.526  0.66 11.40 ?  46  GLY   A C    1 
ATOM   1341 O O    A GLY   A 1 46  ? 21.539 10.895  -0.557  0.34 10.50 ?  46  GLY   A O    1 
ATOM   1342 O O    B GLY   A 1 46  ? 21.444 10.779  -0.064  0.66 12.53 ?  46  GLY   A O    1 
ATOM   1343 H H    A GLY   A 1 46  ? 24.699 8.344   -1.301  0.34 11.83 ?  46  GLY   A H    1 
ATOM   1344 H H    B GLY   A 1 46  ? 24.324 8.120   -1.159  0.66 13.31 ?  46  GLY   A H    1 
ATOM   1345 H HA2  A GLY   A 1 46  ? 24.024 10.801  -0.526  0.34 12.52 ?  46  GLY   A HA2  1 
ATOM   1346 H HA2  B GLY   A 1 46  ? 23.850 10.699  -0.546  0.66 14.54 ?  46  GLY   A HA2  1 
ATOM   1347 H HA3  A GLY   A 1 46  ? 23.860 10.211  -1.968  0.34 12.52 ?  46  GLY   A HA3  1 
ATOM   1348 H HA3  B GLY   A 1 46  ? 23.507 10.007  -1.910  0.66 14.54 ?  46  GLY   A HA3  1 
ATOM   1349 N N    A GLY   A 1 47  ? 21.677 8.684   -0.939  0.34 10.80 ?  47  GLY   A N    1 
ATOM   1350 N N    B GLY   A 1 47  ? 21.432 8.616   -0.684  0.66 11.33 ?  47  GLY   A N    1 
ATOM   1351 C CA   A GLY   A 1 47  ? 20.243 8.488   -0.838  0.34 10.67 ?  47  GLY   A CA   1 
ATOM   1352 C CA   B GLY   A 1 47  ? 20.010 8.446   -0.475  0.66 11.51 ?  47  GLY   A CA   1 
ATOM   1353 C C    A GLY   A 1 47  ? 19.935 7.052   -0.470  0.34 10.19 ?  47  GLY   A C    1 
ATOM   1354 C C    B GLY   A 1 47  ? 19.689 7.021   -0.083  0.66 10.30 ?  47  GLY   A C    1 
ATOM   1355 O O    A GLY   A 1 47  ? 20.833 6.237   -0.255  0.34 10.59 ?  47  GLY   A O    1 
ATOM   1356 O O    B GLY   A 1 47  ? 20.580 6.182   0.067   0.66 10.65 ?  47  GLY   A O    1 
ATOM   1357 H H    A GLY   A 1 47  ? 22.126 7.964   -1.081  0.34 13.11 ?  47  GLY   A H    1 
ATOM   1358 H H    B GLY   A 1 47  ? 21.845 7.894   -0.904  0.66 13.75 ?  47  GLY   A H    1 
ATOM   1359 H HA2  A GLY   A 1 47  ? 19.877 9.086   -0.163  0.34 12.95 ?  47  GLY   A HA2  1 
ATOM   1360 H HA2  B GLY   A 1 47  ? 19.706 9.038   0.230   0.66 13.96 ?  47  GLY   A HA2  1 
ATOM   1361 H HA3  A GLY   A 1 47  ? 19.828 8.692   -1.692  0.34 12.95 ?  47  GLY   A HA3  1 
ATOM   1362 H HA3  B GLY   A 1 47  ? 19.532 8.665   -1.293  0.66 13.96 ?  47  GLY   A HA3  1 
ATOM   1363 N N    A GLY   A 1 48  ? 18.643 6.741   -0.413  0.34 9.84  ?  48  GLY   A N    1 
ATOM   1364 N N    B GLY   A 1 48  ? 18.396 6.750   0.083   0.66 10.69 ?  48  GLY   A N    1 
ATOM   1365 C CA   A GLY   A 1 48  ? 18.245 5.396   -0.040  0.34 9.92  ?  48  GLY   A CA   1 
ATOM   1366 C CA   B GLY   A 1 48  ? 17.978 5.431   0.508   0.66 10.31 ?  48  GLY   A CA   1 
ATOM   1367 C C    A GLY   A 1 48  ? 18.698 5.044   1.366   0.34 9.51  ?  48  GLY   A C    1 
ATOM   1368 C C    B GLY   A 1 48  ? 18.575 5.064   1.855   0.66 10.32 ?  48  GLY   A C    1 
ATOM   1369 O O    A GLY   A 1 48  ? 18.854 5.908   2.236   0.34 9.69  ?  48  GLY   A O    1 
ATOM   1370 O O    B GLY   A 1 48  ? 18.792 5.910   2.735   0.66 10.83 ?  48  GLY   A O    1 
ATOM   1371 H H    A GLY   A 1 48  ? 18.000 7.278   -0.586  0.34 11.95 ?  48  GLY   A H    1 
ATOM   1372 H H    B GLY   A 1 48  ? 17.743 7.307   -0.047  0.66 12.98 ?  48  GLY   A H    1 
ATOM   1373 H HA2  A GLY   A 1 48  ? 17.283 5.316   -0.085  0.34 12.05 ?  48  GLY   A HA2  1 
ATOM   1374 H HA2  B GLY   A 1 48  ? 17.010 5.392   0.571   0.66 12.52 ?  48  GLY   A HA2  1 
ATOM   1375 H HA3  A GLY   A 1 48  ? 18.641 4.755   -0.654  0.34 12.05 ?  48  GLY   A HA3  1 
ATOM   1376 H HA3  B GLY   A 1 48  ? 18.269 4.770   -0.146  0.66 12.52 ?  48  GLY   A HA3  1 
ATOM   1377 N N    A VAL   A 1 49  ? 18.926 3.746   1.592   0.34 10.23 ?  49  VAL   A N    1 
ATOM   1378 N N    B VAL   A 1 49  ? 18.834 3.765   2.021   0.66 10.54 ?  49  VAL   A N    1 
ATOM   1379 C CA   A VAL   A 1 49  ? 19.410 3.293   2.896   0.34 10.91 ?  49  VAL   A CA   1 
ATOM   1380 C CA   B VAL   A 1 49  ? 19.465 3.264   3.240   0.66 10.57 ?  49  VAL   A CA   1 
ATOM   1381 C C    A VAL   A 1 49  ? 20.725 3.976   3.245   0.34 9.74  ?  49  VAL   A C    1 
ATOM   1382 C C    B VAL   A 1 49  ? 20.739 4.037   3.543   0.66 10.05 ?  49  VAL   A C    1 
ATOM   1383 O O    A VAL   A 1 49  ? 20.940 4.385   4.390   0.34 9.91  ?  49  VAL   A O    1 
ATOM   1384 O O    B VAL   A 1 49  ? 20.968 4.472   4.676   0.66 10.02 ?  49  VAL   A O    1 
ATOM   1385 C CB   A VAL   A 1 49  ? 19.538 1.756   2.930   0.34 12.36 ?  49  VAL   A CB   1 
ATOM   1386 C CB   B VAL   A 1 49  ? 19.763 1.760   3.094   0.66 11.16 ?  49  VAL   A CB   1 
ATOM   1387 C CG1  A VAL   A 1 49  ? 20.333 1.303   4.154   0.34 12.78 ?  49  VAL   A CG1  1 
ATOM   1388 C CG1  B VAL   A 1 49  ? 20.613 1.272   4.255   0.66 11.06 ?  49  VAL   A CG1  1 
ATOM   1389 C CG2  A VAL   A 1 49  ? 18.163 1.104   2.928   0.34 13.50 ?  49  VAL   A CG2  1 
ATOM   1390 C CG2  B VAL   A 1 49  ? 18.473 0.950   2.971   0.66 12.37 ?  49  VAL   A CG2  1 
ATOM   1391 H H    A VAL   A 1 49  ? 18.811 3.117   1.018   0.34 12.43 ?  49  VAL   A H    1 
ATOM   1392 H H    B VAL   A 1 49  ? 18.641 3.161   1.447   0.66 12.80 ?  49  VAL   A H    1 
ATOM   1393 H HA   A VAL   A 1 49  ? 18.765 3.539   3.574   0.34 13.25 ?  49  VAL   A HA   1 
ATOM   1394 H HA   B VAL   A 1 49  ? 18.860 3.380   3.987   0.66 12.84 ?  49  VAL   A HA   1 
ATOM   1395 H HB   A VAL   A 1 49  ? 20.012 1.454   2.141   0.34 14.99 ?  49  VAL   A HB   1 
ATOM   1396 H HB   B VAL   A 1 49  ? 20.268 1.623   2.279   0.66 13.54 ?  49  VAL   A HB   1 
ATOM   1397 H HG11 A VAL   A 1 49  ? 20.162 0.357   4.310   0.34 15.49 ?  49  VAL   A HG11 1 
ATOM   1398 H HG11 B VAL   A 1 49  ? 20.540 0.305   4.309   0.66 13.42 ?  49  VAL   A HG11 1 
ATOM   1399 H HG12 A VAL   A 1 49  ? 21.279 1.439   3.992   0.34 15.49 ?  49  VAL   A HG12 1 
ATOM   1400 H HG12 B VAL   A 1 49  ? 21.535 1.524   4.100   0.66 13.42 ?  49  VAL   A HG12 1 
ATOM   1401 H HG13 A VAL   A 1 49  ? 20.047 1.815   4.926   0.34 15.49 ?  49  VAL   A HG13 1 
ATOM   1402 H HG13 B VAL   A 1 49  ? 20.287 1.673   5.074   0.66 13.42 ?  49  VAL   A HG13 1 
ATOM   1403 H HG21 A VAL   A 1 49  ? 18.268 0.139   2.938   0.34 16.35 ?  49  VAL   A HG21 1 
ATOM   1404 H HG21 B VAL   A 1 49  ? 18.694 0.015   2.867   0.66 14.99 ?  49  VAL   A HG21 1 
ATOM   1405 H HG22 A VAL   A 1 49  ? 17.677 1.391   3.717   0.34 16.35 ?  49  VAL   A HG22 1 
ATOM   1406 H HG22 B VAL   A 1 49  ? 17.940 1.081   3.771   0.66 14.99 ?  49  VAL   A HG22 1 
ATOM   1407 H HG23 A VAL   A 1 49  ? 17.688 1.377   2.129   0.34 16.35 ?  49  VAL   A HG23 1 
ATOM   1408 H HG23 B VAL   A 1 49  ? 17.977 1.261   2.193   0.66 14.99 ?  49  VAL   A HG23 1 
ATOM   1409 N N    A ALA   A 1 50  ? 21.633 4.087   2.274   0.34 9.10  ?  50  ALA   A N    1 
ATOM   1410 N N    B ALA   A 1 50  ? 21.612 4.163   2.544   0.66 9.39  ?  50  ALA   A N    1 
ATOM   1411 C CA   A ALA   A 1 50  ? 22.952 4.647   2.552   0.34 9.02  ?  50  ALA   A CA   1 
ATOM   1412 C CA   B ALA   A 1 50  ? 22.934 4.727   2.780   0.66 9.60  ?  50  ALA   A CA   1 
ATOM   1413 C C    A ALA   A 1 50  ? 22.852 6.100   2.996   0.34 9.15  ?  50  ALA   A C    1 
ATOM   1414 C C    B ALA   A 1 50  ? 22.837 6.180   3.213   0.66 9.43  ?  50  ALA   A C    1 
ATOM   1415 O O    A ALA   A 1 50  ? 23.500 6.514   3.963   0.34 9.30  ?  50  ALA   A O    1 
ATOM   1416 O O    B ALA   A 1 50  ? 23.446 6.590   4.209   0.66 9.76  ?  50  ALA   A O    1 
ATOM   1417 C CB   A ALA   A 1 50  ? 23.838 4.511   1.316   0.34 9.52  ?  50  ALA   A CB   1 
ATOM   1418 C CB   B ALA   A 1 50  ? 23.768 4.598   1.512   0.66 10.06 ?  50  ALA   A CB   1 
ATOM   1419 H H    A ALA   A 1 50  ? 21.509 3.848   1.460   0.34 11.07 ?  50  ALA   A H    1 
ATOM   1420 H H    B ALA   A 1 50  ? 21.462 3.944   1.728   0.66 11.42 ?  50  ALA   A H    1 
ATOM   1421 H HA   A ALA   A 1 50  ? 23.364 4.151   3.275   0.34 10.97 ?  50  ALA   A HA   1 
ATOM   1422 H HA   B ALA   A 1 50  ? 23.373 4.235   3.489   0.66 11.67 ?  50  ALA   A HA   1 
ATOM   1423 H HB1  A ALA   A 1 50  ? 24.709 4.891   1.510   0.34 11.57 ?  50  ALA   A HB1  1 
ATOM   1424 H HB1  B ALA   A 1 50  ? 24.647 4.976   1.672   0.66 12.22 ?  50  ALA   A HB1  1 
ATOM   1425 H HB2  A ALA   A 1 50  ? 23.927 3.573   1.092   0.34 11.57 ?  50  ALA   A HB2  1 
ATOM   1426 H HB2  B ALA   A 1 50  ? 23.844 3.662   1.281   0.66 12.22 ?  50  ALA   A HB2  1 
ATOM   1427 H HB3  A ALA   A 1 50  ? 23.424 4.990   0.580   0.34 11.57 ?  50  ALA   A HB3  1 
ATOM   1428 H HB3  B ALA   A 1 50  ? 23.327 5.083   0.795   0.66 12.22 ?  50  ALA   A HB3  1 
ATOM   1429 N N    A GLY   A 1 51  ? 22.041 6.895   2.299   0.34 9.36  ?  51  GLY   A N    1 
ATOM   1430 N N    B GLY   A 1 51  ? 22.067 6.979   2.472   0.66 10.14 ?  51  GLY   A N    1 
ATOM   1431 C CA   A GLY   A 1 51  ? 21.884 8.285   2.690   0.34 10.05 ?  51  GLY   A CA   1 
ATOM   1432 C CA   B GLY   A 1 51  ? 21.915 8.374   2.843   0.66 10.32 ?  51  GLY   A CA   1 
ATOM   1433 C C    A GLY   A 1 51  ? 21.264 8.435   4.065   0.34 9.99  ?  51  GLY   A C    1 
ATOM   1434 C C    B GLY   A 1 51  ? 21.294 8.528   4.216   0.66 10.08 ?  51  GLY   A C    1 
ATOM   1435 O O    A GLY   A 1 51  ? 21.625 9.336   4.825   0.34 10.39 ?  51  GLY   A O    1 
ATOM   1436 O O    B GLY   A 1 51  ? 21.670 9.420   4.984   0.66 10.96 ?  51  GLY   A O    1 
ATOM   1437 H H    A GLY   A 1 51  ? 21.589 6.657   1.610   0.34 11.38 ?  51  GLY   A H    1 
ATOM   1438 H H    B GLY   A 1 51  ? 21.632 6.740   1.769   0.66 12.32 ?  51  GLY   A H    1 
ATOM   1439 H HA2  A GLY   A 1 51  ? 22.747 8.720   2.702   0.34 12.21 ?  51  GLY   A HA2  1 
ATOM   1440 H HA2  B GLY   A 1 51  ? 22.779 8.811   2.842   0.66 12.53 ?  51  GLY   A HA2  1 
ATOM   1441 H HA3  A GLY   A 1 51  ? 21.316 8.739   2.048   0.34 12.21 ?  51  GLY   A HA3  1 
ATOM   1442 H HA3  B GLY   A 1 51  ? 21.344 8.823   2.190   0.66 12.53 ?  51  GLY   A HA3  1 
ATOM   1443 N N    A ALA   A 1 52  ? 20.312 7.557   4.397   0.34 10.47 ?  52  ALA   A N    1 
ATOM   1444 N N    B ALA   A 1 52  ? 20.320 7.669   4.539   0.66 10.28 ?  52  ALA   A N    1 
ATOM   1445 C CA   A ALA   A 1 52  ? 19.647 7.627   5.695   0.34 10.91 ?  52  ALA   A CA   1 
ATOM   1446 C CA   B ALA   A 1 52  ? 19.647 7.758   5.830   0.66 11.11 ?  52  ALA   A CA   1 
ATOM   1447 C C    A ALA   A 1 52  ? 20.591 7.226   6.823   0.34 10.89 ?  52  ALA   A C    1 
ATOM   1448 C C    B ALA   A 1 52  ? 20.559 7.309   6.971   0.66 10.50 ?  52  ALA   A C    1 
ATOM   1449 O O    A ALA   A 1 52  ? 20.653 7.897   7.859   0.34 11.31 ?  52  ALA   A O    1 
ATOM   1450 O O    B ALA   A 1 52  ? 20.598 7.950   8.028   0.66 11.32 ?  52  ALA   A O    1 
ATOM   1451 C CB   A ALA   A 1 52  ? 18.396 6.745   5.687   0.34 11.60 ?  52  ALA   A CB   1 
ATOM   1452 C CB   B ALA   A 1 52  ? 18.340 6.962   5.800   0.66 12.60 ?  52  ALA   A CB   1 
ATOM   1453 H H    A ALA   A 1 52  ? 20.041 6.916   3.896   0.34 12.72 ?  52  ALA   A H    1 
ATOM   1454 H H    B ALA   A 1 52  ? 20.042 7.034   4.026   0.66 12.49 ?  52  ALA   A H    1 
ATOM   1455 H HA   A ALA   A 1 52  ? 19.366 8.538   5.860   0.34 13.24 ?  52  ALA   A HA   1 
ATOM   1456 H HA   B ALA   A 1 52  ? 19.417 8.683   5.986   0.66 13.48 ?  52  ALA   A HA   1 
ATOM   1457 H HB1  A ALA   A 1 52  ? 17.962 6.799   6.555   0.34 14.07 ?  52  ALA   A HB1  1 
ATOM   1458 H HB1  B ALA   A 1 52  ? 17.892 7.062   6.656   0.66 15.27 ?  52  ALA   A HB1  1 
ATOM   1459 H HB2  A ALA   A 1 52  ? 17.792 7.062   4.997   0.34 14.07 ?  52  ALA   A HB2  1 
ATOM   1460 H HB2  B ALA   A 1 52  ? 17.776 7.306   5.091   0.66 15.27 ?  52  ALA   A HB2  1 
ATOM   1461 H HB3  A ALA   A 1 52  ? 18.654 5.828   5.505   0.34 14.07 ?  52  ALA   A HB3  1 
ATOM   1462 H HB3  B ALA   A 1 52  ? 18.540 6.026   5.639   0.66 15.27 ?  52  ALA   A HB3  1 
ATOM   1463 N N    A LEU   A 1 53  ? 21.333 6.128   6.648   0.34 10.76 ?  53  LEU   A N    1 
ATOM   1464 N N    B LEU   A 1 53  ? 21.300 6.210   6.786   0.66 9.84  ?  53  LEU   A N    1 
ATOM   1465 C CA   A LEU   A 1 53  ? 22.271 5.709   7.686   0.34 11.27 ?  53  LEU   A CA   1 
ATOM   1466 C CA   B LEU   A 1 53  ? 22.276 5.817   7.802   0.66 9.85  ?  53  LEU   A CA   1 
ATOM   1467 C C    A LEU   A 1 53  ? 23.330 6.774   7.922   0.34 11.07 ?  53  LEU   A C    1 
ATOM   1468 C C    B LEU   A 1 53  ? 23.307 6.917   7.993   0.66 9.25  ?  53  LEU   A C    1 
ATOM   1469 O O    A LEU   A 1 53  ? 23.723 7.029   9.064   0.34 11.52 ?  53  LEU   A O    1 
ATOM   1470 O O    B LEU   A 1 53  ? 23.595 7.327   9.120   0.66 9.77  ?  53  LEU   A O    1 
ATOM   1471 C CB   A LEU   A 1 53  ? 22.934 4.382   7.306   0.34 11.74 ?  53  LEU   A CB   1 
ATOM   1472 C CB   B LEU   A 1 53  ? 22.982 4.509   7.422   0.66 9.91  ?  53  LEU   A CB   1 
ATOM   1473 C CG   A LEU   A 1 53  ? 22.036 3.142   7.345   0.34 12.26 ?  53  LEU   A CG   1 
ATOM   1474 C CG   B LEU   A 1 53  ? 22.202 3.190   7.490   0.66 10.52 ?  53  LEU   A CG   1 
ATOM   1475 C CD1  A LEU   A 1 53  ? 22.763 1.936   6.783   0.34 12.67 ?  53  LEU   A CD1  1 
ATOM   1476 C CD1  B LEU   A 1 53  ? 23.020 2.089   6.857   0.66 10.89 ?  53  LEU   A CD1  1 
ATOM   1477 C CD2  A LEU   A 1 53  ? 21.568 2.866   8.764   0.34 12.93 ?  53  LEU   A CD2  1 
ATOM   1478 C CD2  B LEU   A 1 53  ? 21.844 2.815   8.919   0.66 11.55 ?  53  LEU   A CD2  1 
ATOM   1479 H H    A LEU   A 1 53  ? 21.318 5.624   5.954   0.34 13.06 ?  53  LEU   A H    1 
ATOM   1480 H H    B LEU   A 1 53  ? 21.257 5.690   6.103   0.66 11.96 ?  53  LEU   A H    1 
ATOM   1481 H HA   A LEU   A 1 53  ? 21.792 5.578   8.519   0.34 13.68 ?  53  LEU   A HA   1 
ATOM   1482 H HA   B LEU   A 1 53  ? 21.821 5.684   8.645   0.66 11.97 ?  53  LEU   A HA   1 
ATOM   1483 H HB2  A LEU   A 1 53  ? 23.279 4.460   6.402   0.34 14.24 ?  53  LEU   A HB2  1 
ATOM   1484 H HB2  B LEU   A 1 53  ? 23.298 4.600   6.508   0.66 12.04 ?  53  LEU   A HB2  1 
ATOM   1485 H HB3  A LEU   A 1 53  ? 23.673 4.220   7.917   0.34 14.24 ?  53  LEU   A HB3  1 
ATOM   1486 H HB3  B LEU   A 1 53  ? 23.751 4.409   8.007   0.66 12.04 ?  53  LEU   A HB3  1 
ATOM   1487 H HG   A LEU   A 1 53  ? 21.253 3.303   6.795   0.34 14.86 ?  53  LEU   A HG   1 
ATOM   1488 H HG   B LEU   A 1 53  ? 21.380 3.285   6.984   0.66 12.78 ?  53  LEU   A HG   1 
ATOM   1489 H HD11 A LEU   A 1 53  ? 22.176 1.166   6.828   0.34 15.36 ?  53  LEU   A HD11 1 
ATOM   1490 H HD11 B LEU   A 1 53  ? 22.520 1.260   6.914   0.66 13.22 ?  53  LEU   A HD11 1 
ATOM   1491 H HD12 A LEU   A 1 53  ? 23.005 2.116   5.861   0.34 15.36 ?  53  LEU   A HD12 1 
ATOM   1492 H HD12 B LEU   A 1 53  ? 23.185 2.315   5.929   0.66 13.22 ?  53  LEU   A HD12 1 
ATOM   1493 H HD13 A LEU   A 1 53  ? 23.562 1.777   7.310   0.34 15.36 ?  53  LEU   A HD13 1 
ATOM   1494 H HD13 B LEU   A 1 53  ? 23.857 2.007   7.335   0.66 13.22 ?  53  LEU   A HD13 1 
ATOM   1495 H HD21 A LEU   A 1 53  ? 21.094 2.020   8.782   0.34 15.66 ?  53  LEU   A HD21 1 
ATOM   1496 H HD21 B LEU   A 1 53  ? 21.321 1.996   8.910   0.66 14.02 ?  53  LEU   A HD21 1 
ATOM   1497 H HD22 A LEU   A 1 53  ? 22.341 2.823   9.349   0.34 15.66 ?  53  LEU   A HD22 1 
ATOM   1498 H HD22 B LEU   A 1 53  ? 22.656 2.684   9.429   0.66 14.02 ?  53  LEU   A HD22 1 
ATOM   1499 H HD23 A LEU   A 1 53  ? 20.977 3.580   9.051   0.34 15.66 ?  53  LEU   A HD23 1 
ATOM   1500 H HD23 B LEU   A 1 53  ? 21.318 3.533   9.314   0.66 14.02 ?  53  LEU   A HD23 1 
ATOM   1501 N N    A ASN   A 1 54  ? 23.800 7.410   6.851   0.34 10.48 ?  54  ASN   A N    1 
ATOM   1502 N N    B ASN   A 1 54  ? 23.871 7.409   6.894   0.66 9.06  ?  54  ASN   A N    1 
ATOM   1503 C CA   A ASN   A 1 54  ? 24.870 8.386   7.001   0.34 10.34 ?  54  ASN   A CA   1 
ATOM   1504 C CA   B ASN   A 1 54  ? 24.908 8.417   7.026   0.66 9.60  ?  54  ASN   A CA   1 
ATOM   1505 C C    A ASN   A 1 54  ? 24.380 9.641   7.720   0.34 10.48 ?  54  ASN   A C    1 
ATOM   1506 C C    B ASN   A 1 54  ? 24.381 9.654   7.745   0.66 10.16 ?  54  ASN   A C    1 
ATOM   1507 O O    A ASN   A 1 54  ? 25.086 10.193  8.572   0.34 10.92 ?  54  ASN   A O    1 
ATOM   1508 O O    B ASN   A 1 54  ? 25.054 10.210  8.621   0.66 10.82 ?  54  ASN   A O    1 
ATOM   1509 C CB   A ASN   A 1 54  ? 25.448 8.726   5.632   0.34 10.34 ?  54  ASN   A CB   1 
ATOM   1510 C CB   B ASN   A 1 54  ? 25.474 8.791   5.666   0.66 9.72  ?  54  ASN   A CB   1 
ATOM   1511 C CG   A ASN   A 1 54  ? 26.540 9.764   5.714   0.34 10.48 ?  54  ASN   A CG   1 
ATOM   1512 C CG   B ASN   A 1 54  ? 26.464 9.920   5.774   0.66 9.38  ?  54  ASN   A CG   1 
ATOM   1513 O OD1  A ASN   A 1 54  ? 27.531 9.581   6.420   0.34 10.85 ?  54  ASN   A OD1  1 
ATOM   1514 O OD1  B ASN   A 1 54  ? 27.474 9.792   6.473   0.66 9.13  ?  54  ASN   A OD1  1 
ATOM   1515 N ND2  A ASN   A 1 54  ? 26.366 10.864  4.999   0.34 10.45 ?  54  ASN   A ND2  1 
ATOM   1516 N ND2  B ASN   A 1 54  ? 26.168 11.046  5.137   0.66 9.87  ?  54  ASN   A ND2  1 
ATOM   1517 H H    A ASN   A 1 54  ? 23.518 7.293   6.046   0.34 12.72 ?  54  ASN   A H    1 
ATOM   1518 H H    B ASN   A 1 54  ? 23.670 7.184   6.088   0.66 11.02 ?  54  ASN   A H    1 
ATOM   1519 H HA   A ASN   A 1 54  ? 25.574 7.993   7.534   0.34 12.56 ?  54  ASN   A HA   1 
ATOM   1520 H HA   B ASN   A 1 54  ? 25.627 8.052   7.557   0.66 11.67 ?  54  ASN   A HA   1 
ATOM   1521 H HB2  A ASN   A 1 54  ? 25.823 7.919   5.240   0.34 12.56 ?  54  ASN   A HB2  1 
ATOM   1522 H HB2  B ASN   A 1 54  ? 25.932 8.019   5.290   0.66 11.81 ?  54  ASN   A HB2  1 
ATOM   1523 H HB3  A ASN   A 1 54  ? 24.743 9.073   5.065   0.34 12.56 ?  54  ASN   A HB3  1 
ATOM   1524 H HB3  B ASN   A 1 54  ? 24.756 9.070   5.081   0.66 11.81 ?  54  ASN   A HB3  1 
ATOM   1525 H HD21 A ASN   A 1 54  ? 26.963 11.479  5.014   0.34 12.70 ?  54  ASN   A HD21 1 
ATOM   1526 H HD21 B ASN   A 1 54  ? 26.698 11.720  5.176   0.66 11.99 ?  54  ASN   A HD21 1 
ATOM   1527 H HD22 A ASN   A 1 54  ? 25.660 10.954  4.519   0.34 12.70 ?  54  ASN   A HD22 1 
ATOM   1528 H HD22 B ASN   A 1 54  ? 25.444 11.096  4.671   0.66 11.99 ?  54  ASN   A HD22 1 
ATOM   1529 N N    . LYS   A 1 55  ? 23.174 10.105  7.386   1.00 10.63 ?  55  LYS   A N    1 
ATOM   1530 C CA   . LYS   A 1 55  ? 22.597 11.262  8.060   1.00 11.26 ?  55  LYS   A CA   1 
ATOM   1531 C C    . LYS   A 1 55  ? 22.494 11.026  9.561   1.00 11.07 ?  55  LYS   A C    1 
ATOM   1532 O O    . LYS   A 1 55  ? 22.781 11.923  10.367  1.00 11.88 ?  55  LYS   A O    1 
ATOM   1533 C CB   . LYS   A 1 55  ? 21.228 11.577  7.446   1.00 12.48 ?  55  LYS   A CB   1 
ATOM   1534 C CG   . LYS   A 1 55  ? 20.476 12.729  8.095   1.00 14.58 ?  55  LYS   A CG   1 
ATOM   1535 C CD   . LYS   A 1 55  ? 19.166 13.018  7.347   1.00 16.55 ?  55  LYS   A CD   1 
ATOM   1536 C CE   . LYS   A 1 55  ? 18.321 14.077  8.046   1.00 18.30 ?  55  LYS   A CE   1 
ATOM   1537 N NZ   . LYS   A 1 55  ? 16.987 14.278  7.401   1.00 19.15 ?  55  LYS   A NZ   1 
ATOM   1538 H H    A LYS   A 1 55  ? 22.669 9.763   6.778   0.34 12.91 ?  55  LYS   A H    1 
ATOM   1539 H H    B LYS   A 1 55  ? 22.674 9.756   6.778   0.66 12.91 ?  55  LYS   A H    1 
ATOM   1540 H HA   . LYS   A 1 55  ? 23.172 12.030  7.916   1.00 13.66 ?  55  LYS   A HA   1 
ATOM   1541 H HB2  . LYS   A 1 55  ? 21.353 11.808  6.512   1.00 15.13 ?  55  LYS   A HB2  1 
ATOM   1542 H HB3  . LYS   A 1 55  ? 20.667 10.791  7.515   1.00 15.13 ?  55  LYS   A HB3  1 
ATOM   1543 H HG2  . LYS   A 1 55  ? 20.257 12.493  9.011   1.00 17.64 ?  55  LYS   A HG2  1 
ATOM   1544 H HG3  . LYS   A 1 55  ? 21.027 13.526  8.073   1.00 17.64 ?  55  LYS   A HG3  1 
ATOM   1545 H HD2  . LYS   A 1 55  ? 19.379 13.338  6.454   1.00 20.01 ?  55  LYS   A HD2  1 
ATOM   1546 H HD3  . LYS   A 1 55  ? 18.647 12.200  7.291   1.00 20.01 ?  55  LYS   A HD3  1 
ATOM   1547 H HE2  . LYS   A 1 55  ? 18.171 13.803  8.964   1.00 22.11 ?  55  LYS   A HE2  1 
ATOM   1548 H HE3  . LYS   A 1 55  ? 18.795 14.922  8.025   1.00 22.11 ?  55  LYS   A HE3  1 
ATOM   1549 H HZ1  . LYS   A 1 55  ? 16.436 14.695  7.965   1.00 23.13 ?  55  LYS   A HZ1  1 
ATOM   1550 H HZ2  . LYS   A 1 55  ? 17.072 14.777  6.667   1.00 23.13 ?  55  LYS   A HZ2  1 
ATOM   1551 H HZ3  . LYS   A 1 55  ? 16.629 13.494  7.179   1.00 23.13 ?  55  LYS   A HZ3  1 
ATOM   1552 N N    . ALA   A 1 56  ? 22.099 9.813   9.957   1.00 11.72 ?  56  ALA   A N    1 
ATOM   1553 C CA   . ALA   A 1 56  ? 21.969 9.488   11.370  1.00 12.15 ?  56  ALA   A CA   1 
ATOM   1554 C C    . ALA   A 1 56  ? 23.306 9.507   12.097  1.00 12.03 ?  56  ALA   A C    1 
ATOM   1555 O O    . ALA   A 1 56  ? 23.321 9.687   13.317  1.00 13.34 ?  56  ALA   A O    1 
ATOM   1556 C CB   . ALA   A 1 56  ? 21.263 8.139   11.549  1.00 13.34 ?  56  ALA   A CB   1 
ATOM   1557 H H    . ALA   A 1 56  ? 21.907 9.174   9.426   1.00 14.22 ?  56  ALA   A H    1 
ATOM   1558 H HA   . ALA   A 1 56  ? 21.420 10.158  11.791  1.00 14.73 ?  56  ALA   A HA   1 
ATOM   1559 H HB1  . ALA   A 1 56  ? 21.201 7.937   12.496  1.00 16.16 ?  56  ALA   A HB1  1 
ATOM   1560 H HB2  . ALA   A 1 56  ? 20.375 8.199   11.165  1.00 16.16 ?  56  ALA   A HB2  1 
ATOM   1561 H HB3  . ALA   A 1 56  ? 21.773 7.448   11.096  1.00 16.16 ?  56  ALA   A HB3  1 
ATOM   1562 N N    . THR   A 1 57  ? 24.424 9.332   11.380  1.00 11.00 ?  57  THR   A N    1 
ATOM   1563 C CA   . THR   A 1 57  ? 25.764 9.458   11.962  1.00 11.28 ?  57  THR   A CA   1 
ATOM   1564 C C    . THR   A 1 57  ? 26.317 10.878  11.889  1.00 11.37 ?  57  THR   A C    1 
ATOM   1565 O O    . THR   A 1 57  ? 27.504 11.089  12.189  1.00 12.12 ?  57  THR   A O    1 
ATOM   1566 C CB   . THR   A 1 57  ? 26.780 8.509   11.295  1.00 11.29 ?  57  THR   A CB   1 
ATOM   1567 O OG1  . THR   A 1 57  ? 27.174 9.002   10.001  1.00 10.67 ?  57  THR   A OG1  1 
ATOM   1568 C CG2  . THR   A 1 57  ? 26.260 7.087   11.193  1.00 11.23 ?  57  THR   A CG2  1 
ATOM   1569 H H    . THR   A 1 57  ? 24.432 9.113   10.539  1.00 13.35 ?  57  THR   A H    1 
ATOM   1570 H HA   . THR   A 1 57  ? 25.713 9.200   12.897  1.00 13.69 ?  57  THR   A HA   1 
ATOM   1571 H HB   . THR   A 1 57  ? 27.578 8.468   11.858  1.00 13.70 ?  57  THR   A HB   1 
ATOM   1572 H HG1  . THR   A 1 57  ? 26.503 9.070   9.506   1.00 12.95 ?  57  THR   A HG1  1 
ATOM   1573 H HG21 . THR   A 1 57  ? 26.931 6.510   10.788  1.00 13.63 ?  57  THR   A HG21 1 
ATOM   1574 H HG22 . THR   A 1 57  ? 26.047 6.745   12.075  1.00 13.63 ?  57  THR   A HG22 1 
ATOM   1575 H HG23 . THR   A 1 57  ? 25.462 7.065   10.647  1.00 13.63 ?  57  THR   A HG23 1 
ATOM   1576 N N    . ASN   A 1 58  ? 25.501 11.850  11.479  1.00 11.96 ?  58  ASN   A N    1 
ATOM   1577 C CA   . ASN   A 1 58  ? 25.970 13.230  11.380  1.00 12.86 ?  58  ASN   A CA   1 
ATOM   1578 C C    . ASN   A 1 58  ? 27.114 13.358  10.371  1.00 11.52 ?  58  ASN   A C    1 
ATOM   1579 O O    . ASN   A 1 58  ? 28.006 14.193  10.529  1.00 12.46 ?  58  ASN   A O    1 
ATOM   1580 C CB   . ASN   A 1 58  ? 26.349 13.765  12.775  1.00 15.69 ?  58  ASN   A CB   1 
ATOM   1581 C CG   . ASN   A 1 58  ? 26.751 15.221  12.777  1.00 19.49 ?  58  ASN   A CG   1 
ATOM   1582 O OD1  . ASN   A 1 58  ? 26.132 16.041  12.115  1.00 21.12 ?  58  ASN   A OD1  1 
ATOM   1583 N ND2  . ASN   A 1 58  ? 27.793 15.554  13.545  1.00 20.62 ?  58  ASN   A ND2  1 
ATOM   1584 H H    . ASN   A 1 58  ? 24.676 11.727  11.243  1.00 14.50 ?  58  ASN   A H    1 
ATOM   1585 H HA   . ASN   A 1 58  ? 25.234 13.766  11.056  1.00 15.59 ?  58  ASN   A HA   1 
ATOM   1586 H HB2  . ASN   A 1 58  ? 25.581 13.664  13.368  1.00 18.98 ?  58  ASN   A HB2  1 
ATOM   1587 H HB3  . ASN   A 1 58  ? 27.094 13.256  13.121  1.00 18.98 ?  58  ASN   A HB3  1 
ATOM   1588 H HD21 . ASN   A 1 58  ? 28.054 16.373  13.583  1.00 24.90 ?  58  ASN   A HD21 1 
ATOM   1589 H HD22 . ASN   A 1 58  ? 28.195 14.950  14.001  1.00 24.90 ?  58  ASN   A HD22 1 
ATOM   1590 N N    . ASN   A 1 59  ? 27.099 12.534  9.318   1.00 10.76 ?  59  ASN   A N    1 
ATOM   1591 C CA   . ASN   A 1 59  ? 28.083 12.507  8.227   1.00 10.03 ?  59  ASN   A CA   1 
ATOM   1592 C C    . ASN   A 1 59  ? 29.399 11.827  8.620   1.00 9.88  ?  59  ASN   A C    1 
ATOM   1593 O O    . ASN   A 1 59  ? 30.319 11.784  7.796   1.00 10.52 ?  59  ASN   A O    1 
ATOM   1594 C CB   . ASN   A 1 59  ? 28.378 13.894  7.625   1.00 10.62 ?  59  ASN   A CB   1 
ATOM   1595 C CG   . ASN   A 1 59  ? 28.742 13.829  6.157   1.00 10.64 ?  59  ASN   A CG   1 
ATOM   1596 O OD1  . ASN   A 1 59  ? 28.045 13.204  5.361   1.00 11.29 ?  59  ASN   A OD1  1 
ATOM   1597 N ND2  . ASN   A 1 59  ? 29.827 14.489  5.784   1.00 11.85 ?  59  ASN   A ND2  1 
ATOM   1598 H H    . ASN   A 1 59  ? 26.489 11.934  9.208   1.00 13.06 ?  59  ASN   A H    1 
ATOM   1599 H HA   . ASN   A 1 59  ? 27.702 11.979  7.514   1.00 12.18 ?  59  ASN   A HA   1 
ATOM   1600 H HB2  . ASN   A 1 59  ? 27.591 14.454  7.702   1.00 12.90 ?  59  ASN   A HB2  1 
ATOM   1601 H HB3  . ASN   A 1 59  ? 29.124 14.297  8.090   1.00 12.90 ?  59  ASN   A HB3  1 
ATOM   1602 H HD21 . ASN   A 1 59  ? 30.076 14.490  4.957   1.00 14.37 ?  59  ASN   A HD21 1 
ATOM   1603 H HD22 . ASN   A 1 59  ? 30.292 14.923  6.366   1.00 14.37 ?  59  ASN   A HD22 1 
ATOM   1604 N N    . ALA   A 1 60  ? 29.518 11.287  9.830   1.00 10.21 ?  60  ALA   A N    1 
ATOM   1605 C CA   . ALA   A 1 60  ? 30.753 10.598  10.189  1.00 10.52 ?  60  ALA   A CA   1 
ATOM   1606 C C    . ALA   A 1 60  ? 30.981 9.361   9.326   1.00 10.26 ?  60  ALA   A C    1 
ATOM   1607 O O    . ALA   A 1 60  ? 32.131 9.046   8.991   1.00 11.03 ?  60  ALA   A O    1 
ATOM   1608 C CB   . ALA   A 1 60  ? 30.760 10.253  11.677  1.00 11.35 ?  60  ALA   A CB   1 
ATOM   1609 H H    . ALA   A 1 60  ? 28.915 11.301  10.445  1.00 12.41 ?  60  ALA   A H    1 
ATOM   1610 H HA   . ALA   A 1 60  ? 31.493 11.204  10.030  1.00 12.78 ?  60  ALA   A HA   1 
ATOM   1611 H HB1  . ALA   A 1 60  ? 31.590 9.803   11.893  1.00 13.77 ?  60  ALA   A HB1  1 
ATOM   1612 H HB2  . ALA   A 1 60  ? 30.690 11.077  12.192  1.00 13.77 ?  60  ALA   A HB2  1 
ATOM   1613 H HB3  . ALA   A 1 60  ? 30.006 9.679   11.874  1.00 13.77 ?  60  ALA   A HB3  1 
ATOM   1614 N N    . MET   A 1 61  ? 29.911 8.660   8.943   1.00 9.93  ?  61  MET   A N    1 
ATOM   1615 C CA   . MET   A 1 61  ? 30.053 7.526   8.037   1.00 9.77  ?  61  MET   A CA   1 
ATOM   1616 C C    . MET   A 1 61  ? 30.683 7.951   6.709   1.00 9.91  ?  61  MET   A C    1 
ATOM   1617 O O    . MET   A 1 61  ? 31.580 7.267   6.194   1.00 10.32 ?  61  MET   A O    1 
ATOM   1618 C CB   . MET   A 1 61  ? 28.692 6.862   7.826   1.00 10.03 ?  61  MET   A CB   1 
ATOM   1619 C CG   . MET   A 1 61  ? 28.703 5.703   6.853   1.00 10.73 ?  61  MET   A CG   1 
ATOM   1620 S SD   . MET   A 1 61  ? 27.086 4.933   6.657   1.00 11.27 ?  61  MET   A SD   1 
ATOM   1621 C CE   . MET   A 1 61  ? 26.981 4.039   8.211   1.00 13.17 ?  61  MET   A CE   1 
ATOM   1622 H H    . MET   A 1 61  ? 29.100 8.823   9.188   1.00 12.06 ?  61  MET   A H    1 
ATOM   1623 H HA   . MET   A 1 61  ? 30.633 6.870   8.457   1.00 11.87 ?  61  MET   A HA   1 
ATOM   1624 H HB2  . MET   A 1 61  ? 28.374 6.525   8.679   1.00 12.19 ?  61  MET   A HB2  1 
ATOM   1625 H HB3  . MET   A 1 61  ? 28.069 7.521   7.486   1.00 12.19 ?  61  MET   A HB3  1 
ATOM   1626 H HG2  . MET   A 1 61  ? 28.983 6.009   5.979   1.00 13.03 ?  61  MET   A HG2  1 
ATOM   1627 H HG3  . MET   A 1 61  ? 29.310 5.015   7.175   1.00 13.03 ?  61  MET   A HG3  1 
ATOM   1628 H HE1  . MET   A 1 61  ? 26.146 3.546   8.233   1.00 15.95 ?  61  MET   A HE1  1 
ATOM   1629 H HE2  . MET   A 1 61  ? 27.730 3.429   8.274   1.00 15.95 ?  61  MET   A HE2  1 
ATOM   1630 H HE3  . MET   A 1 61  ? 27.008 4.674   8.946   1.00 15.95 ?  61  MET   A HE3  1 
ATOM   1631 N N    . GLN   A 1 62  ? 30.240 9.076   6.146   1.00 9.79  ?  62  GLN   A N    1 
ATOM   1632 C CA   . GLN   A 1 62  ? 30.811 9.543   4.883   1.00 9.92  ?  62  GLN   A CA   1 
ATOM   1633 C C    . GLN   A 1 62  ? 32.280 9.924   5.036   1.00 9.85  ?  62  GLN   A C    1 
ATOM   1634 O O    . GLN   A 1 62  ? 33.098 9.609   4.164   1.00 10.37 ?  62  GLN   A O    1 
ATOM   1635 C CB   . GLN   A 1 62  ? 30.014 10.726  4.335   1.00 10.16 ?  62  GLN   A CB   1 
ATOM   1636 C CG   . GLN   A 1 62  ? 30.405 11.081  2.912   1.00 10.15 ?  62  GLN   A CG   1 
ATOM   1637 C CD   . GLN   A 1 62  ? 30.060 9.941   1.969   1.00 10.27 ?  62  GLN   A CD   1 
ATOM   1638 O OE1  . GLN   A 1 62  ? 28.884 9.645   1.760   1.00 11.05 ?  62  GLN   A OE1  1 
ATOM   1639 N NE2  . GLN   A 1 62  ? 31.071 9.264   1.439   1.00 10.73 ?  62  GLN   A NE2  1 
ATOM   1640 H H    . GLN   A 1 62  ? 29.611 9.569   6.464   1.00 11.89 ?  62  GLN   A H    1 
ATOM   1641 H HA   . GLN   A 1 62  ? 30.762 8.819   4.241   1.00 12.05 ?  62  GLN   A HA   1 
ATOM   1642 H HB2  . GLN   A 1 62  ? 29.076 10.509  4.345   1.00 12.34 ?  62  GLN   A HB2  1 
ATOM   1643 H HB3  . GLN   A 1 62  ? 30.188 11.505  4.891   1.00 12.34 ?  62  GLN   A HB3  1 
ATOM   1644 H HG2  . GLN   A 1 62  ? 29.910 11.865  2.629   1.00 12.33 ?  62  GLN   A HG2  1 
ATOM   1645 H HG3  . GLN   A 1 62  ? 31.359 11.246  2.861   1.00 12.33 ?  62  GLN   A HG3  1 
ATOM   1646 H HE21 . GLN   A 1 62  ? 31.884 9.485   1.618   1.00 13.02 ?  62  GLN   A HE21 1 
ATOM   1647 H HE22 . GLN   A 1 62  ? 30.916 8.602   0.908   1.00 13.02 ?  62  GLN   A HE22 1 
ATOM   1648 N N    . VAL   A 1 63  ? 32.633 10.616  6.122   1.00 10.39 ?  63  VAL   A N    1 
ATOM   1649 C CA   . VAL   A 1 63  ? 34.025 11.005  6.340   1.00 11.23 ?  63  VAL   A CA   1 
ATOM   1650 C C    . VAL   A 1 63  ? 34.922 9.770   6.405   1.00 10.71 ?  63  VAL   A C    1 
ATOM   1651 O O    . VAL   A 1 63  ? 35.978 9.703   5.759   1.00 11.15 ?  63  VAL   A O    1 
ATOM   1652 C CB   . VAL   A 1 63  ? 34.128 11.875  7.606   1.00 12.94 ?  63  VAL   A CB   1 
ATOM   1653 C CG1  . VAL   A 1 63  ? 35.573 12.098  7.991   1.00 14.85 ?  63  VAL   A CG1  1 
ATOM   1654 C CG2  . VAL   A 1 63  ? 33.415 13.210  7.379   1.00 13.10 ?  63  VAL   A CG2  1 
ATOM   1655 H H    . VAL   A 1 63  ? 32.086 10.866  6.739   1.00 12.62 ?  63  VAL   A H    1 
ATOM   1656 H HA   . VAL   A 1 63  ? 34.314 11.546  5.589   1.00 13.63 ?  63  VAL   A HA   1 
ATOM   1657 H HB   . VAL   A 1 63  ? 33.686 11.423  8.343   1.00 15.68 ?  63  VAL   A HB   1 
ATOM   1658 H HG11 . VAL   A 1 63  ? 35.615 12.836  8.619   1.00 17.97 ?  63  VAL   A HG11 1 
ATOM   1659 H HG12 . VAL   A 1 63  ? 35.916 11.293  8.403   1.00 17.97 ?  63  VAL   A HG12 1 
ATOM   1660 H HG13 . VAL   A 1 63  ? 36.077 12.313  7.193   1.00 17.97 ?  63  VAL   A HG13 1 
ATOM   1661 H HG21 . VAL   A 1 63  ? 33.498 13.754  8.180   1.00 15.87 ?  63  VAL   A HG21 1 
ATOM   1662 H HG22 . VAL   A 1 63  ? 33.833 13.666  6.629   1.00 15.87 ?  63  VAL   A HG22 1 
ATOM   1663 H HG23 . VAL   A 1 63  ? 32.481 13.044  7.187   1.00 15.87 ?  63  VAL   A HG23 1 
ATOM   1664 N N    . GLU   A 1 64  ? 34.500 8.764   7.176   1.00 10.55 ?  64  GLU   A N    1 
ATOM   1665 C CA   . GLU   A 1 64  ? 35.259 7.524   7.275   1.00 10.28 ?  64  GLU   A CA   1 
ATOM   1666 C C    . GLU   A 1 64  ? 35.351 6.832   5.921   1.00 10.32 ?  64  GLU   A C    1 
ATOM   1667 O O    . GLU   A 1 64  ? 36.401 6.287   5.549   1.00 10.64 ?  64  GLU   A O    1 
ATOM   1668 C CB   . GLU   A 1 64  ? 34.568 6.610   8.289   1.00 11.33 ?  64  GLU   A CB   1 
ATOM   1669 C CG   . GLU   A 1 64  ? 35.220 5.253   8.437   1.00 11.83 ?  64  GLU   A CG   1 
ATOM   1670 C CD   . GLU   A 1 64  ? 34.347 4.264   9.176   1.00 12.45 ?  64  GLU   A CD   1 
ATOM   1671 O OE1  . GLU   A 1 64  ? 33.110 4.375   9.043   1.00 13.34 ?  64  GLU   A OE1  1 
ATOM   1672 O OE2  . GLU   A 1 64  ? 34.906 3.372   9.869   1.00 12.75 -1 64  GLU   A OE2  1 
ATOM   1673 H H    . GLU   A 1 64  ? 33.769 8.773   7.638   1.00 12.81 ?  64  GLU   A H    1 
ATOM   1674 H HA   . GLU   A 1 64  ? 36.156 7.722   7.595   1.00 12.49 ?  64  GLU   A HA   1 
ATOM   1675 H HB2  . GLU   A 1 64  ? 34.589 7.040   9.162   1.00 13.75 ?  64  GLU   A HB2  1 
ATOM   1676 H HB3  . GLU   A 1 64  ? 33.652 6.478   8.011   1.00 13.75 ?  64  GLU   A HB3  1 
ATOM   1677 H HG2  . GLU   A 1 64  ? 35.405 4.884   7.555   1.00 14.35 ?  64  GLU   A HG2  1 
ATOM   1678 H HG3  . GLU   A 1 64  ? 36.044 5.351   8.930   1.00 14.35 ?  64  GLU   A HG3  1 
ATOM   1679 N N    . SER   A 1 65  ? 34.234 6.817   5.189   1.00 9.90  ?  65  SER   A N    1 
ATOM   1680 C CA   . SER   A 1 65  ? 34.179 6.153   3.894   1.00 10.12 ?  65  SER   A CA   1 
ATOM   1681 C C    . SER   A 1 65  ? 35.101 6.815   2.882   1.00 10.22 ?  65  SER   A C    1 
ATOM   1682 O O    . SER   A 1 65  ? 35.746 6.127   2.081   1.00 11.14 ?  65  SER   A O    1 
ATOM   1683 C CB   . SER   A 1 65  ? 32.747 6.158   3.362   1.00 10.08 ?  65  SER   A CB   1 
ATOM   1684 O OG   . SER   A 1 65  ? 31.895 5.353   4.160   1.00 10.43 ?  65  SER   A OG   1 
ATOM   1685 H H    . SER   A 1 65  ? 33.497 7.184   5.428   1.00 12.03 ?  65  SER   A H    1 
ATOM   1686 H HA   . SER   A 1 65  ? 34.466 5.234   3.997   1.00 12.29 ?  65  SER   A HA   1 
ATOM   1687 H HB2  . SER   A 1 65  ? 32.410 7.063   3.366   1.00 12.25 ?  65  SER   A HB2  1 
ATOM   1688 H HB3  . SER   A 1 65  ? 32.750 5.805   2.460   1.00 12.25 ?  65  SER   A HB3  1 
ATOM   1689 H HG   . SER   A 1 65  ? 31.889 5.641   4.956   1.00 12.67 ?  65  SER   A HG   1 
ATOM   1690 N N    . ASP   A 1 66  ? 35.175 8.149   2.890   1.00 10.38 ?  66  ASP   A N    1 
ATOM   1691 C CA   . ASP   A 1 66  ? 36.041 8.840   1.942   1.00 11.17 ?  66  ASP   A CA   1 
ATOM   1692 C C    . ASP   A 1 66  ? 37.508 8.496   2.197   1.00 10.94 ?  66  ASP   A C    1 
ATOM   1693 O O    . ASP   A 1 66  ? 38.289 8.320   1.253   1.00 11.86 ?  66  ASP   A O    1 
ATOM   1694 C CB   . ASP   A 1 66  ? 35.814 10.348  2.031   1.00 12.47 ?  66  ASP   A CB   1 
ATOM   1695 C CG   . ASP   A 1 66  ? 34.479 10.798  1.414   1.00 13.87 ?  66  ASP   A CG   1 
ATOM   1696 O OD1  . ASP   A 1 66  ? 33.775 9.992   0.764   1.00 14.34 ?  66  ASP   A OD1  1 
ATOM   1697 O OD2  . ASP   A 1 66  ? 34.166 11.999  1.559   1.00 16.75 -1 66  ASP   A OD2  1 
ATOM   1698 H H    . ASP   A 1 66  ? 34.739 8.668   3.425   1.00 12.61 ?  66  ASP   A H    1 
ATOM   1699 H HA   . ASP   A 1 66  ? 35.810 8.553   1.043   1.00 13.56 ?  66  ASP   A HA   1 
ATOM   1700 H HB2  . ASP   A 1 66  ? 35.810 10.612  2.962   1.00 15.11 ?  66  ASP   A HB2  1 
ATOM   1701 H HB3  . ASP   A 1 66  ? 36.533 10.800  1.560   1.00 15.11 ?  66  ASP   A HB3  1 
ATOM   1702 N N    . ASP   A 1 67  ? 37.898 8.376   3.465   1.00 11.39 ?  67  ASP   A N    1 
ATOM   1703 C CA   . ASP   A 1 67  ? 39.255 7.933   3.775   1.00 12.31 ?  67  ASP   A CA   1 
ATOM   1704 C C    . ASP   A 1 67  ? 39.486 6.502   3.306   1.00 12.21 ?  67  ASP   A C    1 
ATOM   1705 O O    . ASP   A 1 67  ? 40.554 6.185   2.766   1.00 12.98 ?  67  ASP   A O    1 
ATOM   1706 C CB   . ASP   A 1 67  ? 39.516 8.073   5.274   1.00 13.62 ?  67  ASP   A CB   1 
ATOM   1707 C CG   . ASP   A 1 67  ? 40.818 7.428   5.700   1.00 14.84 ?  67  ASP   A CG   1 
ATOM   1708 O OD1  . ASP   A 1 67  ? 41.885 8.067   5.565   1.00 18.07 ?  67  ASP   A OD1  1 
ATOM   1709 O OD2  . ASP   A 1 67  ? 40.767 6.267   6.158   1.00 14.52 -1 67  ASP   A OD2  1 
ATOM   1710 H H    . ASP   A 1 67  ? 37.406 8.543   4.150   1.00 13.82 ?  67  ASP   A H    1 
ATOM   1711 H HA   . ASP   A 1 67  ? 39.884 8.504   3.309   1.00 14.92 ?  67  ASP   A HA   1 
ATOM   1712 H HB2  . ASP   A 1 67  ? 39.558 9.013   5.499   1.00 16.49 ?  67  ASP   A HB2  1 
ATOM   1713 H HB3  . ASP   A 1 67  ? 38.790 7.646   5.762   1.00 16.49 ?  67  ASP   A HB3  1 
ATOM   1714 N N    . TYR   A 1 68  ? 38.492 5.625   3.489   1.00 11.70 ?  68  TYR   A N    1 
ATOM   1715 C CA   . TYR   A 1 68  ? 38.621 4.246   3.023   1.00 11.81 ?  68  TYR   A CA   1 
ATOM   1716 C C    . TYR   A 1 68  ? 38.865 4.192   1.517   1.00 11.78 ?  68  TYR   A C    1 
ATOM   1717 O O    . TYR   A 1 68  ? 39.744 3.455   1.046   1.00 12.74 ?  68  TYR   A O    1 
ATOM   1718 C CB   . TYR   A 1 68  ? 37.377 3.416   3.409   1.00 12.24 ?  68  TYR   A CB   1 
ATOM   1719 C CG   . TYR   A 1 68  ? 37.404 2.031   2.776   1.00 13.52 ?  68  TYR   A CG   1 
ATOM   1720 C CD1  . TYR   A 1 68  ? 36.947 1.840   1.478   1.00 14.25 ?  68  TYR   A CD1  1 
ATOM   1721 C CD2  . TYR   A 1 68  ? 37.947 0.943   3.442   1.00 15.06 ?  68  TYR   A CD2  1 
ATOM   1722 C CE1  . TYR   A 1 68  ? 37.027 0.627   0.856   1.00 15.74 ?  68  TYR   A CE1  1 
ATOM   1723 C CE2  . TYR   A 1 68  ? 38.016 -0.308  2.821   1.00 15.48 ?  68  TYR   A CE2  1 
ATOM   1724 C CZ   . TYR   A 1 68  ? 37.560 -0.439  1.528   1.00 15.82 ?  68  TYR   A CZ   1 
ATOM   1725 O OH   . TYR   A 1 68  ? 37.647 -1.649  0.894   1.00 17.12 ?  68  TYR   A OH   1 
ATOM   1726 H H    . TYR   A 1 68  ? 37.741 5.805   3.877   1.00 14.19 ?  68  TYR   A H    1 
ATOM   1727 H HA   . TYR   A 1 68  ? 39.383 3.842   3.460   1.00 14.33 ?  68  TYR   A HA   1 
ATOM   1728 H HB2  . TYR   A 1 68  ? 37.348 3.308   4.375   1.00 14.84 ?  68  TYR   A HB2  1 
ATOM   1729 H HB3  . TYR   A 1 68  ? 36.575 3.876   3.105   1.00 14.84 ?  68  TYR   A HB3  1 
ATOM   1730 H HD1  . TYR   A 1 68  ? 36.600 2.568   1.011   1.00 17.25 ?  68  TYR   A HD1  1 
ATOM   1731 H HD2  . TYR   A 1 68  ? 38.276 1.048   4.303   1.00 18.22 ?  68  TYR   A HD2  1 
ATOM   1732 H HE1  . TYR   A 1 68  ? 36.712 0.524   -0.013  1.00 19.04 ?  68  TYR   A HE1  1 
ATOM   1733 H HE2  . TYR   A 1 68  ? 38.389 -1.034  3.262   1.00 18.73 ?  68  TYR   A HE2  1 
ATOM   1734 H HH   . TYR   A 1 68  ? 37.984 -2.225  1.410   1.00 20.70 ?  68  TYR   A HH   1 
ATOM   1735 N N    . ILE   A 1 69  ? 38.080 4.949   0.741   1.00 11.17 ?  69  ILE   A N    1 
ATOM   1736 C CA   . ILE   A 1 69  ? 38.221 4.933   -0.712  1.00 11.26 ?  69  ILE   A CA   1 
ATOM   1737 C C    . ILE   A 1 69  ? 39.554 5.544   -1.139  1.00 11.44 ?  69  ILE   A C    1 
ATOM   1738 O O    . ILE   A 1 69  ? 40.208 5.057   -2.069  1.00 12.01 ?  69  ILE   A O    1 
ATOM   1739 C CB   . ILE   A 1 69  ? 37.025 5.646   -1.374  1.00 12.08 ?  69  ILE   A CB   1 
ATOM   1740 C CG1  . ILE   A 1 69  ? 35.712 4.909   -1.097  1.00 12.47 ?  69  ILE   A CG1  1 
ATOM   1741 C CG2  . ILE   A 1 69  ? 37.261 5.827   -2.876  1.00 13.39 ?  69  ILE   A CG2  1 
ATOM   1742 C CD1  . ILE   A 1 69  ? 35.557 3.612   -1.857  1.00 13.52 ?  69  ILE   A CD1  1 
ATOM   1743 H H    . ILE   A 1 69  ? 37.461 5.477   1.033   1.00 13.56 ?  69  ILE   A H    1 
ATOM   1744 H HA   . ILE   A 1 69  ? 38.212 4.010   -1.011  1.00 13.66 ?  69  ILE   A HA   1 
ATOM   1745 H HB   . ILE   A 1 69  ? 36.955 6.528   -0.982  1.00 14.65 ?  69  ILE   A HB   1 
ATOM   1746 H HG12 . ILE   A 1 69  ? 35.667 4.706   -0.147  1.00 15.12 ?  69  ILE   A HG12 1 
ATOM   1747 H HG13 . ILE   A 1 69  ? 34.977 5.490   -1.340  1.00 15.12 ?  69  ILE   A HG13 1 
ATOM   1748 H HG21 . ILE   A 1 69  ? 36.413 6.036   -3.306  1.00 16.22 ?  69  ILE   A HG21 1 
ATOM   1749 H HG22 . ILE   A 1 69  ? 37.882 6.564   -3.015  1.00 16.22 ?  69  ILE   A HG22 1 
ATOM   1750 H HG23 . ILE   A 1 69  ? 37.625 5.011   -3.246  1.00 16.22 ?  69  ILE   A HG23 1 
ATOM   1751 H HD11 . ILE   A 1 69  ? 34.760 3.162   -1.549  1.00 16.37 ?  69  ILE   A HD11 1 
ATOM   1752 H HD12 . ILE   A 1 69  ? 35.483 3.809   -2.805  1.00 16.37 ?  69  ILE   A HD12 1 
ATOM   1753 H HD13 . ILE   A 1 69  ? 36.337 3.055   -1.696  1.00 16.37 ?  69  ILE   A HD13 1 
ATOM   1754 N N    . ALA   A 1 70  ? 39.969 6.630   -0.485  1.00 11.97 ?  70  ALA   A N    1 
ATOM   1755 C CA   . ALA   A 1 70  ? 41.246 7.248   -0.828  1.00 12.62 ?  70  ALA   A CA   1 
ATOM   1756 C C    . ALA   A 1 70  ? 42.399 6.267   -0.658  1.00 13.17 ?  70  ALA   A C    1 
ATOM   1757 O O    . ALA   A 1 70  ? 43.375 6.316   -1.412  1.00 15.08 ?  70  ALA   A O    1 
ATOM   1758 C CB   . ALA   A 1 70  ? 41.467 8.500   0.025   1.00 12.89 ?  70  ALA   A CB   1 
ATOM   1759 H H    . ALA   A 1 70  ? 39.531 7.021   0.140   1.00 14.51 ?  70  ALA   A H    1 
ATOM   1760 H HA   . ALA   A 1 70  ? 41.220 7.528   -1.757  1.00 15.30 ?  70  ALA   A HA   1 
ATOM   1761 H HB1  . ALA   A 1 70  ? 42.321 8.897   -0.212  1.00 15.62 ?  70  ALA   A HB1  1 
ATOM   1762 H HB2  . ALA   A 1 70  ? 40.751 9.133   -0.142  1.00 15.62 ?  70  ALA   A HB2  1 
ATOM   1763 H HB3  . ALA   A 1 70  ? 41.472 8.248   0.963   1.00 15.62 ?  70  ALA   A HB3  1 
ATOM   1764 N N    . THR   A 1 71  ? 42.292 5.349   0.297   1.00 12.52 ?  71  THR   A N    1 
ATOM   1765 C CA   . THR   A 1 71  ? 43.342 4.373   0.553   1.00 13.99 ?  71  THR   A CA   1 
ATOM   1766 C C    . THR   A 1 71  ? 43.226 3.141   -0.331  1.00 14.24 ?  71  THR   A C    1 
ATOM   1767 O O    . THR   A 1 71  ? 44.242 2.637   -0.828  1.00 16.78 ?  71  THR   A O    1 
ATOM   1768 C CB   . THR   A 1 71  ? 43.274 3.937   2.017   1.00 16.24 ?  71  THR   A CB   1 
ATOM   1769 O OG1  . THR   A 1 71  ? 43.516 5.070   2.855   1.00 17.81 ?  71  THR   A OG1  1 
ATOM   1770 C CG2  . THR   A 1 71  ? 44.288 2.835   2.321   1.00 17.76 ?  71  THR   A CG2  1 
ATOM   1771 H H    . THR   A 1 71  ? 41.603 5.256   0.800   1.00 15.18 ?  71  THR   A H    1 
ATOM   1772 H HA   . THR   A 1 71  ? 44.205 4.773   0.389   1.00 16.93 ?  71  THR   A HA   1 
ATOM   1773 H HB   . THR   A 1 71  ? 42.390 3.581   2.202   1.00 19.64 ?  71  THR   A HB   1 
ATOM   1774 H HG1  . THR   A 1 71  ? 42.929 5.652   2.718   1.00 21.53 ?  71  THR   A HG1  1 
ATOM   1775 H HG21 . THR   A 1 71  ? 44.417 2.764   3.281   1.00 21.47 ?  71  THR   A HG21 1 
ATOM   1776 H HG22 . THR   A 1 71  ? 43.971 1.982   1.985   1.00 21.47 ?  71  THR   A HG22 1 
ATOM   1777 H HG23 . THR   A 1 71  ? 45.139 3.045   1.906   1.00 21.47 ?  71  THR   A HG23 1 
ATOM   1778 N N    . ASN   A 1 72  ? 42.004 2.634   -0.523  1.00 13.33 ?  72  ASN   A N    1 
ATOM   1779 C CA   . ASN   A 1 72  ? 41.787 1.309   -1.088  1.00 13.54 ?  72  ASN   A CA   1 
ATOM   1780 C C    . ASN   A 1 72  ? 41.161 1.301   -2.472  1.00 13.57 ?  72  ASN   A C    1 
ATOM   1781 O O    . ASN   A 1 72  ? 41.153 0.246   -3.119  1.00 14.80 ?  72  ASN   A O    1 
ATOM   1782 C CB   . ASN   A 1 72  ? 40.901 0.486   -0.145  1.00 14.30 ?  72  ASN   A CB   1 
ATOM   1783 C CG   . ASN   A 1 72  ? 41.519 0.333   1.222   1.00 15.22 ?  72  ASN   A CG   1 
ATOM   1784 O OD1  . ASN   A 1 72  ? 41.062 0.926   2.199   1.00 17.24 ?  72  ASN   A OD1  1 
ATOM   1785 N ND2  . ASN   A 1 72  ? 42.577 -0.444  1.295   1.00 16.16 ?  72  ASN   A ND2  1 
ATOM   1786 H H    . ASN   A 1 72  ? 41.271 3.049   -0.330  1.00 16.15 ?  72  ASN   A H    1 
ATOM   1787 H HA   . ASN   A 1 72  ? 42.636 0.855   -1.157  1.00 16.39 ?  72  ASN   A HA   1 
ATOM   1788 H HB2  . ASN   A 1 72  ? 40.043 0.925   -0.043  1.00 17.31 ?  72  ASN   A HB2  1 
ATOM   1789 H HB3  . ASN   A 1 72  ? 40.776 -0.404  -0.517  1.00 17.31 ?  72  ASN   A HB3  1 
ATOM   1790 H HD21 . ASN   A 1 72  ? 42.973 -0.562  2.050   1.00 19.55 ?  72  ASN   A HD21 1 
ATOM   1791 H HD22 . ASN   A 1 72  ? 42.873 -0.838  0.590   1.00 19.55 ?  72  ASN   A HD22 1 
ATOM   1792 N N    . GLY   A 1 73  ? 40.613 2.419   -2.930  1.00 12.71 ?  73  GLY   A N    1 
ATOM   1793 C CA   . GLY   A 1 73  ? 39.877 2.437   -4.168  1.00 12.84 ?  73  GLY   A CA   1 
ATOM   1794 C C    . GLY   A 1 73  ? 38.490 1.850   -3.999  1.00 12.33 ?  73  GLY   A C    1 
ATOM   1795 O O    . GLY   A 1 73  ? 38.103 1.397   -2.915  1.00 12.89 ?  73  GLY   A O    1 
ATOM   1796 H H    . GLY   A 1 73  ? 40.652 3.186   -2.533  1.00 15.40 ?  73  GLY   A H    1 
ATOM   1797 H HA2  . GLY   A 1 73  ? 39.795 3.355   -4.480  1.00 15.56 ?  73  GLY   A HA2  1 
ATOM   1798 H HA3  . GLY   A 1 73  ? 40.356 1.926   -4.837  1.00 15.56 ?  73  GLY   A HA3  1 
ATOM   1799 N N    . PRO   A 1 74  ? 37.713 1.860   -5.078  1.00 12.97 ?  74  PRO   A N    1 
ATOM   1800 C CA   . PRO   A 1 74  ? 36.316 1.430   -4.988  1.00 13.23 ?  74  PRO   A CA   1 
ATOM   1801 C C    . PRO   A 1 74  ? 36.166 -0.056  -4.692  1.00 12.36 ?  74  PRO   A C    1 
ATOM   1802 O O    . PRO   A 1 74  ? 37.035 -0.884  -4.985  1.00 13.31 ?  74  PRO   A O    1 
ATOM   1803 C CB   . PRO   A 1 74  ? 35.756 1.754   -6.377  1.00 14.64 ?  74  PRO   A CB   1 
ATOM   1804 C CG   . PRO   A 1 74  ? 36.693 2.757   -6.964  1.00 17.00 ?  74  PRO   A CG   1 
ATOM   1805 C CD   . PRO   A 1 74  ? 38.037 2.393   -6.412  1.00 14.72 ?  74  PRO   A CD   1 
ATOM   1806 H HA   . PRO   A 1 74  ? 35.845 1.945   -4.313  1.00 16.02 ?  74  PRO   A HA   1 
ATOM   1807 H HB2  . PRO   A 1 74  ? 35.731 0.951   -6.914  1.00 17.72 ?  74  PRO   A HB2  1 
ATOM   1808 H HB3  . PRO   A 1 74  ? 34.866 2.135   -6.284  1.00 17.72 ?  74  PRO   A HB3  1 
ATOM   1809 H HG2  . PRO   A 1 74  ? 36.688 2.685   -7.930  1.00 20.55 ?  74  PRO   A HG2  1 
ATOM   1810 H HG3  . PRO   A 1 74  ? 36.440 3.650   -6.683  1.00 20.55 ?  74  PRO   A HG3  1 
ATOM   1811 H HD2  . PRO   A 1 74  ? 38.458 1.707   -6.959  1.00 17.82 ?  74  PRO   A HD2  1 
ATOM   1812 H HD3  . PRO   A 1 74  ? 38.600 3.184   -6.349  1.00 17.82 ?  74  PRO   A HD3  1 
ATOM   1813 N N    A LEU   A 1 75  ? 35.035 -0.389  -4.079  0.34 11.76 ?  75  LEU   A N    1 
ATOM   1814 N N    B LEU   A 1 75  ? 35.020 -0.385  -4.103  0.66 11.27 ?  75  LEU   A N    1 
ATOM   1815 C CA   A LEU   A 1 75  ? 34.675 -1.785  -3.924  0.34 11.65 ?  75  LEU   A CA   1 
ATOM   1816 C CA   B LEU   A 1 75  ? 34.629 -1.773  -3.928  0.66 11.04 ?  75  LEU   A CA   1 
ATOM   1817 C C    A LEU   A 1 75  ? 34.359 -2.392  -5.290  0.34 11.38 ?  75  LEU   A C    1 
ATOM   1818 C C    B LEU   A 1 75  ? 34.223 -2.378  -5.268  0.66 11.54 ?  75  LEU   A C    1 
ATOM   1819 O O    A LEU   A 1 75  ? 34.298 -1.704  -6.313  0.34 11.41 ?  75  LEU   A O    1 
ATOM   1820 O O    B LEU   A 1 75  ? 33.939 -1.677  -6.241  0.66 12.51 ?  75  LEU   A O    1 
ATOM   1821 C CB   A LEU   A 1 75  ? 33.461 -1.926  -3.004  0.34 11.92 ?  75  LEU   A CB   1 
ATOM   1822 C CB   B LEU   A 1 75  ? 33.443 -1.885  -2.972  0.66 11.23 ?  75  LEU   A CB   1 
ATOM   1823 C CG   A LEU   A 1 75  ? 33.619 -1.388  -1.580  0.34 12.87 ?  75  LEU   A CG   1 
ATOM   1824 C CG   B LEU   A 1 75  ? 33.656 -1.515  -1.508  0.66 12.99 ?  75  LEU   A CG   1 
ATOM   1825 C CD1  A LEU   A 1 75  ? 32.300 -1.438  -0.809  0.34 13.49 ?  75  LEU   A CD1  1 
ATOM   1826 C CD1  B LEU   A 1 75  ? 32.386 -1.812  -0.735  0.66 14.31 ?  75  LEU   A CD1  1 
ATOM   1827 C CD2  A LEU   A 1 75  ? 34.701 -2.133  -0.827  0.34 13.81 ?  75  LEU   A CD2  1 
ATOM   1828 C CD2  B LEU   A 1 75  ? 34.813 -2.255  -0.899  0.66 16.20 ?  75  LEU   A CD2  1 
ATOM   1829 H H    A LEU   A 1 75  ? 34.469 0.169   -3.745  0.34 14.26 ?  75  LEU   A H    1 
ATOM   1830 H H    B LEU   A 1 75  ? 34.452 0.182   -3.794  0.66 13.67 ?  75  LEU   A H    1 
ATOM   1831 H HA   A LEU   A 1 75  ? 35.422 -2.266  -3.533  0.34 14.13 ?  75  LEU   A HA   1 
ATOM   1832 H HA   B LEU   A 1 75  ? 35.372 -2.279  -3.569  0.66 13.40 ?  75  LEU   A HA   1 
ATOM   1833 H HB2  A LEU   A 1 75  ? 32.719 -1.455  -3.411  0.34 14.45 ?  75  LEU   A HB2  1 
ATOM   1834 H HB2  B LEU   A 1 75  ? 32.735 -1.314  -3.307  0.66 13.62 ?  75  LEU   A HB2  1 
ATOM   1835 H HB3  A LEU   A 1 75  ? 33.245 -2.869  -2.936  0.34 14.45 ?  75  LEU   A HB3  1 
ATOM   1836 H HB3  B LEU   A 1 75  ? 33.140 -2.807  -2.985  0.66 13.62 ?  75  LEU   A HB3  1 
ATOM   1837 H HG   A LEU   A 1 75  ? 33.888 -0.460  -1.632  0.34 15.59 ?  75  LEU   A HG   1 
ATOM   1838 H HG   B LEU   A 1 75  ? 33.841 -0.561  -1.443  0.66 15.74 ?  75  LEU   A HG   1 
ATOM   1839 H HD11 A LEU   A 1 75  ? 32.447 -1.109  0.093   0.34 16.34 ?  75  LEU   A HD11 1 
ATOM   1840 H HD11 B LEU   A 1 75  ? 32.518 -1.566  0.192   0.66 17.33 ?  75  LEU   A HD11 1 
ATOM   1841 H HD12 A LEU   A 1 75  ? 31.646 -0.882  -1.260  0.34 16.34 ?  75  LEU   A HD12 1 
ATOM   1842 H HD12 B LEU   A 1 75  ? 31.662 -1.290  -1.117  0.66 17.33 ?  75  LEU   A HD12 1 
ATOM   1843 H HD13 A LEU   A 1 75  ? 31.985 -2.357  -0.776  0.34 16.34 ?  75  LEU   A HD13 1 
ATOM   1844 H HD13 B LEU   A 1 75  ? 32.190 -2.756  -0.809  0.66 17.33 ?  75  LEU   A HD13 1 
ATOM   1845 H HD21 A LEU   A 1 75  ? 34.729 -1.814  0.088   0.34 16.73 ?  75  LEU   A HD21 1 
ATOM   1846 H HD21 B LEU   A 1 75  ? 34.851 -2.052  0.049   0.66 19.59 ?  75  LEU   A HD21 1 
ATOM   1847 H HD22 A LEU   A 1 75  ? 34.503 -3.083  -0.840  0.34 16.73 ?  75  LEU   A HD22 1 
ATOM   1848 H HD22 B LEU   A 1 75  ? 34.680 -3.206  -1.030  0.66 19.59 ?  75  LEU   A HD22 1 
ATOM   1849 H HD23 A LEU   A 1 75  ? 35.557 -1.970  -1.258  0.34 16.73 ?  75  LEU   A HD23 1 
ATOM   1850 H HD23 B LEU   A 1 75  ? 35.635 -1.972  -1.330  0.66 19.59 ?  75  LEU   A HD23 1 
ATOM   1851 N N    . LYS   A 1 76  ? 34.177 -3.708  -5.293  1.00 11.81 ?  76  LYS   A N    1 
ATOM   1852 C CA   . LYS   A 1 76  ? 33.616 -4.434  -6.423  1.00 12.49 ?  76  LYS   A CA   1 
ATOM   1853 C C    . LYS   A 1 76  ? 32.099 -4.521  -6.265  1.00 11.37 ?  76  LYS   A C    1 
ATOM   1854 O O    . LYS   A 1 76  ? 31.580 -4.591  -5.153  1.00 11.76 ?  76  LYS   A O    1 
ATOM   1855 C CB   . LYS   A 1 76  ? 34.157 -5.871  -6.441  1.00 13.26 ?  76  LYS   A CB   1 
ATOM   1856 C CG   . LYS   A 1 76  ? 35.657 -5.981  -6.675  1.00 14.76 ?  76  LYS   A CG   1 
ATOM   1857 C CD   . LYS   A 1 76  ? 36.188 -7.370  -6.392  1.00 16.09 ?  76  LYS   A CD   1 
ATOM   1858 C CE   . LYS   A 1 76  ? 37.671 -7.443  -6.680  1.00 18.60 ?  76  LYS   A CE   1 
ATOM   1859 N NZ   . LYS   A 1 76  ? 38.224 -8.793  -6.460  1.00 19.71 ?  76  LYS   A NZ   1 
ATOM   1860 H H    A LYS   A 1 76  ? 34.370 -4.217  -4.625  0.34 14.33 ?  76  LYS   A H    1 
ATOM   1861 H H    B LYS   A 1 76  ? 34.469 -4.216  -4.661  0.66 14.33 ?  76  LYS   A H    1 
ATOM   1862 H HA   . LYS   A 1 76  ? 33.839 -3.989  -7.260  1.00 15.13 ?  76  LYS   A HA   1 
ATOM   1863 H HB2  . LYS   A 1 76  ? 33.964 -6.280  -5.587  1.00 16.06 ?  76  LYS   A HB2  1 
ATOM   1864 H HB3  . LYS   A 1 76  ? 33.714 -6.355  -7.151  1.00 16.06 ?  76  LYS   A HB3  1 
ATOM   1865 H HG2  . LYS   A 1 76  ? 35.850 -5.767  -7.603  1.00 17.87 ?  76  LYS   A HG2  1 
ATOM   1866 H HG3  . LYS   A 1 76  ? 36.118 -5.357  -6.090  1.00 17.87 ?  76  LYS   A HG3  1 
ATOM   1867 H HD2  . LYS   A 1 76  ? 36.048 -7.588  -5.458  1.00 19.46 ?  76  LYS   A HD2  1 
ATOM   1868 H HD3  . LYS   A 1 76  ? 35.736 -8.013  -6.962  1.00 19.46 ?  76  LYS   A HD3  1 
ATOM   1869 H HE2  . LYS   A 1 76  ? 37.826 -7.200  -7.606  1.00 22.47 ?  76  LYS   A HE2  1 
ATOM   1870 H HE3  . LYS   A 1 76  ? 38.137 -6.829  -6.091  1.00 22.47 ?  76  LYS   A HE3  1 
ATOM   1871 H HZ1  . LYS   A 1 76  ? 39.095 -8.805  -6.640  1.00 23.80 ?  76  LYS   A HZ1  1 
ATOM   1872 H HZ2  . LYS   A 1 76  ? 38.099 -9.046  -5.616  1.00 23.80 ?  76  LYS   A HZ2  1 
ATOM   1873 H HZ3  . LYS   A 1 76  ? 37.815 -9.384  -6.996  1.00 23.80 ?  76  LYS   A HZ3  1 
ATOM   1874 N N    A VAL   A 1 77  ? 31.392 -4.560  -7.392  0.34 11.92 ?  77  VAL   A N    1 
ATOM   1875 N N    B VAL   A 1 77  ? 31.387 -4.504  -7.391  0.66 12.06 ?  77  VAL   A N    1 
ATOM   1876 C CA   A VAL   A 1 77  ? 29.970 -4.891  -7.342  0.34 12.02 ?  77  VAL   A CA   1 
ATOM   1877 C CA   B VAL   A 1 77  ? 29.986 -4.896  -7.344  0.66 12.30 ?  77  VAL   A CA   1 
ATOM   1878 C C    A VAL   A 1 77  ? 29.839 -6.349  -6.917  0.34 11.49 ?  77  VAL   A C    1 
ATOM   1879 C C    B VAL   A 1 77  ? 29.926 -6.335  -6.851  0.66 11.50 ?  77  VAL   A C    1 
ATOM   1880 O O    A VAL   A 1 77  ? 30.410 -7.248  -7.547  0.34 11.77 ?  77  VAL   A O    1 
ATOM   1881 O O    B VAL   A 1 77  ? 30.640 -7.210  -7.357  0.66 11.97 ?  77  VAL   A O    1 
ATOM   1882 C CB   A VAL   A 1 77  ? 29.280 -4.622  -8.685  0.34 12.86 ?  77  VAL   A CB   1 
ATOM   1883 C CB   B VAL   A 1 77  ? 29.330 -4.732  -8.723  0.66 13.68 ?  77  VAL   A CB   1 
ATOM   1884 C CG1  A VAL   A 1 77  ? 27.820 -5.061  -8.624  0.34 13.55 ?  77  VAL   A CG1  1 
ATOM   1885 C CG1  B VAL   A 1 77  ? 27.854 -5.100  -8.655  0.66 14.73 ?  77  VAL   A CG1  1 
ATOM   1886 C CG2  A VAL   A 1 77  ? 29.371 -3.147  -9.038  0.34 13.41 ?  77  VAL   A CG2  1 
ATOM   1887 C CG2  B VAL   A 1 77  ? 29.515 -3.311  -9.238  0.66 14.29 ?  77  VAL   A CG2  1 
ATOM   1888 H H    A VAL   A 1 77  ? 31.708 -4.410  -8.176  0.34 14.45 ?  77  VAL   A H    1 
ATOM   1889 H H    B VAL   A 1 77  ? 31.690 -4.283  -8.165  0.66 14.63 ?  77  VAL   A H    1 
ATOM   1890 H HA   A VAL   A 1 77  ? 29.540 -4.344  -6.671  0.34 14.57 ?  77  VAL   A HA   1 
ATOM   1891 H HA   B VAL   A 1 77  ? 29.519 -4.336  -6.708  0.66 14.92 ?  77  VAL   A HA   1 
ATOM   1892 H HB   A VAL   A 1 77  ? 29.722 -5.129  -9.386  0.34 15.59 ?  77  VAL   A HB   1 
ATOM   1893 H HB   B VAL   A 1 77  ? 29.766 -5.331  -9.350  0.66 16.57 ?  77  VAL   A HB   1 
ATOM   1894 H HG11 A VAL   A 1 77  ? 27.355 -4.713  -9.400  0.34 16.41 ?  77  VAL   A HG11 1 
ATOM   1895 H HG11 B VAL   A 1 77  ? 27.436 -4.866  -9.497  0.66 17.83 ?  77  VAL   A HG11 1 
ATOM   1896 H HG12 A VAL   A 1 77  ? 27.777 -6.029  -8.620  0.34 16.41 ?  77  VAL   A HG12 1 
ATOM   1897 H HG12 B VAL   A 1 77  ? 27.774 -6.051  -8.495  0.66 17.83 ?  77  VAL   A HG12 1 
ATOM   1898 H HG13 A VAL   A 1 77  ? 27.421 -4.706  -7.814  0.34 16.41 ?  77  VAL   A HG13 1 
ATOM   1899 H HG13 B VAL   A 1 77  ? 27.442 -4.603  -7.931  0.66 17.83 ?  77  VAL   A HG13 1 
ATOM   1900 H HG21 A VAL   A 1 77  ? 28.907 -2.992  -9.874  0.34 16.25 ?  77  VAL   A HG21 1 
ATOM   1901 H HG21 B VAL   A 1 77  ? 28.989 -3.196  -10.042 0.66 17.29 ?  77  VAL   A HG21 1 
ATOM   1902 H HG22 A VAL   A 1 77  ? 28.958 -2.629  -8.329  0.34 16.25 ?  77  VAL   A HG22 1 
ATOM   1903 H HG22 B VAL   A 1 77  ? 29.220 -2.687  -8.555  0.66 17.29 ?  77  VAL   A HG22 1 
ATOM   1904 H HG23 A VAL   A 1 77  ? 30.305 -2.900  -9.126  0.34 16.25 ?  77  VAL   A HG23 1 
ATOM   1905 H HG23 B VAL   A 1 77  ? 30.456 -3.160  -9.435  0.66 17.29 ?  77  VAL   A HG23 1 
ATOM   1906 N N    . GLY   A 1 78  ? 29.090 -6.587  -5.839  1.00 11.27 ?  78  GLY   A N    1 
ATOM   1907 C CA   . GLY   A 1 78  ? 29.040 -7.872  -5.169  1.00 11.54 ?  78  GLY   A CA   1 
ATOM   1908 C C    . GLY   A 1 78  ? 29.945 -7.960  -3.956  1.00 11.13 ?  78  GLY   A C    1 
ATOM   1909 O O    . GLY   A 1 78  ? 29.877 -8.957  -3.219  1.00 11.69 ?  78  GLY   A O    1 
ATOM   1910 H H    A GLY   A 1 78  ? 28.591 -5.992  -5.471  0.34 13.67 ?  78  GLY   A H    1 
ATOM   1911 H H    B GLY   A 1 78  ? 28.528 -6.013  -5.530  0.66 13.67 ?  78  GLY   A H    1 
ATOM   1912 H HA2  . GLY   A 1 78  ? 28.131 -8.046  -4.888  1.00 14.00 ?  78  GLY   A HA2  1 
ATOM   1913 H HA3  . GLY   A 1 78  ? 29.302 -8.567  -5.796  1.00 14.00 ?  78  GLY   A HA3  1 
ATOM   1914 N N    . GLY   A 1 79  ? 30.793 -6.949  -3.733  1.00 11.20 ?  79  GLY   A N    1 
ATOM   1915 C CA   . GLY   A 1 79  ? 31.742 -6.948  -2.642  1.00 11.35 ?  79  GLY   A CA   1 
ATOM   1916 C C    . GLY   A 1 79  ? 31.274 -6.152  -1.435  1.00 10.38 ?  79  GLY   A C    1 
ATOM   1917 O O    . GLY   A 1 79  ? 30.149 -5.649  -1.370  1.00 11.33 ?  79  GLY   A O    1 
ATOM   1918 H H    . GLY   A 1 79  ? 30.846 -6.239  -4.223  1.00 13.60 ?  79  GLY   A H    1 
ATOM   1919 H HA2  . GLY   A 1 79  ? 31.904 -7.868  -2.361  1.00 13.77 ?  79  GLY   A HA2  1 
ATOM   1920 H HA3  . GLY   A 1 79  ? 32.584 -6.575  -2.942  1.00 13.77 ?  79  GLY   A HA3  1 
ATOM   1921 N N    . SER   A 1 80  ? 32.171 -6.048  -0.454  1.00 11.27 ?  80  SER   A N    1 
ATOM   1922 C CA   . SER   A 1 80  ? 31.845 -5.411  0.812   1.00 10.60 ?  80  SER   A CA   1 
ATOM   1923 C C    . SER   A 1 80  ? 33.110 -4.949  1.518   1.00 10.56 ?  80  SER   A C    1 
ATOM   1924 O O    . SER   A 1 80  ? 34.227 -5.376  1.202   1.00 12.15 ?  80  SER   A O    1 
ATOM   1925 C CB   . SER   A 1 80  ? 31.089 -6.370  1.740   1.00 11.32 ?  80  SER   A CB   1 
ATOM   1926 O OG   . SER   A 1 80  ? 31.921 -7.416  2.210   1.00 12.99 ?  80  SER   A OG   1 
ATOM   1927 H H    . SER   A 1 80  ? 32.981 -6.333  -0.504  1.00 13.68 ?  80  SER   A H    1 
ATOM   1928 H HA   . SER   A 1 80  ? 31.285 -4.641  0.633   1.00 12.88 ?  80  SER   A HA   1 
ATOM   1929 H HB2  . SER   A 1 80  ? 30.764 -5.868  2.505   1.00 13.73 ?  80  SER   A HB2  1 
ATOM   1930 H HB3  . SER   A 1 80  ? 30.344 -6.752  1.257   1.00 13.73 ?  80  SER   A HB3  1 
ATOM   1931 H HG   . SER   A 1 80  ? 32.204 -7.871  1.563   1.00 15.74 ?  80  SER   A HG   1 
ATOM   1932 N N    . CYS   A 1 81  ? 32.906 -4.099  2.524   1.00 10.12 ?  81  CYS   A N    1 
ATOM   1933 C CA   . CYS   A 1 81  ? 33.948 -3.801  3.495   1.00 10.53 ?  81  CYS   A CA   1 
ATOM   1934 C C    . CYS   A 1 81  ? 33.298 -3.575  4.851   1.00 10.07 ?  81  CYS   A C    1 
ATOM   1935 O O    . CYS   A 1 81  ? 32.131 -3.173  4.935   1.00 11.39 ?  81  CYS   A O    1 
ATOM   1936 C CB   . CYS   A 1 81  ? 34.811 -2.603  3.078   1.00 11.11 ?  81  CYS   A CB   1 
ATOM   1937 S SG   . CYS   A 1 81  ? 33.911 -1.042  3.085   1.00 11.09 ?  81  CYS   A SG   1 
ATOM   1938 H H    . CYS   A 1 81  ? 32.167 -3.679  2.663   1.00 12.29 ?  81  CYS   A H    1 
ATOM   1939 H HA   . CYS   A 1 81  ? 34.531 -4.570  3.568   1.00 12.78 ?  81  CYS   A HA   1 
ATOM   1940 H HB2  . CYS   A 1 81  ? 35.558 -2.532  3.699   1.00 13.48 ?  81  CYS   A HB2  1 
ATOM   1941 H HB3  . CYS   A 1 81  ? 35.151 -2.763  2.181   1.00 13.48 ?  81  CYS   A HB3  1 
ATOM   1942 H HG   . CYS   A 1 81  ? 34.653 -0.159  2.752   1.00 13.46 ?  81  CYS   A HG   1 
ATOM   1943 N N    . VAL   A 1 82  ? 34.064 -3.838  5.910   1.00 10.55 ?  82  VAL   A N    1 
ATOM   1944 C CA   . VAL   A 1 82  ? 33.642 -3.591  7.282   1.00 11.10 ?  82  VAL   A CA   1 
ATOM   1945 C C    . VAL   A 1 82  ? 34.235 -2.273  7.750   1.00 11.07 ?  82  VAL   A C    1 
ATOM   1946 O O    . VAL   A 1 82  ? 35.459 -2.098  7.752   1.00 12.00 ?  82  VAL   A O    1 
ATOM   1947 C CB   . VAL   A 1 82  ? 34.068 -4.725  8.226   1.00 12.67 ?  82  VAL   A CB   1 
ATOM   1948 C CG1  . VAL   A 1 82  ? 33.601 -4.434  9.646   1.00 14.31 ?  82  VAL   A CG1  1 
ATOM   1949 C CG2  . VAL   A 1 82  ? 33.537 -6.063  7.750   1.00 13.74 ?  82  VAL   A CG2  1 
ATOM   1950 H H    . VAL   A 1 82  ? 34.858 -4.180  5.851   1.00 12.82 ?  82  VAL   A H    1 
ATOM   1951 H HA   . VAL   A 1 82  ? 32.676 -3.515  7.309   1.00 13.47 ?  82  VAL   A HA   1 
ATOM   1952 H HB   . VAL   A 1 82  ? 35.035 -4.772  8.240   1.00 15.36 ?  82  VAL   A HB   1 
ATOM   1953 H HG11 . VAL   A 1 82  ? 33.694 -5.236  10.181  1.00 17.32 ?  82  VAL   A HG11 1 
ATOM   1954 H HG12 . VAL   A 1 82  ? 34.141 -3.721  10.024  1.00 17.32 ?  82  VAL   A HG12 1 
ATOM   1955 H HG13 . VAL   A 1 82  ? 32.667 -4.161  9.623   1.00 17.32 ?  82  VAL   A HG13 1 
ATOM   1956 H HG21 . VAL   A 1 82  ? 33.785 -6.744  8.393   1.00 16.64 ?  82  VAL   A HG21 1 
ATOM   1957 H HG22 . VAL   A 1 82  ? 32.573 -6.011  7.674   1.00 16.64 ?  82  VAL   A HG22 1 
ATOM   1958 H HG23 . VAL   A 1 82  ? 33.929 -6.264  6.886   1.00 16.64 ?  82  VAL   A HG23 1 
ATOM   1959 N N    . LEU   A 1 83  ? 33.371 -1.352  8.163   1.00 10.80 ?  83  LEU   A N    1 
ATOM   1960 C CA   . LEU   A 1 83  ? 33.775 -0.082  8.743   1.00 10.73 ?  83  LEU   A CA   1 
ATOM   1961 C C    . LEU   A 1 83  ? 33.049 0.097   10.071  1.00 10.55 ?  83  LEU   A C    1 
ATOM   1962 O O    . LEU   A 1 83  ? 32.323 -0.792  10.528  1.00 11.68 ?  83  LEU   A O    1 
ATOM   1963 C CB   . LEU   A 1 83  ? 33.521 1.070   7.761   1.00 11.30 ?  83  LEU   A CB   1 
ATOM   1964 C CG   . LEU   A 1 83  ? 34.422 1.072   6.519   1.00 12.18 ?  83  LEU   A CG   1 
ATOM   1965 C CD1  . LEU   A 1 83  ? 33.969 2.125   5.530   1.00 12.54 ?  83  LEU   A CD1  1 
ATOM   1966 C CD2  . LEU   A 1 83  ? 35.888 1.288   6.885   1.00 12.76 ?  83  LEU   A CD2  1 
ATOM   1967 H H    . LEU   A 1 83  ? 32.523 -1.448  8.110   1.00 13.11 ?  83  LEU   A H    1 
ATOM   1968 H HA   . LEU   A 1 83  ? 34.727 -0.100  8.930   1.00 13.03 ?  83  LEU   A HA   1 
ATOM   1969 H HB2  . LEU   A 1 83  ? 32.603 1.024   7.453   1.00 13.71 ?  83  LEU   A HB2  1 
ATOM   1970 H HB3  . LEU   A 1 83  ? 33.662 1.915   8.221   1.00 13.71 ?  83  LEU   A HB3  1 
ATOM   1971 H HG   . LEU   A 1 83  ? 34.350 0.212   6.084   1.00 14.76 ?  83  LEU   A HG   1 
ATOM   1972 H HD11 . LEU   A 1 83  ? 34.549 2.097   4.754   1.00 15.20 ?  83  LEU   A HD11 1 
ATOM   1973 H HD12 . LEU   A 1 83  ? 33.054 1.930   5.265   1.00 15.20 ?  83  LEU   A HD12 1 
ATOM   1974 H HD13 . LEU   A 1 83  ? 34.014 2.995   5.951   1.00 15.20 ?  83  LEU   A HD13 1 
ATOM   1975 H HD21 . LEU   A 1 83  ? 36.400 1.426   6.069   1.00 15.46 ?  83  LEU   A HD21 1 
ATOM   1976 H HD22 . LEU   A 1 83  ? 35.962 2.073   7.452   1.00 15.46 ?  83  LEU   A HD22 1 
ATOM   1977 H HD23 . LEU   A 1 83  ? 36.217 0.508   7.353   1.00 15.46 ?  83  LEU   A HD23 1 
ATOM   1978 N N    . SER   A 1 84  ? 33.243 1.251   10.702  1.00 11.74 ?  84  SER   A N    1 
ATOM   1979 C CA   . SER   A 1 84  ? 32.585 1.502   11.974  1.00 11.94 ?  84  SER   A CA   1 
ATOM   1980 C C    . SER   A 1 84  ? 31.071 1.608   11.808  1.00 11.88 ?  84  SER   A C    1 
ATOM   1981 O O    . SER   A 1 84  ? 30.565 2.056   10.780  1.00 11.76 ?  84  SER   A O    1 
ATOM   1982 C CB   . SER   A 1 84  ? 33.093 2.817   12.559  1.00 12.91 ?  84  SER   A CB   1 
ATOM   1983 O OG   . SER   A 1 84  ? 32.454 3.108   13.784  1.00 14.07 ?  84  SER   A OG   1 
ATOM   1984 H H    . SER   A 1 84  ? 33.733 1.900   10.411  1.00 14.24 ?  84  SER   A H    1 
ATOM   1985 H HA   . SER   A 1 84  ? 32.788 0.777   12.590  1.00 14.48 ?  84  SER   A HA   1 
ATOM   1986 H HB2  . SER   A 1 84  ? 34.052 2.748   12.701  1.00 15.64 ?  84  SER   A HB2  1 
ATOM   1987 H HB3  . SER   A 1 84  ? 32.903 3.532   11.933  1.00 15.64 ?  84  SER   A HB3  1 
ATOM   1988 H HG   . SER   A 1 84  ? 32.755 3.827   14.099  1.00 17.04 ?  84  SER   A HG   1 
ATOM   1989 N N    A GLY   A 1 85  ? 30.350 1.201   12.850  0.34 12.48 ?  85  GLY   A N    1 
ATOM   1990 N N    B GLY   A 1 85  ? 30.344 1.199   12.845  0.66 12.85 ?  85  GLY   A N    1 
ATOM   1991 C CA   A GLY   A 1 85  ? 28.927 1.438   12.951  0.34 12.90 ?  85  GLY   A CA   1 
ATOM   1992 C CA   B GLY   A 1 85  ? 28.922 1.452   12.924  0.66 13.31 ?  85  GLY   A CA   1 
ATOM   1993 C C    A GLY   A 1 85  ? 28.560 2.766   13.572  0.34 12.88 ?  85  GLY   A C    1 
ATOM   1994 C C    B GLY   A 1 85  ? 28.557 2.759   13.591  0.66 13.07 ?  85  GLY   A C    1 
ATOM   1995 O O    A GLY   A 1 85  ? 27.373 3.105   13.636  0.34 13.30 ?  85  GLY   A O    1 
ATOM   1996 O O    B GLY   A 1 85  ? 27.368 3.071   13.720  0.66 13.44 ?  85  GLY   A O    1 
ATOM   1997 H H    A GLY   A 1 85  ? 30.674 0.771   13.523  0.34 15.13 ?  85  GLY   A H    1 
ATOM   1998 H H    B GLY   A 1 85  ? 30.657 0.762   13.518  0.66 15.57 ?  85  GLY   A H    1 
ATOM   1999 H HA2  A GLY   A 1 85  ? 28.539 1.405   12.063  0.34 15.63 ?  85  GLY   A HA2  1 
ATOM   2000 H HA2  B GLY   A 1 85  ? 28.551 1.452   12.026  0.66 16.12 ?  85  GLY   A HA2  1 
ATOM   2001 H HA3  A GLY   A 1 85  ? 28.524 0.735   13.482  0.34 15.63 ?  85  GLY   A HA3  1 
ATOM   2002 H HA3  B GLY   A 1 85  ? 28.497 0.740   13.422  0.66 16.12 ?  85  GLY   A HA3  1 
ATOM   2003 N N    . HIS   A 1 86  ? 29.545 3.532   14.033  1.00 12.84 ?  86  HIS   A N    1 
ATOM   2004 C CA   . HIS   A 1 86  ? 29.328 4.867   14.605  1.00 12.99 ?  86  HIS   A CA   1 
ATOM   2005 C C    . HIS   A 1 86  ? 28.336 4.757   15.756  1.00 13.77 ?  86  HIS   A C    1 
ATOM   2006 O O    . HIS   A 1 86  ? 28.516 3.884   16.621  1.00 15.19 ?  86  HIS   A O    1 
ATOM   2007 C CB   . HIS   A 1 86  ? 28.966 5.847   13.492  1.00 12.95 ?  86  HIS   A CB   1 
ATOM   2008 C CG   . HIS   A 1 86  ? 30.029 5.934   12.453  1.00 12.96 ?  86  HIS   A CG   1 
ATOM   2009 N ND1  . HIS   A 1 86  ? 31.121 6.765   12.583  1.00 14.16 ?  86  HIS   A ND1  1 
ATOM   2010 C CD2  . HIS   A 1 86  ? 30.217 5.229   11.314  1.00 12.37 ?  86  HIS   A CD2  1 
ATOM   2011 C CE1  . HIS   A 1 86  ? 31.923 6.585   11.548  1.00 14.09 ?  86  HIS   A CE1  1 
ATOM   2012 N NE2  . HIS   A 1 86  ? 31.400 5.658   10.767  1.00 13.03 ?  86  HIS   A NE2  1 
ATOM   2013 H H    A HIS   A 1 86  ? 30.370 3.305   14.021  0.34 15.56 ?  86  HIS   A H    1 
ATOM   2014 H H    B HIS   A 1 86  ? 30.370 3.306   14.019  0.66 15.56 ?  86  HIS   A H    1 
ATOM   2015 H HA   . HIS   A 1 86  ? 30.162 5.176   14.976  1.00 15.74 ?  86  HIS   A HA   1 
ATOM   2016 H HB2  . HIS   A 1 86  ? 28.142 5.564   13.060  1.00 15.69 ?  86  HIS   A HB2  1 
ATOM   2017 H HB3  . HIS   A 1 86  ? 28.846 6.738   13.869  1.00 15.69 ?  86  HIS   A HB3  1 
ATOM   2018 H HD2  . HIS   A 1 86  ? 29.653 4.573   10.962  1.00 15.00 ?  86  HIS   A HD2  1 
ATOM   2019 H HE1  . HIS   A 1 86  ? 32.719 7.040   11.385  1.00 17.06 ?  86  HIS   A HE1  1 
ATOM   2020 H HE2  . HIS   A 1 86  ? 31.741 5.376   10.021  1.00 15.79 ?  86  HIS   A HE2  1 
ATOM   2021 N N    A ASN   A 1 87  ? 27.300 5.590   15.812  0.34 14.94 ?  87  ASN   A N    1 
ATOM   2022 N N    B ASN   A 1 87  ? 27.319 5.610   15.818  0.66 14.74 ?  87  ASN   A N    1 
ATOM   2023 C CA   A ASN   A 1 87  ? 26.303 5.529   16.873  0.34 16.14 ?  87  ASN   A CA   1 
ATOM   2024 C CA   B ASN   A 1 87  ? 26.337 5.616   16.887  0.66 15.85 ?  87  ASN   A CA   1 
ATOM   2025 C C    A ASN   A 1 87  ? 25.214 4.496   16.612  0.34 16.87 ?  87  ASN   A C    1 
ATOM   2026 C C    B ASN   A 1 87  ? 25.178 4.663   16.632  0.66 16.40 ?  87  ASN   A C    1 
ATOM   2027 O O    A ASN   A 1 87  ? 24.277 4.399   17.411  0.34 18.42 ?  87  ASN   A O    1 
ATOM   2028 O O    B ASN   A 1 87  ? 24.220 4.663   17.409  0.66 18.21 ?  87  ASN   A O    1 
ATOM   2029 C CB   A ASN   A 1 87  ? 25.660 6.908   17.067  0.34 16.80 ?  87  ASN   A CB   1 
ATOM   2030 C CB   B ASN   A 1 87  ? 25.780 7.033   17.062  0.66 16.91 ?  87  ASN   A CB   1 
ATOM   2031 C CG   A ASN   A 1 87  ? 25.254 7.555   15.752  0.34 17.19 ?  87  ASN   A CG   1 
ATOM   2032 C CG   B ASN   A 1 87  ? 25.207 7.602   15.766  0.66 17.71 ?  87  ASN   A CG   1 
ATOM   2033 O OD1  A ASN   A 1 87  ? 25.979 7.476   14.759  0.34 17.47 ?  87  ASN   A OD1  1 
ATOM   2034 O OD1  B ASN   A 1 87  ? 25.767 7.412   14.686  0.66 17.81 ?  87  ASN   A OD1  1 
ATOM   2035 N ND2  A ASN   A 1 87  ? 24.092 8.193   15.738  0.34 18.06 ?  87  ASN   A ND2  1 
ATOM   2036 N ND2  B ASN   A 1 87  ? 24.085 8.295   15.871  0.66 19.56 ?  87  ASN   A ND2  1 
ATOM   2037 H H    A ASN   A 1 87  ? 27.150 6.207   15.231  0.34 18.08 ?  87  ASN   A H    1 
ATOM   2038 H H    B ASN   A 1 87  ? 27.173 6.220   15.229  0.66 17.83 ?  87  ASN   A H    1 
ATOM   2039 H HA   A ASN   A 1 87  ? 26.739 5.284   17.704  0.34 19.52 ?  87  ASN   A HA   1 
ATOM   2040 H HA   B ASN   A 1 87  ? 26.764 5.348   17.720  0.66 19.17 ?  87  ASN   A HA   1 
ATOM   2041 H HB2  A ASN   A 1 87  ? 24.862 6.813   17.615  0.34 20.32 ?  87  ASN   A HB2  1 
ATOM   2042 H HB2  B ASN   A 1 87  ? 25.067 7.014   17.726  0.66 20.44 ?  87  ASN   A HB2  1 
ATOM   2043 H HB3  A ASN   A 1 87  ? 26.295 7.494   17.506  0.34 20.32 ?  87  ASN   A HB3  1 
ATOM   2044 H HB3  B ASN   A 1 87  ? 26.494 7.615   17.363  0.66 20.44 ?  87  ASN   A HB3  1 
ATOM   2045 H HD21 A ASN   A 1 87  ? 23.822 8.574   15.017  0.34 21.82 ?  87  ASN   A HD21 1 
ATOM   2046 H HD21 B ASN   A 1 87  ? 23.728 8.630   15.166  0.66 23.63 ?  87  ASN   A HD21 1 
ATOM   2047 H HD22 A ASN   A 1 87  ? 23.613 8.232   16.451  0.34 21.82 ?  87  ASN   A HD22 1 
ATOM   2048 H HD22 B ASN   A 1 87  ? 23.719 8.409   16.639  0.66 23.63 ?  87  ASN   A HD22 1 
ATOM   2049 N N    A LEU   A 1 88  ? 25.320 3.713   15.541  0.34 16.01 ?  88  LEU   A N    1 
ATOM   2050 N N    B LEU   A 1 88  ? 25.234 3.863   15.565  0.66 14.83 ?  88  LEU   A N    1 
ATOM   2051 C CA   A LEU   A 1 88  ? 24.243 2.824   15.122  0.34 15.34 ?  88  LEU   A CA   1 
ATOM   2052 C CA   B LEU   A 1 88  ? 24.116 3.009   15.179  0.66 14.73 ?  88  LEU   A CA   1 
ATOM   2053 C C    A LEU   A 1 88  ? 24.499 1.357   15.427  0.34 15.49 ?  88  LEU   A C    1 
ATOM   2054 C C    B LEU   A 1 88  ? 24.339 1.525   15.439  0.66 14.31 ?  88  LEU   A C    1 
ATOM   2055 O O    A LEU   A 1 88  ? 23.543 0.606   15.634  0.34 16.34 ?  88  LEU   A O    1 
ATOM   2056 O O    B LEU   A 1 88  ? 23.358 0.784   15.557  0.66 15.31 ?  88  LEU   A O    1 
ATOM   2057 C CB   A LEU   A 1 88  ? 24.005 2.965   13.615  0.34 14.83 ?  88  LEU   A CB   1 
ATOM   2058 C CB   B LEU   A 1 88  ? 23.812 3.195   13.687  0.66 15.02 ?  88  LEU   A CB   1 
ATOM   2059 C CG   A LEU   A 1 88  ? 23.758 4.378   13.086  0.34 14.97 ?  88  LEU   A CG   1 
ATOM   2060 C CG   B LEU   A 1 88  ? 23.544 4.639   13.259  0.66 15.92 ?  88  LEU   A CG   1 
ATOM   2061 C CD1  A LEU   A 1 88  ? 23.651 4.352   11.573  0.34 14.88 ?  88  LEU   A CD1  1 
ATOM   2062 C CD1  B LEU   A 1 88  ? 23.317 4.737   11.756  0.66 16.25 ?  88  LEU   A CD1  1 
ATOM   2063 C CD2  A LEU   A 1 88  ? 22.504 4.971   13.705  0.34 16.07 ?  88  LEU   A CD2  1 
ATOM   2064 C CD2  B LEU   A 1 88  ? 22.357 5.216   14.019  0.66 17.14 ?  88  LEU   A CD2  1 
ATOM   2065 H H    A LEU   A 1 88  ? 26.022 3.667   15.046  0.34 19.37 ?  88  LEU   A H    1 
ATOM   2066 H H    B LEU   A 1 88  ? 25.914 3.802   15.043  0.66 17.94 ?  88  LEU   A H    1 
ATOM   2067 H HA   A LEU   A 1 88  ? 23.427 3.088   15.572  0.34 18.56 ?  88  LEU   A HA   1 
ATOM   2068 H HA   B LEU   A 1 88  ? 23.329 3.285   15.675  0.66 17.83 ?  88  LEU   A HA   1 
ATOM   2069 H HB2  A LEU   A 1 88  ? 24.781 2.617   13.153  0.34 17.95 ?  88  LEU   A HB2  1 
ATOM   2070 H HB2  B LEU   A 1 88  ? 24.566 2.872   13.173  0.66 18.18 ?  88  LEU   A HB2  1 
ATOM   2071 H HB3  A LEU   A 1 88  ? 23.227 2.433   13.385  0.34 17.95 ?  88  LEU   A HB3  1 
ATOM   2072 H HB3  B LEU   A 1 88  ? 23.021 2.675   13.467  0.66 18.18 ?  88  LEU   A HB3  1 
ATOM   2073 H HG   A LEU   A 1 88  ? 24.508 4.947   13.322  0.34 18.12 ?  88  LEU   A HG   1 
ATOM   2074 H HG   B LEU   A 1 88  ? 24.321 5.176   13.471  0.66 19.26 ?  88  LEU   A HG   1 
ATOM   2075 H HD11 A LEU   A 1 88  ? 23.526 5.258   11.248  0.34 18.00 ?  88  LEU   A HD11 1 
ATOM   2076 H HD11 B LEU   A 1 88  ? 23.186 5.669   11.515  0.66 19.65 ?  88  LEU   A HD11 1 
ATOM   2077 H HD12 A LEU   A 1 88  ? 24.466 3.976   11.206  0.34 18.00 ?  88  LEU   A HD12 1 
ATOM   2078 H HD12 B LEU   A 1 88  ? 24.093 4.383   11.294  0.66 19.65 ?  88  LEU   A HD12 1 
ATOM   2079 H HD13 A LEU   A 1 88  ? 22.891 3.803   11.323  0.34 18.00 ?  88  LEU   A HD13 1 
ATOM   2080 H HD13 B LEU   A 1 88  ? 22.528 4.223   11.519  0.66 19.65 ?  88  LEU   A HD13 1 
ATOM   2081 H HD21 A LEU   A 1 88  ? 22.331 5.836   13.301  0.34 19.43 ?  88  LEU   A HD21 1 
ATOM   2082 H HD21 B LEU   A 1 88  ? 22.122 6.070   13.627  0.66 20.72 ?  88  LEU   A HD21 1 
ATOM   2083 H HD22 A LEU   A 1 88  ? 21.759 4.374   13.541  0.34 19.43 ?  88  LEU   A HD22 1 
ATOM   2084 H HD22 B LEU   A 1 88  ? 21.614 4.600   13.950  0.66 20.72 ?  88  LEU   A HD22 1 
ATOM   2085 H HD23 A LEU   A 1 88  ? 22.644 5.075   14.659  0.34 19.43 ?  88  LEU   A HD23 1 
ATOM   2086 H HD23 B LEU   A 1 88  ? 22.610 5.333   14.947  0.66 20.72 ?  88  LEU   A HD23 1 
ATOM   2087 N N    A ALA   A 1 89  ? 25.758 0.934   15.456  0.34 15.10 ?  89  ALA   A N    1 
ATOM   2088 N N    B ALA   A 1 89  ? 25.586 1.079   15.520  0.66 13.65 ?  89  ALA   A N    1 
ATOM   2089 C CA   A ALA   A 1 89  ? 26.118 -0.471  15.592  0.34 14.81 ?  89  ALA   A CA   1 
ATOM   2090 C CA   B ALA   A 1 89  ? 25.932 -0.332  15.601  0.66 13.59 ?  89  ALA   A CA   1 
ATOM   2091 C C    A ALA   A 1 89  ? 27.601 -0.531  15.922  0.34 14.92 ?  89  ALA   A C    1 
ATOM   2092 C C    B ALA   A 1 89  ? 27.415 -0.399  15.909  0.66 13.54 ?  89  ALA   A C    1 
ATOM   2093 O O    A ALA   A 1 89  ? 28.300 0.484   15.894  0.34 15.39 ?  89  ALA   A O    1 
ATOM   2094 O O    B ALA   A 1 89  ? 28.128 0.593   15.760  0.66 14.36 ?  89  ALA   A O    1 
ATOM   2095 C CB   A ALA   A 1 89  ? 25.830 -1.232  14.298  0.34 14.53 ?  89  ALA   A CB   1 
ATOM   2096 C CB   B ALA   A 1 89  ? 25.654 -1.036  14.273  0.66 13.42 ?  89  ALA   A CB   1 
ATOM   2097 H H    A ALA   A 1 89  ? 26.435 1.459   15.396  0.34 18.27 ?  89  ALA   A H    1 
ATOM   2098 H H    B ALA   A 1 89  ? 26.268 1.600   15.520  0.66 16.54 ?  89  ALA   A H    1 
ATOM   2099 H HA   A ALA   A 1 89  ? 25.612 -0.873  16.315  0.34 17.92 ?  89  ALA   A HA   1 
ATOM   2100 H HA   B ALA   A 1 89  ? 25.423 -0.759  16.311  0.66 16.46 ?  89  ALA   A HA   1 
ATOM   2101 H HB1  A ALA   A 1 89  ? 26.107 -2.154  14.407  0.34 17.59 ?  89  ALA   A HB1  1 
ATOM   2102 H HB1  B ALA   A 1 89  ? 25.895 -1.970  14.357  0.66 16.25 ?  89  ALA   A HB1  1 
ATOM   2103 H HB2  A ALA   A 1 89  ? 24.879 -1.190  14.109  0.34 17.59 ?  89  ALA   A HB2  1 
ATOM   2104 H HB2  B ALA   A 1 89  ? 24.707 -0.956  14.062  0.66 16.25 ?  89  ALA   A HB2  1 
ATOM   2105 H HB3  A ALA   A 1 89  ? 26.329 -0.821  13.574  0.34 17.59 ?  89  ALA   A HB3  1 
ATOM   2106 H HB3  B ALA   A 1 89  ? 26.182 -0.616  13.577  0.66 16.25 ?  89  ALA   A HB3  1 
ATOM   2107 N N    A LYS   A 1 90  ? 28.082 -1.733  16.239  0.34 15.49 ?  90  LYS   A N    1 
ATOM   2108 N N    B LYS   A 1 90  ? 27.888 -1.568  16.332  0.66 13.41 ?  90  LYS   A N    1 
ATOM   2109 C CA   A LYS   A 1 90  ? 29.522 -1.903  16.404  0.34 16.61 ?  90  LYS   A CA   1 
ATOM   2110 C CA   B LYS   A 1 90  ? 29.331 -1.714  16.490  0.66 14.08 ?  90  LYS   A CA   1 
ATOM   2111 C C    A LYS   A 1 90  ? 30.238 -1.774  15.065  0.34 15.97 ?  90  LYS   A C    1 
ATOM   2112 C C    B LYS   A 1 90  ? 30.038 -1.527  15.150  0.66 13.03 ?  90  LYS   A C    1 
ATOM   2113 O O    A LYS   A 1 90  ? 31.245 -1.062  14.951  0.34 16.63 ?  90  LYS   A O    1 
ATOM   2114 O O    B LYS   A 1 90  ? 30.964 -0.708  15.022  0.66 13.97 ?  90  LYS   A O    1 
ATOM   2115 C CB   A LYS   A 1 90  ? 29.837 -3.248  17.056  0.34 18.75 ?  90  LYS   A CB   1 
ATOM   2116 C CB   B LYS   A 1 90  ? 29.667 -3.072  17.105  0.66 16.73 ?  90  LYS   A CB   1 
ATOM   2117 C CG   A LYS   A 1 90  ? 31.311 -3.416  17.396  0.34 21.61 ?  90  LYS   A CG   1 
ATOM   2118 C CG   B LYS   A 1 90  ? 31.132 -3.214  17.471  0.66 20.86 ?  90  LYS   A CG   1 
ATOM   2119 C CD   A LYS   A 1 90  ? 31.541 -4.620  18.295  0.34 23.94 ?  90  LYS   A CD   1 
ATOM   2120 C CD   B LYS   A 1 90  ? 31.384 -4.484  18.267  0.66 24.50 ?  90  LYS   A CD   1 
ATOM   2121 C CE   A LYS   A 1 90  ? 32.964 -4.660  18.834  0.34 25.68 ?  90  LYS   A CE   1 
ATOM   2122 C CE   B LYS   A 1 90  ? 32.738 -4.446  18.961  0.66 27.61 ?  90  LYS   A CE   1 
ATOM   2123 N NZ   A LYS   A 1 90  ? 33.968 -4.972  17.781  0.34 26.94 ?  90  LYS   A NZ   1 
ATOM   2124 N NZ   B LYS   A 1 90  ? 33.873 -4.421  17.998  0.66 29.40 ?  90  LYS   A NZ   1 
ATOM   2125 H H    A LYS   A 1 90  ? 27.606 -2.437  16.372  0.34 18.74 ?  90  LYS   A H    1 
ATOM   2126 H H    B LYS   A 1 90  ? 27.409 -2.253  16.529  0.66 16.25 ?  90  LYS   A H    1 
ATOM   2127 H HA   A LYS   A 1 90  ? 29.853 -1.203  16.985  0.34 20.08 ?  90  LYS   A HA   1 
ATOM   2128 H HA   B LYS   A 1 90  ? 29.648 -1.023  17.090  0.66 17.05 ?  90  LYS   A HA   1 
ATOM   2129 H HB2  A LYS   A 1 90  ? 29.328 -3.325  17.877  0.34 22.65 ?  90  LYS   A HB2  1 
ATOM   2130 H HB2  B LYS   A 1 90  ? 29.138 -3.186  17.913  0.66 20.23 ?  90  LYS   A HB2  1 
ATOM   2131 H HB3  A LYS   A 1 90  ? 29.588 -3.959  16.444  0.34 22.65 ?  90  LYS   A HB3  1 
ATOM   2132 H HB3  B LYS   A 1 90  ? 29.444 -3.767  16.467  0.66 20.23 ?  90  LYS   A HB3  1 
ATOM   2133 H HG2  A LYS   A 1 90  ? 31.816 -3.544  16.578  0.34 26.08 ?  90  LYS   A HG2  1 
ATOM   2134 H HG2  B LYS   A 1 90  ? 31.663 -3.253  16.660  0.66 25.19 ?  90  LYS   A HG2  1 
ATOM   2135 H HG3  A LYS   A 1 90  ? 31.622 -2.624  17.861  0.34 26.08 ?  90  LYS   A HG3  1 
ATOM   2136 H HG3  B LYS   A 1 90  ? 31.403 -2.457  18.013  0.66 25.19 ?  90  LYS   A HG3  1 
ATOM   2137 H HD2  A LYS   A 1 90  ? 30.932 -4.576  19.048  0.34 28.88 ?  90  LYS   A HD2  1 
ATOM   2138 H HD2  B LYS   A 1 90  ? 30.697 -4.581  18.947  0.66 29.55 ?  90  LYS   A HD2  1 
ATOM   2139 H HD3  A LYS   A 1 90  ? 31.387 -5.431  17.786  0.34 28.88 ?  90  LYS   A HD3  1 
ATOM   2140 H HD3  B LYS   A 1 90  ? 31.372 -5.248  17.668  0.66 29.55 ?  90  LYS   A HD3  1 
ATOM   2141 H HE2  A LYS   A 1 90  ? 33.184 -3.793  19.212  0.34 30.97 ?  90  LYS   A HE2  1 
ATOM   2142 H HE2  B LYS   A 1 90  ? 32.792 -3.646  19.508  0.66 33.28 ?  90  LYS   A HE2  1 
ATOM   2143 H HE3  A LYS   A 1 90  ? 33.023 -5.344  19.519  0.34 30.97 ?  90  LYS   A HE3  1 
ATOM   2144 H HE3  B LYS   A 1 90  ? 32.833 -5.235  19.518  0.66 33.28 ?  90  LYS   A HE3  1 
ATOM   2145 H HZ1  A LYS   A 1 90  ? 34.781 -5.022  18.141  0.34 32.47 ?  90  LYS   A HZ1  1 
ATOM   2146 H HZ1  B LYS   A 1 90  ? 34.647 -4.399  18.439  0.66 35.44 ?  90  LYS   A HZ1  1 
ATOM   2147 H HZ2  A LYS   A 1 90  ? 33.773 -5.751  17.397  0.34 32.47 ?  90  LYS   A HZ2  1 
ATOM   2148 H HZ2  B LYS   A 1 90  ? 33.854 -5.150  17.487  0.66 35.44 ?  90  LYS   A HZ2  1 
ATOM   2149 H HZ3  A LYS   A 1 90  ? 33.965 -4.334  17.160  0.34 32.47 ?  90  LYS   A HZ3  1 
ATOM   2150 H HZ3  B LYS   A 1 90  ? 33.816 -3.702  17.478  0.66 35.44 ?  90  LYS   A HZ3  1 
ATOM   2151 N N    A HIS   A 1 91  ? 29.724 -2.448  14.038  0.34 14.95 ?  91  HIS   A N    1 
ATOM   2152 N N    B HIS   A 1 91  ? 29.583 -2.257  14.132  0.66 11.49 ?  91  HIS   A N    1 
ATOM   2153 C CA   A HIS   A 1 91  ? 30.294 -2.407  12.703  0.34 14.36 ?  91  HIS   A CA   1 
ATOM   2154 C CA   B HIS   A 1 91  ? 30.178 -2.251  12.808  0.66 11.13 ?  91  HIS   A CA   1 
ATOM   2155 C C    A HIS   A 1 91  ? 29.191 -2.164  11.689  0.34 12.31 ?  91  HIS   A C    1 
ATOM   2156 C C    B HIS   A 1 91  ? 29.107 -1.988  11.765  0.66 10.79 ?  91  HIS   A C    1 
ATOM   2157 O O    A HIS   A 1 91  ? 28.056 -2.620  11.858  0.34 11.62 ?  91  HIS   A O    1 
ATOM   2158 O O    B HIS   A 1 91  ? 27.929 -2.301  11.965  0.66 11.33 ?  91  HIS   A O    1 
ATOM   2159 C CB   A HIS   A 1 91  ? 30.964 -3.735  12.335  0.34 16.38 ?  91  HIS   A CB   1 
ATOM   2160 C CB   B HIS   A 1 91  ? 30.787 -3.616  12.469  0.66 13.79 ?  91  HIS   A CB   1 
ATOM   2161 C CG   A HIS   A 1 91  ? 31.919 -4.240  13.368  0.34 18.91 ?  91  HIS   A CG   1 
ATOM   2162 C CG   B HIS   A 1 91  ? 31.771 -4.106  13.479  0.66 17.65 ?  91  HIS   A CG   1 
ATOM   2163 N ND1  A HIS   A 1 91  ? 33.188 -3.726  13.522  0.34 20.22 ?  91  HIS   A ND1  1 
ATOM   2164 N ND1  B HIS   A 1 91  ? 33.047 -3.597  13.577  0.66 19.88 ?  91  HIS   A ND1  1 
ATOM   2165 C CD2  A HIS   A 1 91  ? 31.795 -5.220  14.294  0.34 20.04 ?  91  HIS   A CD2  1 
ATOM   2166 C CD2  B HIS   A 1 91  ? 31.671 -5.061  14.432  0.66 19.51 ?  91  HIS   A CD2  1 
ATOM   2167 C CE1  A HIS   A 1 91  ? 33.803 -4.365  14.501  0.34 20.72 ?  91  HIS   A CE1  1 
ATOM   2168 C CE1  B HIS   A 1 91  ? 33.693 -4.221  14.547  0.66 20.81 ?  91  HIS   A CE1  1 
ATOM   2169 N NE2  A HIS   A 1 91  ? 32.979 -5.277  14.986  0.34 20.89 ?  91  HIS   A NE2  1 
ATOM   2170 N NE2  B HIS   A 1 91  ? 32.879 -5.114  15.083  0.66 21.06 ?  91  HIS   A NE2  1 
ATOM   2171 H H    A HIS   A 1 91  ? 29.023 -2.949  14.094  0.34 18.09 ?  91  HIS   A H    1 
ATOM   2172 H H    B HIS   A 1 91  ? 28.894 -2.786  14.192  0.66 13.93 ?  91  HIS   A H    1 
ATOM   2173 H HA   A HIS   A 1 91  ? 30.944 -1.694  12.635  0.34 17.39 ?  91  HIS   A HA   1 
ATOM   2174 H HA   B HIS   A 1 91  ? 30.859 -1.567  12.751  0.66 13.50 ?  91  HIS   A HA   1 
ATOM   2175 H HB2  A HIS   A 1 91  ? 30.276 -4.407  12.211  0.34 19.81 ?  91  HIS   A HB2  1 
ATOM   2176 H HB2  B HIS   A 1 91  ? 30.072 -4.269  12.406  0.66 16.70 ?  91  HIS   A HB2  1 
ATOM   2177 H HB3  A HIS   A 1 91  ? 31.457 -3.613  11.508  0.34 19.81 ?  91  HIS   A HB3  1 
ATOM   2178 H HB3  B HIS   A 1 91  ? 31.242 -3.546  11.614  0.66 16.70 ?  91  HIS   A HB3  1 
ATOM   2179 H HD1  A HIS   A 1 91  ? 33.526 -3.087  13.054  0.34 24.41 ?  91  HIS   A HD1  1 
ATOM   2180 H HD1  B HIS   A 1 91  ? 33.374 -2.973  13.079  0.66 24.01 ?  91  HIS   A HD1  1 
ATOM   2181 H HD2  A HIS   A 1 91  ? 31.046 -5.750  14.435  0.34 24.20 ?  91  HIS   A HD2  1 
ATOM   2182 H HD2  B HIS   A 1 91  ? 30.927 -5.585  14.610  0.66 23.57 ?  91  HIS   A HD2  1 
ATOM   2183 H HE1  A HIS   A 1 91  ? 34.669 -4.199  14.797  0.34 25.01 ?  91  HIS   A HE1  1 
ATOM   2184 H HE1  B HIS   A 1 91  ? 34.571 -4.054  14.807  0.66 25.12 ?  91  HIS   A HE1  1 
ATOM   2185 N N    . CYS   A 1 92  ? 29.538 -1.446  10.628  1.00 11.03 ?  92  CYS   A N    1 
ATOM   2186 C CA   . CYS   A 1 92  ? 28.712 -1.371  9.433   1.00 10.73 ?  92  CYS   A CA   1 
ATOM   2187 C C    . CYS   A 1 92  ? 29.371 -2.191  8.333   1.00 10.26 ?  92  CYS   A C    1 
ATOM   2188 O O    . CYS   A 1 92  ? 30.528 -1.942  7.968   1.00 11.22 ?  92  CYS   A O    1 
ATOM   2189 C CB   . CYS   A 1 92  ? 28.498 0.069   8.968   1.00 11.02 ?  92  CYS   A CB   1 
ATOM   2190 S SG   . CYS   A 1 92  ? 27.488 0.160   7.456   1.00 10.87 ?  92  CYS   A SG   1 
ATOM   2191 H H    A CYS   A 1 92  ? 30.260 -0.984  10.579  0.34 13.38 ?  92  CYS   A H    1 
ATOM   2192 H H    B CYS   A 1 92  ? 30.326 -1.121  10.522  0.66 13.38 ?  92  CYS   A H    1 
ATOM   2193 H HA   . CYS   A 1 92  ? 27.843 -1.758  9.619   1.00 13.02 ?  92  CYS   A HA   1 
ATOM   2194 H HB2  . CYS   A 1 92  ? 28.039 0.567   9.666   1.00 13.37 ?  92  CYS   A HB2  1 
ATOM   2195 H HB3  . CYS   A 1 92  ? 29.356 0.477   8.780   1.00 13.37 ?  92  CYS   A HB3  1 
ATOM   2196 H HG   . CYS   A 1 92  ? 27.341 1.312   7.155   1.00 13.19 ?  92  CYS   A HG   1 
ATOM   2197 N N    . LEU   A 1 93  ? 28.641 -3.178  7.826   1.00 10.31 ?  93  LEU   A N    1 
ATOM   2198 C CA   . LEU   A 1 93  ? 29.060 -3.945  6.661   1.00 10.17 ?  93  LEU   A CA   1 
ATOM   2199 C C    . LEU   A 1 93  ? 28.472 -3.266  5.429   1.00 9.91  ?  93  LEU   A C    1 
ATOM   2200 O O    . LEU   A 1 93  ? 27.259 -3.329  5.197   1.00 9.98  ?  93  LEU   A O    1 
ATOM   2201 C CB   . LEU   A 1 93  ? 28.599 -5.400  6.782   1.00 10.09 ?  93  LEU   A CB   1 
ATOM   2202 C CG   . LEU   A 1 93  ? 28.992 -6.293  5.609   1.00 10.65 ?  93  LEU   A CG   1 
ATOM   2203 C CD1  . LEU   A 1 93  ? 30.502 -6.539  5.589   1.00 11.90 ?  93  LEU   A CD1  1 
ATOM   2204 C CD2  . LEU   A 1 93  ? 28.231 -7.625  5.659   1.00 11.41 ?  93  LEU   A CD2  1 
ATOM   2205 H H    . LEU   A 1 93  ? 27.880 -3.423  8.153   1.00 12.52 ?  93  LEU   A H    1 
ATOM   2206 H HA   . LEU   A 1 93  ? 30.022 -3.923  6.597   1.00 12.36 ?  93  LEU   A HA   1 
ATOM   2207 H HB2  . LEU   A 1 93  ? 28.990 -5.778  7.586   1.00 12.25 ?  93  LEU   A HB2  1 
ATOM   2208 H HB3  . LEU   A 1 93  ? 27.634 -5.416  6.850   1.00 12.25 ?  93  LEU   A HB3  1 
ATOM   2209 H HG   . LEU   A 1 93  ? 28.761 -5.852  4.783   1.00 12.93 ?  93  LEU   A HG   1 
ATOM   2210 H HD11 . LEU   A 1 93  ? 30.717 -7.144  4.864   1.00 14.43 ?  93  LEU   A HD11 1 
ATOM   2211 H HD12 . LEU   A 1 93  ? 30.960 -5.690  5.458   1.00 14.43 ?  93  LEU   A HD12 1 
ATOM   2212 H HD13 . LEU   A 1 93  ? 30.774 -6.928  6.437   1.00 14.43 ?  93  LEU   A HD13 1 
ATOM   2213 H HD21 . LEU   A 1 93  ? 28.506 -8.174  4.907   1.00 13.84 ?  93  LEU   A HD21 1 
ATOM   2214 H HD22 . LEU   A 1 93  ? 28.441 -8.080  6.492   1.00 13.84 ?  93  LEU   A HD22 1 
ATOM   2215 H HD23 . LEU   A 1 93  ? 27.281 -7.446  5.611   1.00 13.84 ?  93  LEU   A HD23 1 
ATOM   2216 N N    . HIS   A 1 94  ? 29.320 -2.569  4.668   1.00 9.57  ?  94  HIS   A N    1 
ATOM   2217 C CA   . HIS   A 1 94  ? 28.896 -1.915  3.435   1.00 9.60  ?  94  HIS   A CA   1 
ATOM   2218 C C    . HIS   A 1 94  ? 28.920 -2.944  2.320   1.00 9.44  ?  94  HIS   A C    1 
ATOM   2219 O O    . HIS   A 1 94  ? 29.991 -3.462  1.994   1.00 10.85 ?  94  HIS   A O    1 
ATOM   2220 C CB   . HIS   A 1 94  ? 29.829 -0.750  3.104   1.00 9.52  ?  94  HIS   A CB   1 
ATOM   2221 C CG   . HIS   A 1 94  ? 29.807 0.340   4.123   1.00 9.63  ?  94  HIS   A CG   1 
ATOM   2222 N ND1  . HIS   A 1 94  ? 28.932 1.405   4.064   1.00 9.71  ?  94  HIS   A ND1  1 
ATOM   2223 C CD2  . HIS   A 1 94  ? 30.550 0.515   5.240   1.00 10.17 ?  94  HIS   A CD2  1 
ATOM   2224 C CE1  . HIS   A 1 94  ? 29.140 2.184   5.108   1.00 10.04 ?  94  HIS   A CE1  1 
ATOM   2225 N NE2  . HIS   A 1 94  ? 30.118 1.671   5.834   1.00 10.16 ?  94  HIS   A NE2  1 
ATOM   2226 H H    . HIS   A 1 94  ? 30.157 -2.466  4.848   1.00 11.63 ?  94  HIS   A H    1 
ATOM   2227 H HA   . HIS   A 1 94  ? 27.993 -1.579  3.536   1.00 11.67 ?  94  HIS   A HA   1 
ATOM   2228 H HB2  . HIS   A 1 94  ? 30.735 -1.081  3.044   1.00 11.57 ?  94  HIS   A HB2  1 
ATOM   2229 H HB3  . HIS   A 1 94  ? 29.556 -0.366  2.257   1.00 11.57 ?  94  HIS   A HB3  1 
ATOM   2230 H HD2  . HIS   A 1 94  ? 31.228 -0.036  5.550   1.00 12.35 ?  94  HIS   A HD2  1 
ATOM   2231 H HE1  . HIS   A 1 94  ? 28.673 2.973   5.292   1.00 12.20 ?  94  HIS   A HE1  1 
ATOM   2232 H HE2  . HIS   A 1 94  ? 30.430 2.020   6.555   1.00 12.35 ?  94  HIS   A HE2  1 
ATOM   2233 N N    . VAL   A 1 95  ? 27.758 -3.254  1.747   1.00 9.25  ?  95  VAL   A N    1 
ATOM   2234 C CA   . VAL   A 1 95  ? 27.630 -4.302  0.737   1.00 9.52  ?  95  VAL   A CA   1 
ATOM   2235 C C    . VAL   A 1 95  ? 27.088 -3.685  -0.539  1.00 9.46  ?  95  VAL   A C    1 
ATOM   2236 O O    . VAL   A 1 95  ? 26.087 -2.959  -0.498  1.00 10.54 ?  95  VAL   A O    1 
ATOM   2237 C CB   . VAL   A 1 95  ? 26.705 -5.445  1.198   1.00 10.12 ?  95  VAL   A CB   1 
ATOM   2238 C CG1  . VAL   A 1 95  ? 26.599 -6.493  0.094   1.00 10.95 ?  95  VAL   A CG1  1 
ATOM   2239 C CG2  . VAL   A 1 95  ? 27.195 -6.052  2.491   1.00 10.44 ?  95  VAL   A CG2  1 
ATOM   2240 H H    . VAL   A 1 95  ? 27.011 -2.874  1.942   1.00 11.25 ?  95  VAL   A H    1 
ATOM   2241 H HA   . VAL   A 1 95  ? 28.503 -4.680  0.550   1.00 11.57 ?  95  VAL   A HA   1 
ATOM   2242 H HB   . VAL   A 1 95  ? 25.818 -5.090  1.353   1.00 12.30 ?  95  VAL   A HB   1 
ATOM   2243 H HG11 . VAL   A 1 95  ? 26.229 -7.311  0.464   1.00 13.30 ?  95  VAL   A HG11 1 
ATOM   2244 H HG12 . VAL   A 1 95  ? 26.020 -6.163  -0.612  1.00 13.30 ?  95  VAL   A HG12 1 
ATOM   2245 H HG13 . VAL   A 1 95  ? 27.486 -6.672  -0.265  1.00 13.30 ?  95  VAL   A HG13 1 
ATOM   2246 H HG21 . VAL   A 1 95  ? 26.628 -6.805  2.718   1.00 12.68 ?  95  VAL   A HG21 1 
ATOM   2247 H HG22 . VAL   A 1 95  ? 28.110 -6.350  2.371   1.00 12.68 ?  95  VAL   A HG22 1 
ATOM   2248 H HG23 . VAL   A 1 95  ? 27.151 -5.380  3.187   1.00 12.68 ?  95  VAL   A HG23 1 
ATOM   2249 N N    A VAL   A 1 96  ? 27.721 -3.996  -1.668  0.34 9.52  ?  96  VAL   A N    1 
ATOM   2250 N N    B VAL   A 1 96  ? 27.718 -3.990  -1.672  0.66 9.55  ?  96  VAL   A N    1 
ATOM   2251 C CA   A VAL   A 1 96  ? 27.351 -3.439  -2.965  0.34 9.92  ?  96  VAL   A CA   1 
ATOM   2252 C CA   B VAL   A 1 96  ? 27.301 -3.462  -2.967  0.66 10.18 ?  96  VAL   A CA   1 
ATOM   2253 C C    A VAL   A 1 96  ? 26.511 -4.470  -3.711  0.34 10.37 ?  96  VAL   A C    1 
ATOM   2254 C C    B VAL   A 1 96  ? 26.571 -4.548  -3.747  0.66 10.71 ?  96  VAL   A C    1 
ATOM   2255 O O    A VAL   A 1 96  ? 27.042 -5.406  -4.316  0.34 10.62 ?  96  VAL   A O    1 
ATOM   2256 O O    B VAL   A 1 96  ? 27.191 -5.498  -4.237  0.66 11.86 ?  96  VAL   A O    1 
ATOM   2257 C CB   A VAL   A 1 96  ? 28.579 -3.023  -3.776  0.34 10.28 ?  96  VAL   A CB   1 
ATOM   2258 C CB   B VAL   A 1 96  ? 28.487 -2.924  -3.774  0.66 10.84 ?  96  VAL   A CB   1 
ATOM   2259 C CG1  A VAL   A 1 96  ? 28.150 -2.368  -5.083  0.34 10.57 ?  96  VAL   A CG1  1 
ATOM   2260 C CG1  B VAL   A 1 96  ? 27.982 -2.335  -5.078  0.66 10.97 ?  96  VAL   A CG1  1 
ATOM   2261 C CG2  A VAL   A 1 96  ? 29.464 -2.090  -2.966  0.34 10.11 ?  96  VAL   A CG2  1 
ATOM   2262 C CG2  B VAL   A 1 96  ? 29.272 -1.890  -2.981  0.66 10.67 ?  96  VAL   A CG2  1 
ATOM   2263 H H    A VAL   A 1 96  ? 28.393 -4.536  -1.707  0.34 11.57 ?  96  VAL   A H    1 
ATOM   2264 H H    B VAL   A 1 96  ? 28.412 -4.504  -1.713  0.66 11.61 ?  96  VAL   A H    1 
ATOM   2265 H HA   A VAL   A 1 96  ? 26.805 -2.651  -2.824  0.34 12.06 ?  96  VAL   A HA   1 
ATOM   2266 H HA   B VAL   A 1 96  ? 26.687 -2.727  -2.822  0.66 12.37 ?  96  VAL   A HA   1 
ATOM   2267 H HB   A VAL   A 1 96  ? 29.098 -3.810  -3.995  0.34 12.49 ?  96  VAL   A HB   1 
ATOM   2268 H HB   B VAL   A 1 96  ? 29.086 -3.651  -3.986  0.66 13.16 ?  96  VAL   A HB   1 
ATOM   2269 H HG11 A VAL   A 1 96  ? 28.932 -1.991  -5.519  0.34 12.84 ?  96  VAL   A HG11 1 
ATOM   2270 H HG11 B VAL   A 1 96  ? 28.692 -1.805  -5.481  0.66 13.31 ?  96  VAL   A HG11 1 
ATOM   2271 H HG12 A VAL   A 1 96  ? 27.743 -3.034  -5.657  0.34 12.84 ?  96  VAL   A HG12 1 
ATOM   2272 H HG12 B VAL   A 1 96  ? 27.729 -3.052  -5.676  0.66 13.31 ?  96  VAL   A HG12 1 
ATOM   2273 H HG13 A VAL   A 1 96  ? 27.512 -1.661  -4.889  0.34 12.84 ?  96  VAL   A HG13 1 
ATOM   2274 H HG13 B VAL   A 1 96  ? 27.217 -1.766  -4.895  0.66 13.31 ?  96  VAL   A HG13 1 
ATOM   2275 H HG21 A VAL   A 1 96  ? 30.181 -1.765  -3.531  0.34 12.29 ?  96  VAL   A HG21 1 
ATOM   2276 H HG21 B VAL   A 1 96  ? 29.975 -1.528  -3.542  0.66 12.95 ?  96  VAL   A HG21 1 
ATOM   2277 H HG22 A VAL   A 1 96  ? 28.929 -1.345  -2.648  0.34 12.29 ?  96  VAL   A HG22 1 
ATOM   2278 H HG22 B VAL   A 1 96  ? 28.671 -1.182  -2.702  0.66 12.95 ?  96  VAL   A HG22 1 
ATOM   2279 H HG23 A VAL   A 1 96  ? 29.830 -2.579  -2.213  0.34 12.29 ?  96  VAL   A HG23 1 
ATOM   2280 H HG23 B VAL   A 1 96  ? 29.659 -2.321  -2.201  0.66 12.95 ?  96  VAL   A HG23 1 
ATOM   2281 N N    A GLY   A 1 97  ? 25.192 -4.291  -3.685  0.34 10.77 ?  97  GLY   A N    1 
ATOM   2282 N N    B GLY   A 1 97  ? 25.255 -4.407  -3.885  0.66 10.31 ?  97  GLY   A N    1 
ATOM   2283 C CA   A GLY   A 1 97  ? 24.312 -5.041  -4.547  0.34 11.04 ?  97  GLY   A CA   1 
ATOM   2284 C CA   B GLY   A 1 97  ? 24.509 -5.204  -4.826  0.66 10.79 ?  97  GLY   A CA   1 
ATOM   2285 C C    A GLY   A 1 97  ? 24.286 -4.405  -5.922  0.34 11.24 ?  97  GLY   A C    1 
ATOM   2286 C C    B GLY   A 1 97  ? 24.582 -4.602  -6.215  0.66 11.03 ?  97  GLY   A C    1 
ATOM   2287 O O    A GLY   A 1 97  ? 24.557 -3.210  -6.072  0.34 11.62 ?  97  GLY   A O    1 
ATOM   2288 O O    B GLY   A 1 97  ? 24.923 -3.427  -6.384  0.66 12.19 ?  97  GLY   A O    1 
ATOM   2289 H H    A GLY   A 1 97  ? 24.780 -3.728  -3.176  0.34 13.07 ?  97  GLY   A H    1 
ATOM   2290 H H    B GLY   A 1 97  ? 24.770 -3.854  -3.431  0.66 12.52 ?  97  GLY   A H    1 
ATOM   2291 H HA2  A GLY   A 1 97  ? 24.630 -5.951  -4.625  0.34 13.41 ?  97  GLY   A HA2  1 
ATOM   2292 H HA2  B GLY   A 1 97  ? 24.872 -6.103  -4.845  0.66 13.10 ?  97  GLY   A HA2  1 
ATOM   2293 H HA3  A GLY   A 1 97  ? 23.411 -5.052  -4.182  0.34 13.41 ?  97  GLY   A HA3  1 
ATOM   2294 H HA3  B GLY   A 1 97  ? 23.578 -5.248  -4.560  0.66 13.10 ?  97  GLY   A HA3  1 
ATOM   2295 N N    A PRO   A 1 98  ? 23.968 -5.184  -6.955  0.34 11.10 ?  98  PRO   A N    1 
ATOM   2296 N N    B PRO   A 1 98  ? 24.268 -5.395  -7.238  0.66 11.44 ?  98  PRO   A N    1 
ATOM   2297 C CA   A PRO   A 1 98  ? 23.892 -4.605  -8.302  0.34 11.72 ?  98  PRO   A CA   1 
ATOM   2298 C CA   B PRO   A 1 98  ? 24.255 -4.862  -8.605  0.66 12.49 ?  98  PRO   A CA   1 
ATOM   2299 C C    A PRO   A 1 98  ? 22.785 -3.566  -8.393  0.34 12.25 ?  98  PRO   A C    1 
ATOM   2300 C C    B PRO   A 1 98  ? 23.161 -3.818  -8.787  0.66 12.65 ?  98  PRO   A C    1 
ATOM   2301 O O    A PRO   A 1 98  ? 21.705 -3.732  -7.820  0.34 11.75 ?  98  PRO   A O    1 
ATOM   2302 O O    B PRO   A 1 98  ? 22.060 -3.931  -8.238  0.66 13.27 ?  98  PRO   A O    1 
ATOM   2303 C CB   A PRO   A 1 98  ? 23.606 -5.819  -9.197  0.34 11.86 ?  98  PRO   A CB   1 
ATOM   2304 C CB   B PRO   A 1 98  ? 23.986 -6.104  -9.466  0.66 13.18 ?  98  PRO   A CB   1 
ATOM   2305 C CG   A PRO   A 1 98  ? 22.983 -6.831  -8.286  0.34 11.68 ?  98  PRO   A CG   1 
ATOM   2306 C CG   B PRO   A 1 98  ? 23.290 -7.057  -8.544  0.66 13.57 ?  98  PRO   A CG   1 
ATOM   2307 C CD   A PRO   A 1 98  ? 23.651 -6.624  -6.952  0.34 11.14 ?  98  PRO   A CD   1 
ATOM   2308 C CD   B PRO   A 1 98  ? 23.941 -6.831  -7.206  0.66 12.62 ?  98  PRO   A CD   1 
ATOM   2309 H HA   A PRO   A 1 98  ? 24.736 -4.206  -8.552  0.34 14.21 ?  98  PRO   A HA   1 
ATOM   2310 H HA   B PRO   A 1 98  ? 25.125 -4.489  -8.839  0.66 15.14 ?  98  PRO   A HA   1 
ATOM   2311 H HB2  A PRO   A 1 98  ? 22.992 -5.571  -9.907  0.34 14.38 ?  98  PRO   A HB2  1 
ATOM   2312 H HB2  B PRO   A 1 98  ? 23.415 -5.869  -10.211 0.66 15.97 ?  98  PRO   A HB2  1 
ATOM   2313 H HB3  A PRO   A 1 98  ? 24.439 -6.155  -9.568  0.34 14.38 ?  98  PRO   A HB3  1 
ATOM   2314 H HB3  B PRO   A 1 98  ? 24.825 -6.483  -9.778  0.66 15.97 ?  98  PRO   A HB3  1 
ATOM   2315 H HG2  A PRO   A 1 98  ? 22.030 -6.672  -8.221  0.34 14.17 ?  98  PRO   A HG2  1 
ATOM   2316 H HG2  B PRO   A 1 98  ? 22.343 -6.845  -8.502  0.66 16.44 ?  98  PRO   A HG2  1 
ATOM   2317 H HG3  A PRO   A 1 98  ? 23.159 -7.727  -8.621  0.34 14.17 ?  98  PRO   A HG3  1 
ATOM   2318 H HG3  B PRO   A 1 98  ? 23.424 -7.971  -8.844  0.66 16.44 ?  98  PRO   A HG3  1 
ATOM   2319 H HD2  A PRO   A 1 98  ? 23.039 -6.842  -6.230  0.34 13.52 ?  98  PRO   A HD2  1 
ATOM   2320 H HD2  B PRO   A 1 98  ? 23.320 -7.024  -6.485  0.66 15.30 ?  98  PRO   A HD2  1 
ATOM   2321 H HD3  A PRO   A 1 98  ? 24.468 -7.146  -6.895  0.34 13.52 ?  98  PRO   A HD3  1 
ATOM   2322 H HD3  B PRO   A 1 98  ? 24.751 -7.368  -7.126  0.66 15.30 ?  98  PRO   A HD3  1 
ATOM   2323 N N    A ASN   A 1 99  ? 23.071 -2.477  -9.108  0.34 13.81 ?  99  ASN   A N    1 
ATOM   2324 N N    B ASN   A 1 99  ? 23.478 -2.794  -9.571  0.66 13.79 ?  99  ASN   A N    1 
ATOM   2325 C CA   A ASN   A 1 99  ? 22.105 -1.411  -9.352  0.34 15.97 ?  99  ASN   A CA   1 
ATOM   2326 C CA   B ASN   A 1 99  ? 22.523 -1.753  -9.939  0.66 15.37 ?  99  ASN   A CA   1 
ATOM   2327 C C    A ASN   A 1 99  ? 21.543 -1.598  -10.757 0.34 17.88 ?  99  ASN   A C    1 
ATOM   2328 C C    B ASN   A 1 99  ? 22.016 -2.097  -11.335 0.66 15.33 ?  99  ASN   A C    1 
ATOM   2329 O O    A ASN   A 1 99  ? 22.232 -1.337  -11.749 0.34 18.38 ?  99  ASN   A O    1 
ATOM   2330 O O    B ASN   A 1 99  ? 22.720 -1.906  -12.330 0.66 15.23 ?  99  ASN   A O    1 
ATOM   2331 C CB   A ASN   A 1 99  ? 22.763 -0.040  -9.209  0.34 16.81 ?  99  ASN   A CB   1 
ATOM   2332 C CB   B ASN   A 1 99  ? 23.190 -0.384  -9.917  0.66 17.07 ?  99  ASN   A CB   1 
ATOM   2333 C CG   A ASN   A 1 99  ? 21.749 1.097   -9.153  0.34 17.82 ?  99  ASN   A CG   1 
ATOM   2334 C CG   B ASN   A 1 99  ? 22.222 0.743   -10.218 0.66 18.35 ?  99  ASN   A CG   1 
ATOM   2335 O OD1  A ASN   A 1 99  ? 20.702 1.049   -9.799  0.34 18.24 ?  99  ASN   A OD1  1 
ATOM   2336 O OD1  B ASN   A 1 99  ? 21.186 0.536   -10.844 0.66 18.38 ?  99  ASN   A OD1  1 
ATOM   2337 N ND2  A ASN   A 1 99  ? 22.063 2.127   -8.373  0.34 18.09 ?  99  ASN   A ND2  1 
ATOM   2338 N ND2  B ASN   A 1 99  ? 22.561 1.948   -9.776  0.66 19.68 ?  99  ASN   A ND2  1 
ATOM   2339 H H    A ASN   A 1 99  ? 23.842 -2.328  -9.457  0.34 16.72 ?  99  ASN   A H    1 
ATOM   2340 H H    B ASN   A 1 99  ? 24.264 -2.679  -9.905  0.66 16.70 ?  99  ASN   A H    1 
ATOM   2341 H HA   A ASN   A 1 99  ? 21.376 -1.478  -8.715  0.34 19.32 ?  99  ASN   A HA   1 
ATOM   2342 H HA   B ASN   A 1 99  ? 21.775 -1.759  -9.320  0.66 18.59 ?  99  ASN   A HA   1 
ATOM   2343 H HB2  A ASN   A 1 99  ? 23.284 -0.023  -8.392  0.34 20.32 ?  99  ASN   A HB2  1 
ATOM   2344 H HB2  B ASN   A 1 99  ? 23.574 -0.231  -9.041  0.66 20.63 ?  99  ASN   A HB2  1 
ATOM   2345 H HB3  A ASN   A 1 99  ? 23.339 0.113   -9.975  0.34 20.32 ?  99  ASN   A HB3  1 
ATOM   2346 H HB3  B ASN   A 1 99  ? 23.880 -0.375  -10.594 0.66 20.63 ?  99  ASN   A HB3  1 
ATOM   2347 H HD21 A ASN   A 1 99  ? 21.527 2.795   -8.301  0.34 21.86 ?  99  ASN   A HD21 1 
ATOM   2348 H HD21 B ASN   A 1 99  ? 22.044 2.622   -9.921  0.66 23.76 ?  99  ASN   A HD21 1 
ATOM   2349 H HD22 A ASN   A 1 99  ? 22.806 2.125   -7.937  0.34 21.86 ?  99  ASN   A HD22 1 
ATOM   2350 H HD22 B ASN   A 1 99  ? 23.296 2.056   -9.349  0.66 23.76 ?  99  ASN   A HD22 1 
ATOM   2351 N N    A VAL   A 1 100 ? 20.289 -2.052  -10.834 0.34 19.53 ?  100 VAL   A N    1 
ATOM   2352 N N    B VAL   A 1 100 ? 20.786 -2.607  -11.403 0.66 17.10 ?  100 VAL   A N    1 
ATOM   2353 C CA   A VAL   A 1 100 ? 19.654 -2.286  -12.128 0.34 21.05 ?  100 VAL   A CA   1 
ATOM   2354 C CA   B VAL   A 1 100 ? 20.231 -3.034  -12.684 0.66 19.50 ?  100 VAL   A CA   1 
ATOM   2355 C C    A VAL   A 1 100 ? 19.579 -0.995  -12.934 0.34 22.24 ?  100 VAL   A C    1 
ATOM   2356 C C    B VAL   A 1 100 ? 20.026 -1.848  -13.620 0.66 19.91 ?  100 VAL   A C    1 
ATOM   2357 O O    A VAL   A 1 100 ? 19.673 -1.018  -14.168 0.34 22.76 ?  100 VAL   A O    1 
ATOM   2358 O O    B VAL   A 1 100 ? 20.049 -2.006  -14.847 0.66 20.16 ?  100 VAL   A O    1 
ATOM   2359 C CB   A VAL   A 1 100 ? 18.268 -2.938  -11.927 0.34 21.61 ?  100 VAL   A CB   1 
ATOM   2360 C CB   B VAL   A 1 100 ? 18.940 -3.841  -12.447 0.66 21.76 ?  100 VAL   A CB   1 
ATOM   2361 C CG1  A VAL   A 1 100 ? 17.569 -3.154  -13.262 0.34 22.02 ?  100 VAL   A CG1  1 
ATOM   2362 C CG1  B VAL   A 1 100 ? 18.184 -4.069  -13.749 0.66 22.73 ?  100 VAL   A CG1  1 
ATOM   2363 C CG2  A VAL   A 1 100 ? 18.409 -4.259  -11.180 0.34 21.63 ?  100 VAL   A CG2  1 
ATOM   2364 C CG2  B VAL   A 1 100 ? 19.272 -5.168  -11.785 0.66 22.69 ?  100 VAL   A CG2  1 
ATOM   2365 H H    A VAL   A 1 100 ? 19.791 -2.231  -10.157 0.34 23.59 ?  100 VAL   A H    1 
ATOM   2366 H H    B VAL   A 1 100 ? 20.263 -2.716  -10.732 0.66 20.67 ?  100 VAL   A H    1 
ATOM   2367 H HA   A VAL   A 1 100 ? 20.194 -2.913  -12.631 0.34 25.41 ?  100 VAL   A HA   1 
ATOM   2368 H HA   B VAL   A 1 100 ? 20.866 -3.635  -13.105 0.66 23.55 ?  100 VAL   A HA   1 
ATOM   2369 H HB   A VAL   A 1 100 ? 17.713 -2.351  -11.391 0.34 26.08 ?  100 VAL   A HB   1 
ATOM   2370 H HB   B VAL   A 1 100 ? 18.360 -3.345  -11.848 0.66 26.27 ?  100 VAL   A HB   1 
ATOM   2371 H HG11 A VAL   A 1 100 ? 16.790 -3.717  -13.122 0.34 26.58 ?  100 VAL   A HG11 1 
ATOM   2372 H HG11 B VAL   A 1 100 ? 17.512 -4.757  -13.605 0.66 27.42 ?  100 VAL   A HG11 1 
ATOM   2373 H HG12 A VAL   A 1 100 ? 17.294 -2.296  -13.619 0.34 26.58 ?  100 VAL   A HG12 1 
ATOM   2374 H HG12 B VAL   A 1 100 ? 17.753 -3.242  -14.017 0.66 27.42 ?  100 VAL   A HG12 1 
ATOM   2375 H HG13 A VAL   A 1 100 ? 18.183 -3.589  -13.873 0.34 26.58 ?  100 VAL   A HG13 1 
ATOM   2376 H HG13 B VAL   A 1 100 ? 18.808 -4.358  -14.431 0.66 27.42 ?  100 VAL   A HG13 1 
ATOM   2377 H HG21 A VAL   A 1 100 ? 17.543 -4.693  -11.138 0.34 26.11 ?  100 VAL   A HG21 1 
ATOM   2378 H HG21 B VAL   A 1 100 ? 18.450 -5.667  -11.646 0.66 27.38 ?  100 VAL   A HG21 1 
ATOM   2379 H HG22 A VAL   A 1 100 ? 19.039 -4.823  -11.655 0.34 26.11 ?  100 VAL   A HG22 1 
ATOM   2380 H HG22 B VAL   A 1 100 ? 19.866 -5.671  -12.365 0.66 27.38 ?  100 VAL   A HG22 1 
ATOM   2381 H HG23 A VAL   A 1 100 ? 18.734 -4.082  -10.283 0.34 26.11 ?  100 VAL   A HG23 1 
ATOM   2382 H HG23 B VAL   A 1 100 ? 19.704 -4.999  -10.935 0.66 27.38 ?  100 VAL   A HG23 1 
ATOM   2383 N N    A ASN   A 1 101 ? 19.418 0.145   -12.260 0.34 22.95 ?  101 ASN   A N    1 
ATOM   2384 N N    B ASN   A 1 101 ? 19.829 -0.648  -13.076 0.66 20.47 ?  101 ASN   A N    1 
ATOM   2385 C CA   A ASN   A 1 101 ? 19.351 1.430   -12.946 0.34 23.84 ?  101 ASN   A CA   1 
ATOM   2386 C CA   B ASN   A 1 101 ? 19.718 0.527   -13.929 0.66 21.68 ?  101 ASN   A CA   1 
ATOM   2387 C C    A ASN   A 1 101 ? 20.699 1.876   -13.502 0.34 24.90 ?  101 ASN   A C    1 
ATOM   2388 C C    B ASN   A 1 101 ? 21.057 0.955   -14.515 0.66 22.04 ?  101 ASN   A C    1 
ATOM   2389 O O    A ASN   A 1 101 ? 20.757 2.908   -14.180 0.34 25.14 ?  101 ASN   A O    1 
ATOM   2390 O O    B ASN   A 1 101 ? 21.075 1.799   -15.418 0.66 22.44 ?  101 ASN   A O    1 
ATOM   2391 C CB   A ASN   A 1 101 ? 18.781 2.493   -12.006 0.34 23.78 ?  101 ASN   A CB   1 
ATOM   2392 C CB   B ASN   A 1 101 ? 19.053 1.669   -13.163 0.66 23.38 ?  101 ASN   A CB   1 
ATOM   2393 C CG   A ASN   A 1 101 ? 17.425 2.105   -11.448 0.34 23.82 ?  101 ASN   A CG   1 
ATOM   2394 C CG   B ASN   A 1 101 ? 17.695 1.277   -12.614 0.66 24.88 ?  101 ASN   A CG   1 
ATOM   2395 O OD1  A ASN   A 1 101 ? 16.571 1.580   -12.167 0.34 23.83 ?  101 ASN   A OD1  1 
ATOM   2396 O OD1  B ASN   A 1 101 ? 16.988 0.457   -13.200 0.66 25.79 ?  101 ASN   A OD1  1 
ATOM   2397 N ND2  A ASN   A 1 101 ? 17.221 2.353   -10.158 0.34 23.72 ?  101 ASN   A ND2  1 
ATOM   2398 N ND2  B ASN   A 1 101 ? 17.331 1.848   -11.480 0.66 25.34 ?  101 ASN   A ND2  1 
ATOM   2399 H H    A ASN   A 1 101 ? 19.339 0.196   -11.406 0.34 27.69 ?  101 ASN   A H    1 
ATOM   2400 H H    B ASN   A 1 101 ? 19.747 -0.500  -12.235 0.66 24.71 ?  101 ASN   A H    1 
ATOM   2401 H HA   A ASN   A 1 101 ? 18.739 1.346   -13.692 0.34 28.75 ?  101 ASN   A HA   1 
ATOM   2402 H HA   B ASN   A 1 101 ? 19.145 0.304   -14.676 0.66 26.17 ?  101 ASN   A HA   1 
ATOM   2403 H HB2  A ASN   A 1 101 ? 19.389 2.620   -11.262 0.34 28.69 ?  101 ASN   A HB2  1 
ATOM   2404 H HB2  B ASN   A 1 101 ? 19.614 1.922   -12.418 0.66 28.20 ?  101 ASN   A HB2  1 
ATOM   2405 H HB3  A ASN   A 1 101 ? 18.677 3.325   -12.496 0.34 28.69 ?  101 ASN   A HB3  1 
ATOM   2406 H HB3  B ASN   A 1 101 ? 18.928 2.419   -13.764 0.66 28.20 ?  101 ASN   A HB3  1 
ATOM   2407 H HD21 A ASN   A 1 101 ? 16.468 2.150   -9.794  0.34 28.62 ?  101 ASN   A HD21 1 
ATOM   2408 H HD21 B ASN   A 1 101 ? 16.566 1.660   -11.133 0.66 30.56 ?  101 ASN   A HD21 1 
ATOM   2409 H HD22 A ASN   A 1 101 ? 17.840 2.720   -9.688  0.34 28.62 ?  101 ASN   A HD22 1 
ATOM   2410 H HD22 B ASN   A 1 101 ? 17.847 2.419   -11.104 0.66 30.56 ?  101 ASN   A HD22 1 
ATOM   2411 N N    A LYS   A 1 102 ? 21.774 1.138   -13.224 0.34 25.85 ?  102 LYS   A N    1 
ATOM   2412 N N    B LYS   A 1 102 ? 22.167 0.389   -14.037 0.66 22.66 ?  102 LYS   A N    1 
ATOM   2413 C CA   A LYS   A 1 102 ? 23.059 1.338   -13.879 0.34 26.83 ?  102 LYS   A CA   1 
ATOM   2414 C CA   B LYS   A 1 102 ? 23.482 0.563   -14.641 0.66 23.32 ?  102 LYS   A CA   1 
ATOM   2415 C C    A LYS   A 1 102 ? 23.367 0.244   -14.889 0.34 26.33 ?  102 LYS   A C    1 
ATOM   2416 C C    B LYS   A 1 102 ? 23.863 -0.604  -15.548 0.66 21.86 ?  102 LYS   A C    1 
ATOM   2417 O O    A LYS   A 1 102 ? 24.444 0.263   -15.495 0.34 26.53 ?  102 LYS   A O    1 
ATOM   2418 O O    B LYS   A 1 102 ? 24.996 -0.654  -16.037 0.66 22.64 ?  102 LYS   A O    1 
ATOM   2419 C CB   A LYS   A 1 102 ? 24.188 1.407   -12.843 0.34 28.39 ?  102 LYS   A CB   1 
ATOM   2420 C CB   B LYS   A 1 102 ? 24.559 0.716   -13.559 0.66 26.44 ?  102 LYS   A CB   1 
ATOM   2421 C CG   A LYS   A 1 102 ? 24.050 2.534   -11.836 0.34 29.77 ?  102 LYS   A CG   1 
ATOM   2422 C CG   B LYS   A 1 102 ? 24.439 1.938   -12.663 0.66 29.58 ?  102 LYS   A CG   1 
ATOM   2423 C CD   A LYS   A 1 102 ? 25.204 2.520   -10.845 0.34 31.08 ?  102 LYS   A CD   1 
ATOM   2424 C CD   B LYS   A 1 102 ? 25.482 1.868   -11.546 0.66 32.56 ?  102 LYS   A CD   1 
ATOM   2425 C CE   A LYS   A 1 102 ? 25.083 3.640   -9.825  0.34 32.03 ?  102 LYS   A CE   1 
ATOM   2426 C CE   B LYS   A 1 102 ? 25.401 3.058   -10.604 0.66 34.96 ?  102 LYS   A CE   1 
ATOM   2427 N NZ   A LYS   A 1 102 ? 26.173 3.581   -8.809  0.34 32.52 ?  102 LYS   A NZ   1 
ATOM   2428 N NZ   B LYS   A 1 102 ? 25.731 2.669   -9.199  0.66 36.16 ?  102 LYS   A NZ   1 
ATOM   2429 H H    A LYS   A 1 102 ? 21.781 0.503   -12.645 0.34 31.17 ?  102 LYS   A H    1 
ATOM   2430 H H    B LYS   A 1 102 ? 22.182 -0.121  -13.341 0.66 27.34 ?  102 LYS   A H    1 
ATOM   2431 H HA   A LYS   A 1 102 ? 23.045 2.179   -14.355 0.34 32.34 ?  102 LYS   A HA   1 
ATOM   2432 H HA   B LYS   A 1 102 ? 23.481 1.371   -15.172 0.66 28.13 ?  102 LYS   A HA   1 
ATOM   2433 H HB2  A LYS   A 1 102 ? 24.209 0.573   -12.349 0.34 34.22 ?  102 LYS   A HB2  1 
ATOM   2434 H HB2  B LYS   A 1 102 ? 24.533 -0.064  -12.984 0.66 31.89 ?  102 LYS   A HB2  1 
ATOM   2435 H HB3  A LYS   A 1 102 ? 25.030 1.531   -13.309 0.34 34.22 ?  102 LYS   A HB3  1 
ATOM   2436 H HB3  B LYS   A 1 102 ? 25.426 0.765   -13.993 0.66 31.89 ?  102 LYS   A HB3  1 
ATOM   2437 H HG2  A LYS   A 1 102 ? 24.056 3.385   -12.302 0.34 35.87 ?  102 LYS   A HG2  1 
ATOM   2438 H HG2  B LYS   A 1 102 ? 24.601 2.740   -13.183 0.66 35.64 ?  102 LYS   A HG2  1 
ATOM   2439 H HG3  A LYS   A 1 102 ? 23.221 2.425   -11.343 0.34 35.87 ?  102 LYS   A HG3  1 
ATOM   2440 H HG3  B LYS   A 1 102 ? 23.557 1.963   -12.263 0.66 35.64 ?  102 LYS   A HG3  1 
ATOM   2441 H HD2  A LYS   A 1 102 ? 25.206 1.675   -10.369 0.34 37.44 ?  102 LYS   A HD2  1 
ATOM   2442 H HD2  B LYS   A 1 102 ? 25.348 1.061   -11.026 0.66 39.23 ?  102 LYS   A HD2  1 
ATOM   2443 H HD3  A LYS   A 1 102 ? 26.039 2.636   -11.325 0.34 37.44 ?  102 LYS   A HD3  1 
ATOM   2444 H HD3  B LYS   A 1 102 ? 26.366 1.859   -11.943 0.66 39.23 ?  102 LYS   A HD3  1 
ATOM   2445 H HE2  A LYS   A 1 102 ? 25.139 4.495   -10.281 0.34 38.59 ?  102 LYS   A HE2  1 
ATOM   2446 H HE2  B LYS   A 1 102 ? 26.040 3.732   -10.888 0.66 42.11 ?  102 LYS   A HE2  1 
ATOM   2447 H HE3  A LYS   A 1 102 ? 24.233 3.562   -9.364  0.34 38.59 ?  102 LYS   A HE3  1 
ATOM   2448 H HE3  B LYS   A 1 102 ? 24.503 3.421   -10.619 0.66 42.11 ?  102 LYS   A HE3  1 
ATOM   2449 H HZ1  A LYS   A 1 102 ? 26.080 4.245   -8.224  0.34 39.18 ?  102 LYS   A HZ1  1 
ATOM   2450 H HZ1  B LYS   A 1 102 ? 25.622 3.365   -8.656  0.66 43.55 ?  102 LYS   A HZ1  1 
ATOM   2451 H HZ2  A LYS   A 1 102 ? 26.140 2.805   -8.373  0.34 39.18 ?  102 LYS   A HZ2  1 
ATOM   2452 H HZ2  B LYS   A 1 102 ? 25.195 2.009   -8.932  0.66 43.55 ?  102 LYS   A HZ2  1 
ATOM   2453 H HZ3  A LYS   A 1 102 ? 26.965 3.654   -9.208  0.34 39.18 ?  102 LYS   A HZ3  1 
ATOM   2454 H HZ3  B LYS   A 1 102 ? 26.575 2.392   -9.149  0.66 43.55 ?  102 LYS   A HZ3  1 
ATOM   2455 N N    A GLY   A 1 103 ? 22.456 -0.708  -15.084 0.34 26.15 ?  103 GLY   A N    1 
ATOM   2456 N N    B GLY   A 1 103 ? 22.960 -1.555  -15.766 0.66 20.02 ?  103 GLY   A N    1 
ATOM   2457 C CA   A GLY   A 1 103 ? 22.688 -1.803  -16.000 0.34 25.96 ?  103 GLY   A CA   1 
ATOM   2458 C CA   B GLY   A 1 103 ? 23.285 -2.720  -16.566 0.66 19.45 ?  103 GLY   A CA   1 
ATOM   2459 C C    A GLY   A 1 103 ? 23.572 -2.898  -15.457 0.34 25.83 ?  103 GLY   A C    1 
ATOM   2460 C C    B GLY   A 1 103 ? 24.088 -3.784  -15.849 0.66 19.02 ?  103 GLY   A C    1 
ATOM   2461 O O    A GLY   A 1 103 ? 24.184 -3.629  -16.241 0.34 26.25 ?  103 GLY   A O    1 
ATOM   2462 O O    B GLY   A 1 103 ? 24.627 -4.682  -16.507 0.66 20.06 ?  103 GLY   A O    1 
ATOM   2463 H H    A GLY   A 1 103 ? 21.694 -0.739  -14.692 0.34 31.53 ?  103 GLY   A H    1 
ATOM   2464 H H    B GLY   A 1 103 ? 22.158 -1.546  -15.455 0.66 24.17 ?  103 GLY   A H    1 
ATOM   2465 H HA2  A GLY   A 1 103 ? 21.833 -2.186  -16.266 0.34 31.31 ?  103 GLY   A HA2  1 
ATOM   2466 H HA2  B GLY   A 1 103 ? 22.461 -3.125  -16.873 0.66 23.50 ?  103 GLY   A HA2  1 
ATOM   2467 H HA3  A GLY   A 1 103 ? 23.122 -1.461  -16.792 0.34 31.31 ?  103 GLY   A HA3  1 
ATOM   2468 H HA3  B GLY   A 1 103 ? 23.784 -2.427  -17.349 0.66 23.50 ?  103 GLY   A HA3  1 
ATOM   2469 N N    A GLU   A 1 104 ? 23.671 -3.031  -14.138 0.34 25.18 ?  104 GLU   A N    1 
ATOM   2470 N N    B GLU   A 1 104 ? 24.180 -3.719  -14.527 0.66 17.31 ?  104 GLU   A N    1 
ATOM   2471 C CA   A GLU   A 1 104 ? 24.551 -4.020  -13.536 0.34 24.58 ?  104 GLU   A CA   1 
ATOM   2472 C CA   B GLU   A 1 104 ? 24.989 -4.668  -13.776 0.66 16.18 ?  104 GLU   A CA   1 
ATOM   2473 C C    A GLU   A 1 104 ? 23.866 -5.379  -13.431 0.34 24.46 ?  104 GLU   A C    1 
ATOM   2474 C C    B GLU   A 1 104 ? 24.248 -5.992  -13.598 0.66 16.56 ?  104 GLU   A C    1 
ATOM   2475 O O    A GLU   A 1 104 ? 22.651 -5.476  -13.238 0.34 24.43 ?  104 GLU   A O    1 
ATOM   2476 O O    B GLU   A 1 104 ? 23.018 -6.039  -13.505 0.66 17.87 ?  104 GLU   A O    1 
ATOM   2477 C CB   A GLU   A 1 104 ? 25.030 -3.541  -12.165 0.34 24.26 ?  104 GLU   A CB   1 
ATOM   2478 C CB   B GLU   A 1 104 ? 25.406 -4.056  -12.434 0.66 15.28 ?  104 GLU   A CB   1 
ATOM   2479 C CG   A GLU   A 1 104 ? 25.967 -2.341  -12.266 0.34 24.10 ?  104 GLU   A CG   1 
ATOM   2480 C CG   B GLU   A 1 104 ? 26.288 -2.815  -12.630 0.66 15.55 ?  104 GLU   A CG   1 
ATOM   2481 C CD   A GLU   A 1 104 ? 26.237 -1.667  -10.931 0.34 23.96 ?  104 GLU   A CD   1 
ATOM   2482 C CD   B GLU   A 1 104 ? 26.613 -2.035  -11.363 0.66 15.69 ?  104 GLU   A CD   1 
ATOM   2483 O OE1  A GLU   A 1 104 ? 25.641 -2.080  -9.915  0.34 23.60 ?  104 GLU   A OE1  1 
ATOM   2484 O OE1  B GLU   A 1 104 ? 26.074 -2.342  -10.282 0.66 16.22 ?  104 GLU   A OE1  1 
ATOM   2485 O OE2  A GLU   A 1 104 ? 27.039 -0.709  -10.903 0.34 24.32 -1 104 GLU   A OE2  1 
ATOM   2486 O OE2  B GLU   A 1 104 ? 27.411 -1.076  -11.469 0.66 16.75 -1 104 GLU   A OE2  1 
ATOM   2487 H H    A GLU   A 1 104 ? 23.246 -2.544  -13.566 0.34 30.37 ?  104 GLU   A H    1 
ATOM   2488 H H    B GLU   A 1 104 ? 23.787 -3.128  -14.046 0.66 20.92 ?  104 GLU   A H    1 
ATOM   2489 H HA   A GLU   A 1 104 ? 25.327 -4.127  -14.103 0.34 29.64 ?  104 GLU   A HA   1 
ATOM   2490 H HA   B GLU   A 1 104 ? 25.798 -4.849  -14.281 0.66 19.57 ?  104 GLU   A HA   1 
ATOM   2491 H HB2  A GLU   A 1 104 ? 24.262 -3.281  -11.633 0.34 29.26 ?  104 GLU   A HB2  1 
ATOM   2492 H HB2  B GLU   A 1 104 ? 24.615 -3.796  -11.943 0.66 18.49 ?  104 GLU   A HB2  1 
ATOM   2493 H HB3  A GLU   A 1 104 ? 25.508 -4.264  -11.728 0.34 29.26 ?  104 GLU   A HB3  1 
ATOM   2494 H HB3  B GLU   A 1 104 ? 25.914 -4.715  -11.933 0.66 18.49 ?  104 GLU   A HB3  1 
ATOM   2495 H HG2  A GLU   A 1 104 ? 26.812 -2.638  -12.645 0.34 29.08 ?  104 GLU   A HG2  1 
ATOM   2496 H HG2  B GLU   A 1 104 ? 27.123 -3.093  -13.035 0.66 18.82 ?  104 GLU   A HG2  1 
ATOM   2497 H HG3  A GLU   A 1 104 ? 25.564 -1.679  -12.849 0.34 29.08 ?  104 GLU   A HG3  1 
ATOM   2498 H HG3  B GLU   A 1 104 ? 25.825 -2.202  -13.221 0.66 18.82 ?  104 GLU   A HG3  1 
ATOM   2499 N N    A ASP   A 1 105 ? 24.672 -6.431  -13.561 0.34 24.60 ?  105 ASP   A N    1 
ATOM   2500 N N    B ASP   A 1 105 ? 25.026 -7.075  -13.566 0.66 16.45 ?  105 ASP   A N    1 
ATOM   2501 C CA   A ASP   A 1 105 ? 24.168 -7.795  -13.653 0.34 24.82 ?  105 ASP   A CA   1 
ATOM   2502 C CA   B ASP   A 1 105 ? 24.498 -8.435  -13.629 0.66 17.14 ?  105 ASP   A CA   1 
ATOM   2503 C C    A ASP   A 1 105 ? 23.490 -8.192  -12.346 0.34 23.91 ?  105 ASP   A C    1 
ATOM   2504 C C    B ASP   A 1 105 ? 23.741 -8.784  -12.352 0.66 15.72 ?  105 ASP   A C    1 
ATOM   2505 O O    A ASP   A 1 105 ? 24.109 -8.147  -11.278 0.34 23.66 ?  105 ASP   A O    1 
ATOM   2506 O O    B ASP   A 1 105 ? 24.318 -8.789  -11.263 0.66 14.37 ?  105 ASP   A O    1 
ATOM   2507 C CB   A ASP   A 1 105 ? 25.334 -8.734  -13.955 0.34 26.06 ?  105 ASP   A CB   1 
ATOM   2508 C CB   B ASP   A 1 105 ? 25.675 -9.390  -13.823 0.66 19.82 ?  105 ASP   A CB   1 
ATOM   2509 C CG   A ASP   A 1 105 ? 24.882 -10.147 -14.250 0.34 27.14 ?  105 ASP   A CG   1 
ATOM   2510 C CG   B ASP   A 1 105 ? 25.252 -10.835 -13.968 0.66 22.61 ?  105 ASP   A CG   1 
ATOM   2511 O OD1  A ASP   A 1 105 ? 23.658 -10.369 -14.355 0.34 27.48 ?  105 ASP   A OD1  1 
ATOM   2512 O OD1  B ASP   A 1 105 ? 24.039 -11.116 -14.049 0.66 22.55 ?  105 ASP   A OD1  1 
ATOM   2513 O OD2  A ASP   A 1 105 ? 25.752 -11.034 -14.384 0.34 27.78 -1 105 ASP   A OD2  1 
ATOM   2514 O OD2  B ASP   A 1 105 ? 26.158 -11.697 -14.002 0.66 24.61 -1 105 ASP   A OD2  1 
ATOM   2515 H H    A ASP   A 1 105 ? 25.528 -6.379  -13.592 0.34 29.67 ?  105 ASP   A H    1 
ATOM   2516 H H    B ASP   A 1 105 ? 25.883 -7.044  -13.508 0.66 19.89 ?  105 ASP   A H    1 
ATOM   2517 H HA   A ASP   A 1 105 ? 23.521 -7.866  -14.374 0.34 29.94 ?  105 ASP   A HA   1 
ATOM   2518 H HA   B ASP   A 1 105 ? 23.895 -8.525  -14.382 0.66 20.73 ?  105 ASP   A HA   1 
ATOM   2519 H HB2  A ASP   A 1 105 ? 25.809 -8.410  -14.738 0.34 31.42 ?  105 ASP   A HB2  1 
ATOM   2520 H HB2  B ASP   A 1 105 ? 26.163 -9.132  -14.621 0.66 23.94 ?  105 ASP   A HB2  1 
ATOM   2521 H HB3  A ASP   A 1 105 ? 25.935 -8.751  -13.191 0.34 31.42 ?  105 ASP   A HB3  1 
ATOM   2522 H HB3  B ASP   A 1 105 ? 26.256 -9.340  -13.050 0.66 23.94 ?  105 ASP   A HB3  1 
ATOM   2523 N N    A ILE   A 1 106 ? 22.214 -8.584  -12.432 0.34 23.35 ?  106 ILE   A N    1 
ATOM   2524 N N    B ILE   A 1 106 ? 22.457 -9.123  -12.493 0.66 16.87 ?  106 ILE   A N    1 
ATOM   2525 C CA   A ILE   A 1 106 ? 21.475 -8.993  -11.243 0.34 22.79 ?  106 ILE   A CA   1 
ATOM   2526 C CA   B ILE   A 1 106 ? 21.644 -9.491  -11.337 0.66 16.85 ?  106 ILE   A CA   1 
ATOM   2527 C C    A ILE   A 1 106 ? 22.016 -10.287 -10.652 0.34 22.86 ?  106 ILE   A C    1 
ATOM   2528 C C    B ILE   A 1 106 ? 22.228 -10.692 -10.610 0.66 15.82 ?  106 ILE   A C    1 
ATOM   2529 O O    A ILE   A 1 106 ? 21.777 -10.570 -9.473  0.34 22.62 ?  106 ILE   A O    1 
ATOM   2530 O O    B ILE   A 1 106 ? 22.007 -10.861 -9.404  0.66 15.31 ?  106 ILE   A O    1 
ATOM   2531 C CB   A ILE   A 1 106 ? 19.965 -9.094  -11.544 0.34 22.43 ?  106 ILE   A CB   1 
ATOM   2532 C CB   B ILE   A 1 106 ? 20.187 -9.746  -11.770 0.66 18.90 ?  106 ILE   A CB   1 
ATOM   2533 C CG1  A ILE   A 1 106 ? 19.149 -9.086  -10.248 0.34 22.48 ?  106 ILE   A CG1  1 
ATOM   2534 C CG1  B ILE   A 1 106 ? 19.258 -9.808  -10.557 0.66 19.58 ?  106 ILE   A CG1  1 
ATOM   2535 C CG2  A ILE   A 1 106 ? 19.659 -10.360 -12.323 0.34 22.17 ?  106 ILE   A CG2  1 
ATOM   2536 C CG2  B ILE   A 1 106 ? 20.085 -11.057 -12.527 0.66 19.73 ?  106 ILE   A CG2  1 
ATOM   2537 C CD1  A ILE   A 1 106 ? 19.373 -7.858  -9.392  0.34 22.54 ?  106 ILE   A CD1  1 
ATOM   2538 C CD1  B ILE   A 1 106 ? 19.249 -8.551  -9.729  0.66 20.32 ?  106 ILE   A CD1  1 
ATOM   2539 H H    A ILE   A 1 106 ? 21.759 -8.608  -13.158 0.34 28.17 ?  106 ILE   A H    1 
ATOM   2540 H H    B ILE   A 1 106 ? 22.043 -9.150  -13.239 0.66 20.39 ?  106 ILE   A H    1 
ATOM   2541 H HA   A ILE   A 1 106 ? 21.597 -8.310  -10.574 0.34 27.50 ?  106 ILE   A HA   1 
ATOM   2542 H HA   B ILE   A 1 106 ? 21.649 -8.759  -10.714 0.66 20.37 ?  106 ILE   A HA   1 
ATOM   2543 H HB   A ILE   A 1 106 ? 19.701 -8.330  -12.081 0.34 27.07 ?  106 ILE   A HB   1 
ATOM   2544 H HB   B ILE   A 1 106 ? 19.900 -9.028  -12.354 0.66 22.84 ?  106 ILE   A HB   1 
ATOM   2545 H HG12 A ILE   A 1 106 ? 18.204 -9.120  -10.472 0.34 27.13 ?  106 ILE   A HG12 1 
ATOM   2546 H HG12 B ILE   A 1 106 ? 18.351 -9.966  -10.869 0.66 23.64 ?  106 ILE   A HG12 1 
ATOM   2547 H HG13 A ILE   A 1 106 ? 19.388 -9.864  -9.721  0.34 27.13 ?  106 ILE   A HG13 1 
ATOM   2548 H HG13 B ILE   A 1 106 ? 19.537 -10.542 -9.987  0.66 23.64 ?  106 ILE   A HG13 1 
ATOM   2549 H HG21 A ILE   A 1 106 ? 18.785 -10.273 -12.733 0.34 26.75 ?  106 ILE   A HG21 1 
ATOM   2550 H HG21 B ILE   A 1 106 ? 19.217 -11.108 -12.953 0.66 23.82 ?  106 ILE   A HG21 1 
ATOM   2551 H HG22 A ILE   A 1 106 ? 20.336 -10.478 -13.005 0.34 26.75 ?  106 ILE   A HG22 1 
ATOM   2552 H HG22 B ILE   A 1 106 ? 20.788 -11.092 -13.194 0.66 23.82 ?  106 ILE   A HG22 1 
ATOM   2553 H HG23 A ILE   A 1 106 ? 19.666 -11.115 -11.714 0.34 26.75 ?  106 ILE   A HG23 1 
ATOM   2554 H HG23 B ILE   A 1 106 ? 20.186 -11.794 -11.902 0.66 23.82 ?  106 ILE   A HG23 1 
ATOM   2555 H HD11 A ILE   A 1 106 ? 18.621 -7.753  -8.791  0.34 27.20 ?  106 ILE   A HD11 1 
ATOM   2556 H HD11 B ILE   A 1 106 ? 18.460 -8.551  -9.170  0.66 24.54 ?  106 ILE   A HD11 1 
ATOM   2557 H HD12 A ILE   A 1 106 ? 20.190 -7.974  -8.882  0.34 27.20 ?  106 ILE   A HD12 1 
ATOM   2558 H HD12 B ILE   A 1 106 ? 20.048 -8.532  -9.180  0.66 24.54 ?  106 ILE   A HD12 1 
ATOM   2559 H HD13 A ILE   A 1 106 ? 19.447 -7.082  -9.969  0.34 27.20 ?  106 ILE   A HD13 1 
ATOM   2560 H HD13 B ILE   A 1 106 ? 19.235 -7.785  -10.325 0.66 24.54 ?  106 ILE   A HD13 1 
ATOM   2561 N N    A GLN   A 1 107 ? 22.749 -11.080 -11.438 0.34 23.59 ?  107 GLN   A N    1 
ATOM   2562 N N    B GLN   A 1 107 ? 22.977 -11.544 -11.319 0.66 16.81 ?  107 GLN   A N    1 
ATOM   2563 C CA   A GLN   A 1 107 ? 23.325 -12.317 -10.922 0.34 24.47 ?  107 GLN   A CA   1 
ATOM   2564 C CA   B GLN   A 1 107 ? 23.610 -12.690 -10.670 0.66 19.03 ?  107 GLN   A CA   1 
ATOM   2565 C C    A GLN   A 1 107 ? 24.327 -12.056 -9.804  0.34 22.15 ?  107 GLN   A C    1 
ATOM   2566 C C    B GLN   A 1 107 ? 24.540 -12.251 -9.547  0.66 16.32 ?  107 GLN   A C    1 
ATOM   2567 O O    A GLN   A 1 107 ? 24.576 -12.950 -8.988  0.34 22.99 ?  107 GLN   A O    1 
ATOM   2568 O O    B GLN   A 1 107 ? 24.781 -13.011 -8.599  0.66 16.68 ?  107 GLN   A O    1 
ATOM   2569 C CB   A GLN   A 1 107 ? 23.998 -13.096 -12.056 0.34 27.86 ?  107 GLN   A CB   1 
ATOM   2570 C CB   B GLN   A 1 107 ? 24.374 -13.526 -11.705 0.66 24.68 ?  107 GLN   A CB   1 
ATOM   2571 C CG   A GLN   A 1 107 ? 23.104 -13.324 -13.267 0.34 31.17 ?  107 GLN   A CG   1 
ATOM   2572 C CG   B GLN   A 1 107 ? 23.492 -14.087 -12.814 0.66 30.92 ?  107 GLN   A CG   1 
ATOM   2573 C CD   A GLN   A 1 107 ? 21.834 -14.076 -12.923 0.34 33.87 ?  107 GLN   A CD   1 
ATOM   2574 C CD   B GLN   A 1 107 ? 22.409 -15.006 -12.285 0.66 36.06 ?  107 GLN   A CD   1 
ATOM   2575 O OE1  A GLN   A 1 107 ? 21.872 -15.111 -12.257 0.34 34.87 ?  107 GLN   A OE1  1 
ATOM   2576 O OE1  B GLN   A 1 107 ? 22.649 -15.818 -11.391 0.66 37.57 ?  107 GLN   A OE1  1 
ATOM   2577 N NE2  A GLN   A 1 107 ? 20.699 -13.555 -13.371 0.34 34.74 ?  107 GLN   A NE2  1 
ATOM   2578 N NE2  B GLN   A 1 107 ? 21.204 -14.875 -12.829 0.66 37.57 ?  107 GLN   A NE2  1 
ATOM   2579 H H    A GLN   A 1 107 ? 22.927 -10.922 -12.263 0.34 28.46 ?  107 GLN   A H    1 
ATOM   2580 H H    B GLN   A 1 107 ? 23.134 -11.486 -12.164 0.66 20.32 ?  107 GLN   A H    1 
ATOM   2581 H HA   A GLN   A 1 107 ? 22.617 -12.872 -10.563 0.34 29.51 ?  107 GLN   A HA   1 
ATOM   2582 H HA   B GLN   A 1 107 ? 22.933 -13.255 -10.283 0.66 22.99 ?  107 GLN   A HA   1 
ATOM   2583 H HB2  A GLN   A 1 107 ? 24.779 -12.605 -12.355 0.34 33.59 ?  107 GLN   A HB2  1 
ATOM   2584 H HB2  B GLN   A 1 107 ? 25.054 -12.976 -12.125 0.66 29.77 ?  107 GLN   A HB2  1 
ATOM   2585 H HB3  A GLN   A 1 107 ? 24.267 -13.968 -11.723 0.34 33.59 ?  107 GLN   A HB3  1 
ATOM   2586 H HB3  B GLN   A 1 107 ? 24.794 -14.281 -11.260 0.66 29.77 ?  107 GLN   A HB3  1 
ATOM   2587 H HG2  A GLN   A 1 107 ? 22.850 -12.467 -13.643 0.34 37.56 ?  107 GLN   A HG2  1 
ATOM   2588 H HG2  B GLN   A 1 107 ? 23.063 -13.352 -13.280 0.66 37.26 ?  107 GLN   A HG2  1 
ATOM   2589 H HG3  A GLN   A 1 107 ? 23.592 -13.842 -13.926 0.34 37.56 ?  107 GLN   A HG3  1 
ATOM   2590 H HG3  B GLN   A 1 107 ? 24.042 -14.595 -13.434 0.66 37.26 ?  107 GLN   A HG3  1 
ATOM   2591 H HE21 A GLN   A 1 107 ? 20.710 -12.829 -13.832 0.34 41.84 ?  107 GLN   A HE21 1 
ATOM   2592 H HE21 B GLN   A 1 107 ? 21.073 -14.295 -13.450 0.66 45.23 ?  107 GLN   A HE21 1 
ATOM   2593 H HE22 A GLN   A 1 107 ? 19.952 -13.945 -13.202 0.34 41.84 ?  107 GLN   A HE22 1 
ATOM   2594 H HE22 B GLN   A 1 107 ? 20.557 -15.373 -12.561 0.66 45.23 ?  107 GLN   A HE22 1 
ATOM   2595 N N    A LEU   A 1 108 ? 24.902 -10.852 -9.745  0.34 19.24 ?  108 LEU   A N    1 
ATOM   2596 N N    B LEU   A 1 108 ? 25.063 -11.026 -9.627  0.66 14.30 ?  108 LEU   A N    1 
ATOM   2597 C CA   A LEU   A 1 108 ? 25.848 -10.497 -8.692  0.34 16.80 ?  108 LEU   A CA   1 
ATOM   2598 C CA   B LEU   A 1 108 ? 25.932 -10.514 -8.579  0.66 13.82 ?  108 LEU   A CA   1 
ATOM   2599 C C    A LEU   A 1 108 ? 25.178 -10.315 -7.333  0.34 14.57 ?  108 LEU   A C    1 
ATOM   2600 C C    B LEU   A 1 108 ? 25.183 -10.264 -7.279  0.66 12.90 ?  108 LEU   A C    1 
ATOM   2601 O O    A LEU   A 1 108 ? 25.883 -10.180 -6.326  0.34 14.47 ?  108 LEU   A O    1 
ATOM   2602 O O    B LEU   A 1 108 ? 25.833 -10.046 -6.249  0.66 13.24 ?  108 LEU   A O    1 
ATOM   2603 C CB   A LEU   A 1 108 ? 26.597 -9.221  -9.083  0.34 16.70 ?  108 LEU   A CB   1 
ATOM   2604 C CB   B LEU   A 1 108 ? 26.658 -9.248  -9.048  0.66 14.30 ?  108 LEU   A CB   1 
ATOM   2605 C CG   A LEU   A 1 108 ? 27.535 -9.353  -10.285 0.34 17.18 ?  108 LEU   A CG   1 
ATOM   2606 C CG   B LEU   A 1 108 ? 27.694 -9.485  -10.151 0.66 16.02 ?  108 LEU   A CG   1 
ATOM   2607 C CD1  A LEU   A 1 108 ? 27.916 -7.987  -10.831 0.34 17.44 ?  108 LEU   A CD1  1 
ATOM   2608 C CD1  B LEU   A 1 108 ? 28.147 -8.177  -10.781 0.66 16.73 ?  108 LEU   A CD1  1 
ATOM   2609 C CD2  A LEU   A 1 108 ? 28.781 -10.136 -9.897  0.34 17.92 ?  108 LEU   A CD2  1 
ATOM   2610 C CD2  B LEU   A 1 108 ? 28.892 -10.247 -9.600  0.66 17.56 ?  108 LEU   A CD2  1 
ATOM   2611 H H    A LEU   A 1 108 ? 24.760 -10.227 -10.314 0.34 23.24 ?  108 LEU   A H    1 
ATOM   2612 H H    B LEU   A 1 108 ? 24.927 -10.477 -10.277 0.66 17.31 ?  108 LEU   A H    1 
ATOM   2613 H HA   A LEU   A 1 108 ? 26.499 -11.209 -8.607  0.34 20.31 ?  108 LEU   A HA   1 
ATOM   2614 H HA   B LEU   A 1 108 ? 26.607 -11.185 -8.395  0.66 16.73 ?  108 LEU   A HA   1 
ATOM   2615 H HB2  A LEU   A 1 108 ? 25.946 -8.536  -9.299  0.34 20.19 ?  108 LEU   A HB2  1 
ATOM   2616 H HB2  B LEU   A 1 108 ? 26.002 -8.624  -9.390  0.66 17.31 ?  108 LEU   A HB2  1 
ATOM   2617 H HB3  A LEU   A 1 108 ? 27.133 -8.936  -8.329  0.34 20.19 ?  108 LEU   A HB3  1 
ATOM   2618 H HB3  B LEU   A 1 108 ? 27.119 -8.861  -8.290  0.66 17.31 ?  108 LEU   A HB3  1 
ATOM   2619 H HG   A LEU   A 1 108 ? 27.082 -9.842  -10.991 0.34 20.76 ?  108 LEU   A HG   1 
ATOM   2620 H HG   B LEU   A 1 108 ? 27.292 -10.027 -10.848 0.66 19.38 ?  108 LEU   A HG   1 
ATOM   2621 H HD11 A LEU   A 1 108 ? 28.419 -8.104  -11.652 0.34 21.08 ?  108 LEU   A HD11 1 
ATOM   2622 H HD11 B LEU   A 1 108 ? 28.794 -8.370  -11.478 0.66 20.23 ?  108 LEU   A HD11 1 
ATOM   2623 H HD12 A LEU   A 1 108 ? 27.109 -7.480  -11.007 0.34 21.08 ?  108 LEU   A HD12 1 
ATOM   2624 H HD12 B LEU   A 1 108 ? 27.376 -7.726  -11.160 0.66 20.23 ?  108 LEU   A HD12 1 
ATOM   2625 H HD13 A LEU   A 1 108 ? 28.461 -7.526  -10.174 0.34 21.08 ?  108 LEU   A HD13 1 
ATOM   2626 H HD13 B LEU   A 1 108 ? 28.553 -7.621  -10.097 0.66 20.23 ?  108 LEU   A HD13 1 
ATOM   2627 H HD21 A LEU   A 1 108 ? 29.387 -10.162 -10.653 0.34 21.66 ?  108 LEU   A HD21 1 
ATOM   2628 H HD21 B LEU   A 1 108 ? 29.591 -10.261 -10.271 0.66 21.22 ?  108 LEU   A HD21 1 
ATOM   2629 H HD22 A LEU   A 1 108 ? 29.209 -9.695  -9.145  0.34 21.66 ?  108 LEU   A HD22 1 
ATOM   2630 H HD22 B LEU   A 1 108 ? 29.209 -9.799  -8.800  0.66 21.22 ?  108 LEU   A HD22 1 
ATOM   2631 H HD23 A LEU   A 1 108 ? 28.523 -11.037 -9.647  0.34 21.66 ?  108 LEU   A HD23 1 
ATOM   2632 H HD23 B LEU   A 1 108 ? 28.619 -11.153 -9.386  0.66 21.22 ?  108 LEU   A HD23 1 
ATOM   2633 N N    . LEU   A 1 109 ? 23.844 -10.325 -7.285  1.00 13.13 ?  109 LEU   A N    1 
ATOM   2634 C CA   . LEU   A 1 109 ? 23.129 -10.183 -6.026  1.00 12.31 ?  109 LEU   A CA   1 
ATOM   2635 C C    . LEU   A 1 109 ? 23.439 -11.343 -5.085  1.00 11.78 ?  109 LEU   A C    1 
ATOM   2636 O O    . LEU   A 1 109 ? 23.542 -11.155 -3.871  1.00 12.19 ?  109 LEU   A O    1 
ATOM   2637 C CB   . LEU   A 1 109 ? 21.625 -10.087 -6.298  1.00 13.27 ?  109 LEU   A CB   1 
ATOM   2638 C CG   . LEU   A 1 109 ? 20.712 -9.802  -5.106  1.00 13.91 ?  109 LEU   A CG   1 
ATOM   2639 C CD1  . LEU   A 1 109 ? 21.144 -8.541  -4.383  1.00 14.29 ?  109 LEU   A CD1  1 
ATOM   2640 C CD2  . LEU   A 1 109 ? 19.267 -9.664  -5.566  1.00 15.26 ?  109 LEU   A CD2  1 
ATOM   2641 H H    A LEU   A 1 109 ? 23.332 -10.420 -7.969  0.34 15.91 ?  109 LEU   A H    1 
ATOM   2642 H H    B LEU   A 1 109 ? 23.350 -10.448 -7.978  0.66 15.91 ?  109 LEU   A H    1 
ATOM   2643 H HA   . LEU   A 1 109 ? 23.415 -9.360  -5.597  1.00 14.93 ?  109 LEU   A HA   1 
ATOM   2644 H HB2  . LEU   A 1 109 ? 21.479 -9.375  -6.939  1.00 16.08 ?  109 LEU   A HB2  1 
ATOM   2645 H HB3  . LEU   A 1 109 ? 21.333 -10.927 -6.677  1.00 16.08 ?  109 LEU   A HB3  1 
ATOM   2646 H HG   . LEU   A 1 109 ? 20.757 -10.536 -4.476  1.00 16.84 ?  109 LEU   A HG   1 
ATOM   2647 H HD11 . LEU   A 1 109 ? 20.466 -8.295  -3.736  1.00 17.30 ?  109 LEU   A HD11 1 
ATOM   2648 H HD12 . LEU   A 1 109 ? 21.988 -8.703  -3.937  1.00 17.30 ?  109 LEU   A HD12 1 
ATOM   2649 H HD13 . LEU   A 1 109 ? 21.248 -7.824  -5.036  1.00 17.30 ?  109 LEU   A HD13 1 
ATOM   2650 H HD21 . LEU   A 1 109 ? 18.718 -9.383  -4.814  1.00 18.46 ?  109 LEU   A HD21 1 
ATOM   2651 H HD22 . LEU   A 1 109 ? 19.221 -8.996  -6.270  1.00 18.46 ?  109 LEU   A HD22 1 
ATOM   2652 H HD23 . LEU   A 1 109 ? 18.957 -10.518 -5.900  1.00 18.46 ?  109 LEU   A HD23 1 
ATOM   2653 N N    . LYS   A 1 110 ? 23.592 -12.558 -5.621  1.00 11.84 ?  110 LYS   A N    1 
ATOM   2654 C CA   . LYS   A 1 110 ? 23.959 -13.679 -4.760  1.00 11.63 ?  110 LYS   A CA   1 
ATOM   2655 C C    . LYS   A 1 110 ? 25.331 -13.450 -4.137  1.00 11.32 ?  110 LYS   A C    1 
ATOM   2656 O O    . LYS   A 1 110 ? 25.513 -13.656 -2.933  1.00 11.63 ?  110 LYS   A O    1 
ATOM   2657 C CB   . LYS   A 1 110 ? 23.899 -14.998 -5.528  1.00 12.91 ?  110 LYS   A CB   1 
ATOM   2658 C CG   . LYS   A 1 110 ? 24.071 -16.206 -4.623  1.00 12.75 ?  110 LYS   A CG   1 
ATOM   2659 C CD   . LYS   A 1 110 ? 23.832 -17.521 -5.354  1.00 13.20 ?  110 LYS   A CD   1 
ATOM   2660 C CE   . LYS   A 1 110 ? 23.930 -18.721 -4.422  1.00 14.05 ?  110 LYS   A CE   1 
ATOM   2661 N NZ   . LYS   A 1 110 ? 22.752 -18.846 -3.525  1.00 14.55 ?  110 LYS   A NZ   1 
ATOM   2662 H H    . LYS   A 1 110 ? 23.492 -12.750 -6.451  1.00 14.36 ?  110 LYS   A H    1 
ATOM   2663 H HA   . LYS   A 1 110 ? 23.312 -13.732 -4.037  1.00 14.11 ?  110 LYS   A HA   1 
ATOM   2664 H HB2  . LYS   A 1 110 ? 23.039 -15.072 -5.967  1.00 15.65 ?  110 LYS   A HB2  1 
ATOM   2665 H HB3  . LYS   A 1 110 ? 24.613 -15.015 -6.184  1.00 15.65 ?  110 LYS   A HB3  1 
ATOM   2666 H HG2  . LYS   A 1 110 ? 24.973 -16.217 -4.269  1.00 15.45 ?  110 LYS   A HG2  1 
ATOM   2667 H HG3  . LYS   A 1 110 ? 23.430 -16.149 -3.893  1.00 15.45 ?  110 LYS   A HG3  1 
ATOM   2668 H HD2  . LYS   A 1 110 ? 22.945 -17.508 -5.740  1.00 16.00 ?  110 LYS   A HD2  1 
ATOM   2669 H HD3  . LYS   A 1 110 ? 24.502 -17.616 -6.047  1.00 16.00 ?  110 LYS   A HD3  1 
ATOM   2670 H HE2  . LYS   A 1 110 ? 23.995 -19.528 -4.954  1.00 17.01 ?  110 LYS   A HE2  1 
ATOM   2671 H HE3  . LYS   A 1 110 ? 24.724 -18.627 -3.865  1.00 17.01 ?  110 LYS   A HE3  1 
ATOM   2672 H HZ1  . LYS   A 1 110 ? 22.843 -19.556 -2.999  1.00 17.61 ?  110 LYS   A HZ1  1 
ATOM   2673 H HZ2  . LYS   A 1 110 ? 22.675 -18.117 -3.020  1.00 17.61 ?  110 LYS   A HZ2  1 
ATOM   2674 H HZ3  . LYS   A 1 110 ? 22.011 -18.938 -4.012  1.00 17.61 ?  110 LYS   A HZ3  1 
ATOM   2675 N N    . SER   A 1 111 ? 26.297 -12.986 -4.937  1.00 11.53 ?  111 SER   A N    1 
ATOM   2676 C CA   . SER   A 1 111 ? 27.621 -12.690 -4.402  1.00 11.44 ?  111 SER   A CA   1 
ATOM   2677 C C    . SER   A 1 111 ? 27.541 -11.642 -3.297  1.00 10.93 ?  111 SER   A C    1 
ATOM   2678 O O    . SER   A 1 111 ? 28.233 -11.744 -2.276  1.00 11.38 ?  111 SER   A O    1 
ATOM   2679 C CB   . SER   A 1 111 ? 28.528 -12.206 -5.533  1.00 12.85 ?  111 SER   A CB   1 
ATOM   2680 O OG   . SER   A 1 111 ? 28.571 -13.167 -6.577  1.00 14.89 ?  111 SER   A OG   1 
ATOM   2681 H H    . SER   A 1 111 ? 26.201 -12.832 -5.775  1.00 13.99 ?  111 SER   A H    1 
ATOM   2682 H HA   . SER   A 1 111 ? 27.999 -13.503 -4.030  1.00 13.88 ?  111 SER   A HA   1 
ATOM   2683 H HB2  . SER   A 1 111 ? 28.172 -11.379 -5.890  1.00 15.57 ?  111 SER   A HB2  1 
ATOM   2684 H HB3  . SER   A 1 111 ? 29.419 -12.065 -5.182  1.00 15.57 ?  111 SER   A HB3  1 
ATOM   2685 H HG   . SER   A 1 111 ? 29.087 -12.900 -7.190  1.00 18.02 ?  111 SER   A HG   1 
ATOM   2686 N N    . ALA   A 1 112 ? 26.694 -10.629 -3.485  1.00 11.01 ?  112 ALA   A N    1 
ATOM   2687 C CA   . ALA   A 1 112 ? 26.526 -9.590  -2.470  1.00 10.83 ?  112 ALA   A CA   1 
ATOM   2688 C C    . ALA   A 1 112 ? 26.039 -10.194 -1.155  1.00 10.45 ?  112 ALA   A C    1 
ATOM   2689 O O    . ALA   A 1 112 ? 26.582 -9.909  -0.083  1.00 11.10 ?  112 ALA   A O    1 
ATOM   2690 C CB   . ALA   A 1 112 ? 25.553 -8.518  -2.974  1.00 11.62 ?  112 ALA   A CB   1 
ATOM   2691 H H    . ALA   A 1 112 ? 26.217 -10.516 -4.189  1.00 13.36 ?  112 ALA   A H    1 
ATOM   2692 H HA   . ALA   A 1 112 ? 27.380 -9.163  -2.306  1.00 13.15 ?  112 ALA   A HA   1 
ATOM   2693 H HB1  . ALA   A 1 112 ? 25.454 -7.833  -2.289  1.00 14.10 ?  112 ALA   A HB1  1 
ATOM   2694 H HB2  . ALA   A 1 112 ? 25.911 -8.120  -3.784  1.00 14.10 ?  112 ALA   A HB2  1 
ATOM   2695 H HB3  . ALA   A 1 112 ? 24.694 -8.926  -3.157  1.00 14.10 ?  112 ALA   A HB3  1 
ATOM   2696 N N    A TYR   A 1 113 ? 25.010 -11.042 -1.221  0.34 10.59 ?  113 TYR   A N    1 
ATOM   2697 N N    B TYR   A 1 113 ? 25.002 -11.033 -1.215  0.66 10.77 ?  113 TYR   A N    1 
ATOM   2698 C CA   A TYR   A 1 113 ? 24.474 -11.647 -0.005  0.34 10.48 ?  113 TYR   A CA   1 
ATOM   2699 C CA   B TYR   A 1 113 ? 24.482 -11.638 0.009   0.66 10.57 ?  113 TYR   A CA   1 
ATOM   2700 C C    A TYR   A 1 113 ? 25.467 -12.609 0.648   0.34 10.29 ?  113 TYR   A C    1 
ATOM   2701 C C    B TYR   A 1 113 ? 25.483 -12.594 0.656   0.66 10.28 ?  113 TYR   A C    1 
ATOM   2702 O O    A TYR   A 1 113 ? 25.412 -12.810 1.866   0.34 10.65 ?  113 TYR   A O    1 
ATOM   2703 O O    B TYR   A 1 113 ? 25.449 -12.777 1.878   0.66 10.89 ?  113 TYR   A O    1 
ATOM   2704 C CB   A TYR   A 1 113 ? 23.140 -12.346 -0.295  0.34 10.65 ?  113 TYR   A CB   1 
ATOM   2705 C CB   B TYR   A 1 113 ? 23.160 -12.361 -0.261  0.66 10.82 ?  113 TYR   A CB   1 
ATOM   2706 C CG   A TYR   A 1 113 ? 21.924 -11.436 -0.216  0.34 10.76 ?  113 TYR   A CG   1 
ATOM   2707 C CG   B TYR   A 1 113 ? 21.949 -11.452 -0.280  0.66 11.18 ?  113 TYR   A CG   1 
ATOM   2708 C CD1  A TYR   A 1 113 ? 21.565 -10.825 0.982   0.34 10.94 ?  113 TYR   A CD1  1 
ATOM   2709 C CD1  B TYR   A 1 113 ? 21.550 -10.764 0.864   0.66 11.59 ?  113 TYR   A CD1  1 
ATOM   2710 C CD2  A TYR   A 1 113 ? 21.125 -11.204 -1.331  0.34 10.94 ?  113 TYR   A CD2  1 
ATOM   2711 C CD2  B TYR   A 1 113 ? 21.195 -11.298 -1.433  0.66 11.82 ?  113 TYR   A CD2  1 
ATOM   2712 C CE1  A TYR   A 1 113 ? 20.450 -10.005 1.067   0.34 11.19 ?  113 TYR   A CE1  1 
ATOM   2713 C CE1  B TYR   A 1 113 ? 20.431 -9.946  0.852   0.66 11.94 ?  113 TYR   A CE1  1 
ATOM   2714 C CE2  A TYR   A 1 113 ? 20.000 -10.381 -1.255  0.34 10.95 ?  113 TYR   A CE2  1 
ATOM   2715 C CE2  B TYR   A 1 113 ? 20.067 -10.484 -1.454  0.66 12.30 ?  113 TYR   A CE2  1 
ATOM   2716 C CZ   A TYR   A 1 113 ? 19.673 -9.784  -0.053  0.34 10.71 ?  113 TYR   A CZ   1 
ATOM   2717 C CZ   B TYR   A 1 113 ? 19.692 -9.813  -0.309  0.66 12.18 ?  113 TYR   A CZ   1 
ATOM   2718 O OH   A TYR   A 1 113 ? 18.560 -8.972  0.038   0.34 10.56 ?  113 TYR   A OH   1 
ATOM   2719 O OH   B TYR   A 1 113 ? 18.574 -9.004  -0.329  0.66 13.45 ?  113 TYR   A OH   1 
ATOM   2720 H H    A TYR   A 1 113 ? 24.612 -11.273 -1.946  0.34 12.85 ?  113 TYR   A H    1 
ATOM   2721 H H    B TYR   A 1 113 ? 24.592 -11.260 -1.936  0.66 13.07 ?  113 TYR   A H    1 
ATOM   2722 H HA   A TYR   A 1 113 ? 24.299 -10.943 0.632   0.34 12.72 ?  113 TYR   A HA   1 
ATOM   2723 H HA   B TYR   A 1 113 ? 24.307 -10.936 0.649   0.66 12.83 ?  113 TYR   A HA   1 
ATOM   2724 H HB2  A TYR   A 1 113 ? 23.170 -12.717 -1.191  0.34 12.93 ?  113 TYR   A HB2  1 
ATOM   2725 H HB2  B TYR   A 1 113 ? 23.214 -12.795 -1.129  0.66 13.14 ?  113 TYR   A HB2  1 
ATOM   2726 H HB3  A TYR   A 1 113 ? 23.016 -13.058 0.350   0.34 12.93 ?  113 TYR   A HB3  1 
ATOM   2727 H HB3  B TYR   A 1 113 ? 23.021 -13.027 0.429   0.66 13.14 ?  113 TYR   A HB3  1 
ATOM   2728 H HD1  A TYR   A 1 113 ? 22.082 -10.973 1.740   0.34 13.28 ?  113 TYR   A HD1  1 
ATOM   2729 H HD1  B TYR   A 1 113 ? 22.041 -10.862 1.651   0.66 14.06 ?  113 TYR   A HD1  1 
ATOM   2730 H HD2  A TYR   A 1 113 ? 21.342 -11.606 -2.142  0.34 13.28 ?  113 TYR   A HD2  1 
ATOM   2731 H HD2  B TYR   A 1 113 ? 21.443 -11.754 -2.203  0.66 14.33 ?  113 TYR   A HD2  1 
ATOM   2732 H HE1  A TYR   A 1 113 ? 20.224 -9.609  1.877   0.34 13.58 ?  113 TYR   A HE1  1 
ATOM   2733 H HE1  B TYR   A 1 113 ? 20.175 -9.502  1.627   0.66 14.48 ?  113 TYR   A HE1  1 
ATOM   2734 H HE2  A TYR   A 1 113 ? 19.472 -10.234 -2.009  0.34 13.29 ?  113 TYR   A HE2  1 
ATOM   2735 H HE2  B TYR   A 1 113 ? 19.568 -10.389 -2.233  0.66 14.92 ?  113 TYR   A HE2  1 
ATOM   2736 H HH   A TYR   A 1 113 ? 18.177 -8.928  -0.709  0.34 12.82 ?  113 TYR   A HH   1 
ATOM   2737 H HH   B TYR   A 1 113 ? 18.221 -9.023  -1.093  0.66 16.29 ?  113 TYR   A HH   1 
ATOM   2738 N N    . GLU   A 1 114 ? 26.383 -13.205 -0.129  1.00 10.46 ?  114 GLU   A N    1 
ATOM   2739 C CA   . GLU   A 1 114 ? 27.378 -14.104 0.461   1.00 11.19 ?  114 GLU   A CA   1 
ATOM   2740 C C    . GLU   A 1 114 ? 28.222 -13.396 1.516   1.00 10.81 ?  114 GLU   A C    1 
ATOM   2741 O O    . GLU   A 1 114 ? 28.701 -14.035 2.463   1.00 10.96 ?  114 GLU   A O    1 
ATOM   2742 C CB   . GLU   A 1 114 ? 28.256 -14.740 -0.630  1.00 11.15 ?  114 GLU   A CB   1 
ATOM   2743 C CG   . GLU   A 1 114 ? 27.508 -15.799 -1.415  1.00 11.76 ?  114 GLU   A CG   1 
ATOM   2744 C CD   . GLU   A 1 114 ? 28.233 -16.319 -2.652  1.00 11.80 ?  114 GLU   A CD   1 
ATOM   2745 O OE1  . GLU   A 1 114 ? 29.181 -15.682 -3.157  1.00 12.09 ?  114 GLU   A OE1  1 
ATOM   2746 O OE2  . GLU   A 1 114 ? 27.808 -17.391 -3.145  1.00 13.23 -1 114 GLU   A OE2  1 
ATOM   2747 H H    A GLU   A 1 114 ? 26.440 -13.109 -0.983  0.34 12.70 ?  114 GLU   A H    1 
ATOM   2748 H H    B GLU   A 1 114 ? 26.430 -13.118 -0.985  0.66 12.70 ?  114 GLU   A H    1 
ATOM   2749 H HA   . GLU   A 1 114 ? 26.906 -14.824 0.903   1.00 13.58 ?  114 GLU   A HA   1 
ATOM   2750 H HB2  . GLU   A 1 114 ? 28.541 -14.054 -1.255  1.00 13.53 ?  114 GLU   A HB2  1 
ATOM   2751 H HB3  . GLU   A 1 114 ? 29.022 -15.161 -0.219  1.00 13.53 ?  114 GLU   A HB3  1 
ATOM   2752 H HG2  . GLU   A 1 114 ? 27.349 -16.558 -0.834  1.00 14.26 ?  114 GLU   A HG2  1 
ATOM   2753 H HG3  . GLU   A 1 114 ? 26.658 -15.430 -1.704  1.00 14.26 ?  114 GLU   A HG3  1 
ATOM   2754 N N    . ASN   A 1 115 ? 28.411 -12.079 1.383   1.00 10.76 ?  115 ASN   A N    1 
ATOM   2755 C CA   . ASN   A 1 115 ? 29.181 -11.351 2.386   1.00 10.85 ?  115 ASN   A CA   1 
ATOM   2756 C C    . ASN   A 1 115 ? 28.556 -11.469 3.773   1.00 10.90 ?  115 ASN   A C    1 
ATOM   2757 O O    . ASN   A 1 115 ? 29.269 -11.396 4.783   1.00 11.34 ?  115 ASN   A O    1 
ATOM   2758 C CB   . ASN   A 1 115 ? 29.299 -9.881  1.995   1.00 11.02 ?  115 ASN   A CB   1 
ATOM   2759 C CG   . ASN   A 1 115 ? 30.096 -9.681  0.730   1.00 11.47 ?  115 ASN   A CG   1 
ATOM   2760 O OD1  . ASN   A 1 115 ? 31.311 -9.813  0.738   1.00 15.02 ?  115 ASN   A OD1  1 
ATOM   2761 N ND2  . ASN   A 1 115 ? 29.424 -9.351  -0.357  1.00 11.29 ?  115 ASN   A ND2  1 
ATOM   2762 H H    . ASN   A 1 115 ? 28.107 -11.591 0.740   1.00 13.06 ?  115 ASN   A H    1 
ATOM   2763 H HA   . ASN   A 1 115 ? 30.077 -11.725 2.425   1.00 13.18 ?  115 ASN   A HA   1 
ATOM   2764 H HB2  . ASN   A 1 115 ? 28.412 -9.518  1.859   1.00 13.38 ?  115 ASN   A HB2  1 
ATOM   2765 H HB3  . ASN   A 1 115 ? 29.748 -9.400  2.710   1.00 13.38 ?  115 ASN   A HB3  1 
ATOM   2766 H HD21 . ASN   A 1 115 ? 29.840 -9.218  -1.100  1.00 13.70 ?  115 ASN   A HD21 1 
ATOM   2767 H HD22 . ASN   A 1 115 ? 28.569 -9.269  -0.325  1.00 13.70 ?  115 ASN   A HD22 1 
ATOM   2768 N N    . PHE   A 1 116 ? 27.231 -11.636 3.849   1.00 10.84 ?  116 PHE   A N    1 
ATOM   2769 C CA   . PHE   A 1 116 ? 26.578 -11.725 5.153   1.00 10.79 ?  116 PHE   A CA   1 
ATOM   2770 C C    . PHE   A 1 116 ? 27.048 -12.953 5.935   1.00 10.77 ?  116 PHE   A C    1 
ATOM   2771 O O    . PHE   A 1 116 ? 26.969 -12.967 7.164   1.00 11.50 ?  116 PHE   A O    1 
ATOM   2772 C CB   . PHE   A 1 116 ? 25.053 -11.858 5.015   1.00 11.01 ?  116 PHE   A CB   1 
ATOM   2773 C CG   . PHE   A 1 116 ? 24.294 -10.624 4.510   1.00 10.73 ?  116 PHE   A CG   1 
ATOM   2774 C CD1  . PHE   A 1 116 ? 24.862 -9.621  3.732   1.00 11.02 ?  116 PHE   A CD1  1 
ATOM   2775 C CD2  . PHE   A 1 116 ? 22.943 -10.514 4.830   1.00 11.32 ?  116 PHE   A CD2  1 
ATOM   2776 C CE1  . PHE   A 1 116 ? 24.094 -8.559  3.282   1.00 11.38 ?  116 PHE   A CE1  1 
ATOM   2777 C CE2  . PHE   A 1 116 ? 22.172 -9.454  4.392   1.00 11.64 ?  116 PHE   A CE2  1 
ATOM   2778 C CZ   . PHE   A 1 116 ? 22.743 -8.476  3.616   1.00 11.35 ?  116 PHE   A CZ   1 
ATOM   2779 H H    . PHE   A 1 116 ? 26.701 -11.691 3.170   1.00 13.16 ?  116 PHE   A H    1 
ATOM   2780 H HA   . PHE   A 1 116 ? 26.780 -10.930 5.670   1.00 13.10 ?  116 PHE   A HA   1 
ATOM   2781 H HB2  . PHE   A 1 116 ? 24.867 -12.584 4.401   1.00 13.36 ?  116 PHE   A HB2  1 
ATOM   2782 H HB3  . PHE   A 1 116 ? 24.694 -12.083 5.891   1.00 13.36 ?  116 PHE   A HB3  1 
ATOM   2783 H HD1  . PHE   A 1 116 ? 25.755 -9.682  3.502   1.00 13.37 ?  116 PHE   A HD1  1 
ATOM   2784 H HD2  . PHE   A 1 116 ? 22.541 -11.182 5.345   1.00 13.73 ?  116 PHE   A HD2  1 
ATOM   2785 H HE1  . PHE   A 1 116 ? 24.483 -7.895  2.770   1.00 13.81 ?  116 PHE   A HE1  1 
ATOM   2786 H HE2  . PHE   A 1 116 ? 21.268 -9.405  4.620   1.00 14.12 ?  116 PHE   A HE2  1 
ATOM   2787 H HZ   . PHE   A 1 116 ? 22.232 -7.753  3.328   1.00 13.77 ?  116 PHE   A HZ   1 
ATOM   2788 N N    . ASN   A 1 117 ? 27.493 -14.007 5.245   1.00 11.03 ?  117 ASN   A N    1 
ATOM   2789 C CA   . ASN   A 1 117 ? 27.862 -15.246 5.923   1.00 11.24 ?  117 ASN   A CA   1 
ATOM   2790 C C    . ASN   A 1 117 ? 29.119 -15.120 6.764   1.00 11.79 ?  117 ASN   A C    1 
ATOM   2791 O O    . ASN   A 1 117 ? 29.416 -16.032 7.543   1.00 12.50 ?  117 ASN   A O    1 
ATOM   2792 C CB   . ASN   A 1 117 ? 27.990 -16.371 4.905   1.00 11.22 ?  117 ASN   A CB   1 
ATOM   2793 C CG   . ASN   A 1 117 ? 26.646 -16.763 4.355   1.00 11.46 ?  117 ASN   A CG   1 
ATOM   2794 O OD1  . ASN   A 1 117 ? 25.669 -16.800 5.098   1.00 12.38 ?  117 ASN   A OD1  1 
ATOM   2795 N ND2  . ASN   A 1 117 ? 26.568 -17.025 3.067   1.00 11.55 ?  117 ASN   A ND2  1 
ATOM   2796 H H    . ASN   A 1 117 ? 27.573 -14.029 4.388   1.00 13.39 ?  117 ASN   A H    1 
ATOM   2797 H HA   . ASN   A 1 117 ? 27.131 -15.479 6.521   1.00 13.64 ?  117 ASN   A HA   1 
ATOM   2798 H HB2  . ASN   A 1 117 ? 28.545 -16.068 4.166   1.00 13.61 ?  117 ASN   A HB2  1 
ATOM   2799 H HB3  . ASN   A 1 117 ? 28.391 -17.139 5.333   1.00 13.61 ?  117 ASN   A HB3  1 
ATOM   2800 H HD21 . ASN   A 1 117 ? 25.816 -17.247 2.728   1.00 14.01 ?  117 ASN   A HD21 1 
ATOM   2801 H HD22 . ASN   A 1 117 ? 27.273 -16.969 2.583   1.00 14.01 ?  117 ASN   A HD22 1 
ATOM   2802 N N    . GLN   A 1 118 ? 29.852 -14.014 6.639   1.00 11.49 ?  118 GLN   A N    1 
ATOM   2803 C CA   . GLN   A 1 118 ? 31.020 -13.779 7.472   1.00 12.18 ?  118 GLN   A CA   1 
ATOM   2804 C C    . GLN   A 1 118 ? 30.667 -13.199 8.835   1.00 12.59 ?  118 GLN   A C    1 
ATOM   2805 O O    . GLN   A 1 118 ? 31.583 -12.890 9.608   1.00 13.69 ?  118 GLN   A O    1 
ATOM   2806 C CB   . GLN   A 1 118 ? 32.023 -12.879 6.740   1.00 12.30 ?  118 GLN   A CB   1 
ATOM   2807 C CG   . GLN   A 1 118 ? 32.493 -13.458 5.414   1.00 12.67 ?  118 GLN   A CG   1 
ATOM   2808 C CD   . GLN   A 1 118 ? 33.327 -14.712 5.593   1.00 12.74 ?  118 GLN   A CD   1 
ATOM   2809 O OE1  . GLN   A 1 118 ? 34.187 -14.775 6.478   1.00 13.75 ?  118 GLN   A OE1  1 
ATOM   2810 N NE2  . GLN   A 1 118 ? 33.077 -15.721 4.754   1.00 13.01 ?  118 GLN   A NE2  1 
ATOM   2811 H H    . GLN   A 1 118 ? 29.681 -13.373 6.078   1.00 13.94 ?  118 GLN   A H    1 
ATOM   2812 H HA   . GLN   A 1 118 ? 31.446 -14.634 7.626   1.00 14.77 ?  118 GLN   A HA   1 
ATOM   2813 H HB2  . GLN   A 1 118 ? 31.606 -12.024 6.569   1.00 14.91 ?  118 GLN   A HB2  1 
ATOM   2814 H HB3  . GLN   A 1 118 ? 32.799 -12.763 7.313   1.00 14.91 ?  118 GLN   A HB3  1 
ATOM   2815 H HG2  . GLN   A 1 118 ? 31.724 -13.682 4.870   1.00 15.36 ?  118 GLN   A HG2  1 
ATOM   2816 H HG3  . GLN   A 1 118 ? 33.042 -12.798 4.960   1.00 15.36 ?  118 GLN   A HG3  1 
ATOM   2817 H HE21 . GLN   A 1 118 ? 32.457 -15.641 4.155   1.00 15.77 ?  118 GLN   A HE21 1 
ATOM   2818 H HE22 . GLN   A 1 118 ? 33.514 -16.457 4.816   1.00 15.77 ?  118 GLN   A HE22 1 
ATOM   2819 N N    . HIS   A 1 119 ? 29.376 -13.039 9.141   1.00 11.95 ?  119 HIS   A N    1 
ATOM   2820 C CA   . HIS   A 1 119 ? 28.918 -12.422 10.382  1.00 12.34 ?  119 HIS   A CA   1 
ATOM   2821 C C    . HIS   A 1 119 ? 27.781 -13.247 10.957  1.00 12.94 ?  119 HIS   A C    1 
ATOM   2822 O O    . HIS   A 1 119 ? 26.839 -13.594 10.238  1.00 13.16 ?  119 HIS   A O    1 
ATOM   2823 C CB   . HIS   A 1 119 ? 28.452 -10.993 10.105  1.00 12.88 ?  119 HIS   A CB   1 
ATOM   2824 C CG   . HIS   A 1 119 ? 29.524 -10.183 9.477   1.00 14.31 ?  119 HIS   A CG   1 
ATOM   2825 N ND1  . HIS   A 1 119 ? 30.497 -9.561  10.224  1.00 16.55 ?  119 HIS   A ND1  1 
ATOM   2826 C CD2  . HIS   A 1 119 ? 29.860 -10.004 8.179   1.00 15.50 ?  119 HIS   A CD2  1 
ATOM   2827 C CE1  . HIS   A 1 119 ? 31.364 -8.989  9.409   1.00 16.94 ?  119 HIS   A CE1  1 
ATOM   2828 N NE2  . HIS   A 1 119 ? 31.009 -9.253  8.163   1.00 16.76 ?  119 HIS   A NE2  1 
ATOM   2829 H H    . HIS   A 1 119 ? 28.726 -13.298 8.636   1.00 14.49 ?  119 HIS   A H    1 
ATOM   2830 H HA   . HIS   A 1 119 ? 29.641 -12.397 11.026  1.00 14.95 ?  119 HIS   A HA   1 
ATOM   2831 H HB2  . HIS   A 1 119 ? 27.694 -11.016 9.502   1.00 15.61 ?  119 HIS   A HB2  1 
ATOM   2832 H HB3  . HIS   A 1 119 ? 28.205 -10.571 10.943  1.00 15.61 ?  119 HIS   A HB3  1 
ATOM   2833 H HD2  . HIS   A 1 119 ? 29.406 -10.333 7.437   1.00 18.75 ?  119 HIS   A HD2  1 
ATOM   2834 H HE1  . HIS   A 1 119 ? 32.102 -8.484  9.666   1.00 20.48 ?  119 HIS   A HE1  1 
ATOM   2835 H HE2  . HIS   A 1 119 ? 31.415 -8.971  7.457   1.00 20.26 ?  119 HIS   A HE2  1 
ATOM   2836 N N    A GLU   A 1 120 ? 27.867 -13.564 12.251  0.34 14.34 ?  120 GLU   A N    1 
ATOM   2837 N N    B GLU   A 1 120 ? 27.868 -13.540 12.256  0.66 13.03 ?  120 GLU   A N    1 
ATOM   2838 C CA   A GLU   A 1 120 ? 26.901 -14.493 12.839  0.34 16.42 ?  120 GLU   A CA   1 
ATOM   2839 C CA   B GLU   A 1 120 ? 26.922 -14.465 12.878  0.66 14.97 ?  120 GLU   A CA   1 
ATOM   2840 C C    A GLU   A 1 120 ? 25.491 -13.911 12.908  0.34 14.86 ?  120 GLU   A C    1 
ATOM   2841 C C    B GLU   A 1 120 ? 25.503 -13.911 12.923  0.66 13.88 ?  120 GLU   A C    1 
ATOM   2842 O O    A GLU   A 1 120 ? 24.512 -14.660 12.791  0.34 14.86 ?  120 GLU   A O    1 
ATOM   2843 O O    B GLU   A 1 120 ? 24.536 -14.681 12.822  0.66 13.76 ?  120 GLU   A O    1 
ATOM   2844 C CB   A GLU   A 1 120 ? 27.367 -14.946 14.225  0.34 20.36 ?  120 GLU   A CB   1 
ATOM   2845 C CB   B GLU   A 1 120 ? 27.390 -14.819 14.291  0.66 18.74 ?  120 GLU   A CB   1 
ATOM   2846 C CG   A GLU   A 1 120 ? 28.549 -15.903 14.191  0.34 24.64 ?  120 GLU   A CG   1 
ATOM   2847 C CG   B GLU   A 1 120 ? 28.575 -15.760 14.336  0.66 24.37 ?  120 GLU   A CG   1 
ATOM   2848 C CD   A GLU   A 1 120 ? 28.773 -16.607 15.514  0.34 28.37 ?  120 GLU   A CD   1 
ATOM   2849 C CD   B GLU   A 1 120 ? 28.658 -16.521 15.640  0.66 29.44 ?  120 GLU   A CD   1 
ATOM   2850 O OE1  A GLU   A 1 120 ? 28.448 -16.017 16.566  0.34 29.56 ?  120 GLU   A OE1  1 
ATOM   2851 O OE1  B GLU   A 1 120 ? 28.231 -15.969 16.678  0.66 30.92 ?  120 GLU   A OE1  1 
ATOM   2852 O OE2  A GLU   A 1 120 ? 29.272 -17.753 15.499  0.34 29.76 -1 120 GLU   A OE2  1 
ATOM   2853 O OE2  B GLU   A 1 120 ? 29.137 -17.674 15.624  0.66 31.49 -1 120 GLU   A OE2  1 
ATOM   2854 H H    A GLU   A 1 120 ? 28.470 -13.273 12.796  0.34 17.36 ?  120 GLU   A H    1 
ATOM   2855 H H    B GLU   A 1 120 ? 28.464 -13.225 12.791  0.66 15.79 ?  120 GLU   A H    1 
ATOM   2856 H HA   A GLU   A 1 120 ? 26.862 -15.283 12.279  0.34 19.86 ?  120 GLU   A HA   1 
ATOM   2857 H HA   B GLU   A 1 120 ? 26.909 -15.285 12.370  0.66 18.12 ?  120 GLU   A HA   1 
ATOM   2858 H HB2  A GLU   A 1 120 ? 27.632 -14.170 14.741  0.34 24.59 ?  120 GLU   A HB2  1 
ATOM   2859 H HB2  B GLU   A 1 120 ? 27.648 -14.010 14.758  0.66 22.64 ?  120 GLU   A HB2  1 
ATOM   2860 H HB3  A GLU   A 1 120 ? 26.633 -15.401 14.669  0.34 24.59 ?  120 GLU   A HB3  1 
ATOM   2861 H HB3  B GLU   A 1 120 ? 26.662 -15.253 14.767  0.66 22.64 ?  120 GLU   A HB3  1 
ATOM   2862 H HG2  A GLU   A 1 120 ? 28.392 -16.575 13.509  0.34 29.72 ?  120 GLU   A HG2  1 
ATOM   2863 H HG2  B GLU   A 1 120 ? 28.500 -16.400 13.614  0.66 29.40 ?  120 GLU   A HG2  1 
ATOM   2864 H HG3  A GLU   A 1 120 ? 29.354 -15.404 13.989  0.34 29.72 ?  120 GLU   A HG3  1 
ATOM   2865 H HG3  B GLU   A 1 120 ? 29.391 -15.246 14.245  0.66 29.40 ?  120 GLU   A HG3  1 
ATOM   2866 N N    . VAL   A 1 121 ? 25.358 -12.599 13.107  1.00 13.86 ?  121 VAL   A N    1 
ATOM   2867 C CA   . VAL   A 1 121 ? 24.055 -11.947 13.223  1.00 13.88 ?  121 VAL   A CA   1 
ATOM   2868 C C    . VAL   A 1 121 ? 24.148 -10.573 12.568  1.00 12.66 ?  121 VAL   A C    1 
ATOM   2869 O O    . VAL   A 1 121 ? 25.100 -9.828  12.820  1.00 13.39 ?  121 VAL   A O    1 
ATOM   2870 C CB   . VAL   A 1 121 ? 23.613 -11.779 14.694  1.00 17.07 ?  121 VAL   A CB   1 
ATOM   2871 C CG1  . VAL   A 1 121 ? 22.213 -11.187 14.759  1.00 17.97 ?  121 VAL   A CG1  1 
ATOM   2872 C CG2  . VAL   A 1 121 ? 23.653 -13.084 15.467  1.00 19.10 ?  121 VAL   A CG2  1 
ATOM   2873 H H    A VAL   A 1 121 ? 26.025 -12.056 13.175  0.34 16.78 ?  121 VAL   A H    1 
ATOM   2874 H H    B VAL   A 1 121 ? 26.022 -12.053 13.171  0.66 16.78 ?  121 VAL   A H    1 
ATOM   2875 H HA   . VAL   A 1 121 ? 23.389 -12.473 12.757  1.00 16.81 ?  121 VAL   A HA   1 
ATOM   2876 H HB   . VAL   A 1 121 ? 24.214 -11.161 15.134  1.00 20.64 ?  121 VAL   A HB   1 
ATOM   2877 H HG11 . VAL   A 1 121 ? 21.889 -11.237 15.674  1.00 21.72 ?  121 VAL   A HG11 1 
ATOM   2878 H HG12 . VAL   A 1 121 ? 22.243 -10.262 14.472  1.00 21.72 ?  121 VAL   A HG12 1 
ATOM   2879 H HG13 . VAL   A 1 121 ? 21.625 -11.697 14.177  1.00 21.72 ?  121 VAL   A HG13 1 
ATOM   2880 H HG21 . VAL   A 1 121 ? 23.312 -12.926 16.368  1.00 23.07 ?  121 VAL   A HG21 1 
ATOM   2881 H HG22 . VAL   A 1 121 ? 23.092 -13.736 15.019  1.00 23.07 ?  121 VAL   A HG22 1 
ATOM   2882 H HG23 . VAL   A 1 121 ? 24.564 -13.400 15.513  1.00 23.07 ?  121 VAL   A HG23 1 
ATOM   2883 N N    . LEU   A 1 122 ? 23.146 -10.215 11.761  1.00 11.75 ?  122 LEU   A N    1 
ATOM   2884 C CA   . LEU   A 1 122 ? 23.137 -8.922  11.082  1.00 11.75 ?  122 LEU   A CA   1 
ATOM   2885 C C    . LEU   A 1 122 ? 21.732 -8.343  11.049  1.00 11.79 ?  122 LEU   A C    1 
ATOM   2886 O O    . LEU   A 1 122 ? 20.750 -9.073  10.920  1.00 12.79 ?  122 LEU   A O    1 
ATOM   2887 C CB   . LEU   A 1 122 ? 23.563 -9.024  9.615   1.00 13.08 ?  122 LEU   A CB   1 
ATOM   2888 C CG   . LEU   A 1 122 ? 24.795 -9.854  9.284   1.00 13.48 ?  122 LEU   A CG   1 
ATOM   2889 C CD1  . LEU   A 1 122 ? 24.424 -11.323 9.090   1.00 14.11 ?  122 LEU   A CD1  1 
ATOM   2890 C CD2  . LEU   A 1 122 ? 25.474 -9.302  8.048   1.00 12.92 ?  122 LEU   A CD2  1 
ATOM   2891 H H    . LEU   A 1 122 ? 22.452 -10.703 11.598  1.00 14.25 ?  122 LEU   A H    1 
ATOM   2892 H HA   . LEU   A 1 122 ? 23.729 -8.304  11.540  1.00 14.25 ?  122 LEU   A HA   1 
ATOM   2893 H HB2  . LEU   A 1 122 ? 22.832 -9.411  9.112   1.00 15.85 ?  122 LEU   A HB2  1 
ATOM   2894 H HB3  . LEU   A 1 122 ? 23.742 -8.133  9.287   1.00 15.85 ?  122 LEU   A HB3  1 
ATOM   2895 H HG   . LEU   A 1 122 ? 25.434 -9.806  10.015  1.00 16.33 ?  122 LEU   A HG   1 
ATOM   2896 H HD11 . LEU   A 1 122 ? 25.208 -11.823 8.810   1.00 17.08 ?  122 LEU   A HD11 1 
ATOM   2897 H HD12 . LEU   A 1 122 ? 24.095 -11.681 9.933   1.00 17.08 ?  122 LEU   A HD12 1 
ATOM   2898 H HD13 . LEU   A 1 122 ? 23.733 -11.390 8.413   1.00 17.08 ?  122 LEU   A HD13 1 
ATOM   2899 H HD21 . LEU   A 1 122 ? 26.237 -9.865  7.818   1.00 15.66 ?  122 LEU   A HD21 1 
ATOM   2900 H HD22 . LEU   A 1 122 ? 24.843 -9.294  7.314   1.00 15.66 ?  122 LEU   A HD22 1 
ATOM   2901 H HD23 . LEU   A 1 122 ? 25.782 -8.400  8.232   1.00 15.66 ?  122 LEU   A HD23 1 
ATOM   2902 N N    . LEU   A 1 123 ? 21.659 -7.011  11.134  1.00 11.69 ?  123 LEU   A N    1 
ATOM   2903 C CA   . LEU   A 1 123 ? 20.484 -6.231  10.749  1.00 11.47 ?  123 LEU   A CA   1 
ATOM   2904 C C    . LEU   A 1 123 ? 20.737 -5.717  9.340   1.00 10.92 ?  123 LEU   A C    1 
ATOM   2905 O O    . LEU   A 1 123 ? 21.784 -5.110  9.096   1.00 11.78 ?  123 LEU   A O    1 
ATOM   2906 C CB   . LEU   A 1 123 ? 20.336 -5.041  11.697  1.00 12.06 ?  123 LEU   A CB   1 
ATOM   2907 C CG   . LEU   A 1 123 ? 19.298 -3.985  11.341  1.00 12.74 ?  123 LEU   A CG   1 
ATOM   2908 C CD1  . LEU   A 1 123 ? 17.886 -4.565  11.340  1.00 13.69 ?  123 LEU   A CD1  1 
ATOM   2909 C CD2  . LEU   A 1 123 ? 19.403 -2.811  12.305  1.00 13.31 ?  123 LEU   A CD2  1 
ATOM   2910 H H    . LEU   A 1 123 ? 22.307 -6.518  11.425  1.00 14.17 ?  123 LEU   A H    1 
ATOM   2911 H HA   . LEU   A 1 123 ? 19.682 -6.782  10.772  1.00 13.92 ?  123 LEU   A HA   1 
ATOM   2912 H HB2  . LEU   A 1 123 ? 20.102 -5.377  12.575  1.00 14.62 ?  123 LEU   A HB2  1 
ATOM   2913 H HB3  . LEU   A 1 123 ? 21.189 -4.586  11.745  1.00 14.62 ?  123 LEU   A HB3  1 
ATOM   2914 H HG   . LEU   A 1 123 ? 19.472 -3.643  10.450  1.00 15.44 ?  123 LEU   A HG   1 
ATOM   2915 H HD11 . LEU   A 1 123 ? 17.248 -3.854  11.168  1.00 16.58 ?  123 LEU   A HD11 1 
ATOM   2916 H HD12 . LEU   A 1 123 ? 17.823 -5.240  10.649  1.00 16.58 ?  123 LEU   A HD12 1 
ATOM   2917 H HD13 . LEU   A 1 123 ? 17.708 -4.962  12.209  1.00 16.58 ?  123 LEU   A HD13 1 
ATOM   2918 H HD21 . LEU   A 1 123 ? 18.737 -2.149  12.077  1.00 16.12 ?  123 LEU   A HD21 1 
ATOM   2919 H HD22 . LEU   A 1 123 ? 19.252 -3.137  13.209  1.00 16.12 ?  123 LEU   A HD22 1 
ATOM   2920 H HD23 . LEU   A 1 123 ? 20.293 -2.432  12.237  1.00 16.12 ?  123 LEU   A HD23 1 
ATOM   2921 N N    A ALA   A 1 124 ? 19.798 -5.944  8.422   0.34 10.63 ?  124 ALA   A N    1 
ATOM   2922 N N    B ALA   A 1 124 ? 19.794 -5.928  8.421   0.66 10.98 ?  124 ALA   A N    1 
ATOM   2923 C CA   A ALA   A 1 124 ? 20.073 -5.634  7.027   0.34 10.44 ?  124 ALA   A CA   1 
ATOM   2924 C CA   B ALA   A 1 124 ? 20.090 -5.678  7.016   0.66 11.04 ?  124 ALA   A CA   1 
ATOM   2925 C C    A ALA   A 1 124 ? 18.827 -5.164  6.297   0.34 10.94 ?  124 ALA   A C    1 
ATOM   2926 C C    B ALA   A 1 124 ? 18.855 -5.196  6.267   0.66 10.87 ?  124 ALA   A C    1 
ATOM   2927 O O    A ALA   A 1 124 ? 17.704 -5.536  6.663   0.34 11.35 ?  124 ALA   A O    1 
ATOM   2928 O O    B ALA   A 1 124 ? 17.718 -5.514  6.646   0.66 12.12 ?  124 ALA   A O    1 
ATOM   2929 C CB   A ALA   A 1 124 ? 20.648 -6.845  6.284   0.34 10.33 ?  124 ALA   A CB   1 
ATOM   2930 C CB   B ALA   A 1 124 ? 20.640 -6.934  6.329   0.66 11.86 ?  124 ALA   A CB   1 
ATOM   2931 H H    A ALA   A 1 124 ? 19.010 -6.260  8.577   0.34 12.91 ?  124 ALA   A H    1 
ATOM   2932 H H    B ALA   A 1 124 ? 18.990 -6.206  8.585   0.66 13.33 ?  124 ALA   A H    1 
ATOM   2933 H HA   A ALA   A 1 124 ? 20.737 -4.929  6.997   0.34 12.67 ?  124 ALA   A HA   1 
ATOM   2934 H HA   B ALA   A 1 124 ? 20.769 -4.986  6.972   0.66 13.40 ?  124 ALA   A HA   1 
ATOM   2935 H HB1  A ALA   A 1 124 ? 20.822 -6.599  5.360   0.34 12.55 ?  124 ALA   A HB1  1 
ATOM   2936 H HB1  B ALA   A 1 124 ? 20.834 -6.738  5.396   0.66 14.38 ?  124 ALA   A HB1  1 
ATOM   2937 H HB2  A ALA   A 1 124 ? 21.476 -7.116  6.712   0.34 12.55 ?  124 ALA   A HB2  1 
ATOM   2938 H HB2  B ALA   A 1 124 ? 21.462 -7.217  6.774   0.66 14.38 ?  124 ALA   A HB2  1 
ATOM   2939 H HB3  A ALA   A 1 124 ? 20.007 -7.571  6.316   0.34 12.55 ?  124 ALA   A HB3  1 
ATOM   2940 H HB3  B ALA   A 1 124 ? 19.984 -7.649  6.382   0.66 14.38 ?  124 ALA   A HB3  1 
ATOM   2941 N N    A PRO   A 1 125 ? 19.001 -4.353  5.253   0.34 11.48 ?  125 PRO   A N    1 
ATOM   2942 N N    B PRO   A 1 125 ? 19.055 -4.464  5.169   0.66 10.26 ?  125 PRO   A N    1 
ATOM   2943 C CA   A PRO   A 1 125 ? 17.922 -4.092  4.296   0.34 12.02 ?  125 PRO   A CA   1 
ATOM   2944 C CA   B PRO   A 1 125 ? 17.981 -4.164  4.224   0.66 10.81 ?  125 PRO   A CA   1 
ATOM   2945 C C    A PRO   A 1 125 ? 17.927 -5.137  3.195   0.34 12.27 ?  125 PRO   A C    1 
ATOM   2946 C C    B PRO   A 1 125 ? 17.972 -5.214  3.114   0.66 11.24 ?  125 PRO   A C    1 
ATOM   2947 O O    A PRO   A 1 125 ? 18.818 -5.993  3.147   0.34 12.24 ?  125 PRO   A O    1 
ATOM   2948 O O    B PRO   A 1 125 ? 18.904 -6.010  2.976   0.66 11.62 ?  125 PRO   A O    1 
ATOM   2949 C CB   A PRO   A 1 125 ? 18.320 -2.727  3.729   0.34 12.32 ?  125 PRO   A CB   1 
ATOM   2950 C CB   B PRO   A 1 125 ? 18.465 -2.828  3.646   0.66 10.95 ?  125 PRO   A CB   1 
ATOM   2951 C CG   A PRO   A 1 125 ? 19.825 -2.805  3.698   0.34 12.58 ?  125 PRO   A CG   1 
ATOM   2952 C CG   B PRO   A 1 125 ? 19.974 -3.052  3.506   0.66 10.15 ?  125 PRO   A CG   1 
ATOM   2953 C CD   A PRO   A 1 125 ? 20.216 -3.586  4.927   0.34 12.05 ?  125 PRO   A CD   1 
ATOM   2954 C CD   B PRO   A 1 125 ? 20.349 -3.921  4.701   0.66 9.85  ?  125 PRO   A CD   1 
ATOM   2955 H HA   A PRO   A 1 125 ? 17.046 -4.051  4.719   0.34 14.57 ?  125 PRO   A HA   1 
ATOM   2956 H HA   B PRO   A 1 125 ? 17.119 -4.072  4.658   0.66 13.13 ?  125 PRO   A HA   1 
ATOM   2957 H HB2  A PRO   A 1 125 ? 17.962 -2.613  2.835   0.34 14.94 ?  125 PRO   A HB2  1 
ATOM   2958 H HB2  B PRO   A 1 125 ? 18.048 -2.671  2.785   0.66 13.29 ?  125 PRO   A HB2  1 
ATOM   2959 H HB3  A PRO   A 1 125 ? 18.023 -2.017  4.319   0.34 14.94 ?  125 PRO   A HB3  1 
ATOM   2960 H HB3  B PRO   A 1 125 ? 18.271 -2.108  4.266   0.66 13.29 ?  125 PRO   A HB3  1 
ATOM   2961 H HG2  A PRO   A 1 125 ? 20.113 -3.269  2.896   0.34 15.24 ?  125 PRO   A HG2  1 
ATOM   2962 H HG2  B PRO   A 1 125 ? 20.161 -3.504  2.667   0.66 12.33 ?  125 PRO   A HG2  1 
ATOM   2963 H HG3  A PRO   A 1 125 ? 20.202 -1.912  3.730   0.34 15.24 ?  125 PRO   A HG3  1 
ATOM   2964 H HG3  B PRO   A 1 125 ? 20.433 -2.192  3.537   0.66 12.33 ?  125 PRO   A HG3  1 
ATOM   2965 H HD2  A PRO   A 1 125 ? 20.948 -4.188  4.730   0.34 14.61 ?  125 PRO   A HD2  1 
ATOM   2966 H HD2  B PRO   A 1 125 ? 20.947 -4.633  4.417   0.66 11.97 ?  125 PRO   A HD2  1 
ATOM   2967 H HD3  A PRO   A 1 125 ? 20.433 -2.985  5.656   0.34 14.61 ?  125 PRO   A HD3  1 
ATOM   2968 H HD3  B PRO   A 1 125 ? 20.758 -3.375  5.392   0.66 11.97 ?  125 PRO   A HD3  1 
ATOM   2969 N N    A LEU   A 1 126 ? 16.948 -5.068  2.298   0.34 12.88 ?  126 LEU   A N    1 
ATOM   2970 N N    B LEU   A 1 126 ? 16.913 -5.182  2.296   0.66 12.57 ?  126 LEU   A N    1 
ATOM   2971 C CA   A LEU   A 1 126 ? 16.930 -5.919  1.113   0.34 13.19 ?  126 LEU   A CA   1 
ATOM   2972 C CA   B LEU   A 1 126 ? 16.967 -5.897  1.026   0.66 14.04 ?  126 LEU   A CA   1 
ATOM   2973 C C    A LEU   A 1 126 ? 17.832 -5.322  0.042   0.34 12.99 ?  126 LEU   A C    1 
ATOM   2974 C C    B LEU   A 1 126 ? 17.959 -5.203  0.101   0.66 14.05 ?  126 LEU   A C    1 
ATOM   2975 O O    A LEU   A 1 126 ? 17.536 -4.256  -0.515  0.34 12.68 ?  126 LEU   A O    1 
ATOM   2976 O O    B LEU   A 1 126 ? 17.955 -3.975  -0.017  0.66 15.79 ?  126 LEU   A O    1 
ATOM   2977 C CB   A LEU   A 1 126 ? 15.510 -6.088  0.591   0.34 13.72 ?  126 LEU   A CB   1 
ATOM   2978 C CB   B LEU   A 1 126 ? 15.597 -5.942  0.358   0.66 15.77 ?  126 LEU   A CB   1 
ATOM   2979 C CG   A LEU   A 1 126 ? 14.664 -7.088  1.367   0.34 13.87 ?  126 LEU   A CG   1 
ATOM   2980 C CG   B LEU   A 1 126 ? 14.612 -6.981  0.867   0.66 16.68 ?  126 LEU   A CG   1 
ATOM   2981 C CD1  A LEU   A 1 126 ? 13.249 -7.047  0.848   0.34 14.28 ?  126 LEU   A CD1  1 
ATOM   2982 C CD1  B LEU   A 1 126 ? 13.292 -6.810  0.141   0.66 17.18 ?  126 LEU   A CD1  1 
ATOM   2983 C CD2  A LEU   A 1 126 ? 15.230 -8.495  1.248   0.34 13.18 ?  126 LEU   A CD2  1 
ATOM   2984 C CD2  B LEU   A 1 126 ? 15.120 -8.409  0.690   0.66 16.60 ?  126 LEU   A CD2  1 
ATOM   2985 H H    A LEU   A 1 126 ? 16.281 -4.535  2.369   0.34 15.61 ?  126 LEU   A H    1 
ATOM   2986 H H    B LEU   A 1 126 ? 16.179 -4.744  2.434   0.66 15.24 ?  126 LEU   A H    1 
ATOM   2987 H HA   A LEU   A 1 126 ? 17.283 -6.788  1.346   0.34 15.98 ?  126 LEU   A HA   1 
ATOM   2988 H HA   B LEU   A 1 126 ? 17.276 -6.799  1.175   0.66 17.00 ?  126 LEU   A HA   1 
ATOM   2989 H HB2  A LEU   A 1 126 ? 15.065 -5.227  0.628   0.34 16.62 ?  126 LEU   A HB2  1 
ATOM   2990 H HB2  B LEU   A 1 126 ? 15.182 -5.073  0.469   0.66 19.08 ?  126 LEU   A HB2  1 
ATOM   2991 H HB3  A LEU   A 1 126 ? 15.559 -6.391  -0.329  0.34 16.62 ?  126 LEU   A HB3  1 
ATOM   2992 H HB3  B LEU   A 1 126 ? 15.729 -6.111  -0.589  0.66 19.08 ?  126 LEU   A HB3  1 
ATOM   2993 H HG   A LEU   A 1 126 ? 14.651 -6.838  2.306   0.34 16.80 ?  126 LEU   A HG   1 
ATOM   2994 H HG   B LEU   A 1 126 ? 14.452 -6.832  1.810   0.66 20.17 ?  126 LEU   A HG   1 
ATOM   2995 H HD11 A LEU   A 1 126 ? 12.710 -7.679  1.348   0.34 17.29 ?  126 LEU   A HD11 1 
ATOM   2996 H HD11 B LEU   A 1 126 ? 12.660 -7.474  0.469   0.66 20.77 ?  126 LEU   A HD11 1 
ATOM   2997 H HD12 A LEU   A 1 126 ? 12.895 -6.150  0.960   0.34 17.29 ?  126 LEU   A HD12 1 
ATOM   2998 H HD12 B LEU   A 1 126 ? 12.946 -5.919  0.310   0.66 20.77 ?  126 LEU   A HD12 1 
ATOM   2999 H HD13 A LEU   A 1 126 ? 13.251 -7.285  -0.093  0.34 17.29 ?  126 LEU   A HD13 1 
ATOM   3000 H HD13 B LEU   A 1 126 ? 13.431 -6.935  -0.811  0.66 20.77 ?  126 LEU   A HD13 1 
ATOM   3001 H HD21 A LEU   A 1 126 ? 14.562 -9.131  1.546   0.34 15.96 ?  126 LEU   A HD21 1 
ATOM   3002 H HD21 B LEU   A 1 126 ? 14.405 -9.029  0.893   0.66 20.07 ?  126 LEU   A HD21 1 
ATOM   3003 H HD22 A LEU   A 1 126 ? 15.458 -8.665  0.320   0.34 15.96 ?  126 LEU   A HD22 1 
ATOM   3004 H HD22 B LEU   A 1 126 ? 15.410 -8.529  -0.230  0.66 20.07 ?  126 LEU   A HD22 1 
ATOM   3005 H HD23 A LEU   A 1 126 ? 16.024 -8.566  1.801   0.34 15.96 ?  126 LEU   A HD23 1 
ATOM   3006 H HD23 B LEU   A 1 126 ? 15.868 -8.554  1.291   0.66 20.07 ?  126 LEU   A HD23 1 
ATOM   3007 N N    A LEU   A 1 127 ? 18.914 -6.033  -0.267  0.34 13.33 ?  127 LEU   A N    1 
ATOM   3008 N N    B LEU   A 1 127 ? 18.816 -5.986  -0.549  0.66 12.64 ?  127 LEU   A N    1 
ATOM   3009 C CA   A LEU   A 1 127 ? 19.895 -5.561  -1.230  0.34 13.66 ?  127 LEU   A CA   1 
ATOM   3010 C CA   B LEU   A 1 127 ? 19.825 -5.441  -1.443  0.66 12.79 ?  127 LEU   A CA   1 
ATOM   3011 C C    A LEU   A 1 127 ? 19.257 -5.369  -2.598  0.34 13.65 ?  127 LEU   A C    1 
ATOM   3012 C C    B LEU   A 1 127 ? 19.309 -5.385  -2.875  0.66 12.80 ?  127 LEU   A C    1 
ATOM   3013 O O    A LEU   A 1 127 ? 18.326 -6.083  -2.990  0.34 13.72 ?  127 LEU   A O    1 
ATOM   3014 O O    B LEU   A 1 127 ? 18.519 -6.231  -3.318  0.66 13.09 ?  127 LEU   A O    1 
ATOM   3015 C CB   A LEU   A 1 127 ? 21.041 -6.567  -1.340  0.34 13.49 ?  127 LEU   A CB   1 
ATOM   3016 C CB   B LEU   A 1 127 ? 21.115 -6.267  -1.388  0.66 13.34 ?  127 LEU   A CB   1 
ATOM   3017 C CG   A LEU   A 1 127 ? 21.831 -6.821  -0.056  0.34 13.04 ?  127 LEU   A CG   1 
ATOM   3018 C CG   B LEU   A 1 127 ? 21.877 -6.242  -0.057  0.66 14.03 ?  127 LEU   A CG   1 
ATOM   3019 C CD1  A LEU   A 1 127 ? 22.923 -7.839  -0.317  0.34 12.91 ?  127 LEU   A CD1  1 
ATOM   3020 C CD1  B LEU   A 1 127 ? 23.063 -7.193  -0.090  0.66 14.62 ?  127 LEU   A CD1  1 
ATOM   3021 C CD2  A LEU   A 1 127 ? 22.424 -5.528  0.475   0.34 13.11 ?  127 LEU   A CD2  1 
ATOM   3022 C CD2  B LEU   A 1 127 ? 22.336 -4.830  0.280   0.66 14.80 ?  127 LEU   A CD2  1 
ATOM   3023 H H    A LEU   A 1 127 ? 19.099 -6.805  0.067   0.34 16.15 ?  127 LEU   A H    1 
ATOM   3024 H H    B LEU   A 1 127 ? 18.833 -6.847  -0.481  0.66 15.32 ?  127 LEU   A H    1 
ATOM   3025 H HA   A LEU   A 1 127 ? 20.256 -4.712  -0.939  0.34 16.54 ?  127 LEU   A HA   1 
ATOM   3026 H HA   B LEU   A 1 127 ? 20.038 -4.543  -1.161  0.66 15.50 ?  127 LEU   A HA   1 
ATOM   3027 H HB2  A LEU   A 1 127 ? 20.677 -7.421  -1.625  0.34 16.34 ?  127 LEU   A HB2  1 
ATOM   3028 H HB2  B LEU   A 1 127 ? 20.899 -7.195  -1.571  0.66 16.16 ?  127 LEU   A HB2  1 
ATOM   3029 H HB3  A LEU   A 1 127 ? 21.671 -6.249  -2.005  0.34 16.34 ?  127 LEU   A HB3  1 
ATOM   3030 H HB3  B LEU   A 1 127 ? 21.720 -5.937  -2.069  0.66 16.16 ?  127 LEU   A HB3  1 
ATOM   3031 H HG   A LEU   A 1 127 ? 21.236 -7.184  0.621   0.34 15.79 ?  127 LEU   A HG   1 
ATOM   3032 H HG   B LEU   A 1 127 ? 21.286 -6.536  0.652   0.66 16.99 ?  127 LEU   A HG   1 
ATOM   3033 H HD11 A LEU   A 1 127 ? 23.395 -8.018  0.512   0.34 15.65 ?  127 LEU   A HD11 1 
ATOM   3034 H HD11 B LEU   A 1 127 ? 23.524 -7.155  0.766   0.66 17.70 ?  127 LEU   A HD11 1 
ATOM   3035 H HD12 A LEU   A 1 127 ? 22.519 -8.658  -0.649  0.34 15.65 ?  127 LEU   A HD12 1 
ATOM   3036 H HD12 B LEU   A 1 127 ? 22.742 -8.093  -0.250  0.66 17.70 ?  127 LEU   A HD12 1 
ATOM   3037 H HD13 A LEU   A 1 127 ? 23.536 -7.482  -0.978  0.34 15.65 ?  127 LEU   A HD13 1 
ATOM   3038 H HD13 B LEU   A 1 127 ? 23.666 -6.924  -0.800  0.66 17.70 ?  127 LEU   A HD13 1 
ATOM   3039 H HD21 A LEU   A 1 127 ? 23.040 -5.737  1.194   0.34 15.88 ?  127 LEU   A HD21 1 
ATOM   3040 H HD21 B LEU   A 1 127 ? 22.934 -4.862  1.044   0.66 17.91 ?  127 LEU   A HD21 1 
ATOM   3041 H HD22 A LEU   A 1 127 ? 22.897 -5.083  -0.247  0.34 15.88 ?  127 LEU   A HD22 1 
ATOM   3042 H HD22 B LEU   A 1 127 ? 22.801 -4.456  -0.487  0.66 17.91 ?  127 LEU   A HD22 1 
ATOM   3043 H HD23 A LEU   A 1 127 ? 21.709 -4.964  0.801   0.34 15.88 ?  127 LEU   A HD23 1 
ATOM   3044 H HD23 B LEU   A 1 127 ? 21.560 -4.287  0.491   0.66 17.91 ?  127 LEU   A HD23 1 
ATOM   3045 N N    A SER   A 1 128 ? 19.765 -4.373  -3.318  0.34 14.05 ?  128 SER   A N    1 
ATOM   3046 N N    B SER   A 1 128 ? 19.757 -4.351  -3.584  0.66 13.98 ?  128 SER   A N    1 
ATOM   3047 C CA   A SER   A 1 128 ? 19.341 -4.019  -4.667  0.34 14.08 ?  128 SER   A CA   1 
ATOM   3048 C CA   B SER   A 1 128 ? 19.521 -4.093  -4.998  0.66 15.41 ?  128 SER   A CA   1 
ATOM   3049 C C    A SER   A 1 128 ? 17.875 -3.612  -4.746  0.34 14.22 ?  128 SER   A C    1 
ATOM   3050 C C    B SER   A 1 128 ? 18.093 -3.672  -5.315  0.66 16.58 ?  128 SER   A C    1 
ATOM   3051 O O    A SER   A 1 128 ? 17.348 -3.434  -5.848  0.34 14.47 ?  128 SER   A O    1 
ATOM   3052 O O    B SER   A 1 128 ? 17.813 -3.356  -6.472  0.66 16.98 ?  128 SER   A O    1 
ATOM   3053 C CB   A SER   A 1 128 ? 19.668 -5.111  -5.693  0.34 14.07 ?  128 SER   A CB   1 
ATOM   3054 C CB   B SER   A 1 128 ? 19.954 -5.253  -5.908  0.66 15.27 ?  128 SER   A CB   1 
ATOM   3055 O OG   A SER   A 1 128 ? 21.070 -5.333  -5.751  0.34 14.05 ?  128 SER   A OG   1 
ATOM   3056 O OG   B SER   A 1 128 ? 21.368 -5.371  -5.918  0.66 14.53 ?  128 SER   A OG   1 
ATOM   3057 H H    A SER   A 1 128 ? 20.390 -3.853  -3.024  0.34 17.02 ?  128 SER   A H    1 
ATOM   3058 H H    B SER   A 1 128 ? 20.247 -3.733  -3.227  0.66 16.92 ?  128 SER   A H    1 
ATOM   3059 H HA   A SER   A 1 128 ? 19.859 -3.249  -4.927  0.34 17.05 ?  128 SER   A HA   1 
ATOM   3060 H HA   B SER   A 1 128 ? 20.075 -3.342  -5.240  0.66 18.64 ?  128 SER   A HA   1 
ATOM   3061 H HB2  A SER   A 1 128 ? 19.226 -5.932  -5.439  0.34 17.03 ?  128 SER   A HB2  1 
ATOM   3062 H HB2  B SER   A 1 128 ? 19.567 -6.078  -5.584  0.66 18.48 ?  128 SER   A HB2  1 
ATOM   3063 H HB3  A SER   A 1 128 ? 19.359 -4.821  -6.569  0.34 17.03 ?  128 SER   A HB3  1 
ATOM   3064 H HB3  B SER   A 1 128 ? 19.651 -5.072  -6.813  0.66 18.48 ?  128 SER   A HB3  1 
ATOM   3065 H HG   A SER   A 1 128 ? 21.463 -4.620  -5.967  0.34 17.01 ?  128 SER   A HG   1 
ATOM   3066 H HG   B SER   A 1 128 ? 21.712 -4.648  -6.183  0.66 17.59 ?  128 SER   A HG   1 
ATOM   3067 N N    A ALA   A 1 129 ? 17.201 -3.456  -3.608  0.34 14.76 ?  129 ALA   A N    1 
ATOM   3068 N N    B ALA   A 1 129 ? 17.192 -3.625  -4.332  0.66 17.90 ?  129 ALA   A N    1 
ATOM   3069 C CA   A ALA   A 1 129 ? 15.838 -2.954  -3.603  0.34 15.77 ?  129 ALA   A CA   1 
ATOM   3070 C CA   B ALA   A 1 129 ? 15.769 -3.430  -4.582  0.66 20.44 ?  129 ALA   A CA   1 
ATOM   3071 C C    A ALA   A 1 129 ? 15.849 -1.428  -3.634  0.34 16.05 ?  129 ALA   A C    1 
ATOM   3072 C C    B ALA   A 1 129 ? 15.296 -2.000  -4.335  0.66 22.39 ?  129 ALA   A C    1 
ATOM   3073 O O    A ALA   A 1 129 ? 16.893 -0.784  -3.773  0.34 16.52 ?  129 ALA   A O    1 
ATOM   3074 O O    B ALA   A 1 129 ? 14.087 -1.769  -4.221  0.66 23.29 ?  129 ALA   A O    1 
ATOM   3075 C CB   A ALA   A 1 129 ? 15.074 -3.510  -2.400  0.34 16.68 ?  129 ALA   A CB   1 
ATOM   3076 C CB   B ALA   A 1 129 ? 14.946 -4.412  -3.750  0.66 21.52 ?  129 ALA   A CB   1 
ATOM   3077 H H    A ALA   A 1 129 ? 17.512 -3.637  -2.826  0.34 17.86 ?  129 ALA   A H    1 
ATOM   3078 H H    B ALA   A 1 129 ? 17.387 -3.706  -3.498  0.66 21.63 ?  129 ALA   A H    1 
ATOM   3079 H HA   A ALA   A 1 129 ? 15.388 -3.247  -4.403  0.34 19.07 ?  129 ALA   A HA   1 
ATOM   3080 H HA   B ALA   A 1 129 ? 15.598 -3.632  -5.513  0.66 24.68 ?  129 ALA   A HA   1 
ATOM   3081 H HB1  A ALA   A 1 129 ? 14.163 -3.179  -2.421  0.34 20.16 ?  129 ALA   A HB1  1 
ATOM   3082 H HB1  B ALA   A 1 129 ? 14.003 -4.267  -3.937  0.66 25.98 ?  129 ALA   A HB1  1 
ATOM   3083 H HB2  A ALA   A 1 129 ? 15.073 -4.481  -2.448  0.34 20.16 ?  129 ALA   A HB2  1 
ATOM   3084 H HB2  B ALA   A 1 129 ? 15.194 -5.316  -3.995  0.66 25.98 ?  129 ALA   A HB2  1 
ATOM   3085 H HB3  A ALA   A 1 129 ? 15.512 -3.224  -1.582  0.34 20.16 ?  129 ALA   A HB3  1 
ATOM   3086 H HB3  B ALA   A 1 129 ? 15.124 -4.259  -2.811  0.66 25.98 ?  129 ALA   A HB3  1 
ATOM   3087 N N    A GLY   A 1 130 ? 14.665 -0.840  -3.533  0.34 16.50 ?  130 GLY   A N    1 
ATOM   3088 N N    B GLY   A 1 130 ? 16.209 -1.039  -4.257  0.66 22.80 ?  130 GLY   A N    1 
ATOM   3089 C CA   A GLY   A 1 130 ? 14.583 0.609   -3.488  0.34 16.93 ?  130 GLY   A CA   1 
ATOM   3090 C CA   B GLY   A 1 130 ? 15.805 0.349   -4.139  0.66 23.50 ?  130 GLY   A CA   1 
ATOM   3091 C C    A GLY   A 1 130 ? 15.176 1.218   -4.745  0.34 16.90 ?  130 GLY   A C    1 
ATOM   3092 C C    B GLY   A 1 130 ? 15.945 1.079   -5.456  0.66 24.06 ?  130 GLY   A C    1 
ATOM   3093 O O    A GLY   A 1 130 ? 14.877 0.799   -5.870  0.34 17.04 ?  130 GLY   A O    1 
ATOM   3094 O O    B GLY   A 1 130 ? 15.324 0.699   -6.456  0.66 23.40 ?  130 GLY   A O    1 
ATOM   3095 H H    A GLY   A 1 130 ? 13.912 -1.253  -3.501  0.34 19.96 ?  130 GLY   A H    1 
ATOM   3096 H H    B GLY   A 1 130 ? 17.060 -1.163  -4.277  0.66 27.51 ?  130 GLY   A H    1 
ATOM   3097 H HA2  A GLY   A 1 130 ? 13.653 0.879   -3.399  0.34 20.47 ?  130 GLY   A HA2  1 
ATOM   3098 H HA2  B GLY   A 1 130 ? 14.882 0.405   -3.851  0.66 28.35 ?  130 GLY   A HA2  1 
ATOM   3099 H HA3  A GLY   A 1 130 ? 15.072 0.943   -2.714  0.34 20.47 ?  130 GLY   A HA3  1 
ATOM   3100 H HA3  B GLY   A 1 130 ? 16.362 0.792   -3.484  0.66 28.35 ?  130 GLY   A HA3  1 
ATOM   3101 N N    A ILE   A 1 131 ? 16.053 2.206   -4.552  0.34 16.75 ?  131 ILE   A N    1 
ATOM   3102 N N    B ILE   A 1 131 ? 16.765 2.134   -5.467  0.66 25.13 ?  131 ILE   A N    1 
ATOM   3103 C CA   A ILE   A 1 131 ? 16.600 2.966   -5.672  0.34 15.93 ?  131 ILE   A CA   1 
ATOM   3104 C CA   B ILE   A 1 131 ? 17.130 2.784   -6.720  0.66 25.45 ?  131 ILE   A CA   1 
ATOM   3105 C C    A ILE   A 1 131 ? 17.609 2.184   -6.498  0.34 15.26 ?  131 ILE   A C    1 
ATOM   3106 C C    B ILE   A 1 131 ? 17.966 1.880   -7.613  0.66 23.84 ?  131 ILE   A C    1 
ATOM   3107 O O    A ILE   A 1 131 ? 18.060 2.686   -7.538  0.34 15.34 ?  131 ILE   A O    1 
ATOM   3108 O O    B ILE   A 1 131 ? 18.157 2.190   -8.792  0.66 23.80 ?  131 ILE   A O    1 
ATOM   3109 C CB   A ILE   A 1 131 ? 17.193 4.309   -5.194  0.34 16.52 ?  131 ILE   A CB   1 
ATOM   3110 C CB   B ILE   A 1 131 ? 17.836 4.137   -6.479  0.66 27.89 ?  131 ILE   A CB   1 
ATOM   3111 C CG1  A ILE   A 1 131 ? 18.464 4.086   -4.370  0.34 17.25 ?  131 ILE   A CG1  1 
ATOM   3112 C CG1  B ILE   A 1 131 ? 19.278 3.932   -6.000  0.66 29.56 ?  131 ILE   A CG1  1 
ATOM   3113 C CG2  A ILE   A 1 131 ? 16.165 5.078   -4.378  0.34 16.54 ?  131 ILE   A CG2  1 
ATOM   3114 C CG2  B ILE   A 1 131 ? 17.047 4.983   -5.477  0.66 28.73 ?  131 ILE   A CG2  1 
ATOM   3115 C CD1  A ILE   A 1 131 ? 19.139 5.376   -3.940  0.34 17.76 ?  131 ILE   A CD1  1 
ATOM   3116 C CD1  B ILE   A 1 131 ? 20.245 4.972   -6.525  0.66 30.64 ?  131 ILE   A CD1  1 
ATOM   3117 H H    A ILE   A 1 131 ? 16.337 2.453   -3.777  0.34 20.26 ?  131 ILE   A H    1 
ATOM   3118 H H    B ILE   A 1 131 ? 17.121 2.486   -4.765  0.66 30.31 ?  131 ILE   A H    1 
ATOM   3119 H HA   A ILE   A 1 131 ? 15.868 3.177   -6.264  0.34 19.27 ?  131 ILE   A HA   1 
ATOM   3120 H HA   B ILE   A 1 131 ? 16.319 2.979   -7.206  0.66 30.69 ?  131 ILE   A HA   1 
ATOM   3121 H HB   A ILE   A 1 131 ? 17.416 4.836   -5.974  0.34 19.98 ?  131 ILE   A HB   1 
ATOM   3122 H HB   B ILE   A 1 131 ? 17.859 4.625   -7.312  0.66 33.63 ?  131 ILE   A HB   1 
ATOM   3123 H HG12 A ILE   A 1 131 ? 18.234 3.588   -3.571  0.34 20.85 ?  131 ILE   A HG12 1 
ATOM   3124 H HG12 B ILE   A 1 131 ? 19.283 3.990   -5.038  0.66 35.62 ?  131 ILE   A HG12 1 
ATOM   3125 H HG13 A ILE   A 1 131 ? 19.102 3.588   -4.900  0.34 20.85 ?  131 ILE   A HG13 1 
ATOM   3126 H HG13 B ILE   A 1 131 ? 19.612 3.064   -6.270  0.66 35.62 ?  131 ILE   A HG13 1 
ATOM   3127 H HG21 A ILE   A 1 131 ? 16.476 5.990   -4.255  0.34 20.00 ?  131 ILE   A HG21 1 
ATOM   3128 H HG21 B ILE   A 1 131 ? 17.426 5.877   -5.447  0.66 34.62 ?  131 ILE   A HG21 1 
ATOM   3129 H HG22 A ILE   A 1 131 ? 15.320 5.080   -4.854  0.34 20.00 ?  131 ILE   A HG22 1 
ATOM   3130 H HG22 B ILE   A 1 131 ? 16.121 5.029   -5.762  0.66 34.62 ?  131 ILE   A HG22 1 
ATOM   3131 H HG23 A ILE   A 1 131 ? 16.057 4.646   -3.516  0.34 20.00 ?  131 ILE   A HG23 1 
ATOM   3132 H HG23 B ILE   A 1 131 ? 17.103 4.573   -4.600  0.66 34.62 ?  131 ILE   A HG23 1 
ATOM   3133 H HD11 A ILE   A 1 131 ? 19.998 5.165   -3.545  0.34 21.46 ?  131 ILE   A HD11 1 
ATOM   3134 H HD11 B ILE   A 1 131 ? 21.132 4.769   -6.189  0.66 36.92 ?  131 ILE   A HD11 1 
ATOM   3135 H HD12 A ILE   A 1 131 ? 19.262 5.943   -4.718  0.34 21.46 ?  131 ILE   A HD12 1 
ATOM   3136 H HD12 B ILE   A 1 131 ? 20.245 4.945   -7.496  0.66 36.92 ?  131 ILE   A HD12 1 
ATOM   3137 H HD13 A ILE   A 1 131 ? 18.577 5.827   -3.289  0.34 21.46 ?  131 ILE   A HD13 1 
ATOM   3138 H HD13 B ILE   A 1 131 ? 19.965 5.846   -6.217  0.66 36.92 ?  131 ILE   A HD13 1 
ATOM   3139 N N    A PHE   A 1 132 ? 17.974 0.972   -6.063  0.34 14.94 ?  132 PHE   A N    1 
ATOM   3140 N N    B PHE   A 1 132 ? 18.488 0.774   -7.081  0.66 22.55 ?  132 PHE   A N    1 
ATOM   3141 C CA   A PHE   A 1 132 ? 18.857 0.122   -6.854  0.34 15.68 ?  132 PHE   A CA   1 
ATOM   3142 C CA   B PHE   A 1 132 ? 19.235 -0.153  -7.922  0.66 22.57 ?  132 PHE   A CA   1 
ATOM   3143 C C    A PHE   A 1 132 ? 18.115 -0.621  -7.959  0.34 16.61 ?  132 PHE   A C    1 
ATOM   3144 C C    B PHE   A 1 132 ? 18.332 -0.964  -8.841  0.66 22.36 ?  132 PHE   A C    1 
ATOM   3145 O O    A PHE   A 1 132 ? 18.760 -1.146  -8.874  0.34 16.88 ?  132 PHE   A O    1 
ATOM   3146 O O    B PHE   A 1 132 ? 18.843 -1.712  -9.680  0.66 22.73 ?  132 PHE   A O    1 
ATOM   3147 C CB   A PHE   A 1 132 ? 19.605 -0.862  -5.950  0.34 14.74 ?  132 PHE   A CB   1 
ATOM   3148 C CB   B PHE   A 1 132 ? 20.125 -1.066  -7.071  0.66 23.29 ?  132 PHE   A CB   1 
ATOM   3149 C CG   A PHE   A 1 132 ? 20.811 -0.271  -5.264  0.34 14.07 ?  132 PHE   A CG   1 
ATOM   3150 C CG   B PHE   A 1 132 ? 21.430 -0.433  -6.658  0.66 24.83 ?  132 PHE   A CG   1 
ATOM   3151 C CD1  A PHE   A 1 132 ? 20.675 0.760   -4.349  0.34 14.71 ?  132 PHE   A CD1  1 
ATOM   3152 C CD1  B PHE   A 1 132 ? 21.700 0.900   -6.939  0.66 25.95 ?  132 PHE   A CD1  1 
ATOM   3153 C CD2  A PHE   A 1 132 ? 22.081 -0.764  -5.523  0.34 13.84 ?  132 PHE   A CD2  1 
ATOM   3154 C CD2  B PHE   A 1 132 ? 22.391 -1.177  -6.000  0.66 25.19 ?  132 PHE   A CD2  1 
ATOM   3155 C CE1  A PHE   A 1 132 ? 21.784 1.297   -3.715  0.34 14.48 ?  132 PHE   A CE1  1 
ATOM   3156 C CE1  B PHE   A 1 132 ? 22.896 1.473   -6.566  0.66 26.29 ?  132 PHE   A CE1  1 
ATOM   3157 C CE2  A PHE   A 1 132 ? 23.192 -0.234  -4.889  0.34 13.84 ?  132 PHE   A CE2  1 
ATOM   3158 C CE2  B PHE   A 1 132 ? 23.591 -0.605  -5.623  0.66 25.75 ?  132 PHE   A CE2  1 
ATOM   3159 C CZ   A PHE   A 1 132 ? 23.044 0.797   -3.983  0.34 13.68 ?  132 PHE   A CZ   1 
ATOM   3160 C CZ   B PHE   A 1 132 ? 23.844 0.720   -5.907  0.66 26.03 ?  132 PHE   A CZ   1 
ATOM   3161 H H    A PHE   A 1 132 ? 17.730 0.622   -5.308  0.34 18.08 ?  132 PHE   A H    1 
ATOM   3162 H H    B PHE   A 1 132 ? 18.423 0.549   -6.254  0.66 27.21 ?  132 PHE   A H    1 
ATOM   3163 H HA   A PHE   A 1 132 ? 19.518 0.682   -7.275  0.34 18.97 ?  132 PHE   A HA   1 
ATOM   3164 H HA   B PHE   A 1 132 ? 19.808 0.367   -8.507  0.66 27.23 ?  132 PHE   A HA   1 
ATOM   3165 H HB2  A PHE   A 1 132 ? 19.003 -1.176  -5.258  0.34 17.84 ?  132 PHE   A HB2  1 
ATOM   3166 H HB2  B PHE   A 1 132 ? 19.645 -1.307  -6.264  0.66 28.10 ?  132 PHE   A HB2  1 
ATOM   3167 H HB3  A PHE   A 1 132 ? 19.910 -1.609  -6.486  0.34 17.84 ?  132 PHE   A HB3  1 
ATOM   3168 H HB3  B PHE   A 1 132 ? 20.329 -1.864  -7.583  0.66 28.10 ?  132 PHE   A HB3  1 
ATOM   3169 H HD1  A PHE   A 1 132 ? 19.833 1.101   -4.159  0.34 17.81 ?  132 PHE   A HD1  1 
ATOM   3170 H HD1  B PHE   A 1 132 ? 21.063 1.414   -7.385  0.66 31.29 ?  132 PHE   A HD1  1 
ATOM   3171 H HD2  A PHE   A 1 132 ? 22.191 -1.459  -6.127  0.34 16.76 ?  132 PHE   A HD2  1 
ATOM   3172 H HD2  B PHE   A 1 132 ? 22.227 -2.071  -5.806  0.66 30.38 ?  132 PHE   A HD2  1 
ATOM   3173 H HE1  A PHE   A 1 132 ? 21.683 1.992   -3.102  0.34 17.53 ?  132 PHE   A HE1  1 
ATOM   3174 H HE1  B PHE   A 1 132 ? 23.062 2.368   -6.761  0.66 31.71 ?  132 PHE   A HE1  1 
ATOM   3175 H HE2  A PHE   A 1 132 ? 24.039 -0.571  -5.073  0.34 16.76 ?  132 PHE   A HE2  1 
ATOM   3176 H HE2  B PHE   A 1 132 ? 24.229 -1.114  -5.179  0.66 31.05 ?  132 PHE   A HE2  1 
ATOM   3177 H HZ   A PHE   A 1 132 ? 23.790 1.158   -3.558  0.34 16.56 ?  132 PHE   A HZ   1 
ATOM   3178 H HZ   B PHE   A 1 132 ? 24.651 1.105   -5.654  0.66 31.38 ?  132 PHE   A HZ   1 
ATOM   3179 N N    A GLY   A 1 133 ? 16.787 -0.690  -7.890  0.34 17.02 ?  133 GLY   A N    1 
ATOM   3180 N N    B GLY   A 1 133 ? 17.016 -0.840  -8.695  0.66 21.84 ?  133 GLY   A N    1 
ATOM   3181 C CA   A GLY   A 1 133 ? 15.985 -1.074  -9.033  0.34 17.75 ?  133 GLY   A CA   1 
ATOM   3182 C CA   B GLY   A 1 133 ? 16.088 -1.246  -9.727  0.66 21.83 ?  133 GLY   A CA   1 
ATOM   3183 C C    A GLY   A 1 133 ? 15.696 -2.548  -9.212  0.34 18.13 ?  133 GLY   A C    1 
ATOM   3184 C C    B GLY   A 1 133 ? 15.691 -2.706  -9.740  0.66 22.19 ?  133 GLY   A C    1 
ATOM   3185 O O    A GLY   A 1 133 ? 15.123 -2.919  -10.244 0.34 18.81 ?  133 GLY   A O    1 
ATOM   3186 O O    B GLY   A 1 133 ? 14.876 -3.093  -10.588 0.66 23.00 ?  133 GLY   A O    1 
ATOM   3187 H H    A GLY   A 1 133 ? 16.324 -0.512  -7.183  0.34 20.58 ?  133 GLY   A H    1 
ATOM   3188 H H    B GLY   A 1 133 ? 16.640 -0.520  -7.993  0.66 26.36 ?  133 GLY   A H    1 
ATOM   3189 H HA2  A GLY   A 1 133 ? 15.131 -0.617  -8.975  0.34 21.45 ?  133 GLY   A HA2  1 
ATOM   3190 H HA2  B GLY   A 1 133 ? 15.285 -0.703  -9.647  0.66 26.35 ?  133 GLY   A HA2  1 
ATOM   3191 H HA3  A GLY   A 1 133 ? 16.431 -0.767  -9.834  0.34 21.45 ?  133 GLY   A HA3  1 
ATOM   3192 H HA3  B GLY   A 1 133 ? 16.483 -1.055  -10.593 0.66 26.35 ?  133 GLY   A HA3  1 
ATOM   3193 N N    A ALA   A 1 134 ? 16.056 -3.402  -8.259  0.34 18.16 ?  134 ALA   A N    1 
ATOM   3194 N N    B ALA   A 1 134 ? 16.224 -3.533  -8.848  0.66 21.59 ?  134 ALA   A N    1 
ATOM   3195 C CA   A ALA   A 1 134 ? 15.733 -4.815  -8.390  0.34 18.57 ?  134 ALA   A CA   1 
ATOM   3196 C CA   B ALA   A 1 134 ? 15.877 -4.944  -8.896  0.66 21.50 ?  134 ALA   A CA   1 
ATOM   3197 C C    A ALA   A 1 134 ? 14.401 -5.127  -7.716  0.34 18.76 ?  134 ALA   A C    1 
ATOM   3198 C C    B ALA   A 1 134 ? 14.525 -5.199  -8.235  0.66 21.13 ?  134 ALA   A C    1 
ATOM   3199 O O    A ALA   A 1 134 ? 13.902 -4.369  -6.880  0.34 19.47 ?  134 ALA   A O    1 
ATOM   3200 O O    B ALA   A 1 134 ? 13.982 -4.359  -7.511  0.66 21.38 ?  134 ALA   A O    1 
ATOM   3201 C CB   A ALA   A 1 134 ? 16.834 -5.696  -7.802  0.34 18.67 ?  134 ALA   A CB   1 
ATOM   3202 C CB   B ALA   A 1 134 ? 16.951 -5.797  -8.227  0.66 21.78 ?  134 ALA   A CB   1 
ATOM   3203 H H    A ALA   A 1 134 ? 16.477 -3.189  -7.537  0.34 21.95 ?  134 ALA   A H    1 
ATOM   3204 H H    B ALA   A 1 134 ? 16.780 -3.307  -8.232  0.66 26.07 ?  134 ALA   A H    1 
ATOM   3205 H HA   A ALA   A 1 134 ? 15.649 -5.031  -9.330  0.34 22.44 ?  134 ALA   A HA   1 
ATOM   3206 H HA   B ALA   A 1 134 ? 15.810 -5.212  -9.824  0.66 25.95 ?  134 ALA   A HA   1 
ATOM   3207 H HB1  A ALA   A 1 134 ? 16.602 -6.626  -7.955  0.34 22.56 ?  134 ALA   A HB1  1 
ATOM   3208 H HB1  B ALA   A 1 134 ? 16.693 -6.730  -8.294  0.66 26.29 ?  134 ALA   A HB1  1 
ATOM   3209 H HB2  A ALA   A 1 134 ? 17.671 -5.487  -8.244  0.34 22.56 ?  134 ALA   A HB2  1 
ATOM   3210 H HB2  B ALA   A 1 134 ? 17.794 -5.653  -8.683  0.66 26.29 ?  134 ALA   A HB2  1 
ATOM   3211 H HB3  A ALA   A 1 134 ? 16.905 -5.523  -6.853  0.34 22.56 ?  134 ALA   A HB3  1 
ATOM   3212 H HB3  B ALA   A 1 134 ? 17.026 -5.539  -7.297  0.66 26.29 ?  134 ALA   A HB3  1 
ATOM   3213 N N    A ASP   A 1 135 ? 13.825 -6.256  -8.104  0.34 18.09 ?  135 ASP   A N    1 
ATOM   3214 N N    B ASP   A 1 135 ? 13.982 -6.382  -8.507  0.66 21.05 ?  135 ASP   A N    1 
ATOM   3215 C CA   A ASP   A 1 135 ? 12.568 -6.715  -7.528  0.34 17.46 ?  135 ASP   A CA   1 
ATOM   3216 C CA   B ASP   A 1 135 ? 12.689 -6.774  -7.962  0.66 21.19 ?  135 ASP   A CA   1 
ATOM   3217 C C    A ASP   A 1 135 ? 12.805 -7.127  -6.081  0.34 16.25 ?  135 ASP   A C    1 
ATOM   3218 C C    B ASP   A 1 135 ? 12.860 -7.276  -6.531  0.66 19.24 ?  135 ASP   A C    1 
ATOM   3219 O O    A ASP   A 1 135 ? 13.565 -8.074  -5.836  0.34 15.59 ?  135 ASP   A O    1 
ATOM   3220 O O    B ASP   A 1 135 ? 13.667 -8.182  -6.290  0.66 18.05 ?  135 ASP   A O    1 
ATOM   3221 C CB   A ASP   A 1 135 ? 12.064 -7.912  -8.331  0.34 18.44 ?  135 ASP   A CB   1 
ATOM   3222 C CB   B ASP   A 1 135 ? 12.079 -7.876  -8.818  0.66 24.12 ?  135 ASP   A CB   1 
ATOM   3223 C CG   A ASP   A 1 135 ? 10.663 -8.348  -7.925  0.34 19.20 ?  135 ASP   A CG   1 
ATOM   3224 C CG   B ASP   A 1 135 ? 10.873 -8.523  -8.170  0.66 26.57 ?  135 ASP   A CG   1 
ATOM   3225 O OD1  A ASP   A 1 135 ? 10.182 -7.905  -6.861  0.34 19.26 ?  135 ASP   A OD1  1 
ATOM   3226 O OD1  B ASP   A 1 135 ? 9.840  -7.844  -8.008  0.66 28.15 ?  135 ASP   A OD1  1 
ATOM   3227 O OD2  A ASP   A 1 135 ? 10.036 -9.123  -8.681  0.34 20.33 -1 135 ASP   A OD2  1 
ATOM   3228 O OD2  B ASP   A 1 135 ? 10.961 -9.718  -7.828  0.66 27.15 -1 135 ASP   A OD2  1 
ATOM   3229 H H    A ASP   A 1 135 ? 14.145 -6.781  -8.703  0.34 21.86 ?  135 ASP   A H    1 
ATOM   3230 H H    B ASP   A 1 135 ? 14.348 -6.977  -9.008  0.66 25.41 ?  135 ASP   A H    1 
ATOM   3231 H HA   A ASP   A 1 135 ? 11.904 -6.009  -7.572  0.34 21.10 ?  135 ASP   A HA   1 
ATOM   3232 H HA   B ASP   A 1 135 ? 12.097 -6.006  -7.983  0.66 25.58 ?  135 ASP   A HA   1 
ATOM   3233 H HB2  A ASP   A 1 135 ? 12.030 -7.671  -9.268  0.34 22.28 ?  135 ASP   A HB2  1 
ATOM   3234 H HB2  B ASP   A 1 135 ? 11.800 -7.497  -9.664  0.66 29.10 ?  135 ASP   A HB2  1 
ATOM   3235 H HB3  A ASP   A 1 135 ? 12.680 -8.655  -8.204  0.34 22.28 ?  135 ASP   A HB3  1 
ATOM   3236 H HB3  B ASP   A 1 135 ? 12.742 -8.565  -8.958  0.66 29.10 ?  135 ASP   A HB3  1 
ATOM   3237 N N    A PRO   A 1 136 ? 12.196 -6.458  -5.096  0.34 15.84 ?  136 PRO   A N    1 
ATOM   3238 N N    B PRO   A 1 136 ? 12.126 -6.720  -5.564  0.66 18.56 ?  136 PRO   A N    1 
ATOM   3239 C CA   A PRO   A 1 136 ? 12.438 -6.856  -3.698  0.34 15.44 ?  136 PRO   A CA   1 
ATOM   3240 C CA   B PRO   A 1 136 ? 12.330 -7.130  -4.164  0.66 17.59 ?  136 PRO   A CA   1 
ATOM   3241 C C    A PRO   A 1 136 ? 11.984 -8.274  -3.376  0.34 14.50 ?  136 PRO   A C    1 
ATOM   3242 C C    B PRO   A 1 136 ? 11.953 -8.575  -3.878  0.66 16.66 ?  136 PRO   A C    1 
ATOM   3243 O O    A PRO   A 1 136 ? 12.564 -8.911  -2.487  0.34 13.78 ?  136 PRO   A O    1 
ATOM   3244 O O    B PRO   A 1 136 ? 12.556 -9.189  -2.990  0.66 15.47 ?  136 PRO   A O    1 
ATOM   3245 C CB   A PRO   A 1 136 ? 11.684 -5.790  -2.887  0.34 16.01 ?  136 PRO   A CB   1 
ATOM   3246 C CB   B PRO   A 1 136 ? 11.464 -6.136  -3.375  0.66 18.76 ?  136 PRO   A CB   1 
ATOM   3247 C CG   A PRO   A 1 136 ? 10.678 -5.224  -3.833  0.34 16.55 ?  136 PRO   A CG   1 
ATOM   3248 C CG   B PRO   A 1 136 ? 10.464 -5.630  -4.368  0.66 19.84 ?  136 PRO   A CG   1 
ATOM   3249 C CD   A PRO   A 1 136 ? 11.291 -5.299  -5.195  0.34 16.04 ?  136 PRO   A CD   1 
ATOM   3250 C CD   B PRO   A 1 136 ? 11.151 -5.623  -5.689  0.66 19.46 ?  136 PRO   A CD   1 
ATOM   3251 H HA   A PRO   A 1 136 ? 13.384 -6.779  -3.496  0.34 18.68 ?  136 PRO   A HA   1 
ATOM   3252 H HA   B PRO   A 1 136 ? 13.263 -6.998  -3.913  0.66 21.26 ?  136 PRO   A HA   1 
ATOM   3253 H HB2  A PRO   A 1 136 ? 11.247 -6.201  -2.127  0.34 19.37 ?  136 PRO   A HB2  1 
ATOM   3254 H HB2  B PRO   A 1 136 ? 11.026 -6.597  -2.642  0.66 22.67 ?  136 PRO   A HB2  1 
ATOM   3255 H HB3  A PRO   A 1 136 ? 12.303 -5.098  -2.595  0.34 19.37 ?  136 PRO   A HB3  1 
ATOM   3256 H HB3  B PRO   A 1 136 ? 12.021 -5.412  -3.039  0.66 22.67 ?  136 PRO   A HB3  1 
ATOM   3257 H HG2  A PRO   A 1 136 ? 9.868  -5.758  -3.798  0.34 20.01 ?  136 PRO   A HG2  1 
ATOM   3258 H HG2  B PRO   A 1 136 ? 9.704  -6.226  -4.390  0.66 23.96 ?  136 PRO   A HG2  1 
ATOM   3259 H HG3  A PRO   A 1 136 ? 10.489 -4.304  -3.597  0.34 20.01 ?  136 PRO   A HG3  1 
ATOM   3260 H HG3  B PRO   A 1 136 ? 10.195 -4.734  -4.125  0.66 23.96 ?  136 PRO   A HG3  1 
ATOM   3261 H HD2  A PRO   A 1 136 ? 10.605 -5.462  -5.865  0.34 19.40 ?  136 PRO   A HD2  1 
ATOM   3262 H HD2  B PRO   A 1 136 ? 10.521 -5.816  -6.400  0.66 23.50 ?  136 PRO   A HD2  1 
ATOM   3263 H HD3  A PRO   A 1 136 ? 11.793 -4.492  -5.391  0.34 19.40 ?  136 PRO   A HD3  1 
ATOM   3264 H HD3  B PRO   A 1 136 ? 11.605 -4.775  -5.836  0.66 23.50 ?  136 PRO   A HD3  1 
ATOM   3265 N N    A ILE   A 1 137 ? 10.969 -8.794  -4.071  0.34 14.69 ?  137 ILE   A N    1 
ATOM   3266 N N    B ILE   A 1 137 ? 10.965 -9.133  -4.584  0.66 17.42 ?  137 ILE   A N    1 
ATOM   3267 C CA   A ILE   A 1 137 ? 10.593 -10.193 -3.879  0.34 14.82 ?  137 ILE   A CA   1 
ATOM   3268 C CA   B ILE   A 1 137 ? 10.620 -10.544 -4.402  0.66 17.82 ?  137 ILE   A CA   1 
ATOM   3269 C C    A ILE   A 1 137 ? 11.744 -11.107 -4.278  0.34 14.24 ?  137 ILE   A C    1 
ATOM   3270 C C    B ILE   A 1 137 ? 11.829 -11.427 -4.696  0.66 16.98 ?  137 ILE   A C    1 
ATOM   3271 O O    A ILE   A 1 137 ? 12.040 -12.099 -3.598  0.34 14.35 ?  137 ILE   A O    1 
ATOM   3272 O O    B ILE   A 1 137 ? 12.168 -12.336 -3.926  0.66 16.87 ?  137 ILE   A O    1 
ATOM   3273 C CB   A ILE   A 1 137 ? 9.306  -10.518 -4.661  0.34 15.67 ?  137 ILE   A CB   1 
ATOM   3274 C CB   B ILE   A 1 137 ? 9.412  -10.917 -5.283  0.66 19.13 ?  137 ILE   A CB   1 
ATOM   3275 C CG1  A ILE   A 1 137 ? 8.155  -9.625  -4.191  0.34 16.78 ?  137 ILE   A CG1  1 
ATOM   3276 C CG1  B ILE   A 1 137 ? 8.140  -10.229 -4.773  0.66 20.24 ?  137 ILE   A CG1  1 
ATOM   3277 C CG2  A ILE   A 1 137 ? 8.949  -11.992 -4.501  0.34 15.96 ?  137 ILE   A CG2  1 
ATOM   3278 C CG2  B ILE   A 1 137 ? 9.224  -12.427 -5.326  0.66 19.90 ?  137 ILE   A CG2  1 
ATOM   3279 C CD1  A ILE   A 1 137 ? 6.872  -9.840  -4.958  0.34 17.45 ?  137 ILE   A CD1  1 
ATOM   3280 C CD1  B ILE   A 1 137 ? 6.902  -10.547 -5.588  0.66 21.36 ?  137 ILE   A CD1  1 
ATOM   3281 H H    A ILE   A 1 137 ? 10.500 -8.365  -4.649  0.34 17.78 ?  137 ILE   A H    1 
ATOM   3282 H H    B ILE   A 1 137 ? 10.486 -8.716  -5.160  0.66 21.05 ?  137 ILE   A H    1 
ATOM   3283 H HA   A ILE   A 1 137 ? 10.417 -10.337 -2.940  0.34 17.93 ?  137 ILE   A HA   1 
ATOM   3284 H HA   B ILE   A 1 137 ? 10.369 -10.684 -3.478  0.66 21.54 ?  137 ILE   A HA   1 
ATOM   3285 H HB   A ILE   A 1 137 ? 9.468  -10.341 -5.599  0.34 18.95 ?  137 ILE   A HB   1 
ATOM   3286 H HB   B ILE   A 1 137 ? 9.586  -10.604 -6.185  0.66 23.10 ?  137 ILE   A HB   1 
ATOM   3287 H HG12 A ILE   A 1 137 ? 7.979  -9.808  -3.254  0.34 20.29 ?  137 ILE   A HG12 1 
ATOM   3288 H HG12 B ILE   A 1 137 ? 7.980  -10.512 -3.860  0.66 24.44 ?  137 ILE   A HG12 1 
ATOM   3289 H HG13 A ILE   A 1 137 ? 8.412  -8.695  -4.300  0.34 20.29 ?  137 ILE   A HG13 1 
ATOM   3290 H HG13 B ILE   A 1 137 ? 8.276  -9.267  -4.799  0.66 24.44 ?  137 ILE   A HG13 1 
ATOM   3291 H HG21 A ILE   A 1 137 ? 8.092  -12.162 -4.917  0.34 19.31 ?  137 ILE   A HG21 1 
ATOM   3292 H HG21 B ILE   A 1 137 ? 8.392  -12.637 -5.776  0.66 24.04 ?  137 ILE   A HG21 1 
ATOM   3293 H HG22 A ILE   A 1 137 ? 9.631  -12.530 -4.929  0.34 19.31 ?  137 ILE   A HG22 1 
ATOM   3294 H HG22 B ILE   A 1 137 ? 9.959  -12.826 -5.815  0.66 24.04 ?  137 ILE   A HG22 1 
ATOM   3295 H HG23 A ILE   A 1 137 ? 8.906  -12.202 -3.556  0.34 19.31 ?  137 ILE   A HG23 1 
ATOM   3296 H HG23 B ILE   A 1 137 ? 9.204  -12.765 -4.419  0.66 24.04 ?  137 ILE   A HG23 1 
ATOM   3297 H HD11 A ILE   A 1 137 ? 6.534  -8.980  -5.241  0.34 21.09 ?  137 ILE   A HD11 1 
ATOM   3298 H HD11 B ILE   A 1 137 ? 6.231  -9.874  -5.413  0.66 25.78 ?  137 ILE   A HD11 1 
ATOM   3299 H HD12 A ILE   A 1 137 ? 7.056  -10.392 -5.735  0.34 21.09 ?  137 ILE   A HD12 1 
ATOM   3300 H HD12 B ILE   A 1 137 ? 7.139  -10.546 -6.529  0.66 25.78 ?  137 ILE   A HD12 1 
ATOM   3301 H HD13 A ILE   A 1 137 ? 6.229  -10.283 -4.382  0.34 21.09 ?  137 ILE   A HD13 1 
ATOM   3302 H HD13 B ILE   A 1 137 ? 6.575  -11.423 -5.332  0.66 25.78 ?  137 ILE   A HD13 1 
ATOM   3303 N N    A HIS   A 1 138 ? 12.403 -10.791 -5.395  0.34 13.91 ?  138 HIS   A N    1 
ATOM   3304 N N    B HIS   A 1 138 ? 12.491 -11.175 -5.825  0.66 16.92 ?  138 HIS   A N    1 
ATOM   3305 C CA   A HIS   A 1 138 ? 13.582 -11.547 -5.804  0.34 13.50 ?  138 HIS   A CA   1 
ATOM   3306 C CA   B HIS   A 1 138 ? 13.680 -11.943 -6.176  0.66 16.83 ?  138 HIS   A CA   1 
ATOM   3307 C C    A HIS   A 1 138 ? 14.718 -11.377 -4.802  0.34 12.50 ?  138 HIS   A C    1 
ATOM   3308 C C    B HIS   A 1 138 ? 14.784 -11.756 -5.142  0.66 15.60 ?  138 HIS   A C    1 
ATOM   3309 O O    A HIS   A 1 138 ? 15.395 -12.351 -4.446  0.34 12.74 ?  138 HIS   A O    1 
ATOM   3310 O O    B HIS   A 1 138 ? 15.467 -12.718 -4.769  0.66 15.96 ?  138 HIS   A O    1 
ATOM   3311 C CB   A HIS   A 1 138 ? 14.008 -11.115 -7.211  0.34 14.18 ?  138 HIS   A CB   1 
ATOM   3312 C CB   B HIS   A 1 138 ? 14.172 -11.527 -7.561  0.66 17.63 ?  138 HIS   A CB   1 
ATOM   3313 C CG   A HIS   A 1 138 ? 15.265 -11.771 -7.694  0.34 15.01 ?  138 HIS   A CG   1 
ATOM   3314 C CG   B HIS   A 1 138 ? 15.466 -12.166 -7.955  0.66 18.50 ?  138 HIS   A CG   1 
ATOM   3315 N ND1  A HIS   A 1 138 ? 15.351 -13.123 -7.952  0.34 15.71 ?  138 HIS   A ND1  1 
ATOM   3316 N ND1  B HIS   A 1 138 ? 15.586 -13.520 -8.183  0.66 19.03 ?  138 HIS   A ND1  1 
ATOM   3317 C CD2  A HIS   A 1 138 ? 16.487 -11.258 -7.970  0.34 15.34 ?  138 HIS   A CD2  1 
ATOM   3318 C CD2  B HIS   A 1 138 ? 16.700 -11.641 -8.147  0.66 18.95 ?  138 HIS   A CD2  1 
ATOM   3319 C CE1  A HIS   A 1 138 ? 16.573 -13.413 -8.365  0.34 15.96 ?  138 HIS   A CE1  1 
ATOM   3320 C CE1  B HIS   A 1 138 ? 16.835 -13.800 -8.508  0.66 19.27 ?  138 HIS   A CE1  1 
ATOM   3321 N NE2  A HIS   A 1 138 ? 17.282 -12.299 -8.383  0.34 15.71 ?  138 HIS   A NE2  1 
ATOM   3322 N NE2  B HIS   A 1 138 ? 17.532 -12.678 -8.492  0.66 19.08 ?  138 HIS   A NE2  1 
ATOM   3323 H H    A HIS   A 1 138 ? 12.189 -10.152 -5.931  0.34 16.84 ?  138 HIS   A H    1 
ATOM   3324 H H    B HIS   A 1 138 ? 12.277 -10.567 -6.394  0.66 20.45 ?  138 HIS   A H    1 
ATOM   3325 H HA   A HIS   A 1 138 ? 13.359 -12.486 -5.840  0.34 16.35 ?  138 HIS   A HA   1 
ATOM   3326 H HA   B HIS   A 1 138 ? 13.451 -12.883 -6.209  0.66 20.35 ?  138 HIS   A HA   1 
ATOM   3327 H HB2  A HIS   A 1 138 ? 13.299 -11.342 -7.837  0.34 17.17 ?  138 HIS   A HB2  1 
ATOM   3328 H HB2  B HIS   A 1 138 ? 13.504 -11.775 -8.220  0.66 21.30 ?  138 HIS   A HB2  1 
ATOM   3329 H HB3  A HIS   A 1 138 ? 14.156 -10.157 -7.219  0.34 17.17 ?  138 HIS   A HB3  1 
ATOM   3330 H HB3  B HIS   A 1 138 ? 14.301 -10.564 -7.573  0.66 21.30 ?  138 HIS   A HB3  1 
ATOM   3331 H HD1  A HIS   A 1 138 ? 14.710 -13.690 -7.861  0.34 19.00 ?  138 HIS   A HD1  1 
ATOM   3332 H HD2  A HIS   A 1 138 ? 16.742 -10.368 -7.896  0.34 18.56 ?  138 HIS   A HD2  1 
ATOM   3333 H HD2  B HIS   A 1 138 ? 16.939 -10.747 -8.063  0.66 22.89 ?  138 HIS   A HD2  1 
ATOM   3334 H HE1  A HIS   A 1 138 ? 16.880 -14.261 -8.601  0.34 19.31 ?  138 HIS   A HE1  1 
ATOM   3335 H HE1  B HIS   A 1 138 ? 17.163 -14.643 -8.711  0.66 23.27 ?  138 HIS   A HE1  1 
ATOM   3336 H HE2  B HIS   A 1 138 ? 18.370 -12.610 -8.669  0.66 23.05 ?  138 HIS   A HE2  1 
ATOM   3337 N N    A SER   A 1 139 ? 14.936 -10.147 -4.325  0.34 11.46 ?  139 SER   A N    1 
ATOM   3338 N N    B SER   A 1 139 ? 14.978 -10.523 -4.667  0.66 14.40 ?  139 SER   A N    1 
ATOM   3339 C CA   A SER   A 1 139 ? 15.998 -9.909  -3.352  0.34 11.15 ?  139 SER   A CA   1 
ATOM   3340 C CA   B SER   A 1 139 ? 16.050 -10.272 -3.709  0.66 13.28 ?  139 SER   A CA   1 
ATOM   3341 C C    A SER   A 1 139 ? 15.784 -10.739 -2.092  0.34 10.86 ?  139 SER   A C    1 
ATOM   3342 C C    B SER   A 1 139 ? 15.826 -11.039 -2.413  0.66 13.14 ?  139 SER   A C    1 
ATOM   3343 O O    A SER   A 1 139 ? 16.739 -11.294 -1.534  0.34 11.17 ?  139 SER   A O    1 
ATOM   3344 O O    B SER   A 1 139 ? 16.776 -11.582 -1.835  0.66 12.94 ?  139 SER   A O    1 
ATOM   3345 C CB   A SER   A 1 139 ? 16.087 -8.413  -3.027  0.34 11.04 ?  139 SER   A CB   1 
ATOM   3346 C CB   B SER   A 1 139 ? 16.165 -8.775  -3.427  0.66 12.77 ?  139 SER   A CB   1 
ATOM   3347 O OG   A SER   A 1 139 ? 17.092 -8.154  -2.059  0.34 11.41 ?  139 SER   A OG   1 
ATOM   3348 O OG   B SER   A 1 139 ? 17.235 -8.520  -2.533  0.66 11.99 ?  139 SER   A OG   1 
ATOM   3349 H H    A SER   A 1 139 ? 14.488 -9.445  -4.539  0.34 13.91 ?  139 SER   A H    1 
ATOM   3350 H H    B SER   A 1 139 ? 14.520 -9.834  -4.877  0.66 17.43 ?  139 SER   A H    1 
ATOM   3351 H HA   A SER   A 1 139 ? 16.847 -10.174 -3.735  0.34 13.53 ?  139 SER   A HA   1 
ATOM   3352 H HA   B SER   A 1 139 ? 16.896 -10.571 -4.091  0.66 16.09 ?  139 SER   A HA   1 
ATOM   3353 H HB2  A SER   A 1 139 ? 16.299 -7.923  -3.842  0.34 13.40 ?  139 SER   A HB2  1 
ATOM   3354 H HB2  B SER   A 1 139 ? 16.351 -8.309  -4.253  0.66 15.48 ?  139 SER   A HB2  1 
ATOM   3355 H HB3  A SER   A 1 139 ? 15.242 -8.109  -2.672  0.34 13.40 ?  139 SER   A HB3  1 
ATOM   3356 H HB3  B SER   A 1 139 ? 15.341 -8.462  -3.035  0.66 15.48 ?  139 SER   A HB3  1 
ATOM   3357 H HG   A SER   A 1 139 ? 17.145 -7.322  -1.906  0.34 13.84 ?  139 SER   A HG   1 
ATOM   3358 H HG   B SER   A 1 139 ? 17.290 -7.697  -2.361  0.66 14.54 ?  139 SER   A HG   1 
ATOM   3359 N N    A LEU   A 1 140 ? 14.535 -10.853 -1.637  0.34 11.22 ?  140 LEU   A N    1 
ATOM   3360 N N    B LEU   A 1 140 ? 14.582 -11.094 -1.934  0.66 13.61 ?  140 LEU   A N    1 
ATOM   3361 C CA   A LEU   A 1 140 ? 14.270 -11.677 -0.461  0.34 11.71 ?  140 LEU   A CA   1 
ATOM   3362 C CA   B LEU   A 1 140 ? 14.303 -11.861 -0.725  0.66 13.42 ?  140 LEU   A CA   1 
ATOM   3363 C C    A LEU   A 1 140 ? 14.556 -13.150 -0.741  0.34 12.32 ?  140 LEU   A C    1 
ATOM   3364 C C    B LEU   A 1 140 ? 14.586 -13.340 -0.944  0.66 13.38 ?  140 LEU   A C    1 
ATOM   3365 O O    A LEU   A 1 140 ? 15.076 -13.861 0.127   0.34 12.40 ?  140 LEU   A O    1 
ATOM   3366 O O    B LEU   A 1 140 ? 15.166 -14.006 -0.079  0.66 13.77 ?  140 LEU   A O    1 
ATOM   3367 C CB   A LEU   A 1 140 ? 12.828 -11.474 0.004   0.34 11.74 ?  140 LEU   A CB   1 
ATOM   3368 C CB   B LEU   A 1 140 ? 12.853 -11.651 -0.294  0.66 14.11 ?  140 LEU   A CB   1 
ATOM   3369 C CG   A LEU   A 1 140 ? 12.362 -12.334 1.180   0.34 12.30 ?  140 LEU   A CG   1 
ATOM   3370 C CG   B LEU   A 1 140 ? 12.410 -12.475 0.917   0.66 14.80 ?  140 LEU   A CG   1 
ATOM   3371 C CD1  A LEU   A 1 140 ? 13.274 -12.164 2.381   0.34 12.82 ?  140 LEU   A CD1  1 
ATOM   3372 C CD1  B LEU   A 1 140 ? 13.270 -12.168 2.133   0.66 15.25 ?  140 LEU   A CD1  1 
ATOM   3373 C CD2  A LEU   A 1 140 ? 10.925 -11.998 1.549   0.34 12.53 ?  140 LEU   A CD2  1 
ATOM   3374 C CD2  B LEU   A 1 140 ? 10.941 -12.222 1.222   0.66 15.39 ?  140 LEU   A CD2  1 
ATOM   3375 H H    A LEU   A 1 140 ? 13.842 -10.478 -1.985  0.34 13.61 ?  140 LEU   A H    1 
ATOM   3376 H H    B LEU   A 1 140 ? 13.907 -10.706 -2.281  0.66 16.48 ?  140 LEU   A H    1 
ATOM   3377 H HA   A LEU   A 1 140 ? 14.853 -11.390 0.256   0.34 14.20 ?  140 LEU   A HA   1 
ATOM   3378 H HA   B LEU   A 1 140 ? 14.878 -11.551 -0.009  0.66 16.25 ?  140 LEU   A HA   1 
ATOM   3379 H HB2  A LEU   A 1 140 ? 12.719 -10.549 0.271   0.34 14.24 ?  140 LEU   A HB2  1 
ATOM   3380 H HB2  B LEU   A 1 140 ? 12.729 -10.719 -0.068  0.66 17.09 ?  140 LEU   A HB2  1 
ATOM   3381 H HB3  A LEU   A 1 140 ? 12.236 -11.666 -0.739  0.34 14.24 ?  140 LEU   A HB3  1 
ATOM   3382 H HB3  B LEU   A 1 140 ? 12.272 -11.890 -1.033  0.66 17.09 ?  140 LEU   A HB3  1 
ATOM   3383 H HG   A LEU   A 1 140 ? 12.385 -13.269 0.917   0.34 14.92 ?  140 LEU   A HG   1 
ATOM   3384 H HG   B LEU   A 1 140 ? 12.505 -13.421 0.715   0.66 17.91 ?  140 LEU   A HG   1 
ATOM   3385 H HD11 A LEU   A 1 140 ? 12.894 -12.649 3.132   0.34 15.53 ?  140 LEU   A HD11 1 
ATOM   3386 H HD11 B LEU   A 1 140 ? 12.888 -12.614 2.907   0.66 18.45 ?  140 LEU   A HD11 1 
ATOM   3387 H HD12 A LEU   A 1 140 ? 14.147 -12.523 2.165   0.34 15.53 ?  140 LEU   A HD12 1 
ATOM   3388 H HD12 B LEU   A 1 140 ? 14.167 -12.494 1.974   0.66 18.45 ?  140 LEU   A HD12 1 
ATOM   3389 H HD13 A LEU   A 1 140 ? 13.340 -11.223 2.593   0.34 15.53 ?  140 LEU   A HD13 1 
ATOM   3390 H HD13 B LEU   A 1 140 ? 13.279 -11.211 2.276   0.66 18.45 ?  140 LEU   A HD13 1 
ATOM   3391 H HD21 A LEU   A 1 140 ? 10.650 -12.557 2.295   0.34 15.18 ?  140 LEU   A HD21 1 
ATOM   3392 H HD21 B LEU   A 1 140 ? 10.679 -12.756 1.992   0.66 18.62 ?  140 LEU   A HD21 1 
ATOM   3393 H HD22 A LEU   A 1 140 ? 10.873 -11.063 1.801   0.34 15.18 ?  140 LEU   A HD22 1 
ATOM   3394 H HD22 B LEU   A 1 140 ? 10.815 -11.281 1.418   0.66 18.62 ?  140 LEU   A HD22 1 
ATOM   3395 H HD23 A LEU   A 1 140 ? 10.353 -12.167 0.783   0.34 15.18 ?  140 LEU   A HD23 1 
ATOM   3396 H HD23 B LEU   A 1 140 ? 10.407 -12.474 0.452   0.66 18.62 ?  140 LEU   A HD23 1 
ATOM   3397 N N    A ARG   A 1 141 ? 14.238 -13.619 -1.951  0.34 13.24 ?  141 ARG   A N    1 
ATOM   3398 N N    B ARG   A 1 141 ? 14.176 -13.871 -2.097  0.66 13.62 ?  141 ARG   A N    1 
ATOM   3399 C CA   A ARG   A 1 141 ? 14.445 -15.023 -2.300  0.34 14.42 ?  141 ARG   A CA   1 
ATOM   3400 C CA   B ARG   A 1 141 ? 14.460 -15.261 -2.426  0.66 14.90 ?  141 ARG   A CA   1 
ATOM   3401 C C    A ARG   A 1 141 ? 15.929 -15.378 -2.281  0.34 13.74 ?  141 ARG   A C    1 
ATOM   3402 C C    B ARG   A 1 141 ? 15.958 -15.521 -2.426  0.66 14.36 ?  141 ARG   A C    1 
ATOM   3403 O O    A ARG   A 1 141 ? 16.344 -16.337 -1.618  0.34 13.28 ?  141 ARG   A O    1 
ATOM   3404 O O    B ARG   A 1 141 ? 16.415 -16.541 -1.897  0.66 13.97 ?  141 ARG   A O    1 
ATOM   3405 C CB   A ARG   A 1 141 ? 13.832 -15.290 -3.680  0.34 16.48 ?  141 ARG   A CB   1 
ATOM   3406 C CB   B ARG   A 1 141 ? 13.863 -15.587 -3.795  0.66 16.93 ?  141 ARG   A CB   1 
ATOM   3407 C CG   A ARG   A 1 141 ? 13.812 -16.747 -4.125  0.34 18.73 ?  141 ARG   A CG   1 
ATOM   3408 C CG   B ARG   A 1 141 ? 13.947 -17.045 -4.204  0.66 19.50 ?  141 ARG   A CG   1 
ATOM   3409 C CD   A ARG   A 1 141 ? 12.757 -17.534 -3.382  0.34 20.76 ?  141 ARG   A CD   1 
ATOM   3410 C CD   B ARG   A 1 141 ? 12.919 -17.862 -3.471  0.66 22.01 ?  141 ARG   A CD   1 
ATOM   3411 N NE   A ARG   A 1 141 ? 13.341 -18.379 -2.350  0.34 21.74 ?  141 ARG   A NE   1 
ATOM   3412 N NE   B ARG   A 1 141 ? 13.507 -18.644 -2.394  0.66 23.45 ?  141 ARG   A NE   1 
ATOM   3413 C CZ   A ARG   A 1 141 ? 12.648 -18.956 -1.378  0.34 22.70 ?  141 ARG   A CZ   1 
ATOM   3414 C CZ   B ARG   A 1 141 ? 12.817 -19.163 -1.387  0.66 24.19 ?  141 ARG   A CZ   1 
ATOM   3415 N NH1  A ARG   A 1 141 ? 11.346 -18.757 -1.244  0.34 22.96 ?  141 ARG   A NH1  1 
ATOM   3416 N NH1  B ARG   A 1 141 ? 11.522 -18.930 -1.241  0.66 24.28 ?  141 ARG   A NH1  1 
ATOM   3417 N NH2  A ARG   A 1 141 ? 13.277 -19.749 -0.515  0.34 23.24 ?  141 ARG   A NH2  1 
ATOM   3418 N NH2  B ARG   A 1 141 ? 13.445 -19.928 -0.497  0.66 24.91 ?  141 ARG   A NH2  1 
ATOM   3419 H H    A ARG   A 1 141 ? 13.910 -13.142 -2.585  0.34 16.04 ?  141 ARG   A H    1 
ATOM   3420 H H    B ARG   A 1 141 ? 13.742 -13.449 -2.700  0.66 16.49 ?  141 ARG   A H    1 
ATOM   3421 H HA   A ARG   A 1 141 ? 13.993 -15.583 -1.654  0.34 17.46 ?  141 ARG   A HA   1 
ATOM   3422 H HA   B ARG   A 1 141 ? 14.055 -15.846 -1.765  0.66 18.03 ?  141 ARG   A HA   1 
ATOM   3423 H HB2  A ARG   A 1 141 ? 12.912 -14.975 -3.676  0.34 19.93 ?  141 ARG   A HB2  1 
ATOM   3424 H HB2  B ARG   A 1 141 ? 12.928 -15.333 -3.794  0.66 20.47 ?  141 ARG   A HB2  1 
ATOM   3425 H HB3  A ARG   A 1 141 ? 14.336 -14.795 -4.343  0.34 19.93 ?  141 ARG   A HB3  1 
ATOM   3426 H HB3  B ARG   A 1 141 ? 14.337 -15.073 -4.466  0.66 20.47 ?  141 ARG   A HB3  1 
ATOM   3427 H HG2  A ARG   A 1 141 ? 13.611 -16.792 -5.075  0.34 22.62 ?  141 ARG   A HG2  1 
ATOM   3428 H HG2  B ARG   A 1 141 ? 13.780 -17.123 -5.157  0.66 23.55 ?  141 ARG   A HG2  1 
ATOM   3429 H HG3  A ARG   A 1 141 ? 14.676 -17.152 -3.949  0.34 22.62 ?  141 ARG   A HG3  1 
ATOM   3430 H HG3  B ARG   A 1 141 ? 14.827 -17.397 -3.989  0.66 23.55 ?  141 ARG   A HG3  1 
ATOM   3431 H HD2  A ARG   A 1 141 ? 12.140 -16.922 -2.952  0.34 25.07 ?  141 ARG   A HD2  1 
ATOM   3432 H HD2  B ARG   A 1 141 ? 12.256 -17.267 -3.081  0.66 26.56 ?  141 ARG   A HD2  1 
ATOM   3433 H HD3  A ARG   A 1 141 ? 12.278 -18.101 -4.009  0.34 25.07 ?  141 ARG   A HD3  1 
ATOM   3434 H HD3  B ARG   A 1 141 ? 12.488 -18.468 -4.096  0.66 26.56 ?  141 ARG   A HD3  1 
ATOM   3435 H HE   A ARG   A 1 141 ? 14.174 -18.579 -2.420  0.34 26.24 ?  141 ARG   A HE   1 
ATOM   3436 H HE   B ARG   A 1 141 ? 14.338 -18.846 -2.455  0.66 28.29 ?  141 ARG   A HE   1 
ATOM   3437 H HH11 A ARG   A 1 141 ? 10.927 -18.251 -1.798  0.34 27.70 ?  141 ARG   A HH11 1 
ATOM   3438 H HH11 B ARG   A 1 141 ? 11.101 -18.445 -1.814  0.66 29.29 ?  141 ARG   A HH11 1 
ATOM   3439 H HH12 A ARG   A 1 141 ? 10.918 -19.140 -0.603  0.34 27.70 ?  141 ARG   A HH12 1 
ATOM   3440 H HH12 B ARG   A 1 141 ? 11.095 -19.274 -0.579  0.66 29.29 ?  141 ARG   A HH12 1 
ATOM   3441 H HH21 A ARG   A 1 141 ? 14.123 -19.885 -0.595  0.34 28.03 ?  141 ARG   A HH21 1 
ATOM   3442 H HH21 B ARG   A 1 141 ? 14.286 -20.082 -0.582  0.66 30.04 ?  141 ARG   A HH21 1 
ATOM   3443 H HH22 A ARG   A 1 141 ? 12.839 -20.124 0.123   0.34 28.03 ?  141 ARG   A HH22 1 
ATOM   3444 H HH22 B ARG   A 1 141 ? 13.010 -20.261 0.166   0.66 30.04 ?  141 ARG   A HH22 1 
ATOM   3445 N N    . VAL   A 1 142 ? 16.742 -14.613 -3.013  1.00 13.69 ?  142 VAL   A N    1 
ATOM   3446 C CA   . VAL   A 1 142 ? 18.188 -14.813 -3.026  1.00 13.71 ?  142 VAL   A CA   1 
ATOM   3447 C C    . VAL   A 1 142 ? 18.745 -14.760 -1.612  1.00 12.85 ?  142 VAL   A C    1 
ATOM   3448 O O    . VAL   A 1 142 ? 19.613 -15.561 -1.242  1.00 13.27 ?  142 VAL   A O    1 
ATOM   3449 C CB   . VAL   A 1 142 ? 18.875 -13.793 -3.952  1.00 14.19 ?  142 VAL   A CB   1 
ATOM   3450 C CG1  . VAL   A 1 142 ? 20.384 -13.979 -3.906  1.00 13.36 ?  142 VAL   A CG1  1 
ATOM   3451 C CG2  . VAL   A 1 142 ? 18.381 -13.933 -5.383  1.00 15.75 ?  142 VAL   A CG2  1 
ATOM   3452 H H    A VAL   A 1 142 ? 16.478 -13.962 -3.512  0.34 16.58 ?  142 VAL   A H    1 
ATOM   3453 H H    B VAL   A 1 142 ? 16.471 -13.892 -3.399  0.66 16.58 ?  142 VAL   A H    1 
ATOM   3454 H HA   . VAL   A 1 142 ? 18.379 -15.690 -3.378  1.00 16.61 ?  142 VAL   A HA   1 
ATOM   3455 H HB   . VAL   A 1 142 ? 18.676 -12.889 -3.646  1.00 17.18 ?  142 VAL   A HB   1 
ATOM   3456 H HG11 . VAL   A 1 142 ? 20.784 -13.493 -4.645  1.00 16.18 ?  142 VAL   A HG11 1 
ATOM   3457 H HG12 . VAL   A 1 142 ? 20.724 -13.630 -3.065  1.00 16.18 ?  142 VAL   A HG12 1 
ATOM   3458 H HG13 . VAL   A 1 142 ? 20.587 -14.922 -3.982  1.00 16.18 ?  142 VAL   A HG13 1 
ATOM   3459 H HG21 . VAL   A 1 142 ? 18.735 -13.198 -5.912  1.00 19.05 ?  142 VAL   A HG21 1 
ATOM   3460 H HG22 . VAL   A 1 142 ? 18.694 -14.776 -5.739  1.00 19.05 ?  142 VAL   A HG22 1 
ATOM   3461 H HG23 . VAL   A 1 142 ? 17.414 -13.905 -5.391  1.00 19.05 ?  142 VAL   A HG23 1 
ATOM   3462 N N    . CYS   A 1 143 ? 18.271 -13.808 -0.805  1.00 12.68 ?  143 CYS   A N    1 
ATOM   3463 C CA   . CYS   A 1 143 ? 18.723 -13.723 0.579   1.00 12.71 ?  143 CYS   A CA   1 
ATOM   3464 C C    . CYS   A 1 143 ? 18.491 -15.046 1.301   1.00 12.50 ?  143 CYS   A C    1 
ATOM   3465 O O    . CYS   A 1 143 ? 19.405 -15.621 1.899   1.00 12.45 ?  143 CYS   A O    1 
ATOM   3466 C CB   . CYS   A 1 143 ? 17.986 -12.590 1.289   1.00 13.20 ?  143 CYS   A CB   1 
ATOM   3467 S SG   . CYS   A 1 143 ? 18.472 -12.378 3.014   1.00 13.47 ?  143 CYS   A SG   1 
ATOM   3468 H H    . CYS   A 1 143 ? 17.691 -13.214 -1.026  1.00 15.36 ?  143 CYS   A H    1 
ATOM   3469 H HA   . CYS   A 1 143 ? 19.671 -13.536 0.601   1.00 15.41 ?  143 CYS   A HA   1 
ATOM   3470 H HB2  . CYS   A 1 143 ? 18.161 -11.760 0.821   1.00 15.99 ?  143 CYS   A HB2  1 
ATOM   3471 H HB3  . CYS   A 1 143 ? 17.038 -12.776 1.277   1.00 15.99 ?  143 CYS   A HB3  1 
ATOM   3472 H HG   . CYS   A 1 143 ? 19.652 -12.130 3.070   1.00 16.32 ?  143 CYS   A HG   1 
ATOM   3473 N N    . VAL   A 1 144 ? 17.263 -15.553 1.240   1.00 12.95 ?  144 VAL   A N    1 
ATOM   3474 C CA   . VAL   A 1 144 ? 16.910 -16.780 1.946   1.00 14.21 ?  144 VAL   A CA   1 
ATOM   3475 C C    . VAL   A 1 144 ? 17.745 -17.957 1.462   1.00 13.71 ?  144 VAL   A C    1 
ATOM   3476 O O    . VAL   A 1 144 ? 18.123 -18.833 2.251   1.00 14.41 ?  144 VAL   A O    1 
ATOM   3477 C CB   . VAL   A 1 144 ? 15.401 -17.032 1.769   1.00 16.26 ?  144 VAL   A CB   1 
ATOM   3478 C CG1  . VAL   A 1 144 ? 15.033 -18.474 2.078   1.00 17.57 ?  144 VAL   A CG1  1 
ATOM   3479 C CG2  . VAL   A 1 144 ? 14.611 -16.053 2.630   1.00 16.68 ?  144 VAL   A CG2  1 
ATOM   3480 H H    . VAL   A 1 144 ? 16.611 -15.209 0.790   1.00 15.69 ?  144 VAL   A H    1 
ATOM   3481 H HA   . VAL   A 1 144 ? 17.074 -16.664 2.889   1.00 17.21 ?  144 VAL   A HA   1 
ATOM   3482 H HB   . VAL   A 1 144 ? 15.157 -16.861 0.842   1.00 19.66 ?  144 VAL   A HB   1 
ATOM   3483 H HG11 . VAL   A 1 144 ? 14.069 -18.534 2.216   1.00 21.23 ?  144 VAL   A HG11 1 
ATOM   3484 H HG12 . VAL   A 1 144 ? 15.285 -19.039 1.330   1.00 21.23 ?  144 VAL   A HG12 1 
ATOM   3485 H HG13 . VAL   A 1 144 ? 15.493 -18.756 2.881   1.00 21.23 ?  144 VAL   A HG13 1 
ATOM   3486 H HG21 . VAL   A 1 144 ? 13.661 -16.254 2.559   1.00 20.16 ?  144 VAL   A HG21 1 
ATOM   3487 H HG22 . VAL   A 1 144 ? 14.894 -16.140 3.553   1.00 20.16 ?  144 VAL   A HG22 1 
ATOM   3488 H HG23 . VAL   A 1 144 ? 14.776 -15.148 2.318   1.00 20.16 ?  144 VAL   A HG23 1 
ATOM   3489 N N    . ASP   A 1 145 ? 18.025 -18.011 0.163   1.00 14.32 ?  145 ASP   A N    1 
ATOM   3490 C CA   . ASP   A 1 145 ? 18.746 -19.128 -0.439  1.00 15.11 ?  145 ASP   A CA   1 
ATOM   3491 C C    . ASP   A 1 145 ? 20.265 -18.979 -0.375  1.00 14.68 ?  145 ASP   A C    1 
ATOM   3492 O O    . ASP   A 1 145 ? 20.977 -19.882 -0.827  1.00 17.00 ?  145 ASP   A O    1 
ATOM   3493 C CB   . ASP   A 1 145 ? 18.313 -19.291 -1.899  1.00 16.76 ?  145 ASP   A CB   1 
ATOM   3494 C CG   . ASP   A 1 145 ? 16.878 -19.765 -2.036  1.00 18.91 ?  145 ASP   A CG   1 
ATOM   3495 O OD1  . ASP   A 1 145 ? 16.299 -20.270 -1.044  1.00 19.59 ?  145 ASP   A OD1  1 
ATOM   3496 O OD2  . ASP   A 1 145 ? 16.332 -19.633 -3.150  1.00 20.44 -1 145 ASP   A OD2  1 
ATOM   3497 H H    . ASP   A 1 145 ? 17.796 -17.401 -0.401  1.00 17.34 ?  145 ASP   A H    1 
ATOM   3498 H HA   . ASP   A 1 145 ? 18.507 -19.938 0.033   1.00 18.28 ?  145 ASP   A HA   1 
ATOM   3499 H HB2  . ASP   A 1 145 ? 18.395 -18.436 -2.354  1.00 20.27 ?  145 ASP   A HB2  1 
ATOM   3500 H HB3  . ASP   A 1 145 ? 18.884 -19.948 -2.326  1.00 20.27 ?  145 ASP   A HB3  1 
ATOM   3501 N N    . THR   A 1 146 ? 20.777 -17.873 0.165   1.00 13.04 ?  146 THR   A N    1 
ATOM   3502 C CA   . THR   A 1 146 ? 22.211 -17.594 0.189   1.00 12.69 ?  146 THR   A CA   1 
ATOM   3503 C C    . THR   A 1 146 ? 22.749 -17.395 1.595   1.00 12.62 ?  146 THR   A C    1 
ATOM   3504 O O    . THR   A 1 146 ? 23.830 -17.913 1.924   1.00 13.30 ?  146 THR   A O    1 
ATOM   3505 C CB   . THR   A 1 146 ? 22.519 -16.344 -0.663  1.00 12.50 ?  146 THR   A CB   1 
ATOM   3506 O OG1  . THR   A 1 146 ? 22.019 -16.529 -1.990  1.00 13.16 ?  146 THR   A OG1  1 
ATOM   3507 C CG2  . THR   A 1 146 ? 24.015 -16.080 -0.731  1.00 13.00 ?  146 THR   A CG2  1 
ATOM   3508 H H    . THR   A 1 146 ? 20.300 -17.253 0.529   1.00 15.80 ?  146 THR   A H    1 
ATOM   3509 H HA   . THR   A 1 146 ? 22.685 -18.337 -0.200  1.00 15.38 ?  146 THR   A HA   1 
ATOM   3510 H HB   . THR   A 1 146 ? 22.095 -15.565 -0.267  1.00 15.15 ?  146 THR   A HB   1 
ATOM   3511 H HG1  . THR   A 1 146 ? 21.189 -16.638 -1.963  1.00 15.94 ?  146 THR   A HG1  1 
ATOM   3512 H HG21 . THR   A 1 146 ? 24.200 -15.410 -1.410  1.00 15.75 ?  146 THR   A HG21 1 
ATOM   3513 H HG22 . THR   A 1 146 ? 24.335 -15.749 0.125   1.00 15.75 ?  146 THR   A HG22 1 
ATOM   3514 H HG23 . THR   A 1 146 ? 24.485 -16.894 -0.954  1.00 15.75 ?  146 THR   A HG23 1 
ATOM   3515 N N    . VAL   A 1 147 ? 22.056 -16.618 2.421   1.00 12.21 ?  147 VAL   A N    1 
ATOM   3516 C CA   . VAL   A 1 147 ? 22.531 -16.310 3.764   1.00 12.16 ?  147 VAL   A CA   1 
ATOM   3517 C C    . VAL   A 1 147 ? 22.204 -17.481 4.679   1.00 12.60 ?  147 VAL   A C    1 
ATOM   3518 O O    . VAL   A 1 147 ? 21.061 -17.961 4.713   1.00 13.21 ?  147 VAL   A O    1 
ATOM   3519 C CB   . VAL   A 1 147 ? 21.890 -15.009 4.270   1.00 12.38 ?  147 VAL   A CB   1 
ATOM   3520 C CG1  . VAL   A 1 147 ? 22.381 -14.681 5.663   1.00 13.40 ?  147 VAL   A CG1  1 
ATOM   3521 C CG2  . VAL   A 1 147 ? 22.151 -13.863 3.292   1.00 12.59 ?  147 VAL   A CG2  1 
ATOM   3522 H H    . VAL   A 1 147 ? 21.296 -16.263 2.236   1.00 14.80 ?  147 VAL   A H    1 
ATOM   3523 H HA   . VAL   A 1 147 ? 23.494 -16.191 3.749   1.00 14.74 ?  147 VAL   A HA   1 
ATOM   3524 H HB   . VAL   A 1 147 ? 20.932 -15.139 4.325   1.00 15.01 ?  147 VAL   A HB   1 
ATOM   3525 H HG11 . VAL   A 1 147 ? 22.110 -13.779 5.889   1.00 16.23 ?  147 VAL   A HG11 1 
ATOM   3526 H HG12 . VAL   A 1 147 ? 21.984 -15.308 6.295   1.00 16.23 ?  147 VAL   A HG12 1 
ATOM   3527 H HG13 . VAL   A 1 147 ? 23.345 -14.757 5.687   1.00 16.23 ?  147 VAL   A HG13 1 
ATOM   3528 H HG21 . VAL   A 1 147 ? 21.811 -13.040 3.679   1.00 15.26 ?  147 VAL   A HG21 1 
ATOM   3529 H HG22 . VAL   A 1 147 ? 23.100 -13.793 3.135   1.00 15.26 ?  147 VAL   A HG22 1 
ATOM   3530 H HG23 . VAL   A 1 147 ? 21.685 -14.052 2.462   1.00 15.26 ?  147 VAL   A HG23 1 
ATOM   3531 N N    . ARG   A 1 148 ? 23.218 -17.938 5.422   1.00 12.96 ?  148 ARG   A N    1 
ATOM   3532 C CA   . ARG   A 1 148 ? 23.085 -19.020 6.386   1.00 13.28 ?  148 ARG   A CA   1 
ATOM   3533 C C    . ARG   A 1 148 ? 23.200 -18.551 7.823   1.00 13.25 ?  148 ARG   A C    1 
ATOM   3534 O O    . ARG   A 1 148 ? 22.785 -19.275 8.734   1.00 14.60 ?  148 ARG   A O    1 
ATOM   3535 C CB   . ARG   A 1 148 ? 24.136 -20.108 6.123   1.00 13.88 ?  148 ARG   A CB   1 
ATOM   3536 C CG   . ARG   A 1 148 ? 23.983 -20.759 4.769   1.00 14.87 ?  148 ARG   A CG   1 
ATOM   3537 C CD   . ARG   A 1 148 ? 25.077 -21.782 4.492   1.00 15.71 ?  148 ARG   A CD   1 
ATOM   3538 N NE   . ARG   A 1 148 ? 26.411 -21.193 4.509   1.00 15.62 ?  148 ARG   A NE   1 
ATOM   3539 C CZ   . ARG   A 1 148 ? 26.923 -20.473 3.521   1.00 14.54 ?  148 ARG   A CZ   1 
ATOM   3540 N NH1  . ARG   A 1 148 ? 26.247 -20.246 2.406   1.00 14.84 ?  148 ARG   A NH1  1 
ATOM   3541 N NH2  . ARG   A 1 148 ? 28.140 -19.948 3.660   1.00 15.11 ?  148 ARG   A NH2  1 
ATOM   3542 H H    . ARG   A 1 148 ? 24.023 -17.624 5.367   1.00 15.70 ?  148 ARG   A H    1 
ATOM   3543 H HA   . ARG   A 1 148 ? 22.211 -19.418 6.281   1.00 16.09 ?  148 ARG   A HA   1 
ATOM   3544 H HB2  . ARG   A 1 148 ? 25.018 -19.714 6.170   1.00 16.81 ?  148 ARG   A HB2  1 
ATOM   3545 H HB3  . ARG   A 1 148 ? 24.042 -20.799 6.797   1.00 16.81 ?  148 ARG   A HB3  1 
ATOM   3546 H HG2  . ARG   A 1 148 ? 23.127 -21.208 4.734   1.00 17.99 ?  148 ARG   A HG2  1 
ATOM   3547 H HG3  . ARG   A 1 148 ? 24.029 -20.070 4.088   1.00 17.99 ?  148 ARG   A HG3  1 
ATOM   3548 H HD2  . ARG   A 1 148 ? 25.049 -22.471 5.174   1.00 19.01 ?  148 ARG   A HD2  1 
ATOM   3549 H HD3  . ARG   A 1 148 ? 24.930 -22.173 3.617   1.00 19.01 ?  148 ARG   A HD3  1 
ATOM   3550 H HE   . ARG   A 1 148 ? 26.904 -21.326 5.200   1.00 18.89 ?  148 ARG   A HE   1 
ATOM   3551 H HH11 . ARG   A 1 148 ? 25.461 -20.570 2.306   1.00 17.97 ?  148 ARG   A HH11 1 
ATOM   3552 H HH12 . ARG   A 1 148 ? 26.600 -19.770 1.780   1.00 17.97 ?  148 ARG   A HH12 1 
ATOM   3553 H HH21 . ARG   A 1 148 ? 28.591 -20.087 4.379   1.00 18.28 ?  148 ARG   A HH21 1 
ATOM   3554 H HH22 . ARG   A 1 148 ? 28.487 -19.477 3.025   1.00 18.28 ?  148 ARG   A HH22 1 
ATOM   3555 N N    . THR   A 1 149 ? 23.744 -17.359 8.039   1.00 13.03 ?  149 THR   A N    1 
ATOM   3556 C CA   . THR   A 1 149 ? 23.815 -16.755 9.354   1.00 13.19 ?  149 THR   A CA   1 
ATOM   3557 C C    . THR   A 1 149 ? 22.486 -16.059 9.652   1.00 12.65 ?  149 THR   A C    1 
ATOM   3558 O O    . THR   A 1 149 ? 21.557 -16.053 8.831   1.00 13.43 ?  149 THR   A O    1 
ATOM   3559 C CB   . THR   A 1 149 ? 25.011 -15.812 9.406   1.00 13.47 ?  149 THR   A CB   1 
ATOM   3560 O OG1  . THR   A 1 149 ? 24.877 -14.881 8.330   1.00 13.60 ?  149 THR   A OG1  1 
ATOM   3561 C CG2  . THR   A 1 149 ? 26.327 -16.601 9.279   1.00 13.87 ?  149 THR   A CG2  1 
ATOM   3562 H H    . THR   A 1 149 ? 24.098 -16.863 7.419   1.00 15.79 ?  149 THR   A H    1 
ATOM   3563 H HA   . THR   A 1 149 ? 23.948 -17.460 10.011  1.00 15.97 ?  149 THR   A HA   1 
ATOM   3564 H HB   . THR   A 1 149 ? 25.006 -15.344 10.252  1.00 16.31 ?  149 THR   A HB   1 
ATOM   3565 H HG1  . THR   A 1 149 ? 25.522 -14.343 8.333   1.00 16.47 ?  149 THR   A HG1  1 
ATOM   3566 H HG21 . THR   A 1 149 ? 27.083 -15.998 9.335   1.00 16.79 ?  149 THR   A HG21 1 
ATOM   3567 H HG22 . THR   A 1 149 ? 26.397 -17.258 9.994   1.00 16.79 ?  149 THR   A HG22 1 
ATOM   3568 H HG23 . THR   A 1 149 ? 26.361 -17.068 8.427   1.00 16.79 ?  149 THR   A HG23 1 
ATOM   3569 N N    . ASN   A 1 150 ? 22.355 -15.528 10.863  1.00 13.27 ?  150 ASN   A N    1 
ATOM   3570 C CA   . ASN   A 1 150 ? 21.068 -15.010 11.322  1.00 13.53 ?  150 ASN   A CA   1 
ATOM   3571 C C    . ASN   A 1 150 ? 20.890 -13.574 10.853  1.00 12.97 ?  150 ASN   A C    1 
ATOM   3572 O O    . ASN   A 1 150 ? 21.638 -12.678 11.263  1.00 14.23 ?  150 ASN   A O    1 
ATOM   3573 C CB   . ASN   A 1 150 ? 20.979 -15.106 12.840  1.00 15.65 ?  150 ASN   A CB   1 
ATOM   3574 C CG   . ASN   A 1 150 ? 20.906 -16.536 13.316  1.00 19.51 ?  150 ASN   A CG   1 
ATOM   3575 O OD1  . ASN   A 1 150 ? 20.343 -17.394 12.636  1.00 20.90 ?  150 ASN   A OD1  1 
ATOM   3576 N ND2  . ASN   A 1 150 ? 21.498 -16.810 14.475  1.00 21.77 ?  150 ASN   A ND2  1 
ATOM   3577 H H    . ASN   A 1 150 ? 22.989 -15.456 11.434  1.00 16.08 ?  150 ASN   A H    1 
ATOM   3578 H HA   . ASN   A 1 150 ? 20.351 -15.544 10.946  1.00 16.39 ?  150 ASN   A HA   1 
ATOM   3579 H HB2  . ASN   A 1 150 ? 21.764 -14.695 13.234  1.00 18.93 ?  150 ASN   A HB2  1 
ATOM   3580 H HB3  . ASN   A 1 150 ? 20.177 -14.646 13.143  1.00 18.93 ?  150 ASN   A HB3  1 
ATOM   3581 H HD21 . ASN   A 1 150 ? 21.486 -17.611 14.791  1.00 26.28 ?  150 ASN   A HD21 1 
ATOM   3582 H HD22 . ASN   A 1 150 ? 21.889 -16.183 14.918  1.00 26.28 ?  150 ASN   A HD22 1 
ATOM   3583 N N    . VAL   A 1 151 ? 19.900 -13.351 9.997   1.00 12.46 ?  151 VAL   A N    1 
ATOM   3584 C CA   . VAL   A 1 151 ? 19.690 -12.055 9.374   1.00 12.39 ?  151 VAL   A CA   1 
ATOM   3585 C C    . VAL   A 1 151 ? 18.298 -11.539 9.711   1.00 12.58 ?  151 VAL   A C    1 
ATOM   3586 O O    . VAL   A 1 151 ? 17.292 -12.254 9.566   1.00 13.77 ?  151 VAL   A O    1 
ATOM   3587 C CB   . VAL   A 1 151 ? 19.993 -12.066 7.862   1.00 13.30 ?  151 VAL   A CB   1 
ATOM   3588 C CG1  . VAL   A 1 151 ? 19.159 -13.080 7.119   1.00 14.59 ?  151 VAL   A CG1  1 
ATOM   3589 C CG2  . VAL   A 1 151 ? 19.835 -10.663 7.269   1.00 13.85 ?  151 VAL   A CG2  1 
ATOM   3590 H H    . VAL   A 1 151 ? 19.324 -13.947 9.759   1.00 15.11 ?  151 VAL   A H    1 
ATOM   3591 H HA   . VAL   A 1 151 ? 20.323 -11.433 9.772   1.00 15.02 ?  151 VAL   A HA   1 
ATOM   3592 H HB   . VAL   A 1 151 ? 20.922 -12.320 7.742   1.00 16.11 ?  151 VAL   A HB   1 
ATOM   3593 H HG11 . VAL   A 1 151 ? 19.378 -13.048 6.176   1.00 17.66 ?  151 VAL   A HG11 1 
ATOM   3594 H HG12 . VAL   A 1 151 ? 19.349 -13.968 7.470   1.00 17.66 ?  151 VAL   A HG12 1 
ATOM   3595 H HG13 . VAL   A 1 151 ? 18.217 -12.876 7.246   1.00 17.66 ?  151 VAL   A HG13 1 
ATOM   3596 H HG21 . VAL   A 1 151 ? 20.151 -10.675 6.350   1.00 16.77 ?  151 VAL   A HG21 1 
ATOM   3597 H HG22 . VAL   A 1 151 ? 18.900 -10.412 7.291   1.00 16.77 ?  151 VAL   A HG22 1 
ATOM   3598 H HG23 . VAL   A 1 151 ? 20.362 -10.038 7.789   1.00 16.77 ?  151 VAL   A HG23 1 
ATOM   3599 N N    A TYR   A 1 152 ? 18.255 -10.275 10.136  0.34 12.58 ?  152 TYR   A N    1 
ATOM   3600 N N    B TYR   A 1 152 ? 18.265 -10.303 10.192  0.66 12.23 ?  152 TYR   A N    1 
ATOM   3601 C CA   A TYR   A 1 152 ? 17.042 -9.575  10.540  0.34 12.57 ?  152 TYR   A CA   1 
ATOM   3602 C CA   B TYR   A 1 152 ? 17.053 -9.580  10.533  0.66 12.22 ?  152 TYR   A CA   1 
ATOM   3603 C C    A TYR   A 1 152 ? 16.801 -8.455  9.535   0.34 12.20 ?  152 TYR   A C    1 
ATOM   3604 C C    B TYR   A 1 152 ? 16.867 -8.506  9.472   0.66 11.31 ?  152 TYR   A C    1 
ATOM   3605 O O    A TYR   A 1 152 ? 17.466 -7.416  9.576   0.34 12.99 ?  152 TYR   A O    1 
ATOM   3606 O O    B TYR   A 1 152 ? 17.662 -7.562  9.390   0.66 11.31 ?  152 TYR   A O    1 
ATOM   3607 C CB   A TYR   A 1 152 ? 17.201 -9.058  11.965  0.34 13.04 ?  152 TYR   A CB   1 
ATOM   3608 C CB   B TYR   A 1 152 ? 17.200 -8.999  11.936  0.66 13.19 ?  152 TYR   A CB   1 
ATOM   3609 C CG   A TYR   A 1 152 ? 17.204 -10.181 12.973  0.34 13.38 ?  152 TYR   A CG   1 
ATOM   3610 C CG   B TYR   A 1 152 ? 17.126 -10.080 12.986  0.66 13.85 ?  152 TYR   A CG   1 
ATOM   3611 C CD1  A TYR   A 1 152 ? 18.377 -10.846 13.303  0.34 14.27 ?  152 TYR   A CD1  1 
ATOM   3612 C CD1  B TYR   A 1 152 ? 18.203 -10.922 13.231  0.66 15.37 ?  152 TYR   A CD1  1 
ATOM   3613 C CD2  A TYR   A 1 152 ? 16.025 -10.604 13.566  0.34 13.41 ?  152 TYR   A CD2  1 
ATOM   3614 C CD2  B TYR   A 1 152 ? 15.957 -10.296 13.699  0.66 14.06 ?  152 TYR   A CD2  1 
ATOM   3615 C CE1  A TYR   A 1 152 ? 18.380 -11.889 14.212  0.34 14.83 ?  152 TYR   A CE1  1 
ATOM   3616 C CE1  B TYR   A 1 152 ? 18.127 -11.933 14.176  0.66 16.78 ?  152 TYR   A CE1  1 
ATOM   3617 C CE2  A TYR   A 1 152 ? 16.014 -11.649 14.475  0.34 13.92 ?  152 TYR   A CE2  1 
ATOM   3618 C CE2  B TYR   A 1 152 ? 15.867 -11.304 14.644  0.66 15.82 ?  152 TYR   A CE2  1 
ATOM   3619 C CZ   A TYR   A 1 152 ? 17.197 -12.287 14.796  0.34 14.69 ?  152 TYR   A CZ   1 
ATOM   3620 C CZ   B TYR   A 1 152 ? 16.955 -12.117 14.881  0.66 17.12 ?  152 TYR   A CZ   1 
ATOM   3621 O OH   A TYR   A 1 152 ? 17.195 -13.329 15.698  0.34 15.78 ?  152 TYR   A OH   1 
ATOM   3622 O OH   B TYR   A 1 152 ? 16.873 -13.121 15.818  0.66 19.41 ?  152 TYR   A OH   1 
ATOM   3623 H H    A TYR   A 1 152 ? 18.957 -9.771  10.189  0.34 15.25 ?  152 TYR   A H    1 
ATOM   3624 H H    B TYR   A 1 152 ? 18.979 -9.827  10.318  0.66 14.83 ?  152 TYR   A H    1 
ATOM   3625 H HA   A TYR   A 1 152 ? 16.292 -10.181 10.510  0.34 15.24 ?  152 TYR   A HA   1 
ATOM   3626 H HA   B TYR   A 1 152 ? 16.295 -10.186 10.514  0.66 14.82 ?  152 TYR   A HA   1 
ATOM   3627 H HB2  A TYR   A 1 152 ? 18.043 -8.585  12.038  0.34 15.80 ?  152 TYR   A HB2  1 
ATOM   3628 H HB2  B TYR   A 1 152 ? 18.061 -8.560  12.011  0.66 15.98 ?  152 TYR   A HB2  1 
ATOM   3629 H HB3  A TYR   A 1 152 ? 16.466 -8.463  12.173  0.34 15.80 ?  152 TYR   A HB3  1 
ATOM   3630 H HB3  B TYR   A 1 152 ? 16.483 -8.367  12.095  0.66 15.98 ?  152 TYR   A HB3  1 
ATOM   3631 H HD1  A TYR   A 1 152 ? 19.176 -10.581 12.909  0.34 17.28 ?  152 TYR   A HD1  1 
ATOM   3632 H HD1  B TYR   A 1 152 ? 18.994 -10.797 12.756  0.66 18.59 ?  152 TYR   A HD1  1 
ATOM   3633 H HD2  A TYR   A 1 152 ? 15.227 -10.175 13.349  0.34 16.24 ?  152 TYR   A HD2  1 
ATOM   3634 H HD2  B TYR   A 1 152 ? 15.218 -9.751  13.545  0.66 17.02 ?  152 TYR   A HD2  1 
ATOM   3635 H HE1  A TYR   A 1 152 ? 19.174 -12.320 14.429  0.34 17.95 ?  152 TYR   A HE1  1 
ATOM   3636 H HE1  B TYR   A 1 152 ? 18.865 -12.480 14.334  0.66 20.29 ?  152 TYR   A HE1  1 
ATOM   3637 H HE2  A TYR   A 1 152 ? 15.214 -11.913 14.870  0.34 16.85 ?  152 TYR   A HE2  1 
ATOM   3638 H HE2  B TYR   A 1 152 ? 15.081 -11.433 15.125  0.66 19.14 ?  152 TYR   A HE2  1 
ATOM   3639 H HH   A TYR   A 1 152 ? 16.412 -13.458 15.980  0.34 19.08 ?  152 TYR   A HH   1 
ATOM   3640 H HH   B TYR   A 1 152 ? 16.129 -13.098 16.202  0.66 23.44 ?  152 TYR   A HH   1 
ATOM   3641 N N    . LEU   A 1 153 ? 15.854 -8.680  8.627   1.00 12.14 ?  153 LEU   A N    1 
ATOM   3642 C CA   . LEU   A 1 153 ? 15.592 -7.781  7.514   1.00 12.36 ?  153 LEU   A CA   1 
ATOM   3643 C C    . LEU   A 1 153 ? 14.575 -6.723  7.898   1.00 12.84 ?  153 LEU   A C    1 
ATOM   3644 O O    . LEU   A 1 153 ? 13.464 -7.042  8.345   1.00 13.83 ?  153 LEU   A O    1 
ATOM   3645 C CB   . LEU   A 1 153 ? 15.053 -8.567  6.318   1.00 12.83 ?  153 LEU   A CB   1 
ATOM   3646 C CG   . LEU   A 1 153 ? 16.013 -9.570  5.693   1.00 12.71 ?  153 LEU   A CG   1 
ATOM   3647 C CD1  . LEU   A 1 153 ? 15.263 -10.446 4.709   1.00 13.37 ?  153 LEU   A CD1  1 
ATOM   3648 C CD2  . LEU   A 1 153 ? 17.167 -8.837  5.015   1.00 13.66 ?  153 LEU   A CD2  1 
ATOM   3649 H H    A LEU   A 1 153 ? 15.341 -9.374  8.633   0.34 14.72 ?  153 LEU   A H    1 
ATOM   3650 H H    B LEU   A 1 153 ? 15.293 -9.334  8.676   0.66 14.72 ?  153 LEU   A H    1 
ATOM   3651 H HA   . LEU   A 1 153 ? 16.414 -7.346  7.254   1.00 14.98 ?  153 LEU   A HA   1 
ATOM   3652 H HB2  . LEU   A 1 153 ? 14.265 -9.048  6.600   1.00 15.54 ?  153 LEU   A HB2  1 
ATOM   3653 H HB3  . LEU   A 1 153 ? 14.809 -7.926  5.624   1.00 15.54 ?  153 LEU   A HB3  1 
ATOM   3654 H HG   . LEU   A 1 153 ? 16.385 -10.133 6.393   1.00 15.41 ?  153 LEU   A HG   1 
ATOM   3655 H HD11 . LEU   A 1 153 ? 15.884 -11.074 4.314   1.00 16.20 ?  153 LEU   A HD11 1 
ATOM   3656 H HD12 . LEU   A 1 153 ? 14.563 -10.916 5.183   1.00 16.20 ?  153 LEU   A HD12 1 
ATOM   3657 H HD13 . LEU   A 1 153 ? 14.879 -9.879  4.022   1.00 16.20 ?  153 LEU   A HD13 1 
ATOM   3658 H HD21 . LEU   A 1 153 ? 17.711 -9.484  4.547   1.00 16.55 ?  153 LEU   A HD21 1 
ATOM   3659 H HD22 . LEU   A 1 153 ? 16.798 -8.193  4.393   1.00 16.55 ?  153 LEU   A HD22 1 
ATOM   3660 H HD23 . LEU   A 1 153 ? 17.692 -8.384  5.692   1.00 16.55 ?  153 LEU   A HD23 1 
ATOM   3661 N N    . ALA   A 1 154 ? 14.947 -5.468  7.685   1.00 12.80 ?  154 ALA   A N    1 
ATOM   3662 C CA   . ALA   A 1 154 ? 14.064 -4.328  7.886   1.00 13.36 ?  154 ALA   A CA   1 
ATOM   3663 C C    . ALA   A 1 154 ? 13.581 -3.839  6.525   1.00 13.56 ?  154 ALA   A C    1 
ATOM   3664 O O    . ALA   A 1 154 ? 14.393 -3.415  5.693   1.00 14.42 ?  154 ALA   A O    1 
ATOM   3665 C CB   . ALA   A 1 154 ? 14.786 -3.201  8.622   1.00 13.87 ?  154 ALA   A CB   1 
ATOM   3666 H H    . ALA   A 1 154 ? 15.728 -5.242  7.398   1.00 15.51 ?  154 ALA   A H    1 
ATOM   3667 H HA   . ALA   A 1 154 ? 13.293 -4.597  8.409   1.00 16.19 ?  154 ALA   A HA   1 
ATOM   3668 H HB1  . ALA   A 1 154 ? 14.174 -2.457  8.741   1.00 16.79 ?  154 ALA   A HB1  1 
ATOM   3669 H HB2  . ALA   A 1 154 ? 15.087 -3.525  9.481   1.00 16.79 ?  154 ALA   A HB2  1 
ATOM   3670 H HB3  . ALA   A 1 154 ? 15.549 -2.914  8.089   1.00 16.79 ?  154 ALA   A HB3  1 
ATOM   3671 N N    A VAL   A 1 155 ? 12.268 -3.896  6.325   0.34 14.32 ?  155 VAL   A N    1 
ATOM   3672 N N    B VAL   A 1 155 ? 12.267 -3.923  6.291   0.66 13.85 ?  155 VAL   A N    1 
ATOM   3673 C CA   A VAL   A 1 155 ? 11.597 -3.349  5.154   0.34 14.91 ?  155 VAL   A CA   1 
ATOM   3674 C CA   B VAL   A 1 155 ? 11.633 -3.566  5.017   0.66 13.81 ?  155 VAL   A CA   1 
ATOM   3675 C C    A VAL   A 1 155 ? 10.950 -2.040  5.585   0.34 14.69 ?  155 VAL   A C    1 
ATOM   3676 C C    B VAL   A 1 155 ? 10.885 -2.249  5.219   0.66 13.26 ?  155 VAL   A C    1 
ATOM   3677 O O    A VAL   A 1 155 ? 10.035 -2.031  6.415   0.34 14.72 ?  155 VAL   A O    1 
ATOM   3678 O O    B VAL   A 1 155 ? 9.908  -2.198  5.977   0.66 13.29 ?  155 VAL   A O    1 
ATOM   3679 C CB   A VAL   A 1 155 ? 10.554 -4.331  4.605   0.34 15.33 ?  155 VAL   A CB   1 
ATOM   3680 C CB   B VAL   A 1 155 ? 10.684 -4.673  4.513   0.66 14.18 ?  155 VAL   A CB   1 
ATOM   3681 C CG1  A VAL   A 1 155 ? 9.888  -3.762  3.363   0.34 16.07 ?  155 VAL   A CG1  1 
ATOM   3682 C CG1  B VAL   A 1 155 ? 9.895  -4.194  3.300   0.66 14.58 ?  155 VAL   A CG1  1 
ATOM   3683 C CG2  A VAL   A 1 155 ? 11.205 -5.666  4.300   0.34 15.35 ?  155 VAL   A CG2  1 
ATOM   3684 C CG2  B VAL   A 1 155 ? 11.468 -5.937  4.148   0.66 15.07 ?  155 VAL   A CG2  1 
ATOM   3685 H H    A VAL   A 1 155 ? 11.721 -4.270  6.877   0.34 17.34 ?  155 VAL   A H    1 
ATOM   3686 H H    B VAL   A 1 155 ? 11.695 -4.191  6.880   0.66 16.77 ?  155 VAL   A H    1 
ATOM   3687 H HA   A VAL   A 1 155 ? 12.247 -3.157  4.465   0.34 18.04 ?  155 VAL   A HA   1 
ATOM   3688 H HA   B VAL   A 1 155 ? 12.308 -3.435  4.341   0.66 16.73 ?  155 VAL   A HA   1 
ATOM   3689 H HB   A VAL   A 1 155 ? 9.866  -4.473  5.278   0.34 18.55 ?  155 VAL   A HB   1 
ATOM   3690 H HB   B VAL   A 1 155 ? 10.052 -4.912  5.208   0.66 17.16 ?  155 VAL   A HB   1 
ATOM   3691 H HG11 A VAL   A 1 155 ? 9.322  -4.445  2.971   0.34 19.44 ?  155 VAL   A HG11 1 
ATOM   3692 H HG11 B VAL   A 1 155 ? 9.526  -4.961  2.831   0.66 17.64 ?  155 VAL   A HG11 1 
ATOM   3693 H HG12 A VAL   A 1 155 ? 9.353  -2.992  3.610   0.34 19.44 ?  155 VAL   A HG12 1 
ATOM   3694 H HG12 B VAL   A 1 155 ? 9.174  -3.617  3.597   0.66 17.64 ?  155 VAL   A HG12 1 
ATOM   3695 H HG13 A VAL   A 1 155 ? 10.575 -3.500  2.730   0.34 19.44 ?  155 VAL   A HG13 1 
ATOM   3696 H HG13 B VAL   A 1 155 ? 10.489 -3.705  2.708   0.66 17.64 ?  155 VAL   A HG13 1 
ATOM   3697 H HG21 A VAL   A 1 155 ? 10.561 -6.233  3.854   0.34 18.57 ?  155 VAL   A HG21 1 
ATOM   3698 H HG21 B VAL   A 1 155 ? 10.861 -6.602  3.787   0.66 18.23 ?  155 VAL   A HG21 1 
ATOM   3699 H HG22 A VAL   A 1 155 ? 11.971 -5.515  3.723   0.34 18.57 ?  155 VAL   A HG22 1 
ATOM   3700 H HG22 B VAL   A 1 155 ? 12.140 -5.711  3.482   0.66 18.23 ?  155 VAL   A HG22 1 
ATOM   3701 H HG23 A VAL   A 1 155 ? 11.493 -6.076  5.130   0.34 18.57 ?  155 VAL   A HG23 1 
ATOM   3702 H HG23 B VAL   A 1 155 ? 11.901 -6.282  4.945   0.66 18.23 ?  155 VAL   A HG23 1 
ATOM   3703 N N    A PHE   A 1 156 ? 11.422 -0.928  5.019   0.34 14.81 ?  156 PHE   A N    1 
ATOM   3704 N N    B PHE   A 1 156 ? 11.312 -1.199  4.503   0.66 13.21 ?  156 PHE   A N    1 
ATOM   3705 C CA   A PHE   A 1 156 ? 10.921 0.383   5.425   0.34 15.37 ?  156 PHE   A CA   1 
ATOM   3706 C CA   B PHE   A 1 156 ? 10.805 0.156   4.745   0.66 13.29 ?  156 PHE   A CA   1 
ATOM   3707 C C    A PHE   A 1 156 ? 9.457  0.576   5.042   0.34 14.63 ?  156 PHE   A C    1 
ATOM   3708 C C    B PHE   A 1 156 ? 9.343  0.322   4.330   0.66 13.59 ?  156 PHE   A C    1 
ATOM   3709 O O    A PHE   A 1 156 ? 8.688  1.182   5.799   0.34 14.76 ?  156 PHE   A O    1 
ATOM   3710 O O    B PHE   A 1 156 ? 8.560  0.958   5.048   0.66 14.99 ?  156 PHE   A O    1 
ATOM   3711 C CB   A PHE   A 1 156 ? 11.787 1.484   4.806   0.34 16.76 ?  156 PHE   A CB   1 
ATOM   3712 C CB   B PHE   A 1 156 ? 11.708 1.142   3.993   0.66 12.68 ?  156 PHE   A CB   1 
ATOM   3713 C CG   A PHE   A 1 156 ? 11.294 2.877   5.094   0.34 18.54 ?  156 PHE   A CG   1 
ATOM   3714 C CG   B PHE   A 1 156 ? 11.401 2.620   4.215   0.66 12.84 ?  156 PHE   A CG   1 
ATOM   3715 C CD1  A PHE   A 1 156 ? 11.245 3.350   6.394   0.34 19.56 ?  156 PHE   A CD1  1 
ATOM   3716 C CD1  B PHE   A 1 156 ? 11.918 3.301   5.313   0.66 14.17 ?  156 PHE   A CD1  1 
ATOM   3717 C CD2  A PHE   A 1 156 ? 10.888 3.713   4.066   0.34 19.34 ?  156 PHE   A CD2  1 
ATOM   3718 C CD2  B PHE   A 1 156 ? 10.674 3.338   3.278   0.66 13.95 ?  156 PHE   A CD2  1 
ATOM   3719 C CE1  A PHE   A 1 156 ? 10.792 4.627   6.667   0.34 20.09 ?  156 PHE   A CE1  1 
ATOM   3720 C CE1  B PHE   A 1 156 ? 11.674 4.661   5.491   0.66 14.99 ?  156 PHE   A CE1  1 
ATOM   3721 C CE2  A PHE   A 1 156 ? 10.436 4.995   4.332   0.34 19.94 ?  156 PHE   A CE2  1 
ATOM   3722 C CE2  B PHE   A 1 156 ? 10.434 4.694   3.451   0.66 14.55 ?  156 PHE   A CE2  1 
ATOM   3723 C CZ   A PHE   A 1 156 ? 10.389 5.452   5.635   0.34 20.30 ?  156 PHE   A CZ   1 
ATOM   3724 C CZ   B PHE   A 1 156 ? 10.937 5.354   4.560   0.66 15.01 ?  156 PHE   A CZ   1 
ATOM   3725 H H    A PHE   A 1 156 ? 12.024 -0.906  4.408   0.34 17.93 ?  156 PHE   A H    1 
ATOM   3726 H H    B PHE   A 1 156 ? 11.889 -1.260  3.869   0.66 16.01 ?  156 PHE   A H    1 
ATOM   3727 H HA   A PHE   A 1 156 ? 10.987 0.467   6.387   0.34 18.60 ?  156 PHE   A HA   1 
ATOM   3728 H HA   B PHE   A 1 156 ? 10.862 0.337   5.687   0.66 16.10 ?  156 PHE   A HA   1 
ATOM   3729 H HB2  A PHE   A 1 156 ? 12.689 1.411   5.157   0.34 20.27 ?  156 PHE   A HB2  1 
ATOM   3730 H HB2  B PHE   A 1 156 ? 12.620 0.983   4.278   0.66 15.37 ?  156 PHE   A HB2  1 
ATOM   3731 H HB3  A PHE   A 1 156 ? 11.802 1.370   3.842   0.34 20.27 ?  156 PHE   A HB3  1 
ATOM   3732 H HB3  B PHE   A 1 156 ? 11.632 0.963   3.041   0.66 15.37 ?  156 PHE   A HB3  1 
ATOM   3733 H HD1  A PHE   A 1 156 ? 11.515 2.798   7.093   0.34 23.62 ?  156 PHE   A HD1  1 
ATOM   3734 H HD1  B PHE   A 1 156 ? 12.422 2.829   5.945   0.66 17.16 ?  156 PHE   A HD1  1 
ATOM   3735 H HD2  A PHE   A 1 156 ? 10.920 3.409   3.187   0.34 23.36 ?  156 PHE   A HD2  1 
ATOM   3736 H HD2  B PHE   A 1 156 ? 10.334 2.900   2.531   0.66 16.89 ?  156 PHE   A HD2  1 
ATOM   3737 H HE1  A PHE   A 1 156 ? 10.763 4.930   7.547   0.34 24.26 ?  156 PHE   A HE1  1 
ATOM   3738 H HE1  B PHE   A 1 156 ? 12.014 5.091   6.240   0.66 18.13 ?  156 PHE   A HE1  1 
ATOM   3739 H HE2  A PHE   A 1 156 ? 10.166 5.547   3.635   0.34 24.08 ?  156 PHE   A HE2  1 
ATOM   3740 H HE2  B PHE   A 1 156 ? 9.929  5.161   2.827   0.66 17.61 ?  156 PHE   A HE2  1 
ATOM   3741 H HZ   A PHE   A 1 156 ? 10.085 6.312   5.819   0.34 24.51 ?  156 PHE   A HZ   1 
ATOM   3742 H HZ   B PHE   A 1 156 ? 10.766 6.259   4.684   0.66 18.16 ?  156 PHE   A HZ   1 
ATOM   3743 N N    A ASP   A 1 157 ? 9.052  0.082   3.875   0.34 14.85 ?  157 ASP   A N    1 
ATOM   3744 N N    B ASP   A 1 157 ? 8.956  -0.225  3.176   0.66 14.53 ?  157 ASP   A N    1 
ATOM   3745 C CA   A ASP   A 1 157 ? 7.727  0.355   3.329   0.34 15.70 ?  157 ASP   A CA   1 
ATOM   3746 C CA   B ASP   A 1 157 ? 7.643  0.040   2.595   0.66 15.80 ?  157 ASP   A CA   1 
ATOM   3747 C C    A ASP   A 1 157 ? 6.732  -0.679  3.847   0.34 15.49 ?  157 ASP   A C    1 
ATOM   3748 C C    B ASP   A 1 157 ? 6.632  -0.999  3.075   0.66 15.10 ?  157 ASP   A C    1 
ATOM   3749 O O    A ASP   A 1 157 ? 6.930  -1.883  3.658   0.34 15.31 ?  157 ASP   A O    1 
ATOM   3750 O O    B ASP   A 1 157 ? 6.836  -2.200  2.879   0.66 14.36 ?  157 ASP   A O    1 
ATOM   3751 C CB   A ASP   A 1 157 ? 7.788  0.309   1.805   0.34 16.78 ?  157 ASP   A CB   1 
ATOM   3752 C CB   B ASP   A 1 157 ? 7.727  0.014   1.070   0.66 17.57 ?  157 ASP   A CB   1 
ATOM   3753 C CG   A ASP   A 1 157 ? 6.534  0.842   1.162   0.34 17.82 ?  157 ASP   A CG   1 
ATOM   3754 C CG   B ASP   A 1 157 ? 6.437  0.466   0.405   0.66 19.68 ?  157 ASP   A CG   1 
ATOM   3755 O OD1  A ASP   A 1 157 ? 6.387  2.081   1.109   0.34 19.49 ?  157 ASP   A OD1  1 
ATOM   3756 O OD1  B ASP   A 1 157 ? 6.151  1.682   0.413   0.66 21.97 ?  157 ASP   A OD1  1 
ATOM   3757 O OD2  A ASP   A 1 157 ? 5.690  0.032   0.722   0.34 17.49 -1 157 ASP   A OD2  1 
ATOM   3758 O OD2  B ASP   A 1 157 ? 5.698  -0.384  -0.131  0.66 20.38 -1 157 ASP   A OD2  1 
ATOM   3759 H H    A ASP   A 1 157 ? 9.531  -0.425  3.373   0.34 17.97 ?  157 ASP   A H    1 
ATOM   3760 H H    B ASP   A 1 157 ? 9.435  -0.772  2.707   0.66 17.59 ?  157 ASP   A H    1 
ATOM   3761 H HA   A ASP   A 1 157 ? 7.429  1.239   3.600   0.34 18.99 ?  157 ASP   A HA   1 
ATOM   3762 H HA   B ASP   A 1 157 ? 7.334  0.909   2.873   0.66 19.11 ?  157 ASP   A HA   1 
ATOM   3763 H HB2  A ASP   A 1 157 ? 8.538  0.844   1.501   0.34 20.29 ?  157 ASP   A HB2  1 
ATOM   3764 H HB2  B ASP   A 1 157 ? 8.439  0.601   0.786   0.66 21.23 ?  157 ASP   A HB2  1 
ATOM   3765 H HB3  A ASP   A 1 157 ? 7.901  -0.608  1.517   0.34 20.29 ?  157 ASP   A HB3  1 
ATOM   3766 H HB3  B ASP   A 1 157 ? 7.907  -0.896  0.776   0.66 21.23 ?  157 ASP   A HB3  1 
ATOM   3767 N N    A LYS   A 1 158 ? 5.654  -0.209  4.485   0.34 15.83 ?  158 LYS   A N    1 
ATOM   3768 N N    B LYS   A 1 158 ? 5.529  -0.533  3.672   0.66 15.66 ?  158 LYS   A N    1 
ATOM   3769 C CA   A LYS   A 1 158 ? 4.674  -1.134  5.051   0.34 16.47 ?  158 LYS   A CA   1 
ATOM   3770 C CA   B LYS   A 1 158 ? 4.520  -1.442  4.219   0.66 16.77 ?  158 LYS   A CA   1 
ATOM   3771 C C    A LYS   A 1 158 ? 3.964  -1.928  3.961   0.34 16.74 ?  158 LYS   A C    1 
ATOM   3772 C C    B LYS   A 1 158 ? 3.883  -2.305  3.130   0.66 16.20 ?  158 LYS   A C    1 
ATOM   3773 O O    A LYS   A 1 158 ? 3.791  -3.145  4.089   0.34 16.69 ?  158 LYS   A O    1 
ATOM   3774 O O    B LYS   A 1 158 ? 3.716  -3.519  3.300   0.66 16.14 ?  158 LYS   A O    1 
ATOM   3775 C CB   A LYS   A 1 158 ? 3.673  -0.378  5.932   0.34 16.84 ?  158 LYS   A CB   1 
ATOM   3776 C CB   B LYS   A 1 158 ? 3.450  -0.646  4.975   0.66 19.36 ?  158 LYS   A CB   1 
ATOM   3777 C CG   A LYS   A 1 158 ? 2.458  -1.198  6.372   0.34 17.51 ?  158 LYS   A CG   1 
ATOM   3778 C CG   B LYS   A 1 158 ? 2.240  -1.481  5.384   0.66 22.08 ?  158 LYS   A CG   1 
ATOM   3779 C CD   A LYS   A 1 158 ? 2.836  -2.447  7.166   0.34 18.01 ?  158 LYS   A CD   1 
ATOM   3780 C CD   B LYS   A 1 158 ? 1.284  -0.720  6.300   0.66 24.99 ?  158 LYS   A CD   1 
ATOM   3781 C CE   A LYS   A 1 158 ? 1.587  -3.154  7.690   0.34 18.09 ?  158 LYS   A CE   1 
ATOM   3782 C CE   B LYS   A 1 158 ? 0.598  0.440   5.590   0.66 27.53 ?  158 LYS   A CE   1 
ATOM   3783 N NZ   A LYS   A 1 158 ? 1.861  -4.507  8.252   0.34 17.94 ?  158 LYS   A NZ   1 
ATOM   3784 N NZ   B LYS   A 1 158 ? -0.513 1.021   6.405   0.66 28.50 ?  158 LYS   A NZ   1 
ATOM   3785 H H    A LYS   A 1 158 ? 5.469  0.623   4.597   0.34 19.15 ?  158 LYS   A H    1 
ATOM   3786 H H    B LYS   A 1 158 ? 5.350  0.297   3.782   0.66 18.94 ?  158 LYS   A H    1 
ATOM   3787 H HA   A LYS   A 1 158 ? 5.137  -1.767  5.617   0.34 19.91 ?  158 LYS   A HA   1 
ATOM   3788 H HA   B LYS   A 1 158 ? 4.942  -2.038  4.859   0.66 20.28 ?  158 LYS   A HA   1 
ATOM   3789 H HB2  A LYS   A 1 158 ? 4.131  -0.082  6.737   0.34 20.36 ?  158 LYS   A HB2  1 
ATOM   3790 H HB2  B LYS   A 1 158 ? 3.840  -0.281  5.787   0.66 23.38 ?  158 LYS   A HB2  1 
ATOM   3791 H HB3  A LYS   A 1 158 ? 3.344  0.392   5.444   0.34 20.36 ?  158 LYS   A HB3  1 
ATOM   3792 H HB3  B LYS   A 1 158 ? 3.132  0.075   4.411   0.66 23.38 ?  158 LYS   A HB3  1 
ATOM   3793 H HG2  A LYS   A 1 158 ? 1.899  -0.647  6.941   0.34 21.16 ?  158 LYS   A HG2  1 
ATOM   3794 H HG2  B LYS   A 1 158 ? 1.744  -1.736  4.590   0.66 26.65 ?  158 LYS   A HG2  1 
ATOM   3795 H HG3  A LYS   A 1 158 ? 1.954  -1.477  5.592   0.34 21.16 ?  158 LYS   A HG3  1 
ATOM   3796 H HG3  B LYS   A 1 158 ? 2.544  -2.272  5.856   0.66 26.65 ?  158 LYS   A HG3  1 
ATOM   3797 H HD2  A LYS   A 1 158 ? 3.318  -3.064  6.593   0.34 21.76 ?  158 LYS   A HD2  1 
ATOM   3798 H HD2  B LYS   A 1 158 ? 0.595  -1.327  6.616   0.66 30.15 ?  158 LYS   A HD2  1 
ATOM   3799 H HD3  A LYS   A 1 158 ? 3.387  -2.193  7.925   0.34 21.76 ?  158 LYS   A HD3  1 
ATOM   3800 H HD3  B LYS   A 1 158 ? 1.780  -0.362  7.052   0.66 30.15 ?  158 LYS   A HD3  1 
ATOM   3801 H HE2  A LYS   A 1 158 ? 1.187  -2.615  8.390   0.34 21.86 ?  158 LYS   A HE2  1 
ATOM   3802 H HE2  B LYS   A 1 158 ? 1.248  1.142   5.426   0.66 33.18 ?  158 LYS   A HE2  1 
ATOM   3803 H HE3  A LYS   A 1 158 ? 0.961  -3.260  6.962   0.34 21.86 ?  158 LYS   A HE3  1 
ATOM   3804 H HE3  B LYS   A 1 158 ? 0.225  0.128   4.752   0.66 33.18 ?  158 LYS   A HE3  1 
ATOM   3805 H HZ1  A LYS   A 1 158 ? 1.106  -4.876  8.545   0.34 21.68 ?  158 LYS   A HZ1  1 
ATOM   3806 H HZ1  B LYS   A 1 158 ? -0.894 1.696   5.966   0.66 34.35 ?  158 LYS   A HZ1  1 
ATOM   3807 H HZ2  A LYS   A 1 158 ? 2.214  -5.032  7.624   0.34 21.68 ?  158 LYS   A HZ2  1 
ATOM   3808 H HZ2  B LYS   A 1 158 ? -1.130 0.399   6.567   0.66 34.35 ?  158 LYS   A HZ2  1 
ATOM   3809 H HZ3  A LYS   A 1 158 ? 2.434  -4.448  8.932   0.34 21.68 ?  158 LYS   A HZ3  1 
ATOM   3810 H HZ3  B LYS   A 1 158 ? -0.198 1.324   7.181   0.66 34.35 ?  158 LYS   A HZ3  1 
ATOM   3811 N N    A ASN   A 1 159 ? 3.551  -1.265  2.879   0.34 17.65 ?  159 ASN   A N    1 
ATOM   3812 N N    B ASN   A 1 159 ? 3.487  -1.690  2.013   0.66 16.77 ?  159 ASN   A N    1 
ATOM   3813 C CA   A ASN   A 1 159 ? 2.870  -1.977  1.803   0.34 18.58 ?  159 ASN   A CA   1 
ATOM   3814 C CA   B ASN   A 1 159 ? 2.855  -2.459  0.944   0.66 18.02 ?  159 ASN   A CA   1 
ATOM   3815 C C    A ASN   A 1 159 ? 3.772  -3.044  1.196   0.34 18.08 ?  159 ASN   A C    1 
ATOM   3816 C C    B ASN   A 1 159 ? 3.790  -3.555  0.446   0.66 17.13 ?  159 ASN   A C    1 
ATOM   3817 O O    A ASN   A 1 159 ? 3.319  -4.155  0.900   0.34 18.34 ?  159 ASN   A O    1 
ATOM   3818 O O    B ASN   A 1 159 ? 3.368  -4.694  0.201   0.66 17.91 ?  159 ASN   A O    1 
ATOM   3819 C CB   A ASN   A 1 159 ? 2.389  -0.988  0.739   0.34 19.97 ?  159 ASN   A CB   1 
ATOM   3820 C CB   B ASN   A 1 159 ? 2.454  -1.523  -0.201  0.66 21.10 ?  159 ASN   A CB   1 
ATOM   3821 C CG   A ASN   A 1 159 ? 1.218  -0.151  1.215   0.34 21.47 ?  159 ASN   A CG   1 
ATOM   3822 C CG   B ASN   A 1 159 ? 1.443  -0.480  0.225   0.66 24.46 ?  159 ASN   A CG   1 
ATOM   3823 O OD1  A ASN   A 1 159 ? 0.362  -0.636  1.953   0.34 22.42 ?  159 ASN   A OD1  1 
ATOM   3824 O OD1  B ASN   A 1 159 ? 0.479  -0.792  0.921   0.66 25.63 ?  159 ASN   A OD1  1 
ATOM   3825 N ND2  A ASN   A 1 159 ? 1.173  1.110   0.795   0.34 22.16 ?  159 ASN   A ND2  1 
ATOM   3826 N ND2  B ASN   A 1 159 ? 1.657  0.768   -0.192  0.66 25.80 ?  159 ASN   A ND2  1 
ATOM   3827 H H    A ASN   A 1 159 ? 3.655  -0.424  2.745   0.34 21.33 ?  159 ASN   A H    1 
ATOM   3828 H H    B ASN   A 1 159 ? 3.569  -0.848  1.859   0.66 20.27 ?  159 ASN   A H    1 
ATOM   3829 H HA   A ASN   A 1 159 ? 2.088  -2.424  2.164   0.34 22.45 ?  159 ASN   A HA   1 
ATOM   3830 H HA   B ASN   A 1 159 ? 2.045  -2.872  1.286   0.66 21.78 ?  159 ASN   A HA   1 
ATOM   3831 H HB2  A ASN   A 1 159 ? 3.111  -0.385  0.512   0.34 24.12 ?  159 ASN   A HB2  1 
ATOM   3832 H HB2  B ASN   A 1 159 ? 3.238  -1.055  -0.523  0.66 25.47 ?  159 ASN   A HB2  1 
ATOM   3833 H HB3  A ASN   A 1 159 ? 2.104  -1.479  -0.049  0.34 24.12 ?  159 ASN   A HB3  1 
ATOM   3834 H HB3  B ASN   A 1 159 ? 2.059  -2.045  -0.917  0.66 25.47 ?  159 ASN   A HB3  1 
ATOM   3835 H HD21 A ASN   A 1 159 ? 0.528  1.624   1.038   0.34 26.74 ?  159 ASN   A HD21 1 
ATOM   3836 H HD21 B ASN   A 1 159 ? 1.109  1.397   0.022   0.66 31.11 ?  159 ASN   A HD21 1 
ATOM   3837 H HD22 A ASN   A 1 159 ? 1.793  1.414   0.286   0.34 26.74 ?  159 ASN   A HD22 1 
ATOM   3838 H HD22 B ASN   A 1 159 ? 2.346  0.946   -0.675  0.66 31.11 ?  159 ASN   A HD22 1 
ATOM   3839 N N    A LEU   A 1 160 ? 5.055  -2.733  1.016   0.34 17.42 ?  160 LEU   A N    1 
ATOM   3840 N N    B LEU   A 1 160 ? 5.072  -3.229  0.301   0.66 16.42 ?  160 LEU   A N    1 
ATOM   3841 C CA   A LEU   A 1 160 ? 5.979  -3.730  0.488   0.34 17.37 ?  160 LEU   A CA   1 
ATOM   3842 C CA   B LEU   A 1 160 ? 6.034  -4.223  -0.150  0.66 15.74 ?  160 LEU   A CA   1 
ATOM   3843 C C    A LEU   A 1 160 ? 6.186  -4.865  1.482   0.34 16.61 ?  160 LEU   A C    1 
ATOM   3844 C C    B LEU   A 1 160 ? 6.172  -5.348  0.866   0.66 15.34 ?  160 LEU   A C    1 
ATOM   3845 O O    A LEU   A 1 160 ? 6.267  -6.036  1.092   0.34 16.70 ?  160 LEU   A O    1 
ATOM   3846 O O    B LEU   A 1 160 ? 6.178  -6.528  0.502   0.66 15.99 ?  160 LEU   A O    1 
ATOM   3847 C CB   A LEU   A 1 160 ? 7.312  -3.073  0.140   0.34 18.25 ?  160 LEU   A CB   1 
ATOM   3848 C CB   B LEU   A 1 160 ? 7.386  -3.565  -0.392  0.66 16.19 ?  160 LEU   A CB   1 
ATOM   3849 C CG   A LEU   A 1 160 ? 8.402  -4.042  -0.312  0.34 19.01 ?  160 LEU   A CG   1 
ATOM   3850 C CG   B LEU   A 1 160 ? 8.479  -4.588  -0.687  0.66 16.88 ?  160 LEU   A CG   1 
ATOM   3851 C CD1  A LEU   A 1 160 ? 7.957  -4.779  -1.560  0.34 19.09 ?  160 LEU   A CD1  1 
ATOM   3852 C CD1  B LEU   A 1 160 ? 8.093  -5.407  -1.907  0.66 17.98 ?  160 LEU   A CD1  1 
ATOM   3853 C CD2  A LEU   A 1 160 ? 9.700  -3.302  -0.550  0.34 19.19 ?  160 LEU   A CD2  1 
ATOM   3854 C CD2  B LEU   A 1 160 ? 9.804  -3.894  -0.882  0.66 17.02 ?  160 LEU   A CD2  1 
ATOM   3855 H H    A LEU   A 1 160 ? 5.407  -1.971  1.194   0.34 21.06 ?  160 LEU   A H    1 
ATOM   3856 H H    B LEU   A 1 160 ? 5.399  -2.453  0.461   0.66 19.86 ?  160 LEU   A H    1 
ATOM   3857 H HA   A LEU   A 1 160 ? 5.607  -4.104  -0.325  0.34 21.00 ?  160 LEU   A HA   1 
ATOM   3858 H HA   B LEU   A 1 160 ? 5.722  -4.603  -0.983  0.66 19.04 ?  160 LEU   A HA   1 
ATOM   3859 H HB2  A LEU   A 1 160 ? 7.168  -2.430  -0.577  0.34 22.05 ?  160 LEU   A HB2  1 
ATOM   3860 H HB2  B LEU   A 1 160 ? 7.314  -2.963  -1.152  0.66 19.58 ?  160 LEU   A HB2  1 
ATOM   3861 H HB3  A LEU   A 1 160 ? 7.641  -2.617  0.927   0.34 22.05 ?  160 LEU   A HB3  1 
ATOM   3862 H HB3  B LEU   A 1 160 ? 7.641  -3.065  0.402   0.66 19.58 ?  160 LEU   A HB3  1 
ATOM   3863 H HG   A LEU   A 1 160 ? 8.559  -4.696  0.387   0.34 22.96 ?  160 LEU   A HG   1 
ATOM   3864 H HG   B LEU   A 1 160 ? 8.574  -5.188  0.069   0.66 20.41 ?  160 LEU   A HG   1 
ATOM   3865 H HD11 A LEU   A 1 160 ? 8.698  -5.308  -1.890  0.34 23.06 ?  160 LEU   A HD11 1 
ATOM   3866 H HD11 B LEU   A 1 160 ? 8.859  -5.919  -2.192  0.66 21.73 ?  160 LEU   A HD11 1 
ATOM   3867 H HD12 A LEU   A 1 160 ? 7.211  -5.358  -1.338  0.34 23.06 ?  160 LEU   A HD12 1 
ATOM   3868 H HD12 B LEU   A 1 160 ? 7.364  -6.007  -1.670  0.66 21.73 ?  160 LEU   A HD12 1 
ATOM   3869 H HD13 A LEU   A 1 160 ? 7.687  -4.130  -2.229  0.34 23.06 ?  160 LEU   A HD13 1 
ATOM   3870 H HD13 B LEU   A 1 160 ? 7.807  -4.806  -2.613  0.66 21.73 ?  160 LEU   A HD13 1 
ATOM   3871 H HD21 A LEU   A 1 160 ? 10.376 -3.937  -0.832  0.34 23.17 ?  160 LEU   A HD21 1 
ATOM   3872 H HD21 B LEU   A 1 160 ? 10.483 -4.561  -1.064  0.66 20.57 ?  160 LEU   A HD21 1 
ATOM   3873 H HD22 A LEU   A 1 160 ? 9.561  -2.636  -1.240  0.34 23.17 ?  160 LEU   A HD22 1 
ATOM   3874 H HD22 B LEU   A 1 160 ? 9.732  -3.280  -1.629  0.66 20.57 ?  160 LEU   A HD22 1 
ATOM   3875 H HD23 A LEU   A 1 160 ? 9.974  -2.871  0.276   0.34 23.17 ?  160 LEU   A HD23 1 
ATOM   3876 H HD23 B LEU   A 1 160 ? 10.029 -3.405  -0.073  0.66 20.57 ?  160 LEU   A HD23 1 
ATOM   3877 N N    A TYR   A 1 161 ? 6.273  -4.538  2.772   0.34 16.31 ?  161 TYR   A N    1 
ATOM   3878 N N    B TYR   A 1 161 ? 6.309  -5.000  2.146   0.66 15.16 ?  161 TYR   A N    1 
ATOM   3879 C CA   A TYR   A 1 161 ? 6.398  -5.576  3.787   0.34 16.12 ?  161 TYR   A CA   1 
ATOM   3880 C CA   B TYR   A 1 161 ? 6.392  -6.013  3.195   0.66 15.17 ?  161 TYR   A CA   1 
ATOM   3881 C C    A TYR   A 1 161 ? 5.242  -6.564  3.701   0.34 16.43 ?  161 TYR   A C    1 
ATOM   3882 C C    B TYR   A 1 161 ? 5.224  -6.988  3.115   0.66 15.81 ?  161 TYR   A C    1 
ATOM   3883 O O    A TYR   A 1 161 ? 5.448  -7.782  3.713   0.34 16.00 ?  161 TYR   A O    1 
ATOM   3884 O O    B TYR   A 1 161 ? 5.418  -8.207  3.143   0.66 15.82 ?  161 TYR   A O    1 
ATOM   3885 C CB   A TYR   A 1 161 ? 6.467  -4.953  5.181   0.34 16.30 ?  161 TYR   A CB   1 
ATOM   3886 C CB   B TYR   A 1 161 ? 6.454  -5.330  4.563   0.66 15.54 ?  161 TYR   A CB   1 
ATOM   3887 C CG   A TYR   A 1 161 ? 6.431  -6.001  6.266   0.34 16.54 ?  161 TYR   A CG   1 
ATOM   3888 C CG   B TYR   A 1 161 ? 6.344  -6.262  5.749   0.66 16.81 ?  161 TYR   A CG   1 
ATOM   3889 C CD1  A TYR   A 1 161 ? 7.592  -6.633  6.679   0.34 16.76 ?  161 TYR   A CD1  1 
ATOM   3890 C CD1  B TYR   A 1 161 ? 7.449  -6.960  6.220   0.66 17.80 ?  161 TYR   A CD1  1 
ATOM   3891 C CD2  A TYR   A 1 161 ? 5.230  -6.382  6.855   0.34 17.06 ?  161 TYR   A CD2  1 
ATOM   3892 C CD2  B TYR   A 1 161 ? 5.134  -6.426  6.419   0.66 18.11 ?  161 TYR   A CD2  1 
ATOM   3893 C CE1  A TYR   A 1 161 ? 7.566  -7.603  7.654   0.34 17.63 ?  161 TYR   A CE1  1 
ATOM   3894 C CE1  B TYR   A 1 161 ? 7.343  -7.814  7.309   0.66 18.60 ?  161 TYR   A CE1  1 
ATOM   3895 C CE2  A TYR   A 1 161 ? 5.195  -7.355  7.834   0.34 17.60 ?  161 TYR   A CE2  1 
ATOM   3896 C CE2  B TYR   A 1 161 ? 5.021  -7.271  7.511   0.66 19.09 ?  161 TYR   A CE2  1 
ATOM   3897 C CZ   A TYR   A 1 161 ? 6.369  -7.961  8.229   0.34 18.03 ?  161 TYR   A CZ   1 
ATOM   3898 C CZ   B TYR   A 1 161 ? 6.126  -7.961  7.950   0.66 19.74 ?  161 TYR   A CZ   1 
ATOM   3899 O OH   A TYR   A 1 161 ? 6.350  -8.932  9.203   0.34 18.62 ?  161 TYR   A OH   1 
ATOM   3900 O OH   B TYR   A 1 161 ? 6.011  -8.804  9.036   0.66 21.61 ?  161 TYR   A OH   1 
ATOM   3901 H H    A TYR   A 1 161 ? 6.257  -3.738  3.077   0.34 19.72 ?  161 TYR   A H    1 
ATOM   3902 H H    B TYR   A 1 161 ? 6.349  -4.197  2.436   0.66 18.34 ?  161 TYR   A H    1 
ATOM   3903 H HA   A TYR   A 1 161 ? 7.219  -6.068  3.640   0.34 19.49 ?  161 TYR   A HA   1 
ATOM   3904 H HA   B TYR   A 1 161 ? 7.202  -6.530  3.080   0.66 18.36 ?  161 TYR   A HA   1 
ATOM   3905 H HB2  A TYR   A 1 161 ? 7.296  -4.455  5.269   0.34 19.71 ?  161 TYR   A HB2  1 
ATOM   3906 H HB2  B TYR   A 1 161 ? 7.303  -4.873  4.636   0.66 18.80 ?  161 TYR   A HB2  1 
ATOM   3907 H HB3  A TYR   A 1 161 ? 5.709  -4.359  5.306   0.34 19.71 ?  161 TYR   A HB3  1 
ATOM   3908 H HB3  B TYR   A 1 161 ? 5.728  -4.696  4.626   0.66 18.80 ?  161 TYR   A HB3  1 
ATOM   3909 H HD1  A TYR   A 1 161 ? 8.402  -6.393  6.293   0.34 20.27 ?  161 TYR   A HD1  1 
ATOM   3910 H HD1  B TYR   A 1 161 ? 8.265  -6.876  5.790   0.66 21.51 ?  161 TYR   A HD1  1 
ATOM   3911 H HD2  A TYR   A 1 161 ? 4.437  -5.974  6.588   0.34 20.62 ?  161 TYR   A HD2  1 
ATOM   3912 H HD2  B TYR   A 1 161 ? 4.382  -5.965  6.128   0.66 21.88 ?  161 TYR   A HD2  1 
ATOM   3913 H HE1  A TYR   A 1 161 ? 8.356  -8.015  7.922   0.34 21.31 ?  161 TYR   A HE1  1 
ATOM   3914 H HE1  B TYR   A 1 161 ? 8.088  -8.284  7.614   0.66 22.47 ?  161 TYR   A HE1  1 
ATOM   3915 H HE2  A TYR   A 1 161 ? 4.385  -7.601  8.223   0.34 21.27 ?  161 TYR   A HE2  1 
ATOM   3916 H HE2  B TYR   A 1 161 ? 4.202  -7.371  7.950   0.66 23.06 ?  161 TYR   A HE2  1 
ATOM   3917 H HH   A TYR   A 1 161 ? 7.124  -9.218  9.339   0.34 22.50 ?  161 TYR   A HH   1 
ATOM   3918 H HH   B TYR   A 1 161 ? 5.239  -8.754  9.369   0.66 26.08 ?  161 TYR   A HH   1 
ATOM   3919 N N    A ASP   A 1 162 ? 4.011  -6.056  3.610   0.34 17.50 ?  162 ASP   A N    1 
ATOM   3920 N N    B ASP   A 1 162 ? 3.996  -6.466  3.001   0.66 16.27 ?  162 ASP   A N    1 
ATOM   3921 C CA   A ASP   A 1 162 ? 2.855  -6.945  3.556   0.34 18.40 ?  162 ASP   A CA   1 
ATOM   3922 C CA   B ASP   A 1 162 ? 2.824  -7.336  2.908   0.66 17.50 ?  162 ASP   A CA   1 
ATOM   3923 C C    A ASP   A 1 162 ? 2.880  -7.807  2.300   0.34 19.32 ?  162 ASP   A C    1 
ATOM   3924 C C    B ASP   A 1 162 ? 2.916  -8.252  1.694   0.66 17.79 ?  162 ASP   A C    1 
ATOM   3925 O O    A ASP   A 1 162 ? 2.468  -8.972  2.331   0.34 19.66 ?  162 ASP   A O    1 
ATOM   3926 O O    B ASP   A 1 162 ? 2.568  -9.437  1.766   0.66 18.37 ?  162 ASP   A O    1 
ATOM   3927 C CB   A ASP   A 1 162 ? 1.559  -6.138  3.634   0.34 18.54 ?  162 ASP   A CB   1 
ATOM   3928 C CB   B ASP   A 1 162 ? 1.544  -6.497  2.816   0.66 19.93 ?  162 ASP   A CB   1 
ATOM   3929 C CG   A ASP   A 1 162 ? 1.276  -5.610  5.026   0.34 18.83 ?  162 ASP   A CG   1 
ATOM   3930 C CG   B ASP   A 1 162 ? 1.309  -5.622  4.034   0.66 22.03 ?  162 ASP   A CG   1 
ATOM   3931 O OD1  A ASP   A 1 162 ? 1.944  -6.048  5.986   0.34 19.40 ?  162 ASP   A OD1  1 
ATOM   3932 O OD1  B ASP   A 1 162 ? 1.880  -5.902  5.104   0.66 22.69 ?  162 ASP   A OD1  1 
ATOM   3933 O OD2  A ASP   A 1 162 ? 0.375  -4.755  5.158   0.34 18.81 -1 162 ASP   A OD2  1 
ATOM   3934 O OD2  B ASP   A 1 162 ? 0.511  -4.661  3.924   0.66 23.33 -1 162 ASP   A OD2  1 
ATOM   3935 H H    A ASP   A 1 162 ? 3.824  -5.217  3.574   0.34 21.16 ?  162 ASP   A H    1 
ATOM   3936 H H    B ASP   A 1 162 ? 3.813  -5.630  2.974   0.66 19.68 ?  162 ASP   A H    1 
ATOM   3937 H HA   A ASP   A 1 162 ? 2.883  -7.540  4.319   0.34 22.23 ?  162 ASP   A HA   1 
ATOM   3938 H HA   B ASP   A 1 162 ? 2.758  -7.893  3.699   0.66 21.16 ?  162 ASP   A HA   1 
ATOM   3939 H HB2  A ASP   A 1 162 ? 1.619  -5.379  3.037   0.34 22.40 ?  162 ASP   A HB2  1 
ATOM   3940 H HB2  B ASP   A 1 162 ? 1.590  -5.923  2.038   0.66 24.06 ?  162 ASP   A HB2  1 
ATOM   3941 H HB3  A ASP   A 1 162 ? 0.815  -6.707  3.378   0.34 22.40 ?  162 ASP   A HB3  1 
ATOM   3942 H HB3  B ASP   A 1 162 ? 0.773  -7.086  2.748   0.66 24.06 ?  162 ASP   A HB3  1 
ATOM   3943 N N    A LYS   A 1 163 ? 3.360  -7.255  1.184   0.34 20.32 ?  163 LYS   A N    1 
ATOM   3944 N N    B LYS   A 1 163 ? 3.368  -7.708  0.565   0.66 18.35 ?  163 LYS   A N    1 
ATOM   3945 C CA   A LYS   A 1 163 ? 3.440  -8.038  -0.045  0.34 21.44 ?  163 LYS   A CA   1 
ATOM   3946 C CA   B LYS   A 1 163 ? 3.505  -8.485  -0.662  0.66 19.89 ?  163 LYS   A CA   1 
ATOM   3947 C C    A LYS   A 1 163 ? 4.539  -9.092  0.041   0.34 20.30 ?  163 LYS   A C    1 
ATOM   3948 C C    B LYS   A 1 163 ? 4.568  -9.567  -0.514  0.66 18.17 ?  163 LYS   A C    1 
ATOM   3949 O O    A LYS   A 1 163 ? 4.375  -10.209 -0.463  0.34 20.71 ?  163 LYS   A O    1 
ATOM   3950 O O    B LYS   A 1 163 ? 4.374  -10.709 -0.950  0.66 19.35 ?  163 LYS   A O    1 
ATOM   3951 C CB   A LYS   A 1 163 ? 3.656  -7.114  -1.245  0.34 23.86 ?  163 LYS   A CB   1 
ATOM   3952 C CB   B LYS   A 1 163 ? 3.877  -7.522  -1.786  0.66 23.87 ?  163 LYS   A CB   1 
ATOM   3953 C CG   A LYS   A 1 163 ? 3.667  -7.827  -2.589  0.34 26.13 ?  163 LYS   A CG   1 
ATOM   3954 C CG   B LYS   A 1 163 ? 4.082  -8.140  -3.145  0.66 28.11 ?  163 LYS   A CG   1 
ATOM   3955 C CD   A LYS   A 1 163 ? 4.085  -6.893  -3.713  0.34 28.13 ?  163 LYS   A CD   1 
ATOM   3956 C CD   B LYS   A 1 163 ? 4.918  -7.204  -4.001  0.66 31.77 ?  163 LYS   A CD   1 
ATOM   3957 C CE   A LYS   A 1 163 ? 4.023  -7.590  -5.062  0.34 29.96 ?  163 LYS   A CE   1 
ATOM   3958 C CE   B LYS   A 1 163 ? 4.348  -7.054  -5.396  0.66 34.44 ?  163 LYS   A CE   1 
ATOM   3959 N NZ   A LYS   A 1 163 ? 4.666  -6.786  -6.140  0.34 30.87 ?  163 LYS   A NZ   1 
ATOM   3960 N NZ   B LYS   A 1 163 ? 5.274  -6.303  -6.288  0.66 36.03 ?  163 LYS   A NZ   1 
ATOM   3961 H H    A LYS   A 1 163 ? 3.635  -6.444  1.112   0.34 24.54 ?  163 LYS   A H    1 
ATOM   3962 H H    B LYS   A 1 163 ? 3.605  -6.886  0.487   0.66 22.17 ?  163 LYS   A H    1 
ATOM   3963 H HA   A LYS   A 1 163 ? 2.599  -8.501  -0.179  0.34 25.88 ?  163 LYS   A HA   1 
ATOM   3964 H HA   B LYS   A 1 163 ? 2.660  -8.905  -0.883  0.66 24.02 ?  163 LYS   A HA   1 
ATOM   3965 H HB2  A LYS   A 1 163 ? 2.937  -6.459  -1.268  0.34 28.78 ?  163 LYS   A HB2  1 
ATOM   3966 H HB2  B LYS   A 1 163 ? 3.173  -6.861  -1.873  0.66 28.80 ?  163 LYS   A HB2  1 
ATOM   3967 H HB3  A LYS   A 1 163 ? 4.506  -6.661  -1.146  0.34 28.78 ?  163 LYS   A HB3  1 
ATOM   3968 H HB3  B LYS   A 1 163 ? 4.707  -7.079  -1.541  0.66 28.80 ?  163 LYS   A HB3  1 
ATOM   3969 H HG2  A LYS   A 1 163 ? 4.298  -8.563  -2.561  0.34 31.51 ?  163 LYS   A HG2  1 
ATOM   3970 H HG2  B LYS   A 1 163 ? 4.553  -8.984  -3.061  0.66 33.88 ?  163 LYS   A HG2  1 
ATOM   3971 H HG3  A LYS   A 1 163 ? 2.776  -8.157  -2.785  0.34 31.51 ?  163 LYS   A HG3  1 
ATOM   3972 H HG3  B LYS   A 1 163 ? 3.223  -8.270  -3.573  0.66 33.88 ?  163 LYS   A HG3  1 
ATOM   3973 H HD2  A LYS   A 1 163 ? 3.487  -6.131  -3.738  0.34 33.90 ?  163 LYS   A HD2  1 
ATOM   3974 H HD2  B LYS   A 1 163 ? 4.938  -6.326  -3.586  0.66 38.27 ?  163 LYS   A HD2  1 
ATOM   3975 H HD3  A LYS   A 1 163 ? 4.998  -6.599  -3.564  0.34 33.90 ?  163 LYS   A HD3  1 
ATOM   3976 H HD3  B LYS   A 1 163 ? 5.816  -7.560  -4.072  0.66 38.27 ?  163 LYS   A HD3  1 
ATOM   3977 H HE2  A LYS   A 1 163 ? 4.477  -8.445  -5.003  0.34 36.10 ?  163 LYS   A HE2  1 
ATOM   3978 H HE2  B LYS   A 1 163 ? 4.203  -7.933  -5.776  0.66 41.48 ?  163 LYS   A HE2  1 
ATOM   3979 H HE3  A LYS   A 1 163 ? 3.095  -7.726  -5.305  0.34 36.10 ?  163 LYS   A HE3  1 
ATOM   3980 H HE3  B LYS   A 1 163 ? 3.510  -6.567  -5.346  0.66 41.48 ?  163 LYS   A HE3  1 
ATOM   3981 H HZ1  A LYS   A 1 163 ? 4.614  -7.220  -6.915  0.34 37.20 ?  163 LYS   A HZ1  1 
ATOM   3982 H HZ1  B LYS   A 1 163 ? 4.895  -6.179  -7.083  0.66 43.39 ?  163 LYS   A HZ1  1 
ATOM   3983 H HZ2  A LYS   A 1 163 ? 4.253  -6.001  -6.219  0.34 37.20 ?  163 LYS   A HZ2  1 
ATOM   3984 H HZ2  B LYS   A 1 163 ? 5.464  -5.510  -5.931  0.66 43.39 ?  163 LYS   A HZ2  1 
ATOM   3985 H HZ3  A LYS   A 1 163 ? 5.523  -6.644  -5.944  0.34 37.20 ?  163 LYS   A HZ3  1 
ATOM   3986 H HZ3  B LYS   A 1 163 ? 6.029  -6.761  -6.394  0.66 43.39 ?  163 LYS   A HZ3  1 
ATOM   3987 N N    A LEU   A 1 164 ? 5.666  -8.761  0.677   0.34 18.76 ?  164 LEU   A N    1 
ATOM   3988 N N    B LEU   A 1 164 ? 5.710  -9.216  0.083   0.66 17.25 ?  164 LEU   A N    1 
ATOM   3989 C CA   A LEU   A 1 164 ? 6.745  -9.734  0.825   0.34 17.49 ?  164 LEU   A CA   1 
ATOM   3990 C CA   B LEU   A 1 164 ? 6.778  -10.190 0.279   0.66 16.34 ?  164 LEU   A CA   1 
ATOM   3991 C C    A LEU   A 1 164 ? 6.306  -10.909 1.689   0.34 17.18 ?  164 LEU   A C    1 
ATOM   3992 C C    B LEU   A 1 164 ? 6.312  -11.345 1.151   0.66 16.20 ?  164 LEU   A C    1 
ATOM   3993 O O    A LEU   A 1 164 ? 6.616  -12.067 1.386   0.34 16.67 ?  164 LEU   A O    1 
ATOM   3994 O O    B LEU   A 1 164 ? 6.601  -12.508 0.854   0.66 17.14 ?  164 LEU   A O    1 
ATOM   3995 C CB   A LEU   A 1 164 ? 7.971  -9.061  1.442   0.34 16.71 ?  164 LEU   A CB   1 
ATOM   3996 C CB   B LEU   A 1 164 ? 7.989  -9.519  0.920   0.66 15.91 ?  164 LEU   A CB   1 
ATOM   3997 C CG   A LEU   A 1 164 ? 8.750  -8.079  0.564   0.34 16.48 ?  164 LEU   A CG   1 
ATOM   3998 C CG   B LEU   A 1 164 ? 8.760  -8.517  0.063   0.66 16.27 ?  164 LEU   A CG   1 
ATOM   3999 C CD1  A LEU   A 1 164 ? 9.669  -7.220  1.417   0.34 16.29 ?  164 LEU   A CD1  1 
ATOM   4000 C CD1  B LEU   A 1 164 ? 9.761  -7.761  0.923   0.66 15.77 ?  164 LEU   A CD1  1 
ATOM   4001 C CD2  A LEU   A 1 164 ? 9.553  -8.822  -0.495  0.34 16.30 ?  164 LEU   A CD2  1 
ATOM   4002 C CD2  B LEU   A 1 164 ? 9.468  -9.220  -1.082  0.66 17.30 ?  164 LEU   A CD2  1 
ATOM   4003 H H    A LEU   A 1 164 ? 5.824  -7.993  1.029   0.34 22.66 ?  164 LEU   A H    1 
ATOM   4004 H H    B LEU   A 1 164 ? 5.891  -8.433  0.381   0.66 20.86 ?  164 LEU   A H    1 
ATOM   4005 H HA   A LEU   A 1 164 ? 6.995  -10.074 -0.049  0.34 21.14 ?  164 LEU   A HA   1 
ATOM   4006 H HA   B LEU   A 1 164 ? 7.041  -10.559 -0.575  0.66 19.75 ?  164 LEU   A HA   1 
ATOM   4007 H HB2  A LEU   A 1 164 ? 7.683  -8.570  2.226   0.34 20.20 ?  164 LEU   A HB2  1 
ATOM   4008 H HB2  B LEU   A 1 164 ? 7.688  -9.054  1.714   0.66 19.25 ?  164 LEU   A HB2  1 
ATOM   4009 H HB3  A LEU   A 1 164 ? 8.594  -9.754  1.709   0.34 20.20 ?  164 LEU   A HB3  1 
ATOM   4010 H HB3  B LEU   A 1 164 ? 8.614  -10.218 1.179   0.66 19.25 ?  164 LEU   A HB3  1 
ATOM   4011 H HG   A LEU   A 1 164 ? 8.125  -7.492  0.112   0.34 19.93 ?  164 LEU   A HG   1 
ATOM   4012 H HG   B LEU   A 1 164 ? 8.137  -7.875  -0.311  0.66 19.68 ?  164 LEU   A HG   1 
ATOM   4013 H HD11 A LEU   A 1 164 ? 10.163 -6.618  0.839   0.34 19.70 ?  164 LEU   A HD11 1 
ATOM   4014 H HD11 B LEU   A 1 164 ? 10.244 -7.132  0.367   0.66 19.07 ?  164 LEU   A HD11 1 
ATOM   4015 H HD12 A LEU   A 1 164 ? 9.132  -6.711  2.045   0.34 19.70 ?  164 LEU   A HD12 1 
ATOM   4016 H HD12 B LEU   A 1 164 ? 9.284  -7.288  1.624   0.66 19.07 ?  164 LEU   A HD12 1 
ATOM   4017 H HD13 A LEU   A 1 164 ? 10.283 -7.797  1.898   0.34 19.70 ?  164 LEU   A HD13 1 
ATOM   4018 H HD13 B LEU   A 1 164 ? 10.381 -8.396  1.319   0.66 19.07 ?  164 LEU   A HD13 1 
ATOM   4019 H HD21 A LEU   A 1 164 ? 10.052 -8.178  -1.023  0.34 19.71 ?  164 LEU   A HD21 1 
ATOM   4020 H HD21 B LEU   A 1 164 ? 10.003 -8.572  -1.564  0.66 20.92 ?  164 LEU   A HD21 1 
ATOM   4021 H HD22 A LEU   A 1 164 ? 10.165 -9.434  -0.056  0.34 19.71 ?  164 LEU   A HD22 1 
ATOM   4022 H HD22 B LEU   A 1 164 ? 10.035 -9.918  -0.720  0.66 20.92 ?  164 LEU   A HD22 1 
ATOM   4023 H HD23 A LEU   A 1 164 ? 8.944  -9.316  -1.065  0.34 19.71 ?  164 LEU   A HD23 1 
ATOM   4024 H HD23 B LEU   A 1 164 ? 8.802  -9.607  -1.673  0.66 20.92 ?  164 LEU   A HD23 1 
ATOM   4025 N N    A VAL   A 1 165 ? 5.589  -10.628 2.776   0.34 17.75 ?  165 VAL   A N    1 
ATOM   4026 N N    B VAL   A 1 165 ? 5.606  -11.042 2.242   0.66 16.26 ?  165 VAL   A N    1 
ATOM   4027 C CA   A VAL   A 1 165 ? 5.150  -11.686 3.681   0.34 18.70 ?  165 VAL   A CA   1 
ATOM   4028 C CA   B VAL   A 1 165 ? 5.133  -12.088 3.143   0.66 17.24 ?  165 VAL   A CA   1 
ATOM   4029 C C    A VAL   A 1 165 ? 4.097  -12.561 3.012   0.34 19.99 ?  165 VAL   A C    1 
ATOM   4030 C C    B VAL   A 1 165 ? 4.114  -12.975 2.440   0.66 17.58 ?  165 VAL   A C    1 
ATOM   4031 O O    A VAL   A 1 165 ? 4.161  -13.793 3.073   0.34 20.07 ?  165 VAL   A O    1 
ATOM   4032 O O    B VAL   A 1 165 ? 4.216  -14.208 2.452   0.66 18.06 ?  165 VAL   A O    1 
ATOM   4033 C CB   A VAL   A 1 165 ? 4.635  -11.074 4.996   0.34 18.70 ?  165 VAL   A CB   1 
ATOM   4034 C CB   B VAL   A 1 165 ? 4.554  -11.457 4.424   0.66 18.56 ?  165 VAL   A CB   1 
ATOM   4035 C CG1  A VAL   A 1 165 ? 3.872  -12.112 5.803   0.34 18.77 ?  165 VAL   A CG1  1 
ATOM   4036 C CG1  B VAL   A 1 165 ? 3.886  -12.518 5.284   0.66 19.19 ?  165 VAL   A CG1  1 
ATOM   4037 C CG2  A VAL   A 1 165 ? 5.794  -10.498 5.799   0.34 18.81 ?  165 VAL   A CG2  1 
ATOM   4038 C CG2  B VAL   A 1 165 ? 5.644  -10.748 5.209   0.66 19.08 ?  165 VAL   A CG2  1 
ATOM   4039 H H    A VAL   A 1 165 ? 5.349  -9.839  3.008   0.34 21.45 ?  165 VAL   A H    1 
ATOM   4040 H H    B VAL   A 1 165 ? 5.386  -10.248 2.483   0.66 19.66 ?  165 VAL   A H    1 
ATOM   4041 H HA   A VAL   A 1 165 ? 5.909  -12.251 3.893   0.34 22.59 ?  165 VAL   A HA   1 
ATOM   4042 H HA   B VAL   A 1 165 ? 5.879  -12.646 3.407   0.66 20.84 ?  165 VAL   A HA   1 
ATOM   4043 H HB   A VAL   A 1 165 ? 4.024  -10.352 4.787   0.34 22.59 ?  165 VAL   A HB   1 
ATOM   4044 H HB   B VAL   A 1 165 ? 3.878  -10.804 4.187   0.66 22.42 ?  165 VAL   A HB   1 
ATOM   4045 H HG11 A VAL   A 1 165 ? 3.804  -11.806 6.719   0.34 22.67 ?  165 VAL   A HG11 1 
ATOM   4046 H HG11 B VAL   A 1 165 ? 3.771  -12.172 6.184   0.66 23.18 ?  165 VAL   A HG11 1 
ATOM   4047 H HG12 A VAL   A 1 165 ? 2.983  -12.219 5.425   0.34 22.67 ?  165 VAL   A HG12 1 
ATOM   4048 H HG12 B VAL   A 1 165 ? 3.019  -12.739 4.906   0.66 23.18 ?  165 VAL   A HG12 1 
ATOM   4049 H HG13 A VAL   A 1 165 ? 4.351  -12.954 5.769   0.34 22.67 ?  165 VAL   A HG13 1 
ATOM   4050 H HG13 B VAL   A 1 165 ? 4.448  -13.309 5.307   0.66 23.18 ?  165 VAL   A HG13 1 
ATOM   4051 H HG21 A VAL   A 1 165 ? 5.450  -10.130 6.627   0.34 22.72 ?  165 VAL   A HG21 1 
ATOM   4052 H HG21 B VAL   A 1 165 ? 5.250  -10.328 5.991   0.66 23.04 ?  165 VAL   A HG21 1 
ATOM   4053 H HG22 A VAL   A 1 165 ? 6.430  -11.205 5.988   0.34 22.72 ?  165 VAL   A HG22 1 
ATOM   4054 H HG22 B VAL   A 1 165 ? 6.309  -11.398 5.483   0.66 23.04 ?  165 VAL   A HG22 1 
ATOM   4055 H HG23 A VAL   A 1 165 ? 6.221  -9.800  5.278   0.34 22.72 ?  165 VAL   A HG23 1 
ATOM   4056 H HG23 B VAL   A 1 165 ? 6.050  -10.075 4.642   0.66 23.04 ?  165 VAL   A HG23 1 
ATOM   4057 N N    A SER   A 1 166 ? 3.110  -11.937 2.366   0.34 21.53 ?  166 SER   A N    1 
ATOM   4058 N N    B SER   A 1 166 ? 3.117  -12.358 1.809   0.66 18.30 ?  166 SER   A N    1 
ATOM   4059 C CA   A SER   A 1 166 ? 2.014  -12.700 1.778   0.34 23.35 ?  166 SER   A CA   1 
ATOM   4060 C CA   B SER   A 1 166 ? 2.020  -13.114 1.216   0.66 20.68 ?  166 SER   A CA   1 
ATOM   4061 C C    A SER   A 1 166 ? 2.480  -13.563 0.612   0.34 24.17 ?  166 SER   A C    1 
ATOM   4062 C C    B SER   A 1 166 ? 2.449  -13.911 -0.004  0.66 21.88 ?  166 SER   A C    1 
ATOM   4063 O O    A SER   A 1 166 ? 1.913  -14.636 0.377   0.34 24.36 ?  166 SER   A O    1 
ATOM   4064 O O    B SER   A 1 166 ? 1.731  -14.831 -0.413  0.66 22.84 ?  166 SER   A O    1 
ATOM   4065 C CB   A SER   A 1 166 ? 0.900  -11.752 1.330   0.34 24.53 ?  166 SER   A CB   1 
ATOM   4066 C CB   B SER   A 1 166 ? 0.888  -12.163 0.829   0.66 22.92 ?  166 SER   A CB   1 
ATOM   4067 O OG   A SER   A 1 166 ? 0.428  -10.969 2.416   0.34 25.56 ?  166 SER   A OG   1 
ATOM   4068 O OG   B SER   A 1 166 ? 0.526  -11.353 1.931   0.66 25.90 ?  166 SER   A OG   1 
ATOM   4069 H H    A SER   A 1 166 ? 3.048  -11.088 2.263   0.34 25.99 ?  166 SER   A H    1 
ATOM   4070 H H    B SER   A 1 166 ? 3.045  -11.512 1.724   0.66 22.12 ?  166 SER   A H    1 
ATOM   4071 H HA   A SER   A 1 166 ? 1.645  -13.292 2.448   0.34 28.17 ?  166 SER   A HA   1 
ATOM   4072 H HA   B SER   A 1 166 ? 1.663  -13.737 1.869   0.66 24.97 ?  166 SER   A HA   1 
ATOM   4073 H HB2  A SER   A 1 166 ? 1.243  -11.160 0.644   0.34 29.58 ?  166 SER   A HB2  1 
ATOM   4074 H HB2  B SER   A 1 166 ? 1.178  -11.598 0.094   0.66 27.66 ?  166 SER   A HB2  1 
ATOM   4075 H HB3  A SER   A 1 166 ? 0.161  -12.275 0.976   0.34 29.58 ?  166 SER   A HB3  1 
ATOM   4076 H HB3  B SER   A 1 166 ? 0.108  -12.677 0.557   0.66 27.66 ?  166 SER   A HB3  1 
ATOM   4077 H HG   A SER   A 1 166 ? 1.056  -10.510 2.732   0.34 30.83 ?  166 SER   A HG   1 
ATOM   4078 H HG   B SER   A 1 166 ? 1.168  -10.853 2.150   0.66 31.23 ?  166 SER   A HG   1 
ATOM   4079 N N    A SER   A 1 167 ? 3.505  -13.128 -0.119  0.34 25.09 ?  167 SER   A N    1 
ATOM   4080 N N    B SER   A 1 167 ? 3.591  -13.578 -0.596  0.66 22.66 ?  167 SER   A N    1 
ATOM   4081 C CA   A SER   A 1 167 ? 3.974  -13.835 -1.303  0.34 26.28 ?  167 SER   A CA   1 
ATOM   4082 C CA   B SER   A 1 167 ? 4.104  -14.292 -1.753  0.66 24.70 ?  167 SER   A CA   1 
ATOM   4083 C C    A SER   A 1 167 ? 5.158  -14.753 -1.030  0.34 27.62 ?  167 SER   A C    1 
ATOM   4084 C C    B SER   A 1 167 ? 5.294  -15.171 -1.415  0.66 26.54 ?  167 SER   A C    1 
ATOM   4085 O O    A SER   A 1 167 ? 5.659  -15.384 -1.966  0.34 27.51 ?  167 SER   A O    1 
ATOM   4086 O O    B SER   A 1 167 ? 5.815  -15.850 -2.306  0.66 26.68 ?  167 SER   A O    1 
ATOM   4087 C CB   A SER   A 1 167 ? 4.344  -12.838 -2.408  0.34 26.29 ?  167 SER   A CB   1 
ATOM   4088 C CB   B SER   A 1 167 ? 4.492  -13.301 -2.857  0.66 25.05 ?  167 SER   A CB   1 
ATOM   4089 O OG   A SER   A 1 167 ? 5.408  -11.994 -2.001  0.34 26.40 ?  167 SER   A OG   1 
ATOM   4090 O OG   B SER   A 1 167 ? 5.567  -12.477 -2.445  0.66 25.24 ?  167 SER   A OG   1 
ATOM   4091 H H    A SER   A 1 167 ? 3.950  -12.414 0.056   0.34 30.26 ?  167 SER   A H    1 
ATOM   4092 H H    B SER   A 1 167 ? 4.092  -12.928 -0.337  0.66 27.35 ?  167 SER   A H    1 
ATOM   4093 H HA   A SER   A 1 167 ? 3.253  -14.384 -1.642  0.34 31.68 ?  167 SER   A HA   1 
ATOM   4094 H HA   B SER   A 1 167 ? 3.407  -14.865 -2.101  0.66 29.79 ?  167 SER   A HA   1 
ATOM   4095 H HB2  A SER   A 1 167 ? 4.618  -13.331 -3.200  0.34 31.70 ?  167 SER   A HB2  1 
ATOM   4096 H HB2  B SER   A 1 167 ? 4.757  -13.798 -3.646  0.66 30.21 ?  167 SER   A HB2  1 
ATOM   4097 H HB3  A SER   A 1 167 ? 3.568  -12.292 -2.615  0.34 31.70 ?  167 SER   A HB3  1 
ATOM   4098 H HB3  B SER   A 1 167 ? 3.726  -12.740 -3.061  0.66 30.21 ?  167 SER   A HB3  1 
ATOM   4099 H HG   A SER   A 1 167 ? 5.183  -11.556 -1.322  0.34 31.83 ?  167 SER   A HG   1 
ATOM   4100 H HG   B SER   A 1 167 ? 5.349  -12.045 -1.757  0.66 30.44 ?  167 SER   A HG   1 
ATOM   4101 N N    A PHE   A 1 168 ? 5.616  -14.852 0.216   0.34 29.29 ?  168 PHE   A N    1 
ATOM   4102 N N    B PHE   A 1 168 ? 5.733  -15.190 -0.159  0.66 28.34 ?  168 PHE   A N    1 
ATOM   4103 C CA   A PHE   A 1 168 ? 6.797  -15.655 0.504   0.34 31.33 ?  168 PHE   A CA   1 
ATOM   4104 C CA   B PHE   A 1 168 ? 6.931  -15.941 0.185   0.66 30.44 ?  168 PHE   A CA   1 
ATOM   4105 C C    A PHE   A 1 168 ? 6.468  -17.138 0.419   0.34 35.36 ?  168 PHE   A C    1 
ATOM   4106 C C    B PHE   A 1 168 ? 6.659  -17.433 0.069   0.66 35.96 ?  168 PHE   A C    1 
ATOM   4107 O O    A PHE   A 1 168 ? 5.503  -17.610 1.030   0.34 35.72 ?  168 PHE   A O    1 
ATOM   4108 O O    B PHE   A 1 168 ? 5.639  -17.931 0.552   0.66 36.42 ?  168 PHE   A O    1 
ATOM   4109 C CB   A PHE   A 1 168 ? 7.348  -15.330 1.890   0.34 29.48 ?  168 PHE   A CB   1 
ATOM   4110 C CB   B PHE   A 1 168 ? 7.401  -15.607 1.598   0.66 27.28 ?  168 PHE   A CB   1 
ATOM   4111 C CG   A PHE   A 1 168 ? 8.603  -16.087 2.224   0.34 27.88 ?  168 PHE   A CG   1 
ATOM   4112 C CG   B PHE   A 1 168 ? 8.676  -16.307 1.979   0.66 24.28 ?  168 PHE   A CG   1 
ATOM   4113 C CD1  A PHE   A 1 168 ? 9.803  -15.755 1.620   0.34 27.30 ?  168 PHE   A CD1  1 
ATOM   4114 C CD1  B PHE   A 1 168 ? 9.863  -15.993 1.340   0.66 23.27 ?  168 PHE   A CD1  1 
ATOM   4115 C CD2  A PHE   A 1 168 ? 8.582  -17.137 3.128   0.34 27.17 ?  168 PHE   A CD2  1 
ATOM   4116 C CD2  B PHE   A 1 168 ? 8.688  -17.289 2.958   0.66 22.74 ?  168 PHE   A CD2  1 
ATOM   4117 C CE1  A PHE   A 1 168 ? 10.960 -16.447 1.916   0.34 26.87 ?  168 PHE   A CE1  1 
ATOM   4118 C CE1  B PHE   A 1 168 ? 11.037 -16.636 1.672   0.66 22.19 ?  168 PHE   A CE1  1 
ATOM   4119 C CE2  A PHE   A 1 168 ? 9.741  -17.831 3.433   0.34 26.81 ?  168 PHE   A CE2  1 
ATOM   4120 C CE2  B PHE   A 1 168 ? 9.869  -17.935 3.299   0.66 21.87 ?  168 PHE   A CE2  1 
ATOM   4121 C CZ   A PHE   A 1 168 ? 10.929 -17.486 2.823   0.34 26.77 ?  168 PHE   A CZ   1 
ATOM   4122 C CZ   B PHE   A 1 168 ? 11.043 -17.606 2.654   0.66 21.89 ?  168 PHE   A CZ   1 
ATOM   4123 H H    A PHE   A 1 168 ? 5.266  -14.469 0.901   0.34 35.30 ?  168 PHE   A H    1 
ATOM   4124 H H    B PHE   A 1 168 ? 5.358  -14.788 0.505   0.66 34.15 ?  168 PHE   A H    1 
ATOM   4125 H HA   A PHE   A 1 168 ? 7.484  -15.459 -0.150  0.34 37.75 ?  168 PHE   A HA   1 
ATOM   4126 H HA   B PHE   A 1 168 ? 7.639  -15.714 -0.434  0.66 36.68 ?  168 PHE   A HA   1 
ATOM   4127 H HB2  A PHE   A 1 168 ? 7.550  -14.382 1.932   0.34 35.52 ?  168 PHE   A HB2  1 
ATOM   4128 H HB2  B PHE   A 1 168 ? 7.559  -14.652 1.661   0.66 32.89 ?  168 PHE   A HB2  1 
ATOM   4129 H HB3  A PHE   A 1 168 ? 6.678  -15.555 2.555   0.34 35.52 ?  168 PHE   A HB3  1 
ATOM   4130 H HB3  B PHE   A 1 168 ? 6.717  -15.871 2.233   0.66 32.89 ?  168 PHE   A HB3  1 
ATOM   4131 H HD1  A PHE   A 1 168 ? 9.830  -15.056 1.007   0.34 32.91 ?  168 PHE   A HD1  1 
ATOM   4132 H HD1  B PHE   A 1 168 ? 9.871  -15.340 0.679   0.66 28.08 ?  168 PHE   A HD1  1 
ATOM   4133 H HD2  A PHE   A 1 168 ? 7.784  -17.369 3.545   0.34 32.75 ?  168 PHE   A HD2  1 
ATOM   4134 H HD2  B PHE   A 1 168 ? 7.899  -17.515 3.395   0.66 27.44 ?  168 PHE   A HD2  1 
ATOM   4135 H HE1  A PHE   A 1 168 ? 11.760 -16.213 1.503   0.34 32.39 ?  168 PHE   A HE1  1 
ATOM   4136 H HE1  B PHE   A 1 168 ? 11.830 -16.412 1.238   0.66 26.78 ?  168 PHE   A HE1  1 
ATOM   4137 H HE2  A PHE   A 1 168 ? 9.717  -18.531 4.045   0.34 32.32 ?  168 PHE   A HE2  1 
ATOM   4138 H HE2  B PHE   A 1 168 ? 9.867  -18.594 3.959   0.66 26.39 ?  168 PHE   A HE2  1 
ATOM   4139 H HZ   A PHE   A 1 168 ? 11.709 -17.953 3.024   0.34 32.27 ?  168 PHE   A HZ   1 
ATOM   4140 H HZ   B PHE   A 1 168 ? 11.834 -18.041 2.879   0.66 26.42 ?  168 PHE   A HZ   1 
ATOM   4141 N N    A LEU   A 1 169 ? 7.281  -17.873 -0.331  0.34 38.89 ?  169 LEU   A N    1 
ATOM   4142 N N    B LEU   A 1 169 ? 7.567  -18.144 -0.586  0.66 40.72 ?  169 LEU   A N    1 
ATOM   4143 C CA   A LEU   A 1 169 ? 7.101  -19.309 -0.474  0.34 42.28 ?  169 LEU   A CA   1 
ATOM   4144 C CA   B LEU   A 1 169 ? 7.433  -19.584 -0.706  0.66 45.19 ?  169 LEU   A CA   1 
ATOM   4145 C C    A LEU   A 1 169 ? 8.007  -20.046 0.507   0.34 43.25 ?  169 LEU   A C    1 
ATOM   4146 C C    B LEU   A 1 169 ? 8.278  -20.280 0.356   0.66 46.70 ?  169 LEU   A C    1 
ATOM   4147 O O    A LEU   A 1 169 ? 7.548  -20.544 1.536   0.34 43.47 ?  169 LEU   A O    1 
ATOM   4148 O O    B LEU   A 1 169 ? 7.757  -20.769 1.359   0.66 47.11 ?  169 LEU   A O    1 
ATOM   4149 C CB   A LEU   A 1 169 ? 7.407  -19.740 -1.911  0.34 44.23 ?  169 LEU   A CB   1 
ATOM   4150 C CB   B LEU   A 1 169 ? 7.857  -20.043 -2.102  0.66 47.47 ?  169 LEU   A CB   1 
ATOM   4151 C CG   A LEU   A 1 169 ? 7.068  -21.184 -2.282  0.34 45.84 ?  169 LEU   A CG   1 
ATOM   4152 C CG   B LEU   A 1 169 ? 7.311  -21.402 -2.543  0.66 49.36 ?  169 LEU   A CG   1 
ATOM   4153 C CD1  A LEU   A 1 169 ? 5.624  -21.502 -1.927  0.34 46.40 ?  169 LEU   A CD1  1 
ATOM   4154 C CD1  B LEU   A 1 169 ? 5.827  -21.504 -2.229  0.66 50.01 ?  169 LEU   A CD1  1 
ATOM   4155 C CD2  A LEU   A 1 169 ? 7.321  -21.422 -3.763  0.34 46.34 ?  169 LEU   A CD2  1 
ATOM   4156 C CD2  B LEU   A 1 169 ? 7.555  -21.609 -4.028  0.66 49.92 ?  169 LEU   A CD2  1 
ATOM   4157 O OXT  A LEU   A 1 169 ? 9.217  -20.150 0.303   0.34 43.48 -1 169 LEU   A OXT  1 
ATOM   4158 O OXT  B LEU   A 1 169 ? 9.502  -20.360 0.243   0.66 47.03 -1 169 LEU   A OXT  1 
ATOM   4159 H H    A LEU   A 1 169 ? 7.949  -17.559 -0.772  0.34 46.82 ?  169 LEU   A H    1 
ATOM   4160 H H    B LEU   A 1 169 ? 8.256  -17.815 -0.978  0.66 49.01 ?  169 LEU   A H    1 
ATOM   4161 H HA   A LEU   A 1 169 ? 6.182  -19.536 -0.270  0.34 50.89 ?  169 LEU   A HA   1 
ATOM   4162 H HA   B LEU   A 1 169 ? 6.500  -19.810 -0.561  0.66 54.37 ?  169 LEU   A HA   1 
ATOM   4163 H HB2  A LEU   A 1 169 ? 6.908  -19.166 -2.512  0.34 53.23 ?  169 LEU   A HB2  1 
ATOM   4164 H HB2  B LEU   A 1 169 ? 7.559  -19.387 -2.750  0.66 57.12 ?  169 LEU   A HB2  1 
ATOM   4165 H HB3  A LEU   A 1 169 ? 8.357  -19.620 -2.068  0.34 53.23 ?  169 LEU   A HB3  1 
ATOM   4166 H HB3  B LEU   A 1 169 ? 8.826  -20.099 -2.121  0.66 57.12 ?  169 LEU   A HB3  1 
ATOM   4167 H HG   A LEU   A 1 169 ? 7.642  -21.785 -1.780  0.34 55.16 ?  169 LEU   A HG   1 
ATOM   4168 H HG   B LEU   A 1 169 ? 7.774  -22.105 -2.059  0.66 59.38 ?  169 LEU   A HG   1 
ATOM   4169 H HD11 A LEU   A 1 169 ? 5.371  -22.333 -2.356  0.34 55.83 ?  169 LEU   A HD11 1 
ATOM   4170 H HD11 B LEU   A 1 169 ? 5.432  -22.181 -2.792  0.66 60.17 ?  169 LEU   A HD11 1 
ATOM   4171 H HD12 A LEU   A 1 169 ? 5.547  -21.589 -0.964  0.34 55.83 ?  169 LEU   A HD12 1 
ATOM   4172 H HD12 B LEU   A 1 169 ? 5.718  -21.743 -1.293  0.66 60.17 ?  169 LEU   A HD12 1 
ATOM   4173 H HD13 A LEU   A 1 169 ? 5.057  -20.780 -2.242  0.34 55.83 ?  169 LEU   A HD13 1 
ATOM   4174 H HD13 B LEU   A 1 169 ? 5.411  -20.643 -2.401  0.66 60.17 ?  169 LEU   A HD13 1 
ATOM   4175 H HD21 A LEU   A 1 169 ? 7.106  -22.343 -3.976  0.34 55.76 ?  169 LEU   A HD21 1 
ATOM   4176 H HD21 B LEU   A 1 169 ? 7.218  -22.482 -4.283  0.66 60.06 ?  169 LEU   A HD21 1 
ATOM   4177 H HD22 A LEU   A 1 169 ? 6.759  -20.823 -4.279  0.34 55.76 ?  169 LEU   A HD22 1 
ATOM   4178 H HD22 B LEU   A 1 169 ? 7.088  -20.917 -4.523  0.66 60.06 ?  169 LEU   A HD22 1 
ATOM   4179 H HD23 A LEU   A 1 169 ? 8.255  -21.247 -3.956  0.34 55.76 ?  169 LEU   A HD23 1 
ATOM   4180 H HD23 B LEU   A 1 169 ? 8.507  -21.557 -4.203  0.66 60.06 ?  169 LEU   A HD23 1 
ATOM   4181 N N    A SER   B 1 1   ? 50.875 -9.214  -23.656 0.34 28.10 ?  1   SER   B N    1 
ATOM   4182 N N    B SER   B 1 1   ? 50.949 -9.340  -23.702 0.66 27.32 ?  1   SER   B N    1 
ATOM   4183 C CA   A SER   B 1 1   ? 51.430 -10.302 -22.823 0.34 27.97 ?  1   SER   B CA   1 
ATOM   4184 C CA   B SER   B 1 1   ? 51.409 -10.324 -22.701 0.66 27.37 ?  1   SER   B CA   1 
ATOM   4185 C C    A SER   B 1 1   ? 50.380 -11.376 -22.585 0.34 27.02 ?  1   SER   B C    1 
ATOM   4186 C C    B SER   B 1 1   ? 50.361 -11.405 -22.479 0.66 25.95 ?  1   SER   B C    1 
ATOM   4187 O O    A SER   B 1 1   ? 49.195 -11.188 -22.876 0.34 26.70 ?  1   SER   B O    1 
ATOM   4188 O O    B SER   B 1 1   ? 49.156 -11.205 -22.699 0.66 25.79 ?  1   SER   B O    1 
ATOM   4189 C CB   A SER   B 1 1   ? 51.930 -9.755  -21.488 0.34 28.49 ?  1   SER   B CB   1 
ATOM   4190 C CB   B SER   B 1 1   ? 51.731 -9.640  -21.376 0.66 28.44 ?  1   SER   B CB   1 
ATOM   4191 O OG   A SER   B 1 1   ? 50.849 -9.421  -20.639 0.34 29.51 ?  1   SER   B OG   1 
ATOM   4192 O OG   B SER   B 1 1   ? 50.560 -9.465  -20.600 0.66 30.31 ?  1   SER   B OG   1 
ATOM   4193 H H1   A SER   B 1 1   ? 50.688 -9.535  -24.463 0.34 33.87 ?  1   SER   B H1   1 
ATOM   4194 H H1   B SER   B 1 1   ? 51.658 -8.987  -24.105 0.66 32.93 ?  1   SER   B H1   1 
ATOM   4195 H H2   A SER   B 1 1   ? 50.138 -8.905  -23.274 0.34 33.87 ?  1   SER   B H2   1 
ATOM   4196 H H2   B SER   B 1 1   ? 50.437 -9.751  -24.299 0.66 32.93 ?  1   SER   B H2   1 
ATOM   4197 H H3   A SER   B 1 1   ? 51.479 -8.567  -23.721 0.34 33.87 ?  1   SER   B H3   1 
ATOM   4198 H H3   B SER   B 1 1   ? 50.488 -8.705  -23.290 0.66 32.93 ?  1   SER   B H3   1 
ATOM   4199 H HA   A SER   B 1 1   ? 52.175 -10.697 -23.294 0.34 33.72 ?  1   SER   B HA   1 
ATOM   4200 H HA   B SER   B 1 1   ? 52.216 -10.741 -23.036 0.66 32.99 ?  1   SER   B HA   1 
ATOM   4201 H HB2  A SER   B 1 1   ? 52.473 -10.434 -21.062 0.34 34.34 ?  1   SER   B HB2  1 
ATOM   4202 H HB2  B SER   B 1 1   ? 52.359 -10.194 -20.888 0.66 34.29 ?  1   SER   B HB2  1 
ATOM   4203 H HB3  A SER   B 1 1   ? 52.458 -8.959  -21.652 0.34 34.34 ?  1   SER   B HB3  1 
ATOM   4204 H HB3  B SER   B 1 1   ? 52.122 -8.771  -21.555 0.66 34.29 ?  1   SER   B HB3  1 
ATOM   4205 H HG   A SER   B 1 1   ? 51.139 -9.054  -19.941 0.34 35.56 ?  1   SER   B HG   1 
ATOM   4206 H HG   B SER   B 1 1   ? 50.737 -9.003  -19.921 0.66 36.52 ?  1   SER   B HG   1 
ATOM   4207 N N    A MET   B 1 2   ? 50.827 -12.505 -22.047 0.34 26.31 ?  2   MET   B N    1 
ATOM   4208 N N    B MET   B 1 2   ? 50.839 -12.561 -22.037 0.66 24.72 ?  2   MET   B N    1 
ATOM   4209 C CA   A MET   B 1 2   ? 49.996 -13.686 -21.873 0.34 25.93 ?  2   MET   B CA   1 
ATOM   4210 C CA   B MET   B 1 2   ? 50.010 -13.741 -21.850 0.66 24.41 ?  2   MET   B CA   1 
ATOM   4211 C C    A MET   B 1 2   ? 49.741 -13.893 -20.387 0.34 23.67 ?  2   MET   B C    1 
ATOM   4212 C C    B MET   B 1 2   ? 49.738 -13.903 -20.365 0.66 23.05 ?  2   MET   B C    1 
ATOM   4213 O O    A MET   B 1 2   ? 50.676 -14.147 -19.622 0.34 23.94 ?  2   MET   B O    1 
ATOM   4214 O O    B MET   B 1 2   ? 50.660 -14.135 -19.580 0.66 23.54 ?  2   MET   B O    1 
ATOM   4215 C CB   A MET   B 1 2   ? 50.693 -14.900 -22.482 0.34 28.46 ?  2   MET   B CB   1 
ATOM   4216 C CB   B MET   B 1 2   ? 50.744 -14.953 -22.394 0.66 27.07 ?  2   MET   B CB   1 
ATOM   4217 C CG   A MET   B 1 2   ? 49.823 -16.140 -22.589 0.34 30.89 ?  2   MET   B CG   1 
ATOM   4218 C CG   B MET   B 1 2   ? 49.856 -16.135 -22.766 0.66 29.31 ?  2   MET   B CG   1 
ATOM   4219 S SD   A MET   B 1 2   ? 50.624 -17.438 -23.546 0.34 33.32 ?  2   MET   B SD   1 
ATOM   4220 S SD   B MET   B 1 2   ? 50.713 -17.216 -23.915 0.66 31.51 ?  2   MET   B SD   1 
ATOM   4221 C CE   A MET   B 1 2   ? 51.204 -16.468 -24.937 0.34 33.61 ?  2   MET   B CE   1 
ATOM   4222 C CE   B MET   B 1 2   ? 51.644 -16.007 -24.822 0.66 32.23 ?  2   MET   B CE   1 
ATOM   4223 H H    A MET   B 1 2   ? 51.635 -12.615 -21.771 0.34 31.73 ?  2   MET   B H    1 
ATOM   4224 H H    B MET   B 1 2   ? 51.669 -12.701 -21.845 0.66 29.82 ?  2   MET   B H    1 
ATOM   4225 H HA   A MET   B 1 2   ? 49.154 -13.568 -22.336 0.34 31.27 ?  2   MET   B HA   1 
ATOM   4226 H HA   B MET   B 1 2   ? 49.182 -13.655 -22.343 0.66 29.45 ?  2   MET   B HA   1 
ATOM   4227 H HB2  A MET   B 1 2   ? 50.981 -14.639 -23.371 0.34 34.30 ?  2   MET   B HB2  1 
ATOM   4228 H HB2  B MET   B 1 2   ? 51.213 -14.598 -23.153 0.66 32.64 ?  2   MET   B HB2  1 
ATOM   4229 H HB3  A MET   B 1 2   ? 51.465 -15.136 -21.949 0.34 34.30 ?  2   MET   B HB3  1 
ATOM   4230 H HB3  B MET   B 1 2   ? 51.380 -15.290 -21.755 0.66 32.64 ?  2   MET   B HB3  1 
ATOM   4231 H HG2  A MET   B 1 2   ? 49.645 -16.482 -21.697 0.34 37.22 ?  2   MET   B HG2  1 
ATOM   4232 H HG2  B MET   B 1 2   ? 49.637 -16.650 -21.963 0.66 35.32 ?  2   MET   B HG2  1 
ATOM   4233 H HG3  A MET   B 1 2   ? 48.992 -15.913 -23.034 0.34 37.22 ?  2   MET   B HG3  1 
ATOM   4234 H HG3  B MET   B 1 2   ? 49.045 -15.830 -23.197 0.66 35.32 ?  2   MET   B HG3  1 
ATOM   4235 H HE1  A MET   B 1 2   ? 51.367 -17.056 -25.679 0.34 40.49 ?  2   MET   B HE1  1 
ATOM   4236 H HE1  B MET   B 1 2   ? 51.898 -16.432 -25.616 0.66 38.83 ?  2   MET   B HE1  1 
ATOM   4237 H HE2  A MET   B 1 2   ? 50.520 -15.816 -25.168 0.34 40.49 ?  2   MET   B HE2  1 
ATOM   4238 H HE2  B MET   B 1 2   ? 51.074 -15.240 -25.026 0.66 38.83 ?  2   MET   B HE2  1 
ATOM   4239 H HE3  A MET   B 1 2   ? 52.025 -16.005 -24.690 0.34 40.49 ?  2   MET   B HE3  1 
ATOM   4240 H HE3  B MET   B 1 2   ? 52.435 -15.729 -24.312 0.66 38.83 ?  2   MET   B HE3  1 
ATOM   4241 N N    . VAL   B 1 3   ? 48.476 -13.771 -19.983 1.00 21.20 ?  3   VAL   B N    1 
ATOM   4242 C CA   . VAL   B 1 3   ? 48.054 -13.988 -18.607 1.00 20.07 ?  3   VAL   B CA   1 
ATOM   4243 C C    . VAL   B 1 3   ? 46.816 -14.871 -18.616 1.00 18.23 ?  3   VAL   B C    1 
ATOM   4244 O O    . VAL   B 1 3   ? 46.085 -14.949 -19.607 1.00 18.67 ?  3   VAL   B O    1 
ATOM   4245 C CB   . VAL   B 1 3   ? 47.767 -12.668 -17.859 1.00 21.65 ?  3   VAL   B CB   1 
ATOM   4246 C CG1  . VAL   B 1 3   ? 49.026 -11.805 -17.765 1.00 22.38 ?  3   VAL   B CG1  1 
ATOM   4247 C CG2  . VAL   B 1 3   ? 46.625 -11.917 -18.535 1.00 22.22 ?  3   VAL   B CG2  1 
ATOM   4248 H H    A VAL   B 1 3   ? 47.831 -13.571 -20.515 0.34 25.60 ?  3   VAL   B H    1 
ATOM   4249 H H    B VAL   B 1 3   ? 47.837 -13.558 -20.517 0.66 25.60 ?  3   VAL   B H    1 
ATOM   4250 H HA   . VAL   B 1 3   ? 48.761 -14.460 -18.133 1.00 24.23 ?  3   VAL   B HA   1 
ATOM   4251 H HB   . VAL   B 1 3   ? 47.486 -12.889 -16.957 1.00 26.13 ?  3   VAL   B HB   1 
ATOM   4252 H HG11 . VAL   B 1 3   ? 48.809 -10.993 -17.282 1.00 27.01 ?  3   VAL   B HG11 1 
ATOM   4253 H HG12 . VAL   B 1 3   ? 49.712 -12.300 -17.290 1.00 27.01 ?  3   VAL   B HG12 1 
ATOM   4254 H HG13 . VAL   B 1 3   ? 49.328 -11.592 -18.660 1.00 27.01 ?  3   VAL   B HG13 1 
ATOM   4255 H HG21 . VAL   B 1 3   ? 46.565 -11.033 -18.154 1.00 26.82 ?  3   VAL   B HG21 1 
ATOM   4256 H HG22 . VAL   B 1 3   ? 46.802 -11.863 -19.486 1.00 26.82 ?  3   VAL   B HG22 1 
ATOM   4257 H HG23 . VAL   B 1 3   ? 45.793 -12.402 -18.384 1.00 26.82 ?  3   VAL   B HG23 1 
ATOM   4258 N N    . ASN   B 1 4   ? 46.589 -15.543 -17.489 1.00 16.11 ?  4   ASN   B N    1 
ATOM   4259 C CA   . ASN   B 1 4   ? 45.450 -16.445 -17.353 1.00 15.19 ?  4   ASN   B CA   1 
ATOM   4260 C C    . ASN   B 1 4   ? 45.383 -17.417 -18.529 1.00 15.24 ?  4   ASN   B C    1 
ATOM   4261 O O    . ASN   B 1 4   ? 44.323 -17.646 -19.110 1.00 16.13 ?  4   ASN   B O    1 
ATOM   4262 C CB   . ASN   B 1 4   ? 44.143 -15.663 -17.204 1.00 14.63 ?  4   ASN   B CB   1 
ATOM   4263 C CG   . ASN   B 1 4   ? 44.081 -14.866 -15.908 1.00 14.15 ?  4   ASN   B CG   1 
ATOM   4264 O OD1  . ASN   B 1 4   ? 44.367 -15.384 -14.833 1.00 13.85 ?  4   ASN   B OD1  1 
ATOM   4265 N ND2  . ASN   B 1 4   ? 43.727 -13.588 -16.014 1.00 14.89 ?  4   ASN   B ND2  1 
ATOM   4266 H H    . ASN   B 1 4   ? 47.087 -15.499 -16.793 1.00 19.49 ?  4   ASN   B H    1 
ATOM   4267 H HA   . ASN   B 1 4   ? 45.574 -16.972 -16.548 1.00 18.38 ?  4   ASN   B HA   1 
ATOM   4268 H HB2  . ASN   B 1 4   ? 44.065 -15.044 -17.949 1.00 17.70 ?  4   ASN   B HB2  1 
ATOM   4269 H HB3  . ASN   B 1 4   ? 43.402 -16.289 -17.217 1.00 17.70 ?  4   ASN   B HB3  1 
ATOM   4270 H HD21 . ASN   B 1 4   ? 43.675 -13.096 -15.310 1.00 18.02 ?  4   ASN   B HD21 1 
ATOM   4271 H HD22 . ASN   B 1 4   ? 43.534 -13.254 -16.785 1.00 18.02 ?  4   ASN   B HD22 1 
ATOM   4272 N N    . SER   B 1 5   ? 46.536 -17.982 -18.900 1.00 15.97 ?  5   SER   B N    1 
ATOM   4273 C CA   . SER   B 1 5   ? 46.629 -18.901 -20.034 1.00 18.22 ?  5   SER   B CA   1 
ATOM   4274 C C    . SER   B 1 5   ? 46.606 -20.317 -19.475 1.00 19.70 ?  5   SER   B C    1 
ATOM   4275 O O    . SER   B 1 5   ? 47.629 -20.984 -19.348 1.00 21.83 ?  5   SER   B O    1 
ATOM   4276 C CB   . SER   B 1 5   ? 47.894 -18.630 -20.847 1.00 20.51 ?  5   SER   B CB   1 
ATOM   4277 O OG   . SER   B 1 5   ? 49.062 -18.808 -20.062 1.00 23.56 ?  5   SER   B OG   1 
ATOM   4278 H H    . SER   B 1 5   ? 47.290 -17.852 -18.506 1.00 19.32 ?  5   SER   B H    1 
ATOM   4279 H HA   . SER   B 1 5   ? 45.858 -18.793 -20.610 1.00 22.02 ?  5   SER   B HA   1 
ATOM   4280 H HB2  . SER   B 1 5   ? 47.918 -19.244 -21.602 1.00 24.76 ?  5   SER   B HB2  1 
ATOM   4281 H HB3  . SER   B 1 5   ? 47.855 -17.717 -21.169 1.00 24.76 ?  5   SER   B HB3  1 
ATOM   4282 H HG   . SER   B 1 5   ? 49.105 -19.605 -19.801 1.00 28.43 ?  5   SER   B HG   1 
ATOM   4283 N N    . PHE   B 1 6   ? 45.409 -20.756 -19.100 1.00 20.67 ?  6   PHE   B N    1 
ATOM   4284 C CA   . PHE   B 1 6   ? 45.208 -22.095 -18.569 1.00 20.59 ?  6   PHE   B CA   1 
ATOM   4285 C C    . PHE   B 1 6   ? 45.110 -23.077 -19.726 1.00 24.64 ?  6   PHE   B C    1 
ATOM   4286 O O    . PHE   B 1 6   ? 44.396 -22.828 -20.702 1.00 27.04 ?  6   PHE   B O    1 
ATOM   4287 C CB   . PHE   B 1 6   ? 43.925 -22.141 -17.739 1.00 18.67 ?  6   PHE   B CB   1 
ATOM   4288 C CG   . PHE   B 1 6   ? 43.955 -21.267 -16.514 1.00 17.18 ?  6   PHE   B CG   1 
ATOM   4289 C CD1  . PHE   B 1 6   ? 44.455 -21.746 -15.322 1.00 15.93 ?  6   PHE   B CD1  1 
ATOM   4290 C CD2  . PHE   B 1 6   ? 43.475 -19.968 -16.559 1.00 16.49 ?  6   PHE   B CD2  1 
ATOM   4291 C CE1  . PHE   B 1 6   ? 44.474 -20.947 -14.191 1.00 15.58 ?  6   PHE   B CE1  1 
ATOM   4292 C CE2  . PHE   B 1 6   ? 43.498 -19.161 -15.436 1.00 16.70 ?  6   PHE   B CE2  1 
ATOM   4293 C CZ   . PHE   B 1 6   ? 44.000 -19.647 -14.252 1.00 15.74 ?  6   PHE   B CZ   1 
ATOM   4294 H H    . PHE   B 1 6   ? 44.685 -20.297 -19.151 1.00 24.96 ?  6   PHE   B H    1 
ATOM   4295 H HA   . PHE   B 1 6   ? 45.951 -22.351 -18.004 1.00 24.86 ?  6   PHE   B HA   1 
ATOM   4296 H HB2  . PHE   B 1 6   ? 43.181 -21.849 -18.290 1.00 22.56 ?  6   PHE   B HB2  1 
ATOM   4297 H HB3  . PHE   B 1 6   ? 43.768 -23.055 -17.443 1.00 22.56 ?  6   PHE   B HB3  1 
ATOM   4298 H HD1  . PHE   B 1 6   ? 44.780 -22.619 -15.275 1.00 19.27 ?  6   PHE   B HD1  1 
ATOM   4299 H HD2  . PHE   B 1 6   ? 43.130 -19.637 -17.355 1.00 19.94 ?  6   PHE   B HD2  1 
ATOM   4300 H HE1  . PHE   B 1 6   ? 44.819 -21.280 -13.392 1.00 18.85 ?  6   PHE   B HE1  1 
ATOM   4301 H HE2  . PHE   B 1 6   ? 43.166 -18.295 -15.482 1.00 20.20 ?  6   PHE   B HE2  1 
ATOM   4302 H HZ   . PHE   B 1 6   ? 44.013 -19.116 -13.491 1.00 19.04 ?  6   PHE   B HZ   1 
ATOM   4303 N N    . SER   B 1 7   ? 45.844 -24.183 -19.624 1.00 26.18 ?  7   SER   B N    1 
ATOM   4304 C CA   . SER   B 1 7   ? 45.905 -25.167 -20.693 1.00 29.36 ?  7   SER   B CA   1 
ATOM   4305 C C    . SER   B 1 7   ? 45.814 -26.569 -20.113 1.00 28.34 ?  7   SER   B C    1 
ATOM   4306 O O    . SER   B 1 7   ? 46.425 -26.869 -19.083 1.00 29.27 ?  7   SER   B O    1 
ATOM   4307 C CB   . SER   B 1 7   ? 47.204 -25.023 -21.498 1.00 32.71 ?  7   SER   B CB   1 
ATOM   4308 O OG   . SER   B 1 7   ? 47.226 -25.925 -22.592 1.00 34.73 ?  7   SER   B OG   1 
ATOM   4309 H H    . SER   B 1 7   ? 46.332 -24.379 -18.941 1.00 31.57 ?  7   SER   B H    1 
ATOM   4310 H HA   . SER   B 1 7   ? 45.160 -25.039 -21.296 1.00 35.38 ?  7   SER   B HA   1 
ATOM   4311 H HB2  . SER   B 1 7   ? 47.269 -24.113 -21.836 1.00 39.40 ?  7   SER   B HB2  1 
ATOM   4312 H HB3  . SER   B 1 7   ? 47.960 -25.214 -20.921 1.00 39.40 ?  7   SER   B HB3  1 
ATOM   4313 H HG   . SER   B 1 7   ? 47.938 -25.831 -23.029 1.00 41.83 ?  7   SER   B HG   1 
ATOM   4314 N N    . GLY   B 1 8   ? 45.045 -27.422 -20.782 1.00 27.79 ?  8   GLY   B N    1 
ATOM   4315 C CA   . GLY   B 1 8   ? 44.974 -28.815 -20.411 1.00 26.71 ?  8   GLY   B CA   1 
ATOM   4316 C C    . GLY   B 1 8   ? 44.053 -29.128 -19.264 1.00 24.95 ?  8   GLY   B C    1 
ATOM   4317 O O    . GLY   B 1 8   ? 44.203 -30.188 -18.643 1.00 26.61 ?  8   GLY   B O    1 
ATOM   4318 H H    . GLY   B 1 8   ? 44.561 -27.208 -21.455 1.00 33.50 ?  8   GLY   B H    1 
ATOM   4319 H HA2  . GLY   B 1 8   ? 44.669 -29.327 -21.172 1.00 32.20 ?  8   GLY   B HA2  1 
ATOM   4320 H HA3  . GLY   B 1 8   ? 45.856 -29.126 -20.166 1.00 32.20 ?  8   GLY   B HA3  1 
ATOM   4321 N N    . TYR   B 1 9   ? 43.076 -28.269 -18.982 1.00 22.66 ?  9   TYR   B N    1 
ATOM   4322 C CA   . TYR   B 1 9   ? 42.131 -28.535 -17.911 1.00 20.51 ?  9   TYR   B CA   1 
ATOM   4323 C C    . TYR   B 1 9   ? 40.943 -29.325 -18.425 1.00 19.89 ?  9   TYR   B C    1 
ATOM   4324 O O    . TYR   B 1 9   ? 40.523 -29.192 -19.579 1.00 21.69 ?  9   TYR   B O    1 
ATOM   4325 C CB   . TYR   B 1 9   ? 41.635 -27.247 -17.254 1.00 19.89 ?  9   TYR   B CB   1 
ATOM   4326 C CG   . TYR   B 1 9   ? 42.674 -26.626 -16.356 1.00 19.15 ?  9   TYR   B CG   1 
ATOM   4327 C CD1  . TYR   B 1 9   ? 43.744 -25.931 -16.892 1.00 19.54 ?  9   TYR   B CD1  1 
ATOM   4328 C CD2  . TYR   B 1 9   ? 42.598 -26.753 -14.976 1.00 18.36 ?  9   TYR   B CD2  1 
ATOM   4329 C CE1  . TYR   B 1 9   ? 44.713 -25.377 -16.081 1.00 19.58 ?  9   TYR   B CE1  1 
ATOM   4330 C CE2  . TYR   B 1 9   ? 43.567 -26.202 -14.154 1.00 18.59 ?  9   TYR   B CE2  1 
ATOM   4331 C CZ   . TYR   B 1 9   ? 44.622 -25.508 -14.712 1.00 19.37 ?  9   TYR   B CZ   1 
ATOM   4332 O OH   . TYR   B 1 9   ? 45.585 -24.958 -13.900 1.00 20.36 ?  9   TYR   B OH   1 
ATOM   4333 H H    . TYR   B 1 9   ? 42.909 -27.542 -19.415 1.00 27.34 ?  9   TYR   B H    1 
ATOM   4334 H HA   . TYR   B 1 9   ? 42.556 -29.070 -17.229 1.00 24.76 ?  9   TYR   B HA   1 
ATOM   4335 H HB2  . TYR   B 1 9   ? 41.390 -26.601 -17.937 1.00 24.02 ?  9   TYR   B HB2  1 
ATOM   4336 H HB3  . TYR   B 1 9   ? 40.862 -27.463 -16.709 1.00 24.02 ?  9   TYR   B HB3  1 
ATOM   4337 H HD1  . TYR   B 1 9   ? 43.805 -25.840 -17.817 1.00 23.60 ?  9   TYR   B HD1  1 
ATOM   4338 H HD2  . TYR   B 1 9   ? 41.884 -27.230 -14.599 1.00 22.18 ?  9   TYR   B HD2  1 
ATOM   4339 H HE1  . TYR   B 1 9   ? 45.418 -24.909 -16.459 1.00 23.65 ?  9   TYR   B HE1  1 
ATOM   4340 H HE2  . TYR   B 1 9   ? 43.498 -26.298 -13.233 1.00 22.46 ?  9   TYR   B HE2  1 
ATOM   4341 H HH   . TYR   B 1 9   ? 46.153 -24.571 -14.373 1.00 24.58 ?  9   TYR   B HH   1 
ATOM   4342 N N    . LEU   B 1 10  ? 40.419 -30.170 -17.546 1.00 18.07 ?  10  LEU   B N    1 
ATOM   4343 C CA   . LEU   B 1 10  ? 39.214 -30.935 -17.807 1.00 17.78 ?  10  LEU   B CA   1 
ATOM   4344 C C    . LEU   B 1 10  ? 38.032 -30.170 -17.233 1.00 17.79 ?  10  LEU   B C    1 
ATOM   4345 O O    . LEU   B 1 10  ? 38.062 -29.756 -16.070 1.00 17.57 ?  10  LEU   B O    1 
ATOM   4346 C CB   . LEU   B 1 10  ? 39.323 -32.298 -17.123 1.00 18.98 ?  10  LEU   B CB   1 
ATOM   4347 C CG   . LEU   B 1 10  ? 38.216 -33.295 -17.445 1.00 20.53 ?  10  LEU   B CG   1 
ATOM   4348 C CD1  . LEU   B 1 10  ? 38.418 -33.866 -18.842 1.00 21.41 ?  10  LEU   B CD1  1 
ATOM   4349 C CD2  . LEU   B 1 10  ? 38.155 -34.402 -16.405 1.00 21.26 ?  10  LEU   B CD2  1 
ATOM   4350 H H    . LEU   B 1 10  ? 40.736 -30.316 -16.759 1.00 21.83 ?  10  LEU   B H    1 
ATOM   4351 H HA   . LEU   B 1 10  ? 39.077 -31.061 -18.757 1.00 21.49 ?  10  LEU   B HA   1 
ATOM   4352 H HB2  . LEU   B 1 10  ? 40.163 -32.701 -17.389 1.00 22.93 ?  10  LEU   B HB2  1 
ATOM   4353 H HB3  . LEU   B 1 10  ? 39.319 -32.163 -16.162 1.00 22.93 ?  10  LEU   B HB3  1 
ATOM   4354 H HG   . LEU   B 1 10  ? 37.362 -32.835 -17.435 1.00 24.79 ?  10  LEU   B HG   1 
ATOM   4355 H HD11 . LEU   B 1 10  ? 37.718 -34.511 -19.022 1.00 25.85 ?  10  LEU   B HD11 1 
ATOM   4356 H HD12 . LEU   B 1 10  ? 38.377 -33.142 -19.485 1.00 25.85 ?  10  LEU   B HD12 1 
ATOM   4357 H HD13 . LEU   B 1 10  ? 39.286 -34.297 -18.882 1.00 25.85 ?  10  LEU   B HD13 1 
ATOM   4358 H HD21 . LEU   B 1 10  ? 37.447 -35.018 -16.644 1.00 25.66 ?  10  LEU   B HD21 1 
ATOM   4359 H HD22 . LEU   B 1 10  ? 39.007 -34.860 -16.386 1.00 25.66 ?  10  LEU   B HD22 1 
ATOM   4360 H HD23 . LEU   B 1 10  ? 37.970 -34.004 -15.539 1.00 25.66 ?  10  LEU   B HD23 1 
ATOM   4361 N N    . LYS   B 1 11  ? 37.005 -29.980 -18.055 1.00 18.95 ?  11  LYS   B N    1 
ATOM   4362 C CA   . LYS   B 1 11  ? 35.804 -29.274 -17.637 1.00 21.56 ?  11  LYS   B CA   1 
ATOM   4363 C C    . LYS   B 1 11  ? 34.958 -30.205 -16.775 1.00 20.26 ?  11  LYS   B C    1 
ATOM   4364 O O    . LYS   B 1 11  ? 34.599 -31.307 -17.208 1.00 22.00 ?  11  LYS   B O    1 
ATOM   4365 C CB   . LYS   B 1 11  ? 35.037 -28.837 -18.886 1.00 26.47 ?  11  LYS   B CB   1 
ATOM   4366 C CG   . LYS   B 1 11  ? 33.903 -27.860 -18.651 1.00 30.96 ?  11  LYS   B CG   1 
ATOM   4367 C CD   . LYS   B 1 11  ? 33.173 -27.577 -19.960 1.00 34.65 ?  11  LYS   B CD   1 
ATOM   4368 C CE   . LYS   B 1 11  ? 32.182 -26.435 -19.821 1.00 37.10 ?  11  LYS   B CE   1 
ATOM   4369 N NZ   . LYS   B 1 11  ? 32.865 -25.126 -19.629 1.00 38.51 ?  11  LYS   B NZ   1 
ATOM   4370 H H    . LYS   B 1 11  ? 36.967 -30.262 -18.870 1.00 22.89 ?  11  LYS   B H    1 
ATOM   4371 H HA   . LYS   B 1 11  ? 36.036 -28.488 -17.122 1.00 26.02 ?  11  LYS   B HA   1 
ATOM   4372 H HB2  . LYS   B 1 11  ? 35.661 -28.407 -19.496 1.00 31.92 ?  11  LYS   B HB2  1 
ATOM   4373 H HB3  . LYS   B 1 11  ? 34.658 -29.620 -19.312 1.00 31.92 ?  11  LYS   B HB3  1 
ATOM   4374 H HG2  . LYS   B 1 11  ? 33.270 -28.242 -18.025 1.00 37.31 ?  11  LYS   B HG2  1 
ATOM   4375 H HG3  . LYS   B 1 11  ? 34.258 -27.024 -18.312 1.00 37.31 ?  11  LYS   B HG3  1 
ATOM   4376 H HD2  . LYS   B 1 11  ? 33.822 -27.335 -20.641 1.00 41.73 ?  11  LYS   B HD2  1 
ATOM   4377 H HD3  . LYS   B 1 11  ? 32.685 -28.371 -20.231 1.00 41.73 ?  11  LYS   B HD3  1 
ATOM   4378 H HE2  . LYS   B 1 11  ? 31.643 -26.379 -20.625 1.00 44.67 ?  11  LYS   B HE2  1 
ATOM   4379 H HE3  . LYS   B 1 11  ? 31.617 -26.603 -19.051 1.00 44.67 ?  11  LYS   B HE3  1 
ATOM   4380 H HZ1  . LYS   B 1 11  ? 32.262 -24.474 -19.565 1.00 46.36 ?  11  LYS   B HZ1  1 
ATOM   4381 H HZ2  . LYS   B 1 11  ? 33.353 -25.142 -18.886 1.00 46.36 ?  11  LYS   B HZ2  1 
ATOM   4382 H HZ3  . LYS   B 1 11  ? 33.398 -24.957 -20.323 1.00 46.36 ?  11  LYS   B HZ3  1 
ATOM   4383 N N    . LEU   B 1 12  ? 34.649 -29.774 -15.554 1.00 18.40 ?  12  LEU   B N    1 
ATOM   4384 C CA   . LEU   B 1 12  ? 33.686 -30.475 -14.709 1.00 17.66 ?  12  LEU   B CA   1 
ATOM   4385 C C    . LEU   B 1 12  ? 32.298 -29.862 -14.802 1.00 17.81 ?  12  LEU   B C    1 
ATOM   4386 O O    . LEU   B 1 12  ? 31.312 -30.575 -14.970 1.00 18.47 ?  12  LEU   B O    1 
ATOM   4387 C CB   . LEU   B 1 12  ? 34.145 -30.494 -13.245 1.00 17.22 ?  12  LEU   B CB   1 
ATOM   4388 C CG   . LEU   B 1 12  ? 35.493 -31.166 -12.989 1.00 17.05 ?  12  LEU   B CG   1 
ATOM   4389 C CD1  . LEU   B 1 12  ? 35.874 -31.127 -11.513 1.00 17.41 ?  12  LEU   B CD1  1 
ATOM   4390 C CD2  . LEU   B 1 12  ? 35.493 -32.597 -13.505 1.00 17.44 ?  12  LEU   B CD2  1 
ATOM   4391 H H    . LEU   B 1 12  ? 34.977 -29.072 -15.191 1.00 22.23 ?  12  LEU   B H    1 
ATOM   4392 H HA   . LEU   B 1 12  ? 33.611 -31.394 -15.010 1.00 21.34 ?  12  LEU   B HA   1 
ATOM   4393 H HB2  . LEU   B 1 12  ? 34.202 -29.584 -12.927 1.00 20.82 ?  12  LEU   B HB2  1 
ATOM   4394 H HB3  . LEU   B 1 12  ? 33.476 -30.977 -12.721 1.00 20.82 ?  12  LEU   B HB3  1 
ATOM   4395 H HG   . LEU   B 1 12  ? 36.170 -30.679 -13.479 1.00 20.61 ?  12  LEU   B HG   1 
ATOM   4396 H HD11 . LEU   B 1 12  ? 36.740 -31.557 -11.398 1.00 21.05 ?  12  LEU   B HD11 1 
ATOM   4397 H HD12 . LEU   B 1 12  ? 35.926 -30.205 -11.219 1.00 21.05 ?  12  LEU   B HD12 1 
ATOM   4398 H HD13 . LEU   B 1 12  ? 35.204 -31.602 -10.995 1.00 21.05 ?  12  LEU   B HD13 1 
ATOM   4399 H HD21 . LEU   B 1 12  ? 36.290 -33.045 -13.189 1.00 21.09 ?  12  LEU   B HD21 1 
ATOM   4400 H HD22 . LEU   B 1 12  ? 34.702 -33.052 -13.174 1.00 21.09 ?  12  LEU   B HD22 1 
ATOM   4401 H HD23 . LEU   B 1 12  ? 35.482 -32.582 -14.476 1.00 21.09 ?  12  LEU   B HD23 1 
ATOM   4402 N N    . THR   B 1 13  ? 32.214 -28.547 -14.684 1.00 17.91 ?  13  THR   B N    1 
ATOM   4403 C CA   . THR   B 1 13  ? 30.998 -27.786 -14.900 1.00 17.50 ?  13  THR   B CA   1 
ATOM   4404 C C    . THR   B 1 13  ? 31.352 -26.600 -15.791 1.00 19.42 ?  13  THR   B C    1 
ATOM   4405 O O    . THR   B 1 13  ? 32.505 -26.421 -16.200 1.00 20.37 ?  13  THR   B O    1 
ATOM   4406 C CB   . THR   B 1 13  ? 30.404 -27.294 -13.575 1.00 16.89 ?  13  THR   B CB   1 
ATOM   4407 O OG1  . THR   B 1 13  ? 31.254 -26.273 -13.037 1.00 16.62 ?  13  THR   B OG1  1 
ATOM   4408 C CG2  . THR   B 1 13  ? 30.274 -28.438 -12.581 1.00 17.48 ?  13  THR   B CG2  1 
ATOM   4409 H H    . THR   B 1 13  ? 32.878 -28.054 -14.461 1.00 21.64 ?  13  THR   B H    1 
ATOM   4410 H HA   . THR   B 1 13  ? 30.335 -28.339 -15.350 1.00 21.15 ?  13  THR   B HA   1 
ATOM   4411 H HB   . THR   B 1 13  ? 29.515 -26.925 -13.736 1.00 20.43 ?  13  THR   B HB   1 
ATOM   4412 H HG1  . THR   B 1 13  ? 30.944 -25.512 -13.234 1.00 20.10 ?  13  THR   B HG1  1 
ATOM   4413 H HG21 . THR   B 1 13  ? 29.769 -28.149 -11.805 1.00 21.13 ?  13  THR   B HG21 1 
ATOM   4414 H HG22 . THR   B 1 13  ? 29.813 -29.185 -12.994 1.00 21.13 ?  13  THR   B HG22 1 
ATOM   4415 H HG23 . THR   B 1 13  ? 31.153 -28.729 -12.295 1.00 21.13 ?  13  THR   B HG23 1 
ATOM   4416 N N    A ASP   B 1 14  ? 30.353 -25.761 -16.068 0.34 20.39 ?  14  ASP   B N    1 
ATOM   4417 N N    B ASP   B 1 14  ? 30.353 -25.768 -16.085 0.66 20.33 ?  14  ASP   B N    1 
ATOM   4418 C CA   A ASP   B 1 14  ? 30.587 -24.616 -16.940 0.34 21.64 ?  14  ASP   B CA   1 
ATOM   4419 C CA   B ASP   B 1 14  ? 30.592 -24.620 -16.952 0.66 21.88 ?  14  ASP   B CA   1 
ATOM   4420 C C    A ASP   B 1 14  ? 31.674 -23.700 -16.395 0.34 20.01 ?  14  ASP   B C    1 
ATOM   4421 C C    B ASP   B 1 14  ? 31.632 -23.661 -16.389 0.66 20.20 ?  14  ASP   B C    1 
ATOM   4422 O O    A ASP   B 1 14  ? 32.341 -23.008 -17.173 0.34 20.92 ?  14  ASP   B O    1 
ATOM   4423 O O    B ASP   B 1 14  ? 32.204 -22.878 -17.156 0.66 21.68 ?  14  ASP   B O    1 
ATOM   4424 C CB   A ASP   B 1 14  ? 29.287 -23.841 -17.160 0.34 24.63 ?  14  ASP   B CB   1 
ATOM   4425 C CB   B ASP   B 1 14  ? 29.291 -23.863 -17.216 0.66 25.61 ?  14  ASP   B CB   1 
ATOM   4426 C CG   A ASP   B 1 14  ? 28.287 -24.602 -18.014 0.34 27.37 ?  14  ASP   B CG   1 
ATOM   4427 C CG   B ASP   B 1 14  ? 28.444 -24.512 -18.292 0.66 29.35 ?  14  ASP   B CG   1 
ATOM   4428 O OD1  A ASP   B 1 14  ? 28.662 -25.629 -18.619 0.34 28.09 ?  14  ASP   B OD1  1 
ATOM   4429 O OD1  B ASP   B 1 14  ? 28.940 -25.427 -18.984 0.66 30.51 ?  14  ASP   B OD1  1 
ATOM   4430 O OD2  A ASP   B 1 14  ? 27.114 -24.176 -18.071 0.34 28.59 -1 14  ASP   B OD2  1 
ATOM   4431 O OD2  B ASP   B 1 14  ? 27.273 -24.105 -18.447 0.66 30.93 -1 14  ASP   B OD2  1 
ATOM   4432 H H    A ASP   B 1 14  ? 29.553 -25.820 -15.762 0.34 24.62 ?  14  ASP   B H    1 
ATOM   4433 H H    B ASP   B 1 14  ? 29.549 -25.836 -15.795 0.66 24.55 ?  14  ASP   B H    1 
ATOM   4434 H HA   A ASP   B 1 14  ? 30.893 -24.932 -17.800 0.34 26.13 ?  14  ASP   B HA   1 
ATOM   4435 H HA   B ASP   B 1 14  ? 30.929 -24.936 -17.801 0.66 26.41 ?  14  ASP   B HA   1 
ATOM   4436 H HB2  A ASP   B 1 14  ? 28.859 -23.685 -16.307 0.34 29.71 ?  14  ASP   B HB2  1 
ATOM   4437 H HB2  B ASP   B 1 14  ? 28.769 -23.836 -16.401 0.66 30.88 ?  14  ASP   B HB2  1 
ATOM   4438 H HB3  A ASP   B 1 14  ? 29.492 -22.992 -17.589 0.34 29.71 ?  14  ASP   B HB3  1 
ATOM   4439 H HB3  B ASP   B 1 14  ? 29.502 -22.961 -17.507 0.66 30.88 ?  14  ASP   B HB3  1 
ATOM   4440 N N    . ASN   B 1 15  ? 31.883 -23.687 -15.075 1.00 17.91 ?  15  ASN   B N    1 
ATOM   4441 C CA   . ASN   B 1 15  ? 32.853 -22.777 -14.467 1.00 15.77 ?  15  ASN   B CA   1 
ATOM   4442 C C    . ASN   B 1 15  ? 33.945 -23.440 -13.634 1.00 14.30 ?  15  ASN   B C    1 
ATOM   4443 O O    . ASN   B 1 15  ? 34.812 -22.724 -13.122 1.00 14.20 ?  15  ASN   B O    1 
ATOM   4444 C CB   . ASN   B 1 15  ? 32.150 -21.719 -13.598 1.00 15.61 ?  15  ASN   B CB   1 
ATOM   4445 C CG   . ASN   B 1 15  ? 31.519 -22.320 -12.357 1.00 15.54 ?  15  ASN   B CG   1 
ATOM   4446 O OD1  . ASN   B 1 15  ? 30.565 -23.107 -12.446 1.00 17.14 ?  15  ASN   B OD1  1 
ATOM   4447 N ND2  . ASN   B 1 15  ? 32.057 -21.989 -11.195 1.00 14.51 ?  15  ASN   B ND2  1 
ATOM   4448 H H    A ASN   B 1 15  ? 31.470 -24.190 -14.508 0.34 21.65 ?  15  ASN   B H    1 
ATOM   4449 H H    B ASN   B 1 15  ? 31.488 -24.206 -14.510 0.66 21.65 ?  15  ASN   B H    1 
ATOM   4450 H HA   . ASN   B 1 15  ? 33.301 -22.289 -15.171 1.00 19.08 ?  15  ASN   B HA   1 
ATOM   4451 H HB2  . ASN   B 1 15  ? 32.804 -21.050 -13.313 1.00 18.89 ?  15  ASN   B HB2  1 
ATOM   4452 H HB3  . ASN   B 1 15  ? 31.450 -21.283 -14.112 1.00 18.89 ?  15  ASN   B HB3  1 
ATOM   4453 H HD21 . ASN   B 1 15  ? 31.733 -22.305 -10.460 1.00 17.56 ?  15  ASN   B HD21 1 
ATOM   4454 H HD22 . ASN   B 1 15  ? 32.729 -21.446 -11.158 1.00 17.56 ?  15  ASN   B HD22 1 
ATOM   4455 N N    . VAL   B 1 16  ? 33.930 -24.759 -13.464 1.00 14.10 ?  16  VAL   B N    1 
ATOM   4456 C CA   . VAL   B 1 16  ? 34.927 -25.456 -12.655 1.00 13.50 ?  16  VAL   B CA   1 
ATOM   4457 C C    . VAL   B 1 16  ? 35.719 -26.394 -13.550 1.00 13.76 ?  16  VAL   B C    1 
ATOM   4458 O O    . VAL   B 1 16  ? 35.144 -27.275 -14.208 1.00 15.02 ?  16  VAL   B O    1 
ATOM   4459 C CB   . VAL   B 1 16  ? 34.300 -26.219 -11.477 1.00 14.12 ?  16  VAL   B CB   1 
ATOM   4460 C CG1  . VAL   B 1 16  ? 35.381 -26.962 -10.684 1.00 14.41 ?  16  VAL   B CG1  1 
ATOM   4461 C CG2  . VAL   B 1 16  ? 33.509 -25.273 -10.580 1.00 14.62 ?  16  VAL   B CG2  1 
ATOM   4462 H H    . VAL   B 1 16  ? 33.329 -25.277 -13.805 1.00 17.08 ?  16  VAL   B H    1 
ATOM   4463 H HA   . VAL   B 1 16  ? 35.536 -24.805 -12.287 1.00 16.35 ?  16  VAL   B HA   1 
ATOM   4464 H HB   . VAL   B 1 16  ? 33.675 -26.880 -11.818 1.00 17.10 ?  16  VAL   B HB   1 
ATOM   4465 H HG11 . VAL   B 1 16  ? 35.003 -27.258 -9.838  1.00 17.44 ?  16  VAL   B HG11 1 
ATOM   4466 H HG12 . VAL   B 1 16  ? 35.679 -27.725 -11.197 1.00 17.44 ?  16  VAL   B HG12 1 
ATOM   4467 H HG13 . VAL   B 1 16  ? 36.118 -26.355 -10.519 1.00 17.44 ?  16  VAL   B HG13 1 
ATOM   4468 H HG21 . VAL   B 1 16  ? 33.169 -25.768 -9.815  1.00 17.69 ?  16  VAL   B HG21 1 
ATOM   4469 H HG22 . VAL   B 1 16  ? 34.092 -24.561 -10.278 1.00 17.69 ?  16  VAL   B HG22 1 
ATOM   4470 H HG23 . VAL   B 1 16  ? 32.767 -24.901 -11.085 1.00 17.69 ?  16  VAL   B HG23 1 
ATOM   4471 N N    . TYR   B 1 17  ? 37.040 -26.225 -13.534 1.00 13.90 ?  17  TYR   B N    1 
ATOM   4472 C CA   . TYR   B 1 17  ? 37.984 -26.972 -14.346 1.00 14.79 ?  17  TYR   B CA   1 
ATOM   4473 C C    . TYR   B 1 17  ? 39.040 -27.587 -13.435 1.00 14.06 ?  17  TYR   B C    1 
ATOM   4474 O O    . TYR   B 1 17  ? 39.325 -27.063 -12.357 1.00 14.35 ?  17  TYR   B O    1 
ATOM   4475 C CB   . TYR   B 1 17  ? 38.696 -26.044 -15.338 1.00 18.11 ?  17  TYR   B CB   1 
ATOM   4476 C CG   . TYR   B 1 17  ? 37.774 -25.273 -16.251 1.00 21.90 ?  17  TYR   B CG   1 
ATOM   4477 C CD1  . TYR   B 1 17  ? 37.243 -24.047 -15.868 1.00 23.65 ?  17  TYR   B CD1  1 
ATOM   4478 C CD2  . TYR   B 1 17  ? 37.436 -25.769 -17.502 1.00 24.27 ?  17  TYR   B CD2  1 
ATOM   4479 C CE1  . TYR   B 1 17  ? 36.400 -23.338 -16.705 1.00 25.57 ?  17  TYR   B CE1  1 
ATOM   4480 C CE2  . TYR   B 1 17  ? 36.596 -25.068 -18.347 1.00 25.85 ?  17  TYR   B CE2  1 
ATOM   4481 C CZ   . TYR   B 1 17  ? 36.079 -23.854 -17.943 1.00 26.68 ?  17  TYR   B CZ   1 
ATOM   4482 O OH   . TYR   B 1 17  ? 35.243 -23.155 -18.782 1.00 27.84 ?  17  TYR   B OH   1 
ATOM   4483 H H    . TYR   B 1 17  ? 37.428 -25.635 -13.034 1.00 16.84 ?  17  TYR   B H    1 
ATOM   4484 H HA   . TYR   B 1 17  ? 37.517 -27.671 -14.835 1.00 17.89 ?  17  TYR   B HA   1 
ATOM   4485 H HB2  . TYR   B 1 17  ? 39.233 -25.406 -14.845 1.00 21.89 ?  17  TYR   B HB2  1 
ATOM   4486 H HB3  . TYR   B 1 17  ? 39.262 -26.586 -15.901 1.00 21.89 ?  17  TYR   B HB3  1 
ATOM   4487 H HD1  . TYR   B 1 17  ? 37.459 -23.694 -15.036 1.00 28.53 ?  17  TYR   B HD1  1 
ATOM   4488 H HD2  . TYR   B 1 17  ? 37.777 -26.586 -17.780 1.00 29.27 ?  17  TYR   B HD2  1 
ATOM   4489 H HE1  . TYR   B 1 17  ? 36.053 -22.517 -16.437 1.00 30.83 ?  17  TYR   B HE1  1 
ATOM   4490 H HE2  . TYR   B 1 17  ? 36.372 -25.413 -19.183 1.00 31.18 ?  17  TYR   B HE2  1 
ATOM   4491 H HH   . TYR   B 1 17  ? 35.130 -23.580 -19.498 1.00 33.56 ?  17  TYR   B HH   1 
ATOM   4492 N N    . ILE   B 1 18  ? 39.640 -28.694 -13.869 1.00 14.09 ?  18  ILE   B N    1 
ATOM   4493 C CA   . ILE   B 1 18  ? 40.565 -29.426 -13.009 1.00 14.21 ?  18  ILE   B CA   1 
ATOM   4494 C C    . ILE   B 1 18  ? 41.722 -29.988 -13.827 1.00 14.63 ?  18  ILE   B C    1 
ATOM   4495 O O    . ILE   B 1 18  ? 41.561 -30.386 -14.986 1.00 15.60 ?  18  ILE   B O    1 
ATOM   4496 C CB   . ILE   B 1 18  ? 39.811 -30.525 -12.213 1.00 14.48 ?  18  ILE   B CB   1 
ATOM   4497 C CG1  . ILE   B 1 18  ? 40.665 -31.059 -11.059 1.00 14.92 ?  18  ILE   B CG1  1 
ATOM   4498 C CG2  . ILE   B 1 18  ? 39.311 -31.642 -13.143 1.00 15.11 ?  18  ILE   B CG2  1 
ATOM   4499 C CD1  . ILE   B 1 18  ? 39.859 -31.869 -10.058 1.00 16.48 ?  18  ILE   B CD1  1 
ATOM   4500 H H    . ILE   B 1 18  ? 39.524 -29.038 -14.644 1.00 17.06 ?  18  ILE   B H    1 
ATOM   4501 H HA   . ILE   B 1 18  ? 40.922 -28.816 -12.350 1.00 17.21 ?  18  ILE   B HA   1 
ATOM   4502 H HB   . ILE   B 1 18  ? 39.019 -30.127 -11.818 1.00 17.53 ?  18  ILE   B HB   1 
ATOM   4503 H HG12 . ILE   B 1 18  ? 41.358 -31.626 -11.411 1.00 18.06 ?  18  ILE   B HG12 1 
ATOM   4504 H HG13 . ILE   B 1 18  ? 41.047 -30.304 -10.586 1.00 18.06 ?  18  ILE   B HG13 1 
ATOM   4505 H HG21 . ILE   B 1 18  ? 38.714 -32.228 -12.647 1.00 18.28 ?  18  ILE   B HG21 1 
ATOM   4506 H HG22 . ILE   B 1 18  ? 38.832 -31.239 -13.884 1.00 18.28 ?  18  ILE   B HG22 1 
ATOM   4507 H HG23 . ILE   B 1 18  ? 40.069 -32.146 -13.472 1.00 18.28 ?  18  ILE   B HG23 1 
ATOM   4508 H HD11 . ILE   B 1 18  ? 40.440 -32.139 -9.330  1.00 19.92 ?  18  ILE   B HD11 1 
ATOM   4509 H HD12 . ILE   B 1 18  ? 39.132 -31.323 -9.715  1.00 19.92 ?  18  ILE   B HD12 1 
ATOM   4510 H HD13 . ILE   B 1 18  ? 39.499 -32.654 -10.502 1.00 19.92 ?  18  ILE   B HD13 1 
ATOM   4511 N N    . LYS   B 1 19  ? 42.900 -30.024 -13.208 1.00 14.50 ?  19  LYS   B N    1 
ATOM   4512 C CA   . LYS   B 1 19  ? 44.100 -30.505 -13.873 1.00 16.06 ?  19  LYS   B CA   1 
ATOM   4513 C C    . LYS   B 1 19  ? 45.010 -31.181 -12.858 1.00 16.08 ?  19  LYS   B C    1 
ATOM   4514 O O    . LYS   B 1 19  ? 45.106 -30.744 -11.708 1.00 15.67 ?  19  LYS   B O    1 
ATOM   4515 C CB   . LYS   B 1 19  ? 44.852 -29.342 -14.530 1.00 17.55 ?  19  LYS   B CB   1 
ATOM   4516 C CG   . LYS   B 1 19  ? 46.066 -29.754 -15.345 1.00 19.74 ?  19  LYS   B CG   1 
ATOM   4517 C CD   . LYS   B 1 19  ? 46.770 -28.532 -15.913 1.00 21.38 ?  19  LYS   B CD   1 
ATOM   4518 C CE   . LYS   B 1 19  ? 47.976 -28.904 -16.753 1.00 23.48 ?  19  LYS   B CE   1 
ATOM   4519 N NZ   . LYS   B 1 19  ? 48.637 -27.696 -17.317 1.00 24.50 ?  19  LYS   B NZ   1 
ATOM   4520 H H    . LYS   B 1 19  ? 43.018 -29.764 -12.392 1.00 17.55 ?  19  LYS   B H    1 
ATOM   4521 H HA   . LYS   B 1 19  ? 43.848 -31.148 -14.555 1.00 19.43 ?  19  LYS   B HA   1 
ATOM   4522 H HB2  . LYS   B 1 19  ? 44.237 -28.881 -15.121 1.00 21.21 ?  19  LYS   B HB2  1 
ATOM   4523 H HB3  . LYS   B 1 19  ? 45.145 -28.737 -13.828 1.00 21.21 ?  19  LYS   B HB3  1 
ATOM   4524 H HG2  . LYS   B 1 19  ? 46.680 -30.237 -14.773 1.00 23.84 ?  19  LYS   B HG2  1 
ATOM   4525 H HG3  . LYS   B 1 19  ? 45.770 -30.318 -16.078 1.00 23.84 ?  19  LYS   B HG3  1 
ATOM   4526 H HD2  . LYS   B 1 19  ? 46.148 -28.039 -16.471 1.00 25.81 ?  19  LYS   B HD2  1 
ATOM   4527 H HD3  . LYS   B 1 19  ? 47.070 -27.973 -15.177 1.00 25.81 ?  19  LYS   B HD3  1 
ATOM   4528 H HE2  . LYS   B 1 19  ? 48.618 -29.374 -16.198 1.00 28.33 ?  19  LYS   B HE2  1 
ATOM   4529 H HE3  . LYS   B 1 19  ? 47.690 -29.469 -17.487 1.00 28.33 ?  19  LYS   B HE3  1 
ATOM   4530 H HZ1  . LYS   B 1 19  ? 49.328 -27.937 -17.825 1.00 29.55 ?  19  LYS   B HZ1  1 
ATOM   4531 H HZ2  . LYS   B 1 19  ? 48.060 -27.235 -17.814 1.00 29.55 ?  19  LYS   B HZ2  1 
ATOM   4532 H HZ3  . LYS   B 1 19  ? 48.932 -27.174 -16.659 1.00 29.55 ?  19  LYS   B HZ3  1 
ATOM   4533 N N    . ASN   B 1 20  ? 45.693 -32.236 -13.293 1.00 17.02 ?  20  ASN   B N    1 
ATOM   4534 C CA   . ASN   B 1 20  ? 46.723 -32.872 -12.478 1.00 18.01 ?  20  ASN   B CA   1 
ATOM   4535 C C    . ASN   B 1 20  ? 48.010 -32.069 -12.654 1.00 18.34 ?  20  ASN   B C    1 
ATOM   4536 O O    . ASN   B 1 20  ? 48.658 -32.140 -13.705 1.00 20.50 ?  20  ASN   B O    1 
ATOM   4537 C CB   . ASN   B 1 20  ? 46.886 -34.333 -12.903 1.00 19.87 ?  20  ASN   B CB   1 
ATOM   4538 C CG   . ASN   B 1 20  ? 48.065 -35.029 -12.233 1.00 21.14 ?  20  ASN   B CG   1 
ATOM   4539 O OD1  . ASN   B 1 20  ? 48.746 -35.853 -12.859 1.00 23.29 ?  20  ASN   B OD1  1 
ATOM   4540 N ND2  . ASN   B 1 20  ? 48.308 -34.717 -10.964 1.00 20.82 ?  20  ASN   B ND2  1 
ATOM   4541 H H    . ASN   B 1 20  ? 45.579 -32.596 -14.064 1.00 20.58 ?  20  ASN   B H    1 
ATOM   4542 H HA   . ASN   B 1 20  ? 46.449 -32.852 -11.544 1.00 21.77 ?  20  ASN   B HA   1 
ATOM   4543 H HB2  . ASN   B 1 20  ? 46.076 -34.821 -12.670 1.00 23.99 ?  20  ASN   B HB2  1 
ATOM   4544 H HB3  . ASN   B 1 20  ? 47.022 -34.365 -13.860 1.00 23.99 ?  20  ASN   B HB3  1 
ATOM   4545 H HD21 . ASN   B 1 20  ? 48.963 -35.080 -10.547 1.00 25.14 ?  20  ASN   B HD21 1 
ATOM   4546 H HD22 . ASN   B 1 20  ? 47.810 -34.138 -10.554 1.00 25.14 ?  20  ASN   B HD22 1 
ATOM   4547 N N    . ALA   B 1 21  ? 48.371 -31.277 -11.643 1.00 17.75 ?  21  ALA   B N    1 
ATOM   4548 C CA   . ALA   B 1 21  ? 49.494 -30.366 -11.799 1.00 18.16 ?  21  ALA   B CA   1 
ATOM   4549 C C    . ALA   B 1 21  ? 49.954 -29.852 -10.442 1.00 17.16 ?  21  ALA   B C    1 
ATOM   4550 O O    . ALA   B 1 21  ? 49.211 -29.873 -9.455  1.00 16.66 ?  21  ALA   B O    1 
ATOM   4551 C CB   . ALA   B 1 21  ? 49.121 -29.207 -12.722 1.00 19.56 ?  21  ALA   B CB   1 
ATOM   4552 H H    . ALA   B 1 21  ? 47.982 -31.253 -10.869 1.00 21.45 ?  21  ALA   B H    1 
ATOM   4553 H HA   . ALA   B 1 21  ? 50.229 -30.854 -12.201 1.00 21.95 ?  21  ALA   B HA   1 
ATOM   4554 H HB1  . ALA   B 1 21  ? 49.911 -28.673 -12.871 1.00 23.62 ?  21  ALA   B HB1  1 
ATOM   4555 H HB2  . ALA   B 1 21  ? 48.804 -29.574 -13.564 1.00 23.62 ?  21  ALA   B HB2  1 
ATOM   4556 H HB3  . ALA   B 1 21  ? 48.425 -28.685 -12.304 1.00 23.62 ?  21  ALA   B HB3  1 
ATOM   4557 N N    . ASP   B 1 22  ? 51.211 -29.401 -10.429 1.00 16.16 ?  22  ASP   B N    1 
ATOM   4558 C CA   . ASP   B 1 22  ? 51.836 -28.709 -9.306  1.00 15.33 ?  22  ASP   B CA   1 
ATOM   4559 C C    . ASP   B 1 22  ? 51.431 -27.236 -9.381  1.00 13.70 ?  22  ASP   B C    1 
ATOM   4560 O O    . ASP   B 1 22  ? 51.740 -26.560 -10.367 1.00 14.27 ?  22  ASP   B O    1 
ATOM   4561 C CB   . ASP   B 1 22  ? 53.354 -28.888 -9.462  1.00 16.65 ?  22  ASP   B CB   1 
ATOM   4562 C CG   . ASP   B 1 22  ? 54.180 -28.145 -8.417  1.00 18.12 ?  22  ASP   B CG   1 
ATOM   4563 O OD1  . ASP   B 1 22  ? 53.827 -27.018 -8.033  1.00 18.13 ?  22  ASP   B OD1  1 
ATOM   4564 O OD2  . ASP   B 1 22  ? 55.229 -28.691 -8.004  1.00 20.75 -1 22  ASP   B OD2  1 
ATOM   4565 H H    . ASP   B 1 22  ? 51.744 -29.479 -11.104 1.00 19.54 ?  22  ASP   B H    1 
ATOM   4566 H HA   . ASP   B 1 22  ? 51.545 -29.093 -8.462  1.00 18.55 ?  22  ASP   B HA   1 
ATOM   4567 H HB2  . ASP   B 1 22  ? 53.569 -29.829 -9.395  1.00 20.13 ?  22  ASP   B HB2  1 
ATOM   4568 H HB3  . ASP   B 1 22  ? 53.618 -28.552 -10.335 1.00 20.13 ?  22  ASP   B HB3  1 
ATOM   4569 N N    . ILE   B 1 23  ? 50.727 -26.745 -8.353  1.00 13.29 ?  23  ILE   B N    1 
ATOM   4570 C CA   . ILE   B 1 23  ? 50.141 -25.402 -8.407  1.00 12.57 ?  23  ILE   B CA   1 
ATOM   4571 C C    . ILE   B 1 23  ? 51.202 -24.317 -8.561  1.00 12.23 ?  23  ILE   B C    1 
ATOM   4572 O O    . ILE   B 1 23  ? 50.937 -23.281 -9.178  1.00 12.02 ?  23  ILE   B O    1 
ATOM   4573 C CB   . ILE   B 1 23  ? 49.211 -25.149 -7.200  1.00 12.81 ?  23  ILE   B CB   1 
ATOM   4574 C CG1  . ILE   B 1 23  ? 48.389 -23.870 -7.394  1.00 12.94 ?  23  ILE   B CG1  1 
ATOM   4575 C CG2  . ILE   B 1 23  ? 49.996 -25.134 -5.894  1.00 13.46 ?  23  ILE   B CG2  1 
ATOM   4576 C CD1  . ILE   B 1 23  ? 47.267 -23.703 -6.383  1.00 13.95 ?  23  ILE   B CD1  1 
ATOM   4577 H H    . ILE   B 1 23  ? 50.564 -27.171 -7.623  1.00 16.10 ?  23  ILE   B H    1 
ATOM   4578 H HA   . ILE   B 1 23  ? 49.581 -25.353 -9.196  1.00 15.24 ?  23  ILE   B HA   1 
ATOM   4579 H HB   . ILE   B 1 23  ? 48.582 -25.887 -7.156  1.00 15.52 ?  23  ILE   B HB   1 
ATOM   4580 H HG12 . ILE   B 1 23  ? 48.983 -23.101 -7.309  1.00 15.67 ?  23  ILE   B HG12 1 
ATOM   4581 H HG13 . ILE   B 1 23  ? 47.995 -23.877 -8.280  1.00 15.67 ?  23  ILE   B HG13 1 
ATOM   4582 H HG21 . ILE   B 1 23  ? 49.376 -25.105 -5.151  1.00 16.31 ?  23  ILE   B HG21 1 
ATOM   4583 H HG22 . ILE   B 1 23  ? 50.531 -25.946 -5.844  1.00 16.31 ?  23  ILE   B HG22 1 
ATOM   4584 H HG23 . ILE   B 1 23  ? 50.575 -24.359 -5.881  1.00 16.31 ?  23  ILE   B HG23 1 
ATOM   4585 H HD11 . ILE   B 1 23  ? 46.760 -22.905 -6.603  1.00 16.89 ?  23  ILE   B HD11 1 
ATOM   4586 H HD12 . ILE   B 1 23  ? 46.695 -24.482 -6.420  1.00 16.89 ?  23  ILE   B HD12 1 
ATOM   4587 H HD13 . ILE   B 1 23  ? 47.652 -23.614 -5.496  1.00 16.89 ?  23  ILE   B HD13 1 
ATOM   4588 N N    . VAL   B 1 24  ? 52.399 -24.520 -8.002  1.00 12.22 ?  24  VAL   B N    1 
ATOM   4589 C CA   . VAL   B 1 24  ? 53.476 -23.543 -8.174  1.00 13.02 ?  24  VAL   B CA   1 
ATOM   4590 C C    . VAL   B 1 24  ? 53.931 -23.505 -9.625  1.00 13.19 ?  24  VAL   B C    1 
ATOM   4591 O O    . VAL   B 1 24  ? 54.066 -22.433 -10.226 1.00 13.86 ?  24  VAL   B O    1 
ATOM   4592 C CB   . VAL   B 1 24  ? 54.650 -23.856 -7.227  1.00 13.68 ?  24  VAL   B CB   1 
ATOM   4593 C CG1  . VAL   B 1 24  ? 55.862 -22.978 -7.552  1.00 14.65 ?  24  VAL   B CG1  1 
ATOM   4594 C CG2  . VAL   B 1 24  ? 54.221 -23.677 -5.787  1.00 14.66 ?  24  VAL   B CG2  1 
ATOM   4595 H H    . VAL   B 1 24  ? 52.606 -25.202 -7.527  1.00 14.82 ?  24  VAL   B H    1 
ATOM   4596 H HA   . VAL   B 1 24  ? 53.141 -22.663 -7.945  1.00 15.77 ?  24  VAL   B HA   1 
ATOM   4597 H HB   . VAL   B 1 24  ? 54.912 -24.785 -7.342  1.00 16.56 ?  24  VAL   B HB   1 
ATOM   4598 H HG11 . VAL   B 1 24  ? 56.463 -22.976 -6.788  1.00 17.73 ?  24  VAL   B HG11 1 
ATOM   4599 H HG12 . VAL   B 1 24  ? 56.319 -23.345 -8.325  1.00 17.73 ?  24  VAL   B HG12 1 
ATOM   4600 H HG13 . VAL   B 1 24  ? 55.560 -22.078 -7.736  1.00 17.73 ?  24  VAL   B HG13 1 
ATOM   4601 H HG21 . VAL   B 1 24  ? 54.949 -23.935 -5.201  1.00 17.75 ?  24  VAL   B HG21 1 
ATOM   4602 H HG22 . VAL   B 1 24  ? 53.992 -22.745 -5.640  1.00 17.75 ?  24  VAL   B HG22 1 
ATOM   4603 H HG23 . VAL   B 1 24  ? 53.445 -24.237 -5.614  1.00 17.75 ?  24  VAL   B HG23 1 
ATOM   4604 N N    . GLU   B 1 25  ? 54.202 -24.679 -10.205 1.00 14.32 ?  25  GLU   B N    1 
ATOM   4605 C CA   . GLU   B 1 25  ? 54.583 -24.725 -11.611 1.00 15.99 ?  25  GLU   B CA   1 
ATOM   4606 C C    . GLU   B 1 25  ? 53.474 -24.172 -12.495 1.00 14.72 ?  25  GLU   B C    1 
ATOM   4607 O O    . GLU   B 1 25  ? 53.743 -23.457 -13.470 1.00 15.70 ?  25  GLU   B O    1 
ATOM   4608 C CB   . GLU   B 1 25  ? 54.967 -26.151 -12.006 1.00 21.14 ?  25  GLU   B CB   1 
ATOM   4609 C CG   . GLU   B 1 25  ? 56.251 -26.624 -11.336 1.00 27.85 ?  25  GLU   B CG   1 
ATOM   4610 C CD   . GLU   B 1 25  ? 57.380 -25.605 -11.405 1.00 33.52 ?  25  GLU   B CD   1 
ATOM   4611 O OE1  . GLU   B 1 25  ? 57.742 -25.181 -12.523 1.00 35.77 ?  25  GLU   B OE1  1 
ATOM   4612 O OE2  . GLU   B 1 25  ? 57.896 -25.213 -10.333 1.00 35.64 -1 25  GLU   B OE2  1 
ATOM   4613 H H    . GLU   B 1 25  ? 54.181 -25.442 -9.808  1.00 17.33 ?  25  GLU   B H    1 
ATOM   4614 H HA   . GLU   B 1 25  ? 55.347 -24.151 -11.746 1.00 19.34 ?  25  GLU   B HA   1 
ATOM   4615 H HB2  . GLU   B 1 25  ? 54.252 -26.757 -11.741 1.00 25.52 ?  25  GLU   B HB2  1 
ATOM   4616 H HB3  . GLU   B 1 25  ? 55.092 -26.192 -12.967 1.00 25.52 ?  25  GLU   B HB3  1 
ATOM   4617 H HG2  . GLU   B 1 25  ? 56.078 -26.783 -10.401 1.00 33.57 ?  25  GLU   B HG2  1 
ATOM   4618 H HG3  . GLU   B 1 25  ? 56.549 -27.437 -11.771 1.00 33.57 ?  25  GLU   B HG3  1 
ATOM   4619 N N    A GLU   B 1 26  ? 52.218 -24.479 -12.164 0.34 13.77 ?  26  GLU   B N    1 
ATOM   4620 N N    B GLU   B 1 26  ? 52.218 -24.481 -12.163 0.66 14.03 ?  26  GLU   B N    1 
ATOM   4621 C CA   A GLU   B 1 26  ? 51.099 -23.946 -12.935 0.34 13.58 ?  26  GLU   B CA   1 
ATOM   4622 C CA   B GLU   B 1 26  ? 51.093 -23.954 -12.931 0.66 14.97 ?  26  GLU   B CA   1 
ATOM   4623 C C    A GLU   B 1 26  ? 51.059 -22.428 -12.858 0.34 13.40 ?  26  GLU   B C    1 
ATOM   4624 C C    B GLU   B 1 26  ? 51.043 -22.434 -12.855 0.66 14.02 ?  26  GLU   B C    1 
ATOM   4625 O O    A GLU   B 1 26  ? 50.889 -21.746 -13.874 0.34 14.31 ?  26  GLU   B O    1 
ATOM   4626 O O    B GLU   B 1 26  ? 50.835 -21.757 -13.867 0.66 15.34 ?  26  GLU   B O    1 
ATOM   4627 C CB   A GLU   B 1 26  ? 49.785 -24.532 -12.423 0.34 13.95 ?  26  GLU   B CB   1 
ATOM   4628 C CB   B GLU   B 1 26  ? 49.777 -24.542 -12.413 0.66 17.35 ?  26  GLU   B CB   1 
ATOM   4629 C CG   A GLU   B 1 26  ? 49.496 -25.919 -12.936 0.34 15.15 ?  26  GLU   B CG   1 
ATOM   4630 C CG   B GLU   B 1 26  ? 49.264 -25.754 -13.174 0.66 20.88 ?  26  GLU   B CG   1 
ATOM   4631 C CD   A GLU   B 1 26  ? 49.322 -25.967 -14.436 0.34 15.03 ?  26  GLU   B CD   1 
ATOM   4632 C CD   B GLU   B 1 26  ? 48.933 -25.441 -14.630 0.66 22.09 ?  26  GLU   B CD   1 
ATOM   4633 O OE1  A GLU   B 1 26  ? 48.486 -25.203 -14.962 0.34 14.29 ?  26  GLU   B OE1  1 
ATOM   4634 O OE1  B GLU   B 1 26  ? 47.922 -24.756 -14.906 0.66 23.34 ?  26  GLU   B OE1  1 
ATOM   4635 O OE2  A GLU   B 1 26  ? 50.027 -26.763 -15.085 0.34 15.83 -1 26  GLU   B OE2  1 
ATOM   4636 O OE2  B GLU   B 1 26  ? 49.694 -25.888 -15.503 0.66 22.38 -1 26  GLU   B OE2  1 
ATOM   4637 H H    A GLU   B 1 26  ? 51.987 -24.982 -11.502 0.34 16.68 ?  26  GLU   B H    1 
ATOM   4638 H H    B GLU   B 1 26  ? 51.990 -24.986 -11.501 0.66 16.99 ?  26  GLU   B H    1 
ATOM   4639 H HA   A GLU   B 1 26  ? 51.205 -24.195 -13.864 0.34 16.45 ?  26  GLU   B HA   1 
ATOM   4640 H HA   B GLU   B 1 26  ? 51.198 -24.207 -13.860 0.66 18.11 ?  26  GLU   B HA   1 
ATOM   4641 H HB2  A GLU   B 1 26  ? 49.818 -24.574 -11.453 0.34 16.89 ?  26  GLU   B HB2  1 
ATOM   4642 H HB2  B GLU   B 1 26  ? 49.899 -24.802 -11.488 0.66 20.97 ?  26  GLU   B HB2  1 
ATOM   4643 H HB3  A GLU   B 1 26  ? 49.055 -23.950 -12.697 0.34 16.89 ?  26  GLU   B HB3  1 
ATOM   4644 H HB3  B GLU   B 1 26  ? 49.094 -23.853 -12.468 0.66 20.97 ?  26  GLU   B HB3  1 
ATOM   4645 H HG2  A GLU   B 1 26  ? 50.241 -26.486 -12.714 0.34 18.33 ?  26  GLU   B HG2  1 
ATOM   4646 H HG2  B GLU   B 1 26  ? 49.944 -26.446 -13.146 0.66 25.21 ?  26  GLU   B HG2  1 
ATOM   4647 H HG3  A GLU   B 1 26  ? 48.682 -26.237 -12.524 0.34 18.33 ?  26  GLU   B HG3  1 
ATOM   4648 H HG3  B GLU   B 1 26  ? 48.452 -26.069 -12.748 0.66 25.21 ?  26  GLU   B HG3  1 
ATOM   4649 N N    . ALA   B 1 27  ? 51.200 -21.880 -11.651 1.00 12.99 ?  27  ALA   B N    1 
ATOM   4650 C CA   . ALA   B 1 27  ? 51.161 -20.431 -11.501 1.00 13.14 ?  27  ALA   B CA   1 
ATOM   4651 C C    . ALA   B 1 27  ? 52.227 -19.770 -12.364 1.00 14.47 ?  27  ALA   B C    1 
ATOM   4652 O O    . ALA   B 1 27  ? 51.965 -18.769 -13.043 1.00 15.02 ?  27  ALA   B O    1 
ATOM   4653 C CB   . ALA   B 1 27  ? 51.328 -20.052 -10.030 1.00 13.07 ?  27  ALA   B CB   1 
ATOM   4654 H H    A ALA   B 1 27  ? 51.316 -22.315 -10.919 0.34 15.74 ?  27  ALA   B H    1 
ATOM   4655 H H    B ALA   B 1 27  ? 51.319 -22.314 -10.919 0.66 15.74 ?  27  ALA   B H    1 
ATOM   4656 H HA   . ALA   B 1 27  ? 50.299 -20.104 -11.792 1.00 15.92 ?  27  ALA   B HA   1 
ATOM   4657 H HB1  . ALA   B 1 27  ? 51.296 -19.087 -9.944  1.00 15.84 ?  27  ALA   B HB1  1 
ATOM   4658 H HB2  . ALA   B 1 27  ? 50.605 -20.453 -9.518  1.00 15.84 ?  27  ALA   B HB2  1 
ATOM   4659 H HB3  . ALA   B 1 27  ? 52.181 -20.386 -9.710  1.00 15.84 ?  27  ALA   B HB3  1 
ATOM   4660 N N    . LYS   B 1 28  ? 53.438 -20.328 -12.368 1.00 15.51 ?  28  LYS   B N    1 
ATOM   4661 C CA   . LYS   B 1 28  ? 54.515 -19.719 -13.138 1.00 17.76 ?  28  LYS   B CA   1 
ATOM   4662 C C    . LYS   B 1 28  ? 54.259 -19.801 -14.637 1.00 18.21 ?  28  LYS   B C    1 
ATOM   4663 O O    . LYS   B 1 28  ? 54.674 -18.903 -15.380 1.00 19.37 ?  28  LYS   B O    1 
ATOM   4664 C CB   . LYS   B 1 28  ? 55.872 -20.321 -12.750 1.00 21.29 ?  28  LYS   B CB   1 
ATOM   4665 C CG   . LYS   B 1 28  ? 56.286 -19.974 -11.321 1.00 24.95 ?  28  LYS   B CG   1 
ATOM   4666 C CD   . LYS   B 1 28  ? 57.711 -20.394 -10.982 1.00 29.79 ?  28  LYS   B CD   1 
ATOM   4667 C CE   . LYS   B 1 28  ? 57.812 -21.875 -10.695 1.00 33.61 ?  28  LYS   B CE   1 
ATOM   4668 N NZ   . LYS   B 1 28  ? 59.163 -22.237 -10.174 1.00 35.39 ?  28  LYS   B NZ   1 
ATOM   4669 H H    . LYS   B 1 28  ? 53.658 -21.034 -11.934 1.00 18.76 ?  28  LYS   B H    1 
ATOM   4670 H HA   . LYS   B 1 28  ? 54.555 -18.779 -12.918 1.00 21.46 ?  28  LYS   B HA   1 
ATOM   4671 H HB2  . LYS   B 1 28  ? 55.829 -21.284 -12.823 1.00 25.70 ?  28  LYS   B HB2  1 
ATOM   4672 H HB3  . LYS   B 1 28  ? 56.556 -19.973 -13.349 1.00 25.70 ?  28  LYS   B HB3  1 
ATOM   4673 H HG2  . LYS   B 1 28  ? 56.222 -19.013 -11.203 1.00 30.09 ?  28  LYS   B HG2  1 
ATOM   4674 H HG3  . LYS   B 1 28  ? 55.688 -20.424 -10.708 1.00 30.09 ?  28  LYS   B HG3  1 
ATOM   4675 H HD2  . LYS   B 1 28  ? 58.292 -20.188 -11.732 1.00 35.90 ?  28  LYS   B HD2  1 
ATOM   4676 H HD3  . LYS   B 1 28  ? 58.004 -19.910 -10.192 1.00 35.90 ?  28  LYS   B HD3  1 
ATOM   4677 H HE2  . LYS   B 1 28  ? 57.152 -22.117 -10.026 1.00 40.49 ?  28  LYS   B HE2  1 
ATOM   4678 H HE3  . LYS   B 1 28  ? 57.658 -22.371 -11.514 1.00 40.49 ?  28  LYS   B HE3  1 
ATOM   4679 H HZ1  . LYS   B 1 28  ? 59.203 -23.110 -10.011 1.00 42.61 ?  28  LYS   B HZ1  1 
ATOM   4680 H HZ2  . LYS   B 1 28  ? 59.786 -22.025 -10.773 1.00 42.61 ?  28  LYS   B HZ2  1 
ATOM   4681 H HZ3  . LYS   B 1 28  ? 59.326 -21.794 -9.419  1.00 42.61 ?  28  LYS   B HZ3  1 
ATOM   4682 N N    . LYS   B 1 29  ? 53.562 -20.842 -15.097 1.00 19.60 ?  29  LYS   B N    1 
ATOM   4683 C CA   . LYS   B 1 29  ? 53.292 -20.994 -16.524 1.00 22.31 ?  29  LYS   B CA   1 
ATOM   4684 C C    . LYS   B 1 29  ? 52.041 -20.242 -16.975 1.00 21.20 ?  29  LYS   B C    1 
ATOM   4685 O O    . LYS   B 1 29  ? 52.042 -19.627 -18.046 1.00 22.47 ?  29  LYS   B O    1 
ATOM   4686 C CB   . LYS   B 1 29  ? 53.169 -22.477 -16.886 1.00 27.49 ?  29  LYS   B CB   1 
ATOM   4687 C CG   . LYS   B 1 29  ? 52.914 -22.734 -18.362 1.00 32.54 ?  29  LYS   B CG   1 
ATOM   4688 C CD   . LYS   B 1 29  ? 53.083 -24.208 -18.705 1.00 36.40 ?  29  LYS   B CD   1 
ATOM   4689 C CE   . LYS   B 1 29  ? 51.990 -25.068 -18.088 1.00 39.20 ?  29  LYS   B CE   1 
ATOM   4690 N NZ   . LYS   B 1 29  ? 52.208 -26.517 -18.366 1.00 40.54 ?  29  LYS   B NZ   1 
ATOM   4691 H H    . LYS   B 1 29  ? 53.229 -21.470 -14.603 1.00 23.67 ?  29  LYS   B H    1 
ATOM   4692 H HA   . LYS   B 1 29  ? 54.043 -20.643 -17.016 1.00 26.92 ?  29  LYS   B HA   1 
ATOM   4693 H HB2  . LYS   B 1 29  ? 53.999 -22.927 -16.653 1.00 33.14 ?  29  LYS   B HB2  1 
ATOM   4694 H HB3  . LYS   B 1 29  ? 52.436 -22.865 -16.390 1.00 33.14 ?  29  LYS   B HB3  1 
ATOM   4695 H HG2  . LYS   B 1 29  ? 52.005 -22.472 -18.580 1.00 39.19 ?  29  LYS   B HG2  1 
ATOM   4696 H HG3  . LYS   B 1 29  ? 53.546 -22.221 -18.892 1.00 39.19 ?  29  LYS   B HG3  1 
ATOM   4697 H HD2  . LYS   B 1 29  ? 53.048 -24.318 -19.667 1.00 43.83 ?  29  LYS   B HD2  1 
ATOM   4698 H HD3  . LYS   B 1 29  ? 53.938 -24.517 -18.364 1.00 43.83 ?  29  LYS   B HD3  1 
ATOM   4699 H HE2  . LYS   B 1 29  ? 51.984 -24.943 -17.126 1.00 47.19 ?  29  LYS   B HE2  1 
ATOM   4700 H HE3  . LYS   B 1 29  ? 51.132 -24.812 -18.464 1.00 47.19 ?  29  LYS   B HE3  1 
ATOM   4701 H HZ1  . LYS   B 1 29  ? 51.557 -26.999 -17.997 1.00 48.80 ?  29  LYS   B HZ1  1 
ATOM   4702 H HZ2  . LYS   B 1 29  ? 52.212 -26.661 -19.244 1.00 48.80 ?  29  LYS   B HZ2  1 
ATOM   4703 H HZ3  . LYS   B 1 29  ? 52.989 -26.777 -18.026 1.00 48.80 ?  29  LYS   B HZ3  1 
ATOM   4704 N N    . VAL   B 1 30  ? 50.971 -20.295 -16.179 1.00 19.36 ?  30  VAL   B N    1 
ATOM   4705 C CA   . VAL   B 1 30  ? 49.683 -19.708 -16.557 1.00 19.22 ?  30  VAL   B CA   1 
ATOM   4706 C C    . VAL   B 1 30  ? 49.682 -18.196 -16.391 1.00 17.84 ?  30  VAL   B C    1 
ATOM   4707 O O    . VAL   B 1 30  ? 48.940 -17.483 -17.087 1.00 18.44 ?  30  VAL   B O    1 
ATOM   4708 C CB   . VAL   B 1 30  ? 48.585 -20.332 -15.674 1.00 21.12 ?  30  VAL   B CB   1 
ATOM   4709 C CG1  . VAL   B 1 30  ? 47.298 -19.524 -15.739 1.00 22.04 ?  30  VAL   B CG1  1 
ATOM   4710 C CG2  . VAL   B 1 30  ? 48.348 -21.792 -16.054 1.00 22.22 ?  30  VAL   B CG2  1 
ATOM   4711 H H    . VAL   B 1 30  ? 50.958 -20.696 -15.408 1.00 23.38 ?  30  VAL   B H    1 
ATOM   4712 H HA   . VAL   B 1 30  ? 49.490 -19.937 -17.483 1.00 23.21 ?  30  VAL   B HA   1 
ATOM   4713 H HB   . VAL   B 1 30  ? 48.886 -20.327 -14.752 1.00 25.49 ?  30  VAL   B HB   1 
ATOM   4714 H HG11 . VAL   B 1 30  ? 46.561 -20.100 -15.482 1.00 26.60 ?  30  VAL   B HG11 1 
ATOM   4715 H HG12 . VAL   B 1 30  ? 47.359 -18.778 -15.125 1.00 26.60 ?  30  VAL   B HG12 1 
ATOM   4716 H HG13 . VAL   B 1 30  ? 47.164 -19.213 -16.643 1.00 26.60 ?  30  VAL   B HG13 1 
ATOM   4717 H HG21 . VAL   B 1 30  ? 47.658 -22.165 -15.479 1.00 26.82 ?  30  VAL   B HG21 1 
ATOM   4718 H HG22 . VAL   B 1 30  ? 48.058 -21.836 -16.981 1.00 26.82 ?  30  VAL   B HG22 1 
ATOM   4719 H HG23 . VAL   B 1 30  ? 49.172 -22.289 -15.943 1.00 26.82 ?  30  VAL   B HG23 1 
ATOM   4720 N N    A LYS   B 1 31  ? 50.488 -17.690 -15.467 0.34 17.95 ?  31  LYS   B N    1 
ATOM   4721 N N    B LYS   B 1 31  ? 50.483 -17.687 -15.463 0.66 17.28 ?  31  LYS   B N    1 
ATOM   4722 C CA   A LYS   B 1 31  ? 50.495 -16.279 -15.103 0.34 18.53 ?  31  LYS   B CA   1 
ATOM   4723 C CA   B LYS   B 1 31  ? 50.497 -16.274 -15.105 0.66 17.84 ?  31  LYS   B CA   1 
ATOM   4724 C C    A LYS   B 1 31  ? 49.094 -15.789 -14.723 0.34 16.28 ?  31  LYS   B C    1 
ATOM   4725 C C    B LYS   B 1 31  ? 49.104 -15.771 -14.710 0.66 15.76 ?  31  LYS   B C    1 
ATOM   4726 O O    A LYS   B 1 31  ? 48.542 -14.900 -15.378 0.34 16.26 ?  31  LYS   B O    1 
ATOM   4727 O O    B LYS   B 1 31  ? 48.566 -14.852 -15.337 0.66 15.95 ?  31  LYS   B O    1 
ATOM   4728 C CB   A LYS   B 1 31  ? 51.106 -15.426 -16.206 0.34 21.38 ?  31  LYS   B CB   1 
ATOM   4729 C CB   B LYS   B 1 31  ? 51.110 -15.432 -16.217 0.66 20.75 ?  31  LYS   B CB   1 
ATOM   4730 C CG   A LYS   B 1 31  ? 52.560 -15.788 -16.495 0.34 24.15 ?  31  LYS   B CG   1 
ATOM   4731 C CG   B LYS   B 1 31  ? 52.525 -15.886 -16.574 0.66 24.24 ?  31  LYS   B CG   1 
ATOM   4732 C CD   A LYS   B 1 31  ? 53.128 -14.974 -17.641 0.34 26.51 ?  31  LYS   B CD   1 
ATOM   4733 C CD   B LYS   B 1 31  ? 53.112 -15.095 -17.725 0.66 27.77 ?  31  LYS   B CD   1 
ATOM   4734 C CE   A LYS   B 1 31  ? 54.600 -15.277 -17.856 0.34 28.40 ?  31  LYS   B CE   1 
ATOM   4735 C CE   B LYS   B 1 31  ? 54.607 -15.324 -17.834 0.66 30.37 ?  31  LYS   B CE   1 
ATOM   4736 N NZ   A LYS   B 1 31  ? 55.413 -14.938 -16.655 0.34 29.36 ?  31  LYS   B NZ   1 
ATOM   4737 N NZ   B LYS   B 1 31  ? 55.312 -14.939 -16.578 0.66 31.58 ?  31  LYS   B NZ   1 
ATOM   4738 H H    A LYS   B 1 31  ? 51.058 -18.166 -15.033 0.34 21.70 ?  31  LYS   B H    1 
ATOM   4739 H H    B LYS   B 1 31  ? 51.053 -18.168 -15.029 0.66 20.89 ?  31  LYS   B H    1 
ATOM   4740 H HA   A LYS   B 1 31  ? 51.054 -16.188 -14.328 0.34 22.38 ?  31  LYS   B HA   1 
ATOM   4741 H HA   B LYS   B 1 31  ? 51.058 -16.188 -14.331 0.66 21.56 ?  31  LYS   B HA   1 
ATOM   4742 H HB2  A LYS   B 1 31  ? 50.603 -15.547 -17.026 0.34 25.81 ?  31  LYS   B HB2  1 
ATOM   4743 H HB2  B LYS   B 1 31  ? 50.564 -15.502 -17.015 0.66 25.06 ?  31  LYS   B HB2  1 
ATOM   4744 H HB3  A LYS   B 1 31  ? 51.080 -14.498 -15.931 0.34 25.81 ?  31  LYS   B HB3  1 
ATOM   4745 H HB3  B LYS   B 1 31  ? 51.156 -14.515 -15.917 0.66 25.06 ?  31  LYS   B HB3  1 
ATOM   4746 H HG2  A LYS   B 1 31  ? 53.093 -15.614 -15.703 0.34 29.13 ?  31  LYS   B HG2  1 
ATOM   4747 H HG2  B LYS   B 1 31  ? 53.092 -15.771 -15.797 0.66 29.24 ?  31  LYS   B HG2  1 
ATOM   4748 H HG3  A LYS   B 1 31  ? 52.616 -16.727 -16.733 0.34 29.13 ?  31  LYS   B HG3  1 
ATOM   4749 H HG3  B LYS   B 1 31  ? 52.503 -16.822 -16.833 0.66 29.24 ?  31  LYS   B HG3  1 
ATOM   4750 H HD2  A LYS   B 1 31  ? 52.650 -15.193 -18.455 0.34 31.97 ?  31  LYS   B HD2  1 
ATOM   4751 H HD2  B LYS   B 1 31  ? 52.696 -15.383 -18.553 0.66 33.47 ?  31  LYS   B HD2  1 
ATOM   4752 H HD3  A LYS   B 1 31  ? 53.037 -14.031 -17.438 0.34 31.97 ?  31  LYS   B HD3  1 
ATOM   4753 H HD3  B LYS   B 1 31  ? 52.954 -14.152 -17.576 0.66 33.47 ?  31  LYS   B HD3  1 
ATOM   4754 H HE2  A LYS   B 1 31  ? 54.709 -16.225 -18.038 0.34 34.23 ?  31  LYS   B HE2  1 
ATOM   4755 H HE2  B LYS   B 1 31  ? 54.777 -16.264 -18.003 0.66 36.59 ?  31  LYS   B HE2  1 
ATOM   4756 H HE3  A LYS   B 1 31  ? 54.929 -14.753 -18.603 0.34 34.23 ?  31  LYS   B HE3  1 
ATOM   4757 H HE3  B LYS   B 1 31  ? 54.960 -14.784 -18.558 0.66 36.59 ?  31  LYS   B HE3  1 
ATOM   4758 H HZ1  A LYS   B 1 31  ? 56.278 -15.055 -16.830 0.34 35.38 ?  31  LYS   B HZ1  1 
ATOM   4759 H HZ1  B LYS   B 1 31  ? 56.190 -14.912 -16.718 0.66 38.04 ?  31  LYS   B HZ1  1 
ATOM   4760 H HZ2  A LYS   B 1 31  ? 55.277 -14.089 -16.427 0.34 35.38 ?  31  LYS   B HZ2  1 
ATOM   4761 H HZ2  B LYS   B 1 31  ? 55.037 -14.136 -16.308 0.66 38.04 ?  31  LYS   B HZ2  1 
ATOM   4762 H HZ3  A LYS   B 1 31  ? 55.182 -15.461 -15.973 0.34 35.38 ?  31  LYS   B HZ3  1 
ATOM   4763 H HZ3  B LYS   B 1 31  ? 55.140 -15.532 -15.936 0.66 38.04 ?  31  LYS   B HZ3  1 
ATOM   4764 N N    . PRO   B 1 32  ? 48.499 -16.350 -13.669 1.00 14.34 ?  32  PRO   B N    1 
ATOM   4765 C CA   . PRO   B 1 32  ? 47.126 -15.978 -13.304 1.00 13.26 ?  32  PRO   B CA   1 
ATOM   4766 C C    . PRO   B 1 32  ? 47.058 -14.636 -12.591 1.00 13.30 ?  32  PRO   B C    1 
ATOM   4767 O O    . PRO   B 1 32  ? 47.990 -14.222 -11.894 1.00 14.34 ?  32  PRO   B O    1 
ATOM   4768 C CB   . PRO   B 1 32  ? 46.720 -17.093 -12.331 1.00 13.58 ?  32  PRO   B CB   1 
ATOM   4769 C CG   . PRO   B 1 32  ? 48.020 -17.439 -11.650 1.00 13.77 ?  32  PRO   B CG   1 
ATOM   4770 C CD   . PRO   B 1 32  ? 49.076 -17.324 -12.719 1.00 14.08 ?  32  PRO   B CD   1 
ATOM   4771 H HA   . PRO   B 1 32  ? 46.540 -15.989 -14.092 1.00 16.06 ?  32  PRO   B HA   1 
ATOM   4772 H HB2  . PRO   B 1 32  ? 46.070 -16.749 -11.698 1.00 16.44 ?  32  PRO   B HB2  1 
ATOM   4773 H HB3  . PRO   B 1 32  ? 46.364 -17.852 -12.819 1.00 16.44 ?  32  PRO   B HB3  1 
ATOM   4774 H HG2  . PRO   B 1 32  ? 48.187 -16.811 -10.932 1.00 16.67 ?  32  PRO   B HG2  1 
ATOM   4775 H HG3  . PRO   B 1 32  ? 47.971 -18.347 -11.309 1.00 16.67 ?  32  PRO   B HG3  1 
ATOM   4776 H HD2  . PRO   B 1 32  ? 49.892 -16.977 -12.343 1.00 17.05 ?  32  PRO   B HD2  1 
ATOM   4777 H HD3  . PRO   B 1 32  ? 49.208 -18.184 -13.146 1.00 17.05 ?  32  PRO   B HD3  1 
ATOM   4778 N N    . THR   B 1 33  ? 45.908 -13.972 -12.743 1.00 12.77 ?  33  THR   B N    1 
ATOM   4779 C CA   . THR   B 1 33  ? 45.633 -12.793 -11.929 1.00 12.69 ?  33  THR   B CA   1 
ATOM   4780 C C    . THR   B 1 33  ? 45.583 -13.146 -10.448 1.00 12.62 ?  33  THR   B C    1 
ATOM   4781 O O    . THR   B 1 33  ? 46.056 -12.369 -9.607  1.00 13.75 ?  33  THR   B O    1 
ATOM   4782 C CB   . THR   B 1 33  ? 44.312 -12.158 -12.366 1.00 13.28 ?  33  THR   B CB   1 
ATOM   4783 O OG1  . THR   B 1 33  ? 44.342 -11.910 -13.773 1.00 13.85 ?  33  THR   B OG1  1 
ATOM   4784 C CG2  . THR   B 1 33  ? 44.059 -10.865 -11.618 1.00 15.13 ?  33  THR   B CG2  1 
ATOM   4785 H H    . THR   B 1 33  ? 45.284 -14.190 -13.299 1.00 15.47 ?  33  THR   B H    1 
ATOM   4786 H HA   . THR   B 1 33  ? 46.340 -12.150 -12.067 1.00 15.38 ?  33  THR   B HA   1 
ATOM   4787 H HB   . THR   B 1 33  ? 43.584 -12.775 -12.173 1.00 16.09 ?  33  THR   B HB   1 
ATOM   4788 H HG1  . THR   B 1 33  ? 43.619 -11.546 -14.020 1.00 16.77 ?  33  THR   B HG1  1 
ATOM   4789 H HG21 . THR   B 1 33  ? 43.301 -10.405 -12.001 1.00 18.31 ?  33  THR   B HG21 1 
ATOM   4790 H HG22 . THR   B 1 33  ? 43.874 -11.056 -10.683 1.00 18.31 ?  33  THR   B HG22 1 
ATOM   4791 H HG23 . THR   B 1 33  ? 44.841 -10.296 -11.674 1.00 18.31 ?  33  THR   B HG23 1 
ATOM   4792 N N    . VAL   B 1 34  ? 45.016 -14.311 -10.107 1.00 11.99 ?  34  VAL   B N    1 
ATOM   4793 C CA   . VAL   B 1 34  ? 44.808 -14.708 -8.716  1.00 11.41 ?  34  VAL   B CA   1 
ATOM   4794 C C    . VAL   B 1 34  ? 45.229 -16.159 -8.543  1.00 10.51 ?  34  VAL   B C    1 
ATOM   4795 O O    . VAL   B 1 34  ? 44.709 -17.046 -9.232  1.00 11.33 ?  34  VAL   B O    1 
ATOM   4796 C CB   . VAL   B 1 34  ? 43.337 -14.560 -8.275  1.00 12.65 ?  34  VAL   B CB   1 
ATOM   4797 C CG1  . VAL   B 1 34  ? 43.165 -15.018 -6.827  1.00 12.71 ?  34  VAL   B CG1  1 
ATOM   4798 C CG2  . VAL   B 1 34  ? 42.852 -13.140 -8.462  1.00 13.64 ?  34  VAL   B CG2  1 
ATOM   4799 H H    . VAL   B 1 34  ? 44.754 -14.903 -10.676 1.00 14.54 ?  34  VAL   B H    1 
ATOM   4800 H HA   . VAL   B 1 34  ? 45.355 -14.155 -8.135  1.00 13.84 ?  34  VAL   B HA   1 
ATOM   4801 H HB   . VAL   B 1 34  ? 42.787 -15.132 -8.840  1.00 15.34 ?  34  VAL   B HB   1 
ATOM   4802 H HG11 . VAL   B 1 34  ? 42.311 -14.694 -6.495  1.00 15.40 ?  34  VAL   B HG11 1 
ATOM   4803 H HG12 . VAL   B 1 34  ? 43.179 -15.988 -6.796  1.00 15.40 ?  34  VAL   B HG12 1 
ATOM   4804 H HG13 . VAL   B 1 34  ? 43.885 -14.655 -6.294  1.00 15.40 ?  34  VAL   B HG13 1 
ATOM   4805 H HG21 . VAL   B 1 34  ? 41.929 -13.081 -8.162  1.00 16.51 ?  34  VAL   B HG21 1 
ATOM   4806 H HG22 . VAL   B 1 34  ? 43.409 -12.546 -7.943  1.00 16.51 ?  34  VAL   B HG22 1 
ATOM   4807 H HG23 . VAL   B 1 34  ? 42.904 -12.907 -9.405  1.00 16.51 ?  34  VAL   B HG23 1 
ATOM   4808 N N    . VAL   B 1 35  ? 46.132 -16.412 -7.595  1.00 9.97  ?  35  VAL   B N    1 
ATOM   4809 C CA   . VAL   B 1 35  ? 46.365 -17.756 -7.076  1.00 9.80  ?  35  VAL   B CA   1 
ATOM   4810 C C    . VAL   B 1 35  ? 45.817 -17.809 -5.659  1.00 9.41  ?  35  VAL   B C    1 
ATOM   4811 O O    . VAL   B 1 35  ? 46.036 -16.885 -4.868  1.00 9.89  ?  35  VAL   B O    1 
ATOM   4812 C CB   . VAL   B 1 35  ? 47.846 -18.199 -7.155  1.00 10.61 ?  35  VAL   B CB   1 
ATOM   4813 C CG1  . VAL   B 1 35  ? 48.752 -17.369 -6.249  1.00 11.40 ?  35  VAL   B CG1  1 
ATOM   4814 C CG2  . VAL   B 1 35  ? 47.977 -19.692 -6.837  1.00 11.27 ?  35  VAL   B CG2  1 
ATOM   4815 H H    . VAL   B 1 35  ? 46.628 -15.810 -7.230  1.00 12.11 ?  35  VAL   B H    1 
ATOM   4816 H HA   . VAL   B 1 35  ? 45.848 -18.382 -7.607  1.00 11.91 ?  35  VAL   B HA   1 
ATOM   4817 H HB   . VAL   B 1 35  ? 48.155 -18.085 -8.068  1.00 12.88 ?  35  VAL   B HB   1 
ATOM   4818 H HG11 . VAL   B 1 35  ? 49.676 -17.623 -6.416  1.00 13.83 ?  35  VAL   B HG11 1 
ATOM   4819 H HG12 . VAL   B 1 35  ? 48.619 -16.438 -6.447  1.00 13.83 ?  35  VAL   B HG12 1 
ATOM   4820 H HG13 . VAL   B 1 35  ? 48.524 -17.557 -5.323  1.00 13.83 ?  35  VAL   B HG13 1 
ATOM   4821 H HG21 . VAL   B 1 35  ? 48.897 -19.965 -6.938  1.00 13.68 ?  35  VAL   B HG21 1 
ATOM   4822 H HG22 . VAL   B 1 35  ? 47.684 -19.848 -5.920  1.00 13.68 ?  35  VAL   B HG22 1 
ATOM   4823 H HG23 . VAL   B 1 35  ? 47.411 -20.201 -7.445  1.00 13.68 ?  35  VAL   B HG23 1 
ATOM   4824 N N    . VAL   B 1 36  ? 45.097 -18.884 -5.345  1.00 9.71  ?  36  VAL   B N    1 
ATOM   4825 C CA   . VAL   B 1 36  ? 44.549 -19.087 -4.012  1.00 9.40  ?  36  VAL   B CA   1 
ATOM   4826 C C    . VAL   B 1 36  ? 45.555 -19.844 -3.157  1.00 8.84  ?  36  VAL   B C    1 
ATOM   4827 O O    . VAL   B 1 36  ? 46.096 -20.878 -3.572  1.00 10.20 ?  36  VAL   B O    1 
ATOM   4828 C CB   . VAL   B 1 36  ? 43.212 -19.843 -4.087  1.00 9.48  ?  36  VAL   B CB   1 
ATOM   4829 C CG1  . VAL   B 1 36  ? 42.696 -20.193 -2.699  1.00 10.46 ?  36  VAL   B CG1  1 
ATOM   4830 C CG2  . VAL   B 1 36  ? 42.194 -19.028 -4.856  1.00 10.43 ?  36  VAL   B CG2  1 
ATOM   4831 H H    . VAL   B 1 36  ? 44.916 -19.524 -5.893  1.00 11.80 ?  36  VAL   B H    1 
ATOM   4832 H HA   . VAL   B 1 36  ? 44.385 -18.231 -3.595  1.00 11.43 ?  36  VAL   B HA   1 
ATOM   4833 H HB   . VAL   B 1 36  ? 43.345 -20.676 -4.565  1.00 11.53 ?  36  VAL   B HB   1 
ATOM   4834 H HG11 . VAL   B 1 36  ? 41.759 -20.439 -2.765  1.00 12.71 ?  36  VAL   B HG11 1 
ATOM   4835 H HG12 . VAL   B 1 36  ? 43.208 -20.932 -2.345  1.00 12.71 ?  36  VAL   B HG12 1 
ATOM   4836 H HG13 . VAL   B 1 36  ? 42.788 -19.414 -2.126  1.00 12.71 ?  36  VAL   B HG13 1 
ATOM   4837 H HG21 . VAL   B 1 36  ? 41.347 -19.500 -4.868  1.00 12.67 ?  36  VAL   B HG21 1 
ATOM   4838 H HG22 . VAL   B 1 36  ? 42.088 -18.165 -4.429  1.00 12.67 ?  36  VAL   B HG22 1 
ATOM   4839 H HG23 . VAL   B 1 36  ? 42.513 -18.906 -5.769  1.00 12.67 ?  36  VAL   B HG23 1 
ATOM   4840 N N    . ASN   B 1 37  ? 45.772 -19.351 -1.944  1.00 9.11  ?  37  ASN   B N    1 
ATOM   4841 C CA   . ASN   B 1 37  ? 46.523 -20.075 -0.931  1.00 9.85  ?  37  ASN   B CA   1 
ATOM   4842 C C    . ASN   B 1 37  ? 45.568 -20.747 0.049   1.00 9.57  ?  37  ASN   B C    1 
ATOM   4843 O O    . ASN   B 1 37  ? 44.564 -20.157 0.465   1.00 10.37 ?  37  ASN   B O    1 
ATOM   4844 C CB   . ASN   B 1 37  ? 47.441 -19.126 -0.159  1.00 9.56  ?  37  ASN   B CB   1 
ATOM   4845 C CG   . ASN   B 1 37  ? 48.302 -19.842 0.846   1.00 9.95  ?  37  ASN   B CG   1 
ATOM   4846 O OD1  . ASN   B 1 37  ? 48.633 -21.020 0.675   1.00 10.87 ?  37  ASN   B OD1  1 
ATOM   4847 N ND2  . ASN   B 1 37  ? 48.653 -19.146 1.915   1.00 10.00 ?  37  ASN   B ND2  1 
ATOM   4848 H H    . ASN   B 1 37  ? 45.503 -18.579 -1.679  1.00 11.08 ?  37  ASN   B H    1 
ATOM   4849 H HA   . ASN   B 1 37  ? 47.066 -20.765 -1.346  1.00 11.98 ?  37  ASN   B HA   1 
ATOM   4850 H HB2  . ASN   B 1 37  ? 48.028 -18.684 -0.781  1.00 11.63 ?  37  ASN   B HB2  1 
ATOM   4851 H HB3  . ASN   B 1 37  ? 46.900 -18.482 0.320   1.00 11.63 ?  37  ASN   B HB3  1 
ATOM   4852 H HD21 . ASN   B 1 37  ? 49.147 -19.515 2.520   1.00 12.15 ?  37  ASN   B HD21 1 
ATOM   4853 H HD22 . ASN   B 1 37  ? 48.403 -18.339 2.004   1.00 12.15 ?  37  ASN   B HD22 1 
ATOM   4854 N N    . ALA   B 1 38  ? 45.915 -21.978 0.434   1.00 10.09 ?  38  ALA   B N    1 
ATOM   4855 C CA   . ALA   B 1 38  ? 45.259 -22.718 1.510   1.00 10.53 ?  38  ALA   B CA   1 
ATOM   4856 C C    . ALA   B 1 38  ? 45.844 -22.235 2.835   1.00 10.13 ?  38  ALA   B C    1 
ATOM   4857 O O    . ALA   B 1 38  ? 46.743 -22.848 3.425   1.00 11.17 ?  38  ALA   B O    1 
ATOM   4858 C CB   . ALA   B 1 38  ? 45.480 -24.212 1.324   1.00 11.55 ?  38  ALA   B CB   1 
ATOM   4859 H H    . ALA   B 1 38  ? 46.566 -22.413 0.085   1.00 12.26 ?  38  ALA   B H    1 
ATOM   4860 H HA   . ALA   B 1 38  ? 44.306 -22.537 1.504   1.00 12.79 ?  38  ALA   B HA   1 
ATOM   4861 H HB1  . ALA   B 1 38  ? 45.034 -24.691 2.047   1.00 14.01 ?  38  ALA   B HB1  1 
ATOM   4862 H HB2  . ALA   B 1 38  ? 45.101 -24.483 0.473   1.00 14.01 ?  38  ALA   B HB2  1 
ATOM   4863 H HB3  . ALA   B 1 38  ? 46.428 -24.400 1.342   1.00 14.01 ?  38  ALA   B HB3  1 
ATOM   4864 N N    . ALA   B 1 39  ? 45.330 -21.094 3.292   1.00 10.10 ?  39  ALA   B N    1 
ATOM   4865 C CA   . ALA   B 1 39  ? 45.886 -20.360 4.417   1.00 10.96 ?  39  ALA   B CA   1 
ATOM   4866 C C    . ALA   B 1 39  ? 45.269 -20.800 5.744   1.00 10.69 ?  39  ALA   B C    1 
ATOM   4867 O O    . ALA   B 1 39  ? 44.233 -21.463 5.795   1.00 11.49 ?  39  ALA   B O    1 
ATOM   4868 C CB   . ALA   B 1 39  ? 45.658 -18.859 4.215   1.00 10.88 ?  39  ALA   B CB   1 
ATOM   4869 H H    . ALA   B 1 39  ? 44.634 -20.717 2.947   1.00 12.27 ?  39  ALA   B H    1 
ATOM   4870 H HA   . ALA   B 1 39  ? 46.837 -20.520 4.457   1.00 13.30 ?  39  ALA   B HA   1 
ATOM   4871 H HB1  . ALA   B 1 39  ? 46.035 -18.376 4.968   1.00 13.21 ?  39  ALA   B HB1  1 
ATOM   4872 H HB2  . ALA   B 1 39  ? 46.100 -18.575 3.393   1.00 13.21 ?  39  ALA   B HB2  1 
ATOM   4873 H HB3  . ALA   B 1 39  ? 44.707 -18.680 4.151   1.00 13.21 ?  39  ALA   B HB3  1 
ATOM   4874 N N    . ASN   B 1 40  ? 45.912 -20.380 6.828   1.00 11.34 ?  40  ASN   B N    1 
ATOM   4875 C CA   . ASN   B 1 40  ? 45.351 -20.425 8.167   1.00 12.03 ?  40  ASN   B CA   1 
ATOM   4876 C C    . ASN   B 1 40  ? 45.167 -18.997 8.693   1.00 11.48 ?  40  ASN   B C    1 
ATOM   4877 O O    . ASN   B 1 40  ? 45.574 -18.016 8.057   1.00 11.59 ?  40  ASN   B O    1 
ATOM   4878 C CB   . ASN   B 1 40  ? 46.201 -21.305 9.096   1.00 12.60 ?  40  ASN   B CB   1 
ATOM   4879 C CG   . ASN   B 1 40  ? 47.654 -20.889 9.137   1.00 14.05 ?  40  ASN   B CG   1 
ATOM   4880 O OD1  . ASN   B 1 40  ? 47.967 -19.705 9.182   1.00 16.20 ?  40  ASN   B OD1  1 
ATOM   4881 N ND2  . ASN   B 1 40  ? 48.553 -21.863 9.119   1.00 14.05 ?  40  ASN   B ND2  1 
ATOM   4882 H H    . ASN   B 1 40  ? 46.702 -20.045 6.798   1.00 13.76 ?  40  ASN   B H    1 
ATOM   4883 H HA   . ASN   B 1 40  ? 44.471 -20.825 8.117   1.00 14.59 ?  40  ASN   B HA   1 
ATOM   4884 H HB2  . ASN   B 1 40  ? 45.842 -21.242 9.996   1.00 15.28 ?  40  ASN   B HB2  1 
ATOM   4885 H HB3  . ASN   B 1 40  ? 46.158 -22.220 8.785   1.00 15.28 ?  40  ASN   B HB3  1 
ATOM   4886 H HD21 . ASN   B 1 40  ? 49.393 -21.679 9.152   1.00 17.02 ?  40  ASN   B HD21 1 
ATOM   4887 H HD22 . ASN   B 1 40  ? 48.295 -22.683 9.088   1.00 17.02 ?  40  ASN   B HD22 1 
ATOM   4888 N N    . VAL   B 1 41  ? 44.511 -18.871 9.850   1.00 12.11 ?  41  VAL   B N    1 
ATOM   4889 C CA   . VAL   B 1 41  ? 44.050 -17.551 10.294  1.00 12.56 ?  41  VAL   B CA   1 
ATOM   4890 C C    . VAL   B 1 41  ? 45.201 -16.594 10.576  1.00 12.33 ?  41  VAL   B C    1 
ATOM   4891 O O    . VAL   B 1 41  ? 45.025 -15.374 10.489  1.00 12.48 ?  41  VAL   B O    1 
ATOM   4892 C CB   . VAL   B 1 41  ? 43.079 -17.623 11.492  1.00 14.01 ?  41  VAL   B CB   1 
ATOM   4893 C CG1  . VAL   B 1 41  ? 41.763 -18.291 11.103  1.00 14.84 ?  41  VAL   B CG1  1 
ATOM   4894 C CG2  . VAL   B 1 41  ? 43.727 -18.301 12.689  1.00 14.98 ?  41  VAL   B CG2  1 
ATOM   4895 H H    . VAL   B 1 41  ? 44.321 -19.520 10.379  1.00 14.68 ?  41  VAL   B H    1 
ATOM   4896 H HA   . VAL   B 1 41  ? 43.542 -17.164 9.564   1.00 15.23 ?  41  VAL   B HA   1 
ATOM   4897 H HB   . VAL   B 1 41  ? 42.863 -16.716 11.763  1.00 16.97 ?  41  VAL   B HB   1 
ATOM   4898 H HG11 . VAL   B 1 41  ? 41.168 -18.293 11.872  1.00 17.96 ?  41  VAL   B HG11 1 
ATOM   4899 H HG12 . VAL   B 1 41  ? 41.357 -17.791 10.377  1.00 17.96 ?  41  VAL   B HG12 1 
ATOM   4900 H HG13 . VAL   B 1 41  ? 41.940 -19.200 10.821  1.00 17.96 ?  41  VAL   B HG13 1 
ATOM   4901 H HG21 . VAL   B 1 41  ? 43.090 -18.333 13.420  1.00 18.13 ?  41  VAL   B HG21 1 
ATOM   4902 H HG22 . VAL   B 1 41  ? 43.983 -19.205 12.438  1.00 18.13 ?  41  VAL   B HG22 1 
ATOM   4903 H HG23 . VAL   B 1 41  ? 44.510 -17.797 12.952  1.00 18.13 ?  41  VAL   B HG23 1 
ATOM   4904 N N    . TYR   B 1 42  ? 46.369 -17.108 10.956  1.00 12.75 ?  42  TYR   B N    1 
ATOM   4905 C CA   . TYR   B 1 42  ? 47.518 -16.259 11.234  1.00 13.14 ?  42  TYR   B CA   1 
ATOM   4906 C C    . TYR   B 1 42  ? 48.487 -16.183 10.056  1.00 12.43 ?  42  TYR   B C    1 
ATOM   4907 O O    . TYR   B 1 42  ? 49.574 -15.605 10.193  1.00 13.42 ?  42  TYR   B O    1 
ATOM   4908 C CB   . TYR   B 1 42  ? 48.203 -16.671 12.546  1.00 15.14 ?  42  TYR   B CB   1 
ATOM   4909 C CG   . TYR   B 1 42  ? 47.626 -15.957 13.770  1.00 15.05 ?  42  TYR   B CG   1 
ATOM   4910 C CD1  . TYR   B 1 42  ? 47.866 -14.603 13.976  1.00 13.91 ?  42  TYR   B CD1  1 
ATOM   4911 C CD2  . TYR   B 1 42  ? 46.854 -16.628 14.714  1.00 16.37 ?  42  TYR   B CD2  1 
ATOM   4912 C CE1  . TYR   B 1 42  ? 47.358 -13.936 15.066  1.00 14.56 ?  42  TYR   B CE1  1 
ATOM   4913 C CE2  . TYR   B 1 42  ? 46.340 -15.963 15.825  1.00 16.23 ?  42  TYR   B CE2  1 
ATOM   4914 C CZ   . TYR   B 1 42  ? 46.601 -14.611 15.993  1.00 16.14 ?  42  TYR   B CZ   1 
ATOM   4915 O OH   . TYR   B 1 42  ? 46.117 -13.915 17.084  1.00 18.57 ?  42  TYR   B OH   1 
ATOM   4916 H H    . TYR   B 1 42  ? 46.519 -17.952 11.057  1.00 15.45 ?  42  TYR   B H    1 
ATOM   4917 H HA   . TYR   B 1 42  ? 47.187 -15.360 11.371  1.00 15.92 ?  42  TYR   B HA   1 
ATOM   4918 H HB2  . TYR   B 1 42  ? 48.091 -17.624 12.676  1.00 18.31 ?  42  TYR   B HB2  1 
ATOM   4919 H HB3  . TYR   B 1 42  ? 49.146 -16.452 12.487  1.00 18.31 ?  42  TYR   B HB3  1 
ATOM   4920 H HD1  . TYR   B 1 42  ? 48.384 -14.136 13.355  1.00 16.84 ?  42  TYR   B HD1  1 
ATOM   4921 H HD2  . TYR   B 1 42  ? 46.678 -17.535 14.598  1.00 19.79 ?  42  TYR   B HD2  1 
ATOM   4922 H HE1  . TYR   B 1 42  ? 47.541 -13.029 15.184  1.00 17.62 ?  42  TYR   B HE1  1 
ATOM   4923 H HE2  . TYR   B 1 42  ? 45.823 -16.420 16.448  1.00 19.63 ?  42  TYR   B HE2  1 
ATOM   4924 H HH   . TYR   B 1 42  ? 46.363 -13.114 17.045  1.00 22.43 ?  42  TYR   B HH   1 
ATOM   4925 N N    . LEU   B 1 43  ? 48.093 -16.706 8.894   1.00 11.29 ?  43  LEU   B N    1 
ATOM   4926 C CA   . LEU   B 1 43  ? 48.907 -16.640 7.684   1.00 11.27 ?  43  LEU   B CA   1 
ATOM   4927 C C    . LEU   B 1 43  ? 50.322 -17.148 7.939   1.00 11.29 ?  43  LEU   B C    1 
ATOM   4928 O O    . LEU   B 1 43  ? 51.303 -16.550 7.496   1.00 12.33 ?  43  LEU   B O    1 
ATOM   4929 C CB   . LEU   B 1 43  ? 48.924 -15.238 7.068   1.00 11.42 ?  43  LEU   B CB   1 
ATOM   4930 C CG   . LEU   B 1 43  ? 47.569 -14.620 6.707   1.00 11.68 ?  43  LEU   B CG   1 
ATOM   4931 C CD1  . LEU   B 1 43  ? 47.785 -13.226 6.139   1.00 13.12 ?  43  LEU   B CD1  1 
ATOM   4932 C CD2  . LEU   B 1 43  ? 46.804 -15.500 5.738   1.00 12.02 ?  43  LEU   B CD2  1 
ATOM   4933 H H    . LEU   B 1 43  ? 47.349 -17.130 8.784   1.00 13.70 ?  43  LEU   B H    1 
ATOM   4934 H HA   . LEU   B 1 43  ? 48.512 -17.239 7.024   1.00 13.68 ?  43  LEU   B HA   1 
ATOM   4935 H HB2  . LEU   B 1 43  ? 49.353 -14.642 7.694   1.00 13.86 ?  43  LEU   B HB2  1 
ATOM   4936 H HB3  . LEU   B 1 43  ? 49.444 -15.279 6.249   1.00 13.86 ?  43  LEU   B HB3  1 
ATOM   4937 H HG   . LEU   B 1 43  ? 47.040 -14.539 7.513   1.00 14.16 ?  43  LEU   B HG   1 
ATOM   4938 H HD11 . LEU   B 1 43  ? 46.924 -12.838 5.914   1.00 15.89 ?  43  LEU   B HD11 1 
ATOM   4939 H HD12 . LEU   B 1 43  ? 48.226 -12.677 6.810   1.00 15.89 ?  43  LEU   B HD12 1 
ATOM   4940 H HD13 . LEU   B 1 43  ? 48.339 -13.285 5.346   1.00 15.89 ?  43  LEU   B HD13 1 
ATOM   4941 H HD21 . LEU   B 1 43  ? 45.999 -15.036 5.459   1.00 14.57 ?  43  LEU   B HD21 1 
ATOM   4942 H HD22 . LEU   B 1 43  ? 47.363 -15.686 4.967   1.00 14.57 ?  43  LEU   B HD22 1 
ATOM   4943 H HD23 . LEU   B 1 43  ? 46.568 -16.332 6.182   1.00 14.57 ?  43  LEU   B HD23 1 
ATOM   4944 N N    . LYS   B 1 44  ? 50.425 -18.273 8.648   1.00 11.38 ?  44  LYS   B N    1 
ATOM   4945 C CA   . LYS   B 1 44  ? 51.692 -18.949 8.894   1.00 12.35 ?  44  LYS   B CA   1 
ATOM   4946 C C    . LYS   B 1 44  ? 51.808 -20.072 7.874   1.00 11.75 ?  44  LYS   B C    1 
ATOM   4947 O O    . LYS   B 1 44  ? 51.109 -21.085 7.969   1.00 13.24 ?  44  LYS   B O    1 
ATOM   4948 C CB   . LYS   B 1 44  ? 51.734 -19.463 10.329  1.00 14.05 ?  44  LYS   B CB   1 
ATOM   4949 C CG   . LYS   B 1 44  ? 51.943 -18.341 11.344  1.00 17.02 ?  44  LYS   B CG   1 
ATOM   4950 C CD   . LYS   B 1 44  ? 53.150 -17.497 10.921  1.00 20.67 ?  44  LYS   B CD   1 
ATOM   4951 C CE   . LYS   B 1 44  ? 53.734 -16.661 12.028  1.00 24.09 ?  44  LYS   B CE   1 
ATOM   4952 N NZ   . LYS   B 1 44  ? 54.873 -15.828 11.579  1.00 25.10 ?  44  LYS   B NZ   1 
ATOM   4953 H H    . LYS   B 1 44  ? 49.752 -18.668 9.007   1.00 13.81 ?  44  LYS   B H    1 
ATOM   4954 H HA   . LYS   B 1 44  ? 52.424 -18.342 8.728   1.00 14.97 ?  44  LYS   B HA   1 
ATOM   4955 H HB2  . LYS   B 1 44  ? 50.883 -19.899 10.534  1.00 17.01 ?  44  LYS   B HB2  1 
ATOM   4956 H HB3  . LYS   B 1 44  ? 52.457 -20.098 10.422  1.00 17.01 ?  44  LYS   B HB3  1 
ATOM   4957 H HG2  . LYS   B 1 44  ? 51.157 -17.775 11.373  1.00 20.58 ?  44  LYS   B HG2  1 
ATOM   4958 H HG3  . LYS   B 1 44  ? 52.124 -18.725 12.218  1.00 20.58 ?  44  LYS   B HG3  1 
ATOM   4959 H HD2  . LYS   B 1 44  ? 53.837 -18.098 10.578  1.00 24.96 ?  44  LYS   B HD2  1 
ATOM   4960 H HD3  . LYS   B 1 44  ? 52.864 -16.894 10.215  1.00 24.96 ?  44  LYS   B HD3  1 
ATOM   4961 H HE2  . LYS   B 1 44  ? 53.056 -16.044 12.309  1.00 29.06 ?  44  LYS   B HE2  1 
ATOM   4962 H HE3  . LYS   B 1 44  ? 54.018 -17.236 12.760  1.00 29.06 ?  44  LYS   B HE3  1 
ATOM   4963 H HZ1  . LYS   B 1 44  ? 55.180 -15.345 12.260  1.00 30.27 ?  44  LYS   B HZ1  1 
ATOM   4964 H HZ2  . LYS   B 1 44  ? 55.526 -16.339 11.264  1.00 30.27 ?  44  LYS   B HZ2  1 
ATOM   4965 H HZ3  . LYS   B 1 44  ? 54.602 -15.273 10.933  1.00 30.27 ?  44  LYS   B HZ3  1 
ATOM   4966 N N    . HIS   B 1 45  ? 52.660 -19.864 6.873   1.00 11.44 ?  45  HIS   B N    1 
ATOM   4967 C CA   . HIS   B 1 45  ? 52.670 -20.695 5.671   1.00 11.75 ?  45  HIS   B CA   1 
ATOM   4968 C C    . HIS   B 1 45  ? 53.684 -21.821 5.833   1.00 13.98 ?  45  HIS   B C    1 
ATOM   4969 O O    . HIS   B 1 45  ? 54.753 -21.837 5.229   1.00 16.87 ?  45  HIS   B O    1 
ATOM   4970 C CB   . HIS   B 1 45  ? 52.994 -19.839 4.459   1.00 11.78 ?  45  HIS   B CB   1 
ATOM   4971 C CG   . HIS   B 1 45  ? 52.130 -18.632 4.348   1.00 11.72 ?  45  HIS   B CG   1 
ATOM   4972 N ND1  . HIS   B 1 45  ? 50.752 -18.703 4.314   1.00 11.77 ?  45  HIS   B ND1  1 
ATOM   4973 C CD2  . HIS   B 1 45  ? 52.455 -17.321 4.270   1.00 12.54 ?  45  HIS   B CD2  1 
ATOM   4974 C CE1  . HIS   B 1 45  ? 50.273 -17.475 4.214   1.00 11.42 ?  45  HIS   B CE1  1 
ATOM   4975 N NE2  . HIS   B 1 45  ? 51.281 -16.620 4.185   1.00 12.04 ?  45  HIS   B NE2  1 
ATOM   4976 H H    . HIS   B 1 45  ? 53.242 -19.230 6.858   1.00 13.88 ?  45  HIS   B H    1 
ATOM   4977 H HA   . HIS   B 1 45  ? 51.788 -21.088 5.540   1.00 14.25 ?  45  HIS   B HA   1 
ATOM   4978 H HB2  . HIS   B 1 45  ? 53.914 -19.548 4.516   1.00 14.28 ?  45  HIS   B HB2  1 
ATOM   4979 H HB3  . HIS   B 1 45  ? 52.869 -20.376 3.653   1.00 14.28 ?  45  HIS   B HB3  1 
ATOM   4980 H HD2  . HIS   B 1 45  ? 53.314 -16.962 4.275   1.00 15.19 ?  45  HIS   B HD2  1 
ATOM   4981 H HE1  . HIS   B 1 45  ? 49.372 -17.249 4.164   1.00 13.86 ?  45  HIS   B HE1  1 
ATOM   4982 H HE2  . HIS   B 1 45  ? 51.211 -15.765 4.129   1.00 14.60 ?  45  HIS   B HE2  1 
ATOM   4983 N N    A GLY   B 1 46  ? 53.311 -22.791 6.663   0.34 15.17 ?  46  GLY   B N    1 
ATOM   4984 N N    B GLY   B 1 46  ? 53.319 -22.786 6.667   0.66 14.91 ?  46  GLY   B N    1 
ATOM   4985 C CA   A GLY   B 1 46  ? 54.228 -23.844 7.050   0.34 16.77 ?  46  GLY   B CA   1 
ATOM   4986 C CA   B GLY   B 1 46  ? 54.249 -23.840 7.020   0.66 16.80 ?  46  GLY   B CA   1 
ATOM   4987 C C    A GLY   B 1 46  ? 54.277 -25.055 6.138   0.34 18.24 ?  46  GLY   B C    1 
ATOM   4988 C C    B GLY   B 1 46  ? 54.277 -25.038 6.091   0.66 18.52 ?  46  GLY   B C    1 
ATOM   4989 O O    A GLY   B 1 46  ? 55.359 -25.470 5.712   0.34 20.23 ?  46  GLY   B O    1 
ATOM   4990 O O    B GLY   B 1 46  ? 55.344 -25.431 5.607   0.66 21.52 ?  46  GLY   B O    1 
ATOM   4991 H H    A GLY   B 1 46  ? 52.530 -22.848 7.024   0.34 18.36 ?  46  GLY   B H    1 
ATOM   4992 H H    B GLY   B 1 46  ? 52.549 -22.837 7.052   0.66 18.04 ?  46  GLY   B H    1 
ATOM   4993 H HA2  A GLY   B 1 46  ? 55.123 -23.474 7.099   0.34 20.28 ?  46  GLY   B HA2  1 
ATOM   4994 H HA2  B GLY   B 1 46  ? 55.145 -23.467 7.052   0.66 20.32 ?  46  GLY   B HA2  1 
ATOM   4995 H HA3  A GLY   B 1 46  ? 53.987 -24.153 7.938   0.34 20.28 ?  46  GLY   B HA3  1 
ATOM   4996 H HA3  B GLY   B 1 46  ? 54.031 -24.165 7.906   0.66 20.32 ?  46  GLY   B HA3  1 
ATOM   4997 N N    . GLY   B 1 47  ? 53.120 -25.646 5.836   1.00 18.14 ?  47  GLY   B N    1 
ATOM   4998 C CA   . GLY   B 1 47  ? 53.065 -26.922 5.150   1.00 15.92 ?  47  GLY   B CA   1 
ATOM   4999 C C    . GLY   B 1 47  ? 52.152 -26.903 3.941   1.00 13.76 ?  47  GLY   B C    1 
ATOM   5000 O O    . GLY   B 1 47  ? 51.506 -25.899 3.647   1.00 13.89 ?  47  GLY   B O    1 
ATOM   5001 H H    A GLY   B 1 47  ? 52.345 -25.319 6.028   0.34 21.92 ?  47  GLY   B H    1 
ATOM   5002 H H    B GLY   B 1 47  ? 52.348 -25.337 6.066   0.66 21.92 ?  47  GLY   B H    1 
ATOM   5003 H HA2  . GLY   B 1 47  ? 53.948 -27.174 4.847   1.00 19.25 ?  47  GLY   B HA2  1 
ATOM   5004 H HA3  . GLY   B 1 47  ? 52.744 -27.600 5.762   1.00 19.25 ?  47  GLY   B HA3  1 
ATOM   5005 N N    . GLY   B 1 48  ? 52.100 -28.048 3.261   1.00 12.84 ?  48  GLY   B N    1 
ATOM   5006 C CA   . GLY   B 1 48  ? 51.192 -28.193 2.138   1.00 12.88 ?  48  GLY   B CA   1 
ATOM   5007 C C    . GLY   B 1 48  ? 51.326 -27.072 1.133   1.00 12.08 ?  48  GLY   B C    1 
ATOM   5008 O O    . GLY   B 1 48  ? 52.429 -26.607 0.826   1.00 12.63 ?  48  GLY   B O    1 
ATOM   5009 H H    . GLY   B 1 48  ? 52.569 -28.747 3.430   1.00 15.56 ?  48  GLY   B H    1 
ATOM   5010 H HA2  . GLY   B 1 48  ? 51.372 -29.037 1.682   1.00 15.60 ?  48  GLY   B HA2  1 
ATOM   5011 H HA3  . GLY   B 1 48  ? 50.277 -28.210 2.452   1.00 15.60 ?  48  GLY   B HA3  1 
ATOM   5012 N N    . VAL   B 1 49  ? 50.181 -26.630 0.609   1.00 11.88 ?  49  VAL   B N    1 
ATOM   5013 C CA   . VAL   B 1 49  ? 50.175 -25.607 -0.434  1.00 11.85 ?  49  VAL   B CA   1 
ATOM   5014 C C    . VAL   B 1 49  ? 50.840 -24.321 0.051   1.00 10.65 ?  49  VAL   B C    1 
ATOM   5015 O O    . VAL   B 1 49  ? 51.630 -23.700 -0.673  1.00 11.53 ?  49  VAL   B O    1 
ATOM   5016 C CB   . VAL   B 1 49  ? 48.735 -25.355 -0.922  1.00 12.95 ?  49  VAL   B CB   1 
ATOM   5017 C CG1  . VAL   B 1 49  ? 48.668 -24.114 -1.805  1.00 13.26 ?  49  VAL   B CG1  1 
ATOM   5018 C CG2  . VAL   B 1 49  ? 48.200 -26.571 -1.664  1.00 14.24 ?  49  VAL   B CG2  1 
ATOM   5019 H H    . VAL   B 1 49  ? 49.395 -26.887 0.852   1.00 14.41 ?  49  VAL   B H    1 
ATOM   5020 H HA   . VAL   B 1 49  ? 50.683 -25.933 -1.191  1.00 14.37 ?  49  VAL   B HA   1 
ATOM   5021 H HB   . VAL   B 1 49  ? 48.163 -25.201 -0.155  1.00 15.69 ?  49  VAL   B HB   1 
ATOM   5022 H HG11 . VAL   B 1 49  ? 47.837 -24.129 -2.309  1.00 16.06 ?  49  VAL   B HG11 1 
ATOM   5023 H HG12 . VAL   B 1 49  ? 48.695 -23.321 -1.245  1.00 16.06 ?  49  VAL   B HG12 1 
ATOM   5024 H HG13 . VAL   B 1 49  ? 49.421 -24.117 -2.416  1.00 16.06 ?  49  VAL   B HG13 1 
ATOM   5025 H HG21 . VAL   B 1 49  ? 47.293 -26.390 -1.961  1.00 17.23 ?  49  VAL   B HG21 1 
ATOM   5026 H HG22 . VAL   B 1 49  ? 48.767 -26.748 -2.433  1.00 17.23 ?  49  VAL   B HG22 1 
ATOM   5027 H HG23 . VAL   B 1 49  ? 48.206 -27.334 -1.067  1.00 17.23 ?  49  VAL   B HG23 1 
ATOM   5028 N N    . ALA   B 1 50  ? 50.494 -23.873 1.259   1.00 10.80 ?  50  ALA   B N    1 
ATOM   5029 C CA   . ALA   B 1 50  ? 51.018 -22.595 1.738   1.00 10.73 ?  50  ALA   B CA   1 
ATOM   5030 C C    . ALA   B 1 50  ? 52.535 -22.633 1.847   1.00 10.68 ?  50  ALA   B C    1 
ATOM   5031 O O    . ALA   B 1 50  ? 53.221 -21.671 1.477   1.00 10.96 ?  50  ALA   B O    1 
ATOM   5032 C CB   . ALA   B 1 50  ? 50.392 -22.244 3.083   1.00 11.38 ?  50  ALA   B CB   1 
ATOM   5033 H H    . ALA   B 1 50  ? 49.969 -24.275 1.806   1.00 13.11 ?  50  ALA   B H    1 
ATOM   5034 H HA   . ALA   B 1 50  ? 50.791 -21.898 1.110   1.00 13.02 ?  50  ALA   B HA   1 
ATOM   5035 H HB1  . ALA   B 1 50  ? 50.748 -21.393 3.388   1.00 13.81 ?  50  ALA   B HB1  1 
ATOM   5036 H HB2  . ALA   B 1 50  ? 49.428 -22.173 2.973   1.00 13.81 ?  50  ALA   B HB2  1 
ATOM   5037 H HB3  . ALA   B 1 50  ? 50.599 -22.938 3.726   1.00 13.81 ?  50  ALA   B HB3  1 
ATOM   5038 N N    . GLY   B 1 51  ? 53.079 -23.735 2.358   1.00 11.57 ?  51  GLY   B N    1 
ATOM   5039 C CA   . GLY   B 1 51  ? 54.522 -23.851 2.432   1.00 12.66 ?  51  GLY   B CA   1 
ATOM   5040 C C    . GLY   B 1 51  ? 55.173 -23.796 1.066   1.00 12.13 ?  51  GLY   B C    1 
ATOM   5041 O O    . GLY   B 1 51  ? 56.219 -23.165 0.892   1.00 13.07 ?  51  GLY   B O    1 
ATOM   5042 H H    . GLY   B 1 51  ? 52.645 -24.419 2.660   1.00 14.03 ?  51  GLY   B H    1 
ATOM   5043 H HA2  . GLY   B 1 51  ? 54.878 -23.126 2.968   1.00 15.34 ?  51  GLY   B HA2  1 
ATOM   5044 H HA3  . GLY   B 1 51  ? 54.762 -24.692 2.855   1.00 15.34 ?  51  GLY   B HA3  1 
ATOM   5045 N N    . ALA   B 1 52  ? 54.570 -24.460 0.079   1.00 11.64 ?  52  ALA   B N    1 
ATOM   5046 C CA   . ALA   B 1 52  ? 55.136 -24.467 -1.264  1.00 11.84 ?  52  ALA   B CA   1 
ATOM   5047 C C    . ALA   B 1 52  ? 55.058 -23.087 -1.912  1.00 11.28 ?  52  ALA   B C    1 
ATOM   5048 O O    . ALA   B 1 52  ? 56.026 -22.637 -2.541  1.00 12.02 ?  52  ALA   B O    1 
ATOM   5049 C CB   . ALA   B 1 52  ? 54.421 -25.507 -2.119  1.00 12.49 ?  52  ALA   B CB   1 
ATOM   5050 H H    . ALA   B 1 52  ? 53.828 -24.896 0.157   1.00 14.12 ?  52  ALA   B H    1 
ATOM   5051 H HA   . ALA   B 1 52  ? 56.071 -24.715 -1.204  1.00 14.36 ?  52  ALA   B HA   1 
ATOM   5052 H HB1  . ALA   B 1 52  ? 54.815 -25.503 -3.008  1.00 15.14 ?  52  ALA   B HB1  1 
ATOM   5053 H HB2  . ALA   B 1 52  ? 54.537 -26.379 -1.713  1.00 15.14 ?  52  ALA   B HB2  1 
ATOM   5054 H HB3  . ALA   B 1 52  ? 53.483 -25.282 -2.171  1.00 15.14 ?  52  ALA   B HB3  1 
ATOM   5055 N N    . LEU   B 1 53  ? 53.915 -22.402 -1.788  1.00 11.19 ?  53  LEU   B N    1 
ATOM   5056 C CA   . LEU   B 1 53  ? 53.810 -21.062 -2.358  1.00 11.04 ?  53  LEU   B CA   1 
ATOM   5057 C C    . LEU   B 1 53  ? 54.821 -20.122 -1.711  1.00 11.09 ?  53  LEU   B C    1 
ATOM   5058 O O    . LEU   B 1 53  ? 55.526 -19.373 -2.399  1.00 12.04 ?  53  LEU   B O    1 
ATOM   5059 C CB   . LEU   B 1 53  ? 52.386 -20.516 -2.192  1.00 11.65 ?  53  LEU   B CB   1 
ATOM   5060 C CG   . LEU   B 1 53  ? 51.250 -21.245 -2.923  1.00 11.98 ?  53  LEU   B CG   1 
ATOM   5061 C CD1  . LEU   B 1 53  ? 49.908 -20.631 -2.577  1.00 13.06 ?  53  LEU   B CD1  1 
ATOM   5062 C CD2  . LEU   B 1 53  ? 51.456 -21.225 -4.431  1.00 13.68 ?  53  LEU   B CD2  1 
ATOM   5063 H H    . LEU   B 1 53  ? 53.211 -22.685 -1.386  1.00 13.58 ?  53  LEU   B H    1 
ATOM   5064 H HA   . LEU   B 1 53  ? 54.009 -21.112 -3.310  1.00 13.40 ?  53  LEU   B HA   1 
ATOM   5065 H HB2  . LEU   B 1 53  ? 52.171 -20.542 -1.249  1.00 14.14 ?  53  LEU   B HB2  1 
ATOM   5066 H HB3  . LEU   B 1 53  ? 52.380 -19.606 -2.504  1.00 14.14 ?  53  LEU   B HB3  1 
ATOM   5067 H HG   . LEU   B 1 53  ? 51.229 -22.175 -2.641  1.00 14.52 ?  53  LEU   B HG   1 
ATOM   5068 H HD11 . LEU   B 1 53  ? 49.205 -21.112 -3.051  1.00 15.82 ?  53  LEU   B HD11 1 
ATOM   5069 H HD12 . LEU   B 1 53  ? 49.762 -20.707 -1.619  1.00 15.82 ?  53  LEU   B HD12 1 
ATOM   5070 H HD13 . LEU   B 1 53  ? 49.905 -19.701 -2.841  1.00 15.82 ?  53  LEU   B HD13 1 
ATOM   5071 H HD21 . LEU   B 1 53  ? 50.757 -21.745 -4.857  1.00 16.57 ?  53  LEU   B HD21 1 
ATOM   5072 H HD22 . LEU   B 1 53  ? 51.414 -20.305 -4.742  1.00 16.57 ?  53  LEU   B HD22 1 
ATOM   5073 H HD23 . LEU   B 1 53  ? 52.323 -21.605 -4.641  1.00 16.57 ?  53  LEU   B HD23 1 
ATOM   5074 N N    . ASN   B 1 54  ? 54.906 -20.145 -0.383  1.00 10.72 ?  54  ASN   B N    1 
ATOM   5075 C CA   . ASN   B 1 54  ? 55.828 -19.240 0.288   1.00 11.26 ?  54  ASN   B CA   1 
ATOM   5076 C C    . ASN   B 1 54  ? 57.272 -19.527 -0.109  1.00 11.96 ?  54  ASN   B C    1 
ATOM   5077 O O    . ASN   B 1 54  ? 58.050 -18.596 -0.348  1.00 12.01 ?  54  ASN   B O    1 
ATOM   5078 C CB   . ASN   B 1 54  ? 55.663 -19.319 1.799   1.00 12.21 ?  54  ASN   B CB   1 
ATOM   5079 C CG   . ASN   B 1 54  ? 56.635 -18.402 2.512   1.00 12.44 ?  54  ASN   B CG   1 
ATOM   5080 O OD1  . ASN   B 1 54  ? 56.647 -17.195 2.266   1.00 12.82 ?  54  ASN   B OD1  1 
ATOM   5081 N ND2  . ASN   B 1 54  ? 57.473 -18.966 3.374   1.00 14.05 ?  54  ASN   B ND2  1 
ATOM   5082 H H    . ASN   B 1 54  ? 54.455 -20.662 0.134   1.00 13.02 ?  54  ASN   B H    1 
ATOM   5083 H HA   . ASN   B 1 54  ? 55.618 -18.332 0.014   1.00 13.66 ?  54  ASN   B HA   1 
ATOM   5084 H HB2  . ASN   B 1 54  ? 54.760 -19.044 2.038   1.00 14.80 ?  54  ASN   B HB2  1 
ATOM   5085 H HB3  . ASN   B 1 54  ? 55.828 -20.223 2.095   1.00 14.80 ?  54  ASN   B HB3  1 
ATOM   5086 H HD21 . ASN   B 1 54  ? 58.047 -18.484 3.797   1.00 17.01 ?  54  ASN   B HD21 1 
ATOM   5087 H HD22 . ASN   B 1 54  ? 57.443 -19.816 3.514   1.00 17.01 ?  54  ASN   B HD22 1 
ATOM   5088 N N    . LYS   B 1 55  ? 57.653 -20.807 -0.174  1.00 12.60 ?  55  LYS   B N    1 
ATOM   5089 C CA   . LYS   B 1 55  ? 59.011 -21.153 -0.589  1.00 13.63 ?  55  LYS   B CA   1 
ATOM   5090 C C    . LYS   B 1 55  ? 59.312 -20.612 -1.981  1.00 13.48 ?  55  LYS   B C    1 
ATOM   5091 O O    . LYS   B 1 55  ? 60.413 -20.107 -2.233  1.00 14.08 ?  55  LYS   B O    1 
ATOM   5092 C CB   . LYS   B 1 55  ? 59.187 -22.672 -0.541  1.00 15.12 ?  55  LYS   B CB   1 
ATOM   5093 C CG   . LYS   B 1 55  ? 60.544 -23.161 -0.999  1.00 18.98 ?  55  LYS   B CG   1 
ATOM   5094 C CD   . LYS   B 1 55  ? 60.696 -24.663 -0.788  1.00 22.81 ?  55  LYS   B CD   1 
ATOM   5095 C CE   . LYS   B 1 55  ? 60.796 -25.021 0.694   1.00 26.08 ?  55  LYS   B CE   1 
ATOM   5096 N NZ   . LYS   B 1 55  ? 61.129 -26.449 0.916   1.00 27.71 ?  55  LYS   B NZ   1 
ATOM   5097 H H    . LYS   B 1 55  ? 57.153 -21.475 0.011   1.00 15.27 ?  55  LYS   B H    1 
ATOM   5098 H HA   . LYS   B 1 55  ? 59.644 -20.756 0.028   1.00 16.51 ?  55  LYS   B HA   1 
ATOM   5099 H HB2  . LYS   B 1 55  ? 59.057 -22.962 0.376   1.00 18.29 ?  55  LYS   B HB2  1 
ATOM   5100 H HB3  . LYS   B 1 55  ? 58.517 -23.080 -1.110  1.00 18.29 ?  55  LYS   B HB3  1 
ATOM   5101 H HG2  . LYS   B 1 55  ? 60.649 -22.975 -1.947  1.00 22.93 ?  55  LYS   B HG2  1 
ATOM   5102 H HG3  . LYS   B 1 55  ? 61.236 -22.708 -0.491  1.00 22.93 ?  55  LYS   B HG3  1 
ATOM   5103 H HD2  . LYS   B 1 55  ? 59.924 -25.119 -1.158  1.00 27.53 ?  55  LYS   B HD2  1 
ATOM   5104 H HD3  . LYS   B 1 55  ? 61.507 -24.968 -1.227  1.00 27.53 ?  55  LYS   B HD3  1 
ATOM   5105 H HE2  . LYS   B 1 55  ? 61.491 -24.476 1.101   1.00 31.44 ?  55  LYS   B HE2  1 
ATOM   5106 H HE3  . LYS   B 1 55  ? 59.943 -24.838 1.120   1.00 31.44 ?  55  LYS   B HE3  1 
ATOM   5107 H HZ1  . LYS   B 1 55  ? 61.159 -26.620 1.789   1.00 33.41 ?  55  LYS   B HZ1  1 
ATOM   5108 H HZ2  . LYS   B 1 55  ? 60.509 -26.964 0.541   1.00 33.41 ?  55  LYS   B HZ2  1 
ATOM   5109 H HZ3  . LYS   B 1 55  ? 61.920 -26.635 0.555   1.00 33.41 ?  55  LYS   B HZ3  1 
ATOM   5110 N N    . ALA   B 1 56  ? 58.338 -20.692 -2.895  1.00 13.10 ?  56  ALA   B N    1 
ATOM   5111 C CA   . ALA   B 1 56  ? 58.555 -20.197 -4.249  1.00 13.51 ?  56  ALA   B CA   1 
ATOM   5112 C C    . ALA   B 1 56  ? 58.835 -18.700 -4.254  1.00 13.05 ?  56  ALA   B C    1 
ATOM   5113 O O    . ALA   B 1 56  ? 59.569 -18.208 -5.122  1.00 14.17 ?  56  ALA   B O    1 
ATOM   5114 C CB   . ALA   B 1 56  ? 57.353 -20.538 -5.132  1.00 14.40 ?  56  ALA   B CB   1 
ATOM   5115 H H    . ALA   B 1 56  ? 57.555 -21.022 -2.752  1.00 15.87 ?  56  ALA   B H    1 
ATOM   5116 H HA   . ALA   B 1 56  ? 59.329 -20.637 -4.622  1.00 16.37 ?  56  ALA   B HA   1 
ATOM   5117 H HB1  . ALA   B 1 56  ? 57.517 -20.204 -6.029  1.00 17.43 ?  56  ALA   B HB1  1 
ATOM   5118 H HB2  . ALA   B 1 56  ? 57.243 -21.502 -5.156  1.00 17.43 ?  56  ALA   B HB2  1 
ATOM   5119 H HB3  . ALA   B 1 56  ? 56.558 -20.124 -4.765  1.00 17.43 ?  56  ALA   B HB3  1 
ATOM   5120 N N    . THR   B 1 57  ? 58.261 -17.964 -3.299  1.00 12.89 ?  57  THR   B N    1 
ATOM   5121 C CA   . THR   B 1 57  ? 58.506 -16.531 -3.171  1.00 13.15 ?  57  THR   B CA   1 
ATOM   5122 C C    . THR   B 1 57  ? 59.758 -16.207 -2.361  1.00 13.99 ?  57  THR   B C    1 
ATOM   5123 O O    . THR   B 1 57  ? 59.994 -15.031 -2.060  1.00 14.20 ?  57  THR   B O    1 
ATOM   5124 C CB   . THR   B 1 57  ? 57.302 -15.806 -2.537  1.00 12.39 ?  57  THR   B CB   1 
ATOM   5125 O OG1  . THR   B 1 57  ? 57.283 -16.014 -1.117  1.00 12.49 ?  57  THR   B OG1  1 
ATOM   5126 C CG2  . THR   B 1 57  ? 55.979 -16.238 -3.172  1.00 12.50 ?  57  THR   B CG2  1 
ATOM   5127 H H    . THR   B 1 57  ? 57.713 -18.274 -2.704  1.00 15.62 ?  57  THR   B H    1 
ATOM   5128 H HA   . THR   B 1 57  ? 58.627 -16.162 -4.060  1.00 15.93 ?  57  THR   B HA   1 
ATOM   5129 H HB   . THR   B 1 57  ? 57.399 -14.856 -2.701  1.00 15.02 ?  57  THR   B HB   1 
ATOM   5130 H HG1  . THR   B 1 57  ? 57.215 -16.839 -0.950  1.00 15.14 ?  57  THR   B HG1  1 
ATOM   5131 H HG21 . THR   B 1 57  ? 55.259 -15.672 -2.866  1.00 15.15 ?  57  THR   B HG21 1 
ATOM   5132 H HG22 . THR   B 1 57  ? 56.040 -16.181 -4.140  1.00 15.15 ?  57  THR   B HG22 1 
ATOM   5133 H HG23 . THR   B 1 57  ? 55.780 -17.159 -2.931  1.00 15.15 ?  57  THR   B HG23 1 
ATOM   5134 N N    . ASN   B 1 58  ? 60.554 -17.210 -1.996  1.00 14.99 ?  58  ASN   B N    1 
ATOM   5135 C CA   . ASN   B 1 58  ? 61.750 -16.992 -1.187  1.00 17.22 ?  58  ASN   B CA   1 
ATOM   5136 C C    . ASN   B 1 58  ? 61.414 -16.280 0.124   1.00 14.87 ?  58  ASN   B C    1 
ATOM   5137 O O    . ASN   B 1 58  ? 62.151 -15.402 0.585   1.00 15.86 ?  58  ASN   B O    1 
ATOM   5138 C CB   . ASN   B 1 58  ? 62.829 -16.237 -1.969  1.00 24.40 ?  58  ASN   B CB   1 
ATOM   5139 C CG   . ASN   B 1 58  ? 64.203 -16.367 -1.341  1.00 32.76 ?  58  ASN   B CG   1 
ATOM   5140 O OD1  . ASN   B 1 58  ? 64.516 -17.378 -0.711  1.00 35.21 ?  58  ASN   B OD1  1 
ATOM   5141 N ND2  . ASN   B 1 58  ? 65.030 -15.341 -1.508  1.00 37.70 ?  58  ASN   B ND2  1 
ATOM   5142 H H    . ASN   B 1 58  ? 60.415 -18.034 -2.201  1.00 18.14 ?  58  ASN   B H    1 
ATOM   5143 H HA   . ASN   B 1 58  ? 62.117 -17.860 -0.962  1.00 20.82 ?  58  ASN   B HA   1 
ATOM   5144 H HB2  . ASN   B 1 58  ? 62.875 -16.593 -2.873  1.00 29.43 ?  58  ASN   B HB2  1 
ATOM   5145 H HB3  . ASN   B 1 58  ? 62.602 -15.295 -1.998  1.00 29.43 ?  58  ASN   B HB3  1 
ATOM   5146 H HD21 . ASN   B 1 58  ? 65.822 -15.368 -1.172  1.00 45.40 ?  58  ASN   B HD21 1 
ATOM   5147 H HD22 . ASN   B 1 58  ? 64.776 -14.651 -1.953  1.00 45.40 ?  58  ASN   B HD22 1 
ATOM   5148 N N    . ASN   B 1 59  ? 60.288 -16.662 0.729   1.00 13.68 ?  59  ASN   B N    1 
ATOM   5149 C CA   . ASN   B 1 59  ? 59.809 -16.187 2.023   1.00 13.75 ?  59  ASN   B CA   1 
ATOM   5150 C C    . ASN   B 1 59  ? 59.210 -14.781 1.959   1.00 13.34 ?  59  ASN   B C    1 
ATOM   5151 O O    . ASN   B 1 59  ? 58.784 -14.266 2.995   1.00 13.40 ?  59  ASN   B O    1 
ATOM   5152 C CB   . ASN   B 1 59  ? 60.880 -16.247 3.129   1.00 14.76 ?  59  ASN   B CB   1 
ATOM   5153 C CG   . ASN   B 1 59  ? 60.289 -16.420 4.508   1.00 15.57 ?  59  ASN   B CG   1 
ATOM   5154 O OD1  . ASN   B 1 59  ? 59.452 -17.298 4.731   1.00 15.97 ?  59  ASN   B OD1  1 
ATOM   5155 N ND2  . ASN   B 1 59  ? 60.713 -15.579 5.446   1.00 16.27 ?  59  ASN   B ND2  1 
ATOM   5156 H H    . ASN   B 1 59  ? 59.754 -17.246 0.387   1.00 16.56 ?  59  ASN   B H    1 
ATOM   5157 H HA   . ASN   B 1 59  ? 59.098 -16.780 2.306   1.00 16.65 ?  59  ASN   B HA   1 
ATOM   5158 H HB2  . ASN   B 1 59  ? 61.466 -17.002 2.975   1.00 17.86 ?  59  ASN   B HB2  1 
ATOM   5159 H HB3  . ASN   B 1 59  ? 61.388 -15.424 3.135   1.00 17.86 ?  59  ASN   B HB3  1 
ATOM   5160 H HD21 . ASN   B 1 59  ? 60.406 -15.634 6.251   1.00 19.68 ?  59  ASN   B HD21 1 
ATOM   5161 H HD22 . ASN   B 1 59  ? 61.296 -14.976 5.254   1.00 19.68 ?  59  ASN   B HD22 1 
ATOM   5162 N N    . ALA   B 1 60  ? 59.150 -14.145 0.786   1.00 13.03 ?  60  ALA   B N    1 
ATOM   5163 C CA   . ALA   B 1 60  ? 58.562 -12.809 0.713   1.00 13.37 ?  60  ALA   B CA   1 
ATOM   5164 C C    . ALA   B 1 60  ? 57.095 -12.826 1.120   1.00 12.40 ?  60  ALA   B C    1 
ATOM   5165 O O    . ALA   B 1 60  ? 56.595 -11.868 1.725   1.00 13.04 ?  60  ALA   B O    1 
ATOM   5166 C CB   . ALA   B 1 60  ? 58.714 -12.240 -0.697  1.00 13.99 ?  60  ALA   B CB   1 
ATOM   5167 H H    . ALA   B 1 60  ? 59.440 -14.462 0.046   1.00 15.79 ?  60  ALA   B H    1 
ATOM   5168 H HA   . ALA   B 1 60  ? 59.038 -12.225 1.324   1.00 16.20 ?  60  ALA   B HA   1 
ATOM   5169 H HB1  . ALA   B 1 60  ? 58.317 -11.358 -0.722  1.00 16.94 ?  60  ALA   B HB1  1 
ATOM   5170 H HB2  . ALA   B 1 60  ? 59.657 -12.190 -0.919  1.00 16.94 ?  60  ALA   B HB2  1 
ATOM   5171 H HB3  . ALA   B 1 60  ? 58.259 -12.828 -1.323  1.00 16.94 ?  60  ALA   B HB3  1 
ATOM   5172 N N    . MET   B 1 61  ? 56.382 -13.896 0.767   1.00 11.88 ?  61  MET   B N    1 
ATOM   5173 C CA   . MET   B 1 61  ? 54.986 -14.023 1.164   1.00 11.07 ?  61  MET   B CA   1 
ATOM   5174 C C    . MET   B 1 61  ? 54.845 -14.025 2.683   1.00 11.29 ?  61  MET   B C    1 
ATOM   5175 O O    . MET   B 1 61  ? 53.952 -13.363 3.230   1.00 11.31 ?  61  MET   B O    1 
ATOM   5176 C CB   . MET   B 1 61  ? 54.397 -15.289 0.530   1.00 11.05 ?  61  MET   B CB   1 
ATOM   5177 C CG   . MET   B 1 61  ? 52.963 -15.579 0.946   1.00 11.40 ?  61  MET   B CG   1 
ATOM   5178 S SD   . MET   B 1 61  ? 52.315 -17.084 0.197   1.00 11.83 ?  61  MET   B SD   1 
ATOM   5179 C CE   . MET   B 1 61  ? 52.061 -16.501 -1.478  1.00 12.98 ?  61  MET   B CE   1 
ATOM   5180 H H    . MET   B 1 61  ? 56.686 -14.559 0.298   1.00 14.41 ?  61  MET   B H    1 
ATOM   5181 H HA   . MET   B 1 61  ? 54.495 -13.271 0.800   1.00 13.43 ?  61  MET   B HA   1 
ATOM   5182 H HB2  . MET   B 1 61  ? 54.404 -15.196 -0.437  1.00 13.41 ?  61  MET   B HB2  1 
ATOM   5183 H HB3  . MET   B 1 61  ? 54.936 -16.053 0.787   1.00 13.41 ?  61  MET   B HB3  1 
ATOM   5184 H HG2  . MET   B 1 61  ? 52.928 -15.694 1.910   1.00 13.83 ?  61  MET   B HG2  1 
ATOM   5185 H HG3  . MET   B 1 61  ? 52.399 -14.841 0.677   1.00 13.83 ?  61  MET   B HG3  1 
ATOM   5186 H HE1  . MET   B 1 61  ? 51.669 -17.214 -2.003  1.00 15.72 ?  61  MET   B HE1  1 
ATOM   5187 H HE2  . MET   B 1 61  ? 51.465 -15.736 -1.457  1.00 15.72 ?  61  MET   B HE2  1 
ATOM   5188 H HE3  . MET   B 1 61  ? 52.917 -16.242 -1.858  1.00 15.72 ?  61  MET   B HE3  1 
ATOM   5189 N N    . GLN   B 1 62  ? 55.722 -14.743 3.389   1.00 11.31 ?  62  GLN   B N    1 
ATOM   5190 C CA   . GLN   B 1 62  ? 55.615 -14.791 4.843   1.00 11.48 ?  62  GLN   B CA   1 
ATOM   5191 C C    . GLN   B 1 62  ? 55.899 -13.432 5.470   1.00 11.75 ?  62  GLN   B C    1 
ATOM   5192 O O    . GLN   B 1 62  ? 55.217 -13.029 6.418   1.00 12.25 ?  62  GLN   B O    1 
ATOM   5193 C CB   . GLN   B 1 62  ? 56.571 -15.837 5.416   1.00 12.17 ?  62  GLN   B CB   1 
ATOM   5194 C CG   . GLN   B 1 62  ? 56.338 -16.112 6.892   1.00 12.61 ?  62  GLN   B CG   1 
ATOM   5195 C CD   . GLN   B 1 62  ? 54.959 -16.705 7.127   1.00 11.90 ?  62  GLN   B CD   1 
ATOM   5196 O OE1  . GLN   B 1 62  ? 54.703 -17.852 6.763   1.00 12.56 ?  62  GLN   B OE1  1 
ATOM   5197 N NE2  . GLN   B 1 62  ? 54.046 -15.912 7.684   1.00 12.16 ?  62  GLN   B NE2  1 
ATOM   5198 H H    . GLN   B 1 62  ? 56.362 -15.209 3.049   1.00 13.73 ?  62  GLN   B H    1 
ATOM   5199 H HA   . GLN   B 1 62  ? 54.710 -15.046 5.079   1.00 13.93 ?  62  GLN   B HA   1 
ATOM   5200 H HB2  . GLN   B 1 62  ? 56.455 -16.669 4.931   1.00 14.76 ?  62  GLN   B HB2  1 
ATOM   5201 H HB3  . GLN   B 1 62  ? 57.482 -15.518 5.311   1.00 14.76 ?  62  GLN   B HB3  1 
ATOM   5202 H HG2  . GLN   B 1 62  ? 56.998 -16.753 7.201   1.00 15.28 ?  62  GLN   B HG2  1 
ATOM   5203 H HG3  . GLN   B 1 62  ? 56.407 -15.288 7.390   1.00 15.28 ?  62  GLN   B HG3  1 
ATOM   5204 H HE21 . GLN   B 1 62  ? 54.251 -15.110 7.914   1.00 14.74 ?  62  GLN   B HE21 1 
ATOM   5205 H HE22 . GLN   B 1 62  ? 53.249 -16.208 7.827   1.00 14.74 ?  62  GLN   B HE22 1 
ATOM   5206 N N    . VAL   B 1 63  ? 56.918 -12.722 4.977   1.00 12.49 ?  63  VAL   B N    1 
ATOM   5207 C CA   . VAL   B 1 63  ? 57.226 -11.402 5.525   1.00 13.13 ?  63  VAL   B CA   1 
ATOM   5208 C C    . VAL   B 1 63  ? 56.034 -10.466 5.343   1.00 12.50 ?  63  VAL   B C    1 
ATOM   5209 O O    . VAL   B 1 63  ? 55.621 -9.756  6.271   1.00 12.91 ?  63  VAL   B O    1 
ATOM   5210 C CB   . VAL   B 1 63  ? 58.509 -10.843 4.887   1.00 14.11 ?  63  VAL   B CB   1 
ATOM   5211 C CG1  . VAL   B 1 63  ? 58.730 -9.394  5.329   1.00 14.90 ?  63  VAL   B CG1  1 
ATOM   5212 C CG2  . VAL   B 1 63  ? 59.701 -11.711 5.263   1.00 14.88 ?  63  VAL   B CG2  1 
ATOM   5213 H H    . VAL   B 1 63  ? 57.438 -12.982 4.334   1.00 15.14 ?  63  VAL   B H    1 
ATOM   5214 H HA   . VAL   B 1 63  ? 57.389 -11.496 6.472   1.00 15.91 ?  63  VAL   B HA   1 
ATOM   5215 H HB   . VAL   B 1 63  ? 58.425 -10.857 3.921   1.00 17.09 ?  63  VAL   B HB   1 
ATOM   5216 H HG11 . VAL   B 1 63  ? 59.644 -9.143  5.142   1.00 18.03 ?  63  VAL   B HG11 1 
ATOM   5217 H HG12 . VAL   B 1 63  ? 58.119 -8.820  4.840   1.00 18.03 ?  63  VAL   B HG12 1 
ATOM   5218 H HG13 . VAL   B 1 63  ? 58.556 -9.329  6.282   1.00 18.03 ?  63  VAL   B HG13 1 
ATOM   5219 H HG21 . VAL   B 1 63  ? 60.508 -11.330 4.876   1.00 18.00 ?  63  VAL   B HG21 1 
ATOM   5220 H HG22 . VAL   B 1 63  ? 59.786 -11.732 6.232   1.00 18.00 ?  63  VAL   B HG22 1 
ATOM   5221 H HG23 . VAL   B 1 63  ? 59.566 -12.608 4.925   1.00 18.00 ?  63  VAL   B HG23 1 
ATOM   5222 N N    . GLU   B 1 64  ? 55.464 -10.456 4.140   1.00 11.89 ?  64  GLU   B N    1 
ATOM   5223 C CA   . GLU   B 1 64  ? 54.295 -9.629  3.861   1.00 11.53 ?  64  GLU   B CA   1 
ATOM   5224 C C    . GLU   B 1 64  ? 53.111 -10.025 4.737   1.00 11.46 ?  64  GLU   B C    1 
ATOM   5225 O O    . GLU   B 1 64  ? 52.370 -9.161  5.233   1.00 12.11 ?  64  GLU   B O    1 
ATOM   5226 C CB   . GLU   B 1 64  ? 53.931 -9.794  2.386   1.00 11.71 ?  64  GLU   B CB   1 
ATOM   5227 C CG   . GLU   B 1 64  ? 52.685 -9.041  1.949   1.00 12.04 ?  64  GLU   B CG   1 
ATOM   5228 C CD   . GLU   B 1 64  ? 52.146 -9.533  0.616   1.00 13.04 ?  64  GLU   B CD   1 
ATOM   5229 O OE1  . GLU   B 1 64  ? 52.326 -10.737 0.298   1.00 13.54 ?  64  GLU   B OE1  1 
ATOM   5230 O OE2  . GLU   B 1 64  ? 51.517 -8.713  -0.096  1.00 14.02 -1 64  GLU   B OE2  1 
ATOM   5231 H H    . GLU   B 1 64  ? 55.731 -10.930 3.465   1.00 14.41 ?  64  GLU   B H    1 
ATOM   5232 H HA   . GLU   B 1 64  ? 54.507 -8.705  4.025   1.00 13.98 ?  64  GLU   B HA   1 
ATOM   5233 H HB2  . GLU   B 1 64  ? 54.666 -9.465  1.841   1.00 14.20 ?  64  GLU   B HB2  1 
ATOM   5234 H HB3  . GLU   B 1 64  ? 53.784 -10.733 2.197   1.00 14.20 ?  64  GLU   B HB3  1 
ATOM   5235 H HG2  . GLU   B 1 64  ? 51.982 -9.156  2.611   1.00 14.60 ?  64  GLU   B HG2  1 
ATOM   5236 H HG3  . GLU   B 1 64  ? 52.897 -8.099  1.861   1.00 14.60 ?  64  GLU   B HG3  1 
ATOM   5237 N N    . SER   B 1 65  ? 52.923 -11.333 4.933   1.00 11.32 ?  65  SER   B N    1 
ATOM   5238 C CA   . SER   B 1 65  ? 51.809 -11.835 5.727   1.00 11.23 ?  65  SER   B CA   1 
ATOM   5239 C C    . SER   B 1 65  ? 51.936 -11.432 7.188   1.00 11.30 ?  65  SER   B C    1 
ATOM   5240 O O    . SER   B 1 65  ? 50.937 -11.060 7.822   1.00 11.79 ?  65  SER   B O    1 
ATOM   5241 C CB   . SER   B 1 65  ? 51.733 -13.360 5.611   1.00 11.86 ?  65  SER   B CB   1 
ATOM   5242 O OG   . SER   B 1 65  ? 51.396 -13.770 4.296   1.00 11.64 ?  65  SER   B OG   1 
ATOM   5243 H H    . SER   B 1 65  ? 53.435 -11.957 4.623   1.00 13.73 ?  65  SER   B H    1 
ATOM   5244 H HA   . SER   B 1 65  ? 50.980 -11.469 5.381   1.00 13.63 ?  65  SER   B HA   1 
ATOM   5245 H HB2  . SER   B 1 65  ? 52.589 -13.740 5.854   1.00 14.38 ?  65  SER   B HB2  1 
ATOM   5246 H HB3  . SER   B 1 65  ? 51.046 -13.687 6.222   1.00 14.38 ?  65  SER   B HB3  1 
ATOM   5247 H HG   . SER   B 1 65  ? 51.984 -13.498 3.754   1.00 14.12 ?  65  SER   B HG   1 
ATOM   5248 N N    . ASP   B 1 66  ? 53.144 -11.531 7.755   1.00 11.92 ?  66  ASP   B N    1 
ATOM   5249 C CA   . ASP   B 1 66  ? 53.336 -11.133 9.144   1.00 12.34 ?  66  ASP   B CA   1 
ATOM   5250 C C    . ASP   B 1 66  ? 53.025 -9.653  9.338   1.00 12.04 ?  66  ASP   B C    1 
ATOM   5251 O O    . ASP   B 1 66  ? 52.448 -9.260  10.358  1.00 12.89 ?  66  ASP   B O    1 
ATOM   5252 C CB   . ASP   B 1 66  ? 54.769 -11.441 9.591   1.00 13.60 ?  66  ASP   B CB   1 
ATOM   5253 C CG   . ASP   B 1 66  ? 55.040 -12.935 9.759   1.00 15.15 ?  66  ASP   B CG   1 
ATOM   5254 O OD1  . ASP   B 1 66  ? 54.086 -13.746 9.674   1.00 15.78 ?  66  ASP   B OD1  1 
ATOM   5255 O OD2  . ASP   B 1 66  ? 56.225 -13.287 9.987   1.00 18.07 -1 66  ASP   B OD2  1 
ATOM   5256 H H    . ASP   B 1 66  ? 53.845 -11.835 7.366   1.00 14.46 ?  66  ASP   B H    1 
ATOM   5257 H HA   . ASP   B 1 66  ? 52.738 -11.638 9.714   1.00 14.96 ?  66  ASP   B HA   1 
ATOM   5258 H HB2  . ASP   B 1 66  ? 55.389 -11.106 8.926   1.00 16.48 ?  66  ASP   B HB2  1 
ATOM   5259 H HB3  . ASP   B 1 66  ? 54.937 -11.006 10.446  1.00 16.48 ?  66  ASP   B HB3  1 
ATOM   5260 N N    . ASP   B 1 67  ? 53.401 -8.815  8.373   1.00 11.90 ?  67  ASP   B N    1 
ATOM   5261 C CA   . ASP   B 1 67  ? 53.053 -7.403  8.453   1.00 12.79 ?  67  ASP   B CA   1 
ATOM   5262 C C    . ASP   B 1 67  ? 51.540 -7.199  8.373   1.00 12.76 ?  67  ASP   B C    1 
ATOM   5263 O O    . ASP   B 1 67  ? 50.978 -6.389  9.123   1.00 13.45 ?  67  ASP   B O    1 
ATOM   5264 C CB   . ASP   B 1 67  ? 53.776 -6.643  7.347   1.00 13.80 ?  67  ASP   B CB   1 
ATOM   5265 C CG   . ASP   B 1 67  ? 53.343 -5.202  7.274   1.00 15.06 ?  67  ASP   B CG   1 
ATOM   5266 O OD1  . ASP   B 1 67  ? 53.854 -4.371  8.059   1.00 16.37 ?  67  ASP   B OD1  1 
ATOM   5267 O OD2  . ASP   B 1 67  ? 52.460 -4.913  6.446   1.00 16.06 -1 67  ASP   B OD2  1 
ATOM   5268 H H    . ASP   B 1 67  ? 53.856 -9.039  7.677   1.00 14.43 ?  67  ASP   B H    1 
ATOM   5269 H HA   . ASP   B 1 67  ? 53.360 -7.051  9.303   1.00 15.49 ?  67  ASP   B HA   1 
ATOM   5270 H HB2  . ASP   B 1 67  ? 54.733 -6.670  7.514   1.00 16.71 ?  67  ASP   B HB2  1 
ATOM   5271 H HB3  . ASP   B 1 67  ? 53.580 -7.066  6.492   1.00 16.71 ?  67  ASP   B HB3  1 
ATOM   5272 N N    . TYR   B 1 68  ? 50.864 -7.931  7.482   1.00 12.48 ?  68  TYR   B N    1 
ATOM   5273 C CA   . TYR   B 1 68  ? 49.406 -7.854  7.407   1.00 13.10 ?  68  TYR   B CA   1 
ATOM   5274 C C    . TYR   B 1 68  ? 48.771 -8.196  8.750   1.00 12.72 ?  68  TYR   B C    1 
ATOM   5275 O O    . TYR   B 1 68  ? 47.837 -7.516  9.197   1.00 13.32 ?  68  TYR   B O    1 
ATOM   5276 C CB   . TYR   B 1 68  ? 48.871 -8.800  6.324   1.00 13.79 ?  68  TYR   B CB   1 
ATOM   5277 C CG   . TYR   B 1 68  ? 47.359 -8.950  6.385   1.00 14.91 ?  68  TYR   B CG   1 
ATOM   5278 C CD1  . TYR   B 1 68  ? 46.773 -9.900  7.217   1.00 15.44 ?  68  TYR   B CD1  1 
ATOM   5279 C CD2  . TYR   B 1 68  ? 46.525 -8.123  5.650   1.00 15.88 ?  68  TYR   B CD2  1 
ATOM   5280 C CE1  . TYR   B 1 68  ? 45.407 -10.026 7.314   1.00 16.63 ?  68  TYR   B CE1  1 
ATOM   5281 C CE2  . TYR   B 1 68  ? 45.143 -8.251  5.733   1.00 15.98 ?  68  TYR   B CE2  1 
ATOM   5282 C CZ   . TYR   B 1 68  ? 44.604 -9.202  6.571   1.00 16.37 ?  68  TYR   B CZ   1 
ATOM   5283 O OH   . TYR   B 1 68  ? 43.236 -9.312  6.667   1.00 17.20 ?  68  TYR   B OH   1 
ATOM   5284 H H    . TYR   B 1 68  ? 51.225 -8.480  6.919   1.00 15.13 ?  68  TYR   B H    1 
ATOM   5285 H HA   . TYR   B 1 68  ? 49.153 -6.950  7.171   1.00 15.87 ?  68  TYR   B HA   1 
ATOM   5286 H HB2  . TYR   B 1 68  ? 49.099 -8.447  5.452   1.00 16.70 ?  68  TYR   B HB2  1 
ATOM   5287 H HB3  . TYR   B 1 68  ? 49.264 -9.678  6.446   1.00 16.70 ?  68  TYR   B HB3  1 
ATOM   5288 H HD1  . TYR   B 1 68  ? 47.315 -10.461 7.725   1.00 18.68 ?  68  TYR   B HD1  1 
ATOM   5289 H HD2  . TYR   B 1 68  ? 46.895 -7.473  5.101   1.00 19.20 ?  68  TYR   B HD2  1 
ATOM   5290 H HE1  . TYR   B 1 68  ? 45.027 -10.674 7.867   1.00 20.10 ?  68  TYR   B HE1  1 
ATOM   5291 H HE2  . TYR   B 1 68  ? 44.583 -7.689  5.244   1.00 19.33 ?  68  TYR   B HE2  1 
ATOM   5292 H HH   . TYR   B 1 68  ? 42.853 -8.758  6.156   1.00 20.79 ?  68  TYR   B HH   1 
ATOM   5293 N N    . ILE   B 1 69  ? 49.256 -9.258  9.401   1.00 12.43 ?  69  ILE   B N    1 
ATOM   5294 C CA   . ILE   B 1 69  ? 48.703 -9.679  10.687  1.00 12.74 ?  69  ILE   B CA   1 
ATOM   5295 C C    . ILE   B 1 69  ? 48.953 -8.625  11.760  1.00 12.41 ?  69  ILE   B C    1 
ATOM   5296 O O    . ILE   B 1 69  ? 48.082 -8.345  12.593  1.00 13.04 ?  69  ILE   B O    1 
ATOM   5297 C CB   . ILE   B 1 69  ? 49.279 -11.048 11.091  1.00 13.31 ?  69  ILE   B CB   1 
ATOM   5298 C CG1  . ILE   B 1 69  ? 48.753 -12.161 10.173  1.00 13.94 ?  69  ILE   B CG1  1 
ATOM   5299 C CG2  . ILE   B 1 69  ? 48.983 -11.352 12.556  1.00 14.39 ?  69  ILE   B CG2  1 
ATOM   5300 C CD1  . ILE   B 1 69  ? 47.273 -12.474 10.344  1.00 14.46 ?  69  ILE   B CD1  1 
ATOM   5301 H H    . ILE   B 1 69  ? 49.912 -9.739  9.120   1.00 15.06 ?  69  ILE   B H    1 
ATOM   5302 H HA   . ILE   B 1 69  ? 47.752 -9.776  10.588  1.00 15.44 ?  69  ILE   B HA   1 
ATOM   5303 H HB   . ILE   B 1 69  ? 50.246 -11.013 10.989  1.00 16.12 ?  69  ILE   B HB   1 
ATOM   5304 H HG12 . ILE   B 1 69  ? 48.895 -11.893 9.251   1.00 16.88 ?  69  ILE   B HG12 1 
ATOM   5305 H HG13 . ILE   B 1 69  ? 49.252 -12.975 10.354  1.00 16.88 ?  69  ILE   B HG13 1 
ATOM   5306 H HG21 . ILE   B 1 69  ? 49.114 -12.302 12.710  1.00 17.42 ?  69  ILE   B HG21 1 
ATOM   5307 H HG22 . ILE   B 1 69  ? 49.584 -10.842 13.117  1.00 17.42 ?  69  ILE   B HG22 1 
ATOM   5308 H HG23 . ILE   B 1 69  ? 48.062 -11.114 12.746  1.00 17.42 ?  69  ILE   B HG23 1 
ATOM   5309 H HD11 . ILE   B 1 69  ? 47.034 -13.178 9.724   1.00 17.51 ?  69  ILE   B HD11 1 
ATOM   5310 H HD12 . ILE   B 1 69  ? 47.117 -12.769 11.255  1.00 17.51 ?  69  ILE   B HD12 1 
ATOM   5311 H HD13 . ILE   B 1 69  ? 46.758 -11.677 10.158  1.00 17.51 ?  69  ILE   B HD13 1 
ATOM   5312 N N    . ALA   B 1 70  ? 50.145 -8.033  11.776  1.00 12.28 ?  70  ALA   B N    1 
ATOM   5313 C CA   . ALA   B 1 70  ? 50.422 -6.992  12.762  1.00 12.24 ?  70  ALA   B CA   1 
ATOM   5314 C C    . ALA   B 1 70  ? 49.417 -5.854  12.648  1.00 12.65 ?  70  ALA   B C    1 
ATOM   5315 O O    . ALA   B 1 70  ? 48.969 -5.310  13.659  1.00 13.45 ?  70  ALA   B O    1 
ATOM   5316 C CB   . ALA   B 1 70  ? 51.848 -6.466  12.594  1.00 12.97 ?  70  ALA   B CB   1 
ATOM   5317 H H    . ALA   B 1 70  ? 50.794 -8.210  11.249  1.00 14.88 ?  70  ALA   B H    1 
ATOM   5318 H HA   . ALA   B 1 70  ? 50.349 -7.368  13.657  1.00 14.84 ?  70  ALA   B HA   1 
ATOM   5319 H HB1  . ALA   B 1 70  ? 52.037 -5.822  13.300  1.00 15.72 ?  70  ALA   B HB1  1 
ATOM   5320 H HB2  . ALA   B 1 70  ? 52.471 -7.206  12.655  1.00 15.72 ?  70  ALA   B HB2  1 
ATOM   5321 H HB3  . ALA   B 1 70  ? 51.930 -6.036  11.728  1.00 15.72 ?  70  ALA   B HB3  1 
ATOM   5322 N N    . THR   B 1 71  ? 49.047 -5.489  11.423  1.00 13.04 ?  71  THR   B N    1 
ATOM   5323 C CA   . THR   B 1 71  ? 48.141 -4.366  11.206  1.00 14.27 ?  71  THR   B CA   1 
ATOM   5324 C C    . THR   B 1 71  ? 46.674 -4.740  11.421  1.00 14.85 ?  71  THR   B C    1 
ATOM   5325 O O    . THR   B 1 71  ? 45.897 -3.927  11.943  1.00 16.23 ?  71  THR   B O    1 
ATOM   5326 C CB   . THR   B 1 71  ? 48.354 -3.813  9.794   1.00 16.18 ?  71  THR   B CB   1 
ATOM   5327 O OG1  . THR   B 1 71  ? 49.677 -3.276  9.687   1.00 17.96 ?  71  THR   B OG1  1 
ATOM   5328 C CG2  . THR   B 1 71  ? 47.335 -2.731  9.469   1.00 17.12 ?  71  THR   B CG2  1 
ATOM   5329 H H    . THR   B 1 71  ? 49.312 -5.883  10.704  1.00 15.80 ?  71  THR   B H    1 
ATOM   5330 H HA   . THR   B 1 71  ? 48.362 -3.667  11.832  1.00 17.28 ?  71  THR   B HA   1 
ATOM   5331 H HB   . THR   B 1 71  ? 48.260 -4.527  9.143   1.00 19.57 ?  71  THR   B HB   1 
ATOM   5332 H HG1  . THR   B 1 71  ? 49.797 -2.949  8.917   1.00 21.70 ?  71  THR   B HG1  1 
ATOM   5333 H HG21 . THR   B 1 71  ? 47.633 -2.216  8.702   1.00 20.69 ?  71  THR   B HG21 1 
ATOM   5334 H HG22 . THR   B 1 71  ? 46.478 -3.131  9.265   1.00 20.69 ?  71  THR   B HG22 1 
ATOM   5335 H HG23 . THR   B 1 71  ? 47.237 -2.133  10.227  1.00 20.69 ?  71  THR   B HG23 1 
ATOM   5336 N N    . ASN   B 1 72  ? 46.277 -5.958  11.030  1.00 14.59 ?  72  ASN   B N    1 
ATOM   5337 C CA   . ASN   B 1 72  ? 44.873 -6.326  10.918  1.00 15.13 ?  72  ASN   B CA   1 
ATOM   5338 C C    . ASN   B 1 72  ? 44.416 -7.419  11.871  1.00 15.57 ?  72  ASN   B C    1 
ATOM   5339 O O    . ASN   B 1 72  ? 43.203 -7.579  12.049  1.00 16.60 ?  72  ASN   B O    1 
ATOM   5340 C CB   . ASN   B 1 72  ? 44.554 -6.758  9.477   1.00 16.20 ?  72  ASN   B CB   1 
ATOM   5341 C CG   . ASN   B 1 72  ? 44.844 -5.660  8.470   1.00 17.08 ?  72  ASN   B CG   1 
ATOM   5342 O OD1  . ASN   B 1 72  ? 45.868 -5.678  7.777   1.00 18.24 ?  72  ASN   B OD1  1 
ATOM   5343 N ND2  . ASN   B 1 72  ? 43.969 -4.676  8.413   1.00 18.59 ?  72  ASN   B ND2  1 
ATOM   5344 H H    . ASN   B 1 72  ? 46.819 -6.603  10.824  1.00 17.66 ?  72  ASN   B H    1 
ATOM   5345 H HA   . ASN   B 1 72  ? 44.339 -5.544  11.109  1.00 18.31 ?  72  ASN   B HA   1 
ATOM   5346 H HB2  . ASN   B 1 72  ? 45.095 -7.530  9.247   1.00 19.59 ?  72  ASN   B HB2  1 
ATOM   5347 H HB3  . ASN   B 1 72  ? 43.612 -6.980  9.414   1.00 19.59 ?  72  ASN   B HB3  1 
ATOM   5348 H HD21 . ASN   B 1 72  ? 44.084 -4.028  7.858   1.00 22.46 ?  72  ASN   B HD21 1 
ATOM   5349 H HD22 . ASN   B 1 72  ? 43.267 -4.692  8.911   1.00 22.46 ?  72  ASN   B HD22 1 
ATOM   5350 N N    . GLY   B 1 73  ? 45.329 -8.170  12.482  1.00 14.94 ?  73  GLY   B N    1 
ATOM   5351 C CA   . GLY   B 1 73  ? 44.948 -9.316  13.273  1.00 14.24 ?  73  GLY   B CA   1 
ATOM   5352 C C    . GLY   B 1 73  ? 44.575 -10.496 12.401  1.00 12.99 ?  73  GLY   B C    1 
ATOM   5353 O O    . GLY   B 1 73  ? 44.561 -10.410 11.172  1.00 13.23 ?  73  GLY   B O    1 
ATOM   5354 H H    . GLY   B 1 73  ? 46.179 -8.032  12.450  1.00 18.08 ?  73  GLY   B H    1 
ATOM   5355 H HA2  . GLY   B 1 73  ? 45.686 -9.575  13.849  1.00 17.24 ?  73  GLY   B HA2  1 
ATOM   5356 H HA3  . GLY   B 1 73  ? 44.187 -9.089  13.830  1.00 17.24 ?  73  GLY   B HA3  1 
ATOM   5357 N N    . PRO   B 1 74  ? 44.267 -11.623 13.038  1.00 13.25 ?  74  PRO   B N    1 
ATOM   5358 C CA   . PRO   B 1 74  ? 44.010 -12.855 12.292  1.00 12.71 ?  74  PRO   B CA   1 
ATOM   5359 C C    . PRO   B 1 74  ? 42.710 -12.792 11.509  1.00 12.14 ?  74  PRO   B C    1 
ATOM   5360 O O    . PRO   B 1 74  ? 41.776 -12.053 11.837  1.00 13.69 ?  74  PRO   B O    1 
ATOM   5361 C CB   . PRO   B 1 74  ? 43.940 -13.919 13.393  1.00 14.10 ?  74  PRO   B CB   1 
ATOM   5362 C CG   . PRO   B 1 74  ? 43.499 -13.164 14.611  1.00 15.65 ?  74  PRO   B CG   1 
ATOM   5363 C CD   . PRO   B 1 74  ? 44.167 -11.823 14.493  1.00 15.08 ?  74  PRO   B CD   1 
ATOM   5364 H HA   . PRO   B 1 74  ? 44.747 -13.051 11.688  1.00 15.41 ?  74  PRO   B HA   1 
ATOM   5365 H HB2  . PRO   B 1 74  ? 43.292 -14.599 13.150  1.00 17.08 ?  74  PRO   B HB2  1 
ATOM   5366 H HB3  . PRO   B 1 74  ? 44.818 -14.311 13.528  1.00 17.08 ?  74  PRO   B HB3  1 
ATOM   5367 H HG2  . PRO   B 1 74  ? 42.532 -13.068 14.603  1.00 18.93 ?  74  PRO   B HG2  1 
ATOM   5368 H HG3  . PRO   B 1 74  ? 43.792 -13.628 15.409  1.00 18.93 ?  74  PRO   B HG3  1 
ATOM   5369 H HD2  . PRO   B 1 74  ? 43.613 -11.134 14.898  1.00 18.25 ?  74  PRO   B HD2  1 
ATOM   5370 H HD3  . PRO   B 1 74  ? 45.049 -11.850 14.896  1.00 18.25 ?  74  PRO   B HD3  1 
ATOM   5371 N N    . LEU   B 1 75  ? 42.673 -13.595 10.454  1.00 11.80 ?  75  LEU   B N    1 
ATOM   5372 C CA   . LEU   B 1 75  ? 41.461 -13.796 9.685   1.00 11.88 ?  75  LEU   B CA   1 
ATOM   5373 C C    . LEU   B 1 75  ? 40.477 -14.647 10.483  1.00 12.66 ?  75  LEU   B C    1 
ATOM   5374 O O    . LEU   B 1 75  ? 40.819 -15.247 11.503  1.00 13.95 ?  75  LEU   B O    1 
ATOM   5375 C CB   . LEU   B 1 75  ? 41.781 -14.517 8.375   1.00 11.57 ?  75  LEU   B CB   1 
ATOM   5376 C CG   . LEU   B 1 75  ? 42.624 -13.771 7.337   1.00 13.75 ?  75  LEU   B CG   1 
ATOM   5377 C CD1  . LEU   B 1 75  ? 42.901 -14.643 6.115   1.00 15.63 ?  75  LEU   B CD1  1 
ATOM   5378 C CD2  . LEU   B 1 75  ? 41.968 -12.484 6.917   1.00 17.50 ?  75  LEU   B CD2  1 
ATOM   5379 H H    . LEU   B 1 75  ? 43.346 -14.037 10.158  1.00 14.31 ?  75  LEU   B H    1 
ATOM   5380 H HA   . LEU   B 1 75  ? 41.048 -12.941 9.479   1.00 14.41 ?  75  LEU   B HA   1 
ATOM   5381 H HB2  . LEU   B 1 75  ? 42.265 -15.333 8.593   1.00 14.04 ?  75  LEU   B HB2  1 
ATOM   5382 H HB3  . LEU   B 1 75  ? 40.946 -14.752 7.945   1.00 14.04 ?  75  LEU   B HB3  1 
ATOM   5383 H HG   . LEU   B 1 75  ? 43.480 -13.548 7.732   1.00 16.66 ?  75  LEU   B HG   1 
ATOM   5384 H HD11 . LEU   B 1 75  ? 43.441 -14.136 5.481   1.00 18.91 ?  75  LEU   B HD11 1 
ATOM   5385 H HD12 . LEU   B 1 75  ? 43.388 -15.435 6.394   1.00 18.91 ?  75  LEU   B HD12 1 
ATOM   5386 H HD13 . LEU   B 1 75  ? 42.063 -14.895 5.704   1.00 18.91 ?  75  LEU   B HD13 1 
ATOM   5387 H HD21 . LEU   B 1 75  ? 42.488 -12.080 6.207   1.00 21.15 ?  75  LEU   B HD21 1 
ATOM   5388 H HD22 . LEU   B 1 75  ? 41.069 -12.675 6.604   1.00 21.15 ?  75  LEU   B HD22 1 
ATOM   5389 H HD23 . LEU   B 1 75  ? 41.931 -11.887 7.681   1.00 21.15 ?  75  LEU   B HD23 1 
ATOM   5390 N N    . LYS   B 1 76  ? 39.241 -14.703 9.990   1.00 13.94 ?  76  LYS   B N    1 
ATOM   5391 C CA   . LYS   B 1 76  ? 38.254 -15.667 10.454  1.00 15.11 ?  76  LYS   B CA   1 
ATOM   5392 C C    . LYS   B 1 76  ? 38.369 -16.953 9.638   1.00 13.98 ?  76  LYS   B C    1 
ATOM   5393 O O    . LYS   B 1 76  ? 38.648 -16.917 8.443   1.00 13.62 ?  76  LYS   B O    1 
ATOM   5394 C CB   . LYS   B 1 76  ? 36.841 -15.105 10.239  1.00 17.35 ?  76  LYS   B CB   1 
ATOM   5395 C CG   . LYS   B 1 76  ? 36.555 -13.730 10.867  1.00 19.03 ?  76  LYS   B CG   1 
ATOM   5396 C CD   . LYS   B 1 76  ? 35.146 -13.211 10.521  1.00 20.17 ?  76  LYS   B CD   1 
ATOM   5397 C CE   . LYS   B 1 76  ? 34.884 -11.837 11.130  1.00 21.96 ?  76  LYS   B CE   1 
ATOM   5398 N NZ   . LYS   B 1 76  ? 33.609 -11.222 10.667  1.00 22.45 ?  76  LYS   B NZ   1 
ATOM   5399 H H    . LYS   B 1 76  ? 38.947 -14.188 9.363   1.00 16.88 ?  76  LYS   B H    1 
ATOM   5400 H HA   . LYS   B 1 76  ? 38.388 -15.867 11.392  1.00 18.28 ?  76  LYS   B HA   1 
ATOM   5401 H HB2  . LYS   B 1 76  ? 36.687 -15.024 9.286   1.00 20.98 ?  76  LYS   B HB2  1 
ATOM   5402 H HB3  . LYS   B 1 76  ? 36.205 -15.730 10.618  1.00 20.98 ?  76  LYS   B HB3  1 
ATOM   5403 H HG2  . LYS   B 1 76  ? 36.623 -13.797 11.832  1.00 22.99 ?  76  LYS   B HG2  1 
ATOM   5404 H HG3  . LYS   B 1 76  ? 37.202 -13.085 10.533  1.00 22.99 ?  76  LYS   B HG3  1 
ATOM   5405 H HD2  . LYS   B 1 76  ? 35.058 -13.137 9.557   1.00 24.36 ?  76  LYS   B HD2  1 
ATOM   5406 H HD3  . LYS   B 1 76  ? 34.483 -13.828 10.870  1.00 24.36 ?  76  LYS   B HD3  1 
ATOM   5407 H HE2  . LYS   B 1 76  ? 34.841 -11.926 12.094  1.00 26.51 ?  76  LYS   B HE2  1 
ATOM   5408 H HE3  . LYS   B 1 76  ? 35.611 -11.244 10.884  1.00 26.51 ?  76  LYS   B HE3  1 
ATOM   5409 H HZ1  . LYS   B 1 76  ? 33.501 -10.425 11.047  1.00 27.09 ?  76  LYS   B HZ1  1 
ATOM   5410 H HZ2  . LYS   B 1 76  ? 33.624 -11.121 9.782   1.00 27.09 ?  76  LYS   B HZ2  1 
ATOM   5411 H HZ3  . LYS   B 1 76  ? 32.922 -11.743 10.886  1.00 27.09 ?  76  LYS   B HZ3  1 
ATOM   5412 N N    . VAL   B 1 77  ? 38.135 -18.100 10.284  1.00 14.62 ?  77  VAL   B N    1 
ATOM   5413 C CA   . VAL   B 1 77  ? 37.925 -19.320 9.509   1.00 14.68 ?  77  VAL   B CA   1 
ATOM   5414 C C    . VAL   B 1 77  ? 36.730 -19.098 8.591   1.00 13.42 ?  77  VAL   B C    1 
ATOM   5415 O O    . VAL   B 1 77  ? 35.663 -18.656 9.036   1.00 13.53 ?  77  VAL   B O    1 
ATOM   5416 C CB   . VAL   B 1 77  ? 37.728 -20.534 10.431  1.00 16.60 ?  77  VAL   B CB   1 
ATOM   5417 C CG1  . VAL   B 1 77  ? 37.436 -21.770 9.591   1.00 17.36 ?  77  VAL   B CG1  1 
ATOM   5418 C CG2  . VAL   B 1 77  ? 38.960 -20.757 11.309  1.00 17.71 ?  77  VAL   B CG2  1 
ATOM   5419 H H    . VAL   B 1 77  ? 38.099 -18.192 11.134  1.00 17.70 ?  77  VAL   B H    1 
ATOM   5420 H HA   . VAL   B 1 77  ? 38.701 -19.485 8.951   1.00 17.77 ?  77  VAL   B HA   1 
ATOM   5421 H HB   . VAL   B 1 77  ? 36.963 -20.373 11.006  1.00 20.07 ?  77  VAL   B HB   1 
ATOM   5422 H HG11 . VAL   B 1 77  ? 37.497 -22.553 10.159  1.00 20.99 ?  77  VAL   B HG11 1 
ATOM   5423 H HG12 . VAL   B 1 77  ? 36.542 -21.702 9.219   1.00 20.99 ?  77  VAL   B HG12 1 
ATOM   5424 H HG13 . VAL   B 1 77  ? 38.089 -21.827 8.877   1.00 20.99 ?  77  VAL   B HG13 1 
ATOM   5425 H HG21 . VAL   B 1 77  ? 38.816 -21.548 11.851  1.00 21.41 ?  77  VAL   B HG21 1 
ATOM   5426 H HG22 . VAL   B 1 77  ? 39.733 -20.880 10.739  1.00 21.41 ?  77  VAL   B HG22 1 
ATOM   5427 H HG23 . VAL   B 1 77  ? 39.083 -19.982 11.878  1.00 21.41 ?  77  VAL   B HG23 1 
ATOM   5428 N N    . GLY   B 1 78  ? 36.902 -19.388 7.302   1.00 13.01 ?  78  GLY   B N    1 
ATOM   5429 C CA   . GLY   B 1 78  ? 35.921 -19.067 6.291   1.00 12.67 ?  78  GLY   B CA   1 
ATOM   5430 C C    . GLY   B 1 78  ? 36.165 -17.753 5.583   1.00 12.16 ?  78  GLY   B C    1 
ATOM   5431 O O    . GLY   B 1 78  ? 35.476 -17.468 4.600   1.00 12.38 ?  78  GLY   B O    1 
ATOM   5432 H H    . GLY   B 1 78  ? 37.597 -19.784 6.987   1.00 15.77 ?  78  GLY   B H    1 
ATOM   5433 H HA2  . GLY   B 1 78  ? 35.908 -19.766 5.623   1.00 15.35 ?  78  GLY   B HA2  1 
ATOM   5434 H HA3  . GLY   B 1 78  ? 35.040 -19.027 6.704   1.00 15.35 ?  78  GLY   B HA3  1 
ATOM   5435 N N    . GLY   B 1 79  ? 37.123 -16.949 6.053   1.00 12.18 ?  79  GLY   B N    1 
ATOM   5436 C CA   . GLY   B 1 79  ? 37.419 -15.655 5.472   1.00 11.78 ?  79  GLY   B CA   1 
ATOM   5437 C C    . GLY   B 1 79  ? 38.659 -15.674 4.592   1.00 11.14 ?  79  GLY   B C    1 
ATOM   5438 O O    . GLY   B 1 79  ? 39.273 -16.713 4.358   1.00 11.87 ?  79  GLY   B O    1 
ATOM   5439 H H    . GLY   B 1 79  ? 37.627 -17.141 6.721   1.00 14.77 ?  79  GLY   B H    1 
ATOM   5440 H HA2  . GLY   B 1 79  ? 36.667 -15.364 4.927   1.00 14.29 ?  79  GLY   B HA2  1 
ATOM   5441 H HA3  . GLY   B 1 79  ? 37.556 -15.006 6.174   1.00 14.29 ?  79  GLY   B HA3  1 
ATOM   5442 N N    . SER   B 1 80  ? 39.027 -14.483 4.110   1.00 11.06 ?  80  SER   B N    1 
ATOM   5443 C CA   . SER   B 1 80  ? 40.142 -14.357 3.180   1.00 10.76 ?  80  SER   B CA   1 
ATOM   5444 C C    . SER   B 1 80  ? 40.723 -12.952 3.231   1.00 10.57 ?  80  SER   B C    1 
ATOM   5445 O O    . SER   B 1 80  ? 40.107 -12.015 3.745   1.00 11.90 ?  80  SER   B O    1 
ATOM   5446 C CB   . SER   B 1 80  ? 39.711 -14.653 1.739   1.00 11.30 ?  80  SER   B CB   1 
ATOM   5447 O OG   . SER   B 1 80  ? 38.868 -13.637 1.230   1.00 12.38 ?  80  SER   B OG   1 
ATOM   5448 H H    . SER   B 1 80  ? 38.654 -13.741 4.309   1.00 13.42 ?  80  SER   B H    1 
ATOM   5449 H HA   . SER   B 1 80  ? 40.833 -14.991 3.429   1.00 13.06 ?  80  SER   B HA   1 
ATOM   5450 H HB2  . SER   B 1 80  ? 40.494 -14.712 1.173   1.00 13.71 ?  80  SER   B HB2  1 
ATOM   5451 H HB3  . SER   B 1 80  ? 39.226 -15.495 1.718   1.00 13.71 ?  80  SER   B HB3  1 
ATOM   5452 H HG   . SER   B 1 80  ? 38.168 -13.574 1.699   1.00 15.00 ?  80  SER   B HG   1 
ATOM   5453 N N    . CYS   B 1 81  ? 41.911 -12.809 2.641   1.00 10.64 ?  81  CYS   B N    1 
ATOM   5454 C CA   . CYS   B 1 81  ? 42.462 -11.499 2.333   1.00 11.03 ?  81  CYS   B CA   1 
ATOM   5455 C C    . CYS   B 1 81  ? 43.237 -11.587 1.028   1.00 10.03 ?  81  CYS   B C    1 
ATOM   5456 O O    . CYS   B 1 81  ? 43.736 -12.655 0.655   1.00 11.28 ?  81  CYS   B O    1 
ATOM   5457 C CB   . CYS   B 1 81  ? 43.343 -10.954 3.462   1.00 11.55 ?  81  CYS   B CB   1 
ATOM   5458 S SG   . CYS   B 1 81  ? 44.872 -11.895 3.702   1.00 11.82 ?  81  CYS   B SG   1 
ATOM   5459 H H    . CYS   B 1 81  ? 42.414 -13.464 2.391   1.00 12.92 ?  81  CYS   B H    1 
ATOM   5460 H HA   . CYS   B 1 81  ? 41.734 -10.877 2.200   1.00 13.39 ?  81  CYS   B HA   1 
ATOM   5461 H HB2  . CYS   B 1 81  ? 43.577 -10.039 3.262   1.00 14.01 ?  81  CYS   B HB2  1 
ATOM   5462 H HB3  . CYS   B 1 81  ? 42.832 -10.988 4.293   1.00 14.01 ?  81  CYS   B HB3  1 
ATOM   5463 H HG   . CYS   B 1 81  ? 45.493 -11.406 4.606   1.00 14.34 ?  81  CYS   B HG   1 
ATOM   5464 N N    . VAL   B 1 82  ? 43.346 -10.448 0.350   1.00 10.67 ?  82  VAL   B N    1 
ATOM   5465 C CA   . VAL   B 1 82  ? 44.099 -10.323 -0.891  1.00 10.60 ?  82  VAL   B CA   1 
ATOM   5466 C C    . VAL   B 1 82  ? 45.440 -9.686  -0.572  1.00 10.80 ?  82  VAL   B C    1 
ATOM   5467 O O    . VAL   B 1 82  ? 45.496 -8.568  -0.042  1.00 11.98 ?  82  VAL   B O    1 
ATOM   5468 C CB   . VAL   B 1 82  ? 43.349 -9.479  -1.932  1.00 11.68 ?  82  VAL   B CB   1 
ATOM   5469 C CG1  . VAL   B 1 82  ? 44.182 -9.334  -3.194  1.00 13.01 ?  82  VAL   B CG1  1 
ATOM   5470 C CG2  . VAL   B 1 82  ? 41.990 -10.075 -2.246  1.00 12.80 ?  82  VAL   B CG2  1 
ATOM   5471 H H    . VAL   B 1 82  ? 42.975 -9.708  0.596   1.00 12.96 ?  82  VAL   B H    1 
ATOM   5472 H HA   . VAL   B 1 82  ? 44.255 -11.199 -1.267  1.00 12.87 ?  82  VAL   B HA   1 
ATOM   5473 H HB   . VAL   B 1 82  ? 43.200 -8.593  -1.574  1.00 14.17 ?  82  VAL   B HB   1 
ATOM   5474 H HG11 . VAL   B 1 82  ? 43.616 -9.006  -3.913  1.00 15.76 ?  82  VAL   B HG11 1 
ATOM   5475 H HG12 . VAL   B 1 82  ? 44.897 -8.694  -3.028  1.00 15.76 ?  82  VAL   B HG12 1 
ATOM   5476 H HG13 . VAL   B 1 82  ? 44.555 -10.193 -3.432  1.00 15.76 ?  82  VAL   B HG13 1 
ATOM   5477 H HG21 . VAL   B 1 82  ? 41.556 -9.535  -2.930  1.00 15.51 ?  82  VAL   B HG21 1 
ATOM   5478 H HG22 . VAL   B 1 82  ? 42.105 -10.982 -2.569  1.00 15.51 ?  82  VAL   B HG22 1 
ATOM   5479 H HG23 . VAL   B 1 82  ? 41.450 -10.076 -1.440  1.00 15.51 ?  82  VAL   B HG23 1 
ATOM   5480 N N    . LEU   B 1 83  ? 46.516 -10.378 -0.934  1.00 10.55 ?  83  LEU   B N    1 
ATOM   5481 C CA   . LEU   B 1 83  ? 47.875 -9.862  -0.818  1.00 10.49 ?  83  LEU   B CA   1 
ATOM   5482 C C    . LEU   B 1 83  ? 48.575 -10.010 -2.170  1.00 10.53 ?  83  LEU   B C    1 
ATOM   5483 O O    . LEU   B 1 83  ? 47.971 -10.436 -3.160  1.00 10.63 ?  83  LEU   B O    1 
ATOM   5484 C CB   . LEU   B 1 83  ? 48.629 -10.537 0.334   1.00 10.97 ?  83  LEU   B CB   1 
ATOM   5485 C CG   . LEU   B 1 83  ? 48.128 -10.167 1.736   1.00 12.47 ?  83  LEU   B CG   1 
ATOM   5486 C CD1  . LEU   B 1 83  ? 48.774 -11.037 2.803   1.00 12.68 ?  83  LEU   B CD1  1 
ATOM   5487 C CD2  . LEU   B 1 83  ? 48.325 -8.684  2.049   1.00 13.55 ?  83  LEU   B CD2  1 
ATOM   5488 H H    . LEU   B 1 83  ? 46.475 -11.175 -1.262  1.00 12.81 ?  83  LEU   B H    1 
ATOM   5489 H HA   . LEU   B 1 83  ? 47.823 -8.912  -0.626  1.00 12.73 ?  83  LEU   B HA   1 
ATOM   5490 H HB2  . LEU   B 1 83  ? 48.545 -11.497 0.233   1.00 13.31 ?  83  LEU   B HB2  1 
ATOM   5491 H HB3  . LEU   B 1 83  ? 49.562 -10.283 0.277   1.00 13.31 ?  83  LEU   B HB3  1 
ATOM   5492 H HG   . LEU   B 1 83  ? 47.178 -10.344 1.767   1.00 15.11 ?  83  LEU   B HG   1 
ATOM   5493 H HD11 . LEU   B 1 83  ? 48.427 -10.778 3.673   1.00 15.37 ?  83  LEU   B HD11 1 
ATOM   5494 H HD12 . LEU   B 1 83  ? 48.557 -11.968 2.628   1.00 15.37 ?  83  LEU   B HD12 1 
ATOM   5495 H HD13 . LEU   B 1 83  ? 49.734 -10.912 2.780   1.00 15.37 ?  83  LEU   B HD13 1 
ATOM   5496 H HD21 . LEU   B 1 83  ? 48.128 -8.532  2.986   1.00 16.41 ?  83  LEU   B HD21 1 
ATOM   5497 H HD22 . LEU   B 1 83  ? 49.240 -8.436  1.855   1.00 16.41 ?  83  LEU   B HD22 1 
ATOM   5498 H HD23 . LEU   B 1 83  ? 47.717 -8.164  1.497   1.00 16.41 ?  83  LEU   B HD23 1 
ATOM   5499 N N    . SER   B 1 84  ? 49.852 -9.640  -2.227  1.00 11.49 ?  84  SER   B N    1 
ATOM   5500 C CA   . SER   B 1 84  ? 50.585 -9.767  -3.477  1.00 11.64 ?  84  SER   B CA   1 
ATOM   5501 C C    . SER   B 1 84  ? 50.749 -11.231 -3.879  1.00 10.70 ?  84  SER   B C    1 
ATOM   5502 O O    . SER   B 1 84  ? 50.868 -12.124 -3.038  1.00 11.08 ?  84  SER   B O    1 
ATOM   5503 C CB   . SER   B 1 84  ? 51.976 -9.153  -3.338  1.00 13.38 ?  84  SER   B CB   1 
ATOM   5504 O OG   . SER   B 1 84  ? 52.721 -9.381  -4.518  1.00 14.88 ?  84  SER   B OG   1 
ATOM   5505 H H    . SER   B 1 84  ? 50.298 -9.300  -1.569  1.00 13.94 ?  84  SER   B H    1 
ATOM   5506 H HA   . SER   B 1 84  ? 50.107 -9.302  -4.182  1.00 14.12 ?  84  SER   B HA   1 
ATOM   5507 H HB2  . SER   B 1 84  ? 51.891 -8.194  -3.199  1.00 16.21 ?  84  SER   B HB2  1 
ATOM   5508 H HB3  . SER   B 1 84  ? 52.431 -9.557  -2.583  1.00 16.21 ?  84  SER   B HB3  1 
ATOM   5509 H HG   . SER   B 1 84  ? 53.495 -9.046  -4.439  1.00 18.01 ?  84  SER   B HG   1 
ATOM   5510 N N    . GLY   B 1 85  ? 50.807 -11.465 -5.182  1.00 12.00 ?  85  GLY   B N    1 
ATOM   5511 C CA   . GLY   B 1 85  ? 51.162 -12.762 -5.708  1.00 12.70 ?  85  GLY   B CA   1 
ATOM   5512 C C    . GLY   B 1 85  ? 52.632 -12.950 -6.013  1.00 11.81 ?  85  GLY   B C    1 
ATOM   5513 O O    . GLY   B 1 85  ? 53.017 -14.035 -6.460  1.00 12.53 ?  85  GLY   B O    1 
ATOM   5514 H H    . GLY   B 1 85  ? 50.633 -10.885 -5.789  1.00 14.55 ?  85  GLY   B H    1 
ATOM   5515 H HA2  . GLY   B 1 85  ? 50.902 -13.448 -5.069  1.00 15.39 ?  85  GLY   B HA2  1 
ATOM   5516 H HA3  . GLY   B 1 85  ? 50.671 -12.922 -6.526  1.00 15.39 ?  85  GLY   B HA3  1 
ATOM   5517 N N    . HIS   B 1 86  ? 53.477 -11.944 -5.796  1.00 12.15 ?  86  HIS   B N    1 
ATOM   5518 C CA   . HIS   B 1 86  ? 54.942 -12.103 -5.888  1.00 11.75 ?  86  HIS   B CA   1 
ATOM   5519 C C    . HIS   B 1 86  ? 55.317 -12.620 -7.275  1.00 11.96 ?  86  HIS   B C    1 
ATOM   5520 O O    . HIS   B 1 86  ? 54.926 -12.009 -8.280  1.00 12.81 ?  86  HIS   B O    1 
ATOM   5521 C CB   . HIS   B 1 86  ? 55.448 -12.933 -4.709  1.00 12.63 ?  86  HIS   B CB   1 
ATOM   5522 C CG   . HIS   B 1 86  ? 55.131 -12.325 -3.386  1.00 12.68 ?  86  HIS   B CG   1 
ATOM   5523 N ND1  . HIS   B 1 86  ? 55.947 -11.398 -2.776  1.00 13.90 ?  86  HIS   B ND1  1 
ATOM   5524 C CD2  . HIS   B 1 86  ? 54.059 -12.480 -2.573  1.00 12.85 ?  86  HIS   B CD2  1 
ATOM   5525 C CE1  . HIS   B 1 86  ? 55.389 -11.010 -1.642  1.00 13.83 ?  86  HIS   B CE1  1 
ATOM   5526 N NE2  . HIS   B 1 86  ? 54.239 -11.644 -1.499  1.00 13.18 ?  86  HIS   B NE2  1 
ATOM   5527 H H    . HIS   B 1 86  ? 53.235 -11.145 -5.594  1.00 14.73 ?  86  HIS   B H    1 
ATOM   5528 H HA   . HIS   B 1 86  ? 55.348 -11.229 -5.800  1.00 14.25 ?  86  HIS   B HA   1 
ATOM   5529 H HB2  . HIS   B 1 86  ? 55.040 -13.814 -4.741  1.00 15.31 ?  86  HIS   B HB2  1 
ATOM   5530 H HB3  . HIS   B 1 86  ? 56.415 -13.020 -4.772  1.00 15.31 ?  86  HIS   B HB3  1 
ATOM   5531 H HD2  . HIS   B 1 86  ? 53.325 -13.035 -2.729  1.00 15.57 ?  86  HIS   B HD2  1 
ATOM   5532 H HE1  . HIS   B 1 86  ? 55.750 -10.405 -1.037  1.00 16.74 ?  86  HIS   B HE1  1 
ATOM   5533 H HE2  . HIS   B 1 86  ? 53.701 -11.572 -0.830  1.00 15.97 ?  86  HIS   B HE2  1 
ATOM   5534 N N    . ASN   B 1 87  ? 56.086 -13.706 -7.381  1.00 12.56 ?  87  ASN   B N    1 
ATOM   5535 C CA   . ASN   B 1 87  ? 56.484 -14.288 -8.654  1.00 13.47 ?  87  ASN   B CA   1 
ATOM   5536 C C    . ASN   B 1 87  ? 55.491 -15.320 -9.162  1.00 12.72 ?  87  ASN   B C    1 
ATOM   5537 O O    . ASN   B 1 87  ? 55.793 -16.020 -10.133 1.00 14.71 ?  87  ASN   B O    1 
ATOM   5538 C CB   . ASN   B 1 87  ? 57.876 -14.931 -8.538  1.00 15.22 ?  87  ASN   B CB   1 
ATOM   5539 C CG   . ASN   B 1 87  ? 57.936 -16.020 -7.471  1.00 15.80 ?  87  ASN   B CG   1 
ATOM   5540 O OD1  . ASN   B 1 87  ? 57.295 -15.919 -6.424  1.00 14.82 ?  87  ASN   B OD1  1 
ATOM   5541 N ND2  . ASN   B 1 87  ? 58.705 -17.081 -7.745  1.00 18.20 ?  87  ASN   B ND2  1 
ATOM   5542 H H    . ASN   B 1 87  ? 56.392 -14.138 -6.704  1.00 15.22 ?  87  ASN   B H    1 
ATOM   5543 H HA   . ASN   B 1 87  ? 56.536 -13.588 -9.315  1.00 16.31 ?  87  ASN   B HA   1 
ATOM   5544 H HB2  . ASN   B 1 87  ? 58.111 -15.335 -9.392  1.00 18.41 ?  87  ASN   B HB2  1 
ATOM   5545 H HB3  . ASN   B 1 87  ? 58.519 -14.247 -8.308  1.00 18.41 ?  87  ASN   B HB3  1 
ATOM   5546 H HD21 . ASN   B 1 87  ? 58.783 -17.716 -7.173  1.00 21.99 ?  87  ASN   B HD21 1 
ATOM   5547 H HD22 . ASN   B 1 87  ? 59.143 -17.118 -8.489  1.00 21.99 ?  87  ASN   B HD22 1 
ATOM   5548 N N    . LEU   B 1 88  ? 54.320 -15.432 -8.532  1.00 12.00 ?  88  LEU   B N    1 
ATOM   5549 C CA   . LEU   B 1 88  ? 53.342 -16.460 -8.860  1.00 12.47 ?  88  LEU   B CA   1 
ATOM   5550 C C    . LEU   B 1 88  ? 52.112 -15.936 -9.582  1.00 12.05 ?  88  LEU   B C    1 
ATOM   5551 O O    . LEU   B 1 88  ? 51.508 -16.677 -10.364 1.00 13.77 ?  88  LEU   B O    1 
ATOM   5552 C CB   . LEU   B 1 88  ? 52.871 -17.144 -7.575  1.00 13.46 ?  88  LEU   B CB   1 
ATOM   5553 C CG   . LEU   B 1 88  ? 53.994 -17.808 -6.785  1.00 15.94 ?  88  LEU   B CG   1 
ATOM   5554 C CD1  . LEU   B 1 88  ? 53.521 -18.192 -5.395  1.00 17.43 ?  88  LEU   B CD1  1 
ATOM   5555 C CD2  . LEU   B 1 88  ? 54.508 -19.019 -7.540  1.00 19.20 ?  88  LEU   B CD2  1 
ATOM   5556 H H    . LEU   B 1 88  ? 54.066 -14.914 -7.888  1.00 14.55 ?  88  LEU   B H    1 
ATOM   5557 H HA   . LEU   B 1 88  ? 53.759 -17.127 -9.421  1.00 15.11 ?  88  LEU   B HA   1 
ATOM   5558 H HB2  . LEU   B 1 88  ? 52.453 -16.480 -7.001  1.00 16.31 ?  88  LEU   B HB2  1 
ATOM   5559 H HB3  . LEU   B 1 88  ? 52.221 -17.828 -7.806  1.00 16.31 ?  88  LEU   B HB3  1 
ATOM   5560 H HG   . LEU   B 1 88  ? 54.724 -17.179 -6.689  1.00 19.28 ?  88  LEU   B HG   1 
ATOM   5561 H HD11 . LEU   B 1 88  ? 54.198 -18.743 -4.974  1.00 21.06 ?  88  LEU   B HD11 1 
ATOM   5562 H HD12 . LEU   B 1 88  ? 53.376 -17.387 -4.876  1.00 21.06 ?  88  LEU   B HD12 1 
ATOM   5563 H HD13 . LEU   B 1 88  ? 52.692 -18.689 -5.474  1.00 21.06 ?  88  LEU   B HD13 1 
ATOM   5564 H HD21 . LEU   B 1 88  ? 55.142 -19.492 -6.977  1.00 23.19 ?  88  LEU   B HD21 1 
ATOM   5565 H HD22 . LEU   B 1 88  ? 53.763 -19.597 -7.759  1.00 23.19 ?  88  LEU   B HD22 1 
ATOM   5566 H HD23 . LEU   B 1 88  ? 54.948 -18.722 -8.353  1.00 23.19 ?  88  LEU   B HD23 1 
ATOM   5567 N N    . ALA   B 1 89  ? 51.701 -14.704 -9.309  1.00 11.54 ?  89  ALA   B N    1 
ATOM   5568 C CA   . ALA   B 1 89  ? 50.408 -14.207 -9.756  1.00 11.04 ?  89  ALA   B CA   1 
ATOM   5569 C C    . ALA   B 1 89  ? 50.397 -12.718 -9.468  1.00 11.42 ?  89  ALA   B C    1 
ATOM   5570 O O    . ALA   B 1 89  ? 51.230 -12.217 -8.715  1.00 12.16 ?  89  ALA   B O    1 
ATOM   5571 C CB   . ALA   B 1 89  ? 49.278 -14.881 -8.985  1.00 11.26 ?  89  ALA   B CB   1 
ATOM   5572 H H    . ALA   B 1 89  ? 52.154 -14.129 -8.859  1.00 14.00 ?  89  ALA   B H    1 
ATOM   5573 H HA   . ALA   B 1 89  ? 50.289 -14.357 -10.714 1.00 13.39 ?  89  ALA   B HA   1 
ATOM   5574 H HB1  . ALA   B 1 89  ? 48.431 -14.538 -9.307  1.00 13.66 ?  89  ALA   B HB1  1 
ATOM   5575 H HB2  . ALA   B 1 89  ? 49.328 -15.838 -9.133  1.00 13.66 ?  89  ALA   B HB2  1 
ATOM   5576 H HB3  . ALA   B 1 89  ? 49.385 -14.682 -8.045  1.00 13.66 ?  89  ALA   B HB3  1 
ATOM   5577 N N    . LYS   B 1 90  ? 49.425 -12.011 -10.036 1.00 12.39 ?  90  LYS   B N    1 
ATOM   5578 C CA   . LYS   B 1 90  ? 49.244 -10.624 -9.625  1.00 12.48 ?  90  LYS   B CA   1 
ATOM   5579 C C    . LYS   B 1 90  ? 48.913 -10.550 -8.138  1.00 11.79 ?  90  LYS   B C    1 
ATOM   5580 O O    . LYS   B 1 90  ? 49.547 -9.797  -7.382  1.00 12.72 ?  90  LYS   B O    1 
ATOM   5581 C CB   . LYS   B 1 90  ? 48.173 -9.957  -10.488 1.00 13.74 ?  90  LYS   B CB   1 
ATOM   5582 C CG   . LYS   B 1 90  ? 47.871 -8.524  -10.103 1.00 14.27 ?  90  LYS   B CG   1 
ATOM   5583 C CD   . LYS   B 1 90  ? 49.080 -7.627  -10.149 1.00 16.92 ?  90  LYS   B CD   1 
ATOM   5584 C CE   . LYS   B 1 90  ? 48.613 -6.223  -9.858  1.00 19.27 ?  90  LYS   B CE   1 
ATOM   5585 N NZ   . LYS   B 1 90  ? 49.728 -5.251  -9.798  1.00 19.50 ?  90  LYS   B NZ   1 
ATOM   5586 H H    . LYS   B 1 90  ? 48.880 -12.300 -10.634 1.00 15.02 ?  90  LYS   B H    1 
ATOM   5587 H HA   . LYS   B 1 90  ? 50.076 -10.152 -9.766  1.00 15.12 ?  90  LYS   B HA   1 
ATOM   5588 H HB2  . LYS   B 1 90  ? 48.471 -9.960  -11.413 1.00 16.64 ?  90  LYS   B HB2  1 
ATOM   5589 H HB3  . LYS   B 1 90  ? 47.348 -10.466 -10.413 1.00 16.64 ?  90  LYS   B HB3  1 
ATOM   5590 H HG2  . LYS   B 1 90  ? 47.213 -8.166  -10.719 1.00 17.27 ?  90  LYS   B HG2  1 
ATOM   5591 H HG3  . LYS   B 1 90  ? 47.517 -8.506  -9.199  1.00 17.27 ?  90  LYS   B HG3  1 
ATOM   5592 H HD2  . LYS   B 1 90  ? 49.722 -7.893  -9.467  1.00 20.46 ?  90  LYS   B HD2  1 
ATOM   5593 H HD3  . LYS   B 1 90  ? 49.484 -7.653  -11.031 1.00 20.46 ?  90  LYS   B HD3  1 
ATOM   5594 H HE2  . LYS   B 1 90  ? 48.005 -5.941  -10.561 1.00 23.28 ?  90  LYS   B HE2  1 
ATOM   5595 H HE3  . LYS   B 1 90  ? 48.157 -6.210  -9.002  1.00 23.28 ?  90  LYS   B HE3  1 
ATOM   5596 H HZ1  . LYS   B 1 90  ? 49.415 -4.434  -9.629  1.00 23.55 ?  90  LYS   B HZ1  1 
ATOM   5597 H HZ2  . LYS   B 1 90  ? 50.301 -5.479  -9.157  1.00 23.55 ?  90  LYS   B HZ2  1 
ATOM   5598 H HZ3  . LYS   B 1 90  ? 50.162 -5.233  -10.578 1.00 23.55 ?  90  LYS   B HZ3  1 
ATOM   5599 N N    . HIS   B 1 91  ? 47.941 -11.356 -7.698  1.00 10.57 ?  91  HIS   B N    1 
ATOM   5600 C CA   . HIS   B 1 91  ? 47.470 -11.383 -6.326  1.00 10.75 ?  91  HIS   B CA   1 
ATOM   5601 C C    . HIS   B 1 91  ? 47.462 -12.810 -5.803  1.00 9.84  ?  91  HIS   B C    1 
ATOM   5602 O O    . HIS   B 1 91  ? 47.229 -13.761 -6.558  1.00 10.60 ?  91  HIS   B O    1 
ATOM   5603 C CB   . HIS   B 1 91  ? 46.018 -10.896 -6.217  1.00 12.42 ?  91  HIS   B CB   1 
ATOM   5604 C CG   . HIS   B 1 91  ? 45.816 -9.485  -6.642  1.00 15.58 ?  91  HIS   B CG   1 
ATOM   5605 N ND1  . HIS   B 1 91  ? 46.440 -8.420  -6.028  1.00 18.11 ?  91  HIS   B ND1  1 
ATOM   5606 C CD2  . HIS   B 1 91  ? 45.017 -8.956  -7.593  1.00 17.78 ?  91  HIS   B CD2  1 
ATOM   5607 C CE1  . HIS   B 1 91  ? 46.060 -7.294  -6.607  1.00 18.98 ?  91  HIS   B CE1  1 
ATOM   5608 N NE2  . HIS   B 1 91  ? 45.188 -7.593  -7.554  1.00 19.20 ?  91  HIS   B NE2  1 
ATOM   5609 H H    . HIS   B 1 91  ? 47.519 -11.906 -8.208  1.00 12.83 ?  91  HIS   B H    1 
ATOM   5610 H HA   . HIS   B 1 91  ? 48.037 -10.828 -5.761  1.00 13.05 ?  91  HIS   B HA   1 
ATOM   5611 H HB2  . HIS   B 1 91  ? 45.456 -11.454 -6.781  1.00 15.05 ?  91  HIS   B HB2  1 
ATOM   5612 H HB3  . HIS   B 1 91  ? 45.726 -10.972 -5.293  1.00 15.05 ?  91  HIS   B HB3  1 
ATOM   5613 H HD1  . HIS   B 1 91  ? 47.004 -8.475  -5.380  1.00 21.88 ?  91  HIS   B HD1  1 
ATOM   5614 H HD2  . HIS   B 1 91  ? 44.460 -9.415  -8.176  1.00 21.49 ?  91  HIS   B HD2  1 
ATOM   5615 H HE1  . HIS   B 1 91  ? 46.345 -6.434  -6.376  1.00 22.93 ?  91  HIS   B HE1  1 
ATOM   5616 N N    . CYS   B 1 92  ? 47.656 -12.946 -4.505  1.00 9.71  ?  92  CYS   B N    1 
ATOM   5617 C CA   . CYS   B 1 92  ? 47.351 -14.180 -3.795  1.00 9.75  ?  92  CYS   B CA   1 
ATOM   5618 C C    . CYS   B 1 92  ? 46.128 -13.947 -2.915  1.00 9.44  ?  92  CYS   B C    1 
ATOM   5619 O O    . CYS   B 1 92  ? 46.121 -13.038 -2.074  1.00 10.37 ?  92  CYS   B O    1 
ATOM   5620 C CB   . CYS   B 1 92  ? 48.532 -14.648 -2.949  1.00 10.25 ?  92  CYS   B CB   1 
ATOM   5621 S SG   . CYS   B 1 92  ? 48.158 -16.177 -2.038  1.00 10.57 ?  92  CYS   B SG   1 
ATOM   5622 H H    . CYS   B 1 92  ? 47.988 -12.329 -4.001  1.00 11.81 ?  92  CYS   B H    1 
ATOM   5623 H HA   . CYS   B 1 92  ? 47.145 -14.875 -4.443  1.00 11.85 ?  92  CYS   B HA   1 
ATOM   5624 H HB2  . CYS   B 1 92  ? 49.289 -14.816 -3.528  1.00 12.45 ?  92  CYS   B HB2  1 
ATOM   5625 H HB3  . CYS   B 1 92  ? 48.746 -13.957 -2.305  1.00 12.45 ?  92  CYS   B HB3  1 
ATOM   5626 H HG   . CYS   B 1 92  ? 49.130 -16.497 -1.414  1.00 12.83 ?  92  CYS   B HG   1 
ATOM   5627 N N    . LEU   B 1 93  ? 45.092 -14.757 -3.126  1.00 9.21  ?  93  LEU   B N    1 
ATOM   5628 C CA   . LEU   B 1 93  ? 43.910 -14.759 -2.273  1.00 9.43  ?  93  LEU   B CA   1 
ATOM   5629 C C    . LEU   B 1 93  ? 44.132 -15.819 -1.204  1.00 9.13  ?  93  LEU   B C    1 
ATOM   5630 O O    . LEU   B 1 93  ? 44.094 -17.021 -1.495  1.00 9.89  ?  93  LEU   B O    1 
ATOM   5631 C CB   . LEU   B 1 93  ? 42.642 -15.048 -3.075  1.00 9.95  ?  93  LEU   B CB   1 
ATOM   5632 C CG   . LEU   B 1 93  ? 41.346 -15.068 -2.260  1.00 10.65 ?  93  LEU   B CG   1 
ATOM   5633 C CD1  . LEU   B 1 93  ? 40.983 -13.674 -1.761  1.00 11.12 ?  93  LEU   B CD1  1 
ATOM   5634 C CD2  . LEU   B 1 93  ? 40.214 -15.654 -3.076  1.00 11.05 ?  93  LEU   B CD2  1 
ATOM   5635 H H    . LEU   B 1 93  ? 45.050 -15.333 -3.776  1.00 11.20 ?  93  LEU   B H    1 
ATOM   5636 H HA   . LEU   B 1 93  ? 43.817 -13.898 -1.848  1.00 11.46 ?  93  LEU   B HA   1 
ATOM   5637 H HB2  . LEU   B 1 93  ? 42.543 -14.358 -3.755  1.00 12.10 ?  93  LEU   B HB2  1 
ATOM   5638 H HB3  . LEU   B 1 93  ? 42.729 -15.911 -3.502  1.00 12.10 ?  93  LEU   B HB3  1 
ATOM   5639 H HG   . LEU   B 1 93  ? 41.468 -15.631 -1.483  1.00 12.94 ?  93  LEU   B HG   1 
ATOM   5640 H HD11 . LEU   B 1 93  ? 40.135 -13.715 -1.293  1.00 13.49 ?  93  LEU   B HD11 1 
ATOM   5641 H HD12 . LEU   B 1 93  ? 41.678 -13.359 -1.167  1.00 13.49 ?  93  LEU   B HD12 1 
ATOM   5642 H HD13 . LEU   B 1 93  ? 40.905 -13.076 -2.527  1.00 13.49 ?  93  LEU   B HD13 1 
ATOM   5643 H HD21 . LEU   B 1 93  ? 39.401 -15.647 -2.543  1.00 13.42 ?  93  LEU   B HD21 1 
ATOM   5644 H HD22 . LEU   B 1 93  ? 40.088 -15.121 -3.876  1.00 13.42 ?  93  LEU   B HD22 1 
ATOM   5645 H HD23 . LEU   B 1 93  ? 40.440 -16.566 -3.319  1.00 13.42 ?  93  LEU   B HD23 1 
ATOM   5646 N N    . HIS   B 1 94  ? 44.397 -15.382 0.021   1.00 9.28  ?  94  HIS   B N    1 
ATOM   5647 C CA   . HIS   B 1 94  ? 44.621 -16.286 1.142   1.00 9.36  ?  94  HIS   B CA   1 
ATOM   5648 C C    . HIS   B 1 94  ? 43.259 -16.634 1.725   1.00 9.81  ?  94  HIS   B C    1 
ATOM   5649 O O    . HIS   B 1 94  ? 42.588 -15.757 2.273   1.00 11.09 ?  94  HIS   B O    1 
ATOM   5650 C CB   . HIS   B 1 94  ? 45.494 -15.611 2.198   1.00 9.92  ?  94  HIS   B CB   1 
ATOM   5651 C CG   . HIS   B 1 94  ? 46.877 -15.315 1.729   1.00 9.71  ?  94  HIS   B CG   1 
ATOM   5652 N ND1  . HIS   B 1 94  ? 47.903 -16.229 1.816   1.00 10.03 ?  94  HIS   B ND1  1 
ATOM   5653 C CD2  . HIS   B 1 94  ? 47.384 -14.207 1.131   1.00 10.12 ?  94  HIS   B CD2  1 
ATOM   5654 C CE1  . HIS   B 1 94  ? 48.993 -15.679 1.309   1.00 9.81  ?  94  HIS   B CE1  1 
ATOM   5655 N NE2  . HIS   B 1 94  ? 48.708 -14.457 0.883   1.00 10.39 ?  94  HIS   B NE2  1 
ATOM   5656 H H    . HIS   B 1 94  ? 44.459 -14.544 0.229   1.00 11.29 ?  94  HIS   B H    1 
ATOM   5657 H HA   . HIS   B 1 94  ? 45.054 -17.096 0.836   1.00 11.38 ?  94  HIS   B HA   1 
ATOM   5658 H HB2  . HIS   B 1 94  ? 45.082 -14.773 2.456   1.00 12.06 ?  94  HIS   B HB2  1 
ATOM   5659 H HB3  . HIS   B 1 94  ? 45.565 -16.197 2.965   1.00 12.06 ?  94  HIS   B HB3  1 
ATOM   5660 H HD2  . HIS   B 1 94  ? 46.932 -13.421 0.931   1.00 12.29 ?  94  HIS   B HD2  1 
ATOM   5661 H HE1  . HIS   B 1 94  ? 49.825 -16.096 1.254   1.00 11.93 ?  94  HIS   B HE1  1 
ATOM   5662 H HE2  . HIS   B 1 94  ? 49.268 -13.918 0.517   1.00 12.62 ?  94  HIS   B HE2  1 
ATOM   5663 N N    . VAL   B 1 95  ? 42.826 -17.889 1.573   1.00 9.74  ?  95  VAL   B N    1 
ATOM   5664 C CA   . VAL   B 1 95  ? 41.497 -18.320 2.006   1.00 9.92  ?  95  VAL   B CA   1 
ATOM   5665 C C    . VAL   B 1 95  ? 41.659 -19.354 3.103   1.00 10.04 ?  95  VAL   B C    1 
ATOM   5666 O O    . VAL   B 1 95  ? 42.429 -20.308 2.947   1.00 10.75 ?  95  VAL   B O    1 
ATOM   5667 C CB   . VAL   B 1 95  ? 40.675 -18.928 0.853   1.00 10.01 ?  95  VAL   B CB   1 
ATOM   5668 C CG1  . VAL   B 1 95  ? 39.307 -19.377 1.349   1.00 11.32 ?  95  VAL   B CG1  1 
ATOM   5669 C CG2  . VAL   B 1 95  ? 40.547 -17.950 -0.289  1.00 10.27 ?  95  VAL   B CG2  1 
ATOM   5670 H H    . VAL   B 1 95  ? 43.290 -18.518 1.210   1.00 11.84 ?  95  VAL   B H    1 
ATOM   5671 H HA   . VAL   B 1 95  ? 41.010 -17.562 2.364   1.00 12.06 ?  95  VAL   B HA   1 
ATOM   5672 H HB   . VAL   B 1 95  ? 41.136 -19.708 0.519   1.00 12.16 ?  95  VAL   B HB   1 
ATOM   5673 H HG11 . VAL   B 1 95  ? 38.732 -19.550 0.583   1.00 13.74 ?  95  VAL   B HG11 1 
ATOM   5674 H HG12 . VAL   B 1 95  ? 39.404 -20.187 1.873   1.00 13.74 ?  95  VAL   B HG12 1 
ATOM   5675 H HG13 . VAL   B 1 95  ? 38.916 -18.674 1.895   1.00 13.74 ?  95  VAL   B HG13 1 
ATOM   5676 H HG21 . VAL   B 1 95  ? 39.970 -18.340 -0.966  1.00 12.47 ?  95  VAL   B HG21 1 
ATOM   5677 H HG22 . VAL   B 1 95  ? 40.157 -17.129 0.046   1.00 12.47 ?  95  VAL   B HG22 1 
ATOM   5678 H HG23 . VAL   B 1 95  ? 41.425 -17.782 -0.653  1.00 12.47 ?  95  VAL   B HG23 1 
ATOM   5679 N N    . VAL   B 1 96  ? 40.928 -19.179 4.196   1.00 10.55 ?  96  VAL   B N    1 
ATOM   5680 C CA   . VAL   B 1 96  ? 41.010 -20.089 5.337   1.00 11.19 ?  96  VAL   B CA   1 
ATOM   5681 C C    . VAL   B 1 96  ? 39.822 -21.051 5.293   1.00 11.75 ?  96  VAL   B C    1 
ATOM   5682 O O    . VAL   B 1 96  ? 38.704 -20.701 5.679   1.00 12.22 ?  96  VAL   B O    1 
ATOM   5683 C CB   . VAL   B 1 96  ? 41.067 -19.336 6.667   1.00 11.76 ?  96  VAL   B CB   1 
ATOM   5684 C CG1  . VAL   B 1 96  ? 41.217 -20.325 7.817   1.00 12.17 ?  96  VAL   B CG1  1 
ATOM   5685 C CG2  . VAL   B 1 96  ? 42.198 -18.318 6.673   1.00 12.31 ?  96  VAL   B CG2  1 
ATOM   5686 H H    . VAL   B 1 96  ? 40.361 -18.539 4.307   1.00 12.81 ?  96  VAL   B H    1 
ATOM   5687 H HA   . VAL   B 1 96  ? 41.823 -20.617 5.263   1.00 13.58 ?  96  VAL   B HA   1 
ATOM   5688 H HB   . VAL   B 1 96  ? 40.232 -18.857 6.795   1.00 14.26 ?  96  VAL   B HB   1 
ATOM   5689 H HG11 . VAL   B 1 96  ? 41.419 -19.835 8.633   1.00 14.76 ?  96  VAL   B HG11 1 
ATOM   5690 H HG12 . VAL   B 1 96  ? 40.386 -20.815 7.931   1.00 14.76 ?  96  VAL   B HG12 1 
ATOM   5691 H HG13 . VAL   B 1 96  ? 41.939 -20.940 7.617   1.00 14.76 ?  96  VAL   B HG13 1 
ATOM   5692 H HG21 . VAL   B 1 96  ? 42.250 -17.901 7.548   1.00 14.92 ?  96  VAL   B HG21 1 
ATOM   5693 H HG22 . VAL   B 1 96  ? 43.033 -18.767 6.471   1.00 14.92 ?  96  VAL   B HG22 1 
ATOM   5694 H HG23 . VAL   B 1 96  ? 42.018 -17.640 5.999   1.00 14.92 ?  96  VAL   B HG23 1 
ATOM   5695 N N    . GLY   B 1 97  ? 40.055 -22.283 4.846   1.00 11.57 ?  97  GLY   B N    1 
ATOM   5696 C CA   . GLY   B 1 97  ? 39.080 -23.340 5.014   1.00 12.49 ?  97  GLY   B CA   1 
ATOM   5697 C C    . GLY   B 1 97  ? 39.212 -23.955 6.393   1.00 13.79 ?  97  GLY   B C    1 
ATOM   5698 O O    . GLY   B 1 97  ? 40.259 -23.839 7.046   1.00 14.36 ?  97  GLY   B O    1 
ATOM   5699 H H    . GLY   B 1 97  ? 40.776 -22.525 4.436   1.00 14.04 ?  97  GLY   B H    1 
ATOM   5700 H HA2  . GLY   B 1 97  ? 38.186 -22.971 4.900   1.00 15.13 ?  97  GLY   B HA2  1 
ATOM   5701 H HA3  . GLY   B 1 97  ? 39.219 -24.024 4.338   1.00 15.13 ?  97  GLY   B HA3  1 
ATOM   5702 N N    . PRO   B 1 98  ? 38.163 -24.633 6.863   1.00 14.67 ?  98  PRO   B N    1 
ATOM   5703 C CA   . PRO   B 1 98  ? 38.260 -25.332 8.149   1.00 16.45 ?  98  PRO   B CA   1 
ATOM   5704 C C    . PRO   B 1 98  ? 39.288 -26.453 8.096   1.00 15.79 ?  98  PRO   B C    1 
ATOM   5705 O O    . PRO   B 1 98  ? 39.391 -27.182 7.112   1.00 15.91 ?  98  PRO   B O    1 
ATOM   5706 C CB   . PRO   B 1 98  ? 36.840 -25.874 8.362   1.00 17.03 ?  98  PRO   B CB   1 
ATOM   5707 C CG   . PRO   B 1 98  ? 36.258 -25.982 7.001   1.00 16.41 ?  98  PRO   B CG   1 
ATOM   5708 C CD   . PRO   B 1 98  ? 36.841 -24.821 6.232   1.00 15.33 ?  98  PRO   B CD   1 
ATOM   5709 H HA   . PRO   B 1 98  ? 38.482 -24.708 8.853   1.00 19.89 ?  98  PRO   B HA   1 
ATOM   5710 H HB2  . PRO   B 1 98  ? 36.886 -26.746 8.783   1.00 20.58 ?  98  PRO   B HB2  1 
ATOM   5711 H HB3  . PRO   B 1 98  ? 36.329 -25.254 8.901   1.00 20.58 ?  98  PRO   B HB3  1 
ATOM   5712 H HG2  . PRO   B 1 98  ? 36.520 -26.828 6.597   1.00 19.85 ?  98  PRO   B HG2  1 
ATOM   5713 H HG3  . PRO   B 1 98  ? 35.291 -25.915 7.050   1.00 19.85 ?  98  PRO   B HG3  1 
ATOM   5714 H HD2  . PRO   B 1 98  ? 36.933 -25.052 5.289   1.00 18.55 ?  98  PRO   B HD2  1 
ATOM   5715 H HD3  . PRO   B 1 98  ? 36.290 -24.030 6.345   1.00 18.55 ?  98  PRO   B HD3  1 
ATOM   5716 N N    . ASN   B 1 99  ? 40.053 -26.582 9.175   1.00 17.44 ?  99  ASN   B N    1 
ATOM   5717 C CA   . ASN   B 1 99  ? 41.033 -27.656 9.329   1.00 18.44 ?  99  ASN   B CA   1 
ATOM   5718 C C    . ASN   B 1 99  ? 40.418 -28.729 10.224  1.00 21.11 ?  99  ASN   B C    1 
ATOM   5719 O O    . ASN   B 1 99  ? 40.358 -28.573 11.446  1.00 21.85 ?  99  ASN   B O    1 
ATOM   5720 C CB   . ASN   B 1 99  ? 42.317 -27.095 9.927   1.00 18.53 ?  99  ASN   B CB   1 
ATOM   5721 C CG   . ASN   B 1 99  ? 43.448 -28.102 9.940   1.00 19.27 ?  99  ASN   B CG   1 
ATOM   5722 O OD1  . ASN   B 1 99  ? 43.229 -29.291 10.127  1.00 20.33 ?  99  ASN   B OD1  1 
ATOM   5723 N ND2  . ASN   B 1 99  ? 44.665 -27.629 9.735   1.00 19.65 ?  99  ASN   B ND2  1 
ATOM   5724 H H    . ASN   B 1 99  ? 40.021 -26.045 9.843   1.00 21.07 ?  99  ASN   B H    1 
ATOM   5725 H HA   . ASN   B 1 99  ? 41.226 -28.050 8.465   1.00 22.28 ?  99  ASN   B HA   1 
ATOM   5726 H HB2  . ASN   B 1 99  ? 42.593 -26.333 9.406   1.00 22.39 ?  99  ASN   B HB2  1 
ATOM   5727 H HB3  . ASN   B 1 99  ? 42.140 -26.834 10.844  1.00 22.39 ?  99  ASN   B HB3  1 
ATOM   5728 H HD21 . ASN   B 1 99  ? 45.338 -28.161 9.729   1.00 23.73 ?  99  ASN   B HD21 1 
ATOM   5729 H HD22 . ASN   B 1 99  ? 44.775 -26.786 9.615   1.00 23.73 ?  99  ASN   B HD22 1 
ATOM   5730 N N    A VAL   B 1 100 ? 39.943 -29.815 9.605   0.34 23.67 ?  100 VAL   B N    1 
ATOM   5731 N N    B VAL   B 1 100 ? 39.958 -29.819 9.603   0.66 23.42 ?  100 VAL   B N    1 
ATOM   5732 C CA   A VAL   B 1 100 ? 39.333 -30.900 10.372  0.34 26.20 ?  100 VAL   B CA   1 
ATOM   5733 C CA   B VAL   B 1 100 ? 39.336 -30.905 10.358  0.66 26.10 ?  100 VAL   B CA   1 
ATOM   5734 C C    A VAL   B 1 100 ? 40.351 -31.555 11.297  0.34 27.03 ?  100 VAL   B C    1 
ATOM   5735 C C    B VAL   B 1 100 ? 40.346 -31.581 11.277  0.66 26.71 ?  100 VAL   B C    1 
ATOM   5736 O O    A VAL   B 1 100 ? 39.999 -32.025 12.386  0.34 27.74 ?  100 VAL   B O    1 
ATOM   5737 O O    B VAL   B 1 100 ? 39.980 -32.100 12.340  0.66 27.64 ?  100 VAL   B O    1 
ATOM   5738 C CB   A VAL   B 1 100 ? 38.658 -31.915 9.425   0.34 27.80 ?  100 VAL   B CB   1 
ATOM   5739 C CB   B VAL   B 1 100 ? 38.657 -31.899 9.395   0.66 28.31 ?  100 VAL   B CB   1 
ATOM   5740 C CG1  A VAL   B 1 100 ? 38.159 -33.130 10.194  0.34 28.35 ?  100 VAL   B CG1  1 
ATOM   5741 C CG1  B VAL   B 1 100 ? 38.187 -33.141 10.139  0.66 29.10 ?  100 VAL   B CG1  1 
ATOM   5742 C CG2  A VAL   B 1 100 ? 37.507 -31.253 8.678   0.34 28.28 ?  100 VAL   B CG2  1 
ATOM   5743 C CG2  B VAL   B 1 100 ? 37.488 -31.228 8.691   0.66 28.91 ?  100 VAL   B CG2  1 
ATOM   5744 H H    A VAL   B 1 100 ? 39.954 -29.942 8.751   0.34 28.56 ?  100 VAL   B H    1 
ATOM   5745 H H    B VAL   B 1 100 ? 39.990 -29.949 8.752   0.66 28.26 ?  100 VAL   B H    1 
ATOM   5746 H HA   A VAL   B 1 100 ? 38.632 -30.525 10.928  0.34 31.60 ?  100 VAL   B HA   1 
ATOM   5747 H HA   B VAL   B 1 100 ? 38.639 -30.529 10.915  0.66 31.47 ?  100 VAL   B HA   1 
ATOM   5748 H HB   A VAL   B 1 100 ? 39.306 -32.221 8.773   0.34 33.51 ?  100 VAL   B HB   1 
ATOM   5749 H HB   B VAL   B 1 100 ? 39.294 -32.181 8.721   0.66 34.13 ?  100 VAL   B HB   1 
ATOM   5750 H HG11 A VAL   B 1 100 ? 37.566 -33.643 9.620   0.34 34.17 ?  100 VAL   B HG11 1 
ATOM   5751 H HG11 B VAL   B 1 100 ? 37.576 -33.637 9.569   0.66 35.07 ?  100 VAL   B HG11 1 
ATOM   5752 H HG12 A VAL   B 1 100 ? 38.916 -33.676 10.455  0.34 34.17 ?  100 VAL   B HG12 1 
ATOM   5753 H HG12 B VAL   B 1 100 ? 38.954 -33.694 10.355  0.66 35.07 ?  100 VAL   B HG12 1 
ATOM   5754 H HG13 A VAL   B 1 100 ? 37.676 -32.831 10.980  0.34 34.17 ?  100 VAL   B HG13 1 
ATOM   5755 H HG13 B VAL   B 1 100 ? 37.731 -32.871 10.950  0.66 35.07 ?  100 VAL   B HG13 1 
ATOM   5756 H HG21 A VAL   B 1 100 ? 37.083 -31.911 8.105   0.34 34.09 ?  100 VAL   B HG21 1 
ATOM   5757 H HG21 B VAL   B 1 100 ? 37.062 -31.870 8.102   0.66 34.84 ?  100 VAL   B HG21 1 
ATOM   5758 H HG22 A VAL   B 1 100 ? 36.865 -30.915 9.323   0.34 34.09 ?  100 VAL   B HG22 1 
ATOM   5759 H HG22 B VAL   B 1 100 ? 36.854 -30.920 9.358   0.66 34.84 ?  100 VAL   B HG22 1 
ATOM   5760 H HG23 A VAL   B 1 100 ? 37.856 -30.524 8.145   0.34 34.09 ?  100 VAL   B HG23 1 
ATOM   5761 H HG23 B VAL   B 1 100 ? 37.821 -30.477 8.178   0.66 34.84 ?  100 VAL   B HG23 1 
ATOM   5762 N N    . ASN   B 1 101 ? 41.623 -31.602 10.889  1.00 27.36 ?  101 ASN   B N    1 
ATOM   5763 C CA   . ASN   B 1 101 ? 42.663 -32.130 11.768  1.00 29.34 ?  101 ASN   B CA   1 
ATOM   5764 C C    . ASN   B 1 101 ? 42.851 -31.276 13.015  1.00 33.18 ?  101 ASN   B C    1 
ATOM   5765 O O    . ASN   B 1 101 ? 43.487 -31.735 13.972  1.00 33.92 ?  101 ASN   B O    1 
ATOM   5766 C CB   . ASN   B 1 101 ? 43.984 -32.283 11.010  1.00 28.87 ?  101 ASN   B CB   1 
ATOM   5767 C CG   . ASN   B 1 101 ? 43.961 -33.445 10.029  1.00 28.22 ?  101 ASN   B CG   1 
ATOM   5768 O OD1  . ASN   B 1 101 ? 43.224 -34.414 10.216  1.00 28.91 ?  101 ASN   B OD1  1 
ATOM   5769 N ND2  . ASN   B 1 101 ? 44.767 -33.351 8.977   1.00 27.74 ?  101 ASN   B ND2  1 
ATOM   5770 H H    A ASN   B 1 101 ? 41.901 -31.342 10.118  0.34 32.98 ?  101 ASN   B H    1 
ATOM   5771 H H    B ASN   B 1 101 ? 41.906 -31.323 10.126  0.66 32.98 ?  101 ASN   B H    1 
ATOM   5772 H HA   . ASN   B 1 101 ? 42.393 -33.012 12.059  1.00 35.36 ?  101 ASN   B HA   1 
ATOM   5773 H HB2  . ASN   B 1 101 ? 44.163 -31.470 10.512  1.00 34.79 ?  101 ASN   B HB2  1 
ATOM   5774 H HB3  . ASN   B 1 101 ? 44.696 -32.446 11.646  1.00 34.79 ?  101 ASN   B HB3  1 
ATOM   5775 H HD21 . ASN   B 1 101 ? 44.788 -33.984 8.394   1.00 33.44 ?  101 ASN   B HD21 1 
ATOM   5776 H HD22 . ASN   B 1 101 ? 45.273 -32.662 8.882   1.00 33.44 ?  101 ASN   B HD22 1 
ATOM   5777 N N    A LYS   B 1 102 ? 42.323 -30.051 13.022  0.34 35.20 ?  102 LYS   B N    1 
ATOM   5778 N N    B LYS   B 1 102 ? 42.323 -30.052 13.023  0.66 35.13 ?  102 LYS   B N    1 
ATOM   5779 C CA   A LYS   B 1 102 ? 42.274 -29.208 14.209  0.34 37.08 ?  102 LYS   B CA   1 
ATOM   5780 C CA   B LYS   B 1 102 ? 42.272 -29.214 14.212  0.66 37.15 ?  102 LYS   B CA   1 
ATOM   5781 C C    A LYS   B 1 102 ? 40.897 -29.207 14.864  0.34 36.66 ?  102 LYS   B C    1 
ATOM   5782 C C    B LYS   B 1 102 ? 40.879 -29.169 14.826  0.66 36.48 ?  102 LYS   B C    1 
ATOM   5783 O O    A LYS   B 1 102 ? 40.669 -28.437 15.802  0.34 36.81 ?  102 LYS   B O    1 
ATOM   5784 O O    B LYS   B 1 102 ? 40.619 -28.324 15.689  0.66 36.50 ?  102 LYS   B O    1 
ATOM   5785 C CB   A LYS   B 1 102 ? 42.668 -27.771 13.861  0.34 39.25 ?  102 LYS   B CB   1 
ATOM   5786 C CB   B LYS   B 1 102 ? 42.730 -27.792 13.885  0.66 39.86 ?  102 LYS   B CB   1 
ATOM   5787 C CG   A LYS   B 1 102 ? 44.126 -27.571 13.486  0.34 41.11 ?  102 LYS   B CG   1 
ATOM   5788 C CG   B LYS   B 1 102 ? 44.197 -27.664 13.517  0.66 42.33 ?  102 LYS   B CG   1 
ATOM   5789 C CD   A LYS   B 1 102 ? 44.383 -26.109 13.146  0.34 42.78 ?  102 LYS   B CD   1 
ATOM   5790 C CD   B LYS   B 1 102 ? 44.513 -26.243 13.077  0.66 44.69 ?  102 LYS   B CD   1 
ATOM   5791 C CE   A LYS   B 1 102 ? 45.842 -25.848 12.817  0.34 43.94 ?  102 LYS   B CE   1 
ATOM   5792 C CE   B LYS   B 1 102 ? 45.999 -26.032 12.846  0.66 46.37 ?  102 LYS   B CE   1 
ATOM   5793 N NZ   A LYS   B 1 102 ? 46.072 -24.423 12.444  0.34 44.60 ?  102 LYS   B NZ   1 
ATOM   5794 N NZ   B LYS   B 1 102 ? 46.282 -24.642 12.383  0.66 47.39 ?  102 LYS   B NZ   1 
ATOM   5795 H H    A LYS   B 1 102 ? 41.980 -29.678 12.327  0.34 42.39 ?  102 LYS   B H    1 
ATOM   5796 H H    B LYS   B 1 102 ? 41.977 -29.678 12.330  0.66 42.31 ?  102 LYS   B H    1 
ATOM   5797 H HA   A LYS   B 1 102 ? 42.912 -29.541 14.857  0.34 44.65 ?  102 LYS   B HA   1 
ATOM   5798 H HA   B LYS   B 1 102 ? 42.882 -29.574 14.874  0.66 44.74 ?  102 LYS   B HA   1 
ATOM   5799 H HB2  A LYS   B 1 102 ? 42.133 -27.475 13.109  0.34 47.25 ?  102 LYS   B HB2  1 
ATOM   5800 H HB2  B LYS   B 1 102 ? 42.209 -27.465 13.136  0.66 47.99 ?  102 LYS   B HB2  1 
ATOM   5801 H HB3  A LYS   B 1 102 ? 42.488 -27.206 14.629  0.34 47.25 ?  102 LYS   B HB3  1 
ATOM   5802 H HB3  B LYS   B 1 102 ? 42.572 -27.231 14.661  0.66 47.99 ?  102 LYS   B HB3  1 
ATOM   5803 H HG2  A LYS   B 1 102 ? 44.692 -27.816 14.235  0.34 49.48 ?  102 LYS   B HG2  1 
ATOM   5804 H HG2  B LYS   B 1 102 ? 44.744 -27.874 14.291  0.66 50.95 ?  102 LYS   B HG2  1 
ATOM   5805 H HG3  A LYS   B 1 102 ? 44.339 -28.110 12.708  0.34 49.48 ?  102 LYS   B HG3  1 
ATOM   5806 H HG3  B LYS   B 1 102 ? 44.401 -28.266 12.785  0.66 50.95 ?  102 LYS   B HG3  1 
ATOM   5807 H HD2  A LYS   B 1 102 ? 43.849 -25.864 12.373  0.34 51.49 ?  102 LYS   B HD2  1 
ATOM   5808 H HD2  B LYS   B 1 102 ? 44.049 -26.058 12.245  0.66 53.78 ?  102 LYS   B HD2  1 
ATOM   5809 H HD3  A LYS   B 1 102 ? 44.140 -25.558 13.907  0.34 51.49 ?  102 LYS   B HD3  1 
ATOM   5810 H HD3  B LYS   B 1 102 ? 44.223 -25.624 13.766  0.66 53.78 ?  102 LYS   B HD3  1 
ATOM   5811 H HE2  A LYS   B 1 102 ? 46.386 -26.051 13.594  0.34 52.88 ?  102 LYS   B HE2  1 
ATOM   5812 H HE2  B LYS   B 1 102 ? 46.477 -26.179 13.678  0.66 55.79 ?  102 LYS   B HE2  1 
ATOM   5813 H HE3  A LYS   B 1 102 ? 46.106 -26.405 12.068  0.34 52.88 ?  102 LYS   B HE3  1 
ATOM   5814 H HE3  B LYS   B 1 102 ? 46.309 -26.650 12.166  0.66 55.79 ?  102 LYS   B HE3  1 
ATOM   5815 H HZ1  A LYS   B 1 102 ? 46.932 -24.293 12.256  0.34 53.68 ?  102 LYS   B HZ1  1 
ATOM   5816 H HZ1  B LYS   B 1 102 ? 47.155 -24.536 12.253  0.66 57.02 ?  102 LYS   B HZ1  1 
ATOM   5817 H HZ2  A LYS   B 1 102 ? 45.585 -24.213 11.729  0.34 53.68 ?  102 LYS   B HZ2  1 
ATOM   5818 H HZ2  B LYS   B 1 102 ? 45.854 -24.484 11.618  0.66 57.02 ?  102 LYS   B HZ2  1 
ATOM   5819 H HZ3  A LYS   B 1 102 ? 45.840 -23.891 13.119  0.34 53.68 ?  102 LYS   B HZ3  1 
ATOM   5820 H HZ3  B LYS   B 1 102 ? 46.006 -24.056 12.994  0.66 57.02 ?  102 LYS   B HZ3  1 
ATOM   5821 N N    . GLY   B 1 103 ? 39.973 -30.040 14.387  1.00 36.24 ?  103 GLY   B N    1 
ATOM   5822 C CA   . GLY   B 1 103 ? 38.639 -30.101 14.949  1.00 36.08 ?  103 GLY   B CA   1 
ATOM   5823 C C    . GLY   B 1 103 ? 37.691 -29.013 14.498  1.00 35.48 ?  103 GLY   B C    1 
ATOM   5824 O O    . GLY   B 1 103 ? 36.596 -28.898 15.061  1.00 35.78 ?  103 GLY   B O    1 
ATOM   5825 H H    A GLY   B 1 103 ? 40.102 -30.583 13.733  0.34 43.64 ?  103 GLY   B H    1 
ATOM   5826 H H    B GLY   B 1 103 ? 40.112 -30.604 13.754  0.66 43.64 ?  103 GLY   B H    1 
ATOM   5827 H HA2  . GLY   B 1 103 ? 38.242 -30.956 14.718  1.00 43.45 ?  103 GLY   B HA2  1 
ATOM   5828 H HA3  . GLY   B 1 103 ? 38.702 -30.053 15.915  1.00 43.45 ?  103 GLY   B HA3  1 
ATOM   5829 N N    A GLU   B 1 104 ? 38.079 -28.203 13.516  0.34 35.09 ?  104 GLU   B N    1 
ATOM   5830 N N    B GLU   B 1 104 ? 38.061 -28.222 13.495  0.66 34.42 ?  104 GLU   B N    1 
ATOM   5831 C CA   A GLU   B 1 104 ? 37.238 -27.103 13.073  0.34 34.53 ?  104 GLU   B CA   1 
ATOM   5832 C CA   B GLU   B 1 104 ? 37.197 -27.146 13.036  0.66 33.32 ?  104 GLU   B CA   1 
ATOM   5833 C C    A GLU   B 1 104 ? 36.045 -27.625 12.273  0.34 34.61 ?  104 GLU   B C    1 
ATOM   5834 C C    B GLU   B 1 104 ? 36.022 -27.698 12.228  0.66 33.47 ?  104 GLU   B C    1 
ATOM   5835 O O    A GLU   B 1 104 ? 36.074 -28.714 11.692  0.34 34.87 ?  104 GLU   B O    1 
ATOM   5836 O O    B GLU   B 1 104 ? 36.076 -28.796 11.665  0.66 34.06 ?  104 GLU   B O    1 
ATOM   5837 C CB   A GLU   B 1 104 ? 38.062 -26.105 12.258  0.34 33.88 ?  104 GLU   B CB   1 
ATOM   5838 C CB   B GLU   B 1 104 ? 38.007 -26.129 12.231  0.66 32.27 ?  104 GLU   B CB   1 
ATOM   5839 C CG   A GLU   B 1 104 ? 39.170 -25.446 13.072  0.34 33.30 ?  104 GLU   B CG   1 
ATOM   5840 C CG   B GLU   B 1 104 ? 39.103 -25.479 13.068  0.66 31.26 ?  104 GLU   B CG   1 
ATOM   5841 C CD   A GLU   B 1 104 ? 40.069 -24.550 12.244  0.34 32.78 ?  104 GLU   B CD   1 
ATOM   5842 C CD   B GLU   B 1 104 ? 40.055 -24.609 12.270  0.66 30.28 ?  104 GLU   B CD   1 
ATOM   5843 O OE1  A GLU   B 1 104 ? 40.020 -24.632 10.999  0.34 32.21 ?  104 GLU   B OE1  1 
ATOM   5844 O OE1  B GLU   B 1 104 ? 40.048 -24.678 11.024  0.66 28.96 ?  104 GLU   B OE1  1 
ATOM   5845 O OE2  A GLU   B 1 104 ? 40.832 -23.764 12.844  0.34 32.62 -1 104 GLU   B OE2  1 
ATOM   5846 O OE2  B GLU   B 1 104 ? 40.822 -23.854 12.902  0.66 29.89 -1 104 GLU   B OE2  1 
ATOM   5847 H H    A GLU   B 1 104 ? 38.827 -28.268 13.097  0.34 42.26 ?  104 GLU   B H    1 
ATOM   5848 H H    B GLU   B 1 104 ? 38.806 -28.284 13.071  0.66 41.45 ?  104 GLU   B H    1 
ATOM   5849 H HA   A GLU   B 1 104 ? 36.894 -26.637 13.849  0.34 41.58 ?  104 GLU   B HA   1 
ATOM   5850 H HA   B GLU   B 1 104 ? 36.833 -26.688 13.808  0.66 40.13 ?  104 GLU   B HA   1 
ATOM   5851 H HB2  A GLU   B 1 104 ? 38.476 -26.567 11.513  0.34 40.81 ?  104 GLU   B HB2  1 
ATOM   5852 H HB2  B GLU   B 1 104 ? 38.423 -26.576 11.479  0.66 38.88 ?  104 GLU   B HB2  1 
ATOM   5853 H HB3  A GLU   B 1 104 ? 37.477 -25.404 11.929  0.34 40.81 ?  104 GLU   B HB3  1 
ATOM   5854 H HB3  B GLU   B 1 104 ? 37.412 -25.429 11.915  0.66 38.88 ?  104 GLU   B HB3  1 
ATOM   5855 H HG2  A GLU   B 1 104 ? 38.769 -24.905 13.771  0.34 40.11 ?  104 GLU   B HG2  1 
ATOM   5856 H HG2  B GLU   B 1 104 ? 38.690 -24.922 13.747  0.66 37.67 ?  104 GLU   B HG2  1 
ATOM   5857 H HG3  A GLU   B 1 104 ? 39.727 -26.134 13.466  0.34 40.11 ?  104 GLU   B HG3  1 
ATOM   5858 H HG3  B GLU   B 1 104 ? 39.631 -26.174 13.488  0.66 37.67 ?  104 GLU   B HG3  1 
ATOM   5859 N N    A ASP   B 1 105 ? 34.981 -26.825 12.254  0.34 34.20 ?  105 ASP   B N    1 
ATOM   5860 N N    B ASP   B 1 105 ? 34.944 -26.917 12.185  0.66 32.55 ?  105 ASP   B N    1 
ATOM   5861 C CA   A ASP   B 1 105 ? 33.709 -27.262 11.691  0.34 34.09 ?  105 ASP   B CA   1 
ATOM   5862 C CA   B ASP   B 1 105 ? 33.677 -27.379 11.629  0.66 32.34 ?  105 ASP   B CA   1 
ATOM   5863 C C    A ASP   B 1 105 ? 33.792 -27.312 10.169  0.34 32.40 ?  105 ASP   B C    1 
ATOM   5864 C C    B ASP   B 1 105 ? 33.745 -27.391 10.107  0.66 29.92 ?  105 ASP   B C    1 
ATOM   5865 O O    A ASP   B 1 105 ? 34.037 -26.292 9.517   0.34 32.06 ?  105 ASP   B O    1 
ATOM   5866 O O    B ASP   B 1 105 ? 33.918 -26.342 9.477   0.66 29.32 ?  105 ASP   B O    1 
ATOM   5867 C CB   A ASP   B 1 105 ? 32.598 -26.311 12.133  0.34 35.60 ?  105 ASP   B CB   1 
ATOM   5868 C CB   B ASP   B 1 105 ? 32.539 -26.477 12.103  0.66 34.93 ?  105 ASP   B CB   1 
ATOM   5869 C CG   A ASP   B 1 105 ? 31.221 -26.786 11.712  0.34 37.01 ?  105 ASP   B CG   1 
ATOM   5870 C CG   B ASP   B 1 105 ? 31.170 -27.026 11.744  0.66 37.14 ?  105 ASP   B CG   1 
ATOM   5871 O OD1  A ASP   B 1 105 ? 31.114 -27.903 11.163  0.34 37.31 ?  105 ASP   B OD1  1 
ATOM   5872 O OD1  B ASP   B 1 105 ? 31.101 -28.050 11.034  0.66 37.57 ?  105 ASP   B OD1  1 
ATOM   5873 O OD2  A ASP   B 1 105 ? 30.244 -26.038 11.927  0.34 37.66 -1 105 ASP   B OD2  1 
ATOM   5874 O OD2  B ASP   B 1 105 ? 30.158 -26.435 12.180  0.66 37.99 -1 105 ASP   B OD2  1 
ATOM   5875 H H    A ASP   B 1 105 ? 34.971 -26.023 12.560  0.34 41.19 ?  105 ASP   B H    1 
ATOM   5876 H H    B ASP   B 1 105 ? 34.922 -26.107 12.471  0.66 39.22 ?  105 ASP   B H    1 
ATOM   5877 H HA   A ASP   B 1 105 ? 33.498 -28.151 12.015  0.34 41.06 ?  105 ASP   B HA   1 
ATOM   5878 H HA   B ASP   B 1 105 ? 33.498 -28.282 11.930  0.66 38.96 ?  105 ASP   B HA   1 
ATOM   5879 H HB2  A ASP   B 1 105 ? 32.613 -26.235 13.101  0.34 42.87 ?  105 ASP   B HB2  1 
ATOM   5880 H HB2  B ASP   B 1 105 ? 32.582 -26.391 13.068  0.66 42.06 ?  105 ASP   B HB2  1 
ATOM   5881 H HB3  A ASP   B 1 105 ? 32.743 -25.442 11.730  0.34 42.87 ?  105 ASP   B HB3  1 
ATOM   5882 H HB3  B ASP   B 1 105 ? 32.630 -25.603 11.689  0.66 42.06 ?  105 ASP   B HB3  1 
ATOM   5883 N N    A ILE   B 1 106 ? 33.578 -28.505 9.607   0.34 31.24 ?  106 ILE   B N    1 
ATOM   5884 N N    B ILE   B 1 106 ? 33.573 -28.579 9.519   0.66 29.07 ?  106 ILE   B N    1 
ATOM   5885 C CA   A ILE   B 1 106 ? 33.589 -28.686 8.161   0.34 30.15 ?  106 ILE   B CA   1 
ATOM   5886 C CA   B ILE   B 1 106 ? 33.579 -28.729 8.070   0.66 28.11 ?  106 ILE   B CA   1 
ATOM   5887 C C    A ILE   B 1 106 ? 32.501 -27.868 7.478   0.34 29.21 ?  106 ILE   B C    1 
ATOM   5888 C C    B ILE   B 1 106 ? 32.489 -27.891 7.419   0.66 26.81 ?  106 ILE   B C    1 
ATOM   5889 O O    A ILE   B 1 106 ? 32.608 -27.573 6.283   0.34 28.94 ?  106 ILE   B O    1 
ATOM   5890 O O    B ILE   B 1 106 ? 32.576 -27.580 6.227   0.66 25.70 ?  106 ILE   B O    1 
ATOM   5891 C CB   A ILE   B 1 106 ? 33.473 -30.192 7.827   0.34 30.06 ?  106 ILE   B CB   1 
ATOM   5892 C CB   B ILE   B 1 106 ? 33.460 -30.228 7.701   0.66 28.54 ?  106 ILE   B CB   1 
ATOM   5893 C CG1  A ILE   B 1 106 ? 33.705 -30.442 6.334   0.34 29.74 ?  106 ILE   B CG1  1 
ATOM   5894 C CG1  B ILE   B 1 106 ? 33.803 -30.459 6.227   0.66 28.54 ?  106 ILE   B CG1  1 
ATOM   5895 C CG2  A ILE   B 1 106 ? 32.113 -30.731 8.252   0.34 30.38 ?  106 ILE   B CG2  1 
ATOM   5896 C CG2  B ILE   B 1 106 ? 32.063 -30.758 8.017   0.66 29.22 ?  106 ILE   B CG2  1 
ATOM   5897 C CD1  A ILE   B 1 106 ? 35.064 -29.993 5.845   0.34 29.49 ?  106 ILE   B CD1  1 
ATOM   5898 C CD1  B ILE   B 1 106 ? 35.172 -29.959 5.837   0.66 28.40 ?  106 ILE   B CD1  1 
ATOM   5899 H H    A ILE   B 1 106 ? 33.432 -29.226 10.047  0.34 37.64 ?  106 ILE   B H    1 
ATOM   5900 H H    B ILE   B 1 106 ? 33.443 -29.310 9.940   0.66 35.03 ?  106 ILE   B H    1 
ATOM   5901 H HA   A ILE   B 1 106 ? 34.440 -28.373 7.822   0.34 36.33 ?  106 ILE   B HA   1 
ATOM   5902 H HA   B ILE   B 1 106 ? 34.430 -28.411 7.736   0.66 33.88 ?  106 ILE   B HA   1 
ATOM   5903 H HB   A ILE   B 1 106 ? 34.156 -30.668 8.323   0.34 36.22 ?  106 ILE   B HB   1 
ATOM   5904 H HB   B ILE   B 1 106 ? 34.096 -30.722 8.237   0.66 34.40 ?  106 ILE   B HB   1 
ATOM   5905 H HG12 A ILE   B 1 106 ? 33.633 -31.395 6.163   0.34 35.84 ?  106 ILE   B HG12 1 
ATOM   5906 H HG12 B ILE   B 1 106 ? 33.778 -31.414 6.046   0.66 34.40 ?  106 ILE   B HG12 1 
ATOM   5907 H HG13 A ILE   B 1 106 ? 33.033 -29.967 5.824   0.34 35.84 ?  106 ILE   B HG13 1 
ATOM   5908 H HG13 B ILE   B 1 106 ? 33.152 -30.003 5.675   0.66 34.40 ?  106 ILE   B HG13 1 
ATOM   5909 H HG21 A ILE   B 1 106 ? 32.114 -31.697 8.160   0.34 36.61 ?  106 ILE   B HG21 1 
ATOM   5910 H HG21 B ILE   B 1 106 ? 32.074 -31.727 7.957   0.66 35.22 ?  106 ILE   B HG21 1 
ATOM   5911 H HG22 A ILE   B 1 106 ? 31.952 -30.488 9.177   0.34 36.61 ?  106 ILE   B HG22 1 
ATOM   5912 H HG22 B ILE   B 1 106 ? 31.821 -30.486 8.916   0.66 35.22 ?  106 ILE   B HG22 1 
ATOM   5913 H HG23 A ILE   B 1 106 ? 31.427 -30.346 7.685   0.34 36.61 ?  106 ILE   B HG23 1 
ATOM   5914 H HG23 B ILE   B 1 106 ? 31.431 -30.395 7.378   0.66 35.22 ?  106 ILE   B HG23 1 
ATOM   5915 H HD11 A ILE   B 1 106 ? 35.232 -30.389 4.977   0.34 35.54 ?  106 ILE   B HD11 1 
ATOM   5916 H HD11 B ILE   B 1 106 ? 35.446 -30.395 5.017   0.66 34.23 ?  106 ILE   B HD11 1 
ATOM   5917 H HD12 A ILE   B 1 106 ? 35.070 -29.025 5.774   0.34 35.54 ?  106 ILE   B HD12 1 
ATOM   5918 H HD12 B ILE   B 1 106 ? 35.132 -28.998 5.702   0.66 34.23 ?  106 ILE   B HD12 1 
ATOM   5919 H HD13 A ILE   B 1 106 ? 35.739 -30.284 6.478   0.34 35.54 ?  106 ILE   B HD13 1 
ATOM   5920 H HD13 B ILE   B 1 106 ? 35.800 -30.167 6.547   0.66 34.23 ?  106 ILE   B HD13 1 
ATOM   5921 N N    A GLN   B 1 107 ? 31.450 -27.487 8.210   0.34 28.77 ?  107 GLN   B N    1 
ATOM   5922 N N    B GLN   B 1 107 ? 31.471 -27.488 8.182   0.66 27.17 ?  107 GLN   B N    1 
ATOM   5923 C CA   A GLN   B 1 107 ? 30.375 -26.699 7.616   0.34 28.16 ?  107 GLN   B CA   1 
ATOM   5924 C CA   B GLN   B 1 107 ? 30.383 -26.703 7.613   0.66 26.87 ?  107 GLN   B CA   1 
ATOM   5925 C C    A GLN   B 1 107 ? 30.868 -25.349 7.109   0.34 25.45 ?  107 GLN   B C    1 
ATOM   5926 C C    B GLN   B 1 107 ? 30.851 -25.337 7.133   0.66 24.49 ?  107 GLN   B C    1 
ATOM   5927 O O    A GLN   B 1 107 ? 30.242 -24.772 6.214   0.34 25.73 ?  107 GLN   B O    1 
ATOM   5928 O O    B GLN   B 1 107 ? 30.196 -24.743 6.273   0.66 25.10 ?  107 GLN   B O    1 
ATOM   5929 C CB   A GLN   B 1 107 ? 29.251 -26.498 8.637   0.34 30.69 ?  107 GLN   B CB   1 
ATOM   5930 C CB   B GLN   B 1 107 ? 29.257 -26.547 8.633   0.66 30.51 ?  107 GLN   B CB   1 
ATOM   5931 C CG   A GLN   B 1 107 ? 27.935 -25.993 8.049   0.34 32.93 ?  107 GLN   B CG   1 
ATOM   5932 C CG   B GLN   B 1 107 ? 27.911 -26.154 8.034   0.66 33.95 ?  107 GLN   B CG   1 
ATOM   5933 C CD   A GLN   B 1 107 ? 27.872 -24.479 7.937   0.34 34.69 ?  107 GLN   B CD   1 
ATOM   5934 C CD   B GLN   B 1 107 ? 27.758 -24.657 7.838   0.66 36.58 ?  107 GLN   B CD   1 
ATOM   5935 O OE1  A GLN   B 1 107 ? 28.699 -23.766 8.509   0.34 35.35 ?  107 GLN   B OE1  1 
ATOM   5936 O OE1  B GLN   B 1 107 ? 28.466 -23.861 8.455   0.66 37.58 ?  107 GLN   B OE1  1 
ATOM   5937 N NE2  A GLN   B 1 107 ? 26.883 -23.980 7.200   0.34 35.37 ?  107 GLN   B NE2  1 
ATOM   5938 N NE2  B GLN   B 1 107 ? 26.825 -24.266 6.974   0.66 37.59 ?  107 GLN   B NE2  1 
ATOM   5939 H H    A GLN   B 1 107 ? 31.341 -27.666 9.042   0.34 34.68 ?  107 GLN   B H    1 
ATOM   5940 H H    B GLN   B 1 107 ? 31.408 -27.629 9.021   0.66 32.75 ?  107 GLN   B H    1 
ATOM   5941 H HA   A GLN   B 1 107 ? 30.005 -27.190 6.862   0.34 33.94 ?  107 GLN   B HA   1 
ATOM   5942 H HA   B GLN   B 1 107 ? 30.024 -27.179 6.850   0.66 32.39 ?  107 GLN   B HA   1 
ATOM   5943 H HB2  A GLN   B 1 107 ? 29.069 -27.345 9.069   0.34 36.98 ?  107 GLN   B HB2  1 
ATOM   5944 H HB2  B GLN   B 1 107 ? 29.142 -27.393 9.085   0.66 36.76 ?  107 GLN   B HB2  1 
ATOM   5945 H HB3  A GLN   B 1 107 ? 29.545 -25.852 9.299   0.34 36.98 ?  107 GLN   B HB3  1 
ATOM   5946 H HB3  B GLN   B 1 107 ? 29.511 -25.863 9.271   0.66 36.76 ?  107 GLN   B HB3  1 
ATOM   5947 H HG2  A GLN   B 1 107 ? 27.824 -26.360 7.159   0.34 39.67 ?  107 GLN   B HG2  1 
ATOM   5948 H HG2  B GLN   B 1 107 ? 27.812 -26.577 7.168   0.66 40.89 ?  107 GLN   B HG2  1 
ATOM   5949 H HG3  A GLN   B 1 107 ? 27.203 -26.283 8.619   0.34 39.67 ?  107 GLN   B HG3  1 
ATOM   5950 H HG3  B GLN   B 1 107 ? 27.206 -26.453 8.630   0.66 40.89 ?  107 GLN   B HG3  1 
ATOM   5951 H HE21 A GLN   B 1 107 ? 26.325 -24.509 6.814   0.34 42.59 ?  107 GLN   B HE21 1 
ATOM   5952 H HE21 B GLN   B 1 107 ? 26.350 -24.851 6.559   0.66 45.26 ?  107 GLN   B HE21 1 
ATOM   5953 H HE22 A GLN   B 1 107 ? 26.801 -23.129 7.107   0.34 42.59 ?  107 GLN   B HE22 1 
ATOM   5954 H HE22 B GLN   B 1 107 ? 26.696 -23.427 6.829   0.66 45.26 ?  107 GLN   B HE22 1 
ATOM   5955 N N    . LEU   B 1 108 ? 31.977 -24.838 7.652   1.00 22.82 ?  108 LEU   B N    1 
ATOM   5956 C CA   . LEU   B 1 108 ? 32.525 -23.544 7.238   1.00 19.66 ?  108 LEU   B CA   1 
ATOM   5957 C C    . LEU   B 1 108 ? 33.170 -23.572 5.860   1.00 16.74 ?  108 LEU   B C    1 
ATOM   5958 O O    . LEU   B 1 108 ? 33.609 -22.521 5.373   1.00 15.75 ?  108 LEU   B O    1 
ATOM   5959 C CB   . LEU   B 1 108 ? 33.528 -23.050 8.281   1.00 20.22 ?  108 LEU   B CB   1 
ATOM   5960 C CG   . LEU   B 1 108 ? 32.905 -22.478 9.555   1.00 21.79 ?  108 LEU   B CG   1 
ATOM   5961 C CD1  . LEU   B 1 108 ? 33.901 -22.484 10.696  1.00 22.46 ?  108 LEU   B CD1  1 
ATOM   5962 C CD2  . LEU   B 1 108 ? 32.411 -21.063 9.299   1.00 22.54 ?  108 LEU   B CD2  1 
ATOM   5963 H H    A LEU   B 1 108 ? 32.423 -25.227 8.274   0.34 27.54 ?  108 LEU   B H    1 
ATOM   5964 H H    B LEU   B 1 108 ? 32.429 -25.233 8.266   0.66 27.54 ?  108 LEU   B H    1 
ATOM   5965 H HA   . LEU   B 1 108 ? 31.802 -22.905 7.209   1.00 23.74 ?  108 LEU   B HA   1 
ATOM   5966 H HB2  . LEU   B 1 108 ? 34.092 -23.792 8.545   1.00 24.42 ?  108 LEU   B HB2  1 
ATOM   5967 H HB3  . LEU   B 1 108 ? 34.067 -22.352 7.884   1.00 24.42 ?  108 LEU   B HB3  1 
ATOM   5968 H HG   . LEU   B 1 108 ? 32.142 -23.020 9.814   1.00 26.30 ?  108 LEU   B HG   1 
ATOM   5969 H HD11 . LEU   B 1 108 ? 33.465 -22.157 11.499  1.00 27.10 ?  108 LEU   B HD11 1 
ATOM   5970 H HD12 . LEU   B 1 108 ? 34.215 -23.390 10.835  1.00 27.10 ?  108 LEU   B HD12 1 
ATOM   5971 H HD13 . LEU   B 1 108 ? 34.646 -21.906 10.466  1.00 27.10 ?  108 LEU   B HD13 1 
ATOM   5972 H HD21 . LEU   B 1 108 ? 32.032 -20.705 10.118  1.00 27.19 ?  108 LEU   B HD21 1 
ATOM   5973 H HD22 . LEU   B 1 108 ? 33.160 -20.514 9.016   1.00 27.19 ?  108 LEU   B HD22 1 
ATOM   5974 H HD23 . LEU   B 1 108 ? 31.735 -21.082 8.604   1.00 27.19 ?  108 LEU   B HD23 1 
ATOM   5975 N N    . LEU   B 1 109 ? 33.224 -24.739 5.225   1.00 15.35 ?  109 LEU   B N    1 
ATOM   5976 C CA   . LEU   B 1 109 ? 33.861 -24.856 3.922   1.00 14.54 ?  109 LEU   B CA   1 
ATOM   5977 C C    . LEU   B 1 109 ? 33.099 -24.080 2.858   1.00 13.72 ?  109 LEU   B C    1 
ATOM   5978 O O    . LEU   B 1 109 ? 33.715 -23.493 1.962   1.00 13.00 ?  109 LEU   B O    1 
ATOM   5979 C CB   . LEU   B 1 109 ? 33.970 -26.335 3.543   1.00 14.57 ?  109 LEU   B CB   1 
ATOM   5980 C CG   . LEU   B 1 109 ? 34.770 -26.679 2.289   1.00 13.88 ?  109 LEU   B CG   1 
ATOM   5981 C CD1  . LEU   B 1 109 ? 36.149 -26.034 2.314   1.00 13.81 ?  109 LEU   B CD1  1 
ATOM   5982 C CD2  . LEU   B 1 109 ? 34.879 -28.195 2.148   1.00 14.93 ?  109 LEU   B CD2  1 
ATOM   5983 H H    . LEU   B 1 109 ? 32.911 -25.476 5.524   1.00 18.57 ?  109 LEU   B H    1 
ATOM   5984 H HA   . LEU   B 1 109 ? 34.760 -24.489 3.971   1.00 17.60 ?  109 LEU   B HA   1 
ATOM   5985 H HB2  . LEU   B 1 109 ? 34.382 -26.806 4.279   1.00 17.63 ?  109 LEU   B HB2  1 
ATOM   5986 H HB3  . LEU   B 1 109 ? 33.072 -26.676 3.405   1.00 17.63 ?  109 LEU   B HB3  1 
ATOM   5987 H HG   . LEU   B 1 109 ? 34.301 -26.354 1.506   1.00 16.80 ?  109 LEU   B HG   1 
ATOM   5988 H HD11 . LEU   B 1 109 ? 36.688 -26.409 1.598   1.00 16.72 ?  109 LEU   B HD11 1 
ATOM   5989 H HD12 . LEU   B 1 109 ? 36.049 -25.081 2.190   1.00 16.72 ?  109 LEU   B HD12 1 
ATOM   5990 H HD13 . LEU   B 1 109 ? 36.566 -26.221 3.170   1.00 16.72 ?  109 LEU   B HD13 1 
ATOM   5991 H HD21 . LEU   B 1 109 ? 35.464 -28.405 1.398   1.00 18.07 ?  109 LEU   B HD21 1 
ATOM   5992 H HD22 . LEU   B 1 109 ? 35.251 -28.565 2.964   1.00 18.07 ?  109 LEU   B HD22 1 
ATOM   5993 H HD23 . LEU   B 1 109 ? 33.997 -28.566 1.988   1.00 18.07 ?  109 LEU   B HD23 1 
ATOM   5994 N N    . LYS   B 1 110 ? 31.766 -24.044 2.943   1.00 13.32 ?  110 LYS   B N    1 
ATOM   5995 C CA   . LYS   B 1 110 ? 31.012 -23.279 1.956   1.00 13.12 ?  110 LYS   B CA   1 
ATOM   5996 C C    . LYS   B 1 110 ? 31.353 -21.793 2.047   1.00 12.72 ?  110 LYS   B C    1 
ATOM   5997 O O    . LYS   B 1 110 ? 31.610 -21.141 1.027   1.00 12.63 ?  110 LYS   B O    1 
ATOM   5998 C CB   . LYS   B 1 110 ? 29.508 -23.529 2.106   1.00 13.82 ?  110 LYS   B CB   1 
ATOM   5999 C CG   . LYS   B 1 110 ? 28.699 -22.928 0.949   1.00 14.11 ?  110 LYS   B CG   1 
ATOM   6000 C CD   . LYS   B 1 110 ? 27.225 -23.351 0.979   1.00 14.30 ?  110 LYS   B CD   1 
ATOM   6001 C CE   . LYS   B 1 110 ? 26.460 -22.825 -0.237  1.00 15.16 ?  110 LYS   B CE   1 
ATOM   6002 N NZ   . LYS   B 1 110 ? 26.817 -23.549 -1.491  1.00 15.55 ?  110 LYS   B NZ   1 
ATOM   6003 H H    . LYS   B 1 110 ? 31.298 -24.442 3.543   1.00 16.13 ?  110 LYS   B H    1 
ATOM   6004 H HA   . LYS   B 1 110 ? 31.267 -23.583 1.074   1.00 15.89 ?  110 LYS   B HA   1 
ATOM   6005 H HB2  . LYS   B 1 110 ? 29.345 -24.487 2.125   1.00 16.74 ?  110 LYS   B HB2  1 
ATOM   6006 H HB3  . LYS   B 1 110 ? 29.197 -23.126 2.932   1.00 16.74 ?  110 LYS   B HB3  1 
ATOM   6007 H HG2  . LYS   B 1 110 ? 28.727 -21.965 1.004   1.00 17.09 ?  110 LYS   B HG2  1 
ATOM   6008 H HG3  . LYS   B 1 110 ? 29.072 -23.232 0.109   1.00 17.09 ?  110 LYS   B HG3  1 
ATOM   6009 H HD2  . LYS   B 1 110 ? 27.166 -24.323 0.976   1.00 17.31 ?  110 LYS   B HD2  1 
ATOM   6010 H HD3  . LYS   B 1 110 ? 26.802 -22.998 1.779   1.00 17.31 ?  110 LYS   B HD3  1 
ATOM   6011 H HE2  . LYS   B 1 110 ? 25.507 -22.937 -0.090  1.00 18.35 ?  110 LYS   B HE2  1 
ATOM   6012 H HE3  . LYS   B 1 110 ? 26.670 -21.887 -0.362  1.00 18.35 ?  110 LYS   B HE3  1 
ATOM   6013 H HZ1  . LYS   B 1 110 ? 26.363 -23.222 -2.178  1.00 18.81 ?  110 LYS   B HZ1  1 
ATOM   6014 H HZ2  . LYS   B 1 110 ? 27.692 -23.462 -1.654  1.00 18.81 ?  110 LYS   B HZ2  1 
ATOM   6015 H HZ3  . LYS   B 1 110 ? 26.632 -24.418 -1.406  1.00 18.81 ?  110 LYS   B HZ3  1 
ATOM   6016 N N    . SER   B 1 111 ? 31.377 -21.243 3.266   1.00 13.12 ?  111 SER   B N    1 
ATOM   6017 C CA   . SER   B 1 111 ? 31.767 -19.844 3.434   1.00 12.99 ?  111 SER   B CA   1 
ATOM   6018 C C    . SER   B 1 111 ? 33.146 -19.590 2.841   1.00 12.19 ?  111 SER   B C    1 
ATOM   6019 O O    . SER   B 1 111 ? 33.375 -18.560 2.191   1.00 12.69 ?  111 SER   B O    1 
ATOM   6020 C CB   . SER   B 1 111 ? 31.766 -19.478 4.917   1.00 14.10 ?  111 SER   B CB   1 
ATOM   6021 O OG   . SER   B 1 111 ? 30.457 -19.482 5.448   1.00 15.58 ?  111 SER   B OG   1 
ATOM   6022 H H    . SER   B 1 111 ? 31.197 -21.658 3.997   1.00 15.90 ?  111 SER   B H    1 
ATOM   6023 H HA   . SER   B 1 111 ? 31.132 -19.278 2.978   1.00 15.74 ?  111 SER   B HA   1 
ATOM   6024 H HB2  . SER   B 1 111 ? 32.298 -20.128 5.406   1.00 17.07 ?  111 SER   B HB2  1 
ATOM   6025 H HB3  . SER   B 1 111 ? 32.145 -18.594 5.027   1.00 17.07 ?  111 SER   B HB3  1 
ATOM   6026 H HG   . SER   B 1 111 ? 30.473 -19.276 6.269   1.00 18.85 ?  111 SER   B HG   1 
ATOM   6027 N N    . ALA   B 1 112 ? 34.081 -20.517 3.058   1.00 12.34 ?  112 ALA   B N    1 
ATOM   6028 C CA   . ALA   B 1 112 ? 35.425 -20.348 2.517   1.00 12.02 ?  112 ALA   B CA   1 
ATOM   6029 C C    . ALA   B 1 112 ? 35.398 -20.256 0.993   1.00 11.65 ?  112 ALA   B C    1 
ATOM   6030 O O    . ALA   B 1 112 ? 36.021 -19.366 0.404   1.00 11.84 ?  112 ALA   B O    1 
ATOM   6031 C CB   . ALA   B 1 112 ? 36.317 -21.492 3.001   1.00 12.19 ?  112 ALA   B CB   1 
ATOM   6032 H H    . ALA   B 1 112 ? 33.966 -21.241 3.513   1.00 14.95 ?  112 ALA   B H    1 
ATOM   6033 H HA   . ALA   B 1 112 ? 35.797 -19.521 2.858   1.00 14.57 ?  112 ALA   B HA   1 
ATOM   6034 H HB1  . ALA   B 1 112 ? 37.210 -21.369 2.641   1.00 14.78 ?  112 ALA   B HB1  1 
ATOM   6035 H HB2  . ALA   B 1 112 ? 36.352 -21.473 3.974   1.00 14.78 ?  112 ALA   B HB2  1 
ATOM   6036 H HB3  . ALA   B 1 112 ? 35.948 -22.333 2.701   1.00 14.78 ?  112 ALA   B HB3  1 
ATOM   6037 N N    . TYR   B 1 113 ? 34.665 -21.159 0.332   1.00 11.44 ?  113 TYR   B N    1 
ATOM   6038 C CA   . TYR   B 1 113 ? 34.584 -21.116 -1.124  1.00 11.42 ?  113 TYR   B CA   1 
ATOM   6039 C C    . TYR   B 1 113 ? 33.877 -19.864 -1.644  1.00 10.87 ?  113 TYR   B C    1 
ATOM   6040 O O    . TYR   B 1 113 ? 34.157 -19.433 -2.769  1.00 10.99 ?  113 TYR   B O    1 
ATOM   6041 C CB   . TYR   B 1 113 ? 33.914 -22.376 -1.672  1.00 11.34 ?  113 TYR   B CB   1 
ATOM   6042 C CG   . TYR   B 1 113 ? 34.874 -23.523 -1.916  1.00 11.79 ?  113 TYR   B CG   1 
ATOM   6043 C CD1  . TYR   B 1 113 ? 35.872 -23.428 -2.876  1.00 11.98 ?  113 TYR   B CD1  1 
ATOM   6044 C CD2  . TYR   B 1 113 ? 34.769 -24.708 -1.206  1.00 12.51 ?  113 TYR   B CD2  1 
ATOM   6045 C CE1  . TYR   B 1 113 ? 36.751 -24.461 -3.114  1.00 11.77 ?  113 TYR   B CE1  1 
ATOM   6046 C CE2  . TYR   B 1 113 ? 35.647 -25.763 -1.439  1.00 12.41 ?  113 TYR   B CE2  1 
ATOM   6047 C CZ   . TYR   B 1 113 ? 36.627 -25.634 -2.402  1.00 12.32 ?  113 TYR   B CZ   1 
ATOM   6048 O OH   . TYR   B 1 113 ? 37.508 -26.645 -2.664  1.00 13.41 ?  113 TYR   B OH   1 
ATOM   6049 H H    . TYR   B 1 113 ? 34.198 -21.780 0.707   1.00 13.88 ?  113 TYR   B H    1 
ATOM   6050 H HA   . TYR   B 1 113 ? 35.484 -21.092 -1.466  1.00 13.85 ?  113 TYR   B HA   1 
ATOM   6051 H HB2  . TYR   B 1 113 ? 33.247 -22.684 -1.036  1.00 13.76 ?  113 TYR   B HB2  1 
ATOM   6052 H HB3  . TYR   B 1 113 ? 33.486 -22.164 -2.516  1.00 13.76 ?  113 TYR   B HB3  1 
ATOM   6053 H HD1  . TYR   B 1 113 ? 35.957 -22.635 -3.363  1.00 14.53 ?  113 TYR   B HD1  1 
ATOM   6054 H HD2  . TYR   B 1 113 ? 34.101 -24.802 -0.567  1.00 15.16 ?  113 TYR   B HD2  1 
ATOM   6055 H HE1  . TYR   B 1 113 ? 37.410 -24.369 -3.765  1.00 14.27 ?  113 TYR   B HE1  1 
ATOM   6056 H HE2  . TYR   B 1 113 ? 35.562 -26.558 -0.965  1.00 15.05 ?  113 TYR   B HE2  1 
ATOM   6057 H HH   . TYR   B 1 113 ? 37.332 -27.311 -2.188  1.00 16.24 ?  113 TYR   B HH   1 
ATOM   6058 N N    . GLU   B 1 114 ? 32.956 -19.282 -0.867  1.00 11.22 ?  114 GLU   B N    1 
ATOM   6059 C CA   . GLU   B 1 114 ? 32.271 -18.071 -1.324  1.00 11.24 ?  114 GLU   B CA   1 
ATOM   6060 C C    . GLU   B 1 114 ? 33.259 -16.948 -1.623  1.00 10.93 ?  114 GLU   B C    1 
ATOM   6061 O O    . GLU   B 1 114 ? 32.987 -16.083 -2.460  1.00 11.52 ?  114 GLU   B O    1 
ATOM   6062 C CB   . GLU   B 1 114 ? 31.204 -17.639 -0.309  1.00 11.57 ?  114 GLU   B CB   1 
ATOM   6063 C CG   . GLU   B 1 114 ? 29.994 -18.566 -0.363  1.00 12.20 ?  114 GLU   B CG   1 
ATOM   6064 C CD   . GLU   B 1 114 ? 28.964 -18.367 0.739   1.00 11.91 ?  114 GLU   B CD   1 
ATOM   6065 O OE1  . GLU   B 1 114 ? 29.254 -17.750 1.783   1.00 12.26 ?  114 GLU   B OE1  1 
ATOM   6066 O OE2  . GLU   B 1 114 ? 27.839 -18.899 0.564   1.00 13.30 -1 114 GLU   B OE2  1 
ATOM   6067 H H    . GLU   B 1 114 ? 32.704 -19.571 -0.094  1.00 13.61 ?  114 GLU   B H    1 
ATOM   6068 H HA   . GLU   B 1 114 ? 31.809 -18.276 -2.148  1.00 13.64 ?  114 GLU   B HA   1 
ATOM   6069 H HB2  . GLU   B 1 114 ? 31.576 -17.673 0.589   1.00 14.04 ?  114 GLU   B HB2  1 
ATOM   6070 H HB3  . GLU   B 1 114 ? 30.907 -16.739 -0.515  1.00 14.04 ?  114 GLU   B HB3  1 
ATOM   6071 H HG2  . GLU   B 1 114 ? 29.545 -18.429 -1.207  1.00 14.79 ?  114 GLU   B HG2  1 
ATOM   6072 H HG3  . GLU   B 1 114 ? 30.312 -19.481 -0.306  1.00 14.79 ?  114 GLU   B HG3  1 
ATOM   6073 N N    . ASN   B 1 115 ? 34.424 -16.946 -0.971  1.00 10.93 ?  115 ASN   B N    1 
ATOM   6074 C CA   . ASN   B 1 115 ? 35.422 -15.915 -1.263  1.00 10.70 ?  115 ASN   B CA   1 
ATOM   6075 C C    . ASN   B 1 115 ? 35.839 -15.939 -2.726  1.00 10.70 ?  115 ASN   B C    1 
ATOM   6076 O O    . ASN   B 1 115 ? 36.219 -14.897 -3.287  1.00 11.25 ?  115 ASN   B O    1 
ATOM   6077 C CB   . ASN   B 1 115 ? 36.662 -16.097 -0.375  1.00 11.49 ?  115 ASN   B CB   1 
ATOM   6078 C CG   . ASN   B 1 115 ? 36.387 -15.817 1.086   1.00 11.96 ?  115 ASN   B CG   1 
ATOM   6079 O OD1  . ASN   B 1 115 ? 36.386 -14.665 1.519   1.00 13.79 ?  115 ASN   B OD1  1 
ATOM   6080 N ND2  . ASN   B 1 115 ? 36.200 -16.876 1.872   1.00 11.84 ?  115 ASN   B ND2  1 
ATOM   6081 H H    . ASN   B 1 115 ? 34.654 -17.508 -0.359  1.00 13.27 ?  115 ASN   B H    1 
ATOM   6082 H HA   . ASN   B 1 115 ? 35.041 -15.042 -1.075  1.00 13.00 ?  115 ASN   B HA   1 
ATOM   6083 H HB2  . ASN   B 1 115 ? 36.967 -17.013 -0.453  1.00 13.94 ?  115 ASN   B HB2  1 
ATOM   6084 H HB3  . ASN   B 1 115 ? 37.349 -15.487 -0.670  1.00 13.94 ?  115 ASN   B HB3  1 
ATOM   6085 H HD21 . ASN   B 1 115 ? 36.055 -16.765 2.716   1.00 14.36 ?  115 ASN   B HD21 1 
ATOM   6086 H HD22 . ASN   B 1 115 ? 36.220 -17.667 1.543   1.00 14.36 ?  115 ASN   B HD22 1 
ATOM   6087 N N    . PHE   B 1 116 ? 35.811 -17.119 -3.355  1.00 10.37 ?  116 PHE   B N    1 
ATOM   6088 C CA   . PHE   B 1 116 ? 36.238 -17.223 -4.744  1.00 10.49 ?  116 PHE   B CA   1 
ATOM   6089 C C    . PHE   B 1 116 ? 35.343 -16.403 -5.666  1.00 10.36 ?  116 PHE   B C    1 
ATOM   6090 O O    . PHE   B 1 116 ? 35.784 -15.976 -6.737  1.00 11.04 ?  116 PHE   B O    1 
ATOM   6091 C CB   . PHE   B 1 116 ? 36.203 -18.669 -5.264  1.00 10.15 ?  116 PHE   B CB   1 
ATOM   6092 C CG   . PHE   B 1 116 ? 37.271 -19.622 -4.718  1.00 10.46 ?  116 PHE   B CG   1 
ATOM   6093 C CD1  . PHE   B 1 116 ? 37.918 -19.442 -3.503  1.00 10.99 ?  116 PHE   B CD1  1 
ATOM   6094 C CD2  . PHE   B 1 116 ? 37.572 -20.759 -5.454  1.00 10.70 ?  116 PHE   B CD2  1 
ATOM   6095 C CE1  . PHE   B 1 116 ? 38.847 -20.385 -3.052  1.00 11.42 ?  116 PHE   B CE1  1 
ATOM   6096 C CE2  . PHE   B 1 116 ? 38.497 -21.696 -5.012  1.00 10.81 ?  116 PHE   B CE2  1 
ATOM   6097 C CZ   . PHE   B 1 116 ? 39.127 -21.516 -3.814  1.00 10.66 ?  116 PHE   B CZ   1 
ATOM   6098 H H    . PHE   B 1 116 ? 35.553 -17.867 -3.002  1.00 12.59 ?  116 PHE   B H    1 
ATOM   6099 H HA   . PHE   B 1 116 ? 37.141 -16.896 -4.828  1.00 12.74 ?  116 PHE   B HA   1 
ATOM   6100 H HB2  . PHE   B 1 116 ? 35.333 -19.048 -5.045  1.00 12.33 ?  116 PHE   B HB2  1 
ATOM   6101 H HB3  . PHE   B 1 116 ? 36.302 -18.646 -6.228  1.00 12.33 ?  116 PHE   B HB3  1 
ATOM   6102 H HD1  . PHE   B 1 116 ? 37.719 -18.698 -2.979  1.00 13.34 ?  116 PHE   B HD1  1 
ATOM   6103 H HD2  . PHE   B 1 116 ? 37.135 -20.902 -6.265  1.00 13.00 ?  116 PHE   B HD2  1 
ATOM   6104 H HE1  . PHE   B 1 116 ? 39.282 -20.258 -2.240  1.00 13.85 ?  116 PHE   B HE1  1 
ATOM   6105 H HE2  . PHE   B 1 116 ? 38.684 -22.444 -5.529  1.00 13.12 ?  116 PHE   B HE2  1 
ATOM   6106 H HZ   . PHE   B 1 116 ? 39.761 -22.128 -3.516  1.00 12.94 ?  116 PHE   B HZ   1 
ATOM   6107 N N    . ASN   B 1 117 ? 34.073 -16.197 -5.291  1.00 10.97 ?  117 ASN   B N    1 
ATOM   6108 C CA   . ASN   B 1 117 ? 33.131 -15.487 -6.160  1.00 11.51 ?  117 ASN   B CA   1 
ATOM   6109 C C    . ASN   B 1 117 ? 33.448 -14.007 -6.306  1.00 11.57 ?  117 ASN   B C    1 
ATOM   6110 O O    . ASN   B 1 117 ? 32.846 -13.343 -7.155  1.00 12.72 ?  117 ASN   B O    1 
ATOM   6111 C CB   . ASN   B 1 117 ? 31.706 -15.699 -5.665  1.00 11.81 ?  117 ASN   B CB   1 
ATOM   6112 C CG   . ASN   B 1 117 ? 31.248 -17.110 -5.911  1.00 12.01 ?  117 ASN   B CG   1 
ATOM   6113 O OD1  . ASN   B 1 117 ? 31.611 -17.703 -6.923  1.00 12.50 ?  117 ASN   B OD1  1 
ATOM   6114 N ND2  . ASN   B 1 117 ? 30.507 -17.679 -4.973  1.00 12.02 ?  117 ASN   B ND2  1 
ATOM   6115 H H    . ASN   B 1 117 ? 33.739 -16.459 -4.541  1.00 13.32 ?  117 ASN   B H    1 
ATOM   6116 H HA   . ASN   B 1 117 ? 33.187 -15.876 -7.040  1.00 13.96 ?  117 ASN   B HA   1 
ATOM   6117 H HB2  . ASN   B 1 117 ? 31.664 -15.527 -4.709  1.00 14.33 ?  117 ASN   B HB2  1 
ATOM   6118 H HB3  . ASN   B 1 117 ? 31.110 -15.092 -6.137  1.00 14.33 ?  117 ASN   B HB3  1 
ATOM   6119 H HD21 . ASN   B 1 117 ? 30.231 -18.486 -5.070  1.00 14.58 ?  117 ASN   B HD21 1 
ATOM   6120 H HD22 . ASN   B 1 117 ? 30.280 -17.230 -4.271  1.00 14.58 ?  117 ASN   B HD22 1 
ATOM   6121 N N    . GLN   B 1 118 ? 34.373 -13.482 -5.515  1.00 11.37 ?  118 GLN   B N    1 
ATOM   6122 C CA   . GLN   B 1 118 ? 34.806 -12.098 -5.653  1.00 11.76 ?  118 GLN   B CA   1 
ATOM   6123 C C    . GLN   B 1 118 ? 35.876 -11.908 -6.722  1.00 11.78 ?  118 GLN   B C    1 
ATOM   6124 O O    . GLN   B 1 118 ? 36.362 -10.780 -6.894  1.00 13.19 ?  118 GLN   B O    1 
ATOM   6125 C CB   . GLN   B 1 118 ? 35.283 -11.566 -4.298  1.00 12.29 ?  118 GLN   B CB   1 
ATOM   6126 C CG   . GLN   B 1 118 ? 34.196 -11.605 -3.233  1.00 12.62 ?  118 GLN   B CG   1 
ATOM   6127 C CD   . GLN   B 1 118 ? 33.039 -10.692 -3.561  1.00 12.35 ?  118 GLN   B CD   1 
ATOM   6128 O OE1  . GLN   B 1 118 ? 33.239 -9.555  -3.988  1.00 13.22 ?  118 GLN   B OE1  1 
ATOM   6129 N NE2  . GLN   B 1 118 ? 31.823 -11.177 -3.375  1.00 12.64 ?  118 GLN   B NE2  1 
ATOM   6130 H H    . GLN   B 1 118 ? 34.773 -13.908 -4.878  1.00 13.79 ?  118 GLN   B H    1 
ATOM   6131 H HA   . GLN   B 1 118 ? 34.044 -11.566 -5.921  1.00 14.26 ?  118 GLN   B HA   1 
ATOM   6132 H HB2  . GLN   B 1 118 ? 36.025 -12.100 -3.985  1.00 14.90 ?  118 GLN   B HB2  1 
ATOM   6133 H HB3  . GLN   B 1 118 ? 35.559 -10.639 -4.400  1.00 14.90 ?  118 GLN   B HB3  1 
ATOM   6134 H HG2  . GLN   B 1 118 ? 33.858 -12.512 -3.160  1.00 15.29 ?  118 GLN   B HG2  1 
ATOM   6135 H HG3  . GLN   B 1 118 ? 34.572 -11.320 -2.386  1.00 15.29 ?  118 GLN   B HG3  1 
ATOM   6136 H HE21 . GLN   B 1 118 ? 31.721 -11.978 -3.077  1.00 15.32 ?  118 GLN   B HE21 1 
ATOM   6137 H HE22 . GLN   B 1 118 ? 31.139 -10.694 -3.559  1.00 15.32 ?  118 GLN   B HE22 1 
ATOM   6138 N N    . HIS   B 1 119 ? 36.228 -12.966 -7.459  1.00 11.11 ?  119 HIS   B N    1 
ATOM   6139 C CA   . HIS   B 1 119 ? 37.279 -12.922 -8.467  1.00 11.77 ?  119 HIS   B CA   1 
ATOM   6140 C C    . HIS   B 1 119 ? 36.798 -13.648 -9.709  1.00 11.64 ?  119 HIS   B C    1 
ATOM   6141 O O    . HIS   B 1 119 ? 36.288 -14.764 -9.612  1.00 12.54 ?  119 HIS   B O    1 
ATOM   6142 C CB   . HIS   B 1 119 ? 38.547 -13.563 -7.908  1.00 12.19 ?  119 HIS   B CB   1 
ATOM   6143 C CG   . HIS   B 1 119 ? 39.025 -12.872 -6.679  1.00 13.33 ?  119 HIS   B CG   1 
ATOM   6144 N ND1  . HIS   B 1 119 ? 39.841 -11.761 -6.725  1.00 14.96 ?  119 HIS   B ND1  1 
ATOM   6145 C CD2  . HIS   B 1 119 ? 38.723 -13.068 -5.375  1.00 14.65 ?  119 HIS   B CD2  1 
ATOM   6146 C CE1  . HIS   B 1 119 ? 40.044 -11.325 -5.496  1.00 16.04 ?  119 HIS   B CE1  1 
ATOM   6147 N NE2  . HIS   B 1 119 ? 39.375 -12.097 -4.659  1.00 16.03 ?  119 HIS   B NE2  1 
ATOM   6148 H H    . HIS   B 1 119 ? 35.848 -13.741 -7.395  1.00 13.48 ?  119 HIS   B H    1 
ATOM   6149 H HA   . HIS   B 1 119 ? 37.467 -11.997 -8.694  1.00 14.27 ?  119 HIS   B HA   1 
ATOM   6150 H HB2  . HIS   B 1 119 ? 38.360 -14.490 -7.685  1.00 14.77 ?  119 HIS   B HB2  1 
ATOM   6151 H HB3  . HIS   B 1 119 ? 39.245 -13.514 -8.576  1.00 14.77 ?  119 HIS   B HB3  1 
ATOM   6152 H HD2  . HIS   B 1 119 ? 38.178 -13.739 -5.025  1.00 17.74 ?  119 HIS   B HD2  1 
ATOM   6153 H HE1  . HIS   B 1 119 ? 40.588 -10.613 -5.257  1.00 19.39 ?  119 HIS   B HE1  1 
ATOM   6154 H HE2  . HIS   B 1 119 ? 39.375 -12.023 -3.797  1.00 19.39 ?  119 HIS   B HE2  1 
ATOM   6155 N N    . GLU   B 1 120 ? 36.948 -13.023 -10.877 1.00 12.36 ?  120 GLU   B N    1 
ATOM   6156 C CA   . GLU   B 1 120 ? 36.348 -13.605 -12.074 1.00 13.59 ?  120 GLU   B CA   1 
ATOM   6157 C C    . GLU   B 1 120 ? 37.029 -14.898 -12.503 1.00 12.56 ?  120 GLU   B C    1 
ATOM   6158 O O    . GLU   B 1 120 ? 36.373 -15.766 -13.091 1.00 12.86 ?  120 GLU   B O    1 
ATOM   6159 C CB   . GLU   B 1 120 ? 36.335 -12.587 -13.213 1.00 17.53 ?  120 GLU   B CB   1 
ATOM   6160 C CG   . GLU   B 1 120 ? 35.370 -11.443 -12.973 1.00 22.91 ?  120 GLU   B CG   1 
ATOM   6161 C CD   . GLU   B 1 120 ? 35.137 -10.589 -14.201 1.00 28.02 ?  120 GLU   B CD   1 
ATOM   6162 O OE1  . GLU   B 1 120 ? 36.117 -10.315 -14.928 1.00 30.23 ?  120 GLU   B OE1  1 
ATOM   6163 O OE2  . GLU   B 1 120 ? 33.975 -10.187 -14.435 1.00 30.60 -1 120 GLU   B OE2  1 
ATOM   6164 H H    . GLU   B 1 120 ? 37.371 -12.282 -10.998 1.00 14.99 ?  120 GLU   B H    1 
ATOM   6165 H HA   . GLU   B 1 120 ? 35.425 -13.821 -11.873 1.00 16.47 ?  120 GLU   B HA   1 
ATOM   6166 H HB2  . GLU   B 1 120 ? 37.220 -12.213 -13.316 1.00 21.19 ?  120 GLU   B HB2  1 
ATOM   6167 H HB3  . GLU   B 1 120 ? 36.066 -13.036 -14.032 1.00 21.19 ?  120 GLU   B HB3  1 
ATOM   6168 H HG2  . GLU   B 1 120 ? 34.511 -11.802 -12.700 1.00 27.64 ?  120 GLU   B HG2  1 
ATOM   6169 H HG3  . GLU   B 1 120 ? 35.726 -10.866 -12.285 1.00 27.64 ?  120 GLU   B HG3  1 
ATOM   6170 N N    . VAL   B 1 121 ? 38.326 -15.046 -12.235 1.00 12.24 ?  121 VAL   B N    1 
ATOM   6171 C CA   . VAL   B 1 121 ? 39.066 -16.257 -12.585 1.00 11.87 ?  121 VAL   B CA   1 
ATOM   6172 C C    . VAL   B 1 121 ? 40.185 -16.471 -11.571 1.00 11.76 ?  121 VAL   B C    1 
ATOM   6173 O O    . VAL   B 1 121 ? 40.874 -15.521 -11.181 1.00 12.34 ?  121 VAL   B O    1 
ATOM   6174 C CB   . VAL   B 1 121 ? 39.577 -16.210 -14.044 1.00 14.14 ?  121 VAL   B CB   1 
ATOM   6175 C CG1  . VAL   B 1 121 ? 40.418 -14.970 -14.295 1.00 15.38 ?  121 VAL   B CG1  1 
ATOM   6176 C CG2  . VAL   B 1 121 ? 40.332 -17.491 -14.394 1.00 15.40 ?  121 VAL   B CG2  1 
ATOM   6177 H H    . VAL   B 1 121 ? 38.808 -14.445 -11.850 1.00 14.84 ?  121 VAL   B H    1 
ATOM   6178 H HA   . VAL   B 1 121 ? 38.454 -17.006 -12.516 1.00 14.39 ?  121 VAL   B HA   1 
ATOM   6179 H HB   . VAL   B 1 121 ? 38.807 -16.160 -14.632 1.00 17.12 ?  121 VAL   B HB   1 
ATOM   6180 H HG11 . VAL   B 1 121 ? 40.744 -14.990 -15.209 1.00 18.60 ?  121 VAL   B HG11 1 
ATOM   6181 H HG12 . VAL   B 1 121 ? 39.867 -14.180 -14.162 1.00 18.60 ?  121 VAL   B HG12 1 
ATOM   6182 H HG13 . VAL   B 1 121 ? 41.164 -14.959 -13.677 1.00 18.60 ?  121 VAL   B HG13 1 
ATOM   6183 H HG21 . VAL   B 1 121 ? 40.529 -17.489 -15.344 1.00 18.63 ?  121 VAL   B HG21 1 
ATOM   6184 H HG22 . VAL   B 1 121 ? 41.158 -17.523 -13.886 1.00 18.63 ?  121 VAL   B HG22 1 
ATOM   6185 H HG23 . VAL   B 1 121 ? 39.777 -18.255 -14.174 1.00 18.63 ?  121 VAL   B HG23 1 
ATOM   6186 N N    . LEU   B 1 122 ? 40.370 -17.727 -11.151 1.00 11.11 ?  122 LEU   B N    1 
ATOM   6187 C CA   . LEU   B 1 122 ? 41.343 -18.081 -10.124 1.00 10.67 ?  122 LEU   B CA   1 
ATOM   6188 C C    . LEU   B 1 122 ? 41.997 -19.412 -10.449 1.00 10.57 ?  122 LEU   B C    1 
ATOM   6189 O O    . LEU   B 1 122 ? 41.335 -20.334 -10.943 1.00 11.96 ?  122 LEU   B O    1 
ATOM   6190 C CB   . LEU   B 1 122 ? 40.688 -18.320 -8.747  1.00 12.63 ?  122 LEU   B CB   1 
ATOM   6191 C CG   . LEU   B 1 122 ? 39.657 -17.297 -8.260  1.00 12.64 ?  122 LEU   B CG   1 
ATOM   6192 C CD1  . LEU   B 1 122 ? 38.273 -17.677 -8.738  1.00 13.15 ?  122 LEU   B CD1  1 
ATOM   6193 C CD2  . LEU   B 1 122 ? 39.691 -17.184 -6.748  1.00 11.91 ?  122 LEU   B CD2  1 
ATOM   6194 H H    . LEU   B 1 122 ? 39.945 -18.408 -11.461 1.00 13.49 ?  122 LEU   B H    1 
ATOM   6195 H HA   . LEU   B 1 122 ? 42.023 -17.389 -10.042 1.00 12.96 ?  122 LEU   B HA   1 
ATOM   6196 H HB2  . LEU   B 1 122 ? 40.242 -19.178 -8.772  1.00 15.31 ?  122 LEU   B HB2  1 
ATOM   6197 H HB3  . LEU   B 1 122 ? 41.392 -18.344 -8.079  1.00 15.31 ?  122 LEU   B HB3  1 
ATOM   6198 H HG   . LEU   B 1 122 ? 39.871 -16.424 -8.631  1.00 15.32 ?  122 LEU   B HG   1 
ATOM   6199 H HD11 . LEU   B 1 122 ? 37.633 -17.033 -8.404  1.00 15.94 ?  122 LEU   B HD11 1 
ATOM   6200 H HD12 . LEU   B 1 122 ? 38.263 -17.681 -9.709  1.00 15.94 ?  122 LEU   B HD12 1 
ATOM   6201 H HD13 . LEU   B 1 122 ? 38.058 -18.563 -8.404  1.00 15.94 ?  122 LEU   B HD13 1 
ATOM   6202 H HD21 . LEU   B 1 122 ? 39.013 -16.552 -6.456  1.00 14.44 ?  122 LEU   B HD21 1 
ATOM   6203 H HD22 . LEU   B 1 122 ? 39.516 -18.056 -6.359  1.00 14.44 ?  122 LEU   B HD22 1 
ATOM   6204 H HD23 . LEU   B 1 122 ? 40.569 -16.872 -6.471  1.00 14.44 ?  122 LEU   B HD23 1 
ATOM   6205 N N    . LEU   B 1 123 ? 43.284 -19.524 -10.087 1.00 10.07 ?  123 LEU   B N    1 
ATOM   6206 C CA   . LEU   B 1 123 ? 43.996 -20.797 -9.965  1.00 10.43 ?  123 LEU   B CA   1 
ATOM   6207 C C    . LEU   B 1 123 ? 43.964 -21.191 -8.493  1.00 10.09 ?  123 LEU   B C    1 
ATOM   6208 O O    . LEU   B 1 123 ? 44.318 -20.361 -7.644  1.00 10.64 ?  123 LEU   B O    1 
ATOM   6209 C CB   . LEU   B 1 123 ? 45.451 -20.624 -10.416 1.00 10.98 ?  123 LEU   B CB   1 
ATOM   6210 C CG   . LEU   B 1 123 ? 46.387 -21.810 -10.177 1.00 11.21 ?  123 LEU   B CG   1 
ATOM   6211 C CD1  . LEU   B 1 123 ? 45.940 -23.048 -10.944 1.00 11.90 ?  123 LEU   B CD1  1 
ATOM   6212 C CD2  . LEU   B 1 123 ? 47.801 -21.425 -10.562 1.00 12.20 ?  123 LEU   B CD2  1 
ATOM   6213 H H    . LEU   B 1 123 ? 43.775 -18.850 -9.876  1.00 12.24 ?  123 LEU   B H    1 
ATOM   6214 H HA   . LEU   B 1 123 ? 43.560 -21.485 -10.494 1.00 12.67 ?  123 LEU   B HA   1 
ATOM   6215 H HB2  . LEU   B 1 123 ? 45.450 -20.447 -11.371 1.00 13.32 ?  123 LEU   B HB2  1 
ATOM   6216 H HB3  . LEU   B 1 123 ? 45.826 -19.862 -9.949  1.00 13.32 ?  123 LEU   B HB3  1 
ATOM   6217 H HG   . LEU   B 1 123 ? 46.388 -22.031 -9.230  1.00 13.61 ?  123 LEU   B HG   1 
ATOM   6218 H HD11 . LEU   B 1 123 ? 46.571 -23.767 -10.784 1.00 14.43 ?  123 LEU   B HD11 1 
ATOM   6219 H HD12 . LEU   B 1 123 ? 45.056 -23.314 -10.630 1.00 14.43 ?  123 LEU   B HD12 1 
ATOM   6220 H HD13 . LEU   B 1 123 ? 45.903 -22.841 -11.888 1.00 14.43 ?  123 LEU   B HD13 1 
ATOM   6221 H HD21 . LEU   B 1 123 ? 48.387 -22.180 -10.411 1.00 14.80 ?  123 LEU   B HD21 1 
ATOM   6222 H HD22 . LEU   B 1 123 ? 47.812 -21.179 -11.503 1.00 14.80 ?  123 LEU   B HD22 1 
ATOM   6223 H HD23 . LEU   B 1 123 ? 48.079 -20.671 -10.021 1.00 14.80 ?  123 LEU   B HD23 1 
ATOM   6224 N N    . ALA   B 1 124 ? 43.520 -22.416 -8.176  1.00 10.02 ?  124 ALA   B N    1 
ATOM   6225 C CA   . ALA   B 1 124 ? 43.269 -22.727 -6.775  1.00 10.06 ?  124 ALA   B CA   1 
ATOM   6226 C C    . ALA   B 1 124 ? 43.546 -24.189 -6.455  1.00 9.67  ?  124 ALA   B C    1 
ATOM   6227 O O    . ALA   B 1 124 ? 43.398 -25.064 -7.320  1.00 10.59 ?  124 ALA   B O    1 
ATOM   6228 C CB   . ALA   B 1 124 ? 41.815 -22.432 -6.401  1.00 10.76 ?  124 ALA   B CB   1 
ATOM   6229 H H    . ALA   B 1 124 ? 43.341 -23.058 -8.738  1.00 12.18 ?  124 ALA   B H    1 
ATOM   6230 H HA   . ALA   B 1 124 ? 43.850 -22.177 -6.233  1.00 12.22 ?  124 ALA   B HA   1 
ATOM   6231 H HB1  . ALA   B 1 124 ? 41.675 -22.644 -5.466  1.00 13.06 ?  124 ALA   B HB1  1 
ATOM   6232 H HB2  . ALA   B 1 124 ? 41.636 -21.490 -6.557  1.00 13.06 ?  124 ALA   B HB2  1 
ATOM   6233 H HB3  . ALA   B 1 124 ? 41.227 -22.973 -6.954  1.00 13.06 ?  124 ALA   B HB3  1 
ATOM   6234 N N    . PRO   B 1 125 ? 43.851 -24.488 -5.195  1.00 10.33 ?  125 PRO   B N    1 
ATOM   6235 C CA   . PRO   B 1 125 ? 43.774 -25.854 -4.676  1.00 10.99 ?  125 PRO   B CA   1 
ATOM   6236 C C    . PRO   B 1 125 ? 42.369 -26.121 -4.131  1.00 10.93 ?  125 PRO   B C    1 
ATOM   6237 O O    . PRO   B 1 125 ? 41.574 -25.202 -3.923  1.00 11.48 ?  125 PRO   B O    1 
ATOM   6238 C CB   . PRO   B 1 125 ? 44.766 -25.790 -3.509  1.00 12.06 ?  125 PRO   B CB   1 
ATOM   6239 C CG   . PRO   B 1 125 ? 44.522 -24.401 -2.935  1.00 12.10 ?  125 PRO   B CG   1 
ATOM   6240 C CD   . PRO   B 1 125 ? 44.179 -23.525 -4.128  1.00 11.09 ?  125 PRO   B CD   1 
ATOM   6241 H HA   . PRO   B 1 125 ? 44.042 -26.521 -5.329  1.00 13.33 ?  125 PRO   B HA   1 
ATOM   6242 H HB2  . PRO   B 1 125 ? 44.558 -26.478 -2.853  1.00 14.62 ?  125 PRO   B HB2  1 
ATOM   6243 H HB3  . PRO   B 1 125 ? 45.675 -25.881 -3.832  1.00 14.62 ?  125 PRO   B HB3  1 
ATOM   6244 H HG2  . PRO   B 1 125 ? 43.779 -24.423 -2.309  1.00 14.68 ?  125 PRO   B HG2  1 
ATOM   6245 H HG3  . PRO   B 1 125 ? 45.326 -24.077 -2.492  1.00 14.68 ?  125 PRO   B HG3  1 
ATOM   6246 H HD2  . PRO   B 1 125 ? 43.417 -22.966 -3.934  1.00 13.47 ?  125 PRO   B HD2  1 
ATOM   6247 H HD3  . PRO   B 1 125 ? 44.956 -22.991 -4.382  1.00 13.47 ?  125 PRO   B HD3  1 
ATOM   6248 N N    . LEU   B 1 126 ? 42.092 -27.399 -3.852  1.00 11.66 ?  126 LEU   B N    1 
ATOM   6249 C CA   . LEU   B 1 126 ? 40.880 -27.756 -3.119  1.00 12.23 ?  126 LEU   B CA   1 
ATOM   6250 C C    . LEU   B 1 126 ? 41.004 -27.356 -1.655  1.00 12.60 ?  126 LEU   B C    1 
ATOM   6251 O O    . LEU   B 1 126 ? 41.898 -27.818 -0.942  1.00 14.62 ?  126 LEU   B O    1 
ATOM   6252 C CB   . LEU   B 1 126 ? 40.617 -29.250 -3.222  1.00 13.74 ?  126 LEU   B CB   1 
ATOM   6253 C CG   . LEU   B 1 126 ? 40.105 -29.744 -4.574  1.00 14.93 ?  126 LEU   B CG   1 
ATOM   6254 C CD1  . LEU   B 1 126 ? 40.138 -31.259 -4.609  1.00 16.67 ?  126 LEU   B CD1  1 
ATOM   6255 C CD2  . LEU   B 1 126 ? 38.696 -29.232 -4.862  1.00 15.09 ?  126 LEU   B CD2  1 
ATOM   6256 H H    . LEU   B 1 126 ? 42.584 -28.072 -4.077  1.00 14.14 ?  126 LEU   B H    1 
ATOM   6257 H HA   . LEU   B 1 126 ? 40.125 -27.281 -3.508  1.00 14.83 ?  126 LEU   B HA   1 
ATOM   6258 H HB2  . LEU   B 1 126 ? 41.445 -29.716 -3.038  1.00 16.63 ?  126 LEU   B HB2  1 
ATOM   6259 H HB3  . LEU   B 1 126 ? 39.953 -29.485 -2.560  1.00 16.63 ?  126 LEU   B HB3  1 
ATOM   6260 H HG   . LEU   B 1 126 ? 40.695 -29.409 -5.275  1.00 18.07 ?  126 LEU   B HG   1 
ATOM   6261 H HD11 . LEU   B 1 126 ? 39.808 -31.562 -5.468  1.00 20.16 ?  126 LEU   B HD11 1 
ATOM   6262 H HD12 . LEU   B 1 126 ? 41.051 -31.558 -4.479  1.00 20.16 ?  126 LEU   B HD12 1 
ATOM   6263 H HD13 . LEU   B 1 126 ? 39.573 -31.600 -3.897  1.00 20.16 ?  126 LEU   B HD13 1 
ATOM   6264 H HD21 . LEU   B 1 126 ? 38.369 -29.651 -5.674  1.00 18.26 ?  126 LEU   B HD21 1 
ATOM   6265 H HD22 . LEU   B 1 126 ? 38.121 -29.456 -4.117  1.00 18.26 ?  126 LEU   B HD22 1 
ATOM   6266 H HD23 . LEU   B 1 126 ? 38.723 -28.267 -4.980  1.00 18.26 ?  126 LEU   B HD23 1 
ATOM   6267 N N    . LEU   B 1 127 ? 40.074 -26.534 -1.190  1.00 12.42 ?  127 LEU   B N    1 
ATOM   6268 C CA   . LEU   B 1 127 ? 40.129 -26.044 0.174   1.00 12.94 ?  127 LEU   B CA   1 
ATOM   6269 C C    . LEU   B 1 127 ? 39.846 -27.162 1.168   1.00 12.46 ?  127 LEU   B C    1 
ATOM   6270 O O    . LEU   B 1 127 ? 39.020 -28.051 0.939   1.00 13.13 ?  127 LEU   B O    1 
ATOM   6271 C CB   . LEU   B 1 127 ? 39.117 -24.920 0.381   1.00 13.13 ?  127 LEU   B CB   1 
ATOM   6272 C CG   . LEU   B 1 127 ? 39.303 -23.661 -0.465  1.00 13.82 ?  127 LEU   B CG   1 
ATOM   6273 C CD1  . LEU   B 1 127 ? 38.183 -22.682 -0.135  1.00 14.23 ?  127 LEU   B CD1  1 
ATOM   6274 C CD2  . LEU   B 1 127 ? 40.682 -23.031 -0.261  1.00 14.68 ?  127 LEU   B CD2  1 
ATOM   6275 H H    . LEU   B 1 127 ? 39.405 -26.232 -1.651  1.00 15.06 ?  127 LEU   B H    1 
ATOM   6276 H HA   . LEU   B 1 127 ? 41.016 -25.690 0.351   1.00 15.68 ?  127 LEU   B HA   1 
ATOM   6277 H HB2  . LEU   B 1 127 ? 38.234 -25.272 0.180   1.00 15.91 ?  127 LEU   B HB2  1 
ATOM   6278 H HB3  . LEU   B 1 127 ? 39.151 -24.651 1.310   1.00 15.91 ?  127 LEU   B HB3  1 
ATOM   6279 H HG   . LEU   B 1 127 ? 39.218 -23.895 -1.401  1.00 16.73 ?  127 LEU   B HG   1 
ATOM   6280 H HD11 . LEU   B 1 127 ? 38.308 -21.872 -0.661  1.00 17.22 ?  127 LEU   B HD11 1 
ATOM   6281 H HD12 . LEU   B 1 127 ? 37.332 -23.086 -0.346  1.00 17.22 ?  127 LEU   B HD12 1 
ATOM   6282 H HD13 . LEU   B 1 127 ? 38.225 -22.462 0.811   1.00 17.22 ?  127 LEU   B HD13 1 
ATOM   6283 H HD21 . LEU   B 1 127 ? 40.718 -22.186 -0.733  1.00 17.77 ?  127 LEU   B HD21 1 
ATOM   6284 H HD22 . LEU   B 1 127 ? 40.826 -22.887 0.688   1.00 17.77 ?  127 LEU   B HD22 1 
ATOM   6285 H HD23 . LEU   B 1 127 ? 41.358 -23.635 -0.609  1.00 17.77 ?  127 LEU   B HD23 1 
ATOM   6286 N N    . SER   B 1 128 ? 40.520 -27.076 2.303   1.00 12.60 ?  128 SER   B N    1 
ATOM   6287 C CA   . SER   B 1 128 ? 40.406 -27.987 3.431   1.00 13.42 ?  128 SER   B CA   1 
ATOM   6288 C C    . SER   B 1 128 ? 40.896 -29.399 3.114   1.00 14.69 ?  128 SER   B C    1 
ATOM   6289 O O    . SER   B 1 128 ? 40.793 -30.276 3.969   1.00 16.47 ?  128 SER   B O    1 
ATOM   6290 C CB   . SER   B 1 128 ? 39.004 -27.979 4.069   1.00 13.68 ?  128 SER   B CB   1 
ATOM   6291 O OG   . SER   B 1 128 ? 38.710 -26.690 4.609   1.00 14.17 ?  128 SER   B OG   1 
ATOM   6292 H H    . SER   B 1 128 ? 41.082 -26.446 2.453   1.00 15.27 ?  128 SER   B H    1 
ATOM   6293 H HA   . SER   B 1 128 ? 40.997 -27.652 4.109   1.00 16.25 ?  128 SER   B HA   1 
ATOM   6294 H HB2  . SER   B 1 128 ? 38.338 -28.208 3.405   1.00 16.56 ?  128 SER   B HB2  1 
ATOM   6295 H HB3  . SER   B 1 128 ? 38.984 -28.637 4.794   1.00 16.56 ?  128 SER   B HB3  1 
ATOM   6296 H HG   . SER   B 1 128 ? 39.282 -26.484 5.192   1.00 17.16 ?  128 SER   B HG   1 
ATOM   6297 N N    . ALA   B 1 129 ? 41.470 -29.630 1.927   1.00 15.71 ?  129 ALA   B N    1 
ATOM   6298 C CA   . ALA   B 1 129 ? 42.019 -30.924 1.552   1.00 16.90 ?  129 ALA   B CA   1 
ATOM   6299 C C    . ALA   B 1 129 ? 43.409 -31.109 2.151   1.00 15.66 ?  129 ALA   B C    1 
ATOM   6300 O O    . ALA   B 1 129 ? 43.970 -30.213 2.797   1.00 15.23 ?  129 ALA   B O    1 
ATOM   6301 C CB   . ALA   B 1 129 ? 42.081 -31.052 0.031   1.00 18.93 ?  129 ALA   B CB   1 
ATOM   6302 H H    . ALA   B 1 129 ? 41.547 -29.034 1.307   1.00 19.00 ?  129 ALA   B H    1 
ATOM   6303 H HA   . ALA   B 1 129 ? 41.447 -31.622 1.892   1.00 20.43 ?  129 ALA   B HA   1 
ATOM   6304 H HB1  . ALA   B 1 129 ? 42.442 -31.922 -0.199  1.00 22.87 ?  129 ALA   B HB1  1 
ATOM   6305 H HB2  . ALA   B 1 129 ? 41.186 -30.959 -0.331  1.00 22.87 ?  129 ALA   B HB2  1 
ATOM   6306 H HB3  . ALA   B 1 129 ? 42.654 -30.353 -0.326  1.00 22.87 ?  129 ALA   B HB3  1 
ATOM   6307 N N    . GLY   B 1 130 ? 43.974 -32.290 1.914   1.00 15.64 ?  130 GLY   B N    1 
ATOM   6308 C CA   . GLY   B 1 130 ? 45.366 -32.521 2.256   1.00 16.33 ?  130 GLY   B CA   1 
ATOM   6309 C C    . GLY   B 1 130 ? 45.586 -32.430 3.748   1.00 15.86 ?  130 GLY   B C    1 
ATOM   6310 O O    . GLY   B 1 130 ? 44.888 -33.073 4.544   1.00 16.89 ?  130 GLY   B O    1 
ATOM   6311 H H    . GLY   B 1 130 ? 43.577 -32.960 1.544   1.00 18.92 ?  130 GLY   B H    1 
ATOM   6312 H HA2  . GLY   B 1 130 ? 45.636 -33.408 1.956   1.00 19.75 ?  130 GLY   B HA2  1 
ATOM   6313 H HA3  . GLY   B 1 130 ? 45.931 -31.866 1.815   1.00 19.75 ?  130 GLY   B HA3  1 
ATOM   6314 N N    . ILE   B 1 131 ? 46.564 -31.604 4.137   1.00 16.79 ?  131 ILE   B N    1 
ATOM   6315 C CA   . ILE   B 1 131 ? 46.942 -31.477 5.539   1.00 17.77 ?  131 ILE   B CA   1 
ATOM   6316 C C    . ILE   B 1 131 ? 45.831 -30.880 6.385   1.00 17.00 ?  131 ILE   B C    1 
ATOM   6317 O O    . ILE   B 1 131 ? 45.910 -30.944 7.615   1.00 18.42 ?  131 ILE   B O    1 
ATOM   6318 C CB   . ILE   B 1 131 ? 48.266 -30.698 5.714   1.00 19.46 ?  131 ILE   B CB   1 
ATOM   6319 C CG1  . ILE   B 1 131 ? 48.092 -29.216 5.359   1.00 20.14 ?  131 ILE   B CG1  1 
ATOM   6320 C CG2  . ILE   B 1 131 ? 49.371 -31.329 4.868   1.00 20.41 ?  131 ILE   B CG2  1 
ATOM   6321 C CD1  . ILE   B 1 131 ? 49.315 -28.363 5.650   1.00 21.24 ?  131 ILE   B CD1  1 
ATOM   6322 H H    . ILE   B 1 131 ? 47.023 -31.108 3.611   1.00 20.29 ?  131 ILE   B H    1 
ATOM   6323 H HA   . ILE   B 1 131 ? 47.098 -32.369 5.884   1.00 21.47 ?  131 ILE   B HA   1 
ATOM   6324 H HB   . ILE   B 1 131 ? 48.532 -30.756 6.643   1.00 23.51 ?  131 ILE   B HB   1 
ATOM   6325 H HG12 . ILE   B 1 131 ? 47.895 -29.144 4.412   1.00 24.32 ?  131 ILE   B HG12 1 
ATOM   6326 H HG13 . ILE   B 1 131 ? 47.355 -28.851 5.874   1.00 24.32 ?  131 ILE   B HG13 1 
ATOM   6327 H HG21 . ILE   B 1 131 ? 50.219 -30.929 5.109   1.00 24.64 ?  131 ILE   B HG21 1 
ATOM   6328 H HG22 . ILE   B 1 131 ? 49.389 -32.281 5.041   1.00 24.64 ?  131 ILE   B HG22 1 
ATOM   6329 H HG23 . ILE   B 1 131 ? 49.179 -31.165 3.930   1.00 24.64 ?  131 ILE   B HG23 1 
ATOM   6330 H HD11 . ILE   B 1 131 ? 49.090 -27.432 5.496   1.00 25.63 ?  131 ILE   B HD11 1 
ATOM   6331 H HD12 . ILE   B 1 131 ? 49.575 -28.492 6.575   1.00 25.63 ?  131 ILE   B HD12 1 
ATOM   6332 H HD13 . ILE   B 1 131 ? 50.035 -28.632 5.061   1.00 25.63 ?  131 ILE   B HD13 1 
ATOM   6333 N N    . PHE   B 1 132 ? 44.792 -30.313 5.762   1.00 15.89 ?  132 PHE   B N    1 
ATOM   6334 C CA   . PHE   B 1 132 ? 43.645 -29.790 6.496   1.00 16.23 ?  132 PHE   B CA   1 
ATOM   6335 C C    . PHE   B 1 132 ? 42.615 -30.868 6.831   1.00 17.80 ?  132 PHE   B C    1 
ATOM   6336 O O    . PHE   B 1 132 ? 41.711 -30.603 7.632   1.00 19.56 ?  132 PHE   B O    1 
ATOM   6337 C CB   . PHE   B 1 132 ? 42.972 -28.663 5.701   1.00 15.18 ?  132 PHE   B CB   1 
ATOM   6338 C CG   . PHE   B 1 132 ? 43.661 -27.314 5.807   1.00 14.55 ?  132 PHE   B CG   1 
ATOM   6339 C CD1  . PHE   B 1 132 ? 44.959 -27.128 5.356   1.00 15.82 ?  132 PHE   B CD1  1 
ATOM   6340 C CD2  . PHE   B 1 132 ? 42.967 -26.219 6.305   1.00 14.12 ?  132 PHE   B CD2  1 
ATOM   6341 C CE1  . PHE   B 1 132 ? 45.565 -25.883 5.445   1.00 16.07 ?  132 PHE   B CE1  1 
ATOM   6342 C CE2  . PHE   B 1 132 ? 43.564 -24.972 6.387   1.00 14.69 ?  132 PHE   B CE2  1 
ATOM   6343 C CZ   . PHE   B 1 132 ? 44.862 -24.806 5.956   1.00 15.58 ?  132 PHE   B CZ   1 
ATOM   6344 H H    . PHE   B 1 132 ? 44.726 -30.229 4.910   1.00 19.22 ?  132 PHE   B H    1 
ATOM   6345 H HA   . PHE   B 1 132 ? 43.958 -29.417 7.333   1.00 19.62 ?  132 PHE   B HA   1 
ATOM   6346 H HB2  . PHE   B 1 132 ? 42.967 -28.915 4.766   1.00 18.37 ?  132 PHE   B HB2  1 
ATOM   6347 H HB3  . PHE   B 1 132 ? 42.064 -28.563 6.021   1.00 18.37 ?  132 PHE   B HB3  1 
ATOM   6348 H HD1  . PHE   B 1 132 ? 45.434 -27.857 5.020   1.00 19.14 ?  132 PHE   B HD1  1 
ATOM   6349 H HD2  . PHE   B 1 132 ? 42.087 -26.333 6.600   1.00 17.10 ?  132 PHE   B HD2  1 
ATOM   6350 H HE1  . PHE   B 1 132 ? 46.439 -25.774 5.156   1.00 19.43 ?  132 PHE   B HE1  1 
ATOM   6351 H HE2  . PHE   B 1 132 ? 43.085 -24.254 6.738   1.00 17.78 ?  132 PHE   B HE2  1 
ATOM   6352 H HZ   . PHE   B 1 132 ? 45.262 -23.969 6.019   1.00 18.84 ?  132 PHE   B HZ   1 
ATOM   6353 N N    . GLY   B 1 133 ? 42.704 -32.060 6.228   1.00 17.84 ?  133 GLY   B N    1 
ATOM   6354 C CA   . GLY   B 1 133 ? 41.987 -33.222 6.724   1.00 18.92 ?  133 GLY   B CA   1 
ATOM   6355 C C    . GLY   B 1 133 ? 40.593 -33.482 6.183   1.00 19.31 ?  133 GLY   B C    1 
ATOM   6356 O O    . GLY   B 1 133 ? 40.004 -34.508 6.543   1.00 21.32 ?  133 GLY   B O    1 
ATOM   6357 H H    . GLY   B 1 133 ? 43.182 -32.213 5.528   1.00 21.56 ?  133 GLY   B H    1 
ATOM   6358 H HA2  . GLY   B 1 133 ? 42.526 -34.007 6.542   1.00 22.85 ?  133 GLY   B HA2  1 
ATOM   6359 H HA3  . GLY   B 1 133 ? 41.905 -33.138 7.684   1.00 22.85 ?  133 GLY   B HA3  1 
ATOM   6360 N N    . ALA   B 1 134 ? 40.032 -32.609 5.352   1.00 17.94 ?  134 ALA   B N    1 
ATOM   6361 C CA   . ALA   B 1 134 ? 38.705 -32.887 4.815   1.00 18.02 ?  134 ALA   B CA   1 
ATOM   6362 C C    . ALA   B 1 134 ? 38.787 -33.883 3.663   1.00 17.37 ?  134 ALA   B C    1 
ATOM   6363 O O    . ALA   B 1 134 ? 39.837 -34.073 3.043   1.00 18.72 ?  134 ALA   B O    1 
ATOM   6364 C CB   . ALA   B 1 134 ? 38.026 -31.607 4.332   1.00 18.65 ?  134 ALA   B CB   1 
ATOM   6365 H H    . ALA   B 1 134 ? 40.383 -31.866 5.095   1.00 21.68 ?  134 ALA   B H    1 
ATOM   6366 H HA   . ALA   B 1 134 ? 38.157 -33.277 5.512   1.00 21.78 ?  134 ALA   B HA   1 
ATOM   6367 H HB1  . ALA   B 1 134 ? 37.138 -31.829 4.008   1.00 22.53 ?  134 ALA   B HB1  1 
ATOM   6368 H HB2  . ALA   B 1 134 ? 37.964 -30.988 5.073   1.00 22.53 ?  134 ALA   B HB2  1 
ATOM   6369 H HB3  . ALA   B 1 134 ? 38.554 -31.221 3.617   1.00 22.53 ?  134 ALA   B HB3  1 
ATOM   6370 N N    . ASP   B 1 135 ? 37.653 -34.514 3.377   1.00 17.76 ?  135 ASP   B N    1 
ATOM   6371 C CA   . ASP   B 1 135 ? 37.551 -35.407 2.232   1.00 18.51 ?  135 ASP   B CA   1 
ATOM   6372 C C    . ASP   B 1 135 ? 37.645 -34.567 0.966   1.00 17.16 ?  135 ASP   B C    1 
ATOM   6373 O O    . ASP   B 1 135 ? 36.788 -33.698 0.746   1.00 17.24 ?  135 ASP   B O    1 
ATOM   6374 C CB   . ASP   B 1 135 ? 36.214 -36.138 2.287   1.00 20.30 ?  135 ASP   B CB   1 
ATOM   6375 C CG   . ASP   B 1 135 ? 36.036 -37.133 1.159   1.00 22.26 ?  135 ASP   B CG   1 
ATOM   6376 O OD1  . ASP   B 1 135 ? 36.894 -37.187 0.256   1.00 22.15 ?  135 ASP   B OD1  1 
ATOM   6377 O OD2  . ASP   B 1 135 ? 35.034 -37.882 1.187   1.00 25.02 -1 135 ASP   B OD2  1 
ATOM   6378 H H    . ASP   B 1 135 ? 36.925 -34.436 3.825   1.00 21.47 ?  135 ASP   B H    1 
ATOM   6379 H HA   . ASP   B 1 135 ? 38.269 -36.057 2.256   1.00 22.36 ?  135 ASP   B HA   1 
ATOM   6380 H HB2  . ASP   B 1 135 ? 36.159 -36.626 3.122   1.00 24.51 ?  135 ASP   B HB2  1 
ATOM   6381 H HB3  . ASP   B 1 135 ? 35.497 -35.494 2.225   1.00 24.51 ?  135 ASP   B HB3  1 
ATOM   6382 N N    . PRO   B 1 136 ? 38.660 -34.767 0.120   1.00 17.36 ?  136 PRO   B N    1 
ATOM   6383 C CA   . PRO   B 1 136 ? 38.749 -33.955 -1.103  1.00 16.52 ?  136 PRO   B CA   1 
ATOM   6384 C C    . PRO   B 1 136 ? 37.555 -34.112 -2.023  1.00 15.60 ?  136 PRO   B C    1 
ATOM   6385 O O    . PRO   B 1 136 ? 37.232 -33.167 -2.752  1.00 14.73 ?  136 PRO   B O    1 
ATOM   6386 C CB   . PRO   B 1 136 ? 40.058 -34.427 -1.754  1.00 17.62 ?  136 PRO   B CB   1 
ATOM   6387 C CG   . PRO   B 1 136 ? 40.290 -35.798 -1.185  1.00 18.99 ?  136 PRO   B CG   1 
ATOM   6388 C CD   . PRO   B 1 136 ? 39.760 -35.741 0.215   1.00 18.52 ?  136 PRO   B CD   1 
ATOM   6389 H HA   . PRO   B 1 136 ? 38.830 -33.017 -0.880  1.00 19.98 ?  136 PRO   B HA   1 
ATOM   6390 H HB2  . PRO   B 1 136 ? 39.957 -34.465 -2.721  1.00 21.29 ?  136 PRO   B HB2  1 
ATOM   6391 H HB3  . PRO   B 1 136 ? 40.776 -33.822 -1.511  1.00 21.29 ?  136 PRO   B HB3  1 
ATOM   6392 H HG2  . PRO   B 1 136 ? 39.804 -36.457 -1.706  1.00 22.94 ?  136 PRO   B HG2  1 
ATOM   6393 H HG3  . PRO   B 1 136 ? 41.239 -35.996 -1.181  1.00 22.94 ?  136 PRO   B HG3  1 
ATOM   6394 H HD2  . PRO   B 1 136 ? 39.423 -36.608 0.484   1.00 22.37 ?  136 PRO   B HD2  1 
ATOM   6395 H HD3  . PRO   B 1 136 ? 40.438 -35.412 0.825   1.00 22.37 ?  136 PRO   B HD3  1 
ATOM   6396 N N    . ILE   B 1 137 ? 36.899 -35.277 -2.023  1.00 15.92 ?  137 ILE   B N    1 
ATOM   6397 C CA   . ILE   B 1 137 ? 35.674 -35.445 -2.803  1.00 16.48 ?  137 ILE   B CA   1 
ATOM   6398 C C    . ILE   B 1 137 ? 34.602 -34.469 -2.327  1.00 16.00 ?  137 ILE   B C    1 
ATOM   6399 O O    . ILE   B 1 137 ? 33.883 -33.862 -3.132  1.00 15.64 ?  137 ILE   B O    1 
ATOM   6400 C CB   . ILE   B 1 137 ? 35.197 -36.912 -2.737  1.00 18.63 ?  137 ILE   B CB   1 
ATOM   6401 C CG1  . ILE   B 1 137 ? 36.204 -37.822 -3.440  1.00 20.95 ?  137 ILE   B CG1  1 
ATOM   6402 C CG2  . ILE   B 1 137 ? 33.817 -37.072 -3.370  1.00 19.17 ?  137 ILE   B CG2  1 
ATOM   6403 C CD1  . ILE   B 1 137 ? 35.906 -39.308 -3.289  1.00 22.97 ?  137 ILE   B CD1  1 
ATOM   6404 H H    . ILE   B 1 137 ? 37.140 -35.977 -1.592  1.00 19.25 ?  137 ILE   B H    1 
ATOM   6405 H HA   . ILE   B 1 137 ? 35.861 -35.247 -3.736  1.00 19.92 ?  137 ILE   B HA   1 
ATOM   6406 H HB   . ILE   B 1 137 ? 35.138 -37.179 -1.810  1.00 22.51 ?  137 ILE   B HB   1 
ATOM   6407 H HG12 . ILE   B 1 137 ? 36.206 -37.625 -4.389  1.00 25.29 ?  137 ILE   B HG12 1 
ATOM   6408 H HG13 . ILE   B 1 137 ? 37.085 -37.667 -3.069  1.00 25.29 ?  137 ILE   B HG13 1 
ATOM   6409 H HG21 . ILE   B 1 137 ? 33.542 -38.002 -3.322  1.00 23.15 ?  137 ILE   B HG21 1 
ATOM   6410 H HG22 . ILE   B 1 137 ? 33.177 -36.530 -2.890  1.00 23.15 ?  137 ILE   B HG22 1 
ATOM   6411 H HG23 . ILE   B 1 137 ? 33.861 -36.792 -4.298  1.00 23.15 ?  137 ILE   B HG23 1 
ATOM   6412 H HD11 . ILE   B 1 137 ? 36.497 -39.796 -3.879  1.00 27.72 ?  137 ILE   B HD11 1 
ATOM   6413 H HD12 . ILE   B 1 137 ? 36.063 -39.571 -2.368  1.00 27.72 ?  137 ILE   B HD12 1 
ATOM   6414 H HD13 . ILE   B 1 137 ? 34.988 -39.490 -3.535  1.00 27.72 ?  137 ILE   B HD13 1 
ATOM   6415 N N    . HIS   B 1 138 ? 34.469 -34.316 -1.013  1.00 16.26 ?  138 HIS   B N    1 
ATOM   6416 C CA   . HIS   B 1 138 ? 33.522 -33.346 -0.480  1.00 16.60 ?  138 HIS   B CA   1 
ATOM   6417 C C    . HIS   B 1 138 ? 33.944 -31.920 -0.800  1.00 15.75 ?  138 HIS   B C    1 
ATOM   6418 O O    . HIS   B 1 138 ? 33.097 -31.073 -1.103  1.00 16.41 ?  138 HIS   B O    1 
ATOM   6419 C CB   . HIS   B 1 138 ? 33.393 -33.521 1.025   1.00 18.27 ?  138 HIS   B CB   1 
ATOM   6420 C CG   . HIS   B 1 138 ? 32.462 -32.538 1.652   1.00 19.72 ?  138 HIS   B CG   1 
ATOM   6421 N ND1  . HIS   B 1 138 ? 31.122 -32.479 1.337   1.00 21.15 ?  138 HIS   B ND1  1 
ATOM   6422 C CD2  . HIS   B 1 138 ? 32.681 -31.549 2.550   1.00 20.17 ?  138 HIS   B CD2  1 
ATOM   6423 C CE1  . HIS   B 1 138 ? 30.550 -31.511 2.029   1.00 21.11 ?  138 HIS   B CE1  1 
ATOM   6424 N NE2  . HIS   B 1 138 ? 31.473 -30.933 2.777   1.00 20.40 ?  138 HIS   B NE2  1 
ATOM   6425 H H    . HIS   B 1 138 ? 34.904 -34.760 -0.423  1.00 19.67 ?  138 HIS   B H    1 
ATOM   6426 H HA   . HIS   B 1 138 ? 32.654 -33.500 -0.881  1.00 20.07 ?  138 HIS   B HA   1 
ATOM   6427 H HB2  . HIS   B 1 138 ? 33.053 -34.411 1.209   1.00 22.07 ?  138 HIS   B HB2  1 
ATOM   6428 H HB3  . HIS   B 1 138 ? 34.263 -33.408 1.432   1.00 22.07 ?  138 HIS   B HB3  1 
ATOM   6429 H HD1  . HIS   B 1 138 ? 30.718 -33.005 0.784   1.00 25.53 ?  138 HIS   B HD1  1 
ATOM   6430 H HD2  . HIS   B 1 138 ? 33.486 -31.337 2.953   1.00 24.35 ?  138 HIS   B HD2  1 
ATOM   6431 H HE1  . HIS   B 1 138 ? 29.644 -31.287 1.999   1.00 25.48 ?  138 HIS   B HE1  1 
ATOM   6432 N N    . SER   B 1 139 ? 35.240 -31.624 -0.719  1.00 15.26 ?  139 SER   B N    1 
ATOM   6433 C CA   . SER   B 1 139 ? 35.688 -30.280 -1.049  1.00 14.23 ?  139 SER   B CA   1 
ATOM   6434 C C    . SER   B 1 139 ? 35.345 -29.933 -2.489  1.00 13.22 ?  139 SER   B C    1 
ATOM   6435 O O    . SER   B 1 139 ? 34.904 -28.817 -2.775  1.00 13.53 ?  139 SER   B O    1 
ATOM   6436 C CB   . SER   B 1 139 ? 37.185 -30.143 -0.792  1.00 14.49 ?  139 SER   B CB   1 
ATOM   6437 O OG   . SER   B 1 139 ? 37.597 -28.809 -1.048  1.00 14.59 ?  139 SER   B OG   1 
ATOM   6438 H H    . SER   B 1 139 ? 35.864 -32.166 -0.485  1.00 18.47 ?  139 SER   B H    1 
ATOM   6439 H HA   . SER   B 1 139 ? 35.226 -29.646 -0.479  1.00 17.22 ?  139 SER   B HA   1 
ATOM   6440 H HB2  . SER   B 1 139 ? 37.372 -30.367 0.132   1.00 17.54 ?  139 SER   B HB2  1 
ATOM   6441 H HB3  . SER   B 1 139 ? 37.670 -30.729 -1.388  1.00 17.54 ?  139 SER   B HB3  1 
ATOM   6442 H HG   . SER   B 1 139 ? 38.419 -28.719 -0.888  1.00 17.65 ?  139 SER   B HG   1 
ATOM   6443 N N    . LEU   B 1 140 ? 35.535 -30.877 -3.410  1.00 13.31 ?  140 LEU   B N    1 
ATOM   6444 C CA   . LEU   B 1 140 ? 35.175 -30.630 -4.800  1.00 13.35 ?  140 LEU   B CA   1 
ATOM   6445 C C    . LEU   B 1 140 ? 33.673 -30.393 -4.938  1.00 13.73 ?  140 LEU   B C    1 
ATOM   6446 O O    . LEU   B 1 140 ? 33.241 -29.510 -5.686  1.00 13.48 ?  140 LEU   B O    1 
ATOM   6447 C CB   . LEU   B 1 140 ? 35.644 -31.796 -5.672  1.00 13.67 ?  140 LEU   B CB   1 
ATOM   6448 C CG   . LEU   B 1 140 ? 35.295 -31.691 -7.149  1.00 13.85 ?  140 LEU   B CG   1 
ATOM   6449 C CD1  . LEU   B 1 140 ? 35.880 -30.428 -7.748  1.00 14.68 ?  140 LEU   B CD1  1 
ATOM   6450 C CD2  . LEU   B 1 140 ? 35.762 -32.926 -7.906  1.00 14.92 ?  140 LEU   B CD2  1 
ATOM   6451 H H    . LEU   B 1 140 ? 35.863 -31.653 -3.260  1.00 16.13 ?  140 LEU   B H    1 
ATOM   6452 H HA   . LEU   B 1 140 ? 35.634 -29.829 -5.106  1.00 16.17 ?  140 LEU   B HA   1 
ATOM   6453 H HB2  . LEU   B 1 140 ? 36.610 -31.864 -5.604  1.00 16.56 ?  140 LEU   B HB2  1 
ATOM   6454 H HB3  . LEU   B 1 140 ? 35.238 -32.610 -5.337  1.00 16.56 ?  140 LEU   B HB3  1 
ATOM   6455 H HG   . LEU   B 1 140 ? 34.334 -31.634 -7.239  1.00 16.77 ?  140 LEU   B HG   1 
ATOM   6456 H HD11 . LEU   B 1 140 ? 35.768 -30.460 -8.710  1.00 17.77 ?  140 LEU   B HD11 1 
ATOM   6457 H HD12 . LEU   B 1 140 ? 35.410 -29.660 -7.386  1.00 17.77 ?  140 LEU   B HD12 1 
ATOM   6458 H HD13 . LEU   B 1 140 ? 36.821 -30.379 -7.523  1.00 17.77 ?  140 LEU   B HD13 1 
ATOM   6459 H HD21 . LEU   B 1 140 ? 35.520 -32.826 -8.842  1.00 18.06 ?  140 LEU   B HD21 1 
ATOM   6460 H HD22 . LEU   B 1 140 ? 36.719 -33.010 -7.815  1.00 18.06 ?  140 LEU   B HD22 1 
ATOM   6461 H HD23 . LEU   B 1 140 ? 35.317 -33.703 -7.532  1.00 18.06 ?  140 LEU   B HD23 1 
ATOM   6462 N N    . ARG   B 1 141 ? 32.865 -31.186 -4.229  1.00 14.31 ?  141 ARG   B N    1 
ATOM   6463 C CA   . ARG   B 1 141 ? 31.415 -31.005 -4.217  1.00 15.18 ?  141 ARG   B CA   1 
ATOM   6464 C C    . ARG   B 1 141 ? 31.041 -29.592 -3.785  1.00 14.54 ?  141 ARG   B C    1 
ATOM   6465 O O    . ARG   B 1 141 ? 30.239 -28.910 -4.443  1.00 14.80 ?  141 ARG   B O    1 
ATOM   6466 C CB   . ARG   B 1 141 ? 30.811 -32.046 -3.264  1.00 16.62 ?  141 ARG   B CB   1 
ATOM   6467 C CG   . ARG   B 1 141 ? 29.350 -31.900 -2.939  1.00 18.69 ?  141 ARG   B CG   1 
ATOM   6468 C CD   . ARG   B 1 141 ? 28.537 -32.534 -4.002  1.00 20.70 ?  141 ARG   B CD   1 
ATOM   6469 N NE   . ARG   B 1 141 ? 28.280 -31.624 -5.106  1.00 21.22 ?  141 ARG   B NE   1 
ATOM   6470 C CZ   . ARG   B 1 141 ? 28.256 -31.973 -6.385  1.00 20.47 ?  141 ARG   B CZ   1 
ATOM   6471 N NH1  . ARG   B 1 141 ? 28.674 -33.163 -6.788  1.00 20.37 ?  141 ARG   B NH1  1 
ATOM   6472 N NH2  . ARG   B 1 141 ? 27.804 -31.103 -7.284  1.00 21.15 ?  141 ARG   B NH2  1 
ATOM   6473 H H    . ARG   B 1 141 ? 33.141 -31.835 -3.740  1.00 17.32 ?  141 ARG   B H    1 
ATOM   6474 H HA   . ARG   B 1 141 ? 31.064 -31.152 -5.102  1.00 18.37 ?  141 ARG   B HA   1 
ATOM   6475 H HB2  . ARG   B 1 141 ? 30.946 -32.923 -3.658  1.00 20.09 ?  141 ARG   B HB2  1 
ATOM   6476 H HB3  . ARG   B 1 141 ? 31.296 -32.002 -2.426  1.00 20.09 ?  141 ARG   B HB3  1 
ATOM   6477 H HG2  . ARG   B 1 141 ? 29.167 -32.341 -2.099  1.00 22.58 ?  141 ARG   B HG2  1 
ATOM   6478 H HG3  . ARG   B 1 141 ? 29.109 -30.957 -2.881  1.00 22.58 ?  141 ARG   B HG3  1 
ATOM   6479 H HD2  . ARG   B 1 141 ? 29.005 -33.315 -4.342  1.00 24.99 ?  141 ARG   B HD2  1 
ATOM   6480 H HD3  . ARG   B 1 141 ? 27.690 -32.803 -3.625  1.00 24.99 ?  141 ARG   B HD3  1 
ATOM   6481 H HE   . ARG   B 1 141 ? 28.111 -30.801 -4.913  1.00 25.62 ?  141 ARG   B HE   1 
ATOM   6482 H HH11 . ARG   B 1 141 ? 28.954 -33.742 -6.219  1.00 24.60 ?  141 ARG   B HH11 1 
ATOM   6483 H HH12 . ARG   B 1 141 ? 28.653 -33.360 -7.623  1.00 24.60 ?  141 ARG   B HH12 1 
ATOM   6484 H HH21 . ARG   B 1 141 ? 27.536 -30.320 -7.034  1.00 25.54 ?  141 ARG   B HH21 1 
ATOM   6485 H HH22 . ARG   B 1 141 ? 27.800 -31.306 -8.120  1.00 25.54 ?  141 ARG   B HH22 1 
ATOM   6486 N N    . VAL   B 1 142 ? 31.590 -29.142 -2.658  1.00 14.30 ?  142 VAL   B N    1 
ATOM   6487 C CA   . VAL   B 1 142 ? 31.258 -27.807 -2.177  1.00 13.89 ?  142 VAL   B CA   1 
ATOM   6488 C C    . VAL   B 1 142 ? 31.736 -26.754 -3.169  1.00 13.43 ?  142 VAL   B C    1 
ATOM   6489 O O    . VAL   B 1 142 ? 31.040 -25.766 -3.434  1.00 13.89 ?  142 VAL   B O    1 
ATOM   6490 C CB   . VAL   B 1 142 ? 31.812 -27.584 -0.757  1.00 14.46 ?  142 VAL   B CB   1 
ATOM   6491 C CG1  . VAL   B 1 142 ? 31.497 -26.172 -0.266  1.00 14.66 ?  142 VAL   B CG1  1 
ATOM   6492 C CG2  . VAL   B 1 142 ? 31.249 -28.617 0.197   1.00 15.38 ?  142 VAL   B CG2  1 
ATOM   6493 H H    . VAL   B 1 142 ? 32.141 -29.577 -2.164  1.00 17.31 ?  142 VAL   B H    1 
ATOM   6494 H HA   . VAL   B 1 142 ? 30.296 -27.728 -2.116  1.00 16.82 ?  142 VAL   B HA   1 
ATOM   6495 H HB   . VAL   B 1 142 ? 32.779 -27.684 -0.770  1.00 17.50 ?  142 VAL   B HB   1 
ATOM   6496 H HG11 . VAL   B 1 142 ? 31.703 -26.114 0.682   1.00 17.74 ?  142 VAL   B HG11 1 
ATOM   6497 H HG12 . VAL   B 1 142 ? 32.040 -25.536 -0.758  1.00 17.74 ?  142 VAL   B HG12 1 
ATOM   6498 H HG13 . VAL   B 1 142 ? 30.557 -25.992 -0.411  1.00 17.74 ?  142 VAL   B HG13 1 
ATOM   6499 H HG21 . VAL   B 1 142 ? 31.568 -28.430 1.093   1.00 18.60 ?  142 VAL   B HG21 1 
ATOM   6500 H HG22 . VAL   B 1 142 ? 30.282 -28.575 0.171   1.00 18.60 ?  142 VAL   B HG22 1 
ATOM   6501 H HG23 . VAL   B 1 142 ? 31.549 -29.499 -0.081  1.00 18.60 ?  142 VAL   B HG23 1 
ATOM   6502 N N    . CYS   B 1 143 ? 32.918 -26.957 -3.752  1.00 13.16 ?  143 CYS   B N    1 
ATOM   6503 C CA   . CYS   B 1 143 ? 33.419 -26.023 -4.756  1.00 13.08 ?  143 CYS   B CA   1 
ATOM   6504 C C    . CYS   B 1 143 ? 32.417 -25.878 -5.898  1.00 13.37 ?  143 CYS   B C    1 
ATOM   6505 O O    . CYS   B 1 143 ? 32.008 -24.765 -6.250  1.00 13.42 ?  143 CYS   B O    1 
ATOM   6506 C CB   . CYS   B 1 143 ? 34.772 -26.518 -5.281  1.00 13.07 ?  143 CYS   B CB   1 
ATOM   6507 S SG   . CYS   B 1 143 ? 35.526 -25.416 -6.499  1.00 13.38 ?  143 CYS   B SG   1 
ATOM   6508 H H    . CYS   B 1 143 ? 33.442 -27.613 -3.583  1.00 15.94 ?  143 CYS   B H    1 
ATOM   6509 H HA   . CYS   B 1 143 ? 33.552 -25.148 -4.352  1.00 15.85 ?  143 CYS   B HA   1 
ATOM   6510 H HB2  . CYS   B 1 143 ? 35.390 -26.601 -4.540  1.00 15.84 ?  143 CYS   B HB2  1 
ATOM   6511 H HB3  . CYS   B 1 143 ? 34.646 -27.376 -5.703  1.00 15.84 ?  143 CYS   B HB3  1 
ATOM   6512 H HG   . CYS   B 1 143 ? 36.586 -25.860 -6.824  1.00 16.21 ?  143 CYS   B HG   1 
ATOM   6513 N N    . VAL   B 1 144 ? 32.012 -27.000 -6.493  1.00 13.86 ?  144 VAL   B N    1 
ATOM   6514 C CA   . VAL   B 1 144 ? 31.102 -26.944 -7.631  1.00 14.90 ?  144 VAL   B CA   1 
ATOM   6515 C C    . VAL   B 1 144 ? 29.762 -26.328 -7.255  1.00 14.79 ?  144 VAL   B C    1 
ATOM   6516 O O    . VAL   B 1 144 ? 29.147 -25.626 -8.067  1.00 16.20 ?  144 VAL   B O    1 
ATOM   6517 C CB   . VAL   B 1 144 ? 30.941 -28.360 -8.192  1.00 17.34 ?  144 VAL   B CB   1 
ATOM   6518 C CG1  . VAL   B 1 144 ? 29.656 -28.498 -9.011  1.00 19.47 ?  144 VAL   B CG1  1 
ATOM   6519 C CG2  . VAL   B 1 144 ? 32.173 -28.766 -8.994  1.00 17.53 ?  144 VAL   B CG2  1 
ATOM   6520 H H    . VAL   B 1 144 ? 32.245 -27.792 -6.259  1.00 16.79 ?  144 VAL   B H    1 
ATOM   6521 H HA   . VAL   B 1 144 ? 31.489 -26.398 -8.327  1.00 18.04 ?  144 VAL   B HA   1 
ATOM   6522 H HB   . VAL   B 1 144 ? 30.868 -28.983 -7.449  1.00 20.96 ?  144 VAL   B HB   1 
ATOM   6523 H HG11 . VAL   B 1 144 ? 29.723 -29.295 -9.568  1.00 23.52 ?  144 VAL   B HG11 1 
ATOM   6524 H HG12 . VAL   B 1 144 ? 28.901 -28.589 -8.409  1.00 23.52 ?  144 VAL   B HG12 1 
ATOM   6525 H HG13 . VAL   B 1 144 ? 29.551 -27.718 -9.571  1.00 23.52 ?  144 VAL   B HG13 1 
ATOM   6526 H HG21 . VAL   B 1 144 ? 32.047 -29.671 -9.333  1.00 21.19 ?  144 VAL   B HG21 1 
ATOM   6527 H HG22 . VAL   B 1 144 ? 32.280 -28.152 -9.737  1.00 21.19 ?  144 VAL   B HG22 1 
ATOM   6528 H HG23 . VAL   B 1 144 ? 32.948 -28.734 -8.419  1.00 21.19 ?  144 VAL   B HG23 1 
ATOM   6529 N N    . ASP   B 1 145 ? 29.294 -26.564 -6.032  1.00 14.80 ?  145 ASP   B N    1 
ATOM   6530 C CA   . ASP   B 1 145 ? 27.987 -26.089 -5.594  1.00 15.94 ?  145 ASP   B CA   1 
ATOM   6531 C C    . ASP   B 1 145 ? 28.017 -24.665 -5.055  1.00 15.44 ?  145 ASP   B C    1 
ATOM   6532 O O    . ASP   B 1 145 ? 26.961 -24.127 -4.704  1.00 17.18 ?  145 ASP   B O    1 
ATOM   6533 C CB   . ASP   B 1 145 ? 27.411 -27.008 -4.507  1.00 17.70 ?  145 ASP   B CB   1 
ATOM   6534 C CG   . ASP   B 1 145 ? 27.028 -28.383 -5.021  1.00 19.69 ?  145 ASP   B CG   1 
ATOM   6535 O OD1  . ASP   B 1 145 ? 26.913 -28.567 -6.249  1.00 19.75 ?  145 ASP   B OD1  1 
ATOM   6536 O OD2  . ASP   B 1 145 ? 26.837 -29.276 -4.172  1.00 21.65 -1 145 ASP   B OD2  1 
ATOM   6537 H H    . ASP   B 1 145 ? 29.732 -26.983 -5.427  1.00 17.92 ?  145 ASP   B H    1 
ATOM   6538 H HA   . ASP   B 1 145 ? 27.385 -26.095 -6.350  1.00 19.27 ?  145 ASP   B HA   1 
ATOM   6539 H HB2  . ASP   B 1 145 ? 28.072 -27.130 -3.813  1.00 21.39 ?  145 ASP   B HB2  1 
ATOM   6540 H HB3  . ASP   B 1 145 ? 26.613 -26.595 -4.141  1.00 21.39 ?  145 ASP   B HB3  1 
ATOM   6541 N N    . THR   B 1 146 ? 29.188 -24.048 -4.969  1.00 13.74 ?  146 THR   B N    1 
ATOM   6542 C CA   . THR   B 1 146 ? 29.331 -22.730 -4.362  1.00 13.35 ?  146 THR   B CA   1 
ATOM   6543 C C    . THR   B 1 146 ? 29.970 -21.708 -5.281  1.00 12.76 ?  146 THR   B C    1 
ATOM   6544 O O    . THR   B 1 146 ? 29.514 -20.550 -5.333  1.00 13.03 ?  146 THR   B O    1 
ATOM   6545 C CB   . THR   B 1 146 ? 30.159 -22.836 -3.077  1.00 13.38 ?  146 THR   B CB   1 
ATOM   6546 O OG1  . THR   B 1 146 ? 29.583 -23.824 -2.220  1.00 13.71 ?  146 THR   B OG1  1 
ATOM   6547 C CG2  . THR   B 1 146 ? 30.225 -21.491 -2.354  1.00 13.93 ?  146 THR   B CG2  1 
ATOM   6548 H H    . THR   B 1 146 ? 29.930 -24.369 -5.265  1.00 16.64 ?  146 THR   B H    1 
ATOM   6549 H HA   . THR   B 1 146 ? 28.460 -22.393 -4.122  1.00 16.17 ?  146 THR   B HA   1 
ATOM   6550 H HB   . THR   B 1 146 ? 31.068 -23.090 -3.301  1.00 16.21 ?  146 THR   B HB   1 
ATOM   6551 H HG1  . THR   B 1 146 ? 29.618 -24.582 -2.595  1.00 16.60 ?  146 THR   B HG1  1 
ATOM   6552 H HG21 . THR   B 1 146 ? 30.576 -21.609 -1.460  1.00 16.87 ?  146 THR   B HG21 1 
ATOM   6553 H HG22 . THR   B 1 146 ? 30.799 -20.875 -2.839  1.00 16.87 ?  146 THR   B HG22 1 
ATOM   6554 H HG23 . THR   B 1 146 ? 29.334 -21.105 -2.292  1.00 16.87 ?  146 THR   B HG23 1 
ATOM   6555 N N    . VAL   B 1 147 ? 31.037 -22.088 -5.976  1.00 12.69 ?  147 VAL   B N    1 
ATOM   6556 C CA   . VAL   B 1 147 ? 31.758 -21.149 -6.818  1.00 12.59 ?  147 VAL   B CA   1 
ATOM   6557 C C    . VAL   B 1 147 ? 31.026 -21.012 -8.142  1.00 12.92 ?  147 VAL   B C    1 
ATOM   6558 O O    . VAL   B 1 147 ? 30.654 -22.012 -8.771  1.00 13.82 ?  147 VAL   B O    1 
ATOM   6559 C CB   . VAL   B 1 147 ? 33.213 -21.598 -7.015  1.00 12.28 ?  147 VAL   B CB   1 
ATOM   6560 C CG1  . VAL   B 1 147 ? 33.973 -20.576 -7.838  1.00 12.51 ?  147 VAL   B CG1  1 
ATOM   6561 C CG2  . VAL   B 1 147 ? 33.884 -21.808 -5.673  1.00 12.71 ?  147 VAL   B CG2  1 
ATOM   6562 H H    . VAL   B 1 147 ? 31.361 -22.888 -5.981  1.00 15.38 ?  147 VAL   B H    1 
ATOM   6563 H HA   . VAL   B 1 147 ? 31.770 -20.280 -6.384  1.00 15.26 ?  147 VAL   B HA   1 
ATOM   6564 H HB   . VAL   B 1 147 ? 33.225 -22.441 -7.498  1.00 14.88 ?  147 VAL   B HB   1 
ATOM   6565 H HG11 . VAL   B 1 147 ? 34.915 -20.797 -7.824  1.00 15.16 ?  147 VAL   B HG11 1 
ATOM   6566 H HG12 . VAL   B 1 147 ? 33.643 -20.595 -8.751  1.00 15.16 ?  147 VAL   B HG12 1 
ATOM   6567 H HG13 . VAL   B 1 147 ? 33.832 -19.697 -7.454  1.00 15.16 ?  147 VAL   B HG13 1 
ATOM   6568 H HG21 . VAL   B 1 147 ? 34.825 -21.987 -5.813  1.00 15.40 ?  147 VAL   B HG21 1 
ATOM   6569 H HG22 . VAL   B 1 147 ? 33.772 -21.009 -5.137  1.00 15.40 ?  147 VAL   B HG22 1 
ATOM   6570 H HG23 . VAL   B 1 147 ? 33.466 -22.565 -5.228  1.00 15.40 ?  147 VAL   B HG23 1 
ATOM   6571 N N    . ARG   B 1 148 ? 30.819 -19.761 -8.562  1.00 12.74 ?  148 ARG   B N    1 
ATOM   6572 C CA   . ARG   B 1 148 ? 30.197 -19.436 -9.836  1.00 12.72 ?  148 ARG   B CA   1 
ATOM   6573 C C    . ARG   B 1 148 ? 31.154 -18.759 -10.805 1.00 12.33 ?  148 ARG   B C    1 
ATOM   6574 O O    . ARG   B 1 148 ? 30.872 -18.740 -12.006 1.00 14.02 ?  148 ARG   B O    1 
ATOM   6575 C CB   . ARG   B 1 148 ? 28.960 -18.549 -9.616  1.00 13.29 ?  148 ARG   B CB   1 
ATOM   6576 C CG   . ARG   B 1 148 ? 27.887 -19.260 -8.804  1.00 14.14 ?  148 ARG   B CG   1 
ATOM   6577 C CD   . ARG   B 1 148 ? 26.678 -18.385 -8.505  1.00 15.25 ?  148 ARG   B CD   1 
ATOM   6578 N NE   . ARG   B 1 148 ? 27.054 -17.175 -7.781  1.00 15.35 ?  148 ARG   B NE   1 
ATOM   6579 C CZ   . ARG   B 1 148 ? 27.368 -17.133 -6.493  1.00 14.36 ?  148 ARG   B CZ   1 
ATOM   6580 N NH1  . ARG   B 1 148 ? 27.322 -18.217 -5.732  1.00 14.48 ?  148 ARG   B NH1  1 
ATOM   6581 N NH2  . ARG   B 1 148 ? 27.762 -15.978 -5.960  1.00 14.38 ?  148 ARG   B NH2  1 
ATOM   6582 H H    . ARG   B 1 148 ? 31.042 -19.062 -8.106  1.00 15.44 ?  148 ARG   B H    1 
ATOM   6583 H HA   . ARG   B 1 148 ? 29.899 -20.260 -10.251 1.00 15.41 ?  148 ARG   B HA   1 
ATOM   6584 H HB2  . ARG   B 1 148 ? 29.224 -17.751 -9.136  1.00 16.10 ?  148 ARG   B HB2  1 
ATOM   6585 H HB3  . ARG   B 1 148 ? 28.583 -18.315 -10.478 1.00 16.10 ?  148 ARG   B HB3  1 
ATOM   6586 H HG2  . ARG   B 1 148 ? 27.579 -20.036 -9.303  1.00 17.12 ?  148 ARG   B HG2  1 
ATOM   6587 H HG3  . ARG   B 1 148 ? 28.267 -19.544 -7.960  1.00 17.12 ?  148 ARG   B HG3  1 
ATOM   6588 H HD2  . ARG   B 1 148 ? 26.258 -18.122 -9.340  1.00 18.46 ?  148 ARG   B HD2  1 
ATOM   6589 H HD3  . ARG   B 1 148 ? 26.048 -18.884 -7.959  1.00 18.46 ?  148 ARG   B HD3  1 
ATOM   6590 H HE   . ARG   B 1 148 ? 27.070 -16.437 -8.220  1.00 18.58 ?  148 ARG   B HE   1 
ATOM   6591 H HH11 . ARG   B 1 148 ? 27.074 -18.970 -6.065  1.00 17.52 ?  148 ARG   B HH11 1 
ATOM   6592 H HH12 . ARG   B 1 148 ? 27.533 -18.166 -4.899  1.00 17.52 ?  148 ARG   B HH12 1 
ATOM   6593 H HH21 . ARG   B 1 148 ? 27.799 -15.269 -6.447  1.00 17.41 ?  148 ARG   B HH21 1 
ATOM   6594 H HH22 . ARG   B 1 148 ? 27.970 -15.936 -5.127  1.00 17.41 ?  148 ARG   B HH22 1 
ATOM   6595 N N    . THR   B 1 149 ? 32.265 -18.212 -10.318 1.00 12.55 ?  149 THR   B N    1 
ATOM   6596 C CA   . THR   B 1 149 ? 33.307 -17.658 -11.165 1.00 12.49 ?  149 THR   B CA   1 
ATOM   6597 C C    . THR   B 1 149 ? 34.186 -18.797 -11.682 1.00 12.36 ?  149 THR   B C    1 
ATOM   6598 O O    . THR   B 1 149 ? 33.988 -19.967 -11.346 1.00 12.77 ?  149 THR   B O    1 
ATOM   6599 C CB   . THR   B 1 149 ? 34.074 -16.604 -10.381 1.00 12.90 ?  149 THR   B CB   1 
ATOM   6600 O OG1  . THR   B 1 149 ? 34.528 -17.208 -9.170  1.00 12.69 ?  149 THR   B OG1  1 
ATOM   6601 C CG2  . THR   B 1 149 ? 33.189 -15.394 -10.074 1.00 13.93 ?  149 THR   B CG2  1 
ATOM   6602 H H    . THR   B 1 149 ? 32.426 -18.136 -9.474  1.00 15.21 ?  149 THR   B H    1 
ATOM   6603 H HA   . THR   B 1 149 ? 32.896 -17.216 -11.925 1.00 15.14 ?  149 THR   B HA   1 
ATOM   6604 H HB   . THR   B 1 149 ? 34.834 -16.313 -10.893 1.00 15.63 ?  149 THR   B HB   1 
ATOM   6605 H HG1  . THR   B 1 149 ? 34.958 -16.644 -8.704  1.00 15.38 ?  149 THR   B HG1  1 
ATOM   6606 H HG21 . THR   B 1 149 ? 33.698 -14.727 -9.584  1.00 16.87 ?  149 THR   B HG21 1 
ATOM   6607 H HG22 . THR   B 1 149 ? 32.871 -15.001 -10.900 1.00 16.87 ?  149 THR   B HG22 1 
ATOM   6608 H HG23 . THR   B 1 149 ? 32.426 -15.661 -9.537  1.00 16.87 ?  149 THR   B HG23 1 
ATOM   6609 N N    . ASN   B 1 150 ? 35.145 -18.472 -12.538 1.00 11.93 ?  150 ASN   B N    1 
ATOM   6610 C CA   . ASN   B 1 150 ? 35.916 -19.492 -13.237 1.00 12.78 ?  150 ASN   B CA   1 
ATOM   6611 C C    . ASN   B 1 150 ? 37.077 -19.942 -12.364 1.00 12.20 ?  150 ASN   B C    1 
ATOM   6612 O O    . ASN   B 1 150 ? 38.019 -19.183 -12.130 1.00 12.81 ?  150 ASN   B O    1 
ATOM   6613 C CB   . ASN   B 1 150 ? 36.392 -18.961 -14.580 1.00 14.51 ?  150 ASN   B CB   1 
ATOM   6614 C CG   . ASN   B 1 150 ? 35.254 -18.742 -15.536 1.00 17.29 ?  150 ASN   B CG   1 
ATOM   6615 O OD1  . ASN   B 1 150 ? 34.355 -19.573 -15.635 1.00 18.59 ?  150 ASN   B OD1  1 
ATOM   6616 N ND2  . ASN   B 1 150 ? 35.265 -17.616 -16.227 1.00 19.48 ?  150 ASN   B ND2  1 
ATOM   6617 H H    . ASN   B 1 150 ? 35.367 -17.663 -12.727 1.00 14.46 ?  150 ASN   B H    1 
ATOM   6618 H HA   . ASN   B 1 150 ? 35.339 -20.262 -13.396 1.00 15.49 ?  150 ASN   B HA   1 
ATOM   6619 H HB2  . ASN   B 1 150 ? 36.838 -18.110 -14.437 1.00 17.56 ?  150 ASN   B HB2  1 
ATOM   6620 H HB3  . ASN   B 1 150 ? 37.002 -19.600 -14.970 1.00 17.56 ?  150 ASN   B HB3  1 
ATOM   6621 H HD21 . ASN   B 1 150 ? 34.636 -17.446 -16.792 1.00 23.53 ?  150 ASN   B HD21 1 
ATOM   6622 H HD22 . ASN   B 1 150 ? 35.909 -17.051 -16.126 1.00 23.53 ?  150 ASN   B HD22 1 
ATOM   6623 N N    . VAL   B 1 151 ? 37.021 -21.184 -11.891 1.00 11.95 ?  151 VAL   B N    1 
ATOM   6624 C CA   . VAL   B 1 151 ? 38.039 -21.718 -10.998 1.00 12.11 ?  151 VAL   B CA   1 
ATOM   6625 C C    . VAL   B 1 151 ? 38.737 -22.891 -11.674 1.00 11.93 ?  151 VAL   B C    1 
ATOM   6626 O O    . VAL   B 1 151 ? 38.088 -23.825 -12.171 1.00 13.12 ?  151 VAL   B O    1 
ATOM   6627 C CB   . VAL   B 1 151 ? 37.481 -22.060 -9.601  1.00 13.06 ?  151 VAL   B CB   1 
ATOM   6628 C CG1  . VAL   B 1 151 ? 36.334 -23.067 -9.670  1.00 14.39 ?  151 VAL   B CG1  1 
ATOM   6629 C CG2  . VAL   B 1 151 ? 38.600 -22.546 -8.679  1.00 13.28 ?  151 VAL   B CG2  1 
ATOM   6630 H H    . VAL   B 1 151 ? 36.390 -21.744 -12.065 1.00 14.50 ?  151 VAL   B H    1 
ATOM   6631 H HA   . VAL   B 1 151 ? 38.709 -21.024 -10.858 1.00 14.68 ?  151 VAL   B HA   1 
ATOM   6632 H HB   . VAL   B 1 151 ? 37.124 -21.249 -9.201  1.00 15.83 ?  151 VAL   B HB   1 
ATOM   6633 H HG11 . VAL   B 1 151 ? 36.012 -23.246 -8.769  1.00 17.42 ?  151 VAL   B HG11 1 
ATOM   6634 H HG12 . VAL   B 1 151 ? 35.620 -22.697 -10.207 1.00 17.42 ?  151 VAL   B HG12 1 
ATOM   6635 H HG13 . VAL   B 1 151 ? 36.660 -23.891 -10.069 1.00 17.42 ?  151 VAL   B HG13 1 
ATOM   6636 H HG21 . VAL   B 1 151 ? 38.250 -22.629 -7.775  1.00 16.09 ?  151 VAL   B HG21 1 
ATOM   6637 H HG22 . VAL   B 1 151 ? 38.916 -23.407 -8.989  1.00 16.09 ?  151 VAL   B HG22 1 
ATOM   6638 H HG23 . VAL   B 1 151 ? 39.323 -21.899 -8.691  1.00 16.09 ?  151 VAL   B HG23 1 
ATOM   6639 N N    . TYR   B 1 152 ? 40.073 -22.810 -11.698 1.00 11.62 ?  152 TYR   B N    1 
ATOM   6640 C CA   . TYR   B 1 152 ? 40.969 -23.798 -12.277 1.00 11.91 ?  152 TYR   B CA   1 
ATOM   6641 C C    . TYR   B 1 152 ? 41.695 -24.477 -11.120 1.00 11.07 ?  152 TYR   B C    1 
ATOM   6642 O O    . TYR   B 1 152 ? 42.551 -23.865 -10.469 1.00 11.60 ?  152 TYR   B O    1 
ATOM   6643 C CB   . TYR   B 1 152 ? 41.939 -23.099 -13.233 1.00 12.41 ?  152 TYR   B CB   1 
ATOM   6644 C CG   . TYR   B 1 152 ? 41.263 -22.634 -14.503 1.00 13.34 ?  152 TYR   B CG   1 
ATOM   6645 C CD1  . TYR   B 1 152 ? 40.609 -21.405 -14.573 1.00 13.71 ?  152 TYR   B CD1  1 
ATOM   6646 C CD2  . TYR   B 1 152 ? 41.255 -23.439 -15.628 1.00 14.62 ?  152 TYR   B CD2  1 
ATOM   6647 C CE1  . TYR   B 1 152 ? 39.970 -21.000 -15.730 1.00 15.52 ?  152 TYR   B CE1  1 
ATOM   6648 C CE2  . TYR   B 1 152 ? 40.620 -23.046 -16.787 1.00 15.56 ?  152 TYR   B CE2  1 
ATOM   6649 C CZ   . TYR   B 1 152 ? 39.986 -21.819 -16.837 1.00 16.09 ?  152 TYR   B CZ   1 
ATOM   6650 O OH   . TYR   B 1 152 ? 39.354 -21.431 -17.993 1.00 18.49 ?  152 TYR   B OH   1 
ATOM   6651 H H    . TYR   B 1 152 ? 40.508 -22.142 -11.354 1.00 14.09 ?  152 TYR   B H    1 
ATOM   6652 H HA   . TYR   B 1 152 ? 40.455 -24.464 -12.765 1.00 14.44 ?  152 TYR   B HA   1 
ATOM   6653 H HB2  . TYR   B 1 152 ? 42.313 -22.326 -12.786 1.00 15.04 ?  152 TYR   B HB2  1 
ATOM   6654 H HB3  . TYR   B 1 152 ? 42.645 -23.719 -13.472 1.00 15.04 ?  152 TYR   B HB3  1 
ATOM   6655 H HD1  . TYR   B 1 152 ? 40.594 -20.852 -13.826 1.00 16.60 ?  152 TYR   B HD1  1 
ATOM   6656 H HD2  . TYR   B 1 152 ? 41.674 -24.272 -15.598 1.00 17.70 ?  152 TYR   B HD2  1 
ATOM   6657 H HE1  . TYR   B 1 152 ? 39.541 -20.178 -15.765 1.00 18.77 ?  152 TYR   B HE1  1 
ATOM   6658 H HE2  . TYR   B 1 152 ? 40.626 -23.605 -17.535 1.00 18.82 ?  152 TYR   B HE2  1 
ATOM   6659 H HH   . TYR   B 1 152 ? 39.442 -22.023 -18.583 1.00 22.34 ?  152 TYR   B HH   1 
ATOM   6660 N N    . LEU   B 1 153 ? 41.315 -25.727 -10.848 1.00 11.29 ?  153 LEU   B N    1 
ATOM   6661 C CA   . LEU   B 1 153 ? 41.823 -26.479 -9.711  1.00 11.02 ?  153 LEU   B CA   1 
ATOM   6662 C C    . LEU   B 1 153 ? 43.050 -27.286 -10.104 1.00 11.43 ?  153 LEU   B C    1 
ATOM   6663 O O    . LEU   B 1 153 ? 43.026 -28.015 -11.099 1.00 12.74 ?  153 LEU   B O    1 
ATOM   6664 C CB   . LEU   B 1 153 ? 40.748 -27.436 -9.198  1.00 11.75 ?  153 LEU   B CB   1 
ATOM   6665 C CG   . LEU   B 1 153 ? 39.497 -26.786 -8.619  1.00 12.35 ?  153 LEU   B CG   1 
ATOM   6666 C CD1  . LEU   B 1 153 ? 38.416 -27.837 -8.460  1.00 13.45 ?  153 LEU   B CD1  1 
ATOM   6667 C CD2  . LEU   B 1 153 ? 39.795 -26.112 -7.287  1.00 12.69 ?  153 LEU   B CD2  1 
ATOM   6668 H H    . LEU   B 1 153 ? 40.748 -26.173 -11.325 1.00 13.69 ?  153 LEU   B H    1 
ATOM   6669 H HA   . LEU   B 1 153 ? 42.056 -25.867 -9.002  1.00 13.37 ?  153 LEU   B HA   1 
ATOM   6670 H HB2  . LEU   B 1 153 ? 40.466 -28.007 -9.929  1.00 14.25 ?  153 LEU   B HB2  1 
ATOM   6671 H HB3  . LEU   B 1 153 ? 41.137 -27.984 -8.495  1.00 14.25 ?  153 LEU   B HB3  1 
ATOM   6672 H HG   . LEU   B 1 153 ? 39.170 -26.106 -9.234  1.00 14.97 ?  153 LEU   B HG   1 
ATOM   6673 H HD11 . LEU   B 1 153 ? 37.616 -27.413 -8.109  1.00 16.30 ?  153 LEU   B HD11 1 
ATOM   6674 H HD12 . LEU   B 1 153 ? 38.233 -28.228 -9.325  1.00 16.30 ?  153 LEU   B HD12 1 
ATOM   6675 H HD13 . LEU   B 1 153 ? 38.731 -28.513 -7.843  1.00 16.30 ?  153 LEU   B HD13 1 
ATOM   6676 H HD21 . LEU   B 1 153 ? 38.976 -25.748 -6.923  1.00 15.38 ?  153 LEU   B HD21 1 
ATOM   6677 H HD22 . LEU   B 1 153 ? 40.163 -26.775 -6.679  1.00 15.38 ?  153 LEU   B HD22 1 
ATOM   6678 H HD23 . LEU   B 1 153 ? 40.441 -25.403 -7.431  1.00 15.38 ?  153 LEU   B HD23 1 
ATOM   6679 N N    . ALA   B 1 154 ? 44.100 -27.185 -9.293  1.00 11.69 ?  154 ALA   B N    1 
ATOM   6680 C CA   . ALA   B 1 154 ? 45.330 -27.943 -9.478  1.00 12.39 ?  154 ALA   B CA   1 
ATOM   6681 C C    . ALA   B 1 154 ? 45.401 -29.018 -8.403  1.00 12.89 ?  154 ALA   B C    1 
ATOM   6682 O O    . ALA   B 1 154 ? 45.337 -28.715 -7.204  1.00 14.30 ?  154 ALA   B O    1 
ATOM   6683 C CB   . ALA   B 1 154 ? 46.550 -27.028 -9.410  1.00 13.44 ?  154 ALA   B CB   1 
ATOM   6684 H H    . ALA   B 1 154 ? 44.121 -26.661 -8.601  1.00 14.18 ?  154 ALA   B H    1 
ATOM   6685 H HA   . ALA   B 1 154 ? 45.315 -28.369 -10.347 1.00 15.02 ?  154 ALA   B HA   1 
ATOM   6686 H HB1  . ALA   B 1 154 ? 47.349 -27.561 -9.540  1.00 16.28 ?  154 ALA   B HB1  1 
ATOM   6687 H HB2  . ALA   B 1 154 ? 46.482 -26.357 -10.108 1.00 16.28 ?  154 ALA   B HB2  1 
ATOM   6688 H HB3  . ALA   B 1 154 ? 46.575 -26.598 -8.540  1.00 16.28 ?  154 ALA   B HB3  1 
ATOM   6689 N N    . VAL   B 1 155 ? 45.502 -30.269 -8.836  1.00 12.43 ?  155 VAL   B N    1 
ATOM   6690 C CA   . VAL   B 1 155 ? 45.611 -31.417 -7.944  1.00 13.11 ?  155 VAL   B CA   1 
ATOM   6691 C C    . VAL   B 1 155 ? 46.946 -32.092 -8.228  1.00 13.21 ?  155 VAL   B C    1 
ATOM   6692 O O    . VAL   B 1 155 ? 47.177 -32.581 -9.341  1.00 15.15 ?  155 VAL   B O    1 
ATOM   6693 C CB   . VAL   B 1 155 ? 44.450 -32.407 -8.136  1.00 14.53 ?  155 VAL   B CB   1 
ATOM   6694 C CG1  . VAL   B 1 155 ? 44.628 -33.602 -7.212  1.00 14.57 ?  155 VAL   B CG1  1 
ATOM   6695 C CG2  . VAL   B 1 155 ? 43.112 -31.713 -7.891  1.00 15.83 ?  155 VAL   B CG2  1 
ATOM   6696 H H    . VAL   B 1 155 ? 45.521 -30.486 -9.671  1.00 15.07 ?  155 VAL   B H    1 
ATOM   6697 H HA   . VAL   B 1 155 ? 45.603 -31.116 -7.025  1.00 15.88 ?  155 VAL   B HA   1 
ATOM   6698 H HB   . VAL   B 1 155 ? 44.454 -32.731 -9.051  1.00 17.58 ?  155 VAL   B HB   1 
ATOM   6699 H HG11 . VAL   B 1 155 ? 43.796 -34.099 -7.173  1.00 17.64 ?  155 VAL   B HG11 1 
ATOM   6700 H HG12 . VAL   B 1 155 ? 45.335 -34.171 -7.558  1.00 17.64 ?  155 VAL   B HG12 1 
ATOM   6701 H HG13 . VAL   B 1 155 ? 44.863 -33.284 -6.326  1.00 17.64 ?  155 VAL   B HG13 1 
ATOM   6702 H HG21 . VAL   B 1 155 ? 42.396 -32.365 -7.976  1.00 19.15 ?  155 VAL   B HG21 1 
ATOM   6703 H HG22 . VAL   B 1 155 ? 43.110 -31.336 -6.997  1.00 19.15 ?  155 VAL   B HG22 1 
ATOM   6704 H HG23 . VAL   B 1 155 ? 42.994 -31.008 -8.547  1.00 19.15 ?  155 VAL   B HG23 1 
ATOM   6705 N N    . PHE   B 1 156 ? 47.816 -32.129 -7.217  1.00 13.57 ?  156 PHE   B N    1 
ATOM   6706 C CA   . PHE   B 1 156 ? 49.192 -32.589 -7.422  1.00 14.70 ?  156 PHE   B CA   1 
ATOM   6707 C C    . PHE   B 1 156 ? 49.285 -34.087 -7.708  1.00 16.07 ?  156 PHE   B C    1 
ATOM   6708 O O    . PHE   B 1 156 ? 50.011 -34.515 -8.616  1.00 18.02 ?  156 PHE   B O    1 
ATOM   6709 C CB   . PHE   B 1 156 ? 50.020 -32.233 -6.191  1.00 14.31 ?  156 PHE   B CB   1 
ATOM   6710 C CG   . PHE   B 1 156 ? 51.447 -32.693 -6.259  1.00 15.14 ?  156 PHE   B CG   1 
ATOM   6711 C CD1  . PHE   B 1 156 ? 52.325 -32.154 -7.184  1.00 16.61 ?  156 PHE   B CD1  1 
ATOM   6712 C CD2  . PHE   B 1 156 ? 51.917 -33.652 -5.384  1.00 15.85 ?  156 PHE   B CD2  1 
ATOM   6713 C CE1  . PHE   B 1 156 ? 53.650 -32.565 -7.236  1.00 17.55 ?  156 PHE   B CE1  1 
ATOM   6714 C CE2  . PHE   B 1 156 ? 53.236 -34.070 -5.432  1.00 17.05 ?  156 PHE   B CE2  1 
ATOM   6715 C CZ   . PHE   B 1 156 ? 54.096 -33.526 -6.362  1.00 17.29 ?  156 PHE   B CZ   1 
ATOM   6716 H H    . PHE   B 1 156 ? 47.632 -31.901 -6.405  1.00 16.44 ?  156 PHE   B H    1 
ATOM   6717 H HA   . PHE   B 1 156 ? 49.562 -32.116 -8.177  1.00 17.79 ?  156 PHE   B HA   1 
ATOM   6718 H HB2  . PHE   B 1 156 ? 50.028 -31.270 -6.091  1.00 17.33 ?  156 PHE   B HB2  1 
ATOM   6719 H HB3  . PHE   B 1 156 ? 49.617 -32.642 -5.410  1.00 17.33 ?  156 PHE   B HB3  1 
ATOM   6720 H HD1  . PHE   B 1 156 ? 52.025 -31.500 -7.775  1.00 20.08 ?  156 PHE   B HD1  1 
ATOM   6721 H HD2  . PHE   B 1 156 ? 51.340 -34.026 -4.757  1.00 19.17 ?  156 PHE   B HD2  1 
ATOM   6722 H HE1  . PHE   B 1 156 ? 54.230 -32.196 -7.864  1.00 21.21 ?  156 PHE   B HE1  1 
ATOM   6723 H HE2  . PHE   B 1 156 ? 53.537 -34.725 -4.840  1.00 20.61 ?  156 PHE   B HE2  1 
ATOM   6724 H HZ   . PHE   B 1 156 ? 54.984 -33.811 -6.393  1.00 20.91 ?  156 PHE   B HZ   1 
ATOM   6725 N N    . ASP   B 1 157 ? 48.612 -34.904 -6.911  1.00 16.50 ?  157 ASP   B N    1 
ATOM   6726 C CA   . ASP   B 1 157 ? 48.756 -36.353 -7.006  1.00 17.60 ?  157 ASP   B CA   1 
ATOM   6727 C C    . ASP   B 1 157 ? 47.840 -36.907 -8.093  1.00 17.67 ?  157 ASP   B C    1 
ATOM   6728 O O    . ASP   B 1 157 ? 46.613 -36.774 -8.000  1.00 16.97 ?  157 ASP   B O    1 
ATOM   6729 C CB   . ASP   B 1 157 ? 48.394 -36.964 -5.659  1.00 19.32 ?  157 ASP   B CB   1 
ATOM   6730 C CG   . ASP   B 1 157 ? 48.525 -38.471 -5.640  1.00 21.28 ?  157 ASP   B CG   1 
ATOM   6731 O OD1  . ASP   B 1 157 ? 48.880 -39.077 -6.679  1.00 21.79 ?  157 ASP   B OD1  1 
ATOM   6732 O OD2  . ASP   B 1 157 ? 48.273 -39.051 -4.568  1.00 23.39 -1 157 ASP   B OD2  1 
ATOM   6733 H H    . ASP   B 1 157 ? 48.071 -34.649 -6.300  1.00 19.96 ?  157 ASP   B H    1 
ATOM   6734 H HA   . ASP   B 1 157 ? 49.677 -36.588 -7.221  1.00 21.27 ?  157 ASP   B HA   1 
ATOM   6735 H HB2  . ASP   B 1 157 ? 48.974 -36.589 -4.981  1.00 23.33 ?  157 ASP   B HB2  1 
ATOM   6736 H HB3  . ASP   B 1 157 ? 47.468 -36.745 -5.458  1.00 23.33 ?  157 ASP   B HB3  1 
ATOM   6737 N N    A LYS   B 1 158 ? 48.438 -37.549 -9.104  0.34 18.26 ?  158 LYS   B N    1 
ATOM   6738 N N    B LYS   B 1 158 ? 48.434 -37.551 -9.106  0.66 18.53 ?  158 LYS   B N    1 
ATOM   6739 C CA   A LYS   B 1 158 ? 47.663 -38.138 -10.195 0.34 19.15 ?  158 LYS   B CA   1 
ATOM   6740 C CA   B LYS   B 1 158 ? 47.653 -38.136 -10.197 0.66 19.62 ?  158 LYS   B CA   1 
ATOM   6741 C C    A LYS   B 1 158 ? 46.594 -39.096 -9.674  0.34 19.20 ?  158 LYS   B C    1 
ATOM   6742 C C    B LYS   B 1 158 ? 46.590 -39.099 -9.673  0.66 19.49 ?  158 LYS   B C    1 
ATOM   6743 O O    A LYS   B 1 158 ? 45.486 -39.161 -10.220 0.34 19.06 ?  158 LYS   B O    1 
ATOM   6744 O O    B LYS   B 1 158 ? 45.482 -39.174 -10.221 0.66 19.62 ?  158 LYS   B O    1 
ATOM   6745 C CB   A LYS   B 1 158 ? 48.613 -38.856 -11.163 0.34 20.34 ?  158 LYS   B CB   1 
ATOM   6746 C CB   B LYS   B 1 158 ? 48.594 -38.847 -11.178 0.66 21.22 ?  158 LYS   B CB   1 
ATOM   6747 C CG   A LYS   B 1 158 ? 47.936 -39.774 -12.173 0.34 21.79 ?  158 LYS   B CG   1 
ATOM   6748 C CG   B LYS   B 1 158 ? 47.902 -39.715 -12.225 0.66 23.15 ?  158 LYS   B CG   1 
ATOM   6749 C CD   A LYS   B 1 158 ? 47.051 -39.006 -13.134 0.34 23.16 ?  158 LYS   B CD   1 
ATOM   6750 C CD   B LYS   B 1 158 ? 47.040 -38.898 -13.167 0.66 25.15 ?  158 LYS   B CD   1 
ATOM   6751 C CE   A LYS   B 1 158 ? 46.469 -39.929 -14.190 0.34 24.20 ?  158 LYS   B CE   1 
ATOM   6752 C CE   B LYS   B 1 158 ? 46.447 -39.775 -14.259 0.66 26.49 ?  158 LYS   B CE   1 
ATOM   6753 N NZ   A LYS   B 1 158 ? 45.432 -39.251 -15.012 0.34 24.53 ?  158 LYS   B NZ   1 
ATOM   6754 N NZ   B LYS   B 1 158 ? 45.401 -39.063 -15.047 0.66 26.94 ?  158 LYS   B NZ   1 
ATOM   6755 H H    A LYS   B 1 158 ? 49.291 -37.659 -9.177  0.34 22.06 ?  158 LYS   B H    1 
ATOM   6756 H H    B LYS   B 1 158 ? 49.287 -37.670 -9.178  0.66 22.39 ?  158 LYS   B H    1 
ATOM   6757 H HA   A LYS   B 1 158 ? 47.224 -37.430 -10.690 0.34 23.13 ?  158 LYS   B HA   1 
ATOM   6758 H HA   B LYS   B 1 158 ? 47.210 -37.425 -10.682 0.66 23.69 ?  158 LYS   B HA   1 
ATOM   6759 H HB2  A LYS   B 1 158 ? 49.109 -38.188 -11.669 0.34 24.56 ?  158 LYS   B HB2  1 
ATOM   6760 H HB2  B LYS   B 1 158 ? 49.112 -38.177 -11.658 0.66 25.62 ?  158 LYS   B HB2  1 
ATOM   6761 H HB3  A LYS   B 1 158 ? 49.234 -39.395 -10.650 0.34 24.56 ?  158 LYS   B HB3  1 
ATOM   6762 H HB3  B LYS   B 1 158 ? 49.196 -39.420 -10.678 0.66 25.62 ?  158 LYS   B HB3  1 
ATOM   6763 H HG2  A LYS   B 1 158 ? 48.620 -40.222 -12.694 0.34 26.30 ?  158 LYS   B HG2  1 
ATOM   6764 H HG2  B LYS   B 1 158 ? 48.580 -40.162 -12.757 0.66 27.94 ?  158 LYS   B HG2  1 
ATOM   6765 H HG3  A LYS   B 1 158 ? 47.393 -40.433 -11.712 0.34 26.30 ?  158 LYS   B HG3  1 
ATOM   6766 H HG3  B LYS   B 1 158 ? 47.342 -40.376 -11.789 0.66 27.94 ?  158 LYS   B HG3  1 
ATOM   6767 H HD2  A LYS   B 1 158 ? 46.318 -38.600 -12.645 0.34 27.94 ?  158 LYS   B HD2  1 
ATOM   6768 H HD2  B LYS   B 1 158 ? 46.312 -38.494 -12.669 0.66 30.34 ?  158 LYS   B HD2  1 
ATOM   6769 H HD3  A LYS   B 1 158 ? 47.577 -38.323 -13.581 0.34 27.94 ?  158 LYS   B HD3  1 
ATOM   6770 H HD3  B LYS   B 1 158 ? 47.583 -38.211 -13.587 0.66 30.34 ?  158 LYS   B HD3  1 
ATOM   6771 H HE2  A LYS   B 1 158 ? 47.179 -40.222 -14.781 0.34 29.20 ?  158 LYS   B HE2  1 
ATOM   6772 H HE2  B LYS   B 1 158 ? 47.151 -40.046 -14.868 0.66 31.93 ?  158 LYS   B HE2  1 
ATOM   6773 H HE3  A LYS   B 1 158 ? 46.060 -40.693 -13.755 0.34 29.20 ?  158 LYS   B HE3  1 
ATOM   6774 H HE3  B LYS   B 1 158 ? 46.038 -40.556 -13.853 0.66 31.93 ?  158 LYS   B HE3  1 
ATOM   6775 H HZ1  A LYS   B 1 158 ? 45.110 -39.814 -15.619 0.34 29.59 ?  158 LYS   B HZ1  1 
ATOM   6776 H HZ1  B LYS   B 1 158 ? 45.074 -39.601 -15.676 0.66 32.48 ?  158 LYS   B HZ1  1 
ATOM   6777 H HZ2  A LYS   B 1 158 ? 44.766 -38.973 -14.491 0.34 29.59 ?  158 LYS   B HZ2  1 
ATOM   6778 H HZ2  B LYS   B 1 158 ? 44.738 -38.807 -14.511 0.66 32.48 ?  158 LYS   B HZ2  1 
ATOM   6779 H HZ3  A LYS   B 1 158 ? 45.787 -38.547 -15.427 0.34 29.59 ?  158 LYS   B HZ3  1 
ATOM   6780 H HZ3  B LYS   B 1 158 ? 45.752 -38.343 -15.436 0.66 32.48 ?  158 LYS   B HZ3  1 
ATOM   6781 N N    . ASN   B 1 159 ? 46.909 -39.855 -8.622  1.00 19.93 ?  159 ASN   B N    1 
ATOM   6782 C CA   . ASN   B 1 159 ? 45.953 -40.831 -8.103  1.00 21.08 ?  159 ASN   B CA   1 
ATOM   6783 C C    . ASN   B 1 159 ? 44.761 -40.152 -7.428  1.00 19.79 ?  159 ASN   B C    1 
ATOM   6784 O O    . ASN   B 1 159 ? 43.623 -40.635 -7.526  1.00 20.10 ?  159 ASN   B O    1 
ATOM   6785 C CB   . ASN   B 1 159 ? 46.664 -41.794 -7.157  1.00 23.52 ?  159 ASN   B CB   1 
ATOM   6786 C CG   . ASN   B 1 159 ? 47.685 -42.647 -7.872  1.00 26.31 ?  159 ASN   B CG   1 
ATOM   6787 O OD1  . ASN   B 1 159 ? 47.428 -43.147 -8.972  1.00 27.74 ?  159 ASN   B OD1  1 
ATOM   6788 N ND2  . ASN   B 1 159 ? 48.859 -42.810 -7.260  1.00 27.23 ?  159 ASN   B ND2  1 
ATOM   6789 H H    A ASN   B 1 159 ? 47.658 -39.820 -8.203  0.34 24.06 ?  159 ASN   B H    1 
ATOM   6790 H H    B ASN   B 1 159 ? 47.658 -39.817 -8.202  0.66 24.06 ?  159 ASN   B H    1 
ATOM   6791 H HA   . ASN   B 1 159 ? 45.616 -41.349 -8.851  1.00 25.45 ?  159 ASN   B HA   1 
ATOM   6792 H HB2  . ASN   B 1 159 ? 47.123 -41.293 -6.469  1.00 28.37 ?  159 ASN   B HB2  1 
ATOM   6793 H HB3  . ASN   B 1 159 ? 46.010 -42.391 -6.763  1.00 28.37 ?  159 ASN   B HB3  1 
ATOM   6794 H HD21 . ASN   B 1 159 ? 49.483 -43.286 -7.623  1.00 32.83 ?  159 ASN   B HD21 1 
ATOM   6795 H HD22 . ASN   B 1 159 ? 49.002 -42.444 -6.492  1.00 32.83 ?  159 ASN   B HD22 1 
ATOM   6796 N N    . LEU   B 1 160 ? 44.987 -39.026 -6.750  1.00 18.26 ?  160 LEU   B N    1 
ATOM   6797 C CA   . LEU   B 1 160 ? 43.858 -38.291 -6.196  1.00 17.36 ?  160 LEU   B CA   1 
ATOM   6798 C C    . LEU   B 1 160 ? 43.060 -37.622 -7.303  1.00 16.70 ?  160 LEU   B C    1 
ATOM   6799 O O    . LEU   B 1 160 ? 41.820 -37.617 -7.265  1.00 16.45 ?  160 LEU   B O    1 
ATOM   6800 C CB   . LEU   B 1 160 ? 44.326 -37.254 -5.179  1.00 17.04 ?  160 LEU   B CB   1 
ATOM   6801 C CG   . LEU   B 1 160 ? 43.197 -36.352 -4.664  1.00 16.87 ?  160 LEU   B CG   1 
ATOM   6802 C CD1  . LEU   B 1 160 ? 42.071 -37.155 -4.022  1.00 17.81 ?  160 LEU   B CD1  1 
ATOM   6803 C CD2  . LEU   B 1 160 ? 43.750 -35.320 -3.689  1.00 17.15 ?  160 LEU   B CD2  1 
ATOM   6804 H H    . LEU   B 1 160 ? 45.761 -38.677 -6.614  1.00 22.07 ?  160 LEU   B H    1 
ATOM   6805 H HA   . LEU   B 1 160 ? 43.273 -38.918 -5.751  1.00 20.98 ?  160 LEU   B HA   1 
ATOM   6806 H HB2  . LEU   B 1 160 ? 44.708 -37.718 -4.421  1.00 20.60 ?  160 LEU   B HB2  1 
ATOM   6807 H HB3  . LEU   B 1 160 ? 44.995 -36.688 -5.595  1.00 20.60 ?  160 LEU   B HB3  1 
ATOM   6808 H HG   . LEU   B 1 160 ? 42.817 -35.864 -5.413  1.00 20.40 ?  160 LEU   B HG   1 
ATOM   6809 H HD11 . LEU   B 1 160 ? 41.435 -36.539 -3.622  1.00 21.53 ?  160 LEU   B HD11 1 
ATOM   6810 H HD12 . LEU   B 1 160 ? 41.628 -37.688 -4.702  1.00 21.53 ?  160 LEU   B HD12 1 
ATOM   6811 H HD13 . LEU   B 1 160 ? 42.444 -37.733 -3.339  1.00 21.53 ?  160 LEU   B HD13 1 
ATOM   6812 H HD21 . LEU   B 1 160 ? 43.025 -34.748 -3.394  1.00 20.73 ?  160 LEU   B HD21 1 
ATOM   6813 H HD22 . LEU   B 1 160 ? 44.142 -35.780 -2.934  1.00 20.73 ?  160 LEU   B HD22 1 
ATOM   6814 H HD23 . LEU   B 1 160 ? 44.425 -34.790 -4.144  1.00 20.73 ?  160 LEU   B HD23 1 
ATOM   6815 N N    . TYR   B 1 161 ? 43.755 -37.049 -8.294  1.00 16.91 ?  161 TYR   B N    1 
ATOM   6816 C CA   . TYR   B 1 161 ? 43.080 -36.484 -9.460  1.00 16.67 ?  161 TYR   B CA   1 
ATOM   6817 C C    . TYR   B 1 161 ? 42.126 -37.502 -10.078 1.00 16.37 ?  161 TYR   B C    1 
ATOM   6818 O O    . TYR   B 1 161 ? 40.953 -37.202 -10.331 1.00 15.84 ?  161 TYR   B O    1 
ATOM   6819 C CB   . TYR   B 1 161 ? 44.118 -36.005 -10.485 1.00 17.35 ?  161 TYR   B CB   1 
ATOM   6820 C CG   . TYR   B 1 161 ? 43.533 -35.531 -11.800 1.00 18.01 ?  161 TYR   B CG   1 
ATOM   6821 C CD1  . TYR   B 1 161 ? 43.151 -34.204 -11.974 1.00 18.21 ?  161 TYR   B CD1  1 
ATOM   6822 C CD2  . TYR   B 1 161 ? 43.358 -36.408 -12.867 1.00 18.65 ?  161 TYR   B CD2  1 
ATOM   6823 C CE1  . TYR   B 1 161 ? 42.614 -33.767 -13.166 1.00 19.44 ?  161 TYR   B CE1  1 
ATOM   6824 C CE2  . TYR   B 1 161 ? 42.820 -35.979 -14.061 1.00 19.75 ?  161 TYR   B CE2  1 
ATOM   6825 C CZ   . TYR   B 1 161 ? 42.451 -34.659 -14.206 1.00 19.86 ?  161 TYR   B CZ   1 
ATOM   6826 O OH   . TYR   B 1 161 ? 41.915 -34.229 -15.394 1.00 21.91 ?  161 TYR   B OH   1 
ATOM   6827 H H    . TYR   B 1 161 ? 44.609 -36.985 -8.320  1.00 20.45 ?  161 TYR   B H    1 
ATOM   6828 H HA   . TYR   B 1 161 ? 42.558 -35.715 -9.185  1.00 20.16 ?  161 TYR   B HA   1 
ATOM   6829 H HB2  . TYR   B 1 161 ? 44.614 -35.260 -10.105 1.00 20.97 ?  161 TYR   B HB2  1 
ATOM   6830 H HB3  . TYR   B 1 161 ? 44.726 -36.732 -10.684 1.00 20.97 ?  161 TYR   B HB3  1 
ATOM   6831 H HD1  . TYR   B 1 161 ? 43.263 -33.597 -11.279 1.00 22.00 ?  161 TYR   B HD1  1 
ATOM   6832 H HD2  . TYR   B 1 161 ? 43.602 -37.302 -12.776 1.00 22.54 ?  161 TYR   B HD2  1 
ATOM   6833 H HE1  . TYR   B 1 161 ? 42.366 -32.873 -13.267 1.00 23.48 ?  161 TYR   B HE1  1 
ATOM   6834 H HE2  . TYR   B 1 161 ? 42.704 -36.578 -14.765 1.00 23.85 ?  161 TYR   B HE2  1 
ATOM   6835 H HH   . TYR   B 1 161 ? 41.870 -34.871 -15.936 1.00 26.45 ?  161 TYR   B HH   1 
ATOM   6836 N N    . ASP   B 1 162 ? 42.615 -38.723 -10.311 1.00 16.92 ?  162 ASP   B N    1 
ATOM   6837 C CA   . ASP   B 1 162 ? 41.777 -39.755 -10.914 1.00 17.39 ?  162 ASP   B CA   1 
ATOM   6838 C C    . ASP   B 1 162 ? 40.575 -40.085 -10.032 1.00 17.04 ?  162 ASP   B C    1 
ATOM   6839 O O    . ASP   B 1 162 ? 39.463 -40.291 -10.536 1.00 17.59 ?  162 ASP   B O    1 
ATOM   6840 C CB   . ASP   B 1 162 ? 42.598 -41.021 -11.172 1.00 18.84 ?  162 ASP   B CB   1 
ATOM   6841 C CG   . ASP   B 1 162 ? 43.602 -40.861 -12.298 1.00 20.20 ?  162 ASP   B CG   1 
ATOM   6842 O OD1  . ASP   B 1 162 ? 43.469 -39.919 -13.104 1.00 20.78 ?  162 ASP   B OD1  1 
ATOM   6843 O OD2  . ASP   B 1 162 ? 44.512 -41.714 -12.392 1.00 21.95 -1 162 ASP   B OD2  1 
ATOM   6844 H H    . ASP   B 1 162 ? 43.419 -38.972 -10.129 1.00 20.46 ?  162 ASP   B H    1 
ATOM   6845 H HA   . ASP   B 1 162 ? 41.445 -39.433 -11.766 1.00 21.01 ?  162 ASP   B HA   1 
ATOM   6846 H HB2  . ASP   B 1 162 ? 43.089 -41.249 -10.371 1.00 22.75 ?  162 ASP   B HB2  1 
ATOM   6847 H HB3  . ASP   B 1 162 ? 41.996 -41.741 -11.413 1.00 22.75 ?  162 ASP   B HB3  1 
ATOM   6848 N N    . LYS   B 1 163 ? 40.781 -40.167 -8.715  1.00 16.47 ?  163 LYS   B N    1 
ATOM   6849 C CA   . LYS   B 1 163 ? 39.663 -40.437 -7.813  1.00 17.15 ?  163 LYS   B CA   1 
ATOM   6850 C C    . LYS   B 1 163 ? 38.623 -39.322 -7.869  1.00 15.86 ?  163 LYS   B C    1 
ATOM   6851 O O    . LYS   B 1 163 ? 37.410 -39.583 -7.861  1.00 16.88 ?  163 LYS   B O    1 
ATOM   6852 C CB   . LYS   B 1 163 ? 40.172 -40.613 -6.383  1.00 20.30 ?  163 LYS   B CB   1 
ATOM   6853 C CG   . LYS   B 1 163 ? 39.099 -41.095 -5.432  1.00 26.35 ?  163 LYS   B CG   1 
ATOM   6854 C CD   . LYS   B 1 163 ? 39.620 -41.295 -4.022  1.00 31.75 ?  163 LYS   B CD   1 
ATOM   6855 C CE   . LYS   B 1 163 ? 38.530 -41.865 -3.125  1.00 35.39 ?  163 LYS   B CE   1 
ATOM   6856 N NZ   . LYS   B 1 163 ? 38.829 -41.679 -1.678  1.00 37.63 ?  163 LYS   B NZ   1 
ATOM   6857 H H    . LYS   B 1 163 ? 41.546 -40.075 -8.331  1.00 19.92 ?  163 LYS   B H    1 
ATOM   6858 H HA   . LYS   B 1 163 ? 39.237 -41.261 -8.082  1.00 20.73 ?  163 LYS   B HA   1 
ATOM   6859 H HB2  . LYS   B 1 163 ? 40.892 -41.268 -6.381  1.00 24.51 ?  163 LYS   B HB2  1 
ATOM   6860 H HB3  . LYS   B 1 163 ? 40.504 -39.762 -6.056  1.00 24.51 ?  163 LYS   B HB3  1 
ATOM   6861 H HG2  . LYS   B 1 163 ? 38.387 -40.439 -5.398  1.00 31.77 ?  163 LYS   B HG2  1 
ATOM   6862 H HG3  . LYS   B 1 163 ? 38.754 -41.945 -5.750  1.00 31.77 ?  163 LYS   B HG3  1 
ATOM   6863 H HD2  . LYS   B 1 163 ? 40.362 -41.922 -4.038  1.00 38.25 ?  163 LYS   B HD2  1 
ATOM   6864 H HD3  . LYS   B 1 163 ? 39.904 -40.443 -3.659  1.00 38.25 ?  163 LYS   B HD3  1 
ATOM   6865 H HE2  . LYS   B 1 163 ? 37.689 -41.424 -3.321  1.00 42.62 ?  163 LYS   B HE2  1 
ATOM   6866 H HE3  . LYS   B 1 163 ? 38.448 -42.816 -3.295  1.00 42.62 ?  163 LYS   B HE3  1 
ATOM   6867 H HZ1  . LYS   B 1 163 ? 38.171 -42.021 -1.186  1.00 45.31 ?  163 LYS   B HZ1  1 
ATOM   6868 H HZ2  . LYS   B 1 163 ? 39.590 -42.090 -1.471  1.00 45.31 ?  163 LYS   B HZ2  1 
ATOM   6869 H HZ3  . LYS   B 1 163 ? 38.907 -40.812 -1.493  1.00 45.31 ?  163 LYS   B HZ3  1 
ATOM   6870 N N    . LEU   B 1 164 ? 39.084 -38.072 -7.924  1.00 14.45 ?  164 LEU   B N    1 
ATOM   6871 C CA   . LEU   B 1 164 ? 38.182 -36.926 -7.979  1.00 14.08 ?  164 LEU   B CA   1 
ATOM   6872 C C    . LEU   B 1 164 ? 37.388 -36.902 -9.282  1.00 14.75 ?  164 LEU   B C    1 
ATOM   6873 O O    . LEU   B 1 164 ? 36.166 -36.697 -9.271  1.00 15.86 ?  164 LEU   B O    1 
ATOM   6874 C CB   . LEU   B 1 164 ? 38.986 -35.634 -7.819  1.00 14.10 ?  164 LEU   B CB   1 
ATOM   6875 C CG   . LEU   B 1 164 ? 39.532 -35.361 -6.422  1.00 14.85 ?  164 LEU   B CG   1 
ATOM   6876 C CD1  . LEU   B 1 164 ? 40.607 -34.293 -6.488  1.00 14.66 ?  164 LEU   B CD1  1 
ATOM   6877 C CD2  . LEU   B 1 164 ? 38.423 -34.939 -5.472  1.00 16.54 ?  164 LEU   B CD2  1 
ATOM   6878 H H    . LEU   B 1 164 ? 39.925 -37.856 -7.937  1.00 17.50 ?  164 LEU   B H    1 
ATOM   6879 H HA   . LEU   B 1 164 ? 37.557 -36.982 -7.248  1.00 17.05 ?  164 LEU   B HA   1 
ATOM   6880 H HB2  . LEU   B 1 164 ? 39.746 -35.667 -8.423  1.00 17.07 ?  164 LEU   B HB2  1 
ATOM   6881 H HB3  . LEU   B 1 164 ? 38.418 -34.888 -8.058  1.00 17.07 ?  164 LEU   B HB3  1 
ATOM   6882 H HG   . LEU   B 1 164 ? 39.938 -36.168 -6.074  1.00 17.97 ?  164 LEU   B HG   1 
ATOM   6883 H HD11 . LEU   B 1 164 ? 40.938 -34.117 -5.590  1.00 17.74 ?  164 LEU   B HD11 1 
ATOM   6884 H HD12 . LEU   B 1 164 ? 41.336 -34.607 -7.049  1.00 17.74 ?  164 LEU   B HD12 1 
ATOM   6885 H HD13 . LEU   B 1 164 ? 40.230 -33.481 -6.862  1.00 17.74 ?  164 LEU   B HD13 1 
ATOM   6886 H HD21 . LEU   B 1 164 ? 38.810 -34.707 -4.615  1.00 19.99 ?  164 LEU   B HD21 1 
ATOM   6887 H HD22 . LEU   B 1 164 ? 37.961 -34.171 -5.845  1.00 19.99 ?  164 LEU   B HD22 1 
ATOM   6888 H HD23 . LEU   B 1 164 ? 37.802 -35.678 -5.366  1.00 19.99 ?  164 LEU   B HD23 1 
ATOM   6889 N N    . VAL   B 1 165 ? 38.069 -37.078 -10.417 1.00 16.27 ?  165 VAL   B N    1 
ATOM   6890 C CA   . VAL   B 1 165 ? 37.402 -37.016 -11.714 1.00 18.08 ?  165 VAL   B CA   1 
ATOM   6891 C C    . VAL   B 1 165 ? 36.494 -38.223 -11.901 1.00 20.33 ?  165 VAL   B C    1 
ATOM   6892 O O    . VAL   B 1 165 ? 35.334 -38.092 -12.313 1.00 21.66 ?  165 VAL   B O    1 
ATOM   6893 C CB   . VAL   B 1 165 ? 38.438 -36.927 -12.849 1.00 19.06 ?  165 VAL   B CB   1 
ATOM   6894 C CG1  . VAL   B 1 165 ? 37.756 -37.021 -14.196 1.00 20.59 ?  165 VAL   B CG1  1 
ATOM   6895 C CG2  . VAL   B 1 165 ? 39.242 -35.647 -12.741 1.00 19.30 ?  165 VAL   B CG2  1 
ATOM   6896 H H    . VAL   B 1 165 ? 38.915 -37.237 -10.461 1.00 19.67 ?  165 VAL   B H    1 
ATOM   6897 H HA   . VAL   B 1 165 ? 36.850 -36.221 -11.749 1.00 21.85 ?  165 VAL   B HA   1 
ATOM   6898 H HB   . VAL   B 1 165 ? 39.059 -37.667 -12.768 1.00 23.02 ?  165 VAL   B HB   1 
ATOM   6899 H HG11 . VAL   B 1 165 ? 38.359 -36.697 -14.879 1.00 24.86 ?  165 VAL   B HG11 1 
ATOM   6900 H HG12 . VAL   B 1 165 ? 37.534 -37.951 -14.370 1.00 24.86 ?  165 VAL   B HG12 1 
ATOM   6901 H HG13 . VAL   B 1 165 ? 36.949 -36.486 -14.181 1.00 24.86 ?  165 VAL   B HG13 1 
ATOM   6902 H HG21 . VAL   B 1 165 ? 39.874 -35.604 -13.477 1.00 23.32 ?  165 VAL   B HG21 1 
ATOM   6903 H HG22 . VAL   B 1 165 ? 38.638 -34.886 -12.785 1.00 23.32 ?  165 VAL   B HG22 1 
ATOM   6904 H HG23 . VAL   B 1 165 ? 39.721 -35.636 -11.896 1.00 23.32 ?  165 VAL   B HG23 1 
ATOM   6905 N N    . SER   B 1 166 ? 37.019 -39.422 -11.615 1.00 21.34 ?  166 SER   B N    1 
ATOM   6906 C CA   . SER   B 1 166 ? 36.281 -40.642 -11.911 1.00 22.50 ?  166 SER   B CA   1 
ATOM   6907 C C    . SER   B 1 166 ? 35.010 -40.737 -11.081 1.00 22.78 ?  166 SER   B C    1 
ATOM   6908 O O    . SER   B 1 166 ? 34.046 -41.372 -11.509 1.00 23.97 ?  166 SER   B O    1 
ATOM   6909 C CB   . SER   B 1 166 ? 37.162 -41.887 -11.716 1.00 23.50 ?  166 SER   B CB   1 
ATOM   6910 O OG   . SER   B 1 166 ? 37.475 -42.101 -10.349 1.00 23.61 ?  166 SER   B OG   1 
ATOM   6911 H H    . SER   B 1 166 ? 37.797 -39.548 -11.256 1.00 25.76 ?  166 SER   B H    1 
ATOM   6912 H HA   . SER   B 1 166 ? 36.027 -40.625 -12.845 1.00 27.15 ?  166 SER   B HA   1 
ATOM   6913 H HB2  . SER   B 1 166 ? 36.691 -42.661 -12.054 1.00 28.35 ?  166 SER   B HB2  1 
ATOM   6914 H HB3  . SER   B 1 166 ? 37.993 -41.767 -12.212 1.00 28.35 ?  166 SER   B HB3  1 
ATOM   6915 H HG   . SER   B 1 166 ? 37.893 -41.434 -10.047 1.00 28.48 ?  166 SER   B HG   1 
ATOM   6916 N N    . SER   B 1 167 ? 34.977 -40.106 -9.908  1.00 20.99 ?  167 SER   B N    1 
ATOM   6917 C CA   . SER   B 1 167 ? 33.826 -40.169 -9.017  1.00 20.51 ?  167 SER   B CA   1 
ATOM   6918 C C    . SER   B 1 167 ? 32.911 -38.945 -9.096  1.00 19.85 ?  167 SER   B C    1 
ATOM   6919 O O    . SER   B 1 167 ? 31.836 -38.951 -8.484  1.00 20.26 ?  167 SER   B O    1 
ATOM   6920 C CB   . SER   B 1 167 ? 34.286 -40.362 -7.565  1.00 20.99 ?  167 SER   B CB   1 
ATOM   6921 O OG   . SER   B 1 167 ? 34.940 -39.194 -7.076  1.00 21.05 ?  167 SER   B OG   1 
ATOM   6922 H H    . SER   B 1 167 ? 35.621 -39.633 -9.608  1.00 25.34 ?  167 SER   B H    1 
ATOM   6923 H HA   . SER   B 1 167 ? 33.292 -40.941 -9.263  1.00 24.76 ?  167 SER   B HA   1 
ATOM   6924 H HB2  . SER   B 1 167 ? 33.505 -40.554 -7.017  1.00 25.33 ?  167 SER   B HB2  1 
ATOM   6925 H HB3  . SER   B 1 167 ? 34.893 -41.127 -7.534  1.00 25.33 ?  167 SER   B HB3  1 
ATOM   6926 H HG   . SER   B 1 167 ? 35.624 -39.054 -7.533  1.00 25.42 ?  167 SER   B HG   1 
ATOM   6927 N N    . PHE   B 1 168 ? 33.295 -37.892 -9.823  1.00 19.72 ?  168 PHE   B N    1 
ATOM   6928 C CA   . PHE   B 1 168 ? 32.455 -36.692 -9.878  1.00 18.82 ?  168 PHE   B CA   1 
ATOM   6929 C C    . PHE   B 1 168 ? 31.146 -36.951 -10.624 1.00 15.71 ?  168 PHE   B C    1 
ATOM   6930 O O    . PHE   B 1 168 ? 30.099 -36.355 -10.297 1.00 16.19 ?  168 PHE   B O    1 
ATOM   6931 C CB   . PHE   B 1 168 ? 33.218 -35.540 -10.530 1.00 19.53 ?  168 PHE   B CB   1 
ATOM   6932 C CG   . PHE   B 1 168 ? 32.393 -34.303 -10.701 1.00 19.74 ?  168 PHE   B CG   1 
ATOM   6933 C CD1  . PHE   B 1 168 ? 32.022 -33.551 -9.596  1.00 20.91 ?  168 PHE   B CD1  1 
ATOM   6934 C CD2  . PHE   B 1 168 ? 31.973 -33.898 -11.953 1.00 18.95 ?  168 PHE   B CD2  1 
ATOM   6935 C CE1  . PHE   B 1 168 ? 31.249 -32.415 -9.733  1.00 20.97 ?  168 PHE   B CE1  1 
ATOM   6936 C CE2  . PHE   B 1 168 ? 31.211 -32.749 -12.105 1.00 19.88 ?  168 PHE   B CE2  1 
ATOM   6937 C CZ   . PHE   B 1 168 ? 30.839 -32.006 -10.988 1.00 19.88 ?  168 PHE   B CZ   1 
ATOM   6938 H H    . PHE   B 1 168 ? 34.026 -37.844 -10.279 1.00 23.82 ?  168 PHE   B H    1 
ATOM   6939 H HA   . PHE   B 1 168 ? 32.230 -36.427 -8.976  1.00 22.73 ?  168 PHE   B HA   1 
ATOM   6940 H HB2  . PHE   B 1 168 ? 33.980 -35.313 -9.973  1.00 23.59 ?  168 PHE   B HB2  1 
ATOM   6941 H HB3  . PHE   B 1 168 ? 33.524 -35.817 -11.407 1.00 23.59 ?  168 PHE   B HB3  1 
ATOM   6942 H HD1  . PHE   B 1 168 ? 32.289 -33.823 -8.750  1.00 25.24 ?  168 PHE   B HD1  1 
ATOM   6943 H HD2  . PHE   B 1 168 ? 32.217 -34.385 -12.702 1.00 22.89 ?  168 PHE   B HD2  1 
ATOM   6944 H HE1  . PHE   B 1 168 ? 31.005 -31.924 -8.984  1.00 25.32 ?  168 PHE   B HE1  1 
ATOM   6945 H HE2  . PHE   B 1 168 ? 30.929 -32.481 -12.953 1.00 24.01 ?  168 PHE   B HE2  1 
ATOM   6946 H HZ   . PHE   B 1 168 ? 30.316 -31.240 -11.087 1.00 24.01 ?  168 PHE   B HZ   1 
ATOM   6947 N N    . LEU   B 1 169 ? 31.192 -37.824 -11.629 1.00 15.60 ?  169 LEU   B N    1 
ATOM   6948 C CA   . LEU   B 1 169 ? 30.016 -38.158 -12.430 1.00 18.07 ?  169 LEU   B CA   1 
ATOM   6949 C C    . LEU   B 1 169 ? 29.997 -39.602 -12.913 1.00 21.17 ?  169 LEU   B C    1 
ATOM   6950 O O    . LEU   B 1 169 ? 29.073 -40.027 -13.612 1.00 23.64 ?  169 LEU   B O    1 
ATOM   6951 C CB   . LEU   B 1 169 ? 29.943 -37.252 -13.655 1.00 20.12 ?  169 LEU   B CB   1 
ATOM   6952 C CG   . LEU   B 1 169 ? 28.724 -36.342 -13.762 1.00 23.51 ?  169 LEU   B CG   1 
ATOM   6953 C CD1  . LEU   B 1 169 ? 28.652 -35.756 -15.155 1.00 24.35 ?  169 LEU   B CD1  1 
ATOM   6954 C CD2  . LEU   B 1 169 ? 27.441 -37.081 -13.424 1.00 23.74 ?  169 LEU   B CD2  1 
ATOM   6955 O OXT  . LEU   B 1 169 ? 30.908 -40.370 -12.639 1.00 22.23 -1 169 LEU   B OXT  1 
ATOM   6956 H H    . LEU   B 1 169 ? 31.909 -38.230 -11.883 1.00 18.87 ?  169 LEU   B H    1 
ATOM   6957 H HA   . LEU   B 1 169 ? 29.232 -38.011 -11.885 1.00 21.84 ?  169 LEU   B HA   1 
ATOM   6958 H HB2  . LEU   B 1 169 ? 30.726 -36.681 -13.666 1.00 24.29 ?  169 LEU   B HB2  1 
ATOM   6959 H HB3  . LEU   B 1 169 ? 29.944 -37.811 -14.449 1.00 24.29 ?  169 LEU   B HB3  1 
ATOM   6960 H HG   . LEU   B 1 169 ? 28.820 -35.606 -13.135 1.00 28.37 ?  169 LEU   B HG   1 
ATOM   6961 H HD11 . LEU   B 1 169 ? 27.895 -35.152 -15.204 1.00 29.37 ?  169 LEU   B HD11 1 
ATOM   6962 H HD12 . LEU   B 1 169 ? 29.474 -35.275 -15.334 1.00 29.37 ?  169 LEU   B HD12 1 
ATOM   6963 H HD13 . LEU   B 1 169 ? 28.543 -36.479 -15.792 1.00 29.37 ?  169 LEU   B HD13 1 
ATOM   6964 H HD21 . LEU   B 1 169 ? 26.698 -36.646 -13.864 1.00 28.63 ?  169 LEU   B HD21 1 
ATOM   6965 H HD22 . LEU   B 1 169 ? 27.519 -37.999 -13.734 1.00 28.63 ?  169 LEU   B HD22 1 
ATOM   6966 H HD23 . LEU   B 1 169 ? 27.314 -37.068 -12.463 1.00 28.63 ?  169 LEU   B HD23 1 
HETATM 6967 N N2   B A1A6Z C 2 .   ? 14.950 -0.189  3.669   0.66 11.06 ?  201 A1A6Z A N2   1 
HETATM 6968 C C3   B A1A6Z C 2 .   ? 12.591 1.843   -0.124  0.66 14.15 ?  201 A1A6Z A C3   1 
HETATM 6969 C C6   B A1A6Z C 2 .   ? 16.152 -1.082  0.683   0.66 12.46 ?  201 A1A6Z A C6   1 
HETATM 6970 C C9   B A1A6Z C 2 .   ? 15.285 2.015   5.183   0.66 10.01 ?  201 A1A6Z A C9   1 
HETATM 6971 C C12  B A1A6Z C 2 .   ? 15.663 4.209   4.848   0.66 9.67  ?  201 A1A6Z A C12  1 
HETATM 6972 C C1   B A1A6Z C 2 .   ? 14.386 2.594   -1.747  0.66 13.89 ?  201 A1A6Z A C1   1 
HETATM 6973 C C10  B A1A6Z C 2 .   ? 15.318 2.185   3.765   0.66 10.26 ?  201 A1A6Z A C10  1 
HETATM 6974 C C11  B A1A6Z C 2 .   ? 15.562 3.607   3.581   0.66 10.04 ?  201 A1A6Z A C11  1 
HETATM 6975 C C13  B A1A6Z C 2 .   ? 14.930 2.203   0.751   0.66 11.54 ?  201 A1A6Z A C13  1 
HETATM 6976 C C2   B A1A6Z C 2 .   ? 14.087 1.757   -0.473  0.66 12.87 ?  201 A1A6Z A C2   1 
HETATM 6977 C C4   B A1A6Z C 2 .   ? 14.485 0.283   -0.640  0.66 13.38 ?  201 A1A6Z A C4   1 
HETATM 6978 C C5   B A1A6Z C 2 .   ? 14.889 -0.210  0.773   0.66 12.14 ?  201 A1A6Z A C5   1 
HETATM 6979 C C7   B A1A6Z C 2 .   ? 15.112 0.991   3.020   0.66 10.81 ?  201 A1A6Z A C7   1 
HETATM 6980 C C8   B A1A6Z C 2 .   ? 14.941 -0.194  5.040   0.66 10.81 ?  201 A1A6Z A C8   1 
HETATM 6981 N N1   B A1A6Z C 2 .   ? 15.115 0.985   1.607   0.66 10.80 ?  201 A1A6Z A N1   1 
HETATM 6982 N N3   B A1A6Z C 2 .   ? 15.106 0.864   5.868   0.66 11.05 ?  201 A1A6Z A N3   1 
HETATM 6983 N N4   B A1A6Z C 2 .   ? 15.500 3.250   5.806   0.66 9.87  ?  201 A1A6Z A N4   1 
HETATM 6984 O O1   B A1A6Z C 2 .   ? 15.779 -2.241  -0.075  0.66 14.78 ?  201 A1A6Z A O1   1 
HETATM 6985 H H6   B A1A6Z C 2 .   ? 11.917 1.534   -0.950  0.66 17.13 ?  201 A1A6Z A H6   1 
HETATM 6986 H H7   B A1A6Z C 2 .   ? 12.286 2.875   0.132   0.66 17.13 ?  201 A1A6Z A H7   1 
HETATM 6987 H H5   B A1A6Z C 2 .   ? 12.281 1.223   0.741   0.66 17.13 ?  201 A1A6Z A H5   1 
HETATM 6988 H H11  B A1A6Z C 2 .   ? 16.983 -0.533  0.169   0.66 15.11 ?  201 A1A6Z A H11  1 
HETATM 6989 H H10  B A1A6Z C 2 .   ? 16.500 -1.383  1.691   0.66 15.11 ?  201 A1A6Z A H10  1 
HETATM 6990 H H15  B A1A6Z C 2 .   ? 15.821 5.246   5.177   0.66 11.75 ?  201 A1A6Z A H15  1 
HETATM 6991 H H2   B A1A6Z C 2 .   ? 13.827 2.265   -2.653  0.66 16.82 ?  201 A1A6Z A H2   1 
HETATM 6992 H H4   B A1A6Z C 2 .   ? 15.445 2.584   -2.051  0.66 16.82 ?  201 A1A6Z A H4   1 
HETATM 6993 H H3   B A1A6Z C 2 .   ? 14.122 3.665   -1.638  0.66 16.82 ?  201 A1A6Z A H3   1 
HETATM 6994 H H14  B A1A6Z C 2 .   ? 15.641 4.197   2.677   0.66 12.20 ?  201 A1A6Z A H14  1 
HETATM 6995 H H18  B A1A6Z C 2 .   ? 14.413 3.039   1.269   0.66 14.00 ?  201 A1A6Z A H18  1 
HETATM 6996 H H17  B A1A6Z C 2 .   ? 15.905 2.614   0.401   0.66 14.00 ?  201 A1A6Z A H17  1 
HETATM 6997 H H9   B A1A6Z C 2 .   ? 15.305 0.153   -1.377  0.66 16.20 ?  201 A1A6Z A H9   1 
HETATM 6998 H H8   B A1A6Z C 2 .   ? 13.646 -0.330  -1.069  0.66 16.20 ?  201 A1A6Z A H8   1 
HETATM 6999 H H1   B A1A6Z C 2 .   ? 14.044 -0.802  1.213   0.66 14.72 ?  201 A1A6Z A H1   1 
HETATM 7000 H H13  B A1A6Z C 2 .   ? 14.780 -1.150  5.614   0.66 13.12 ?  201 A1A6Z A H13  1 
HETATM 7001 H H16  B A1A6Z C 2 .   ? 15.525 3.385   6.829   0.66 11.99 ?  201 A1A6Z A H16  1 
HETATM 7002 H H12  B A1A6Z C 2 .   ? 16.493 -2.902  0.039   0.66 17.88 ?  201 A1A6Z A H12  1 
HETATM 7003 O O    . HOH   D 3 .   ? 14.335 -4.678  -12.027 1.00 46.74 ?  301 HOH   A O    1 
HETATM 7004 O O    . HOH   D 3 .   ? 7.617  -6.273  -6.614  1.00 48.23 ?  302 HOH   A O    1 
HETATM 7005 O O    . HOH   D 3 .   ? 28.962 0.329   -9.887  1.00 21.70 ?  303 HOH   A O    1 
HETATM 7006 O O    A HOH   D 3 .   ? 14.825 -4.615  20.379  0.34 30.09 ?  304 HOH   A O    1 
HETATM 7007 O O    . HOH   D 3 .   ? 3.785  -9.542  9.700   1.00 38.68 ?  305 HOH   A O    1 
HETATM 7008 O O    . HOH   D 3 .   ? 4.754  3.778   0.452   1.00 38.32 ?  306 HOH   A O    1 
HETATM 7009 O O    . HOH   D 3 .   ? 25.902 -1.034  -7.707  1.00 22.69 ?  307 HOH   A O    1 
HETATM 7010 O O    . HOH   D 3 .   ? 14.703 -13.803 16.748  1.00 26.78 ?  308 HOH   A O    1 
HETATM 7011 O O    . HOH   D 3 .   ? 28.513 -0.290  -13.546 1.00 36.99 ?  309 HOH   A O    1 
HETATM 7012 O O    . HOH   D 3 .   ? 10.877 1.696   12.079  1.00 21.99 ?  310 HOH   A O    1 
HETATM 7013 O O    . HOH   D 3 .   ? 34.401 -1.816  12.503  1.00 36.84 ?  311 HOH   A O    1 
HETATM 7014 O O    . HOH   D 3 .   ? 15.096 -12.187 18.553  1.00 45.62 ?  312 HOH   A O    1 
HETATM 7015 O O    . HOH   D 3 .   ? 22.614 -12.003 21.940  1.00 59.87 ?  313 HOH   A O    1 
HETATM 7016 O O    . HOH   D 3 .   ? 10.328 -22.203 -1.254  1.00 53.73 ?  314 HOH   A O    1 
HETATM 7017 O O    . HOH   D 3 .   ? 22.281 5.258   18.920  1.00 49.95 ?  315 HOH   A O    1 
HETATM 7018 O O    B HOH   D 3 .   ? 18.689 -1.985  -1.469  0.66 30.46 ?  316 HOH   A O    1 
HETATM 7019 O O    . HOH   D 3 .   ? 17.237 -18.008 14.946  1.00 32.29 ?  317 HOH   A O    1 
HETATM 7020 O O    . HOH   D 3 .   ? 28.211 -6.251  19.573  1.00 44.36 ?  318 HOH   A O    1 
HETATM 7021 O O    . HOH   D 3 .   ? 0.791  -4.698  -0.086  1.00 39.08 ?  319 HOH   A O    1 
HETATM 7022 O O    . HOH   D 3 .   ? 14.892 3.907   17.396  1.00 39.98 ?  320 HOH   A O    1 
HETATM 7023 O O    . HOH   D 3 .   ? 30.353 -13.299 -8.478  1.00 22.67 ?  321 HOH   A O    1 
HETATM 7024 O O    . HOH   D 3 .   ? 42.328 10.584  5.018   1.00 19.91 ?  322 HOH   A O    1 
HETATM 7025 O O    . HOH   D 3 .   ? -0.916 -8.734  2.064   1.00 42.85 ?  323 HOH   A O    1 
HETATM 7026 O O    . HOH   D 3 .   ? 9.306  -10.090 19.364  1.00 44.70 ?  324 HOH   A O    1 
HETATM 7027 O O    . HOH   D 3 .   ? 23.988 -15.862 -9.118  1.00 38.22 ?  325 HOH   A O    1 
HETATM 7028 O O    . HOH   D 3 .   ? 11.830 0.431   14.540  1.00 36.63 ?  326 HOH   A O    1 
HETATM 7029 O O    . HOH   D 3 .   ? 8.055  -12.893 -1.322  1.00 24.68 ?  327 HOH   A O    1 
HETATM 7030 O O    . HOH   D 3 .   ? 10.107 -21.445 5.679   1.00 21.86 ?  328 HOH   A O    1 
HETATM 7031 O O    . HOH   D 3 .   ? 27.345 13.789  2.862   1.00 27.75 ?  329 HOH   A O    1 
HETATM 7032 O O    . HOH   D 3 .   ? 20.189 -12.757 -8.690  1.00 26.75 ?  330 HOH   A O    1 
HETATM 7033 O O    A HOH   D 3 .   ? 14.692 -3.689  3.055   0.34 19.67 ?  331 HOH   A O    1 
HETATM 7034 O O    A HOH   D 3 .   ? 17.554 -1.749  0.401   0.34 31.15 ?  332 HOH   A O    1 
HETATM 7035 O O    . HOH   D 3 .   ? 5.293  2.397   4.936   1.00 35.68 ?  333 HOH   A O    1 
HETATM 7036 O O    . HOH   D 3 .   ? 19.098 -21.992 6.873   1.00 35.03 ?  334 HOH   A O    1 
HETATM 7037 O O    . HOH   D 3 .   ? 44.277 7.201   6.402   1.00 27.21 ?  335 HOH   A O    1 
HETATM 7038 O O    . HOH   D 3 .   ? 18.731 -19.298 13.616  1.00 34.38 ?  336 HOH   A O    1 
HETATM 7039 O O    . HOH   D 3 .   ? 31.103 -18.100 7.828   1.00 19.36 ?  337 HOH   A O    1 
HETATM 7040 O O    . HOH   D 3 .   ? 34.040 -1.167  -8.931  1.00 26.30 ?  338 HOH   A O    1 
HETATM 7041 O O    . HOH   D 3 .   ? 36.304 -5.091  -0.478  1.00 35.05 ?  339 HOH   A O    1 
HETATM 7042 O O    . HOH   D 3 .   ? 22.237 -19.316 11.367  1.00 36.03 ?  340 HOH   A O    1 
HETATM 7043 O O    . HOH   D 3 .   ? 37.518 2.852   10.259  1.00 25.74 ?  341 HOH   A O    1 
HETATM 7044 O O    . HOH   D 3 .   ? 11.865 -10.975 -10.035 1.00 54.52 ?  342 HOH   A O    1 
HETATM 7045 O O    . HOH   D 3 .   ? 38.530 4.998   6.973   1.00 14.97 ?  343 HOH   A O    1 
HETATM 7046 O O    . HOH   D 3 .   ? 38.271 10.348  7.031   1.00 44.96 ?  344 HOH   A O    1 
HETATM 7047 O O    B HOH   D 3 .   ? 9.122  2.007   7.473   0.66 24.41 ?  345 HOH   A O    1 
HETATM 7048 O O    B HOH   D 3 .   ? 14.975 -2.813  3.016   0.66 12.83 ?  346 HOH   A O    1 
HETATM 7049 O O    . HOH   D 3 .   ? 14.583 -21.385 -4.239  1.00 29.29 ?  347 HOH   A O    1 
HETATM 7050 O O    . HOH   D 3 .   ? 22.745 12.504  1.565   1.00 14.32 ?  348 HOH   A O    1 
HETATM 7051 O O    . HOH   D 3 .   ? 21.233 10.106  14.992  1.00 34.77 ?  349 HOH   A O    1 
HETATM 7052 O O    . HOH   D 3 .   ? 43.309 7.770   2.689   1.00 26.12 ?  350 HOH   A O    1 
HETATM 7053 O O    B HOH   D 3 .   ? 15.197 6.816   7.075   0.66 16.62 ?  351 HOH   A O    1 
HETATM 7054 O O    . HOH   D 3 .   ? 26.801 -3.048  19.603  1.00 37.85 ?  352 HOH   A O    1 
HETATM 7055 O O    . HOH   D 3 .   ? 26.825 11.426  1.644   1.00 15.61 ?  353 HOH   A O    1 
HETATM 7056 O O    . HOH   D 3 .   ? 20.721 -19.775 -5.095  1.00 28.84 ?  354 HOH   A O    1 
HETATM 7057 O O    . HOH   D 3 .   ? 30.761 3.091   8.260   1.00 11.68 ?  355 HOH   A O    1 
HETATM 7058 O O    B HOH   D 3 .   ? 10.848 -1.205  1.462   0.66 15.90 ?  356 HOH   A O    1 
HETATM 7059 O O    . HOH   D 3 .   ? 39.760 -1.041  -5.183  1.00 20.65 ?  357 HOH   A O    1 
HETATM 7060 O O    . HOH   D 3 .   ? 30.820 6.282   -12.249 1.00 24.68 ?  358 HOH   A O    1 
HETATM 7061 O O    . HOH   D 3 .   ? 42.513 4.293   5.407   1.00 33.24 ?  359 HOH   A O    1 
HETATM 7062 O O    . HOH   D 3 .   ? 18.502 9.491   8.895   1.00 22.11 ?  360 HOH   A O    1 
HETATM 7063 O O    B HOH   D 3 .   ? 11.035 6.361   8.808   0.66 22.62 ?  361 HOH   A O    1 
HETATM 7064 O O    . HOH   D 3 .   ? 31.195 -13.960 -2.432  1.00 13.26 ?  362 HOH   A O    1 
HETATM 7065 O O    A HOH   D 3 .   ? 14.324 0.542   6.752   0.34 30.37 ?  363 HOH   A O    1 
HETATM 7066 O O    . HOH   D 3 .   ? 24.101 -2.189  -2.284  1.00 11.98 ?  364 HOH   A O    1 
HETATM 7067 O O    A HOH   D 3 .   ? 6.999  -8.193  11.801  0.34 14.82 ?  365 HOH   A O    1 
HETATM 7068 O O    . HOH   D 3 .   ? 35.862 -12.624 6.882   1.00 15.40 ?  366 HOH   A O    1 
HETATM 7069 O O    . HOH   D 3 .   ? 13.673 -15.446 -7.705  1.00 31.98 ?  367 HOH   A O    1 
HETATM 7070 O O    . HOH   D 3 .   ? 16.732 -22.119 0.955   1.00 30.65 ?  368 HOH   A O    1 
HETATM 7071 O O    . HOH   D 3 .   ? 26.939 4.125   -0.728  1.00 12.22 ?  369 HOH   A O    1 
HETATM 7072 O O    . HOH   D 3 .   ? 15.338 -8.277  -9.986  1.00 35.04 ?  370 HOH   A O    1 
HETATM 7073 O O    . HOH   D 3 .   ? 16.246 16.644  8.614   1.00 44.84 ?  371 HOH   A O    1 
HETATM 7074 O O    . HOH   D 3 .   ? 37.245 12.012  4.931   1.00 26.53 ?  372 HOH   A O    1 
HETATM 7075 O O    . HOH   D 3 .   ? 37.218 -2.996  9.683   1.00 49.13 ?  373 HOH   A O    1 
HETATM 7076 O O    . HOH   D 3 .   ? 31.652 8.242   14.856  1.00 24.40 ?  374 HOH   A O    1 
HETATM 7077 O O    . HOH   D 3 .   ? 17.154 -19.312 4.874   1.00 15.37 ?  375 HOH   A O    1 
HETATM 7078 O O    . HOH   D 3 .   ? 21.927 -21.895 8.532   1.00 27.60 ?  376 HOH   A O    1 
HETATM 7079 O O    . HOH   D 3 .   ? 33.692 -7.132  4.319   1.00 15.87 ?  377 HOH   A O    1 
HETATM 7080 O O    A HOH   D 3 .   ? 21.308 -2.431  -2.087  0.34 14.67 ?  378 HOH   A O    1 
HETATM 7081 O O    . HOH   D 3 .   ? 27.453 -10.523 14.109  1.00 17.04 ?  379 HOH   A O    1 
HETATM 7082 O O    A HOH   D 3 .   ? 20.161 4.501   -7.591  0.34 27.46 ?  380 HOH   A O    1 
HETATM 7083 O O    . HOH   D 3 .   ? 28.721 -10.632 -14.102 1.00 44.41 ?  381 HOH   A O    1 
HETATM 7084 O O    . HOH   D 3 .   ? 32.122 -7.349  -9.736  1.00 21.14 ?  382 HOH   A O    1 
HETATM 7085 O O    A HOH   D 3 .   ? -0.421 -3.140  3.038   0.34 26.20 ?  383 HOH   A O    1 
HETATM 7086 O O    . HOH   D 3 .   ? 43.927 8.507   -3.035  1.00 31.37 ?  384 HOH   A O    1 
HETATM 7087 O O    . HOH   D 3 .   ? 15.293 -21.502 14.265  1.00 18.86 ?  385 HOH   A O    1 
HETATM 7088 O O    B HOH   D 3 .   ? 21.190 2.695   0.011   0.66 11.33 ?  386 HOH   A O    1 
HETATM 7089 O O    . HOH   D 3 .   ? 8.802  -11.834 17.197  1.00 31.12 ?  387 HOH   A O    1 
HETATM 7090 O O    . HOH   D 3 .   ? 30.558 1.919   16.721  1.00 20.89 ?  388 HOH   A O    1 
HETATM 7091 O O    . HOH   D 3 .   ? 8.248  -21.590 4.038   1.00 54.39 ?  389 HOH   A O    1 
HETATM 7092 O O    . HOH   D 3 .   ? 17.367 -17.939 -5.129  1.00 31.91 ?  390 HOH   A O    1 
HETATM 7093 O O    . HOH   D 3 .   ? 24.208 -7.711  14.428  1.00 16.44 ?  391 HOH   A O    1 
HETATM 7094 O O    B HOH   D 3 .   ? 13.315 -3.118  -1.088  0.66 22.57 ?  392 HOH   A O    1 
HETATM 7095 O O    . HOH   D 3 .   ? 13.710 -4.647  17.128  1.00 26.49 ?  393 HOH   A O    1 
HETATM 7096 O O    A HOH   D 3 .   ? 21.403 3.123   -0.391  0.34 8.62  ?  394 HOH   A O    1 
HETATM 7097 O O    . HOH   D 3 .   ? 20.651 -20.012 2.830   1.00 19.26 ?  395 HOH   A O    1 
HETATM 7098 O O    . HOH   D 3 .   ? 24.349 3.587   -1.820  1.00 19.48 ?  396 HOH   A O    1 
HETATM 7099 O O    A HOH   D 3 .   ? 24.647 2.004   -7.024  0.34 19.07 ?  397 HOH   A O    1 
HETATM 7100 O O    A HOH   D 3 .   ? 6.515  -5.638  11.127  0.34 16.11 ?  398 HOH   A O    1 
HETATM 7101 O O    . HOH   D 3 .   ? 14.350 -0.275  -12.450 1.00 48.86 ?  399 HOH   A O    1 
HETATM 7102 O O    . HOH   D 3 .   ? 9.659  -16.610 -2.042  1.00 49.92 ?  400 HOH   A O    1 
HETATM 7103 O O    B HOH   D 3 .   ? 21.268 -2.019  -2.963  0.66 16.82 ?  401 HOH   A O    1 
HETATM 7104 O O    . HOH   D 3 .   ? 15.753 2.233   24.494  1.00 60.09 ?  402 HOH   A O    1 
HETATM 7105 O O    . HOH   D 3 .   ? 38.088 -1.320  -1.902  1.00 17.88 ?  403 HOH   A O    1 
HETATM 7106 O O    . HOH   D 3 .   ? 13.544 -1.540  -7.028  1.00 25.69 ?  404 HOH   A O    1 
HETATM 7107 O O    . HOH   D 3 .   ? 41.020 -8.295  -6.759  1.00 38.18 ?  405 HOH   A O    1 
HETATM 7108 O O    A HOH   D 3 .   ? 18.652 -2.516  -16.377 0.34 25.39 ?  406 HOH   A O    1 
HETATM 7109 O O    . HOH   D 3 .   ? 32.810 -9.253  5.941   1.00 20.11 ?  407 HOH   A O    1 
HETATM 7110 O O    . HOH   D 3 .   ? 24.766 -17.530 12.708  1.00 23.49 ?  408 HOH   A O    1 
HETATM 7111 O O    . HOH   D 3 .   ? 37.541 -1.998  5.787   1.00 25.92 ?  409 HOH   A O    1 
HETATM 7112 O O    . HOH   D 3 .   ? 27.918 0.781   -7.294  1.00 15.07 ?  410 HOH   A O    1 
HETATM 7113 O O    . HOH   D 3 .   ? 10.584 -13.948 -1.961  1.00 20.55 ?  411 HOH   A O    1 
HETATM 7114 O O    . HOH   D 3 .   ? 18.451 -15.875 16.103  1.00 37.25 ?  412 HOH   A O    1 
HETATM 7115 O O    . HOH   D 3 .   ? 23.475 11.425  4.011   1.00 12.20 ?  413 HOH   A O    1 
HETATM 7116 O O    . HOH   D 3 .   ? 27.767 -6.438  -14.143 1.00 34.19 ?  414 HOH   A O    1 
HETATM 7117 O O    A HOH   D 3 .   ? 15.852 -0.976  5.226   0.34 35.14 ?  415 HOH   A O    1 
HETATM 7118 O O    . HOH   D 3 .   ? 14.212 -23.119 7.421   1.00 19.61 ?  416 HOH   A O    1 
HETATM 7119 O O    . HOH   D 3 .   ? 16.293 -14.174 20.284  1.00 54.66 ?  417 HOH   A O    1 
HETATM 7120 O O    . HOH   D 3 .   ? 27.119 2.407   18.670  1.00 35.07 ?  418 HOH   A O    1 
HETATM 7121 O O    . HOH   D 3 .   ? -1.413 -5.034  7.423   1.00 50.20 ?  419 HOH   A O    1 
HETATM 7122 O O    . HOH   D 3 .   ? 11.797 -10.609 16.939  1.00 27.54 ?  420 HOH   A O    1 
HETATM 7123 O O    . HOH   D 3 .   ? 22.593 8.263   18.361  1.00 51.53 ?  421 HOH   A O    1 
HETATM 7124 O O    . HOH   D 3 .   ? 30.363 -12.854 13.574  1.00 19.87 ?  422 HOH   A O    1 
HETATM 7125 O O    . HOH   D 3 .   ? 35.164 -5.256  -3.038  1.00 19.13 ?  423 HOH   A O    1 
HETATM 7126 O O    . HOH   D 3 .   ? 32.623 -10.655 3.195   1.00 31.17 ?  424 HOH   A O    1 
HETATM 7127 O O    . HOH   D 3 .   ? 23.950 3.965   -4.813  1.00 32.52 ?  425 HOH   A O    1 
HETATM 7128 O O    . HOH   D 3 .   ? 15.412 11.857  7.772   1.00 42.98 ?  426 HOH   A O    1 
HETATM 7129 O O    . HOH   D 3 .   ? 14.458 -24.714 11.526  1.00 41.65 ?  427 HOH   A O    1 
HETATM 7130 O O    . HOH   D 3 .   ? 41.654 1.486   4.998   1.00 37.80 ?  428 HOH   A O    1 
HETATM 7131 O O    A HOH   D 3 .   ? 11.122 -0.419  1.883   0.34 24.27 ?  429 HOH   A O    1 
HETATM 7132 O O    . HOH   D 3 .   ? 30.076 -10.049 13.074  1.00 24.68 ?  430 HOH   A O    1 
HETATM 7133 O O    . HOH   D 3 .   ? 18.957 -10.606 24.107  1.00 87.58 ?  431 HOH   A O    1 
HETATM 7134 O O    . HOH   D 3 .   ? 32.893 -4.574  -9.917  1.00 27.63 ?  432 HOH   A O    1 
HETATM 7135 O O    . HOH   D 3 .   ? 16.068 7.042   2.804   1.00 17.19 ?  433 HOH   A O    1 
HETATM 7136 O O    . HOH   D 3 .   ? 24.055 -20.296 -1.306  1.00 17.88 ?  434 HOH   A O    1 
HETATM 7137 O O    . HOH   D 3 .   ? 36.746 -4.978  5.402   1.00 25.12 ?  435 HOH   A O    1 
HETATM 7138 O O    A HOH   D 3 .   ? 18.919 1.998   -0.795  0.34 11.94 ?  436 HOH   A O    1 
HETATM 7139 O O    . HOH   D 3 .   ? 21.907 -14.075 -8.312  1.00 62.41 ?  437 HOH   A O    1 
HETATM 7140 O O    . HOH   D 3 .   ? 29.883 -2.061  -12.827 1.00 56.09 ?  438 HOH   A O    1 
HETATM 7141 O O    B HOH   D 3 .   ? 7.379  3.548   4.140   0.66 22.89 ?  439 HOH   A O    1 
HETATM 7142 O O    . HOH   D 3 .   ? 18.637 4.822   -15.072 1.00 64.24 ?  440 HOH   A O    1 
HETATM 7143 O O    A HOH   D 3 .   ? 19.018 -0.705  -1.666  0.34 18.42 ?  441 HOH   A O    1 
HETATM 7144 O O    . HOH   D 3 .   ? 37.859 -8.849  -3.450  1.00 23.44 ?  442 HOH   A O    1 
HETATM 7145 O O    B HOH   D 3 .   ? 19.145 -0.353  -3.892  0.66 28.65 ?  443 HOH   A O    1 
HETATM 7146 O O    . HOH   D 3 .   ? 6.531  -3.570  12.768  1.00 34.40 ?  444 HOH   A O    1 
HETATM 7147 O O    . HOH   D 3 .   ? 23.471 -20.975 1.349   1.00 18.48 ?  445 HOH   A O    1 
HETATM 7148 O O    . HOH   D 3 .   ? 45.119 -0.582  2.991   1.00 39.30 ?  446 HOH   A O    1 
HETATM 7149 O O    . HOH   D 3 .   ? 20.547 -17.687 24.802  1.00 57.59 ?  447 HOH   A O    1 
HETATM 7150 O O    . HOH   D 3 .   ? 23.447 -7.983  17.051  1.00 22.51 ?  448 HOH   A O    1 
HETATM 7151 O O    . HOH   D 3 .   ? 21.553 -14.720 17.826  1.00 57.02 ?  449 HOH   A O    1 
HETATM 7152 O O    . HOH   D 3 .   ? 34.217 -8.369  -0.351  1.00 30.31 ?  450 HOH   A O    1 
HETATM 7153 O O    . HOH   D 3 .   ? 31.405 -12.830 0.008   1.00 19.25 ?  451 HOH   A O    1 
HETATM 7154 O O    A HOH   D 3 .   ? 16.314 2.909   -1.489  0.34 33.17 ?  452 HOH   A O    1 
HETATM 7155 O O    A HOH   D 3 .   ? 14.081 -0.373  3.415   0.34 39.48 ?  453 HOH   A O    1 
HETATM 7156 O O    . HOH   D 3 .   ? 23.245 7.486   -3.407  1.00 37.96 ?  454 HOH   A O    1 
HETATM 7157 O O    B HOH   D 3 .   ? 18.303 1.890   -0.474  0.66 16.46 ?  455 HOH   A O    1 
HETATM 7158 O O    . HOH   D 3 .   ? 30.572 14.757  2.718   1.00 18.78 ?  456 HOH   A O    1 
HETATM 7159 O O    B HOH   D 3 .   ? 20.630 4.266   -2.532  0.66 32.95 ?  457 HOH   A O    1 
HETATM 7160 O O    . HOH   D 3 .   ? 29.796 -15.961 10.764  1.00 32.95 ?  458 HOH   A O    1 
HETATM 7161 O O    . HOH   D 3 .   ? 21.544 -9.007  21.355  1.00 58.48 ?  459 HOH   A O    1 
HETATM 7162 O O    . HOH   D 3 .   ? 20.085 -17.515 -4.970  1.00 28.79 ?  460 HOH   A O    1 
HETATM 7163 O O    . HOH   D 3 .   ? 25.501 8.417   -4.811  1.00 31.29 ?  461 HOH   A O    1 
HETATM 7164 O O    . HOH   D 3 .   ? 32.392 -15.927 10.900  1.00 30.37 ?  462 HOH   A O    1 
HETATM 7165 O O    . HOH   D 3 .   ? 24.819 5.619   20.621  1.00 55.10 ?  463 HOH   A O    1 
HETATM 7166 O O    . HOH   D 3 .   ? 27.813 7.088   -6.674  1.00 40.85 ?  464 HOH   A O    1 
HETATM 7167 O O    . HOH   D 3 .   ? 24.743 14.629  7.679   1.00 33.98 ?  465 HOH   A O    1 
HETATM 7168 O O    . HOH   D 3 .   ? 23.312 -22.372 -3.275  1.00 36.63 ?  466 HOH   A O    1 
HETATM 7169 O O    B HOH   D 3 .   ? 12.638 -3.284  1.455   0.66 16.73 ?  467 HOH   A O    1 
HETATM 7170 O O    . HOH   D 3 .   ? 18.784 11.004  11.170  1.00 29.86 ?  468 HOH   A O    1 
HETATM 7171 O O    . HOH   D 3 .   ? 26.979 11.626  -1.274  1.00 34.91 ?  469 HOH   A O    1 
HETATM 7172 O O    . HOH   D 3 .   ? 12.052 -13.239 16.249  1.00 52.50 ?  470 HOH   A O    1 
HETATM 7173 O O    . HOH   D 3 .   ? 11.272 -15.182 -6.194  1.00 37.26 ?  471 HOH   A O    1 
HETATM 7174 O O    . HOH   D 3 .   ? 27.551 -11.392 16.596  1.00 41.63 ?  472 HOH   A O    1 
HETATM 7175 O O    . HOH   D 3 .   ? 39.855 -7.095  -3.472  1.00 41.96 ?  473 HOH   A O    1 
HETATM 7176 O O    . HOH   D 3 .   ? 23.474 13.723  5.490   1.00 19.16 ?  474 HOH   A O    1 
HETATM 7177 O O    . HOH   D 3 .   ? 16.004 -21.652 3.731   1.00 24.42 ?  475 HOH   A O    1 
HETATM 7178 O O    . HOH   D 3 .   ? 18.383 -16.396 -8.873  1.00 52.61 ?  476 HOH   A O    1 
HETATM 7179 O O    . HOH   D 3 .   ? 25.952 10.953  -3.610  1.00 26.95 ?  477 HOH   A O    1 
HETATM 7180 O O    . HOH   D 3 .   ? 12.241 1.572   17.149  1.00 40.28 ?  478 HOH   A O    1 
HETATM 7181 O O    A HOH   D 3 .   ? 22.024 5.229   -5.879  0.34 25.69 ?  479 HOH   A O    1 
HETATM 7182 O O    . HOH   D 3 .   ? 16.019 -17.379 -7.027  1.00 38.44 ?  480 HOH   A O    1 
HETATM 7183 O O    . HOH   D 3 .   ? 28.810 9.005   17.468  1.00 37.68 ?  481 HOH   A O    1 
HETATM 7184 O O    . HOH   D 3 .   ? 23.286 12.085  -4.030  1.00 24.33 ?  482 HOH   A O    1 
HETATM 7185 O O    . HOH   D 3 .   ? 28.723 -4.828  -12.331 1.00 43.15 ?  483 HOH   A O    1 
HETATM 7186 O O    . HOH   D 3 .   ? 35.148 7.485   12.195  1.00 46.75 ?  484 HOH   A O    1 
HETATM 7187 O O    . HOH   D 3 .   ? 16.197 -6.847  -11.938 1.00 55.08 ?  485 HOH   A O    1 
HETATM 7188 O O    . HOH   D 3 .   ? 41.089 -3.931  -0.326  1.00 37.34 ?  486 HOH   A O    1 
HETATM 7189 O O    . HOH   D 3 .   ? 30.789 0.704   19.196  1.00 40.45 ?  487 HOH   A O    1 
HETATM 7190 O O    . HOH   D 3 .   ? 17.450 -18.792 19.804  1.00 48.55 ?  488 HOH   A O    1 
HETATM 7191 O O    . HOH   D 3 .   ? 16.963 -20.494 16.152  1.00 34.66 ?  489 HOH   A O    1 
HETATM 7192 O O    . HOH   D 3 .   ? 44.487 10.423  -1.599  1.00 34.94 ?  490 HOH   A O    1 
HETATM 7193 O O    . HOH   D 3 .   ? 20.711 -15.987 -7.567  1.00 32.41 ?  491 HOH   A O    1 
HETATM 7194 O O    . HOH   D 3 .   ? 14.183 -10.382 -11.049 1.00 38.43 ?  492 HOH   A O    1 
HETATM 7195 O O    . HOH   D 3 .   ? 28.908 -8.061  -15.206 1.00 57.57 ?  493 HOH   A O    1 
HETATM 7196 O O    . HOH   D 3 .   ? 23.256 -13.004 19.280  1.00 57.61 ?  494 HOH   A O    1 
HETATM 7197 O O    . HOH   D 3 .   ? 39.190 2.424   7.375   1.00 32.52 ?  495 HOH   A O    1 
HETATM 7198 O O    . HOH   D 3 .   ? 41.689 9.421   -3.925  1.00 32.10 ?  496 HOH   A O    1 
HETATM 7199 O O    . HOH   D 3 .   ? 31.666 -0.608  -10.525 1.00 25.55 ?  497 HOH   A O    1 
HETATM 7200 O O    . HOH   D 3 .   ? 13.855 -25.194 8.923   1.00 39.17 ?  498 HOH   A O    1 
HETATM 7201 O O    . HOH   D 3 .   ? 18.558 -23.202 1.928   1.00 46.73 ?  499 HOH   A O    1 
HETATM 7202 O O    . HOH   D 3 .   ? 8.279  -3.051  -5.747  1.00 48.98 ?  500 HOH   A O    1 
HETATM 7203 O O    . HOH   D 3 .   ? 40.611 -0.225  -7.760  1.00 31.64 ?  501 HOH   A O    1 
HETATM 7204 O O    . HOH   D 3 .   ? 30.810 5.758   -14.726 1.00 37.67 ?  502 HOH   A O    1 
HETATM 7205 O O    . HOH   D 3 .   ? 16.305 -23.441 5.893   1.00 30.46 ?  503 HOH   A O    1 
HETATM 7206 O O    . HOH   D 3 .   ? 25.832 -18.948 -11.946 1.00 43.52 ?  504 HOH   A O    1 
HETATM 7207 O O    . HOH   D 3 .   ? 20.208 -22.381 4.237   1.00 29.74 ?  505 HOH   A O    1 
HETATM 7208 O O    . HOH   D 3 .   ? 30.842 -5.883  -11.935 1.00 54.98 ?  506 HOH   A O    1 
HETATM 7209 O O    B HOH   D 3 .   ? 14.653 8.006   4.977   0.66 17.88 ?  507 HOH   A O    1 
HETATM 7210 O O    . HOH   D 3 .   ? 23.400 -23.827 1.648   1.00 30.47 ?  508 HOH   A O    1 
HETATM 7211 O O    B HOH   D 3 .   ? 10.156 -0.432  -1.428  0.66 27.16 ?  509 HOH   A O    1 
HETATM 7212 O O    B HOH   D 3 .   ? 8.919  4.941   7.880   0.66 23.65 ?  510 HOH   A O    1 
HETATM 7213 O O    . HOH   D 3 .   ? 37.465 -6.627  7.508   1.00 22.81 ?  511 HOH   A O    1 
HETATM 7214 O O    . HOH   D 3 .   ? 39.535 -0.052  6.580   1.00 34.26 ?  512 HOH   A O    1 
HETATM 7215 O O    . HOH   D 3 .   ? 29.028 14.413  0.847   1.00 54.39 ?  513 HOH   A O    1 
HETATM 7216 O O    . HOH   D 3 .   ? 37.920 14.018  6.658   1.00 31.32 ?  514 HOH   A O    1 
HETATM 7217 O O    B HOH   D 3 .   ? 7.419  5.736   5.445   0.66 26.12 ?  515 HOH   A O    1 
HETATM 7218 O O    B HOH   D 3 .   ? 5.551  6.499   1.499   0.66 31.50 ?  516 HOH   A O    1 
HETATM 7219 O O    . HOH   D 3 .   ? 22.169 -24.076 4.506   1.00 25.73 ?  517 HOH   A O    1 
HETATM 7220 O O    . HOH   D 3 .   ? 36.530 -6.490  10.238  1.00 48.13 ?  518 HOH   A O    1 
HETATM 7221 O O    . HOH   D 3 .   ? 17.493 -7.258  -14.152 1.00 52.80 ?  519 HOH   A O    1 
HETATM 7222 O O    A HOH   D 3 .   ? 14.893 8.618   4.833   0.34 19.34 ?  520 HOH   A O    1 
HETATM 7223 O O    . HOH   D 3 .   ? 24.136 9.145   -7.198  1.00 42.30 ?  521 HOH   A O    1 
HETATM 7224 O O    . HOH   D 3 .   ? 15.795 -12.435 27.337  1.00 48.54 ?  522 HOH   A O    1 
HETATM 7225 O O    . HOH   D 3 .   ? 16.262 -21.191 18.753  1.00 48.07 ?  523 HOH   A O    1 
HETATM 7226 O O    B HOH   D 3 .   ? 8.268  7.229   2.091   0.66 29.05 ?  524 HOH   A O    1 
HETATM 7227 O O    . HOH   D 3 .   ? 14.749 -22.759 19.843  1.00 39.59 ?  525 HOH   A O    1 
HETATM 7228 O O    . HOH   E 3 .   ? 29.967 -22.432 5.553   1.00 20.01 ?  201 HOH   B O    1 
HETATM 7229 O O    . HOH   E 3 .   ? 27.751 -29.115 -1.871  1.00 37.01 ?  202 HOH   B O    1 
HETATM 7230 O O    . HOH   E 3 .   ? 41.737 -36.028 -17.177 1.00 33.72 ?  203 HOH   B O    1 
HETATM 7231 O O    . HOH   E 3 .   ? 49.440 -22.769 -19.731 1.00 43.54 ?  204 HOH   B O    1 
HETATM 7232 O O    . HOH   E 3 .   ? 38.094 -39.435 -0.100  1.00 37.43 ?  205 HOH   B O    1 
HETATM 7233 O O    . HOH   E 3 .   ? 59.212 -18.721 6.865   1.00 35.75 ?  206 HOH   B O    1 
HETATM 7234 O O    . HOH   E 3 .   ? 27.910 -41.810 -15.067 1.00 37.15 ?  207 HOH   B O    1 
HETATM 7235 O O    . HOH   E 3 .   ? 30.079 -26.325 4.156   1.00 28.39 ?  208 HOH   B O    1 
HETATM 7236 O O    . HOH   E 3 .   ? 31.064 -28.697 4.446   1.00 29.73 ?  209 HOH   B O    1 
HETATM 7237 O O    . HOH   E 3 .   ? 54.585 -9.466  -8.648  1.00 18.51 ?  210 HOH   B O    1 
HETATM 7238 O O    . HOH   E 3 .   ? 47.402 -7.421  -3.818  1.00 41.91 ?  211 HOH   B O    1 
HETATM 7239 O O    . HOH   E 3 .   ? 44.718 -7.207  2.050   1.00 36.25 ?  212 HOH   B O    1 
HETATM 7240 O O    . HOH   E 3 .   ? 58.313 -12.917 8.443   1.00 28.19 ?  213 HOH   B O    1 
HETATM 7241 O O    . HOH   E 3 .   ? 30.255 -41.015 -8.030  1.00 17.31 ?  214 HOH   B O    1 
HETATM 7242 O O    . HOH   E 3 .   ? 50.243 -3.413  7.108   1.00 32.14 ?  215 HOH   B O    1 
HETATM 7243 O O    . HOH   E 3 .   ? 41.533 -7.732  5.397   1.00 37.32 ?  216 HOH   B O    1 
HETATM 7244 O O    . HOH   E 3 .   ? 34.611 -36.420 -7.131  1.00 18.65 ?  217 HOH   B O    1 
HETATM 7245 O O    . HOH   E 3 .   ? 48.119 -7.029  15.512  1.00 34.35 ?  218 HOH   B O    1 
HETATM 7246 O O    . HOH   E 3 .   ? 56.767 -30.857 -7.769  1.00 27.33 ?  219 HOH   B O    1 
HETATM 7247 O O    . HOH   E 3 .   ? 34.975 -24.681 13.850  1.00 34.04 ?  220 HOH   B O    1 
HETATM 7248 O O    . HOH   E 3 .   ? 26.603 -19.348 -1.764  1.00 13.96 ?  221 HOH   B O    1 
HETATM 7249 O O    . HOH   E 3 .   ? 57.803 -24.513 5.080   1.00 39.03 ?  222 HOH   B O    1 
HETATM 7250 O O    . HOH   E 3 .   ? 53.159 -13.461 -20.360 1.00 34.13 ?  223 HOH   B O    1 
HETATM 7251 O O    . HOH   E 3 .   ? 57.484 -16.328 -12.199 1.00 17.95 ?  224 HOH   B O    1 
HETATM 7252 O O    . HOH   E 3 .   ? 44.990 -43.584 -10.518 1.00 27.31 ?  225 HOH   B O    1 
HETATM 7253 O O    . HOH   E 3 .   ? 41.539 -39.201 -14.844 1.00 22.83 ?  226 HOH   B O    1 
HETATM 7254 O O    . HOH   E 3 .   ? 56.484 -19.770 7.416   1.00 30.21 ?  227 HOH   B O    1 
HETATM 7255 O O    . HOH   E 3 .   ? 50.862 -6.107  0.189   1.00 25.68 ?  228 HOH   B O    1 
HETATM 7256 O O    . HOH   E 3 .   ? 51.741 -6.525  4.391   1.00 19.47 ?  229 HOH   B O    1 
HETATM 7257 O O    . HOH   E 3 .   ? 37.228 -19.750 -18.112 1.00 41.71 ?  230 HOH   B O    1 
HETATM 7258 O O    . HOH   E 3 .   ? 41.519 -9.638  13.057  1.00 21.33 ?  231 HOH   B O    1 
HETATM 7259 O O    . HOH   E 3 .   ? 40.632 -16.091 14.080  1.00 23.77 ?  232 HOH   B O    1 
HETATM 7260 O O    . HOH   E 3 .   ? 32.292 -9.271  -6.520  1.00 23.52 ?  233 HOH   B O    1 
HETATM 7261 O O    . HOH   E 3 .   ? 27.158 -31.818 -9.826  1.00 23.23 ?  234 HOH   B O    1 
HETATM 7262 O O    . HOH   E 3 .   ? 35.223 -8.036  -2.915  1.00 18.31 ?  235 HOH   B O    1 
HETATM 7263 O O    . HOH   E 3 .   ? 29.755 -34.106 -0.360  1.00 33.55 ?  236 HOH   B O    1 
HETATM 7264 O O    . HOH   E 3 .   ? 55.499 -16.559 -14.268 1.00 33.16 ?  237 HOH   B O    1 
HETATM 7265 O O    . HOH   E 3 .   ? 38.581 -11.063 -2.251  1.00 18.91 ?  238 HOH   B O    1 
HETATM 7266 O O    . HOH   E 3 .   ? 48.659 -36.562 -15.505 1.00 47.20 ?  239 HOH   B O    1 
HETATM 7267 O O    . HOH   E 3 .   ? 28.539 -19.653 -13.121 1.00 26.55 ?  240 HOH   B O    1 
HETATM 7268 O O    . HOH   E 3 .   ? 50.999 -39.982 -8.167  1.00 38.68 ?  241 HOH   B O    1 
HETATM 7269 O O    . HOH   E 3 .   ? 46.476 -1.540  13.166  1.00 27.08 ?  242 HOH   B O    1 
HETATM 7270 O O    . HOH   E 3 .   ? 44.628 -27.782 -0.653  1.00 21.06 ?  243 HOH   B O    1 
HETATM 7271 O O    . HOH   E 3 .   ? 36.061 -43.365 -8.362  1.00 40.87 ?  244 HOH   B O    1 
HETATM 7272 O O    . HOH   E 3 .   ? 39.643 -11.161 0.326   1.00 15.75 ?  245 HOH   B O    1 
HETATM 7273 O O    . HOH   E 3 .   ? 39.385 -10.805 6.107   1.00 23.06 ?  246 HOH   B O    1 
HETATM 7274 O O    . HOH   E 3 .   ? 32.829 -43.830 -11.298 1.00 22.22 ?  247 HOH   B O    1 
HETATM 7275 O O    . HOH   E 3 .   ? 25.484 -25.944 -1.198  1.00 33.49 ?  248 HOH   B O    1 
HETATM 7276 O O    . HOH   E 3 .   ? 50.865 -13.017 -0.427  1.00 11.24 ?  249 HOH   B O    1 
HETATM 7277 O O    . HOH   E 3 .   ? 42.676 -25.391 2.693   1.00 14.87 ?  250 HOH   B O    1 
HETATM 7278 O O    . HOH   E 3 .   ? 43.129 -43.287 -8.147  1.00 29.23 ?  251 HOH   B O    1 
HETATM 7279 O O    . HOH   E 3 .   ? 41.974 -23.582 9.340   1.00 18.33 ?  252 HOH   B O    1 
HETATM 7280 O O    . HOH   E 3 .   ? 33.651 -16.960 8.167   1.00 19.43 ?  253 HOH   B O    1 
HETATM 7281 O O    . HOH   E 3 .   ? 57.712 -24.446 -3.792  1.00 21.92 ?  254 HOH   B O    1 
HETATM 7282 O O    . HOH   E 3 .   ? 45.293 -34.937 6.766   1.00 38.25 ?  255 HOH   B O    1 
HETATM 7283 O O    . HOH   E 3 .   ? 58.290 -10.622 -4.040  1.00 19.98 ?  256 HOH   B O    1 
HETATM 7284 O O    . HOH   E 3 .   ? 28.328 -34.328 -9.281  1.00 19.94 ?  257 HOH   B O    1 
HETATM 7285 O O    . HOH   E 3 .   ? 40.493 -12.792 -11.502 1.00 14.93 ?  258 HOH   B O    1 
HETATM 7286 O O    . HOH   E 3 .   ? 29.806 -25.226 -10.734 1.00 16.77 ?  259 HOH   B O    1 
HETATM 7287 O O    . HOH   E 3 .   ? 51.631 -13.877 10.965  1.00 25.13 ?  260 HOH   B O    1 
HETATM 7288 O O    . HOH   E 3 .   ? 42.754 -22.896 3.929   1.00 11.50 ?  261 HOH   B O    1 
HETATM 7289 O O    . HOH   E 3 .   ? 34.306 -18.438 11.454  1.00 26.69 ?  262 HOH   B O    1 
HETATM 7290 O O    . HOH   E 3 .   ? 31.874 -17.883 -14.464 1.00 29.18 ?  263 HOH   B O    1 
HETATM 7291 O O    . HOH   E 3 .   ? 57.274 -12.105 12.287  1.00 37.26 ?  264 HOH   B O    1 
HETATM 7292 O O    . HOH   E 3 .   ? 30.958 -15.725 2.701   1.00 13.23 ?  265 HOH   B O    1 
HETATM 7293 O O    . HOH   E 3 .   ? 28.532 -30.882 -14.801 1.00 30.25 ?  266 HOH   B O    1 
HETATM 7294 O O    . HOH   E 3 .   ? 57.580 -9.260  1.429   1.00 18.61 ?  267 HOH   B O    1 
HETATM 7295 O O    . HOH   E 3 .   ? 51.731 -5.993  -7.979  1.00 44.79 ?  268 HOH   B O    1 
HETATM 7296 O O    . HOH   E 3 .   ? 57.291 -26.838 -7.571  1.00 43.68 ?  269 HOH   B O    1 
HETATM 7297 O O    . HOH   E 3 .   ? 48.104 -22.827 5.883   1.00 16.62 ?  270 HOH   B O    1 
HETATM 7298 O O    . HOH   E 3 .   ? 56.293 -23.609 -14.647 1.00 28.67 ?  271 HOH   B O    1 
HETATM 7299 O O    . HOH   E 3 .   ? 49.393 -28.746 -6.883  1.00 15.24 ?  272 HOH   B O    1 
HETATM 7300 O O    . HOH   E 3 .   ? 46.690 -31.307 -4.766  1.00 20.36 ?  273 HOH   B O    1 
HETATM 7301 O O    . HOH   E 3 .   ? 57.073 -8.631  8.415   1.00 18.46 ?  274 HOH   B O    1 
HETATM 7302 O O    . HOH   E 3 .   ? 30.569 -42.287 -10.592 1.00 30.91 ?  275 HOH   B O    1 
HETATM 7303 O O    . HOH   E 3 .   ? 43.186 -32.359 -17.094 1.00 23.96 ?  276 HOH   B O    1 
HETATM 7304 O O    . HOH   E 3 .   ? 43.514 -15.824 -12.153 1.00 14.10 ?  277 HOH   B O    1 
HETATM 7305 O O    . HOH   E 3 .   ? 42.459 -9.948  9.317   1.00 19.12 ?  278 HOH   B O    1 
HETATM 7306 O O    . HOH   E 3 .   ? 49.851 -0.489  10.187  1.00 27.38 ?  279 HOH   B O    1 
HETATM 7307 O O    . HOH   E 3 .   ? 41.250 -5.565  11.574  1.00 46.64 ?  280 HOH   B O    1 
HETATM 7308 O O    . HOH   E 3 .   ? 47.065 -29.539 9.805   1.00 32.94 ?  281 HOH   B O    1 
HETATM 7309 O O    . HOH   E 3 .   ? 38.996 -11.843 12.419  1.00 32.83 ?  282 HOH   B O    1 
HETATM 7310 O O    . HOH   E 3 .   ? 52.641 -10.378 12.972  1.00 22.32 ?  283 HOH   B O    1 
HETATM 7311 O O    . HOH   E 3 .   ? 35.003 -33.380 -19.126 1.00 28.23 ?  284 HOH   B O    1 
HETATM 7312 O O    . HOH   E 3 .   ? 34.566 -12.800 2.684   1.00 20.44 ?  285 HOH   B O    1 
HETATM 7313 O O    . HOH   E 3 .   ? 48.500 -25.084 3.127   1.00 13.11 ?  286 HOH   B O    1 
HETATM 7314 O O    . HOH   E 3 .   ? 28.063 -22.887 -7.932  1.00 17.42 ?  287 HOH   B O    1 
HETATM 7315 O O    . HOH   E 3 .   ? 36.922 -12.774 -1.501  1.00 24.34 ?  288 HOH   B O    1 
HETATM 7316 O O    . HOH   E 3 .   ? 48.062 -24.613 -17.768 1.00 31.74 ?  289 HOH   B O    1 
HETATM 7317 O O    . HOH   E 3 .   ? 50.035 -24.736 5.822   1.00 34.11 ?  290 HOH   B O    1 
HETATM 7318 O O    . HOH   E 3 .   ? 33.655 -15.357 -13.925 1.00 20.92 ?  291 HOH   B O    1 
HETATM 7319 O O    . HOH   E 3 .   ? 47.159 -34.036 -4.587  1.00 17.59 ?  292 HOH   B O    1 
HETATM 7320 O O    . HOH   E 3 .   ? 27.669 -26.652 -15.532 1.00 33.88 ?  293 HOH   B O    1 
HETATM 7321 O O    . HOH   E 3 .   ? 48.830 -20.057 5.975   1.00 13.42 ?  294 HOH   B O    1 
HETATM 7322 O O    . HOH   E 3 .   ? 42.531 -34.697 3.846   1.00 27.00 ?  295 HOH   B O    1 
HETATM 7323 O O    . HOH   E 3 .   ? 52.619 -35.735 -8.674  1.00 29.63 ?  296 HOH   B O    1 
HETATM 7324 O O    . HOH   E 3 .   ? 43.000 -20.292 -20.650 1.00 41.31 ?  297 HOH   B O    1 
HETATM 7325 O O    . HOH   E 3 .   ? 48.722 -12.124 -14.373 1.00 27.36 ?  298 HOH   B O    1 
HETATM 7326 O O    . HOH   E 3 .   ? 51.298 -37.653 -9.578  1.00 27.82 ?  299 HOH   B O    1 
HETATM 7327 O O    . HOH   E 3 .   ? 59.956 -15.320 8.235   1.00 32.71 ?  300 HOH   B O    1 
HETATM 7328 O O    . HOH   E 3 .   ? 45.344 -33.462 -15.908 1.00 23.74 ?  301 HOH   B O    1 
HETATM 7329 O O    . HOH   E 3 .   ? 37.537 -17.960 13.129  1.00 31.53 ?  302 HOH   B O    1 
HETATM 7330 O O    . HOH   E 3 .   ? 44.729 -27.491 2.078   1.00 15.10 ?  303 HOH   B O    1 
HETATM 7331 O O    . HOH   E 3 .   ? 45.804 -36.378 -16.117 1.00 37.22 ?  304 HOH   B O    1 
HETATM 7332 O O    . HOH   E 3 .   ? 42.567 -9.835  -14.820 1.00 35.16 ?  305 HOH   B O    1 
HETATM 7333 O O    . HOH   E 3 .   ? 45.898 -40.417 -3.543  1.00 31.21 ?  306 HOH   B O    1 
HETATM 7334 O O    . HOH   E 3 .   ? 42.915 -12.158 -18.437 1.00 27.66 ?  307 HOH   B O    1 
HETATM 7335 O O    . HOH   E 3 .   ? 35.163 -33.579 4.629   1.00 31.29 ?  308 HOH   B O    1 
HETATM 7336 O O    . HOH   E 3 .   ? 26.060 -21.494 -3.453  1.00 17.15 ?  309 HOH   B O    1 
HETATM 7337 O O    . HOH   E 3 .   ? 37.986 -10.275 -10.719 1.00 17.63 ?  310 HOH   B O    1 
HETATM 7338 O O    . HOH   E 3 .   ? 40.416 -10.888 -9.476  1.00 16.79 ?  311 HOH   B O    1 
HETATM 7339 O O    . HOH   E 3 .   ? 44.123 -29.399 -4.603  1.00 21.92 ?  312 HOH   B O    1 
HETATM 7340 O O    . HOH   E 3 .   ? 37.404 -35.691 7.273   1.00 33.46 ?  313 HOH   B O    1 
HETATM 7341 O O    . HOH   E 3 .   ? 62.822 -13.628 4.779   1.00 25.57 ?  314 HOH   B O    1 
HETATM 7342 O O    . HOH   E 3 .   ? 53.502 -30.277 4.592   1.00 17.95 ?  315 HOH   B O    1 
HETATM 7343 O O    . HOH   E 3 .   ? 53.082 -15.969 -12.760 1.00 25.28 ?  316 HOH   B O    1 
HETATM 7344 O O    . HOH   E 3 .   ? 43.326 -21.437 10.707  1.00 16.06 ?  317 HOH   B O    1 
HETATM 7345 O O    . HOH   E 3 .   ? 41.870 -8.103  1.396   1.00 23.96 ?  318 HOH   B O    1 
HETATM 7346 O O    . HOH   E 3 .   ? 57.634 -21.929 3.424   1.00 31.75 ?  319 HOH   B O    1 
HETATM 7347 O O    . HOH   E 3 .   ? 44.183 -1.784  7.775   1.00 45.73 ?  320 HOH   B O    1 
HETATM 7348 O O    . HOH   E 3 .   ? 53.804 -12.555 -22.205 1.00 36.80 ?  321 HOH   B O    1 
HETATM 7349 O O    . HOH   E 3 .   ? 32.897 -34.648 -5.822  1.00 17.33 ?  322 HOH   B O    1 
HETATM 7350 O O    . HOH   E 3 .   ? 52.648 -29.297 -13.031 1.00 24.84 ?  323 HOH   B O    1 
HETATM 7351 O O    . HOH   E 3 .   ? 48.224 -32.714 -16.591 1.00 43.95 ?  324 HOH   B O    1 
HETATM 7352 O O    . HOH   E 3 .   ? 38.438 -12.660 7.982   1.00 17.76 ?  325 HOH   B O    1 
HETATM 7353 O O    . HOH   E 3 .   ? 27.741 -14.771 -9.412  1.00 33.97 ?  326 HOH   B O    1 
HETATM 7354 O O    . HOH   E 3 .   ? 63.035 -20.175 -0.798  1.00 38.83 ?  327 HOH   B O    1 
HETATM 7355 O O    . HOH   E 3 .   ? 37.172 -30.614 -20.978 1.00 33.43 ?  328 HOH   B O    1 
HETATM 7356 O O    . HOH   E 3 .   ? 33.739 -31.087 11.150  1.00 38.17 ?  329 HOH   B O    1 
HETATM 7357 O O    . HOH   E 3 .   ? 44.796 -24.626 9.599   1.00 21.51 ?  330 HOH   B O    1 
HETATM 7358 O O    . HOH   E 3 .   ? 26.448 -21.068 -6.183  1.00 16.23 ?  331 HOH   B O    1 
HETATM 7359 O O    . HOH   E 3 .   ? 51.466 -33.074 -10.831 1.00 42.27 ?  332 HOH   B O    1 
HETATM 7360 O O    . HOH   E 3 .   ? 36.834 -12.410 4.297   1.00 17.15 ?  333 HOH   B O    1 
HETATM 7361 O O    . HOH   E 3 .   ? 43.217 -34.620 0.130   1.00 22.71 ?  334 HOH   B O    1 
HETATM 7362 O O    . HOH   E 3 .   ? 47.354 -24.503 8.197   1.00 27.09 ?  335 HOH   B O    1 
HETATM 7363 O O    . HOH   E 3 .   ? 38.510 -9.397  -13.265 1.00 28.64 ?  336 HOH   B O    1 
HETATM 7364 O O    . HOH   E 3 .   ? 39.693 -23.416 -20.321 1.00 36.67 ?  337 HOH   B O    1 
HETATM 7365 O O    . HOH   E 3 .   ? 41.452 -24.486 15.850  1.00 45.94 ?  338 HOH   B O    1 
HETATM 7366 O O    . HOH   E 3 .   ? 37.120 -15.172 -16.544 1.00 37.48 ?  339 HOH   B O    1 
HETATM 7367 O O    . HOH   E 3 .   ? 60.066 -17.350 -10.500 1.00 36.11 ?  340 HOH   B O    1 
HETATM 7368 O O    . HOH   E 3 .   ? 42.927 -43.532 -14.346 1.00 43.18 ?  341 HOH   B O    1 
HETATM 7369 O O    . HOH   E 3 .   ? 43.598 -15.399 18.128  1.00 27.27 ?  342 HOH   B O    1 
HETATM 7370 O O    . HOH   E 3 .   ? 47.560 -27.480 2.056   1.00 15.02 ?  343 HOH   B O    1 
HETATM 7371 O O    . HOH   E 3 .   ? 28.932 -42.894 -12.301 1.00 39.54 ?  344 HOH   B O    1 
HETATM 7372 O O    . HOH   E 3 .   ? 46.926 -19.948 12.240  1.00 29.90 ?  345 HOH   B O    1 
HETATM 7373 O O    . HOH   E 3 .   ? 34.542 -10.329 7.714   1.00 22.54 ?  346 HOH   B O    1 
HETATM 7374 O O    . HOH   E 3 .   ? 33.112 -14.705 1.131   1.00 18.34 ?  347 HOH   B O    1 
HETATM 7375 O O    . HOH   E 3 .   ? 39.825 -44.274 -11.147 1.00 44.12 ?  348 HOH   B O    1 
HETATM 7376 O O    . HOH   E 3 .   ? 44.225 -37.428 -17.697 1.00 34.60 ?  349 HOH   B O    1 
HETATM 7377 O O    . HOH   E 3 .   ? 40.465 -43.475 -9.083  1.00 25.33 ?  350 HOH   B O    1 
HETATM 7378 O O    . HOH   E 3 .   ? 38.574 -12.231 -16.194 1.00 43.83 ?  351 HOH   B O    1 
HETATM 7379 O O    . HOH   E 3 .   ? 37.131 -45.363 -9.599  1.00 39.58 ?  352 HOH   B O    1 
HETATM 7380 O O    . HOH   E 3 .   ? 27.932 -26.607 -0.505  1.00 30.25 ?  353 HOH   B O    1 
HETATM 7381 O O    . HOH   E 3 .   ? 62.648 -19.910 -4.804  1.00 53.77 ?  354 HOH   B O    1 
HETATM 7382 O O    . HOH   E 3 .   ? 38.604 -22.482 15.120  1.00 44.92 ?  355 HOH   B O    1 
HETATM 7383 O O    . HOH   E 3 .   ? 23.411 -23.725 6.836   1.00 33.89 ?  356 HOH   B O    1 
HETATM 7384 O O    . HOH   E 3 .   ? 33.974 -9.194  -8.850  1.00 28.61 ?  357 HOH   B O    1 
HETATM 7385 O O    . HOH   E 3 .   ? 55.800 -8.250  10.823  1.00 23.50 ?  358 HOH   B O    1 
HETATM 7386 O O    . HOH   E 3 .   ? 34.140 -7.790  11.501  1.00 40.03 ?  359 HOH   B O    1 
HETATM 7387 O O    . HOH   E 3 .   ? 56.680 -7.282  2.999   1.00 27.02 ?  360 HOH   B O    1 
HETATM 7388 O O    . HOH   E 3 .   ? 36.305 -8.534  -9.722  1.00 31.92 ?  361 HOH   B O    1 
HETATM 7389 O O    . HOH   E 3 .   ? 56.965 -21.580 -16.394 1.00 41.77 ?  362 HOH   B O    1 
HETATM 7390 O O    . HOH   E 3 .   ? 61.627 -19.919 1.827   1.00 39.84 ?  363 HOH   B O    1 
HETATM 7391 O O    . HOH   E 3 .   ? 40.338 -8.824  9.925   1.00 37.60 ?  364 HOH   B O    1 
HETATM 7392 O O    . HOH   E 3 .   ? 27.244 -25.906 -11.347 1.00 33.78 ?  365 HOH   B O    1 
HETATM 7393 O O    . HOH   E 3 .   ? 43.289 -12.739 -21.208 1.00 41.68 ?  366 HOH   B O    1 
HETATM 7394 O O    . HOH   E 3 .   ? 48.397 -26.476 8.834   1.00 44.00 ?  367 HOH   B O    1 
HETATM 7395 O O    . HOH   E 3 .   ? 40.376 -11.334 -13.932 1.00 32.37 ?  368 HOH   B O    1 
HETATM 7396 O O    . HOH   E 3 .   ? 36.229 -8.607  9.001   1.00 34.29 ?  369 HOH   B O    1 
HETATM 7397 O O    . HOH   E 3 .   ? 59.071 -10.463 9.218   1.00 40.33 ?  370 HOH   B O    1 
HETATM 7398 O O    . HOH   E 3 .   ? 32.747 -23.623 14.080  1.00 41.25 ?  371 HOH   B O    1 
HETATM 7399 O O    . HOH   E 3 .   ? 54.377 -5.813  2.938   1.00 35.65 ?  372 HOH   B O    1 
HETATM 7400 O O    . HOH   E 3 .   ? 39.992 -7.039  7.784   1.00 42.35 ?  373 HOH   B O    1 
HETATM 7401 O O    . HOH   E 3 .   ? 56.094 -7.872  -0.597  1.00 35.11 ?  374 HOH   B O    1 
HETATM 7402 O O    . HOH   E 3 .   ? 52.142 -12.975 13.359  1.00 27.58 ?  375 HOH   B O    1 
HETATM 7403 O O    . HOH   E 3 .   ? 41.952 -10.023 -17.470 1.00 57.02 ?  376 HOH   B O    1 
HETATM 7404 O O    . HOH   E 3 .   ? 63.064 -12.373 6.959   1.00 36.27 ?  377 HOH   B O    1 
HETATM 7405 O O    . HOH   E 3 .   ? 41.957 -6.759  -4.822  1.00 44.29 ?  378 HOH   B O    1 
HETATM 7406 O O    . HOH   E 3 .   ? 40.278 -7.742  3.136   1.00 40.67 ?  379 HOH   B O    1 
HETATM 7407 O O    . HOH   E 3 .   ? 36.641 -22.818 13.309  1.00 33.57 ?  380 HOH   B O    1 
HETATM 7408 O O    . HOH   E 3 .   ? 38.122 -10.486 10.021  1.00 27.16 ?  381 HOH   B O    1 
HETATM 7409 O O    . HOH   E 3 .   ? 42.767 -17.161 -23.177 1.00 42.70 ?  382 HOH   B O    1 
HETATM 7410 O O    . HOH   E 3 .   ? 39.699 -13.992 15.575  1.00 44.26 ?  383 HOH   B O    1 
HETATM 7411 O O    . HOH   E 3 .   ? 44.153 -5.629  -3.448  1.00 41.10 ?  384 HOH   B O    1 
HETATM 7412 O O    . HOH   E 3 .   ? 60.520 -22.282 2.901   1.00 40.47 ?  385 HOH   B O    1 
HETATM 7413 O O    . HOH   E 3 .   ? 46.805 -5.480  2.919   1.00 37.45 ?  386 HOH   B O    1 
HETATM 7414 O O    . HOH   E 3 .   ? 52.962 -29.954 7.251   1.00 23.03 ?  387 HOH   B O    1 
HETATM 7415 O O    . HOH   E 3 .   ? 35.361 -20.382 13.326  1.00 34.19 ?  388 HOH   B O    1 
HETATM 7416 O O    . HOH   E 3 .   ? 35.509 -33.774 7.431   1.00 41.92 ?  389 HOH   B O    1 
HETATM 7417 O O    . HOH   E 3 .   ? 24.040 -20.914 -7.693  1.00 26.74 ?  390 HOH   B O    1 
HETATM 7418 O O    . HOH   E 3 .   ? 41.025 -9.767  15.861  1.00 45.36 ?  391 HOH   B O    1 
HETATM 7419 O O    . HOH   E 3 .   ? 40.924 -6.575  -0.824  1.00 24.36 ?  392 HOH   B O    1 
HETATM 7420 O O    . HOH   E 3 .   ? 44.199 -31.855 -3.792  1.00 37.24 ?  393 HOH   B O    1 
HETATM 7421 O O    . HOH   E 3 .   ? 28.055 -27.023 2.360   1.00 31.95 ?  394 HOH   B O    1 
HETATM 7422 O O    . HOH   E 3 .   ? 26.735 -27.982 -13.438 1.00 36.73 ?  395 HOH   B O    1 
HETATM 7423 O O    . HOH   E 3 .   ? 50.708 -30.938 8.761   1.00 29.06 ?  396 HOH   B O    1 
HETATM 7424 O O    . HOH   E 3 .   ? 24.773 -20.612 -10.527 1.00 43.65 ?  397 HOH   B O    1 
HETATM 7425 O O    . HOH   E 3 .   ? 34.547 -33.484 9.651   1.00 38.71 ?  398 HOH   B O    1 
HETATM 7426 O O    . HOH   E 3 .   ? 26.897 -30.638 -12.552 1.00 28.57 ?  399 HOH   B O    1 
HETATM 7427 O O    . HOH   E 3 .   ? 57.636 -6.549  -2.354  1.00 32.30 ?  400 HOH   B O    1 
HETATM 7428 O O    . HOH   E 3 .   ? 45.747 -20.053 15.346  1.00 43.15 ?  401 HOH   B O    1 
HETATM 7429 O O    . HOH   E 3 .   ? 40.907 -11.861 -22.325 1.00 37.55 ?  402 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6715 0.6693 0.7727 0.0074  -0.0092 0.0405  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7135 0.6780 0.8048 -0.0019 -0.0140 0.0723  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6681 0.6658 0.7640 0.0065  -0.0086 0.0405  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7098 0.6733 0.7897 -0.0031 -0.0137 0.0730  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6510 0.6493 0.7256 0.0025  -0.0101 0.0417  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6917 0.6530 0.7384 -0.0096 -0.0167 0.0729  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6540 0.6522 0.7386 0.0034  -0.0107 0.0426  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6953 0.6567 0.7526 -0.0087 -0.0185 0.0732  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6785 0.6758 0.7851 0.0088  -0.0062 0.0396  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7205 0.6854 0.8138 0.0009  -0.0095 0.0729  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6820 0.6791 0.7913 0.0098  -0.0055 0.0394  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7241 0.6892 0.8218 0.0023  -0.0084 0.0733  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6819 0.6792 0.7911 0.0096  -0.0053 0.0394  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7242 0.6895 0.8218 0.0023  -0.0078 0.0731  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6279 0.6269 0.6663 -0.0030 -0.0100 0.0414  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6667 0.6252 0.6599 -0.0175 -0.0163 0.0727  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6020 0.6021 0.6003 -0.0089 -0.0092 0.0399  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6385 0.5947 0.5732 -0.0262 -0.0138 0.0702  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5636 0.5683 0.5646 -0.0179 -0.0013 0.0308  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5959 0.5581 0.5298 -0.0395 0.0101  0.0565  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5656 0.5698 0.5682 -0.0182 -0.0006 0.0311  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5988 0.5602 0.5293 -0.0401 0.0113  0.0574  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6118 0.6089 0.5652 -0.0062 -0.0147 0.0471  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6501 0.5988 0.5261 -0.0227 -0.0325 0.0822  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6191 0.6137 0.5333 -0.0043 -0.0192 0.0534  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6587 0.6010 0.4823 -0.0203 -0.0490 0.0921  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6219 0.6158 0.5227 -0.0039 -0.0209 0.0555  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6619 0.6015 0.4683 -0.0199 -0.0548 0.0950  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6215 0.6151 0.5244 -0.0034 -0.0208 0.0562  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6611 0.6012 0.4689 -0.0189 -0.0548 0.0977  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5209 0.5311 0.5199 -0.0272 0.0060  0.0218  5   SER   A N   
60   N N   B SER   A 5   ? 0.5476 0.5175 0.4823 -0.0531 0.0342  0.0436  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4765 0.4925 0.4732 -0.0360 0.0156  0.0136  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4965 0.4753 0.4357 -0.0664 0.0622  0.0326  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4280 0.4505 0.4207 -0.0424 0.0272  0.0102  5   SER   A C   
64   C C   B SER   A 5   ? 0.4392 0.4255 0.3678 -0.0756 0.0935  0.0294  5   SER   A C   
65   O O   A SER   A 5   ? 0.4298 0.4512 0.4189 -0.0428 0.0294  0.0087  5   SER   A O   
66   O O   B SER   A 5   ? 0.4411 0.4245 0.3508 -0.0789 0.1010  0.0201  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4798 0.4955 0.4808 -0.0375 0.0142  0.0104  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.5019 0.4819 0.4601 -0.0673 0.0606  0.0284  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4816 0.4969 0.4834 -0.0380 0.0134  0.0089  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.5052 0.4850 0.4752 -0.0673 0.0589  0.0258  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3766 0.4069 0.3673 -0.0473 0.0364  0.0100  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3790 0.3776 0.3119 -0.0803 0.1151  0.0345  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3256 0.3622 0.3144 -0.0511 0.0439  0.0127  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3184 0.3287 0.2687 -0.0835 0.1285  0.0449  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3064 0.3460 0.3065 -0.0603 0.0545  0.0117  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3094 0.3193 0.2829 -0.0804 0.1478  0.0392  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3077 0.3456 0.3151 -0.0644 0.0585  0.0120  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3178 0.3194 0.3119 -0.0729 0.1438  0.0452  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2964 0.3349 0.2736 -0.0428 0.0387  0.0130  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2777 0.2934 0.2356 -0.0785 0.0982  0.0488  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2709 0.3103 0.2422 -0.0339 0.0334  0.0128  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2421 0.2644 0.2203 -0.0712 0.0748  0.0428  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2600 0.2996 0.2245 -0.0282 0.0292  0.0120  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2292 0.2530 0.2141 -0.0628 0.0634  0.0451  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2620 0.3005 0.2359 -0.0274 0.0330  0.0118  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2367 0.2559 0.2401 -0.0641 0.0575  0.0367  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2549 0.2928 0.2209 -0.0260 0.0285  0.0135  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2228 0.2432 0.2178 -0.0638 0.0533  0.0418  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2572 0.2957 0.2336 -0.0239 0.0337  0.0139  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2310 0.2520 0.2503 -0.0598 0.0507  0.0328  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2550 0.2923 0.2261 -0.0238 0.0302  0.0124  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2260 0.2441 0.2382 -0.0631 0.0443  0.0314  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2861 0.3299 0.2930 -0.0638 0.0553  0.0103  7   SER   A N   
122  N N   B SER   A 7   ? 0.2932 0.3114 0.2862 -0.0755 0.1530  0.0189  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2699 0.3159 0.2840 -0.0610 0.0519  -0.0012 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2841 0.3074 0.3115 -0.0641 0.1414  -0.0070 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2469 0.2895 0.2692 -0.0582 0.0545  0.0025  7   SER   A C   
126  C C   B SER   A 7   ? 0.2496 0.2816 0.2936 -0.0707 0.1417  -0.0018 7   SER   A C   
127  O O   A SER   A 7   ? 0.2522 0.2878 0.2756 -0.0569 0.0532  0.0053  7   SER   A O   
128  O O   B SER   A 7   ? 0.2505 0.2750 0.2946 -0.0782 0.1349  0.0037  7   SER   A O   
129  C CB  A SER   A 7   ? 0.2765 0.3251 0.2864 -0.0607 0.0447  -0.0114 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3050 0.3279 0.3505 -0.0527 0.1294  -0.0265 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2863 0.3342 0.2958 -0.0589 0.0330  -0.0209 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3257 0.3446 0.3980 -0.0459 0.1090  -0.0362 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2257 0.2682 0.2552 -0.0532 0.0528  0.0014  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2268 0.2668 0.2930 -0.0623 0.1292  0.0010  8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2047 0.2472 0.2409 -0.0458 0.0588  0.0064  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2097 0.2468 0.2950 -0.0475 0.1105  0.0061  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1870 0.2301 0.2330 -0.0330 0.0548  0.0067  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1880 0.2279 0.2929 -0.0302 0.0917  0.0166  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1869 0.2341 0.2403 -0.0274 0.0518  -0.0039 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1819 0.2235 0.3073 -0.0192 0.0804  0.0058  8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1719 0.2107 0.2111 -0.0231 0.0561  0.0146  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1763 0.2157 0.2690 -0.0162 0.0849  0.0360  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1558 0.1914 0.1966 -0.0156 0.0490  0.0275  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1626 0.1981 0.2496 -0.0121 0.0671  0.0564  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1546 0.1777 0.2032 -0.0077 0.0513  0.0419  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1599 0.1867 0.2444 -0.0042 0.0635  0.0767  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1622 0.1892 0.2140 -0.0077 0.0477  0.0380  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1711 0.2058 0.2612 -0.0099 0.0541  0.0743  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1480 0.1900 0.1866 -0.0126 0.0438  0.0263  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1616 0.2024 0.2369 -0.0011 0.0595  0.0550  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1454 0.1937 0.1856 -0.0054 0.0437  0.0206  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1578 0.2060 0.2319 0.0031  0.0661  0.0488  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1505 0.1967 0.1915 -0.0038 0.0426  0.0175  9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1705 0.2080 0.2423 -0.0024 0.0658  0.0501  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1465 0.1923 0.1855 -0.0043 0.0390  0.0296  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1562 0.1989 0.2178 0.0136  0.0589  0.0573  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1498 0.1975 0.1967 -0.0034 0.0386  0.0189  9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1708 0.2024 0.2401 -0.0008 0.0609  0.0520  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1483 0.1958 0.1929 -0.0053 0.0344  0.0260  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1551 0.1972 0.2263 0.0174  0.0536  0.0545  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1487 0.1997 0.2029 -0.0111 0.0382  0.0234  9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1548 0.1956 0.2281 0.0058  0.0601  0.0574  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1543 0.2025 0.2142 -0.0181 0.0287  0.0285  9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1554 0.1956 0.2332 -0.0046 0.0545  0.0546  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1550 0.1603 0.2109 -0.0119 0.0473  0.0454  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1524 0.1733 0.2479 -0.0020 0.0509  0.0743  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1546 0.1530 0.2082 -0.0178 0.0413  0.0514  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1461 0.1762 0.2596 -0.0120 0.0367  0.0798  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1419 0.1406 0.1925 -0.0220 0.0386  0.0449  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1355 0.1678 0.2565 -0.0166 0.0257  0.0715  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1390 0.1351 0.1804 -0.0194 0.0385  0.0361  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1348 0.1572 0.2551 -0.0109 0.0299  0.0632  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1642 0.1593 0.2339 -0.0120 0.0400  0.0483  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1433 0.1767 0.2875 -0.0143 0.0309  0.0847  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1829 0.1635 0.2596 -0.0110 0.0237  0.0453  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1597 0.1812 0.3147 -0.0108 0.0013  0.0849  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1884 0.1680 0.2631 -0.0086 0.0216  0.0445  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1595 0.1893 0.3290 -0.0153 0.0085  0.0764  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1931 0.1691 0.2746 -0.0163 0.0154  0.0341  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1781 0.1921 0.3185 -0.0153 -0.0174 0.0886  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1420 0.1340 0.1973 -0.0224 0.0326  0.0468  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1406 0.1623 0.2642 -0.0229 0.0150  0.0720  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1402 0.1362 0.2170 -0.0279 0.0325  0.0388  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1364 0.1556 0.2603 -0.0295 0.0042  0.0688  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1334 0.1453 0.2335 -0.0258 0.0276  0.0260  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1244 0.1474 0.2593 -0.0323 0.0038  0.0592  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1282 0.1449 0.2560 -0.0393 0.0285  0.0134  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1262 0.1484 0.2925 -0.0380 0.0164  0.0490  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1517 0.1373 0.2052 -0.0252 0.0300  0.0357  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1453 0.1594 0.2514 -0.0275 0.0082  0.0599  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1640 0.1410 0.1898 -0.0256 0.0244  0.0360  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1654 0.1622 0.2451 -0.0320 0.0157  0.0682  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1781 0.1464 0.1824 -0.0220 0.0172  0.0307  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1870 0.1652 0.2431 -0.0267 0.0175  0.0635  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1829 0.1514 0.1765 -0.0131 0.0120  0.0345  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1945 0.1626 0.2353 -0.0147 0.0170  0.0690  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1828 0.1542 0.1792 -0.0081 0.0054  0.0320  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1942 0.1624 0.2374 -0.0060 0.0131  0.0600  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1361 0.1458 0.2248 -0.0260 0.0218  0.0327  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1285 0.1623 0.2482 -0.0286 -0.0161 0.0549  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1434 0.1551 0.2122 -0.0346 0.0193  0.0453  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1371 0.1843 0.2483 -0.0339 -0.0108 0.0630  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1421 0.1631 0.2110 -0.0377 0.0094  0.0466  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1406 0.1809 0.2312 -0.0323 -0.0050 0.0637  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1408 0.1712 0.2073 -0.0386 0.0160  0.0381  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1418 0.1904 0.2345 -0.0177 -0.0048 0.0586  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1500 0.1476 0.2053 -0.0351 0.0218  0.0525  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1430 0.1989 0.2740 -0.0226 -0.0051 0.0770  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1637 0.1527 0.2256 -0.0260 0.0214  0.0483  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1528 0.2102 0.3109 -0.0126 -0.0035 0.0838  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1750 0.1597 0.2343 -0.0209 0.0168  0.0494  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1651 0.2189 0.3386 -0.0103 0.0040  0.0842  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1700 0.1492 0.2344 -0.0196 0.0193  0.0442  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1582 0.2109 0.3185 0.0023  -0.0172 0.0746  12  LEU   A CD2 
319  N N   . THR   A 13  ? 0.1364 0.1674 0.2220 -0.0296 -0.0056 0.0497  13  THR   A N   
320  C CA  . THR   A 13  ? 0.1439 0.1621 0.2263 -0.0346 0.0093  0.0487  13  THR   A CA  
321  C C   . THR   A 13  ? 0.1389 0.1566 0.2331 -0.0342 0.0094  0.0452  13  THR   A C   
322  O O   . THR   A 13  ? 0.1474 0.1572 0.2282 -0.0215 0.0088  0.0371  13  THR   A O   
323  C CB  . THR   A 13  ? 0.1503 0.1757 0.2366 -0.0286 0.0025  0.0488  13  THR   A CB  
324  O OG1 . THR   A 13  ? 0.1505 0.1680 0.2485 -0.0320 0.0073  0.0511  13  THR   A OG1 
325  C CG2 . THR   A 13  ? 0.1583 0.2025 0.2322 -0.0328 0.0089  0.0301  13  THR   A CG2 
334  N N   A ASP   A 14  ? 0.1433 0.1490 0.2308 -0.0305 0.0085  0.0480  14  ASP   A N   
335  N N   B ASP   A 14  ? 0.1532 0.1548 0.2501 -0.0352 0.0182  0.0562  14  ASP   A N   
336  C CA  A ASP   A 14  ? 0.1423 0.1460 0.2251 -0.0235 0.0039  0.0508  14  ASP   A CA  
337  C CA  B ASP   A 14  ? 0.1624 0.1683 0.2637 -0.0261 0.0187  0.0629  14  ASP   A CA  
338  C C   A ASP   A 14  ? 0.1420 0.1490 0.1901 -0.0171 -0.0019 0.0507  14  ASP   A C   
339  C C   B ASP   A 14  ? 0.1538 0.1660 0.2387 -0.0215 0.0104  0.0606  14  ASP   A C   
340  O O   A ASP   A 14  ? 0.1522 0.1559 0.1860 -0.0242 -0.0105 0.0506  14  ASP   A O   
341  O O   B ASP   A 14  ? 0.1707 0.1780 0.2563 -0.0313 -0.0014 0.0630  14  ASP   A O   
342  C CB  A ASP   A 14  ? 0.1556 0.1499 0.2681 -0.0232 0.0004  0.0584  14  ASP   A CB  
343  C CB  B ASP   A 14  ? 0.2018 0.2015 0.3207 -0.0186 0.0195  0.0800  14  ASP   A CB  
344  C CG  A ASP   A 14  ? 0.1627 0.1775 0.3199 -0.0258 -0.0011 0.0522  14  ASP   A CG  
345  C CG  B ASP   A 14  ? 0.2277 0.2546 0.3950 -0.0099 0.0133  0.0752  14  ASP   A CG  
346  O OD1 A ASP   A 14  ? 0.1728 0.1854 0.3384 -0.0191 -0.0159 0.0616  14  ASP   A OD1 
347  O OD1 B ASP   A 14  ? 0.2432 0.2752 0.4249 0.0092  -0.0036 0.0841  14  ASP   A OD1 
348  O OD2 A ASP   A 14  ? 0.1733 0.1928 0.3472 -0.0224 -0.0011 0.0369  14  ASP   A OD2 
349  O OD2 B ASP   A 14  ? 0.2344 0.2667 0.4316 -0.0069 0.0095  0.0661  14  ASP   A OD2 
358  N N   A ASN   A 15  ? 0.1405 0.1448 0.1819 -0.0168 0.0038  0.0463  15  ASN   A N   
359  N N   B ASN   A 15  ? 0.1424 0.1518 0.2308 -0.0249 0.0189  0.0494  15  ASN   A N   
360  C CA  A ASN   A 15  ? 0.1417 0.1413 0.1931 -0.0146 0.0008  0.0415  15  ASN   A CA  
361  C CA  B ASN   A 15  ? 0.1364 0.1383 0.2477 -0.0236 0.0145  0.0355  15  ASN   A CA  
362  C C   A ASN   A 15  ? 0.1355 0.1359 0.1973 -0.0142 0.0112  0.0394  15  ASN   A C   
363  C C   B ASN   A 15  ? 0.1281 0.1314 0.2685 -0.0224 0.0178  0.0355  15  ASN   A C   
364  O O   A ASN   A 15  ? 0.1294 0.1345 0.2039 -0.0078 0.0101  0.0386  15  ASN   A O   
365  O O   B ASN   A 15  ? 0.1232 0.1344 0.2862 -0.0154 0.0089  0.0309  15  ASN   A O   
366  C CB  A ASN   A 15  ? 0.1496 0.1449 0.1930 -0.0110 -0.0028 0.0493  15  ASN   A CB  
367  C CB  B ASN   A 15  ? 0.1387 0.1389 0.2381 -0.0211 0.0130  0.0388  15  ASN   A CB  
368  C CG  A ASN   A 15  ? 0.1483 0.1499 0.2005 -0.0159 0.0008  0.0388  15  ASN   A CG  
369  C CG  B ASN   A 15  ? 0.1315 0.1545 0.2462 -0.0225 0.0143  0.0309  15  ASN   A CG  
370  O OD1 A ASN   A 15  ? 0.1519 0.1538 0.2109 -0.0203 0.0029  0.0374  15  ASN   A OD1 
371  O OD1 B ASN   A 15  ? 0.1401 0.1635 0.2598 -0.0299 0.0163  0.0261  15  ASN   A OD1 
372  N ND2 A ASN   A 15  ? 0.1497 0.1541 0.2040 -0.0206 0.0084  0.0324  15  ASN   A ND2 
373  N ND2 B ASN   A 15  ? 0.1338 0.1643 0.2513 -0.0211 0.0176  0.0243  15  ASN   A ND2 
386  N N   A VAL   A 16  ? 0.1370 0.1368 0.1949 -0.0148 0.0101  0.0390  16  VAL   A N   
387  N N   B VAL   A 16  ? 0.1269 0.1418 0.2666 -0.0181 0.0061  0.0432  16  VAL   A N   
388  C CA  A VAL   A 16  ? 0.1392 0.1375 0.1907 -0.0147 0.0156  0.0375  16  VAL   A CA  
389  C CA  B VAL   A 16  ? 0.1269 0.1472 0.2476 -0.0195 0.0113  0.0560  16  VAL   A CA  
390  C C   A VAL   A 16  ? 0.1367 0.1346 0.1922 -0.0175 0.0123  0.0388  16  VAL   A C   
391  C C   B VAL   A 16  ? 0.1198 0.1509 0.2394 -0.0191 0.0050  0.0605  16  VAL   A C   
392  O O   A VAL   A 16  ? 0.1338 0.1331 0.2057 -0.0205 0.0172  0.0421  16  VAL   A O   
393  O O   B VAL   A 16  ? 0.1187 0.1546 0.2601 -0.0236 0.0179  0.0529  16  VAL   A O   
394  C CB  A VAL   A 16  ? 0.1468 0.1469 0.1906 -0.0045 0.0211  0.0284  16  VAL   A CB  
395  C CB  B VAL   A 16  ? 0.1441 0.1573 0.2392 -0.0039 0.0181  0.0533  16  VAL   A CB  
396  C CG1 A VAL   A 16  ? 0.1560 0.1553 0.1902 0.0026  0.0231  0.0239  16  VAL   A CG1 
397  C CG1 B VAL   A 16  ? 0.1631 0.1703 0.2357 0.0081  0.0188  0.0506  16  VAL   A CG1 
398  C CG2 A VAL   A 16  ? 0.1530 0.1539 0.1971 -0.0012 0.0298  0.0199  16  VAL   A CG2 
399  C CG2 B VAL   A 16  ? 0.1568 0.1677 0.2540 -0.0011 0.0346  0.0476  16  VAL   A CG2 
418  N N   A TYR   A 17  ? 0.1375 0.1288 0.1930 -0.0186 0.0209  0.0354  17  TYR   A N   
419  N N   B TYR   A 17  ? 0.1177 0.1439 0.2354 -0.0216 0.0178  0.0562  17  TYR   A N   
420  C CA  A TYR   A 17  ? 0.1419 0.1289 0.1823 -0.0189 0.0213  0.0360  17  TYR   A CA  
421  C CA  B TYR   A 17  ? 0.1219 0.1489 0.2100 -0.0200 0.0177  0.0549  17  TYR   A CA  
422  C C   A TYR   A 17  ? 0.1348 0.1235 0.1860 -0.0154 0.0171  0.0402  17  TYR   A C   
423  C C   B TYR   A 17  ? 0.1224 0.1497 0.2224 -0.0190 0.0130  0.0552  17  TYR   A C   
424  O O   A TYR   A 17  ? 0.1270 0.1105 0.1847 -0.0180 0.0180  0.0291  17  TYR   A O   
425  O O   B TYR   A 17  ? 0.1165 0.1575 0.2094 -0.0205 0.0034  0.0517  17  TYR   A O   
426  C CB  A TYR   A 17  ? 0.1613 0.1358 0.1879 -0.0242 0.0153  0.0393  17  TYR   A CB  
427  C CB  B TYR   A 17  ? 0.1387 0.1577 0.2110 -0.0173 0.0079  0.0561  17  TYR   A CB  
428  C CG  A TYR   A 17  ? 0.1806 0.1401 0.1972 -0.0293 0.0009  0.0350  17  TYR   A CG  
429  C CG  B TYR   A 17  ? 0.1545 0.1673 0.2163 -0.0168 -0.0058 0.0478  17  TYR   A CG  
430  C CD1 A TYR   A 17  ? 0.1876 0.1455 0.1999 -0.0301 -0.0063 0.0303  17  TYR   A CD1 
431  C CD1 B TYR   A 17  ? 0.1654 0.1780 0.2202 -0.0047 -0.0034 0.0462  17  TYR   A CD1 
432  C CD2 A TYR   A 17  ? 0.1887 0.1418 0.1926 -0.0406 -0.0035 0.0362  17  TYR   A CD2 
433  C CD2 B TYR   A 17  ? 0.1659 0.1797 0.2104 -0.0294 -0.0028 0.0449  17  TYR   A CD2 
434  C CE1 A TYR   A 17  ? 0.1988 0.1415 0.2027 -0.0351 -0.0175 0.0323  17  TYR   A CE1 
435  C CE1 B TYR   A 17  ? 0.1940 0.1853 0.2281 -0.0019 -0.0074 0.0487  17  TYR   A CE1 
436  C CE2 A TYR   A 17  ? 0.2007 0.1426 0.2001 -0.0449 -0.0101 0.0302  17  TYR   A CE2 
437  C CE2 B TYR   A 17  ? 0.1886 0.1903 0.2184 -0.0310 0.0020  0.0383  17  TYR   A CE2 
438  C CZ  A TYR   A 17  ? 0.2116 0.1355 0.2029 -0.0435 -0.0214 0.0356  17  TYR   A CZ  
439  C CZ  B TYR   A 17  ? 0.2104 0.1897 0.2307 -0.0149 -0.0144 0.0478  17  TYR   A CZ  
440  O OH  A TYR   A 17  ? 0.2273 0.1295 0.2088 -0.0486 -0.0251 0.0435  17  TYR   A OH  
441  O OH  B TYR   A 17  ? 0.2319 0.1973 0.2550 -0.0124 -0.0132 0.0520  17  TYR   A OH  
460  N N   A ILE   A 18  ? 0.1339 0.1308 0.1852 -0.0149 0.0116  0.0488  18  ILE   A N   
461  N N   B ILE   A 18  ? 0.1293 0.1429 0.2409 -0.0240 0.0219  0.0526  18  ILE   A N   
462  C CA  A ILE   A 18  ? 0.1360 0.1394 0.1727 -0.0034 0.0132  0.0510  18  ILE   A CA  
463  C CA  B ILE   A 18  ? 0.1403 0.1440 0.2455 -0.0242 0.0327  0.0523  18  ILE   A CA  
464  C C   A ILE   A 18  ? 0.1324 0.1530 0.1665 0.0012  0.0070  0.0501  18  ILE   A C   
465  C C   B ILE   A 18  ? 0.1411 0.1563 0.2654 -0.0210 0.0416  0.0468  18  ILE   A C   
466  O O   A ILE   A 18  ? 0.1322 0.1610 0.1688 -0.0046 0.0115  0.0553  18  ILE   A O   
467  O O   B ILE   A 18  ? 0.1384 0.1606 0.2689 -0.0278 0.0519  0.0530  18  ILE   A O   
468  C CB  A ILE   A 18  ? 0.1431 0.1506 0.1750 0.0021  0.0144  0.0612  18  ILE   A CB  
469  C CB  B ILE   A 18  ? 0.1559 0.1507 0.2357 -0.0116 0.0216  0.0656  18  ILE   A CB  
470  C CG1 A ILE   A 18  ? 0.1596 0.1677 0.1890 -0.0032 0.0233  0.0603  18  ILE   A CG1 
471  C CG1 B ILE   A 18  ? 0.1621 0.1558 0.2290 -0.0019 0.0150  0.0498  18  ILE   A CG1 
472  C CG2 A ILE   A 18  ? 0.1436 0.1627 0.1886 -0.0014 0.0082  0.0565  18  ILE   A CG2 
473  C CG2 B ILE   A 18  ? 0.1540 0.1584 0.2531 -0.0120 0.0232  0.0634  18  ILE   A CG2 
474  C CD1 A ILE   A 18  ? 0.1794 0.1814 0.2040 -0.0005 0.0239  0.0548  18  ILE   A CD1 
475  C CD1 B ILE   A 18  ? 0.1866 0.1647 0.2455 0.0065  0.0139  0.0481  18  ILE   A CD1 
498  N N   A LYS   A 19  ? 0.1365 0.1523 0.1661 0.0087  0.0156  0.0443  19  LYS   A N   
499  N N   B LYS   A 19  ? 0.1392 0.1497 0.2622 -0.0155 0.0459  0.0516  19  LYS   A N   
500  C CA  A LYS   A 19  ? 0.1453 0.1643 0.1657 0.0128  0.0196  0.0403  19  LYS   A CA  
501  C CA  B LYS   A 19  ? 0.1450 0.1582 0.2495 -0.0024 0.0360  0.0487  19  LYS   A CA  
502  C C   A LYS   A 19  ? 0.1447 0.1628 0.1586 0.0158  0.0281  0.0400  19  LYS   A C   
503  C C   B LYS   A 19  ? 0.1323 0.1497 0.2340 -0.0033 0.0360  0.0400  19  LYS   A C   
504  O O   A LYS   A 19  ? 0.1393 0.1669 0.1648 0.0177  0.0262  0.0321  19  LYS   A O   
505  O O   B LYS   A 19  ? 0.1250 0.1401 0.2212 -0.0003 0.0348  0.0429  19  LYS   A O   
506  C CB  A LYS   A 19  ? 0.1453 0.1774 0.1717 0.0070  0.0287  0.0335  19  LYS   A CB  
507  C CB  B LYS   A 19  ? 0.1513 0.1726 0.2439 0.0014  0.0416  0.0495  19  LYS   A CB  
508  C CG  A LYS   A 19  ? 0.1593 0.1870 0.1756 0.0076  0.0184  0.0368  19  LYS   A CG  
509  C CG  B LYS   A 19  ? 0.1625 0.1895 0.2508 0.0024  0.0356  0.0355  19  LYS   A CG  
510  C CD  A LYS   A 19  ? 0.1659 0.1940 0.1768 0.0033  0.0182  0.0433  19  LYS   A CD  
511  C CD  B LYS   A 19  ? 0.1775 0.2082 0.2465 0.0024  0.0384  0.0264  19  LYS   A CD  
512  C CE  A LYS   A 19  ? 0.1741 0.1999 0.1884 -0.0046 0.0095  0.0474  19  LYS   A CE  
513  C CE  B LYS   A 19  ? 0.1906 0.2199 0.2474 -0.0034 0.0354  0.0233  19  LYS   A CE  
514  N NZ  A LYS   A 19  ? 0.1725 0.2030 0.1893 -0.0133 0.0116  0.0539  19  LYS   A NZ  
515  N NZ  B LYS   A 19  ? 0.2023 0.2308 0.2384 -0.0064 0.0343  0.0217  19  LYS   A NZ  
542  N N   A ASN   A 20  ? 0.1497 0.1578 0.1606 0.0114  0.0290  0.0360  20  ASN   A N   
543  N N   B ASN   A 20  ? 0.1322 0.1543 0.2437 -0.0056 0.0306  0.0440  20  ASN   A N   
544  C CA  A ASN   A 20  ? 0.1500 0.1670 0.1582 0.0152  0.0251  0.0251  20  ASN   A CA  
545  C CA  B ASN   A 20  ? 0.1391 0.1677 0.2422 0.0048  0.0380  0.0353  20  ASN   A CA  
546  C C   A ASN   A 20  ? 0.1587 0.1752 0.1581 0.0102  0.0253  0.0129  20  ASN   A C   
547  C C   B ASN   A 20  ? 0.1543 0.1743 0.2204 -0.0008 0.0460  0.0317  20  ASN   A C   
548  O O   A ASN   A 20  ? 0.1738 0.1920 0.1468 -0.0014 0.0228  0.0040  20  ASN   A O   
549  O O   B ASN   A 20  ? 0.1814 0.1989 0.2393 -0.0112 0.0476  0.0265  20  ASN   A O   
550  C CB  A ASN   A 20  ? 0.1508 0.1679 0.1609 0.0192  0.0195  0.0271  20  ASN   A CB  
551  C CB  B ASN   A 20  ? 0.1413 0.1867 0.2701 0.0089  0.0354  0.0412  20  ASN   A CB  
552  C CG  A ASN   A 20  ? 0.1624 0.1727 0.1729 0.0258  0.0133  0.0272  20  ASN   A CG  
553  C CG  B ASN   A 20  ? 0.1473 0.2020 0.3002 0.0265  0.0342  0.0501  20  ASN   A CG  
554  O OD1 A ASN   A 20  ? 0.1762 0.1873 0.2034 0.0208  0.0121  0.0185  20  ASN   A OD1 
555  O OD1 B ASN   A 20  ? 0.1681 0.2167 0.3234 0.0442  0.0427  0.0545  20  ASN   A OD1 
556  N ND2 A ASN   A 20  ? 0.1644 0.1712 0.1789 0.0292  0.0101  0.0337  20  ASN   A ND2 
557  N ND2 B ASN   A 20  ? 0.1533 0.1962 0.3002 0.0211  0.0228  0.0534  20  ASN   A ND2 
570  N N   A ALA   A 21  ? 0.1569 0.1642 0.1533 0.0125  0.0227  0.0122  21  ALA   A N   
571  N N   B ALA   A 21  ? 0.1506 0.1618 0.2126 -0.0088 0.0458  0.0249  21  ALA   A N   
572  C CA  A ALA   A 21  ? 0.1722 0.1646 0.1532 0.0020  0.0098  0.0151  21  ALA   A CA  
573  C CA  B ALA   A 21  ? 0.1626 0.1604 0.2132 -0.0073 0.0366  0.0259  21  ALA   A CA  
574  C C   A ALA   A 21  ? 0.1840 0.1694 0.1491 0.0010  0.0259  0.0039  21  ALA   A C   
575  C C   B ALA   A 21  ? 0.1462 0.1450 0.1951 -0.0021 0.0279  0.0275  21  ALA   A C   
576  O O   A ALA   A 21  ? 0.1855 0.1817 0.1461 -0.0029 0.0395  -0.0040 21  ALA   A O   
577  O O   B ALA   A 21  ? 0.1439 0.1488 0.1944 -0.0094 0.0316  0.0046  21  ALA   A O   
578  C CB  A ALA   A 21  ? 0.1761 0.1731 0.1685 -0.0066 -0.0249 0.0179  21  ALA   A CB  
579  C CB  B ALA   A 21  ? 0.1971 0.1806 0.2295 -0.0111 0.0320  0.0293  21  ALA   A CB  
590  N N   A ASP   A 22  ? 0.1980 0.1710 0.1698 0.0023  0.0266  -0.0005 22  ASP   A N   
591  N N   B ASP   A 22  ? 0.1425 0.1454 0.1798 0.0030  0.0329  0.0272  22  ASP   A N   
592  C CA  A ASP   A 22  ? 0.2080 0.1820 0.1703 -0.0022 0.0239  0.0037  22  ASP   A CA  
593  C CA  B ASP   A 22  ? 0.1423 0.1393 0.1582 0.0060  0.0313  0.0313  22  ASP   A CA  
594  C C   A ASP   A 22  ? 0.1990 0.1877 0.1582 -0.0075 0.0252  -0.0015 22  ASP   A C   
595  C C   B ASP   A 22  ? 0.1355 0.1464 0.1299 -0.0031 0.0387  0.0364  22  ASP   A C   
596  O O   A ASP   A 22  ? 0.1975 0.2006 0.1581 -0.0124 0.0212  -0.0017 22  ASP   A O   
597  O O   B ASP   A 22  ? 0.1402 0.1688 0.1469 -0.0110 0.0423  0.0250  22  ASP   A O   
598  C CB  A ASP   A 22  ? 0.2272 0.1868 0.1834 -0.0031 0.0231  0.0032  22  ASP   A CB  
599  C CB  B ASP   A 22  ? 0.1533 0.1440 0.1825 0.0083  0.0245  0.0198  22  ASP   A CB  
600  C CG  A ASP   A 22  ? 0.2347 0.1855 0.1828 -0.0112 0.0190  0.0162  22  ASP   A CG  
601  C CG  B ASP   A 22  ? 0.1623 0.1442 0.2116 0.0095  0.0282  0.0190  22  ASP   A CG  
602  O OD1 A ASP   A 22  ? 0.2358 0.1834 0.1861 -0.0228 0.0150  0.0328  22  ASP   A OD1 
603  O OD1 B ASP   A 22  ? 0.1624 0.1460 0.1811 0.0004  0.0360  0.0192  22  ASP   A OD1 
604  O OD2 A ASP   A 22  ? 0.2396 0.1881 0.1835 -0.0156 0.0169  0.0151  22  ASP   A OD2 
605  O OD2 B ASP   A 22  ? 0.1718 0.1598 0.2754 0.0092  0.0223  0.0307  22  ASP   A OD2 
614  N N   A ILE   A 23  ? 0.1883 0.1779 0.1557 -0.0096 0.0284  -0.0077 23  ILE   A N   
615  N N   B ILE   A 23  ? 0.1352 0.1375 0.1475 -0.0059 0.0266  0.0359  23  ILE   A N   
616  C CA  A ILE   A 23  ? 0.1782 0.1680 0.1518 -0.0104 0.0315  -0.0034 23  ILE   A CA  
617  C CA  B ILE   A 23  ? 0.1327 0.1468 0.1479 -0.0092 0.0219  0.0388  23  ILE   A CA  
618  C C   A ILE   A 23  ? 0.1679 0.1716 0.1507 -0.0043 0.0301  -0.0016 23  ILE   A C   
619  C C   B ILE   A 23  ? 0.1351 0.1523 0.1496 -0.0072 0.0076  0.0258  23  ILE   A C   
620  O O   A ILE   A 23  ? 0.1633 0.1718 0.1561 -0.0008 0.0284  -0.0030 23  ILE   A O   
621  O O   B ILE   A 23  ? 0.1349 0.1544 0.1581 -0.0034 0.0066  0.0222  23  ILE   A O   
622  C CB  A ILE   A 23  ? 0.1824 0.1589 0.1493 -0.0116 0.0407  0.0005  23  ILE   A CB  
623  C CB  B ILE   A 23  ? 0.1429 0.1379 0.1528 -0.0003 0.0301  0.0176  23  ILE   A CB  
624  C CG1 A ILE   A 23  ? 0.1876 0.1522 0.1564 -0.0089 0.0397  -0.0025 23  ILE   A CG1 
625  C CG1 B ILE   A 23  ? 0.1492 0.1390 0.1712 -0.0053 0.0223  0.0080  23  ILE   A CG1 
626  C CG2 A ILE   A 23  ? 0.1843 0.1560 0.1477 -0.0121 0.0458  0.0036  23  ILE   A CG2 
627  C CG2 B ILE   A 23  ? 0.1429 0.1396 0.1627 0.0052  0.0334  0.0214  23  ILE   A CG2 
628  C CD1 A ILE   A 23  ? 0.1898 0.1467 0.1702 -0.0067 0.0283  -0.0095 23  ILE   A CD1 
629  C CD1 B ILE   A 23  ? 0.1470 0.1422 0.1844 0.0034  0.0112  0.0034  23  ILE   A CD1 
652  N N   A VAL   A 24  ? 0.1654 0.1779 0.1661 -0.0121 0.0241  -0.0061 24  VAL   A N   
653  N N   B VAL   A 24  ? 0.1441 0.1596 0.1517 -0.0165 0.0067  0.0193  24  VAL   A N   
654  C CA  A VAL   A 24  ? 0.1709 0.1889 0.1805 -0.0128 0.0201  -0.0073 24  VAL   A CA  
655  C CA  B VAL   A 24  ? 0.1615 0.1623 0.1675 -0.0151 0.0037  0.0102  24  VAL   A CA  
656  C C   A VAL   A 24  ? 0.1720 0.2046 0.1921 -0.0155 0.0165  -0.0071 24  VAL   A C   
657  C C   B VAL   A 24  ? 0.1629 0.1751 0.1791 -0.0127 0.0093  -0.0007 24  VAL   A C   
658  O O   A VAL   A 24  ? 0.1726 0.2020 0.1921 -0.0141 0.0128  -0.0019 24  VAL   A O   
659  O O   B VAL   A 24  ? 0.1817 0.1815 0.1973 -0.0105 0.0102  0.0040  24  VAL   A O   
660  C CB  A VAL   A 24  ? 0.1686 0.1872 0.1743 -0.0147 0.0290  -0.0009 24  VAL   A CB  
661  C CB  B VAL   A 24  ? 0.1706 0.1624 0.1805 -0.0263 0.0078  0.0173  24  VAL   A CB  
662  C CG1 A VAL   A 24  ? 0.1697 0.1917 0.1609 -0.0062 0.0392  -0.0085 24  VAL   A CG1 
663  C CG1 B VAL   A 24  ? 0.1949 0.1690 0.2046 -0.0323 0.0003  0.0183  24  VAL   A CG1 
664  C CG2 A VAL   A 24  ? 0.1739 0.1831 0.1796 -0.0178 0.0320  0.0023  24  VAL   A CG2 
665  C CG2 B VAL   A 24  ? 0.1753 0.1709 0.1908 -0.0299 0.0152  0.0254  24  VAL   A CG2 
684  N N   A GLU   A 25  ? 0.1815 0.2251 0.1957 -0.0246 0.0217  -0.0153 25  GLU   A N   
685  N N   B GLU   A 25  ? 0.1611 0.2011 0.1894 -0.0022 0.0294  -0.0005 25  GLU   A N   
686  C CA  A GLU   A 25  ? 0.2027 0.2443 0.2125 -0.0278 0.0244  -0.0180 25  GLU   A CA  
687  C CA  B GLU   A 25  ? 0.1648 0.2209 0.1925 0.0045  0.0329  0.0021  25  GLU   A CA  
688  C C   A GLU   A 25  ? 0.1996 0.2441 0.1875 -0.0385 0.0383  -0.0141 25  GLU   A C   
689  C C   B GLU   A 25  ? 0.1603 0.2305 0.1761 0.0033  0.0354  0.0055  25  GLU   A C   
690  O O   A GLU   A 25  ? 0.1994 0.2463 0.1775 -0.0432 0.0318  -0.0090 25  GLU   A O   
691  O O   B GLU   A 25  ? 0.1743 0.2402 0.1880 0.0051  0.0392  0.0050  25  GLU   A O   
692  C CB  A GLU   A 25  ? 0.2239 0.2584 0.2499 -0.0246 0.0178  -0.0195 25  GLU   A CB  
693  C CB  B GLU   A 25  ? 0.1834 0.2289 0.2233 0.0096  0.0407  0.0000  25  GLU   A CB  
694  C CG  A GLU   A 25  ? 0.2425 0.2696 0.2863 -0.0275 0.0020  -0.0257 25  GLU   A CG  
695  C CG  B GLU   A 25  ? 0.2312 0.2501 0.3019 0.0065  0.0307  -0.0096 25  GLU   A CG  
696  C CD  A GLU   A 25  ? 0.2544 0.2791 0.3155 -0.0292 -0.0121 -0.0274 25  GLU   A CD  
697  C CD  B GLU   A 25  ? 0.2706 0.2715 0.3647 0.0031  0.0323  -0.0189 25  GLU   A CD  
698  O OE1 A GLU   A 25  ? 0.2621 0.2829 0.3194 -0.0280 -0.0220 -0.0308 25  GLU   A OE1 
699  O OE1 B GLU   A 25  ? 0.2846 0.2828 0.3955 0.0017  0.0300  -0.0269 25  GLU   A OE1 
700  O OE2 A GLU   A 25  ? 0.2582 0.2833 0.3350 -0.0284 -0.0148 -0.0294 25  GLU   A OE2 
701  O OE2 B GLU   A 25  ? 0.2829 0.2802 0.3912 0.0013  0.0280  -0.0208 25  GLU   A OE2 
714  N N   A GLU   A 26  ? 0.1959 0.2356 0.1794 -0.0537 0.0555  -0.0141 26  GLU   A N   
715  N N   B GLU   A 26  ? 0.1505 0.2259 0.1797 -0.0066 0.0387  -0.0029 26  GLU   A N   
716  C CA  A GLU   A 26  ? 0.2075 0.2320 0.1788 -0.0652 0.0592  -0.0007 26  GLU   A CA  
717  C CA  B GLU   A 26  ? 0.1643 0.2198 0.1859 -0.0146 0.0409  0.0099  26  GLU   A CA  
718  C C   A GLU   A 26  ? 0.2111 0.2348 0.1751 -0.0678 0.0548  0.0082  26  GLU   A C   
719  C C   B GLU   A 26  ? 0.1637 0.2059 0.1614 -0.0105 0.0313  0.0217  26  GLU   A C   
720  O O   A GLU   A 26  ? 0.2145 0.2399 0.1791 -0.0720 0.0494  0.0104  26  GLU   A O   
721  O O   B GLU   A 26  ? 0.1836 0.2189 0.1589 -0.0174 0.0300  0.0286  26  GLU   A O   
722  C CB  A GLU   A 26  ? 0.2199 0.2221 0.1903 -0.0722 0.0630  0.0093  26  GLU   A CB  
723  C CB  B GLU   A 26  ? 0.1830 0.2229 0.2161 -0.0245 0.0382  0.0151  26  GLU   A CB  
724  C CG  A GLU   A 26  ? 0.2281 0.2174 0.2232 -0.0749 0.0617  0.0088  26  GLU   A CG  
725  C CG  B GLU   A 26  ? 0.1923 0.2290 0.2580 -0.0209 0.0426  0.0142  26  GLU   A CG  
726  C CD  A GLU   A 26  ? 0.2343 0.2153 0.2416 -0.0794 0.0697  0.0130  26  GLU   A CD  
727  C CD  B GLU   A 26  ? 0.1970 0.2369 0.2831 -0.0183 0.0518  0.0159  26  GLU   A CD  
728  O OE1 A GLU   A 26  ? 0.2353 0.2219 0.2500 -0.0710 0.0803  -0.0032 26  GLU   A OE1 
729  O OE1 B GLU   A 26  ? 0.2067 0.2498 0.2924 -0.0035 0.0708  0.0113  26  GLU   A OE1 
730  O OE2 A GLU   A 26  ? 0.2388 0.2161 0.2373 -0.0816 0.0705  0.0232  26  GLU   A OE2 
731  O OE2 B GLU   A 26  ? 0.1969 0.2400 0.2626 -0.0217 0.0561  0.0176  26  GLU   A OE2 
744  N N   A ALA   A 27  ? 0.2105 0.2346 0.1795 -0.0650 0.0542  0.0104  27  ALA   A N   
745  N N   B ALA   A 27  ? 0.1466 0.1830 0.1567 0.0009  0.0284  0.0281  27  ALA   A N   
746  C CA  A ALA   A 27  ? 0.2167 0.2444 0.1875 -0.0581 0.0522  0.0130  27  ALA   A CA  
747  C CA  B ALA   A 27  ? 0.1508 0.1815 0.1627 0.0102  0.0267  0.0244  27  ALA   A CA  
748  C C   A ALA   A 27  ? 0.2310 0.2612 0.2116 -0.0547 0.0509  0.0076  27  ALA   A C   
749  C C   B ALA   A 27  ? 0.1675 0.1944 0.1621 0.0073  0.0154  0.0151  27  ALA   A C   
750  O O   A ALA   A 27  ? 0.2320 0.2617 0.2125 -0.0549 0.0490  0.0042  27  ALA   A O   
751  O O   B ALA   A 27  ? 0.1700 0.1961 0.1695 0.0023  0.0183  0.0107  27  ALA   A O   
752  C CB  A ALA   A 27  ? 0.2107 0.2379 0.1864 -0.0582 0.0449  0.0187  27  ALA   A CB  
753  C CB  B ALA   A 27  ? 0.1465 0.1747 0.1782 0.0012  0.0243  0.0186  27  ALA   A CB  
764  N N   A LYS   A 28  ? 0.2509 0.2827 0.2393 -0.0438 0.0470  -0.0027 28  LYS   A N   
765  N N   B LYS   A 28  ? 0.2077 0.2137 0.1542 0.0280  0.0053  -0.0027 28  LYS   A N   
766  C CA  A LYS   A 28  ? 0.2757 0.3068 0.2709 -0.0292 0.0423  -0.0083 28  LYS   A CA  
767  C CA  B LYS   A 28  ? 0.2481 0.2558 0.1852 0.0527  0.0082  -0.0240 28  LYS   A CA  
768  C C   A LYS   A 28  ? 0.2877 0.3248 0.2747 -0.0293 0.0466  -0.0081 28  LYS   A C   
769  C C   B LYS   A 28  ? 0.2678 0.2847 0.1730 0.0570  0.0177  -0.0160 28  LYS   A C   
770  O O   A LYS   A 28  ? 0.2892 0.3286 0.2857 -0.0264 0.0401  -0.0103 28  LYS   A O   
771  O O   B LYS   A 28  ? 0.2839 0.3012 0.1868 0.0515  -0.0016 -0.0113 28  LYS   A O   
772  C CB  A LYS   A 28  ? 0.2886 0.3150 0.3034 -0.0141 0.0328  -0.0120 28  LYS   A CB  
773  C CB  B LYS   A 28  ? 0.2777 0.2780 0.2460 0.0673  -0.0002 -0.0449 28  LYS   A CB  
774  C CG  A LYS   A 28  ? 0.2989 0.3232 0.3356 -0.0016 0.0245  -0.0106 28  LYS   A CG  
775  C CG  B LYS   A 28  ? 0.3034 0.3066 0.3145 0.0726  -0.0041 -0.0459 28  LYS   A CG  
776  C CD  A LYS   A 28  ? 0.3066 0.3318 0.3661 0.0084  0.0143  -0.0081 28  LYS   A CD  
777  C CD  B LYS   A 28  ? 0.3289 0.3361 0.3885 0.0761  -0.0151 -0.0460 28  LYS   A CD  
778  C CE  A LYS   A 28  ? 0.3114 0.3379 0.3858 0.0146  0.0070  -0.0073 28  LYS   A CE  
779  C CE  B LYS   A 28  ? 0.3495 0.3563 0.4354 0.0776  -0.0244 -0.0523 28  LYS   A CE  
780  N NZ  A LYS   A 28  ? 0.3161 0.3410 0.4018 0.0183  0.0053  -0.0098 28  LYS   A NZ  
781  N NZ  B LYS   A 28  ? 0.3598 0.3654 0.4573 0.0805  -0.0307 -0.0583 28  LYS   A NZ  
808  N N   A LYS   A 29  ? 0.2969 0.3392 0.2797 -0.0329 0.0548  0.0006  29  LYS   A N   
809  N N   B LYS   A 29  ? 0.2633 0.2999 0.1710 0.0622  0.0568  0.0086  29  LYS   A N   
810  C CA  A LYS   A 29  ? 0.3094 0.3524 0.2914 -0.0345 0.0573  0.0056  29  LYS   A CA  
811  C CA  B LYS   A 29  ? 0.2724 0.3204 0.1857 0.0578  0.0755  0.0265  29  LYS   A CA  
812  C C   A LYS   A 29  ? 0.2979 0.3404 0.2638 -0.0463 0.0535  0.0124  29  LYS   A C   
813  C C   B LYS   A 29  ? 0.2610 0.3052 0.1618 0.0459  0.0601  0.0427  29  LYS   A C   
814  O O   A LYS   A 29  ? 0.3021 0.3452 0.2722 -0.0425 0.0484  0.0060  29  LYS   A O   
815  O O   B LYS   A 29  ? 0.2716 0.3185 0.1895 0.0514  0.0402  0.0341  29  LYS   A O   
816  C CB  A LYS   A 29  ? 0.3282 0.3742 0.3338 -0.0262 0.0640  0.0059  29  LYS   A CB  
817  C CB  B LYS   A 29  ? 0.2955 0.3554 0.2329 0.0562  0.1120  0.0270  29  LYS   A CB  
818  C CG  A LYS   A 29  ? 0.3453 0.3927 0.3810 -0.0193 0.0632  0.0064  29  LYS   A CG  
819  C CG  B LYS   A 29  ? 0.3248 0.3882 0.3094 0.0563  0.1236  0.0208  29  LYS   A CG  
820  C CD  A LYS   A 29  ? 0.3593 0.4079 0.4266 -0.0141 0.0608  0.0061  29  LYS   A CD  
821  C CD  B LYS   A 29  ? 0.3503 0.4147 0.3882 0.0568  0.1242  0.0132  29  LYS   A CD  
822  C CE  A LYS   A 29  ? 0.3692 0.4184 0.4569 -0.0109 0.0596  0.0061  29  LYS   A CE  
823  C CE  B LYS   A 29  ? 0.3683 0.4340 0.4421 0.0558  0.1267  0.0056  29  LYS   A CE  
824  N NZ  A LYS   A 29  ? 0.3743 0.4243 0.4780 -0.0086 0.0576  0.0050  29  LYS   A NZ  
825  N NZ  B LYS   A 29  ? 0.3772 0.4437 0.4794 0.0574  0.1244  0.0008  29  LYS   A NZ  
852  N N   A VAL   A 30  ? 0.2829 0.3216 0.2379 -0.0607 0.0474  0.0212  30  VAL   A N   
853  N N   B VAL   A 30  ? 0.2375 0.2791 0.1552 0.0267  0.0602  0.0521  30  VAL   A N   
854  C CA  A VAL   A 30  ? 0.2758 0.3065 0.2198 -0.0656 0.0348  0.0249  30  VAL   A CA  
855  C CA  B VAL   A 30  ? 0.2229 0.2596 0.1601 0.0134  0.0509  0.0517  30  VAL   A CA  
856  C C   A VAL   A 30  ? 0.2715 0.2887 0.1940 -0.0626 0.0288  0.0278  30  VAL   A C   
857  C C   B VAL   A 30  ? 0.2225 0.2486 0.1421 0.0079  0.0442  0.0443  30  VAL   A C   
858  O O   A VAL   A 30  ? 0.2738 0.2891 0.1929 -0.0601 0.0256  0.0267  30  VAL   A O   
859  O O   B VAL   A 30  ? 0.2332 0.2532 0.1571 -0.0005 0.0293  0.0452  30  VAL   A O   
860  C CB  A VAL   A 30  ? 0.2740 0.3071 0.2278 -0.0709 0.0275  0.0218  30  VAL   A CB  
861  C CB  B VAL   A 30  ? 0.2222 0.2524 0.1900 0.0050  0.0366  0.0495  30  VAL   A CB  
862  C CG1 A VAL   A 30  ? 0.2754 0.3064 0.2304 -0.0713 0.0251  0.0200  30  VAL   A CG1 
863  C CG1 B VAL   A 30  ? 0.2295 0.2508 0.2098 0.0031  0.0325  0.0419  30  VAL   A CG1 
864  C CG2 A VAL   A 30  ? 0.2726 0.3090 0.2374 -0.0736 0.0246  0.0194  30  VAL   A CG2 
865  C CG2 B VAL   A 30  ? 0.2206 0.2530 0.2159 -0.0021 0.0300  0.0595  30  VAL   A CG2 
884  N N   A LYS   A 31  ? 0.2636 0.2710 0.1861 -0.0594 0.0238  0.0287  31  LYS   A N   
885  N N   B LYS   A 31  ? 0.2187 0.2341 0.1459 0.0095  0.0421  0.0399  31  LYS   A N   
886  C CA  A LYS   A 31  ? 0.2655 0.2617 0.2003 -0.0500 0.0092  0.0249  31  LYS   A CA  
887  C CA  B LYS   A 31  ? 0.2284 0.2310 0.1635 0.0143  0.0223  0.0277  31  LYS   A CA  
888  C C   A LYS   A 31  ? 0.2474 0.2318 0.1570 -0.0456 -0.0005 0.0401  31  LYS   A C   
889  C C   B LYS   A 31  ? 0.2115 0.2172 0.1309 0.0157  0.0122  0.0381  31  LYS   A C   
890  O O   A LYS   A 31  ? 0.2424 0.2273 0.1493 -0.0416 -0.0087 0.0488  31  LYS   A O   
891  O O   B LYS   A 31  ? 0.2252 0.2205 0.1576 0.0171  0.0023  0.0222  31  LYS   A O   
892  C CB  A LYS   A 31  ? 0.2877 0.2842 0.2697 -0.0425 -0.0022 0.0122  31  LYS   A CB  
893  C CB  B LYS   A 31  ? 0.2633 0.2523 0.2466 0.0174  0.0029  0.0020  31  LYS   A CB  
894  C CG  A LYS   A 31  ? 0.3091 0.3029 0.3427 -0.0322 -0.0143 0.0041  31  LYS   A CG  
895  C CG  B LYS   A 31  ? 0.3048 0.2881 0.3606 0.0180  -0.0169 -0.0205 31  LYS   A CG  
896  C CD  A LYS   A 31  ? 0.3270 0.3168 0.4025 -0.0248 -0.0268 -0.0027 31  LYS   A CD  
897  C CD  B LYS   A 31  ? 0.3349 0.3201 0.4517 0.0167  -0.0361 -0.0404 31  LYS   A CD  
898  C CE  A LYS   A 31  ? 0.3374 0.3253 0.4456 -0.0204 -0.0357 -0.0078 31  LYS   A CE  
899  C CE  B LYS   A 31  ? 0.3562 0.3476 0.5157 0.0117  -0.0515 -0.0544 31  LYS   A CE  
900  N NZ  A LYS   A 31  ? 0.3422 0.3288 0.4682 -0.0167 -0.0436 -0.0100 31  LYS   A NZ  
901  N NZ  B LYS   A 31  ? 0.3708 0.3598 0.5514 0.0079  -0.0579 -0.0636 31  LYS   A NZ  
928  N N   A PRO   A 32  ? 0.2336 0.2125 0.1502 -0.0445 0.0063  0.0347  32  PRO   A N   
929  N N   B PRO   A 32  ? 0.1925 0.2049 0.1325 0.0103  0.0287  0.0333  32  PRO   A N   
930  C CA  A PRO   A 32  ? 0.2257 0.2019 0.1572 -0.0444 0.0055  0.0397  32  PRO   A CA  
931  C CA  B PRO   A 32  ? 0.1944 0.2007 0.1439 0.0119  0.0270  0.0431  32  PRO   A CA  
932  C C   A PRO   A 32  ? 0.2142 0.1919 0.1551 -0.0417 0.0033  0.0362  32  PRO   A C   
933  C C   B PRO   A 32  ? 0.1961 0.2015 0.1434 0.0153  0.0212  0.0345  32  PRO   A C   
934  O O   A PRO   A 32  ? 0.2095 0.1828 0.1497 -0.0497 0.0036  0.0307  32  PRO   A O   
935  O O   B PRO   A 32  ? 0.2000 0.1993 0.1706 0.0062  0.0113  0.0286  32  PRO   A O   
936  C CB  A PRO   A 32  ? 0.2280 0.2084 0.1678 -0.0440 0.0047  0.0309  32  PRO   A CB  
937  C CB  B PRO   A 32  ? 0.1916 0.2129 0.1680 0.0070  0.0189  0.0287  32  PRO   A CB  
938  C CG  A PRO   A 32  ? 0.2312 0.2128 0.1586 -0.0419 0.0037  0.0283  32  PRO   A CG  
939  C CG  B PRO   A 32  ? 0.1944 0.2200 0.1519 0.0061  0.0162  0.0243  32  PRO   A CG  
940  C CD  A PRO   A 32  ? 0.2319 0.2099 0.1500 -0.0440 0.0057  0.0322  32  PRO   A CD  
941  C CD  B PRO   A 32  ? 0.1893 0.2080 0.1352 0.0077  0.0209  0.0314  32  PRO   A CD  
956  N N   A THR   A 33  ? 0.2111 0.1913 0.1519 -0.0347 0.0061  0.0372  33  THR   A N   
957  N N   B THR   A 33  ? 0.1958 0.2042 0.1444 0.0169  0.0193  0.0321  33  THR   A N   
958  C CA  A THR   A 33  ? 0.2092 0.1913 0.1504 -0.0249 0.0001  0.0342  33  THR   A CA  
959  C CA  B THR   A 33  ? 0.2003 0.2056 0.1515 0.0240  0.0013  0.0305  33  THR   A CA  
960  C C   A THR   A 33  ? 0.1918 0.1804 0.1343 -0.0284 0.0019  0.0356  33  THR   A C   
961  C C   B THR   A 33  ? 0.1756 0.1813 0.1501 0.0113  -0.0009 0.0195  33  THR   A C   
962  O O   A THR   A 33  ? 0.1913 0.1819 0.1254 -0.0146 -0.0068 0.0442  33  THR   A O   
963  O O   B THR   A 33  ? 0.1657 0.1765 0.1486 0.0088  0.0028  0.0104  33  THR   A O   
964  C CB  A THR   A 33  ? 0.2239 0.2033 0.1754 -0.0149 0.0012  0.0327  33  THR   A CB  
965  C CB  B THR   A 33  ? 0.2296 0.2320 0.1651 0.0339  0.0002  0.0525  33  THR   A CB  
966  O OG1 A THR   A 33  ? 0.2330 0.2063 0.1891 -0.0095 0.0069  0.0322  33  THR   A OG1 
967  O OG1 B THR   A 33  ? 0.2471 0.2568 0.1872 0.0359  -0.0018 0.0653  33  THR   A OG1 
968  C CG2 A THR   A 33  ? 0.2266 0.2097 0.1809 -0.0097 -0.0054 0.0306  33  THR   A CG2 
969  C CG2 B THR   A 33  ? 0.2353 0.2403 0.1791 0.0373  -0.0030 0.0478  33  THR   A CG2 
984  N N   A VAL   A 34  ? 0.1737 0.1689 0.1284 -0.0378 0.0127  0.0319  34  VAL   A N   
985  N N   B VAL   A 34  ? 0.1609 0.1727 0.1522 0.0048  0.0044  0.0201  34  VAL   A N   
986  C CA  A VAL   A 34  ? 0.1644 0.1575 0.1255 -0.0399 0.0135  0.0310  34  VAL   A CA  
987  C CA  B VAL   A 34  ? 0.1570 0.1627 0.1405 0.0019  0.0096  0.0209  34  VAL   A CA  
988  C C   A VAL   A 34  ? 0.1533 0.1487 0.1256 -0.0335 0.0168  0.0238  34  VAL   A C   
989  C C   B VAL   A 34  ? 0.1503 0.1521 0.1316 -0.0035 0.0142  0.0208  34  VAL   A C   
990  O O   A VAL   A 34  ? 0.1485 0.1460 0.1217 -0.0375 0.0271  0.0178  34  VAL   A O   
991  O O   B VAL   A 34  ? 0.1583 0.1584 0.1556 -0.0084 0.0081  0.0278  34  VAL   A O   
992  C CB  A VAL   A 34  ? 0.1695 0.1586 0.1230 -0.0416 0.0114  0.0318  34  VAL   A CB  
993  C CB  B VAL   A 34  ? 0.1686 0.1692 0.1562 0.0045  0.0165  0.0202  34  VAL   A CB  
994  C CG1 A VAL   A 34  ? 0.1774 0.1634 0.1326 -0.0393 0.0118  0.0229  34  VAL   A CG1 
995  C CG1 B VAL   A 34  ? 0.1829 0.1738 0.1459 0.0104  0.0192  -0.0017 34  VAL   A CG1 
996  C CG2 A VAL   A 34  ? 0.1735 0.1666 0.1336 -0.0369 0.0115  0.0260  34  VAL   A CG2 
997  C CG2 B VAL   A 34  ? 0.1729 0.1849 0.1893 0.0025  0.0264  0.0194  34  VAL   A CG2 
1016 N N   . VAL   A 35  ? 0.1439 0.1484 0.1380 -0.0217 0.0054  0.0243  35  VAL   A N   
1017 C CA  . VAL   A 35  ? 0.1335 0.1455 0.1368 -0.0140 0.0160  0.0224  35  VAL   A CA  
1018 C C   . VAL   A 35  ? 0.1268 0.1304 0.1313 -0.0122 0.0175  0.0139  35  VAL   A C   
1019 O O   . VAL   A 35  ? 0.1255 0.1505 0.1518 -0.0222 0.0186  0.0131  35  VAL   A O   
1020 C CB  . VAL   A 35  ? 0.1460 0.1512 0.1390 -0.0116 0.0212  0.0180  35  VAL   A CB  
1021 C CG1 . VAL   A 35  ? 0.1560 0.1549 0.1495 -0.0051 0.0205  0.0075  35  VAL   A CG1 
1022 C CG2 . VAL   A 35  ? 0.1503 0.1496 0.1655 -0.0094 0.0244  0.0110  35  VAL   A CG2 
1033 N N   . VAL   A 36  ? 0.1177 0.1306 0.1287 -0.0159 0.0161  0.0227  36  VAL   A N   
1034 C CA  . VAL   A 36  ? 0.1159 0.1202 0.1352 -0.0101 0.0119  0.0177  36  VAL   A CA  
1035 C C   . VAL   A 36  ? 0.1136 0.1252 0.1386 -0.0125 0.0107  0.0145  36  VAL   A C   
1036 O O   . VAL   A 36  ? 0.1156 0.1236 0.1704 -0.0079 0.0168  0.0228  36  VAL   A O   
1037 C CB  . VAL   A 36  ? 0.1159 0.1189 0.1463 -0.0117 0.0159  0.0187  36  VAL   A CB  
1038 C CG1 . VAL   A 36  ? 0.1192 0.1199 0.1619 -0.0124 0.0087  0.0053  36  VAL   A CG1 
1039 C CG2 . VAL   A 36  ? 0.1231 0.1236 0.1564 -0.0083 0.0076  0.0190  36  VAL   A CG2 
1049 N N   A ASN   A 37  ? 0.1121 0.1209 0.1332 -0.0045 0.0091  0.0118  37  ASN   A N   
1050 N N   B ASN   A 37  ? 0.1133 0.1124 0.1230 -0.0026 0.0096  0.0218  37  ASN   A N   
1051 C CA  A ASN   A 37  ? 0.1130 0.1250 0.1276 -0.0013 0.0082  0.0115  37  ASN   A CA  
1052 C CA  B ASN   A 37  ? 0.1089 0.1108 0.1270 -0.0031 0.0070  0.0225  37  ASN   A CA  
1053 C C   A ASN   A 37  ? 0.1107 0.1297 0.1134 -0.0045 0.0217  0.0136  37  ASN   A C   
1054 C C   B ASN   A 37  ? 0.1071 0.1016 0.1297 -0.0006 0.0112  0.0275  37  ASN   A C   
1055 O O   A ASN   A 37  ? 0.1205 0.1399 0.1023 0.0048  0.0239  -0.0042 37  ASN   A O   
1056 O O   B ASN   A 37  ? 0.1167 0.1080 0.1538 0.0059  0.0031  0.0223  37  ASN   A O   
1057 C CB  A ASN   A 37  ? 0.1147 0.1209 0.1296 0.0032  0.0010  0.0076  37  ASN   A CB  
1058 C CB  B ASN   A 37  ? 0.1092 0.1076 0.1358 0.0054  0.0086  0.0214  37  ASN   A CB  
1059 C CG  A ASN   A 37  ? 0.1132 0.1164 0.1193 0.0065  -0.0111 0.0007  37  ASN   A CG  
1060 C CG  B ASN   A 37  ? 0.1142 0.1089 0.1301 -0.0016 0.0050  0.0080  37  ASN   A CG  
1061 O OD1 A ASN   A 37  ? 0.1154 0.1147 0.1168 0.0067  -0.0099 0.0052  37  ASN   A OD1 
1062 O OD1 B ASN   A 37  ? 0.1110 0.1100 0.1329 -0.0082 0.0098  0.0129  37  ASN   A OD1 
1063 N ND2 A ASN   A 37  ? 0.1095 0.1152 0.1314 0.0062  -0.0147 0.0122  37  ASN   A ND2 
1064 N ND2 B ASN   A 37  ? 0.1109 0.1017 0.1477 -0.0084 0.0121  0.0190  37  ASN   A ND2 
1077 N N   A ALA   A 38  ? 0.1099 0.1271 0.1279 -0.0113 0.0125  0.0086  38  ALA   A N   
1078 N N   B ALA   A 38  ? 0.1134 0.1002 0.1367 0.0071  0.0013  0.0120  38  ALA   A N   
1079 C CA  A ALA   A 38  ? 0.1168 0.1136 0.1215 -0.0050 0.0032  -0.0061 38  ALA   A CA  
1080 C CA  B ALA   A 38  ? 0.1232 0.1150 0.1457 -0.0015 -0.0054 0.0165  38  ALA   A CA  
1081 C C   A ALA   A 38  ? 0.1205 0.1129 0.1229 -0.0001 0.0021  -0.0069 38  ALA   A C   
1082 C C   B ALA   A 38  ? 0.1222 0.1173 0.1504 -0.0015 -0.0085 0.0070  38  ALA   A C   
1083 O O   A ALA   A 38  ? 0.1245 0.1057 0.1159 -0.0054 -0.0117 -0.0164 38  ALA   A O   
1084 O O   B ALA   A 38  ? 0.1241 0.1140 0.1572 -0.0012 -0.0166 0.0197  38  ALA   A O   
1085 C CB  A ALA   A 38  ? 0.1125 0.1132 0.1259 -0.0056 -0.0040 -0.0160 38  ALA   A CB  
1086 C CB  B ALA   A 38  ? 0.1257 0.1258 0.1508 -0.0049 -0.0097 0.0085  38  ALA   A CB  
1097 N N   A ALA   A 39  ? 0.1193 0.1137 0.1320 0.0057  0.0079  0.0057  39  ALA   A N   
1098 N N   B ALA   A 39  ? 0.1291 0.1299 0.1609 -0.0036 0.0007  0.0258  39  ALA   A N   
1099 C CA  A ALA   A 39  ? 0.1122 0.1075 0.1193 0.0097  0.0116  0.0118  39  ALA   A CA  
1100 C CA  B ALA   A 39  ? 0.1252 0.1285 0.1426 -0.0082 -0.0011 0.0108  39  ALA   A CA  
1101 C C   A ALA   A 39  ? 0.1214 0.1208 0.1196 0.0037  0.0053  0.0128  39  ALA   A C   
1102 C C   B ALA   A 39  ? 0.1216 0.1202 0.1439 -0.0085 -0.0104 0.0046  39  ALA   A C   
1103 O O   A ALA   A 39  ? 0.1303 0.1217 0.1176 -0.0007 0.0052  0.0206  39  ALA   A O   
1104 O O   B ALA   A 39  ? 0.1477 0.1210 0.1542 -0.0080 -0.0122 0.0028  39  ALA   A O   
1105 C CB  A ALA   A 39  ? 0.1061 0.1134 0.1263 0.0053  0.0130  0.0115  39  ALA   A CB  
1106 C CB  B ALA   A 39  ? 0.1361 0.1504 0.1437 -0.0123 -0.0068 0.0184  39  ALA   A CB  
1117 N N   A ASN   A 40  ? 0.1202 0.1326 0.1235 0.0003  0.0022  0.0091  40  ASN   A N   
1118 N N   B ASN   A 40  ? 0.1200 0.1130 0.1377 -0.0063 0.0113  0.0087  40  ASN   A N   
1119 C CA  A ASN   A 40  ? 0.1251 0.1342 0.1219 -0.0036 -0.0016 0.0091  40  ASN   A CA  
1120 C CA  B ASN   A 40  ? 0.1258 0.1072 0.1351 -0.0018 -0.0053 0.0107  40  ASN   A CA  
1121 C C   A ASN   A 40  ? 0.1282 0.1270 0.1135 -0.0012 -0.0046 0.0140  40  ASN   A C   
1122 C C   B ASN   A 40  ? 0.1268 0.1020 0.1280 -0.0042 0.0066  0.0169  40  ASN   A C   
1123 O O   A ASN   A 40  ? 0.1276 0.1273 0.1247 -0.0026 -0.0025 0.0134  40  ASN   A O   
1124 O O   B ASN   A 40  ? 0.1176 0.1060 0.1343 -0.0077 0.0031  0.0217  40  ASN   A O   
1125 C CB  A ASN   A 40  ? 0.1336 0.1431 0.1346 0.0002  -0.0059 0.0096  40  ASN   A CB  
1126 C CB  B ASN   A 40  ? 0.1336 0.1148 0.1443 0.0028  -0.0131 0.0105  40  ASN   A CB  
1127 C CG  A ASN   A 40  ? 0.1487 0.1445 0.1540 -0.0009 -0.0095 0.0166  40  ASN   A CG  
1128 C CG  B ASN   A 40  ? 0.1420 0.1162 0.1572 0.0044  -0.0146 0.0181  40  ASN   A CG  
1129 O OD1 A ASN   A 40  ? 0.1535 0.1391 0.1414 -0.0038 -0.0143 0.0219  40  ASN   A OD1 
1130 O OD1 B ASN   A 40  ? 0.1464 0.1183 0.1661 0.0017  -0.0075 0.0120  40  ASN   A OD1 
1131 N ND2 A ASN   A 40  ? 0.1551 0.1544 0.1779 0.0061  -0.0096 0.0065  40  ASN   A ND2 
1132 N ND2 B ASN   A 40  ? 0.1401 0.1312 0.1789 0.0042  -0.0175 -0.0094 40  ASN   A ND2 
1145 N N   A VAL   A 41  ? 0.1227 0.1272 0.1159 -0.0026 -0.0015 0.0087  41  VAL   A N   
1146 N N   B VAL   A 41  ? 0.1372 0.1133 0.1335 -0.0036 0.0064  0.0182  41  VAL   A N   
1147 C CA  A VAL   A 41  ? 0.1241 0.1228 0.1309 -0.0040 0.0082  0.0090  41  VAL   A CA  
1148 C CA  B VAL   A 41  ? 0.1351 0.1245 0.1443 -0.0022 0.0104  0.0215  41  VAL   A CA  
1149 C C   A VAL   A 41  ? 0.1234 0.1175 0.1318 -0.0008 0.0049  0.0148  41  VAL   A C   
1150 C C   B VAL   A 41  ? 0.1304 0.1209 0.1357 -0.0018 0.0193  0.0196  41  VAL   A C   
1151 O O   A VAL   A 41  ? 0.1297 0.1130 0.1231 0.0035  -0.0049 0.0148  41  VAL   A O   
1152 O O   B VAL   A 41  ? 0.1433 0.1220 0.1212 -0.0007 0.0138  0.0168  41  VAL   A O   
1153 C CB  A VAL   A 41  ? 0.1294 0.1170 0.1199 -0.0082 0.0110  -0.0029 41  VAL   A CB  
1154 C CB  B VAL   A 41  ? 0.1584 0.1422 0.1562 -0.0027 0.0267  0.0257  41  VAL   A CB  
1155 C CG1 A VAL   A 41  ? 0.1207 0.1066 0.1304 -0.0061 -0.0037 0.0009  41  VAL   A CG1 
1156 C CG1 B VAL   A 41  ? 0.1751 0.1502 0.1741 0.0003  0.0290  0.0170  41  VAL   A CG1 
1157 C CG2 A VAL   A 41  ? 0.1484 0.1266 0.1214 -0.0068 0.0170  -0.0080 41  VAL   A CG2 
1158 C CG2 B VAL   A 41  ? 0.1871 0.1580 0.1634 -0.0122 0.0354  0.0195  41  VAL   A CG2 
1177 N N   A TYR   A 42  ? 0.1136 0.1122 0.1549 -0.0030 0.0033  0.0233  42  TYR   A N   
1178 N N   B TYR   A 42  ? 0.1192 0.1135 0.1580 0.0002  0.0211  0.0199  42  TYR   A N   
1179 C CA  A TYR   A 42  ? 0.1143 0.1116 0.1484 -0.0115 0.0044  0.0235  42  TYR   A CA  
1180 C CA  B TYR   A 42  ? 0.1162 0.1128 0.1544 -0.0032 0.0160  0.0196  42  TYR   A CA  
1181 C C   A TYR   A 42  ? 0.1183 0.1107 0.1420 -0.0043 0.0027  0.0234  42  TYR   A C   
1182 C C   B TYR   A 42  ? 0.1193 0.1167 0.1584 -0.0021 0.0173  0.0298  42  TYR   A C   
1183 O O   A TYR   A 42  ? 0.1222 0.1120 0.1516 -0.0077 -0.0026 0.0084  42  TYR   A O   
1184 O O   B TYR   A 42  ? 0.1199 0.1194 0.1738 -0.0116 0.0237  0.0181  42  TYR   A O   
1185 C CB  A TYR   A 42  ? 0.1172 0.1294 0.1434 -0.0094 0.0178  0.0229  42  TYR   A CB  
1186 C CB  B TYR   A 42  ? 0.1247 0.1212 0.1463 -0.0018 0.0148  0.0286  42  TYR   A CB  
1187 C CG  A TYR   A 42  ? 0.1154 0.1377 0.1304 -0.0118 0.0147  0.0313  42  TYR   A CG  
1188 C CG  B TYR   A 42  ? 0.1336 0.1337 0.1440 0.0063  0.0096  0.0397  42  TYR   A CG  
1189 C CD1 A TYR   A 42  ? 0.1164 0.1451 0.1373 -0.0133 0.0163  0.0369  42  TYR   A CD1 
1190 C CD1 B TYR   A 42  ? 0.1384 0.1446 0.1480 -0.0059 0.0207  0.0388  42  TYR   A CD1 
1191 C CD2 A TYR   A 42  ? 0.1122 0.1457 0.1302 -0.0037 0.0047  0.0298  42  TYR   A CD2 
1192 C CD2 B TYR   A 42  ? 0.1478 0.1552 0.1663 0.0113  0.0084  0.0310  42  TYR   A CD2 
1193 C CE1 A TYR   A 42  ? 0.1157 0.1496 0.1294 -0.0095 0.0132  0.0294  42  TYR   A CE1 
1194 C CE1 B TYR   A 42  ? 0.1449 0.1506 0.1424 -0.0055 0.0226  0.0318  42  TYR   A CE1 
1195 C CE2 A TYR   A 42  ? 0.1094 0.1530 0.1297 -0.0092 0.0067  0.0371  42  TYR   A CE2 
1196 C CE2 B TYR   A 42  ? 0.1567 0.1713 0.1754 0.0118  0.0053  0.0310  42  TYR   A CE2 
1197 C CZ  A TYR   A 42  ? 0.1172 0.1569 0.1238 -0.0071 0.0093  0.0349  42  TYR   A CZ  
1198 C CZ  B TYR   A 42  ? 0.1601 0.1654 0.1496 0.0028  0.0158  0.0249  42  TYR   A CZ  
1199 O OH  A TYR   A 42  ? 0.1257 0.1730 0.1360 -0.0038 0.0027  0.0262  42  TYR   A OH  
1200 O OH  B TYR   A 42  ? 0.1743 0.1850 0.1706 0.0005  0.0116  0.0120  42  TYR   A OH  
1219 N N   A LEU   A 43  ? 0.1222 0.1134 0.1241 -0.0058 0.0087  0.0088  43  LEU   A N   
1220 N N   B LEU   A 43  ? 0.1176 0.1157 0.1570 -0.0026 0.0107  0.0166  43  LEU   A N   
1221 C CA  A LEU   A 43  ? 0.1164 0.1180 0.1257 -0.0110 0.0084  0.0059  43  LEU   A CA  
1222 C CA  B LEU   A 43  ? 0.1127 0.1142 0.1490 -0.0020 0.0030  0.0201  43  LEU   A CA  
1223 C C   A LEU   A 43  ? 0.1224 0.1257 0.1351 -0.0107 0.0108  -0.0006 43  LEU   A C   
1224 C C   B LEU   A 43  ? 0.1194 0.1157 0.1417 -0.0023 0.0041  0.0115  43  LEU   A C   
1225 O O   A LEU   A 43  ? 0.1309 0.1267 0.1429 -0.0015 0.0016  -0.0009 43  LEU   A O   
1226 O O   B LEU   A 43  ? 0.1374 0.1212 0.1504 0.0042  -0.0111 0.0094  43  LEU   A O   
1227 C CB  A LEU   A 43  ? 0.1226 0.1213 0.1360 -0.0117 0.0048  0.0012  43  LEU   A CB  
1228 C CB  B LEU   A 43  ? 0.1154 0.1078 0.1572 -0.0075 0.0053  0.0203  43  LEU   A CB  
1229 C CG  A LEU   A 43  ? 0.1307 0.1276 0.1448 -0.0167 0.0010  0.0012  43  LEU   A CG  
1230 C CG  B LEU   A 43  ? 0.1157 0.1121 0.1660 0.0028  0.0091  0.0160  43  LEU   A CG  
1231 C CD1 A LEU   A 43  ? 0.1334 0.1347 0.1507 -0.0194 0.0053  0.0032  43  LEU   A CD1 
1232 C CD1 B LEU   A 43  ? 0.1263 0.1213 0.1770 0.0056  0.0080  0.0156  43  LEU   A CD1 
1233 C CD2 A LEU   A 43  ? 0.1354 0.1299 0.1444 -0.0188 -0.0031 0.0066  43  LEU   A CD2 
1234 C CD2 B LEU   A 43  ? 0.1262 0.1153 0.1715 -0.0006 0.0068  0.0321  43  LEU   A CD2 
1257 N N   A LYS   A 44  ? 0.1299 0.1304 0.1490 -0.0109 0.0140  -0.0001 44  LYS   A N   
1258 N N   B LYS   A 44  ? 0.1207 0.1152 0.1417 0.0024  -0.0014 0.0168  44  LYS   A N   
1259 C CA  A LYS   A 44  ? 0.1373 0.1371 0.1635 -0.0143 0.0150  0.0063  44  LYS   A CA  
1260 C CA  B LYS   A 44  ? 0.1295 0.1141 0.1343 0.0011  0.0038  0.0258  44  LYS   A CA  
1261 C C   A LYS   A 44  ? 0.1254 0.1314 0.1447 -0.0065 0.0037  0.0042  44  LYS   A C   
1262 C C   B LYS   A 44  ? 0.1241 0.1101 0.1262 0.0018  -0.0038 0.0177  44  LYS   A C   
1263 O O   A LYS   A 44  ? 0.1293 0.1425 0.1607 -0.0002 -0.0074 -0.0079 44  LYS   A O   
1264 O O   B LYS   A 44  ? 0.1317 0.1254 0.1459 -0.0032 -0.0023 -0.0048 44  LYS   A O   
1265 C CB  A LYS   A 44  ? 0.1675 0.1521 0.1954 -0.0194 0.0162  0.0126  44  LYS   A CB  
1266 C CB  B LYS   A 44  ? 0.1719 0.1327 0.1568 0.0124  0.0181  0.0381  44  LYS   A CB  
1267 C CG  A LYS   A 44  ? 0.1980 0.1735 0.2382 -0.0254 0.0278  0.0274  44  LYS   A CG  
1268 C CG  B LYS   A 44  ? 0.2020 0.1756 0.2202 0.0103  0.0390  0.0507  44  LYS   A CG  
1269 C CD  A LYS   A 44  ? 0.2279 0.2086 0.2979 -0.0289 0.0282  0.0225  44  LYS   A CD  
1270 C CD  B LYS   A 44  ? 0.2296 0.2384 0.3145 0.0019  0.0272  0.0403  44  LYS   A CD  
1271 C CE  A LYS   A 44  ? 0.2462 0.2345 0.3404 -0.0269 0.0299  0.0177  44  LYS   A CE  
1272 C CE  B LYS   A 44  ? 0.2420 0.2738 0.3731 -0.0032 0.0197  0.0346  44  LYS   A CE  
1273 N NZ  A LYS   A 44  ? 0.2554 0.2519 0.3615 -0.0273 0.0322  0.0149  44  LYS   A NZ  
1274 N NZ  B LYS   A 44  ? 0.2494 0.2923 0.3984 -0.0129 0.0160  0.0314  44  LYS   A NZ  
1301 N N   A HIS   A 45  ? 0.1162 0.1230 0.1343 -0.0076 0.0060  0.0078  45  HIS   A N   
1302 N N   B HIS   A 45  ? 0.1231 0.1099 0.1391 -0.0033 -0.0099 0.0154  45  HIS   A N   
1303 C CA  A HIS   A 45  ? 0.1134 0.1163 0.1271 -0.0000 0.0072  0.0071  45  HIS   A CA  
1304 C CA  B HIS   A 45  ? 0.1284 0.1159 0.1525 0.0014  -0.0060 0.0087  45  HIS   A CA  
1305 C C   A HIS   A 45  ? 0.1151 0.1162 0.1266 0.0003  0.0054  0.0116  45  HIS   A C   
1306 C C   B HIS   A 45  ? 0.1350 0.1237 0.1530 0.0001  -0.0088 0.0117  45  HIS   A C   
1307 O O   A HIS   A 45  ? 0.1228 0.1185 0.1505 0.0007  0.0065  0.0020  45  HIS   A O   
1308 O O   B HIS   A 45  ? 0.1578 0.1360 0.1899 0.0150  -0.0083 0.0050  45  HIS   A O   
1309 C CB  A HIS   A 45  ? 0.1143 0.1116 0.1151 0.0007  0.0091  0.0057  45  HIS   A CB  
1310 C CB  B HIS   A 45  ? 0.1299 0.1112 0.1483 -0.0044 0.0005  0.0006  45  HIS   A CB  
1311 C CG  A HIS   A 45  ? 0.1116 0.1030 0.1028 -0.0061 0.0037  0.0117  45  HIS   A CG  
1312 C CG  B HIS   A 45  ? 0.1202 0.1140 0.1404 -0.0044 0.0085  0.0096  45  HIS   A CG  
1313 N ND1 A HIS   A 45  ? 0.1051 0.1036 0.0855 -0.0122 -0.0037 0.0017  45  HIS   A ND1 
1314 N ND1 B HIS   A 45  ? 0.1182 0.1216 0.1642 -0.0017 0.0050  0.0128  45  HIS   A ND1 
1315 C CD2 A HIS   A 45  ? 0.1155 0.1121 0.1166 -0.0134 -0.0013 0.0208  45  HIS   A CD2 
1316 C CD2 B HIS   A 45  ? 0.1121 0.1139 0.1331 -0.0076 0.0044  0.0037  45  HIS   A CD2 
1317 C CE1 A HIS   A 45  ? 0.1102 0.1187 0.1104 -0.0111 -0.0026 0.0158  45  HIS   A CE1 
1318 C CE1 B HIS   A 45  ? 0.1130 0.1196 0.1221 -0.0071 -0.0034 0.0079  45  HIS   A CE1 
1319 N NE2 A HIS   A 45  ? 0.1189 0.1208 0.1238 -0.0050 0.0028  0.0247  45  HIS   A NE2 
1320 N NE2 B HIS   A 45  ? 0.1160 0.1165 0.1200 -0.0040 0.0003  0.0073  45  HIS   A NE2 
1335 N N   A GLY   A 46  ? 0.1188 0.1200 0.1310 0.0069  -0.0002 0.0198  46  GLY   A N   
1336 N N   B GLY   A 46  ? 0.1344 0.1256 0.1568 -0.0025 -0.0192 0.0166  46  GLY   A N   
1337 C CA  A GLY   A 46  ? 0.1230 0.1232 0.1456 0.0131  -0.0089 0.0175  46  GLY   A CA  
1338 C CA  B GLY   A 46  ? 0.1385 0.1377 0.1792 0.0014  -0.0159 0.0195  46  GLY   A CA  
1339 C C   A GLY   A 46  ? 0.1303 0.1189 0.1515 0.0197  -0.0125 0.0285  46  GLY   A C   
1340 C C   B GLY   A 46  ? 0.1361 0.1354 0.1616 0.0072  -0.0061 0.0187  46  GLY   A C   
1341 O O   A GLY   A 46  ? 0.1388 0.1113 0.1487 0.0291  -0.0238 0.0439  46  GLY   A O   
1342 O O   B GLY   A 46  ? 0.1507 0.1448 0.1806 -0.0021 -0.0078 0.0025  46  GLY   A O   
1349 N N   A GLY   A 47  ? 0.1242 0.1261 0.1599 0.0128  -0.0035 0.0191  47  GLY   A N   
1350 N N   B GLY   A 47  ? 0.1352 0.1368 0.1586 0.0072  0.0070  0.0125  47  GLY   A N   
1351 C CA  A GLY   A 47  ? 0.1200 0.1314 0.1540 0.0145  -0.0040 0.0070  47  GLY   A CA  
1352 C CA  B GLY   A 47  ? 0.1322 0.1378 0.1671 0.0074  -0.0030 0.0098  47  GLY   A CA  
1353 C C   A GLY   A 47  ? 0.1109 0.1296 0.1467 0.0120  -0.0012 0.0018  47  GLY   A C   
1354 C C   B GLY   A 47  ? 0.1218 0.1224 0.1472 0.0089  -0.0016 0.0131  47  GLY   A C   
1355 O O   A GLY   A 47  ? 0.1117 0.1270 0.1635 0.0133  0.0048  0.0068  47  GLY   A O   
1356 O O   B GLY   A 47  ? 0.1195 0.1157 0.1693 0.0188  -0.0121 0.0153  47  GLY   A O   
1363 N N   A GLY   A 48  ? 0.1024 0.1293 0.1420 0.0167  -0.0008 -0.0081 48  GLY   A N   
1364 N N   B GLY   A 48  ? 0.1207 0.1296 0.1559 0.0110  0.0024  0.0124  48  GLY   A N   
1365 C CA  A GLY   A 48  ? 0.1000 0.1327 0.1440 0.0085  -0.0004 -0.0086 48  GLY   A CA  
1366 C CA  B GLY   A 48  ? 0.1187 0.1233 0.1498 0.0062  0.0006  0.0069  48  GLY   A CA  
1367 C C   A GLY   A 48  ? 0.1034 0.1299 0.1281 0.0004  0.0009  0.0001  48  GLY   A C   
1368 C C   B GLY   A 48  ? 0.1186 0.1227 0.1508 -0.0003 0.0049  0.0038  48  GLY   A C   
1369 O O   A GLY   A 48  ? 0.1119 0.1343 0.1221 -0.0050 -0.0045 0.0111  48  GLY   A O   
1370 O O   B GLY   A 48  ? 0.1311 0.1216 0.1587 0.0080  0.0056  -0.0130 48  GLY   A O   
1377 N N   A VAL   A 49  ? 0.1152 0.1270 0.1465 -0.0078 0.0048  0.0122  49  VAL   A N   
1378 N N   B VAL   A 49  ? 0.1130 0.1171 0.1705 -0.0028 -0.0054 -0.0018 49  VAL   A N   
1379 C CA  A VAL   A 49  ? 0.1287 0.1281 0.1578 -0.0109 0.0042  0.0176  49  VAL   A CA  
1380 C CA  B VAL   A 49  ? 0.1120 0.1198 0.1699 -0.0020 -0.0110 0.0107  49  VAL   A CA  
1381 C C   A VAL   A 49  ? 0.1196 0.1107 0.1400 -0.0095 0.0061  0.0277  49  VAL   A C   
1382 C C   B VAL   A 49  ? 0.1167 0.1126 0.1527 0.0036  -0.0073 -0.0061 49  VAL   A C   
1383 O O   A VAL   A 49  ? 0.1223 0.1086 0.1458 -0.0150 -0.0003 0.0111  49  VAL   A O   
1384 O O   B VAL   A 49  ? 0.1214 0.1207 0.1385 0.0033  0.0065  -0.0041 49  VAL   A O   
1385 C CB  A VAL   A 49  ? 0.1486 0.1387 0.1825 -0.0145 -0.0069 0.0038  49  VAL   A CB  
1386 C CB  B VAL   A 49  ? 0.1092 0.1176 0.1970 -0.0073 -0.0265 0.0191  49  VAL   A CB  
1387 C CG1 A VAL   A 49  ? 0.1530 0.1411 0.1915 -0.0116 -0.0041 0.0020  49  VAL   A CG1 
1388 C CG1 B VAL   A 49  ? 0.1081 0.1134 0.1988 -0.0056 -0.0294 0.0276  49  VAL   A CG1 
1389 C CG2 A VAL   A 49  ? 0.1591 0.1463 0.2077 -0.0219 -0.0111 -0.0002 49  VAL   A CG2 
1390 C CG2 B VAL   A 49  ? 0.1129 0.1258 0.2312 -0.0054 -0.0281 0.0271  49  VAL   A CG2 
1409 N N   A ALA   A 50  ? 0.1109 0.1081 0.1267 -0.0021 -0.0008 0.0400  50  ALA   A N   
1410 N N   B ALA   A 50  ? 0.1143 0.1128 0.1296 0.0061  -0.0111 -0.0074 50  ALA   A N   
1411 C CA  A ALA   A 50  ? 0.1101 0.1058 0.1267 -0.0043 -0.0082 0.0474  50  ALA   A CA  
1412 C CA  B ALA   A 50  ? 0.1109 0.1155 0.1385 -0.0060 -0.0003 -0.0145 50  ALA   A CA  
1413 C C   A ALA   A 50  ? 0.1055 0.1091 0.1329 0.0034  -0.0014 0.0356  50  ALA   A C   
1414 C C   B ALA   A 50  ? 0.1048 0.1164 0.1372 -0.0100 -0.0034 -0.0116 50  ALA   A C   
1415 O O   A ALA   A 50  ? 0.1080 0.1083 0.1371 0.0105  0.0041  0.0331  50  ALA   A O   
1416 O O   B ALA   A 50  ? 0.1099 0.1143 0.1465 -0.0104 -0.0052 -0.0096 50  ALA   A O   
1417 C CB  A ALA   A 50  ? 0.1125 0.1064 0.1427 -0.0054 -0.0097 0.0511  50  ALA   A CB  
1418 C CB  B ALA   A 50  ? 0.1161 0.1138 0.1523 -0.0087 0.0070  -0.0249 50  ALA   A CB  
1429 N N   A GLY   A 51  ? 0.1118 0.1067 0.1372 0.0089  -0.0136 0.0332  51  GLY   A N   
1430 N N   B GLY   A 51  ? 0.1196 0.1081 0.1575 -0.0019 -0.0124 -0.0060 51  GLY   A N   
1431 C CA  A GLY   A 51  ? 0.1167 0.1127 0.1524 0.0091  -0.0092 0.0375  51  GLY   A CA  
1432 C CA  B GLY   A 51  ? 0.1278 0.1079 0.1564 -0.0001 -0.0136 -0.0087 51  GLY   A CA  
1433 C C   A GLY   A 51  ? 0.1070 0.1211 0.1516 0.0060  -0.0003 0.0298  51  GLY   A C   
1434 C C   B GLY   A 51  ? 0.1130 0.1167 0.1533 0.0105  -0.0133 -0.0232 51  GLY   A C   
1435 O O   A GLY   A 51  ? 0.1148 0.1270 0.1531 -0.0024 0.0006  0.0350  51  GLY   A O   
1436 O O   B GLY   A 51  ? 0.1231 0.1238 0.1695 0.0057  -0.0182 -0.0291 51  GLY   A O   
1443 N N   A ALA   A 52  ? 0.1048 0.1298 0.1632 -0.0010 0.0003  0.0282  52  ALA   A N   
1444 N N   B ALA   A 52  ? 0.1141 0.1230 0.1536 0.0018  -0.0028 -0.0224 52  ALA   A N   
1445 C CA  A ALA   A 52  ? 0.1118 0.1410 0.1617 -0.0034 0.0012  0.0219  52  ALA   A CA  
1446 C CA  B ALA   A 52  ? 0.1223 0.1327 0.1669 -0.0016 -0.0007 -0.0128 52  ALA   A CA  
1447 C C   A ALA   A 52  ? 0.1105 0.1437 0.1597 -0.0014 0.0149  0.0219  52  ALA   A C   
1448 C C   B ALA   A 52  ? 0.1198 0.1292 0.1500 -0.0106 0.0097  -0.0165 52  ALA   A C   
1449 O O   A ALA   A 52  ? 0.1139 0.1495 0.1663 0.0075  0.0130  0.0200  52  ALA   A O   
1450 O O   B ALA   A 52  ? 0.1259 0.1395 0.1645 -0.0064 0.0033  -0.0256 52  ALA   A O   
1451 C CB  A ALA   A 52  ? 0.1156 0.1589 0.1661 -0.0076 -0.0068 0.0145  52  ALA   A CB  
1452 C CB  B ALA   A 52  ? 0.1317 0.1598 0.1871 -0.0027 -0.0085 -0.0056 52  ALA   A CB  
1463 N N   A LEU   A 53  ? 0.1118 0.1407 0.1563 0.0000  0.0162  0.0244  53  LEU   A N   
1464 N N   B LEU   A 53  ? 0.1121 0.1226 0.1391 -0.0076 0.0014  -0.0047 53  LEU   A N   
1465 C CA  A LEU   A 53  ? 0.1267 0.1413 0.1602 -0.0074 0.0173  0.0164  53  LEU   A CA  
1466 C CA  B LEU   A 53  ? 0.1217 0.1276 0.1248 -0.0079 0.0009  -0.0003 53  LEU   A CA  
1467 C C   A LEU   A 53  ? 0.1240 0.1393 0.1572 -0.0066 0.0167  0.0066  53  LEU   A C   
1468 C C   B LEU   A 53  ? 0.1179 0.1292 0.1044 0.0004  0.0036  0.0041  53  LEU   A C   
1469 O O   A LEU   A 53  ? 0.1286 0.1333 0.1758 -0.0111 0.0175  -0.0041 53  LEU   A O   
1470 O O   B LEU   A 53  ? 0.1325 0.1276 0.1112 0.0056  -0.0016 0.0093  53  LEU   A O   
1471 C CB  A LEU   A 53  ? 0.1377 0.1430 0.1653 -0.0122 0.0246  0.0133  53  LEU   A CB  
1472 C CB  B LEU   A 53  ? 0.1221 0.1326 0.1217 -0.0085 -0.0003 0.0060  53  LEU   A CB  
1473 C CG  A LEU   A 53  ? 0.1489 0.1440 0.1728 -0.0210 0.0180  0.0132  53  LEU   A CG  
1474 C CG  B LEU   A 53  ? 0.1350 0.1329 0.1320 -0.0086 -0.0038 0.0091  53  LEU   A CG  
1475 C CD1 A LEU   A 53  ? 0.1545 0.1470 0.1799 -0.0147 0.0219  0.0149  53  LEU   A CD1 
1476 C CD1 B LEU   A 53  ? 0.1472 0.1324 0.1340 -0.0058 -0.0168 0.0032  53  LEU   A CD1 
1477 C CD2 A LEU   A 53  ? 0.1601 0.1554 0.1756 -0.0292 0.0078  0.0138  53  LEU   A CD2 
1478 C CD2 B LEU   A 53  ? 0.1459 0.1486 0.1444 -0.0194 -0.0034 0.0166  53  LEU   A CD2 
1501 N N   A ASN   A 54  ? 0.1178 0.1330 0.1472 -0.0073 0.0003  0.0084  54  ASN   A N   
1502 N N   B ASN   A 54  ? 0.1060 0.1265 0.1117 -0.0013 -0.0044 0.0009  54  ASN   A N   
1503 C CA  A ASN   A 54  ? 0.1175 0.1260 0.1493 -0.0078 -0.0011 0.0045  54  ASN   A CA  
1504 C CA  B ASN   A 54  ? 0.1056 0.1234 0.1356 0.0001  0.0025  0.0007  54  ASN   A CA  
1505 C C   A ASN   A 54  ? 0.1218 0.1295 0.1468 -0.0079 0.0004  0.0055  54  ASN   A C   
1506 C C   B ASN   A 54  ? 0.1179 0.1260 0.1422 -0.0099 0.0031  0.0018  54  ASN   A C   
1507 O O   A ASN   A 54  ? 0.1245 0.1369 0.1536 -0.0064 -0.0063 0.0020  54  ASN   A O   
1508 O O   B ASN   A 54  ? 0.1228 0.1318 0.1565 -0.0074 -0.0047 -0.0125 54  ASN   A O   
1509 C CB  A ASN   A 54  ? 0.1179 0.1199 0.1550 -0.0161 -0.0090 0.0018  54  ASN   A CB  
1510 C CB  B ASN   A 54  ? 0.1059 0.1250 0.1382 -0.0029 -0.0066 0.0068  54  ASN   A CB  
1511 C CG  A ASN   A 54  ? 0.1219 0.1181 0.1581 -0.0100 -0.0073 -0.0027 54  ASN   A CG  
1512 C CG  B ASN   A 54  ? 0.1080 0.1265 0.1218 0.0063  -0.0016 -0.0057 54  ASN   A CG  
1513 O OD1 A ASN   A 54  ? 0.1245 0.1117 0.1759 -0.0102 -0.0009 0.0103  54  ASN   A OD1 
1514 O OD1 B ASN   A 54  ? 0.1042 0.1205 0.1220 0.0034  -0.0051 -0.0084 54  ASN   A OD1 
1515 N ND2 A ASN   A 54  ? 0.1176 0.1167 0.1629 -0.0101 -0.0166 0.0010  54  ASN   A ND2 
1516 N ND2 B ASN   A 54  ? 0.1130 0.1238 0.1381 0.0013  -0.0069 0.0089  54  ASN   A ND2 
1529 N N   . LYS   A 55  ? 0.1214 0.1304 0.1520 0.0010  0.0043  0.0027  55  LYS   A N   
1530 C CA  . LYS   A 55  ? 0.1319 0.1387 0.1570 0.0074  -0.0038 -0.0075 55  LYS   A CA  
1531 C C   . LYS   A 55  ? 0.1231 0.1431 0.1545 -0.0021 -0.0032 -0.0085 55  LYS   A C   
1532 O O   . LYS   A 55  ? 0.1348 0.1549 0.1616 0.0065  -0.0090 -0.0232 55  LYS   A O   
1533 C CB  . LYS   A 55  ? 0.1461 0.1532 0.1750 0.0212  -0.0052 -0.0142 55  LYS   A CB  
1534 C CG  . LYS   A 55  ? 0.1680 0.1904 0.1954 0.0389  -0.0236 -0.0301 55  LYS   A CG  
1535 C CD  . LYS   A 55  ? 0.1814 0.2290 0.2185 0.0533  -0.0237 -0.0271 55  LYS   A CD  
1536 C CE  . LYS   A 55  ? 0.1994 0.2612 0.2346 0.0725  -0.0275 -0.0288 55  LYS   A CE  
1537 N NZ  . LYS   A 55  ? 0.2125 0.2799 0.2351 0.0753  -0.0301 -0.0206 55  LYS   A NZ  
1552 N N   . ALA   A 56  ? 0.1290 0.1542 0.1622 -0.0096 0.0038  -0.0139 56  ALA   A N   
1553 C CA  . ALA   A 56  ? 0.1374 0.1675 0.1566 -0.0106 0.0102  -0.0123 56  ALA   A CA  
1554 C C   . ALA   A 56  ? 0.1445 0.1764 0.1362 -0.0084 0.0101  -0.0228 56  ALA   A C   
1555 O O   . ALA   A 56  ? 0.1532 0.2041 0.1496 0.0031  0.0156  -0.0058 56  ALA   A O   
1556 C CB  . ALA   A 56  ? 0.1476 0.1853 0.1740 -0.0178 0.0089  0.0010  56  ALA   A CB  
1562 N N   . THR   A 57  ? 0.1300 0.1599 0.1279 -0.0087 0.0089  -0.0124 57  THR   A N   
1563 C CA  . THR   A 57  ? 0.1366 0.1562 0.1358 -0.0082 0.0043  -0.0068 57  THR   A CA  
1564 C C   . THR   A 57  ? 0.1349 0.1630 0.1342 -0.0072 0.0056  -0.0180 57  THR   A C   
1565 O O   . THR   A 57  ? 0.1376 0.1714 0.1514 -0.0134 -0.0064 -0.0226 57  THR   A O   
1566 C CB  . THR   A 57  ? 0.1324 0.1566 0.1399 -0.0092 0.0047  0.0030  57  THR   A CB  
1567 O OG1 . THR   A 57  ? 0.1244 0.1456 0.1353 -0.0117 0.0015  -0.0042 57  THR   A OG1 
1568 C CG2 . THR   A 57  ? 0.1437 0.1549 0.1281 -0.0060 0.0025  0.0034  57  THR   A CG2 
1576 N N   . ASN   A 58  ? 0.1380 0.1561 0.1601 -0.0036 0.0046  -0.0218 58  ASN   A N   
1577 C CA  . ASN   A 58  ? 0.1569 0.1518 0.1801 -0.0114 0.0125  -0.0379 58  ASN   A CA  
1578 C C   . ASN   A 58  ? 0.1354 0.1438 0.1586 -0.0032 -0.0059 -0.0153 58  ASN   A C   
1579 O O   . ASN   A 58  ? 0.1439 0.1517 0.1778 -0.0166 -0.0012 -0.0276 58  ASN   A O   
1580 C CB  . ASN   A 58  ? 0.2044 0.1692 0.2226 -0.0181 0.0394  -0.0429 58  ASN   A CB  
1581 C CG  . ASN   A 58  ? 0.2541 0.1906 0.2958 -0.0186 0.0395  -0.0352 58  ASN   A CG  
1582 O OD1 . ASN   A 58  ? 0.2774 0.1826 0.3424 0.0188  0.0742  -0.0210 58  ASN   A OD1 
1583 N ND2 . ASN   A 58  ? 0.2688 0.2012 0.3135 -0.0254 0.0204  -0.0378 58  ASN   A ND2 
1590 N N   . ASN   A 59  ? 0.1228 0.1320 0.1540 -0.0069 -0.0055 -0.0145 59  ASN   A N   
1591 C CA  . ASN   A 59  ? 0.1243 0.1204 0.1363 -0.0023 -0.0126 -0.0042 59  ASN   A CA  
1592 C C   . ASN   A 59  ? 0.1237 0.1225 0.1290 -0.0096 -0.0080 -0.0029 59  ASN   A C   
1593 O O   . ASN   A 59  ? 0.1229 0.1322 0.1446 -0.0083 -0.0030 0.0087  59  ASN   A O   
1594 C CB  . ASN   A 59  ? 0.1352 0.1176 0.1506 0.0046  -0.0233 -0.0152 59  ASN   A CB  
1595 C CG  . ASN   A 59  ? 0.1322 0.1232 0.1488 0.0021  -0.0278 -0.0077 59  ASN   A CG  
1596 O OD1 . ASN   A 59  ? 0.1468 0.1343 0.1478 -0.0132 -0.0191 0.0028  59  ASN   A OD1 
1597 N ND2 . ASN   A 59  ? 0.1476 0.1369 0.1656 -0.0195 -0.0184 0.0043  59  ASN   A ND2 
1604 N N   . ALA   A 60  ? 0.1180 0.1256 0.1444 0.0004  -0.0103 0.0025  60  ALA   A N   
1605 C CA  . ALA   A 60  ? 0.1265 0.1281 0.1451 -0.0042 -0.0084 0.0037  60  ALA   A CA  
1606 C C   . ALA   A 60  ? 0.1177 0.1292 0.1431 -0.0001 -0.0045 -0.0002 60  ALA   A C   
1607 O O   . ALA   A 60  ? 0.1220 0.1285 0.1687 -0.0050 -0.0116 -0.0031 60  ALA   A O   
1608 C CB  . ALA   A 60  ? 0.1329 0.1367 0.1614 -0.0018 -0.0157 -0.0101 60  ALA   A CB  
1614 N N   . MET   A 61  ? 0.1173 0.1205 0.1395 -0.0065 0.0018  -0.0035 61  MET   A N   
1615 C CA  . MET   A 61  ? 0.1164 0.1134 0.1412 -0.0042 0.0075  0.0079  61  MET   A CA  
1616 C C   . MET   A 61  ? 0.1143 0.1138 0.1486 -0.0059 -0.0070 -0.0040 61  MET   A C   
1617 O O   . MET   A 61  ? 0.1152 0.1204 0.1564 -0.0037 0.0058  0.0078  61  MET   A O   
1618 C CB  . MET   A 61  ? 0.1235 0.1167 0.1409 -0.0075 0.0104  0.0006  61  MET   A CB  
1619 C CG  . MET   A 61  ? 0.1228 0.1244 0.1604 -0.0035 -0.0017 0.0028  61  MET   A CG  
1620 S SD  . MET   A 61  ? 0.1243 0.1296 0.1745 -0.0119 -0.0013 -0.0124 61  MET   A SD  
1621 C CE  . MET   A 61  ? 0.1410 0.1420 0.2174 -0.0188 0.0131  -0.0096 61  MET   A CE  
1631 N N   . GLN   A 62  ? 0.1111 0.1123 0.1484 -0.0090 0.0024  -0.0012 62  GLN   A N   
1632 C CA  . GLN   A 62  ? 0.1160 0.1139 0.1470 -0.0089 0.0015  0.0035  62  GLN   A CA  
1633 C C   . GLN   A 62  ? 0.1236 0.1103 0.1405 -0.0018 0.0068  -0.0006 62  GLN   A C   
1634 O O   . GLN   A 62  ? 0.1228 0.1223 0.1487 -0.0074 0.0027  -0.0018 62  GLN   A O   
1635 C CB  . GLN   A 62  ? 0.1231 0.1162 0.1467 -0.0039 0.0003  -0.0013 62  GLN   A CB  
1636 C CG  . GLN   A 62  ? 0.1238 0.1113 0.1505 -0.0058 -0.0084 0.0135  62  GLN   A CG  
1637 C CD  . GLN   A 62  ? 0.1288 0.1130 0.1483 -0.0043 -0.0017 0.0103  62  GLN   A CD  
1638 O OE1 . GLN   A 62  ? 0.1313 0.1290 0.1596 -0.0053 -0.0055 0.0000  62  GLN   A OE1 
1639 N NE2 . GLN   A 62  ? 0.1348 0.1203 0.1524 0.0012  0.0006  0.0012  62  GLN   A NE2 
1648 N N   . VAL   A 63  ? 0.1178 0.1205 0.1563 -0.0085 0.0064  -0.0118 63  VAL   A N   
1649 C CA  . VAL   A 63  ? 0.1199 0.1271 0.1797 -0.0121 0.0054  -0.0111 63  VAL   A CA  
1650 C C   . VAL   A 63  ? 0.1068 0.1328 0.1673 -0.0181 -0.0034 -0.0121 63  VAL   A C   
1651 O O   . VAL   A 63  ? 0.1103 0.1291 0.1843 -0.0160 -0.0000 -0.0056 63  VAL   A O   
1652 C CB  . VAL   A 63  ? 0.1340 0.1441 0.2136 -0.0176 -0.0028 -0.0312 63  VAL   A CB  
1653 C CG1 . VAL   A 63  ? 0.1439 0.1635 0.2569 -0.0146 -0.0084 -0.0606 63  VAL   A CG1 
1654 C CG2 . VAL   A 63  ? 0.1376 0.1366 0.2235 -0.0128 0.0121  -0.0283 63  VAL   A CG2 
1664 N N   . GLU   A 64  ? 0.1116 0.1308 0.1585 -0.0109 0.0028  -0.0094 64  GLU   A N   
1665 C CA  . GLU   A 64  ? 0.1115 0.1286 0.1507 -0.0075 -0.0101 0.0013  64  GLU   A CA  
1666 C C   . GLU   A 64  ? 0.1111 0.1235 0.1574 -0.0076 0.0029  0.0079  64  GLU   A C   
1667 O O   . GLU   A 64  ? 0.1205 0.1327 0.1510 -0.0014 -0.0022 0.0054  64  GLU   A O   
1668 C CB  . GLU   A 64  ? 0.1254 0.1407 0.1644 -0.0076 -0.0009 0.0039  64  GLU   A CB  
1669 C CG  . GLU   A 64  ? 0.1273 0.1404 0.1819 -0.0098 -0.0031 -0.0055 64  GLU   A CG  
1670 C CD  . GLU   A 64  ? 0.1401 0.1475 0.1854 -0.0181 -0.0020 -0.0051 64  GLU   A CD  
1671 O OE1 . GLU   A 64  ? 0.1426 0.1625 0.2019 -0.0236 0.0076  0.0049  64  GLU   A OE1 
1672 O OE2 . GLU   A 64  ? 0.1558 0.1496 0.1789 -0.0215 -0.0080 0.0112  64  GLU   A OE2 
1679 N N   . SER   A 65  ? 0.1028 0.1247 0.1487 -0.0004 0.0037  0.0043  65  SER   A N   
1680 C CA  . SER   A 65  ? 0.1114 0.1168 0.1562 -0.0043 0.0050  0.0007  65  SER   A CA  
1681 C C   . SER   A 65  ? 0.1120 0.1232 0.1533 -0.0024 -0.0023 0.0008  65  SER   A C   
1682 O O   . SER   A 65  ? 0.1178 0.1305 0.1751 -0.0032 0.0163  -0.0014 65  SER   A O   
1683 C CB  . SER   A 65  ? 0.1121 0.1206 0.1504 -0.0068 0.0016  0.0106  65  SER   A CB  
1684 O OG  . SER   A 65  ? 0.1160 0.1269 0.1533 -0.0097 -0.0015 0.0131  65  SER   A OG  
1690 N N   . ASP   A 66  ? 0.1181 0.1250 0.1513 -0.0062 0.0090  0.0083  66  ASP   A N   
1691 C CA  . ASP   A 66  ? 0.1273 0.1346 0.1626 -0.0054 0.0084  0.0172  66  ASP   A CA  
1692 C C   . ASP   A 66  ? 0.1264 0.1285 0.1608 -0.0142 0.0149  0.0141  66  ASP   A C   
1693 O O   . ASP   A 66  ? 0.1291 0.1387 0.1827 -0.0048 0.0264  0.0292  66  ASP   A O   
1694 C CB  . ASP   A 66  ? 0.1365 0.1392 0.1981 0.0047  0.0114  0.0375  66  ASP   A CB  
1695 C CG  . ASP   A 66  ? 0.1608 0.1525 0.2137 -0.0005 0.0026  0.0498  66  ASP   A CG  
1696 O OD1 . ASP   A 66  ? 0.1617 0.1833 0.1997 -0.0105 -0.0081 0.0392  66  ASP   A OD1 
1697 O OD2 . ASP   A 66  ? 0.1757 0.1686 0.2922 0.0182  -0.0107 0.0318  66  ASP   A OD2 
1702 N N   . ASP   A 67  ? 0.1181 0.1326 0.1822 -0.0068 0.0077  0.0182  67  ASP   A N   
1703 C CA  . ASP   A 67  ? 0.1137 0.1499 0.2041 -0.0005 0.0010  0.0325  67  ASP   A CA  
1704 C C   . ASP   A 67  ? 0.1197 0.1526 0.1916 0.0034  0.0137  0.0286  67  ASP   A C   
1705 O O   . ASP   A 67  ? 0.1158 0.1670 0.2104 0.0017  0.0284  0.0360  67  ASP   A O   
1706 C CB  . ASP   A 67  ? 0.1245 0.1606 0.2322 -0.0023 -0.0090 0.0379  67  ASP   A CB  
1707 C CG  . ASP   A 67  ? 0.1235 0.1765 0.2637 -0.0132 -0.0253 0.0523  67  ASP   A CG  
1708 O OD1 . ASP   A 67  ? 0.1305 0.2001 0.3559 -0.0173 -0.0399 0.0694  67  ASP   A OD1 
1709 O OD2 . ASP   A 67  ? 0.1295 0.1791 0.2432 -0.0021 -0.0245 0.0431  67  ASP   A OD2 
1714 N N   . TYR   A 68  ? 0.1232 0.1376 0.1836 0.0063  0.0192  0.0329  68  TYR   A N   
1715 C CA  . TYR   A 68  ? 0.1336 0.1297 0.1855 0.0056  0.0200  0.0325  68  TYR   A CA  
1716 C C   . TYR   A 68  ? 0.1294 0.1292 0.1890 0.0003  0.0286  0.0205  68  TYR   A C   
1717 O O   . TYR   A 68  ? 0.1374 0.1421 0.2044 0.0127  0.0354  0.0237  68  TYR   A O   
1718 C CB  . TYR   A 68  ? 0.1421 0.1288 0.1940 0.0065  0.0402  0.0324  68  TYR   A CB  
1719 C CG  . TYR   A 68  ? 0.1474 0.1467 0.2195 0.0054  0.0588  0.0326  68  TYR   A CG  
1720 C CD1 . TYR   A 68  ? 0.1499 0.1495 0.2419 -0.0157 0.0496  0.0067  68  TYR   A CD1 
1721 C CD2 . TYR   A 68  ? 0.1661 0.1478 0.2582 0.0124  0.0577  0.0489  68  TYR   A CD2 
1722 C CE1 . TYR   A 68  ? 0.1638 0.1609 0.2735 -0.0127 0.0452  -0.0007 68  TYR   A CE1 
1723 C CE2 . TYR   A 68  ? 0.1666 0.1522 0.2696 -0.0000 0.0595  0.0333  68  TYR   A CE2 
1724 C CZ  . TYR   A 68  ? 0.1650 0.1552 0.2808 -0.0137 0.0501  0.0021  68  TYR   A CZ  
1725 O OH  . TYR   A 68  ? 0.1994 0.1519 0.2994 -0.0079 0.0288  -0.0254 68  TYR   A OH  
1735 N N   . ILE   A 69  ? 0.1259 0.1232 0.1753 -0.0023 0.0212  0.0223  69  ILE   A N   
1736 C CA  . ILE   A 69  ? 0.1275 0.1259 0.1743 0.0029  0.0177  0.0102  69  ILE   A CA  
1737 C C   . ILE   A 69  ? 0.1316 0.1300 0.1733 0.0082  0.0183  0.0159  69  ILE   A C   
1738 O O   . ILE   A 69  ? 0.1370 0.1441 0.1753 0.0020  0.0284  0.0171  69  ILE   A O   
1739 C CB  . ILE   A 69  ? 0.1386 0.1447 0.1758 0.0041  0.0178  0.0033  69  ILE   A CB  
1740 C CG1 . ILE   A 69  ? 0.1385 0.1540 0.1814 0.0059  0.0130  -0.0113 69  ILE   A CG1 
1741 C CG2 . ILE   A 69  ? 0.1571 0.1696 0.1820 0.0066  0.0086  -0.0051 69  ILE   A CG2 
1742 C CD1 . ILE   A 69  ? 0.1463 0.1695 0.1977 -0.0043 0.0204  -0.0167 69  ILE   A CD1 
1754 N N   . ALA   A 70  ? 0.1353 0.1343 0.1850 -0.0049 0.0214  0.0279  70  ALA   A N   
1755 C CA  . ALA   A 70  ? 0.1354 0.1515 0.1926 -0.0143 0.0297  0.0301  70  ALA   A CA  
1756 C C   . ALA   A 70  ? 0.1388 0.1663 0.1953 -0.0133 0.0277  0.0281  70  ALA   A C   
1757 O O   . ALA   A 70  ? 0.1538 0.2040 0.2153 0.0112  0.0504  0.0435  70  ALA   A O   
1758 C CB  . ALA   A 70  ? 0.1353 0.1472 0.2072 -0.0176 0.0301  0.0197  70  ALA   A CB  
1764 N N   . THR   A 71  ? 0.1321 0.1584 0.1853 -0.0026 0.0136  0.0250  71  THR   A N   
1765 C CA  . THR   A 71  ? 0.1393 0.1782 0.2139 0.0079  0.0136  0.0390  71  THR   A CA  
1766 C C   . THR   A 71  ? 0.1292 0.1700 0.2418 0.0187  0.0295  0.0358  71  THR   A C   
1767 O O   . THR   A 71  ? 0.1413 0.1930 0.3032 0.0143  0.0474  -0.0009 71  THR   A O   
1768 C CB  . THR   A 71  ? 0.1725 0.2082 0.2364 0.0175  -0.0188 0.0376  71  THR   A CB  
1769 O OG1 . THR   A 71  ? 0.2076 0.2222 0.2470 0.0069  -0.0338 0.0276  71  THR   A OG1 
1770 C CG2 . THR   A 71  ? 0.1871 0.2301 0.2577 0.0190  -0.0215 0.0466  71  THR   A CG2 
1778 N N   . ASN   A 72  ? 0.1346 0.1534 0.2185 0.0176  0.0327  0.0302  72  ASN   A N   
1779 C CA  . ASN   A 72  ? 0.1394 0.1509 0.2240 0.0227  0.0411  0.0257  72  ASN   A CA  
1780 C C   . ASN   A 72  ? 0.1547 0.1515 0.2094 0.0128  0.0454  0.0210  72  ASN   A C   
1781 O O   . ASN   A 72  ? 0.1760 0.1534 0.2328 0.0153  0.0454  0.0060  72  ASN   A O   
1782 C CB  . ASN   A 72  ? 0.1603 0.1622 0.2210 0.0213  0.0447  0.0306  72  ASN   A CB  
1783 C CG  . ASN   A 72  ? 0.1817 0.1706 0.2260 0.0289  0.0439  0.0399  72  ASN   A CG  
1784 O OD1 . ASN   A 72  ? 0.2019 0.1977 0.2555 0.0288  0.0473  0.0305  72  ASN   A OD1 
1785 N ND2 . ASN   A 72  ? 0.1968 0.1748 0.2425 0.0547  0.0158  0.0319  72  ASN   A ND2 
1792 N N   . GLY   A 73  ? 0.1547 0.1458 0.1823 0.0046  0.0437  0.0143  73  GLY   A N   
1793 C CA  . GLY   A 73  ? 0.1668 0.1443 0.1768 -0.0049 0.0411  0.0084  73  GLY   A CA  
1794 C C   . GLY   A 73  ? 0.1643 0.1322 0.1721 0.0022  0.0492  0.0239  73  GLY   A C   
1795 O O   . GLY   A 73  ? 0.1582 0.1413 0.1902 0.0132  0.0410  0.0304  73  GLY   A O   
1799 N N   . PRO   A 74  ? 0.1732 0.1358 0.1837 -0.0075 0.0513  0.0130  74  PRO   A N   
1800 C CA  . PRO   A 74  ? 0.1702 0.1359 0.1965 -0.0032 0.0493  0.0146  74  PRO   A CA  
1801 C C   . PRO   A 74  ? 0.1602 0.1232 0.1864 -0.0012 0.0340  0.0137  74  PRO   A C   
1802 O O   . PRO   A 74  ? 0.1677 0.1270 0.2108 0.0050  0.0350  0.0074  74  PRO   A O   
1803 C CB  . PRO   A 74  ? 0.1853 0.1647 0.2061 0.0039  0.0425  0.0294  74  PRO   A CB  
1804 C CG  . PRO   A 74  ? 0.2121 0.1983 0.2355 -0.0126 0.0299  0.0193  74  PRO   A CG  
1805 C CD  . PRO   A 74  ? 0.1901 0.1764 0.1927 -0.0203 0.0421  0.0064  74  PRO   A CD  
1813 N N   A LEU   A 75  ? 0.1586 0.1259 0.1621 0.0051  0.0289  0.0133  75  LEU   A N   
1814 N N   B LEU   A 75  ? 0.1605 0.1115 0.1562 -0.0011 0.0267  0.0117  75  LEU   A N   
1815 C CA  A LEU   A 75  ? 0.1600 0.1351 0.1475 0.0084  0.0183  0.0170  75  LEU   A CA  
1816 C CA  B LEU   A 75  ? 0.1645 0.1107 0.1444 -0.0049 0.0070  0.0141  75  LEU   A CA  
1817 C C   A LEU   A 75  ? 0.1603 0.1347 0.1375 0.0031  0.0259  0.0136  75  LEU   A C   
1818 C C   B LEU   A 75  ? 0.1740 0.1198 0.1447 0.0029  0.0131  0.0181  75  LEU   A C   
1819 O O   A LEU   A 75  ? 0.1556 0.1505 0.1275 0.0073  0.0250  0.0022  75  LEU   A O   
1820 O O   B LEU   A 75  ? 0.1891 0.1263 0.1599 0.0077  0.0098  0.0154  75  LEU   A O   
1821 C CB  A LEU   A 75  ? 0.1626 0.1482 0.1419 0.0199  0.0138  0.0251  75  LEU   A CB  
1822 C CB  B LEU   A 75  ? 0.1695 0.1131 0.1440 -0.0194 0.0088  0.0186  75  LEU   A CB  
1823 C CG  A LEU   A 75  ? 0.1722 0.1730 0.1437 0.0208  0.0123  0.0283  75  LEU   A CG  
1824 C CG  B LEU   A 75  ? 0.1896 0.1430 0.1610 -0.0492 0.0088  0.0168  75  LEU   A CG  
1825 C CD1 A LEU   A 75  ? 0.1756 0.1812 0.1556 0.0270  0.0085  0.0262  75  LEU   A CD1 
1826 C CD1 B LEU   A 75  ? 0.1960 0.1744 0.1735 -0.0528 0.0061  0.0120  75  LEU   A CD1 
1827 C CD2 A LEU   A 75  ? 0.1787 0.1909 0.1553 0.0295  0.0188  0.0302  75  LEU   A CD2 
1828 C CD2 B LEU   A 75  ? 0.2152 0.1890 0.2113 -0.0315 0.0172  0.0153  75  LEU   A CD2 
1851 N N   . LYS   A 76  ? 0.1756 0.1225 0.1507 -0.0027 0.0127  0.0097  76  LYS   A N   
1852 C CA  . LYS   A 76  ? 0.1729 0.1374 0.1641 -0.0080 0.0065  0.0059  76  LYS   A CA  
1853 C C   . LYS   A 76  ? 0.1741 0.1279 0.1302 -0.0027 0.0069  0.0101  76  LYS   A C   
1854 O O   . LYS   A 76  ? 0.1781 0.1246 0.1439 -0.0040 0.0145  0.0134  76  LYS   A O   
1855 C CB  . LYS   A 76  ? 0.1725 0.1491 0.1821 -0.0007 0.0078  -0.0122 76  LYS   A CB  
1856 C CG  . LYS   A 76  ? 0.1822 0.1537 0.2251 0.0068  0.0004  -0.0224 76  LYS   A CG  
1857 C CD  . LYS   A 76  ? 0.1853 0.1591 0.2669 0.0128  -0.0146 -0.0297 76  LYS   A CD  
1858 C CE  . LYS   A 76  ? 0.1968 0.1759 0.3339 0.0024  -0.0085 -0.0310 76  LYS   A CE  
1859 N NZ  . LYS   A 76  ? 0.1939 0.1700 0.3849 -0.0074 -0.0035 -0.0407 76  LYS   A NZ  
1874 N N   A VAL   A 77  ? 0.1825 0.1328 0.1375 0.0020  0.0105  0.0110  77  VAL   A N   
1875 N N   B VAL   A 77  ? 0.1861 0.1339 0.1382 -0.0047 0.0187  0.0186  77  VAL   A N   
1876 C CA  A VAL   A 77  ? 0.1812 0.1321 0.1432 0.0064  0.0046  0.0119  77  VAL   A CA  
1877 C CA  B VAL   A 77  ? 0.1826 0.1315 0.1534 -0.0038 0.0047  0.0139  77  VAL   A CA  
1878 C C   A VAL   A 77  ? 0.1751 0.1301 0.1313 0.0072  0.0061  0.0093  77  VAL   A C   
1879 C C   B VAL   A 77  ? 0.1723 0.1274 0.1372 -0.0005 0.0047  0.0134  77  VAL   A C   
1880 O O   A VAL   A 77  ? 0.1767 0.1373 0.1332 0.0127  0.0129  0.0032  77  VAL   A O   
1881 O O   B VAL   A 77  ? 0.1736 0.1333 0.1481 0.0010  0.0162  0.0046  77  VAL   A O   
1882 C CB  A VAL   A 77  ? 0.1909 0.1405 0.1574 0.0094  -0.0032 0.0181  77  VAL   A CB  
1883 C CB  B VAL   A 77  ? 0.1986 0.1478 0.1734 -0.0065 -0.0102 0.0169  77  VAL   A CB  
1884 C CG1 A VAL   A 77  ? 0.1966 0.1474 0.1707 0.0098  -0.0069 0.0152  77  VAL   A CG1 
1885 C CG1 B VAL   A 77  ? 0.2079 0.1587 0.1931 -0.0028 -0.0197 0.0121  77  VAL   A CG1 
1886 C CG2 A VAL   A 77  ? 0.1976 0.1442 0.1677 0.0135  -0.0084 0.0241  77  VAL   A CG2 
1887 C CG2 B VAL   A 77  ? 0.2043 0.1564 0.1821 -0.0005 -0.0177 0.0123  77  VAL   A CG2 
1906 N N   . GLY   A 78  ? 0.1676 0.1251 0.1354 0.0031  0.0110  0.0097  78  GLY   A N   
1907 C CA  . GLY   A 78  ? 0.1672 0.1227 0.1485 -0.0040 0.0190  0.0151  78  GLY   A CA  
1908 C C   . GLY   A 78  ? 0.1530 0.1202 0.1496 0.0006  0.0221  0.0163  78  GLY   A C   
1909 O O   . GLY   A 78  ? 0.1504 0.1263 0.1674 -0.0005 0.0145  0.0288  78  GLY   A O   
1914 N N   . GLY   A 79  ? 0.1601 0.1212 0.1443 -0.0018 0.0134  0.0176  79  GLY   A N   
1915 C CA  . GLY   A 79  ? 0.1470 0.1235 0.1609 -0.0049 0.0186  0.0168  79  GLY   A CA  
1916 C C   . GLY   A 79  ? 0.1345 0.1178 0.1423 0.0004  0.0208  0.0092  79  GLY   A C   
1917 O O   . GLY   A 79  ? 0.1404 0.1311 0.1591 0.0139  0.0139  0.0084  79  GLY   A O   
1921 N N   . SER   A 80  ? 0.1262 0.1324 0.1696 -0.0021 0.0129  -0.0065 80  SER   A N   
1922 C CA  . SER   A 80  ? 0.1169 0.1270 0.1590 -0.0012 0.0137  0.0017  80  SER   A CA  
1923 C C   . SER   A 80  ? 0.1169 0.1260 0.1582 -0.0032 0.0103  0.0140  80  SER   A C   
1924 O O   . SER   A 80  ? 0.1170 0.1517 0.1929 0.0046  0.0125  0.0012  80  SER   A O   
1925 C CB  . SER   A 80  ? 0.1345 0.1246 0.1709 -0.0064 0.0013  0.0028  80  SER   A CB  
1926 O OG  . SER   A 80  ? 0.1575 0.1267 0.2096 0.0049  -0.0012 0.0244  80  SER   A OG  
1932 N N   . CYS   A 81  ? 0.1151 0.1195 0.1497 -0.0005 -0.0021 0.0156  81  CYS   A N   
1933 C CA  . CYS   A 81  ? 0.1156 0.1330 0.1514 -0.0029 -0.0062 0.0228  81  CYS   A CA  
1934 C C   . CYS   A 81  ? 0.1131 0.1281 0.1414 -0.0097 0.0028  0.0295  81  CYS   A C   
1935 O O   . CYS   A 81  ? 0.1103 0.1603 0.1621 0.0024  0.0077  0.0288  81  CYS   A O   
1936 C CB  . CYS   A 81  ? 0.1245 0.1439 0.1536 -0.0167 0.0049  0.0261  81  CYS   A CB  
1937 S SG  . CYS   A 81  ? 0.1361 0.1287 0.1567 -0.0141 0.0044  0.0152  81  CYS   A SG  
1943 N N   . VAL   A 82  ? 0.1181 0.1346 0.1483 -0.0012 -0.0019 0.0179  82  VAL   A N   
1944 C CA  . VAL   A 82  ? 0.1287 0.1399 0.1532 0.0037  -0.0105 0.0252  82  VAL   A CA  
1945 C C   . VAL   A 82  ? 0.1234 0.1379 0.1591 -0.0041 -0.0056 0.0226  82  VAL   A C   
1946 O O   . VAL   A 82  ? 0.1178 0.1539 0.1841 -0.0021 -0.0067 0.0032  82  VAL   A O   
1947 C CB  . VAL   A 82  ? 0.1585 0.1491 0.1739 0.0012  -0.0019 0.0367  82  VAL   A CB  
1948 C CG1 . VAL   A 82  ? 0.1793 0.1664 0.1980 0.0061  0.0013  0.0291  82  VAL   A CG1 
1949 C CG2 . VAL   A 82  ? 0.1724 0.1506 0.1991 -0.0025 -0.0004 0.0346  82  VAL   A CG2 
1959 N N   . LEU   A 83  ? 0.1204 0.1343 0.1555 -0.0027 -0.0026 0.0177  83  LEU   A N   
1960 C CA  . LEU   A 83  ? 0.1236 0.1368 0.1474 -0.0072 -0.0077 0.0139  83  LEU   A CA  
1961 C C   . LEU   A 83  ? 0.1318 0.1381 0.1311 -0.0057 -0.0088 0.0159  83  LEU   A C   
1962 O O   . LEU   A 83  ? 0.1448 0.1446 0.1543 -0.0117 -0.0005 0.0260  83  LEU   A O   
1963 C CB  . LEU   A 83  ? 0.1282 0.1414 0.1598 -0.0120 -0.0078 0.0156  83  LEU   A CB  
1964 C CG  . LEU   A 83  ? 0.1435 0.1493 0.1699 -0.0108 -0.0012 0.0143  83  LEU   A CG  
1965 C CD1 . LEU   A 83  ? 0.1562 0.1517 0.1686 -0.0163 -0.0011 0.0239  83  LEU   A CD1 
1966 C CD2 . LEU   A 83  ? 0.1443 0.1655 0.1751 -0.0073 0.0095  0.0211  83  LEU   A CD2 
1978 N N   . SER   A 84  ? 0.1507 0.1431 0.1523 -0.0140 -0.0074 0.0205  84  SER   A N   
1979 C CA  . SER   A 84  ? 0.1600 0.1502 0.1436 -0.0109 -0.0115 0.0180  84  SER   A CA  
1980 C C   . SER   A 84  ? 0.1603 0.1509 0.1401 -0.0157 0.0031  0.0143  84  SER   A C   
1981 O O   . SER   A 84  ? 0.1485 0.1628 0.1357 -0.0103 -0.0086 0.0151  84  SER   A O   
1982 C CB  . SER   A 84  ? 0.1661 0.1685 0.1559 -0.0036 -0.0170 0.0072  84  SER   A CB  
1983 O OG  . SER   A 84  ? 0.1771 0.1935 0.1640 -0.0068 -0.0202 -0.0038 84  SER   A OG  
1989 N N   A GLY   A 85  ? 0.1723 0.1622 0.1397 -0.0176 0.0112  0.0131  85  GLY   A N   
1990 N N   B GLY   A 85  ? 0.1739 0.1656 0.1487 -0.0214 0.0165  0.0150  85  GLY   A N   
1991 C CA  A GLY   A 85  ? 0.1747 0.1693 0.1462 -0.0174 0.0149  0.0069  85  GLY   A CA  
1992 C CA  B GLY   A 85  ? 0.1731 0.1726 0.1600 -0.0251 0.0246  0.0061  85  GLY   A CA  
1993 C C   A GLY   A 85  ? 0.1761 0.1746 0.1386 -0.0111 0.0031  0.0061  85  GLY   A C   
1994 C C   B GLY   A 85  ? 0.1742 0.1781 0.1444 -0.0167 0.0050  0.0025  85  GLY   A C   
1995 O O   A GLY   A 85  ? 0.1741 0.1848 0.1466 -0.0127 0.0093  -0.0017 85  GLY   A O   
1996 O O   B GLY   A 85  ? 0.1675 0.1919 0.1513 -0.0254 0.0138  -0.0142 85  GLY   A O   
2003 N N   . HIS   A 86  ? 0.1778 0.1709 0.1392 -0.0081 -0.0021 0.0093  86  HIS   A N   
2004 C CA  . HIS   A 86  ? 0.1938 0.1760 0.1236 -0.0082 -0.0024 0.0081  86  HIS   A CA  
2005 C C   . HIS   A 86  ? 0.2241 0.1921 0.1068 -0.0063 -0.0049 0.0109  86  HIS   A C   
2006 O O   . HIS   A 86  ? 0.2386 0.2100 0.1284 0.0032  0.0038  0.0143  86  HIS   A O   
2007 C CB  . HIS   A 86  ? 0.1860 0.1683 0.1378 -0.0068 -0.0093 0.0070  86  HIS   A CB  
2008 C CG  . HIS   A 86  ? 0.1822 0.1670 0.1433 -0.0007 0.0004  0.0157  86  HIS   A CG  
2009 N ND1 . HIS   A 86  ? 0.1889 0.1687 0.1805 -0.0136 -0.0075 0.0083  86  HIS   A ND1 
2010 C CD2 . HIS   A 86  ? 0.1780 0.1592 0.1330 0.0059  0.0028  0.0157  86  HIS   A CD2 
2011 C CE1 . HIS   A 86  ? 0.1844 0.1707 0.1802 -0.0090 0.0096  0.0154  86  HIS   A CE1 
2012 N NE2 . HIS   A 86  ? 0.1776 0.1639 0.1536 0.0067  0.0081  0.0265  86  HIS   A NE2 
2021 N N   A ASN   A 87  ? 0.2354 0.1989 0.1333 0.0036  0.0059  -0.0008 87  ASN   A N   
2022 N N   B ASN   A 87  ? 0.2366 0.2028 0.1205 0.0083  0.0173  0.0073  87  ASN   A N   
2023 C CA  A ASN   A 87  ? 0.2471 0.2059 0.1603 0.0053  0.0164  -0.0105 87  ASN   A CA  
2024 C CA  B ASN   A 87  ? 0.2519 0.2173 0.1328 0.0106  0.0361  0.0032  87  ASN   A CA  
2025 C C   A ASN   A 87  ? 0.2448 0.2099 0.1861 0.0003  0.0235  -0.0079 87  ASN   A C   
2026 C C   B ASN   A 87  ? 0.2473 0.2304 0.1454 -0.0056 0.0602  0.0022  87  ASN   A C   
2027 O O   A ASN   A 87  ? 0.2589 0.2224 0.2185 -0.0042 0.0376  -0.0128 87  ASN   A O   
2028 O O   B ASN   A 87  ? 0.2682 0.2537 0.1701 -0.0251 0.0894  -0.0017 87  ASN   A O   
2029 C CB  A ASN   A 87  ? 0.2597 0.2089 0.1699 0.0132  0.0219  -0.0187 87  ASN   A CB  
2030 C CB  B ASN   A 87  ? 0.2700 0.2149 0.1575 0.0289  0.0309  0.0023  87  ASN   A CB  
2031 C CG  A ASN   A 87  ? 0.2690 0.2161 0.1681 0.0137  0.0347  -0.0222 87  ASN   A CG  
2032 C CG  B ASN   A 87  ? 0.2877 0.2244 0.1610 0.0394  0.0356  0.0071  87  ASN   A CG  
2033 O OD1 A ASN   A 87  ? 0.2760 0.2170 0.1708 0.0188  0.0405  -0.0259 87  ASN   A OD1 
2034 O OD1 B ASN   A 87  ? 0.2972 0.2209 0.1588 0.0558  0.0308  0.0109  87  ASN   A OD1 
2035 N ND2 A ASN   A 87  ? 0.2740 0.2281 0.1839 0.0137  0.0335  -0.0170 87  ASN   A ND2 
2036 N ND2 B ASN   A 87  ? 0.2986 0.2472 0.1976 0.0386  0.0338  0.0109  87  ASN   A ND2 
2049 N N   A LEU   A 88  ? 0.2265 0.2018 0.1800 -0.0045 0.0165  0.0026  88  LEU   A N   
2050 N N   B LEU   A 88  ? 0.2142 0.2136 0.1355 -0.0063 0.0517  0.0096  88  LEU   A N   
2051 C CA  A LEU   A 88  ? 0.2121 0.1923 0.1785 -0.0082 0.0177  0.0195  88  LEU   A CA  
2052 C CA  B LEU   A 88  ? 0.1938 0.2081 0.1578 -0.0058 0.0454  0.0255  88  LEU   A CA  
2053 C C   A LEU   A 88  ? 0.2080 0.1960 0.1844 -0.0111 0.0290  0.0233  88  LEU   A C   
2054 C C   B LEU   A 88  ? 0.1745 0.2090 0.1604 -0.0053 0.0392  0.0438  88  LEU   A C   
2055 O O   A LEU   A 88  ? 0.2063 0.2041 0.2103 -0.0136 0.0446  0.0261  88  LEU   A O   
2056 O O   B LEU   A 88  ? 0.1725 0.2142 0.1949 -0.0069 0.0378  0.0737  88  LEU   A O   
2057 C CB  A LEU   A 88  ? 0.2045 0.1881 0.1709 -0.0104 -0.0054 0.0358  88  LEU   A CB  
2058 C CB  B LEU   A 88  ? 0.1960 0.2101 0.1647 -0.0053 0.0300  0.0195  88  LEU   A CB  
2059 C CG  A LEU   A 88  ? 0.2074 0.1876 0.1740 -0.0120 -0.0209 0.0471  88  LEU   A CG  
2060 C CG  B LEU   A 88  ? 0.2042 0.2169 0.1838 -0.0022 0.0235  0.0102  88  LEU   A CG  
2061 C CD1 A LEU   A 88  ? 0.2079 0.1857 0.1716 -0.0120 -0.0259 0.0495  88  LEU   A CD1 
2062 C CD1 B LEU   A 88  ? 0.2025 0.2226 0.1923 -0.0032 0.0214  0.0089  88  LEU   A CD1 
2063 C CD2 A LEU   A 88  ? 0.2196 0.1971 0.1938 -0.0078 -0.0197 0.0394  88  LEU   A CD2 
2064 C CD2 B LEU   A 88  ? 0.2220 0.2260 0.2032 0.0113  0.0237  0.0005  88  LEU   A CD2 
2087 N N   A ALA   A 89  ? 0.2081 0.1953 0.1702 -0.0075 0.0235  0.0167  89  ALA   A N   
2088 N N   B ALA   A 89  ? 0.1622 0.2070 0.1496 -0.0029 0.0249  0.0230  89  ALA   A N   
2089 C CA  A ALA   A 89  ? 0.2105 0.1950 0.1571 0.0006  0.0169  0.0167  89  ALA   A CA  
2090 C CA  B ALA   A 89  ? 0.1676 0.2067 0.1422 -0.0046 0.0118  0.0182  89  ALA   A CA  
2091 C C   A ALA   A 89  ? 0.2176 0.1977 0.1517 0.0062  0.0005  0.0239  89  ALA   A C   
2092 C C   B ALA   A 89  ? 0.1662 0.2074 0.1409 -0.0043 0.0032  0.0229  89  ALA   A C   
2093 O O   A ALA   A 89  ? 0.2192 0.1966 0.1690 0.0042  -0.0038 0.0099  89  ALA   A O   
2094 O O   B ALA   A 89  ? 0.1545 0.2094 0.1817 -0.0203 -0.0015 -0.0042 89  ALA   A O   
2095 C CB  A ALA   A 89  ? 0.2050 0.1943 0.1527 0.0025  0.0229  0.0119  89  ALA   A CB  
2096 C CB  B ALA   A 89  ? 0.1656 0.1977 0.1464 -0.0066 0.0122  0.0115  89  ALA   A CB  
2107 N N   A LYS   A 90  ? 0.2246 0.2071 0.1569 0.0034  -0.0085 0.0248  90  LYS   A N   
2108 N N   B LYS   A 90  ? 0.1729 0.2100 0.1268 -0.0039 0.0014  0.0260  90  LYS   A N   
2109 C CA  A LYS   A 90  ? 0.2290 0.2212 0.1809 -0.0019 -0.0148 0.0176  90  LYS   A CA  
2110 C CA  B LYS   A 90  ? 0.1844 0.2167 0.1339 -0.0016 -0.0162 0.0279  90  LYS   A CA  
2111 C C   A LYS   A 90  ? 0.2129 0.2177 0.1762 -0.0093 -0.0107 -0.0001 90  LYS   A C   
2112 C C   B LYS   A 90  ? 0.1645 0.1936 0.1371 -0.0027 -0.0174 0.0128  90  LYS   A C   
2113 O O   A LYS   A 90  ? 0.2086 0.2299 0.1935 -0.0119 -0.0128 -0.0119 90  LYS   A O   
2114 O O   B LYS   A 90  ? 0.1664 0.1941 0.1702 -0.0012 -0.0215 0.0159  90  LYS   A O   
2115 C CB  A LYS   A 90  ? 0.2461 0.2414 0.2249 -0.0006 -0.0186 0.0300  90  LYS   A CB  
2116 C CB  B LYS   A 90  ? 0.2162 0.2481 0.1714 -0.0018 -0.0290 0.0491  90  LYS   A CB  
2117 C CG  A LYS   A 90  ? 0.2656 0.2623 0.2930 -0.0009 -0.0185 0.0333  90  LYS   A CG  
2118 C CG  B LYS   A 90  ? 0.2482 0.2747 0.2698 0.0061  -0.0424 0.0575  90  LYS   A CG  
2119 C CD  A LYS   A 90  ? 0.2812 0.2785 0.3500 -0.0007 -0.0155 0.0375  90  LYS   A CD  
2120 C CD  B LYS   A 90  ? 0.2773 0.2985 0.3551 0.0078  -0.0390 0.0578  90  LYS   A CD  
2121 C CE  A LYS   A 90  ? 0.2941 0.2891 0.3926 -0.0004 -0.0129 0.0385  90  LYS   A CE  
2122 C CE  B LYS   A 90  ? 0.3050 0.3199 0.4241 0.0057  -0.0336 0.0512  90  LYS   A CE  
2123 N NZ  A LYS   A 90  ? 0.3041 0.2959 0.4234 -0.0006 -0.0105 0.0361  90  LYS   A NZ  
2124 N NZ  B LYS   A 90  ? 0.3164 0.3309 0.4699 0.0037  -0.0243 0.0461  90  LYS   A NZ  
2151 N N   A HIS   A 91  ? 0.2030 0.2043 0.1608 -0.0110 -0.0095 0.0053  91  HIS   A N   
2152 N N   B HIS   A 91  ? 0.1565 0.1705 0.1094 -0.0055 -0.0230 0.0186  91  HIS   A N   
2153 C CA  A HIS   A 91  ? 0.1933 0.1909 0.1615 -0.0108 -0.0061 0.0124  91  HIS   A CA  
2154 C CA  B HIS   A 91  ? 0.1499 0.1598 0.1130 -0.0022 -0.0202 0.0129  91  HIS   A CA  
2155 C C   A HIS   A 91  ? 0.1638 0.1667 0.1372 -0.0145 0.0032  0.0226  91  HIS   A C   
2156 C C   B HIS   A 91  ? 0.1412 0.1509 0.1180 -0.0070 -0.0091 0.0118  91  HIS   A C   
2157 O O   A HIS   A 91  ? 0.1551 0.1598 0.1266 -0.0137 0.0211  0.0316  91  HIS   A O   
2158 O O   B HIS   A 91  ? 0.1329 0.1533 0.1441 -0.0129 -0.0009 0.0158  91  HIS   A O   
2159 C CB  A HIS   A 91  ? 0.2158 0.2104 0.1963 -0.0009 -0.0189 0.0077  91  HIS   A CB  
2160 C CB  B HIS   A 91  ? 0.1698 0.1912 0.1630 0.0228  -0.0284 0.0183  91  HIS   A CB  
2161 C CG  A HIS   A 91  ? 0.2429 0.2395 0.2363 0.0054  -0.0332 0.0006  91  HIS   A CG  
2162 C CG  B HIS   A 91  ? 0.2065 0.2444 0.2198 0.0371  -0.0571 0.0088  91  HIS   A CG  
2163 N ND1 A HIS   A 91  ? 0.2521 0.2556 0.2605 0.0093  -0.0395 -0.0056 91  HIS   A ND1 
2164 N ND1 B HIS   A 91  ? 0.2138 0.2746 0.2671 0.0397  -0.0612 -0.0110 91  HIS   A ND1 
2165 C CD2 A HIS   A 91  ? 0.2566 0.2508 0.2540 0.0088  -0.0403 0.0024  91  HIS   A CD2 
2166 C CD2 B HIS   A 91  ? 0.2353 0.2634 0.2427 0.0416  -0.0647 0.0170  91  HIS   A CD2 
2167 C CE1 A HIS   A 91  ? 0.2583 0.2600 0.2689 0.0139  -0.0418 -0.0026 91  HIS   A CE1 
2168 C CE1 B HIS   A 91  ? 0.2306 0.2821 0.2779 0.0443  -0.0623 0.0002  91  HIS   A CE1 
2169 N NE2 A HIS   A 91  ? 0.2647 0.2592 0.2699 0.0157  -0.0434 -0.0003 91  HIS   A NE2 
2170 N NE2 B HIS   A 91  ? 0.2475 0.2808 0.2721 0.0464  -0.0638 0.0079  91  HIS   A NE2 
2185 N N   . CYS   A 92  ? 0.1402 0.1499 0.1290 -0.0164 -0.0001 0.0162  92  CYS   A N   
2186 C CA  . CYS   A 92  ? 0.1268 0.1404 0.1405 -0.0184 -0.0034 0.0155  92  CYS   A CA  
2187 C C   . CYS   A 92  ? 0.1243 0.1334 0.1323 -0.0177 0.0058  0.0214  92  CYS   A C   
2188 O O   . CYS   A 92  ? 0.1281 0.1432 0.1549 -0.0161 -0.0012 0.0157  92  CYS   A O   
2189 C CB  . CYS   A 92  ? 0.1368 0.1379 0.1439 -0.0147 -0.0034 0.0062  92  CYS   A CB  
2190 S SG  . CYS   A 92  ? 0.1341 0.1329 0.1459 -0.0119 0.0004  0.0150  92  CYS   A SG  
2197 N N   . LEU   A 93  ? 0.1204 0.1245 0.1466 -0.0093 0.0102  0.0237  93  LEU   A N   
2198 C CA  . LEU   A 93  ? 0.1144 0.1238 0.1484 -0.0028 0.0090  0.0174  93  LEU   A CA  
2199 C C   . LEU   A 93  ? 0.1138 0.1128 0.1499 -0.0027 0.0085  0.0124  93  LEU   A C   
2200 O O   . LEU   A 93  ? 0.1098 0.1230 0.1463 -0.0002 0.0104  0.0162  93  LEU   A O   
2201 C CB  . LEU   A 93  ? 0.1171 0.1172 0.1489 -0.0028 0.0040  0.0213  93  LEU   A CB  
2202 C CG  . LEU   A 93  ? 0.1278 0.1222 0.1546 -0.0061 0.0046  0.0306  93  LEU   A CG  
2203 C CD1 . LEU   A 93  ? 0.1342 0.1300 0.1880 -0.0027 0.0185  0.0184  93  LEU   A CD1 
2204 C CD2 . LEU   A 93  ? 0.1423 0.1228 0.1682 -0.0067 0.0086  0.0190  93  LEU   A CD2 
2216 N N   . HIS   A 94  ? 0.1130 0.1104 0.1401 -0.0042 0.0081  0.0213  94  HIS   A N   
2217 C CA  . HIS   A 94  ? 0.1111 0.1138 0.1398 -0.0014 0.0010  0.0201  94  HIS   A CA  
2218 C C   . HIS   A 94  ? 0.1091 0.1107 0.1389 -0.0069 0.0035  0.0081  94  HIS   A C   
2219 O O   . HIS   A 94  ? 0.1114 0.1341 0.1668 0.0021  0.0027  -0.0032 94  HIS   A O   
2220 C CB  . HIS   A 94  ? 0.1107 0.1108 0.1402 -0.0055 0.0060  0.0189  94  HIS   A CB  
2221 C CG  . HIS   A 94  ? 0.1118 0.1131 0.1410 -0.0093 -0.0026 0.0179  94  HIS   A CG  
2222 N ND1 . HIS   A 94  ? 0.1113 0.1121 0.1455 -0.0059 0.0027  0.0202  94  HIS   A ND1 
2223 C CD2 . HIS   A 94  ? 0.1228 0.1205 0.1430 -0.0050 -0.0079 0.0114  94  HIS   A CD2 
2224 C CE1 . HIS   A 94  ? 0.1199 0.1140 0.1476 -0.0031 -0.0043 0.0104  94  HIS   A CE1 
2225 N NE2 . HIS   A 94  ? 0.1273 0.1210 0.1378 -0.0080 -0.0062 0.0102  94  HIS   A NE2 
2233 N N   . VAL   A 95  ? 0.1099 0.1032 0.1381 -0.0036 0.0048  0.0085  95  VAL   A N   
2234 C CA  . VAL   A 95  ? 0.1145 0.1132 0.1338 -0.0044 0.0100  0.0163  95  VAL   A CA  
2235 C C   . VAL   A 95  ? 0.1201 0.1102 0.1292 -0.0092 0.0060  0.0121  95  VAL   A C   
2236 O O   . VAL   A 95  ? 0.1270 0.1234 0.1500 0.0085  -0.0010 0.0108  95  VAL   A O   
2237 C CB  . VAL   A 95  ? 0.1188 0.1121 0.1536 -0.0096 0.0062  0.0111  95  VAL   A CB  
2238 C CG1 . VAL   A 95  ? 0.1389 0.1158 0.1616 -0.0106 -0.0013 0.0057  95  VAL   A CG1 
2239 C CG2 . VAL   A 95  ? 0.1199 0.1180 0.1588 -0.0090 0.0071  0.0285  95  VAL   A CG2 
2249 N N   A VAL   A 96  ? 0.1256 0.1103 0.1257 -0.0030 -0.0002 0.0146  96  VAL   A N   
2250 N N   B VAL   A 96  ? 0.1268 0.1140 0.1222 -0.0011 -0.0007 0.0187  96  VAL   A N   
2251 C CA  A VAL   A 96  ? 0.1344 0.1098 0.1328 -0.0009 -0.0004 0.0141  96  VAL   A CA  
2252 C CA  B VAL   A 96  ? 0.1403 0.1183 0.1281 -0.0030 0.0007  0.0196  96  VAL   A CA  
2253 C C   A VAL   A 96  ? 0.1377 0.1200 0.1364 -0.0058 -0.0037 0.0173  96  VAL   A C   
2254 C C   B VAL   A 96  ? 0.1468 0.1209 0.1393 -0.0045 0.0008  0.0140  96  VAL   A C   
2255 O O   A VAL   A 96  ? 0.1367 0.1186 0.1483 -0.0103 -0.0069 0.0086  96  VAL   A O   
2256 O O   B VAL   A 96  ? 0.1553 0.1202 0.1749 -0.0029 0.0062  -0.0000 96  VAL   A O   
2257 C CB  A VAL   A 96  ? 0.1390 0.1060 0.1456 0.0040  0.0063  0.0047  96  VAL   A CB  
2258 C CB  B VAL   A 96  ? 0.1431 0.1301 0.1386 -0.0045 0.0103  0.0145  96  VAL   A CB  
2259 C CG1 A VAL   A 96  ? 0.1471 0.1047 0.1498 0.0006  0.0015  0.0024  96  VAL   A CG1 
2260 C CG1 B VAL   A 96  ? 0.1472 0.1357 0.1338 -0.0101 0.0100  0.0235  96  VAL   A CG1 
2261 C CG2 A VAL   A 96  ? 0.1322 0.1037 0.1484 0.0052  0.0137  -0.0004 96  VAL   A CG2 
2262 C CG2 B VAL   A 96  ? 0.1367 0.1326 0.1360 -0.0144 0.0124  0.0094  96  VAL   A CG2 
2281 N N   A GLY   A 97  ? 0.1400 0.1287 0.1405 -0.0080 0.0018  0.0171  97  GLY   A N   
2282 N N   B GLY   A 97  ? 0.1431 0.1178 0.1307 -0.0086 0.0015  0.0060  97  GLY   A N   
2283 C CA  A GLY   A 97  ? 0.1477 0.1340 0.1380 -0.0026 -0.0062 0.0191  97  GLY   A CA  
2284 C CA  B GLY   A 97  ? 0.1496 0.1291 0.1312 -0.0118 -0.0072 0.0093  97  GLY   A CA  
2285 C C   A GLY   A 97  ? 0.1541 0.1479 0.1252 0.0040  -0.0062 0.0081  97  GLY   A C   
2286 C C   B GLY   A 97  ? 0.1498 0.1379 0.1313 -0.0103 -0.0051 0.0057  97  GLY   A C   
2287 O O   A GLY   A 97  ? 0.1554 0.1481 0.1380 0.0069  0.0057  0.0102  97  GLY   A O   
2288 O O   B GLY   A 97  ? 0.1640 0.1358 0.1632 -0.0130 -0.0015 0.0231  97  GLY   A O   
2295 N N   A PRO   A 98  ? 0.1640 0.1512 0.1064 0.0113  -0.0097 0.0116  98  PRO   A N   
2296 N N   B PRO   A 98  ? 0.1606 0.1396 0.1346 -0.0005 -0.0011 0.0165  98  PRO   A N   
2297 C CA  A PRO   A 98  ? 0.1701 0.1660 0.1090 0.0097  -0.0019 0.0157  98  PRO   A CA  
2298 C CA  B PRO   A 98  ? 0.1701 0.1570 0.1477 -0.0033 -0.0017 0.0060  98  PRO   A CA  
2299 C C   A PRO   A 98  ? 0.1766 0.1820 0.1067 0.0037  0.0108  0.0354  98  PRO   A C   
2300 C C   B PRO   A 98  ? 0.1864 0.1527 0.1414 -0.0115 -0.0106 0.0143  98  PRO   A C   
2301 O O   A PRO   A 98  ? 0.1686 0.1708 0.1072 0.0035  0.0121  0.0305  98  PRO   A O   
2302 O O   B PRO   A 98  ? 0.1799 0.1526 0.1718 -0.0084 -0.0111 0.0191  98  PRO   A O   
2303 C CB  A PRO   A 98  ? 0.1739 0.1653 0.1113 0.0214  -0.0029 -0.0045 98  PRO   A CB  
2304 C CB  B PRO   A 98  ? 0.1812 0.1645 0.1553 0.0041  0.0002  0.0061  98  PRO   A CB  
2305 C CG  A PRO   A 98  ? 0.1725 0.1535 0.1178 0.0207  -0.0039 -0.0110 98  PRO   A CG  
2306 C CG  B PRO   A 98  ? 0.1868 0.1558 0.1732 -0.0030 -0.0089 0.0040  98  PRO   A CG  
2307 C CD  A PRO   A 98  ? 0.1672 0.1466 0.1097 0.0203  -0.0020 0.0087  98  PRO   A CD  
2308 C CD  B PRO   A 98  ? 0.1717 0.1387 0.1692 -0.0023 -0.0119 0.0136  98  PRO   A CD  
2323 N N   A ASN   A 99  ? 0.1892 0.2125 0.1228 0.0087  0.0145  0.0456  99  ASN   A N   
2324 N N   B ASN   A 99  ? 0.2238 0.1518 0.1485 -0.0039 -0.0270 0.0257  99  ASN   A N   
2325 C CA  A ASN   A 99  ? 0.2098 0.2410 0.1560 0.0120  0.0086  0.0505  99  ASN   A CA  
2326 C CA  B ASN   A 99  ? 0.2580 0.1534 0.1724 0.0077  -0.0289 0.0376  99  ASN   A CA  
2327 C C   A ASN   A 99  ? 0.2329 0.2642 0.1822 0.0068  0.0097  0.0452  99  ASN   A C   
2328 C C   B ASN   A 99  ? 0.2625 0.1667 0.1532 0.0044  -0.0255 0.0458  99  ASN   A C   
2329 O O   A ASN   A 99  ? 0.2379 0.2740 0.1866 0.0126  0.0050  0.0430  99  ASN   A O   
2330 O O   B ASN   A 99  ? 0.2564 0.1692 0.1532 0.0173  -0.0234 0.0333  99  ASN   A O   
2331 C CB  A ASN   A 99  ? 0.2110 0.2454 0.1822 0.0212  0.0025  0.0582  99  ASN   A CB  
2332 C CB  B ASN   A 99  ? 0.2888 0.1523 0.2075 0.0080  -0.0330 0.0370  99  ASN   A CB  
2333 C CG  A ASN   A 99  ? 0.2158 0.2522 0.2091 0.0297  -0.0005 0.0572  99  ASN   A CG  
2334 C CG  B ASN   A 99  ? 0.3153 0.1596 0.2224 0.0084  -0.0382 0.0393  99  ASN   A CG  
2335 O OD1 A ASN   A 99  ? 0.2193 0.2568 0.2169 0.0366  0.0065  0.0448  99  ASN   A OD1 
2336 O OD1 B ASN   A 99  ? 0.3210 0.1677 0.2096 0.0175  -0.0483 0.0502  99  ASN   A OD1 
2337 N ND2 A ASN   A 99  ? 0.2196 0.2498 0.2180 0.0312  -0.0029 0.0704  99  ASN   A ND2 
2338 N ND2 B ASN   A 99  ? 0.3290 0.1579 0.2607 0.0102  -0.0496 0.0193  99  ASN   A ND2 
2351 N N   A VAL   A 100 ? 0.2502 0.2764 0.2156 0.0040  0.0041  0.0371  100 VAL   A N   
2352 N N   B VAL   A 100 ? 0.2819 0.2059 0.1620 -0.0120 -0.0293 0.0424  100 VAL   A N   
2353 C CA  A VAL   A 100 ? 0.2703 0.2896 0.2400 0.0031  0.0038  0.0352  100 VAL   A CA  
2354 C CA  B VAL   A 100 ? 0.3058 0.2372 0.1978 -0.0178 -0.0378 0.0353  100 VAL   A CA  
2355 C C   A VAL   A 100 ? 0.2869 0.3051 0.2529 0.0004  -0.0118 0.0446  100 VAL   A C   
2356 C C   B VAL   A 100 ? 0.3139 0.2531 0.1896 -0.0050 -0.0393 0.0349  100 VAL   A C   
2357 O O   A VAL   A 100 ? 0.2891 0.3083 0.2675 -0.0019 -0.0056 0.0456  100 VAL   A O   
2358 O O   B VAL   A 100 ? 0.3155 0.2619 0.1887 -0.0090 -0.0497 0.0265  100 VAL   A O   
2359 C CB  A VAL   A 100 ? 0.2741 0.2881 0.2588 0.0054  0.0160  0.0245  100 VAL   A CB  
2360 C CB  B VAL   A 100 ? 0.3226 0.2546 0.2497 -0.0345 -0.0389 0.0292  100 VAL   A CB  
2361 C CG1 A VAL   A 100 ? 0.2755 0.2896 0.2716 0.0043  0.0240  0.0169  100 VAL   A CG1 
2362 C CG1 B VAL   A 100 ? 0.3272 0.2618 0.2745 -0.0369 -0.0422 0.0308  100 VAL   A CG1 
2363 C CG2 A VAL   A 100 ? 0.2760 0.2874 0.2585 0.0057  0.0204  0.0252  100 VAL   A CG2 
2364 C CG2 B VAL   A 100 ? 0.3317 0.2606 0.2697 -0.0390 -0.0388 0.0266  100 VAL   A CG2 
2383 N N   A ASN   A 101 ? 0.3022 0.3142 0.2556 -0.0009 -0.0338 0.0558  101 ASN   A N   
2384 N N   B ASN   A 101 ? 0.3206 0.2656 0.1914 0.0135  -0.0307 0.0422  101 ASN   A N   
2385 C CA  A ASN   A 101 ? 0.3190 0.3237 0.2629 0.0011  -0.0480 0.0574  101 ASN   A CA  
2386 C CA  B ASN   A 101 ? 0.3371 0.2806 0.2061 0.0377  -0.0162 0.0563  101 ASN   A CA  
2387 C C   A ASN   A 101 ? 0.3333 0.3342 0.2787 0.0087  -0.0449 0.0643  101 ASN   A C   
2388 C C   B ASN   A 101 ? 0.3523 0.2839 0.2012 0.0420  -0.0001 0.0697  101 ASN   A C   
2389 O O   A ASN   A 101 ? 0.3366 0.3334 0.2851 0.0113  -0.0423 0.0664  101 ASN   A O   
2390 O O   B ASN   A 101 ? 0.3595 0.2874 0.2055 0.0416  0.0109  0.0790  101 ASN   A O   
2391 C CB  A ASN   A 101 ? 0.3233 0.3216 0.2587 -0.0065 -0.0569 0.0464  101 ASN   A CB  
2392 C CB  B ASN   A 101 ? 0.3432 0.2946 0.2504 0.0457  -0.0094 0.0509  101 ASN   A CB  
2393 C CG  A ASN   A 101 ? 0.3273 0.3213 0.2564 -0.0143 -0.0606 0.0288  101 ASN   A CG  
2394 C CG  B ASN   A 101 ? 0.3493 0.3074 0.2888 0.0506  -0.0032 0.0372  101 ASN   A CG  
2395 O OD1 A ASN   A 101 ? 0.3281 0.3221 0.2555 -0.0168 -0.0577 0.0169  101 ASN   A OD1 
2396 O OD1 B ASN   A 101 ? 0.3516 0.3148 0.3134 0.0541  -0.0057 0.0292  101 ASN   A OD1 
2397 N ND2 A ASN   A 101 ? 0.3297 0.3200 0.2516 -0.0158 -0.0668 0.0288  101 ASN   A ND2 
2398 N ND2 B ASN   A 101 ? 0.3531 0.3115 0.2982 0.0488  0.0043  0.0353  101 ASN   A ND2 
2411 N N   A LYS   A 102 ? 0.3421 0.3466 0.2935 0.0111  -0.0456 0.0606  102 LYS   A N   
2412 N N   B LYS   A 102 ? 0.3579 0.2868 0.2163 0.0458  0.0008  0.0608  102 LYS   A N   
2413 C CA  A LYS   A 102 ? 0.3510 0.3583 0.3099 0.0123  -0.0470 0.0490  102 LYS   A CA  
2414 C CA  B LYS   A 102 ? 0.3659 0.3027 0.2174 0.0436  0.0115  0.0488  102 LYS   A CA  
2415 C C   A LYS   A 102 ? 0.3501 0.3585 0.2916 0.0153  -0.0381 0.0508  102 LYS   A C   
2416 C C   B LYS   A 102 ? 0.3537 0.2962 0.1805 0.0482  0.0161  0.0521  102 LYS   A C   
2417 O O   A LYS   A 102 ? 0.3534 0.3609 0.2939 0.0188  -0.0364 0.0519  102 LYS   A O   
2418 O O   B LYS   A 102 ? 0.3539 0.2991 0.2073 0.0456  0.0333  0.0460  102 LYS   A O   
2419 C CB  A LYS   A 102 ? 0.3599 0.3689 0.3500 0.0102  -0.0531 0.0294  102 LYS   A CB  
2420 C CB  B LYS   A 102 ? 0.3865 0.3266 0.2917 0.0395  0.0036  0.0200  102 LYS   A CB  
2421 C CG  A LYS   A 102 ? 0.3676 0.3769 0.3865 0.0078  -0.0572 0.0096  102 LYS   A CG  
2422 C CG  B LYS   A 102 ? 0.4048 0.3489 0.3701 0.0349  -0.0051 -0.0021 102 LYS   A CG  
2423 C CD  A LYS   A 102 ? 0.3752 0.3842 0.4214 0.0069  -0.0608 -0.0088 102 LYS   A CD  
2424 C CD  B LYS   A 102 ? 0.4216 0.3723 0.4433 0.0314  -0.0117 -0.0190 102 LYS   A CD  
2425 C CE  A LYS   A 102 ? 0.3804 0.3894 0.4472 0.0065  -0.0629 -0.0218 102 LYS   A CE  
2426 C CE  B LYS   A 102 ? 0.4340 0.3905 0.5040 0.0311  -0.0180 -0.0265 102 LYS   A CE  
2427 N NZ  A LYS   A 102 ? 0.3831 0.3930 0.4597 0.0054  -0.0628 -0.0306 102 LYS   A NZ  
2428 N NZ  B LYS   A 102 ? 0.4408 0.3969 0.5364 0.0311  -0.0199 -0.0309 102 LYS   A NZ  
2455 N N   A GLY   A 103 ? 0.3466 0.3571 0.2899 0.0160  -0.0330 0.0439  103 GLY   A N   
2456 N N   B GLY   A 103 ? 0.3381 0.2900 0.1325 0.0545  0.0026  0.0413  103 GLY   A N   
2457 C CA  A GLY   A 103 ? 0.3427 0.3542 0.2895 0.0179  -0.0262 0.0402  103 GLY   A CA  
2458 C CA  B GLY   A 103 ? 0.3230 0.2814 0.1348 0.0588  -0.0092 0.0360  103 GLY   A CA  
2459 C C   A GLY   A 103 ? 0.3376 0.3511 0.2928 0.0176  -0.0180 0.0349  103 GLY   A C   
2460 C C   B GLY   A 103 ? 0.3061 0.2687 0.1477 0.0547  -0.0181 0.0256  103 GLY   A C   
2461 O O   A GLY   A 103 ? 0.3385 0.3521 0.3068 0.0196  -0.0179 0.0306  103 GLY   A O   
2462 O O   B GLY   A 103 ? 0.3236 0.2765 0.1622 0.0561  -0.0097 0.0130  103 GLY   A O   
2469 N N   A GLU   A 104 ? 0.3305 0.3468 0.2795 0.0139  -0.0095 0.0306  104 GLU   A N   
2470 N N   B GLU   A 104 ? 0.2707 0.2465 0.1404 0.0444  -0.0308 0.0301  104 GLU   A N   
2471 C CA  A GLU   A 104 ? 0.3231 0.3419 0.2687 0.0092  -0.0034 0.0256  104 GLU   A CA  
2472 C CA  B GLU   A 104 ? 0.2428 0.2295 0.1424 0.0282  -0.0278 0.0257  104 GLU   A CA  
2473 C C   A GLU   A 104 ? 0.3215 0.3417 0.2662 0.0087  -0.0063 0.0147  104 GLU   A C   
2474 C C   B GLU   A 104 ? 0.2320 0.2318 0.1654 0.0194  -0.0229 0.0087  104 GLU   A C   
2475 O O   A GLU   A 104 ? 0.3215 0.3410 0.2656 0.0079  -0.0051 0.0119  104 GLU   A O   
2476 O O   B GLU   A 104 ? 0.2250 0.2340 0.2199 0.0173  -0.0244 0.0033  104 GLU   A O   
2477 C CB  A GLU   A 104 ? 0.3178 0.3382 0.2655 0.0061  0.0054  0.0311  104 GLU   A CB  
2478 C CB  B GLU   A 104 ? 0.2310 0.2127 0.1368 0.0164  -0.0240 0.0359  104 GLU   A CB  
2479 C CG  A GLU   A 104 ? 0.3133 0.3344 0.2682 0.0049  0.0127  0.0349  104 GLU   A CG  
2480 C CG  B GLU   A 104 ? 0.2286 0.2106 0.1518 -0.0031 -0.0186 0.0410  104 GLU   A CG  
2481 C CD  A GLU   A 104 ? 0.3098 0.3312 0.2695 0.0055  0.0191  0.0403  104 GLU   A CD  
2482 C CD  B GLU   A 104 ? 0.2343 0.2106 0.1514 -0.0231 -0.0209 0.0483  104 GLU   A CD  
2483 O OE1 A GLU   A 104 ? 0.3079 0.3292 0.2597 0.0053  0.0238  0.0470  104 GLU   A OE1 
2484 O OE1 B GLU   A 104 ? 0.2435 0.2140 0.1589 -0.0302 -0.0258 0.0444  104 GLU   A OE1 
2485 O OE2 A GLU   A 104 ? 0.3109 0.3315 0.2817 0.0076  0.0199  0.0350  104 GLU   A OE2 
2486 O OE2 B GLU   A 104 ? 0.2418 0.2187 0.1759 -0.0293 -0.0078 0.0383  104 GLU   A OE2 
2499 N N   A ASP   A 105 ? 0.3206 0.3435 0.2705 0.0091  -0.0071 0.0041  105 ASP   A N   
2500 N N   B ASP   A 105 ? 0.2379 0.2221 0.1651 0.0135  -0.0155 0.0040  105 ASP   A N   
2501 C CA  A ASP   A 105 ? 0.3179 0.3452 0.2800 0.0094  -0.0087 -0.0117 105 ASP   A CA  
2502 C CA  B ASP   A 105 ? 0.2438 0.2136 0.1940 0.0114  -0.0112 -0.0116 105 ASP   A CA  
2503 C C   A ASP   A 105 ? 0.3074 0.3380 0.2629 -0.0014 -0.0160 -0.0241 105 ASP   A C   
2504 C C   B ASP   A 105 ? 0.2326 0.1889 0.1759 0.0107  -0.0111 -0.0209 105 ASP   A C   
2505 O O   A ASP   A 105 ? 0.3062 0.3405 0.2522 -0.0027 -0.0197 -0.0237 105 ASP   A O   
2506 O O   B ASP   A 105 ? 0.2179 0.1711 0.1570 0.0153  -0.0151 -0.0137 105 ASP   A O   
2507 C CB  A ASP   A 105 ? 0.3256 0.3525 0.3119 0.0190  -0.0019 -0.0148 105 ASP   A CB  
2508 C CB  B ASP   A 105 ? 0.2658 0.2328 0.2547 0.0216  -0.0001 -0.0268 105 ASP   A CB  
2509 C CG  A ASP   A 105 ? 0.3312 0.3585 0.3416 0.0261  -0.0012 -0.0166 105 ASP   A CG  
2510 C CG  B ASP   A 105 ? 0.2890 0.2533 0.3167 0.0317  0.0118  -0.0523 105 ASP   A CG  
2511 O OD1 A ASP   A 105 ? 0.3330 0.3613 0.3500 0.0275  -0.0054 -0.0221 105 ASP   A OD1 
2512 O OD1 B ASP   A 105 ? 0.2921 0.2564 0.3083 0.0274  0.0066  -0.0688 105 ASP   A OD1 
2513 O OD2 A ASP   A 105 ? 0.3351 0.3602 0.3601 0.0300  0.0025  -0.0111 105 ASP   A OD2 
2514 O OD2 B ASP   A 105 ? 0.3031 0.2660 0.3661 0.0387  0.0223  -0.0549 105 ASP   A OD2 
2523 N N   A ILE   A 106 ? 0.2983 0.3266 0.2621 -0.0115 -0.0222 -0.0376 106 ILE   A N   
2524 N N   B ILE   A 106 ? 0.2315 0.2059 0.2035 0.0031  -0.0266 -0.0094 106 ILE   A N   
2525 C CA  A ILE   A 106 ? 0.2886 0.3155 0.2619 -0.0228 -0.0286 -0.0494 106 ILE   A CA  
2526 C CA  B ILE   A 106 ? 0.2214 0.2089 0.2099 -0.0099 -0.0427 -0.0189 106 ILE   A CA  
2527 C C   A ILE   A 106 ? 0.2859 0.3138 0.2689 -0.0292 -0.0256 -0.0522 106 ILE   A C   
2528 C C   B ILE   A 106 ? 0.2161 0.1937 0.1912 -0.0220 -0.0466 -0.0178 106 ILE   A C   
2529 O O   A ILE   A 106 ? 0.2815 0.3134 0.2645 -0.0309 -0.0245 -0.0556 106 ILE   A O   
2530 O O   B ILE   A 106 ? 0.2006 0.1890 0.1921 -0.0261 -0.0263 -0.0128 106 ILE   A O   
2531 C CB  A ILE   A 106 ? 0.2827 0.3056 0.2641 -0.0267 -0.0371 -0.0535 106 ILE   A CB  
2532 C CB  B ILE   A 106 ? 0.2296 0.2433 0.2454 -0.0082 -0.0502 -0.0283 106 ILE   A CB  
2533 C CG1 A ILE   A 106 ? 0.2779 0.3015 0.2748 -0.0282 -0.0360 -0.0499 106 ILE   A CG1 
2534 C CG1 B ILE   A 106 ? 0.2257 0.2572 0.2609 -0.0025 -0.0554 -0.0266 106 ILE   A CG1 
2535 C CG2 A ILE   A 106 ? 0.2806 0.3016 0.2599 -0.0273 -0.0442 -0.0567 106 ILE   A CG2 
2536 C CG2 B ILE   A 106 ? 0.2366 0.2566 0.2563 -0.0140 -0.0539 -0.0373 106 ILE   A CG2 
2537 C CD1 A ILE   A 106 ? 0.2754 0.2999 0.2812 -0.0286 -0.0344 -0.0474 106 ILE   A CD1 
2538 C CD1 B ILE   A 106 ? 0.2241 0.2636 0.2845 0.0001  -0.0499 -0.0286 106 ILE   A CD1 
2561 N N   A GLN   A 107 ? 0.2921 0.3123 0.2919 -0.0304 -0.0185 -0.0541 107 GLN   A N   
2562 N N   B GLN   A 107 ? 0.2404 0.1884 0.2097 -0.0126 -0.0404 -0.0228 107 GLN   A N   
2563 C CA  A GLN   A 107 ? 0.2972 0.3108 0.3217 -0.0282 -0.0102 -0.0520 107 GLN   A CA  
2564 C CA  B GLN   A 107 ? 0.2684 0.1927 0.2619 -0.0031 -0.0253 -0.0145 107 GLN   A CA  
2565 C C   A GLN   A 107 ? 0.2669 0.2810 0.2938 -0.0290 0.0011  -0.0450 107 GLN   A C   
2566 C C   B GLN   A 107 ? 0.2331 0.1611 0.2261 0.0051  -0.0153 0.0066  107 GLN   A C   
2567 O O   A GLN   A 107 ? 0.2705 0.2855 0.3174 -0.0292 0.0098  -0.0433 107 GLN   A O   
2568 O O   B GLN   A 107 ? 0.2359 0.1629 0.2351 0.0031  -0.0206 0.0042  107 GLN   A O   
2569 C CB  A GLN   A 107 ? 0.3312 0.3383 0.3893 -0.0277 -0.0130 -0.0508 107 GLN   A CB  
2570 C CB  B GLN   A 107 ? 0.3264 0.2506 0.3609 -0.0123 -0.0332 -0.0155 107 GLN   A CB  
2571 C CG  A GLN   A 107 ? 0.3611 0.3641 0.4592 -0.0248 -0.0146 -0.0454 107 GLN   A CG  
2572 C CG  B GLN   A 107 ? 0.3869 0.3230 0.4651 -0.0185 -0.0424 0.0040  107 GLN   A CG  
2573 C CD  A GLN   A 107 ? 0.3850 0.3843 0.5176 -0.0227 -0.0166 -0.0379 107 GLN   A CD  
2574 C CD  B GLN   A 107 ? 0.4347 0.3811 0.5543 -0.0230 -0.0477 0.0210  107 GLN   A CD  
2575 O OE1 A GLN   A 107 ? 0.3932 0.3917 0.5401 -0.0215 -0.0178 -0.0361 107 GLN   A OE1 
2576 O OE1 B GLN   A 107 ? 0.4482 0.3976 0.5817 -0.0235 -0.0479 0.0296  107 GLN   A OE1 
2577 N NE2 A GLN   A 107 ? 0.3929 0.3897 0.5373 -0.0227 -0.0176 -0.0360 107 GLN   A NE2 
2578 N NE2 B GLN   A 107 ? 0.4467 0.3967 0.5840 -0.0255 -0.0519 0.0246  107 GLN   A NE2 
2595 N N   A LEU   A 108 ? 0.2358 0.2464 0.2489 -0.0294 0.0049  -0.0366 108 LEU   A N   
2596 N N   B LEU   A 108 ? 0.2069 0.1473 0.1892 -0.0050 -0.0022 -0.0000 108 LEU   A N   
2597 C CA  A LEU   A 108 ? 0.2099 0.2149 0.2133 -0.0197 0.0029  -0.0147 108 LEU   A CA  
2598 C CA  B LEU   A 108 ? 0.1928 0.1491 0.1831 -0.0067 0.0027  0.0133  108 LEU   A CA  
2599 C C   A LEU   A 108 ? 0.1856 0.1777 0.1903 -0.0116 -0.0044 0.0011  108 LEU   A C   
2600 C C   B LEU   A 108 ? 0.1734 0.1394 0.1772 -0.0103 -0.0031 0.0219  108 LEU   A C   
2601 O O   A LEU   A 108 ? 0.1817 0.1797 0.1885 -0.0092 -0.0018 0.0021  108 LEU   A O   
2602 O O   B LEU   A 108 ? 0.1688 0.1480 0.1862 -0.0075 0.0134  0.0285  108 LEU   A O   
2603 C CB  A LEU   A 108 ? 0.2091 0.2217 0.2037 -0.0197 0.0096  -0.0131 108 LEU   A CB  
2604 C CB  B LEU   A 108 ? 0.1977 0.1686 0.1770 -0.0131 0.0081  0.0052  108 LEU   A CB  
2605 C CG  A LEU   A 108 ? 0.2129 0.2290 0.2108 -0.0148 0.0174  -0.0081 108 LEU   A CG  
2606 C CG  B LEU   A 108 ? 0.2176 0.1890 0.2021 -0.0028 0.0167  0.0095  108 LEU   A CG  
2607 C CD1 A LEU   A 108 ? 0.2168 0.2289 0.2168 -0.0165 0.0225  -0.0085 108 LEU   A CD1 
2608 C CD1 B LEU   A 108 ? 0.2290 0.1907 0.2160 -0.0078 0.0253  0.0057  108 LEU   A CD1 
2609 C CD2 A LEU   A 108 ? 0.2137 0.2390 0.2284 -0.0099 0.0196  -0.0035 108 LEU   A CD2 
2610 C CD2 B LEU   A 108 ? 0.2224 0.2122 0.2325 0.0056  0.0151  0.0158  108 LEU   A CD2 
2633 N N   . LEU   A 109 ? 0.1710 0.1479 0.1799 0.0000  -0.0079 0.0167  109 LEU   A N   
2634 C CA  . LEU   A 109 ? 0.1582 0.1370 0.1727 -0.0028 -0.0155 0.0135  109 LEU   A CA  
2635 C C   . LEU   A 109 ? 0.1403 0.1308 0.1763 -0.0059 -0.0021 0.0099  109 LEU   A C   
2636 O O   . LEU   A 109 ? 0.1459 0.1254 0.1918 -0.0081 -0.0057 0.0102  109 LEU   A O   
2637 C CB  . LEU   A 109 ? 0.1653 0.1459 0.1931 0.0019  -0.0152 0.0228  109 LEU   A CB  
2638 C CG  . LEU   A 109 ? 0.1615 0.1579 0.2090 0.0020  -0.0042 0.0267  109 LEU   A CG  
2639 C CD1 . LEU   A 109 ? 0.1719 0.1500 0.2212 -0.0058 0.0018  0.0175  109 LEU   A CD1 
2640 C CD2 . LEU   A 109 ? 0.1568 0.1791 0.2438 -0.0030 -0.0072 0.0261  109 LEU   A CD2 
2653 N N   . LYS   A 110 ? 0.1477 0.1290 0.1731 -0.0047 -0.0135 0.0044  110 LYS   A N   
2654 C CA  . LYS   A 110 ? 0.1383 0.1203 0.1833 -0.0106 -0.0071 0.0082  110 LYS   A CA  
2655 C C   . LYS   A 110 ? 0.1390 0.1194 0.1717 -0.0154 -0.0014 0.0006  110 LYS   A C   
2656 O O   . LYS   A 110 ? 0.1359 0.1206 0.1854 -0.0081 0.0028  0.0031  110 LYS   A O   
2657 C CB  . LYS   A 110 ? 0.1505 0.1324 0.2078 -0.0087 -0.0101 -0.0021 110 LYS   A CB  
2658 C CG  . LYS   A 110 ? 0.1457 0.1275 0.2111 -0.0088 -0.0013 0.0044  110 LYS   A CG  
2659 C CD  . LYS   A 110 ? 0.1471 0.1296 0.2251 -0.0099 -0.0018 -0.0121 110 LYS   A CD  
2660 C CE  . LYS   A 110 ? 0.1623 0.1351 0.2365 -0.0094 0.0118  -0.0062 110 LYS   A CE  
2661 N NZ  . LYS   A 110 ? 0.1652 0.1376 0.2502 -0.0153 0.0166  -0.0009 110 LYS   A NZ  
2675 N N   . SER   A 111 ? 0.1418 0.1216 0.1748 -0.0090 -0.0072 0.0095  111 SER   A N   
2676 C CA  . SER   A 111 ? 0.1366 0.1308 0.1674 -0.0064 -0.0005 0.0049  111 SER   A CA  
2677 C C   . SER   A 111 ? 0.1319 0.1230 0.1604 -0.0088 -0.0016 0.0079  111 SER   A C   
2678 O O   . SER   A 111 ? 0.1426 0.1136 0.1760 -0.0064 0.0030  0.0098  111 SER   A O   
2679 C CB  . SER   A 111 ? 0.1601 0.1520 0.1761 -0.0069 0.0121  -0.0117 111 SER   A CB  
2680 O OG  . SER   A 111 ? 0.1972 0.1757 0.1930 0.0003  0.0234  -0.0153 111 SER   A OG  
2686 N N   . ALA   A 112 ? 0.1344 0.1169 0.1670 -0.0021 0.0041  0.0103  112 ALA   A N   
2687 C CA  . ALA   A 112 ? 0.1376 0.1141 0.1598 -0.0038 0.0070  0.0036  112 ALA   A CA  
2688 C C   . ALA   A 112 ? 0.1271 0.1065 0.1635 -0.0054 0.0034  0.0116  112 ALA   A C   
2689 O O   . ALA   A 112 ? 0.1338 0.1114 0.1766 -0.0139 0.0085  0.0129  112 ALA   A O   
2690 C CB  . ALA   A 112 ? 0.1523 0.1228 0.1665 -0.0019 0.0023  0.0175  112 ALA   A CB  
2696 N N   A TYR   A 113 ? 0.1235 0.1156 0.1631 -0.0049 0.0050  0.0113  113 TYR   A N   
2697 N N   B TYR   A 113 ? 0.1222 0.1140 0.1729 -0.0027 0.0026  0.0126  113 TYR   A N   
2698 C CA  A TYR   A 113 ? 0.1216 0.1183 0.1582 -0.0074 0.0099  0.0102  113 TYR   A CA  
2699 C CA  B TYR   A 113 ? 0.1230 0.1099 0.1686 -0.0057 0.0113  0.0137  113 TYR   A CA  
2700 C C   A TYR   A 113 ? 0.1173 0.1151 0.1585 -0.0098 0.0093  0.0123  113 TYR   A C   
2701 C C   B TYR   A 113 ? 0.1157 0.1105 0.1644 -0.0111 0.0065  0.0140  113 TYR   A C   
2702 O O   A TYR   A 113 ? 0.1173 0.1189 0.1686 -0.0061 0.0155  0.0126  113 TYR   A O   
2703 O O   B TYR   A 113 ? 0.1189 0.1114 0.1836 0.0001  0.0128  0.0150  113 TYR   A O   
2704 C CB  A TYR   A 113 ? 0.1202 0.1283 0.1562 -0.0074 0.0027  0.0077  113 TYR   A CB  
2705 C CB  B TYR   A 113 ? 0.1248 0.1148 0.1716 0.0005  0.0021  0.0172  113 TYR   A CB  
2706 C CG  A TYR   A 113 ? 0.1213 0.1337 0.1538 -0.0140 0.0078  0.0086  113 TYR   A CG  
2707 C CG  B TYR   A 113 ? 0.1313 0.1157 0.1776 -0.0089 0.0108  0.0175  113 TYR   A CG  
2708 C CD1 A TYR   A 113 ? 0.1219 0.1417 0.1522 -0.0089 0.0054  0.0090  113 TYR   A CD1 
2709 C CD1 B TYR   A 113 ? 0.1366 0.1216 0.1822 0.0042  0.0030  0.0193  113 TYR   A CD1 
2710 C CD2 A TYR   A 113 ? 0.1276 0.1378 0.1502 -0.0146 -0.0006 0.0087  113 TYR   A CD2 
2711 C CD2 B TYR   A 113 ? 0.1432 0.1237 0.1821 -0.0087 -0.0009 0.0141  113 TYR   A CD2 
2712 C CE1 A TYR   A 113 ? 0.1226 0.1449 0.1576 -0.0076 0.0046  0.0070  113 TYR   A CE1 
2713 C CE1 B TYR   A 113 ? 0.1423 0.1221 0.1892 0.0023  -0.0011 0.0123  113 TYR   A CE1 
2714 C CE2 A TYR   A 113 ? 0.1237 0.1415 0.1509 -0.0123 0.0012  0.0189  113 TYR   A CE2 
2715 C CE2 B TYR   A 113 ? 0.1465 0.1299 0.1911 -0.0049 -0.0042 0.0207  113 TYR   A CE2 
2716 C CZ  A TYR   A 113 ? 0.1165 0.1432 0.1472 -0.0042 0.0016  0.0213  113 TYR   A CZ  
2717 C CZ  B TYR   A 113 ? 0.1368 0.1281 0.1978 0.0058  -0.0056 0.0181  113 TYR   A CZ  
2718 O OH  A TYR   A 113 ? 0.1158 0.1467 0.1387 0.0046  -0.0036 0.0224  113 TYR   A OH  
2719 O OH  B TYR   A 113 ? 0.1479 0.1400 0.2231 0.0193  -0.0073 0.0110  113 TYR   A OH  
2738 N N   . GLU   A 114 ? 0.1195 0.1073 0.1706 -0.0053 0.0148  0.0162  114 GLU   A N   
2739 C CA  . GLU   A 114 ? 0.1234 0.1081 0.1936 -0.0035 0.0027  0.0178  114 GLU   A CA  
2740 C C   . GLU   A 114 ? 0.1169 0.1090 0.1847 -0.0044 0.0137  0.0169  114 GLU   A C   
2741 O O   . GLU   A 114 ? 0.1304 0.1128 0.1731 -0.0008 0.0062  0.0189  114 GLU   A O   
2742 C CB  . GLU   A 114 ? 0.1221 0.1086 0.1928 -0.0055 0.0056  0.0152  114 GLU   A CB  
2743 C CG  . GLU   A 114 ? 0.1342 0.1146 0.1980 0.0001  0.0088  0.0113  114 GLU   A CG  
2744 C CD  . GLU   A 114 ? 0.1410 0.1109 0.1965 -0.0028 0.0048  0.0056  114 GLU   A CD  
2745 O OE1 . GLU   A 114 ? 0.1431 0.1175 0.1987 -0.0099 0.0126  0.0004  114 GLU   A OE1 
2746 O OE2 . GLU   A 114 ? 0.1616 0.1239 0.2172 -0.0108 0.0204  -0.0163 114 GLU   A OE2 
2754 N N   . ASN   A 115 ? 0.1190 0.1147 0.1751 -0.0100 0.0123  0.0110  115 ASN   A N   
2755 C CA  . ASN   A 115 ? 0.1184 0.1135 0.1805 -0.0078 0.0174  0.0161  115 ASN   A CA  
2756 C C   . ASN   A 115 ? 0.1200 0.1092 0.1851 -0.0108 0.0094  0.0138  115 ASN   A C   
2757 O O   . ASN   A 115 ? 0.1231 0.1271 0.1805 -0.0088 0.0108  0.0162  115 ASN   A O   
2758 C CB  . ASN   A 115 ? 0.1305 0.1239 0.1644 -0.0102 0.0160  0.0159  115 ASN   A CB  
2759 C CG  . ASN   A 115 ? 0.1258 0.1377 0.1721 -0.0137 0.0152  0.0151  115 ASN   A CG  
2760 O OD1 . ASN   A 115 ? 0.1338 0.2452 0.1918 -0.0104 0.0219  0.0272  115 ASN   A OD1 
2761 N ND2 . ASN   A 115 ? 0.1391 0.1267 0.1633 -0.0107 0.0184  0.0229  115 ASN   A ND2 
2768 N N   . PHE   A 116 ? 0.1160 0.1149 0.1809 -0.0042 0.0172  0.0144  116 PHE   A N   
2769 C CA  . PHE   A 116 ? 0.1173 0.1226 0.1701 -0.0025 0.0185  0.0129  116 PHE   A CA  
2770 C C   . PHE   A 116 ? 0.1161 0.1269 0.1664 -0.0038 0.0094  0.0185  116 PHE   A C   
2771 O O   . PHE   A 116 ? 0.1225 0.1347 0.1797 0.0034  0.0156  0.0275  116 PHE   A O   
2772 C CB  . PHE   A 116 ? 0.1230 0.1136 0.1818 -0.0037 0.0182  0.0121  116 PHE   A CB  
2773 C CG  . PHE   A 116 ? 0.1191 0.1127 0.1761 -0.0042 0.0066  0.0088  116 PHE   A CG  
2774 C CD1 . PHE   A 116 ? 0.1179 0.1140 0.1867 -0.0021 0.0113  0.0197  116 PHE   A CD1 
2775 C CD2 . PHE   A 116 ? 0.1222 0.1193 0.1885 -0.0045 0.0197  0.0181  116 PHE   A CD2 
2776 C CE1 . PHE   A 116 ? 0.1207 0.1205 0.1913 -0.0164 0.0128  0.0096  116 PHE   A CE1 
2777 C CE2 . PHE   A 116 ? 0.1239 0.1169 0.2015 -0.0050 0.0190  0.0138  116 PHE   A CE2 
2778 C CZ  . PHE   A 116 ? 0.1335 0.1109 0.1868 -0.0001 0.0132  0.0145  116 PHE   A CZ  
2788 N N   . ASN   A 117 ? 0.1227 0.1212 0.1754 -0.0047 0.0147  0.0235  117 ASN   A N   
2789 C CA  . ASN   A 117 ? 0.1257 0.1179 0.1836 -0.0039 0.0215  0.0265  117 ASN   A CA  
2790 C C   . ASN   A 117 ? 0.1252 0.1288 0.1938 -0.0014 0.0180  0.0201  117 ASN   A C   
2791 O O   . ASN   A 117 ? 0.1341 0.1310 0.2098 -0.0018 0.0035  0.0416  117 ASN   A O   
2792 C CB  . ASN   A 117 ? 0.1238 0.1216 0.1807 -0.0014 0.0131  0.0306  117 ASN   A CB  
2793 C CG  . ASN   A 117 ? 0.1235 0.1209 0.1909 -0.0009 0.0162  0.0263  117 ASN   A CG  
2794 O OD1 . ASN   A 117 ? 0.1196 0.1458 0.2051 -0.0103 0.0192  0.0209  117 ASN   A OD1 
2795 N ND2 . ASN   A 117 ? 0.1162 0.1188 0.2038 -0.0062 0.0155  0.0241  117 ASN   A ND2 
2802 N N   . GLN   A 118 ? 0.1177 0.1282 0.1907 -0.0060 0.0078  0.0335  118 GLN   A N   
2803 C CA  . GLN   A 118 ? 0.1276 0.1354 0.1998 -0.0069 0.0026  0.0186  118 GLN   A CA  
2804 C C   . GLN   A 118 ? 0.1319 0.1474 0.1992 -0.0074 0.0059  0.0288  118 GLN   A C   
2805 O O   . GLN   A 118 ? 0.1298 0.1698 0.2206 0.0022  -0.0060 0.0143  118 GLN   A O   
2806 C CB  . GLN   A 118 ? 0.1269 0.1342 0.2064 0.0005  0.0211  0.0196  118 GLN   A CB  
2807 C CG  . GLN   A 118 ? 0.1270 0.1414 0.2132 0.0016  0.0176  0.0291  118 GLN   A CG  
2808 C CD  . GLN   A 118 ? 0.1243 0.1440 0.2156 0.0066  0.0135  0.0203  118 GLN   A CD  
2809 O OE1 . GLN   A 118 ? 0.1312 0.1653 0.2261 0.0143  0.0017  0.0086  118 GLN   A OE1 
2810 N NE2 . GLN   A 118 ? 0.1274 0.1427 0.2243 0.0076  0.0087  0.0219  118 GLN   A NE2 
2819 N N   . HIS   A 119 ? 0.1319 0.1417 0.1805 0.0012  0.0070  0.0338  119 HIS   A N   
2820 C CA  . HIS   A 119 ? 0.1407 0.1504 0.1775 -0.0007 0.0119  0.0312  119 HIS   A CA  
2821 C C   . HIS   A 119 ? 0.1503 0.1605 0.1809 -0.0046 0.0156  0.0393  119 HIS   A C   
2822 O O   . HIS   A 119 ? 0.1526 0.1591 0.1884 -0.0175 0.0102  0.0336  119 HIS   A O   
2823 C CB  . HIS   A 119 ? 0.1439 0.1447 0.2007 0.0028  0.0246  0.0293  119 HIS   A CB  
2824 C CG  . HIS   A 119 ? 0.1439 0.1480 0.2519 0.0043  0.0274  0.0463  119 HIS   A CG  
2825 N ND1 . HIS   A 119 ? 0.1538 0.1605 0.3146 -0.0057 0.0148  0.0263  119 HIS   A ND1 
2826 C CD2 . HIS   A 119 ? 0.1558 0.1586 0.2743 0.0179  0.0421  0.0652  119 HIS   A CD2 
2827 C CE1 . HIS   A 119 ? 0.1530 0.1647 0.3259 -0.0122 0.0325  0.0448  119 HIS   A CE1 
2828 N NE2 . HIS   A 119 ? 0.1648 0.1602 0.3117 0.0021  0.0509  0.0671  119 HIS   A NE2 
2836 N N   A GLU   A 120 ? 0.1667 0.1847 0.1934 -0.0008 0.0114  0.0492  120 GLU   A N   
2837 N N   B GLU   A 120 ? 0.1504 0.1752 0.1695 -0.0013 0.0012  0.0681  120 GLU   A N   
2838 C CA  A GLU   A 120 ? 0.1872 0.2091 0.2276 0.0065  0.0139  0.0617  120 GLU   A CA  
2839 C CA  B GLU   A 120 ? 0.1667 0.1973 0.2049 0.0122  0.0082  0.0955  120 GLU   A CA  
2840 C C   A GLU   A 120 ? 0.1692 0.1973 0.1981 0.0021  0.0171  0.0636  120 GLU   A C   
2841 C C   B GLU   A 120 ? 0.1527 0.1896 0.1850 0.0025  0.0155  0.0841  120 GLU   A C   
2842 O O   A GLU   A 120 ? 0.1709 0.1981 0.1956 -0.0005 0.0134  0.0613  120 GLU   A O   
2843 O O   B GLU   A 120 ? 0.1513 0.1849 0.1867 -0.0045 0.0100  0.0838  120 GLU   A O   
2844 C CB  A GLU   A 120 ? 0.2303 0.2492 0.2942 0.0137  0.0143  0.0677  120 GLU   A CB  
2845 C CB  B GLU   A 120 ? 0.2138 0.2432 0.2550 0.0205  0.0172  0.1275  120 GLU   A CB  
2846 C CG  A GLU   A 120 ? 0.2787 0.2841 0.3733 0.0231  0.0120  0.0653  120 GLU   A CG  
2847 C CG  B GLU   A 120 ? 0.2824 0.2846 0.3590 0.0362  0.0120  0.1289  120 GLU   A CG  
2848 C CD  A GLU   A 120 ? 0.3197 0.3155 0.4426 0.0324  0.0139  0.0589  120 GLU   A CD  
2849 C CD  B GLU   A 120 ? 0.3406 0.3232 0.4546 0.0516  0.0184  0.1179  120 GLU   A CD  
2850 O OE1 A GLU   A 120 ? 0.3314 0.3274 0.4642 0.0338  0.0132  0.0556  120 GLU   A OE1 
2851 O OE1 B GLU   A 120 ? 0.3591 0.3386 0.4771 0.0547  0.0233  0.1125  120 GLU   A OE1 
2852 O OE2 A GLU   A 120 ? 0.3340 0.3261 0.4707 0.0334  0.0146  0.0553  120 GLU   A OE2 
2853 O OE2 B GLU   A 120 ? 0.3641 0.3356 0.4967 0.0524  0.0188  0.1130  120 GLU   A OE2 
2866 N N   . VAL   A 121 ? 0.1551 0.1842 0.1873 0.0013  0.0180  0.0645  121 VAL   A N   
2867 C CA  . VAL   A 121 ? 0.1614 0.1903 0.1758 -0.0036 0.0295  0.0605  121 VAL   A CA  
2868 C C   . VAL   A 121 ? 0.1480 0.1738 0.1592 -0.0135 0.0226  0.0485  121 VAL   A C   
2869 O O   . VAL   A 121 ? 0.1471 0.1765 0.1852 -0.0220 0.0091  0.0330  121 VAL   A O   
2870 C CB  . VAL   A 121 ? 0.2025 0.2350 0.2112 0.0052  0.0418  0.0705  121 VAL   A CB  
2871 C CG1 . VAL   A 121 ? 0.2065 0.2500 0.2263 0.0133  0.0514  0.0728  121 VAL   A CG1 
2872 C CG2 . VAL   A 121 ? 0.2275 0.2569 0.2413 -0.0021 0.0344  0.0612  121 VAL   A CG2 
2883 N N   . LEU   A 122 ? 0.1432 0.1485 0.1548 -0.0112 0.0249  0.0400  122 LEU   A N   
2884 C CA  . LEU   A 122 ? 0.1453 0.1425 0.1588 -0.0154 0.0332  0.0440  122 LEU   A CA  
2885 C C   . LEU   A 122 ? 0.1429 0.1375 0.1674 -0.0119 0.0225  0.0361  122 LEU   A C   
2886 O O   . LEU   A 122 ? 0.1348 0.1452 0.2058 -0.0194 0.0165  0.0402  122 LEU   A O   
2887 C CB  . LEU   A 122 ? 0.1652 0.1445 0.1872 -0.0058 0.0205  0.0423  122 LEU   A CB  
2888 C CG  . LEU   A 122 ? 0.1749 0.1492 0.1880 -0.0063 0.0283  0.0294  122 LEU   A CG  
2889 C CD1 . LEU   A 122 ? 0.1850 0.1523 0.1987 -0.0118 0.0217  0.0341  122 LEU   A CD1 
2890 C CD2 . LEU   A 122 ? 0.1750 0.1366 0.1795 -0.0035 0.0441  0.0207  122 LEU   A CD2 
2902 N N   . LEU   A 123 ? 0.1361 0.1346 0.1733 -0.0114 0.0214  0.0342  123 LEU   A N   
2903 C CA  . LEU   A 123 ? 0.1344 0.1373 0.1642 -0.0064 0.0267  0.0338  123 LEU   A CA  
2904 C C   . LEU   A 123 ? 0.1255 0.1315 0.1580 -0.0061 0.0232  0.0321  123 LEU   A C   
2905 O O   . LEU   A 123 ? 0.1290 0.1418 0.1768 -0.0182 0.0202  0.0381  123 LEU   A O   
2906 C CB  . LEU   A 123 ? 0.1451 0.1481 0.1650 -0.0081 0.0313  0.0327  123 LEU   A CB  
2907 C CG  . LEU   A 123 ? 0.1481 0.1603 0.1757 -0.0044 0.0358  0.0253  123 LEU   A CG  
2908 C CD1 . LEU   A 123 ? 0.1524 0.1734 0.1943 0.0007  0.0312  0.0160  123 LEU   A CD1 
2909 C CD2 . LEU   A 123 ? 0.1566 0.1608 0.1881 0.0002  0.0256  0.0216  123 LEU   A CD2 
2921 N N   A ALA   A 124 ? 0.1243 0.1288 0.1510 -0.0038 0.0232  0.0302  124 ALA   A N   
2922 N N   B ALA   A 124 ? 0.1221 0.1282 0.1669 -0.0148 0.0232  0.0281  124 ALA   A N   
2923 C CA  A ALA   A 124 ? 0.1219 0.1265 0.1481 0.0019  0.0252  0.0315  124 ALA   A CA  
2924 C CA  B ALA   A 124 ? 0.1171 0.1224 0.1801 -0.0115 0.0187  0.0288  124 ALA   A CA  
2925 C C   A ALA   A 124 ? 0.1259 0.1327 0.1570 -0.0025 0.0275  0.0299  124 ALA   A C   
2926 C C   B ALA   A 124 ? 0.1122 0.1135 0.1874 -0.0179 0.0141  0.0319  124 ALA   A C   
2927 O O   A ALA   A 124 ? 0.1237 0.1395 0.1679 -0.0014 0.0364  0.0313  124 ALA   A O   
2928 O O   B ALA   A 124 ? 0.1162 0.1302 0.2141 -0.0149 0.0205  0.0355  124 ALA   A O   
2929 C CB  A ALA   A 124 ? 0.1210 0.1241 0.1474 0.0050  0.0177  0.0376  124 ALA   A CB  
2930 C CB  B ALA   A 124 ? 0.1237 0.1317 0.1952 -0.0065 0.0036  0.0257  124 ALA   A CB  
2941 N N   A PRO   A 125 ? 0.1356 0.1389 0.1618 -0.0048 0.0219  0.0245  125 PRO   A N   
2942 N N   B PRO   A 125 ? 0.1041 0.1086 0.1771 -0.0057 0.0119  0.0372  125 PRO   A N   
2943 C CA  A PRO   A 125 ? 0.1454 0.1461 0.1652 -0.0064 0.0095  0.0182  125 PRO   A CA  
2944 C CA  B PRO   A 125 ? 0.1155 0.1133 0.1820 -0.0061 0.0054  0.0291  125 PRO   A CA  
2945 C C   A PRO   A 125 ? 0.1423 0.1525 0.1714 -0.0095 0.0028  0.0164  125 PRO   A C   
2946 C C   B PRO   A 125 ? 0.1092 0.1207 0.1972 -0.0140 -0.0011 0.0272  125 PRO   A C   
2947 O O   A PRO   A 125 ? 0.1439 0.1531 0.1679 -0.0120 0.0065  0.0164  125 PRO   A O   
2948 O O   B PRO   A 125 ? 0.1177 0.1136 0.2103 -0.0071 -0.0001 0.0200  125 PRO   A O   
2949 C CB  A PRO   A 125 ? 0.1534 0.1460 0.1688 -0.0064 0.0147  0.0117  125 PRO   A CB  
2950 C CB  B PRO   A 125 ? 0.1237 0.1071 0.1852 -0.0087 0.0057  0.0254  125 PRO   A CB  
2951 C CG  A PRO   A 125 ? 0.1570 0.1458 0.1751 -0.0064 0.0114  0.0120  125 PRO   A CG  
2952 C CG  B PRO   A 125 ? 0.1114 0.1022 0.1720 -0.0132 0.0008  0.0193  125 PRO   A CG  
2953 C CD  A PRO   A 125 ? 0.1443 0.1453 0.1682 -0.0060 0.0194  0.0141  125 PRO   A CD  
2954 C CD  B PRO   A 125 ? 0.1047 0.1013 0.1682 -0.0125 0.0116  0.0233  125 PRO   A CD  
2969 N N   A LEU   A 126 ? 0.1449 0.1602 0.1843 -0.0021 -0.0073 0.0074  126 LEU   A N   
2970 N N   B LEU   A 126 ? 0.1186 0.1434 0.2157 -0.0060 -0.0061 0.0131  126 LEU   A N   
2971 C CA  A LEU   A 126 ? 0.1501 0.1530 0.1982 -0.0056 -0.0167 0.0124  126 LEU   A CA  
2972 C CA  B LEU   A 126 ? 0.1432 0.1421 0.2481 -0.0154 -0.0113 0.0144  126 LEU   A CA  
2973 C C   A LEU   A 126 ? 0.1500 0.1425 0.2012 -0.0035 -0.0132 0.0072  126 LEU   A C   
2974 C C   B LEU   A 126 ? 0.1561 0.1357 0.2421 0.0026  -0.0095 0.0082  126 LEU   A C   
2975 O O   A LEU   A 126 ? 0.1426 0.1305 0.2085 -0.0030 -0.0085 0.0010  126 LEU   A O   
2976 O O   B LEU   A 126 ? 0.1780 0.1394 0.2824 -0.0025 0.0185  0.0051  126 LEU   A O   
2977 C CB  A LEU   A 126 ? 0.1574 0.1635 0.2006 -0.0070 -0.0282 0.0224  126 LEU   A CB  
2978 C CB  B LEU   A 126 ? 0.1616 0.1651 0.2726 -0.0305 -0.0218 0.0210  126 LEU   A CB  
2979 C CG  A LEU   A 126 ? 0.1528 0.1796 0.1947 -0.0040 -0.0243 0.0206  126 LEU   A CG  
2980 C CG  B LEU   A 126 ? 0.1606 0.1784 0.2949 -0.0332 -0.0297 0.0373  126 LEU   A CG  
2981 C CD1 A LEU   A 126 ? 0.1537 0.1838 0.2050 -0.0020 -0.0220 0.0120  126 LEU   A CD1 
2982 C CD1 B LEU   A 126 ? 0.1643 0.1785 0.3100 -0.0299 -0.0401 0.0417  126 LEU   A CD1 
2983 C CD2 A LEU   A 126 ? 0.1555 0.1774 0.1677 -0.0114 -0.0159 0.0369  126 LEU   A CD2 
2984 C CD2 B LEU   A 126 ? 0.1608 0.1758 0.2942 -0.0441 -0.0183 0.0405  126 LEU   A CD2 
3007 N N   A LEU   A 127 ? 0.1625 0.1456 0.1986 -0.0012 -0.0167 0.0067  127 LEU   A N   
3008 N N   B LEU   A 127 ? 0.1518 0.1298 0.1987 0.0151  -0.0234 0.0221  127 LEU   A N   
3009 C CA  A LEU   A 127 ? 0.1750 0.1492 0.1948 -0.0022 -0.0166 0.0146  127 LEU   A CA  
3010 C CA  B LEU   A 127 ? 0.1494 0.1430 0.1934 0.0065  -0.0097 0.0275  127 LEU   A CA  
3011 C C   A LEU   A 127 ? 0.1808 0.1504 0.1875 -0.0063 -0.0190 0.0259  127 LEU   A C   
3012 C C   B LEU   A 127 ? 0.1494 0.1474 0.1898 -0.0054 -0.0112 0.0183  127 LEU   A C   
3013 O O   A LEU   A 127 ? 0.1894 0.1584 0.1735 -0.0092 -0.0175 0.0319  127 LEU   A O   
3014 O O   B LEU   A 127 ? 0.1603 0.1550 0.1821 -0.0199 -0.0057 0.0081  127 LEU   A O   
3015 C CB  A LEU   A 127 ? 0.1787 0.1469 0.1868 0.0050  -0.0170 0.0132  127 LEU   A CB  
3016 C CB  B LEU   A 127 ? 0.1481 0.1603 0.1983 0.0140  -0.0021 0.0246  127 LEU   A CB  
3017 C CG  A LEU   A 127 ? 0.1780 0.1365 0.1807 0.0107  -0.0205 0.0214  127 LEU   A CG  
3018 C CG  B LEU   A 127 ? 0.1494 0.1808 0.2029 0.0141  -0.0059 0.0232  127 LEU   A CG  
3019 C CD1 A LEU   A 127 ? 0.1780 0.1294 0.1833 0.0072  -0.0197 0.0140  127 LEU   A CD1 
3020 C CD1 B LEU   A 127 ? 0.1487 0.1912 0.2157 0.0200  -0.0007 0.0304  127 LEU   A CD1 
3021 C CD2 A LEU   A 127 ? 0.1817 0.1323 0.1841 0.0176  -0.0247 0.0285  127 LEU   A CD2 
3022 C CD2 B LEU   A 127 ? 0.1637 0.1908 0.2077 0.0078  -0.0169 0.0107  127 LEU   A CD2 
3045 N N   A SER   A 128 ? 0.1842 0.1529 0.1968 -0.0097 -0.0248 0.0391  128 SER   A N   
3046 N N   B SER   A 128 ? 0.1608 0.1595 0.2107 -0.0045 -0.0233 0.0296  128 SER   A N   
3047 C CA  A SER   A 128 ? 0.1858 0.1655 0.1836 -0.0126 -0.0251 0.0446  128 SER   A CA  
3048 C CA  B SER   A 128 ? 0.1789 0.1918 0.2148 -0.0036 -0.0216 0.0313  128 SER   A CA  
3049 C C   A SER   A 128 ? 0.1880 0.1752 0.1772 -0.0005 -0.0316 0.0401  128 SER   A C   
3050 C C   B SER   A 128 ? 0.2005 0.2084 0.2210 0.0095  -0.0373 0.0437  128 SER   A C   
3051 O O   A SER   A 128 ? 0.1959 0.1833 0.1705 0.0200  -0.0234 0.0357  128 SER   A O   
3052 O O   B SER   A 128 ? 0.2069 0.2130 0.2251 -0.0046 -0.0348 0.0437  128 SER   A O   
3053 C CB  A SER   A 128 ? 0.1833 0.1718 0.1794 -0.0196 -0.0267 0.0537  128 SER   A CB  
3054 C CB  B SER   A 128 ? 0.1688 0.2068 0.2046 -0.0153 -0.0225 0.0338  128 SER   A CB  
3055 O OG  A SER   A 128 ? 0.1793 0.1747 0.1798 -0.0166 -0.0295 0.0555  128 SER   A OG  
3056 O OG  B SER   A 128 ? 0.1503 0.2122 0.1896 -0.0182 -0.0160 0.0219  128 SER   A OG  
3067 N N   A ALA   A 129 ? 0.1806 0.1899 0.1902 -0.0089 -0.0357 0.0475  129 ALA   A N   
3068 N N   B ALA   A 129 ? 0.2138 0.2350 0.2314 0.0425  -0.0430 0.0609  129 ALA   A N   
3069 C CA  A ALA   A 129 ? 0.1795 0.2019 0.2177 -0.0154 -0.0322 0.0480  129 ALA   A CA  
3070 C CA  B ALA   A 129 ? 0.2423 0.2698 0.2647 0.0495  -0.0381 0.0428  129 ALA   A CA  
3071 C C   A ALA   A 129 ? 0.1802 0.2014 0.2284 -0.0136 -0.0455 0.0346  129 ALA   A C   
3072 C C   B ALA   A 129 ? 0.2795 0.2916 0.2798 0.0579  -0.0364 0.0327  129 ALA   A C   
3073 O O   A ALA   A 129 ? 0.1813 0.2007 0.2458 -0.0170 -0.0544 0.0366  129 ALA   A O   
3074 O O   B ALA   A 129 ? 0.2917 0.3064 0.2870 0.0579  -0.0371 0.0194  129 ALA   A O   
3075 C CB  A ALA   A 129 ? 0.1849 0.2134 0.2353 -0.0097 -0.0216 0.0518  129 ALA   A CB  
3076 C CB  B ALA   A 129 ? 0.2425 0.2850 0.2903 0.0380  -0.0238 0.0405  129 ALA   A CB  
3087 N N   A GLY   A 130 ? 0.1876 0.1991 0.2404 -0.0106 -0.0407 0.0241  130 GLY   A N   
3088 N N   B GLY   A 130 ? 0.2990 0.2913 0.2759 0.0664  -0.0489 0.0454  130 GLY   A N   
3089 C CA  A GLY   A 130 ? 0.2014 0.1968 0.2451 -0.0091 -0.0388 0.0251  130 GLY   A CA  
3090 C CA  B GLY   A 130 ? 0.3127 0.2925 0.2877 0.0661  -0.0436 0.0381  130 GLY   A CA  
3091 C C   A GLY   A 130 ? 0.2123 0.1874 0.2425 -0.0094 -0.0398 0.0308  130 GLY   A C   
3092 C C   B GLY   A 130 ? 0.3228 0.2940 0.2975 0.0528  -0.0426 0.0286  130 GLY   A C   
3093 O O   A GLY   A 130 ? 0.2133 0.1821 0.2522 -0.0143 -0.0290 0.0407  130 GLY   A O   
3094 O O   B GLY   A 130 ? 0.3237 0.2834 0.2821 0.0516  -0.0366 0.0344  130 GLY   A O   
3101 N N   A ILE   A 131 ? 0.2224 0.1786 0.2355 -0.0091 -0.0401 0.0323  131 ILE   A N   
3102 N N   B ILE   A 131 ? 0.3289 0.2947 0.3314 0.0464  -0.0480 0.0197  131 ILE   A N   
3103 C CA  A ILE   A 131 ? 0.2225 0.1711 0.2118 -0.0092 -0.0558 0.0390  131 ILE   A CA  
3104 C CA  B ILE   A 131 ? 0.3281 0.2887 0.3500 0.0449  -0.0699 0.0262  131 ILE   A CA  
3105 C C   A ILE   A 131 ? 0.2137 0.1708 0.1953 -0.0196 -0.0593 0.0429  131 ILE   A C   
3106 C C   B ILE   A 131 ? 0.3112 0.2754 0.3192 0.0479  -0.0913 0.0499  131 ILE   A C   
3107 O O   A ILE   A 131 ? 0.2106 0.1781 0.1940 -0.0171 -0.0740 0.0190  131 ILE   A O   
3108 O O   B ILE   A 131 ? 0.3106 0.2765 0.3170 0.0487  -0.0764 0.0621  131 ILE   A O   
3109 C CB  A ILE   A 131 ? 0.2327 0.1775 0.2175 -0.0091 -0.0513 0.0265  131 ILE   A CB  
3110 C CB  B ILE   A 131 ? 0.3482 0.3045 0.4072 0.0341  -0.0630 0.0075  131 ILE   A CB  
3111 C CG1 A ILE   A 131 ? 0.2393 0.1906 0.2254 -0.0162 -0.0483 0.0033  131 ILE   A CG1 
3112 C CG1 B ILE   A 131 ? 0.3608 0.3131 0.4492 0.0284  -0.0561 -0.0011 131 ILE   A CG1 
3113 C CG2 A ILE   A 131 ? 0.2348 0.1752 0.2185 -0.0053 -0.0438 0.0322  131 ILE   A CG2 
3114 C CG2 B ILE   A 131 ? 0.3561 0.3111 0.4243 0.0303  -0.0603 0.0011  131 ILE   A CG2 
3115 C CD1 A ILE   A 131 ? 0.2428 0.1964 0.2356 -0.0176 -0.0473 -0.0041 131 ILE   A CD1 
3116 C CD1 B ILE   A 131 ? 0.3687 0.3203 0.4751 0.0264  -0.0504 -0.0036 131 ILE   A CD1 
3139 N N   A PHE   A 132 ? 0.2119 0.1620 0.1938 -0.0200 -0.0565 0.0609  132 PHE   A N   
3140 N N   B PHE   A 132 ? 0.3006 0.2624 0.2939 0.0429  -0.1132 0.0622  132 PHE   A N   
3141 C CA  A PHE   A 132 ? 0.2173 0.1826 0.1958 -0.0196 -0.0592 0.0385  132 PHE   A CA  
3142 C CA  B PHE   A 132 ? 0.2878 0.2674 0.3023 0.0304  -0.1116 0.0440  132 PHE   A CA  
3143 C C   A PHE   A 132 ? 0.2207 0.2042 0.2063 -0.0170 -0.0645 0.0309  132 PHE   A C   
3144 C C   B PHE   A 132 ? 0.2813 0.2845 0.2837 0.0271  -0.1002 0.0311  132 PHE   A C   
3145 O O   A PHE   A 132 ? 0.2259 0.2109 0.2046 -0.0177 -0.0727 0.0150  132 PHE   A O   
3146 O O   B PHE   A 132 ? 0.2891 0.2868 0.2878 0.0303  -0.0875 0.0200  132 PHE   A O   
3147 C CB  A PHE   A 132 ? 0.2167 0.1698 0.1735 -0.0171 -0.0612 0.0387  132 PHE   A CB  
3148 C CB  B PHE   A 132 ? 0.2840 0.2569 0.3440 0.0239  -0.1204 0.0383  132 PHE   A CB  
3149 C CG  A PHE   A 132 ? 0.2149 0.1636 0.1563 -0.0105 -0.0634 0.0323  132 PHE   A CG  
3150 C CG  B PHE   A 132 ? 0.2867 0.2528 0.4038 0.0189  -0.1148 0.0401  132 PHE   A CG  
3151 C CD1 A PHE   A 132 ? 0.2182 0.1704 0.1705 0.0001  -0.0600 0.0191  132 PHE   A CD1 
3152 C CD1 B PHE   A 132 ? 0.2925 0.2567 0.4366 0.0129  -0.1104 0.0341  132 PHE   A CD1 
3153 C CD2 A PHE   A 132 ? 0.2128 0.1625 0.1505 -0.0155 -0.0592 0.0341  132 PHE   A CD2 
3154 C CD2 B PHE   A 132 ? 0.2872 0.2527 0.4173 0.0167  -0.1098 0.0387  132 PHE   A CD2 
3155 C CE1 A PHE   A 132 ? 0.2158 0.1756 0.1588 0.0004  -0.0622 0.0201  132 PHE   A CE1 
3156 C CE1 B PHE   A 132 ? 0.2925 0.2575 0.4491 0.0114  -0.1084 0.0288  132 PHE   A CE1 
3157 C CE2 A PHE   A 132 ? 0.2103 0.1637 0.1520 -0.0097 -0.0631 0.0275  132 PHE   A CE2 
3158 C CE2 B PHE   A 132 ? 0.2890 0.2547 0.4347 0.0093  -0.1103 0.0316  132 PHE   A CE2 
3159 C CZ  A PHE   A 132 ? 0.2099 0.1666 0.1431 -0.0042 -0.0681 0.0231  132 PHE   A CZ  
3160 C CZ  B PHE   A 132 ? 0.2873 0.2558 0.4457 0.0086  -0.1134 0.0261  132 PHE   A CZ  
3179 N N   A GLY   A 133 ? 0.2181 0.2203 0.2085 -0.0126 -0.0772 0.0444  133 GLY   A N   
3180 N N   B GLY   A 133 ? 0.2693 0.2914 0.2692 0.0202  -0.0925 0.0292  133 GLY   A N   
3181 C CA  A GLY   A 133 ? 0.2155 0.2397 0.2191 -0.0158 -0.0830 0.0372  133 GLY   A CA  
3182 C CA  B GLY   A 133 ? 0.2600 0.3072 0.2623 0.0044  -0.0971 0.0185  133 GLY   A CA  
3183 C C   A GLY   A 133 ? 0.2102 0.2539 0.2246 -0.0224 -0.0853 0.0237  133 GLY   A C   
3184 C C   B GLY   A 133 ? 0.2519 0.3190 0.2724 -0.0150 -0.0959 0.0076  133 GLY   A C   
3185 O O   A GLY   A 133 ? 0.2151 0.2654 0.2342 -0.0310 -0.0851 0.0021  133 GLY   A O   
3186 O O   B GLY   A 133 ? 0.2536 0.3364 0.2840 -0.0239 -0.1013 0.0017  133 GLY   A O   
3193 N N   A ALA   A 134 ? 0.2084 0.2525 0.2292 -0.0222 -0.0674 0.0285  134 ALA   A N   
3194 N N   B ALA   A 134 ? 0.2442 0.3079 0.2684 -0.0269 -0.0792 -0.0008 134 ALA   A N   
3195 C CA  A ALA   A 134 ? 0.2076 0.2535 0.2446 -0.0203 -0.0465 0.0303  134 ALA   A CA  
3196 C CA  B ALA   A 134 ? 0.2413 0.3039 0.2715 -0.0332 -0.0652 0.0027  134 ALA   A CA  
3197 C C   A ALA   A 134 ? 0.2071 0.2556 0.2502 -0.0190 -0.0400 0.0321  134 ALA   A C   
3198 C C   B ALA   A 134 ? 0.2360 0.3069 0.2601 -0.0331 -0.0584 0.0286  134 ALA   A C   
3199 O O   A ALA   A 134 ? 0.2132 0.2598 0.2668 -0.0155 -0.0342 0.0302  134 ALA   A O   
3200 O O   B ALA   A 134 ? 0.2444 0.3064 0.2615 -0.0329 -0.0526 0.0454  134 ALA   A O   
3201 C CB  A ALA   A 134 ? 0.2062 0.2515 0.2518 -0.0203 -0.0367 0.0291  134 ALA   A CB  
3202 C CB  B ALA   A 134 ? 0.2413 0.2979 0.2884 -0.0370 -0.0591 -0.0108 134 ALA   A CB  
3213 N N   A ASP   A 135 ? 0.2011 0.2513 0.2351 -0.0242 -0.0371 0.0354  135 ASP   A N   
3214 N N   B ASP   A 135 ? 0.2251 0.3089 0.2656 -0.0298 -0.0491 0.0528  135 ASP   A N   
3215 C CA  A ASP   A 135 ? 0.1955 0.2489 0.2190 -0.0294 -0.0529 0.0378  135 ASP   A CA  
3216 C CA  B ASP   A 135 ? 0.2189 0.3145 0.2719 -0.0250 -0.0486 0.0706  135 ASP   A CA  
3217 C C   A ASP   A 135 ? 0.1912 0.2337 0.1925 -0.0170 -0.0489 0.0424  135 ASP   A C   
3218 C C   B ASP   A 135 ? 0.2028 0.3008 0.2273 -0.0074 -0.0470 0.0684  135 ASP   A C   
3219 O O   A ASP   A 135 ? 0.1859 0.2293 0.1771 -0.0226 -0.0452 0.0466  135 ASP   A O   
3220 O O   B ASP   A 135 ? 0.1900 0.2896 0.2060 -0.0182 -0.0362 0.0504  135 ASP   A O   
3221 C CB  A ASP   A 135 ? 0.1995 0.2638 0.2374 -0.0428 -0.0677 0.0282  135 ASP   A CB  
3222 C CB  B ASP   A 135 ? 0.2366 0.3332 0.3467 -0.0295 -0.0424 0.0797  135 ASP   A CB  
3223 C CG  A ASP   A 135 ? 0.1992 0.2739 0.2563 -0.0500 -0.0814 0.0176  135 ASP   A CG  
3224 C CG  B ASP   A 135 ? 0.2474 0.3442 0.4181 -0.0234 -0.0425 0.0895  135 ASP   A CG  
3225 O OD1 A ASP   A 135 ? 0.1954 0.2777 0.2586 -0.0518 -0.0878 0.0256  135 ASP   A OD1 
3226 O OD1 B ASP   A 135 ? 0.2592 0.3517 0.4587 -0.0178 -0.0295 0.0921  135 ASP   A OD1 
3227 O OD2 A ASP   A 135 ? 0.2102 0.2819 0.2804 -0.0519 -0.0710 0.0055  135 ASP   A OD2 
3228 O OD2 B ASP   A 135 ? 0.2496 0.3459 0.4362 -0.0169 -0.0494 0.0966  135 ASP   A OD2 
3237 N N   A PRO   A 136 ? 0.1888 0.2177 0.1955 -0.0026 -0.0467 0.0421  136 PRO   A N   
3238 N N   B PRO   A 136 ? 0.1943 0.2913 0.2195 0.0169  -0.0373 0.0782  136 PRO   A N   
3239 C CA  A PRO   A 136 ? 0.1833 0.2089 0.1946 -0.0005 -0.0362 0.0350  136 PRO   A CA  
3240 C CA  B PRO   A 136 ? 0.1823 0.2737 0.2125 0.0180  -0.0227 0.0644  136 PRO   A CA  
3241 C C   A PRO   A 136 ? 0.1668 0.2024 0.1818 -0.0051 -0.0261 0.0245  136 PRO   A C   
3242 C C   B PRO   A 136 ? 0.1511 0.2561 0.2260 0.0103  -0.0205 0.0367  136 PRO   A C   
3243 O O   A PRO   A 136 ? 0.1594 0.1920 0.1723 -0.0085 -0.0226 0.0358  136 PRO   A O   
3244 O O   B PRO   A 136 ? 0.1340 0.2379 0.2159 0.0139  -0.0085 0.0329  136 PRO   A O   
3245 C CB  A PRO   A 136 ? 0.1960 0.2073 0.2051 0.0041  -0.0379 0.0340  136 PRO   A CB  
3246 C CB  B PRO   A 136 ? 0.2041 0.2781 0.2308 0.0222  -0.0146 0.0711  136 PRO   A CB  
3247 C CG  A PRO   A 136 ? 0.2012 0.2112 0.2163 0.0059  -0.0459 0.0326  136 PRO   A CG  
3248 C CG  B PRO   A 136 ? 0.2155 0.2918 0.2464 0.0247  -0.0222 0.0668  136 PRO   A CG  
3249 C CD  A PRO   A 136 ? 0.1951 0.2108 0.2035 0.0035  -0.0460 0.0458  136 PRO   A CD  
3250 C CD  B PRO   A 136 ? 0.2072 0.2938 0.2382 0.0238  -0.0321 0.0823  136 PRO   A CD  
3265 N N   A ILE   A 137 ? 0.1676 0.2071 0.1835 -0.0093 -0.0207 0.0020  137 ILE   A N   
3266 N N   B ILE   A 137 ? 0.1588 0.2651 0.2380 -0.0018 -0.0355 0.0224  137 ILE   A N   
3267 C CA  A ILE   A 137 ? 0.1659 0.2120 0.1851 -0.0163 -0.0120 -0.0117 137 ILE   A CA  
3268 C CA  B ILE   A 137 ? 0.1537 0.2716 0.2518 -0.0082 -0.0336 0.0036  137 ILE   A CA  
3269 C C   A ILE   A 137 ? 0.1624 0.2009 0.1776 -0.0244 -0.0026 -0.0008 137 ILE   A C   
3270 C C   B ILE   A 137 ? 0.1522 0.2588 0.2339 -0.0088 -0.0311 0.0073  137 ILE   A C   
3271 O O   A ILE   A 137 ? 0.1613 0.2004 0.1836 -0.0354 -0.0014 0.0050  137 ILE   A O   
3272 O O   B ILE   A 137 ? 0.1461 0.2471 0.2477 -0.0178 -0.0132 -0.0041 137 ILE   A O   
3273 C CB  A ILE   A 137 ? 0.1648 0.2250 0.2054 -0.0179 -0.0218 -0.0273 137 ILE   A CB  
3274 C CB  B ILE   A 137 ? 0.1572 0.2896 0.2799 -0.0023 -0.0336 -0.0086 137 ILE   A CB  
3275 C CG1 A ILE   A 137 ? 0.1764 0.2373 0.2239 -0.0140 -0.0251 -0.0337 137 ILE   A CG1 
3276 C CG1 B ILE   A 137 ? 0.1702 0.3028 0.2962 0.0077  -0.0308 -0.0194 137 ILE   A CG1 
3277 C CG2 A ILE   A 137 ? 0.1658 0.2274 0.2134 -0.0136 -0.0231 -0.0311 137 ILE   A CG2 
3278 C CG2 B ILE   A 137 ? 0.1709 0.2964 0.2891 -0.0069 -0.0377 -0.0142 137 ILE   A CG2 
3279 C CD1 A ILE   A 137 ? 0.1836 0.2430 0.2364 -0.0114 -0.0204 -0.0347 137 ILE   A CD1 
3280 C CD1 B ILE   A 137 ? 0.1890 0.3134 0.3089 0.0111  -0.0278 -0.0231 137 ILE   A CD1 
3303 N N   A HIS   A 138 ? 0.1623 0.1973 0.1687 -0.0191 0.0083  -0.0039 138 HIS   A N   
3304 N N   B HIS   A 138 ? 0.1613 0.2587 0.2226 0.0039  -0.0286 0.0033  138 HIS   A N   
3305 C CA  A HIS   A 138 ? 0.1562 0.1870 0.1697 -0.0195 0.0071  0.0010  138 HIS   A CA  
3306 C CA  B HIS   A 138 ? 0.1661 0.2516 0.2220 0.0056  -0.0216 -0.0114 138 HIS   A CA  
3307 C C   A HIS   A 138 ? 0.1484 0.1639 0.1626 -0.0198 0.0035  0.0062  138 HIS   A C   
3308 C C   B HIS   A 138 ? 0.1546 0.2249 0.2131 0.0043  -0.0249 -0.0142 138 HIS   A C   
3309 O O   A HIS   A 138 ? 0.1519 0.1630 0.1691 -0.0219 -0.0003 0.0033  138 HIS   A O   
3310 O O   B HIS   A 138 ? 0.1608 0.2239 0.2215 0.0061  -0.0217 -0.0110 138 HIS   A O   
3311 C CB  A HIS   A 138 ? 0.1622 0.1998 0.1766 -0.0160 -0.0042 -0.0062 138 HIS   A CB  
3312 C CB  B HIS   A 138 ? 0.1860 0.2623 0.2214 0.0110  -0.0227 -0.0127 138 HIS   A CB  
3313 C CG  A HIS   A 138 ? 0.1662 0.2079 0.1960 -0.0153 -0.0041 -0.0167 138 HIS   A CG  
3314 C CG  B HIS   A 138 ? 0.2010 0.2649 0.2371 0.0109  -0.0128 -0.0206 138 HIS   A CG  
3315 N ND1 A HIS   A 138 ? 0.1719 0.2136 0.2114 -0.0146 -0.0004 -0.0282 138 HIS   A ND1 
3316 N ND1 B HIS   A 138 ? 0.2087 0.2658 0.2487 0.0129  -0.0088 -0.0328 138 HIS   A ND1 
3317 C CD2 A HIS   A 138 ? 0.1662 0.2146 0.2022 -0.0135 -0.0115 -0.0198 138 HIS   A CD2 
3318 C CD2 B HIS   A 138 ? 0.2071 0.2685 0.2444 0.0113  -0.0181 -0.0187 138 HIS   A CD2 
3319 C CE1 A HIS   A 138 ? 0.1730 0.2164 0.2172 -0.0131 -0.0020 -0.0277 138 HIS   A CE1 
3320 C CE1 B HIS   A 138 ? 0.2130 0.2699 0.2493 0.0132  -0.0070 -0.0314 138 HIS   A CE1 
3321 N NE2 A HIS   A 138 ? 0.1698 0.2175 0.2097 -0.0120 -0.0052 -0.0255 138 HIS   A NE2 
3322 N NE2 B HIS   A 138 ? 0.2083 0.2700 0.2466 0.0132  -0.0187 -0.0238 138 HIS   A NE2 
3337 N N   A SER   A 139 ? 0.1392 0.1474 0.1489 -0.0104 0.0074  0.0117  139 SER   A N   
3338 N N   B SER   A 139 ? 0.1435 0.2016 0.2019 0.0093  -0.0154 -0.0138 139 SER   A N   
3339 C CA  A SER   A 139 ? 0.1368 0.1430 0.1438 -0.0062 0.0137  0.0093  139 SER   A CA  
3340 C CA  B SER   A 139 ? 0.1321 0.1848 0.1878 0.0058  -0.0080 -0.0024 139 SER   A CA  
3341 C C   A SER   A 139 ? 0.1322 0.1392 0.1411 -0.0075 0.0113  0.0149  139 SER   A C   
3342 C C   B SER   A 139 ? 0.1242 0.1732 0.2017 -0.0039 -0.0079 0.0050  139 SER   A C   
3343 O O   A SER   A 139 ? 0.1369 0.1330 0.1546 -0.0072 -0.0033 0.0189  139 SER   A O   
3344 O O   B SER   A 139 ? 0.1240 0.1594 0.2081 -0.0067 -0.0084 0.0064  139 SER   A O   
3345 C CB  A SER   A 139 ? 0.1396 0.1405 0.1394 -0.0012 0.0195  0.0071  139 SER   A CB  
3346 C CB  B SER   A 139 ? 0.1337 0.1703 0.1813 0.0087  0.0047  0.0040  139 SER   A CB  
3347 O OG  A SER   A 139 ? 0.1441 0.1362 0.1532 -0.0023 0.0122  0.0077  139 SER   A OG  
3348 O OG  B SER   A 139 ? 0.1336 0.1516 0.1704 0.0125  -0.0008 0.0096  139 SER   A OG  
3359 N N   A LEU   A 140 ? 0.1368 0.1503 0.1392 -0.0145 0.0161  0.0248  140 LEU   A N   
3360 N N   B LEU   A 140 ? 0.1251 0.1814 0.2107 0.0027  -0.0137 0.0088  140 LEU   A N   
3361 C CA  A LEU   A 140 ? 0.1395 0.1509 0.1543 -0.0214 0.0115  0.0274  140 LEU   A CA  
3362 C CA  B LEU   A 140 ? 0.1148 0.1735 0.2214 0.0084  -0.0101 0.0146  140 LEU   A CA  
3363 C C   A LEU   A 140 ? 0.1370 0.1618 0.1692 -0.0343 0.0049  0.0215  140 LEU   A C   
3364 C C   B LEU   A 140 ? 0.1124 0.1738 0.2224 -0.0015 -0.0059 0.0187  140 LEU   A C   
3365 O O   A LEU   A 140 ? 0.1329 0.1609 0.1772 -0.0378 0.0001  0.0257  140 LEU   A O   
3366 O O   B LEU   A 140 ? 0.1208 0.1685 0.2338 0.0094  -0.0039 0.0192  140 LEU   A O   
3367 C CB  A LEU   A 140 ? 0.1418 0.1518 0.1524 -0.0266 0.0116  0.0374  140 LEU   A CB  
3368 C CB  B LEU   A 140 ? 0.1131 0.1806 0.2424 0.0065  -0.0067 0.0146  140 LEU   A CB  
3369 C CG  A LEU   A 140 ? 0.1441 0.1556 0.1678 -0.0331 0.0135  0.0427  140 LEU   A CG  
3370 C CG  B LEU   A 140 ? 0.1123 0.1895 0.2603 -0.0104 0.0049  0.0268  140 LEU   A CG  
3371 C CD1 A LEU   A 140 ? 0.1470 0.1606 0.1793 -0.0294 0.0147  0.0397  140 LEU   A CD1 
3372 C CD1 B LEU   A 140 ? 0.1233 0.1910 0.2650 -0.0055 -0.0001 0.0382  140 LEU   A CD1 
3373 C CD2 A LEU   A 140 ? 0.1502 0.1562 0.1695 -0.0312 0.0182  0.0438  140 LEU   A CD2 
3374 C CD2 B LEU   A 140 ? 0.1277 0.1916 0.2654 -0.0065 0.0121  0.0224  140 LEU   A CD2 
3397 N N   A ARG   A 141 ? 0.1492 0.1720 0.1818 -0.0342 -0.0035 0.0056  141 ARG   A N   
3398 N N   B ARG   A 141 ? 0.1167 0.1764 0.2243 -0.0083 -0.0178 0.0046  141 ARG   A N   
3399 C CA  A ARG   A 141 ? 0.1590 0.1866 0.2025 -0.0307 -0.0087 -0.0053 141 ARG   A CA  
3400 C CA  B ARG   A 141 ? 0.1360 0.1896 0.2406 -0.0215 -0.0178 -0.0144 141 ARG   A CA  
3401 C C   A ARG   A 141 ? 0.1479 0.1795 0.1944 -0.0191 -0.0092 -0.0045 141 ARG   A C   
3402 C C   B ARG   A 141 ? 0.1394 0.1797 0.2264 -0.0178 -0.0082 -0.0051 141 ARG   A C   
3403 O O   A ARG   A 141 ? 0.1446 0.1761 0.1839 -0.0138 -0.0010 -0.0164 141 ARG   A O   
3404 O O   B ARG   A 141 ? 0.1362 0.1624 0.2320 -0.0221 0.0072  -0.0154 141 ARG   A O   
3405 C CB  A ARG   A 141 ? 0.1829 0.2098 0.2336 -0.0266 -0.0110 -0.0187 141 ARG   A CB  
3406 C CB  B ARG   A 141 ? 0.1536 0.2154 0.2741 -0.0318 -0.0188 -0.0396 141 ARG   A CB  
3407 C CG  A ARG   A 141 ? 0.2083 0.2308 0.2724 -0.0258 -0.0151 -0.0198 141 ARG   A CG  
3408 C CG  B ARG   A 141 ? 0.1839 0.2503 0.3068 -0.0312 -0.0138 -0.0512 141 ARG   A CG  
3409 C CD  A ARG   A 141 ? 0.2316 0.2482 0.3091 -0.0267 -0.0216 -0.0129 141 ARG   A CD  
3410 C CD  B ARG   A 141 ? 0.2068 0.2866 0.3429 -0.0385 -0.0055 -0.0403 141 ARG   A CD  
3411 N NE  A ARG   A 141 ? 0.2397 0.2581 0.3283 -0.0244 -0.0273 -0.0096 141 ARG   A NE  
3412 N NE  B ARG   A 141 ? 0.2063 0.3213 0.3632 -0.0471 -0.0013 -0.0356 141 ARG   A NE  
3413 C CZ  A ARG   A 141 ? 0.2476 0.2702 0.3449 -0.0267 -0.0248 -0.0027 141 ARG   A CZ  
3414 C CZ  B ARG   A 141 ? 0.2039 0.3431 0.3720 -0.0665 0.0076  -0.0236 141 ARG   A CZ  
3415 N NH1 A ARG   A 141 ? 0.2471 0.2741 0.3511 -0.0292 -0.0196 -0.0063 141 ARG   A NH1 
3416 N NH1 B ARG   A 141 ? 0.1965 0.3466 0.3795 -0.0818 0.0284  -0.0282 141 ARG   A NH1 
3417 N NH2 A ARG   A 141 ? 0.2548 0.2753 0.3528 -0.0239 -0.0279 0.0006  141 ARG   A NH2 
3418 N NH2 B ARG   A 141 ? 0.2115 0.3575 0.3775 -0.0643 -0.0008 -0.0199 141 ARG   A NH2 
3445 N N   . VAL   A 142 ? 0.1351 0.1760 0.2090 -0.0101 -0.0132 0.0050  142 VAL   A N   
3446 C CA  . VAL   A 142 ? 0.1320 0.1703 0.2188 -0.0114 0.0067  0.0046  142 VAL   A CA  
3447 C C   . VAL   A 142 ? 0.1254 0.1534 0.2095 -0.0183 0.0058  0.0081  142 VAL   A C   
3448 O O   . VAL   A 142 ? 0.1317 0.1546 0.2181 -0.0062 0.0003  0.0084  142 VAL   A O   
3449 C CB  . VAL   A 142 ? 0.1445 0.1861 0.2085 -0.0118 0.0018  0.0183  142 VAL   A CB  
3450 C CG1 . VAL   A 142 ? 0.1375 0.1629 0.2071 -0.0166 0.0018  0.0248  142 VAL   A CG1 
3451 C CG2 . VAL   A 142 ? 0.1594 0.2086 0.2304 -0.0151 0.0033  0.0184  142 VAL   A CG2 
3462 N N   . CYS   A 143 ? 0.1251 0.1506 0.2059 -0.0109 0.0021  0.0178  143 CYS   A N   
3463 C CA  . CYS   A 143 ? 0.1259 0.1444 0.2127 -0.0088 -0.0024 0.0258  143 CYS   A CA  
3464 C C   . CYS   A 143 ? 0.1283 0.1328 0.2139 -0.0134 0.0015  0.0211  143 CYS   A C   
3465 O O   . CYS   A 143 ? 0.1243 0.1347 0.2141 -0.0092 0.0038  0.0217  143 CYS   A O   
3466 C CB  . CYS   A 143 ? 0.1381 0.1458 0.2176 -0.0046 0.0038  0.0307  143 CYS   A CB  
3467 S SG  . CYS   A 143 ? 0.1531 0.1479 0.2108 0.0031  0.0026  0.0134  143 CYS   A SG  
3473 N N   . VAL   A 144 ? 0.1241 0.1385 0.2295 -0.0152 0.0076  0.0187  144 VAL   A N   
3474 C CA  . VAL   A 144 ? 0.1302 0.1498 0.2601 -0.0146 0.0191  0.0190  144 VAL   A CA  
3475 C C   . VAL   A 144 ? 0.1319 0.1376 0.2514 -0.0177 -0.0032 0.0100  144 VAL   A C   
3476 O O   . VAL   A 144 ? 0.1499 0.1458 0.2519 -0.0047 0.0043  0.0242  144 VAL   A O   
3477 C CB  . VAL   A 144 ? 0.1476 0.1679 0.3022 -0.0024 0.0260  0.0200  144 VAL   A CB  
3478 C CG1 . VAL   A 144 ? 0.1582 0.1847 0.3247 -0.0189 0.0242  0.0215  144 VAL   A CG1 
3479 C CG2 . VAL   A 144 ? 0.1429 0.1681 0.3226 -0.0026 0.0188  0.0357  144 VAL   A CG2 
3489 N N   . ASP   A 145 ? 0.1429 0.1386 0.2627 -0.0232 -0.0000 0.0022  145 ASP   A N   
3490 C CA  . ASP   A 145 ? 0.1525 0.1510 0.2705 -0.0223 0.0033  -0.0094 145 ASP   A CA  
3491 C C   . ASP   A 145 ? 0.1444 0.1419 0.2713 -0.0200 0.0054  -0.0165 145 ASP   A C   
3492 O O   . ASP   A 145 ? 0.1587 0.1553 0.3317 -0.0197 0.0000  -0.0447 145 ASP   A O   
3493 C CB  . ASP   A 145 ? 0.1635 0.1818 0.2916 -0.0317 -0.0019 -0.0260 145 ASP   A CB  
3494 C CG  . ASP   A 145 ? 0.1791 0.2181 0.3212 -0.0455 -0.0078 -0.0227 145 ASP   A CG  
3495 O OD1 . ASP   A 145 ? 0.1752 0.2255 0.3436 -0.0571 0.0029  -0.0171 145 ASP   A OD1 
3496 O OD2 . ASP   A 145 ? 0.2010 0.2414 0.3344 -0.0513 -0.0331 -0.0252 145 ASP   A OD2 
3501 N N   . THR   A 146 ? 0.1368 0.1299 0.2287 -0.0162 0.0058  0.0029  146 THR   A N   
3502 C CA  . THR   A 146 ? 0.1288 0.1303 0.2231 -0.0132 0.0111  0.0046  146 THR   A CA  
3503 C C   . THR   A 146 ? 0.1256 0.1267 0.2273 -0.0069 0.0060  0.0134  146 THR   A C   
3504 O O   . THR   A 146 ? 0.1343 0.1402 0.2308 -0.0017 -0.0007 0.0146  146 THR   A O   
3505 C CB  . THR   A 146 ? 0.1265 0.1316 0.2168 -0.0062 0.0116  0.0077  146 THR   A CB  
3506 O OG1 . THR   A 146 ? 0.1338 0.1500 0.2161 -0.0089 0.0007  -0.0024 146 THR   A OG1 
3507 C CG2 . THR   A 146 ? 0.1317 0.1361 0.2260 -0.0140 0.0104  0.0131  146 THR   A CG2 
3515 N N   . VAL   A 147 ? 0.1222 0.1308 0.2108 -0.0089 0.0125  0.0132  147 VAL   A N   
3516 C CA  . VAL   A 147 ? 0.1187 0.1334 0.2099 -0.0140 0.0229  0.0173  147 VAL   A CA  
3517 C C   . VAL   A 147 ? 0.1283 0.1330 0.2173 -0.0132 0.0228  0.0226  147 VAL   A C   
3518 O O   . VAL   A 147 ? 0.1292 0.1308 0.2420 -0.0119 0.0143  0.0275  147 VAL   A O   
3519 C CB  . VAL   A 147 ? 0.1327 0.1317 0.2060 -0.0116 0.0206  0.0292  147 VAL   A CB  
3520 C CG1 . VAL   A 147 ? 0.1589 0.1389 0.2112 -0.0034 0.0167  0.0428  147 VAL   A CG1 
3521 C CG2 . VAL   A 147 ? 0.1346 0.1304 0.2135 -0.0086 0.0091  0.0247  147 VAL   A CG2 
3531 N N   . ARG   A 148 ? 0.1292 0.1340 0.2293 -0.0122 0.0228  0.0394  148 ARG   A N   
3532 C CA  . ARG   A 148 ? 0.1381 0.1308 0.2358 -0.0099 0.0225  0.0462  148 ARG   A CA  
3533 C C   . ARG   A 148 ? 0.1492 0.1247 0.2295 -0.0094 0.0253  0.0494  148 ARG   A C   
3534 O O   . ARG   A 148 ? 0.1812 0.1408 0.2327 -0.0167 0.0321  0.0448  148 ARG   A O   
3535 C CB  . ARG   A 148 ? 0.1420 0.1354 0.2501 -0.0055 0.0262  0.0393  148 ARG   A CB  
3536 C CG  . ARG   A 148 ? 0.1546 0.1369 0.2734 -0.0085 0.0499  0.0287  148 ARG   A CG  
3537 C CD  . ARG   A 148 ? 0.1717 0.1380 0.2874 -0.0049 0.0537  0.0479  148 ARG   A CD  
3538 N NE  . ARG   A 148 ? 0.1688 0.1406 0.2840 0.0092  0.0508  0.0535  148 ARG   A NE  
3539 C CZ  . ARG   A 148 ? 0.1615 0.1290 0.2618 0.0092  0.0493  0.0453  148 ARG   A CZ  
3540 N NH1 . ARG   A 148 ? 0.1717 0.1314 0.2609 -0.0055 0.0459  0.0191  148 ARG   A NH1 
3541 N NH2 . ARG   A 148 ? 0.1505 0.1507 0.2728 0.0139  0.0470  0.0427  148 ARG   A NH2 
3555 N N   . THR   A 149 ? 0.1445 0.1382 0.2124 -0.0112 0.0144  0.0498  149 THR   A N   
3556 C CA  . THR   A 149 ? 0.1411 0.1460 0.2139 -0.0084 0.0146  0.0452  149 THR   A CA  
3557 C C   . THR   A 149 ? 0.1364 0.1455 0.1987 -0.0173 0.0165  0.0472  149 THR   A C   
3558 O O   . THR   A 149 ? 0.1360 0.1540 0.2203 -0.0185 0.0157  0.0437  149 THR   A O   
3559 C CB  . THR   A 149 ? 0.1435 0.1554 0.2127 -0.0128 0.0139  0.0403  149 THR   A CB  
3560 O OG1 . THR   A 149 ? 0.1460 0.1441 0.2265 -0.0187 0.0097  0.0388  149 THR   A OG1 
3561 C CG2 . THR   A 149 ? 0.1362 0.1723 0.2184 -0.0061 0.0130  0.0424  149 THR   A CG2 
3569 N N   . ASN   A 150 ? 0.1428 0.1486 0.2128 -0.0059 0.0135  0.0555  150 ASN   A N   
3570 C CA  . ASN   A 150 ? 0.1495 0.1580 0.2067 -0.0097 0.0221  0.0507  150 ASN   A CA  
3571 C C   . ASN   A 150 ? 0.1321 0.1469 0.2138 -0.0159 0.0143  0.0473  150 ASN   A C   
3572 O O   . ASN   A 150 ? 0.1445 0.1509 0.2451 -0.0111 0.0004  0.0509  150 ASN   A O   
3573 C CB  . ASN   A 150 ? 0.1859 0.1786 0.2300 -0.0137 0.0283  0.0702  150 ASN   A CB  
3574 C CG  . ASN   A 150 ? 0.2437 0.2122 0.2855 -0.0114 0.0141  0.0708  150 ASN   A CG  
3575 O OD1 . ASN   A 150 ? 0.2697 0.2243 0.3000 -0.0219 0.0210  0.0887  150 ASN   A OD1 
3576 N ND2 . ASN   A 150 ? 0.2758 0.2347 0.3168 -0.0080 0.0002  0.0675  150 ASN   A ND2 
3583 N N   . VAL   A 151 ? 0.1327 0.1330 0.2079 -0.0170 0.0093  0.0403  151 VAL   A N   
3584 C CA  . VAL   A 151 ? 0.1345 0.1382 0.1981 -0.0140 0.0116  0.0392  151 VAL   A CA  
3585 C C   . VAL   A 151 ? 0.1294 0.1377 0.2110 -0.0179 0.0242  0.0445  151 VAL   A C   
3586 O O   . VAL   A 151 ? 0.1317 0.1450 0.2465 -0.0145 0.0258  0.0389  151 VAL   A O   
3587 C CB  . VAL   A 151 ? 0.1520 0.1532 0.1999 -0.0032 0.0100  0.0401  151 VAL   A CB  
3588 C CG1 . VAL   A 151 ? 0.1562 0.1745 0.2235 -0.0150 0.0183  0.0391  151 VAL   A CG1 
3589 C CG2 . VAL   A 151 ? 0.1608 0.1582 0.2074 -0.0055 0.0260  0.0357  151 VAL   A CG2 
3599 N N   A TYR   A 152 ? 0.1319 0.1422 0.2039 -0.0154 0.0209  0.0410  152 TYR   A N   
3600 N N   B TYR   A 152 ? 0.1259 0.1341 0.2049 -0.0128 0.0226  0.0494  152 TYR   A N   
3601 C CA  A TYR   A 152 ? 0.1368 0.1481 0.1927 -0.0142 0.0209  0.0370  152 TYR   A CA  
3602 C CA  B TYR   A 152 ? 0.1274 0.1410 0.1960 -0.0107 0.0268  0.0416  152 TYR   A CA  
3603 C C   A TYR   A 152 ? 0.1325 0.1406 0.1904 -0.0169 0.0248  0.0413  152 TYR   A C   
3604 C C   B TYR   A 152 ? 0.1223 0.1304 0.1773 -0.0153 0.0336  0.0448  152 TYR   A C   
3605 O O   A TYR   A 152 ? 0.1433 0.1461 0.2041 -0.0148 0.0217  0.0348  152 TYR   A O   
3606 O O   B TYR   A 152 ? 0.1288 0.1287 0.1722 -0.0145 0.0395  0.0292  152 TYR   A O   
3607 C CB  A TYR   A 152 ? 0.1478 0.1585 0.1892 -0.0108 0.0241  0.0380  152 TYR   A CB  
3608 C CB  B TYR   A 152 ? 0.1396 0.1550 0.2066 -0.0048 0.0362  0.0465  152 TYR   A CB  
3609 C CG  A TYR   A 152 ? 0.1602 0.1680 0.1801 -0.0136 0.0257  0.0410  152 TYR   A CG  
3610 C CG  B TYR   A 152 ? 0.1538 0.1723 0.2000 -0.0072 0.0393  0.0513  152 TYR   A CG  
3611 C CD1 A TYR   A 152 ? 0.1736 0.1827 0.1859 -0.0072 0.0272  0.0429  152 TYR   A CD1 
3612 C CD1 B TYR   A 152 ? 0.1710 0.1957 0.2172 0.0003  0.0436  0.0522  152 TYR   A CD1 
3613 C CD2 A TYR   A 152 ? 0.1645 0.1703 0.1746 -0.0200 0.0293  0.0409  152 TYR   A CD2 
3614 C CD2 B TYR   A 152 ? 0.1581 0.1832 0.1928 -0.0113 0.0398  0.0496  152 TYR   A CD2 
3615 C CE1 A TYR   A 152 ? 0.1878 0.1882 0.1875 -0.0056 0.0300  0.0520  152 TYR   A CE1 
3616 C CE1 B TYR   A 152 ? 0.1993 0.2119 0.2263 0.0027  0.0322  0.0622  152 TYR   A CE1 
3617 C CE2 A TYR   A 152 ? 0.1774 0.1768 0.1747 -0.0217 0.0392  0.0475  152 TYR   A CE2 
3618 C CE2 B TYR   A 152 ? 0.1882 0.2045 0.2085 -0.0104 0.0359  0.0558  152 TYR   A CE2 
3619 C CZ  A TYR   A 152 ? 0.1917 0.1833 0.1833 -0.0094 0.0344  0.0595  152 TYR   A CZ  
3620 C CZ  B TYR   A 152 ? 0.2131 0.2155 0.2218 -0.0043 0.0305  0.0739  152 TYR   A CZ  
3621 O OH  A TYR   A 152 ? 0.2049 0.1938 0.2007 0.0062  0.0406  0.0701  152 TYR   A OH  
3622 O OH  B TYR   A 152 ? 0.2436 0.2424 0.2515 -0.0013 0.0327  0.0863  152 TYR   A OH  
3641 N N   . LEU   A 153 ? 0.1285 0.1328 0.2000 -0.0174 0.0282  0.0488  153 LEU   A N   
3642 C CA  . LEU   A 153 ? 0.1220 0.1316 0.2159 -0.0089 0.0280  0.0430  153 LEU   A CA  
3643 C C   . LEU   A 153 ? 0.1291 0.1333 0.2255 -0.0069 0.0335  0.0481  153 LEU   A C   
3644 O O   . LEU   A 153 ? 0.1332 0.1459 0.2465 -0.0079 0.0497  0.0449  153 LEU   A O   
3645 C CB  . LEU   A 153 ? 0.1204 0.1381 0.2289 -0.0066 0.0230  0.0369  153 LEU   A CB  
3646 C CG  . LEU   A 153 ? 0.1314 0.1385 0.2131 -0.0129 0.0128  0.0339  153 LEU   A CG  
3647 C CD1 . LEU   A 153 ? 0.1407 0.1537 0.2137 -0.0117 -0.0006 0.0329  153 LEU   A CD1 
3648 C CD2 . LEU   A 153 ? 0.1347 0.1556 0.2288 -0.0192 0.0299  0.0141  153 LEU   A CD2 
3661 N N   . ALA   A 154 ? 0.1284 0.1331 0.2248 -0.0041 0.0376  0.0457  154 ALA   A N   
3662 C CA  . ALA   A 154 ? 0.1449 0.1363 0.2265 0.0008  0.0439  0.0522  154 ALA   A CA  
3663 C C   . ALA   A 154 ? 0.1480 0.1384 0.2287 0.0049  0.0441  0.0613  154 ALA   A C   
3664 O O   . ALA   A 154 ? 0.1564 0.1475 0.2439 0.0054  0.0479  0.0618  154 ALA   A O   
3665 C CB  . ALA   A 154 ? 0.1470 0.1493 0.2306 0.0006  0.0375  0.0381  154 ALA   A CB  
3671 N N   A VAL   A 155 ? 0.1627 0.1586 0.2229 0.0188  0.0299  0.0554  155 VAL   A N   
3672 N N   B VAL   A 155 ? 0.1408 0.1483 0.2370 0.0096  0.0397  0.0649  155 VAL   A N   
3673 C CA  A VAL   A 155 ? 0.1785 0.1703 0.2177 0.0262  0.0149  0.0457  155 VAL   A CA  
3674 C CA  B VAL   A 155 ? 0.1396 0.1422 0.2429 -0.0000 0.0317  0.0631  155 VAL   A CA  
3675 C C   A VAL   A 155 ? 0.1814 0.1728 0.2039 0.0387  0.0053  0.0374  155 VAL   A C   
3676 C C   B VAL   A 155 ? 0.1306 0.1353 0.2378 -0.0128 0.0306  0.0484  155 VAL   A C   
3677 O O   A VAL   A 155 ? 0.1812 0.1793 0.1990 0.0445  0.0020  0.0326  155 VAL   A O   
3678 O O   B VAL   A 155 ? 0.1260 0.1366 0.2425 -0.0072 0.0461  0.0439  155 VAL   A O   
3679 C CB  A VAL   A 155 ? 0.1840 0.1742 0.2244 0.0233  0.0017  0.0361  155 VAL   A CB  
3680 C CB  B VAL   A 155 ? 0.1483 0.1266 0.2638 -0.0067 0.0031  0.0545  155 VAL   A CB  
3681 C CG1 A VAL   A 155 ? 0.1972 0.1794 0.2342 0.0162  -0.0031 0.0314  155 VAL   A CG1 
3682 C CG1 B VAL   A 155 ? 0.1546 0.1185 0.2807 -0.0126 -0.0107 0.0455  155 VAL   A CG1 
3683 C CG2 A VAL   A 155 ? 0.1821 0.1779 0.2234 0.0274  -0.0090 0.0376  155 VAL   A CG2 
3684 C CG2 B VAL   A 155 ? 0.1643 0.1355 0.2727 0.0096  -0.0135 0.0340  155 VAL   A CG2 
3703 N N   A PHE   A 156 ? 0.1825 0.1686 0.2117 0.0499  0.0036  0.0352  156 PHE   A N   
3704 N N   B PHE   A 156 ? 0.1300 0.1271 0.2450 -0.0138 0.0304  0.0352  156 PHE   A N   
3705 C CA  A PHE   A 156 ? 0.1943 0.1744 0.2153 0.0585  -0.0024 0.0292  156 PHE   A CA  
3706 C CA  B PHE   A 156 ? 0.1342 0.1377 0.2329 -0.0088 0.0132  0.0400  156 PHE   A CA  
3707 C C   A PHE   A 156 ? 0.1847 0.1684 0.2028 0.0654  0.0027  0.0389  156 PHE   A C   
3708 C C   B PHE   A 156 ? 0.1336 0.1489 0.2340 -0.0056 0.0190  0.0433  156 PHE   A C   
3709 O O   A PHE   A 156 ? 0.1816 0.1738 0.2052 0.0572  0.0139  0.0254  156 PHE   A O   
3710 O O   B PHE   A 156 ? 0.1448 0.1708 0.2541 -0.0100 0.0190  0.0299  156 PHE   A O   
3711 C CB  A PHE   A 156 ? 0.2201 0.1898 0.2270 0.0542  -0.0127 0.0171  156 PHE   A CB  
3712 C CB  B PHE   A 156 ? 0.1381 0.1320 0.2117 -0.0096 0.0061  0.0497  156 PHE   A CB  
3713 C CG  A PHE   A 156 ? 0.2459 0.2072 0.2515 0.0536  -0.0216 0.0001  156 PHE   A CG  
3714 C CG  B PHE   A 156 ? 0.1438 0.1352 0.2090 -0.0113 0.0016  0.0556  156 PHE   A CG  
3715 C CD1 A PHE   A 156 ? 0.2597 0.2160 0.2675 0.0558  -0.0251 0.0006  156 PHE   A CD1 
3716 C CD1 B PHE   A 156 ? 0.1575 0.1477 0.2332 0.0071  -0.0003 0.0509  156 PHE   A CD1 
3717 C CD2 A PHE   A 156 ? 0.2606 0.2157 0.2586 0.0504  -0.0281 -0.0100 156 PHE   A CD2 
3718 C CD2 B PHE   A 156 ? 0.1676 0.1368 0.2257 -0.0109 -0.0008 0.0436  156 PHE   A CD2 
3719 C CE1 A PHE   A 156 ? 0.2686 0.2201 0.2746 0.0555  -0.0249 -0.0034 156 PHE   A CE1 
3720 C CE1 B PHE   A 156 ? 0.1669 0.1523 0.2502 0.0074  0.0040  0.0445  156 PHE   A CE1 
3721 C CE2 A PHE   A 156 ? 0.2695 0.2205 0.2676 0.0502  -0.0304 -0.0149 156 PHE   A CE2 
3722 C CE2 B PHE   A 156 ? 0.1767 0.1413 0.2348 -0.0073 -0.0023 0.0388  156 PHE   A CE2 
3723 C CZ  A PHE   A 156 ? 0.2728 0.2238 0.2745 0.0528  -0.0244 -0.0117 156 PHE   A CZ  
3724 C CZ  B PHE   A 156 ? 0.1718 0.1447 0.2537 -0.0039 0.0128  0.0455  156 PHE   A CZ  
3743 N N   A ASP   A 157 ? 0.1876 0.1770 0.1995 0.0591  0.0002  0.0487  157 ASP   A N   
3744 N N   B ASP   A 157 ? 0.1458 0.1603 0.2460 -0.0144 0.0025  0.0521  157 ASP   A N   
3745 C CA  A ASP   A 157 ? 0.1989 0.1917 0.2057 0.0495  -0.0101 0.0463  157 ASP   A CA  
3746 C CA  B ASP   A 157 ? 0.1578 0.1763 0.2662 -0.0162 -0.0130 0.0431  157 ASP   A CA  
3747 C C   A ASP   A 157 ? 0.1893 0.2043 0.1948 0.0471  -0.0091 0.0448  157 ASP   A C   
3748 C C   B ASP   A 157 ? 0.1463 0.1756 0.2518 -0.0118 -0.0093 0.0431  157 ASP   A C   
3749 O O   A ASP   A 157 ? 0.1924 0.2035 0.1857 0.0457  -0.0096 0.0485  157 ASP   A O   
3750 O O   B ASP   A 157 ? 0.1385 0.1668 0.2404 -0.0114 -0.0087 0.0490  157 ASP   A O   
3751 C CB  A ASP   A 157 ? 0.2219 0.1909 0.2248 0.0477  -0.0211 0.0491  157 ASP   A CB  
3752 C CB  B ASP   A 157 ? 0.1793 0.1853 0.3030 -0.0231 -0.0361 0.0402  157 ASP   A CB  
3753 C CG  A ASP   A 157 ? 0.2433 0.1944 0.2394 0.0522  -0.0352 0.0521  157 ASP   A CG  
3754 C CG  B ASP   A 157 ? 0.2077 0.1890 0.3512 -0.0253 -0.0612 0.0272  157 ASP   A CG  
3755 O OD1 A ASP   A 157 ? 0.2627 0.2049 0.2729 0.0462  -0.0469 0.0402  157 ASP   A OD1 
3756 O OD1 B ASP   A 157 ? 0.2501 0.1988 0.3858 -0.0148 -0.0892 0.0231  157 ASP   A OD1 
3757 O OD2 A ASP   A 157 ? 0.2479 0.1838 0.2327 0.0560  -0.0323 0.0514  157 ASP   A OD2 
3758 O OD2 B ASP   A 157 ? 0.2024 0.1957 0.3761 -0.0299 -0.0593 0.0179  157 ASP   A OD2 
3767 N N   A LYS   A 158 ? 0.1803 0.2173 0.2039 0.0486  -0.0123 0.0354  158 LYS   A N   
3768 N N   B LYS   A 158 ? 0.1447 0.1828 0.2674 -0.0110 0.0016  0.0282  158 LYS   A N   
3769 C CA  A LYS   A 158 ? 0.1776 0.2294 0.2188 0.0517  -0.0103 0.0214  158 LYS   A CA  
3770 C CA  B LYS   A 158 ? 0.1544 0.2026 0.2802 -0.0104 0.0023  0.0220  158 LYS   A CA  
3771 C C   A LYS   A 158 ? 0.1863 0.2336 0.2163 0.0611  -0.0200 0.0162  158 LYS   A C   
3772 C C   B LYS   A 158 ? 0.1461 0.1941 0.2752 -0.0121 -0.0079 0.0200  158 LYS   A C   
3773 O O   A LYS   A 158 ? 0.1838 0.2366 0.2139 0.0584  -0.0106 0.0054  158 LYS   A O   
3774 O O   B LYS   A 158 ? 0.1453 0.1951 0.2730 -0.0230 -0.0102 0.0308  158 LYS   A O   
3775 C CB  A LYS   A 158 ? 0.1727 0.2379 0.2293 0.0435  0.0084  0.0206  158 LYS   A CB  
3776 C CB  B LYS   A 158 ? 0.1809 0.2421 0.3126 -0.0083 0.0047  0.0142  158 LYS   A CB  
3777 C CG  A LYS   A 158 ? 0.1714 0.2473 0.2464 0.0333  0.0238  0.0195  158 LYS   A CG  
3778 C CG  B LYS   A 158 ? 0.2116 0.2735 0.3540 0.0012  0.0008  0.0004  158 LYS   A CG  
3779 C CD  A LYS   A 158 ? 0.1705 0.2521 0.2617 0.0250  0.0405  0.0296  158 LYS   A CD  
3780 C CD  B LYS   A 158 ? 0.2457 0.3021 0.4019 0.0083  -0.0033 -0.0133 158 LYS   A CD  
3781 C CE  A LYS   A 158 ? 0.1680 0.2521 0.2671 0.0141  0.0507  0.0416  158 LYS   A CE  
3782 C CE  B LYS   A 158 ? 0.2780 0.3258 0.4421 0.0135  -0.0173 -0.0217 158 LYS   A CE  
3783 N NZ  A LYS   A 158 ? 0.1654 0.2483 0.2681 0.0066  0.0615  0.0508  158 LYS   A NZ  
3784 N NZ  B LYS   A 158 ? 0.2864 0.3323 0.4641 0.0188  -0.0251 -0.0283 158 LYS   A NZ  
3811 N N   A ASN   A 159 ? 0.2005 0.2335 0.2367 0.0677  -0.0302 0.0216  159 ASN   A N   
3812 N N   B ASN   A 159 ? 0.1595 0.1957 0.2819 -0.0035 -0.0204 0.0203  159 ASN   A N   
3813 C CA  A ASN   A 159 ? 0.2178 0.2355 0.2526 0.0721  -0.0280 0.0234  159 ASN   A CA  
3814 C CA  B ASN   A 159 ? 0.1768 0.2091 0.2988 0.0075  -0.0336 0.0331  159 ASN   A CA  
3815 C C   A ASN   A 159 ? 0.2289 0.2274 0.2306 0.0676  -0.0159 0.0229  159 ASN   A C   
3816 C C   B ASN   A 159 ? 0.1647 0.1957 0.2906 -0.0155 -0.0328 0.0244  159 ASN   A C   
3817 O O   A ASN   A 159 ? 0.2371 0.2311 0.2287 0.0626  -0.0141 0.0195  159 ASN   A O   
3818 O O   B ASN   A 159 ? 0.1643 0.2031 0.3130 -0.0089 -0.0398 0.0075  159 ASN   A O   
3819 C CB  A ASN   A 159 ? 0.2252 0.2437 0.2899 0.0790  -0.0337 0.0280  159 ASN   A CB  
3820 C CB  B ASN   A 159 ? 0.2179 0.2395 0.3444 0.0323  -0.0188 0.0465  159 ASN   A CB  
3821 C CG  A ASN   A 159 ? 0.2371 0.2563 0.3223 0.0709  -0.0318 0.0257  159 ASN   A CG  
3822 C CG  B ASN   A 159 ? 0.2547 0.2706 0.4041 0.0349  0.0130  0.0445  159 ASN   A CG  
3823 O OD1 A ASN   A 159 ? 0.2481 0.2673 0.3366 0.0572  -0.0270 0.0275  159 ASN   A OD1 
3824 O OD1 B ASN   A 159 ? 0.2608 0.2826 0.4304 0.0300  0.0268  0.0409  159 ASN   A OD1 
3825 N ND2 A ASN   A 159 ? 0.2400 0.2603 0.3417 0.0723  -0.0277 0.0175  159 ASN   A ND2 
3826 N ND2 B ASN   A 159 ? 0.2678 0.2847 0.4276 0.0286  0.0256  0.0331  159 ASN   A ND2 
3839 N N   A LEU   A 160 ? 0.2331 0.2140 0.2148 0.0670  -0.0120 0.0272  160 LEU   A N   
3840 N N   B LEU   A 160 ? 0.1629 0.1822 0.2789 -0.0212 -0.0354 0.0365  160 LEU   A N   
3841 C CA  A LEU   A 160 ? 0.2359 0.2080 0.2162 0.0595  -0.0004 0.0282  160 LEU   A CA  
3842 C CA  B LEU   A 160 ? 0.1602 0.1710 0.2669 -0.0198 -0.0280 0.0375  160 LEU   A CA  
3843 C C   A LEU   A 160 ? 0.2245 0.2066 0.1999 0.0555  0.0013  0.0334  160 LEU   A C   
3844 C C   B LEU   A 160 ? 0.1487 0.1663 0.2680 -0.0170 -0.0137 0.0257  160 LEU   A C   
3845 O O   A LEU   A 160 ? 0.2251 0.2051 0.2042 0.0561  -0.0026 0.0266  160 LEU   A O   
3846 O O   B LEU   A 160 ? 0.1612 0.1602 0.2863 -0.0257 -0.0146 0.0102  160 LEU   A O   
3847 C CB  A LEU   A 160 ? 0.2482 0.2097 0.2353 0.0536  0.0163  0.0130  160 LEU   A CB  
3848 C CB  B LEU   A 160 ? 0.1785 0.1685 0.2680 -0.0259 -0.0380 0.0473  160 LEU   A CB  
3849 C CG  A LEU   A 160 ? 0.2571 0.2112 0.2539 0.0443  0.0291  0.0024  160 LEU   A CG  
3850 C CG  B LEU   A 160 ? 0.1868 0.1760 0.2786 -0.0325 -0.0373 0.0399  160 LEU   A CG  
3851 C CD1 A LEU   A 160 ? 0.2598 0.2085 0.2570 0.0410  0.0348  -0.0022 160 LEU   A CD1 
3852 C CD1 B LEU   A 160 ? 0.1934 0.1880 0.3019 -0.0322 -0.0288 0.0369  160 LEU   A CD1 
3853 C CD2 A LEU   A 160 ? 0.2583 0.2107 0.2600 0.0438  0.0325  -0.0033 160 LEU   A CD2 
3854 C CD2 B LEU   A 160 ? 0.1911 0.1775 0.2779 -0.0366 -0.0439 0.0352  160 LEU   A CD2 
3877 N N   A TYR   A 161 ? 0.2125 0.2115 0.1957 0.0498  0.0008  0.0395  161 TYR   A N   
3878 N N   B TYR   A 161 ? 0.1427 0.1692 0.2640 -0.0128 -0.0005 0.0350  161 TYR   A N   
3879 C CA  A TYR   A 161 ? 0.1945 0.2186 0.1994 0.0447  -0.0013 0.0476  161 TYR   A CA  
3880 C CA  B TYR   A 161 ? 0.1409 0.1719 0.2638 -0.0168 0.0087  0.0501  161 TYR   A CA  
3881 C C   A TYR   A 161 ? 0.1881 0.2338 0.2024 0.0473  -0.0035 0.0399  161 TYR   A C   
3882 C C   B TYR   A 161 ? 0.1382 0.1809 0.2816 -0.0173 0.0130  0.0340  161 TYR   A C   
3883 O O   A TYR   A 161 ? 0.1825 0.2337 0.1918 0.0498  -0.0080 0.0335  161 TYR   A O   
3884 O O   B TYR   A 161 ? 0.1423 0.1780 0.2807 -0.0144 0.0103  0.0371  161 TYR   A O   
3885 C CB  A TYR   A 161 ? 0.1887 0.2117 0.2190 0.0339  -0.0033 0.0560  161 TYR   A CB  
3886 C CB  B TYR   A 161 ? 0.1450 0.1793 0.2661 -0.0118 0.0173  0.0582  161 TYR   A CB  
3887 C CG  A TYR   A 161 ? 0.1810 0.2079 0.2397 0.0226  -0.0141 0.0651  161 TYR   A CG  
3888 C CG  B TYR   A 161 ? 0.1543 0.1905 0.2939 -0.0204 -0.0025 0.0697  161 TYR   A CG  
3889 C CD1 A TYR   A 161 ? 0.1771 0.2038 0.2560 0.0177  -0.0221 0.0635  161 TYR   A CD1 
3890 C CD1 B TYR   A 161 ? 0.1526 0.1993 0.3243 -0.0198 -0.0154 0.0600  161 TYR   A CD1 
3891 C CD2 A TYR   A 161 ? 0.1836 0.2159 0.2486 0.0128  -0.0226 0.0724  161 TYR   A CD2 
3892 C CD2 B TYR   A 161 ? 0.1667 0.2136 0.3078 -0.0232 -0.0163 0.0869  161 TYR   A CD2 
3893 C CE1 A TYR   A 161 ? 0.1880 0.2103 0.2717 0.0086  -0.0296 0.0730  161 TYR   A CE1 
3894 C CE1 B TYR   A 161 ? 0.1699 0.2044 0.3325 -0.0232 -0.0373 0.0800  161 TYR   A CE1 
3895 C CE2 A TYR   A 161 ? 0.1907 0.2178 0.2603 0.0069  -0.0337 0.0817  161 TYR   A CE2 
3896 C CE2 B TYR   A 161 ? 0.1818 0.2216 0.3220 -0.0264 -0.0310 0.0999  161 TYR   A CE2 
3897 C CZ  A TYR   A 161 ? 0.1977 0.2146 0.2726 0.0049  -0.0455 0.0894  161 TYR   A CZ  
3898 C CZ  B TYR   A 161 ? 0.1954 0.2164 0.3382 -0.0313 -0.0423 0.1078  161 TYR   A CZ  
3899 O OH  A TYR   A 161 ? 0.2080 0.2182 0.2814 0.0070  -0.0690 0.1065  161 TYR   A OH  
3900 O OH  B TYR   A 161 ? 0.2239 0.2309 0.3662 -0.0320 -0.0507 0.1204  161 TYR   A OH  
3919 N N   A ASP   A 162 ? 0.1909 0.2507 0.2235 0.0496  -0.0014 0.0387  162 ASP   A N   
3920 N N   B ASP   A 162 ? 0.1313 0.1914 0.2955 -0.0171 0.0093  0.0318  162 ASP   A N   
3921 C CA  A ASP   A 162 ? 0.1940 0.2703 0.2348 0.0452  -0.0013 0.0367  162 ASP   A CA  
3922 C CA  B ASP   A 162 ? 0.1363 0.2174 0.3113 -0.0184 0.0012  0.0384  162 ASP   A CA  
3923 C C   A ASP   A 162 ? 0.2075 0.2810 0.2456 0.0502  -0.0021 0.0257  162 ASP   A C   
3924 C C   B ASP   A 162 ? 0.1389 0.2226 0.3144 -0.0256 -0.0135 0.0312  162 ASP   A C   
3925 O O   A ASP   A 162 ? 0.2087 0.2812 0.2571 0.0533  0.0053  0.0181  162 ASP   A O   
3926 O O   B ASP   A 162 ? 0.1418 0.2157 0.3403 -0.0316 0.0027  0.0224  162 ASP   A O   
3927 C CB  A ASP   A 162 ? 0.1869 0.2831 0.2346 0.0364  0.0052  0.0425  162 ASP   A CB  
3928 C CB  B ASP   A 162 ? 0.1549 0.2542 0.3481 -0.0107 0.0016  0.0385  162 ASP   A CB  
3929 C CG  A ASP   A 162 ? 0.1831 0.2971 0.2352 0.0298  0.0170  0.0575  162 ASP   A CG  
3930 C CG  B ASP   A 162 ? 0.1780 0.2830 0.3761 0.0113  -0.0018 0.0442  162 ASP   A CG  
3931 O OD1 A ASP   A 162 ? 0.1858 0.3076 0.2438 0.0261  0.0127  0.0565  162 ASP   A OD1 
3932 O OD1 B ASP   A 162 ? 0.1875 0.2959 0.3787 0.0245  -0.0044 0.0568  162 ASP   A OD1 
3933 O OD2 A ASP   A 162 ? 0.1809 0.2992 0.2348 0.0283  0.0360  0.0667  162 ASP   A OD2 
3934 O OD2 B ASP   A 162 ? 0.1945 0.2935 0.3982 0.0210  0.0010  0.0376  162 ASP   A OD2 
3943 N N   A LYS   A 163 ? 0.2259 0.2879 0.2584 0.0495  -0.0142 0.0254  163 LYS   A N   
3944 N N   B LYS   A 163 ? 0.1555 0.2369 0.3047 -0.0229 -0.0348 0.0330  163 LYS   A N   
3945 C CA  A LYS   A 163 ? 0.2469 0.2980 0.2698 0.0439  -0.0204 0.0194  163 LYS   A CA  
3946 C CA  B LYS   A 163 ? 0.1807 0.2532 0.3217 -0.0237 -0.0392 0.0292  163 LYS   A CA  
3947 C C   A LYS   A 163 ? 0.2420 0.2863 0.2430 0.0391  -0.0226 0.0127  163 LYS   A C   
3948 C C   B LYS   A 163 ? 0.1662 0.2276 0.2967 -0.0335 -0.0366 0.0115  163 LYS   A C   
3949 O O   A LYS   A 163 ? 0.2464 0.2916 0.2488 0.0375  -0.0338 0.0036  163 LYS   A O   
3950 O O   B LYS   A 163 ? 0.1810 0.2373 0.3171 -0.0230 -0.0365 -0.0018 163 LYS   A O   
3951 C CB  A LYS   A 163 ? 0.2730 0.3179 0.3155 0.0413  -0.0184 0.0187  163 LYS   A CB  
3952 C CB  B LYS   A 163 ? 0.2315 0.2963 0.3792 -0.0174 -0.0351 0.0448  163 LYS   A CB  
3953 C CG  A LYS   A 163 ? 0.2945 0.3335 0.3648 0.0379  -0.0133 0.0180  163 LYS   A CG  
3954 C CG  B LYS   A 163 ? 0.2891 0.3327 0.4461 -0.0137 -0.0187 0.0610  163 LYS   A CG  
3955 C CD  A LYS   A 163 ? 0.3134 0.3448 0.4105 0.0353  -0.0111 0.0184  163 LYS   A CD  
3956 C CD  B LYS   A 163 ? 0.3348 0.3630 0.5093 -0.0146 -0.0068 0.0747  163 LYS   A CD  
3957 C CE  A LYS   A 163 ? 0.3336 0.3556 0.4490 0.0309  -0.0093 0.0199  163 LYS   A CE  
3958 C CE  B LYS   A 163 ? 0.3669 0.3859 0.5556 -0.0143 0.0011  0.0851  163 LYS   A CE  
3959 N NZ  A LYS   A 163 ? 0.3396 0.3621 0.4714 0.0269  -0.0067 0.0214  163 LYS   A NZ  
3960 N NZ  B LYS   A 163 ? 0.3895 0.3946 0.5848 -0.0129 0.0052  0.0880  163 LYS   A NZ  
3987 N N   A LEU   A 164 ? 0.2311 0.2678 0.2138 0.0317  -0.0123 0.0091  164 LEU   A N   
3988 N N   B LEU   A 164 ? 0.1537 0.2135 0.2884 -0.0309 -0.0238 0.0069  164 LEU   A N   
3989 C CA  A LEU   A 164 ? 0.2194 0.2520 0.1932 0.0239  0.0083  0.0092  164 LEU   A CA  
3990 C CA  B LEU   A 164 ? 0.1531 0.1928 0.2747 -0.0232 -0.0009 0.0146  164 LEU   A CA  
3991 C C   A LEU   A 164 ? 0.2108 0.2545 0.1873 0.0254  0.0131  0.0121  164 LEU   A C   
3992 C C   B LEU   A 164 ? 0.1508 0.1842 0.2805 -0.0280 0.0047  0.0184  164 LEU   A C   
3993 O O   A LEU   A 164 ? 0.2066 0.2497 0.1772 0.0272  0.0195  0.0070  164 LEU   A O   
3994 O O   B LEU   A 164 ? 0.1684 0.1872 0.2957 -0.0178 0.0065  0.0100  164 LEU   A O   
3995 C CB  A LEU   A 164 ? 0.2171 0.2368 0.1810 0.0145  0.0222  0.0119  164 LEU   A CB  
3996 C CB  B LEU   A 164 ? 0.1618 0.1839 0.2589 -0.0235 0.0121  0.0206  164 LEU   A CB  
3997 C CG  A LEU   A 164 ? 0.2174 0.2266 0.1822 0.0038  0.0269  0.0090  164 LEU   A CG  
3998 C CG  B LEU   A 164 ? 0.1700 0.1887 0.2597 -0.0192 0.0147  0.0171  164 LEU   A CG  
3999 C CD1 A LEU   A 164 ? 0.2150 0.2229 0.1810 0.0039  0.0276  0.0085  164 LEU   A CD1 
4000 C CD1 B LEU   A 164 ? 0.1614 0.1847 0.2529 -0.0166 0.0064  0.0179  164 LEU   A CD1 
4001 C CD2 A LEU   A 164 ? 0.2181 0.2219 0.1793 -0.0032 0.0268  0.0029  164 LEU   A CD2 
4002 C CD2 B LEU   A 164 ? 0.1913 0.2008 0.2654 -0.0110 0.0174  0.0148  164 LEU   A CD2 
4025 N N   A VAL   A 165 ? 0.2097 0.2646 0.2000 0.0242  0.0128  0.0119  165 VAL   A N   
4026 N N   B VAL   A 165 ? 0.1571 0.1840 0.2765 -0.0222 0.0117  0.0305  165 VAL   A N   
4027 C CA  A VAL   A 165 ? 0.2141 0.2772 0.2192 0.0155  0.0145  0.0069  165 VAL   A CA  
4028 C CA  B VAL   A 165 ? 0.1688 0.1968 0.2894 -0.0357 0.0257  0.0388  165 VAL   A CA  
4029 C C   A VAL   A 165 ? 0.2217 0.2947 0.2431 0.0139  0.0093  -0.0029 165 VAL   A C   
4030 C C   B VAL   A 165 ? 0.1569 0.1981 0.3131 -0.0420 0.0176  0.0202  165 VAL   A C   
4031 O O   A VAL   A 165 ? 0.2205 0.2950 0.2469 0.0182  0.0052  -0.0115 165 VAL   A O   
4032 O O   B VAL   A 165 ? 0.1623 0.1967 0.3273 -0.0422 0.0236  0.0227  165 VAL   A O   
4033 C CB  A VAL   A 165 ? 0.2143 0.2746 0.2215 0.0117  0.0168  0.0099  165 VAL   A CB  
4034 C CB  B VAL   A 165 ? 0.1983 0.2157 0.2911 -0.0327 0.0269  0.0450  165 VAL   A CB  
4035 C CG1 A VAL   A 165 ? 0.2150 0.2740 0.2240 0.0070  0.0212  0.0119  165 VAL   A CG1 
4036 C CG1 B VAL   A 165 ? 0.2070 0.2242 0.2980 -0.0343 0.0260  0.0423  165 VAL   A CG1 
4037 C CG2 A VAL   A 165 ? 0.2173 0.2759 0.2214 0.0143  0.0107  0.0127  165 VAL   A CG2 
4038 C CG2 B VAL   A 165 ? 0.2128 0.2238 0.2882 -0.0252 0.0229  0.0505  165 VAL   A CG2 
4057 N N   A SER   A 166 ? 0.2334 0.3122 0.2724 0.0118  0.0123  -0.0059 166 SER   A N   
4058 N N   B SER   A 166 ? 0.1562 0.2119 0.3274 -0.0383 0.0082  0.0074  166 SER   A N   
4059 C CA  A SER   A 166 ? 0.2509 0.3323 0.3041 0.0056  0.0156  -0.0100 166 SER   A CA  
4060 C CA  B SER   A 166 ? 0.1746 0.2504 0.3609 -0.0406 -0.0054 -0.0077 166 SER   A CA  
4061 C C   A SER   A 166 ? 0.2662 0.3475 0.3046 -0.0030 0.0066  -0.0106 166 SER   A C   
4062 C C   B SER   A 166 ? 0.1835 0.2857 0.3621 -0.0497 -0.0068 -0.0127 166 SER   A C   
4063 O O   A SER   A 166 ? 0.2678 0.3509 0.3067 -0.0071 0.0035  -0.0194 166 SER   A O   
4064 O O   B SER   A 166 ? 0.1878 0.2979 0.3820 -0.0594 -0.0111 -0.0250 166 SER   A O   
4065 C CB  A SER   A 166 ? 0.2578 0.3390 0.3350 0.0120  0.0265  -0.0169 166 SER   A CB  
4066 C CB  B SER   A 166 ? 0.1993 0.2706 0.4012 -0.0251 -0.0144 -0.0149 166 SER   A CB  
4067 O OG  A SER   A 166 ? 0.2670 0.3457 0.3586 0.0146  0.0352  -0.0171 166 SER   A OG  
4068 O OG  B SER   A 166 ? 0.2371 0.2945 0.4524 -0.0123 -0.0099 -0.0167 166 SER   A OG  
4079 N N   A SER   A 167 ? 0.2838 0.3602 0.3095 -0.0041 -0.0025 -0.0046 167 SER   A N   
4080 N N   B SER   A 167 ? 0.1995 0.3118 0.3498 -0.0348 -0.0160 -0.0141 167 SER   A N   
4081 C CA  A SER   A 167 ? 0.3065 0.3714 0.3205 -0.0044 -0.0108 -0.0009 167 SER   A CA  
4082 C CA  B SER   A 167 ? 0.2389 0.3380 0.3617 -0.0215 -0.0275 -0.0101 167 SER   A CA  
4083 C C   A SER   A 167 ? 0.3275 0.3856 0.3365 -0.0050 -0.0129 0.0038  167 SER   A C   
4084 C C   B SER   A 167 ? 0.2687 0.3580 0.3818 -0.0142 -0.0392 -0.0103 167 SER   A C   
4085 O O   A SER   A 167 ? 0.3270 0.3829 0.3353 -0.0039 -0.0159 0.0008  167 SER   A O   
4086 O O   B SER   A 167 ? 0.2716 0.3623 0.3797 -0.0090 -0.0520 -0.0203 167 SER   A O   
4087 C CB  A SER   A 167 ? 0.3075 0.3687 0.3228 -0.0032 -0.0111 -0.0018 167 SER   A CB  
4088 C CB  B SER   A 167 ? 0.2502 0.3443 0.3572 -0.0136 -0.0191 -0.0093 167 SER   A CB  
4089 O OG  A SER   A 167 ? 0.3090 0.3681 0.3261 -0.0017 -0.0106 -0.0012 167 SER   A OG  
4090 O OG  B SER   A 167 ? 0.2573 0.3473 0.3546 -0.0086 -0.0131 -0.0112 167 SER   A OG  
4101 N N   A PHE   A 168 ? 0.3491 0.4029 0.3608 -0.0048 -0.0134 0.0162  168 PHE   A N   
4102 N N   B PHE   A 168 ? 0.2956 0.3739 0.4071 -0.0125 -0.0369 0.0059  168 PHE   A N   
4103 C CA  A PHE   A 168 ? 0.3743 0.4218 0.3943 -0.0071 -0.0149 0.0251  168 PHE   A CA  
4104 C CA  B PHE   A 168 ? 0.3249 0.3925 0.4393 -0.0155 -0.0323 0.0164  168 PHE   A CA  
4105 C C   A PHE   A 168 ? 0.4202 0.4597 0.4636 -0.0108 -0.0166 0.0171  168 PHE   A C   
4106 C C   B PHE   A 168 ? 0.4006 0.4460 0.5199 -0.0207 -0.0210 0.0021  168 PHE   A C   
4107 O O   A PHE   A 168 ? 0.4227 0.4617 0.4728 -0.0117 -0.0167 0.0207  168 PHE   A O   
4108 O O   B PHE   A 168 ? 0.4063 0.4480 0.5294 -0.0202 -0.0169 0.0007  168 PHE   A O   
4109 C CB  A PHE   A 168 ? 0.3543 0.4037 0.3620 -0.0057 -0.0160 0.0404  168 PHE   A CB  
4110 C CB  B PHE   A 168 ? 0.2811 0.3619 0.3936 -0.0189 -0.0428 0.0407  168 PHE   A CB  
4111 C CG  A PHE   A 168 ? 0.3374 0.3881 0.3340 -0.0059 -0.0153 0.0518  168 PHE   A CG  
4112 C CG  B PHE   A 168 ? 0.2390 0.3338 0.3499 -0.0274 -0.0502 0.0598  168 PHE   A CG  
4113 C CD1 A PHE   A 168 ? 0.3318 0.3821 0.3233 -0.0068 -0.0153 0.0580  168 PHE   A CD1 
4114 C CD1 B PHE   A 168 ? 0.2238 0.3245 0.3360 -0.0353 -0.0575 0.0702  168 PHE   A CD1 
4115 C CD2 A PHE   A 168 ? 0.3293 0.3808 0.3220 -0.0068 -0.0110 0.0557  168 PHE   A CD2 
4116 C CD2 B PHE   A 168 ? 0.2155 0.3179 0.3306 -0.0346 -0.0383 0.0672  168 PHE   A CD2 
4117 C CE1 A PHE   A 168 ? 0.3265 0.3780 0.3164 -0.0076 -0.0149 0.0610  168 PHE   A CE1 
4118 C CE1 B PHE   A 168 ? 0.2026 0.3182 0.3223 -0.0453 -0.0628 0.0697  168 PHE   A CE1 
4119 C CE2 A PHE   A 168 ? 0.3257 0.3769 0.3160 -0.0083 -0.0105 0.0590  168 PHE   A CE2 
4120 C CE2 B PHE   A 168 ? 0.1998 0.3090 0.3221 -0.0440 -0.0376 0.0707  168 PHE   A CE2 
4121 C CZ  A PHE   A 168 ? 0.3252 0.3763 0.3155 -0.0082 -0.0127 0.0607  168 PHE   A CZ  
4122 C CZ  B PHE   A 168 ? 0.1990 0.3123 0.3206 -0.0475 -0.0499 0.0690  168 PHE   A CZ  
4141 N N   A LEU   A 169 ? 0.4625 0.4932 0.5220 -0.0137 -0.0182 0.0041  169 LEU   A N   
4142 N N   B LEU   A 169 ? 0.4648 0.4944 0.5879 -0.0269 -0.0138 -0.0097 169 LEU   A N   
4143 C CA  A LEU   A 169 ? 0.5027 0.5259 0.5780 -0.0149 -0.0180 -0.0063 169 LEU   A CA  
4144 C CA  B LEU   A 169 ? 0.5261 0.5418 0.6489 -0.0311 -0.0066 -0.0186 169 LEU   A CA  
4145 C C   A LEU   A 169 ? 0.5161 0.5366 0.5908 -0.0153 -0.0192 -0.0003 169 LEU   A C   
4146 C C   B LEU   A 169 ? 0.5480 0.5577 0.6688 -0.0327 -0.0066 -0.0060 169 LEU   A C   
4147 O O   A LEU   A 169 ? 0.5205 0.5400 0.5910 -0.0152 -0.0196 0.0024  169 LEU   A O   
4148 O O   B LEU   A 169 ? 0.5554 0.5634 0.6711 -0.0336 -0.0068 0.0008  169 LEU   A O   
4149 C CB  A LEU   A 169 ? 0.5248 0.5440 0.6118 -0.0160 -0.0167 -0.0221 169 LEU   A CB  
4150 C CB  B LEU   A 169 ? 0.5580 0.5687 0.6772 -0.0341 -0.0001 -0.0388 169 LEU   A CB  
4151 C CG  A LEU   A 169 ? 0.5420 0.5587 0.6411 -0.0167 -0.0153 -0.0359 169 LEU   A CG  
4152 C CG  B LEU   A 169 ? 0.5832 0.5899 0.7023 -0.0357 0.0038  -0.0566 169 LEU   A CG  
4153 C CD1 A LEU   A 169 ? 0.5476 0.5636 0.6516 -0.0167 -0.0152 -0.0402 169 LEU   A CD1 
4154 C CD1 B LEU   A 169 ? 0.5915 0.5971 0.7117 -0.0360 0.0047  -0.0623 169 LEU   A CD1 
4155 C CD2 A LEU   A 169 ? 0.5478 0.5638 0.6492 -0.0170 -0.0145 -0.0405 169 LEU   A CD2 
4156 C CD2 B LEU   A 169 ? 0.5915 0.5970 0.7084 -0.0364 0.0054  -0.0625 169 LEU   A CD2 
4157 O OXT A LEU   A 169 ? 0.5193 0.5395 0.5933 -0.0160 -0.0189 0.0014  169 LEU   A OXT 
4158 O OXT B LEU   A 169 ? 0.5527 0.5620 0.6723 -0.0339 -0.0059 -0.0030 169 LEU   A OXT 
4181 N N   A SER   B 1   ? 0.3476 0.3577 0.3623 -0.0882 -0.0726 0.0311  1   SER   B N   
4182 N N   B SER   B 1   ? 0.3362 0.3403 0.3613 -0.1311 -0.0543 0.0236  1   SER   B N   
4183 C CA  A SER   B 1   ? 0.3423 0.3592 0.3613 -0.0901 -0.0764 0.0324  1   SER   B CA  
4184 C CA  B SER   B 1   ? 0.3262 0.3483 0.3653 -0.1336 -0.0634 0.0225  1   SER   B CA  
4185 C C   A SER   B 1   ? 0.3260 0.3568 0.3440 -0.0922 -0.0799 0.0499  1   SER   B C   
4186 C C   B SER   B 1   ? 0.2973 0.3498 0.3388 -0.1361 -0.0757 0.0442  1   SER   B C   
4187 O O   A SER   B 1   ? 0.3292 0.3566 0.3285 -0.0908 -0.0841 0.0477  1   SER   B O   
4188 O O   B SER   B 1   ? 0.3057 0.3507 0.3234 -0.1315 -0.0672 0.0386  1   SER   B O   
4189 C CB  A SER   B 1   ? 0.3507 0.3607 0.3712 -0.0894 -0.0731 0.0196  1   SER   B CB  
4190 C CB  B SER   B 1   ? 0.3421 0.3503 0.3884 -0.1309 -0.0530 0.0031  1   SER   B CB  
4191 O OG  A SER   B 1   ? 0.3594 0.3666 0.3952 -0.0874 -0.0672 0.0139  1   SER   B OG  
4192 O OG  B SER   B 1   ? 0.3593 0.3617 0.4307 -0.1247 -0.0463 -0.0071 1   SER   B OG  
4207 N N   A MET   B 2   ? 0.3089 0.3528 0.3381 -0.0939 -0.0738 0.0755  2   MET   B N   
4208 N N   B MET   B 2   ? 0.2719 0.3479 0.3194 -0.1350 -0.0814 0.0864  2   MET   B N   
4209 C CA  A MET   B 2   ? 0.2932 0.3513 0.3408 -0.0894 -0.0705 0.0947  2   MET   B CA  
4210 C CA  B MET   B 2   ? 0.2572 0.3546 0.3159 -0.1133 -0.0919 0.1125  2   MET   B CA  
4211 C C   A MET   B 2   ? 0.2593 0.3330 0.3072 -0.0927 -0.0822 0.1224  2   MET   B C   
4212 C C   B MET   B 2   ? 0.2371 0.3396 0.2992 -0.0972 -0.0973 0.1353  2   MET   B C   
4213 O O   A MET   B 2   ? 0.2610 0.3414 0.3070 -0.0855 -0.0854 0.1207  2   MET   B O   
4214 O O   B MET   B 2   ? 0.2316 0.3539 0.3089 -0.0823 -0.1063 0.1345  2   MET   B O   
4215 C CB  A MET   B 2   ? 0.3143 0.3708 0.3963 -0.0754 -0.0506 0.0766  2   MET   B CB  
4216 C CB  B MET   B 2   ? 0.2752 0.3820 0.3714 -0.0911 -0.0761 0.0990  2   MET   B CB  
4217 C CG  A MET   B 2   ? 0.3343 0.3886 0.4506 -0.0603 -0.0314 0.0631  2   MET   B CG  
4218 C CG  B MET   B 2   ? 0.2953 0.4051 0.4132 -0.0621 -0.0595 0.1025  2   MET   B CG  
4219 S SD  A MET   B 2   ? 0.3538 0.4053 0.5068 -0.0460 -0.0178 0.0510  2   MET   B SD  
4220 S SD  B MET   B 2   ? 0.3179 0.4326 0.4467 -0.0333 -0.0571 0.1057  2   MET   B SD  
4221 C CE  A MET   B 2   ? 0.3565 0.4093 0.5113 -0.0450 -0.0117 0.0492  2   MET   B CE  
4222 C CE  B MET   B 2   ? 0.3186 0.4379 0.4681 -0.0364 -0.0505 0.0953  2   MET   B CE  
4241 N N   . VAL   B 3   ? 0.2218 0.3000 0.2839 -0.1077 -0.0864 0.1465  3   VAL   B N   
4242 C CA  . VAL   B 3   ? 0.2117 0.2593 0.2916 -0.0897 -0.0794 0.1352  3   VAL   B CA  
4243 C C   . VAL   B 3   ? 0.1906 0.2463 0.2559 -0.0794 -0.0737 0.1166  3   VAL   B C   
4244 O O   . VAL   B 3   ? 0.1916 0.2680 0.2499 -0.0760 -0.0695 0.1222  3   VAL   B O   
4245 C CB  . VAL   B 3   ? 0.2219 0.2499 0.3508 -0.0823 -0.0748 0.1138  3   VAL   B CB  
4246 C CG1 . VAL   B 3   ? 0.2269 0.2488 0.3748 -0.0810 -0.0699 0.1102  3   VAL   B CG1 
4247 C CG2 . VAL   B 3   ? 0.2244 0.2512 0.3687 -0.0713 -0.0657 0.1199  3   VAL   B CG2 
4258 N N   . ASN   B 4   ? 0.1811 0.2125 0.2185 -0.0692 -0.0653 0.0935  4   ASN   B N   
4259 C CA  . ASN   B 4   ? 0.1831 0.2141 0.1801 -0.0621 -0.0538 0.0526  4   ASN   B CA  
4260 C C   . ASN   B 4   ? 0.1803 0.2305 0.1683 -0.0667 -0.0385 0.0422  4   ASN   B C   
4261 O O   . ASN   B 4   ? 0.1825 0.2377 0.1928 -0.0600 -0.0331 0.0138  4   ASN   B O   
4262 C CB  . ASN   B 4   ? 0.1858 0.2063 0.1637 -0.0633 -0.0492 0.0382  4   ASN   B CB  
4263 C CG  . ASN   B 4   ? 0.1913 0.1881 0.1582 -0.0597 -0.0464 0.0419  4   ASN   B CG  
4264 O OD1 . ASN   B 4   ? 0.1883 0.1767 0.1612 -0.0567 -0.0471 0.0412  4   ASN   B OD1 
4265 N ND2 . ASN   B 4   ? 0.2117 0.1959 0.1581 -0.0394 -0.0363 0.0360  4   ASN   B ND2 
4272 N N   . SER   B 5   ? 0.1841 0.2449 0.1779 -0.0650 -0.0373 0.0377  5   SER   B N   
4273 C CA  . SER   B 5   ? 0.2055 0.2864 0.2004 -0.0530 -0.0174 0.0379  5   SER   B CA  
4274 C C   . SER   B 5   ? 0.2349 0.2872 0.2266 -0.0747 0.0062  0.0343  5   SER   B C   
4275 O O   . SER   B 5   ? 0.2582 0.2773 0.2941 -0.0689 0.0394  0.0254  5   SER   B O   
4276 C CB  . SER   B 5   ? 0.2194 0.3125 0.2473 -0.0400 0.0048  0.0545  5   SER   B CB  
4277 O OG  . SER   B 5   ? 0.2505 0.3291 0.3157 -0.0269 0.0083  0.0581  5   SER   B OG  
4283 N N   . PHE   B 6   ? 0.2606 0.3144 0.2105 -0.0833 0.0297  0.0512  6   PHE   B N   
4284 C CA  . PHE   B 6   ? 0.2816 0.3254 0.1754 -0.1040 0.0339  0.0303  6   PHE   B CA  
4285 C C   . PHE   B 6   ? 0.3390 0.3675 0.2299 -0.1073 0.0658  0.0033  6   PHE   B C   
4286 O O   . PHE   B 6   ? 0.3528 0.3989 0.2756 -0.0978 0.0592  -0.0092 6   PHE   B O   
4287 C CB  . PHE   B 6   ? 0.2513 0.3019 0.1562 -0.1012 0.0132  0.0299  6   PHE   B CB  
4288 C CG  . PHE   B 6   ? 0.2191 0.2689 0.1649 -0.0944 -0.0041 0.0309  6   PHE   B CG  
4289 C CD1 . PHE   B 6   ? 0.2161 0.2406 0.1487 -0.0840 -0.0129 0.0292  6   PHE   B CD1 
4290 C CD2 . PHE   B 6   ? 0.1979 0.2646 0.1640 -0.0744 -0.0118 0.0539  6   PHE   B CD2 
4291 C CE1 . PHE   B 6   ? 0.2089 0.2153 0.1679 -0.0674 -0.0197 0.0275  6   PHE   B CE1 
4292 C CE2 . PHE   B 6   ? 0.1905 0.2437 0.2005 -0.0622 -0.0044 0.0537  6   PHE   B CE2 
4293 C CZ  . PHE   B 6   ? 0.1913 0.2218 0.1849 -0.0629 -0.0135 0.0334  6   PHE   B CZ  
4303 N N   . SER   B 7   ? 0.3804 0.3586 0.2557 -0.1287 0.1048  -0.0152 7   SER   B N   
4304 C CA  . SER   B 7   ? 0.4166 0.3772 0.3217 -0.1273 0.1284  -0.0294 7   SER   B CA  
4305 C C   . SER   B 7   ? 0.4154 0.3539 0.3074 -0.1397 0.1431  -0.0518 7   SER   B C   
4306 O O   . SER   B 7   ? 0.4257 0.3494 0.3371 -0.1521 0.1389  -0.0565 7   SER   B O   
4307 C CB  . SER   B 7   ? 0.4392 0.4065 0.3970 -0.1214 0.1487  -0.0237 7   SER   B CB  
4308 O OG  . SER   B 7   ? 0.4541 0.4125 0.4529 -0.1170 0.1485  -0.0200 7   SER   B OG  
4314 N N   . GLY   B 8   ? 0.4153 0.3414 0.2993 -0.1250 0.1418  -0.0715 8   GLY   B N   
4315 C CA  . GLY   B 8   ? 0.3996 0.3221 0.2931 -0.1137 0.1469  -0.0769 8   GLY   B CA  
4316 C C   . GLY   B 8   ? 0.3769 0.2903 0.2809 -0.1085 0.1467  -0.0697 8   GLY   B C   
4317 O O   . GLY   B 8   ? 0.3893 0.2970 0.3249 -0.1025 0.1460  -0.0722 8   GLY   B O   
4321 N N   . TYR   B 9   ? 0.3528 0.2625 0.2455 -0.0971 0.1194  -0.0848 9   TYR   B N   
4322 C CA  . TYR   B 9   ? 0.3286 0.2338 0.2168 -0.0821 0.0929  -0.0661 9   TYR   B CA  
4323 C C   . TYR   B 9   ? 0.3206 0.2273 0.2078 -0.0745 0.0636  -0.0584 9   TYR   B C   
4324 O O   . TYR   B 9   ? 0.3288 0.2391 0.2564 -0.0788 0.0640  -0.0420 9   TYR   B O   
4325 C CB  . TYR   B 9   ? 0.3197 0.2135 0.2225 -0.0749 0.0843  -0.0624 9   TYR   B CB  
4326 C CG  . TYR   B 9   ? 0.3088 0.1955 0.2233 -0.0825 0.0716  -0.0611 9   TYR   B CG  
4327 C CD1 . TYR   B 9   ? 0.3091 0.1960 0.2375 -0.0950 0.0774  -0.0497 9   TYR   B CD1 
4328 C CD2 . TYR   B 9   ? 0.2929 0.1890 0.2154 -0.0780 0.0592  -0.0628 9   TYR   B CD2 
4329 C CE1 . TYR   B 9   ? 0.3002 0.2062 0.2375 -0.0971 0.0813  -0.0629 9   TYR   B CE1 
4330 C CE2 . TYR   B 9   ? 0.2894 0.1950 0.2219 -0.0782 0.0699  -0.0466 9   TYR   B CE2 
4331 C CZ  . TYR   B 9   ? 0.2918 0.2051 0.2389 -0.0912 0.0780  -0.0664 9   TYR   B CZ  
4332 O OH  . TYR   B 9   ? 0.2909 0.2178 0.2647 -0.1015 0.0725  -0.0828 9   TYR   B OH  
4342 N N   . LEU   B 10  ? 0.3014 0.2024 0.1828 -0.0775 0.0362  -0.0537 10  LEU   B N   
4343 C CA  . LEU   B 10  ? 0.3023 0.1968 0.1764 -0.0876 -0.0047 -0.0374 10  LEU   B CA  
4344 C C   . LEU   B 10  ? 0.2937 0.1977 0.1847 -0.0784 -0.0232 -0.0268 10  LEU   B C   
4345 O O   . LEU   B 10  ? 0.2746 0.1994 0.1936 -0.0697 -0.0193 -0.0192 10  LEU   B O   
4346 C CB  . LEU   B 10  ? 0.3200 0.1965 0.2046 -0.0932 -0.0224 -0.0084 10  LEU   B CB  
4347 C CG  . LEU   B 10  ? 0.3373 0.2040 0.2387 -0.0909 -0.0545 0.0034  10  LEU   B CG  
4348 C CD1 . LEU   B 10  ? 0.3490 0.2111 0.2535 -0.0860 -0.0502 0.0062  10  LEU   B CD1 
4349 C CD2 . LEU   B 10  ? 0.3436 0.2136 0.2505 -0.0878 -0.0523 0.0275  10  LEU   B CD2 
4361 N N   . LYS   B 11  ? 0.3109 0.2198 0.1894 -0.0760 -0.0361 -0.0132 11  LYS   B N   
4362 C CA  . LYS   B 11  ? 0.3310 0.2481 0.2401 -0.0663 -0.0429 -0.0193 11  LYS   B CA  
4363 C C   . LYS   B 11  ? 0.3082 0.2232 0.2384 -0.0841 -0.0419 -0.0313 11  LYS   B C   
4364 O O   . LYS   B 11  ? 0.3251 0.2399 0.2709 -0.1013 -0.0455 -0.0635 11  LYS   B O   
4365 C CB  . LYS   B 11  ? 0.3725 0.3017 0.3316 -0.0446 -0.0491 -0.0252 11  LYS   B CB  
4366 C CG  . LYS   B 11  ? 0.4067 0.3431 0.4267 -0.0300 -0.0525 -0.0348 11  LYS   B CG  
4367 C CD  . LYS   B 11  ? 0.4346 0.3735 0.5085 -0.0215 -0.0531 -0.0423 11  LYS   B CD  
4368 C CE  . LYS   B 11  ? 0.4552 0.3865 0.5680 -0.0171 -0.0555 -0.0474 11  LYS   B CE  
4369 N NZ  . LYS   B 11  ? 0.4616 0.4033 0.5983 -0.0155 -0.0583 -0.0485 11  LYS   B NZ  
4383 N N   . LEU   B 12  ? 0.2630 0.2030 0.2331 -0.0793 -0.0465 -0.0350 12  LEU   B N   
4384 C CA  . LEU   B 12  ? 0.2419 0.1829 0.2461 -0.0693 -0.0272 -0.0322 12  LEU   B CA  
4385 C C   . LEU   B 12  ? 0.2253 0.1859 0.2654 -0.0688 -0.0401 -0.0221 12  LEU   B C   
4386 O O   . LEU   B 12  ? 0.2207 0.1934 0.2876 -0.0780 -0.0596 -0.0238 12  LEU   B O   
4387 C CB  . LEU   B 12  ? 0.2465 0.1661 0.2418 -0.0487 -0.0190 -0.0294 12  LEU   B CB  
4388 C CG  . LEU   B 12  ? 0.2478 0.1562 0.2438 -0.0483 -0.0090 -0.0173 12  LEU   B CG  
4389 C CD1 . LEU   B 12  ? 0.2599 0.1593 0.2424 -0.0364 -0.0156 -0.0028 12  LEU   B CD1 
4390 C CD2 . LEU   B 12  ? 0.2480 0.1630 0.2518 -0.0508 -0.0092 -0.0206 12  LEU   B CD2 
4402 N N   . THR   B 13  ? 0.2201 0.1892 0.2711 -0.0654 -0.0479 -0.0264 13  THR   B N   
4403 C CA  . THR   B 13  ? 0.2204 0.1970 0.2476 -0.0652 -0.0628 -0.0130 13  THR   B CA  
4404 C C   . THR   B 13  ? 0.2618 0.2147 0.2614 -0.0784 -0.0826 -0.0074 13  THR   B C   
4405 O O   . THR   B 13  ? 0.2805 0.2154 0.2781 -0.0751 -0.0544 -0.0147 13  THR   B O   
4406 C CB  . THR   B 13  ? 0.1994 0.1969 0.2457 -0.0611 -0.0618 -0.0099 13  THR   B CB  
4407 O OG1 . THR   B 13  ? 0.1873 0.1884 0.2559 -0.0588 -0.0430 -0.0077 13  THR   B OG1 
4408 C CG2 . THR   B 13  ? 0.2115 0.2041 0.2484 -0.0566 -0.0533 -0.0025 13  THR   B CG2 
4416 N N   A ASP   B 14  ? 0.2730 0.2253 0.2765 -0.0810 -0.0958 -0.0001 14  ASP   B N   
4417 N N   B ASP   B 14  ? 0.2754 0.2292 0.2678 -0.0863 -0.1119 0.0047  14  ASP   B N   
4418 C CA  A ASP   B 14  ? 0.2844 0.2364 0.3016 -0.0789 -0.0980 0.0100  14  ASP   B CA  
4419 C CA  B ASP   B 14  ? 0.2908 0.2438 0.2967 -0.0829 -0.1162 0.0249  14  ASP   B CA  
4420 C C   A ASP   B 14  ? 0.2746 0.2197 0.2660 -0.0796 -0.0923 0.0174  14  ASP   B C   
4421 C C   B ASP   B 14  ? 0.2811 0.2258 0.2605 -0.0836 -0.1038 0.0280  14  ASP   B C   
4422 O O   A ASP   B 14  ? 0.2923 0.2314 0.2713 -0.0805 -0.0847 0.0208  14  ASP   B O   
4423 O O   B ASP   B 14  ? 0.3093 0.2439 0.2705 -0.0845 -0.0960 0.0365  14  ASP   B O   
4424 C CB  A ASP   B 14  ? 0.3035 0.2656 0.3668 -0.0742 -0.1016 0.0053  14  ASP   B CB  
4425 C CB  B ASP   B 14  ? 0.3149 0.2813 0.3768 -0.0740 -0.1213 0.0246  14  ASP   B CB  
4426 C CG  A ASP   B 14  ? 0.3218 0.2911 0.4270 -0.0689 -0.0978 -0.0009 14  ASP   B CG  
4427 C CG  B ASP   B 14  ? 0.3396 0.3183 0.4573 -0.0645 -0.1117 0.0162  14  ASP   B CG  
4428 O OD1 A ASP   B 14  ? 0.3277 0.2968 0.4428 -0.0734 -0.1009 -0.0082 14  ASP   B OD1 
4429 O OD1 B ASP   B 14  ? 0.3526 0.3288 0.4777 -0.0644 -0.1068 0.0104  14  ASP   B OD1 
4430 O OD2 A ASP   B 14  ? 0.3286 0.3039 0.4539 -0.0656 -0.0915 0.0001  14  ASP   B OD2 
4431 O OD2 B ASP   B 14  ? 0.3459 0.3355 0.4937 -0.0597 -0.1068 0.0152  14  ASP   B OD2 
4440 N N   . ASN   B 15  ? 0.2488 0.1966 0.2353 -0.0732 -0.0908 0.0226  15  ASN   B N   
4441 C CA  . ASN   B 15  ? 0.2028 0.1719 0.2246 -0.0471 -0.0649 0.0075  15  ASN   B CA  
4442 C C   . ASN   B 15  ? 0.1774 0.1540 0.2119 -0.0306 -0.0511 0.0021  15  ASN   B C   
4443 O O   . ASN   B 15  ? 0.1681 0.1485 0.2228 -0.0320 -0.0563 -0.0073 15  ASN   B O   
4444 C CB  . ASN   B 15  ? 0.1873 0.1614 0.2445 -0.0266 -0.0596 0.0048  15  ASN   B CB  
4445 C CG  . ASN   B 15  ? 0.1721 0.1603 0.2580 -0.0290 -0.0376 0.0143  15  ASN   B CG  
4446 O OD1 . ASN   B 15  ? 0.1768 0.1956 0.2788 -0.0467 -0.0417 0.0215  15  ASN   B OD1 
4447 N ND2 . ASN   B 15  ? 0.1648 0.1430 0.2434 -0.0201 -0.0050 -0.0072 15  ASN   B ND2 
4455 N N   . VAL   B 16  ? 0.1801 0.1436 0.2122 -0.0403 -0.0582 0.0015  16  VAL   B N   
4456 C CA  . VAL   B 16  ? 0.1782 0.1431 0.1916 -0.0337 -0.0480 -0.0130 16  VAL   B CA  
4457 C C   . VAL   B 16  ? 0.1780 0.1570 0.1880 -0.0478 -0.0373 -0.0079 16  VAL   B C   
4458 O O   . VAL   B 16  ? 0.1836 0.1682 0.2188 -0.0454 -0.0436 -0.0156 16  VAL   B O   
4459 C CB  . VAL   B 16  ? 0.1777 0.1446 0.2143 -0.0167 -0.0307 -0.0133 16  VAL   B CB  
4460 C CG1 . VAL   B 16  ? 0.1799 0.1451 0.2225 -0.0115 -0.0233 -0.0085 16  VAL   B CG1 
4461 C CG2 . VAL   B 16  ? 0.1792 0.1409 0.2353 -0.0039 -0.0251 -0.0108 16  VAL   B CG2 
4471 N N   . TYR   B 17  ? 0.1840 0.1666 0.1777 -0.0463 -0.0284 -0.0160 17  TYR   B N   
4472 C CA  . TYR   B 17  ? 0.1941 0.1891 0.1786 -0.0531 -0.0357 0.0079  17  TYR   B CA  
4473 C C   . TYR   B 17  ? 0.1871 0.1605 0.1867 -0.0529 -0.0224 -0.0055 17  TYR   B C   
4474 O O   . TYR   B 17  ? 0.1869 0.1651 0.1931 -0.0439 -0.0282 -0.0372 17  TYR   B O   
4475 C CB  . TYR   B 17  ? 0.2316 0.2419 0.2147 -0.0395 -0.0428 0.0437  17  TYR   B CB  
4476 C CG  . TYR   B 17  ? 0.2657 0.3009 0.2654 -0.0288 -0.0621 0.0601  17  TYR   B CG  
4477 C CD1 . TYR   B 17  ? 0.2841 0.3212 0.2933 -0.0260 -0.0742 0.0751  17  TYR   B CD1 
4478 C CD2 . TYR   B 17  ? 0.2892 0.3331 0.2998 -0.0190 -0.0704 0.0608  17  TYR   B CD2 
4479 C CE1 . TYR   B 17  ? 0.3046 0.3510 0.3159 -0.0163 -0.0863 0.0777  17  TYR   B CE1 
4480 C CE2 . TYR   B 17  ? 0.3063 0.3566 0.3195 -0.0082 -0.0867 0.0707  17  TYR   B CE2 
4481 C CZ  . TYR   B 17  ? 0.3169 0.3697 0.3273 -0.0062 -0.0945 0.0799  17  TYR   B CZ  
4482 O OH  . TYR   B 17  ? 0.3342 0.3837 0.3399 0.0021  -0.0994 0.0805  17  TYR   B OH  
4492 N N   . ILE   B 18  ? 0.1974 0.1608 0.1771 -0.0461 -0.0174 -0.0094 18  ILE   B N   
4493 C CA  . ILE   B 18  ? 0.1978 0.1588 0.1833 -0.0472 -0.0023 -0.0287 18  ILE   B CA  
4494 C C   . ILE   B 18  ? 0.2093 0.1592 0.1875 -0.0591 -0.0012 -0.0431 18  ILE   B C   
4495 O O   . ILE   B 18  ? 0.2275 0.1717 0.1936 -0.0548 0.0055  -0.0393 18  ILE   B O   
4496 C CB  . ILE   B 18  ? 0.2017 0.1603 0.1881 -0.0580 -0.0092 -0.0206 18  ILE   B CB  
4497 C CG1 . ILE   B 18  ? 0.2040 0.1638 0.1992 -0.0529 -0.0002 -0.0206 18  ILE   B CG1 
4498 C CG2 . ILE   B 18  ? 0.2092 0.1674 0.1974 -0.0577 -0.0053 -0.0161 18  ILE   B CG2 
4499 C CD1 . ILE   B 18  ? 0.2051 0.1922 0.2288 -0.0509 -0.0106 0.0129  18  ILE   B CD1 
4511 N N   . LYS   B 19  ? 0.2117 0.1535 0.1858 -0.0352 0.0416  -0.0470 19  LYS   B N   
4512 C CA  . LYS   B 19  ? 0.2184 0.1695 0.2225 -0.0454 0.0309  -0.0636 19  LYS   B CA  
4513 C C   . LYS   B 19  ? 0.1975 0.1654 0.2482 -0.0317 0.0467  -0.0711 19  LYS   B C   
4514 O O   . LYS   B 19  ? 0.1980 0.1657 0.2317 -0.0287 0.0430  -0.0629 19  LYS   B O   
4515 C CB  . LYS   B 19  ? 0.2426 0.1944 0.2296 -0.0525 0.0522  -0.0552 19  LYS   B CB  
4516 C CG  . LYS   B 19  ? 0.2746 0.2182 0.2572 -0.0618 0.0668  -0.0504 19  LYS   B CG  
4517 C CD  . LYS   B 19  ? 0.3028 0.2459 0.2636 -0.0681 0.0895  -0.0485 19  LYS   B CD  
4518 C CE  . LYS   B 19  ? 0.3331 0.2690 0.2902 -0.0710 0.0857  -0.0563 19  LYS   B CE  
4519 N NZ  . LYS   B 19  ? 0.3513 0.2815 0.2980 -0.0732 0.0826  -0.0571 19  LYS   B NZ  
4533 N N   . ASN   B 20  ? 0.1890 0.1784 0.2793 -0.0327 0.0576  -0.0730 20  ASN   B N   
4534 C CA  . ASN   B 20  ? 0.1934 0.1908 0.3002 -0.0258 0.0633  -0.0931 20  ASN   B CA  
4535 C C   . ASN   B 20  ? 0.1920 0.2125 0.2925 -0.0322 0.0684  -0.1026 20  ASN   B C   
4536 O O   . ASN   B 20  ? 0.2100 0.2494 0.3196 -0.0399 0.0676  -0.0982 20  ASN   B O   
4537 C CB  . ASN   B 20  ? 0.2290 0.1947 0.3311 0.0003  0.0452  -0.0976 20  ASN   B CB  
4538 C CG  . ASN   B 20  ? 0.2565 0.1960 0.3508 0.0296  0.0368  -0.1080 20  ASN   B CG  
4539 O OD1 . ASN   B 20  ? 0.2846 0.2259 0.3744 0.0433  0.0268  -0.1043 20  ASN   B OD1 
4540 N ND2 . ASN   B 20  ? 0.2493 0.1962 0.3457 0.0293  0.0261  -0.0983 20  ASN   B ND2 
4547 N N   . ALA   B 21  ? 0.1956 0.2040 0.2747 -0.0411 0.0638  -0.0894 21  ALA   B N   
4548 C CA  . ALA   B 21  ? 0.2055 0.2045 0.2802 -0.0446 0.0510  -0.0689 21  ALA   B CA  
4549 C C   . ALA   B 21  ? 0.2031 0.1790 0.2699 -0.0331 0.0498  -0.0458 21  ALA   B C   
4550 O O   . ALA   B 21  ? 0.2081 0.1661 0.2587 -0.0370 0.0457  -0.0421 21  ALA   B O   
4551 C CB  . ALA   B 21  ? 0.2203 0.2336 0.2892 -0.0588 0.0428  -0.0496 21  ALA   B CB  
4557 N N   . ASP   B 22  ? 0.1901 0.1660 0.2577 -0.0263 0.0378  -0.0422 22  ASP   B N   
4558 C CA  . ASP   B 22  ? 0.1850 0.1569 0.2407 -0.0154 0.0264  -0.0285 22  ASP   B CA  
4559 C C   . ASP   B 22  ? 0.1759 0.1530 0.1917 -0.0189 0.0213  -0.0141 22  ASP   B C   
4560 O O   . ASP   B 22  ? 0.1785 0.1587 0.2052 -0.0165 0.0122  -0.0081 22  ASP   B O   
4561 C CB  . ASP   B 22  ? 0.1925 0.1613 0.2786 -0.0070 0.0346  -0.0220 22  ASP   B CB  
4562 C CG  . ASP   B 22  ? 0.1931 0.1779 0.3173 0.0068  0.0135  -0.0101 22  ASP   B CG  
4563 O OD1 . ASP   B 22  ? 0.2006 0.1699 0.3183 0.0017  -0.0074 -0.0033 22  ASP   B OD1 
4564 O OD2 . ASP   B 22  ? 0.2024 0.2088 0.3772 0.0181  -0.0017 -0.0202 22  ASP   B OD2 
4569 N N   . ILE   B 23  ? 0.1869 0.1465 0.1716 -0.0185 0.0045  0.0058  23  ILE   B N   
4570 C CA  . ILE   B 23  ? 0.1733 0.1408 0.1636 -0.0167 0.0010  0.0045  23  ILE   B CA  
4571 C C   . ILE   B 23  ? 0.1661 0.1417 0.1567 -0.0112 -0.0095 0.0042  23  ILE   B C   
4572 O O   . ILE   B 23  ? 0.1561 0.1426 0.1582 -0.0140 -0.0074 0.0008  23  ILE   B O   
4573 C CB  . ILE   B 23  ? 0.1685 0.1462 0.1720 -0.0266 0.0038  0.0160  23  ILE   B CB  
4574 C CG1 . ILE   B 23  ? 0.1618 0.1591 0.1706 -0.0132 0.0077  0.0254  23  ILE   B CG1 
4575 C CG2 . ILE   B 23  ? 0.1767 0.1666 0.1682 -0.0150 -0.0025 0.0112  23  ILE   B CG2 
4576 C CD1 . ILE   B 23  ? 0.1739 0.1705 0.1856 -0.0096 0.0129  0.0225  23  ILE   B CD1 
4588 N N   . VAL   B 24  ? 0.1638 0.1401 0.1605 -0.0132 -0.0113 -0.0002 24  VAL   B N   
4589 C CA  . VAL   B 24  ? 0.1607 0.1467 0.1872 -0.0096 -0.0184 -0.0007 24  VAL   B CA  
4590 C C   . VAL   B 24  ? 0.1625 0.1515 0.1872 -0.0167 -0.0085 0.0086  24  VAL   B C   
4591 O O   . VAL   B 24  ? 0.1588 0.1645 0.2034 -0.0186 -0.0047 0.0180  24  VAL   B O   
4592 C CB  . VAL   B 24  ? 0.1660 0.1600 0.1937 -0.0018 -0.0245 -0.0101 24  VAL   B CB  
4593 C CG1 . VAL   B 24  ? 0.1678 0.1628 0.2261 -0.0138 -0.0269 -0.0067 24  VAL   B CG1 
4594 C CG2 . VAL   B 24  ? 0.1715 0.1932 0.1924 0.0059  -0.0164 -0.0096 24  VAL   B CG2 
4604 N N   . GLU   B 25  ? 0.1865 0.1622 0.1953 -0.0140 -0.0011 -0.0015 25  GLU   B N   
4605 C CA  . GLU   B 25  ? 0.1989 0.1931 0.2155 -0.0035 0.0192  -0.0170 25  GLU   B CA  
4606 C C   . GLU   B 25  ? 0.1920 0.1853 0.1818 -0.0204 0.0149  -0.0063 25  GLU   B C   
4607 O O   . GLU   B 25  ? 0.1955 0.1991 0.2021 -0.0221 0.0229  0.0001  25  GLU   B O   
4608 C CB  . GLU   B 25  ? 0.2522 0.2526 0.2983 0.0289  0.0409  -0.0231 25  GLU   B CB  
4609 C CG  . GLU   B 25  ? 0.2989 0.3325 0.4267 0.0388  0.0434  -0.0258 25  GLU   B CG  
4610 C CD  . GLU   B 25  ? 0.3433 0.3987 0.5316 0.0420  0.0409  -0.0273 25  GLU   B CD  
4611 O OE1 . GLU   B 25  ? 0.3716 0.4206 0.5668 0.0464  0.0424  -0.0247 25  GLU   B OE1 
4612 O OE2 . GLU   B 25  ? 0.3680 0.4201 0.5658 0.0432  0.0397  -0.0317 25  GLU   B OE2 
4619 N N   A GLU   B 26  ? 0.1888 0.1725 0.1618 -0.0323 0.0129  -0.0069 26  GLU   B N   
4620 N N   B GLU   B 26  ? 0.1845 0.1750 0.1735 -0.0350 0.0219  0.0024  26  GLU   B N   
4621 C CA  A GLU   B 26  ? 0.1881 0.1736 0.1545 -0.0385 -0.0017 -0.0036 26  GLU   B CA  
4622 C CA  B GLU   B 26  ? 0.1836 0.1929 0.1921 -0.0384 0.0038  0.0136  26  GLU   B CA  
4623 C C   A GLU   B 26  ? 0.1748 0.1759 0.1584 -0.0329 0.0031  0.0084  26  GLU   B C   
4624 C C   B GLU   B 26  ? 0.1721 0.1879 0.1729 -0.0305 0.0083  0.0187  26  GLU   B C   
4625 O O   A GLU   B 26  ? 0.1850 0.1901 0.1688 -0.0277 -0.0014 0.0104  26  GLU   B O   
4626 O O   B GLU   B 26  ? 0.1878 0.2112 0.1837 -0.0221 0.0021  0.0234  26  GLU   B O   
4627 C CB  A GLU   B 26  ? 0.2065 0.1728 0.1508 -0.0430 -0.0056 -0.0022 26  GLU   B CB  
4628 C CB  B GLU   B 26  ? 0.2055 0.2156 0.2379 -0.0382 0.0075  0.0341  26  GLU   B CB  
4629 C CG  A GLU   B 26  ? 0.2328 0.1737 0.1692 -0.0434 -0.0016 -0.0097 26  GLU   B CG  
4630 C CG  B GLU   B 26  ? 0.2366 0.2455 0.3113 -0.0288 0.0161  0.0372  26  GLU   B CG  
4631 C CD  A GLU   B 26  ? 0.2474 0.1676 0.1562 -0.0544 0.0150  -0.0287 26  GLU   B CD  
4632 C CD  B GLU   B 26  ? 0.2466 0.2531 0.3398 -0.0298 0.0401  0.0422  26  GLU   B CD  
4633 O OE1 A GLU   B 26  ? 0.2527 0.1500 0.1404 -0.0505 0.0415  -0.0511 26  GLU   B OE1 
4634 O OE1 B GLU   B 26  ? 0.2552 0.2552 0.3765 -0.0330 0.0780  0.0396  26  GLU   B OE1 
4635 O OE2 A GLU   B 26  ? 0.2569 0.1870 0.1577 -0.0547 0.0211  -0.0012 26  GLU   B OE2 
4636 O OE2 B GLU   B 26  ? 0.2460 0.2568 0.3474 -0.0215 0.0365  0.0310  26  GLU   B OE2 
4649 N N   . ALA   B 27  ? 0.1583 0.1715 0.1637 -0.0323 0.0076  0.0191  27  ALA   B N   
4650 C CA  . ALA   B 27  ? 0.1526 0.1653 0.1813 -0.0188 -0.0042 0.0304  27  ALA   B CA  
4651 C C   . ALA   B 27  ? 0.1588 0.1787 0.2123 -0.0202 0.0066  0.0428  27  ALA   B C   
4652 O O   . ALA   B 27  ? 0.1664 0.1843 0.2199 -0.0142 0.0044  0.0498  27  ALA   B O   
4653 C CB  . ALA   B 27  ? 0.1666 0.1524 0.1776 -0.0165 -0.0054 0.0313  27  ALA   B CB  
4660 N N   . LYS   B 28  ? 0.1521 0.1962 0.2411 -0.0247 0.0178  0.0666  28  LYS   B N   
4661 C CA  . LYS   B 28  ? 0.1699 0.2347 0.2702 -0.0168 0.0480  0.0957  28  LYS   B CA  
4662 C C   . LYS   B 28  ? 0.1931 0.2471 0.2517 -0.0097 0.0568  0.0832  28  LYS   B C   
4663 O O   . LYS   B 28  ? 0.2164 0.2588 0.2606 -0.0112 0.0600  0.0745  28  LYS   B O   
4664 C CB  . LYS   B 28  ? 0.1941 0.2781 0.3367 -0.0025 0.0739  0.1217  28  LYS   B CB  
4665 C CG  . LYS   B 28  ? 0.2247 0.3310 0.3923 0.0092  0.0935  0.1413  28  LYS   B CG  
4666 C CD  . LYS   B 28  ? 0.2779 0.3992 0.4548 0.0188  0.1205  0.1423  28  LYS   B CD  
4667 C CE  . LYS   B 28  ? 0.3234 0.4468 0.5069 0.0296  0.1288  0.1451  28  LYS   B CE  
4668 N NZ  . LYS   B 28  ? 0.3546 0.4620 0.5279 0.0373  0.1318  0.1518  28  LYS   B NZ  
4682 N N   . LYS   B 29  ? 0.2153 0.2720 0.2574 0.0051  0.0546  0.0692  29  LYS   B N   
4683 C CA  . LYS   B 29  ? 0.2544 0.3106 0.2827 0.0046  0.0540  0.0645  29  LYS   B CA  
4684 C C   . LYS   B 29  ? 0.2447 0.3125 0.2481 0.0022  0.0328  0.0763  29  LYS   B C   
4685 O O   . LYS   B 29  ? 0.2627 0.3359 0.2552 0.0128  0.0329  0.0804  29  LYS   B O   
4686 C CB  . LYS   B 29  ? 0.3129 0.3531 0.3785 0.0056  0.0542  0.0428  29  LYS   B CB  
4687 C CG  . LYS   B 29  ? 0.3621 0.3902 0.4838 0.0026  0.0600  0.0289  29  LYS   B CG  
4688 C CD  . LYS   B 29  ? 0.4055 0.4171 0.5604 -0.0020 0.0712  0.0152  29  LYS   B CD  
4689 C CE  . LYS   B 29  ? 0.4414 0.4360 0.6120 -0.0050 0.0821  0.0054  29  LYS   B CE  
4690 N NZ  . LYS   B 29  ? 0.4498 0.4457 0.6449 -0.0054 0.0864  -0.0007 29  LYS   B NZ  
4704 N N   . VAL   B 30  ? 0.2131 0.2879 0.2346 -0.0177 0.0197  0.0770  30  VAL   B N   
4705 C CA  . VAL   B 30  ? 0.2013 0.2735 0.2553 -0.0306 -0.0124 0.0804  30  VAL   B CA  
4706 C C   . VAL   B 30  ? 0.1743 0.2611 0.2426 -0.0339 -0.0159 0.0876  30  VAL   B C   
4707 O O   . VAL   B 30  ? 0.1858 0.2760 0.2390 -0.0255 -0.0089 0.1058  30  VAL   B O   
4708 C CB  . VAL   B 30  ? 0.2153 0.2678 0.3194 -0.0449 -0.0402 0.0840  30  VAL   B CB  
4709 C CG1 . VAL   B 30  ? 0.2278 0.2804 0.3292 -0.0384 -0.0354 0.0813  30  VAL   B CG1 
4710 C CG2 . VAL   B 30  ? 0.2337 0.2614 0.3492 -0.0509 -0.0494 0.0647  30  VAL   B CG2 
4720 N N   A LYS   B 31  ? 0.1829 0.2446 0.2547 -0.0376 -0.0169 0.0839  31  LYS   B N   
4721 N N   B LYS   B 31  ? 0.1650 0.2290 0.2628 -0.0519 -0.0098 0.0968  31  LYS   B N   
4722 C CA  A LYS   B 31  ? 0.1904 0.2395 0.2740 -0.0372 -0.0219 0.0784  31  LYS   B CA  
4723 C CA  B LYS   B 31  ? 0.1550 0.2282 0.2948 -0.0541 -0.0145 0.1008  31  LYS   B CA  
4724 C C   A LYS   B 31  ? 0.1777 0.2023 0.2385 -0.0403 -0.0337 0.0703  31  LYS   B C   
4725 C C   B LYS   B 31  ? 0.1492 0.1933 0.2565 -0.0478 -0.0314 0.0885  31  LYS   B C   
4726 O O   A LYS   B 31  ? 0.1786 0.2049 0.2344 -0.0352 -0.0332 0.0755  31  LYS   B O   
4727 O O   B LYS   B 31  ? 0.1446 0.1960 0.2654 -0.0341 -0.0276 0.1032  31  LYS   B O   
4728 C CB  A LYS   B 31  ? 0.2137 0.2746 0.3241 -0.0339 -0.0106 0.0790  31  LYS   B CB  
4729 C CB  B LYS   B 31  ? 0.1653 0.2756 0.3477 -0.0570 0.0121  0.1140  31  LYS   B CB  
4730 C CG  A LYS   B 31  ? 0.2395 0.3048 0.3732 -0.0334 -0.0026 0.0757  31  LYS   B CG  
4731 C CG  B LYS   B 31  ? 0.1984 0.3241 0.3986 -0.0571 0.0222  0.1144  31  LYS   B CG  
4732 C CD  A LYS   B 31  ? 0.2604 0.3314 0.4156 -0.0311 -0.0001 0.0693  31  LYS   B CD  
4733 C CD  B LYS   B 31  ? 0.2334 0.3754 0.4463 -0.0564 0.0193  0.1084  31  LYS   B CD  
4734 C CE  A LYS   B 31  ? 0.2763 0.3508 0.4518 -0.0284 -0.0011 0.0620  31  LYS   B CE  
4735 C CE  B LYS   B 31  ? 0.2547 0.4078 0.4914 -0.0553 0.0107  0.0986  31  LYS   B CE  
4736 N NZ  A LYS   B 31  ? 0.2867 0.3615 0.4673 -0.0240 -0.0044 0.0550  31  LYS   B NZ  
4737 N NZ  B LYS   B 31  ? 0.2701 0.4231 0.5065 -0.0484 -0.0002 0.0882  31  LYS   B NZ  
4764 N N   . PRO   B 32  ? 0.1700 0.1647 0.2102 -0.0467 -0.0432 0.0551  32  PRO   B N   
4765 C CA  . PRO   B 32  ? 0.1833 0.1588 0.1618 -0.0477 -0.0486 0.0324  32  PRO   B CA  
4766 C C   . PRO   B 32  ? 0.1967 0.1500 0.1587 -0.0519 -0.0613 0.0378  32  PRO   B C   
4767 O O   . PRO   B 32  ? 0.2062 0.1442 0.1944 -0.0484 -0.0763 0.0430  32  PRO   B O   
4768 C CB  . PRO   B 32  ? 0.2032 0.1568 0.1558 -0.0565 -0.0369 0.0205  32  PRO   B CB  
4769 C CG  . PRO   B 32  ? 0.2133 0.1418 0.1681 -0.0416 -0.0550 0.0264  32  PRO   B CG  
4770 C CD  . PRO   B 32  ? 0.1943 0.1434 0.1973 -0.0284 -0.0620 0.0319  32  PRO   B CD  
4778 N N   . THR   B 33  ? 0.1996 0.1401 0.1454 -0.0447 -0.0555 0.0247  33  THR   B N   
4779 C CA  . THR   B 33  ? 0.2055 0.1408 0.1359 -0.0450 -0.0503 0.0378  33  THR   B CA  
4780 C C   . THR   B 33  ? 0.2042 0.1342 0.1411 -0.0477 -0.0562 0.0248  33  THR   B C   
4781 O O   . THR   B 33  ? 0.2261 0.1443 0.1519 -0.0583 -0.0572 0.0208  33  THR   B O   
4782 C CB  . THR   B 33  ? 0.2156 0.1481 0.1409 -0.0282 -0.0575 0.0340  33  THR   B CB  
4783 O OG1 . THR   B 33  ? 0.1990 0.1546 0.1726 -0.0291 -0.0576 0.0378  33  THR   B OG1 
4784 C CG2 . THR   B 33  ? 0.2471 0.1625 0.1653 -0.0191 -0.0521 0.0231  33  THR   B CG2 
4792 N N   . VAL   B 34  ? 0.1836 0.1303 0.1417 -0.0391 -0.0494 0.0172  34  VAL   B N   
4793 C CA  . VAL   B 34  ? 0.1680 0.1301 0.1353 -0.0332 -0.0404 0.0154  34  VAL   B CA  
4794 C C   . VAL   B 34  ? 0.1486 0.1273 0.1234 -0.0357 -0.0253 0.0128  34  VAL   B C   
4795 O O   . VAL   B 34  ? 0.1729 0.1332 0.1246 -0.0324 -0.0374 0.0130  34  VAL   B O   
4796 C CB  . VAL   B 34  ? 0.1804 0.1407 0.1597 -0.0139 -0.0349 0.0079  34  VAL   B CB  
4797 C CG1 . VAL   B 34  ? 0.1736 0.1488 0.1606 -0.0182 -0.0220 0.0013  34  VAL   B CG1 
4798 C CG2 . VAL   B 34  ? 0.1869 0.1480 0.1831 -0.0121 -0.0363 0.0061  34  VAL   B CG2 
4808 N N   . VAL   B 35  ? 0.1414 0.1193 0.1181 -0.0331 -0.0169 0.0121  35  VAL   B N   
4809 C CA  . VAL   B 35  ? 0.1390 0.1190 0.1144 -0.0237 -0.0105 0.0092  35  VAL   B CA  
4810 C C   . VAL   B 35  ? 0.1271 0.1125 0.1179 -0.0203 -0.0144 0.0077  35  VAL   B C   
4811 O O   . VAL   B 35  ? 0.1384 0.1229 0.1146 -0.0264 -0.0045 -0.0003 35  VAL   B O   
4812 C CB  . VAL   B 35  ? 0.1388 0.1403 0.1239 -0.0236 0.0012  0.0006  35  VAL   B CB  
4813 C CG1 . VAL   B 35  ? 0.1328 0.1551 0.1452 -0.0252 0.0037  0.0057  35  VAL   B CG1 
4814 C CG2 . VAL   B 35  ? 0.1449 0.1387 0.1447 -0.0116 -0.0011 0.0034  35  VAL   B CG2 
4824 N N   . VAL   B 36  ? 0.1303 0.1189 0.1195 -0.0222 -0.0150 0.0137  36  VAL   B N   
4825 C CA  . VAL   B 36  ? 0.1301 0.1092 0.1179 -0.0118 -0.0033 0.0054  36  VAL   B CA  
4826 C C   . VAL   B 36  ? 0.1213 0.1159 0.0988 -0.0062 0.0003  0.0034  36  VAL   B C   
4827 O O   . VAL   B 36  ? 0.1327 0.1266 0.1282 -0.0111 -0.0082 -0.0037 36  VAL   B O   
4828 C CB  . VAL   B 36  ? 0.1254 0.1171 0.1179 -0.0143 -0.0064 0.0079  36  VAL   B CB  
4829 C CG1 . VAL   B 36  ? 0.1240 0.1355 0.1380 -0.0133 -0.0055 0.0206  36  VAL   B CG1 
4830 C CG2 . VAL   B 36  ? 0.1362 0.1249 0.1352 -0.0185 -0.0149 0.0098  36  VAL   B CG2 
4840 N N   . ASN   B 37  ? 0.1271 0.1181 0.1007 0.0015  -0.0071 0.0066  37  ASN   B N   
4841 C CA  . ASN   B 37  ? 0.1295 0.1227 0.1222 0.0016  -0.0119 0.0003  37  ASN   B CA  
4842 C C   . ASN   B 37  ? 0.1293 0.1281 0.1064 0.0046  -0.0088 0.0044  37  ASN   B C   
4843 O O   . ASN   B 37  ? 0.1380 0.1307 0.1253 0.0019  0.0025  0.0089  37  ASN   B O   
4844 C CB  . ASN   B 37  ? 0.1254 0.1234 0.1146 0.0026  -0.0072 0.0030  37  ASN   B CB  
4845 C CG  . ASN   B 37  ? 0.1299 0.1279 0.1200 0.0040  -0.0071 0.0009  37  ASN   B CG  
4846 O OD1 . ASN   B 37  ? 0.1436 0.1288 0.1407 0.0126  -0.0147 0.0011  37  ASN   B OD1 
4847 N ND2 . ASN   B 37  ? 0.1396 0.1217 0.1187 0.0018  -0.0152 0.0051  37  ASN   B ND2 
4854 N N   . ALA   B 38  ? 0.1485 0.1159 0.1191 0.0108  0.0025  0.0058  38  ALA   B N   
4855 C CA  . ALA   B 38  ? 0.1521 0.1231 0.1250 -0.0013 -0.0008 0.0057  38  ALA   B CA  
4856 C C   . ALA   B 38  ? 0.1414 0.1210 0.1223 0.0017  0.0082  0.0119  38  ALA   B C   
4857 O O   . ALA   B 38  ? 0.1564 0.1307 0.1374 0.0135  -0.0004 0.0149  38  ALA   B O   
4858 C CB  . ALA   B 38  ? 0.1707 0.1336 0.1344 -0.0092 0.0120  0.0048  38  ALA   B CB  
4864 N N   . ALA   B 39  ? 0.1396 0.1214 0.1227 0.0059  -0.0024 0.0048  39  ALA   B N   
4865 C CA  . ALA   B 39  ? 0.1496 0.1268 0.1400 0.0099  -0.0054 0.0051  39  ALA   B CA  
4866 C C   . ALA   B 39  ? 0.1577 0.1329 0.1154 0.0135  -0.0042 -0.0040 39  ALA   B C   
4867 O O   . ALA   B 39  ? 0.1608 0.1400 0.1356 -0.0002 -0.0022 0.0107  39  ALA   B O   
4868 C CB  . ALA   B 39  ? 0.1431 0.1340 0.1364 0.0008  -0.0051 0.0026  39  ALA   B CB  
4874 N N   . ASN   B 40  ? 0.1590 0.1553 0.1165 0.0028  0.0028  -0.0091 40  ASN   B N   
4875 C CA  . ASN   B 40  ? 0.1703 0.1568 0.1299 0.0128  0.0009  0.0017  40  ASN   B CA  
4876 C C   . ASN   B 40  ? 0.1731 0.1551 0.1081 0.0181  -0.0014 -0.0006 40  ASN   B C   
4877 O O   . ASN   B 40  ? 0.1679 0.1472 0.1253 0.0153  -0.0093 0.0007  40  ASN   B O   
4878 C CB  . ASN   B 40  ? 0.1847 0.1531 0.1411 0.0176  -0.0125 0.0166  40  ASN   B CB  
4879 C CG  . ASN   B 40  ? 0.1910 0.1645 0.1783 0.0158  -0.0226 0.0181  40  ASN   B CG  
4880 O OD1 . ASN   B 40  ? 0.1895 0.1633 0.2628 0.0070  -0.0373 0.0229  40  ASN   B OD1 
4881 N ND2 . ASN   B 40  ? 0.1947 0.1676 0.1718 0.0118  -0.0202 0.0138  40  ASN   B ND2 
4888 N N   . VAL   B 41  ? 0.1818 0.1628 0.1156 0.0274  0.0117  0.0008  41  VAL   B N   
4889 C CA  . VAL   B 41  ? 0.1866 0.1728 0.1179 0.0188  0.0030  -0.0146 41  VAL   B CA  
4890 C C   . VAL   B 41  ? 0.1813 0.1708 0.1164 0.0247  -0.0064 -0.0031 41  VAL   B C   
4891 O O   . VAL   B 41  ? 0.1740 0.1704 0.1297 0.0225  -0.0057 -0.0099 41  VAL   B O   
4892 C CB  . VAL   B 41  ? 0.1989 0.1906 0.1429 0.0081  0.0269  -0.0248 41  VAL   B CB  
4893 C CG1 . VAL   B 41  ? 0.1972 0.1967 0.1700 -0.0003 0.0337  -0.0245 41  VAL   B CG1 
4894 C CG2 . VAL   B 41  ? 0.2124 0.2121 0.1446 -0.0014 0.0285  -0.0144 41  VAL   B CG2 
4904 N N   . TYR   B 42  ? 0.1958 0.1698 0.1188 0.0268  -0.0129 -0.0059 42  TYR   B N   
4905 C CA  . TYR   B 42  ? 0.2045 0.1767 0.1179 0.0281  -0.0327 -0.0175 42  TYR   B CA  
4906 C C   . TYR   B 42  ? 0.1830 0.1621 0.1271 0.0270  -0.0306 -0.0227 42  TYR   B C   
4907 O O   . TYR   B 42  ? 0.1812 0.1700 0.1587 0.0273  -0.0362 -0.0183 42  TYR   B O   
4908 C CB  . TYR   B 42  ? 0.2267 0.2062 0.1422 0.0192  -0.0362 -0.0050 42  TYR   B CB  
4909 C CG  . TYR   B 42  ? 0.2251 0.2148 0.1321 0.0011  -0.0268 0.0091  42  TYR   B CG  
4910 C CD1 . TYR   B 42  ? 0.2101 0.2114 0.1070 -0.0105 -0.0181 0.0135  42  TYR   B CD1 
4911 C CD2 . TYR   B 42  ? 0.2344 0.2245 0.1630 -0.0035 -0.0159 0.0175  42  TYR   B CD2 
4912 C CE1 . TYR   B 42  ? 0.2211 0.2287 0.1034 -0.0138 -0.0153 0.0108  42  TYR   B CE1 
4913 C CE2 . TYR   B 42  ? 0.2307 0.2396 0.1463 -0.0074 0.0151  0.0352  42  TYR   B CE2 
4914 C CZ  . TYR   B 42  ? 0.2346 0.2490 0.1297 0.0022  0.0130  0.0174  42  TYR   B CZ  
4915 O OH  . TYR   B 42  ? 0.2603 0.2738 0.1714 0.0178  0.0130  0.0136  42  TYR   B OH  
4925 N N   . LEU   B 43  ? 0.1631 0.1443 0.1215 0.0160  -0.0150 -0.0141 43  LEU   B N   
4926 C CA  . LEU   B 43  ? 0.1668 0.1449 0.1167 0.0111  -0.0165 -0.0085 43  LEU   B CA  
4927 C C   . LEU   B 43  ? 0.1679 0.1446 0.1166 0.0136  -0.0209 0.0017  43  LEU   B C   
4928 O O   . LEU   B 43  ? 0.1703 0.1488 0.1495 0.0122  -0.0273 0.0144  43  LEU   B O   
4929 C CB  . LEU   B 43  ? 0.1631 0.1368 0.1340 0.0043  -0.0251 -0.0091 43  LEU   B CB  
4930 C CG  . LEU   B 43  ? 0.1642 0.1345 0.1449 0.0022  -0.0286 -0.0027 43  LEU   B CG  
4931 C CD1 . LEU   B 43  ? 0.1775 0.1417 0.1791 -0.0042 -0.0428 -0.0049 43  LEU   B CD1 
4932 C CD2 . LEU   B 43  ? 0.1640 0.1421 0.1504 -0.0039 -0.0352 -0.0030 43  LEU   B CD2 
4944 N N   . LYS   B 44  ? 0.1678 0.1448 0.1199 0.0144  -0.0186 -0.0066 44  LYS   B N   
4945 C CA  . LYS   B 44  ? 0.1857 0.1559 0.1276 0.0162  -0.0122 -0.0006 44  LYS   B CA  
4946 C C   . LYS   B 44  ? 0.1775 0.1502 0.1189 0.0191  -0.0178 -0.0021 44  LYS   B C   
4947 O O   . LYS   B 44  ? 0.2027 0.1475 0.1529 0.0147  -0.0051 0.0018  44  LYS   B O   
4948 C CB  . LYS   B 44  ? 0.2146 0.1767 0.1425 0.0281  -0.0291 -0.0040 44  LYS   B CB  
4949 C CG  . LYS   B 44  ? 0.2529 0.2054 0.1884 0.0190  -0.0547 0.0008  44  LYS   B CG  
4950 C CD  . LYS   B 44  ? 0.2935 0.2256 0.2663 0.0022  -0.0694 -0.0058 44  LYS   B CD  
4951 C CE  . LYS   B 44  ? 0.3317 0.2557 0.3278 -0.0076 -0.0752 0.0018  44  LYS   B CE  
4952 N NZ  . LYS   B 44  ? 0.3389 0.2640 0.3509 -0.0070 -0.0866 0.0207  44  LYS   B NZ  
4966 N N   . HIS   B 45  ? 0.1645 0.1518 0.1185 0.0104  -0.0099 0.0072  45  HIS   B N   
4967 C CA  . HIS   B 45  ? 0.1685 0.1521 0.1258 0.0149  -0.0190 -0.0018 45  HIS   B CA  
4968 C C   . HIS   B 45  ? 0.1935 0.1729 0.1648 0.0264  -0.0234 -0.0068 45  HIS   B C   
4969 O O   . HIS   B 45  ? 0.2023 0.2106 0.2278 0.0563  0.0053  -0.0007 45  HIS   B O   
4970 C CB  . HIS   B 45  ? 0.1592 0.1571 0.1312 0.0061  -0.0143 -0.0027 45  HIS   B CB  
4971 C CG  . HIS   B 45  ? 0.1567 0.1482 0.1402 0.0028  -0.0167 -0.0003 45  HIS   B CG  
4972 N ND1 . HIS   B 45  ? 0.1613 0.1428 0.1433 0.0049  -0.0225 -0.0022 45  HIS   B ND1 
4973 C CD2 . HIS   B 45  ? 0.1677 0.1482 0.1603 -0.0021 -0.0212 0.0028  45  HIS   B CD2 
4974 C CE1 . HIS   B 45  ? 0.1664 0.1364 0.1311 0.0035  -0.0337 -0.0051 45  HIS   B CE1 
4975 N NE2 . HIS   B 45  ? 0.1762 0.1384 0.1428 0.0034  -0.0243 -0.0058 45  HIS   B NE2 
4983 N N   A GLY   B 46  ? 0.2044 0.1771 0.1950 0.0252  -0.0353 0.0033  46  GLY   B N   
4984 N N   B GLY   B 46  ? 0.2064 0.1671 0.1928 0.0310  -0.0434 0.0184  46  GLY   B N   
4985 C CA  A GLY   B 46  ? 0.2134 0.1888 0.2352 0.0182  -0.0406 0.0025  46  GLY   B CA  
4986 C CA  B GLY   B 46  ? 0.2179 0.1821 0.2385 0.0224  -0.0513 0.0158  46  GLY   B CA  
4987 C C   A GLY   B 46  ? 0.2166 0.2018 0.2749 0.0199  -0.0379 0.0021  46  GLY   B C   
4988 C C   B GLY   B 46  ? 0.2196 0.1995 0.2845 0.0283  -0.0467 0.0164  46  GLY   B C   
4989 O O   A GLY   B 46  ? 0.2242 0.2132 0.3314 0.0234  -0.0243 -0.0159 46  GLY   B O   
4990 O O   B GLY   B 46  ? 0.2327 0.2176 0.3672 0.0340  -0.0233 -0.0088 46  GLY   B O   
4997 N N   . GLY   B 47  ? 0.2153 0.2074 0.2667 0.0088  -0.0326 -0.0004 47  GLY   B N   
4998 C CA  . GLY   B 47  ? 0.1998 0.1778 0.2271 -0.0013 -0.0254 -0.0017 47  GLY   B CA  
4999 C C   . GLY   B 47  ? 0.1809 0.1523 0.1897 -0.0031 -0.0096 0.0039  47  GLY   B C   
5000 O O   . GLY   B 47  ? 0.1915 0.1459 0.1903 0.0075  -0.0162 0.0109  47  GLY   B O   
5005 N N   . GLY   B 48  ? 0.1599 0.1401 0.1879 0.0015  -0.0138 0.0134  48  GLY   B N   
5006 C CA  . GLY   B 48  ? 0.1597 0.1375 0.1921 0.0024  -0.0028 0.0061  48  GLY   B CA  
5007 C C   . GLY   B 48  ? 0.1493 0.1402 0.1695 0.0058  -0.0012 0.0007  48  GLY   B C   
5008 O O   . GLY   B 48  ? 0.1397 0.1420 0.1982 0.0085  -0.0080 0.0060  48  GLY   B O   
5012 N N   . VAL   B 49  ? 0.1500 0.1399 0.1616 0.0085  0.0004  0.0050  49  VAL   B N   
5013 C CA  . VAL   B 49  ? 0.1491 0.1506 0.1503 0.0131  -0.0120 -0.0115 49  VAL   B CA  
5014 C C   . VAL   B 49  ? 0.1347 0.1442 0.1259 0.0136  -0.0054 -0.0030 49  VAL   B C   
5015 O O   . VAL   B 49  ? 0.1499 0.1439 0.1441 0.0047  -0.0074 -0.0007 49  VAL   B O   
5016 C CB  . VAL   B 49  ? 0.1532 0.1659 0.1728 0.0030  -0.0187 -0.0086 49  VAL   B CB  
5017 C CG1 . VAL   B 49  ? 0.1570 0.1772 0.1695 0.0083  -0.0314 -0.0014 49  VAL   B CG1 
5018 C CG2 . VAL   B 49  ? 0.1716 0.1832 0.1860 -0.0110 -0.0346 -0.0103 49  VAL   B CG2 
5028 N N   . ALA   B 50  ? 0.1373 0.1398 0.1333 0.0042  -0.0058 0.0040  50  ALA   B N   
5029 C CA  . ALA   B 50  ? 0.1392 0.1258 0.1425 0.0114  -0.0032 0.0000  50  ALA   B CA  
5030 C C   . ALA   B 50  ? 0.1443 0.1314 0.1300 0.0063  -0.0031 0.0029  50  ALA   B C   
5031 O O   . ALA   B 50  ? 0.1481 0.1348 0.1335 0.0053  0.0042  -0.0005 50  ALA   B O   
5032 C CB  . ALA   B 50  ? 0.1584 0.1305 0.1437 0.0018  -0.0085 0.0064  50  ALA   B CB  
5038 N N   . GLY   B 51  ? 0.1491 0.1396 0.1509 0.0139  -0.0161 0.0080  51  GLY   B N   
5039 C CA  . GLY   B 51  ? 0.1534 0.1490 0.1786 0.0192  -0.0144 0.0019  51  GLY   B CA  
5040 C C   . GLY   B 51  ? 0.1439 0.1437 0.1733 0.0229  -0.0152 0.0054  51  GLY   B C   
5041 O O   . GLY   B 51  ? 0.1501 0.1561 0.1905 0.0176  -0.0157 -0.0067 51  GLY   B O   
5045 N N   . ALA   B 52  ? 0.1444 0.1413 0.1566 0.0163  -0.0092 -0.0014 52  ALA   B N   
5046 C CA  . ALA   B 52  ? 0.1478 0.1451 0.1569 0.0172  -0.0001 -0.0102 52  ALA   B CA  
5047 C C   . ALA   B 52  ? 0.1427 0.1402 0.1458 0.0079  0.0011  -0.0040 52  ALA   B C   
5048 O O   . ALA   B 52  ? 0.1413 0.1467 0.1687 0.0076  -0.0066 0.0004  52  ALA   B O   
5049 C CB  . ALA   B 52  ? 0.1649 0.1465 0.1631 0.0086  -0.0032 -0.0118 52  ALA   B CB  
5055 N N   . LEU   B 53  ? 0.1373 0.1419 0.1460 0.0166  -0.0027 -0.0001 53  LEU   B N   
5056 C CA  . LEU   B 53  ? 0.1403 0.1496 0.1296 0.0123  -0.0031 -0.0055 53  LEU   B CA  
5057 C C   . LEU   B 53  ? 0.1442 0.1402 0.1369 0.0134  0.0057  -0.0049 53  LEU   B C   
5058 O O   . LEU   B 53  ? 0.1475 0.1510 0.1588 -0.0024 0.0065  0.0041  53  LEU   B O   
5059 C CB  . LEU   B 53  ? 0.1372 0.1529 0.1527 0.0104  -0.0016 0.0141  53  LEU   B CB  
5060 C CG  . LEU   B 53  ? 0.1343 0.1674 0.1534 0.0052  -0.0010 0.0130  53  LEU   B CG  
5061 C CD1 . LEU   B 53  ? 0.1447 0.1906 0.1609 0.0165  -0.0002 0.0016  53  LEU   B CD1 
5062 C CD2 . LEU   B 53  ? 0.1485 0.1966 0.1748 -0.0047 -0.0071 -0.0144 53  LEU   B CD2 
5074 N N   . ASN   B 54  ? 0.1411 0.1302 0.1361 0.0082  -0.0089 0.0008  54  ASN   B N   
5075 C CA  . ASN   B 54  ? 0.1408 0.1486 0.1382 0.0104  -0.0096 -0.0104 54  ASN   B CA  
5076 C C   . ASN   B 54  ? 0.1403 0.1540 0.1600 0.0033  -0.0010 -0.0092 54  ASN   B C   
5077 O O   . ASN   B 54  ? 0.1352 0.1546 0.1665 0.0005  -0.0007 -0.0069 54  ASN   B O   
5078 C CB  . ASN   B 54  ? 0.1439 0.1616 0.1584 0.0112  -0.0003 -0.0068 54  ASN   B CB  
5079 C CG  . ASN   B 54  ? 0.1478 0.1710 0.1539 0.0069  -0.0093 0.0036  54  ASN   B CG  
5080 O OD1 . ASN   B 54  ? 0.1413 0.1689 0.1770 0.0022  -0.0118 -0.0142 54  ASN   B OD1 
5081 N ND2 . ASN   B 54  ? 0.1638 0.1857 0.1842 0.0066  -0.0297 0.0161  54  ASN   B ND2 
5088 N N   . LYS   B 55  ? 0.1380 0.1567 0.1838 0.0133  -0.0017 -0.0016 55  LYS   B N   
5089 C CA  . LYS   B 55  ? 0.1497 0.1697 0.1985 0.0200  -0.0013 -0.0069 55  LYS   B CA  
5090 C C   . LYS   B 55  ? 0.1415 0.1693 0.2014 0.0157  0.0032  -0.0131 55  LYS   B C   
5091 O O   . LYS   B 55  ? 0.1418 0.1817 0.2113 0.0126  0.0083  -0.0106 55  LYS   B O   
5092 C CB  . LYS   B 55  ? 0.1613 0.1800 0.2331 0.0385  0.0131  -0.0024 55  LYS   B CB  
5093 C CG  . LYS   B 55  ? 0.1992 0.2099 0.3120 0.0443  0.0226  0.0130  55  LYS   B CG  
5094 C CD  . LYS   B 55  ? 0.2380 0.2402 0.3886 0.0506  0.0380  0.0273  55  LYS   B CD  
5095 C CE  . LYS   B 55  ? 0.2662 0.2655 0.4591 0.0474  0.0507  0.0406  55  LYS   B CE  
5096 N NZ  . LYS   B 55  ? 0.2718 0.2854 0.4958 0.0459  0.0381  0.0563  55  LYS   B NZ  
5110 N N   . ALA   B 56  ? 0.1432 0.1699 0.1847 0.0135  0.0041  -0.0153 56  ALA   B N   
5111 C CA  . ALA   B 56  ? 0.1551 0.1849 0.1734 0.0087  0.0070  -0.0083 56  ALA   B CA  
5112 C C   . ALA   B 56  ? 0.1506 0.1798 0.1654 0.0075  0.0127  -0.0047 56  ALA   B C   
5113 O O   . ALA   B 56  ? 0.1639 0.1872 0.1874 0.0045  0.0255  -0.0026 56  ALA   B O   
5114 C CB  . ALA   B 56  ? 0.1718 0.2004 0.1751 -0.0131 0.0102  -0.0130 56  ALA   B CB  
5120 N N   . THR   B 57  ? 0.1457 0.1720 0.1720 0.0038  0.0172  -0.0061 57  THR   B N   
5121 C CA  . THR   B 57  ? 0.1573 0.1702 0.1722 -0.0047 0.0219  -0.0049 57  THR   B CA  
5122 C C   . THR   B 57  ? 0.1552 0.1807 0.1956 -0.0086 0.0215  -0.0113 57  THR   B C   
5123 O O   . THR   B 57  ? 0.1618 0.1798 0.1980 -0.0173 0.0137  -0.0097 57  THR   B O   
5124 C CB  . THR   B 57  ? 0.1655 0.1543 0.1511 -0.0050 0.0120  0.0042  57  THR   B CB  
5125 O OG1 . THR   B 57  ? 0.1517 0.1501 0.1728 -0.0022 0.0079  0.0007  57  THR   B OG1 
5126 C CG2 . THR   B 57  ? 0.1555 0.1614 0.1579 0.0009  0.0190  0.0055  57  THR   B CG2 
5134 N N   . ASN   B 58  ? 0.1437 0.2016 0.2242 -0.0122 0.0109  -0.0291 58  ASN   B N   
5135 C CA  . ASN   B 58  ? 0.1576 0.2404 0.2564 -0.0220 0.0365  -0.0265 58  ASN   B CA  
5136 C C   . ASN   B 58  ? 0.1384 0.2174 0.2091 -0.0119 0.0004  -0.0214 58  ASN   B C   
5137 O O   . ASN   B 58  ? 0.1423 0.2328 0.2276 -0.0131 -0.0006 -0.0226 58  ASN   B O   
5138 C CB  . ASN   B 58  ? 0.2442 0.3106 0.3721 -0.0337 0.0895  -0.0165 58  ASN   B CB  
5139 C CG  . ASN   B 58  ? 0.3490 0.3813 0.5145 -0.0355 0.1190  0.0115  58  ASN   B CG  
5140 O OD1 . ASN   B 58  ? 0.3703 0.4009 0.5667 -0.0340 0.1243  0.0185  58  ASN   B OD1 
5141 N ND2 . ASN   B 58  ? 0.4347 0.4347 0.5633 -0.0375 0.1303  0.0192  58  ASN   B ND2 
5148 N N   . ASN   B 59  ? 0.1395 0.1997 0.1805 -0.0053 -0.0080 -0.0144 59  ASN   B N   
5149 C CA  . ASN   B 59  ? 0.1415 0.2003 0.1805 -0.0066 -0.0159 -0.0044 59  ASN   B CA  
5150 C C   . ASN   B 59  ? 0.1361 0.1895 0.1813 -0.0092 -0.0159 -0.0140 59  ASN   B C   
5151 O O   . ASN   B 59  ? 0.1439 0.1869 0.1785 -0.0100 -0.0146 -0.0160 59  ASN   B O   
5152 C CB  . ASN   B 59  ? 0.1499 0.2196 0.1913 0.0021  -0.0181 -0.0036 59  ASN   B CB  
5153 C CG  . ASN   B 59  ? 0.1644 0.2291 0.1981 0.0108  -0.0354 -0.0001 59  ASN   B CG  
5154 O OD1 . ASN   B 59  ? 0.1662 0.2300 0.2107 0.0102  -0.0255 0.0132  59  ASN   B OD1 
5155 N ND2 . ASN   B 59  ? 0.1765 0.2397 0.2020 0.0102  -0.0372 -0.0125 59  ASN   B ND2 
5162 N N   . ALA   B 60  ? 0.1405 0.1773 0.1775 -0.0114 -0.0090 -0.0067 60  ALA   B N   
5163 C CA  . ALA   B 60  ? 0.1518 0.1729 0.1834 -0.0218 -0.0067 -0.0011 60  ALA   B CA  
5164 C C   . ALA   B 60  ? 0.1506 0.1626 0.1579 -0.0079 -0.0050 -0.0040 60  ALA   B C   
5165 O O   . ALA   B 60  ? 0.1535 0.1638 0.1783 -0.0152 0.0000  -0.0137 60  ALA   B O   
5166 C CB  . ALA   B 60  ? 0.1655 0.1725 0.1934 -0.0223 0.0046  0.0033  60  ALA   B CB  
5172 N N   . MET   B 61  ? 0.1443 0.1492 0.1581 -0.0032 -0.0063 -0.0039 61  MET   B N   
5173 C CA  . MET   B 61  ? 0.1374 0.1442 0.1387 -0.0029 -0.0159 0.0077  61  MET   B CA  
5174 C C   . MET   B 61  ? 0.1395 0.1448 0.1445 -0.0059 -0.0173 -0.0003 61  MET   B C   
5175 O O   . MET   B 61  ? 0.1411 0.1466 0.1420 -0.0003 -0.0157 -0.0182 61  MET   B O   
5176 C CB  . MET   B 61  ? 0.1313 0.1408 0.1477 0.0037  -0.0131 -0.0014 61  MET   B CB  
5177 C CG  . MET   B 61  ? 0.1351 0.1452 0.1528 0.0030  -0.0162 -0.0032 61  MET   B CG  
5178 S SD  . MET   B 61  ? 0.1372 0.1465 0.1657 -0.0020 -0.0076 -0.0120 61  MET   B SD  
5179 C CE  . MET   B 61  ? 0.1426 0.1761 0.1744 -0.0033 -0.0133 -0.0128 61  MET   B CE  
5189 N N   . GLN   B 62  ? 0.1413 0.1485 0.1400 -0.0034 -0.0226 -0.0020 62  GLN   B N   
5190 C CA  . GLN   B 62  ? 0.1464 0.1470 0.1427 0.0041  -0.0253 -0.0038 62  GLN   B CA  
5191 C C   . GLN   B 62  ? 0.1455 0.1567 0.1443 0.0072  -0.0268 -0.0121 62  GLN   B C   
5192 O O   . GLN   B 62  ? 0.1552 0.1619 0.1484 0.0055  -0.0289 -0.0149 62  GLN   B O   
5193 C CB  . GLN   B 62  ? 0.1519 0.1531 0.1574 0.0080  -0.0124 -0.0004 62  GLN   B CB  
5194 C CG  . GLN   B 62  ? 0.1595 0.1590 0.1606 0.0114  -0.0280 -0.0043 62  GLN   B CG  
5195 C CD  . GLN   B 62  ? 0.1571 0.1552 0.1399 0.0140  -0.0320 0.0037  62  GLN   B CD  
5196 O OE1 . GLN   B 62  ? 0.1603 0.1570 0.1600 0.0105  -0.0326 -0.0073 62  GLN   B OE1 
5197 N NE2 . GLN   B 62  ? 0.1591 0.1597 0.1432 0.0120  -0.0246 -0.0102 62  GLN   B NE2 
5206 N N   . VAL   B 63  ? 0.1446 0.1605 0.1696 -0.0027 -0.0296 -0.0149 63  VAL   B N   
5207 C CA  . VAL   B 63  ? 0.1559 0.1678 0.1751 -0.0039 -0.0282 -0.0124 63  VAL   B CA  
5208 C C   . VAL   B 63  ? 0.1581 0.1526 0.1640 -0.0099 -0.0279 -0.0217 63  VAL   B C   
5209 O O   . VAL   B 63  ? 0.1640 0.1534 0.1733 -0.0016 -0.0439 -0.0163 63  VAL   B O   
5210 C CB  . VAL   B 63  ? 0.1544 0.1792 0.2027 -0.0071 -0.0268 -0.0103 63  VAL   B CB  
5211 C CG1 . VAL   B 63  ? 0.1620 0.1829 0.2212 -0.0217 -0.0133 -0.0111 63  VAL   B CG1 
5212 C CG2 . VAL   B 63  ? 0.1531 0.1968 0.2153 -0.0050 -0.0327 -0.0291 63  VAL   B CG2 
5222 N N   . GLU   B 64  ? 0.1551 0.1440 0.1525 -0.0052 -0.0283 -0.0155 64  GLU   B N   
5223 C CA  . GLU   B 64  ? 0.1497 0.1385 0.1497 -0.0063 -0.0339 -0.0102 64  GLU   B CA  
5224 C C   . GLU   B 64  ? 0.1512 0.1389 0.1453 -0.0011 -0.0310 -0.0158 64  GLU   B C   
5225 O O   . GLU   B 64  ? 0.1663 0.1476 0.1463 -0.0028 -0.0308 -0.0209 64  GLU   B O   
5226 C CB  . GLU   B 64  ? 0.1478 0.1467 0.1504 -0.0102 -0.0217 -0.0019 64  GLU   B CB  
5227 C CG  . GLU   B 64  ? 0.1568 0.1510 0.1497 -0.0163 -0.0194 -0.0111 64  GLU   B CG  
5228 C CD  . GLU   B 64  ? 0.1626 0.1628 0.1702 -0.0211 -0.0292 -0.0039 64  GLU   B CD  
5229 O OE1 . GLU   B 64  ? 0.1660 0.1759 0.1724 -0.0257 -0.0188 -0.0307 64  GLU   B OE1 
5230 O OE2 . GLU   B 64  ? 0.1810 0.1767 0.1750 -0.0259 -0.0464 -0.0109 64  GLU   B OE2 
5237 N N   . SER   B 65  ? 0.1508 0.1363 0.1430 -0.0016 -0.0249 -0.0211 65  SER   B N   
5238 C CA  . SER   B 65  ? 0.1472 0.1428 0.1369 0.0013  -0.0180 -0.0121 65  SER   B CA  
5239 C C   . SER   B 65  ? 0.1499 0.1412 0.1383 0.0039  -0.0273 -0.0149 65  SER   B C   
5240 O O   . SER   B 65  ? 0.1552 0.1520 0.1407 0.0067  -0.0215 -0.0196 65  SER   B O   
5241 C CB  . SER   B 65  ? 0.1552 0.1465 0.1489 -0.0124 -0.0213 -0.0124 65  SER   B CB  
5242 O OG  . SER   B 65  ? 0.1564 0.1417 0.1443 -0.0030 -0.0172 -0.0184 65  SER   B OG  
5248 N N   . ASP   B 66  ? 0.1646 0.1516 0.1367 0.0044  -0.0388 -0.0160 66  ASP   B N   
5249 C CA  . ASP   B 66  ? 0.1788 0.1563 0.1339 0.0087  -0.0345 -0.0075 66  ASP   B CA  
5250 C C   . ASP   B 66  ? 0.1736 0.1557 0.1281 0.0011  -0.0216 -0.0127 66  ASP   B C   
5251 O O   . ASP   B 66  ? 0.1766 0.1601 0.1532 0.0053  -0.0292 -0.0214 66  ASP   B O   
5252 C CB  . ASP   B 66  ? 0.1918 0.1651 0.1599 0.0159  -0.0560 -0.0172 66  ASP   B CB  
5253 C CG  . ASP   B 66  ? 0.2125 0.1800 0.1831 0.0251  -0.0651 -0.0132 66  ASP   B CG  
5254 O OD1 . ASP   B 66  ? 0.2364 0.1697 0.1935 0.0198  -0.0480 -0.0119 66  ASP   B OD1 
5255 O OD2 . ASP   B 66  ? 0.2214 0.2066 0.2587 0.0483  -0.0626 -0.0077 66  ASP   B OD2 
5260 N N   . ASP   B 67  ? 0.1666 0.1540 0.1314 -0.0016 -0.0284 -0.0230 67  ASP   B N   
5261 C CA  . ASP   B 67  ? 0.1794 0.1493 0.1571 -0.0025 -0.0246 -0.0144 67  ASP   B CA  
5262 C C   . ASP   B 67  ? 0.1790 0.1499 0.1558 0.0049  -0.0210 -0.0169 67  ASP   B C   
5263 O O   . ASP   B 67  ? 0.1840 0.1571 0.1701 0.0020  -0.0174 -0.0282 67  ASP   B O   
5264 C CB  . ASP   B 67  ? 0.1968 0.1563 0.1711 -0.0082 -0.0422 -0.0129 67  ASP   B CB  
5265 C CG  . ASP   B 67  ? 0.2353 0.1605 0.1762 -0.0074 -0.0637 -0.0142 67  ASP   B CG  
5266 O OD1 . ASP   B 67  ? 0.2543 0.1653 0.2026 -0.0111 -0.0562 -0.0142 67  ASP   B OD1 
5267 O OD2 . ASP   B 67  ? 0.2539 0.1651 0.1910 0.0113  -0.0615 -0.0090 67  ASP   B OD2 
5272 N N   . TYR   B 68  ? 0.1723 0.1551 0.1468 0.0017  -0.0354 -0.0244 68  TYR   B N   
5273 C CA  . TYR   B 68  ? 0.1675 0.1646 0.1656 0.0087  -0.0370 -0.0338 68  TYR   B CA  
5274 C C   . TYR   B 68  ? 0.1624 0.1529 0.1679 0.0051  -0.0267 -0.0394 68  TYR   B C   
5275 O O   . TYR   B 68  ? 0.1703 0.1639 0.1719 0.0115  -0.0276 -0.0469 68  TYR   B O   
5276 C CB  . TYR   B 68  ? 0.1702 0.1837 0.1701 0.0167  -0.0443 -0.0381 68  TYR   B CB  
5277 C CG  . TYR   B 68  ? 0.1873 0.2001 0.1791 0.0233  -0.0390 -0.0543 68  TYR   B CG  
5278 C CD1 . TYR   B 68  ? 0.1867 0.1998 0.2002 0.0028  -0.0366 -0.0572 68  TYR   B CD1 
5279 C CD2 . TYR   B 68  ? 0.1999 0.2149 0.1884 0.0263  -0.0501 -0.0465 68  TYR   B CD2 
5280 C CE1 . TYR   B 68  ? 0.1970 0.2135 0.2212 0.0074  -0.0263 -0.0503 68  TYR   B CE1 
5281 C CE2 . TYR   B 68  ? 0.1986 0.2157 0.1928 0.0239  -0.0326 -0.0597 68  TYR   B CE2 
5282 C CZ  . TYR   B 68  ? 0.1915 0.2181 0.2123 0.0104  -0.0293 -0.0534 68  TYR   B CZ  
5283 O OH  . TYR   B 68  ? 0.1831 0.2316 0.2387 0.0080  -0.0177 -0.0274 68  TYR   B OH  
5293 N N   . ILE   B 69  ? 0.1669 0.1449 0.1603 0.0070  -0.0299 -0.0280 69  ILE   B N   
5294 C CA  . ILE   B 69  ? 0.1671 0.1564 0.1604 0.0044  -0.0238 -0.0325 69  ILE   B CA  
5295 C C   . ILE   B 69  ? 0.1695 0.1532 0.1490 0.0124  -0.0309 -0.0232 69  ILE   B C   
5296 O O   . ILE   B 69  ? 0.1747 0.1630 0.1580 0.0075  -0.0232 -0.0299 69  ILE   B O   
5297 C CB  . ILE   B 69  ? 0.1709 0.1578 0.1770 0.0015  -0.0063 -0.0267 69  ILE   B CB  
5298 C CG1 . ILE   B 69  ? 0.1733 0.1643 0.1919 -0.0046 0.0067  -0.0251 69  ILE   B CG1 
5299 C CG2 . ILE   B 69  ? 0.1754 0.1721 0.1993 0.0052  -0.0078 -0.0187 69  ILE   B CG2 
5300 C CD1 . ILE   B 69  ? 0.1739 0.1725 0.2030 -0.0135 0.0008  -0.0416 69  ILE   B CD1 
5312 N N   . ALA   B 70  ? 0.1660 0.1558 0.1447 0.0117  -0.0313 -0.0197 70  ALA   B N   
5313 C CA  . ALA   B 70  ? 0.1676 0.1605 0.1370 0.0062  -0.0302 -0.0198 70  ALA   B CA  
5314 C C   . ALA   B 70  ? 0.1742 0.1570 0.1494 -0.0021 -0.0369 -0.0338 70  ALA   B C   
5315 O O   . ALA   B 70  ? 0.1896 0.1583 0.1632 0.0038  -0.0356 -0.0362 70  ALA   B O   
5316 C CB  . ALA   B 70  ? 0.1685 0.1746 0.1497 0.0073  -0.0288 -0.0300 70  ALA   B CB  
5322 N N   . THR   B 71  ? 0.1791 0.1568 0.1596 0.0045  -0.0490 -0.0259 71  THR   B N   
5323 C CA  . THR   B 71  ? 0.1954 0.1577 0.1892 0.0112  -0.0643 -0.0288 71  THR   B CA  
5324 C C   . THR   B 71  ? 0.1881 0.1597 0.2162 0.0269  -0.0628 -0.0454 71  THR   B C   
5325 O O   . THR   B 71  ? 0.1965 0.1701 0.2502 0.0297  -0.0461 -0.0593 71  THR   B O   
5326 C CB  . THR   B 71  ? 0.2208 0.1796 0.2143 0.0043  -0.0729 -0.0178 71  THR   B CB  
5327 O OG1 . THR   B 71  ? 0.2311 0.2070 0.2441 -0.0163 -0.0672 0.0095  71  THR   B OG1 
5328 C CG2 . THR   B 71  ? 0.2406 0.1776 0.2323 0.0121  -0.0601 -0.0012 71  THR   B CG2 
5336 N N   . ASN   B 72  ? 0.1804 0.1657 0.2083 0.0173  -0.0604 -0.0577 72  ASN   B N   
5337 C CA  . ASN   B 72  ? 0.1782 0.1831 0.2137 0.0230  -0.0411 -0.0732 72  ASN   B CA  
5338 C C   . ASN   B 72  ? 0.1767 0.1933 0.2215 0.0159  -0.0240 -0.0663 72  ASN   B C   
5339 O O   . ASN   B 72  ? 0.1729 0.2090 0.2488 0.0139  -0.0174 -0.0616 72  ASN   B O   
5340 C CB  . ASN   B 72  ? 0.1839 0.1957 0.2359 0.0112  -0.0556 -0.0608 72  ASN   B CB  
5341 C CG  . ASN   B 72  ? 0.2023 0.2072 0.2395 0.0260  -0.0656 -0.0367 72  ASN   B CG  
5342 O OD1 . ASN   B 72  ? 0.2289 0.2218 0.2423 0.0098  -0.0468 -0.0405 72  ASN   B OD1 
5343 N ND2 . ASN   B 72  ? 0.2087 0.2160 0.2818 0.0428  -0.0596 -0.0096 72  ASN   B ND2 
5350 N N   . GLY   B 73  ? 0.1807 0.1897 0.1974 0.0143  -0.0291 -0.0648 73  GLY   B N   
5351 C CA  . GLY   B 73  ? 0.1753 0.1994 0.1663 0.0096  -0.0176 -0.0559 73  GLY   B CA  
5352 C C   . GLY   B 73  ? 0.1700 0.1917 0.1318 0.0108  -0.0245 -0.0447 73  GLY   B C   
5353 O O   . GLY   B 73  ? 0.1672 0.1805 0.1549 0.0103  -0.0212 -0.0285 73  GLY   B O   
5357 N N   . PRO   B 74  ? 0.1734 0.1994 0.1308 0.0080  -0.0212 -0.0325 74  PRO   B N   
5358 C CA  . PRO   B 74  ? 0.1685 0.1991 0.1155 0.0119  -0.0134 -0.0195 74  PRO   B CA  
5359 C C   . PRO   B 74  ? 0.1580 0.1820 0.1214 0.0099  -0.0088 -0.0211 74  PRO   B C   
5360 O O   . PRO   B 74  ? 0.1596 0.1879 0.1727 0.0117  -0.0070 -0.0282 74  PRO   B O   
5361 C CB  . PRO   B 74  ? 0.1809 0.2197 0.1353 0.0063  -0.0133 -0.0129 74  PRO   B CB  
5362 C CG  . PRO   B 74  ? 0.2090 0.2321 0.1534 -0.0000 -0.0125 -0.0066 74  PRO   B CG  
5363 C CD  . PRO   B 74  ? 0.1996 0.2246 0.1488 0.0031  -0.0037 -0.0182 74  PRO   B CD  
5371 N N   . LEU   B 75  ? 0.1596 0.1729 0.1157 0.0110  -0.0167 -0.0213 75  LEU   B N   
5372 C CA  . LEU   B 75  ? 0.1592 0.1760 0.1163 0.0050  -0.0145 -0.0032 75  LEU   B CA  
5373 C C   . LEU   B 75  ? 0.1688 0.1905 0.1218 0.0071  -0.0085 0.0002  75  LEU   B C   
5374 O O   . LEU   B 75  ? 0.1879 0.2003 0.1418 0.0031  -0.0009 0.0039  75  LEU   B O   
5375 C CB  . LEU   B 75  ? 0.1613 0.1750 0.1035 -0.0080 -0.0168 0.0084  75  LEU   B CB  
5376 C CG  . LEU   B 75  ? 0.2007 0.1947 0.1272 -0.0303 -0.0104 0.0020  75  LEU   B CG  
5377 C CD1 . LEU   B 75  ? 0.2332 0.2158 0.1449 -0.0371 0.0161  -0.0052 75  LEU   B CD1 
5378 C CD2 . LEU   B 75  ? 0.2442 0.2158 0.2049 -0.0159 -0.0013 0.0074  75  LEU   B CD2 
5390 N N   . LYS   B 76  ? 0.1657 0.2100 0.1540 0.0025  0.0058  0.0067  76  LYS   B N   
5391 C CA  . LYS   B 76  ? 0.1810 0.2168 0.1761 -0.0055 0.0232  -0.0008 76  LYS   B CA  
5392 C C   . LYS   B 76  ? 0.1796 0.2029 0.1486 0.0046  0.0155  0.0241  76  LYS   B C   
5393 O O   . LYS   B 76  ? 0.1878 0.1786 0.1511 -0.0006 0.0116  0.0212  76  LYS   B O   
5394 C CB  . LYS   B 76  ? 0.1968 0.2228 0.2398 -0.0107 0.0475  -0.0346 76  LYS   B CB  
5395 C CG  . LYS   B 76  ? 0.1998 0.2418 0.2814 -0.0044 0.0346  -0.0474 76  LYS   B CG  
5396 C CD  . LYS   B 76  ? 0.1978 0.2454 0.3232 0.0022  0.0265  -0.0623 76  LYS   B CD  
5397 C CE  . LYS   B 76  ? 0.2021 0.2559 0.3764 0.0047  0.0110  -0.0707 76  LYS   B CE  
5398 N NZ  . LYS   B 76  ? 0.1988 0.2617 0.3925 0.0049  -0.0052 -0.0850 76  LYS   B NZ  
5412 N N   . VAL   B 77  ? 0.1877 0.2163 0.1516 0.0136  0.0193  0.0235  77  VAL   B N   
5413 C CA  . VAL   B 77  ? 0.1890 0.2089 0.1600 0.0170  0.0263  0.0556  77  VAL   B CA  
5414 C C   . VAL   B 77  ? 0.1712 0.1811 0.1577 0.0194  0.0392  0.0405  77  VAL   B C   
5415 O O   . VAL   B 77  ? 0.1715 0.1762 0.1663 0.0192  0.0428  0.0284  77  VAL   B O   
5416 C CB  . VAL   B 77  ? 0.2006 0.2226 0.2073 0.0163  0.0391  0.0715  77  VAL   B CB  
5417 C CG1 . VAL   B 77  ? 0.2040 0.2158 0.2399 0.0063  0.0378  0.0958  77  VAL   B CG1 
5418 C CG2 . VAL   B 77  ? 0.2093 0.2377 0.2261 0.0160  0.0224  0.0742  77  VAL   B CG2 
5428 N N   . GLY   B 78  ? 0.1631 0.1667 0.1646 0.0135  0.0293  0.0338  78  GLY   B N   
5429 C CA  . GLY   B 78  ? 0.1618 0.1645 0.1550 0.0140  0.0255  0.0249  78  GLY   B CA  
5430 C C   . GLY   B 78  ? 0.1512 0.1548 0.1559 0.0130  0.0262  0.0245  78  GLY   B C   
5431 O O   . GLY   B 78  ? 0.1517 0.1480 0.1706 0.0186  0.0241  0.0268  78  GLY   B O   
5435 N N   . GLY   B 79  ? 0.1466 0.1534 0.1629 0.0141  0.0247  0.0160  79  GLY   B N   
5436 C CA  . GLY   B 79  ? 0.1451 0.1513 0.1513 0.0143  0.0111  0.0172  79  GLY   B CA  
5437 C C   . GLY   B 79  ? 0.1376 0.1396 0.1463 0.0176  0.0113  0.0138  79  GLY   B C   
5438 O O   . GLY   B 79  ? 0.1452 0.1411 0.1648 0.0146  0.0195  0.0244  79  GLY   B O   
5442 N N   . SER   B 80  ? 0.1386 0.1347 0.1470 0.0116  0.0154  0.0126  80  SER   B N   
5443 C CA  . SER   B 80  ? 0.1324 0.1318 0.1444 0.0050  0.0054  0.0062  80  SER   B CA  
5444 C C   . SER   B 80  ? 0.1372 0.1249 0.1394 0.0066  0.0019  -0.0007 80  SER   B C   
5445 O O   . SER   B 80  ? 0.1512 0.1348 0.1663 0.0111  0.0056  -0.0014 80  SER   B O   
5446 C CB  . SER   B 80  ? 0.1398 0.1353 0.1543 -0.0033 0.0030  0.0043  80  SER   B CB  
5447 O OG  . SER   B 80  ? 0.1443 0.1527 0.1733 -0.0029 -0.0176 0.0084  80  SER   B OG  
5453 N N   . CYS   B 81  ? 0.1353 0.1235 0.1455 0.0011  -0.0038 -0.0013 81  CYS   B N   
5454 C CA  . CYS   B 81  ? 0.1426 0.1208 0.1558 0.0010  -0.0122 -0.0017 81  CYS   B CA  
5455 C C   . CYS   B 81  ? 0.1366 0.1189 0.1257 -0.0016 -0.0095 -0.0007 81  CYS   B C   
5456 O O   . CYS   B 81  ? 0.1547 0.1173 0.1566 0.0090  -0.0011 -0.0002 81  CYS   B O   
5457 C CB  . CYS   B 81  ? 0.1526 0.1313 0.1549 -0.0072 -0.0152 -0.0056 81  CYS   B CB  
5458 S SG  . CYS   B 81  ? 0.1560 0.1505 0.1426 -0.0026 -0.0256 -0.0111 81  CYS   B SG  
5464 N N   . VAL   B 82  ? 0.1410 0.1171 0.1474 -0.0000 -0.0118 0.0023  82  VAL   B N   
5465 C CA  . VAL   B 82  ? 0.1465 0.1191 0.1370 -0.0034 -0.0093 0.0114  82  VAL   B CA  
5466 C C   . VAL   B 82  ? 0.1497 0.1157 0.1452 -0.0026 -0.0110 0.0052  82  VAL   B C   
5467 O O   . VAL   B 82  ? 0.1587 0.1152 0.1811 -0.0026 -0.0090 -0.0141 82  VAL   B O   
5468 C CB  . VAL   B 82  ? 0.1523 0.1399 0.1517 -0.0039 -0.0139 0.0074  82  VAL   B CB  
5469 C CG1 . VAL   B 82  ? 0.1660 0.1632 0.1650 -0.0000 -0.0160 0.0221  82  VAL   B CG1 
5470 C CG2 . VAL   B 82  ? 0.1528 0.1585 0.1750 -0.0023 -0.0329 0.0196  82  VAL   B CG2 
5480 N N   . LEU   B 83  ? 0.1426 0.1142 0.1442 -0.0106 -0.0266 -0.0060 83  LEU   B N   
5481 C CA  . LEU   B 83  ? 0.1413 0.1252 0.1319 -0.0092 -0.0233 -0.0069 83  LEU   B CA  
5482 C C   . LEU   B 83  ? 0.1432 0.1198 0.1370 -0.0140 -0.0239 0.0054  83  LEU   B C   
5483 O O   . LEU   B 83  ? 0.1441 0.1353 0.1245 -0.0232 -0.0234 0.0014  83  LEU   B O   
5484 C CB  . LEU   B 83  ? 0.1482 0.1351 0.1334 -0.0075 -0.0247 -0.0080 83  LEU   B CB  
5485 C CG  . LEU   B 83  ? 0.1651 0.1562 0.1525 -0.0081 -0.0165 -0.0092 83  LEU   B CG  
5486 C CD1 . LEU   B 83  ? 0.1778 0.1579 0.1460 -0.0136 -0.0246 0.0027  83  LEU   B CD1 
5487 C CD2 . LEU   B 83  ? 0.1874 0.1579 0.1694 -0.0040 -0.0220 -0.0274 83  LEU   B CD2 
5499 N N   . SER   B 84  ? 0.1425 0.1387 0.1556 -0.0227 -0.0213 0.0054  84  SER   B N   
5500 C CA  . SER   B 84  ? 0.1452 0.1510 0.1461 -0.0216 -0.0151 0.0118  84  SER   B CA  
5501 C C   . SER   B 84  ? 0.1367 0.1664 0.1034 -0.0224 -0.0180 0.0159  84  SER   B C   
5502 O O   . SER   B 84  ? 0.1503 0.1545 0.1163 -0.0214 -0.0127 -0.0009 84  SER   B O   
5503 C CB  . SER   B 84  ? 0.1662 0.1541 0.1882 -0.0220 0.0079  0.0128  84  SER   B CB  
5504 O OG  . SER   B 84  ? 0.1645 0.1701 0.2309 -0.0311 -0.0019 0.0172  84  SER   B OG  
5510 N N   . GLY   B 85  ? 0.1417 0.1864 0.1277 -0.0257 -0.0115 0.0145  85  GLY   B N   
5511 C CA  . GLY   B 85  ? 0.1470 0.1960 0.1395 -0.0415 0.0014  -0.0089 85  GLY   B CA  
5512 C C   . GLY   B 85  ? 0.1457 0.1797 0.1233 -0.0449 -0.0054 0.0029  85  GLY   B C   
5513 O O   . GLY   B 85  ? 0.1578 0.1785 0.1398 -0.0602 0.0111  -0.0160 85  GLY   B O   
5517 N N   . HIS   B 86  ? 0.1402 0.1661 0.1552 -0.0356 -0.0176 0.0153  86  HIS   B N   
5518 C CA  . HIS   B 86  ? 0.1441 0.1607 0.1416 -0.0349 -0.0179 0.0154  86  HIS   B CA  
5519 C C   . HIS   B 86  ? 0.1488 0.1742 0.1315 -0.0451 -0.0083 0.0254  86  HIS   B C   
5520 O O   . HIS   B 86  ? 0.1614 0.1881 0.1373 -0.0392 0.0088  0.0250  86  HIS   B O   
5521 C CB  . HIS   B 86  ? 0.1518 0.1730 0.1553 -0.0159 -0.0180 0.0058  86  HIS   B CB  
5522 C CG  . HIS   B 86  ? 0.1519 0.1824 0.1476 -0.0095 -0.0217 0.0045  86  HIS   B CG  
5523 N ND1 . HIS   B 86  ? 0.1616 0.2020 0.1646 -0.0246 -0.0188 -0.0115 86  HIS   B ND1 
5524 C CD2 . HIS   B 86  ? 0.1592 0.1816 0.1474 -0.0084 -0.0133 -0.0015 86  HIS   B CD2 
5525 C CE1 . HIS   B 86  ? 0.1690 0.1973 0.1591 -0.0131 -0.0141 -0.0287 86  HIS   B CE1 
5526 N NE2 . HIS   B 86  ? 0.1698 0.1855 0.1456 0.0008  -0.0134 -0.0073 86  HIS   B NE2 
5534 N N   . ASN   B 87  ? 0.1456 0.1756 0.1560 -0.0363 0.0076  0.0135  87  ASN   B N   
5535 C CA  . ASN   B 87  ? 0.1613 0.1931 0.1573 -0.0360 0.0269  0.0132  87  ASN   B CA  
5536 C C   . ASN   B 87  ? 0.1771 0.1794 0.1268 -0.0331 0.0317  0.0102  87  ASN   B C   
5537 O O   . ASN   B 87  ? 0.2065 0.1875 0.1650 -0.0246 0.0536  0.0034  87  ASN   B O   
5538 C CB  . ASN   B 87  ? 0.1600 0.2269 0.1912 -0.0330 0.0376  0.0123  87  ASN   B CB  
5539 C CG  . ASN   B 87  ? 0.1679 0.2402 0.1922 0.0010  0.0387  0.0233  87  ASN   B CG  
5540 O OD1 . ASN   B 87  ? 0.1662 0.2212 0.1759 0.0120  0.0455  0.0259  87  ASN   B OD1 
5541 N ND2 . ASN   B 87  ? 0.2038 0.2494 0.2382 0.0087  0.0469  0.0202  87  ASN   B ND2 
5548 N N   . LEU   B 88  ? 0.1618 0.1703 0.1239 -0.0385 0.0181  0.0045  88  LEU   B N   
5549 C CA  . LEU   B 88  ? 0.1785 0.1607 0.1344 -0.0397 0.0003  -0.0005 88  LEU   B CA  
5550 C C   . LEU   B 88  ? 0.1769 0.1528 0.1279 -0.0492 -0.0024 0.0020  88  LEU   B C   
5551 O O   . LEU   B 88  ? 0.1979 0.1589 0.1663 -0.0282 -0.0285 -0.0127 88  LEU   B O   
5552 C CB  . LEU   B 88  ? 0.1938 0.1693 0.1484 -0.0543 -0.0220 0.0141  88  LEU   B CB  
5553 C CG  . LEU   B 88  ? 0.2345 0.1988 0.1723 -0.0436 -0.0342 0.0256  88  LEU   B CG  
5554 C CD1 . LEU   B 88  ? 0.2434 0.2308 0.1879 -0.0535 -0.0267 0.0425  88  LEU   B CD1 
5555 C CD2 . LEU   B 88  ? 0.2750 0.2234 0.2310 0.0009  -0.0495 0.0093  88  LEU   B CD2 
5567 N N   . ALA   B 89  ? 0.1584 0.1535 0.1266 -0.0493 0.0170  -0.0016 89  ALA   B N   
5568 C CA  . ALA   B 89  ? 0.1581 0.1504 0.1108 -0.0437 0.0000  0.0077  89  ALA   B CA  
5569 C C   . ALA   B 89  ? 0.1708 0.1486 0.1146 -0.0468 0.0116  0.0029  89  ALA   B C   
5570 O O   . ALA   B 89  ? 0.1499 0.1608 0.1515 -0.0454 0.0173  -0.0303 89  ALA   B O   
5571 C CB  . ALA   B 89  ? 0.1451 0.1502 0.1324 -0.0396 -0.0029 0.0181  89  ALA   B CB  
5577 N N   . LYS   B 90  ? 0.2041 0.1370 0.1295 -0.0483 -0.0124 0.0140  90  LYS   B N   
5578 C CA  . LYS   B 90  ? 0.2151 0.1368 0.1222 -0.0464 -0.0190 0.0137  90  LYS   B CA  
5579 C C   . LYS   B 90  ? 0.1898 0.1302 0.1279 -0.0403 -0.0094 0.0030  90  LYS   B C   
5580 O O   . LYS   B 90  ? 0.1950 0.1459 0.1424 -0.0538 -0.0082 0.0033  90  LYS   B O   
5581 C CB  . LYS   B 90  ? 0.2290 0.1423 0.1508 -0.0404 -0.0044 0.0221  90  LYS   B CB  
5582 C CG  . LYS   B 90  ? 0.2261 0.1543 0.1617 -0.0302 0.0233  0.0126  90  LYS   B CG  
5583 C CD  . LYS   B 90  ? 0.2441 0.1742 0.2246 -0.0159 0.0490  -0.0037 90  LYS   B CD  
5584 C CE  . LYS   B 90  ? 0.2585 0.1923 0.2815 -0.0182 0.0665  -0.0166 90  LYS   B CE  
5585 N NZ  . LYS   B 90  ? 0.2741 0.1888 0.2779 -0.0317 0.0884  -0.0140 90  LYS   B NZ  
5599 N N   . HIS   B 91  ? 0.1629 0.1217 0.1169 -0.0319 -0.0153 0.0099  91  HIS   B N   
5600 C CA  . HIS   B 91  ? 0.1536 0.1271 0.1279 -0.0249 -0.0124 0.0056  91  HIS   B CA  
5601 C C   . HIS   B 91  ? 0.1411 0.1243 0.1083 -0.0248 -0.0133 0.0003  91  HIS   B C   
5602 O O   . HIS   B 91  ? 0.1567 0.1326 0.1133 -0.0306 -0.0171 0.0018  91  HIS   B O   
5603 C CB  . HIS   B 91  ? 0.1736 0.1277 0.1704 -0.0105 -0.0167 0.0160  91  HIS   B CB  
5604 C CG  . HIS   B 91  ? 0.2111 0.1485 0.2323 -0.0007 0.0143  0.0294  91  HIS   B CG  
5605 N ND1 . HIS   B 91  ? 0.2424 0.1519 0.2937 -0.0038 0.0250  0.0080  91  HIS   B ND1 
5606 C CD2 . HIS   B 91  ? 0.2210 0.1730 0.2817 0.0147  -0.0008 0.0582  91  HIS   B CD2 
5607 C CE1 . HIS   B 91  ? 0.2444 0.1620 0.3147 0.0122  0.0275  0.0167  91  HIS   B CE1 
5608 N NE2 . HIS   B 91  ? 0.2385 0.1796 0.3116 0.0226  0.0156  0.0543  91  HIS   B NE2 
5616 N N   . CYS   B 92  ? 0.1345 0.1243 0.1103 -0.0249 -0.0083 -0.0003 92  CYS   B N   
5617 C CA  . CYS   B 92  ? 0.1365 0.1234 0.1105 -0.0175 -0.0075 0.0010  92  CYS   B CA  
5618 C C   . CYS   B 92  ? 0.1357 0.1152 0.1079 -0.0093 -0.0119 0.0064  92  CYS   B C   
5619 O O   . CYS   B 92  ? 0.1433 0.1250 0.1257 -0.0141 -0.0067 -0.0010 92  CYS   B O   
5620 C CB  . CYS   B 92  ? 0.1397 0.1301 0.1196 -0.0161 -0.0086 -0.0001 92  CYS   B CB  
5621 S SG  . CYS   B 92  ? 0.1380 0.1305 0.1331 -0.0112 -0.0129 0.0062  92  CYS   B SG  
5627 N N   . LEU   B 93  ? 0.1280 0.1174 0.1046 -0.0131 -0.0100 -0.0002 93  LEU   B N   
5628 C CA  . LEU   B 93  ? 0.1301 0.1174 0.1107 -0.0034 -0.0116 0.0014  93  LEU   B CA  
5629 C C   . LEU   B 93  ? 0.1234 0.1164 0.1072 -0.0012 -0.0095 0.0081  93  LEU   B C   
5630 O O   . LEU   B 93  ? 0.1326 0.1149 0.1282 -0.0058 -0.0083 -0.0029 93  LEU   B O   
5631 C CB  . LEU   B 93  ? 0.1357 0.1155 0.1270 -0.0020 -0.0120 0.0056  93  LEU   B CB  
5632 C CG  . LEU   B 93  ? 0.1274 0.1321 0.1453 -0.0078 -0.0072 0.0184  93  LEU   B CG  
5633 C CD1 . LEU   B 93  ? 0.1323 0.1413 0.1489 0.0037  -0.0030 -0.0004 93  LEU   B CD1 
5634 C CD2 . LEU   B 93  ? 0.1329 0.1319 0.1552 -0.0062 -0.0151 0.0063  93  LEU   B CD2 
5646 N N   . HIS   B 94  ? 0.1270 0.1159 0.1097 -0.0055 -0.0124 0.0132  94  HIS   B N   
5647 C CA  . HIS   B 94  ? 0.1301 0.1152 0.1102 0.0003  -0.0080 0.0081  94  HIS   B CA  
5648 C C   . HIS   B 94  ? 0.1322 0.1162 0.1244 0.0035  -0.0052 0.0206  94  HIS   B C   
5649 O O   . HIS   B 94  ? 0.1259 0.1229 0.1725 0.0022  0.0101  -0.0012 94  HIS   B O   
5650 C CB  . HIS   B 94  ? 0.1322 0.1232 0.1217 -0.0000 -0.0150 0.0093  94  HIS   B CB  
5651 C CG  . HIS   B 94  ? 0.1304 0.1182 0.1204 -0.0041 -0.0223 0.0033  94  HIS   B CG  
5652 N ND1 . HIS   B 94  ? 0.1342 0.1263 0.1204 0.0008  -0.0260 0.0023  94  HIS   B ND1 
5653 C CD2 . HIS   B 94  ? 0.1339 0.1241 0.1263 -0.0007 -0.0181 0.0024  94  HIS   B CD2 
5654 C CE1 . HIS   B 94  ? 0.1330 0.1238 0.1160 -0.0068 -0.0172 0.0022  94  HIS   B CE1 
5655 N NE2 . HIS   B 94  ? 0.1332 0.1310 0.1306 -0.0163 -0.0112 -0.0013 94  HIS   B NE2 
5663 N N   . VAL   B 95  ? 0.1264 0.1156 0.1282 0.0038  -0.0039 0.0117  95  VAL   B N   
5664 C CA  . VAL   B 95  ? 0.1256 0.1255 0.1259 -0.0012 0.0027  0.0141  95  VAL   B CA  
5665 C C   . VAL   B 95  ? 0.1347 0.1263 0.1205 0.0068  0.0132  0.0103  95  VAL   B C   
5666 O O   . VAL   B 95  ? 0.1357 0.1220 0.1506 0.0120  0.0065  0.0220  95  VAL   B O   
5667 C CB  . VAL   B 95  ? 0.1328 0.1195 0.1281 0.0016  -0.0098 0.0100  95  VAL   B CB  
5668 C CG1 . VAL   B 95  ? 0.1461 0.1347 0.1495 -0.0077 -0.0012 0.0128  95  VAL   B CG1 
5669 C CG2 . VAL   B 95  ? 0.1406 0.1166 0.1328 0.0002  -0.0126 0.0008  95  VAL   B CG2 
5679 N N   . VAL   B 96  ? 0.1442 0.1219 0.1347 0.0116  0.0033  0.0186  96  VAL   B N   
5680 C CA  . VAL   B 96  ? 0.1541 0.1418 0.1293 0.0111  0.0054  0.0240  96  VAL   B CA  
5681 C C   . VAL   B 96  ? 0.1594 0.1446 0.1426 0.0106  0.0137  0.0225  96  VAL   B C   
5682 O O   . VAL   B 96  ? 0.1601 0.1478 0.1562 0.0033  0.0237  0.0101  96  VAL   B O   
5683 C CB  . VAL   B 96  ? 0.1577 0.1614 0.1276 0.0158  0.0036  0.0117  96  VAL   B CB  
5684 C CG1 . VAL   B 96  ? 0.1520 0.1720 0.1385 0.0164  0.0088  0.0083  96  VAL   B CG1 
5685 C CG2 . VAL   B 96  ? 0.1684 0.1676 0.1318 0.0086  0.0037  0.0068  96  VAL   B CG2 
5695 N N   . GLY   B 97  ? 0.1605 0.1463 0.1330 0.0097  0.0054  0.0190  97  GLY   B N   
5696 C CA  . GLY   B 97  ? 0.1832 0.1469 0.1443 0.0110  0.0063  0.0258  97  GLY   B CA  
5697 C C   . GLY   B 97  ? 0.2093 0.1566 0.1579 0.0252  0.0180  0.0264  97  GLY   B C   
5698 O O   . GLY   B 97  ? 0.2283 0.1636 0.1538 0.0187  0.0129  0.0142  97  GLY   B O   
5702 N N   . PRO   B 98  ? 0.2255 0.1614 0.1705 0.0228  0.0445  0.0399  98  PRO   B N   
5703 C CA  . PRO   B 98  ? 0.2473 0.1876 0.1902 0.0361  0.0578  0.0385  98  PRO   B CA  
5704 C C   . PRO   B 98  ? 0.2623 0.1900 0.1476 0.0609  0.0725  0.0617  98  PRO   B C   
5705 O O   . PRO   B 98  ? 0.2491 0.1824 0.1730 0.0484  0.0704  0.0537  98  PRO   B O   
5706 C CB  . PRO   B 98  ? 0.2373 0.1964 0.2132 0.0284  0.0704  0.0418  98  PRO   B CB  
5707 C CG  . PRO   B 98  ? 0.2335 0.1841 0.2060 0.0238  0.0587  0.0598  98  PRO   B CG  
5708 C CD  . PRO   B 98  ? 0.2161 0.1672 0.1991 0.0298  0.0551  0.0530  98  PRO   B CD  
5716 N N   . ASN   B 99  ? 0.2812 0.2159 0.1654 0.0811  0.0712  0.0484  99  ASN   B N   
5717 C CA  . ASN   B 99  ? 0.3036 0.2285 0.1684 0.0948  0.0606  0.0690  99  ASN   B CA  
5718 C C   . ASN   B 99  ? 0.3319 0.2668 0.2034 0.0945  0.0902  0.1006  99  ASN   B C   
5719 O O   . ASN   B 99  ? 0.3466 0.2716 0.2118 0.1001  0.0922  0.0962  99  ASN   B O   
5720 C CB  . ASN   B 99  ? 0.3107 0.2198 0.1736 0.0912  0.0452  0.0531  99  ASN   B CB  
5721 C CG  . ASN   B 99  ? 0.3177 0.2235 0.1909 0.0819  0.0408  0.0449  99  ASN   B CG  
5722 O OD1 . ASN   B 99  ? 0.3214 0.2219 0.2292 0.0880  0.0494  0.0522  99  ASN   B OD1 
5723 N ND2 . ASN   B 99  ? 0.3163 0.2270 0.2033 0.0735  0.0106  0.0325  99  ASN   B ND2 
5730 N N   A VAL   B 100 ? 0.3535 0.2863 0.2597 0.0761  0.0799  0.1175  100 VAL   B N   
5731 N N   B VAL   B 100 ? 0.3479 0.2855 0.2567 0.0743  0.0960  0.1295  100 VAL   B N   
5732 C CA  A VAL   B 100 ? 0.3776 0.3043 0.3138 0.0589  0.0640  0.1288  100 VAL   B CA  
5733 C CA  B VAL   B 100 ? 0.3714 0.3034 0.3167 0.0558  0.0863  0.1486  100 VAL   B CA  
5734 C C   A VAL   B 100 ? 0.3959 0.3116 0.3197 0.0589  0.0561  0.1500  100 VAL   B C   
5735 C C   B VAL   B 100 ? 0.3921 0.3093 0.3136 0.0577  0.0743  0.1653  100 VAL   B C   
5736 O O   A VAL   B 100 ? 0.3996 0.3198 0.3345 0.0573  0.0591  0.1399  100 VAL   B O   
5737 O O   B VAL   B 100 ? 0.3969 0.3216 0.3317 0.0576  0.0828  0.1507  100 VAL   B O   
5738 C CB  A VAL   B 100 ? 0.3840 0.3139 0.3582 0.0412  0.0543  0.1221  100 VAL   B CB  
5739 C CB  B VAL   B 100 ? 0.3777 0.3151 0.3829 0.0311  0.0800  0.1554  100 VAL   B CB  
5740 C CG1 A VAL   B 100 ? 0.3867 0.3171 0.3733 0.0373  0.0504  0.1209  100 VAL   B CG1 
5741 C CG1 B VAL   B 100 ? 0.3806 0.3191 0.4059 0.0269  0.0766  0.1592  100 VAL   B CG1 
5742 C CG2 A VAL   B 100 ? 0.3858 0.3176 0.3712 0.0340  0.0514  0.1208  100 VAL   B CG2 
5743 C CG2 B VAL   B 100 ? 0.3789 0.3193 0.4001 0.0195  0.0793  0.1606  100 VAL   B CG2 
5762 N N   . ASN   B 101 ? 0.4103 0.3153 0.3139 0.0625  0.0458  0.1668  101 ASN   B N   
5763 C CA  . ASN   B 101 ? 0.4504 0.3376 0.3267 0.0576  0.0142  0.1655  101 ASN   B CA  
5764 C C   . ASN   B 101 ? 0.4988 0.3958 0.3660 0.0398  0.0014  0.1418  101 ASN   B C   
5765 O O   . ASN   B 101 ? 0.5027 0.4014 0.3847 0.0449  0.0038  0.1257  101 ASN   B O   
5766 C CB  . ASN   B 101 ? 0.4460 0.3159 0.3349 0.0575  0.0116  0.1457  101 ASN   B CB  
5767 C CG  . ASN   B 101 ? 0.4402 0.2929 0.3389 0.0552  0.0162  0.1329  101 ASN   B CG  
5768 O OD1 . ASN   B 101 ? 0.4409 0.2961 0.3615 0.0485  0.0273  0.1195  101 ASN   B OD1 
5769 N ND2 . ASN   B 101 ? 0.4363 0.2860 0.3318 0.0572  0.0130  0.1172  101 ASN   B ND2 
5777 N N   A LYS   B 102 ? 0.5176 0.4254 0.3945 0.0265  0.0024  0.1207  102 LYS   B N   
5778 N N   B LYS   B 102 ? 0.5227 0.4255 0.3865 0.0266  0.0009  0.1259  102 LYS   B N   
5779 C CA  A LYS   B 102 ? 0.5344 0.4550 0.4196 0.0127  0.0060  0.0962  102 LYS   B CA  
5780 C CA  B LYS   B 102 ? 0.5446 0.4587 0.4083 0.0112  0.0029  0.0999  102 LYS   B CA  
5781 C C   A LYS   B 102 ? 0.5369 0.4600 0.3962 0.0120  0.0097  0.1063  102 LYS   B C   
5782 C C   B LYS   B 102 ? 0.5434 0.4620 0.3806 0.0114  0.0065  0.1114  102 LYS   B C   
5783 O O   A LYS   B 102 ? 0.5408 0.4630 0.3949 0.0115  0.0039  0.1074  102 LYS   B O   
5784 O O   B LYS   B 102 ? 0.5495 0.4656 0.3716 0.0114  -0.0031 0.1140  102 LYS   B O   
5785 C CB  A LYS   B 102 ? 0.5460 0.4763 0.4688 0.0009  0.0114  0.0602  102 LYS   B CB  
5786 C CB  B LYS   B 102 ? 0.5644 0.4857 0.4645 -0.0033 0.0109  0.0579  102 LYS   B CB  
5787 C CG  A LYS   B 102 ? 0.5554 0.4939 0.5126 -0.0088 0.0177  0.0283  102 LYS   B CG  
5788 C CG  B LYS   B 102 ? 0.5812 0.5089 0.5183 -0.0153 0.0194  0.0211  102 LYS   B CG  
5789 C CD  A LYS   B 102 ? 0.5636 0.5081 0.5539 -0.0158 0.0234  0.0032  102 LYS   B CD  
5790 C CD  B LYS   B 102 ? 0.5961 0.5285 0.5734 -0.0242 0.0274  -0.0075 102 LYS   B CD  
5791 C CE  A LYS   B 102 ? 0.5691 0.5174 0.5830 -0.0206 0.0271  -0.0152 102 LYS   B CE  
5792 C CE  B LYS   B 102 ? 0.6062 0.5418 0.6138 -0.0309 0.0323  -0.0289 102 LYS   B CE  
5793 N NZ  A LYS   B 102 ? 0.5726 0.5229 0.5993 -0.0226 0.0282  -0.0259 102 LYS   B NZ  
5794 N NZ  B LYS   B 102 ? 0.6125 0.5498 0.6383 -0.0339 0.0334  -0.0422 102 LYS   B NZ  
5821 N N   . GLY   B 103 ? 0.5333 0.4593 0.3843 0.0131  0.0213  0.1106  103 GLY   B N   
5822 C CA  . GLY   B 103 ? 0.5184 0.4544 0.3982 0.0172  0.0478  0.1015  103 GLY   B CA  
5823 C C   . GLY   B 103 ? 0.4994 0.4457 0.4030 0.0211  0.0713  0.0890  103 GLY   B C   
5824 O O   . GLY   B 103 ? 0.5034 0.4510 0.4053 0.0207  0.0779  0.0966  103 GLY   B O   
5829 N N   A GLU   B 104 ? 0.4881 0.4406 0.4045 0.0217  0.0691  0.0721  104 GLU   B N   
5830 N N   B GLU   B 104 ? 0.4846 0.4339 0.3893 0.0250  0.0895  0.0795  104 GLU   B N   
5831 C CA  A GLU   B 104 ? 0.4758 0.4346 0.4015 0.0232  0.0644  0.0506  104 GLU   B CA  
5832 C CA  B GLU   B 104 ? 0.4684 0.4222 0.3752 0.0315  0.1013  0.0650  104 GLU   B CA  
5833 C C   A GLU   B 104 ? 0.4709 0.4319 0.4123 0.0166  0.0829  0.0471  104 GLU   B C   
5834 C C   B GLU   B 104 ? 0.4646 0.4203 0.3869 0.0201  0.1440  0.0752  104 GLU   B C   
5835 O O   A GLU   B 104 ? 0.4713 0.4332 0.4205 0.0154  0.0837  0.0491  104 GLU   B O   
5836 O O   B GLU   B 104 ? 0.4653 0.4221 0.4065 0.0173  0.1457  0.0795  104 GLU   B O   
5837 C CB  A GLU   B 104 ? 0.4696 0.4298 0.3879 0.0313  0.0404  0.0282  104 GLU   B CB  
5838 C CB  B GLU   B 104 ? 0.4595 0.4104 0.3564 0.0501  0.0647  0.0310  104 GLU   B CB  
5839 C CG  A GLU   B 104 ? 0.4641 0.4261 0.3749 0.0392  0.0153  0.0054  104 GLU   B CG  
5840 C CG  B GLU   B 104 ? 0.4504 0.4003 0.3372 0.0694  0.0242  -0.0041 104 GLU   B CG  
5841 C CD  A GLU   B 104 ? 0.4600 0.4230 0.3627 0.0456  -0.0065 -0.0129 104 GLU   B CD  
5842 C CD  B GLU   B 104 ? 0.4431 0.3911 0.3164 0.0852  -0.0100 -0.0316 104 GLU   B CD  
5843 O OE1 A GLU   B 104 ? 0.4570 0.4193 0.3477 0.0479  -0.0087 -0.0194 104 GLU   B OE1 
5844 O OE1 B GLU   B 104 ? 0.4354 0.3807 0.2842 0.0961  -0.0084 -0.0449 104 GLU   B OE1 
5845 O OE2 A GLU   B 104 ? 0.4589 0.4234 0.3570 0.0481  -0.0202 -0.0231 104 GLU   B OE2 
5846 O OE2 B GLU   B 104 ? 0.4413 0.3919 0.3026 0.0879  -0.0340 -0.0481 104 GLU   B OE2 
5859 N N   A ASP   B 105 ? 0.4637 0.4269 0.4089 0.0115  0.0985  0.0395  105 ASP   B N   
5860 N N   B ASP   B 105 ? 0.4564 0.4148 0.3658 0.0122  0.1820  0.0753  105 ASP   B N   
5861 C CA  A ASP   B 105 ? 0.4581 0.4222 0.4150 0.0070  0.1086  0.0262  105 ASP   B CA  
5862 C CA  B ASP   B 105 ? 0.4507 0.4098 0.3684 0.0053  0.2083  0.0603  105 ASP   B CA  
5863 C C   A ASP   B 105 ? 0.4441 0.4058 0.3812 -0.0001 0.1128  0.0169  105 ASP   B C   
5864 C C   B ASP   B 105 ? 0.4308 0.3842 0.3218 -0.0080 0.2112  0.0513  105 ASP   B C   
5865 O O   A ASP   B 105 ? 0.4440 0.4048 0.3693 0.0026  0.1173  0.0173  105 ASP   B O   
5866 O O   B ASP   B 105 ? 0.4204 0.3793 0.3144 -0.0043 0.2067  0.0507  105 ASP   B O   
5867 C CB  A ASP   B 105 ? 0.4640 0.4311 0.4575 0.0100  0.1137  0.0196  105 ASP   B CB  
5868 C CB  B ASP   B 105 ? 0.4621 0.4264 0.4386 0.0126  0.2125  0.0445  105 ASP   B CB  
5869 C CG  A ASP   B 105 ? 0.4689 0.4381 0.4991 0.0109  0.1188  0.0149  105 ASP   B CG  
5870 C CG  B ASP   B 105 ? 0.4695 0.4387 0.5028 0.0132  0.2208  0.0381  105 ASP   B CG  
5871 O OD1 A ASP   B 105 ? 0.4693 0.4396 0.5086 0.0093  0.1240  0.0164  105 ASP   B OD1 
5872 O OD1 B ASP   B 105 ? 0.4696 0.4418 0.5163 0.0078  0.2298  0.0448  105 ASP   B OD1 
5873 O OD2 A ASP   B 105 ? 0.4710 0.4414 0.5187 0.0134  0.1176  0.0102  105 ASP   B OD2 
5874 O OD2 B ASP   B 105 ? 0.4708 0.4438 0.5290 0.0168  0.2234  0.0298  105 ASP   B OD2 
5883 N N   A ILE   B 106 ? 0.4289 0.3886 0.3695 -0.0081 0.1077  0.0102  106 ILE   B N   
5884 N N   B ILE   B 106 ? 0.4214 0.3609 0.3222 -0.0237 0.2048  0.0463  106 ILE   B N   
5885 C CA  A ILE   B 106 ? 0.4106 0.3714 0.3636 -0.0148 0.1074  0.0019  106 ILE   B CA  
5886 C CA  B ILE   B 106 ? 0.4008 0.3376 0.3296 -0.0377 0.2032  0.0314  106 ILE   B CA  
5887 C C   A ILE   B 106 ? 0.3882 0.3616 0.3600 -0.0126 0.1068  -0.0056 106 ILE   B C   
5888 C C   B ILE   B 106 ? 0.3657 0.3265 0.3265 -0.0379 0.1996  0.0199  106 ILE   B C   
5889 O O   A ILE   B 106 ? 0.3860 0.3547 0.3591 -0.0137 0.1064  -0.0089 106 ILE   B O   
5890 O O   B ILE   B 106 ? 0.3532 0.3057 0.3175 -0.0463 0.1881  0.0269  106 ILE   B O   
5891 C CB  A ILE   B 106 ? 0.4142 0.3653 0.3626 -0.0225 0.1072  0.0012  106 ILE   B CB  
5892 C CB  B ILE   B 106 ? 0.4138 0.3294 0.3413 -0.0475 0.1988  0.0250  106 ILE   B CB  
5893 C CG1 A ILE   B 106 ? 0.4144 0.3610 0.3546 -0.0242 0.1058  0.0004  106 ILE   B CG1 
5894 C CG1 B ILE   B 106 ? 0.4199 0.3281 0.3365 -0.0430 0.1886  0.0149  106 ILE   B CG1 
5895 C CG2 A ILE   B 106 ? 0.4166 0.3667 0.3711 -0.0252 0.1078  0.0013  106 ILE   B CG2 
5896 C CG2 B ILE   B 106 ? 0.4189 0.3320 0.3595 -0.0546 0.2008  0.0252  106 ILE   B CG2 
5897 C CD1 A ILE   B 106 ? 0.4140 0.3586 0.3479 -0.0244 0.1054  0.0006  106 ILE   B CD1 
5898 C CD1 B ILE   B 106 ? 0.4227 0.3276 0.3286 -0.0387 0.1838  0.0113  106 ILE   B CD1 
5921 N N   A GLN   B 107 ? 0.3685 0.3593 0.3654 -0.0125 0.1054  -0.0055 107 GLN   B N   
5922 N N   B GLN   B 107 ? 0.3469 0.3357 0.3497 -0.0364 0.1897  0.0124  107 GLN   B N   
5923 C CA  A GLN   B 107 ? 0.3474 0.3543 0.3682 -0.0114 0.1022  -0.0035 107 GLN   B CA  
5924 C CA  B GLN   B 107 ? 0.3224 0.3418 0.3565 -0.0359 0.1781  0.0070  107 GLN   B CA  
5925 C C   A GLN   B 107 ? 0.3113 0.3258 0.3300 -0.0048 0.1104  -0.0043 107 GLN   B C   
5926 C C   B GLN   B 107 ? 0.2918 0.3171 0.3216 -0.0201 0.1541  -0.0025 107 GLN   B C   
5927 O O   A GLN   B 107 ? 0.3076 0.3282 0.3417 -0.0005 0.0946  -0.0170 107 GLN   B O   
5928 O O   B GLN   B 107 ? 0.2807 0.3213 0.3519 -0.0093 0.1257  -0.0310 107 GLN   B O   
5929 C CB  A GLN   B 107 ? 0.3661 0.3786 0.4213 -0.0131 0.0822  -0.0019 107 GLN   B CB  
5930 C CB  B GLN   B 107 ? 0.3502 0.3798 0.4291 -0.0362 0.1454  0.0050  107 GLN   B CB  
5931 C CG  A GLN   B 107 ? 0.3830 0.3991 0.4693 -0.0129 0.0607  -0.0005 107 GLN   B CG  
5932 C CG  B GLN   B 107 ? 0.3801 0.4128 0.4971 -0.0320 0.1009  0.0008  107 GLN   B CG  
5933 C CD  A GLN   B 107 ? 0.3952 0.4147 0.5083 -0.0139 0.0449  0.0021  107 GLN   B CD  
5934 C CD  B GLN   B 107 ? 0.4019 0.4380 0.5498 -0.0317 0.0688  0.0002  107 GLN   B CD  
5935 O OE1 A GLN   B 107 ? 0.3995 0.4203 0.5234 -0.0135 0.0421  0.0021  107 GLN   B OE1 
5936 O OE1 B GLN   B 107 ? 0.4100 0.4478 0.5700 -0.0315 0.0639  0.0012  107 GLN   B OE1 
5937 N NE2 A GLN   B 107 ? 0.4006 0.4203 0.5229 -0.0140 0.0383  0.0037  107 GLN   B NE2 
5938 N NE2 B GLN   B 107 ? 0.4115 0.4473 0.5694 -0.0308 0.0551  -0.0003 107 GLN   B NE2 
5955 N N   . LEU   B 108 ? 0.2772 0.2955 0.2945 0.0023  0.1277  0.0044  108 LEU   B N   
5956 C CA  . LEU   B 108 ? 0.2437 0.2577 0.2454 0.0215  0.1003  0.0261  108 LEU   B CA  
5957 C C   . LEU   B 108 ? 0.2025 0.2009 0.2325 0.0281  0.0613  0.0299  108 LEU   B C   
5958 O O   . LEU   B 108 ? 0.1955 0.1827 0.2203 0.0293  0.0409  0.0225  108 LEU   B O   
5959 C CB  . LEU   B 108 ? 0.2620 0.2816 0.2248 0.0255  0.1025  0.0405  108 LEU   B CB  
5960 C CG  . LEU   B 108 ? 0.2761 0.3119 0.2400 0.0314  0.0895  0.0253  108 LEU   B CG  
5961 C CD1 . LEU   B 108 ? 0.2913 0.3282 0.2337 0.0276  0.0799  0.0255  108 LEU   B CD1 
5962 C CD2 . LEU   B 108 ? 0.2843 0.3200 0.2519 0.0394  0.0753  0.0066  108 LEU   B CD2 
5975 N N   . LEU   B 109 ? 0.1873 0.1672 0.2287 0.0224  0.0503  0.0293  109 LEU   B N   
5976 C CA  . LEU   B 109 ? 0.1628 0.1482 0.2416 0.0158  0.0447  0.0353  109 LEU   B CA  
5977 C C   . LEU   B 109 ? 0.1488 0.1302 0.2422 0.0048  0.0444  0.0229  109 LEU   B C   
5978 O O   . LEU   B 109 ? 0.1431 0.1211 0.2297 0.0040  0.0423  0.0354  109 LEU   B O   
5979 C CB  . LEU   B 109 ? 0.1704 0.1354 0.2478 0.0088  0.0380  0.0386  109 LEU   B CB  
5980 C CG  . LEU   B 109 ? 0.1654 0.1348 0.2271 0.0049  0.0305  0.0341  109 LEU   B CG  
5981 C CD1 . LEU   B 109 ? 0.1631 0.1456 0.2159 0.0042  0.0263  0.0322  109 LEU   B CD1 
5982 C CD2 . LEU   B 109 ? 0.1788 0.1466 0.2419 0.0095  0.0223  0.0295  109 LEU   B CD2 
5994 N N   . LYS   B 110 ? 0.1471 0.1325 0.2264 -0.0041 0.0451  0.0145  110 LYS   B N   
5995 C CA  . LYS   B 110 ? 0.1475 0.1253 0.2255 -0.0041 0.0366  0.0171  110 LYS   B CA  
5996 C C   . LYS   B 110 ? 0.1361 0.1306 0.2168 -0.0011 0.0412  0.0127  110 LYS   B C   
5997 O O   . LYS   B 110 ? 0.1331 0.1322 0.2144 -0.0068 0.0305  0.0093  110 LYS   B O   
5998 C CB  . LYS   B 110 ? 0.1510 0.1244 0.2497 -0.0036 0.0386  0.0137  110 LYS   B CB  
5999 C CG  . LYS   B 110 ? 0.1471 0.1289 0.2603 -0.0086 0.0227  0.0326  110 LYS   B CG  
6000 C CD  . LYS   B 110 ? 0.1506 0.1285 0.2640 -0.0033 0.0167  0.0145  110 LYS   B CD  
6001 C CE  . LYS   B 110 ? 0.1457 0.1409 0.2895 0.0003  0.0188  0.0085  110 LYS   B CE  
6002 N NZ  . LYS   B 110 ? 0.1456 0.1610 0.2843 0.0028  0.0098  0.0087  110 LYS   B NZ  
6016 N N   . SER   B 111 ? 0.1417 0.1294 0.2275 0.0022  0.0320  0.0118  111 SER   B N   
6017 C CA  . SER   B 111 ? 0.1501 0.1333 0.2103 0.0027  0.0310  0.0158  111 SER   B CA  
6018 C C   . SER   B 111 ? 0.1435 0.1268 0.1929 -0.0030 0.0237  0.0070  111 SER   B C   
6019 O O   . SER   B 111 ? 0.1423 0.1342 0.2055 -0.0038 0.0171  0.0105  111 SER   B O   
6020 C CB  . SER   B 111 ? 0.1683 0.1540 0.2132 0.0081  0.0474  0.0260  111 SER   B CB  
6021 O OG  . SER   B 111 ? 0.1879 0.1819 0.2223 0.0153  0.0528  0.0289  111 SER   B OG  
6027 N N   . ALA   B 112 ? 0.1362 0.1316 0.2009 0.0072  0.0296  0.0164  112 ALA   B N   
6028 C CA  . ALA   B 112 ? 0.1325 0.1367 0.1873 -0.0001 0.0174  0.0064  112 ALA   B CA  
6029 C C   . ALA   B 112 ? 0.1276 0.1241 0.1908 0.0013  0.0156  0.0083  112 ALA   B C   
6030 O O   . ALA   B 112 ? 0.1285 0.1268 0.1945 -0.0009 0.0180  0.0065  112 ALA   B O   
6031 C CB  . ALA   B 112 ? 0.1398 0.1407 0.1827 0.0049  0.0202  0.0153  112 ALA   B CB  
6037 N N   . TYR   B 113 ? 0.1244 0.1166 0.1936 -0.0012 0.0129  0.0150  113 TYR   B N   
6038 C CA  . TYR   B 113 ? 0.1229 0.1163 0.1946 -0.0044 0.0140  0.0061  113 TYR   B CA  
6039 C C   . TYR   B 113 ? 0.1223 0.1130 0.1776 -0.0085 0.0108  0.0059  113 TYR   B C   
6040 O O   . TYR   B 113 ? 0.1278 0.1120 0.1778 -0.0053 0.0092  -0.0009 113 TYR   B O   
6041 C CB  . TYR   B 113 ? 0.1278 0.1052 0.1980 -0.0014 0.0215  0.0072  113 TYR   B CB  
6042 C CG  . TYR   B 113 ? 0.1266 0.1137 0.2077 -0.0029 0.0162  0.0135  113 TYR   B CG  
6043 C CD1 . TYR   B 113 ? 0.1339 0.1157 0.2057 -0.0039 0.0178  0.0228  113 TYR   B CD1 
6044 C CD2 . TYR   B 113 ? 0.1411 0.1164 0.2178 -0.0072 0.0087  0.0144  113 TYR   B CD2 
6045 C CE1 . TYR   B 113 ? 0.1384 0.1176 0.1911 0.0007  0.0240  0.0119  113 TYR   B CE1 
6046 C CE2 . TYR   B 113 ? 0.1436 0.1088 0.2192 -0.0021 0.0152  0.0165  113 TYR   B CE2 
6047 C CZ  . TYR   B 113 ? 0.1416 0.1151 0.2113 0.0050  0.0186  0.0071  113 TYR   B CZ  
6048 O OH  . TYR   B 113 ? 0.1465 0.1142 0.2488 0.0089  0.0255  0.0117  113 TYR   B OH  
6058 N N   . GLU   B 114 ? 0.1161 0.1101 0.2000 -0.0074 0.0178  0.0074  114 GLU   B N   
6059 C CA  . GLU   B 114 ? 0.1186 0.1112 0.1974 -0.0002 0.0078  -0.0013 114 GLU   B CA  
6060 C C   . GLU   B 114 ? 0.1151 0.1110 0.1893 -0.0044 0.0077  -0.0008 114 GLU   B C   
6061 O O   . GLU   B 114 ? 0.1210 0.1124 0.2042 -0.0013 -0.0042 0.0125  114 GLU   B O   
6062 C CB  . GLU   B 114 ? 0.1212 0.1106 0.2078 -0.0019 0.0184  0.0036  114 GLU   B CB  
6063 C CG  . GLU   B 114 ? 0.1293 0.1127 0.2216 -0.0004 0.0118  -0.0040 114 GLU   B CG  
6064 C CD  . GLU   B 114 ? 0.1207 0.1137 0.2183 -0.0044 0.0100  0.0056  114 GLU   B CD  
6065 O OE1 . GLU   B 114 ? 0.1230 0.1339 0.2091 -0.0058 0.0262  0.0061  114 GLU   B OE1 
6066 O OE2 . GLU   B 114 ? 0.1244 0.1382 0.2429 -0.0132 0.0176  0.0063  114 GLU   B OE2 
6073 N N   . ASN   B 115 ? 0.1192 0.1137 0.1823 -0.0043 0.0059  0.0046  115 ASN   B N   
6074 C CA  . ASN   B 115 ? 0.1262 0.1130 0.1676 -0.0056 0.0080  0.0072  115 ASN   B CA  
6075 C C   . ASN   B 115 ? 0.1228 0.1086 0.1751 -0.0023 -0.0000 -0.0002 115 ASN   B C   
6076 O O   . ASN   B 115 ? 0.1349 0.1116 0.1808 -0.0119 -0.0014 0.0074  115 ASN   B O   
6077 C CB  . ASN   B 115 ? 0.1370 0.1263 0.1735 -0.0070 0.0149  0.0002  115 ASN   B CB  
6078 C CG  . ASN   B 115 ? 0.1486 0.1289 0.1770 0.0037  0.0080  0.0029  115 ASN   B CG  
6079 O OD1 . ASN   B 115 ? 0.1848 0.1420 0.1969 0.0006  0.0121  -0.0064 115 ASN   B OD1 
6080 N ND2 . ASN   B 115 ? 0.1430 0.1362 0.1708 -0.0014 0.0053  0.0134  115 ASN   B ND2 
6087 N N   . PHE   B 116 ? 0.1284 0.1118 0.1536 -0.0088 -0.0044 0.0048  116 PHE   B N   
6088 C CA  . PHE   B 116 ? 0.1226 0.1167 0.1595 -0.0101 -0.0038 0.0054  116 PHE   B CA  
6089 C C   . PHE   B 116 ? 0.1300 0.1056 0.1581 -0.0107 -0.0048 0.0010  116 PHE   B C   
6090 O O   . PHE   B 116 ? 0.1357 0.1198 0.1638 -0.0075 -0.0077 0.0043  116 PHE   B O   
6091 C CB  . PHE   B 116 ? 0.1213 0.1130 0.1513 -0.0030 -0.0030 0.0017  116 PHE   B CB  
6092 C CG  . PHE   B 116 ? 0.1172 0.1180 0.1622 -0.0115 -0.0010 0.0044  116 PHE   B CG  
6093 C CD1 . PHE   B 116 ? 0.1273 0.1187 0.1717 -0.0031 -0.0056 0.0010  116 PHE   B CD1 
6094 C CD2 . PHE   B 116 ? 0.1299 0.1228 0.1539 -0.0096 -0.0020 0.0013  116 PHE   B CD2 
6095 C CE1 . PHE   B 116 ? 0.1335 0.1255 0.1747 -0.0065 -0.0120 0.0131  116 PHE   B CE1 
6096 C CE2 . PHE   B 116 ? 0.1278 0.1202 0.1627 -0.0020 0.0021  -0.0007 116 PHE   B CE2 
6097 C CZ  . PHE   B 116 ? 0.1190 0.1258 0.1602 -0.0051 -0.0023 0.0123  116 PHE   B CZ  
6107 N N   . ASN   B 117 ? 0.1287 0.1094 0.1789 -0.0049 -0.0086 0.0072  117 ASN   B N   
6108 C CA  . ASN   B 117 ? 0.1394 0.1160 0.1818 0.0008  -0.0112 0.0077  117 ASN   B CA  
6109 C C   . ASN   B 117 ? 0.1330 0.1125 0.1942 -0.0060 -0.0153 0.0130  117 ASN   B C   
6110 O O   . ASN   B 117 ? 0.1411 0.1195 0.2229 -0.0078 -0.0390 0.0199  117 ASN   B O   
6111 C CB  . ASN   B 117 ? 0.1375 0.1179 0.1935 0.0018  -0.0125 0.0022  117 ASN   B CB  
6112 C CG  . ASN   B 117 ? 0.1312 0.1182 0.2070 0.0017  0.0006  -0.0043 117 ASN   B CG  
6113 O OD1 . ASN   B 117 ? 0.1459 0.1238 0.2053 -0.0168 -0.0047 -0.0057 117 ASN   B OD1 
6114 N ND2 . ASN   B 117 ? 0.1373 0.1218 0.1976 -0.0065 -0.0043 -0.0075 117 ASN   B ND2 
6121 N N   . GLN   B 118 ? 0.1373 0.1061 0.1885 -0.0101 -0.0183 0.0053  118 GLN   B N   
6122 C CA  . GLN   B 118 ? 0.1402 0.1101 0.1966 -0.0047 -0.0184 0.0055  118 GLN   B CA  
6123 C C   . GLN   B 118 ? 0.1416 0.1093 0.1965 -0.0051 -0.0122 0.0097  118 GLN   B C   
6124 O O   . GLN   B 118 ? 0.1600 0.1174 0.2236 -0.0077 0.0011  0.0129  118 GLN   B O   
6125 C CB  . GLN   B 118 ? 0.1436 0.1160 0.2072 -0.0021 -0.0195 -0.0014 118 GLN   B CB  
6126 C CG  . GLN   B 118 ? 0.1547 0.1235 0.2012 0.0082  -0.0152 -0.0095 118 GLN   B CG  
6127 C CD  . GLN   B 118 ? 0.1618 0.1127 0.1950 0.0052  -0.0084 -0.0076 118 GLN   B CD  
6128 O OE1 . GLN   B 118 ? 0.1680 0.1121 0.2220 0.0066  0.0021  0.0018  118 GLN   B OE1 
6129 N NE2 . GLN   B 118 ? 0.1706 0.1114 0.1983 0.0012  -0.0173 -0.0022 118 GLN   B NE2 
6138 N N   . HIS   B 119 ? 0.1438 0.1149 0.1635 -0.0128 -0.0173 0.0136  119 HIS   B N   
6139 C CA  . HIS   B 119 ? 0.1562 0.1293 0.1616 -0.0086 -0.0232 0.0188  119 HIS   B CA  
6140 C C   . HIS   B 119 ? 0.1522 0.1302 0.1598 -0.0055 -0.0357 0.0147  119 HIS   B C   
6141 O O   . HIS   B 119 ? 0.1639 0.1322 0.1803 -0.0290 -0.0252 0.0129  119 HIS   B O   
6142 C CB  . HIS   B 119 ? 0.1595 0.1464 0.1571 -0.0002 -0.0247 0.0058  119 HIS   B CB  
6143 C CG  . HIS   B 119 ? 0.1621 0.1646 0.1798 0.0064  -0.0462 -0.0102 119 HIS   B CG  
6144 N ND1 . HIS   B 119 ? 0.1638 0.1821 0.2225 -0.0027 -0.0562 -0.0328 119 HIS   B ND1 
6145 C CD2 . HIS   B 119 ? 0.1834 0.1880 0.1854 0.0404  -0.0552 -0.0129 119 HIS   B CD2 
6146 C CE1 . HIS   B 119 ? 0.1850 0.2014 0.2229 0.0147  -0.0671 -0.0434 119 HIS   B CE1 
6147 N NE2 . HIS   B 119 ? 0.1950 0.2132 0.2008 0.0339  -0.0576 -0.0317 119 HIS   B NE2 
6155 N N   . GLU   B 120 ? 0.1680 0.1343 0.1674 -0.0182 -0.0470 0.0212  120 GLU   B N   
6156 C CA  . GLU   B 120 ? 0.2019 0.1411 0.1735 -0.0114 -0.0497 0.0276  120 GLU   B CA  
6157 C C   . GLU   B 120 ? 0.1793 0.1372 0.1608 -0.0218 -0.0404 0.0267  120 GLU   B C   
6158 O O   . GLU   B 120 ? 0.1725 0.1504 0.1658 -0.0227 -0.0439 0.0147  120 GLU   B O   
6159 C CB  . GLU   B 120 ? 0.2629 0.1673 0.2358 0.0059  -0.0760 0.0431  120 GLU   B CB  
6160 C CG  . GLU   B 120 ? 0.3084 0.2319 0.3300 0.0167  -0.0983 0.0512  120 GLU   B CG  
6161 C CD  . GLU   B 120 ? 0.3461 0.2901 0.4285 0.0212  -0.1003 0.0667  120 GLU   B CD  
6162 O OE1 . GLU   B 120 ? 0.3675 0.3158 0.4652 0.0141  -0.0907 0.0777  120 GLU   B OE1 
6163 O OE2 . GLU   B 120 ? 0.3654 0.3163 0.4810 0.0229  -0.0986 0.0595  120 GLU   B OE2 
6170 N N   . VAL   B 121 ? 0.1720 0.1352 0.1579 -0.0265 -0.0290 0.0246  121 VAL   B N   
6171 C CA  . VAL   B 121 ? 0.1689 0.1427 0.1393 -0.0212 -0.0303 0.0188  121 VAL   B CA  
6172 C C   . VAL   B 121 ? 0.1613 0.1407 0.1448 -0.0283 -0.0283 0.0143  121 VAL   B C   
6173 O O   . VAL   B 121 ? 0.1703 0.1373 0.1614 -0.0347 -0.0366 0.0218  121 VAL   B O   
6174 C CB  . VAL   B 121 ? 0.1942 0.1816 0.1614 -0.0154 -0.0298 0.0283  121 VAL   B CB  
6175 C CG1 . VAL   B 121 ? 0.1938 0.1963 0.1942 -0.0268 -0.0254 0.0264  121 VAL   B CG1 
6176 C CG2 . VAL   B 121 ? 0.2182 0.2062 0.1608 -0.0030 -0.0161 0.0177  121 VAL   B CG2 
6186 N N   . LEU   B 122 ? 0.1512 0.1336 0.1375 -0.0211 -0.0288 0.0128  122 LEU   B N   
6187 C CA  . LEU   B 122 ? 0.1446 0.1394 0.1216 -0.0263 -0.0213 0.0120  122 LEU   B CA  
6188 C C   . LEU   B 122 ? 0.1401 0.1298 0.1317 -0.0314 -0.0226 0.0103  122 LEU   B C   
6189 O O   . LEU   B 122 ? 0.1519 0.1360 0.1665 -0.0353 -0.0314 0.0051  122 LEU   B O   
6190 C CB  . LEU   B 122 ? 0.1675 0.1470 0.1654 -0.0065 -0.0219 0.0182  122 LEU   B CB  
6191 C CG  . LEU   B 122 ? 0.1534 0.1563 0.1704 -0.0177 -0.0073 0.0149  122 LEU   B CG  
6192 C CD1 . LEU   B 122 ? 0.1644 0.1765 0.1589 -0.0227 -0.0165 0.0064  122 LEU   B CD1 
6193 C CD2 . LEU   B 122 ? 0.1484 0.1600 0.1440 -0.0082 -0.0109 0.0092  122 LEU   B CD2 
6205 N N   . LEU   B 123 ? 0.1432 0.1196 0.1200 -0.0269 -0.0250 0.0113  123 LEU   B N   
6206 C CA  . LEU   B 123 ? 0.1437 0.1238 0.1288 -0.0294 -0.0239 0.0021  123 LEU   B CA  
6207 C C   . LEU   B 123 ? 0.1381 0.1199 0.1253 -0.0257 -0.0089 0.0077  123 LEU   B C   
6208 O O   . LEU   B 123 ? 0.1514 0.1229 0.1299 -0.0347 -0.0184 0.0006  123 LEU   B O   
6209 C CB  . LEU   B 123 ? 0.1487 0.1270 0.1414 -0.0320 -0.0170 0.0002  123 LEU   B CB  
6210 C CG  . LEU   B 123 ? 0.1538 0.1265 0.1457 -0.0220 -0.0151 0.0091  123 LEU   B CG  
6211 C CD1 . LEU   B 123 ? 0.1618 0.1294 0.1609 -0.0175 -0.0016 -0.0070 123 LEU   B CD1 
6212 C CD2 . LEU   B 123 ? 0.1593 0.1414 0.1630 -0.0190 -0.0015 0.0131  123 LEU   B CD2 
6224 N N   . ALA   B 124 ? 0.1339 0.1170 0.1299 -0.0198 -0.0077 -0.0014 124 ALA   B N   
6225 C CA  . ALA   B 124 ? 0.1297 0.1155 0.1371 -0.0138 -0.0101 -0.0015 124 ALA   B CA  
6226 C C   . ALA   B 124 ? 0.1267 0.1154 0.1254 -0.0137 -0.0101 -0.0038 124 ALA   B C   
6227 O O   . ALA   B 124 ? 0.1350 0.1255 0.1420 -0.0161 -0.0104 0.0053  124 ALA   B O   
6228 C CB  . ALA   B 124 ? 0.1365 0.1179 0.1544 -0.0100 0.0054  0.0020  124 ALA   B CB  
6234 N N   . PRO   B 125 ? 0.1362 0.1175 0.1387 -0.0155 -0.0155 0.0110  125 PRO   B N   
6235 C CA  . PRO   B 125 ? 0.1462 0.1199 0.1513 -0.0182 -0.0183 0.0207  125 PRO   B CA  
6236 C C   . PRO   B 125 ? 0.1395 0.1130 0.1627 -0.0146 -0.0100 0.0112  125 PRO   B C   
6237 O O   . PRO   B 125 ? 0.1393 0.1161 0.1809 -0.0079 -0.0042 0.0173  125 PRO   B O   
6238 C CB  . PRO   B 125 ? 0.1476 0.1443 0.1663 -0.0236 -0.0274 0.0317  125 PRO   B CB  
6239 C CG  . PRO   B 125 ? 0.1546 0.1532 0.1521 -0.0310 -0.0218 0.0235  125 PRO   B CG  
6240 C CD  . PRO   B 125 ? 0.1503 0.1325 0.1388 -0.0332 -0.0150 0.0107  125 PRO   B CD  
6248 N N   . LEU   B 126 ? 0.1476 0.1091 0.1863 -0.0140 0.0092  0.0179  126 LEU   B N   
6249 C CA  . LEU   B 126 ? 0.1563 0.1216 0.1868 -0.0124 0.0253  0.0166  126 LEU   B CA  
6250 C C   . LEU   B 126 ? 0.1565 0.1332 0.1889 0.0035  0.0214  0.0250  126 LEU   B C   
6251 O O   . LEU   B 126 ? 0.1748 0.1642 0.2163 0.0185  -0.0008 0.0051  126 LEU   B O   
6252 C CB  . LEU   B 126 ? 0.1686 0.1273 0.2260 -0.0199 0.0260  0.0162  126 LEU   B CB  
6253 C CG  . LEU   B 126 ? 0.1852 0.1407 0.2414 -0.0327 0.0268  -0.0018 126 LEU   B CG  
6254 C CD1 . LEU   B 126 ? 0.2030 0.1426 0.2880 -0.0244 0.0239  -0.0091 126 LEU   B CD1 
6255 C CD2 . LEU   B 126 ? 0.1878 0.1556 0.2299 -0.0390 0.0184  -0.0063 126 LEU   B CD2 
6267 N N   . LEU   B 127 ? 0.1492 0.1201 0.2026 0.0009  0.0312  0.0139  127 LEU   B N   
6268 C CA  . LEU   B 127 ? 0.1520 0.1295 0.2101 -0.0047 0.0341  0.0223  127 LEU   B CA  
6269 C C   . LEU   B 127 ? 0.1444 0.1258 0.2033 -0.0015 0.0233  0.0216  127 LEU   B C   
6270 O O   . LEU   B 127 ? 0.1487 0.1288 0.2213 -0.0112 0.0138  0.0249  127 LEU   B O   
6271 C CB  . LEU   B 127 ? 0.1637 0.1206 0.2146 -0.0054 0.0332  0.0177  127 LEU   B CB  
6272 C CG  . LEU   B 127 ? 0.1767 0.1237 0.2247 0.0018  0.0338  0.0100  127 LEU   B CG  
6273 C CD1 . LEU   B 127 ? 0.1823 0.1268 0.2314 0.0078  0.0304  0.0103  127 LEU   B CD1 
6274 C CD2 . LEU   B 127 ? 0.1809 0.1405 0.2366 -0.0103 0.0373  0.0241  127 LEU   B CD2 
6286 N N   . SER   B 128 ? 0.1477 0.1217 0.2092 -0.0005 0.0054  0.0143  128 SER   B N   
6287 C CA  . SER   B 128 ? 0.1646 0.1329 0.2123 0.0086  0.0023  0.0250  128 SER   B CA  
6288 C C   . SER   B 128 ? 0.1810 0.1394 0.2375 0.0068  -0.0177 0.0252  128 SER   B C   
6289 O O   . SER   B 128 ? 0.1979 0.1382 0.2897 0.0083  -0.0138 0.0439  128 SER   B O   
6290 C CB  . SER   B 128 ? 0.1690 0.1425 0.2081 0.0025  0.0089  0.0302  128 SER   B CB  
6291 O OG  . SER   B 128 ? 0.1713 0.1601 0.2071 0.0096  0.0130  0.0328  128 SER   B OG  
6297 N N   . ALA   B 129 ? 0.1955 0.1475 0.2540 0.0268  -0.0098 0.0066  129 ALA   B N   
6298 C CA  . ALA   B 129 ? 0.2143 0.1561 0.2717 0.0397  -0.0098 0.0016  129 ALA   B CA  
6299 C C   . ALA   B 129 ? 0.1985 0.1483 0.2481 0.0291  0.0078  -0.0001 129 ALA   B C   
6300 O O   . ALA   B 129 ? 0.1845 0.1511 0.2430 0.0216  -0.0015 0.0055  129 ALA   B O   
6301 C CB  . ALA   B 129 ? 0.2352 0.1778 0.3064 0.0433  0.0042  -0.0094 129 ALA   B CB  
6307 N N   . GLY   B 130 ? 0.1951 0.1445 0.2546 0.0317  0.0094  -0.0004 130 GLY   B N   
6308 C CA  . GLY   B 130 ? 0.1974 0.1538 0.2692 0.0309  0.0240  -0.0036 130 GLY   B CA  
6309 C C   . GLY   B 130 ? 0.1977 0.1551 0.2497 0.0257  0.0246  0.0112  130 GLY   B C   
6310 O O   . GLY   B 130 ? 0.2125 0.1716 0.2575 0.0214  0.0163  0.0210  130 GLY   B O   
6314 N N   . ILE   B 131 ? 0.1948 0.1789 0.2641 0.0367  0.0243  0.0135  131 ILE   B N   
6315 C CA  . ILE   B 131 ? 0.2170 0.1936 0.2644 0.0344  0.0178  0.0248  131 ILE   B CA  
6316 C C   . ILE   B 131 ? 0.2285 0.1821 0.2354 0.0277  0.0170  0.0330  131 ILE   B C   
6317 O O   . ILE   B 131 ? 0.2524 0.2014 0.2459 0.0300  0.0016  0.0357  131 ILE   B O   
6318 C CB  . ILE   B 131 ? 0.2182 0.2239 0.2974 0.0307  0.0004  0.0304  131 ILE   B CB  
6319 C CG1 . ILE   B 131 ? 0.2201 0.2413 0.3039 -0.0009 0.0063  0.0363  131 ILE   B CG1 
6320 C CG2 . ILE   B 131 ? 0.2213 0.2366 0.3175 0.0349  0.0065  0.0098  131 ILE   B CG2 
6321 C CD1 . ILE   B 131 ? 0.2305 0.2589 0.3175 -0.0204 0.0011  0.0410  131 ILE   B CD1 
6333 N N   . PHE   B 132 ? 0.2183 0.1661 0.2193 0.0240  0.0358  0.0326  132 PHE   B N   
6334 C CA  . PHE   B 132 ? 0.2285 0.1651 0.2229 0.0122  0.0579  0.0245  132 PHE   B CA  
6335 C C   . PHE   B 132 ? 0.2458 0.1814 0.2490 0.0130  0.0658  0.0175  132 PHE   B C   
6336 O O   . PHE   B 132 ? 0.2600 0.2091 0.2739 0.0101  0.0739  0.0194  132 PHE   B O   
6337 C CB  . PHE   B 132 ? 0.2131 0.1604 0.2033 0.0184  0.0529  0.0261  132 PHE   B CB  
6338 C CG  . PHE   B 132 ? 0.2011 0.1615 0.1903 0.0215  0.0384  0.0288  132 PHE   B CG  
6339 C CD1 . PHE   B 132 ? 0.2141 0.1586 0.2285 0.0165  0.0336  0.0312  132 PHE   B CD1 
6340 C CD2 . PHE   B 132 ? 0.1999 0.1723 0.1643 0.0269  0.0273  0.0299  132 PHE   B CD2 
6341 C CE1 . PHE   B 132 ? 0.2125 0.1632 0.2347 0.0099  0.0246  0.0235  132 PHE   B CE1 
6342 C CE2 . PHE   B 132 ? 0.2065 0.1737 0.1778 0.0254  0.0179  0.0246  132 PHE   B CE2 
6343 C CZ  . PHE   B 132 ? 0.2125 0.1652 0.2141 0.0165  0.0081  0.0314  132 PHE   B CZ  
6353 N N   . GLY   B 133 ? 0.2457 0.1691 0.2630 0.0050  0.0541  0.0333  133 GLY   B N   
6354 C CA  . GLY   B 133 ? 0.2592 0.1746 0.2849 -0.0166 0.0491  0.0451  133 GLY   B CA  
6355 C C   . GLY   B 133 ? 0.2622 0.1807 0.2907 -0.0316 0.0607  0.0505  133 GLY   B C   
6356 O O   . GLY   B 133 ? 0.2789 0.2014 0.3297 -0.0482 0.0584  0.0516  133 GLY   B O   
6360 N N   . ALA   B 134 ? 0.2435 0.1755 0.2625 -0.0276 0.0634  0.0319  134 ALA   B N   
6361 C CA  . ALA   B 134 ? 0.2405 0.1737 0.2706 -0.0207 0.0635  0.0181  134 ALA   B CA  
6362 C C   . ALA   B 134 ? 0.2454 0.1576 0.2569 -0.0131 0.0552  0.0334  134 ALA   B C   
6363 O O   . ALA   B 134 ? 0.2478 0.1897 0.2738 -0.0002 0.0434  0.0258  134 ALA   B O   
6364 C CB  . ALA   B 134 ? 0.2398 0.1770 0.2918 -0.0209 0.0466  0.0132  134 ALA   B CB  
6370 N N   . ASP   B 135 ? 0.2523 0.1625 0.2602 -0.0132 0.0339  0.0376  135 ASP   B N   
6371 C CA  . ASP   B 135 ? 0.2665 0.1539 0.2829 -0.0092 0.0170  0.0455  135 ASP   B CA  
6372 C C   . ASP   B 135 ? 0.2461 0.1422 0.2638 0.0003  0.0165  0.0453  135 ASP   B C   
6373 O O   . ASP   B 135 ? 0.2334 0.1478 0.2739 -0.0027 0.0220  0.0441  135 ASP   B O   
6374 C CB  . ASP   B 135 ? 0.2969 0.1649 0.3095 -0.0332 0.0127  0.0495  135 ASP   B CB  
6375 C CG  . ASP   B 135 ? 0.3219 0.1686 0.3552 -0.0526 0.0030  0.0349  135 ASP   B CG  
6376 O OD1 . ASP   B 135 ? 0.3269 0.1599 0.3546 -0.0378 -0.0044 0.0343  135 ASP   B OD1 
6377 O OD2 . ASP   B 135 ? 0.3414 0.1985 0.4107 -0.0664 0.0020  0.0114  135 ASP   B OD2 
6382 N N   . PRO   B 136 ? 0.2343 0.1502 0.2752 0.0150  -0.0031 0.0324  136 PRO   B N   
6383 C CA  . PRO   B 136 ? 0.2086 0.1469 0.2724 0.0167  -0.0075 0.0207  136 PRO   B CA  
6384 C C   . PRO   B 136 ? 0.1857 0.1302 0.2767 0.0134  -0.0019 0.0186  136 PRO   B C   
6385 O O   . PRO   B 136 ? 0.1644 0.1273 0.2678 0.0121  -0.0030 0.0124  136 PRO   B O   
6386 C CB  . PRO   B 136 ? 0.2160 0.1669 0.2864 0.0310  -0.0099 0.0122  136 PRO   B CB  
6387 C CG  . PRO   B 136 ? 0.2408 0.1751 0.3057 0.0319  -0.0012 0.0095  136 PRO   B CG  
6388 C CD  . PRO   B 136 ? 0.2449 0.1643 0.2943 0.0337  0.0008  0.0243  136 PRO   B CD  
6396 N N   . ILE   B 137 ? 0.1988 0.1163 0.2897 0.0090  0.0013  0.0170  137 ILE   B N   
6397 C CA  . ILE   B 137 ? 0.2050 0.1186 0.3024 -0.0018 0.0034  0.0016  137 ILE   B CA  
6398 C C   . ILE   B 137 ? 0.1909 0.1246 0.2925 -0.0053 0.0193  0.0118  137 ILE   B C   
6399 O O   . ILE   B 137 ? 0.1804 0.1296 0.2842 -0.0060 0.0185  0.0109  137 ILE   B O   
6400 C CB  . ILE   B 137 ? 0.2338 0.1266 0.3474 -0.0010 0.0018  0.0083  137 ILE   B CB  
6401 C CG1 . ILE   B 137 ? 0.2623 0.1450 0.3886 0.0118  0.0046  -0.0054 137 ILE   B CG1 
6402 C CG2 . ILE   B 137 ? 0.2403 0.1322 0.3558 -0.0266 0.0038  0.0123  137 ILE   B CG2 
6403 C CD1 . ILE   B 137 ? 0.2843 0.1703 0.4182 0.0198  -0.0027 0.0019  137 ILE   B CD1 
6415 N N   . HIS   B 138 ? 0.1959 0.1216 0.3004 -0.0053 0.0314  0.0123  138 HIS   B N   
6416 C CA  . HIS   B 138 ? 0.2101 0.1291 0.2914 -0.0057 0.0462  0.0228  138 HIS   B CA  
6417 C C   . HIS   B 138 ? 0.1888 0.1296 0.2799 -0.0077 0.0439  0.0292  138 HIS   B C   
6418 O O   . HIS   B 138 ? 0.1840 0.1387 0.3009 -0.0015 0.0491  0.0377  138 HIS   B O   
6419 C CB  . HIS   B 138 ? 0.2467 0.1416 0.3057 -0.0118 0.0664  0.0315  138 HIS   B CB  
6420 C CG  . HIS   B 138 ? 0.2729 0.1617 0.3145 -0.0095 0.0804  0.0439  138 HIS   B CG  
6421 N ND1 . HIS   B 138 ? 0.2818 0.1826 0.3391 -0.0040 0.0919  0.0357  138 HIS   B ND1 
6422 C CD2 . HIS   B 138 ? 0.2895 0.1683 0.3085 -0.0115 0.0843  0.0381  138 HIS   B CD2 
6423 C CE1 . HIS   B 138 ? 0.2900 0.1800 0.3319 0.0015  0.0939  0.0347  138 HIS   B CE1 
6424 N NE2 . HIS   B 138 ? 0.2977 0.1676 0.3100 0.0033  0.0907  0.0219  138 HIS   B NE2 
6432 N N   . SER   B 139 ? 0.1815 0.1260 0.2724 0.0022  0.0352  0.0190  139 SER   B N   
6433 C CA  . SER   B 139 ? 0.1819 0.1136 0.2450 -0.0009 0.0339  0.0094  139 SER   B CA  
6434 C C   . SER   B 139 ? 0.1565 0.1100 0.2360 -0.0043 0.0271  0.0067  139 SER   B C   
6435 O O   . SER   B 139 ? 0.1531 0.1137 0.2473 -0.0036 0.0120  0.0076  139 SER   B O   
6436 C CB  . SER   B 139 ? 0.1884 0.1145 0.2476 -0.0033 0.0153  0.0040  139 SER   B CB  
6437 O OG  . SER   B 139 ? 0.1825 0.1203 0.2514 -0.0027 -0.0058 0.0225  139 SER   B OG  
6443 N N   . LEU   B 140 ? 0.1559 0.1071 0.2427 -0.0060 0.0277  0.0056  140 LEU   B N   
6444 C CA  . LEU   B 140 ? 0.1497 0.1153 0.2421 -0.0037 0.0230  0.0079  140 LEU   B CA  
6445 C C   . LEU   B 140 ? 0.1446 0.1156 0.2617 -0.0068 0.0162  -0.0010 140 LEU   B C   
6446 O O   . LEU   B 140 ? 0.1404 0.1196 0.2520 -0.0042 0.0054  0.0103  140 LEU   B O   
6447 C CB  . LEU   B 140 ? 0.1536 0.1197 0.2462 -0.0121 0.0293  0.0081  140 LEU   B CB  
6448 C CG  . LEU   B 140 ? 0.1607 0.1178 0.2476 -0.0113 0.0102  0.0121  140 LEU   B CG  
6449 C CD1 . LEU   B 140 ? 0.1690 0.1225 0.2662 -0.0104 0.0204  -0.0037 140 LEU   B CD1 
6450 C CD2 . LEU   B 140 ? 0.1825 0.1239 0.2607 -0.0041 0.0091  -0.0029 140 LEU   B CD2 
6462 N N   . ARG   B 141 ? 0.1489 0.1125 0.2822 -0.0130 0.0218  -0.0028 141 ARG   B N   
6463 C CA  . ARG   B 141 ? 0.1471 0.1119 0.3179 -0.0181 0.0378  -0.0013 141 ARG   B CA  
6464 C C   . ARG   B 141 ? 0.1410 0.1115 0.2999 -0.0154 0.0260  -0.0032 141 ARG   B C   
6465 O O   . ARG   B 141 ? 0.1475 0.1160 0.2987 -0.0121 0.0123  -0.0138 141 ARG   B O   
6466 C CB  . ARG   B 141 ? 0.1621 0.1296 0.3396 -0.0265 0.0372  -0.0019 141 ARG   B CB  
6467 C CG  . ARG   B 141 ? 0.1948 0.1605 0.3548 -0.0316 0.0389  -0.0034 141 ARG   B CG  
6468 C CD  . ARG   B 141 ? 0.2526 0.1855 0.3483 -0.0285 0.0258  -0.0137 141 ARG   B CD  
6469 N NE  . ARG   B 141 ? 0.2849 0.1862 0.3353 -0.0481 0.0301  -0.0131 141 ARG   B NE  
6470 C CZ  . ARG   B 141 ? 0.3045 0.1693 0.3041 -0.0442 0.0312  -0.0305 141 ARG   B CZ  
6471 N NH1 . ARG   B 141 ? 0.3220 0.1647 0.2873 -0.0348 0.0279  -0.0249 141 ARG   B NH1 
6472 N NH2 . ARG   B 141 ? 0.3154 0.1767 0.3117 -0.0280 0.0208  -0.0208 141 ARG   B NH2 
6486 N N   . VAL   B 142 ? 0.1472 0.1100 0.2861 -0.0110 0.0290  -0.0039 142 VAL   B N   
6487 C CA  . VAL   B 142 ? 0.1384 0.1141 0.2751 -0.0038 0.0320  -0.0032 142 VAL   B CA  
6488 C C   . VAL   B 142 ? 0.1321 0.1151 0.2632 -0.0082 0.0164  -0.0061 142 VAL   B C   
6489 O O   . VAL   B 142 ? 0.1406 0.1138 0.2734 -0.0006 0.0190  0.0024  142 VAL   B O   
6490 C CB  . VAL   B 142 ? 0.1516 0.1275 0.2703 -0.0033 0.0305  0.0034  142 VAL   B CB  
6491 C CG1 . VAL   B 142 ? 0.1519 0.1293 0.2757 0.0026  0.0247  -0.0072 142 VAL   B CG1 
6492 C CG2 . VAL   B 142 ? 0.1790 0.1291 0.2762 0.0026  0.0281  0.0121  142 VAL   B CG2 
6502 N N   . CYS   B 143 ? 0.1327 0.1203 0.2469 -0.0068 0.0129  0.0052  143 CYS   B N   
6503 C CA  . CYS   B 143 ? 0.1318 0.1216 0.2437 -0.0138 0.0139  0.0033  143 CYS   B CA  
6504 C C   . CYS   B 143 ? 0.1318 0.1211 0.2551 -0.0138 0.0043  -0.0016 143 CYS   B C   
6505 O O   . CYS   B 143 ? 0.1288 0.1197 0.2613 -0.0065 -0.0077 -0.0014 143 CYS   B O   
6506 C CB  . CYS   B 143 ? 0.1379 0.1248 0.2339 -0.0135 0.0021  0.0091  143 CYS   B CB  
6507 S SG  . CYS   B 143 ? 0.1432 0.1377 0.2274 -0.0065 0.0059  0.0060  143 CYS   B SG  
6513 N N   . VAL   B 144 ? 0.1345 0.1191 0.2731 -0.0117 -0.0027 -0.0124 144 VAL   B N   
6514 C CA  . VAL   B 144 ? 0.1444 0.1294 0.2925 -0.0166 -0.0101 -0.0280 144 VAL   B CA  
6515 C C   . VAL   B 144 ? 0.1390 0.1293 0.2935 -0.0104 -0.0037 0.0013  144 VAL   B C   
6516 O O   . VAL   B 144 ? 0.1497 0.1556 0.3103 0.0071  0.0010  0.0204  144 VAL   B O   
6517 C CB  . VAL   B 144 ? 0.1717 0.1472 0.3398 -0.0160 -0.0151 -0.0382 144 VAL   B CB  
6518 C CG1 . VAL   B 144 ? 0.1899 0.1807 0.3692 -0.0133 -0.0249 -0.0313 144 VAL   B CG1 
6519 C CG2 . VAL   B 144 ? 0.1834 0.1550 0.3277 -0.0083 -0.0329 -0.0439 144 VAL   B CG2 
6529 N N   . ASP   B 145 ? 0.1397 0.1225 0.3003 -0.0139 0.0069  -0.0129 145 ASP   B N   
6530 C CA  . ASP   B 145 ? 0.1376 0.1306 0.3373 -0.0092 0.0159  -0.0052 145 ASP   B CA  
6531 C C   . ASP   B 145 ? 0.1328 0.1322 0.3218 -0.0111 0.0116  -0.0065 145 ASP   B C   
6532 O O   . ASP   B 145 ? 0.1319 0.1458 0.3748 -0.0169 0.0115  -0.0217 145 ASP   B O   
6533 C CB  . ASP   B 145 ? 0.1518 0.1403 0.3804 -0.0210 0.0297  0.0152  145 ASP   B CB  
6534 C CG  . ASP   B 145 ? 0.1674 0.1495 0.4314 -0.0293 0.0285  0.0089  145 ASP   B CG  
6535 O OD1 . ASP   B 145 ? 0.1688 0.1472 0.4344 -0.0292 -0.0070 0.0021  145 ASP   B OD1 
6536 O OD2 . ASP   B 145 ? 0.1922 0.1615 0.4690 -0.0378 0.0474  0.0113  145 ASP   B OD2 
6541 N N   . THR   B 146 ? 0.1259 0.1168 0.2793 -0.0103 0.0031  0.0046  146 THR   B N   
6542 C CA  . THR   B 146 ? 0.1319 0.1192 0.2561 -0.0043 0.0150  0.0019  146 THR   B CA  
6543 C C   . THR   B 146 ? 0.1332 0.1176 0.2340 -0.0065 0.0041  -0.0001 146 THR   B C   
6544 O O   . THR   B 146 ? 0.1392 0.1195 0.2362 -0.0072 -0.0008 -0.0008 146 THR   B O   
6545 C CB  . THR   B 146 ? 0.1371 0.1163 0.2551 -0.0029 0.0256  0.0012  146 THR   B CB  
6546 O OG1 . THR   B 146 ? 0.1421 0.1194 0.2595 -0.0059 0.0289  0.0169  146 THR   B OG1 
6547 C CG2 . THR   B 146 ? 0.1502 0.1313 0.2477 -0.0039 0.0274  -0.0067 146 THR   B CG2 
6555 N N   . VAL   B 147 ? 0.1374 0.1235 0.2212 -0.0106 0.0181  -0.0008 147 VAL   B N   
6556 C CA  . VAL   B 147 ? 0.1378 0.1205 0.2200 -0.0166 0.0000  -0.0035 147 VAL   B CA  
6557 C C   . VAL   B 147 ? 0.1399 0.1184 0.2324 -0.0219 -0.0122 -0.0004 147 VAL   B C   
6558 O O   . VAL   B 147 ? 0.1482 0.1293 0.2475 -0.0219 -0.0285 -0.0024 147 VAL   B O   
6559 C CB  . VAL   B 147 ? 0.1323 0.1306 0.2036 -0.0110 -0.0086 0.0019  147 VAL   B CB  
6560 C CG1 . VAL   B 147 ? 0.1337 0.1473 0.1941 -0.0114 -0.0094 0.0007  147 VAL   B CG1 
6561 C CG2 . VAL   B 147 ? 0.1389 0.1300 0.2139 -0.0178 0.0050  0.0037  147 VAL   B CG2 
6571 N N   . ARG   B 148 ? 0.1389 0.1241 0.2211 -0.0156 -0.0206 -0.0085 148 ARG   B N   
6572 C CA  . ARG   B 148 ? 0.1434 0.1315 0.2084 -0.0110 -0.0307 -0.0138 148 ARG   B CA  
6573 C C   . ARG   B 148 ? 0.1396 0.1377 0.1912 -0.0128 -0.0344 -0.0046 148 ARG   B C   
6574 O O   . ARG   B 148 ? 0.1652 0.1691 0.1986 -0.0278 -0.0397 0.0049  148 ARG   B O   
6575 C CB  . ARG   B 148 ? 0.1498 0.1341 0.2210 -0.0065 -0.0291 -0.0155 148 ARG   B CB  
6576 C CG  . ARG   B 148 ? 0.1513 0.1537 0.2322 -0.0070 -0.0277 -0.0354 148 ARG   B CG  
6577 C CD  . ARG   B 148 ? 0.1581 0.1761 0.2454 0.0060  -0.0380 -0.0416 148 ARG   B CD  
6578 N NE  . ARG   B 148 ? 0.1624 0.1782 0.2428 0.0196  -0.0308 -0.0380 148 ARG   B NE  
6579 C CZ  . ARG   B 148 ? 0.1537 0.1634 0.2283 0.0169  -0.0244 -0.0309 148 ARG   B CZ  
6580 N NH1 . ARG   B 148 ? 0.1488 0.1626 0.2387 -0.0002 -0.0102 -0.0320 148 ARG   B NH1 
6581 N NH2 . ARG   B 148 ? 0.1701 0.1508 0.2255 0.0217  -0.0245 -0.0233 148 ARG   B NH2 
6595 N N   . THR   B 149 ? 0.1454 0.1291 0.2023 -0.0183 -0.0345 0.0070  149 THR   B N   
6596 C CA  . THR   B 149 ? 0.1551 0.1260 0.1936 -0.0210 -0.0305 0.0138  149 THR   B CA  
6597 C C   . THR   B 149 ? 0.1541 0.1298 0.1855 -0.0243 -0.0329 0.0064  149 THR   B C   
6598 O O   . THR   B 149 ? 0.1614 0.1316 0.1923 -0.0233 -0.0155 0.0049  149 THR   B O   
6599 C CB  . THR   B 149 ? 0.1592 0.1322 0.1988 -0.0213 -0.0285 0.0104  149 THR   B CB  
6600 O OG1 . THR   B 149 ? 0.1535 0.1345 0.1943 -0.0218 -0.0288 0.0029  149 THR   B OG1 
6601 C CG2 . THR   B 149 ? 0.1754 0.1346 0.2193 -0.0139 -0.0299 0.0038  149 THR   B CG2 
6609 N N   . ASN   B 150 ? 0.1609 0.1292 0.1631 -0.0202 -0.0376 0.0037  150 ASN   B N   
6610 C CA  . ASN   B 150 ? 0.1678 0.1535 0.1642 -0.0267 -0.0352 0.0007  150 ASN   B CA  
6611 C C   . ASN   B 150 ? 0.1538 0.1472 0.1625 -0.0164 -0.0309 -0.0028 150 ASN   B C   
6612 O O   . ASN   B 150 ? 0.1587 0.1420 0.1860 -0.0288 -0.0467 0.0052  150 ASN   B O   
6613 C CB  . ASN   B 150 ? 0.1932 0.1912 0.1667 -0.0320 -0.0413 0.0135  150 ASN   B CB  
6614 C CG  . ASN   B 150 ? 0.2206 0.2295 0.2068 -0.0290 -0.0548 0.0366  150 ASN   B CG  
6615 O OD1 . ASN   B 150 ? 0.2300 0.2480 0.2282 -0.0385 -0.0738 0.0332  150 ASN   B OD1 
6616 N ND2 . ASN   B 150 ? 0.2400 0.2518 0.2483 -0.0174 -0.0637 0.0776  150 ASN   B ND2 
6623 N N   . VAL   B 151 ? 0.1505 0.1385 0.1652 -0.0247 -0.0353 0.0071  151 VAL   B N   
6624 C CA  . VAL   B 151 ? 0.1556 0.1363 0.1682 -0.0304 -0.0216 0.0091  151 VAL   B CA  
6625 C C   . VAL   B 151 ? 0.1594 0.1310 0.1629 -0.0388 -0.0298 0.0060  151 VAL   B C   
6626 O O   . VAL   B 151 ? 0.1622 0.1454 0.1910 -0.0306 -0.0299 -0.0035 151 VAL   B O   
6627 C CB  . VAL   B 151 ? 0.1764 0.1439 0.1760 -0.0151 -0.0187 0.0021  151 VAL   B CB  
6628 C CG1 . VAL   B 151 ? 0.1881 0.1554 0.2034 -0.0218 -0.0088 -0.0068 151 VAL   B CG1 
6629 C CG2 . VAL   B 151 ? 0.1867 0.1614 0.1565 -0.0006 -0.0113 0.0092  151 VAL   B CG2 
6639 N N   . TYR   B 152 ? 0.1537 0.1270 0.1607 -0.0338 -0.0249 -0.0014 152 TYR   B N   
6640 C CA  . TYR   B 152 ? 0.1542 0.1449 0.1534 -0.0367 -0.0207 -0.0064 152 TYR   B CA  
6641 C C   . TYR   B 152 ? 0.1458 0.1278 0.1469 -0.0258 -0.0150 -0.0112 152 TYR   B C   
6642 O O   . TYR   B 152 ? 0.1533 0.1281 0.1592 -0.0284 -0.0191 0.0025  152 TYR   B O   
6643 C CB  . TYR   B 152 ? 0.1665 0.1588 0.1461 -0.0392 -0.0101 0.0100  152 TYR   B CB  
6644 C CG  . TYR   B 152 ? 0.1830 0.1715 0.1525 -0.0541 -0.0139 0.0089  152 TYR   B CG  
6645 C CD1 . TYR   B 152 ? 0.1981 0.1844 0.1384 -0.0482 -0.0281 0.0161  152 TYR   B CD1 
6646 C CD2 . TYR   B 152 ? 0.2075 0.1924 0.1557 -0.0540 -0.0113 0.0045  152 TYR   B CD2 
6647 C CE1 . TYR   B 152 ? 0.2155 0.2073 0.1668 -0.0414 -0.0280 0.0279  152 TYR   B CE1 
6648 C CE2 . TYR   B 152 ? 0.2188 0.2138 0.1585 -0.0516 -0.0231 -0.0035 152 TYR   B CE2 
6649 C CZ  . TYR   B 152 ? 0.2245 0.2307 0.1561 -0.0471 -0.0387 0.0228  152 TYR   B CZ  
6650 O OH  . TYR   B 152 ? 0.2484 0.2672 0.1870 -0.0353 -0.0445 0.0235  152 TYR   B OH  
6660 N N   . LEU   B 153 ? 0.1526 0.1262 0.1500 -0.0317 -0.0109 -0.0071 153 LEU   B N   
6661 C CA  . LEU   B 153 ? 0.1536 0.1201 0.1449 -0.0218 -0.0054 -0.0091 153 LEU   B CA  
6662 C C   . LEU   B 153 ? 0.1581 0.1227 0.1533 -0.0286 -0.0067 -0.0193 153 LEU   B C   
6663 O O   . LEU   B 153 ? 0.1619 0.1491 0.1730 -0.0212 -0.0082 -0.0346 153 LEU   B O   
6664 C CB  . LEU   B 153 ? 0.1530 0.1247 0.1686 -0.0271 0.0022  -0.0044 153 LEU   B CB  
6665 C CG  . LEU   B 153 ? 0.1476 0.1320 0.1896 -0.0240 -0.0072 -0.0058 153 LEU   B CG  
6666 C CD1 . LEU   B 153 ? 0.1534 0.1477 0.2101 -0.0252 -0.0073 0.0067  153 LEU   B CD1 
6667 C CD2 . LEU   B 153 ? 0.1482 0.1391 0.1948 -0.0249 0.0030  0.0067  153 LEU   B CD2 
6679 N N   . ALA   B 154 ? 0.1506 0.1206 0.1730 -0.0117 -0.0031 -0.0205 154 ALA   B N   
6680 C CA  . ALA   B 154 ? 0.1620 0.1315 0.1772 -0.0027 -0.0109 -0.0255 154 ALA   B CA  
6681 C C   . ALA   B 154 ? 0.1753 0.1349 0.1796 0.0015  -0.0178 -0.0276 154 ALA   B C   
6682 O O   . ALA   B 154 ? 0.2042 0.1394 0.1996 0.0065  -0.0063 -0.0035 154 ALA   B O   
6683 C CB  . ALA   B 154 ? 0.1623 0.1515 0.1968 -0.0047 -0.0018 -0.0307 154 ALA   B CB  
6689 N N   . VAL   B 155 ? 0.1414 0.1282 0.2028 -0.0011 -0.0019 -0.0173 155 VAL   B N   
6690 C CA  . VAL   B 155 ? 0.1388 0.1285 0.2307 -0.0081 -0.0061 -0.0082 155 VAL   B CA  
6691 C C   . VAL   B 155 ? 0.1398 0.1317 0.2306 -0.0078 -0.0007 -0.0334 155 VAL   B C   
6692 O O   . VAL   B 155 ? 0.1529 0.1518 0.2708 0.0061  -0.0009 -0.0523 155 VAL   B O   
6693 C CB  . VAL   B 155 ? 0.1426 0.1445 0.2650 -0.0092 -0.0119 0.0099  155 VAL   B CB  
6694 C CG1 . VAL   B 155 ? 0.1464 0.1431 0.2641 -0.0114 -0.0103 0.0097  155 VAL   B CG1 
6695 C CG2 . VAL   B 155 ? 0.1424 0.1592 0.3000 -0.0093 -0.0233 0.0338  155 VAL   B CG2 
6705 N N   . PHE   B 156 ? 0.1331 0.1392 0.2434 0.0007  0.0012  -0.0280 156 PHE   B N   
6706 C CA  . PHE   B 156 ? 0.1378 0.1457 0.2749 0.0081  -0.0010 -0.0310 156 PHE   B CA  
6707 C C   . PHE   B 156 ? 0.1402 0.1577 0.3129 0.0137  -0.0034 -0.0423 156 PHE   B C   
6708 O O   . PHE   B 156 ? 0.1635 0.1769 0.3444 0.0190  0.0040  -0.0519 156 PHE   B O   
6709 C CB  . PHE   B 156 ? 0.1417 0.1414 0.2608 0.0020  -0.0151 -0.0203 156 PHE   B CB  
6710 C CG  . PHE   B 156 ? 0.1441 0.1501 0.2809 -0.0008 -0.0179 -0.0073 156 PHE   B CG  
6711 C CD1 . PHE   B 156 ? 0.1494 0.1738 0.3077 0.0067  -0.0055 0.0199  156 PHE   B CD1 
6712 C CD2 . PHE   B 156 ? 0.1595 0.1625 0.2802 0.0135  -0.0152 -0.0034 156 PHE   B CD2 
6713 C CE1 . PHE   B 156 ? 0.1559 0.1901 0.3207 0.0080  -0.0026 0.0175  156 PHE   B CE1 
6714 C CE2 . PHE   B 156 ? 0.1651 0.1820 0.3008 0.0168  -0.0101 0.0042  156 PHE   B CE2 
6715 C CZ  . PHE   B 156 ? 0.1523 0.1860 0.3188 0.0118  -0.0175 0.0063  156 PHE   B CZ  
6725 N N   . ASP   B 157 ? 0.1426 0.1488 0.3356 0.0147  -0.0214 -0.0278 157 ASP   B N   
6726 C CA  . ASP   B 157 ? 0.1540 0.1553 0.3595 0.0151  -0.0301 -0.0396 157 ASP   B CA  
6727 C C   . ASP   B 157 ? 0.1524 0.1526 0.3664 0.0059  -0.0146 -0.0604 157 ASP   B C   
6728 O O   . ASP   B 157 ? 0.1367 0.1491 0.3592 0.0069  -0.0161 -0.0419 157 ASP   B O   
6729 C CB  . ASP   B 157 ? 0.1929 0.1704 0.3707 0.0107  -0.0548 -0.0211 157 ASP   B CB  
6730 C CG  . ASP   B 157 ? 0.2357 0.1770 0.3957 0.0133  -0.0492 -0.0194 157 ASP   B CG  
6731 O OD1 . ASP   B 157 ? 0.2424 0.1675 0.4181 0.0267  -0.0263 -0.0118 157 ASP   B OD1 
6732 O OD2 . ASP   B 157 ? 0.2719 0.2016 0.4152 0.0066  -0.0404 -0.0127 157 ASP   B OD2 
6737 N N   A LYS   B 158 ? 0.1633 0.1750 0.3555 0.0052  -0.0111 -0.0748 158 LYS   B N   
6738 N N   B LYS   B 158 ? 0.1538 0.1799 0.3703 0.0078  -0.0046 -0.0849 158 LYS   B N   
6739 C CA  A LYS   B 158 ? 0.1811 0.1954 0.3511 0.0059  -0.0074 -0.0849 158 LYS   B CA  
6740 C CA  B LYS   B 158 ? 0.1709 0.2049 0.3697 0.0104  0.0043  -0.1026 158 LYS   B CA  
6741 C C   A LYS   B 158 ? 0.1746 0.1893 0.3656 0.0060  -0.0138 -0.0831 158 LYS   B C   
6742 C C   B LYS   B 158 ? 0.1659 0.1923 0.3823 0.0074  -0.0068 -0.0939 158 LYS   B C   
6743 O O   A LYS   B 158 ? 0.1757 0.1907 0.3579 0.0012  -0.0167 -0.0863 158 LYS   B O   
6744 O O   B LYS   B 158 ? 0.1654 0.1923 0.3877 -0.0030 -0.0125 -0.1022 158 LYS   B O   
6745 C CB  A LYS   B 158 ? 0.2064 0.2230 0.3434 0.0070  -0.0023 -0.0907 158 LYS   B CB  
6746 C CB  B LYS   B 158 ? 0.1984 0.2466 0.3614 0.0164  0.0145  -0.1153 158 LYS   B CB  
6747 C CG  A LYS   B 158 ? 0.2307 0.2509 0.3463 0.0059  -0.0023 -0.0942 158 LYS   B CG  
6748 C CG  B LYS   B 158 ? 0.2283 0.2913 0.3602 0.0171  0.0146  -0.1209 158 LYS   B CG  
6749 C CD  A LYS   B 158 ? 0.2492 0.2753 0.3553 0.0049  -0.0029 -0.0903 158 LYS   B CD  
6750 C CD  B LYS   B 158 ? 0.2522 0.3353 0.3682 0.0144  0.0105  -0.1122 158 LYS   B CD  
6751 C CE  A LYS   B 158 ? 0.2629 0.2930 0.3638 0.0069  -0.0029 -0.0868 158 LYS   B CE  
6752 C CE  B LYS   B 158 ? 0.2704 0.3626 0.3734 0.0181  0.0087  -0.1038 158 LYS   B CE  
6753 N NZ  A LYS   B 158 ? 0.2643 0.3012 0.3666 0.0050  -0.0046 -0.0861 158 LYS   B NZ  
6754 N NZ  B LYS   B 158 ? 0.2719 0.3773 0.3744 0.0174  0.0101  -0.0989 158 LYS   B NZ  
6781 N N   . ASN   B 159 ? 0.1716 0.1837 0.4017 0.0076  -0.0207 -0.0754 159 ASN   B N   
6782 C CA  . ASN   B 159 ? 0.1932 0.1721 0.4357 0.0300  -0.0521 -0.0623 159 ASN   B CA  
6783 C C   . ASN   B 159 ? 0.1749 0.1514 0.4254 0.0223  -0.0563 -0.0503 159 ASN   B C   
6784 O O   . ASN   B 159 ? 0.1751 0.1469 0.4419 0.0007  -0.0604 -0.0347 159 ASN   B O   
6785 C CB  . ASN   B 159 ? 0.2287 0.1929 0.4719 0.0551  -0.0660 -0.0655 159 ASN   B CB  
6786 C CG  . ASN   B 159 ? 0.2633 0.2282 0.5080 0.0610  -0.0794 -0.0719 159 ASN   B CG  
6787 O OD1 . ASN   B 159 ? 0.2829 0.2511 0.5201 0.0713  -0.0775 -0.0798 159 ASN   B OD1 
6788 N ND2 . ASN   B 159 ? 0.2637 0.2457 0.5253 0.0701  -0.0936 -0.0705 159 ASN   B ND2 
6796 N N   . LEU   B 160 ? 0.1651 0.1420 0.3868 0.0139  -0.0553 -0.0452 160 LEU   B N   
6797 C CA  . LEU   B 160 ? 0.1590 0.1447 0.3557 0.0105  -0.0356 -0.0225 160 LEU   B CA  
6798 C C   . LEU   B 160 ? 0.1470 0.1395 0.3480 0.0009  -0.0181 -0.0307 160 LEU   B C   
6799 O O   . LEU   B 160 ? 0.1332 0.1473 0.3445 -0.0023 -0.0290 -0.0129 160 LEU   B O   
6800 C CB  . LEU   B 160 ? 0.1548 0.1563 0.3365 0.0061  -0.0315 -0.0142 160 LEU   B CB  
6801 C CG  . LEU   B 160 ? 0.1585 0.1681 0.3145 0.0040  -0.0281 -0.0039 160 LEU   B CG  
6802 C CD1 . LEU   B 160 ? 0.1745 0.1888 0.3135 -0.0042 -0.0124 -0.0007 160 LEU   B CD1 
6803 C CD2 . LEU   B 160 ? 0.1639 0.1700 0.3176 0.0141  -0.0375 -0.0110 160 LEU   B CD2 
6815 N N   . TYR   B 161 ? 0.1506 0.1443 0.3476 -0.0078 0.0002  -0.0440 161 TYR   B N   
6816 C CA  . TYR   B 161 ? 0.1594 0.1487 0.3254 -0.0182 0.0215  -0.0451 161 TYR   B CA  
6817 C C   . TYR   B 161 ? 0.1656 0.1457 0.3108 -0.0146 0.0251  -0.0356 161 TYR   B C   
6818 O O   . TYR   B 161 ? 0.1662 0.1466 0.2890 -0.0233 0.0119  -0.0324 161 TYR   B O   
6819 C CB  . TYR   B 161 ? 0.1726 0.1574 0.3293 -0.0283 0.0352  -0.0529 161 TYR   B CB  
6820 C CG  . TYR   B 161 ? 0.2065 0.1557 0.3221 -0.0407 0.0408  -0.0549 161 TYR   B CG  
6821 C CD1 . TYR   B 161 ? 0.2178 0.1542 0.3199 -0.0427 0.0434  -0.0583 161 TYR   B CD1 
6822 C CD2 . TYR   B 161 ? 0.2307 0.1635 0.3145 -0.0305 0.0407  -0.0601 161 TYR   B CD2 
6823 C CE1 . TYR   B 161 ? 0.2363 0.1782 0.3241 -0.0457 0.0476  -0.0554 161 TYR   B CE1 
6824 C CE2 . TYR   B 161 ? 0.2483 0.1807 0.3213 -0.0353 0.0468  -0.0524 161 TYR   B CE2 
6825 C CZ  . TYR   B 161 ? 0.2499 0.1866 0.3181 -0.0527 0.0397  -0.0482 161 TYR   B CZ  
6826 O OH  . TYR   B 161 ? 0.2777 0.2147 0.3403 -0.0586 0.0376  -0.0476 161 TYR   B OH  
6836 N N   . ASP   B 162 ? 0.1688 0.1448 0.3295 -0.0102 0.0043  -0.0536 162 ASP   B N   
6837 C CA  . ASP   B 162 ? 0.1723 0.1513 0.3370 -0.0092 -0.0036 -0.0509 162 ASP   B CA  
6838 C C   . ASP   B 162 ? 0.1701 0.1441 0.3331 -0.0094 -0.0087 -0.0417 162 ASP   B C   
6839 O O   . ASP   B 162 ? 0.1744 0.1504 0.3437 -0.0214 -0.0239 -0.0303 162 ASP   B O   
6840 C CB  . ASP   B 162 ? 0.1917 0.1663 0.3577 -0.0028 -0.0104 -0.0695 162 ASP   B CB  
6841 C CG  . ASP   B 162 ? 0.1989 0.1900 0.3788 0.0022  -0.0087 -0.0905 162 ASP   B CG  
6842 O OD1 . ASP   B 162 ? 0.2014 0.2170 0.3711 -0.0133 0.0080  -0.0894 162 ASP   B OD1 
6843 O OD2 . ASP   B 162 ? 0.2065 0.2178 0.4098 0.0218  -0.0068 -0.0851 162 ASP   B OD2 
6848 N N   . LYS   B 163 ? 0.1702 0.1302 0.3255 -0.0137 -0.0152 -0.0248 163 LYS   B N   
6849 C CA  . LYS   B 163 ? 0.1790 0.1413 0.3312 -0.0195 -0.0117 -0.0145 163 LYS   B CA  
6850 C C   . LYS   B 163 ? 0.1516 0.1357 0.3152 -0.0157 -0.0140 -0.0001 163 LYS   B C   
6851 O O   . LYS   B 163 ? 0.1576 0.1455 0.3384 -0.0230 -0.0219 0.0179  163 LYS   B O   
6852 C CB  . LYS   B 163 ? 0.2305 0.1712 0.3694 -0.0181 -0.0132 0.0077  163 LYS   B CB  
6853 C CG  . LYS   B 163 ? 0.3161 0.2555 0.4296 -0.0231 0.0068  0.0127  163 LYS   B CG  
6854 C CD  . LYS   B 163 ? 0.3917 0.3285 0.4861 -0.0327 0.0172  0.0196  163 LYS   B CD  
6855 C CE  . LYS   B 163 ? 0.4486 0.3728 0.5232 -0.0416 0.0257  0.0253  163 LYS   B CE  
6856 N NZ  . LYS   B 163 ? 0.4804 0.4046 0.5448 -0.0476 0.0305  0.0238  163 LYS   B NZ  
6870 N N   . LEU   B 164 ? 0.1400 0.1260 0.2832 -0.0144 -0.0123 0.0011  164 LEU   B N   
6871 C CA  . LEU   B 164 ? 0.1386 0.1286 0.2679 -0.0160 -0.0230 0.0068  164 LEU   B CA  
6872 C C   . LEU   B 164 ? 0.1472 0.1347 0.2784 -0.0188 -0.0296 0.0101  164 LEU   B C   
6873 O O   . LEU   B 164 ? 0.1538 0.1584 0.2904 -0.0174 -0.0302 0.0148  164 LEU   B O   
6874 C CB  . LEU   B 164 ? 0.1372 0.1314 0.2671 -0.0118 -0.0136 0.0011  164 LEU   B CB  
6875 C CG  . LEU   B 164 ? 0.1458 0.1514 0.2671 -0.0166 -0.0122 0.0067  164 LEU   B CG  
6876 C CD1 . LEU   B 164 ? 0.1601 0.1469 0.2499 -0.0152 -0.0194 -0.0087 164 LEU   B CD1 
6877 C CD2 . LEU   B 164 ? 0.1585 0.1874 0.2824 -0.0117 -0.0003 -0.0059 164 LEU   B CD2 
6889 N N   . VAL   B 165 ? 0.1806 0.1441 0.2934 -0.0287 -0.0390 -0.0022 165 VAL   B N   
6890 C CA  . VAL   B 165 ? 0.2249 0.1513 0.3108 -0.0423 -0.0669 -0.0015 165 VAL   B CA  
6891 C C   . VAL   B 165 ? 0.2614 0.1681 0.3431 -0.0538 -0.0916 0.0119  165 VAL   B C   
6892 O O   . VAL   B 165 ? 0.2811 0.1897 0.3523 -0.0562 -0.1023 0.0108  165 VAL   B O   
6893 C CB  . VAL   B 165 ? 0.2487 0.1636 0.3119 -0.0256 -0.0409 -0.0144 165 VAL   B CB  
6894 C CG1 . VAL   B 165 ? 0.2712 0.1716 0.3396 -0.0221 -0.0351 -0.0112 165 VAL   B CG1 
6895 C CG2 . VAL   B 165 ? 0.2472 0.1780 0.3082 -0.0198 -0.0193 -0.0145 165 VAL   B CG2 
6905 N N   . SER   B 166 ? 0.2745 0.1574 0.3788 -0.0475 -0.1071 -0.0063 166 SER   B N   
6906 C CA  . SER   B 166 ? 0.2643 0.1568 0.4337 -0.0483 -0.0939 -0.0225 166 SER   B CA  
6907 C C   . SER   B 166 ? 0.2484 0.1687 0.4484 -0.0502 -0.0857 -0.0021 166 SER   B C   
6908 O O   . SER   B 166 ? 0.2473 0.1926 0.4709 -0.0614 -0.0944 -0.0278 166 SER   B O   
6909 C CB  . SER   B 166 ? 0.2607 0.1656 0.4665 -0.0373 -0.0888 -0.0302 166 SER   B CB  
6910 O OG  . SER   B 166 ? 0.2468 0.1651 0.4851 -0.0249 -0.0910 -0.0149 166 SER   B OG  
6916 N N   . SER   B 167 ? 0.2247 0.1529 0.4197 -0.0501 -0.0825 0.0379  167 SER   B N   
6917 C CA  . SER   B 167 ? 0.2108 0.1620 0.4065 -0.0408 -0.0549 0.0429  167 SER   B CA  
6918 C C   . SER   B 167 ? 0.1988 0.1768 0.3786 -0.0536 -0.0564 0.0558  167 SER   B C   
6919 O O   . SER   B 167 ? 0.1966 0.1881 0.3852 -0.0490 -0.0558 0.0510  167 SER   B O   
6920 C CB  . SER   B 167 ? 0.1954 0.1738 0.4282 -0.0363 -0.0188 0.0342  167 SER   B CB  
6921 O OG  . SER   B 167 ? 0.1830 0.1865 0.4305 -0.0275 0.0015  0.0328  167 SER   B OG  
6927 N N   . PHE   B 168 ? 0.2039 0.1820 0.3634 -0.0508 -0.0438 0.0609  168 PHE   B N   
6928 C CA  . PHE   B 168 ? 0.2036 0.1835 0.3279 -0.0515 -0.0322 0.0322  168 PHE   B CA  
6929 C C   . PHE   B 168 ? 0.1768 0.1626 0.2574 -0.0292 -0.0161 0.0192  168 PHE   B C   
6930 O O   . PHE   B 168 ? 0.2159 0.1550 0.2444 -0.0031 -0.0086 -0.0034 168 PHE   B O   
6931 C CB  . PHE   B 168 ? 0.2131 0.1909 0.3380 -0.0599 -0.0458 0.0457  168 PHE   B CB  
6932 C CG  . PHE   B 168 ? 0.2412 0.1710 0.3379 -0.0568 -0.0428 0.0171  168 PHE   B CG  
6933 C CD1 . PHE   B 168 ? 0.2680 0.1708 0.3555 -0.0544 -0.0439 0.0105  168 PHE   B CD1 
6934 C CD2 . PHE   B 168 ? 0.2276 0.1545 0.3378 -0.0423 -0.0374 0.0243  168 PHE   B CD2 
6935 C CE1 . PHE   B 168 ? 0.2754 0.1730 0.3484 -0.0425 -0.0382 0.0263  168 PHE   B CE1 
6936 C CE2 . PHE   B 168 ? 0.2563 0.1585 0.3405 -0.0200 -0.0404 0.0151  168 PHE   B CE2 
6937 C CZ  . PHE   B 168 ? 0.2650 0.1485 0.3420 -0.0172 -0.0483 0.0358  168 PHE   B CZ  
6947 N N   . LEU   B 169 ? 0.1791 0.1671 0.2464 -0.0064 -0.0030 -0.0006 169 LEU   B N   
6948 C CA  . LEU   B 169 ? 0.2151 0.1984 0.2732 -0.0033 0.0041  -0.0281 169 LEU   B CA  
6949 C C   . LEU   B 169 ? 0.2512 0.2270 0.3262 0.0103  -0.0003 -0.0548 169 LEU   B C   
6950 O O   . LEU   B 169 ? 0.2743 0.2469 0.3769 0.0034  -0.0062 -0.0814 169 LEU   B O   
6951 C CB  . LEU   B 169 ? 0.2359 0.2405 0.2879 -0.0105 -0.0109 -0.0040 169 LEU   B CB  
6952 C CG  . LEU   B 169 ? 0.2797 0.2778 0.3360 -0.0034 -0.0131 -0.0033 169 LEU   B CG  
6953 C CD1 . LEU   B 169 ? 0.2933 0.2926 0.3393 -0.0051 -0.0168 0.0101  169 LEU   B CD1 
6954 C CD2 . LEU   B 169 ? 0.2768 0.2831 0.3420 0.0080  -0.0031 -0.0171 169 LEU   B CD2 
6955 O OXT . LEU   B 169 ? 0.2714 0.2469 0.3264 0.0421  0.0078  -0.0466 169 LEU   B OXT 
6967 N N2  B A1A6Z C .   ? 0.1160 0.1101 0.1943 -0.0029 -0.0165 0.0299  201 A1A6Z A N2  
6968 C C3  B A1A6Z C .   ? 0.1711 0.1489 0.2177 0.0007  -0.0285 0.0293  201 A1A6Z A C3  
6969 C C6  B A1A6Z C .   ? 0.1630 0.1189 0.1917 -0.0005 -0.0010 0.0125  201 A1A6Z A C6  
6970 C C9  B A1A6Z C .   ? 0.1125 0.1058 0.1619 0.0038  0.0123  0.0168  201 A1A6Z A C9  
6971 C C12 B A1A6Z C .   ? 0.1199 0.1182 0.1293 -0.0025 -0.0062 0.0177  201 A1A6Z A C12 
6972 C C1  B A1A6Z C .   ? 0.2033 0.1422 0.1823 0.0022  -0.0348 0.0103  201 A1A6Z A C1  
6973 C C10 B A1A6Z C .   ? 0.1122 0.1074 0.1703 0.0028  -0.0118 0.0126  201 A1A6Z A C10 
6974 C C11 B A1A6Z C .   ? 0.1183 0.1139 0.1493 -0.0007 -0.0026 0.0246  201 A1A6Z A C11 
6975 C C13 B A1A6Z C .   ? 0.1524 0.1154 0.1706 -0.0044 -0.0066 0.0142  201 A1A6Z A C13 
6976 C C2  B A1A6Z C .   ? 0.1769 0.1323 0.1798 -0.0034 -0.0201 0.0218  201 A1A6Z A C2  
6977 C C4  B A1A6Z C .   ? 0.1874 0.1352 0.1856 -0.0018 -0.0162 0.0101  201 A1A6Z A C4  
6978 C C5  B A1A6Z C .   ? 0.1639 0.1195 0.1779 -0.0004 -0.0187 0.0124  201 A1A6Z A C5  
6979 C C7  B A1A6Z C .   ? 0.1222 0.1088 0.1796 0.0158  -0.0091 0.0140  201 A1A6Z A C7  
6980 C C8  B A1A6Z C .   ? 0.1181 0.1114 0.1811 0.0046  0.0129  0.0465  201 A1A6Z A C8  
6981 N N1  B A1A6Z C .   ? 0.1334 0.1047 0.1721 0.0022  -0.0220 0.0171  201 A1A6Z A N1  
6982 N N3  B A1A6Z C .   ? 0.1282 0.1118 0.1799 0.0019  0.0217  0.0364  201 A1A6Z A N3  
6983 N N4  B A1A6Z C .   ? 0.1253 0.1230 0.1265 0.0044  -0.0026 0.0191  201 A1A6Z A N4  
6984 O O1  B A1A6Z C .   ? 0.1820 0.1450 0.2344 -0.0035 -0.0118 0.0078  201 A1A6Z A O1  
7003 O O   . HOH   D .   ? 0.5315 0.6455 0.5990 -0.1205 -0.1269 -0.0206 301 HOH   A O   
7004 O O   . HOH   D .   ? 0.4236 0.7835 0.6252 -0.0900 -0.1447 0.1972  302 HOH   A O   
7005 O O   . HOH   D .   ? 0.3389 0.2920 0.1937 -0.0634 0.0288  0.0483  303 HOH   A O   
7006 O O   A HOH   D .   ? 0.2969 0.5368 0.3097 -0.0302 0.0256  0.1302  304 HOH   A O   
7007 O O   . HOH   D .   ? 0.4747 0.4852 0.5099 -0.1133 0.1440  0.2083  305 HOH   A O   
7008 O O   . HOH   D .   ? 0.7343 0.2200 0.5016 -0.0809 -0.1385 -0.0194 306 HOH   A O   
7009 O O   . HOH   D .   ? 0.3191 0.2948 0.2482 -0.1380 -0.0742 0.1088  307 HOH   A O   
7010 O O   . HOH   D .   ? 0.3394 0.3443 0.3339 -0.1262 -0.0027 0.1166  308 HOH   A O   
7011 O O   . HOH   D .   ? 0.4422 0.5546 0.4087 -0.1495 0.1150  -0.0065 309 HOH   A O   
7012 O O   . HOH   D .   ? 0.2181 0.2976 0.3199 0.0110  0.0877  0.0129  310 HOH   A O   
7013 O O   . HOH   D .   ? 0.6363 0.4834 0.2799 0.2296  -0.0316 0.0712  311 HOH   A O   
7014 O O   . HOH   D .   ? 0.5826 0.4798 0.6710 -0.0633 0.1759  0.2127  312 HOH   A O   
7015 O O   . HOH   D .   ? 0.7176 0.7248 0.8325 -0.1383 -0.0976 0.1182  313 HOH   A O   
7016 O O   . HOH   D .   ? 0.6754 0.6975 0.6687 -0.0709 0.0934  -0.1130 314 HOH   A O   
7017 O O   . HOH   D .   ? 0.6033 0.6619 0.6328 -0.0372 0.3387  -0.1372 315 HOH   A O   
7018 O O   B HOH   D .   ? 0.4351 0.3381 0.3841 0.1448  -0.0319 -0.1070 316 HOH   A O   
7019 O O   . HOH   D .   ? 0.3005 0.2733 0.6532 -0.0181 -0.1236 0.1652  317 HOH   A O   
7020 O O   . HOH   D .   ? 0.6522 0.6640 0.3694 -0.1194 -0.1017 0.1140  318 HOH   A O   
7021 O O   . HOH   D .   ? 0.3516 0.6806 0.4526 0.0360  -0.0285 0.1454  319 HOH   A O   
7022 O O   . HOH   D .   ? 0.4922 0.5804 0.4466 0.2346  0.0542  -0.1128 320 HOH   A O   
7023 O O   . HOH   D .   ? 0.1813 0.3931 0.2869 0.0537  -0.0097 0.0017  321 HOH   A O   
7024 O O   . HOH   D .   ? 0.2165 0.1843 0.3559 -0.0487 0.0206  -0.0100 322 HOH   A O   
7025 O O   . HOH   D .   ? 0.6381 0.4796 0.5104 -0.0012 -0.0082 -0.0289 323 HOH   A O   
7026 O O   . HOH   D .   ? 0.6604 0.4745 0.5635 -0.1249 0.2019  0.1955  324 HOH   A O   
7027 O O   . HOH   D .   ? 0.4447 0.4002 0.6072 0.1188  -0.0493 0.0955  325 HOH   A O   
7028 O O   . HOH   D .   ? 0.4438 0.3637 0.5845 -0.0232 0.1698  0.0681  326 HOH   A O   
7029 O O   . HOH   D .   ? 0.1928 0.3606 0.3842 -0.0123 0.0299  0.0754  327 HOH   A O   
7030 O O   . HOH   D .   ? 0.2980 0.2757 0.2568 -0.0416 0.0230  -0.0306 328 HOH   A O   
7031 O O   . HOH   D .   ? 0.5537 0.1692 0.3314 0.0034  -0.1507 0.0355  329 HOH   A O   
7032 O O   . HOH   D .   ? 0.2250 0.3437 0.4476 -0.0630 0.0572  -0.0376 330 HOH   A O   
7033 O O   A HOH   D .   ? 0.1613 0.3830 0.2030 0.0909  0.0249  0.0591  331 HOH   A O   
7034 O O   A HOH   D .   ? 0.3050 0.4851 0.3933 -0.0261 -0.0228 -0.0843 332 HOH   A O   
7035 O O   . HOH   D .   ? 0.3225 0.3228 0.7105 0.0941  0.1677  -0.0125 333 HOH   A O   
7036 O O   . HOH   D .   ? 0.5143 0.2020 0.6147 0.0856  -0.0460 -0.0389 334 HOH   A O   
7037 O O   . HOH   D .   ? 0.2523 0.4417 0.3400 0.1259  -0.0576 0.0059  335 HOH   A O   
7038 O O   . HOH   D .   ? 0.4680 0.4315 0.4069 -0.1621 -0.0693 0.2171  336 HOH   A O   
7039 O O   . HOH   D .   ? 0.2454 0.2058 0.2845 0.0573  0.0395  0.0386  337 HOH   A O   
7040 O O   . HOH   D .   ? 0.3503 0.4396 0.2093 -0.0309 0.0658  0.0225  338 HOH   A O   
7041 O O   . HOH   D .   ? 0.3505 0.4841 0.4970 -0.0141 0.1335  -0.0453 339 HOH   A O   
7042 O O   . HOH   D .   ? 0.7327 0.3208 0.3155 0.0920  0.1335  0.0865  340 HOH   A O   
7043 O O   . HOH   D .   ? 0.2226 0.3895 0.3659 -0.0391 -0.0756 0.1359  341 HOH   A O   
7044 O O   . HOH   D .   ? 0.6613 0.7464 0.6637 -0.1010 -0.1343 -0.0584 342 HOH   A O   
7045 O O   . HOH   D .   ? 0.1412 0.2168 0.2107 0.0027  -0.0047 0.0640  343 HOH   A O   
7046 O O   . HOH   D .   ? 0.6697 0.6629 0.3757 0.0657  -0.0354 -0.0625 344 HOH   A O   
7047 O O   B HOH   D .   ? 0.2781 0.3014 0.3481 0.0479  -0.0073 0.0391  345 HOH   A O   
7048 O O   B HOH   D .   ? 0.1356 0.1552 0.1966 0.0238  0.0088  0.0285  346 HOH   A O   
7049 O O   . HOH   D .   ? 0.3120 0.3760 0.4247 -0.0584 -0.0777 -0.1165 347 HOH   A O   
7050 O O   . HOH   D .   ? 0.1701 0.1562 0.2176 0.0124  -0.0285 0.0165  348 HOH   A O   
7051 O O   . HOH   D .   ? 0.4075 0.6149 0.2985 0.1410  0.1130  -0.0233 349 HOH   A O   
7052 O O   . HOH   D .   ? 0.2586 0.4246 0.3093 -0.0339 -0.0241 0.0570  350 HOH   A O   
7053 O O   B HOH   D .   ? 0.2007 0.2145 0.2162 -0.0441 -0.0121 0.0533  351 HOH   A O   
7054 O O   . HOH   D .   ? 0.5140 0.5181 0.4062 0.0245  -0.1582 -0.0373 352 HOH   A O   
7055 O O   . HOH   D .   ? 0.1900 0.1651 0.2382 0.0207  -0.0342 0.0086  353 HOH   A O   
7056 O O   . HOH   D .   ? 0.3341 0.3793 0.3823 -0.1069 -0.0838 -0.0082 354 HOH   A O   
7057 O O   . HOH   D .   ? 0.1393 0.1472 0.1572 -0.0046 -0.0109 0.0039  355 HOH   A O   
7058 O O   B HOH   D .   ? 0.1632 0.1961 0.2447 -0.0179 -0.0019 0.0088  356 HOH   A O   
7059 O O   . HOH   D .   ? 0.1956 0.1983 0.3907 0.0125  0.0907  -0.0339 357 HOH   A O   
7060 O O   . HOH   D .   ? 0.4172 0.2677 0.2529 -0.1000 -0.0096 0.0548  358 HOH   A O   
7061 O O   . HOH   D .   ? 0.3607 0.5077 0.3944 0.2125  0.0884  0.1116  359 HOH   A O   
7062 O O   . HOH   D .   ? 0.1878 0.2402 0.4121 0.0136  0.0839  -0.0700 360 HOH   A O   
7063 O O   B HOH   D .   ? 0.1995 0.2264 0.4335 0.0242  0.0149  0.0137  361 HOH   A O   
7064 O O   . HOH   D .   ? 0.1567 0.1242 0.2229 -0.0072 0.0159  -0.0097 362 HOH   A O   
7065 O O   A HOH   D .   ? 0.3667 0.4189 0.3682 0.0439  -0.0807 -0.0634 363 HOH   A O   
7066 O O   . HOH   D .   ? 0.1419 0.1258 0.1874 -0.0038 0.0040  0.0140  364 HOH   A O   
7067 O O   A HOH   D .   ? 0.1539 0.1764 0.2329 -0.0232 0.0437  0.0862  365 HOH   A O   
7068 O O   . HOH   D .   ? 0.1450 0.1893 0.2508 0.0050  -0.0040 0.0032  366 HOH   A O   
7069 O O   . HOH   D .   ? 0.4508 0.3511 0.4130 -0.0610 -0.0512 -0.0554 367 HOH   A O   
7070 O O   . HOH   D .   ? 0.3659 0.2158 0.5829 -0.0631 0.0097  -0.0043 368 HOH   A O   
7071 O O   . HOH   D .   ? 0.1578 0.1339 0.1728 -0.0213 0.0116  0.0057  369 HOH   A O   
7072 O O   . HOH   D .   ? 0.5879 0.4354 0.3081 0.0177  -0.1193 -0.0357 370 HOH   A O   
7073 O O   . HOH   D .   ? 0.6388 0.5323 0.5324 0.1755  -0.1013 -0.1499 371 HOH   A O   
7074 O O   . HOH   D .   ? 0.3681 0.2347 0.4051 -0.1234 0.1719  -0.0819 372 HOH   A O   
7075 O O   . HOH   D .   ? 0.4134 0.8073 0.6461 -0.1080 -0.1424 -0.0151 373 HOH   A O   
7076 O O   . HOH   D .   ? 0.3474 0.3596 0.2199 -0.0964 -0.0265 -0.0751 374 HOH   A O   
7077 O O   . HOH   D .   ? 0.1617 0.1623 0.2599 -0.0236 0.0137  0.0329  375 HOH   A O   
7078 O O   . HOH   D .   ? 0.4299 0.2158 0.4030 -0.1075 0.1077  0.0191  376 HOH   A O   
7079 O O   . HOH   D .   ? 0.1742 0.1725 0.2561 -0.0163 0.0258  0.0260  377 HOH   A O   
7080 O O   A HOH   D .   ? 0.1433 0.1280 0.2860 0.0187  -0.0781 -0.0262 378 HOH   A O   
7081 O O   . HOH   D .   ? 0.1888 0.2069 0.2519 -0.0121 -0.0253 0.0424  379 HOH   A O   
7082 O O   A HOH   D .   ? 0.3433 0.3718 0.3283 0.0723  0.0158  -0.1069 380 HOH   A O   
7083 O O   . HOH   D .   ? 0.4694 0.7810 0.4370 0.2118  -0.0923 -0.0422 381 HOH   A O   
7084 O O   . HOH   D .   ? 0.3121 0.2673 0.2239 0.0380  0.0547  0.0224  382 HOH   A O   
7085 O O   A HOH   D .   ? 0.2284 0.3858 0.3815 0.0465  0.0008  0.0876  383 HOH   A O   
7086 O O   . HOH   D .   ? 0.3824 0.4859 0.3236 -0.0135 0.0888  0.2022  384 HOH   A O   
7087 O O   . HOH   D .   ? 0.2003 0.2153 0.3009 -0.0193 -0.0202 0.0913  385 HOH   A O   
7088 O O   B HOH   D .   ? 0.1407 0.1084 0.1813 -0.0179 -0.0180 0.0272  386 HOH   A O   
7089 O O   . HOH   D .   ? 0.4196 0.4535 0.3092 -0.1182 -0.0048 0.1384  387 HOH   A O   
7090 O O   . HOH   D .   ? 0.3133 0.2147 0.2656 -0.0398 -0.1026 0.0280  388 HOH   A O   
7091 O O   . HOH   D .   ? 0.7713 0.6207 0.6746 -0.1172 -0.1323 0.1556  389 HOH   A O   
7092 O O   . HOH   D .   ? 0.3174 0.4784 0.4165 -0.0809 0.0627  -0.0608 390 HOH   A O   
7093 O O   . HOH   D .   ? 0.2460 0.1869 0.1919 -0.0429 0.0372  0.0302  391 HOH   A O   
7094 O O   B HOH   D .   ? 0.3036 0.2259 0.3281 -0.1086 0.0663  -0.0144 392 HOH   A O   
7095 O O   . HOH   D .   ? 0.2960 0.3152 0.3952 -0.1000 0.1292  0.0038  393 HOH   A O   
7096 O O   A HOH   D .   ? 0.1311 0.0791 0.1173 -0.0072 0.0181  0.0287  394 HOH   A O   
7097 O O   . HOH   D .   ? 0.2090 0.1710 0.3515 0.0060  -0.0284 0.0012  395 HOH   A O   
7098 O O   . HOH   D .   ? 0.2732 0.2198 0.2470 -0.0480 0.0631  -0.0012 396 HOH   A O   
7099 O O   A HOH   D .   ? 0.1996 0.1962 0.3287 0.0271  -0.0364 0.0829  397 HOH   A O   
7100 O O   A HOH   D .   ? 0.1727 0.1851 0.2542 0.0037  0.0829  0.0952  398 HOH   A O   
7101 O O   . HOH   D .   ? 0.6293 0.8161 0.4110 -0.1323 -0.0746 -0.0964 399 HOH   A O   
7102 O O   . HOH   D .   ? 0.4676 0.7522 0.6769 0.1143  0.0560  -0.0951 400 HOH   A O   
7103 O O   B HOH   D .   ? 0.1758 0.2218 0.2415 -0.0176 -0.0155 0.0218  401 HOH   A O   
7104 O O   . HOH   D .   ? 0.7446 0.7958 0.7426 0.1343  0.0423  0.0675  402 HOH   A O   
7105 O O   . HOH   D .   ? 0.2345 0.1999 0.2450 -0.0442 0.0145  0.0530  403 HOH   A O   
7106 O O   . HOH   D .   ? 0.3037 0.2616 0.4109 -0.0126 -0.0382 -0.0341 404 HOH   A O   
7107 O O   . HOH   D .   ? 0.2290 0.3599 0.8617 -0.0428 0.0226  -0.0184 405 HOH   A O   
7108 O O   A HOH   D .   ? 0.3944 0.3080 0.2623 -0.0861 0.0448  0.0914  406 HOH   A O   
7109 O O   . HOH   D .   ? 0.1760 0.1917 0.3966 0.0357  0.1041  0.1065  407 HOH   A O   
7110 O O   . HOH   D .   ? 0.3087 0.2434 0.3403 -0.0059 -0.0277 0.1088  408 HOH   A O   
7111 O O   . HOH   D .   ? 0.2295 0.4188 0.3366 -0.0395 0.0880  -0.0979 409 HOH   A O   
7112 O O   . HOH   D .   ? 0.2221 0.1621 0.1886 -0.0109 0.0121  0.0166  410 HOH   A O   
7113 O O   . HOH   D .   ? 0.1895 0.2661 0.3253 -0.0533 -0.0117 0.0223  411 HOH   A O   
7114 O O   . HOH   D .   ? 0.4065 0.5675 0.4413 -0.0283 -0.0732 -0.1164 412 HOH   A O   
7115 O O   . HOH   D .   ? 0.1318 0.1339 0.1979 -0.0001 -0.0250 0.0101  413 HOH   A O   
7116 O O   . HOH   D .   ? 0.3086 0.5901 0.4001 -0.0189 0.0049  0.1452  414 HOH   A O   
7117 O O   A HOH   D .   ? 0.4456 0.4874 0.4022 -0.0947 -0.0136 0.0606  415 HOH   A O   
7118 O O   . HOH   D .   ? 0.2781 0.2048 0.2622 -0.0170 0.0151  0.0390  416 HOH   A O   
7119 O O   . HOH   D .   ? 0.5881 0.7159 0.7727 -0.0486 -0.0355 -0.0144 417 HOH   A O   
7120 O O   . HOH   D .   ? 0.5316 0.5261 0.2749 0.0081  -0.0027 -0.0586 418 HOH   A O   
7121 O O   . HOH   D .   ? 0.6928 0.7107 0.5037 0.0296  0.1207  0.2183  419 HOH   A O   
7122 O O   . HOH   D .   ? 0.4572 0.3114 0.2779 -0.0287 0.0653  0.0523  420 HOH   A O   
7123 O O   . HOH   D .   ? 0.6384 0.8294 0.4902 0.0711  0.3152  -0.0775 421 HOH   A O   
7124 O O   . HOH   D .   ? 0.2105 0.2549 0.2896 -0.0098 -0.0621 0.0601  422 HOH   A O   
7125 O O   . HOH   D .   ? 0.3877 0.1242 0.2151 -0.0050 -0.0916 0.0227  423 HOH   A O   
7126 O O   . HOH   D .   ? 0.4119 0.2425 0.5301 -0.0862 -0.2356 0.1221  424 HOH   A O   
7127 O O   . HOH   D .   ? 0.4537 0.2826 0.4994 0.0109  -0.1788 -0.0483 425 HOH   A O   
7128 O O   . HOH   D .   ? 0.4597 0.5896 0.5837 0.1308  -0.0321 0.1086  426 HOH   A O   
7129 O O   . HOH   D .   ? 0.3907 0.4937 0.6982 0.1245  0.1909  -0.1281 427 HOH   A O   
7130 O O   . HOH   D .   ? 0.4203 0.6857 0.3301 -0.0975 -0.0169 0.1256  428 HOH   A O   
7131 O O   A HOH   D .   ? 0.3458 0.2937 0.2825 0.0189  0.0687  0.0236  429 HOH   A O   
7132 O O   . HOH   D .   ? 0.1837 0.2597 0.4945 -0.0059 -0.0100 0.0526  430 HOH   A O   
7133 O O   . HOH   D .   ? 1.2326 1.1203 0.9748 -0.0834 -0.0947 0.0330  431 HOH   A O   
7134 O O   . HOH   D .   ? 0.2909 0.5870 0.1720 -0.0139 0.0516  0.0438  432 HOH   A O   
7135 O O   . HOH   D .   ? 0.2000 0.1838 0.2693 0.0210  -0.0552 0.0283  433 HOH   A O   
7136 O O   . HOH   D .   ? 0.1582 0.1585 0.3628 0.0036  0.0089  0.0207  434 HOH   A O   
7137 O O   . HOH   D .   ? 0.2654 0.4183 0.2708 0.1895  0.0102  0.0264  435 HOH   A O   
7138 O O   A HOH   D .   ? 0.1372 0.1710 0.1454 0.0064  0.0404  0.0154  436 HOH   A O   
7139 O O   . HOH   D .   ? 0.8203 0.8117 0.7393 0.3469  0.2333  0.1144  437 HOH   A O   
7140 O O   . HOH   D .   ? 0.7342 0.7420 0.6548 -0.1141 0.0549  0.2712  438 HOH   A O   
7141 O O   B HOH   D .   ? 0.2065 0.2032 0.4599 -0.0231 -0.0108 0.0526  439 HOH   A O   
7142 O O   . HOH   D .   ? 0.7675 0.9510 0.7224 0.2623  -0.1031 0.2634  440 HOH   A O   
7143 O O   A HOH   D .   ? 0.1549 0.2189 0.3262 0.0438  -0.0496 -0.0497 441 HOH   A O   
7144 O O   . HOH   D .   ? 0.1967 0.2159 0.4778 -0.0345 -0.1102 0.0734  442 HOH   A O   
7145 O O   B HOH   D .   ? 0.3847 0.2406 0.4631 0.1307  -0.0047 0.0772  443 HOH   A O   
7146 O O   . HOH   D .   ? 0.3136 0.3969 0.5965 0.0320  0.0686  -0.0727 444 HOH   A O   
7147 O O   . HOH   D .   ? 0.2398 0.1653 0.2973 0.0108  -0.0009 0.0049  445 HOH   A O   
7148 O O   . HOH   D .   ? 0.6833 0.3585 0.4515 0.1413  -0.1014 0.0833  446 HOH   A O   
7149 O O   . HOH   D .   ? 0.7689 0.6802 0.7390 0.0942  0.0381  -0.0207 447 HOH   A O   
7150 O O   . HOH   D .   ? 0.3994 0.2594 0.1964 -0.0879 0.0432  0.0447  448 HOH   A O   
7151 O O   . HOH   D .   ? 0.7058 0.7158 0.7449 0.0152  -0.1069 0.2608  449 HOH   A O   
7152 O O   . HOH   D .   ? 0.4799 0.3986 0.2732 0.2563  -0.0717 -0.0515 450 HOH   A O   
7153 O O   . HOH   D .   ? 0.2133 0.2686 0.2496 0.0020  -0.0111 -0.0443 451 HOH   A O   
7154 O O   A HOH   D .   ? 0.5513 0.3763 0.3328 -0.1145 -0.0975 -0.0702 452 HOH   A O   
7155 O O   A HOH   D .   ? 0.5731 0.4686 0.4585 0.0835  0.0534  0.0704  453 HOH   A O   
7156 O O   . HOH   D .   ? 0.2946 0.4845 0.6634 0.0451  0.0144  -0.1721 454 HOH   A O   
7157 O O   B HOH   D .   ? 0.1333 0.1590 0.3333 -0.0325 0.0298  -0.0108 455 HOH   A O   
7158 O O   . HOH   D .   ? 0.2263 0.2218 0.2654 0.0153  0.0206  0.0485  456 HOH   A O   
7159 O O   B HOH   D .   ? 0.6780 0.1972 0.3767 0.0483  -0.0585 -0.0156 457 HOH   A O   
7160 O O   . HOH   D .   ? 0.3438 0.4328 0.4752 0.1220  0.1396  0.1380  458 HOH   A O   
7161 O O   . HOH   D .   ? 0.7867 0.6741 0.7611 -0.1340 0.1593  -0.1322 459 HOH   A O   
7162 O O   . HOH   D .   ? 0.3153 0.3079 0.4706 -0.0446 0.0106  -0.1141 460 HOH   A O   
7163 O O   . HOH   D .   ? 0.3928 0.3978 0.3981 0.1727  -0.0888 0.0008  461 HOH   A O   
7164 O O   . HOH   D .   ? 0.4682 0.3067 0.3791 0.0394  0.0797  0.0156  462 HOH   A O   
7165 O O   . HOH   D .   ? 0.8190 0.7884 0.4859 -0.0774 -0.1257 -0.0151 463 HOH   A O   
7166 O O   . HOH   D .   ? 0.5014 0.6286 0.4220 -0.0781 -0.0161 0.1191  464 HOH   A O   
7167 O O   . HOH   D .   ? 0.3168 0.4814 0.4929 0.0435  -0.1579 0.1010  465 HOH   A O   
7168 O O   . HOH   D .   ? 0.3607 0.5816 0.4495 -0.1793 0.0577  -0.0814 466 HOH   A O   
7169 O O   B HOH   D .   ? 0.1551 0.1511 0.3294 -0.0192 -0.0303 0.0189  467 HOH   A O   
7170 O O   . HOH   D .   ? 0.2432 0.4249 0.4665 0.0210  0.0151  -0.1767 468 HOH   A O   
7171 O O   . HOH   D .   ? 0.4963 0.4574 0.3728 -0.1568 0.0569  0.0020  469 HOH   A O   
7172 O O   . HOH   D .   ? 0.7367 0.6793 0.5786 0.2365  0.2463  0.2127  470 HOH   A O   
7173 O O   . HOH   D .   ? 0.4647 0.5558 0.3952 0.0668  -0.1055 -0.0977 471 HOH   A O   
7174 O O   . HOH   D .   ? 0.4033 0.6479 0.5308 -0.0626 -0.1493 0.2872  472 HOH   A O   
7175 O O   . HOH   D .   ? 0.5627 0.3512 0.6805 0.1147  0.1290  0.2339  473 HOH   A O   
7176 O O   . HOH   D .   ? 0.2792 0.1721 0.2767 0.0348  -0.1051 -0.0466 474 HOH   A O   
7177 O O   . HOH   D .   ? 0.3120 0.2608 0.3550 -0.1070 0.0350  -0.0013 475 HOH   A O   
7178 O O   . HOH   D .   ? 0.6929 0.7085 0.5975 0.2573  -0.0794 -0.0645 476 HOH   A O   
7179 O O   . HOH   D .   ? 0.3332 0.3579 0.3329 0.0478  0.0834  0.0517  477 HOH   A O   
7180 O O   . HOH   D .   ? 0.5819 0.4471 0.5016 -0.0421 0.1273  -0.0114 478 HOH   A O   
7181 O O   A HOH   D .   ? 0.2892 0.2478 0.4390 -0.0097 -0.0967 -0.0280 479 HOH   A O   
7182 O O   . HOH   D .   ? 0.5560 0.5553 0.3491 -0.0427 -0.0682 0.0918  480 HOH   A O   
7183 O O   . HOH   D .   ? 0.4447 0.4367 0.5502 -0.2100 -0.0550 -0.0112 481 HOH   A O   
7184 O O   . HOH   D .   ? 0.3164 0.3406 0.2673 0.1042  -0.0084 0.0217  482 HOH   A O   
7185 O O   . HOH   D .   ? 0.7257 0.4062 0.5075 -0.0226 0.0378  0.0432  483 HOH   A O   
7186 O O   . HOH   D .   ? 0.5733 0.7565 0.4467 -0.1553 -0.1318 -0.0643 484 HOH   A O   
7187 O O   . HOH   D .   ? 0.7292 0.6795 0.6841 -0.1318 0.0236  -0.1169 485 HOH   A O   
7188 O O   . HOH   D .   ? 0.5304 0.4070 0.4812 0.0130  -0.0561 -0.1119 486 HOH   A O   
7189 O O   . HOH   D .   ? 0.7891 0.3890 0.3588 -0.0303 -0.1100 0.0049  487 HOH   A O   
7190 O O   . HOH   D .   ? 0.5856 0.5736 0.6856 -0.1365 0.0668  -0.0648 488 HOH   A O   
7191 O O   . HOH   D .   ? 0.6352 0.3117 0.3700 -0.0998 -0.0904 0.0399  489 HOH   A O   
7192 O O   . HOH   D .   ? 0.3843 0.4522 0.4912 0.0298  0.2165  0.1265  490 HOH   A O   
7193 O O   . HOH   D .   ? 0.3225 0.5173 0.3917 0.0127  -0.0680 -0.0439 491 HOH   A O   
7194 O O   . HOH   D .   ? 0.5129 0.5196 0.4277 0.0077  0.0010  -0.0634 492 HOH   A O   
7195 O O   . HOH   D .   ? 0.6502 0.7374 0.7996 -0.0018 0.1702  -0.1354 493 HOH   A O   
7196 O O   . HOH   D .   ? 0.8368 0.7524 0.5996 -0.1189 0.2494  0.1266  494 HOH   A O   
7197 O O   . HOH   D .   ? 0.2707 0.2181 0.7468 0.0067  -0.1471 -0.0032 495 HOH   A O   
7198 O O   . HOH   D .   ? 0.2637 0.5355 0.4206 0.1155  0.0979  0.2719  496 HOH   A O   
7199 O O   . HOH   D .   ? 0.4241 0.3057 0.2411 -0.0594 0.1000  -0.0363 497 HOH   A O   
7200 O O   . HOH   D .   ? 0.5724 0.4472 0.4688 -0.0569 0.1034  0.1730  498 HOH   A O   
7201 O O   . HOH   D .   ? 0.5300 0.6654 0.5802 0.0727  -0.1016 0.0110  499 HOH   A O   
7202 O O   . HOH   D .   ? 0.5701 0.7638 0.5271 0.1773  -0.1423 0.0367  500 HOH   A O   
7203 O O   . HOH   D .   ? 0.4533 0.3240 0.4251 -0.0158 0.2208  0.0451  501 HOH   A O   
7204 O O   . HOH   D .   ? 0.6599 0.2701 0.5014 -0.0244 0.1441  0.0757  502 HOH   A O   
7205 O O   . HOH   D .   ? 0.3009 0.2903 0.5664 0.0085  0.0641  -0.0534 503 HOH   A O   
7206 O O   . HOH   D .   ? 0.6087 0.5921 0.4528 -0.0031 -0.1204 -0.0567 504 HOH   A O   
7207 O O   . HOH   D .   ? 0.2947 0.1951 0.6404 -0.0098 0.0846  0.0404  505 HOH   A O   
7208 O O   . HOH   D .   ? 0.4943 0.9923 0.6022 -0.1273 -0.0482 0.1144  506 HOH   A O   
7209 O O   B HOH   D .   ? 0.2437 0.2565 0.1793 0.0064  0.0316  0.0008  507 HOH   A O   
7210 O O   . HOH   D .   ? 0.4609 0.2383 0.4586 -0.1297 0.0272  0.0113  508 HOH   A O   
7211 O O   B HOH   D .   ? 0.5065 0.2574 0.2680 -0.1337 0.0293  -0.0174 509 HOH   A O   
7212 O O   B HOH   D .   ? 0.2788 0.3385 0.2814 -0.0474 0.0190  0.0729  510 HOH   A O   
7213 O O   . HOH   D .   ? 0.2363 0.3170 0.3134 0.0366  -0.0409 0.0567  511 HOH   A O   
7214 O O   . HOH   D .   ? 0.2500 0.4791 0.5727 -0.0106 -0.0817 0.0875  512 HOH   A O   
7215 O O   . HOH   D .   ? 0.5891 0.8419 0.6356 0.1631  -0.0022 0.1971  513 HOH   A O   
7216 O O   . HOH   D .   ? 0.3220 0.3780 0.4899 -0.0280 -0.1264 0.1805  514 HOH   A O   
7217 O O   B HOH   D .   ? 0.3691 0.2069 0.4166 -0.0446 0.1516  0.0031  515 HOH   A O   
7218 O O   B HOH   D .   ? 0.4417 0.2009 0.5544 -0.0350 -0.0949 0.1249  516 HOH   A O   
7219 O O   . HOH   D .   ? 0.3083 0.2124 0.4567 0.0005  0.0344  0.0374  517 HOH   A O   
7220 O O   . HOH   D .   ? 0.5417 0.7341 0.5531 0.3392  -0.0765 0.0765  518 HOH   A O   
7221 O O   . HOH   D .   ? 0.6101 0.8103 0.5859 -0.1175 -0.1362 -0.1278 519 HOH   A O   
7222 O O   A HOH   D .   ? 0.2185 0.3468 0.1694 0.0931  -0.0054 0.0744  520 HOH   A O   
7223 O O   . HOH   D .   ? 0.4023 0.7242 0.4806 0.1517  0.0199  -0.0687 521 HOH   A O   
7224 O O   . HOH   D .   ? 0.5552 0.7318 0.5574 -0.0321 0.0201  0.1822  522 HOH   A O   
7225 O O   . HOH   D .   ? 0.6794 0.5879 0.5592 0.0819  0.1519  0.0843  523 HOH   A O   
7226 O O   B HOH   D .   ? 0.3069 0.3381 0.4587 0.0317  -0.0501 0.1274  524 HOH   A O   
7227 O O   . HOH   D .   ? 0.4156 0.4808 0.6078 -0.1083 -0.0641 0.2833  525 HOH   A O   
7228 O O   . HOH   E .   ? 0.2283 0.2234 0.3086 0.0273  0.0820  0.0228  201 HOH   B O   
7229 O O   . HOH   E .   ? 0.3142 0.3885 0.7035 -0.0501 0.0305  0.0150  202 HOH   B O   
7230 O O   . HOH   E .   ? 0.4403 0.4045 0.4364 -0.0217 -0.0138 -0.1824 203 HOH   B O   
7231 O O   . HOH   E .   ? 0.6150 0.5531 0.4863 0.1482  0.0792  0.0874  204 HOH   B O   
7232 O O   . HOH   E .   ? 0.7039 0.3279 0.3904 0.0135  0.0331  0.0081  205 HOH   B O   
7233 O O   . HOH   E .   ? 0.2885 0.6739 0.3960 0.0323  -0.0355 0.2603  206 HOH   B O   
7234 O O   . HOH   E .   ? 0.2817 0.6663 0.4636 -0.0410 0.1339  -0.1967 207 HOH   B O   
7235 O O   . HOH   E .   ? 0.3132 0.2033 0.5620 0.0147  0.1969  0.0810  208 HOH   B O   
7236 O O   . HOH   E .   ? 0.3436 0.2127 0.5734 -0.0077 0.2242  0.0229  209 HOH   B O   
7237 O O   . HOH   E .   ? 0.2036 0.2179 0.2818 -0.0006 0.0312  -0.0224 210 HOH   B O   
7238 O O   . HOH   E .   ? 0.5801 0.3786 0.6338 0.0429  -0.0864 0.2570  211 HOH   B O   
7239 O O   . HOH   E .   ? 0.5738 0.4057 0.3978 0.0788  0.1008  -0.1525 212 HOH   B O   
7240 O O   . HOH   E .   ? 0.3515 0.4101 0.3095 0.0435  -0.1043 0.0505  213 HOH   B O   
7241 O O   . HOH   E .   ? 0.1599 0.2086 0.2893 -0.0333 -0.0080 0.0093  214 HOH   B O   
7242 O O   . HOH   E .   ? 0.3866 0.4721 0.3623 0.1507  -0.0288 -0.0346 215 HOH   B O   
7243 O O   . HOH   E .   ? 0.5110 0.5789 0.3282 0.3133  -0.1054 -0.0821 216 HOH   B O   
7244 O O   . HOH   E .   ? 0.1765 0.2203 0.3118 -0.0289 0.0146  -0.0371 217 HOH   B O   
7245 O O   . HOH   E .   ? 0.4429 0.6512 0.2110 0.0732  -0.0163 -0.1045 218 HOH   B O   
7246 O O   . HOH   E .   ? 0.2983 0.2820 0.4579 0.0264  -0.0806 -0.0225 219 HOH   B O   
7247 O O   . HOH   E .   ? 0.5451 0.4754 0.2727 -0.0982 0.0076  0.0417  220 HOH   B O   
7248 O O   . HOH   E .   ? 0.1517 0.1492 0.2295 -0.0263 0.0054  0.0021  221 HOH   B O   
7249 O O   . HOH   E .   ? 0.3715 0.5506 0.5606 0.2483  0.0374  -0.0715 222 HOH   B O   
7250 O O   . HOH   E .   ? 0.3366 0.3917 0.5683 -0.1240 -0.0034 -0.1236 223 HOH   B O   
7251 O O   . HOH   E .   ? 0.2336 0.1637 0.2848 -0.0189 0.0978  -0.0084 224 HOH   B O   
7252 O O   . HOH   E .   ? 0.3327 0.2592 0.4457 0.0568  -0.0144 -0.0425 225 HOH   B O   
7253 O O   . HOH   E .   ? 0.2232 0.2235 0.4208 -0.0356 0.0209  -0.0600 226 HOH   B O   
7254 O O   . HOH   E .   ? 0.3144 0.2716 0.5617 0.0898  -0.0764 0.0586  227 HOH   B O   
7255 O O   . HOH   E .   ? 0.4950 0.2011 0.2796 -0.0031 -0.0814 0.0151  228 HOH   B O   
7256 O O   . HOH   E .   ? 0.3769 0.1700 0.1929 0.0289  -0.0964 -0.0156 229 HOH   B O   
7257 O O   . HOH   E .   ? 0.5100 0.6798 0.3949 0.2828  0.0724  0.1054  230 HOH   B O   
7258 O O   . HOH   E .   ? 0.2495 0.2660 0.2949 0.0129  0.0496  -0.0818 231 HOH   B O   
7259 O O   . HOH   E .   ? 0.3633 0.3324 0.2074 0.0321  0.0681  0.0348  232 HOH   B O   
7260 O O   . HOH   E .   ? 0.4666 0.2019 0.2253 0.1357  0.0454  0.0285  233 HOH   B O   
7261 O O   . HOH   E .   ? 0.2098 0.1877 0.4853 0.0146  -0.0684 -0.0844 234 HOH   B O   
7262 O O   . HOH   E .   ? 0.2368 0.1287 0.3302 0.0101  -0.0827 -0.0133 235 HOH   B O   
7263 O O   . HOH   E .   ? 0.3958 0.4088 0.4701 -0.1459 -0.0045 0.0890  236 HOH   B O   
7264 O O   . HOH   E .   ? 0.5778 0.2741 0.4078 -0.1794 0.0022  0.0223  237 HOH   B O   
7265 O O   . HOH   E .   ? 0.2449 0.2375 0.2359 0.0846  -0.0848 -0.0644 238 HOH   B O   
7266 O O   . HOH   E .   ? 0.6803 0.5814 0.5317 0.0936  0.0461  -0.0586 239 HOH   B O   
7267 O O   . HOH   E .   ? 0.2179 0.4424 0.3483 -0.0571 -0.0589 -0.1026 240 HOH   B O   
7268 O O   . HOH   E .   ? 0.2635 0.5986 0.6077 0.1690  -0.0346 -0.1238 241 HOH   B O   
7269 O O   . HOH   E .   ? 0.3504 0.2512 0.4272 0.0450  -0.0656 -0.1374 242 HOH   B O   
7270 O O   . HOH   E .   ? 0.2068 0.3511 0.2422 -0.0163 -0.0230 0.0516  243 HOH   B O   
7271 O O   . HOH   E .   ? 0.3254 0.5386 0.6888 0.0699  0.1414  0.0649  244 HOH   B O   
7272 O O   . HOH   E .   ? 0.2156 0.1841 0.1988 -0.0246 -0.0317 0.0139  245 HOH   B O   
7273 O O   . HOH   E .   ? 0.2904 0.3549 0.2309 -0.0828 0.0433  -0.0655 246 HOH   B O   
7274 O O   . HOH   E .   ? 0.2578 0.2906 0.2959 -0.0919 0.0182  -0.0169 247 HOH   B O   
7275 O O   . HOH   E .   ? 0.6040 0.3109 0.3577 -0.2298 0.0324  0.0030  248 HOH   B O   
7276 O O   . HOH   E .   ? 0.1451 0.1407 0.1411 -0.0085 -0.0075 -0.0018 249 HOH   B O   
7277 O O   . HOH   E .   ? 0.1530 0.1480 0.2638 -0.0038 0.0094  -0.0077 250 HOH   B O   
7278 O O   . HOH   E .   ? 0.2983 0.1746 0.6378 -0.0104 -0.1311 -0.0207 251 HOH   B O   
7279 O O   . HOH   E .   ? 0.2806 0.2248 0.1912 0.0197  -0.0124 0.0014  252 HOH   B O   
7280 O O   . HOH   E .   ? 0.1762 0.2686 0.2933 0.0409  0.0533  0.0965  253 HOH   B O   
7281 O O   . HOH   E .   ? 0.2919 0.2445 0.2966 0.0990  0.0814  0.0058  254 HOH   B O   
7282 O O   . HOH   E .   ? 0.5748 0.5305 0.3479 0.0717  0.1218  -0.0093 255 HOH   B O   
7283 O O   . HOH   E .   ? 0.2330 0.3252 0.2010 -0.0620 0.0241  0.0464  256 HOH   B O   
7284 O O   . HOH   E .   ? 0.1677 0.1409 0.4489 -0.0067 -0.0164 -0.0161 257 HOH   B O   
7285 O O   . HOH   E .   ? 0.2172 0.1587 0.1914 -0.0345 -0.0446 0.0294  258 HOH   B O   
7286 O O   . HOH   E .   ? 0.1609 0.1754 0.3007 -0.0276 -0.0122 0.0098  259 HOH   B O   
7287 O O   . HOH   E .   ? 0.2740 0.3969 0.2838 -0.0831 -0.0504 -0.0300 260 HOH   B O   
7288 O O   . HOH   E .   ? 0.1546 0.1275 0.1548 0.0027  -0.0048 0.0020  261 HOH   B O   
7289 O O   . HOH   E .   ? 0.4297 0.3651 0.2194 -0.0040 0.1121  -0.0017 262 HOH   B O   
7290 O O   . HOH   E .   ? 0.3032 0.5156 0.2900 -0.0384 -0.0840 0.0699  263 HOH   B O   
7291 O O   . HOH   E .   ? 0.4410 0.5790 0.3958 0.0348  -0.1590 0.0527  264 HOH   B O   
7292 O O   . HOH   E .   ? 0.1371 0.1549 0.2106 -0.0057 0.0077  0.0122  265 HOH   B O   
7293 O O   . HOH   E .   ? 0.2256 0.5055 0.4181 -0.0713 0.0045  -0.1254 266 HOH   B O   
7294 O O   . HOH   E .   ? 0.2542 0.1944 0.2586 -0.0443 0.0114  -0.0072 267 HOH   B O   
7295 O O   . HOH   E .   ? 0.5919 0.6504 0.4594 0.2989  -0.0128 0.0629  268 HOH   B O   
7296 O O   . HOH   E .   ? 0.4842 0.5032 0.6723 0.1807  -0.1459 -0.1373 269 HOH   B O   
7297 O O   . HOH   E .   ? 0.2452 0.2119 0.1742 0.0261  0.0031  0.0006  270 HOH   B O   
7298 O O   . HOH   E .   ? 0.2806 0.4312 0.3775 -0.0053 0.1391  0.0051  271 HOH   B O   
7299 O O   . HOH   E .   ? 0.2080 0.1489 0.2222 -0.0294 -0.0129 0.0169  272 HOH   B O   
7300 O O   . HOH   E .   ? 0.2218 0.3113 0.2407 0.0812  -0.0461 -0.0393 273 HOH   B O   
7301 O O   . HOH   E .   ? 0.2251 0.2604 0.2158 -0.0421 -0.0596 -0.0421 274 HOH   B O   
7302 O O   . HOH   E .   ? 0.5034 0.3749 0.2961 0.0273  0.0047  -0.0765 275 HOH   B O   
7303 O O   . HOH   E .   ? 0.3464 0.2656 0.2985 -0.0607 0.0355  -0.0479 276 HOH   B O   
7304 O O   . HOH   E .   ? 0.1944 0.1772 0.1642 -0.0496 -0.0412 0.0143  277 HOH   B O   
7305 O O   . HOH   E .   ? 0.2327 0.2716 0.2221 -0.0146 -0.0745 0.0072  278 HOH   B O   
7306 O O   . HOH   E .   ? 0.3951 0.2717 0.3735 -0.0436 -0.0858 -0.0371 279 HOH   B O   
7307 O O   . HOH   E .   ? 0.3079 0.7162 0.7478 0.0812  -0.0701 -0.1239 280 HOH   B O   
7308 O O   . HOH   E .   ? 0.4252 0.3876 0.4386 0.1579  -0.0382 -0.0950 281 HOH   B O   
7309 O O   . HOH   E .   ? 0.3345 0.3609 0.5520 0.0139  -0.0078 -0.1202 282 HOH   B O   
7310 O O   . HOH   E .   ? 0.3900 0.2526 0.2053 0.0478  -0.0982 -0.0042 283 HOH   B O   
7311 O O   . HOH   E .   ? 0.4661 0.2794 0.3273 0.0483  -0.0318 -0.0774 284 HOH   B O   
7312 O O   . HOH   E .   ? 0.2112 0.2680 0.2973 -0.0216 0.0361  -0.0727 285 HOH   B O   
7313 O O   . HOH   E .   ? 0.1718 0.1487 0.1777 0.0031  0.0076  -0.0010 286 HOH   B O   
7314 O O   . HOH   E .   ? 0.1691 0.1568 0.3358 -0.0215 0.0126  -0.0106 287 HOH   B O   
7315 O O   . HOH   E .   ? 0.3565 0.2045 0.3638 -0.0694 -0.1899 0.0764  288 HOH   B O   
7316 O O   . HOH   E .   ? 0.5228 0.3456 0.3375 -0.1232 0.0569  -0.0700 289 HOH   B O   
7317 O O   . HOH   E .   ? 0.5945 0.3877 0.3137 0.2676  0.1094  0.0819  290 HOH   B O   
7318 O O   . HOH   E .   ? 0.2489 0.2604 0.2855 0.0097  -0.0757 0.0313  291 HOH   B O   
7319 O O   . HOH   E .   ? 0.1739 0.1988 0.2957 0.0183  0.0000  0.0049  292 HOH   B O   
7320 O O   . HOH   E .   ? 0.2640 0.4606 0.5626 -0.1006 -0.1642 0.0944  293 HOH   B O   
7321 O O   . HOH   E .   ? 0.1664 0.1969 0.1467 -0.0120 -0.0135 0.0037  294 HOH   B O   
7322 O O   . HOH   E .   ? 0.3336 0.2170 0.4752 0.0433  0.1170  0.0504  295 HOH   B O   
7323 O O   . HOH   E .   ? 0.2232 0.3337 0.5688 0.0872  -0.0721 -0.1598 296 HOH   B O   
7324 O O   . HOH   E .   ? 0.5306 0.7405 0.2986 -0.0347 -0.1526 -0.0260 297 HOH   B O   
7325 O O   . HOH   E .   ? 0.2269 0.2467 0.5658 -0.0561 -0.0192 0.1493  298 HOH   B O   
7326 O O   . HOH   E .   ? 0.1726 0.3337 0.5510 0.0275  -0.0160 -0.1751 299 HOH   B O   
7327 O O   . HOH   E .   ? 0.2729 0.7397 0.2301 0.1333  -0.0481 -0.0951 300 HOH   B O   
7328 O O   . HOH   E .   ? 0.3145 0.2924 0.2951 -0.0423 0.0509  -0.1273 301 HOH   B O   
7329 O O   . HOH   E .   ? 0.4435 0.5163 0.2383 0.0392  0.0947  0.1083  302 HOH   B O   
7330 O O   . HOH   E .   ? 0.1752 0.1596 0.2389 0.0149  0.0060  0.0242  303 HOH   B O   
7331 O O   . HOH   E .   ? 0.5594 0.3671 0.4878 -0.0215 0.1711  -0.1732 304 HOH   B O   
7332 O O   . HOH   E .   ? 0.3852 0.5954 0.3552 0.2032  -0.0327 0.0474  305 HOH   B O   
7333 O O   . HOH   E .   ? 0.3212 0.2852 0.5796 -0.0203 -0.0933 0.1466  306 HOH   B O   
7334 O O   . HOH   E .   ? 0.4223 0.3948 0.2338 0.1248  -0.0700 0.0617  307 HOH   B O   
7335 O O   . HOH   E .   ? 0.3947 0.3437 0.4506 -0.1400 0.1832  -0.0766 308 HOH   B O   
7336 O O   . HOH   E .   ? 0.1686 0.1413 0.3418 0.0032  0.0092  0.0055  309 HOH   B O   
7337 O O   . HOH   E .   ? 0.2506 0.1551 0.2641 -0.0313 -0.0163 0.0350  310 HOH   B O   
7338 O O   . HOH   E .   ? 0.2190 0.1667 0.2521 -0.0332 -0.0227 -0.0084 311 HOH   B O   
7339 O O   . HOH   E .   ? 0.3210 0.1753 0.3365 0.0547  0.1034  0.0408  312 HOH   B O   
7340 O O   . HOH   E .   ? 0.4479 0.4174 0.4059 -0.0872 0.0368  0.1502  313 HOH   B O   
7341 O O   . HOH   E .   ? 0.2046 0.3161 0.4508 -0.0178 -0.0691 -0.0197 314 HOH   B O   
7342 O O   . HOH   E .   ? 0.2050 0.1507 0.3264 0.0335  -0.0904 -0.0035 315 HOH   B O   
7343 O O   . HOH   E .   ? 0.4510 0.2734 0.2361 -0.1719 0.0586  -0.0238 316 HOH   B O   
7344 O O   . HOH   E .   ? 0.2258 0.1977 0.1869 -0.0037 0.0233  0.0212  317 HOH   B O   
7345 O O   . HOH   E .   ? 0.4240 0.2220 0.2644 0.1530  0.0940  0.0384  318 HOH   B O   
7346 O O   . HOH   E .   ? 0.2953 0.3061 0.6049 -0.0725 -0.1979 0.1777  319 HOH   B O   
7347 O O   . HOH   E .   ? 0.5061 0.6250 0.6064 0.1762  -0.0619 0.2600  320 HOH   B O   
7348 O O   . HOH   E .   ? 0.2316 0.6913 0.4754 -0.1408 -0.0014 -0.0014 321 HOH   B O   
7349 O O   . HOH   E .   ? 0.1638 0.1788 0.3157 -0.0263 -0.0078 0.0142  322 HOH   B O   
7350 O O   . HOH   E .   ? 0.2904 0.3019 0.3516 -0.0465 0.1221  -0.1139 323 HOH   B O   
7351 O O   . HOH   E .   ? 0.6267 0.4809 0.5622 0.1541  0.2054  0.1104  324 HOH   B O   
7352 O O   . HOH   E .   ? 0.1726 0.2840 0.2182 -0.0177 -0.0234 0.0654  325 HOH   B O   
7353 O O   . HOH   E .   ? 0.7083 0.1989 0.3834 0.0050  -0.0855 0.0007  326 HOH   B O   
7354 O O   . HOH   E .   ? 0.4655 0.3881 0.6217 0.0798  0.0002  0.0047  327 HOH   B O   
7355 O O   . HOH   E .   ? 0.5906 0.3973 0.2820 -0.0048 -0.0468 -0.0700 328 HOH   B O   
7356 O O   . HOH   E .   ? 0.6367 0.3895 0.4242 0.0578  0.1888  0.1855  329 HOH   B O   
7357 O O   . HOH   E .   ? 0.3510 0.2368 0.2297 0.0510  -0.0228 0.0420  330 HOH   B O   
7358 O O   . HOH   E .   ? 0.1579 0.1655 0.2931 -0.0161 -0.0029 -0.0138 331 HOH   B O   
7359 O O   . HOH   E .   ? 0.4044 0.3779 0.8236 -0.0354 -0.1229 0.1964  332 HOH   B O   
7360 O O   . HOH   E .   ? 0.1893 0.1862 0.2762 0.0300  0.0455  0.0195  333 HOH   B O   
7361 O O   . HOH   E .   ? 0.2014 0.3279 0.3336 0.0508  -0.0180 -0.1126 334 HOH   B O   
7362 O O   . HOH   E .   ? 0.2685 0.1918 0.5688 0.0128  -0.0111 0.0407  335 HOH   B O   
7363 O O   . HOH   E .   ? 0.4748 0.2654 0.3481 0.0534  0.1135  0.1106  336 HOH   B O   
7364 O O   . HOH   E .   ? 0.5052 0.5546 0.3334 0.0250  -0.1072 0.0479  337 HOH   B O   
7365 O O   . HOH   E .   ? 0.6608 0.5504 0.5344 -0.1122 -0.0599 0.1923  338 HOH   B O   
7366 O O   . HOH   E .   ? 0.4326 0.6273 0.3643 -0.0684 -0.0872 0.1437  339 HOH   B O   
7367 O O   . HOH   E .   ? 0.5063 0.3177 0.5480 0.1400  0.2435  0.1825  340 HOH   B O   
7368 O O   . HOH   E .   ? 0.5689 0.4709 0.6008 -0.1084 -0.1037 -0.1365 341 HOH   B O   
7369 O O   . HOH   E .   ? 0.4369 0.4122 0.1871 0.0623  -0.0767 -0.0148 342 HOH   B O   
7370 O O   . HOH   E .   ? 0.1875 0.1507 0.2324 0.0098  -0.0155 0.0110  343 HOH   B O   
7371 O O   . HOH   E .   ? 0.3815 0.5018 0.6192 -0.0384 0.0973  0.0300  344 HOH   B O   
7372 O O   . HOH   E .   ? 0.5119 0.3287 0.2953 0.0786  -0.1134 -0.0642 345 HOH   B O   
7373 O O   . HOH   E .   ? 0.2929 0.1949 0.3685 0.0456  -0.1034 -0.0710 346 HOH   B O   
7374 O O   . HOH   E .   ? 0.2131 0.1885 0.2951 -0.0139 0.0624  -0.0116 347 HOH   B O   
7375 O O   . HOH   E .   ? 0.4306 0.6312 0.6147 -0.0252 -0.1145 0.0804  348 HOH   B O   
7376 O O   . HOH   E .   ? 0.3311 0.5625 0.4209 -0.1349 0.0464  -0.0520 349 HOH   B O   
7377 O O   . HOH   E .   ? 0.2794 0.2215 0.4614 -0.0254 -0.0659 -0.0456 350 HOH   B O   
7378 O O   . HOH   E .   ? 0.7648 0.5596 0.3408 0.0497  -0.0790 0.0564  351 HOH   B O   
7379 O O   . HOH   E .   ? 0.4237 0.5870 0.4930 -0.1123 -0.1187 -0.0912 352 HOH   B O   
7380 O O   . HOH   E .   ? 0.2316 0.4138 0.5039 0.0252  0.0531  0.0033  353 HOH   B O   
7381 O O   . HOH   E .   ? 0.4793 0.7283 0.8355 0.0896  0.1923  0.0492  354 HOH   B O   
7382 O O   . HOH   E .   ? 0.5791 0.5674 0.5605 -0.1366 0.0742  0.1279  355 HOH   B O   
7383 O O   . HOH   E .   ? 0.5581 0.2510 0.4787 -0.0812 0.1716  0.0220  356 HOH   B O   
7384 O O   . HOH   E .   ? 0.2039 0.5469 0.3363 0.1086  -0.0463 -0.1098 357 HOH   B O   
7385 O O   . HOH   E .   ? 0.3883 0.2088 0.2956 -0.0645 0.0225  -0.0795 358 HOH   B O   
7386 O O   . HOH   E .   ? 0.5069 0.5206 0.4934 0.2278  -0.1284 0.1202  359 HOH   B O   
7387 O O   . HOH   E .   ? 0.3846 0.2571 0.3852 -0.0902 -0.0291 -0.0506 360 HOH   B O   
7388 O O   . HOH   E .   ? 0.4841 0.3450 0.3836 -0.0139 0.1267  -0.0500 361 HOH   B O   
7389 O O   . HOH   E .   ? 0.5498 0.4267 0.6104 0.0574  0.1395  0.1675  362 HOH   B O   
7390 O O   . HOH   E .   ? 0.6506 0.3657 0.4976 0.0423  -0.1557 -0.0836 363 HOH   B O   
7391 O O   . HOH   E .   ? 0.4440 0.6633 0.3213 0.2378  -0.0090 0.0245  364 HOH   B O   
7392 O O   . HOH   E .   ? 0.2107 0.4438 0.6289 -0.0881 -0.0618 -0.0814 365 HOH   B O   
7393 O O   . HOH   E .   ? 0.6489 0.4500 0.4847 0.0755  0.0958  0.1076  366 HOH   B O   
7394 O O   . HOH   E .   ? 0.5503 0.5979 0.5238 -0.0322 -0.0605 -0.1122 367 HOH   B O   
7395 O O   . HOH   E .   ? 0.6097 0.2594 0.3609 0.0076  -0.0171 0.0916  368 HOH   B O   
7396 O O   . HOH   E .   ? 0.4103 0.3971 0.4953 0.0862  -0.1708 -0.0128 369 HOH   B O   
7397 O O   . HOH   E .   ? 0.4488 0.7323 0.3513 0.1756  -0.1162 0.1067  370 HOH   B O   
7398 O O   . HOH   E .   ? 0.6583 0.5288 0.3804 0.1829  0.0479  0.0866  371 HOH   B O   
7399 O O   . HOH   E .   ? 0.5402 0.2948 0.5195 -0.1060 -0.0619 -0.0021 372 HOH   B O   
7400 O O   . HOH   E .   ? 0.4179 0.6252 0.5659 0.2793  0.0505  0.1321  373 HOH   B O   
7401 O O   . HOH   E .   ? 0.6270 0.4062 0.3008 -0.0758 -0.1055 -0.0695 374 HOH   B O   
7402 O O   . HOH   E .   ? 0.4826 0.2967 0.2685 0.1041  -0.0922 -0.0392 375 HOH   B O   
7403 O O   . HOH   E .   ? 0.8146 0.7765 0.5754 0.3231  -0.1074 -0.0338 376 HOH   B O   
7404 O O   . HOH   E .   ? 0.4313 0.4893 0.4575 -0.0400 -0.0680 -0.0093 377 HOH   B O   
7405 O O   . HOH   E .   ? 0.4279 0.6157 0.6391 0.0751  0.0113  0.2587  378 HOH   B O   
7406 O O   . HOH   E .   ? 0.3483 0.5962 0.6006 0.0609  -0.0929 0.0336  379 HOH   B O   
7407 O O   . HOH   E .   ? 0.3558 0.7023 0.2173 -0.0654 -0.0012 0.0665  380 HOH   B O   
7408 O O   . HOH   E .   ? 0.2413 0.4026 0.3881 0.0337  -0.0712 -0.0787 381 HOH   B O   
7409 O O   . HOH   E .   ? 0.5115 0.7280 0.3828 -0.1333 -0.0543 -0.1339 382 HOH   B O   
7410 O O   . HOH   E .   ? 0.4925 0.6773 0.5118 -0.0536 0.1873  0.0675  383 HOH   B O   
7411 O O   . HOH   E .   ? 0.5945 0.3458 0.6213 -0.0627 -0.1272 -0.0318 384 HOH   B O   
7412 O O   . HOH   E .   ? 0.3434 0.7663 0.4279 0.1765  0.0476  0.1889  385 HOH   B O   
7413 O O   . HOH   E .   ? 0.6821 0.3214 0.4194 0.0278  0.0190  -0.1014 386 HOH   B O   
7414 O O   . HOH   E .   ? 0.2880 0.2724 0.3148 0.0163  0.0029  0.0100  387 HOH   B O   
7415 O O   . HOH   E .   ? 0.4850 0.4836 0.3307 0.0042  0.0991  0.0131  388 HOH   B O   
7416 O O   . HOH   E .   ? 0.5954 0.4626 0.5347 -0.0765 0.0397  0.0954  389 HOH   B O   
7417 O O   . HOH   E .   ? 0.2202 0.3798 0.4159 -0.0363 -0.0681 -0.0299 390 HOH   B O   
7418 O O   . HOH   E .   ? 0.7085 0.5747 0.4402 0.2435  0.0063  -0.0213 391 HOH   B O   
7419 O O   . HOH   E .   ? 0.4069 0.2260 0.2929 0.0874  -0.0505 0.0117  392 HOH   B O   
7420 O O   . HOH   E .   ? 0.5439 0.4202 0.4510 0.0558  0.0363  0.0725  393 HOH   B O   
7421 O O   . HOH   E .   ? 0.4251 0.2110 0.5777 -0.0351 0.0668  0.0858  394 HOH   B O   
7422 O O   . HOH   E .   ? 0.2567 0.4599 0.6791 -0.1378 -0.0896 0.0271  395 HOH   B O   
7423 O O   . HOH   E .   ? 0.3320 0.4402 0.3318 0.0259  0.0232  -0.0917 396 HOH   B O   
7424 O O   . HOH   E .   ? 0.4448 0.7259 0.4879 -0.0130 -0.0274 -0.1362 397 HOH   B O   
7425 O O   . HOH   E .   ? 0.5649 0.4811 0.4249 0.1461  0.1213  0.0778  398 HOH   B O   
7426 O O   . HOH   E .   ? 0.2139 0.2633 0.6082 -0.0492 -0.0747 0.0250  399 HOH   B O   
7427 O O   . HOH   E .   ? 0.5572 0.3810 0.2892 -0.2013 -0.0669 0.0745  400 HOH   B O   
7428 O O   . HOH   E .   ? 0.5249 0.5895 0.5252 -0.0713 -0.1169 0.3171  401 HOH   B O   
7429 O O   . HOH   E .   ? 0.6025 0.4819 0.3424 0.1593  -0.0292 -0.0506 402 HOH   B O   
# 
