data_7HDH
# 
_entry.id   7HDH 
# 
_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   7HDH         pdb_00007hdh 10.2210/pdb7hdh/pdb 
WWPDB D_1001407335 ?            ?                   
# 
_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                        7HDH 
_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 '[(2R)-5,5-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' 260.335   2   ? ? ? ? 
3 non-polymer syn '[(2S)-5,5-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' 260.335   1   ? ? ? ? 
4 water       nat water                                                                           18.015    413 ? ? ? ? 
# 
_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 '[(2R)-5,5-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' A1A8F 
3 '[(2S)-5,5-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' A1A8E 
4 water                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A8E non-polymer         . '[(2S)-5,5-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' ? 'C14 H20 N4 O'   
260.335 
A1A8F non-polymer         . '[(2R)-5,5-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-2-yl]methanol' ? 'C14 H20 N4 O'   
260.335 
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 A1A8F 1   201 201  A1A8F LA1 A . 
D 2 A1A8F 1   202 301  A1A8F LA2 A . 
E 3 A1A8E 1   203 401  A1A8E LA3 A . 
F 4 HOH   1   301 196  HOH   HOH A . 
F 4 HOH   2   302 292  HOH   HOH A . 
F 4 HOH   3   303 192  HOH   HOH A . 
F 4 HOH   4   304 86   HOH   HOH A . 
F 4 HOH   5   305 625  HOH   HOH A . 
F 4 HOH   6   306 109  HOH   HOH A . 
F 4 HOH   7   307 93   HOH   HOH A . 
F 4 HOH   8   308 493  HOH   HOH A . 
F 4 HOH   9   309 247  HOH   HOH A . 
F 4 HOH   10  310 1301 HOH   HOH A . 
F 4 HOH   11  311 229  HOH   HOH A . 
F 4 HOH   12  312 209  HOH   HOH A . 
F 4 HOH   13  313 1283 HOH   HOH A . 
F 4 HOH   14  314 393  HOH   HOH A . 
F 4 HOH   15  315 661  HOH   HOH A . 
F 4 HOH   16  316 124  HOH   HOH A . 
F 4 HOH   17  317 76   HOH   HOH A . 
F 4 HOH   18  318 1295 HOH   HOH A . 
F 4 HOH   19  319 136  HOH   HOH A . 
F 4 HOH   20  320 1290 HOH   HOH A . 
F 4 HOH   21  321 105  HOH   HOH A . 
F 4 HOH   22  322 964  HOH   HOH A . 
F 4 HOH   23  323 281  HOH   HOH A . 
F 4 HOH   24  324 3    HOH   HOH A . 
F 4 HOH   25  325 155  HOH   HOH A . 
F 4 HOH   26  326 1309 HOH   HOH A . 
F 4 HOH   27  327 26   HOH   HOH A . 
F 4 HOH   28  328 15   HOH   HOH A . 
F 4 HOH   29  329 396  HOH   HOH A . 
F 4 HOH   30  330 199  HOH   HOH A . 
F 4 HOH   31  331 1300 HOH   HOH A . 
F 4 HOH   32  332 164  HOH   HOH A . 
F 4 HOH   33  333 140  HOH   HOH A . 
F 4 HOH   34  334 1313 HOH   HOH A . 
F 4 HOH   35  335 236  HOH   HOH A . 
F 4 HOH   36  336 5    HOH   HOH A . 
F 4 HOH   37  337 469  HOH   HOH A . 
F 4 HOH   38  338 165  HOH   HOH A . 
F 4 HOH   39  339 8    HOH   HOH A . 
F 4 HOH   40  340 337  HOH   HOH A . 
F 4 HOH   41  341 151  HOH   HOH A . 
F 4 HOH   42  342 153  HOH   HOH A . 
F 4 HOH   43  343 36   HOH   HOH A . 
F 4 HOH   44  344 2    HOH   HOH A . 
F 4 HOH   45  345 33   HOH   HOH A . 
F 4 HOH   46  346 241  HOH   HOH A . 
F 4 HOH   47  347 225  HOH   HOH A . 
F 4 HOH   48  348 630  HOH   HOH A . 
F 4 HOH   49  349 18   HOH   HOH A . 
F 4 HOH   50  350 461  HOH   HOH A . 
F 4 HOH   51  351 42   HOH   HOH A . 
F 4 HOH   52  352 139  HOH   HOH A . 
F 4 HOH   53  353 24   HOH   HOH A . 
F 4 HOH   54  354 354  HOH   HOH A . 
F 4 HOH   55  355 102  HOH   HOH A . 
F 4 HOH   56  356 320  HOH   HOH A . 
F 4 HOH   57  357 662  HOH   HOH A . 
F 4 HOH   58  358 21   HOH   HOH A . 
F 4 HOH   59  359 169  HOH   HOH A . 
F 4 HOH   60  360 92   HOH   HOH A . 
F 4 HOH   61  361 5    HOH   HOH A . 
F 4 HOH   62  362 66   HOH   HOH A . 
F 4 HOH   63  363 19   HOH   HOH A . 
F 4 HOH   64  364 2    HOH   HOH A . 
F 4 HOH   65  365 17   HOH   HOH A . 
F 4 HOH   66  366 409  HOH   HOH A . 
F 4 HOH   67  367 162  HOH   HOH A . 
F 4 HOH   68  368 138  HOH   HOH A . 
F 4 HOH   69  369 81   HOH   HOH A . 
F 4 HOH   70  370 159  HOH   HOH A . 
F 4 HOH   71  371 218  HOH   HOH A . 
F 4 HOH   72  372 1310 HOH   HOH A . 
F 4 HOH   73  373 57   HOH   HOH A . 
F 4 HOH   74  374 46   HOH   HOH A . 
F 4 HOH   75  375 45   HOH   HOH A . 
F 4 HOH   76  376 939  HOH   HOH A . 
F 4 HOH   77  377 56   HOH   HOH A . 
F 4 HOH   78  378 78   HOH   HOH A . 
F 4 HOH   79  379 39   HOH   HOH A . 
F 4 HOH   80  380 96   HOH   HOH A . 
F 4 HOH   81  381 186  HOH   HOH A . 
F 4 HOH   82  382 27   HOH   HOH A . 
F 4 HOH   83  383 49   HOH   HOH A . 
F 4 HOH   84  384 122  HOH   HOH A . 
F 4 HOH   85  385 366  HOH   HOH A . 
F 4 HOH   86  386 62   HOH   HOH A . 
F 4 HOH   87  387 12   HOH   HOH A . 
F 4 HOH   88  388 35   HOH   HOH A . 
F 4 HOH   89  389 132  HOH   HOH A . 
F 4 HOH   90  390 134  HOH   HOH A . 
F 4 HOH   91  391 154  HOH   HOH A . 
F 4 HOH   92  392 3    HOH   HOH A . 
F 4 HOH   93  393 58   HOH   HOH A . 
F 4 HOH   94  394 83   HOH   HOH A . 
F 4 HOH   95  395 1308 HOH   HOH A . 
F 4 HOH   96  396 85   HOH   HOH A . 
F 4 HOH   97  397 1289 HOH   HOH A . 
F 4 HOH   98  398 296  HOH   HOH A . 
F 4 HOH   99  399 116  HOH   HOH A . 
F 4 HOH   100 400 1315 HOH   HOH A . 
F 4 HOH   101 401 6    HOH   HOH A . 
F 4 HOH   102 402 67   HOH   HOH A . 
F 4 HOH   103 403 121  HOH   HOH A . 
F 4 HOH   104 404 278  HOH   HOH A . 
F 4 HOH   105 405 74   HOH   HOH A . 
F 4 HOH   106 406 148  HOH   HOH A . 
F 4 HOH   107 407 4    HOH   HOH A . 
F 4 HOH   108 408 405  HOH   HOH A . 
F 4 HOH   109 409 68   HOH   HOH A . 
F 4 HOH   110 410 1134 HOH   HOH A . 
F 4 HOH   111 411 195  HOH   HOH A . 
F 4 HOH   112 412 1068 HOH   HOH A . 
F 4 HOH   113 413 123  HOH   HOH A . 
F 4 HOH   114 414 7    HOH   HOH A . 
F 4 HOH   115 415 381  HOH   HOH A . 
F 4 HOH   116 416 34   HOH   HOH A . 
F 4 HOH   117 417 53   HOH   HOH A . 
F 4 HOH   118 418 51   HOH   HOH A . 
F 4 HOH   119 419 303  HOH   HOH A . 
F 4 HOH   120 420 397  HOH   HOH A . 
F 4 HOH   121 421 25   HOH   HOH A . 
F 4 HOH   122 422 156  HOH   HOH A . 
F 4 HOH   123 423 125  HOH   HOH A . 
F 4 HOH   124 424 1222 HOH   HOH A . 
F 4 HOH   125 425 582  HOH   HOH A . 
F 4 HOH   126 426 115  HOH   HOH A . 
F 4 HOH   127 427 95   HOH   HOH A . 
F 4 HOH   128 428 351  HOH   HOH A . 
F 4 HOH   129 429 1275 HOH   HOH A . 
F 4 HOH   130 430 212  HOH   HOH A . 
F 4 HOH   131 431 1279 HOH   HOH A . 
F 4 HOH   132 432 1296 HOH   HOH A . 
F 4 HOH   133 433 333  HOH   HOH A . 
F 4 HOH   134 434 16   HOH   HOH A . 
F 4 HOH   135 435 1286 HOH   HOH A . 
F 4 HOH   136 436 1189 HOH   HOH A . 
F 4 HOH   137 437 1238 HOH   HOH A . 
F 4 HOH   138 438 1094 HOH   HOH A . 
F 4 HOH   139 439 80   HOH   HOH A . 
F 4 HOH   140 440 952  HOH   HOH A . 
F 4 HOH   141 441 70   HOH   HOH A . 
F 4 HOH   142 442 40   HOH   HOH A . 
F 4 HOH   143 443 71   HOH   HOH A . 
F 4 HOH   144 444 73   HOH   HOH A . 
F 4 HOH   145 445 944  HOH   HOH A . 
F 4 HOH   146 446 94   HOH   HOH A . 
F 4 HOH   147 447 188  HOH   HOH A . 
F 4 HOH   148 448 97   HOH   HOH A . 
F 4 HOH   149 449 104  HOH   HOH A . 
F 4 HOH   150 450 79   HOH   HOH A . 
F 4 HOH   151 451 4    HOH   HOH A . 
F 4 HOH   152 452 576  HOH   HOH A . 
F 4 HOH   153 453 330  HOH   HOH A . 
F 4 HOH   154 454 1    HOH   HOH A . 
F 4 HOH   155 455 107  HOH   HOH A . 
F 4 HOH   156 456 6    HOH   HOH A . 
F 4 HOH   157 457 509  HOH   HOH A . 
F 4 HOH   158 458 1119 HOH   HOH A . 
F 4 HOH   159 459 163  HOH   HOH A . 
F 4 HOH   160 460 726  HOH   HOH A . 
F 4 HOH   161 461 756  HOH   HOH A . 
F 4 HOH   162 462 408  HOH   HOH A . 
F 4 HOH   163 463 319  HOH   HOH A . 
F 4 HOH   164 464 370  HOH   HOH A . 
F 4 HOH   165 465 556  HOH   HOH A . 
F 4 HOH   166 466 361  HOH   HOH A . 
F 4 HOH   167 467 63   HOH   HOH A . 
F 4 HOH   168 468 126  HOH   HOH A . 
F 4 HOH   169 469 342  HOH   HOH A . 
F 4 HOH   170 470 1307 HOH   HOH A . 
F 4 HOH   171 471 801  HOH   HOH A . 
F 4 HOH   172 472 521  HOH   HOH A . 
F 4 HOH   173 473 250  HOH   HOH A . 
F 4 HOH   174 474 1276 HOH   HOH A . 
F 4 HOH   175 475 280  HOH   HOH A . 
F 4 HOH   176 476 135  HOH   HOH A . 
F 4 HOH   177 477 1306 HOH   HOH A . 
F 4 HOH   178 478 1287 HOH   HOH A . 
F 4 HOH   179 479 224  HOH   HOH A . 
F 4 HOH   180 480 711  HOH   HOH A . 
F 4 HOH   181 481 202  HOH   HOH A . 
F 4 HOH   182 482 674  HOH   HOH A . 
F 4 HOH   183 483 919  HOH   HOH A . 
F 4 HOH   184 484 695  HOH   HOH A . 
F 4 HOH   185 485 267  HOH   HOH A . 
F 4 HOH   186 486 318  HOH   HOH A . 
F 4 HOH   187 487 315  HOH   HOH A . 
F 4 HOH   188 488 1314 HOH   HOH A . 
F 4 HOH   189 489 1299 HOH   HOH A . 
F 4 HOH   190 490 309  HOH   HOH A . 
F 4 HOH   191 491 805  HOH   HOH A . 
F 4 HOH   192 492 331  HOH   HOH A . 
F 4 HOH   193 493 326  HOH   HOH A . 
F 4 HOH   194 494 356  HOH   HOH A . 
F 4 HOH   195 495 941  HOH   HOH A . 
F 4 HOH   196 496 263  HOH   HOH A . 
F 4 HOH   197 497 981  HOH   HOH A . 
F 4 HOH   198 498 1284 HOH   HOH A . 
F 4 HOH   199 499 208  HOH   HOH A . 
F 4 HOH   200 500 152  HOH   HOH A . 
F 4 HOH   201 501 1071 HOH   HOH A . 
F 4 HOH   202 502 180  HOH   HOH A . 
F 4 HOH   203 503 350  HOH   HOH A . 
F 4 HOH   204 504 363  HOH   HOH A . 
F 4 HOH   205 505 371  HOH   HOH A . 
F 4 HOH   206 506 313  HOH   HOH A . 
F 4 HOH   207 507 376  HOH   HOH A . 
F 4 HOH   208 508 185  HOH   HOH A . 
F 4 HOH   209 509 429  HOH   HOH A . 
F 4 HOH   210 510 772  HOH   HOH A . 
F 4 HOH   211 511 1074 HOH   HOH A . 
F 4 HOH   212 512 346  HOH   HOH A . 
F 4 HOH   213 513 1292 HOH   HOH A . 
F 4 HOH   214 514 1078 HOH   HOH A . 
G 4 HOH   1   201 64   HOH   HOH B . 
G 4 HOH   2   202 549  HOH   HOH B . 
G 4 HOH   3   203 240  HOH   HOH B . 
G 4 HOH   4   204 232  HOH   HOH B . 
G 4 HOH   5   205 358  HOH   HOH B . 
G 4 HOH   6   206 120  HOH   HOH B . 
G 4 HOH   7   207 364  HOH   HOH B . 
G 4 HOH   8   208 1249 HOH   HOH B . 
G 4 HOH   9   209 398  HOH   HOH B . 
G 4 HOH   10  210 900  HOH   HOH B . 
G 4 HOH   11  211 264  HOH   HOH B . 
G 4 HOH   12  212 654  HOH   HOH B . 
G 4 HOH   13  213 50   HOH   HOH B . 
G 4 HOH   14  214 353  HOH   HOH B . 
G 4 HOH   15  215 758  HOH   HOH B . 
G 4 HOH   16  216 743  HOH   HOH B . 
G 4 HOH   17  217 531  HOH   HOH B . 
G 4 HOH   18  218 444  HOH   HOH B . 
G 4 HOH   19  219 452  HOH   HOH B . 
G 4 HOH   20  220 205  HOH   HOH B . 
G 4 HOH   21  221 276  HOH   HOH B . 
G 4 HOH   22  222 332  HOH   HOH B . 
G 4 HOH   23  223 343  HOH   HOH B . 
G 4 HOH   24  224 75   HOH   HOH B . 
G 4 HOH   25  225 723  HOH   HOH B . 
G 4 HOH   26  226 131  HOH   HOH B . 
G 4 HOH   27  227 166  HOH   HOH B . 
G 4 HOH   28  228 1278 HOH   HOH B . 
G 4 HOH   29  229 172  HOH   HOH B . 
G 4 HOH   30  230 54   HOH   HOH B . 
G 4 HOH   31  231 272  HOH   HOH B . 
G 4 HOH   32  232 82   HOH   HOH B . 
G 4 HOH   33  233 325  HOH   HOH B . 
G 4 HOH   34  234 127  HOH   HOH B . 
G 4 HOH   35  235 128  HOH   HOH B . 
G 4 HOH   36  236 1140 HOH   HOH B . 
G 4 HOH   37  237 110  HOH   HOH B . 
G 4 HOH   38  238 300  HOH   HOH B . 
G 4 HOH   39  239 60   HOH   HOH B . 
G 4 HOH   40  240 133  HOH   HOH B . 
G 4 HOH   41  241 69   HOH   HOH B . 
G 4 HOH   42  242 30   HOH   HOH B . 
G 4 HOH   43  243 1    HOH   HOH B . 
G 4 HOH   44  244 41   HOH   HOH B . 
G 4 HOH   45  245 14   HOH   HOH B . 
G 4 HOH   46  246 282  HOH   HOH B . 
G 4 HOH   47  247 129  HOH   HOH B . 
G 4 HOH   48  248 72   HOH   HOH B . 
G 4 HOH   49  249 181  HOH   HOH B . 
G 4 HOH   50  250 9    HOH   HOH B . 
G 4 HOH   51  251 1312 HOH   HOH B . 
G 4 HOH   52  252 52   HOH   HOH B . 
G 4 HOH   53  253 271  HOH   HOH B . 
G 4 HOH   54  254 31   HOH   HOH B . 
G 4 HOH   55  255 150  HOH   HOH B . 
G 4 HOH   56  256 47   HOH   HOH B . 
G 4 HOH   57  257 144  HOH   HOH B . 
G 4 HOH   58  258 143  HOH   HOH B . 
G 4 HOH   59  259 252  HOH   HOH B . 
G 4 HOH   60  260 103  HOH   HOH B . 
G 4 HOH   61  261 10   HOH   HOH B . 
G 4 HOH   62  262 231  HOH   HOH B . 
G 4 HOH   63  263 391  HOH   HOH B . 
G 4 HOH   64  264 221  HOH   HOH B . 
G 4 HOH   65  265 243  HOH   HOH B . 
G 4 HOH   66  266 84   HOH   HOH B . 
G 4 HOH   67  267 287  HOH   HOH B . 
G 4 HOH   68  268 59   HOH   HOH B . 
G 4 HOH   69  269 20   HOH   HOH B . 
G 4 HOH   70  270 61   HOH   HOH B . 
G 4 HOH   71  271 347  HOH   HOH B . 
G 4 HOH   72  272 242  HOH   HOH B . 
G 4 HOH   73  273 117  HOH   HOH B . 
G 4 HOH   74  274 1277 HOH   HOH B . 
G 4 HOH   75  275 11   HOH   HOH B . 
G 4 HOH   76  276 302  HOH   HOH B . 
G 4 HOH   77  277 1106 HOH   HOH B . 
G 4 HOH   78  278 114  HOH   HOH B . 
G 4 HOH   79  279 77   HOH   HOH B . 
G 4 HOH   80  280 43   HOH   HOH B . 
G 4 HOH   81  281 175  HOH   HOH B . 
G 4 HOH   82  282 147  HOH   HOH B . 
G 4 HOH   83  283 22   HOH   HOH B . 
G 4 HOH   84  284 13   HOH   HOH B . 
G 4 HOH   85  285 89   HOH   HOH B . 
G 4 HOH   86  286 387  HOH   HOH B . 
G 4 HOH   87  287 416  HOH   HOH B . 
G 4 HOH   88  288 1066 HOH   HOH B . 
G 4 HOH   89  289 106  HOH   HOH B . 
G 4 HOH   90  290 88   HOH   HOH B . 
G 4 HOH   91  291 235  HOH   HOH B . 
G 4 HOH   92  292 1305 HOH   HOH B . 
G 4 HOH   93  293 311  HOH   HOH B . 
G 4 HOH   94  294 99   HOH   HOH B . 
G 4 HOH   95  295 316  HOH   HOH B . 
G 4 HOH   96  296 112  HOH   HOH B . 
G 4 HOH   97  297 216  HOH   HOH B . 
G 4 HOH   98  298 220  HOH   HOH B . 
G 4 HOH   99  299 160  HOH   HOH B . 
G 4 HOH   100 300 137  HOH   HOH B . 
G 4 HOH   101 301 170  HOH   HOH B . 
G 4 HOH   102 302 297  HOH   HOH B . 
G 4 HOH   103 303 704  HOH   HOH B . 
G 4 HOH   104 304 635  HOH   HOH B . 
G 4 HOH   105 305 299  HOH   HOH B . 
G 4 HOH   106 306 142  HOH   HOH B . 
G 4 HOH   107 307 38   HOH   HOH B . 
G 4 HOH   108 308 48   HOH   HOH B . 
G 4 HOH   109 309 32   HOH   HOH B . 
G 4 HOH   110 310 1285 HOH   HOH B . 
G 4 HOH   111 311 101  HOH   HOH B . 
G 4 HOH   112 312 44   HOH   HOH B . 
G 4 HOH   113 313 37   HOH   HOH B . 
G 4 HOH   114 314 177  HOH   HOH B . 
G 4 HOH   115 315 215  HOH   HOH B . 
G 4 HOH   116 316 91   HOH   HOH B . 
G 4 HOH   117 317 118  HOH   HOH B . 
G 4 HOH   118 318 341  HOH   HOH B . 
G 4 HOH   119 319 1291 HOH   HOH B . 
G 4 HOH   120 320 23   HOH   HOH B . 
G 4 HOH   121 321 28   HOH   HOH B . 
G 4 HOH   122 322 197  HOH   HOH B . 
G 4 HOH   123 323 100  HOH   HOH B . 
G 4 HOH   124 324 717  HOH   HOH B . 
G 4 HOH   125 325 207  HOH   HOH B . 
G 4 HOH   126 326 1294 HOH   HOH B . 
G 4 HOH   127 327 1274 HOH   HOH B . 
G 4 HOH   128 328 161  HOH   HOH B . 
G 4 HOH   129 329 29   HOH   HOH B . 
G 4 HOH   130 330 182  HOH   HOH B . 
G 4 HOH   131 331 141  HOH   HOH B . 
G 4 HOH   132 332 55   HOH   HOH B . 
G 4 HOH   133 333 98   HOH   HOH B . 
G 4 HOH   134 334 1126 HOH   HOH B . 
G 4 HOH   135 335 445  HOH   HOH B . 
G 4 HOH   136 336 234  HOH   HOH B . 
G 4 HOH   137 337 334  HOH   HOH B . 
G 4 HOH   138 338 65   HOH   HOH B . 
G 4 HOH   139 339 339  HOH   HOH B . 
G 4 HOH   140 340 619  HOH   HOH B . 
G 4 HOH   141 341 1293 HOH   HOH B . 
G 4 HOH   142 342 362  HOH   HOH B . 
G 4 HOH   143 343 960  HOH   HOH B . 
G 4 HOH   144 344 178  HOH   HOH B . 
G 4 HOH   145 345 90   HOH   HOH B . 
G 4 HOH   146 346 463  HOH   HOH B . 
G 4 HOH   147 347 87   HOH   HOH B . 
G 4 HOH   148 348 191  HOH   HOH B . 
G 4 HOH   149 349 623  HOH   HOH B . 
G 4 HOH   150 350 335  HOH   HOH B . 
G 4 HOH   151 351 203  HOH   HOH B . 
G 4 HOH   152 352 304  HOH   HOH B . 
G 4 HOH   153 353 1304 HOH   HOH B . 
G 4 HOH   154 354 1280 HOH   HOH B . 
G 4 HOH   155 355 1046 HOH   HOH B . 
G 4 HOH   156 356 1077 HOH   HOH B . 
G 4 HOH   157 357 290  HOH   HOH B . 
G 4 HOH   158 358 541  HOH   HOH B . 
G 4 HOH   159 359 389  HOH   HOH B . 
G 4 HOH   160 360 718  HOH   HOH B . 
G 4 HOH   161 361 1072 HOH   HOH B . 
G 4 HOH   162 362 283  HOH   HOH B . 
G 4 HOH   163 363 479  HOH   HOH B . 
G 4 HOH   164 364 291  HOH   HOH B . 
G 4 HOH   165 365 898  HOH   HOH B . 
G 4 HOH   166 366 373  HOH   HOH B . 
G 4 HOH   167 367 615  HOH   HOH B . 
G 4 HOH   168 368 340  HOH   HOH B . 
G 4 HOH   169 369 667  HOH   HOH B . 
G 4 HOH   170 370 1316 HOH   HOH B . 
G 4 HOH   171 371 190  HOH   HOH B . 
G 4 HOH   172 372 1303 HOH   HOH B . 
G 4 HOH   173 373 310  HOH   HOH B . 
G 4 HOH   174 374 431  HOH   HOH B . 
G 4 HOH   175 375 149  HOH   HOH B . 
G 4 HOH   176 376 183  HOH   HOH B . 
G 4 HOH   177 377 1173 HOH   HOH B . 
G 4 HOH   178 378 418  HOH   HOH B . 
G 4 HOH   179 379 1163 HOH   HOH B . 
G 4 HOH   180 380 1000 HOH   HOH B . 
G 4 HOH   181 381 176  HOH   HOH B . 
G 4 HOH   182 382 491  HOH   HOH B . 
G 4 HOH   183 383 1311 HOH   HOH B . 
G 4 HOH   184 384 424  HOH   HOH B . 
G 4 HOH   185 385 248  HOH   HOH B . 
G 4 HOH   186 386 265  HOH   HOH B . 
G 4 HOH   187 387 1298 HOH   HOH B . 
G 4 HOH   188 388 470  HOH   HOH B . 
G 4 HOH   189 389 184  HOH   HOH B . 
G 4 HOH   190 390 360  HOH   HOH B . 
G 4 HOH   191 391 410  HOH   HOH B . 
G 4 HOH   192 392 355  HOH   HOH B . 
G 4 HOH   193 393 274  HOH   HOH B . 
G 4 HOH   194 394 314  HOH   HOH B . 
G 4 HOH   195 395 566  HOH   HOH B . 
G 4 HOH   196 396 157  HOH   HOH B . 
G 4 HOH   197 397 321  HOH   HOH B . 
G 4 HOH   198 398 792  HOH   HOH B . 
G 4 HOH   199 399 558  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           7HDH 
_cell.length_a           88.853 
_cell.length_b           88.853 
_cell.length_c           39.488 
_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                         7HDH 
_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          7HDH 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.72 
_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                     7HDH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.430 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165608 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.046 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.800 
_reflns.B_iso_Wilson_estimate        12.380 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.050 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1060691 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 34163 7588 ? 1.614 ? ? ? 4.500 ? 0.700  ? ? ? ? ? ? 93.000 1.825 0.832 0.499 
1 2 5.480 44.430 ? 7512  1094 ? 0.033 ? ? ? 6.900 ? 52.000 ? ? ? ? ? ? 99.800 0.036 0.014 0.999 
# 
_refine.entry_id                                 7HDH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.4300 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5400 
_refine.ls_number_reflns_obs                     165498 
_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                          0.1453 
_refine.ls_R_factor_R_work                       0.1447 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1579 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7973 
_refine.ls_number_reflns_R_work                  157525 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.0407 
_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                            0.1100 
_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                                79.370 
_refine.B_iso_min                                8.370 
_refine.pdbx_overall_phase_error                 18.2800 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.4300 
_refine_hist.pdbx_number_atoms_ligand         117 
_refine_hist.number_atoms_solvent             413 
_refine_hist.number_atoms_total               3072 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.01 
_refine_hist.pdbx_B_iso_mean_solvent          31.47 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 91.0000  4797 . 0.4311 0.4063 . 245 0.0000 5042 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  5083 . 0.3536 0.3723 . 229 0.0000 5312 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5243 . 0.3088 0.2989 . 243 0.0000 5486 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5188 . 0.2633 0.2727 . 276 0.0000 5464 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5179 . 0.2374 0.2348 . 330 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5295 . 0.2160 0.2458 . 255 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5245 . 0.2003 0.2270 . 256 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5233 . 0.1844 0.2076 . 257 0.0000 5490 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5246 . 0.1722 0.1927 . 278 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5297 . 0.1592 0.1747 . 243 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5252 . 0.1509 0.1760 . 252 0.0000 5504 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5273 . 0.1416 0.1757 . 271 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5203 . 0.1318 0.1722 . 295 0.0000 5498 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5289 . 0.1276 0.1573 . 237 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5230 . 0.1290 0.1412 . 259 0.0000 5489 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5274 . 0.1277 0.1433 . 273 0.0000 5547 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5242 . 0.1269 0.1471 . 290 0.0000 5532 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5250 . 0.1288 0.1434 . 271 0.0000 5521 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5293 . 0.1280 0.1502 . 249 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5227 . 0.1279 0.1546 . 262 0.0000 5489 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5348 . 0.1234 0.1258 . 253 0.0000 5601 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5225 . 0.1190 0.1305 . 282 0.0000 5507 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5279 . 0.1184 0.1340 . 261 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5323 . 0.1247 0.1452 . 270 0.0000 5593 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5271 . 0.1342 0.1326 . 250 0.0000 5521 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5295 . 0.1333 0.1324 . 282 0.0000 5577 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5301 . 0.1367 0.1383 . 287 0.0000 5588 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5306 . 0.1367 0.1442 . 292 0.0000 5598 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5347 . 0.1485 0.1684 . 256 0.0000 5603 . 'X-RAY DIFFRACTION' 
3.1100 44.4300 30 100.0000 5491 . 0.1479 0.1671 . 269 0.0000 5760 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDH 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003726' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDH 
_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 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HDH A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDH 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 7HDH SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDH MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDH SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDH MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HDH 
_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_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.15   -132.64 
2 1 ASP A 157 ? B -163.29 111.04  
3 1 HIS B 86  ? ? 57.30   -127.60 
# 
_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 512 ? 5.94 . 
2 1 O ? A HOH 513 ? 5.95 . 
3 1 O ? A HOH 514 ? 7.60 . 
4 1 O ? B HOH 399 ? 6.57 . 
# 
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 
A1A8E C1   C N N 1   
A1A8E C2   C N N 2   
A1A8E C3   C N N 3   
A1A8E C4   C N N 4   
A1A8E C5   C N N 5   
A1A8E C6   C N S 6   
A1A8E C7   C N N 7   
A1A8E C8   C Y N 8   
A1A8E C9   C Y N 9   
A1A8E C10  C Y N 10  
A1A8E C11  C Y N 11  
A1A8E C12  C Y N 12  
A1A8E C13  C Y N 13  
A1A8E C14  C N N 14  
A1A8E N1   N N N 15  
A1A8E N2   N Y N 16  
A1A8E N3   N Y N 17  
A1A8E N4   N Y N 18  
A1A8E O1   O N N 19  
A1A8E H3   H N N 20  
A1A8E H4   H N N 21  
A1A8E H2   H N N 22  
A1A8E H6   H N N 23  
A1A8E H7   H N N 24  
A1A8E H5   H N N 25  
A1A8E H9   H N N 26  
A1A8E H8   H N N 27  
A1A8E H10  H N N 28  
A1A8E H11  H N N 29  
A1A8E H1   H N N 30  
A1A8E H13  H N N 31  
A1A8E H12  H N N 32  
A1A8E H15  H N N 33  
A1A8E H16  H N N 34  
A1A8E H17  H N N 35  
A1A8E H19  H N N 36  
A1A8E H20  H N N 37  
A1A8E H18  H N N 38  
A1A8E H14  H N N 39  
A1A8F O1   O N N 40  
A1A8F C1   C N N 41  
A1A8F C2   C N N 42  
A1A8F C3   C N N 43  
A1A8F C4   C N N 44  
A1A8F C5   C N N 45  
A1A8F C6   C N R 46  
A1A8F C7   C N N 47  
A1A8F C8   C Y N 48  
A1A8F C10  C Y N 49  
A1A8F C11  C Y N 50  
A1A8F C12  C Y N 51  
A1A8F C13  C Y N 52  
A1A8F C14  C N N 53  
A1A8F C9   C Y N 54  
A1A8F N1   N N N 55  
A1A8F N2   N Y N 56  
A1A8F N3   N Y N 57  
A1A8F N4   N Y N 58  
A1A8F H14  H N N 59  
A1A8F H3   H N N 60  
A1A8F H4   H N N 61  
A1A8F H2   H N N 62  
A1A8F H6   H N N 63  
A1A8F H5   H N N 64  
A1A8F H7   H N N 65  
A1A8F H8   H N N 66  
A1A8F H9   H N N 67  
A1A8F H11  H N N 68  
A1A8F H10  H N N 69  
A1A8F H1   H N N 70  
A1A8F H12  H N N 71  
A1A8F H13  H N N 72  
A1A8F H16  H N N 73  
A1A8F H17  H N N 74  
A1A8F H19  H N N 75  
A1A8F H20  H N N 76  
A1A8F H15  H N N 77  
A1A8F H18  H N N 78  
ALA   N    N N N 79  
ALA   CA   C N S 80  
ALA   C    C N N 81  
ALA   O    O N N 82  
ALA   CB   C N N 83  
ALA   OXT  O N N 84  
ALA   H    H N N 85  
ALA   H2   H N N 86  
ALA   HA   H N N 87  
ALA   HB1  H N N 88  
ALA   HB2  H N N 89  
ALA   HB3  H N N 90  
ALA   HXT  H N N 91  
ARG   N    N N N 92  
ARG   CA   C N S 93  
ARG   C    C N N 94  
ARG   O    O N N 95  
ARG   CB   C N N 96  
ARG   CG   C N N 97  
ARG   CD   C N N 98  
ARG   NE   N N N 99  
ARG   CZ   C N N 100 
ARG   NH1  N N N 101 
ARG   NH2  N N N 102 
ARG   OXT  O N N 103 
ARG   H    H N N 104 
ARG   H2   H N N 105 
ARG   HA   H N N 106 
ARG   HB2  H N N 107 
ARG   HB3  H N N 108 
ARG   HG2  H N N 109 
ARG   HG3  H N N 110 
ARG   HD2  H N N 111 
ARG   HD3  H N N 112 
ARG   HE   H N N 113 
ARG   HH11 H N N 114 
ARG   HH12 H N N 115 
ARG   HH21 H N N 116 
ARG   HH22 H N N 117 
ARG   HXT  H N N 118 
ASN   N    N N N 119 
ASN   CA   C N S 120 
ASN   C    C N N 121 
ASN   O    O N N 122 
ASN   CB   C N N 123 
ASN   CG   C N N 124 
ASN   OD1  O N N 125 
ASN   ND2  N N N 126 
ASN   OXT  O N N 127 
ASN   H    H N N 128 
ASN   H2   H N N 129 
ASN   HA   H N N 130 
ASN   HB2  H N N 131 
ASN   HB3  H N N 132 
ASN   HD21 H N N 133 
ASN   HD22 H N N 134 
ASN   HXT  H N N 135 
ASP   N    N N N 136 
ASP   CA   C N S 137 
ASP   C    C N N 138 
ASP   O    O N N 139 
ASP   CB   C N N 140 
ASP   CG   C N N 141 
ASP   OD1  O N N 142 
ASP   OD2  O N N 143 
ASP   OXT  O N N 144 
ASP   H    H N N 145 
ASP   H2   H N N 146 
ASP   HA   H N N 147 
ASP   HB2  H N N 148 
ASP   HB3  H N N 149 
ASP   HD2  H N N 150 
ASP   HXT  H N N 151 
CYS   N    N N N 152 
CYS   CA   C N R 153 
CYS   C    C N N 154 
CYS   O    O N N 155 
CYS   CB   C N N 156 
CYS   SG   S N N 157 
CYS   OXT  O N N 158 
CYS   H    H N N 159 
CYS   H2   H N N 160 
CYS   HA   H N N 161 
CYS   HB2  H N N 162 
CYS   HB3  H N N 163 
CYS   HG   H N N 164 
CYS   HXT  H N N 165 
GLN   N    N N N 166 
GLN   CA   C N S 167 
GLN   C    C N N 168 
GLN   O    O N N 169 
GLN   CB   C N N 170 
GLN   CG   C N N 171 
GLN   CD   C N N 172 
GLN   OE1  O N N 173 
GLN   NE2  N N N 174 
GLN   OXT  O N N 175 
GLN   H    H N N 176 
GLN   H2   H N N 177 
GLN   HA   H N N 178 
GLN   HB2  H N N 179 
GLN   HB3  H N N 180 
GLN   HG2  H N N 181 
GLN   HG3  H N N 182 
GLN   HE21 H N N 183 
GLN   HE22 H N N 184 
GLN   HXT  H N N 185 
GLU   N    N N N 186 
GLU   CA   C N S 187 
GLU   C    C N N 188 
GLU   O    O N N 189 
GLU   CB   C N N 190 
GLU   CG   C N N 191 
GLU   CD   C N N 192 
GLU   OE1  O N N 193 
GLU   OE2  O N N 194 
GLU   OXT  O N N 195 
GLU   H    H N N 196 
GLU   H2   H N N 197 
GLU   HA   H N N 198 
GLU   HB2  H N N 199 
GLU   HB3  H N N 200 
GLU   HG2  H N N 201 
GLU   HG3  H N N 202 
GLU   HE2  H N N 203 
GLU   HXT  H N N 204 
GLY   N    N N N 205 
GLY   CA   C N N 206 
GLY   C    C N N 207 
GLY   O    O N N 208 
GLY   OXT  O N N 209 
GLY   H    H N N 210 
GLY   H2   H N N 211 
GLY   HA2  H N N 212 
GLY   HA3  H N N 213 
GLY   HXT  H N N 214 
HIS   N    N N N 215 
HIS   CA   C N S 216 
HIS   C    C N N 217 
HIS   O    O N N 218 
HIS   CB   C N N 219 
HIS   CG   C Y N 220 
HIS   ND1  N Y N 221 
HIS   CD2  C Y N 222 
HIS   CE1  C Y N 223 
HIS   NE2  N Y N 224 
HIS   OXT  O N N 225 
HIS   H    H N N 226 
HIS   H2   H N N 227 
HIS   HA   H N N 228 
HIS   HB2  H N N 229 
HIS   HB3  H N N 230 
HIS   HD1  H N N 231 
HIS   HD2  H N N 232 
HIS   HE1  H N N 233 
HIS   HE2  H N N 234 
HIS   HXT  H N N 235 
HOH   O    O N N 236 
HOH   H1   H N N 237 
HOH   H2   H N N 238 
ILE   N    N N N 239 
ILE   CA   C N S 240 
ILE   C    C N N 241 
ILE   O    O N N 242 
ILE   CB   C N S 243 
ILE   CG1  C N N 244 
ILE   CG2  C N N 245 
ILE   CD1  C N N 246 
ILE   OXT  O N N 247 
ILE   H    H N N 248 
ILE   H2   H N N 249 
ILE   HA   H N N 250 
ILE   HB   H N N 251 
ILE   HG12 H N N 252 
ILE   HG13 H N N 253 
ILE   HG21 H N N 254 
ILE   HG22 H N N 255 
ILE   HG23 H N N 256 
ILE   HD11 H N N 257 
ILE   HD12 H N N 258 
ILE   HD13 H N N 259 
ILE   HXT  H N N 260 
LEU   N    N N N 261 
LEU   CA   C N S 262 
LEU   C    C N N 263 
LEU   O    O N N 264 
LEU   CB   C N N 265 
LEU   CG   C N N 266 
LEU   CD1  C N N 267 
LEU   CD2  C N N 268 
LEU   OXT  O N N 269 
LEU   H    H N N 270 
LEU   H2   H N N 271 
LEU   HA   H N N 272 
LEU   HB2  H N N 273 
LEU   HB3  H N N 274 
LEU   HG   H N N 275 
LEU   HD11 H N N 276 
LEU   HD12 H N N 277 
LEU   HD13 H N N 278 
LEU   HD21 H N N 279 
LEU   HD22 H N N 280 
LEU   HD23 H N N 281 
LEU   HXT  H N N 282 
LYS   N    N N N 283 
LYS   CA   C N S 284 
LYS   C    C N N 285 
LYS   O    O N N 286 
LYS   CB   C N N 287 
LYS   CG   C N N 288 
LYS   CD   C N N 289 
LYS   CE   C N N 290 
LYS   NZ   N N N 291 
LYS   OXT  O N N 292 
LYS   H    H N N 293 
LYS   H2   H N N 294 
LYS   HA   H N N 295 
LYS   HB2  H N N 296 
LYS   HB3  H N N 297 
LYS   HG2  H N N 298 
LYS   HG3  H N N 299 
LYS   HD2  H N N 300 
LYS   HD3  H N N 301 
LYS   HE2  H N N 302 
LYS   HE3  H N N 303 
LYS   HZ1  H N N 304 
LYS   HZ2  H N N 305 
LYS   HZ3  H N N 306 
LYS   HXT  H N N 307 
MET   N    N N N 308 
MET   CA   C N S 309 
MET   C    C N N 310 
MET   O    O N N 311 
MET   CB   C N N 312 
MET   CG   C N N 313 
MET   SD   S N N 314 
MET   CE   C N N 315 
MET   OXT  O N N 316 
MET   H    H N N 317 
MET   H2   H N N 318 
MET   HA   H N N 319 
MET   HB2  H N N 320 
MET   HB3  H N N 321 
MET   HG2  H N N 322 
MET   HG3  H N N 323 
MET   HE1  H N N 324 
MET   HE2  H N N 325 
MET   HE3  H N N 326 
MET   HXT  H N N 327 
PHE   N    N N N 328 
PHE   CA   C N S 329 
PHE   C    C N N 330 
PHE   O    O N N 331 
PHE   CB   C N N 332 
PHE   CG   C Y N 333 
PHE   CD1  C Y N 334 
PHE   CD2  C Y N 335 
PHE   CE1  C Y N 336 
PHE   CE2  C Y N 337 
PHE   CZ   C Y N 338 
PHE   OXT  O N N 339 
PHE   H    H N N 340 
PHE   H2   H N N 341 
PHE   HA   H N N 342 
PHE   HB2  H N N 343 
PHE   HB3  H N N 344 
PHE   HD1  H N N 345 
PHE   HD2  H N N 346 
PHE   HE1  H N N 347 
PHE   HE2  H N N 348 
PHE   HZ   H N N 349 
PHE   HXT  H N N 350 
PRO   N    N N N 351 
PRO   CA   C N S 352 
PRO   C    C N N 353 
PRO   O    O N N 354 
PRO   CB   C N N 355 
PRO   CG   C N N 356 
PRO   CD   C N N 357 
PRO   OXT  O N N 358 
PRO   H    H N N 359 
PRO   HA   H N N 360 
PRO   HB2  H N N 361 
PRO   HB3  H N N 362 
PRO   HG2  H N N 363 
PRO   HG3  H N N 364 
PRO   HD2  H N N 365 
PRO   HD3  H N N 366 
PRO   HXT  H N N 367 
SER   N    N N N 368 
SER   CA   C N S 369 
SER   C    C N N 370 
SER   O    O N N 371 
SER   CB   C N N 372 
SER   OG   O N N 373 
SER   OXT  O N N 374 
SER   H    H N N 375 
SER   H2   H N N 376 
SER   HA   H N N 377 
SER   HB2  H N N 378 
SER   HB3  H N N 379 
SER   HG   H N N 380 
SER   HXT  H N N 381 
THR   N    N N N 382 
THR   CA   C N S 383 
THR   C    C N N 384 
THR   O    O N N 385 
THR   CB   C N R 386 
THR   OG1  O N N 387 
THR   CG2  C N N 388 
THR   OXT  O N N 389 
THR   H    H N N 390 
THR   H2   H N N 391 
THR   HA   H N N 392 
THR   HB   H N N 393 
THR   HG1  H N N 394 
THR   HG21 H N N 395 
THR   HG22 H N N 396 
THR   HG23 H N N 397 
THR   HXT  H N N 398 
TYR   N    N N N 399 
TYR   CA   C N S 400 
TYR   C    C N N 401 
TYR   O    O N N 402 
TYR   CB   C N N 403 
TYR   CG   C Y N 404 
TYR   CD1  C Y N 405 
TYR   CD2  C Y N 406 
TYR   CE1  C Y N 407 
TYR   CE2  C Y N 408 
TYR   CZ   C Y N 409 
TYR   OH   O N N 410 
TYR   OXT  O N N 411 
TYR   H    H N N 412 
TYR   H2   H N N 413 
TYR   HA   H N N 414 
TYR   HB2  H N N 415 
TYR   HB3  H N N 416 
TYR   HD1  H N N 417 
TYR   HD2  H N N 418 
TYR   HE1  H N N 419 
TYR   HE2  H N N 420 
TYR   HH   H N N 421 
TYR   HXT  H N N 422 
VAL   N    N N N 423 
VAL   CA   C N S 424 
VAL   C    C N N 425 
VAL   O    O N N 426 
VAL   CB   C N N 427 
VAL   CG1  C N N 428 
VAL   CG2  C N N 429 
VAL   OXT  O N N 430 
VAL   H    H N N 431 
VAL   H2   H N N 432 
VAL   HA   H N N 433 
VAL   HB   H N N 434 
VAL   HG11 H N N 435 
VAL   HG12 H N N 436 
VAL   HG13 H N N 437 
VAL   HG21 H N N 438 
VAL   HG22 H N N 439 
VAL   HG23 H N N 440 
VAL   HXT  H N N 441 
# 
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 
A1A8E C1  C2   sing N N 1   
A1A8E O1  C7   sing N N 2   
A1A8E C7  C6   sing N N 3   
A1A8E C5  C4   sing N N 4   
A1A8E C5  C6   sing N N 5   
A1A8E C2  C4   sing N N 6   
A1A8E C2  C3   sing N N 7   
A1A8E C2  C14  sing N N 8   
A1A8E C6  N1   sing N N 9   
A1A8E C14 N1   sing N N 10  
A1A8E N1  C8   sing N N 11  
A1A8E C8  C11  doub Y N 12  
A1A8E C8  N2   sing Y N 13  
A1A8E C12 C11  sing Y N 14  
A1A8E C12 C13  doub Y N 15  
A1A8E C11 C10  sing Y N 16  
A1A8E N2  C9   doub Y N 17  
A1A8E C13 N4   sing Y N 18  
A1A8E C9  N3   sing Y N 19  
A1A8E C10 N4   sing Y N 20  
A1A8E C10 N3   doub Y N 21  
A1A8E C1  H3   sing N N 22  
A1A8E C1  H4   sing N N 23  
A1A8E C1  H2   sing N N 24  
A1A8E C3  H6   sing N N 25  
A1A8E C3  H7   sing N N 26  
A1A8E C3  H5   sing N N 27  
A1A8E C4  H9   sing N N 28  
A1A8E C4  H8   sing N N 29  
A1A8E C5  H10  sing N N 30  
A1A8E C5  H11  sing N N 31  
A1A8E C6  H1   sing N N 32  
A1A8E C7  H13  sing N N 33  
A1A8E C7  H12  sing N N 34  
A1A8E C9  H15  sing N N 35  
A1A8E C12 H16  sing N N 36  
A1A8E C13 H17  sing N N 37  
A1A8E C14 H19  sing N N 38  
A1A8E C14 H20  sing N N 39  
A1A8E N4  H18  sing N N 40  
A1A8E O1  H14  sing N N 41  
A1A8F C1  C2   sing N N 42  
A1A8F C3  C2   sing N N 43  
A1A8F C4  C2   sing N N 44  
A1A8F C4  C5   sing N N 45  
A1A8F C2  C14  sing N N 46  
A1A8F C5  C6   sing N N 47  
A1A8F C14 N1   sing N N 48  
A1A8F C6  N1   sing N N 49  
A1A8F C6  C7   sing N N 50  
A1A8F N1  C8   sing N N 51  
A1A8F C7  O1   sing N N 52  
A1A8F C12 C11  sing Y N 53  
A1A8F C12 C13  doub Y N 54  
A1A8F C8  C11  doub Y N 55  
A1A8F C8  N2   sing Y N 56  
A1A8F C11 C10  sing Y N 57  
A1A8F C13 N4   sing Y N 58  
A1A8F N2  C9   doub Y N 59  
A1A8F C10 N4   sing Y N 60  
A1A8F C10 N3   doub Y N 61  
A1A8F C9  N3   sing Y N 62  
A1A8F O1  H14  sing N N 63  
A1A8F C1  H3   sing N N 64  
A1A8F C1  H4   sing N N 65  
A1A8F C1  H2   sing N N 66  
A1A8F C3  H6   sing N N 67  
A1A8F C3  H5   sing N N 68  
A1A8F C3  H7   sing N N 69  
A1A8F C4  H8   sing N N 70  
A1A8F C4  H9   sing N N 71  
A1A8F C5  H11  sing N N 72  
A1A8F C5  H10  sing N N 73  
A1A8F C6  H1   sing N N 74  
A1A8F C7  H12  sing N N 75  
A1A8F C7  H13  sing N N 76  
A1A8F C12 H16  sing N N 77  
A1A8F C13 H17  sing N N 78  
A1A8F C14 H19  sing N N 79  
A1A8F C14 H20  sing N N 80  
A1A8F C9  H15  sing N N 81  
A1A8F N4  H18  sing N N 82  
ALA   N   CA   sing N N 83  
ALA   N   H    sing N N 84  
ALA   N   H2   sing N N 85  
ALA   CA  C    sing N N 86  
ALA   CA  CB   sing N N 87  
ALA   CA  HA   sing N N 88  
ALA   C   O    doub N N 89  
ALA   C   OXT  sing N N 90  
ALA   CB  HB1  sing N N 91  
ALA   CB  HB2  sing N N 92  
ALA   CB  HB3  sing N N 93  
ALA   OXT HXT  sing N N 94  
ARG   N   CA   sing N N 95  
ARG   N   H    sing N N 96  
ARG   N   H2   sing N N 97  
ARG   CA  C    sing N N 98  
ARG   CA  CB   sing N N 99  
ARG   CA  HA   sing N N 100 
ARG   C   O    doub N N 101 
ARG   C   OXT  sing N N 102 
ARG   CB  CG   sing N N 103 
ARG   CB  HB2  sing N N 104 
ARG   CB  HB3  sing N N 105 
ARG   CG  CD   sing N N 106 
ARG   CG  HG2  sing N N 107 
ARG   CG  HG3  sing N N 108 
ARG   CD  NE   sing N N 109 
ARG   CD  HD2  sing N N 110 
ARG   CD  HD3  sing N N 111 
ARG   NE  CZ   sing N N 112 
ARG   NE  HE   sing N N 113 
ARG   CZ  NH1  sing N N 114 
ARG   CZ  NH2  doub N N 115 
ARG   NH1 HH11 sing N N 116 
ARG   NH1 HH12 sing N N 117 
ARG   NH2 HH21 sing N N 118 
ARG   NH2 HH22 sing N N 119 
ARG   OXT HXT  sing N N 120 
ASN   N   CA   sing N N 121 
ASN   N   H    sing N N 122 
ASN   N   H2   sing N N 123 
ASN   CA  C    sing N N 124 
ASN   CA  CB   sing N N 125 
ASN   CA  HA   sing N N 126 
ASN   C   O    doub N N 127 
ASN   C   OXT  sing N N 128 
ASN   CB  CG   sing N N 129 
ASN   CB  HB2  sing N N 130 
ASN   CB  HB3  sing N N 131 
ASN   CG  OD1  doub N N 132 
ASN   CG  ND2  sing N N 133 
ASN   ND2 HD21 sing N N 134 
ASN   ND2 HD22 sing N N 135 
ASN   OXT HXT  sing N N 136 
ASP   N   CA   sing N N 137 
ASP   N   H    sing N N 138 
ASP   N   H2   sing N N 139 
ASP   CA  C    sing N N 140 
ASP   CA  CB   sing N N 141 
ASP   CA  HA   sing N N 142 
ASP   C   O    doub N N 143 
ASP   C   OXT  sing N N 144 
ASP   CB  CG   sing N N 145 
ASP   CB  HB2  sing N N 146 
ASP   CB  HB3  sing N N 147 
ASP   CG  OD1  doub N N 148 
ASP   CG  OD2  sing N N 149 
ASP   OD2 HD2  sing N N 150 
ASP   OXT HXT  sing N N 151 
CYS   N   CA   sing N N 152 
CYS   N   H    sing N N 153 
CYS   N   H2   sing N N 154 
CYS   CA  C    sing N N 155 
CYS   CA  CB   sing N N 156 
CYS   CA  HA   sing N N 157 
CYS   C   O    doub N N 158 
CYS   C   OXT  sing N N 159 
CYS   CB  SG   sing N N 160 
CYS   CB  HB2  sing N N 161 
CYS   CB  HB3  sing N N 162 
CYS   SG  HG   sing N N 163 
CYS   OXT HXT  sing N N 164 
GLN   N   CA   sing N N 165 
GLN   N   H    sing N N 166 
GLN   N   H2   sing N N 167 
GLN   CA  C    sing N N 168 
GLN   CA  CB   sing N N 169 
GLN   CA  HA   sing N N 170 
GLN   C   O    doub N N 171 
GLN   C   OXT  sing N N 172 
GLN   CB  CG   sing N N 173 
GLN   CB  HB2  sing N N 174 
GLN   CB  HB3  sing N N 175 
GLN   CG  CD   sing N N 176 
GLN   CG  HG2  sing N N 177 
GLN   CG  HG3  sing N N 178 
GLN   CD  OE1  doub N N 179 
GLN   CD  NE2  sing N N 180 
GLN   NE2 HE21 sing N N 181 
GLN   NE2 HE22 sing N N 182 
GLN   OXT HXT  sing N N 183 
GLU   N   CA   sing N N 184 
GLU   N   H    sing N N 185 
GLU   N   H2   sing N N 186 
GLU   CA  C    sing N N 187 
GLU   CA  CB   sing N N 188 
GLU   CA  HA   sing N N 189 
GLU   C   O    doub N N 190 
GLU   C   OXT  sing N N 191 
GLU   CB  CG   sing N N 192 
GLU   CB  HB2  sing N N 193 
GLU   CB  HB3  sing N N 194 
GLU   CG  CD   sing N N 195 
GLU   CG  HG2  sing N N 196 
GLU   CG  HG3  sing N N 197 
GLU   CD  OE1  doub N N 198 
GLU   CD  OE2  sing N N 199 
GLU   OE2 HE2  sing N N 200 
GLU   OXT HXT  sing N N 201 
GLY   N   CA   sing N N 202 
GLY   N   H    sing N N 203 
GLY   N   H2   sing N N 204 
GLY   CA  C    sing N N 205 
GLY   CA  HA2  sing N N 206 
GLY   CA  HA3  sing N N 207 
GLY   C   O    doub N N 208 
GLY   C   OXT  sing N N 209 
GLY   OXT HXT  sing N N 210 
HIS   N   CA   sing N N 211 
HIS   N   H    sing N N 212 
HIS   N   H2   sing N N 213 
HIS   CA  C    sing N N 214 
HIS   CA  CB   sing N N 215 
HIS   CA  HA   sing N N 216 
HIS   C   O    doub N N 217 
HIS   C   OXT  sing N N 218 
HIS   CB  CG   sing N N 219 
HIS   CB  HB2  sing N N 220 
HIS   CB  HB3  sing N N 221 
HIS   CG  ND1  sing Y N 222 
HIS   CG  CD2  doub Y N 223 
HIS   ND1 CE1  doub Y N 224 
HIS   ND1 HD1  sing N N 225 
HIS   CD2 NE2  sing Y N 226 
HIS   CD2 HD2  sing N N 227 
HIS   CE1 NE2  sing Y N 228 
HIS   CE1 HE1  sing N N 229 
HIS   NE2 HE2  sing N N 230 
HIS   OXT HXT  sing N N 231 
HOH   O   H1   sing N N 232 
HOH   O   H2   sing N N 233 
ILE   N   CA   sing N N 234 
ILE   N   H    sing N N 235 
ILE   N   H2   sing N N 236 
ILE   CA  C    sing N N 237 
ILE   CA  CB   sing N N 238 
ILE   CA  HA   sing N N 239 
ILE   C   O    doub N N 240 
ILE   C   OXT  sing N N 241 
ILE   CB  CG1  sing N N 242 
ILE   CB  CG2  sing N N 243 
ILE   CB  HB   sing N N 244 
ILE   CG1 CD1  sing N N 245 
ILE   CG1 HG12 sing N N 246 
ILE   CG1 HG13 sing N N 247 
ILE   CG2 HG21 sing N N 248 
ILE   CG2 HG22 sing N N 249 
ILE   CG2 HG23 sing N N 250 
ILE   CD1 HD11 sing N N 251 
ILE   CD1 HD12 sing N N 252 
ILE   CD1 HD13 sing N N 253 
ILE   OXT HXT  sing N N 254 
LEU   N   CA   sing N N 255 
LEU   N   H    sing N N 256 
LEU   N   H2   sing N N 257 
LEU   CA  C    sing N N 258 
LEU   CA  CB   sing N N 259 
LEU   CA  HA   sing N N 260 
LEU   C   O    doub N N 261 
LEU   C   OXT  sing N N 262 
LEU   CB  CG   sing N N 263 
LEU   CB  HB2  sing N N 264 
LEU   CB  HB3  sing N N 265 
LEU   CG  CD1  sing N N 266 
LEU   CG  CD2  sing N N 267 
LEU   CG  HG   sing N N 268 
LEU   CD1 HD11 sing N N 269 
LEU   CD1 HD12 sing N N 270 
LEU   CD1 HD13 sing N N 271 
LEU   CD2 HD21 sing N N 272 
LEU   CD2 HD22 sing N N 273 
LEU   CD2 HD23 sing N N 274 
LEU   OXT HXT  sing N N 275 
LYS   N   CA   sing N N 276 
LYS   N   H    sing N N 277 
LYS   N   H2   sing N N 278 
LYS   CA  C    sing N N 279 
LYS   CA  CB   sing N N 280 
LYS   CA  HA   sing N N 281 
LYS   C   O    doub N N 282 
LYS   C   OXT  sing N N 283 
LYS   CB  CG   sing N N 284 
LYS   CB  HB2  sing N N 285 
LYS   CB  HB3  sing N N 286 
LYS   CG  CD   sing N N 287 
LYS   CG  HG2  sing N N 288 
LYS   CG  HG3  sing N N 289 
LYS   CD  CE   sing N N 290 
LYS   CD  HD2  sing N N 291 
LYS   CD  HD3  sing N N 292 
LYS   CE  NZ   sing N N 293 
LYS   CE  HE2  sing N N 294 
LYS   CE  HE3  sing N N 295 
LYS   NZ  HZ1  sing N N 296 
LYS   NZ  HZ2  sing N N 297 
LYS   NZ  HZ3  sing N N 298 
LYS   OXT HXT  sing N N 299 
MET   N   CA   sing N N 300 
MET   N   H    sing N N 301 
MET   N   H2   sing N N 302 
MET   CA  C    sing N N 303 
MET   CA  CB   sing N N 304 
MET   CA  HA   sing N N 305 
MET   C   O    doub N N 306 
MET   C   OXT  sing N N 307 
MET   CB  CG   sing N N 308 
MET   CB  HB2  sing N N 309 
MET   CB  HB3  sing N N 310 
MET   CG  SD   sing N N 311 
MET   CG  HG2  sing N N 312 
MET   CG  HG3  sing N N 313 
MET   SD  CE   sing N N 314 
MET   CE  HE1  sing N N 315 
MET   CE  HE2  sing N N 316 
MET   CE  HE3  sing N N 317 
MET   OXT HXT  sing N N 318 
PHE   N   CA   sing N N 319 
PHE   N   H    sing N N 320 
PHE   N   H2   sing N N 321 
PHE   CA  C    sing N N 322 
PHE   CA  CB   sing N N 323 
PHE   CA  HA   sing N N 324 
PHE   C   O    doub N N 325 
PHE   C   OXT  sing N N 326 
PHE   CB  CG   sing N N 327 
PHE   CB  HB2  sing N N 328 
PHE   CB  HB3  sing N N 329 
PHE   CG  CD1  doub Y N 330 
PHE   CG  CD2  sing Y N 331 
PHE   CD1 CE1  sing Y N 332 
PHE   CD1 HD1  sing N N 333 
PHE   CD2 CE2  doub Y N 334 
PHE   CD2 HD2  sing N N 335 
PHE   CE1 CZ   doub Y N 336 
PHE   CE1 HE1  sing N N 337 
PHE   CE2 CZ   sing Y N 338 
PHE   CE2 HE2  sing N N 339 
PHE   CZ  HZ   sing N N 340 
PHE   OXT HXT  sing N N 341 
PRO   N   CA   sing N N 342 
PRO   N   CD   sing N N 343 
PRO   N   H    sing N N 344 
PRO   CA  C    sing N N 345 
PRO   CA  CB   sing N N 346 
PRO   CA  HA   sing N N 347 
PRO   C   O    doub N N 348 
PRO   C   OXT  sing N N 349 
PRO   CB  CG   sing N N 350 
PRO   CB  HB2  sing N N 351 
PRO   CB  HB3  sing N N 352 
PRO   CG  CD   sing N N 353 
PRO   CG  HG2  sing N N 354 
PRO   CG  HG3  sing N N 355 
PRO   CD  HD2  sing N N 356 
PRO   CD  HD3  sing N N 357 
PRO   OXT HXT  sing N N 358 
SER   N   CA   sing N N 359 
SER   N   H    sing N N 360 
SER   N   H2   sing N N 361 
SER   CA  C    sing N N 362 
SER   CA  CB   sing N N 363 
SER   CA  HA   sing N N 364 
SER   C   O    doub N N 365 
SER   C   OXT  sing N N 366 
SER   CB  OG   sing N N 367 
SER   CB  HB2  sing N N 368 
SER   CB  HB3  sing N N 369 
SER   OG  HG   sing N N 370 
SER   OXT HXT  sing N N 371 
THR   N   CA   sing N N 372 
THR   N   H    sing N N 373 
THR   N   H2   sing N N 374 
THR   CA  C    sing N N 375 
THR   CA  CB   sing N N 376 
THR   CA  HA   sing N N 377 
THR   C   O    doub N N 378 
THR   C   OXT  sing N N 379 
THR   CB  OG1  sing N N 380 
THR   CB  CG2  sing N N 381 
THR   CB  HB   sing N N 382 
THR   OG1 HG1  sing N N 383 
THR   CG2 HG21 sing N N 384 
THR   CG2 HG22 sing N N 385 
THR   CG2 HG23 sing N N 386 
THR   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HDH 
_atom_sites.fract_transf_matrix[1][1]   0.011255 
_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]   0.011255 
_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]   0.025324 
_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   ? 19.770 -16.166 22.245  0.66 61.46 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.677 -16.103 22.400  0.34 60.85 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.781 -15.108 22.412  0.66 61.13 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.702 -15.032 22.561  0.34 60.56 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.413 -13.747 22.134  0.66 59.63 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.341 -13.685 22.248  0.34 59.29 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.513 -13.456 22.604  0.66 60.10 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.389 -13.346 22.798  0.34 59.70 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.139 -15.157 23.813  0.66 61.98 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.093 -15.036 23.976  0.34 61.26 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.094 -14.062 23.959  0.66 62.19 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.076 -13.913 24.120  0.34 61.43 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.520 -16.525 24.066  0.66 62.23 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.456 -16.384 24.278  0.34 61.47 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.073 -15.238 21.765  0.66 73.33 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.980 -15.169 21.932  0.34 72.65 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.825 -15.011 24.483  0.66 74.35 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.798 -14.887 24.625  0.34 73.49 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.591 -14.213 24.775  0.66 74.60 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.570 -14.050 24.936  0.34 73.69 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.540 -13.202 24.001  0.66 74.60 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.543 -13.064 24.160  0.34 73.69 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.498 -14.091 23.194  0.66 74.60 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.479 -13.928 23.356  0.34 73.69 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.060 -16.509 24.920  0.66 74.65 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.019 -16.339 25.143  0.34 73.74 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.891 -16.722 23.355  0.66 74.65 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.805 -16.586 23.588  0.34 73.74 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.222 -17.194 24.081  0.66 74.65 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.146 -17.065 24.291  0.34 73.74 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.709 -12.920 21.363  1.00 57.28 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.154 -11.571 21.027  1.00 52.55 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.031 -10.576 21.316  1.00 48.04 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.920 -10.952 21.702  1.00 48.14 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.678 -11.481 19.587  1.00 51.96 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.647 -11.887 18.559  1.00 51.26 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.503 -11.435 18.593  1.00 50.99 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.051 -12.747 17.630  1.00 51.18 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.948 -13.127 21.018  0.66 68.72 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 18.004 -13.169 20.935  0.34 68.72 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.892 -11.342 21.604  1.00 63.04 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.942 -10.564 19.403  1.00 62.33 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.444 -12.069 19.490  1.00 62.33 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.507 -13.008 17.019  1.00 61.39 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.860 -13.043 17.640  1.00 61.39 ?  4   ASN   A HD22 1 
ATOM   46   N N    A SER   A 1 5   ? 18.328 -9.290  21.128  0.66 45.51 ?  5   SER   A N    1 
ATOM   47   N N    B SER   A 1 5   ? 18.334 -9.293  21.116  0.34 45.60 ?  5   SER   A N    1 
ATOM   48   C CA   A SER   A 1 5   ? 17.421 -8.214  21.507  0.66 42.83 ?  5   SER   A CA   1 
ATOM   49   C CA   B SER   A 1 5   ? 17.445 -8.204  21.495  0.34 42.96 ?  5   SER   A CA   1 
ATOM   50   C C    A SER   A 1 5   ? 16.560 -7.718  20.350  0.66 39.49 ?  5   SER   A C    1 
ATOM   51   C C    B SER   A 1 5   ? 16.578 -7.709  20.343  0.34 39.66 ?  5   SER   A C    1 
ATOM   52   O O    A SER   A 1 5   ? 15.929 -6.663  20.473  0.66 39.23 ?  5   SER   A O    1 
ATOM   53   O O    B SER   A 1 5   ? 15.958 -6.648  20.464  0.34 39.62 ?  5   SER   A O    1 
ATOM   54   C CB   A SER   A 1 5   ? 18.202 -7.046  22.113  0.66 43.58 ?  5   SER   A CB   1 
ATOM   55   C CB   B SER   A 1 5   ? 18.252 -7.041  22.080  0.34 43.56 ?  5   SER   A CB   1 
ATOM   56   O OG   A SER   A 1 5   ? 19.150 -6.530  21.194  0.66 43.96 ?  5   SER   A OG   1 
ATOM   57   O OG   B SER   A 1 5   ? 19.173 -6.528  21.132  0.34 43.86 ?  5   SER   A OG   1 
ATOM   58   H H    A SER   A 1 5   ? 19.061 -9.017  20.774  0.66 54.59 ?  5   SER   A H    1 
ATOM   59   H H    B SER   A 1 5   ? 19.063 -9.028  20.748  0.34 54.69 ?  5   SER   A H    1 
ATOM   60   H HA   A SER   A 1 5   ? 16.828 -8.548  22.197  0.66 51.38 ?  5   SER   A HA   1 
ATOM   61   H HA   B SER   A 1 5   ? 16.854 -8.521  22.194  0.34 51.53 ?  5   SER   A HA   1 
ATOM   62   H HB2  A SER   A 1 5   ? 17.578 -6.341  22.352  0.66 52.27 ?  5   SER   A HB2  1 
ATOM   63   H HB2  B SER   A 1 5   ? 17.640 -6.333  22.341  0.34 52.25 ?  5   SER   A HB2  1 
ATOM   64   H HB3  A SER   A 1 5   ? 18.667 -7.355  22.906  0.66 52.27 ?  5   SER   A HB3  1 
ATOM   65   H HB3  B SER   A 1 5   ? 18.742 -7.356  22.855  0.34 52.25 ?  5   SER   A HB3  1 
ATOM   66   H HG   A SER   A 1 5   ? 19.567 -5.889  21.544  0.66 52.73 ?  5   SER   A HG   1 
ATOM   67   H HG   B SER   A 1 5   ? 19.605 -5.889  21.468  0.34 52.61 ?  5   SER   A HG   1 
ATOM   68   N N    . PHE   A 1 6   ? 16.520 -8.441  19.234  1.00 36.26 ?  6   PHE   A N    1 
ATOM   69   C CA   . PHE   A 1 6   ? 15.629 -8.074  18.140  1.00 30.00 ?  6   PHE   A CA   1 
ATOM   70   C C    . PHE   A 1 6   ? 14.198 -8.431  18.523  1.00 29.37 ?  6   PHE   A C    1 
ATOM   71   O O    . PHE   A 1 6   ? 13.941 -9.529  19.022  1.00 30.13 ?  6   PHE   A O    1 
ATOM   72   C CB   . PHE   A 1 6   ? 16.024 -8.802  16.857  1.00 26.00 ?  6   PHE   A CB   1 
ATOM   73   C CG   . PHE   A 1 6   ? 17.302 -8.296  16.241  1.00 23.02 ?  6   PHE   A CG   1 
ATOM   74   C CD1  . PHE   A 1 6   ? 17.322 -7.111  15.522  1.00 21.78 ?  6   PHE   A CD1  1 
ATOM   75   C CD2  . PHE   A 1 6   ? 18.480 -9.011  16.376  1.00 22.87 ?  6   PHE   A CD2  1 
ATOM   76   C CE1  . PHE   A 1 6   ? 18.495 -6.647  14.954  1.00 21.30 ?  6   PHE   A CE1  1 
ATOM   77   C CE2  . PHE   A 1 6   ? 19.653 -8.555  15.810  1.00 22.57 ?  6   PHE   A CE2  1 
ATOM   78   C CZ   . PHE   A 1 6   ? 19.661 -7.370  15.097  1.00 21.75 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 16.998 -9.141  19.084  0.66 43.48 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 16.984 -9.152  19.091  0.34 43.48 ?  6   PHE   A H    1 
ATOM   81   H HA   . PHE   A 1 6   ? 15.673 -7.123  17.990  1.00 35.98 ?  6   PHE   A HA   1 
ATOM   82   H HB2  . PHE   A 1 6   ? 16.139 -9.746  17.058  1.00 31.18 ?  6   PHE   A HB2  1 
ATOM   83   H HB3  . PHE   A 1 6   ? 15.313 -8.692  16.207  1.00 31.18 ?  6   PHE   A HB3  1 
ATOM   84   H HD1  . PHE   A 1 6   ? 16.537 -6.621  15.425  1.00 26.11 ?  6   PHE   A HD1  1 
ATOM   85   H HD2  . PHE   A 1 6   ? 18.477 -9.809  16.857  1.00 27.42 ?  6   PHE   A HD2  1 
ATOM   86   H HE1  . PHE   A 1 6   ? 18.498 -5.848  14.475  1.00 25.54 ?  6   PHE   A HE1  1 
ATOM   87   H HE2  . PHE   A 1 6   ? 20.440 -9.042  15.910  1.00 27.06 ?  6   PHE   A HE2  1 
ATOM   88   H HZ   . PHE   A 1 6   ? 20.452 -7.058  14.717  1.00 26.08 ?  6   PHE   A HZ   1 
ATOM   89   N N    . SER   A 1 7   ? 13.264 -7.509  18.286  1.00 28.28 ?  7   SER   A N    1 
ATOM   90   C CA   . SER   A 1 7   ? 11.897 -7.641  18.778  1.00 28.43 ?  7   SER   A CA   1 
ATOM   91   C C    . SER   A 1 7   ? 10.893 -7.391  17.661  1.00 26.00 ?  7   SER   A C    1 
ATOM   92   O O    . SER   A 1 7   ? 11.085 -6.504  16.826  1.00 25.74 ?  7   SER   A O    1 
ATOM   93   C CB   . SER   A 1 7   ? 11.643 -6.646  19.918  1.00 30.50 ?  7   SER   A CB   1 
ATOM   94   O OG   . SER   A 1 7   ? 10.312 -6.740  20.389  1.00 32.11 ?  7   SER   A OG   1 
ATOM   95   H H    . SER   A 1 7   ? 13.400 -6.793  17.831  1.00 33.91 ?  7   SER   A H    1 
ATOM   96   H HA   . SER   A 1 7   ? 11.757 -8.538  19.120  1.00 34.09 ?  7   SER   A HA   1 
ATOM   97   H HB2  . SER   A 1 7   ? 12.248 -6.844  20.651  1.00 36.58 ?  7   SER   A HB2  1 
ATOM   98   H HB3  . SER   A 1 7   ? 11.801 -5.746  19.593  1.00 36.58 ?  7   SER   A HB3  1 
ATOM   99   H HG   . SER   A 1 7   ? 10.186 -6.187  21.010  1.00 38.51 ?  7   SER   A HG   1 
ATOM   100  N N    . GLY   A 1 8   ? 9.815  -8.174  17.656  1.00 24.60 ?  8   GLY   A N    1 
ATOM   101  C CA   . GLY   A 1 8   ? 8.731  -7.937  16.727  1.00 23.29 ?  8   GLY   A CA   1 
ATOM   102  C C    . GLY   A 1 8   ? 8.935  -8.460  15.328  1.00 21.86 ?  8   GLY   A C    1 
ATOM   103  O O    . GLY   A 1 8   ? 8.198  -8.056  14.422  1.00 22.64 ?  8   GLY   A O    1 
ATOM   104  H H    . GLY   A 1 8   ? 9.696  -8.844  18.178  1.00 29.50 ?  8   GLY   A H    1 
ATOM   105  H HA2  . GLY   A 1 8   ? 7.927  -8.347  17.076  1.00 27.92 ?  8   GLY   A HA2  1 
ATOM   106  H HA3  . GLY   A 1 8   ? 8.579  -6.983  16.659  1.00 27.92 ?  8   GLY   A HA3  1 
ATOM   107  N N    . TYR   A 1 9   ? 9.911  -9.340  15.112  1.00 20.17 ?  9   TYR   A N    1 
ATOM   108  C CA   . TYR   A 1 9   ? 10.165 -9.876  13.784  1.00 18.66 ?  9   TYR   A CA   1 
ATOM   109  C C    . TYR   A 1 9   ? 9.285  -11.090 13.507  1.00 18.03 ?  9   TYR   A C    1 
ATOM   110  O O    . TYR   A 1 9   ? 8.964  -11.879 14.403  1.00 20.23 ?  9   TYR   A O    1 
ATOM   111  C CB   . TYR   A 1 9   ? 11.641 -10.265 13.620  1.00 18.33 ?  9   TYR   A CB   1 
ATOM   112  C CG   . TYR   A 1 9   ? 12.559 -9.070  13.451  1.00 17.95 ?  9   TYR   A CG   1 
ATOM   113  C CD1  . TYR   A 1 9   ? 12.863 -8.253  14.528  1.00 18.52 ?  9   TYR   A CD1  1 
ATOM   114  C CD2  . TYR   A 1 9   ? 13.086 -8.743  12.211  1.00 17.10 ?  9   TYR   A CD2  1 
ATOM   115  C CE1  . TYR   A 1 9   ? 13.674 -7.145  14.381  1.00 18.93 ?  9   TYR   A CE1  1 
ATOM   116  C CE2  . TYR   A 1 9   ? 13.902 -7.637  12.050  1.00 17.18 ?  9   TYR   A CE2  1 
ATOM   117  C CZ   . TYR   A 1 9   ? 14.184 -6.840  13.137  1.00 18.40 ?  9   TYR   A CZ   1 
ATOM   118  O OH   . TYR   A 1 9   ? 14.987 -5.739  12.975  1.00 19.56 ?  9   TYR   A OH   1 
ATOM   119  H H    . TYR   A 1 9   ? 10.439 -9.652  15.723  1.00 24.18 ?  9   TYR   A H    1 
ATOM   120  H HA   . TYR   A 1 9   ? 9.959  -9.194  13.129  1.00 22.37 ?  9   TYR   A HA   1 
ATOM   121  H HB2  . TYR   A 1 9   ? 11.928 -10.761 14.402  1.00 21.98 ?  9   TYR   A HB2  1 
ATOM   122  H HB3  . TYR   A 1 9   ? 11.721 -10.819 12.828  1.00 21.98 ?  9   TYR   A HB3  1 
ATOM   123  H HD1  . TYR   A 1 9   ? 12.499 -8.455  15.367  1.00 22.20 ?  9   TYR   A HD1  1 
ATOM   124  H HD2  . TYR   A 1 9   ? 12.891 -9.276  11.477  1.00 20.50 ?  9   TYR   A HD2  1 
ATOM   125  H HE1  . TYR   A 1 9   ? 13.866 -6.610  15.116  1.00 22.69 ?  9   TYR   A HE1  1 
ATOM   126  H HE2  . TYR   A 1 9   ? 14.259 -7.432  11.217  1.00 20.59 ?  9   TYR   A HE2  1 
ATOM   127  H HH   . TYR   A 1 9   ? 15.097 -5.358  13.718  1.00 23.45 ?  9   TYR   A HH   1 
ATOM   128  N N    . LEU   A 1 10  ? 8.901  -11.230 12.243  1.00 17.45 ?  10  LEU   A N    1 
ATOM   129  C CA   . LEU   A 1 10  ? 8.270  -12.443 11.744  1.00 17.08 ?  10  LEU   A CA   1 
ATOM   130  C C    . LEU   A 1 10  ? 9.381  -13.386 11.291  1.00 16.20 ?  10  LEU   A C    1 
ATOM   131  O O    . LEU   A 1 10  ? 10.331 -12.963 10.622  1.00 15.53 ?  10  LEU   A O    1 
ATOM   132  C CB   . LEU   A 1 10  ? 7.357  -12.104 10.565  1.00 18.32 ?  10  LEU   A CB   1 
ATOM   133  C CG   . LEU   A 1 10  ? 6.663  -13.285 9.880   1.00 20.22 ?  10  LEU   A CG   1 
ATOM   134  C CD1  . LEU   A 1 10  ? 5.610  -13.900 10.785  1.00 21.57 ?  10  LEU   A CD1  1 
ATOM   135  C CD2  . LEU   A 1 10  ? 6.066  -12.867 8.546   1.00 22.21 ?  10  LEU   A CD2  1 
ATOM   136  H H    . LEU   A 1 10  ? 9.005  -10.621 11.636  1.00 20.91 ?  10  LEU   A H    1 
ATOM   137  H HA   . LEU   A 1 10  ? 7.747  -12.862 12.449  1.00 20.47 ?  10  LEU   A HA   1 
ATOM   138  H HB2  . LEU   A 1 10  ? 6.659  -11.506 10.881  1.00 21.96 ?  10  LEU   A HB2  1 
ATOM   139  H HB3  . LEU   A 1 10  ? 7.887  -11.650 9.893   1.00 21.96 ?  10  LEU   A HB3  1 
ATOM   140  H HG   . LEU   A 1 10  ? 7.328  -13.970 9.700   1.00 24.24 ?  10  LEU   A HG   1 
ATOM   141  H HD11 . LEU   A 1 10  ? 5.229  -14.676 10.344  1.00 25.86 ?  10  LEU   A HD11 1 
ATOM   142  H HD12 . LEU   A 1 10  ? 6.023  -14.166 11.623  1.00 25.86 ?  10  LEU   A HD12 1 
ATOM   143  H HD13 . LEU   A 1 10  ? 4.917  -13.244 10.955  1.00 25.86 ?  10  LEU   A HD13 1 
ATOM   144  H HD21 . LEU   A 1 10  ? 5.638  -13.639 8.142   1.00 26.62 ?  10  LEU   A HD21 1 
ATOM   145  H HD22 . LEU   A 1 10  ? 5.416  -12.168 8.700   1.00 26.62 ?  10  LEU   A HD22 1 
ATOM   146  H HD23 . LEU   A 1 10  ? 6.777  -12.544 7.972   1.00 26.62 ?  10  LEU   A HD23 1 
ATOM   147  N N    . LYS   A 1 11  ? 9.271  -14.655 11.664  1.00 16.40 ?  11  LYS   A N    1 
ATOM   148  C CA   . LYS   A 1 11  ? 10.263 -15.656 11.304  1.00 16.05 ?  11  LYS   A CA   1 
ATOM   149  C C    . LYS   A 1 11  ? 9.898  -16.211 9.936   1.00 16.08 ?  11  LYS   A C    1 
ATOM   150  O O    . LYS   A 1 11  ? 8.795  -16.737 9.756   1.00 18.28 ?  11  LYS   A O    1 
ATOM   151  C CB   . LYS   A 1 11  ? 10.273 -16.762 12.359  1.00 15.60 ?  11  LYS   A CB   1 
ATOM   152  C CG   . LYS   A 1 11  ? 11.313 -17.855 12.165  1.00 15.47 ?  11  LYS   A CG   1 
ATOM   153  C CD   . LYS   A 1 11  ? 11.381 -18.750 13.404  1.00 15.95 ?  11  LYS   A CD   1 
ATOM   154  C CE   . LYS   A 1 11  ? 12.395 -19.887 13.258  1.00 15.91 ?  11  LYS   A CE   1 
ATOM   155  N NZ   . LYS   A 1 11  ? 13.777 -19.383 13.032  1.00 16.09 ?  11  LYS   A NZ   1 
ATOM   156  H H    . LYS   A 1 11  ? 8.600  -14.969 12.115  1.00 19.66 ?  11  LYS   A H    1 
ATOM   157  H HA   . LYS   A 1 11  ? 11.133 -15.244 11.257  1.00 19.24 ?  11  LYS   A HA   1 
ATOM   158  H HB2  . LYS   A 1 11  ? 10.433 -16.352 13.221  1.00 18.70 ?  11  LYS   A HB2  1 
ATOM   159  H HB3  . LYS   A 1 11  ? 9.399  -17.187 12.361  1.00 18.70 ?  11  LYS   A HB3  1 
ATOM   160  H HG2  . LYS   A 1 11  ? 11.071 -18.401 11.400  1.00 18.54 ?  11  LYS   A HG2  1 
ATOM   161  H HG3  . LYS   A 1 11  ? 12.184 -17.448 12.029  1.00 18.54 ?  11  LYS   A HG3  1 
ATOM   162  H HD2  . LYS   A 1 11  ? 11.636 -18.212 14.169  1.00 19.12 ?  11  LYS   A HD2  1 
ATOM   163  H HD3  . LYS   A 1 11  ? 10.505 -19.145 13.555  1.00 19.12 ?  11  LYS   A HD3  1 
ATOM   164  H HE2  . LYS   A 1 11  ? 12.397 -20.416 14.070  1.00 19.07 ?  11  LYS   A HE2  1 
ATOM   165  H HE3  . LYS   A 1 11  ? 12.147 -20.437 12.500  1.00 19.07 ?  11  LYS   A HE3  1 
ATOM   166  H HZ1  . LYS   A 1 11  ? 14.320 -20.063 12.850  1.00 19.28 ?  11  LYS   A HZ1  1 
ATOM   167  H HZ2  . LYS   A 1 11  ? 13.785 -18.815 12.347  1.00 19.28 ?  11  LYS   A HZ2  1 
ATOM   168  H HZ3  . LYS   A 1 11  ? 14.071 -18.964 13.759  1.00 19.28 ?  11  LYS   A HZ3  1 
ATOM   169  N N    . LEU   A 1 12  ? 10.810 -16.092 8.971   1.00 15.35 ?  12  LEU   A N    1 
ATOM   170  C CA   . LEU   A 1 12  ? 10.555 -16.644 7.645   1.00 15.91 ?  12  LEU   A CA   1 
ATOM   171  C C    . LEU   A 1 12  ? 11.137 -18.042 7.484   1.00 15.39 ?  12  LEU   A C    1 
ATOM   172  O O    . LEU   A 1 12  ? 10.507 -18.911 6.870   1.00 15.79 ?  12  LEU   A O    1 
ATOM   173  C CB   . LEU   A 1 12  ? 11.121 -15.733 6.553   1.00 16.98 ?  12  LEU   A CB   1 
ATOM   174  C CG   . LEU   A 1 12  ? 10.448 -14.377 6.349   1.00 18.51 ?  12  LEU   A CG   1 
ATOM   175  C CD1  . LEU   A 1 12  ? 11.167 -13.595 5.260   1.00 19.31 ?  12  LEU   A CD1  1 
ATOM   176  C CD2  . LEU   A 1 12  ? 8.974  -14.550 6.008   1.00 19.79 ?  12  LEU   A CD2  1 
ATOM   177  H H    . LEU   A 1 12  ? 11.582 -15.704 9.057   1.00 18.40 ?  12  LEU   A H    1 
ATOM   178  H HA   . LEU   A 1 12  ? 9.601  -16.709 7.514   1.00 19.07 ?  12  LEU   A HA   1 
ATOM   179  H HB2  . LEU   A 1 12  ? 12.051 -15.557 6.760   1.00 20.35 ?  12  LEU   A HB2  1 
ATOM   180  H HB3  . LEU   A 1 12  ? 11.066 -16.208 5.710   1.00 20.35 ?  12  LEU   A HB3  1 
ATOM   181  H HG   . LEU   A 1 12  ? 10.506 -13.868 7.169   1.00 22.19 ?  12  LEU   A HG   1 
ATOM   182  H HD11 . LEU   A 1 12  ? 10.718 -12.749 5.124   1.00 23.15 ?  12  LEU   A HD11 1 
ATOM   183  H HD12 . LEU   A 1 12  ? 12.087 -13.441 5.539   1.00 23.15 ?  12  LEU   A HD12 1 
ATOM   184  H HD13 . LEU   A 1 12  ? 11.158 -14.112 4.438   1.00 23.15 ?  12  LEU   A HD13 1 
ATOM   185  H HD21 . LEU   A 1 12  ? 8.611  -13.695 5.731   1.00 23.73 ?  12  LEU   A HD21 1 
ATOM   186  H HD22 . LEU   A 1 12  ? 8.889  -15.194 5.286   1.00 23.73 ?  12  LEU   A HD22 1 
ATOM   187  H HD23 . LEU   A 1 12  ? 8.503  -14.872 6.792   1.00 23.73 ?  12  LEU   A HD23 1 
ATOM   188  N N    . THR   A 1 13  ? 12.348 -18.258 7.990   1.00 15.01 ?  13  THR   A N    1 
ATOM   189  C CA   . THR   A 1 13  ? 13.035 -19.539 7.895   1.00 15.04 ?  13  THR   A CA   1 
ATOM   190  C C    . THR   A 1 13  ? 13.803 -19.765 9.188   1.00 15.21 ?  13  THR   A C    1 
ATOM   191  O O    . THR   A 1 13  ? 13.706 -18.989 10.143  1.00 15.27 ?  13  THR   A O    1 
ATOM   192  C CB   . THR   A 1 13  ? 14.011 -19.587 6.713   1.00 15.88 ?  13  THR   A CB   1 
ATOM   193  O OG1  . THR   A 1 13  ? 15.067 -18.658 6.952   1.00 15.92 ?  13  THR   A OG1  1 
ATOM   194  C CG2  . THR   A 1 13  ? 13.328 -19.259 5.390   1.00 16.99 ?  13  THR   A CG2  1 
ATOM   195  H H    . THR   A 1 13  ? 12.816 -17.655 8.388   1.00 17.99 ?  13  THR   A H    1 
ATOM   196  H HA   . THR   A 1 13  ? 12.387 -20.253 7.788   1.00 18.03 ?  13  THR   A HA   1 
ATOM   197  H HB   . THR   A 1 13  ? 14.387 -20.481 6.640   1.00 19.03 ?  13  THR   A HB   1 
ATOM   198  H HG1  . THR   A 1 13  ? 15.736 -19.054 7.272   1.00 19.08 ?  13  THR   A HG1  1 
ATOM   199  H HG21 . THR   A 1 13  ? 13.954 -19.376 4.655   1.00 20.37 ?  13  THR   A HG21 1 
ATOM   200  H HG22 . THR   A 1 13  ? 12.573 -19.854 5.252   1.00 20.37 ?  13  THR   A HG22 1 
ATOM   201  H HG23 . THR   A 1 13  ? 13.015 -18.345 5.395   1.00 20.37 ?  13  THR   A HG23 1 
ATOM   202  N N    . ASP   A 1 14  ? 14.600 -20.833 9.202   1.00 15.52 ?  14  ASP   A N    1 
ATOM   203  C CA   . ASP   A 1 14  ? 15.443 -21.115 10.351  1.00 16.29 ?  14  ASP   A CA   1 
ATOM   204  C C    . ASP   A 1 14  ? 16.286 -19.905 10.748  1.00 15.61 ?  14  ASP   A C    1 
ATOM   205  O O    . ASP   A 1 14  ? 16.519 -19.672 11.938  1.00 16.76 ?  14  ASP   A O    1 
ATOM   206  C CB   . ASP   A 1 14  ? 16.355 -22.296 10.033  1.00 19.02 ?  14  ASP   A CB   1 
ATOM   207  C CG   . ASP   A 1 14  ? 17.279 -22.617 11.170  1.00 22.57 ?  14  ASP   A CG   1 
ATOM   208  O OD1  . ASP   A 1 14  ? 16.778 -22.984 12.256  1.00 24.13 ?  14  ASP   A OD1  1 
ATOM   209  O OD2  . ASP   A 1 14  ? 18.503 -22.490 10.981  1.00 25.32 -1 14  ASP   A OD2  1 
ATOM   210  H H    . ASP   A 1 14  ? 14.675 -21.394 8.560   1.00 18.60 ?  14  ASP   A H    1 
ATOM   211  H HA   . ASP   A 1 14  ? 14.886 -21.359 11.108  1.00 19.52 ?  14  ASP   A HA   1 
ATOM   212  H HB2  . ASP   A 1 14  ? 15.802 -23.083 9.853   1.00 22.81 ?  14  ASP   A HB2  1 
ATOM   213  H HB3  . ASP   A 1 14  ? 16.886 -22.089 9.249   1.00 22.81 ?  14  ASP   A HB3  1 
ATOM   214  N N    . ASN   A 1 15  ? 16.749 -19.114 9.769   1.00 14.49 ?  15  ASN   A N    1 
ATOM   215  C CA   . ASN   A 1 15  ? 17.743 -18.078 10.036  1.00 15.10 ?  15  ASN   A CA   1 
ATOM   216  C C    . ASN   A 1 15  ? 17.379 -16.688 9.531   1.00 15.37 ?  15  ASN   A C    1 
ATOM   217  O O    . ASN   A 1 15  ? 18.161 -15.759 9.754   1.00 16.65 ?  15  ASN   A O    1 
ATOM   218  C CB   . ASN   A 1 15  ? 19.113 -18.481 9.459   1.00 14.59 ?  15  ASN   A CB   1 
ATOM   219  C CG   . ASN   A 1 15  ? 19.105 -18.566 7.950   1.00 15.12 ?  15  ASN   A CG   1 
ATOM   220  O OD1  . ASN   A 1 15  ? 18.395 -19.392 7.366   1.00 16.12 ?  15  ASN   A OD1  1 
ATOM   221  N ND2  . ASN   A 1 15  ? 19.893 -17.705 7.305   1.00 14.91 ?  15  ASN   A ND2  1 
ATOM   222  H H    . ASN   A 1 15  ? 16.491 -19.154 8.958   1.00 17.36 ?  15  ASN   A H    1 
ATOM   223  H HA   . ASN   A 1 15  ? 17.858 -18.010 10.998  1.00 18.10 ?  15  ASN   A HA   1 
ATOM   224  H HB2  . ASN   A 1 15  ? 19.780 -17.819 9.727   1.00 17.48 ?  15  ASN   A HB2  1 
ATOM   225  H HB3  . ASN   A 1 15  ? 19.370 -19.353 9.810   1.00 17.48 ?  15  ASN   A HB3  1 
ATOM   226  H HD21 . ASN   A 1 15  ? 19.927 -17.709 6.445   1.00 17.87 ?  15  ASN   A HD21 1 
ATOM   227  H HD22 . ASN   A 1 15  ? 20.377 -17.135 7.744   1.00 17.87 ?  15  ASN   A HD22 1 
ATOM   228  N N    . VAL   A 1 16  ? 16.234 -16.505 8.877   1.00 15.14 ?  16  VAL   A N    1 
ATOM   229  C CA   . VAL   A 1 16  ? 15.847 -15.221 8.304   1.00 14.68 ?  16  VAL   A CA   1 
ATOM   230  C C    . VAL   A 1 16  ? 14.570 -14.732 8.977   1.00 14.48 ?  16  VAL   A C    1 
ATOM   231  O O    . VAL   A 1 16  ? 13.574 -15.465 9.059   1.00 14.44 ?  16  VAL   A O    1 
ATOM   232  C CB   . VAL   A 1 16  ? 15.668 -15.300 6.778   1.00 15.18 ?  16  VAL   A CB   1 
ATOM   233  C CG1  . VAL   A 1 16  ? 15.229 -13.943 6.214   1.00 15.91 ?  16  VAL   A CG1  1 
ATOM   234  C CG2  . VAL   A 1 16  ? 16.952 -15.773 6.108   1.00 16.04 ?  16  VAL   A CG2  1 
ATOM   235  H H    . VAL   A 1 16  ? 15.651 -17.127 8.765   1.00 18.15 ?  16  VAL   A H    1 
ATOM   236  H HA   . VAL   A 1 16  ? 16.549 -14.575 8.488   1.00 17.60 ?  16  VAL   A HA   1 
ATOM   237  H HB   . VAL   A 1 16  ? 14.977 -15.947 6.581   1.00 18.19 ?  16  VAL   A HB   1 
ATOM   238  H HG11 . VAL   A 1 16  ? 15.311 -13.968 5.249   1.00 19.07 ?  16  VAL   A HG11 1 
ATOM   239  H HG12 . VAL   A 1 16  ? 14.304 -13.784 6.463   1.00 19.07 ?  16  VAL   A HG12 1 
ATOM   240  H HG13 . VAL   A 1 16  ? 15.797 -13.250 6.579   1.00 19.07 ?  16  VAL   A HG13 1 
ATOM   241  H HG21 . VAL   A 1 16  ? 16.838 -15.739 5.146   1.00 19.22 ?  16  VAL   A HG21 1 
ATOM   242  H HG22 . VAL   A 1 16  ? 17.685 -15.192 6.373   1.00 19.22 ?  16  VAL   A HG22 1 
ATOM   243  H HG23 . VAL   A 1 16  ? 17.141 -16.683 6.387   1.00 19.22 ?  16  VAL   A HG23 1 
ATOM   244  N N    . TYR   A 1 17  ? 14.601 -13.469 9.408   1.00 14.36 ?  17  TYR   A N    1 
ATOM   245  C CA   . TYR   A 1 17  ? 13.520 -12.786 10.107  1.00 14.11 ?  17  TYR   A CA   1 
ATOM   246  C C    . TYR   A 1 17  ? 13.259 -11.452 9.419   1.00 14.47 ?  17  TYR   A C    1 
ATOM   247  O O    . TYR   A 1 17  ? 14.161 -10.900 8.787   1.00 14.90 ?  17  TYR   A O    1 
ATOM   248  C CB   . TYR   A 1 17  ? 13.935 -12.528 11.556  1.00 14.81 ?  17  TYR   A CB   1 
ATOM   249  C CG   . TYR   A 1 17  ? 14.139 -13.793 12.358  1.00 15.60 ?  17  TYR   A CG   1 
ATOM   250  C CD1  . TYR   A 1 17  ? 15.315 -14.535 12.261  1.00 16.56 ?  17  TYR   A CD1  1 
ATOM   251  C CD2  . TYR   A 1 17  ? 13.148 -14.255 13.211  1.00 16.32 ?  17  TYR   A CD2  1 
ATOM   252  C CE1  . TYR   A 1 17  ? 15.490 -15.709 12.990  1.00 17.28 ?  17  TYR   A CE1  1 
ATOM   253  C CE2  . TYR   A 1 17  ? 13.315 -15.426 13.944  1.00 17.22 ?  17  TYR   A CE2  1 
ATOM   254  C CZ   . TYR   A 1 17  ? 14.487 -16.145 13.834  1.00 17.06 ?  17  TYR   A CZ   1 
ATOM   255  O OH   . TYR   A 1 17  ? 14.652 -17.304 14.566  1.00 18.35 ?  17  TYR   A OH   1 
ATOM   256  H H    . TYR   A 1 17  ? 15.280 -12.952 9.278   1.00 17.21 ?  17  TYR   A H    1 
ATOM   257  H HA   . TYR   A 1 17  ? 12.711 -13.325 10.086  1.00 16.91 ?  17  TYR   A HA   1 
ATOM   258  H HB2  . TYR   A 1 17  ? 14.768 -12.035 11.553  1.00 17.75 ?  17  TYR   A HB2  1 
ATOM   259  H HB3  . TYR   A 1 17  ? 13.244 -12.008 11.985  1.00 17.75 ?  17  TYR   A HB3  1 
ATOM   260  H HD1  . TYR   A 1 17  ? 15.991 -14.247 11.688  1.00 19.85 ?  17  TYR   A HD1  1 
ATOM   261  H HD2  . TYR   A 1 17  ? 12.353 -13.778 13.290  1.00 19.56 ?  17  TYR   A HD2  1 
ATOM   262  H HE1  . TYR   A 1 17  ? 16.285 -16.193 12.916  1.00 20.71 ?  17  TYR   A HE1  1 
ATOM   263  H HE2  . TYR   A 1 17  ? 12.641 -15.716 14.516  1.00 20.64 ?  17  TYR   A HE2  1 
ATOM   264  H HH   . TYR   A 1 17  ? 13.928 -17.512 14.933  1.00 21.99 ?  17  TYR   A HH   1 
ATOM   265  N N    A ILE   A 1 18  ? 12.004 -10.990 9.426   0.66 14.39 ?  18  ILE   A N    1 
ATOM   266  N N    B ILE   A 1 18  ? 12.084 -10.864 9.680   0.34 13.47 ?  18  ILE   A N    1 
ATOM   267  C CA   A ILE   A 1 18  ? 11.618 -9.823  8.633   0.66 14.37 ?  18  ILE   A CA   1 
ATOM   268  C CA   B ILE   A 1 18  ? 11.700 -9.606  9.043   0.34 12.44 ?  18  ILE   A CA   1 
ATOM   269  C C    A ILE   A 1 18  ? 10.633 -8.957  9.409   0.66 14.68 ?  18  ILE   A C    1 
ATOM   270  C C    B ILE   A 1 18  ? 10.804 -8.777  9.962   0.34 12.39 ?  18  ILE   A C    1 
ATOM   271  O O    A ILE   A 1 18  ? 9.794  -9.463  10.160  0.66 15.01 ?  18  ILE   A O    1 
ATOM   272  O O    B ILE   A 1 18  ? 9.980  -9.314  10.710  0.34 12.81 ?  18  ILE   A O    1 
ATOM   273  C CB   A ILE   A 1 18  ? 11.078 -10.236 7.239   0.66 14.24 ?  18  ILE   A CB   1 
ATOM   274  C CB   B ILE   A 1 18  ? 11.029 -9.877  7.680   0.34 11.43 ?  18  ILE   A CB   1 
ATOM   275  C CG1  A ILE   A 1 18  ? 10.996 -9.030  6.304   0.66 14.22 ?  18  ILE   A CG1  1 
ATOM   276  C CG1  B ILE   A 1 18  ? 10.934 -8.590  6.869   0.34 12.41 ?  18  ILE   A CG1  1 
ATOM   277  C CG2  A ILE   A 1 18  ? 9.741  -10.963 7.363   0.66 14.52 ?  18  ILE   A CG2  1 
ATOM   278  C CG2  B ILE   A 1 18  ? 9.660  -10.517 7.876   0.34 11.34 ?  18  ILE   A CG2  1 
ATOM   279  C CD1  A ILE   A 1 18  ? 10.728 -9.400  4.867   0.66 15.42 ?  18  ILE   A CD1  1 
ATOM   280  C CD1  B ILE   A 1 18  ? 10.549 -8.826  5.432   0.34 13.24 ?  18  ILE   A CD1  1 
ATOM   281  H H    A ILE   A 1 18  ? 11.358 -11.350 9.868   0.66 17.24 ?  18  ILE   A H    1 
ATOM   282  H H    B ILE   A 1 18  ? 11.500 -11.176 10.231  0.34 16.14 ?  18  ILE   A H    1 
ATOM   283  H HA   A ILE   A 1 18  ? 12.411 -9.293  8.475   0.66 17.22 ?  18  ILE   A HA   1 
ATOM   284  H HA   B ILE   A 1 18  ? 12.508 -9.093  8.875   0.34 14.90 ?  18  ILE   A HA   1 
ATOM   285  H HB   A ILE   A 1 18  ? 11.709 -10.865 6.846   0.66 17.06 ?  18  ILE   A HB   1 
ATOM   286  H HB   B ILE   A 1 18  ? 11.589 -10.496 7.194   0.34 13.69 ?  18  ILE   A HB   1 
ATOM   287  H HG12 A ILE   A 1 18  ? 10.280 -8.451  6.597   0.66 17.05 ?  18  ILE   A HG12 1 
ATOM   288  H HG12 B ILE   A 1 18  ? 10.265 -8.011  7.268   0.34 14.87 ?  18  ILE   A HG12 1 
ATOM   289  H HG13 A ILE   A 1 18  ? 11.841 -8.556  6.329   0.66 17.05 ?  18  ILE   A HG13 1 
ATOM   290  H HG13 B ILE   A 1 18  ? 11.799 -8.146  6.877   0.34 14.87 ?  18  ILE   A HG13 1 
ATOM   291  H HG21 A ILE   A 1 18  ? 9.502  -11.344 6.499   0.66 17.40 ?  18  ILE   A HG21 1 
ATOM   292  H HG21 B ILE   A 1 18  ? 9.343  -10.846 7.020   0.34 13.59 ?  18  ILE   A HG21 1 
ATOM   293  H HG22 A ILE   A 1 18  ? 9.826  -11.673 8.019   0.66 17.40 ?  18  ILE   A HG22 1 
ATOM   294  H HG22 B ILE   A 1 18  ? 9.741  -11.251 8.503   0.34 13.59 ?  18  ILE   A HG22 1 
ATOM   295  H HG23 A ILE   A 1 18  ? 9.060  -10.333 7.642   0.66 17.40 ?  18  ILE   A HG23 1 
ATOM   296  H HG23 B ILE   A 1 18  ? 9.043  -9.853  8.223   0.34 13.59 ?  18  ILE   A HG23 1 
ATOM   297  H HD11 A ILE   A 1 18  ? 10.753 -8.593  4.324   0.66 18.49 ?  18  ILE   A HD11 1 
ATOM   298  H HD11 B ILE   A 1 18  ? 10.564 -7.980  4.958   0.34 15.86 ?  18  ILE   A HD11 1 
ATOM   299  H HD12 A ILE   A 1 18  ? 11.408 -10.021 4.565   0.66 18.49 ?  18  ILE   A HD12 1 
ATOM   300  H HD12 B ILE   A 1 18  ? 11.184 -9.441  5.033   0.34 15.86 ?  18  ILE   A HD12 1 
ATOM   301  H HD13 A ILE   A 1 18  ? 9.851  -9.810  4.803   0.66 18.49 ?  18  ILE   A HD13 1 
ATOM   302  H HD13 B ILE   A 1 18  ? 9.657  -9.206  5.404   0.34 15.86 ?  18  ILE   A HD13 1 
ATOM   303  N N    A LYS   A 1 19  ? 10.732 -7.639  9.209   0.66 14.45 ?  19  LYS   A N    1 
ATOM   304  N N    B LYS   A 1 19  ? 10.969 -7.447  9.887   0.34 12.89 ?  19  LYS   A N    1 
ATOM   305  C CA   A LYS   A 1 19  ? 9.927  -6.674  9.950   0.66 15.39 ?  19  LYS   A CA   1 
ATOM   306  C CA   B LYS   A 1 19  ? 10.186 -6.485  10.659  0.34 13.94 ?  19  LYS   A CA   1 
ATOM   307  C C    A LYS   A 1 19  ? 9.732  -5.418  9.111   0.66 15.63 ?  19  LYS   A C    1 
ATOM   308  C C    B LYS   A 1 19  ? 9.917  -5.264  9.791   0.34 14.62 ?  19  LYS   A C    1 
ATOM   309  O O    A LYS   A 1 19  ? 10.621 -5.025  8.350   0.66 15.37 ?  19  LYS   A O    1 
ATOM   310  O O    B LYS   A 1 19  ? 10.785 -4.840  9.025   0.34 14.39 ?  19  LYS   A O    1 
ATOM   311  C CB   A LYS   A 1 19  ? 10.635 -6.303  11.262  0.66 16.14 ?  19  LYS   A CB   1 
ATOM   312  C CB   B LYS   A 1 19  ? 10.936 -6.058  11.935  0.34 14.15 ?  19  LYS   A CB   1 
ATOM   313  C CG   A LYS   A 1 19  ? 9.883  -5.360  12.201  0.66 17.30 ?  19  LYS   A CG   1 
ATOM   314  C CG   B LYS   A 1 19  ? 10.202 -5.104  12.873  0.34 14.95 ?  19  LYS   A CG   1 
ATOM   315  C CD   A LYS   A 1 19  ? 10.744 -5.074  13.433  0.66 18.50 ?  19  LYS   A CD   1 
ATOM   316  C CD   B LYS   A 1 19  ? 11.104 -4.760  14.059  0.34 15.58 ?  19  LYS   A CD   1 
ATOM   317  C CE   A LYS   A 1 19  ? 10.078 -4.131  14.419  0.66 19.17 ?  19  LYS   A CE   1 
ATOM   318  C CE   B LYS   A 1 19  ? 10.418 -3.874  15.087  0.34 16.25 ?  19  LYS   A CE   1 
ATOM   319  N NZ   A LYS   A 1 19  ? 10.963 -3.844  15.588  0.66 19.75 ?  19  LYS   A NZ   1 
ATOM   320  N NZ   B LYS   A 1 19  ? 11.272 -3.693  16.300  0.34 16.70 ?  19  LYS   A NZ   1 
ATOM   321  H H    A LYS   A 1 19  ? 11.272 -7.286  8.641   0.66 17.32 ?  19  LYS   A H    1 
ATOM   322  H H    B LYS   A 1 19  ? 11.560 -7.059  9.384   0.34 15.44 ?  19  LYS   A H    1 
ATOM   323  H HA   A LYS   A 1 19  ? 9.060  -7.067  10.153  0.66 18.44 ?  19  LYS   A HA   1 
ATOM   324  H HA   B LYS   A 1 19  ? 9.341  -6.874  10.916  0.34 16.71 ?  19  LYS   A HA   1 
ATOM   325  H HB2  A LYS   A 1 19  ? 10.803 -7.123  11.756  0.66 19.35 ?  19  LYS   A HB2  1 
ATOM   326  H HB2  B LYS   A 1 19  ? 11.136 -6.850  12.454  0.34 16.96 ?  19  LYS   A HB2  1 
ATOM   327  H HB3  A LYS   A 1 19  ? 11.475 -5.883  11.041  0.66 19.35 ?  19  LYS   A HB3  1 
ATOM   328  H HB3  B LYS   A 1 19  ? 11.763 -5.619  11.682  0.34 16.96 ?  19  LYS   A HB3  1 
ATOM   329  H HG2  A LYS   A 1 19  ? 9.702  -4.522  11.748  0.66 20.73 ?  19  LYS   A HG2  1 
ATOM   330  H HG2  B LYS   A 1 19  ? 9.983  -4.282  12.408  0.34 17.91 ?  19  LYS   A HG2  1 
ATOM   331  H HG3  A LYS   A 1 19  ? 9.054  -5.776  12.493  0.66 20.73 ?  19  LYS   A HG3  1 
ATOM   332  H HG3  B LYS   A 1 19  ? 9.399  -5.528  13.215  0.34 17.91 ?  19  LYS   A HG3  1 
ATOM   333  H HD2  A LYS   A 1 19  ? 10.924 -5.909  13.894  0.66 22.18 ?  19  LYS   A HD2  1 
ATOM   334  H HD2  B LYS   A 1 19  ? 11.371 -5.579  14.505  0.34 18.68 ?  19  LYS   A HD2  1 
ATOM   335  H HD3  A LYS   A 1 19  ? 11.578 -4.668  13.147  0.66 22.18 ?  19  LYS   A HD3  1 
ATOM   336  H HD3  B LYS   A 1 19  ? 11.888 -4.292  13.733  0.34 18.68 ?  19  LYS   A HD3  1 
ATOM   337  H HE2  A LYS   A 1 19  ? 9.882  -3.289  13.977  0.66 22.98 ?  19  LYS   A HE2  1 
ATOM   338  H HE2  B LYS   A 1 19  ? 10.253 -3.000  14.701  0.34 19.47 ?  19  LYS   A HE2  1 
ATOM   339  H HE3  A LYS   A 1 19  ? 9.262  -4.534  14.750  0.66 22.98 ?  19  LYS   A HE3  1 
ATOM   340  H HE3  B LYS   A 1 19  ? 9.584  -4.285  15.361  0.34 19.47 ?  19  LYS   A HE3  1 
ATOM   341  H HZ1  A LYS   A 1 19  ? 10.549 -3.298  16.157  0.66 23.68 ?  19  LYS   A HZ1  1 
ATOM   342  H HZ1  B LYS   A 1 19  ? 10.854 -3.174  16.892  0.34 20.01 ?  19  LYS   A HZ1  1 
ATOM   343  H HZ2  A LYS   A 1 19  ? 11.164 -4.602  16.010  0.66 23.68 ?  19  LYS   A HZ2  1 
ATOM   344  H HZ2  B LYS   A 1 19  ? 11.436 -4.483  16.677  0.34 20.01 ?  19  LYS   A HZ2  1 
ATOM   345  H HZ3  A LYS   A 1 19  ? 11.716 -3.458  15.313  0.66 23.68 ?  19  LYS   A HZ3  1 
ATOM   346  H HZ3  B LYS   A 1 19  ? 12.043 -3.312  16.077  0.34 20.01 ?  19  LYS   A HZ3  1 
ATOM   347  N N    A ASN   A 1 20  ? 8.556  -4.797  9.248   0.66 16.80 ?  20  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 20  ? 8.712  -4.704  9.905   0.34 16.19 ?  20  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 20  ? 8.322  -3.461  8.709   0.66 18.34 ?  20  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 20  ? 8.329  -3.518  9.136   0.34 17.80 ?  20  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 20  ? 8.933  -2.462  9.684   0.66 19.41 ?  20  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 20  ? 8.864  -2.293  9.867   0.34 18.33 ?  20  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 20  ? 8.400  -2.249  10.779  0.66 19.96 ?  20  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 20  ? 8.220  -1.745  10.764  0.34 18.84 ?  20  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 20  ? 6.826  -3.214  8.521   0.66 19.00 ?  20  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 20  ? 6.812  -3.467  8.970   0.34 18.83 ?  20  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 20  ? 6.502  -1.761  8.198   0.66 20.32 ?  20  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 20  ? 6.335  -2.248  8.187   0.34 19.86 ?  20  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 20  ? 5.595  -1.166  8.787   0.66 22.54 ?  20  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 20  ? 5.240  -1.727  8.432   0.34 20.46 ?  20  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 20  ? 7.246  -1.183  7.263   0.66 20.48 ?  20  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 20  ? 7.149  -1.791  7.241   0.34 20.63 ?  20  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 20  ? 7.877  -5.138  9.655   0.66 20.14 ?  20  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 20  ? 8.091  -5.000  10.419  0.34 19.40 ?  20  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 20  ? 8.763  -3.381  7.852   0.66 21.99 ?  20  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 20  ? 8.745  -3.560  8.261   0.34 21.33 ?  20  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 20  ? 6.507  -3.763  7.787   0.66 22.78 ?  20  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 20  ? 6.523  -4.260  8.495   0.34 22.57 ?  20  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 20  ? 6.363  -3.455  9.338   0.66 22.78 ?  20  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 20  ? 6.403  -3.436  9.848   0.34 22.57 ?  20  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 20  ? 7.101  -0.365  7.049   0.66 24.55 ?  20  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 20  ? 6.919  -1.107  6.778   0.34 24.74 ?  20  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 20  ? 7.871  -1.628  6.872   0.66 24.55 ?  20  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 20  ? 7.904  -2.175  7.090   0.34 24.74 ?  20  ASN   A HD22 1 
ATOM   375  N N    A ALA   A 1 21  ? 10.066 -1.872  9.312   0.66 19.83 ?  21  ALA   A N    1 
ATOM   376  N N    B ALA   A 1 21  ? 10.059 -1.850  9.477   0.34 18.44 ?  21  ALA   A N    1 
ATOM   377  C CA   A ALA   A 1 21  ? 10.757 -0.974  10.225  0.66 19.55 ?  21  ALA   A CA   1 
ATOM   378  C CA   B ALA   A 1 21  ? 10.717 -0.764  10.189  0.34 18.01 ?  21  ALA   A CA   1 
ATOM   379  C C    A ALA   A 1 21  ? 11.721 -0.102  9.445   0.66 19.12 ?  21  ALA   A C    1 
ATOM   380  C C    B ALA   A 1 21  ? 11.828 -0.172  9.334   0.34 16.96 ?  21  ALA   A C    1 
ATOM   381  O O    A ALA   A 1 21  ? 12.148 -0.451  8.342   0.66 18.82 ?  21  ALA   A O    1 
ATOM   382  O O    B ALA   A 1 21  ? 12.360 -0.822  8.431   0.34 16.66 ?  21  ALA   A O    1 
ATOM   383  C CB   A ALA   A 1 21  ? 11.517 -1.747  11.306  0.66 20.10 ?  21  ALA   A CB   1 
ATOM   384  C CB   B ALA   A 1 21  ? 11.279 -1.242  11.532  0.34 18.74 ?  21  ALA   A CB   1 
ATOM   385  H H    A ALA   A 1 21  ? 10.447 -1.974  8.547   0.66 23.78 ?  21  ALA   A H    1 
ATOM   386  H H    B ALA   A 1 21  ? 10.502 -2.157  8.805   0.34 22.11 ?  21  ALA   A H    1 
ATOM   387  H HA   A ALA   A 1 21  ? 10.105 -0.398  10.658  0.66 23.44 ?  21  ALA   A HA   1 
ATOM   388  H HA   B ALA   A 1 21  ? 10.068 -0.066  10.367  0.34 21.59 ?  21  ALA   A HA   1 
ATOM   389  H HB1  A ALA   A 1 21  ? 11.938 -1.112  11.903  0.66 24.09 ?  21  ALA   A HB1  1 
ATOM   390  H HB1  B ALA   A 1 21  ? 11.738 -0.505  11.963  0.34 22.46 ?  21  ALA   A HB1  1 
ATOM   391  H HB2  A ALA   A 1 21  ? 10.884 -2.295  11.798  0.66 24.09 ?  21  ALA   A HB2  1 
ATOM   392  H HB2  B ALA   A 1 21  ? 10.547 -1.550  12.090  0.34 22.46 ?  21  ALA   A HB2  1 
ATOM   393  H HB3  A ALA   A 1 21  ? 12.183 -2.305  10.883  0.66 24.09 ?  21  ALA   A HB3  1 
ATOM   394  H HB3  B ALA   A 1 21  ? 11.901 -1.970  11.372  0.34 22.46 ?  21  ALA   A HB3  1 
ATOM   395  N N    A ASP   A 1 22  ? 12.042 1.048   10.045  0.66 18.81 ?  22  ASP   A N    1 
ATOM   396  N N    B ASP   A 1 22  ? 12.145 1.090   9.628   0.34 16.47 ?  22  ASP   A N    1 
ATOM   397  C CA   A ASP   A 1 22  ? 13.099 1.929   9.563   0.66 18.46 ?  22  ASP   A CA   1 
ATOM   398  C CA   B ASP   A 1 22  ? 13.336 1.745   9.096   0.34 15.85 ?  22  ASP   A CA   1 
ATOM   399  C C    A ASP   A 1 22  ? 14.424 1.434   10.130  0.66 16.72 ?  22  ASP   A C    1 
ATOM   400  C C    B ASP   A 1 22  ? 14.573 1.118   9.731   0.34 14.62 ?  22  ASP   A C    1 
ATOM   401  O O    A ASP   A 1 22  ? 14.618 1.427   11.350  0.66 17.39 ?  22  ASP   A O    1 
ATOM   402  O O    B ASP   A 1 22  ? 14.681 1.046   10.958  0.34 14.78 ?  22  ASP   A O    1 
ATOM   403  C CB   A ASP   A 1 22  ? 12.817 3.356   10.032  0.66 20.58 ?  22  ASP   A CB   1 
ATOM   404  C CB   B ASP   A 1 22  ? 13.263 3.238   9.442   0.34 16.76 ?  22  ASP   A CB   1 
ATOM   405  C CG   A ASP   A 1 22  ? 13.815 4.372   9.490   0.66 22.25 ?  22  ASP   A CG   1 
ATOM   406  C CG   B ASP   A 1 22  ? 14.380 4.068   8.815   0.34 17.12 ?  22  ASP   A CG   1 
ATOM   407  O OD1  A ASP   A 1 22  ? 14.910 3.988   9.033   0.66 22.48 ?  22  ASP   A OD1  1 
ATOM   408  O OD1  B ASP   A 1 22  ? 15.306 3.498   8.206   0.34 16.32 ?  22  ASP   A OD1  1 
ATOM   409  O OD2  A ASP   A 1 22  ? 13.493 5.578   9.525   0.66 23.83 -1 22  ASP   A OD2  1 
ATOM   410  O OD2  B ASP   A 1 22  ? 14.328 5.312   8.939   0.34 17.85 -1 22  ASP   A OD2  1 
ATOM   411  H H    A ASP   A 1 22  ? 11.644 1.350   10.749  0.66 22.55 ?  22  ASP   A H    1 
ATOM   412  H H    B ASP   A 1 22  ? 11.668 1.595   10.137  0.34 19.74 ?  22  ASP   A H    1 
ATOM   413  H HA   A ASP   A 1 22  ? 13.141 1.913   8.597   0.66 22.13 ?  22  ASP   A HA   1 
ATOM   414  H HA   B ASP   A 1 22  ? 13.381 1.638   8.133   0.34 18.99 ?  22  ASP   A HA   1 
ATOM   415  H HB2  A ASP   A 1 22  ? 11.940 3.626   9.719   0.66 24.67 ?  22  ASP   A HB2  1 
ATOM   416  H HB2  B ASP   A 1 22  ? 12.418 3.592   9.131   0.34 20.09 ?  22  ASP   A HB2  1 
ATOM   417  H HB3  A ASP   A 1 22  ? 12.842 3.382   11.003  0.66 24.67 ?  22  ASP   A HB3  1 
ATOM   418  H HB3  B ASP   A 1 22  ? 13.329 3.333   10.403  0.34 20.09 ?  22  ASP   A HB3  1 
ATOM   419  N N    A ILE   A 1 23  ? 15.330 1.007   9.247   0.66 15.95 ?  23  ILE   A N    1 
ATOM   420  N N    B ILE   A 1 23  ? 15.504 0.646   8.893   0.34 13.80 ?  23  ILE   A N    1 
ATOM   421  C CA   A ILE   A 1 23  ? 16.590 0.414   9.689   0.66 15.01 ?  23  ILE   A CA   1 
ATOM   422  C CA   B ILE   A 1 23  ? 16.726 0.027   9.399   0.34 12.96 ?  23  ILE   A CA   1 
ATOM   423  C C    A ILE   A 1 23  ? 17.378 1.381   10.561  0.66 14.88 ?  23  ILE   A C    1 
ATOM   424  C C    B ILE   A 1 23  ? 17.479 0.985   10.308  0.34 13.38 ?  23  ILE   A C    1 
ATOM   425  O O    A ILE   A 1 23  ? 18.103 0.959   11.469  0.66 15.14 ?  23  ILE   A O    1 
ATOM   426  O O    B ILE   A 1 23  ? 18.145 0.560   11.259  0.34 13.27 ?  23  ILE   A O    1 
ATOM   427  C CB   A ILE   A 1 23  ? 17.404 -0.088  8.476   0.66 14.58 ?  23  ILE   A CB   1 
ATOM   428  C CB   B ILE   A 1 23  ? 17.615 -0.497  8.245   0.34 12.25 ?  23  ILE   A CB   1 
ATOM   429  C CG1  A ILE   A 1 23  ? 18.561 -0.982  8.937   0.66 14.81 ?  23  ILE   A CG1  1 
ATOM   430  C CG1  B ILE   A 1 23  ? 18.687 -1.442  8.801   0.34 12.14 ?  23  ILE   A CG1  1 
ATOM   431  C CG2  A ILE   A 1 23  ? 17.887 1.084   7.623   0.66 14.75 ?  23  ILE   A CG2  1 
ATOM   432  C CG2  B ILE   A 1 23  ? 18.265 0.653   7.470   0.34 12.08 ?  23  ILE   A CG2  1 
ATOM   433  C CD1  A ILE   A 1 23  ? 19.287 -1.676  7.796   0.66 15.19 ?  23  ILE   A CD1  1 
ATOM   434  C CD1  B ILE   A 1 23  ? 19.613 -2.031  7.747   0.34 12.21 ?  23  ILE   A CD1  1 
ATOM   435  H H    A ILE   A 1 23  ? 15.233 1.041   8.400   0.66 19.12 ?  23  ILE   A H    1 
ATOM   436  H H    B ILE   A 1 23  ? 15.457 0.662   8.050   0.34 16.54 ?  23  ILE   A H    1 
ATOM   437  H HA   A ILE   A 1 23  ? 16.390 -0.360  10.237  0.66 17.99 ?  23  ILE   A HA   1 
ATOM   438  H HA   B ILE   A 1 23  ? 16.468 -0.740  9.928   0.34 15.52 ?  23  ILE   A HA   1 
ATOM   439  H HB   A ILE   A 1 23  ? 16.815 -0.630  7.930   0.66 17.48 ?  23  ILE   A HB   1 
ATOM   440  H HB   B ILE   A 1 23  ? 17.057 -1.002  7.632   0.34 14.68 ?  23  ILE   A HB   1 
ATOM   441  H HG12 A ILE   A 1 23  ? 19.210 -0.440  9.412   0.66 17.75 ?  23  ILE   A HG12 1 
ATOM   442  H HG12 B ILE   A 1 23  ? 19.238 -0.954  9.433   0.34 14.54 ?  23  ILE   A HG12 1 
ATOM   443  H HG13 A ILE   A 1 23  ? 18.213 -1.670  9.526   0.66 17.75 ?  23  ILE   A HG13 1 
ATOM   444  H HG13 B ILE   A 1 23  ? 18.250 -2.182  9.251   0.34 14.54 ?  23  ILE   A HG13 1 
ATOM   445  H HG21 A ILE   A 1 23  ? 18.244 0.740   6.789   0.66 17.68 ?  23  ILE   A HG21 1 
ATOM   446  H HG21 B ILE   A 1 23  ? 18.633 0.305   6.640   0.34 14.48 ?  23  ILE   A HG21 1 
ATOM   447  H HG22 A ILE   A 1 23  ? 17.134 1.669   7.441   0.66 17.68 ?  23  ILE   A HG22 1 
ATOM   448  H HG22 B ILE   A 1 23  ? 17.592 1.321   7.278   0.34 14.48 ?  23  ILE   A HG22 1 
ATOM   449  H HG23 A ILE   A 1 23  ? 18.573 1.567   8.105   0.66 17.68 ?  23  ILE   A HG23 1 
ATOM   450  H HG23 B ILE   A 1 23  ? 18.973 1.037   8.009   0.34 14.48 ?  23  ILE   A HG23 1 
ATOM   451  H HD11 A ILE   A 1 23  ? 19.960 -2.270  8.164   0.66 18.21 ?  23  ILE   A HD11 1 
ATOM   452  H HD11 B ILE   A 1 23  ? 20.175 -2.705  8.163   0.34 14.62 ?  23  ILE   A HD11 1 
ATOM   453  H HD12 A ILE   A 1 23  ? 18.644 -2.185  7.278   0.66 18.21 ?  23  ILE   A HD12 1 
ATOM   454  H HD12 B ILE   A 1 23  ? 19.078 -2.432  7.046   0.34 14.62 ?  23  ILE   A HD12 1 
ATOM   455  H HD13 A ILE   A 1 23  ? 19.708 -1.006  7.235   0.66 18.21 ?  23  ILE   A HD13 1 
ATOM   456  H HD13 B ILE   A 1 23  ? 20.165 -1.323  7.380   0.34 14.62 ?  23  ILE   A HD13 1 
ATOM   457  N N    A VAL   A 1 24  ? 17.241 2.685   10.319  0.66 15.80 ?  24  VAL   A N    1 
ATOM   458  N N    B VAL   A 1 24  ? 17.386 2.287   10.040  0.34 14.54 ?  24  VAL   A N    1 
ATOM   459  C CA   A VAL   A 1 24  ? 17.931 3.670   11.148  0.66 16.89 ?  24  VAL   A CA   1 
ATOM   460  C CA   B VAL   A 1 24  ? 18.055 3.269   10.886  0.34 15.68 ?  24  VAL   A CA   1 
ATOM   461  C C    A VAL   A 1 24  ? 17.419 3.607   12.580  0.66 17.77 ?  24  VAL   A C    1 
ATOM   462  C C    B VAL   A 1 24  ? 17.446 3.272   12.282  0.34 16.78 ?  24  VAL   A C    1 
ATOM   463  O O    A VAL   A 1 24  ? 18.199 3.557   13.539  0.66 18.37 ?  24  VAL   A O    1 
ATOM   464  O O    B VAL   A 1 24  ? 18.167 3.297   13.286  0.34 17.43 ?  24  VAL   A O    1 
ATOM   465  C CB   A VAL   A 1 24  ? 17.770 5.078   10.549  0.66 17.68 ?  24  VAL   A CB   1 
ATOM   466  C CB   B VAL   A 1 24  ? 18.007 4.656   10.222  0.34 16.12 ?  24  VAL   A CB   1 
ATOM   467  C CG1  A VAL   A 1 24  ? 18.266 6.136   11.526  0.66 18.29 ?  24  VAL   A CG1  1 
ATOM   468  C CG1  B VAL   A 1 24  ? 18.727 5.678   11.078  0.34 16.67 ?  24  VAL   A CG1  1 
ATOM   469  C CG2  A VAL   A 1 24  ? 18.509 5.170   9.222   0.66 18.59 ?  24  VAL   A CG2  1 
ATOM   470  C CG2  B VAL   A 1 24  ? 18.617 4.586   8.834   0.34 15.97 ?  24  VAL   A CG2  1 
ATOM   471  H H    A VAL   A 1 24  ? 16.763 3.021   9.690   0.66 18.94 ?  24  VAL   A H    1 
ATOM   472  H H    B VAL   A 1 24  ? 16.948 2.621   9.386   0.34 17.43 ?  24  VAL   A H    1 
ATOM   473  H HA   A VAL   A 1 24  ? 18.878 3.463   11.163  0.66 20.24 ?  24  VAL   A HA   1 
ATOM   474  H HA   B VAL   A 1 24  ? 18.986 3.018   10.978  0.34 18.80 ?  24  VAL   A HA   1 
ATOM   475  H HB   A VAL   A 1 24  ? 16.830 5.245   10.376  0.66 21.19 ?  24  VAL   A HB   1 
ATOM   476  H HB   B VAL   A 1 24  ? 17.081 4.933   10.133  0.34 19.32 ?  24  VAL   A HB   1 
ATOM   477  H HG11 A VAL   A 1 24  ? 18.418 6.962   11.041  0.66 21.93 ?  24  VAL   A HG11 1 
ATOM   478  H HG11 B VAL   A 1 24  ? 18.839 6.494   10.568  0.34 19.98 ?  24  VAL   A HG11 1 
ATOM   479  H HG12 A VAL   A 1 24  ? 17.595 6.274   12.210  0.66 21.93 ?  24  VAL   A HG12 1 
ATOM   480  H HG12 B VAL   A 1 24  ? 18.190 5.852   11.867  0.34 19.98 ?  24  VAL   A HG12 1 
ATOM   481  H HG13 A VAL   A 1 24  ? 19.095 5.830   11.925  0.66 21.93 ?  24  VAL   A HG13 1 
ATOM   482  H HG13 B VAL   A 1 24  ? 19.592 5.323   11.335  0.34 19.98 ?  24  VAL   A HG13 1 
ATOM   483  H HG21 A VAL   A 1 24  ? 18.251 5.990   8.771   0.66 22.29 ?  24  VAL   A HG21 1 
ATOM   484  H HG21 B VAL   A 1 24  ? 18.780 5.486   8.517   0.34 19.14 ?  24  VAL   A HG21 1 
ATOM   485  H HG22 A VAL   A 1 24  ? 19.465 5.177   9.392   0.66 22.29 ?  24  VAL   A HG22 1 
ATOM   486  H HG22 B VAL   A 1 24  ? 19.453 4.096   8.884   0.34 19.14 ?  24  VAL   A HG22 1 
ATOM   487  H HG23 A VAL   A 1 24  ? 18.276 4.405   8.672   0.66 22.29 ?  24  VAL   A HG23 1 
ATOM   488  H HG23 B VAL   A 1 24  ? 18.001 4.128   8.242   0.34 19.14 ?  24  VAL   A HG23 1 
ATOM   489  N N    A GLU   A 1 25  ? 16.094 3.618   12.744  0.66 18.69 ?  25  GLU   A N    1 
ATOM   490  N N    B GLU   A 1 25  ? 16.114 3.226   12.371  0.34 17.79 ?  25  GLU   A N    1 
ATOM   491  C CA   A GLU   A 1 25  ? 15.516 3.558   14.082  0.66 19.81 ?  25  GLU   A CA   1 
ATOM   492  C CA   B GLU   A 1 25  ? 15.462 3.195   13.677  0.34 19.00 ?  25  GLU   A CA   1 
ATOM   493  C C    A GLU   A 1 25  ? 15.762 2.200   14.724  0.66 18.54 ?  25  GLU   A C    1 
ATOM   494  C C    B GLU   A 1 25  ? 15.717 1.871   14.389  0.34 18.88 ?  25  GLU   A C    1 
ATOM   495  O O    A GLU   A 1 25  ? 16.000 2.114   15.934  0.66 19.43 ?  25  GLU   A O    1 
ATOM   496  O O    B GLU   A 1 25  ? 15.901 1.843   15.611  0.34 19.38 ?  25  GLU   A O    1 
ATOM   497  C CB   A GLU   A 1 25  ? 14.022 3.887   14.022  0.66 22.24 ?  25  GLU   A CB   1 
ATOM   498  C CB   B GLU   A 1 25  ? 13.963 3.466   13.528  0.34 20.27 ?  25  GLU   A CB   1 
ATOM   499  C CG   A GLU   A 1 25  ? 13.738 5.346   13.679  0.66 25.11 ?  25  GLU   A CG   1 
ATOM   500  C CG   B GLU   A 1 25  ? 13.646 4.856   12.994  0.34 22.11 ?  25  GLU   A CG   1 
ATOM   501  C CD   A GLU   A 1 25  ? 14.515 6.319   14.554  0.66 27.59 ?  25  GLU   A CD   1 
ATOM   502  C CD   B GLU   A 1 25  ? 14.152 5.954   13.901  0.34 23.66 ?  25  GLU   A CD   1 
ATOM   503  O OE1  A GLU   A 1 25  ? 14.580 6.101   15.783  0.66 28.36 ?  25  GLU   A OE1  1 
ATOM   504  O OE1  B GLU   A 1 25  ? 14.122 5.765   15.136  0.34 24.63 ?  25  GLU   A OE1  1 
ATOM   505  O OE2  A GLU   A 1 25  ? 15.084 7.286   14.008  0.66 28.74 -1 25  GLU   A OE2  1 
ATOM   506  O OE2  B GLU   A 1 25  ? 14.585 7.003   13.380  0.34 24.14 -1 25  GLU   A OE2  1 
ATOM   507  H H    A GLU   A 1 25  ? 15.519 3.663   12.106  0.66 22.40 ?  25  GLU   A H    1 
ATOM   508  H H    B GLU   A 1 25  ? 15.576 3.210   11.701  0.34 21.32 ?  25  GLU   A H    1 
ATOM   509  H HA   A GLU   A 1 25  ? 15.949 4.220   14.638  0.66 23.75 ?  25  GLU   A HA   1 
ATOM   510  H HA   B GLU   A 1 25  ? 15.836 3.897   14.229  0.34 22.78 ?  25  GLU   A HA   1 
ATOM   511  H HB2  A GLU   A 1 25  ? 13.600 3.336   13.340  0.66 26.66 ?  25  GLU   A HB2  1 
ATOM   512  H HB2  B GLU   A 1 25  ? 13.585 2.822   12.911  0.34 24.30 ?  25  GLU   A HB2  1 
ATOM   513  H HB3  A GLU   A 1 25  ? 13.619 3.704   14.885  0.66 26.66 ?  25  GLU   A HB3  1 
ATOM   514  H HB3  B GLU   A 1 25  ? 13.539 3.381   14.397  0.34 24.30 ?  25  GLU   A HB3  1 
ATOM   515  H HG2  A GLU   A 1 25  ? 13.995 5.507   12.758  0.66 30.11 ?  25  GLU   A HG2  1 
ATOM   516  H HG2  B GLU   A 1 25  ? 14.061 4.966   12.124  0.34 26.51 ?  25  GLU   A HG2  1 
ATOM   517  H HG3  A GLU   A 1 25  ? 12.788 5.517   13.794  0.66 30.11 ?  25  GLU   A HG3  1 
ATOM   518  H HG3  B GLU   A 1 25  ? 12.686 4.961   12.921  0.34 26.51 ?  25  GLU   A HG3  1 
ATOM   519  N N    A GLU   A 1 26  ? 15.722 1.129   13.928  0.66 18.31 ?  26  GLU   A N    1 
ATOM   520  N N    B GLU   A 1 26  ? 15.737 0.763   13.643  0.34 18.65 ?  26  GLU   A N    1 
ATOM   521  C CA   A GLU   A 1 26  ? 16.033 -0.196  14.454  0.66 18.28 ?  26  GLU   A CA   1 
ATOM   522  C CA   B GLU   A 1 26  ? 16.095 -0.517  14.246  0.34 18.83 ?  26  GLU   A CA   1 
ATOM   523  C C    A GLU   A 1 26  ? 17.458 -0.247  14.989  0.66 17.17 ?  26  GLU   A C    1 
ATOM   524  C C    B GLU   A 1 26  ? 17.522 -0.502  14.775  0.34 18.14 ?  26  GLU   A C    1 
ATOM   525  O O    A GLU   A 1 26  ? 17.703 -0.742  16.094  0.66 17.14 ?  26  GLU   A O    1 
ATOM   526  O O    B GLU   A 1 26  ? 17.815 -1.137  15.794  0.34 18.22 ?  26  GLU   A O    1 
ATOM   527  C CB   A GLU   A 1 26  ? 15.850 -1.249  13.361  0.66 20.06 ?  26  GLU   A CB   1 
ATOM   528  C CB   B GLU   A 1 26  ? 15.928 -1.645  13.227  0.34 19.93 ?  26  GLU   A CB   1 
ATOM   529  C CG   A GLU   A 1 26  ? 14.458 -1.837  13.253  0.66 22.83 ?  26  GLU   A CG   1 
ATOM   530  C CG   B GLU   A 1 26  ? 14.488 -2.009  12.946  0.34 20.89 ?  26  GLU   A CG   1 
ATOM   531  C CD   A GLU   A 1 26  ? 14.046 -2.631  14.487  0.66 24.15 ?  26  GLU   A CD   1 
ATOM   532  C CD   B GLU   A 1 26  ? 13.771 -2.522  14.173  0.34 21.39 ?  26  GLU   A CD   1 
ATOM   533  O OE1  A GLU   A 1 26  ? 14.499 -3.786  14.669  0.66 24.60 ?  26  GLU   A OE1  1 
ATOM   534  O OE1  B GLU   A 1 26  ? 14.320 -3.409  14.860  0.34 22.11 ?  26  GLU   A OE1  1 
ATOM   535  O OE2  A GLU   A 1 26  ? 13.264 -2.086  15.282  0.66 24.65 -1 26  GLU   A OE2  1 
ATOM   536  O OE2  B GLU   A 1 26  ? 12.663 -2.026  14.455  0.34 20.80 -1 26  GLU   A OE2  1 
ATOM   537  H H    A GLU   A 1 26  ? 15.529 1.151   13.091  0.66 21.95 ?  26  GLU   A H    1 
ATOM   538  H H    B GLU   A 1 26  ? 15.550 0.727   12.806  0.34 22.36 ?  26  GLU   A H    1 
ATOM   539  H HA   A GLU   A 1 26  ? 15.430 -0.394  15.182  0.66 21.92 ?  26  GLU   A HA   1 
ATOM   540  H HA   B GLU   A 1 26  ? 15.503 -0.693  14.993  0.34 22.57 ?  26  GLU   A HA   1 
ATOM   541  H HB2  A GLU   A 1 26  ? 16.067 -0.841  12.504  0.66 24.05 ?  26  GLU   A HB2  1 
ATOM   542  H HB2  B GLU   A 1 26  ? 16.331 -1.371  12.387  0.34 23.89 ?  26  GLU   A HB2  1 
ATOM   543  H HB3  A GLU   A 1 26  ? 16.465 -1.976  13.535  0.66 24.05 ?  26  GLU   A HB3  1 
ATOM   544  H HB3  B GLU   A 1 26  ? 16.375 -2.439  13.561  0.34 23.89 ?  26  GLU   A HB3  1 
ATOM   545  H HG2  A GLU   A 1 26  ? 13.826 -1.111  13.115  0.66 27.38 ?  26  GLU   A HG2  1 
ATOM   546  H HG2  B GLU   A 1 26  ? 14.012 -1.221  12.644  0.34 25.05 ?  26  GLU   A HG2  1 
ATOM   547  H HG3  A GLU   A 1 26  ? 14.433 -2.442  12.497  0.66 27.38 ?  26  GLU   A HG3  1 
ATOM   548  H HG3  B GLU   A 1 26  ? 14.459 -2.700  12.267  0.34 25.05 ?  26  GLU   A HG3  1 
ATOM   549  N N    A ALA   A 1 27  ? 18.416 0.260   14.211  0.66 16.33 ?  27  ALA   A N    1 
ATOM   550  N N    B ALA   A 1 27  ? 18.424 0.212   14.101  0.34 17.34 ?  27  ALA   A N    1 
ATOM   551  C CA   A ALA   A 1 27  ? 19.812 0.210   14.634  0.66 16.79 ?  27  ALA   A CA   1 
ATOM   552  C CA   B ALA   A 1 27  ? 19.797 0.289   14.586  0.34 17.24 ?  27  ALA   A CA   1 
ATOM   553  C C    A ALA   A 1 27  ? 20.022 0.988   15.927  0.66 18.03 ?  27  ALA   A C    1 
ATOM   554  C C    B ALA   A 1 27  ? 19.896 1.177   15.822  0.34 18.10 ?  27  ALA   A C    1 
ATOM   555  O O    A ALA   A 1 27  ? 20.693 0.509   16.848  0.66 18.40 ?  27  ALA   A O    1 
ATOM   556  O O    B ALA   A 1 27  ? 20.591 0.835   16.785  0.34 18.02 ?  27  ALA   A O    1 
ATOM   557  C CB   A ALA   A 1 27  ? 20.724 0.738   13.523  0.66 16.34 ?  27  ALA   A CB   1 
ATOM   558  C CB   B ALA   A 1 27  ? 20.723 0.786   13.475  0.34 16.79 ?  27  ALA   A CB   1 
ATOM   559  H H    A ALA   A 1 27  ? 18.287 0.643   13.452  0.66 19.57 ?  27  ALA   A H    1 
ATOM   560  H H    B ALA   A 1 27  ? 18.267 0.647   13.376  0.34 20.78 ?  27  ALA   A H    1 
ATOM   561  H HA   A ALA   A 1 27  ? 20.054 -0.712  14.801  0.66 20.13 ?  27  ALA   A HA   1 
ATOM   562  H HA   B ALA   A 1 27  ? 20.087 -0.601  14.834  0.34 20.66 ?  27  ALA   A HA   1 
ATOM   563  H HB1  A ALA   A 1 27  ? 21.648 0.692   13.822  0.66 19.58 ?  27  ALA   A HB1  1 
ATOM   564  H HB1  B ALA   A 1 27  ? 21.630 0.826   13.817  0.34 20.12 ?  27  ALA   A HB1  1 
ATOM   565  H HB2  A ALA   A 1 27  ? 20.608 0.187   12.732  0.66 19.58 ?  27  ALA   A HB2  1 
ATOM   566  H HB2  B ALA   A 1 27  ? 20.680 0.168   12.727  0.34 20.12 ?  27  ALA   A HB2  1 
ATOM   567  H HB3  A ALA   A 1 27  ? 20.488 1.656   13.325  0.66 19.58 ?  27  ALA   A HB3  1 
ATOM   568  H HB3  B ALA   A 1 27  ? 20.436 1.667   13.192  0.34 20.12 ?  27  ALA   A HB3  1 
ATOM   569  N N    A LYS   A 1 28  ? 19.448 2.190   16.020  0.66 20.15 ?  28  LYS   A N    1 
ATOM   570  N N    B LYS   A 1 28  ? 19.196 2.315   15.822  0.34 19.40 ?  28  LYS   A N    1 
ATOM   571  C CA   A LYS   A 1 28  ? 19.602 2.992   17.230  0.66 22.92 ?  28  LYS   A CA   1 
ATOM   572  C CA   B LYS   A 1 28  ? 19.260 3.219   16.967  0.34 21.07 ?  28  LYS   A CA   1 
ATOM   573  C C    A LYS   A 1 28  ? 19.042 2.273   18.453  0.66 24.25 ?  28  LYS   A C    1 
ATOM   574  C C    B LYS   A 1 28  ? 18.735 2.566   18.238  0.34 22.62 ?  28  LYS   A C    1 
ATOM   575  O O    A LYS   A 1 28  ? 19.603 2.374   19.551  0.66 25.48 ?  28  LYS   A O    1 
ATOM   576  O O    B LYS   A 1 28  ? 19.156 2.933   19.341  0.34 23.01 ?  28  LYS   A O    1 
ATOM   577  C CB   A LYS   A 1 28  ? 18.949 4.365   17.042  0.66 24.60 ?  28  LYS   A CB   1 
ATOM   578  C CB   B LYS   A 1 28  ? 18.471 4.495   16.677  0.34 21.63 ?  28  LYS   A CB   1 
ATOM   579  C CG   A LYS   A 1 28  ? 19.762 5.313   16.165  0.66 26.04 ?  28  LYS   A CG   1 
ATOM   580  C CG   B LYS   A 1 28  ? 19.073 5.367   15.594  0.34 22.39 ?  28  LYS   A CG   1 
ATOM   581  C CD   A LYS   A 1 28  ? 19.241 6.743   16.216  0.66 27.88 ?  28  LYS   A CD   1 
ATOM   582  C CD   B LYS   A 1 28  ? 18.326 6.684   15.474  0.34 23.30 ?  28  LYS   A CD   1 
ATOM   583  C CE   A LYS   A 1 28  ? 17.916 6.882   15.491  0.66 29.16 ?  28  LYS   A CE   1 
ATOM   584  C CE   B LYS   A 1 28  ? 18.894 7.545   14.358  0.34 24.14 ?  28  LYS   A CE   1 
ATOM   585  N NZ   A LYS   A 1 28  ? 17.481 8.304   15.418  0.66 29.86 ?  28  LYS   A NZ   1 
ATOM   586  N NZ   B LYS   A 1 28  ? 18.296 8.909   14.339  0.34 24.63 ?  28  LYS   A NZ   1 
ATOM   587  H H    A LYS   A 1 28  ? 18.979 2.556   15.405  0.66 24.16 ?  28  LYS   A H    1 
ATOM   588  H H    B LYS   A 1 28  ? 18.689 2.580   15.182  0.34 23.26 ?  28  LYS   A H    1 
ATOM   589  H HA   A LYS   A 1 28  ? 20.545 3.139   17.395  0.66 27.48 ?  28  LYS   A HA   1 
ATOM   590  H HA   B LYS   A 1 28  ? 20.183 3.467   17.119  0.34 25.26 ?  28  LYS   A HA   1 
ATOM   591  H HB2  A LYS   A 1 28  ? 18.084 4.250   16.621  0.66 29.50 ?  28  LYS   A HB2  1 
ATOM   592  H HB2  B LYS   A 1 28  ? 17.575 4.252   16.396  0.34 25.94 ?  28  LYS   A HB2  1 
ATOM   593  H HB3  A LYS   A 1 28  ? 18.843 4.789   17.907  0.66 29.50 ?  28  LYS   A HB3  1 
ATOM   594  H HB3  B LYS   A 1 28  ? 18.427 5.025   17.489  0.34 25.94 ?  28  LYS   A HB3  1 
ATOM   595  H HG2  A LYS   A 1 28  ? 20.683 5.319   16.470  0.66 31.22 ?  28  LYS   A HG2  1 
ATOM   596  H HG2  B LYS   A 1 28  ? 19.996 5.560   15.814  0.34 26.84 ?  28  LYS   A HG2  1 
ATOM   597  H HG3  A LYS   A 1 28  ? 19.719 5.012   15.244  0.66 31.22 ?  28  LYS   A HG3  1 
ATOM   598  H HG3  B LYS   A 1 28  ? 19.021 4.908   14.742  0.34 26.84 ?  28  LYS   A HG3  1 
ATOM   599  H HD2  A LYS   A 1 28  ? 19.109 7.003   17.141  0.66 33.43 ?  28  LYS   A HD2  1 
ATOM   600  H HD2  B LYS   A 1 28  ? 17.392 6.507   15.279  0.34 27.94 ?  28  LYS   A HD2  1 
ATOM   601  H HD3  A LYS   A 1 28  ? 19.883 7.334   15.791  0.66 33.43 ?  28  LYS   A HD3  1 
ATOM   602  H HD3  B LYS   A 1 28  ? 18.407 7.175   16.308  0.34 27.94 ?  28  LYS   A HD3  1 
ATOM   603  H HE2  A LYS   A 1 28  ? 18.011 6.546   14.586  0.66 34.96 ?  28  LYS   A HE2  1 
ATOM   604  H HE2  B LYS   A 1 28  ? 19.852 7.634   14.482  0.34 28.95 ?  28  LYS   A HE2  1 
ATOM   605  H HE3  A LYS   A 1 28  ? 17.237 6.380   15.967  0.66 34.96 ?  28  LYS   A HE3  1 
ATOM   606  H HE3  B LYS   A 1 28  ? 18.708 7.123   13.505  0.34 28.95 ?  28  LYS   A HE3  1 
ATOM   607  H HZ1  A LYS   A 1 28  ? 16.704 8.362   14.989  0.66 35.81 ?  28  LYS   A HZ1  1 
ATOM   608  H HZ1  B LYS   A 1 28  ? 18.648 9.386   13.676  0.34 29.54 ?  28  LYS   A HZ1  1 
ATOM   609  H HZ2  A LYS   A 1 28  ? 17.386 8.635   16.239  0.66 35.81 ?  28  LYS   A HZ2  1 
ATOM   610  H HZ2  B LYS   A 1 28  ? 17.416 8.854   14.220  0.34 29.54 ?  28  LYS   A HZ2  1 
ATOM   611  H HZ3  A LYS   A 1 28  ? 18.090 8.786   14.981  0.66 35.81 ?  28  LYS   A HZ3  1 
ATOM   612  H HZ3  B LYS   A 1 28  ? 18.458 9.322   15.110  0.34 29.54 ?  28  LYS   A HZ3  1 
ATOM   613  N N    A LYS   A 1 29  ? 17.947 1.530   18.284  0.66 24.91 ?  29  LYS   A N    1 
ATOM   614  N N    B LYS   A 1 29  ? 17.818 1.608   18.111  0.34 24.09 ?  29  LYS   A N    1 
ATOM   615  C CA   A LYS   A 1 29  ? 17.343 0.827   19.413  0.66 26.66 ?  29  LYS   A CA   1 
ATOM   616  C CA   B LYS   A 1 29  ? 17.227 0.947   19.268  0.34 26.04 ?  29  LYS   A CA   1 
ATOM   617  C C    A LYS   A 1 29  ? 18.164 -0.396  19.807  0.66 26.35 ?  29  LYS   A C    1 
ATOM   618  C C    B LYS   A 1 29  ? 18.017 -0.280  19.704  0.34 25.62 ?  29  LYS   A C    1 
ATOM   619  O O    A LYS   A 1 29  ? 18.487 -0.589  20.985  0.66 27.48 ?  29  LYS   A O    1 
ATOM   620  O O    B LYS   A 1 29  ? 18.243 -0.475  20.903  0.34 26.08 ?  29  LYS   A O    1 
ATOM   621  C CB   A LYS   A 1 29  ? 15.916 0.407   19.056  0.66 29.11 ?  29  LYS   A CB   1 
ATOM   622  C CB   B LYS   A 1 29  ? 15.789 0.531   18.948  0.34 28.41 ?  29  LYS   A CB   1 
ATOM   623  C CG   A LYS   A 1 29  ? 15.173 -0.302  20.180  0.66 32.06 ?  29  LYS   A CG   1 
ATOM   624  C CG   B LYS   A 1 29  ? 15.066 -0.174  20.088  0.34 30.84 ?  29  LYS   A CG   1 
ATOM   625  C CD   A LYS   A 1 29  ? 14.829 0.659   21.305  0.66 34.95 ?  29  LYS   A CD   1 
ATOM   626  C CD   B LYS   A 1 29  ? 14.764 0.782   21.229  0.34 33.04 ?  29  LYS   A CD   1 
ATOM   627  C CE   A LYS   A 1 29  ? 13.968 -0.012  22.363  0.66 36.94 ?  29  LYS   A CE   1 
ATOM   628  C CE   B LYS   A 1 29  ? 13.990 0.092   22.339  0.34 34.58 ?  29  LYS   A CE   1 
ATOM   629  N NZ   A LYS   A 1 29  ? 13.534 0.951   23.412  0.66 38.16 ?  29  LYS   A NZ   1 
ATOM   630  N NZ   B LYS   A 1 29  ? 13.633 1.035   23.433  0.34 35.45 ?  29  LYS   A NZ   1 
ATOM   631  H H    A LYS   A 1 29  ? 17.539 1.419   17.537  0.66 29.87 ?  29  LYS   A H    1 
ATOM   632  H H    B LYS   A 1 29  ? 17.519 1.322   17.360  0.34 28.88 ?  29  LYS   A H    1 
ATOM   633  H HA   A LYS   A 1 29  ? 17.300 1.422   20.178  0.66 31.97 ?  29  LYS   A HA   1 
ATOM   634  H HA   B LYS   A 1 29  ? 17.204 1.568   20.012  0.34 31.23 ?  29  LYS   A HA   1 
ATOM   635  H HB2  A LYS   A 1 29  ? 15.406 1.197   18.822  0.66 34.91 ?  29  LYS   A HB2  1 
ATOM   636  H HB2  B LYS   A 1 29  ? 15.281 1.325   18.727  0.34 34.07 ?  29  LYS   A HB2  1 
ATOM   637  H HB3  A LYS   A 1 29  ? 15.949 -0.200  18.300  0.66 34.91 ?  29  LYS   A HB3  1 
ATOM   638  H HB3  B LYS   A 1 29  ? 15.802 -0.074  18.191  0.34 34.07 ?  29  LYS   A HB3  1 
ATOM   639  H HG2  A LYS   A 1 29  ? 14.346 -0.669  19.833  0.66 38.45 ?  29  LYS   A HG2  1 
ATOM   640  H HG2  B LYS   A 1 29  ? 14.225 -0.525  19.759  0.34 36.99 ?  29  LYS   A HG2  1 
ATOM   641  H HG3  A LYS   A 1 29  ? 15.725 -1.013  20.545  0.66 38.45 ?  29  LYS   A HG3  1 
ATOM   642  H HG3  B LYS   A 1 29  ? 15.615 -0.897  20.432  0.34 36.99 ?  29  LYS   A HG3  1 
ATOM   643  H HD2  A LYS   A 1 29  ? 15.646 0.966   21.728  0.66 41.91 ?  29  LYS   A HD2  1 
ATOM   644  H HD2  B LYS   A 1 29  ? 15.597 1.114   21.599  0.34 39.62 ?  29  LYS   A HD2  1 
ATOM   645  H HD3  A LYS   A 1 29  ? 14.335 1.412   20.943  0.66 41.91 ?  29  LYS   A HD3  1 
ATOM   646  H HD3  B LYS   A 1 29  ? 14.228 1.519   20.895  0.34 39.62 ?  29  LYS   A HD3  1 
ATOM   647  H HE2  A LYS   A 1 29  ? 13.175 -0.381  21.943  0.66 44.31 ?  29  LYS   A HE2  1 
ATOM   648  H HE2  B LYS   A 1 29  ? 13.169 -0.275  21.974  0.34 41.47 ?  29  LYS   A HE2  1 
ATOM   649  H HE3  A LYS   A 1 29  ? 14.479 -0.717  22.791  0.66 44.31 ?  29  LYS   A HE3  1 
ATOM   650  H HE3  B LYS   A 1 29  ? 14.535 -0.618  22.714  0.34 41.47 ?  29  LYS   A HE3  1 
ATOM   651  H HZ1  A LYS   A 1 29  ? 13.033 0.535   24.018  0.66 45.77 ?  29  LYS   A HZ1  1 
ATOM   652  H HZ1  B LYS   A 1 29  ? 13.181 0.606   24.069  0.34 42.52 ?  29  LYS   A HZ1  1 
ATOM   653  H HZ2  A LYS   A 1 29  ? 14.245 1.301   23.816  0.66 45.77 ?  29  LYS   A HZ2  1 
ATOM   654  H HZ2  B LYS   A 1 29  ? 14.372 1.382   23.788  0.34 42.52 ?  29  LYS   A HZ2  1 
ATOM   655  H HZ3  A LYS   A 1 29  ? 13.058 1.607   23.044  0.66 45.77 ?  29  LYS   A HZ3  1 
ATOM   656  H HZ3  B LYS   A 1 29  ? 13.128 1.694   23.113  0.34 42.52 ?  29  LYS   A HZ3  1 
ATOM   657  N N    A VAL   A 1 30  ? 18.491 -1.246  18.833  0.66 24.61 ?  30  VAL   A N    1 
ATOM   658  N N    B VAL   A 1 30  ? 18.436 -1.114  18.755  0.34 24.86 ?  30  VAL   A N    1 
ATOM   659  C CA   A VAL   A 1 30  ? 19.152 -2.511  19.130  0.66 23.64 ?  30  VAL   A CA   1 
ATOM   660  C CA   B VAL   A 1 30  ? 19.072 -2.382  19.092  0.34 24.27 ?  30  VAL   A CA   1 
ATOM   661  C C    A VAL   A 1 30  ? 20.650 -2.326  19.336  0.66 22.16 ?  30  VAL   A C    1 
ATOM   662  C C    B VAL   A 1 30  ? 20.575 -2.232  19.311  0.34 23.56 ?  30  VAL   A C    1 
ATOM   663  O O    A VAL   A 1 30  ? 21.262 -3.041  20.137  0.66 22.44 ?  30  VAL   A O    1 
ATOM   664  O O    B VAL   A 1 30  ? 21.151 -2.936  20.146  0.34 23.62 ?  30  VAL   A O    1 
ATOM   665  C CB   A VAL   A 1 30  ? 18.865 -3.521  18.004  0.66 24.23 ?  30  VAL   A CB   1 
ATOM   666  C CB   B VAL   A 1 30  ? 18.777 -3.421  17.995  0.34 24.50 ?  30  VAL   A CB   1 
ATOM   667  C CG1  A VAL   A 1 30  ? 19.644 -4.813  18.225  0.66 24.61 ?  30  VAL   A CG1  1 
ATOM   668  C CG1  B VAL   A 1 30  ? 19.504 -4.729  18.281  0.34 24.67 ?  30  VAL   A CG1  1 
ATOM   669  C CG2  A VAL   A 1 30  ? 17.375 -3.804  17.908  0.66 24.67 ?  30  VAL   A CG2  1 
ATOM   670  C CG2  B VAL   A 1 30  ? 17.279 -3.654  17.872  0.34 24.74 ?  30  VAL   A CG2  1 
ATOM   671  H H    A VAL   A 1 30  ? 18.329 -1.119  18.001  0.66 29.50 ?  30  VAL   A H    1 
ATOM   672  H H    B VAL   A 1 30  ? 18.366 -0.968  17.910  0.34 29.81 ?  30  VAL   A H    1 
ATOM   673  H HA   A VAL   A 1 30  ? 18.775 -2.874  19.949  0.66 28.35 ?  30  VAL   A HA   1 
ATOM   674  H HA   B VAL   A 1 30  ? 18.679 -2.711  19.916  0.34 29.10 ?  30  VAL   A HA   1 
ATOM   675  H HB   A VAL   A 1 30  ? 19.156 -3.142  17.160  0.66 29.05 ?  30  VAL   A HB   1 
ATOM   676  H HB   B VAL   A 1 30  ? 19.101 -3.083  17.145  0.34 29.38 ?  30  VAL   A HB   1 
ATOM   677  H HG11 A VAL   A 1 30  ? 19.286 -5.499  17.639  0.66 29.51 ?  30  VAL   A HG11 1 
ATOM   678  H HG11 B VAL   A 1 30  ? 19.136 -5.423  17.710  0.34 29.58 ?  30  VAL   A HG11 1 
ATOM   679  H HG12 A VAL   A 1 30  ? 20.580 -4.662  18.021  0.66 29.51 ?  30  VAL   A HG12 1 
ATOM   680  H HG12 B VAL   A 1 30  ? 20.449 -4.616  18.094  0.34 29.58 ?  30  VAL   A HG12 1 
ATOM   681  H HG13 A VAL   A 1 30  ? 19.545 -5.087  19.150  0.66 29.51 ?  30  VAL   A HG13 1 
ATOM   682  H HG13 B VAL   A 1 30  ? 19.374 -4.964  19.212  0.34 29.58 ?  30  VAL   A HG13 1 
ATOM   683  H HG21 A VAL   A 1 30  ? 17.225 -4.474  17.224  0.66 29.58 ?  30  VAL   A HG21 1 
ATOM   684  H HG21 B VAL   A 1 30  ? 17.121 -4.347  17.211  0.34 29.67 ?  30  VAL   A HG21 1 
ATOM   685  H HG22 A VAL   A 1 30  ? 17.061 -4.130  18.766  0.66 29.58 ?  30  VAL   A HG22 1 
ATOM   686  H HG22 B VAL   A 1 30  ? 16.933 -3.934  18.734  0.34 29.67 ?  30  VAL   A HG22 1 
ATOM   687  H HG23 A VAL   A 1 30  ? 16.914 -2.984  17.675  0.66 29.58 ?  30  VAL   A HG23 1 
ATOM   688  H HG23 B VAL   A 1 30  ? 16.854 -2.829  17.595  0.34 29.67 ?  30  VAL   A HG23 1 
ATOM   689  N N    A LYS   A 1 31  ? 21.261 -1.379  18.634  0.66 21.25 ?  31  LYS   A N    1 
ATOM   690  N N    B LYS   A 1 31  ? 21.219 -1.325  18.585  0.34 23.13 ?  31  LYS   A N    1 
ATOM   691  C CA   A LYS   A 1 31  ? 22.711 -1.246  18.573  0.66 21.95 ?  31  LYS   A CA   1 
ATOM   692  C CA   B LYS   A 1 31  ? 22.673 -1.229  18.536  0.34 23.35 ?  31  LYS   A CA   1 
ATOM   693  C C    A LYS   A 1 31  ? 23.345 -2.598  18.239  0.66 19.49 ?  31  LYS   A C    1 
ATOM   694  C C    B LYS   A 1 31  ? 23.292 -2.602  18.254  0.34 20.64 ?  31  LYS   A C    1 
ATOM   695  O O    A LYS   A 1 31  ? 24.140 -3.130  19.023  0.66 20.21 ?  31  LYS   A O    1 
ATOM   696  O O    B LYS   A 1 31  ? 24.023 -3.145  19.088  0.34 21.07 ?  31  LYS   A O    1 
ATOM   697  C CB   A LYS   A 1 31  ? 23.289 -0.676  19.861  0.66 26.52 ?  31  LYS   A CB   1 
ATOM   698  C CB   B LYS   A 1 31  ? 23.250 -0.617  19.804  0.34 26.65 ?  31  LYS   A CB   1 
ATOM   699  C CG   A LYS   A 1 31  ? 22.604 0.584   20.355  0.66 31.32 ?  31  LYS   A CG   1 
ATOM   700  C CG   B LYS   A 1 31  ? 22.574 0.672   20.237  0.34 30.04 ?  31  LYS   A CG   1 
ATOM   701  C CD   A LYS   A 1 31  ? 23.618 1.628   20.795  0.66 34.93 ?  31  LYS   A CD   1 
ATOM   702  C CD   B LYS   A 1 31  ? 23.586 1.677   20.761  0.34 32.71 ?  31  LYS   A CD   1 
ATOM   703  C CE   A LYS   A 1 31  ? 22.989 2.656   21.718  0.66 37.25 ?  31  LYS   A CE   1 
ATOM   704  C CE   B LYS   A 1 31  ? 22.936 2.695   21.683  0.34 34.47 ?  31  LYS   A CE   1 
ATOM   705  N NZ   A LYS   A 1 31  ? 21.765 3.267   21.133  0.66 38.51 ?  31  LYS   A NZ   1 
ATOM   706  N NZ   B LYS   A 1 31  ? 21.709 3.300   21.099  0.34 35.44 ?  31  LYS   A NZ   1 
ATOM   707  H H    A LYS   A 1 31  ? 20.840 -0.789  18.176  0.66 25.47 ?  31  LYS   A H    1 
ATOM   708  H H    B LYS   A 1 31  ? 20.818 -0.742  18.100  0.34 27.73 ?  31  LYS   A H    1 
ATOM   709  H HA   A LYS   A 1 31  ? 22.926 -0.631  17.861  0.66 26.32 ?  31  LYS   A HA   1 
ATOM   710  H HA   B LYS   A 1 31  ? 22.904 -0.644  17.805  0.34 27.99 ?  31  LYS   A HA   1 
ATOM   711  H HB2  A LYS   A 1 31  ? 23.219 -1.344  20.557  0.66 31.81 ?  31  LYS   A HB2  1 
ATOM   712  H HB2  B LYS   A 1 31  ? 23.142 -1.251  20.519  0.34 31.96 ?  31  LYS   A HB2  1 
ATOM   713  H HB3  A LYS   A 1 31  ? 24.225 -0.461  19.708  0.66 31.81 ?  31  LYS   A HB3  1 
ATOM   714  H HB3  B LYS   A 1 31  ? 24.196 -0.430  19.664  0.34 31.96 ?  31  LYS   A HB3  1 
ATOM   715  H HG2  A LYS   A 1 31  ? 22.069 0.962   19.640  0.66 37.56 ?  31  LYS   A HG2  1 
ATOM   716  H HG2  B LYS   A 1 31  ? 22.116 1.065   19.478  0.34 36.02 ?  31  LYS   A HG2  1 
ATOM   717  H HG3  A LYS   A 1 31  ? 22.043 0.367   21.117  0.66 37.56 ?  31  LYS   A HG3  1 
ATOM   718  H HG3  B LYS   A 1 31  ? 21.941 0.477   20.948  0.34 36.02 ?  31  LYS   A HG3  1 
ATOM   719  H HD2  A LYS   A 1 31  ? 24.342 1.192   21.272  0.66 41.89 ?  31  LYS   A HD2  1 
ATOM   720  H HD2  B LYS   A 1 31  ? 24.273 1.209   21.260  0.34 39.23 ?  31  LYS   A HD2  1 
ATOM   721  H HD3  A LYS   A 1 31  ? 23.962 2.090   20.013  0.66 41.89 ?  31  LYS   A HD3  1 
ATOM   722  H HD3  B LYS   A 1 31  ? 23.980 2.152   20.012  0.34 39.23 ?  31  LYS   A HD3  1 
ATOM   723  H HE2  A LYS   A 1 31  ? 22.743 2.225   22.551  0.66 44.68 ?  31  LYS   A HE2  1 
ATOM   724  H HE2  B LYS   A 1 31  ? 22.692 2.256   22.512  0.34 41.34 ?  31  LYS   A HE2  1 
ATOM   725  H HE3  A LYS   A 1 31  ? 23.630 3.365   21.886  0.66 44.68 ?  31  LYS   A HE3  1 
ATOM   726  H HE3  B LYS   A 1 31  ? 23.568 3.409   21.860  0.34 41.34 ?  31  LYS   A HE3  1 
ATOM   727  H HZ1  A LYS   A 1 31  ? 21.446 3.892   21.680  0.66 46.19 ?  31  LYS   A HZ1  1 
ATOM   728  H HZ1  B LYS   A 1 31  ? 21.388 3.924   21.646  0.34 42.51 ?  31  LYS   A HZ1  1 
ATOM   729  H HZ2  A LYS   A 1 31  ? 21.957 3.640   20.348  0.66 46.19 ?  31  LYS   A HZ2  1 
ATOM   730  H HZ2  B LYS   A 1 31  ? 21.898 3.673   20.314  0.34 42.51 ?  31  LYS   A HZ2  1 
ATOM   731  H HZ3  A LYS   A 1 31  ? 21.141 2.644   21.012  0.66 46.19 ?  31  LYS   A HZ3  1 
ATOM   732  H HZ3  B LYS   A 1 31  ? 21.087 2.674   20.979  0.34 42.51 ?  31  LYS   A HZ3  1 
ATOM   733  N N    . PRO   A 1 32  ? 23.014 -3.178  17.090  1.00 18.09 ?  32  PRO   A N    1 
ATOM   734  C CA   . PRO   A 1 32  ? 23.501 -4.523  16.780  1.00 17.87 ?  32  PRO   A CA   1 
ATOM   735  C C    . PRO   A 1 32  ? 25.003 -4.537  16.567  1.00 17.52 ?  32  PRO   A C    1 
ATOM   736  O O    . PRO   A 1 32  ? 25.645 -3.510  16.347  1.00 17.39 ?  32  PRO   A O    1 
ATOM   737  C CB   . PRO   A 1 32  ? 22.773 -4.851  15.476  1.00 18.04 ?  32  PRO   A CB   1 
ATOM   738  C CG   . PRO   A 1 32  ? 22.598 -3.512  14.819  1.00 16.81 ?  32  PRO   A CG   1 
ATOM   739  C CD   . PRO   A 1 32  ? 22.289 -2.581  15.957  1.00 16.80 ?  32  PRO   A CD   1 
ATOM   740  H HA   . PRO   A 1 32  ? 23.255 -5.149  17.473  1.00 21.42 ?  32  PRO   A HA   1 
ATOM   741  H HB2  . PRO   A 1 32  ? 23.320 -5.442  14.930  1.00 21.63 ?  32  PRO   A HB2  1 
ATOM   742  H HB3  . PRO   A 1 32  ? 21.914 -5.262  15.671  1.00 21.63 ?  32  PRO   A HB3  1 
ATOM   743  H HG2  . PRO   A 1 32  ? 23.418 -3.262  14.369  1.00 20.15 ?  32  PRO   A HG2  1 
ATOM   744  H HG3  . PRO   A 1 32  ? 21.858 -3.557  14.189  1.00 20.15 ?  32  PRO   A HG3  1 
ATOM   745  H HD2  . PRO   A 1 32  ? 22.629 -1.695  15.749  1.00 20.14 ?  32  PRO   A HD2  1 
ATOM   746  H HD3  . PRO   A 1 32  ? 21.337 -2.568  16.124  1.00 20.14 ?  32  PRO   A HD3  1 
ATOM   747  N N    . THR   A 1 33  ? 25.558 -5.746  16.593  1.00 17.46 ?  33  THR   A N    1 
ATOM   748  C CA   . THR   A 1 33  ? 26.968 -5.912  16.270  1.00 17.40 ?  33  THR   A CA   1 
ATOM   749  C C    . THR   A 1 33  ? 27.262 -5.451  14.848  1.00 15.87 ?  33  THR   A C    1 
ATOM   750  O O    . THR   A 1 33  ? 28.289 -4.802  14.598  1.00 16.02 ?  33  THR   A O    1 
ATOM   751  C CB   . THR   A 1 33  ? 27.372 -7.373  16.468  1.00 19.33 ?  33  THR   A CB   1 
ATOM   752  O OG1  . THR   A 1 33  ? 27.089 -7.761  17.816  1.00 21.28 ?  33  THR   A OG1  1 
ATOM   753  C CG2  . THR   A 1 33  ? 28.857 -7.574  16.189  1.00 20.07 ?  33  THR   A CG2  1 
ATOM   754  H H    . THR   A 1 33  ? 25.144 -6.475  16.787  1.00 20.93 ?  33  THR   A H    1 
ATOM   755  H HA   . THR   A 1 33  ? 27.499 -5.374  16.878  1.00 20.86 ?  33  THR   A HA   1 
ATOM   756  H HB   . THR   A 1 33  ? 26.869 -7.941  15.861  1.00 23.17 ?  33  THR   A HB   1 
ATOM   757  H HG1  . THR   A 1 33  ? 27.535 -7.291  18.356  1.00 25.51 ?  33  THR   A HG1  1 
ATOM   758  H HG21 . THR   A 1 33  ? 29.134 -8.459  16.473  1.00 24.06 ?  33  THR   A HG21 1 
ATOM   759  H HG22 . THR   A 1 33  ? 29.032 -7.482  15.238  1.00 24.06 ?  33  THR   A HG22 1 
ATOM   760  H HG23 . THR   A 1 33  ? 29.376 -6.912  16.670  1.00 24.06 ?  33  THR   A HG23 1 
ATOM   761  N N    . VAL   A 1 34  ? 26.372 -5.770  13.906  1.00 14.48 ?  34  VAL   A N    1 
ATOM   762  C CA   . VAL   A 1 34  ? 26.561 -5.444  12.496  1.00 13.17 ?  34  VAL   A CA   1 
ATOM   763  C C    . VAL   A 1 34  ? 25.259 -4.895  11.930  1.00 12.74 ?  34  VAL   A C    1 
ATOM   764  O O    . VAL   A 1 34  ? 24.220 -5.567  11.989  1.00 13.52 ?  34  VAL   A O    1 
ATOM   765  C CB   . VAL   A 1 34  ? 27.014 -6.659  11.667  1.00 14.02 ?  34  VAL   A CB   1 
ATOM   766  C CG1  . VAL   A 1 34  ? 27.208 -6.267  10.210  1.00 14.21 ?  34  VAL   A CG1  1 
ATOM   767  C CG2  . VAL   A 1 34  ? 28.289 -7.272  12.244  1.00 15.32 ?  34  VAL   A CG2  1 
ATOM   768  H H    . VAL   A 1 34  ? 25.637 -6.193  14.068  1.00 17.36 ?  34  VAL   A H    1 
ATOM   769  H HA   . VAL   A 1 34  ? 27.237 -4.752  12.422  1.00 15.78 ?  34  VAL   A HA   1 
ATOM   770  H HB   . VAL   A 1 34  ? 26.319 -7.333  11.705  1.00 16.80 ?  34  VAL   A HB   1 
ATOM   771  H HG11 . VAL   A 1 34  ? 27.687 -6.979  9.757   1.00 17.03 ?  34  VAL   A HG11 1 
ATOM   772  H HG12 . VAL   A 1 34  ? 26.343 -6.136  9.797   1.00 17.03 ?  34  VAL   A HG12 1 
ATOM   773  H HG13 . VAL   A 1 34  ? 27.726 -5.446  10.170  1.00 17.03 ?  34  VAL   A HG13 1 
ATOM   774  H HG21 . VAL   A 1 34  ? 28.582 -7.995  11.666  1.00 18.36 ?  34  VAL   A HG21 1 
ATOM   775  H HG22 . VAL   A 1 34  ? 28.977 -6.590  12.294  1.00 18.36 ?  34  VAL   A HG22 1 
ATOM   776  H HG23 . VAL   A 1 34  ? 28.103 -7.618  13.133  1.00 18.36 ?  34  VAL   A HG23 1 
ATOM   777  N N    . VAL   A 1 35  ? 25.321 -3.690  11.363  1.00 12.13 ?  35  VAL   A N    1 
ATOM   778  C CA   . VAL   A 1 35  ? 24.281 -3.184  10.477  1.00 11.71 ?  35  VAL   A CA   1 
ATOM   779  C C    . VAL   A 1 35  ? 24.832 -3.192  9.058   1.00 11.10 ?  35  VAL   A C    1 
ATOM   780  O O    . VAL   A 1 35  ? 25.973 -2.778  8.822   1.00 11.80 ?  35  VAL   A O    1 
ATOM   781  C CB   . VAL   A 1 35  ? 23.748 -1.789  10.882  1.00 12.53 ?  35  VAL   A CB   1 
ATOM   782  C CG1  . VAL   A 1 35  ? 24.813 -0.697  10.741  1.00 13.20 ?  35  VAL   A CG1  1 
ATOM   783  C CG2  . VAL   A 1 35  ? 22.504 -1.436  10.063  1.00 13.29 ?  35  VAL   A CG2  1 
ATOM   784  H H    . VAL   A 1 35  ? 25.970 -3.139  11.471  1.00 14.53 ?  35  VAL   A H    1 
ATOM   785  H HA   . VAL   A 1 35  ? 23.526 -3.797  10.501  1.00 14.03 ?  35  VAL   A HA   1 
ATOM   786  H HB   . VAL   A 1 35  ? 23.478 -1.817  11.809  1.00 15.01 ?  35  VAL   A HB   1 
ATOM   787  H HG11 . VAL   A 1 35  ? 24.468 0.132   11.112  1.00 15.81 ?  35  VAL   A HG11 1 
ATOM   788  H HG12 . VAL   A 1 35  ? 25.608 -0.970  11.224  1.00 15.81 ?  35  VAL   A HG12 1 
ATOM   789  H HG13 . VAL   A 1 35  ? 25.023 -0.573  9.801   1.00 15.81 ?  35  VAL   A HG13 1 
ATOM   790  H HG21 . VAL   A 1 35  ? 22.153 -0.587  10.367  1.00 15.93 ?  35  VAL   A HG21 1 
ATOM   791  H HG22 . VAL   A 1 35  ? 22.747 -1.376  9.123   1.00 15.93 ?  35  VAL   A HG22 1 
ATOM   792  H HG23 . VAL   A 1 35  ? 21.838 -2.133  10.184  1.00 15.93 ?  35  VAL   A HG23 1 
ATOM   793  N N    . VAL   A 1 36  ? 24.016 -3.652  8.112   1.00 10.86 ?  36  VAL   A N    1 
ATOM   794  C CA   . VAL   A 1 36  ? 24.389 -3.659  6.703   1.00 10.64 ?  36  VAL   A CA   1 
ATOM   795  C C    . VAL   A 1 36  ? 23.925 -2.371  6.042   1.00 10.71 ?  36  VAL   A C    1 
ATOM   796  O O    . VAL   A 1 36  ? 22.763 -1.970  6.193   1.00 11.31 ?  36  VAL   A O    1 
ATOM   797  C CB   . VAL   A 1 36  ? 23.790 -4.879  5.988   1.00 10.45 ?  36  VAL   A CB   1 
ATOM   798  C CG1  . VAL   A 1 36  ? 24.054 -4.811  4.504   1.00 11.12 ?  36  VAL   A CG1  1 
ATOM   799  C CG2  . VAL   A 1 36  ? 24.344 -6.160  6.564   1.00 11.44 ?  36  VAL   A CG2  1 
ATOM   800  H H    . VAL   A 1 36  ? 23.225 -3.963  8.263   1.00 13.01 ?  36  VAL   A H    1 
ATOM   801  H HA   . VAL   A 1 36  ? 25.358 -3.715  6.632   1.00 12.74 ?  36  VAL   A HA   1 
ATOM   802  H HB   . VAL   A 1 36  ? 22.831 -4.881  6.121   1.00 12.51 ?  36  VAL   A HB   1 
ATOM   803  H HG11 . VAL   A 1 36  ? 23.918 -5.691  4.119   1.00 13.33 ?  36  VAL   A HG11 1 
ATOM   804  H HG12 . VAL   A 1 36  ? 23.444 -4.176  4.098   1.00 13.33 ?  36  VAL   A HG12 1 
ATOM   805  H HG13 . VAL   A 1 36  ? 24.973 -4.529  4.359   1.00 13.33 ?  36  VAL   A HG13 1 
ATOM   806  H HG21 . VAL   A 1 36  ? 23.956 -6.917  6.092   1.00 13.70 ?  36  VAL   A HG21 1 
ATOM   807  H HG22 . VAL   A 1 36  ? 25.309 -6.168  6.458   1.00 13.70 ?  36  VAL   A HG22 1 
ATOM   808  H HG23 . VAL   A 1 36  ? 24.117 -6.214  7.507   1.00 13.70 ?  36  VAL   A HG23 1 
ATOM   809  N N    . ASN   A 1 37  ? 24.832 -1.738  5.293   1.00 10.13 ?  37  ASN   A N    1 
ATOM   810  C CA   . ASN   A 1 37  ? 24.498 -0.616  4.429   1.00 9.95  ?  37  ASN   A CA   1 
ATOM   811  C C    . ASN   A 1 37  ? 24.366 -1.088  2.990   1.00 9.89  ?  37  ASN   A C    1 
ATOM   812  O O    . ASN   A 1 37  ? 25.159 -1.915  2.517   1.00 10.37 ?  37  ASN   A O    1 
ATOM   813  C CB   . ASN   A 1 37  ? 25.571 0.470   4.509   1.00 9.96  ?  37  ASN   A CB   1 
ATOM   814  C CG   . ASN   A 1 37  ? 25.247 1.662   3.653   1.00 10.60 ?  37  ASN   A CG   1 
ATOM   815  O OD1  . ASN   A 1 37  ? 24.066 1.987   3.465   1.00 11.14 ?  37  ASN   A OD1  1 
ATOM   816  N ND2  . ASN   A 1 37  ? 26.276 2.320   3.128   1.00 10.77 ?  37  ASN   A ND2  1 
ATOM   817  H H    . ASN   A 1 37  ? 25.670 -1.947  5.277   1.00 12.14 ?  37  ASN   A H    1 
ATOM   818  H HA   . ASN   A 1 37  ? 23.656 -0.235  4.708   1.00 11.92 ?  37  ASN   A HA   1 
ATOM   819  H HB2  . ASN   A 1 37  ? 25.649 0.772   5.430   1.00 11.93 ?  37  ASN   A HB2  1 
ATOM   820  H HB3  . ASN   A 1 37  ? 26.422 0.104   4.211   1.00 11.93 ?  37  ASN   A HB3  1 
ATOM   821  H HD21 . ASN   A 1 37  ? 26.135 3.004   2.626   1.00 12.91 ?  37  ASN   A HD21 1 
ATOM   822  H HD22 . ASN   A 1 37  ? 27.075 2.060   3.277   1.00 12.91 ?  37  ASN   A HD22 1 
ATOM   823  N N    A ALA   A 1 38  ? 23.349 -0.549  2.310   0.66 10.48 ?  38  ALA   A N    1 
ATOM   824  N N    B ALA   A 1 38  ? 23.344 -0.594  2.295   0.34 10.54 ?  38  ALA   A N    1 
ATOM   825  C CA   A ALA   A 1 38  ? 23.157 -0.674  0.865   0.66 10.39 ?  38  ALA   A CA   1 
ATOM   826  C CA   B ALA   A 1 38  ? 23.185 -0.883  0.869   0.34 11.12 ?  38  ALA   A CA   1 
ATOM   827  C C    A ALA   A 1 38  ? 24.078 0.328   0.171   0.66 10.23 ?  38  ALA   A C    1 
ATOM   828  C C    B ALA   A 1 38  ? 23.960 0.175   0.093   0.34 11.14 ?  38  ALA   A C    1 
ATOM   829  O O    A ALA   A 1 38  ? 23.680 1.425   -0.227  0.66 10.13 ?  38  ALA   A O    1 
ATOM   830  O O    B ALA   A 1 38  ? 23.421 1.205   -0.316  0.34 11.34 ?  38  ALA   A O    1 
ATOM   831  C CB   A ALA   A 1 38  ? 21.698 -0.414  0.512   0.66 11.33 ?  38  ALA   A CB   1 
ATOM   832  C CB   B ALA   A 1 38  ? 21.713 -0.921  0.482   0.34 11.81 ?  38  ALA   A CB   1 
ATOM   833  H H    A ALA   A 1 38  ? 22.740 -0.075  2.685   0.66 12.55 ?  38  ALA   A H    1 
ATOM   834  H H    B ALA   A 1 38  ? 22.729 -0.093  2.629   0.34 12.63 ?  38  ALA   A H    1 
ATOM   835  H HA   A ALA   A 1 38  ? 23.393 -1.567  0.577   0.66 12.45 ?  38  ALA   A HA   1 
ATOM   836  H HA   B ALA   A 1 38  ? 23.572 -1.753  0.673   0.34 13.32 ?  38  ALA   A HA   1 
ATOM   837  H HB1  A ALA   A 1 38  ? 21.580 -0.509  -0.446  0.66 13.57 ?  38  ALA   A HB1  1 
ATOM   838  H HB1  B ALA   A 1 38  ? 21.644 -1.117  -0.466  0.34 14.14 ?  38  ALA   A HB1  1 
ATOM   839  H HB2  A ALA   A 1 38  ? 21.140 -1.057  0.979   0.66 13.57 ?  38  ALA   A HB2  1 
ATOM   840  H HB2  B ALA   A 1 38  ? 21.266 -1.613  0.996   0.34 14.14 ?  38  ALA   A HB2  1 
ATOM   841  H HB3  A ALA   A 1 38  ? 21.460 0.487   0.785   0.66 13.57 ?  38  ALA   A HB3  1 
ATOM   842  H HB3  B ALA   A 1 38  ? 21.316 -0.058  0.672   0.34 14.14 ?  38  ALA   A HB3  1 
ATOM   843  N N    A ALA   A 1 39  ? 25.341 -0.065  0.025   0.66 10.42 ?  39  ALA   A N    1 
ATOM   844  N N    B ALA   A 1 39  ? 25.244 -0.091  -0.121  0.34 11.36 ?  39  ALA   A N    1 
ATOM   845  C CA   A ALA   A 1 39  ? 26.397 0.814   -0.450  0.66 9.93  ?  39  ALA   A CA   1 
ATOM   846  C CA   B ALA   A 1 39  ? 26.175 0.900   -0.636  0.34 11.31 ?  39  ALA   A CA   1 
ATOM   847  C C    A ALA   A 1 39  ? 26.528 0.771   -1.971  0.66 10.03 ?  39  ALA   A C    1 
ATOM   848  C C    B ALA   A 1 39  ? 26.339 0.774   -2.147  0.34 10.93 ?  39  ALA   A C    1 
ATOM   849  O O    A ALA   A 1 39  ? 26.039 -0.141  -2.640  0.66 10.87 ?  39  ALA   A O    1 
ATOM   850  O O    B ALA   A 1 39  ? 25.950 -0.217  -2.770  0.34 11.77 ?  39  ALA   A O    1 
ATOM   851  C CB   A ALA   A 1 39  ? 27.724 0.404   0.191   0.66 10.14 ?  39  ALA   A CB   1 
ATOM   852  C CB   B ALA   A 1 39  ? 27.532 0.746   0.054   0.34 11.97 ?  39  ALA   A CB   1 
ATOM   853  H H    A ALA   A 1 39  ? 25.615 -0.864  0.200   0.66 12.48 ?  39  ALA   A H    1 
ATOM   854  H H    B ALA   A 1 39  ? 25.599 -0.863  0.029   0.34 13.61 ?  39  ALA   A H    1 
ATOM   855  H HA   A ALA   A 1 39  ? 26.196 1.727   -0.189  0.66 11.89 ?  39  ALA   A HA   1 
ATOM   856  H HA   B ALA   A 1 39  ? 25.830 1.782   -0.432  0.34 13.54 ?  39  ALA   A HA   1 
ATOM   857  H HB1  A ALA   A 1 39  ? 28.421 1.000   -0.128  0.66 12.14 ?  39  ALA   A HB1  1 
ATOM   858  H HB1  B ALA   A 1 39  ? 28.138 1.414   -0.301  0.34 14.34 ?  39  ALA   A HB1  1 
ATOM   859  H HB2  A ALA   A 1 39  ? 27.641 0.483   1.156   0.66 12.14 ?  39  ALA   A HB2  1 
ATOM   860  H HB2  B ALA   A 1 39  ? 27.420 0.876   1.010   0.34 14.34 ?  39  ALA   A HB2  1 
ATOM   861  H HB3  A ALA   A 1 39  ? 27.924 -0.507  -0.055  0.66 12.14 ?  39  ALA   A HB3  1 
ATOM   862  H HB3  B ALA   A 1 39  ? 27.877 -0.143  -0.120  0.34 14.34 ?  39  ALA   A HB3  1 
ATOM   863  N N    A ASN   A 1 40  ? 27.223 1.777   -2.509  0.66 9.97  ?  40  ASN   A N    1 
ATOM   864  N N    B ASN   A 1 40  ? 26.920 1.814   -2.736  0.34 10.42 ?  40  ASN   A N    1 
ATOM   865  C CA   A ASN   A 1 40  ? 27.770 1.736   -3.862  0.66 10.06 ?  40  ASN   A CA   1 
ATOM   866  C CA   B ASN   A 1 40  ? 27.450 1.750   -4.089  0.34 10.25 ?  40  ASN   A CA   1 
ATOM   867  C C    A ASN   A 1 40  ? 29.293 1.618   -3.788  0.66 9.45  ?  40  ASN   A C    1 
ATOM   868  C C    B ASN   A 1 40  ? 28.972 1.624   -4.032  0.34 9.64  ?  40  ASN   A C    1 
ATOM   869  O O    A ASN   A 1 40  ? 29.887 1.714   -2.711  0.66 9.88  ?  40  ASN   A O    1 
ATOM   870  O O    B ASN   A 1 40  ? 29.592 1.738   -2.974  0.34 9.60  ?  40  ASN   A O    1 
ATOM   871  C CB   A ASN   A 1 40  ? 27.295 2.922   -4.723  0.66 11.18 ?  40  ASN   A CB   1 
ATOM   872  C CB   B ASN   A 1 40  ? 27.024 2.973   -4.907  0.34 10.67 ?  40  ASN   A CB   1 
ATOM   873  C CG   A ASN   A 1 40  ? 27.670 4.269   -4.146  0.66 12.12 ?  40  ASN   A CG   1 
ATOM   874  C CG   B ASN   A 1 40  ? 27.403 4.278   -4.249  0.34 10.74 ?  40  ASN   A CG   1 
ATOM   875  O OD1  A ASN   A 1 40  ? 28.836 4.519   -3.816  0.66 12.45 ?  40  ASN   A OD1  1 
ATOM   876  O OD1  B ASN   A 1 40  ? 28.586 4.578   -4.072  0.34 11.44 ?  40  ASN   A OD1  1 
ATOM   877  N ND2  A ASN   A 1 40  ? 26.679 5.156   -4.033  0.66 13.10 ?  40  ASN   A ND2  1 
ATOM   878  N ND2  B ASN   A 1 40  ? 26.398 5.072   -3.893  0.34 10.97 ?  40  ASN   A ND2  1 
ATOM   879  H H    A ASN   A 1 40  ? 27.399 2.509   -2.101  0.66 11.95 ?  40  ASN   A H    1 
ATOM   880  H H    B ASN   A 1 40  ? 27.014 2.578   -2.356  0.34 12.48 ?  40  ASN   A H    1 
ATOM   881  H HA   A ASN   A 1 40  ? 27.450 0.930   -4.295  0.66 12.05 ?  40  ASN   A HA   1 
ATOM   882  H HA   B ASN   A 1 40  ? 27.087 0.953   -4.523  0.34 12.27 ?  40  ASN   A HA   1 
ATOM   883  H HB2  A ASN   A 1 40  ? 27.691 2.846   -5.612  0.66 13.40 ?  40  ASN   A HB2  1 
ATOM   884  H HB2  B ASN   A 1 40  ? 27.460 2.930   -5.767  0.34 12.79 ?  40  ASN   A HB2  1 
ATOM   885  H HB3  A ASN   A 1 40  ? 26.327 2.885   -4.800  0.66 13.40 ?  40  ASN   A HB3  1 
ATOM   886  H HB3  B ASN   A 1 40  ? 26.061 2.951   -5.020  0.34 12.79 ?  40  ASN   A HB3  1 
ATOM   887  H HD21 A ASN   A 1 40  ? 26.837 5.943   -3.723  0.66 15.70 ?  40  ASN   A HD21 1 
ATOM   888  H HD21 B ASN   A 1 40  ? 26.561 5.825   -3.513  0.34 13.15 ?  40  ASN   A HD21 1 
ATOM   889  H HD22 A ASN   A 1 40  ? 25.878 4.942   -4.267  0.66 15.70 ?  40  ASN   A HD22 1 
ATOM   890  H HD22 B ASN   A 1 40  ? 25.584 4.831   -4.040  0.34 13.15 ?  40  ASN   A HD22 1 
ATOM   891  N N    A VAL   A 1 41  ? 29.922 1.368   -4.944  0.66 9.89  ?  41  VAL   A N    1 
ATOM   892  N N    B VAL   A 1 41  ? 29.577 1.383   -5.197  0.34 9.93  ?  41  VAL   A N    1 
ATOM   893  C CA   A VAL   A 1 41  ? 31.348 1.049   -4.952  0.66 10.71 ?  41  VAL   A CA   1 
ATOM   894  C CA   B VAL   A 1 41  ? 31.004 1.074   -5.241  0.34 9.85  ?  41  VAL   A CA   1 
ATOM   895  C C    A VAL   A 1 41  ? 32.200 2.203   -4.460  0.66 10.21 ?  41  VAL   A C    1 
ATOM   896  C C    B VAL   A 1 41  ? 31.876 2.226   -4.764  0.34 10.01 ?  41  VAL   A C    1 
ATOM   897  O O    A VAL   A 1 41  ? 33.321 1.982   -3.988  0.66 10.39 ?  41  VAL   A O    1 
ATOM   898  O O    B VAL   A 1 41  ? 33.054 2.015   -4.450  0.34 9.77  ?  41  VAL   A O    1 
ATOM   899  C CB   A VAL   A 1 41  ? 31.861 0.541   -6.326  0.66 11.16 ?  41  VAL   A CB   1 
ATOM   900  C CB   B VAL   A 1 41  ? 31.443 0.634   -6.651  0.34 10.27 ?  41  VAL   A CB   1 
ATOM   901  C CG1  A VAL   A 1 41  ? 31.133 -0.729  -6.749  0.66 11.80 ?  41  VAL   A CG1  1 
ATOM   902  C CG1  B VAL   A 1 41  ? 30.749 -0.656  -7.047  0.34 11.61 ?  41  VAL   A CG1  1 
ATOM   903  C CG2  A VAL   A 1 41  ? 31.781 1.615   -7.410  0.66 11.25 ?  41  VAL   A CG2  1 
ATOM   904  C CG2  B VAL   A 1 41  ? 31.181 1.734   -7.669  0.34 10.06 ?  41  VAL   A CG2  1 
ATOM   905  H H    A VAL   A 1 41  ? 29.555 1.369   -5.723  0.66 11.85 ?  41  VAL   A H    1 
ATOM   906  H H    B VAL   A 1 41  ? 29.176 1.382   -5.953  0.34 11.89 ?  41  VAL   A H    1 
ATOM   907  H HA   A VAL   A 1 41  ? 31.495 0.326   -4.329  0.66 12.82 ?  41  VAL   A HA   1 
ATOM   908  H HA   B VAL   A 1 41  ? 31.156 0.322   -4.646  0.34 11.80 ?  41  VAL   A HA   1 
ATOM   909  H HB   A VAL   A 1 41  ? 32.800 0.302   -6.230  0.66 13.37 ?  41  VAL   A HB   1 
ATOM   910  H HB   B VAL   A 1 41  ? 32.396 0.466   -6.632  0.34 12.30 ?  41  VAL   A HB   1 
ATOM   911  H HG11 A VAL   A 1 41  ? 31.482 -1.032  -7.603  0.66 14.14 ?  41  VAL   A HG11 1 
ATOM   912  H HG11 B VAL   A 1 41  ? 30.998 -0.876  -7.956  0.34 13.91 ?  41  VAL   A HG11 1 
ATOM   913  H HG12 A VAL   A 1 41  ? 31.265 -1.415  -6.076  0.66 14.14 ?  41  VAL   A HG12 1 
ATOM   914  H HG12 B VAL   A 1 41  ? 31.031 -1.362  -6.444  0.34 13.91 ?  41  VAL   A HG12 1 
ATOM   915  H HG13 A VAL   A 1 41  ? 30.183 -0.532  -6.835  0.66 14.14 ?  41  VAL   A HG13 1 
ATOM   916  H HG13 B VAL   A 1 41  ? 29.790 -0.534  -6.985  0.34 13.91 ?  41  VAL   A HG13 1 
ATOM   917  H HG21 A VAL   A 1 41  ? 32.013 1.213   -8.267  0.66 13.48 ?  41  VAL   A HG21 1 
ATOM   918  H HG21 B VAL   A 1 41  ? 31.454 1.420   -8.544  0.34 12.05 ?  41  VAL   A HG21 1 
ATOM   919  H HG22 A VAL   A 1 41  ? 30.889 1.969   -7.437  0.66 13.48 ?  41  VAL   A HG22 1 
ATOM   920  H HG22 B VAL   A 1 41  ? 30.232 1.942   -7.675  0.34 12.05 ?  41  VAL   A HG22 1 
ATOM   921  H HG23 A VAL   A 1 41  ? 32.420 2.317   -7.200  0.66 13.48 ?  41  VAL   A HG23 1 
ATOM   922  H HG23 B VAL   A 1 41  ? 31.690 2.522   -7.425  0.34 12.05 ?  41  VAL   A HG23 1 
ATOM   923  N N    A TYR   A 1 42  ? 31.710 3.436   -4.575  0.66 10.63 ?  42  TYR   A N    1 
ATOM   924  N N    B TYR   A 1 42  ? 31.346 3.448   -4.737  0.34 10.13 ?  42  TYR   A N    1 
ATOM   925  C CA   A TYR   A 1 42  ? 32.450 4.619   -4.148  0.66 11.10 ?  42  TYR   A CA   1 
ATOM   926  C CA   B TYR   A 1 42  ? 32.110 4.621   -4.329  0.34 9.92  ?  42  TYR   A CA   1 
ATOM   927  C C    A TYR   A 1 42  ? 32.164 4.994   -2.704  0.66 10.73 ?  42  TYR   A C    1 
ATOM   928  C C    B TYR   A 1 42  ? 31.890 5.005   -2.874  0.34 10.40 ?  42  TYR   A C    1 
ATOM   929  O O    A TYR   A 1 42  ? 32.734 5.972   -2.202  0.66 11.06 ?  42  TYR   A O    1 
ATOM   930  O O    B TYR   A 1 42  ? 32.454 6.007   -2.423  0.34 10.77 ?  42  TYR   A O    1 
ATOM   931  C CB   A TYR   A 1 42  ? 32.141 5.814   -5.071  0.66 11.87 ?  42  TYR   A CB   1 
ATOM   932  C CB   B TYR   A 1 42  ? 31.766 5.815   -5.224  0.34 10.08 ?  42  TYR   A CB   1 
ATOM   933  C CG   A TYR   A 1 42  ? 32.325 5.493   -6.539  0.66 12.04 ?  42  TYR   A CG   1 
ATOM   934  C CG   B TYR   A 1 42  ? 31.930 5.523   -6.693  0.34 10.64 ?  42  TYR   A CG   1 
ATOM   935  C CD1  A TYR   A 1 42  ? 33.591 5.276   -7.066  0.66 12.70 ?  42  TYR   A CD1  1 
ATOM   936  C CD1  B TYR   A 1 42  ? 33.189 5.349   -7.250  0.34 10.62 ?  42  TYR   A CD1  1 
ATOM   937  C CD2  A TYR   A 1 42  ? 31.234 5.371   -7.391  0.66 13.14 ?  42  TYR   A CD2  1 
ATOM   938  C CD2  B TYR   A 1 42  ? 30.823 5.410   -7.523  0.34 11.88 ?  42  TYR   A CD2  1 
ATOM   939  C CE1  A TYR   A 1 42  ? 33.770 4.961   -8.402  0.66 13.40 ?  42  TYR   A CE1  1 
ATOM   940  C CE1  B TYR   A 1 42  ? 33.340 5.072   -8.594  0.34 10.91 ?  42  TYR   A CE1  1 
ATOM   941  C CE2  A TYR   A 1 42  ? 31.408 5.065   -8.734  0.66 14.04 ?  42  TYR   A CE2  1 
ATOM   942  C CE2  B TYR   A 1 42  ? 30.964 5.146   -8.868  0.34 12.64 ?  42  TYR   A CE2  1 
ATOM   943  C CZ   A TYR   A 1 42  ? 32.682 4.859   -9.230  0.66 13.82 ?  42  TYR   A CZ   1 
ATOM   944  C CZ   B TYR   A 1 42  ? 32.223 4.975   -9.400  0.34 11.80 ?  42  TYR   A CZ   1 
ATOM   945  O OH   A TYR   A 1 42  ? 32.873 4.545   -10.556 0.66 15.07 ?  42  TYR   A OH   1 
ATOM   946  O OH   B TYR   A 1 42  ? 32.366 4.710   -10.741 0.34 12.40 ?  42  TYR   A OH   1 
ATOM   947  H H    A TYR   A 1 42  ? 30.934 3.616   -4.896  0.66 12.73 ?  42  TYR   A H    1 
ATOM   948  H H    B TYR   A 1 42  ? 30.534 3.629   -4.967  0.34 12.14 ?  42  TYR   A H    1 
ATOM   949  H HA   A TYR   A 1 42  ? 33.399 4.439   -4.215  0.66 13.30 ?  42  TYR   A HA   1 
ATOM   950  H HA   B TYR   A 1 42  ? 33.051 4.430   -4.442  0.34 11.88 ?  42  TYR   A HA   1 
ATOM   951  H HB2  A TYR   A 1 42  ? 31.223 6.092   -4.935  0.66 14.22 ?  42  TYR   A HB2  1 
ATOM   952  H HB2  B TYR   A 1 42  ? 30.842 6.070   -5.070  0.34 12.07 ?  42  TYR   A HB2  1 
ATOM   953  H HB3  A TYR   A 1 42  ? 32.743 6.548   -4.847  0.66 14.22 ?  42  TYR   A HB3  1 
ATOM   954  H HB3  B TYR   A 1 42  ? 32.353 6.555   -4.999  0.34 12.07 ?  42  TYR   A HB3  1 
ATOM   955  H HD1  A TYR   A 1 42  ? 34.337 5.343   -6.513  0.66 15.22 ?  42  TYR   A HD1  1 
ATOM   956  H HD1  B TYR   A 1 42  ? 33.942 5.413   -6.705  0.34 12.73 ?  42  TYR   A HD1  1 
ATOM   957  H HD2  A TYR   A 1 42  ? 30.378 5.516   -7.058  0.66 15.74 ?  42  TYR   A HD2  1 
ATOM   958  H HD2  B TYR   A 1 42  ? 29.971 5.529   -7.166  0.34 14.23 ?  42  TYR   A HD2  1 
ATOM   959  H HE1  A TYR   A 1 42  ? 34.626 4.824   -8.745  0.66 16.05 ?  42  TYR   A HE1  1 
ATOM   960  H HE1  B TYR   A 1 42  ? 34.191 4.957   -8.951  0.34 13.07 ?  42  TYR   A HE1  1 
ATOM   961  H HE2  A TYR   A 1 42  ? 30.666 4.996   -9.296  0.66 16.82 ?  42  TYR   A HE2  1 
ATOM   962  H HE2  B TYR   A 1 42  ? 30.213 5.076   -9.410  0.34 15.15 ?  42  TYR   A HE2  1 
ATOM   963  H HH   A TYR   A 1 42  ? 33.684 4.395   -10.706 0.66 18.06 ?  42  TYR   A HH   1 
ATOM   964  H HH   B TYR   A 1 42  ? 31.615 4.672   -11.105 0.34 14.85 ?  42  TYR   A HH   1 
ATOM   965  N N    A LEU   A 1 43  ? 31.288 4.243   -2.035  0.66 10.46 ?  43  LEU   A N    1 
ATOM   966  N N    B LEU   A 1 43  ? 31.079 4.243   -2.138  0.34 10.57 ?  43  LEU   A N    1 
ATOM   967  C CA   A LEU   A 1 43  ? 30.828 4.576   -0.689  0.66 10.08 ?  43  LEU   A CA   1 
ATOM   968  C CA   B LEU   A 1 43  ? 30.673 4.590   -0.774  0.34 10.63 ?  43  LEU   A CA   1 
ATOM   969  C C    A LEU   A 1 43  ? 30.353 6.027   -0.602  0.66 10.15 ?  43  LEU   A C    1 
ATOM   970  C C    B LEU   A 1 43  ? 30.190 6.036   -0.678  0.34 10.81 ?  43  LEU   A C    1 
ATOM   971  O O    A LEU   A 1 43  ? 30.626 6.736   0.370   0.66 11.68 ?  43  LEU   A O    1 
ATOM   972  O O    B LEU   A 1 43  ? 30.430 6.732   0.310   0.34 10.94 ?  43  LEU   A O    1 
ATOM   973  C CB   A LEU   A 1 43  ? 31.879 4.264   0.374   0.66 10.84 ?  43  LEU   A CB   1 
ATOM   974  C CB   B LEU   A 1 43  ? 31.762 4.287   0.256   0.34 10.65 ?  43  LEU   A CB   1 
ATOM   975  C CG   A LEU   A 1 43  ? 32.406 2.829   0.449   0.66 11.04 ?  43  LEU   A CG   1 
ATOM   976  C CG   B LEU   A 1 43  ? 32.184 2.820   0.385   0.34 10.83 ?  43  LEU   A CG   1 
ATOM   977  C CD1  A LEU   A 1 43  ? 33.469 2.739   1.530   0.66 11.81 ?  43  LEU   A CD1  1 
ATOM   978  C CD1  B LEU   A 1 43  ? 33.224 2.675   1.485   0.34 11.40 ?  43  LEU   A CD1  1 
ATOM   979  C CD2  A LEU   A 1 43  ? 31.289 1.821   0.701   0.66 11.08 ?  43  LEU   A CD2  1 
ATOM   980  C CD2  B LEU   A 1 43  ? 30.987 1.898   0.634   0.34 10.68 ?  43  LEU   A CD2  1 
ATOM   981  H H    A LEU   A 1 43  ? 30.934 3.516   -2.346  0.66 12.52 ?  43  LEU   A H    1 
ATOM   982  H H    B LEU   A 1 43  ? 30.739 3.506   -2.411  0.34 12.66 ?  43  LEU   A H    1 
ATOM   983  H HA   A LEU   A 1 43  ? 30.058 4.014   -0.492  0.66 12.07 ?  43  LEU   A HA   1 
ATOM   984  H HA   B LEU   A 1 43  ? 29.913 4.033   -0.546  0.34 12.73 ?  43  LEU   A HA   1 
ATOM   985  H HB2  A LEU   A 1 43  ? 32.642 4.841   0.221   0.66 12.99 ?  43  LEU   A HB2  1 
ATOM   986  H HB2  B LEU   A 1 43  ? 32.552 4.797   0.026   0.34 12.76 ?  43  LEU   A HB2  1 
ATOM   987  H HB3  A LEU   A 1 43  ? 31.494 4.466   1.242   0.66 12.99 ?  43  LEU   A HB3  1 
ATOM   988  H HB3  B LEU   A 1 43  ? 31.441 4.569   1.130   0.34 12.76 ?  43  LEU   A HB3  1 
ATOM   989  H HG   A LEU   A 1 43  ? 32.825 2.604   -0.397  0.66 13.22 ?  43  LEU   A HG   1 
ATOM   990  H HG   B LEU   A 1 43  ? 32.598 2.547   -0.447  0.34 12.97 ?  43  LEU   A HG   1 
ATOM   991  H HD11 A LEU   A 1 43  ? 33.799 1.829   1.572   0.66 14.14 ?  43  LEU   A HD11 1 
ATOM   992  H HD11 B LEU   A 1 43  ? 33.483 1.743   1.552   0.34 13.65 ?  43  LEU   A HD11 1 
ATOM   993  H HD12 A LEU   A 1 43  ? 34.193 3.346   1.312   0.66 14.14 ?  43  LEU   A HD12 1 
ATOM   994  H HD12 B LEU   A 1 43  ? 33.996 3.218   1.263   0.34 13.65 ?  43  LEU   A HD12 1 
ATOM   995  H HD13 A LEU   A 1 43  ? 33.073 2.989   2.380   0.66 14.14 ?  43  LEU   A HD13 1 
ATOM   996  H HD13 B LEU   A 1 43  ? 32.840 2.973   2.324   0.34 13.65 ?  43  LEU   A HD13 1 
ATOM   997  H HD21 A LEU   A 1 43  ? 31.679 0.940   0.806   0.66 13.27 ?  43  LEU   A HD21 1 
ATOM   998  H HD21 B LEU   A 1 43  ? 31.312 1.015   0.863   0.34 12.79 ?  43  LEU   A HD21 1 
ATOM   999  H HD22 A LEU   A 1 43  ? 30.817 2.074   1.509   0.66 13.27 ?  43  LEU   A HD22 1 
ATOM   1000 H HD22 B LEU   A 1 43  ? 30.458 2.257   1.363   0.34 12.79 ?  43  LEU   A HD22 1 
ATOM   1001 H HD23 A LEU   A 1 43  ? 30.683 1.830   -0.055  0.66 13.27 ?  43  LEU   A HD23 1 
ATOM   1002 H HD23 B LEU   A 1 43  ? 30.449 1.855   -0.173  0.34 12.79 ?  43  LEU   A HD23 1 
ATOM   1003 N N    A LYS   A 1 44  ? 29.630 6.471   -1.634  0.66 10.42 ?  44  LYS   A N    1 
ATOM   1004 N N    B LYS   A 1 44  ? 29.480 6.484   -1.711  0.34 11.20 ?  44  LYS   A N    1 
ATOM   1005 C CA   A LYS   A 1 44  ? 28.985 7.782   -1.630  0.66 10.86 ?  44  LYS   A CA   1 
ATOM   1006 C CA   B LYS   A 1 44  ? 28.819 7.788   -1.700  0.34 11.90 ?  44  LYS   A CA   1 
ATOM   1007 C C    A LYS   A 1 44  ? 27.553 7.599   -1.141  0.66 10.29 ?  44  LYS   A C    1 
ATOM   1008 C C    B LYS   A 1 44  ? 27.411 7.584   -1.158  0.34 11.34 ?  44  LYS   A C    1 
ATOM   1009 O O    A LYS   A 1 44  ? 26.699 7.076   -1.865  0.66 11.56 ?  44  LYS   A O    1 
ATOM   1010 O O    B LYS   A 1 44  ? 26.520 7.104   -1.863  0.34 11.60 ?  44  LYS   A O    1 
ATOM   1011 C CB   A LYS   A 1 44  ? 29.035 8.413   -3.017  0.66 12.86 ?  44  LYS   A CB   1 
ATOM   1012 C CB   B LYS   A 1 44  ? 28.813 8.401   -3.096  0.34 14.32 ?  44  LYS   A CB   1 
ATOM   1013 C CG   A LYS   A 1 44  ? 30.423 8.866   -3.440  0.66 15.83 ?  44  LYS   A CG   1 
ATOM   1014 C CG   B LYS   A 1 44  ? 30.174 8.908   -3.558  0.34 17.16 ?  44  LYS   A CG   1 
ATOM   1015 C CD   A LYS   A 1 44  ? 31.053 9.834   -2.443  0.66 21.24 ?  44  LYS   A CD   1 
ATOM   1016 C CD   B LYS   A 1 44  ? 30.936 9.588   -2.426  0.34 20.66 ?  44  LYS   A CD   1 
ATOM   1017 C CE   A LYS   A 1 44  ? 32.387 10.347  -2.948  0.66 24.53 ?  44  LYS   A CE   1 
ATOM   1018 C CE   B LYS   A 1 44  ? 32.151 10.341  -2.932  0.34 22.66 ?  44  LYS   A CE   1 
ATOM   1019 N NZ   A LYS   A 1 44  ? 33.193 10.961  -1.862  0.66 26.43 ?  44  LYS   A NZ   1 
ATOM   1020 N NZ   B LYS   A 1 44  ? 33.025 10.789  -1.812  0.34 23.70 ?  44  LYS   A NZ   1 
ATOM   1021 H H    A LYS   A 1 44  ? 29.508 6.022   -2.360  0.66 12.48 ?  44  LYS   A H    1 
ATOM   1022 H H    B LYS   A 1 44  ? 29.363 6.044   -2.438  0.34 13.42 ?  44  LYS   A H    1 
ATOM   1023 H HA   A LYS   A 1 44  ? 29.442 8.358   -0.998  0.66 13.01 ?  44  LYS   A HA   1 
ATOM   1024 H HA   B LYS   A 1 44  ? 29.274 8.380   -1.080  0.34 14.26 ?  44  LYS   A HA   1 
ATOM   1025 H HB2  A LYS   A 1 44  ? 28.725 7.769   -3.667  0.66 15.41 ?  44  LYS   A HB2  1 
ATOM   1026 H HB2  B LYS   A 1 44  ? 28.519 7.729   -3.733  0.34 17.16 ?  44  LYS   A HB2  1 
ATOM   1027 H HB3  A LYS   A 1 44  ? 28.460 9.194   -3.021  0.66 15.41 ?  44  LYS   A HB3  1 
ATOM   1028 H HB3  B LYS   A 1 44  ? 28.200 9.153   -3.109  0.34 17.16 ?  44  LYS   A HB3  1 
ATOM   1029 H HG2  A LYS   A 1 44  ? 31.005 8.092   -3.515  0.66 18.98 ?  44  LYS   A HG2  1 
ATOM   1030 H HG2  B LYS   A 1 44  ? 30.704 8.159   -3.875  0.34 20.57 ?  44  LYS   A HG2  1 
ATOM   1031 H HG3  A LYS   A 1 44  ? 30.366 9.319   -4.298  0.66 18.98 ?  44  LYS   A HG3  1 
ATOM   1032 H HG3  B LYS   A 1 44  ? 30.051 9.556   -4.271  0.34 20.57 ?  44  LYS   A HG3  1 
ATOM   1033 H HD2  A LYS   A 1 44  ? 30.456 10.585  -2.308  0.66 25.46 ?  44  LYS   A HD2  1 
ATOM   1034 H HD2  B LYS   A 1 44  ? 30.346 10.215  -1.975  0.34 24.76 ?  44  LYS   A HD2  1 
ATOM   1035 H HD3  A LYS   A 1 44  ? 31.209 9.370   -1.603  0.66 25.46 ?  44  LYS   A HD3  1 
ATOM   1036 H HD3  B LYS   A 1 44  ? 31.246 8.912   -1.799  0.34 24.76 ?  44  LYS   A HD3  1 
ATOM   1037 H HE2  A LYS   A 1 44  ? 32.892 9.605   -3.319  0.66 29.41 ?  44  LYS   A HE2  1 
ATOM   1038 H HE2  B LYS   A 1 44  ? 32.671 9.757   -3.506  0.34 27.16 ?  44  LYS   A HE2  1 
ATOM   1039 H HE3  A LYS   A 1 44  ? 32.229 11.017  -3.629  0.66 29.41 ?  44  LYS   A HE3  1 
ATOM   1040 H HE3  B LYS   A 1 44  ? 31.860 11.124  -3.423  0.34 27.16 ?  44  LYS   A HE3  1 
ATOM   1041 H HZ1  A LYS   A 1 44  ? 33.968 11.250  -2.187  0.66 31.70 ?  44  LYS   A HZ1  1 
ATOM   1042 H HZ1  B LYS   A 1 44  ? 33.730 11.228  -2.133  0.34 28.41 ?  44  LYS   A HZ1  1 
ATOM   1043 H HZ2  A LYS   A 1 44  ? 32.751 11.649  -1.509  0.66 31.70 ?  44  LYS   A HZ2  1 
ATOM   1044 H HZ2  B LYS   A 1 44  ? 32.571 11.331  -1.269  0.34 28.41 ?  44  LYS   A HZ2  1 
ATOM   1045 H HZ3  A LYS   A 1 44  ? 33.351 10.362  -1.224  0.66 31.70 ?  44  LYS   A HZ3  1 
ATOM   1046 H HZ3  B LYS   A 1 44  ? 33.309 10.087  -1.346  0.34 28.41 ?  44  LYS   A HZ3  1 
ATOM   1047 N N    A HIS   A 1 45  ? 27.302 8.010   0.096   0.66 9.97  ?  45  HIS   A N    1 
ATOM   1048 N N    B HIS   A 1 45  ? 27.216 7.941   0.109   0.34 11.28 ?  45  HIS   A N    1 
ATOM   1049 C CA   A HIS   A 1 45  ? 26.068 7.652   0.793   0.66 10.06 ?  45  HIS   A CA   1 
ATOM   1050 C CA   B HIS   A 1 45  ? 25.963 7.673   0.812   0.34 11.40 ?  45  HIS   A CA   1 
ATOM   1051 C C    A HIS   A 1 45  ? 25.023 8.760   0.635   0.66 10.55 ?  45  HIS   A C    1 
ATOM   1052 C C    B HIS   A 1 45  ? 25.021 8.847   0.592   0.34 11.83 ?  45  HIS   A C    1 
ATOM   1053 O O    A HIS   A 1 45  ? 24.653 9.461   1.579   0.66 11.47 ?  45  HIS   A O    1 
ATOM   1054 O O    B HIS   A 1 45  ? 24.991 9.802   1.369   0.34 12.70 ?  45  HIS   A O    1 
ATOM   1055 C CB   A HIS   A 1 45  ? 26.375 7.367   2.254   0.66 9.92  ?  45  HIS   A CB   1 
ATOM   1056 C CB   B HIS   A 1 45  ? 26.239 7.465   2.292   0.34 10.89 ?  45  HIS   A CB   1 
ATOM   1057 C CG   A HIS   A 1 45  ? 27.483 6.379   2.453   0.66 9.69  ?  45  HIS   A CG   1 
ATOM   1058 C CG   B HIS   A 1 45  ? 27.373 6.531   2.562   0.34 10.09 ?  45  HIS   A CG   1 
ATOM   1059 N ND1  A HIS   A 1 45  ? 27.449 5.097   1.940   0.66 10.10 ?  45  HIS   A ND1  1 
ATOM   1060 N ND1  B HIS   A 1 45  ? 27.403 5.238   2.084   0.34 10.52 ?  45  HIS   A ND1  1 
ATOM   1061 C CD2  A HIS   A 1 45  ? 28.666 6.502   3.101   0.66 10.18 ?  45  HIS   A CD2  1 
ATOM   1062 C CD2  B HIS   A 1 45  ? 28.526 6.708   3.251   0.34 9.16  ?  45  HIS   A CD2  1 
ATOM   1063 C CE1  A HIS   A 1 45  ? 28.563 4.471   2.283   0.66 10.52 ?  45  HIS   A CE1  1 
ATOM   1064 C CE1  B HIS   A 1 45  ? 28.523 4.658   2.475   0.34 9.21  ?  45  HIS   A CE1  1 
ATOM   1065 N NE2  A HIS   A 1 45  ? 29.319 5.301   2.983   0.66 10.68 ?  45  HIS   A NE2  1 
ATOM   1066 N NE2  B HIS   A 1 45  ? 29.223 5.528   3.183   0.34 8.65  ?  45  HIS   A NE2  1 
ATOM   1067 H H    A HIS   A 1 45  ? 27.833 8.511   0.556   0.66 11.94 ?  45  HIS   A H    1 
ATOM   1068 H H    B HIS   A 1 45  ? 27.804 8.350   0.590   0.34 13.51 ?  45  HIS   A H    1 
ATOM   1069 H HA   A HIS   A 1 45  ? 25.711 6.844   0.401   0.66 12.05 ?  45  HIS   A HA   1 
ATOM   1070 H HA   B HIS   A 1 45  ? 25.554 6.870   0.451   0.34 13.65 ?  45  HIS   A HA   1 
ATOM   1071 H HB2  A HIS   A 1 45  ? 26.634 8.192   2.694   0.66 11.89 ?  45  HIS   A HB2  1 
ATOM   1072 H HB2  B HIS   A 1 45  ? 26.455 8.323   2.692   0.34 13.04 ?  45  HIS   A HB2  1 
ATOM   1073 H HB3  A HIS   A 1 45  ? 25.580 7.004   2.679   0.66 11.89 ?  45  HIS   A HB3  1 
ATOM   1074 H HB3  B HIS   A 1 45  ? 25.443 7.099   2.707   0.34 13.04 ?  45  HIS   A HB3  1 
ATOM   1075 H HD2  A HIS   A 1 45  ? 28.981 7.256   3.548   0.66 12.20 ?  45  HIS   A HD2  1 
ATOM   1076 H HD2  B HIS   A 1 45  ? 28.794 7.485   3.689   0.34 10.97 ?  45  HIS   A HD2  1 
ATOM   1077 H HE1  A HIS   A 1 45  ? 28.782 3.588   2.073   0.66 12.60 ?  45  HIS   A HE1  1 
ATOM   1078 H HE1  B HIS   A 1 45  ? 28.773 3.786   2.282   0.34 11.02 ?  45  HIS   A HE1  1 
ATOM   1079 H HE2  A HIS   A 1 45  ? 30.097 5.115   3.316   0.66 12.79 ?  45  HIS   A HE2  1 
ATOM   1080 H HE2  B HIS   A 1 45  ? 29.987 5.378   3.542   0.34 10.36 ?  45  HIS   A HE2  1 
ATOM   1081 N N    A GLY   A 1 46  ? 24.531 8.895   -0.596  0.66 11.21 ?  46  GLY   A N    1 
ATOM   1082 N N    B GLY   A 1 46  ? 24.225 8.770   -0.469  0.34 11.61 ?  46  GLY   A N    1 
ATOM   1083 C CA   A GLY   A 1 46  ? 23.734 10.053  -0.961  0.66 12.20 ?  46  GLY   A CA   1 
ATOM   1084 C CA   B GLY   A 1 46  ? 23.397 9.897   -0.846  0.34 11.80 ?  46  GLY   A CA   1 
ATOM   1085 C C    A GLY   A 1 46  ? 22.241 9.938   -0.722  0.66 12.18 ?  46  GLY   A C    1 
ATOM   1086 C C    B GLY   A 1 46  ? 21.953 9.788   -0.406  0.34 11.30 ?  46  GLY   A C    1 
ATOM   1087 O O    A GLY   A 1 46  ? 21.571 10.946  -0.469  0.66 12.88 ?  46  GLY   A O    1 
ATOM   1088 O O    B GLY   A 1 46  ? 21.375 10.762  0.085   0.34 11.50 ?  46  GLY   A O    1 
ATOM   1089 H H    A GLY   A 1 46  ? 24.644 8.324   -1.228  0.66 13.43 ?  46  GLY   A H    1 
ATOM   1090 H H    B GLY   A 1 46  ? 24.145 8.078   -0.978  0.34 13.91 ?  46  GLY   A H    1 
ATOM   1091 H HA2  A GLY   A 1 46  ? 24.061 10.819  -0.463  0.66 14.62 ?  46  GLY   A HA2  1 
ATOM   1092 H HA2  B GLY   A 1 46  ? 23.763 10.705  -0.454  0.34 14.13 ?  46  GLY   A HA2  1 
ATOM   1093 H HA3  A GLY   A 1 46  ? 23.867 10.231  -1.902  0.66 14.62 ?  46  GLY   A HA3  1 
ATOM   1094 H HA3  B GLY   A 1 46  ? 23.416 9.993   -1.807  0.34 14.13 ?  46  GLY   A HA3  1 
ATOM   1095 N N    A GLY   A 1 47  ? 21.701 8.728   -0.814  0.66 11.86 ?  47  GLY   A N    1 
ATOM   1096 N N    B GLY   A 1 47  ? 21.357 8.609   -0.569  0.34 11.26 ?  47  GLY   A N    1 
ATOM   1097 C CA   A GLY   A 1 47  ? 20.266 8.538   -0.750  0.66 11.94 ?  47  GLY   A CA   1 
ATOM   1098 C CA   B GLY   A 1 47  ? 19.944 8.433   -0.309  0.34 11.23 ?  47  GLY   A CA   1 
ATOM   1099 C C    A GLY   A 1 47  ? 19.936 7.105   -0.392  0.66 11.44 ?  47  GLY   A C    1 
ATOM   1100 C C    B GLY   A 1 47  ? 19.620 7.004   0.066   0.34 10.46 ?  47  GLY   A C    1 
ATOM   1101 O O    A GLY   A 1 47  ? 20.821 6.276   -0.174  0.66 11.51 ?  47  GLY   A O    1 
ATOM   1102 O O    B GLY   A 1 47  ? 20.505 6.155   0.191   0.34 10.64 ?  47  GLY   A O    1 
ATOM   1103 H H    A GLY   A 1 47  ? 22.152 8.001   -0.895  0.66 14.21 ?  47  GLY   A H    1 
ATOM   1104 H H    B GLY   A 1 47  ? 21.762 7.894   -0.820  0.34 13.49 ?  47  GLY   A H    1 
ATOM   1105 H HA2  A GLY   A 1 47  ? 19.880 9.135   -0.086  0.66 14.30 ?  47  GLY   A HA2  1 
ATOM   1106 H HA2  B GLY   A 1 47  ? 19.671 9.007   0.420   0.34 13.45 ?  47  GLY   A HA2  1 
ATOM   1107 H HA3  A GLY   A 1 47  ? 19.877 8.742   -1.615  0.66 14.30 ?  47  GLY   A HA3  1 
ATOM   1108 H HA3  B GLY   A 1 47  ? 19.436 8.666   -1.099  0.34 13.45 ?  47  GLY   A HA3  1 
ATOM   1109 N N    A GLY   A 1 48  ? 18.641 6.812   -0.357  0.66 11.26 ?  48  GLY   A N    1 
ATOM   1110 N N    B GLY   A 1 48  ? 18.324 6.745   0.243   0.34 10.41 ?  48  GLY   A N    1 
ATOM   1111 C CA   A GLY   A 1 48  ? 18.204 5.486   0.015   0.66 11.27 ?  48  GLY   A CA   1 
ATOM   1112 C CA   B GLY   A 1 48  ? 17.894 5.424   0.670   0.34 9.98  ?  48  GLY   A CA   1 
ATOM   1113 C C    A GLY   A 1 48  ? 18.652 5.136   1.419   0.66 11.01 ?  48  GLY   A C    1 
ATOM   1114 C C    B GLY   A 1 48  ? 18.527 5.050   1.996   0.34 9.93  ?  48  GLY   A C    1 
ATOM   1115 O O    A GLY   A 1 48  ? 18.817 6.002   2.287   0.66 11.37 ?  48  GLY   A O    1 
ATOM   1116 O O    B GLY   A 1 48  ? 18.737 5.893   2.877   0.34 10.14 ?  48  GLY   A O    1 
ATOM   1117 H H    A GLY   A 1 48  ? 18.013 7.360   -0.545  0.66 13.48 ?  48  GLY   A H    1 
ATOM   1118 H H    B GLY   A 1 48  ? 17.675 7.312   0.129   0.34 12.47 ?  48  GLY   A H    1 
ATOM   1119 H HA2  A GLY   A 1 48  ? 17.241 5.438   -0.021  0.66 13.51 ?  48  GLY   A HA2  1 
ATOM   1120 H HA2  B GLY   A 1 48  ? 16.922 5.400   0.758   0.34 11.95 ?  48  GLY   A HA2  1 
ATOM   1121 H HA3  A GLY   A 1 48  ? 18.580 4.833   -0.591  0.66 13.51 ?  48  GLY   A HA3  1 
ATOM   1122 H HA3  B GLY   A 1 48  ? 18.152 4.765   0.004   0.34 11.95 ?  48  GLY   A HA3  1 
ATOM   1123 N N    A VAL   A 1 49  ? 18.870 3.838   1.642   0.66 11.18 ?  49  VAL   A N    1 
ATOM   1124 N N    B VAL   A 1 49  ? 18.839 3.761   2.139   0.34 9.92  ?  49  VAL   A N    1 
ATOM   1125 C CA   A VAL   A 1 49  ? 19.343 3.374   2.943   0.66 11.49 ?  49  VAL   A CA   1 
ATOM   1126 C CA   B VAL   A 1 49  ? 19.460 3.263   3.365   0.34 10.18 ?  49  VAL   A CA   1 
ATOM   1127 C C    A VAL   A 1 49  ? 20.659 4.051   3.307   0.66 10.60 ?  49  VAL   A C    1 
ATOM   1128 C C    B VAL   A 1 49  ? 20.753 4.013   3.661   0.34 9.56  ?  49  VAL   A C    1 
ATOM   1129 O O    A VAL   A 1 49  ? 20.849 4.486   4.446   0.66 10.63 ?  49  VAL   A O    1 
ATOM   1130 O O    B VAL   A 1 49  ? 21.013 4.408   4.805   0.34 9.68  ?  49  VAL   A O    1 
ATOM   1131 C CB   A VAL   A 1 49  ? 19.471 1.839   2.954   0.66 12.64 ?  49  VAL   A CB   1 
ATOM   1132 C CB   B VAL   A 1 49  ? 19.699 1.747   3.255   0.34 11.44 ?  49  VAL   A CB   1 
ATOM   1133 C CG1  A VAL   A 1 49  ? 20.196 1.367   4.216   0.66 13.18 ?  49  VAL   A CG1  1 
ATOM   1134 C CG1  B VAL   A 1 49  ? 20.653 1.280   4.344   0.34 11.24 ?  49  VAL   A CG1  1 
ATOM   1135 C CG2  A VAL   A 1 49  ? 18.102 1.180   2.853   0.66 14.26 ?  49  VAL   A CG2  1 
ATOM   1136 C CG2  B VAL   A 1 49  ? 18.379 0.990   3.324   0.34 12.14 ?  49  VAL   A CG2  1 
ATOM   1137 H H    A VAL   A 1 49  ? 18.758 3.215   1.067   0.66 13.39 ?  49  VAL   A H    1 
ATOM   1138 H H    B VAL   A 1 49  ? 18.694 3.156   1.542   0.34 11.88 ?  49  VAL   A H    1 
ATOM   1139 H HA   A VAL   A 1 49  ? 18.696 3.613   3.623   0.66 13.77 ?  49  VAL   A HA   1 
ATOM   1140 H HA   B VAL   A 1 49  ? 18.856 3.412   4.105   0.34 12.19 ?  49  VAL   A HA   1 
ATOM   1141 H HB   A VAL   A 1 49  ? 20.002 1.556   2.193   0.66 15.15 ?  49  VAL   A HB   1 
ATOM   1142 H HB   B VAL   A 1 49  ? 20.110 1.552   2.397   0.34 13.70 ?  49  VAL   A HB   1 
ATOM   1143 H HG11 A VAL   A 1 49  ? 20.026 0.418   4.342   0.66 15.79 ?  49  VAL   A HG11 1 
ATOM   1144 H HG11 B VAL   A 1 49  ? 20.563 0.321   4.450   0.34 13.46 ?  49  VAL   A HG11 1 
ATOM   1145 H HG12 A VAL   A 1 49  ? 21.148 1.519   4.121   0.66 15.79 ?  49  VAL   A HG12 1 
ATOM   1146 H HG12 B VAL   A 1 49  ? 21.564 1.498   4.085   0.34 13.46 ?  49  VAL   A HG12 1 
ATOM   1147 H HG13 A VAL   A 1 49  ? 19.854 1.861   4.981   0.66 15.79 ?  49  VAL   A HG13 1 
ATOM   1148 H HG13 B VAL   A 1 49  ? 20.427 1.726   5.174   0.34 13.46 ?  49  VAL   A HG13 1 
ATOM   1149 H HG21 A VAL   A 1 49  ? 18.216 0.216   2.859   0.66 17.09 ?  49  VAL   A HG21 1 
ATOM   1150 H HG21 B VAL   A 1 49  ? 18.556 0.040   3.246   0.34 14.54 ?  49  VAL   A HG21 1 
ATOM   1151 H HG22 A VAL   A 1 49  ? 17.567 1.455   3.613   0.66 17.09 ?  49  VAL   A HG22 1 
ATOM   1152 H HG22 B VAL   A 1 49  ? 17.952 1.181   4.172   0.34 14.54 ?  49  VAL   A HG22 1 
ATOM   1153 H HG23 A VAL   A 1 49  ? 17.684 1.461   2.028   0.66 17.09 ?  49  VAL   A HG23 1 
ATOM   1154 H HG23 B VAL   A 1 49  ? 17.812 1.283   2.593   0.34 14.54 ?  49  VAL   A HG23 1 
ATOM   1155 N N    A ALA   A 1 50  ? 21.597 4.118   2.357   0.66 10.27 ?  50  ALA   A N    1 
ATOM   1156 N N    B ALA   A 1 50  ? 21.600 4.186   2.642   0.34 9.56  ?  50  ALA   A N    1 
ATOM   1157 C CA   A ALA   A 1 50  ? 22.918 4.668   2.649   0.66 10.49 ?  50  ALA   A CA   1 
ATOM   1158 C CA   B ALA   A 1 50  ? 22.922 4.760   2.871   0.34 9.31  ?  50  ALA   A CA   1 
ATOM   1159 C C    A ALA   A 1 50  ? 22.829 6.129   3.061   0.66 10.11 ?  50  ALA   A C    1 
ATOM   1160 C C    B ALA   A 1 50  ? 22.817 6.199   3.355   0.34 9.11  ?  50  ALA   A C    1 
ATOM   1161 O O    A ALA   A 1 50  ? 23.476 6.555   4.023   0.66 10.36 ?  50  ALA   A O    1 
ATOM   1162 O O    B ALA   A 1 50  ? 23.427 6.574   4.364   0.34 9.34  ?  50  ALA   A O    1 
ATOM   1163 C CB   A ALA   A 1 50  ? 23.823 4.523   1.429   0.66 10.85 ?  50  ALA   A CB   1 
ATOM   1164 C CB   B ALA   A 1 50  ? 23.760 4.667   1.595   0.34 8.70  ?  50  ALA   A CB   1 
ATOM   1165 H H    A ALA   A 1 50  ? 21.491 3.860   1.548   0.66 12.30 ?  50  ALA   A H    1 
ATOM   1166 H H    B ALA   A 1 50  ? 21.431 3.990   1.818   0.34 11.44 ?  50  ALA   A H    1 
ATOM   1167 H HA   A ALA   A 1 50  ? 23.315 4.177   3.387   0.66 12.57 ?  50  ALA   A HA   1 
ATOM   1168 H HA   B ALA   A 1 50  ? 23.370 4.254   3.561   0.34 11.14 ?  50  ALA   A HA   1 
ATOM   1169 H HB1  A ALA   A 1 50  ? 24.694 4.894   1.639   0.66 12.99 ?  50  ALA   A HB1  1 
ATOM   1170 H HB1  B ALA   A 1 50  ? 24.635 5.051   1.763   0.34 10.42 ?  50  ALA   A HB1  1 
ATOM   1171 H HB2  A ALA   A 1 50  ? 23.903 3.584   1.209   0.66 12.99 ?  50  ALA   A HB2  1 
ATOM   1172 H HB2  B ALA   A 1 50  ? 23.852 3.733   1.346   0.34 10.42 ?  50  ALA   A HB2  1 
ATOM   1173 H HB3  A ALA   A 1 50  ? 23.426 5.007   0.688   0.66 12.99 ?  50  ALA   A HB3  1 
ATOM   1174 H HB3  B ALA   A 1 50  ? 23.315 5.155   0.885   0.34 10.42 ?  50  ALA   A HB3  1 
ATOM   1175 N N    A GLY   A 1 51  ? 22.046 6.921   2.330   0.66 10.16 ?  51  GLY   A N    1 
ATOM   1176 N N    B GLY   A 1 51  ? 22.033 7.019   2.653   0.34 9.49  ?  51  GLY   A N    1 
ATOM   1177 C CA   A GLY   A 1 51  ? 21.899 8.320   2.693   0.66 10.66 ?  51  GLY   A CA   1 
ATOM   1178 C CA   B GLY   A 1 51  ? 21.862 8.397   3.082   0.34 9.51  ?  51  GLY   A CA   1 
ATOM   1179 C C    A GLY   A 1 51  ? 21.281 8.493   4.066   0.66 10.43 ?  51  GLY   A C    1 
ATOM   1180 C C    B GLY   A 1 51  ? 21.260 8.489   4.470   0.34 9.80  ?  51  GLY   A C    1 
ATOM   1181 O O    A GLY   A 1 51  ? 21.667 9.391   4.820   0.66 10.69 ?  51  GLY   A O    1 
ATOM   1182 O O    B GLY   A 1 51  ? 21.639 9.352   5.269   0.34 10.05 ?  51  GLY   A O    1 
ATOM   1183 H H    A GLY   A 1 51  ? 21.604 6.677   1.637   0.66 12.17 ?  51  GLY   A H    1 
ATOM   1184 H H    B GLY   A 1 51  ? 21.590 6.802   1.942   0.34 11.37 ?  51  GLY   A H    1 
ATOM   1185 H HA2  A GLY   A 1 51  ? 22.764 8.750   2.698   0.66 12.77 ?  51  GLY   A HA2  1 
ATOM   1186 H HA2  B GLY   A 1 51  ? 22.723 8.843   3.081   0.34 11.39 ?  51  GLY   A HA2  1 
ATOM   1187 H HA3  A GLY   A 1 51  ? 21.331 8.768   2.046   0.66 12.77 ?  51  GLY   A HA3  1 
ATOM   1188 H HA3  B GLY   A 1 51  ? 21.279 8.860   2.452   0.34 11.39 ?  51  GLY   A HA3  1 
ATOM   1189 N N    A ALA   A 1 52  ? 20.307 7.641   4.407   0.66 10.78 ?  52  ALA   A N    1 
ATOM   1190 N N    B ALA   A 1 52  ? 20.321 7.591   4.780   0.34 10.07 ?  52  ALA   A N    1 
ATOM   1191 C CA   A ALA   A 1 52  ? 19.650 7.730   5.707   0.66 11.28 ?  52  ALA   A CA   1 
ATOM   1192 C CA   B ALA   A 1 52  ? 19.675 7.622   6.086   0.34 10.42 ?  52  ALA   A CA   1 
ATOM   1193 C C    A ALA   A 1 52  ? 20.588 7.315   6.838   0.66 10.92 ?  52  ALA   A C    1 
ATOM   1194 C C    B ALA   A 1 52  ? 20.629 7.177   7.191   0.34 9.74  ?  52  ALA   A C    1 
ATOM   1195 O O    A ALA   A 1 52  ? 20.652 7.978   7.879   0.66 11.24 ?  52  ALA   A O    1 
ATOM   1196 O O    B ALA   A 1 52  ? 20.680 7.796   8.261   0.34 10.00 ?  52  ALA   A O    1 
ATOM   1197 C CB   A ALA   A 1 52  ? 18.383 6.871   5.708   0.66 12.50 ?  52  ALA   A CB   1 
ATOM   1198 C CB   B ALA   A 1 52  ? 18.406 6.769   6.058   0.34 11.85 ?  52  ALA   A CB   1 
ATOM   1199 H H    A ALA   A 1 52  ? 20.028 6.997   3.915   0.66 12.91 ?  52  ALA   A H    1 
ATOM   1200 H H    B ALA   A 1 52  ? 20.052 6.960   4.253   0.34 12.06 ?  52  ALA   A H    1 
ATOM   1201 H HA   A ALA   A 1 52  ? 19.383 8.647   5.864   0.66 13.52 ?  52  ALA   A HA   1 
ATOM   1202 H HA   B ALA   A 1 52  ? 19.414 8.534   6.270   0.34 12.48 ?  52  ALA   A HA   1 
ATOM   1203 H HB1  A ALA   A 1 52  ? 17.950 6.941   6.578   0.66 14.98 ?  52  ALA   A HB1  1 
ATOM   1204 H HB1  B ALA   A 1 52  ? 17.962 6.843   6.915   0.34 14.20 ?  52  ALA   A HB1  1 
ATOM   1205 H HB2  A ALA   A 1 52  ? 17.782 7.192   5.018   0.66 14.98 ?  52  ALA   A HB2  1 
ATOM   1206 H HB2  B ALA   A 1 52  ? 17.821 7.102   5.354   0.34 14.20 ?  52  ALA   A HB2  1 
ATOM   1207 H HB3  A ALA   A 1 52  ? 18.622 5.947   5.536   0.66 14.98 ?  52  ALA   A HB3  1 
ATOM   1208 H HB3  B ALA   A 1 52  ? 18.644 5.849   5.878   0.34 14.20 ?  52  ALA   A HB3  1 
ATOM   1209 N N    A LEU   A 1 53  ? 21.308 6.204   6.668   0.66 10.73 ?  53  LEU   A N    1 
ATOM   1210 N N    B LEU   A 1 53  ? 21.392 6.104   6.960   0.34 9.76  ?  53  LEU   A N    1 
ATOM   1211 C CA   A LEU   A 1 53  ? 22.242 5.779   7.707   0.66 11.14 ?  53  LEU   A CA   1 
ATOM   1212 C CA   B LEU   A 1 53  ? 22.430 5.733   7.917   0.34 9.86  ?  53  LEU   A CA   1 
ATOM   1213 C C    A LEU   A 1 53  ? 23.314 6.834   7.929   0.66 10.73 ?  53  LEU   A C    1 
ATOM   1214 C C    B LEU   A 1 53  ? 23.431 6.868   8.089   0.34 9.78  ?  53  LEU   A C    1 
ATOM   1215 O O    A LEU   A 1 53  ? 23.657 7.154   9.070   0.66 11.85 ?  53  LEU   A O    1 
ATOM   1216 O O    B LEU   A 1 53  ? 23.726 7.291   9.212   0.34 10.43 ?  53  LEU   A O    1 
ATOM   1217 C CB   A LEU   A 1 53  ? 22.884 4.439   7.336   0.66 11.78 ?  53  LEU   A CB   1 
ATOM   1218 C CB   B LEU   A 1 53  ? 23.144 4.454   7.467   0.34 9.74  ?  53  LEU   A CB   1 
ATOM   1219 C CG   A LEU   A 1 53  ? 22.007 3.181   7.405   0.66 11.82 ?  53  LEU   A CG   1 
ATOM   1220 C CG   B LEU   A 1 53  ? 22.404 3.113   7.558   0.34 10.19 ?  53  LEU   A CG   1 
ATOM   1221 C CD1  A LEU   A 1 53  ? 22.749 1.993   6.817   0.66 12.01 ?  53  LEU   A CD1  1 
ATOM   1222 C CD1  B LEU   A 1 53  ? 23.236 2.017   6.905   0.34 10.86 ?  53  LEU   A CD1  1 
ATOM   1223 C CD2  A LEU   A 1 53  ? 21.578 2.884   8.836   0.66 13.11 ?  53  LEU   A CD2  1 
ATOM   1224 C CD2  B LEU   A 1 53  ? 22.083 2.739   8.998   0.34 10.24 ?  53  LEU   A CD2  1 
ATOM   1225 H H    A LEU   A 1 53  ? 21.276 5.694   5.985   0.66 12.85 ?  53  LEU   A H    1 
ATOM   1226 H H    B LEU   A 1 53  ? 21.327 5.584   6.273   0.34 11.69 ?  53  LEU   A H    1 
ATOM   1227 H HA   A LEU   A 1 53  ? 21.765 5.660   8.545   0.66 13.35 ?  53  LEU   A HA   1 
ATOM   1228 H HA   B LEU   A 1 53  ? 22.017 5.561   8.775   0.34 11.81 ?  53  LEU   A HA   1 
ATOM   1229 H HB2  A LEU   A 1 53  ? 23.211 4.508   6.425   0.66 14.11 ?  53  LEU   A HB2  1 
ATOM   1230 H HB2  B LEU   A 1 53  ? 23.400 4.568   6.539   0.34 11.67 ?  53  LEU   A HB2  1 
ATOM   1231 H HB3  A LEU   A 1 53  ? 23.637 4.289   7.931   0.66 14.11 ?  53  LEU   A HB3  1 
ATOM   1232 H HB3  B LEU   A 1 53  ? 23.947 4.363   8.005   0.34 11.67 ?  53  LEU   A HB3  1 
ATOM   1233 H HG   A LEU   A 1 53  ? 21.209 3.327   6.871   0.66 14.15 ?  53  LEU   A HG   1 
ATOM   1234 H HG   B LEU   A 1 53  ? 21.570 3.179   7.070   0.34 12.21 ?  53  LEU   A HG   1 
ATOM   1235 H HD11 A LEU   A 1 53  ? 22.181 1.209   6.869   0.66 14.39 ?  53  LEU   A HD11 1 
ATOM   1236 H HD11 B LEU   A 1 53  ? 22.758 1.175   6.971   0.34 13.00 ?  53  LEU   A HD11 1 
ATOM   1237 H HD12 A LEU   A 1 53  ? 22.971 2.181   5.891   0.66 14.39 ?  53  LEU   A HD12 1 
ATOM   1238 H HD12 B LEU   A 1 53  ? 23.382 2.242   5.973   0.34 13.00 ?  53  LEU   A HD12 1 
ATOM   1239 H HD13 A LEU   A 1 53  ? 23.563 1.845   7.327   0.66 14.39 ?  53  LEU   A HD13 1 
ATOM   1240 H HD13 B LEU   A 1 53  ? 24.088 1.949   7.366   0.34 13.00 ?  53  LEU   A HD13 1 
ATOM   1241 H HD21 A LEU   A 1 53  ? 21.059 2.067   8.845   0.66 15.70 ?  53  LEU   A HD21 1 
ATOM   1242 H HD21 B LEU   A 1 53  ? 21.586 1.907   9.004   0.34 12.27 ?  53  LEU   A HD21 1 
ATOM   1243 H HD22 A LEU   A 1 53  ? 22.369 2.784   9.387   0.66 15.70 ?  53  LEU   A HD22 1 
ATOM   1244 H HD22 B LEU   A 1 53  ? 22.911 2.635   9.490   0.34 12.27 ?  53  LEU   A HD22 1 
ATOM   1245 H HD23 A LEU   A 1 53  ? 21.040 3.623   9.163   0.66 15.70 ?  53  LEU   A HD23 1 
ATOM   1246 H HD23 B LEU   A 1 53  ? 21.549 3.446   9.394   0.34 12.27 ?  53  LEU   A HD23 1 
ATOM   1247 N N    A ASN   A 1 54  ? 23.851 7.392   6.849   0.66 10.51 ?  54  ASN   A N    1 
ATOM   1248 N N    B ASN   A 1 54  ? 23.955 7.387   6.978   0.34 10.16 ?  54  ASN   A N    1 
ATOM   1249 C CA   A ASN   A 1 54  ? 24.916 8.370   7.009   0.66 10.34 ?  54  ASN   A CA   1 
ATOM   1250 C CA   B ASN   A 1 54  ? 24.980 8.418   7.078   0.34 10.38 ?  54  ASN   A CA   1 
ATOM   1251 C C    A ASN   A 1 54  ? 24.419 9.607   7.757   0.66 11.01 ?  54  ASN   A C    1 
ATOM   1252 C C    B ASN   A 1 54  ? 24.442 9.672   7.757   0.34 10.72 ?  54  ASN   A C    1 
ATOM   1253 O O    A ASN   A 1 54  ? 25.112 10.135  8.637   0.66 11.69 ?  54  ASN   A O    1 
ATOM   1254 O O    B ASN   A 1 54  ? 25.133 10.284  8.581   0.34 10.61 ?  54  ASN   A O    1 
ATOM   1255 C CB   A ASN   A 1 54  ? 25.480 8.747   5.650   0.66 10.38 ?  54  ASN   A CB   1 
ATOM   1256 C CB   B ASN   A 1 54  ? 25.546 8.758   5.704   0.34 10.82 ?  54  ASN   A CB   1 
ATOM   1257 C CG   A ASN   A 1 54  ? 26.524 9.821   5.766   0.66 10.54 ?  54  ASN   A CG   1 
ATOM   1258 C CG   B ASN   A 1 54  ? 26.502 9.931   5.766   0.34 10.73 ?  54  ASN   A CG   1 
ATOM   1259 O OD1  A ASN   A 1 54  ? 27.516 9.652   6.480   0.66 10.48 ?  54  ASN   A OD1  1 
ATOM   1260 O OD1  B ASN   A 1 54  ? 27.556 9.847   6.399   0.34 10.43 ?  54  ASN   A OD1  1 
ATOM   1261 N ND2  A ASN   A 1 54  ? 26.312 10.940  5.096   0.66 11.18 ?  54  ASN   A ND2  1 
ATOM   1262 N ND2  B ASN   A 1 54  ? 26.134 11.037  5.136   0.34 11.41 ?  54  ASN   A ND2  1 
ATOM   1263 H H    A ASN   A 1 54  ? 23.620 7.224   6.041   0.66 12.59 ?  54  ASN   A H    1 
ATOM   1264 H H    B ASN   A 1 54  ? 23.737 7.166   6.176   0.34 12.17 ?  54  ASN   A H    1 
ATOM   1265 H HA   A ASN   A 1 54  ? 25.628 7.977   7.531   0.66 12.39 ?  54  ASN   A HA   1 
ATOM   1266 H HA   B ASN   A 1 54  ? 25.703 8.082   7.623   0.34 12.43 ?  54  ASN   A HA   1 
ATOM   1267 H HB2  A ASN   A 1 54  ? 25.889 7.960   5.249   0.66 12.43 ?  54  ASN   A HB2  1 
ATOM   1268 H HB2  B ASN   A 1 54  ? 26.030 7.987   5.364   0.34 12.95 ?  54  ASN   A HB2  1 
ATOM   1269 H HB3  A ASN   A 1 54  ? 24.766 9.076   5.085   0.66 12.43 ?  54  ASN   A HB3  1 
ATOM   1270 H HB3  B ASN   A 1 54  ? 24.820 8.987   5.105   0.34 12.95 ?  54  ASN   A HB3  1 
ATOM   1271 H HD21 A ASN   A 1 54  ? 26.884 11.579  5.139   0.66 13.40 ?  54  ASN   A HD21 1 
ATOM   1272 H HD21 B ASN   A 1 54  ? 26.646 11.728  5.151   0.34 13.66 ?  54  ASN   A HD21 1 
ATOM   1273 H HD22 A ASN   A 1 54  ? 25.604 11.025  4.617   0.66 13.40 ?  54  ASN   A HD22 1 
ATOM   1274 H HD22 B ASN   A 1 54  ? 25.389 11.062  4.711   0.34 13.66 ?  54  ASN   A HD22 1 
ATOM   1275 N N    . LYS   A 1 55  ? 23.214 10.080  7.419   1.00 11.15 ?  55  LYS   A N    1 
ATOM   1276 C CA   . LYS   A 1 55  ? 22.633 11.237  8.091   1.00 11.83 ?  55  LYS   A CA   1 
ATOM   1277 C C    . LYS   A 1 55  ? 22.538 11.000  9.592   1.00 11.91 ?  55  LYS   A C    1 
ATOM   1278 O O    . LYS   A 1 55  ? 22.820 11.899  10.391  1.00 12.77 ?  55  LYS   A O    1 
ATOM   1279 C CB   . LYS   A 1 55  ? 21.263 11.542  7.478   1.00 12.81 ?  55  LYS   A CB   1 
ATOM   1280 C CG   . LYS   A 1 55  ? 20.514 12.704  8.112   1.00 14.74 ?  55  LYS   A CG   1 
ATOM   1281 C CD   . LYS   A 1 55  ? 19.191 12.960  7.379   1.00 16.36 ?  55  LYS   A CD   1 
ATOM   1282 C CE   . LYS   A 1 55  ? 18.351 14.040  8.053   1.00 18.47 ?  55  LYS   A CE   1 
ATOM   1283 N NZ   . LYS   A 1 55  ? 17.011 14.214  7.405   1.00 19.49 ?  55  LYS   A NZ   1 
ATOM   1284 H H    A LYS   A 1 55  ? 22.708 9.739   6.811   0.66 13.36 ?  55  LYS   A H    1 
ATOM   1285 H H    B LYS   A 1 55  ? 22.705 9.706   6.834   0.34 13.36 ?  55  LYS   A H    1 
ATOM   1286 H HA   . LYS   A 1 55  ? 23.203 12.006  7.944   1.00 14.18 ?  55  LYS   A HA   1 
ATOM   1287 H HB2  . LYS   A 1 55  ? 21.383 11.757  6.540   1.00 15.34 ?  55  LYS   A HB2  1 
ATOM   1288 H HB3  . LYS   A 1 55  ? 20.701 10.758  7.564   1.00 15.34 ?  55  LYS   A HB3  1 
ATOM   1289 H HG2  . LYS   A 1 55  ? 20.313 12.492  9.037   1.00 17.67 ?  55  LYS   A HG2  1 
ATOM   1290 H HG3  . LYS   A 1 55  ? 21.056 13.505  8.057   1.00 17.67 ?  55  LYS   A HG3  1 
ATOM   1291 H HD2  . LYS   A 1 55  ? 19.384 13.249  6.472   1.00 19.60 ?  55  LYS   A HD2  1 
ATOM   1292 H HD3  . LYS   A 1 55  ? 18.674 12.140  7.362   1.00 19.60 ?  55  LYS   A HD3  1 
ATOM   1293 H HE2  . LYS   A 1 55  ? 18.204 13.797  8.980   1.00 22.14 ?  55  LYS   A HE2  1 
ATOM   1294 H HE3  . LYS   A 1 55  ? 18.819 14.888  8.000   1.00 22.14 ?  55  LYS   A HE3  1 
ATOM   1295 H HZ1  . LYS   A 1 55  ? 16.438 14.582  7.981   1.00 23.37 ?  55  LYS   A HZ1  1 
ATOM   1296 H HZ2  . LYS   A 1 55  ? 17.078 14.746  6.694   1.00 23.37 ?  55  LYS   A HZ2  1 
ATOM   1297 H HZ3  . LYS   A 1 55  ? 16.688 13.425  7.147   1.00 23.37 ?  55  LYS   A HZ3  1 
ATOM   1298 N N    . ALA   A 1 56  ? 22.153 9.788   9.994   1.00 12.19 ?  56  ALA   A N    1 
ATOM   1299 C CA   . ALA   A 1 56  ? 22.034 9.463   11.407  1.00 12.75 ?  56  ALA   A CA   1 
ATOM   1300 C C    . ALA   A 1 56  ? 23.376 9.487   12.128  1.00 12.98 ?  56  ALA   A C    1 
ATOM   1301 O O    . ALA   A 1 56  ? 23.400 9.666   13.349  1.00 14.45 ?  56  ALA   A O    1 
ATOM   1302 C CB   . ALA   A 1 56  ? 21.336 8.109   11.582  1.00 13.86 ?  56  ALA   A CB   1 
ATOM   1303 H H    . ALA   A 1 56  ? 21.957 9.143   9.463   1.00 14.60 ?  56  ALA   A H    1 
ATOM   1304 H HA   . ALA   A 1 56  ? 21.477 10.127  11.829  1.00 15.28 ?  56  ALA   A HA   1 
ATOM   1305 H HB1  . ALA   A 1 56  ? 21.272 7.905   12.531  1.00 16.60 ?  56  ALA   A HB1  1 
ATOM   1306 H HB2  . ALA   A 1 56  ? 20.447 8.159   11.197  1.00 16.60 ?  56  ALA   A HB2  1 
ATOM   1307 H HB3  . ALA   A 1 56  ? 21.852 7.420   11.133  1.00 16.60 ?  56  ALA   A HB3  1 
ATOM   1308 N N    . THR   A 1 57  ? 24.489 9.312   11.406  1.00 11.73 ?  57  THR   A N    1 
ATOM   1309 C CA   . THR   A 1 57  ? 25.833 9.437   11.979  1.00 11.81 ?  57  THR   A CA   1 
ATOM   1310 C C    . THR   A 1 57  ? 26.383 10.856  11.902  1.00 12.23 ?  57  THR   A C    1 
ATOM   1311 O O    . THR   A 1 57  ? 27.568 11.067  12.193  1.00 12.81 ?  57  THR   A O    1 
ATOM   1312 C CB   . THR   A 1 57  ? 26.840 8.487   11.306  1.00 11.68 ?  57  THR   A CB   1 
ATOM   1313 O OG1  . THR   A 1 57  ? 27.226 8.984   10.011  1.00 11.42 ?  57  THR   A OG1  1 
ATOM   1314 C CG2  . THR   A 1 57  ? 26.309 7.068   11.195  1.00 11.77 ?  57  THR   A CG2  1 
ATOM   1315 H H    . THR   A 1 57  ? 24.493 9.099   10.570  1.00 14.06 ?  57  THR   A H    1 
ATOM   1316 H HA   . THR   A 1 57  ? 25.789 9.182   12.918  1.00 14.15 ?  57  THR   A HA   1 
ATOM   1317 H HB   . THR   A 1 57  ? 27.640 8.442   11.863  1.00 14.00 ?  57  THR   A HB   1 
ATOM   1318 H HG1  . THR   A 1 57  ? 26.548 9.056   9.522   1.00 13.68 ?  57  THR   A HG1  1 
ATOM   1319 H HG21 . THR   A 1 57  ? 27.040 6.438   11.081  1.00 14.10 ?  57  THR   A HG21 1 
ATOM   1320 H HG22 . THR   A 1 57  ? 25.814 6.830   11.994  1.00 14.10 ?  57  THR   A HG22 1 
ATOM   1321 H HG23 . THR   A 1 57  ? 25.716 6.994   10.428  1.00 14.10 ?  57  THR   A HG23 1 
ATOM   1322 N N    . ASN   A 1 58  ? 25.565 11.829  11.501  1.00 12.72 ?  58  ASN   A N    1 
ATOM   1323 C CA   . ASN   A 1 58  ? 26.026 13.210  11.402  1.00 13.58 ?  58  ASN   A CA   1 
ATOM   1324 C C    . ASN   A 1 58  ? 27.169 13.340  10.389  1.00 12.32 ?  58  ASN   A C    1 
ATOM   1325 O O    . ASN   A 1 58  ? 28.062 14.178  10.543  1.00 13.06 ?  58  ASN   A O    1 
ATOM   1326 C CB   . ASN   A 1 58  ? 26.403 13.746  12.796  1.00 16.04 ?  58  ASN   A CB   1 
ATOM   1327 C CG   . ASN   A 1 58  ? 26.828 15.202  12.791  1.00 19.77 ?  58  ASN   A CG   1 
ATOM   1328 O OD1  . ASN   A 1 58  ? 26.199 16.036  12.153  1.00 21.55 ?  58  ASN   A OD1  1 
ATOM   1329 N ND2  . ASN   A 1 58  ? 27.899 15.515  13.525  1.00 20.89 ?  58  ASN   A ND2  1 
ATOM   1330 H H    . ASN   A 1 58  ? 24.744 11.705  11.269  1.00 15.24 ?  58  ASN   A H    1 
ATOM   1331 H HA   . ASN   A 1 58  ? 25.288 13.743  11.078  1.00 16.27 ?  58  ASN   A HA   1 
ATOM   1332 H HB2  . ASN   A 1 58  ? 25.629 13.660  13.386  1.00 19.23 ?  58  ASN   A HB2  1 
ATOM   1333 H HB3  . ASN   A 1 58  ? 27.138 13.228  13.153  1.00 19.23 ?  58  ASN   A HB3  1 
ATOM   1334 H HD21 . ASN   A 1 58  ? 28.173 16.328  13.557  1.00 25.05 ?  58  ASN   A HD21 1 
ATOM   1335 H HD22 . ASN   A 1 58  ? 28.312 14.901  13.959  1.00 25.05 ?  58  ASN   A HD22 1 
ATOM   1336 N N    . ASN   A 1 59  ? 27.144 12.522  9.334   1.00 11.48 ?  59  ASN   A N    1 
ATOM   1337 C CA   . ASN   A 1 59  ? 28.126 12.499  8.243   1.00 11.01 ?  59  ASN   A CA   1 
ATOM   1338 C C    . ASN   A 1 59  ? 29.442 11.816  8.627   1.00 10.74 ?  59  ASN   A C    1 
ATOM   1339 O O    . ASN   A 1 59  ? 30.361 11.778  7.794   1.00 11.41 ?  59  ASN   A O    1 
ATOM   1340 C CB   . ASN   A 1 59  ? 28.416 13.884  7.634   1.00 11.41 ?  59  ASN   A CB   1 
ATOM   1341 C CG   . ASN   A 1 59  ? 28.771 13.814  6.164   1.00 11.66 ?  59  ASN   A CG   1 
ATOM   1342 O OD1  . ASN   A 1 59  ? 28.067 13.184  5.368   1.00 12.23 ?  59  ASN   A OD1  1 
ATOM   1343 N ND2  . ASN   A 1 59  ? 29.857 14.478  5.786   1.00 12.44 ?  59  ASN   A ND2  1 
ATOM   1344 H H    . ASN   A 1 59  ? 26.531 11.927  9.221   1.00 13.75 ?  59  ASN   A H    1 
ATOM   1345 H HA   . ASN   A 1 59  ? 27.747 11.970  7.529   1.00 13.18 ?  59  ASN   A HA   1 
ATOM   1346 H HB2  . ASN   A 1 59  ? 27.632 14.445  7.720   1.00 13.67 ?  59  ASN   A HB2  1 
ATOM   1347 H HB3  . ASN   A 1 59  ? 29.168 14.289  8.097   1.00 13.67 ?  59  ASN   A HB3  1 
ATOM   1348 H HD21 . ASN   A 1 59  ? 30.102 14.478  4.959   1.00 14.91 ?  59  ASN   A HD21 1 
ATOM   1349 H HD22 . ASN   A 1 59  ? 30.327 14.914  6.365   1.00 14.91 ?  59  ASN   A HD22 1 
ATOM   1350 N N    . ALA   A 1 60  ? 29.572 11.272  9.837   1.00 10.89 ?  60  ALA   A N    1 
ATOM   1351 C CA   . ALA   A 1 60  ? 30.813 10.591  10.188  1.00 11.13 ?  60  ALA   A CA   1 
ATOM   1352 C C    . ALA   A 1 60  ? 31.036 9.353   9.324   1.00 11.36 ?  60  ALA   A C    1 
ATOM   1353 O O    . ALA   A 1 60  ? 32.183 9.030   8.986   1.00 11.63 ?  60  ALA   A O    1 
ATOM   1354 C CB   . ALA   A 1 60  ? 30.816 10.224  11.670  1.00 11.91 ?  60  ALA   A CB   1 
ATOM   1355 H H    . ALA   A 1 60  ? 28.975 11.278  10.454  1.00 13.04 ?  60  ALA   A H    1 
ATOM   1356 H HA   . ALA   A 1 60  ? 31.557 11.196  10.033  1.00 13.33 ?  60  ALA   A HA   1 
ATOM   1357 H HB1  . ALA   A 1 60  ? 31.646 9.776   11.888  1.00 14.27 ?  60  ALA   A HB1  1 
ATOM   1358 H HB2  . ALA   A 1 60  ? 30.731 11.038  12.197  1.00 14.27 ?  60  ALA   A HB2  1 
ATOM   1359 H HB3  . ALA   A 1 60  ? 30.064 9.638   11.853  1.00 14.27 ?  60  ALA   A HB3  1 
ATOM   1360 N N    . MET   A 1 61  ? 29.963 8.659   8.941   1.00 10.70 ?  61  MET   A N    1 
ATOM   1361 C CA   . MET   A 1 61  ? 30.102 7.522   8.035   1.00 10.74 ?  61  MET   A CA   1 
ATOM   1362 C C    . MET   A 1 61  ? 30.733 7.944   6.708   1.00 10.69 ?  61  MET   A C    1 
ATOM   1363 O O    . MET   A 1 61  ? 31.627 7.261   6.191   1.00 10.89 ?  61  MET   A O    1 
ATOM   1364 C CB   . MET   A 1 61  ? 28.741 6.855   7.828   1.00 10.58 ?  61  MET   A CB   1 
ATOM   1365 C CG   . MET   A 1 61  ? 28.748 5.696   6.845   1.00 11.12 ?  61  MET   A CG   1 
ATOM   1366 S SD   . MET   A 1 61  ? 27.127 4.937   6.646   1.00 12.22 ?  61  MET   A SD   1 
ATOM   1367 C CE   . MET   A 1 61  ? 26.995 4.061   8.205   1.00 13.76 ?  61  MET   A CE   1 
ATOM   1368 H H    . MET   A 1 61  ? 29.156 8.826   9.183   1.00 12.81 ?  61  MET   A H    1 
ATOM   1369 H HA   . MET   A 1 61  ? 30.683 6.868   8.450   1.00 12.86 ?  61  MET   A HA   1 
ATOM   1370 H HB2  . MET   A 1 61  ? 28.431 6.517   8.678   1.00 12.67 ?  61  MET   A HB2  1 
ATOM   1371 H HB3  . MET   A 1 61  ? 28.119 7.518   7.490   1.00 12.67 ?  61  MET   A HB3  1 
ATOM   1372 H HG2  . MET   A 1 61  ? 29.023 6.009   5.971   1.00 13.32 ?  61  MET   A HG2  1 
ATOM   1373 H HG3  . MET   A 1 61  ? 29.354 5.010   7.162   1.00 13.32 ?  61  MET   A HG3  1 
ATOM   1374 H HE1  . MET   A 1 61  ? 26.161 3.565   8.221   1.00 16.49 ?  61  MET   A HE1  1 
ATOM   1375 H HE2  . MET   A 1 61  ? 27.744 3.455   8.293   1.00 16.49 ?  61  MET   A HE2  1 
ATOM   1376 H HE3  . MET   A 1 61  ? 27.005 4.707   8.933   1.00 16.49 ?  61  MET   A HE3  1 
ATOM   1377 N N    . GLN   A 1 62  ? 30.288 9.070   6.148   1.00 10.43 ?  62  GLN   A N    1 
ATOM   1378 C CA   . GLN   A 1 62  ? 30.851 9.543   4.887   1.00 10.63 ?  62  GLN   A CA   1 
ATOM   1379 C C    . GLN   A 1 62  ? 32.321 9.922   5.032   1.00 10.65 ?  62  GLN   A C    1 
ATOM   1380 O O    . GLN   A 1 62  ? 33.131 9.613   4.151   1.00 11.02 ?  62  GLN   A O    1 
ATOM   1381 C CB   . GLN   A 1 62  ? 30.047 10.728  4.355   1.00 10.79 ?  62  GLN   A CB   1 
ATOM   1382 C CG   . GLN   A 1 62  ? 30.416 11.092  2.932   1.00 10.69 ?  62  GLN   A CG   1 
ATOM   1383 C CD   . GLN   A 1 62  ? 30.088 9.963   1.981   1.00 10.98 ?  62  GLN   A CD   1 
ATOM   1384 O OE1  . GLN   A 1 62  ? 28.914 9.655   1.767   1.00 11.76 ?  62  GLN   A OE1  1 
ATOM   1385 N NE2  . GLN   A 1 62  ? 31.114 9.286   1.463   1.00 11.66 ?  62  GLN   A NE2  1 
ATOM   1386 H H    . GLN   A 1 62  ? 29.668 9.565   6.472   1.00 12.50 ?  62  GLN   A H    1 
ATOM   1387 H HA   . GLN   A 1 62  ? 30.797 8.827   4.236   1.00 12.73 ?  62  GLN   A HA   1 
ATOM   1388 H HB2  . GLN   A 1 62  ? 29.103 10.507  4.374   1.00 12.92 ?  62  GLN   A HB2  1 
ATOM   1389 H HB3  . GLN   A 1 62  ? 30.218 11.504  4.913   1.00 12.92 ?  62  GLN   A HB3  1 
ATOM   1390 H HG2  . GLN   A 1 62  ? 29.906 11.868  2.655   1.00 12.81 ?  62  GLN   A HG2  1 
ATOM   1391 H HG3  . GLN   A 1 62  ? 31.365 11.271  2.875   1.00 12.81 ?  62  GLN   A HG3  1 
ATOM   1392 H HE21 . GLN   A 1 62  ? 31.921 9.514   1.655   1.00 13.97 ?  62  GLN   A HE21 1 
ATOM   1393 H HE22 . GLN   A 1 62  ? 30.972 8.626   0.927   1.00 13.97 ?  62  GLN   A HE22 1 
ATOM   1394 N N    . VAL   A 1 63  ? 32.681 10.607  6.122   1.00 11.14 ?  63  VAL   A N    1 
ATOM   1395 C CA   . VAL   A 1 63  ? 34.072 11.002  6.334   1.00 11.95 ?  63  VAL   A CA   1 
ATOM   1396 C C    . VAL   A 1 63  ? 34.971 9.768   6.395   1.00 11.70 ?  63  VAL   A C    1 
ATOM   1397 O O    . VAL   A 1 63  ? 36.023 9.704   5.742   1.00 11.89 ?  63  VAL   A O    1 
ATOM   1398 C CB   . VAL   A 1 63  ? 34.188 11.879  7.595   1.00 13.41 ?  63  VAL   A CB   1 
ATOM   1399 C CG1  . VAL   A 1 63  ? 35.641 12.121  7.951   1.00 15.14 ?  63  VAL   A CG1  1 
ATOM   1400 C CG2  . VAL   A 1 63  ? 33.464 13.205  7.377   1.00 13.83 ?  63  VAL   A CG2  1 
ATOM   1401 H H    . VAL   A 1 63  ? 32.137 10.852  6.747   1.00 13.35 ?  63  VAL   A H    1 
ATOM   1402 H HA   . VAL   A 1 63  ? 34.354 11.540  5.579   1.00 14.32 ?  63  VAL   A HA   1 
ATOM   1403 H HB   . VAL   A 1 63  ? 33.766 11.424  8.342   1.00 16.07 ?  63  VAL   A HB   1 
ATOM   1404 H HG11 . VAL   A 1 63  ? 35.691 12.853  8.583   1.00 18.15 ?  63  VAL   A HG11 1 
ATOM   1405 H HG12 . VAL   A 1 63  ? 36.010 11.316  8.345   1.00 18.15 ?  63  VAL   A HG12 1 
ATOM   1406 H HG13 . VAL   A 1 63  ? 36.127 12.350  7.142   1.00 18.15 ?  63  VAL   A HG13 1 
ATOM   1407 H HG21 . VAL   A 1 63  ? 33.557 13.750  8.176   1.00 16.58 ?  63  VAL   A HG21 1 
ATOM   1408 H HG22 . VAL   A 1 63  ? 33.860 13.660  6.619   1.00 16.58 ?  63  VAL   A HG22 1 
ATOM   1409 H HG23 . VAL   A 1 63  ? 32.526 13.028  7.207   1.00 16.58 ?  63  VAL   A HG23 1 
ATOM   1410 N N    . GLU   A 1 64  ? 34.553 8.759   7.164   1.00 11.53 ?  64  GLU   A N    1 
ATOM   1411 C CA   . GLU   A 1 64  ? 35.316 7.523   7.258   1.00 11.23 ?  64  GLU   A CA   1 
ATOM   1412 C C    . GLU   A 1 64  ? 35.402 6.834   5.904   1.00 10.91 ?  64  GLU   A C    1 
ATOM   1413 O O    . GLU   A 1 64  ? 36.457 6.295   5.526   1.00 11.36 ?  64  GLU   A O    1 
ATOM   1414 C CB   . GLU   A 1 64  ? 34.634 6.613   8.282   1.00 12.07 ?  64  GLU   A CB   1 
ATOM   1415 C CG   . GLU   A 1 64  ? 35.286 5.264   8.435   1.00 12.64 ?  64  GLU   A CG   1 
ATOM   1416 C CD   . GLU   A 1 64  ? 34.409 4.268   9.163   1.00 13.18 ?  64  GLU   A CD   1 
ATOM   1417 O OE1  . GLU   A 1 64  ? 33.172 4.357   9.029   1.00 14.12 ?  64  GLU   A OE1  1 
ATOM   1418 O OE2  . GLU   A 1 64  ? 34.962 3.376   9.847   1.00 13.44 -1 64  GLU   A OE2  1 
ATOM   1419 H H    . GLU   A 1 64  ? 33.827 8.766   7.624   1.00 13.81 ?  64  GLU   A H    1 
ATOM   1420 H HA   . GLU   A 1 64  ? 36.217 7.724   7.568   1.00 13.46 ?  64  GLU   A HA   1 
ATOM   1421 H HB2  . GLU   A 1 64  ? 34.658 7.055   9.150   1.00 14.47 ?  64  GLU   A HB2  1 
ATOM   1422 H HB3  . GLU   A 1 64  ? 33.716 6.481   8.009   1.00 14.47 ?  64  GLU   A HB3  1 
ATOM   1423 H HG2  . GLU   A 1 64  ? 35.483 4.896   7.556   1.00 15.14 ?  64  GLU   A HG2  1 
ATOM   1424 H HG3  . GLU   A 1 64  ? 36.108 5.367   8.937   1.00 15.14 ?  64  GLU   A HG3  1 
ATOM   1425 N N    . SER   A 1 65  ? 34.284 6.819   5.175   1.00 10.53 ?  65  SER   A N    1 
ATOM   1426 C CA   . SER   A 1 65  ? 34.227 6.162   3.875   1.00 10.46 ?  65  SER   A CA   1 
ATOM   1427 C C    . SER   A 1 65  ? 35.149 6.828   2.864   1.00 10.85 ?  65  SER   A C    1 
ATOM   1428 O O    . SER   A 1 65  ? 35.784 6.145   2.053   1.00 11.63 ?  65  SER   A O    1 
ATOM   1429 C CB   . SER   A 1 65  ? 32.794 6.171   3.342   1.00 10.88 ?  65  SER   A CB   1 
ATOM   1430 O OG   . SER   A 1 65  ? 31.939 5.355   4.132   1.00 11.31 ?  65  SER   A OG   1 
ATOM   1431 H H    . SER   A 1 65  ? 33.547 7.188   5.415   1.00 12.61 ?  65  SER   A H    1 
ATOM   1432 H HA   . SER   A 1 65  ? 34.509 5.241   3.973   1.00 12.52 ?  65  SER   A HA   1 
ATOM   1433 H HB2  . SER   A 1 65  ? 32.458 7.078   3.358   1.00 13.04 ?  65  SER   A HB2  1 
ATOM   1434 H HB3  . SER   A 1 65  ? 32.799 5.834   2.434   1.00 13.04 ?  65  SER   A HB3  1 
ATOM   1435 H HG   . SER   A 1 65  ? 31.933 5.630   4.930   1.00 13.55 ?  65  SER   A HG   1 
ATOM   1436 N N    . ASP   A 1 66  ? 35.223 8.161   2.877   1.00 10.98 ?  66  ASP   A N    1 
ATOM   1437 C CA   . ASP   A 1 66  ? 36.085 8.856   1.925   1.00 11.95 ?  66  ASP   A CA   1 
ATOM   1438 C C    . ASP   A 1 66  ? 37.549 8.502   2.166   1.00 11.76 ?  66  ASP   A C    1 
ATOM   1439 O O    . ASP   A 1 66  ? 38.323 8.328   1.216   1.00 12.84 ?  66  ASP   A O    1 
ATOM   1440 C CB   . ASP   A 1 66  ? 35.867 10.364  2.020   1.00 12.98 ?  66  ASP   A CB   1 
ATOM   1441 C CG   . ASP   A 1 66  ? 34.530 10.824  1.423   1.00 14.61 ?  66  ASP   A CG   1 
ATOM   1442 O OD1  . ASP   A 1 66  ? 33.816 10.022  0.782   1.00 15.13 ?  66  ASP   A OD1  1 
ATOM   1443 O OD2  . ASP   A 1 66  ? 34.223 12.022  1.581   1.00 17.72 -1 66  ASP   A OD2  1 
ATOM   1444 H H    . ASP   A 1 66  ? 34.785 8.678   3.415   1.00 13.15 ?  66  ASP   A H    1 
ATOM   1445 H HA   . ASP   A 1 66  ? 35.848 8.576   1.027   1.00 14.32 ?  66  ASP   A HA   1 
ATOM   1446 H HB2  . ASP   A 1 66  ? 35.882 10.629  2.952   1.00 15.55 ?  66  ASP   A HB2  1 
ATOM   1447 H HB3  . ASP   A 1 66  ? 36.580 10.814  1.537   1.00 15.55 ?  66  ASP   A HB3  1 
ATOM   1448 N N    . ASP   A 1 67  ? 37.944 8.385   3.432   1.00 11.74 ?  67  ASP   A N    1 
ATOM   1449 C CA   . ASP   A 1 67  ? 39.298 7.938   3.736   1.00 12.72 ?  67  ASP   A CA   1 
ATOM   1450 C C    . ASP   A 1 67  ? 39.525 6.507   3.263   1.00 12.85 ?  67  ASP   A C    1 
ATOM   1451 O O    . ASP   A 1 67  ? 40.589 6.187   2.720   1.00 13.35 ?  67  ASP   A O    1 
ATOM   1452 C CB   . ASP   A 1 67  ? 39.568 8.073   5.233   1.00 13.78 ?  67  ASP   A CB   1 
ATOM   1453 C CG   . ASP   A 1 67  ? 40.875 7.418   5.653   1.00 15.37 ?  67  ASP   A CG   1 
ATOM   1454 O OD1  . ASP   A 1 67  ? 41.944 8.059   5.517   1.00 18.48 ?  67  ASP   A OD1  1 
ATOM   1455 O OD2  . ASP   A 1 67  ? 40.831 6.256   6.113   1.00 15.03 -1 67  ASP   A OD2  1 
ATOM   1456 H H    . ASP   A 1 67  ? 37.459 8.557   4.118   1.00 14.06 ?  67  ASP   A H    1 
ATOM   1457 H HA   . ASP   A 1 67  ? 39.928 8.504   3.264   1.00 15.25 ?  67  ASP   A HA   1 
ATOM   1458 H HB2  . ASP   A 1 67  ? 39.617 9.013   5.453   1.00 16.51 ?  67  ASP   A HB2  1 
ATOM   1459 H HB3  . ASP   A 1 67  ? 38.844 7.650   5.721   1.00 16.51 ?  67  ASP   A HB3  1 
ATOM   1460 N N    . TYR   A 1 68  ? 38.531 5.627   3.452   1.00 12.00 ?  68  TYR   A N    1 
ATOM   1461 C CA   . TYR   A 1 68  ? 38.657 4.246   2.983   1.00 12.14 ?  68  TYR   A CA   1 
ATOM   1462 C C    . TYR   A 1 68  ? 38.894 4.197   1.476   1.00 12.40 ?  68  TYR   A C    1 
ATOM   1463 O O    . TYR   A 1 68  ? 39.772 3.465   1.001   1.00 12.88 ?  68  TYR   A O    1 
ATOM   1464 C CB   . TYR   A 1 68  ? 37.407 3.420   3.362   1.00 12.64 ?  68  TYR   A CB   1 
ATOM   1465 C CG   . TYR   A 1 68  ? 37.433 2.034   2.733   1.00 13.92 ?  68  TYR   A CG   1 
ATOM   1466 C CD1  . TYR   A 1 68  ? 36.970 1.841   1.435   1.00 15.24 ?  68  TYR   A CD1  1 
ATOM   1467 C CD2  . TYR   A 1 68  ? 37.983 0.951   3.399   1.00 15.88 ?  68  TYR   A CD2  1 
ATOM   1468 C CE1  . TYR   A 1 68  ? 37.042 0.624   0.818   1.00 16.76 ?  68  TYR   A CE1  1 
ATOM   1469 C CE2  . TYR   A 1 68  ? 38.048 -0.305  2.787   1.00 16.32 ?  68  TYR   A CE2  1 
ATOM   1470 C CZ   . TYR   A 1 68  ? 37.579 -0.445  1.495   1.00 16.84 ?  68  TYR   A CZ   1 
ATOM   1471 O OH   . TYR   A 1 68  ? 37.672 -1.659  0.870   1.00 17.98 ?  68  TYR   A OH   1 
ATOM   1472 H H    . TYR   A 1 68  ? 37.778 5.803   3.841   1.00 14.37 ?  68  TYR   A H    1 
ATOM   1473 H HA   . TYR   A 1 68  ? 39.416 3.838   3.414   1.00 14.54 ?  68  TYR   A HA   1 
ATOM   1474 H HB2  . TYR   A 1 68  ? 37.372 3.313   4.325   1.00 15.15 ?  68  TYR   A HB2  1 
ATOM   1475 H HB3  . TYR   A 1 68  ? 36.608 3.879   3.048   1.00 15.15 ?  68  TYR   A HB3  1 
ATOM   1476 H HD1  . TYR   A 1 68  ? 36.613 2.563   0.968   1.00 18.27 ?  68  TYR   A HD1  1 
ATOM   1477 H HD2  . TYR   A 1 68  ? 38.320 1.059   4.256   1.00 19.03 ?  68  TYR   A HD2  1 
ATOM   1478 H HE1  . TYR   A 1 68  ? 36.717 0.516   -0.047  1.00 20.09 ?  68  TYR   A HE1  1 
ATOM   1479 H HE2  . TYR   A 1 68  ? 38.427 -1.030  3.227   1.00 19.56 ?  68  TYR   A HE2  1 
ATOM   1480 H HH   . TYR   A 1 68  ? 38.008 -2.230  1.395   1.00 21.55 ?  68  TYR   A HH   1 
ATOM   1481 N N    . ILE   A 1 69  ? 38.105 4.956   0.703   1.00 11.74 ?  69  ILE   A N    1 
ATOM   1482 C CA   . ILE   A 1 69  ? 38.246 4.939   -0.752  1.00 11.92 ?  69  ILE   A CA   1 
ATOM   1483 C C    . ILE   A 1 69  ? 39.576 5.551   -1.180  1.00 11.80 ?  69  ILE   A C    1 
ATOM   1484 O O    . ILE   A 1 69  ? 40.224 5.062   -2.111  1.00 12.37 ?  69  ILE   A O    1 
ATOM   1485 C CB   . ILE   A 1 69  ? 37.047 5.640   -1.423  1.00 12.82 ?  69  ILE   A CB   1 
ATOM   1486 C CG1  . ILE   A 1 69  ? 35.733 4.907   -1.129  1.00 13.47 ?  69  ILE   A CG1  1 
ATOM   1487 C CG2  . ILE   A 1 69  ? 37.292 5.824   -2.930  1.00 14.04 ?  69  ILE   A CG2  1 
ATOM   1488 C CD1  . ILE   A 1 69  ? 35.557 3.611   -1.878  1.00 14.18 ?  69  ILE   A CD1  1 
ATOM   1489 H H    . ILE   A 1 69  ? 37.493 5.487   0.993   1.00 14.06 ?  69  ILE   A H    1 
ATOM   1490 H HA   . ILE   A 1 69  ? 38.246 4.016   -1.047  1.00 14.28 ?  69  ILE   A HA   1 
ATOM   1491 H HB   . ILE   A 1 69  ? 36.976 6.522   -1.039  1.00 15.36 ?  69  ILE   A HB   1 
ATOM   1492 H HG12 . ILE   A 1 69  ? 35.699 4.705   -0.180  1.00 16.15 ?  69  ILE   A HG12 1 
ATOM   1493 H HG13 . ILE   A 1 69  ? 34.996 5.488   -1.366  1.00 16.15 ?  69  ILE   A HG13 1 
ATOM   1494 H HG21 . ILE   A 1 69  ? 36.447 6.027   -3.366  1.00 16.82 ?  69  ILE   A HG21 1 
ATOM   1495 H HG22 . ILE   A 1 69  ? 37.913 6.560   -3.066  1.00 16.82 ?  69  ILE   A HG22 1 
ATOM   1496 H HG23 . ILE   A 1 69  ? 37.662 5.007   -3.299  1.00 16.82 ?  69  ILE   A HG23 1 
ATOM   1497 H HD11 . ILE   A 1 69  ? 34.750 3.176   -1.563  1.00 16.99 ?  69  ILE   A HD11 1 
ATOM   1498 H HD12 . ILE   A 1 69  ? 35.480 3.803   -2.826  1.00 16.99 ?  69  ILE   A HD12 1 
ATOM   1499 H HD13 . ILE   A 1 69  ? 36.325 3.043   -1.715  1.00 16.99 ?  69  ILE   A HD13 1 
ATOM   1500 N N    . ALA   A 1 70  ? 39.993 6.631   -0.525  1.00 12.11 ?  70  ALA   A N    1 
ATOM   1501 C CA   . ALA   A 1 70  ? 41.270 7.246   -0.875  1.00 13.12 ?  70  ALA   A CA   1 
ATOM   1502 C C    . ALA   A 1 70  ? 42.422 6.262   -0.706  1.00 13.60 ?  70  ALA   A C    1 
ATOM   1503 O O    . ALA   A 1 70  ? 43.394 6.303   -1.464  1.00 15.42 ?  70  ALA   A O    1 
ATOM   1504 C CB   . ALA   A 1 70  ? 41.502 8.499   -0.028  1.00 13.79 ?  70  ALA   A CB   1 
ATOM   1505 H H    . ALA   A 1 70  ? 39.561 7.022   0.103   1.00 14.51 ?  70  ALA   A H    1 
ATOM   1506 H HA   . ALA   A 1 70  ? 41.244 7.522   -1.805  1.00 15.73 ?  70  ALA   A HA   1 
ATOM   1507 H HB1  . ALA   A 1 70  ? 42.358 8.893   -0.273  1.00 16.52 ?  70  ALA   A HB1  1 
ATOM   1508 H HB2  . ALA   A 1 70  ? 40.790 9.135   -0.194  1.00 16.52 ?  70  ALA   A HB2  1 
ATOM   1509 H HB3  . ALA   A 1 70  ? 41.513 8.252   0.910   1.00 16.52 ?  70  ALA   A HB3  1 
ATOM   1510 N N    . THR   A 1 71  ? 42.320 5.354   0.264   1.00 13.01 ?  71  THR   A N    1 
ATOM   1511 C CA   . THR   A 1 71  ? 43.374 4.379   0.517   1.00 14.38 ?  71  THR   A CA   1 
ATOM   1512 C C    . THR   A 1 71  ? 43.258 3.158   -0.384  1.00 14.57 ?  71  THR   A C    1 
ATOM   1513 O O    . THR   A 1 71  ? 44.271 2.654   -0.884  1.00 16.82 ?  71  THR   A O    1 
ATOM   1514 C CB   . THR   A 1 71  ? 43.307 3.931   1.974   1.00 16.61 ?  71  THR   A CB   1 
ATOM   1515 O OG1  . THR   A 1 71  ? 43.567 5.057   2.817   1.00 18.07 ?  71  THR   A OG1  1 
ATOM   1516 C CG2  . THR   A 1 71  ? 44.309 2.812   2.266   1.00 18.26 ?  71  THR   A CG2  1 
ATOM   1517 H H    . THR   A 1 71  ? 41.641 5.273   0.782   1.00 15.59 ?  71  THR   A H    1 
ATOM   1518 H HA   . THR   A 1 71  ? 44.237 4.785   0.354   1.00 17.23 ?  71  THR   A HA   1 
ATOM   1519 H HB   . THR   A 1 71  ? 42.417 3.585   2.158   1.00 19.91 ?  71  THR   A HB   1 
ATOM   1520 H HG1  . THR   A 1 71  ? 42.987 5.645   2.685   1.00 21.66 ?  71  THR   A HG1  1 
ATOM   1521 H HG21 . THR   A 1 71  ? 44.443 2.733   3.224   1.00 21.89 ?  71  THR   A HG21 1 
ATOM   1522 H HG22 . THR   A 1 71  ? 43.981 1.964   1.926   1.00 21.89 ?  71  THR   A HG22 1 
ATOM   1523 H HG23 . THR   A 1 71  ? 45.161 3.012   1.846   1.00 21.89 ?  71  THR   A HG23 1 
ATOM   1524 N N    . ASN   A 1 72  ? 42.036 2.652   -0.575  1.00 13.52 ?  72  ASN   A N    1 
ATOM   1525 C CA   . ASN   A 1 72  ? 41.813 1.326   -1.135  1.00 14.02 ?  72  ASN   A CA   1 
ATOM   1526 C C    . ASN   A 1 72  ? 41.189 1.316   -2.519  1.00 14.06 ?  72  ASN   A C    1 
ATOM   1527 O O    . ASN   A 1 72  ? 41.189 0.260   -3.167  1.00 15.51 ?  72  ASN   A O    1 
ATOM   1528 C CB   . ASN   A 1 72  ? 40.929 0.505   -0.188  1.00 14.97 ?  72  ASN   A CB   1 
ATOM   1529 C CG   . ASN   A 1 72  ? 41.554 0.351   1.174   1.00 15.93 ?  72  ASN   A CG   1 
ATOM   1530 O OD1  . ASN   A 1 72  ? 41.094 0.937   2.150   1.00 17.76 ?  72  ASN   A OD1  1 
ATOM   1531 N ND2  . ASN   A 1 72  ? 42.623 -0.417  1.247   1.00 16.35 ?  72  ASN   A ND2  1 
ATOM   1532 H H    . ASN   A 1 72  ? 41.304 3.072   -0.391  1.00 16.21 ?  72  ASN   A H    1 
ATOM   1533 H HA   . ASN   A 1 72  ? 42.665 0.874   -1.206  1.00 16.80 ?  72  ASN   A HA   1 
ATOM   1534 H HB2  . ASN   A 1 72  ? 40.074 0.946   -0.083  1.00 17.95 ?  72  ASN   A HB2  1 
ATOM   1535 H HB3  . ASN   A 1 72  ? 40.804 -0.384  -0.560  1.00 17.95 ?  72  ASN   A HB3  1 
ATOM   1536 H HD21 . ASN   A 1 72  ? 43.021 -0.528  2.003   1.00 19.60 ?  72  ASN   A HD21 1 
ATOM   1537 H HD22 . ASN   A 1 72  ? 42.925 -0.804  0.543   1.00 19.60 ?  72  ASN   A HD22 1 
ATOM   1538 N N    . GLY   A 1 73  ? 40.632 2.431   -2.975  1.00 13.60 ?  73  GLY   A N    1 
ATOM   1539 C CA   . GLY   A 1 73  ? 39.889 2.440   -4.209  1.00 13.29 ?  73  GLY   A CA   1 
ATOM   1540 C C    . GLY   A 1 73  ? 38.501 1.855   -4.040  1.00 12.42 ?  73  GLY   A C    1 
ATOM   1541 O O    . GLY   A 1 73  ? 38.114 1.403   -2.956  1.00 12.97 ?  73  GLY   A O    1 
ATOM   1542 H H    . GLY   A 1 73  ? 40.677 3.204   -2.585  1.00 16.29 ?  73  GLY   A H    1 
ATOM   1543 H HA2  . GLY   A 1 73  ? 39.808 3.360   -4.528  1.00 15.93 ?  73  GLY   A HA2  1 
ATOM   1544 H HA3  . GLY   A 1 73  ? 40.365 1.928   -4.880  1.00 15.93 ?  73  GLY   A HA3  1 
ATOM   1545 N N    . PRO   A 1 74  ? 37.722 1.876   -5.120  1.00 13.07 ?  74  PRO   A N    1 
ATOM   1546 C CA   . PRO   A 1 74  ? 36.326 1.441   -5.034  1.00 13.25 ?  74  PRO   A CA   1 
ATOM   1547 C C    . PRO   A 1 74  ? 36.181 -0.042  -4.720  1.00 12.54 ?  74  PRO   A C    1 
ATOM   1548 O O    . PRO   A 1 74  ? 37.054 -0.869  -5.004  1.00 13.69 ?  74  PRO   A O    1 
ATOM   1549 C CB   . PRO   A 1 74  ? 35.772 1.748   -6.430  1.00 15.01 ?  74  PRO   A CB   1 
ATOM   1550 C CG   . PRO   A 1 74  ? 36.707 2.749   -7.019  1.00 17.67 ?  74  PRO   A CG   1 
ATOM   1551 C CD   . PRO   A 1 74  ? 38.050 2.403   -6.454  1.00 15.04 ?  74  PRO   A CD   1 
ATOM   1552 H HA   . PRO   A 1 74  ? 35.845 1.962   -4.369  1.00 15.88 ?  74  PRO   A HA   1 
ATOM   1553 H HB2  . PRO   A 1 74  ? 35.754 0.935   -6.958  1.00 17.99 ?  74  PRO   A HB2  1 
ATOM   1554 H HB3  . PRO   A 1 74  ? 34.876 2.120   -6.348  1.00 17.99 ?  74  PRO   A HB3  1 
ATOM   1555 H HG2  . PRO   A 1 74  ? 36.710 2.666   -7.984  1.00 21.18 ?  74  PRO   A HG2  1 
ATOM   1556 H HG3  . PRO   A 1 74  ? 36.444 3.642   -6.750  1.00 21.18 ?  74  PRO   A HG3  1 
ATOM   1557 H HD2  . PRO   A 1 74  ? 38.483 1.720   -6.993  1.00 18.02 ?  74  PRO   A HD2  1 
ATOM   1558 H HD3  . PRO   A 1 74  ? 38.601 3.201   -6.388  1.00 18.02 ?  74  PRO   A HD3  1 
ATOM   1559 N N    . LEU   A 1 75  ? 35.038 -0.372  -4.125  1.00 12.11 ?  75  LEU   A N    1 
ATOM   1560 C CA   . LEU   A 1 75  ? 34.646 -1.764  -3.967  1.00 11.58 ?  75  LEU   A CA   1 
ATOM   1561 C C    . LEU   A 1 75  ? 34.271 -2.355  -5.324  1.00 12.24 ?  75  LEU   A C    1 
ATOM   1562 O O    . LEU   A 1 75  ? 34.112 -1.645  -6.320  1.00 13.74 ?  75  LEU   A O    1 
ATOM   1563 C CB   . LEU   A 1 75  ? 33.452 -1.888  -3.023  1.00 11.88 ?  75  LEU   A CB   1 
ATOM   1564 C CG   . LEU   A 1 75  ? 33.661 -1.461  -1.576  1.00 13.40 ?  75  LEU   A CG   1 
ATOM   1565 C CD1  . LEU   A 1 75  ? 32.375 -1.650  -0.785  1.00 15.35 ?  75  LEU   A CD1  1 
ATOM   1566 C CD2  . LEU   A 1 75  ? 34.799 -2.183  -0.906  1.00 16.80 ?  75  LEU   A CD2  1 
ATOM   1567 H H    . LEU   A 1 75  ? 34.471 0.192   -3.807  1.00 14.51 ?  75  LEU   A H    1 
ATOM   1568 H HA   . LEU   A 1 75  ? 35.388 -2.269  -3.606  1.00 13.87 ?  75  LEU   A HA   1 
ATOM   1569 H HB2  . LEU   A 1 75  ? 32.727 -1.355  -3.381  1.00 14.23 ?  75  LEU   A HB2  1 
ATOM   1570 H HB3  . LEU   A 1 75  ? 33.180 -2.824  -3.011  1.00 14.23 ?  75  LEU   A HB3  1 
ATOM   1571 H HG   . LEU   A 1 75  ? 33.878 -0.516  -1.567  1.00 16.05 ?  75  LEU   A HG   1 
ATOM   1572 H HD11 . LEU   A 1 75  ? 32.527 -1.367  0.132   1.00 18.39 ?  75  LEU   A HD11 1 
ATOM   1573 H HD12 . LEU   A 1 75  ? 31.680 -1.106  -1.187  1.00 18.39 ?  75  LEU   A HD12 1 
ATOM   1574 H HD13 . LEU   A 1 75  ? 32.124 -2.583  -0.808  1.00 18.39 ?  75  LEU   A HD13 1 
ATOM   1575 H HD21 . LEU   A 1 75  ? 34.842 -1.913  0.025   1.00 20.13 ?  75  LEU   A HD21 1 
ATOM   1576 H HD22 . LEU   A 1 75  ? 34.650 -3.139  -0.967  1.00 20.13 ?  75  LEU   A HD22 1 
ATOM   1577 H HD23 . LEU   A 1 75  ? 35.632 -1.951  -1.353  1.00 20.13 ?  75  LEU   A HD23 1 
ATOM   1578 N N    . LYS   A 1 76  ? 34.129 -3.678  -5.347  1.00 12.57 ?  76  LYS   A N    1 
ATOM   1579 C CA   . LYS   A 1 76  ? 33.533 -4.404  -6.464  1.00 12.84 ?  76  LYS   A CA   1 
ATOM   1580 C C    . LYS   A 1 76  ? 32.019 -4.474  -6.282  1.00 11.91 ?  76  LYS   A C    1 
ATOM   1581 O O    . LYS   A 1 76  ? 31.521 -4.572  -5.160  1.00 11.93 ?  76  LYS   A O    1 
ATOM   1582 C CB   . LYS   A 1 76  ? 34.072 -5.843  -6.505  1.00 14.76 ?  76  LYS   A CB   1 
ATOM   1583 C CG   . LYS   A 1 76  ? 35.583 -5.949  -6.698  1.00 16.12 ?  76  LYS   A CG   1 
ATOM   1584 C CD   . LYS   A 1 76  ? 36.108 -7.350  -6.466  1.00 17.29 ?  76  LYS   A CD   1 
ATOM   1585 C CE   . LYS   A 1 76  ? 37.604 -7.413  -6.683  1.00 19.76 ?  76  LYS   A CE   1 
ATOM   1586 N NZ   . LYS   A 1 76  ? 38.141 -8.767  -6.468  1.00 20.72 ?  76  LYS   A NZ   1 
ATOM   1587 H H    . LYS   A 1 76  ? 34.381 -4.196  -4.704  1.00 15.06 ?  76  LYS   A H    1 
ATOM   1588 H HA   . LYS   A 1 76  ? 33.739 -3.959  -7.302  1.00 15.39 ?  76  LYS   A HA   1 
ATOM   1589 H HB2  . LYS   A 1 76  ? 33.851 -6.279  -5.671  1.00 17.69 ?  76  LYS   A HB2  1 
ATOM   1590 H HB3  . LYS   A 1 76  ? 33.649 -6.307  -7.244  1.00 17.69 ?  76  LYS   A HB3  1 
ATOM   1591 H HG2  . LYS   A 1 76  ? 35.804 -5.692  -7.608  1.00 19.32 ?  76  LYS   A HG2  1 
ATOM   1592 H HG3  . LYS   A 1 76  ? 36.025 -5.357  -6.070  1.00 19.32 ?  76  LYS   A HG3  1 
ATOM   1593 H HD2  . LYS   A 1 76  ? 35.915 -7.619  -5.554  1.00 20.73 ?  76  LYS   A HD2  1 
ATOM   1594 H HD3  . LYS   A 1 76  ? 35.679 -7.961  -7.091  1.00 20.73 ?  76  LYS   A HD3  1 
ATOM   1595 H HE2  . LYS   A 1 76  ? 37.802 -7.151  -7.594  1.00 23.68 ?  76  LYS   A HE2  1 
ATOM   1596 H HE3  . LYS   A 1 76  ? 38.038 -6.816  -6.058  1.00 23.68 ?  76  LYS   A HE3  1 
ATOM   1597 H HZ1  . LYS   A 1 76  ? 39.019 -8.780  -6.603  1.00 24.84 ?  76  LYS   A HZ1  1 
ATOM   1598 H HZ2  . LYS   A 1 76  ? 37.972 -9.041  -5.636  1.00 24.84 ?  76  LYS   A HZ2  1 
ATOM   1599 H HZ3  . LYS   A 1 76  ? 37.758 -9.346  -7.036  1.00 24.84 ?  76  LYS   A HZ3  1 
ATOM   1600 N N    . VAL   A 1 77  ? 31.282 -4.460  -7.396  1.00 12.39 ?  77  VAL   A N    1 
ATOM   1601 C CA   . VAL   A 1 77  ? 29.873 -4.834  -7.319  1.00 12.51 ?  77  VAL   A CA   1 
ATOM   1602 C C    . VAL   A 1 77  ? 29.796 -6.285  -6.871  1.00 12.10 ?  77  VAL   A C    1 
ATOM   1603 O O    . VAL   A 1 77  ? 30.458 -7.160  -7.441  1.00 12.45 ?  77  VAL   A O    1 
ATOM   1604 C CB   . VAL   A 1 77  ? 29.166 -4.628  -8.667  1.00 14.00 ?  77  VAL   A CB   1 
ATOM   1605 C CG1  . VAL   A 1 77  ? 27.703 -5.056  -8.568  1.00 14.85 ?  77  VAL   A CG1  1 
ATOM   1606 C CG2  . VAL   A 1 77  ? 29.278 -3.182  -9.109  1.00 15.45 ?  77  VAL   A CG2  1 
ATOM   1607 H H    . VAL   A 1 77  ? 31.569 -4.249  -8.177  1.00 14.84 ?  77  VAL   A H    1 
ATOM   1608 H HA   . VAL   A 1 77  ? 29.433 -4.283  -6.653  1.00 14.99 ?  77  VAL   A HA   1 
ATOM   1609 H HB   . VAL   A 1 77  ? 29.600 -5.180  -9.337  1.00 16.78 ?  77  VAL   A HB   1 
ATOM   1610 H HG11 . VAL   A 1 77  ? 27.242 -4.771  -9.369  1.00 17.80 ?  77  VAL   A HG11 1 
ATOM   1611 H HG12 . VAL   A 1 77  ? 27.662 -6.022  -8.487  1.00 17.80 ?  77  VAL   A HG12 1 
ATOM   1612 H HG13 . VAL   A 1 77  ? 27.308 -4.640  -7.788  1.00 17.80 ?  77  VAL   A HG13 1 
ATOM   1613 H HG21 . VAL   A 1 77  ? 28.774 -3.067  -9.929  1.00 18.51 ?  77  VAL   A HG21 1 
ATOM   1614 H HG22 . VAL   A 1 77  ? 28.915 -2.613  -8.413  1.00 18.51 ?  77  VAL   A HG22 1 
ATOM   1615 H HG23 . VAL   A 1 77  ? 30.212 -2.969  -9.259  1.00 18.51 ?  77  VAL   A HG23 1 
ATOM   1616 N N    . GLY   A 1 78  ? 28.999 -6.547  -5.834  1.00 11.59 ?  78  GLY   A N    1 
ATOM   1617 C CA   . GLY   A 1 78  ? 28.979 -7.834  -5.170  1.00 11.77 ?  78  GLY   A CA   1 
ATOM   1618 C C    . GLY   A 1 78  ? 29.893 -7.922  -3.968  1.00 11.41 ?  78  GLY   A C    1 
ATOM   1619 O O    . GLY   A 1 78  ? 29.836 -8.926  -3.237  1.00 12.14 ?  78  GLY   A O    1 
ATOM   1620 H H    . GLY   A 1 78  ? 28.442 -5.976  -5.502  1.00 13.88 ?  78  GLY   A H    1 
ATOM   1621 H HA2  . GLY   A 1 78  ? 28.074 -8.021  -4.878  1.00 14.11 ?  78  GLY   A HA2  1 
ATOM   1622 H HA3  . GLY   A 1 78  ? 29.238 -8.518  -5.808  1.00 14.11 ?  78  GLY   A HA3  1 
ATOM   1623 N N    . GLY   A 1 79  ? 30.747 -6.915  -3.751  1.00 11.30 ?  79  GLY   A N    1 
ATOM   1624 C CA   . GLY   A 1 79  ? 31.709 -6.926  -2.673  1.00 11.56 ?  79  GLY   A CA   1 
ATOM   1625 C C    . GLY   A 1 79  ? 31.256 -6.132  -1.461  1.00 10.95 ?  79  GLY   A C    1 
ATOM   1626 O O    . GLY   A 1 79  ? 30.133 -5.629  -1.385  1.00 11.74 ?  79  GLY   A O    1 
ATOM   1627 H H    . GLY   A 1 79  ? 30.795 -6.207  -4.240  1.00 13.53 ?  79  GLY   A H    1 
ATOM   1628 H HA2  . GLY   A 1 79  ? 31.867 -7.851  -2.398  1.00 13.85 ?  79  GLY   A HA2  1 
ATOM   1629 H HA3  . GLY   A 1 79  ? 32.550 -6.562  -2.984  1.00 13.85 ?  79  GLY   A HA3  1 
ATOM   1630 N N    . SER   A 1 80  ? 32.158 -6.031  -0.488  1.00 12.10 ?  80  SER   A N    1 
ATOM   1631 C CA   . SER   A 1 80  ? 31.837 -5.403  0.785   1.00 11.21 ?  80  SER   A CA   1 
ATOM   1632 C C    . SER   A 1 80  ? 33.107 -4.948  1.487   1.00 11.25 ?  80  SER   A C    1 
ATOM   1633 O O    . SER   A 1 80  ? 34.220 -5.378  1.162   1.00 12.72 ?  80  SER   A O    1 
ATOM   1634 C CB   . SER   A 1 80  ? 31.079 -6.367  1.702   1.00 12.14 ?  80  SER   A CB   1 
ATOM   1635 O OG   . SER   A 1 80  ? 31.914 -7.415  2.175   1.00 14.05 ?  80  SER   A OG   1 
ATOM   1636 H H    . SER   A 1 80  ? 32.969 -6.307  -0.550  1.00 14.49 ?  80  SER   A H    1 
ATOM   1637 H HA   . SER   A 1 80  ? 31.280 -4.626  0.612   1.00 13.43 ?  80  SER   A HA   1 
ATOM   1638 H HB2  . SER   A 1 80  ? 30.737 -5.872  2.459   1.00 14.55 ?  80  SER   A HB2  1 
ATOM   1639 H HB3  . SER   A 1 80  ? 30.340 -6.753  1.200   1.00 14.55 ?  80  SER   A HB3  1 
ATOM   1640 H HG   . SER   A 1 80  ? 32.212 -7.855  1.521   1.00 16.84 ?  80  SER   A HG   1 
ATOM   1641 N N    . CYS   A 1 81  ? 32.916 -4.097  2.494   1.00 10.98 ?  81  CYS   A N    1 
ATOM   1642 C CA   . CYS   A 1 81  ? 33.968 -3.807  3.458   1.00 10.84 ?  81  CYS   A CA   1 
ATOM   1643 C C    . CYS   A 1 81  ? 33.325 -3.574  4.818   1.00 10.94 ?  81  CYS   A C    1 
ATOM   1644 O O    . CYS   A 1 81  ? 32.157 -3.175  4.907   1.00 12.01 ?  81  CYS   A O    1 
ATOM   1645 C CB   . CYS   A 1 81  ? 34.837 -2.615  3.038   1.00 11.61 ?  81  CYS   A CB   1 
ATOM   1646 S SG   . CYS   A 1 81  ? 33.930 -1.038  3.059   1.00 11.84 ?  81  CYS   A SG   1 
ATOM   1647 H H    . CYS   A 1 81  ? 32.178 -3.679  2.645   1.00 13.16 ?  81  CYS   A H    1 
ATOM   1648 H HA   . CYS   A 1 81  ? 34.547 -4.579  3.529   1.00 12.99 ?  81  CYS   A HA   1 
ATOM   1649 H HB2  . CYS   A 1 81  ? 35.590 -2.542  3.648   1.00 13.91 ?  81  CYS   A HB2  1 
ATOM   1650 H HB3  . CYS   A 1 81  ? 35.165 -2.766  2.133   1.00 13.91 ?  81  CYS   A HB3  1 
ATOM   1651 H HG   . CYS   A 1 81  ? 34.674 -0.157  2.720   1.00 14.19 ?  81  CYS   A HG   1 
ATOM   1652 N N    . VAL   A 1 82  ? 34.092 -3.840  5.875   1.00 11.43 ?  82  VAL   A N    1 
ATOM   1653 C CA   . VAL   A 1 82  ? 33.670 -3.598  7.249   1.00 11.64 ?  82  VAL   A CA   1 
ATOM   1654 C C    . VAL   A 1 82  ? 34.266 -2.280  7.718   1.00 11.67 ?  82  VAL   A C    1 
ATOM   1655 O O    . VAL   A 1 82  ? 35.491 -2.103  7.707   1.00 12.60 ?  82  VAL   A O    1 
ATOM   1656 C CB   . VAL   A 1 82  ? 34.100 -4.737  8.186   1.00 13.13 ?  82  VAL   A CB   1 
ATOM   1657 C CG1  . VAL   A 1 82  ? 33.655 -4.441  9.609   1.00 14.73 ?  82  VAL   A CG1  1 
ATOM   1658 C CG2  . VAL   A 1 82  ? 33.546 -6.065  7.713   1.00 14.17 ?  82  VAL   A CG2  1 
ATOM   1659 H H    . VAL   A 1 82  ? 34.883 -4.183  5.817   1.00 13.69 ?  82  VAL   A H    1 
ATOM   1660 H HA   . VAL   A 1 82  ? 32.701 -3.523  7.277   1.00 13.94 ?  82  VAL   A HA   1 
ATOM   1661 H HB   . VAL   A 1 82  ? 35.066 -4.793  8.183   1.00 15.74 ?  82  VAL   A HB   1 
ATOM   1662 H HG11 . VAL   A 1 82  ? 33.741 -5.246  10.140  1.00 17.65 ?  82  VAL   A HG11 1 
ATOM   1663 H HG12 . VAL   A 1 82  ? 34.211 -3.737  9.981   1.00 17.65 ?  82  VAL   A HG12 1 
ATOM   1664 H HG13 . VAL   A 1 82  ? 32.725 -4.153  9.598   1.00 17.65 ?  82  VAL   A HG13 1 
ATOM   1665 H HG21 . VAL   A 1 82  ? 33.795 -6.753  8.348   1.00 16.98 ?  82  VAL   A HG21 1 
ATOM   1666 H HG22 . VAL   A 1 82  ? 32.580 -6.002  7.654   1.00 16.98 ?  82  VAL   A HG22 1 
ATOM   1667 H HG23 . VAL   A 1 82  ? 33.918 -6.268  6.840   1.00 16.98 ?  82  VAL   A HG23 1 
ATOM   1668 N N    . LEU   A 1 83  ? 33.407 -1.358  8.140   1.00 11.53 ?  83  LEU   A N    1 
ATOM   1669 C CA   . LEU   A 1 83  ? 33.828 -0.094  8.720   1.00 11.47 ?  83  LEU   A CA   1 
ATOM   1670 C C    . LEU   A 1 83  ? 33.111 0.084   10.053  1.00 11.51 ?  83  LEU   A C    1 
ATOM   1671 O O    . LEU   A 1 83  ? 32.390 -0.802  10.518  1.00 12.19 ?  83  LEU   A O    1 
ATOM   1672 C CB   . LEU   A 1 83  ? 33.574 1.062   7.742   1.00 11.94 ?  83  LEU   A CB   1 
ATOM   1673 C CG   . LEU   A 1 83  ? 34.475 1.074   6.499   1.00 13.05 ?  83  LEU   A CG   1 
ATOM   1674 C CD1  . LEU   A 1 83  ? 34.028 2.117   5.498   1.00 13.06 ?  83  LEU   A CD1  1 
ATOM   1675 C CD2  . LEU   A 1 83  ? 35.944 1.297   6.878   1.00 13.57 ?  83  LEU   A CD2  1 
ATOM   1676 H H    . LEU   A 1 83  ? 32.552 -1.445  8.095   1.00 13.81 ?  83  LEU   A H    1 
ATOM   1677 H HA   . LEU   A 1 83  ? 34.777 -0.120  8.898   1.00 13.74 ?  83  LEU   A HA   1 
ATOM   1678 H HB2  . LEU   A 1 83  ? 32.655 1.013   7.428   1.00 14.31 ?  83  LEU   A HB2  1 
ATOM   1679 H HB3  . LEU   A 1 83  ? 33.708 1.904   8.205   1.00 14.31 ?  83  LEU   A HB3  1 
ATOM   1680 H HG   . LEU   A 1 83  ? 34.418 0.210   6.067   1.00 15.63 ?  83  LEU   A HG   1 
ATOM   1681 H HD11 . LEU   A 1 83  ? 34.620 2.090   4.726   1.00 15.65 ?  83  LEU   A HD11 1 
ATOM   1682 H HD12 . LEU   A 1 83  ? 33.120 1.918   5.221   1.00 15.65 ?  83  LEU   A HD12 1 
ATOM   1683 H HD13 . LEU   A 1 83  ? 34.065 2.993   5.910   1.00 15.65 ?  83  LEU   A HD13 1 
ATOM   1684 H HD21 . LEU   A 1 83  ? 36.464 1.443   6.068   1.00 16.26 ?  83  LEU   A HD21 1 
ATOM   1685 H HD22 . LEU   A 1 83  ? 36.011 2.081   7.451   1.00 16.26 ?  83  LEU   A HD22 1 
ATOM   1686 H HD23 . LEU   A 1 83  ? 36.279 0.518   7.345   1.00 16.26 ?  83  LEU   A HD23 1 
ATOM   1687 N N    . SER   A 1 84  ? 33.320 1.235   10.683  1.00 12.36 ?  84  SER   A N    1 
ATOM   1688 C CA   . SER   A 1 84  ? 32.672 1.487   11.959  1.00 12.28 ?  84  SER   A CA   1 
ATOM   1689 C C    . SER   A 1 84  ? 31.155 1.583   11.805  1.00 12.52 ?  84  SER   A C    1 
ATOM   1690 O O    . SER   A 1 84  ? 30.637 2.049   10.789  1.00 12.47 ?  84  SER   A O    1 
ATOM   1691 C CB   . SER   A 1 84  ? 33.173 2.803   12.542  1.00 13.57 ?  84  SER   A CB   1 
ATOM   1692 O OG   . SER   A 1 84  ? 32.549 3.082   13.775  1.00 14.41 ?  84  SER   A OG   1 
ATOM   1693 H H    . SER   A 1 84  ? 33.814 1.879   10.392  1.00 14.81 ?  84  SER   A H    1 
ATOM   1694 H HA   . SER   A 1 84  ? 32.883 0.770   12.575  1.00 14.71 ?  84  SER   A HA   1 
ATOM   1695 H HB2  . SER   A 1 84  ? 34.133 2.741   12.677  1.00 16.26 ?  84  SER   A HB2  1 
ATOM   1696 H HB3  . SER   A 1 84  ? 32.974 3.520   11.920  1.00 16.26 ?  84  SER   A HB3  1 
ATOM   1697 H HG   . SER   A 1 84  ? 32.838 3.805   14.089  1.00 17.27 ?  84  SER   A HG   1 
ATOM   1698 N N    . GLY   A 1 85  ? 30.441 1.170   12.851  1.00 13.39 ?  85  GLY   A N    1 
ATOM   1699 C CA   . GLY   A 1 85  ? 29.019 1.413   12.945  1.00 13.93 ?  85  GLY   A CA   1 
ATOM   1700 C C    . GLY   A 1 85  ? 28.654 2.727   13.595  1.00 13.54 ?  85  GLY   A C    1 
ATOM   1701 O O    . GLY   A 1 85  ? 27.463 3.038   13.712  1.00 14.44 ?  85  GLY   A O    1 
ATOM   1702 H H    . GLY   A 1 85  ? 30.769 0.742   13.523  1.00 16.04 ?  85  GLY   A H    1 
ATOM   1703 H HA2  . GLY   A 1 85  ? 28.640 1.405   12.053  1.00 16.69 ?  85  GLY   A HA2  1 
ATOM   1704 H HA3  . GLY   A 1 85  ? 28.610 0.702   13.455  1.00 16.69 ?  85  GLY   A HA3  1 
ATOM   1705 N N    . HIS   A 1 86  ? 29.641 3.501   14.039  1.00 13.32 ?  86  HIS   A N    1 
ATOM   1706 C CA   . HIS   A 1 86  ? 29.417 4.837   14.603  1.00 14.11 ?  86  HIS   A CA   1 
ATOM   1707 C C    . HIS   A 1 86  ? 28.437 4.712   15.762  1.00 14.90 ?  86  HIS   A C    1 
ATOM   1708 O O    . HIS   A 1 86  ? 28.634 3.836   16.619  1.00 16.15 ?  86  HIS   A O    1 
ATOM   1709 C CB   . HIS   A 1 86  ? 29.036 5.809   13.493  1.00 13.93 ?  86  HIS   A CB   1 
ATOM   1710 C CG   . HIS   A 1 86  ? 30.092 5.911   12.452  1.00 13.68 ?  86  HIS   A CG   1 
ATOM   1711 N ND1  . HIS   A 1 86  ? 31.183 6.742   12.588  1.00 14.73 ?  86  HIS   A ND1  1 
ATOM   1712 C CD2  . HIS   A 1 86  ? 30.275 5.223   11.302  1.00 13.35 ?  86  HIS   A CD2  1 
ATOM   1713 C CE1  . HIS   A 1 86  ? 31.982 6.576   11.549  1.00 14.34 ?  86  HIS   A CE1  1 
ATOM   1714 N NE2  . HIS   A 1 86  ? 31.459 5.655   10.760  1.00 13.72 ?  86  HIS   A NE2  1 
ATOM   1715 H H    . HIS   A 1 86  ? 30.468 3.279   14.029  1.00 15.96 ?  86  HIS   A H    1 
ATOM   1716 H HA   . HIS   A 1 86  ? 30.251 5.157   14.974  1.00 16.91 ?  86  HIS   A HA   1 
ATOM   1717 H HB2  . HIS   A 1 86  ? 28.217 5.510   13.065  1.00 16.69 ?  86  HIS   A HB2  1 
ATOM   1718 H HB3  . HIS   A 1 86  ? 28.903 6.698   13.868  1.00 16.69 ?  86  HIS   A HB3  1 
ATOM   1719 H HD2  . HIS   A 1 86  ? 29.710 4.569   10.947  1.00 16.00 ?  86  HIS   A HD2  1 
ATOM   1720 H HE1  . HIS   A 1 86  ? 32.778 7.030   11.388  1.00 17.18 ?  86  HIS   A HE1  1 
ATOM   1721 H HE2  . HIS   A 1 86  ? 31.795 5.383   10.007  1.00 16.44 ?  86  HIS   A HE2  1 
ATOM   1722 N N    . ASN   A 1 87  ? 27.414 5.551   15.834  1.00 15.93 ?  87  ASN   A N    1 
ATOM   1723 C CA   . ASN   A 1 87  ? 26.436 5.534   16.907  1.00 16.62 ?  87  ASN   A CA   1 
ATOM   1724 C C    . ASN   A 1 87  ? 25.303 4.551   16.660  1.00 17.70 ?  87  ASN   A C    1 
ATOM   1725 O O    . ASN   A 1 87  ? 24.370 4.496   17.464  1.00 20.24 ?  87  ASN   A O    1 
ATOM   1726 C CB   . ASN   A 1 87  ? 25.847 6.941   17.084  1.00 17.72 ?  87  ASN   A CB   1 
ATOM   1727 C CG   . ASN   A 1 87  ? 25.342 7.535   15.773  1.00 18.49 ?  87  ASN   A CG   1 
ATOM   1728 O OD1  . ASN   A 1 87  ? 25.988 7.425   14.732  1.00 19.05 ?  87  ASN   A OD1  1 
ATOM   1729 N ND2  . ASN   A 1 87  ? 24.186 8.172   15.825  1.00 19.97 ?  87  ASN   A ND2  1 
ATOM   1730 H H    . ASN   A 1 87  ? 27.251 6.157   15.247  1.00 19.10 ?  87  ASN   A H    1 
ATOM   1731 H HA   . ASN   A 1 87  ? 26.866 5.281   17.739  1.00 19.92 ?  87  ASN   A HA   1 
ATOM   1732 H HB2  . ASN   A 1 87  ? 25.099 6.895   17.708  1.00 21.24 ?  87  ASN   A HB2  1 
ATOM   1733 H HB3  . ASN   A 1 87  ? 26.534 7.524   17.442  1.00 21.24 ?  87  ASN   A HB3  1 
ATOM   1734 H HD21 . ASN   A 1 87  ? 23.863 8.524   15.113  1.00 23.94 ?  87  ASN   A HD21 1 
ATOM   1735 H HD22 . ASN   A 1 87  ? 23.762 8.238   16.571  1.00 23.94 ?  87  ASN   A HD22 1 
ATOM   1736 N N    A LEU   A 1 88  ? 25.367 3.772   15.584  0.66 16.57 ?  88  LEU   A N    1 
ATOM   1737 N N    B LEU   A 1 88  ? 25.361 3.767   15.583  0.34 17.08 ?  88  LEU   A N    1 
ATOM   1738 C CA   A LEU   A 1 88  ? 24.261 2.911   15.182  0.66 16.22 ?  88  LEU   A CA   1 
ATOM   1739 C CA   B LEU   A 1 88  ? 24.249 2.911   15.190  0.34 16.86 ?  88  LEU   A CA   1 
ATOM   1740 C C    A LEU   A 1 88  ? 24.487 1.438   15.493  0.66 15.73 ?  88  LEU   A C    1 
ATOM   1741 C C    B LEU   A 1 88  ? 24.487 1.427   15.431  0.34 16.23 ?  88  LEU   A C    1 
ATOM   1742 O O    A LEU   A 1 88  ? 23.514 0.709   15.713  0.66 16.95 ?  88  LEU   A O    1 
ATOM   1743 O O    B LEU   A 1 88  ? 23.513 0.674   15.532  0.34 16.81 ?  88  LEU   A O    1 
ATOM   1744 C CB   A LEU   A 1 88  ? 24.013 3.058   13.678  0.66 16.77 ?  88  LEU   A CB   1 
ATOM   1745 C CB   B LEU   A 1 88  ? 23.931 3.116   13.703  0.34 17.40 ?  88  LEU   A CB   1 
ATOM   1746 C CG   A LEU   A 1 88  ? 23.720 4.465   13.153  0.66 17.97 ?  88  LEU   A CG   1 
ATOM   1747 C CG   B LEU   A 1 88  ? 23.644 4.564   13.299  0.34 17.98 ?  88  LEU   A CG   1 
ATOM   1748 C CD1  A LEU   A 1 88  ? 23.540 4.427   11.644  0.66 18.29 ?  88  LEU   A CD1  1 
ATOM   1749 C CD1  B LEU   A 1 88  ? 23.461 4.683   11.794  0.34 18.02 ?  88  LEU   A CD1  1 
ATOM   1750 C CD2  A LEU   A 1 88  ? 22.484 5.047   13.822  0.66 19.43 ?  88  LEU   A CD2  1 
ATOM   1751 C CD2  B LEU   A 1 88  ? 22.418 5.092   14.032  0.34 18.65 ?  88  LEU   A CD2  1 
ATOM   1752 H H    A LEU   A 1 88  ? 26.056 3.718   15.074  0.66 19.86 ?  88  LEU   A H    1 
ATOM   1753 H H    B LEU   A 1 88  ? 26.044 3.716   15.067  0.34 20.47 ?  88  LEU   A H    1 
ATOM   1754 H HA   A LEU   A 1 88  ? 23.460 3.191   15.645  0.66 19.44 ?  88  LEU   A HA   1 
ATOM   1755 H HA   B LEU   A 1 88  ? 23.464 3.170   15.695  0.34 20.21 ?  88  LEU   A HA   1 
ATOM   1756 H HB2  A LEU   A 1 88  ? 24.796 2.740   13.208  0.66 20.10 ?  88  LEU   A HB2  1 
ATOM   1757 H HB2  B LEU   A 1 88  ? 24.686 2.809   13.179  0.34 20.85 ?  88  LEU   A HB2  1 
ATOM   1758 H HB3  A LEU   A 1 88  ? 23.250 2.508   13.445  0.66 20.10 ?  88  LEU   A HB3  1 
ATOM   1759 H HB3  B LEU   A 1 88  ? 23.146 2.590   13.482  0.34 20.85 ?  88  LEU   A HB3  1 
ATOM   1760 H HG   A LEU   A 1 88  ? 24.472 5.046   13.348  0.66 21.54 ?  88  LEU   A HG   1 
ATOM   1761 H HG   B LEU   A 1 88  ? 24.401 5.115   13.548  0.34 21.56 ?  88  LEU   A HG   1 
ATOM   1762 H HD11 A LEU   A 1 88  ? 23.363 5.326   11.321  0.66 21.92 ?  88  LEU   A HD11 1 
ATOM   1763 H HD11 B LEU   A 1 88  ? 23.293 5.612   11.569  0.34 21.60 ?  88  LEU   A HD11 1 
ATOM   1764 H HD12 A LEU   A 1 88  ? 24.350 4.084   11.236  0.66 21.92 ?  88  LEU   A HD12 1 
ATOM   1765 H HD12 B LEU   A 1 88  ? 24.269 4.377   11.352  0.34 21.60 ?  88  LEU   A HD12 1 
ATOM   1766 H HD13 A LEU   A 1 88  ? 22.791 3.848   11.429  0.66 21.92 ?  88  LEU   A HD13 1 
ATOM   1767 H HD13 B LEU   A 1 88  ? 22.708 4.135   11.522  0.34 21.60 ?  88  LEU   A HD13 1 
ATOM   1768 H HD21 A LEU   A 1 88  ? 22.272 5.898   13.407  0.66 23.30 ?  88  LEU   A HD21 1 
ATOM   1769 H HD21 B LEU   A 1 88  ? 22.184 5.959   13.667  0.34 22.35 ?  88  LEU   A HD21 1 
ATOM   1770 H HD22 A LEU   A 1 88  ? 21.747 4.429   13.709  0.66 23.30 ?  88  LEU   A HD22 1 
ATOM   1771 H HD22 B LEU   A 1 88  ? 21.686 4.469   13.907  0.34 22.35 ?  88  LEU   A HD22 1 
ATOM   1772 H HD23 A LEU   A 1 88  ? 22.670 5.175   14.765  0.66 23.30 ?  88  LEU   A HD23 1 
ATOM   1773 H HD23 B LEU   A 1 88  ? 22.628 5.173   14.975  0.34 22.35 ?  88  LEU   A HD23 1 
ATOM   1774 N N    . ALA   A 1 89  ? 25.741 0.993   15.512  1.00 15.57 ?  89  ALA   A N    1 
ATOM   1775 C CA   . ALA   A 1 89  ? 26.091 -0.415  15.635  1.00 15.31 ?  89  ALA   A CA   1 
ATOM   1776 C C    . ALA   A 1 89  ? 27.578 -0.475  15.949  1.00 15.50 ?  89  ALA   A C    1 
ATOM   1777 O O    . ALA   A 1 89  ? 28.290 0.523   15.830  1.00 16.34 ?  89  ALA   A O    1 
ATOM   1778 C CB   . ALA   A 1 89  ? 25.817 -1.148  14.322  1.00 14.74 ?  89  ALA   A CB   1 
ATOM   1779 H H    A ALA   A 1 89  ? 26.427 1.510   15.453  0.66 18.66 ?  89  ALA   A H    1 
ATOM   1780 H H    B ALA   A 1 89  ? 26.426 1.514   15.482  0.34 18.66 ?  89  ALA   A H    1 
ATOM   1781 H HA   . ALA   A 1 89  ? 25.587 -0.827  16.355  1.00 18.34 ?  89  ALA   A HA   1 
ATOM   1782 H HB1  . ALA   A 1 89  ? 26.077 -2.079  14.422  1.00 17.66 ?  89  ALA   A HB1  1 
ATOM   1783 H HB2  . ALA   A 1 89  ? 24.868 -1.094  14.120  1.00 17.66 ?  89  ALA   A HB2  1 
ATOM   1784 H HB3  . ALA   A 1 89  ? 26.332 -0.736  13.615  1.00 17.66 ?  89  ALA   A HB3  1 
ATOM   1785 N N    . LYS   A 1 90  ? 28.058 -1.653  16.335  1.00 16.15 ?  90  LYS   A N    1 
ATOM   1786 C CA   . LYS   A 1 90  ? 29.503 -1.804  16.474  1.00 16.73 ?  90  LYS   A CA   1 
ATOM   1787 C C    . LYS   A 1 90  ? 30.195 -1.622  15.126  1.00 15.52 ?  90  LYS   A C    1 
ATOM   1788 O O    . LYS   A 1 90  ? 31.133 -0.818  14.993  1.00 16.61 ?  90  LYS   A O    1 
ATOM   1789 C CB   . LYS   A 1 90  ? 29.841 -3.159  17.094  1.00 19.72 ?  90  LYS   A CB   1 
ATOM   1790 C CG   . LYS   A 1 90  ? 31.322 -3.316  17.407  1.00 24.71 ?  90  LYS   A CG   1 
ATOM   1791 C CD   . LYS   A 1 90  ? 31.572 -4.514  18.308  1.00 29.97 ?  90  LYS   A CD   1 
ATOM   1792 C CE   . LYS   A 1 90  ? 32.980 -4.502  18.886  1.00 34.37 ?  90  LYS   A CE   1 
ATOM   1793 N NZ   . LYS   A 1 90  ? 34.017 -4.877  17.887  1.00 36.54 ?  90  LYS   A NZ   1 
ATOM   1794 H H    . LYS   A 1 90  ? 27.586 -2.343  16.522  1.00 19.35 ?  90  LYS   A H    1 
ATOM   1795 H HA   . LYS   A 1 90  ? 29.833 -1.114  17.068  1.00 20.06 ?  90  LYS   A HA   1 
ATOM   1796 H HB2  . LYS   A 1 90  ? 29.345 -3.257  17.925  1.00 23.64 ?  90  LYS   A HB2  1 
ATOM   1797 H HB3  . LYS   A 1 90  ? 29.587 -3.862  16.476  1.00 23.64 ?  90  LYS   A HB3  1 
ATOM   1798 H HG2  . LYS   A 1 90  ? 31.811 -3.447  16.581  1.00 29.63 ?  90  LYS   A HG2  1 
ATOM   1799 H HG3  . LYS   A 1 90  ? 31.638 -2.520  17.863  1.00 29.63 ?  90  LYS   A HG3  1 
ATOM   1800 H HD2  . LYS   A 1 90  ? 30.941 -4.497  19.046  1.00 35.94 ?  90  LYS   A HD2  1 
ATOM   1801 H HD3  . LYS   A 1 90  ? 31.462 -5.329  17.793  1.00 35.94 ?  90  LYS   A HD3  1 
ATOM   1802 H HE2  . LYS   A 1 90  ? 33.183 -3.608  19.207  1.00 41.22 ?  90  LYS   A HE2  1 
ATOM   1803 H HE3  . LYS   A 1 90  ? 33.027 -5.135  19.619  1.00 41.22 ?  90  LYS   A HE3  1 
ATOM   1804 H HZ1  . LYS   A 1 90  ? 33.860 -5.697  17.579  1.00 43.82 ?  90  LYS   A HZ1  1 
ATOM   1805 H HZ2  . LYS   A 1 90  ? 34.005 -4.305  17.206  1.00 43.82 ?  90  LYS   A HZ2  1 
ATOM   1806 H HZ3  . LYS   A 1 90  ? 34.824 -4.860  18.264  1.00 43.82 ?  90  LYS   A HZ3  1 
ATOM   1807 N N    . HIS   A 1 91  ? 29.726 -2.346  14.109  1.00 13.70 ?  91  HIS   A N    1 
ATOM   1808 C CA   . HIS   A 1 91  ? 30.300 -2.329  12.777  1.00 13.08 ?  91  HIS   A CA   1 
ATOM   1809 C C    . HIS   A 1 91  ? 29.213 -2.061  11.754  1.00 12.00 ?  91  HIS   A C    1 
ATOM   1810 O O    . HIS   A 1 91  ? 28.050 -2.430  11.948  1.00 12.83 ?  91  HIS   A O    1 
ATOM   1811 C CB   . HIS   A 1 91  ? 30.909 -3.693  12.415  1.00 15.59 ?  91  HIS   A CB   1 
ATOM   1812 C CG   . HIS   A 1 91  ? 31.902 -4.197  13.411  1.00 19.55 ?  91  HIS   A CG   1 
ATOM   1813 N ND1  . HIS   A 1 91  ? 33.174 -3.679  13.519  1.00 21.62 ?  91  HIS   A ND1  1 
ATOM   1814 C CD2  . HIS   A 1 91  ? 31.817 -5.181  14.337  1.00 21.50 ?  91  HIS   A CD2  1 
ATOM   1815 C CE1  . HIS   A 1 91  ? 33.829 -4.318  14.472  1.00 22.50 ?  91  HIS   A CE1  1 
ATOM   1816 N NE2  . HIS   A 1 91  ? 33.027 -5.235  14.985  1.00 22.76 ?  91  HIS   A NE2  1 
ATOM   1817 H H    . HIS   A 1 91  ? 29.050 -2.889  14.180  1.00 16.41 ?  91  HIS   A H    1 
ATOM   1818 H HA   . HIS   A 1 91  ? 30.982 -1.650  12.712  1.00 15.67 ?  91  HIS   A HA   1 
ATOM   1819 H HB2  . HIS   A 1 91  ? 30.199 -4.352  12.351  1.00 18.69 ?  91  HIS   A HB2  1 
ATOM   1820 H HB3  . HIS   A 1 91  ? 31.360 -3.618  11.558  1.00 18.69 ?  91  HIS   A HB3  1 
ATOM   1821 H HD1  . HIS   A 1 91  ? 33.493 -3.038  13.037  1.00 25.92 ?  91  HIS   A HD1  1 
ATOM   1822 H HD2  . HIS   A 1 91  ? 31.083 -5.719  14.506  1.00 25.77 ?  91  HIS   A HD2  1 
ATOM   1823 H HE1  . HIS   A 1 91  ? 34.707 -4.145  14.736  1.00 26.98 ?  91  HIS   A HE1  1 
ATOM   1824 N N    . CYS   A 1 92  ? 29.613 -1.457  10.640  1.00 11.65 ?  92  CYS   A N    1 
ATOM   1825 C CA   . CYS   A 1 92  ? 28.780 -1.389  9.449   1.00 11.59 ?  92  CYS   A CA   1 
ATOM   1826 C C    . CYS   A 1 92  ? 29.426 -2.206  8.338   1.00 10.93 ?  92  CYS   A C    1 
ATOM   1827 O O    . CYS   A 1 92  ? 30.578 -1.947  7.958   1.00 11.80 ?  92  CYS   A O    1 
ATOM   1828 C CB   . CYS   A 1 92  ? 28.559 0.055   8.990   1.00 11.98 ?  92  CYS   A CB   1 
ATOM   1829 S SG   . CYS   A 1 92  ? 27.541 0.158   7.479   1.00 11.32 ?  92  CYS   A SG   1 
ATOM   1830 H H    . CYS   A 1 92  ? 30.378 -1.072  10.550  1.00 13.96 ?  92  CYS   A H    1 
ATOM   1831 H HA   . CYS   A 1 92  ? 27.913 -1.771  9.645   1.00 13.89 ?  92  CYS   A HA   1 
ATOM   1832 H HB2  . CYS   A 1 92  ? 28.097 0.549   9.689   1.00 14.35 ?  92  CYS   A HB2  1 
ATOM   1833 H HB3  . CYS   A 1 92  ? 29.412 0.469   8.800   1.00 14.35 ?  92  CYS   A HB3  1 
ATOM   1834 H HG   . CYS   A 1 92  ? 27.396 1.313   7.187   1.00 13.56 ?  92  CYS   A HG   1 
ATOM   1835 N N    . LEU   A 1 93  ? 28.688 -3.197  7.839   1.00 10.84 ?  93  LEU   A N    1 
ATOM   1836 C CA   . LEU   A 1 93  ? 29.093 -3.957  6.661   1.00 10.76 ?  93  LEU   A CA   1 
ATOM   1837 C C    . LEU   A 1 93  ? 28.494 -3.268  5.438   1.00 10.30 ?  93  LEU   A C    1 
ATOM   1838 O O    . LEU   A 1 93  ? 27.283 -3.328  5.213   1.00 10.47 ?  93  LEU   A O    1 
ATOM   1839 C CB   . LEU   A 1 93  ? 28.622 -5.406  6.775   1.00 11.23 ?  93  LEU   A CB   1 
ATOM   1840 C CG   . LEU   A 1 93  ? 29.005 -6.303  5.602   1.00 11.13 ?  93  LEU   A CG   1 
ATOM   1841 C CD1  . LEU   A 1 93  ? 30.515 -6.555  5.575   1.00 12.47 ?  93  LEU   A CD1  1 
ATOM   1842 C CD2  . LEU   A 1 93  ? 28.247 -7.625  5.654   1.00 12.42 ?  93  LEU   A CD2  1 
ATOM   1843 H H    . LEU   A 1 93  ? 27.933 -3.442  8.176   1.00 12.98 ?  93  LEU   A H    1 
ATOM   1844 H HA   . LEU   A 1 93  ? 30.056 -3.941  6.590   1.00 12.88 ?  93  LEU   A HA   1 
ATOM   1845 H HB2  . LEU   A 1 93  ? 29.009 -5.787  7.583   1.00 13.45 ?  93  LEU   A HB2  1 
ATOM   1846 H HB3  . LEU   A 1 93  ? 27.656 -5.410  6.848   1.00 13.45 ?  93  LEU   A HB3  1 
ATOM   1847 H HG   . LEU   A 1 93  ? 28.773 -5.862  4.779   1.00 13.34 ?  93  LEU   A HG   1 
ATOM   1848 H HD11 . LEU   A 1 93  ? 30.726 -7.165  4.853   1.00 14.94 ?  93  LEU   A HD11 1 
ATOM   1849 H HD12 . LEU   A 1 93  ? 30.979 -5.712  5.444   1.00 14.94 ?  93  LEU   A HD12 1 
ATOM   1850 H HD13 . LEU   A 1 93  ? 30.791 -6.947  6.426   1.00 14.94 ?  93  LEU   A HD13 1 
ATOM   1851 H HD21 . LEU   A 1 93  ? 28.517 -8.174  4.900   1.00 14.88 ?  93  LEU   A HD21 1 
ATOM   1852 H HD22 . LEU   A 1 93  ? 28.455 -8.082  6.485   1.00 14.88 ?  93  LEU   A HD22 1 
ATOM   1853 H HD23 . LEU   A 1 93  ? 27.296 -7.444  5.606   1.00 14.88 ?  93  LEU   A HD23 1 
ATOM   1854 N N    . HIS   A 1 94  ? 29.339 -2.572  4.677   1.00 10.19 ?  94  HIS   A N    1 
ATOM   1855 C CA   . HIS   A 1 94  ? 28.912 -1.902  3.453   1.00 10.20 ?  94  HIS   A CA   1 
ATOM   1856 C C    . HIS   A 1 94  ? 28.925 -2.936  2.339   1.00 9.88  ?  94  HIS   A C    1 
ATOM   1857 O O    . HIS   A 1 94  ? 29.994 -3.450  1.999   1.00 11.50 ?  94  HIS   A O    1 
ATOM   1858 C CB   . HIS   A 1 94  ? 29.862 -0.748  3.118   1.00 10.37 ?  94  HIS   A CB   1 
ATOM   1859 C CG   . HIS   A 1 94  ? 29.849 0.345   4.130   1.00 10.06 ?  94  HIS   A CG   1 
ATOM   1860 N ND1  . HIS   A 1 94  ? 28.969 1.408   4.072   1.00 10.48 ?  94  HIS   A ND1  1 
ATOM   1861 C CD2  . HIS   A 1 94  ? 30.591 0.520   5.246   1.00 10.93 ?  94  HIS   A CD2  1 
ATOM   1862 C CE1  . HIS   A 1 94  ? 29.181 2.188   5.117   1.00 10.68 ?  94  HIS   A CE1  1 
ATOM   1863 N NE2  . HIS   A 1 94  ? 30.163 1.676   5.839   1.00 10.76 ?  94  HIS   A NE2  1 
ATOM   1864 H H    . HIS   A 1 94  ? 30.178 -2.475  4.850   1.00 12.20 ?  94  HIS   A H    1 
ATOM   1865 H HA   . HIS   A 1 94  ? 28.006 -1.562  3.559   1.00 12.21 ?  94  HIS   A HA   1 
ATOM   1866 H HB2  . HIS   A 1 94  ? 30.759 -1.094  3.064   1.00 12.42 ?  94  HIS   A HB2  1 
ATOM   1867 H HB3  . HIS   A 1 94  ? 29.594 -0.368  2.268   1.00 12.42 ?  94  HIS   A HB3  1 
ATOM   1868 H HD2  . HIS   A 1 94  ? 31.266 -0.031  5.554   1.00 13.10 ?  94  HIS   A HD2  1 
ATOM   1869 H HE1  . HIS   A 1 94  ? 28.712 2.975   5.300   1.00 12.79 ?  94  HIS   A HE1  1 
ATOM   1870 H HE2  . HIS   A 1 94  ? 30.472 2.026   6.560   1.00 12.89 ?  94  HIS   A HE2  1 
ATOM   1871 N N    . VAL   A 1 95  ? 27.757 -3.254  1.782   1.00 9.55  ?  95  VAL   A N    1 
ATOM   1872 C CA   . VAL   A 1 95  ? 27.624 -4.294  0.765   1.00 9.99  ?  95  VAL   A CA   1 
ATOM   1873 C C    . VAL   A 1 95  ? 27.077 -3.662  -0.503  1.00 9.77  ?  95  VAL   A C    1 
ATOM   1874 O O    . VAL   A 1 95  ? 26.072 -2.941  -0.451  1.00 10.69 ?  95  VAL   A O    1 
ATOM   1875 C CB   . VAL   A 1 95  ? 26.696 -5.436  1.220   1.00 10.54 ?  95  VAL   A CB   1 
ATOM   1876 C CG1  . VAL   A 1 95  ? 26.586 -6.480  0.119   1.00 11.38 ?  95  VAL   A CG1  1 
ATOM   1877 C CG2  . VAL   A 1 95  ? 27.198 -6.056  2.508   1.00 10.84 ?  95  VAL   A CG2  1 
ATOM   1878 H H    . VAL   A 1 95  ? 27.007 -2.878  1.983   1.00 11.44 ?  95  VAL   A H    1 
ATOM   1879 H HA   . VAL   A 1 95  ? 28.493 -4.671  0.567   1.00 11.97 ?  95  VAL   A HA   1 
ATOM   1880 H HB   . VAL   A 1 95  ? 25.809 -5.083  1.385   1.00 12.63 ?  95  VAL   A HB   1 
ATOM   1881 H HG11 . VAL   A 1 95  ? 26.205 -7.295  0.488   1.00 13.63 ?  95  VAL   A HG11 1 
ATOM   1882 H HG12 . VAL   A 1 95  ? 26.013 -6.144  -0.589  1.00 13.63 ?  95  VAL   A HG12 1 
ATOM   1883 H HG13 . VAL   A 1 95  ? 27.472 -6.667  -0.234  1.00 13.63 ?  95  VAL   A HG13 1 
ATOM   1884 H HG21 . VAL   A 1 95  ? 26.634 -6.814  2.734   1.00 12.99 ?  95  VAL   A HG21 1 
ATOM   1885 H HG22 . VAL   A 1 95  ? 28.113 -6.354  2.378   1.00 12.99 ?  95  VAL   A HG22 1 
ATOM   1886 H HG23 . VAL   A 1 95  ? 27.161 -5.393  3.211   1.00 12.99 ?  95  VAL   A HG23 1 
ATOM   1887 N N    . VAL   A 1 96  ? 27.701 -3.960  -1.641  1.00 9.92  ?  96  VAL   A N    1 
ATOM   1888 C CA   . VAL   A 1 96  ? 27.287 -3.412  -2.927  1.00 10.63 ?  96  VAL   A CA   1 
ATOM   1889 C C    . VAL   A 1 96  ? 26.495 -4.465  -3.698  1.00 11.23 ?  96  VAL   A C    1 
ATOM   1890 O O    . VAL   A 1 96  ? 27.064 -5.416  -4.241  1.00 11.99 ?  96  VAL   A O    1 
ATOM   1891 C CB   . VAL   A 1 96  ? 28.484 -2.928  -3.750  1.00 11.05 ?  96  VAL   A CB   1 
ATOM   1892 C CG1  . VAL   A 1 96  ? 27.989 -2.302  -5.034  1.00 11.09 ?  96  VAL   A CG1  1 
ATOM   1893 C CG2  . VAL   A 1 96  ? 29.332 -1.941  -2.955  1.00 11.63 ?  96  VAL   A CG2  1 
ATOM   1894 H H    . VAL   A 1 96  ? 28.390 -4.480  -1.694  1.00 11.88 ?  96  VAL   A H    1 
ATOM   1895 H HA   . VAL   A 1 96  ? 26.705 -2.653  -2.775  1.00 12.74 ?  96  VAL   A HA   1 
ATOM   1896 H HB   . VAL   A 1 96  ? 29.040 -3.681  -3.982  1.00 13.24 ?  96  VAL   A HB   1 
ATOM   1897 H HG11 . VAL   A 1 96  ? 28.723 -1.814  -5.447  1.00 13.28 ?  96  VAL   A HG11 1 
ATOM   1898 H HG12 . VAL   A 1 96  ? 27.682 -2.998  -5.632  1.00 13.28 ?  96  VAL   A HG12 1 
ATOM   1899 H HG13 . VAL   A 1 96  ? 27.265 -1.689  -4.832  1.00 13.28 ?  96  VAL   A HG13 1 
ATOM   1900 H HG21 . VAL   A 1 96  ? 30.035 -1.593  -3.522  1.00 13.93 ?  96  VAL   A HG21 1 
ATOM   1901 H HG22 . VAL   A 1 96  ? 28.765 -1.209  -2.648  1.00 13.93 ?  96  VAL   A HG22 1 
ATOM   1902 H HG23 . VAL   A 1 96  ? 29.716 -2.397  -2.190  1.00 13.93 ?  96  VAL   A HG23 1 
ATOM   1903 N N    A GLY   A 1 97  ? 25.175 -4.319  -3.705  0.66 11.21 ?  97  GLY   A N    1 
ATOM   1904 N N    B GLY   A 1 97  ? 25.182 -4.282  -3.804  0.34 10.96 ?  97  GLY   A N    1 
ATOM   1905 C CA   A GLY   A 1 97  ? 24.342 -5.069  -4.604  0.66 12.00 ?  97  GLY   A CA   1 
ATOM   1906 C CA   B GLY   A 1 97  ? 24.393 -5.077  -4.717  0.34 11.37 ?  97  GLY   A CA   1 
ATOM   1907 C C    A GLY   A 1 97  ? 24.319 -4.388  -5.955  0.66 12.05 ?  97  GLY   A C    1 
ATOM   1908 C C    B GLY   A 1 97  ? 24.500 -4.540  -6.133  0.34 11.67 ?  97  GLY   A C    1 
ATOM   1909 O O    A GLY   A 1 97  ? 24.582 -3.186  -6.068  0.66 12.32 ?  97  GLY   A O    1 
ATOM   1910 O O    B GLY   A 1 97  ? 24.895 -3.389  -6.351  0.34 11.99 ?  97  GLY   A O    1 
ATOM   1911 H H    A GLY   A 1 97  ? 24.742 -3.782  -3.188  0.66 13.43 ?  97  GLY   A H    1 
ATOM   1912 H H    B GLY   A 1 97  ? 24.727 -3.706  -3.353  0.34 13.12 ?  97  GLY   A H    1 
ATOM   1913 H HA2  A GLY   A 1 97  ? 24.694 -5.964  -4.703  0.66 14.37 ?  97  GLY   A HA2  1 
ATOM   1914 H HA2  B GLY   A 1 97  ? 24.709 -5.995  -4.698  0.34 13.62 ?  97  GLY   A HA2  1 
ATOM   1915 H HA3  A GLY   A 1 97  ? 23.437 -5.119  -4.256  0.66 14.37 ?  97  GLY   A HA3  1 
ATOM   1916 H HA3  B GLY   A 1 97  ? 23.462 -5.065  -4.445  0.34 13.62 ?  97  GLY   A HA3  1 
ATOM   1917 N N    A PRO   A 1 98  ? 24.007 -5.137  -7.010  0.66 12.09 ?  98  PRO   A N    1 
ATOM   1918 N N    B PRO   A 1 98  ? 24.161 -5.361  -7.128  0.34 12.17 ?  98  PRO   A N    1 
ATOM   1919 C CA   A PRO   A 1 98  ? 23.904 -4.522  -8.337  0.66 12.70 ?  98  PRO   A CA   1 
ATOM   1920 C CA   B PRO   A 1 98  ? 24.170 -4.873  -8.514  0.34 12.90 ?  98  PRO   A CA   1 
ATOM   1921 C C    A PRO   A 1 98  ? 22.795 -3.482  -8.378  0.66 12.69 ?  98  PRO   A C    1 
ATOM   1922 C C    B PRO   A 1 98  ? 23.079 -3.838  -8.759  0.34 13.39 ?  98  PRO   A C    1 
ATOM   1923 O O    A PRO   A 1 98  ? 21.727 -3.659  -7.789  0.66 12.31 ?  98  PRO   A O    1 
ATOM   1924 O O    B PRO   A 1 98  ? 21.957 -3.953  -8.259  0.34 13.66 ?  98  PRO   A O    1 
ATOM   1925 C CB   A PRO   A 1 98  ? 23.589 -5.710  -9.252  0.66 12.89 ?  98  PRO   A CB   1 
ATOM   1926 C CB   B PRO   A 1 98  ? 23.927 -6.143  -9.342  0.34 12.62 ?  98  PRO   A CB   1 
ATOM   1927 C CG   A PRO   A 1 98  ? 22.944 -6.718  -8.353  0.66 12.75 ?  98  PRO   A CG   1 
ATOM   1928 C CG   B PRO   A 1 98  ? 23.284 -7.105  -8.395  0.34 12.85 ?  98  PRO   A CG   1 
ATOM   1929 C CD   A PRO   A 1 98  ? 23.657 -6.568  -7.033  0.66 12.09 ?  98  PRO   A CD   1 
ATOM   1930 C CD   B PRO   A 1 98  ? 23.893 -6.808  -7.055  0.34 12.21 ?  98  PRO   A CD   1 
ATOM   1931 H HA   A PRO   A 1 98  ? 24.746 -4.119  -8.591  0.66 15.21 ?  98  PRO   A HA   1 
ATOM   1932 H HA   B PRO   A 1 98  ? 25.038 -4.499  -8.740  0.34 15.46 ?  98  PRO   A HA   1 
ATOM   1933 H HB2  A PRO   A 1 98  ? 22.976 -5.434  -9.949  0.66 15.44 ?  98  PRO   A HB2  1 
ATOM   1934 H HB2  B PRO   A 1 98  ? 23.334 -5.939  -10.082 0.34 15.12 ?  98  PRO   A HB2  1 
ATOM   1935 H HB3  A PRO   A 1 98  ? 24.410 -6.060  -9.628  0.66 15.44 ?  98  PRO   A HB3  1 
ATOM   1936 H HB3  B PRO   A 1 98  ? 24.773 -6.492  -9.667  0.34 15.12 ?  98  PRO   A HB3  1 
ATOM   1937 H HG2  A PRO   A 1 98  ? 22.001 -6.520  -8.255  0.66 15.28 ?  98  PRO   A HG2  1 
ATOM   1938 H HG2  B PRO   A 1 98  ? 22.326 -6.954  -8.376  0.34 15.40 ?  98  PRO   A HG2  1 
ATOM   1939 H HG3  A PRO   A 1 98  ? 23.076 -7.610  -8.709  0.66 15.28 ?  98  PRO   A HG3  1 
ATOM   1940 H HG3  B PRO   A 1 98  ? 23.481 -8.015  -8.669  0.34 15.40 ?  98  PRO   A HG3  1 
ATOM   1941 H HD2  A PRO   A 1 98  ? 23.062 -6.791  -6.296  0.66 14.49 ?  98  PRO   A HD2  1 
ATOM   1942 H HD2  B PRO   A 1 98  ? 23.262 -7.003  -6.344  0.34 14.63 ?  98  PRO   A HD2  1 
ATOM   1943 H HD3  A PRO   A 1 98  ? 24.463 -7.108  -7.012  0.66 14.49 ?  98  PRO   A HD3  1 
ATOM   1944 H HD3  B PRO   A 1 98  ? 24.720 -7.309  -6.940  0.34 14.63 ?  98  PRO   A HD3  1 
ATOM   1945 N N    A ASN   A 1 99  ? 23.068 -2.384  -9.078  0.66 13.67 ?  99  ASN   A N    1 
ATOM   1946 N N    B ASN   A 1 99  ? 23.422 -2.818  -9.544  0.34 14.11 ?  99  ASN   A N    1 
ATOM   1947 C CA   A ASN   A 1 99  ? 22.089 -1.329  -9.316  0.66 14.70 ?  99  ASN   A CA   1 
ATOM   1948 C CA   B ASN   A 1 99  ? 22.482 -1.776  -9.956  0.34 15.06 ?  99  ASN   A CA   1 
ATOM   1949 C C    A ASN   A 1 99  ? 21.526 -1.520  -10.720 0.66 16.19 ?  99  ASN   A C    1 
ATOM   1950 C C    B ASN   A 1 99  ? 22.002 -2.128  -11.359 0.34 15.84 ?  99  ASN   A C    1 
ATOM   1951 O O    A ASN   A 1 99  ? 22.216 -1.266  -11.714 0.66 17.70 ?  99  ASN   A O    1 
ATOM   1952 O O    B ASN   A 1 99  ? 22.703 -1.889  -12.345 0.34 14.76 ?  99  ASN   A O    1 
ATOM   1953 C CB   A ASN   A 1 99  ? 22.732 0.048   -9.161  0.66 15.55 ?  99  ASN   A CB   1 
ATOM   1954 C CB   B ASN   A 1 99  ? 23.155 -0.407  -9.933  0.34 15.55 ?  99  ASN   A CB   1 
ATOM   1955 C CG   A ASN   A 1 99  ? 21.706 1.187   -9.136  0.66 16.66 ?  99  ASN   A CG   1 
ATOM   1956 C CG   B ASN   A 1 99  ? 22.185 0.731   -10.219 0.34 16.02 ?  99  ASN   A CG   1 
ATOM   1957 O OD1  A ASN   A 1 99  ? 20.698 1.151   -9.843  0.66 17.36 ?  99  ASN   A OD1  1 
ATOM   1958 O OD1  B ASN   A 1 99  ? 21.117 0.527   -10.792 0.34 16.25 ?  99  ASN   A OD1  1 
ATOM   1959 N ND2  A ASN   A 1 99  ? 21.973 2.201   -8.321  0.66 17.26 ?  99  ASN   A ND2  1 
ATOM   1960 N ND2  B ASN   A 1 99  ? 22.560 1.938   -9.824  0.34 17.11 ?  99  ASN   A ND2  1 
ATOM   1961 H H    A ASN   A 1 99  ? 23.839 -2.222  -9.420  0.66 16.38 ?  99  ASN   A H    1 
ATOM   1962 H H    B ASN   A 1 99  ? 24.218 -2.708  -9.851  0.34 16.91 ?  99  ASN   A H    1 
ATOM   1963 H HA   A ASN   A 1 99  ? 21.363 -1.409  -8.675  0.66 17.62 ?  99  ASN   A HA   1 
ATOM   1964 H HA   B ASN   A 1 99  ? 21.719 -1.771  -9.357  0.34 18.05 ?  99  ASN   A HA   1 
ATOM   1965 H HB2  A ASN   A 1 99  ? 23.234 0.071   -8.334  0.66 18.64 ?  99  ASN   A HB2  1 
ATOM   1966 H HB2  B ASN   A 1 99  ? 23.542 -0.265  -9.058  0.34 18.63 ?  99  ASN   A HB2  1 
ATOM   1967 H HB3  A ASN   A 1 99  ? 23.328 0.198   -9.915  0.66 18.64 ?  99  ASN   A HB3  1 
ATOM   1968 H HB3  B ASN   A 1 99  ? 23.849 -0.395  -10.611 0.34 18.63 ?  99  ASN   A HB3  1 
ATOM   1969 H HD21 A ASN   A 1 99  ? 21.430 2.863   -8.267  0.66 20.69 ?  99  ASN   A HD21 1 
ATOM   1970 H HD21 B ASN   A 1 99  ? 22.045 2.609   -9.965  0.34 20.50 ?  99  ASN   A HD21 1 
ATOM   1971 H HD22 A ASN   A 1 99  ? 22.691 2.192   -7.842  0.66 20.69 ?  99  ASN   A HD22 1 
ATOM   1972 H HD22 B ASN   A 1 99  ? 23.314 2.043   -9.433  0.34 20.50 ?  99  ASN   A HD22 1 
ATOM   1973 N N    A VAL   A 1 100 ? 20.273 -1.981  -10.794 0.66 17.19 ?  100 VAL   A N    1 
ATOM   1974 N N    B VAL   A 1 100 ? 20.803 -2.707  -11.445 0.34 18.50 ?  100 VAL   A N    1 
ATOM   1975 C CA   A VAL   A 1 100 ? 19.631 -2.227  -12.083 0.66 19.66 ?  100 VAL   A CA   1 
ATOM   1976 C CA   B VAL   A 1 100 ? 20.274 -3.138  -12.736 0.34 20.86 ?  100 VAL   A CA   1 
ATOM   1977 C C    A VAL   A 1 100 ? 19.520 -0.939  -12.887 0.66 20.84 ?  100 VAL   A C    1 
ATOM   1978 C C    B VAL   A 1 100 ? 20.052 -1.950  -13.663 0.34 22.16 ?  100 VAL   A C    1 
ATOM   1979 O O    A VAL   A 1 100 ? 19.561 -0.966  -14.123 0.66 21.69 ?  100 VAL   A O    1 
ATOM   1980 O O    B VAL   A 1 100 ? 20.097 -2.094  -14.891 0.34 22.33 ?  100 VAL   A O    1 
ATOM   1981 C CB   A VAL   A 1 100 ? 18.260 -2.912  -11.880 0.66 20.94 ?  100 VAL   A CB   1 
ATOM   1982 C CB   B VAL   A 1 100 ? 18.995 -3.974  -12.530 0.34 21.90 ?  100 VAL   A CB   1 
ATOM   1983 C CG1  A VAL   A 1 100 ? 17.543 -3.103  -13.211 0.66 21.56 ?  100 VAL   A CG1  1 
ATOM   1984 C CG1  B VAL   A 1 100 ? 18.183 -4.058  -13.813 0.34 22.33 ?  100 VAL   A CG1  1 
ATOM   1985 C CG2  A VAL   A 1 100 ? 18.439 -4.251  -11.177 0.66 21.19 ?  100 VAL   A CG2  1 
ATOM   1986 C CG2  B VAL   A 1 100 ? 19.357 -5.367  -12.041 0.34 22.49 ?  100 VAL   A CG2  1 
ATOM   1987 H H    A VAL   A 1 100 ? 19.774 -2.161  -10.111 0.66 20.61 ?  100 VAL   A H    1 
ATOM   1988 H H    B VAL   A 1 100 ? 20.288 -2.869  -10.776 0.34 22.18 ?  100 VAL   A H    1 
ATOM   1989 H HA   A VAL   A 1 100 ? 20.182 -2.841  -12.589 0.66 23.57 ?  100 VAL   A HA   1 
ATOM   1990 H HA   B VAL   A 1 100 ? 20.929 -3.719  -13.156 0.34 25.01 ?  100 VAL   A HA   1 
ATOM   1991 H HB   A VAL   A 1 100 ? 17.702 -2.352  -11.318 0.66 25.10 ?  100 VAL   A HB   1 
ATOM   1992 H HB   B VAL   A 1 100 ? 18.445 -3.551  -11.854 0.34 26.26 ?  100 VAL   A HB   1 
ATOM   1993 H HG11 A VAL   A 1 100 ? 16.784 -3.694  -13.078 0.66 25.84 ?  100 VAL   A HG11 1 
ATOM   1994 H HG11 B VAL   A 1 100 ? 17.515 -4.756  -13.715 0.34 26.78 ?  100 VAL   A HG11 1 
ATOM   1995 H HG12 A VAL   A 1 100 ? 17.236 -2.242  -13.534 0.66 25.84 ?  100 VAL   A HG12 1 
ATOM   1996 H HG12 B VAL   A 1 100 ? 17.743 -3.207  -13.969 0.34 26.78 ?  100 VAL   A HG12 1 
ATOM   1997 H HG13 A VAL   A 1 100 ? 18.159 -3.498  -13.848 0.66 25.84 ?  100 VAL   A HG13 1 
ATOM   1998 H HG13 B VAL   A 1 100 ? 18.774 -4.269  -14.551 0.34 26.78 ?  100 VAL   A HG13 1 
ATOM   1999 H HG21 A VAL   A 1 100 ? 17.576 -4.691  -11.109 0.66 25.41 ?  100 VAL   A HG21 1 
ATOM   2000 H HG21 B VAL   A 1 100 ? 18.542 -5.874  -11.903 0.34 26.97 ?  100 VAL   A HG21 1 
ATOM   2001 H HG22 A VAL   A 1 100 ? 19.049 -4.800  -11.694 0.66 25.41 ?  100 VAL   A HG22 1 
ATOM   2002 H HG22 B VAL   A 1 100 ? 19.909 -5.803  -12.710 0.34 26.97 ?  100 VAL   A HG22 1 
ATOM   2003 H HG23 A VAL   A 1 100 ? 18.801 -4.098  -10.291 0.66 25.41 ?  100 VAL   A HG23 1 
ATOM   2004 H HG23 B VAL   A 1 100 ? 19.846 -5.291  -11.208 0.34 26.97 ?  100 VAL   A HG23 1 
ATOM   2005 N N    A ASN   A 1 101 ? 19.369 0.201   -12.212 0.66 22.13 ?  101 ASN   A N    1 
ATOM   2006 N N    B ASN   A 1 101 ? 19.805 -0.766  -13.104 0.34 23.07 ?  101 ASN   A N    1 
ATOM   2007 C CA   A ASN   A 1 101 ? 19.311 1.486   -12.901 0.66 24.04 ?  101 ASN   A CA   1 
ATOM   2008 C CA   B ASN   A 1 101 ? 19.695 0.427   -13.934 0.34 24.06 ?  101 ASN   A CA   1 
ATOM   2009 C C    A ASN   A 1 101 ? 20.666 1.927   -13.450 0.66 25.90 ?  101 ASN   A C    1 
ATOM   2010 C C    B ASN   A 1 101 ? 21.047 0.920   -14.437 0.34 24.19 ?  101 ASN   A C    1 
ATOM   2011 O O    A ASN   A 1 101 ? 20.738 2.982   -14.094 0.66 27.42 ?  101 ASN   A O    1 
ATOM   2012 O O    B ASN   A 1 101 ? 21.079 1.797   -15.307 0.34 24.13 ?  101 ASN   A O    1 
ATOM   2013 C CB   A ASN   A 1 101 ? 18.720 2.547   -11.971 0.66 23.71 ?  101 ASN   A CB   1 
ATOM   2014 C CB   B ASN   A 1 101 ? 18.946 1.527   -13.180 0.34 24.91 ?  101 ASN   A CB   1 
ATOM   2015 C CG   A ASN   A 1 101 ? 17.355 2.150   -11.432 0.66 23.41 ?  101 ASN   A CG   1 
ATOM   2016 C CG   B ASN   A 1 101 ? 17.559 1.089   -12.745 0.34 25.49 ?  101 ASN   A CG   1 
ATOM   2017 O OD1  A ASN   A 1 101 ? 16.501 1.646   -12.169 0.66 23.73 ?  101 ASN   A OD1  1 
ATOM   2018 O OD1  B ASN   A 1 101 ? 16.955 0.205   -13.352 0.34 25.87 ?  101 ASN   A OD1  1 
ATOM   2019 N ND2  A ASN   A 1 101 ? 17.146 2.366   -10.138 0.66 23.51 ?  101 ASN   A ND2  1 
ATOM   2020 N ND2  B ASN   A 1 101 ? 17.047 1.706   -11.691 0.34 25.74 ?  101 ASN   A ND2  1 
ATOM   2021 H H    A ASN   A 1 101 ? 19.290 0.252   -11.357 0.66 26.53 ?  101 ASN   A H    1 
ATOM   2022 H H    B ASN   A 1 101 ? 19.681 -0.638  -12.264 0.34 27.67 ?  101 ASN   A H    1 
ATOM   2023 H HA   A ASN   A 1 101 ? 18.712 1.399   -13.654 0.66 28.83 ?  101 ASN   A HA   1 
ATOM   2024 H HA   B ASN   A 1 101 ? 19.169 0.204   -14.713 0.34 28.85 ?  101 ASN   A HA   1 
ATOM   2025 H HB2  A ASN   A 1 101 ? 19.316 2.681   -11.218 0.66 28.43 ?  101 ASN   A HB2  1 
ATOM   2026 H HB2  B ASN   A 1 101 ? 19.447 1.768   -12.386 0.34 29.87 ?  101 ASN   A HB2  1 
ATOM   2027 H HB3  A ASN   A 1 101 ? 18.618 3.377   -12.465 0.66 28.43 ?  101 ASN   A HB3  1 
ATOM   2028 H HB3  B ASN   A 1 101 ? 18.848 2.297   -13.760 0.34 29.87 ?  101 ASN   A HB3  1 
ATOM   2029 H HD21 A ASN   A 1 101 ? 16.390 2.158   -9.785  0.66 28.19 ?  101 ASN   A HD21 1 
ATOM   2030 H HD21 B ASN   A 1 101 ? 16.265 1.490   -11.407 0.34 30.86 ?  101 ASN   A HD21 1 
ATOM   2031 H HD22 A ASN   A 1 101 ? 17.764 2.720   -9.655  0.66 28.19 ?  101 ASN   A HD22 1 
ATOM   2032 H HD22 B ASN   A 1 101 ? 17.496 2.321   -11.296 0.34 30.86 ?  101 ASN   A HD22 1 
ATOM   2033 N N    A LYS   A 1 102 ? 21.727 1.151   -13.215 0.66 27.63 ?  102 LYS   A N    1 
ATOM   2034 N N    B LYS   A 1 102 ? 22.151 0.381   -13.918 0.34 24.68 ?  102 LYS   A N    1 
ATOM   2035 C CA   A LYS   A 1 102 ? 23.017 1.351   -13.862 0.66 29.06 ?  102 LYS   A CA   1 
ATOM   2036 C CA   B LYS   A 1 102 ? 23.481 0.602   -14.474 0.34 24.85 ?  102 LYS   A CA   1 
ATOM   2037 C C    A LYS   A 1 102 ? 23.347 0.242   -14.852 0.66 28.87 ?  102 LYS   A C    1 
ATOM   2038 C C    B LYS   A 1 102 ? 23.897 -0.511  -15.433 0.34 24.02 ?  102 LYS   A C    1 
ATOM   2039 O O    A LYS   A 1 102 ? 24.439 0.251   -15.429 0.66 29.42 ?  102 LYS   A O    1 
ATOM   2040 O O    B LYS   A 1 102 ? 25.059 -0.557  -15.848 0.34 24.13 ?  102 LYS   A O    1 
ATOM   2041 C CB   A LYS   A 1 102 ? 24.135 1.435   -12.815 0.66 30.85 ?  102 LYS   A CB   1 
ATOM   2042 C CB   B LYS   A 1 102 ? 24.523 0.706   -13.356 0.34 26.15 ?  102 LYS   A CB   1 
ATOM   2043 C CG   A LYS   A 1 102 ? 23.983 2.558   -11.805 0.66 32.25 ?  102 LYS   A CG   1 
ATOM   2044 C CG   B LYS   A 1 102 ? 24.491 1.987   -12.537 0.34 27.57 ?  102 LYS   A CG   1 
ATOM   2045 C CD   A LYS   A 1 102 ? 25.145 2.555   -10.820 0.66 33.53 ?  102 LYS   A CD   1 
ATOM   2046 C CD   B LYS   A 1 102 ? 25.581 1.954   -11.469 0.34 29.02 ?  102 LYS   A CD   1 
ATOM   2047 C CE   A LYS   A 1 102 ? 25.028 3.676   -9.800  0.66 34.50 ?  102 LYS   A CE   1 
ATOM   2048 C CE   B LYS   A 1 102 ? 25.463 3.110   -10.491 0.34 30.20 ?  102 LYS   A CE   1 
ATOM   2049 N NZ   A LYS   A 1 102 ? 26.144 3.637   -8.808  0.66 34.97 ?  102 LYS   A NZ   1 
ATOM   2050 N NZ   B LYS   A 1 102 ? 25.612 2.644   -9.082  0.34 30.95 ?  102 LYS   A NZ   1 
ATOM   2051 H H    A LYS   A 1 102 ? 21.721 0.482   -12.673 0.66 33.13 ?  102 LYS   A H    1 
ATOM   2052 H H    B LYS   A 1 102 ? 22.152 -0.129  -13.225 0.34 29.59 ?  102 LYS   A H    1 
ATOM   2053 H HA   A LYS   A 1 102 ? 23.000 2.191   -14.344 0.66 34.85 ?  102 LYS   A HA   1 
ATOM   2054 H HA   B LYS   A 1 102 ? 23.481 1.446   -14.956 0.34 29.79 ?  102 LYS   A HA   1 
ATOM   2055 H HB2  A LYS   A 1 102 ? 24.163 0.601   -12.322 0.66 36.99 ?  102 LYS   A HB2  1 
ATOM   2056 H HB2  B LYS   A 1 102 ? 24.391 -0.034  -12.744 0.34 31.36 ?  102 LYS   A HB2  1 
ATOM   2057 H HB3  A LYS   A 1 102 ? 24.979 1.569   -13.275 0.66 36.99 ?  102 LYS   A HB3  1 
ATOM   2058 H HB3  B LYS   A 1 102 ? 25.406 0.642   -13.753 0.34 31.36 ?  102 LYS   A HB3  1 
ATOM   2059 H HG2  A LYS   A 1 102 ? 23.976 3.410   -12.269 0.66 38.67 ?  102 LYS   A HG2  1 
ATOM   2060 H HG2  B LYS   A 1 102 ? 24.655 2.747   -13.116 0.34 33.06 ?  102 LYS   A HG2  1 
ATOM   2061 H HG3  A LYS   A 1 102 ? 23.159 2.436   -11.309 0.66 38.67 ?  102 LYS   A HG3  1 
ATOM   2062 H HG3  B LYS   A 1 102 ? 23.631 2.074   -12.100 0.34 33.06 ?  102 LYS   A HG3  1 
ATOM   2063 H HD2  A LYS   A 1 102 ? 25.155 1.710   -10.343 0.66 40.21 ?  102 LYS   A HD2  1 
ATOM   2064 H HD2  B LYS   A 1 102 ? 25.513 1.127   -10.968 0.34 34.79 ?  102 LYS   A HD2  1 
ATOM   2065 H HD3  A LYS   A 1 102 ? 25.976 2.673   -11.308 0.66 40.21 ?  102 LYS   A HD3  1 
ATOM   2066 H HD3  B LYS   A 1 102 ? 26.450 2.011   -11.900 0.34 34.79 ?  102 LYS   A HD3  1 
ATOM   2067 H HE2  A LYS   A 1 102 ? 25.059 4.530   -10.259 0.66 41.37 ?  102 LYS   A HE2  1 
ATOM   2068 H HE2  B LYS   A 1 102 ? 26.166 3.756   -10.673 0.34 36.21 ?  102 LYS   A HE2  1 
ATOM   2069 H HE3  A LYS   A 1 102 ? 24.191 3.584   -9.319  0.66 41.37 ?  102 LYS   A HE3  1 
ATOM   2070 H HE3  B LYS   A 1 102 ? 24.593 3.525   -10.587 0.34 36.21 ?  102 LYS   A HE3  1 
ATOM   2071 H HZ1  A LYS   A 1 102 ? 26.054 4.301   -8.223  0.66 41.95 ?  102 LYS   A HZ1  1 
ATOM   2072 H HZ1  B LYS   A 1 102 ? 25.333 3.275   -8.521  0.34 37.12 ?  102 LYS   A HZ1  1 
ATOM   2073 H HZ2  A LYS   A 1 102 ? 26.134 2.862   -8.370  0.66 41.95 ?  102 LYS   A HZ2  1 
ATOM   2074 H HZ2  B LYS   A 1 102 ? 25.128 1.907   -8.953  0.34 37.12 ?  102 LYS   A HZ2  1 
ATOM   2075 H HZ3  A LYS   A 1 102 ? 26.925 3.723   -9.226  0.66 41.95 ?  102 LYS   A HZ3  1 
ATOM   2076 H HZ3  B LYS   A 1 102 ? 26.465 2.459   -8.911  0.34 37.12 ?  102 LYS   A HZ3  1 
ATOM   2077 N N    A GLY   A 1 103 ? 22.444 -0.718  -15.050 0.66 28.84 ?  103 GLY   A N    1 
ATOM   2078 N N    B GLY   A 1 103 ? 22.983 -1.414  -15.779 0.34 23.20 ?  103 GLY   A N    1 
ATOM   2079 C CA   A GLY   A 1 103 ? 22.679 -1.819  -15.963 0.66 28.61 ?  103 GLY   A CA   1 
ATOM   2080 C CA   B GLY   A 1 103 ? 23.326 -2.537  -16.630 0.34 22.69 ?  103 GLY   A CA   1 
ATOM   2081 C C    A GLY   A 1 103 ? 23.495 -2.962  -15.401 0.66 28.49 ?  103 GLY   A C    1 
ATOM   2082 C C    B GLY   A 1 103 ? 24.099 -3.641  -15.946 0.34 22.25 ?  103 GLY   A C    1 
ATOM   2083 O O    A GLY   A 1 103 ? 23.982 -3.796  -16.169 0.66 29.42 ?  103 GLY   A O    1 
ATOM   2084 O O    B GLY   A 1 103 ? 24.756 -4.436  -16.626 0.34 23.02 ?  103 GLY   A O    1 
ATOM   2085 H H    A GLY   A 1 103 ? 21.681 -0.747  -14.663 0.66 34.59 ?  103 GLY   A H    1 
ATOM   2086 H H    B GLY   A 1 103 ? 22.159 -1.386  -15.536 0.34 27.81 ?  103 GLY   A H    1 
ATOM   2087 H HA2  A GLY   A 1 103 ? 21.820 -2.173  -16.253 0.66 34.31 ?  103 GLY   A HA2  1 
ATOM   2088 H HA2  B GLY   A 1 103 ? 22.511 -2.913  -17.002 0.34 27.20 ?  103 GLY   A HA2  1 
ATOM   2089 H HA3  A GLY   A 1 103 ? 23.139 -1.481  -16.748 0.66 34.31 ?  103 GLY   A HA3  1 
ATOM   2090 H HA3  B GLY   A 1 103 ? 23.870 -2.209  -17.364 0.34 27.20 ?  103 GLY   A HA3  1 
ATOM   2091 N N    A GLU   A 1 104 ? 23.650 -3.040  -14.083 0.66 26.76 ?  104 GLU   A N    1 
ATOM   2092 N N    B GLU   A 1 104 ? 24.033 -3.728  -14.623 0.34 20.56 ?  104 GLU   A N    1 
ATOM   2093 C CA   A GLU   A 1 104 ? 24.529 -4.031  -13.479 0.66 25.36 ?  104 GLU   A CA   1 
ATOM   2094 C CA   B GLU   A 1 104 ? 24.861 -4.658  -13.871 0.34 18.91 ?  104 GLU   A CA   1 
ATOM   2095 C C    A GLU   A 1 104 ? 23.846 -5.393  -13.367 0.66 25.58 ?  104 GLU   A C    1 
ATOM   2096 C C    B GLU   A 1 104 ? 24.143 -5.987  -13.657 0.34 18.45 ?  104 GLU   A C    1 
ATOM   2097 O O    A GLU   A 1 104 ? 22.630 -5.496  -13.177 0.66 25.61 ?  104 GLU   A O    1 
ATOM   2098 O O    B GLU   A 1 104 ? 22.913 -6.054  -13.585 0.34 18.62 ?  104 GLU   A O    1 
ATOM   2099 C CB   A GLU   A 1 104 ? 25.023 -3.533  -12.118 0.66 23.46 ?  104 GLU   A CB   1 
ATOM   2100 C CB   B GLU   A 1 104 ? 25.282 -4.039  -12.537 0.34 18.19 ?  104 GLU   A CB   1 
ATOM   2101 C CG   A GLU   A 1 104 ? 25.900 -2.283  -12.265 0.66 22.71 ?  104 GLU   A CG   1 
ATOM   2102 C CG   B GLU   A 1 104 ? 26.105 -2.764  -12.727 0.34 18.13 ?  104 GLU   A CG   1 
ATOM   2103 C CD   A GLU   A 1 104 ? 26.254 -1.571  -10.968 0.66 21.60 ?  104 GLU   A CD   1 
ATOM   2104 C CD   B GLU   A 1 104 ? 26.534 -2.092  -11.433 0.34 17.82 ?  104 GLU   A CD   1 
ATOM   2105 O OE1  A GLU   A 1 104 ? 25.691 -1.899  -9.906  0.66 20.01 ?  104 GLU   A OE1  1 
ATOM   2106 O OE1  B GLU   A 1 104 ? 26.017 -2.451  -10.357 0.34 18.17 ?  104 GLU   A OE1  1 
ATOM   2107 O OE2  A GLU   A 1 104 ? 27.098 -0.646  -11.033 0.66 22.57 -1 104 GLU   A OE2  1 
ATOM   2108 O OE2  B GLU   A 1 104 ? 27.389 -1.181  -11.502 0.34 17.78 -1 104 GLU   A OE2  1 
ATOM   2109 H H    A GLU   A 1 104 ? 23.261 -2.523  -13.520 0.66 32.08 ?  104 GLU   A H    1 
ATOM   2110 H H    B GLU   A 1 104 ? 23.506 -3.252  -14.142 0.34 24.64 ?  104 GLU   A H    1 
ATOM   2111 H HA   A GLU   A 1 104 ? 25.304 -4.138  -14.052 0.66 30.40 ?  104 GLU   A HA   1 
ATOM   2112 H HA   B GLU   A 1 104 ? 25.664 -4.834  -14.387 0.34 22.67 ?  104 GLU   A HA   1 
ATOM   2113 H HB2  A GLU   A 1 104 ? 24.257 -3.313  -11.566 0.66 28.13 ?  104 GLU   A HB2  1 
ATOM   2114 H HB2  B GLU   A 1 104 ? 24.488 -3.819  -12.030 0.34 21.81 ?  104 GLU   A HB2  1 
ATOM   2115 H HB3  A GLU   A 1 104 ? 25.549 -4.234  -11.702 0.66 28.13 ?  104 GLU   A HB3  1 
ATOM   2116 H HB3  B GLU   A 1 104 ? 25.823 -4.684  -12.057 0.34 21.81 ?  104 GLU   A HB3  1 
ATOM   2117 H HG2  A GLU   A 1 104 ? 26.726 -2.541  -12.697 0.66 27.23 ?  104 GLU   A HG2  1 
ATOM   2118 H HG2  B GLU   A 1 104 ? 26.901 -2.982  -13.236 0.34 21.74 ?  104 GLU   A HG2  1 
ATOM   2119 H HG3  A GLU   A 1 104 ? 25.426 -1.641  -12.813 0.66 27.23 ?  104 GLU   A HG3  1 
ATOM   2120 H HG3  B GLU   A 1 104 ? 25.569 -2.119  -13.212 0.34 21.74 ?  104 GLU   A HG3  1 
ATOM   2121 N N    A ASP   A 1 105 ? 24.656 -6.443  -13.484 0.66 25.87 ?  105 ASP   A N    1 
ATOM   2122 N N    B ASP   A 1 105 ? 24.942 -7.046  -13.542 0.34 18.50 ?  105 ASP   A N    1 
ATOM   2123 C CA   A ASP   A 1 105 ? 24.158 -7.809  -13.607 0.66 26.63 ?  105 ASP   A CA   1 
ATOM   2124 C CA   B ASP   A 1 105 ? 24.450 -8.418  -13.605 0.34 18.98 ?  105 ASP   A CA   1 
ATOM   2125 C C    A ASP   A 1 105 ? 23.475 -8.247  -12.315 0.66 24.70 ?  105 ASP   A C    1 
ATOM   2126 C C    B ASP   A 1 105 ? 23.671 -8.774  -12.343 0.34 17.57 ?  105 ASP   A C    1 
ATOM   2127 O O    A ASP   A 1 105 ? 24.104 -8.285  -11.254 0.66 23.41 ?  105 ASP   A O    1 
ATOM   2128 O O    B ASP   A 1 105 ? 24.213 -8.729  -11.235 0.34 15.58 ?  105 ASP   A O    1 
ATOM   2129 C CB   A ASP   A 1 105 ? 25.331 -8.733  -13.928 0.66 29.28 ?  105 ASP   A CB   1 
ATOM   2130 C CB   B ASP   A 1 105 ? 25.649 -9.348  -13.770 0.34 20.88 ?  105 ASP   A CB   1 
ATOM   2131 C CG   A ASP   A 1 105 ? 24.900 -10.159 -14.183 0.66 31.61 ?  105 ASP   A CG   1 
ATOM   2132 C CG   B ASP   A 1 105 ? 25.254 -10.800 -13.900 0.34 22.48 ?  105 ASP   A CG   1 
ATOM   2133 O OD1  A ASP   A 1 105 ? 23.679 -10.407 -14.254 0.66 32.04 ?  105 ASP   A OD1  1 
ATOM   2134 O OD1  B ASP   A 1 105 ? 24.044 -11.094 -13.980 0.34 22.48 ?  105 ASP   A OD1  1 
ATOM   2135 O OD2  A ASP   A 1 105 ? 25.788 -11.030 -14.316 0.66 33.14 -1 105 ASP   A OD2  1 
ATOM   2136 O OD2  B ASP   A 1 105 ? 26.170 -11.651 -13.915 0.34 23.40 -1 105 ASP   A OD2  1 
ATOM   2137 H H    A ASP   A 1 105 ? 25.514 -6.388  -13.491 0.66 31.02 ?  105 ASP   A H    1 
ATOM   2138 H H    B ASP   A 1 105 ? 25.790 -6.991  -13.420 0.34 22.18 ?  105 ASP   A H    1 
ATOM   2139 H HA   A ASP   A 1 105 ? 23.515 -7.864  -14.332 0.66 31.93 ?  105 ASP   A HA   1 
ATOM   2140 H HA   B ASP   A 1 105 ? 23.867 -8.527  -14.373 0.34 22.76 ?  105 ASP   A HA   1 
ATOM   2141 H HB2  A ASP   A 1 105 ? 25.780 -8.412  -14.728 0.66 35.11 ?  105 ASP   A HB2  1 
ATOM   2142 H HB2  B ASP   A 1 105 ? 26.148 -9.085  -14.563 0.34 25.03 ?  105 ASP   A HB2  1 
ATOM   2143 H HB3  A ASP   A 1 105 ? 25.950 -8.733  -13.181 0.66 35.11 ?  105 ASP   A HB3  1 
ATOM   2144 H HB3  B ASP   A 1 105 ? 26.216 -9.281  -12.988 0.34 25.03 ?  105 ASP   A HB3  1 
ATOM   2145 N N    A ILE   A 1 106 ? 22.190 -8.603  -12.410 0.66 23.86 ?  106 ILE   A N    1 
ATOM   2146 N N    B ILE   A 1 106 ? 22.404 -9.163  -12.516 0.34 18.61 ?  106 ILE   A N    1 
ATOM   2147 C CA   A ILE   A 1 106 ? 21.430 -9.003  -11.232 0.66 23.03 ?  106 ILE   A CA   1 
ATOM   2148 C CA   B ILE   A 1 106 ? 21.573 -9.540  -11.375 0.34 19.65 ?  106 ILE   A CA   1 
ATOM   2149 C C    A ILE   A 1 106 ? 21.953 -10.303 -10.639 0.66 21.88 ?  106 ILE   A C    1 
ATOM   2150 C C    B ILE   A 1 106 ? 22.174 -10.720 -10.625 0.34 19.76 ?  106 ILE   A C    1 
ATOM   2151 O O    A ILE   A 1 106 ? 21.736 -10.566 -9.451  0.66 21.45 ?  106 ILE   A O    1 
ATOM   2152 O O    B ILE   A 1 106 ? 21.968 -10.861 -9.413  0.34 19.91 ?  106 ILE   A O    1 
ATOM   2153 C CB   A ILE   A 1 106 ? 19.924 -9.083  -11.561 0.66 24.03 ?  106 ILE   A CB   1 
ATOM   2154 C CB   B ILE   A 1 106 ? 20.131 -9.832  -11.834 0.34 20.81 ?  106 ILE   A CB   1 
ATOM   2155 C CG1  A ILE   A 1 106 ? 19.087 -9.178  -10.282 0.66 24.44 ?  106 ILE   A CG1  1 
ATOM   2156 C CG1  B ILE   A 1 106 ? 19.195 -9.992  -10.633 0.34 21.33 ?  106 ILE   A CG1  1 
ATOM   2157 C CG2  A ILE   A 1 106 ? 19.633 -10.272 -12.465 0.66 24.57 ?  106 ILE   A CG2  1 
ATOM   2158 C CG2  B ILE   A 1 106 ? 20.086 -11.103 -12.656 0.34 21.15 ?  106 ILE   A CG2  1 
ATOM   2159 C CD1  A ILE   A 1 106 ? 19.210 -7.966  -9.376  0.66 24.69 ?  106 ILE   A CD1  1 
ATOM   2160 C CD1  B ILE   A 1 106 ? 19.065 -8.758  -9.778  0.34 21.75 ?  106 ILE   A CD1  1 
ATOM   2161 H H    A ILE   A 1 106 ? 21.747 -8.621  -13.141 0.66 28.61 ?  106 ILE   A H    1 
ATOM   2162 H H    B ILE   A 1 106 ? 22.011 -9.221  -13.275 0.34 22.31 ?  106 ILE   A H    1 
ATOM   2163 H HA   A ILE   A 1 106 ? 21.548 -8.322  -10.556 0.66 27.61 ?  106 ILE   A HA   1 
ATOM   2164 H HA   B ILE   A 1 106 ? 21.546 -8.799  -10.759 0.34 23.56 ?  106 ILE   A HA   1 
ATOM   2165 H HB   A ILE   A 1 106 ? 19.671 -8.274  -12.031 0.66 28.81 ?  106 ILE   A HB   1 
ATOM   2166 H HB   B ILE   A 1 106 ? 19.820 -9.095  -12.381 0.34 24.95 ?  106 ILE   A HB   1 
ATOM   2167 H HG12 A ILE   A 1 106 ? 18.153 -9.266  -10.526 0.66 29.31 ?  106 ILE   A HG12 1 
ATOM   2168 H HG12 B ILE   A 1 106 ? 18.310 -10.221 -10.960 0.34 25.57 ?  106 ILE   A HG12 1 
ATOM   2169 H HG13 A ILE   A 1 106 ? 19.369 -9.954  -9.776  0.66 29.31 ?  106 ILE   A HG13 1 
ATOM   2170 H HG13 B ILE   A 1 106 ? 19.527 -10.709 -10.072 0.34 25.57 ?  106 ILE   A HG13 1 
ATOM   2171 H HG21 A ILE   A 1 106 ? 18.732 -10.186 -12.813 0.66 29.46 ?  106 ILE   A HG21 1 
ATOM   2172 H HG21 B ILE   A 1 106 ? 19.218 -11.172 -13.079 0.34 25.36 ?  106 ILE   A HG21 1 
ATOM   2173 H HG22 A ILE   A 1 106 ? 20.271 -10.272 -13.194 0.66 29.46 ?  106 ILE   A HG22 1 
ATOM   2174 H HG22 B ILE   A 1 106 ? 20.784 -11.069 -13.327 0.34 25.36 ?  106 ILE   A HG22 1 
ATOM   2175 H HG23 A ILE   A 1 106 ? 19.715 -11.088 -11.950 0.66 29.46 ?  106 ILE   A HG23 1 
ATOM   2176 H HG23 B ILE   A 1 106 ? 20.228 -11.864 -12.069 0.34 25.36 ?  106 ILE   A HG23 1 
ATOM   2177 H HD11 A ILE   A 1 106 ? 18.490 -7.984  -8.727  0.66 29.60 ?  106 ILE   A HD11 1 
ATOM   2178 H HD11 B ILE   A 1 106 ? 18.313 -8.873  -9.179  0.34 26.08 ?  106 ILE   A HD11 1 
ATOM   2179 H HD12 A ILE   A 1 106 ? 20.066 -7.995  -8.920  0.66 29.60 ?  106 ILE   A HD12 1 
ATOM   2180 H HD12 B ILE   A 1 106 ? 19.881 -8.642  -9.268  0.34 26.08 ?  106 ILE   A HD12 1 
ATOM   2181 H HD13 A ILE   A 1 106 ? 19.148 -7.161  -9.915  0.66 29.60 ?  106 ILE   A HD13 1 
ATOM   2182 H HD13 B ILE   A 1 106 ? 18.918 -7.993  -10.354 0.34 26.08 ?  106 ILE   A HD13 1 
ATOM   2183 N N    A GLN   A 1 107 ? 22.655 -11.116 -11.435 0.66 22.96 ?  107 GLN   A N    1 
ATOM   2184 N N    B GLN   A 1 107 ? 22.921 -11.584 -11.321 0.34 20.10 ?  107 GLN   A N    1 
ATOM   2185 C CA   A GLN   A 1 107 ? 23.268 -12.333 -10.917 0.66 24.69 ?  107 GLN   A CA   1 
ATOM   2186 C CA   B GLN   A 1 107 ? 23.544 -12.722 -10.652 0.34 21.38 ?  107 GLN   A CA   1 
ATOM   2187 C C    A GLN   A 1 107 ? 24.263 -12.037 -9.801  0.66 22.10 ?  107 GLN   A C    1 
ATOM   2188 C C    B GLN   A 1 107 ? 24.448 -12.263 -9.517  0.34 18.83 ?  107 GLN   A C    1 
ATOM   2189 O O    A GLN   A 1 107 ? 24.538 -12.915 -8.977  0.66 23.73 ?  107 GLN   A O    1 
ATOM   2190 O O    B GLN   A 1 107 ? 24.637 -12.989 -8.533  0.34 18.09 ?  107 GLN   A O    1 
ATOM   2191 C CB   A GLN   A 1 107 ? 23.957 -13.091 -12.058 0.66 29.15 ?  107 GLN   A CB   1 
ATOM   2192 C CB   B GLN   A 1 107 ? 24.324 -13.566 -11.666 0.34 25.01 ?  107 GLN   A CB   1 
ATOM   2193 C CG   A GLN   A 1 107 ? 23.062 -13.344 -13.266 0.66 33.81 ?  107 GLN   A CG   1 
ATOM   2194 C CG   B GLN   A 1 107 ? 23.478 -14.075 -12.828 0.34 28.34 ?  107 GLN   A CG   1 
ATOM   2195 C CD   A GLN   A 1 107 ? 21.801 -14.104 -12.909 0.66 37.68 ?  107 GLN   A CD   1 
ATOM   2196 C CD   B GLN   A 1 107 ? 22.394 -15.037 -12.385 0.34 31.18 ?  107 GLN   A CD   1 
ATOM   2197 O OE1  A GLN   A 1 107 ? 21.851 -15.140 -12.246 0.66 39.23 ?  107 GLN   A OE1  1 
ATOM   2198 O OE1  B GLN   A 1 107 ? 22.585 -15.820 -11.454 0.34 31.99 ?  107 GLN   A OE1  1 
ATOM   2199 N NE2  A GLN   A 1 107 ? 20.658 -13.587 -13.343 0.66 38.87 ?  107 GLN   A NE2  1 
ATOM   2200 N NE2  B GLN   A 1 107 ? 21.244 -14.980 -13.050 0.34 32.06 ?  107 GLN   A NE2  1 
ATOM   2201 H H    A GLN   A 1 107 ? 22.796 -10.976 -12.271 0.66 27.53 ?  107 GLN   A H    1 
ATOM   2202 H H    B GLN   A 1 107 ? 23.092 -11.530 -12.162 0.34 24.10 ?  107 GLN   A H    1 
ATOM   2203 H HA   A GLN   A 1 107 ? 22.580 -12.908 -10.557 0.66 29.60 ?  107 GLN   A HA   1 
ATOM   2204 H HA   B GLN   A 1 107 ? 22.856 -13.287 -10.273 0.34 25.63 ?  107 GLN   A HA   1 
ATOM   2205 H HB2  A GLN   A 1 107 ? 24.722 -12.579 -12.364 0.66 34.95 ?  107 GLN   A HB2  1 
ATOM   2206 H HB2  B GLN   A 1 107 ? 25.041 -13.032 -12.040 0.34 29.98 ?  107 GLN   A HB2  1 
ATOM   2207 H HB3  A GLN   A 1 107 ? 24.252 -13.956 -11.731 0.66 34.95 ?  107 GLN   A HB3  1 
ATOM   2208 H HB3  B GLN   A 1 107 ? 24.695 -14.344 -11.216 0.34 29.98 ?  107 GLN   A HB3  1 
ATOM   2209 H HG2  A GLN   A 1 107 ? 22.800 -12.495 -13.655 0.66 40.55 ?  107 GLN   A HG2  1 
ATOM   2210 H HG2  B GLN   A 1 107 ? 23.051 -13.322 -13.265 0.34 33.98 ?  107 GLN   A HG2  1 
ATOM   2211 H HG3  A GLN   A 1 107 ? 23.554 -13.867 -13.921 0.66 40.55 ?  107 GLN   A HG3  1 
ATOM   2212 H HG3  B GLN   A 1 107 ? 24.052 -14.540 -13.459 0.34 33.98 ?  107 GLN   A HG3  1 
ATOM   2213 H HE21 A GLN   A 1 107 ? 20.661 -12.860 -13.803 0.66 46.62 ?  107 GLN   A HE21 1 
ATOM   2214 H HE21 B GLN   A 1 107 ? 21.147 -14.419 -13.694 0.34 38.45 ?  107 GLN   A HE21 1 
ATOM   2215 H HE22 A GLN   A 1 107 ? 19.916 -13.982 -13.165 0.66 46.62 ?  107 GLN   A HE22 1 
ATOM   2216 H HE22 B GLN   A 1 107 ? 20.598 -15.507 -12.837 0.34 38.45 ?  107 GLN   A HE22 1 
ATOM   2217 N N    A LEU   A 1 108 ? 24.794 -10.812 -9.739  0.66 18.03 ?  108 LEU   A N    1 
ATOM   2218 N N    B LEU   A 1 108 ? 24.996 -11.052 -9.624  0.34 17.11 ?  108 LEU   A N    1 
ATOM   2219 C CA   A LEU   A 1 108 ? 25.736 -10.441 -8.689  0.66 15.88 ?  108 LEU   A CA   1 
ATOM   2220 C CA   B LEU   A 1 108 ? 25.832 -10.502 -8.567  0.34 15.93 ?  108 LEU   A CA   1 
ATOM   2221 C C    A LEU   A 1 108 ? 25.058 -10.270 -7.336  0.66 14.20 ?  108 LEU   A C    1 
ATOM   2222 C C    B LEU   A 1 108 ? 25.062 -10.243 -7.280  0.34 14.53 ?  108 LEU   A C    1 
ATOM   2223 O O    A LEU   A 1 108 ? 25.753 -10.128 -6.326  0.66 14.37 ?  108 LEU   A O    1 
ATOM   2224 O O    B LEU   A 1 108 ? 25.696 -9.992  -6.250  0.34 14.74 ?  108 LEU   A O    1 
ATOM   2225 C CB   A LEU   A 1 108 ? 26.491 -9.166  -9.080  0.66 15.74 ?  108 LEU   A CB   1 
ATOM   2226 C CB   B LEU   A 1 108 ? 26.525 -9.223  -9.047  0.34 16.26 ?  108 LEU   A CB   1 
ATOM   2227 C CG   A LEU   A 1 108 ? 27.480 -9.364  -10.231 0.66 17.25 ?  108 LEU   A CG   1 
ATOM   2228 C CG   B LEU   A 1 108 ? 27.572 -9.438  -10.143 0.34 17.23 ?  108 LEU   A CG   1 
ATOM   2229 C CD1  A LEU   A 1 108 ? 27.943 -8.033  -10.798 0.66 18.18 ?  108 LEU   A CD1  1 
ATOM   2230 C CD1  B LEU   A 1 108 ? 28.083 -8.111  -10.677 0.34 17.69 ?  108 LEU   A CD1  1 
ATOM   2231 C CD2  A LEU   A 1 108 ? 28.679 -10.189 -9.780  0.66 18.82 ?  108 LEU   A CD2  1 
ATOM   2232 C CD2  B LEU   A 1 108 ? 28.729 -10.283 -9.628  0.34 18.19 ?  108 LEU   A CD2  1 
ATOM   2233 H H    A LEU   A 1 108 ? 24.615 -10.187 -10.293 0.66 21.62 ?  108 LEU   A H    1 
ATOM   2234 H H    B LEU   A 1 108 ? 24.897 -10.537 -10.300 0.34 20.51 ?  108 LEU   A H    1 
ATOM   2235 H HA   A LEU   A 1 108 ? 26.385 -11.154 -8.596  0.66 19.03 ?  108 LEU   A HA   1 
ATOM   2236 H HA   B LEU   A 1 108 ? 26.523 -11.148 -8.357  0.34 19.09 ?  108 LEU   A HA   1 
ATOM   2237 H HB2  A LEU   A 1 108 ? 25.845 -8.497  -9.357  0.66 18.86 ?  108 LEU   A HB2  1 
ATOM   2238 H HB2  B LEU   A 1 108 ? 25.853 -8.619  -9.398  0.34 19.49 ?  108 LEU   A HB2  1 
ATOM   2239 H HB3  A LEU   A 1 108 ? 26.985 -8.852  -8.311  0.66 18.86 ?  108 LEU   A HB3  1 
ATOM   2240 H HB3  B LEU   A 1 108 ? 26.972 -8.812  -8.292  0.34 19.49 ?  108 LEU   A HB3  1 
ATOM   2241 H HG   A LEU   A 1 108 ? 27.039 -9.854  -10.943 0.66 20.67 ?  108 LEU   A HG   1 
ATOM   2242 H HG   B LEU   A 1 108 ? 27.162 -9.916  -10.881 0.34 20.65 ?  108 LEU   A HG   1 
ATOM   2243 H HD11 A LEU   A 1 108 ? 28.548 -8.199  -11.540 0.66 21.79 ?  108 LEU   A HD11 1 
ATOM   2244 H HD11 B LEU   A 1 108 ? 28.720 -8.281  -11.390 0.34 21.21 ?  108 LEU   A HD11 1 
ATOM   2245 H HD12 A LEU   A 1 108 ? 27.170 -7.536  -11.107 0.66 21.79 ?  108 LEU   A HD12 1 
ATOM   2246 H HD12 B LEU   A 1 108 ? 27.333 -7.600  -11.020 0.34 21.21 ?  108 LEU   A HD12 1 
ATOM   2247 H HD13 A LEU   A 1 108 ? 28.402 -7.535  -10.104 0.66 21.79 ?  108 LEU   A HD13 1 
ATOM   2248 H HD13 B LEU   A 1 108 ? 28.514 -7.626  -9.957  0.34 21.21 ?  108 LEU   A HD13 1 
ATOM   2249 H HD21 A LEU   A 1 108 ? 29.347 -10.183 -10.482 0.66 22.56 ?  108 LEU   A HD21 1 
ATOM   2250 H HD21 B LEU   A 1 108 ? 29.459 -10.238 -10.264 0.34 21.80 ?  108 LEU   A HD21 1 
ATOM   2251 H HD22 A LEU   A 1 108 ? 29.044 -9.796  -8.971  0.66 22.56 ?  108 LEU   A HD22 1 
ATOM   2252 H HD22 B LEU   A 1 108 ? 29.015 -9.932  -8.770  0.34 21.80 ?  108 LEU   A HD22 1 
ATOM   2253 H HD23 A LEU   A 1 108 ? 28.390 -11.098 -9.604  0.66 22.56 ?  108 LEU   A HD23 1 
ATOM   2254 H HD23 B LEU   A 1 108 ? 28.431 -11.200 -9.529  0.34 21.80 ?  108 LEU   A HD23 1 
ATOM   2255 N N    . LEU   A 1 109 ? 23.725 -10.313 -7.290  1.00 13.61 ?  109 LEU   A N    1 
ATOM   2256 C CA   . LEU   A 1 109 ? 23.010 -10.182 -6.027  1.00 12.79 ?  109 LEU   A CA   1 
ATOM   2257 C C    . LEU   A 1 109 ? 23.347 -11.335 -5.085  1.00 12.10 ?  109 LEU   A C    1 
ATOM   2258 O O    . LEU   A 1 109 ? 23.482 -11.137 -3.873  1.00 12.74 ?  109 LEU   A O    1 
ATOM   2259 C CB   . LEU   A 1 109 ? 21.507 -10.101 -6.288  1.00 13.92 ?  109 LEU   A CB   1 
ATOM   2260 C CG   . LEU   A 1 109 ? 20.605 -9.812  -5.088  1.00 14.28 ?  109 LEU   A CG   1 
ATOM   2261 C CD1  . LEU   A 1 109 ? 21.051 -8.540  -4.377  1.00 14.67 ?  109 LEU   A CD1  1 
ATOM   2262 C CD2  . LEU   A 1 109 ? 19.156 -9.691  -5.533  1.00 15.35 ?  109 LEU   A CD2  1 
ATOM   2263 H H    A LEU   A 1 109 ? 23.214 -10.424 -7.974  0.66 16.31 ?  109 LEU   A H    1 
ATOM   2264 H H    B LEU   A 1 109 ? 23.231 -10.439 -7.984  0.34 16.31 ?  109 LEU   A H    1 
ATOM   2265 H HA   . LEU   A 1 109 ? 23.287 -9.358  -5.600  1.00 15.32 ?  109 LEU   A HA   1 
ATOM   2266 H HB2  . LEU   A 1 109 ? 21.353 -9.394  -6.935  1.00 16.68 ?  109 LEU   A HB2  1 
ATOM   2267 H HB3  . LEU   A 1 109 ? 21.218 -10.945 -6.662  1.00 16.68 ?  109 LEU   A HB3  1 
ATOM   2268 H HG   . LEU   A 1 109 ? 20.664 -10.542 -4.458  1.00 17.11 ?  109 LEU   A HG   1 
ATOM   2269 H HD11 . LEU   A 1 109 ? 20.367 -8.267  -3.746  1.00 17.58 ?  109 LEU   A HD11 1 
ATOM   2270 H HD12 . LEU   A 1 109 ? 21.884 -8.709  -3.912  1.00 17.58 ?  109 LEU   A HD12 1 
ATOM   2271 H HD13 . LEU   A 1 109 ? 21.181 -7.836  -5.039  1.00 17.58 ?  109 LEU   A HD13 1 
ATOM   2272 H HD21 . LEU   A 1 109 ? 18.613 -9.396  -4.781  1.00 18.40 ?  109 LEU   A HD21 1 
ATOM   2273 H HD22 . LEU   A 1 109 ? 19.091 -9.044  -6.254  1.00 18.40 ?  109 LEU   A HD22 1 
ATOM   2274 H HD23 . LEU   A 1 109 ? 18.842 -10.558 -5.841  1.00 18.40 ?  109 LEU   A HD23 1 
ATOM   2275 N N    . LYS   A 1 110 ? 23.495 -12.550 -5.619  1.00 12.26 ?  110 LYS   A N    1 
ATOM   2276 C CA   . LYS   A 1 110 ? 23.877 -13.668 -4.762  1.00 12.41 ?  110 LYS   A CA   1 
ATOM   2277 C C    . LYS   A 1 110 ? 25.257 -13.440 -4.154  1.00 12.09 ?  110 LYS   A C    1 
ATOM   2278 O O    . LYS   A 1 110 ? 25.452 -13.643 -2.951  1.00 12.37 ?  110 LYS   A O    1 
ATOM   2279 C CB   . LYS   A 1 110 ? 23.810 -14.991 -5.528  1.00 13.31 ?  110 LYS   A CB   1 
ATOM   2280 C CG   . LYS   A 1 110 ? 24.000 -16.204 -4.616  1.00 13.79 ?  110 LYS   A CG   1 
ATOM   2281 C CD   . LYS   A 1 110 ? 23.767 -17.528 -5.332  1.00 14.38 ?  110 LYS   A CD   1 
ATOM   2282 C CE   . LYS   A 1 110 ? 23.871 -18.708 -4.375  1.00 15.30 ?  110 LYS   A CE   1 
ATOM   2283 N NZ   . LYS   A 1 110 ? 22.681 -18.821 -3.493  1.00 15.54 ?  110 LYS   A NZ   1 
ATOM   2284 H H    . LYS   A 1 110 ? 23.385 -12.747 -6.447  1.00 14.69 ?  110 LYS   A H    1 
ATOM   2285 H HA   . LYS   A 1 110 ? 23.239 -13.723 -4.029  1.00 14.87 ?  110 LYS   A HA   1 
ATOM   2286 H HB2  . LYS   A 1 110 ? 22.944 -15.067 -5.954  1.00 15.95 ?  110 LYS   A HB2  1 
ATOM   2287 H HB3  . LYS   A 1 110 ? 24.514 -15.005 -6.193  1.00 15.95 ?  110 LYS   A HB3  1 
ATOM   2288 H HG2  . LYS   A 1 110 ? 24.905 -16.206 -4.271  1.00 16.52 ?  110 LYS   A HG2  1 
ATOM   2289 H HG3  . LYS   A 1 110 ? 23.366 -16.150 -3.882  1.00 16.52 ?  110 LYS   A HG3  1 
ATOM   2290 H HD2  . LYS   A 1 110 ? 22.882 -17.532 -5.721  1.00 17.23 ?  110 LYS   A HD2  1 
ATOM   2291 H HD3  . LYS   A 1 110 ? 24.441 -17.637 -6.023  1.00 17.23 ?  110 LYS   A HD3  1 
ATOM   2292 H HE2  . LYS   A 1 110 ? 23.952 -19.528 -4.885  1.00 18.34 ?  110 LYS   A HE2  1 
ATOM   2293 H HE3  . LYS   A 1 110 ? 24.655 -18.590 -3.808  1.00 18.34 ?  110 LYS   A HE3  1 
ATOM   2294 H HZ1  . LYS   A 1 110 ? 22.765 -19.514 -2.946  1.00 18.62 ?  110 LYS   A HZ1  1 
ATOM   2295 H HZ2  . LYS   A 1 110 ? 22.586 -18.077 -3.009  1.00 18.62 ?  110 LYS   A HZ2  1 
ATOM   2296 H HZ3  . LYS   A 1 110 ? 21.946 -18.931 -3.989  1.00 18.62 ?  110 LYS   A HZ3  1 
ATOM   2297 N N    . SER   A 1 111 ? 26.220 -12.994 -4.966  1.00 12.05 ?  111 SER   A N    1 
ATOM   2298 C CA   . SER   A 1 111 ? 27.548 -12.695 -4.444  1.00 12.04 ?  111 SER   A CA   1 
ATOM   2299 C C    . SER   A 1 111 ? 27.480 -11.644 -3.340  1.00 11.40 ?  111 SER   A C    1 
ATOM   2300 O O    . SER   A 1 111 ? 28.179 -11.747 -2.324  1.00 12.06 ?  111 SER   A O    1 
ATOM   2301 C CB   . SER   A 1 111 ? 28.443 -12.203 -5.581  1.00 13.83 ?  111 SER   A CB   1 
ATOM   2302 O OG   . SER   A 1 111 ? 28.514 -13.177 -6.613  1.00 15.55 ?  111 SER   A OG   1 
ATOM   2303 H H    . SER   A 1 111 ? 26.122 -12.856 -5.806  1.00 14.43 ?  111 SER   A H    1 
ATOM   2304 H HA   . SER   A 1 111 ? 27.935 -13.504 -4.074  1.00 14.42 ?  111 SER   A HA   1 
ATOM   2305 H HB2  . SER   A 1 111 ? 28.066 -11.392 -5.952  1.00 16.57 ?  111 SER   A HB2  1 
ATOM   2306 H HB3  . SER   A 1 111 ? 29.330 -12.029 -5.229  1.00 16.57 ?  111 SER   A HB3  1 
ATOM   2307 H HG   . SER   A 1 111 ? 29.032 -12.904 -7.224  1.00 18.63 ?  111 SER   A HG   1 
ATOM   2308 N N    . ALA   A 1 112 ? 26.636 -10.624 -3.523  1.00 11.45 ?  112 ALA   A N    1 
ATOM   2309 C CA   . ALA   A 1 112 ? 26.482 -9.585  -2.506  1.00 11.48 ?  112 ALA   A CA   1 
ATOM   2310 C C    . ALA   A 1 112 ? 26.003 -10.183 -1.187  1.00 11.16 ?  112 ALA   A C    1 
ATOM   2311 O O    . ALA   A 1 112 ? 26.553 -9.896  -0.118  1.00 11.70 ?  112 ALA   A O    1 
ATOM   2312 C CB   . ALA   A 1 112 ? 25.511 -8.509  -2.998  1.00 12.02 ?  112 ALA   A CB   1 
ATOM   2313 H H    . ALA   A 1 112 ? 26.152 -10.506 -4.223  1.00 13.72 ?  112 ALA   A H    1 
ATOM   2314 H HA   . ALA   A 1 112 ? 27.343 -9.159  -2.350  1.00 13.76 ?  112 ALA   A HA   1 
ATOM   2315 H HB1  . ALA   A 1 112 ? 25.433 -7.815  -2.319  1.00 14.40 ?  112 ALA   A HB1  1 
ATOM   2316 H HB2  . ALA   A 1 112 ? 25.853 -8.121  -3.820  1.00 14.40 ?  112 ALA   A HB2  1 
ATOM   2317 H HB3  . ALA   A 1 112 ? 24.644 -8.911  -3.157  1.00 14.40 ?  112 ALA   A HB3  1 
ATOM   2318 N N    . TYR   A 1 113 ? 24.967 -11.026 -1.238  1.00 11.43 ?  113 TYR   A N    1 
ATOM   2319 C CA   . TYR   A 1 113 ? 24.455 -11.628 -0.009  1.00 11.23 ?  113 TYR   A CA   1 
ATOM   2320 C C    . TYR   A 1 113 ? 25.455 -12.586 0.637   1.00 10.86 ?  113 TYR   A C    1 
ATOM   2321 O O    . TYR   A 1 113 ? 25.418 -12.772 1.858   1.00 11.52 ?  113 TYR   A O    1 
ATOM   2322 C CB   . TYR   A 1 113 ? 23.135 -12.355 -0.279  1.00 11.70 ?  113 TYR   A CB   1 
ATOM   2323 C CG   . TYR   A 1 113 ? 21.918 -11.456 -0.216  1.00 11.69 ?  113 TYR   A CG   1 
ATOM   2324 C CD1  . TYR   A 1 113 ? 21.551 -10.829 0.972   1.00 12.26 ?  113 TYR   A CD1  1 
ATOM   2325 C CD2  . TYR   A 1 113 ? 21.122 -11.254 -1.335  1.00 12.39 ?  113 TYR   A CD2  1 
ATOM   2326 C CE1  . TYR   A 1 113 ? 20.428 -10.030 1.041   1.00 13.04 ?  113 TYR   A CE1  1 
ATOM   2327 C CE2  . TYR   A 1 113 ? 19.978 -10.446 -1.274  1.00 12.77 ?  113 TYR   A CE2  1 
ATOM   2328 C CZ   . TYR   A 1 113 ? 19.644 -9.842  -0.081  1.00 12.70 ?  113 TYR   A CZ   1 
ATOM   2329 O OH   . TYR   A 1 113 ? 18.518 -9.047  0.006   1.00 13.89 ?  113 TYR   A OH   1 
ATOM   2330 H H    . TYR   A 1 113 ? 24.557 -11.260 -1.956  1.00 13.70 ?  113 TYR   A H    1 
ATOM   2331 H HA   . TYR   A 1 113 ? 24.280 -10.921 0.629   1.00 13.45 ?  113 TYR   A HA   1 
ATOM   2332 H HB2  . TYR   A 1 113 ? 23.168 -12.743 -1.166  1.00 14.01 ?  113 TYR   A HB2  1 
ATOM   2333 H HB3  . TYR   A 1 113 ? 23.025 -13.054 0.384   1.00 14.01 ?  113 TYR   A HB3  1 
ATOM   2334 H HD1  . TYR   A 1 113 ? 22.072 -10.962 1.736   1.00 14.69 ?  113 TYR   A HD1  1 
ATOM   2335 H HD2  . TYR   A 1 113 ? 21.343 -11.671 -2.135  1.00 14.84 ?  113 TYR   A HD2  1 
ATOM   2336 H HE1  . TYR   A 1 113 ? 20.197 -9.625  1.843   1.00 15.62 ?  113 TYR   A HE1  1 
ATOM   2337 H HE2  . TYR   A 1 113 ? 19.447 -10.320 -2.028  1.00 15.30 ?  113 TYR   A HE2  1 
ATOM   2338 H HH   . TYR   A 1 113 ? 18.139 -9.018  -0.748  1.00 16.65 ?  113 TYR   A HH   1 
ATOM   2339 N N    . GLU   A 1 114 ? 26.352 -13.204 -0.147  1.00 11.22 ?  114 GLU   A N    1 
ATOM   2340 C CA   . GLU   A 1 114 ? 27.348 -14.100 0.443   1.00 11.56 ?  114 GLU   A CA   1 
ATOM   2341 C C    . GLU   A 1 114 ? 28.200 -13.388 1.491   1.00 11.53 ?  114 GLU   A C    1 
ATOM   2342 O O    . GLU   A 1 114 ? 28.682 -14.021 2.440   1.00 11.87 ?  114 GLU   A O    1 
ATOM   2343 C CB   . GLU   A 1 114 ? 28.215 -14.735 -0.652  1.00 11.85 ?  114 GLU   A CB   1 
ATOM   2344 C CG   . GLU   A 1 114 ? 27.458 -15.792 -1.435  1.00 12.32 ?  114 GLU   A CG   1 
ATOM   2345 C CD   . GLU   A 1 114 ? 28.176 -16.325 -2.666  1.00 12.59 ?  114 GLU   A CD   1 
ATOM   2346 O OE1  . GLU   A 1 114 ? 29.128 -15.683 -3.165  1.00 12.94 ?  114 GLU   A OE1  1 
ATOM   2347 O OE2  . GLU   A 1 114 ? 27.742 -17.393 -3.159  1.00 13.97 -1 114 GLU   A OE2  1 
ATOM   2348 H H    . GLU   A 1 114 ? 26.403 -13.112 -1.008  1.00 13.45 ?  114 GLU   A H    1 
ATOM   2349 H HA   . GLU   A 1 114 ? 26.877 -14.815 0.887   1.00 13.85 ?  114 GLU   A HA   1 
ATOM   2350 H HB2  . GLU   A 1 114 ? 28.505 -14.050 -1.277  1.00 14.20 ?  114 GLU   A HB2  1 
ATOM   2351 H HB3  . GLU   A 1 114 ? 28.985 -15.160 -0.243  1.00 14.20 ?  114 GLU   A HB3  1 
ATOM   2352 H HG2  . GLU   A 1 114 ? 27.292 -16.550 -0.855  1.00 14.76 ?  114 GLU   A HG2  1 
ATOM   2353 H HG3  . GLU   A 1 114 ? 26.612 -15.417 -1.729  1.00 14.76 ?  114 GLU   A HG3  1 
ATOM   2354 N N    . ASN   A 1 115 ? 28.381 -12.070 1.358   1.00 11.29 ?  115 ASN   A N    1 
ATOM   2355 C CA   . ASN   A 1 115 ? 29.153 -11.342 2.360   1.00 11.65 ?  115 ASN   A CA   1 
ATOM   2356 C C    . ASN   A 1 115 ? 28.538 -11.473 3.748   1.00 11.44 ?  115 ASN   A C    1 
ATOM   2357 O O    . ASN   A 1 115 ? 29.253 -11.408 4.756   1.00 11.91 ?  115 ASN   A O    1 
ATOM   2358 C CB   . ASN   A 1 115 ? 29.264 -9.866  1.980   1.00 11.87 ?  115 ASN   A CB   1 
ATOM   2359 C CG   . ASN   A 1 115 ? 30.055 -9.655  0.713   1.00 12.41 ?  115 ASN   A CG   1 
ATOM   2360 O OD1  . ASN   A 1 115 ? 31.273 -9.779  0.716   1.00 15.82 ?  115 ASN   A OD1  1 
ATOM   2361 N ND2  . ASN   A 1 115 ? 29.376 -9.333  -0.373  1.00 11.83 ?  115 ASN   A ND2  1 
ATOM   2362 H H    . ASN   A 1 115 ? 28.069 -11.581 0.719   1.00 13.52 ?  115 ASN   A H    1 
ATOM   2363 H HA   . ASN   A 1 115 ? 30.047 -11.710 2.398   1.00 13.95 ?  115 ASN   A HA   1 
ATOM   2364 H HB2  . ASN   A 1 115 ? 28.375 -9.504  1.853   1.00 14.22 ?  115 ASN   A HB2  1 
ATOM   2365 H HB3  . ASN   A 1 115 ? 29.714 -9.390  2.700   1.00 14.22 ?  115 ASN   A HB3  1 
ATOM   2366 H HD21 . ASN   A 1 115 ? 29.787 -9.200  -1.117  1.00 14.18 ?  115 ASN   A HD21 1 
ATOM   2367 H HD22 . ASN   A 1 115 ? 28.518 -9.266  -0.339  1.00 14.18 ?  115 ASN   A HD22 1 
ATOM   2368 N N    . PHE   A 1 116 ? 27.211 -11.640 3.829   1.00 11.59 ?  116 PHE   A N    1 
ATOM   2369 C CA   . PHE   A 1 116 ? 26.561 -11.735 5.134   1.00 11.19 ?  116 PHE   A CA   1 
ATOM   2370 C C    . PHE   A 1 116 ? 27.034 -12.966 5.907   1.00 11.59 ?  116 PHE   A C    1 
ATOM   2371 O O    . PHE   A 1 116 ? 26.964 -12.981 7.138   1.00 12.23 ?  116 PHE   A O    1 
ATOM   2372 C CB   . PHE   A 1 116 ? 25.033 -11.862 5.000   1.00 11.73 ?  116 PHE   A CB   1 
ATOM   2373 C CG   . PHE   A 1 116 ? 24.274 -10.620 4.526   1.00 11.52 ?  116 PHE   A CG   1 
ATOM   2374 C CD1  . PHE   A 1 116 ? 24.841 -9.605  3.760   1.00 11.71 ?  116 PHE   A CD1  1 
ATOM   2375 C CD2  . PHE   A 1 116 ? 22.922 -10.515 4.853   1.00 12.01 ?  116 PHE   A CD2  1 
ATOM   2376 C CE1  . PHE   A 1 116 ? 24.068 -8.532  3.335   1.00 12.05 ?  116 PHE   A CE1  1 
ATOM   2377 C CE2  . PHE   A 1 116 ? 22.153 -9.447  4.440   1.00 12.23 ?  116 PHE   A CE2  1 
ATOM   2378 C CZ   . PHE   A 1 116 ? 22.719 -8.454  3.680   1.00 11.85 ?  116 PHE   A CZ   1 
ATOM   2379 H H    . PHE   A 1 116 ? 26.675 -11.688 3.156   1.00 13.88 ?  116 PHE   A H    1 
ATOM   2380 H HA   . PHE   A 1 116 ? 26.758 -10.942 5.657   1.00 13.40 ?  116 PHE   A HA   1 
ATOM   2381 H HB2  . PHE   A 1 116 ? 24.848 -12.576 4.367   1.00 14.05 ?  116 PHE   A HB2  1 
ATOM   2382 H HB3  . PHE   A 1 116 ? 24.677 -12.110 5.869   1.00 14.05 ?  116 PHE   A HB3  1 
ATOM   2383 H HD1  . PHE   A 1 116 ? 25.735 -9.667  3.520   1.00 14.03 ?  116 PHE   A HD1  1 
ATOM   2384 H HD2  . PHE   A 1 116 ? 22.525 -11.197 5.362   1.00 14.38 ?  116 PHE   A HD2  1 
ATOM   2385 H HE1  . PHE   A 1 116 ? 24.457 -7.861  2.829   1.00 14.44 ?  116 PHE   A HE1  1 
ATOM   2386 H HE2  . PHE   A 1 116 ? 21.254 -9.409  4.680   1.00 14.65 ?  116 PHE   A HE2  1 
ATOM   2387 H HZ   . PHE   A 1 116 ? 22.208 -7.728  3.410   1.00 14.20 ?  116 PHE   A HZ   1 
ATOM   2388 N N    . ASN   A 1 117 ? 27.475 -14.016 5.203   1.00 11.68 ?  117 ASN   A N    1 
ATOM   2389 C CA   . ASN   A 1 117 ? 27.844 -15.260 5.873   1.00 12.14 ?  117 ASN   A CA   1 
ATOM   2390 C C    . ASN   A 1 117 ? 29.106 -15.139 6.709   1.00 12.67 ?  117 ASN   A C    1 
ATOM   2391 O O    . ASN   A 1 117 ? 29.407 -16.056 7.480   1.00 13.63 ?  117 ASN   A O    1 
ATOM   2392 C CB   . ASN   A 1 117 ? 27.966 -16.386 4.852   1.00 12.13 ?  117 ASN   A CB   1 
ATOM   2393 C CG   . ASN   A 1 117 ? 26.618 -16.778 4.311   1.00 12.33 ?  117 ASN   A CG   1 
ATOM   2394 O OD1  . ASN   A 1 117 ? 25.642 -16.809 5.058   1.00 13.12 ?  117 ASN   A OD1  1 
ATOM   2395 N ND2  . ASN   A 1 117 ? 26.537 -17.031 3.019   1.00 12.25 ?  117 ASN   A ND2  1 
ATOM   2396 H H    . ASN   A 1 117 ? 27.551 -14.029 4.343   1.00 14.00 ?  117 ASN   A H    1 
ATOM   2397 H HA   . ASN   A 1 117 ? 27.119 -15.492 6.474   1.00 14.55 ?  117 ASN   A HA   1 
ATOM   2398 H HB2  . ASN   A 1 117 ? 28.519 -16.084 4.111   1.00 14.54 ?  117 ASN   A HB2  1 
ATOM   2399 H HB3  . ASN   A 1 117 ? 28.363 -17.154 5.280   1.00 14.54 ?  117 ASN   A HB3  1 
ATOM   2400 H HD21 . ASN   A 1 117 ? 25.786 -17.251 2.677   1.00 14.67 ?  117 ASN   A HD21 1 
ATOM   2401 H HD22 . ASN   A 1 117 ? 27.243 -16.978 2.531   1.00 14.67 ?  117 ASN   A HD22 1 
ATOM   2402 N N    . GLN   A 1 118 ? 29.838 -14.033 6.587   1.00 12.45 ?  118 GLN   A N    1 
ATOM   2403 C CA   . GLN   A 1 118 ? 31.013 -13.796 7.412   1.00 13.05 ?  118 GLN   A CA   1 
ATOM   2404 C C    . GLN   A 1 118 ? 30.668 -13.218 8.779   1.00 13.15 ?  118 GLN   A C    1 
ATOM   2405 O O    . GLN   A 1 118 ? 31.584 -12.925 9.557   1.00 14.39 ?  118 GLN   A O    1 
ATOM   2406 C CB   . GLN   A 1 118 ? 32.007 -12.893 6.675   1.00 13.23 ?  118 GLN   A CB   1 
ATOM   2407 C CG   . GLN   A 1 118 ? 32.472 -13.475 5.350   1.00 13.27 ?  118 GLN   A CG   1 
ATOM   2408 C CD   . GLN   A 1 118 ? 33.305 -14.732 5.531   1.00 13.33 ?  118 GLN   A CD   1 
ATOM   2409 O OE1  . GLN   A 1 118 ? 34.173 -14.793 6.414   1.00 14.32 ?  118 GLN   A OE1  1 
ATOM   2410 N NE2  . GLN   A 1 118 ? 33.063 -15.738 4.687   1.00 13.57 ?  118 GLN   A NE2  1 
ATOM   2411 H H    . GLN   A 1 118 ? 29.665 -13.387 6.033   1.00 14.91 ?  118 GLN   A H    1 
ATOM   2412 H HA   . GLN   A 1 118 ? 31.444 -14.652 7.562   1.00 15.64 ?  118 GLN   A HA   1 
ATOM   2413 H HB2  . GLN   A 1 118 ? 31.583 -12.041 6.499   1.00 15.86 ?  118 GLN   A HB2  1 
ATOM   2414 H HB3  . GLN   A 1 118 ? 32.786 -12.768 7.240   1.00 15.86 ?  118 GLN   A HB3  1 
ATOM   2415 H HG2  . GLN   A 1 118 ? 31.698 -13.701 4.809   1.00 15.90 ?  118 GLN   A HG2  1 
ATOM   2416 H HG3  . GLN   A 1 118 ? 33.018 -12.820 4.890   1.00 15.90 ?  118 GLN   A HG3  1 
ATOM   2417 H HE21 . GLN   A 1 118 ? 32.446 -15.659 4.084   1.00 16.26 ?  118 GLN   A HE21 1 
ATOM   2418 H HE22 . GLN   A 1 118 ? 33.502 -16.474 4.746   1.00 16.26 ?  118 GLN   A HE22 1 
ATOM   2419 N N    . HIS   A 1 119 ? 29.380 -13.060 9.090   1.00 12.76 ?  119 HIS   A N    1 
ATOM   2420 C CA   . HIS   A 1 119 ? 28.931 -12.453 10.338  1.00 13.42 ?  119 HIS   A CA   1 
ATOM   2421 C C    . HIS   A 1 119 ? 27.796 -13.279 10.919  1.00 13.71 ?  119 HIS   A C    1 
ATOM   2422 O O    . HIS   A 1 119 ? 26.846 -13.620 10.208  1.00 14.25 ?  119 HIS   A O    1 
ATOM   2423 C CB   . HIS   A 1 119 ? 28.472 -11.019 10.070  1.00 13.68 ?  119 HIS   A CB   1 
ATOM   2424 C CG   . HIS   A 1 119 ? 29.543 -10.208 9.440   1.00 14.81 ?  119 HIS   A CG   1 
ATOM   2425 N ND1  . HIS   A 1 119 ? 30.529 -9.604  10.183  1.00 17.12 ?  119 HIS   A ND1  1 
ATOM   2426 C CD2  . HIS   A 1 119 ? 29.869 -10.020 8.142   1.00 16.06 ?  119 HIS   A CD2  1 
ATOM   2427 C CE1  . HIS   A 1 119 ? 31.385 -9.018  9.366   1.00 17.50 ?  119 HIS   A CE1  1 
ATOM   2428 N NE2  . HIS   A 1 119 ? 31.019 -9.269  8.122   1.00 17.33 ?  119 HIS   A NE2  1 
ATOM   2429 H H    . HIS   A 1 119 ? 28.726 -13.317 8.585   1.00 15.29 ?  119 HIS   A H    1 
ATOM   2430 H HA   . HIS   A 1 119 ? 29.662 -12.441 10.975  1.00 16.08 ?  119 HIS   A HA   1 
ATOM   2431 H HB2  . HIS   A 1 119 ? 27.706 -11.043 9.475   1.00 16.39 ?  119 HIS   A HB2  1 
ATOM   2432 H HB3  . HIS   A 1 119 ? 28.226 -10.610 10.915  1.00 16.39 ?  119 HIS   A HB3  1 
ATOM   2433 H HD1  . HIS   A 1 119 ? 30.564 -9.585  11.042  1.00 20.52 ?  119 HIS   A HD1  1 
ATOM   2434 H HD2  . HIS   A 1 119 ? 29.396 -10.335 7.403   1.00 19.25 ?  119 HIS   A HD2  1 
ATOM   2435 H HE1  . HIS   A 1 119 ? 32.121 -8.515  9.622   1.00 20.97 ?  119 HIS   A HE1  1 
ATOM   2436 N N    . GLU   A 1 120 ? 27.890 -13.583 12.216  1.00 14.69 ?  120 GLU   A N    1 
ATOM   2437 C CA   . GLU   A 1 120 ? 26.945 -14.513 12.833  1.00 17.07 ?  120 GLU   A CA   1 
ATOM   2438 C C    . GLU   A 1 120 ? 25.525 -13.955 12.888  1.00 15.64 ?  120 GLU   A C    1 
ATOM   2439 O O    . GLU   A 1 120 ? 24.551 -14.719 12.786  1.00 15.70 ?  120 GLU   A O    1 
ATOM   2440 C CB   . GLU   A 1 120 ? 27.421 -14.892 14.238  1.00 21.80 ?  120 GLU   A CB   1 
ATOM   2441 C CG   . GLU   A 1 120 ? 28.602 -15.846 14.255  1.00 28.96 ?  120 GLU   A CG   1 
ATOM   2442 C CD   . GLU   A 1 120 ? 28.716 -16.611 15.557  1.00 35.48 ?  120 GLU   A CD   1 
ATOM   2443 O OE1  . GLU   A 1 120 ? 28.316 -16.065 16.608  1.00 37.29 ?  120 GLU   A OE1  1 
ATOM   2444 O OE2  . GLU   A 1 120 ? 29.201 -17.762 15.528  1.00 38.07 -1 120 GLU   A OE2  1 
ATOM   2445 H H    . GLU   A 1 120 ? 28.495 -13.277 12.754  1.00 17.60 ?  120 GLU   A H    1 
ATOM   2446 H HA   . GLU   A 1 120 ? 26.923 -15.325 12.310  1.00 20.47 ?  120 GLU   A HA   1 
ATOM   2447 H HB2  . GLU   A 1 120 ? 27.687 -14.089 14.713  1.00 26.13 ?  120 GLU   A HB2  1 
ATOM   2448 H HB3  . GLU   A 1 120 ? 26.689 -15.323 14.713  1.00 26.13 ?  120 GLU   A HB3  1 
ATOM   2449 H HG2  . GLU   A 1 120 ? 28.504 -16.486 13.534  1.00 34.73 ?  120 GLU   A HG2  1 
ATOM   2450 H HG3  . GLU   A 1 120 ? 29.421 -15.342 14.149  1.00 34.73 ?  120 GLU   A HG3  1 
ATOM   2451 N N    . VAL   A 1 121 ? 25.385 -12.643 13.099  1.00 14.63 ?  121 VAL   A N    1 
ATOM   2452 C CA   . VAL   A 1 121 ? 24.087 -11.982 13.215  1.00 14.78 ?  121 VAL   A CA   1 
ATOM   2453 C C    . VAL   A 1 121 ? 24.190 -10.602 12.573  1.00 13.74 ?  121 VAL   A C    1 
ATOM   2454 O O    . VAL   A 1 121 ? 25.156 -9.871  12.816  1.00 14.37 ?  121 VAL   A O    1 
ATOM   2455 C CB   . VAL   A 1 121 ? 23.641 -11.844 14.689  1.00 18.08 ?  121 VAL   A CB   1 
ATOM   2456 C CG1  . VAL   A 1 121 ? 22.252 -11.230 14.775  1.00 18.73 ?  121 VAL   A CG1  1 
ATOM   2457 C CG2  . VAL   A 1 121 ? 23.663 -13.183 15.414  1.00 20.58 ?  121 VAL   A CG2  1 
ATOM   2458 H H    . VAL   A 1 121 ? 26.046 -12.096 13.181  1.00 17.54 ?  121 VAL   A H    1 
ATOM   2459 H HA   . VAL   A 1 121 ? 23.417 -12.495 12.742  1.00 17.71 ?  121 VAL   A HA   1 
ATOM   2460 H HB   . VAL   A 1 121 ? 24.250 -11.252 15.152  1.00 21.68 ?  121 VAL   A HB   1 
ATOM   2461 H HG11 . VAL   A 1 121 ? 21.931 -11.295 15.691  1.00 22.46 ?  121 VAL   A HG11 1 
ATOM   2462 H HG12 . VAL   A 1 121 ? 22.298 -10.299 14.510  1.00 22.46 ?  121 VAL   A HG12 1 
ATOM   2463 H HG13 . VAL   A 1 121 ? 21.653 -11.715 14.185  1.00 22.46 ?  121 VAL   A HG13 1 
ATOM   2464 H HG21 . VAL   A 1 121 ? 23.304 -13.066 16.313  1.00 24.67 ?  121 VAL   A HG21 1 
ATOM   2465 H HG22 . VAL   A 1 121 ? 23.115 -13.819 14.927  1.00 24.67 ?  121 VAL   A HG22 1 
ATOM   2466 H HG23 . VAL   A 1 121 ? 24.575 -13.502 15.467  1.00 24.67 ?  121 VAL   A HG23 1 
ATOM   2467 N N    . LEU   A 1 122 ? 23.182 -10.229 11.777  1.00 13.06 ?  122 LEU   A N    1 
ATOM   2468 C CA   . LEU   A 1 122 ? 23.174 -8.928  11.113  1.00 12.85 ?  122 LEU   A CA   1 
ATOM   2469 C C    . LEU   A 1 122 ? 21.777 -8.334  11.076  1.00 12.83 ?  122 LEU   A C    1 
ATOM   2470 O O    . LEU   A 1 122 ? 20.788 -9.053  10.941  1.00 13.99 ?  122 LEU   A O    1 
ATOM   2471 C CB   . LEU   A 1 122 ? 23.609 -9.018  9.645   1.00 14.21 ?  122 LEU   A CB   1 
ATOM   2472 C CG   . LEU   A 1 122 ? 24.816 -9.867  9.286   1.00 14.39 ?  122 LEU   A CG   1 
ATOM   2473 C CD1  . LEU   A 1 122 ? 24.420 -11.320 9.069   1.00 15.14 ?  122 LEU   A CD1  1 
ATOM   2474 C CD2  . LEU   A 1 122 ? 25.492 -9.298  8.044   1.00 13.75 ?  122 LEU   A CD2  1 
ATOM   2475 H H    . LEU   A 1 122 ? 22.486 -10.711 11.610  1.00 15.65 ?  122 LEU   A H    1 
ATOM   2476 H HA   . LEU   A 1 122 ? 23.767 -8.315  11.577  1.00 15.39 ?  122 LEU   A HA   1 
ATOM   2477 H HB2  . LEU   A 1 122 ? 22.871 -9.375  9.136   1.00 17.03 ?  122 LEU   A HB2  1 
ATOM   2478 H HB3  . LEU   A 1 122 ? 23.807 -8.122  9.337   1.00 17.03 ?  122 LEU   A HB3  1 
ATOM   2479 H HG   . LEU   A 1 122 ? 25.470 -9.837  10.006  1.00 17.25 ?  122 LEU   A HG   1 
ATOM   2480 H HD11 . LEU   A 1 122 ? 25.197 -11.828 8.780   1.00 18.14 ?  122 LEU   A HD11 1 
ATOM   2481 H HD12 . LEU   A 1 122 ? 24.085 -11.682 9.904   1.00 18.14 ?  122 LEU   A HD12 1 
ATOM   2482 H HD13 . LEU   A 1 122 ? 23.730 -11.361 8.389   1.00 18.14 ?  122 LEU   A HD13 1 
ATOM   2483 H HD21 . LEU   A 1 122 ? 26.241 -9.870  7.791   1.00 16.47 ?  122 LEU   A HD21 1 
ATOM   2484 H HD22 . LEU   A 1 122 ? 24.850 -9.264  7.319   1.00 16.47 ?  122 LEU   A HD22 1 
ATOM   2485 H HD23 . LEU   A 1 122 ? 25.820 -8.405  8.238   1.00 16.47 ?  122 LEU   A HD23 1 
ATOM   2486 N N    A LEU   A 1 123 ? 21.714 -7.008  11.157  0.66 12.64 ?  123 LEU   A N    1 
ATOM   2487 N N    B LEU   A 1 123 ? 21.726 -7.006  11.206  0.34 12.45 ?  123 LEU   A N    1 
ATOM   2488 C CA   A LEU   A 1 123 ? 20.542 -6.227  10.771  0.66 12.31 ?  123 LEU   A CA   1 
ATOM   2489 C CA   B LEU   A 1 123 ? 20.551 -6.198  10.900  0.34 12.20 ?  123 LEU   A CA   1 
ATOM   2490 C C    A LEU   A 1 123 ? 20.787 -5.708  9.361   0.66 11.51 ?  123 LEU   A C    1 
ATOM   2491 C C    B LEU   A 1 123 ? 20.774 -5.653  9.496   0.34 11.73 ?  123 LEU   A C    1 
ATOM   2492 O O    A LEU   A 1 123 ? 21.879 -5.205  9.077   0.66 11.50 ?  123 LEU   A O    1 
ATOM   2493 O O    B LEU   A 1 123 ? 21.708 -4.876  9.274   0.34 11.73 ?  123 LEU   A O    1 
ATOM   2494 C CB   A LEU   A 1 123 ? 20.381 -5.043  11.724  0.66 13.04 ?  123 LEU   A CB   1 
ATOM   2495 C CB   B LEU   A 1 123 ? 20.424 -5.055  11.906  0.34 12.47 ?  123 LEU   A CB   1 
ATOM   2496 C CG   A LEU   A 1 123 ? 19.329 -3.991  11.374  0.66 13.99 ?  123 LEU   A CG   1 
ATOM   2497 C CG   B LEU   A 1 123 ? 19.396 -3.978  11.546  0.34 13.06 ?  123 LEU   A CG   1 
ATOM   2498 C CD1  A LEU   A 1 123 ? 17.932 -4.590  11.388  0.66 14.92 ?  123 LEU   A CD1  1 
ATOM   2499 C CD1  B LEU   A 1 123 ? 17.995 -4.568  11.517  0.34 13.94 ?  123 LEU   A CD1  1 
ATOM   2500 C CD2  A LEU   A 1 123 ? 19.422 -2.809  12.335  0.66 14.55 ?  123 LEU   A CD2  1 
ATOM   2501 C CD2  B LEU   A 1 123 ? 19.469 -2.792  12.500  0.34 13.55 ?  123 LEU   A CD2  1 
ATOM   2502 H H    A LEU   A 1 123 ? 22.368 -6.518  11.438  0.66 15.15 ?  123 LEU   A H    1 
ATOM   2503 H H    B LEU   A 1 123 ? 22.396 -6.528  11.463  0.34 14.92 ?  123 LEU   A H    1 
ATOM   2504 H HA   A LEU   A 1 123 ? 19.746 -6.780  10.785  0.66 14.75 ?  123 LEU   A HA   1 
ATOM   2505 H HA   B LEU   A 1 123 ? 19.749 -6.738  10.915  0.34 14.61 ?  123 LEU   A HA   1 
ATOM   2506 H HB2  A LEU   A 1 123 ? 20.148 -5.392  12.596  0.66 15.63 ?  123 LEU   A HB2  1 
ATOM   2507 H HB2  B LEU   A 1 123 ? 20.165 -5.427  12.765  0.34 14.94 ?  123 LEU   A HB2  1 
ATOM   2508 H HB3  A LEU   A 1 123 ? 21.229 -4.583  11.776  0.66 15.63 ?  123 LEU   A HB3  1 
ATOM   2509 H HB3  B LEU   A 1 123 ? 21.285 -4.615  11.991  0.34 14.94 ?  123 LEU   A HB3  1 
ATOM   2510 H HG   A LEU   A 1 123 ? 19.493 -3.652  10.479  0.66 16.77 ?  123 LEU   A HG   1 
ATOM   2511 H HG   B LEU   A 1 123 ? 19.585 -3.637  10.658  0.34 15.65 ?  123 LEU   A HG   1 
ATOM   2512 H HD11 A LEU   A 1 123 ? 17.284 -3.895  11.194  0.66 17.87 ?  123 LEU   A HD11 1 
ATOM   2513 H HD11 B LEU   A 1 123 ? 17.355 -3.860  11.349  0.34 16.70 ?  123 LEU   A HD11 1 
ATOM   2514 H HD12 A LEU   A 1 123 ? 17.881 -5.287  10.716  0.66 17.87 ?  123 LEU   A HD12 1 
ATOM   2515 H HD12 B LEU   A 1 123 ? 17.945 -5.233  10.811  0.34 16.70 ?  123 LEU   A HD12 1 
ATOM   2516 H HD13 A LEU   A 1 123 ? 17.760 -4.966  12.267  0.66 17.87 ?  123 LEU   A HD13 1 
ATOM   2517 H HD13 B LEU   A 1 123 ? 17.810 -4.984  12.374  0.34 16.70 ?  123 LEU   A HD13 1 
ATOM   2518 H HD21 A LEU   A 1 123 ? 18.745 -2.155  12.100  0.66 17.44 ?  123 LEU   A HD21 1 
ATOM   2519 H HD21 B LEU   A 1 123 ? 18.804 -2.136  12.237  0.34 16.24 ?  123 LEU   A HD21 1 
ATOM   2520 H HD22 A LEU   A 1 123 ? 19.270 -3.130  13.240  0.66 17.44 ?  123 LEU   A HD22 1 
ATOM   2521 H HD22 B LEU   A 1 123 ? 19.291 -3.103  13.400  0.34 16.24 ?  123 LEU   A HD22 1 
ATOM   2522 H HD23 A LEU   A 1 123 ? 20.304 -2.417  12.266  0.66 17.44 ?  123 LEU   A HD23 1 
ATOM   2523 H HD23 B LEU   A 1 123 ? 20.355 -2.404  12.450  0.34 16.24 ?  123 LEU   A HD23 1 
ATOM   2524 N N    A ALA   A 1 124 ? 19.789 -5.809  8.482   0.66 11.02 ?  124 ALA   A N    1 
ATOM   2525 N N    B ALA   A 1 124 ? 19.933 -6.058  8.548   0.34 11.59 ?  124 ALA   A N    1 
ATOM   2526 C CA   A ALA   A 1 124 ? 20.062 -5.545  7.075   0.66 10.67 ?  124 ALA   A CA   1 
ATOM   2527 C CA   B ALA   A 1 124 ? 20.221 -5.812  7.144   0.34 12.19 ?  124 ALA   A CA   1 
ATOM   2528 C C    A ALA   A 1 124 ? 18.809 -5.091  6.338   0.66 10.70 ?  124 ALA   A C    1 
ATOM   2529 C C    B ALA   A 1 124 ? 18.997 -5.312  6.390   0.34 11.84 ?  124 ALA   A C    1 
ATOM   2530 O O    A ALA   A 1 124 ? 17.682 -5.426  6.733   0.66 11.73 ?  124 ALA   A O    1 
ATOM   2531 O O    B ALA   A 1 124 ? 17.858 -5.630  6.757   0.34 12.30 ?  124 ALA   A O    1 
ATOM   2532 C CB   A ALA   A 1 124 ? 20.642 -6.782  6.383   0.66 11.03 ?  124 ALA   A CB   1 
ATOM   2533 C CB   B ALA   A 1 124 ? 20.753 -7.084  6.465   0.34 13.12 ?  124 ALA   A CB   1 
ATOM   2534 H H    A ALA   A 1 124 ? 18.974 -6.009  8.672   0.66 13.21 ?  124 ALA   A H    1 
ATOM   2535 H H    B ALA   A 1 124 ? 19.199 -6.482  8.690   0.34 13.89 ?  124 ALA   A H    1 
ATOM   2536 H HA   A ALA   A 1 124 ? 20.725 -4.837  7.027   0.66 12.78 ?  124 ALA   A HA   1 
ATOM   2537 H HA   B ALA   A 1 124 ? 20.909 -5.138  7.086   0.34 14.61 ?  124 ALA   A HA   1 
ATOM   2538 H HB1  A ALA   A 1 124 ? 20.816 -6.570  5.453   0.66 13.21 ?  124 ALA   A HB1  1 
ATOM   2539 H HB1  B ALA   A 1 124 ? 20.940 -6.896  5.533   0.34 15.73 ?  124 ALA   A HB1  1 
ATOM   2540 H HB2  A ALA   A 1 124 ? 21.472 -7.032  6.824   0.66 13.21 ?  124 ALA   A HB2  1 
ATOM   2541 H HB2  B ALA   A 1 124 ? 21.570 -7.365  6.914   0.34 15.73 ?  124 ALA   A HB2  1 
ATOM   2542 H HB3  A ALA   A 1 124 ? 20.004 -7.508  6.447   0.66 13.21 ?  124 ALA   A HB3  1 
ATOM   2543 H HB3  B ALA   A 1 124 ? 20.086 -7.786  6.535   0.34 15.73 ?  124 ALA   A HB3  1 
ATOM   2544 N N    A PRO   A 1 125 ? 18.980 -4.357  5.238   0.66 11.27 ?  125 PRO   A N    1 
ATOM   2545 N N    B PRO   A 1 125 ? 19.206 -4.540  5.326   0.34 11.07 ?  125 PRO   A N    1 
ATOM   2546 C CA   A PRO   A 1 125 ? 17.909 -4.153  4.262   0.66 11.98 ?  125 PRO   A CA   1 
ATOM   2547 C CA   B PRO   A 1 125 ? 18.109 -4.138  4.449   0.34 11.56 ?  125 PRO   A CA   1 
ATOM   2548 C C    A PRO   A 1 125 ? 17.985 -5.228  3.181   0.66 11.87 ?  125 PRO   A C    1 
ATOM   2549 C C    B PRO   A 1 125 ? 18.033 -5.122  3.284   0.34 12.50 ?  125 PRO   A C    1 
ATOM   2550 O O    A PRO   A 1 125 ? 18.952 -5.986  3.087   0.66 12.59 ?  125 PRO   A O    1 
ATOM   2551 O O    B PRO   A 1 125 ? 18.919 -5.956  3.091   0.34 12.70 ?  125 PRO   A O    1 
ATOM   2552 C CB   A PRO   A 1 125 ? 18.297 -2.796  3.654   0.66 12.10 ?  125 PRO   A CB   1 
ATOM   2553 C CB   B PRO   A 1 125 ? 18.604 -2.772  3.957   0.34 10.96 ?  125 PRO   A CB   1 
ATOM   2554 C CG   A PRO   A 1 125 ? 19.802 -2.884  3.582   0.66 11.96 ?  125 PRO   A CG   1 
ATOM   2555 C CG   B PRO   A 1 125 ? 20.079 -2.998  3.765   0.34 10.73 ?  125 PRO   A CG   1 
ATOM   2556 C CD   A PRO   A 1 125 ? 20.215 -3.653  4.836   0.66 11.69 ?  125 PRO   A CD   1 
ATOM   2557 C CD   B PRO   A 1 125 ? 20.492 -3.982  4.856   0.34 10.55 ?  125 PRO   A CD   1 
ATOM   2558 H HA   A PRO   A 1 125 ? 17.031 -4.130  4.676   0.66 14.35 ?  125 PRO   A HA   1 
ATOM   2559 H HA   B PRO   A 1 125 ? 17.275 -4.055  4.935   0.34 13.85 ?  125 PRO   A HA   1 
ATOM   2560 H HB2  A PRO   A 1 125 ? 17.901 -2.706  2.772   0.66 14.49 ?  125 PRO   A HB2  1 
ATOM   2561 H HB2  B PRO   A 1 125 ? 18.190 -2.554  3.115   0.34 13.13 ?  125 PRO   A HB2  1 
ATOM   2562 H HB3  A PRO   A 1 125 ? 18.007 -2.080  4.243   0.66 14.49 ?  125 PRO   A HB3  1 
ATOM   2563 H HB3  B PRO   A 1 125 ? 18.431 -2.082  4.628   0.34 13.13 ?  125 PRO   A HB3  1 
ATOM   2564 H HG2  A PRO   A 1 125 ? 20.065 -3.366  2.783   0.66 14.33 ?  125 PRO   A HG2  1 
ATOM   2565 H HG2  B PRO   A 1 125 ? 20.235 -3.373  2.882   0.34 12.85 ?  125 PRO   A HG2  1 
ATOM   2566 H HG3  A PRO   A 1 125 ? 20.180 -1.990  3.584   0.66 14.33 ?  125 PRO   A HG3  1 
ATOM   2567 H HG3  B PRO   A 1 125 ? 20.554 -2.155  3.860   0.34 12.85 ?  125 PRO   A HG3  1 
ATOM   2568 H HD2  A PRO   A 1 125 ? 20.920 -4.283  4.630   0.66 14.01 ?  125 PRO   A HD2  1 
ATOM   2569 H HD2  B PRO   A 1 125 ? 21.063 -4.676  4.479   0.34 12.63 ?  125 PRO   A HD2  1 
ATOM   2570 H HD3  A PRO   A 1 125 ? 20.488 -3.032  5.535   0.66 14.01 ?  125 PRO   A HD3  1 
ATOM   2571 H HD3  B PRO   A 1 125 ? 20.945 -3.509  5.573   0.34 12.63 ?  125 PRO   A HD3  1 
ATOM   2572 N N    A LEU   A 1 126 ? 16.951 -5.261  2.345   0.66 12.08 ?  126 LEU   A N    1 
ATOM   2573 N N    B LEU   A 1 126 ? 16.960 -5.015  2.498   0.34 13.55 ?  126 LEU   A N    1 
ATOM   2574 C CA   A LEU   A 1 126 ? 16.983 -6.069  1.134   0.66 12.38 ?  126 LEU   A CA   1 
ATOM   2575 C CA   B LEU   A 1 126 ? 16.960 -5.707  1.214   0.34 14.22 ?  126 LEU   A CA   1 
ATOM   2576 C C    A LEU   A 1 126 ? 17.907 -5.431  0.105   0.66 12.35 ?  126 LEU   A C    1 
ATOM   2577 C C    B LEU   A 1 126 ? 17.997 -5.062  0.302   0.34 14.08 ?  126 LEU   A C    1 
ATOM   2578 O O    A LEU   A 1 126 ? 17.666 -4.309  -0.365  0.66 12.36 ?  126 LEU   A O    1 
ATOM   2579 O O    B LEU   A 1 126 ? 18.113 -3.837  0.243   0.34 15.24 ?  126 LEU   A O    1 
ATOM   2580 C CB   A LEU   A 1 126 ? 15.581 -6.214  0.557   0.66 12.95 ?  126 LEU   A CB   1 
ATOM   2581 C CB   B LEU   A 1 126 ? 15.585 -5.631  0.549   0.34 15.54 ?  126 LEU   A CB   1 
ATOM   2582 C CG   A LEU   A 1 126 ? 14.679 -7.182  1.316   0.66 14.29 ?  126 LEU   A CG   1 
ATOM   2583 C CG   B LEU   A 1 126 ? 14.511 -6.634  0.975   0.34 16.79 ?  126 LEU   A CG   1 
ATOM   2584 C CD1  A LEU   A 1 126 ? 13.259 -7.063  0.807   0.66 15.14 ?  126 LEU   A CD1  1 
ATOM   2585 C CD1  B LEU   A 1 126 ? 13.257 -6.436  0.138   0.34 16.98 ?  126 LEU   A CD1  1 
ATOM   2586 C CD2  A LEU   A 1 126 ? 15.183 -8.616  1.180   0.66 14.40 ?  126 LEU   A CD2  1 
ATOM   2587 C CD2  B LEU   A 1 126 ? 15.004 -8.064  0.845   0.34 17.62 ?  126 LEU   A CD2  1 
ATOM   2588 H H    A LEU   A 1 126 ? 16.222 -4.819  2.453   0.66 14.48 ?  126 LEU   A H    1 
ATOM   2589 H H    B LEU   A 1 126 ? 16.228 -4.573  2.668   0.34 16.24 ?  126 LEU   A H    1 
ATOM   2590 H HA   A LEU   A 1 126 ? 17.322 -6.953  1.342   0.66 14.83 ?  126 LEU   A HA   1 
ATOM   2591 H HA   B LEU   A 1 126 ? 17.196 -6.639  1.351   0.34 17.04 ?  126 LEU   A HA   1 
ATOM   2592 H HB2  A LEU   A 1 126 ? 15.147 -5.346  0.568   0.66 15.52 ?  126 LEU   A HB2  1 
ATOM   2593 H HB2  B LEU   A 1 126 ? 15.224 -4.746  0.712   0.34 18.62 ?  126 LEU   A HB2  1 
ATOM   2594 H HB3  A LEU   A 1 126 ? 15.647 -6.533  -0.357  0.66 15.52 ?  126 LEU   A HB3  1 
ATOM   2595 H HB3  B LEU   A 1 126 ? 15.713 -5.748  -0.406  0.34 18.62 ?  126 LEU   A HB3  1 
ATOM   2596 H HG   A LEU   A 1 126 ? 14.682 -6.952  2.257   0.66 17.12 ?  126 LEU   A HG   1 
ATOM   2597 H HG   B LEU   A 1 126 ? 14.277 -6.476  1.902   0.34 20.12 ?  126 LEU   A HG   1 
ATOM   2598 H HD11 A LEU   A 1 126 ? 12.695 -7.687  1.294   0.66 18.14 ?  126 LEU   A HD11 1 
ATOM   2599 H HD11 B LEU   A 1 126 ? 12.581 -7.071  0.423   0.34 20.35 ?  126 LEU   A HD11 1 
ATOM   2600 H HD12 A LEU   A 1 126 ? 12.948 -6.157  0.948   0.66 18.14 ?  126 LEU   A HD12 1 
ATOM   2601 H HD12 B LEU   A 1 126 ? 12.933 -5.530  0.261   0.34 20.35 ?  126 LEU   A HD12 1 
ATOM   2602 H HD13 A LEU   A 1 126 ? 13.243 -7.276  -0.140  0.66 18.14 ?  126 LEU   A HD13 1 
ATOM   2603 H HD13 B LEU   A 1 126 ? 13.474 -6.584  -0.797  0.34 20.35 ?  126 LEU   A HD13 1 
ATOM   2604 H HD21 A LEU   A 1 126 ? 14.505 -9.224  1.508   0.66 17.25 ?  126 LEU   A HD21 1 
ATOM   2605 H HD21 B LEU   A 1 126 ? 14.249 -8.666  0.919   0.34 21.12 ?  126 LEU   A HD21 1 
ATOM   2606 H HD22 A LEU   A 1 126 ? 15.369 -8.798  0.245   0.66 17.25 ?  126 LEU   A HD22 1 
ATOM   2607 H HD22 B LEU   A 1 126 ? 15.430 -8.171  -0.021  0.34 21.12 ?  126 LEU   A HD22 1 
ATOM   2608 H HD23 A LEU   A 1 126 ? 15.998 -8.716  1.701   0.66 17.25 ?  126 LEU   A HD23 1 
ATOM   2609 H HD23 B LEU   A 1 126 ? 15.642 -8.241  1.552   0.34 21.12 ?  126 LEU   A HD23 1 
ATOM   2610 N N    A LEU   A 1 127 ? 18.960 -6.164  -0.251  0.66 12.53 ?  127 LEU   A N    1 
ATOM   2611 N N    B LEU   A 1 127 ? 18.771 -5.884  -0.400  0.34 12.92 ?  127 LEU   A N    1 
ATOM   2612 C CA   A LEU   A 1 127 ? 19.949 -5.667  -1.190  0.66 12.37 ?  127 LEU   A CA   1 
ATOM   2613 C CA   B LEU   A 1 127 ? 19.789 -5.374  -1.307  0.34 12.80 ?  127 LEU   A CA   1 
ATOM   2614 C C    A LEU   A 1 127 ? 19.324 -5.462  -2.558  0.66 11.90 ?  127 LEU   A C    1 
ATOM   2615 C C    B LEU   A 1 127 ? 19.270 -5.335  -2.742  0.34 13.29 ?  127 LEU   A C    1 
ATOM   2616 O O    A LEU   A 1 127 ? 18.493 -6.256  -3.015  0.66 12.33 ?  127 LEU   A O    1 
ATOM   2617 O O    B LEU   A 1 127 ? 18.424 -6.137  -3.148  0.34 13.60 ?  127 LEU   A O    1 
ATOM   2618 C CB   A LEU   A 1 127 ? 21.110 -6.656  -1.297  0.66 12.86 ?  127 LEU   A CB   1 
ATOM   2619 C CB   B LEU   A 1 127 ? 21.072 -6.209  -1.241  0.34 12.76 ?  127 LEU   A CB   1 
ATOM   2620 C CG   A LEU   A 1 127 ? 21.918 -6.868  -0.016  0.66 13.04 ?  127 LEU   A CG   1 
ATOM   2621 C CG   B LEU   A 1 127 ? 21.864 -6.186  0.073   0.34 12.69 ?  127 LEU   A CG   1 
ATOM   2622 C CD1  A LEU   A 1 127 ? 23.022 -7.868  -0.268  0.66 13.37 ?  127 LEU   A CD1  1 
ATOM   2623 C CD1  B LEU   A 1 127 ? 23.067 -7.119  0.001   0.34 13.03 ?  127 LEU   A CD1  1 
ATOM   2624 C CD2  A LEU   A 1 127 ? 22.500 -5.559  0.480   0.66 14.02 ?  127 LEU   A CD2  1 
ATOM   2625 C CD2  B LEU   A 1 127 ? 22.306 -4.769  0.423   0.34 13.04 ?  127 LEU   A CD2  1 
ATOM   2626 H H    A LEU   A 1 127 ? 19.115 -6.962  0.036   0.66 15.02 ?  127 LEU   A H    1 
ATOM   2627 H H    B LEU   A 1 127 ? 18.728 -6.742  -0.355  0.34 15.47 ?  127 LEU   A H    1 
ATOM   2628 H HA   A LEU   A 1 127 ? 20.290 -4.820  -0.883  0.66 14.82 ?  127 LEU   A HA   1 
ATOM   2629 H HA   B LEU   A 1 127 ? 20.013 -4.466  -1.043  0.34 15.33 ?  127 LEU   A HA   1 
ATOM   2630 H HB2  A LEU   A 1 127 ? 20.756 -7.521  -1.564  0.66 15.40 ?  127 LEU   A HB2  1 
ATOM   2631 H HB2  B LEU   A 1 127 ? 20.840 -7.132  -1.417  0.34 15.29 ?  127 LEU   A HB2  1 
ATOM   2632 H HB3  A LEU   A 1 127 ? 21.724 -6.337  -1.977  0.66 15.40 ?  127 LEU   A HB3  1 
ATOM   2633 H HB3  B LEU   A 1 127 ? 21.668 -5.890  -1.937  0.34 15.29 ?  127 LEU   A HB3  1 
ATOM   2634 H HG   A LEU   A 1 127 ? 21.334 -7.225  0.675   0.66 15.63 ?  127 LEU   A HG   1 
ATOM   2635 H HG   B LEU   A 1 127 ? 21.292 -6.502  0.788   0.34 15.21 ?  127 LEU   A HG   1 
ATOM   2636 H HD11 A LEU   A 1 127 ? 23.497 -8.029  0.563   0.66 16.02 ?  127 LEU   A HD11 1 
ATOM   2637 H HD11 B LEU   A 1 127 ? 23.545 -7.084  0.844   0.34 15.61 ?  127 LEU   A HD11 1 
ATOM   2638 H HD12 A LEU   A 1 127 ? 22.631 -8.696  -0.590  0.66 16.02 ?  127 LEU   A HD12 1 
ATOM   2639 H HD12 B LEU   A 1 127 ? 22.755 -8.023  -0.165  0.34 15.61 ?  127 LEU   A HD12 1 
ATOM   2640 H HD13 A LEU   A 1 127 ? 23.627 -7.507  -0.932  0.66 16.02 ?  127 LEU   A HD13 1 
ATOM   2641 H HD13 B LEU   A 1 127 ? 23.647 -6.832  -0.721  0.34 15.61 ?  127 LEU   A HD13 1 
ATOM   2642 H HD21 A LEU   A 1 127 ? 23.136 -5.746  1.187   0.66 16.81 ?  127 LEU   A HD21 1 
ATOM   2643 H HD21 B LEU   A 1 127 ? 22.904 -4.804  1.186   0.34 15.63 ?  127 LEU   A HD21 1 
ATOM   2644 H HD22 A LEU   A 1 127 ? 22.949 -5.117  -0.260  0.66 16.81 ?  127 LEU   A HD22 1 
ATOM   2645 H HD22 B LEU   A 1 127 ? 22.764 -4.384  -0.340  0.34 15.63 ?  127 LEU   A HD22 1 
ATOM   2646 H HD23 A LEU   A 1 127 ? 21.784 -5.000  0.814   0.66 16.81 ?  127 LEU   A HD23 1 
ATOM   2647 H HD23 B LEU   A 1 127 ? 21.523 -4.240  0.640   0.34 15.63 ?  127 LEU   A HD23 1 
ATOM   2648 N N    A SER   A 1 128 ? 19.740 -4.383  -3.209  0.66 12.08 ?  128 SER   A N    1 
ATOM   2649 N N    B SER   A 1 128 ? 19.798 -4.378  -3.503  0.34 13.83 ?  128 SER   A N    1 
ATOM   2650 C CA   A SER   A 1 128 ? 19.350 -3.991  -4.551  0.66 12.13 ?  128 SER   A CA   1 
ATOM   2651 C CA   B SER   A 1 128 ? 19.520 -4.115  -4.913  0.34 14.31 ?  128 SER   A CA   1 
ATOM   2652 C C    A SER   A 1 128 ? 17.892 -3.560  -4.647  0.66 12.25 ?  128 SER   A C    1 
ATOM   2653 C C    B SER   A 1 128 ? 18.118 -3.580  -5.187  0.34 15.06 ?  128 SER   A C    1 
ATOM   2654 O O    A SER   A 1 128 ? 17.429 -3.256  -5.747  0.66 13.18 ?  128 SER   A O    1 
ATOM   2655 O O    B SER   A 1 128 ? 17.785 -3.352  -6.357  0.34 14.92 ?  128 SER   A O    1 
ATOM   2656 C CB   A SER   A 1 128 ? 19.690 -5.039  -5.619  0.66 12.16 ?  128 SER   A CB   1 
ATOM   2657 C CB   B SER   A 1 128 ? 19.835 -5.297  -5.841  0.34 13.91 ?  128 SER   A CB   1 
ATOM   2658 O OG   A SER   A 1 128 ? 21.100 -5.212  -5.718  0.66 12.58 ?  128 SER   A OG   1 
ATOM   2659 O OG   B SER   A 1 128 ? 21.228 -5.564  -5.861  0.34 13.69 ?  128 SER   A OG   1 
ATOM   2660 H H    A SER   A 1 128 ? 20.287 -3.821  -2.858  0.66 14.47 ?  128 SER   A H    1 
ATOM   2661 H H    B SER   A 1 128 ? 20.377 -3.830  -3.189  0.34 16.58 ?  128 SER   A H    1 
ATOM   2662 H HA   A SER   A 1 128 ? 19.863 -3.207  -4.769  0.66 14.53 ?  128 SER   A HA   1 
ATOM   2663 H HA   B SER   A 1 128 ? 20.119 -3.408  -5.173  0.34 17.14 ?  128 SER   A HA   1 
ATOM   2664 H HB2  A SER   A 1 128 ? 19.274 -5.879  -5.380  0.66 14.57 ?  128 SER   A HB2  1 
ATOM   2665 H HB2  B SER   A 1 128 ? 19.362 -6.080  -5.531  0.34 16.67 ?  128 SER   A HB2  1 
ATOM   2666 H HB3  A SER   A 1 128 ? 19.349 -4.729  -6.476  0.66 14.57 ?  128 SER   A HB3  1 
ATOM   2667 H HB3  B SER   A 1 128 ? 19.547 -5.067  -6.742  0.34 16.67 ?  128 SER   A HB3  1 
ATOM   2668 H HG   A SER   A 1 128 ? 21.459 -4.474  -5.902  0.66 15.08 ?  128 SER   A HG   1 
ATOM   2669 H HG   B SER   A 1 128 ? 21.644 -4.882  -6.120  0.34 16.40 ?  128 SER   A HG   1 
ATOM   2670 N N    A ALA   A 1 129 ? 17.166 -3.497  -3.532  0.66 12.76 ?  129 ALA   A N    1 
ATOM   2671 N N    B ALA   A 1 129 ? 17.297 -3.349  -4.166  0.34 16.42 ?  129 ALA   A N    1 
ATOM   2672 C CA   A ALA   A 1 129 ? 15.808 -2.976  -3.528  0.66 13.15 ?  129 ALA   A CA   1 
ATOM   2673 C CA   B ALA   A 1 129 ? 15.990 -2.736  -4.366  0.34 18.09 ?  129 ALA   A CA   1 
ATOM   2674 C C    A ALA   A 1 129 ? 15.833 -1.445  -3.524  0.66 12.81 ?  129 ALA   A C    1 
ATOM   2675 C C    B ALA   A 1 129 ? 16.144 -1.215  -4.401  0.34 19.26 ?  129 ALA   A C    1 
ATOM   2676 O O    A ALA   A 1 129 ? 16.890 -0.808  -3.597  0.66 12.86 ?  129 ALA   A O    1 
ATOM   2677 O O    B ALA   A 1 129 ? 17.253 -0.676  -4.410  0.34 19.28 ?  129 ALA   A O    1 
ATOM   2678 C CB   A ALA   A 1 129 ? 15.026 -3.540  -2.338  0.66 14.24 ?  129 ALA   A CB   1 
ATOM   2679 C CB   B ALA   A 1 129 ? 15.012 -3.187  -3.286  0.34 18.63 ?  129 ALA   A CB   1 
ATOM   2680 H H    A ALA   A 1 129 ? 17.435 -3.759  -2.755  0.66 15.29 ?  129 ALA   A H    1 
ATOM   2681 H H    B ALA   A 1 129 ? 17.474 -3.531  -3.345  0.34 19.68 ?  129 ALA   A H    1 
ATOM   2682 H HA   A ALA   A 1 129 ? 15.355 -3.262  -4.331  0.66 15.76 ?  129 ALA   A HA   1 
ATOM   2683 H HA   B ALA   A 1 129 ? 15.639 -3.022  -5.222  0.34 21.68 ?  129 ALA   A HA   1 
ATOM   2684 H HB1  A ALA   A 1 129 ? 14.118 -3.188  -2.354  0.66 17.07 ?  129 ALA   A HB1  1 
ATOM   2685 H HB1  B ALA   A 1 129 ? 14.147 -2.775  -3.453  0.34 22.34 ?  129 ALA   A HB1  1 
ATOM   2686 H HB2  A ALA   A 1 129 ? 15.001 -4.508  -2.398  0.66 17.07 ?  129 ALA   A HB2  1 
ATOM   2687 H HB2  B ALA   A 1 129 ? 14.932 -4.149  -3.321  0.34 22.34 ?  129 ALA   A HB2  1 
ATOM   2688 H HB3  A ALA   A 1 129 ? 15.461 -3.274  -1.510  0.66 17.07 ?  129 ALA   A HB3  1 
ATOM   2689 H HB3  B ALA   A 1 129 ? 15.347 -2.908  -2.421  0.34 22.34 ?  129 ALA   A HB3  1 
ATOM   2690 N N    A GLY   A 1 130 ? 14.648 -0.844  -3.449  0.66 14.02 ?  130 GLY   A N    1 
ATOM   2691 N N    B GLY   A 1 130 ? 15.023 -0.501  -4.419  0.34 20.33 ?  130 GLY   A N    1 
ATOM   2692 C CA   A GLY   A 1 130 ? 14.569 0.605   -3.398  0.66 15.30 ?  130 GLY   A CA   1 
ATOM   2693 C CA   B GLY   A 1 130 ? 15.092 0.948   -4.478  0.34 20.97 ?  130 GLY   A CA   1 
ATOM   2694 C C    A GLY   A 1 130 ? 15.180 1.222   -4.639  0.66 15.39 ?  130 GLY   A C    1 
ATOM   2695 C C    B GLY   A 1 130 ? 15.719 1.396   -5.783  0.34 21.64 ?  130 GLY   A C    1 
ATOM   2696 O O    A GLY   A 1 130 ? 14.927 0.780   -5.766  0.66 14.89 ?  130 GLY   A O    1 
ATOM   2697 O O    B GLY   A 1 130 ? 15.396 0.884   -6.860  0.34 21.39 ?  130 GLY   A O    1 
ATOM   2698 H H    A GLY   A 1 130 ? 13.885 -1.251  -3.429  0.66 16.80 ?  130 GLY   A H    1 
ATOM   2699 H H    B GLY   A 1 130 ? 14.227 -0.821  -4.407  0.34 24.37 ?  130 GLY   A H    1 
ATOM   2700 H HA2  A GLY   A 1 130 ? 13.640 0.878   -3.330  0.66 18.34 ?  130 GLY   A HA2  1 
ATOM   2701 H HA2  B GLY   A 1 130 ? 14.199 1.329   -4.406  0.34 25.14 ?  130 GLY   A HA2  1 
ATOM   2702 H HA3  A GLY   A 1 130 ? 15.047 0.929   -2.621  0.66 18.34 ?  130 GLY   A HA3  1 
ATOM   2703 H HA3  B GLY   A 1 130 ? 15.633 1.286   -3.750  0.34 25.14 ?  130 GLY   A HA3  1 
ATOM   2704 N N    A ILE   A 1 131 ? 16.008 2.251   -4.432  0.66 15.08 ?  131 ILE   A N    1 
ATOM   2705 N N    B ILE   A 1 131 ? 16.652 2.348   -5.689  0.34 22.45 ?  131 ILE   A N    1 
ATOM   2706 C CA   A ILE   A 1 131 ? 16.576 3.011   -5.543  0.66 14.69 ?  131 ILE   A CA   1 
ATOM   2707 C CA   B ILE   A 1 131 ? 17.210 2.965   -6.887  0.34 23.28 ?  131 ILE   A CA   1 
ATOM   2708 C C    A ILE   A 1 131 ? 17.587 2.227   -6.365  0.66 14.04 ?  131 ILE   A C    1 
ATOM   2709 C C    B ILE   A 1 131 ? 17.997 1.972   -7.735  0.34 22.85 ?  131 ILE   A C    1 
ATOM   2710 O O    A ILE   A 1 131 ? 18.019 2.723   -7.415  0.66 14.24 ?  131 ILE   A O    1 
ATOM   2711 O O    B ILE   A 1 131 ? 18.185 2.202   -8.934  0.34 23.22 ?  131 ILE   A O    1 
ATOM   2712 C CB   A ILE   A 1 131 ? 17.164 4.365   -5.088  0.66 16.23 ?  131 ILE   A CB   1 
ATOM   2713 C CB   B ILE   A 1 131 ? 18.024 4.235   -6.539  0.34 24.58 ?  131 ILE   A CB   1 
ATOM   2714 C CG1  A ILE   A 1 131 ? 18.460 4.180   -4.290  0.66 17.21 ?  131 ILE   A CG1  1 
ATOM   2715 C CG1  B ILE   A 1 131 ? 19.392 3.882   -5.951  0.34 25.26 ?  131 ILE   A CG1  1 
ATOM   2716 C CG2  A ILE   A 1 131 ? 16.136 5.142   -4.277  0.66 16.93 ?  131 ILE   A CG2  1 
ATOM   2717 C CG2  B ILE   A 1 131 ? 17.231 5.125   -5.583  0.34 25.00 ?  131 ILE   A CG2  1 
ATOM   2718 C CD1  A ILE   A 1 131 ? 19.094 5.499   -3.850  0.66 18.31 ?  131 ILE   A CD1  1 
ATOM   2719 C CD1  B ILE   A 1 131 ? 20.408 4.995   -6.079  0.34 25.69 ?  131 ILE   A CD1  1 
ATOM   2720 H H    A ILE   A 1 131 ? 16.242 2.532   -3.654  0.66 18.07 ?  131 ILE   A H    1 
ATOM   2721 H H    B ILE   A 1 131 ? 16.974 2.646   -4.948  0.34 26.91 ?  131 ILE   A H    1 
ATOM   2722 H HA   A ILE   A 1 131 ? 15.849 3.222   -6.145  0.66 17.60 ?  131 ILE   A HA   1 
ATOM   2723 H HA   B ILE   A 1 131 ? 16.477 3.263   -7.439  0.34 27.91 ?  131 ILE   A HA   1 
ATOM   2724 H HB   A ILE   A 1 131 ? 17.368 4.882   -5.881  0.66 19.45 ?  131 ILE   A HB   1 
ATOM   2725 H HB   B ILE   A 1 131 ? 18.177 4.744   -7.343  0.34 29.47 ?  131 ILE   A HB   1 
ATOM   2726 H HG12 A ILE   A 1 131 ? 18.268 3.660   -3.496  0.66 20.63 ?  131 ILE   A HG12 1 
ATOM   2727 H HG12 B ILE   A 1 131 ? 19.280 3.688   -5.011  0.34 30.29 ?  131 ILE   A HG12 1 
ATOM   2728 H HG13 A ILE   A 1 131 ? 19.108 3.715   -4.842  0.66 20.63 ?  131 ILE   A HG13 1 
ATOM   2729 H HG13 B ILE   A 1 131 ? 19.760 3.111   -6.404  0.34 30.29 ?  131 ILE   A HG13 1 
ATOM   2730 H HG21 A ILE   A 1 131 ? 16.439 6.057   -4.176  0.66 20.30 ?  131 ILE   A HG21 1 
ATOM   2731 H HG21 B ILE   A 1 131 ? 17.619 6.015   -5.579  0.34 29.98 ?  131 ILE   A HG21 1 
ATOM   2732 H HG22 A ILE   A 1 131 ? 15.287 5.123   -4.744  0.66 20.30 ?  131 ILE   A HG22 1 
ATOM   2733 H HG22 B ILE   A 1 131 ? 16.306 5.166   -5.877  0.34 29.98 ?  131 ILE   A HG22 1 
ATOM   2734 H HG23 A ILE   A 1 131 ? 16.043 4.724   -3.405  0.66 20.30 ?  131 ILE   A HG23 1 
ATOM   2735 H HG23 B ILE   A 1 131 ? 17.271 4.747   -4.694  0.34 29.98 ?  131 ILE   A HG23 1 
ATOM   2736 H HD11 A ILE   A 1 131 ? 19.973 5.318   -3.482  0.66 21.95 ?  131 ILE   A HD11 1 
ATOM   2737 H HD11 B ILE   A 1 131 ? 21.247 4.697   -5.695  0.34 30.81 ?  131 ILE   A HD11 1 
ATOM   2738 H HD12 A ILE   A 1 131 ? 19.172 6.084   -4.620  0.66 21.95 ?  131 ILE   A HD12 1 
ATOM   2739 H HD12 B ILE   A 1 131 ? 20.532 5.204   -7.020  0.34 30.81 ?  131 ILE   A HD12 1 
ATOM   2740 H HD13 A ILE   A 1 131 ? 18.532 5.912   -3.176  0.66 21.95 ?  131 ILE   A HD13 1 
ATOM   2741 H HD13 B ILE   A 1 131 ? 20.084 5.776   -5.607  0.34 30.81 ?  131 ILE   A HD13 1 
ATOM   2742 N N    A PHE   A 1 132 ? 17.975 1.021   -5.931  0.66 13.20 ?  132 PHE   A N    1 
ATOM   2743 N N    B PHE   A 1 132 ? 18.459 0.865   -7.148  0.34 22.25 ?  132 PHE   A N    1 
ATOM   2744 C CA   A PHE   A 1 132 ? 18.836 0.175   -6.753  0.66 13.32 ?  132 PHE   A CA   1 
ATOM   2745 C CA   B PHE   A 1 132 ? 19.205 -0.115  -7.934  0.34 21.58 ?  132 PHE   A CA   1 
ATOM   2746 C C    A PHE   A 1 132 ? 18.067 -0.575  -7.839  0.66 14.16 ?  132 PHE   A C    1 
ATOM   2747 C C    B PHE   A 1 132 ? 18.319 -0.928  -8.867  0.34 21.37 ?  132 PHE   A C    1 
ATOM   2748 O O    A PHE   A 1 132 ? 18.692 -1.197  -8.704  0.66 15.05 ?  132 PHE   A O    1 
ATOM   2749 O O    B PHE   A 1 132 ? 18.844 -1.732  -9.645  0.34 21.13 ?  132 PHE   A O    1 
ATOM   2750 C CB   A PHE   A 1 132 ? 19.634 -0.804  -5.883  0.66 12.74 ?  132 PHE   A CB   1 
ATOM   2751 C CB   B PHE   A 1 132 ? 20.049 -1.024  -7.031  0.34 21.52 ?  132 PHE   A CB   1 
ATOM   2752 C CG   A PHE   A 1 132 ? 20.852 -0.199  -5.212  0.66 12.24 ?  132 PHE   A CG   1 
ATOM   2753 C CG   B PHE   A 1 132 ? 21.364 -0.412  -6.611  0.34 22.12 ?  132 PHE   A CG   1 
ATOM   2754 C CD1  A PHE   A 1 132 ? 20.722 0.811   -4.274  0.66 13.26 ?  132 PHE   A CD1  1 
ATOM   2755 C CD1  B PHE   A 1 132 ? 21.675 0.899   -6.946  0.34 22.53 ?  132 PHE   A CD1  1 
ATOM   2756 C CD2  A PHE   A 1 132 ? 22.122 -0.684  -5.488  0.66 12.90 ?  132 PHE   A CD2  1 
ATOM   2757 C CD2  B PHE   A 1 132 ? 22.292 -1.151  -5.896  0.34 22.13 ?  132 PHE   A CD2  1 
ATOM   2758 C CE1  A PHE   A 1 132 ? 21.842 1.346   -3.649  0.66 13.59 ?  132 PHE   A CE1  1 
ATOM   2759 C CE1  B PHE   A 1 132 ? 22.874 1.461   -6.574  0.34 22.59 ?  132 PHE   A CE1  1 
ATOM   2760 C CE2  A PHE   A 1 132 ? 23.241 -0.159  -4.862  0.66 13.26 ?  132 PHE   A CE2  1 
ATOM   2761 C CE2  B PHE   A 1 132 ? 23.498 -0.590  -5.519  0.34 22.22 ?  132 PHE   A CE2  1 
ATOM   2762 C CZ   A PHE   A 1 132 ? 23.098 0.861   -3.944  0.66 13.09 ?  132 PHE   A CZ   1 
ATOM   2763 C CZ   B PHE   A 1 132 ? 23.788 0.718   -5.859  0.34 22.30 ?  132 PHE   A CZ   1 
ATOM   2764 H H    A PHE   A 1 132 ? 17.756 0.675   -5.170  0.66 15.82 ?  132 PHE   A H    1 
ATOM   2765 H H    B PHE   A 1 132 ? 18.348 0.662   -6.319  0.34 26.67 ?  132 PHE   A H    1 
ATOM   2766 H HA   A PHE   A 1 132 ? 19.477 0.747   -7.195  0.66 15.97 ?  132 PHE   A HA   1 
ATOM   2767 H HA   B PHE   A 1 132 ? 19.809 0.370   -8.515  0.34 25.87 ?  132 PHE   A HA   1 
ATOM   2768 H HB2  A PHE   A 1 132 ? 19.053 -1.144  -5.183  0.66 15.26 ?  132 PHE   A HB2  1 
ATOM   2769 H HB2  B PHE   A 1 132 ? 19.548 -1.226  -6.225  0.34 25.80 ?  132 PHE   A HB2  1 
ATOM   2770 H HB3  A PHE   A 1 132 ? 19.939 -1.540  -6.439  0.66 15.26 ?  132 PHE   A HB3  1 
ATOM   2771 H HB3  B PHE   A 1 132 ? 20.244 -1.845  -7.511  0.34 25.80 ?  132 PHE   A HB3  1 
ATOM   2772 H HD1  A PHE   A 1 132 ? 19.880 1.143   -4.065  0.66 15.89 ?  132 PHE   A HD1  1 
ATOM   2773 H HD1  B PHE   A 1 132 ? 21.063 1.407   -7.430  0.34 27.01 ?  132 PHE   A HD1  1 
ATOM   2774 H HD2  A PHE   A 1 132 ? 22.225 -1.366  -6.111  0.66 15.46 ?  132 PHE   A HD2  1 
ATOM   2775 H HD2  B PHE   A 1 132 ? 22.102 -2.032  -5.665  0.34 26.53 ?  132 PHE   A HD2  1 
ATOM   2776 H HE1  A PHE   A 1 132 ? 21.745 2.031   -3.026  0.66 16.28 ?  132 PHE   A HE1  1 
ATOM   2777 H HE1  B PHE   A 1 132 ? 23.063 2.341   -6.807  0.34 27.08 ?  132 PHE   A HE1  1 
ATOM   2778 H HE2  A PHE   A 1 132 ? 24.085 -0.480  -5.074  0.66 15.88 ?  132 PHE   A HE2  1 
ATOM   2779 H HE2  B PHE   A 1 132 ? 24.114 -1.092  -5.037  0.34 26.64 ?  132 PHE   A HE2  1 
ATOM   2780 H HZ   A PHE   A 1 132 ? 23.846 1.224   -3.529  0.66 15.69 ?  132 PHE   A HZ   1 
ATOM   2781 H HZ   B PHE   A 1 132 ? 24.598 1.097   -5.607  0.34 26.74 ?  132 PHE   A HZ   1 
ATOM   2782 N N    A GLY   A 1 133 ? 16.735 -0.550  -7.808  0.66 14.27 ?  133 GLY   A N    1 
ATOM   2783 N N    B GLY   A 1 133 ? 17.002 -0.743  -8.809  0.34 21.50 ?  133 GLY   A N    1 
ATOM   2784 C CA   A GLY   A 1 133 ? 15.927 -0.922  -8.952  0.66 15.29 ?  133 GLY   A CA   1 
ATOM   2785 C CA   B GLY   A 1 133 ? 16.112 -1.172  -9.862  0.34 21.56 ?  133 GLY   A CA   1 
ATOM   2786 C C    A GLY   A 1 133 ? 15.588 -2.389  -9.118  0.66 15.60 ?  133 GLY   A C    1 
ATOM   2787 C C    B GLY   A 1 133 ? 15.549 -2.571  -9.723  0.34 21.71 ?  133 GLY   A C    1 
ATOM   2788 O O    A GLY   A 1 133 ? 14.934 -2.731  -10.110 0.66 17.67 ?  133 GLY   A O    1 
ATOM   2789 O O    B GLY   A 1 133 ? 14.494 -2.853  -10.303 0.34 22.36 ?  133 GLY   A O    1 
ATOM   2790 H H    A GLY   A 1 133 ? 16.269 -0.310  -7.125  0.66 17.10 ?  133 GLY   A H    1 
ATOM   2791 H H    B GLY   A 1 133 ? 16.605 -0.363  -8.150  0.34 25.78 ?  133 GLY   A H    1 
ATOM   2792 H HA2  A GLY   A 1 133 ? 15.086 -0.437  -8.909  0.66 18.32 ?  133 GLY   A HA2  1 
ATOM   2793 H HA2  B GLY   A 1 133 ? 15.370 -0.551  -9.907  0.34 25.85 ?  133 GLY   A HA2  1 
ATOM   2794 H HA3  A GLY   A 1 133 ? 16.383 -0.645  -9.760  0.66 18.32 ?  133 GLY   A HA3  1 
ATOM   2795 H HA3  B GLY   A 1 133 ? 16.589 -1.125  -10.707 0.34 25.85 ?  133 GLY   A HA3  1 
ATOM   2796 N N    A ALA   A 1 134 ? 15.994 -3.269  -8.202  0.66 14.27 ?  134 ALA   A N    1 
ATOM   2797 N N    B ALA   A 1 134 ? 16.209 -3.455  -8.980  0.34 21.14 ?  134 ALA   A N    1 
ATOM   2798 C CA   A ALA   A 1 134 ? 15.655 -4.679  -8.343  0.66 14.70 ?  134 ALA   A CA   1 
ATOM   2799 C CA   B ALA   A 1 134 ? 15.791 -4.849  -8.950  0.34 20.55 ?  134 ALA   A CA   1 
ATOM   2800 C C    A ALA   A 1 134 ? 14.304 -4.990  -7.701  0.66 15.14 ?  134 ALA   A C    1 
ATOM   2801 C C    B ALA   A 1 134 ? 14.485 -5.019  -8.174  0.34 20.43 ?  134 ALA   A C    1 
ATOM   2802 O O    A ALA   A 1 134 ? 13.763 -4.211  -6.911  0.66 16.42 ?  134 ALA   A O    1 
ATOM   2803 O O    B ALA   A 1 134 ? 14.099 -4.183  -7.352  0.34 20.84 ?  134 ALA   A O    1 
ATOM   2804 C CB   A ALA   A 1 134 ? 16.735 -5.573  -7.733  0.66 15.12 ?  134 ALA   A CB   1 
ATOM   2805 C CB   B ALA   A 1 134 ? 16.884 -5.724  -8.337  0.34 20.25 ?  134 ALA   A CB   1 
ATOM   2806 H H    A ALA   A 1 134 ? 16.460 -3.073  -7.503  0.66 17.11 ?  134 ALA   A H    1 
ATOM   2807 H H    B ALA   A 1 134 ? 16.896 -3.274  -8.494  0.34 25.34 ?  134 ALA   A H    1 
ATOM   2808 H HA   A ALA   A 1 134 ? 15.587 -4.887  -9.286  0.66 17.61 ?  134 ALA   A HA   1 
ATOM   2809 H HA   B ALA   A 1 134 ? 15.638 -5.150  -9.857  0.34 24.64 ?  134 ALA   A HA   1 
ATOM   2810 H HB1  A ALA   A 1 134 ? 16.483 -6.499  -7.870  0.66 18.12 ?  134 ALA   A HB1  1 
ATOM   2811 H HB1  B ALA   A 1 134 ? 16.586 -6.647  -8.342  0.34 24.27 ?  134 ALA   A HB1  1 
ATOM   2812 H HB2  A ALA   A 1 134 ? 17.576 -5.387  -8.174  0.66 18.12 ?  134 ALA   A HB2  1 
ATOM   2813 H HB2  B ALA   A 1 134 ? 17.691 -5.634  -8.867  0.34 24.27 ?  134 ALA   A HB2  1 
ATOM   2814 H HB3  A ALA   A 1 134 ? 16.803 -5.382  -6.786  0.66 18.12 ?  134 ALA   A HB3  1 
ATOM   2815 H HB3  B ALA   A 1 134 ? 17.049 -5.434  -7.428  0.34 24.27 ?  134 ALA   A HB3  1 
ATOM   2816 N N    A ASP   A 1 135 ? 13.768 -6.157  -8.059  0.66 16.43 ?  135 ASP   A N    1 
ATOM   2817 N N    B ASP   A 1 135 ? 13.805 -6.129  -8.450  0.34 20.27 ?  135 ASP   A N    1 
ATOM   2818 C CA   A ASP   A 1 135 ? 12.513 -6.659  -7.505  0.66 17.53 ?  135 ASP   A CA   1 
ATOM   2819 C CA   B ASP   A 1 135 ? 12.525 -6.420  -7.817  0.34 20.16 ?  135 ASP   A CA   1 
ATOM   2820 C C    A ASP   A 1 135 ? 12.740 -7.100  -6.064  0.66 16.84 ?  135 ASP   A C    1 
ATOM   2821 C C    B ASP   A 1 135 ? 12.757 -6.924  -6.397  0.34 19.20 ?  135 ASP   A C    1 
ATOM   2822 O O    A ASP   A 1 135 ? 13.528 -8.025  -5.829  0.66 15.95 ?  135 ASP   A O    1 
ATOM   2823 O O    B ASP   A 1 135 ? 13.460 -7.925  -6.213  0.34 18.85 ?  135 ASP   A O    1 
ATOM   2824 C CB   A ASP   A 1 135 ? 12.060 -7.848  -8.351  0.66 19.79 ?  135 ASP   A CB   1 
ATOM   2825 C CB   B ASP   A 1 135 ? 11.782 -7.481  -8.618  0.34 21.25 ?  135 ASP   A CB   1 
ATOM   2826 C CG   A ASP   A 1 135 ? 10.789 -8.505  -7.831  0.66 22.21 ?  135 ASP   A CG   1 
ATOM   2827 C CG   B ASP   A 1 135 ? 10.390 -7.758  -8.077  0.34 22.24 ?  135 ASP   A CG   1 
ATOM   2828 O OD1  A ASP   A 1 135 ? 10.181 -7.988  -6.870  0.66 22.30 ?  135 ASP   A OD1  1 
ATOM   2829 O OD1  B ASP   A 1 135 ? 10.017 -7.171  -7.038  0.34 22.89 ?  135 ASP   A OD1  1 
ATOM   2830 O OD2  A ASP   A 1 135 ? 10.404 -9.552  -8.393  0.66 24.83 -1 135 ASP   A OD2  1 
ATOM   2831 O OD2  B ASP   A 1 135 ? 9.664  -8.564  -8.694  0.34 22.50 -1 135 ASP   A OD2  1 
ATOM   2832 H H    A ASP   A 1 135 ? 14.122 -6.688  -8.633  0.66 19.69 ?  135 ASP   A H    1 
ATOM   2833 H H    B ASP   A 1 135 ? 14.061 -6.730  -9.004  0.34 24.30 ?  135 ASP   A H    1 
ATOM   2834 H HA   A ASP   A 1 135 ? 11.831 -5.970  -7.544  0.66 21.02 ?  135 ASP   A HA   1 
ATOM   2835 H HA   B ASP   A 1 135 ? 11.984 -5.616  -7.803  0.34 24.17 ?  135 ASP   A HA   1 
ATOM   2836 H HB2  A ASP   A 1 135 ? 11.901 -7.546  -9.261  0.66 23.72 ?  135 ASP   A HB2  1 
ATOM   2837 H HB2  B ASP   A 1 135 ? 11.705 -7.182  -9.539  0.34 25.47 ?  135 ASP   A HB2  1 
ATOM   2838 H HB3  A ASP   A 1 135 ? 12.757 -8.523  -8.347  0.66 23.72 ?  135 ASP   A HB3  1 
ATOM   2839 H HB3  B ASP   A 1 135 ? 12.280 -8.312  -8.582  0.34 25.47 ?  135 ASP   A HB3  1 
ATOM   2840 N N    A PRO   A 1 136 ? 12.096 -6.475  -5.076  0.66 17.03 ?  136 PRO   A N    1 
ATOM   2841 N N    B PRO   A 1 136 ? 12.197 -6.272  -5.374  0.34 18.94 ?  136 PRO   A N    1 
ATOM   2842 C CA   A PRO   A 1 136 ? 12.352 -6.865  -3.677  0.66 16.95 ?  136 PRO   A CA   1 
ATOM   2843 C CA   B PRO   A 1 136 ? 12.389 -6.762  -3.998  0.34 18.92 ?  136 PRO   A CA   1 
ATOM   2844 C C    A PRO   A 1 136 ? 11.933 -8.286  -3.339  0.66 15.32 ?  136 PRO   A C    1 
ATOM   2845 C C    B PRO   A 1 136 ? 11.965 -8.208  -3.786  0.34 18.56 ?  136 PRO   A C    1 
ATOM   2846 O O    A PRO   A 1 136 ? 12.530 -8.898  -2.445  0.66 14.54 ?  136 PRO   A O    1 
ATOM   2847 O O    B PRO   A 1 136 ? 12.571 -8.900  -2.959  0.34 18.31 ?  136 PRO   A O    1 
ATOM   2848 C CB   A PRO   A 1 136 ? 11.563 -5.823  -2.871  0.66 18.39 ?  136 PRO   A CB   1 
ATOM   2849 C CB   B PRO   A 1 136 ? 11.564 -5.778  -3.152  0.34 19.33 ?  136 PRO   A CB   1 
ATOM   2850 C CG   A PRO   A 1 136 ? 10.507 -5.336  -3.812  0.66 19.41 ?  136 PRO   A CG   1 
ATOM   2851 C CG   B PRO   A 1 136 ? 10.685 -5.043  -4.135  0.34 19.60 ?  136 PRO   A CG   1 
ATOM   2852 C CD   A PRO   A 1 136 ? 11.119 -5.378  -5.179  0.66 18.40 ?  136 PRO   A CD   1 
ATOM   2853 C CD   B PRO   A 1 136 ? 11.445 -5.007  -5.408  0.34 19.27 ?  136 PRO   A CD   1 
ATOM   2854 H HA   A PRO   A 1 136 ? 13.297 -6.767  -3.474  0.66 20.31 ?  136 PRO   A HA   1 
ATOM   2855 H HA   B PRO   A 1 136 ? 13.321 -6.680  -3.742  0.34 22.68 ?  136 PRO   A HA   1 
ATOM   2856 H HB2  A PRO   A 1 136 ? 11.164 -6.243  -2.094  0.66 22.05 ?  136 PRO   A HB2  1 
ATOM   2857 H HB2  B PRO   A 1 136 ? 11.027 -6.266  -2.509  0.34 23.17 ?  136 PRO   A HB2  1 
ATOM   2858 H HB3  A PRO   A 1 136 ? 12.154 -5.099  -2.608  0.66 22.05 ?  136 PRO   A HB3  1 
ATOM   2859 H HB3  B PRO   A 1 136 ? 12.159 -5.157  -2.699  0.34 23.17 ?  136 PRO   A HB3  1 
ATOM   2860 H HG2  A PRO   A 1 136 ? 9.738  -5.921  -3.767  0.66 23.27 ?  136 PRO   A HG2  1 
ATOM   2861 H HG2  B PRO   A 1 136 ? 9.852  -5.528  -4.254  0.34 23.49 ?  136 PRO   A HG2  1 
ATOM   2862 H HG3  A PRO   A 1 136 ? 10.265 -4.427  -3.582  0.66 23.27 ?  136 PRO   A HG3  1 
ATOM   2863 H HG3  B PRO   A 1 136 ? 10.514 -4.144  -3.819  0.34 23.49 ?  136 PRO   A HG3  1 
ATOM   2864 H HD2  A PRO   A 1 136 ? 10.444 -5.594  -5.846  0.66 22.05 ?  136 PRO   A HD2  1 
ATOM   2865 H HD2  B PRO   A 1 136 ? 10.835 -4.992  -6.162  0.34 23.10 ?  136 PRO   A HD2  1 
ATOM   2866 H HD3  A PRO   A 1 136 ? 11.569 -4.545  -5.385  0.66 22.05 ?  136 PRO   A HD3  1 
ATOM   2867 H HD3  B PRO   A 1 136 ? 12.057 -4.253  -5.427  0.34 23.10 ?  136 PRO   A HD3  1 
ATOM   2868 N N    A ILE   A 1 137 ? 10.900 -8.818  -3.996  0.66 15.64 ?  137 ILE   A N    1 
ATOM   2869 N N    B ILE   A 1 137 ? 10.943 -8.686  -4.501  0.34 18.57 ?  137 ILE   A N    1 
ATOM   2870 C CA   A ILE   A 1 137 ? 10.535 -10.218 -3.789  0.66 15.90 ?  137 ILE   A CA   1 
ATOM   2871 C CA   B ILE   A 1 137 ? 10.531 -10.082 -4.369  0.34 18.83 ?  137 ILE   A CA   1 
ATOM   2872 C C    A ILE   A 1 137 ? 11.689 -11.126 -4.202  0.66 15.51 ?  137 ILE   A C    1 
ATOM   2873 C C    B ILE   A 1 137 ? 11.702 -11.014 -4.658  0.34 18.73 ?  137 ILE   A C    1 
ATOM   2874 O O    A ILE   A 1 137 ? 12.029 -12.094 -3.506  0.66 15.52 ?  137 ILE   A O    1 
ATOM   2875 O O    B ILE   A 1 137 ? 11.913 -12.011 -3.956  0.34 18.95 ?  137 ILE   A O    1 
ATOM   2876 C CB   A ILE   A 1 137 ? 9.239  -10.545 -4.557  0.66 17.08 ?  137 ILE   A CB   1 
ATOM   2877 C CB   B ILE   A 1 137 ? 9.326  -10.370 -5.284  0.34 19.15 ?  137 ILE   A CB   1 
ATOM   2878 C CG1  A ILE   A 1 137 ? 8.070  -9.685  -4.051  0.66 18.62 ?  137 ILE   A CG1  1 
ATOM   2879 C CG1  B ILE   A 1 137 ? 8.087  -9.624  -4.779  0.34 19.72 ?  137 ILE   A CG1  1 
ATOM   2880 C CG2  A ILE   A 1 137 ? 8.905  -12.031 -4.445  0.66 17.60 ?  137 ILE   A CG2  1 
ATOM   2881 C CG2  B ILE   A 1 137 ? 9.066  -11.870 -5.374  0.34 19.15 ?  137 ILE   A CG2  1 
ATOM   2882 C CD1  A ILE   A 1 137 ? 6.776  -9.895  -4.813  0.66 19.88 ?  137 ILE   A CD1  1 
ATOM   2883 C CD1  B ILE   A 1 137 ? 6.899  -9.694  -5.718  0.34 20.09 ?  137 ILE   A CD1  1 
ATOM   2884 H H    A ILE   A 1 137 ? 10.408 -8.396  -4.561  0.66 18.74 ?  137 ILE   A H    1 
ATOM   2885 H H    B ILE   A 1 137 ? 10.480 -8.227  -5.059  0.34 22.26 ?  137 ILE   A H    1 
ATOM   2886 H HA   A ILE   A 1 137 ? 10.365 -10.363 -2.849  0.66 19.05 ?  137 ILE   A HA   1 
ATOM   2887 H HA   B ILE   A 1 137 ? 10.250 -10.241 -3.455  0.34 22.57 ?  137 ILE   A HA   1 
ATOM   2888 H HB   A ILE   A 1 137 ? 9.374  -10.335 -5.492  0.66 20.48 ?  137 ILE   A HB   1 
ATOM   2889 H HB   B ILE   A 1 137 ? 9.535  -10.045 -6.172  0.34 22.96 ?  137 ILE   A HB   1 
ATOM   2890 H HG12 A ILE   A 1 137 ? 7.903  -9.892  -3.118  0.66 22.32 ?  137 ILE   A HG12 1 
ATOM   2891 H HG12 B ILE   A 1 137 ? 7.817  -10.007 -3.930  0.34 23.64 ?  137 ILE   A HG12 1 
ATOM   2892 H HG13 A ILE   A 1 137 ? 8.311  -8.744  -4.136  0.66 22.32 ?  137 ILE   A HG13 1 
ATOM   2893 H HG13 B ILE   A 1 137 ? 8.315  -8.689  -4.659  0.34 23.64 ?  137 ILE   A HG13 1 
ATOM   2894 H HG21 A ILE   A 1 137 ? 8.156  -12.235 -5.025  0.66 21.09 ?  137 ILE   A HG21 1 
ATOM   2895 H HG21 B ILE   A 1 137 ? 8.182  -12.019 -5.745  0.34 22.96 ?  137 ILE   A HG21 1 
ATOM   2896 H HG22 A ILE   A 1 137 ? 9.668  -12.555 -4.720  0.66 21.09 ?  137 ILE   A HG22 1 
ATOM   2897 H HG22 B ILE   A 1 137 ? 9.733  -12.273 -5.953  0.34 22.96 ?  137 ILE   A HG22 1 
ATOM   2898 H HG23 A ILE   A 1 137 ? 8.676  -12.230 -3.526  0.66 21.09 ?  137 ILE   A HG23 1 
ATOM   2899 H HG23 B ILE   A 1 137 ? 9.120  -12.254 -4.487  0.34 22.96 ?  137 ILE   A HG23 1 
ATOM   2900 H HD11 A ILE   A 1 137 ? 6.061  -9.509  -4.294  0.66 23.83 ?  137 ILE   A HD11 1 
ATOM   2901 H HD11 B ILE   A 1 137 ? 6.505  -8.812  -5.795  0.34 24.09 ?  137 ILE   A HD11 1 
ATOM   2902 H HD12 A ILE   A 1 137 ? 6.839  -9.459  -5.678  0.66 23.83 ?  137 ILE   A HD12 1 
ATOM   2903 H HD12 B ILE   A 1 137 ? 7.203  -9.997  -6.587  0.34 24.09 ?  137 ILE   A HD12 1 
ATOM   2904 H HD13 A ILE   A 1 137 ? 6.608  -10.843 -4.931  0.66 23.83 ?  137 ILE   A HD13 1 
ATOM   2905 H HD13 B ILE   A 1 137 ? 6.250  -10.319 -5.358  0.34 24.09 ?  137 ILE   A HD13 1 
ATOM   2906 N N    A HIS   A 1 138 ? 12.293 -10.835 -5.353  0.66 15.81 ?  138 HIS   A N    1 
ATOM   2907 N N    B HIS   A 1 138 ? 12.475 -10.712 -5.701  0.34 18.54 ?  138 HIS   A N    1 
ATOM   2908 C CA   A HIS   A 1 138 ? 13.457 -11.591 -5.797  0.66 15.93 ?  138 HIS   A CA   1 
ATOM   2909 C CA   B HIS   A 1 138 ? 13.635 -11.539 -6.016  0.34 17.85 ?  138 HIS   A CA   1 
ATOM   2910 C C    A HIS   A 1 138 ? 14.612 -11.443 -4.813  0.66 15.42 ?  138 HIS   A C    1 
ATOM   2911 C C    B HIS   A 1 138 ? 14.720 -11.407 -4.950  0.34 16.36 ?  138 HIS   A C    1 
ATOM   2912 O O    A HIS   A 1 138 ? 15.262 -12.429 -4.443  0.66 15.91 ?  138 HIS   A O    1 
ATOM   2913 O O    B HIS   A 1 138 ? 15.410 -12.385 -4.637  0.34 16.27 ?  138 HIS   A O    1 
ATOM   2914 C CB   A HIS   A 1 138 ? 13.861 -11.129 -7.197  0.66 16.41 ?  138 HIS   A CB   1 
ATOM   2915 C CB   B HIS   A 1 138 ? 14.175 -11.174 -7.400  0.34 18.68 ?  138 HIS   A CB   1 
ATOM   2916 C CG   A HIS   A 1 138 ? 15.151 -11.720 -7.671  0.66 17.56 ?  138 HIS   A CG   1 
ATOM   2917 C CG   B HIS   A 1 138 ? 15.371 -11.974 -7.812  0.34 19.20 ?  138 HIS   A CG   1 
ATOM   2918 N ND1  A HIS   A 1 138 ? 15.302 -13.065 -7.931  0.66 18.62 ?  138 HIS   A ND1  1 
ATOM   2919 N ND1  B HIS   A 1 138 ? 15.298 -13.311 -8.140  0.34 19.70 ?  138 HIS   A ND1  1 
ATOM   2920 C CD2  A HIS   A 1 138 ? 16.357 -11.153 -7.913  0.66 17.53 ?  138 HIS   A CD2  1 
ATOM   2921 C CD2  B HIS   A 1 138 ? 16.672 -11.624 -7.948  0.34 19.37 ?  138 HIS   A CD2  1 
ATOM   2922 C CE1  A HIS   A 1 138 ? 16.541 -13.299 -8.325  0.66 18.63 ?  138 HIS   A CE1  1 
ATOM   2923 C CE1  B HIS   A 1 138 ? 16.502 -13.750 -8.461  0.34 19.72 ?  138 HIS   A CE1  1 
ATOM   2924 N NE2  A HIS   A 1 138 ? 17.203 -12.156 -8.320  0.66 18.04 ?  138 HIS   A NE2  1 
ATOM   2925 N NE2  B HIS   A 1 138 ? 17.354 -12.746 -8.352  0.34 19.36 ?  138 HIS   A NE2  1 
ATOM   2926 H H    A HIS   A 1 138 ? 12.049 -10.205 -5.892  0.66 18.95 ?  138 HIS   A H    1 
ATOM   2927 H H    B HIS   A 1 138 ? 12.342 -10.053 -6.239  0.34 22.22 ?  138 HIS   A H    1 
ATOM   2928 H HA   A HIS   A 1 138 ? 13.222 -12.527 -5.851  0.66 19.10 ?  138 HIS   A HA   1 
ATOM   2929 H HA   B HIS   A 1 138 ? 13.355 -12.466 -6.046  0.34 21.40 ?  138 HIS   A HA   1 
ATOM   2930 H HB2  A HIS   A 1 138 ? 13.166 -11.385 -7.828  0.66 19.67 ?  138 HIS   A HB2  1 
ATOM   2931 H HB2  B HIS   A 1 138 ? 13.477 -11.325 -8.060  0.34 22.39 ?  138 HIS   A HB2  1 
ATOM   2932 H HB3  A HIS   A 1 138 ? 13.960 -10.163 -7.196  0.66 19.67 ?  138 HIS   A HB3  1 
ATOM   2933 H HB3  B HIS   A 1 138 ? 14.430 -10.239 -7.402  0.34 22.39 ?  138 HIS   A HB3  1 
ATOM   2934 H HD1  A HIS   A 1 138 ? 14.681 -13.658 -7.858  0.66 22.32 ?  138 HIS   A HD1  1 
ATOM   2935 H HD1  B HIS   A 1 138 ? 14.580 -13.786 -8.138  0.34 23.61 ?  138 HIS   A HD1  1 
ATOM   2936 H HD2  A HIS   A 1 138 ? 16.568 -10.252 -7.824  0.66 21.01 ?  138 HIS   A HD2  1 
ATOM   2937 H HD2  B HIS   A 1 138 ? 17.035 -10.784 -7.795  0.34 23.22 ?  138 HIS   A HD2  1 
ATOM   2938 H HE1  A HIS   A 1 138 ? 16.887 -14.128 -8.561  0.66 22.33 ?  138 HIS   A HE1  1 
ATOM   2939 H HE1  B HIS   A 1 138 ? 16.714 -14.618 -8.719  0.34 23.64 ?  138 HIS   A HE1  1 
ATOM   2940 N N    . SER   A 1 139 ? 14.881 -10.213 -4.375  1.00 15.26 ?  139 SER   A N    1 
ATOM   2941 C CA   . SER   A 1 139 ? 15.949 -10.006 -3.404  1.00 15.01 ?  139 SER   A CA   1 
ATOM   2942 C C    . SER   A 1 139 ? 15.735 -10.842 -2.147  1.00 14.46 ?  139 SER   A C    1 
ATOM   2943 O O    . SER   A 1 139 ? 16.688 -11.423 -1.612  1.00 14.51 ?  139 SER   A O    1 
ATOM   2944 C CB   . SER   A 1 139 ? 16.070 -8.523  -3.060  1.00 14.59 ?  139 SER   A CB   1 
ATOM   2945 O OG   . SER   A 1 139 ? 17.156 -8.345  -2.172  1.00 15.02 ?  139 SER   A OG   1 
ATOM   2946 H H    A SER   A 1 139 ? 14.468 -9.498  -4.616  0.66 18.28 ?  139 SER   A H    1 
ATOM   2947 H H    B SER   A 1 139 ? 14.397 -9.519  -4.531  0.34 18.28 ?  139 SER   A H    1 
ATOM   2948 H HA   . SER   A 1 139 ? 16.791 -10.282 -3.799  1.00 17.99 ?  139 SER   A HA   1 
ATOM   2949 H HB2  . SER   A 1 139 ? 16.232 -8.011  -3.867  1.00 17.49 ?  139 SER   A HB2  1 
ATOM   2950 H HB3  . SER   A 1 139 ? 15.256 -8.222  -2.626  1.00 17.49 ?  139 SER   A HB3  1 
ATOM   2951 H HG   . SER   A 1 139 ? 17.242 -7.528  -1.969  1.00 18.00 ?  139 SER   A HG   1 
ATOM   2952 N N    . LEU   A 1 140 ? 14.496 -10.908 -1.656  1.00 14.64 ?  140 LEU   A N    1 
ATOM   2953 C CA   . LEU   A 1 140 ? 14.223 -11.726 -0.478  1.00 14.42 ?  140 LEU   A CA   1 
ATOM   2954 C C    . LEU   A 1 140 ? 14.499 -13.201 -0.755  1.00 14.50 ?  140 LEU   A C    1 
ATOM   2955 O O    . LEU   A 1 140 ? 15.057 -13.910 0.094   1.00 15.00 ?  140 LEU   A O    1 
ATOM   2956 C CB   . LEU   A 1 140 ? 12.779 -11.518 -0.024  1.00 14.47 ?  140 LEU   A CB   1 
ATOM   2957 C CG   . LEU   A 1 140 ? 12.328 -12.370 1.161   1.00 15.34 ?  140 LEU   A CG   1 
ATOM   2958 C CD1  . LEU   A 1 140 ? 13.226 -12.167 2.369   1.00 16.03 ?  140 LEU   A CD1  1 
ATOM   2959 C CD2  . LEU   A 1 140 ? 10.867 -12.064 1.515   1.00 16.47 ?  140 LEU   A CD2  1 
ATOM   2960 H H    . LEU   A 1 140 ? 13.814 -10.482 -1.970  1.00 17.54 ?  140 LEU   A H    1 
ATOM   2961 H HA   . LEU   A 1 140 ? 14.800 -11.445 0.245   1.00 17.27 ?  140 LEU   A HA   1 
ATOM   2962 H HB2  . LEU   A 1 140 ? 12.664 -10.593 0.234   1.00 17.34 ?  140 LEU   A HB2  1 
ATOM   2963 H HB3  . LEU   A 1 140 ? 12.188 -11.724 -0.766  1.00 17.34 ?  140 LEU   A HB3  1 
ATOM   2964 H HG   . LEU   A 1 140 ? 12.367 -13.311 0.910   1.00 18.38 ?  140 LEU   A HG   1 
ATOM   2965 H HD11 . LEU   A 1 140 ? 12.841 -12.636 3.128   1.00 19.21 ?  140 LEU   A HD11 1 
ATOM   2966 H HD12 . LEU   A 1 140 ? 14.102 -12.531 2.169   1.00 19.21 ?  140 LEU   A HD12 1 
ATOM   2967 H HD13 . LEU   A 1 140 ? 13.287 -11.223 2.557   1.00 19.21 ?  140 LEU   A HD13 1 
ATOM   2968 H HD21 . LEU   A 1 140 ? 10.597 -12.622 2.268   1.00 19.74 ?  140 LEU   A HD21 1 
ATOM   2969 H HD22 . LEU   A 1 140 ? 10.786 -11.130 1.754   1.00 19.74 ?  140 LEU   A HD22 1 
ATOM   2970 H HD23 . LEU   A 1 140 ? 10.302 -12.262 0.749   1.00 19.74 ?  140 LEU   A HD23 1 
ATOM   2971 N N    . ARG   A 1 141 ? 14.106 -13.681 -1.938  1.00 15.26 ?  141 ARG   A N    1 
ATOM   2972 C CA   . ARG   A 1 141 ? 14.349 -15.073 -2.302  1.00 16.36 ?  141 ARG   A CA   1 
ATOM   2973 C C    . ARG   A 1 141 ? 15.844 -15.376 -2.307  1.00 15.24 ?  141 ARG   A C    1 
ATOM   2974 O O    . ARG   A 1 141 ? 16.291 -16.385 -1.747  1.00 15.15 ?  141 ARG   A O    1 
ATOM   2975 C CB   . ARG   A 1 141 ? 13.736 -15.335 -3.681  1.00 18.58 ?  141 ARG   A CB   1 
ATOM   2976 C CG   . ARG   A 1 141 ? 13.779 -16.775 -4.148  1.00 22.16 ?  141 ARG   A CG   1 
ATOM   2977 C CD   . ARG   A 1 141 ? 12.744 -17.595 -3.433  1.00 24.71 ?  141 ARG   A CD   1 
ATOM   2978 N NE   . ARG   A 1 141 ? 13.333 -18.398 -2.373  1.00 25.40 ?  141 ARG   A NE   1 
ATOM   2979 C CZ   . ARG   A 1 141 ? 12.634 -18.957 -1.393  1.00 26.27 ?  141 ARG   A CZ   1 
ATOM   2980 N NH1  . ARG   A 1 141 ? 11.341 -18.722 -1.245  1.00 26.41 ?  141 ARG   A NH1  1 
ATOM   2981 N NH2  . ARG   A 1 141 ? 13.252 -19.758 -0.530  1.00 26.72 ?  141 ARG   A NH2  1 
ATOM   2982 H H    . ARG   A 1 141 ? 13.699 -13.222 -2.544  1.00 18.29 ?  141 ARG   A H    1 
ATOM   2983 H HA   . ARG   A 1 141 ? 13.921 -15.656 -1.659  1.00 19.61 ?  141 ARG   A HA   1 
ATOM   2984 H HB2  . ARG   A 1 141 ? 12.808 -15.056 -3.665  1.00 22.27 ?  141 ARG   A HB2  1 
ATOM   2985 H HB3  . ARG   A 1 141 ? 14.219 -14.806 -4.335  1.00 22.27 ?  141 ARG   A HB3  1 
ATOM   2986 H HG2  . ARG   A 1 141 ? 13.593 -16.811 -5.101  1.00 26.57 ?  141 ARG   A HG2  1 
ATOM   2987 H HG3  . ARG   A 1 141 ? 14.653 -17.154 -3.963  1.00 26.57 ?  141 ARG   A HG3  1 
ATOM   2988 H HD2  . ARG   A 1 141 ? 12.089 -17.005 -3.028  1.00 29.63 ?  141 ARG   A HD2  1 
ATOM   2989 H HD3  . ARG   A 1 141 ? 12.308 -18.186 -4.069  1.00 29.63 ?  141 ARG   A HD3  1 
ATOM   2990 H HE   . ARG   A 1 141 ? 14.158 -18.621 -2.450  1.00 30.46 ?  141 ARG   A HE   1 
ATOM   2991 H HH11 . ARG   A 1 141 ? 10.922 -18.218 -1.803  1.00 31.67 ?  141 ARG   A HH11 1 
ATOM   2992 H HH12 . ARG   A 1 141 ? 10.906 -19.093 -0.599  1.00 31.67 ?  141 ARG   A HH12 1 
ATOM   2993 H HH21 . ARG   A 1 141 ? 14.093 -19.915 -0.615  1.00 32.04 ?  141 ARG   A HH21 1 
ATOM   2994 H HH22 . ARG   A 1 141 ? 12.812 -20.116 0.118   1.00 32.04 ?  141 ARG   A HH22 1 
ATOM   2995 N N    . VAL   A 1 142 ? 16.639 -14.505 -2.933  1.00 14.25 ?  142 VAL   A N    1 
ATOM   2996 C CA   . VAL   A 1 142 ? 18.084 -14.717 -2.962  1.00 14.26 ?  142 VAL   A CA   1 
ATOM   2997 C C    . VAL   A 1 142 ? 18.655 -14.694 -1.551  1.00 13.48 ?  142 VAL   A C    1 
ATOM   2998 O O    . VAL   A 1 142 ? 19.523 -15.503 -1.201  1.00 13.73 ?  142 VAL   A O    1 
ATOM   2999 C CB   . VAL   A 1 142 ? 18.777 -13.696 -3.883  1.00 14.41 ?  142 VAL   A CB   1 
ATOM   3000 C CG1  . VAL   A 1 142 ? 20.289 -13.920 -3.864  1.00 14.34 ?  142 VAL   A CG1  1 
ATOM   3001 C CG2  . VAL   A 1 142 ? 18.266 -13.818 -5.305  1.00 15.67 ?  142 VAL   A CG2  1 
ATOM   3002 H H    . VAL   A 1 142 ? 16.372 -13.790 -3.342  1.00 17.08 ?  142 VAL   A H    1 
ATOM   3003 H HA   . VAL   A 1 142 ? 18.258 -15.591 -3.329  1.00 17.09 ?  142 VAL   A HA   1 
ATOM   3004 H HB   . VAL   A 1 142 ? 18.606 -12.790 -3.569  1.00 17.26 ?  142 VAL   A HB   1 
ATOM   3005 H HG11 . VAL   A 1 142 ? 20.692 -13.433 -4.599  1.00 17.19 ?  142 VAL   A HG11 1 
ATOM   3006 H HG12 . VAL   A 1 142 ? 20.650 -13.602 -3.021  1.00 17.19 ?  142 VAL   A HG12 1 
ATOM   3007 H HG13 . VAL   A 1 142 ? 20.465 -14.870 -3.962  1.00 17.19 ?  142 VAL   A HG13 1 
ATOM   3008 H HG21 . VAL   A 1 142 ? 18.697 -13.143 -5.855  1.00 18.78 ?  142 VAL   A HG21 1 
ATOM   3009 H HG22 . VAL   A 1 142 ? 18.481 -14.701 -5.637  1.00 18.78 ?  142 VAL   A HG22 1 
ATOM   3010 H HG23 . VAL   A 1 142 ? 17.309 -13.683 -5.306  1.00 18.78 ?  142 VAL   A HG23 1 
ATOM   3011 N N    . CYS   A 1 143 ? 18.192 -13.759 -0.722  1.00 13.33 ?  143 CYS   A N    1 
ATOM   3012 C CA   . CYS   A 1 143 ? 18.655 -13.700 0.659   1.00 13.34 ?  143 CYS   A CA   1 
ATOM   3013 C C    . CYS   A 1 143 ? 18.424 -15.031 1.364   1.00 13.58 ?  143 CYS   A C    1 
ATOM   3014 O O    . CYS   A 1 143 ? 19.343 -15.608 1.953   1.00 13.26 ?  143 CYS   A O    1 
ATOM   3015 C CB   . CYS   A 1 143 ? 17.923 -12.578 1.392   1.00 14.01 ?  143 CYS   A CB   1 
ATOM   3016 S SG   . CYS   A 1 143 ? 18.400 -12.387 3.116   1.00 14.35 ?  143 CYS   A SG   1 
ATOM   3017 H H    . CYS   A 1 143 ? 17.612 -13.159 -0.931  1.00 15.97 ?  143 CYS   A H    1 
ATOM   3018 H HA   . CYS   A 1 143 ? 19.605 -13.513 0.672   1.00 15.98 ?  143 CYS   A HA   1 
ATOM   3019 H HB2  . CYS   A 1 143 ? 18.104 -11.740 0.941   1.00 16.79 ?  143 CYS   A HB2  1 
ATOM   3020 H HB3  . CYS   A 1 143 ? 16.973 -12.760 1.368   1.00 16.79 ?  143 CYS   A HB3  1 
ATOM   3021 H HG   . CYS   A 1 143 ? 17.809 -11.451 3.580   1.00 17.20 ?  143 CYS   A HG   1 
ATOM   3022 N N    . VAL   A 1 144 ? 17.193 -15.537 1.306   1.00 14.15 ?  144 VAL   A N    1 
ATOM   3023 C CA   . VAL   A 1 144 ? 16.850 -16.770 2.007   1.00 15.45 ?  144 VAL   A CA   1 
ATOM   3024 C C    . VAL   A 1 144 ? 17.672 -17.941 1.492   1.00 14.97 ?  144 VAL   A C    1 
ATOM   3025 O O    . VAL   A 1 144 ? 18.046 -18.836 2.259   1.00 16.11 ?  144 VAL   A O    1 
ATOM   3026 C CB   . VAL   A 1 144 ? 15.336 -17.019 1.873   1.00 18.07 ?  144 VAL   A CB   1 
ATOM   3027 C CG1  . VAL   A 1 144 ? 14.971 -18.454 2.213   1.00 19.68 ?  144 VAL   A CG1  1 
ATOM   3028 C CG2  . VAL   A 1 144 ? 14.573 -16.021 2.743   1.00 18.32 ?  144 VAL   A CG2  1 
ATOM   3029 H H    . VAL   A 1 144 ? 16.537 -15.181 0.867   1.00 16.95 ?  144 VAL   A H    1 
ATOM   3030 H HA   . VAL   A 1 144 ? 17.041 -16.658 2.945   1.00 18.52 ?  144 VAL   A HA   1 
ATOM   3031 H HB   . VAL   A 1 144 ? 15.067 -16.859 0.951   1.00 21.66 ?  144 VAL   A HB   1 
ATOM   3032 H HG11 . VAL   A 1 144 ? 14.013 -18.508 2.384   1.00 23.59 ?  144 VAL   A HG11 1 
ATOM   3033 H HG12 . VAL   A 1 144 ? 15.200 -19.029 1.467   1.00 23.59 ?  144 VAL   A HG12 1 
ATOM   3034 H HG13 . VAL   A 1 144 ? 15.458 -18.725 3.006   1.00 23.59 ?  144 VAL   A HG13 1 
ATOM   3035 H HG21 . VAL   A 1 144 ? 13.617 -16.186 2.663   1.00 21.96 ?  144 VAL   A HG21 1 
ATOM   3036 H HG22 . VAL   A 1 144 ? 14.847 -16.127 3.667   1.00 21.96 ?  144 VAL   A HG22 1 
ATOM   3037 H HG23 . VAL   A 1 144 ? 14.771 -15.117 2.442   1.00 21.96 ?  144 VAL   A HG23 1 
ATOM   3038 N N    . ASP   A 1 145 ? 17.941 -17.971 0.191   1.00 15.19 ?  145 ASP   A N    1 
ATOM   3039 C CA   . ASP   A 1 145 ? 18.651 -19.079 -0.436  1.00 16.19 ?  145 ASP   A CA   1 
ATOM   3040 C C    . ASP   A 1 145 ? 20.170 -18.932 -0.386  1.00 15.67 ?  145 ASP   A C    1 
ATOM   3041 O O    . ASP   A 1 145 ? 20.874 -19.832 -0.856  1.00 17.55 ?  145 ASP   A O    1 
ATOM   3042 C CB   . ASP   A 1 145 ? 18.211 -19.225 -1.896  1.00 17.87 ?  145 ASP   A CB   1 
ATOM   3043 C CG   . ASP   A 1 145 ? 16.765 -19.675 -2.033  1.00 20.25 ?  145 ASP   A CG   1 
ATOM   3044 O OD1  . ASP   A 1 145 ? 16.193 -20.206 -1.056  1.00 20.89 ?  145 ASP   A OD1  1 
ATOM   3045 O OD2  . ASP   A 1 145 ? 16.200 -19.491 -3.129  1.00 21.80 -1 145 ASP   A OD2  1 
ATOM   3046 H H    . ASP   A 1 145 ? 17.699 -17.359 -0.365  1.00 18.20 ?  145 ASP   A H    1 
ATOM   3047 H HA   . ASP   A 1 145 ? 18.419 -19.900 0.022   1.00 19.40 ?  145 ASP   A HA   1 
ATOM   3048 H HB2  . ASP   A 1 145 ? 18.310 -18.370 -2.345  1.00 21.42 ?  145 ASP   A HB2  1 
ATOM   3049 H HB3  . ASP   A 1 145 ? 18.767 -19.892 -2.329  1.00 21.42 ?  145 ASP   A HB3  1 
ATOM   3050 N N    . THR   A 1 146 ? 20.693 -17.835 0.164   1.00 13.81 ?  146 THR   A N    1 
ATOM   3051 C CA   . THR   A 1 146 ? 22.131 -17.574 0.182   1.00 13.17 ?  146 THR   A CA   1 
ATOM   3052 C C    . THR   A 1 146 ? 22.682 -17.396 1.585   1.00 13.16 ?  146 THR   A C    1 
ATOM   3053 O O    . THR   A 1 146 ? 23.759 -17.926 1.898   1.00 14.02 ?  146 THR   A O    1 
ATOM   3054 C CB   . THR   A 1 146 ? 22.447 -16.320 -0.654  1.00 13.22 ?  146 THR   A CB   1 
ATOM   3055 O OG1  . THR   A 1 146 ? 21.936 -16.491 -1.978  1.00 13.86 ?  146 THR   A OG1  1 
ATOM   3056 C CG2  . THR   A 1 146 ? 23.947 -16.075 -0.730  1.00 13.72 ?  146 THR   A CG2  1 
ATOM   3057 H H    . THR   A 1 146 ? 20.225 -17.214 0.535   1.00 16.55 ?  146 THR   A H    1 
ATOM   3058 H HA   . THR   A 1 146 ? 22.594 -18.316 -0.223  1.00 15.78 ?  146 THR   A HA   1 
ATOM   3059 H HB   . THR   A 1 146 ? 22.034 -15.541 -0.250  1.00 15.84 ?  146 THR   A HB   1 
ATOM   3060 H HG1  . THR   A 1 146 ? 21.102 -16.581 -1.953  1.00 16.61 ?  146 THR   A HG1  1 
ATOM   3061 H HG21 . THR   A 1 146 ? 24.142 -15.410 -1.410  1.00 16.44 ?  146 THR   A HG21 1 
ATOM   3062 H HG22 . THR   A 1 146 ? 24.276 -15.751 0.125   1.00 16.44 ?  146 THR   A HG22 1 
ATOM   3063 H HG23 . THR   A 1 146 ? 24.407 -16.897 -0.954  1.00 16.44 ?  146 THR   A HG23 1 
ATOM   3064 N N    . VAL   A 1 147 ? 22.004 -16.615 2.421   1.00 12.97 ?  147 VAL   A N    1 
ATOM   3065 C CA   . VAL   A 1 147 ? 22.495 -16.316 3.759   1.00 12.85 ?  147 VAL   A CA   1 
ATOM   3066 C C    . VAL   A 1 147 ? 22.174 -17.486 4.679   1.00 13.51 ?  147 VAL   A C    1 
ATOM   3067 O O    . VAL   A 1 147 ? 21.028 -17.960 4.735   1.00 14.14 ?  147 VAL   A O    1 
ATOM   3068 C CB   . VAL   A 1 147 ? 21.880 -15.009 4.280   1.00 13.23 ?  147 VAL   A CB   1 
ATOM   3069 C CG1  . VAL   A 1 147 ? 22.416 -14.697 5.660   1.00 14.43 ?  147 VAL   A CG1  1 
ATOM   3070 C CG2  . VAL   A 1 147 ? 22.144 -13.862 3.315   1.00 13.57 ?  147 VAL   A CG2  1 
ATOM   3071 H H    . VAL   A 1 147 ? 21.248 -16.245 2.240   1.00 15.54 ?  147 VAL   A H    1 
ATOM   3072 H HA   . VAL   A 1 147 ? 23.460 -16.207 3.727   1.00 15.40 ?  147 VAL   A HA   1 
ATOM   3073 H HB   . VAL   A 1 147 ? 20.923 -15.125 4.358   1.00 15.85 ?  147 VAL   A HB   1 
ATOM   3074 H HG11 . VAL   A 1 147 ? 22.170 -13.795 5.897   1.00 17.29 ?  147 VAL   A HG11 1 
ATOM   3075 H HG12 . VAL   A 1 147 ? 22.029 -15.324 6.299   1.00 17.29 ?  147 VAL   A HG12 1 
ATOM   3076 H HG13 . VAL   A 1 147 ? 23.381 -14.792 5.654   1.00 17.29 ?  147 VAL   A HG13 1 
ATOM   3077 H HG21 . VAL   A 1 147 ? 21.816 -13.039 3.711   1.00 16.26 ?  147 VAL   A HG21 1 
ATOM   3078 H HG22 . VAL   A 1 147 ? 23.096 -13.798 3.154   1.00 16.26 ?  147 VAL   A HG22 1 
ATOM   3079 H HG23 . VAL   A 1 147 ? 21.675 -14.039 2.485   1.00 16.26 ?  147 VAL   A HG23 1 
ATOM   3080 N N    . ARG   A 1 148 ? 23.194 -17.947 5.404   1.00 13.85 ?  148 ARG   A N    1 
ATOM   3081 C CA   . ARG   A 1 148 ? 23.062 -19.027 6.368   1.00 13.83 ?  148 ARG   A CA   1 
ATOM   3082 C C    . ARG   A 1 148 ? 23.187 -18.558 7.806   1.00 13.99 ?  148 ARG   A C    1 
ATOM   3083 O O    . ARG   A 1 148 ? 22.779 -19.284 8.721   1.00 15.60 ?  148 ARG   A O    1 
ATOM   3084 C CB   . ARG   A 1 148 ? 24.108 -20.117 6.095   1.00 14.44 ?  148 ARG   A CB   1 
ATOM   3085 C CG   . ARG   A 1 148 ? 23.944 -20.764 4.734   1.00 16.01 ?  148 ARG   A CG   1 
ATOM   3086 C CD   . ARG   A 1 148 ? 25.034 -21.791 4.443   1.00 16.71 ?  148 ARG   A CD   1 
ATOM   3087 N NE   . ARG   A 1 148 ? 26.374 -21.209 4.460   1.00 16.63 ?  148 ARG   A NE   1 
ATOM   3088 C CZ   . ARG   A 1 148 ? 26.883 -20.477 3.478   1.00 15.69 ?  148 ARG   A CZ   1 
ATOM   3089 N NH1  . ARG   A 1 148 ? 26.209 -20.253 2.360   1.00 15.99 ?  148 ARG   A NH1  1 
ATOM   3090 N NH2  . ARG   A 1 148 ? 28.100 -19.948 3.622   1.00 16.23 ?  148 ARG   A NH2  1 
ATOM   3091 H H    . ARG   A 1 148 ? 24.001 -17.638 5.341   1.00 16.60 ?  148 ARG   A H    1 
ATOM   3092 H HA   . ARG   A 1 148 ? 22.190 -19.424 6.267   1.00 16.57 ?  148 ARG   A HA   1 
ATOM   3093 H HB2  . ARG   A 1 148 ? 24.995 -19.731 6.135   1.00 17.31 ?  148 ARG   A HB2  1 
ATOM   3094 H HB3  . ARG   A 1 148 ? 24.019 -20.815 6.765   1.00 17.31 ?  148 ARG   A HB3  1 
ATOM   3095 H HG2  . ARG   A 1 148 ? 23.083 -21.212 4.702   1.00 19.18 ?  148 ARG   A HG2  1 
ATOM   3096 H HG3  . ARG   A 1 148 ? 23.984 -20.073 4.054   1.00 19.18 ?  148 ARG   A HG3  1 
ATOM   3097 H HD2  . ARG   A 1 148 ? 25.000 -22.484 5.118   1.00 20.02 ?  148 ARG   A HD2  1 
ATOM   3098 H HD3  . ARG   A 1 148 ? 24.880 -22.170 3.564   1.00 20.02 ?  148 ARG   A HD3  1 
ATOM   3099 H HE   . ARG   A 1 148 ? 26.856 -21.338 5.156   1.00 19.93 ?  148 ARG   A HE   1 
ATOM   3100 H HH11 . ARG   A 1 148 ? 25.422 -20.582 2.255   1.00 19.16 ?  148 ARG   A HH11 1 
ATOM   3101 H HH12 . ARG   A 1 148 ? 26.558 -19.773 1.736   1.00 19.16 ?  148 ARG   A HH12 1 
ATOM   3102 H HH21 . ARG   A 1 148 ? 28.540 -20.078 4.346   1.00 19.45 ?  148 ARG   A HH21 1 
ATOM   3103 H HH22 . ARG   A 1 148 ? 28.438 -19.467 2.992   1.00 19.45 ?  148 ARG   A HH22 1 
ATOM   3104 N N    . THR   A 1 149 ? 23.741 -17.367 8.018   1.00 14.39 ?  149 THR   A N    1 
ATOM   3105 C CA   . THR   A 1 149 ? 23.818 -16.769 9.335   1.00 14.39 ?  149 THR   A CA   1 
ATOM   3106 C C    . THR   A 1 149 ? 22.491 -16.077 9.643   1.00 14.03 ?  149 THR   A C    1 
ATOM   3107 O O    . THR   A 1 149 ? 21.557 -16.077 8.830   1.00 14.80 ?  149 THR   A O    1 
ATOM   3108 C CB   . THR   A 1 149 ? 25.014 -15.827 9.391   1.00 14.57 ?  149 THR   A CB   1 
ATOM   3109 O OG1  . THR   A 1 149 ? 24.884 -14.896 8.314   1.00 14.51 ?  149 THR   A OG1  1 
ATOM   3110 C CG2  . THR   A 1 149 ? 26.325 -16.620 9.273   1.00 14.82 ?  149 THR   A CG2  1 
ATOM   3111 H H    . THR   A 1 149 ? 24.095 -16.875 7.399   1.00 17.24 ?  149 THR   A H    1 
ATOM   3112 H HA   . THR   A 1 149 ? 23.948 -17.471 9.990   1.00 17.24 ?  149 THR   A HA   1 
ATOM   3113 H HB   . THR   A 1 149 ? 25.007 -15.354 10.236  1.00 17.46 ?  149 THR   A HB   1 
ATOM   3114 H HG1  . THR   A 1 149 ? 25.536 -14.364 8.317   1.00 17.39 ?  149 THR   A HG1  1 
ATOM   3115 H HG21 . THR   A 1 149 ? 27.083 -16.018 9.329   1.00 17.77 ?  149 THR   A HG21 1 
ATOM   3116 H HG22 . THR   A 1 149 ? 26.389 -17.273 9.989   1.00 17.77 ?  149 THR   A HG22 1 
ATOM   3117 H HG23 . THR   A 1 149 ? 26.359 -17.088 8.422   1.00 17.77 ?  149 THR   A HG23 1 
ATOM   3118 N N    . ASN   A 1 150 ? 22.369 -15.533 10.847  1.00 14.41 ?  150 ASN   A N    1 
ATOM   3119 C CA   . ASN   A 1 150 ? 21.083 -15.024 11.326  1.00 14.96 ?  150 ASN   A CA   1 
ATOM   3120 C C    . ASN   A 1 150 ? 20.897 -13.587 10.858  1.00 14.05 ?  150 ASN   A C    1 
ATOM   3121 O O    . ASN   A 1 150 ? 21.638 -12.687 11.271  1.00 15.29 ?  150 ASN   A O    1 
ATOM   3122 C CB   . ASN   A 1 150 ? 21.009 -15.130 12.843  1.00 17.68 ?  150 ASN   A CB   1 
ATOM   3123 C CG   . ASN   A 1 150 ? 20.909 -16.560 13.312  1.00 21.64 ?  150 ASN   A CG   1 
ATOM   3124 O OD1  . ASN   A 1 150 ? 20.304 -17.396 12.644  1.00 22.82 ?  150 ASN   A OD1  1 
ATOM   3125 N ND2  . ASN   A 1 150 ? 21.519 -16.858 14.454  1.00 24.17 ?  150 ASN   A ND2  1 
ATOM   3126 H H    . ASN   A 1 150 ? 23.012 -15.446 11.409  1.00 17.26 ?  150 ASN   A H    1 
ATOM   3127 H HA   . ASN   A 1 150 ? 20.366 -15.563 10.950  1.00 17.93 ?  150 ASN   A HA   1 
ATOM   3128 H HB2  . ASN   A 1 150 ? 21.807 -14.745 13.230  1.00 21.19 ?  150 ASN   A HB2  1 
ATOM   3129 H HB3  . ASN   A 1 150 ? 20.220 -14.659 13.158  1.00 21.19 ?  150 ASN   A HB3  1 
ATOM   3130 H HD21 . ASN   A 1 150 ? 21.494 -17.662 14.766  1.00 28.98 ?  150 ASN   A HD21 1 
ATOM   3131 H HD22 . ASN   A 1 150 ? 21.938 -16.246 14.890  1.00 28.98 ?  150 ASN   A HD22 1 
ATOM   3132 N N    . VAL   A 1 151 ? 19.910 -13.365 9.997   1.00 13.90 ?  151 VAL   A N    1 
ATOM   3133 C CA   . VAL   A 1 151 ? 19.696 -12.058 9.396   1.00 14.00 ?  151 VAL   A CA   1 
ATOM   3134 C C    . VAL   A 1 151 ? 18.312 -11.541 9.764   1.00 13.92 ?  151 VAL   A C    1 
ATOM   3135 O O    . VAL   A 1 151 ? 17.305 -12.250 9.620   1.00 15.28 ?  151 VAL   A O    1 
ATOM   3136 C CB   . VAL   A 1 151 ? 19.968 -12.060 7.878   1.00 15.04 ?  151 VAL   A CB   1 
ATOM   3137 C CG1  . VAL   A 1 151 ? 19.143 -13.098 7.156   1.00 16.14 ?  151 VAL   A CG1  1 
ATOM   3138 C CG2  . VAL   A 1 151 ? 19.761 -10.661 7.285   1.00 15.13 ?  151 VAL   A CG2  1 
ATOM   3139 H H    . VAL   A 1 151 ? 19.349 -13.964 9.742   1.00 16.65 ?  151 VAL   A H    1 
ATOM   3140 H HA   . VAL   A 1 151 ? 20.342 -11.444 9.783   1.00 16.77 ?  151 VAL   A HA   1 
ATOM   3141 H HB   . VAL   A 1 151 ? 20.901 -12.292 7.736   1.00 18.03 ?  151 VAL   A HB   1 
ATOM   3142 H HG11 . VAL   A 1 151 ? 19.322 -13.052 6.205   1.00 19.35 ?  151 VAL   A HG11 1 
ATOM   3143 H HG12 . VAL   A 1 151 ? 19.383 -13.985 7.488   1.00 19.35 ?  151 VAL   A HG12 1 
ATOM   3144 H HG13 . VAL   A 1 151 ? 18.201 -12.936 7.324   1.00 19.35 ?  151 VAL   A HG13 1 
ATOM   3145 H HG21 . VAL   A 1 151 ? 20.068 -10.664 6.363   1.00 18.13 ?  151 VAL   A HG21 1 
ATOM   3146 H HG22 . VAL   A 1 151 ? 18.817 -10.442 7.316   1.00 18.13 ?  151 VAL   A HG22 1 
ATOM   3147 H HG23 . VAL   A 1 151 ? 20.272 -10.022 7.801   1.00 18.13 ?  151 VAL   A HG23 1 
ATOM   3148 N N    . TYR   A 1 152 ? 18.296 -10.298 10.248  1.00 13.81 ?  152 TYR   A N    1 
ATOM   3149 C CA   . TYR   A 1 152 ? 17.099 -9.567  10.636  1.00 13.63 ?  152 TYR   A CA   1 
ATOM   3150 C C    . TYR   A 1 152 ? 16.896 -8.463  9.610   1.00 12.87 ?  152 TYR   A C    1 
ATOM   3151 O O    . TYR   A 1 152 ? 17.674 -7.500  9.558   1.00 13.47 ?  152 TYR   A O    1 
ATOM   3152 C CB   . TYR   A 1 152 ? 17.278 -9.025  12.050  1.00 14.48 ?  152 TYR   A CB   1 
ATOM   3153 C CG   . TYR   A 1 152 ? 17.240 -10.144 13.055  1.00 15.51 ?  152 TYR   A CG   1 
ATOM   3154 C CD1  . TYR   A 1 152 ? 18.373 -10.894 13.346  1.00 16.97 ?  152 TYR   A CD1  1 
ATOM   3155 C CD2  . TYR   A 1 152 ? 16.057 -10.488 13.685  1.00 15.88 ?  152 TYR   A CD2  1 
ATOM   3156 C CE1  . TYR   A 1 152 ? 18.337 -11.941 14.247  1.00 18.50 ?  152 TYR   A CE1  1 
ATOM   3157 C CE2  . TYR   A 1 152 ? 16.005 -11.544 14.594  1.00 17.29 ?  152 TYR   A CE2  1 
ATOM   3158 C CZ   . TYR   A 1 152 ? 17.153 -12.262 14.868  1.00 18.59 ?  152 TYR   A CZ   1 
ATOM   3159 O OH   . TYR   A 1 152 ? 17.121 -13.312 15.766  1.00 21.18 ?  152 TYR   A OH   1 
ATOM   3160 H H    . TYR   A 1 152 ? 19.016 -9.825  10.352  1.00 16.55 ?  152 TYR   A H    1 
ATOM   3161 H HA   . TYR   A 1 152 ? 16.335 -10.163 10.618  1.00 16.33 ?  152 TYR   A HA   1 
ATOM   3162 H HB2  . TYR   A 1 152 ? 18.136 -8.587  12.121  1.00 17.36 ?  152 TYR   A HB2  1 
ATOM   3163 H HB3  . TYR   A 1 152 ? 16.559 -8.409  12.251  1.00 17.36 ?  152 TYR   A HB3  1 
ATOM   3164 H HD1  . TYR   A 1 152 ? 19.172 -10.681 12.926  1.00 20.34 ?  152 TYR   A HD1  1 
ATOM   3165 H HD2  . TYR   A 1 152 ? 15.274 -10.012 13.501  1.00 19.04 ?  152 TYR   A HD2  1 
ATOM   3166 H HE1  . TYR   A 1 152 ? 19.106 -12.425 14.437  1.00 22.18 ?  152 TYR   A HE1  1 
ATOM   3167 H HE2  . TYR   A 1 152 ? 15.200 -11.761 15.018  1.00 20.73 ?  152 TYR   A HE2  1 
ATOM   3168 H HH   . TYR   A 1 152 ? 16.344 -13.399 16.081  1.00 25.39 ?  152 TYR   A HH   1 
ATOM   3169 N N    . LEU   A 1 153 ? 15.884 -8.632  8.766   1.00 13.46 ?  153 LEU   A N    1 
ATOM   3170 C CA   . LEU   A 1 153 ? 15.615 -7.726  7.660   1.00 13.58 ?  153 LEU   A CA   1 
ATOM   3171 C C    . LEU   A 1 153 ? 14.614 -6.661  8.084   1.00 14.39 ?  153 LEU   A C    1 
ATOM   3172 O O    . LEU   A 1 153 ? 13.524 -6.980  8.572   1.00 15.54 ?  153 LEU   A O    1 
ATOM   3173 C CB   . LEU   A 1 153 ? 15.051 -8.501  6.470   1.00 13.97 ?  153 LEU   A CB   1 
ATOM   3174 C CG   . LEU   A 1 153 ? 15.987 -9.508  5.801   1.00 13.95 ?  153 LEU   A CG   1 
ATOM   3175 C CD1  . LEU   A 1 153 ? 15.207 -10.375 4.817   1.00 14.42 ?  153 LEU   A CD1  1 
ATOM   3176 C CD2  . LEU   A 1 153 ? 17.124 -8.773  5.103   1.00 14.67 ?  153 LEU   A CD2  1 
ATOM   3177 H H    . LEU   A 1 153 ? 15.315 -9.282  8.824   1.00 16.13 ?  153 LEU   A H    1 
ATOM   3178 H HA   . LEU   A 1 153 ? 16.437 -7.298  7.400   1.00 16.27 ?  153 LEU   A HA   1 
ATOM   3179 H HB2  . LEU   A 1 153 ? 14.267 -8.984  6.773   1.00 16.75 ?  153 LEU   A HB2  1 
ATOM   3180 H HB3  . LEU   A 1 153 ? 14.786 -7.853  5.797   1.00 16.75 ?  153 LEU   A HB3  1 
ATOM   3181 H HG   . LEU   A 1 153 ? 16.372 -10.080 6.485   1.00 16.71 ?  153 LEU   A HG   1 
ATOM   3182 H HD11 . LEU   A 1 153 ? 15.795 -11.065 4.480   1.00 17.28 ?  153 LEU   A HD11 1 
ATOM   3183 H HD12 . LEU   A 1 153 ? 14.453 -10.766 5.274   1.00 17.28 ?  153 LEU   A HD12 1 
ATOM   3184 H HD13 . LEU   A 1 153 ? 14.901 -9.812  4.086   1.00 17.28 ?  153 LEU   A HD13 1 
ATOM   3185 H HD21 . LEU   A 1 153 ? 17.667 -9.420  4.635   1.00 17.58 ?  153 LEU   A HD21 1 
ATOM   3186 H HD22 . LEU   A 1 153 ? 16.744 -8.137  4.479   1.00 17.58 ?  153 LEU   A HD22 1 
ATOM   3187 H HD23 . LEU   A 1 153 ? 17.655 -8.308  5.769   1.00 17.58 ?  153 LEU   A HD23 1 
ATOM   3188 N N    A ALA   A 1 154 ? 14.975 -5.402  7.842   0.66 14.17 ?  154 ALA   A N    1 
ATOM   3189 N N    B ALA   A 1 154 ? 14.990 -5.396  7.926   0.34 14.09 ?  154 ALA   A N    1 
ATOM   3190 C CA   A ALA   A 1 154 ? 14.094 -4.261  8.034   0.66 14.71 ?  154 ALA   A CA   1 
ATOM   3191 C CA   B ALA   A 1 154 ? 14.122 -4.266  8.231   0.34 14.38 ?  154 ALA   A CA   1 
ATOM   3192 C C    A ALA   A 1 154 ? 13.608 -3.785  6.672   0.66 14.63 ?  154 ALA   A C    1 
ATOM   3193 C C    B ALA   A 1 154 ? 13.699 -3.643  6.908   0.34 14.57 ?  154 ALA   A C    1 
ATOM   3194 O O    A ALA   A 1 154 ? 14.420 -3.450  5.800   0.66 14.89 ?  154 ALA   A O    1 
ATOM   3195 O O    B ALA   A 1 154 ? 14.552 -3.211  6.125   0.34 14.33 ?  154 ALA   A O    1 
ATOM   3196 C CB   A ALA   A 1 154 ? 14.833 -3.125  8.738   0.66 15.01 ?  154 ALA   A CB   1 
ATOM   3197 C CB   B ALA   A 1 154 ? 14.857 -3.241  9.096   0.34 14.35 ?  154 ALA   A CB   1 
ATOM   3198 H H    A ALA   A 1 154 ? 15.755 -5.182  7.556   0.66 16.98 ?  154 ALA   A H    1 
ATOM   3199 H H    B ALA   A 1 154 ? 15.763 -5.159  7.634   0.34 16.88 ?  154 ALA   A H    1 
ATOM   3200 H HA   A ALA   A 1 154 ? 13.328 -4.513  8.567   0.66 17.63 ?  154 ALA   A HA   1 
ATOM   3201 H HA   B ALA   A 1 154 ? 13.332 -4.565  8.712   0.34 17.23 ?  154 ALA   A HA   1 
ATOM   3202 H HB1  A ALA   A 1 154 ? 14.228 -2.372  8.847   0.66 17.99 ?  154 ALA   A HB1  1 
ATOM   3203 H HB1  B ALA   A 1 154 ? 14.263 -2.497  9.288   0.34 17.19 ?  154 ALA   A HB1  1 
ATOM   3204 H HB2  A ALA   A 1 154 ? 15.138 -3.432  9.603   0.66 17.99 ?  154 ALA   A HB2  1 
ATOM   3205 H HB2  B ALA   A 1 154 ? 15.135 -3.662  9.926   0.34 17.19 ?  154 ALA   A HB2  1 
ATOM   3206 H HB3  A ALA   A 1 154 ? 15.594 -2.855  8.194   0.66 17.99 ?  154 ALA   A HB3  1 
ATOM   3207 H HB3  B ALA   A 1 154 ? 15.638 -2.921  8.613   0.34 17.19 ?  154 ALA   A HB3  1 
ATOM   3208 N N    A VAL   A 1 155 ? 12.290 -3.745  6.500   0.66 15.45 ?  155 VAL   A N    1 
ATOM   3209 N N    B VAL   A 1 155 ? 12.392 -3.606  6.654   0.34 15.48 ?  155 VAL   A N    1 
ATOM   3210 C CA   A VAL   A 1 155 ? 11.647 -3.260  5.285   0.66 16.19 ?  155 VAL   A CA   1 
ATOM   3211 C CA   B VAL   A 1 155 ? 11.845 -3.150  5.378   0.34 16.81 ?  155 VAL   A CA   1 
ATOM   3212 C C    A VAL   A 1 155 ? 10.904 -1.980  5.639   0.66 16.90 ?  155 VAL   A C    1 
ATOM   3213 C C    B VAL   A 1 155 ? 10.872 -2.018  5.666   0.34 18.71 ?  155 VAL   A C    1 
ATOM   3214 O O    A VAL   A 1 155 ? 9.990  -2.002  6.472   0.66 16.91 ?  155 VAL   A O    1 
ATOM   3215 O O    B VAL   A 1 155 ? 9.768  -2.257  6.174   0.34 18.89 ?  155 VAL   A O    1 
ATOM   3216 C CB   A VAL   A 1 155 ? 10.701 -4.315  4.690   0.66 16.11 ?  155 VAL   A CB   1 
ATOM   3217 C CB   B VAL   A 1 155 ? 11.153 -4.286  4.612   0.34 16.06 ?  155 VAL   A CB   1 
ATOM   3218 C CG1  A VAL   A 1 155 ? 9.978  -3.756  3.476   0.66 16.89 ?  155 VAL   A CG1  1 
ATOM   3219 C CG1  B VAL   A 1 155 ? 10.522 -3.761  3.331   0.34 15.87 ?  155 VAL   A CG1  1 
ATOM   3220 C CG2  A VAL   A 1 155 ? 11.482 -5.571  4.316   0.66 16.56 ?  155 VAL   A CG2  1 
ATOM   3221 C CG2  B VAL   A 1 155 ? 12.144 -5.388  4.299   0.34 15.61 ?  155 VAL   A CG2  1 
ATOM   3222 H H    A VAL   A 1 155 ? 11.730 -4.014  7.097   0.66 18.52 ?  155 VAL   A H    1 
ATOM   3223 H H    B VAL   A 1 155 ? 11.788 -3.846  7.223   0.34 18.56 ?  155 VAL   A H    1 
ATOM   3224 H HA   A VAL   A 1 155 ? 12.319 -3.047  4.626   0.66 19.41 ?  155 VAL   A HA   1 
ATOM   3225 H HA   B VAL   A 1 155 ? 12.562 -2.804  4.828   0.34 20.15 ?  155 VAL   A HA   1 
ATOM   3226 H HB   A VAL   A 1 155 ? 10.032 -4.556  5.354   0.66 19.31 ?  155 VAL   A HB   1 
ATOM   3227 H HB   B VAL   A 1 155 ? 10.450 -4.662  5.165   0.34 19.25 ?  155 VAL   A HB   1 
ATOM   3228 H HG11 A VAL   A 1 155 ? 9.528  -4.481  3.015   0.66 20.24 ?  155 VAL   A HG11 1 
ATOM   3229 H HG11 B VAL   A 1 155 ? 10.293 -4.514  2.764   0.34 19.01 ?  155 VAL   A HG11 1 
ATOM   3230 H HG12 A VAL   A 1 155 ? 9.325  -3.096  3.765   0.66 20.24 ?  155 VAL   A HG12 1 
ATOM   3231 H HG12 B VAL   A 1 155 ? 9.723  -3.260  3.552   0.34 19.01 ?  155 VAL   A HG12 1 
ATOM   3232 H HG13 A VAL   A 1 155 ? 10.626 -3.341  2.885   0.66 20.24 ?  155 VAL   A HG13 1 
ATOM   3233 H HG13 B VAL   A 1 155 ? 11.161 -3.190  2.877   0.34 19.01 ?  155 VAL   A HG13 1 
ATOM   3234 H HG21 A VAL   A 1 155 ? 10.875 -6.208  3.907   0.66 19.84 ?  155 VAL   A HG21 1 
ATOM   3235 H HG21 B VAL   A 1 155 ? 11.694 -6.084  3.796   0.34 18.71 ?  155 VAL   A HG21 1 
ATOM   3236 H HG22 A VAL   A 1 155 ? 12.181 -5.330  3.689   0.66 19.84 ?  155 VAL   A HG22 1 
ATOM   3237 H HG22 B VAL   A 1 155 ? 12.872 -5.018  3.774   0.34 18.71 ?  155 VAL   A HG22 1 
ATOM   3238 H HG23 A VAL   A 1 155 ? 11.871 -5.951  5.118   0.66 19.84 ?  155 VAL   A HG23 1 
ATOM   3239 H HG23 B VAL   A 1 155 ? 12.489 -5.750  5.131   0.34 18.71 ?  155 VAL   A HG23 1 
ATOM   3240 N N    A PHE   A 1 156 ? 11.296 -0.869  5.010   0.66 17.79 ?  156 PHE   A N    1 
ATOM   3241 N N    B PHE   A 1 156 ? 11.265 -0.787  5.332   0.34 20.35 ?  156 PHE   A N    1 
ATOM   3242 C CA   A PHE   A 1 156 ? 10.765 0.437   5.401   0.66 19.10 ?  156 PHE   A CA   1 
ATOM   3243 C CA   B PHE   A 1 156 ? 10.442 0.381   5.649   0.34 22.24 ?  156 PHE   A CA   1 
ATOM   3244 C C    A PHE   A 1 156 ? 9.297  0.594   5.018   0.66 19.47 ?  156 PHE   A C    1 
ATOM   3245 C C    B PHE   A 1 156 ? 9.510  0.731   4.485   0.34 22.69 ?  156 PHE   A C    1 
ATOM   3246 O O    A PHE   A 1 156 ? 8.490  1.113   5.803   0.66 20.45 ?  156 PHE   A O    1 
ATOM   3247 O O    B PHE   A 1 156 ? 9.605  1.784   3.852   0.34 23.61 ?  156 PHE   A O    1 
ATOM   3248 C CB   A PHE   A 1 156 ? 11.609 1.542   4.760   0.66 20.16 ?  156 PHE   A CB   1 
ATOM   3249 C CB   B PHE   A 1 156 ? 11.313 1.565   6.054   0.34 23.70 ?  156 PHE   A CB   1 
ATOM   3250 C CG   A PHE   A 1 156 ? 11.126 2.934   5.074   0.66 21.73 ?  156 PHE   A CG   1 
ATOM   3251 C CG   B PHE   A 1 156 ? 10.563 2.643   6.792   0.34 24.88 ?  156 PHE   A CG   1 
ATOM   3252 C CD1  A PHE   A 1 156 ? 11.102 3.388   6.381   0.66 22.70 ?  156 PHE   A CD1  1 
ATOM   3253 C CD1  B PHE   A 1 156 ? 9.393  2.351   7.481   0.34 25.33 ?  156 PHE   A CD1  1 
ATOM   3254 C CD2  A PHE   A 1 156 ? 10.703 3.787   4.064   0.66 22.62 ?  156 PHE   A CD2  1 
ATOM   3255 C CD2  B PHE   A 1 156 ? 11.018 3.949   6.787   0.34 25.38 ?  156 PHE   A CD2  1 
ATOM   3256 C CE1  A PHE   A 1 156 ? 10.660 4.667   6.678   0.66 23.78 ?  156 PHE   A CE1  1 
ATOM   3257 C CE1  B PHE   A 1 156 ? 8.703  3.334   8.154   0.34 25.79 ?  156 PHE   A CE1  1 
ATOM   3258 C CE2  A PHE   A 1 156 ? 10.263 5.067   4.355   0.66 23.73 ?  156 PHE   A CE2  1 
ATOM   3259 C CE2  B PHE   A 1 156 ? 10.328 4.939   7.459   0.34 25.66 ?  156 PHE   A CE2  1 
ATOM   3260 C CZ   A PHE   A 1 156 ? 10.245 5.507   5.664   0.66 24.19 ?  156 PHE   A CZ   1 
ATOM   3261 C CZ   B PHE   A 1 156 ? 9.169  4.630   8.142   0.34 25.88 ?  156 PHE   A CZ   1 
ATOM   3262 H H    A PHE   A 1 156 ? 11.855 -0.850  4.354   0.66 21.33 ?  156 PHE   A H    1 
ATOM   3263 H H    B PHE   A 1 156 ? 12.007 -0.600  4.937   0.34 24.40 ?  156 PHE   A H    1 
ATOM   3264 H HA   A PHE   A 1 156 ? 10.846 0.534   6.361   0.66 22.90 ?  156 PHE   A HA   1 
ATOM   3265 H HA   B PHE   A 1 156 ? 9.893  0.128   6.401   0.34 26.66 ?  156 PHE   A HA   1 
ATOM   3266 H HB2  A PHE   A 1 156 ? 12.526 1.471   5.077   0.66 24.17 ?  156 PHE   A HB2  1 
ATOM   3267 H HB2  B PHE   A 1 156 ? 12.023 1.244   6.630   0.34 28.42 ?  156 PHE   A HB2  1 
ATOM   3268 H HB3  A PHE   A 1 156 ? 11.591 1.438   3.794   0.66 24.17 ?  156 PHE   A HB3  1 
ATOM   3269 H HB3  B PHE   A 1 156 ? 11.698 1.967   5.257   0.34 28.42 ?  156 PHE   A HB3  1 
ATOM   3270 H HD1  A PHE   A 1 156 ? 11.389 2.825   7.067   0.66 27.21 ?  156 PHE   A HD1  1 
ATOM   3271 H HD1  B PHE   A 1 156 ? 9.074  1.474   7.495   0.34 30.37 ?  156 PHE   A HD1  1 
ATOM   3272 H HD2  A PHE   A 1 156 ? 10.719 3.496   3.181   0.66 27.12 ?  156 PHE   A HD2  1 
ATOM   3273 H HD2  B PHE   A 1 156 ? 11.800 4.162   6.329   0.34 30.43 ?  156 PHE   A HD2  1 
ATOM   3274 H HE1  A PHE   A 1 156 ? 10.653 4.960   7.562   0.66 28.51 ?  156 PHE   A HE1  1 
ATOM   3275 H HE1  B PHE   A 1 156 ? 7.922  3.119   8.612   0.34 30.92 ?  156 PHE   A HE1  1 
ATOM   3276 H HE2  A PHE   A 1 156 ? 9.984  5.628   3.670   0.66 28.45 ?  156 PHE   A HE2  1 
ATOM   3277 H HE2  B PHE   A 1 156 ? 10.644 5.813   7.450   0.34 30.77 ?  156 PHE   A HE2  1 
ATOM   3278 H HZ   A PHE   A 1 156 ? 9.950  6.365   5.864   0.66 29.00 ?  156 PHE   A HZ   1 
ATOM   3279 H HZ   B PHE   A 1 156 ? 8.703  5.295   8.594   0.34 31.03 ?  156 PHE   A HZ   1 
ATOM   3280 N N    A ASP   A 1 157 ? 8.939  0.182   3.811   0.66 19.73 ?  157 ASP   A N    1 
ATOM   3281 N N    B ASP   A 1 157 ? 8.579  -0.186  4.223   0.34 22.53 ?  157 ASP   A N    1 
ATOM   3282 C CA   A ASP   A 1 157 ? 7.605  0.427   3.279   0.66 21.14 ?  157 ASP   A CA   1 
ATOM   3283 C CA   B ASP   A 1 157 ? 7.474  0.080   3.300   0.34 22.08 ?  157 ASP   A CA   1 
ATOM   3284 C C    A ASP   A 1 157 ? 6.641  -0.626  3.818   0.66 21.18 ?  157 ASP   A C    1 
ATOM   3285 C C    B ASP   A 1 157 ? 6.407  -0.975  3.551   0.34 21.56 ?  157 ASP   A C    1 
ATOM   3286 O O    A ASP   A 1 157 ? 6.858  -1.828  3.628   0.66 20.96 ?  157 ASP   A O    1 
ATOM   3287 O O    B ASP   A 1 157 ? 6.615  -2.151  3.237   0.34 21.54 ?  157 ASP   A O    1 
ATOM   3288 C CB   A ASP   A 1 157 ? 7.675  0.354   1.759   0.66 23.03 ?  157 ASP   A CB   1 
ATOM   3289 C CB   B ASP   A 1 157 ? 7.943  0.048   1.852   0.34 22.30 ?  157 ASP   A CB   1 
ATOM   3290 C CG   A ASP   A 1 157 ? 6.416  0.859   1.093   0.66 25.01 ?  157 ASP   A CG   1 
ATOM   3291 C CG   B ASP   A 1 157 ? 6.844  0.433   0.874   0.34 23.06 ?  157 ASP   A CG   1 
ATOM   3292 O OD1  A ASP   A 1 157 ? 6.189  2.086   1.087   0.66 26.70 ?  157 ASP   A OD1  1 
ATOM   3293 O OD1  B ASP   A 1 157 ? 5.826  -0.288  0.801   0.34 23.47 ?  157 ASP   A OD1  1 
ATOM   3294 O OD2  A ASP   A 1 157 ? 5.649  0.025   0.574   0.66 25.53 -1 157 ASP   A OD2  1 
ATOM   3295 O OD2  B ASP   A 1 157 ? 6.990  1.474   0.194   0.34 23.40 -1 157 ASP   A OD2  1 
ATOM   3296 H H    A ASP   A 1 157 ? 9.466  -0.227  3.269   0.66 23.66 ?  157 ASP   A H    1 
ATOM   3297 H H    B ASP   A 1 157 ? 8.569  -0.972  4.566   0.34 27.02 ?  157 ASP   A H    1 
ATOM   3298 H HA   A ASP   A 1 157 ? 7.300  1.315   3.544   0.66 25.35 ?  157 ASP   A HA   1 
ATOM   3299 H HA   B ASP   A 1 157 ? 7.097  0.955   3.486   0.34 26.47 ?  157 ASP   A HA   1 
ATOM   3300 H HB2  A ASP   A 1 157 ? 8.443  0.867   1.455   0.66 27.61 ?  157 ASP   A HB2  1 
ATOM   3301 H HB2  B ASP   A 1 157 ? 8.647  0.695   1.745   0.34 26.74 ?  157 ASP   A HB2  1 
ATOM   3302 H HB3  A ASP   A 1 157 ? 7.777  -0.568  1.497   0.66 27.61 ?  157 ASP   A HB3  1 
ATOM   3303 H HB3  B ASP   A 1 157 ? 8.263  -0.845  1.634   0.34 26.74 ?  157 ASP   A HB3  1 
ATOM   3304 N N    A LYS   A 1 158 ? 5.572  -0.178  4.488   0.66 21.81 ?  158 LYS   A N    1 
ATOM   3305 N N    B LYS   A 1 158 ? 5.270  -0.549  4.104   0.34 21.35 ?  158 LYS   A N    1 
ATOM   3306 C CA   A LYS   A 1 158 ? 4.630  -1.123  5.084   0.66 22.45 ?  158 LYS   A CA   1 
ATOM   3307 C CA   B LYS   A 1 158 ? 4.227  -1.494  4.493   0.34 21.29 ?  158 LYS   A CA   1 
ATOM   3308 C C    A LYS   A 1 158 ? 3.900  -1.922  4.013   0.66 22.22 ?  158 LYS   A C    1 
ATOM   3309 C C    B LYS   A 1 158 ? 3.713  -2.278  3.290   0.34 20.07 ?  158 LYS   A C    1 
ATOM   3310 O O    A LYS   A 1 158 ? 3.715  -3.137  4.153   0.66 21.34 ?  158 LYS   A O    1 
ATOM   3311 O O    B LYS   A 1 158 ? 3.600  -3.509  3.339   0.34 19.26 ?  158 LYS   A O    1 
ATOM   3312 C CB   A LYS   A 1 158 ? 3.640  -0.387  5.990   0.66 23.46 ?  158 LYS   A CB   1 
ATOM   3313 C CB   B LYS   A 1 158 ? 3.087  -0.749  5.191   0.34 22.50 ?  158 LYS   A CB   1 
ATOM   3314 C CG   A LYS   A 1 158 ? 2.429  -1.216  6.434   0.66 25.08 ?  158 LYS   A CG   1 
ATOM   3315 C CG   B LYS   A 1 158 ? 1.846  -1.597  5.434   0.34 23.56 ?  158 LYS   A CG   1 
ATOM   3316 C CD   A LYS   A 1 158 ? 2.817  -2.450  7.249   0.66 26.24 ?  158 LYS   A CD   1 
ATOM   3317 C CD   B LYS   A 1 158 ? 0.859  -0.909  6.367   0.34 24.42 ?  158 LYS   A CD   1 
ATOM   3318 C CE   A LYS   A 1 158 ? 1.571  -3.172  7.765   0.66 26.86 ?  158 LYS   A CE   1 
ATOM   3319 C CE   B LYS   A 1 158 ? 0.413  0.439   5.826   0.34 24.99 ?  158 LYS   A CE   1 
ATOM   3320 N NZ   A LYS   A 1 158 ? 1.872  -4.498  8.378   0.66 27.07 ?  158 LYS   A NZ   1 
ATOM   3321 N NZ   B LYS   A 1 158 ? -0.670 1.033   6.656   0.34 25.27 ?  158 LYS   A NZ   1 
ATOM   3322 H H    A LYS   A 1 158 ? 5.378  0.653   4.605   0.66 26.15 ?  158 LYS   A H    1 
ATOM   3323 H H    B LYS   A 1 158 ? 5.080  0.275   4.259   0.34 25.60 ?  158 LYS   A H    1 
ATOM   3324 H HA   A LYS   A 1 158 ? 5.125  -1.747  5.637   0.66 26.92 ?  158 LYS   A HA   1 
ATOM   3325 H HA   B LYS   A 1 158 ? 4.595  -2.128  5.126   0.34 25.53 ?  158 LYS   A HA   1 
ATOM   3326 H HB2  A LYS   A 1 158 ? 4.107  -0.100  6.792   0.66 28.13 ?  158 LYS   A HB2  1 
ATOM   3327 H HB2  B LYS   A 1 158 ? 3.400  -0.434  6.056   0.34 26.98 ?  158 LYS   A HB2  1 
ATOM   3328 H HB3  A LYS   A 1 158 ? 3.305  0.391   5.516   0.66 28.13 ?  158 LYS   A HB3  1 
ATOM   3329 H HB3  B LYS   A 1 158 ? 2.826  0.007   4.643   0.34 26.98 ?  158 LYS   A HB3  1 
ATOM   3330 H HG2  A LYS   A 1 158 ? 1.862  -0.661  6.990   0.66 30.08 ?  158 LYS   A HG2  1 
ATOM   3331 H HG2  B LYS   A 1 158 ? 1.396  -1.756  4.589   0.34 28.25 ?  158 LYS   A HG2  1 
ATOM   3332 H HG3  A LYS   A 1 158 ? 1.932  -1.510  5.654   0.66 30.08 ?  158 LYS   A HG3  1 
ATOM   3333 H HG3  B LYS   A 1 158 ? 2.108  -2.439  5.838   0.34 28.25 ?  158 LYS   A HG3  1 
ATOM   3334 H HD2  A LYS   A 1 158 ? 3.318  -3.062  6.689   0.66 31.46 ?  158 LYS   A HD2  1 
ATOM   3335 H HD2  B LYS   A 1 158 ? 0.072  -1.467  6.470   0.34 29.29 ?  158 LYS   A HD2  1 
ATOM   3336 H HD3  A LYS   A 1 158 ? 3.352  -2.175  8.011   0.66 31.46 ?  158 LYS   A HD3  1 
ATOM   3337 H HD3  B LYS   A 1 158 ? 1.281  -0.764  7.229   0.34 29.29 ?  158 LYS   A HD3  1 
ATOM   3338 H HE2  A LYS   A 1 158 ? 1.146  -2.619  8.439   0.66 32.21 ?  158 LYS   A HE2  1 
ATOM   3339 H HE2  B LYS   A 1 158 ? 1.166  1.053   5.831   0.34 29.96 ?  158 LYS   A HE2  1 
ATOM   3340 H HE3  A LYS   A 1 158 ? 0.965  -3.315  7.023   0.66 32.21 ?  158 LYS   A HE3  1 
ATOM   3341 H HE3  B LYS   A 1 158 ? 0.078  0.327   4.923   0.34 29.96 ?  158 LYS   A HE3  1 
ATOM   3342 H HZ1  A LYS   A 1 158 ? 1.120  -4.879  8.662   0.66 32.46 ?  158 LYS   A HZ1  1 
ATOM   3343 H HZ1  B LYS   A 1 158 ? -0.913 1.821   6.321   0.34 30.30 ?  158 LYS   A HZ1  1 
ATOM   3344 H HZ2  A LYS   A 1 158 ? 2.257  -5.030  7.776   0.66 32.46 ?  158 LYS   A HZ2  1 
ATOM   3345 H HZ2  B LYS   A 1 158 ? -1.376 0.493   6.667   0.34 30.30 ?  158 LYS   A HZ2  1 
ATOM   3346 H HZ3  A LYS   A 1 158 ? 2.425  -4.397  9.068   0.66 32.46 ?  158 LYS   A HZ3  1 
ATOM   3347 H HZ3  B LYS   A 1 158 ? -0.384 1.151   7.491   0.34 30.30 ?  158 LYS   A HZ3  1 
ATOM   3348 N N    A ASN   A 1 159 ? 3.466  -1.260  2.941   0.66 22.89 ?  159 ASN   A N    1 
ATOM   3349 N N    B ASN   A 1 159 ? 3.396  -1.579  2.197   0.34 20.43 ?  159 ASN   A N    1 
ATOM   3350 C CA   A ASN   A 1 159 ? 2.816  -1.986  1.857   0.66 23.60 ?  159 ASN   A CA   1 
ATOM   3351 C CA   B ASN   A 1 159 ? 2.850  -2.249  1.020   0.34 21.15 ?  159 ASN   A CA   1 
ATOM   3352 C C    A ASN   A 1 159 ? 3.754  -3.035  1.270   0.66 22.45 ?  159 ASN   A C    1 
ATOM   3353 C C    B ASN   A 1 159 ? 3.774  -3.365  0.547   0.34 19.77 ?  159 ASN   A C    1 
ATOM   3354 O O    A ASN   A 1 159 ? 3.346  -4.174  1.016   0.66 21.69 ?  159 ASN   A O    1 
ATOM   3355 O O    B ASN   A 1 159 ? 3.314  -4.446  0.161   0.34 20.10 ?  159 ASN   A O    1 
ATOM   3356 C CB   A ASN   A 1 159 ? 2.326  -1.003  0.790   0.66 25.76 ?  159 ASN   A CB   1 
ATOM   3357 C CB   B ASN   A 1 159 ? 2.607  -1.224  -0.093  0.34 23.24 ?  159 ASN   A CB   1 
ATOM   3358 C CG   A ASN   A 1 159 ? 1.126  -0.194  1.251   0.66 28.36 ?  159 ASN   A CG   1 
ATOM   3359 C CG   B ASN   A 1 159 ? 1.766  -0.042  0.368   0.34 25.32 ?  159 ASN   A CG   1 
ATOM   3360 O OD1  A ASN   A 1 159 ? 0.246  -0.716  1.928   0.66 29.17 ?  159 ASN   A OD1  1 
ATOM   3361 O OD1  B ASN   A 1 159 ? 1.915  1.070   -0.139  0.34 26.32 ?  159 ASN   A OD1  1 
ATOM   3362 N ND2  A ASN   A 1 159 ? 1.087  1.084   0.888   0.66 29.36 ?  159 ASN   A ND2  1 
ATOM   3363 N ND2  B ASN   A 1 159 ? 0.883  -0.276  1.333   0.34 26.21 ?  159 ASN   A ND2  1 
ATOM   3364 H H    A ASN   A 1 159 ? 3.537  -0.412  2.821   0.66 27.44 ?  159 ASN   A H    1 
ATOM   3365 H H    B ASN   A 1 159 ? 3.491  -0.729  2.115   0.34 24.49 ?  159 ASN   A H    1 
ATOM   3366 H HA   A ASN   A 1 159 ? 2.039  -2.447  2.210   0.66 28.30 ?  159 ASN   A HA   1 
ATOM   3367 H HA   B ASN   A 1 159 ? 1.996  -2.646  1.244   0.34 25.35 ?  159 ASN   A HA   1 
ATOM   3368 H HB2  A ASN   A 1 159 ? 3.033  -0.378  0.579   0.66 30.88 ?  159 ASN   A HB2  1 
ATOM   3369 H HB2  B ASN   A 1 159 ? 3.458  -0.871  -0.400  0.34 27.87 ?  159 ASN   A HB2  1 
ATOM   3370 H HB3  A ASN   A 1 159 ? 2.063  -1.495  -0.003  0.66 30.88 ?  159 ASN   A HB3  1 
ATOM   3371 H HB3  B ASN   A 1 159 ? 2.140  -1.648  -0.829  0.34 27.87 ?  159 ASN   A HB3  1 
ATOM   3372 H HD21 A ASN   A 1 159 ? 0.424  1.580   1.128   0.66 35.21 ?  159 ASN   A HD21 1 
ATOM   3373 H HD21 B ASN   A 1 159 ? 0.387  0.362   1.624   0.34 31.43 ?  159 ASN   A HD21 1 
ATOM   3374 H HD22 A ASN   A 1 159 ? 1.724  1.414   0.419   0.66 35.21 ?  159 ASN   A HD22 1 
ATOM   3375 H HD22 B ASN   A 1 159 ? 0.807  -1.062  1.670   0.34 31.43 ?  159 ASN   A HD22 1 
ATOM   3376 N N    A LEU   A 1 160 ? 5.026  -2.682  1.081   0.66 21.84 ?  160 LEU   A N    1 
ATOM   3377 N N    B LEU   A 1 160 ? 5.084  -3.125  0.590   0.34 18.64 ?  160 LEU   A N    1 
ATOM   3378 C CA   A LEU   A 1 160 ? 5.974  -3.651  0.545   0.66 21.48 ?  160 LEU   A CA   1 
ATOM   3379 C CA   B LEU   A 1 160 ? 6.048  -4.141  0.181   0.34 17.74 ?  160 LEU   A CA   1 
ATOM   3380 C C    A LEU   A 1 160 ? 6.178  -4.812  1.509   0.66 20.97 ?  160 LEU   A C    1 
ATOM   3381 C C    B LEU   A 1 160 ? 6.205  -5.218  1.252   0.34 17.58 ?  160 LEU   A C    1 
ATOM   3382 O O    A LEU   A 1 160 ? 6.244  -5.971  1.087   0.66 21.75 ?  160 LEU   A O    1 
ATOM   3383 O O    B LEU   A 1 160 ? 6.166  -6.416  0.949   0.34 18.06 ?  160 LEU   A O    1 
ATOM   3384 C CB   A LEU   A 1 160 ? 7.306  -2.977  0.229   0.66 21.46 ?  160 LEU   A CB   1 
ATOM   3385 C CB   B LEU   A 1 160 ? 7.394  -3.480  -0.120  0.34 17.27 ?  160 LEU   A CB   1 
ATOM   3386 C CG   A LEU   A 1 160 ? 8.395  -3.950  -0.222  0.66 21.46 ?  160 LEU   A CG   1 
ATOM   3387 C CG   B LEU   A 1 160 ? 8.521  -4.449  -0.473  0.34 17.19 ?  160 LEU   A CG   1 
ATOM   3388 C CD1  A LEU   A 1 160 ? 7.948  -4.699  -1.464  0.66 21.71 ?  160 LEU   A CD1  1 
ATOM   3389 C CD1  B LEU   A 1 160 ? 8.140  -5.259  -1.697  0.34 17.49 ?  160 LEU   A CD1  1 
ATOM   3390 C CD2  A LEU   A 1 160 ? 9.702  -3.226  -0.470  0.66 21.27 ?  160 LEU   A CD2  1 
ATOM   3391 C CD2  B LEU   A 1 160 ? 9.830  -3.705  -0.691  0.34 17.22 ?  160 LEU   A CD2  1 
ATOM   3392 H H    A LEU   A 1 160 ? 5.355  -1.906  1.262   0.66 26.19 ?  160 LEU   A H    1 
ATOM   3393 H H    B LEU   A 1 160 ? 5.435  -2.386  0.856   0.34 22.34 ?  160 LEU   A H    1 
ATOM   3394 H HA   A LEU   A 1 160 ? 5.612  -4.006  -0.279  0.66 25.76 ?  160 LEU   A HA   1 
ATOM   3395 H HA   B LEU   A 1 160 ? 5.730  -4.560  -0.634  0.34 21.27 ?  160 LEU   A HA   1 
ATOM   3396 H HB2  A LEU   A 1 160 ? 7.172  -2.316  -0.474  0.66 25.73 ?  160 LEU   A HB2  1 
ATOM   3397 H HB2  B LEU   A 1 160 ? 7.280  -2.874  -0.871  0.34 20.70 ?  160 LEU   A HB2  1 
ATOM   3398 H HB3  A LEU   A 1 160 ? 7.624  -2.547  1.033   0.66 25.73 ?  160 LEU   A HB3  1 
ATOM   3399 H HB3  B LEU   A 1 160 ? 7.671  -2.977  0.662   0.34 20.70 ?  160 LEU   A HB3  1 
ATOM   3400 H HG   A LEU   A 1 160 ? 8.551  -4.600  0.480   0.66 25.73 ?  160 LEU   A HG   1 
ATOM   3401 H HG   B LEU   A 1 160 ? 8.651  -5.061  0.265   0.34 20.61 ?  160 LEU   A HG   1 
ATOM   3402 H HD11 A LEU   A 1 160 ? 8.692  -5.218  -1.800  0.66 26.03 ?  160 LEU   A HD11 1 
ATOM   3403 H HD11 B LEU   A 1 160 ? 8.910  -5.765  -1.988  0.34 20.96 ?  160 LEU   A HD11 1 
ATOM   3404 H HD12 A LEU   A 1 160 ? 7.213  -5.290  -1.232  0.66 26.03 ?  160 LEU   A HD12 1 
ATOM   3405 H HD12 B LEU   A 1 160 ? 7.415  -5.861  -1.463  0.34 20.96 ?  160 LEU   A HD12 1 
ATOM   3406 H HD13 A LEU   A 1 160 ? 7.659  -4.059  -2.133  0.66 26.03 ?  160 LEU   A HD13 1 
ATOM   3407 H HD13 B LEU   A 1 160 ? 7.854  -4.652  -2.398  0.34 20.96 ?  160 LEU   A HD13 1 
ATOM   3408 H HD21 A LEU   A 1 160 ? 10.371 -3.873  -0.750  0.66 25.50 ?  160 LEU   A HD21 1 
ATOM   3409 H HD21 B LEU   A 1 160 ? 10.525 -4.347  -0.906  0.34 20.64 ?  160 LEU   A HD21 1 
ATOM   3410 H HD22 A LEU   A 1 160 ? 9.571  -2.564  -1.166  0.66 25.50 ?  160 LEU   A HD22 1 
ATOM   3411 H HD22 B LEU   A 1 160 ? 9.721  -3.078  -1.423  0.34 20.64 ?  160 LEU   A HD22 1 
ATOM   3412 H HD23 A LEU   A 1 160 ? 9.985  -2.794  0.351   0.66 25.50 ?  160 LEU   A HD23 1 
ATOM   3413 H HD23 B LEU   A 1 160 ? 10.063 -3.227  0.121   0.34 20.64 ?  160 LEU   A HD23 1 
ATOM   3414 N N    A TYR   A 1 161 ? 6.274  -4.520  2.807   0.66 20.37 ?  161 TYR   A N    1 
ATOM   3415 N N    B TYR   A 1 161 ? 6.393  -4.804  2.510   0.34 17.63 ?  161 TYR   A N    1 
ATOM   3416 C CA   A TYR   A 1 161 ? 6.435  -5.583  3.793   0.66 20.15 ?  161 TYR   A CA   1 
ATOM   3417 C CA   B TYR   A 1 161 ? 6.457  -5.760  3.614   0.34 18.30 ?  161 TYR   A CA   1 
ATOM   3418 C C    A TYR   A 1 161 ? 5.316  -6.617  3.687   0.66 21.06 ?  161 TYR   A C    1 
ATOM   3419 C C    B TYR   A 1 161 ? 5.231  -6.663  3.612   0.34 19.45 ?  161 TYR   A C    1 
ATOM   3420 O O    A TYR   A 1 161 ? 5.570  -7.827  3.686   0.66 21.04 ?  161 TYR   A O    1 
ATOM   3421 O O    B TYR   A 1 161 ? 5.348  -7.893  3.651   0.34 19.39 ?  161 TYR   A O    1 
ATOM   3422 C CB   A TYR   A 1 161 ? 6.502  -4.991  5.201   0.66 20.02 ?  161 TYR   A CB   1 
ATOM   3423 C CB   B TYR   A 1 161 ? 6.577  -5.009  4.946   0.34 18.11 ?  161 TYR   A CB   1 
ATOM   3424 C CG   A TYR   A 1 161 ? 6.409  -6.037  6.276   0.66 19.66 ?  161 TYR   A CG   1 
ATOM   3425 C CG   B TYR   A 1 161 ? 6.464  -5.877  6.192   0.34 18.01 ?  161 TYR   A CG   1 
ATOM   3426 C CD1  A TYR   A 1 161 ? 7.521  -6.776  6.645   0.66 19.45 ?  161 TYR   A CD1  1 
ATOM   3427 C CD1  B TYR   A 1 161 ? 5.226  -6.144  6.770   0.34 18.25 ?  161 TYR   A CD1  1 
ATOM   3428 C CD2  A TYR   A 1 161 ? 5.203  -6.297  6.916   0.66 19.88 ?  161 TYR   A CD2  1 
ATOM   3429 C CD2  B TYR   A 1 161 ? 7.596  -6.409  6.803   0.34 17.93 ?  161 TYR   A CD2  1 
ATOM   3430 C CE1  A TYR   A 1 161 ? 7.440  -7.740  7.616   0.66 19.38 ?  161 TYR   A CE1  1 
ATOM   3431 C CE1  B TYR   A 1 161 ? 5.118  -6.930  7.908   0.34 18.44 ?  161 TYR   A CE1  1 
ATOM   3432 C CE2  A TYR   A 1 161 ? 5.111  -7.260  7.892   0.66 19.96 ?  161 TYR   A CE2  1 
ATOM   3433 C CE2  B TYR   A 1 161 ? 7.497  -7.197  7.941   0.34 18.28 ?  161 TYR   A CE2  1 
ATOM   3434 C CZ   A TYR   A 1 161 ? 6.233  -7.978  8.237   0.66 20.02 ?  161 TYR   A CZ   1 
ATOM   3435 C CZ   B TYR   A 1 161 ? 6.255  -7.452  8.488   0.34 18.83 ?  161 TYR   A CZ   1 
ATOM   3436 O OH   A TYR   A 1 161 ? 6.157  -8.938  9.212   0.66 20.44 ?  161 TYR   A OH   1 
ATOM   3437 O OH   B TYR   A 1 161 ? 6.150  -8.233  9.619   0.34 19.83 ?  161 TYR   A OH   1 
ATOM   3438 H H    A TYR   A 1 161 ? 6.241  -3.725  3.139   0.66 24.43 ?  161 TYR   A H    1 
ATOM   3439 H H    B TYR   A 1 161 ? 6.476  -3.985  2.742   0.34 21.14 ?  161 TYR   A H    1 
ATOM   3440 H HA   A TYR   A 1 161 ? 7.266  -6.040  3.626   0.66 24.16 ?  161 TYR   A HA   1 
ATOM   3441 H HA   B TYR   A 1 161 ? 7.243  -6.316  3.507   0.34 21.94 ?  161 TYR   A HA   1 
ATOM   3442 H HB2  A TYR   A 1 161 ? 7.349  -4.527  5.308   0.66 24.00 ?  161 TYR   A HB2  1 
ATOM   3443 H HB2  B TYR   A 1 161 ? 7.442  -4.570  4.975   0.34 21.71 ?  161 TYR   A HB2  1 
ATOM   3444 H HB3  A TYR   A 1 161 ? 5.767  -4.368  5.324   0.66 24.00 ?  161 TYR   A HB3  1 
ATOM   3445 H HB3  B TYR   A 1 161 ? 5.874  -4.342  4.989   0.34 21.71 ?  161 TYR   A HB3  1 
ATOM   3446 H HD1  A TYR   A 1 161 ? 8.333  -6.620  6.224   0.66 23.32 ?  161 TYR   A HD1  1 
ATOM   3447 H HD1  B TYR   A 1 161 ? 4.453  -5.798  6.386   0.34 21.88 ?  161 TYR   A HD1  1 
ATOM   3448 H HD2  A TYR   A 1 161 ? 4.443  -5.813  6.683   0.66 23.83 ?  161 TYR   A HD2  1 
ATOM   3449 H HD2  B TYR   A 1 161 ? 8.434  -6.239  6.439   0.34 21.49 ?  161 TYR   A HD2  1 
ATOM   3450 H HE1  A TYR   A 1 161 ? 8.192  -8.235  7.854   0.66 23.23 ?  161 TYR   A HE1  1 
ATOM   3451 H HE1  B TYR   A 1 161 ? 4.281  -7.103  8.282   0.34 22.10 ?  161 TYR   A HE1  1 
ATOM   3452 H HE2  A TYR   A 1 161 ? 4.295  -7.429  8.315   0.66 23.92 ?  161 TYR   A HE2  1 
ATOM   3453 H HE2  B TYR   A 1 161 ? 8.263  -7.547  8.338   0.34 21.92 ?  161 TYR   A HE2  1 
ATOM   3454 H HH   A TYR   A 1 161 ? 5.365  -8.989  9.512   0.66 24.50 ?  161 TYR   A HH   1 
ATOM   3455 H HH   B TYR   A 1 161 ? 6.909  -8.482  9.874   0.34 23.77 ?  161 TYR   A HH   1 
ATOM   3456 N N    A ASP   A 1 162 ? 4.066  -6.157  3.596   0.66 21.66 ?  162 ASP   A N    1 
ATOM   3457 N N    B ASP   A 1 162 ? 4.040  -6.060  3.569   0.34 20.46 ?  162 ASP   A N    1 
ATOM   3458 C CA   A ASP   A 1 162 ? 2.940  -7.088  3.552   0.66 22.10 ?  162 ASP   A CA   1 
ATOM   3459 C CA   B ASP   A 1 162 ? 2.814  -6.843  3.448   0.34 21.30 ?  162 ASP   A CA   1 
ATOM   3460 C C    A ASP   A 1 162 ? 2.987  -7.949  2.294   0.66 22.65 ?  162 ASP   A C    1 
ATOM   3461 C C    B ASP   A 1 162 ? 2.875  -7.771  2.242   0.34 22.17 ?  162 ASP   A C    1 
ATOM   3462 O O    A ASP   A 1 162 ? 2.654  -9.141  2.334   0.66 23.07 ?  162 ASP   A O    1 
ATOM   3463 O O    B ASP   A 1 162 ? 2.459  -8.934  2.319   0.34 22.47 ?  162 ASP   A O    1 
ATOM   3464 C CB   A ASP   A 1 162 ? 1.614  -6.322  3.624   0.66 22.80 ?  162 ASP   A CB   1 
ATOM   3465 C CB   B ASP   A 1 162 ? 1.605  -5.910  3.332   0.34 21.59 ?  162 ASP   A CB   1 
ATOM   3466 C CG   A ASP   A 1 162 ? 1.311  -5.780  5.010   0.66 23.61 ?  162 ASP   A CG   1 
ATOM   3467 C CG   B ASP   A 1 162 ? 1.338  -5.129  4.607   0.34 21.70 ?  162 ASP   A CG   1 
ATOM   3468 O OD1  A ASP   A 1 162 ? 1.964  -6.202  5.986   0.66 24.13 ?  162 ASP   A OD1  1 
ATOM   3469 O OD1  B ASP   A 1 162 ? 1.920  -5.468  5.657   0.34 21.77 ?  162 ASP   A OD1  1 
ATOM   3470 O OD2  A ASP   A 1 162 ? 0.392  -4.933  5.118   0.66 24.20 -1 162 ASP   A OD2  1 
ATOM   3471 O OD2  B ASP   A 1 162 ? 0.536  -4.172  4.557   0.34 21.72 -1 162 ASP   A OD2  1 
ATOM   3472 H H    A ASP   A 1 162 ? 3.839  -5.328  3.554   0.66 25.97 ?  162 ASP   A H    1 
ATOM   3473 H H    B ASP   A 1 162 ? 3.919  -5.210  3.614   0.34 24.53 ?  162 ASP   A H    1 
ATOM   3474 H HA   A ASP   A 1 162 ? 2.978  -7.684  4.314   0.66 26.50 ?  162 ASP   A HA   1 
ATOM   3475 H HA   B ASP   A 1 162 ? 2.700  -7.385  4.245   0.34 25.54 ?  162 ASP   A HA   1 
ATOM   3476 H HB2  A ASP   A 1 162 ? 1.645  -5.567  3.021   0.66 27.34 ?  162 ASP   A HB2  1 
ATOM   3477 H HB2  B ASP   A 1 162 ? 1.760  -5.274  2.617   0.34 25.88 ?  162 ASP   A HB2  1 
ATOM   3478 H HB3  A ASP   A 1 162 ? 0.883  -6.914  3.384   0.66 27.34 ?  162 ASP   A HB3  1 
ATOM   3479 H HB3  B ASP   A 1 162 ? 0.814  -6.439  3.138   0.34 25.88 ?  162 ASP   A HB3  1 
ATOM   3480 N N    A LYS   A 1 163 ? 3.395  -7.362  1.167   0.66 23.44 ?  163 LYS   A N    1 
ATOM   3481 N N    B LYS   A 1 163 ? 3.390  -7.275  1.114   0.34 23.06 ?  163 LYS   A N    1 
ATOM   3482 C CA   A LYS   A 1 163 ? 3.477  -8.120  -0.078  0.66 23.73 ?  163 LYS   A CA   1 
ATOM   3483 C CA   B LYS   A 1 163 ? 3.484  -8.109  -0.080  0.34 23.60 ?  163 LYS   A CA   1 
ATOM   3484 C C    A LYS   A 1 163 ? 4.583  -9.169  -0.018  0.66 22.98 ?  163 LYS   A C    1 
ATOM   3485 C C    B LYS   A 1 163 ? 4.534  -9.202  0.093   0.34 22.81 ?  163 LYS   A C    1 
ATOM   3486 O O    A LYS   A 1 163 ? 4.446  -10.256 -0.590  0.66 23.42 ?  163 LYS   A O    1 
ATOM   3487 O O    B LYS   A 1 163 ? 4.301  -10.360 -0.274  0.34 23.15 ?  163 LYS   A O    1 
ATOM   3488 C CB   A LYS   A 1 163 ? 3.702  -7.167  -1.251  0.66 26.28 ?  163 LYS   A CB   1 
ATOM   3489 C CB   B LYS   A 1 163 ? 3.797  -7.241  -1.301  0.34 25.66 ?  163 LYS   A CB   1 
ATOM   3490 C CG   A LYS   A 1 163 ? 3.696  -7.849  -2.608  0.66 28.86 ?  163 LYS   A CG   1 
ATOM   3491 C CG   B LYS   A 1 163 ? 3.986  -8.031  -2.593  0.34 27.73 ?  163 LYS   A CG   1 
ATOM   3492 C CD   A LYS   A 1 163 ? 4.098  -6.890  -3.712  0.66 31.39 ?  163 LYS   A CD   1 
ATOM   3493 C CD   B LYS   A 1 163 ? 4.827  -7.273  -3.609  0.34 29.77 ?  163 LYS   A CD   1 
ATOM   3494 C CE   A LYS   A 1 163 ? 4.045  -7.565  -5.073  0.66 33.53 ?  163 LYS   A CE   1 
ATOM   3495 C CE   B LYS   A 1 163 ? 3.971  -6.527  -4.620  0.34 31.27 ?  163 LYS   A CE   1 
ATOM   3496 N NZ   A LYS   A 1 163 ? 4.719  -6.757  -6.125  0.66 34.56 ?  163 LYS   A NZ   1 
ATOM   3497 N NZ   B LYS   A 1 163 ? 4.804  -5.926  -5.700  0.34 32.15 ?  163 LYS   A NZ   1 
ATOM   3498 H H    A LYS   A 1 163 ? 3.614  -6.530  1.098   0.66 28.10 ?  163 LYS   A H    1 
ATOM   3499 H H    B LYS   A 1 163 ? 3.688  -6.470  1.019   0.34 27.64 ?  163 LYS   A H    1 
ATOM   3500 H HA   A LYS   A 1 163 ? 2.632  -8.575  -0.225  0.66 28.45 ?  163 LYS   A HA   1 
ATOM   3501 H HA   B LYS   A 1 163 ? 2.627  -8.534  -0.232  0.34 28.30 ?  163 LYS   A HA   1 
ATOM   3502 H HB2  A LYS   A 1 163 ? 2.996  -6.498  -1.255  0.66 31.51 ?  163 LYS   A HB2  1 
ATOM   3503 H HB2  B LYS   A 1 163 ? 3.061  -6.619  -1.444  0.34 30.77 ?  163 LYS   A HB2  1 
ATOM   3504 H HB3  A LYS   A 1 163 ? 4.561  -6.733  -1.142  0.66 31.51 ?  163 LYS   A HB3  1 
ATOM   3505 H HB3  B LYS   A 1 163 ? 4.612  -6.745  -1.131  0.34 30.77 ?  163 LYS   A HB3  1 
ATOM   3506 H HG2  A LYS   A 1 163 ? 4.327  -8.585  -2.603  0.66 34.60 ?  163 LYS   A HG2  1 
ATOM   3507 H HG2  B LYS   A 1 163 ? 4.431  -8.872  -2.409  0.34 33.25 ?  163 LYS   A HG2  1 
ATOM   3508 H HG3  A LYS   A 1 163 ? 2.802  -8.175  -2.798  0.66 34.60 ?  163 LYS   A HG3  1 
ATOM   3509 H HG3  B LYS   A 1 163 ? 3.115  -8.199  -2.986  0.34 33.25 ?  163 LYS   A HG3  1 
ATOM   3510 H HD2  A LYS   A 1 163 ? 3.486  -6.137  -3.723  0.66 37.64 ?  163 LYS   A HD2  1 
ATOM   3511 H HD2  B LYS   A 1 163 ? 5.385  -6.625  -3.150  0.34 35.70 ?  163 LYS   A HD2  1 
ATOM   3512 H HD3  A LYS   A 1 163 ? 5.005  -6.583  -3.557  0.66 37.64 ?  163 LYS   A HD3  1 
ATOM   3513 H HD3  B LYS   A 1 163 ? 5.381  -7.905  -4.090  0.34 35.70 ?  163 LYS   A HD3  1 
ATOM   3514 H HE2  A LYS   A 1 163 ? 4.478  -8.430  -5.025  0.66 40.21 ?  163 LYS   A HE2  1 
ATOM   3515 H HE2  B LYS   A 1 163 ? 3.346  -7.147  -5.029  0.34 37.50 ?  163 LYS   A HE2  1 
ATOM   3516 H HE3  A LYS   A 1 163 ? 3.120  -7.677  -5.330  0.66 40.21 ?  163 LYS   A HE3  1 
ATOM   3517 H HE3  B LYS   A 1 163 ? 3.492  -5.814  -4.171  0.34 37.50 ?  163 LYS   A HE3  1 
ATOM   3518 H HZ1  A LYS   A 1 163 ? 4.674  -7.178  -6.907  0.66 41.45 ?  163 LYS   A HZ1  1 
ATOM   3519 H HZ1  B LYS   A 1 163 ? 4.286  -5.496  -6.281  0.34 38.55 ?  163 LYS   A HZ1  1 
ATOM   3520 H HZ2  A LYS   A 1 163 ? 4.320  -5.965  -6.198  0.66 41.45 ?  163 LYS   A HZ2  1 
ATOM   3521 H HZ2  B LYS   A 1 163 ? 5.386  -5.350  -5.350  0.34 38.55 ?  163 LYS   A HZ2  1 
ATOM   3522 H HZ3  A LYS   A 1 163 ? 5.574  -6.631  -5.912  0.66 41.45 ?  163 LYS   A HZ3  1 
ATOM   3523 H HZ3  B LYS   A 1 163 ? 5.253  -6.564  -6.130  0.34 38.55 ?  163 LYS   A HZ3  1 
ATOM   3524 N N    . LEU   A 1 164 ? 5.695  -8.852  0.649   1.00 21.81 ?  164 LEU   A N    1 
ATOM   3525 C CA   . LEU   A 1 164 ? 6.783  -9.821  0.783   1.00 21.22 ?  164 LEU   A CA   1 
ATOM   3526 C C    . LEU   A 1 164 ? 6.362  -10.998 1.650   1.00 21.85 ?  164 LEU   A C    1 
ATOM   3527 O O    . LEU   A 1 164 ? 6.671  -12.153 1.337   1.00 22.36 ?  164 LEU   A O    1 
ATOM   3528 C CB   . LEU   A 1 164 ? 8.004  -9.142  1.398   1.00 20.76 ?  164 LEU   A CB   1 
ATOM   3529 C CG   . LEU   A 1 164 ? 8.762  -8.119  0.551   1.00 20.92 ?  164 LEU   A CG   1 
ATOM   3530 C CD1  . LEU   A 1 164 ? 9.690  -7.293  1.430   1.00 20.93 ?  164 LEU   A CD1  1 
ATOM   3531 C CD2  . LEU   A 1 164 ? 9.549  -8.810  -0.546  1.00 21.08 ?  164 LEU   A CD2  1 
ATOM   3532 H H    A LEU   A 1 164 ? 5.845  -8.093  1.022   0.66 26.15 ?  164 LEU   A H    1 
ATOM   3533 H H    B LEU   A 1 164 ? 5.872  -8.072  0.963   0.34 26.15 ?  164 LEU   A H    1 
ATOM   3534 H HA   . LEU   A 1 164 ? 7.021  -10.159 -0.094  1.00 25.44 ?  164 LEU   A HA   1 
ATOM   3535 H HB2  . LEU   A 1 164 ? 7.716  -8.686  2.200   1.00 24.89 ?  164 LEU   A HB2  1 
ATOM   3536 H HB3  . LEU   A 1 164 ? 8.638  -9.836  1.633   1.00 24.89 ?  164 LEU   A HB3  1 
ATOM   3537 H HG   . LEU   A 1 164 ? 8.130  -7.515  0.134   1.00 25.08 ?  164 LEU   A HG   1 
ATOM   3538 H HD11 . LEU   A 1 164 ? 10.199 -6.685  0.875   1.00 25.09 ?  164 LEU   A HD11 1 
ATOM   3539 H HD12 . LEU   A 1 164 ? 9.158  -6.791  2.070   1.00 25.09 ?  164 LEU   A HD12 1 
ATOM   3540 H HD13 . LEU   A 1 164 ? 10.293 -7.891  1.904   1.00 25.09 ?  164 LEU   A HD13 1 
ATOM   3541 H HD21 . LEU   A 1 164 ? 10.023 -8.138  -1.065  1.00 25.27 ?  164 LEU   A HD21 1 
ATOM   3542 H HD22 . LEU   A 1 164 ? 10.183 -9.423  -0.144  1.00 25.27 ?  164 LEU   A HD22 1 
ATOM   3543 H HD23 . LEU   A 1 164 ? 8.934  -9.294  -1.118  1.00 25.27 ?  164 LEU   A HD23 1 
ATOM   3544 N N    . VAL   A 1 165 ? 5.675  -10.719 2.757   1.00 21.49 ?  165 VAL   A N    1 
ATOM   3545 C CA   . VAL   A 1 165 ? 5.204  -11.785 3.634   1.00 21.94 ?  165 VAL   A CA   1 
ATOM   3546 C C    . VAL   A 1 165 ? 4.154  -12.629 2.922   1.00 22.57 ?  165 VAL   A C    1 
ATOM   3547 O O    . VAL   A 1 165 ? 4.238  -13.862 2.892   1.00 22.87 ?  165 VAL   A O    1 
ATOM   3548 C CB   . VAL   A 1 165 ? 4.664  -11.179 4.943   1.00 22.70 ?  165 VAL   A CB   1 
ATOM   3549 C CG1  . VAL   A 1 165 ? 3.934  -12.230 5.767   1.00 23.30 ?  165 VAL   A CG1  1 
ATOM   3550 C CG2  . VAL   A 1 165 ? 5.793  -10.535 5.741   1.00 23.16 ?  165 VAL   A CG2  1 
ATOM   3551 H H    . VAL   A 1 165 ? 5.475  -9.929  3.022   1.00 25.76 ?  165 VAL   A H    1 
ATOM   3552 H HA   . VAL   A 1 165 ? 5.945  -12.365 3.863   1.00 26.31 ?  165 VAL   A HA   1 
ATOM   3553 H HB   . VAL   A 1 165 ? 4.027  -10.480 4.728   1.00 27.22 ?  165 VAL   A HB   1 
ATOM   3554 H HG11 . VAL   A 1 165 ? 3.850  -11.912 6.680   1.00 27.93 ?  165 VAL   A HG11 1 
ATOM   3555 H HG12 . VAL   A 1 165 ? 3.052  -12.372 5.387   1.00 27.93 ?  165 VAL   A HG12 1 
ATOM   3556 H HG13 . VAL   A 1 165 ? 4.443  -13.053 5.750   1.00 27.93 ?  165 VAL   A HG13 1 
ATOM   3557 H HG21 . VAL   A 1 165 ? 5.435  -10.173 6.567   1.00 27.77 ?  165 VAL   A HG21 1 
ATOM   3558 H HG22 . VAL   A 1 165 ? 6.465  -11.206 5.939   1.00 27.77 ?  165 VAL   A HG22 1 
ATOM   3559 H HG23 . VAL   A 1 165 ? 6.187  -9.821  5.213   1.00 27.77 ?  165 VAL   A HG23 1 
ATOM   3560 N N    A SER   A 1 166 ? 3.156  -11.975 2.325   0.66 22.93 ?  166 SER   A N    1 
ATOM   3561 N N    B SER   A 1 166 ? 3.163  -11.969 2.313   0.34 22.97 ?  166 SER   A N    1 
ATOM   3562 C CA   A SER   A 1 166 ? 2.037  -12.708 1.743   0.66 24.30 ?  166 SER   A CA   1 
ATOM   3563 C CA   B SER   A 1 166 ? 2.027  -12.678 1.732   0.34 23.99 ?  166 SER   A CA   1 
ATOM   3564 C C    A SER   A 1 166 ? 2.466  -13.561 0.559   0.66 24.92 ?  166 SER   A C    1 
ATOM   3565 C C    B SER   A 1 166 ? 2.427  -13.516 0.525   0.34 24.46 ?  166 SER   A C    1 
ATOM   3566 O O    A SER   A 1 166 ? 1.846  -14.599 0.291   0.66 26.47 ?  166 SER   A O    1 
ATOM   3567 O O    B SER   A 1 166 ? 1.745  -14.496 0.203   0.34 25.12 ?  166 SER   A O    1 
ATOM   3568 C CB   A SER   A 1 166 ? 0.940  -11.736 1.308   0.66 25.83 ?  166 SER   A CB   1 
ATOM   3569 C CB   B SER   A 1 166 ? 0.937  -11.682 1.333   0.34 24.97 ?  166 SER   A CB   1 
ATOM   3570 O OG   A SER   A 1 166 ? 0.439  -11.006 2.415   0.66 28.06 ?  166 SER   A OG   1 
ATOM   3571 O OG   B SER   A 1 166 ? 0.480  -10.950 2.458   0.34 26.27 ?  166 SER   A OG   1 
ATOM   3572 H H    A SER   A 1 166 ? 3.100  -11.121 2.249   0.66 27.49 ?  166 SER   A H    1 
ATOM   3573 H H    B SER   A 1 166 ? 3.126  -11.115 2.228   0.34 27.54 ?  166 SER   A H    1 
ATOM   3574 H HA   A SER   A 1 166 ? 1.656  -13.299 2.411   0.66 29.13 ?  166 SER   A HA   1 
ATOM   3575 H HA   B SER   A 1 166 ? 1.650  -13.269 2.397   0.34 28.77 ?  166 SER   A HA   1 
ATOM   3576 H HB2  A SER   A 1 166 ? 1.301  -11.118 0.653   0.66 30.98 ?  166 SER   A HB2  1 
ATOM   3577 H HB2  B SER   A 1 166 ? 1.295  -11.064 0.675   0.34 29.94 ?  166 SER   A HB2  1 
ATOM   3578 H HB3  A SER   A 1 166 ? 0.205  -12.238 0.913   0.66 30.98 ?  166 SER   A HB3  1 
ATOM   3579 H HB3  B SER   A 1 166 ? 0.185  -12.166 0.952   0.34 29.94 ?  166 SER   A HB3  1 
ATOM   3580 H HG   A SER   A 1 166 ? 1.060  -10.551 2.759   0.66 33.64 ?  166 SER   A HG   1 
ATOM   3581 H HG   B SER   A 1 166 ? 1.114  -10.509 2.790   0.34 31.51 ?  166 SER   A HG   1 
ATOM   3582 N N    . SER   A 1 167 ? 3.507  -13.144 -0.160  1.00 24.77 ?  167 SER   A N    1 
ATOM   3583 C CA   . SER   A 1 167 ? 3.962  -13.858 -1.344  1.00 25.98 ?  167 SER   A CA   1 
ATOM   3584 C C    . SER   A 1 167 ? 5.133  -14.789 -1.067  1.00 27.15 ?  167 SER   A C    1 
ATOM   3585 O O    . SER   A 1 167 ? 5.620  -15.440 -1.996  1.00 27.06 ?  167 SER   A O    1 
ATOM   3586 C CB   . SER   A 1 167 ? 4.345  -12.867 -2.450  1.00 26.35 ?  167 SER   A CB   1 
ATOM   3587 O OG   . SER   A 1 167 ? 5.435  -12.057 -2.044  1.00 26.56 ?  167 SER   A OG   1 
ATOM   3588 H H    A SER   A 1 167 ? 3.967  -12.436 0.020   0.66 29.70 ?  167 SER   A H    1 
ATOM   3589 H H    B SER   A 1 167 ? 3.997  -12.464 0.045   0.34 29.70 ?  167 SER   A H    1 
ATOM   3590 H HA   . SER   A 1 167 ? 3.233  -14.397 -1.681  1.00 31.16 ?  167 SER   A HA   1 
ATOM   3591 H HB2  . SER   A 1 167 ? 4.599  -13.364 -3.245  1.00 31.59 ?  167 SER   A HB2  1 
ATOM   3592 H HB3  . SER   A 1 167 ? 3.575  -12.304 -2.651  1.00 31.59 ?  167 SER   A HB3  1 
ATOM   3593 H HG   . SER   A 1 167 ? 5.215  -11.612 -1.366  1.00 31.85 ?  167 SER   A HG   1 
ATOM   3594 N N    . PHE   A 1 168 ? 5.596  -14.873 0.176   1.00 28.53 ?  168 PHE   A N    1 
ATOM   3595 C CA   . PHE   A 1 168 ? 6.776  -15.676 0.460   1.00 31.31 ?  168 PHE   A CA   1 
ATOM   3596 C C    . PHE   A 1 168 ? 6.465  -17.150 0.250   1.00 38.33 ?  168 PHE   A C    1 
ATOM   3597 O O    . PHE   A 1 168 ? 5.357  -17.612 0.532   1.00 39.23 ?  168 PHE   A O    1 
ATOM   3598 C CB   . PHE   A 1 168 ? 7.258  -15.442 1.891   1.00 28.01 ?  168 PHE   A CB   1 
ATOM   3599 C CG   . PHE   A 1 168 ? 8.548  -16.146 2.211   1.00 25.26 ?  168 PHE   A CG   1 
ATOM   3600 C CD1  . PHE   A 1 168 ? 9.719  -15.777 1.577   1.00 24.58 ?  168 PHE   A CD1  1 
ATOM   3601 C CD2  . PHE   A 1 168 ? 8.592  -17.183 3.131   1.00 23.87 ?  168 PHE   A CD2  1 
ATOM   3602 C CE1  . PHE   A 1 168 ? 10.908 -16.420 1.855   1.00 23.66 ?  168 PHE   A CE1  1 
ATOM   3603 C CE2  . PHE   A 1 168 ? 9.785  -17.830 3.415   1.00 23.60 ?  168 PHE   A CE2  1 
ATOM   3604 C CZ   . PHE   A 1 168 ? 10.941 -17.447 2.775   1.00 23.43 ?  168 PHE   A CZ   1 
ATOM   3605 H H    . PHE   A 1 168 ? 5.253  -14.483 0.859   1.00 34.21 ?  168 PHE   A H    1 
ATOM   3606 H HA   . PHE   A 1 168 ? 7.489  -15.428 -0.147  1.00 37.55 ?  168 PHE   A HA   1 
ATOM   3607 H HB2  . PHE   A 1 168 ? 7.397  -14.491 2.023   1.00 33.59 ?  168 PHE   A HB2  1 
ATOM   3608 H HB3  . PHE   A 1 168 ? 6.582  -15.763 2.505   1.00 33.59 ?  168 PHE   A HB3  1 
ATOM   3609 H HD1  . PHE   A 1 168 ? 9.705  -15.085 0.955   1.00 29.48 ?  168 PHE   A HD1  1 
ATOM   3610 H HD2  . PHE   A 1 168 ? 7.813  -17.448 3.565   1.00 28.62 ?  168 PHE   A HD2  1 
ATOM   3611 H HE1  . PHE   A 1 168 ? 11.690 -16.160 1.422   1.00 28.37 ?  168 PHE   A HE1  1 
ATOM   3612 H HE2  . PHE   A 1 168 ? 9.801  -18.525 4.035   1.00 28.29 ?  168 PHE   A HE2  1 
ATOM   3613 H HZ   . PHE   A 1 168 ? 11.743 -17.879 2.961   1.00 28.09 ?  168 PHE   A HZ   1 
ATOM   3614 N N    . LEU   A 1 169 ? 7.438  -17.887 -0.272  1.00 43.96 ?  169 LEU   A N    1 
ATOM   3615 C CA   . LEU   A 1 169 ? 7.258  -19.318 -0.463  1.00 49.57 ?  169 LEU   A CA   1 
ATOM   3616 C C    . LEU   A 1 169 ? 8.176  -20.087 0.481   1.00 51.36 ?  169 LEU   A C    1 
ATOM   3617 O O    . LEU   A 1 169 ? 7.739  -20.561 1.531   1.00 51.77 ?  169 LEU   A O    1 
ATOM   3618 C CB   . LEU   A 1 169 ? 7.526  -19.714 -1.919  1.00 52.39 ?  169 LEU   A CB   1 
ATOM   3619 C CG   . LEU   A 1 169 ? 7.075  -21.124 -2.313  1.00 54.73 ?  169 LEU   A CG   1 
ATOM   3620 C CD1  . LEU   A 1 169 ? 5.665  -21.393 -1.811  1.00 55.51 ?  169 LEU   A CD1  1 
ATOM   3621 C CD2  . LEU   A 1 169 ? 7.142  -21.305 -3.821  1.00 55.37 ?  169 LEU   A CD2  1 
ATOM   3622 O OXT  . LEU   A 1 169 ? 9.370  -20.239 0.225   1.00 51.70 -1 169 LEU   A OXT  1 
ATOM   3623 H H    . LEU   A 1 169 ? 8.205  -17.586 -0.525  1.00 52.73 ?  169 LEU   A H    1 
ATOM   3624 H HA   . LEU   A 1 169 ? 6.340  -19.541 -0.249  1.00 59.46 ?  169 LEU   A HA   1 
ATOM   3625 H HB2  . LEU   A 1 169 ? 7.063  -19.091 -2.500  1.00 62.84 ?  169 LEU   A HB2  1 
ATOM   3626 H HB3  . LEU   A 1 169 ? 8.481  -19.660 -2.081  1.00 62.84 ?  169 LEU   A HB3  1 
ATOM   3627 H HG   . LEU   A 1 169 ? 7.670  -21.775 -1.906  1.00 65.65 ?  169 LEU   A HG   1 
ATOM   3628 H HD11 . LEU   A 1 169 ? 5.293  -22.141 -2.299  1.00 66.59 ?  169 LEU   A HD11 1 
ATOM   3629 H HD12 . LEU   A 1 169 ? 5.702  -21.601 -0.863  1.00 66.59 ?  169 LEU   A HD12 1 
ATOM   3630 H HD13 . LEU   A 1 169 ? 5.124  -20.600 -1.956  1.00 66.59 ?  169 LEU   A HD13 1 
ATOM   3631 H HD21 . LEU   A 1 169 ? 6.866  -22.208 -4.044  1.00 66.43 ?  169 LEU   A HD21 1 
ATOM   3632 H HD22 . LEU   A 1 169 ? 6.547  -20.664 -4.241  1.00 66.43 ?  169 LEU   A HD22 1 
ATOM   3633 H HD23 . LEU   A 1 169 ? 8.053  -21.155 -4.117  1.00 66.43 ?  169 LEU   A HD23 1 
ATOM   3634 N N    A SER   B 1 1   ? 50.847 -9.240  -23.717 0.66 29.58 ?  1   SER   B N    1 
ATOM   3635 N N    B SER   B 1 1   ? 50.842 -9.264  -23.729 0.34 28.14 ?  1   SER   B N    1 
ATOM   3636 C CA   A SER   B 1 1   ? 51.356 -10.305 -22.830 0.66 29.46 ?  1   SER   B CA   1 
ATOM   3637 C CA   B SER   B 1 1   ? 51.335 -10.259 -22.755 0.34 28.07 ?  1   SER   B CA   1 
ATOM   3638 C C    A SER   B 1 1   ? 50.282 -11.352 -22.566 0.66 28.11 ?  1   SER   B C    1 
ATOM   3639 C C    B SER   B 1 1   ? 50.291 -11.340 -22.531 0.34 27.14 ?  1   SER   B C    1 
ATOM   3640 O O    A SER   B 1 1   ? 49.092 -11.147 -22.844 0.66 27.66 ?  1   SER   B O    1 
ATOM   3641 O O    B SER   B 1 1   ? 49.104 -11.154 -22.814 0.34 27.01 ?  1   SER   B O    1 
ATOM   3642 C CB   A SER   B 1 1   ? 51.848 -9.718  -21.509 0.66 30.27 ?  1   SER   B CB   1 
ATOM   3643 C CB   B SER   B 1 1   ? 51.674 -9.592  -21.427 0.34 28.59 ?  1   SER   B CB   1 
ATOM   3644 O OG   A SER   B 1 1   ? 50.764 -9.432  -20.648 0.66 32.03 ?  1   SER   B OG   1 
ATOM   3645 O OG   B SER   B 1 1   ? 50.514 -9.441  -20.630 0.34 29.57 ?  1   SER   B OG   1 
ATOM   3646 H H1   A SER   B 1 1   ? 50.653 -9.591  -24.509 0.66 35.47 ?  1   SER   B H1   1 
ATOM   3647 H H1   B SER   B 1 1   ? 51.539 -8.845  -24.086 0.34 33.74 ?  1   SER   B H1   1 
ATOM   3648 H H2   A SER   B 1 1   ? 50.120 -8.885  -23.356 0.66 35.47 ?  1   SER   B H2   1 
ATOM   3649 H H2   B SER   B 1 1   ? 50.383 -9.681  -24.363 0.34 33.74 ?  1   SER   B H2   1 
ATOM   3650 H H3   A SER   B 1 1   ? 51.475 -8.619  -23.809 0.66 35.47 ?  1   SER   B H3   1 
ATOM   3651 H H3   B SER   B 1 1   ? 50.322 -8.683  -23.309 0.34 33.74 ?  1   SER   B H3   1 
ATOM   3652 H HA   A SER   B 1 1   ? 52.102 -10.733 -23.271 0.66 35.33 ?  1   SER   B HA   1 
ATOM   3653 H HA   B SER   B 1 1   ? 52.133 -10.668 -23.112 0.34 33.66 ?  1   SER   B HA   1 
ATOM   3654 H HB2  A SER   B 1 1   ? 52.430 -10.364 -21.083 0.66 36.30 ?  1   SER   B HB2  1 
ATOM   3655 H HB2  B SER   B 1 1   ? 52.320 -10.145 -20.962 0.34 34.28 ?  1   SER   B HB2  1 
ATOM   3656 H HB3  A SER   B 1 1   ? 52.334 -8.898  -21.688 0.66 36.30 ?  1   SER   B HB3  1 
ATOM   3657 H HB3  B SER   B 1 1   ? 52.049 -8.715  -21.600 0.34 34.28 ?  1   SER   B HB3  1 
ATOM   3658 H HG   A SER   B 1 1   ? 51.026 -8.943  -20.017 0.66 38.41 ?  1   SER   B HG   1 
ATOM   3659 H HG   B SER   B 1 1   ? 50.662 -8.886  -20.018 0.34 35.47 ?  1   SER   B HG   1 
ATOM   3660 N N    A MET   B 1 2   ? 50.722 -12.476 -22.014 0.66 27.24 ?  2   MET   B N    1 
ATOM   3661 N N    B MET   B 1 2   ? 50.749 -12.470 -22.010 0.34 26.31 ?  2   MET   B N    1 
ATOM   3662 C CA   A MET   B 1 2   ? 49.900 -13.668 -21.860 0.66 27.20 ?  2   MET   B CA   1 
ATOM   3663 C CA   B MET   B 1 2   ? 49.923 -13.655 -21.829 0.34 25.80 ?  2   MET   B CA   1 
ATOM   3664 C C    A MET   B 1 2   ? 49.650 -13.895 -20.375 0.66 24.67 ?  2   MET   B C    1 
ATOM   3665 C C    B MET   B 1 2   ? 49.667 -13.825 -20.342 0.34 24.00 ?  2   MET   B C    1 
ATOM   3666 O O    A MET   B 1 2   ? 50.572 -14.238 -19.631 0.66 24.74 ?  2   MET   B O    1 
ATOM   3667 O O    B MET   B 1 2   ? 50.600 -14.054 -19.565 0.34 23.90 ?  2   MET   B O    1 
ATOM   3668 C CB   A MET   B 1 2   ? 50.624 -14.856 -22.484 0.66 31.17 ?  2   MET   B CB   1 
ATOM   3669 C CB   B MET   B 1 2   ? 50.650 -14.861 -22.398 0.34 27.91 ?  2   MET   B CB   1 
ATOM   3670 C CG   A MET   B 1 2   ? 49.784 -16.112 -22.640 0.66 34.74 ?  2   MET   B CG   1 
ATOM   3671 C CG   B MET   B 1 2   ? 49.754 -16.027 -22.793 0.34 29.63 ?  2   MET   B CG   1 
ATOM   3672 S SD   A MET   B 1 2   ? 50.646 -17.355 -23.619 0.66 38.16 ?  2   MET   B SD   1 
ATOM   3673 S SD   B MET   B 1 2   ? 50.624 -17.153 -23.887 0.34 31.17 ?  2   MET   B SD   1 
ATOM   3674 C CE   A MET   B 1 2   ? 51.193 -16.345 -24.991 0.66 38.54 ?  2   MET   B CE   1 
ATOM   3675 C CE   B MET   B 1 2   ? 51.589 -15.985 -24.827 0.34 31.57 ?  2   MET   B CE   1 
ATOM   3676 H H    A MET   B 1 2   ? 51.522 -12.577 -21.713 0.66 32.66 ?  2   MET   B H    1 
ATOM   3677 H H    B MET   B 1 2   ? 51.562 -12.584 -21.748 0.34 31.54 ?  2   MET   B H    1 
ATOM   3678 H HA   A MET   B 1 2   ? 49.057 -13.552 -22.323 0.66 32.61 ?  2   MET   B HA   1 
ATOM   3679 H HA   B MET   B 1 2   ? 49.088 -13.560 -22.311 0.34 30.94 ?  2   MET   B HA   1 
ATOM   3680 H HB2  A MET   B 1 2   ? 50.925 -14.573 -23.358 0.66 37.38 ?  2   MET   B HB2  1 
ATOM   3681 H HB2  B MET   B 1 2   ? 51.114 -14.508 -23.165 0.34 33.47 ?  2   MET   B HB2  1 
ATOM   3682 H HB3  A MET   B 1 2   ? 51.388 -15.093 -21.938 0.66 37.38 ?  2   MET   B HB3  1 
ATOM   3683 H HB3  B MET   B 1 2   ? 51.291 -15.208 -21.765 0.34 33.47 ?  2   MET   B HB3  1 
ATOM   3684 H HG2  A MET   B 1 2   ? 49.600 -16.486 -21.762 0.66 41.67 ?  2   MET   B HG2  1 
ATOM   3685 H HG2  B MET   B 1 2   ? 49.489 -16.517 -21.994 0.34 35.53 ?  2   MET   B HG2  1 
ATOM   3686 H HG3  A MET   B 1 2   ? 48.956 -15.899 -23.096 0.66 41.67 ?  2   MET   B HG3  1 
ATOM   3687 H HG3  B MET   B 1 2   ? 48.972 -15.707 -23.263 0.34 35.53 ?  2   MET   B HG3  1 
ATOM   3688 H HE1  A MET   B 1 2   ? 51.373 -16.916 -25.743 0.66 46.23 ?  2   MET   B HE1  1 
ATOM   3689 H HE1  B MET   B 1 2   ? 51.883 -16.436 -25.603 0.34 37.87 ?  2   MET   B HE1  1 
ATOM   3690 H HE2  A MET   B 1 2   ? 50.487 -15.713 -25.208 0.66 46.23 ?  2   MET   B HE2  1 
ATOM   3691 H HE2  B MET   B 1 2   ? 51.025 -15.227 -25.073 0.34 37.87 ?  2   MET   B HE2  1 
ATOM   3692 H HE3  A MET   B 1 2   ? 51.999 -15.861 -24.737 0.66 46.23 ?  2   MET   B HE3  1 
ATOM   3693 H HE3  B MET   B 1 2   ? 52.358 -15.681 -24.302 0.34 37.87 ?  2   MET   B HE3  1 
ATOM   3694 N N    . VAL   B 1 3   ? 48.405 -13.690 -19.947 1.00 22.51 ?  3   VAL   B N    1 
ATOM   3695 C CA   . VAL   B 1 3   ? 47.985 -13.934 -18.576 1.00 21.15 ?  3   VAL   B CA   1 
ATOM   3696 C C    . VAL   B 1 3   ? 46.748 -14.820 -18.607 1.00 19.16 ?  3   VAL   B C    1 
ATOM   3697 O O    . VAL   B 1 3   ? 46.019 -14.883 -19.600 1.00 19.83 ?  3   VAL   B O    1 
ATOM   3698 C CB   . VAL   B 1 3   ? 47.703 -12.628 -17.799 1.00 22.60 ?  3   VAL   B CB   1 
ATOM   3699 C CG1  . VAL   B 1 3   ? 48.969 -11.770 -17.696 1.00 23.29 ?  3   VAL   B CG1  1 
ATOM   3700 C CG2  . VAL   B 1 3   ? 46.567 -11.855 -18.453 1.00 23.34 ?  3   VAL   B CG2  1 
ATOM   3701 H H    A VAL   B 1 3   ? 47.773 -13.409 -20.457 0.66 26.99 ?  3   VAL   B H    1 
ATOM   3702 H H    B VAL   B 1 3   ? 47.767 -13.445 -20.469 0.34 26.99 ?  3   VAL   B H    1 
ATOM   3703 H HA   . VAL   B 1 3   ? 48.684 -14.415 -18.107 1.00 25.36 ?  3   VAL   B HA   1 
ATOM   3704 H HB   . VAL   B 1 3   ? 47.429 -12.859 -16.896 1.00 27.09 ?  3   VAL   B HB   1 
ATOM   3705 H HG11 . VAL   B 1 3   ? 48.761 -10.967 -17.193 1.00 27.93 ?  3   VAL   B HG11 1 
ATOM   3706 H HG12 . VAL   B 1 3   ? 49.657 -12.279 -17.238 1.00 27.93 ?  3   VAL   B HG12 1 
ATOM   3707 H HG13 . VAL   B 1 3   ? 49.264 -11.539 -18.588 1.00 27.93 ?  3   VAL   B HG13 1 
ATOM   3708 H HG21 . VAL   B 1 3   ? 46.520 -10.974 -18.057 1.00 27.98 ?  3   VAL   B HG21 1 
ATOM   3709 H HG22 . VAL   B 1 3   ? 46.738 -11.788 -19.403 1.00 27.98 ?  3   VAL   B HG22 1 
ATOM   3710 H HG23 . VAL   B 1 3   ? 45.734 -12.332 -18.299 1.00 27.98 ?  3   VAL   B HG23 1 
ATOM   3711 N N    . ASN   B 1 4   ? 46.519 -15.515 -17.498 1.00 17.17 ?  4   ASN   B N    1 
ATOM   3712 C CA   . ASN   B 1 4   ? 45.382 -16.425 -17.379 1.00 16.11 ?  4   ASN   B CA   1 
ATOM   3713 C C    . ASN   B 1 4   ? 45.330 -17.393 -18.560 1.00 16.44 ?  4   ASN   B C    1 
ATOM   3714 O O    . ASN   B 1 4   ? 44.271 -17.656 -19.126 1.00 17.18 ?  4   ASN   B O    1 
ATOM   3715 C CB   . ASN   B 1 4   ? 44.066 -15.656 -17.228 1.00 15.59 ?  4   ASN   B CB   1 
ATOM   3716 C CG   . ASN   B 1 4   ? 44.012 -14.847 -15.940 1.00 14.74 ?  4   ASN   B CG   1 
ATOM   3717 O OD1  . ASN   B 1 4   ? 44.307 -15.354 -14.862 1.00 14.44 ?  4   ASN   B OD1  1 
ATOM   3718 N ND2  . ASN   B 1 4   ? 43.654 -13.575 -16.054 1.00 15.72 ?  4   ASN   B ND2  1 
ATOM   3719 H H    . ASN   B 1 4   ? 47.017 -15.485 -16.800 1.00 20.58 ?  4   ASN   B H    1 
ATOM   3720 H HA   . ASN   B 1 4   ? 45.504 -16.954 -16.576 1.00 19.31 ?  4   ASN   B HA   1 
ATOM   3721 H HB2  . ASN   B 1 4   ? 43.970 -15.043 -17.974 1.00 18.69 ?  4   ASN   B HB2  1 
ATOM   3722 H HB3  . ASN   B 1 4   ? 43.330 -16.288 -17.222 1.00 18.69 ?  4   ASN   B HB3  1 
ATOM   3723 H HD21 . ASN   B 1 4   ? 43.606 -13.077 -15.352 1.00 18.85 ?  4   ASN   B HD21 1 
ATOM   3724 H HD22 . ASN   B 1 4   ? 43.455 -13.248 -16.824 1.00 18.85 ?  4   ASN   B HD22 1 
ATOM   3725 N N    . SER   B 1 5   ? 46.491 -17.926 -18.937 1.00 17.53 ?  5   SER   B N    1 
ATOM   3726 C CA   . SER   B 1 5   ? 46.588 -18.851 -20.066 1.00 19.18 ?  5   SER   B CA   1 
ATOM   3727 C C    . SER   B 1 5   ? 46.566 -20.283 -19.540 1.00 20.93 ?  5   SER   B C    1 
ATOM   3728 O O    . SER   B 1 5   ? 47.575 -20.982 -19.486 1.00 23.34 ?  5   SER   B O    1 
ATOM   3729 C CB   . SER   B 1 5   ? 47.841 -18.563 -20.890 1.00 20.47 ?  5   SER   B CB   1 
ATOM   3730 O OG   . SER   B 1 5   ? 49.018 -18.797 -20.138 1.00 23.61 ?  5   SER   B OG   1 
ATOM   3731 H H    . SER   B 1 5   ? 47.247 -17.770 -18.553 1.00 21.02 ?  5   SER   B H    1 
ATOM   3732 H HA   . SER   B 1 5   ? 45.818 -18.733 -20.641 1.00 22.99 ?  5   SER   B HA   1 
ATOM   3733 H HB2  . SER   B 1 5   ? 47.839 -19.139 -21.674 1.00 24.55 ?  5   SER   B HB2  1 
ATOM   3734 H HB3  . SER   B 1 5   ? 47.812 -17.635 -21.166 1.00 24.55 ?  5   SER   B HB3  1 
ATOM   3735 H HG   . SER   B 1 5   ? 49.060 -19.608 -19.927 1.00 28.31 ?  5   SER   B HG   1 
ATOM   3736 N N    . PHE   B 1 6   ? 45.376 -20.693 -19.119 1.00 21.46 ?  6   PHE   B N    1 
ATOM   3737 C CA   . PHE   B 1 6   ? 45.154 -22.037 -18.610 1.00 21.17 ?  6   PHE   B CA   1 
ATOM   3738 C C    . PHE   B 1 6   ? 45.070 -23.005 -19.778 1.00 24.25 ?  6   PHE   B C    1 
ATOM   3739 O O    . PHE   B 1 6   ? 44.414 -22.716 -20.783 1.00 26.47 ?  6   PHE   B O    1 
ATOM   3740 C CB   . PHE   B 1 6   ? 43.858 -22.073 -17.800 1.00 19.46 ?  6   PHE   B CB   1 
ATOM   3741 C CG   . PHE   B 1 6   ? 43.893 -21.222 -16.562 1.00 17.79 ?  6   PHE   B CG   1 
ATOM   3742 C CD1  . PHE   B 1 6   ? 44.402 -21.724 -15.381 1.00 16.52 ?  6   PHE   B CD1  1 
ATOM   3743 C CD2  . PHE   B 1 6   ? 43.416 -19.918 -16.583 1.00 17.09 ?  6   PHE   B CD2  1 
ATOM   3744 C CE1  . PHE   B 1 6   ? 44.432 -20.943 -14.235 1.00 16.11 ?  6   PHE   B CE1  1 
ATOM   3745 C CE2  . PHE   B 1 6   ? 43.448 -19.130 -15.447 1.00 17.69 ?  6   PHE   B CE2  1 
ATOM   3746 C CZ   . PHE   B 1 6   ? 43.962 -19.636 -14.276 1.00 16.35 ?  6   PHE   B CZ   1 
ATOM   3747 H H    . PHE   B 1 6   ? 44.672 -20.207 -19.121 1.00 25.73 ?  6   PHE   B H    1 
ATOM   3748 H HA   . PHE   B 1 6   ? 45.886 -22.304 -18.038 1.00 25.38 ?  6   PHE   B HA   1 
ATOM   3749 H HB2  . PHE   B 1 6   ? 43.129 -21.755 -18.359 1.00 23.33 ?  6   PHE   B HB2  1 
ATOM   3750 H HB3  . PHE   B 1 6   ? 43.681 -22.988 -17.526 1.00 23.33 ?  6   PHE   B HB3  1 
ATOM   3751 H HD1  . PHE   B 1 6   ? 44.730 -22.595 -15.352 1.00 19.80 ?  6   PHE   B HD1  1 
ATOM   3752 H HD2  . PHE   B 1 6   ? 43.067 -19.571 -17.373 1.00 20.49 ?  6   PHE   B HD2  1 
ATOM   3753 H HE1  . PHE   B 1 6   ? 44.787 -21.284 -13.445 1.00 19.31 ?  6   PHE   B HE1  1 
ATOM   3754 H HE2  . PHE   B 1 6   ? 43.122 -18.260 -15.474 1.00 21.21 ?  6   PHE   B HE2  1 
ATOM   3755 H HZ   . PHE   B 1 6   ? 43.982 -19.114 -13.508 1.00 19.59 ?  6   PHE   B HZ   1 
ATOM   3756 N N    . SER   B 1 7   ? 45.750 -24.144 -19.653 1.00 25.52 ?  7   SER   B N    1 
ATOM   3757 C CA   . SER   B 1 7   ? 45.823 -25.122 -20.728 1.00 28.47 ?  7   SER   B CA   1 
ATOM   3758 C C    . SER   B 1 7   ? 45.762 -26.530 -20.154 1.00 27.57 ?  7   SER   B C    1 
ATOM   3759 O O    . SER   B 1 7   ? 46.365 -26.817 -19.116 1.00 28.60 ?  7   SER   B O    1 
ATOM   3760 C CB   . SER   B 1 7   ? 47.113 -24.947 -21.541 1.00 31.73 ?  7   SER   B CB   1 
ATOM   3761 O OG   . SER   B 1 7   ? 47.091 -25.748 -22.708 1.00 33.94 ?  7   SER   B OG   1 
ATOM   3762 H H    . SER   B 1 7   ? 46.189 -24.372 -18.945 1.00 30.60 ?  7   SER   B H    1 
ATOM   3763 H HA   . SER   B 1 7   ? 45.071 -25.007 -21.324 1.00 34.14 ?  7   SER   B HA   1 
ATOM   3764 H HB2  . SER   B 1 7   ? 47.199 -24.014 -21.800 1.00 38.05 ?  7   SER   B HB2  1 
ATOM   3765 H HB3  . SER   B 1 7   ? 47.872 -25.207 -20.994 1.00 38.05 ?  7   SER   B HB3  1 
ATOM   3766 H HG   . SER   B 1 7   ? 47.802 -25.641 -23.145 1.00 40.71 ?  7   SER   B HG   1 
ATOM   3767 N N    . GLY   B 1 8   ? 45.027 -27.404 -20.837 1.00 27.42 ?  8   GLY   B N    1 
ATOM   3768 C CA   . GLY   B 1 8   ? 44.984 -28.798 -20.460 1.00 26.56 ?  8   GLY   B CA   1 
ATOM   3769 C C    . GLY   B 1 8   ? 44.058 -29.125 -19.318 1.00 24.90 ?  8   GLY   B C    1 
ATOM   3770 O O    . GLY   B 1 8   ? 44.206 -30.191 -18.707 1.00 26.40 ?  8   GLY   B O    1 
ATOM   3771 H H    . GLY   B 1 8   ? 44.549 -27.201 -21.518 1.00 32.88 ?  8   GLY   B H    1 
ATOM   3772 H HA2  . GLY   B 1 8   ? 44.703 -29.318 -21.224 1.00 31.84 ?  8   GLY   B HA2  1 
ATOM   3773 H HA3  . GLY   B 1 8   ? 45.874 -29.084 -20.206 1.00 31.84 ?  8   GLY   B HA3  1 
ATOM   3774 N N    . TYR   B 1 9   ? 43.086 -28.265 -19.024 1.00 22.77 ?  9   TYR   B N    1 
ATOM   3775 C CA   . TYR   B 1 9   ? 42.140 -28.543 -17.956 1.00 20.85 ?  9   TYR   B CA   1 
ATOM   3776 C C    . TYR   B 1 9   ? 40.955 -29.339 -18.471 1.00 20.59 ?  9   TYR   B C    1 
ATOM   3777 O O    . TYR   B 1 9   ? 40.532 -29.197 -19.623 1.00 22.62 ?  9   TYR   B O    1 
ATOM   3778 C CB   . TYR   B 1 9   ? 41.635 -27.258 -17.305 1.00 19.97 ?  9   TYR   B CB   1 
ATOM   3779 C CG   . TYR   B 1 9   ? 42.663 -26.634 -16.395 1.00 19.15 ?  9   TYR   B CG   1 
ATOM   3780 C CD1  . TYR   B 1 9   ? 43.743 -25.945 -16.918 1.00 19.69 ?  9   TYR   B CD1  1 
ATOM   3781 C CD2  . TYR   B 1 9   ? 42.570 -26.756 -15.016 1.00 18.27 ?  9   TYR   B CD2  1 
ATOM   3782 C CE1  . TYR   B 1 9   ? 44.702 -25.387 -16.095 1.00 19.87 ?  9   TYR   B CE1  1 
ATOM   3783 C CE2  . TYR   B 1 9   ? 43.525 -26.198 -14.182 1.00 18.72 ?  9   TYR   B CE2  1 
ATOM   3784 C CZ   . TYR   B 1 9   ? 44.589 -25.508 -14.729 1.00 19.65 ?  9   TYR   B CZ   1 
ATOM   3785 O OH   . TYR   B 1 9   ? 45.546 -24.961 -13.912 1.00 20.54 ?  9   TYR   B OH   1 
ATOM   3786 H H    . TYR   B 1 9   ? 42.933 -27.528 -19.444 1.00 27.30 ?  9   TYR   B H    1 
ATOM   3787 H HA   . TYR   B 1 9   ? 42.571 -29.073 -17.276 1.00 25.00 ?  9   TYR   B HA   1 
ATOM   3788 H HB2  . TYR   B 1 9   ? 41.396 -26.614 -17.992 1.00 23.94 ?  9   TYR   B HB2  1 
ATOM   3789 H HB3  . TYR   B 1 9   ? 40.857 -27.479 -16.771 1.00 23.94 ?  9   TYR   B HB3  1 
ATOM   3790 H HD1  . TYR   B 1 9   ? 43.820 -25.859 -17.843 1.00 23.61 ?  9   TYR   B HD1  1 
ATOM   3791 H HD2  . TYR   B 1 9   ? 41.846 -27.227 -14.647 1.00 21.90 ?  9   TYR   B HD2  1 
ATOM   3792 H HE1  . TYR   B 1 9   ? 45.413 -24.927 -16.465 1.00 23.82 ?  9   TYR   B HE1  1 
ATOM   3793 H HE2  . TYR   B 1 9   ? 43.439 -26.295 -13.261 1.00 22.45 ?  9   TYR   B HE2  1 
ATOM   3794 H HH   . TYR   B 1 9   ? 46.123 -24.580 -14.378 1.00 24.62 ?  9   TYR   B HH   1 
ATOM   3795 N N    . LEU   B 1 10  ? 40.439 -30.197 -17.598 1.00 18.74 ?  10  LEU   B N    1 
ATOM   3796 C CA   . LEU   B 1 10  ? 39.231 -30.959 -17.855 1.00 18.61 ?  10  LEU   B CA   1 
ATOM   3797 C C    . LEU   B 1 10  ? 38.048 -30.186 -17.291 1.00 18.16 ?  10  LEU   B C    1 
ATOM   3798 O O    . LEU   B 1 10  ? 38.068 -29.773 -16.129 1.00 17.95 ?  10  LEU   B O    1 
ATOM   3799 C CB   . LEU   B 1 10  ? 39.338 -32.321 -17.170 1.00 19.59 ?  10  LEU   B CB   1 
ATOM   3800 C CG   . LEU   B 1 10  ? 38.199 -33.292 -17.467 1.00 21.42 ?  10  LEU   B CG   1 
ATOM   3801 C CD1  . LEU   B 1 10  ? 38.315 -33.822 -18.889 1.00 22.77 ?  10  LEU   B CD1  1 
ATOM   3802 C CD2  . LEU   B 1 10  ? 38.170 -34.428 -16.457 1.00 22.57 ?  10  LEU   B CD2  1 
ATOM   3803 H H    . LEU   B 1 10  ? 40.776 -30.358 -16.819 1.00 22.47 ?  10  LEU   B H    1 
ATOM   3804 H HA   . LEU   B 1 10  ? 39.103 -31.090 -18.804 1.00 22.31 ?  10  LEU   B HA   1 
ATOM   3805 H HB2  . LEU   B 1 10  ? 40.164 -32.746 -17.454 1.00 23.49 ?  10  LEU   B HB2  1 
ATOM   3806 H HB3  . LEU   B 1 10  ? 39.361 -32.188 -16.207 1.00 23.49 ?  10  LEU   B HB3  1 
ATOM   3807 H HG   . LEU   B 1 10  ? 37.357 -32.817 -17.398 1.00 25.68 ?  10  LEU   B HG   1 
ATOM   3808 H HD11 . LEU   B 1 10  ? 37.611 -34.472 -19.042 1.00 27.30 ?  10  LEU   B HD11 1 
ATOM   3809 H HD12 . LEU   B 1 10  ? 38.223 -33.083 -19.510 1.00 27.30 ?  10  LEU   B HD12 1 
ATOM   3810 H HD13 . LEU   B 1 10  ? 39.182 -34.242 -18.999 1.00 27.30 ?  10  LEU   B HD13 1 
ATOM   3811 H HD21 . LEU   B 1 10  ? 37.439 -35.024 -16.678 1.00 27.06 ?  10  LEU   B HD21 1 
ATOM   3812 H HD22 . LEU   B 1 10  ? 39.012 -34.902 -16.495 1.00 27.06 ?  10  LEU   B HD22 1 
ATOM   3813 H HD23 . LEU   B 1 10  ? 38.037 -34.053 -15.572 1.00 27.06 ?  10  LEU   B HD23 1 
ATOM   3814 N N    . LYS   B 1 11  ? 37.021 -30.003 -18.110 1.00 19.16 ?  11  LYS   B N    1 
ATOM   3815 C CA   . LYS   B 1 11  ? 35.821 -29.295 -17.691 1.00 21.39 ?  11  LYS   B CA   1 
ATOM   3816 C C    . LYS   B 1 11  ? 34.956 -30.225 -16.843 1.00 20.44 ?  11  LYS   B C    1 
ATOM   3817 O O    . LYS   B 1 11  ? 34.588 -31.318 -17.289 1.00 22.29 ?  11  LYS   B O    1 
ATOM   3818 C CB   . LYS   B 1 11  ? 35.065 -28.833 -18.936 1.00 25.80 ?  11  LYS   B CB   1 
ATOM   3819 C CG   . LYS   B 1 11  ? 33.927 -27.859 -18.690 1.00 29.96 ?  11  LYS   B CG   1 
ATOM   3820 C CD   . LYS   B 1 11  ? 33.192 -27.559 -19.993 1.00 33.20 ?  11  LYS   B CD   1 
ATOM   3821 C CE   . LYS   B 1 11  ? 32.190 -26.429 -19.833 1.00 35.51 ?  11  LYS   B CE   1 
ATOM   3822 N NZ   . LYS   B 1 11  ? 32.859 -25.114 -19.628 1.00 36.77 ?  11  LYS   B NZ   1 
ATOM   3823 H H    . LYS   B 1 11  ? 36.986 -30.293 -18.922 1.00 22.97 ?  11  LYS   B H    1 
ATOM   3824 H HA   . LYS   B 1 11  ? 36.062 -28.519 -17.164 1.00 25.65 ?  11  LYS   B HA   1 
ATOM   3825 H HB2  . LYS   B 1 11  ? 35.695 -28.394 -19.532 1.00 30.93 ?  11  LYS   B HB2  1 
ATOM   3826 H HB3  . LYS   B 1 11  ? 34.690 -29.609 -19.378 1.00 30.93 ?  11  LYS   B HB3  1 
ATOM   3827 H HG2  . LYS   B 1 11  ? 33.297 -28.250 -18.066 1.00 35.92 ?  11  LYS   B HG2  1 
ATOM   3828 H HG3  . LYS   B 1 11  ? 34.282 -27.028 -18.340 1.00 35.92 ?  11  LYS   B HG3  1 
ATOM   3829 H HD2  . LYS   B 1 11  ? 33.838 -27.299 -20.670 1.00 39.82 ?  11  LYS   B HD2  1 
ATOM   3830 H HD3  . LYS   B 1 11  ? 32.712 -28.353 -20.278 1.00 39.82 ?  11  LYS   B HD3  1 
ATOM   3831 H HE2  . LYS   B 1 11  ? 31.645 -26.369 -20.634 1.00 42.59 ?  11  LYS   B HE2  1 
ATOM   3832 H HE3  . LYS   B 1 11  ? 31.631 -26.612 -19.063 1.00 42.59 ?  11  LYS   B HE3  1 
ATOM   3833 H HZ1  . LYS   B 1 11  ? 32.249 -24.471 -19.548 1.00 44.10 ?  11  LYS   B HZ1  1 
ATOM   3834 H HZ2  . LYS   B 1 11  ? 33.355 -25.137 -18.890 1.00 44.10 ?  11  LYS   B HZ2  1 
ATOM   3835 H HZ3  . LYS   B 1 11  ? 33.384 -24.929 -20.324 1.00 44.10 ?  11  LYS   B HZ3  1 
ATOM   3836 N N    . LEU   B 1 12  ? 34.637 -29.798 -15.621 1.00 18.64 ?  12  LEU   B N    1 
ATOM   3837 C CA   . LEU   B 1 12  ? 33.674 -30.498 -14.777 1.00 18.12 ?  12  LEU   B CA   1 
ATOM   3838 C C    . LEU   B 1 12  ? 32.285 -29.885 -14.864 1.00 17.97 ?  12  LEU   B C    1 
ATOM   3839 O O    . LEU   B 1 12  ? 31.296 -30.600 -15.034 1.00 18.41 ?  12  LEU   B O    1 
ATOM   3840 C CB   . LEU   B 1 12  ? 34.139 -30.512 -13.317 1.00 17.45 ?  12  LEU   B CB   1 
ATOM   3841 C CG   . LEU   B 1 12  ? 35.480 -31.189 -13.057 1.00 17.66 ?  12  LEU   B CG   1 
ATOM   3842 C CD1  . LEU   B 1 12  ? 35.845 -31.122 -11.582 1.00 17.90 ?  12  LEU   B CD1  1 
ATOM   3843 C CD2  . LEU   B 1 12  ? 35.457 -32.631 -13.545 1.00 18.33 ?  12  LEU   B CD2  1 
ATOM   3844 H H    . LEU   B 1 12  ? 34.967 -29.091 -15.254 1.00 22.34 ?  12  LEU   B H    1 
ATOM   3845 H HA   . LEU   B 1 12  ? 33.603 -31.416 -15.077 1.00 21.72 ?  12  LEU   B HA   1 
ATOM   3846 H HB2  . LEU   B 1 12  ? 34.205 -29.596 -13.007 1.00 20.92 ?  12  LEU   B HB2  1 
ATOM   3847 H HB3  . LEU   B 1 12  ? 33.470 -30.981 -12.788 1.00 20.92 ?  12  LEU   B HB3  1 
ATOM   3848 H HG   . LEU   B 1 12  ? 36.167 -30.715 -13.554 1.00 21.17 ?  12  LEU   B HG   1 
ATOM   3849 H HD11 . LEU   B 1 12  ? 36.706 -31.553 -11.448 1.00 21.45 ?  12  LEU   B HD11 1 
ATOM   3850 H HD12 . LEU   B 1 12  ? 35.901 -30.190 -11.309 1.00 21.45 ?  12  LEU   B HD12 1 
ATOM   3851 H HD13 . LEU   B 1 12  ? 35.165 -31.576 -11.063 1.00 21.45 ?  12  LEU   B HD13 1 
ATOM   3852 H HD21 . LEU   B 1 12  ? 36.250 -33.082 -13.223 1.00 21.97 ?  12  LEU   B HD21 1 
ATOM   3853 H HD22 . LEU   B 1 12  ? 34.661 -33.064 -13.200 1.00 21.97 ?  12  LEU   B HD22 1 
ATOM   3854 H HD23 . LEU   B 1 12  ? 35.442 -32.632 -14.515 1.00 21.97 ?  12  LEU   B HD23 1 
ATOM   3855 N N    . THR   B 1 13  ? 32.198 -28.568 -14.749 1.00 17.99 ?  13  THR   B N    1 
ATOM   3856 C CA   . THR   B 1 13  ? 30.975 -27.815 -14.958 1.00 17.83 ?  13  THR   B CA   1 
ATOM   3857 C C    . THR   B 1 13  ? 31.317 -26.619 -15.841 1.00 20.18 ?  13  THR   B C    1 
ATOM   3858 O O    . THR   B 1 13  ? 32.467 -26.428 -16.253 1.00 20.85 ?  13  THR   B O    1 
ATOM   3859 C CB   . THR   B 1 13  ? 30.379 -27.331 -13.632 1.00 17.46 ?  13  THR   B CB   1 
ATOM   3860 O OG1  . THR   B 1 13  ? 31.230 -26.315 -13.084 1.00 17.08 ?  13  THR   B OG1  1 
ATOM   3861 C CG2  . THR   B 1 13  ? 30.244 -28.482 -12.640 1.00 18.40 ?  13  THR   B CG2  1 
ATOM   3862 H H    . THR   B 1 13  ? 32.866 -28.067 -14.536 1.00 21.57 ?  13  THR   B H    1 
ATOM   3863 H HA   . THR   B 1 13  ? 30.319 -28.372 -15.407 1.00 21.38 ?  13  THR   B HA   1 
ATOM   3864 H HB   . THR   B 1 13  ? 29.488 -26.965 -13.788 1.00 20.92 ?  13  THR   B HB   1 
ATOM   3865 H HG1  . THR   B 1 13  ? 30.930 -25.556 -13.286 1.00 20.47 ?  13  THR   B HG1  1 
ATOM   3866 H HG21 . THR   B 1 13  ? 29.739 -28.197 -11.861 1.00 22.06 ?  13  THR   B HG21 1 
ATOM   3867 H HG22 . THR   B 1 13  ? 29.779 -29.227 -13.056 1.00 22.06 ?  13  THR   B HG22 1 
ATOM   3868 H HG23 . THR   B 1 13  ? 31.121 -28.779 -12.356 1.00 22.06 ?  13  THR   B HG23 1 
ATOM   3869 N N    A ASP   B 1 14  ? 30.309 -25.793 -16.117 0.66 21.31 ?  14  ASP   B N    1 
ATOM   3870 N N    B ASP   B 1 14  ? 30.312 -25.786 -16.116 0.34 21.18 ?  14  ASP   B N    1 
ATOM   3871 C CA   A ASP   B 1 14  ? 30.533 -24.636 -16.975 0.66 22.92 ?  14  ASP   B CA   1 
ATOM   3872 C CA   B ASP   B 1 14  ? 30.528 -24.630 -16.980 0.34 22.32 ?  14  ASP   B CA   1 
ATOM   3873 C C    A ASP   B 1 14  ? 31.632 -23.730 -16.434 0.66 21.06 ?  14  ASP   B C    1 
ATOM   3874 C C    B ASP   B 1 14  ? 31.548 -23.650 -16.416 0.34 20.57 ?  14  ASP   B C    1 
ATOM   3875 O O    A ASP   B 1 14  ? 32.310 -23.051 -17.216 0.66 22.20 ?  14  ASP   B O    1 
ATOM   3876 O O    B ASP   B 1 14  ? 32.060 -22.814 -17.169 0.34 21.14 ?  14  ASP   B O    1 
ATOM   3877 C CB   A ASP   B 1 14  ? 29.235 -23.850 -17.151 0.66 26.75 ?  14  ASP   B CB   1 
ATOM   3878 C CB   B ASP   B 1 14  ? 29.215 -23.889 -17.225 0.34 25.28 ?  14  ASP   B CB   1 
ATOM   3879 C CG   A ASP   B 1 14  ? 28.256 -24.533 -18.082 0.66 30.31 ?  14  ASP   B CG   1 
ATOM   3880 C CG   B ASP   B 1 14  ? 28.317 -24.605 -18.215 0.34 27.96 ?  14  ASP   B CG   1 
ATOM   3881 O OD1  A ASP   B 1 14  ? 28.637 -25.522 -18.747 0.66 31.39 ?  14  ASP   B OD1  1 
ATOM   3882 O OD1  B ASP   B 1 14  ? 28.849 -25.308 -19.100 0.34 28.74 ?  14  ASP   B OD1  1 
ATOM   3883 O OD2  A ASP   B 1 14  ? 27.095 -24.079 -18.142 0.66 31.78 -1 14  ASP   B OD2  1 
ATOM   3884 O OD2  B ASP   B 1 14  ? 27.081 -24.467 -18.110 0.34 29.00 -1 14  ASP   B OD2  1 
ATOM   3885 H H    A ASP   B 1 14  ? 29.507 -25.870 -15.814 0.66 25.55 ?  14  ASP   B H    1 
ATOM   3886 H H    B ASP   B 1 14  ? 29.510 -25.866 -15.818 0.34 25.39 ?  14  ASP   B H    1 
ATOM   3887 H HA   A ASP   B 1 14  ? 30.818 -24.943 -17.845 0.66 27.48 ?  14  ASP   B HA   1 
ATOM   3888 H HA   B ASP   B 1 14  ? 30.858 -24.942 -17.836 0.34 26.76 ?  14  ASP   B HA   1 
ATOM   3889 H HB2  A ASP   B 1 14  ? 28.796 -23.760 -16.294 0.66 32.07 ?  14  ASP   B HB2  1 
ATOM   3890 H HB2  B ASP   B 1 14  ? 28.737 -23.810 -16.385 0.34 30.32 ?  14  ASP   B HB2  1 
ATOM   3891 H HB3  A ASP   B 1 14  ? 29.441 -22.975 -17.516 0.66 32.07 ?  14  ASP   B HB3  1 
ATOM   3892 H HB3  B ASP   B 1 14  ? 29.418 -23.002 -17.571 0.34 30.32 ?  14  ASP   B HB3  1 
ATOM   3893 N N    . ASN   B 1 15  ? 31.837 -23.709 -15.113 1.00 18.54 ?  15  ASN   B N    1 
ATOM   3894 C CA   . ASN   B 1 15  ? 32.799 -22.794 -14.506 1.00 16.08 ?  15  ASN   B CA   1 
ATOM   3895 C C    . ASN   B 1 15  ? 33.895 -23.451 -13.676 1.00 14.73 ?  15  ASN   B C    1 
ATOM   3896 O O    . ASN   B 1 15  ? 34.750 -22.728 -13.157 1.00 14.89 ?  15  ASN   B O    1 
ATOM   3897 C CB   . ASN   B 1 15  ? 32.090 -21.739 -13.642 1.00 16.29 ?  15  ASN   B CB   1 
ATOM   3898 C CG   . ASN   B 1 15  ? 31.469 -22.337 -12.398 1.00 15.78 ?  15  ASN   B CG   1 
ATOM   3899 O OD1  . ASN   B 1 15  ? 30.524 -23.131 -12.487 1.00 17.41 ?  15  ASN   B OD1  1 
ATOM   3900 N ND2  . ASN   B 1 15  ? 31.994 -21.988 -11.237 1.00 14.83 ?  15  ASN   B ND2  1 
ATOM   3901 H H    A ASN   B 1 15  ? 31.426 -24.216 -14.549 0.66 22.23 ?  15  ASN   B H    1 
ATOM   3902 H H    B ASN   B 1 15  ? 31.464 -24.251 -14.556 0.34 22.23 ?  15  ASN   B H    1 
ATOM   3903 H HA   . ASN   B 1 15  ? 33.243 -22.308 -15.210 1.00 19.27 ?  15  ASN   B HA   1 
ATOM   3904 H HB2  . ASN   B 1 15  ? 32.735 -21.064 -13.365 1.00 19.53 ?  15  ASN   B HB2  1 
ATOM   3905 H HB3  . ASN   B 1 15  ? 31.381 -21.318 -14.160 1.00 19.53 ?  15  ASN   B HB3  1 
ATOM   3906 H HD21 . ASN   B 1 15  ? 31.672 -22.296 -10.500 1.00 17.78 ?  15  ASN   B HD21 1 
ATOM   3907 H HD22 . ASN   B 1 15  ? 32.661 -21.435 -11.207 1.00 17.78 ?  15  ASN   B HD22 1 
ATOM   3908 N N    . VAL   B 1 16  ? 33.902 -24.774 -13.522 1.00 14.83 ?  16  VAL   B N    1 
ATOM   3909 C CA   . VAL   B 1 16  ? 34.904 -25.464 -12.711 1.00 14.59 ?  16  VAL   B CA   1 
ATOM   3910 C C    . VAL   B 1 16  ? 35.694 -26.402 -13.609 1.00 14.60 ?  16  VAL   B C    1 
ATOM   3911 O O    . VAL   B 1 16  ? 35.114 -27.285 -14.262 1.00 15.45 ?  16  VAL   B O    1 
ATOM   3912 C CB   . VAL   B 1 16  ? 34.277 -26.230 -11.536 1.00 14.56 ?  16  VAL   B CB   1 
ATOM   3913 C CG1  . VAL   B 1 16  ? 35.359 -26.961 -10.737 1.00 14.83 ?  16  VAL   B CG1  1 
ATOM   3914 C CG2  . VAL   B 1 16  ? 33.477 -25.280 -10.646 1.00 15.29 ?  16  VAL   B CG2  1 
ATOM   3915 H H    . VAL   B 1 16  ? 33.319 -25.302 -13.878 1.00 17.77 ?  16  VAL   B H    1 
ATOM   3916 H HA   . VAL   B 1 16  ? 35.515 -24.812 -12.343 1.00 17.48 ?  16  VAL   B HA   1 
ATOM   3917 H HB   . VAL   B 1 16  ? 33.662 -26.897 -11.883 1.00 17.45 ?  16  VAL   B HB   1 
ATOM   3918 H HG11 . VAL   B 1 16  ? 34.976 -27.262 -9.895  1.00 17.78 ?  16  VAL   B HG11 1 
ATOM   3919 H HG12 . VAL   B 1 16  ? 35.672 -27.720 -11.247 1.00 17.78 ?  16  VAL   B HG12 1 
ATOM   3920 H HG13 . VAL   B 1 16  ? 36.088 -26.346 -10.563 1.00 17.78 ?  16  VAL   B HG13 1 
ATOM   3921 H HG21 . VAL   B 1 16  ? 33.137 -25.773 -9.881  1.00 18.32 ?  16  VAL   B HG21 1 
ATOM   3922 H HG22 . VAL   B 1 16  ? 34.054 -24.563 -10.348 1.00 18.32 ?  16  VAL   B HG22 1 
ATOM   3923 H HG23 . VAL   B 1 16  ? 32.734 -24.918 -11.158 1.00 18.32 ?  16  VAL   B HG23 1 
ATOM   3924 N N    . TYR   B 1 17  ? 37.015 -26.233 -13.597 1.00 14.73 ?  17  TYR   B N    1 
ATOM   3925 C CA   . TYR   B 1 17  ? 37.957 -26.987 -14.409 1.00 15.32 ?  17  TYR   B CA   1 
ATOM   3926 C C    . TYR   B 1 17  ? 39.008 -27.604 -13.496 1.00 14.22 ?  17  TYR   B C    1 
ATOM   3927 O O    . TYR   B 1 17  ? 39.287 -27.077 -12.416 1.00 14.62 ?  17  TYR   B O    1 
ATOM   3928 C CB   . TYR   B 1 17  ? 38.667 -26.064 -15.413 1.00 17.98 ?  17  TYR   B CB   1 
ATOM   3929 C CG   . TYR   B 1 17  ? 37.744 -25.292 -16.324 1.00 21.37 ?  17  TYR   B CG   1 
ATOM   3930 C CD1  . TYR   B 1 17  ? 37.180 -24.089 -15.922 1.00 22.90 ?  17  TYR   B CD1  1 
ATOM   3931 C CD2  . TYR   B 1 17  ? 37.440 -25.767 -17.592 1.00 23.42 ?  17  TYR   B CD2  1 
ATOM   3932 C CE1  . TYR   B 1 17  ? 36.333 -23.381 -16.757 1.00 24.63 ?  17  TYR   B CE1  1 
ATOM   3933 C CE2  . TYR   B 1 17  ? 36.600 -25.067 -18.436 1.00 24.94 ?  17  TYR   B CE2  1 
ATOM   3934 C CZ   . TYR   B 1 17  ? 36.048 -23.875 -18.012 1.00 25.78 ?  17  TYR   B CZ   1 
ATOM   3935 O OH   . TYR   B 1 17  ? 35.210 -23.175 -18.848 1.00 27.14 ?  17  TYR   B OH   1 
ATOM   3936 H H    . TYR   B 1 17  ? 37.410 -25.647 -13.096 1.00 17.65 ?  17  TYR   B H    1 
ATOM   3937 H HA   . TYR   B 1 17  ? 37.494 -27.689 -14.890 1.00 18.36 ?  17  TYR   B HA   1 
ATOM   3938 H HB2  . TYR   B 1 17  ? 39.210 -25.425 -14.927 1.00 21.55 ?  17  TYR   B HB2  1 
ATOM   3939 H HB3  . TYR   B 1 17  ? 39.229 -26.610 -15.978 1.00 21.55 ?  17  TYR   B HB3  1 
ATOM   3940 H HD1  . TYR   B 1 17  ? 37.371 -23.754 -15.078 1.00 27.46 ?  17  TYR   B HD1  1 
ATOM   3941 H HD2  . TYR   B 1 17  ? 37.807 -26.570 -17.882 1.00 28.08 ?  17  TYR   B HD2  1 
ATOM   3942 H HE1  . TYR   B 1 17  ? 35.962 -22.575 -16.477 1.00 29.53 ?  17  TYR   B HE1  1 
ATOM   3943 H HE2  . TYR   B 1 17  ? 36.401 -25.398 -19.285 1.00 29.91 ?  17  TYR   B HE2  1 
ATOM   3944 H HH   . TYR   B 1 17  ? 35.118 -23.582 -19.579 1.00 32.54 ?  17  TYR   B HH   1 
ATOM   3945 N N    . ILE   B 1 18  ? 39.619 -28.704 -13.932 1.00 14.21 ?  18  ILE   B N    1 
ATOM   3946 C CA   . ILE   B 1 18  ? 40.546 -29.429 -13.071 1.00 14.42 ?  18  ILE   B CA   1 
ATOM   3947 C C    . ILE   B 1 18  ? 41.705 -29.982 -13.891 1.00 14.68 ?  18  ILE   B C    1 
ATOM   3948 O O    . ILE   B 1 18  ? 41.543 -30.381 -15.049 1.00 15.97 ?  18  ILE   B O    1 
ATOM   3949 C CB   . ILE   B 1 18  ? 39.793 -30.524 -12.265 1.00 14.82 ?  18  ILE   B CB   1 
ATOM   3950 C CG1  . ILE   B 1 18  ? 40.650 -31.062 -11.116 1.00 15.08 ?  18  ILE   B CG1  1 
ATOM   3951 C CG2  . ILE   B 1 18  ? 39.302 -31.658 -13.182 1.00 15.20 ?  18  ILE   B CG2  1 
ATOM   3952 C CD1  . ILE   B 1 18  ? 39.853 -31.865 -10.096 1.00 16.69 ?  18  ILE   B CD1  1 
ATOM   3953 H H    . ILE   B 1 18  ? 39.513 -29.047 -14.710 1.00 17.03 ?  18  ILE   B H    1 
ATOM   3954 H HA   . ILE   B 1 18  ? 40.909 -28.816 -12.419 1.00 17.28 ?  18  ILE   B HA   1 
ATOM   3955 H HB   . ILE   B 1 18  ? 39.000 -30.123 -11.869 1.00 17.76 ?  18  ILE   B HB   1 
ATOM   3956 H HG12 . ILE   B 1 18  ? 41.335 -31.638 -11.475 1.00 18.07 ?  18  ILE   B HG12 1 
ATOM   3957 H HG13 . ILE   B 1 18  ? 41.047 -30.311 -10.651 1.00 18.07 ?  18  ILE   B HG13 1 
ATOM   3958 H HG21 . ILE   B 1 18  ? 38.710 -32.243 -12.679 1.00 18.21 ?  18  ILE   B HG21 1 
ATOM   3959 H HG22 . ILE   B 1 18  ? 38.822 -31.269 -13.929 1.00 18.21 ?  18  ILE   B HG22 1 
ATOM   3960 H HG23 . ILE   B 1 18  ? 40.066 -32.159 -13.501 1.00 18.21 ?  18  ILE   B HG23 1 
ATOM   3961 H HD11 . ILE   B 1 18  ? 40.444 -32.135 -9.376  1.00 20.01 ?  18  ILE   B HD11 1 
ATOM   3962 H HD12 . ILE   B 1 18  ? 39.135 -31.313 -9.745  1.00 20.01 ?  18  ILE   B HD12 1 
ATOM   3963 H HD13 . ILE   B 1 18  ? 39.481 -32.650 -10.530 1.00 20.01 ?  18  ILE   B HD13 1 
ATOM   3964 N N    . LYS   B 1 19  ? 42.885 -30.015 -13.270 1.00 15.11 ?  19  LYS   B N    1 
ATOM   3965 C CA   . LYS   B 1 19  ? 44.094 -30.493 -13.926 1.00 15.75 ?  19  LYS   B CA   1 
ATOM   3966 C C    . LYS   B 1 19  ? 44.997 -31.175 -12.907 1.00 15.97 ?  19  LYS   B C    1 
ATOM   3967 O O    . LYS   B 1 19  ? 45.085 -30.740 -11.757 1.00 15.39 ?  19  LYS   B O    1 
ATOM   3968 C CB   . LYS   B 1 19  ? 44.856 -29.325 -14.563 1.00 17.29 ?  19  LYS   B CB   1 
ATOM   3969 C CG   . LYS   B 1 19  ? 46.051 -29.731 -15.405 1.00 19.39 ?  19  LYS   B CG   1 
ATOM   3970 C CD   . LYS   B 1 19  ? 46.752 -28.500 -15.968 1.00 21.39 ?  19  LYS   B CD   1 
ATOM   3971 C CE   . LYS   B 1 19  ? 47.939 -28.874 -16.837 1.00 23.36 ?  19  LYS   B CE   1 
ATOM   3972 N NZ   . LYS   B 1 19  ? 48.653 -27.672 -17.344 1.00 24.38 ?  19  LYS   B NZ   1 
ATOM   3973 H H    . LYS   B 1 19  ? 42.997 -29.762 -12.451 1.00 18.10 ?  19  LYS   B H    1 
ATOM   3974 H HA   . LYS   B 1 19  ? 43.850 -31.134 -14.613 1.00 18.88 ?  19  LYS   B HA   1 
ATOM   3975 H HB2  . LYS   B 1 19  ? 44.238 -28.843 -15.133 1.00 20.73 ?  19  LYS   B HB2  1 
ATOM   3976 H HB3  . LYS   B 1 19  ? 45.165 -28.742 -13.850 1.00 20.73 ?  19  LYS   B HB3  1 
ATOM   3977 H HG2  . LYS   B 1 19  ? 46.675 -30.223 -14.853 1.00 23.25 ?  19  LYS   B HG2  1 
ATOM   3978 H HG3  . LYS   B 1 19  ? 45.742 -30.281 -16.143 1.00 23.25 ?  19  LYS   B HG3  1 
ATOM   3979 H HD2  . LYS   B 1 19  ? 46.121 -27.995 -16.508 1.00 25.65 ?  19  LYS   B HD2  1 
ATOM   3980 H HD3  . LYS   B 1 19  ? 47.070 -27.954 -15.231 1.00 25.65 ?  19  LYS   B HD3  1 
ATOM   3981 H HE2  . LYS   B 1 19  ? 48.561 -29.403 -16.313 1.00 28.01 ?  19  LYS   B HE2  1 
ATOM   3982 H HE3  . LYS   B 1 19  ? 47.624 -29.387 -17.599 1.00 28.01 ?  19  LYS   B HE3  1 
ATOM   3983 H HZ1  . LYS   B 1 19  ? 49.329 -27.920 -17.869 1.00 29.23 ?  19  LYS   B HZ1  1 
ATOM   3984 H HZ2  . LYS   B 1 19  ? 48.096 -27.161 -17.814 1.00 29.23 ?  19  LYS   B HZ2  1 
ATOM   3985 H HZ3  . LYS   B 1 19  ? 48.976 -27.199 -16.663 1.00 29.23 ?  19  LYS   B HZ3  1 
ATOM   3986 N N    . ASN   B 1 20  ? 45.678 -32.234 -13.341 1.00 17.17 ?  20  ASN   B N    1 
ATOM   3987 C CA   . ASN   B 1 20  ? 46.716 -32.866 -12.530 1.00 18.18 ?  20  ASN   B CA   1 
ATOM   3988 C C    . ASN   B 1 20  ? 47.988 -32.043 -12.715 1.00 18.44 ?  20  ASN   B C    1 
ATOM   3989 O O    . ASN   B 1 20  ? 48.634 -32.115 -13.764 1.00 20.13 ?  20  ASN   B O    1 
ATOM   3990 C CB   . ASN   B 1 20  ? 46.893 -34.318 -12.967 1.00 19.95 ?  20  ASN   B CB   1 
ATOM   3991 C CG   . ASN   B 1 20  ? 48.051 -35.023 -12.276 1.00 21.57 ?  20  ASN   B CG   1 
ATOM   3992 O OD1  . ASN   B 1 20  ? 48.722 -35.866 -12.885 1.00 23.99 ?  20  ASN   B OD1  1 
ATOM   3993 N ND2  . ASN   B 1 20  ? 48.281 -34.708 -11.008 1.00 21.38 ?  20  ASN   B ND2  1 
ATOM   3994 H H    . ASN   B 1 20  ? 45.554 -32.605 -14.106 1.00 20.58 ?  20  ASN   B H    1 
ATOM   3995 H HA   . ASN   B 1 20  ? 46.449 -32.847 -11.596 1.00 21.80 ?  20  ASN   B HA   1 
ATOM   3996 H HB2  . ASN   B 1 20  ? 46.079 -34.808 -12.763 1.00 23.92 ?  20  ASN   B HB2  1 
ATOM   3997 H HB3  . ASN   B 1 20  ? 47.057 -34.337 -13.921 1.00 23.92 ?  20  ASN   B HB3  1 
ATOM   3998 H HD21 . ASN   B 1 20  ? 48.926 -35.077 -10.581 1.00 25.64 ?  20  ASN   B HD21 1 
ATOM   3999 H HD22 . ASN   B 1 20  ? 47.788 -34.118 -10.608 1.00 25.64 ?  20  ASN   B HD22 1 
ATOM   4000 N N    . ALA   B 1 21  ? 48.346 -31.244 -11.704 1.00 18.02 ?  21  ALA   B N    1 
ATOM   4001 C CA   . ALA   B 1 21  ? 49.450 -30.304 -11.849 1.00 18.64 ?  21  ALA   B CA   1 
ATOM   4002 C C    . ALA   B 1 21  ? 49.923 -29.825 -10.484 1.00 17.51 ?  21  ALA   B C    1 
ATOM   4003 O O    . ALA   B 1 21  ? 49.186 -29.857 -9.494  1.00 17.39 ?  21  ALA   B O    1 
ATOM   4004 C CB   . ALA   B 1 21  ? 49.040 -29.113 -12.714 1.00 19.79 ?  21  ALA   B CB   1 
ATOM   4005 H H    . ALA   B 1 21  ? 47.960 -31.232 -10.928 1.00 21.61 ?  21  ALA   B H    1 
ATOM   4006 H HA   . ALA   B 1 21  ? 50.185 -30.761 -12.280 1.00 22.34 ?  21  ALA   B HA   1 
ATOM   4007 H HB1  . ALA   B 1 21  ? 49.822 -28.567 -12.864 1.00 23.72 ?  21  ALA   B HB1  1 
ATOM   4008 H HB2  . ALA   B 1 21  ? 48.697 -29.447 -13.556 1.00 23.72 ?  21  ALA   B HB2  1 
ATOM   4009 H HB3  . ALA   B 1 21  ? 48.354 -28.609 -12.251 1.00 23.72 ?  21  ALA   B HB3  1 
ATOM   4010 N N    . ASP   B 1 22  ? 51.184 -29.386 -10.464 1.00 16.70 ?  22  ASP   B N    1 
ATOM   4011 C CA   . ASP   B 1 22  ? 51.805 -28.693 -9.338  1.00 16.15 ?  22  ASP   B CA   1 
ATOM   4012 C C    . ASP   B 1 22  ? 51.397 -27.223 -9.421  1.00 14.55 ?  22  ASP   B C    1 
ATOM   4013 O O    . ASP   B 1 22  ? 51.702 -26.551 -10.411 1.00 14.98 ?  22  ASP   B O    1 
ATOM   4014 C CB   . ASP   B 1 22  ? 53.322 -28.875 -9.495  1.00 17.47 ?  22  ASP   B CB   1 
ATOM   4015 C CG   . ASP   B 1 22  ? 54.159 -28.115 -8.468  1.00 19.03 ?  22  ASP   B CG   1 
ATOM   4016 O OD1  . ASP   B 1 22  ? 53.798 -26.996 -8.069  1.00 18.94 ?  22  ASP   B OD1  1 
ATOM   4017 O OD2  . ASP   B 1 22  ? 55.237 -28.634 -8.094  1.00 21.41 -1 22  ASP   B OD2  1 
ATOM   4018 H H    . ASP   B 1 22  ? 51.723 -29.483 -11.132 1.00 20.01 ?  22  ASP   B H    1 
ATOM   4019 H HA   . ASP   B 1 22  ? 51.511 -29.076 -8.495  1.00 19.36 ?  22  ASP   B HA   1 
ATOM   4020 H HB2  . ASP   B 1 22  ? 53.539 -29.812 -9.417  1.00 20.93 ?  22  ASP   B HB2  1 
ATOM   4021 H HB3  . ASP   B 1 22  ? 53.586 -28.541 -10.366 1.00 20.93 ?  22  ASP   B HB3  1 
ATOM   4022 N N    . ILE   B 1 23  ? 50.686 -26.731 -8.399  1.00 13.88 ?  23  ILE   B N    1 
ATOM   4023 C CA   . ILE   B 1 23  ? 50.100 -25.387 -8.465  1.00 13.38 ?  23  ILE   B CA   1 
ATOM   4024 C C    . ILE   B 1 23  ? 51.162 -24.297 -8.606  1.00 12.76 ?  23  ILE   B C    1 
ATOM   4025 O O    . ILE   B 1 23  ? 50.901 -23.254 -9.213  1.00 12.51 ?  23  ILE   B O    1 
ATOM   4026 C CB   . ILE   B 1 23  ? 49.167 -25.141 -7.263  1.00 13.34 ?  23  ILE   B CB   1 
ATOM   4027 C CG1  . ILE   B 1 23  ? 48.346 -23.864 -7.460  1.00 13.85 ?  23  ILE   B CG1  1 
ATOM   4028 C CG2  . ILE   B 1 23  ? 49.948 -25.116 -5.961  1.00 14.35 ?  23  ILE   B CG2  1 
ATOM   4029 C CD1  . ILE   B 1 23  ? 47.215 -23.713 -6.459  1.00 15.11 ?  23  ILE   B CD1  1 
ATOM   4030 H H    . ILE   B 1 23  ? 50.538 -27.149 -7.664  1.00 16.63 ?  23  ILE   B H    1 
ATOM   4031 H HA   . ILE   B 1 23  ? 49.551 -25.345 -9.262  1.00 16.03 ?  23  ILE   B HA   1 
ATOM   4032 H HB   . ILE   B 1 23  ? 48.546 -25.885 -7.221  1.00 15.99 ?  23  ILE   B HB   1 
ATOM   4033 H HG12 . ILE   B 1 23  ? 48.936 -23.096 -7.366  1.00 16.60 ?  23  ILE   B HG12 1 
ATOM   4034 H HG13 . ILE   B 1 23  ? 47.963 -23.871 -8.353  1.00 16.60 ?  23  ILE   B HG13 1 
ATOM   4035 H HG21 . ILE   B 1 23  ? 49.325 -25.103 -5.221  1.00 17.20 ?  23  ILE   B HG21 1 
ATOM   4036 H HG22 . ILE   B 1 23  ? 50.504 -25.911 -5.912  1.00 17.20 ?  23  ILE   B HG22 1 
ATOM   4037 H HG23 . ILE   B 1 23  ? 50.506 -24.323 -5.942  1.00 17.20 ?  23  ILE   B HG23 1 
ATOM   4038 H HD11 . ILE   B 1 23  ? 46.700 -22.925 -6.684  1.00 18.11 ?  23  ILE   B HD11 1 
ATOM   4039 H HD12 . ILE   B 1 23  ? 46.651 -24.503 -6.508  1.00 18.11 ?  23  ILE   B HD12 1 
ATOM   4040 H HD13 . ILE   B 1 23  ? 47.590 -23.628 -5.571  1.00 18.11 ?  23  ILE   B HD13 1 
ATOM   4041 N N    . VAL   B 1 24  ? 52.359 -24.502 -8.050  1.00 13.23 ?  24  VAL   B N    1 
ATOM   4042 C CA   . VAL   B 1 24  ? 53.435 -23.523 -8.217  1.00 13.73 ?  24  VAL   B CA   1 
ATOM   4043 C C    . VAL   B 1 24  ? 53.890 -23.479 -9.670  1.00 13.89 ?  24  VAL   B C    1 
ATOM   4044 O O    . VAL   B 1 24  ? 54.020 -22.403 -10.266 1.00 14.48 ?  24  VAL   B O    1 
ATOM   4045 C CB   . VAL   B 1 24  ? 54.610 -23.839 -7.271  1.00 14.76 ?  24  VAL   B CB   1 
ATOM   4046 C CG1  . VAL   B 1 24  ? 55.816 -22.958 -7.591  1.00 15.61 ?  24  VAL   B CG1  1 
ATOM   4047 C CG2  . VAL   B 1 24  ? 54.185 -23.667 -5.830  1.00 15.84 ?  24  VAL   B CG2  1 
ATOM   4048 H H    . VAL   B 1 24  ? 52.571 -25.190 -7.583  1.00 15.85 ?  24  VAL   B H    1 
ATOM   4049 H HA   . VAL   B 1 24  ? 53.097 -22.645 -7.985  1.00 16.46 ?  24  VAL   B HA   1 
ATOM   4050 H HB   . VAL   B 1 24  ? 54.875 -24.764 -7.392  1.00 17.69 ?  24  VAL   B HB   1 
ATOM   4051 H HG11 . VAL   B 1 24  ? 56.414 -22.954 -6.825  1.00 18.71 ?  24  VAL   B HG11 1 
ATOM   4052 H HG12 . VAL   B 1 24  ? 56.277 -23.324 -8.362  1.00 18.71 ?  24  VAL   B HG12 1 
ATOM   4053 H HG13 . VAL   B 1 24  ? 55.512 -22.059 -7.777  1.00 18.71 ?  24  VAL   B HG13 1 
ATOM   4054 H HG21 . VAL   B 1 24  ? 54.906 -23.955 -5.251  1.00 18.98 ?  24  VAL   B HG21 1 
ATOM   4055 H HG22 . VAL   B 1 24  ? 53.987 -22.730 -5.673  1.00 18.98 ?  24  VAL   B HG22 1 
ATOM   4056 H HG23 . VAL   B 1 24  ? 53.394 -24.205 -5.668  1.00 18.98 ?  24  VAL   B HG23 1 
ATOM   4057 N N    . GLU   B 1 25  ? 54.155 -24.651 -10.257 1.00 14.74 ?  25  GLU   B N    1 
ATOM   4058 C CA   . GLU   B 1 25  ? 54.545 -24.690 -11.661 1.00 16.44 ?  25  GLU   B CA   1 
ATOM   4059 C C    . GLU   B 1 25  ? 53.434 -24.149 -12.549 1.00 15.49 ?  25  GLU   B C    1 
ATOM   4060 O O    . GLU   B 1 25  ? 53.700 -23.430 -13.521 1.00 16.17 ?  25  GLU   B O    1 
ATOM   4061 C CB   . GLU   B 1 25  ? 54.939 -26.111 -12.054 1.00 20.79 ?  25  GLU   B CB   1 
ATOM   4062 C CG   . GLU   B 1 25  ? 56.237 -26.562 -11.402 1.00 26.94 ?  25  GLU   B CG   1 
ATOM   4063 C CD   . GLU   B 1 25  ? 57.351 -25.529 -11.500 1.00 32.60 ?  25  GLU   B CD   1 
ATOM   4064 O OE1  . GLU   B 1 25  ? 57.738 -25.169 -12.633 1.00 34.68 ?  25  GLU   B OE1  1 
ATOM   4065 O OE2  . GLU   B 1 25  ? 57.827 -25.059 -10.441 1.00 34.61 -1 25  GLU   B OE2  1 
ATOM   4066 H H    . GLU   B 1 25  ? 54.117 -25.415 -9.869  1.00 17.66 ?  25  GLU   B H    1 
ATOM   4067 H HA   . GLU   B 1 25  ? 55.304 -24.104 -11.789 1.00 19.71 ?  25  GLU   B HA   1 
ATOM   4068 H HB2  . GLU   B 1 25  ? 54.236 -26.723 -11.776 1.00 24.93 ?  25  GLU   B HB2  1 
ATOM   4069 H HB3  . GLU   B 1 25  ? 55.050 -26.153 -13.017 1.00 24.93 ?  25  GLU   B HB3  1 
ATOM   4070 H HG2  . GLU   B 1 25  ? 56.081 -26.717 -10.463 1.00 32.30 ?  25  GLU   B HG2  1 
ATOM   4071 H HG3  . GLU   B 1 25  ? 56.541 -27.372 -11.837 1.00 32.30 ?  25  GLU   B HG3  1 
ATOM   4072 N N    . GLU   B 1 26  ? 52.181 -24.463 -12.213 1.00 14.24 ?  26  GLU   B N    1 
ATOM   4073 C CA   . GLU   B 1 26  ? 51.053 -23.939 -12.976 1.00 15.05 ?  26  GLU   B CA   1 
ATOM   4074 C C    . GLU   B 1 26  ? 51.004 -22.420 -12.900 1.00 14.05 ?  26  GLU   B C    1 
ATOM   4075 O O    . GLU   B 1 26  ? 50.816 -21.745 -13.916 1.00 15.40 ?  26  GLU   B O    1 
ATOM   4076 C CB   . GLU   B 1 26  ? 49.741 -24.524 -12.452 1.00 16.99 ?  26  GLU   B CB   1 
ATOM   4077 C CG   . GLU   B 1 26  ? 49.261 -25.778 -13.162 1.00 21.38 ?  26  GLU   B CG   1 
ATOM   4078 C CD   . GLU   B 1 26  ? 48.998 -25.592 -14.658 1.00 22.61 ?  26  GLU   B CD   1 
ATOM   4079 O OE1  . GLU   B 1 26  ? 48.007 -24.947 -15.061 1.00 23.10 ?  26  GLU   B OE1  1 
ATOM   4080 O OE2  . GLU   B 1 26  ? 49.788 -26.137 -15.437 1.00 25.04 -1 26  GLU   B OE2  1 
ATOM   4081 H H    . GLU   B 1 26  ? 51.958 -24.965 -11.547 1.00 17.07 ?  26  GLU   B H    1 
ATOM   4082 H HA   . GLU   B 1 26  ? 51.152 -24.194 -13.903 1.00 18.04 ?  26  GLU   B HA   1 
ATOM   4083 H HB2  . GLU   B 1 26  ? 49.853 -24.744 -11.510 1.00 20.36 ?  26  GLU   B HB2  1 
ATOM   4084 H HB3  . GLU   B 1 26  ? 49.046 -23.849 -12.538 1.00 20.36 ?  26  GLU   B HB3  1 
ATOM   4085 H HG2  . GLU   B 1 26  ? 49.948 -26.444 -13.080 1.00 25.63 ?  26  GLU   B HG2  1 
ATOM   4086 H HG3  . GLU   B 1 26  ? 48.441 -26.074 -12.741 1.00 25.63 ?  26  GLU   B HG3  1 
ATOM   4087 N N    . ALA   B 1 27  ? 51.152 -21.864 -11.696 1.00 13.44 ?  27  ALA   B N    1 
ATOM   4088 C CA   . ALA   B 1 27  ? 51.113 -20.414 -11.551 1.00 13.59 ?  27  ALA   B CA   1 
ATOM   4089 C C    . ALA   B 1 27  ? 52.184 -19.750 -12.407 1.00 14.59 ?  27  ALA   B C    1 
ATOM   4090 O O    . ALA   B 1 27  ? 51.925 -18.743 -13.081 1.00 15.39 ?  27  ALA   B O    1 
ATOM   4091 C CB   . ALA   B 1 27  ? 51.272 -20.032 -10.080 1.00 13.46 ?  27  ALA   B CB   1 
ATOM   4092 H H    . ALA   B 1 27  ? 51.271 -22.297 -10.961 1.00 16.11 ?  27  ALA   B H    1 
ATOM   4093 H HA   . ALA   B 1 27  ? 50.252 -20.089 -11.849 1.00 16.28 ?  27  ALA   B HA   1 
ATOM   4094 H HB1  . ALA   B 1 27  ? 51.238 -19.066 -9.997  1.00 16.13 ?  27  ALA   B HB1  1 
ATOM   4095 H HB2  . ALA   B 1 27  ? 50.546 -20.431 -9.571  1.00 16.13 ?  27  ALA   B HB2  1 
ATOM   4096 H HB3  . ALA   B 1 27  ? 52.122 -20.364 -9.754  1.00 16.13 ?  27  ALA   B HB3  1 
ATOM   4097 N N    . LYS   B 1 28  ? 53.396 -20.307 -12.406 1.00 15.93 ?  28  LYS   B N    1 
ATOM   4098 C CA   . LYS   B 1 28  ? 54.475 -19.693 -13.171 1.00 18.11 ?  28  LYS   B CA   1 
ATOM   4099 C C    . LYS   B 1 28  ? 54.222 -19.776 -14.668 1.00 18.88 ?  28  LYS   B C    1 
ATOM   4100 O O    . LYS   B 1 28  ? 54.638 -18.880 -15.414 1.00 20.36 ?  28  LYS   B O    1 
ATOM   4101 C CB   . LYS   B 1 28  ? 55.826 -20.302 -12.780 1.00 20.99 ?  28  LYS   B CB   1 
ATOM   4102 C CG   . LYS   B 1 28  ? 56.233 -19.960 -11.347 1.00 24.44 ?  28  LYS   B CG   1 
ATOM   4103 C CD   . LYS   B 1 28  ? 57.671 -20.343 -11.019 1.00 28.86 ?  28  LYS   B CD   1 
ATOM   4104 C CE   . LYS   B 1 28  ? 57.795 -21.802 -10.649 1.00 32.36 ?  28  LYS   B CE   1 
ATOM   4105 N NZ   . LYS   B 1 28  ? 59.159 -22.121 -10.138 1.00 33.69 ?  28  LYS   B NZ   1 
ATOM   4106 H H    . LYS   B 1 28  ? 53.616 -21.022 -11.980 1.00 19.09 ?  28  LYS   B H    1 
ATOM   4107 H HA   . LYS   B 1 28  ? 54.512 -18.754 -12.950 1.00 21.71 ?  28  LYS   B HA   1 
ATOM   4108 H HB2  . LYS   B 1 28  ? 55.777 -21.267 -12.854 1.00 25.16 ?  28  LYS   B HB2  1 
ATOM   4109 H HB3  . LYS   B 1 28  ? 56.514 -19.959 -13.375 1.00 25.16 ?  28  LYS   B HB3  1 
ATOM   4110 H HG2  . LYS   B 1 28  ? 56.139 -19.001 -11.219 1.00 29.30 ?  28  LYS   B HG2  1 
ATOM   4111 H HG3  . LYS   B 1 28  ? 55.648 -20.433 -10.737 1.00 29.30 ?  28  LYS   B HG3  1 
ATOM   4112 H HD2  . LYS   B 1 28  ? 58.229 -20.174 -11.793 1.00 34.61 ?  28  LYS   B HD2  1 
ATOM   4113 H HD3  . LYS   B 1 28  ? 57.974 -19.809 -10.266 1.00 34.61 ?  28  LYS   B HD3  1 
ATOM   4114 H HE2  . LYS   B 1 28  ? 57.153 -22.012 -9.952  1.00 38.81 ?  28  LYS   B HE2  1 
ATOM   4115 H HE3  . LYS   B 1 28  ? 57.628 -22.348 -11.433 1.00 38.81 ?  28  LYS   B HE3  1 
ATOM   4116 H HZ1  . LYS   B 1 28  ? 59.211 -22.984 -9.926  1.00 40.41 ?  28  LYS   B HZ1  1 
ATOM   4117 H HZ2  . LYS   B 1 28  ? 59.767 -21.939 -10.762 1.00 40.41 ?  28  LYS   B HZ2  1 
ATOM   4118 H HZ3  . LYS   B 1 28  ? 59.334 -21.634 -9.414  1.00 40.41 ?  28  LYS   B HZ3  1 
ATOM   4119 N N    . LYS   B 1 29  ? 53.518 -20.812 -15.125 1.00 20.18 ?  29  LYS   B N    1 
ATOM   4120 C CA   . LYS   B 1 29  ? 53.241 -20.952 -16.550 1.00 23.08 ?  29  LYS   B CA   1 
ATOM   4121 C C    . LYS   B 1 29  ? 51.991 -20.193 -16.989 1.00 21.86 ?  29  LYS   B C    1 
ATOM   4122 O O    . LYS   B 1 29  ? 51.985 -19.586 -18.066 1.00 23.56 ?  29  LYS   B O    1 
ATOM   4123 C CB   . LYS   B 1 29  ? 53.116 -22.433 -16.916 1.00 28.39 ?  29  LYS   B CB   1 
ATOM   4124 C CG   . LYS   B 1 29  ? 52.927 -22.695 -18.400 1.00 33.40 ?  29  LYS   B CG   1 
ATOM   4125 C CD   . LYS   B 1 29  ? 53.140 -24.166 -18.737 1.00 37.38 ?  29  LYS   B CD   1 
ATOM   4126 C CE   . LYS   B 1 29  ? 52.052 -25.049 -18.144 1.00 40.29 ?  29  LYS   B CE   1 
ATOM   4127 N NZ   . LYS   B 1 29  ? 52.271 -26.489 -18.469 1.00 41.62 ?  29  LYS   B NZ   1 
ATOM   4128 H H    . LYS   B 1 29  ? 53.188 -21.445 -14.632 1.00 24.19 ?  29  LYS   B H    1 
ATOM   4129 H HA   . LYS   B 1 29  ? 53.989 -20.593 -17.042 1.00 27.68 ?  29  LYS   B HA   1 
ATOM   4130 H HB2  . LYS   B 1 29  ? 53.929 -22.887 -16.642 1.00 34.05 ?  29  LYS   B HB2  1 
ATOM   4131 H HB3  . LYS   B 1 29  ? 52.357 -22.808 -16.452 1.00 34.05 ?  29  LYS   B HB3  1 
ATOM   4132 H HG2  . LYS   B 1 29  ? 52.023 -22.452 -18.653 1.00 40.06 ?  29  LYS   B HG2  1 
ATOM   4133 H HG3  . LYS   B 1 29  ? 53.569 -22.170 -18.903 1.00 40.06 ?  29  LYS   B HG3  1 
ATOM   4134 H HD2  . LYS   B 1 29  ? 53.129 -24.278 -19.700 1.00 44.84 ?  29  LYS   B HD2  1 
ATOM   4135 H HD3  . LYS   B 1 29  ? 53.993 -24.457 -18.376 1.00 44.84 ?  29  LYS   B HD3  1 
ATOM   4136 H HE2  . LYS   B 1 29  ? 52.050 -24.955 -17.179 1.00 48.32 ?  29  LYS   B HE2  1 
ATOM   4137 H HE3  . LYS   B 1 29  ? 51.192 -24.784 -18.508 1.00 48.32 ?  29  LYS   B HE3  1 
ATOM   4138 H HZ1  . LYS   B 1 29  ? 51.622 -26.984 -18.113 1.00 49.92 ?  29  LYS   B HZ1  1 
ATOM   4139 H HZ2  . LYS   B 1 29  ? 52.271 -26.606 -19.351 1.00 49.92 ?  29  LYS   B HZ2  1 
ATOM   4140 H HZ3  . LYS   B 1 29  ? 53.053 -26.759 -18.141 1.00 49.92 ?  29  LYS   B HZ3  1 
ATOM   4141 N N    . VAL   B 1 30  ? 50.935 -20.220 -16.170 1.00 19.83 ?  30  VAL   B N    1 
ATOM   4142 C CA   . VAL   B 1 30  ? 49.642 -19.638 -16.542 1.00 20.10 ?  30  VAL   B CA   1 
ATOM   4143 C C    . VAL   B 1 30  ? 49.633 -18.124 -16.394 1.00 19.04 ?  30  VAL   B C    1 
ATOM   4144 O O    . VAL   B 1 30  ? 48.892 -17.423 -17.103 1.00 19.90 ?  30  VAL   B O    1 
ATOM   4145 C CB   . VAL   B 1 30  ? 48.538 -20.265 -15.666 1.00 21.40 ?  30  VAL   B CB   1 
ATOM   4146 C CG1  . VAL   B 1 30  ? 47.245 -19.469 -15.757 1.00 21.97 ?  30  VAL   B CG1  1 
ATOM   4147 C CG2  . VAL   B 1 30  ? 48.311 -21.722 -16.050 1.00 22.28 ?  30  VAL   B CG2  1 
ATOM   4148 H H    . VAL   B 1 30  ? 50.935 -20.594 -15.385 1.00 23.77 ?  30  VAL   B H    1 
ATOM   4149 H HA   . VAL   B 1 30  ? 49.451 -19.869 -17.464 1.00 24.10 ?  30  VAL   B HA   1 
ATOM   4150 H HB   . VAL   B 1 30  ? 48.826 -20.256 -14.740 1.00 25.65 ?  30  VAL   B HB   1 
ATOM   4151 H HG11 . VAL   B 1 30  ? 46.508 -20.053 -15.519 1.00 26.34 ?  30  VAL   B HG11 1 
ATOM   4152 H HG12 . VAL   B 1 30  ? 47.285 -18.725 -15.139 1.00 26.34 ?  30  VAL   B HG12 1 
ATOM   4153 H HG13 . VAL   B 1 30  ? 47.128 -19.156 -16.663 1.00 26.34 ?  30  VAL   B HG13 1 
ATOM   4154 H HG21 . VAL   B 1 30  ? 47.622 -22.100 -15.476 1.00 26.71 ?  30  VAL   B HG21 1 
ATOM   4155 H HG22 . VAL   B 1 30  ? 48.022 -21.765 -16.976 1.00 26.71 ?  30  VAL   B HG22 1 
ATOM   4156 H HG23 . VAL   B 1 30  ? 49.138 -22.214 -15.938 1.00 26.71 ?  30  VAL   B HG23 1 
ATOM   4157 N N    . LYS   B 1 31  ? 50.409 -17.613 -15.452 1.00 18.89 ?  31  LYS   B N    1 
ATOM   4158 C CA   . LYS   B 1 31  ? 50.444 -16.202 -15.103 1.00 19.20 ?  31  LYS   B CA   1 
ATOM   4159 C C    . LYS   B 1 31  ? 49.049 -15.722 -14.704 1.00 17.07 ?  31  LYS   B C    1 
ATOM   4160 O O    . LYS   B 1 31  ? 48.507 -14.797 -15.323 1.00 17.92 ?  31  LYS   B O    1 
ATOM   4161 C CB   . LYS   B 1 31  ? 51.076 -15.400 -16.248 1.00 22.34 ?  31  LYS   B CB   1 
ATOM   4162 C CG   . LYS   B 1 31  ? 52.520 -15.822 -16.539 1.00 26.22 ?  31  LYS   B CG   1 
ATOM   4163 C CD   . LYS   B 1 31  ? 53.086 -15.087 -17.738 1.00 30.24 ?  31  LYS   B CD   1 
ATOM   4164 C CE   . LYS   B 1 31  ? 54.571 -15.333 -17.887 1.00 33.42 ?  31  LYS   B CE   1 
ATOM   4165 N NZ   . LYS   B 1 31  ? 55.302 -14.901 -16.665 1.00 35.00 ?  31  LYS   B NZ   1 
ATOM   4166 H H    . LYS   B 1 31  ? 50.944 -18.098 -14.986 1.00 22.65 ?  31  LYS   B H    1 
ATOM   4167 H HA   . LYS   B 1 31  ? 51.009 -16.112 -14.335 1.00 23.02 ?  31  LYS   B HA   1 
ATOM   4168 H HB2  . LYS   B 1 31  ? 50.562 -15.532 -17.060 1.00 26.79 ?  31  LYS   B HB2  1 
ATOM   4169 H HB3  . LYS   B 1 31  ? 51.085 -14.466 -16.004 1.00 26.79 ?  31  LYS   B HB3  1 
ATOM   4170 H HG2  . LYS   B 1 31  ? 53.071 -15.622 -15.765 1.00 31.45 ?  31  LYS   B HG2  1 
ATOM   4171 H HG3  . LYS   B 1 31  ? 52.549 -16.776 -16.728 1.00 31.45 ?  31  LYS   B HG3  1 
ATOM   4172 H HD2  . LYS   B 1 31  ? 52.642 -15.401 -18.539 1.00 36.27 ?  31  LYS   B HD2  1 
ATOM   4173 H HD3  . LYS   B 1 31  ? 52.945 -14.137 -17.621 1.00 36.27 ?  31  LYS   B HD3  1 
ATOM   4174 H HE2  . LYS   B 1 31  ? 54.731 -16.281 -18.021 1.00 40.08 ?  31  LYS   B HE2  1 
ATOM   4175 H HE3  . LYS   B 1 31  ? 54.906 -14.824 -18.642 1.00 40.08 ?  31  LYS   B HE3  1 
ATOM   4176 H HZ1  . LYS   B 1 31  ? 56.177 -14.898 -16.819 1.00 41.97 ?  31  LYS   B HZ1  1 
ATOM   4177 H HZ2  . LYS   B 1 31  ? 55.044 -14.081 -16.433 1.00 41.97 ?  31  LYS   B HZ2  1 
ATOM   4178 H HZ3  . LYS   B 1 31  ? 55.127 -15.458 -15.993 1.00 41.97 ?  31  LYS   B HZ3  1 
ATOM   4179 N N    . PRO   B 1 32  ? 48.441 -16.323 -13.671 1.00 14.71 ?  32  PRO   B N    1 
ATOM   4180 C CA   . PRO   B 1 32  ? 47.063 -15.963 -13.313 1.00 13.79 ?  32  PRO   B CA   1 
ATOM   4181 C C    . PRO   B 1 32  ? 46.987 -14.615 -12.615 1.00 13.85 ?  32  PRO   B C    1 
ATOM   4182 O O    . PRO   B 1 32  ? 47.915 -14.195 -11.918 1.00 15.03 ?  32  PRO   B O    1 
ATOM   4183 C CB   . PRO   B 1 32  ? 46.662 -17.077 -12.342 1.00 13.94 ?  32  PRO   B CB   1 
ATOM   4184 C CG   . PRO   B 1 32  ? 47.960 -17.414 -11.659 1.00 14.66 ?  32  PRO   B CG   1 
ATOM   4185 C CD   . PRO   B 1 32  ? 49.013 -17.308 -12.729 1.00 14.73 ?  32  PRO   B CD   1 
ATOM   4186 H HA   . PRO   B 1 32  ? 46.478 -15.975 -14.093 1.00 16.53 ?  32  PRO   B HA   1 
ATOM   4187 H HB2  . PRO   B 1 32  ? 46.008 -16.745 -11.707 1.00 16.71 ?  32  PRO   B HB2  1 
ATOM   4188 H HB3  . PRO   B 1 32  ? 46.318 -17.841 -12.831 1.00 16.71 ?  32  PRO   B HB3  1 
ATOM   4189 H HG2  . PRO   B 1 32  ? 48.128 -16.775 -10.946 1.00 17.56 ?  32  PRO   B HG2  1 
ATOM   4190 H HG3  . PRO   B 1 32  ? 47.920 -18.317 -11.307 1.00 17.56 ?  32  PRO   B HG3  1 
ATOM   4191 H HD2  . PRO   B 1 32  ? 49.837 -16.966 -12.359 1.00 17.66 ?  32  PRO   B HD2  1 
ATOM   4192 H HD3  . PRO   B 1 32  ? 49.135 -18.160 -13.166 1.00 17.66 ?  32  PRO   B HD3  1 
ATOM   4193 N N    . THR   B 1 33  ? 45.835 -13.957 -12.775 1.00 13.39 ?  33  THR   B N    1 
ATOM   4194 C CA   . THR   B 1 33  ? 45.543 -12.780 -11.966 1.00 13.76 ?  33  THR   B CA   1 
ATOM   4195 C C    . THR   B 1 33  ? 45.497 -13.132 -10.486 1.00 13.33 ?  33  THR   B C    1 
ATOM   4196 O O    . THR   B 1 33  ? 45.974 -12.356 -9.644  1.00 14.20 ?  33  THR   B O    1 
ATOM   4197 C CB   . THR   B 1 33  ? 44.227 -12.144 -12.417 1.00 14.40 ?  33  THR   B CB   1 
ATOM   4198 O OG1  . THR   B 1 33  ? 44.276 -11.891 -13.824 1.00 14.41 ?  33  THR   B OG1  1 
ATOM   4199 C CG2  . THR   B 1 33  ? 43.977 -10.843 -11.670 1.00 15.82 ?  33  THR   B CG2  1 
ATOM   4200 H H    . THR   B 1 33  ? 45.212 -14.178 -13.331 1.00 16.05 ?  33  THR   B H    1 
ATOM   4201 H HA   . THR   B 1 33  ? 46.245 -12.130 -12.094 1.00 16.49 ?  33  THR   B HA   1 
ATOM   4202 H HB   . THR   B 1 33  ? 43.491 -12.754 -12.227 1.00 17.26 ?  33  THR   B HB   1 
ATOM   4203 H HG1  . THR   B 1 33  ? 43.558 -11.527 -14.077 1.00 17.27 ?  33  THR   B HG1  1 
ATOM   4204 H HG21 . THR   B 1 33  ? 43.225 -10.377 -12.062 1.00 18.96 ?  33  THR   B HG21 1 
ATOM   4205 H HG22 . THR   B 1 33  ? 43.783 -11.028 -10.737 1.00 18.96 ?  33  THR   B HG22 1 
ATOM   4206 H HG23 . THR   B 1 33  ? 44.763 -10.279 -11.725 1.00 18.96 ?  33  THR   B HG23 1 
ATOM   4207 N N    . VAL   B 1 34  ? 44.942 -14.302 -10.148 1.00 12.53 ?  34  VAL   B N    1 
ATOM   4208 C CA   . VAL   B 1 34  ? 44.739 -14.696 -8.756  1.00 11.93 ?  34  VAL   B CA   1 
ATOM   4209 C C    . VAL   B 1 34  ? 45.169 -16.144 -8.589  1.00 11.11 ?  34  VAL   B C    1 
ATOM   4210 O O    . VAL   B 1 34  ? 44.649 -17.030 -9.279  1.00 11.90 ?  34  VAL   B O    1 
ATOM   4211 C CB   . VAL   B 1 34  ? 43.270 -14.549 -8.310  1.00 13.10 ?  34  VAL   B CB   1 
ATOM   4212 C CG1  . VAL   B 1 34  ? 43.104 -15.001 -6.865  1.00 13.32 ?  34  VAL   B CG1  1 
ATOM   4213 C CG2  . VAL   B 1 34  ? 42.787 -13.125 -8.497  1.00 14.07 ?  34  VAL   B CG2  1 
ATOM   4214 H H    . VAL   B 1 34  ? 44.683 -14.898 -10.714 1.00 15.01 ?  34  VAL   B H    1 
ATOM   4215 H HA   . VAL   B 1 34  ? 45.290 -14.146 -8.177  1.00 14.29 ?  34  VAL   B HA   1 
ATOM   4216 H HB   . VAL   B 1 34  ? 42.717 -15.123 -8.865  1.00 15.70 ?  34  VAL   B HB   1 
ATOM   4217 H HG11 . VAL   B 1 34  ? 42.251 -14.679 -6.531  1.00 15.95 ?  34  VAL   B HG11 1 
ATOM   4218 H HG12 . VAL   B 1 34  ? 43.128 -15.969 -6.827  1.00 15.95 ?  34  VAL   B HG12 1 
ATOM   4219 H HG13 . VAL   B 1 34  ? 43.826 -14.628 -6.333  1.00 15.95 ?  34  VAL   B HG13 1 
ATOM   4220 H HG21 . VAL   B 1 34  ? 41.871 -13.057 -8.186  1.00 16.85 ?  34  VAL   B HG21 1 
ATOM   4221 H HG22 . VAL   B 1 34  ? 43.356 -12.528 -7.991  1.00 16.85 ?  34  VAL   B HG22 1 
ATOM   4222 H HG23 . VAL   B 1 34  ? 42.829 -12.898 -9.443  1.00 16.85 ?  34  VAL   B HG23 1 
ATOM   4223 N N    . VAL   B 1 35  ? 46.078 -16.396 -7.649  1.00 10.66 ?  35  VAL   B N    1 
ATOM   4224 C CA   . VAL   B 1 35  ? 46.306 -17.741 -7.131  1.00 10.43 ?  35  VAL   B CA   1 
ATOM   4225 C C    . VAL   B 1 35  ? 45.764 -17.795 -5.711  1.00 10.12 ?  35  VAL   B C    1 
ATOM   4226 O O    . VAL   B 1 35  ? 45.986 -16.872 -4.919  1.00 10.79 ?  35  VAL   B O    1 
ATOM   4227 C CB   . VAL   B 1 35  ? 47.789 -18.175 -7.207  1.00 11.16 ?  35  VAL   B CB   1 
ATOM   4228 C CG1  . VAL   B 1 35  ? 48.693 -17.339 -6.294  1.00 11.99 ?  35  VAL   B CG1  1 
ATOM   4229 C CG2  . VAL   B 1 35  ? 47.926 -19.662 -6.874  1.00 11.70 ?  35  VAL   B CG2  1 
ATOM   4230 H H    . VAL   B 1 35  ? 46.579 -15.797 -7.291  1.00 12.77 ?  35  VAL   B H    1 
ATOM   4231 H HA   . VAL   B 1 35  ? 45.792 -18.371 -7.659  1.00 12.49 ?  35  VAL   B HA   1 
ATOM   4232 H HB   . VAL   B 1 35  ? 48.098 -18.056 -8.120  1.00 13.37 ?  35  VAL   B HB   1 
ATOM   4233 H HG11 . VAL   B 1 35  ? 49.615 -17.577 -6.470  1.00 14.36 ?  35  VAL   B HG11 1 
ATOM   4234 H HG12 . VAL   B 1 35  ? 48.542 -16.405 -6.480  1.00 14.36 ?  35  VAL   B HG12 1 
ATOM   4235 H HG13 . VAL   B 1 35  ? 48.469 -17.539 -5.370  1.00 14.36 ?  35  VAL   B HG13 1 
ATOM   4236 H HG21 . VAL   B 1 35  ? 48.846 -19.938 -6.987  1.00 14.01 ?  35  VAL   B HG21 1 
ATOM   4237 H HG22 . VAL   B 1 35  ? 47.645 -19.814 -5.954  1.00 14.01 ?  35  VAL   B HG22 1 
ATOM   4238 H HG23 . VAL   B 1 35  ? 47.353 -20.181 -7.472  1.00 14.01 ?  35  VAL   B HG23 1 
ATOM   4239 N N    . VAL   B 1 36  ? 45.049 -18.874 -5.391  1.00 10.17 ?  36  VAL   B N    1 
ATOM   4240 C CA   . VAL   B 1 36  ? 44.503 -19.074 -4.059  1.00 10.00 ?  36  VAL   B CA   1 
ATOM   4241 C C    . VAL   B 1 36  ? 45.514 -19.833 -3.205  1.00 9.59  ?  36  VAL   B C    1 
ATOM   4242 O O    . VAL   B 1 36  ? 46.051 -20.868 -3.624  1.00 10.98 ?  36  VAL   B O    1 
ATOM   4243 C CB   . VAL   B 1 36  ? 43.168 -19.836 -4.132  1.00 10.42 ?  36  VAL   B CB   1 
ATOM   4244 C CG1  . VAL   B 1 36  ? 42.662 -20.196 -2.740  1.00 11.28 ?  36  VAL   B CG1  1 
ATOM   4245 C CG2  . VAL   B 1 36  ? 42.141 -19.016 -4.882  1.00 11.27 ?  36  VAL   B CG2  1 
ATOM   4246 H H    . VAL   B 1 36  ? 44.873 -19.518 -5.935  1.00 12.18 ?  36  VAL   B H    1 
ATOM   4247 H HA   . VAL   B 1 36  ? 44.339 -18.213 -3.644  1.00 11.97 ?  36  VAL   B HA   1 
ATOM   4248 H HB   . VAL   B 1 36  ? 43.305 -20.662 -4.621  1.00 12.48 ?  36  VAL   B HB   1 
ATOM   4249 H HG11 . VAL   B 1 36  ? 41.726 -20.439 -2.798  1.00 13.51 ?  36  VAL   B HG11 1 
ATOM   4250 H HG12 . VAL   B 1 36  ? 43.178 -20.941 -2.396  1.00 13.51 ?  36  VAL   B HG12 1 
ATOM   4251 H HG13 . VAL   B 1 36  ? 42.766 -19.424 -2.158  1.00 13.51 ?  36  VAL   B HG13 1 
ATOM   4252 H HG21 . VAL   B 1 36  ? 41.301 -19.500 -4.900  1.00 13.51 ?  36  VAL   B HG21 1 
ATOM   4253 H HG22 . VAL   B 1 36  ? 42.027 -18.165 -4.437  1.00 13.51 ?  36  VAL   B HG22 1 
ATOM   4254 H HG23 . VAL   B 1 36  ? 42.456 -18.873 -5.792  1.00 13.51 ?  36  VAL   B HG23 1 
ATOM   4255 N N    . ASN   B 1 37  ? 45.731 -19.345 -1.986  1.00 10.04 ?  37  ASN   B N    1 
ATOM   4256 C CA   . ASN   B 1 37  ? 46.485 -20.073 -0.978  1.00 10.43 ?  37  ASN   B CA   1 
ATOM   4257 C C    . ASN   B 1 37  ? 45.538 -20.741 0.009   1.00 10.27 ?  37  ASN   B C    1 
ATOM   4258 O O    . ASN   B 1 37  ? 44.526 -20.160 0.417   1.00 10.83 ?  37  ASN   B O    1 
ATOM   4259 C CB   . ASN   B 1 37  ? 47.418 -19.123 -0.221  1.00 10.17 ?  37  ASN   B CB   1 
ATOM   4260 C CG   . ASN   B 1 37  ? 48.270 -19.834 0.798   1.00 10.54 ?  37  ASN   B CG   1 
ATOM   4261 O OD1  . ASN   B 1 37  ? 48.603 -21.014 0.629   1.00 11.48 ?  37  ASN   B OD1  1 
ATOM   4262 N ND2  . ASN   B 1 37  ? 48.621 -19.131 1.870   1.00 10.91 ?  37  ASN   B ND2  1 
ATOM   4263 H H    . ASN   B 1 37  ? 45.450 -18.579 -1.714  1.00 12.03 ?  37  ASN   B H    1 
ATOM   4264 H HA   . ASN   B 1 37  ? 47.021 -20.765 -1.397  1.00 12.50 ?  37  ASN   B HA   1 
ATOM   4265 H HB2  . ASN   B 1 37  ? 48.016 -18.699 -0.855  1.00 12.18 ?  37  ASN   B HB2  1 
ATOM   4266 H HB3  . ASN   B 1 37  ? 46.893 -18.459 0.244   1.00 12.18 ?  37  ASN   B HB3  1 
ATOM   4267 H HD21 . ASN   B 1 37  ? 49.111 -19.490 2.481   1.00 13.07 ?  37  ASN   B HD21 1 
ATOM   4268 H HD22 . ASN   B 1 37  ? 48.371 -18.318 1.953   1.00 13.07 ?  37  ASN   B HD22 1 
ATOM   4269 N N    . ALA   B 1 38  ? 45.883 -21.972 0.386   1.00 10.71 ?  38  ALA   B N    1 
ATOM   4270 C CA   . ALA   B 1 38  ? 45.230 -22.714 1.465   1.00 10.95 ?  38  ALA   B CA   1 
ATOM   4271 C C    . ALA   B 1 38  ? 45.818 -22.231 2.789   1.00 10.84 ?  38  ALA   B C    1 
ATOM   4272 O O    . ALA   B 1 38  ? 46.720 -22.843 3.372   1.00 11.80 ?  38  ALA   B O    1 
ATOM   4273 C CB   . ALA   B 1 38  ? 45.448 -24.208 1.272   1.00 12.13 ?  38  ALA   B CB   1 
ATOM   4274 H H    . ALA   B 1 38  ? 46.533 -22.407 0.032   1.00 12.83 ?  38  ALA   B H    1 
ATOM   4275 H HA   . ALA   B 1 38  ? 44.278 -22.529 1.461   1.00 13.11 ?  38  ALA   B HA   1 
ATOM   4276 H HB1  . ALA   B 1 38  ? 45.001 -24.687 1.997   1.00 14.53 ?  38  ALA   B HB1  1 
ATOM   4277 H HB2  . ALA   B 1 38  ? 45.063 -24.476 0.423   1.00 14.53 ?  38  ALA   B HB2  1 
ATOM   4278 H HB3  . ALA   B 1 38  ? 46.394 -24.399 1.289   1.00 14.53 ?  38  ALA   B HB3  1 
ATOM   4279 N N    . ALA   B 1 39  ? 45.305 -21.089 3.250   1.00 10.69 ?  39  ALA   B N    1 
ATOM   4280 C CA   . ALA   B 1 39  ? 45.854 -20.352 4.378   1.00 11.29 ?  39  ALA   B CA   1 
ATOM   4281 C C    . ALA   B 1 39  ? 45.236 -20.798 5.702   1.00 11.18 ?  39  ALA   B C    1 
ATOM   4282 O O    . ALA   B 1 39  ? 44.206 -21.473 5.752   1.00 12.12 ?  39  ALA   B O    1 
ATOM   4283 C CB   . ALA   B 1 39  ? 45.611 -18.852 4.185   1.00 11.85 ?  39  ALA   B CB   1 
ATOM   4284 H H    . ALA   B 1 39  ? 44.607 -20.714 2.910   1.00 12.80 ?  39  ALA   B H    1 
ATOM   4285 H HA   . ALA   B 1 39  ? 46.807 -20.502 4.422   1.00 13.52 ?  39  ALA   B HA   1 
ATOM   4286 H HB1  . ALA   B 1 39  ? 45.983 -18.372 4.943   1.00 14.19 ?  39  ALA   B HB1  1 
ATOM   4287 H HB2  . ALA   B 1 39  ? 46.046 -18.563 3.367   1.00 14.19 ?  39  ALA   B HB2  1 
ATOM   4288 H HB3  . ALA   B 1 39  ? 44.656 -18.688 4.127   1.00 14.19 ?  39  ALA   B HB3  1 
ATOM   4289 N N    . ASN   B 1 40  ? 45.880 -20.379 6.788   1.00 12.02 ?  40  ASN   B N    1 
ATOM   4290 C CA   . ASN   B 1 40  ? 45.323 -20.422 8.129   1.00 12.72 ?  40  ASN   B CA   1 
ATOM   4291 C C    . ASN   B 1 40  ? 45.140 -18.993 8.650   1.00 12.13 ?  40  ASN   B C    1 
ATOM   4292 O O    . ASN   B 1 40  ? 45.545 -18.014 8.015   1.00 12.23 ?  40  ASN   B O    1 
ATOM   4293 C CB   . ASN   B 1 40  ? 46.173 -21.298 9.066   1.00 13.39 ?  40  ASN   B CB   1 
ATOM   4294 C CG   . ASN   B 1 40  ? 47.625 -20.891 9.097   1.00 14.60 ?  40  ASN   B CG   1 
ATOM   4295 O OD1  . ASN   B 1 40  ? 47.942 -19.708 9.175   1.00 16.43 ?  40  ASN   B OD1  1 
ATOM   4296 N ND2  . ASN   B 1 40  ? 48.521 -21.866 9.041   1.00 14.59 ?  40  ASN   B ND2  1 
ATOM   4297 H H    . ASN   B 1 40  ? 46.676 -20.052 6.762   1.00 14.40 ?  40  ASN   B H    1 
ATOM   4298 H HA   . ASN   B 1 40  ? 44.442 -20.818 8.082   1.00 15.24 ?  40  ASN   B HA   1 
ATOM   4299 H HB2  . ASN   B 1 40  ? 45.819 -21.227 9.965   1.00 16.04 ?  40  ASN   B HB2  1 
ATOM   4300 H HB3  . ASN   B 1 40  ? 46.121 -22.217 8.759   1.00 16.04 ?  40  ASN   B HB3  1 
ATOM   4301 H HD21 . ASN   B 1 40  ? 49.360 -21.685 9.058   1.00 17.48 ?  40  ASN   B HD21 1 
ATOM   4302 H HD22 . ASN   B 1 40  ? 48.260 -22.687 8.988   1.00 17.48 ?  40  ASN   B HD22 1 
ATOM   4303 N N    . VAL   B 1 41  ? 44.489 -18.868 9.809   1.00 12.75 ?  41  VAL   B N    1 
ATOM   4304 C CA   . VAL   B 1 41  ? 44.030 -17.549 10.256  1.00 13.37 ?  41  VAL   B CA   1 
ATOM   4305 C C    . VAL   B 1 41  ? 45.182 -16.597 10.554  1.00 13.24 ?  41  VAL   B C    1 
ATOM   4306 O O    . VAL   B 1 41  ? 45.004 -15.377 10.473  1.00 13.29 ?  41  VAL   B O    1 
ATOM   4307 C CB   . VAL   B 1 41  ? 43.050 -17.623 11.445  1.00 14.97 ?  41  VAL   B CB   1 
ATOM   4308 C CG1  . VAL   B 1 41  ? 41.749 -18.302 11.039  1.00 15.54 ?  41  VAL   B CG1  1 
ATOM   4309 C CG2  . VAL   B 1 41  ? 43.694 -18.310 12.640  1.00 16.01 ?  41  VAL   B CG2  1 
ATOM   4310 H H    . VAL   B 1 41  ? 44.306 -19.512 10.341  1.00 15.28 ?  41  VAL   B H    1 
ATOM   4311 H HA   . VAL   B 1 41  ? 43.534 -17.154 9.525   1.00 16.02 ?  41  VAL   B HA   1 
ATOM   4312 H HB   . VAL   B 1 41  ? 42.829 -16.720 11.719  1.00 17.94 ?  41  VAL   B HB   1 
ATOM   4313 H HG11 . VAL   B 1 41  ? 41.143 -18.306 11.798  1.00 18.62 ?  41  VAL   B HG11 1 
ATOM   4314 H HG12 . VAL   B 1 41  ? 41.353 -17.811 10.303  1.00 18.62 ?  41  VAL   B HG12 1 
ATOM   4315 H HG13 . VAL   B 1 41  ? 41.940 -19.213 10.765  1.00 18.62 ?  41  VAL   B HG13 1 
ATOM   4316 H HG21 . VAL   B 1 41  ? 43.055 -18.342 13.370  1.00 19.19 ?  41  VAL   B HG21 1 
ATOM   4317 H HG22 . VAL   B 1 41  ? 43.949 -19.213 12.389  1.00 19.19 ?  41  VAL   B HG22 1 
ATOM   4318 H HG23 . VAL   B 1 41  ? 44.478 -17.809 12.910  1.00 19.19 ?  41  VAL   B HG23 1 
ATOM   4319 N N    . TYR   B 1 42  ? 46.353 -17.114 10.925  1.00 13.23 ?  42  TYR   B N    1 
ATOM   4320 C CA   . TYR   B 1 42  ? 47.506 -16.267 11.193  1.00 13.71 ?  42  TYR   B CA   1 
ATOM   4321 C C    . TYR   B 1 42  ? 48.468 -16.190 10.012  1.00 13.16 ?  42  TYR   B C    1 
ATOM   4322 O O    . TYR   B 1 42  ? 49.556 -15.615 10.146  1.00 14.30 ?  42  TYR   B O    1 
ATOM   4323 C CB   . TYR   B 1 42  ? 48.201 -16.677 12.499  1.00 15.59 ?  42  TYR   B CB   1 
ATOM   4324 C CG   . TYR   B 1 42  ? 47.604 -15.978 13.722  1.00 16.05 ?  42  TYR   B CG   1 
ATOM   4325 C CD1  . TYR   B 1 42  ? 47.835 -14.622 13.946  1.00 15.16 ?  42  TYR   B CD1  1 
ATOM   4326 C CD2  . TYR   B 1 42  ? 46.814 -16.661 14.637  1.00 17.76 ?  42  TYR   B CD2  1 
ATOM   4327 C CE1  . TYR   B 1 42  ? 47.304 -13.971 15.038  1.00 16.38 ?  42  TYR   B CE1  1 
ATOM   4328 C CE2  . TYR   B 1 42  ? 46.275 -16.015 15.740  1.00 18.04 ?  42  TYR   B CE2  1 
ATOM   4329 C CZ   . TYR   B 1 42  ? 46.523 -14.666 15.934  1.00 17.89 ?  42  TYR   B CZ   1 
ATOM   4330 O OH   . TYR   B 1 42  ? 46.003 -14.008 17.033  1.00 20.85 ?  42  TYR   B OH   1 
ATOM   4331 H H    . TYR   B 1 42  ? 46.503 -17.962 11.014  1.00 15.86 ?  42  TYR   B H    1 
ATOM   4332 H HA   . TYR   B 1 42  ? 47.176 -15.370 11.328  1.00 16.43 ?  42  TYR   B HA   1 
ATOM   4333 H HB2  . TYR   B 1 42  ? 48.104 -17.634 12.623  1.00 18.69 ?  42  TYR   B HB2  1 
ATOM   4334 H HB3  . TYR   B 1 42  ? 49.139 -16.441 12.443  1.00 18.69 ?  42  TYR   B HB3  1 
ATOM   4335 H HD1  . TYR   B 1 42  ? 48.365 -14.148 13.338  1.00 18.17 ?  42  TYR   B HD1  1 
ATOM   4336 H HD2  . TYR   B 1 42  ? 46.643 -17.568 14.504  1.00 21.29 ?  42  TYR   B HD2  1 
ATOM   4337 H HE1  . TYR   B 1 42  ? 47.475 -13.067 15.168  1.00 19.63 ?  42  TYR   B HE1  1 
ATOM   4338 H HE2  . TYR   B 1 42  ? 45.747 -16.487 16.343  1.00 21.63 ?  42  TYR   B HE2  1 
ATOM   4339 H HH   . TYR   B 1 42  ? 46.237 -13.206 17.015  1.00 25.00 ?  42  TYR   B HH   1 
ATOM   4340 N N    . LEU   B 1 43  ? 48.070 -16.702 8.848   1.00 12.11 ?  43  LEU   B N    1 
ATOM   4341 C CA   . LEU   B 1 43  ? 48.886 -16.637 7.638   1.00 11.94 ?  43  LEU   B CA   1 
ATOM   4342 C C    . LEU   B 1 43  ? 50.297 -17.146 7.897   1.00 12.33 ?  43  LEU   B C    1 
ATOM   4343 O O    . LEU   B 1 43  ? 51.280 -16.554 7.452   1.00 12.90 ?  43  LEU   B O    1 
ATOM   4344 C CB   . LEU   B 1 43  ? 48.907 -15.233 7.024   1.00 11.92 ?  43  LEU   B CB   1 
ATOM   4345 C CG   . LEU   B 1 43  ? 47.546 -14.619 6.665   1.00 12.37 ?  43  LEU   B CG   1 
ATOM   4346 C CD1  . LEU   B 1 43  ? 47.753 -13.218 6.095   1.00 13.92 ?  43  LEU   B CD1  1 
ATOM   4347 C CD2  . LEU   B 1 43  ? 46.761 -15.495 5.696   1.00 12.83 ?  43  LEU   B CD2  1 
ATOM   4348 H H    . LEU   B 1 43  ? 47.323 -17.111 8.731   1.00 14.51 ?  43  LEU   B H    1 
ATOM   4349 H HA   . LEU   B 1 43  ? 48.489 -17.227 6.974   1.00 14.31 ?  43  LEU   B HA   1 
ATOM   4350 H HB2  . LEU   B 1 43  ? 49.337 -14.634 7.650   1.00 14.28 ?  43  LEU   B HB2  1 
ATOM   4351 H HB3  . LEU   B 1 43  ? 49.427 -15.270 6.204   1.00 14.28 ?  43  LEU   B HB3  1 
ATOM   4352 H HG   . LEU   B 1 43  ? 47.022 -14.532 7.474   1.00 14.82 ?  43  LEU   B HG   1 
ATOM   4353 H HD11 . LEU   B 1 43  ? 46.887 -12.834 5.873   1.00 16.69 ?  43  LEU   B HD11 1 
ATOM   4354 H HD12 . LEU   B 1 43  ? 48.191 -12.666 6.764   1.00 16.69 ?  43  LEU   B HD12 1 
ATOM   4355 H HD13 . LEU   B 1 43  ? 48.302 -13.273 5.300   1.00 16.69 ?  43  LEU   B HD13 1 
ATOM   4356 H HD21 . LEU   B 1 43  ? 45.949 -15.029 5.435   1.00 15.37 ?  43  LEU   B HD21 1 
ATOM   4357 H HD22 . LEU   B 1 43  ? 47.306 -15.672 4.914   1.00 15.37 ?  43  LEU   B HD22 1 
ATOM   4358 H HD23 . LEU   B 1 43  ? 46.534 -16.328 6.138   1.00 15.37 ?  43  LEU   B HD23 1 
ATOM   4359 N N    . LYS   B 1 44  ? 50.396 -18.266 8.613   1.00 12.31 ?  44  LYS   B N    1 
ATOM   4360 C CA   . LYS   B 1 44  ? 51.663 -18.943 8.853   1.00 13.17 ?  44  LYS   B CA   1 
ATOM   4361 C C    . LYS   B 1 44  ? 51.778 -20.063 7.829   1.00 12.77 ?  44  LYS   B C    1 
ATOM   4362 O O    . LYS   B 1 44  ? 51.079 -21.077 7.921   1.00 13.84 ?  44  LYS   B O    1 
ATOM   4363 C CB   . LYS   B 1 44  ? 51.716 -19.459 10.289  1.00 14.87 ?  44  LYS   B CB   1 
ATOM   4364 C CG   . LYS   B 1 44  ? 51.928 -18.352 11.311  1.00 17.61 ?  44  LYS   B CG   1 
ATOM   4365 C CD   . LYS   B 1 44  ? 53.124 -17.489 10.899  1.00 21.00 ?  44  LYS   B CD   1 
ATOM   4366 C CE   . LYS   B 1 44  ? 53.645 -16.619 12.010  1.00 24.07 ?  44  LYS   B CE   1 
ATOM   4367 N NZ   . LYS   B 1 44  ? 54.803 -15.798 11.588  1.00 25.28 ?  44  LYS   B NZ   1 
ATOM   4368 H H    . LYS   B 1 44  ? 49.722 -18.655 8.976   1.00 14.75 ?  44  LYS   B H    1 
ATOM   4369 H HA   . LYS   B 1 44  ? 52.395 -18.331 8.688   1.00 15.78 ?  44  LYS   B HA   1 
ATOM   4370 H HB2  . LYS   B 1 44  ? 50.869 -19.895 10.498  1.00 17.82 ?  44  LYS   B HB2  1 
ATOM   4371 H HB3  . LYS   B 1 44  ? 52.440 -20.091 10.374  1.00 17.82 ?  44  LYS   B HB3  1 
ATOM   4372 H HG2  . LYS   B 1 44  ? 51.140 -17.793 11.359  1.00 21.11 ?  44  LYS   B HG2  1 
ATOM   4373 H HG3  . LYS   B 1 44  ? 52.120 -18.748 12.179  1.00 21.11 ?  44  LYS   B HG3  1 
ATOM   4374 H HD2  . LYS   B 1 44  ? 53.839 -18.076 10.590  1.00 25.17 ?  44  LYS   B HD2  1 
ATOM   4375 H HD3  . LYS   B 1 44  ? 52.845 -16.905 10.174  1.00 25.17 ?  44  LYS   B HD3  1 
ATOM   4376 H HE2  . LYS   B 1 44  ? 52.945 -16.006 12.255  1.00 28.86 ?  44  LYS   B HE2  1 
ATOM   4377 H HE3  . LYS   B 1 44  ? 53.905 -17.175 12.763  1.00 28.86 ?  44  LYS   B HE3  1 
ATOM   4378 H HZ1  . LYS   B 1 44  ? 55.077 -15.292 12.266  1.00 30.32 ?  44  LYS   B HZ1  1 
ATOM   4379 H HZ2  . LYS   B 1 44  ? 55.471 -16.320 11.324  1.00 30.32 ?  44  LYS   B HZ2  1 
ATOM   4380 H HZ3  . LYS   B 1 44  ? 54.566 -15.267 10.910  1.00 30.32 ?  44  LYS   B HZ3  1 
ATOM   4381 N N    . HIS   B 1 45  ? 52.633 -19.857 6.831   1.00 12.53 ?  45  HIS   B N    1 
ATOM   4382 C CA   . HIS   B 1 45  ? 52.646 -20.689 5.630   1.00 12.30 ?  45  HIS   B CA   1 
ATOM   4383 C C    . HIS   B 1 45  ? 53.665 -21.811 5.788   1.00 14.60 ?  45  HIS   B C    1 
ATOM   4384 O O    . HIS   B 1 45  ? 54.723 -21.828 5.168   1.00 16.86 ?  45  HIS   B O    1 
ATOM   4385 C CB   . HIS   B 1 45  ? 52.963 -19.834 4.415   1.00 12.42 ?  45  HIS   B CB   1 
ATOM   4386 C CG   . HIS   B 1 45  ? 52.097 -18.625 4.305   1.00 12.28 ?  45  HIS   B CG   1 
ATOM   4387 N ND1  . HIS   B 1 45  ? 50.719 -18.699 4.269   1.00 12.30 ?  45  HIS   B ND1  1 
ATOM   4388 C CD2  . HIS   B 1 45  ? 52.415 -17.312 4.229   1.00 13.01 ?  45  HIS   B CD2  1 
ATOM   4389 C CE1  . HIS   B 1 45  ? 50.234 -17.475 4.162   1.00 11.80 ?  45  HIS   B CE1  1 
ATOM   4390 N NE2  . HIS   B 1 45  ? 51.238 -16.616 4.137   1.00 12.51 ?  45  HIS   B NE2  1 
ATOM   4391 H H    . HIS   B 1 45  ? 53.211 -19.221 6.818   1.00 15.01 ?  45  HIS   B H    1 
ATOM   4392 H HA   . HIS   B 1 45  ? 51.766 -21.085 5.502   1.00 14.74 ?  45  HIS   B HA   1 
ATOM   4393 H HB2  . HIS   B 1 45  ? 53.882 -19.543 4.461   1.00 14.88 ?  45  HIS   B HB2  1 
ATOM   4394 H HB3  . HIS   B 1 45  ? 52.829 -20.374 3.610   1.00 14.88 ?  45  HIS   B HB3  1 
ATOM   4395 H HD2  . HIS   B 1 45  ? 53.274 -16.952 4.234   1.00 15.58 ?  45  HIS   B HD2  1 
ATOM   4396 H HE1  . HIS   B 1 45  ? 49.331 -17.252 4.108   1.00 14.14 ?  45  HIS   B HE1  1 
ATOM   4397 H HE2  . HIS   B 1 45  ? 51.165 -15.761 4.080   1.00 14.99 ?  45  HIS   B HE2  1 
ATOM   4398 N N    A GLY   B 1 46  ? 53.304 -22.777 6.628   0.66 15.80 ?  46  GLY   B N    1 
ATOM   4399 N N    B GLY   B 1 46  ? 53.315 -22.763 6.644   0.34 15.52 ?  46  GLY   B N    1 
ATOM   4400 C CA   A GLY   B 1 46  ? 54.229 -23.829 7.007   0.66 17.53 ?  46  GLY   B CA   1 
ATOM   4401 C CA   B GLY   B 1 46  ? 54.235 -23.829 6.978   0.34 16.67 ?  46  GLY   B CA   1 
ATOM   4402 C C    A GLY   B 1 46  ? 54.278 -25.063 6.126   0.66 19.08 ?  46  GLY   B C    1 
ATOM   4403 C C    B GLY   B 1 46  ? 54.264 -24.972 5.982   0.34 17.93 ?  46  GLY   B C    1 
ATOM   4404 O O    A GLY   B 1 46  ? 55.365 -25.530 5.774   0.66 21.69 ?  46  GLY   B O    1 
ATOM   4405 O O    B GLY   B 1 46  ? 55.302 -25.254 5.374   0.34 18.78 ?  46  GLY   B O    1 
ATOM   4406 H H    A GLY   B 1 46  ? 52.531 -22.827 7.009   0.66 18.94 ?  46  GLY   B H    1 
ATOM   4407 H H    B GLY   B 1 46  ? 52.552 -22.804 7.048   0.34 18.60 ?  46  GLY   B H    1 
ATOM   4408 H HA2  A GLY   B 1 46  ? 55.123 -23.453 7.041   0.66 21.01 ?  46  GLY   B HA2  1 
ATOM   4409 H HA2  B GLY   B 1 46  ? 55.129 -23.460 7.041   0.34 19.98 ?  46  GLY   B HA2  1 
ATOM   4410 H HA3  A GLY   B 1 46  ? 54.002 -24.132 7.898   0.66 21.01 ?  46  GLY   B HA3  1 
ATOM   4411 H HA3  B GLY   B 1 46  ? 53.997 -24.183 7.851   0.34 19.98 ?  46  GLY   B HA3  1 
ATOM   4412 N N    . GLY   B 1 47  ? 53.122 -25.627 5.785   1.00 18.31 ?  47  GLY   B N    1 
ATOM   4413 C CA   . GLY   B 1 47  ? 53.067 -26.898 5.090   1.00 16.26 ?  47  GLY   B CA   1 
ATOM   4414 C C    . GLY   B 1 47  ? 52.141 -26.887 3.889   1.00 14.20 ?  47  GLY   B C    1 
ATOM   4415 O O    . GLY   B 1 47  ? 51.481 -25.892 3.596   1.00 14.43 ?  47  GLY   B O    1 
ATOM   4416 H H    A GLY   B 1 47  ? 52.348 -25.301 5.974   0.66 21.95 ?  47  GLY   B H    1 
ATOM   4417 H H    B GLY   B 1 47  ? 52.352 -25.345 6.049   0.34 21.95 ?  47  GLY   B H    1 
ATOM   4418 H HA2  . GLY   B 1 47  ? 53.954 -27.143 4.783   1.00 19.49 ?  47  GLY   B HA2  1 
ATOM   4419 H HA3  . GLY   B 1 47  ? 52.760 -27.584 5.704   1.00 19.49 ?  47  GLY   B HA3  1 
ATOM   4420 N N    . GLY   B 1 48  ? 52.090 -28.032 3.211   1.00 13.56 ?  48  GLY   B N    1 
ATOM   4421 C CA   . GLY   B 1 48  ? 51.161 -28.184 2.107   1.00 13.26 ?  48  GLY   B CA   1 
ATOM   4422 C C    . GLY   B 1 48  ? 51.303 -27.077 1.087   1.00 12.59 ?  48  GLY   B C    1 
ATOM   4423 O O    . GLY   B 1 48  ? 52.409 -26.612 0.779   1.00 13.10 ?  48  GLY   B O    1 
ATOM   4424 H H    . GLY   B 1 48  ? 52.583 -28.715 3.364   1.00 16.25 ?  48  GLY   B H    1 
ATOM   4425 H HA2  . GLY   B 1 48  ? 51.320 -29.034 1.663   1.00 15.89 ?  48  GLY   B HA2  1 
ATOM   4426 H HA3  . GLY   B 1 48  ? 50.252 -28.178 2.441   1.00 15.89 ?  48  GLY   B HA3  1 
ATOM   4427 N N    . VAL   B 1 49  ? 50.159 -26.640 0.559   1.00 12.47 ?  49  VAL   B N    1 
ATOM   4428 C CA   . VAL   B 1 49  ? 50.144 -25.614 -0.482  1.00 12.45 ?  49  VAL   B CA   1 
ATOM   4429 C C    . VAL   B 1 49  ? 50.805 -24.324 0.004   1.00 11.61 ?  49  VAL   B C    1 
ATOM   4430 O O    . VAL   B 1 49  ? 51.594 -23.704 -0.719  1.00 12.26 ?  49  VAL   B O    1 
ATOM   4431 C CB   . VAL   B 1 49  ? 48.702 -25.366 -0.967  1.00 13.75 ?  49  VAL   B CB   1 
ATOM   4432 C CG1  . VAL   B 1 49  ? 48.626 -24.123 -1.851  1.00 13.70 ?  49  VAL   B CG1  1 
ATOM   4433 C CG2  . VAL   B 1 49  ? 48.173 -26.582 -1.719  1.00 15.17 ?  49  VAL   B CG2  1 
ATOM   4434 H H    . VAL   B 1 49  ? 49.372 -26.917 0.784   1.00 14.94 ?  49  VAL   B H    1 
ATOM   4435 H HA   . VAL   B 1 49  ? 50.648 -25.932 -1.244  1.00 14.92 ?  49  VAL   B HA   1 
ATOM   4436 H HB   . VAL   B 1 49  ? 48.126 -25.217 -0.202  1.00 16.47 ?  49  VAL   B HB   1 
ATOM   4437 H HG11 . VAL   B 1 49  ? 47.792 -24.137 -2.350  1.00 16.42 ?  49  VAL   B HG11 1 
ATOM   4438 H HG12 . VAL   B 1 49  ? 48.655 -23.330 -1.291  1.00 16.42 ?  49  VAL   B HG12 1 
ATOM   4439 H HG13 . VAL   B 1 49  ? 49.375 -24.123 -2.466  1.00 16.42 ?  49  VAL   B HG13 1 
ATOM   4440 H HG21 . VAL   B 1 49  ? 47.265 -26.406 -2.016  1.00 18.18 ?  49  VAL   B HG21 1 
ATOM   4441 H HG22 . VAL   B 1 49  ? 48.742 -26.751 -2.489  1.00 18.18 ?  49  VAL   B HG22 1 
ATOM   4442 H HG23 . VAL   B 1 49  ? 48.184 -27.349 -1.126  1.00 18.18 ?  49  VAL   B HG23 1 
ATOM   4443 N N    . ALA   B 1 50  ? 50.466 -23.880 1.216   1.00 11.50 ?  50  ALA   B N    1 
ATOM   4444 C CA   . ALA   B 1 50  ? 50.986 -22.603 1.694   1.00 11.60 ?  50  ALA   B CA   1 
ATOM   4445 C C    . ALA   B 1 50  ? 52.504 -22.639 1.797   1.00 11.67 ?  50  ALA   B C    1 
ATOM   4446 O O    . ALA   B 1 50  ? 53.185 -21.673 1.429   1.00 11.62 ?  50  ALA   B O    1 
ATOM   4447 C CB   . ALA   B 1 50  ? 50.367 -22.253 3.044   1.00 11.70 ?  50  ALA   B CB   1 
ATOM   4448 H H    . ALA   B 1 50  ? 49.951 -24.291 1.769   1.00 13.77 ?  50  ALA   B H    1 
ATOM   4449 H HA   . ALA   B 1 50  ? 50.751 -21.908 1.065   1.00 13.89 ?  50  ALA   B HA   1 
ATOM   4450 H HB1  . ALA   B 1 50  ? 50.725 -21.401 3.345   1.00 14.02 ?  50  ALA   B HB1  1 
ATOM   4451 H HB2  . ALA   B 1 50  ? 49.405 -22.190 2.944   1.00 14.02 ?  50  ALA   B HB2  1 
ATOM   4452 H HB3  . ALA   B 1 50  ? 50.589 -22.947 3.686   1.00 14.02 ?  50  ALA   B HB3  1 
ATOM   4453 N N    . GLY   B 1 51  ? 53.055 -23.734 2.315   1.00 12.26 ?  51  GLY   B N    1 
ATOM   4454 C CA   . GLY   B 1 51  ? 54.500 -23.834 2.386   1.00 12.73 ?  51  GLY   B CA   1 
ATOM   4455 C C    . GLY   B 1 51  ? 55.144 -23.780 1.015   1.00 12.43 ?  51  GLY   B C    1 
ATOM   4456 O O    . GLY   B 1 51  ? 56.186 -23.144 0.833   1.00 13.62 ?  51  GLY   B O    1 
ATOM   4457 H H    . GLY   B 1 51  ? 52.627 -24.412 2.623   1.00 14.69 ?  51  GLY   B H    1 
ATOM   4458 H HA2  . GLY   B 1 51  ? 54.852 -23.101 2.919   1.00 15.25 ?  51  GLY   B HA2  1 
ATOM   4459 H HA3  . GLY   B 1 51  ? 54.750 -24.668 2.811   1.00 15.25 ?  51  GLY   B HA3  1 
ATOM   4460 N N    . ALA   B 1 52  ? 54.537 -24.445 0.032   1.00 12.25 ?  52  ALA   B N    1 
ATOM   4461 C CA   . ALA   B 1 52  ? 55.105 -24.455 -1.309  1.00 12.89 ?  52  ALA   B CA   1 
ATOM   4462 C C    . ALA   B 1 52  ? 55.027 -23.076 -1.959  1.00 12.18 ?  52  ALA   B C    1 
ATOM   4463 O O    . ALA   B 1 52  ? 56.002 -22.622 -2.581  1.00 13.00 ?  52  ALA   B O    1 
ATOM   4464 C CB   . ALA   B 1 52  ? 54.406 -25.498 -2.169  1.00 13.32 ?  52  ALA   B CB   1 
ATOM   4465 H H    . ALA   B 1 52  ? 53.797 -24.879 0.117   1.00 14.68 ?  52  ALA   B H    1 
ATOM   4466 H HA   . ALA   B 1 52  ? 56.040 -24.695 -1.243  1.00 15.45 ?  52  ALA   B HA   1 
ATOM   4467 H HB1  . ALA   B 1 52  ? 54.805 -25.491 -3.054  1.00 15.96 ?  52  ALA   B HB1  1 
ATOM   4468 H HB2  . ALA   B 1 52  ? 54.529 -26.371 -1.761  1.00 15.96 ?  52  ALA   B HB2  1 
ATOM   4469 H HB3  . ALA   B 1 52  ? 53.465 -25.286 -2.225  1.00 15.96 ?  52  ALA   B HB3  1 
ATOM   4470 N N    . LEU   B 1 53  ? 53.878 -22.400 -1.845  1.00 11.68 ?  53  LEU   B N    1 
ATOM   4471 C CA   . LEU   B 1 53  ? 53.765 -21.057 -2.411  1.00 12.11 ?  53  LEU   B CA   1 
ATOM   4472 C C    . LEU   B 1 53  ? 54.777 -20.116 -1.764  1.00 11.88 ?  53  LEU   B C    1 
ATOM   4473 O O    . LEU   B 1 53  ? 55.479 -19.363 -2.452  1.00 12.62 ?  53  LEU   B O    1 
ATOM   4474 C CB   . LEU   B 1 53  ? 52.339 -20.520 -2.241  1.00 12.25 ?  53  LEU   B CB   1 
ATOM   4475 C CG   . LEU   B 1 53  ? 51.210 -21.250 -2.979  1.00 12.51 ?  53  LEU   B CG   1 
ATOM   4476 C CD1  . LEU   B 1 53  ? 49.860 -20.661 -2.628  1.00 14.17 ?  53  LEU   B CD1  1 
ATOM   4477 C CD2  . LEU   B 1 53  ? 51.424 -21.241 -4.488  1.00 14.36 ?  53  LEU   B CD2  1 
ATOM   4478 H H    . LEU   B 1 53  ? 53.169 -22.691 -1.457  1.00 14.00 ?  53  LEU   B H    1 
ATOM   4479 H HA   . LEU   B 1 53  ? 53.961 -21.102 -3.365  1.00 14.51 ?  53  LEU   B HA   1 
ATOM   4480 H HB2  . LEU   B 1 53  ? 52.122 -20.548 -1.300  1.00 14.68 ?  53  LEU   B HB2  1 
ATOM   4481 H HB3  . LEU   B 1 53  ? 52.327 -19.605 -2.551  1.00 14.68 ?  53  LEU   B HB3  1 
ATOM   4482 H HG   . LEU   B 1 53  ? 51.201 -22.180 -2.692  1.00 14.99 ?  53  LEU   B HG   1 
ATOM   4483 H HD11 . LEU   B 1 53  ? 49.167 -21.151 -3.106  1.00 16.99 ?  53  LEU   B HD11 1 
ATOM   4484 H HD12 . LEU   B 1 53  ? 49.716 -20.752 -1.670  1.00 16.99 ?  53  LEU   B HD12 1 
ATOM   4485 H HD13 . LEU   B 1 53  ? 49.844 -19.731 -2.881  1.00 16.99 ?  53  LEU   B HD13 1 
ATOM   4486 H HD21 . LEU   B 1 53  ? 50.700 -21.728 -4.915  1.00 17.21 ?  53  LEU   B HD21 1 
ATOM   4487 H HD22 . LEU   B 1 53  ? 51.435 -20.326 -4.801  1.00 17.21 ?  53  LEU   B HD22 1 
ATOM   4488 H HD23 . LEU   B 1 53  ? 52.270 -21.674 -4.691  1.00 17.21 ?  53  LEU   B HD23 1 
ATOM   4489 N N    . ASN   B 1 54  ? 54.868 -20.144 -0.437  1.00 11.49 ?  54  ASN   B N    1 
ATOM   4490 C CA   . ASN   B 1 54  ? 55.785 -19.235 0.235   1.00 12.22 ?  54  ASN   B CA   1 
ATOM   4491 C C    . ASN   B 1 54  ? 57.225 -19.517 -0.164  1.00 12.62 ?  54  ASN   B C    1 
ATOM   4492 O O    . ASN   B 1 54  ? 58.002 -18.583 -0.404  1.00 12.88 ?  54  ASN   B O    1 
ATOM   4493 C CB   . ASN   B 1 54  ? 55.620 -19.305 1.745   1.00 12.89 ?  54  ASN   B CB   1 
ATOM   4494 C CG   . ASN   B 1 54  ? 56.596 -18.388 2.453   1.00 12.93 ?  54  ASN   B CG   1 
ATOM   4495 O OD1  . ASN   B 1 54  ? 56.614 -17.180 2.203   1.00 13.28 ?  54  ASN   B OD1  1 
ATOM   4496 N ND2  . ASN   B 1 54  ? 57.442 -18.959 3.308   1.00 14.52 ?  54  ASN   B ND2  1 
ATOM   4497 H H    . ASN   B 1 54  ? 54.427 -20.673 0.079   1.00 13.76 ?  54  ASN   B H    1 
ATOM   4498 H HA   . ASN   B 1 54  ? 55.574 -18.331 -0.045  1.00 14.64 ?  54  ASN   B HA   1 
ATOM   4499 H HB2  . ASN   B 1 54  ? 54.720 -19.029 1.981   1.00 15.44 ?  54  ASN   B HB2  1 
ATOM   4500 H HB3  . ASN   B 1 54  ? 55.781 -20.213 2.043   1.00 15.44 ?  54  ASN   B HB3  1 
ATOM   4501 H HD21 . ASN   B 1 54  ? 58.022 -18.480 3.727   1.00 17.41 ?  54  ASN   B HD21 1 
ATOM   4502 H HD22 . ASN   B 1 54  ? 57.411 -19.810 3.446   1.00 17.41 ?  54  ASN   B HD22 1 
ATOM   4503 N N    . LYS   B 1 55  ? 57.607 -20.793 -0.229  1.00 13.12 ?  55  LYS   B N    1 
ATOM   4504 C CA   . LYS   B 1 55  ? 58.963 -21.132 -0.646  1.00 14.33 ?  55  LYS   B CA   1 
ATOM   4505 C C    . LYS   B 1 55  ? 59.259 -20.591 -2.038  1.00 13.82 ?  55  LYS   B C    1 
ATOM   4506 O O    . LYS   B 1 55  ? 60.361 -20.088 -2.291  1.00 14.51 ?  55  LYS   B O    1 
ATOM   4507 C CB   . LYS   B 1 55  ? 59.158 -22.647 -0.594  1.00 15.64 ?  55  LYS   B CB   1 
ATOM   4508 C CG   . LYS   B 1 55  ? 60.539 -23.116 -1.022  1.00 19.97 ?  55  LYS   B CG   1 
ATOM   4509 C CD   . LYS   B 1 55  ? 60.700 -24.617 -0.846  1.00 23.67 ?  55  LYS   B CD   1 
ATOM   4510 C CE   . LYS   B 1 55  ? 60.695 -25.019 0.628   1.00 26.66 ?  55  LYS   B CE   1 
ATOM   4511 N NZ   . LYS   B 1 55  ? 61.069 -26.438 0.835   1.00 28.33 ?  55  LYS   B NZ   1 
ATOM   4512 H H    . LYS   B 1 55  ? 57.109 -21.465 -0.037  1.00 15.72 ?  55  LYS   B H    1 
ATOM   4513 H HA   . LYS   B 1 55  ? 59.596 -20.730 -0.034  1.00 17.17 ?  55  LYS   B HA   1 
ATOM   4514 H HB2  . LYS   B 1 55  ? 59.014 -22.942 0.320   1.00 18.74 ?  55  LYS   B HB2  1 
ATOM   4515 H HB3  . LYS   B 1 55  ? 58.511 -23.070 -1.179  1.00 18.74 ?  55  LYS   B HB3  1 
ATOM   4516 H HG2  . LYS   B 1 55  ? 60.673 -22.906 -1.961  1.00 23.94 ?  55  LYS   B HG2  1 
ATOM   4517 H HG3  . LYS   B 1 55  ? 61.211 -22.671 -0.481  1.00 23.94 ?  55  LYS   B HG3  1 
ATOM   4518 H HD2  . LYS   B 1 55  ? 59.966 -25.074 -1.286  1.00 28.37 ?  55  LYS   B HD2  1 
ATOM   4519 H HD3  . LYS   B 1 55  ? 61.547 -24.898 -1.230  1.00 28.37 ?  55  LYS   B HD3  1 
ATOM   4520 H HE2  . LYS   B 1 55  ? 61.328 -24.457 1.106   1.00 31.97 ?  55  LYS   B HE2  1 
ATOM   4521 H HE3  . LYS   B 1 55  ? 59.801 -24.882 0.986   1.00 31.97 ?  55  LYS   B HE3  1 
ATOM   4522 H HZ1  . LYS   B 1 55  ? 61.028 -26.635 1.702   1.00 33.97 ?  55  LYS   B HZ1  1 
ATOM   4523 H HZ2  . LYS   B 1 55  ? 60.505 -26.964 0.392   1.00 33.97 ?  55  LYS   B HZ2  1 
ATOM   4524 H HZ3  . LYS   B 1 55  ? 61.894 -26.579 0.542   1.00 33.97 ?  55  LYS   B HZ3  1 
ATOM   4525 N N    . ALA   B 1 56  ? 58.288 -20.677 -2.952  1.00 13.50 ?  56  ALA   B N    1 
ATOM   4526 C CA   . ALA   B 1 56  ? 58.506 -20.179 -4.304  1.00 14.38 ?  56  ALA   B CA   1 
ATOM   4527 C C    . ALA   B 1 56  ? 58.787 -18.683 -4.306  1.00 13.94 ?  56  ALA   B C    1 
ATOM   4528 O O    . ALA   B 1 56  ? 59.524 -18.191 -5.171  1.00 15.10 ?  56  ALA   B O    1 
ATOM   4529 C CB   . ALA   B 1 56  ? 57.310 -20.514 -5.197  1.00 15.05 ?  56  ALA   B CB   1 
ATOM   4530 H H    . ALA   B 1 56  ? 57.504 -21.005 -2.813  1.00 16.17 ?  56  ALA   B H    1 
ATOM   4531 H HA   . ALA   B 1 56  ? 59.283 -20.614 -4.676  1.00 17.23 ?  56  ALA   B HA   1 
ATOM   4532 H HB1  . ALA   B 1 56  ? 57.480 -20.177 -6.093  1.00 18.03 ?  56  ALA   B HB1  1 
ATOM   4533 H HB2  . ALA   B 1 56  ? 57.201 -21.477 -5.223  1.00 18.03 ?  56  ALA   B HB2  1 
ATOM   4534 H HB3  . ALA   B 1 56  ? 56.514 -20.099 -4.834  1.00 18.03 ?  56  ALA   B HB3  1 
ATOM   4535 N N    . THR   B 1 57  ? 58.214 -17.944 -3.353  1.00 13.51 ?  57  THR   B N    1 
ATOM   4536 C CA   . THR   B 1 57  ? 58.455 -16.509 -3.233  1.00 13.59 ?  57  THR   B CA   1 
ATOM   4537 C C    . THR   B 1 57  ? 59.705 -16.180 -2.424  1.00 14.48 ?  57  THR   B C    1 
ATOM   4538 O O    . THR   B 1 57  ? 59.940 -15.005 -2.121  1.00 15.05 ?  57  THR   B O    1 
ATOM   4539 C CB   . THR   B 1 57  ? 57.257 -15.777 -2.599  1.00 12.99 ?  57  THR   B CB   1 
ATOM   4540 O OG1  . THR   B 1 57  ? 57.236 -15.986 -1.179  1.00 13.34 ?  57  THR   B OG1  1 
ATOM   4541 C CG2  . THR   B 1 57  ? 55.941 -16.197 -3.239  1.00 13.18 ?  57  THR   B CG2  1 
ATOM   4542 H H    . THR   B 1 57  ? 57.669 -18.252 -2.758  1.00 16.19 ?  57  THR   B H    1 
ATOM   4543 H HA   . THR   B 1 57  ? 58.572 -16.142 -4.124  1.00 16.29 ?  57  THR   B HA   1 
ATOM   4544 H HB   . THR   B 1 57  ? 57.361 -14.823 -2.764  1.00 15.56 ?  57  THR   B HB   1 
ATOM   4545 H HG1  . THR   B 1 57  ? 57.161 -16.805 -1.015  1.00 15.99 ?  57  THR   B HG1  1 
ATOM   4546 H HG21 . THR   B 1 57  ? 55.215 -15.649 -2.902  1.00 15.80 ?  57  THR   B HG21 1 
ATOM   4547 H HG22 . THR   B 1 57  ? 55.991 -16.090 -4.204  1.00 15.80 ?  57  THR   B HG22 1 
ATOM   4548 H HG23 . THR   B 1 57  ? 55.755 -17.125 -3.037  1.00 15.80 ?  57  THR   B HG23 1 
ATOM   4549 N N    . ASN   B 1 58  ? 60.504 -17.181 -2.066  1.00 15.46 ?  58  ASN   B N    1 
ATOM   4550 C CA   . ASN   B 1 58  ? 61.701 -16.968 -1.257  1.00 18.18 ?  58  ASN   B CA   1 
ATOM   4551 C C    . ASN   B 1 58  ? 61.366 -16.255 0.053   1.00 15.93 ?  58  ASN   B C    1 
ATOM   4552 O O    . ASN   B 1 58  ? 62.106 -15.382 0.516   1.00 16.67 ?  58  ASN   B O    1 
ATOM   4553 C CB   . ASN   B 1 58  ? 62.789 -16.223 -2.039  1.00 25.76 ?  58  ASN   B CB   1 
ATOM   4554 C CG   . ASN   B 1 58  ? 64.157 -16.344 -1.393  1.00 34.66 ?  58  ASN   B CG   1 
ATOM   4555 O OD1  . ASN   B 1 58  ? 64.463 -17.343 -0.743  1.00 37.57 ?  58  ASN   B OD1  1 
ATOM   4556 N ND2  . ASN   B 1 58  ? 64.987 -15.324 -1.568  1.00 39.21 ?  58  ASN   B ND2  1 
ATOM   4557 H H    . ASN   B 1 58  ? 60.368 -18.005 -2.277  1.00 18.52 ?  58  ASN   B H    1 
ATOM   4558 H HA   . ASN   B 1 58  ? 62.062 -17.839 -1.032  1.00 21.79 ?  58  ASN   B HA   1 
ATOM   4559 H HB2  . ASN   B 1 58  ? 62.846 -16.593 -2.937  1.00 30.89 ?  58  ASN   B HB2  1 
ATOM   4560 H HB3  . ASN   B 1 58  ? 62.563 -15.283 -2.083  1.00 30.89 ?  58  ASN   B HB3  1 
ATOM   4561 H HD21 . ASN   B 1 58  ? 65.775 -15.346 -1.223  1.00 47.02 ?  58  ASN   B HD21 1 
ATOM   4562 H HD22 . ASN   B 1 58  ? 64.738 -14.642 -2.026  1.00 47.02 ?  58  ASN   B HD22 1 
ATOM   4563 N N    . ASN   B 1 59  ? 60.243 -16.638 0.660   1.00 14.75 ?  59  ASN   B N    1 
ATOM   4564 C CA   . ASN   B 1 59  ? 59.771 -16.163 1.961   1.00 14.62 ?  59  ASN   B CA   1 
ATOM   4565 C C    . ASN   B 1 59  ? 59.171 -14.758 1.904   1.00 14.25 ?  59  ASN   B C    1 
ATOM   4566 O O    . ASN   B 1 59  ? 58.747 -14.249 2.949   1.00 14.16 ?  59  ASN   B O    1 
ATOM   4567 C CB   . ASN   B 1 59  ? 60.843 -16.220 3.066   1.00 15.59 ?  59  ASN   B CB   1 
ATOM   4568 C CG   . ASN   B 1 59  ? 60.253 -16.392 4.447   1.00 16.65 ?  59  ASN   B CG   1 
ATOM   4569 O OD1  . ASN   B 1 59  ? 59.421 -17.275 4.672   1.00 17.01 ?  59  ASN   B OD1  1 
ATOM   4570 N ND2  . ASN   B 1 59  ? 60.672 -15.548 5.381   1.00 17.60 ?  59  ASN   B ND2  1 
ATOM   4571 H H    . ASN   B 1 59  ? 59.707 -17.220 0.317   1.00 17.67 ?  59  ASN   B H    1 
ATOM   4572 H HA   . ASN   B 1 59  ? 59.061 -16.759 2.244   1.00 17.53 ?  59  ASN   B HA   1 
ATOM   4573 H HB2  . ASN   B 1 59  ? 61.431 -16.975 2.910   1.00 18.69 ?  59  ASN   B HB2  1 
ATOM   4574 H HB3  . ASN   B 1 59  ? 61.348 -15.396 3.068   1.00 18.69 ?  59  ASN   B HB3  1 
ATOM   4575 H HD21 . ASN   B 1 59  ? 60.361 -15.601 6.185   1.00 21.10 ?  59  ASN   B HD21 1 
ATOM   4576 H HD22 . ASN   B 1 59  ? 61.251 -14.945 5.187   1.00 21.10 ?  59  ASN   B HD22 1 
ATOM   4577 N N    . ALA   B 1 60  ? 59.107 -14.116 0.734   1.00 13.88 ?  60  ALA   B N    1 
ATOM   4578 C CA   . ALA   B 1 60  ? 58.511 -12.783 0.662   1.00 13.80 ?  60  ALA   B CA   1 
ATOM   4579 C C    . ALA   B 1 60  ? 57.044 -12.810 1.065   1.00 12.73 ?  60  ALA   B C    1 
ATOM   4580 O O    . ALA   B 1 60  ? 56.539 -11.860 1.678   1.00 13.71 ?  60  ALA   B O    1 
ATOM   4581 C CB   . ALA   B 1 60  ? 58.674 -12.208 -0.744  1.00 14.61 ?  60  ALA   B CB   1 
ATOM   4582 H H    . ALA   B 1 60  ? 59.409 -14.426 -0.011  1.00 16.63 ?  60  ALA   B H    1 
ATOM   4583 H HA   . ALA   B 1 60  ? 58.981 -12.201 1.280   1.00 16.54 ?  60  ALA   B HA   1 
ATOM   4584 H HB1  . ALA   B 1 60  ? 58.276 -11.328 -0.769  1.00 17.51 ?  60  ALA   B HB1  1 
ATOM   4585 H HB2  . ALA   B 1 60  ? 59.623 -12.149 -0.955  1.00 17.51 ?  60  ALA   B HB2  1 
ATOM   4586 H HB3  . ALA   B 1 60  ? 58.234 -12.795 -1.378  1.00 17.51 ?  60  ALA   B HB3  1 
ATOM   4587 N N    . MET   B 1 61  ? 56.338 -13.887 0.719   1.00 12.59 ?  61  MET   B N    1 
ATOM   4588 C CA   . MET   B 1 61  ? 54.943 -14.011 1.114   1.00 12.09 ?  61  MET   B CA   1 
ATOM   4589 C C    . MET   B 1 61  ? 54.805 -14.016 2.634   1.00 12.01 ?  61  MET   B C    1 
ATOM   4590 O O    . MET   B 1 61  ? 53.907 -13.366 3.182   1.00 12.33 ?  61  MET   B O    1 
ATOM   4591 C CB   . MET   B 1 61  ? 54.359 -15.277 0.482   1.00 11.66 ?  61  MET   B CB   1 
ATOM   4592 C CG   . MET   B 1 61  ? 52.919 -15.572 0.902   1.00 11.83 ?  61  MET   B CG   1 
ATOM   4593 S SD   . MET   B 1 61  ? 52.276 -17.077 0.143   1.00 12.57 ?  61  MET   B SD   1 
ATOM   4594 C CE   . MET   B 1 61  ? 52.013 -16.491 -1.529  1.00 14.17 ?  61  MET   B CE   1 
ATOM   4595 H H    . MET   B 1 61  ? 56.645 -14.556 0.257   1.00 15.09 ?  61  MET   B H    1 
ATOM   4596 H HA   . MET   B 1 61  ? 54.455 -13.257 0.754   1.00 14.48 ?  61  MET   B HA   1 
ATOM   4597 H HB2  . MET   B 1 61  ? 54.365 -15.179 -0.486  1.00 13.97 ?  61  MET   B HB2  1 
ATOM   4598 H HB3  . MET   B 1 61  ? 54.904 -16.037 0.735   1.00 13.97 ?  61  MET   B HB3  1 
ATOM   4599 H HG2  . MET   B 1 61  ? 52.890 -15.694 1.866   1.00 14.18 ?  61  MET   B HG2  1 
ATOM   4600 H HG3  . MET   B 1 61  ? 52.355 -14.833 0.641   1.00 14.18 ?  61  MET   B HG3  1 
ATOM   4601 H HE1  . MET   B 1 61  ? 51.625 -17.207 -2.055  1.00 16.98 ?  61  MET   B HE1  1 
ATOM   4602 H HE2  . MET   B 1 61  ? 51.407 -15.733 -1.505  1.00 16.98 ?  61  MET   B HE2  1 
ATOM   4603 H HE3  . MET   B 1 61  ? 52.863 -16.222 -1.908  1.00 16.98 ?  61  MET   B HE3  1 
ATOM   4604 N N    . GLN   B 1 62  ? 55.685 -14.733 3.337   1.00 12.00 ?  62  GLN   B N    1 
ATOM   4605 C CA   . GLN   B 1 62  ? 55.583 -14.785 4.793   1.00 12.57 ?  62  GLN   B CA   1 
ATOM   4606 C C    . GLN   B 1 62  ? 55.867 -13.428 5.424   1.00 12.93 ?  62  GLN   B C    1 
ATOM   4607 O O    . GLN   B 1 62  ? 55.187 -13.023 6.373   1.00 13.36 ?  62  GLN   B O    1 
ATOM   4608 C CB   . GLN   B 1 62  ? 56.530 -15.842 5.361   1.00 12.69 ?  62  GLN   B CB   1 
ATOM   4609 C CG   . GLN   B 1 62  ? 56.306 -16.109 6.840   1.00 13.21 ?  62  GLN   B CG   1 
ATOM   4610 C CD   . GLN   B 1 62  ? 54.930 -16.707 7.086   1.00 12.71 ?  62  GLN   B CD   1 
ATOM   4611 O OE1  . GLN   B 1 62  ? 54.675 -17.856 6.728   1.00 13.33 ?  62  GLN   B OE1  1 
ATOM   4612 N NE2  . GLN   B 1 62  ? 54.017 -15.913 7.646   1.00 13.33 ?  62  GLN   B NE2  1 
ATOM   4613 H H    . GLN   B 1 62  ? 56.334 -15.192 2.999   1.00 14.37 ?  62  GLN   B H    1 
ATOM   4614 H HA   . GLN   B 1 62  ? 54.678 -15.039 5.028   1.00 15.06 ?  62  GLN   B HA   1 
ATOM   4615 H HB2  . GLN   B 1 62  ? 56.402 -16.676 4.880   1.00 15.20 ?  62  GLN   B HB2  1 
ATOM   4616 H HB3  . GLN   B 1 62  ? 57.447 -15.537 5.247   1.00 15.20 ?  62  GLN   B HB3  1 
ATOM   4617 H HG2  . GLN   B 1 62  ? 56.972 -16.743 7.150   1.00 15.83 ?  62  GLN   B HG2  1 
ATOM   4618 H HG3  . GLN   B 1 62  ? 56.372 -15.280 7.330   1.00 15.83 ?  62  GLN   B HG3  1 
ATOM   4619 H HE21 . GLN   B 1 62  ? 54.223 -15.114 7.873   1.00 15.97 ?  62  GLN   B HE21 1 
ATOM   4620 H HE22 . GLN   B 1 62  ? 53.224 -16.216 7.795   1.00 15.97 ?  62  GLN   B HE22 1 
ATOM   4621 N N    . VAL   B 1 63  ? 56.881 -12.716 4.930   1.00 13.38 ?  63  VAL   B N    1 
ATOM   4622 C CA   . VAL   B 1 63  ? 57.185 -11.398 5.484   1.00 14.24 ?  63  VAL   B CA   1 
ATOM   4623 C C    . VAL   B 1 63  ? 55.993 -10.464 5.307   1.00 13.68 ?  63  VAL   B C    1 
ATOM   4624 O O    . VAL   B 1 63  ? 55.580 -9.761  6.239   1.00 14.15 ?  63  VAL   B O    1 
ATOM   4625 C CB   . VAL   B 1 63  ? 58.471 -10.835 4.856   1.00 15.65 ?  63  VAL   B CB   1 
ATOM   4626 C CG1  . VAL   B 1 63  ? 58.706 -9.400  5.307   1.00 16.09 ?  63  VAL   B CG1  1 
ATOM   4627 C CG2  . VAL   B 1 63  ? 59.655 -11.710 5.235   1.00 16.22 ?  63  VAL   B CG2  1 
ATOM   4628 H H    . VAL   B 1 63  ? 57.392 -12.963 4.280   1.00 16.04 ?  63  VAL   B H    1 
ATOM   4629 H HA   . VAL   B 1 63  ? 57.347 -11.497 6.434   1.00 17.06 ?  63  VAL   B HA   1 
ATOM   4630 H HB   . VAL   B 1 63  ? 58.391 -10.842 3.890   1.00 18.76 ?  63  VAL   B HB   1 
ATOM   4631 H HG11 . VAL   B 1 63  ? 59.620 -9.151  5.102   1.00 19.28 ?  63  VAL   B HG11 1 
ATOM   4632 H HG12 . VAL   B 1 63  ? 58.091 -8.816  4.839   1.00 19.28 ?  63  VAL   B HG12 1 
ATOM   4633 H HG13 . VAL   B 1 63  ? 58.556 -9.344  6.265   1.00 19.28 ?  63  VAL   B HG13 1 
ATOM   4634 H HG21 . VAL   B 1 63  ? 60.465 -11.329 4.855   1.00 19.44 ?  63  VAL   B HG21 1 
ATOM   4635 H HG22 . VAL   B 1 63  ? 59.731 -11.735 6.204   1.00 19.44 ?  63  VAL   B HG22 1 
ATOM   4636 H HG23 . VAL   B 1 63  ? 59.516 -12.603 4.890   1.00 19.44 ?  63  VAL   B HG23 1 
ATOM   4637 N N    . GLU   B 1 64  ? 55.422 -10.448 4.103   1.00 13.15 ?  64  GLU   B N    1 
ATOM   4638 C CA   . GLU   B 1 64  ? 54.255 -9.613  3.834   1.00 12.56 ?  64  GLU   B CA   1 
ATOM   4639 C C    . GLU   B 1 64  ? 53.073 -10.016 4.711   1.00 12.18 ?  64  GLU   B C    1 
ATOM   4640 O O    . GLU   B 1 64  ? 52.326 -9.157  5.209   1.00 12.92 ?  64  GLU   B O    1 
ATOM   4641 C CB   . GLU   B 1 64  ? 53.885 -9.761  2.357   1.00 12.87 ?  64  GLU   B CB   1 
ATOM   4642 C CG   . GLU   B 1 64  ? 52.620 -9.024  1.927   1.00 12.94 ?  64  GLU   B CG   1 
ATOM   4643 C CD   . GLU   B 1 64  ? 52.088 -9.519  0.588   1.00 13.85 ?  64  GLU   B CD   1 
ATOM   4644 O OE1  . GLU   B 1 64  ? 52.272 -10.725 0.272   1.00 14.64 ?  64  GLU   B OE1  1 
ATOM   4645 O OE2  . GLU   B 1 64  ? 51.464 -8.708  -0.142  1.00 14.55 -1 64  GLU   B OE2  1 
ATOM   4646 H H    . GLU   B 1 64  ? 55.689 -10.913 3.429   1.00 15.75 ?  64  GLU   B H    1 
ATOM   4647 H HA   . GLU   B 1 64  ? 54.468 -8.686  4.011   1.00 15.05 ?  64  GLU   B HA   1 
ATOM   4648 H HB2  . GLU   B 1 64  ? 54.614 -9.407  1.819   1.00 15.42 ?  64  GLU   B HB2  1 
ATOM   4649 H HB3  . GLU   B 1 64  ? 53.760 -10.697 2.159   1.00 15.42 ?  64  GLU   B HB3  1 
ATOM   4650 H HG2  . GLU   B 1 64  ? 51.916 -9.160  2.587   1.00 15.51 ?  64  GLU   B HG2  1 
ATOM   4651 H HG3  . GLU   B 1 64  ? 52.809 -8.077  1.844   1.00 15.51 ?  64  GLU   B HG3  1 
ATOM   4652 N N    . SER   B 1 65  ? 52.891 -11.323 4.902   1.00 12.07 ?  65  SER   B N    1 
ATOM   4653 C CA   . SER   B 1 65  ? 51.783 -11.829 5.699   1.00 12.26 ?  65  SER   B CA   1 
ATOM   4654 C C    . SER   B 1 65  ? 51.913 -11.429 7.162   1.00 12.40 ?  65  SER   B C    1 
ATOM   4655 O O    . SER   B 1 65  ? 50.914 -11.058 7.794   1.00 12.78 ?  65  SER   B O    1 
ATOM   4656 C CB   . SER   B 1 65  ? 51.702 -13.352 5.564   1.00 12.58 ?  65  SER   B CB   1 
ATOM   4657 O OG   . SER   B 1 65  ? 51.344 -13.749 4.245   1.00 12.58 ?  65  SER   B OG   1 
ATOM   4658 H H    . SER   B 1 65  ? 53.402 -11.943 4.584   1.00 14.46 ?  65  SER   B H    1 
ATOM   4659 H HA   . SER   B 1 65  ? 50.951 -11.460 5.361   1.00 14.69 ?  65  SER   B HA   1 
ATOM   4660 H HB2  . SER   B 1 65  ? 52.564 -13.736 5.781   1.00 15.08 ?  65  SER   B HB2  1 
ATOM   4661 H HB3  . SER   B 1 65  ? 51.029 -13.688 6.182   1.00 15.08 ?  65  SER   B HB3  1 
ATOM   4662 H HG   . SER   B 1 65  ? 51.915 -13.460 3.695   1.00 15.08 ?  65  SER   B HG   1 
ATOM   4663 N N    . ASP   B 1 66  ? 53.120 -11.533 7.731   1.00 12.88 ?  66  ASP   B N    1 
ATOM   4664 C CA   . ASP   B 1 66  ? 53.307 -11.140 9.126   1.00 12.97 ?  66  ASP   B CA   1 
ATOM   4665 C C    . ASP   B 1 66  ? 52.993 -9.661  9.323   1.00 13.44 ?  66  ASP   B C    1 
ATOM   4666 O O    . ASP   B 1 66  ? 52.422 -9.266  10.346  1.00 13.90 ?  66  ASP   B O    1 
ATOM   4667 C CB   . ASP   B 1 66  ? 54.738 -11.442 9.574   1.00 14.37 ?  66  ASP   B CB   1 
ATOM   4668 C CG   . ASP   B 1 66  ? 55.016 -12.933 9.722   1.00 16.16 ?  66  ASP   B CG   1 
ATOM   4669 O OD1  . ASP   B 1 66  ? 54.068 -13.749 9.644   1.00 16.90 ?  66  ASP   B OD1  1 
ATOM   4670 O OD2  . ASP   B 1 66  ? 56.202 -13.286 9.935   1.00 18.96 -1 66  ASP   B OD2  1 
ATOM   4671 H H    . ASP   B 1 66  ? 53.822 -11.839 7.343   1.00 15.43 ?  66  ASP   B H    1 
ATOM   4672 H HA   . ASP   B 1 66  ? 52.705 -11.650 9.690   1.00 15.54 ?  66  ASP   B HA   1 
ATOM   4673 H HB2  . ASP   B 1 66  ? 55.358 -11.093 8.918   1.00 17.22 ?  66  ASP   B HB2  1 
ATOM   4674 H HB3  . ASP   B 1 66  ? 54.896 -11.020 10.437  1.00 17.22 ?  66  ASP   B HB3  1 
ATOM   4675 N N    . ASP   B 1 67  ? 53.371 -8.822  8.358   1.00 13.17 ?  67  ASP   B N    1 
ATOM   4676 C CA   . ASP   B 1 67  ? 53.024 -7.410  8.441   1.00 13.62 ?  67  ASP   B CA   1 
ATOM   4677 C C    . ASP   B 1 67  ? 51.512 -7.203  8.362   1.00 13.88 ?  67  ASP   B C    1 
ATOM   4678 O O    . ASP   B 1 67  ? 50.951 -6.392  9.111   1.00 14.36 ?  67  ASP   B O    1 
ATOM   4679 C CB   . ASP   B 1 67  ? 53.738 -6.646  7.334   1.00 14.79 ?  67  ASP   B CB   1 
ATOM   4680 C CG   . ASP   B 1 67  ? 53.316 -5.203  7.287   1.00 16.24 ?  67  ASP   B CG   1 
ATOM   4681 O OD1  . ASP   B 1 67  ? 53.819 -4.387  8.093   1.00 17.44 ?  67  ASP   B OD1  1 
ATOM   4682 O OD2  . ASP   B 1 67  ? 52.443 -4.902  6.461   1.00 17.24 -1 67  ASP   B OD2  1 
ATOM   4683 H H    . ASP   B 1 67  ? 53.826 -9.044  7.661   1.00 15.78 ?  67  ASP   B H    1 
ATOM   4684 H HA   . ASP   B 1 67  ? 53.331 -7.057  9.288   1.00 16.33 ?  67  ASP   B HA   1 
ATOM   4685 H HB2  . ASP   B 1 67  ? 54.699 -6.682  7.486   1.00 17.72 ?  67  ASP   B HB2  1 
ATOM   4686 H HB3  . ASP   B 1 67  ? 53.531 -7.057  6.474   1.00 17.72 ?  67  ASP   B HB3  1 
ATOM   4687 N N    . TYR   B 1 68  ? 50.836 -7.932  7.466   1.00 13.58 ?  68  TYR   B N    1 
ATOM   4688 C CA   . TYR   B 1 68  ? 49.379 -7.856  7.392   1.00 14.09 ?  68  TYR   B CA   1 
ATOM   4689 C C    . TYR   B 1 68  ? 48.744 -8.198  8.736   1.00 13.83 ?  68  TYR   B C    1 
ATOM   4690 O O    . TYR   B 1 68  ? 47.808 -7.521  9.182   1.00 14.34 ?  68  TYR   B O    1 
ATOM   4691 C CB   . TYR   B 1 68  ? 48.845 -8.795  6.301   1.00 14.76 ?  68  TYR   B CB   1 
ATOM   4692 C CG   . TYR   B 1 68  ? 47.334 -8.945  6.360   1.00 15.54 ?  68  TYR   B CG   1 
ATOM   4693 C CD1  . TYR   B 1 68  ? 46.743 -9.894  7.190   1.00 16.39 ?  68  TYR   B CD1  1 
ATOM   4694 C CD2  . TYR   B 1 68  ? 46.503 -8.115  5.625   1.00 16.91 ?  68  TYR   B CD2  1 
ATOM   4695 C CE1  . TYR   B 1 68  ? 45.378 -10.012 7.283   1.00 17.71 ?  68  TYR   B CE1  1 
ATOM   4696 C CE2  . TYR   B 1 68  ? 45.119 -8.239  5.705   1.00 17.42 ?  68  TYR   B CE2  1 
ATOM   4697 C CZ   . TYR   B 1 68  ? 44.577 -9.186  6.539   1.00 17.52 ?  68  TYR   B CZ   1 
ATOM   4698 O OH   . TYR   B 1 68  ? 43.212 -9.300  6.639   1.00 18.34 ?  68  TYR   B OH   1 
ATOM   4699 H H    . TYR   B 1 68  ? 51.195 -8.482  6.904   1.00 16.27 ?  68  TYR   B H    1 
ATOM   4700 H HA   . TYR   B 1 68  ? 49.127 -6.951  7.163   1.00 16.88 ?  68  TYR   B HA   1 
ATOM   4701 H HB2  . TYR   B 1 68  ? 49.073 -8.431  5.432   1.00 17.68 ?  68  TYR   B HB2  1 
ATOM   4702 H HB3  . TYR   B 1 68  ? 49.239 -9.672  6.413   1.00 17.68 ?  68  TYR   B HB3  1 
ATOM   4703 H HD1  . TYR   B 1 68  ? 47.285 -10.457 7.701   1.00 19.64 ?  68  TYR   B HD1  1 
ATOM   4704 H HD2  . TYR   B 1 68  ? 46.877 -7.467  5.078   1.00 20.27 ?  68  TYR   B HD2  1 
ATOM   4705 H HE1  . TYR   B 1 68  ? 44.998 -10.663 7.834   1.00 21.23 ?  68  TYR   B HE1  1 
ATOM   4706 H HE2  . TYR   B 1 68  ? 44.566 -7.678  5.214   1.00 20.88 ?  68  TYR   B HE2  1 
ATOM   4707 H HH   . TYR   B 1 68  ? 42.825 -8.752  6.123   1.00 21.99 ?  68  TYR   B HH   1 
ATOM   4708 N N    . ILE   B 1 69  ? 49.225 -9.263  9.384   1.00 13.33 ?  69  ILE   B N    1 
ATOM   4709 C CA   . ILE   B 1 69  ? 48.670 -9.689  10.668  1.00 13.96 ?  69  ILE   B CA   1 
ATOM   4710 C C    . ILE   B 1 69  ? 48.923 -8.642  11.745  1.00 13.45 ?  69  ILE   B C    1 
ATOM   4711 O O    . ILE   B 1 69  ? 48.054 -8.364  12.578  1.00 13.81 ?  69  ILE   B O    1 
ATOM   4712 C CB   . ILE   B 1 69  ? 49.251 -11.062 11.059  1.00 14.70 ?  69  ILE   B CB   1 
ATOM   4713 C CG1  . ILE   B 1 69  ? 48.720 -12.171 10.138  1.00 15.16 ?  69  ILE   B CG1  1 
ATOM   4714 C CG2  . ILE   B 1 69  ? 48.969 -11.377 12.522  1.00 15.73 ?  69  ILE   B CG2  1 
ATOM   4715 C CD1  . ILE   B 1 69  ? 47.251 -12.485 10.313  1.00 15.76 ?  69  ILE   B CD1  1 
ATOM   4716 H H    . ILE   B 1 69  ? 49.871 -9.755  9.101   1.00 15.98 ?  69  ILE   B H    1 
ATOM   4717 H HA   . ILE   B 1 69  ? 47.714 -9.789  10.575  1.00 16.73 ?  69  ILE   B HA   1 
ATOM   4718 H HB   . ILE   B 1 69  ? 50.217 -11.023 10.948  1.00 17.61 ?  69  ILE   B HB   1 
ATOM   4719 H HG12 . ILE   B 1 69  ? 48.856 -11.896 9.216   1.00 18.17 ?  69  ILE   B HG12 1 
ATOM   4720 H HG13 . ILE   B 1 69  ? 49.221 -12.984 10.310  1.00 18.17 ?  69  ILE   B HG13 1 
ATOM   4721 H HG21 . ILE   B 1 69  ? 49.107 -12.327 12.668  1.00 18.86 ?  69  ILE   B HG21 1 
ATOM   4722 H HG22 . ILE   B 1 69  ? 49.576 -10.869 13.081  1.00 18.86 ?  69  ILE   B HG22 1 
ATOM   4723 H HG23 . ILE   B 1 69  ? 48.051 -11.143 12.722  1.00 18.86 ?  69  ILE   B HG23 1 
ATOM   4724 H HD11 . ILE   B 1 69  ? 47.009 -13.189 9.694   1.00 18.89 ?  69  ILE   B HD11 1 
ATOM   4725 H HD12 . ILE   B 1 69  ? 47.098 -12.781 11.224  1.00 18.89 ?  69  ILE   B HD12 1 
ATOM   4726 H HD13 . ILE   B 1 69  ? 46.731 -11.690 10.129  1.00 18.89 ?  69  ILE   B HD13 1 
ATOM   4727 N N    . ALA   B 1 70  ? 50.120 -8.058  11.766  1.00 13.51 ?  70  ALA   B N    1 
ATOM   4728 C CA   . ALA   B 1 70  ? 50.402 -7.013  12.746  1.00 13.35 ?  70  ALA   B CA   1 
ATOM   4729 C C    . ALA   B 1 70  ? 49.401 -5.872  12.636  1.00 13.84 ?  70  ALA   B C    1 
ATOM   4730 O O    . ALA   B 1 70  ? 48.960 -5.327  13.652  1.00 14.52 ?  70  ALA   B O    1 
ATOM   4731 C CB   . ALA   B 1 70  ? 51.827 -6.489  12.559  1.00 14.11 ?  70  ALA   B CB   1 
ATOM   4732 H H    . ALA   B 1 70  ? 50.769 -8.248  11.240  1.00 16.19 ?  70  ALA   B H    1 
ATOM   4733 H HA   . ALA   B 1 70  ? 50.340 -7.388  13.641  1.00 16.00 ?  70  ALA   B HA   1 
ATOM   4734 H HB1  . ALA   B 1 70  ? 52.017 -5.831  13.247  1.00 16.90 ?  70  ALA   B HB1  1 
ATOM   4735 H HB2  . ALA   B 1 70  ? 52.452 -7.229  12.632  1.00 16.90 ?  70  ALA   B HB2  1 
ATOM   4736 H HB3  . ALA   B 1 70  ? 51.903 -6.081  11.681  1.00 16.90 ?  70  ALA   B HB3  1 
ATOM   4737 N N    . THR   B 1 71  ? 49.028 -5.508  11.412  1.00 14.27 ?  71  THR   B N    1 
ATOM   4738 C CA   . THR   B 1 71  ? 48.134 -4.374  11.199  1.00 15.11 ?  71  THR   B CA   1 
ATOM   4739 C C    . THR   B 1 71  ? 46.667 -4.741  11.410  1.00 15.78 ?  71  THR   B C    1 
ATOM   4740 O O    . THR   B 1 71  ? 45.890 -3.923  11.924  1.00 17.18 ?  71  THR   B O    1 
ATOM   4741 C CB   . THR   B 1 71  ? 48.353 -3.812  9.793   1.00 17.03 ?  71  THR   B CB   1 
ATOM   4742 O OG1  . THR   B 1 71  ? 49.679 -3.278  9.694   1.00 19.14 ?  71  THR   B OG1  1 
ATOM   4743 C CG2  . THR   B 1 71  ? 47.335 -2.729  9.465   1.00 17.98 ?  71  THR   B CG2  1 
ATOM   4744 H H    . THR   B 1 71  ? 49.284 -5.903  10.692  1.00 17.10 ?  71  THR   B H    1 
ATOM   4745 H HA   . THR   B 1 71  ? 48.359 -3.679  11.833  1.00 18.11 ?  71  THR   B HA   1 
ATOM   4746 H HB   . THR   B 1 71  ? 48.262 -4.523  9.141   1.00 20.42 ?  71  THR   B HB   1 
ATOM   4747 H HG1  . THR   B 1 71  ? 49.808 -2.948  8.927   1.00 22.94 ?  71  THR   B HG1  1 
ATOM   4748 H HG21 . THR   B 1 71  ? 47.640 -2.206  8.705   1.00 21.55 ?  71  THR   B HG21 1 
ATOM   4749 H HG22 . THR   B 1 71  ? 46.481 -3.129  9.248   1.00 21.55 ?  71  THR   B HG22 1 
ATOM   4750 H HG23 . THR   B 1 71  ? 47.226 -2.136  10.226  1.00 21.55 ?  71  THR   B HG23 1 
ATOM   4751 N N    . ASN   B 1 72  ? 46.270 -5.960  11.025  1.00 15.33 ?  72  ASN   B N    1 
ATOM   4752 C CA   . ASN   B 1 72  ? 44.865 -6.319  10.902  1.00 15.84 ?  72  ASN   B CA   1 
ATOM   4753 C C    . ASN   B 1 72  ? 44.398 -7.416  11.847  1.00 16.28 ?  72  ASN   B C    1 
ATOM   4754 O O    . ASN   B 1 72  ? 43.183 -7.577  12.017  1.00 17.52 ?  72  ASN   B O    1 
ATOM   4755 C CB   . ASN   B 1 72  ? 44.551 -6.745  9.459   1.00 16.59 ?  72  ASN   B CB   1 
ATOM   4756 C CG   . ASN   B 1 72  ? 44.827 -5.642  8.456   1.00 17.79 ?  72  ASN   B CG   1 
ATOM   4757 O OD1  . ASN   B 1 72  ? 45.846 -5.650  7.758   1.00 18.96 ?  72  ASN   B OD1  1 
ATOM   4758 N ND2  . ASN   B 1 72  ? 43.941 -4.669  8.402   1.00 19.62 ?  72  ASN   B ND2  1 
ATOM   4759 H H    . ASN   B 1 72  ? 46.811 -6.608  10.823  1.00 18.38 ?  72  ASN   B H    1 
ATOM   4760 H HA   . ASN   B 1 72  ? 44.336 -5.532  11.089  1.00 18.98 ?  72  ASN   B HA   1 
ATOM   4761 H HB2  . ASN   B 1 72  ? 45.100 -7.511  9.224   1.00 19.88 ?  72  ASN   B HB2  1 
ATOM   4762 H HB3  . ASN   B 1 72  ? 43.612 -6.979  9.394   1.00 19.88 ?  72  ASN   B HB3  1 
ATOM   4763 H HD21 . ASN   B 1 72  ? 44.050 -4.018  7.846   1.00 23.52 ?  72  ASN   B HD21 1 
ATOM   4764 H HD22 . ASN   B 1 72  ? 43.242 -4.690  8.902   1.00 23.52 ?  72  ASN   B HD22 1 
ATOM   4765 N N    . GLY   B 1 73  ? 45.301 -8.166  12.466  1.00 15.82 ?  73  GLY   B N    1 
ATOM   4766 C CA   . GLY   B 1 73  ? 44.906 -9.305  13.255  1.00 15.33 ?  73  GLY   B CA   1 
ATOM   4767 C C    . GLY   B 1 73  ? 44.542 -10.487 12.381  1.00 14.41 ?  73  GLY   B C    1 
ATOM   4768 O O    . GLY   B 1 73  ? 44.540 -10.405 11.149  1.00 14.03 ?  73  GLY   B O    1 
ATOM   4769 H H    . GLY   B 1 73  ? 46.151 -8.022  12.449  1.00 18.96 ?  73  GLY   B H    1 
ATOM   4770 H HA2  . GLY   B 1 73  ? 45.635 -9.559  13.843  1.00 18.37 ?  73  GLY   B HA2  1 
ATOM   4771 H HA3  . GLY   B 1 73  ? 44.137 -9.071  13.800  1.00 18.37 ?  73  GLY   B HA3  1 
ATOM   4772 N N    . PRO   B 1 74  ? 44.231 -11.612 13.017  1.00 14.36 ?  74  PRO   B N    1 
ATOM   4773 C CA   . PRO   B 1 74  ? 43.986 -12.846 12.270  1.00 13.73 ?  74  PRO   B CA   1 
ATOM   4774 C C    . PRO   B 1 74  ? 42.687 -12.790 11.480  1.00 13.29 ?  74  PRO   B C    1 
ATOM   4775 O O    . PRO   B 1 74  ? 41.747 -12.053 11.800  1.00 14.75 ?  74  PRO   B O    1 
ATOM   4776 C CB   . PRO   B 1 74  ? 43.909 -13.908 13.372  1.00 15.20 ?  74  PRO   B CB   1 
ATOM   4777 C CG   . PRO   B 1 74  ? 43.459 -13.155 14.582  1.00 16.77 ?  74  PRO   B CG   1 
ATOM   4778 C CD   . PRO   B 1 74  ? 44.125 -11.812 14.471  1.00 15.86 ?  74  PRO   B CD   1 
ATOM   4779 H HA   . PRO   B 1 74  ? 44.729 -13.037 11.672  1.00 16.45 ?  74  PRO   B HA   1 
ATOM   4780 H HB2  . PRO   B 1 74  ? 43.264 -14.587 13.121  1.00 18.22 ?  74  PRO   B HB2  1 
ATOM   4781 H HB3  . PRO   B 1 74  ? 44.787 -14.297 13.508  1.00 18.22 ?  74  PRO   B HB3  1 
ATOM   4782 H HG2  . PRO   B 1 74  ? 42.493 -13.062 14.568  1.00 20.10 ?  74  PRO   B HG2  1 
ATOM   4783 H HG3  . PRO   B 1 74  ? 43.750 -13.618 15.380  1.00 20.10 ?  74  PRO   B HG3  1 
ATOM   4784 H HD2  . PRO   B 1 74  ? 43.565 -11.124 14.873  1.00 19.01 ?  74  PRO   B HD2  1 
ATOM   4785 H HD3  . PRO   B 1 74  ? 45.005 -11.834 14.877  1.00 19.01 ?  74  PRO   B HD3  1 
ATOM   4786 N N    . LEU   B 1 75  ? 42.654 -13.602 10.428  1.00 12.67 ?  75  LEU   B N    1 
ATOM   4787 C CA   . LEU   B 1 75  ? 41.440 -13.811 9.661   1.00 12.93 ?  75  LEU   B CA   1 
ATOM   4788 C C    . LEU   B 1 75  ? 40.462 -14.670 10.460  1.00 13.57 ?  75  LEU   B C    1 
ATOM   4789 O O    . LEU   B 1 75  ? 40.803 -15.251 11.492  1.00 14.57 ?  75  LEU   B O    1 
ATOM   4790 C CB   . LEU   B 1 75  ? 41.760 -14.526 8.349   1.00 12.80 ?  75  LEU   B CB   1 
ATOM   4791 C CG   . LEU   B 1 75  ? 42.607 -13.780 7.309   1.00 14.52 ?  75  LEU   B CG   1 
ATOM   4792 C CD1  . LEU   B 1 75  ? 42.808 -14.637 6.060   1.00 16.27 ?  75  LEU   B CD1  1 
ATOM   4793 C CD2  . LEU   B 1 75  ? 42.008 -12.452 6.941   1.00 17.80 ?  75  LEU   B CD2  1 
ATOM   4794 H H    . LEU   B 1 75  ? 43.329 -14.047 10.133  1.00 15.18 ?  75  LEU   B H    1 
ATOM   4795 H HA   . LEU   B 1 75  ? 41.019 -12.961 9.459   1.00 15.49 ?  75  LEU   B HA   1 
ATOM   4796 H HB2  . LEU   B 1 75  ? 42.236 -15.346 8.561   1.00 15.33 ?  75  LEU   B HB2  1 
ATOM   4797 H HB3  . LEU   B 1 75  ? 40.923 -14.754 7.914   1.00 15.33 ?  75  LEU   B HB3  1 
ATOM   4798 H HG   . LEU   B 1 75  ? 43.485 -13.614 7.687   1.00 17.41 ?  75  LEU   B HG   1 
ATOM   4799 H HD11 . LEU   B 1 75  ? 43.352 -14.142 5.420   1.00 19.50 ?  75  LEU   B HD11 1 
ATOM   4800 H HD12 . LEU   B 1 75  ? 43.263 -15.459 6.305   1.00 19.50 ?  75  LEU   B HD12 1 
ATOM   4801 H HD13 . LEU   B 1 75  ? 41.946 -14.839 5.668   1.00 19.50 ?  75  LEU   B HD13 1 
ATOM   4802 H HD21 . LEU   B 1 75  ? 42.529 -12.056 6.228   1.00 21.34 ?  75  LEU   B HD21 1 
ATOM   4803 H HD22 . LEU   B 1 75  ? 41.094 -12.591 6.650   1.00 21.34 ?  75  LEU   B HD22 1 
ATOM   4804 H HD23 . LEU   B 1 75  ? 42.023 -11.876 7.722   1.00 21.34 ?  75  LEU   B HD23 1 
ATOM   4805 N N    . LYS   B 1 76  ? 39.230 -14.750 9.958   1.00 14.87 ?  76  LYS   B N    1 
ATOM   4806 C CA   . LYS   B 1 76  ? 38.243 -15.710 10.432  1.00 15.93 ?  76  LYS   B CA   1 
ATOM   4807 C C    . LYS   B 1 76  ? 38.341 -16.990 9.604   1.00 14.56 ?  76  LYS   B C    1 
ATOM   4808 O O    . LYS   B 1 76  ? 38.615 -16.944 8.406   1.00 14.28 ?  76  LYS   B O    1 
ATOM   4809 C CB   . LYS   B 1 76  ? 36.825 -15.142 10.250  1.00 18.12 ?  76  LYS   B CB   1 
ATOM   4810 C CG   . LYS   B 1 76  ? 36.550 -13.757 10.865  1.00 19.91 ?  76  LYS   B CG   1 
ATOM   4811 C CD   . LYS   B 1 76  ? 35.144 -13.234 10.501  1.00 21.07 ?  76  LYS   B CD   1 
ATOM   4812 C CE   . LYS   B 1 76  ? 34.886 -11.848 11.074  1.00 23.13 ?  76  LYS   B CE   1 
ATOM   4813 N NZ   . LYS   B 1 76  ? 33.597 -11.256 10.618  1.00 23.83 ?  76  LYS   B NZ   1 
ATOM   4814 H H    . LYS   B 1 76  ? 38.938 -14.254 9.317   1.00 17.82 ?  76  LYS   B H    1 
ATOM   4815 H HA   . LYS   B 1 76  ? 38.391 -15.924 11.365  1.00 19.09 ?  76  LYS   B HA   1 
ATOM   4816 H HB2  . LYS   B 1 76  ? 36.645 -15.071 9.300   1.00 21.72 ?  76  LYS   B HB2  1 
ATOM   4817 H HB3  . LYS   B 1 76  ? 36.195 -15.760 10.651  1.00 21.72 ?  76  LYS   B HB3  1 
ATOM   4818 H HG2  . LYS   B 1 76  ? 36.611 -13.819 11.832  1.00 23.87 ?  76  LYS   B HG2  1 
ATOM   4819 H HG3  . LYS   B 1 76  ? 37.207 -13.123 10.531  1.00 23.87 ?  76  LYS   B HG3  1 
ATOM   4820 H HD2  . LYS   B 1 76  ? 35.066 -13.183 9.534   1.00 25.26 ?  76  LYS   B HD2  1 
ATOM   4821 H HD3  . LYS   B 1 76  ? 34.477 -13.840 10.857  1.00 25.26 ?  76  LYS   B HD3  1 
ATOM   4822 H HE2  . LYS   B 1 76  ? 34.863 -11.909 12.041  1.00 27.73 ?  76  LYS   B HE2  1 
ATOM   4823 H HE3  . LYS   B 1 76  ? 35.603 -11.256 10.796  1.00 27.73 ?  76  LYS   B HE3  1 
ATOM   4824 H HZ1  . LYS   B 1 76  ? 33.488 -10.448 10.977  1.00 28.57 ?  76  LYS   B HZ1  1 
ATOM   4825 H HZ2  . LYS   B 1 76  ? 33.592 -11.179 9.730   1.00 28.57 ?  76  LYS   B HZ2  1 
ATOM   4826 H HZ3  . LYS   B 1 76  ? 32.917 -11.775 10.866  1.00 28.57 ?  76  LYS   B HZ3  1 
ATOM   4827 N N    . VAL   B 1 77  ? 38.102 -18.141 10.242  1.00 15.28 ?  77  VAL   B N    1 
ATOM   4828 C CA   . VAL   B 1 77  ? 37.888 -19.360 9.467   1.00 15.47 ?  77  VAL   B CA   1 
ATOM   4829 C C    . VAL   B 1 77  ? 36.693 -19.131 8.552   1.00 14.12 ?  77  VAL   B C    1 
ATOM   4830 O O    . VAL   B 1 77  ? 35.629 -18.687 8.999   1.00 14.31 ?  77  VAL   B O    1 
ATOM   4831 C CB   . VAL   B 1 77  ? 37.691 -20.575 10.388  1.00 17.05 ?  77  VAL   B CB   1 
ATOM   4832 C CG1  . VAL   B 1 77  ? 37.382 -21.815 9.557   1.00 17.90 ?  77  VAL   B CG1  1 
ATOM   4833 C CG2  . VAL   B 1 77  ? 38.927 -20.806 11.256  1.00 18.23 ?  77  VAL   B CG2  1 
ATOM   4834 H H    . VAL   B 1 77  ? 38.058 -18.237 11.090  1.00 18.31 ?  77  VAL   B H    1 
ATOM   4835 H HA   . VAL   B 1 77  ? 38.661 -19.524 8.908   1.00 18.54 ?  77  VAL   B HA   1 
ATOM   4836 H HB   . VAL   B 1 77  ? 36.933 -20.408 10.973  1.00 20.44 ?  77  VAL   B HB   1 
ATOM   4837 H HG11 . VAL   B 1 77  ? 37.414 -22.595 10.135  1.00 21.46 ?  77  VAL   B HG11 1 
ATOM   4838 H HG12 . VAL   B 1 77  ? 36.491 -21.732 9.174   1.00 21.46 ?  77  VAL   B HG12 1 
ATOM   4839 H HG13 . VAL   B 1 77  ? 38.038 -21.897 8.853   1.00 21.46 ?  77  VAL   B HG13 1 
ATOM   4840 H HG21 . VAL   B 1 77  ? 38.781 -21.594 11.800  1.00 21.86 ?  77  VAL   B HG21 1 
ATOM   4841 H HG22 . VAL   B 1 77  ? 39.692 -20.934 10.678  1.00 21.86 ?  77  VAL   B HG22 1 
ATOM   4842 H HG23 . VAL   B 1 77  ? 39.059 -20.030 11.821  1.00 21.86 ?  77  VAL   B HG23 1 
ATOM   4843 N N    . GLY   B 1 78  ? 36.870 -19.413 7.263   1.00 13.24 ?  78  GLY   B N    1 
ATOM   4844 C CA   . GLY   B 1 78  ? 35.895 -19.090 6.247   1.00 13.29 ?  78  GLY   B CA   1 
ATOM   4845 C C    . GLY   B 1 78  ? 36.139 -17.771 5.545   1.00 12.74 ?  78  GLY   B C    1 
ATOM   4846 O O    . GLY   B 1 78  ? 35.459 -17.484 4.554   1.00 13.44 ?  78  GLY   B O    1 
ATOM   4847 H H    . GLY   B 1 78  ? 37.567 -19.808 6.947   1.00 15.86 ?  78  GLY   B H    1 
ATOM   4848 H HA2  . GLY   B 1 78  ? 35.887 -19.786 5.577   1.00 15.92 ?  78  GLY   B HA2  1 
ATOM   4849 H HA3  . GLY   B 1 78  ? 35.014 -19.050 6.654   1.00 15.92 ?  78  GLY   B HA3  1 
ATOM   4850 N N    . GLY   B 1 79  ? 37.091 -16.964 6.026   1.00 12.70 ?  79  GLY   B N    1 
ATOM   4851 C CA   . GLY   B 1 79  ? 37.391 -15.670 5.447   1.00 12.47 ?  79  GLY   B CA   1 
ATOM   4852 C C    . GLY   B 1 79  ? 38.624 -15.689 4.556   1.00 11.85 ?  79  GLY   B C    1 
ATOM   4853 O O    . GLY   B 1 79  ? 39.235 -16.728 4.307   1.00 12.50 ?  79  GLY   B O    1 
ATOM   4854 H H    . GLY   B 1 79  ? 37.590 -17.153 6.698   1.00 15.22 ?  79  GLY   B H    1 
ATOM   4855 H HA2  . GLY   B 1 79  ? 36.638 -15.368 4.913   1.00 14.94 ?  79  GLY   B HA2  1 
ATOM   4856 H HA3  . GLY   B 1 79  ? 37.541 -15.024 6.154   1.00 14.94 ?  79  GLY   B HA3  1 
ATOM   4857 N N    . SER   B 1 80  ? 38.993 -14.495 4.081   1.00 11.84 ?  80  SER   B N    1 
ATOM   4858 C CA   . SER   B 1 80  ? 40.103 -14.368 3.148   1.00 11.49 ?  80  SER   B CA   1 
ATOM   4859 C C    . SER   B 1 80  ? 40.685 -12.962 3.203   1.00 11.46 ?  80  SER   B C    1 
ATOM   4860 O O    . SER   B 1 80  ? 40.066 -12.027 3.714   1.00 12.78 ?  80  SER   B O    1 
ATOM   4861 C CB   . SER   B 1 80  ? 39.672 -14.657 1.707   1.00 11.97 ?  80  SER   B CB   1 
ATOM   4862 O OG   . SER   B 1 80  ? 38.823 -13.644 1.201   1.00 13.37 ?  80  SER   B OG   1 
ATOM   4863 H H    . SER   B 1 80  ? 38.619 -13.748 4.284   1.00 14.19 ?  80  SER   B H    1 
ATOM   4864 H HA   . SER   B 1 80  ? 40.795 -14.997 3.400   1.00 13.77 ?  80  SER   B HA   1 
ATOM   4865 H HB2  . SER   B 1 80  ? 40.464 -14.707 1.145   1.00 14.34 ?  80  SER   B HB2  1 
ATOM   4866 H HB3  . SER   B 1 80  ? 39.201 -15.505 1.685   1.00 14.34 ?  80  SER   B HB3  1 
ATOM   4867 H HG   . SER   B 1 80  ? 38.129 -13.589 1.682   1.00 16.02 ?  80  SER   B HG   1 
ATOM   4868 N N    . CYS   B 1 81  ? 41.872 -12.817 2.615   1.00 11.35 ?  81  CYS   B N    1 
ATOM   4869 C CA   . CYS   B 1 81  ? 42.418 -11.505 2.301   1.00 11.56 ?  81  CYS   B CA   1 
ATOM   4870 C C    . CYS   B 1 81  ? 43.186 -11.591 0.991   1.00 10.85 ?  81  CYS   B C    1 
ATOM   4871 O O    . CYS   B 1 81  ? 43.694 -12.655 0.614   1.00 12.10 ?  81  CYS   B O    1 
ATOM   4872 C CB   . CYS   B 1 81  ? 43.317 -10.949 3.418   1.00 12.36 ?  81  CYS   B CB   1 
ATOM   4873 S SG   . CYS   B 1 81  ? 44.833 -11.893 3.665   1.00 12.69 ?  81  CYS   B SG   1 
ATOM   4874 H H    . CYS   B 1 81  ? 42.382 -13.470 2.376   1.00 13.59 ?  81  CYS   B H    1 
ATOM   4875 H HA   . CYS   B 1 81  ? 41.686 -10.879 2.172   1.00 13.84 ?  81  CYS   B HA   1 
ATOM   4876 H HB2  . CYS   B 1 81  ? 43.567 -10.038 3.199   1.00 14.81 ?  81  CYS   B HB2  1 
ATOM   4877 H HB3  . CYS   B 1 81  ? 42.817 -10.957 4.253   1.00 14.81 ?  81  CYS   B HB3  1 
ATOM   4878 H HG   . CYS   B 1 81  ? 45.464 -11.394 4.561   1.00 15.21 ?  81  CYS   B HG   1 
ATOM   4879 N N    . VAL   B 1 82  ? 43.288 -10.449 0.314   1.00 11.51 ?  82  VAL   B N    1 
ATOM   4880 C CA   . VAL   B 1 82  ? 44.054 -10.324 -0.922  1.00 11.50 ?  82  VAL   B CA   1 
ATOM   4881 C C    . VAL   B 1 82  ? 45.393 -9.681  -0.602  1.00 11.71 ?  82  VAL   B C    1 
ATOM   4882 O O    . VAL   B 1 82  ? 45.446 -8.564  -0.066  1.00 12.93 ?  82  VAL   B O    1 
ATOM   4883 C CB   . VAL   B 1 82  ? 43.307 -9.488  -1.973  1.00 12.54 ?  82  VAL   B CB   1 
ATOM   4884 C CG1  . VAL   B 1 82  ? 44.144 -9.355  -3.235  1.00 13.49 ?  82  VAL   B CG1  1 
ATOM   4885 C CG2  . VAL   B 1 82  ? 41.948 -10.086 -2.281  1.00 13.38 ?  82  VAL   B CG2  1 
ATOM   4886 H H    . VAL   B 1 82  ? 42.902 -9.713  0.549   1.00 13.79 ?  82  VAL   B H    1 
ATOM   4887 H HA   . VAL   B 1 82  ? 44.215 -11.205 -1.294  1.00 13.77 ?  82  VAL   B HA   1 
ATOM   4888 H HB   . VAL   B 1 82  ? 43.163 -8.599  -1.625  1.00 15.02 ?  82  VAL   B HB   1 
ATOM   4889 H HG11 . VAL   B 1 82  ? 43.582 -9.030  -3.959  1.00 16.16 ?  82  VAL   B HG11 1 
ATOM   4890 H HG12 . VAL   B 1 82  ? 44.866 -8.725  -3.076  1.00 16.16 ?  82  VAL   B HG12 1 
ATOM   4891 H HG13 . VAL   B 1 82  ? 44.509 -10.223 -3.471  1.00 16.16 ?  82  VAL   B HG13 1 
ATOM   4892 H HG21 . VAL   B 1 82  ? 41.515 -9.562  -2.979  1.00 16.04 ?  82  VAL   B HG21 1 
ATOM   4893 H HG22 . VAL   B 1 82  ? 42.059 -11.002 -2.587  1.00 16.04 ?  82  VAL   B HG22 1 
ATOM   4894 H HG23 . VAL   B 1 82  ? 41.402 -10.072 -1.479  1.00 16.04 ?  82  VAL   B HG23 1 
ATOM   4895 N N    . LEU   B 1 83  ? 46.472 -10.367 -0.972  1.00 11.34 ?  83  LEU   B N    1 
ATOM   4896 C CA   . LEU   B 1 83  ? 47.827 -9.854  -0.855  1.00 11.42 ?  83  LEU   B CA   1 
ATOM   4897 C C    . LEU   B 1 83  ? 48.527 -10.003 -2.207  1.00 11.19 ?  83  LEU   B C    1 
ATOM   4898 O O    . LEU   B 1 83  ? 47.923 -10.424 -3.198  1.00 11.38 ?  83  LEU   B O    1 
ATOM   4899 C CB   . LEU   B 1 83  ? 48.577 -10.531 0.301   1.00 12.00 ?  83  LEU   B CB   1 
ATOM   4900 C CG   . LEU   B 1 83  ? 48.078 -10.173 1.709   1.00 13.17 ?  83  LEU   B CG   1 
ATOM   4901 C CD1  . LEU   B 1 83  ? 48.719 -11.044 2.774   1.00 13.67 ?  83  LEU   B CD1  1 
ATOM   4902 C CD2  . LEU   B 1 83  ? 48.287 -8.688  2.034   1.00 14.31 ?  83  LEU   B CD2  1 
ATOM   4903 H H    . LEU   B 1 83  ? 46.432 -11.160 -1.310  1.00 13.59 ?  83  LEU   B H    1 
ATOM   4904 H HA   . LEU   B 1 83  ? 47.776 -8.908  -0.661  1.00 13.68 ?  83  LEU   B HA   1 
ATOM   4905 H HB2  . LEU   B 1 83  ? 48.503 -11.490 0.198   1.00 14.37 ?  83  LEU   B HB2  1 
ATOM   4906 H HB3  . LEU   B 1 83  ? 49.512 -10.271 0.247   1.00 14.37 ?  83  LEU   B HB3  1 
ATOM   4907 H HG   . LEU   B 1 83  ? 47.127 -10.340 1.740   1.00 15.79 ?  83  LEU   B HG   1 
ATOM   4908 H HD11 . LEU   B 1 83  ? 48.369 -10.788 3.644   1.00 16.39 ?  83  LEU   B HD11 1 
ATOM   4909 H HD12 . LEU   B 1 83  ? 48.502 -11.974 2.594   1.00 16.39 ?  83  LEU   B HD12 1 
ATOM   4910 H HD13 . LEU   B 1 83  ? 49.680 -10.920 2.755   1.00 16.39 ?  83  LEU   B HD13 1 
ATOM   4911 H HD21 . LEU   B 1 83  ? 48.070 -8.539  2.968   1.00 17.15 ?  83  LEU   B HD21 1 
ATOM   4912 H HD22 . LEU   B 1 83  ? 49.212 -8.455  1.866   1.00 17.15 ?  83  LEU   B HD22 1 
ATOM   4913 H HD23 . LEU   B 1 83  ? 47.703 -8.159  1.470   1.00 17.15 ?  83  LEU   B HD23 1 
ATOM   4914 N N    . SER   B 1 84  ? 49.805 -9.627  -2.264  1.00 12.16 ?  84  SER   B N    1 
ATOM   4915 C CA   . SER   B 1 84  ? 50.539 -9.746  -3.516  1.00 12.32 ?  84  SER   B CA   1 
ATOM   4916 C C    . SER   B 1 84  ? 50.700 -11.210 -3.921  1.00 11.60 ?  84  SER   B C    1 
ATOM   4917 O O    . SER   B 1 84  ? 50.819 -12.102 -3.082  1.00 11.52 ?  84  SER   B O    1 
ATOM   4918 C CB   . SER   B 1 84  ? 51.931 -9.134  -3.372  1.00 13.94 ?  84  SER   B CB   1 
ATOM   4919 O OG   . SER   B 1 84  ? 52.678 -9.364  -4.551  1.00 15.59 ?  84  SER   B OG   1 
ATOM   4920 H H    . SER   B 1 84  ? 50.250 -9.289  -1.610  1.00 14.56 ?  84  SER   B H    1 
ATOM   4921 H HA   . SER   B 1 84  ? 50.064 -9.282  -4.223  1.00 14.76 ?  84  SER   B HA   1 
ATOM   4922 H HB2  . SER   B 1 84  ? 51.839 -8.175  -3.222  1.00 16.71 ?  84  SER   B HB2  1 
ATOM   4923 H HB3  . SER   B 1 84  ? 52.383 -9.544  -2.620  1.00 16.71 ?  84  SER   B HB3  1 
ATOM   4924 H HG   . SER   B 1 84  ? 53.444 -9.013  -4.473  1.00 18.68 ?  84  SER   B HG   1 
ATOM   4925 N N    . GLY   B 1 85  ? 50.762 -11.442 -5.224  1.00 12.78 ?  85  GLY   B N    1 
ATOM   4926 C CA   . GLY   B 1 85  ? 51.114 -12.735 -5.760  1.00 13.44 ?  85  GLY   B CA   1 
ATOM   4927 C C    . GLY   B 1 85  ? 52.584 -12.923 -6.065  1.00 12.42 ?  85  GLY   B C    1 
ATOM   4928 O O    . GLY   B 1 85  ? 52.971 -14.003 -6.516  1.00 13.15 ?  85  GLY   B O    1 
ATOM   4929 H H    . GLY   B 1 85  ? 50.606 -10.856 -5.825  1.00 15.31 ?  85  GLY   B H    1 
ATOM   4930 H HA2  . GLY   B 1 85  ? 50.851 -13.424 -5.126  1.00 16.11 ?  85  GLY   B HA2  1 
ATOM   4931 H HA3  . GLY   B 1 85  ? 50.625 -12.882 -6.579  1.00 16.11 ?  85  GLY   B HA3  1 
ATOM   4932 N N    . HIS   B 1 86  ? 53.429 -11.919 -5.841  1.00 12.53 ?  86  HIS   B N    1 
ATOM   4933 C CA   . HIS   B 1 86  ? 54.894 -12.084 -5.927  1.00 12.69 ?  86  HIS   B CA   1 
ATOM   4934 C C    . HIS   B 1 86  ? 55.268 -12.598 -7.315  1.00 12.82 ?  86  HIS   B C    1 
ATOM   4935 O O    . HIS   B 1 86  ? 54.879 -11.988 -8.322  1.00 13.81 ?  86  HIS   B O    1 
ATOM   4936 C CB   . HIS   B 1 86  ? 55.396 -12.919 -4.751  1.00 12.88 ?  86  HIS   B CB   1 
ATOM   4937 C CG   . HIS   B 1 86  ? 55.079 -12.312 -3.426  1.00 12.82 ?  86  HIS   B CG   1 
ATOM   4938 N ND1  . HIS   B 1 86  ? 55.901 -11.392 -2.810  1.00 14.65 ?  86  HIS   B ND1  1 
ATOM   4939 C CD2  . HIS   B 1 86  ? 54.001 -12.457 -2.619  1.00 13.69 ?  86  HIS   B CD2  1 
ATOM   4940 C CE1  . HIS   B 1 86  ? 55.339 -11.000 -1.680  1.00 14.37 ?  86  HIS   B CE1  1 
ATOM   4941 N NE2  . HIS   B 1 86  ? 54.185 -11.628 -1.542  1.00 13.83 ?  86  HIS   B NE2  1 
ATOM   4942 H H    . HIS   B 1 86  ? 53.185 -11.125 -5.635  1.00 15.01 ?  86  HIS   B H    1 
ATOM   4943 H HA   . HIS   B 1 86  ? 55.298 -11.209 -5.835  1.00 15.20 ?  86  HIS   B HA   1 
ATOM   4944 H HB2  . HIS   B 1 86  ? 54.988 -13.797 -4.786  1.00 15.43 ?  86  HIS   B HB2  1 
ATOM   4945 H HB3  . HIS   B 1 86  ? 56.364 -13.005 -4.813  1.00 15.43 ?  86  HIS   B HB3  1 
ATOM   4946 H HD2  . HIS   B 1 86  ? 53.265 -13.007 -2.776  1.00 16.40 ?  86  HIS   B HD2  1 
ATOM   4947 H HE1  . HIS   B 1 86  ? 55.703 -10.399 -1.072  1.00 17.22 ?  86  HIS   B HE1  1 
ATOM   4948 H HE2  . HIS   B 1 86  ? 53.646 -11.551 -0.875  1.00 16.57 ?  86  HIS   B HE2  1 
ATOM   4949 N N    . ASN   B 1 87  ? 56.033 -13.685 -7.422  1.00 13.19 ?  87  ASN   B N    1 
ATOM   4950 C CA   . ASN   B 1 87  ? 56.427 -14.256 -8.699  1.00 14.19 ?  87  ASN   B CA   1 
ATOM   4951 C C    . ASN   B 1 87  ? 55.442 -15.297 -9.204  1.00 13.70 ?  87  ASN   B C    1 
ATOM   4952 O O    . ASN   B 1 87  ? 55.758 -16.005 -10.163 1.00 15.42 ?  87  ASN   B O    1 
ATOM   4953 C CB   . ASN   B 1 87  ? 57.823 -14.886 -8.586  1.00 15.93 ?  87  ASN   B CB   1 
ATOM   4954 C CG   . ASN   B 1 87  ? 57.885 -16.000 -7.547  1.00 17.09 ?  87  ASN   B CG   1 
ATOM   4955 O OD1  . ASN   B 1 87  ? 57.249 -15.919 -6.493  1.00 15.93 ?  87  ASN   B OD1  1 
ATOM   4956 N ND2  . ASN   B 1 87  ? 58.635 -17.063 -7.857  1.00 19.14 ?  87  ASN   B ND2  1 
ATOM   4957 H H    . ASN   B 1 87  ? 56.334 -14.124 -6.749  1.00 15.80 ?  87  ASN   B H    1 
ATOM   4958 H HA   . ASN   B 1 87  ? 56.470 -13.550 -9.358  1.00 17.00 ?  87  ASN   B HA   1 
ATOM   4959 H HB2  . ASN   B 1 87  ? 58.070 -15.261 -9.449  1.00 19.09 ?  87  ASN   B HB2  1 
ATOM   4960 H HB3  . ASN   B 1 87  ? 58.456 -14.200 -8.331  1.00 19.09 ?  87  ASN   B HB3  1 
ATOM   4961 H HD21 . ASN   B 1 87  ? 58.708 -17.717 -7.306  1.00 22.95 ?  87  ASN   B HD21 1 
ATOM   4962 H HD22 . ASN   B 1 87  ? 59.062 -17.087 -8.608  1.00 22.95 ?  87  ASN   B HD22 1 
ATOM   4963 N N    . LEU   B 1 88  ? 54.264 -15.401 -8.586  1.00 12.78 ?  88  LEU   B N    1 
ATOM   4964 C CA   . LEU   B 1 88  ? 53.285 -16.432 -8.913  1.00 13.00 ?  88  LEU   B CA   1 
ATOM   4965 C C    . LEU   B 1 88  ? 52.053 -15.914 -9.636  1.00 12.96 ?  88  LEU   B C    1 
ATOM   4966 O O    . LEU   B 1 88  ? 51.443 -16.663 -10.410 1.00 14.65 ?  88  LEU   B O    1 
ATOM   4967 C CB   . LEU   B 1 88  ? 52.816 -17.118 -7.626  1.00 14.07 ?  88  LEU   B CB   1 
ATOM   4968 C CG   . LEU   B 1 88  ? 53.935 -17.795 -6.846  1.00 16.45 ?  88  LEU   B CG   1 
ATOM   4969 C CD1  . LEU   B 1 88  ? 53.453 -18.161 -5.452  1.00 17.99 ?  88  LEU   B CD1  1 
ATOM   4970 C CD2  . LEU   B 1 88  ? 54.401 -19.024 -7.599  1.00 19.71 ?  88  LEU   B CD2  1 
ATOM   4971 H H    . LEU   B 1 88  ? 54.003 -14.871 -7.954  1.00 15.32 ?  88  LEU   B H    1 
ATOM   4972 H HA   . LEU   B 1 88  ? 53.699 -17.097 -9.473  1.00 15.58 ?  88  LEU   B HA   1 
ATOM   4973 H HB2  . LEU   B 1 88  ? 52.410 -16.455 -7.042  1.00 16.86 ?  88  LEU   B HB2  1 
ATOM   4974 H HB3  . LEU   B 1 88  ? 52.159 -17.796 -7.853  1.00 16.86 ?  88  LEU   B HB3  1 
ATOM   4975 H HG   . LEU   B 1 88  ? 54.682 -17.185 -6.761  1.00 19.71 ?  88  LEU   B HG   1 
ATOM   4976 H HD11 . LEU   B 1 88  ? 54.101 -18.753 -5.041  1.00 21.57 ?  88  LEU   B HD11 1 
ATOM   4977 H HD12 . LEU   B 1 88  ? 53.362 -17.351 -4.927  1.00 21.57 ?  88  LEU   B HD12 1 
ATOM   4978 H HD13 . LEU   B 1 88  ? 52.596 -18.607 -5.525  1.00 21.57 ?  88  LEU   B HD13 1 
ATOM   4979 H HD21 . LEU   B 1 88  ? 55.039 -19.505 -7.050  1.00 23.63 ?  88  LEU   B HD21 1 
ATOM   4980 H HD22 . LEU   B 1 88  ? 53.635 -19.588 -7.789  1.00 23.63 ?  88  LEU   B HD22 1 
ATOM   4981 H HD23 . LEU   B 1 88  ? 54.822 -18.746 -8.428  1.00 23.63 ?  88  LEU   B HD23 1 
ATOM   4982 N N    . ALA   B 1 89  ? 51.653 -14.675 -9.376  1.00 12.21 ?  89  ALA   B N    1 
ATOM   4983 C CA   . ALA   B 1 89  ? 50.357 -14.177 -9.814  1.00 11.67 ?  89  ALA   B CA   1 
ATOM   4984 C C    . ALA   B 1 89  ? 50.336 -12.688 -9.526  1.00 12.27 ?  89  ALA   B C    1 
ATOM   4985 O O    . ALA   B 1 89  ? 51.171 -12.180 -8.777  1.00 12.90 ?  89  ALA   B O    1 
ATOM   4986 C CB   . ALA   B 1 89  ? 49.228 -14.850 -9.043  1.00 12.12 ?  89  ALA   B CB   1 
ATOM   4987 H H    . ALA   B 1 89  ? 52.113 -14.091 -8.937  1.00 14.62 ?  89  ALA   B H    1 
ATOM   4988 H HA   . ALA   B 1 89  ? 50.237 -14.326 -10.769 1.00 13.98 ?  89  ALA   B HA   1 
ATOM   4989 H HB1  . ALA   B 1 89  ? 48.377 -14.512 -9.371  1.00 14.52 ?  89  ALA   B HB1  1 
ATOM   4990 H HB2  . ALA   B 1 89  ? 49.277 -15.809 -9.190  1.00 14.52 ?  89  ALA   B HB2  1 
ATOM   4991 H HB3  . ALA   B 1 89  ? 49.326 -14.651 -8.104  1.00 14.52 ?  89  ALA   B HB3  1 
ATOM   4992 N N    . LYS   B 1 90  ? 49.357 -11.988 -10.096 1.00 13.08 ?  90  LYS   B N    1 
ATOM   4993 C CA   . LYS   B 1 90  ? 49.163 -10.602 -9.688  1.00 13.23 ?  90  LYS   B CA   1 
ATOM   4994 C C    . LYS   B 1 90  ? 48.847 -10.529 -8.199  1.00 12.90 ?  90  LYS   B C    1 
ATOM   4995 O O    . LYS   B 1 90  ? 49.488 -9.779  -7.449  1.00 13.88 ?  90  LYS   B O    1 
ATOM   4996 C CB   . LYS   B 1 90  ? 48.077 -9.944  -10.538 1.00 14.69 ?  90  LYS   B CB   1 
ATOM   4997 C CG   . LYS   B 1 90  ? 47.781 -8.508  -10.156 1.00 15.07 ?  90  LYS   B CG   1 
ATOM   4998 C CD   . LYS   B 1 90  ? 48.986 -7.612  -10.251 1.00 17.78 ?  90  LYS   B CD   1 
ATOM   4999 C CE   . LYS   B 1 90  ? 48.535 -6.191  -10.020 1.00 19.97 ?  90  LYS   B CE   1 
ATOM   5000 N NZ   . LYS   B 1 90  ? 49.671 -5.256  -9.873  1.00 19.89 ?  90  LYS   B NZ   1 
ATOM   5001 H H    . LYS   B 1 90  ? 48.813 -12.281 -10.698 1.00 15.67 ?  90  LYS   B H    1 
ATOM   5002 H HA   . LYS   B 1 90  ? 49.986 -10.118 -9.839  1.00 15.86 ?  90  LYS   B HA   1 
ATOM   5003 H HB2  . LYS   B 1 90  ? 48.358 -9.950  -11.468 1.00 17.60 ?  90  LYS   B HB2  1 
ATOM   5004 H HB3  . LYS   B 1 90  ? 47.253 -10.452 -10.446 1.00 17.60 ?  90  LYS   B HB3  1 
ATOM   5005 H HG2  . LYS   B 1 90  ? 47.100 -8.158  -10.754 1.00 18.06 ?  90  LYS   B HG2  1 
ATOM   5006 H HG3  . LYS   B 1 90  ? 47.453 -8.482  -9.241  1.00 18.06 ?  90  LYS   B HG3  1 
ATOM   5007 H HD2  . LYS   B 1 90  ? 49.630 -7.851  -9.565  1.00 21.31 ?  90  LYS   B HD2  1 
ATOM   5008 H HD3  . LYS   B 1 90  ? 49.379 -7.679  -11.134 1.00 21.31 ?  90  LYS   B HD3  1 
ATOM   5009 H HE2  . LYS   B 1 90  ? 48.002 -5.897  -10.777 1.00 23.94 ?  90  LYS   B HE2  1 
ATOM   5010 H HE3  . LYS   B 1 90  ? 48.008 -6.148  -9.207  1.00 23.94 ?  90  LYS   B HE3  1 
ATOM   5011 H HZ1  . LYS   B 1 90  ? 49.373 -4.427  -9.741  1.00 23.84 ?  90  LYS   B HZ1  1 
ATOM   5012 H HZ2  . LYS   B 1 90  ? 50.177 -5.494  -9.182  1.00 23.84 ?  90  LYS   B HZ2  1 
ATOM   5013 H HZ3  . LYS   B 1 90  ? 50.171 -5.265  -10.612 1.00 23.84 ?  90  LYS   B HZ3  1 
ATOM   5014 N N    . HIS   B 1 91  ? 47.880 -11.342 -7.752  1.00 11.43 ?  91  HIS   B N    1 
ATOM   5015 C CA   . HIS   B 1 91  ? 47.407 -11.367 -6.380  1.00 11.46 ?  91  HIS   B CA   1 
ATOM   5016 C C    . HIS   B 1 91  ? 47.407 -12.796 -5.860  1.00 10.96 ?  91  HIS   B C    1 
ATOM   5017 O O    . HIS   B 1 91  ? 47.181 -13.748 -6.616  1.00 11.36 ?  91  HIS   B O    1 
ATOM   5018 C CB   . HIS   B 1 91  ? 45.954 -10.884 -6.268  1.00 12.99 ?  91  HIS   B CB   1 
ATOM   5019 C CG   . HIS   B 1 91  ? 45.748 -9.475  -6.698  1.00 16.38 ?  91  HIS   B CG   1 
ATOM   5020 N ND1  . HIS   B 1 91  ? 46.341 -8.403  -6.064  1.00 19.01 ?  91  HIS   B ND1  1 
ATOM   5021 C CD2  . HIS   B 1 91  ? 44.983 -8.953  -7.682  1.00 18.88 ?  91  HIS   B CD2  1 
ATOM   5022 C CE1  . HIS   B 1 91  ? 45.965 -7.280  -6.653  1.00 20.02 ?  91  HIS   B CE1  1 
ATOM   5023 N NE2  . HIS   B 1 91  ? 45.135 -7.589  -7.634  1.00 20.10 ?  91  HIS   B NE2  1 
ATOM   5024 H H    . HIS   B 1 91  ? 47.463 -11.905 -8.258  1.00 13.69 ?  91  HIS   B H    1 
ATOM   5025 H HA   . HIS   B 1 91  ? 47.973 -10.812 -5.817  1.00 13.73 ?  91  HIS   B HA   1 
ATOM   5026 H HB2  . HIS   B 1 91  ? 45.391 -11.445 -6.823  1.00 15.56 ?  91  HIS   B HB2  1 
ATOM   5027 H HB3  . HIS   B 1 91  ? 45.669 -10.953 -5.340  1.00 15.56 ?  91  HIS   B HB3  1 
ATOM   5028 H HD1  . HIS   B 1 91  ? 46.875 -8.453  -5.391  1.00 22.79 ?  91  HIS   B HD1  1 
ATOM   5029 H HD2  . HIS   B 1 91  ? 44.456 -9.416  -8.287  1.00 22.63 ?  91  HIS   B HD2  1 
ATOM   5030 H HE1  . HIS   B 1 91  ? 46.233 -6.418  -6.409  1.00 24.00 ?  91  HIS   B HE1  1 
ATOM   5031 N N    . CYS   B 1 92  ? 47.601 -12.931 -4.557  1.00 10.65 ?  92  CYS   B N    1 
ATOM   5032 C CA   . CYS   B 1 92  ? 47.294 -14.165 -3.844  1.00 10.54 ?  92  CYS   B CA   1 
ATOM   5033 C C    . CYS   B 1 92  ? 46.076 -13.925 -2.959  1.00 10.13 ?  92  CYS   B C    1 
ATOM   5034 O O    . CYS   B 1 92  ? 46.081 -13.019 -2.110  1.00 11.11 ?  92  CYS   B O    1 
ATOM   5035 C CB   . CYS   B 1 92  ? 48.472 -14.634 -2.995  1.00 10.81 ?  92  CYS   B CB   1 
ATOM   5036 S SG   . CYS   B 1 92  ? 48.116 -16.163 -2.087  1.00 11.07 ?  92  CYS   B SG   1 
ATOM   5037 H H    . CYS   B 1 92  ? 47.935 -12.314 -4.056  1.00 12.75 ?  92  CYS   B H    1 
ATOM   5038 H HA   . CYS   B 1 92  ? 47.087 -14.860 -4.491  1.00 12.63 ?  92  CYS   B HA   1 
ATOM   5039 H HB2  . CYS   B 1 92  ? 49.232 -14.794 -3.571  1.00 12.95 ?  92  CYS   B HB2  1 
ATOM   5040 H HB3  . CYS   B 1 92  ? 48.681 -13.942 -2.349  1.00 12.95 ?  92  CYS   B HB3  1 
ATOM   5041 H HG   . CYS   B 1 92  ? 49.093 -16.476 -1.467  1.00 13.26 ?  92  CYS   B HG   1 
ATOM   5042 N N    . LEU   B 1 93  ? 45.040 -14.733 -3.167  1.00 10.25 ?  93  LEU   B N    1 
ATOM   5043 C CA   . LEU   B 1 93  ? 43.864 -14.745 -2.307  1.00 10.35 ?  93  LEU   B CA   1 
ATOM   5044 C C    . LEU   B 1 93  ? 44.090 -15.808 -1.241  1.00 9.78  ?  93  LEU   B C    1 
ATOM   5045 O O    . LEU   B 1 93  ? 44.044 -17.011 -1.530  1.00 10.61 ?  93  LEU   B O    1 
ATOM   5046 C CB   . LEU   B 1 93  ? 42.604 -15.032 -3.117  1.00 10.81 ?  93  LEU   B CB   1 
ATOM   5047 C CG   . LEU   B 1 93  ? 41.305 -15.056 -2.310  1.00 11.62 ?  93  LEU   B CG   1 
ATOM   5048 C CD1  . LEU   B 1 93  ? 40.935 -13.672 -1.806  1.00 12.03 ?  93  LEU   B CD1  1 
ATOM   5049 C CD2  . LEU   B 1 93  ? 40.175 -15.646 -3.132  1.00 11.98 ?  93  LEU   B CD2  1 
ATOM   5050 H H    . LEU   B 1 93  ? 44.996 -15.305 -3.822  1.00 12.28 ?  93  LEU   B H    1 
ATOM   5051 H HA   . LEU   B 1 93  ? 43.772 -13.885 -1.880  1.00 12.39 ?  93  LEU   B HA   1 
ATOM   5052 H HB2  . LEU   B 1 93  ? 42.513 -14.339 -3.795  1.00 12.95 ?  93  LEU   B HB2  1 
ATOM   5053 H HB3  . LEU   B 1 93  ? 42.698 -15.893 -3.546  1.00 12.95 ?  93  LEU   B HB3  1 
ATOM   5054 H HG   . LEU   B 1 93  ? 41.432 -15.622 -1.537  1.00 13.93 ?  93  LEU   B HG   1 
ATOM   5055 H HD11 . LEU   B 1 93  ? 40.088 -13.721 -1.339  1.00 14.41 ?  93  LEU   B HD11 1 
ATOM   5056 H HD12 . LEU   B 1 93  ? 41.629 -13.356 -1.206  1.00 14.41 ?  93  LEU   B HD12 1 
ATOM   5057 H HD13 . LEU   B 1 93  ? 40.859 -13.068 -2.566  1.00 14.41 ?  93  LEU   B HD13 1 
ATOM   5058 H HD21 . LEU   B 1 93  ? 39.362 -15.642 -2.601  1.00 14.35 ?  93  LEU   B HD21 1 
ATOM   5059 H HD22 . LEU   B 1 93  ? 40.049 -15.113 -3.933  1.00 14.35 ?  93  LEU   B HD22 1 
ATOM   5060 H HD23 . LEU   B 1 93  ? 40.403 -16.559 -3.376  1.00 14.35 ?  93  LEU   B HD23 1 
ATOM   5061 N N    . HIS   B 1 94  ? 44.360 -15.374 -0.017  1.00 10.09 ?  94  HIS   B N    1 
ATOM   5062 C CA   . HIS   B 1 94  ? 44.585 -16.283 1.100   1.00 10.07 ?  94  HIS   B CA   1 
ATOM   5063 C C    . HIS   B 1 94  ? 43.223 -16.637 1.682   1.00 10.61 ?  94  HIS   B C    1 
ATOM   5064 O O    . HIS   B 1 94  ? 42.555 -15.765 2.237   1.00 12.00 ?  94  HIS   B O    1 
ATOM   5065 C CB   . HIS   B 1 94  ? 45.458 -15.607 2.155   1.00 10.62 ?  94  HIS   B CB   1 
ATOM   5066 C CG   . HIS   B 1 94  ? 46.838 -15.306 1.682   1.00 10.40 ?  94  HIS   B CG   1 
ATOM   5067 N ND1  . HIS   B 1 94  ? 47.865 -16.222 1.764   1.00 10.72 ?  94  HIS   B ND1  1 
ATOM   5068 C CD2  . HIS   B 1 94  ? 47.346 -14.199 1.086   1.00 10.64 ?  94  HIS   B CD2  1 
ATOM   5069 C CE1  . HIS   B 1 94  ? 48.953 -15.676 1.250   1.00 10.85 ?  94  HIS   B CE1  1 
ATOM   5070 N NE2  . HIS   B 1 94  ? 48.669 -14.449 0.837   1.00 10.84 ?  94  HIS   B NE2  1 
ATOM   5071 H H    . HIS   B 1 94  ? 44.419 -14.539 0.192   1.00 12.09 ?  94  HIS   B H    1 
ATOM   5072 H HA   . HIS   B 1 94  ? 45.018 -17.090 0.789   1.00 12.06 ?  94  HIS   B HA   1 
ATOM   5073 H HB2  . HIS   B 1 94  ? 45.045 -14.770 2.414   1.00 12.72 ?  94  HIS   B HB2  1 
ATOM   5074 H HB3  . HIS   B 1 94  ? 45.532 -16.194 2.920   1.00 12.72 ?  94  HIS   B HB3  1 
ATOM   5075 H HD2  . HIS   B 1 94  ? 46.893 -13.412 0.890   1.00 12.74 ?  94  HIS   B HD2  1 
ATOM   5076 H HE1  . HIS   B 1 94  ? 49.784 -16.096 1.191   1.00 13.00 ?  94  HIS   B HE1  1 
ATOM   5077 H HE2  . HIS   B 1 94  ? 49.228 -13.912 0.466   1.00 12.99 ?  94  HIS   B HE2  1 
ATOM   5078 N N    . VAL   B 1 95  ? 42.785 -17.889 1.527   1.00 10.42 ?  95  VAL   B N    1 
ATOM   5079 C CA   . VAL   B 1 95  ? 41.457 -18.324 1.961   1.00 10.41 ?  95  VAL   B CA   1 
ATOM   5080 C C    . VAL   B 1 95  ? 41.622 -19.362 3.056   1.00 10.82 ?  95  VAL   B C    1 
ATOM   5081 O O    . VAL   B 1 95  ? 42.397 -20.314 2.898   1.00 11.45 ?  95  VAL   B O    1 
ATOM   5082 C CB   . VAL   B 1 95  ? 40.635 -18.927 0.805   1.00 10.63 ?  95  VAL   B CB   1 
ATOM   5083 C CG1  . VAL   B 1 95  ? 39.261 -19.371 1.292   1.00 12.04 ?  95  VAL   B CG1  1 
ATOM   5084 C CG2  . VAL   B 1 95  ? 40.514 -17.944 -0.326  1.00 10.63 ?  95  VAL   B CG2  1 
ATOM   5085 H H    . VAL   B 1 95  ? 43.244 -18.517 1.155   1.00 12.48 ?  95  VAL   B H    1 
ATOM   5086 H HA   . VAL   B 1 95  ? 40.967 -17.569 2.324   1.00 12.46 ?  95  VAL   B HA   1 
ATOM   5087 H HB   . VAL   B 1 95  ? 41.093 -19.706 0.467   1.00 12.74 ?  95  VAL   B HB   1 
ATOM   5088 H HG11 . VAL   B 1 95  ? 38.696 -19.560 0.522   1.00 14.43 ?  95  VAL   B HG11 1 
ATOM   5089 H HG12 . VAL   B 1 95  ? 39.355 -20.172 1.830   1.00 14.43 ?  95  VAL   B HG12 1 
ATOM   5090 H HG13 . VAL   B 1 95  ? 38.861 -18.661 1.820   1.00 14.43 ?  95  VAL   B HG13 1 
ATOM   5091 H HG21 . VAL   B 1 95  ? 39.932 -18.317 -1.006  1.00 12.73 ?  95  VAL   B HG21 1 
ATOM   5092 H HG22 . VAL   B 1 95  ? 40.136 -17.117 0.015   1.00 12.73 ?  95  VAL   B HG22 1 
ATOM   5093 H HG23 . VAL   B 1 95  ? 41.394 -17.780 -0.693  1.00 12.73 ?  95  VAL   B HG23 1 
ATOM   5094 N N    . VAL   B 1 96  ? 40.899 -19.187 4.156   1.00 11.28 ?  96  VAL   B N    1 
ATOM   5095 C CA   . VAL   B 1 96  ? 40.983 -20.104 5.293   1.00 11.78 ?  96  VAL   B CA   1 
ATOM   5096 C C    . VAL   B 1 96  ? 39.792 -21.063 5.248   1.00 12.26 ?  96  VAL   B C    1 
ATOM   5097 O O    . VAL   B 1 96  ? 38.673 -20.704 5.629   1.00 12.85 ?  96  VAL   B O    1 
ATOM   5098 C CB   . VAL   B 1 96  ? 41.033 -19.355 6.629   1.00 12.77 ?  96  VAL   B CB   1 
ATOM   5099 C CG1  . VAL   B 1 96  ? 41.201 -20.352 7.777   1.00 13.35 ?  96  VAL   B CG1  1 
ATOM   5100 C CG2  . VAL   B 1 96  ? 42.144 -18.323 6.639   1.00 13.47 ?  96  VAL   B CG2  1 
ATOM   5101 H H    . VAL   B 1 96  ? 40.343 -18.544 4.272   1.00 13.51 ?  96  VAL   B H    1 
ATOM   5102 H HA   . VAL   B 1 96  ? 41.796 -20.632 5.220   1.00 14.11 ?  96  VAL   B HA   1 
ATOM   5103 H HB   . VAL   B 1 96  ? 40.190 -18.893 6.762   1.00 15.30 ?  96  VAL   B HB   1 
ATOM   5104 H HG11 . VAL   B 1 96  ? 41.387 -19.862 8.597   1.00 16.00 ?  96  VAL   B HG11 1 
ATOM   5105 H HG12 . VAL   B 1 96  ? 40.384 -20.865 7.882   1.00 16.00 ?  96  VAL   B HG12 1 
ATOM   5106 H HG13 . VAL   B 1 96  ? 41.942 -20.946 7.577   1.00 16.00 ?  96  VAL   B HG13 1 
ATOM   5107 H HG21 . VAL   B 1 96  ? 42.190 -17.916 7.521   1.00 16.15 ?  96  VAL   B HG21 1 
ATOM   5108 H HG22 . VAL   B 1 96  ? 42.983 -18.755 6.429   1.00 16.15 ?  96  VAL   B HG22 1 
ATOM   5109 H HG23 . VAL   B 1 96  ? 41.946 -17.640 5.975   1.00 16.15 ?  96  VAL   B HG23 1 
ATOM   5110 N N    . GLY   B 1 97  ? 40.021 -22.294 4.799   1.00 12.26 ?  97  GLY   B N    1 
ATOM   5111 C CA   . GLY   B 1 97  ? 39.048 -23.350 4.965   1.00 12.76 ?  97  GLY   B CA   1 
ATOM   5112 C C    . GLY   B 1 97  ? 39.184 -23.968 6.339   1.00 14.00 ?  97  GLY   B C    1 
ATOM   5113 O O    . GLY   B 1 97  ? 40.229 -23.845 6.992   1.00 14.69 ?  97  GLY   B O    1 
ATOM   5114 H H    . GLY   B 1 97  ? 40.742 -22.534 4.386   1.00 14.69 ?  97  GLY   B H    1 
ATOM   5115 H HA2  . GLY   B 1 97  ? 38.153 -22.976 4.855   1.00 15.29 ?  97  GLY   B HA2  1 
ATOM   5116 H HA3  . GLY   B 1 97  ? 39.181 -24.028 4.282   1.00 15.29 ?  97  GLY   B HA3  1 
ATOM   5117 N N    . PRO   B 1 98  ? 38.134 -24.649 6.806   1.00 14.85 ?  98  PRO   B N    1 
ATOM   5118 C CA   . PRO   B 1 98  ? 38.223 -25.342 8.095   1.00 15.96 ?  98  PRO   B CA   1 
ATOM   5119 C C    . PRO   B 1 98  ? 39.249 -26.464 8.056   1.00 15.68 ?  98  PRO   B C    1 
ATOM   5120 O O    . PRO   B 1 98  ? 39.362 -27.200 7.078   1.00 15.80 ?  98  PRO   B O    1 
ATOM   5121 C CB   . PRO   B 1 98  ? 36.803 -25.882 8.299   1.00 16.46 ?  98  PRO   B CB   1 
ATOM   5122 C CG   . PRO   B 1 98  ? 36.247 -26.018 6.929   1.00 15.96 ?  98  PRO   B CG   1 
ATOM   5123 C CD   . PRO   B 1 98  ? 36.815 -24.843 6.172   1.00 15.08 ?  98  PRO   B CD   1 
ATOM   5124 H HA   . PRO   B 1 98  ? 38.441 -24.717 8.795   1.00 19.13 ?  98  PRO   B HA   1 
ATOM   5125 H HB2  . PRO   B 1 98  ? 36.841 -26.747 8.738   1.00 19.73 ?  98  PRO   B HB2  1 
ATOM   5126 H HB3  . PRO   B 1 98  ? 36.281 -25.253 8.816   1.00 19.73 ?  98  PRO   B HB3  1 
ATOM   5127 H HG2  . PRO   B 1 98  ? 36.541 -26.859 6.538   1.00 19.13 ?  98  PRO   B HG2  1 
ATOM   5128 H HG3  . PRO   B 1 98  ? 35.279 -25.978 6.962   1.00 19.13 ?  98  PRO   B HG3  1 
ATOM   5129 H HD2  . PRO   B 1 98  ? 36.907 -25.067 5.225   1.00 18.07 ?  98  PRO   B HD2  1 
ATOM   5130 H HD3  . PRO   B 1 98  ? 36.257 -24.060 6.293   1.00 18.07 ?  98  PRO   B HD3  1 
ATOM   5131 N N    . ASN   B 1 99  ? 39.993 -26.593 9.145   1.00 16.94 ?  99  ASN   B N    1 
ATOM   5132 C CA   . ASN   B 1 99  ? 40.974 -27.665 9.302   1.00 18.03 ?  99  ASN   B CA   1 
ATOM   5133 C C    . ASN   B 1 99  ? 40.355 -28.749 10.183  1.00 20.52 ?  99  ASN   B C    1 
ATOM   5134 O O    . ASN   B 1 99  ? 40.279 -28.602 11.405  1.00 21.22 ?  99  ASN   B O    1 
ATOM   5135 C CB   . ASN   B 1 99  ? 42.250 -27.108 9.918   1.00 18.03 ?  99  ASN   B CB   1 
ATOM   5136 C CG   . ASN   B 1 99  ? 43.386 -28.111 9.918   1.00 18.69 ?  99  ASN   B CG   1 
ATOM   5137 O OD1  . ASN   B 1 99  ? 43.171 -29.304 10.098  1.00 19.60 ?  99  ASN   B OD1  1 
ATOM   5138 N ND2  . ASN   B 1 99  ? 44.599 -27.631 9.710   1.00 19.04 ?  99  ASN   B ND2  1 
ATOM   5139 H H    . ASN   B 1 99  ? 39.943 -26.064 9.817   1.00 20.30 ?  99  ASN   B H    1 
ATOM   5140 H HA   . ASN   B 1 99  ? 41.178 -28.053 8.439   1.00 21.61 ?  99  ASN   B HA   1 
ATOM   5141 H HB2  . ASN   B 1 99  ? 42.523 -26.334 9.414   1.00 21.61 ?  99  ASN   B HB2  1 
ATOM   5142 H HB3  . ASN   B 1 99  ? 42.063 -26.861 10.840  1.00 21.61 ?  99  ASN   B HB3  1 
ATOM   5143 H HD21 . ASN   B 1 99  ? 45.272 -28.160 9.698   1.00 22.83 ?  99  ASN   B HD21 1 
ATOM   5144 H HD22 . ASN   B 1 99  ? 44.705 -26.787 9.591   1.00 22.83 ?  99  ASN   B HD22 1 
ATOM   5145 N N    A VAL   B 1 100 ? 39.895 -29.835 9.555   0.66 22.67 ?  100 VAL   B N    1 
ATOM   5146 N N    B VAL   B 1 100 ? 39.914 -29.840 9.550   0.34 22.71 ?  100 VAL   B N    1 
ATOM   5147 C CA   A VAL   B 1 100 ? 39.286 -30.926 10.315  0.66 25.31 ?  100 VAL   B CA   1 
ATOM   5148 C CA   B VAL   B 1 100 ? 39.292 -30.934 10.293  0.34 25.05 ?  100 VAL   B CA   1 
ATOM   5149 C C    A VAL   B 1 100 ? 40.301 -31.578 11.248  0.66 25.78 ?  100 VAL   B C    1 
ATOM   5150 C C    B VAL   B 1 100 ? 40.296 -31.594 11.230  0.34 25.73 ?  100 VAL   B C    1 
ATOM   5151 O O    A VAL   B 1 100 ? 39.941 -32.055 12.332  0.66 26.52 ?  100 VAL   B O    1 
ATOM   5152 O O    B VAL   B 1 100 ? 39.924 -32.088 12.302  0.34 26.17 ?  100 VAL   B O    1 
ATOM   5153 C CB   A VAL   B 1 100 ? 38.619 -31.940 9.363   0.66 27.68 ?  100 VAL   B CB   1 
ATOM   5154 C CB   B VAL   B 1 100 ? 38.644 -31.939 9.320   0.34 26.69 ?  100 VAL   B CB   1 
ATOM   5155 C CG1  A VAL   B 1 100 ? 38.152 -33.172 10.128  0.66 28.61 ?  100 VAL   B CG1  1 
ATOM   5156 C CG1  B VAL   B 1 100 ? 38.146 -33.168 10.067  0.34 27.31 ?  100 VAL   B CG1  1 
ATOM   5157 C CG2  A VAL   B 1 100 ? 37.447 -31.288 8.643   0.66 28.30 ?  100 VAL   B CG2  1 
ATOM   5158 C CG2  B VAL   B 1 100 ? 37.498 -31.277 8.567   0.34 27.20 ?  100 VAL   B CG2  1 
ATOM   5159 H H    A VAL   B 1 100 ? 39.908 -29.955 8.700   0.66 27.18 ?  100 VAL   B H    1 
ATOM   5160 H H    B VAL   B 1 100 ? 39.962 -29.971 8.699   0.34 27.23 ?  100 VAL   B H    1 
ATOM   5161 H HA   A VAL   B 1 100 ? 38.578 -30.556 10.864  0.66 30.34 ?  100 VAL   B HA   1 
ATOM   5162 H HA   B VAL   B 1 100 ? 38.580 -30.569 10.838  0.34 30.03 ?  100 VAL   B HA   1 
ATOM   5163 H HB   A VAL   B 1 100 ? 39.260 -32.229 8.696   0.66 33.19 ?  100 VAL   B HB   1 
ATOM   5164 H HB   B VAL   B 1 100 ? 39.302 -32.233 8.670   0.34 32.01 ?  100 VAL   B HB   1 
ATOM   5165 H HG11 A VAL   B 1 100 ? 37.548 -33.684 9.565   0.66 34.31 ?  100 VAL   B HG11 1 
ATOM   5166 H HG11 B VAL   B 1 100 ? 37.552 -33.671 9.486   0.34 32.75 ?  100 VAL   B HG11 1 
ATOM   5167 H HG12 A VAL   B 1 100 ? 38.922 -33.715 10.360  0.66 34.31 ?  100 VAL   B HG12 1 
ATOM   5168 H HG12 B VAL   B 1 100 ? 38.904 -33.718 10.317  0.34 32.75 ?  100 VAL   B HG12 1 
ATOM   5169 H HG13 A VAL   B 1 100 ? 37.689 -32.889 10.932  0.66 34.31 ?  100 VAL   B HG13 1 
ATOM   5170 H HG13 B VAL   B 1 100 ? 37.665 -32.881 10.859  0.34 32.75 ?  100 VAL   B HG13 1 
ATOM   5171 H HG21 A VAL   B 1 100 ? 37.033 -31.940 8.055   0.66 33.94 ?  100 VAL   B HG21 1 
ATOM   5172 H HG21 B VAL   B 1 100 ? 37.091 -31.927 7.973   0.34 32.61 ?  100 VAL   B HG21 1 
ATOM   5173 H HG22 A VAL   B 1 100 ? 36.803 -30.983 9.302   0.66 33.94 ?  100 VAL   B HG22 1 
ATOM   5174 H HG22 B VAL   B 1 100 ? 36.842 -30.961 9.209   0.34 32.61 ?  100 VAL   B HG22 1 
ATOM   5175 H HG23 A VAL   B 1 100 ? 37.774 -30.537 8.127   0.66 33.94 ?  100 VAL   B HG23 1 
ATOM   5176 H HG23 B VAL   B 1 100 ? 37.847 -30.533 8.055   0.34 32.61 ?  100 VAL   B HG23 1 
ATOM   5177 N N    . ASN   B 1 101 ? 41.575 -31.624 10.848  1.00 26.19 ?  101 ASN   B N    1 
ATOM   5178 C CA   . ASN   B 1 101 ? 42.617 -32.155 11.727  1.00 27.79 ?  101 ASN   B CA   1 
ATOM   5179 C C    . ASN   B 1 101 ? 42.808 -31.317 12.988  1.00 30.38 ?  101 ASN   B C    1 
ATOM   5180 O O    . ASN   B 1 101 ? 43.438 -31.792 13.942  1.00 31.60 ?  101 ASN   B O    1 
ATOM   5181 C CB   . ASN   B 1 101 ? 43.937 -32.287 10.962  1.00 27.52 ?  101 ASN   B CB   1 
ATOM   5182 C CG   . ASN   B 1 101 ? 43.922 -33.441 9.974   1.00 27.13 ?  101 ASN   B CG   1 
ATOM   5183 O OD1  . ASN   B 1 101 ? 43.241 -34.440 10.187  1.00 27.65 ?  101 ASN   B OD1  1 
ATOM   5184 N ND2  . ASN   B 1 101 ? 44.669 -33.304 8.886   1.00 26.88 ?  101 ASN   B ND2  1 
ATOM   5185 H H    A ASN   B 1 101 ? 41.848 -31.380 10.072  0.66 31.40 ?  101 ASN   B H    1 
ATOM   5186 H H    B ASN   B 1 101 ? 41.854 -31.363 10.080  0.34 31.40 ?  101 ASN   B H    1 
ATOM   5187 H HA   . ASN   B 1 101 ? 42.358 -33.040 12.012  1.00 33.33 ?  101 ASN   B HA   1 
ATOM   5188 H HB2  . ASN   B 1 101 ? 44.107 -31.470 10.465  1.00 33.00 ?  101 ASN   B HB2  1 
ATOM   5189 H HB3  . ASN   B 1 101 ? 44.656 -32.443 11.594  1.00 33.00 ?  101 ASN   B HB3  1 
ATOM   5190 H HD21 . ASN   B 1 101 ? 44.691 -33.933 8.300   1.00 32.23 ?  101 ASN   B HD21 1 
ATOM   5191 H HD22 . ASN   B 1 101 ? 45.133 -32.589 8.767   1.00 32.23 ?  101 ASN   B HD22 1 
ATOM   5192 N N    . LYS   B 1 102 ? 42.291 -30.086 13.010  1.00 33.01 ?  102 LYS   B N    1 
ATOM   5193 C CA   . LYS   B 1 102 ? 42.250 -29.254 14.206  1.00 35.87 ?  102 LYS   B CA   1 
ATOM   5194 C C    . LYS   B 1 102 ? 40.859 -29.200 14.825  1.00 35.30 ?  102 LYS   B C    1 
ATOM   5195 O O    . LYS   B 1 102 ? 40.621 -28.383 15.719  1.00 35.93 ?  102 LYS   B O    1 
ATOM   5196 C CB   . LYS   B 1 102 ? 42.705 -27.829 13.885  1.00 39.56 ?  102 LYS   B CB   1 
ATOM   5197 C CG   . LYS   B 1 102 ? 44.164 -27.686 13.499  1.00 42.92 ?  102 LYS   B CG   1 
ATOM   5198 C CD   . LYS   B 1 102 ? 44.435 -26.277 12.996  1.00 46.17 ?  102 LYS   B CD   1 
ATOM   5199 C CE   . LYS   B 1 102 ? 45.919 -25.974 12.901  1.00 48.64 ?  102 LYS   B CE   1 
ATOM   5200 N NZ   . LYS   B 1 102 ? 46.145 -24.573 12.440  1.00 50.07 ?  102 LYS   B NZ   1 
ATOM   5201 H H    . LYS   B 1 102 ? 41.943 -29.700 12.325  1.00 39.59 ?  102 LYS   B H    1 
ATOM   5202 H HA   . LYS   B 1 102 ? 42.864 -29.617 14.865  1.00 43.02 ?  102 LYS   B HA   1 
ATOM   5203 H HB2  . LYS   B 1 102 ? 42.173 -27.493 13.148  1.00 47.45 ?  102 LYS   B HB2  1 
ATOM   5204 H HB3  . LYS   B 1 102 ? 42.557 -27.272 14.669  1.00 47.45 ?  102 LYS   B HB3  1 
ATOM   5205 H HG2  . LYS   B 1 102 ? 44.724 -27.849 14.274  1.00 51.48 ?  102 LYS   B HG2  1 
ATOM   5206 H HG3  . LYS   B 1 102 ? 44.373 -28.313 12.789  1.00 51.48 ?  102 LYS   B HG3  1 
ATOM   5207 H HD2  . LYS   B 1 102 ? 44.049 -26.177 12.110  1.00 55.38 ?  102 LYS   B HD2  1 
ATOM   5208 H HD3  . LYS   B 1 102 ? 44.035 -25.639 13.607  1.00 55.38 ?  102 LYS   B HD3  1 
ATOM   5209 H HE2  . LYS   B 1 102 ? 46.327 -26.079 13.776  1.00 58.35 ?  102 LYS   B HE2  1 
ATOM   5210 H HE3  . LYS   B 1 102 ? 46.332 -26.577 12.262  1.00 58.35 ?  102 LYS   B HE3  1 
ATOM   5211 H HZ1  . LYS   B 1 102 ? 47.017 -24.406 12.388  1.00 60.06 ?  102 LYS   B HZ1  1 
ATOM   5212 H HZ2  . LYS   B 1 102 ? 45.779 -24.455 11.637  1.00 60.06 ?  102 LYS   B HZ2  1 
ATOM   5213 H HZ3  . LYS   B 1 102 ? 45.774 -24.002 13.013  1.00 60.06 ?  102 LYS   B HZ3  1 
ATOM   5214 N N    . GLY   B 1 103 ? 39.931 -30.027 14.351  1.00 34.57 ?  103 GLY   B N    1 
ATOM   5215 C CA   . GLY   B 1 103 ? 38.596 -30.091 14.911  1.00 34.07 ?  103 GLY   B CA   1 
ATOM   5216 C C    . GLY   B 1 103 ? 37.649 -29.002 14.462  1.00 32.90 ?  103 GLY   B C    1 
ATOM   5217 O O    . GLY   B 1 103 ? 36.557 -28.883 15.030  1.00 33.45 ?  103 GLY   B O    1 
ATOM   5218 H H    . GLY   B 1 103 ? 40.056 -30.562 13.695  1.00 41.46 ?  103 GLY   B H    1 
ATOM   5219 H HA2  . GLY   B 1 103 ? 38.202 -30.947 14.677  1.00 40.86 ?  103 GLY   B HA2  1 
ATOM   5220 H HA3  . GLY   B 1 103 ? 38.657 -30.047 15.878  1.00 40.86 ?  103 GLY   B HA3  1 
ATOM   5221 N N    A GLU   B 1 104 ? 38.034 -28.195 13.475  0.66 31.53 ?  104 GLU   B N    1 
ATOM   5222 N N    B GLU   B 1 104 ? 38.014 -28.217 13.453  0.34 32.13 ?  104 GLU   B N    1 
ATOM   5223 C CA   A GLU   B 1 104 ? 37.192 -27.097 13.028  0.66 30.07 ?  104 GLU   B CA   1 
ATOM   5224 C CA   B GLU   B 1 104 ? 37.150 -27.142 12.994  0.34 31.17 ?  104 GLU   B CA   1 
ATOM   5225 C C    A GLU   B 1 104 ? 36.006 -27.619 12.218  0.66 30.55 ?  104 GLU   B C    1 
ATOM   5226 C C    B GLU   B 1 104 ? 35.991 -27.694 12.164  0.34 31.33 ?  104 GLU   B C    1 
ATOM   5227 O O    A GLU   B 1 104 ? 36.042 -28.707 11.634  0.66 31.24 ?  104 GLU   B O    1 
ATOM   5228 O O    B GLU   B 1 104 ? 36.071 -28.775 11.573  0.34 31.61 ?  104 GLU   B O    1 
ATOM   5229 C CB   A GLU   B 1 104 ? 38.022 -26.095 12.222  0.66 28.68 ?  104 GLU   B CB   1 
ATOM   5230 C CB   B GLU   B 1 104 ? 37.961 -26.114 12.205  0.34 30.26 ?  104 GLU   B CB   1 
ATOM   5231 C CG   A GLU   B 1 104 ? 39.133 -25.458 13.048  0.66 27.28 ?  104 GLU   B CG   1 
ATOM   5232 C CG   B GLU   B 1 104 ? 39.060 -25.476 13.043  0.34 29.46 ?  104 GLU   B CG   1 
ATOM   5233 C CD   A GLU   B 1 104 ? 40.069 -24.575 12.248  0.66 25.94 ?  104 GLU   B CD   1 
ATOM   5234 C CD   B GLU   B 1 104 ? 40.006 -24.611 12.236  0.34 28.83 ?  104 GLU   B CD   1 
ATOM   5235 O OE1  A GLU   B 1 104 ? 40.076 -24.652 11.002  0.66 23.77 ?  104 GLU   B OE1  1 
ATOM   5236 O OE1  B GLU   B 1 104 ? 39.939 -24.641 10.990  0.34 28.21 ?  104 GLU   B OE1  1 
ATOM   5237 O OE2  A GLU   B 1 104 ? 40.810 -23.798 12.883  0.66 26.26 -1 104 GLU   B OE2  1 
ATOM   5238 O OE2  B GLU   B 1 104 ? 40.821 -23.898 12.857  0.34 28.79 -1 104 GLU   B OE2  1 
ATOM   5239 H H    A GLU   B 1 104 ? 38.783 -28.257 13.058  0.66 37.81 ?  104 GLU   B H    1 
ATOM   5240 H H    B GLU   B 1 104 ? 38.758 -28.282 13.025  0.34 38.53 ?  104 GLU   B H    1 
ATOM   5241 H HA   A GLU   B 1 104 ? 36.846 -26.631 13.807  0.66 36.06 ?  104 GLU   B HA   1 
ATOM   5242 H HA   B GLU   B 1 104 ? 36.775 -26.692 13.765  0.34 37.38 ?  104 GLU   B HA   1 
ATOM   5243 H HB2  A GLU   B 1 104 ? 38.431 -26.552 11.472  0.66 34.39 ?  104 GLU   B HB2  1 
ATOM   5244 H HB2  B GLU   B 1 104 ? 38.375 -26.552 11.446  0.34 36.29 ?  104 GLU   B HB2  1 
ATOM   5245 H HB3  A GLU   B 1 104 ? 37.441 -25.385 11.904  0.66 34.39 ?  104 GLU   B HB3  1 
ATOM   5246 H HB3  B GLU   B 1 104 ? 37.368 -25.409 11.899  0.34 36.29 ?  104 GLU   B HB3  1 
ATOM   5247 H HG2  A GLU   B 1 104 ? 38.737 -24.908 13.742  0.66 32.72 ?  104 GLU   B HG2  1 
ATOM   5248 H HG2  B GLU   B 1 104 ? 38.653 -24.916 13.723  0.34 35.33 ?  104 GLU   B HG2  1 
ATOM   5249 H HG3  A GLU   B 1 104 ? 39.671 -26.156 13.450  0.66 32.72 ?  104 GLU   B HG3  1 
ATOM   5250 H HG3  B GLU   B 1 104 ? 39.583 -26.177 13.465  0.34 35.33 ?  104 GLU   B HG3  1 
ATOM   5251 N N    A ASP   B 1 105 ? 34.942 -26.818 12.190  0.66 30.10 ?  105 ASP   B N    1 
ATOM   5252 N N    B ASP   B 1 105 ? 34.901 -26.928 12.131  0.34 30.96 ?  105 ASP   B N    1 
ATOM   5253 C CA   A ASP   B 1 105 ? 33.664 -27.260 11.645  0.66 30.58 ?  105 ASP   B CA   1 
ATOM   5254 C CA   B ASP   B 1 105 ? 33.639 -27.398 11.569  0.34 30.99 ?  105 ASP   B CA   1 
ATOM   5255 C C    A ASP   B 1 105 ? 33.722 -27.318 10.122  0.66 28.55 ?  105 ASP   B C    1 
ATOM   5256 C C    B ASP   B 1 105 ? 33.717 -27.415 10.047  0.34 29.75 ?  105 ASP   B C    1 
ATOM   5257 O O    A ASP   B 1 105 ? 33.886 -26.289 9.459   0.66 27.51 ?  105 ASP   B O    1 
ATOM   5258 O O    B ASP   B 1 105 ? 33.940 -26.376 9.417   0.34 29.38 ?  105 ASP   B O    1 
ATOM   5259 C CB   A ASP   B 1 105 ? 32.559 -26.306 12.095  0.66 33.64 ?  105 ASP   B CB   1 
ATOM   5260 C CB   B ASP   B 1 105 ? 32.497 -26.498 12.037  0.34 32.28 ?  105 ASP   B CB   1 
ATOM   5261 C CG   A ASP   B 1 105 ? 31.179 -26.763 11.663  0.66 36.36 ?  105 ASP   B CG   1 
ATOM   5262 C CG   B ASP   B 1 105 ? 31.129 -27.063 11.691  0.34 33.51 ?  105 ASP   B CG   1 
ATOM   5263 O OD1  A ASP   B 1 105 ? 31.061 -27.869 11.096  0.66 36.75 ?  105 ASP   B OD1  1 
ATOM   5264 O OD1  B ASP   B 1 105 ? 31.068 -28.072 10.957  0.34 33.81 ?  105 ASP   B OD1  1 
ATOM   5265 O OD2  A ASP   B 1 105 ? 30.208 -26.008 11.889  0.66 37.85 -1 105 ASP   B OD2  1 
ATOM   5266 O OD2  B ASP   B 1 105 ? 30.114 -26.506 12.162  0.34 33.92 -1 105 ASP   B OD2  1 
ATOM   5267 H H    A ASP   B 1 105 ? 34.939 -26.010 12.483  0.66 36.09 ?  105 ASP   B H    1 
ATOM   5268 H H    B ASP   B 1 105 ? 34.868 -26.122 12.427  0.34 37.13 ?  105 ASP   B H    1 
ATOM   5269 H HA   A ASP   B 1 105 ? 33.459 -28.146 11.979  0.66 36.67 ?  105 ASP   B HA   1 
ATOM   5270 H HA   B ASP   B 1 105 ? 33.459 -28.300 11.877  0.34 37.17 ?  105 ASP   B HA   1 
ATOM   5271 H HB2  A ASP   B 1 105 ? 32.578 -26.233 13.064  0.66 40.34 ?  105 ASP   B HB2  1 
ATOM   5272 H HB2  B ASP   B 1 105 ? 32.544 -26.399 13.002  0.34 38.71 ?  105 ASP   B HB2  1 
ATOM   5273 H HB3  A ASP   B 1 105 ? 32.707 -25.436 11.696  0.66 40.34 ?  105 ASP   B HB3  1 
ATOM   5274 H HB3  B ASP   B 1 105 ? 32.583 -25.627 11.613  0.34 38.71 ?  105 ASP   B HB3  1 
ATOM   5275 N N    A ILE   B 1 106 ? 33.549 -28.523 9.572   0.66 28.06 ?  106 ILE   B N    1 
ATOM   5276 N N    B ILE   B 1 106 ? 33.517 -28.599 9.459   0.34 28.90 ?  106 ILE   B N    1 
ATOM   5277 C CA   A ILE   B 1 106 ? 33.551 -28.713 8.126   0.66 27.04 ?  106 ILE   B CA   1 
ATOM   5278 C CA   B ILE   B 1 106 ? 33.527 -28.747 8.009   0.34 28.14 ?  106 ILE   B CA   1 
ATOM   5279 C C    A ILE   B 1 106 ? 32.458 -27.895 7.447   0.66 25.65 ?  106 ILE   B C    1 
ATOM   5280 C C    B ILE   B 1 106 ? 32.430 -27.923 7.347   0.34 27.28 ?  106 ILE   B C    1 
ATOM   5281 O O    A ILE   B 1 106 ? 32.575 -27.571 6.260   0.66 24.85 ?  106 ILE   B O    1 
ATOM   5282 O O    B ILE   B 1 106 ? 32.507 -27.642 6.146   0.34 26.93 ?  106 ILE   B O    1 
ATOM   5283 C CB   A ILE   B 1 106 ? 33.447 -30.222 7.803   0.66 27.53 ?  106 ILE   B CB   1 
ATOM   5284 C CB   B ILE   B 1 106 ? 33.425 -30.245 7.640   0.34 28.33 ?  106 ILE   B CB   1 
ATOM   5285 C CG1  A ILE   B 1 106 ? 33.700 -30.484 6.317   0.66 27.48 ?  106 ILE   B CG1  1 
ATOM   5286 C CG1  B ILE   B 1 106 ? 33.721 -30.468 6.155   0.34 28.24 ?  106 ILE   B CG1  1 
ATOM   5287 C CG2  A ILE   B 1 106 ? 32.083 -30.765 8.215   0.66 28.26 ?  106 ILE   B CG2  1 
ATOM   5288 C CG2  B ILE   B 1 106 ? 32.049 -30.792 7.994   0.34 28.73 ?  106 ILE   B CG2  1 
ATOM   5289 C CD1  A ILE   B 1 106 ? 35.062 -30.028 5.848   0.66 27.25 ?  106 ILE   B CD1  1 
ATOM   5290 C CD1  B ILE   B 1 106 ? 35.087 -29.983 5.729   0.34 28.15 ?  106 ILE   B CD1  1 
ATOM   5291 H H    A ILE   B 1 106 ? 33.426 -29.243 10.021  0.66 33.64 ?  106 ILE   B H    1 
ATOM   5292 H H    B ILE   B 1 106 ? 33.384 -29.332 9.884   0.34 34.66 ?  106 ILE   B H    1 
ATOM   5293 H HA   A ILE   B 1 106 ? 34.397 -28.397 7.785   0.66 32.43 ?  106 ILE   B HA   1 
ATOM   5294 H HA   B ILE   B 1 106 ? 34.374 -28.416 7.680   0.34 33.74 ?  106 ILE   B HA   1 
ATOM   5295 H HB   A ILE   B 1 106 ? 34.125 -30.692 8.315   0.66 33.01 ?  106 ILE   B HB   1 
ATOM   5296 H HB   B ILE   B 1 106 ? 34.085 -30.730 8.157   0.34 33.98 ?  106 ILE   B HB   1 
ATOM   5297 H HG12 A ILE   B 1 106 ? 33.637 -31.439 6.153   0.66 32.95 ?  106 ILE   B HG12 1 
ATOM   5298 H HG12 B ILE   B 1 106 ? 33.676 -31.421 5.967   0.34 33.86 ?  106 ILE   B HG12 1 
ATOM   5299 H HG13 A ILE   B 1 106 ? 33.032 -30.016 5.795   0.66 32.95 ?  106 ILE   B HG13 1 
ATOM   5300 H HG13 B ILE   B 1 106 ? 33.060 -29.999 5.626   0.34 33.86 ?  106 ILE   B HG13 1 
ATOM   5301 H HG21 A ILE   B 1 106 ? 32.095 -31.733 8.149   0.66 33.88 ?  106 ILE   B HG21 1 
ATOM   5302 H HG21 B ILE   B 1 106 ? 32.064 -31.759 7.913   0.34 34.45 ?  106 ILE   B HG21 1 
ATOM   5303 H HG22 A ILE   B 1 106 ? 31.901 -30.500 9.131   0.66 33.88 ?  106 ILE   B HG22 1 
ATOM   5304 H HG22 B ILE   B 1 106 ? 31.836 -30.542 8.907   0.34 34.45 ?  106 ILE   B HG22 1 
ATOM   5305 H HG23 A ILE   B 1 106 ? 31.405 -30.401 7.625   0.66 33.88 ?  106 ILE   B HG23 1 
ATOM   5306 H HG23 B ILE   B 1 106 ? 31.391 -30.420 7.387   0.34 34.45 ?  106 ILE   B HG23 1 
ATOM   5307 H HD11 A ILE   B 1 106 ? 35.256 -30.441 4.993   0.66 32.68 ?  106 ILE   B HD11 1 
ATOM   5308 H HD11 B ILE   B 1 106 ? 35.312 -30.387 4.879   0.34 33.76 ?  106 ILE   B HD11 1 
ATOM   5309 H HD12 A ILE   B 1 106 ? 35.059 -29.062 5.755   0.66 32.68 ?  106 ILE   B HD12 1 
ATOM   5310 H HD12 B ILE   B 1 106 ? 35.066 -29.017 5.642   0.34 33.76 ?  106 ILE   B HD12 1 
ATOM   5311 H HD13 A ILE   B 1 106 ? 35.728 -30.295 6.502   0.66 32.68 ?  106 ILE   B HD13 1 
ATOM   5312 H HD13 B ILE   B 1 106 ? 35.736 -30.243 6.402   0.34 33.76 ?  106 ILE   B HD13 1 
ATOM   5313 N N    A GLN   B 1 107 ? 31.396 -27.542 8.176   0.66 25.86 ?  107 GLN   B N    1 
ATOM   5314 N N    B GLN   B 1 107 ? 31.405 -27.524 8.103   0.34 27.15 ?  107 GLN   B N    1 
ATOM   5315 C CA   A GLN   B 1 107 ? 30.325 -26.731 7.604   0.66 26.11 ?  107 GLN   B CA   1 
ATOM   5316 C CA   B GLN   B 1 107 ? 30.326 -26.720 7.541   0.34 26.93 ?  107 GLN   B CA   1 
ATOM   5317 C C    A GLN   B 1 107 ? 30.820 -25.385 7.083   0.66 23.90 ?  107 GLN   B C    1 
ATOM   5318 C C    B GLN   B 1 107 ? 30.809 -25.351 7.081   0.34 24.46 ?  107 GLN   B C    1 
ATOM   5319 O O    A GLN   B 1 107 ? 30.189 -24.817 6.187   0.66 24.49 ?  107 GLN   B O    1 
ATOM   5320 O O    B GLN   B 1 107 ? 30.153 -24.728 6.240   0.34 24.84 ?  107 GLN   B O    1 
ATOM   5321 C CB   A GLN   B 1 107 ? 29.221 -26.519 8.646   0.66 29.86 ?  107 GLN   B CB   1 
ATOM   5322 C CB   B GLN   B 1 107 ? 29.203 -26.568 8.572   0.34 29.59 ?  107 GLN   B CB   1 
ATOM   5323 C CG   A GLN   B 1 107 ? 27.889 -26.042 8.073   0.66 33.46 ?  107 GLN   B CG   1 
ATOM   5324 C CG   B GLN   B 1 107 ? 27.872 -26.089 8.003   0.34 32.05 ?  107 GLN   B CG   1 
ATOM   5325 C CD   A GLN   B 1 107 ? 27.808 -24.531 7.929   0.66 36.22 ?  107 GLN   B CD   1 
ATOM   5326 C CD   B GLN   B 1 107 ? 27.753 -24.577 7.966   0.34 34.00 ?  107 GLN   B CD   1 
ATOM   5327 O OE1  A GLN   B 1 107 ? 28.637 -23.798 8.471   0.66 37.24 ?  107 GLN   B OE1  1 
ATOM   5328 O OE1  B GLN   B 1 107 ? 28.570 -23.862 8.549   0.34 34.69 ?  107 GLN   B OE1  1 
ATOM   5329 N NE2  A GLN   B 1 107 ? 26.801 -24.059 7.198   0.66 37.18 ?  107 GLN   B NE2  1 
ATOM   5330 N NE2  B GLN   B 1 107 ? 26.728 -24.081 7.281   0.34 34.69 ?  107 GLN   B NE2  1 
ATOM   5331 H H    A GLN   B 1 107 ? 31.273 -27.763 8.993   0.66 31.01 ?  107 GLN   B H    1 
ATOM   5332 H H    B GLN   B 1 107 ? 31.311 -27.704 8.936   0.34 32.56 ?  107 GLN   B H    1 
ATOM   5333 H HA   A GLN   B 1 107 ? 29.933 -27.211 6.856   0.66 31.31 ?  107 GLN   B HA   1 
ATOM   5334 H HA   B GLN   B 1 107 ? 29.960 -27.180 6.771   0.34 32.29 ?  107 GLN   B HA   1 
ATOM   5335 H HB2  A GLN   B 1 107 ? 29.059 -27.359 9.100   0.66 35.81 ?  107 GLN   B HB2  1 
ATOM   5336 H HB2  B GLN   B 1 107 ? 29.048 -27.429 8.983   0.34 35.49 ?  107 GLN   B HB2  1 
ATOM   5337 H HB3  A GLN   B 1 107 ? 29.523 -25.856 9.287   0.66 35.81 ?  107 GLN   B HB3  1 
ATOM   5338 H HB3  B GLN   B 1 107 ? 29.483 -25.930 9.246   0.34 35.49 ?  107 GLN   B HB3  1 
ATOM   5339 H HG2  A GLN   B 1 107 ? 27.764 -26.430 7.194   0.66 40.13 ?  107 GLN   B HG2  1 
ATOM   5340 H HG2  B GLN   B 1 107 ? 27.777 -26.417 7.096   0.34 38.44 ?  107 GLN   B HG2  1 
ATOM   5341 H HG3  A GLN   B 1 107 ? 27.171 -26.327 8.664   0.66 40.13 ?  107 GLN   B HG3  1 
ATOM   5342 H HG3  B GLN   B 1 107 ? 27.150 -26.436 8.556   0.34 38.44 ?  107 GLN   B HG3  1 
ATOM   5343 H HE21 A GLN   B 1 107 ? 26.241 -24.603 6.833   0.66 44.59 ?  107 GLN   B HE21 1 
ATOM   5344 H HE21 B GLN   B 1 107 ? 26.178 -24.611 6.885   0.34 41.60 ?  107 GLN   B HE21 1 
ATOM   5345 H HE22 A GLN   B 1 107 ? 26.705 -23.211 7.089   0.66 44.59 ?  107 GLN   B HE22 1 
ATOM   5346 H HE22 B GLN   B 1 107 ? 26.615 -23.230 7.233   0.34 41.60 ?  107 GLN   B HE22 1 
ATOM   5347 N N    . LEU   B 1 108 ? 31.940 -24.872 7.604   1.00 21.98 ?  108 LEU   B N    1 
ATOM   5348 C CA   . LEU   B 1 108 ? 32.485 -23.574 7.192   1.00 19.29 ?  108 LEU   B CA   1 
ATOM   5349 C C    . LEU   B 1 108 ? 33.131 -23.598 5.815   1.00 16.68 ?  108 LEU   B C    1 
ATOM   5350 O O    . LEU   B 1 108 ? 33.565 -22.543 5.328   1.00 16.08 ?  108 LEU   B O    1 
ATOM   5351 C CB   . LEU   B 1 108 ? 33.491 -23.075 8.230   1.00 20.07 ?  108 LEU   B CB   1 
ATOM   5352 C CG   . LEU   B 1 108 ? 32.878 -22.512 9.513   1.00 21.52 ?  108 LEU   B CG   1 
ATOM   5353 C CD1  . LEU   B 1 108 ? 33.886 -22.502 10.646  1.00 21.78 ?  108 LEU   B CD1  1 
ATOM   5354 C CD2  . LEU   B 1 108 ? 32.360 -21.105 9.261   1.00 22.21 ?  108 LEU   B CD2  1 
ATOM   5355 H H    A LEU   B 1 108 ? 32.401 -25.262 8.211   0.66 26.35 ?  108 LEU   B H    1 
ATOM   5356 H H    B LEU   B 1 108 ? 32.399 -25.274 8.204   0.34 26.35 ?  108 LEU   B H    1 
ATOM   5357 H HA   . LEU   B 1 108 ? 31.758 -22.936 7.162   1.00 23.12 ?  108 LEU   B HA   1 
ATOM   5358 H HB2  . LEU   B 1 108 ? 34.063 -23.813 8.489   1.00 24.06 ?  108 LEU   B HB2  1 
ATOM   5359 H HB3  . LEU   B 1 108 ? 34.022 -22.371 7.832   1.00 24.06 ?  108 LEU   B HB3  1 
ATOM   5360 H HG   . LEU   B 1 108 ? 32.125 -23.062 9.783   1.00 25.81 ?  108 LEU   B HG   1 
ATOM   5361 H HD11 . LEU   B 1 108 ? 33.447 -22.205 11.460  1.00 26.11 ?  108 LEU   B HD11 1 
ATOM   5362 H HD12 . LEU   B 1 108 ? 34.233 -23.399 10.766  1.00 26.11 ?  108 LEU   B HD12 1 
ATOM   5363 H HD13 . LEU   B 1 108 ? 34.608 -21.894 10.421  1.00 26.11 ?  108 LEU   B HD13 1 
ATOM   5364 H HD21 . LEU   B 1 108 ? 31.991 -20.749 10.084  1.00 26.63 ?  108 LEU   B HD21 1 
ATOM   5365 H HD22 . LEU   B 1 108 ? 33.096 -20.548 8.961   1.00 26.63 ?  108 LEU   B HD22 1 
ATOM   5366 H HD23 . LEU   B 1 108 ? 31.672 -21.139 8.577   1.00 26.63 ?  108 LEU   B HD23 1 
ATOM   5367 N N    . LEU   B 1 109 ? 33.191 -24.766 5.181   1.00 15.53 ?  109 LEU   B N    1 
ATOM   5368 C CA   . LEU   B 1 109 ? 33.820 -24.877 3.873   1.00 14.78 ?  109 LEU   B CA   1 
ATOM   5369 C C    . LEU   B 1 109 ? 33.055 -24.093 2.814   1.00 13.97 ?  109 LEU   B C    1 
ATOM   5370 O O    . LEU   B 1 109 ? 33.671 -23.497 1.921   1.00 13.71 ?  109 LEU   B O    1 
ATOM   5371 C CB   . LEU   B 1 109 ? 33.935 -26.355 3.496   1.00 14.74 ?  109 LEU   B CB   1 
ATOM   5372 C CG   . LEU   B 1 109 ? 34.723 -26.692 2.233   1.00 14.42 ?  109 LEU   B CG   1 
ATOM   5373 C CD1  . LEU   B 1 109 ? 36.104 -26.041 2.249   1.00 14.13 ?  109 LEU   B CD1  1 
ATOM   5374 C CD2  . LEU   B 1 109 ? 34.844 -28.207 2.080   1.00 15.24 ?  109 LEU   B CD2  1 
ATOM   5375 H H    . LEU   B 1 109 ? 32.881 -25.509 5.486   1.00 18.61 ?  109 LEU   B H    1 
ATOM   5376 H HA   . LEU   B 1 109 ? 34.716 -24.511 3.925   1.00 17.71 ?  109 LEU   B HA   1 
ATOM   5377 H HB2  . LEU   B 1 109 ? 34.366 -26.822 4.230   1.00 17.67 ?  109 LEU   B HB2  1 
ATOM   5378 H HB3  . LEU   B 1 109 ? 33.040 -26.709 3.376   1.00 17.67 ?  109 LEU   B HB3  1 
ATOM   5379 H HG   . LEU   B 1 109 ? 34.240 -26.364 1.459   1.00 17.28 ?  109 LEU   B HG   1 
ATOM   5380 H HD11 . LEU   B 1 109 ? 36.634 -26.406 1.522   1.00 16.93 ?  109 LEU   B HD11 1 
ATOM   5381 H HD12 . LEU   B 1 109 ? 35.999 -25.086 2.135   1.00 16.93 ?  109 LEU   B HD12 1 
ATOM   5382 H HD13 . LEU   B 1 109 ? 36.532 -26.234 3.097   1.00 16.93 ?  109 LEU   B HD13 1 
ATOM   5383 H HD21 . LEU   B 1 109 ? 35.415 -28.404 1.318   1.00 18.26 ?  109 LEU   B HD21 1 
ATOM   5384 H HD22 . LEU   B 1 109 ? 35.233 -28.578 2.886   1.00 18.26 ?  109 LEU   B HD22 1 
ATOM   5385 H HD23 . LEU   B 1 109 ? 33.961 -28.585 1.933   1.00 18.26 ?  109 LEU   B HD23 1 
ATOM   5386 N N    . LYS   B 1 110 ? 31.721 -24.065 2.892   1.00 13.71 ?  110 LYS   B N    1 
ATOM   5387 C CA   . LYS   B 1 110 ? 30.966 -23.298 1.908   1.00 13.75 ?  110 LYS   B CA   1 
ATOM   5388 C C    . LYS   B 1 110 ? 31.312 -21.811 2.000   1.00 13.34 ?  110 LYS   B C    1 
ATOM   5389 O O    . LYS   B 1 110 ? 31.571 -21.160 0.982   1.00 13.25 ?  110 LYS   B O    1 
ATOM   5390 C CB   . LYS   B 1 110 ? 29.462 -23.540 2.060   1.00 14.44 ?  110 LYS   B CB   1 
ATOM   5391 C CG   . LYS   B 1 110 ? 28.657 -22.921 0.918   1.00 14.89 ?  110 LYS   B CG   1 
ATOM   5392 C CD   . LYS   B 1 110 ? 27.190 -23.346 0.955   1.00 15.09 ?  110 LYS   B CD   1 
ATOM   5393 C CE   . LYS   B 1 110 ? 26.422 -22.816 -0.256  1.00 16.00 ?  110 LYS   B CE   1 
ATOM   5394 N NZ   . LYS   B 1 110 ? 26.760 -23.539 -1.511  1.00 16.16 ?  110 LYS   B NZ   1 
ATOM   5395 H H    . LYS   B 1 110 ? 31.249 -24.477 3.480   1.00 16.42 ?  110 LYS   B H    1 
ATOM   5396 H HA   . LYS   B 1 110 ? 31.221 -23.600 1.023   1.00 16.48 ?  110 LYS   B HA   1 
ATOM   5397 H HB2  . LYS   B 1 110 ? 29.294 -24.498 2.062   1.00 17.31 ?  110 LYS   B HB2  1 
ATOM   5398 H HB3  . LYS   B 1 110 ? 29.158 -23.149 2.892   1.00 17.31 ?  110 LYS   B HB3  1 
ATOM   5399 H HG2  . LYS   B 1 110 ? 28.689 -21.956 0.989   1.00 17.84 ?  110 LYS   B HG2  1 
ATOM   5400 H HG3  . LYS   B 1 110 ? 29.028 -23.209 0.070   1.00 17.84 ?  110 LYS   B HG3  1 
ATOM   5401 H HD2  . LYS   B 1 110 ? 27.134 -24.317 0.951   1.00 18.09 ?  110 LYS   B HD2  1 
ATOM   5402 H HD3  . LYS   B 1 110 ? 26.772 -22.993 1.758   1.00 18.09 ?  110 LYS   B HD3  1 
ATOM   5403 H HE2  . LYS   B 1 110 ? 25.472 -22.918 -0.101  1.00 19.18 ?  110 LYS   B HE2  1 
ATOM   5404 H HE3  . LYS   B 1 110 ? 26.642 -21.880 -0.383  1.00 19.18 ?  110 LYS   B HE3  1 
ATOM   5405 H HZ1  . LYS   B 1 110 ? 26.301 -23.205 -2.191  1.00 19.36 ?  110 LYS   B HZ1  1 
ATOM   5406 H HZ2  . LYS   B 1 110 ? 27.633 -23.460 -1.682  1.00 19.36 ?  110 LYS   B HZ2  1 
ATOM   5407 H HZ3  . LYS   B 1 110 ? 26.566 -24.406 -1.425  1.00 19.36 ?  110 LYS   B HZ3  1 
ATOM   5408 N N    . SER   B 1 111 ? 31.330 -21.258 3.221   1.00 13.75 ?  111 SER   B N    1 
ATOM   5409 C CA   . SER   B 1 111 ? 31.725 -19.860 3.396   1.00 13.60 ?  111 SER   B CA   1 
ATOM   5410 C C    . SER   B 1 111 ? 33.103 -19.602 2.797   1.00 12.67 ?  111 SER   B C    1 
ATOM   5411 O O    . SER   B 1 111 ? 33.328 -18.569 2.150   1.00 13.26 ?  111 SER   B O    1 
ATOM   5412 C CB   . SER   B 1 111 ? 31.728 -19.503 4.881   1.00 14.65 ?  111 SER   B CB   1 
ATOM   5413 O OG   . SER   B 1 111 ? 30.420 -19.479 5.412   1.00 16.08 ?  111 SER   B OG   1 
ATOM   5414 H H    . SER   B 1 111 ? 31.129 -21.672 3.950   1.00 16.47 ?  111 SER   B H    1 
ATOM   5415 H HA   . SER   B 1 111 ? 31.087 -19.293 2.946   1.00 16.30 ?  111 SER   B HA   1 
ATOM   5416 H HB2  . SER   B 1 111 ? 32.245 -20.168 5.366   1.00 17.55 ?  111 SER   B HB2  1 
ATOM   5417 H HB3  . SER   B 1 111 ? 32.125 -18.629 4.994   1.00 17.55 ?  111 SER   B HB3  1 
ATOM   5418 H HG   . SER   B 1 111 ? 30.442 -19.280 6.234   1.00 19.28 ?  111 SER   B HG   1 
ATOM   5419 N N    . ALA   B 1 112 ? 34.040 -20.527 3.006   1.00 13.12 ?  112 ALA   B N    1 
ATOM   5420 C CA   . ALA   B 1 112 ? 35.385 -20.350 2.467   1.00 12.66 ?  112 ALA   B CA   1 
ATOM   5421 C C    . ALA   B 1 112 ? 35.356 -20.259 0.944   1.00 12.35 ?  112 ALA   B C    1 
ATOM   5422 O O    . ALA   B 1 112 ? 35.981 -19.369 0.352   1.00 12.44 ?  112 ALA   B O    1 
ATOM   5423 C CB   . ALA   B 1 112 ? 36.295 -21.483 2.949   1.00 13.36 ?  112 ALA   B CB   1 
ATOM   5424 H H    . ALA   B 1 112 ? 33.927 -21.256 3.453   1.00 15.73 ?  112 ALA   B H    1 
ATOM   5425 H HA   . ALA   B 1 112 ? 35.744 -19.514 2.805   1.00 15.17 ?  112 ALA   B HA   1 
ATOM   5426 H HB1  . ALA   B 1 112 ? 37.186 -21.342 2.589   1.00 16.01 ?  112 ALA   B HB1  1 
ATOM   5427 H HB2  . ALA   B 1 112 ? 36.329 -21.466 3.920   1.00 16.01 ?  112 ALA   B HB2  1 
ATOM   5428 H HB3  . ALA   B 1 112 ? 35.941 -22.327 2.642   1.00 16.01 ?  112 ALA   B HB3  1 
ATOM   5429 N N    . TYR   B 1 113 ? 34.619 -21.161 0.289   1.00 12.25 ?  113 TYR   B N    1 
ATOM   5430 C CA   . TYR   B 1 113 ? 34.544 -21.115 -1.165  1.00 11.83 ?  113 TYR   B CA   1 
ATOM   5431 C C    . TYR   B 1 113 ? 33.835 -19.864 -1.678  1.00 11.61 ?  113 TYR   B C    1 
ATOM   5432 O O    . TYR   B 1 113 ? 34.103 -19.430 -2.803  1.00 11.66 ?  113 TYR   B O    1 
ATOM   5433 C CB   . TYR   B 1 113 ? 33.872 -22.375 -1.714  1.00 11.97 ?  113 TYR   B CB   1 
ATOM   5434 C CG   . TYR   B 1 113 ? 34.830 -23.522 -1.968  1.00 12.59 ?  113 TYR   B CG   1 
ATOM   5435 C CD1  . TYR   B 1 113 ? 35.832 -23.419 -2.930  1.00 12.99 ?  113 TYR   B CD1  1 
ATOM   5436 C CD2  . TYR   B 1 113 ? 34.729 -24.705 -1.261  1.00 12.68 ?  113 TYR   B CD2  1 
ATOM   5437 C CE1  . TYR   B 1 113 ? 36.711 -24.454 -3.169  1.00 12.98 ?  113 TYR   B CE1  1 
ATOM   5438 C CE2  . TYR   B 1 113 ? 35.599 -25.757 -1.501  1.00 13.07 ?  113 TYR   B CE2  1 
ATOM   5439 C CZ   . TYR   B 1 113 ? 36.580 -25.630 -2.463  1.00 12.99 ?  113 TYR   B CZ   1 
ATOM   5440 O OH   . TYR   B 1 113 ? 37.463 -26.647 -2.728  1.00 13.77 ?  113 TYR   B OH   1 
ATOM   5441 H H    . TYR   B 1 113 ? 34.155 -21.786 0.662   1.00 14.68 ?  113 TYR   B H    1 
ATOM   5442 H HA   . TYR   B 1 113 ? 35.445 -21.096 -1.507  1.00 14.17 ?  113 TYR   B HA   1 
ATOM   5443 H HB2  . TYR   B 1 113 ? 33.209 -22.684 -1.075  1.00 14.35 ?  113 TYR   B HB2  1 
ATOM   5444 H HB3  . TYR   B 1 113 ? 33.438 -22.157 -2.554  1.00 14.35 ?  113 TYR   B HB3  1 
ATOM   5445 H HD1  . TYR   B 1 113 ? 35.918 -22.628 -3.416  1.00 15.57 ?  113 TYR   B HD1  1 
ATOM   5446 H HD2  . TYR   B 1 113 ? 34.060 -24.800 -0.626  1.00 15.19 ?  113 TYR   B HD2  1 
ATOM   5447 H HE1  . TYR   B 1 113 ? 37.370 -24.368 -3.823  1.00 15.56 ?  113 TYR   B HE1  1 
ATOM   5448 H HE2  . TYR   B 1 113 ? 35.512 -26.551 -1.027  1.00 15.66 ?  113 TYR   B HE2  1 
ATOM   5449 H HH   . TYR   B 1 113 ? 37.279 -27.314 -2.248  1.00 16.50 ?  113 TYR   B HH   1 
ATOM   5450 N N    . GLU   B 1 114 ? 32.913 -19.284 -0.898  1.00 11.93 ?  114 GLU   B N    1 
ATOM   5451 C CA   . GLU   B 1 114 ? 32.222 -18.075 -1.351  1.00 11.79 ?  114 GLU   B CA   1 
ATOM   5452 C C    . GLU   B 1 114 ? 33.208 -16.951 -1.650  1.00 11.78 ?  114 GLU   B C    1 
ATOM   5453 O O    . GLU   B 1 114 ? 32.935 -16.090 -2.492  1.00 11.96 ?  114 GLU   B O    1 
ATOM   5454 C CB   . GLU   B 1 114 ? 31.163 -17.640 -0.330  1.00 12.06 ?  114 GLU   B CB   1 
ATOM   5455 C CG   . GLU   B 1 114 ? 29.961 -18.571 -0.384  1.00 12.53 ?  114 GLU   B CG   1 
ATOM   5456 C CD   . GLU   B 1 114 ? 28.929 -18.369 0.711   1.00 12.75 ?  114 GLU   B CD   1 
ATOM   5457 O OE1  . GLU   B 1 114 ? 29.221 -17.754 1.758   1.00 12.87 ?  114 GLU   B OE1  1 
ATOM   5458 O OE2  . GLU   B 1 114 ? 27.802 -18.901 0.534   1.00 13.91 -1 114 GLU   B OE2  1 
ATOM   5459 H H    . GLU   B 1 114 ? 32.665 -19.578 -0.127  1.00 14.29 ?  114 GLU   B H    1 
ATOM   5460 H HA   . GLU   B 1 114 ? 31.762 -18.277 -2.173  1.00 14.13 ?  114 GLU   B HA   1 
ATOM   5461 H HB2  . GLU   B 1 114 ? 31.540 -17.675 0.566   1.00 14.45 ?  114 GLU   B HB2  1 
ATOM   5462 H HB3  . GLU   B 1 114 ? 30.865 -16.743 -0.535  1.00 14.45 ?  114 GLU   B HB3  1 
ATOM   5463 H HG2  . GLU   B 1 114 ? 29.513 -18.444 -1.228  1.00 15.01 ?  114 GLU   B HG2  1 
ATOM   5464 H HG3  . GLU   B 1 114 ? 30.281 -19.487 -0.317  1.00 15.01 ?  114 GLU   B HG3  1 
ATOM   5465 N N    . ASN   B 1 115 ? 34.376 -16.947 -1.000  1.00 11.47 ?  115 ASN   B N    1 
ATOM   5466 C CA   . ASN   B 1 115 ? 35.372 -15.916 -1.298  1.00 11.44 ?  115 ASN   B CA   1 
ATOM   5467 C C    . ASN   B 1 115 ? 35.781 -15.936 -2.768  1.00 11.18 ?  115 ASN   B C    1 
ATOM   5468 O O    . ASN   B 1 115 ? 36.171 -14.896 -3.322  1.00 12.04 ?  115 ASN   B O    1 
ATOM   5469 C CB   . ASN   B 1 115 ? 36.616 -16.090 -0.415  1.00 12.23 ?  115 ASN   B CB   1 
ATOM   5470 C CG   . ASN   B 1 115 ? 36.351 -15.822 1.050   1.00 12.50 ?  115 ASN   B CG   1 
ATOM   5471 O OD1  . ASN   B 1 115 ? 36.354 -14.676 1.498   1.00 14.53 ?  115 ASN   B OD1  1 
ATOM   5472 N ND2  . ASN   B 1 115 ? 36.171 -16.891 1.823   1.00 12.67 ?  115 ASN   B ND2  1 
ATOM   5473 H H    . ASN   B 1 115 ? 34.612 -17.506 -0.383  1.00 13.74 ?  115 ASN   B H    1 
ATOM   5474 H HA   . ASN   B 1 115 ? 34.995 -15.044 -1.106  1.00 13.71 ?  115 ASN   B HA   1 
ATOM   5475 H HB2  . ASN   B 1 115 ? 36.940 -17.000 -0.503  1.00 14.66 ?  115 ASN   B HB2  1 
ATOM   5476 H HB3  . ASN   B 1 115 ? 37.301 -15.468 -0.709  1.00 14.66 ?  115 ASN   B HB3  1 
ATOM   5477 H HD21 . ASN   B 1 115 ? 36.029 -16.794 2.667   1.00 15.18 ?  115 ASN   B HD21 1 
ATOM   5478 H HD22 . ASN   B 1 115 ? 36.185 -17.681 1.480   1.00 15.18 ?  115 ASN   B HD22 1 
ATOM   5479 N N    . PHE   B 1 116 ? 35.757 -17.115 -3.404  1.00 10.86 ?  116 PHE   B N    1 
ATOM   5480 C CA   . PHE   B 1 116 ? 36.185 -17.211 -4.795  1.00 11.12 ?  116 PHE   B CA   1 
ATOM   5481 C C    . PHE   B 1 116 ? 35.282 -16.389 -5.710  1.00 11.00 ?  116 PHE   B C    1 
ATOM   5482 O O    . PHE   B 1 116 ? 35.714 -15.957 -6.784  1.00 11.73 ?  116 PHE   B O    1 
ATOM   5483 C CB   . PHE   B 1 116 ? 36.148 -18.661 -5.311  1.00 11.06 ?  116 PHE   B CB   1 
ATOM   5484 C CG   . PHE   B 1 116 ? 37.222 -19.614 -4.765  1.00 11.06 ?  116 PHE   B CG   1 
ATOM   5485 C CD1  . PHE   B 1 116 ? 37.873 -19.430 -3.557  1.00 11.61 ?  116 PHE   B CD1  1 
ATOM   5486 C CD2  . PHE   B 1 116 ? 37.519 -20.752 -5.501  1.00 11.36 ?  116 PHE   B CD2  1 
ATOM   5487 C CE1  . PHE   B 1 116 ? 38.806 -20.372 -3.111  1.00 12.09 ?  116 PHE   B CE1  1 
ATOM   5488 C CE2  . PHE   B 1 116 ? 38.447 -21.689 -5.065  1.00 11.43 ?  116 PHE   B CE2  1 
ATOM   5489 C CZ   . PHE   B 1 116 ? 39.084 -21.503 -3.874  1.00 11.41 ?  116 PHE   B CZ   1 
ATOM   5490 H H    . PHE   B 1 116 ? 35.494 -17.862 -3.056  1.00 13.00 ?  116 PHE   B H    1 
ATOM   5491 H HA   . PHE   B 1 116 ? 37.092 -16.886 -4.877  1.00 13.33 ?  116 PHE   B HA   1 
ATOM   5492 H HB2  . PHE   B 1 116 ? 35.278 -19.041 -5.085  1.00 13.25 ?  116 PHE   B HB2  1 
ATOM   5493 H HB3  . PHE   B 1 116 ? 36.239 -18.643 -6.277  1.00 13.25 ?  116 PHE   B HB3  1 
ATOM   5494 H HD1  . PHE   B 1 116 ? 37.679 -18.683 -3.037  1.00 13.91 ?  116 PHE   B HD1  1 
ATOM   5495 H HD2  . PHE   B 1 116 ? 37.076 -20.898 -6.309  1.00 13.60 ?  116 PHE   B HD2  1 
ATOM   5496 H HE1  . PHE   B 1 116 ? 39.248 -20.239 -2.304  1.00 14.48 ?  116 PHE   B HE1  1 
ATOM   5497 H HE2  . PHE   B 1 116 ? 38.629 -22.436 -5.582  1.00 13.69 ?  116 PHE   B HE2  1 
ATOM   5498 H HZ   . PHE   B 1 116 ? 39.719 -22.115 -3.582  1.00 13.67 ?  116 PHE   B HZ   1 
ATOM   5499 N N    . ASN   B 1 117 ? 34.014 -16.189 -5.323  1.00 11.64 ?  117 ASN   B N    1 
ATOM   5500 C CA   . ASN   B 1 117 ? 33.064 -15.482 -6.182  1.00 12.05 ?  117 ASN   B CA   1 
ATOM   5501 C C    . ASN   B 1 117 ? 33.378 -14.002 -6.330  1.00 12.17 ?  117 ASN   B C    1 
ATOM   5502 O O    . ASN   B 1 117 ? 32.776 -13.344 -7.182  1.00 13.14 ?  117 ASN   B O    1 
ATOM   5503 C CB   . ASN   B 1 117 ? 31.644 -15.705 -5.682  1.00 12.30 ?  117 ASN   B CB   1 
ATOM   5504 C CG   . ASN   B 1 117 ? 31.188 -17.113 -5.940  1.00 12.45 ?  117 ASN   B CG   1 
ATOM   5505 O OD1  . ASN   B 1 117 ? 31.546 -17.705 -6.962  1.00 13.38 ?  117 ASN   B OD1  1 
ATOM   5506 N ND2  . ASN   B 1 117 ? 30.450 -17.686 -5.003  1.00 12.53 ?  117 ASN   B ND2  1 
ATOM   5507 H H    . ASN   B 1 117 ? 33.693 -16.445 -4.567  1.00 13.94 ?  117 ASN   B H    1 
ATOM   5508 H HA   . ASN   B 1 117 ? 33.118 -15.874 -7.061  1.00 14.44 ?  117 ASN   B HA   1 
ATOM   5509 H HB2  . ASN   B 1 117 ? 31.610 -15.545 -4.721  1.00 14.74 ?  117 ASN   B HB2  1 
ATOM   5510 H HB3  . ASN   B 1 117 ? 31.045 -15.094 -6.139  1.00 14.74 ?  117 ASN   B HB3  1 
ATOM   5511 H HD21 . ASN   B 1 117 ? 30.166 -18.490 -5.111  1.00 15.01 ?  117 ASN   B HD21 1 
ATOM   5512 H HD22 . ASN   B 1 117 ? 30.229 -17.243 -4.298  1.00 15.01 ?  117 ASN   B HD22 1 
ATOM   5513 N N    . GLN   B 1 118 ? 34.316 -13.473 -5.554  1.00 11.75 ?  118 GLN   B N    1 
ATOM   5514 C CA   . GLN   B 1 118 ? 34.746 -12.087 -5.692  1.00 12.30 ?  118 GLN   B CA   1 
ATOM   5515 C C    . GLN   B 1 118 ? 35.812 -11.898 -6.768  1.00 12.50 ?  118 GLN   B C    1 
ATOM   5516 O O    . GLN   B 1 118 ? 36.289 -10.772 -6.953  1.00 13.80 ?  118 GLN   B O    1 
ATOM   5517 C CB   . GLN   B 1 118 ? 35.223 -11.563 -4.334  1.00 12.80 ?  118 GLN   B CB   1 
ATOM   5518 C CG   . GLN   B 1 118 ? 34.136 -11.593 -3.266  1.00 13.22 ?  118 GLN   B CG   1 
ATOM   5519 C CD   . GLN   B 1 118 ? 32.969 -10.684 -3.601  1.00 13.02 ?  118 GLN   B CD   1 
ATOM   5520 O OE1  . GLN   B 1 118 ? 33.157 -9.542  -4.039  1.00 13.86 ?  118 GLN   B OE1  1 
ATOM   5521 N NE2  . GLN   B 1 118 ? 31.757 -11.180 -3.402  1.00 13.47 ?  118 GLN   B NE2  1 
ATOM   5522 H H    . GLN   B 1 118 ? 34.740 -13.903 -4.937  1.00 14.08 ?  118 GLN   B H    1 
ATOM   5523 H HA   . GLN   B 1 118 ? 33.980 -11.557 -5.958  1.00 14.74 ?  118 GLN   B HA   1 
ATOM   5524 H HB2  . GLN   B 1 118 ? 35.961 -12.101 -4.024  1.00 15.33 ?  118 GLN   B HB2  1 
ATOM   5525 H HB3  . GLN   B 1 118 ? 35.507 -10.636 -4.436  1.00 15.33 ?  118 GLN   B HB3  1 
ATOM   5526 H HG2  . GLN   B 1 118 ? 33.799 -12.499 -3.183  1.00 15.84 ?  118 GLN   B HG2  1 
ATOM   5527 H HG3  . GLN   B 1 118 ? 34.512 -11.300 -2.420  1.00 15.84 ?  118 GLN   B HG3  1 
ATOM   5528 H HE21 . GLN   B 1 118 ? 31.664 -11.981 -3.094  1.00 16.14 ?  118 GLN   B HE21 1 
ATOM   5529 H HE22 . GLN   B 1 118 ? 31.066 -10.706 -3.578  1.00 16.14 ?  118 GLN   B HE22 1 
ATOM   5530 N N    . HIS   B 1 119 ? 36.160 -12.956 -7.505  1.00 12.04 ?  119 HIS   B N    1 
ATOM   5531 C CA   . HIS   B 1 119 ? 37.210 -12.916 -8.516  1.00 12.37 ?  119 HIS   B CA   1 
ATOM   5532 C C    . HIS   B 1 119 ? 36.733 -13.644 -9.760  1.00 12.14 ?  119 HIS   B C    1 
ATOM   5533 O O    . HIS   B 1 119 ? 36.217 -14.757 -9.663  1.00 13.01 ?  119 HIS   B O    1 
ATOM   5534 C CB   . HIS   B 1 119 ? 38.484 -13.555 -7.958  1.00 12.70 ?  119 HIS   B CB   1 
ATOM   5535 C CG   . HIS   B 1 119 ? 38.966 -12.856 -6.731  1.00 13.94 ?  119 HIS   B CG   1 
ATOM   5536 N ND1  . HIS   B 1 119 ? 39.761 -11.731 -6.782  1.00 15.70 ?  119 HIS   B ND1  1 
ATOM   5537 C CD2  . HIS   B 1 119 ? 38.677 -13.059 -5.425  1.00 14.99 ?  119 HIS   B CD2  1 
ATOM   5538 C CE1  . HIS   B 1 119 ? 39.974 -11.298 -5.553  1.00 16.51 ?  119 HIS   B CE1  1 
ATOM   5539 N NE2  . HIS   B 1 119 ? 39.321 -12.080 -4.713  1.00 16.64 ?  119 HIS   B NE2  1 
ATOM   5540 H H    . HIS   B 1 119 ? 35.784 -13.729 -7.440  1.00 14.42 ?  119 HIS   B H    1 
ATOM   5541 H HA   . HIS   B 1 119 ? 37.400 -11.989 -8.748  1.00 14.82 ?  119 HIS   B HA   1 
ATOM   5542 H HB2  . HIS   B 1 119 ? 38.302 -14.479 -7.734  1.00 15.22 ?  119 HIS   B HB2  1 
ATOM   5543 H HB3  . HIS   B 1 119 ? 39.183 -13.504 -8.630  1.00 15.22 ?  119 HIS   B HB3  1 
ATOM   5544 H HD2  . HIS   B 1 119 ? 38.150 -13.744 -5.075  1.00 17.96 ?  119 HIS   B HD2  1 
ATOM   5545 H HE1  . HIS   B 1 119 ? 40.502 -10.572 -5.315  1.00 19.79 ?  119 HIS   B HE1  1 
ATOM   5546 H HE2  . HIS   B 1 119 ? 39.328 -12.010 -3.853  1.00 19.94 ?  119 HIS   B HE2  1 
ATOM   5547 N N    . GLU   B 1 120 ? 36.888 -13.023 -10.929 1.00 12.84 ?  120 GLU   B N    1 
ATOM   5548 C CA   . GLU   B 1 120 ? 36.292 -13.601 -12.130 1.00 14.56 ?  120 GLU   B CA   1 
ATOM   5549 C C    . GLU   B 1 120 ? 36.967 -14.904 -12.547 1.00 13.42 ?  120 GLU   B C    1 
ATOM   5550 O O    . GLU   B 1 120 ? 36.305 -15.781 -13.119 1.00 13.46 ?  120 GLU   B O    1 
ATOM   5551 C CB   . GLU   B 1 120 ? 36.305 -12.585 -13.271 1.00 18.94 ?  120 GLU   B CB   1 
ATOM   5552 C CG   . GLU   B 1 120 ? 35.337 -11.437 -13.049 1.00 24.98 ?  120 GLU   B CG   1 
ATOM   5553 C CD   . GLU   B 1 120 ? 35.155 -10.565 -14.273 1.00 30.90 ?  120 GLU   B CD   1 
ATOM   5554 O OE1  . GLU   B 1 120 ? 36.144 -10.353 -15.006 1.00 33.11 ?  120 GLU   B OE1  1 
ATOM   5555 O OE2  . GLU   B 1 120 ? 34.020 -10.092 -14.498 1.00 33.71 -1 120 GLU   B OE2  1 
ATOM   5556 H H    . GLU   B 1 120 ? 37.312 -12.280 -11.051 1.00 15.38 ?  120 GLU   B H    1 
ATOM   5557 H HA   . GLU   B 1 120 ? 35.367 -13.807 -11.938 1.00 17.44 ?  120 GLU   B HA   1 
ATOM   5558 H HB2  . GLU   B 1 120 ? 37.193 -12.213 -13.358 1.00 22.71 ?  120 GLU   B HB2  1 
ATOM   5559 H HB3  . GLU   B 1 120 ? 36.049 -13.034 -14.094 1.00 22.71 ?  120 GLU   B HB3  1 
ATOM   5560 H HG2  . GLU   B 1 120 ? 34.465 -11.795 -12.814 1.00 29.95 ?  120 GLU   B HG2  1 
ATOM   5561 H HG3  . GLU   B 1 120 ? 35.668 -10.875 -12.334 1.00 29.95 ?  120 GLU   B HG3  1 
ATOM   5562 N N    . VAL   B 1 121 ? 38.265 -15.049 -12.278 1.00 12.75 ?  121 VAL   B N    1 
ATOM   5563 C CA   . VAL   B 1 121 ? 39.008 -16.259 -12.625 1.00 12.32 ?  121 VAL   B CA   1 
ATOM   5564 C C    . VAL   B 1 121 ? 40.122 -16.464 -11.607 1.00 12.19 ?  121 VAL   B C    1 
ATOM   5565 O O    . VAL   B 1 121 ? 40.806 -15.510 -11.216 1.00 12.78 ?  121 VAL   B O    1 
ATOM   5566 C CB   . VAL   B 1 121 ? 39.517 -16.210 -14.084 1.00 14.49 ?  121 VAL   B CB   1 
ATOM   5567 C CG1  . VAL   B 1 121 ? 40.383 -14.979 -14.328 1.00 16.12 ?  121 VAL   B CG1  1 
ATOM   5568 C CG2  . VAL   B 1 121 ? 40.257 -17.489 -14.448 1.00 15.90 ?  121 VAL   B CG2  1 
ATOM   5569 H H    . VAL   B 1 121 ? 38.747 -14.448 -11.893 1.00 15.28 ?  121 VAL   B H    1 
ATOM   5570 H HA   . VAL   B 1 121 ? 38.401 -17.011 -12.558 1.00 14.77 ?  121 VAL   B HA   1 
ATOM   5571 H HB   . VAL   B 1 121 ? 38.746 -16.142 -14.675 1.00 17.36 ?  121 VAL   B HB   1 
ATOM   5572 H HG11 . VAL   B 1 121 ? 40.692 -14.986 -15.247 1.00 19.32 ?  121 VAL   B HG11 1 
ATOM   5573 H HG12 . VAL   B 1 121 ? 39.853 -14.180 -14.166 1.00 19.32 ?  121 VAL   B HG12 1 
ATOM   5574 H HG13 . VAL   B 1 121 ? 41.140 -15.001 -13.724 1.00 19.32 ?  121 VAL   B HG13 1 
ATOM   5575 H HG21 . VAL   B 1 121 ? 40.460 -17.476 -15.398 1.00 19.05 ?  121 VAL   B HG21 1 
ATOM   5576 H HG22 . VAL   B 1 121 ? 41.080 -17.534 -13.937 1.00 19.05 ?  121 VAL   B HG22 1 
ATOM   5577 H HG23 . VAL   B 1 121 ? 39.695 -18.250 -14.242 1.00 19.05 ?  121 VAL   B HG23 1 
ATOM   5578 N N    . LEU   B 1 122 ? 40.302 -17.717 -11.176 1.00 11.76 ?  122 LEU   B N    1 
ATOM   5579 C CA   . LEU   B 1 122 ? 41.282 -18.074 -10.156 1.00 11.14 ?  122 LEU   B CA   1 
ATOM   5580 C C    . LEU   B 1 122 ? 41.945 -19.402 -10.486 1.00 11.25 ?  122 LEU   B C    1 
ATOM   5581 O O    . LEU   B 1 122 ? 41.285 -20.326 -10.983 1.00 12.66 ?  122 LEU   B O    1 
ATOM   5582 C CB   . LEU   B 1 122 ? 40.625 -18.304 -8.779  1.00 13.27 ?  122 LEU   B CB   1 
ATOM   5583 C CG   . LEU   B 1 122 ? 39.597 -17.280 -8.288  1.00 13.06 ?  122 LEU   B CG   1 
ATOM   5584 C CD1  . LEU   B 1 122 ? 38.196 -17.623 -8.767  1.00 13.75 ?  122 LEU   B CD1  1 
ATOM   5585 C CD2  . LEU   B 1 122 ? 39.640 -17.173 -6.776  1.00 12.69 ?  122 LEU   B CD2  1 
ATOM   5586 H H    . LEU   B 1 122 ? 39.854 -18.394 -11.463 1.00 14.08 ?  122 LEU   B H    1 
ATOM   5587 H HA   . LEU   B 1 122 ? 41.956 -17.380 -10.070 1.00 13.34 ?  122 LEU   B HA   1 
ATOM   5588 H HB2  . LEU   B 1 122 ? 40.175 -19.161 -8.803  1.00 15.90 ?  122 LEU   B HB2  1 
ATOM   5589 H HB3  . LEU   B 1 122 ? 41.328 -18.333 -8.112  1.00 15.90 ?  122 LEU   B HB3  1 
ATOM   5590 H HG   . LEU   B 1 122 ? 39.825 -16.409 -8.648  1.00 15.65 ?  122 LEU   B HG   1 
ATOM   5591 H HD11 . LEU   B 1 122 ? 37.569 -16.979 -8.398  1.00 16.47 ?  122 LEU   B HD11 1 
ATOM   5592 H HD12 . LEU   B 1 122 ? 38.173 -17.582 -9.737  1.00 16.47 ?  122 LEU   B HD12 1 
ATOM   5593 H HD13 . LEU   B 1 122 ? 37.966 -18.515 -8.467  1.00 16.47 ?  122 LEU   B HD13 1 
ATOM   5594 H HD21 . LEU   B 1 122 ? 38.961 -16.545 -6.479  1.00 15.20 ?  122 LEU   B HD21 1 
ATOM   5595 H HD22 . LEU   B 1 122 ? 39.469 -18.048 -6.389  1.00 15.20 ?  122 LEU   B HD22 1 
ATOM   5596 H HD23 . LEU   B 1 122 ? 40.518 -16.860 -6.504  1.00 15.20 ?  122 LEU   B HD23 1 
ATOM   5597 N N    . LEU   B 1 123 ? 43.231 -19.509 -10.130 1.00 11.01 ?  123 LEU   B N    1 
ATOM   5598 C CA   . LEU   B 1 123 ? 43.943 -20.782 -10.009 1.00 11.18 ?  123 LEU   B CA   1 
ATOM   5599 C C    . LEU   B 1 123 ? 43.914 -21.183 -8.538  1.00 10.95 ?  123 LEU   B C    1 
ATOM   5600 O O    . LEU   B 1 123 ? 44.260 -20.354 -7.682  1.00 11.31 ?  123 LEU   B O    1 
ATOM   5601 C CB   . LEU   B 1 123 ? 45.393 -20.604 -10.469 1.00 11.58 ?  123 LEU   B CB   1 
ATOM   5602 C CG   . LEU   B 1 123 ? 46.335 -21.791 -10.229 1.00 11.84 ?  123 LEU   B CG   1 
ATOM   5603 C CD1  . LEU   B 1 123 ? 45.899 -23.035 -10.993 1.00 12.41 ?  123 LEU   B CD1  1 
ATOM   5604 C CD2  . LEU   B 1 123 ? 47.753 -21.405 -10.605 1.00 12.83 ?  123 LEU   B CD2  1 
ATOM   5605 H H    . LEU   B 1 123 ? 43.725 -18.830 -9.934  1.00 13.18 ?  123 LEU   B H    1 
ATOM   5606 H HA   . LEU   B 1 123 ? 43.504 -21.466 -10.542 1.00 13.39 ?  123 LEU   B HA   1 
ATOM   5607 H HB2  . LEU   B 1 123 ? 45.384 -20.431 -11.424 1.00 13.87 ?  123 LEU   B HB2  1 
ATOM   5608 H HB3  . LEU   B 1 123 ? 45.764 -19.840 -10.006 1.00 13.87 ?  123 LEU   B HB3  1 
ATOM   5609 H HG   . LEU   B 1 123 ? 46.332 -22.009 -9.284  1.00 14.18 ?  123 LEU   B HG   1 
ATOM   5610 H HD11 . LEU   B 1 123 ? 46.534 -23.746 -10.822 1.00 14.86 ?  123 LEU   B HD11 1 
ATOM   5611 H HD12 . LEU   B 1 123 ? 45.016 -23.299 -10.683 1.00 14.86 ?  123 LEU   B HD12 1 
ATOM   5612 H HD13 . LEU   B 1 123 ? 45.870 -22.830 -11.938 1.00 14.86 ?  123 LEU   B HD13 1 
ATOM   5613 H HD21 . LEU   B 1 123 ? 48.336 -22.164 -10.448 1.00 15.37 ?  123 LEU   B HD21 1 
ATOM   5614 H HD22 . LEU   B 1 123 ? 47.774 -21.159 -11.543 1.00 15.37 ?  123 LEU   B HD22 1 
ATOM   5615 H HD23 . LEU   B 1 123 ? 48.030 -20.655 -10.058 1.00 15.37 ?  123 LEU   B HD23 1 
ATOM   5616 N N    . ALA   B 1 124 ? 43.476 -22.413 -8.228  1.00 10.81 ?  124 ALA   B N    1 
ATOM   5617 C CA   . ALA   B 1 124 ? 43.227 -22.726 -6.828  1.00 10.88 ?  124 ALA   B CA   1 
ATOM   5618 C C    . ALA   B 1 124 ? 43.501 -24.183 -6.503  1.00 10.67 ?  124 ALA   B C    1 
ATOM   5619 O O    . ALA   B 1 124 ? 43.358 -25.060 -7.366  1.00 11.28 ?  124 ALA   B O    1 
ATOM   5620 C CB   . ALA   B 1 124 ? 41.776 -22.421 -6.451  1.00 11.34 ?  124 ALA   B CB   1 
ATOM   5621 H H    . ALA   B 1 124 ? 43.298 -23.047 -8.791  1.00 12.95 ?  124 ALA   B H    1 
ATOM   5622 H HA   . ALA   B 1 124 ? 43.807 -22.175 -6.289  1.00 13.04 ?  124 ALA   B HA   1 
ATOM   5623 H HB1  . ALA   B 1 124 ? 41.634 -22.638 -5.519  1.00 13.58 ?  124 ALA   B HB1  1 
ATOM   5624 H HB2  . ALA   B 1 124 ? 41.605 -21.475 -6.602  1.00 13.58 ?  124 ALA   B HB2  1 
ATOM   5625 H HB3  . ALA   B 1 124 ? 41.183 -22.951 -7.010  1.00 13.58 ?  124 ALA   B HB3  1 
ATOM   5626 N N    . PRO   B 1 125 ? 43.796 -24.478 -5.238  1.00 10.91 ?  125 PRO   B N    1 
ATOM   5627 C CA   . PRO   B 1 125 ? 43.733 -25.843 -4.713  1.00 11.74 ?  125 PRO   B CA   1 
ATOM   5628 C C    . PRO   B 1 125 ? 42.330 -26.118 -4.168  1.00 11.74 ?  125 PRO   B C    1 
ATOM   5629 O O    . PRO   B 1 125 ? 41.530 -25.205 -3.967  1.00 12.14 ?  125 PRO   B O    1 
ATOM   5630 C CB   . PRO   B 1 125 ? 44.723 -25.765 -3.544  1.00 12.80 ?  125 PRO   B CB   1 
ATOM   5631 C CG   . PRO   B 1 125 ? 44.478 -24.380 -2.973  1.00 12.80 ?  125 PRO   B CG   1 
ATOM   5632 C CD   . PRO   B 1 125 ? 44.120 -23.505 -4.175  1.00 11.48 ?  125 PRO   B CD   1 
ATOM   5633 H HA   . PRO   B 1 125 ? 44.007 -26.512 -5.361  1.00 14.07 ?  125 PRO   B HA   1 
ATOM   5634 H HB2  . PRO   B 1 125 ? 44.519 -26.452 -2.883  1.00 15.34 ?  125 PRO   B HB2  1 
ATOM   5635 H HB3  . PRO   B 1 125 ? 45.633 -25.855 -3.864  1.00 15.34 ?  125 PRO   B HB3  1 
ATOM   5636 H HG2  . PRO   B 1 125 ? 43.741 -24.404 -2.341  1.00 15.34 ?  125 PRO   B HG2  1 
ATOM   5637 H HG3  . PRO   B 1 125 ? 45.285 -24.053 -2.536  1.00 15.34 ?  125 PRO   B HG3  1 
ATOM   5638 H HD2  . PRO   B 1 125 ? 43.355 -22.948 -3.980  1.00 13.75 ?  125 PRO   B HD2  1 
ATOM   5639 H HD3  . PRO   B 1 125 ? 44.891 -22.964 -4.437  1.00 13.75 ?  125 PRO   B HD3  1 
ATOM   5640 N N    . LEU   B 1 126 ? 42.060 -27.394 -3.883  1.00 12.33 ?  126 LEU   B N    1 
ATOM   5641 C CA   . LEU   B 1 126 ? 40.841 -27.764 -3.168  1.00 12.90 ?  126 LEU   B CA   1 
ATOM   5642 C C    . LEU   B 1 126 ? 40.962 -27.362 -1.705  1.00 13.05 ?  126 LEU   B C    1 
ATOM   5643 O O    . LEU   B 1 126 ? 41.858 -27.820 -0.990  1.00 14.90 ?  126 LEU   B O    1 
ATOM   5644 C CB   . LEU   B 1 126 ? 40.577 -29.259 -3.287  1.00 14.28 ?  126 LEU   B CB   1 
ATOM   5645 C CG   . LEU   B 1 126 ? 40.052 -29.750 -4.639  1.00 15.04 ?  126 LEU   B CG   1 
ATOM   5646 C CD1  . LEU   B 1 126 ? 40.101 -31.260 -4.703  1.00 17.02 ?  126 LEU   B CD1  1 
ATOM   5647 C CD2  . LEU   B 1 126 ? 38.639 -29.253 -4.901  1.00 15.26 ?  126 LEU   B CD2  1 
ATOM   5648 H H    . LEU   B 1 126 ? 42.571 -28.060 -4.080  1.00 14.78 ?  126 LEU   B H    1 
ATOM   5649 H HA   . LEU   B 1 126 ? 40.094 -27.280 -3.554  1.00 15.46 ?  126 LEU   B HA   1 
ATOM   5650 H HB2  . LEU   B 1 126 ? 41.404 -29.724 -3.112  1.00 17.11 ?  126 LEU   B HB2  1 
ATOM   5651 H HB3  . LEU   B 1 126 ? 39.917 -29.498 -2.620  1.00 17.11 ?  126 LEU   B HB3  1 
ATOM   5652 H HG   . LEU   B 1 126 ? 40.624 -29.398 -5.343  1.00 18.03 ?  126 LEU   B HG   1 
ATOM   5653 H HD11 . LEU   B 1 126 ? 39.763 -31.549 -5.564  1.00 20.40 ?  126 LEU   B HD11 1 
ATOM   5654 H HD12 . LEU   B 1 126 ? 41.018 -31.550 -4.590  1.00 20.40 ?  126 LEU   B HD12 1 
ATOM   5655 H HD13 . LEU   B 1 126 ? 39.548 -31.620 -3.991  1.00 20.40 ?  126 LEU   B HD13 1 
ATOM   5656 H HD21 . LEU   B 1 126 ? 38.311 -29.652 -5.724  1.00 18.28 ?  126 LEU   B HD21 1 
ATOM   5657 H HD22 . LEU   B 1 126 ? 38.069 -29.514 -4.160  1.00 18.28 ?  126 LEU   B HD22 1 
ATOM   5658 H HD23 . LEU   B 1 126 ? 38.647 -28.286 -4.986  1.00 18.28 ?  126 LEU   B HD23 1 
ATOM   5659 N N    . LEU   B 1 127 ? 40.034 -26.530 -1.247  1.00 12.87 ?  127 LEU   B N    1 
ATOM   5660 C CA   . LEU   B 1 127 ? 40.092 -26.040 0.116   1.00 13.26 ?  127 LEU   B CA   1 
ATOM   5661 C C    . LEU   B 1 127 ? 39.817 -27.162 1.110   1.00 13.10 ?  127 LEU   B C    1 
ATOM   5662 O O    . LEU   B 1 127 ? 38.987 -28.052 0.885   1.00 13.33 ?  127 LEU   B O    1 
ATOM   5663 C CB   . LEU   B 1 127 ? 39.074 -24.915 0.326   1.00 13.84 ?  127 LEU   B CB   1 
ATOM   5664 C CG   . LEU   B 1 127 ? 39.251 -23.644 -0.503  1.00 14.17 ?  127 LEU   B CG   1 
ATOM   5665 C CD1  . LEU   B 1 127 ? 38.127 -22.676 -0.165  1.00 14.23 ?  127 LEU   B CD1  1 
ATOM   5666 C CD2  . LEU   B 1 127 ? 40.613 -23.006 -0.278  1.00 14.80 ?  127 LEU   B CD2  1 
ATOM   5667 H H    . LEU   B 1 127 ? 39.362 -26.229 -1.706  1.00 15.42 ?  127 LEU   B H    1 
ATOM   5668 H HA   . LEU   B 1 127 ? 40.976 -25.679 0.289   1.00 15.88 ?  127 LEU   B HA   1 
ATOM   5669 H HB2  . LEU   B 1 127 ? 38.189 -25.267 0.122   1.00 16.59 ?  127 LEU   B HB2  1 
ATOM   5670 H HB3  . LEU   B 1 127 ? 39.099 -24.653 1.260   1.00 16.59 ?  127 LEU   B HB3  1 
ATOM   5671 H HG   . LEU   B 1 127 ? 39.168 -23.862 -1.440  1.00 16.98 ?  127 LEU   B HG   1 
ATOM   5672 H HD11 . LEU   B 1 127 ? 38.239 -21.861 -0.687  1.00 17.05 ?  127 LEU   B HD11 1 
ATOM   5673 H HD12 . LEU   B 1 127 ? 37.273 -23.083 -0.375  1.00 17.05 ?  127 LEU   B HD12 1 
ATOM   5674 H HD13 . LEU   B 1 127 ? 38.163 -22.459 0.783   1.00 17.05 ?  127 LEU   B HD13 1 
ATOM   5675 H HD21 . LEU   B 1 127 ? 40.647 -22.153 -0.739  1.00 17.74 ?  127 LEU   B HD21 1 
ATOM   5676 H HD22 . LEU   B 1 127 ? 40.748 -22.870 0.675   1.00 17.74 ?  127 LEU   B HD22 1 
ATOM   5677 H HD23 . LEU   B 1 127 ? 41.297 -23.599 -0.625  1.00 17.74 ?  127 LEU   B HD23 1 
ATOM   5678 N N    . SER   B 1 128 ? 40.495 -27.076 2.242   1.00 13.17 ?  128 SER   B N    1 
ATOM   5679 C CA   . SER   B 1 128 ? 40.377 -27.992 3.365   1.00 13.84 ?  128 SER   B CA   1 
ATOM   5680 C C    . SER   B 1 128 ? 40.871 -29.401 3.043   1.00 14.71 ?  128 SER   B C    1 
ATOM   5681 O O    . SER   B 1 128 ? 40.772 -30.282 3.896   1.00 16.40 ?  128 SER   B O    1 
ATOM   5682 C CB   . SER   B 1 128 ? 38.970 -27.993 3.988   1.00 13.82 ?  128 SER   B CB   1 
ATOM   5683 O OG   . SER   B 1 128 ? 38.676 -26.713 4.548   1.00 14.66 ?  128 SER   B OG   1 
ATOM   5684 H H    . SER   B 1 128 ? 41.066 -26.450 2.393   1.00 15.78 ?  128 SER   B H    1 
ATOM   5685 H HA   . SER   B 1 128 ? 40.962 -27.661 4.052   1.00 16.58 ?  128 SER   B HA   1 
ATOM   5686 H HB2  . SER   B 1 128 ? 38.310 -28.207 3.308   1.00 16.56 ?  128 SER   B HB2  1 
ATOM   5687 H HB3  . SER   B 1 128 ? 38.936 -28.671 4.694   1.00 16.56 ?  128 SER   B HB3  1 
ATOM   5688 H HG   . SER   B 1 128 ? 39.243 -26.535 5.143   1.00 17.57 ?  128 SER   B HG   1 
ATOM   5689 N N    . ALA   B 1 129 ? 41.444 -29.625 1.857   1.00 15.74 ?  129 ALA   B N    1 
ATOM   5690 C CA   . ALA   B 1 129 ? 41.991 -30.926 1.505   1.00 16.66 ?  129 ALA   B CA   1 
ATOM   5691 C C    . ALA   B 1 129 ? 43.386 -31.101 2.096   1.00 15.62 ?  129 ALA   B C    1 
ATOM   5692 O O    . ALA   B 1 129 ? 43.942 -30.206 2.749   1.00 15.26 ?  129 ALA   B O    1 
ATOM   5693 C CB   . ALA   B 1 129 ? 42.029 -31.098 -0.012  1.00 18.71 ?  129 ALA   B CB   1 
ATOM   5694 H H    . ALA   B 1 129 ? 41.525 -29.035 1.233   1.00 18.86 ?  129 ALA   B H    1 
ATOM   5695 H HA   . ALA   B 1 129 ? 41.423 -31.618 1.870   1.00 19.97 ?  129 ALA   B HA   1 
ATOM   5696 H HB1  . ALA   B 1 129 ? 42.388 -31.977 -0.223  1.00 22.43 ?  129 ALA   B HB1  1 
ATOM   5697 H HB2  . ALA   B 1 129 ? 41.129 -31.018 -0.362  1.00 22.43 ?  129 ALA   B HB2  1 
ATOM   5698 H HB3  . ALA   B 1 129 ? 42.597 -30.412 -0.397  1.00 22.43 ?  129 ALA   B HB3  1 
ATOM   5699 N N    . GLY   B 1 130 ? 43.953 -32.282 1.859   1.00 15.55 ?  130 GLY   B N    1 
ATOM   5700 C CA   . GLY   B 1 130 ? 45.343 -32.513 2.202   1.00 16.00 ?  130 GLY   B CA   1 
ATOM   5701 C C    . GLY   B 1 130 ? 45.557 -32.421 3.693   1.00 16.16 ?  130 GLY   B C    1 
ATOM   5702 O O    . GLY   B 1 130 ? 44.867 -33.076 4.486   1.00 17.39 ?  130 GLY   B O    1 
ATOM   5703 H H    . GLY   B 1 130 ? 43.561 -32.957 1.496   1.00 18.64 ?  130 GLY   B H    1 
ATOM   5704 H HA2  . GLY   B 1 130 ? 45.614 -33.399 1.904   1.00 19.17 ?  130 GLY   B HA2  1 
ATOM   5705 H HA3  . GLY   B 1 130 ? 45.907 -31.857 1.762   1.00 19.17 ?  130 GLY   B HA3  1 
ATOM   5706 N N    . ILE   B 1 131 ? 46.531 -31.592 4.084   1.00 16.70 ?  131 ILE   B N    1 
ATOM   5707 C CA   . ILE   B 1 131 ? 46.887 -31.468 5.490   1.00 17.69 ?  131 ILE   B CA   1 
ATOM   5708 C C    . ILE   B 1 131 ? 45.772 -30.872 6.328   1.00 16.92 ?  131 ILE   B C    1 
ATOM   5709 O O    . ILE   B 1 131 ? 45.846 -30.942 7.559   1.00 18.47 ?  131 ILE   B O    1 
ATOM   5710 C CB   . ILE   B 1 131 ? 48.214 -30.702 5.687   1.00 19.47 ?  131 ILE   B CB   1 
ATOM   5711 C CG1  . ILE   B 1 131 ? 48.051 -29.223 5.318   1.00 20.44 ?  131 ILE   B CG1  1 
ATOM   5712 C CG2  . ILE   B 1 131 ? 49.326 -31.345 4.862   1.00 20.60 ?  131 ILE   B CG2  1 
ATOM   5713 C CD1  . ILE   B 1 131 ? 49.272 -28.368 5.614   1.00 21.45 ?  131 ILE   B CD1  1 
ATOM   5714 H H    . ILE   B 1 131 ? 46.993 -31.087 3.558   1.00 20.02 ?  131 ILE   B H    1 
ATOM   5715 H HA   . ILE   B 1 131 ? 47.030 -32.359 5.834   1.00 21.20 ?  131 ILE   B HA   1 
ATOM   5716 H HB   . ILE   B 1 131 ? 48.456 -30.754 6.626   1.00 23.34 ?  131 ILE   B HB   1 
ATOM   5717 H HG12 . ILE   B 1 131 ? 47.866 -29.160 4.368   1.00 24.51 ?  131 ILE   B HG12 1 
ATOM   5718 H HG13 . ILE   B 1 131 ? 47.308 -28.847 5.819   1.00 24.51 ?  131 ILE   B HG13 1 
ATOM   5719 H HG21 . ILE   B 1 131 ? 50.172 -30.949 5.116   1.00 24.70 ?  131 ILE   B HG21 1 
ATOM   5720 H HG22 . ILE   B 1 131 ? 49.333 -32.296 5.039   1.00 24.70 ?  131 ILE   B HG22 1 
ATOM   5721 H HG23 . ILE   B 1 131 ? 49.149 -31.182 3.922   1.00 24.70 ?  131 ILE   B HG23 1 
ATOM   5722 H HD11 . ILE   B 1 131 ? 49.052 -27.439 5.442   1.00 25.72 ?  131 ILE   B HD11 1 
ATOM   5723 H HD12 . ILE   B 1 131 ? 49.517 -28.484 6.545   1.00 25.72 ?  131 ILE   B HD12 1 
ATOM   5724 H HD13 . ILE   B 1 131 ? 49.999 -28.650 5.040   1.00 25.72 ?  131 ILE   B HD13 1 
ATOM   5725 N N    . PHE   B 1 132 ? 44.740 -30.296 5.699   1.00 15.62 ?  132 PHE   B N    1 
ATOM   5726 C CA   . PHE   B 1 132 ? 43.587 -29.784 6.430   1.00 16.16 ?  132 PHE   B CA   1 
ATOM   5727 C C    . PHE   B 1 132 ? 42.558 -30.865 6.759   1.00 17.44 ?  132 PHE   B C    1 
ATOM   5728 O O    . PHE   B 1 132 ? 41.657 -30.608 7.564   1.00 19.05 ?  132 PHE   B O    1 
ATOM   5729 C CB   . PHE   B 1 132 ? 42.918 -28.647 5.646   1.00 15.06 ?  132 PHE   B CB   1 
ATOM   5730 C CG   . PHE   B 1 132 ? 43.618 -27.305 5.764   1.00 14.86 ?  132 PHE   B CG   1 
ATOM   5731 C CD1  . PHE   B 1 132 ? 44.922 -27.125 5.325   1.00 16.34 ?  132 PHE   B CD1  1 
ATOM   5732 C CD2  . PHE   B 1 132 ? 42.932 -26.203 6.263   1.00 14.73 ?  132 PHE   B CD2  1 
ATOM   5733 C CE1  . PHE   B 1 132 ? 45.540 -25.885 5.427   1.00 16.74 ?  132 PHE   B CE1  1 
ATOM   5734 C CE2  . PHE   B 1 132 ? 43.538 -24.961 6.356   1.00 15.23 ?  132 PHE   B CE2  1 
ATOM   5735 C CZ   . PHE   B 1 132 ? 44.842 -24.803 5.940   1.00 16.07 ?  132 PHE   B CZ   1 
ATOM   5736 H H    . PHE   B 1 132 ? 44.684 -30.192 4.844   1.00 18.72 ?  132 PHE   B H    1 
ATOM   5737 H HA   . PHE   B 1 132 ? 43.895 -29.411 7.268   1.00 19.37 ?  132 PHE   B HA   1 
ATOM   5738 H HB2  . PHE   B 1 132 ? 42.904 -28.885 4.708   1.00 18.05 ?  132 PHE   B HB2  1 
ATOM   5739 H HB3  . PHE   B 1 132 ? 42.009 -28.536 5.971   1.00 18.05 ?  132 PHE   B HB3  1 
ATOM   5740 H HD1  . PHE   B 1 132 ? 45.396 -27.855 4.989   1.00 19.59 ?  132 PHE   B HD1  1 
ATOM   5741 H HD2  . PHE   B 1 132 ? 42.050 -26.304 6.548   1.00 17.66 ?  132 PHE   B HD2  1 
ATOM   5742 H HE1  . PHE   B 1 132 ? 46.421 -25.785 5.147   1.00 20.07 ?  132 PHE   B HE1  1 
ATOM   5743 H HE2  . PHE   B 1 132 ? 43.068 -24.237 6.707   1.00 18.26 ?  132 PHE   B HE2  1 
ATOM   5744 H HZ   . PHE   B 1 132 ? 45.256 -23.972 6.010   1.00 19.26 ?  132 PHE   B HZ   1 
ATOM   5745 N N    . GLY   B 1 133 ? 42.654 -32.057 6.157   1.00 17.35 ?  133 GLY   B N    1 
ATOM   5746 C CA   . GLY   B 1 133 ? 41.941 -33.223 6.651   1.00 18.17 ?  133 GLY   B CA   1 
ATOM   5747 C C    . GLY   B 1 133 ? 40.547 -33.485 6.113   1.00 18.81 ?  133 GLY   B C    1 
ATOM   5748 O O    . GLY   B 1 133 ? 39.962 -34.512 6.470   1.00 20.79 ?  133 GLY   B O    1 
ATOM   5749 H H    . GLY   B 1 133 ? 43.133 -32.205 5.457   1.00 20.80 ?  133 GLY   B H    1 
ATOM   5750 H HA2  . GLY   B 1 133 ? 42.478 -34.005 6.460   1.00 21.79 ?  133 GLY   B HA2  1 
ATOM   5751 H HA3  . GLY   B 1 133 ? 41.866 -33.144 7.613   1.00 21.79 ?  133 GLY   B HA3  1 
ATOM   5752 N N    . ALA   B 1 134 ? 39.982 -32.611 5.287   1.00 17.94 ?  134 ALA   B N    1 
ATOM   5753 C CA   . ALA   B 1 134 ? 38.657 -32.895 4.754   1.00 17.56 ?  134 ALA   B CA   1 
ATOM   5754 C C    . ALA   B 1 134 ? 38.746 -33.888 3.601   1.00 17.76 ?  134 ALA   B C    1 
ATOM   5755 O O    . ALA   B 1 134 ? 39.805 -34.085 2.996   1.00 19.02 ?  134 ALA   B O    1 
ATOM   5756 C CB   . ALA   B 1 134 ? 37.974 -31.613 4.279   1.00 17.96 ?  134 ALA   B CB   1 
ATOM   5757 H H    . ALA   B 1 134 ? 40.328 -31.863 5.030   1.00 21.50 ?  134 ALA   B H    1 
ATOM   5758 H HA   . ALA   B 1 134 ? 38.110 -33.287 5.453   1.00 21.04 ?  134 ALA   B HA   1 
ATOM   5759 H HB1  . ALA   B 1 134 ? 37.088 -31.834 3.947   1.00 21.53 ?  134 ALA   B HB1  1 
ATOM   5760 H HB2  . ALA   B 1 134 ? 37.902 -30.998 5.025   1.00 21.53 ?  134 ALA   B HB2  1 
ATOM   5761 H HB3  . ALA   B 1 134 ? 38.502 -31.217 3.570   1.00 21.53 ?  134 ALA   B HB3  1 
ATOM   5762 N N    . ASP   B 1 135 ? 37.610 -34.510 3.302   1.00 18.06 ?  135 ASP   B N    1 
ATOM   5763 C CA   . ASP   B 1 135 ? 37.518 -35.410 2.160   1.00 18.88 ?  135 ASP   B CA   1 
ATOM   5764 C C    . ASP   B 1 135 ? 37.612 -34.576 0.891   1.00 17.48 ?  135 ASP   B C    1 
ATOM   5765 O O    . ASP   B 1 135 ? 36.761 -33.700 0.674   1.00 17.46 ?  135 ASP   B O    1 
ATOM   5766 C CB   . ASP   B 1 135 ? 36.179 -36.143 2.210   1.00 20.45 ?  135 ASP   B CB   1 
ATOM   5767 C CG   . ASP   B 1 135 ? 36.003 -37.145 1.083   1.00 22.33 ?  135 ASP   B CG   1 
ATOM   5768 O OD1  . ASP   B 1 135 ? 36.864 -37.197 0.182   1.00 21.96 ?  135 ASP   B OD1  1 
ATOM   5769 O OD2  . ASP   B 1 135 ? 35.009 -37.910 1.116   1.00 25.53 -1 135 ASP   B OD2  1 
ATOM   5770 H H    . ASP   B 1 135 ? 36.877 -34.427 3.746   1.00 21.65 ?  135 ASP   B H    1 
ATOM   5771 H HA   . ASP   B 1 135 ? 38.239 -36.056 2.193   1.00 22.64 ?  135 ASP   B HA   1 
ATOM   5772 H HB2  . ASP   B 1 135 ? 36.124 -36.629 3.042   1.00 24.52 ?  135 ASP   B HB2  1 
ATOM   5773 H HB3  . ASP   B 1 135 ? 35.467 -35.492 2.147   1.00 24.52 ?  135 ASP   B HB3  1 
ATOM   5774 N N    . PRO   B 1 136 ? 38.620 -34.784 0.041   1.00 17.57 ?  136 PRO   B N    1 
ATOM   5775 C CA   . PRO   B 1 136 ? 38.713 -33.961 -1.176  1.00 16.85 ?  136 PRO   B CA   1 
ATOM   5776 C C    . PRO   B 1 136 ? 37.520 -34.111 -2.096  1.00 15.93 ?  136 PRO   B C    1 
ATOM   5777 O O    . PRO   B 1 136 ? 37.198 -33.165 -2.821  1.00 15.15 ?  136 PRO   B O    1 
ATOM   5778 C CB   . PRO   B 1 136 ? 40.019 -34.438 -1.831  1.00 18.05 ?  136 PRO   B CB   1 
ATOM   5779 C CG   . PRO   B 1 136 ? 40.238 -35.822 -1.274  1.00 19.25 ?  136 PRO   B CG   1 
ATOM   5780 C CD   . PRO   B 1 136 ? 39.710 -35.770 0.126   1.00 18.54 ?  136 PRO   B CD   1 
ATOM   5781 H HA   . PRO   B 1 136 ? 38.803 -33.023 -0.946  1.00 20.20 ?  136 PRO   B HA   1 
ATOM   5782 H HB2  . PRO   B 1 136 ? 39.917 -34.464 -2.798  1.00 21.63 ?  136 PRO   B HB2  1 
ATOM   5783 H HB3  . PRO   B 1 136 ? 40.745 -33.844 -1.582  1.00 21.63 ?  136 PRO   B HB3  1 
ATOM   5784 H HG2  . PRO   B 1 136 ? 39.743 -36.468 -1.801  1.00 23.08 ?  136 PRO   B HG2  1 
ATOM   5785 H HG3  . PRO   B 1 136 ? 41.185 -36.029 -1.275  1.00 23.08 ?  136 PRO   B HG3  1 
ATOM   5786 H HD2  . PRO   B 1 136 ? 39.360 -36.632 0.390   1.00 22.22 ?  136 PRO   B HD2  1 
ATOM   5787 H HD3  . PRO   B 1 136 ? 40.395 -35.457 0.741   1.00 22.22 ?  136 PRO   B HD3  1 
ATOM   5788 N N    . ILE   B 1 137 ? 36.866 -35.278 -2.103  1.00 16.23 ?  137 ILE   B N    1 
ATOM   5789 C CA   . ILE   B 1 137 ? 35.646 -35.443 -2.889  1.00 16.81 ?  137 ILE   B CA   1 
ATOM   5790 C C    . ILE   B 1 137 ? 34.575 -34.471 -2.407  1.00 16.48 ?  137 ILE   B C    1 
ATOM   5791 O O    . ILE   B 1 137 ? 33.850 -33.863 -3.205  1.00 15.97 ?  137 ILE   B O    1 
ATOM   5792 C CB   . ILE   B 1 137 ? 35.172 -36.912 -2.823  1.00 18.92 ?  137 ILE   B CB   1 
ATOM   5793 C CG1  . ILE   B 1 137 ? 36.154 -37.823 -3.567  1.00 21.25 ?  137 ILE   B CG1  1 
ATOM   5794 C CG2  . ILE   B 1 137 ? 33.768 -37.062 -3.396  1.00 19.48 ?  137 ILE   B CG2  1 
ATOM   5795 C CD1  . ILE   B 1 137 ? 35.859 -39.308 -3.415  1.00 23.68 ?  137 ILE   B CD1  1 
ATOM   5796 H H    . ILE   B 1 137 ? 37.105 -35.981 -1.672  1.00 19.45 ?  137 ILE   B H    1 
ATOM   5797 H HA   . ILE   B 1 137 ? 35.835 -35.242 -3.821  1.00 20.15 ?  137 ILE   B HA   1 
ATOM   5798 H HB   . ILE   B 1 137 ? 35.148 -37.186 -1.898  1.00 22.68 ?  137 ILE   B HB   1 
ATOM   5799 H HG12 . ILE   B 1 137 ? 36.124 -37.617 -4.515  1.00 25.48 ?  137 ILE   B HG12 1 
ATOM   5800 H HG13 . ILE   B 1 137 ? 37.047 -37.668 -3.226  1.00 25.48 ?  137 ILE   B HG13 1 
ATOM   5801 H HG21 . ILE   B 1 137 ? 33.539 -38.004 -3.458  1.00 23.36 ?  137 ILE   B HG21 1 
ATOM   5802 H HG22 . ILE   B 1 137 ? 33.134 -36.621 -2.811  1.00 23.36 ?  137 ILE   B HG22 1 
ATOM   5803 H HG23 . ILE   B 1 137 ? 33.740 -36.662 -4.279  1.00 23.36 ?  137 ILE   B HG23 1 
ATOM   5804 H HD11 . ILE   B 1 137 ? 36.565 -39.809 -3.851  1.00 28.39 ?  137 ILE   B HD11 1 
ATOM   5805 H HD12 . ILE   B 1 137 ? 35.827 -39.534 -2.471  1.00 28.39 ?  137 ILE   B HD12 1 
ATOM   5806 H HD13 . ILE   B 1 137 ? 35.009 -39.518 -3.834  1.00 28.39 ?  137 ILE   B HD13 1 
ATOM   5807 N N    . HIS   B 1 138 ? 34.449 -34.325 -1.093  1.00 16.38 ?  138 HIS   B N    1 
ATOM   5808 C CA   . HIS   B 1 138 ? 33.499 -33.360 -0.556  1.00 16.89 ?  138 HIS   B CA   1 
ATOM   5809 C C    . HIS   B 1 138 ? 33.918 -31.931 -0.875  1.00 16.04 ?  138 HIS   B C    1 
ATOM   5810 O O    . HIS   B 1 138 ? 33.071 -31.085 -1.184  1.00 16.76 ?  138 HIS   B O    1 
ATOM   5811 C CB   . HIS   B 1 138 ? 33.366 -33.545 0.948   1.00 18.38 ?  138 HIS   B CB   1 
ATOM   5812 C CG   . HIS   B 1 138 ? 32.438 -32.561 1.579   1.00 19.56 ?  138 HIS   B CG   1 
ATOM   5813 N ND1  . HIS   B 1 138 ? 31.102 -32.485 1.249   1.00 20.93 ?  138 HIS   B ND1  1 
ATOM   5814 C CD2  . HIS   B 1 138 ? 32.657 -31.582 2.488   1.00 20.19 ?  138 HIS   B CD2  1 
ATOM   5815 C CE1  . HIS   B 1 138 ? 30.532 -31.516 1.942   1.00 20.95 ?  138 HIS   B CE1  1 
ATOM   5816 N NE2  . HIS   B 1 138 ? 31.453 -30.954 2.706   1.00 20.25 ?  138 HIS   B NE2  1 
ATOM   5817 H H    . HIS   B 1 138 ? 34.894 -34.768 -0.507  1.00 19.63 ?  138 HIS   B H    1 
ATOM   5818 H HA   . HIS   B 1 138 ? 32.631 -33.522 -0.960  1.00 20.25 ?  138 HIS   B HA   1 
ATOM   5819 H HB2  . HIS   B 1 138 ? 33.019 -34.436 1.125   1.00 22.03 ?  138 HIS   B HB2  1 
ATOM   5820 H HB3  . HIS   B 1 138 ? 34.235 -33.441 1.357   1.00 22.03 ?  138 HIS   B HB3  1 
ATOM   5821 H HD1  . HIS   B 1 138 ? 30.699 -33.000 0.684   1.00 25.09 ?  138 HIS   B HD1  1 
ATOM   5822 H HD2  . HIS   B 1 138 ? 33.461 -31.382 2.900   1.00 24.20 ?  138 HIS   B HD2  1 
ATOM   5823 H HE1  . HIS   B 1 138 ? 29.630 -31.281 1.905   1.00 25.11 ?  138 HIS   B HE1  1 
ATOM   5824 N N    . SER   B 1 139 ? 35.212 -31.634 -0.799  1.00 15.54 ?  139 SER   B N    1 
ATOM   5825 C CA   . SER   B 1 139 ? 35.652 -30.283 -1.118  1.00 14.90 ?  139 SER   B CA   1 
ATOM   5826 C C    . SER   B 1 139 ? 35.317 -29.931 -2.558  1.00 13.93 ?  139 SER   B C    1 
ATOM   5827 O O    . SER   B 1 139 ? 34.876 -28.811 -2.839  1.00 14.36 ?  139 SER   B O    1 
ATOM   5828 C CB   . SER   B 1 139 ? 37.143 -30.137 -0.840  1.00 14.97 ?  139 SER   B CB   1 
ATOM   5829 O OG   . SER   B 1 139 ? 37.560 -28.806 -1.105  1.00 15.10 ?  139 SER   B OG   1 
ATOM   5830 H H    . SER   B 1 139 ? 35.836 -32.179 -0.583  1.00 18.62 ?  139 SER   B H    1 
ATOM   5831 H HA   . SER   B 1 139 ? 35.175 -29.660 -0.553  1.00 17.86 ?  139 SER   B HA   1 
ATOM   5832 H HB2  . SER   B 1 139 ? 37.310 -30.350 0.093   1.00 17.94 ?  139 SER   B HB2  1 
ATOM   5833 H HB3  . SER   B 1 139 ? 37.638 -30.735 -1.415  1.00 17.94 ?  139 SER   B HB3  1 
ATOM   5834 H HG   . SER   B 1 139 ? 38.377 -28.719 -0.931  1.00 18.09 ?  139 SER   B HG   1 
ATOM   5835 N N    . LEU   B 1 140 ? 35.508 -30.874 -3.484  1.00 14.12 ?  140 LEU   B N    1 
ATOM   5836 C CA   . LEU   B 1 140 ? 35.137 -30.631 -4.872  1.00 14.15 ?  140 LEU   B CA   1 
ATOM   5837 C C    . LEU   B 1 140 ? 33.632 -30.398 -5.000  1.00 14.32 ?  140 LEU   B C    1 
ATOM   5838 O O    . LEU   B 1 140 ? 33.195 -29.510 -5.738  1.00 13.93 ?  140 LEU   B O    1 
ATOM   5839 C CB   . LEU   B 1 140 ? 35.603 -31.796 -5.745  1.00 14.10 ?  140 LEU   B CB   1 
ATOM   5840 C CG   . LEU   B 1 140 ? 35.238 -31.684 -7.217  1.00 14.31 ?  140 LEU   B CG   1 
ATOM   5841 C CD1  . LEU   B 1 140 ? 35.822 -30.416 -7.809  1.00 15.63 ?  140 LEU   B CD1  1 
ATOM   5842 C CD2  . LEU   B 1 140 ? 35.698 -32.918 -7.973  1.00 15.27 ?  140 LEU   B CD2  1 
ATOM   5843 H H    . LEU   B 1 140 ? 35.842 -31.649 -3.337  1.00 16.92 ?  140 LEU   B H    1 
ATOM   5844 H HA   . LEU   B 1 140 ? 35.591 -29.831 -5.183  1.00 16.95 ?  140 LEU   B HA   1 
ATOM   5845 H HB2  . LEU   B 1 140 ? 36.569 -31.865 -5.688  1.00 16.90 ?  140 LEU   B HB2  1 
ATOM   5846 H HB3  . LEU   B 1 140 ? 35.200 -32.616 -5.412  1.00 16.90 ?  140 LEU   B HB3  1 
ATOM   5847 H HG   . LEU   B 1 140 ? 34.276 -31.625 -7.299  1.00 17.14 ?  140 LEU   B HG   1 
ATOM   5848 H HD11 . LEU   B 1 140 ? 35.729 -30.444 -8.772  1.00 18.74 ?  140 LEU   B HD11 1 
ATOM   5849 H HD12 . LEU   B 1 140 ? 35.346 -29.649 -7.452  1.00 18.74 ?  140 LEU   B HD12 1 
ATOM   5850 H HD13 . LEU   B 1 140 ? 36.763 -30.359 -7.570  1.00 18.74 ?  140 LEU   B HD13 1 
ATOM   5851 H HD21 . LEU   B 1 140 ? 35.449 -32.820 -8.907  1.00 18.30 ?  140 LEU   B HD21 1 
ATOM   5852 H HD22 . LEU   B 1 140 ? 36.653 -33.005 -7.887  1.00 18.30 ?  140 LEU   B HD22 1 
ATOM   5853 H HD23 . LEU   B 1 140 ? 35.251 -33.694 -7.596  1.00 18.30 ?  140 LEU   B HD23 1 
ATOM   5854 N N    . ARG   B 1 141 ? 32.830 -31.188 -4.281  1.00 14.69 ?  141 ARG   B N    1 
ATOM   5855 C CA   . ARG   B 1 141 ? 31.379 -31.012 -4.264  1.00 15.54 ?  141 ARG   B CA   1 
ATOM   5856 C C    . ARG   B 1 141 ? 30.999 -29.600 -3.835  1.00 15.24 ?  141 ARG   B C    1 
ATOM   5857 O O    . ARG   B 1 141 ? 30.196 -28.922 -4.494  1.00 15.12 ?  141 ARG   B O    1 
ATOM   5858 C CB   . ARG   B 1 141 ? 30.788 -32.039 -3.291  1.00 16.77 ?  141 ARG   B CB   1 
ATOM   5859 C CG   . ARG   B 1 141 ? 29.318 -31.916 -2.979  1.00 18.64 ?  141 ARG   B CG   1 
ATOM   5860 C CD   . ARG   B 1 141 ? 28.528 -32.558 -4.050  1.00 20.60 ?  141 ARG   B CD   1 
ATOM   5861 N NE   . ARG   B 1 141 ? 28.258 -31.646 -5.150  1.00 20.81 ?  141 ARG   B NE   1 
ATOM   5862 C CZ   . ARG   B 1 141 ? 28.228 -31.995 -6.429  1.00 20.17 ?  141 ARG   B CZ   1 
ATOM   5863 N NH1  . ARG   B 1 141 ? 28.645 -33.185 -6.834  1.00 20.00 ?  141 ARG   B NH1  1 
ATOM   5864 N NH2  . ARG   B 1 141 ? 27.767 -31.126 -7.325  1.00 21.00 ?  141 ARG   B NH2  1 
ATOM   5865 H H    . ARG   B 1 141 ? 33.110 -31.830 -3.788  1.00 17.60 ?  141 ARG   B H    1 
ATOM   5866 H HA   . ARG   B 1 141 ? 31.019 -31.167 -5.146  1.00 18.63 ?  141 ARG   B HA   1 
ATOM   5867 H HB2  . ARG   B 1 141 ? 30.943 -32.921 -3.659  1.00 20.10 ?  141 ARG   B HB2  1 
ATOM   5868 H HB3  . ARG   B 1 141 ? 31.263 -31.961 -2.450  1.00 20.10 ?  141 ARG   B HB3  1 
ATOM   5869 H HG2  . ARG   B 1 141 ? 29.133 -32.358 -2.141  1.00 22.34 ?  141 ARG   B HG2  1 
ATOM   5870 H HG3  . ARG   B 1 141 ? 29.063 -30.975 -2.925  1.00 22.34 ?  141 ARG   B HG3  1 
ATOM   5871 H HD2  . ARG   B 1 141 ? 29.018 -33.326 -4.394  1.00 24.70 ?  141 ARG   B HD2  1 
ATOM   5872 H HD3  . ARG   B 1 141 ? 27.685 -32.853 -3.682  1.00 24.70 ?  141 ARG   B HD3  1 
ATOM   5873 H HE   . ARG   B 1 141 ? 28.083 -30.826 -4.954  1.00 24.95 ?  141 ARG   B HE   1 
ATOM   5874 H HH11 . ARG   B 1 141 ? 28.932 -33.761 -6.267  1.00 23.98 ?  141 ARG   B HH11 1 
ATOM   5875 H HH12 . ARG   B 1 141 ? 28.622 -33.381 -7.669  1.00 23.98 ?  141 ARG   B HH12 1 
ATOM   5876 H HH21 . ARG   B 1 141 ? 27.500 -30.345 -7.075  1.00 25.18 ?  141 ARG   B HH21 1 
ATOM   5877 H HH22 . ARG   B 1 141 ? 27.761 -31.329 -8.162  1.00 25.18 ?  141 ARG   B HH22 1 
ATOM   5878 N N    . VAL   B 1 142 ? 31.546 -29.151 -2.709  1.00 14.78 ?  142 VAL   B N    1 
ATOM   5879 C CA   . VAL   B 1 142 ? 31.218 -27.817 -2.224  1.00 14.17 ?  142 VAL   B CA   1 
ATOM   5880 C C    . VAL   B 1 142 ? 31.695 -26.759 -3.214  1.00 14.12 ?  142 VAL   B C    1 
ATOM   5881 O O    . VAL   B 1 142 ? 30.997 -25.773 -3.475  1.00 14.62 ?  142 VAL   B O    1 
ATOM   5882 C CB   . VAL   B 1 142 ? 31.772 -27.597 -0.803  1.00 15.00 ?  142 VAL   B CB   1 
ATOM   5883 C CG1  . VAL   B 1 142 ? 31.452 -26.183 -0.315  1.00 14.71 ?  142 VAL   B CG1  1 
ATOM   5884 C CG2  . VAL   B 1 142 ? 31.195 -28.627 0.154   1.00 15.84 ?  142 VAL   B CG2  1 
ATOM   5885 H H    . VAL   B 1 142 ? 32.108 -29.583 -2.220  1.00 17.71 ?  142 VAL   B H    1 
ATOM   5886 H HA   . VAL   B 1 142 ? 30.257 -27.741 -2.164  1.00 16.98 ?  142 VAL   B HA   1 
ATOM   5887 H HB   . VAL   B 1 142 ? 32.737 -27.698 -0.810  1.00 17.98 ?  142 VAL   B HB   1 
ATOM   5888 H HG11 . VAL   B 1 142 ? 31.641 -26.126 0.635   1.00 17.63 ?  142 VAL   B HG11 1 
ATOM   5889 H HG12 . VAL   B 1 142 ? 32.002 -25.548 -0.799  1.00 17.63 ?  142 VAL   B HG12 1 
ATOM   5890 H HG13 . VAL   B 1 142 ? 30.513 -26.001 -0.476  1.00 17.63 ?  142 VAL   B HG13 1 
ATOM   5891 H HG21 . VAL   B 1 142 ? 31.511 -28.443 1.051   1.00 18.98 ?  142 VAL   B HG21 1 
ATOM   5892 H HG22 . VAL   B 1 142 ? 30.227 -28.576 0.125   1.00 18.98 ?  142 VAL   B HG22 1 
ATOM   5893 H HG23 . VAL   B 1 142 ? 31.486 -29.512 -0.124  1.00 18.98 ?  142 VAL   B HG23 1 
ATOM   5894 N N    . CYS   B 1 143 ? 32.878 -26.956 -3.798  1.00 13.64 ?  143 CYS   B N    1 
ATOM   5895 C CA   . CYS   B 1 143 ? 33.370 -26.020 -4.803  1.00 13.36 ?  143 CYS   B CA   1 
ATOM   5896 C C    . CYS   B 1 143 ? 32.368 -25.878 -5.945  1.00 13.64 ?  143 CYS   B C    1 
ATOM   5897 O O    . CYS   B 1 143 ? 31.964 -24.768 -6.308  1.00 13.87 ?  143 CYS   B O    1 
ATOM   5898 C CB   . CYS   B 1 143 ? 34.724 -26.506 -5.328  1.00 13.65 ?  143 CYS   B CB   1 
ATOM   5899 S SG   . CYS   B 1 143 ? 35.477 -25.410 -6.556  1.00 14.07 ?  143 CYS   B SG   1 
ATOM   5900 H H    . CYS   B 1 143 ? 33.403 -27.611 -3.629  1.00 16.34 ?  143 CYS   B H    1 
ATOM   5901 H HA   . CYS   B 1 143 ? 33.499 -25.145 -4.395  1.00 16.01 ?  143 CYS   B HA   1 
ATOM   5902 H HB2  . CYS   B 1 143 ? 35.344 -26.583 -4.585  1.00 16.36 ?  143 CYS   B HB2  1 
ATOM   5903 H HB3  . CYS   B 1 143 ? 34.603 -27.372 -5.739  1.00 16.36 ?  143 CYS   B HB3  1 
ATOM   5904 H HG   . CYS   B 1 143 ? 36.552 -25.849 -6.870  1.00 16.86 ?  143 CYS   B HG   1 
ATOM   5905 N N    . VAL   B 1 144 ? 31.961 -27.000 -6.531  1.00 14.41 ?  144 VAL   B N    1 
ATOM   5906 C CA   . VAL   B 1 144 ? 31.054 -26.940 -7.673  1.00 15.54 ?  144 VAL   B CA   1 
ATOM   5907 C C    . VAL   B 1 144 ? 29.712 -26.326 -7.298  1.00 15.18 ?  144 VAL   B C    1 
ATOM   5908 O O    . VAL   B 1 144 ? 29.098 -25.616 -8.108  1.00 16.38 ?  144 VAL   B O    1 
ATOM   5909 C CB   . VAL   B 1 144 ? 30.898 -28.349 -8.254  1.00 17.73 ?  144 VAL   B CB   1 
ATOM   5910 C CG1  . VAL   B 1 144 ? 29.625 -28.475 -9.094  1.00 20.24 ?  144 VAL   B CG1  1 
ATOM   5911 C CG2  . VAL   B 1 144 ? 32.146 -28.743 -9.039  1.00 17.83 ?  144 VAL   B CG2  1 
ATOM   5912 H H    . VAL   B 1 144 ? 32.191 -27.792 -6.294  1.00 17.27 ?  144 VAL   B H    1 
ATOM   5913 H HA   . VAL   B 1 144 ? 31.444 -26.381 -8.359  1.00 18.62 ?  144 VAL   B HA   1 
ATOM   5914 H HB   . VAL   B 1 144 ? 30.815 -28.979 -7.518  1.00 21.25 ?  144 VAL   B HB   1 
ATOM   5915 H HG11 . VAL   B 1 144 ? 29.703 -29.260 -9.662  1.00 24.27 ?  144 VAL   B HG11 1 
ATOM   5916 H HG12 . VAL   B 1 144 ? 28.864 -28.575 -8.503  1.00 24.27 ?  144 VAL   B HG12 1 
ATOM   5917 H HG13 . VAL   B 1 144 ? 29.529 -27.683 -9.641  1.00 24.27 ?  144 VAL   B HG13 1 
ATOM   5918 H HG21 . VAL   B 1 144 ? 32.029 -29.640 -9.391  1.00 21.38 ?  144 VAL   B HG21 1 
ATOM   5919 H HG22 . VAL   B 1 144 ? 32.266 -28.115 -9.771  1.00 21.38 ?  144 VAL   B HG22 1 
ATOM   5920 H HG23 . VAL   B 1 144 ? 32.911 -28.715 -8.448  1.00 21.38 ?  144 VAL   B HG23 1 
ATOM   5921 N N    . ASP   B 1 145 ? 29.244 -26.566 -6.078  1.00 15.56 ?  145 ASP   B N    1 
ATOM   5922 C CA   . ASP   B 1 145 ? 27.937 -26.100 -5.642  1.00 16.04 ?  145 ASP   B CA   1 
ATOM   5923 C C    . ASP   B 1 145 ? 27.967 -24.678 -5.099  1.00 15.93 ?  145 ASP   B C    1 
ATOM   5924 O O    . ASP   B 1 145 ? 26.907 -24.136 -4.762  1.00 17.67 ?  145 ASP   B O    1 
ATOM   5925 C CB   . ASP   B 1 145 ? 27.364 -27.021 -4.559  1.00 17.62 ?  145 ASP   B CB   1 
ATOM   5926 C CG   . ASP   B 1 145 ? 27.000 -28.393 -5.073  1.00 19.52 ?  145 ASP   B CG   1 
ATOM   5927 O OD1  . ASP   B 1 145 ? 26.878 -28.581 -6.302  1.00 19.80 ?  145 ASP   B OD1  1 
ATOM   5928 O OD2  . ASP   B 1 145 ? 26.825 -29.281 -4.220  1.00 21.39 -1 145 ASP   B OD2  1 
ATOM   5929 H H    . ASP   B 1 145 ? 29.682 -26.987 -5.470  1.00 18.64 ?  145 ASP   B H    1 
ATOM   5930 H HA   . ASP   B 1 145 ? 27.336 -26.097 -6.398  1.00 19.22 ?  145 ASP   B HA   1 
ATOM   5931 H HB2  . ASP   B 1 145 ? 28.024 -27.142 -3.868  1.00 21.12 ?  145 ASP   B HB2  1 
ATOM   5932 H HB3  . ASP   B 1 145 ? 26.563 -26.613 -4.197  1.00 21.12 ?  145 ASP   B HB3  1 
ATOM   5933 N N    . THR   B 1 146 ? 29.144 -24.060 -5.003  1.00 14.06 ?  146 THR   B N    1 
ATOM   5934 C CA   . THR   B 1 146 ? 29.282 -22.739 -4.395  1.00 13.66 ?  146 THR   B CA   1 
ATOM   5935 C C    . THR   B 1 146 ? 29.919 -21.709 -5.311  1.00 13.39 ?  146 THR   B C    1 
ATOM   5936 O O    . THR   B 1 146 ? 29.467 -20.551 -5.356  1.00 13.74 ?  146 THR   B O    1 
ATOM   5937 C CB   . THR   B 1 146 ? 30.114 -22.844 -3.112  1.00 14.02 ?  146 THR   B CB   1 
ATOM   5938 O OG1  . THR   B 1 146 ? 29.538 -23.831 -2.248  1.00 14.10 ?  146 THR   B OG1  1 
ATOM   5939 C CG2  . THR   B 1 146 ? 30.208 -21.504 -2.395  1.00 14.15 ?  146 THR   B CG2  1 
ATOM   5940 H H    . THR   B 1 146 ? 29.893 -24.382 -5.289  1.00 16.85 ?  146 THR   B H    1 
ATOM   5941 H HA   . THR   B 1 146 ? 28.409 -22.408 -4.151  1.00 16.37 ?  146 THR   B HA   1 
ATOM   5942 H HB   . THR   B 1 146 ? 31.019 -23.110 -3.340  1.00 16.80 ?  146 THR   B HB   1 
ATOM   5943 H HG1  . THR   B 1 146 ? 29.568 -24.589 -2.620  1.00 16.90 ?  146 THR   B HG1  1 
ATOM   5944 H HG21 . THR   B 1 146 ? 30.555 -21.627 -1.499  1.00 16.95 ?  146 THR   B HG21 1 
ATOM   5945 H HG22 . THR   B 1 146 ? 30.806 -20.907 -2.880  1.00 16.95 ?  146 THR   B HG22 1 
ATOM   5946 H HG23 . THR   B 1 146 ? 29.332 -21.094 -2.342  1.00 16.95 ?  146 THR   B HG23 1 
ATOM   5947 N N    . VAL   B 1 147 ? 30.982 -22.086 -6.013  1.00 13.16 ?  147 VAL   B N    1 
ATOM   5948 C CA   . VAL   B 1 147 ? 31.706 -21.144 -6.855  1.00 12.96 ?  147 VAL   B CA   1 
ATOM   5949 C C    . VAL   B 1 147 ? 30.971 -21.010 -8.177  1.00 13.16 ?  147 VAL   B C    1 
ATOM   5950 O O    . VAL   B 1 147 ? 30.597 -22.014 -8.801  1.00 14.05 ?  147 VAL   B O    1 
ATOM   5951 C CB   . VAL   B 1 147 ? 33.159 -21.603 -7.063  1.00 12.85 ?  147 VAL   B CB   1 
ATOM   5952 C CG1  . VAL   B 1 147 ? 33.921 -20.586 -7.892  1.00 13.04 ?  147 VAL   B CG1  1 
ATOM   5953 C CG2  . VAL   B 1 147 ? 33.845 -21.805 -5.726  1.00 13.09 ?  147 VAL   B CG2  1 
ATOM   5954 H H    . VAL   B 1 147 ? 31.308 -22.887 -6.024  1.00 15.76 ?  147 VAL   B H    1 
ATOM   5955 H HA   . VAL   B 1 147 ? 31.725 -20.276 -6.426  1.00 15.53 ?  147 VAL   B HA   1 
ATOM   5956 H HB   . VAL   B 1 147 ? 33.166 -22.449 -7.543  1.00 15.40 ?  147 VAL   B HB   1 
ATOM   5957 H HG11 . VAL   B 1 147 ? 34.863 -20.814 -7.884  1.00 15.62 ?  147 VAL   B HG11 1 
ATOM   5958 H HG12 . VAL   B 1 147 ? 33.586 -20.602 -8.803  1.00 15.62 ?  147 VAL   B HG12 1 
ATOM   5959 H HG13 . VAL   B 1 147 ? 33.790 -19.706 -7.506  1.00 15.62 ?  147 VAL   B HG13 1 
ATOM   5960 H HG21 . VAL   B 1 147 ? 34.782 -22.003 -5.878  1.00 15.69 ?  147 VAL   B HG21 1 
ATOM   5961 H HG22 . VAL   B 1 147 ? 33.759 -20.992 -5.204  1.00 15.69 ?  147 VAL   B HG22 1 
ATOM   5962 H HG23 . VAL   B 1 147 ? 33.422 -22.544 -5.263  1.00 15.69 ?  147 VAL   B HG23 1 
ATOM   5963 N N    . ARG   B 1 148 ? 30.763 -19.761 -8.601  1.00 13.39 ?  148 ARG   B N    1 
ATOM   5964 C CA   . ARG   B 1 148 ? 30.138 -19.441 -9.875  1.00 13.51 ?  148 ARG   B CA   1 
ATOM   5965 C C    . ARG   B 1 148 ? 31.096 -18.768 -10.848 1.00 13.62 ?  148 ARG   B C    1 
ATOM   5966 O O    . ARG   B 1 148 ? 30.814 -18.752 -12.050 1.00 15.13 ?  148 ARG   B O    1 
ATOM   5967 C CB   . ARG   B 1 148 ? 28.902 -18.553 -9.656  1.00 13.67 ?  148 ARG   B CB   1 
ATOM   5968 C CG   . ARG   B 1 148 ? 27.830 -19.260 -8.843  1.00 14.63 ?  148 ARG   B CG   1 
ATOM   5969 C CD   . ARG   B 1 148 ? 26.624 -18.372 -8.539  1.00 15.73 ?  148 ARG   B CD   1 
ATOM   5970 N NE   . ARG   B 1 148 ? 27.001 -17.172 -7.801  1.00 15.38 ?  148 ARG   B NE   1 
ATOM   5971 C CZ   . ARG   B 1 148 ? 27.299 -17.143 -6.509  1.00 14.65 ?  148 ARG   B CZ   1 
ATOM   5972 N NH1  . ARG   B 1 148 ? 27.236 -18.234 -5.756  1.00 14.85 ?  148 ARG   B NH1  1 
ATOM   5973 N NH2  . ARG   B 1 148 ? 27.700 -15.997 -5.964  1.00 14.61 ?  148 ARG   B NH2  1 
ATOM   5974 H H    . ARG   B 1 148 ? 30.988 -19.061 -8.147  1.00 16.04 ?  148 ARG   B H    1 
ATOM   5975 H HA   . ARG   B 1 148 ? 29.840 -20.266 -10.285 1.00 16.19 ?  148 ARG   B HA   1 
ATOM   5976 H HB2  . ARG   B 1 148 ? 29.167 -17.754 -9.176  1.00 16.38 ?  148 ARG   B HB2  1 
ATOM   5977 H HB3  . ARG   B 1 148 ? 28.526 -18.319 -10.518 1.00 16.38 ?  148 ARG   B HB3  1 
ATOM   5978 H HG2  . ARG   B 1 148 ? 27.513 -20.032 -9.345  1.00 17.53 ?  148 ARG   B HG2  1 
ATOM   5979 H HG3  . ARG   B 1 148 ? 28.209 -19.551 -8.000  1.00 17.53 ?  148 ARG   B HG3  1 
ATOM   5980 H HD2  . ARG   B 1 148 ? 26.216 -18.096 -9.374  1.00 18.85 ?  148 ARG   B HD2  1 
ATOM   5981 H HD3  . ARG   B 1 148 ? 25.990 -18.870 -8.003  1.00 18.85 ?  148 ARG   B HD3  1 
ATOM   5982 H HE   . ARG   B 1 148 ? 27.055 -16.435 -8.237  1.00 18.44 ?  148 ARG   B HE   1 
ATOM   5983 H HH11 . ARG   B 1 148 ? 26.978 -18.982 -6.094  1.00 17.80 ?  148 ARG   B HH11 1 
ATOM   5984 H HH12 . ARG   B 1 148 ? 27.426 -18.191 -4.916  1.00 17.80 ?  148 ARG   B HH12 1 
ATOM   5985 H HH21 . ARG   B 1 148 ? 27.757 -15.290 -6.445  1.00 17.51 ?  148 ARG   B HH21 1 
ATOM   5986 H HH22 . ARG   B 1 148 ? 27.897 -15.965 -5.126  1.00 17.51 ?  148 ARG   B HH22 1 
ATOM   5987 N N    . THR   B 1 149 ? 32.201 -18.210 -10.359 1.00 13.33 ?  149 THR   B N    1 
ATOM   5988 C CA   . THR   B 1 149 ? 33.243 -17.649 -11.206 1.00 13.12 ?  149 THR   B CA   1 
ATOM   5989 C C    . THR   B 1 149 ? 34.127 -18.788 -11.720 1.00 12.77 ?  149 THR   B C    1 
ATOM   5990 O O    . THR   B 1 149 ? 33.929 -19.957 -11.382 1.00 13.33 ?  149 THR   B O    1 
ATOM   5991 C CB   . THR   B 1 149 ? 34.015 -16.596 -10.422 1.00 13.38 ?  149 THR   B CB   1 
ATOM   5992 O OG1  . THR   B 1 149 ? 34.476 -17.202 -9.213  1.00 13.28 ?  149 THR   B OG1  1 
ATOM   5993 C CG2  . THR   B 1 149 ? 33.123 -15.387 -10.118 1.00 14.30 ?  149 THR   B CG2  1 
ATOM   5994 H H    . THR   B 1 149 ? 32.362 -18.135 -9.517  1.00 15.98 ?  149 THR   B H    1 
ATOM   5995 H HA   . THR   B 1 149 ? 32.828 -17.214 -11.969 1.00 15.72 ?  149 THR   B HA   1 
ATOM   5996 H HB   . THR   B 1 149 ? 34.773 -16.303 -10.942 1.00 16.04 ?  149 THR   B HB   1 
ATOM   5997 H HG1  . THR   B 1 149 ? 34.897 -16.628 -8.751  1.00 15.91 ?  149 THR   B HG1  1 
ATOM   5998 H HG21 . THR   B 1 149 ? 33.629 -14.717 -9.631  1.00 17.14 ?  149 THR   B HG21 1 
ATOM   5999 H HG22 . THR   B 1 149 ? 32.800 -14.996 -10.946 1.00 17.14 ?  149 THR   B HG22 1 
ATOM   6000 H HG23 . THR   B 1 149 ? 32.361 -15.658 -9.581  1.00 17.14 ?  149 THR   B HG23 1 
ATOM   6001 N N    . ASN   B 1 150 ? 35.092 -18.467 -12.570 1.00 13.10 ?  150 ASN   B N    1 
ATOM   6002 C CA   . ASN   B 1 150 ? 35.857 -19.490 -13.272 1.00 13.35 ?  150 ASN   B CA   1 
ATOM   6003 C C    . ASN   B 1 150 ? 37.021 -19.947 -12.404 1.00 13.04 ?  150 ASN   B C    1 
ATOM   6004 O O    . ASN   B 1 150 ? 37.954 -19.180 -12.150 1.00 13.72 ?  150 ASN   B O    1 
ATOM   6005 C CB   . ASN   B 1 150 ? 36.324 -18.957 -14.618 1.00 15.59 ?  150 ASN   B CB   1 
ATOM   6006 C CG   . ASN   B 1 150 ? 35.175 -18.746 -15.566 1.00 18.37 ?  150 ASN   B CG   1 
ATOM   6007 O OD1  . ASN   B 1 150 ? 34.281 -19.580 -15.651 1.00 19.36 ?  150 ASN   B OD1  1 
ATOM   6008 N ND2  . ASN   B 1 150 ? 35.169 -17.620 -16.256 1.00 20.29 ?  150 ASN   B ND2  1 
ATOM   6009 H H    . ASN   B 1 150 ? 35.331 -17.659 -12.749 1.00 15.69 ?  150 ASN   B H    1 
ATOM   6010 H HA   . ASN   B 1 150 ? 35.277 -20.256 -13.435 1.00 16.00 ?  150 ASN   B HA   1 
ATOM   6011 H HB2  . ASN   B 1 150 ? 36.764 -18.103 -14.483 1.00 18.68 ?  150 ASN   B HB2  1 
ATOM   6012 H HB3  . ASN   B 1 150 ? 36.934 -19.592 -15.017 1.00 18.68 ?  150 ASN   B HB3  1 
ATOM   6013 H HD21 . ASN   B 1 150 ? 34.530 -17.453 -16.813 1.00 24.32 ?  150 ASN   B HD21 1 
ATOM   6014 H HD22 . ASN   B 1 150 ? 35.808 -17.049 -16.162 1.00 24.32 ?  150 ASN   B HD22 1 
ATOM   6015 N N    . VAL   B 1 151 ? 36.971 -21.193 -11.946 1.00 12.65 ?  151 VAL   B N    1 
ATOM   6016 C CA   . VAL   B 1 151 ? 37.987 -21.725 -11.051 1.00 12.68 ?  151 VAL   B CA   1 
ATOM   6017 C C    . VAL   B 1 151 ? 38.692 -22.895 -11.723 1.00 12.59 ?  151 VAL   B C    1 
ATOM   6018 O O    . VAL   B 1 151 ? 38.048 -23.832 -12.222 1.00 13.65 ?  151 VAL   B O    1 
ATOM   6019 C CB   . VAL   B 1 151 ? 37.424 -22.060 -9.655  1.00 13.90 ?  151 VAL   B CB   1 
ATOM   6020 C CG1  . VAL   B 1 151 ? 36.261 -23.052 -9.730  1.00 14.88 ?  151 VAL   B CG1  1 
ATOM   6021 C CG2  . VAL   B 1 151 ? 38.539 -22.556 -8.740  1.00 14.32 ?  151 VAL   B CG2  1 
ATOM   6022 H H    . VAL   B 1 151 ? 36.344 -21.753 -12.140 1.00 15.15 ?  151 VAL   B H    1 
ATOM   6023 H HA   . VAL   B 1 151 ? 38.653 -21.030 -10.918 1.00 15.19 ?  151 VAL   B HA   1 
ATOM   6024 H HB   . VAL   B 1 151 ? 37.078 -21.242 -9.262  1.00 16.66 ?  151 VAL   B HB   1 
ATOM   6025 H HG11 . VAL   B 1 151 ? 35.944 -23.240 -8.832  1.00 17.84 ?  151 VAL   B HG11 1 
ATOM   6026 H HG12 . VAL   B 1 151 ? 35.545 -22.665 -10.258 1.00 17.84 ?  151 VAL   B HG12 1 
ATOM   6027 H HG13 . VAL   B 1 151 ? 36.570 -23.874 -10.146 1.00 17.84 ?  151 VAL   B HG13 1 
ATOM   6028 H HG21 . VAL   B 1 151 ? 38.193 -22.628 -7.835  1.00 17.16 ?  151 VAL   B HG21 1 
ATOM   6029 H HG22 . VAL   B 1 151 ? 38.837 -23.427 -9.047  1.00 17.16 ?  151 VAL   B HG22 1 
ATOM   6030 H HG23 . VAL   B 1 151 ? 39.273 -21.925 -8.763  1.00 17.16 ?  151 VAL   B HG23 1 
ATOM   6031 N N    . TYR   B 1 152 ? 40.022 -22.807 -11.746 1.00 11.95 ?  152 TYR   B N    1 
ATOM   6032 C CA   . TYR   B 1 152 ? 40.924 -23.790 -12.328 1.00 12.44 ?  152 TYR   B CA   1 
ATOM   6033 C C    . TYR   B 1 152 ? 41.646 -24.471 -11.171 1.00 11.65 ?  152 TYR   B C    1 
ATOM   6034 O O    . TYR   B 1 152 ? 42.503 -23.860 -10.524 1.00 12.46 ?  152 TYR   B O    1 
ATOM   6035 C CB   . TYR   B 1 152 ? 41.896 -23.089 -13.281 1.00 13.27 ?  152 TYR   B CB   1 
ATOM   6036 C CG   . TYR   B 1 152 ? 41.218 -22.625 -14.547 1.00 14.00 ?  152 TYR   B CG   1 
ATOM   6037 C CD1  . TYR   B 1 152 ? 40.561 -21.399 -14.609 1.00 14.49 ?  152 TYR   B CD1  1 
ATOM   6038 C CD2  . TYR   B 1 152 ? 41.213 -23.426 -15.676 1.00 15.22 ?  152 TYR   B CD2  1 
ATOM   6039 C CE1  . TYR   B 1 152 ? 39.920 -20.989 -15.766 1.00 16.06 ?  152 TYR   B CE1  1 
ATOM   6040 C CE2  . TYR   B 1 152 ? 40.576 -23.028 -16.835 1.00 16.45 ?  152 TYR   B CE2  1 
ATOM   6041 C CZ   . TYR   B 1 152 ? 39.936 -21.803 -16.879 1.00 16.58 ?  152 TYR   B CZ   1 
ATOM   6042 O OH   . TYR   B 1 152 ? 39.306 -21.413 -18.038 1.00 19.08 ?  152 TYR   B OH   1 
ATOM   6043 H H    . TYR   B 1 152 ? 40.453 -22.136 -11.405 1.00 14.32 ?  152 TYR   B H    1 
ATOM   6044 H HA   . TYR   B 1 152 ? 40.415 -24.453 -12.818 1.00 14.90 ?  152 TYR   B HA   1 
ATOM   6045 H HB2  . TYR   B 1 152 ? 42.270 -22.313 -12.834 1.00 15.90 ?  152 TYR   B HB2  1 
ATOM   6046 H HB3  . TYR   B 1 152 ? 42.603 -23.707 -13.521 1.00 15.90 ?  152 TYR   B HB3  1 
ATOM   6047 H HD1  . TYR   B 1 152 ? 40.543 -20.848 -13.858 1.00 17.36 ?  152 TYR   B HD1  1 
ATOM   6048 H HD2  . TYR   B 1 152 ? 41.640 -24.254 -15.649 1.00 18.24 ?  152 TYR   B HD2  1 
ATOM   6049 H HE1  . TYR   B 1 152 ? 39.486 -20.167 -15.798 1.00 19.24 ?  152 TYR   B HE1  1 
ATOM   6050 H HE2  . TYR   B 1 152 ? 40.589 -23.580 -17.584 1.00 19.72 ?  152 TYR   B HE2  1 
ATOM   6051 H HH   . TYR   B 1 152 ? 39.401 -22.006 -18.626 1.00 22.88 ?  152 TYR   B HH   1 
ATOM   6052 N N    . LEU   B 1 153 ? 41.274 -25.724 -10.898 1.00 11.95 ?  153 LEU   B N    1 
ATOM   6053 C CA   . LEU   B 1 153 ? 41.787 -26.477 -9.762  1.00 11.70 ?  153 LEU   B CA   1 
ATOM   6054 C C    . LEU   B 1 153 ? 43.019 -27.276 -10.162 1.00 12.02 ?  153 LEU   B C    1 
ATOM   6055 O O    . LEU   B 1 153 ? 43.002 -28.001 -11.159 1.00 13.39 ?  153 LEU   B O    1 
ATOM   6056 C CB   . LEU   B 1 153 ? 40.712 -27.438 -9.244  1.00 12.39 ?  153 LEU   B CB   1 
ATOM   6057 C CG   . LEU   B 1 153 ? 39.459 -26.782 -8.660  1.00 13.15 ?  153 LEU   B CG   1 
ATOM   6058 C CD1  . LEU   B 1 153 ? 38.359 -27.818 -8.490  1.00 14.03 ?  153 LEU   B CD1  1 
ATOM   6059 C CD2  . LEU   B 1 153 ? 39.770 -26.124 -7.324  1.00 13.49 ?  153 LEU   B CD2  1 
ATOM   6060 H H    . LEU   B 1 153 ? 40.705 -26.171 -11.374 1.00 14.32 ?  153 LEU   B H    1 
ATOM   6061 H HA   . LEU   B 1 153 ? 42.019 -25.865 -9.051  1.00 14.02 ?  153 LEU   B HA   1 
ATOM   6062 H HB2  . LEU   B 1 153 ? 40.425 -28.005 -9.973  1.00 14.84 ?  153 LEU   B HB2  1 
ATOM   6063 H HB3  . LEU   B 1 153 ? 41.102 -27.985 -8.542  1.00 14.84 ?  153 LEU   B HB3  1 
ATOM   6064 H HG   . LEU   B 1 153 ? 39.140 -26.092 -9.266  1.00 15.75 ?  153 LEU   B HG   1 
ATOM   6065 H HD11 . LEU   B 1 153 ? 37.556 -27.370 -8.173  1.00 16.82 ?  153 LEU   B HD11 1 
ATOM   6066 H HD12 . LEU   B 1 153 ? 38.192 -28.235 -9.343  1.00 16.82 ?  153 LEU   B HD12 1 
ATOM   6067 H HD13 . LEU   B 1 153 ? 38.649 -28.474 -7.841  1.00 16.82 ?  153 LEU   B HD13 1 
ATOM   6068 H HD21 . LEU   B 1 153 ? 38.959 -25.754 -6.950  1.00 16.17 ?  153 LEU   B HD21 1 
ATOM   6069 H HD22 . LEU   B 1 153 ? 40.142 -26.790 -6.723  1.00 16.17 ?  153 LEU   B HD22 1 
ATOM   6070 H HD23 . LEU   B 1 153 ? 40.422 -25.414 -7.465  1.00 16.17 ?  153 LEU   B HD23 1 
ATOM   6071 N N    . ALA   B 1 154 ? 44.071 -27.174 -9.356  1.00 12.14 ?  154 ALA   B N    1 
ATOM   6072 C CA   . ALA   B 1 154 ? 45.299 -27.933 -9.540  1.00 13.21 ?  154 ALA   B CA   1 
ATOM   6073 C C    . ALA   B 1 154 ? 45.367 -29.012 -8.466  1.00 13.98 ?  154 ALA   B C    1 
ATOM   6074 O O    . ALA   B 1 154 ? 45.299 -28.713 -7.265  1.00 15.34 ?  154 ALA   B O    1 
ATOM   6075 C CB   . ALA   B 1 154 ? 46.519 -27.014 -9.477  1.00 14.26 ?  154 ALA   B CB   1 
ATOM   6076 H H    . ALA   B 1 154 ? 44.093 -26.643 -8.674  1.00 14.55 ?  154 ALA   B H    1 
ATOM   6077 H HA   . ALA   B 1 154 ? 45.285 -28.360 -10.408 1.00 15.83 ?  154 ALA   B HA   1 
ATOM   6078 H HB1  . ALA   B 1 154 ? 47.323 -27.544 -9.601  1.00 17.09 ?  154 ALA   B HB1  1 
ATOM   6079 H HB2  . ALA   B 1 154 ? 46.454 -26.346 -10.179 1.00 17.09 ?  154 ALA   B HB2  1 
ATOM   6080 H HB3  . ALA   B 1 154 ? 46.546 -26.576 -8.609  1.00 17.09 ?  154 ALA   B HB3  1 
ATOM   6081 N N    . VAL   B 1 155 ? 45.483 -30.261 -8.897  1.00 13.32 ?  155 VAL   B N    1 
ATOM   6082 C CA   . VAL   B 1 155 ? 45.591 -31.406 -8.002  1.00 13.23 ?  155 VAL   B CA   1 
ATOM   6083 C C    . VAL   B 1 155 ? 46.926 -32.083 -8.285  1.00 13.43 ?  155 VAL   B C    1 
ATOM   6084 O O    . VAL   B 1 155 ? 47.156 -32.573 -9.398  1.00 15.43 ?  155 VAL   B O    1 
ATOM   6085 C CB   . VAL   B 1 155 ? 44.424 -32.392 -8.188  1.00 14.94 ?  155 VAL   B CB   1 
ATOM   6086 C CG1  . VAL   B 1 155 ? 44.609 -33.602 -7.291  1.00 14.93 ?  155 VAL   B CG1  1 
ATOM   6087 C CG2  . VAL   B 1 155 ? 43.093 -31.695 -7.898  1.00 15.83 ?  155 VAL   B CG2  1 
ATOM   6088 H H    . VAL   B 1 155 ? 45.509 -30.476 -9.731  1.00 15.96 ?  155 VAL   B H    1 
ATOM   6089 H HA   . VAL   B 1 155 ? 45.585 -31.102 -7.082  1.00 15.85 ?  155 VAL   B HA   1 
ATOM   6090 H HB   . VAL   B 1 155 ? 44.404 -32.695 -9.110  1.00 17.90 ?  155 VAL   B HB   1 
ATOM   6091 H HG11 . VAL   B 1 155 ? 43.778 -34.098 -7.249  1.00 17.90 ?  155 VAL   B HG11 1 
ATOM   6092 H HG12 . VAL   B 1 155 ? 45.310 -34.165 -7.659  1.00 17.90 ?  155 VAL   B HG12 1 
ATOM   6093 H HG13 . VAL   B 1 155 ? 44.859 -33.302 -6.402  1.00 17.90 ?  155 VAL   B HG13 1 
ATOM   6094 H HG21 . VAL   B 1 155 ? 42.371 -32.338 -7.987  1.00 18.97 ?  155 VAL   B HG21 1 
ATOM   6095 H HG22 . VAL   B 1 155 ? 43.110 -31.341 -6.994  1.00 18.97 ?  155 VAL   B HG22 1 
ATOM   6096 H HG23 . VAL   B 1 155 ? 42.966 -30.970 -8.532  1.00 18.97 ?  155 VAL   B HG23 1 
ATOM   6097 N N    . PHE   B 1 156 ? 47.796 -32.120 -7.275  1.00 14.16 ?  156 PHE   B N    1 
ATOM   6098 C CA   . PHE   B 1 156 ? 49.174 -32.579 -7.477  1.00 15.14 ?  156 PHE   B CA   1 
ATOM   6099 C C    . PHE   B 1 156 ? 49.265 -34.077 -7.762  1.00 16.37 ?  156 PHE   B C    1 
ATOM   6100 O O    . PHE   B 1 156 ? 49.980 -34.505 -8.679  1.00 18.20 ?  156 PHE   B O    1 
ATOM   6101 C CB   . PHE   B 1 156 ? 50.002 -32.221 -6.247  1.00 15.38 ?  156 PHE   B CB   1 
ATOM   6102 C CG   . PHE   B 1 156 ? 51.426 -32.682 -6.311  1.00 16.06 ?  156 PHE   B CG   1 
ATOM   6103 C CD1  . PHE   B 1 156 ? 52.305 -32.147 -7.234  1.00 17.30 ?  156 PHE   B CD1  1 
ATOM   6104 C CD2  . PHE   B 1 156 ? 51.891 -33.634 -5.428  1.00 16.35 ?  156 PHE   B CD2  1 
ATOM   6105 C CE1  . PHE   B 1 156 ? 53.627 -32.560 -7.280  1.00 18.01 ?  156 PHE   B CE1  1 
ATOM   6106 C CE2  . PHE   B 1 156 ? 53.207 -34.046 -5.469  1.00 17.38 ?  156 PHE   B CE2  1 
ATOM   6107 C CZ   . PHE   B 1 156 ? 54.069 -33.509 -6.398  1.00 17.75 ?  156 PHE   B CZ   1 
ATOM   6108 H H    . PHE   B 1 156 ? 47.614 -31.884 -6.467  1.00 16.97 ?  156 PHE   B H    1 
ATOM   6109 H HA   . PHE   B 1 156 ? 49.545 -32.110 -8.236  1.00 18.14 ?  156 PHE   B HA   1 
ATOM   6110 H HB2  . PHE   B 1 156 ? 50.009 -31.257 -6.149  1.00 18.44 ?  156 PHE   B HB2  1 
ATOM   6111 H HB3  . PHE   B 1 156 ? 49.596 -32.628 -5.467  1.00 18.44 ?  156 PHE   B HB3  1 
ATOM   6112 H HD1  . PHE   B 1 156 ? 52.007 -31.496 -7.832  1.00 20.73 ?  156 PHE   B HD1  1 
ATOM   6113 H HD2  . PHE   B 1 156 ? 51.310 -34.003 -4.800  1.00 19.59 ?  156 PHE   B HD2  1 
ATOM   6114 H HE1  . PHE   B 1 156 ? 54.209 -32.193 -7.908  1.00 21.59 ?  156 PHE   B HE1  1 
ATOM   6115 H HE2  . PHE   B 1 156 ? 53.506 -34.699 -4.874  1.00 20.83 ?  156 PHE   B HE2  1 
ATOM   6116 H HZ   . PHE   B 1 156 ? 54.954 -33.795 -6.427  1.00 21.28 ?  156 PHE   B HZ   1 
ATOM   6117 N N    . ASP   B 1 157 ? 48.602 -34.895 -6.957  1.00 16.66 ?  157 ASP   B N    1 
ATOM   6118 C CA   . ASP   B 1 157 ? 48.745 -36.342 -7.059  1.00 17.77 ?  157 ASP   B CA   1 
ATOM   6119 C C    . ASP   B 1 157 ? 47.822 -36.886 -8.144  1.00 18.09 ?  157 ASP   B C    1 
ATOM   6120 O O    . ASP   B 1 157 ? 46.597 -36.771 -8.033  1.00 17.52 ?  157 ASP   B O    1 
ATOM   6121 C CB   . ASP   B 1 157 ? 48.388 -36.960 -5.714  1.00 19.28 ?  157 ASP   B CB   1 
ATOM   6122 C CG   . ASP   B 1 157 ? 48.533 -38.467 -5.700  1.00 21.35 ?  157 ASP   B CG   1 
ATOM   6123 O OD1  . ASP   B 1 157 ? 48.861 -39.072 -6.749  1.00 21.87 ?  157 ASP   B OD1  1 
ATOM   6124 O OD2  . ASP   B 1 157 ? 48.326 -39.050 -4.618  1.00 23.35 -1 157 ASP   B OD2  1 
ATOM   6125 H H    . ASP   B 1 157 ? 48.062 -34.641 -6.342  1.00 19.97 ?  157 ASP   B H    1 
ATOM   6126 H HA   . ASP   B 1 157 ? 49.660 -36.576 -7.283  1.00 21.30 ?  157 ASP   B HA   1 
ATOM   6127 H HB2  . ASP   B 1 157 ? 48.964 -36.584 -5.036  1.00 23.11 ?  157 ASP   B HB2  1 
ATOM   6128 H HB3  . ASP   B 1 157 ? 47.459 -36.754 -5.513  1.00 23.11 ?  157 ASP   B HB3  1 
ATOM   6129 N N    . LYS   B 1 158 ? 48.411 -37.505 -9.176  1.00 19.28 ?  158 LYS   B N    1 
ATOM   6130 C CA   . LYS   B 1 158 ? 47.631 -38.118 -10.255 1.00 20.51 ?  158 LYS   B CA   1 
ATOM   6131 C C    . LYS   B 1 158 ? 46.572 -39.083 -9.724  1.00 20.29 ?  158 LYS   B C    1 
ATOM   6132 O O    . LYS   B 1 158 ? 45.467 -39.170 -10.275 1.00 20.54 ?  158 LYS   B O    1 
ATOM   6133 C CB   . LYS   B 1 158 ? 48.578 -38.838 -11.224 1.00 22.51 ?  158 LYS   B CB   1 
ATOM   6134 C CG   . LYS   B 1 158 ? 47.905 -39.744 -12.248 1.00 25.04 ?  158 LYS   B CG   1 
ATOM   6135 C CD   . LYS   B 1 158 ? 47.036 -38.970 -13.219 1.00 27.78 ?  158 LYS   B CD   1 
ATOM   6136 C CE   . LYS   B 1 158 ? 46.430 -39.895 -14.264 1.00 29.80 ?  158 LYS   B CE   1 
ATOM   6137 N NZ   . LYS   B 1 158 ? 45.384 -39.214 -15.078 1.00 30.17 ?  158 LYS   B NZ   1 
ATOM   6138 H H    . LYS   B 1 158 ? 49.262 -37.584 -9.277  1.00 23.12 ?  158 LYS   B H    1 
ATOM   6139 H HA   . LYS   B 1 158 ? 47.177 -37.421 -10.756 1.00 24.59 ?  158 LYS   B HA   1 
ATOM   6140 H HB2  . LYS   B 1 158 ? 49.081 -38.171 -11.722 1.00 26.99 ?  158 LYS   B HB2  1 
ATOM   6141 H HB3  . LYS   B 1 158 ? 49.190 -39.386 -10.711 1.00 26.99 ?  158 LYS   B HB3  1 
ATOM   6142 H HG2  . LYS   B 1 158 ? 48.591 -40.198 -12.764 1.00 30.03 ?  158 LYS   B HG2  1 
ATOM   6143 H HG3  . LYS   B 1 158 ? 47.351 -40.403 -11.798 1.00 30.03 ?  158 LYS   B HG3  1 
ATOM   6144 H HD2  . LYS   B 1 158 ? 46.313 -38.541 -12.735 1.00 33.32 ?  158 LYS   B HD2  1 
ATOM   6145 H HD3  . LYS   B 1 158 ? 47.576 -38.307 -13.677 1.00 33.32 ?  158 LYS   B HD3  1 
ATOM   6146 H HE2  . LYS   B 1 158 ? 47.127 -40.198 -14.864 1.00 35.74 ?  158 LYS   B HE2  1 
ATOM   6147 H HE3  . LYS   B 1 158 ? 46.020 -40.654 -13.820 1.00 35.74 ?  158 LYS   B HE3  1 
ATOM   6148 H HZ1  . LYS   B 1 158 ? 45.048 -39.778 -15.678 1.00 36.18 ?  158 LYS   B HZ1  1 
ATOM   6149 H HZ2  . LYS   B 1 158 ? 44.726 -38.927 -14.551 1.00 36.18 ?  158 LYS   B HZ2  1 
ATOM   6150 H HZ3  . LYS   B 1 158 ? 45.737 -38.516 -15.503 1.00 36.18 ?  158 LYS   B HZ3  1 
ATOM   6151 N N    . ASN   B 1 159 ? 46.897 -39.847 -8.679  1.00 20.48 ?  159 ASN   B N    1 
ATOM   6152 C CA   . ASN   B 1 159 ? 45.939 -40.824 -8.166  1.00 21.10 ?  159 ASN   B CA   1 
ATOM   6153 C C    . ASN   B 1 159 ? 44.747 -40.149 -7.484  1.00 19.93 ?  159 ASN   B C    1 
ATOM   6154 O O    . ASN   B 1 159 ? 43.612 -40.636 -7.579  1.00 20.60 ?  159 ASN   B O    1 
ATOM   6155 C CB   . ASN   B 1 159 ? 46.646 -41.804 -7.234  1.00 22.70 ?  159 ASN   B CB   1 
ATOM   6156 C CG   . ASN   B 1 159 ? 47.677 -42.645 -7.956  1.00 24.54 ?  159 ASN   B CG   1 
ATOM   6157 O OD1  . ASN   B 1 159 ? 47.429 -43.139 -9.064  1.00 25.35 ?  159 ASN   B OD1  1 
ATOM   6158 N ND2  . ASN   B 1 159 ? 48.845 -42.811 -7.336  1.00 25.16 ?  159 ASN   B ND2  1 
ATOM   6159 H H    . ASN   B 1 159 ? 47.646 -39.810 -8.264  1.00 24.55 ?  159 ASN   B H    1 
ATOM   6160 H HA   . ASN   B 1 159 ? 45.596 -41.332 -8.919  1.00 25.30 ?  159 ASN   B HA   1 
ATOM   6161 H HB2  . ASN   B 1 159 ? 47.094 -41.310 -6.533  1.00 27.22 ?  159 ASN   B HB2  1 
ATOM   6162 H HB3  . ASN   B 1 159 ? 45.989 -42.407 -6.857  1.00 27.22 ?  159 ASN   B HB3  1 
ATOM   6163 H HD21 . ASN   B 1 159 ? 49.472 -43.276 -7.704  1.00 30.16 ?  159 ASN   B HD21 1 
ATOM   6164 H HD22 . ASN   B 1 159 ? 48.978 -42.461 -6.560  1.00 30.16 ?  159 ASN   B HD22 1 
ATOM   6165 N N    . LEU   B 1 160 ? 44.970 -39.023 -6.801  1.00 19.04 ?  160 LEU   B N    1 
ATOM   6166 C CA   . LEU   B 1 160 ? 43.839 -38.287 -6.250  1.00 18.01 ?  160 LEU   B CA   1 
ATOM   6167 C C    . LEU   B 1 160 ? 43.042 -37.617 -7.358  1.00 17.36 ?  160 LEU   B C    1 
ATOM   6168 O O    . LEU   B 1 160 ? 41.803 -37.614 -7.330  1.00 17.09 ?  160 LEU   B O    1 
ATOM   6169 C CB   . LEU   B 1 160 ? 44.307 -37.253 -5.228  1.00 17.44 ?  160 LEU   B CB   1 
ATOM   6170 C CG   . LEU   B 1 160 ? 43.183 -36.347 -4.706  1.00 17.15 ?  160 LEU   B CG   1 
ATOM   6171 C CD1  . LEU   B 1 160 ? 42.074 -37.171 -4.066  1.00 17.96 ?  160 LEU   B CD1  1 
ATOM   6172 C CD2  . LEU   B 1 160 ? 43.731 -35.321 -3.725  1.00 17.24 ?  160 LEU   B CD2  1 
ATOM   6173 H H    . LEU   B 1 160 ? 45.744 -38.675 -6.655  1.00 22.83 ?  160 LEU   B H    1 
ATOM   6174 H HA   . LEU   B 1 160 ? 43.253 -38.915 -5.802  1.00 21.59 ?  160 LEU   B HA   1 
ATOM   6175 H HB2  . LEU   B 1 160 ? 44.695 -37.724 -4.472  1.00 20.91 ?  160 LEU   B HB2  1 
ATOM   6176 H HB3  . LEU   B 1 160 ? 44.983 -36.692 -5.645  1.00 20.91 ?  160 LEU   B HB3  1 
ATOM   6177 H HG   . LEU   B 1 160 ? 42.804 -35.863 -5.454  1.00 20.56 ?  160 LEU   B HG   1 
ATOM   6178 H HD11 . LEU   B 1 160 ? 41.450 -36.570 -3.640  1.00 21.53 ?  160 LEU   B HD11 1 
ATOM   6179 H HD12 . LEU   B 1 160 ? 41.624 -37.688 -4.753  1.00 21.53 ?  160 LEU   B HD12 1 
ATOM   6180 H HD13 . LEU   B 1 160 ? 42.465 -37.768 -3.407  1.00 21.53 ?  160 LEU   B HD13 1 
ATOM   6181 H HD21 . LEU   B 1 160 ? 43.002 -34.754 -3.430  1.00 20.66 ?  160 LEU   B HD21 1 
ATOM   6182 H HD22 . LEU   B 1 160 ? 44.123 -35.782 -2.970  1.00 20.66 ?  160 LEU   B HD22 1 
ATOM   6183 H HD23 . LEU   B 1 160 ? 44.406 -34.784 -4.174  1.00 20.66 ?  160 LEU   B HD23 1 
ATOM   6184 N N    . TYR   B 1 161 ? 43.739 -37.045 -8.344  1.00 17.17 ?  161 TYR   B N    1 
ATOM   6185 C CA   . TYR   B 1 161 ? 43.069 -36.475 -9.509  1.00 16.98 ?  161 TYR   B CA   1 
ATOM   6186 C C    . TYR   B 1 161 ? 42.121 -37.494 -10.130 1.00 16.79 ?  161 TYR   B C    1 
ATOM   6187 O O    . TYR   B 1 161 ? 40.950 -37.198 -10.396 1.00 16.85 ?  161 TYR   B O    1 
ATOM   6188 C CB   . TYR   B 1 161 ? 44.113 -36.001 -10.531 1.00 17.60 ?  161 TYR   B CB   1 
ATOM   6189 C CG   . TYR   B 1 161 ? 43.533 -35.533 -11.850 1.00 18.12 ?  161 TYR   B CG   1 
ATOM   6190 C CD1  . TYR   B 1 161 ? 43.137 -34.211 -12.024 1.00 18.35 ?  161 TYR   B CD1  1 
ATOM   6191 C CD2  . TYR   B 1 161 ? 43.363 -36.414 -12.915 1.00 18.53 ?  161 TYR   B CD2  1 
ATOM   6192 C CE1  . TYR   B 1 161 ? 42.604 -33.779 -13.215 1.00 19.19 ?  161 TYR   B CE1  1 
ATOM   6193 C CE2  . TYR   B 1 161 ? 42.828 -35.989 -14.112 1.00 19.78 ?  161 TYR   B CE2  1 
ATOM   6194 C CZ   . TYR   B 1 161 ? 42.451 -34.670 -14.256 1.00 19.85 ?  161 TYR   B CZ   1 
ATOM   6195 O OH   . TYR   B 1 161 ? 41.910 -34.235 -15.442 1.00 21.87 ?  161 TYR   B OH   1 
ATOM   6196 H H    . TYR   B 1 161 ? 44.594 -36.984 -8.366  1.00 20.58 ?  161 TYR   B H    1 
ATOM   6197 H HA   . TYR   B 1 161 ? 42.546 -35.708 -9.234  1.00 20.35 ?  161 TYR   B HA   1 
ATOM   6198 H HB2  . TYR   B 1 161 ? 44.607 -35.259 -10.150 1.00 21.09 ?  161 TYR   B HB2  1 
ATOM   6199 H HB3  . TYR   B 1 161 ? 44.719 -36.734 -10.723 1.00 21.09 ?  161 TYR   B HB3  1 
ATOM   6200 H HD1  . TYR   B 1 161 ? 43.243 -33.603 -11.327 1.00 21.99 ?  161 TYR   B HD1  1 
ATOM   6201 H HD2  . TYR   B 1 161 ? 43.613 -37.303 -12.823 1.00 22.21 ?  161 TYR   B HD2  1 
ATOM   6202 H HE1  . TYR   B 1 161 ? 42.349 -32.884 -13.314 1.00 23.00 ?  161 TYR   B HE1  1 
ATOM   6203 H HE2  . TYR   B 1 161 ? 42.716 -36.583 -14.818 1.00 23.71 ?  161 TYR   B HE2  1 
ATOM   6204 H HH   . TYR   B 1 161 ? 41.873 -34.871 -15.991 1.00 26.21 ?  161 TYR   B HH   1 
ATOM   6205 N N    . ASP   B 1 162 ? 42.617 -38.711 -10.355 1.00 17.46 ?  162 ASP   B N    1 
ATOM   6206 C CA   . ASP   B 1 162 ? 41.787 -39.748 -10.963 1.00 17.81 ?  162 ASP   B CA   1 
ATOM   6207 C C    . ASP   B 1 162 ? 40.582 -40.081 -10.089 1.00 17.11 ?  162 ASP   B C    1 
ATOM   6208 O O    . ASP   B 1 162 ? 39.478 -40.299 -10.602 1.00 17.48 ?  162 ASP   B O    1 
ATOM   6209 C CB   . ASP   B 1 162 ? 42.616 -41.011 -11.214 1.00 19.47 ?  162 ASP   B CB   1 
ATOM   6210 C CG   . ASP   B 1 162 ? 43.609 -40.857 -12.351 1.00 20.93 ?  162 ASP   B CG   1 
ATOM   6211 O OD1  . ASP   B 1 162 ? 43.475 -39.916 -13.156 1.00 21.18 ?  162 ASP   B OD1  1 
ATOM   6212 O OD2  . ASP   B 1 162 ? 44.512 -41.714 -12.457 1.00 22.58 -1 162 ASP   B OD2  1 
ATOM   6213 H H    . ASP   B 1 162 ? 43.420 -38.960 -10.169 1.00 20.93 ?  162 ASP   B H    1 
ATOM   6214 H HA   . ASP   B 1 162 ? 41.458 -39.430 -11.817 1.00 21.35 ?  162 ASP   B HA   1 
ATOM   6215 H HB2  . ASP   B 1 162 ? 43.121 -41.226 -10.417 1.00 23.34 ?  162 ASP   B HB2  1 
ATOM   6216 H HB3  . ASP   B 1 162 ? 42.020 -41.742 -11.441 1.00 23.34 ?  162 ASP   B HB3  1 
ATOM   6217 N N    . LYS   B 1 163 ? 40.776 -40.154 -8.771  1.00 16.73 ?  163 LYS   B N    1 
ATOM   6218 C CA   . LYS   B 1 163 ? 39.657 -40.435 -7.877  1.00 17.45 ?  163 LYS   B CA   1 
ATOM   6219 C C    . LYS   B 1 163 ? 38.610 -39.329 -7.937  1.00 16.37 ?  163 LYS   B C    1 
ATOM   6220 O O    . LYS   B 1 163 ? 37.399 -39.600 -7.932  1.00 17.37 ?  163 LYS   B O    1 
ATOM   6221 C CB   . LYS   B 1 163 ? 40.153 -40.619 -6.446  1.00 20.61 ?  163 LYS   B CB   1 
ATOM   6222 C CG   . LYS   B 1 163 ? 39.068 -41.116 -5.514  1.00 26.64 ?  163 LYS   B CG   1 
ATOM   6223 C CD   . LYS   B 1 163 ? 39.549 -41.274 -4.084  1.00 32.26 ?  163 LYS   B CD   1 
ATOM   6224 C CE   . LYS   B 1 163 ? 38.468 -41.928 -3.233  1.00 36.75 ?  163 LYS   B CE   1 
ATOM   6225 N NZ   . LYS   B 1 163 ? 38.609 -41.618 -1.785  1.00 39.02 ?  163 LYS   B NZ   1 
ATOM   6226 H H    . LYS   B 1 163 ? 41.537 -40.047 -8.380  1.00 20.05 ?  163 LYS   B H    1 
ATOM   6227 H HA   . LYS   B 1 163 ? 39.235 -41.258 -8.156  1.00 20.92 ?  163 LYS   B HA   1 
ATOM   6228 H HB2  . LYS   B 1 163 ? 40.875 -41.270 -6.442  1.00 24.71 ?  163 LYS   B HB2  1 
ATOM   6229 H HB3  . LYS   B 1 163 ? 40.474 -39.769 -6.107  1.00 24.71 ?  163 LYS   B HB3  1 
ATOM   6230 H HG2  . LYS   B 1 163 ? 38.332 -40.486 -5.514  1.00 31.94 ?  163 LYS   B HG2  1 
ATOM   6231 H HG3  . LYS   B 1 163 ? 38.759 -41.985 -5.824  1.00 31.94 ?  163 LYS   B HG3  1 
ATOM   6232 H HD2  . LYS   B 1 163 ? 40.337 -41.841 -4.068  1.00 38.68 ?  163 LYS   B HD2  1 
ATOM   6233 H HD3  . LYS   B 1 163 ? 39.749 -40.402 -3.713  1.00 38.68 ?  163 LYS   B HD3  1 
ATOM   6234 H HE2  . LYS   B 1 163 ? 37.597 -41.620 -3.529  1.00 44.08 ?  163 LYS   B HE2  1 
ATOM   6235 H HE3  . LYS   B 1 163 ? 38.527 -42.889 -3.339  1.00 44.08 ?  163 LYS   B HE3  1 
ATOM   6236 H HZ1  . LYS   B 1 163 ? 37.958 -42.016 -1.325  1.00 46.80 ?  163 LYS   B HZ1  1 
ATOM   6237 H HZ2  . LYS   B 1 163 ? 39.394 -41.910 -1.487  1.00 46.80 ?  163 LYS   B HZ2  1 
ATOM   6238 H HZ3  . LYS   B 1 163 ? 38.558 -40.739 -1.655  1.00 46.80 ?  163 LYS   B HZ3  1 
ATOM   6239 N N    . LEU   B 1 164 ? 39.063 -38.073 -8.000  1.00 15.34 ?  164 LEU   B N    1 
ATOM   6240 C CA   . LEU   B 1 164 ? 38.155 -36.933 -8.061  1.00 14.98 ?  164 LEU   B CA   1 
ATOM   6241 C C    . LEU   B 1 164 ? 37.371 -36.920 -9.369  1.00 15.16 ?  164 LEU   B C    1 
ATOM   6242 O O    . LEU   B 1 164 ? 36.150 -36.716 -9.371  1.00 16.46 ?  164 LEU   B O    1 
ATOM   6243 C CB   . LEU   B 1 164 ? 38.955 -35.635 -7.903  1.00 14.47 ?  164 LEU   B CB   1 
ATOM   6244 C CG   . LEU   B 1 164 ? 39.502 -35.367 -6.504  1.00 15.21 ?  164 LEU   B CG   1 
ATOM   6245 C CD1  . LEU   B 1 164 ? 40.588 -34.308 -6.555  1.00 15.28 ?  164 LEU   B CD1  1 
ATOM   6246 C CD2  . LEU   B 1 164 ? 38.393 -34.935 -5.562  1.00 17.02 ?  164 LEU   B CD2  1 
ATOM   6247 H H    . LEU   B 1 164 ? 39.899 -37.852 -8.013  1.00 18.38 ?  164 LEU   B H    1 
ATOM   6248 H HA   . LEU   B 1 164 ? 37.525 -36.986 -7.334  1.00 17.95 ?  164 LEU   B HA   1 
ATOM   6249 H HB2  . LEU   B 1 164 ? 39.717 -35.663 -8.508  1.00 17.34 ?  164 LEU   B HB2  1 
ATOM   6250 H HB3  . LEU   B 1 164 ? 38.387 -34.887 -8.138  1.00 17.34 ?  164 LEU   B HB3  1 
ATOM   6251 H HG   . LEU   B 1 164 ? 39.897 -36.180 -6.155  1.00 18.23 ?  164 LEU   B HG   1 
ATOM   6252 H HD11 . LEU   B 1 164 ? 40.919 -34.146 -5.654  1.00 18.31 ?  164 LEU   B HD11 1 
ATOM   6253 H HD12 . LEU   B 1 164 ? 41.318 -34.626 -7.116  1.00 18.31 ?  164 LEU   B HD12 1 
ATOM   6254 H HD13 . LEU   B 1 164 ? 40.223 -33.490 -6.923  1.00 18.31 ?  164 LEU   B HD13 1 
ATOM   6255 H HD21 . LEU   B 1 164 ? 38.776 -34.715 -4.699  1.00 20.40 ?  164 LEU   B HD21 1 
ATOM   6256 H HD22 . LEU   B 1 164 ? 37.947 -34.158 -5.934  1.00 20.40 ?  164 LEU   B HD22 1 
ATOM   6257 H HD23 . LEU   B 1 164 ? 37.760 -35.665 -5.467  1.00 20.40 ?  164 LEU   B HD23 1 
ATOM   6258 N N    . VAL   B 1 165 ? 38.063 -37.093 -10.496 1.00 16.78 ?  165 VAL   B N    1 
ATOM   6259 C CA   . VAL   B 1 165 ? 37.402 -37.026 -11.794 1.00 17.99 ?  165 VAL   B CA   1 
ATOM   6260 C C    . VAL   B 1 165 ? 36.484 -38.227 -11.981 1.00 19.86 ?  165 VAL   B C    1 
ATOM   6261 O O    . VAL   B 1 165 ? 35.322 -38.093 -12.386 1.00 21.02 ?  165 VAL   B O    1 
ATOM   6262 C CB   . VAL   B 1 165 ? 38.446 -36.937 -12.923 1.00 19.33 ?  165 VAL   B CB   1 
ATOM   6263 C CG1  . VAL   B 1 165 ? 37.780 -37.061 -14.272 1.00 20.41 ?  165 VAL   B CG1  1 
ATOM   6264 C CG2  . VAL   B 1 165 ? 39.223 -35.642 -12.826 1.00 19.02 ?  165 VAL   B CG2  1 
ATOM   6265 H H    . VAL   B 1 165 ? 38.911 -37.244 -10.534 1.00 20.11 ?  165 VAL   B H    1 
ATOM   6266 H HA   . VAL   B 1 165 ? 36.858 -36.226 -11.833 1.00 21.57 ?  165 VAL   B HA   1 
ATOM   6267 H HB   . VAL   B 1 165 ? 39.081 -37.665 -12.828 1.00 23.17 ?  165 VAL   B HB   1 
ATOM   6268 H HG11 . VAL   B 1 165 ? 38.389 -36.750 -14.956 1.00 24.47 ?  165 VAL   B HG11 1 
ATOM   6269 H HG12 . VAL   B 1 165 ? 37.564 -37.996 -14.427 1.00 24.47 ?  165 VAL   B HG12 1 
ATOM   6270 H HG13 . VAL   B 1 165 ? 36.972 -36.530 -14.275 1.00 24.47 ?  165 VAL   B HG13 1 
ATOM   6271 H HG21 . VAL   B 1 165 ? 39.858 -35.594 -13.560 1.00 22.81 ?  165 VAL   B HG21 1 
ATOM   6272 H HG22 . VAL   B 1 165 ? 38.602 -34.894 -12.883 1.00 22.81 ?  165 VAL   B HG22 1 
ATOM   6273 H HG23 . VAL   B 1 165 ? 39.695 -35.611 -11.979 1.00 22.81 ?  165 VAL   B HG23 1 
ATOM   6274 N N    . SER   B 1 166 ? 37.000 -39.425 -11.689 1.00 20.74 ?  166 SER   B N    1 
ATOM   6275 C CA   . SER   B 1 166 ? 36.250 -40.641 -11.975 1.00 22.04 ?  166 SER   B CA   1 
ATOM   6276 C C    . SER   B 1 166 ? 34.988 -40.732 -11.131 1.00 21.93 ?  166 SER   B C    1 
ATOM   6277 O O    . SER   B 1 166 ? 34.017 -41.357 -11.557 1.00 23.29 ?  166 SER   B O    1 
ATOM   6278 C CB   . SER   B 1 166 ? 37.125 -41.891 -11.795 1.00 23.32 ?  166 SER   B CB   1 
ATOM   6279 O OG   . SER   B 1 166 ? 37.465 -42.106 -10.437 1.00 23.58 ?  166 SER   B OG   1 
ATOM   6280 H H    . SER   B 1 166 ? 37.776 -39.556 -11.337 1.00 24.87 ?  166 SER   B H    1 
ATOM   6281 H HA   . SER   B 1 166 ? 35.979 -40.620 -12.907 1.00 26.42 ?  166 SER   B HA   1 
ATOM   6282 H HB2  . SER   B 1 166 ? 36.636 -42.664 -12.119 1.00 27.96 ?  166 SER   B HB2  1 
ATOM   6283 H HB3  . SER   B 1 166 ? 37.941 -41.780 -12.311 1.00 27.96 ?  166 SER   B HB3  1 
ATOM   6284 H HG   . SER   B 1 166 ? 37.898 -41.444 -10.144 1.00 28.28 ?  166 SER   B HG   1 
ATOM   6285 N N    . SER   B 1 167 ? 34.966 -40.114 -9.953  1.00 20.40 ?  167 SER   B N    1 
ATOM   6286 C CA   . SER   B 1 167 ? 33.813 -40.174 -9.062  1.00 20.15 ?  167 SER   B CA   1 
ATOM   6287 C C    . SER   B 1 167 ? 32.892 -38.957 -9.158  1.00 19.78 ?  167 SER   B C    1 
ATOM   6288 O O    . SER   B 1 167 ? 31.815 -38.966 -8.549  1.00 20.11 ?  167 SER   B O    1 
ATOM   6289 C CB   . SER   B 1 167 ? 34.273 -40.354 -7.609  1.00 20.17 ?  167 SER   B CB   1 
ATOM   6290 O OG   . SER   B 1 167 ? 34.937 -39.189 -7.142  1.00 19.92 ?  167 SER   B OG   1 
ATOM   6291 H H    . SER   B 1 167 ? 35.619 -39.656 -9.647  1.00 24.46 ?  167 SER   B H    1 
ATOM   6292 H HA   . SER   B 1 167 ? 33.289 -40.956 -9.297  1.00 24.16 ?  167 SER   B HA   1 
ATOM   6293 H HB2  . SER   B 1 167 ? 33.496 -40.528 -7.053  1.00 24.18 ?  167 SER   B HB2  1 
ATOM   6294 H HB3  . SER   B 1 167 ? 34.880 -41.120 -7.563  1.00 24.18 ?  167 SER   B HB3  1 
ATOM   6295 H HG   . SER   B 1 167 ? 35.621 -39.053 -7.609  1.00 23.88 ?  167 SER   B HG   1 
ATOM   6296 N N    . PHE   B 1 168 ? 33.268 -37.916 -9.905  1.00 19.50 ?  168 PHE   B N    1 
ATOM   6297 C CA   . PHE   B 1 168 ? 32.431 -36.715 -9.964  1.00 18.98 ?  168 PHE   B CA   1 
ATOM   6298 C C    . PHE   B 1 168 ? 31.121 -36.974 -10.702 1.00 16.41 ?  168 PHE   B C    1 
ATOM   6299 O O    . PHE   B 1 168 ? 30.076 -36.382 -10.365 1.00 17.03 ?  168 PHE   B O    1 
ATOM   6300 C CB   . PHE   B 1 168 ? 33.189 -35.570 -10.633 1.00 19.33 ?  168 PHE   B CB   1 
ATOM   6301 C CG   . PHE   B 1 168 ? 32.376 -34.321 -10.773 1.00 19.15 ?  168 PHE   B CG   1 
ATOM   6302 C CD1  . PHE   B 1 168 ? 32.026 -33.584 -9.650  1.00 20.24 ?  168 PHE   B CD1  1 
ATOM   6303 C CD2  . PHE   B 1 168 ? 31.939 -33.895 -12.013 1.00 18.68 ?  168 PHE   B CD2  1 
ATOM   6304 C CE1  . PHE   B 1 168 ? 31.257 -32.443 -9.759  1.00 20.48 ?  168 PHE   B CE1  1 
ATOM   6305 C CE2  . PHE   B 1 168 ? 31.182 -32.737 -12.135 1.00 19.62 ?  168 PHE   B CE2  1 
ATOM   6306 C CZ   . PHE   B 1 168 ? 30.834 -32.012 -11.003 1.00 19.98 ?  168 PHE   B CZ   1 
ATOM   6307 H H    . PHE   B 1 168 ? 33.994 -37.879 -10.369 1.00 23.38 ?  168 PHE   B H    1 
ATOM   6308 H HA   . PHE   B 1 168 ? 32.213 -36.443 -9.062  1.00 22.75 ?  168 PHE   B HA   1 
ATOM   6309 H HB2  . PHE   B 1 168 ? 33.969 -35.355 -10.098 1.00 23.17 ?  168 PHE   B HB2  1 
ATOM   6310 H HB3  . PHE   B 1 168 ? 33.462 -35.846 -11.520 1.00 23.17 ?  168 PHE   B HB3  1 
ATOM   6311 H HD1  . PHE   B 1 168 ? 32.300 -33.876 -8.812  1.00 24.27 ?  168 PHE   B HD1  1 
ATOM   6312 H HD2  . PHE   B 1 168 ? 32.168 -34.372 -12.773 1.00 22.39 ?  168 PHE   B HD2  1 
ATOM   6313 H HE1  . PHE   B 1 168 ? 31.028 -31.962 -8.998  1.00 24.55 ?  168 PHE   B HE1  1 
ATOM   6314 H HE2  . PHE   B 1 168 ? 30.892 -32.452 -12.974 1.00 23.52 ?  168 PHE   B HE2  1 
ATOM   6315 H HZ   . PHE   B 1 168 ? 30.318 -31.240 -11.083 1.00 23.95 ?  168 PHE   B HZ   1 
ATOM   6316 N N    . LEU   B 1 169 ? 31.162 -37.846 -11.706 1.00 16.90 ?  169 LEU   B N    1 
ATOM   6317 C CA   . LEU   B 1 169 ? 29.984 -38.170 -12.504 1.00 19.13 ?  169 LEU   B CA   1 
ATOM   6318 C C    . LEU   B 1 169 ? 29.978 -39.612 -12.987 1.00 22.06 ?  169 LEU   B C    1 
ATOM   6319 O O    . LEU   B 1 169 ? 29.075 -40.033 -13.713 1.00 24.43 ?  169 LEU   B O    1 
ATOM   6320 C CB   . LEU   B 1 169 ? 29.905 -37.248 -13.718 1.00 20.98 ?  169 LEU   B CB   1 
ATOM   6321 C CG   . LEU   B 1 169 ? 28.673 -36.348 -13.783 1.00 24.25 ?  169 LEU   B CG   1 
ATOM   6322 C CD1  . LEU   B 1 169 ? 28.635 -35.633 -15.115 1.00 25.17 ?  169 LEU   B CD1  1 
ATOM   6323 C CD2  . LEU   B 1 169 ? 27.396 -37.141 -13.559 1.00 24.46 ?  169 LEU   B CD2  1 
ATOM   6324 O OXT  . LEU   B 1 169 ? 30.879 -40.380 -12.675 1.00 23.13 -1 169 LEU   B OXT  1 
ATOM   6325 H H    . LEU   B 1 169 ? 31.874 -38.263 -11.963 1.00 20.25 ?  169 LEU   B H    1 
ATOM   6326 H HA   . LEU   B 1 169 ? 29.200 -38.023 -11.957 1.00 22.94 ?  169 LEU   B HA   1 
ATOM   6327 H HB2  . LEU   B 1 169 ? 30.684 -36.670 -13.724 1.00 25.15 ?  169 LEU   B HB2  1 
ATOM   6328 H HB3  . LEU   B 1 169 ? 29.902 -37.793 -14.522 1.00 25.15 ?  169 LEU   B HB3  1 
ATOM   6329 H HG   . LEU   B 1 169 ? 28.734 -35.674 -13.086 1.00 29.08 ?  169 LEU   B HG   1 
ATOM   6330 H HD11 . LEU   B 1 169 ? 27.863 -35.047 -15.137 1.00 30.18 ?  169 LEU   B HD11 1 
ATOM   6331 H HD12 . LEU   B 1 169 ? 29.449 -35.116 -15.217 1.00 30.18 ?  169 LEU   B HD12 1 
ATOM   6332 H HD13 . LEU   B 1 169 ? 28.570 -36.293 -15.822 1.00 30.18 ?  169 LEU   B HD13 1 
ATOM   6333 H HD21 . LEU   B 1 169 ? 26.657 -36.679 -13.979 1.00 29.33 ?  169 LEU   B HD21 1 
ATOM   6334 H HD22 . LEU   B 1 169 ? 27.504 -38.023 -13.952 1.00 29.33 ?  169 LEU   B HD22 1 
ATOM   6335 H HD23 . LEU   B 1 169 ? 27.241 -37.223 -12.606 1.00 29.33 ?  169 LEU   B HD23 1 
HETATM 6336 O O1   B A1A8F C 2 .   ? 15.024 -2.790  2.920   0.10 15.86 ?  201 A1A8F A O1   1 
HETATM 6337 C C1   B A1A8F C 2 .   ? 12.401 1.116   -1.127  0.10 16.73 ?  201 A1A8F A C1   1 
HETATM 6338 C C2   B A1A8F C 2 .   ? 12.546 0.590   0.346   0.10 16.48 ?  201 A1A8F A C2   1 
HETATM 6339 C C3   B A1A8F C 2 .   ? 11.303 1.065   1.122   0.10 16.52 ?  201 A1A8F A C3   1 
HETATM 6340 C C4   B A1A8F C 2 .   ? 12.599 -0.981  0.303   0.10 16.55 ?  201 A1A8F A C4   1 
HETATM 6341 C C5   B A1A8F C 2 .   ? 13.955 -1.699  0.554   0.10 16.46 ?  201 A1A8F A C5   1 
HETATM 6342 C C6   B A1A8F C 2 .   ? 15.097 -0.915  1.256   0.10 16.02 ?  201 A1A8F A C6   1 
HETATM 6343 C C7   B A1A8F C 2 .   ? 15.881 -1.924  2.194   0.10 15.94 ?  201 A1A8F A C7   1 
HETATM 6344 C C8   B A1A8F C 2 .   ? 14.720 0.650   3.364   0.10 13.99 ?  201 A1A8F A C8   1 
HETATM 6345 C C10  B A1A8F C 2 .   ? 15.230 2.100   5.276   0.10 12.29 ?  201 A1A8F A C10  1 
HETATM 6346 C C11  B A1A8F C 2 .   ? 15.111 1.963   3.845   0.10 12.71 ?  201 A1A8F A C11  1 
HETATM 6347 C C12  B A1A8F C 2 .   ? 15.457 3.292   3.354   0.10 12.14 ?  201 A1A8F A C12  1 
HETATM 6348 C C13  B A1A8F C 2 .   ? 15.750 4.112   4.439   0.10 11.95 ?  201 A1A8F A C13  1 
HETATM 6349 C C14  B A1A8F C 2 .   ? 13.819 1.192   1.041   0.10 16.03 ?  201 A1A8F A C14  1 
HETATM 6350 C C9   B A1A8F C 2 .   ? 14.651 -0.035  5.657   0.10 13.25 ?  201 A1A8F A C9   1 
HETATM 6351 N N1   B A1A8F C 2 .   ? 14.532 0.294   1.954   0.10 15.60 ?  201 A1A8F A N1   1 
HETATM 6352 N N2   B A1A8F C 2 .   ? 14.491 -0.319  4.310   0.10 13.73 ?  201 A1A8F A N2   1 
HETATM 6353 N N3   B A1A8F C 2 .   ? 15.007 1.138   6.174   0.10 12.67 ?  201 A1A8F A N3   1 
HETATM 6354 N N4   B A1A8F C 2 .   ? 15.607 3.377   5.576   0.10 11.97 ?  201 A1A8F A N4   1 
HETATM 6355 H H14  B A1A8F C 2 .   ? 15.050 -2.581  3.860   0.10 19.01 ?  201 A1A8F A H14  1 
HETATM 6356 H H3   B A1A8F C 2 .   ? 13.214 0.798   -1.815  0.10 20.05 ?  201 A1A8F A H3   1 
HETATM 6357 H H4   B A1A8F C 2 .   ? 12.396 2.209   -1.238  0.10 20.05 ?  201 A1A8F A H4   1 
HETATM 6358 H H2   B A1A8F C 2 .   ? 11.490 0.788   -1.670  0.10 20.05 ?  201 A1A8F A H2   1 
HETATM 6359 H H6   B A1A8F C 2 .   ? 11.237 2.160   1.267   0.10 19.80 ?  201 A1A8F A H6   1 
HETATM 6360 H H5   B A1A8F C 2 .   ? 10.365 0.800   0.624   0.10 19.80 ?  201 A1A8F A H5   1 
HETATM 6361 H H7   B A1A8F C 2 .   ? 11.211 0.664   2.149   0.10 19.80 ?  201 A1A8F A H7   1 
HETATM 6362 H H8   B A1A8F C 2 .   ? 12.195 -1.379  -0.633  0.10 19.83 ?  201 A1A8F A H8   1 
HETATM 6363 H H9   B A1A8F C 2 .   ? 11.869 -1.444  1.036   0.10 19.83 ?  201 A1A8F A H9   1 
HETATM 6364 H H11  B A1A8F C 2 .   ? 13.736 -2.640  1.108   0.10 19.73 ?  201 A1A8F A H11  1 
HETATM 6365 H H10  B A1A8F C 2 .   ? 14.308 -2.099  -0.417  0.10 19.73 ?  201 A1A8F A H10  1 
HETATM 6366 H H1   B A1A8F C 2 .   ? 15.815 -0.556  0.454   0.10 19.19 ?  201 A1A8F A H1   1 
HETATM 6367 H H12  B A1A8F C 2 .   ? 16.577 -2.512  1.547   0.10 19.11 ?  201 A1A8F A H12  1 
HETATM 6368 H H13  B A1A8F C 2 .   ? 16.505 -1.342  2.896   0.10 19.11 ?  201 A1A8F A H13  1 
HETATM 6369 H H16  B A1A8F C 2 .   ? 15.500 3.640   2.347   0.10 14.55 ?  201 A1A8F A H16  1 
HETATM 6370 H H17  B A1A8F C 2 .   ? 16.049 5.146   4.594   0.10 14.32 ?  201 A1A8F A H17  1 
HETATM 6371 H H19  B A1A8F C 2 .   ? 13.534 2.135   1.572   0.10 19.21 ?  201 A1A8F A H19  1 
HETATM 6372 H H20  B A1A8F C 2 .   ? 14.509 1.560   0.234   0.10 19.21 ?  201 A1A8F A H20  1 
HETATM 6373 H H15  B A1A8F C 2 .   ? 14.475 -0.830  6.442   0.10 15.88 ?  201 A1A8F A H15  1 
HETATM 6374 H H18  B A1A8F C 2 .   ? 15.773 3.777   6.535   0.10 14.35 ?  201 A1A8F A H18  1 
HETATM 6375 O O1   C A1A8F D 2 .   ? 15.096 -2.934  3.223   0.10 13.40 ?  202 A1A8F A O1   1 
HETATM 6376 C C1   C A1A8F D 2 .   ? 14.442 0.960   -1.544  0.10 15.38 ?  202 A1A8F A C1   1 
HETATM 6377 C C2   C A1A8F D 2 .   ? 13.558 0.489   -0.329  0.10 15.42 ?  202 A1A8F A C2   1 
HETATM 6378 C C3   C A1A8F D 2 .   ? 12.149 1.104   -0.542  0.10 15.58 ?  202 A1A8F A C3   1 
HETATM 6379 C C4   C A1A8F D 2 .   ? 13.480 -1.088  -0.369  0.10 15.40 ?  202 A1A8F A C4   1 
HETATM 6380 C C5   C A1A8F D 2 .   ? 14.204 -1.884  0.749   0.10 15.25 ?  202 A1A8F A C5   1 
HETATM 6381 C C6   C A1A8F D 2 .   ? 15.289 -1.109  1.522   0.10 14.84 ?  202 A1A8F A C6   1 
HETATM 6382 C C7   C A1A8F D 2 .   ? 16.018 -2.075  2.564   0.10 14.18 ?  202 A1A8F A C7   1 
HETATM 6383 C C8   C A1A8F D 2 .   ? 14.749 0.546   3.523   0.10 13.72 ?  202 A1A8F A C8   1 
HETATM 6384 C C10  C A1A8F D 2 .   ? 15.207 2.098   5.388   0.10 12.56 ?  202 A1A8F A C10  1 
HETATM 6385 C C11  C A1A8F D 2 .   ? 15.130 1.880   3.948   0.10 12.71 ?  202 A1A8F A C11  1 
HETATM 6386 C C12  C A1A8F D 2 .   ? 15.495 3.180   3.381   0.10 12.22 ?  202 A1A8F A C12  1 
HETATM 6387 C C13  C A1A8F D 2 .   ? 15.758 4.059   4.422   0.10 12.10 ?  202 A1A8F A C13  1 
HETATM 6388 C C14  C A1A8F D 2 .   ? 14.165 1.059   1.052   0.10 15.26 ?  202 A1A8F A C14  1 
HETATM 6389 C C9   C A1A8F D 2 .   ? 14.611 -0.009  5.865   0.10 13.39 ?  202 A1A8F A C9   1 
HETATM 6390 N N1   C A1A8F D 2 .   ? 14.606 0.099   2.113   0.10 14.96 ?  202 A1A8F A N1   1 
HETATM 6391 N N2   C A1A8F D 2 .   ? 14.494 -0.361  4.522   0.10 13.52 ?  202 A1A8F A N2   1 
HETATM 6392 N N3   C A1A8F D 2 .   ? 14.958 1.184   6.364   0.10 13.03 ?  202 A1A8F A N3   1 
HETATM 6393 N N4   C A1A8F D 2 .   ? 15.579 3.392   5.602   0.10 12.21 ?  202 A1A8F A N4   1 
HETATM 6394 H H14  C A1A8F D 2 .   ? 15.574 -3.579  3.768   0.10 16.05 ?  202 A1A8F A H14  1 
HETATM 6395 H H3   C A1A8F D 2 .   ? 14.048 0.692   -2.546  0.10 18.44 ?  202 A1A8F A H3   1 
HETATM 6396 H H4   C A1A8F D 2 .   ? 15.465 0.538   -1.567  0.10 18.44 ?  202 A1A8F A H4   1 
HETATM 6397 H H2   C A1A8F D 2 .   ? 14.606 2.050   -1.632  0.10 18.44 ?  202 A1A8F A H2   1 
HETATM 6398 H H6   C A1A8F D 2 .   ? 11.603 0.718   -1.422  0.10 18.67 ?  202 A1A8F A H6   1 
HETATM 6399 H H5   C A1A8F D 2 .   ? 12.165 2.201   -0.694  0.10 18.67 ?  202 A1A8F A H5   1 
HETATM 6400 H H7   C A1A8F D 2 .   ? 11.447 0.944   0.289   0.10 18.67 ?  202 A1A8F A H7   1 
HETATM 6401 H H8   C A1A8F D 2 .   ? 13.831 -1.489  -1.341  0.10 18.46 ?  202 A1A8F A H8   1 
HETATM 6402 H H9   C A1A8F D 2 .   ? 12.420 -1.454  -0.385  0.10 18.46 ?  202 A1A8F A H9   1 
HETATM 6403 H H11  C A1A8F D 2 .   ? 14.638 -2.814  0.283   0.10 18.28 ?  202 A1A8F A H11  1 
HETATM 6404 H H10  C A1A8F D 2 .   ? 13.446 -2.314  1.432   0.10 18.28 ?  202 A1A8F A H10  1 
HETATM 6405 H H1   C A1A8F D 2 .   ? 16.058 -0.757  0.761   0.10 17.79 ?  202 A1A8F A H1   1 
HETATM 6406 H H12  C A1A8F D 2 .   ? 16.597 -1.457  3.277   0.10 17.00 ?  202 A1A8F A H12  1 
HETATM 6407 H H13  C A1A8F D 2 .   ? 16.771 -2.695  2.000   0.10 17.00 ?  202 A1A8F A H13  1 
HETATM 6408 H H16  C A1A8F D 2 .   ? 15.568 3.477   2.344   0.10 14.64 ?  202 A1A8F A H16  1 
HETATM 6409 H H17  C A1A8F D 2 .   ? 16.056 5.103   4.518   0.10 14.50 ?  202 A1A8F A H17  1 
HETATM 6410 H H19  C A1A8F D 2 .   ? 13.422 1.770   1.488   0.10 18.28 ?  202 A1A8F A H19  1 
HETATM 6411 H H20  C A1A8F D 2 .   ? 15.016 1.742   0.774   0.10 18.28 ?  202 A1A8F A H20  1 
HETATM 6412 H H15  C A1A8F D 2 .   ? 14.403 -0.766  6.649   0.10 16.05 ?  202 A1A8F A H15  1 
HETATM 6413 H H18  C A1A8F D 2 .   ? 15.719 3.848   6.522   0.10 14.63 ?  202 A1A8F A H18  1 
HETATM 6414 C C1   D A1A8E E 3 .   ? 12.227 0.768   -1.003  0.14 16.94 ?  203 A1A8E A C1   1 
HETATM 6415 C C2   D A1A8E E 3 .   ? 12.215 0.555   0.560   0.14 16.65 ?  203 A1A8E A C2   1 
HETATM 6416 C C3   D A1A8E E 3 .   ? 10.809 0.882   1.099   0.14 16.89 ?  203 A1A8E A C3   1 
HETATM 6417 C C4   D A1A8E E 3 .   ? 12.622 -0.896  0.899   0.14 16.68 ?  203 A1A8E A C4   1 
HETATM 6418 C C5   D A1A8E E 3 .   ? 14.014 -1.199  0.324   0.14 16.12 ?  203 A1A8E A C5   1 
HETATM 6419 C C6   D A1A8E E 3 .   ? 15.139 -0.268  0.910   0.14 15.49 ?  203 A1A8E A C6   1 
HETATM 6420 C C7   D A1A8E E 3 .   ? 16.063 0.288   -0.307  0.14 16.22 ?  203 A1A8E A C7   1 
HETATM 6421 C C8   D A1A8E E 3 .   ? 14.804 0.909   3.180   0.14 11.89 ?  203 A1A8E A C8   1 
HETATM 6422 C C9   D A1A8E E 3 .   ? 14.902 -0.246  5.299   0.14 10.31 ?  203 A1A8E A C9   1 
HETATM 6423 C C10  D A1A8E E 3 .   ? 15.319 1.977   5.316   0.14 8.96  ?  203 A1A8E A C10  1 
HETATM 6424 C C11  D A1A8E E 3 .   ? 15.132 2.128   3.886   0.14 10.01 ?  203 A1A8E A C11  1 
HETATM 6425 C C12  D A1A8E E 3 .   ? 15.366 3.564   3.628   0.14 9.40  ?  203 A1A8E A C12  1 
HETATM 6426 C C13  D A1A8E E 3 .   ? 15.664 4.174   4.847   0.14 8.73  ?  203 A1A8E A C13  1 
HETATM 6427 C C14  D A1A8E E 3 .   ? 13.263 1.502   1.271   0.14 15.69 ?  203 A1A8E A C14  1 
HETATM 6428 N N1   D A1A8E E 3 .   ? 14.563 0.874   1.730   0.14 14.24 ?  203 A1A8E A N1   1 
HETATM 6429 N N2   D A1A8E E 3 .   ? 14.692 -0.249  3.917   0.14 11.70 ?  203 A1A8E A N2   1 
HETATM 6430 N N3   D A1A8E E 3 .   ? 15.218 0.818   6.044   0.14 9.05  ?  203 A1A8E A N3   1 
HETATM 6431 N N4   D A1A8E E 3 .   ? 15.624 3.209   5.786   0.14 8.37  ?  203 A1A8E A N4   1 
HETATM 6432 O O1   D A1A8E E 3 .   ? 15.982 1.698   -0.402  0.14 16.73 ?  203 A1A8E A O1   1 
HETATM 6433 H H3   D A1A8E E 3 .   ? 11.735 -0.050  -1.569  0.14 20.30 ?  203 A1A8E A H3   1 
HETATM 6434 H H4   D A1A8E E 3 .   ? 13.250 0.840   -1.434  0.14 20.30 ?  203 A1A8E A H4   1 
HETATM 6435 H H2   D A1A8E E 3 .   ? 11.717 1.696   -1.330  0.14 20.30 ?  203 A1A8E A H2   1 
HETATM 6436 H H6   D A1A8E E 3 .   ? 10.001 0.340   0.576   0.14 20.24 ?  203 A1A8E A H6   1 
HETATM 6437 H H7   D A1A8E E 3 .   ? 10.546 1.955   1.028   0.14 20.24 ?  203 A1A8E A H7   1 
HETATM 6438 H H5   D A1A8E E 3 .   ? 10.708 0.629   2.172   0.14 20.24 ?  203 A1A8E A H5   1 
HETATM 6439 H H9   D A1A8E E 3 .   ? 12.629 -1.073  2.011   0.14 20.00 ?  203 A1A8E A H9   1 
HETATM 6440 H H8   D A1A8E E 3 .   ? 11.860 -1.630  0.524   0.14 20.00 ?  203 A1A8E A H8   1 
HETATM 6441 H H10  D A1A8E E 3 .   ? 13.992 -1.147  -0.790  0.14 19.32 ?  203 A1A8E A H10  1 
HETATM 6442 H H11  D A1A8E E 3 .   ? 14.293 -2.276  0.501   0.14 19.32 ?  203 A1A8E A H11  1 
HETATM 6443 H H1   D A1A8E E 3 .   ? 15.812 -0.870  1.585   0.14 18.57 ?  203 A1A8E A H1   1 
HETATM 6444 H H13  D A1A8E E 3 .   ? 17.112 -0.011  -0.111  0.14 19.44 ?  203 A1A8E A H13  1 
HETATM 6445 H H12  D A1A8E E 3 .   ? 15.762 -0.172  -1.270  0.14 19.44 ?  203 A1A8E A H12  1 
HETATM 6446 H H15  D A1A8E E 3 .   ? 14.808 -1.207  5.850   0.14 12.34 ?  203 A1A8E A H15  1 
HETATM 6447 H H16  D A1A8E E 3 .   ? 15.329 4.134   2.696   0.14 11.25 ?  203 A1A8E A H16  1 
HETATM 6448 H H17  D A1A8E E 3 .   ? 15.905 5.206   5.163   0.14 10.45 ?  203 A1A8E A H17  1 
HETATM 6449 H H19  D A1A8E E 3 .   ? 12.739 1.993   2.152   0.14 18.80 ?  203 A1A8E A H19  1 
HETATM 6450 H H20  D A1A8E E 3 .   ? 13.486 2.362   0.591   0.14 18.80 ?  203 A1A8E A H20  1 
HETATM 6451 H H18  D A1A8E E 3 .   ? 15.821 3.418   6.811   0.14 10.02 ?  203 A1A8E A H18  1 
HETATM 6452 H H14  D A1A8E E 3 .   ? 16.523 2.022   -1.146  0.14 20.05 ?  203 A1A8E A H14  1 
HETATM 6453 O O    . HOH   F 4 .   ? 4.799  3.850   0.617   1.00 31.38 ?  301 HOH   A O    1 
HETATM 6454 O O    . HOH   F 4 .   ? 14.768 -4.636  20.497  1.00 47.01 ?  302 HOH   A O    1 
HETATM 6455 O O    . HOH   F 4 .   ? 14.199 -4.526  -11.951 1.00 39.92 ?  303 HOH   A O    1 
HETATM 6456 O O    . HOH   F 4 .   ? 7.001  -8.176  11.874  1.00 24.17 ?  304 HOH   A O    1 
HETATM 6457 O O    . HOH   F 4 .   ? 34.424 -1.851  12.502  1.00 39.65 ?  305 HOH   A O    1 
HETATM 6458 O O    . HOH   F 4 .   ? 28.975 0.424   -9.787  1.00 22.47 ?  306 HOH   A O    1 
HETATM 6459 O O    . HOH   F 4 .   ? 26.878 11.446  1.652   1.00 16.83 ?  307 HOH   A O    1 
HETATM 6460 O O    . HOH   F 4 .   ? 7.648  -6.376  -6.674  1.00 42.75 ?  308 HOH   A O    1 
HETATM 6461 O O    . HOH   F 4 .   ? 0.788  -4.605  0.187   1.00 35.92 ?  309 HOH   A O    1 
HETATM 6462 O O    . HOH   F 4 .   ? 11.809 -10.911 -10.019 1.00 53.04 ?  310 HOH   A O    1 
HETATM 6463 O O    . HOH   F 4 .   ? 12.063 0.418   14.822  1.00 36.59 ?  311 HOH   A O    1 
HETATM 6464 O O    . HOH   F 4 .   ? 15.099 -12.296 18.590  1.00 44.15 ?  312 HOH   A O    1 
HETATM 6465 O O    . HOH   F 4 .   ? 15.019 3.830   17.586  1.00 40.02 ?  313 HOH   A O    1 
HETATM 6466 O O    . HOH   F 4 .   ? 3.693  -9.407  9.807   1.00 37.95 ?  314 HOH   A O    1 
HETATM 6467 O O    . HOH   F 4 .   ? 9.220  -10.098 19.283  1.00 46.12 ?  315 HOH   A O    1 
HETATM 6468 O O    . HOH   F 4 .   ? 30.283 -13.300 -8.509  1.00 24.55 ?  316 HOH   A O    1 
HETATM 6469 O O    . HOH   F 4 .   ? 42.434 10.575  5.103   1.00 20.30 ?  317 HOH   A O    1 
HETATM 6470 O O    . HOH   F 4 .   ? 28.267 -6.245  19.579  1.00 44.67 ?  318 HOH   A O    1 
HETATM 6471 O O    . HOH   F 4 .   ? 14.769 -13.980 16.696  1.00 28.42 ?  319 HOH   A O    1 
HETATM 6472 O O    . HOH   F 4 .   ? -0.660 -8.602  2.162   1.00 48.46 ?  320 HOH   A O    1 
HETATM 6473 O O    . HOH   F 4 .   ? 7.978  -12.612 -0.901  1.00 25.50 ?  321 HOH   A O    1 
HETATM 6474 O O    A HOH   F 4 .   ? 28.262 -0.217  -13.355 0.66 29.58 ?  322 HOH   A O    1 
HETATM 6475 O O    . HOH   F 4 .   ? 30.910 6.232   -12.322 1.00 28.37 ?  323 HOH   A O    1 
HETATM 6476 O O    B HOH   F 4 .   ? 21.231 -2.225  -2.968  0.34 16.24 ?  324 HOH   A O    1 
HETATM 6477 O O    . HOH   F 4 .   ? 13.616 -15.285 -7.612  1.00 29.13 ?  325 HOH   A O    1 
HETATM 6478 O O    . HOH   F 4 .   ? 10.438 -22.148 -1.265  1.00 50.30 ?  326 HOH   A O    1 
HETATM 6479 O O    . HOH   F 4 .   ? 25.793 -0.839  -7.481  1.00 20.44 ?  327 HOH   A O    1 
HETATM 6480 O O    . HOH   F 4 .   ? 26.551 -19.346 -1.788  1.00 14.77 ?  328 HOH   A O    1 
HETATM 6481 O O    . HOH   F 4 .   ? 22.250 -19.337 11.336  1.00 34.32 ?  329 HOH   A O    1 
HETATM 6482 O O    . HOH   F 4 .   ? 23.960 -15.778 -9.165  1.00 35.96 ?  330 HOH   A O    1 
HETATM 6483 O O    . HOH   F 4 .   ? 22.340 5.277   19.018  1.00 43.65 ?  331 HOH   A O    1 
HETATM 6484 O O    . HOH   F 4 .   ? 37.552 2.816   10.204  1.00 27.24 ?  332 HOH   A O    1 
HETATM 6485 O O    . HOH   F 4 .   ? 31.076 -18.125 7.775   1.00 20.06 ?  333 HOH   A O    1 
HETATM 6486 O O    . HOH   F 4 .   ? 15.763 2.228   24.545  1.00 54.32 ?  334 HOH   A O    1 
HETATM 6487 O O    . HOH   F 4 .   ? 36.277 -5.068  -0.533  1.00 31.02 ?  335 HOH   A O    1 
HETATM 6488 O O    B HOH   F 4 .   ? 21.206 2.672   0.062   0.34 17.01 ?  336 HOH   A O    1 
HETATM 6489 O O    . HOH   F 4 .   ? 38.302 10.183  7.081   1.00 45.04 ?  337 HOH   A O    1 
HETATM 6490 O O    . HOH   F 4 .   ? 44.327 7.179   6.402   1.00 27.53 ?  338 HOH   A O    1 
HETATM 6491 O O    . HOH   F 4 .   ? 27.911 0.819   -7.235  1.00 14.99 ?  339 HOH   A O    1 
HETATM 6492 O O    . HOH   F 4 .   ? 19.002 -21.975 6.907   1.00 34.02 ?  340 HOH   A O    1 
HETATM 6493 O O    . HOH   F 4 .   ? 20.006 -12.613 -8.806  1.00 27.38 ?  341 HOH   A O    1 
HETATM 6494 O O    . HOH   F 4 .   ? 17.195 -18.103 14.957  1.00 30.31 ?  342 HOH   A O    1 
HETATM 6495 O O    A HOH   F 4 .   ? 17.539 -1.734  0.429   0.66 23.18 ?  343 HOH   A O    1 
HETATM 6496 O O    B HOH   F 4 .   ? 18.595 -2.047  -1.717  0.34 33.57 ?  344 HOH   A O    1 
HETATM 6497 O O    A HOH   F 4 .   ? 14.319 0.553   6.787   0.66 30.01 ?  345 HOH   A O    1 
HETATM 6498 O O    . HOH   F 4 .   ? 27.344 13.787  2.838   1.00 28.17 ?  346 HOH   A O    1 
HETATM 6499 O O    . HOH   F 4 .   ? 34.012 -1.047  -8.951  1.00 26.34 ?  347 HOH   A O    1 
HETATM 6500 O O    . HOH   F 4 .   ? 18.751 -19.377 13.623  1.00 35.23 ?  348 HOH   A O    1 
HETATM 6501 O O    . HOH   F 4 .   ? 22.759 12.520  1.598   1.00 15.36 ?  349 HOH   A O    1 
HETATM 6502 O O    . HOH   F 4 .   ? 22.662 -12.002 21.836  1.00 52.34 ?  350 HOH   A O    1 
HETATM 6503 O O    . HOH   F 4 .   ? 38.584 4.997   6.959   1.00 15.82 ?  351 HOH   A O    1 
HETATM 6504 O O    . HOH   F 4 .   ? 17.212 -17.878 -5.069  1.00 29.32 ?  352 HOH   A O    1 
HETATM 6505 O O    . HOH   F 4 .   ? 6.472  -5.616  11.156  1.00 23.02 ?  353 HOH   A O    1 
HETATM 6506 O O    . HOH   F 4 .   ? 42.570 4.288   5.363   1.00 34.04 ?  354 HOH   A O    1 
HETATM 6507 O O    . HOH   F 4 .   ? 31.721 8.199   14.837  1.00 24.94 ?  355 HOH   A O    1 
HETATM 6508 O O    . HOH   F 4 .   ? 20.683 -19.767 -5.101  1.00 28.82 ?  356 HOH   A O    1 
HETATM 6509 O O    . HOH   F 4 .   ? 8.264  -21.533 4.034   1.00 50.92 ?  357 HOH   A O    1 
HETATM 6510 O O    A HOH   F 4 .   ? 14.680 -3.675  3.085   0.80 22.00 ?  358 HOH   A O    1 
HETATM 6511 O O    . HOH   F 4 .   ? 14.444 -21.286 -4.226  1.00 30.32 ?  359 HOH   A O    1 
HETATM 6512 O O    . HOH   F 4 .   ? 39.782 -1.017  -5.225  1.00 20.20 ?  360 HOH   A O    1 
HETATM 6513 O O    . HOH   F 4 .   ? 30.826 3.089   8.253   1.00 12.44 ?  361 HOH   A O    1 
HETATM 6514 O O    . HOH   F 4 .   ? 35.846 -12.653 6.840   1.00 15.85 ?  362 HOH   A O    1 
HETATM 6515 O O    . HOH   F 4 .   ? 31.144 -13.944 -2.469  1.00 14.16 ?  363 HOH   A O    1 
HETATM 6516 O O    . HOH   F 4 .   ? 24.063 -2.126  -2.162  1.00 11.71 ?  364 HOH   A O    1 
HETATM 6517 O O    A HOH   F 4 .   ? 21.289 -2.416  -2.065  0.66 13.80 ?  365 HOH   A O    1 
HETATM 6518 O O    A HOH   F 4 .   ? -0.433 -3.119  3.092   0.66 34.05 ?  366 HOH   A O    1 
HETATM 6519 O O    . HOH   F 4 .   ? 37.298 11.998  4.901   1.00 28.79 ?  367 HOH   A O    1 
HETATM 6520 O O    . HOH   F 4 .   ? 21.905 -21.892 8.457   1.00 28.99 ?  368 HOH   A O    1 
HETATM 6521 O O    . HOH   F 4 .   ? 32.005 -9.318  -6.668  1.00 23.29 ?  369 HOH   A O    1 
HETATM 6522 O O    . HOH   F 4 .   ? 43.959 8.478   -3.076  1.00 27.99 ?  370 HOH   A O    1 
HETATM 6523 O O    . HOH   F 4 .   ? 43.344 7.815   2.690   1.00 28.59 ?  371 HOH   A O    1 
HETATM 6524 O O    . HOH   F 4 .   ? 28.729 -10.599 -14.054 1.00 41.55 ?  372 HOH   A O    1 
HETATM 6525 O O    . HOH   F 4 .   ? 9.995  -21.376 5.703   1.00 22.05 ?  373 HOH   A O    1 
HETATM 6526 O O    . HOH   F 4 .   ? 27.521 -10.586 14.080  1.00 17.99 ?  374 HOH   A O    1 
HETATM 6527 O O    . HOH   F 4 .   ? 33.699 -7.137  4.283   1.00 16.91 ?  375 HOH   A O    1 
HETATM 6528 O O    . HOH   F 4 .   ? 37.236 -2.901  9.720   1.00 45.17 ?  376 HOH   A O    1 
HETATM 6529 O O    . HOH   F 4 .   ? 18.525 9.417   8.947   1.00 22.14 ?  377 HOH   A O    1 
HETATM 6530 O O    A HOH   F 4 .   ? 20.136 4.521   -7.562  0.66 19.63 ?  378 HOH   A O    1 
HETATM 6531 O O    . HOH   F 4 .   ? 13.398 -1.462  -6.688  1.00 23.39 ?  379 HOH   A O    1 
HETATM 6532 O O    . HOH   F 4 .   ? 15.185 -8.106  -9.854  1.00 29.27 ?  380 HOH   A O    1 
HETATM 6533 O O    . HOH   F 4 .   ? 16.586 -22.077 0.980   1.00 30.79 ?  381 HOH   A O    1 
HETATM 6534 O O    . HOH   F 4 .   ? 24.418 3.597   -1.821  1.00 16.43 ?  382 HOH   A O    1 
HETATM 6535 O O    . HOH   F 4 .   ? 17.080 -19.289 4.899   1.00 16.37 ?  383 HOH   A O    1 
HETATM 6536 O O    . HOH   F 4 .   ? 24.001 3.962   -4.825  1.00 24.37 ?  384 HOH   A O    1 
HETATM 6537 O O    . HOH   F 4 .   ? 21.219 10.200  15.033  1.00 37.05 ?  385 HOH   A O    1 
HETATM 6538 O O    . HOH   F 4 .   ? 33.597 -16.990 8.063   1.00 19.90 ?  386 HOH   A O    1 
HETATM 6539 O O    . HOH   F 4 .   ? 23.489 11.401  4.093   1.00 12.88 ?  387 HOH   A O    1 
HETATM 6540 O O    . HOH   F 4 .   ? 24.315 -7.761  14.473  1.00 17.43 ?  388 HOH   A O    1 
HETATM 6541 O O    . HOH   F 4 .   ? 10.979 1.724   12.564  1.00 27.73 ?  389 HOH   A O    1 
HETATM 6542 O O    . HOH   F 4 .   ? 31.912 -7.299  -9.852  1.00 22.23 ?  390 HOH   A O    1 
HETATM 6543 O O    . HOH   F 4 .   ? 24.786 -17.530 12.735  1.00 24.93 ?  391 HOH   A O    1 
HETATM 6544 O O    . HOH   F 4 .   ? 26.944 4.160   -0.688  1.00 12.81 ?  392 HOH   A O    1 
HETATM 6545 O O    . HOH   F 4 .   ? 32.815 -9.251  5.909   1.00 20.27 ?  393 HOH   A O    1 
HETATM 6546 O O    . HOH   F 4 .   ? 30.717 1.887   16.680  1.00 22.00 ?  394 HOH   A O    1 
HETATM 6547 O O    . HOH   F 4 .   ? 27.643 -6.268  -14.062 1.00 39.53 ?  395 HOH   A O    1 
HETATM 6548 O O    A HOH   F 4 .   ? 24.622 2.020   -7.004  0.66 18.63 ?  396 HOH   A O    1 
HETATM 6549 O O    A HOH   F 4 .   ? 18.611 -2.489  -16.351 0.66 34.82 ?  397 HOH   A O    1 
HETATM 6550 O O    . HOH   F 4 .   ? 15.487 11.841  7.893   1.00 39.65 ?  398 HOH   A O    1 
HETATM 6551 O O    . HOH   F 4 .   ? 37.605 -2.019  5.779   1.00 26.56 ?  399 HOH   A O    1 
HETATM 6552 O O    . HOH   F 4 .   ? 27.363 2.328   18.694  1.00 33.64 ?  400 HOH   A O    1 
HETATM 6553 O O    A HOH   F 4 .   ? 21.389 3.136   -0.365  0.66 12.14 ?  401 HOH   A O    1 
HETATM 6554 O O    . HOH   F 4 .   ? 20.612 -20.022 2.790   1.00 19.42 ?  402 HOH   A O    1 
HETATM 6555 O O    . HOH   F 4 .   ? 30.126 -10.096 12.978  1.00 22.83 ?  403 HOH   A O    1 
HETATM 6556 O O    . HOH   F 4 .   ? 16.238 16.684  8.638   1.00 36.69 ?  404 HOH   A O    1 
HETATM 6557 O O    . HOH   F 4 .   ? 15.237 -21.531 14.247  1.00 19.17 ?  405 HOH   A O    1 
HETATM 6558 O O    . HOH   F 4 .   ? 13.971 -4.871  17.408  1.00 27.69 ?  406 HOH   A O    1 
HETATM 6559 O O    A HOH   F 4 .   ? 19.001 -0.690  -1.640  0.66 13.94 ?  407 HOH   A O    1 
HETATM 6560 O O    . HOH   F 4 .   ? 8.984  -11.985 17.283  1.00 43.71 ?  408 HOH   A O    1 
HETATM 6561 O O    . HOH   F 4 .   ? 38.133 -1.343  -1.959  1.00 18.97 ?  409 HOH   A O    1 
HETATM 6562 O O    . HOH   F 4 .   ? 29.877 -1.925  -12.763 1.00 48.14 ?  410 HOH   A O    1 
HETATM 6563 O O    . HOH   F 4 .   ? 14.326 -0.429  -12.337 1.00 37.91 ?  411 HOH   A O    1 
HETATM 6564 O O    . HOH   F 4 .   ? 40.972 -8.298  -6.806  1.00 35.54 ?  412 HOH   A O    1 
HETATM 6565 O O    . HOH   F 4 .   ? 30.397 -12.919 13.490  1.00 20.57 ?  413 HOH   A O    1 
HETATM 6566 O O    . HOH   F 4 .   ? 16.058 6.989   2.875   1.00 20.08 ?  414 HOH   A O    1 
HETATM 6567 O O    . HOH   F 4 .   ? 5.167  2.630   5.072   1.00 33.43 ?  415 HOH   A O    1 
HETATM 6568 O O    . HOH   F 4 .   ? 14.122 -23.091 7.436   1.00 20.23 ?  416 HOH   A O    1 
HETATM 6569 O O    . HOH   F 4 .   ? 35.125 -5.248  -3.110  1.00 18.54 ?  417 HOH   A O    1 
HETATM 6570 O O    . HOH   F 4 .   ? 10.458 -13.798 -1.740  1.00 20.03 ?  418 HOH   A O    1 
HETATM 6571 O O    A HOH   F 4 .   ? 15.844 -0.965  5.257   0.66 39.64 ?  419 HOH   A O    1 
HETATM 6572 O O    . HOH   F 4 .   ? 41.664 1.487   4.958   1.00 37.57 ?  420 HOH   A O    1 
HETATM 6573 O O    . HOH   F 4 .   ? 23.988 -20.285 -1.325  1.00 17.75 ?  421 HOH   A O    1 
HETATM 6574 O O    . HOH   F 4 .   ? 32.574 -10.632 3.197   1.00 30.99 ?  422 HOH   A O    1 
HETATM 6575 O O    . HOH   F 4 .   ? 32.768 -4.393  -9.922  1.00 28.53 ?  423 HOH   A O    1 
HETATM 6576 O O    . HOH   F 4 .   ? 22.666 8.231   18.334  1.00 49.52 ?  424 HOH   A O    1 
HETATM 6577 O O    . HOH   F 4 .   ? 16.336 -14.245 20.256  1.00 55.56 ?  425 HOH   A O    1 
HETATM 6578 O O    A HOH   F 4 .   ? 11.110 -0.403  1.922   0.76 32.30 ?  426 HOH   A O    1 
HETATM 6579 O O    . HOH   F 4 .   ? 36.747 -4.987  5.362   1.00 25.18 ?  427 HOH   A O    1 
HETATM 6580 O O    . HOH   F 4 .   ? 6.759  -3.394  12.941  1.00 33.10 ?  428 HOH   A O    1 
HETATM 6581 O O    . HOH   F 4 .   ? 14.481 -24.683 11.522  1.00 36.43 ?  429 HOH   A O    1 
HETATM 6582 O O    . HOH   F 4 .   ? 27.081 -3.161  19.418  1.00 38.35 ?  430 HOH   A O    1 
HETATM 6583 O O    . HOH   F 4 .   ? 45.052 -0.595  2.947   1.00 39.72 ?  431 HOH   A O    1 
HETATM 6584 O O    . HOH   F 4 .   ? 19.163 -10.868 23.974  1.00 79.37 ?  432 HOH   A O    1 
HETATM 6585 O O    . HOH   F 4 .   ? 21.778 -13.899 -8.200  1.00 44.66 ?  433 HOH   A O    1 
HETATM 6586 O O    A HOH   F 4 .   ? 18.904 2.013   -0.766  0.66 13.60 ?  434 HOH   A O    1 
HETATM 6587 O O    . HOH   F 4 .   ? 21.350 -9.174  21.259  1.00 50.05 ?  435 HOH   A O    1 
HETATM 6588 O O    . HOH   F 4 .   ? 20.572 -17.721 24.793  1.00 56.92 ?  436 HOH   A O    1 
HETATM 6589 O O    . HOH   F 4 .   ? 18.594 4.849   -15.135 1.00 57.56 ?  437 HOH   A O    1 
HETATM 6590 O O    . HOH   F 4 .   ? -1.410 -5.092  7.554   1.00 43.84 ?  438 HOH   A O    1 
HETATM 6591 O O    . HOH   F 4 .   ? 23.428 -20.953 1.329   1.00 19.35 ?  439 HOH   A O    1 
HETATM 6592 O O    . HOH   F 4 .   ? 9.565  -16.366 -2.050  1.00 48.13 ?  440 HOH   A O    1 
HETATM 6593 O O    . HOH   F 4 .   ? 11.795 -10.794 17.034  1.00 30.50 ?  441 HOH   A O    1 
HETATM 6594 O O    A HOH   F 4 .   ? 16.299 2.926   -1.455  0.86 24.45 ?  442 HOH   A O    1 
HETATM 6595 O O    . HOH   F 4 .   ? 23.556 -8.026  17.078  1.00 22.72 ?  443 HOH   A O    1 
HETATM 6596 O O    . HOH   F 4 .   ? 37.793 -8.833  -3.412  1.00 24.17 ?  444 HOH   A O    1 
HETATM 6597 O O    . HOH   F 4 .   ? 18.460 -16.039 16.308  1.00 39.03 ?  445 HOH   A O    1 
HETATM 6598 O O    . HOH   F 4 .   ? 34.407 -8.161  -0.476  1.00 30.29 ?  446 HOH   A O    1 
HETATM 6599 O O    . HOH   F 4 .   ? 23.196 7.575   -3.271  1.00 34.97 ?  447 HOH   A O    1 
HETATM 6600 O O    . HOH   F 4 .   ? 30.584 14.765  2.774   1.00 19.13 ?  448 HOH   A O    1 
HETATM 6601 O O    . HOH   F 4 .   ? 31.382 -12.816 -0.002  1.00 19.84 ?  449 HOH   A O    1 
HETATM 6602 O O    A HOH   F 4 .   ? 14.071 -0.360  3.449   0.66 35.98 ?  450 HOH   A O    1 
HETATM 6603 O O    B HOH   F 4 .   ? 20.647 4.324   -2.500  0.34 27.31 ?  451 HOH   A O    1 
HETATM 6604 O O    . HOH   F 4 .   ? 21.584 -14.817 17.876  1.00 54.85 ?  452 HOH   A O    1 
HETATM 6605 O O    . HOH   F 4 .   ? 29.899 -16.027 10.741  1.00 35.34 ?  453 HOH   A O    1 
HETATM 6606 O O    B HOH   F 4 .   ? 18.266 2.125   -0.692  0.34 15.00 ?  454 HOH   A O    1 
HETATM 6607 O O    . HOH   F 4 .   ? 25.432 8.306   -4.811  1.00 30.98 ?  455 HOH   A O    1 
HETATM 6608 O O    B HOH   F 4 .   ? 16.713 6.041   -2.626  0.34 32.36 ?  456 HOH   A O    1 
HETATM 6609 O O    . HOH   F 4 .   ? 32.546 -15.920 10.866  1.00 33.64 ?  457 HOH   A O    1 
HETATM 6610 O O    . HOH   F 4 .   ? 27.833 7.104   -6.581  1.00 39.44 ?  458 HOH   A O    1 
HETATM 6611 O O    . HOH   F 4 .   ? 19.963 -17.369 -5.074  1.00 26.53 ?  459 HOH   A O    1 
HETATM 6612 O O    . HOH   F 4 .   ? 24.855 5.587   20.719  1.00 56.02 ?  460 HOH   A O    1 
HETATM 6613 O O    . HOH   F 4 .   ? 24.655 14.609  7.782   1.00 35.68 ?  461 HOH   A O    1 
HETATM 6614 O O    . HOH   F 4 .   ? 23.269 -22.394 -3.302  1.00 35.06 ?  462 HOH   A O    1 
HETATM 6615 O O    . HOH   F 4 .   ? 18.733 10.815  11.277  1.00 33.13 ?  463 HOH   A O    1 
HETATM 6616 O O    . HOH   F 4 .   ? 18.243 -16.279 -8.843  1.00 43.78 ?  464 HOH   A O    1 
HETATM 6617 O O    . HOH   F 4 .   ? 39.733 -7.074  -3.515  1.00 46.48 ?  465 HOH   A O    1 
HETATM 6618 O O    . HOH   F 4 .   ? 26.957 11.668  -1.359  1.00 34.24 ?  466 HOH   A O    1 
HETATM 6619 O O    . HOH   F 4 .   ? 23.476 13.718  5.507   1.00 19.35 ?  467 HOH   A O    1 
HETATM 6620 O O    . HOH   F 4 .   ? 15.857 -21.587 3.718   1.00 23.89 ?  468 HOH   A O    1 
HETATM 6621 O O    . HOH   F 4 .   ? 11.116 -15.072 -6.082  1.00 36.65 ?  469 HOH   A O    1 
HETATM 6622 O O    . HOH   F 4 .   ? 12.398 1.634   17.293  1.00 41.01 ?  470 HOH   A O    1 
HETATM 6623 O O    . HOH   F 4 .   ? 27.497 -11.402 16.536  1.00 39.68 ?  471 HOH   A O    1 
HETATM 6624 O O    . HOH   F 4 .   ? 28.615 -4.781  -12.314 1.00 42.87 ?  472 HOH   A O    1 
HETATM 6625 O O    . HOH   F 4 .   ? 25.871 10.840  -3.696  1.00 27.14 ?  473 HOH   A O    1 
HETATM 6626 O O    . HOH   F 4 .   ? 11.999 -13.437 16.325  1.00 50.74 ?  474 HOH   A O    1 
HETATM 6627 O O    A HOH   F 4 .   ? 22.003 5.246   -5.852  0.66 28.07 ?  475 HOH   A O    1 
HETATM 6628 O O    . HOH   F 4 .   ? 23.159 11.904  -4.051  1.00 22.00 ?  476 HOH   A O    1 
HETATM 6629 O O    . HOH   F 4 .   ? 35.132 7.474   12.198  1.00 52.80 ?  477 HOH   A O    1 
HETATM 6630 O O    . HOH   F 4 .   ? 28.899 8.952   17.544  1.00 36.22 ?  478 HOH   A O    1 
HETATM 6631 O O    . HOH   F 4 .   ? 15.884 -17.196 -7.012  1.00 34.65 ?  479 HOH   A O    1 
HETATM 6632 O O    . HOH   F 4 .   ? 16.066 -6.830  -11.867 1.00 48.84 ?  480 HOH   A O    1 
HETATM 6633 O O    . HOH   F 4 .   ? 16.831 -20.543 16.141  1.00 30.51 ?  481 HOH   A O    1 
HETATM 6634 O O    . HOH   F 4 .   ? 41.065 -3.968  -0.398  1.00 37.90 ?  482 HOH   A O    1 
HETATM 6635 O O    . HOH   F 4 .   ? 30.911 0.687   19.155  1.00 39.68 ?  483 HOH   A O    1 
HETATM 6636 O O    . HOH   F 4 .   ? 17.487 -18.740 19.753  1.00 49.64 ?  484 HOH   A O    1 
HETATM 6637 O O    . HOH   F 4 .   ? 14.053 -10.335 -10.957 1.00 35.40 ?  485 HOH   A O    1 
HETATM 6638 O O    . HOH   F 4 .   ? 44.485 10.420  -1.661  1.00 32.30 ?  486 HOH   A O    1 
HETATM 6639 O O    . HOH   F 4 .   ? 31.523 -0.580  -10.613 1.00 27.38 ?  487 HOH   A O    1 
HETATM 6640 O O    . HOH   F 4 .   ? 28.784 -7.940  -15.313 1.00 48.58 ?  488 HOH   A O    1 
HETATM 6641 O O    . HOH   F 4 .   ? 23.295 -12.922 19.336  1.00 51.15 ?  489 HOH   A O    1 
HETATM 6642 O O    . HOH   F 4 .   ? 41.720 9.385   -4.008  1.00 32.37 ?  490 HOH   A O    1 
HETATM 6643 O O    . HOH   F 4 .   ? 18.468 -23.169 1.905   1.00 43.60 ?  491 HOH   A O    1 
HETATM 6644 O O    . HOH   F 4 .   ? 39.232 2.389   7.389   1.00 31.86 ?  492 HOH   A O    1 
HETATM 6645 O O    . HOH   F 4 .   ? 20.644 -16.036 -7.466  1.00 31.10 ?  493 HOH   A O    1 
HETATM 6646 O O    . HOH   F 4 .   ? 30.765 5.806   -14.759 1.00 36.17 ?  494 HOH   A O    1 
HETATM 6647 O O    . HOH   F 4 .   ? 13.935 -25.237 8.915   1.00 33.83 ?  495 HOH   A O    1 
HETATM 6648 O O    . HOH   F 4 .   ? 40.552 -0.235  -7.854  1.00 32.37 ?  496 HOH   A O    1 
HETATM 6649 O O    . HOH   F 4 .   ? 25.764 -18.937 -11.901 1.00 39.63 ?  497 HOH   A O    1 
HETATM 6650 O O    . HOH   F 4 .   ? 8.189  -2.987  -5.743  1.00 54.11 ?  498 HOH   A O    1 
HETATM 6651 O O    . HOH   F 4 .   ? 16.225 -23.416 5.827   1.00 29.92 ?  499 HOH   A O    1 
HETATM 6652 O O    . HOH   F 4 .   ? 20.133 -22.396 4.197   1.00 31.34 ?  500 HOH   A O    1 
HETATM 6653 O O    . HOH   F 4 .   ? 30.810 -5.840  -11.896 1.00 52.18 ?  501 HOH   A O    1 
HETATM 6654 O O    . HOH   F 4 .   ? 37.452 -6.652  7.481   1.00 24.00 ?  502 HOH   A O    1 
HETATM 6655 O O    . HOH   F 4 .   ? 23.270 -23.812 1.630   1.00 31.76 ?  503 HOH   A O    1 
HETATM 6656 O O    . HOH   F 4 .   ? 39.583 -0.026  6.566   1.00 29.26 ?  504 HOH   A O    1 
HETATM 6657 O O    . HOH   F 4 .   ? 29.036 14.474  0.837   1.00 48.71 ?  505 HOH   A O    1 
HETATM 6658 O O    . HOH   F 4 .   ? 38.020 14.018  6.683   1.00 49.07 ?  506 HOH   A O    1 
HETATM 6659 O O    . HOH   F 4 .   ? 14.877 8.361   4.946   1.00 39.92 ?  507 HOH   A O    1 
HETATM 6660 O O    . HOH   F 4 .   ? 22.091 -24.039 4.520   1.00 26.39 ?  508 HOH   A O    1 
HETATM 6661 O O    . HOH   F 4 .   ? 36.483 -6.547  10.154  1.00 44.79 ?  509 HOH   A O    1 
HETATM 6662 O O    . HOH   F 4 .   ? 17.369 -7.158  -14.172 1.00 47.35 ?  510 HOH   A O    1 
HETATM 6663 O O    . HOH   F 4 .   ? 24.076 9.098   -7.233  1.00 40.56 ?  511 HOH   A O    1 
HETATM 6664 O O    . HOH   F 4 .   ? 16.278 -21.204 18.741  1.00 36.57 ?  512 HOH   A O    1 
HETATM 6665 O O    . HOH   F 4 .   ? 15.842 -12.400 27.368  1.00 46.32 ?  513 HOH   A O    1 
HETATM 6666 O O    . HOH   F 4 .   ? 14.722 -22.773 19.846  1.00 36.47 ?  514 HOH   A O    1 
HETATM 6667 O O    . HOH   G 4 .   ? 29.921 -22.433 5.503   1.00 20.56 ?  201 HOH   B O    1 
HETATM 6668 O O    . HOH   G 4 .   ? 41.747 -36.030 -17.186 1.00 32.44 ?  202 HOH   B O    1 
HETATM 6669 O O    . HOH   G 4 .   ? 27.785 -29.175 -1.865  1.00 34.60 ?  203 HOH   B O    1 
HETATM 6670 O O    . HOH   G 4 .   ? 30.001 -26.310 4.093   1.00 27.92 ?  204 HOH   B O    1 
HETATM 6671 O O    . HOH   G 4 .   ? 48.158 -6.950  15.506  1.00 33.01 ?  205 HOH   B O    1 
HETATM 6672 O O    . HOH   G 4 .   ? 54.552 -9.449  -8.746  1.00 18.84 ?  206 HOH   B O    1 
HETATM 6673 O O    . HOH   G 4 .   ? 59.228 -18.704 6.835   1.00 37.90 ?  207 HOH   B O    1 
HETATM 6674 O O    . HOH   G 4 .   ? 38.065 -39.479 -0.188  1.00 39.81 ?  208 HOH   B O    1 
HETATM 6675 O O    . HOH   G 4 .   ? 27.881 -41.868 -15.126 1.00 36.18 ?  209 HOH   B O    1 
HETATM 6676 O O    . HOH   G 4 .   ? 49.445 -22.772 -19.788 1.00 48.76 ?  210 HOH   B O    1 
HETATM 6677 O O    . HOH   G 4 .   ? 58.273 -12.898 8.373   1.00 33.36 ?  211 HOH   B O    1 
HETATM 6678 O O    . HOH   G 4 .   ? 47.472 -7.393  -3.913  1.00 41.04 ?  212 HOH   B O    1 
HETATM 6679 O O    . HOH   G 4 .   ? 30.259 -41.050 -8.127  1.00 17.01 ?  213 HOH   B O    1 
HETATM 6680 O O    . HOH   G 4 .   ? 50.246 -3.402  7.119   1.00 34.03 ?  214 HOH   B O    1 
HETATM 6681 O O    . HOH   G 4 .   ? 41.434 -7.764  5.431   1.00 37.75 ?  215 HOH   B O    1 
HETATM 6682 O O    . HOH   G 4 .   ? 56.439 -19.736 7.319   1.00 32.53 ?  216 HOH   B O    1 
HETATM 6683 O O    . HOH   G 4 .   ? 53.062 -13.502 -20.364 1.00 35.87 ?  217 HOH   B O    1 
HETATM 6684 O O    . HOH   G 4 .   ? 44.547 -7.225  2.041   1.00 34.51 ?  218 HOH   B O    1 
HETATM 6685 O O    . HOH   G 4 .   ? 57.843 -24.543 5.086   1.00 39.55 ?  219 HOH   B O    1 
HETATM 6686 O O    . HOH   G 4 .   ? 30.966 -28.783 4.297   1.00 28.17 ?  220 HOH   B O    1 
HETATM 6687 O O    . HOH   G 4 .   ? 29.809 -34.132 -0.408  1.00 35.14 ?  221 HOH   B O    1 
HETATM 6688 O O    . HOH   G 4 .   ? 56.731 -30.824 -7.767  1.00 29.07 ?  222 HOH   B O    1 
HETATM 6689 O O    . HOH   G 4 .   ? 55.540 -16.586 -14.363 1.00 35.91 ?  223 HOH   B O    1 
HETATM 6690 O O    . HOH   G 4 .   ? 34.588 -36.414 -7.211  1.00 18.40 ?  224 HOH   B O    1 
HETATM 6691 O O    . HOH   G 4 .   ? 45.215 -34.946 6.835   1.00 38.78 ?  225 HOH   B O    1 
HETATM 6692 O O    . HOH   G 4 .   ? 50.802 -6.117  0.157   1.00 26.59 ?  226 HOH   B O    1 
HETATM 6693 O O    . HOH   G 4 .   ? 44.982 -43.597 -10.566 1.00 27.81 ?  227 HOH   B O    1 
HETATM 6694 O O    . HOH   G 4 .   ? 37.169 -19.746 -18.122 1.00 40.65 ?  228 HOH   B O    1 
HETATM 6695 O O    . HOH   G 4 .   ? 34.949 -24.669 13.846  1.00 30.58 ?  229 HOH   B O    1 
HETATM 6696 O O    . HOH   G 4 .   ? 57.477 -16.300 -12.243 1.00 18.23 ?  230 HOH   B O    1 
HETATM 6697 O O    . HOH   G 4 .   ? 39.379 -10.898 6.090   1.00 25.12 ?  231 HOH   B O    1 
HETATM 6698 O O    . HOH   G 4 .   ? 41.525 -39.208 -14.915 1.00 22.09 ?  232 HOH   B O    1 
HETATM 6699 O O    . HOH   G 4 .   ? 46.449 -1.584  13.195  1.00 27.27 ?  233 HOH   B O    1 
HETATM 6700 O O    . HOH   G 4 .   ? 41.481 -9.641  13.039  1.00 22.36 ?  234 HOH   B O    1 
HETATM 6701 O O    . HOH   G 4 .   ? 40.625 -16.083 14.083  1.00 24.16 ?  235 HOH   B O    1 
HETATM 6702 O O    . HOH   G 4 .   ? 57.239 -26.838 -7.642  1.00 41.72 ?  236 HOH   B O    1 
HETATM 6703 O O    . HOH   G 4 .   ? 35.164 -8.019  -2.986  1.00 18.36 ?  237 HOH   B O    1 
HETATM 6704 O O    . HOH   G 4 .   ? 25.454 -25.929 -1.300  1.00 32.91 ?  238 HOH   B O    1 
HETATM 6705 O O    . HOH   G 4 .   ? 51.714 -6.510  4.370   1.00 20.06 ?  239 HOH   B O    1 
HETATM 6706 O O    . HOH   G 4 .   ? 44.585 -27.808 -0.713  1.00 22.39 ?  240 HOH   B O    1 
HETATM 6707 O O    . HOH   G 4 .   ? 32.836 -43.826 -11.348 1.00 20.90 ?  241 HOH   B O    1 
HETATM 6708 O O    . HOH   G 4 .   ? 39.580 -11.153 0.331   1.00 17.02 ?  242 HOH   B O    1 
HETATM 6709 O O    . HOH   G 4 .   ? 50.813 -13.003 -0.486  1.00 11.89 ?  243 HOH   B O    1 
HETATM 6710 O O    . HOH   G 4 .   ? 38.536 -11.066 -2.276  1.00 19.22 ?  244 HOH   B O    1 
HETATM 6711 O O    . HOH   G 4 .   ? 42.640 -25.393 2.637   1.00 15.38 ?  245 HOH   B O    1 
HETATM 6712 O O    . HOH   G 4 .   ? 36.030 -43.378 -8.456  1.00 35.50 ?  246 HOH   B O    1 
HETATM 6713 O O    . HOH   G 4 .   ? 43.118 -43.266 -8.243  1.00 28.31 ?  247 HOH   B O    1 
HETATM 6714 O O    . HOH   G 4 .   ? 41.927 -23.542 9.284   1.00 18.19 ?  248 HOH   B O    1 
HETATM 6715 O O    . HOH   G 4 .   ? 28.467 -19.718 -13.134 1.00 24.46 ?  249 HOH   B O    1 
HETATM 6716 O O    . HOH   G 4 .   ? 42.715 -22.887 3.857   1.00 12.13 ?  250 HOH   B O    1 
HETATM 6717 O O    . HOH   G 4 .   ? 48.627 -36.606 -15.550 1.00 45.10 ?  251 HOH   B O    1 
HETATM 6718 O O    . HOH   G 4 .   ? 57.697 -24.407 -3.858  1.00 21.29 ?  252 HOH   B O    1 
HETATM 6719 O O    . HOH   G 4 .   ? 31.845 -17.960 -14.504 1.00 31.01 ?  253 HOH   B O    1 
HETATM 6720 O O    . HOH   G 4 .   ? 40.402 -12.778 -11.534 1.00 15.52 ?  254 HOH   B O    1 
HETATM 6721 O O    . HOH   G 4 .   ? 58.267 -10.649 -4.073  1.00 20.23 ?  255 HOH   B O    1 
HETATM 6722 O O    . HOH   G 4 .   ? 29.762 -25.230 -10.786 1.00 16.85 ?  256 HOH   B O    1 
HETATM 6723 O O    . HOH   G 4 .   ? 34.317 -18.486 11.449  1.00 25.67 ?  257 HOH   B O    1 
HETATM 6724 O O    . HOH   G 4 .   ? 43.199 -32.393 -17.089 1.00 24.35 ?  258 HOH   B O    1 
HETATM 6725 O O    . HOH   G 4 .   ? 48.045 -24.550 -17.822 1.00 31.63 ?  259 HOH   B O    1 
HETATM 6726 O O    . HOH   G 4 .   ? 27.159 -31.845 -9.957  1.00 21.02 ?  260 HOH   B O    1 
HETATM 6727 O O    . HOH   G 4 .   ? 30.928 -15.730 2.663   1.00 13.74 ?  261 HOH   B O    1 
HETATM 6728 O O    . HOH   G 4 .   ? 51.596 -13.828 10.963  1.00 27.34 ?  262 HOH   B O    1 
HETATM 6729 O O    . HOH   G 4 .   ? 51.040 -40.007 -8.248  1.00 33.21 ?  263 HOH   B O    1 
HETATM 6730 O O    . HOH   G 4 .   ? 30.589 -42.300 -10.649 1.00 29.51 ?  264 HOH   B O    1 
HETATM 6731 O O    . HOH   G 4 .   ? 28.524 -30.952 -14.768 1.00 30.69 ?  265 HOH   B O    1 
HETATM 6732 O O    . HOH   G 4 .   ? 57.026 -8.629  8.363   1.00 19.61 ?  266 HOH   B O    1 
HETATM 6733 O O    . HOH   G 4 .   ? 46.929 -29.626 9.798   1.00 31.09 ?  267 HOH   B O    1 
HETATM 6734 O O    . HOH   G 4 .   ? 48.096 -22.793 5.827   1.00 17.52 ?  268 HOH   B O    1 
HETATM 6735 O O    . HOH   G 4 .   ? 49.393 -28.742 -6.913  1.00 15.93 ?  269 HOH   B O    1 
HETATM 6736 O O    . HOH   G 4 .   ? 57.547 -9.245  1.391   1.00 19.44 ?  270 HOH   B O    1 
HETATM 6737 O O    . HOH   G 4 .   ? 38.985 -11.959 12.352  1.00 33.26 ?  271 HOH   B O    1 
HETATM 6738 O O    . HOH   G 4 .   ? 56.235 -23.594 -14.743 1.00 27.47 ?  272 HOH   B O    1 
HETATM 6739 O O    . HOH   G 4 .   ? 42.421 -9.910  9.348   1.00 21.01 ?  273 HOH   B O    1 
HETATM 6740 O O    . HOH   G 4 .   ? 34.997 -33.346 -19.214 1.00 35.22 ?  274 HOH   B O    1 
HETATM 6741 O O    . HOH   G 4 .   ? 43.445 -15.823 -12.178 1.00 14.60 ?  275 HOH   B O    1 
HETATM 6742 O O    . HOH   G 4 .   ? 49.853 -0.502  10.207  1.00 29.55 ?  276 HOH   B O    1 
HETATM 6743 O O    . HOH   G 4 .   ? 57.263 -12.095 12.274  1.00 35.57 ?  277 HOH   B O    1 
HETATM 6744 O O    . HOH   G 4 .   ? 46.678 -31.284 -4.808  1.00 20.61 ?  278 HOH   B O    1 
HETATM 6745 O O    . HOH   G 4 .   ? 28.294 -34.369 -9.388  1.00 18.75 ?  279 HOH   B O    1 
HETATM 6746 O O    . HOH   G 4 .   ? 28.020 -22.901 -7.997  1.00 17.66 ?  280 HOH   B O    1 
HETATM 6747 O O    . HOH   G 4 .   ? 34.542 -12.792 2.619   1.00 24.27 ?  281 HOH   B O    1 
HETATM 6748 O O    . HOH   G 4 .   ? 42.480 -34.716 3.790   1.00 27.16 ?  282 HOH   B O    1 
HETATM 6749 O O    . HOH   G 4 .   ? 48.483 -25.087 3.094   1.00 13.74 ?  283 HOH   B O    1 
HETATM 6750 O O    . HOH   G 4 .   ? 48.794 -20.051 5.909   1.00 14.18 ?  284 HOH   B O    1 
HETATM 6751 O O    . HOH   G 4 .   ? 47.127 -34.044 -4.649  1.00 17.95 ?  285 HOH   B O    1 
HETATM 6752 O O    . HOH   G 4 .   ? 42.426 -9.976  -14.895 1.00 34.96 ?  286 HOH   B O    1 
HETATM 6753 O O    . HOH   G 4 .   ? 42.911 -20.270 -20.704 1.00 39.69 ?  287 HOH   B O    1 
HETATM 6754 O O    . HOH   G 4 .   ? 36.933 -12.786 -1.528  1.00 25.59 ?  288 HOH   B O    1 
HETATM 6755 O O    . HOH   G 4 .   ? 33.583 -15.338 -13.930 1.00 22.08 ?  289 HOH   B O    1 
HETATM 6756 O O    . HOH   G 4 .   ? 52.626 -10.404 12.989  1.00 22.99 ?  290 HOH   B O    1 
HETATM 6757 O O    . HOH   G 4 .   ? 27.618 -26.709 -15.599 1.00 32.39 ?  291 HOH   B O    1 
HETATM 6758 O O    . HOH   G 4 .   ? 41.216 -5.500  11.541  1.00 45.85 ?  292 HOH   B O    1 
HETATM 6759 O O    . HOH   G 4 .   ? 37.596 -18.121 13.102  1.00 30.65 ?  293 HOH   B O    1 
HETATM 6760 O O    . HOH   G 4 .   ? 45.377 -33.420 -15.976 1.00 24.08 ?  294 HOH   B O    1 
HETATM 6761 O O    . HOH   G 4 .   ? 52.626 -35.710 -8.631  1.00 29.47 ?  295 HOH   B O    1 
HETATM 6762 O O    . HOH   G 4 .   ? 44.699 -27.495 2.008   1.00 15.52 ?  296 HOH   B O    1 
HETATM 6763 O O    . HOH   G 4 .   ? 59.860 -15.330 8.168   1.00 32.83 ?  297 HOH   B O    1 
HETATM 6764 O O    . HOH   G 4 .   ? 49.986 -24.720 5.804   1.00 34.99 ?  298 HOH   B O    1 
HETATM 6765 O O    . HOH   G 4 .   ? 42.823 -12.271 -18.523 1.00 28.83 ?  299 HOH   B O    1 
HETATM 6766 O O    . HOH   G 4 .   ? 51.288 -37.626 -9.645  1.00 26.58 ?  300 HOH   B O    1 
HETATM 6767 O O    . HOH   G 4 .   ? 62.769 -13.612 4.759   1.00 28.98 ?  301 HOH   B O    1 
HETATM 6768 O O    . HOH   G 4 .   ? 35.144 -33.591 4.575   1.00 31.29 ?  302 HOH   B O    1 
HETATM 6769 O O    . HOH   G 4 .   ? 62.890 -20.261 -0.833  1.00 37.86 ?  303 HOH   B O    1 
HETATM 6770 O O    . HOH   G 4 .   ? 37.392 -35.689 7.241   1.00 34.18 ?  304 HOH   B O    1 
HETATM 6771 O O    . HOH   G 4 .   ? 45.938 -40.447 -3.646  1.00 29.80 ?  305 HOH   B O    1 
HETATM 6772 O O    . HOH   G 4 .   ? 44.090 -29.370 -4.654  1.00 23.83 ?  306 HOH   B O    1 
HETATM 6773 O O    . HOH   G 4 .   ? 26.017 -21.502 -3.492  1.00 17.27 ?  307 HOH   B O    1 
HETATM 6774 O O    . HOH   G 4 .   ? 32.871 -34.632 -5.869  1.00 17.06 ?  308 HOH   B O    1 
HETATM 6775 O O    . HOH   G 4 .   ? 40.319 -10.855 -9.534  1.00 17.77 ?  309 HOH   B O    1 
HETATM 6776 O O    . HOH   G 4 .   ? 51.757 -6.008  -7.938  1.00 44.86 ?  310 HOH   B O    1 
HETATM 6777 O O    . HOH   G 4 .   ? 53.513 -30.244 4.540   1.00 19.08 ?  311 HOH   B O    1 
HETATM 6778 O O    . HOH   G 4 .   ? 38.419 -12.782 7.920   1.00 18.73 ?  312 HOH   B O    1 
HETATM 6779 O O    . HOH   G 4 .   ? 37.910 -10.258 -10.753 1.00 17.53 ?  313 HOH   B O    1 
HETATM 6780 O O    . HOH   G 4 .   ? 37.102 -30.660 -20.989 1.00 32.96 ?  314 HOH   B O    1 
HETATM 6781 O O    . HOH   G 4 .   ? 53.140 -16.052 -12.752 1.00 27.21 ?  315 HOH   B O    1 
HETATM 6782 O O    . HOH   G 4 .   ? 41.835 -8.095  1.377   1.00 24.63 ?  316 HOH   B O    1 
HETATM 6783 O O    . HOH   G 4 .   ? 52.603 -29.277 -13.068 1.00 24.93 ?  317 HOH   B O    1 
HETATM 6784 O O    . HOH   G 4 .   ? 43.614 -15.391 18.133  1.00 30.09 ?  318 HOH   B O    1 
HETATM 6785 O O    . HOH   G 4 .   ? 48.213 -32.648 -16.659 1.00 41.21 ?  319 HOH   B O    1 
HETATM 6786 O O    . HOH   G 4 .   ? 43.285 -21.451 10.674  1.00 16.44 ?  320 HOH   B O    1 
HETATM 6787 O O    . HOH   G 4 .   ? 26.401 -21.056 -6.229  1.00 17.03 ?  321 HOH   B O    1 
HETATM 6788 O O    . HOH   G 4 .   ? 53.740 -12.577 -22.277 1.00 34.81 ?  322 HOH   B O    1 
HETATM 6789 O O    . HOH   G 4 .   ? 44.687 -24.631 9.549   1.00 20.89 ?  323 HOH   B O    1 
HETATM 6790 O O    . HOH   G 4 .   ? 33.705 -31.136 11.061  1.00 36.18 ?  324 HOH   B O    1 
HETATM 6791 O O    . HOH   G 4 .   ? 48.686 -12.026 -14.168 1.00 26.98 ?  325 HOH   B O    1 
HETATM 6792 O O    . HOH   G 4 .   ? 44.168 -1.775  7.606   1.00 45.59 ?  326 HOH   B O    1 
HETATM 6793 O O    . HOH   G 4 .   ? 51.441 -32.994 -10.834 1.00 39.37 ?  327 HOH   B O    1 
HETATM 6794 O O    . HOH   G 4 .   ? 59.967 -17.340 -10.545 1.00 35.07 ?  328 HOH   B O    1 
HETATM 6795 O O    . HOH   G 4 .   ? 36.807 -12.410 4.270   1.00 18.27 ?  329 HOH   B O    1 
HETATM 6796 O O    . HOH   G 4 .   ? 38.420 -9.374  -13.263 1.00 27.98 ?  330 HOH   B O    1 
HETATM 6797 O O    . HOH   G 4 .   ? 57.629 -21.989 3.367   1.00 31.41 ?  331 HOH   B O    1 
HETATM 6798 O O    . HOH   G 4 .   ? 43.177 -34.639 0.096   1.00 21.99 ?  332 HOH   B O    1 
HETATM 6799 O O    . HOH   G 4 .   ? 47.273 -24.508 8.164   1.00 27.08 ?  333 HOH   B O    1 
HETATM 6800 O O    . HOH   G 4 .   ? 41.339 -24.532 15.802  1.00 45.39 ?  334 HOH   B O    1 
HETATM 6801 O O    . HOH   G 4 .   ? 45.795 -36.339 -16.071 1.00 37.25 ?  335 HOH   B O    1 
HETATM 6802 O O    . HOH   G 4 .   ? 42.864 -43.512 -14.368 1.00 42.35 ?  336 HOH   B O    1 
HETATM 6803 O O    . HOH   G 4 .   ? 27.838 -14.716 -9.500  1.00 35.40 ?  337 HOH   B O    1 
HETATM 6804 O O    . HOH   G 4 .   ? 47.549 -27.481 2.017   1.00 15.00 ?  338 HOH   B O    1 
HETATM 6805 O O    . HOH   G 4 .   ? 39.618 -23.466 -20.354 1.00 36.68 ?  339 HOH   B O    1 
HETATM 6806 O O    . HOH   G 4 .   ? 46.897 -19.916 12.258  1.00 32.48 ?  340 HOH   B O    1 
HETATM 6807 O O    . HOH   G 4 .   ? 37.115 -15.141 -16.526 1.00 37.89 ?  341 HOH   B O    1 
HETATM 6808 O O    . HOH   G 4 .   ? 28.907 -42.958 -12.345 1.00 40.72 ?  342 HOH   B O    1 
HETATM 6809 O O    . HOH   G 4 .   ? 38.503 -12.248 -16.282 1.00 43.42 ?  343 HOH   B O    1 
HETATM 6810 O O    . HOH   G 4 .   ? 37.102 -45.310 -9.682  1.00 38.79 ?  344 HOH   B O    1 
HETATM 6811 O O    . HOH   G 4 .   ? 33.067 -14.681 1.068   1.00 19.58 ?  345 HOH   B O    1 
HETATM 6812 O O    . HOH   G 4 .   ? 39.841 -44.315 -11.203 1.00 41.14 ?  346 HOH   B O    1 
HETATM 6813 O O    . HOH   G 4 .   ? 34.629 -10.325 7.571   1.00 23.79 ?  347 HOH   B O    1 
HETATM 6814 O O    . HOH   G 4 .   ? 40.443 -43.503 -9.151  1.00 26.29 ?  348 HOH   B O    1 
HETATM 6815 O O    . HOH   G 4 .   ? 33.849 -9.344  -8.830  1.00 31.14 ?  349 HOH   B O    1 
HETATM 6816 O O    . HOH   G 4 .   ? 27.844 -26.638 -0.583  1.00 30.85 ?  350 HOH   B O    1 
HETATM 6817 O O    . HOH   G 4 .   ? 23.360 -23.710 6.835   1.00 34.53 ?  351 HOH   B O    1 
HETATM 6818 O O    . HOH   G 4 .   ? 55.749 -8.273  10.770  1.00 24.42 ?  352 HOH   B O    1 
HETATM 6819 O O    . HOH   G 4 .   ? 38.566 -22.362 15.076  1.00 43.57 ?  353 HOH   B O    1 
HETATM 6820 O O    . HOH   G 4 .   ? 44.192 -37.417 -17.789 1.00 34.46 ?  354 HOH   B O    1 
HETATM 6821 O O    . HOH   G 4 .   ? 62.653 -20.131 -4.902  1.00 48.12 ?  355 HOH   B O    1 
HETATM 6822 O O    . HOH   G 4 .   ? 34.106 -7.821  11.476  1.00 39.28 ?  356 HOH   B O    1 
HETATM 6823 O O    . HOH   G 4 .   ? 56.681 -7.280  2.970   1.00 28.69 ?  357 HOH   B O    1 
HETATM 6824 O O    . HOH   G 4 .   ? 36.227 -8.498  -9.734  1.00 33.95 ?  358 HOH   B O    1 
HETATM 6825 O O    . HOH   G 4 .   ? 61.541 -19.908 1.695   1.00 34.69 ?  359 HOH   B O    1 
HETATM 6826 O O    . HOH   G 4 .   ? 56.979 -21.577 -16.439 1.00 39.24 ?  360 HOH   B O    1 
HETATM 6827 O O    . HOH   G 4 .   ? 27.206 -25.954 -11.374 1.00 34.11 ?  361 HOH   B O    1 
HETATM 6828 O O    . HOH   G 4 .   ? 40.330 -8.835  9.852   1.00 39.54 ?  362 HOH   B O    1 
HETATM 6829 O O    . HOH   G 4 .   ? 43.241 -12.699 -21.239 1.00 40.21 ?  363 HOH   B O    1 
HETATM 6830 O O    . HOH   G 4 .   ? 40.304 -11.355 -13.964 1.00 32.76 ?  364 HOH   B O    1 
HETATM 6831 O O    . HOH   G 4 .   ? 32.623 -23.651 14.081  1.00 40.43 ?  365 HOH   B O    1 
HETATM 6832 O O    . HOH   G 4 .   ? 59.083 -10.506 9.156   1.00 39.97 ?  366 HOH   B O    1 
HETATM 6833 O O    . HOH   G 4 .   ? 48.417 -26.480 8.783   1.00 43.90 ?  367 HOH   B O    1 
HETATM 6834 O O    . HOH   G 4 .   ? 36.284 -8.651  8.917   1.00 34.93 ?  368 HOH   B O    1 
HETATM 6835 O O    . HOH   G 4 .   ? 39.954 -7.032  7.775   1.00 40.44 ?  369 HOH   B O    1 
HETATM 6836 O O    . HOH   G 4 .   ? 54.309 -5.789  2.886   1.00 36.23 ?  370 HOH   B O    1 
HETATM 6837 O O    . HOH   G 4 .   ? 56.082 -7.792  -0.601  1.00 33.89 ?  371 HOH   B O    1 
HETATM 6838 O O    . HOH   G 4 .   ? 41.843 -10.022 -17.510 1.00 54.44 ?  372 HOH   B O    1 
HETATM 6839 O O    . HOH   G 4 .   ? 52.102 -12.943 13.339  1.00 27.28 ?  373 HOH   B O    1 
HETATM 6840 O O    . HOH   G 4 .   ? 63.075 -12.397 6.968   1.00 37.67 ?  374 HOH   B O    1 
HETATM 6841 O O    . HOH   G 4 .   ? 38.115 -10.555 10.032  1.00 28.36 ?  375 HOH   B O    1 
HETATM 6842 O O    . HOH   G 4 .   ? 36.608 -22.860 13.301  1.00 28.54 ?  376 HOH   B O    1 
HETATM 6843 O O    . HOH   G 4 .   ? 41.886 -6.785  -4.883  1.00 47.63 ?  377 HOH   B O    1 
HETATM 6844 O O    . HOH   G 4 .   ? 40.246 -7.696  3.169   1.00 40.20 ?  378 HOH   B O    1 
HETATM 6845 O O    . HOH   G 4 .   ? 44.127 -5.624  -3.503  1.00 40.49 ?  379 HOH   B O    1 
HETATM 6846 O O    . HOH   G 4 .   ? 42.687 -17.106 -23.199 1.00 43.41 ?  380 HOH   B O    1 
HETATM 6847 O O    . HOH   G 4 .   ? 52.950 -29.923 7.211   1.00 23.53 ?  381 HOH   B O    1 
HETATM 6848 O O    . HOH   G 4 .   ? 46.787 -5.419  2.885   1.00 38.73 ?  382 HOH   B O    1 
HETATM 6849 O O    . HOH   G 4 .   ? 39.656 -14.088 15.704  1.00 48.04 ?  383 HOH   B O    1 
HETATM 6850 O O    . HOH   G 4 .   ? 60.536 -22.349 2.864   1.00 45.96 ?  384 HOH   B O    1 
HETATM 6851 O O    . HOH   G 4 .   ? 23.987 -20.903 -7.641  1.00 28.64 ?  385 HOH   B O    1 
HETATM 6852 O O    . HOH   G 4 .   ? 35.315 -20.355 13.289  1.00 31.90 ?  386 HOH   B O    1 
HETATM 6853 O O    . HOH   G 4 .   ? 41.045 -9.757  15.821  1.00 49.17 ?  387 HOH   B O    1 
HETATM 6854 O O    . HOH   G 4 .   ? 35.439 -33.725 7.340   1.00 42.34 ?  388 HOH   B O    1 
HETATM 6855 O O    . HOH   G 4 .   ? 40.794 -6.624  -0.836  1.00 26.02 ?  389 HOH   B O    1 
HETATM 6856 O O    . HOH   G 4 .   ? 44.188 -31.816 -3.834  1.00 35.52 ?  390 HOH   B O    1 
HETATM 6857 O O    . HOH   G 4 .   ? 28.013 -27.089 2.316   1.00 31.44 ?  391 HOH   B O    1 
HETATM 6858 O O    . HOH   G 4 .   ? 26.673 -27.963 -13.420 1.00 36.81 ?  392 HOH   B O    1 
HETATM 6859 O O    . HOH   G 4 .   ? 24.666 -20.592 -10.482 1.00 41.28 ?  393 HOH   B O    1 
HETATM 6860 O O    . HOH   G 4 .   ? 50.715 -30.896 8.645   1.00 28.99 ?  394 HOH   B O    1 
HETATM 6861 O O    . HOH   G 4 .   ? 34.448 -33.501 9.589   1.00 34.23 ?  395 HOH   B O    1 
HETATM 6862 O O    . HOH   G 4 .   ? 26.873 -30.687 -12.622 1.00 28.44 ?  396 HOH   B O    1 
HETATM 6863 O O    . HOH   G 4 .   ? 57.681 -6.517  -2.324  1.00 33.78 ?  397 HOH   B O    1 
HETATM 6864 O O    . HOH   G 4 .   ? 45.749 -20.118 15.258  1.00 46.38 ?  398 HOH   B O    1 
HETATM 6865 O O    . HOH   G 4 .   ? 40.887 -11.799 -22.317 1.00 42.02 ?  399 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   ? 0.7618 0.7635 0.8098 -0.0002 -0.0213 0.0774  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7593 0.7607 0.7923 -0.0017 -0.0166 0.0568  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7588 0.7608 0.8031 -0.0015 -0.0201 0.0772  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7563 0.7581 0.7868 -0.0027 -0.0162 0.0581  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.7417 0.7466 0.7775 -0.0066 -0.0202 0.0786  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.7405 0.7448 0.7675 -0.0074 -0.0179 0.0675  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.7446 0.7496 0.7893 -0.0054 -0.0220 0.0813  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.7435 0.7475 0.7775 -0.0065 -0.0190 0.0684  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7696 0.7699 0.8153 0.0012  -0.0182 0.0752  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7660 0.7663 0.7952 -0.0001 -0.0140 0.0512  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7732 0.7726 0.8171 0.0023  -0.0177 0.0745  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7692 0.7687 0.7961 0.0009  -0.0133 0.0488  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7734 0.7734 0.8175 0.0019  -0.0178 0.0749  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7695 0.7694 0.7965 0.0008  -0.0134 0.0490  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.7182 0.7263 0.7320 -0.0137 -0.0175 0.0759  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.6692 0.6847 0.6428 -0.0280 -0.0130 0.0785  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.6038 0.6383 0.5831 -0.0479 0.0070  0.0547  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.6050 0.6396 0.5843 -0.0487 0.0053  0.0586  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.6823 0.6877 0.6043 -0.0237 -0.0261 0.1038  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.6916 0.6888 0.5674 -0.0206 -0.0386 0.1253  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.6955 0.6893 0.5527 -0.0201 -0.0442 0.1326  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.6938 0.6887 0.5621 -0.0186 -0.0423 0.1344  4   ASN   A ND2 
46   N N   A SER   A 5   ? 0.5695 0.6137 0.5460 -0.0589 0.0184  0.0412  5   SER   A N   
47   N N   B SER   A 5   ? 0.5691 0.6125 0.5510 -0.0577 0.0183  0.0409  5   SER   A N   
48   C CA  A SER   A 5   ? 0.5331 0.5872 0.5072 -0.0706 0.0342  0.0291  5   SER   A CA  
49   C CA  B SER   A 5   ? 0.5323 0.5848 0.5151 -0.0683 0.0326  0.0290  5   SER   A CA  
50   C C   A SER   A 5   ? 0.4925 0.5522 0.4556 -0.0803 0.0541  0.0275  5   SER   A C   
51   C C   B SER   A 5   ? 0.4918 0.5509 0.4643 -0.0794 0.0524  0.0278  5   SER   A C   
52   O O   A SER   A 5   ? 0.4951 0.5544 0.4409 -0.0785 0.0563  0.0218  5   SER   A O   
53   O O   B SER   A 5   ? 0.4937 0.5528 0.4590 -0.0784 0.0525  0.0227  5   SER   A O   
54   C CB  A SER   A 5   ? 0.5366 0.5942 0.5249 -0.0724 0.0307  0.0213  5   SER   A CB  
55   C CB  B SER   A 5   ? 0.5351 0.5895 0.5305 -0.0679 0.0283  0.0215  5   SER   A CB  
56   O OG  A SER   A 5   ? 0.5385 0.5980 0.5338 -0.0736 0.0283  0.0167  5   SER   A OG  
57   O OG  B SER   A 5   ? 0.5365 0.5920 0.5379 -0.0679 0.0257  0.0173  5   SER   A OG  
68   N N   . PHE   A 6   ? 0.4486 0.5140 0.4150 -0.0912 0.0734  0.0360  6   PHE   A N   
69   C CA  . PHE   A 6   ? 0.3659 0.4378 0.3363 -0.1094 0.1014  0.0592  6   PHE   A CA  
70   C C   . PHE   A 6   ? 0.3473 0.4273 0.3414 -0.1153 0.1166  0.0609  6   PHE   A C   
71   O O   . PHE   A 6   ? 0.3504 0.4295 0.3650 -0.1209 0.1070  0.0729  6   PHE   A O   
72   C CB  . PHE   A 6   ? 0.3182 0.3785 0.2912 -0.1053 0.0835  0.0657  6   PHE   A CB  
73   C CG  . PHE   A 6   ? 0.2777 0.3320 0.2650 -0.0880 0.0650  0.0534  6   PHE   A CG  
74   C CD1 . PHE   A 6   ? 0.2581 0.3137 0.2556 -0.0783 0.0502  0.0469  6   PHE   A CD1 
75   C CD2 . PHE   A 6   ? 0.2755 0.3177 0.2757 -0.0649 0.0560  0.0397  6   PHE   A CD2 
76   C CE1 . PHE   A 6   ? 0.2505 0.2990 0.2598 -0.0746 0.0476  0.0444  6   PHE   A CE1 
77   C CE2 . PHE   A 6   ? 0.2679 0.3057 0.2838 -0.0584 0.0501  0.0337  6   PHE   A CE2 
78   C CZ  . PHE   A 6   ? 0.2573 0.2964 0.2728 -0.0657 0.0456  0.0345  6   PHE   A CZ  
89   N N   . SER   A 7   ? 0.3249 0.4105 0.3390 -0.1119 0.1306  0.0472  7   SER   A N   
90   C CA  . SER   A 7   ? 0.3197 0.4011 0.3595 -0.0962 0.1239  0.0163  7   SER   A CA  
91   C C   . SER   A 7   ? 0.2855 0.3646 0.3378 -0.0886 0.1252  0.0125  7   SER   A C   
92   O O   . SER   A 7   ? 0.2900 0.3543 0.3339 -0.0939 0.1189  0.0094  7   SER   A O   
93   C CB  . SER   A 7   ? 0.3460 0.4242 0.3888 -0.0860 0.1216  0.0080  7   SER   A CB  
94   O OG  . SER   A 7   ? 0.3584 0.4375 0.4243 -0.0753 0.1106  -0.0027 7   SER   A OG  
100  N N   . GLY   A 8   ? 0.2593 0.3392 0.3363 -0.0794 0.1182  0.0095  8   GLY   A N   
101  C CA  . GLY   A 8   ? 0.2403 0.3091 0.3354 -0.0621 0.1119  0.0147  8   GLY   A CA  
102  C C   . GLY   A 8   ? 0.2178 0.2853 0.3274 -0.0453 0.0936  0.0222  8   GLY   A C   
103  O O   . GLY   A 8   ? 0.2148 0.2883 0.3572 -0.0344 0.0838  -0.0048 8   GLY   A O   
107  N N   . TYR   A 9   ? 0.1969 0.2625 0.3071 -0.0291 0.0839  0.0497  9   TYR   A N   
108  C CA  . TYR   A 9   ? 0.1866 0.2394 0.2830 -0.0257 0.0609  0.0613  9   TYR   A CA  
109  C C   . TYR   A 9   ? 0.1893 0.2175 0.2784 -0.0209 0.0603  0.0818  9   TYR   A C   
110  O O   . TYR   A 9   ? 0.2194 0.2458 0.3036 -0.0279 0.0528  0.0838  9   TYR   A O   
111  C CB  . TYR   A 9   ? 0.1776 0.2456 0.2734 -0.0143 0.0540  0.0533  9   TYR   A CB  
112  C CG  . TYR   A 9   ? 0.1687 0.2476 0.2657 -0.0050 0.0609  0.0365  9   TYR   A CG  
113  C CD1 . TYR   A 9   ? 0.1750 0.2547 0.2740 -0.0153 0.0667  0.0254  9   TYR   A CD1 
114  C CD2 . TYR   A 9   ? 0.1653 0.2312 0.2533 -0.0010 0.0505  0.0387  9   TYR   A CD2 
115  C CE1 . TYR   A 9   ? 0.1838 0.2542 0.2812 -0.0198 0.0646  0.0090  9   TYR   A CE1 
116  C CE2 . TYR   A 9   ? 0.1652 0.2355 0.2522 -0.0041 0.0588  0.0215  9   TYR   A CE2 
117  C CZ  . TYR   A 9   ? 0.1761 0.2473 0.2756 -0.0213 0.0694  0.0103  9   TYR   A CZ  
118  O OH  . TYR   A 9   ? 0.1854 0.2596 0.2981 -0.0385 0.0735  0.0001  9   TYR   A OH  
128  N N   . LEU   A 10  ? 0.1769 0.1987 0.2873 -0.0123 0.0503  0.0746  10  LEU   A N   
129  C CA  . LEU   A 10  ? 0.1659 0.1991 0.2839 -0.0194 0.0461  0.0764  10  LEU   A CA  
130  C C   . LEU   A 10  ? 0.1587 0.1857 0.2710 -0.0251 0.0307  0.0688  10  LEU   A C   
131  O O   . LEU   A 10  ? 0.1611 0.1701 0.2590 -0.0251 0.0381  0.0583  10  LEU   A O   
132  C CB  . LEU   A 10  ? 0.1689 0.2146 0.3124 -0.0195 0.0345  0.0906  10  LEU   A CB  
133  C CG  . LEU   A 10  ? 0.1956 0.2289 0.3438 -0.0120 0.0124  0.1039  10  LEU   A CG  
134  C CD1 . LEU   A 10  ? 0.2102 0.2372 0.3721 -0.0202 0.0102  0.0942  10  LEU   A CD1 
135  C CD2 . LEU   A 10  ? 0.2190 0.2560 0.3688 -0.0088 0.0188  0.0872  10  LEU   A CD2 
147  N N   . LYS   A 11  ? 0.1639 0.1834 0.2759 -0.0296 0.0237  0.0755  11  LYS   A N   
148  C CA  . LYS   A 11  ? 0.1647 0.1786 0.2667 -0.0370 0.0126  0.0743  11  LYS   A CA  
149  C C   . LYS   A 11  ? 0.1521 0.1919 0.2670 -0.0440 0.0153  0.0639  11  LYS   A C   
150  O O   . LYS   A 11  ? 0.1573 0.2333 0.3040 -0.0683 0.0213  0.0506  11  LYS   A O   
151  C CB  . LYS   A 11  ? 0.1793 0.1687 0.2447 -0.0369 0.0104  0.0498  11  LYS   A CB  
152  C CG  . LYS   A 11  ? 0.1978 0.1661 0.2241 -0.0361 0.0279  0.0545  11  LYS   A CG  
153  C CD  . LYS   A 11  ? 0.2201 0.1702 0.2158 -0.0322 0.0219  0.0470  11  LYS   A CD  
154  C CE  . LYS   A 11  ? 0.2279 0.1687 0.2079 -0.0279 0.0201  0.0478  11  LYS   A CE  
155  N NZ  . LYS   A 11  ? 0.2225 0.1673 0.2215 -0.0238 0.0073  0.0460  11  LYS   A NZ  
169  N N   . LEU   A 12  ? 0.1373 0.1858 0.2601 -0.0334 0.0105  0.0580  12  LEU   A N   
170  C CA  . LEU   A 12  ? 0.1418 0.2040 0.2587 -0.0323 0.0035  0.0743  12  LEU   A CA  
171  C C   . LEU   A 12  ? 0.1483 0.1968 0.2396 -0.0385 0.0041  0.0689  12  LEU   A C   
172  O O   . LEU   A 12  ? 0.1498 0.2044 0.2459 -0.0343 0.0046  0.0588  12  LEU   A O   
173  C CB  . LEU   A 12  ? 0.1491 0.2138 0.2823 -0.0283 0.0016  0.0879  12  LEU   A CB  
174  C CG  . LEU   A 12  ? 0.1613 0.2232 0.3188 -0.0157 0.0137  0.0999  12  LEU   A CG  
175  C CD1 . LEU   A 12  ? 0.1805 0.2298 0.3235 -0.0065 0.0234  0.1070  12  LEU   A CD1 
176  C CD2 . LEU   A 12  ? 0.1667 0.2332 0.3522 -0.0153 0.0033  0.0910  12  LEU   A CD2 
188  N N   . THR   A 13  ? 0.1456 0.1884 0.2363 -0.0368 0.0036  0.0515  13  THR   A N   
189  C CA  . THR   A 13  ? 0.1502 0.1813 0.2400 -0.0381 0.0125  0.0430  13  THR   A CA  
190  C C   . THR   A 13  ? 0.1537 0.1778 0.2462 -0.0386 0.0103  0.0493  13  THR   A C   
191  O O   . THR   A 13  ? 0.1578 0.1734 0.2490 -0.0337 0.0103  0.0519  13  THR   A O   
192  C CB  . THR   A 13  ? 0.1589 0.1892 0.2553 -0.0291 0.0082  0.0500  13  THR   A CB  
193  O OG1 . THR   A 13  ? 0.1532 0.1844 0.2673 -0.0342 0.0092  0.0500  13  THR   A OG1 
194  C CG2 . THR   A 13  ? 0.1656 0.2090 0.2711 -0.0266 0.0080  0.0299  13  THR   A CG2 
202  N N   . ASP   A 14  ? 0.1642 0.1708 0.2547 -0.0452 0.0104  0.0564  14  ASP   A N   
203  C CA  . ASP   A 14  ? 0.1716 0.1798 0.2675 -0.0393 -0.0010 0.0617  14  ASP   A CA  
204  C C   . ASP   A 14  ? 0.1645 0.1792 0.2493 -0.0320 -0.0086 0.0633  14  ASP   A C   
205  O O   . ASP   A 14  ? 0.1861 0.1923 0.2583 -0.0535 -0.0152 0.0696  14  ASP   A O   
206  C CB  . ASP   A 14  ? 0.2048 0.2032 0.3148 -0.0427 -0.0011 0.0890  14  ASP   A CB  
207  C CG  . ASP   A 14  ? 0.2254 0.2619 0.3702 -0.0458 -0.0018 0.0867  14  ASP   A CG  
208  O OD1 . ASP   A 14  ? 0.2388 0.2875 0.3906 -0.0224 -0.0290 0.0885  14  ASP   A OD1 
209  O OD2 . ASP   A 14  ? 0.2415 0.3059 0.4148 -0.0338 -0.0061 0.0599  14  ASP   A OD2 
214  N N   . ASN   A 15  ? 0.1485 0.1603 0.2416 -0.0278 0.0071  0.0669  15  ASN   A N   
215  C CA  . ASN   A 15  ? 0.1500 0.1613 0.2626 -0.0254 -0.0056 0.0534  15  ASN   A CA  
216  C C   . ASN   A 15  ? 0.1451 0.1573 0.2816 -0.0293 0.0028  0.0536  15  ASN   A C   
217  O O   . ASN   A 15  ? 0.1423 0.1571 0.3334 -0.0214 -0.0109 0.0525  15  ASN   A O   
218  C CB  . ASN   A 15  ? 0.1472 0.1599 0.2473 -0.0208 -0.0053 0.0588  15  ASN   A CB  
219  C CG  . ASN   A 15  ? 0.1434 0.1664 0.2646 -0.0141 -0.0037 0.0409  15  ASN   A CG  
220  O OD1 . ASN   A 15  ? 0.1532 0.1764 0.2828 -0.0318 -0.0002 0.0452  15  ASN   A OD1 
221  N ND2 . ASN   A 15  ? 0.1446 0.1740 0.2480 -0.0231 0.0075  0.0378  15  ASN   A ND2 
228  N N   . VAL   A 16  ? 0.1504 0.1540 0.2710 -0.0244 0.0002  0.0542  16  VAL   A N   
229  C CA  . VAL   A 16  ? 0.1436 0.1534 0.2609 -0.0205 0.0074  0.0591  16  VAL   A CA  
230  C C   . VAL   A 16  ? 0.1390 0.1574 0.2536 -0.0239 0.0074  0.0554  16  VAL   A C   
231  O O   . VAL   A 16  ? 0.1322 0.1553 0.2611 -0.0276 0.0165  0.0471  16  VAL   A O   
232  C CB  . VAL   A 16  ? 0.1568 0.1656 0.2544 -0.0040 0.0204  0.0606  16  VAL   A CB  
233  C CG1 . VAL   A 16  ? 0.1756 0.1788 0.2502 0.0029  0.0176  0.0599  16  VAL   A CG1 
234  C CG2 . VAL   A 16  ? 0.1610 0.1832 0.2652 0.0046  0.0372  0.0543  16  VAL   A CG2 
244  N N   . TYR   A 17  ? 0.1356 0.1533 0.2569 -0.0229 0.0268  0.0545  17  TYR   A N   
245  C CA  . TYR   A 17  ? 0.1407 0.1593 0.2360 -0.0254 0.0260  0.0531  17  TYR   A CA  
246  C C   . TYR   A 17  ? 0.1444 0.1537 0.2517 -0.0200 0.0259  0.0563  17  TYR   A C   
247  O O   . TYR   A 17  ? 0.1350 0.1599 0.2712 -0.0197 0.0231  0.0644  17  TYR   A O   
248  C CB  . TYR   A 17  ? 0.1638 0.1588 0.2403 -0.0284 0.0038  0.0523  17  TYR   A CB  
249  C CG  . TYR   A 17  ? 0.1868 0.1675 0.2385 -0.0328 -0.0003 0.0446  17  TYR   A CG  
250  C CD1 . TYR   A 17  ? 0.2056 0.1817 0.2419 -0.0199 -0.0092 0.0465  17  TYR   A CD1 
251  C CD2 . TYR   A 17  ? 0.2060 0.1804 0.2335 -0.0466 0.0092  0.0420  17  TYR   A CD2 
252  C CE1 . TYR   A 17  ? 0.2243 0.1831 0.2490 -0.0257 -0.0129 0.0558  17  TYR   A CE1 
253  C CE2 . TYR   A 17  ? 0.2264 0.1844 0.2434 -0.0423 0.0011  0.0327  17  TYR   A CE2 
254  C CZ  . TYR   A 17  ? 0.2350 0.1786 0.2344 -0.0415 -0.0131 0.0493  17  TYR   A CZ  
255  O OH  . TYR   A 17  ? 0.2593 0.1842 0.2535 -0.0386 -0.0071 0.0413  17  TYR   A OH  
265  N N   A ILE   A 18  ? 0.1448 0.1520 0.2498 -0.0196 0.0294  0.0553  18  ILE   A N   
266  N N   B ILE   A 18  ? 0.1400 0.1528 0.2191 -0.0224 0.0302  0.0541  18  ILE   A N   
267  C CA  A ILE   A 18  ? 0.1501 0.1513 0.2446 -0.0177 0.0331  0.0401  18  ILE   A CA  
268  C CA  B ILE   A 18  ? 0.1375 0.1533 0.1816 -0.0157 0.0304  0.0396  18  ILE   A CA  
269  C C   A ILE   A 18  ? 0.1509 0.1638 0.2433 -0.0233 0.0329  0.0437  18  ILE   A C   
270  C C   B ILE   A 18  ? 0.1341 0.1754 0.1614 -0.0127 0.0144  0.0343  18  ILE   A C   
271  O O   A ILE   A 18  ? 0.1447 0.1764 0.2491 -0.0275 0.0394  0.0489  18  ILE   A O   
272  O O   B ILE   A 18  ? 0.1336 0.1901 0.1629 -0.0147 0.0126  0.0425  18  ILE   A O   
273  C CB  A ILE   A 18  ? 0.1577 0.1522 0.2311 0.0005  0.0318  0.0422  18  ILE   A CB  
274  C CB  B ILE   A 18  ? 0.1390 0.1369 0.1585 -0.0056 0.0280  0.0376  18  ILE   A CB  
275  C CG1 A ILE   A 18  ? 0.1673 0.1507 0.2224 0.0174  0.0227  0.0448  18  ILE   A CG1 
276  C CG1 B ILE   A 18  ? 0.1574 0.1473 0.1667 -0.0083 0.0338  0.0319  18  ILE   A CG1 
277  C CG2 A ILE   A 18  ? 0.1577 0.1558 0.2383 0.0003  0.0339  0.0300  18  ILE   A CG2 
278  C CG2 B ILE   A 18  ? 0.1386 0.1368 0.1555 -0.0124 0.0145  0.0413  18  ILE   A CG2 
279  C CD1 A ILE   A 18  ? 0.1864 0.1673 0.2324 0.0218  0.0231  0.0399  18  ILE   A CD1 
280  C CD1 B ILE   A 18  ? 0.1697 0.1559 0.1775 -0.0096 0.0316  0.0141  18  ILE   A CD1 
303  N N   A LYS   A 19  ? 0.1552 0.1630 0.2308 -0.0142 0.0368  0.0470  19  LYS   A N   
304  N N   B LYS   A 19  ? 0.1415 0.1824 0.1658 -0.0098 0.0206  0.0226  19  LYS   A N   
305  C CA  A LYS   A 19  ? 0.1641 0.1725 0.2482 -0.0143 0.0425  0.0415  19  LYS   A CA  
306  C CA  B LYS   A 19  ? 0.1572 0.1955 0.1771 -0.0001 0.0261  0.0078  19  LYS   A CA  
307  C C   A LYS   A 19  ? 0.1504 0.1645 0.2789 -0.0047 0.0453  0.0549  19  LYS   A C   
308  C C   B LYS   A 19  ? 0.1608 0.1964 0.1984 0.0102  0.0300  0.0049  19  LYS   A C   
309  O O   A LYS   A 19  ? 0.1413 0.1619 0.2809 -0.0015 0.0359  0.0635  19  LYS   A O   
310  O O   B LYS   A 19  ? 0.1588 0.1940 0.1939 0.0051  0.0238  0.0154  19  LYS   A O   
311  C CB  A LYS   A 19  ? 0.1753 0.1908 0.2472 -0.0285 0.0501  0.0291  19  LYS   A CB  
312  C CB  B LYS   A 19  ? 0.1588 0.2054 0.1734 -0.0055 0.0379  -0.0092 19  LYS   A CB  
313  C CG  A LYS   A 19  ? 0.2065 0.2071 0.2437 -0.0303 0.0441  0.0084  19  LYS   A CG  
314  C CG  B LYS   A 19  ? 0.1726 0.2194 0.1759 -0.0061 0.0389  -0.0144 19  LYS   A CG  
315  C CD  A LYS   A 19  ? 0.2333 0.2283 0.2414 -0.0295 0.0426  0.0004  19  LYS   A CD  
316  C CD  B LYS   A 19  ? 0.1870 0.2285 0.1767 -0.0125 0.0367  -0.0139 19  LYS   A CD  
317  C CE  A LYS   A 19  ? 0.2521 0.2378 0.2383 -0.0364 0.0422  -0.0068 19  LYS   A CE  
318  C CE  B LYS   A 19  ? 0.1953 0.2395 0.1825 -0.0185 0.0310  -0.0137 19  LYS   A CE  
319  N NZ  A LYS   A 19  ? 0.2653 0.2497 0.2355 -0.0417 0.0472  -0.0132 19  LYS   A NZ  
320  N NZ  B LYS   A 19  ? 0.2018 0.2436 0.1890 -0.0279 0.0354  -0.0173 19  LYS   A NZ  
347  N N   A ASN   A 20  ? 0.1576 0.1691 0.3115 -0.0083 0.0598  0.0710  20  ASN   A N   
348  N N   B ASN   A 20  ? 0.1742 0.2070 0.2338 0.0165  0.0426  -0.0057 20  ASN   A N   
349  C CA  A ASN   A 20  ? 0.1645 0.1821 0.3504 0.0151  0.0701  0.0690  20  ASN   A CA  
350  C CA  B ASN   A 20  ? 0.1805 0.2195 0.2762 0.0224  0.0467  -0.0052 20  ASN   A CA  
351  C C   A ASN   A 20  ? 0.1825 0.1928 0.3623 0.0111  0.0826  0.0548  20  ASN   A C   
352  C C   B ASN   A 20  ? 0.1897 0.2211 0.2858 0.0176  0.0573  0.0021  20  ASN   A C   
353  O O   A ASN   A 20  ? 0.2053 0.1917 0.3613 0.0071  0.0875  0.0369  20  ASN   A O   
354  O O   B ASN   A 20  ? 0.1985 0.2238 0.2934 0.0181  0.0612  -0.0016 20  ASN   A O   
355  C CB  A ASN   A 20  ? 0.1637 0.1859 0.3725 0.0264  0.0698  0.0850  20  ASN   A CB  
356  C CB  B ASN   A 20  ? 0.1823 0.2269 0.3061 0.0262  0.0405  -0.0091 20  ASN   A CB  
357  C CG  A ASN   A 20  ? 0.1758 0.1840 0.4125 0.0333  0.0641  0.0930  20  ASN   A CG  
358  C CG  B ASN   A 20  ? 0.1872 0.2311 0.3363 0.0298  0.0310  -0.0155 20  ASN   A CG  
359  O OD1 A ASN   A 20  ? 0.2029 0.1991 0.4544 0.0328  0.0802  0.0765  20  ASN   A OD1 
360  O OD1 B ASN   A 20  ? 0.1874 0.2293 0.3609 0.0276  0.0353  -0.0284 20  ASN   A OD1 
361  N ND2 A ASN   A 20  ? 0.1804 0.1784 0.4193 0.0279  0.0410  0.1098  20  ASN   A ND2 
362  N ND2 B ASN   A 20  ? 0.1991 0.2350 0.3499 0.0310  0.0204  -0.0079 20  ASN   A ND2 
375  N N   A ALA   A 21  ? 0.1882 0.1980 0.3674 0.0107  0.0717  0.0524  21  ALA   A N   
376  N N   B ALA   A 21  ? 0.1943 0.2158 0.2907 0.0103  0.0512  0.0113  21  ALA   A N   
377  C CA  A ALA   A 21  ? 0.1927 0.1972 0.3529 0.0104  0.0606  0.0534  21  ALA   A CA  
378  C CA  B ALA   A 21  ? 0.1965 0.2076 0.2802 0.0032  0.0522  0.0213  21  ALA   A CA  
379  C C   A ALA   A 21  ? 0.1879 0.1988 0.3399 0.0044  0.0521  0.0525  21  ALA   A C   
380  C C   B ALA   A 21  ? 0.1874 0.1937 0.2632 0.0050  0.0608  0.0253  21  ALA   A C   
381  O O   A ALA   A 21  ? 0.1827 0.1937 0.3387 -0.0011 0.0469  0.0599  21  ALA   A O   
382  O O   B ALA   A 21  ? 0.1829 0.1804 0.2697 0.0084  0.0631  0.0194  21  ALA   A O   
383  C CB  A ALA   A 21  ? 0.2072 0.1950 0.3613 0.0125  0.0554  0.0468  21  ALA   A CB  
384  C CB  B ALA   A 21  ? 0.2067 0.2109 0.2943 -0.0007 0.0443  0.0200  21  ALA   A CB  
395  N N   A ASP   A 22  ? 0.1920 0.1965 0.3263 0.0009  0.0483  0.0470  22  ASP   A N   
396  N N   B ASP   A 22  ? 0.1873 0.1874 0.2510 0.0047  0.0614  0.0312  22  ASP   A N   
397  C CA  A ASP   A 22  ? 0.1991 0.1972 0.3052 0.0022  0.0326  0.0369  22  ASP   A CA  
398  C CA  B ASP   A 22  ? 0.1881 0.1786 0.2354 0.0059  0.0534  0.0270  22  ASP   A CA  
399  C C   A ASP   A 22  ? 0.1821 0.1981 0.2550 -0.0040 0.0381  0.0360  22  ASP   A C   
400  C C   B ASP   A 22  ? 0.1734 0.1718 0.2105 -0.0070 0.0556  0.0181  22  ASP   A C   
401  O O   A ASP   A 22  ? 0.1861 0.2085 0.2662 -0.0097 0.0410  0.0285  22  ASP   A O   
402  O O   B ASP   A 22  ? 0.1741 0.1757 0.2118 -0.0105 0.0543  0.0015  22  ASP   A O   
403  C CB  A ASP   A 22  ? 0.2278 0.2011 0.3530 0.0012  0.0202  0.0293  22  ASP   A CB  
404  C CB  B ASP   A 22  ? 0.2031 0.1813 0.2525 0.0181  0.0508  0.0226  22  ASP   A CB  
405  C CG  A ASP   A 22  ? 0.2480 0.2033 0.3941 -0.0057 -0.0021 0.0402  22  ASP   A CG  
406  C CG  B ASP   A 22  ? 0.2134 0.1783 0.2586 0.0237  0.0435  0.0285  22  ASP   A CG  
407  O OD1 A ASP   A 22  ? 0.2452 0.1954 0.4135 -0.0345 -0.0237 0.0565  22  ASP   A OD1 
408  O OD1 B ASP   A 22  ? 0.2158 0.1663 0.2379 0.0264  0.0480  0.0314  22  ASP   A OD1 
409  O OD2 A ASP   A 22  ? 0.2672 0.2142 0.4239 0.0090  -0.0014 0.0348  22  ASP   A OD2 
410  O OD2 B ASP   A 22  ? 0.2165 0.1909 0.2709 0.0208  0.0472  0.0175  22  ASP   A OD2 
419  N N   A ILE   A 23  ? 0.1805 0.1934 0.2323 -0.0011 0.0340  0.0327  23  ILE   A N   
420  N N   B ILE   A 23  ? 0.1645 0.1642 0.1958 -0.0080 0.0495  0.0207  23  ILE   A N   
421  C CA  A ILE   A 23  ? 0.1774 0.1830 0.2100 -0.0025 0.0308  0.0292  23  ILE   A CA  
422  C CA  B ILE   A 23  ? 0.1567 0.1638 0.1717 -0.0119 0.0372  0.0213  23  ILE   A CA  
423  C C   A ILE   A 23  ? 0.1755 0.1847 0.2051 -0.0004 0.0446  0.0253  23  ILE   A C   
424  C C   B ILE   A 23  ? 0.1634 0.1705 0.1744 -0.0214 0.0352  0.0099  23  ILE   A C   
425  O O   A ILE   A 23  ? 0.1807 0.1831 0.2115 0.0022  0.0422  0.0199  23  ILE   A O   
426  O O   B ILE   A 23  ? 0.1623 0.1661 0.1759 -0.0215 0.0294  0.0026  23  ILE   A O   
427  C CB  A ILE   A 23  ? 0.1901 0.1762 0.1878 -0.0046 0.0265  0.0217  23  ILE   A CB  
428  C CB  B ILE   A 23  ? 0.1503 0.1525 0.1627 -0.0039 0.0268  0.0240  23  ILE   A CB  
429  C CG1 A ILE   A 23  ? 0.1989 0.1804 0.1836 -0.0027 0.0290  0.0164  23  ILE   A CG1 
430  C CG1 B ILE   A 23  ? 0.1535 0.1480 0.1597 -0.0052 0.0158  0.0198  23  ILE   A CG1 
431  C CG2 A ILE   A 23  ? 0.1940 0.1750 0.1914 -0.0054 0.0209  0.0257  23  ILE   A CG2 
432  C CG2 B ILE   A 23  ? 0.1484 0.1482 0.1626 0.0035  0.0253  0.0260  23  ILE   A CG2 
433  C CD1 A ILE   A 23  ? 0.2057 0.1781 0.1936 -0.0062 0.0215  0.0124  23  ILE   A CD1 
434  C CD1 B ILE   A 23  ? 0.1500 0.1510 0.1627 -0.0011 0.0048  0.0118  23  ILE   A CD1 
457  N N   A VAL   A 24  ? 0.1796 0.1917 0.2292 -0.0074 0.0395  0.0159  24  VAL   A N   
458  N N   B VAL   A 24  ? 0.1773 0.1835 0.1917 -0.0256 0.0319  -0.0016 24  VAL   A N   
459  C CA  A VAL   A 24  ? 0.1950 0.2013 0.2453 -0.0195 0.0405  0.0037  24  VAL   A CA  
460  C CA  B VAL   A 24  ? 0.1939 0.1950 0.2070 -0.0258 0.0330  -0.0075 24  VAL   A CA  
461  C C   A VAL   A 24  ? 0.2032 0.2186 0.2532 -0.0252 0.0405  -0.0003 24  VAL   A C   
462  C C   B VAL   A 24  ? 0.2026 0.2164 0.2184 -0.0232 0.0347  -0.0130 24  VAL   A C   
463  O O   A VAL   A 24  ? 0.2116 0.2186 0.2676 -0.0193 0.0417  0.0005  24  VAL   A O   
464  O O   B VAL   A 24  ? 0.2057 0.2214 0.2352 -0.0207 0.0323  -0.0082 24  VAL   A O   
465  C CB  A VAL   A 24  ? 0.2008 0.2028 0.2681 -0.0223 0.0461  0.0122  24  VAL   A CB  
466  C CB  B VAL   A 24  ? 0.1997 0.1936 0.2191 -0.0274 0.0298  -0.0063 24  VAL   A CB  
467  C CG1 A VAL   A 24  ? 0.2055 0.2117 0.2778 -0.0174 0.0492  0.0064  24  VAL   A CG1 
468  C CG1 B VAL   A 24  ? 0.2082 0.1952 0.2300 -0.0247 0.0247  -0.0082 24  VAL   A CG1 
469  C CG2 A VAL   A 24  ? 0.2144 0.2077 0.2844 -0.0217 0.0564  0.0262  24  VAL   A CG2 
470  C CG2 B VAL   A 24  ? 0.1996 0.1904 0.2168 -0.0314 0.0324  -0.0123 24  VAL   A CG2 
489  N N   A GLU   A 25  ? 0.2104 0.2472 0.2526 -0.0298 0.0528  -0.0113 25  GLU   A N   
490  N N   B GLU   A 25  ? 0.2107 0.2377 0.2274 -0.0216 0.0455  -0.0189 25  GLU   A N   
491  C CA  A GLU   A 25  ? 0.2267 0.2741 0.2522 -0.0249 0.0615  -0.0159 25  GLU   A CA  
492  C CA  B GLU   A 25  ? 0.2237 0.2598 0.2384 -0.0204 0.0429  -0.0181 25  GLU   A CA  
493  C C   A GLU   A 25  ? 0.2134 0.2769 0.2142 -0.0391 0.0782  -0.0122 25  GLU   A C   
494  C C   B GLU   A 25  ? 0.2193 0.2694 0.2287 -0.0219 0.0509  -0.0190 25  GLU   A C   
495  O O   A GLU   A 25  ? 0.2250 0.2908 0.2225 -0.0393 0.0747  -0.0124 25  GLU   A O   
496  O O   B GLU   A 25  ? 0.2238 0.2748 0.2379 -0.0265 0.0481  -0.0242 25  GLU   A O   
497  C CB  A GLU   A 25  ? 0.2535 0.2991 0.2924 -0.0187 0.0584  -0.0178 25  GLU   A CB  
498  C CB  B GLU   A 25  ? 0.2393 0.2699 0.2609 -0.0176 0.0372  -0.0214 25  GLU   A CB  
499  C CG  A GLU   A 25  ? 0.2834 0.3216 0.3490 -0.0187 0.0389  -0.0215 25  GLU   A CG  
500  C CG  B GLU   A 25  ? 0.2587 0.2813 0.3000 -0.0166 0.0233  -0.0263 25  GLU   A CG  
501  C CD  A GLU   A 25  ? 0.3073 0.3427 0.3985 -0.0156 0.0228  -0.0224 25  GLU   A CD  
502  C CD  B GLU   A 25  ? 0.2728 0.2907 0.3353 -0.0174 0.0098  -0.0263 25  GLU   A CD  
503  O OE1 A GLU   A 25  ? 0.3189 0.3533 0.4054 -0.0117 0.0087  -0.0276 25  GLU   A OE1 
504  O OE1 B GLU   A 25  ? 0.2803 0.2970 0.3584 -0.0175 0.0073  -0.0257 25  GLU   A OE1 
505  O OE2 A GLU   A 25  ? 0.3133 0.3499 0.4286 -0.0148 0.0188  -0.0265 25  GLU   A OE2 
506  O OE2 B GLU   A 25  ? 0.2779 0.2920 0.3473 -0.0187 0.0042  -0.0275 25  GLU   A OE2 
519  N N   A GLU   A 26  ? 0.2007 0.2663 0.2286 -0.0578 0.0841  -0.0104 26  GLU   A N   
520  N N   B GLU   A 26  ? 0.2169 0.2698 0.2221 -0.0229 0.0575  -0.0176 26  GLU   A N   
521  C CA  A GLU   A 26  ? 0.2161 0.2671 0.2115 -0.0651 0.0822  -0.0038 26  GLU   A CA  
522  C CA  B GLU   A 26  ? 0.2228 0.2715 0.2210 -0.0188 0.0568  -0.0102 26  GLU   A CA  
523  C C   A GLU   A 26  ? 0.2165 0.2551 0.1810 -0.0627 0.0750  -0.0003 26  GLU   A C   
524  C C   B GLU   A 26  ? 0.2206 0.2622 0.2063 -0.0100 0.0468  -0.0019 26  GLU   A C   
525  O O   A GLU   A 26  ? 0.2254 0.2523 0.1734 -0.0686 0.0705  -0.0058 26  GLU   A O   
526  O O   B GLU   A 26  ? 0.2249 0.2617 0.2056 -0.0141 0.0460  -0.0059 26  GLU   A O   
527  C CB  A GLU   A 26  ? 0.2372 0.2738 0.2513 -0.0754 0.0725  0.0067  26  GLU   A CB  
528  C CB  B GLU   A 26  ? 0.2329 0.2811 0.2432 -0.0268 0.0474  -0.0072 26  GLU   A CB  
529  C CG  A GLU   A 26  ? 0.2581 0.2889 0.3205 -0.0731 0.0762  0.0069  26  GLU   A CG  
530  C CG  B GLU   A 26  ? 0.2402 0.2887 0.2650 -0.0338 0.0502  -0.0063 26  GLU   A CG  
531  C CD  A GLU   A 26  ? 0.2666 0.2986 0.3523 -0.0778 0.1010  0.0110  26  GLU   A CD  
532  C CD  B GLU   A 26  ? 0.2435 0.2940 0.2753 -0.0441 0.0581  -0.0041 26  GLU   A CD  
533  O OE1 A GLU   A 26  ? 0.2593 0.3184 0.3571 -0.0607 0.1392  -0.0222 26  GLU   A OE1 
534  O OE1 B GLU   A 26  ? 0.2495 0.3062 0.2842 -0.0388 0.0688  -0.0081 26  GLU   A OE1 
535  O OE2 A GLU   A 26  ? 0.2789 0.2993 0.3583 -0.0843 0.0947  0.0273  26  GLU   A OE2 
536  O OE2 B GLU   A 26  ? 0.2412 0.2901 0.2588 -0.0519 0.0647  -0.0034 26  GLU   A OE2 
549  N N   A ALA   A 27  ? 0.2025 0.2414 0.1765 -0.0635 0.0679  0.0046  27  ALA   A N   
550  N N   B ALA   A 27  ? 0.2127 0.2535 0.1925 0.0024  0.0378  0.0066  27  ALA   A N   
551  C CA  A ALA   A 27  ? 0.2105 0.2499 0.1776 -0.0593 0.0615  0.0037  27  ALA   A CA  
552  C CA  B ALA   A 27  ? 0.2164 0.2535 0.1850 0.0137  0.0289  0.0113  27  ALA   A CA  
553  C C   A ALA   A 27  ? 0.2331 0.2662 0.1859 -0.0661 0.0698  -0.0117 27  ALA   A C   
554  C C   B ALA   A 27  ? 0.2302 0.2646 0.1929 0.0182  0.0280  0.0035  27  ALA   A C   
555  O O   A ALA   A 27  ? 0.2420 0.2631 0.1941 -0.0732 0.0589  -0.0198 27  ALA   A O   
556  O O   B ALA   A 27  ? 0.2300 0.2625 0.1922 0.0210  0.0229  0.0035  27  ALA   A O   
557  C CB  A ALA   A 27  ? 0.1988 0.2403 0.1817 -0.0611 0.0460  0.0094  27  ALA   A CB  
558  C CB  B ALA   A 27  ? 0.2107 0.2464 0.1806 0.0119  0.0241  0.0147  27  ALA   A CB  
569  N N   A LYS   A 28  ? 0.2623 0.2916 0.2117 -0.0549 0.0606  -0.0318 28  LYS   A N   
570  N N   B LYS   A 28  ? 0.2491 0.2778 0.2103 0.0226  0.0236  -0.0069 28  LYS   A N   
571  C CA  A LYS   A 28  ? 0.2966 0.3268 0.2474 -0.0391 0.0601  -0.0461 28  LYS   A CA  
572  C CA  B LYS   A 28  ? 0.2692 0.2978 0.2336 0.0289  0.0242  -0.0186 28  LYS   A CA  
573  C C   A LYS   A 28  ? 0.3162 0.3554 0.2500 -0.0369 0.0772  -0.0347 28  LYS   A C   
574  C C   B LYS   A 28  ? 0.2942 0.3201 0.2450 0.0254  0.0260  -0.0129 28  LYS   A C   
575  O O   A LYS   A 28  ? 0.3204 0.3607 0.2869 -0.0299 0.0603  -0.0345 28  LYS   A O   
576  O O   B LYS   A 28  ? 0.3001 0.3224 0.2518 0.0288  0.0166  -0.0131 28  LYS   A O   
577  C CB  A LYS   A 28  ? 0.3111 0.3375 0.2861 -0.0257 0.0518  -0.0568 28  LYS   A CB  
578  C CB  B LYS   A 28  ? 0.2688 0.2992 0.2540 0.0363  0.0235  -0.0287 28  LYS   A CB  
579  C CG  A LYS   A 28  ? 0.3247 0.3456 0.3190 -0.0175 0.0496  -0.0590 28  LYS   A CG  
580  C CG  B LYS   A 28  ? 0.2708 0.3038 0.2759 0.0375  0.0260  -0.0292 28  LYS   A CG  
581  C CD  A LYS   A 28  ? 0.3356 0.3579 0.3659 -0.0129 0.0455  -0.0513 28  LYS   A CD  
582  C CD  B LYS   A 28  ? 0.2763 0.3110 0.2980 0.0379  0.0289  -0.0289 28  LYS   A CD  
583  C CE  A LYS   A 28  ? 0.3438 0.3662 0.3978 -0.0108 0.0441  -0.0493 28  LYS   A CE  
584  C CE  B LYS   A 28  ? 0.2832 0.3170 0.3172 0.0357  0.0303  -0.0287 28  LYS   A CE  
585  N NZ  A LYS   A 28  ? 0.3496 0.3697 0.4152 -0.0078 0.0490  -0.0537 28  LYS   A NZ  
586  N NZ  B LYS   A 28  ? 0.2885 0.3208 0.3267 0.0366  0.0300  -0.0292 28  LYS   A NZ  
613  N N   A LYS   A 29  ? 0.3268 0.3789 0.2408 -0.0442 0.1102  -0.0157 29  LYS   A N   
614  N N   B LYS   A 29  ? 0.3120 0.3409 0.2623 0.0157  0.0404  -0.0026 29  LYS   A N   
615  C CA  A LYS   A 29  ? 0.3466 0.4052 0.2613 -0.0497 0.1238  -0.0010 29  LYS   A CA  
616  C CA  B LYS   A 29  ? 0.3340 0.3636 0.2919 0.0056  0.0460  0.0044  29  LYS   A CA  
617  C C   A LYS   A 29  ? 0.3470 0.4007 0.2535 -0.0637 0.1101  0.0087  29  LYS   A C   
618  C C   B LYS   A 29  ? 0.3360 0.3620 0.2755 -0.0060 0.0397  0.0107  29  LYS   A C   
619  O O   A LYS   A 29  ? 0.3597 0.4117 0.2727 -0.0571 0.1021  0.0074  29  LYS   A O   
620  O O   B LYS   A 29  ? 0.3405 0.3685 0.2821 -0.0051 0.0390  0.0127  29  LYS   A O   
621  C CB  A LYS   A 29  ? 0.3635 0.4331 0.3096 -0.0392 0.1405  0.0016  29  LYS   A CB  
622  C CB  B LYS   A 29  ? 0.3521 0.3859 0.3415 0.0080  0.0561  0.0043  29  LYS   A CB  
623  C CG  A LYS   A 29  ? 0.3825 0.4581 0.3775 -0.0289 0.1408  0.0046  29  LYS   A CG  
624  C CG  B LYS   A 29  ? 0.3696 0.4059 0.3963 0.0109  0.0609  0.0039  29  LYS   A CG  
625  C CD  A LYS   A 29  ? 0.4001 0.4793 0.4484 -0.0209 0.1360  0.0026  29  LYS   A CD  
626  C CD  B LYS   A 29  ? 0.3844 0.4227 0.4481 0.0129  0.0630  0.0020  29  LYS   A CD  
627  C CE  A LYS   A 29  ? 0.4119 0.4942 0.4976 -0.0156 0.1354  0.0001  29  LYS   A CE  
628  C CE  B LYS   A 29  ? 0.3945 0.4347 0.4846 0.0144  0.0656  -0.0008 29  LYS   A CE  
629  N NZ  A LYS   A 29  ? 0.4174 0.5024 0.5300 -0.0118 0.1331  -0.0027 29  LYS   A NZ  
630  N NZ  B LYS   A 29  ? 0.3992 0.4409 0.5068 0.0158  0.0659  -0.0028 29  LYS   A NZ  
657  N N   A VAL   A 30  ? 0.3303 0.3830 0.2216 -0.0833 0.1094  0.0174  30  VAL   A N   
658  N N   B VAL   A 30  ? 0.3327 0.3530 0.2589 -0.0171 0.0371  0.0129  30  VAL   A N   
659  C CA  A VAL   A 30  ? 0.3247 0.3661 0.2075 -0.0955 0.0851  0.0263  30  VAL   A CA  
660  C CA  B VAL   A 30  ? 0.3321 0.3433 0.2468 -0.0270 0.0273  0.0172  30  VAL   A CA  
661  C C   A VAL   A 30  ? 0.3280 0.3501 0.1639 -0.0950 0.0720  0.0338  30  VAL   A C   
662  C C   B VAL   A 30  ? 0.3346 0.3358 0.2246 -0.0319 0.0226  0.0150  30  VAL   A C   
663  O O   A VAL   A 30  ? 0.3376 0.3524 0.1624 -0.0962 0.0654  0.0415  30  VAL   A O   
664  O O   B VAL   A 30  ? 0.3386 0.3368 0.2220 -0.0324 0.0195  0.0163  30  VAL   A O   
665  C CB  A VAL   A 30  ? 0.3183 0.3621 0.2400 -0.1091 0.0665  0.0296  30  VAL   A CB  
666  C CB  B VAL   A 30  ? 0.3297 0.3400 0.2611 -0.0317 0.0207  0.0206  30  VAL   A CB  
667  C CG1 A VAL   A 30  ? 0.3208 0.3599 0.2545 -0.1095 0.0516  0.0276  30  VAL   A CG1 
668  C CG1 B VAL   A 30  ? 0.3302 0.3387 0.2683 -0.0317 0.0158  0.0193  30  VAL   A CG1 
669  C CG2 A VAL   A 30  ? 0.3135 0.3624 0.2613 -0.1176 0.0657  0.0334  30  VAL   A CG2 
670  C CG2 B VAL   A 30  ? 0.3290 0.3397 0.2714 -0.0342 0.0193  0.0247  30  VAL   A CG2 
689  N N   A LYS   A 31  ? 0.3214 0.3326 0.1533 -0.0923 0.0546  0.0287  31  LYS   A N   
690  N N   B LYS   A 31  ? 0.3326 0.3273 0.2189 -0.0374 0.0173  0.0133  31  LYS   A N   
691  C CA  A LYS   A 31  ? 0.3331 0.3276 0.1734 -0.0736 0.0233  0.0222  31  LYS   A CA  
692  C CA  B LYS   A 31  ? 0.3355 0.3236 0.2279 -0.0396 0.0095  0.0136  31  LYS   A CA  
693  C C   A LYS   A 31  ? 0.3105 0.3053 0.1249 -0.0596 0.0107  0.0531  31  LYS   A C   
694  C C   B LYS   A 31  ? 0.3127 0.3029 0.1684 -0.0447 0.0102  0.0357  31  LYS   A C   
695  O O   A LYS   A 31  ? 0.3141 0.3146 0.1394 -0.0539 -0.0138 0.0581  31  LYS   A O   
696  O O   B LYS   A 31  ? 0.3172 0.3075 0.1759 -0.0420 0.0004  0.0397  31  LYS   A O   
697  C CB  A LYS   A 31  ? 0.3705 0.3507 0.2867 -0.0636 0.0008  -0.0089 31  LYS   A CB  
698  C CB  B LYS   A 31  ? 0.3610 0.3423 0.3094 -0.0351 -0.0007 -0.0040 31  LYS   A CB  
699  C CG  A LYS   A 31  ? 0.4083 0.3754 0.4065 -0.0507 -0.0215 -0.0303 31  LYS   A CG  
700  C CG  B LYS   A 31  ? 0.3855 0.3616 0.3942 -0.0297 -0.0116 -0.0173 31  LYS   A CG  
701  C CD  A LYS   A 31  ? 0.4380 0.3945 0.4946 -0.0404 -0.0396 -0.0456 31  LYS   A CD  
702  C CD  B LYS   A 31  ? 0.4047 0.3771 0.4610 -0.0254 -0.0214 -0.0271 31  LYS   A CD  
703  C CE  A LYS   A 31  ? 0.4576 0.4079 0.5498 -0.0327 -0.0525 -0.0573 31  LYS   A CE  
704  C CE  B LYS   A 31  ? 0.4176 0.3884 0.5036 -0.0221 -0.0286 -0.0347 31  LYS   A CE  
705  N NZ  A LYS   A 31  ? 0.4676 0.4149 0.5807 -0.0280 -0.0600 -0.0631 31  LYS   A NZ  
706  N NZ  B LYS   A 31  ? 0.4240 0.3938 0.5288 -0.0199 -0.0327 -0.0389 31  LYS   A NZ  
733  N N   . PRO   A 32  ? 0.2856 0.2792 0.1226 -0.0543 0.0198  0.0424  32  PRO   A N   
734  C CA  . PRO   A 32  ? 0.2715 0.2556 0.1517 -0.0519 0.0079  0.0567  32  PRO   A CA  
735  C C   . PRO   A 32  ? 0.2627 0.2475 0.1554 -0.0422 0.0009  0.0622  32  PRO   A C   
736  O O   . PRO   A 32  ? 0.2595 0.2382 0.1631 -0.0463 -0.0195 0.0580  32  PRO   A O   
737  C CB  . PRO   A 32  ? 0.2637 0.2588 0.1630 -0.0506 0.0064  0.0424  32  PRO   A CB  
738  C CG  . PRO   A 32  ? 0.2589 0.2656 0.1144 -0.0452 -0.0025 0.0307  32  PRO   A CG  
739  C CD  . PRO   A 32  ? 0.2646 0.2707 0.1030 -0.0472 0.0087  0.0332  32  PRO   A CD  
747  N N   . THR   A 33  ? 0.2600 0.2442 0.1593 -0.0363 0.0007  0.0605  33  THR   A N   
748  C CA  . THR   A 33  ? 0.2571 0.2444 0.1597 -0.0240 -0.0118 0.0613  33  THR   A CA  
749  C C   . THR   A 33  ? 0.2252 0.2221 0.1557 -0.0272 -0.0152 0.0466  33  THR   A C   
750  O O   . THR   A 33  ? 0.2192 0.2204 0.1690 -0.0317 -0.0328 0.0487  33  THR   A O   
751  C CB  . THR   A 33  ? 0.2835 0.2691 0.1820 -0.0151 -0.0213 0.0787  33  THR   A CB  
752  O OG1 . THR   A 33  ? 0.3071 0.2833 0.2182 -0.0040 -0.0152 0.0864  33  THR   A OG1 
753  C CG2 . THR   A 33  ? 0.2860 0.2797 0.1967 -0.0123 -0.0352 0.0718  33  THR   A CG2 
761  N N   . VAL   A 34  ? 0.1948 0.2047 0.1507 -0.0305 -0.0070 0.0414  34  VAL   A N   
762  C CA  . VAL   A 34  ? 0.1817 0.1859 0.1329 -0.0242 -0.0025 0.0362  34  VAL   A CA  
763  C C   . VAL   A 34  ? 0.1736 0.1756 0.1349 -0.0246 -0.0003 0.0335  34  VAL   A C   
764  O O   . VAL   A 34  ? 0.1742 0.1758 0.1638 -0.0303 0.0056  0.0406  34  VAL   A O   
765  C CB  . VAL   A 34  ? 0.1897 0.1842 0.1587 -0.0194 0.0023  0.0331  34  VAL   A CB  
766  C CG1 . VAL   A 34  ? 0.1921 0.1842 0.1635 -0.0154 0.0116  0.0237  34  VAL   A CG1 
767  C CG2 . VAL   A 34  ? 0.1955 0.1985 0.1881 -0.0180 -0.0067 0.0300  34  VAL   A CG2 
777  N N   . VAL   A 35  ? 0.1595 0.1591 0.1422 -0.0259 -0.0037 0.0292  35  VAL   A N   
778  C CA  . VAL   A 35  ? 0.1501 0.1563 0.1385 -0.0235 0.0088  0.0220  35  VAL   A CA  
779  C C   . VAL   A 35  ? 0.1410 0.1477 0.1331 -0.0178 0.0058  0.0301  35  VAL   A C   
780  O O   . VAL   A 35  ? 0.1321 0.1587 0.1575 -0.0240 0.0177  0.0203  35  VAL   A O   
781  C CB  . VAL   A 35  ? 0.1576 0.1633 0.1553 -0.0123 0.0175  0.0117  35  VAL   A CB  
782  C CG1 . VAL   A 35  ? 0.1663 0.1646 0.1706 -0.0048 0.0089  0.0044  35  VAL   A CG1 
783  C CG2 . VAL   A 35  ? 0.1551 0.1664 0.1835 -0.0113 0.0186  0.0060  35  VAL   A CG2 
793  N N   . VAL   A 36  ? 0.1281 0.1456 0.1391 -0.0190 0.0118  0.0294  36  VAL   A N   
794  C CA  . VAL   A 36  ? 0.1282 0.1329 0.1430 -0.0110 0.0108  0.0146  36  VAL   A CA  
795  C C   . VAL   A 36  ? 0.1252 0.1394 0.1422 -0.0174 0.0130  0.0160  36  VAL   A C   
796  O O   . VAL   A 36  ? 0.1326 0.1335 0.1637 -0.0078 0.0243  0.0197  36  VAL   A O   
797  C CB  . VAL   A 36  ? 0.1300 0.1232 0.1438 -0.0140 0.0044  0.0190  36  VAL   A CB  
798  C CG1 . VAL   A 36  ? 0.1322 0.1278 0.1627 -0.0169 -0.0006 0.0104  36  VAL   A CG1 
799  C CG2 . VAL   A 36  ? 0.1379 0.1289 0.1679 -0.0094 0.0007  0.0240  36  VAL   A CG2 
809  N N   . ASN   A 37  ? 0.1159 0.1277 0.1414 -0.0046 0.0087  0.0200  37  ASN   A N   
810  C CA  . ASN   A 37  ? 0.1174 0.1245 0.1362 0.0020  0.0040  0.0202  37  ASN   A CA  
811  C C   . ASN   A 37  ? 0.1174 0.1223 0.1359 -0.0048 0.0152  0.0299  37  ASN   A C   
812  O O   . ASN   A 37  ? 0.1296 0.1340 0.1305 0.0032  0.0114  0.0119  37  ASN   A O   
813  C CB  . ASN   A 37  ? 0.1218 0.1219 0.1346 0.0011  0.0089  0.0134  37  ASN   A CB  
814  C CG  . ASN   A 37  ? 0.1225 0.1234 0.1569 0.0038  0.0100  0.0139  37  ASN   A CG  
815  O OD1 . ASN   A 37  ? 0.1245 0.1266 0.1723 -0.0015 0.0132  0.0239  37  ASN   A OD1 
816  N ND2 . ASN   A 37  ? 0.1273 0.1219 0.1602 -0.0036 0.0023  0.0306  37  ASN   A ND2 
823  N N   A ALA   A 38  ? 0.1168 0.1373 0.1440 -0.0018 0.0074  0.0170  38  ALA   A N   
824  N N   B ALA   A 38  ? 0.1207 0.1337 0.1462 -0.0048 0.0041  0.0256  38  ALA   A N   
825  C CA  A ALA   A 38  ? 0.1232 0.1372 0.1344 -0.0023 0.0012  0.0036  38  ALA   A CA  
826  C CA  B ALA   A 38  ? 0.1278 0.1386 0.1561 -0.0094 -0.0051 0.0257  38  ALA   A CA  
827  C C   A ALA   A 38  ? 0.1218 0.1299 0.1368 -0.0022 -0.0049 -0.0008 38  ALA   A C   
828  C C   B ALA   A 38  ? 0.1290 0.1386 0.1556 -0.0064 -0.0133 0.0243  38  ALA   A C   
829  O O   A ALA   A 38  ? 0.1232 0.1192 0.1423 -0.0008 -0.0113 0.0060  38  ALA   A O   
830  O O   B ALA   A 38  ? 0.1241 0.1347 0.1723 -0.0044 -0.0245 0.0280  38  ALA   A O   
831  C CB  A ALA   A 38  ? 0.1272 0.1546 0.1487 -0.0090 -0.0056 0.0070  38  ALA   A CB  
832  C CB  B ALA   A 38  ? 0.1297 0.1431 0.1757 -0.0123 -0.0121 0.0195  38  ALA   A CB  
843  N N   A ALA   A 39  ? 0.1226 0.1257 0.1476 0.0036  0.0020  0.0086  39  ALA   A N   
844  N N   B ALA   A 39  ? 0.1361 0.1417 0.1539 -0.0046 -0.0058 0.0345  39  ALA   A N   
845  C CA  A ALA   A 39  ? 0.1175 0.1201 0.1398 0.0077  0.0057  0.0067  39  ALA   A CA  
846  C CA  B ALA   A 39  ? 0.1358 0.1449 0.1489 -0.0088 -0.0091 0.0246  39  ALA   A CA  
847  C C   A ALA   A 39  ? 0.1217 0.1207 0.1387 0.0009  0.0007  -0.0008 39  ALA   A C   
848  C C   B ALA   A 39  ? 0.1307 0.1324 0.1522 -0.0095 -0.0044 0.0212  39  ALA   A C   
849  O O   A ALA   A 39  ? 0.1411 0.1263 0.1455 -0.0065 0.0057  0.0040  39  ALA   A O   
850  O O   B ALA   A 39  ? 0.1465 0.1320 0.1687 -0.0113 0.0012  0.0156  39  ALA   A O   
851  C CB  A ALA   A 39  ? 0.1194 0.1207 0.1451 0.0124  -0.0037 0.0056  39  ALA   A CB  
852  C CB  B ALA   A 39  ? 0.1477 0.1557 0.1515 -0.0061 -0.0082 0.0227  39  ALA   A CB  
863  N N   A ASN   A 40  ? 0.1204 0.1243 0.1342 -0.0041 0.0077  0.0038  40  ASN   A N   
864  N N   B ASN   A 40  ? 0.1300 0.1254 0.1403 -0.0062 0.0044  0.0214  40  ASN   A N   
865  C CA  A ASN   A 40  ? 0.1283 0.1223 0.1316 0.0017  -0.0039 -0.0016 40  ASN   A CA  
866  C CA  B ASN   A 40  ? 0.1307 0.1233 0.1353 -0.0034 -0.0142 0.0194  40  ASN   A CA  
867  C C   A ASN   A 40  ? 0.1299 0.1129 0.1161 0.0004  -0.0008 0.0077  40  ASN   A C   
868  C C   B ASN   A 40  ? 0.1260 0.1207 0.1196 -0.0063 -0.0020 0.0276  40  ASN   A C   
869  O O   A ASN   A 40  ? 0.1273 0.1147 0.1335 -0.0056 -0.0003 0.0151  40  ASN   A O   
870  O O   B ASN   A 40  ? 0.1191 0.1233 0.1222 -0.0072 -0.0013 0.0302  40  ASN   A O   
871  C CB  A ASN   A 40  ? 0.1405 0.1363 0.1481 0.0056  -0.0153 0.0025  40  ASN   A CB  
872  C CB  B ASN   A 40  ? 0.1350 0.1242 0.1464 0.0013  -0.0193 0.0176  40  ASN   A CB  
873  C CG  A ASN   A 40  ? 0.1501 0.1328 0.1778 0.0038  -0.0030 0.0110  40  ASN   A CG  
874  C CG  B ASN   A 40  ? 0.1347 0.1234 0.1499 0.0038  -0.0255 0.0147  40  ASN   A CG  
875  O OD1 A ASN   A 40  ? 0.1571 0.1350 0.1810 0.0018  -0.0069 0.0144  40  ASN   A OD1 
876  O OD1 B ASN   A 40  ? 0.1426 0.1294 0.1628 0.0059  -0.0236 0.0113  40  ASN   A OD1 
877  N ND2 A ASN   A 40  ? 0.1583 0.1479 0.1915 0.0047  0.0083  -0.0037 40  ASN   A ND2 
878  N ND2 B ASN   A 40  ? 0.1290 0.1274 0.1606 -0.0038 -0.0150 0.0047  40  ASN   A ND2 
891  N N   A VAL   A 41  ? 0.1306 0.1209 0.1244 -0.0003 0.0023  0.0079  41  VAL   A N   
892  N N   B VAL   A 41  ? 0.1318 0.1253 0.1200 -0.0032 -0.0007 0.0319  41  VAL   A N   
893  C CA  A VAL   A 41  ? 0.1362 0.1267 0.1439 0.0007  0.0080  0.0122  41  VAL   A CA  
894  C CA  B VAL   A 41  ? 0.1277 0.1303 0.1165 -0.0015 0.0035  0.0280  41  VAL   A CA  
895  C C   A VAL   A 41  ? 0.1330 0.1212 0.1338 0.0025  0.0069  0.0120  41  VAL   A C   
896  C C   B VAL   A 41  ? 0.1284 0.1309 0.1212 -0.0017 0.0115  0.0191  41  VAL   A C   
897  O O   A VAL   A 41  ? 0.1431 0.1182 0.1335 0.0056  -0.0061 0.0110  41  VAL   A O   
898  O O   B VAL   A 41  ? 0.1378 0.1306 0.1027 -0.0015 0.0027  0.0172  41  VAL   A O   
899  C CB  A VAL   A 41  ? 0.1406 0.1354 0.1480 0.0007  0.0120  0.0042  41  VAL   A CB  
900  C CB  B VAL   A 41  ? 0.1324 0.1385 0.1192 0.0025  0.0114  0.0287  41  VAL   A CB  
901  C CG1 A VAL   A 41  ? 0.1514 0.1423 0.1546 0.0022  0.0065  0.0042  41  VAL   A CG1 
902  C CG1 B VAL   A 41  ? 0.1513 0.1516 0.1382 -0.0003 0.0160  0.0146  41  VAL   A CG1 
903  C CG2 A VAL   A 41  ? 0.1439 0.1457 0.1379 -0.0032 0.0185  0.0052  41  VAL   A CG2 
904  C CG2 B VAL   A 41  ? 0.1273 0.1344 0.1205 0.0025  0.0126  0.0224  41  VAL   A CG2 
923  N N   A TYR   A 42  ? 0.1186 0.1130 0.1722 -0.0053 0.0143  0.0219  42  TYR   A N   
924  N N   B TYR   A 42  ? 0.1219 0.1266 0.1366 0.0036  0.0157  0.0277  42  TYR   A N   
925  C CA  A TYR   A 42  ? 0.1254 0.1152 0.1811 -0.0115 0.0109  0.0205  42  TYR   A CA  
926  C CA  B TYR   A 42  ? 0.1173 0.1276 0.1318 0.0059  0.0228  0.0293  42  TYR   A CA  
927  C C   A TYR   A 42  ? 0.1189 0.1125 0.1765 -0.0061 0.0121  0.0281  42  TYR   A C   
928  C C   B TYR   A 42  ? 0.1235 0.1348 0.1368 0.0025  0.0127  0.0316  42  TYR   A C   
929  O O   A TYR   A 42  ? 0.1200 0.1145 0.1859 -0.0140 0.0120  0.0089  42  TYR   A O   
930  O O   B TYR   A 42  ? 0.1175 0.1399 0.1518 -0.0030 0.0077  0.0211  42  TYR   A O   
931  C CB  A TYR   A 42  ? 0.1435 0.1360 0.1716 -0.0073 0.0199  0.0273  42  TYR   A CB  
932  C CB  B TYR   A 42  ? 0.1203 0.1289 0.1337 0.0061  0.0142  0.0396  42  TYR   A CB  
933  C CG  A TYR   A 42  ? 0.1491 0.1440 0.1643 -0.0073 0.0051  0.0311  42  TYR   A CG  
934  C CG  B TYR   A 42  ? 0.1289 0.1342 0.1411 0.0102  0.0030  0.0373  42  TYR   A CG  
935  C CD1 A TYR   A 42  ? 0.1548 0.1556 0.1722 -0.0121 0.0116  0.0259  42  TYR   A CD1 
936  C CD1 B TYR   A 42  ? 0.1328 0.1383 0.1326 0.0053  0.0086  0.0423  42  TYR   A CD1 
937  C CD2 A TYR   A 42  ? 0.1577 0.1625 0.1790 0.0044  -0.0069 0.0272  42  TYR   A CD2 
938  C CD2 B TYR   A 42  ? 0.1406 0.1482 0.1624 0.0092  0.0092  0.0301  42  TYR   A CD2 
939  C CE1 A TYR   A 42  ? 0.1685 0.1694 0.1711 -0.0074 0.0117  0.0239  42  TYR   A CE1 
940  C CE1 B TYR   A 42  ? 0.1367 0.1461 0.1318 0.0028  0.0091  0.0384  42  TYR   A CE1 
941  C CE2 A TYR   A 42  ? 0.1647 0.1746 0.1942 -0.0107 -0.0021 0.0220  42  TYR   A CE2 
942  C CE2 B TYR   A 42  ? 0.1521 0.1591 0.1692 0.0084  0.0055  0.0261  42  TYR   A CE2 
943  C CZ  A TYR   A 42  ? 0.1763 0.1778 0.1711 -0.0104 0.0106  0.0233  42  TYR   A CZ  
944  C CZ  B TYR   A 42  ? 0.1500 0.1577 0.1406 0.0017  0.0113  0.0249  42  TYR   A CZ  
945  O OH  A TYR   A 42  ? 0.1908 0.1942 0.1875 -0.0109 0.0069  0.0212  42  TYR   A OH  
946  O OH  B TYR   A 42  ? 0.1537 0.1742 0.1431 -0.0100 0.0114  0.0179  42  TYR   A OH  
965  N N   A LEU   A 43  ? 0.1235 0.1140 0.1598 -0.0060 0.0146  0.0054  43  LEU   A N   
966  N N   B LEU   A 43  ? 0.1259 0.1366 0.1392 -0.0001 0.0016  0.0263  43  LEU   A N   
967  C CA  A LEU   A 43  ? 0.1184 0.1125 0.1521 -0.0111 0.0102  0.0034  43  LEU   A CA  
968  C CA  B LEU   A 43  ? 0.1304 0.1361 0.1374 -0.0030 -0.0006 0.0272  43  LEU   A CA  
969  C C   A LEU   A 43  ? 0.1152 0.1174 0.1532 0.0029  0.0056  0.0001  43  LEU   A C   
970  C C   B LEU   A 43  ? 0.1358 0.1391 0.1360 -0.0059 -0.0016 0.0199  43  LEU   A C   
971  O O   A LEU   A 43  ? 0.1326 0.1258 0.1856 0.0137  -0.0061 -0.0016 43  LEU   A O   
972  O O   B LEU   A 43  ? 0.1424 0.1388 0.1345 -0.0111 -0.0065 0.0169  43  LEU   A O   
973  C CB  A LEU   A 43  ? 0.1315 0.1132 0.1673 -0.0119 0.0110  0.0010  43  LEU   A CB  
974  C CB  B LEU   A 43  ? 0.1279 0.1307 0.1460 -0.0055 0.0080  0.0286  43  LEU   A CB  
975  C CG  A LEU   A 43  ? 0.1348 0.1169 0.1676 -0.0083 -0.0011 -0.0022 43  LEU   A CG  
976  C CG  B LEU   A 43  ? 0.1222 0.1291 0.1601 -0.0043 0.0110  0.0257  43  LEU   A CG  
977  C CD1 A LEU   A 43  ? 0.1355 0.1310 0.1821 -0.0020 -0.0026 0.0064  43  LEU   A CD1 
978  C CD1 B LEU   A 43  ? 0.1230 0.1340 0.1760 -0.0078 0.0120  0.0264  43  LEU   A CD1 
979  C CD2 A LEU   A 43  ? 0.1388 0.1245 0.1577 -0.0003 0.0033  0.0080  43  LEU   A CD2 
980  C CD2 B LEU   A 43  ? 0.1245 0.1222 0.1589 -0.0052 0.0096  0.0468  43  LEU   A CD2 
1003 N N   A LYS   A 44  ? 0.1241 0.1166 0.1552 0.0020  0.0086  0.0113  44  LYS   A N   
1004 N N   B LYS   A 44  ? 0.1408 0.1454 0.1395 -0.0060 -0.0039 0.0202  44  LYS   A N   
1005 C CA  A LYS   A 44  ? 0.1397 0.1133 0.1598 -0.0029 0.0131  0.0181  44  LYS   A CA  
1006 C CA  B LYS   A 44  ? 0.1539 0.1530 0.1453 -0.0076 -0.0017 0.0167  44  LYS   A CA  
1007 C C   A LYS   A 44  ? 0.1273 0.1154 0.1481 0.0062  0.0021  0.0099  44  LYS   A C   
1008 C C   B LYS   A 44  ? 0.1468 0.1482 0.1359 -0.0117 -0.0016 0.0064  44  LYS   A C   
1009 O O   A LYS   A 44  ? 0.1386 0.1349 0.1657 0.0093  -0.0055 -0.0027 44  LYS   A O   
1010 O O   B LYS   A 44  ? 0.1491 0.1536 0.1382 -0.0147 -0.0004 -0.0048 44  LYS   A O   
1011 C CB  A LYS   A 44  ? 0.1740 0.1250 0.1897 -0.0009 0.0201  0.0212  44  LYS   A CB  
1012 C CB  B LYS   A 44  ? 0.1795 0.1763 0.1883 -0.0032 0.0105  0.0166  44  LYS   A CB  
1013 C CG  A LYS   A 44  ? 0.2081 0.1559 0.2376 -0.0146 0.0453  0.0336  44  LYS   A CG  
1014 C CG  B LYS   A 44  ? 0.2030 0.2045 0.2444 -0.0004 0.0208  0.0173  44  LYS   A CG  
1015 C CD  A LYS   A 44  ? 0.2484 0.2134 0.3452 -0.0248 0.0435  0.0225  44  LYS   A CD  
1016 C CD  B LYS   A 44  ? 0.2299 0.2396 0.3154 -0.0064 0.0165  0.0118  44  LYS   A CD  
1017 C CE  A LYS   A 44  ? 0.2706 0.2537 0.4076 -0.0268 0.0444  0.0175  44  LYS   A CE  
1018 C CE  B LYS   A 44  ? 0.2423 0.2613 0.3572 -0.0131 0.0128  0.0101  44  LYS   A CE  
1019 N NZ  A LYS   A 44  ? 0.2849 0.2830 0.4364 -0.0281 0.0459  0.0135  44  LYS   A NZ  
1020 N NZ  B LYS   A 44  ? 0.2517 0.2723 0.3764 -0.0214 0.0102  0.0056  44  LYS   A NZ  
1047 N N   A HIS   A 45  ? 0.1195 0.1149 0.1443 0.0033  0.0052  0.0150  45  HIS   A N   
1048 N N   B HIS   A 45  ? 0.1458 0.1433 0.1393 -0.0142 -0.0090 0.0081  45  HIS   A N   
1049 C CA  A HIS   A 45  ? 0.1168 0.1148 0.1508 0.0030  0.0006  0.0089  45  HIS   A CA  
1050 C CA  B HIS   A 45  ? 0.1431 0.1396 0.1504 -0.0116 -0.0111 0.0056  45  HIS   A CA  
1051 C C   A HIS   A 45  ? 0.1220 0.1294 0.1494 0.0110  0.0080  0.0177  45  HIS   A C   
1052 C C   B HIS   A 45  ? 0.1482 0.1440 0.1571 -0.0094 -0.0093 0.0092  45  HIS   A C   
1053 O O   A HIS   A 45  ? 0.1263 0.1255 0.1841 0.0106  0.0114  0.0059  45  HIS   A O   
1054 O O   B HIS   A 45  ? 0.1557 0.1452 0.1818 -0.0046 -0.0048 0.0056  45  HIS   A O   
1055 C CB  A HIS   A 45  ? 0.1152 0.1190 0.1428 0.0021  0.0071  0.0071  45  HIS   A CB  
1056 C CB  B HIS   A 45  ? 0.1336 0.1371 0.1430 -0.0033 -0.0065 0.0015  45  HIS   A CB  
1057 C CG  A HIS   A 45  ? 0.1228 0.1112 0.1339 -0.0011 0.0041  0.0095  45  HIS   A CG  
1058 C CG  B HIS   A 45  ? 0.1210 0.1352 0.1272 -0.0024 0.0087  -0.0015 45  HIS   A CG  
1059 N ND1 A HIS   A 45  ? 0.1211 0.1175 0.1452 -0.0017 0.0022  0.0130  45  HIS   A ND1 
1060 N ND1 B HIS   A 45  ? 0.1127 0.1381 0.1488 0.0011  0.0020  0.0103  45  HIS   A ND1 
1061 C CD2 A HIS   A 45  ? 0.1271 0.1156 0.1442 -0.0083 -0.0033 0.0177  45  HIS   A CD2 
1062 C CD2 B HIS   A 45  ? 0.1083 0.1246 0.1150 -0.0017 0.0155  -0.0069 45  HIS   A CD2 
1063 C CE1 A HIS   A 45  ? 0.1283 0.1272 0.1443 -0.0049 0.0047  0.0189  45  HIS   A CE1 
1064 C CE1 B HIS   A 45  ? 0.1064 0.1261 0.1173 -0.0054 0.0075  -0.0017 45  HIS   A CE1 
1065 N NE2 A HIS   A 45  ? 0.1336 0.1292 0.1430 0.0045  -0.0017 0.0233  45  HIS   A NE2 
1066 N NE2 B HIS   A 45  ? 0.1059 0.1207 0.1022 -0.0048 0.0096  -0.0103 45  HIS   A NE2 
1081 N N   A GLY   A 46  ? 0.1294 0.1401 0.1564 0.0147  -0.0069 0.0237  46  GLY   A N   
1082 N N   B GLY   A 46  ? 0.1479 0.1420 0.1512 -0.0150 -0.0123 0.0133  46  GLY   A N   
1083 C CA  A GLY   A 46  ? 0.1325 0.1489 0.1823 0.0131  -0.0075 0.0301  46  GLY   A CA  
1084 C CA  B GLY   A 46  ? 0.1447 0.1474 0.1562 -0.0113 -0.0049 0.0187  46  GLY   A CA  
1085 C C   A GLY   A 46  ? 0.1388 0.1449 0.1793 0.0219  -0.0062 0.0452  46  GLY   A C   
1086 C C   B GLY   A 46  ? 0.1410 0.1470 0.1411 -0.0031 0.0060  0.0270  46  GLY   A C   
1087 O O   A GLY   A 46  ? 0.1493 0.1446 0.1957 0.0226  -0.0121 0.0440  46  GLY   A O   
1088 O O   B GLY   A 46  ? 0.1451 0.1510 0.1408 -0.0042 0.0034  0.0182  46  GLY   A O   
1095 N N   A GLY   A 47  ? 0.1305 0.1477 0.1723 0.0199  -0.0096 0.0280  47  GLY   A N   
1096 N N   B GLY   A 47  ? 0.1390 0.1490 0.1399 0.0012  0.0120  0.0135  47  GLY   A N   
1097 C CA  A GLY   A 47  ? 0.1344 0.1534 0.1657 0.0226  -0.0137 0.0144  47  GLY   A CA  
1098 C CA  B GLY   A 47  ? 0.1353 0.1516 0.1398 0.0020  0.0058  0.0154  47  GLY   A CA  
1099 C C   A GLY   A 47  ? 0.1341 0.1457 0.1550 0.0191  -0.0123 0.0137  47  GLY   A C   
1100 C C   B GLY   A 47  ? 0.1308 0.1392 0.1272 0.0092  0.0145  0.0104  47  GLY   A C   
1101 O O   A GLY   A 47  ? 0.1312 0.1346 0.1717 0.0202  -0.0167 0.0203  47  GLY   A O   
1102 O O   B GLY   A 47  ? 0.1290 0.1305 0.1446 0.0133  0.0190  0.0144  47  GLY   A O   
1109 N N   A GLY   A 48  ? 0.1337 0.1454 0.1486 0.0179  -0.0167 0.0074  48  GLY   A N   
1110 N N   B GLY   A 48  ? 0.1321 0.1425 0.1209 0.0042  0.0224  0.0100  48  GLY   A N   
1111 C CA  A GLY   A 48  ? 0.1306 0.1426 0.1551 0.0138  -0.0127 -0.0084 48  GLY   A CA  
1112 C CA  B GLY   A 48  ? 0.1355 0.1332 0.1103 -0.0002 0.0207  0.0049  48  GLY   A CA  
1113 C C   A GLY   A 48  ? 0.1318 0.1420 0.1447 0.0053  0.0015  -0.0085 48  GLY   A C   
1114 C C   B GLY   A 48  ? 0.1387 0.1301 0.1086 0.0056  0.0157  0.0030  48  GLY   A C   
1115 O O   A GLY   A 48  ? 0.1425 0.1462 0.1434 0.0007  -0.0013 -0.0103 48  GLY   A O   
1116 O O   B GLY   A 48  ? 0.1502 0.1336 0.1014 0.0103  0.0213  -0.0046 48  GLY   A O   
1123 N N   A VAL   A 49  ? 0.1292 0.1390 0.1566 -0.0024 -0.0058 0.0021  49  VAL   A N   
1124 N N   B VAL   A 49  ? 0.1297 0.1252 0.1221 0.0079  0.0005  -0.0039 49  VAL   A N   
1125 C CA  A VAL   A 49  ? 0.1409 0.1361 0.1597 -0.0127 0.0050  0.0116  49  VAL   A CA  
1126 C CA  B VAL   A 49  ? 0.1265 0.1302 0.1300 0.0084  -0.0101 0.0006  49  VAL   A CA  
1127 C C   A VAL   A 49  ? 0.1366 0.1268 0.1393 -0.0063 0.0031  0.0110  49  VAL   A C   
1128 C C   B VAL   A 49  ? 0.1245 0.1217 0.1172 0.0100  -0.0071 -0.0120 49  VAL   A C   
1129 O O   A VAL   A 49  ? 0.1421 0.1362 0.1258 -0.0136 0.0011  0.0055  49  VAL   A O   
1130 O O   B VAL   A 49  ? 0.1238 0.1272 0.1169 0.0102  -0.0008 0.0051  49  VAL   A O   
1131 C CB  A VAL   A 49  ? 0.1638 0.1379 0.1787 -0.0196 -0.0148 0.0136  49  VAL   A CB  
1132 C CB  B VAL   A 49  ? 0.1315 0.1379 0.1652 0.0087  -0.0311 0.0128  49  VAL   A CB  
1133 C CG1 A VAL   A 49  ? 0.1668 0.1372 0.1966 -0.0162 -0.0088 0.0228  49  VAL   A CG1 
1134 C CG1 B VAL   A 49  ? 0.1183 0.1362 0.1725 0.0146  -0.0313 0.0271  49  VAL   A CG1 
1135 C CG2 A VAL   A 49  ? 0.1799 0.1541 0.2077 -0.0363 -0.0254 0.0192  49  VAL   A CG2 
1136 C CG2 B VAL   A 49  ? 0.1402 0.1422 0.1787 0.0024  -0.0528 0.0261  49  VAL   A CG2 
1155 N N   A ALA   A 50  ? 0.1266 0.1241 0.1396 -0.0028 -0.0064 0.0167  50  ALA   A N   
1156 N N   B ALA   A 50  ? 0.1267 0.1167 0.1197 0.0051  -0.0075 -0.0137 50  ALA   A N   
1157 C CA  A ALA   A 50  ? 0.1228 0.1261 0.1497 -0.0049 -0.0046 0.0220  50  ALA   A CA  
1158 C CA  B ALA   A 50  ? 0.1223 0.1156 0.1156 -0.0018 0.0023  -0.0162 50  ALA   A CA  
1159 C C   A ALA   A 50  ? 0.1149 0.1282 0.1411 -0.0040 -0.0041 0.0167  50  ALA   A C   
1160 C C   B ALA   A 50  ? 0.1247 0.1126 0.1090 -0.0074 0.0019  -0.0125 50  ALA   A C   
1161 O O   A ALA   A 50  ? 0.1156 0.1319 0.1461 0.0007  -0.0010 0.0180  50  ALA   A O   
1162 O O   B ALA   A 50  ? 0.1313 0.1160 0.1077 -0.0052 0.0068  -0.0182 50  ALA   A O   
1163 C CB  A ALA   A 50  ? 0.1254 0.1226 0.1642 -0.0016 -0.0047 0.0189  50  ALA   A CB  
1164 C CB  B ALA   A 50  ? 0.1217 0.1078 0.1010 -0.0011 0.0054  -0.0275 50  ALA   A CB  
1175 N N   A GLY   A 51  ? 0.1229 0.1247 0.1385 0.0100  -0.0065 0.0075  51  GLY   A N   
1176 N N   B GLY   A 51  ? 0.1273 0.1098 0.1236 -0.0038 -0.0033 -0.0173 51  GLY   A N   
1177 C CA  A GLY   A 51  ? 0.1295 0.1225 0.1532 0.0124  -0.0076 0.0061  51  GLY   A CA  
1178 C CA  B GLY   A 51  ? 0.1352 0.1087 0.1175 -0.0025 -0.0093 -0.0185 51  GLY   A CA  
1179 C C   A GLY   A 51  ? 0.1215 0.1303 0.1445 0.0092  0.0002  -0.0026 51  GLY   A C   
1180 C C   B GLY   A 51  ? 0.1320 0.1214 0.1191 0.0028  -0.0054 -0.0183 51  GLY   A C   
1181 O O   A GLY   A 51  ? 0.1249 0.1417 0.1398 -0.0013 -0.0065 0.0038  51  GLY   A O   
1182 O O   B GLY   A 51  ? 0.1345 0.1283 0.1189 0.0068  -0.0009 -0.0219 51  GLY   A O   
1189 N N   A ALA   A 52  ? 0.1198 0.1428 0.1469 0.0066  0.0016  0.0013  52  ALA   A N   
1190 N N   B ALA   A 52  ? 0.1325 0.1327 0.1173 -0.0037 0.0027  -0.0247 52  ALA   A N   
1191 C CA  A ALA   A 52  ? 0.1218 0.1565 0.1505 0.0011  -0.0020 0.0053  52  ALA   A CA  
1192 C CA  B ALA   A 52  ? 0.1273 0.1437 0.1249 0.0008  0.0072  -0.0155 52  ALA   A CA  
1193 C C   A ALA   A 52  ? 0.1239 0.1507 0.1402 -0.0072 -0.0009 0.0062  52  ALA   A C   
1194 C C   B ALA   A 52  ? 0.1203 0.1376 0.1122 -0.0062 0.0094  -0.0103 52  ALA   A C   
1195 O O   A ALA   A 52  ? 0.1373 0.1569 0.1329 -0.0005 0.0029  0.0151  52  ALA   A O   
1196 O O   B ALA   A 52  ? 0.1244 0.1353 0.1202 -0.0044 0.0068  -0.0062 52  ALA   A O   
1197 C CB  A ALA   A 52  ? 0.1298 0.1886 0.1565 -0.0045 -0.0075 0.0089  52  ALA   A CB  
1198 C CB  B ALA   A 52  ? 0.1331 0.1651 0.1522 0.0012  0.0043  -0.0137 52  ALA   A CB  
1209 N N   A LEU   A 53  ? 0.1170 0.1432 0.1476 -0.0041 -0.0047 0.0060  53  LEU   A N   
1210 N N   B LEU   A 53  ? 0.1129 0.1382 0.1197 -0.0052 0.0109  -0.0035 53  LEU   A N   
1211 C CA  A LEU   A 53  ? 0.1304 0.1487 0.1443 -0.0098 0.0051  0.0045  53  LEU   A CA  
1212 C CA  B LEU   A 53  ? 0.1175 0.1453 0.1120 -0.0046 0.0024  -0.0034 53  LEU   A CA  
1213 C C   A LEU   A 53  ? 0.1290 0.1468 0.1317 0.0039  0.0061  0.0035  53  LEU   A C   
1214 C C   B LEU   A 53  ? 0.1250 0.1446 0.1020 -0.0044 0.0095  -0.0045 53  LEU   A C   
1215 O O   A LEU   A 53  ? 0.1475 0.1490 0.1539 -0.0134 0.0078  -0.0013 53  LEU   A O   
1216 O O   B LEU   A 53  ? 0.1351 0.1470 0.1142 -0.0129 0.0133  0.0019  53  LEU   A O   
1217 C CB  A LEU   A 53  ? 0.1387 0.1497 0.1592 -0.0107 0.0096  0.0144  53  LEU   A CB  
1218 C CB  B LEU   A 53  ? 0.1151 0.1480 0.1070 -0.0034 -0.0126 0.0003  53  LEU   A CB  
1219 C CG  A LEU   A 53  ? 0.1399 0.1454 0.1636 -0.0134 0.0047  0.0057  53  LEU   A CG  
1220 C CG  B LEU   A 53  ? 0.1144 0.1519 0.1209 -0.0015 -0.0133 0.0062  53  LEU   A CG  
1221 C CD1 A LEU   A 53  ? 0.1342 0.1535 0.1686 -0.0016 -0.0050 0.0124  53  LEU   A CD1 
1222 C CD1 B LEU   A 53  ? 0.1249 0.1558 0.1318 -0.0042 -0.0063 -0.0031 53  LEU   A CD1 
1223 C CD2 A LEU   A 53  ? 0.1575 0.1659 0.1746 -0.0182 -0.0011 0.0088  53  LEU   A CD2 
1224 C CD2 B LEU   A 53  ? 0.1085 0.1584 0.1223 -0.0058 -0.0110 0.0112  53  LEU   A CD2 
1247 N N   A ASN   A 54  ? 0.1233 0.1410 0.1350 0.0026  -0.0081 0.0077  54  ASN   A N   
1248 N N   B ASN   A 54  ? 0.1253 0.1440 0.1168 -0.0074 0.0074  -0.0078 54  ASN   A N   
1249 C CA  A ASN   A 54  ? 0.1151 0.1276 0.1504 0.0029  -0.0036 0.0065  54  ASN   A CA  
1250 C CA  B ASN   A 54  ? 0.1208 0.1395 0.1341 -0.0058 -0.0003 -0.0099 54  ASN   A CA  
1251 C C   A ASN   A 54  ? 0.1255 0.1370 0.1559 -0.0053 0.0051  0.0087  54  ASN   A C   
1252 C C   B ASN   A 54  ? 0.1265 0.1377 0.1430 -0.0109 0.0019  -0.0015 54  ASN   A C   
1253 O O   A ASN   A 54  ? 0.1322 0.1485 0.1633 0.0000  -0.0002 -0.0026 54  ASN   A O   
1254 O O   B ASN   A 54  ? 0.1290 0.1335 0.1405 -0.0162 -0.0036 -0.0036 54  ASN   A O   
1255 C CB  A ASN   A 54  ? 0.1129 0.1229 0.1586 -0.0042 -0.0094 0.0064  54  ASN   A CB  
1256 C CB  B ASN   A 54  ? 0.1238 0.1440 0.1431 0.0008  -0.0014 -0.0140 54  ASN   A CB  
1257 C CG  A ASN   A 54  ? 0.1169 0.1224 0.1613 -0.0037 -0.0037 0.0049  54  ASN   A CG  
1258 C CG  B ASN   A 54  ? 0.1246 0.1471 0.1361 0.0077  -0.0012 -0.0222 54  ASN   A CG  
1259 O OD1 A ASN   A 54  ? 0.1136 0.1182 0.1664 -0.0084 -0.0043 0.0236  54  ASN   A OD1 
1260 O OD1 B ASN   A 54  ? 0.1208 0.1494 0.1260 0.0092  -0.0047 -0.0341 54  ASN   A OD1 
1261 N ND2 A ASN   A 54  ? 0.1177 0.1310 0.1762 -0.0048 -0.0074 0.0138  54  ASN   A ND2 
1262 N ND2 B ASN   A 54  ? 0.1308 0.1523 0.1503 0.0024  -0.0031 -0.0014 54  ASN   A ND2 
1275 N N   . LYS   A 55  ? 0.1273 0.1363 0.1600 -0.0008 -0.0004 -0.0020 55  LYS   A N   
1276 C CA  . LYS   A 55  ? 0.1384 0.1459 0.1653 0.0090  -0.0038 -0.0156 55  LYS   A CA  
1277 C C   . LYS   A 55  ? 0.1300 0.1526 0.1699 -0.0016 0.0009  -0.0202 55  LYS   A C   
1278 O O   . LYS   A 55  ? 0.1411 0.1639 0.1801 0.0051  -0.0051 -0.0233 55  LYS   A O   
1279 C CB  . LYS   A 55  ? 0.1490 0.1538 0.1838 0.0190  -0.0020 -0.0164 55  LYS   A CB  
1280 C CG  . LYS   A 55  ? 0.1647 0.1930 0.2026 0.0338  -0.0175 -0.0308 55  LYS   A CG  
1281 C CD  . LYS   A 55  ? 0.1807 0.2234 0.2174 0.0485  -0.0144 -0.0306 55  LYS   A CD  
1282 C CE  . LYS   A 55  ? 0.2055 0.2540 0.2423 0.0597  -0.0264 -0.0270 55  LYS   A CE  
1283 N NZ  . LYS   A 55  ? 0.2159 0.2757 0.2490 0.0717  -0.0287 -0.0208 55  LYS   A NZ  
1298 N N   . ALA   A 56  ? 0.1384 0.1639 0.1609 -0.0072 0.0048  -0.0238 56  ALA   A N   
1299 C CA  . ALA   A 56  ? 0.1486 0.1798 0.1562 -0.0084 0.0133  -0.0182 56  ALA   A CA  
1300 C C   . ALA   A 56  ? 0.1551 0.1928 0.1451 -0.0107 0.0150  -0.0242 56  ALA   A C   
1301 O O   . ALA   A 56  ? 0.1631 0.2285 0.1573 0.0015  0.0179  -0.0147 56  ALA   A O   
1302 C CB  . ALA   A 56  ? 0.1542 0.1975 0.1747 -0.0103 0.0117  -0.0098 56  ALA   A CB  
1308 N N   . THR   A 57  ? 0.1358 0.1681 0.1418 -0.0072 0.0126  -0.0183 57  THR   A N   
1309 C CA  . THR   A 57  ? 0.1427 0.1653 0.1407 -0.0036 0.0052  -0.0072 57  THR   A CA  
1310 C C   . THR   A 57  ? 0.1471 0.1692 0.1485 -0.0043 -0.0000 -0.0191 57  THR   A C   
1311 O O   . THR   A 57  ? 0.1441 0.1752 0.1673 -0.0132 -0.0086 -0.0271 57  THR   A O   
1312 C CB  . THR   A 57  ? 0.1396 0.1621 0.1423 -0.0088 0.0033  -0.0030 57  THR   A CB  
1313 O OG1 . THR   A 57  ? 0.1334 0.1568 0.1436 -0.0033 0.0032  -0.0056 57  THR   A OG1 
1314 C CG2 . THR   A 57  ? 0.1454 0.1646 0.1373 -0.0060 0.0006  0.0018  57  THR   A CG2 
1322 N N   . ASN   A 58  ? 0.1499 0.1647 0.1686 -0.0046 0.0040  -0.0309 58  ASN   A N   
1323 C CA  . ASN   A 58  ? 0.1673 0.1620 0.1867 -0.0059 0.0184  -0.0354 58  ASN   A CA  
1324 C C   . ASN   A 58  ? 0.1456 0.1496 0.1728 0.0015  0.0074  -0.0217 58  ASN   A C   
1325 O O   . ASN   A 58  ? 0.1510 0.1583 0.1868 -0.0136 0.0014  -0.0210 58  ASN   A O   
1326 C CB  . ASN   A 58  ? 0.2141 0.1795 0.2159 -0.0148 0.0425  -0.0417 58  ASN   A CB  
1327 C CG  . ASN   A 58  ? 0.2560 0.2054 0.2899 -0.0153 0.0403  -0.0256 58  ASN   A CG  
1328 O OD1 . ASN   A 58  ? 0.2837 0.2008 0.3343 0.0173  0.0682  -0.0232 58  ASN   A OD1 
1329 N ND2 . ASN   A 58  ? 0.2659 0.2146 0.3133 -0.0165 0.0237  -0.0330 58  ASN   A ND2 
1336 N N   . ASN   A 59  ? 0.1336 0.1435 0.1592 -0.0025 -0.0068 -0.0121 59  ASN   A N   
1337 C CA  . ASN   A 59  ? 0.1320 0.1294 0.1568 -0.0056 -0.0053 -0.0035 59  ASN   A CA  
1338 C C   . ASN   A 59  ? 0.1328 0.1326 0.1427 -0.0068 -0.0120 -0.0050 59  ASN   A C   
1339 O O   . ASN   A 59  ? 0.1340 0.1381 0.1614 -0.0078 0.0010  0.0056  59  ASN   A O   
1340 C CB  . ASN   A 59  ? 0.1371 0.1286 0.1679 0.0047  -0.0178 -0.0132 59  ASN   A CB  
1341 C CG  . ASN   A 59  ? 0.1371 0.1373 0.1686 0.0021  -0.0316 0.0028  59  ASN   A CG  
1342 O OD1 . ASN   A 59  ? 0.1531 0.1420 0.1696 -0.0078 -0.0254 0.0034  59  ASN   A OD1 
1343 N ND2 . ASN   A 59  ? 0.1494 0.1412 0.1820 -0.0140 -0.0180 0.0088  59  ASN   A ND2 
1350 N N   . ALA   A 60  ? 0.1252 0.1409 0.1476 0.0002  -0.0061 -0.0011 60  ALA   A N   
1351 C CA  . ALA   A 60  ? 0.1296 0.1379 0.1553 -0.0014 -0.0111 0.0019  60  ALA   A CA  
1352 C C   . ALA   A 60  ? 0.1288 0.1358 0.1671 -0.0008 -0.0025 0.0031  60  ALA   A C   
1353 O O   . ALA   A 60  ? 0.1232 0.1344 0.1841 -0.0013 -0.0113 0.0000  60  ALA   A O   
1354 C CB  . ALA   A 60  ? 0.1381 0.1554 0.1592 0.0035  -0.0166 -0.0175 60  ALA   A CB  
1360 N N   . MET   A 61  ? 0.1232 0.1282 0.1549 -0.0051 -0.0024 -0.0066 61  MET   A N   
1361 C CA  . MET   A 61  ? 0.1260 0.1248 0.1571 -0.0062 -0.0004 0.0023  61  MET   A CA  
1362 C C   . MET   A 61  ? 0.1243 0.1244 0.1575 -0.0075 -0.0029 -0.0038 61  MET   A C   
1363 O O   . MET   A 61  ? 0.1268 0.1234 0.1634 -0.0021 0.0075  0.0010  61  MET   A O   
1364 C CB  . MET   A 61  ? 0.1306 0.1280 0.1433 -0.0060 0.0052  -0.0052 61  MET   A CB  
1365 C CG  . MET   A 61  ? 0.1283 0.1336 0.1605 -0.0055 0.0003  0.0011  61  MET   A CG  
1366 S SD  . MET   A 61  ? 0.1327 0.1384 0.1932 -0.0099 0.0003  -0.0148 61  MET   A SD  
1367 C CE  . MET   A 61  ? 0.1559 0.1547 0.2123 -0.0132 0.0181  -0.0111 61  MET   A CE  
1377 N N   . GLN   A 62  ? 0.1253 0.1184 0.1528 -0.0056 -0.0011 -0.0005 62  GLN   A N   
1378 C CA  . GLN   A 62  ? 0.1293 0.1170 0.1574 -0.0037 0.0025  0.0071  62  GLN   A CA  
1379 C C   . GLN   A 62  ? 0.1297 0.1133 0.1616 -0.0005 0.0089  0.0038  62  GLN   A C   
1380 O O   . GLN   A 62  ? 0.1301 0.1258 0.1627 -0.0023 0.0058  0.0039  62  GLN   A O   
1381 C CB  . GLN   A 62  ? 0.1305 0.1127 0.1667 -0.0066 -0.0022 0.0072  62  GLN   A CB  
1382 C CG  . GLN   A 62  ? 0.1303 0.1148 0.1612 -0.0044 -0.0079 0.0140  62  GLN   A CG  
1383 C CD  . GLN   A 62  ? 0.1341 0.1214 0.1617 -0.0004 0.0020  0.0157  62  GLN   A CD  
1384 O OE1 . GLN   A 62  ? 0.1360 0.1360 0.1749 -0.0013 -0.0028 0.0028  62  GLN   A OE1 
1385 N NE2 . GLN   A 62  ? 0.1412 0.1289 0.1730 0.0036  -0.0039 0.0033  62  GLN   A NE2 
1394 N N   . VAL   A 63  ? 0.1255 0.1232 0.1748 -0.0037 0.0074  -0.0118 63  VAL   A N   
1395 C CA  . VAL   A 63  ? 0.1266 0.1321 0.1955 -0.0130 0.0029  -0.0120 63  VAL   A CA  
1396 C C   . VAL   A 63  ? 0.1146 0.1362 0.1936 -0.0156 -0.0081 -0.0075 63  VAL   A C   
1397 O O   . VAL   A 63  ? 0.1157 0.1318 0.2042 -0.0136 -0.0010 -0.0066 63  VAL   A O   
1398 C CB  . VAL   A 63  ? 0.1397 0.1471 0.2228 -0.0130 0.0000  -0.0346 63  VAL   A CB  
1399 C CG1 . VAL   A 63  ? 0.1540 0.1681 0.2533 -0.0128 -0.0124 -0.0554 63  VAL   A CG1 
1400 C CG2 . VAL   A 63  ? 0.1470 0.1383 0.2403 -0.0126 0.0173  -0.0339 63  VAL   A CG2 
1410 N N   . GLU   A 64  ? 0.1193 0.1408 0.1779 -0.0048 -0.0047 -0.0037 64  GLU   A N   
1411 C CA  . GLU   A 64  ? 0.1179 0.1401 0.1689 -0.0077 -0.0102 0.0006  64  GLU   A CA  
1412 C C   . GLU   A 64  ? 0.1129 0.1333 0.1682 -0.0112 0.0001  0.0082  64  GLU   A C   
1413 O O   . GLU   A 64  ? 0.1234 0.1391 0.1693 -0.0027 -0.0004 0.0050  64  GLU   A O   
1414 C CB  . GLU   A 64  ? 0.1310 0.1523 0.1754 -0.0045 0.0042  -0.0022 64  GLU   A CB  
1415 C CG  . GLU   A 64  ? 0.1393 0.1516 0.1894 -0.0079 -0.0013 -0.0046 64  GLU   A CG  
1416 C CD  . GLU   A 64  ? 0.1526 0.1583 0.1898 -0.0177 0.0057  0.0070  64  GLU   A CD  
1417 O OE1 . GLU   A 64  ? 0.1514 0.1691 0.2161 -0.0241 0.0095  0.0067  64  GLU   A OE1 
1418 O OE2 . GLU   A 64  ? 0.1688 0.1543 0.1875 -0.0227 -0.0008 0.0095  64  GLU   A OE2 
1425 N N   . SER   A 65  ? 0.1119 0.1312 0.1568 0.0035  0.0001  0.0041  65  SER   A N   
1426 C CA  . SER   A 65  ? 0.1234 0.1233 0.1506 -0.0015 -0.0011 0.0004  65  SER   A CA  
1427 C C   . SER   A 65  ? 0.1247 0.1315 0.1563 -0.0027 -0.0044 0.0007  65  SER   A C   
1428 O O   . SER   A 65  ? 0.1343 0.1367 0.1707 0.0008  0.0137  -0.0022 65  SER   A O   
1429 C CB  . SER   A 65  ? 0.1268 0.1261 0.1606 -0.0094 -0.0011 0.0077  65  SER   A CB  
1430 O OG  . SER   A 65  ? 0.1234 0.1335 0.1729 -0.0089 -0.0034 0.0105  65  SER   A OG  
1436 N N   . ASP   A 66  ? 0.1294 0.1281 0.1597 -0.0018 0.0163  0.0077  66  ASP   A N   
1437 C CA  . ASP   A 66  ? 0.1376 0.1384 0.1781 -0.0022 0.0071  0.0177  66  ASP   A CA  
1438 C C   . ASP   A 66  ? 0.1309 0.1320 0.1838 -0.0106 0.0091  0.0164  66  ASP   A C   
1439 O O   . ASP   A 66  ? 0.1382 0.1464 0.2031 -0.0039 0.0258  0.0225  66  ASP   A O   
1440 C CB  . ASP   A 66  ? 0.1430 0.1458 0.2045 0.0049  0.0108  0.0289  66  ASP   A CB  
1441 C CG  . ASP   A 66  ? 0.1682 0.1585 0.2285 0.0004  0.0041  0.0466  66  ASP   A CG  
1442 O OD1 . ASP   A 66  ? 0.1679 0.1922 0.2146 -0.0101 -0.0033 0.0461  66  ASP   A OD1 
1443 O OD2 . ASP   A 66  ? 0.1836 0.1760 0.3135 0.0205  -0.0155 0.0306  66  ASP   A OD2 
1448 N N   . ASP   A 67  ? 0.1216 0.1347 0.1898 -0.0076 0.0056  0.0142  67  ASP   A N   
1449 C CA  . ASP   A 67  ? 0.1281 0.1516 0.2038 -0.0031 0.0036  0.0250  67  ASP   A CA  
1450 C C   . ASP   A 67  ? 0.1298 0.1574 0.2012 0.0029  0.0084  0.0252  67  ASP   A C   
1451 O O   . ASP   A 67  ? 0.1212 0.1655 0.2206 0.0015  0.0240  0.0333  67  ASP   A O   
1452 C CB  . ASP   A 67  ? 0.1337 0.1616 0.2282 -0.0038 -0.0060 0.0317  67  ASP   A CB  
1453 C CG  . ASP   A 67  ? 0.1326 0.1767 0.2746 -0.0084 -0.0232 0.0407  67  ASP   A CG  
1454 O OD1 . ASP   A 67  ? 0.1370 0.2006 0.3646 -0.0165 -0.0332 0.0524  67  ASP   A OD1 
1455 O OD2 . ASP   A 67  ? 0.1353 0.1789 0.2569 0.0004  -0.0170 0.0304  67  ASP   A OD2 
1460 N N   . TYR   A 68  ? 0.1298 0.1404 0.1856 0.0035  0.0167  0.0274  68  TYR   A N   
1461 C CA  . TYR   A 68  ? 0.1418 0.1358 0.1835 0.0038  0.0207  0.0305  68  TYR   A CA  
1462 C C   . TYR   A 68  ? 0.1354 0.1405 0.1952 0.0010  0.0264  0.0224  68  TYR   A C   
1463 O O   . TYR   A 68  ? 0.1427 0.1475 0.1991 0.0081  0.0320  0.0241  68  TYR   A O   
1464 C CB  . TYR   A 68  ? 0.1422 0.1362 0.2020 0.0084  0.0351  0.0323  68  TYR   A CB  
1465 C CG  . TYR   A 68  ? 0.1442 0.1526 0.2323 0.0074  0.0506  0.0310  68  TYR   A CG  
1466 C CD1 . TYR   A 68  ? 0.1527 0.1587 0.2677 -0.0206 0.0415  0.0006  68  TYR   A CD1 
1467 C CD2 . TYR   A 68  ? 0.1707 0.1575 0.2750 0.0124  0.0514  0.0407  68  TYR   A CD2 
1468 C CE1 . TYR   A 68  ? 0.1650 0.1657 0.3061 -0.0127 0.0459  -0.0014 68  TYR   A CE1 
1469 C CE2 . TYR   A 68  ? 0.1680 0.1606 0.2914 0.0030  0.0643  0.0180  68  TYR   A CE2 
1470 C CZ  . TYR   A 68  ? 0.1641 0.1608 0.3151 -0.0112 0.0524  -0.0082 68  TYR   A CZ  
1471 O OH  . TYR   A 68  ? 0.1984 0.1577 0.3270 -0.0111 0.0355  -0.0309 68  TYR   A OH  
1481 N N   . ILE   A 69  ? 0.1265 0.1319 0.1876 -0.0013 0.0189  0.0212  69  ILE   A N   
1482 C CA  . ILE   A 69  ? 0.1339 0.1351 0.1840 0.0059  0.0095  0.0035  69  ILE   A CA  
1483 C C   . ILE   A 69  ? 0.1398 0.1347 0.1740 0.0048  0.0177  0.0135  69  ILE   A C   
1484 O O   . ILE   A 69  ? 0.1438 0.1453 0.1807 -0.0014 0.0259  0.0197  69  ILE   A O   
1485 C CB  . ILE   A 69  ? 0.1446 0.1543 0.1881 0.0033  0.0100  -0.0044 69  ILE   A CB  
1486 C CG1 . ILE   A 69  ? 0.1446 0.1670 0.2003 0.0091  0.0190  -0.0209 69  ILE   A CG1 
1487 C CG2 . ILE   A 69  ? 0.1624 0.1745 0.1964 0.0127  0.0044  -0.0107 69  ILE   A CG2 
1488 C CD1 . ILE   A 69  ? 0.1472 0.1760 0.2155 -0.0079 0.0194  -0.0255 69  ILE   A CD1 
1500 N N   . ALA   A 70  ? 0.1426 0.1402 0.1773 -0.0022 0.0169  0.0208  70  ALA   A N   
1501 C CA  . ALA   A 70  ? 0.1421 0.1557 0.2009 -0.0139 0.0307  0.0251  70  ALA   A CA  
1502 C C   . ALA   A 70  ? 0.1415 0.1700 0.2050 -0.0108 0.0279  0.0242  70  ALA   A C   
1503 O O   . ALA   A 70  ? 0.1599 0.2028 0.2232 0.0099  0.0491  0.0453  70  ALA   A O   
1504 C CB  . ALA   A 70  ? 0.1486 0.1501 0.2253 -0.0157 0.0260  0.0205  70  ALA   A CB  
1510 N N   . THR   A 71  ? 0.1358 0.1638 0.1949 -0.0051 0.0208  0.0282  71  THR   A N   
1511 C CA  . THR   A 71  ? 0.1429 0.1809 0.2226 0.0089  0.0230  0.0306  71  THR   A CA  
1512 C C   . THR   A 71  ? 0.1318 0.1688 0.2529 0.0122  0.0301  0.0244  71  THR   A C   
1513 O O   . THR   A 71  ? 0.1390 0.1979 0.3022 0.0084  0.0434  -0.0035 71  THR   A O   
1514 C CB  . THR   A 71  ? 0.1723 0.2087 0.2501 0.0176  -0.0123 0.0362  71  THR   A CB  
1515 O OG1 . THR   A 71  ? 0.2003 0.2254 0.2608 0.0055  -0.0409 0.0297  71  THR   A OG1 
1516 C CG2 . THR   A 71  ? 0.1859 0.2287 0.2793 0.0232  -0.0165 0.0513  71  THR   A CG2 
1524 N N   . ASN   A 72  ? 0.1372 0.1525 0.2241 0.0138  0.0259  0.0247  72  ASN   A N   
1525 C CA  . ASN   A 72  ? 0.1474 0.1551 0.2302 0.0163  0.0337  0.0188  72  ASN   A CA  
1526 C C   . ASN   A 72  ? 0.1650 0.1532 0.2159 0.0119  0.0474  0.0156  72  ASN   A C   
1527 O O   . ASN   A 72  ? 0.1815 0.1552 0.2528 0.0162  0.0448  0.0017  72  ASN   A O   
1528 C CB  . ASN   A 72  ? 0.1680 0.1641 0.2369 0.0160  0.0437  0.0257  72  ASN   A CB  
1529 C CG  . ASN   A 72  ? 0.1924 0.1753 0.2374 0.0215  0.0382  0.0328  72  ASN   A CG  
1530 O OD1 . ASN   A 72  ? 0.2098 0.2126 0.2526 0.0249  0.0444  0.0308  72  ASN   A OD1 
1531 N ND2 . ASN   A 72  ? 0.2110 0.1752 0.2351 0.0507  0.0176  0.0203  72  ASN   A ND2 
1538 N N   . GLY   A 73  ? 0.1689 0.1519 0.1959 0.0078  0.0445  0.0104  73  GLY   A N   
1539 C CA  . GLY   A 73  ? 0.1711 0.1516 0.1823 -0.0007 0.0450  0.0125  73  GLY   A CA  
1540 C C   . GLY   A 73  ? 0.1672 0.1386 0.1661 0.0025  0.0510  0.0249  73  GLY   A C   
1541 O O   . GLY   A 73  ? 0.1626 0.1470 0.1832 0.0109  0.0367  0.0271  73  GLY   A O   
1545 N N   . PRO   A 74  ? 0.1798 0.1436 0.1734 -0.0105 0.0503  0.0144  74  PRO   A N   
1546 C CA  . PRO   A 74  ? 0.1754 0.1424 0.1858 -0.0044 0.0434  0.0159  74  PRO   A CA  
1547 C C   . PRO   A 74  ? 0.1675 0.1277 0.1815 -0.0031 0.0373  0.0027  74  PRO   A C   
1548 O O   . PRO   A 74  ? 0.1775 0.1361 0.2065 0.0049  0.0411  0.0015  74  PRO   A O   
1549 C CB  . PRO   A 74  ? 0.1907 0.1711 0.2086 -0.0016 0.0426  0.0270  74  PRO   A CB  
1550 C CG  . PRO   A 74  ? 0.2157 0.2080 0.2477 -0.0161 0.0372  0.0195  74  PRO   A CG  
1551 C CD  . PRO   A 74  ? 0.1952 0.1823 0.1939 -0.0203 0.0427  0.0111  74  PRO   A CD  
1559 N N   . LEU   A 75  ? 0.1649 0.1213 0.1739 0.0010  0.0307  0.0057  75  LEU   A N   
1560 C CA  . LEU   A 75  ? 0.1633 0.1220 0.1547 -0.0029 0.0075  0.0146  75  LEU   A CA  
1561 C C   . LEU   A 75  ? 0.1774 0.1330 0.1547 0.0052  0.0192  0.0165  75  LEU   A C   
1562 O O   . LEU   A 75  ? 0.2113 0.1474 0.1633 0.0084  0.0120  0.0080  75  LEU   A O   
1563 C CB  . LEU   A 75  ? 0.1675 0.1290 0.1548 -0.0113 0.0070  0.0174  75  LEU   A CB  
1564 C CG  . LEU   A 75  ? 0.1850 0.1650 0.1590 -0.0366 0.0072  0.0147  75  LEU   A CG  
1565 C CD1 . LEU   A 75  ? 0.1943 0.2135 0.1754 -0.0375 0.0055  0.0033  75  LEU   A CD1 
1566 C CD2 . LEU   A 75  ? 0.2128 0.2024 0.2230 -0.0095 0.0135  0.0113  75  LEU   A CD2 
1578 N N   . LYS   A 76  ? 0.1747 0.1292 0.1735 -0.0054 0.0111  0.0049  76  LYS   A N   
1579 C CA  . LYS   A 76  ? 0.1722 0.1494 0.1663 -0.0102 0.0113  -0.0004 76  LYS   A CA  
1580 C C   . LYS   A 76  ? 0.1709 0.1385 0.1433 -0.0044 0.0075  0.0039  76  LYS   A C   
1581 O O   . LYS   A 76  ? 0.1714 0.1292 0.1528 -0.0024 0.0139  0.0147  76  LYS   A O   
1582 C CB  . LYS   A 76  ? 0.1771 0.1705 0.2131 0.0031  0.0137  -0.0276 76  LYS   A CB  
1583 C CG  . LYS   A 76  ? 0.1852 0.1663 0.2611 0.0050  0.0068  -0.0280 76  LYS   A CG  
1584 C CD  . LYS   A 76  ? 0.1910 0.1671 0.2989 0.0073  -0.0049 -0.0357 76  LYS   A CD  
1585 C CE  . LYS   A 76  ? 0.2071 0.1861 0.3574 -0.0029 -0.0019 -0.0377 76  LYS   A CE  
1586 N NZ  . LYS   A 76  ? 0.2074 0.1767 0.4031 -0.0214 -0.0075 -0.0463 76  LYS   A NZ  
1600 N N   . VAL   A 77  ? 0.1819 0.1457 0.1430 -0.0073 0.0210  0.0138  77  VAL   A N   
1601 C CA  . VAL   A 77  ? 0.1790 0.1448 0.1515 0.0003  0.0106  0.0144  77  VAL   A CA  
1602 C C   . VAL   A 77  ? 0.1731 0.1374 0.1491 0.0063  0.0094  0.0061  77  VAL   A C   
1603 O O   . VAL   A 77  ? 0.1816 0.1443 0.1470 0.0069  0.0226  0.0004  77  VAL   A O   
1604 C CB  . VAL   A 77  ? 0.1950 0.1647 0.1723 -0.0021 0.0031  0.0192  77  VAL   A CB  
1605 C CG1 . VAL   A 77  ? 0.1941 0.1761 0.1940 0.0091  -0.0053 0.0072  77  VAL   A CG1 
1606 C CG2 . VAL   A 77  ? 0.2221 0.1737 0.1911 -0.0068 -0.0099 0.0252  77  VAL   A CG2 
1616 N N   . GLY   A 78  ? 0.1690 0.1317 0.1396 0.0021  0.0195  0.0083  78  GLY   A N   
1617 C CA  . GLY   A 78  ? 0.1652 0.1303 0.1519 0.0015  0.0200  0.0043  78  GLY   A CA  
1618 C C   . GLY   A 78  ? 0.1515 0.1258 0.1561 0.0054  0.0156  0.0186  78  GLY   A C   
1619 O O   . GLY   A 78  ? 0.1445 0.1346 0.1822 0.0019  0.0144  0.0262  78  GLY   A O   
1623 N N   . GLY   A 79  ? 0.1534 0.1213 0.1546 -0.0074 0.0110  0.0194  79  GLY   A N   
1624 C CA  . GLY   A 79  ? 0.1485 0.1269 0.1637 -0.0024 0.0151  0.0193  79  GLY   A CA  
1625 C C   . GLY   A 79  ? 0.1336 0.1234 0.1593 -0.0037 0.0150  0.0050  79  GLY   A C   
1626 O O   . GLY   A 79  ? 0.1384 0.1357 0.1721 0.0159  0.0121  0.0062  79  GLY   A O   
1630 N N   . SER   A 80  ? 0.1285 0.1416 0.1895 -0.0044 0.0131  -0.0026 80  SER   A N   
1631 C CA  . SER   A 80  ? 0.1205 0.1318 0.1737 -0.0046 0.0106  0.0053  80  SER   A CA  
1632 C C   . SER   A 80  ? 0.1245 0.1330 0.1699 -0.0053 0.0086  0.0171  80  SER   A C   
1633 O O   . SER   A 80  ? 0.1241 0.1567 0.2024 0.0049  0.0159  0.0010  80  SER   A O   
1634 C CB  . SER   A 80  ? 0.1378 0.1277 0.1959 -0.0097 0.0000  0.0100  80  SER   A CB  
1635 O OG  . SER   A 80  ? 0.1624 0.1321 0.2393 0.0038  -0.0071 0.0256  80  SER   A OG  
1641 N N   . CYS   A 81  ? 0.1259 0.1297 0.1617 -0.0015 0.0002  0.0209  81  CYS   A N   
1642 C CA  . CYS   A 81  ? 0.1187 0.1399 0.1533 -0.0038 -0.0080 0.0255  81  CYS   A CA  
1643 C C   . CYS   A 81  ? 0.1241 0.1327 0.1589 -0.0083 -0.0029 0.0280  81  CYS   A C   
1644 O O   . CYS   A 81  ? 0.1203 0.1607 0.1753 -0.0019 0.0049  0.0343  81  CYS   A O   
1645 C CB  . CYS   A 81  ? 0.1257 0.1472 0.1683 -0.0100 -0.0006 0.0254  81  CYS   A CB  
1646 S SG  . CYS   A 81  ? 0.1452 0.1330 0.1719 -0.0142 0.0027  0.0155  81  CYS   A SG  
1652 N N   . VAL   A 82  ? 0.1289 0.1428 0.1626 0.0005  -0.0050 0.0237  82  VAL   A N   
1653 C CA  . VAL   A 82  ? 0.1356 0.1442 0.1624 0.0038  -0.0094 0.0259  82  VAL   A CA  
1654 C C   . VAL   A 82  ? 0.1349 0.1523 0.1563 -0.0018 -0.0072 0.0264  82  VAL   A C   
1655 O O   . VAL   A 82  ? 0.1302 0.1556 0.1931 -0.0028 -0.0025 0.0024  82  VAL   A O   
1656 C CB  . VAL   A 82  ? 0.1691 0.1585 0.1714 0.0027  -0.0040 0.0241  82  VAL   A CB  
1657 C CG1 . VAL   A 82  ? 0.1946 0.1691 0.1958 0.0098  -0.0013 0.0249  82  VAL   A CG1 
1658 C CG2 . VAL   A 82  ? 0.1770 0.1636 0.1977 -0.0076 -0.0055 0.0328  82  VAL   A CG2 
1668 N N   . LEU   A 83  ? 0.1327 0.1436 0.1619 -0.0070 -0.0026 0.0189  83  LEU   A N   
1669 C CA  . LEU   A 83  ? 0.1360 0.1425 0.1572 -0.0042 -0.0075 0.0158  83  LEU   A CA  
1670 C C   . LEU   A 83  ? 0.1407 0.1494 0.1474 -0.0054 -0.0070 0.0197  83  LEU   A C   
1671 O O   . LEU   A 83  ? 0.1530 0.1516 0.1584 -0.0131 -0.0050 0.0295  83  LEU   A O   
1672 C CB  . LEU   A 83  ? 0.1407 0.1499 0.1631 -0.0143 -0.0135 0.0181  83  LEU   A CB  
1673 C CG  . LEU   A 83  ? 0.1552 0.1643 0.1761 -0.0129 0.0019  0.0138  83  LEU   A CG  
1674 C CD1 . LEU   A 83  ? 0.1638 0.1650 0.1674 -0.0214 0.0035  0.0293  83  LEU   A CD1 
1675 C CD2 . LEU   A 83  ? 0.1506 0.1800 0.1851 -0.0120 0.0137  0.0277  83  LEU   A CD2 
1687 N N   . SER   A 84  ? 0.1593 0.1548 0.1555 -0.0074 -0.0082 0.0223  84  SER   A N   
1688 C CA  . SER   A 84  ? 0.1659 0.1570 0.1436 -0.0109 -0.0082 0.0237  84  SER   A CA  
1689 C C   . SER   A 84  ? 0.1694 0.1611 0.1451 -0.0155 0.0045  0.0113  84  SER   A C   
1690 O O   . SER   A 84  ? 0.1590 0.1739 0.1408 -0.0088 -0.0072 0.0113  84  SER   A O   
1691 C CB  . SER   A 84  ? 0.1774 0.1833 0.1551 -0.0104 -0.0087 0.0156  84  SER   A CB  
1692 O OG  . SER   A 84  ? 0.1799 0.2035 0.1640 -0.0108 -0.0131 0.0053  84  SER   A OG  
1698 N N   . GLY   A 85  ? 0.1823 0.1751 0.1512 -0.0228 0.0081  0.0132  85  GLY   A N   
1699 C CA  . GLY   A 85  ? 0.1847 0.1818 0.1628 -0.0256 0.0136  -0.0003 85  GLY   A CA  
1700 C C   . GLY   A 85  ? 0.1876 0.1925 0.1344 -0.0176 -0.0008 0.0033  85  GLY   A C   
1701 O O   . GLY   A 85  ? 0.1861 0.2027 0.1597 -0.0241 0.0203  -0.0064 85  GLY   A O   
1705 N N   . HIS   A 86  ? 0.1898 0.1871 0.1292 -0.0137 -0.0044 0.0101  86  HIS   A N   
1706 C CA  . HIS   A 86  ? 0.2088 0.1930 0.1342 -0.0153 -0.0027 0.0092  86  HIS   A CA  
1707 C C   . HIS   A 86  ? 0.2356 0.2103 0.1202 -0.0141 -0.0074 0.0106  86  HIS   A C   
1708 O O   . HIS   A 86  ? 0.2481 0.2293 0.1363 -0.0089 0.0001  0.0055  86  HIS   A O   
1709 C CB  . HIS   A 86  ? 0.2023 0.1803 0.1466 -0.0114 -0.0014 0.0103  86  HIS   A CB  
1710 C CG  . HIS   A 86  ? 0.1942 0.1801 0.1454 -0.0049 0.0069  0.0192  86  HIS   A CG  
1711 N ND1 . HIS   A 86  ? 0.1981 0.1798 0.1818 -0.0146 -0.0036 0.0160  86  HIS   A ND1 
1712 C CD2 . HIS   A 86  ? 0.1939 0.1765 0.1368 0.0036  0.0069  0.0214  86  HIS   A CD2 
1713 C CE1 . HIS   A 86  ? 0.1918 0.1791 0.1739 -0.0142 0.0161  0.0184  86  HIS   A CE1 
1714 N NE2 . HIS   A 86  ? 0.1895 0.1757 0.1561 0.0033  0.0153  0.0242  86  HIS   A NE2 
1722 N N   . ASN   A 87  ? 0.2489 0.2165 0.1399 -0.0081 0.0151  -0.0032 87  ASN   A N   
1723 C CA  . ASN   A 87  ? 0.2652 0.2242 0.1422 -0.0070 0.0373  -0.0090 87  ASN   A CA  
1724 C C   . ASN   A 87  ? 0.2574 0.2454 0.1698 -0.0174 0.0566  0.0020  87  ASN   A C   
1725 O O   . ASN   A 87  ? 0.2842 0.2699 0.2148 -0.0359 0.0911  -0.0095 87  ASN   A O   
1726 C CB  . ASN   A 87  ? 0.2856 0.2285 0.1591 0.0061  0.0427  -0.0059 87  ASN   A CB  
1727 C CG  . ASN   A 87  ? 0.2982 0.2398 0.1645 0.0182  0.0575  -0.0011 87  ASN   A CG  
1728 O OD1 . ASN   A 87  ? 0.3136 0.2354 0.1747 0.0365  0.0529  0.0044  87  ASN   A OD1 
1729 N ND2 . ASN   A 87  ? 0.3034 0.2665 0.1889 0.0165  0.0653  0.0031  87  ASN   A ND2 
1736 N N   A LEU   A 88  ? 0.2317 0.2361 0.1618 -0.0174 0.0380  0.0140  88  LEU   A N   
1737 N N   B LEU   A 88  ? 0.2383 0.2402 0.1703 -0.0184 0.0457  0.0077  88  LEU   A N   
1738 C CA  A LEU   A 88  ? 0.2089 0.2280 0.1794 -0.0197 0.0373  0.0369  88  LEU   A CA  
1739 C CA  B LEU   A 88  ? 0.2207 0.2356 0.1844 -0.0203 0.0433  0.0190  88  LEU   A CA  
1740 C C   A LEU   A 88  ? 0.1999 0.2303 0.1676 -0.0207 0.0347  0.0430  88  LEU   A C   
1741 C C   B LEU   A 88  ? 0.2085 0.2333 0.1750 -0.0203 0.0376  0.0324  88  LEU   A C   
1742 O O   A LEU   A 88  ? 0.2049 0.2357 0.2033 -0.0177 0.0424  0.0547  88  LEU   A O   
1743 O O   B LEU   A 88  ? 0.2099 0.2357 0.1930 -0.0191 0.0449  0.0483  88  LEU   A O   
1744 C CB  A LEU   A 88  ? 0.2071 0.2364 0.1936 -0.0183 0.0049  0.0376  88  LEU   A CB  
1745 C CB  B LEU   A 88  ? 0.2205 0.2414 0.1991 -0.0215 0.0321  0.0105  88  LEU   A CB  
1746 C CG  A LEU   A 88  ? 0.2216 0.2452 0.2158 -0.0168 -0.0044 0.0443  88  LEU   A CG  
1747 C CG  B LEU   A 88  ? 0.2249 0.2465 0.2118 -0.0211 0.0279  0.0066  88  LEU   A CG  
1748 C CD1 A LEU   A 88  ? 0.2292 0.2510 0.2147 -0.0172 -0.0108 0.0380  88  LEU   A CD1 
1749 C CD1 B LEU   A 88  ? 0.2260 0.2493 0.2092 -0.0222 0.0276  -0.0001 88  LEU   A CD1 
1750 C CD2 A LEU   A 88  ? 0.2347 0.2561 0.2476 -0.0127 -0.0004 0.0370  88  LEU   A CD2 
1751 C CD2 B LEU   A 88  ? 0.2304 0.2517 0.2265 -0.0177 0.0275  0.0041  88  LEU   A CD2 
1774 N N   . ALA   A 89  ? 0.2005 0.2283 0.1630 -0.0172 0.0245  0.0209  89  ALA   A N   
1775 C CA  . ALA   A 89  ? 0.2073 0.2257 0.1486 -0.0140 0.0094  0.0296  89  ALA   A CA  
1776 C C   . ALA   A 89  ? 0.2105 0.2257 0.1527 -0.0054 -0.0040 0.0236  89  ALA   A C   
1777 O O   . ALA   A 89  ? 0.2079 0.2204 0.1927 -0.0173 -0.0114 -0.0059 89  ALA   A O   
1778 C CB  . ALA   A 89  ? 0.2041 0.2204 0.1355 -0.0166 0.0115  0.0257  89  ALA   A CB  
1785 N N   . LYS   A 90  ? 0.2235 0.2388 0.1513 -0.0182 -0.0141 0.0243  90  LYS   A N   
1786 C CA  . LYS   A 90  ? 0.2326 0.2549 0.1482 -0.0177 -0.0259 0.0308  90  LYS   A CA  
1787 C C   . LYS   A 90  ? 0.2079 0.2352 0.1467 -0.0238 -0.0232 0.0167  90  LYS   A C   
1788 O O   . LYS   A 90  ? 0.2062 0.2448 0.1800 -0.0258 -0.0307 0.0072  90  LYS   A O   
1789 C CB  . LYS   A 90  ? 0.2660 0.2956 0.1877 -0.0183 -0.0263 0.0580  90  LYS   A CB  
1790 C CG  . LYS   A 90  ? 0.3120 0.3361 0.2906 -0.0170 -0.0202 0.0644  90  LYS   A CG  
1791 C CD  . LYS   A 90  ? 0.3620 0.3787 0.3980 -0.0195 -0.0049 0.0628  90  LYS   A CD  
1792 C CE  . LYS   A 90  ? 0.4072 0.4188 0.4798 -0.0220 0.0051  0.0556  90  LYS   A CE  
1793 N NZ  . LYS   A 90  ? 0.4235 0.4321 0.5327 -0.0241 0.0109  0.0534  90  LYS   A NZ  
1807 N N   . HIS   A 91  ? 0.1909 0.2062 0.1232 -0.0216 -0.0262 0.0216  91  HIS   A N   
1808 C CA  . HIS   A 91  ? 0.1796 0.1822 0.1352 -0.0137 -0.0207 0.0247  91  HIS   A CA  
1809 C C   . HIS   A 91  ? 0.1611 0.1717 0.1232 -0.0106 -0.0143 0.0223  91  HIS   A C   
1810 O O   . HIS   A 91  ? 0.1561 0.1834 0.1479 -0.0184 0.0027  0.0249  91  HIS   A O   
1811 C CB  . HIS   A 91  ? 0.1973 0.2104 0.1848 0.0091  -0.0314 0.0221  91  HIS   A CB  
1812 C CG  . HIS   A 91  ? 0.2368 0.2637 0.2425 0.0208  -0.0572 0.0115  91  HIS   A CG  
1813 N ND1 . HIS   A 91  ? 0.2479 0.2939 0.2797 0.0248  -0.0650 -0.0114 91  HIS   A ND1 
1814 C CD2 . HIS   A 91  ? 0.2636 0.2851 0.2681 0.0276  -0.0708 0.0223  91  HIS   A CD2 
1815 C CE1 . HIS   A 91  ? 0.2606 0.3026 0.2918 0.0292  -0.0652 0.0041  91  HIS   A CE1 
1816 N NE2 . HIS   A 91  ? 0.2750 0.3006 0.2893 0.0368  -0.0720 0.0156  91  HIS   A NE2 
1824 N N   . CYS   A 92  ? 0.1509 0.1624 0.1295 -0.0175 -0.0143 0.0171  92  CYS   A N   
1825 C CA  . CYS   A 92  ? 0.1408 0.1554 0.1443 -0.0141 -0.0007 0.0173  92  CYS   A CA  
1826 C C   . CYS   A 92  ? 0.1348 0.1488 0.1318 -0.0111 0.0027  0.0205  92  CYS   A C   
1827 O O   . CYS   A 92  ? 0.1352 0.1540 0.1590 -0.0171 -0.0037 0.0169  92  CYS   A O   
1828 C CB  . CYS   A 92  ? 0.1410 0.1537 0.1604 -0.0076 -0.0042 0.0127  92  CYS   A CB  
1829 S SG  . CYS   A 92  ? 0.1434 0.1428 0.1440 -0.0111 -0.0002 0.0143  92  CYS   A SG  
1835 N N   . LEU   A 93  ? 0.1337 0.1352 0.1428 -0.0149 0.0065  0.0204  93  LEU   A N   
1836 C CA  . LEU   A 93  ? 0.1240 0.1341 0.1506 -0.0110 0.0030  0.0205  93  LEU   A CA  
1837 C C   . LEU   A 93  ? 0.1229 0.1238 0.1445 -0.0018 0.0042  0.0128  93  LEU   A C   
1838 O O   . LEU   A 93  ? 0.1203 0.1287 0.1487 -0.0025 0.0014  0.0155  93  LEU   A O   
1839 C CB  . LEU   A 93  ? 0.1354 0.1305 0.1608 -0.0029 -0.0010 0.0285  93  LEU   A CB  
1840 C CG  . LEU   A 93  ? 0.1385 0.1283 0.1562 -0.0060 0.0061  0.0230  93  LEU   A CG  
1841 C CD1 . LEU   A 93  ? 0.1437 0.1337 0.1963 -0.0062 0.0170  0.0157  93  LEU   A CD1 
1842 C CD2 . LEU   A 93  ? 0.1525 0.1343 0.1851 -0.0076 0.0058  0.0262  93  LEU   A CD2 
1854 N N   . HIS   A 94  ? 0.1207 0.1193 0.1470 -0.0028 0.0067  0.0204  94  HIS   A N   
1855 C CA  . HIS   A 94  ? 0.1189 0.1190 0.1496 -0.0053 0.0012  0.0234  94  HIS   A CA  
1856 C C   . HIS   A 94  ? 0.1138 0.1189 0.1427 -0.0045 -0.0009 0.0157  94  HIS   A C   
1857 O O   . HIS   A 94  ? 0.1161 0.1400 0.1809 0.0033  -0.0013 -0.0011 94  HIS   A O   
1858 C CB  . HIS   A 94  ? 0.1210 0.1173 0.1556 -0.0044 -0.0010 0.0212  94  HIS   A CB  
1859 C CG  . HIS   A 94  ? 0.1241 0.1150 0.1432 -0.0054 0.0010  0.0166  94  HIS   A CG  
1860 N ND1 . HIS   A 94  ? 0.1207 0.1172 0.1604 -0.0054 0.0021  0.0183  94  HIS   A ND1 
1861 C CD2 . HIS   A 94  ? 0.1326 0.1323 0.1506 -0.0089 -0.0029 0.0136  94  HIS   A CD2 
1862 C CE1 . HIS   A 94  ? 0.1291 0.1209 0.1557 -0.0112 -0.0048 0.0107  94  HIS   A CE1 
1863 N NE2 . HIS   A 94  ? 0.1302 0.1271 0.1515 -0.0120 -0.0100 0.0054  94  HIS   A NE2 
1871 N N   . VAL   A 95  ? 0.1143 0.1116 0.1370 0.0009  0.0083  0.0111  95  VAL   A N   
1872 C CA  . VAL   A 95  ? 0.1226 0.1214 0.1357 -0.0048 0.0152  0.0164  95  VAL   A CA  
1873 C C   . VAL   A 95  ? 0.1226 0.1192 0.1294 -0.0114 0.0067  0.0124  95  VAL   A C   
1874 O O   . VAL   A 95  ? 0.1300 0.1282 0.1478 0.0060  0.0039  0.0122  95  VAL   A O   
1875 C CB  . VAL   A 95  ? 0.1243 0.1173 0.1590 -0.0137 0.0085  0.0107  95  VAL   A CB  
1876 C CG1 . VAL   A 95  ? 0.1424 0.1214 0.1686 -0.0178 0.0027  0.0042  95  VAL   A CG1 
1877 C CG2 . VAL   A 95  ? 0.1262 0.1250 0.1608 -0.0137 0.0076  0.0237  95  VAL   A CG2 
1887 N N   . VAL   A 96  ? 0.1293 0.1207 0.1270 -0.0050 0.0015  0.0193  96  VAL   A N   
1888 C CA  . VAL   A 96  ? 0.1379 0.1208 0.1454 -0.0045 0.0041  0.0204  96  VAL   A CA  
1889 C C   . VAL   A 96  ? 0.1395 0.1304 0.1568 -0.0077 0.0069  0.0212  96  VAL   A C   
1890 O O   . VAL   A 96  ? 0.1473 0.1335 0.1745 -0.0082 0.0160  0.0018  96  VAL   A O   
1891 C CB  . VAL   A 96  ? 0.1398 0.1276 0.1527 -0.0058 0.0189  0.0129  96  VAL   A CB  
1892 C CG1 . VAL   A 96  ? 0.1487 0.1296 0.1431 -0.0020 0.0164  0.0128  96  VAL   A CG1 
1893 C CG2 . VAL   A 96  ? 0.1417 0.1347 0.1654 -0.0189 0.0170  0.0130  96  VAL   A CG2 
1903 N N   A GLY   A 97  ? 0.1382 0.1339 0.1538 -0.0112 0.0041  0.0203  97  GLY   A N   
1904 N N   B GLY   A 97  ? 0.1401 0.1369 0.1393 -0.0139 0.0003  0.0161  97  GLY   A N   
1905 C CA  A GLY   A 97  ? 0.1503 0.1538 0.1516 -0.0073 -0.0005 0.0194  97  GLY   A CA  
1906 C CA  B GLY   A 97  ? 0.1471 0.1461 0.1389 -0.0141 -0.0033 0.0191  97  GLY   A CA  
1907 C C   A GLY   A 97  ? 0.1540 0.1659 0.1381 -0.0028 0.0027  0.0129  97  GLY   A C   
1908 C C   B GLY   A 97  ? 0.1505 0.1489 0.1440 -0.0120 -0.0048 0.0217  97  GLY   A C   
1909 O O   A GLY   A 97  ? 0.1594 0.1641 0.1447 -0.0002 0.0121  0.0136  97  GLY   A O   
1910 O O   B GLY   A 97  ? 0.1527 0.1463 0.1566 -0.0196 0.0030  0.0255  97  GLY   A O   
1917 N N   A PRO   A 98  ? 0.1627 0.1657 0.1310 0.0011  -0.0072 0.0137  98  PRO   A N   
1918 N N   B PRO   A 98  ? 0.1618 0.1511 0.1494 -0.0013 -0.0043 0.0240  98  PRO   A N   
1919 C CA  A PRO   A 98  ? 0.1722 0.1799 0.1303 -0.0045 -0.0083 0.0087  98  PRO   A CA  
1920 C CA  B PRO   A 98  ? 0.1755 0.1577 0.1569 0.0014  -0.0004 0.0130  98  PRO   A CA  
1921 C C   A PRO   A 98  ? 0.1724 0.1885 0.1212 -0.0138 -0.0084 0.0171  98  PRO   A C   
1922 C C   B PRO   A 98  ? 0.1978 0.1589 0.1522 0.0006  -0.0010 0.0130  98  PRO   A C   
1923 O O   A PRO   A 98  ? 0.1704 0.1729 0.1242 -0.0091 -0.0033 0.0055  98  PRO   A O   
1924 O O   B PRO   A 98  ? 0.1962 0.1563 0.1666 -0.0029 0.0071  0.0143  98  PRO   A O   
1925 C CB  A PRO   A 98  ? 0.1784 0.1864 0.1249 0.0067  -0.0149 -0.0030 98  PRO   A CB  
1926 C CB  B PRO   A 98  ? 0.1748 0.1541 0.1506 0.0106  -0.0053 0.0171  98  PRO   A CB  
1927 C CG  A PRO   A 98  ? 0.1767 0.1703 0.1375 0.0080  -0.0154 -0.0075 98  PRO   A CG  
1928 C CG  B PRO   A 98  ? 0.1769 0.1531 0.1584 0.0087  -0.0094 0.0233  98  PRO   A CG  
1929 C CD  A PRO   A 98  ? 0.1699 0.1554 0.1342 0.0057  -0.0068 0.0122  98  PRO   A CD  
1930 C CD  B PRO   A 98  ? 0.1651 0.1474 0.1516 0.0005  -0.0089 0.0272  98  PRO   A CD  
1945 N N   A ASN   A 99  ? 0.1786 0.2145 0.1264 -0.0142 -0.0045 0.0349  99  ASN   A N   
1946 N N   B ASN   A 99  ? 0.2271 0.1608 0.1484 0.0126  -0.0063 0.0249  99  ASN   A N   
1947 C CA  A ASN   A 99  ? 0.1989 0.2334 0.1263 -0.0156 -0.0032 0.0498  99  ASN   A CA  
1948 C CA  B ASN   A 99  ? 0.2524 0.1639 0.1559 0.0220  -0.0061 0.0367  99  ASN   A CA  
1949 C C   A ASN   A 99  ? 0.2232 0.2702 0.1219 -0.0225 0.0009  0.0545  99  ASN   A C   
1950 C C   B ASN   A 99  ? 0.2631 0.1765 0.1624 0.0258  -0.0147 0.0374  99  ASN   A C   
1951 O O   A ASN   A 99  ? 0.2339 0.2967 0.1421 -0.0113 -0.0059 0.0399  99  ASN   A O   
1952 O O   B ASN   A 99  ? 0.2612 0.1628 0.1368 0.0328  -0.0201 0.0364  99  ASN   A O   
1953 C CB  A ASN   A 99  ? 0.1972 0.2263 0.1674 -0.0132 -0.0264 0.0524  99  ASN   A CB  
1954 C CB  B ASN   A 99  ? 0.2653 0.1594 0.1660 0.0231  -0.0038 0.0448  99  ASN   A CB  
1955 C CG  A ASN   A 99  ? 0.2012 0.2275 0.2043 -0.0069 -0.0316 0.0513  99  ASN   A CG  
1956 C CG  B ASN   A 99  ? 0.2765 0.1597 0.1726 0.0243  -0.0004 0.0498  99  ASN   A CG  
1957 O OD1 A ASN   A 99  ? 0.2117 0.2368 0.2110 0.0023  -0.0258 0.0413  99  ASN   A OD1 
1958 O OD1 B ASN   A 99  ? 0.2763 0.1649 0.1764 0.0336  -0.0069 0.0491  99  ASN   A OD1 
1959 N ND2 A ASN   A 99  ? 0.2050 0.2227 0.2281 -0.0035 -0.0309 0.0662  99  ASN   A ND2 
1960 N ND2 B ASN   A 99  ? 0.2837 0.1627 0.2036 0.0241  -0.0042 0.0450  99  ASN   A ND2 
1973 N N   A VAL   A 100 ? 0.2413 0.2812 0.1307 -0.0400 -0.0208 0.0574  100 VAL   A N   
1974 N N   B VAL   A 100 ? 0.2795 0.2127 0.2109 0.0205  -0.0115 0.0363  100 VAL   A N   
1975 C CA  A VAL   A 100 ? 0.2710 0.3095 0.1666 -0.0402 -0.0351 0.0564  100 VAL   A CA  
1976 C CA  B VAL   A 100 ? 0.2980 0.2422 0.2525 0.0165  -0.0123 0.0279  100 VAL   A CA  
1977 C C   A VAL   A 100 ? 0.2907 0.3344 0.1668 -0.0406 -0.0516 0.0822  100 VAL   A C   
1978 C C   B VAL   A 100 ? 0.3126 0.2622 0.2673 0.0163  -0.0151 0.0234  100 VAL   A C   
1979 O O   A VAL   A 100 ? 0.2972 0.3489 0.1780 -0.0414 -0.0309 0.0792  100 VAL   A O   
1980 O O   B VAL   A 100 ? 0.3145 0.2642 0.2699 0.0161  -0.0225 0.0283  100 VAL   A O   
1981 C CB  A VAL   A 100 ? 0.2827 0.3103 0.2024 -0.0425 -0.0370 0.0405  100 VAL   A CB  
1982 C CB  B VAL   A 100 ? 0.3015 0.2491 0.2816 0.0120  -0.0052 0.0288  100 VAL   A CB  
1983 C CG1 A VAL   A 100 ? 0.2829 0.3135 0.2225 -0.0447 -0.0272 0.0375  100 VAL   A CG1 
1984 C CG1 B VAL   A 100 ? 0.3027 0.2532 0.2927 0.0078  -0.0078 0.0253  100 VAL   A CG1 
1985 C CG2 A VAL   A 100 ? 0.2903 0.3114 0.2036 -0.0437 -0.0354 0.0332  100 VAL   A CG2 
1986 C CG2 B VAL   A 100 ? 0.3046 0.2518 0.2981 0.0119  -0.0006 0.0331  100 VAL   A CG2 
2005 N N   A ASN   A 101 ? 0.3054 0.3391 0.1964 -0.0440 -0.0687 0.1119  101 ASN   A N   
2006 N N   B ASN   A 101 ? 0.3251 0.2809 0.2708 0.0180  -0.0131 0.0151  101 ASN   A N   
2007 C CA  A ASN   A 101 ? 0.3328 0.3490 0.2317 -0.0446 -0.0724 0.1203  101 ASN   A CA  
2008 C CA  B ASN   A 101 ? 0.3392 0.2976 0.2774 0.0230  -0.0078 0.0149  101 ASN   A CA  
2009 C C   A ASN   A 101 ? 0.3597 0.3692 0.2553 -0.0422 -0.0479 0.1406  101 ASN   A C   
2010 C C   B ASN   A 101 ? 0.3484 0.3006 0.2701 0.0180  -0.0048 0.0157  101 ASN   A C   
2011 O O   A ASN   A 101 ? 0.3706 0.3733 0.2979 -0.0398 -0.0411 0.1326  101 ASN   A O   
2012 O O   B ASN   A 101 ? 0.3522 0.2995 0.2650 0.0177  -0.0082 0.0213  101 ASN   A O   
2013 C CB  A ASN   A 101 ? 0.3348 0.3351 0.2309 -0.0459 -0.0936 0.1068  101 ASN   A CB  
2014 C CB  B ASN   A 101 ? 0.3452 0.3084 0.2928 0.0292  -0.0050 0.0128  101 ASN   A CB  
2015 C CG  A ASN   A 101 ? 0.3374 0.3251 0.2271 -0.0495 -0.1062 0.0779  101 ASN   A CG  
2016 C CG  B ASN   A 101 ? 0.3509 0.3141 0.3037 0.0344  -0.0006 0.0054  101 ASN   A CG  
2017 O OD1 A ASN   A 101 ? 0.3361 0.3294 0.2362 -0.0449 -0.1024 0.0550  101 ASN   A OD1 
2018 O OD1 B ASN   A 101 ? 0.3523 0.3177 0.3129 0.0351  -0.0033 0.0044  101 ASN   A OD1 
2019 N ND2 A ASN   A 101 ? 0.3437 0.3174 0.2323 -0.0547 -0.1031 0.0680  101 ASN   A ND2 
2020 N ND2 B ASN   A 101 ? 0.3547 0.3169 0.3062 0.0365  0.0040  0.0010  101 ASN   A ND2 
2033 N N   A LYS   A 102 ? 0.3718 0.3922 0.2857 -0.0420 -0.0375 0.1290  102 LYS   A N   
2034 N N   B LYS   A 102 ? 0.3519 0.3049 0.2809 0.0163  0.0006  0.0101  102 LYS   A N   
2035 C CA  A LYS   A 102 ? 0.3878 0.4148 0.3015 -0.0380 -0.0384 0.1053  102 LYS   A CA  
2036 C CA  B LYS   A 102 ? 0.3542 0.3104 0.2795 0.0123  0.0066  0.0108  102 LYS   A CA  
2037 C C   A LYS   A 102 ? 0.3921 0.4316 0.2733 -0.0295 -0.0351 0.1033  102 LYS   A C   
2038 C C   B LYS   A 102 ? 0.3481 0.3045 0.2599 0.0172  0.0088  0.0213  102 LYS   A C   
2039 O O   A LYS   A 102 ? 0.3958 0.4416 0.2805 -0.0250 -0.0384 0.1009  102 LYS   A O   
2040 O O   B LYS   A 102 ? 0.3511 0.3054 0.2604 0.0199  0.0152  0.0297  102 LYS   A O   
2041 C CB  A LYS   A 102 ? 0.4003 0.4212 0.3506 -0.0418 -0.0492 0.0743  102 LYS   A CB  
2042 C CB  B LYS   A 102 ? 0.3618 0.3216 0.3101 0.0068  0.0027  0.0005  102 LYS   A CB  
2043 C CG  A LYS   A 102 ? 0.4105 0.4252 0.3895 -0.0458 -0.0597 0.0431  102 LYS   A CG  
2044 C CG  B LYS   A 102 ? 0.3691 0.3330 0.3455 0.0015  -0.0028 -0.0069 102 LYS   A CG  
2045 C CD  A LYS   A 102 ? 0.4202 0.4289 0.4249 -0.0475 -0.0675 0.0136  102 LYS   A CD  
2046 C CD  B LYS   A 102 ? 0.3765 0.3444 0.3815 -0.0020 -0.0066 -0.0126 102 LYS   A CD  
2047 C CE  A LYS   A 102 ? 0.4278 0.4309 0.4521 -0.0482 -0.0708 -0.0074 102 LYS   A CE  
2048 C CE  B LYS   A 102 ? 0.3825 0.3529 0.4120 -0.0039 -0.0094 -0.0144 102 LYS   A CE  
2049 N NZ  A LYS   A 102 ? 0.4319 0.4318 0.4652 -0.0515 -0.0717 -0.0217 102 LYS   A NZ  
2050 N NZ  B LYS   A 102 ? 0.3867 0.3574 0.4320 -0.0047 -0.0102 -0.0158 102 LYS   A NZ  
2077 N N   A GLY   A 103 ? 0.3893 0.4389 0.2677 -0.0228 -0.0334 0.0858  103 GLY   A N   
2078 N N   B GLY   A 103 ? 0.3379 0.2998 0.2437 0.0223  0.0012  0.0135  103 GLY   A N   
2079 C CA  A GLY   A 103 ? 0.3871 0.4421 0.2578 -0.0180 -0.0243 0.0691  103 GLY   A CA  
2080 C CA  B GLY   A 103 ? 0.3254 0.2929 0.2438 0.0289  -0.0057 0.0171  103 GLY   A CA  
2081 C C   A GLY   A 103 ? 0.3804 0.4440 0.2582 -0.0171 -0.0095 0.0478  103 GLY   A C   
2082 C C   B GLY   A 103 ? 0.3126 0.2862 0.2467 0.0323  -0.0151 0.0188  103 GLY   A C   
2083 O O   A GLY   A 103 ? 0.3874 0.4524 0.2778 -0.0122 -0.0059 0.0359  103 GLY   A O   
2084 O O   B GLY   A 103 ? 0.3160 0.2915 0.2671 0.0389  -0.0173 0.0150  103 GLY   A O   
2091 N N   A GLU   A 104 ? 0.3624 0.4342 0.2200 -0.0250 0.0025  0.0367  104 GLU   A N   
2092 N N   B GLU   A 104 ? 0.2932 0.2691 0.2188 0.0275  -0.0240 0.0328  104 GLU   A N   
2093 C CA  A GLU   A 104 ? 0.3419 0.4221 0.1994 -0.0365 0.0112  0.0280  104 GLU   A CA  
2094 C CA  B GLU   A 104 ? 0.2742 0.2544 0.1901 0.0183  -0.0235 0.0367  104 GLU   A CA  
2095 C C   A GLU   A 104 ? 0.3434 0.4289 0.1996 -0.0327 0.0101  0.0048  104 GLU   A C   
2096 C C   B GLU   A 104 ? 0.2637 0.2567 0.1808 0.0197  -0.0232 0.0248  104 GLU   A C   
2097 O O   A GLU   A 104 ? 0.3429 0.4303 0.2000 -0.0325 0.0085  -0.0068 104 GLU   A O   
2098 O O   B GLU   A 104 ? 0.2625 0.2575 0.1874 0.0197  -0.0310 0.0225  104 GLU   A O   
2099 C CB  A GLU   A 104 ? 0.3175 0.4025 0.1712 -0.0513 0.0235  0.0466  104 GLU   A CB  
2100 C CB  B GLU   A 104 ? 0.2694 0.2407 0.1812 0.0058  -0.0146 0.0487  104 GLU   A CB  
2101 C CG  A GLU   A 104 ? 0.2985 0.3850 0.1794 -0.0614 0.0206  0.0532  104 GLU   A CG  
2102 C CG  B GLU   A 104 ? 0.2683 0.2365 0.1842 -0.0061 -0.0093 0.0521  104 GLU   A CG  
2103 C CD  A GLU   A 104 ? 0.2786 0.3677 0.1744 -0.0691 0.0214  0.0633  104 GLU   A CD  
2104 C CD  B GLU   A 104 ? 0.2682 0.2359 0.1730 -0.0129 -0.0108 0.0563  104 GLU   A CD  
2105 O OE1 A GLU   A 104 ? 0.2639 0.3562 0.1402 -0.0724 0.0081  0.0637  104 GLU   A OE1 
2106 O OE1 B GLU   A 104 ? 0.2712 0.2406 0.1784 -0.0131 -0.0114 0.0504  104 GLU   A OE1 
2107 O OE2 A GLU   A 104 ? 0.2863 0.3663 0.2050 -0.0694 0.0281  0.0653  104 GLU   A OE2 
2108 O OE2 B GLU   A 104 ? 0.2688 0.2369 0.1699 -0.0181 -0.0022 0.0526  104 GLU   A OE2 
2121 N N   A ASP   A 105 ? 0.3426 0.4335 0.2068 -0.0291 0.0106  -0.0098 105 ASP   A N   
2122 N N   B ASP   A 105 ? 0.2612 0.2549 0.1868 0.0204  -0.0220 0.0149  105 ASP   A N   
2123 C CA  A ASP   A 105 ? 0.3383 0.4378 0.2357 -0.0240 0.0113  -0.0365 105 ASP   A CA  
2124 C CA  B ASP   A 105 ? 0.2584 0.2514 0.2115 0.0259  -0.0121 -0.0066 105 ASP   A CA  
2125 C C   A ASP   A 105 ? 0.3069 0.4235 0.2080 -0.0373 -0.0025 -0.0556 105 ASP   A C   
2126 C C   B ASP   A 105 ? 0.2497 0.2350 0.1828 0.0213  -0.0095 -0.0121 105 ASP   A C   
2127 O O   A ASP   A 105 ? 0.2950 0.4265 0.1679 -0.0396 -0.0027 -0.0708 105 ASP   A O   
2128 O O   B ASP   A 105 ? 0.2309 0.2158 0.1451 0.0287  -0.0102 -0.0046 105 ASP   A O   
2129 C CB  A ASP   A 105 ? 0.3623 0.4540 0.2961 -0.0088 0.0224  -0.0427 105 ASP   A CB  
2130 C CB  B ASP   A 105 ? 0.2652 0.2631 0.2650 0.0369  -0.0031 -0.0228 105 ASP   A CB  
2131 C CG  A ASP   A 105 ? 0.3814 0.4678 0.3516 0.0030  0.0280  -0.0492 105 ASP   A CG  
2132 C CG  B ASP   A 105 ? 0.2726 0.2720 0.3098 0.0468  0.0096  -0.0433 105 ASP   A CG  
2133 O OD1 A ASP   A 105 ? 0.3858 0.4733 0.3584 0.0044  0.0255  -0.0587 105 ASP   A OD1 
2134 O OD1 B ASP   A 105 ? 0.2742 0.2700 0.3100 0.0460  0.0074  -0.0575 105 ASP   A OD1 
2135 O OD2 A ASP   A 105 ? 0.3930 0.4735 0.3926 0.0070  0.0356  -0.0434 105 ASP   A OD2 
2136 O OD2 B ASP   A 105 ? 0.2743 0.2773 0.3376 0.0560  0.0168  -0.0426 105 ASP   A OD2 
2145 N N   A ILE   A 106 ? 0.2836 0.4033 0.2197 -0.0482 -0.0264 -0.0614 106 ILE   A N   
2146 N N   B ILE   A 106 ? 0.2571 0.2482 0.2020 0.0117  -0.0165 -0.0144 106 ILE   A N   
2147 C CA  A ILE   A 106 ? 0.2535 0.3800 0.2415 -0.0617 -0.0462 -0.0730 106 ILE   A CA  
2148 C CA  B ILE   A 106 ? 0.2633 0.2575 0.2259 0.0000  -0.0219 -0.0223 106 ILE   A CA  
2149 C C   A ILE   A 106 ? 0.2324 0.3561 0.2428 -0.0842 -0.0495 -0.0878 106 ILE   A C   
2150 C C   B ILE   A 106 ? 0.2717 0.2511 0.2280 -0.0009 -0.0125 -0.0092 106 ILE   A C   
2151 O O   A ILE   A 106 ? 0.2099 0.3476 0.2576 -0.0903 -0.0288 -0.0770 106 ILE   A O   
2152 O O   B ILE   A 106 ? 0.2694 0.2504 0.2366 -0.0021 -0.0061 -0.0025 106 ILE   A O   
2153 C CB  A ILE   A 106 ? 0.2536 0.3822 0.2772 -0.0464 -0.0591 -0.0571 106 ILE   A CB  
2154 C CB  B ILE   A 106 ? 0.2650 0.2753 0.2503 -0.0095 -0.0363 -0.0372 106 ILE   A CB  
2155 C CG1 A ILE   A 106 ? 0.2459 0.3779 0.3048 -0.0344 -0.0631 -0.0427 106 ILE   A CG1 
2156 C CG1 B ILE   A 106 ? 0.2637 0.2842 0.2625 -0.0131 -0.0406 -0.0433 106 ILE   A CG1 
2157 C CG2 A ILE   A 106 ? 0.2579 0.3855 0.2902 -0.0424 -0.0653 -0.0541 106 ILE   A CG2 
2158 C CG2 B ILE   A 106 ? 0.2681 0.2804 0.2552 -0.0123 -0.0398 -0.0400 106 ILE   A CG2 
2159 C CD1 A ILE   A 106 ? 0.2442 0.3732 0.3207 -0.0244 -0.0561 -0.0342 106 ILE   A CD1 
2160 C CD1 B ILE   A 106 ? 0.2627 0.2889 0.2749 -0.0143 -0.0397 -0.0431 106 ILE   A CD1 
2183 N N   A GLN   A 107 ? 0.2519 0.3426 0.2778 -0.0836 -0.0354 -0.0959 107 GLN   A N   
2184 N N   B GLN   A 107 ? 0.2823 0.2440 0.2376 0.0012  -0.0039 -0.0016 107 GLN   A N   
2185 C CA  A GLN   A 107 ? 0.2758 0.3276 0.3346 -0.0708 -0.0133 -0.0907 107 GLN   A CA  
2186 C CA  B GLN   A 107 ? 0.2946 0.2457 0.2720 -0.0014 -0.0023 0.0077  107 GLN   A CA  
2187 C C   A GLN   A 107 ? 0.2466 0.2777 0.3155 -0.0626 0.0155  -0.0714 107 GLN   A C   
2188 C C   B GLN   A 107 ? 0.2695 0.2105 0.2353 0.0005  0.0055  0.0185  107 GLN   A C   
2189 O O   A GLN   A 107 ? 0.2576 0.2762 0.3676 -0.0597 0.0331  -0.0692 107 GLN   A O   
2190 O O   B GLN   A 107 ? 0.2702 0.1993 0.2179 0.0008  -0.0019 0.0139  107 GLN   A O   
2191 C CB  A GLN   A 107 ? 0.3241 0.3593 0.4241 -0.0728 -0.0238 -0.0921 107 GLN   A CB  
2192 C CB  B GLN   A 107 ? 0.3262 0.2844 0.3395 -0.0094 -0.0142 0.0033  107 GLN   A CB  
2193 C CG  A GLN   A 107 ? 0.3703 0.3917 0.5226 -0.0688 -0.0309 -0.0818 107 GLN   A CG  
2194 C CG  B GLN   A 107 ? 0.3532 0.3174 0.4062 -0.0137 -0.0276 0.0092  107 GLN   A CG  
2195 C CD  A GLN   A 107 ? 0.4081 0.4161 0.6076 -0.0652 -0.0353 -0.0695 107 GLN   A CD  
2196 C CD  B GLN   A 107 ? 0.3745 0.3438 0.4666 -0.0159 -0.0374 0.0166  107 GLN   A CD  
2197 O OE1 A GLN   A 107 ? 0.4206 0.4261 0.6440 -0.0640 -0.0365 -0.0638 107 GLN   A OE1 
2198 O OE1 B GLN   A 107 ? 0.3817 0.3513 0.4825 -0.0158 -0.0395 0.0217  107 GLN   A OE1 
2199 N NE2 A GLN   A 107 ? 0.4174 0.4243 0.6350 -0.0648 -0.0381 -0.0691 107 GLN   A NE2 
2200 N NE2 B GLN   A 107 ? 0.3816 0.3515 0.4850 -0.0169 -0.0437 0.0175  107 GLN   A NE2 
2217 N N   A LEU   A 108 ? 0.2079 0.2302 0.2470 -0.0581 0.0170  -0.0659 108 LEU   A N   
2218 N N   B LEU   A 108 ? 0.2434 0.1941 0.2127 -0.0028 0.0128  0.0210  108 LEU   A N   
2219 C CA  A LEU   A 108 ? 0.1903 0.1939 0.2190 -0.0310 0.0197  -0.0327 108 LEU   A CA  
2220 C CA  B LEU   A 108 ? 0.2194 0.1800 0.2058 0.0006  0.0180  0.0162  108 LEU   A CA  
2221 C C   A LEU   A 108 ? 0.1697 0.1555 0.2143 -0.0145 0.0164  -0.0055 108 LEU   A C   
2222 C C   B LEU   A 108 ? 0.1894 0.1586 0.2042 0.0013  0.0174  0.0170  108 LEU   A C   
2223 O O   A LEU   A 108 ? 0.1679 0.1525 0.2257 -0.0121 0.0226  0.0012  108 LEU   A O   
2224 O O   B LEU   A 108 ? 0.1908 0.1593 0.2097 0.0036  0.0270  0.0228  108 LEU   A O   
2225 C CB  A LEU   A 108 ? 0.1928 0.2037 0.2015 -0.0342 0.0280  -0.0274 108 LEU   A CB  
2226 C CB  B LEU   A 108 ? 0.2240 0.1911 0.2026 -0.0011 0.0204  0.0086  108 LEU   A CB  
2227 C CG  A LEU   A 108 ? 0.2092 0.2260 0.2201 -0.0260 0.0364  -0.0286 108 LEU   A CG  
2228 C CG  B LEU   A 108 ? 0.2331 0.2048 0.2167 0.0015  0.0225  0.0010  108 LEU   A CG  
2229 C CD1 A LEU   A 108 ? 0.2233 0.2343 0.2331 -0.0300 0.0431  -0.0254 108 LEU   A CD1 
2230 C CD1 B LEU   A 108 ? 0.2393 0.2102 0.2228 -0.0001 0.0281  0.0008  108 LEU   A CD1 
2231 C CD2 A LEU   A 108 ? 0.2129 0.2463 0.2559 -0.0197 0.0386  -0.0154 108 LEU   A CD2 
2232 C CD2 B LEU   A 108 ? 0.2355 0.2167 0.2388 0.0044  0.0198  0.0019  108 LEU   A CD2 
2255 N N   . LEU   A 109 ? 0.1623 0.1501 0.2046 -0.0016 0.0134  0.0132  109 LEU   A N   
2256 C CA  . LEU   A 109 ? 0.1590 0.1411 0.1858 0.0001  -0.0022 0.0135  109 LEU   A CA  
2257 C C   . LEU   A 109 ? 0.1365 0.1357 0.1878 -0.0118 0.0075  0.0080  109 LEU   A C   
2258 O O   . LEU   A 109 ? 0.1460 0.1306 0.2074 -0.0105 -0.0004 0.0052  109 LEU   A O   
2259 C CB  . LEU   A 109 ? 0.1609 0.1560 0.2119 0.0035  -0.0086 0.0294  109 LEU   A CB  
2260 C CG  . LEU   A 109 ? 0.1507 0.1622 0.2297 0.0003  -0.0022 0.0323  109 LEU   A CG  
2261 C CD1 . LEU   A 109 ? 0.1580 0.1616 0.2378 0.0018  0.0058  0.0167  109 LEU   A CD1 
2262 C CD2 . LEU   A 109 ? 0.1456 0.1852 0.2525 -0.0043 -0.0078 0.0307  109 LEU   A CD2 
2275 N N   . LYS   A 110 ? 0.1445 0.1354 0.1859 -0.0093 -0.0034 0.0113  110 LYS   A N   
2276 C CA  . LYS   A 110 ? 0.1402 0.1282 0.2031 -0.0131 -0.0043 0.0129  110 LYS   A CA  
2277 C C   . LYS   A 110 ? 0.1414 0.1263 0.1916 -0.0143 0.0036  -0.0008 110 LYS   A C   
2278 O O   . LYS   A 110 ? 0.1358 0.1256 0.2088 -0.0130 0.0056  -0.0000 110 LYS   A O   
2279 C CB  . LYS   A 110 ? 0.1481 0.1357 0.2219 -0.0107 -0.0137 -0.0020 110 LYS   A CB  
2280 C CG  . LYS   A 110 ? 0.1509 0.1350 0.2379 -0.0051 -0.0100 -0.0021 110 LYS   A CG  
2281 C CD  . LYS   A 110 ? 0.1542 0.1371 0.2549 -0.0070 -0.0122 -0.0093 110 LYS   A CD  
2282 C CE  . LYS   A 110 ? 0.1647 0.1438 0.2729 -0.0093 0.0060  -0.0111 110 LYS   A CE  
2283 N NZ  . LYS   A 110 ? 0.1620 0.1466 0.2817 -0.0198 0.0143  0.0000  110 LYS   A NZ  
2297 N N   . SER   A 111 ? 0.1423 0.1323 0.1831 -0.0053 -0.0021 0.0026  111 SER   A N   
2298 C CA  . SER   A 111 ? 0.1336 0.1381 0.1857 -0.0014 0.0012  0.0038  111 SER   A CA  
2299 C C   . SER   A 111 ? 0.1263 0.1280 0.1788 -0.0072 0.0044  0.0119  111 SER   A C   
2300 O O   . SER   A 111 ? 0.1426 0.1192 0.1962 -0.0047 0.0086  0.0127  111 SER   A O   
2301 C CB  . SER   A 111 ? 0.1577 0.1609 0.2068 -0.0043 0.0176  -0.0139 111 SER   A CB  
2302 O OG  . SER   A 111 ? 0.1968 0.1776 0.2163 0.0029  0.0214  -0.0182 111 SER   A OG  
2308 N N   . ALA   A 112 ? 0.1345 0.1216 0.1790 -0.0045 0.0126  0.0104  112 ALA   A N   
2309 C CA  . ALA   A 112 ? 0.1346 0.1249 0.1768 -0.0041 0.0153  0.0056  112 ALA   A CA  
2310 C C   . ALA   A 112 ? 0.1265 0.1162 0.1814 -0.0072 0.0030  0.0120  112 ALA   A C   
2311 O O   . ALA   A 112 ? 0.1329 0.1149 0.1968 -0.0138 0.0086  0.0110  112 ALA   A O   
2312 C CB  . ALA   A 112 ? 0.1452 0.1247 0.1867 -0.0078 0.0145  0.0145  112 ALA   A CB  
2318 N N   . TYR   A 113 ? 0.1232 0.1246 0.1866 -0.0068 0.0067  0.0152  113 TYR   A N   
2319 C CA  . TYR   A 113 ? 0.1261 0.1169 0.1835 -0.0044 0.0141  0.0127  113 TYR   A CA  
2320 C C   . TYR   A 113 ? 0.1174 0.1216 0.1737 -0.0084 0.0138  0.0067  113 TYR   A C   
2321 O O   . TYR   A 113 ? 0.1226 0.1237 0.1914 -0.0051 0.0154  0.0072  113 TYR   A O   
2322 C CB  . TYR   A 113 ? 0.1234 0.1319 0.1890 -0.0034 0.0001  0.0262  113 TYR   A CB  
2323 C CG  . TYR   A 113 ? 0.1273 0.1349 0.1820 -0.0128 0.0089  0.0256  113 TYR   A CG  
2324 C CD1 . TYR   A 113 ? 0.1268 0.1529 0.1862 -0.0035 0.0079  0.0210  113 TYR   A CD1 
2325 C CD2 . TYR   A 113 ? 0.1324 0.1426 0.1958 -0.0150 0.0019  0.0264  113 TYR   A CD2 
2326 C CE1 . TYR   A 113 ? 0.1325 0.1615 0.2012 -0.0056 0.0038  0.0151  113 TYR   A CE1 
2327 C CE2 . TYR   A 113 ? 0.1345 0.1566 0.1942 -0.0120 -0.0038 0.0282  113 TYR   A CE2 
2328 C CZ  . TYR   A 113 ? 0.1238 0.1566 0.2023 0.0004  0.0056  0.0290  113 TYR   A CZ  
2329 O OH  . TYR   A 113 ? 0.1282 0.1671 0.2326 0.0124  0.0015  0.0248  113 TYR   A OH  
2339 N N   . GLU   A 114 ? 0.1246 0.1195 0.1824 -0.0060 0.0118  0.0164  114 GLU   A N   
2340 C CA  . GLU   A 114 ? 0.1263 0.1134 0.1994 0.0006  0.0036  0.0172  114 GLU   A CA  
2341 C C   . GLU   A 114 ? 0.1203 0.1190 0.1987 -0.0007 0.0097  0.0154  114 GLU   A C   
2342 O O   . GLU   A 114 ? 0.1319 0.1196 0.1995 -0.0003 0.0062  0.0138  114 GLU   A O   
2343 C CB  . GLU   A 114 ? 0.1267 0.1212 0.2025 -0.0058 0.0064  0.0159  114 GLU   A CB  
2344 C CG  . GLU   A 114 ? 0.1328 0.1228 0.2124 -0.0050 0.0116  0.0052  114 GLU   A CG  
2345 C CD  . GLU   A 114 ? 0.1425 0.1180 0.2179 -0.0039 0.0046  0.0078  114 GLU   A CD  
2346 O OE1 . GLU   A 114 ? 0.1446 0.1234 0.2237 -0.0097 0.0096  -0.0058 114 GLU   A OE1 
2347 O OE2 . GLU   A 114 ? 0.1642 0.1287 0.2379 -0.0107 0.0086  -0.0085 114 GLU   A OE2 
2354 N N   . ASN   A 115 ? 0.1255 0.1215 0.1820 -0.0088 0.0071  0.0115  115 ASN   A N   
2355 C CA  . ASN   A 115 ? 0.1238 0.1253 0.1934 -0.0080 0.0131  0.0163  115 ASN   A CA  
2356 C C   . ASN   A 115 ? 0.1299 0.1186 0.1861 -0.0081 0.0093  0.0141  115 ASN   A C   
2357 O O   . ASN   A 115 ? 0.1312 0.1342 0.1872 -0.0118 0.0129  0.0188  115 ASN   A O   
2358 C CB  . ASN   A 115 ? 0.1377 0.1302 0.1831 -0.0141 0.0124  0.0195  115 ASN   A CB  
2359 C CG  . ASN   A 115 ? 0.1336 0.1503 0.1875 -0.0144 0.0170  0.0118  115 ASN   A CG  
2360 O OD1 . ASN   A 115 ? 0.1326 0.2540 0.2146 -0.0131 0.0233  0.0292  115 ASN   A OD1 
2361 N ND2 . ASN   A 115 ? 0.1431 0.1275 0.1791 -0.0141 0.0197  0.0197  115 ASN   A ND2 
2368 N N   . PHE   A 116 ? 0.1257 0.1251 0.1895 -0.0007 0.0139  0.0263  116 PHE   A N   
2369 C CA  . PHE   A 116 ? 0.1228 0.1319 0.1703 0.0013  0.0120  0.0211  116 PHE   A CA  
2370 C C   . PHE   A 116 ? 0.1273 0.1380 0.1751 -0.0060 0.0157  0.0218  116 PHE   A C   
2371 O O   . PHE   A 116 ? 0.1298 0.1437 0.1912 0.0018  0.0188  0.0333  116 PHE   A O   
2372 C CB  . PHE   A 116 ? 0.1257 0.1246 0.1953 0.0011  0.0154  0.0176  116 PHE   A CB  
2373 C CG  . PHE   A 116 ? 0.1279 0.1199 0.1899 -0.0043 0.0045  0.0119  116 PHE   A CG  
2374 C CD1 . PHE   A 116 ? 0.1304 0.1169 0.1977 -0.0074 0.0106  0.0219  116 PHE   A CD1 
2375 C CD2 . PHE   A 116 ? 0.1307 0.1269 0.1986 -0.0048 0.0207  0.0243  116 PHE   A CD2 
2376 C CE1 . PHE   A 116 ? 0.1316 0.1227 0.2035 -0.0191 0.0101  0.0168  116 PHE   A CE1 
2377 C CE2 . PHE   A 116 ? 0.1329 0.1261 0.2057 -0.0046 0.0191  0.0168  116 PHE   A CE2 
2378 C CZ  . PHE   A 116 ? 0.1378 0.1122 0.2003 -0.0006 0.0044  0.0179  116 PHE   A CZ  
2388 N N   . ASN   A 117 ? 0.1264 0.1267 0.1908 -0.0069 0.0091  0.0223  117 ASN   A N   
2389 C CA  . ASN   A 117 ? 0.1316 0.1292 0.2006 -0.0028 0.0168  0.0272  117 ASN   A CA  
2390 C C   . ASN   A 117 ? 0.1320 0.1381 0.2114 -0.0021 0.0177  0.0261  117 ASN   A C   
2391 O O   . ASN   A 117 ? 0.1418 0.1382 0.2379 -0.0033 0.0002  0.0447  117 ASN   A O   
2392 C CB  . ASN   A 117 ? 0.1285 0.1338 0.1988 -0.0010 0.0108  0.0349  117 ASN   A CB  
2393 C CG  . ASN   A 117 ? 0.1300 0.1336 0.2049 -0.0002 0.0161  0.0389  117 ASN   A CG  
2394 O OD1 . ASN   A 117 ? 0.1333 0.1550 0.2104 -0.0151 0.0175  0.0241  117 ASN   A OD1 
2395 N ND2 . ASN   A 117 ? 0.1203 0.1285 0.2165 -0.0054 0.0115  0.0303  117 ASN   A ND2 
2402 N N   . GLN   A 118 ? 0.1258 0.1392 0.2080 -0.0054 0.0070  0.0324  118 GLN   A N   
2403 C CA  . GLN   A 118 ? 0.1364 0.1455 0.2140 -0.0078 0.0048  0.0221  118 GLN   A CA  
2404 C C   . GLN   A 118 ? 0.1402 0.1529 0.2065 -0.0090 -0.0012 0.0322  118 GLN   A C   
2405 O O   . GLN   A 118 ? 0.1402 0.1849 0.2216 -0.0015 -0.0051 0.0129  118 GLN   A O   
2406 C CB  . GLN   A 118 ? 0.1378 0.1475 0.2175 -0.0006 0.0151  0.0253  118 GLN   A CB  
2407 C CG  . GLN   A 118 ? 0.1312 0.1492 0.2239 -0.0017 0.0112  0.0285  118 GLN   A CG  
2408 C CD  . GLN   A 118 ? 0.1264 0.1515 0.2285 0.0001  0.0125  0.0277  118 GLN   A CD  
2409 O OE1 . GLN   A 118 ? 0.1328 0.1674 0.2437 0.0093  0.0046  0.0107  118 GLN   A OE1 
2410 N NE2 . GLN   A 118 ? 0.1350 0.1488 0.2319 0.0078  0.0052  0.0288  118 GLN   A NE2 
2419 N N   . HIS   A 119 ? 0.1422 0.1510 0.1915 -0.0046 0.0023  0.0323  119 HIS   A N   
2420 C CA  . HIS   A 119 ? 0.1521 0.1644 0.1935 -0.0031 0.0020  0.0372  119 HIS   A CA  
2421 C C   . HIS   A 119 ? 0.1552 0.1704 0.1954 -0.0052 0.0117  0.0425  119 HIS   A C   
2422 O O   . HIS   A 119 ? 0.1586 0.1734 0.2093 -0.0206 0.0078  0.0394  119 HIS   A O   
2423 C CB  . HIS   A 119 ? 0.1529 0.1593 0.2075 -0.0022 0.0221  0.0424  119 HIS   A CB  
2424 C CG  . HIS   A 119 ? 0.1498 0.1633 0.2496 0.0020  0.0178  0.0439  119 HIS   A CG  
2425 N ND1 . HIS   A 119 ? 0.1621 0.1797 0.3086 -0.0064 0.0144  0.0290  119 HIS   A ND1 
2426 C CD2 . HIS   A 119 ? 0.1632 0.1691 0.2779 0.0118  0.0344  0.0613  119 HIS   A CD2 
2427 C CE1 . HIS   A 119 ? 0.1606 0.1748 0.3293 -0.0122 0.0291  0.0427  119 HIS   A CE1 
2428 N NE2 . HIS   A 119 ? 0.1731 0.1669 0.3185 0.0057  0.0449  0.0641  119 HIS   A NE2 
2436 N N   . GLU   A 120 ? 0.1660 0.1939 0.1982 -0.0043 0.0021  0.0622  120 GLU   A N   
2437 C CA  . GLU   A 120 ? 0.1903 0.2267 0.2318 0.0057  0.0041  0.0970  120 GLU   A CA  
2438 C C   . GLU   A 120 ? 0.1726 0.2151 0.2068 -0.0048 0.0097  0.0879  120 GLU   A C   
2439 O O   . GLU   A 120 ? 0.1705 0.2084 0.2175 -0.0077 0.0048  0.0905  120 GLU   A O   
2440 C CB  . GLU   A 120 ? 0.2556 0.2872 0.2854 0.0232  0.0067  0.1479  120 GLU   A CB  
2441 C CG  . GLU   A 120 ? 0.3437 0.3583 0.3983 0.0365  0.0072  0.1506  120 GLU   A CG  
2442 C CD  . GLU   A 120 ? 0.4190 0.4183 0.5108 0.0486  0.0142  0.1416  120 GLU   A CD  
2443 O OE1 . GLU   A 120 ? 0.4423 0.4341 0.5406 0.0506  0.0189  0.1371  120 GLU   A OE1 
2444 O OE2 . GLU   A 120 ? 0.4484 0.4413 0.5568 0.0514  0.0147  0.1373  120 GLU   A OE2 
2451 N N   . VAL   A 121 ? 0.1671 0.2118 0.1771 -0.0067 0.0196  0.0716  121 VAL   A N   
2452 C CA  . VAL   A 121 ? 0.1734 0.2161 0.1720 -0.0084 0.0328  0.0678  121 VAL   A CA  
2453 C C   . VAL   A 121 ? 0.1625 0.1950 0.1645 -0.0205 0.0206  0.0535  121 VAL   A C   
2454 O O   . VAL   A 121 ? 0.1663 0.1971 0.1825 -0.0253 0.0087  0.0421  121 VAL   A O   
2455 C CB  . VAL   A 121 ? 0.2156 0.2610 0.2104 0.0048  0.0374  0.0742  121 VAL   A CB  
2456 C CG1 . VAL   A 121 ? 0.2162 0.2781 0.2174 0.0114  0.0482  0.0733  121 VAL   A CG1 
2457 C CG2 . VAL   A 121 ? 0.2418 0.2803 0.2598 -0.0021 0.0344  0.0627  121 VAL   A CG2 
2467 N N   . LEU   A 122 ? 0.1557 0.1669 0.1737 -0.0192 0.0195  0.0454  122 LEU   A N   
2468 C CA  . LEU   A 122 ? 0.1626 0.1549 0.1707 -0.0197 0.0309  0.0417  122 LEU   A CA  
2469 C C   . LEU   A 122 ? 0.1526 0.1599 0.1751 -0.0161 0.0204  0.0370  122 LEU   A C   
2470 O O   . LEU   A 122 ? 0.1520 0.1661 0.2135 -0.0241 0.0132  0.0441  122 LEU   A O   
2471 C CB  . LEU   A 122 ? 0.1791 0.1577 0.2032 -0.0092 0.0194  0.0459  122 LEU   A CB  
2472 C CG  . LEU   A 122 ? 0.1797 0.1638 0.2033 -0.0097 0.0329  0.0378  122 LEU   A CG  
2473 C CD1 . LEU   A 122 ? 0.1940 0.1649 0.2161 -0.0149 0.0328  0.0362  122 LEU   A CD1 
2474 C CD2 . LEU   A 122 ? 0.1732 0.1580 0.1911 -0.0099 0.0292  0.0285  122 LEU   A CD2 
2486 N N   A LEU   A 123 ? 0.1499 0.1534 0.1771 -0.0214 0.0197  0.0372  123 LEU   A N   
2487 N N   B LEU   A 123 ? 0.1531 0.1529 0.1672 -0.0147 0.0165  0.0325  123 LEU   A N   
2488 C CA  A LEU   A 123 ? 0.1469 0.1570 0.1638 -0.0178 0.0205  0.0386  123 LEU   A CA  
2489 C CA  B LEU   A 123 ? 0.1526 0.1508 0.1600 -0.0091 0.0137  0.0276  123 LEU   A CA  
2490 C C   A LEU   A 123 ? 0.1347 0.1471 0.1554 -0.0124 0.0175  0.0324  123 LEU   A C   
2491 C C   B LEU   A 123 ? 0.1498 0.1436 0.1522 -0.0040 0.0129  0.0208  123 LEU   A C   
2492 O O   A LEU   A 123 ? 0.1278 0.1427 0.1664 -0.0209 0.0188  0.0297  123 LEU   A O   
2493 O O   B LEU   A 123 ? 0.1478 0.1401 0.1577 -0.0040 0.0194  0.0090  123 LEU   A O   
2494 C CB  A LEU   A 123 ? 0.1592 0.1691 0.1672 -0.0177 0.0405  0.0390  123 LEU   A CB  
2495 C CB  B LEU   A 123 ? 0.1545 0.1549 0.1645 -0.0069 0.0104  0.0297  123 LEU   A CB  
2496 C CG  A LEU   A 123 ? 0.1669 0.1843 0.1804 -0.0135 0.0372  0.0229  123 LEU   A CG  
2497 C CG  B LEU   A 123 ? 0.1560 0.1625 0.1778 -0.0083 0.0063  0.0261  123 LEU   A CG  
2498 C CD1 A LEU   A 123 ? 0.1738 0.1922 0.2008 -0.0025 0.0332  0.0190  123 LEU   A CD1 
2499 C CD1 B LEU   A 123 ? 0.1600 0.1688 0.2009 -0.0025 0.0070  0.0206  123 LEU   A CD1 
2500 C CD2 A LEU   A 123 ? 0.1775 0.1917 0.1836 -0.0115 0.0277  0.0182  123 LEU   A CD2 
2501 C CD2 B LEU   A 123 ? 0.1620 0.1673 0.1855 -0.0081 -0.0027 0.0205  123 LEU   A CD2 
2524 N N   A ALA   A 124 ? 0.1284 0.1325 0.1579 -0.0124 0.0191  0.0388  124 ALA   A N   
2525 N N   B ALA   A 124 ? 0.1489 0.1338 0.1578 -0.0060 0.0043  0.0262  124 ALA   A N   
2526 C CA  A ALA   A 124 ? 0.1190 0.1259 0.1604 -0.0054 0.0151  0.0396  124 ALA   A CA  
2527 C CA  B ALA   A 124 ? 0.1504 0.1380 0.1748 -0.0112 0.0076  0.0332  124 ALA   A CA  
2528 C C   A ALA   A 124 ? 0.1132 0.1273 0.1659 -0.0093 0.0107  0.0347  124 ALA   A C   
2529 C C   B ALA   A 124 ? 0.1416 0.1372 0.1712 -0.0074 0.0086  0.0387  124 ALA   A C   
2530 O O   A ALA   A 124 ? 0.1157 0.1382 0.1919 -0.0082 0.0271  0.0405  124 ALA   A O   
2531 O O   B ALA   A 124 ? 0.1397 0.1394 0.1882 0.0055  0.0142  0.0372  124 ALA   A O   
2532 C CB  A ALA   A 124 ? 0.1155 0.1173 0.1862 -0.0021 0.0045  0.0297  124 ALA   A CB  
2533 C CB  B ALA   A 124 ? 0.1643 0.1409 0.1935 -0.0152 0.0075  0.0321  124 ALA   A CB  
2544 N N   A PRO   A 125 ? 0.1155 0.1324 0.1805 -0.0050 0.0101  0.0411  125 PRO   A N   
2545 N N   B PRO   A 125 ? 0.1284 0.1380 0.1542 -0.0047 0.0013  0.0403  125 PRO   A N   
2546 C CA  A PRO   A 125 ? 0.1257 0.1407 0.1888 -0.0100 -0.0012 0.0284  125 PRO   A CA  
2547 C CA  B PRO   A 125 ? 0.1328 0.1484 0.1580 -0.0069 0.0022  0.0260  125 PRO   A CA  
2548 C C   A PRO   A 125 ? 0.1160 0.1424 0.1927 -0.0135 0.0034  0.0313  125 PRO   A C   
2549 C C   B PRO   A 125 ? 0.1482 0.1606 0.1660 -0.0051 0.0053  0.0189  125 PRO   A C   
2550 O O   A PRO   A 125 ? 0.1288 0.1325 0.2172 -0.0085 0.0022  0.0267  125 PRO   A O   
2551 O O   B PRO   A 125 ? 0.1529 0.1587 0.1709 -0.0038 0.0065  0.0187  125 PRO   A O   
2552 C CB  A PRO   A 125 ? 0.1386 0.1397 0.1813 -0.0163 -0.0025 0.0315  125 PRO   A CB  
2553 C CB  B PRO   A 125 ? 0.1169 0.1436 0.1560 -0.0120 0.0003  0.0320  125 PRO   A CB  
2554 C CG  A PRO   A 125 ? 0.1383 0.1340 0.1822 -0.0186 -0.0067 0.0405  125 PRO   A CG  
2555 C CG  B PRO   A 125 ? 0.1114 0.1368 0.1593 -0.0075 0.0052  0.0360  125 PRO   A CG  
2556 C CD  A PRO   A 125 ? 0.1234 0.1363 0.1845 -0.0120 0.0113  0.0344  125 PRO   A CD  
2557 C CD  B PRO   A 125 ? 0.1141 0.1274 0.1591 -0.0054 0.0126  0.0377  125 PRO   A CD  
2572 N N   A LEU   A 126 ? 0.1131 0.1531 0.1930 -0.0075 0.0001  0.0237  126 LEU   A N   
2573 N N   B LEU   A 126 ? 0.1619 0.1728 0.1801 -0.0025 0.0010  0.0065  126 LEU   A N   
2574 C CA  A LEU   A 126 ? 0.1261 0.1501 0.1940 -0.0141 0.0046  0.0286  126 LEU   A CA  
2575 C CA  B LEU   A 126 ? 0.1739 0.1698 0.1966 -0.0023 0.0039  0.0122  126 LEU   A CA  
2576 C C   A LEU   A 126 ? 0.1306 0.1444 0.1943 -0.0063 0.0027  0.0196  126 LEU   A C   
2577 C C   B LEU   A 126 ? 0.1733 0.1625 0.1990 0.0099  0.0126  0.0228  126 LEU   A C   
2578 O O   A LEU   A 126 ? 0.1451 0.1340 0.1904 -0.0120 0.0071  0.0192  126 LEU   A O   
2579 O O   B LEU   A 126 ? 0.1819 0.1609 0.2362 0.0054  0.0277  0.0112  126 LEU   A O   
2580 C CB  A LEU   A 126 ? 0.1307 0.1580 0.2034 -0.0173 -0.0039 0.0298  126 LEU   A CB  
2581 C CB  B LEU   A 126 ? 0.1860 0.1824 0.2219 -0.0112 0.0003  0.0119  126 LEU   A CB  
2582 C CG  A LEU   A 126 ? 0.1298 0.1832 0.2299 -0.0121 0.0050  0.0409  126 LEU   A CG  
2583 C CG  B LEU   A 126 ? 0.1901 0.1874 0.2603 -0.0120 -0.0029 0.0130  126 LEU   A CG  
2584 C CD1 A LEU   A 126 ? 0.1326 0.1948 0.2477 -0.0155 0.0049  0.0478  126 LEU   A CD1 
2585 C CD1 B LEU   A 126 ? 0.1871 0.1863 0.2715 -0.0153 -0.0073 0.0089  126 LEU   A CD1 
2586 C CD2 A LEU   A 126 ? 0.1429 0.1775 0.2266 -0.0259 0.0000  0.0575  126 LEU   A CD2 
2587 C CD2 B LEU   A 126 ? 0.1954 0.1920 0.2821 -0.0124 -0.0142 0.0104  126 LEU   A CD2 
2610 N N   A LEU   A 127 ? 0.1270 0.1502 0.1991 0.0004  0.0046  0.0191  127 LEU   A N   
2611 N N   B LEU   A 127 ? 0.1638 0.1561 0.1708 0.0121  0.0025  0.0449  127 LEU   A N   
2612 C CA  A LEU   A 127 ? 0.1294 0.1554 0.1850 -0.0015 0.0014  0.0165  127 LEU   A CA  
2613 C CA  B LEU   A 127 ? 0.1573 0.1614 0.1675 0.0035  -0.0016 0.0434  127 LEU   A CA  
2614 C C   A LEU   A 127 ? 0.1361 0.1471 0.1688 -0.0057 0.0028  0.0142  127 LEU   A C   
2615 C C   B LEU   A 127 ? 0.1644 0.1667 0.1738 -0.0054 -0.0055 0.0349  127 LEU   A C   
2616 O O   A LEU   A 127 ? 0.1412 0.1493 0.1780 -0.0127 -0.0007 0.0228  127 LEU   A O   
2617 O O   B LEU   A 127 ? 0.1692 0.1715 0.1761 -0.0139 -0.0028 0.0380  127 LEU   A O   
2618 C CB  A LEU   A 127 ? 0.1365 0.1646 0.1875 0.0104  0.0071  0.0116  127 LEU   A CB  
2619 C CB  B LEU   A 127 ? 0.1505 0.1673 0.1670 0.0056  0.0030  0.0362  127 LEU   A CB  
2620 C CG  A LEU   A 127 ? 0.1413 0.1692 0.1851 0.0124  -0.0006 0.0223  127 LEU   A CG  
2621 C CG  B LEU   A 127 ? 0.1461 0.1717 0.1645 0.0096  0.0026  0.0345  127 LEU   A CG  
2622 C CD1 A LEU   A 127 ? 0.1514 0.1600 0.1967 0.0044  0.0015  0.0193  127 LEU   A CD1 
2623 C CD1 B LEU   A 127 ? 0.1408 0.1756 0.1786 0.0163  0.0087  0.0349  127 LEU   A CD1 
2624 C CD2 A LEU   A 127 ? 0.1535 0.1766 0.2027 0.0203  -0.0110 0.0172  127 LEU   A CD2 
2625 C CD2 B LEU   A 127 ? 0.1562 0.1759 0.1634 0.0126  -0.0125 0.0255  127 LEU   A CD2 
2648 N N   A SER   A 128 ? 0.1477 0.1485 0.1628 -0.0096 -0.0009 0.0150  128 SER   A N   
2649 N N   B SER   A 128 ? 0.1721 0.1729 0.1807 -0.0081 -0.0054 0.0275  128 SER   A N   
2650 C CA  A SER   A 128 ? 0.1585 0.1529 0.1495 -0.0066 -0.0059 0.0126  128 SER   A CA  
2651 C CA  B SER   A 128 ? 0.1787 0.1818 0.1830 -0.0051 -0.0114 0.0209  128 SER   A CA  
2652 C C   A SER   A 128 ? 0.1635 0.1500 0.1521 0.0002  -0.0052 0.0159  128 SER   A C   
2653 C C   B SER   A 128 ? 0.1931 0.1958 0.1833 -0.0035 -0.0252 0.0262  128 SER   A C   
2654 O O   A SER   A 128 ? 0.1713 0.1696 0.1597 0.0032  0.0017  0.0106  128 SER   A O   
2655 O O   B SER   A 128 ? 0.1911 0.1926 0.1832 -0.0033 -0.0239 0.0205  128 SER   A O   
2656 C CB  A SER   A 128 ? 0.1570 0.1577 0.1473 -0.0118 -0.0127 0.0112  128 SER   A CB  
2657 C CB  B SER   A 128 ? 0.1742 0.1778 0.1767 -0.0092 -0.0114 0.0262  128 SER   A CB  
2658 O OG  A SER   A 128 ? 0.1523 0.1601 0.1657 -0.0068 -0.0113 0.0074  128 SER   A OG  
2659 O OG  B SER   A 128 ? 0.1663 0.1752 0.1786 -0.0098 -0.0078 0.0224  128 SER   A OG  
2670 N N   A ALA   A 129 ? 0.1503 0.1588 0.1757 -0.0010 -0.0054 0.0358  129 ALA   A N   
2671 N N   B ALA   A 129 ? 0.2077 0.2228 0.1935 0.0051  -0.0287 0.0342  129 ALA   A N   
2672 C CA  A ALA   A 129 ? 0.1449 0.1587 0.1962 -0.0029 -0.0037 0.0369  129 ALA   A CA  
2673 C CA  B ALA   A 129 ? 0.2286 0.2480 0.2107 0.0103  -0.0247 0.0219  129 ALA   A CA  
2674 C C   A ALA   A 129 ? 0.1527 0.1572 0.1767 -0.0018 -0.0111 0.0097  129 ALA   A C   
2675 C C   B ALA   A 129 ? 0.2450 0.2644 0.2224 0.0162  -0.0139 0.0131  129 ALA   A C   
2676 O O   A ALA   A 129 ? 0.1614 0.1654 0.1617 -0.0105 -0.0038 0.0181  129 ALA   A O   
2677 O O   B ALA   A 129 ? 0.2436 0.2673 0.2216 0.0198  -0.0073 0.0090  129 ALA   A O   
2678 C CB  A ALA   A 129 ? 0.1486 0.1687 0.2238 0.0105  -0.0062 0.0518  129 ALA   A CB  
2679 C CB  B ALA   A 129 ? 0.2326 0.2553 0.2201 0.0064  -0.0277 0.0181  129 ALA   A CB  
2690 N N   A GLY   A 130 ? 0.1659 0.1527 0.2141 0.0014  0.0002  0.0078  130 GLY   A N   
2691 N N   B GLY   A 130 ? 0.2599 0.2777 0.2347 0.0201  -0.0102 0.0069  130 GLY   A N   
2692 C CA  A GLY   A 130 ? 0.1951 0.1526 0.2337 0.0030  0.0064  0.0075  130 GLY   A CA  
2693 C CA  B GLY   A 130 ? 0.2710 0.2855 0.2403 0.0232  -0.0043 0.0025  130 GLY   A CA  
2694 C C   A GLY   A 130 ? 0.2053 0.1539 0.2255 0.0017  -0.0075 0.0048  130 GLY   A C   
2695 C C   B GLY   A 130 ? 0.2818 0.2928 0.2474 0.0255  -0.0061 -0.0011 130 GLY   A C   
2696 O O   A GLY   A 130 ? 0.2079 0.1429 0.2151 0.0007  -0.0277 0.0052  130 GLY   A O   
2697 O O   B GLY   A 130 ? 0.2818 0.2962 0.2346 0.0295  0.0046  -0.0064 130 GLY   A O   
2704 N N   A ILE   A 131 ? 0.2162 0.1497 0.2071 -0.0082 -0.0093 0.0121  131 ILE   A N   
2705 N N   B ILE   A 131 ? 0.2890 0.2944 0.2695 0.0247  -0.0151 -0.0005 131 ILE   A N   
2706 C CA  A ILE   A 131 ? 0.2273 0.1452 0.1855 -0.0109 -0.0316 0.0075  131 ILE   A CA  
2707 C CA  B ILE   A 131 ? 0.2960 0.2934 0.2951 0.0207  -0.0177 -0.0027 131 ILE   A CA  
2708 C C   A ILE   A 131 ? 0.2123 0.1536 0.1675 -0.0128 -0.0312 0.0148  131 ILE   A C   
2709 C C   B ILE   A 131 ? 0.2900 0.2884 0.2900 0.0213  -0.0197 0.0066  131 ILE   A C   
2710 O O   A ILE   A 131 ? 0.2125 0.1545 0.1741 -0.0128 -0.0368 0.0181  131 ILE   A O   
2711 O O   B ILE   A 131 ? 0.2904 0.2911 0.3008 0.0235  -0.0098 0.0097  131 ILE   A O   
2712 C CB  A ILE   A 131 ? 0.2516 0.1607 0.2043 -0.0170 -0.0388 0.0010  131 ILE   A CB  
2713 C CB  B ILE   A 131 ? 0.3083 0.2997 0.3258 0.0154  -0.0162 -0.0133 131 ILE   A CB  
2714 C CG1 A ILE   A 131 ? 0.2597 0.1891 0.2052 -0.0290 -0.0459 -0.0090 131 ILE   A CG1 
2715 C CG1 B ILE   A 131 ? 0.3149 0.3044 0.3404 0.0118  -0.0136 -0.0207 131 ILE   A CG1 
2716 C CG2 A ILE   A 131 ? 0.2645 0.1543 0.2245 -0.0125 -0.0328 -0.0097 131 ILE   A CG2 
2717 C CG2 B ILE   A 131 ? 0.3123 0.3012 0.3366 0.0150  -0.0166 -0.0152 131 ILE   A CG2 
2718 C CD1 A ILE   A 131 ? 0.2645 0.2029 0.2284 -0.0354 -0.0488 -0.0106 131 ILE   A CD1 
2719 C CD1 B ILE   A 131 ? 0.3178 0.3082 0.3501 0.0106  -0.0117 -0.0236 131 ILE   A CD1 
2742 N N   A PHE   A 132 ? 0.2003 0.1464 0.1549 -0.0086 -0.0336 0.0194  132 PHE   A N   
2743 N N   B PHE   A 132 ? 0.2836 0.2808 0.2809 0.0192  -0.0298 0.0134  132 PHE   A N   
2744 C CA  A PHE   A 132 ? 0.2010 0.1607 0.1446 -0.0159 -0.0283 0.0084  132 PHE   A CA  
2745 C CA  B PHE   A 132 ? 0.2743 0.2732 0.2724 0.0124  -0.0384 0.0178  132 PHE   A CA  
2746 C C   A PHE   A 132 ? 0.2071 0.1794 0.1515 -0.0126 -0.0312 0.0080  132 PHE   A C   
2747 C C   B PHE   A 132 ? 0.2699 0.2779 0.2643 0.0104  -0.0399 0.0159  132 PHE   A C   
2748 O O   A PHE   A 132 ? 0.2173 0.1932 0.1613 -0.0091 -0.0308 0.0070  132 PHE   A O   
2749 O O   B PHE   A 132 ? 0.2716 0.2784 0.2530 0.0098  -0.0391 0.0131  132 PHE   A O   
2750 C CB  A PHE   A 132 ? 0.1914 0.1464 0.1461 -0.0149 -0.0265 0.0257  132 PHE   A CB  
2751 C CB  B PHE   A 132 ? 0.2696 0.2658 0.2822 0.0092  -0.0492 0.0197  132 PHE   A CB  
2752 C CG  A PHE   A 132 ? 0.1876 0.1426 0.1348 -0.0103 -0.0274 0.0229  132 PHE   A CG  
2753 C CG  B PHE   A 132 ? 0.2724 0.2624 0.3057 0.0031  -0.0498 0.0191  132 PHE   A CG  
2754 C CD1 A PHE   A 132 ? 0.1834 0.1517 0.1686 0.0036  -0.0295 0.0033  132 PHE   A CD1 
2755 C CD1 B PHE   A 132 ? 0.2754 0.2626 0.3181 0.0002  -0.0464 0.0156  132 PHE   A CD1 
2756 C CD2 A PHE   A 132 ? 0.1894 0.1532 0.1477 -0.0051 -0.0296 0.0091  132 PHE   A CD2 
2757 C CD2 B PHE   A 132 ? 0.2721 0.2593 0.3094 0.0008  -0.0501 0.0166  132 PHE   A CD2 
2758 C CE1 A PHE   A 132 ? 0.1785 0.1637 0.1740 0.0095  -0.0336 -0.0080 132 PHE   A CE1 
2759 C CE1 B PHE   A 132 ? 0.2760 0.2602 0.3219 -0.0011 -0.0458 0.0111  132 PHE   A CE1 
2760 C CE2 A PHE   A 132 ? 0.1808 0.1639 0.1589 0.0089  -0.0317 0.0059  132 PHE   A CE2 
2761 C CE2 B PHE   A 132 ? 0.2718 0.2565 0.3159 -0.0022 -0.0487 0.0099  132 PHE   A CE2 
2762 C CZ  A PHE   A 132 ? 0.1736 0.1615 0.1623 0.0065  -0.0348 0.0003  132 PHE   A CZ  
2763 C CZ  B PHE   A 132 ? 0.2721 0.2572 0.3180 -0.0027 -0.0498 0.0086  132 PHE   A CZ  
2782 N N   A GLY   A 133 ? 0.2031 0.1861 0.1531 -0.0074 -0.0499 0.0269  133 GLY   A N   
2783 N N   B GLY   A 133 ? 0.2659 0.2799 0.2711 0.0073  -0.0418 0.0125  133 GLY   A N   
2784 C CA  A GLY   A 133 ? 0.2012 0.2031 0.1767 -0.0144 -0.0557 0.0111  133 GLY   A CA  
2785 C CA  B GLY   A 133 ? 0.2619 0.2824 0.2750 0.0010  -0.0492 0.0043  133 GLY   A CA  
2786 C C   A GLY   A 133 ? 0.2001 0.2162 0.1766 -0.0219 -0.0639 0.0024  133 GLY   A C   
2787 C C   B GLY   A 133 ? 0.2591 0.2843 0.2816 -0.0044 -0.0555 -0.0053 133 GLY   A C   
2788 O O   A GLY   A 133 ? 0.2121 0.2392 0.2201 -0.0286 -0.0744 -0.0117 133 GLY   A O   
2789 O O   B GLY   A 133 ? 0.2596 0.2944 0.2954 -0.0038 -0.0596 -0.0093 133 GLY   A O   
2796 N N   A ALA   A 134 ? 0.1950 0.2039 0.1435 -0.0256 -0.0424 0.0005  134 ALA   A N   
2797 N N   B ALA   A 134 ? 0.2567 0.2749 0.2714 -0.0077 -0.0531 -0.0095 134 ALA   A N   
2798 C CA  A ALA   A 134 ? 0.1880 0.2062 0.1642 -0.0234 -0.0260 -0.0013 134 ALA   A CA  
2799 C CA  B ALA   A 134 ? 0.2539 0.2668 0.2601 -0.0113 -0.0523 -0.0091 134 ALA   A CA  
2800 C C   A ALA   A 134 ? 0.1862 0.2156 0.1733 -0.0254 -0.0170 0.0160  134 ALA   A C   
2801 C C   B ALA   A 134 ? 0.2506 0.2628 0.2629 -0.0108 -0.0503 0.0065  134 ALA   A C   
2802 O O   A ALA   A 134 ? 0.1947 0.2228 0.2063 -0.0190 0.0096  0.0187  134 ALA   A O   
2803 O O   B ALA   A 134 ? 0.2529 0.2661 0.2729 -0.0144 -0.0442 0.0165  134 ALA   A O   
2804 C CB  A ALA   A 134 ? 0.1930 0.2004 0.1810 -0.0191 -0.0141 -0.0040 134 ALA   A CB  
2805 C CB  B ALA   A 134 ? 0.2546 0.2623 0.2524 -0.0112 -0.0497 -0.0191 134 ALA   A CB  
2816 N N   A ASP   A 135 ? 0.1920 0.2252 0.2071 -0.0319 -0.0279 0.0362  135 ASP   A N   
2817 N N   B ASP   A 135 ? 0.2492 0.2567 0.2642 -0.0055 -0.0488 0.0138  135 ASP   A N   
2818 C CA  A ASP   A 135 ? 0.1884 0.2366 0.2412 -0.0461 -0.0472 0.0604  135 ASP   A CA  
2819 C CA  B ASP   A 135 ? 0.2457 0.2536 0.2667 -0.0033 -0.0462 0.0204  135 ASP   A CA  
2820 C C   A ASP   A 135 ? 0.1732 0.2239 0.2427 -0.0329 -0.0354 0.0827  135 ASP   A C   
2821 C C   B ASP   A 135 ? 0.2332 0.2482 0.2482 -0.0000 -0.0404 0.0380  135 ASP   A C   
2822 O O   A ASP   A 135 ? 0.1625 0.2044 0.2390 -0.0338 -0.0442 0.0779  135 ASP   A O   
2823 O O   B ASP   A 135 ? 0.2304 0.2418 0.2439 -0.0023 -0.0405 0.0418  135 ASP   A O   
2824 C CB  A ASP   A 135 ? 0.2073 0.2634 0.2811 -0.0632 -0.0690 0.0540  135 ASP   A CB  
2825 C CB  B ASP   A 135 ? 0.2550 0.2567 0.2955 -0.0050 -0.0439 0.0109  135 ASP   A CB  
2826 C CG  A ASP   A 135 ? 0.2255 0.2872 0.3310 -0.0736 -0.0660 0.0474  135 ASP   A CG  
2827 C CG  B ASP   A 135 ? 0.2631 0.2623 0.3198 -0.0071 -0.0384 0.0035  135 ASP   A CG  
2828 O OD1 A ASP   A 135 ? 0.2202 0.2942 0.3328 -0.0776 -0.0768 0.0638  135 ASP   A OD1 
2829 O OD1 B ASP   A 135 ? 0.2685 0.2641 0.3371 -0.0095 -0.0313 -0.0046 135 ASP   A OD1 
2830 O OD2 A ASP   A 135 ? 0.2574 0.3021 0.3839 -0.0678 -0.0328 0.0391  135 ASP   A OD2 
2831 O OD2 B ASP   A 135 ? 0.2616 0.2638 0.3294 -0.0098 -0.0415 0.0080  135 ASP   A OD2 
2840 N N   A PRO   A 136 ? 0.1655 0.2294 0.2522 -0.0070 -0.0165 0.1036  136 PRO   A N   
2841 N N   B PRO   A 136 ? 0.2233 0.2496 0.2465 0.0044  -0.0283 0.0495  136 PRO   A N   
2842 C CA  A PRO   A 136 ? 0.1555 0.2287 0.2597 -0.0060 0.0004  0.0905  136 PRO   A CA  
2843 C CA  B PRO   A 136 ? 0.2195 0.2538 0.2456 0.0048  -0.0197 0.0480  136 PRO   A CA  
2844 C C   A PRO   A 136 ? 0.1228 0.2210 0.2381 -0.0040 0.0028  0.0771  136 PRO   A C   
2845 C C   B PRO   A 136 ? 0.2087 0.2564 0.2401 0.0057  -0.0225 0.0490  136 PRO   A C   
2846 O O   A PRO   A 136 ? 0.1148 0.2115 0.2260 -0.0058 0.0067  0.0694  136 PRO   A O   
2847 O O   B PRO   A 136 ? 0.2081 0.2548 0.2328 0.0064  -0.0294 0.0568  136 PRO   A O   
2848 C CB  A PRO   A 136 ? 0.1843 0.2324 0.2821 0.0027  0.0082  0.0929  136 PRO   A CB  
2849 C CB  B PRO   A 136 ? 0.2287 0.2524 0.2532 0.0071  -0.0134 0.0480  136 PRO   A CB  
2850 C CG  A PRO   A 136 ? 0.1974 0.2417 0.2983 0.0086  0.0097  0.0958  136 PRO   A CG  
2851 C CG  B PRO   A 136 ? 0.2332 0.2519 0.2595 0.0081  -0.0134 0.0503  136 PRO   A CG  
2852 C CD  A PRO   A 136 ? 0.1840 0.2383 0.2766 0.0093  0.0077  0.1101  136 PRO   A CD  
2853 C CD  B PRO   A 136 ? 0.2252 0.2492 0.2579 0.0057  -0.0197 0.0515  136 PRO   A CD  
2868 N N   A ILE   A 137 ? 0.1260 0.2259 0.2423 -0.0079 -0.0130 0.0705  137 ILE   A N   
2869 N N   B ILE   A 137 ? 0.2054 0.2601 0.2400 0.0002  -0.0206 0.0423  137 ILE   A N   
2870 C CA  A ILE   A 137 ? 0.1289 0.2383 0.2368 -0.0172 -0.0269 0.0693  137 ILE   A CA  
2871 C CA  B ILE   A 137 ? 0.2044 0.2665 0.2445 -0.0046 -0.0252 0.0344  137 ILE   A CA  
2872 C C   A ILE   A 137 ? 0.1288 0.2280 0.2326 -0.0267 -0.0276 0.0684  137 ILE   A C   
2873 C C   B ILE   A 137 ? 0.1985 0.2598 0.2534 -0.0134 -0.0227 0.0256  137 ILE   A C   
2874 O O   A ILE   A 137 ? 0.1360 0.2217 0.2319 -0.0383 -0.0297 0.0649  137 ILE   A O   
2875 O O   B ILE   A 137 ? 0.1989 0.2595 0.2615 -0.0167 -0.0231 0.0199  137 ILE   A O   
2876 C CB  A ILE   A 137 ? 0.1339 0.2676 0.2476 -0.0213 -0.0435 0.0695  137 ILE   A CB  
2877 C CB  B ILE   A 137 ? 0.2096 0.2779 0.2401 -0.0031 -0.0282 0.0351  137 ILE   A CB  
2878 C CG1 A ILE   A 137 ? 0.1486 0.2933 0.2656 -0.0162 -0.0361 0.0740  137 ILE   A CG1 
2879 C CG1 B ILE   A 137 ? 0.2158 0.2868 0.2466 0.0074  -0.0330 0.0394  137 ILE   A CG1 
2880 C CG2 A ILE   A 137 ? 0.1451 0.2695 0.2541 -0.0245 -0.0420 0.0724  137 ILE   A CG2 
2881 C CG2 B ILE   A 137 ? 0.2131 0.2810 0.2337 -0.0035 -0.0264 0.0301  137 ILE   A CG2 
2882 C CD1 A ILE   A 137 ? 0.1636 0.3062 0.2855 -0.0102 -0.0217 0.0739  137 ILE   A CD1 
2883 C CD1 B ILE   A 137 ? 0.2209 0.2898 0.2528 0.0134  -0.0322 0.0450  137 ILE   A CD1 
2906 N N   A HIS   A 138 ? 0.1301 0.2393 0.2314 -0.0200 -0.0128 0.0545  138 HIS   A N   
2907 N N   B HIS   A 138 ? 0.1919 0.2570 0.2554 -0.0166 -0.0201 0.0200  138 HIS   A N   
2908 C CA  A HIS   A 138 ? 0.1395 0.2365 0.2294 -0.0185 -0.0142 0.0449  138 HIS   A CA  
2909 C CA  B HIS   A 138 ? 0.1826 0.2468 0.2488 -0.0202 -0.0200 0.0238  138 HIS   A CA  
2910 C C   A HIS   A 138 ? 0.1373 0.2191 0.2295 -0.0152 -0.0144 0.0513  138 HIS   A C   
2911 C C   B HIS   A 138 ? 0.1576 0.2255 0.2384 -0.0181 -0.0210 0.0381  138 HIS   A C   
2912 O O   A HIS   A 138 ? 0.1500 0.2193 0.2354 -0.0142 -0.0029 0.0490  138 HIS   A O   
2913 O O   B HIS   A 138 ? 0.1596 0.2242 0.2344 -0.0214 -0.0205 0.0395  138 HIS   A O   
2914 C CB  A HIS   A 138 ? 0.1549 0.2474 0.2213 -0.0166 -0.0211 0.0248  138 HIS   A CB  
2915 C CB  B HIS   A 138 ? 0.2023 0.2580 0.2494 -0.0246 -0.0227 0.0130  138 HIS   A CB  
2916 C CG  A HIS   A 138 ? 0.1751 0.2483 0.2436 -0.0208 -0.0265 0.0054  138 HIS   A CG  
2917 C CG  B HIS   A 138 ? 0.2161 0.2628 0.2505 -0.0277 -0.0151 0.0024  138 HIS   A CG  
2918 N ND1 A HIS   A 138 ? 0.1868 0.2538 0.2669 -0.0285 -0.0299 -0.0114 138 HIS   A ND1 
2919 N ND1 B HIS   A 138 ? 0.2225 0.2672 0.2587 -0.0299 -0.0111 -0.0046 138 HIS   A ND1 
2920 C CD2 A HIS   A 138 ? 0.1777 0.2454 0.2428 -0.0139 -0.0337 0.0017  138 HIS   A CD2 
2921 C CD2 B HIS   A 138 ? 0.2210 0.2660 0.2489 -0.0272 -0.0129 -0.0031 138 HIS   A CD2 
2922 C CE1 A HIS   A 138 ? 0.1904 0.2514 0.2660 -0.0240 -0.0318 -0.0149 138 HIS   A CE1 
2923 C CE1 B HIS   A 138 ? 0.2266 0.2677 0.2550 -0.0270 -0.0106 -0.0064 138 HIS   A CE1 
2924 N NE2 A HIS   A 138 ? 0.1875 0.2470 0.2511 -0.0180 -0.0254 -0.0099 138 HIS   A NE2 
2925 N NE2 B HIS   A 138 ? 0.2243 0.2663 0.2450 -0.0254 -0.0094 -0.0058 138 HIS   A NE2 
2940 N N   . SER   A 139 ? 0.1381 0.2062 0.2353 -0.0115 -0.0107 0.0520  139 SER   A N   
2941 C CA  . SER   A 139 ? 0.1387 0.1973 0.2345 -0.0091 -0.0084 0.0497  139 SER   A CA  
2942 C C   . SER   A 139 ? 0.1300 0.1802 0.2394 -0.0100 -0.0097 0.0424  139 SER   A C   
2943 O O   . SER   A 139 ? 0.1295 0.1742 0.2477 -0.0139 -0.0064 0.0453  139 SER   A O   
2944 C CB  . SER   A 139 ? 0.1353 0.1846 0.2345 -0.0135 0.0025  0.0542  139 SER   A CB  
2945 O OG  . SER   A 139 ? 0.1473 0.1841 0.2393 -0.0185 -0.0117 0.0621  139 SER   A OG  
2952 N N   . LEU   A 140 ? 0.1284 0.1859 0.2419 -0.0071 -0.0073 0.0544  140 LEU   A N   
2953 C CA  . LEU   A 140 ? 0.1317 0.1808 0.2352 -0.0130 -0.0031 0.0552  140 LEU   A CA  
2954 C C   . LEU   A 140 ? 0.1212 0.1883 0.2416 -0.0177 -0.0048 0.0552  140 LEU   A C   
2955 O O   . LEU   A 140 ? 0.1259 0.1846 0.2596 -0.0118 -0.0046 0.0518  140 LEU   A O   
2956 C CB  . LEU   A 140 ? 0.1303 0.1871 0.2325 -0.0122 -0.0001 0.0507  140 LEU   A CB  
2957 C CG  . LEU   A 140 ? 0.1317 0.2004 0.2506 -0.0250 0.0093  0.0598  140 LEU   A CG  
2958 C CD1 . LEU   A 140 ? 0.1396 0.1998 0.2695 -0.0127 0.0020  0.0556  140 LEU   A CD1 
2959 C CD2 . LEU   A 140 ? 0.1435 0.2172 0.2650 -0.0189 0.0147  0.0582  140 LEU   A CD2 
2971 N N   . ARG   A 141 ? 0.1285 0.1975 0.2538 -0.0178 -0.0158 0.0493  141 ARG   A N   
2972 C CA  . ARG   A 141 ? 0.1440 0.2111 0.2667 -0.0327 -0.0166 0.0249  141 ARG   A CA  
2973 C C   . ARG   A 141 ? 0.1441 0.1900 0.2452 -0.0265 -0.0124 0.0241  141 ARG   A C   
2974 O O   . ARG   A 141 ? 0.1414 0.1805 0.2536 -0.0294 0.0036  0.0189  141 ARG   A O   
2975 C CB  . ARG   A 141 ? 0.1642 0.2446 0.2970 -0.0398 -0.0297 0.0033  141 ARG   A CB  
2976 C CG  . ARG   A 141 ? 0.2081 0.2874 0.3466 -0.0466 -0.0242 0.0005  141 ARG   A CG  
2977 C CD  . ARG   A 141 ? 0.2379 0.3216 0.3792 -0.0596 -0.0215 0.0058  141 ARG   A CD  
2978 N NE  . ARG   A 141 ? 0.2323 0.3467 0.3862 -0.0712 -0.0307 0.0120  141 ARG   A NE  
2979 C CZ  . ARG   A 141 ? 0.2327 0.3680 0.3976 -0.0880 -0.0287 0.0150  141 ARG   A CZ  
2980 N NH1 . ARG   A 141 ? 0.2225 0.3746 0.4065 -0.0946 -0.0154 0.0070  141 ARG   A NH1 
2981 N NH2 . ARG   A 141 ? 0.2374 0.3789 0.3988 -0.0843 -0.0412 0.0146  141 ARG   A NH2 
2995 N N   . VAL   A 142 ? 0.1304 0.1825 0.2286 -0.0200 -0.0115 0.0156  142 VAL   A N   
2996 C CA  . VAL   A 142 ? 0.1374 0.1730 0.2313 -0.0191 0.0051  0.0167  142 VAL   A CA  
2997 C C   . VAL   A 142 ? 0.1187 0.1655 0.2278 -0.0183 0.0014  0.0213  142 VAL   A C   
2998 O O   . VAL   A 142 ? 0.1274 0.1657 0.2286 -0.0075 0.0039  0.0241  142 VAL   A O   
2999 C CB  . VAL   A 142 ? 0.1448 0.1836 0.2189 -0.0155 0.0019  0.0217  142 VAL   A CB  
3000 C CG1 . VAL   A 142 ? 0.1433 0.1745 0.2271 -0.0236 0.0029  0.0119  142 VAL   A CG1 
3001 C CG2 . VAL   A 142 ? 0.1584 0.2004 0.2365 -0.0096 -0.0025 0.0257  142 VAL   A CG2 
3011 N N   . CYS   A 143 ? 0.1289 0.1613 0.2162 -0.0150 -0.0059 0.0233  143 CYS   A N   
3012 C CA  . CYS   A 143 ? 0.1280 0.1569 0.2218 -0.0135 0.0040  0.0297  143 CYS   A CA  
3013 C C   . CYS   A 143 ? 0.1323 0.1540 0.2296 -0.0127 0.0049  0.0350  143 CYS   A C   
3014 O O   . CYS   A 143 ? 0.1271 0.1524 0.2245 -0.0080 0.0021  0.0403  143 CYS   A O   
3015 C CB  . CYS   A 143 ? 0.1432 0.1532 0.2360 -0.0093 0.0146  0.0427  143 CYS   A CB  
3016 S SG  . CYS   A 143 ? 0.1582 0.1651 0.2221 0.0028  0.0124  0.0266  143 CYS   A SG  
3022 N N   . VAL   A 144 ? 0.1270 0.1594 0.2511 -0.0102 0.0081  0.0415  144 VAL   A N   
3023 C CA  . VAL   A 144 ? 0.1339 0.1655 0.2877 -0.0179 0.0211  0.0432  144 VAL   A CA  
3024 C C   . VAL   A 144 ? 0.1333 0.1518 0.2837 -0.0264 -0.0073 0.0369  144 VAL   A C   
3025 O O   . VAL   A 144 ? 0.1523 0.1614 0.2982 -0.0125 -0.0050 0.0480  144 VAL   A O   
3026 C CB  . VAL   A 144 ? 0.1634 0.1902 0.3330 -0.0067 0.0412  0.0458  144 VAL   A CB  
3027 C CG1 . VAL   A 144 ? 0.1734 0.2097 0.3646 -0.0146 0.0303  0.0406  144 VAL   A CG1 
3028 C CG2 . VAL   A 144 ? 0.1570 0.1966 0.3425 -0.0087 0.0486  0.0546  144 VAL   A CG2 
3038 N N   . ASP   A 145 ? 0.1448 0.1497 0.2825 -0.0212 -0.0019 0.0286  145 ASP   A N   
3039 C CA  . ASP   A 145 ? 0.1595 0.1622 0.2933 -0.0229 -0.0033 0.0153  145 ASP   A CA  
3040 C C   . ASP   A 145 ? 0.1595 0.1490 0.2869 -0.0186 -0.0000 0.0050  145 ASP   A C   
3041 O O   . ASP   A 145 ? 0.1722 0.1537 0.3409 -0.0263 -0.0053 -0.0255 145 ASP   A O   
3042 C CB  . ASP   A 145 ? 0.1729 0.1894 0.3168 -0.0322 -0.0137 0.0028  145 ASP   A CB  
3043 C CG  . ASP   A 145 ? 0.1859 0.2338 0.3496 -0.0532 -0.0239 0.0098  145 ASP   A CG  
3044 O OD1 . ASP   A 145 ? 0.1863 0.2399 0.3674 -0.0681 -0.0124 0.0131  145 ASP   A OD1 
3045 O OD2 . ASP   A 145 ? 0.2105 0.2592 0.3584 -0.0645 -0.0486 0.0029  145 ASP   A OD2 
3050 N N   . THR   A 146 ? 0.1440 0.1429 0.2377 -0.0196 0.0087  0.0144  146 THR   A N   
3051 C CA  . THR   A 146 ? 0.1346 0.1381 0.2276 -0.0141 0.0073  0.0119  146 THR   A CA  
3052 C C   . THR   A 146 ? 0.1310 0.1352 0.2339 -0.0055 0.0080  0.0207  146 THR   A C   
3053 O O   . THR   A 146 ? 0.1419 0.1485 0.2423 0.0006  0.0025  0.0186  146 THR   A O   
3054 C CB  . THR   A 146 ? 0.1350 0.1418 0.2254 -0.0077 0.0104  0.0136  146 THR   A CB  
3055 O OG1 . THR   A 146 ? 0.1334 0.1585 0.2347 -0.0034 -0.0018 0.0106  146 THR   A OG1 
3056 C CG2 . THR   A 146 ? 0.1338 0.1478 0.2397 -0.0118 0.0061  0.0155  146 THR   A CG2 
3064 N N   . VAL   A 147 ? 0.1321 0.1373 0.2234 -0.0039 0.0105  0.0186  147 VAL   A N   
3065 C CA  . VAL   A 147 ? 0.1300 0.1387 0.2196 -0.0126 0.0239  0.0338  147 VAL   A CA  
3066 C C   . VAL   A 147 ? 0.1327 0.1423 0.2384 -0.0140 0.0151  0.0368  147 VAL   A C   
3067 O O   . VAL   A 147 ? 0.1360 0.1451 0.2563 -0.0169 0.0099  0.0399  147 VAL   A O   
3068 C CB  . VAL   A 147 ? 0.1445 0.1375 0.2207 -0.0089 0.0212  0.0347  147 VAL   A CB  
3069 C CG1 . VAL   A 147 ? 0.1793 0.1482 0.2208 -0.0078 0.0155  0.0470  147 VAL   A CG1 
3070 C CG2 . VAL   A 147 ? 0.1523 0.1347 0.2287 -0.0133 0.0137  0.0328  147 VAL   A CG2 
3080 N N   . ARG   A 148 ? 0.1352 0.1443 0.2467 -0.0135 0.0181  0.0555  148 ARG   A N   
3081 C CA  . ARG   A 148 ? 0.1399 0.1423 0.2431 -0.0096 0.0172  0.0536  148 ARG   A CA  
3082 C C   . ARG   A 148 ? 0.1520 0.1403 0.2394 -0.0112 0.0189  0.0681  148 ARG   A C   
3083 O O   . ARG   A 148 ? 0.1819 0.1559 0.2550 -0.0183 0.0233  0.0568  148 ARG   A O   
3084 C CB  . ARG   A 148 ? 0.1451 0.1462 0.2574 -0.0055 0.0247  0.0514  148 ARG   A CB  
3085 C CG  . ARG   A 148 ? 0.1609 0.1507 0.2965 -0.0048 0.0431  0.0371  148 ARG   A CG  
3086 C CD  . ARG   A 148 ? 0.1794 0.1433 0.3121 -0.0029 0.0523  0.0552  148 ARG   A CD  
3087 N NE  . ARG   A 148 ? 0.1704 0.1507 0.3108 0.0069  0.0539  0.0539  148 ARG   A NE  
3088 C CZ  . ARG   A 148 ? 0.1691 0.1396 0.2875 0.0031  0.0575  0.0535  148 ARG   A CZ  
3089 N NH1 . ARG   A 148 ? 0.1792 0.1436 0.2846 -0.0047 0.0477  0.0195  148 ARG   A NH1 
3090 N NH2 . ARG   A 148 ? 0.1613 0.1602 0.2952 0.0159  0.0575  0.0572  148 ARG   A NH2 
3104 N N   . THR   A 149 ? 0.1516 0.1537 0.2414 -0.0147 0.0107  0.0614  149 THR   A N   
3105 C CA  . THR   A 149 ? 0.1511 0.1614 0.2342 -0.0132 0.0124  0.0610  149 THR   A CA  
3106 C C   . THR   A 149 ? 0.1470 0.1596 0.2267 -0.0219 0.0163  0.0628  149 THR   A C   
3107 O O   . THR   A 149 ? 0.1480 0.1659 0.2483 -0.0187 0.0169  0.0522  149 THR   A O   
3108 C CB  . THR   A 149 ? 0.1484 0.1718 0.2335 -0.0143 0.0118  0.0475  149 THR   A CB  
3109 O OG1 . THR   A 149 ? 0.1542 0.1564 0.2407 -0.0232 0.0148  0.0432  149 THR   A OG1 
3110 C CG2 . THR   A 149 ? 0.1440 0.1885 0.2308 -0.0084 0.0018  0.0426  149 THR   A CG2 
3118 N N   . ASN   A 150 ? 0.1522 0.1621 0.2331 -0.0144 0.0064  0.0664  150 ASN   A N   
3119 C CA  . ASN   A 150 ? 0.1665 0.1716 0.2304 -0.0114 0.0193  0.0544  150 ASN   A CA  
3120 C C   . ASN   A 150 ? 0.1466 0.1604 0.2267 -0.0168 0.0136  0.0547  150 ASN   A C   
3121 O O   . ASN   A 150 ? 0.1557 0.1739 0.2512 -0.0148 0.0001  0.0490  150 ASN   A O   
3122 C CB  . ASN   A 150 ? 0.2103 0.1999 0.2615 -0.0185 0.0358  0.0737  150 ASN   A CB  
3123 C CG  . ASN   A 150 ? 0.2643 0.2364 0.3213 -0.0125 0.0217  0.0788  150 ASN   A CG  
3124 O OD1 . ASN   A 150 ? 0.2872 0.2451 0.3347 -0.0195 0.0288  0.1023  150 ASN   A OD1 
3125 N ND2 . ASN   A 150 ? 0.2951 0.2632 0.3600 -0.0077 0.0122  0.0808  150 ASN   A ND2 
3132 N N   . VAL   A 151 ? 0.1463 0.1472 0.2345 -0.0137 0.0101  0.0484  151 VAL   A N   
3133 C CA  . VAL   A 151 ? 0.1539 0.1527 0.2252 -0.0179 0.0149  0.0441  151 VAL   A CA  
3134 C C   . VAL   A 151 ? 0.1460 0.1477 0.2353 -0.0239 0.0240  0.0534  151 VAL   A C   
3135 O O   . VAL   A 151 ? 0.1498 0.1554 0.2752 -0.0216 0.0196  0.0445  151 VAL   A O   
3136 C CB  . VAL   A 151 ? 0.1836 0.1685 0.2194 -0.0080 0.0113  0.0433  151 VAL   A CB  
3137 C CG1 . VAL   A 151 ? 0.1811 0.1857 0.2465 -0.0184 0.0011  0.0391  151 VAL   A CG1 
3138 C CG2 . VAL   A 151 ? 0.1928 0.1712 0.2108 -0.0040 0.0251  0.0344  151 VAL   A CG2 
3148 N N   . TYR   A 152 ? 0.1416 0.1522 0.2309 -0.0172 0.0238  0.0496  152 TYR   A N   
3149 C CA  . TYR   A 152 ? 0.1455 0.1632 0.2090 -0.0173 0.0189  0.0449  152 TYR   A CA  
3150 C C   . TYR   A 152 ? 0.1382 0.1510 0.1996 -0.0170 0.0275  0.0480  152 TYR   A C   
3151 O O   . TYR   A 152 ? 0.1490 0.1509 0.2121 -0.0241 0.0292  0.0378  152 TYR   A O   
3152 C CB  . TYR   A 152 ? 0.1598 0.1715 0.2190 -0.0180 0.0276  0.0528  152 TYR   A CB  
3153 C CG  . TYR   A 152 ? 0.1738 0.1993 0.2164 -0.0230 0.0396  0.0567  152 TYR   A CG  
3154 C CD1 . TYR   A 152 ? 0.1901 0.2245 0.2303 -0.0128 0.0475  0.0622  152 TYR   A CD1 
3155 C CD2 . TYR   A 152 ? 0.1777 0.2168 0.2089 -0.0314 0.0314  0.0544  152 TYR   A CD2 
3156 C CE1 . TYR   A 152 ? 0.2169 0.2423 0.2438 -0.0060 0.0366  0.0749  152 TYR   A CE1 
3157 C CE2 . TYR   A 152 ? 0.2019 0.2341 0.2211 -0.0334 0.0330  0.0621  152 TYR   A CE2 
3158 C CZ  . TYR   A 152 ? 0.2306 0.2422 0.2337 -0.0201 0.0300  0.0877  152 TYR   A CZ  
3159 O OH  . TYR   A 152 ? 0.2635 0.2637 0.2775 -0.0107 0.0272  0.1062  152 TYR   A OH  
3169 N N   . LEU   A 153 ? 0.1387 0.1486 0.2240 -0.0221 0.0284  0.0528  153 LEU   A N   
3170 C CA  . LEU   A 153 ? 0.1344 0.1477 0.2337 -0.0104 0.0244  0.0476  153 LEU   A CA  
3171 C C   . LEU   A 153 ? 0.1379 0.1585 0.2503 -0.0043 0.0385  0.0457  153 LEU   A C   
3172 O O   . LEU   A 153 ? 0.1450 0.1656 0.2799 -0.0075 0.0582  0.0430  153 LEU   A O   
3173 C CB  . LEU   A 153 ? 0.1326 0.1595 0.2388 -0.0067 0.0165  0.0459  153 LEU   A CB  
3174 C CG  . LEU   A 153 ? 0.1398 0.1569 0.2333 -0.0107 0.0207  0.0411  153 LEU   A CG  
3175 C CD1 . LEU   A 153 ? 0.1507 0.1637 0.2337 -0.0132 0.0018  0.0390  153 LEU   A CD1 
3176 C CD2 . LEU   A 153 ? 0.1532 0.1645 0.2398 -0.0186 0.0348  0.0226  153 LEU   A CD2 
3188 N N   A ALA   A 154 ? 0.1379 0.1452 0.2554 -0.0080 0.0418  0.0491  154 ALA   A N   
3189 N N   B ALA   A 154 ? 0.1423 0.1619 0.2311 -0.0034 0.0334  0.0468  154 ALA   A N   
3190 C CA  A ALA   A 154 ? 0.1469 0.1432 0.2688 -0.0040 0.0414  0.0481  154 ALA   A CA  
3191 C CA  B ALA   A 154 ? 0.1507 0.1696 0.2261 -0.0011 0.0263  0.0465  154 ALA   A CA  
3192 C C   A ALA   A 154 ? 0.1391 0.1419 0.2750 -0.0017 0.0345  0.0585  154 ALA   A C   
3193 C C   B ALA   A 154 ? 0.1547 0.1788 0.2201 -0.0048 0.0201  0.0427  154 ALA   A C   
3194 O O   A ALA   A 154 ? 0.1452 0.1440 0.2767 -0.0066 0.0322  0.0538  154 ALA   A O   
3195 O O   B ALA   A 154 ? 0.1560 0.1749 0.2133 -0.0141 0.0231  0.0390  154 ALA   A O   
3196 C CB  A ALA   A 154 ? 0.1585 0.1463 0.2656 0.0023  0.0314  0.0342  154 ALA   A CB  
3197 C CB  B ALA   A 154 ? 0.1505 0.1700 0.2247 0.0028  0.0212  0.0454  154 ALA   A CB  
3208 N N   A VAL   A 155 ? 0.1456 0.1526 0.2889 0.0060  0.0351  0.0775  155 VAL   A N   
3209 N N   B VAL   A 155 ? 0.1656 0.1926 0.2301 0.0001  0.0154  0.0425  155 VAL   A N   
3210 C CA  A VAL   A 155 ? 0.1490 0.1692 0.2970 0.0021  0.0311  0.0875  155 VAL   A CA  
3211 C CA  B VAL   A 155 ? 0.1792 0.2118 0.2477 0.0042  0.0035  0.0379  155 VAL   A CA  
3212 C C   A VAL   A 155 ? 0.1455 0.1719 0.3246 0.0087  0.0255  0.0907  155 VAL   A C   
3213 C C   B VAL   A 155 ? 0.2032 0.2253 0.2823 0.0086  -0.0027 0.0266  155 VAL   A C   
3214 O O   A VAL   A 155 ? 0.1419 0.1682 0.3325 0.0190  0.0307  0.0614  155 VAL   A O   
3215 O O   B VAL   A 155 ? 0.2009 0.2194 0.2974 0.0059  0.0053  0.0173  155 VAL   A O   
3216 C CB  A VAL   A 155 ? 0.1508 0.1847 0.2767 0.0159  0.0196  0.0739  155 VAL   A CB  
3217 C CB  B VAL   A 155 ? 0.1642 0.2177 0.2283 0.0084  -0.0016 0.0408  155 VAL   A CB  
3218 C CG1 A VAL   A 155 ? 0.1593 0.2028 0.2795 0.0190  0.0120  0.0710  155 VAL   A CG1 
3219 C CG1 B VAL   A 155 ? 0.1566 0.2236 0.2226 0.0112  -0.0031 0.0384  155 VAL   A CG1 
3220 C CG2 A VAL   A 155 ? 0.1606 0.1954 0.2730 0.0269  0.0093  0.0645  155 VAL   A CG2 
3221 C CG2 B VAL   A 155 ? 0.1562 0.2183 0.2187 0.0060  0.0009  0.0405  155 VAL   A CG2 
3240 N N   A PHE   A 156 ? 0.1562 0.1770 0.3429 0.0135  0.0141  0.1084  156 PHE   A N   
3241 N N   B PHE   A 156 ? 0.2308 0.2428 0.2998 0.0163  -0.0141 0.0222  156 PHE   A N   
3242 C CA  A PHE   A 156 ? 0.1815 0.1799 0.3644 0.0168  0.0076  0.1066  156 PHE   A CA  
3243 C CA  B PHE   A 156 ? 0.2600 0.2604 0.3246 0.0201  -0.0141 0.0106  156 PHE   A CA  
3244 C C   A PHE   A 156 ? 0.1790 0.1921 0.3685 0.0306  0.0044  0.1085  156 PHE   A C   
3245 C C   B PHE   A 156 ? 0.2708 0.2669 0.3244 0.0169  -0.0102 0.0164  156 PHE   A C   
3246 O O   A PHE   A 156 ? 0.1833 0.1968 0.3970 0.0205  0.0087  0.0815  156 PHE   A O   
3247 O O   B PHE   A 156 ? 0.2828 0.2759 0.3385 0.0149  -0.0106 0.0181  156 PHE   A O   
3248 C CB  A PHE   A 156 ? 0.2201 0.1841 0.3619 0.0099  -0.0086 0.1136  156 PHE   A CB  
3249 C CB  B PHE   A 156 ? 0.2834 0.2739 0.3434 0.0263  -0.0146 -0.0031 156 PHE   A CB  
3250 C CG  A PHE   A 156 ? 0.2600 0.1913 0.3742 0.0227  -0.0307 0.0963  156 PHE   A CG  
3251 C CG  B PHE   A 156 ? 0.3025 0.2873 0.3555 0.0327  -0.0136 -0.0156 156 PHE   A CG  
3252 C CD1 A PHE   A 156 ? 0.2811 0.1974 0.3839 0.0320  -0.0334 0.0848  156 PHE   A CD1 
3253 C CD1 B PHE   A 156 ? 0.3096 0.2931 0.3596 0.0358  -0.0144 -0.0193 156 PHE   A CD1 
3254 C CD2 A PHE   A 156 ? 0.2743 0.2027 0.3825 0.0339  -0.0371 0.0887  156 PHE   A CD2 
3255 C CD2 B PHE   A 156 ? 0.3113 0.2922 0.3606 0.0369  -0.0098 -0.0245 156 PHE   A CD2 
3256 C CE1 A PHE   A 156 ? 0.2983 0.2077 0.3976 0.0388  -0.0330 0.0687  156 PHE   A CE1 
3257 C CE1 B PHE   A 156 ? 0.3161 0.2996 0.3642 0.0345  -0.0123 -0.0245 156 PHE   A CE1 
3258 C CE2 A PHE   A 156 ? 0.2948 0.2145 0.3923 0.0361  -0.0386 0.0720  156 PHE   A CE2 
3259 C CE2 B PHE   A 156 ? 0.3155 0.2973 0.3623 0.0381  -0.0068 -0.0287 156 PHE   A CE2 
3260 C CZ  A PHE   A 156 ? 0.3032 0.2168 0.3989 0.0403  -0.0346 0.0618  156 PHE   A CZ  
3261 C CZ  B PHE   A 156 ? 0.3180 0.3007 0.3645 0.0348  -0.0099 -0.0297 156 PHE   A CZ  
3280 N N   A ASP   A 157 ? 0.1918 0.2082 0.3498 0.0307  0.0010  0.1362  157 ASP   A N   
3281 N N   B ASP   A 157 ? 0.2679 0.2668 0.3215 0.0125  -0.0087 0.0222  157 ASP   A N   
3282 C CA  A ASP   A 157 ? 0.2090 0.2329 0.3614 0.0364  -0.0114 0.1307  157 ASP   A CA  
3283 C CA  B ASP   A 157 ? 0.2618 0.2659 0.3112 0.0069  -0.0112 0.0269  157 ASP   A CA  
3284 C C   A ASP   A 157 ? 0.1948 0.2473 0.3626 0.0395  -0.0029 0.1264  157 ASP   A C   
3285 C C   B ASP   A 157 ? 0.2553 0.2591 0.3048 0.0003  -0.0130 0.0169  157 ASP   A C   
3286 O O   A ASP   A 157 ? 0.1875 0.2427 0.3661 0.0343  -0.0045 0.1337  157 ASP   A O   
3287 O O   B ASP   A 157 ? 0.2522 0.2536 0.3128 -0.0028 -0.0141 0.0171  157 ASP   A O   
3288 C CB  A ASP   A 157 ? 0.2386 0.2466 0.3899 0.0417  -0.0235 0.1252  157 ASP   A CB  
3289 C CB  B ASP   A 157 ? 0.2611 0.2727 0.3137 0.0115  -0.0064 0.0461  157 ASP   A CB  
3290 C CG  A ASP   A 157 ? 0.2676 0.2556 0.4270 0.0530  -0.0384 0.1239  157 ASP   A CG  
3291 C CG  B ASP   A 157 ? 0.2647 0.2824 0.3289 0.0170  -0.0013 0.0590  157 ASP   A CG  
3292 O OD1 A ASP   A 157 ? 0.2960 0.2659 0.4526 0.0497  -0.0499 0.1040  157 ASP   A OD1 
3293 O OD1 B ASP   A 157 ? 0.2657 0.2863 0.3396 0.0198  -0.0040 0.0726  157 ASP   A OD1 
3294 O OD2 A ASP   A 157 ? 0.2640 0.2517 0.4544 0.0581  -0.0407 0.1304  157 ASP   A OD2 
3295 O OD2 B ASP   A 157 ? 0.2642 0.2884 0.3365 0.0164  0.0062  0.0501  157 ASP   A OD2 
3304 N N   A LYS   A 158 ? 0.1949 0.2709 0.3629 0.0457  0.0008  0.1034  158 LYS   A N   
3305 N N   B LYS   A 158 ? 0.2538 0.2622 0.2953 0.0003  -0.0137 0.0095  158 LYS   A N   
3306 C CA  A LYS   A 158 ? 0.1975 0.2975 0.3582 0.0506  0.0169  0.0824  158 LYS   A CA  
3307 C CA  B LYS   A 158 ? 0.2544 0.2678 0.2869 -0.0002 -0.0093 0.0013  158 LYS   A CA  
3308 C C   A LYS   A 158 ? 0.1920 0.3115 0.3409 0.0591  0.0128  0.0865  158 LYS   A C   
3309 C C   B LYS   A 158 ? 0.2365 0.2607 0.2654 -0.0038 -0.0011 0.0105  158 LYS   A C   
3310 O O   A LYS   A 158 ? 0.1778 0.3133 0.3199 0.0567  0.0193  0.0778  158 LYS   A O   
3311 O O   B LYS   A 158 ? 0.2266 0.2537 0.2515 -0.0131 -0.0044 0.0169  158 LYS   A O   
3312 C CB  A LYS   A 158 ? 0.2099 0.3092 0.3724 0.0467  0.0386  0.0669  158 LYS   A CB  
3313 C CB  B LYS   A 158 ? 0.2722 0.2822 0.3005 0.0055  -0.0161 -0.0130 158 LYS   A CB  
3314 C CG  A LYS   A 158 ? 0.2307 0.3250 0.3974 0.0417  0.0584  0.0579  158 LYS   A CG  
3315 C CG  B LYS   A 158 ? 0.2851 0.2938 0.3163 0.0115  -0.0253 -0.0248 158 LYS   A CG  
3316 C CD  A LYS   A 158 ? 0.2455 0.3379 0.4134 0.0362  0.0866  0.0614  158 LYS   A CD  
3317 C CD  B LYS   A 158 ? 0.2950 0.3035 0.3295 0.0165  -0.0317 -0.0332 158 LYS   A CD  
3318 C CE  A LYS   A 158 ? 0.2532 0.3448 0.4227 0.0301  0.1098  0.0716  158 LYS   A CE  
3319 C CE  B LYS   A 158 ? 0.3002 0.3085 0.3408 0.0178  -0.0341 -0.0376 158 LYS   A CE  
3320 N NZ  A LYS   A 158 ? 0.2558 0.3478 0.4249 0.0224  0.1251  0.0811  158 LYS   A NZ  
3321 N NZ  B LYS   A 158 ? 0.3020 0.3103 0.3478 0.0203  -0.0358 -0.0381 158 LYS   A NZ  
3348 N N   A ASN   A 159 ? 0.1964 0.3181 0.3552 0.0703  0.0003  0.0987  159 ASN   A N   
3349 N N   B ASN   A 159 ? 0.2354 0.2670 0.2739 0.0061  0.0097  0.0163  159 ASN   A N   
3350 C CA  A ASN   A 159 ? 0.2064 0.3258 0.3646 0.0711  -0.0040 0.1112  159 ASN   A CA  
3351 C CA  B ASN   A 159 ? 0.2370 0.2737 0.2927 0.0145  0.0190  0.0292  159 ASN   A CA  
3352 C C   A ASN   A 159 ? 0.1939 0.3269 0.3322 0.0657  -0.0007 0.1044  159 ASN   A C   
3353 C C   B ASN   A 159 ? 0.2152 0.2671 0.2688 0.0070  0.0087  0.0273  159 ASN   A C   
3354 O O   A ASN   A 159 ? 0.1812 0.3401 0.3029 0.0665  -0.0111 0.0937  159 ASN   A O   
3355 O O   B ASN   A 159 ? 0.2182 0.2815 0.2638 0.0026  -0.0041 0.0196  159 ASN   A O   
3356 C CB  A ASN   A 159 ? 0.2251 0.3336 0.4199 0.0746  0.0017  0.1224  159 ASN   A CB  
3357 C CB  B ASN   A 159 ? 0.2578 0.2857 0.3395 0.0258  0.0399  0.0429  159 ASN   A CB  
3358 C CG  A ASN   A 159 ? 0.2495 0.3452 0.4829 0.0648  0.0168  0.1182  159 ASN   A CG  
3359 C CG  B ASN   A 159 ? 0.2758 0.2975 0.3889 0.0276  0.0582  0.0501  159 ASN   A CG  
3360 O OD1 A ASN   A 159 ? 0.2570 0.3499 0.5014 0.0543  0.0317  0.1190  159 ASN   A OD1 
3361 O OD1 B ASN   A 159 ? 0.2863 0.3059 0.4081 0.0247  0.0662  0.0508  159 ASN   A OD1 
3362 N ND2 A ASN   A 159 ? 0.2560 0.3506 0.5091 0.0602  0.0225  0.1082  159 ASN   A ND2 
3363 N ND2 B ASN   A 159 ? 0.2821 0.3026 0.4112 0.0312  0.0603  0.0544  159 ASN   A ND2 
3376 N N   A LEU   A 160 ? 0.1888 0.3098 0.3313 0.0606  -0.0086 0.1077  160 LEU   A N   
3377 N N   B LEU   A 160 ? 0.1922 0.2503 0.2657 0.0024  0.0063  0.0394  160 LEU   A N   
3378 C CA  A LEU   A 160 ? 0.1893 0.2979 0.3291 0.0452  0.0101  0.1153  160 LEU   A CA  
3379 C CA  B LEU   A 160 ? 0.1777 0.2363 0.2601 0.0004  0.0116  0.0508  160 LEU   A CA  
3380 C C   A LEU   A 160 ? 0.1637 0.3004 0.3327 0.0283  0.0277  0.1244  160 LEU   A C   
3381 C C   B LEU   A 160 ? 0.1673 0.2374 0.2634 -0.0008 0.0157  0.0571  160 LEU   A C   
3382 O O   A LEU   A 160 ? 0.1574 0.3096 0.3596 0.0257  0.0268  0.1232  160 LEU   A O   
3383 O O   B LEU   A 160 ? 0.1684 0.2349 0.2830 -0.0093 0.0063  0.0487  160 LEU   A O   
3384 C CB  A LEU   A 160 ? 0.2096 0.2894 0.3163 0.0368  0.0220  0.1030  160 LEU   A CB  
3385 C CB  B LEU   A 160 ? 0.1797 0.2253 0.2511 -0.0020 0.0132  0.0547  160 LEU   A CB  
3386 C CG  A LEU   A 160 ? 0.2205 0.2836 0.3112 0.0289  0.0323  0.0770  160 LEU   A CG  
3387 C CG  B LEU   A 160 ? 0.1795 0.2218 0.2519 -0.0031 0.0119  0.0577  160 LEU   A CG  
3388 C CD1 A LEU   A 160 ? 0.2312 0.2811 0.3127 0.0264  0.0342  0.0612  160 LEU   A CD1 
3389 C CD1 B LEU   A 160 ? 0.1810 0.2239 0.2595 -0.0011 0.0202  0.0574  160 LEU   A CD1 
3390 C CD2 A LEU   A 160 ? 0.2211 0.2816 0.3053 0.0285  0.0495  0.0617  160 LEU   A CD2 
3391 C CD2 B LEU   A 160 ? 0.1843 0.2174 0.2527 -0.0088 0.0100  0.0576  160 LEU   A CD2 
3414 N N   A TYR   A 161 ? 0.1562 0.2915 0.3264 0.0201  0.0290  0.1308  161 TYR   A N   
3415 N N   B TYR   A 161 ? 0.1651 0.2484 0.2565 0.0063  0.0280  0.0739  161 TYR   A N   
3416 C CA  A TYR   A 161 ? 0.1515 0.2843 0.3300 0.0129  0.0306  0.1270  161 TYR   A CA  
3417 C CA  B TYR   A 161 ? 0.1744 0.2581 0.2628 0.0087  0.0285  0.0877  161 TYR   A CA  
3418 C C   A TYR   A 161 ? 0.1384 0.3057 0.3560 0.0093  0.0267  0.1167  161 TYR   A C   
3419 C C   B TYR   A 161 ? 0.1806 0.2787 0.2798 0.0096  0.0260  0.0851  161 TYR   A C   
3420 O O   A TYR   A 161 ? 0.1274 0.3128 0.3593 0.0032  0.0240  0.1125  161 TYR   A O   
3421 O O   B TYR   A 161 ? 0.1772 0.2824 0.2770 0.0064  0.0292  0.0837  161 TYR   A O   
3422 C CB  A TYR   A 161 ? 0.1589 0.2679 0.3339 0.0078  0.0333  0.1160  161 TYR   A CB  
3423 C CB  B TYR   A 161 ? 0.1760 0.2514 0.2608 0.0118  0.0320  0.0895  161 TYR   A CB  
3424 C CG  A TYR   A 161 ? 0.1615 0.2569 0.3287 0.0076  0.0260  0.0954  161 TYR   A CG  
3425 C CG  B TYR   A 161 ? 0.1743 0.2477 0.2623 0.0158  0.0319  0.0816  161 TYR   A CG  
3426 C CD1 A TYR   A 161 ? 0.1608 0.2488 0.3295 0.0076  0.0281  0.0853  161 TYR   A CD1 
3427 C CD1 B TYR   A 161 ? 0.1769 0.2496 0.2670 0.0162  0.0279  0.0803  161 TYR   A CD1 
3428 C CD2 A TYR   A 161 ? 0.1657 0.2600 0.3297 0.0086  0.0136  0.0818  161 TYR   A CD2 
3429 C CD2 B TYR   A 161 ? 0.1730 0.2432 0.2650 0.0192  0.0298  0.0731  161 TYR   A CD2 
3430 C CE1 A TYR   A 161 ? 0.1737 0.2367 0.3261 0.0043  0.0223  0.0884  161 TYR   A CE1 
3431 C CE1 B TYR   A 161 ? 0.1798 0.2478 0.2730 0.0142  0.0274  0.0809  161 TYR   A CE1 
3432 C CE2 A TYR   A 161 ? 0.1743 0.2504 0.3336 0.0041  0.0155  0.0832  161 TYR   A CE2 
3433 C CE2 B TYR   A 161 ? 0.1783 0.2466 0.2698 0.0194  0.0251  0.0723  161 TYR   A CE2 
3434 C CZ  A TYR   A 161 ? 0.1888 0.2377 0.3342 -0.0006 0.0111  0.0913  161 TYR   A CZ  
3435 C CZ  B TYR   A 161 ? 0.1893 0.2483 0.2780 0.0146  0.0244  0.0773  161 TYR   A CZ  
3436 O OH  A TYR   A 161 ? 0.2077 0.2228 0.3462 -0.0081 0.0027  0.1077  161 TYR   A OH  
3437 O OH  B TYR   A 161 ? 0.2038 0.2511 0.2985 0.0101  0.0227  0.0773  161 TYR   A OH  
3456 N N   A ASP   A 162 ? 0.1322 0.3176 0.3732 0.0097  0.0297  0.1176  162 ASP   A N   
3457 N N   B ASP   A 162 ? 0.1867 0.2932 0.2977 0.0143  0.0247  0.0882  162 ASP   A N   
3458 C CA  A ASP   A 162 ? 0.1311 0.3337 0.3750 0.0018  0.0288  0.1145  162 ASP   A CA  
3459 C CA  B ASP   A 162 ? 0.1918 0.3090 0.3087 0.0156  0.0222  0.0857  162 ASP   A CA  
3460 C C   A ASP   A 162 ? 0.1334 0.3481 0.3790 -0.0016 0.0240  0.1129  162 ASP   A C   
3461 C C   B ASP   A 162 ? 0.2000 0.3261 0.3163 0.0111  0.0166  0.0796  162 ASP   A C   
3462 O O   A ASP   A 162 ? 0.1276 0.3497 0.3994 -0.0043 0.0243  0.1104  162 ASP   A O   
3463 O O   B ASP   A 162 ? 0.2022 0.3279 0.3239 0.0116  0.0171  0.0746  162 ASP   A O   
3464 C CB  A ASP   A 162 ? 0.1463 0.3355 0.3846 0.0011  0.0317  0.1150  162 ASP   A CB  
3465 C CB  B ASP   A 162 ? 0.1905 0.3076 0.3222 0.0200  0.0229  0.0909  162 ASP   A CB  
3466 C CG  A ASP   A 162 ? 0.1648 0.3398 0.3925 0.0062  0.0371  0.1132  162 ASP   A CG  
3467 C CG  B ASP   A 162 ? 0.1897 0.3072 0.3276 0.0207  0.0235  0.1033  162 ASP   A CG  
3468 O OD1 A ASP   A 162 ? 0.1756 0.3448 0.3966 0.0065  0.0435  0.1117  162 ASP   A OD1 
3469 O OD1 B ASP   A 162 ? 0.1898 0.3044 0.3330 0.0219  0.0250  0.1097  162 ASP   A OD1 
3470 O OD2 A ASP   A 162 ? 0.1779 0.3394 0.4022 0.0110  0.0524  0.1104  162 ASP   A OD2 
3471 O OD2 B ASP   A 162 ? 0.1907 0.3099 0.3245 0.0262  0.0220  0.1091  162 ASP   A OD2 
3480 N N   A LYS   A 163 ? 0.1536 0.3637 0.3731 0.0026  -0.0022 0.1072  163 LYS   A N   
3481 N N   B LYS   A 163 ? 0.2074 0.3424 0.3262 0.0078  0.0033  0.0762  163 LYS   A N   
3482 C CA  A LYS   A 163 ? 0.1694 0.3756 0.3565 0.0011  -0.0043 0.0980  163 LYS   A CA  
3483 C CA  B LYS   A 163 ? 0.2110 0.3560 0.3300 0.0028  -0.0006 0.0728  163 LYS   A CA  
3484 C C   A LYS   A 163 ? 0.1623 0.3701 0.3407 -0.0025 0.0089  0.0941  163 LYS   A C   
3485 C C   B LYS   A 163 ? 0.1881 0.3568 0.3216 -0.0019 0.0052  0.0776  163 LYS   A C   
3486 O O   A LYS   A 163 ? 0.1556 0.3839 0.3502 -0.0096 0.0160  0.0907  163 LYS   A O   
3487 O O   B LYS   A 163 ? 0.1934 0.3647 0.3215 -0.0024 0.0052  0.0699  163 LYS   A O   
3488 C CB  A LYS   A 163 ? 0.2132 0.3952 0.3901 0.0081  -0.0144 0.0874  163 LYS   A CB  
3489 C CB  B LYS   A 163 ? 0.2433 0.3694 0.3624 0.0044  -0.0082 0.0630  163 LYS   A CB  
3490 C CG  A LYS   A 163 ? 0.2549 0.4122 0.4294 0.0091  -0.0086 0.0772  163 LYS   A CG  
3491 C CG  B LYS   A 163 ? 0.2731 0.3813 0.3990 0.0027  -0.0097 0.0554  163 LYS   A CG  
3492 C CD  A LYS   A 163 ? 0.2935 0.4265 0.4727 0.0106  -0.0093 0.0685  163 LYS   A CD  
3493 C CD  B LYS   A 163 ? 0.3000 0.3914 0.4396 0.0009  -0.0102 0.0494  163 LYS   A CD  
3494 C CE  A LYS   A 163 ? 0.3290 0.4365 0.5083 0.0097  -0.0063 0.0623  163 LYS   A CE  
3495 C CE  B LYS   A 163 ? 0.3197 0.3985 0.4700 -0.0009 -0.0081 0.0460  163 LYS   A CE  
3496 N NZ  A LYS   A 163 ? 0.3398 0.4424 0.5311 0.0071  -0.0045 0.0607  163 LYS   A NZ  
3497 N NZ  B LYS   A 163 ? 0.3303 0.4025 0.4886 -0.0020 -0.0080 0.0444  163 LYS   A NZ  
3524 N N   . LEU   A 164 ? 0.1569 0.3482 0.3235 -0.0098 0.0071  0.0894  164 LEU   A N   
3525 C CA  . LEU   A 164 ? 0.1555 0.3251 0.3256 -0.0165 0.0266  0.0877  164 LEU   A CA  
3526 C C   . LEU   A 164 ? 0.1632 0.3264 0.3405 -0.0185 0.0309  0.0871  164 LEU   A C   
3527 O O   . LEU   A 164 ? 0.1672 0.3336 0.3489 -0.0225 0.0392  0.0700  164 LEU   A O   
3528 C CB  . LEU   A 164 ? 0.1574 0.3092 0.3222 -0.0254 0.0348  0.0897  164 LEU   A CB  
3529 C CG  . LEU   A 164 ? 0.1665 0.3027 0.3255 -0.0178 0.0250  0.0825  164 LEU   A CG  
3530 C CD1 . LEU   A 164 ? 0.1653 0.3013 0.3285 -0.0145 0.0102  0.0754  164 LEU   A CD1 
3531 C CD2 . LEU   A 164 ? 0.1823 0.3004 0.3181 -0.0157 0.0297  0.0777  164 LEU   A CD2 
3544 N N   . VAL   A 165 ? 0.1548 0.3247 0.3371 -0.0180 0.0250  0.0915  165 VAL   A N   
3545 C CA  . VAL   A 165 ? 0.1714 0.3341 0.3282 -0.0241 0.0356  0.0956  165 VAL   A CA  
3546 C C   . VAL   A 165 ? 0.1663 0.3543 0.3369 -0.0248 0.0287  0.0830  165 VAL   A C   
3547 O O   . VAL   A 165 ? 0.1670 0.3574 0.3447 -0.0193 0.0295  0.0833  165 VAL   A O   
3548 C CB  . VAL   A 165 ? 0.1948 0.3357 0.3321 -0.0199 0.0412  0.0945  165 VAL   A CB  
3549 C CG1 . VAL   A 165 ? 0.2025 0.3423 0.3404 -0.0260 0.0458  0.0933  165 VAL   A CG1 
3550 C CG2 . VAL   A 165 ? 0.2068 0.3363 0.3368 -0.0094 0.0376  0.0956  165 VAL   A CG2 
3560 N N   A SER   A 166 ? 0.1562 0.3653 0.3496 -0.0249 0.0304  0.0703  166 SER   A N   
3561 N N   B SER   A 166 ? 0.1707 0.3644 0.3376 -0.0235 0.0253  0.0701  166 SER   A N   
3562 C CA  A SER   A 166 ? 0.1668 0.3845 0.3719 -0.0256 0.0161  0.0544  166 SER   A CA  
3563 C CA  B SER   A 166 ? 0.1844 0.3796 0.3476 -0.0231 0.0147  0.0558  166 SER   A CA  
3564 C C   A SER   A 166 ? 0.1742 0.3977 0.3748 -0.0340 0.0073  0.0469  166 SER   A C   
3565 C C   B SER   A 166 ? 0.1852 0.3924 0.3518 -0.0275 0.0065  0.0498  166 SER   A C   
3566 O O   A SER   A 166 ? 0.1885 0.4087 0.4086 -0.0388 0.0127  0.0317  166 SER   A O   
3567 O O   B SER   A 166 ? 0.1937 0.3969 0.3637 -0.0299 0.0085  0.0422  166 SER   A O   
3568 C CB  A SER   A 166 ? 0.1871 0.3949 0.3996 -0.0115 0.0094  0.0372  166 SER   A CB  
3569 C CB  B SER   A 166 ? 0.2025 0.3849 0.3613 -0.0154 0.0110  0.0436  166 SER   A CB  
3570 O OG  A SER   A 166 ? 0.2288 0.4058 0.4314 -0.0113 0.0078  0.0356  166 SER   A OG  
3571 O OG  B SER   A 166 ? 0.2276 0.3908 0.3799 -0.0145 0.0093  0.0409  166 SER   A OG  
3582 N N   . SER   A 167 ? 0.1843 0.4034 0.3534 -0.0241 -0.0026 0.0486  167 SER   A N   
3583 C CA  . SER   A 167 ? 0.2188 0.4168 0.3517 -0.0141 -0.0205 0.0402  167 SER   A CA  
3584 C C   . SER   A 167 ? 0.2429 0.4271 0.3615 -0.0095 -0.0231 0.0372  167 SER   A C   
3585 O O   . SER   A 167 ? 0.2484 0.4225 0.3572 -0.0029 -0.0341 0.0336  167 SER   A O   
3586 C CB  . SER   A 167 ? 0.2250 0.4232 0.3529 -0.0079 -0.0127 0.0401  167 SER   A CB  
3587 O OG  . SER   A 167 ? 0.2284 0.4271 0.3537 -0.0050 0.0001  0.0441  167 SER   A OG  
3594 N N   . PHE   A 168 ? 0.2611 0.4433 0.3795 -0.0060 -0.0290 0.0411  168 PHE   A N   
3595 C CA  . PHE   A 168 ? 0.2978 0.4637 0.4280 -0.0136 -0.0329 0.0341  168 PHE   A CA  
3596 C C   . PHE   A 168 ? 0.3945 0.5180 0.5437 -0.0260 -0.0392 0.0106  168 PHE   A C   
3597 O O   . PHE   A 168 ? 0.3985 0.5210 0.5712 -0.0306 -0.0308 0.0109  168 PHE   A O   
3598 C CB  . PHE   A 168 ? 0.2513 0.4358 0.3772 -0.0159 -0.0259 0.0549  168 PHE   A CB  
3599 C CG  . PHE   A 168 ? 0.2145 0.4123 0.3330 -0.0245 -0.0214 0.0744  168 PHE   A CG  
3600 C CD1 . PHE   A 168 ? 0.2044 0.4067 0.3230 -0.0287 -0.0219 0.0900  168 PHE   A CD1 
3601 C CD2 . PHE   A 168 ? 0.1974 0.3999 0.3098 -0.0288 -0.0037 0.0812  168 PHE   A CD2 
3602 C CE1 . PHE   A 168 ? 0.1915 0.3985 0.3089 -0.0335 -0.0192 0.1057  168 PHE   A CE1 
3603 C CE2 . PHE   A 168 ? 0.1940 0.3937 0.3090 -0.0321 0.0010  0.0935  168 PHE   A CE2 
3604 C CZ  . PHE   A 168 ? 0.1908 0.3936 0.3057 -0.0354 -0.0083 0.1031  168 PHE   A CZ  
3614 N N   . LEU   A 169 ? 0.4834 0.5671 0.6200 -0.0335 -0.0494 -0.0150 169 LEU   A N   
3615 C CA  . LEU   A 169 ? 0.5695 0.6158 0.6982 -0.0386 -0.0562 -0.0339 169 LEU   A CA  
3616 C C   . LEU   A 169 ? 0.6000 0.6310 0.7204 -0.0414 -0.0607 -0.0333 169 LEU   A C   
3617 O O   . LEU   A 169 ? 0.6094 0.6375 0.7202 -0.0425 -0.0618 -0.0337 169 LEU   A O   
3618 C CB  . LEU   A 169 ? 0.6150 0.6442 0.7314 -0.0412 -0.0575 -0.0526 169 LEU   A CB  
3619 C CG  . LEU   A 169 ? 0.6506 0.6669 0.7620 -0.0436 -0.0591 -0.0687 169 LEU   A CG  
3620 C CD1 . LEU   A 169 ? 0.6603 0.6748 0.7740 -0.0444 -0.0602 -0.0738 169 LEU   A CD1 
3621 C CD2 . LEU   A 169 ? 0.6605 0.6744 0.7690 -0.0442 -0.0591 -0.0742 169 LEU   A CD2 
3622 O OXT . LEU   A 169 ? 0.6052 0.6345 0.7248 -0.0433 -0.0604 -0.0332 169 LEU   A OXT 
3634 N N   A SER   B 1   ? 0.3929 0.3623 0.3686 -0.1065 -0.0896 0.0324  1   SER   B N   
3635 N N   B SER   B 1   ? 0.3610 0.3515 0.3567 -0.0866 -0.0565 0.0265  1   SER   B N   
3636 C CA  A SER   B 1   ? 0.3844 0.3645 0.3705 -0.1114 -0.0905 0.0324  1   SER   B CA  
3637 C CA  B SER   B 1   ? 0.3551 0.3529 0.3585 -0.0895 -0.0563 0.0284  1   SER   B CA  
3638 C C   A SER   B 1   ? 0.3556 0.3630 0.3494 -0.1165 -0.0916 0.0521  1   SER   B C   
3639 C C   B SER   B 1   ? 0.3363 0.3509 0.3441 -0.0925 -0.0607 0.0464  1   SER   B C   
3640 O O   A SER   B 1   ? 0.3626 0.3614 0.3271 -0.1143 -0.0899 0.0490  1   SER   B O   
3641 O O   B SER   B 1   ? 0.3416 0.3507 0.3339 -0.0905 -0.0583 0.0419  1   SER   B O   
3642 C CB  A SER   B 1   ? 0.4008 0.3652 0.3843 -0.1081 -0.0846 0.0173  1   SER   B CB  
3643 C CB  B SER   B 1   ? 0.3648 0.3542 0.3672 -0.0875 -0.0484 0.0156  1   SER   B CB  
3644 O OG  A SER   B 1   ? 0.4163 0.3742 0.4264 -0.1024 -0.0762 0.0117  1   SER   B OG  
3645 O OG  B SER   B 1   ? 0.3728 0.3594 0.3915 -0.0857 -0.0443 0.0092  1   SER   B OG  
3660 N N   A MET   B 2   ? 0.3257 0.3620 0.3473 -0.1194 -0.0843 0.0888  2   MET   B N   
3661 N N   B MET   B 2   ? 0.3144 0.3483 0.3368 -0.0954 -0.0624 0.0787  2   MET   B N   
3662 C CA  A MET   B 2   ? 0.3058 0.3669 0.3607 -0.1024 -0.0818 0.1098  2   MET   B CA  
3663 C CA  B MET   B 2   ? 0.2959 0.3482 0.3361 -0.0884 -0.0680 0.1037  2   MET   B CA  
3664 C C   A MET   B 2   ? 0.2680 0.3498 0.3196 -0.0836 -0.0998 0.1347  2   MET   B C   
3665 C C   B MET   B 2   ? 0.2665 0.3347 0.3106 -0.0860 -0.0823 0.1274  2   MET   B C   
3666 O O   A MET   B 2   ? 0.2609 0.3632 0.3159 -0.0665 -0.1171 0.1386  2   MET   B O   
3667 O O   B MET   B 2   ? 0.2648 0.3389 0.3044 -0.0825 -0.0860 0.1285  2   MET   B O   
3668 C CB  A MET   B 2   ? 0.3373 0.4005 0.4466 -0.0811 -0.0585 0.0829  2   MET   B CB  
3669 C CB  B MET   B 2   ? 0.3134 0.3682 0.3789 -0.0709 -0.0591 0.0925  2   MET   B CB  
3670 C CG  A MET   B 2   ? 0.3672 0.4295 0.5234 -0.0593 -0.0361 0.0656  2   MET   B CG  
3671 C CG  B MET   B 2   ? 0.3291 0.3850 0.4115 -0.0531 -0.0516 0.0916  2   MET   B CG  
3672 S SD  A MET   B 2   ? 0.3942 0.4565 0.5993 -0.0402 -0.0205 0.0520  2   MET   B SD  
3673 S SD  B MET   B 2   ? 0.3431 0.4019 0.4392 -0.0369 -0.0504 0.0923  2   MET   B SD  
3674 C CE  A MET   B 2   ? 0.3990 0.4620 0.6034 -0.0379 -0.0136 0.0504  2   MET   B CE  
3675 C CE  B MET   B 2   ? 0.3461 0.4055 0.4482 -0.0355 -0.0459 0.0843  2   MET   B CE  
3694 N N   . VAL   B 3   ? 0.2381 0.3127 0.3045 -0.0935 -0.0846 0.1481  3   VAL   B N   
3695 C CA  . VAL   B 3   ? 0.2232 0.2718 0.3087 -0.0805 -0.0774 0.1331  3   VAL   B CA  
3696 C C   . VAL   B 3   ? 0.2006 0.2596 0.2677 -0.0694 -0.0730 0.1170  3   VAL   B C   
3697 O O   . VAL   B 3   ? 0.2076 0.2763 0.2698 -0.0682 -0.0759 0.1281  3   VAL   B O   
3698 C CB  . VAL   B 3   ? 0.2410 0.2574 0.3602 -0.0744 -0.0726 0.1148  3   VAL   B CB  
3699 C CG1 . VAL   B 3   ? 0.2551 0.2467 0.3831 -0.0747 -0.0746 0.1102  3   VAL   B CG1 
3700 C CG2 . VAL   B 3   ? 0.2447 0.2648 0.3773 -0.0665 -0.0585 0.1218  3   VAL   B CG2 
3711 N N   . ASN   B 4   ? 0.1877 0.2300 0.2347 -0.0634 -0.0614 0.0945  4   ASN   B N   
3712 C CA  . ASN   B 4   ? 0.1903 0.2303 0.1915 -0.0630 -0.0553 0.0582  4   ASN   B CA  
3713 C C   . ASN   B 4   ? 0.1968 0.2470 0.1808 -0.0642 -0.0436 0.0428  4   ASN   B C   
3714 O O   . ASN   B 4   ? 0.1983 0.2507 0.2040 -0.0645 -0.0364 0.0194  4   ASN   B O   
3715 C CB  . ASN   B 4   ? 0.1911 0.2234 0.1779 -0.0570 -0.0625 0.0459  4   ASN   B CB  
3716 C CG  . ASN   B 4   ? 0.1911 0.1979 0.1711 -0.0528 -0.0523 0.0410  4   ASN   B CG  
3717 O OD1 . ASN   B 4   ? 0.1950 0.1787 0.1751 -0.0512 -0.0548 0.0357  4   ASN   B OD1 
3718 N ND2 . ASN   B 4   ? 0.2140 0.2034 0.1800 -0.0293 -0.0336 0.0289  4   ASN   B ND2 
3725 N N   . SER   B 5   ? 0.2057 0.2657 0.1948 -0.0592 -0.0348 0.0346  5   SER   B N   
3726 C CA  . SER   B 5   ? 0.2250 0.2931 0.2107 -0.0481 -0.0129 0.0397  5   SER   B CA  
3727 C C   . SER   B 5   ? 0.2503 0.2933 0.2517 -0.0671 0.0220  0.0348  5   SER   B C   
3728 O O   . SER   B 5   ? 0.2698 0.2835 0.3336 -0.0606 0.0590  0.0283  5   SER   B O   
3729 C CB  . SER   B 5   ? 0.2311 0.3088 0.2380 -0.0359 -0.0053 0.0429  5   SER   B CB  
3730 O OG  . SER   B 5   ? 0.2624 0.3306 0.3040 -0.0201 -0.0083 0.0449  5   SER   B OG  
3736 N N   . PHE   B 6   ? 0.2732 0.3150 0.2274 -0.0738 0.0355  0.0364  6   PHE   B N   
3737 C CA  . PHE   B 6   ? 0.2891 0.3210 0.1943 -0.0948 0.0378  0.0213  6   PHE   B CA  
3738 C C   . PHE   B 6   ? 0.3413 0.3523 0.2279 -0.1065 0.0639  -0.0020 6   PHE   B C   
3739 O O   . PHE   B 6   ? 0.3542 0.3827 0.2690 -0.1012 0.0449  -0.0160 6   PHE   B O   
3740 C CB  . PHE   B 6   ? 0.2615 0.2980 0.1799 -0.0882 0.0101  0.0166  6   PHE   B CB  
3741 C CG  . PHE   B 6   ? 0.2286 0.2678 0.1795 -0.0863 -0.0030 0.0163  6   PHE   B CG  
3742 C CD1 . PHE   B 6   ? 0.2266 0.2372 0.1640 -0.0807 -0.0117 0.0185  6   PHE   B CD1 
3743 C CD2 . PHE   B 6   ? 0.2040 0.2634 0.1820 -0.0749 -0.0015 0.0413  6   PHE   B CD2 
3744 C CE1 . PHE   B 6   ? 0.2227 0.2157 0.1738 -0.0663 -0.0177 0.0184  6   PHE   B CE1 
3745 C CE2 . PHE   B 6   ? 0.2067 0.2506 0.2149 -0.0613 -0.0008 0.0350  6   PHE   B CE2 
3746 C CZ  . PHE   B 6   ? 0.2095 0.2229 0.1886 -0.0622 -0.0068 0.0185  6   PHE   B CZ  
3756 N N   . SER   B 7   ? 0.3802 0.3383 0.2510 -0.1277 0.0986  -0.0317 7   SER   B N   
3757 C CA  . SER   B 7   ? 0.4158 0.3539 0.3121 -0.1243 0.1214  -0.0493 7   SER   B CA  
3758 C C   . SER   B 7   ? 0.4117 0.3364 0.2994 -0.1283 0.1360  -0.0651 7   SER   B C   
3759 O O   . SER   B 7   ? 0.4202 0.3377 0.3288 -0.1285 0.1349  -0.0627 7   SER   B O   
3760 C CB  . SER   B 7   ? 0.4405 0.3778 0.3872 -0.1201 0.1359  -0.0465 7   SER   B CB  
3761 O OG  . SER   B 7   ? 0.4559 0.3850 0.4488 -0.1189 0.1376  -0.0390 7   SER   B OG  
3767 N N   . GLY   B 8   ? 0.4076 0.3264 0.3077 -0.1153 0.1379  -0.0735 8   GLY   B N   
3768 C CA  . GLY   B 8   ? 0.3902 0.3099 0.3088 -0.1055 0.1416  -0.0745 8   GLY   B CA  
3769 C C   . GLY   B 8   ? 0.3654 0.2816 0.2990 -0.1028 0.1407  -0.0666 8   GLY   B C   
3770 O O   . GLY   B 8   ? 0.3776 0.2910 0.3344 -0.0876 0.1414  -0.0765 8   GLY   B O   
3774 N N   . TYR   B 9   ? 0.3432 0.2544 0.2676 -0.0925 0.1096  -0.0791 9   TYR   B N   
3775 C CA  . TYR   B 9   ? 0.3205 0.2315 0.2402 -0.0751 0.0811  -0.0578 9   TYR   B CA  
3776 C C   . TYR   B 9   ? 0.3183 0.2304 0.2337 -0.0734 0.0419  -0.0457 9   TYR   B C   
3777 O O   . TYR   B 9   ? 0.3317 0.2486 0.2794 -0.0804 0.0435  -0.0324 9   TYR   B O   
3778 C CB  . TYR   B 9   ? 0.3078 0.2091 0.2419 -0.0638 0.0739  -0.0558 9   TYR   B CB  
3779 C CG  . TYR   B 9   ? 0.2964 0.1906 0.2405 -0.0687 0.0636  -0.0589 9   TYR   B CG  
3780 C CD1 . TYR   B 9   ? 0.2991 0.1916 0.2576 -0.0838 0.0664  -0.0498 9   TYR   B CD1 
3781 C CD2 . TYR   B 9   ? 0.2841 0.1830 0.2271 -0.0634 0.0541  -0.0621 9   TYR   B CD2 
3782 C CE1 . TYR   B 9   ? 0.2943 0.2011 0.2594 -0.0898 0.0692  -0.0649 9   TYR   B CE1 
3783 C CE2 . TYR   B 9   ? 0.2874 0.1824 0.2416 -0.0651 0.0553  -0.0511 9   TYR   B CE2 
3784 C CZ  . TYR   B 9   ? 0.2892 0.1985 0.2590 -0.0836 0.0619  -0.0676 9   TYR   B CZ  
3785 O OH  . TYR   B 9   ? 0.2857 0.2145 0.2802 -0.0909 0.0697  -0.0808 9   TYR   B OH  
3795 N N   . LEU   B 10  ? 0.2997 0.2056 0.2068 -0.0721 0.0188  -0.0406 10  LEU   B N   
3796 C CA  . LEU   B 10  ? 0.3027 0.1985 0.2058 -0.0833 -0.0128 -0.0355 10  LEU   B CA  
3797 C C   . LEU   B 10  ? 0.2865 0.1934 0.2102 -0.0797 -0.0276 -0.0279 10  LEU   B C   
3798 O O   . LEU   B 10  ? 0.2725 0.1956 0.2141 -0.0681 -0.0174 -0.0208 10  LEU   B O   
3799 C CB  . LEU   B 10  ? 0.3283 0.1931 0.2230 -0.0880 -0.0334 -0.0185 10  LEU   B CB  
3800 C CG  . LEU   B 10  ? 0.3525 0.2019 0.2596 -0.0814 -0.0619 -0.0061 10  LEU   B CG  
3801 C CD1 . LEU   B 10  ? 0.3691 0.2123 0.2838 -0.0750 -0.0573 -0.0088 10  LEU   B CD1 
3802 C CD2 . LEU   B 10  ? 0.3620 0.2111 0.2845 -0.0764 -0.0557 0.0186  10  LEU   B CD2 
3814 N N   . LYS   B 11  ? 0.2985 0.2196 0.2101 -0.0733 -0.0402 -0.0246 11  LYS   B N   
3815 C CA  . LYS   B 11  ? 0.3205 0.2468 0.2456 -0.0578 -0.0446 -0.0270 11  LYS   B CA  
3816 C C   . LYS   B 11  ? 0.2980 0.2237 0.2549 -0.0761 -0.0349 -0.0382 11  LYS   B C   
3817 O O   . LYS   B 11  ? 0.3142 0.2439 0.2886 -0.0906 -0.0367 -0.0711 11  LYS   B O   
3818 C CB  . LYS   B 11  ? 0.3625 0.3007 0.3170 -0.0337 -0.0526 -0.0288 11  LYS   B CB  
3819 C CG  . LYS   B 11  ? 0.3988 0.3367 0.4027 -0.0184 -0.0529 -0.0303 11  LYS   B CG  
3820 C CD  . LYS   B 11  ? 0.4262 0.3609 0.4744 -0.0081 -0.0507 -0.0334 11  LYS   B CD  
3821 C CE  . LYS   B 11  ? 0.4460 0.3782 0.5250 -0.0042 -0.0498 -0.0353 11  LYS   B CE  
3822 N NZ  . LYS   B 11  ? 0.4569 0.3887 0.5515 -0.0029 -0.0495 -0.0359 11  LYS   B NZ  
3836 N N   . LEU   B 12  ? 0.2579 0.2006 0.2496 -0.0683 -0.0328 -0.0434 12  LEU   B N   
3837 C CA  . LEU   B 12  ? 0.2383 0.1836 0.2667 -0.0577 -0.0178 -0.0413 12  LEU   B CA  
3838 C C   . LEU   B 12  ? 0.2198 0.1841 0.2788 -0.0571 -0.0351 -0.0329 12  LEU   B C   
3839 O O   . LEU   B 12  ? 0.2180 0.1879 0.2936 -0.0633 -0.0520 -0.0267 12  LEU   B O   
3840 C CB  . LEU   B 12  ? 0.2358 0.1628 0.2645 -0.0434 -0.0118 -0.0424 12  LEU   B CB  
3841 C CG  . LEU   B 12  ? 0.2346 0.1601 0.2763 -0.0415 -0.0094 -0.0297 12  LEU   B CG  
3842 C CD1 . LEU   B 12  ? 0.2479 0.1611 0.2710 -0.0294 -0.0164 -0.0147 12  LEU   B CD1 
3843 C CD2 . LEU   B 12  ? 0.2385 0.1663 0.2915 -0.0421 -0.0002 -0.0348 12  LEU   B CD2 
3855 N N   . THR   B 13  ? 0.2125 0.1883 0.2829 -0.0549 -0.0479 -0.0396 13  THR   B N   
3856 C CA  . THR   B 13  ? 0.2125 0.1994 0.2658 -0.0622 -0.0639 -0.0243 13  THR   B CA  
3857 C C   . THR   B 13  ? 0.2603 0.2232 0.2832 -0.0727 -0.0789 -0.0216 13  THR   B C   
3858 O O   . THR   B 13  ? 0.2785 0.2271 0.2867 -0.0692 -0.0473 -0.0276 13  THR   B O   
3859 C CB  . THR   B 13  ? 0.1962 0.1976 0.2695 -0.0554 -0.0583 -0.0138 13  THR   B CB  
3860 O OG1 . THR   B 13  ? 0.1851 0.1914 0.2725 -0.0504 -0.0424 -0.0164 13  THR   B OG1 
3861 C CG2 . THR   B 13  ? 0.2106 0.2006 0.2881 -0.0463 -0.0443 -0.0031 13  THR   B CG2 
3869 N N   A ASP   B 14  ? 0.2768 0.2370 0.2959 -0.0824 -0.1112 -0.0105 14  ASP   B N   
3870 N N   B ASP   B 14  ? 0.2739 0.2342 0.2965 -0.0751 -0.0905 -0.0091 14  ASP   B N   
3871 C CA  A ASP   B 14  ? 0.2929 0.2524 0.3255 -0.0837 -0.1156 0.0120  14  ASP   B CA  
3872 C CA  B ASP   B 14  ? 0.2865 0.2454 0.3159 -0.0740 -0.0897 0.0075  14  ASP   B CA  
3873 C C   A ASP   B 14  ? 0.2827 0.2329 0.2848 -0.0860 -0.0968 0.0160  14  ASP   B C   
3874 C C   B ASP   B 14  ? 0.2736 0.2275 0.2803 -0.0769 -0.0865 0.0130  14  ASP   B C   
3875 O O   A ASP   B 14  ? 0.3088 0.2474 0.2875 -0.0878 -0.0913 0.0282  14  ASP   B O   
3876 O O   B ASP   B 14  ? 0.2883 0.2337 0.2812 -0.0768 -0.0837 0.0200  14  ASP   B O   
3877 C CB  A ASP   B 14  ? 0.3168 0.2910 0.4085 -0.0794 -0.1287 0.0140  14  ASP   B CB  
3878 C CB  B ASP   B 14  ? 0.3097 0.2756 0.3754 -0.0684 -0.0877 0.0111  14  ASP   B CB  
3879 C CG  A ASP   B 14  ? 0.3426 0.3236 0.4854 -0.0733 -0.1260 0.0037  14  ASP   B CG  
3880 C CG  B ASP   B 14  ? 0.3318 0.3014 0.4291 -0.0618 -0.0810 0.0080  14  ASP   B CG  
3881 O OD1 A ASP   B 14  ? 0.3562 0.3334 0.5032 -0.0744 -0.1274 -0.0083 14  ASP   B OD1 
3882 O OD1 B ASP   B 14  ? 0.3408 0.3109 0.4401 -0.0604 -0.0779 0.0038  14  ASP   B OD1 
3883 O OD2 A ASP   B 14  ? 0.3485 0.3374 0.5217 -0.0715 -0.1177 0.0065  14  ASP   B OD2 
3884 O OD2 B ASP   B 14  ? 0.3388 0.3112 0.4519 -0.0614 -0.0768 0.0094  14  ASP   B OD2 
3893 N N   . ASN   B 15  ? 0.2456 0.2049 0.2540 -0.0703 -0.0875 0.0163  15  ASN   B N   
3894 C CA  . ASN   B 15  ? 0.1985 0.1749 0.2375 -0.0460 -0.0637 0.0017  15  ASN   B CA  
3895 C C   . ASN   B 15  ? 0.1760 0.1599 0.2236 -0.0279 -0.0531 -0.0036 15  ASN   B C   
3896 O O   . ASN   B 15  ? 0.1725 0.1502 0.2430 -0.0277 -0.0512 -0.0150 15  ASN   B O   
3897 C CB  . ASN   B 15  ? 0.1902 0.1660 0.2629 -0.0228 -0.0592 0.0063  15  ASN   B CB  
3898 C CG  . ASN   B 15  ? 0.1738 0.1639 0.2619 -0.0276 -0.0314 0.0105  15  ASN   B CG  
3899 O OD1 . ASN   B 15  ? 0.1729 0.1959 0.2927 -0.0441 -0.0367 0.0189  15  ASN   B OD1 
3900 N ND2 . ASN   B 15  ? 0.1758 0.1424 0.2454 -0.0154 -0.0110 -0.0068 15  ASN   B ND2 
3908 N N   . VAL   B 16  ? 0.1796 0.1509 0.2328 -0.0367 -0.0569 -0.0079 16  VAL   B N   
3909 C CA  . VAL   B 16  ? 0.1791 0.1494 0.2257 -0.0315 -0.0407 -0.0189 16  VAL   B CA  
3910 C C   . VAL   B 16  ? 0.1743 0.1656 0.2150 -0.0429 -0.0443 -0.0164 16  VAL   B C   
3911 O O   . VAL   B 16  ? 0.1797 0.1746 0.2326 -0.0387 -0.0371 -0.0304 16  VAL   B O   
3912 C CB  . VAL   B 16  ? 0.1762 0.1460 0.2312 -0.0184 -0.0304 -0.0208 16  VAL   B CB  
3913 C CG1 . VAL   B 16  ? 0.1822 0.1429 0.2386 0.0001  -0.0227 -0.0168 16  VAL   B CG1 
3914 C CG2 . VAL   B 16  ? 0.1838 0.1544 0.2426 -0.0088 -0.0248 -0.0178 16  VAL   B CG2 
3924 N N   . TYR   B 17  ? 0.1837 0.1717 0.2041 -0.0389 -0.0350 -0.0174 17  TYR   B N   
3925 C CA  . TYR   B 17  ? 0.1913 0.1879 0.2030 -0.0437 -0.0320 -0.0029 17  TYR   B CA  
3926 C C   . TYR   B 17  ? 0.1835 0.1551 0.2018 -0.0417 -0.0198 -0.0160 17  TYR   B C   
3927 O O   . TYR   B 17  ? 0.1789 0.1636 0.2130 -0.0384 -0.0288 -0.0370 17  TYR   B O   
3928 C CB  . TYR   B 17  ? 0.2287 0.2309 0.2235 -0.0313 -0.0285 0.0320  17  TYR   B CB  
3929 C CG  . TYR   B 17  ? 0.2603 0.2852 0.2665 -0.0250 -0.0484 0.0474  17  TYR   B CG  
3930 C CD1 . TYR   B 17  ? 0.2791 0.3026 0.2885 -0.0243 -0.0630 0.0590  17  TYR   B CD1 
3931 C CD2 . TYR   B 17  ? 0.2820 0.3152 0.2924 -0.0159 -0.0635 0.0492  17  TYR   B CD2 
3932 C CE1 . TYR   B 17  ? 0.3003 0.3294 0.3062 -0.0145 -0.0782 0.0559  17  TYR   B CE1 
3933 C CE2 . TYR   B 17  ? 0.2998 0.3367 0.3112 -0.0048 -0.0880 0.0536  17  TYR   B CE2 
3934 C CZ  . TYR   B 17  ? 0.3119 0.3475 0.3201 -0.0030 -0.0940 0.0579  17  TYR   B CZ  
3935 O OH  . TYR   B 17  ? 0.3293 0.3667 0.3352 0.0060  -0.1031 0.0606  17  TYR   B OH  
3945 N N   . ILE   B 18  ? 0.1938 0.1558 0.1902 -0.0382 -0.0055 -0.0153 18  ILE   B N   
3946 C CA  . ILE   B 18  ? 0.1980 0.1556 0.1943 -0.0443 -0.0039 -0.0208 18  ILE   B CA  
3947 C C   . ILE   B 18  ? 0.2074 0.1576 0.1928 -0.0568 -0.0048 -0.0335 18  ILE   B C   
3948 O O   . ILE   B 18  ? 0.2251 0.1748 0.2068 -0.0474 0.0073  -0.0418 18  ILE   B O   
3949 C CB  . ILE   B 18  ? 0.2034 0.1578 0.2020 -0.0444 -0.0105 -0.0151 18  ILE   B CB  
3950 C CG1 . ILE   B 18  ? 0.2009 0.1596 0.2126 -0.0448 0.0011  -0.0109 18  ILE   B CG1 
3951 C CG2 . ILE   B 18  ? 0.2070 0.1646 0.2058 -0.0472 -0.0215 -0.0185 18  ILE   B CG2 
3952 C CD1 . ILE   B 18  ? 0.2071 0.1865 0.2407 -0.0398 -0.0166 0.0194  18  ILE   B CD1 
3964 N N   . LYS   B 19  ? 0.2084 0.1604 0.2052 -0.0321 0.0312  -0.0428 19  LYS   B N   
3965 C CA  . LYS   B 19  ? 0.2154 0.1608 0.2223 -0.0364 0.0245  -0.0444 19  LYS   B CA  
3966 C C   . LYS   B 19  ? 0.1974 0.1594 0.2498 -0.0270 0.0324  -0.0559 19  LYS   B C   
3967 O O   . LYS   B 19  ? 0.1928 0.1654 0.2266 -0.0195 0.0263  -0.0504 19  LYS   B O   
3968 C CB  . LYS   B 19  ? 0.2430 0.1852 0.2288 -0.0437 0.0391  -0.0342 19  LYS   B CB  
3969 C CG  . LYS   B 19  ? 0.2719 0.2046 0.2603 -0.0512 0.0516  -0.0384 19  LYS   B CG  
3970 C CD  . LYS   B 19  ? 0.3037 0.2373 0.2719 -0.0544 0.0662  -0.0322 19  LYS   B CD  
3971 C CE  . LYS   B 19  ? 0.3307 0.2633 0.2937 -0.0570 0.0626  -0.0416 19  LYS   B CE  
3972 N NZ  . LYS   B 19  ? 0.3459 0.2784 0.3018 -0.0629 0.0620  -0.0441 19  LYS   B NZ  
3986 N N   . ASN   B 20  ? 0.1938 0.1720 0.2866 -0.0275 0.0387  -0.0680 20  ASN   B N   
3987 C CA  . ASN   B 20  ? 0.1970 0.1867 0.3072 -0.0186 0.0431  -0.0828 20  ASN   B CA  
3988 C C   . ASN   B 20  ? 0.1958 0.2057 0.2992 -0.0212 0.0566  -0.0921 20  ASN   B C   
3989 O O   . ASN   B 20  ? 0.2150 0.2398 0.3101 -0.0392 0.0561  -0.0932 20  ASN   B O   
3990 C CB  . ASN   B 20  ? 0.2274 0.1915 0.3391 0.0059  0.0336  -0.0816 20  ASN   B CB  
3991 C CG  . ASN   B 20  ? 0.2561 0.1955 0.3682 0.0382  0.0300  -0.0930 20  ASN   B CG  
3992 O OD1 . ASN   B 20  ? 0.2917 0.2264 0.3933 0.0555  0.0262  -0.0936 20  ASN   B OD1 
3993 N ND2 . ASN   B 20  ? 0.2466 0.1983 0.3675 0.0379  0.0200  -0.0858 20  ASN   B ND2 
4000 N N   . ALA   B 21  ? 0.2020 0.1881 0.2947 -0.0321 0.0555  -0.0744 21  ALA   B N   
4001 C CA  . ALA   B 21  ? 0.2100 0.1956 0.3025 -0.0376 0.0425  -0.0608 21  ALA   B CA  
4002 C C   . ALA   B 21  ? 0.2072 0.1731 0.2850 -0.0279 0.0423  -0.0384 21  ALA   B C   
4003 O O   . ALA   B 21  ? 0.2152 0.1628 0.2827 -0.0362 0.0386  -0.0327 21  ALA   B O   
4004 C CB  . ALA   B 21  ? 0.2225 0.2203 0.3091 -0.0542 0.0423  -0.0456 21  ALA   B CB  
4010 N N   . ASP   B 22  ? 0.1934 0.1603 0.2807 -0.0277 0.0335  -0.0336 22  ASP   B N   
4011 C CA  . ASP   B 22  ? 0.1893 0.1570 0.2673 -0.0144 0.0217  -0.0238 22  ASP   B CA  
4012 C C   . ASP   B 22  ? 0.1849 0.1516 0.2163 -0.0169 0.0229  -0.0141 22  ASP   B C   
4013 O O   . ASP   B 22  ? 0.1898 0.1591 0.2201 -0.0135 0.0108  -0.0111 22  ASP   B O   
4014 C CB  . ASP   B 22  ? 0.1977 0.1622 0.3037 -0.0062 0.0308  -0.0063 22  ASP   B CB  
4015 C CG  . ASP   B 22  ? 0.1970 0.1805 0.3457 -0.0002 0.0085  -0.0060 22  ASP   B CG  
4016 O OD1 . ASP   B 22  ? 0.2118 0.1740 0.3339 0.0044  -0.0160 -0.0036 22  ASP   B OD1 
4017 O OD2 . ASP   B 22  ? 0.2012 0.2083 0.4038 0.0079  -0.0106 -0.0261 22  ASP   B OD2 
4022 N N   . ILE   B 23  ? 0.1882 0.1456 0.1936 -0.0149 0.0015  0.0123  23  ILE   B N   
4023 C CA  . ILE   B 23  ? 0.1796 0.1455 0.1834 -0.0141 0.0017  0.0038  23  ILE   B CA  
4024 C C   . ILE   B 23  ? 0.1657 0.1447 0.1744 -0.0110 -0.0052 0.0005  23  ILE   B C   
4025 O O   . ILE   B 23  ? 0.1605 0.1459 0.1690 -0.0130 -0.0061 0.0041  23  ILE   B O   
4026 C CB  . ILE   B 23  ? 0.1706 0.1483 0.1881 -0.0252 -0.0002 0.0141  23  ILE   B CB  
4027 C CG1 . ILE   B 23  ? 0.1702 0.1591 0.1971 -0.0136 0.0017  0.0248  23  ILE   B CG1 
4028 C CG2 . ILE   B 23  ? 0.1787 0.1703 0.1962 -0.0181 0.0020  0.0073  23  ILE   B CG2 
4029 C CD1 . ILE   B 23  ? 0.1784 0.1735 0.2223 -0.0107 0.0123  0.0190  23  ILE   B CD1 
4041 N N   . VAL   B 24  ? 0.1667 0.1477 0.1882 -0.0153 -0.0065 -0.0007 24  VAL   B N   
4042 C CA  . VAL   B 24  ? 0.1600 0.1483 0.2136 -0.0080 -0.0204 0.0024  24  VAL   B CA  
4043 C C   . VAL   B 24  ? 0.1609 0.1498 0.2170 -0.0118 -0.0091 0.0014  24  VAL   B C   
4044 O O   . VAL   B 24  ? 0.1605 0.1622 0.2274 -0.0135 -0.0078 0.0118  24  VAL   B O   
4045 C CB  . VAL   B 24  ? 0.1686 0.1683 0.2241 -0.0005 -0.0254 0.0001  24  VAL   B CB  
4046 C CG1 . VAL   B 24  ? 0.1671 0.1722 0.2540 -0.0139 -0.0247 0.0005  24  VAL   B CG1 
4047 C CG2 . VAL   B 24  ? 0.1761 0.2015 0.2242 0.0056  -0.0232 -0.0117 24  VAL   B CG2 
4057 N N   . GLU   B 25  ? 0.1804 0.1627 0.2169 -0.0112 0.0000  0.0008  25  GLU   B N   
4058 C CA  . GLU   B 25  ? 0.1972 0.1921 0.2355 0.0014  0.0176  -0.0108 25  GLU   B CA  
4059 C C   . GLU   B 25  ? 0.1937 0.1853 0.2097 -0.0115 0.0192  -0.0002 25  GLU   B C   
4060 O O   . GLU   B 25  ? 0.1994 0.1951 0.2199 -0.0131 0.0228  0.0006  25  GLU   B O   
4061 C CB  . GLU   B 25  ? 0.2421 0.2432 0.3047 0.0281  0.0310  -0.0195 25  GLU   B CB  
4062 C CG  . GLU   B 25  ? 0.2894 0.3128 0.4213 0.0370  0.0285  -0.0230 25  GLU   B CG  
4063 C CD  . GLU   B 25  ? 0.3396 0.3774 0.5218 0.0332  0.0213  -0.0264 25  GLU   B CD  
4064 O OE1 . GLU   B 25  ? 0.3646 0.4014 0.5516 0.0366  0.0231  -0.0264 25  GLU   B OE1 
4065 O OE2 . GLU   B 25  ? 0.3636 0.3972 0.5541 0.0323  0.0156  -0.0320 25  GLU   B OE2 
4072 N N   . GLU   B 26  ? 0.1874 0.1728 0.1809 -0.0277 0.0140  0.0010  26  GLU   B N   
4073 C CA  . GLU   B 26  ? 0.1864 0.1884 0.1972 -0.0409 -0.0025 0.0043  26  GLU   B CA  
4074 C C   . GLU   B 26  ? 0.1691 0.1894 0.1754 -0.0295 0.0037  0.0161  26  GLU   B C   
4075 O O   . GLU   B 26  ? 0.1872 0.2142 0.1836 -0.0248 -0.0044 0.0286  26  GLU   B O   
4076 C CB  . GLU   B 26  ? 0.2190 0.2080 0.2186 -0.0528 0.0084  0.0186  26  GLU   B CB  
4077 C CG  . GLU   B 26  ? 0.2665 0.2491 0.2968 -0.0548 0.0170  -0.0060 26  GLU   B CG  
4078 C CD  . GLU   B 26  ? 0.2846 0.2679 0.3064 -0.0767 0.0337  -0.0428 26  GLU   B CD  
4079 O OE1 . GLU   B 26  ? 0.3015 0.2518 0.3245 -0.0858 0.0723  -0.0487 26  GLU   B OE1 
4080 O OE2 . GLU   B 26  ? 0.2914 0.3078 0.3522 -0.0641 0.0278  -0.0383 26  GLU   B OE2 
4087 N N   . ALA   B 27  ? 0.1589 0.1715 0.1803 -0.0282 0.0078  0.0154  27  ALA   B N   
4088 C CA  . ALA   B 27  ? 0.1598 0.1682 0.1883 -0.0150 -0.0032 0.0316  27  ALA   B CA  
4089 C C   . ALA   B 27  ? 0.1597 0.1779 0.2166 -0.0180 0.0057  0.0401  27  ALA   B C   
4090 O O   . ALA   B 27  ? 0.1701 0.1873 0.2272 -0.0137 0.0055  0.0501  27  ALA   B O   
4091 C CB  . ALA   B 27  ? 0.1716 0.1539 0.1861 -0.0165 0.0011  0.0294  27  ALA   B CB  
4097 N N   . LYS   B 28  ? 0.1561 0.1945 0.2546 -0.0242 0.0149  0.0609  28  LYS   B N   
4098 C CA  . LYS   B 28  ? 0.1759 0.2355 0.2766 -0.0067 0.0443  0.0913  28  LYS   B CA  
4099 C C   . LYS   B 28  ? 0.2019 0.2531 0.2625 0.0033  0.0615  0.0847  28  LYS   B C   
4100 O O   . LYS   B 28  ? 0.2282 0.2634 0.2821 0.0022  0.0661  0.0816  28  LYS   B O   
4101 C CB  . LYS   B 28  ? 0.1969 0.2743 0.3263 0.0030  0.0666  0.1116  28  LYS   B CB  
4102 C CG  . LYS   B 28  ? 0.2241 0.3241 0.3803 0.0127  0.0702  0.1158  28  LYS   B CG  
4103 C CD  . LYS   B 28  ? 0.2680 0.3850 0.4437 0.0205  0.0861  0.1137  28  LYS   B CD  
4104 C CE  . LYS   B 28  ? 0.3031 0.4347 0.4917 0.0317  0.0934  0.1141  28  LYS   B CE  
4105 N NZ  . LYS   B 28  ? 0.3176 0.4476 0.5149 0.0394  0.0917  0.1190  28  LYS   B NZ  
4119 N N   . LYS   B 29  ? 0.2196 0.2795 0.2676 0.0198  0.0570  0.0672  29  LYS   B N   
4120 C CA  . LYS   B 29  ? 0.2672 0.3171 0.2927 0.0168  0.0562  0.0633  29  LYS   B CA  
4121 C C   . LYS   B 29  ? 0.2597 0.3153 0.2556 0.0102  0.0414  0.0769  29  LYS   B C   
4122 O O   . LYS   B 29  ? 0.2811 0.3399 0.2740 0.0172  0.0422  0.0792  29  LYS   B O   
4123 C CB  . LYS   B 29  ? 0.3308 0.3619 0.3860 0.0149  0.0591  0.0420  29  LYS   B CB  
4124 C CG  . LYS   B 29  ? 0.3839 0.3995 0.4857 0.0098  0.0604  0.0303  29  LYS   B CG  
4125 C CD  . LYS   B 29  ? 0.4299 0.4284 0.5621 0.0033  0.0715  0.0194  29  LYS   B CD  
4126 C CE  . LYS   B 29  ? 0.4674 0.4521 0.6113 -0.0025 0.0823  0.0128  29  LYS   B CE  
4127 N NZ  . LYS   B 29  ? 0.4798 0.4601 0.6414 -0.0051 0.0867  0.0085  29  LYS   B NZ  
4141 N N   . VAL   B 30  ? 0.2254 0.2922 0.2356 -0.0106 0.0324  0.0758  30  VAL   B N   
4142 C CA  . VAL   B 30  ? 0.2099 0.2820 0.2720 -0.0202 -0.0077 0.0785  30  VAL   B CA  
4143 C C   . VAL   B 30  ? 0.1849 0.2738 0.2646 -0.0176 -0.0058 0.1019  30  VAL   B C   
4144 O O   . VAL   B 30  ? 0.1959 0.2878 0.2724 -0.0138 0.0019  0.1096  30  VAL   B O   
4145 C CB  . VAL   B 30  ? 0.2162 0.2752 0.3216 -0.0415 -0.0339 0.0714  30  VAL   B CB  
4146 C CG1 . VAL   B 30  ? 0.2255 0.2840 0.3253 -0.0366 -0.0206 0.0665  30  VAL   B CG1 
4147 C CG2 . VAL   B 30  ? 0.2289 0.2742 0.3434 -0.0508 -0.0467 0.0532  30  VAL   B CG2 
4157 N N   . LYS   B 31  ? 0.1743 0.2371 0.3064 -0.0299 -0.0062 0.1030  31  LYS   B N   
4158 C CA  . LYS   B 31  ? 0.1634 0.2305 0.3356 -0.0392 -0.0129 0.1069  31  LYS   B CA  
4159 C C   . LYS   B 31  ? 0.1610 0.1922 0.2956 -0.0402 -0.0259 0.0848  31  LYS   B C   
4160 O O   . LYS   B 31  ? 0.1647 0.2063 0.3100 -0.0274 -0.0220 0.1027  31  LYS   B O   
4161 C CB  . LYS   B 31  ? 0.1830 0.2819 0.3840 -0.0358 0.0139  0.1180  31  LYS   B CB  
4162 C CG  . LYS   B 31  ? 0.2245 0.3378 0.4340 -0.0382 0.0279  0.1094  31  LYS   B CG  
4163 C CD  . LYS   B 31  ? 0.2746 0.3958 0.4787 -0.0372 0.0278  0.0957  31  LYS   B CD  
4164 C CE  . LYS   B 31  ? 0.3150 0.4318 0.5230 -0.0369 0.0226  0.0843  31  LYS   B CE  
4165 N NZ  . LYS   B 31  ? 0.3349 0.4549 0.5399 -0.0310 0.0149  0.0747  31  LYS   B NZ  
4179 N N   . PRO   B 32  ? 0.1744 0.1598 0.2248 -0.0400 -0.0439 0.0490  32  PRO   B N   
4180 C CA  . PRO   B 32  ? 0.1851 0.1570 0.1819 -0.0379 -0.0433 0.0338  32  PRO   B CA  
4181 C C   . PRO   B 32  ? 0.1940 0.1483 0.1839 -0.0420 -0.0552 0.0339  32  PRO   B C   
4182 O O   . PRO   B 32  ? 0.2020 0.1463 0.2225 -0.0421 -0.0702 0.0358  32  PRO   B O   
4183 C CB  . PRO   B 32  ? 0.2001 0.1480 0.1816 -0.0451 -0.0348 0.0205  32  PRO   B CB  
4184 C CG  . PRO   B 32  ? 0.2172 0.1393 0.2004 -0.0298 -0.0520 0.0261  32  PRO   B CG  
4185 C CD  . PRO   B 32  ? 0.2001 0.1430 0.2166 -0.0239 -0.0611 0.0287  32  PRO   B CD  
4193 N N   . THR   B 33  ? 0.2018 0.1381 0.1690 -0.0367 -0.0512 0.0244  33  THR   B N   
4194 C CA  . THR   B 33  ? 0.2087 0.1472 0.1669 -0.0383 -0.0464 0.0286  33  THR   B CA  
4195 C C   . THR   B 33  ? 0.2076 0.1345 0.1643 -0.0346 -0.0483 0.0108  33  THR   B C   
4196 O O   . THR   B 33  ? 0.2274 0.1394 0.1727 -0.0451 -0.0588 0.0176  33  THR   B O   
4197 C CB  . THR   B 33  ? 0.2148 0.1538 0.1786 -0.0250 -0.0581 0.0317  33  THR   B CB  
4198 O OG1 . THR   B 33  ? 0.2050 0.1598 0.1830 -0.0276 -0.0518 0.0374  33  THR   B OG1 
4199 C CG2 . THR   B 33  ? 0.2404 0.1653 0.1954 -0.0170 -0.0529 0.0244  33  THR   B CG2 
4207 N N   . VAL   B 34  ? 0.1855 0.1331 0.1574 -0.0358 -0.0409 0.0128  34  VAL   B N   
4208 C CA  . VAL   B 34  ? 0.1675 0.1328 0.1530 -0.0329 -0.0345 0.0043  34  VAL   B CA  
4209 C C   . VAL   B 34  ? 0.1591 0.1267 0.1363 -0.0306 -0.0253 0.0047  34  VAL   B C   
4210 O O   . VAL   B 34  ? 0.1758 0.1318 0.1446 -0.0252 -0.0379 0.0106  34  VAL   B O   
4211 C CB  . VAL   B 34  ? 0.1774 0.1401 0.1802 -0.0129 -0.0329 0.0039  34  VAL   B CB  
4212 C CG1 . VAL   B 34  ? 0.1742 0.1534 0.1784 -0.0119 -0.0178 -0.0062 34  VAL   B CG1 
4213 C CG2 . VAL   B 34  ? 0.1825 0.1461 0.2057 -0.0111 -0.0324 0.0085  34  VAL   B CG2 
4223 N N   . VAL   B 35  ? 0.1528 0.1217 0.1305 -0.0268 -0.0169 0.0087  35  VAL   B N   
4224 C CA  . VAL   B 35  ? 0.1433 0.1237 0.1294 -0.0210 -0.0126 0.0078  35  VAL   B CA  
4225 C C   . VAL   B 35  ? 0.1310 0.1194 0.1342 -0.0164 -0.0149 0.0050  35  VAL   B C   
4226 O O   . VAL   B 35  ? 0.1368 0.1226 0.1505 -0.0217 -0.0047 0.0008  35  VAL   B O   
4227 C CB  . VAL   B 35  ? 0.1425 0.1414 0.1401 -0.0204 0.0012  0.0074  35  VAL   B CB  
4228 C CG1 . VAL   B 35  ? 0.1347 0.1530 0.1676 -0.0236 -0.0027 -0.0009 35  VAL   B CG1 
4229 C CG2 . VAL   B 35  ? 0.1460 0.1393 0.1591 -0.0123 -0.0029 -0.0034 35  VAL   B CG2 
4239 N N   . VAL   B 36  ? 0.1349 0.1162 0.1354 -0.0175 -0.0140 0.0111  36  VAL   B N   
4240 C CA  . VAL   B 36  ? 0.1267 0.1138 0.1393 -0.0121 -0.0066 0.0063  36  VAL   B CA  
4241 C C   . VAL   B 36  ? 0.1226 0.1170 0.1248 -0.0099 -0.0000 -0.0001 36  VAL   B C   
4242 O O   . VAL   B 36  ? 0.1370 0.1274 0.1528 -0.0140 -0.0038 -0.0073 36  VAL   B O   
4243 C CB  . VAL   B 36  ? 0.1295 0.1230 0.1435 -0.0108 -0.0092 0.0070  36  VAL   B CB  
4244 C CG1 . VAL   B 36  ? 0.1290 0.1394 0.1601 -0.0149 -0.0090 0.0139  36  VAL   B CG1 
4245 C CG2 . VAL   B 36  ? 0.1397 0.1288 0.1599 -0.0160 -0.0172 0.0083  36  VAL   B CG2 
4255 N N   . ASN   B 37  ? 0.1327 0.1215 0.1274 -0.0023 -0.0131 0.0043  37  ASN   B N   
4256 C CA  . ASN   B 37  ? 0.1327 0.1259 0.1378 -0.0002 -0.0113 0.0051  37  ASN   B CA  
4257 C C   . ASN   B 37  ? 0.1266 0.1273 0.1363 0.0030  -0.0083 0.0013  37  ASN   B C   
4258 O O   . ASN   B 37  ? 0.1364 0.1319 0.1430 0.0002  0.0037  0.0112  37  ASN   B O   
4259 C CB  . ASN   B 37  ? 0.1328 0.1284 0.1250 -0.0005 -0.0129 -0.0002 37  ASN   B CB  
4260 C CG  . ASN   B 37  ? 0.1333 0.1270 0.1403 -0.0017 -0.0125 0.0043  37  ASN   B CG  
4261 O OD1 . ASN   B 37  ? 0.1393 0.1335 0.1635 0.0107  -0.0136 -0.0009 37  ASN   B OD1 
4262 N ND2 . ASN   B 37  ? 0.1394 0.1282 0.1470 -0.0005 -0.0170 0.0050  37  ASN   B ND2 
4269 N N   . ALA   B 38  ? 0.1382 0.1244 0.1444 0.0082  0.0036  0.0061  38  ALA   B N   
4270 C CA  . ALA   B 38  ? 0.1496 0.1265 0.1398 0.0001  0.0104  0.0108  38  ALA   B CA  
4271 C C   . ALA   B 38  ? 0.1424 0.1221 0.1473 -0.0000 0.0059  0.0093  38  ALA   B C   
4272 O O   . ALA   B 38  ? 0.1560 0.1335 0.1588 0.0060  0.0010  0.0098  38  ALA   B O   
4273 C CB  . ALA   B 38  ? 0.1713 0.1362 0.1534 -0.0093 0.0168  0.0079  38  ALA   B CB  
4279 N N   . ALA   B 39  ? 0.1474 0.1234 0.1353 0.0058  -0.0021 0.0079  39  ALA   B N   
4280 C CA  . ALA   B 39  ? 0.1544 0.1313 0.1432 0.0061  -0.0037 0.0047  39  ALA   B CA  
4281 C C   . ALA   B 39  ? 0.1614 0.1412 0.1221 0.0096  -0.0089 0.0010  39  ALA   B C   
4282 O O   . ALA   B 39  ? 0.1585 0.1474 0.1547 0.0007  0.0004  0.0082  39  ALA   B O   
4283 C CB  . ALA   B 39  ? 0.1546 0.1352 0.1604 -0.0036 -0.0024 0.0013  39  ALA   B CB  
4289 N N   . ASN   B 40  ? 0.1645 0.1616 0.1308 0.0012  0.0006  -0.0059 40  ASN   B N   
4290 C CA  . ASN   B 40  ? 0.1730 0.1686 0.1417 0.0051  -0.0030 -0.0030 40  ASN   B CA  
4291 C C   . ASN   B 40  ? 0.1767 0.1657 0.1185 0.0086  -0.0067 0.0052  40  ASN   B C   
4292 O O   . ASN   B 40  ? 0.1711 0.1547 0.1391 0.0056  -0.0106 0.0044  40  ASN   B O   
4293 C CB  . ASN   B 40  ? 0.1852 0.1630 0.1604 0.0149  -0.0190 0.0123  40  ASN   B CB  
4294 C CG  . ASN   B 40  ? 0.1903 0.1704 0.1941 0.0086  -0.0242 0.0155  40  ASN   B CG  
4295 O OD1 . ASN   B 40  ? 0.1867 0.1658 0.2718 0.0033  -0.0345 0.0183  40  ASN   B OD1 
4296 N ND2 . ASN   B 40  ? 0.1960 0.1683 0.1899 0.0110  -0.0109 0.0209  40  ASN   B ND2 
4303 N N   . VAL   B 41  ? 0.1825 0.1718 0.1301 0.0162  0.0081  0.0040  41  VAL   B N   
4304 C CA  . VAL   B 41  ? 0.1896 0.1830 0.1354 0.0119  0.0016  -0.0108 41  VAL   B CA  
4305 C C   . VAL   B 41  ? 0.1874 0.1789 0.1368 0.0187  -0.0057 -0.0104 41  VAL   B C   
4306 O O   . VAL   B 41  ? 0.1805 0.1792 0.1452 0.0170  -0.0116 -0.0129 41  VAL   B O   
4307 C CB  . VAL   B 41  ? 0.2071 0.1986 0.1630 -0.0069 0.0220  -0.0243 41  VAL   B CB  
4308 C CG1 . VAL   B 41  ? 0.2035 0.2023 0.1846 -0.0068 0.0383  -0.0216 41  VAL   B CG1 
4309 C CG2 . VAL   B 41  ? 0.2178 0.2227 0.1678 -0.0183 0.0246  -0.0148 41  VAL   B CG2 
4319 N N   . TYR   B 42  ? 0.1930 0.1719 0.1379 0.0199  -0.0199 -0.0027 42  TYR   B N   
4320 C CA  . TYR   B 42  ? 0.1945 0.1814 0.1450 0.0202  -0.0256 -0.0128 42  TYR   B CA  
4321 C C   . TYR   B 42  ? 0.1784 0.1685 0.1529 0.0222  -0.0161 -0.0107 42  TYR   B C   
4322 O O   . TYR   B 42  ? 0.1804 0.1744 0.1885 0.0188  -0.0238 -0.0155 42  TYR   B O   
4323 C CB  . TYR   B 42  ? 0.2191 0.2127 0.1608 0.0101  -0.0287 -0.0019 42  TYR   B CB  
4324 C CG  . TYR   B 42  ? 0.2188 0.2304 0.1605 0.0010  -0.0292 0.0089  42  TYR   B CG  
4325 C CD1 . TYR   B 42  ? 0.2140 0.2287 0.1333 0.0012  -0.0145 0.0041  42  TYR   B CD1 
4326 C CD2 . TYR   B 42  ? 0.2351 0.2413 0.1983 0.0011  -0.0119 0.0196  42  TYR   B CD2 
4327 C CE1 . TYR   B 42  ? 0.2302 0.2463 0.1458 0.0033  -0.0096 0.0048  42  TYR   B CE1 
4328 C CE2 . TYR   B 42  ? 0.2372 0.2515 0.1968 0.0002  0.0162  0.0358  42  TYR   B CE2 
4329 C CZ  . TYR   B 42  ? 0.2475 0.2624 0.1700 0.0149  0.0182  0.0184  42  TYR   B CZ  
4330 O OH  . TYR   B 42  ? 0.2853 0.2921 0.2150 0.0322  0.0220  0.0339  42  TYR   B OH  
4340 N N   . LEU   B 43  ? 0.1673 0.1550 0.1379 0.0103  -0.0161 -0.0111 43  LEU   B N   
4341 C CA  . LEU   B 43  ? 0.1655 0.1545 0.1339 0.0055  -0.0133 -0.0027 43  LEU   B CA  
4342 C C   . LEU   B 43  ? 0.1696 0.1546 0.1445 0.0071  -0.0182 -0.0011 43  LEU   B C   
4343 O O   . LEU   B 43  ? 0.1635 0.1592 0.1674 0.0101  -0.0252 0.0038  43  LEU   B O   
4344 C CB  . LEU   B 43  ? 0.1618 0.1476 0.1437 -0.0002 -0.0243 -0.0066 43  LEU   B CB  
4345 C CG  . LEU   B 43  ? 0.1674 0.1465 0.1562 0.0062  -0.0227 -0.0031 43  LEU   B CG  
4346 C CD1 . LEU   B 43  ? 0.1815 0.1523 0.1953 0.0013  -0.0379 -0.0074 43  LEU   B CD1 
4347 C CD2 . LEU   B 43  ? 0.1676 0.1502 0.1697 -0.0077 -0.0267 -0.0079 43  LEU   B CD2 
4359 N N   . LYS   B 44  ? 0.1656 0.1501 0.1520 0.0089  -0.0129 -0.0087 44  LYS   B N   
4360 C CA  . LYS   B 44  ? 0.1875 0.1639 0.1491 0.0132  -0.0128 -0.0002 44  LYS   B CA  
4361 C C   . LYS   B 44  ? 0.1747 0.1569 0.1536 0.0180  -0.0125 0.0009  44  LYS   B C   
4362 O O   . LYS   B 44  ? 0.1963 0.1557 0.1740 0.0087  -0.0091 0.0031  44  LYS   B O   
4363 C CB  . LYS   B 44  ? 0.2164 0.1869 0.1617 0.0181  -0.0252 -0.0028 44  LYS   B CB  
4364 C CG  . LYS   B 44  ? 0.2541 0.2143 0.2008 0.0083  -0.0617 0.0033  44  LYS   B CG  
4365 C CD  . LYS   B 44  ? 0.2919 0.2363 0.2697 -0.0090 -0.0711 0.0032  44  LYS   B CD  
4366 C CE  . LYS   B 44  ? 0.3251 0.2631 0.3263 -0.0149 -0.0718 0.0129  44  LYS   B CE  
4367 N NZ  . LYS   B 44  ? 0.3339 0.2722 0.3547 -0.0116 -0.0833 0.0289  44  LYS   B NZ  
4381 N N   . HIS   B 45  ? 0.1655 0.1642 0.1463 0.0108  -0.0122 0.0066  45  HIS   B N   
4382 C CA  . HIS   B 45  ? 0.1687 0.1576 0.1411 0.0118  -0.0112 -0.0031 45  HIS   B CA  
4383 C C   . HIS   B 45  ? 0.1914 0.1739 0.1896 0.0225  -0.0192 -0.0048 45  HIS   B C   
4384 O O   . HIS   B 45  ? 0.2013 0.2048 0.2344 0.0481  0.0011  -0.0029 45  HIS   B O   
4385 C CB  . HIS   B 45  ? 0.1563 0.1620 0.1536 0.0065  -0.0093 -0.0057 45  HIS   B CB  
4386 C CG  . HIS   B 45  ? 0.1533 0.1556 0.1579 -0.0031 -0.0089 -0.0038 45  HIS   B CG  
4387 N ND1 . HIS   B 45  ? 0.1634 0.1446 0.1593 0.0007  -0.0192 -0.0079 45  HIS   B ND1 
4388 C CD2 . HIS   B 45  ? 0.1643 0.1567 0.1731 -0.0100 -0.0231 0.0021  45  HIS   B CD2 
4389 C CE1 . HIS   B 45  ? 0.1710 0.1385 0.1391 0.0010  -0.0315 -0.0081 45  HIS   B CE1 
4390 N NE2 . HIS   B 45  ? 0.1770 0.1455 0.1528 -0.0014 -0.0228 -0.0072 45  HIS   B NE2 
4398 N N   A GLY   B 46  ? 0.2059 0.1673 0.2272 0.0267  -0.0397 0.0071  46  GLY   B N   
4399 N N   B GLY   B 46  ? 0.2033 0.1777 0.2086 0.0241  -0.0325 0.0056  46  GLY   B N   
4400 C CA  A GLY   B 46  ? 0.2195 0.1824 0.2640 0.0192  -0.0488 0.0089  46  GLY   B CA  
4401 C CA  B GLY   B 46  ? 0.2143 0.1908 0.2284 0.0202  -0.0399 0.0125  46  GLY   B CA  
4402 C C   A GLY   B 46  ? 0.2211 0.1990 0.3048 0.0227  -0.0428 0.0088  46  GLY   B C   
4403 C C   B GLY   B 46  ? 0.2198 0.2053 0.2564 0.0225  -0.0361 0.0189  46  GLY   B C   
4404 O O   A GLY   B 46  ? 0.2243 0.2096 0.3901 0.0247  -0.0257 -0.0154 46  GLY   B O   
4405 O O   B GLY   B 46  ? 0.2244 0.2163 0.2730 0.0267  -0.0301 0.0306  46  GLY   B O   
4412 N N   . GLY   B 47  ? 0.2191 0.2072 0.2694 0.0128  -0.0236 0.0063  47  GLY   B N   
4413 C CA  . GLY   B 47  ? 0.2062 0.1796 0.2320 0.0067  -0.0190 0.0122  47  GLY   B CA  
4414 C C   . GLY   B 47  ? 0.1826 0.1589 0.1979 0.0033  -0.0034 0.0110  47  GLY   B C   
4415 O O   . GLY   B 47  ? 0.1902 0.1485 0.2094 0.0053  -0.0109 0.0121  47  GLY   B O   
4420 N N   . GLY   B 48  ? 0.1611 0.1469 0.2073 0.0029  -0.0111 0.0168  48  GLY   B N   
4421 C CA  . GLY   B 48  ? 0.1582 0.1481 0.1976 -0.0048 -0.0062 0.0089  48  GLY   B CA  
4422 C C   . GLY   B 48  ? 0.1489 0.1419 0.1876 0.0004  0.0017  0.0030  48  GLY   B C   
4423 O O   . GLY   B 48  ? 0.1475 0.1416 0.2085 0.0101  -0.0118 0.0037  48  GLY   B O   
4427 N N   . VAL   B 49  ? 0.1504 0.1456 0.1777 0.0099  -0.0017 0.0051  49  VAL   B N   
4428 C CA  . VAL   B 49  ? 0.1537 0.1531 0.1664 0.0109  -0.0146 -0.0084 49  VAL   B CA  
4429 C C   . VAL   B 49  ? 0.1419 0.1514 0.1478 0.0096  -0.0070 0.0062  49  VAL   B C   
4430 O O   . VAL   B 49  ? 0.1540 0.1505 0.1612 0.0085  -0.0032 0.0084  49  VAL   B O   
4431 C CB  . VAL   B 49  ? 0.1528 0.1730 0.1964 0.0069  -0.0237 -0.0044 49  VAL   B CB  
4432 C CG1 . VAL   B 49  ? 0.1539 0.1830 0.1838 0.0107  -0.0253 -0.0042 49  VAL   B CG1 
4433 C CG2 . VAL   B 49  ? 0.1724 0.1906 0.2132 -0.0071 -0.0438 -0.0083 49  VAL   B CG2 
4443 N N   . ALA   B 50  ? 0.1419 0.1420 0.1528 0.0030  -0.0041 0.0057  50  ALA   B N   
4444 C CA  . ALA   B 50  ? 0.1431 0.1337 0.1638 0.0094  -0.0054 0.0076  50  ALA   B CA  
4445 C C   . ALA   B 50  ? 0.1530 0.1336 0.1570 0.0005  -0.0001 0.0057  50  ALA   B C   
4446 O O   . ALA   B 50  ? 0.1478 0.1378 0.1561 0.0054  -0.0019 -0.0007 50  ALA   B O   
4447 C CB  . ALA   B 50  ? 0.1501 0.1347 0.1600 -0.0009 -0.0096 0.0173  50  ALA   B CB  
4453 N N   . GLY   B 51  ? 0.1502 0.1460 0.1697 0.0084  -0.0153 0.0120  51  GLY   B N   
4454 C CA  . GLY   B 51  ? 0.1574 0.1520 0.1741 0.0164  -0.0147 0.0074  51  GLY   B CA  
4455 C C   . GLY   B 51  ? 0.1540 0.1436 0.1745 0.0200  -0.0047 0.0068  51  GLY   B C   
4456 O O   . GLY   B 51  ? 0.1558 0.1588 0.2029 0.0109  -0.0032 -0.0017 51  GLY   B O   
4460 N N   . ALA   B 52  ? 0.1511 0.1439 0.1705 0.0169  -0.0063 0.0013  52  ALA   B N   
4461 C CA  . ALA   B 52  ? 0.1552 0.1534 0.1812 0.0185  0.0005  -0.0071 52  ALA   B CA  
4462 C C   . ALA   B 52  ? 0.1399 0.1499 0.1729 0.0099  -0.0050 -0.0094 52  ALA   B C   
4463 O O   . ALA   B 52  ? 0.1409 0.1553 0.1978 0.0108  -0.0029 -0.0011 52  ALA   B O   
4464 C CB  . ALA   B 52  ? 0.1737 0.1537 0.1789 0.0068  0.0044  -0.0074 52  ALA   B CB  
4470 N N   . LEU   B 53  ? 0.1356 0.1471 0.1612 0.0178  -0.0040 -0.0007 53  LEU   B N   
4471 C CA  . LEU   B 53  ? 0.1403 0.1582 0.1617 0.0172  -0.0071 0.0001  53  LEU   B CA  
4472 C C   . LEU   B 53  ? 0.1435 0.1458 0.1623 0.0162  -0.0032 0.0057  53  LEU   B C   
4473 O O   . LEU   B 53  ? 0.1515 0.1563 0.1716 -0.0001 0.0012  0.0122  53  LEU   B O   
4474 C CB  . LEU   B 53  ? 0.1358 0.1592 0.1706 0.0121  -0.0035 0.0113  53  LEU   B CB  
4475 C CG  . LEU   B 53  ? 0.1323 0.1704 0.1725 0.0054  -0.0040 0.0223  53  LEU   B CG  
4476 C CD1 . LEU   B 53  ? 0.1464 0.1941 0.1981 0.0175  -0.0053 0.0095  53  LEU   B CD1 
4477 C CD2 . LEU   B 53  ? 0.1481 0.1989 0.1985 -0.0046 -0.0150 -0.0025 53  LEU   B CD2 
4489 N N   . ASN   B 54  ? 0.1418 0.1358 0.1588 0.0061  -0.0057 0.0097  54  ASN   B N   
4490 C CA  . ASN   B 54  ? 0.1489 0.1514 0.1639 0.0035  -0.0094 0.0037  54  ASN   B CA  
4491 C C   . ASN   B 54  ? 0.1452 0.1535 0.1810 0.0014  0.0017  0.0008  54  ASN   B C   
4492 O O   . ASN   B 54  ? 0.1405 0.1574 0.1914 -0.0015 0.0021  -0.0017 54  ASN   B O   
4493 C CB  . ASN   B 54  ? 0.1533 0.1634 0.1730 0.0044  -0.0045 0.0012  54  ASN   B CB  
4494 C CG  . ASN   B 54  ? 0.1464 0.1702 0.1749 0.0052  -0.0064 -0.0045 54  ASN   B CG  
4495 O OD1 . ASN   B 54  ? 0.1414 0.1719 0.1912 0.0050  -0.0167 -0.0212 54  ASN   B OD1 
4496 N ND2 . ASN   B 54  ? 0.1604 0.1910 0.2004 0.0028  -0.0278 0.0100  54  ASN   B ND2 
4503 N N   . LYS   B 55  ? 0.1419 0.1587 0.1977 0.0120  -0.0007 -0.0010 55  LYS   B N   
4504 C CA  . LYS   B 55  ? 0.1486 0.1757 0.2199 0.0211  -0.0022 -0.0073 55  LYS   B CA  
4505 C C   . LYS   B 55  ? 0.1431 0.1682 0.2137 0.0130  0.0040  -0.0109 55  LYS   B C   
4506 O O   . LYS   B 55  ? 0.1410 0.1845 0.2257 0.0123  0.0037  -0.0038 55  LYS   B O   
4507 C CB  . LYS   B 55  ? 0.1615 0.1834 0.2492 0.0338  0.0041  0.0020  55  LYS   B CB  
4508 C CG  . LYS   B 55  ? 0.2132 0.2138 0.3316 0.0340  0.0130  0.0193  55  LYS   B CG  
4509 C CD  . LYS   B 55  ? 0.2538 0.2410 0.4045 0.0432  0.0304  0.0361  55  LYS   B CD  
4510 C CE  . LYS   B 55  ? 0.2814 0.2619 0.4696 0.0443  0.0465  0.0447  55  LYS   B CE  
4511 N NZ  . LYS   B 55  ? 0.2892 0.2805 0.5067 0.0398  0.0327  0.0560  55  LYS   B NZ  
4525 N N   . ALA   B 56  ? 0.1448 0.1750 0.1929 0.0069  0.0054  -0.0165 56  ALA   B N   
4526 C CA  . ALA   B 56  ? 0.1570 0.1903 0.1990 0.0043  0.0071  -0.0038 56  ALA   B CA  
4527 C C   . ALA   B 56  ? 0.1604 0.1849 0.1842 0.0029  0.0147  -0.0059 56  ALA   B C   
4528 O O   . ALA   B 56  ? 0.1729 0.1937 0.2070 0.0060  0.0318  -0.0011 56  ALA   B O   
4529 C CB  . ALA   B 56  ? 0.1702 0.2133 0.1882 -0.0160 0.0056  -0.0037 56  ALA   B CB  
4535 N N   . THR   B 57  ? 0.1514 0.1724 0.1895 0.0053  0.0118  0.0016  57  THR   B N   
4536 C CA  . THR   B 57  ? 0.1573 0.1742 0.1851 -0.0004 0.0233  0.0047  57  THR   B CA  
4537 C C   . THR   B 57  ? 0.1565 0.1859 0.2077 0.0025  0.0232  -0.0013 57  THR   B C   
4538 O O   . THR   B 57  ? 0.1635 0.1856 0.2226 -0.0132 0.0124  -0.0014 57  THR   B O   
4539 C CB  . THR   B 57  ? 0.1633 0.1587 0.1715 -0.0014 0.0148  0.0079  57  THR   B CB  
4540 O OG1 . THR   B 57  ? 0.1608 0.1544 0.1917 -0.0014 0.0123  -0.0038 57  THR   B OG1 
4541 C CG2 . THR   B 57  ? 0.1527 0.1681 0.1802 -0.0018 0.0246  0.0048  57  THR   B CG2 
4549 N N   . ASN   B 58  ? 0.1425 0.2081 0.2367 -0.0105 0.0094  -0.0182 58  ASN   B N   
4550 C CA  . ASN   B 58  ? 0.1620 0.2501 0.2786 -0.0293 0.0305  -0.0126 58  ASN   B CA  
4551 C C   . ASN   B 58  ? 0.1450 0.2248 0.2356 -0.0217 -0.0059 -0.0165 58  ASN   B C   
4552 O O   . ASN   B 58  ? 0.1476 0.2369 0.2488 -0.0166 0.0026  -0.0189 58  ASN   B O   
4553 C CB  . ASN   B 58  ? 0.2565 0.3301 0.3921 -0.0450 0.0745  -0.0035 58  ASN   B CB  
4554 C CG  . ASN   B 58  ? 0.3742 0.4083 0.5345 -0.0508 0.0970  0.0218  58  ASN   B CG  
4555 O OD1 . ASN   B 58  ? 0.4102 0.4306 0.5866 -0.0529 0.1007  0.0284  58  ASN   B OD1 
4556 N ND2 . ASN   B 58  ? 0.4522 0.4522 0.5852 -0.0532 0.1064  0.0285  58  ASN   B ND2 
4563 N N   . ASN   B 59  ? 0.1461 0.2049 0.2093 -0.0139 -0.0051 -0.0063 59  ASN   B N   
4564 C CA  . ASN   B 59  ? 0.1488 0.2053 0.2016 -0.0125 -0.0173 0.0036  59  ASN   B CA  
4565 C C   . ASN   B 59  ? 0.1427 0.2010 0.1976 -0.0157 -0.0163 -0.0059 59  ASN   B C   
4566 O O   . ASN   B 59  ? 0.1461 0.2002 0.1916 -0.0152 -0.0129 -0.0028 59  ASN   B O   
4567 C CB  . ASN   B 59  ? 0.1606 0.2244 0.2075 0.0003  -0.0270 0.0043  59  ASN   B CB  
4568 C CG  . ASN   B 59  ? 0.1761 0.2399 0.2165 0.0071  -0.0429 0.0033  59  ASN   B CG  
4569 O OD1 . ASN   B 59  ? 0.1764 0.2477 0.2223 0.0071  -0.0268 0.0190  59  ASN   B OD1 
4570 N ND2 . ASN   B 59  ? 0.1857 0.2515 0.2315 0.0050  -0.0422 -0.0094 59  ASN   B ND2 
4577 N N   . ALA   B 60  ? 0.1438 0.1870 0.1965 -0.0169 -0.0019 -0.0087 60  ALA   B N   
4578 C CA  . ALA   B 60  ? 0.1543 0.1743 0.1957 -0.0185 -0.0031 0.0023  60  ALA   B CA  
4579 C C   . ALA   B 60  ? 0.1532 0.1604 0.1701 -0.0110 -0.0059 0.0079  60  ALA   B C   
4580 O O   . ALA   B 60  ? 0.1607 0.1625 0.1979 -0.0160 -0.0014 -0.0047 60  ALA   B O   
4581 C CB  . ALA   B 60  ? 0.1648 0.1708 0.2194 -0.0172 -0.0036 -0.0006 60  ALA   B CB  
4587 N N   . MET   B 61  ? 0.1464 0.1586 0.1734 -0.0105 -0.0066 0.0035  61  MET   B N   
4588 C CA  . MET   B 61  ? 0.1410 0.1517 0.1666 -0.0084 -0.0159 0.0069  61  MET   B CA  
4589 C C   . MET   B 61  ? 0.1468 0.1453 0.1644 -0.0109 -0.0149 0.0060  61  MET   B C   
4590 O O   . MET   B 61  ? 0.1518 0.1487 0.1678 -0.0027 -0.0097 -0.0113 61  MET   B O   
4591 C CB  . MET   B 61  ? 0.1367 0.1493 0.1571 0.0017  -0.0080 -0.0005 61  MET   B CB  
4592 C CG  . MET   B 61  ? 0.1372 0.1478 0.1646 -0.0003 -0.0091 -0.0008 61  MET   B CG  
4593 S SD  . MET   B 61  ? 0.1423 0.1495 0.1856 -0.0024 -0.0068 -0.0080 61  MET   B SD  
4594 C CE  . MET   B 61  ? 0.1543 0.1736 0.2105 -0.0009 0.0003  -0.0183 61  MET   B CE  
4604 N N   . GLN   B 62  ? 0.1480 0.1526 0.1552 -0.0035 -0.0190 0.0044  62  GLN   B N   
4605 C CA  . GLN   B 62  ? 0.1509 0.1560 0.1708 0.0019  -0.0194 -0.0039 62  GLN   B CA  
4606 C C   . GLN   B 62  ? 0.1541 0.1676 0.1697 -0.0037 -0.0259 -0.0026 62  GLN   B C   
4607 O O   . GLN   B 62  ? 0.1686 0.1666 0.1723 -0.0065 -0.0326 -0.0126 62  GLN   B O   
4608 C CB  . GLN   B 62  ? 0.1492 0.1596 0.1733 0.0061  -0.0151 0.0096  62  GLN   B CB  
4609 C CG  . GLN   B 62  ? 0.1603 0.1669 0.1747 0.0071  -0.0244 -0.0028 62  GLN   B CG  
4610 C CD  . GLN   B 62  ? 0.1591 0.1655 0.1583 0.0101  -0.0284 0.0102  62  GLN   B CD  
4611 O OE1 . GLN   B 62  ? 0.1633 0.1605 0.1828 0.0086  -0.0308 -0.0050 62  GLN   B OE1 
4612 N NE2 . GLN   B 62  ? 0.1579 0.1744 0.1743 0.0065  -0.0257 -0.0055 62  GLN   B NE2 
4621 N N   . VAL   B 63  ? 0.1481 0.1683 0.1921 -0.0075 -0.0259 -0.0129 63  VAL   B N   
4622 C CA  . VAL   B 63  ? 0.1583 0.1730 0.2098 -0.0113 -0.0291 -0.0115 63  VAL   B CA  
4623 C C   . VAL   B 63  ? 0.1606 0.1609 0.1983 -0.0142 -0.0305 -0.0174 63  VAL   B C   
4624 O O   . VAL   B 63  ? 0.1727 0.1578 0.2073 -0.0132 -0.0434 -0.0134 63  VAL   B O   
4625 C CB  . VAL   B 63  ? 0.1608 0.1896 0.2441 -0.0128 -0.0348 -0.0083 63  VAL   B CB  
4626 C CG1 . VAL   B 63  ? 0.1696 0.1873 0.2544 -0.0256 -0.0246 -0.0142 63  VAL   B CG1 
4627 C CG2 . VAL   B 63  ? 0.1558 0.2069 0.2537 -0.0075 -0.0327 -0.0135 63  VAL   B CG2 
4637 N N   . GLU   B 64  ? 0.1570 0.1535 0.1890 -0.0055 -0.0274 -0.0158 64  GLU   B N   
4638 C CA  . GLU   B 64  ? 0.1567 0.1437 0.1768 -0.0122 -0.0276 -0.0126 64  GLU   B CA  
4639 C C   . GLU   B 64  ? 0.1513 0.1456 0.1660 -0.0020 -0.0269 -0.0095 64  GLU   B C   
4640 O O   . GLU   B 64  ? 0.1691 0.1508 0.1709 -0.0091 -0.0270 -0.0159 64  GLU   B O   
4641 C CB  . GLU   B 64  ? 0.1557 0.1573 0.1758 -0.0170 -0.0155 0.0009  64  GLU   B CB  
4642 C CG  . GLU   B 64  ? 0.1590 0.1582 0.1746 -0.0238 -0.0218 -0.0146 64  GLU   B CG  
4643 C CD  . GLU   B 64  ? 0.1662 0.1715 0.1883 -0.0292 -0.0219 -0.0142 64  GLU   B CD  
4644 O OE1 . GLU   B 64  ? 0.1691 0.1914 0.1957 -0.0311 -0.0190 -0.0375 64  GLU   B OE1 
4645 O OE2 . GLU   B 64  ? 0.1824 0.1816 0.1888 -0.0286 -0.0365 -0.0159 64  GLU   B OE2 
4652 N N   . SER   B 65  ? 0.1564 0.1388 0.1634 -0.0067 -0.0123 -0.0122 65  SER   B N   
4653 C CA  . SER   B 65  ? 0.1579 0.1406 0.1674 -0.0010 -0.0189 -0.0156 65  SER   B CA  
4654 C C   . SER   B 65  ? 0.1584 0.1436 0.1693 -0.0003 -0.0282 -0.0138 65  SER   B C   
4655 O O   . SER   B 65  ? 0.1688 0.1529 0.1639 0.0003  -0.0226 -0.0213 65  SER   B O   
4656 C CB  . SER   B 65  ? 0.1551 0.1490 0.1740 -0.0098 -0.0190 -0.0068 65  SER   B CB  
4657 O OG  . SER   B 65  ? 0.1550 0.1522 0.1710 -0.0046 -0.0195 -0.0214 65  SER   B OG  
4663 N N   . ASP   B 66  ? 0.1706 0.1512 0.1675 -0.0029 -0.0299 -0.0185 66  ASP   B N   
4664 C CA  . ASP   B 66  ? 0.1819 0.1593 0.1516 0.0019  -0.0364 -0.0095 66  ASP   B CA  
4665 C C   . ASP   B 66  ? 0.1853 0.1704 0.1548 -0.0062 -0.0295 -0.0140 66  ASP   B C   
4666 O O   . ASP   B 66  ? 0.1865 0.1700 0.1715 0.0008  -0.0282 -0.0238 66  ASP   B O   
4667 C CB  . ASP   B 66  ? 0.1970 0.1748 0.1742 0.0115  -0.0461 -0.0135 66  ASP   B CB  
4668 C CG  . ASP   B 66  ? 0.2204 0.1902 0.2035 0.0165  -0.0597 -0.0042 66  ASP   B CG  
4669 O OD1 . ASP   B 66  ? 0.2400 0.1864 0.2158 0.0134  -0.0546 -0.0020 66  ASP   B OD1 
4670 O OD2 . ASP   B 66  ? 0.2374 0.2125 0.2707 0.0374  -0.0609 -0.0075 66  ASP   B OD2 
4675 N N   . ASP   B 67  ? 0.1790 0.1587 0.1627 -0.0089 -0.0270 -0.0253 67  ASP   B N   
4676 C CA  . ASP   B 67  ? 0.1930 0.1558 0.1688 -0.0121 -0.0275 -0.0105 67  ASP   B CA  
4677 C C   . ASP   B 67  ? 0.1879 0.1544 0.1850 -0.0013 -0.0245 -0.0177 67  ASP   B C   
4678 O O   . ASP   B 67  ? 0.1959 0.1597 0.1901 -0.0036 -0.0207 -0.0250 67  ASP   B O   
4679 C CB  . ASP   B 67  ? 0.2123 0.1631 0.1865 -0.0190 -0.0408 -0.0144 67  ASP   B CB  
4680 C CG  . ASP   B 67  ? 0.2508 0.1692 0.1971 -0.0140 -0.0707 -0.0172 67  ASP   B CG  
4681 O OD1 . ASP   B 67  ? 0.2706 0.1734 0.2187 -0.0149 -0.0706 -0.0078 67  ASP   B OD1 
4682 O OD2 . ASP   B 67  ? 0.2658 0.1741 0.2151 0.0027  -0.0683 -0.0109 67  ASP   B OD2 
4687 N N   . TYR   B 68  ? 0.1816 0.1577 0.1766 0.0008  -0.0396 -0.0241 68  TYR   B N   
4688 C CA  . TYR   B 68  ? 0.1768 0.1704 0.1880 0.0101  -0.0347 -0.0360 68  TYR   B CA  
4689 C C   . TYR   B 68  ? 0.1718 0.1658 0.1879 0.0064  -0.0308 -0.0394 68  TYR   B C   
4690 O O   . TYR   B 68  ? 0.1774 0.1763 0.1913 0.0115  -0.0336 -0.0505 68  TYR   B O   
4691 C CB  . TYR   B 68  ? 0.1785 0.1921 0.1901 0.0086  -0.0396 -0.0453 68  TYR   B CB  
4692 C CG  . TYR   B 68  ? 0.1908 0.2034 0.1961 0.0179  -0.0330 -0.0645 68  TYR   B CG  
4693 C CD1 . TYR   B 68  ? 0.1906 0.2106 0.2215 0.0013  -0.0303 -0.0623 68  TYR   B CD1 
4694 C CD2 . TYR   B 68  ? 0.2010 0.2267 0.2150 0.0240  -0.0445 -0.0589 68  TYR   B CD2 
4695 C CE1 . TYR   B 68  ? 0.1979 0.2292 0.2458 0.0081  -0.0222 -0.0542 68  TYR   B CE1 
4696 C CE2 . TYR   B 68  ? 0.2010 0.2344 0.2266 0.0221  -0.0413 -0.0683 68  TYR   B CE2 
4697 C CZ  . TYR   B 68  ? 0.1932 0.2337 0.2387 0.0117  -0.0375 -0.0629 68  TYR   B CZ  
4698 O OH  . TYR   B 68  ? 0.1835 0.2486 0.2648 0.0060  -0.0293 -0.0380 68  TYR   B OH  
4708 N N   . ILE   B 69  ? 0.1705 0.1605 0.1756 0.0081  -0.0304 -0.0335 69  ILE   B N   
4709 C CA  . ILE   B 69  ? 0.1767 0.1637 0.1902 0.0007  -0.0233 -0.0373 69  ILE   B CA  
4710 C C   . ILE   B 69  ? 0.1739 0.1555 0.1816 0.0115  -0.0322 -0.0264 69  ILE   B C   
4711 O O   . ILE   B 69  ? 0.1845 0.1682 0.1720 0.0075  -0.0199 -0.0257 69  ILE   B O   
4712 C CB  . ILE   B 69  ? 0.1816 0.1684 0.2085 -0.0027 -0.0009 -0.0337 69  ILE   B CB  
4713 C CG1 . ILE   B 69  ? 0.1819 0.1773 0.2168 -0.0043 0.0082  -0.0317 69  ILE   B CG1 
4714 C CG2 . ILE   B 69  ? 0.1989 0.1767 0.2222 -0.0051 -0.0048 -0.0215 69  ILE   B CG2 
4715 C CD1 . ILE   B 69  ? 0.1776 0.1827 0.2384 -0.0162 0.0089  -0.0344 69  ILE   B CD1 
4727 N N   . ALA   B 70  ? 0.1745 0.1608 0.1781 0.0118  -0.0363 -0.0215 70  ALA   B N   
4728 C CA  . ALA   B 70  ? 0.1794 0.1684 0.1596 0.0040  -0.0383 -0.0243 70  ALA   B CA  
4729 C C   . ALA   B 70  ? 0.1878 0.1668 0.1713 -0.0028 -0.0424 -0.0356 70  ALA   B C   
4730 O O   . ALA   B 70  ? 0.2001 0.1667 0.1847 0.0021  -0.0401 -0.0354 70  ALA   B O   
4731 C CB  . ALA   B 70  ? 0.1804 0.1823 0.1733 0.0035  -0.0363 -0.0259 70  ALA   B CB  
4737 N N   . THR   B 71  ? 0.1967 0.1660 0.1794 -0.0009 -0.0534 -0.0276 71  THR   B N   
4738 C CA  . THR   B 71  ? 0.2060 0.1659 0.2024 0.0094  -0.0609 -0.0350 71  THR   B CA  
4739 C C   . THR   B 71  ? 0.1995 0.1711 0.2288 0.0273  -0.0553 -0.0437 71  THR   B C   
4740 O O   . THR   B 71  ? 0.2086 0.1796 0.2644 0.0220  -0.0531 -0.0558 71  THR   B O   
4741 C CB  . THR   B 71  ? 0.2290 0.1912 0.2271 0.0080  -0.0682 -0.0207 71  THR   B CB  
4742 O OG1 . THR   B 71  ? 0.2452 0.2203 0.2617 -0.0126 -0.0686 0.0014  71  THR   B OG1 
4743 C CG2 . THR   B 71  ? 0.2450 0.1902 0.2481 0.0137  -0.0597 -0.0080 71  THR   B CG2 
4751 N N   . ASN   B 72  ? 0.1836 0.1776 0.2215 0.0184  -0.0565 -0.0600 72  ASN   B N   
4752 C CA  . ASN   B 72  ? 0.1865 0.1873 0.2279 0.0230  -0.0431 -0.0736 72  ASN   B CA  
4753 C C   . ASN   B 72  ? 0.1853 0.1986 0.2345 0.0049  -0.0181 -0.0652 72  ASN   B C   
4754 O O   . ASN   B 72  ? 0.1861 0.2174 0.2620 0.0090  -0.0068 -0.0649 72  ASN   B O   
4755 C CB  . ASN   B 72  ? 0.1974 0.2001 0.2328 0.0161  -0.0626 -0.0632 72  ASN   B CB  
4756 C CG  . ASN   B 72  ? 0.2144 0.2168 0.2449 0.0302  -0.0633 -0.0325 72  ASN   B CG  
4757 O OD1 . ASN   B 72  ? 0.2373 0.2367 0.2466 0.0141  -0.0474 -0.0408 72  ASN   B OD1 
4758 N ND2 . ASN   B 72  ? 0.2245 0.2263 0.2946 0.0459  -0.0555 0.0017  72  ASN   B ND2 
4765 N N   . GLY   B 73  ? 0.1915 0.1976 0.2119 0.0019  -0.0251 -0.0619 73  GLY   B N   
4766 C CA  . GLY   B 73  ? 0.1864 0.2075 0.1885 -0.0006 -0.0230 -0.0555 73  GLY   B CA  
4767 C C   . GLY   B 73  ? 0.1805 0.2050 0.1620 0.0067  -0.0173 -0.0355 73  GLY   B C   
4768 O O   . GLY   B 73  ? 0.1785 0.1845 0.1702 0.0037  -0.0166 -0.0241 73  GLY   B O   
4772 N N   . PRO   B 74  ? 0.1805 0.2170 0.1481 0.0037  -0.0269 -0.0345 74  PRO   B N   
4773 C CA  . PRO   B 74  ? 0.1759 0.2153 0.1303 0.0073  -0.0181 -0.0159 74  PRO   B CA  
4774 C C   . PRO   B 74  ? 0.1612 0.2013 0.1425 0.0075  -0.0153 -0.0208 74  PRO   B C   
4775 O O   . PRO   B 74  ? 0.1631 0.2037 0.1936 0.0071  -0.0068 -0.0331 74  PRO   B O   
4776 C CB  . PRO   B 74  ? 0.1941 0.2374 0.1461 0.0041  -0.0121 -0.0147 74  PRO   B CB  
4777 C CG  . PRO   B 74  ? 0.2133 0.2454 0.1783 0.0044  -0.0153 -0.0128 74  PRO   B CG  
4778 C CD  . PRO   B 74  ? 0.2061 0.2367 0.1598 0.0065  -0.0173 -0.0224 74  PRO   B CD  
4786 N N   . LEU   B 75  ? 0.1590 0.1858 0.1365 0.0135  -0.0180 -0.0242 75  LEU   B N   
4787 C CA  . LEU   B 75  ? 0.1614 0.1892 0.1406 0.0048  -0.0148 -0.0061 75  LEU   B CA  
4788 C C   . LEU   B 75  ? 0.1727 0.2007 0.1421 0.0033  -0.0079 -0.0087 75  LEU   B C   
4789 O O   . LEU   B 75  ? 0.1886 0.2105 0.1545 -0.0079 -0.0114 -0.0015 75  LEU   B O   
4790 C CB  . LEU   B 75  ? 0.1657 0.1910 0.1296 -0.0074 -0.0189 0.0130  75  LEU   B CB  
4791 C CG  . LEU   B 75  ? 0.2014 0.2072 0.1433 -0.0322 -0.0091 0.0073  75  LEU   B CG  
4792 C CD1 . LEU   B 75  ? 0.2373 0.2263 0.1545 -0.0379 0.0133  0.0004  75  LEU   B CD1 
4793 C CD2 . LEU   B 75  ? 0.2398 0.2265 0.2101 -0.0216 0.0048  0.0075  75  LEU   B CD2 
4805 N N   . LYS   B 76  ? 0.1681 0.2200 0.1769 0.0008  -0.0006 0.0004  76  LYS   B N   
4806 C CA  . LYS   B 76  ? 0.1849 0.2261 0.1941 -0.0000 0.0153  0.0031  76  LYS   B CA  
4807 C C   . LYS   B 76  ? 0.1783 0.2108 0.1642 0.0103  0.0115  0.0278  76  LYS   B C   
4808 O O   . LYS   B 76  ? 0.1821 0.1932 0.1672 0.0036  0.0078  0.0220  76  LYS   B O   
4809 C CB  . LYS   B 76  ? 0.2001 0.2307 0.2577 -0.0088 0.0416  -0.0230 76  LYS   B CB  
4810 C CG  . LYS   B 76  ? 0.2063 0.2483 0.3018 0.0019  0.0248  -0.0290 76  LYS   B CG  
4811 C CD  . LYS   B 76  ? 0.2080 0.2590 0.3336 0.0090  0.0161  -0.0441 76  LYS   B CD  
4812 C CE  . LYS   B 76  ? 0.2170 0.2761 0.3858 0.0112  0.0020  -0.0561 76  LYS   B CE  
4813 N NZ  . LYS   B 76  ? 0.2142 0.2825 0.4086 0.0086  -0.0203 -0.0765 76  LYS   B NZ  
4827 N N   . VAL   B 77  ? 0.1887 0.2249 0.1668 0.0170  0.0155  0.0289  77  VAL   B N   
4828 C CA  . VAL   B 77  ? 0.1873 0.2114 0.1892 0.0201  0.0224  0.0547  77  VAL   B CA  
4829 C C   . VAL   B 77  ? 0.1678 0.1881 0.1804 0.0174  0.0322  0.0343  77  VAL   B C   
4830 O O   . VAL   B 77  ? 0.1733 0.1822 0.1882 0.0251  0.0333  0.0286  77  VAL   B O   
4831 C CB  . VAL   B 77  ? 0.1984 0.2203 0.2294 0.0192  0.0366  0.0743  77  VAL   B CB  
4832 C CG1 . VAL   B 77  ? 0.2037 0.2112 0.2654 0.0120  0.0426  0.0885  77  VAL   B CG1 
4833 C CG2 . VAL   B 77  ? 0.2137 0.2404 0.2387 0.0189  0.0124  0.0733  77  VAL   B CG2 
4843 N N   . GLY   B 78  ? 0.1598 0.1736 0.1697 0.0136  0.0186  0.0245  78  GLY   B N   
4844 C CA  . GLY   B 78  ? 0.1634 0.1689 0.1726 0.0130  0.0276  0.0238  78  GLY   B CA  
4845 C C   . GLY   B 78  ? 0.1574 0.1648 0.1619 0.0077  0.0219  0.0205  78  GLY   B C   
4846 O O   . GLY   B 78  ? 0.1607 0.1626 0.1874 0.0170  0.0189  0.0232  78  GLY   B O   
4850 N N   . GLY   B 79  ? 0.1493 0.1683 0.1649 0.0064  0.0134  0.0157  79  GLY   B N   
4851 C CA  . GLY   B 79  ? 0.1485 0.1587 0.1664 0.0094  0.0065  0.0156  79  GLY   B CA  
4852 C C   . GLY   B 79  ? 0.1393 0.1482 0.1627 0.0165  0.0090  0.0032  79  GLY   B C   
4853 O O   . GLY   B 79  ? 0.1522 0.1454 0.1774 0.0128  0.0197  0.0190  79  GLY   B O   
4857 N N   . SER   B 80  ? 0.1431 0.1389 0.1679 0.0095  0.0168  0.0039  80  SER   B N   
4858 C CA  . SER   B 80  ? 0.1363 0.1365 0.1639 0.0046  0.0092  0.0040  80  SER   B CA  
4859 C C   . SER   B 80  ? 0.1408 0.1357 0.1592 0.0071  -0.0028 -0.0018 80  SER   B C   
4860 O O   . SER   B 80  ? 0.1520 0.1398 0.1937 0.0093  0.0026  -0.0041 80  SER   B O   
4861 C CB  . SER   B 80  ? 0.1415 0.1396 0.1738 -0.0041 0.0022  0.0103  80  SER   B CB  
4862 O OG  . SER   B 80  ? 0.1496 0.1557 0.2027 -0.0068 -0.0102 0.0111  80  SER   B OG  
4868 N N   . CYS   B 81  ? 0.1415 0.1247 0.1650 0.0036  -0.0056 -0.0047 81  CYS   B N   
4869 C CA  . CYS   B 81  ? 0.1462 0.1243 0.1685 0.0036  -0.0081 -0.0018 81  CYS   B CA  
4870 C C   . CYS   B 81  ? 0.1430 0.1197 0.1496 -0.0006 -0.0161 -0.0061 81  CYS   B C   
4871 O O   . CYS   B 81  ? 0.1627 0.1249 0.1721 0.0041  -0.0039 -0.0021 81  CYS   B O   
4872 C CB  . CYS   B 81  ? 0.1594 0.1408 0.1695 -0.0037 -0.0146 -0.0108 81  CYS   B CB  
4873 S SG  . CYS   B 81  ? 0.1599 0.1579 0.1645 -0.0041 -0.0250 -0.0109 81  CYS   B SG  
4879 N N   . VAL   B 82  ? 0.1432 0.1248 0.1692 0.0004  -0.0130 -0.0029 82  VAL   B N   
4880 C CA  . VAL   B 82  ? 0.1478 0.1323 0.1568 -0.0056 -0.0092 0.0023  82  VAL   B CA  
4881 C C   . VAL   B 82  ? 0.1574 0.1179 0.1695 -0.0004 -0.0085 0.0009  82  VAL   B C   
4882 O O   . VAL   B 82  ? 0.1655 0.1214 0.2046 -0.0053 -0.0079 -0.0148 82  VAL   B O   
4883 C CB  . VAL   B 82  ? 0.1586 0.1480 0.1699 -0.0003 -0.0133 0.0044  82  VAL   B CB  
4884 C CG1 . VAL   B 82  ? 0.1746 0.1657 0.1723 0.0042  -0.0171 0.0138  82  VAL   B CG1 
4885 C CG2 . VAL   B 82  ? 0.1627 0.1590 0.1869 -0.0080 -0.0275 0.0165  82  VAL   B CG2 
4895 N N   . LEU   B 83  ? 0.1458 0.1205 0.1647 -0.0155 -0.0203 -0.0075 83  LEU   B N   
4896 C CA  . LEU   B 83  ? 0.1476 0.1317 0.1547 -0.0102 -0.0193 -0.0040 83  LEU   B CA  
4897 C C   . LEU   B 83  ? 0.1508 0.1225 0.1520 -0.0159 -0.0234 0.0025  83  LEU   B C   
4898 O O   . LEU   B 83  ? 0.1516 0.1356 0.1453 -0.0214 -0.0222 0.0037  83  LEU   B O   
4899 C CB  . LEU   B 83  ? 0.1514 0.1428 0.1617 -0.0092 -0.0202 -0.0080 83  LEU   B CB  
4900 C CG  . LEU   B 83  ? 0.1686 0.1612 0.1708 -0.0151 -0.0094 -0.0107 83  LEU   B CG  
4901 C CD1 . LEU   B 83  ? 0.1824 0.1633 0.1739 -0.0136 -0.0193 -0.0015 83  LEU   B CD1 
4902 C CD2 . LEU   B 83  ? 0.1877 0.1683 0.1877 -0.0065 -0.0044 -0.0252 83  LEU   B CD2 
4914 N N   . SER   B 84  ? 0.1498 0.1407 0.1714 -0.0220 -0.0216 0.0045  84  SER   B N   
4915 C CA  . SER   B 84  ? 0.1549 0.1586 0.1545 -0.0268 -0.0201 0.0138  84  SER   B CA  
4916 C C   . SER   B 84  ? 0.1439 0.1751 0.1219 -0.0215 -0.0202 0.0221  84  SER   B C   
4917 O O   . SER   B 84  ? 0.1551 0.1578 0.1247 -0.0178 -0.0115 0.0016  84  SER   B O   
4918 C CB  . SER   B 84  ? 0.1709 0.1611 0.1978 -0.0296 0.0087  0.0121  84  SER   B CB  
4919 O OG  . SER   B 84  ? 0.1747 0.1724 0.2452 -0.0345 0.0055  0.0213  84  SER   B OG  
4925 N N   . GLY   B 85  ? 0.1490 0.1957 0.1408 -0.0260 -0.0136 0.0216  85  GLY   B N   
4926 C CA  . GLY   B 85  ? 0.1525 0.2027 0.1555 -0.0342 -0.0032 -0.0075 85  GLY   B CA  
4927 C C   . GLY   B 85  ? 0.1497 0.1823 0.1398 -0.0381 -0.0067 0.0079  85  GLY   B C   
4928 O O   . GLY   B 85  ? 0.1620 0.1825 0.1551 -0.0518 0.0101  -0.0057 85  GLY   B O   
4932 N N   . HIS   B 86  ? 0.1471 0.1632 0.1657 -0.0318 -0.0198 0.0205  86  HIS   B N   
4933 C CA  . HIS   B 86  ? 0.1555 0.1612 0.1654 -0.0326 -0.0199 0.0148  86  HIS   B CA  
4934 C C   . HIS   B 86  ? 0.1520 0.1803 0.1549 -0.0438 -0.0103 0.0306  86  HIS   B C   
4935 O O   . HIS   B 86  ? 0.1674 0.1908 0.1664 -0.0372 -0.0003 0.0256  86  HIS   B O   
4936 C CB  . HIS   B 86  ? 0.1567 0.1685 0.1641 -0.0198 -0.0203 0.0089  86  HIS   B CB  
4937 C CG  . HIS   B 86  ? 0.1515 0.1770 0.1585 -0.0074 -0.0179 0.0087  86  HIS   B CG  
4938 N ND1 . HIS   B 86  ? 0.1674 0.2024 0.1869 -0.0258 -0.0226 -0.0103 86  HIS   B ND1 
4939 C CD2 . HIS   B 86  ? 0.1616 0.1829 0.1756 -0.0028 -0.0190 0.0019  86  HIS   B CD2 
4940 C CE1 . HIS   B 86  ? 0.1735 0.1975 0.1749 -0.0177 -0.0016 -0.0173 86  HIS   B CE1 
4941 N NE2 . HIS   B 86  ? 0.1750 0.1886 0.1618 -0.0002 -0.0087 -0.0048 86  HIS   B NE2 
4949 N N   . ASN   B 87  ? 0.1514 0.1819 0.1677 -0.0367 -0.0020 0.0187  87  ASN   B N   
4950 C CA  . ASN   B 87  ? 0.1625 0.2026 0.1740 -0.0324 0.0212  0.0086  87  ASN   B CA  
4951 C C   . ASN   B 87  ? 0.1797 0.1889 0.1520 -0.0310 0.0277  0.0075  87  ASN   B C   
4952 O O   . ASN   B 87  ? 0.2055 0.1935 0.1868 -0.0263 0.0475  0.0035  87  ASN   B O   
4953 C CB  . ASN   B 87  ? 0.1624 0.2299 0.2128 -0.0302 0.0311  0.0099  87  ASN   B CB  
4954 C CG  . ASN   B 87  ? 0.1761 0.2472 0.2259 0.0048  0.0391  0.0276  87  ASN   B CG  
4955 O OD1 . ASN   B 87  ? 0.1733 0.2305 0.2016 0.0131  0.0466  0.0399  87  ASN   B OD1 
4956 N ND2 . ASN   B 87  ? 0.2112 0.2597 0.2565 0.0139  0.0423  0.0286  87  ASN   B ND2 
4963 N N   . LEU   B 88  ? 0.1669 0.1743 0.1444 -0.0336 0.0133  0.0055  88  LEU   B N   
4964 C CA  . LEU   B 88  ? 0.1815 0.1622 0.1503 -0.0349 0.0011  -0.0019 88  LEU   B CA  
4965 C C   . LEU   B 88  ? 0.1781 0.1558 0.1586 -0.0411 -0.0036 0.0025  88  LEU   B C   
4966 O O   . LEU   B 88  ? 0.2032 0.1646 0.1891 -0.0216 -0.0287 -0.0070 88  LEU   B O   
4967 C CB  . LEU   B 88  ? 0.1935 0.1728 0.1685 -0.0437 -0.0136 0.0134  88  LEU   B CB  
4968 C CG  . LEU   B 88  ? 0.2320 0.2056 0.1873 -0.0348 -0.0310 0.0315  88  LEU   B CG  
4969 C CD1 . LEU   B 88  ? 0.2395 0.2350 0.2092 -0.0515 -0.0286 0.0420  88  LEU   B CD1 
4970 C CD2 . LEU   B 88  ? 0.2692 0.2288 0.2511 0.0029  -0.0496 0.0108  88  LEU   B CD2 
4982 N N   . ALA   B 89  ? 0.1602 0.1596 0.1440 -0.0420 0.0147  0.0022  89  ALA   B N   
4983 C CA  . ALA   B 89  ? 0.1609 0.1537 0.1289 -0.0399 0.0025  0.0056  89  ALA   B CA  
4984 C C   . ALA   B 89  ? 0.1719 0.1565 0.1377 -0.0399 0.0082  0.0036  89  ALA   B C   
4985 O O   . ALA   B 89  ? 0.1560 0.1612 0.1730 -0.0411 0.0094  -0.0274 89  ALA   B O   
4986 C CB  . ALA   B 89  ? 0.1517 0.1568 0.1521 -0.0371 0.0007  0.0109  89  ALA   B CB  
4992 N N   . LYS   B 90  ? 0.2076 0.1405 0.1489 -0.0477 -0.0153 0.0133  90  LYS   B N   
4993 C CA  . LYS   B 90  ? 0.2216 0.1355 0.1456 -0.0459 -0.0201 0.0150  90  LYS   B CA  
4994 C C   . LYS   B 90  ? 0.2035 0.1311 0.1557 -0.0406 -0.0173 0.0033  90  LYS   B C   
4995 O O   . LYS   B 90  ? 0.2077 0.1549 0.1647 -0.0570 -0.0054 0.0027  90  LYS   B O   
4996 C CB  . LYS   B 90  ? 0.2409 0.1440 0.1732 -0.0383 -0.0115 0.0240  90  LYS   B CB  
4997 C CG  . LYS   B 90  ? 0.2425 0.1569 0.1731 -0.0225 0.0143  0.0118  90  LYS   B CG  
4998 C CD  . LYS   B 90  ? 0.2720 0.1843 0.2193 -0.0126 0.0448  -0.0100 90  LYS   B CD  
4999 C CE  . LYS   B 90  ? 0.2815 0.2032 0.2741 -0.0227 0.0627  -0.0192 90  LYS   B CE  
5000 N NZ  . LYS   B 90  ? 0.2917 0.1925 0.2715 -0.0355 0.0866  -0.0087 90  LYS   B NZ  
5014 N N   . HIS   B 91  ? 0.1747 0.1249 0.1345 -0.0281 -0.0198 0.0110  91  HIS   B N   
5015 C CA  . HIS   B 91  ? 0.1603 0.1244 0.1508 -0.0216 -0.0226 0.0045  91  HIS   B CA  
5016 C C   . HIS   B 91  ? 0.1530 0.1314 0.1320 -0.0268 -0.0031 -0.0038 91  HIS   B C   
5017 O O   . HIS   B 91  ? 0.1635 0.1332 0.1351 -0.0306 -0.0160 0.0040  91  HIS   B O   
5018 C CB  . HIS   B 91  ? 0.1723 0.1262 0.1952 -0.0075 -0.0128 0.0132  91  HIS   B CB  
5019 C CG  . HIS   B 91  ? 0.2146 0.1467 0.2611 0.0014  0.0205  0.0209  91  HIS   B CG  
5020 N ND1 . HIS   B 91  ? 0.2500 0.1545 0.3178 0.0015  0.0298  0.0019  91  HIS   B ND1 
5021 C CD2 . HIS   B 91  ? 0.2281 0.1769 0.3122 0.0202  0.0101  0.0526  91  HIS   B CD2 
5022 C CE1 . HIS   B 91  ? 0.2576 0.1689 0.3340 0.0173  0.0260  0.0077  91  HIS   B CE1 
5023 N NE2 . HIS   B 91  ? 0.2462 0.1829 0.3344 0.0327  0.0231  0.0565  91  HIS   B NE2 
5031 N N   . CYS   B 92  ? 0.1436 0.1268 0.1341 -0.0248 -0.0096 -0.0015 92  CYS   B N   
5032 C CA  . CYS   B 92  ? 0.1401 0.1243 0.1362 -0.0255 -0.0071 -0.0023 92  CYS   B CA  
5033 C C   . CYS   B 92  ? 0.1365 0.1215 0.1271 -0.0150 -0.0098 0.0049  92  CYS   B C   
5034 O O   . CYS   B 92  ? 0.1444 0.1295 0.1481 -0.0152 -0.0061 -0.0005 92  CYS   B O   
5035 C CB  . CYS   B 92  ? 0.1395 0.1345 0.1368 -0.0173 -0.0055 -0.0003 92  CYS   B CB  
5036 S SG  . CYS   B 92  ? 0.1409 0.1353 0.1443 -0.0124 -0.0119 0.0041  92  CYS   B SG  
5042 N N   . LEU   B 93  ? 0.1292 0.1230 0.1374 -0.0145 -0.0101 -0.0003 93  LEU   B N   
5043 C CA  . LEU   B 93  ? 0.1315 0.1200 0.1416 -0.0064 -0.0133 0.0030  93  LEU   B CA  
5044 C C   . LEU   B 93  ? 0.1245 0.1165 0.1306 -0.0030 -0.0054 0.0067  93  LEU   B C   
5045 O O   . LEU   B 93  ? 0.1318 0.1210 0.1505 -0.0070 -0.0053 0.0022  93  LEU   B O   
5046 C CB  . LEU   B 93  ? 0.1372 0.1230 0.1507 -0.0074 -0.0085 0.0086  93  LEU   B CB  
5047 C CG  . LEU   B 93  ? 0.1379 0.1367 0.1670 -0.0079 -0.0106 0.0188  93  LEU   B CG  
5048 C CD1 . LEU   B 93  ? 0.1443 0.1509 0.1618 0.0048  -0.0020 0.0048  93  LEU   B CD1 
5049 C CD2 . LEU   B 93  ? 0.1368 0.1375 0.1809 -0.0035 -0.0151 0.0062  93  LEU   B CD2 
5061 N N   . HIS   B 94  ? 0.1330 0.1180 0.1325 -0.0064 -0.0181 0.0083  94  HIS   B N   
5062 C CA  . HIS   B 94  ? 0.1335 0.1192 0.1300 -0.0024 -0.0047 0.0081  94  HIS   B CA  
5063 C C   . HIS   B 94  ? 0.1317 0.1193 0.1521 0.0028  -0.0066 0.0126  94  HIS   B C   
5064 O O   . HIS   B 94  ? 0.1311 0.1294 0.1954 -0.0032 0.0134  -0.0011 94  HIS   B O   
5065 C CB  . HIS   B 94  ? 0.1316 0.1307 0.1411 -0.0002 -0.0099 -0.0006 94  HIS   B CB  
5066 C CG  . HIS   B 94  ? 0.1327 0.1259 0.1367 -0.0049 -0.0207 0.0022  94  HIS   B CG  
5067 N ND1 . HIS   B 94  ? 0.1383 0.1326 0.1365 -0.0022 -0.0193 -0.0016 94  HIS   B ND1 
5068 C CD2 . HIS   B 94  ? 0.1363 0.1265 0.1414 -0.0030 -0.0187 0.0030  94  HIS   B CD2 
5069 C CE1 . HIS   B 94  ? 0.1412 0.1335 0.1376 -0.0067 -0.0197 0.0038  94  HIS   B CE1 
5070 N NE2 . HIS   B 94  ? 0.1359 0.1354 0.1408 -0.0155 -0.0164 0.0048  94  HIS   B NE2 
5078 N N   . VAL   B 95  ? 0.1243 0.1167 0.1549 -0.0004 -0.0012 0.0066  95  VAL   B N   
5079 C CA  . VAL   B 95  ? 0.1268 0.1288 0.1399 -0.0004 0.0031  0.0138  95  VAL   B CA  
5080 C C   . VAL   B 95  ? 0.1346 0.1323 0.1440 0.0014  0.0077  0.0100  95  VAL   B C   
5081 O O   . VAL   B 95  ? 0.1358 0.1251 0.1739 0.0011  0.0059  0.0239  95  VAL   B O   
5082 C CB  . VAL   B 95  ? 0.1301 0.1290 0.1449 -0.0046 -0.0081 0.0080  95  VAL   B CB  
5083 C CG1 . VAL   B 95  ? 0.1440 0.1468 0.1668 -0.0088 -0.0004 0.0159  95  VAL   B CG1 
5084 C CG2 . VAL   B 95  ? 0.1396 0.1229 0.1412 0.0013  -0.0154 0.0016  95  VAL   B CG2 
5094 N N   . VAL   B 96  ? 0.1465 0.1309 0.1512 0.0094  0.0073  0.0170  96  VAL   B N   
5095 C CA  . VAL   B 96  ? 0.1539 0.1483 0.1453 0.0058  0.0080  0.0191  96  VAL   B CA  
5096 C C   . VAL   B 96  ? 0.1570 0.1509 0.1580 0.0087  0.0153  0.0214  96  VAL   B C   
5097 O O   . VAL   B 96  ? 0.1584 0.1570 0.1727 -0.0013 0.0134  0.0079  96  VAL   B O   
5098 C CB  . VAL   B 96  ? 0.1609 0.1698 0.1545 0.0063  0.0088  0.0082  96  VAL   B CB  
5099 C CG1 . VAL   B 96  ? 0.1569 0.1870 0.1633 0.0139  0.0107  0.0124  96  VAL   B CG1 
5100 C CG2 . VAL   B 96  ? 0.1766 0.1732 0.1622 0.0016  0.0044  0.0064  96  VAL   B CG2 
5110 N N   . GLY   B 97  ? 0.1592 0.1536 0.1530 0.0044  0.0083  0.0203  97  GLY   B N   
5111 C CA  . GLY   B 97  ? 0.1792 0.1511 0.1545 0.0047  0.0079  0.0241  97  GLY   B CA  
5112 C C   . GLY   B 97  ? 0.1985 0.1582 0.1754 0.0137  0.0104  0.0230  97  GLY   B C   
5113 O O   . GLY   B 97  ? 0.2149 0.1658 0.1775 0.0077  0.0076  0.0169  97  GLY   B O   
5117 N N   . PRO   B 98  ? 0.2144 0.1667 0.1832 0.0116  0.0386  0.0343  98  PRO   B N   
5118 C CA  . PRO   B 98  ? 0.2295 0.1859 0.1911 0.0255  0.0544  0.0311  98  PRO   B CA  
5119 C C   . PRO   B 98  ? 0.2442 0.1876 0.1640 0.0401  0.0560  0.0547  98  PRO   B C   
5120 O O   . PRO   B 98  ? 0.2315 0.1846 0.1843 0.0317  0.0532  0.0551  98  PRO   B O   
5121 C CB  . PRO   B 98  ? 0.2201 0.1920 0.2134 0.0178  0.0611  0.0338  98  PRO   B CB  
5122 C CG  . PRO   B 98  ? 0.2159 0.1830 0.2077 0.0128  0.0590  0.0452  98  PRO   B CG  
5123 C CD  . PRO   B 98  ? 0.1974 0.1693 0.2060 0.0164  0.0522  0.0420  98  PRO   B CD  
5131 N N   . ASN   B 99  ? 0.2599 0.2075 0.1762 0.0620  0.0564  0.0322  99  ASN   B N   
5132 C CA  . ASN   B 99  ? 0.2796 0.2186 0.1869 0.0717  0.0513  0.0569  99  ASN   B CA  
5133 C C   . ASN   B 99  ? 0.3083 0.2551 0.2161 0.0721  0.0791  0.0887  99  ASN   B C   
5134 O O   . ASN   B 99  ? 0.3255 0.2574 0.2235 0.0748  0.0748  0.0835  99  ASN   B O   
5135 C CB  . ASN   B 99  ? 0.2867 0.2100 0.1883 0.0716  0.0360  0.0509  99  ASN   B CB  
5136 C CG  . ASN   B 99  ? 0.2894 0.2179 0.2030 0.0654  0.0306  0.0394  99  ASN   B CG  
5137 O OD1 . ASN   B 99  ? 0.2940 0.2189 0.2317 0.0702  0.0335  0.0482  99  ASN   B OD1 
5138 N ND2 . ASN   B 99  ? 0.2864 0.2213 0.2158 0.0634  0.0041  0.0298  99  ASN   B ND2 
5145 N N   A VAL   B 100 ? 0.3246 0.2729 0.2638 0.0574  0.0846  0.1124  100 VAL   B N   
5146 N N   B VAL   B 100 ? 0.3281 0.2723 0.2627 0.0580  0.0715  0.1029  100 VAL   B N   
5147 C CA  A VAL   B 100 ? 0.3507 0.2914 0.3194 0.0420  0.0817  0.1296  100 VAL   B CA  
5148 C CA  B VAL   B 100 ? 0.3527 0.2891 0.3099 0.0446  0.0606  0.1128  100 VAL   B CA  
5149 C C   A VAL   B 100 ? 0.3715 0.2993 0.3088 0.0446  0.0760  0.1444  100 VAL   B C   
5150 C C   B VAL   B 100 ? 0.3719 0.2976 0.3083 0.0464  0.0572  0.1309  100 VAL   B C   
5151 O O   A VAL   B 100 ? 0.3797 0.3124 0.3157 0.0409  0.0894  0.1383  100 VAL   B O   
5152 O O   B VAL   B 100 ? 0.3770 0.3049 0.3123 0.0430  0.0617  0.1254  100 VAL   B O   
5153 C CB  A VAL   B 100 ? 0.3603 0.3036 0.3876 0.0200  0.0750  0.1395  100 VAL   B CB  
5154 C CB  B VAL   B 100 ? 0.3596 0.2979 0.3566 0.0284  0.0510  0.1101  100 VAL   B CB  
5155 C CG1 A VAL   B 100 ? 0.3652 0.3084 0.4135 0.0170  0.0718  0.1419  100 VAL   B CG1 
5156 C CG1 B VAL   B 100 ? 0.3627 0.3010 0.3740 0.0253  0.0476  0.1094  100 VAL   B CG1 
5157 C CG2 A VAL   B 100 ? 0.3615 0.3078 0.4062 0.0083  0.0773  0.1471  100 VAL   B CG2 
5158 C CG2 B VAL   B 100 ? 0.3611 0.3009 0.3714 0.0209  0.0496  0.1102  100 VAL   B CG2 
5177 N N   . ASN   B 101 ? 0.3860 0.3013 0.3077 0.0534  0.0494  0.1454  101 ASN   B N   
5178 C CA  . ASN   B 101 ? 0.4232 0.3149 0.3179 0.0607  0.0125  0.1506  101 ASN   B CA  
5179 C C   . ASN   B 101 ? 0.4692 0.3558 0.3293 0.0616  -0.0037 0.1598  101 ASN   B C   
5180 O O   . ASN   B 101 ? 0.4742 0.3678 0.3587 0.0660  -0.0001 0.1311  101 ASN   B O   
5181 C CB  . ASN   B 101 ? 0.4176 0.2969 0.3312 0.0542  0.0088  0.1248  101 ASN   B CB  
5182 C CG  . ASN   B 101 ? 0.4118 0.2789 0.3400 0.0499  0.0086  0.1151  101 ASN   B CG  
5183 O OD1 . ASN   B 101 ? 0.4132 0.2756 0.3616 0.0390  0.0276  0.1073  101 ASN   B OD1 
5184 N ND2 . ASN   B 101 ? 0.4086 0.2785 0.3343 0.0521  -0.0005 0.0986  101 ASN   B ND2 
5192 N N   . LYS   B 102 ? 0.5077 0.3942 0.3523 0.0495  0.0003  0.1559  102 LYS   B N   
5193 C CA  . LYS   B 102 ? 0.5438 0.4410 0.3781 0.0327  0.0057  0.1274  102 LYS   B CA  
5194 C C   . LYS   B 102 ? 0.5396 0.4446 0.3572 0.0321  0.0135  0.1345  102 LYS   B C   
5195 O O   . LYS   B 102 ? 0.5493 0.4502 0.3657 0.0333  -0.0031 0.1307  102 LYS   B O   
5196 C CB  . LYS   B 102 ? 0.5795 0.4819 0.4417 0.0186  0.0166  0.0769  102 LYS   B CB  
5197 C CG  . LYS   B 102 ? 0.6091 0.5176 0.5040 0.0077  0.0289  0.0290  102 LYS   B CG  
5198 C CD  . LYS   B 102 ? 0.6336 0.5464 0.5744 -0.0002 0.0420  -0.0082 102 LYS   B CD  
5199 C CE  . LYS   B 102 ? 0.6518 0.5667 0.6297 -0.0058 0.0509  -0.0353 102 LYS   B CE  
5200 N NZ  . LYS   B 102 ? 0.6610 0.5779 0.6634 -0.0081 0.0537  -0.0513 102 LYS   B NZ  
5214 N N   . GLY   B 103 ? 0.5213 0.4379 0.3543 0.0292  0.0387  0.1303  103 GLY   B N   
5215 C CA  . GLY   B 103 ? 0.5006 0.4291 0.3647 0.0297  0.0608  0.1098  103 GLY   B CA  
5216 C C   . GLY   B 103 ? 0.4753 0.4151 0.3597 0.0284  0.0802  0.0876  103 GLY   B C   
5217 O O   . GLY   B 103 ? 0.4821 0.4230 0.3660 0.0277  0.0842  0.0921  103 GLY   B O   
5221 N N   A GLU   B 104 ? 0.4564 0.3997 0.3418 0.0332  0.0994  0.0728  104 GLU   B N   
5222 N N   B GLU   B 104 ? 0.4585 0.4048 0.3575 0.0225  0.0736  0.0685  104 GLU   B N   
5223 C CA  A GLU   B 104 ? 0.4358 0.3839 0.3229 0.0427  0.1087  0.0536  104 GLU   B CA  
5224 C CA  B GLU   B 104 ? 0.4403 0.3934 0.3507 0.0183  0.0633  0.0456  104 GLU   B CA  
5225 C C   A GLU   B 104 ? 0.4393 0.3849 0.3364 0.0219  0.1458  0.0593  104 GLU   B C   
5226 C C   B GLU   B 104 ? 0.4358 0.3908 0.3638 0.0104  0.0752  0.0395  104 GLU   B C   
5227 O O   A GLU   B 104 ? 0.4416 0.3895 0.3560 0.0164  0.1468  0.0591  104 GLU   B O   
5228 O O   B GLU   B 104 ? 0.4370 0.3921 0.3720 0.0088  0.0750  0.0371  104 GLU   B O   
5229 C CB  A GLU   B 104 ? 0.4165 0.3651 0.3079 0.0741  0.0707  0.0189  104 GLU   B CB  
5230 C CB  B GLU   B 104 ? 0.4290 0.3835 0.3373 0.0219  0.0389  0.0238  104 GLU   B CB  
5231 C CG  A GLU   B 104 ? 0.3988 0.3506 0.2872 0.1039  0.0284  -0.0176 104 GLU   B CG  
5232 C CG  B GLU   B 104 ? 0.4198 0.3758 0.3236 0.0252  0.0135  0.0008  104 GLU   B CG  
5233 C CD  A GLU   B 104 ? 0.3849 0.3388 0.2617 0.1280  -0.0068 -0.0408 104 GLU   B CD  
5234 C CD  B GLU   B 104 ? 0.4140 0.3696 0.3119 0.0264  -0.0064 -0.0158 104 GLU   B CD  
5235 O OE1 A GLU   B 104 ? 0.3695 0.3252 0.2084 0.1463  -0.0024 -0.0463 104 GLU   B OE1 
5236 O OE1 B GLU   B 104 ? 0.4097 0.3649 0.2972 0.0256  -0.0090 -0.0190 104 GLU   B OE1 
5237 O OE2 A GLU   B 104 ? 0.3846 0.3436 0.2696 0.1291  -0.0373 -0.0515 104 GLU   B OE2 
5238 O OE2 B GLU   B 104 ? 0.4135 0.3697 0.3105 0.0269  -0.0206 -0.0249 104 GLU   B OE2 
5251 N N   A ASP   B 105 ? 0.4353 0.3813 0.3269 0.0083  0.1771  0.0632  105 ASP   B N   
5252 N N   B ASP   B 105 ? 0.4282 0.3867 0.3615 0.0043  0.0858  0.0349  105 ASP   B N   
5253 C CA  A ASP   B 105 ? 0.4351 0.3790 0.3477 -0.0011 0.1964  0.0454  105 ASP   B CA  
5254 C CA  B ASP   B 105 ? 0.4227 0.3825 0.3724 -0.0007 0.0921  0.0240  105 ASP   B CA  
5255 C C   A ASP   B 105 ? 0.4168 0.3487 0.3193 -0.0141 0.1981  0.0412  105 ASP   B C   
5256 C C   B ASP   B 105 ? 0.4117 0.3689 0.3499 -0.0064 0.0944  0.0169  105 ASP   B C   
5257 O O   A ASP   B 105 ? 0.4000 0.3414 0.3037 -0.0125 0.1974  0.0427  105 ASP   B O   
5258 O O   B ASP   B 105 ? 0.4106 0.3666 0.3391 -0.0064 0.0986  0.0182  105 ASP   B O   
5259 C CB  A ASP   B 105 ? 0.4525 0.4032 0.4225 0.0063  0.1973  0.0233  105 ASP   B CB  
5260 C CB  B ASP   B 105 ? 0.4269 0.3905 0.4089 0.0014  0.0938  0.0187  105 ASP   B CB  
5261 C CG  A ASP   B 105 ? 0.4651 0.4224 0.4939 0.0096  0.2049  0.0094  105 ASP   B CG  
5262 C CG  B ASP   B 105 ? 0.4307 0.3963 0.4464 0.0013  0.0982  0.0169  105 ASP   B CG  
5263 O OD1 A ASP   B 105 ? 0.4649 0.4272 0.5041 0.0038  0.2203  0.0165  105 ASP   B OD1 
5264 O OD1 B ASP   B 105 ? 0.4309 0.3987 0.4550 -0.0021 0.1010  0.0201  105 ASP   B OD1 
5265 O OD2 A ASP   B 105 ? 0.4721 0.4316 0.5344 0.0169  0.1967  -0.0059 105 ASP   B OD2 
5266 O OD2 B ASP   B 105 ? 0.4310 0.3984 0.4595 0.0026  0.1010  0.0157  105 ASP   B OD2 
5275 N N   A ILE   B 106 ? 0.4082 0.3234 0.3344 -0.0249 0.1844  0.0401  106 ILE   B N   
5276 N N   B ILE   B 106 ? 0.4000 0.3567 0.3416 -0.0094 0.0893  0.0118  106 ILE   B N   
5277 C CA  A ILE   B 106 ? 0.3870 0.2940 0.3465 -0.0400 0.1855  0.0350  106 ILE   B CA  
5278 C CA  B ILE   B 106 ? 0.3844 0.3444 0.3403 -0.0128 0.0888  0.0051  106 ILE   B CA  
5279 C C   A ILE   B 106 ? 0.3526 0.2856 0.3365 -0.0341 0.1875  0.0246  106 ILE   B C   
5280 C C   B ILE   B 106 ? 0.3630 0.3379 0.3358 -0.0092 0.0888  -0.0023 106 ILE   B C   
5281 O O   A ILE   B 106 ? 0.3421 0.2620 0.3402 -0.0387 0.1887  0.0278  106 ILE   B O   
5282 O O   B ILE   B 106 ? 0.3593 0.3311 0.3329 -0.0108 0.0850  -0.0062 106 ILE   B O   
5283 C CB  A ILE   B 106 ? 0.4028 0.2801 0.3631 -0.0570 0.1778  0.0402  106 ILE   B CB  
5284 C CB  B ILE   B 106 ? 0.3909 0.3416 0.3442 -0.0192 0.0871  0.0060  106 ILE   B CB  
5285 C CG1 A ILE   B 106 ? 0.4099 0.2753 0.3588 -0.0529 0.1658  0.0359  106 ILE   B CG1 
5286 C CG1 B ILE   B 106 ? 0.3927 0.3394 0.3408 -0.0179 0.0831  0.0064  106 ILE   B CG1 
5287 C CG2 A ILE   B 106 ? 0.4079 0.2821 0.3836 -0.0668 0.1800  0.0426  106 ILE   B CG2 
5288 C CG2 B ILE   B 106 ? 0.3939 0.3437 0.3540 -0.0226 0.0883  0.0062  106 ILE   B CG2 
5289 C CD1 A ILE   B 106 ? 0.4132 0.2754 0.3470 -0.0473 0.1611  0.0362  106 ILE   B CD1 
5290 C CD1 B ILE   B 106 ? 0.3933 0.3385 0.3379 -0.0160 0.0807  0.0073  106 ILE   B CD1 
5313 N N   A GLN   B 107 ? 0.3338 0.3033 0.3456 -0.0291 0.1795  0.0194  107 GLN   B N   
5314 N N   B GLN   B 107 ? 0.3471 0.3391 0.3455 -0.0061 0.0897  -0.0035 107 GLN   B N   
5315 C CA  A GLN   B 107 ? 0.3149 0.3200 0.3572 -0.0229 0.1590  0.0172  107 GLN   B CA  
5316 C CA  B GLN   B 107 ? 0.3311 0.3379 0.3541 -0.0023 0.0877  0.0010  107 GLN   B CA  
5317 C C   A GLN   B 107 ? 0.2838 0.2983 0.3260 -0.0061 0.1273  0.0073  107 GLN   B C   
5318 C C   B GLN   B 107 ? 0.2971 0.3110 0.3212 0.0051  0.0928  0.0010  107 GLN   B C   
5319 O O   A GLN   B 107 ? 0.2739 0.2983 0.3582 0.0033  0.1000  -0.0142 107 GLN   B O   
5320 O O   B GLN   B 107 ? 0.2952 0.3149 0.3337 0.0080  0.0799  -0.0104 107 GLN   B O   
5321 C CB  A GLN   B 107 ? 0.3448 0.3622 0.4275 -0.0232 0.1344  0.0184  107 GLN   B CB  
5322 C CB  B GLN   B 107 ? 0.3529 0.3636 0.4079 -0.0029 0.0728  0.0039  107 GLN   B CB  
5323 C CG  A GLN   B 107 ? 0.3753 0.4003 0.4957 -0.0197 0.0989  0.0185  107 GLN   B CG  
5324 C CG  B GLN   B 107 ? 0.3727 0.3864 0.4587 -0.0020 0.0546  0.0069  107 GLN   B CG  
5325 C CD  A GLN   B 107 ? 0.3967 0.4295 0.5501 -0.0195 0.0748  0.0217  107 GLN   B CD  
5326 C CD  B GLN   B 107 ? 0.3871 0.4039 0.5009 -0.0026 0.0413  0.0104  107 GLN   B CD  
5327 O OE1 A GLN   B 107 ? 0.4043 0.4413 0.5693 -0.0198 0.0717  0.0198  107 GLN   B OE1 
5328 O OE1 B GLN   B 107 ? 0.3925 0.4109 0.5147 -0.0035 0.0402  0.0104  107 GLN   B OE1 
5329 N NE2 A GLN   B 107 ? 0.4054 0.4383 0.5689 -0.0156 0.0645  0.0254  107 GLN   B NE2 
5330 N NE2 B GLN   B 107 ? 0.3925 0.4092 0.5162 -0.0005 0.0358  0.0128  107 GLN   B NE2 
5347 N N   . LEU   B 108 ? 0.2630 0.2787 0.2934 0.0150  0.1048  0.0087  108 LEU   B N   
5348 C CA  . LEU   B 108 ? 0.2389 0.2456 0.2484 0.0306  0.0744  0.0282  108 LEU   B CA  
5349 C C   . LEU   B 108 ? 0.1985 0.1970 0.2383 0.0301  0.0518  0.0319  108 LEU   B C   
5350 O O   . LEU   B 108 ? 0.1916 0.1866 0.2326 0.0262  0.0439  0.0270  108 LEU   B O   
5351 C CB  . LEU   B 108 ? 0.2590 0.2712 0.2325 0.0350  0.0708  0.0389  108 LEU   B CB  
5352 C CG  . LEU   B 108 ? 0.2736 0.3063 0.2379 0.0431  0.0671  0.0131  108 LEU   B CG  
5353 C CD1 . LEU   B 108 ? 0.2816 0.3217 0.2243 0.0395  0.0720  0.0083  108 LEU   B CD1 
5354 C CD2 . LEU   B 108 ? 0.2827 0.3155 0.2458 0.0508  0.0561  -0.0053 108 LEU   B CD2 
5367 N N   . LEU   B 109 ? 0.1803 0.1733 0.2363 0.0178  0.0454  0.0284  109 LEU   B N   
5368 C CA  . LEU   B 109 ? 0.1624 0.1502 0.2488 0.0075  0.0423  0.0332  109 LEU   B CA  
5369 C C   . LEU   B 109 ? 0.1543 0.1319 0.2445 0.0008  0.0334  0.0223  109 LEU   B C   
5370 O O   . LEU   B 109 ? 0.1492 0.1319 0.2397 0.0048  0.0372  0.0326  109 LEU   B O   
5371 C CB  . LEU   B 109 ? 0.1704 0.1429 0.2469 0.0083  0.0305  0.0406  109 LEU   B CB  
5372 C CG  . LEU   B 109 ? 0.1721 0.1359 0.2399 0.0033  0.0234  0.0206  109 LEU   B CG  
5373 C CD1 . LEU   B 109 ? 0.1680 0.1453 0.2234 0.0053  0.0323  0.0206  109 LEU   B CD1 
5374 C CD2 . LEU   B 109 ? 0.1829 0.1406 0.2554 0.0021  0.0157  0.0207  109 LEU   B CD2 
5386 N N   . LYS   B 110 ? 0.1454 0.1362 0.2392 -0.0046 0.0293  0.0262  110 LYS   B N   
5387 C CA  . LYS   B 110 ? 0.1459 0.1329 0.2438 -0.0009 0.0322  0.0214  110 LYS   B CA  
5388 C C   . LYS   B 110 ? 0.1381 0.1369 0.2318 -0.0019 0.0322  0.0129  110 LYS   B C   
5389 O O   . LYS   B 110 ? 0.1394 0.1353 0.2286 -0.0046 0.0255  0.0087  110 LYS   B O   
5390 C CB  . LYS   B 110 ? 0.1454 0.1342 0.2692 -0.0006 0.0298  0.0174  110 LYS   B CB  
5391 C CG  . LYS   B 110 ? 0.1453 0.1346 0.2857 -0.0034 0.0099  0.0224  110 LYS   B CG  
5392 C CD  . LYS   B 110 ? 0.1501 0.1319 0.2915 -0.0046 0.0062  0.0202  110 LYS   B CD  
5393 C CE  . LYS   B 110 ? 0.1447 0.1510 0.3122 -0.0054 0.0071  0.0135  110 LYS   B CE  
5394 N NZ  . LYS   B 110 ? 0.1464 0.1650 0.3025 0.0028  0.0003  0.0084  110 LYS   B NZ  
5408 N N   . SER   B 111 ? 0.1457 0.1331 0.2435 -0.0019 0.0260  0.0154  111 SER   B N   
5409 C CA  . SER   B 111 ? 0.1543 0.1374 0.2251 0.0009  0.0202  0.0183  111 SER   B CA  
5410 C C   . SER   B 111 ? 0.1460 0.1277 0.2078 0.0005  0.0163  0.0079  111 SER   B C   
5411 O O   . SER   B 111 ? 0.1402 0.1346 0.2290 0.0003  0.0180  0.0070  111 SER   B O   
5412 C CB  . SER   B 111 ? 0.1645 0.1605 0.2315 0.0048  0.0347  0.0259  111 SER   B CB  
5413 O OG  . SER   B 111 ? 0.1842 0.1926 0.2343 0.0066  0.0429  0.0300  111 SER   B OG  
5419 N N   . ALA   B 112 ? 0.1426 0.1326 0.2234 0.0060  0.0267  0.0214  112 ALA   B N   
5420 C CA  . ALA   B 112 ? 0.1356 0.1380 0.2075 0.0027  0.0117  0.0058  112 ALA   B CA  
5421 C C   . ALA   B 112 ? 0.1283 0.1330 0.2079 0.0021  0.0108  0.0087  112 ALA   B C   
5422 O O   . ALA   B 112 ? 0.1272 0.1361 0.2092 -0.0052 0.0129  0.0043  112 ALA   B O   
5423 C CB  . ALA   B 112 ? 0.1426 0.1420 0.2231 0.0014  0.0071  0.0119  112 ALA   B CB  
5429 N N   . TYR   B 113 ? 0.1295 0.1218 0.2142 -0.0046 0.0102  0.0076  113 TYR   B N   
5430 C CA  . TYR   B 113 ? 0.1291 0.1200 0.2004 -0.0013 0.0119  0.0038  113 TYR   B CA  
5431 C C   . TYR   B 113 ? 0.1299 0.1159 0.1952 -0.0110 0.0116  0.0034  113 TYR   B C   
5432 O O   . TYR   B 113 ? 0.1266 0.1188 0.1977 -0.0042 0.0021  -0.0023 113 TYR   B O   
5433 C CB  . TYR   B 113 ? 0.1323 0.1111 0.2115 -0.0050 0.0148  0.0109  113 TYR   B CB  
5434 C CG  . TYR   B 113 ? 0.1344 0.1190 0.2250 -0.0064 0.0126  0.0141  113 TYR   B CG  
5435 C CD1 . TYR   B 113 ? 0.1389 0.1176 0.2372 -0.0065 0.0083  0.0197  113 TYR   B CD1 
5436 C CD2 . TYR   B 113 ? 0.1401 0.1193 0.2222 -0.0012 0.0104  0.0090  113 TYR   B CD2 
5437 C CE1 . TYR   B 113 ? 0.1418 0.1270 0.2246 -0.0013 0.0197  0.0119  113 TYR   B CE1 
5438 C CE2 . TYR   B 113 ? 0.1491 0.1149 0.2326 0.0013  0.0197  0.0139  113 TYR   B CE2 
5439 C CZ  . TYR   B 113 ? 0.1383 0.1197 0.2353 0.0068  0.0133  0.0065  113 TYR   B CZ  
5440 O OH  . TYR   B 113 ? 0.1429 0.1197 0.2606 0.0087  0.0205  0.0100  113 TYR   B OH  
5450 N N   . GLU   B 114 ? 0.1271 0.1105 0.2157 -0.0083 0.0106  0.0089  114 GLU   B N   
5451 C CA  . GLU   B 114 ? 0.1194 0.1073 0.2214 0.0011  -0.0001 0.0056  114 GLU   B CA  
5452 C C   . GLU   B 114 ? 0.1232 0.1146 0.2099 -0.0009 0.0083  0.0040  114 GLU   B C   
5453 O O   . GLU   B 114 ? 0.1221 0.1179 0.2146 0.0017  0.0012  0.0141  114 GLU   B O   
5454 C CB  . GLU   B 114 ? 0.1217 0.1182 0.2183 -0.0024 0.0092  0.0009  114 GLU   B CB  
5455 C CG  . GLU   B 114 ? 0.1341 0.1197 0.2223 -0.0024 0.0112  0.0021  114 GLU   B CG  
5456 C CD  . GLU   B 114 ? 0.1280 0.1212 0.2353 -0.0078 0.0110  0.0048  114 GLU   B CD  
5457 O OE1 . GLU   B 114 ? 0.1267 0.1390 0.2233 -0.0087 0.0217  0.0140  114 GLU   B OE1 
5458 O OE2 . GLU   B 114 ? 0.1294 0.1462 0.2529 -0.0157 0.0115  0.0108  114 GLU   B OE2 
5465 N N   . ASN   B 115 ? 0.1237 0.1139 0.1981 -0.0058 -0.0029 0.0092  115 ASN   B N   
5466 C CA  . ASN   B 115 ? 0.1307 0.1221 0.1819 -0.0106 0.0015  0.0124  115 ASN   B CA  
5467 C C   . ASN   B 115 ? 0.1262 0.1125 0.1862 -0.0134 -0.0125 0.0054  115 ASN   B C   
5468 O O   . ASN   B 115 ? 0.1361 0.1207 0.2007 -0.0139 -0.0035 0.0057  115 ASN   B O   
5469 C CB  . ASN   B 115 ? 0.1427 0.1313 0.1908 -0.0090 0.0042  0.0091  115 ASN   B CB  
5470 C CG  . ASN   B 115 ? 0.1500 0.1371 0.1879 0.0007  0.0066  0.0045  115 ASN   B CG  
5471 O OD1 . ASN   B 115 ? 0.1908 0.1512 0.2099 -0.0019 0.0117  -0.0026 115 ASN   B OD1 
5472 N ND2 . ASN   B 115 ? 0.1400 0.1504 0.1910 -0.0061 0.0018  0.0086  115 ASN   B ND2 
5479 N N   . PHE   B 116 ? 0.1258 0.1149 0.1717 -0.0082 -0.0029 0.0065  116 PHE   B N   
5480 C CA  . PHE   B 116 ? 0.1293 0.1201 0.1733 -0.0116 -0.0050 0.0016  116 PHE   B CA  
5481 C C   . PHE   B 116 ? 0.1300 0.1105 0.1775 -0.0113 -0.0098 0.0016  116 PHE   B C   
5482 O O   . PHE   B 116 ? 0.1339 0.1237 0.1879 -0.0066 -0.0115 0.0032  116 PHE   B O   
5483 C CB  . PHE   B 116 ? 0.1275 0.1209 0.1717 -0.0058 -0.0042 0.0055  116 PHE   B CB  
5484 C CG  . PHE   B 116 ? 0.1230 0.1190 0.1781 -0.0123 -0.0046 0.0078  116 PHE   B CG  
5485 C CD1 . PHE   B 116 ? 0.1321 0.1233 0.1859 -0.0029 -0.0004 0.0027  116 PHE   B CD1 
5486 C CD2 . PHE   B 116 ? 0.1306 0.1294 0.1715 -0.0069 -0.0029 -0.0003 116 PHE   B CD2 
5487 C CE1 . PHE   B 116 ? 0.1350 0.1321 0.1922 -0.0069 -0.0125 0.0131  116 PHE   B CE1 
5488 C CE2 . PHE   B 116 ? 0.1294 0.1251 0.1797 -0.0059 -0.0035 0.0040  116 PHE   B CE2 
5489 C CZ  . PHE   B 116 ? 0.1240 0.1304 0.1792 -0.0028 -0.0037 0.0127  116 PHE   B CZ  
5499 N N   . ASN   B 117 ? 0.1290 0.1151 0.1980 -0.0060 -0.0132 0.0046  117 ASN   B N   
5500 C CA  . ASN   B 117 ? 0.1410 0.1167 0.2003 -0.0028 -0.0113 0.0043  117 ASN   B CA  
5501 C C   . ASN   B 117 ? 0.1384 0.1185 0.2055 -0.0006 -0.0093 0.0026  117 ASN   B C   
5502 O O   . ASN   B 117 ? 0.1435 0.1251 0.2308 -0.0041 -0.0282 0.0098  117 ASN   B O   
5503 C CB  . ASN   B 117 ? 0.1391 0.1193 0.2090 0.0010  -0.0108 0.0013  117 ASN   B CB  
5504 C CG  . ASN   B 117 ? 0.1336 0.1234 0.2162 0.0018  -0.0119 -0.0043 117 ASN   B CG  
5505 O OD1 . ASN   B 117 ? 0.1516 0.1246 0.2321 -0.0166 -0.0057 -0.0064 117 ASN   B OD1 
5506 N ND2 . ASN   B 117 ? 0.1354 0.1290 0.2116 -0.0091 -0.0058 -0.0016 117 ASN   B ND2 
5513 N N   . GLN   B 118 ? 0.1420 0.1140 0.1904 -0.0101 -0.0146 -0.0014 118 GLN   B N   
5514 C CA  . GLN   B 118 ? 0.1404 0.1169 0.2102 -0.0045 -0.0137 -0.0058 118 GLN   B CA  
5515 C C   . GLN   B 118 ? 0.1415 0.1150 0.2183 -0.0038 -0.0155 -0.0051 118 GLN   B C   
5516 O O   . GLN   B 118 ? 0.1623 0.1197 0.2423 -0.0126 -0.0015 0.0031  118 GLN   B O   
5517 C CB  . GLN   B 118 ? 0.1495 0.1211 0.2156 -0.0046 -0.0134 -0.0048 118 GLN   B CB  
5518 C CG  . GLN   B 118 ? 0.1557 0.1252 0.2214 0.0026  -0.0066 -0.0082 118 GLN   B CG  
5519 C CD  . GLN   B 118 ? 0.1564 0.1199 0.2185 0.0025  -0.0106 -0.0122 118 GLN   B CD  
5520 O OE1 . GLN   B 118 ? 0.1690 0.1214 0.2363 0.0017  0.0053  0.0044  118 GLN   B OE1 
5521 N NE2 . GLN   B 118 ? 0.1675 0.1256 0.2185 0.0029  -0.0189 0.0021  118 GLN   B NE2 
5530 N N   . HIS   B 119 ? 0.1481 0.1210 0.1884 -0.0135 -0.0149 0.0087  119 HIS   B N   
5531 C CA  . HIS   B 119 ? 0.1563 0.1332 0.1806 -0.0085 -0.0175 0.0138  119 HIS   B CA  
5532 C C   . HIS   B 119 ? 0.1590 0.1346 0.1676 -0.0024 -0.0354 0.0098  119 HIS   B C   
5533 O O   . HIS   B 119 ? 0.1653 0.1346 0.1943 -0.0267 -0.0244 0.0085  119 HIS   B O   
5534 C CB  . HIS   B 119 ? 0.1601 0.1461 0.1765 -0.0029 -0.0259 0.0031  119 HIS   B CB  
5535 C CG  . HIS   B 119 ? 0.1653 0.1631 0.2013 0.0033  -0.0366 -0.0151 119 HIS   B CG  
5536 N ND1 . HIS   B 119 ? 0.1812 0.1802 0.2350 0.0001  -0.0456 -0.0348 119 HIS   B ND1 
5537 C CD2 . HIS   B 119 ? 0.1856 0.1800 0.2038 0.0359  -0.0522 -0.0206 119 HIS   B CD2 
5538 C CE1 . HIS   B 119 ? 0.1960 0.1923 0.2389 0.0165  -0.0596 -0.0418 119 HIS   B CE1 
5539 N NE2 . HIS   B 119 ? 0.2073 0.2055 0.2194 0.0306  -0.0528 -0.0364 119 HIS   B NE2 
5547 N N   . GLU   B 120 ? 0.1793 0.1395 0.1690 -0.0113 -0.0415 0.0172  120 GLU   B N   
5548 C CA  . GLU   B 120 ? 0.2133 0.1503 0.1895 -0.0049 -0.0475 0.0277  120 GLU   B CA  
5549 C C   . GLU   B 120 ? 0.1886 0.1413 0.1801 -0.0162 -0.0370 0.0282  120 GLU   B C   
5550 O O   . GLU   B 120 ? 0.1775 0.1507 0.1832 -0.0164 -0.0399 0.0143  120 GLU   B O   
5551 C CB  . GLU   B 120 ? 0.2791 0.1824 0.2582 0.0162  -0.0749 0.0467  120 GLU   B CB  
5552 C CG  . GLU   B 120 ? 0.3341 0.2610 0.3539 0.0292  -0.0989 0.0662  120 GLU   B CG  
5553 C CD  . GLU   B 120 ? 0.3799 0.3337 0.4606 0.0333  -0.1075 0.0831  120 GLU   B CD  
5554 O OE1 . GLU   B 120 ? 0.4015 0.3598 0.4968 0.0291  -0.1017 0.1013  120 GLU   B OE1 
5555 O OE2 . GLU   B 120 ? 0.3990 0.3685 0.5134 0.0323  -0.1096 0.0750  120 GLU   B OE2 
5562 N N   . VAL   B 121 ? 0.1786 0.1404 0.1655 -0.0204 -0.0284 0.0176  121 VAL   B N   
5563 C CA  . VAL   B 121 ? 0.1727 0.1465 0.1490 -0.0210 -0.0255 0.0153  121 VAL   B CA  
5564 C C   . VAL   B 121 ? 0.1665 0.1404 0.1563 -0.0282 -0.0184 0.0117  121 VAL   B C   
5565 O O   . VAL   B 121 ? 0.1743 0.1358 0.1756 -0.0321 -0.0262 0.0103  121 VAL   B O   
5566 C CB  . VAL   B 121 ? 0.1941 0.1880 0.1683 -0.0095 -0.0335 0.0213  121 VAL   B CB  
5567 C CG1 . VAL   B 121 ? 0.2030 0.2007 0.2089 -0.0200 -0.0195 0.0183  121 VAL   B CG1 
5568 C CG2 . VAL   B 121 ? 0.2166 0.2188 0.1687 -0.0032 -0.0263 0.0096  121 VAL   B CG2 
5578 N N   . LEU   B 122 ? 0.1548 0.1367 0.1551 -0.0240 -0.0248 0.0061  122 LEU   B N   
5579 C CA  . LEU   B 122 ? 0.1474 0.1446 0.1311 -0.0210 -0.0247 0.0064  122 LEU   B CA  
5580 C C   . LEU   B 122 ? 0.1464 0.1292 0.1521 -0.0298 -0.0196 0.0081  122 LEU   B C   
5581 O O   . LEU   B 122 ? 0.1584 0.1323 0.1903 -0.0328 -0.0264 0.0055  122 LEU   B O   
5582 C CB  . LEU   B 122 ? 0.1735 0.1544 0.1763 -0.0057 -0.0288 0.0058  122 LEU   B CB  
5583 C CG  . LEU   B 122 ? 0.1538 0.1583 0.1841 -0.0203 -0.0132 0.0033  122 LEU   B CG  
5584 C CD1 . LEU   B 122 ? 0.1594 0.1837 0.1792 -0.0225 -0.0194 0.0054  122 LEU   B CD1 
5585 C CD2 . LEU   B 122 ? 0.1531 0.1646 0.1644 -0.0086 -0.0106 -0.0019 122 LEU   B CD2 
5597 N N   . LEU   B 123 ? 0.1471 0.1221 0.1490 -0.0253 -0.0190 0.0089  123 LEU   B N   
5598 C CA  . LEU   B 123 ? 0.1470 0.1295 0.1483 -0.0246 -0.0227 0.0002  123 LEU   B CA  
5599 C C   . LEU   B 123 ? 0.1416 0.1278 0.1467 -0.0258 -0.0184 0.0020  123 LEU   B C   
5600 O O   . LEU   B 123 ? 0.1536 0.1294 0.1467 -0.0302 -0.0182 -0.0009 123 LEU   B O   
5601 C CB  . LEU   B 123 ? 0.1543 0.1301 0.1556 -0.0228 -0.0180 -0.0064 123 LEU   B CB  
5602 C CG  . LEU   B 123 ? 0.1499 0.1363 0.1636 -0.0189 -0.0096 0.0031  123 LEU   B CG  
5603 C CD1 . LEU   B 123 ? 0.1590 0.1405 0.1719 -0.0192 0.0018  -0.0060 123 LEU   B CD1 
5604 C CD2 . LEU   B 123 ? 0.1626 0.1466 0.1783 -0.0167 -0.0026 0.0104  123 LEU   B CD2 
5616 N N   . ALA   B 124 ? 0.1374 0.1228 0.1505 -0.0222 -0.0068 0.0007  124 ALA   B N   
5617 C CA  . ALA   B 124 ? 0.1306 0.1194 0.1636 -0.0161 -0.0096 -0.0065 124 ALA   B CA  
5618 C C   . ALA   B 124 ? 0.1293 0.1203 0.1558 -0.0211 -0.0090 -0.0049 124 ALA   B C   
5619 O O   . ALA   B 124 ? 0.1419 0.1232 0.1634 -0.0171 -0.0136 0.0010  124 ALA   B O   
5620 C CB  . ALA   B 124 ? 0.1408 0.1238 0.1662 -0.0098 -0.0017 -0.0016 124 ALA   B CB  
5626 N N   . PRO   B 125 ? 0.1404 0.1229 0.1510 -0.0177 -0.0147 0.0088  125 PRO   B N   
5627 C CA  . PRO   B 125 ? 0.1475 0.1278 0.1709 -0.0139 -0.0162 0.0209  125 PRO   B CA  
5628 C C   . PRO   B 125 ? 0.1437 0.1160 0.1863 -0.0144 -0.0081 0.0066  125 PRO   B C   
5629 O O   . PRO   B 125 ? 0.1394 0.1178 0.2042 -0.0094 -0.0038 0.0172  125 PRO   B O   
5630 C CB  . PRO   B 125 ? 0.1480 0.1533 0.1852 -0.0196 -0.0211 0.0327  125 PRO   B CB  
5631 C CG  . PRO   B 125 ? 0.1582 0.1553 0.1730 -0.0281 -0.0231 0.0160  125 PRO   B CG  
5632 C CD  . PRO   B 125 ? 0.1495 0.1330 0.1538 -0.0294 -0.0111 0.0071  125 PRO   B CD  
5640 N N   . LEU   B 126 ? 0.1443 0.1195 0.2048 -0.0158 0.0118  0.0147  126 LEU   B N   
5641 C CA  . LEU   B 126 ? 0.1533 0.1279 0.2090 -0.0078 0.0221  0.0176  126 LEU   B CA  
5642 C C   . LEU   B 126 ? 0.1490 0.1376 0.2094 0.0019  0.0225  0.0252  126 LEU   B C   
5643 O O   . LEU   B 126 ? 0.1698 0.1647 0.2315 0.0192  -0.0005 -0.0008 126 LEU   B O   
5644 C CB  . LEU   B 126 ? 0.1730 0.1272 0.2424 -0.0172 0.0234  0.0198  126 LEU   B CB  
5645 C CG  . LEU   B 126 ? 0.1849 0.1391 0.2475 -0.0225 0.0208  -0.0065 126 LEU   B CG  
5646 C CD1 . LEU   B 126 ? 0.2005 0.1483 0.2979 -0.0181 0.0169  -0.0163 126 LEU   B CD1 
5647 C CD2 . LEU   B 126 ? 0.1870 0.1493 0.2434 -0.0340 0.0120  -0.0091 126 LEU   B CD2 
5659 N N   . LEU   B 127 ? 0.1475 0.1239 0.2175 0.0003  0.0277  0.0153  127 LEU   B N   
5660 C CA  . LEU   B 127 ? 0.1457 0.1356 0.2223 -0.0038 0.0296  0.0259  127 LEU   B CA  
5661 C C   . LEU   B 127 ? 0.1452 0.1296 0.2227 0.0016  0.0202  0.0270  127 LEU   B C   
5662 O O   . LEU   B 127 ? 0.1463 0.1345 0.2255 -0.0134 0.0157  0.0193  127 LEU   B O   
5663 C CB  . LEU   B 127 ? 0.1608 0.1314 0.2338 -0.0041 0.0216  0.0247  127 LEU   B CB  
5664 C CG  . LEU   B 127 ? 0.1702 0.1307 0.2375 0.0029  0.0245  0.0178  127 LEU   B CG  
5665 C CD1 . LEU   B 127 ? 0.1774 0.1295 0.2337 0.0065  0.0172  0.0133  127 LEU   B CD1 
5666 C CD2 . LEU   B 127 ? 0.1709 0.1421 0.2495 -0.0059 0.0235  0.0281  127 LEU   B CD2 
5678 N N   . SER   B 128 ? 0.1518 0.1259 0.2227 0.0025  0.0052  0.0179  128 SER   B N   
5679 C CA  . SER   B 128 ? 0.1638 0.1372 0.2247 0.0101  0.0003  0.0185  128 SER   B CA  
5680 C C   . SER   B 128 ? 0.1770 0.1405 0.2413 0.0099  -0.0177 0.0228  128 SER   B C   
5681 O O   . SER   B 128 ? 0.1946 0.1424 0.2862 0.0090  -0.0145 0.0315  128 SER   B O   
5682 C CB  . SER   B 128 ? 0.1693 0.1396 0.2162 0.0043  0.0076  0.0373  128 SER   B CB  
5683 O OG  . SER   B 128 ? 0.1728 0.1565 0.2277 0.0102  0.0121  0.0442  128 SER   B OG  
5689 N N   . ALA   B 129 ? 0.1890 0.1469 0.2620 0.0250  -0.0137 0.0077  129 ALA   B N   
5690 C CA  . ALA   B 129 ? 0.2077 0.1511 0.2743 0.0319  -0.0106 -0.0046 129 ALA   B CA  
5691 C C   . ALA   B 129 ? 0.1933 0.1468 0.2536 0.0226  0.0092  0.0047  129 ALA   B C   
5692 O O   . ALA   B 129 ? 0.1823 0.1496 0.2480 0.0177  -0.0077 0.0106  129 ALA   B O   
5693 C CB  . ALA   B 129 ? 0.2289 0.1753 0.3067 0.0391  -0.0029 -0.0102 129 ALA   B CB  
5699 N N   . GLY   B 130 ? 0.1877 0.1440 0.2593 0.0270  0.0164  -0.0019 130 GLY   B N   
5700 C CA  . GLY   B 130 ? 0.1881 0.1498 0.2699 0.0266  0.0384  0.0034  130 GLY   B CA  
5701 C C   . GLY   B 130 ? 0.1957 0.1517 0.2665 0.0204  0.0255  0.0179  130 GLY   B C   
5702 O O   . GLY   B 130 ? 0.2139 0.1672 0.2797 0.0169  0.0154  0.0173  130 GLY   B O   
5706 N N   . ILE   B 131 ? 0.1865 0.1705 0.2775 0.0333  0.0234  0.0144  131 ILE   B N   
5707 C CA  . ILE   B 131 ? 0.2090 0.1865 0.2765 0.0310  0.0119  0.0246  131 ILE   B CA  
5708 C C   . ILE   B 131 ? 0.2194 0.1798 0.2436 0.0244  0.0075  0.0281  131 ILE   B C   
5709 O O   . ILE   B 131 ? 0.2483 0.1964 0.2570 0.0220  -0.0095 0.0286  131 ILE   B O   
5710 C CB  . ILE   B 131 ? 0.2122 0.2178 0.3098 0.0246  0.0032  0.0237  131 ILE   B CB  
5711 C CG1 . ILE   B 131 ? 0.2191 0.2362 0.3214 -0.0041 0.0067  0.0248  131 ILE   B CG1 
5712 C CG2 . ILE   B 131 ? 0.2141 0.2362 0.3324 0.0311  0.0045  0.0145  131 ILE   B CG2 
5713 C CD1 . ILE   B 131 ? 0.2284 0.2566 0.3301 -0.0216 0.0024  0.0320  131 ILE   B CD1 
5725 N N   . PHE   B 132 ? 0.2064 0.1592 0.2277 0.0187  0.0174  0.0300  132 PHE   B N   
5726 C CA  . PHE   B 132 ? 0.2184 0.1650 0.2307 0.0107  0.0434  0.0168  132 PHE   B CA  
5727 C C   . PHE   B 132 ? 0.2353 0.1808 0.2465 0.0095  0.0526  0.0155  132 PHE   B C   
5728 O O   . PHE   B 132 ? 0.2507 0.2033 0.2698 0.0024  0.0700  0.0201  132 PHE   B O   
5729 C CB  . PHE   B 132 ? 0.2025 0.1583 0.2116 0.0140  0.0389  0.0220  132 PHE   B CB  
5730 C CG  . PHE   B 132 ? 0.1944 0.1630 0.2070 0.0188  0.0306  0.0227  132 PHE   B CG  
5731 C CD1 . PHE   B 132 ? 0.2057 0.1656 0.2496 0.0107  0.0333  0.0211  132 PHE   B CD1 
5732 C CD2 . PHE   B 132 ? 0.1922 0.1674 0.2002 0.0231  0.0181  0.0232  132 PHE   B CD2 
5733 C CE1 . PHE   B 132 ? 0.2052 0.1703 0.2607 0.0067  0.0250  0.0203  132 PHE   B CE1 
5734 C CE2 . PHE   B 132 ? 0.2002 0.1733 0.2054 0.0155  0.0052  0.0234  132 PHE   B CE2 
5735 C CZ  . PHE   B 132 ? 0.2041 0.1742 0.2323 0.0096  0.0005  0.0369  132 PHE   B CZ  
5745 N N   . GLY   B 133 ? 0.2357 0.1715 0.2520 0.0026  0.0394  0.0347  133 GLY   B N   
5746 C CA  . GLY   B 133 ? 0.2454 0.1799 0.2652 -0.0148 0.0373  0.0448  133 GLY   B CA  
5747 C C   . GLY   B 133 ? 0.2529 0.1883 0.2734 -0.0312 0.0500  0.0493  133 GLY   B C   
5748 O O   . GLY   B 133 ? 0.2712 0.2016 0.3171 -0.0466 0.0422  0.0580  133 GLY   B O   
5752 N N   . ALA   B 134 ? 0.2352 0.1858 0.2606 -0.0279 0.0534  0.0343  134 ALA   B N   
5753 C CA  . ALA   B 134 ? 0.2288 0.1795 0.2587 -0.0212 0.0547  0.0210  134 ALA   B CA  
5754 C C   . ALA   B 134 ? 0.2361 0.1701 0.2687 -0.0123 0.0501  0.0329  134 ALA   B C   
5755 O O   . ALA   B 134 ? 0.2426 0.1904 0.2898 0.0000  0.0387  0.0252  134 ALA   B O   
5756 C CB  . ALA   B 134 ? 0.2280 0.1790 0.2754 -0.0124 0.0433  0.0110  134 ALA   B CB  
5762 N N   . ASP   B 135 ? 0.2485 0.1688 0.2689 -0.0151 0.0301  0.0427  135 ASP   B N   
5763 C CA  . ASP   B 135 ? 0.2648 0.1601 0.2926 -0.0127 0.0079  0.0424  135 ASP   B CA  
5764 C C   . ASP   B 135 ? 0.2398 0.1469 0.2774 -0.0053 0.0086  0.0380  135 ASP   B C   
5765 O O   . ASP   B 135 ? 0.2291 0.1481 0.2863 -0.0038 0.0147  0.0374  135 ASP   B O   
5766 C CB  . ASP   B 135 ? 0.2980 0.1724 0.3066 -0.0365 0.0047  0.0421  135 ASP   B CB  
5767 C CG  . ASP   B 135 ? 0.3301 0.1711 0.3472 -0.0554 0.0019  0.0348  135 ASP   B CG  
5768 O OD1 . ASP   B 135 ? 0.3366 0.1563 0.3414 -0.0387 -0.0008 0.0323  135 ASP   B OD1 
5769 O OD2 . ASP   B 135 ? 0.3554 0.2083 0.4061 -0.0695 -0.0040 0.0100  135 ASP   B OD2 
5774 N N   . PRO   B 136 ? 0.2296 0.1514 0.2866 0.0193  -0.0118 0.0301  136 PRO   B N   
5775 C CA  . PRO   B 136 ? 0.2056 0.1459 0.2888 0.0190  -0.0086 0.0152  136 PRO   B CA  
5776 C C   . PRO   B 136 ? 0.1849 0.1313 0.2889 0.0136  -0.0047 0.0121  136 PRO   B C   
5777 O O   . PRO   B 136 ? 0.1629 0.1283 0.2845 0.0058  -0.0001 0.0120  136 PRO   B O   
5778 C CB  . PRO   B 136 ? 0.2124 0.1715 0.3018 0.0304  -0.0112 0.0041  136 PRO   B CB  
5779 C CG  . PRO   B 136 ? 0.2352 0.1757 0.3206 0.0340  -0.0071 0.0107  136 PRO   B CG  
5780 C CD  . PRO   B 136 ? 0.2375 0.1648 0.3020 0.0390  -0.0106 0.0179  136 PRO   B CD  
5788 N N   . ILE   B 137 ? 0.1974 0.1258 0.2934 0.0140  -0.0077 0.0100  137 ILE   B N   
5789 C CA  . ILE   B 137 ? 0.2033 0.1213 0.3141 -0.0028 -0.0069 0.0099  137 ILE   B CA  
5790 C C   . ILE   B 137 ? 0.1905 0.1308 0.3050 -0.0043 0.0039  0.0132  137 ILE   B C   
5791 O O   . ILE   B 137 ? 0.1778 0.1340 0.2952 -0.0096 0.0078  0.0112  137 ILE   B O   
5792 C CB  . ILE   B 137 ? 0.2291 0.1337 0.3559 -0.0050 -0.0020 0.0130  137 ILE   B CB  
5793 C CG1 . ILE   B 137 ? 0.2571 0.1469 0.4034 -0.0021 -0.0009 -0.0011 137 ILE   B CG1 
5794 C CG2 . ILE   B 137 ? 0.2366 0.1381 0.3656 -0.0309 -0.0006 0.0125  137 ILE   B CG2 
5795 C CD1 . ILE   B 137 ? 0.2830 0.1756 0.4410 0.0121  -0.0017 0.0055  137 ILE   B CD1 
5807 N N   . HIS   B 138 ? 0.1948 0.1270 0.3003 -0.0044 0.0137  0.0183  138 HIS   B N   
5808 C CA  . HIS   B 138 ? 0.2051 0.1374 0.2993 -0.0048 0.0290  0.0170  138 HIS   B CA  
5809 C C   . HIS   B 138 ? 0.1880 0.1337 0.2877 -0.0069 0.0288  0.0278  138 HIS   B C   
5810 O O   . HIS   B 138 ? 0.1840 0.1432 0.3094 -0.0035 0.0295  0.0381  138 HIS   B O   
5811 C CB  . HIS   B 138 ? 0.2386 0.1445 0.3153 -0.0086 0.0504  0.0212  138 HIS   B CB  
5812 C CG  . HIS   B 138 ? 0.2622 0.1641 0.3170 -0.0075 0.0689  0.0462  138 HIS   B CG  
5813 N ND1 . HIS   B 138 ? 0.2675 0.1844 0.3434 -0.0074 0.0858  0.0380  138 HIS   B ND1 
5814 C CD2 . HIS   B 138 ? 0.2796 0.1781 0.3094 -0.0072 0.0810  0.0349  138 HIS   B CD2 
5815 C CE1 . HIS   B 138 ? 0.2759 0.1848 0.3352 -0.0066 0.0901  0.0383  138 HIS   B CE1 
5816 N NE2 . HIS   B 138 ? 0.2854 0.1740 0.3100 0.0006  0.0855  0.0218  138 HIS   B NE2 
5824 N N   . SER   B 139 ? 0.1806 0.1271 0.2826 0.0010  0.0280  0.0168  139 SER   B N   
5825 C CA  . SER   B 139 ? 0.1786 0.1215 0.2660 0.0002  0.0226  0.0076  139 SER   B CA  
5826 C C   . SER   B 139 ? 0.1532 0.1120 0.2639 -0.0065 0.0215  0.0045  139 SER   B C   
5827 O O   . SER   B 139 ? 0.1562 0.1196 0.2697 -0.0060 0.0086  0.0100  139 SER   B O   
5828 C CB  . SER   B 139 ? 0.1845 0.1179 0.2665 0.0010  0.0092  0.0072  139 SER   B CB  
5829 O OG  . SER   B 139 ? 0.1829 0.1242 0.2664 -0.0016 -0.0084 0.0189  139 SER   B OG  
5835 N N   . LEU   B 140 ? 0.1559 0.1086 0.2720 -0.0083 0.0243  -0.0061 140 LEU   B N   
5836 C CA  . LEU   B 140 ? 0.1541 0.1162 0.2672 -0.0078 0.0159  0.0060  140 LEU   B CA  
5837 C C   . LEU   B 140 ? 0.1501 0.1185 0.2754 -0.0081 0.0066  0.0008  140 LEU   B C   
5838 O O   . LEU   B 140 ? 0.1451 0.1261 0.2583 -0.0060 0.0034  0.0058  140 LEU   B O   
5839 C CB  . LEU   B 140 ? 0.1531 0.1150 0.2678 -0.0153 0.0201  0.0031  140 LEU   B CB  
5840 C CG  . LEU   B 140 ? 0.1598 0.1211 0.2626 -0.0113 0.0012  0.0129  140 LEU   B CG  
5841 C CD1 . LEU   B 140 ? 0.1684 0.1381 0.2875 -0.0136 0.0119  0.0066  140 LEU   B CD1 
5842 C CD2 . LEU   B 140 ? 0.1801 0.1277 0.2724 -0.0123 -0.0061 -0.0079 140 LEU   B CD2 
5854 N N   . ARG   B 141 ? 0.1471 0.1191 0.2919 -0.0121 0.0161  0.0019  141 ARG   B N   
5855 C CA  . ARG   B 141 ? 0.1458 0.1177 0.3270 -0.0145 0.0263  0.0001  141 ARG   B CA  
5856 C C   . ARG   B 141 ? 0.1425 0.1233 0.3132 -0.0127 0.0106  0.0030  141 ARG   B C   
5857 O O   . ARG   B 141 ? 0.1471 0.1249 0.3023 -0.0166 0.0028  -0.0086 141 ARG   B O   
5858 C CB  . ARG   B 141 ? 0.1596 0.1310 0.3465 -0.0228 0.0303  -0.0004 141 ARG   B CB  
5859 C CG  . ARG   B 141 ? 0.1925 0.1596 0.3560 -0.0330 0.0313  -0.0056 141 ARG   B CG  
5860 C CD  . ARG   B 141 ? 0.2404 0.1907 0.3516 -0.0261 0.0135  -0.0190 141 ARG   B CD  
5861 N NE  . ARG   B 141 ? 0.2641 0.1878 0.3387 -0.0409 0.0242  -0.0159 141 ARG   B NE  
5862 C CZ  . ARG   B 141 ? 0.2837 0.1699 0.3127 -0.0369 0.0273  -0.0243 141 ARG   B CZ  
5863 N NH1 . ARG   B 141 ? 0.2941 0.1617 0.3043 -0.0309 0.0247  -0.0171 141 ARG   B NH1 
5864 N NH2 . ARG   B 141 ? 0.2985 0.1785 0.3210 -0.0191 0.0132  -0.0215 141 ARG   B NH2 
5878 N N   . VAL   B 142 ? 0.1503 0.1160 0.2951 -0.0097 0.0105  -0.0021 142 VAL   B N   
5879 C CA  . VAL   B 142 ? 0.1418 0.1192 0.2775 -0.0034 0.0180  0.0014  142 VAL   B CA  
5880 C C   . VAL   B 142 ? 0.1376 0.1184 0.2806 -0.0097 0.0083  0.0014  142 VAL   B C   
5881 O O   . VAL   B 142 ? 0.1468 0.1156 0.2931 -0.0018 0.0159  0.0014  142 VAL   B O   
5882 C CB  . VAL   B 142 ? 0.1583 0.1333 0.2785 -0.0008 0.0275  0.0119  142 VAL   B CB  
5883 C CG1 . VAL   B 142 ? 0.1534 0.1335 0.2721 0.0044  0.0290  0.0096  142 VAL   B CG1 
5884 C CG2 . VAL   B 142 ? 0.1843 0.1316 0.2859 0.0056  0.0247  0.0148  142 VAL   B CG2 
5894 N N   . CYS   B 143 ? 0.1356 0.1217 0.2608 -0.0051 0.0069  0.0153  143 CYS   B N   
5895 C CA  . CYS   B 143 ? 0.1312 0.1192 0.2573 -0.0039 0.0101  0.0045  143 CYS   B CA  
5896 C C   . CYS   B 143 ? 0.1310 0.1217 0.2655 -0.0068 0.0074  -0.0027 143 CYS   B C   
5897 O O   . CYS   B 143 ? 0.1296 0.1263 0.2713 -0.0072 -0.0021 0.0004  143 CYS   B O   
5898 C CB  . CYS   B 143 ? 0.1434 0.1268 0.2485 -0.0107 0.0001  0.0017  143 CYS   B CB  
5899 S SG  . CYS   B 143 ? 0.1442 0.1426 0.2478 -0.0063 0.0050  0.0036  143 CYS   B SG  
5905 N N   . VAL   B 144 ? 0.1393 0.1195 0.2889 -0.0091 -0.0014 -0.0174 144 VAL   B N   
5906 C CA  . VAL   B 144 ? 0.1449 0.1334 0.3122 -0.0200 -0.0121 -0.0209 144 VAL   B CA  
5907 C C   . VAL   B 144 ? 0.1391 0.1306 0.3073 -0.0142 -0.0106 -0.0027 144 VAL   B C   
5908 O O   . VAL   B 144 ? 0.1505 0.1521 0.3197 -0.0029 -0.0114 0.0149  144 VAL   B O   
5909 C CB  . VAL   B 144 ? 0.1732 0.1468 0.3536 -0.0160 -0.0168 -0.0363 144 VAL   B CB  
5910 C CG1 . VAL   B 144 ? 0.1979 0.1876 0.3836 -0.0086 -0.0244 -0.0266 144 VAL   B CG1 
5911 C CG2 . VAL   B 144 ? 0.1904 0.1467 0.3405 -0.0036 -0.0364 -0.0505 144 VAL   B CG2 
5921 N N   . ASP   B 145 ? 0.1417 0.1284 0.3209 -0.0125 0.0002  -0.0134 145 ASP   B N   
5922 C CA  . ASP   B 145 ? 0.1389 0.1261 0.3443 -0.0088 0.0031  -0.0089 145 ASP   B CA  
5923 C C   . ASP   B 145 ? 0.1356 0.1387 0.3311 -0.0097 0.0002  -0.0029 145 ASP   B C   
5924 O O   . ASP   B 145 ? 0.1342 0.1510 0.3863 -0.0151 0.0055  -0.0245 145 ASP   B O   
5925 C CB  . ASP   B 145 ? 0.1522 0.1369 0.3805 -0.0193 0.0177  0.0061  145 ASP   B CB  
5926 C CG  . ASP   B 145 ? 0.1705 0.1445 0.4268 -0.0251 0.0270  0.0041  145 ASP   B CG  
5927 O OD1 . ASP   B 145 ? 0.1724 0.1479 0.4322 -0.0317 -0.0082 -0.0099 145 ASP   B OD1 
5928 O OD2 . ASP   B 145 ? 0.1966 0.1520 0.4642 -0.0338 0.0467  0.0103  145 ASP   B OD2 
5933 N N   . THR   B 146 ? 0.1297 0.1238 0.2808 -0.0108 -0.0032 0.0068  146 THR   B N   
5934 C CA  . THR   B 146 ? 0.1370 0.1226 0.2596 -0.0040 0.0054  0.0042  146 THR   B CA  
5935 C C   . THR   B 146 ? 0.1394 0.1235 0.2458 -0.0057 -0.0019 0.0064  146 THR   B C   
5936 O O   . THR   B 146 ? 0.1431 0.1225 0.2564 -0.0093 -0.0052 0.0038  146 THR   B O   
5937 C CB  . THR   B 146 ? 0.1400 0.1239 0.2687 -0.0056 0.0180  0.0086  146 THR   B CB  
5938 O OG1 . THR   B 146 ? 0.1431 0.1242 0.2685 -0.0070 0.0151  0.0137  146 THR   B OG1 
5939 C CG2 . THR   B 146 ? 0.1503 0.1289 0.2582 -0.0033 0.0099  -0.0011 146 THR   B CG2 
5947 N N   . VAL   B 147 ? 0.1436 0.1260 0.2304 -0.0082 0.0120  0.0000  147 VAL   B N   
5948 C CA  . VAL   B 147 ? 0.1412 0.1201 0.2312 -0.0122 -0.0018 0.0025  147 VAL   B CA  
5949 C C   . VAL   B 147 ? 0.1398 0.1229 0.2374 -0.0172 -0.0162 -0.0066 147 VAL   B C   
5950 O O   . VAL   B 147 ? 0.1512 0.1359 0.2468 -0.0174 -0.0337 -0.0062 147 VAL   B O   
5951 C CB  . VAL   B 147 ? 0.1420 0.1315 0.2150 -0.0093 -0.0052 0.0012  147 VAL   B CB  
5952 C CG1 . VAL   B 147 ? 0.1434 0.1459 0.2060 -0.0125 -0.0084 0.0003  147 VAL   B CG1 
5953 C CG2 . VAL   B 147 ? 0.1474 0.1302 0.2198 -0.0130 -0.0002 -0.0033 147 VAL   B CG2 
5963 N N   . ARG   B 148 ? 0.1417 0.1297 0.2373 -0.0103 -0.0211 -0.0127 148 ARG   B N   
5964 C CA  . ARG   B 148 ? 0.1403 0.1408 0.2322 -0.0071 -0.0275 -0.0130 148 ARG   B CA  
5965 C C   . ARG   B 148 ? 0.1479 0.1475 0.2220 -0.0091 -0.0284 -0.0027 148 ARG   B C   
5966 O O   . ARG   B 148 ? 0.1750 0.1757 0.2240 -0.0288 -0.0407 0.0037  148 ARG   B O   
5967 C CB  . ARG   B 148 ? 0.1454 0.1459 0.2280 0.0002  -0.0315 -0.0168 148 ARG   B CB  
5968 C CG  . ARG   B 148 ? 0.1480 0.1624 0.2454 -0.0083 -0.0258 -0.0281 148 ARG   B CG  
5969 C CD  . ARG   B 148 ? 0.1576 0.1786 0.2613 0.0063  -0.0283 -0.0355 148 ARG   B CD  
5970 N NE  . ARG   B 148 ? 0.1593 0.1738 0.2513 0.0209  -0.0277 -0.0325 148 ARG   B NE  
5971 C CZ  . ARG   B 148 ? 0.1548 0.1612 0.2405 0.0184  -0.0219 -0.0279 148 ARG   B CZ  
5972 N NH1 . ARG   B 148 ? 0.1426 0.1684 0.2533 0.0040  -0.0117 -0.0293 148 ARG   B NH1 
5973 N NH2 . ARG   B 148 ? 0.1758 0.1450 0.2342 0.0180  -0.0233 -0.0114 148 ARG   B NH2 
5987 N N   . THR   B 149 ? 0.1476 0.1363 0.2227 -0.0121 -0.0305 0.0068  149 THR   B N   
5988 C CA  . THR   B 149 ? 0.1517 0.1392 0.2075 -0.0181 -0.0327 0.0091  149 THR   B CA  
5989 C C   . THR   B 149 ? 0.1519 0.1359 0.1975 -0.0160 -0.0331 0.0063  149 THR   B C   
5990 O O   . THR   B 149 ? 0.1637 0.1393 0.2036 -0.0243 -0.0167 0.0016  149 THR   B O   
5991 C CB  . THR   B 149 ? 0.1560 0.1373 0.2153 -0.0205 -0.0290 0.0028  149 THR   B CB  
5992 O OG1 . THR   B 149 ? 0.1606 0.1437 0.2003 -0.0233 -0.0350 0.0027  149 THR   B OG1 
5993 C CG2 . THR   B 149 ? 0.1693 0.1422 0.2318 -0.0112 -0.0276 -0.0012 149 THR   B CG2 
6001 N N   . ASN   B 150 ? 0.1648 0.1359 0.1969 -0.0169 -0.0354 -0.0015 150 ASN   B N   
6002 C CA  . ASN   B 150 ? 0.1682 0.1486 0.1905 -0.0252 -0.0313 -0.0046 150 ASN   B CA  
6003 C C   . ASN   B 150 ? 0.1601 0.1456 0.1898 -0.0139 -0.0293 -0.0038 150 ASN   B C   
6004 O O   . ASN   B 150 ? 0.1690 0.1433 0.2090 -0.0286 -0.0469 -0.0025 150 ASN   B O   
6005 C CB  . ASN   B 150 ? 0.1930 0.1929 0.2064 -0.0286 -0.0448 0.0121  150 ASN   B CB  
6006 C CG  . ASN   B 150 ? 0.2239 0.2311 0.2431 -0.0263 -0.0504 0.0305  150 ASN   B CG  
6007 O OD1 . ASN   B 150 ? 0.2340 0.2453 0.2564 -0.0371 -0.0657 0.0236  150 ASN   B OD1 
6008 N ND2 . ASN   B 150 ? 0.2393 0.2520 0.2795 -0.0155 -0.0579 0.0726  150 ASN   B ND2 
6015 N N   . VAL   B 151 ? 0.1516 0.1422 0.1867 -0.0215 -0.0322 0.0040  151 VAL   B N   
6016 C CA  . VAL   B 151 ? 0.1529 0.1408 0.1880 -0.0284 -0.0229 0.0003  151 VAL   B CA  
6017 C C   . VAL   B 151 ? 0.1552 0.1387 0.1844 -0.0309 -0.0275 -0.0061 151 VAL   B C   
6018 O O   . VAL   B 151 ? 0.1647 0.1511 0.2027 -0.0297 -0.0160 -0.0131 151 VAL   B O   
6019 C CB  . VAL   B 151 ? 0.1715 0.1529 0.2039 -0.0140 -0.0167 -0.0005 151 VAL   B CB  
6020 C CG1 . VAL   B 151 ? 0.1799 0.1624 0.2232 -0.0209 -0.0102 -0.0052 151 VAL   B CG1 
6021 C CG2 . VAL   B 151 ? 0.1877 0.1722 0.1842 0.0001  -0.0151 0.0103  151 VAL   B CG2 
6031 N N   . TYR   B 152 ? 0.1495 0.1281 0.1766 -0.0234 -0.0257 -0.0010 152 TYR   B N   
6032 C CA  . TYR   B 152 ? 0.1568 0.1494 0.1665 -0.0330 -0.0184 -0.0024 152 TYR   B CA  
6033 C C   . TYR   B 152 ? 0.1541 0.1312 0.1574 -0.0277 -0.0126 -0.0106 152 TYR   B C   
6034 O O   . TYR   B 152 ? 0.1648 0.1341 0.1743 -0.0280 -0.0125 -0.0042 152 TYR   B O   
6035 C CB  . TYR   B 152 ? 0.1690 0.1599 0.1753 -0.0315 -0.0113 0.0068  152 TYR   B CB  
6036 C CG  . TYR   B 152 ? 0.1864 0.1704 0.1750 -0.0449 -0.0168 0.0031  152 TYR   B CG  
6037 C CD1 . TYR   B 152 ? 0.2007 0.1847 0.1650 -0.0385 -0.0276 0.0097  152 TYR   B CD1 
6038 C CD2 . TYR   B 152 ? 0.2119 0.1895 0.1768 -0.0428 -0.0117 -0.0021 152 TYR   B CD2 
6039 C CE1 . TYR   B 152 ? 0.2200 0.2052 0.1849 -0.0297 -0.0341 0.0215  152 TYR   B CE1 
6040 C CE2 . TYR   B 152 ? 0.2280 0.2140 0.1830 -0.0375 -0.0190 -0.0048 152 TYR   B CE2 
6041 C CZ  . TYR   B 152 ? 0.2313 0.2276 0.1709 -0.0346 -0.0473 0.0199  152 TYR   B CZ  
6042 O OH  . TYR   B 152 ? 0.2574 0.2632 0.2045 -0.0289 -0.0477 0.0205  152 TYR   B OH  
6052 N N   . LEU   B 153 ? 0.1519 0.1280 0.1741 -0.0310 -0.0119 -0.0070 153 LEU   B N   
6053 C CA  . LEU   B 153 ? 0.1582 0.1228 0.1635 -0.0221 -0.0030 -0.0092 153 LEU   B CA  
6054 C C   . LEU   B 153 ? 0.1570 0.1227 0.1770 -0.0270 -0.0053 -0.0138 153 LEU   B C   
6055 O O   . LEU   B 153 ? 0.1690 0.1482 0.1916 -0.0190 -0.0128 -0.0357 153 LEU   B O   
6056 C CB  . LEU   B 153 ? 0.1576 0.1286 0.1846 -0.0286 -0.0055 -0.0062 153 LEU   B CB  
6057 C CG  . LEU   B 153 ? 0.1493 0.1344 0.2158 -0.0243 -0.0054 -0.0039 153 LEU   B CG  
6058 C CD1 . LEU   B 153 ? 0.1582 0.1500 0.2250 -0.0270 0.0004  0.0061  153 LEU   B CD1 
6059 C CD2 . LEU   B 153 ? 0.1516 0.1441 0.2170 -0.0242 0.0076  0.0040  153 LEU   B CD2 
6071 N N   . ALA   B 154 ? 0.1505 0.1221 0.1887 -0.0103 -0.0118 -0.0112 154 ALA   B N   
6072 C CA  . ALA   B 154 ? 0.1605 0.1388 0.2028 -0.0042 -0.0157 -0.0224 154 ALA   B CA  
6073 C C   . ALA   B 154 ? 0.1738 0.1438 0.2134 0.0012  -0.0235 -0.0223 154 ALA   B C   
6074 O O   . ALA   B 154 ? 0.2078 0.1402 0.2347 0.0049  -0.0131 -0.0032 154 ALA   B O   
6075 C CB  . ALA   B 154 ? 0.1566 0.1609 0.2243 -0.0057 -0.0113 -0.0290 154 ALA   B CB  
6081 N N   . VAL   B 155 ? 0.1450 0.1329 0.2282 -0.0021 -0.0038 -0.0178 155 VAL   B N   
6082 C CA  . VAL   B 155 ? 0.1353 0.1282 0.2392 -0.0024 -0.0104 -0.0080 155 VAL   B CA  
6083 C C   . VAL   B 155 ? 0.1402 0.1299 0.2400 -0.0082 -0.0112 -0.0249 155 VAL   B C   
6084 O O   . VAL   B 155 ? 0.1607 0.1526 0.2731 0.0064  -0.0089 -0.0438 155 VAL   B O   
6085 C CB  . VAL   B 155 ? 0.1400 0.1473 0.2803 -0.0079 -0.0156 0.0005  155 VAL   B CB  
6086 C CG1 . VAL   B 155 ? 0.1482 0.1449 0.2743 -0.0105 -0.0145 0.0028  155 VAL   B CG1 
6087 C CG2 . VAL   B 155 ? 0.1365 0.1600 0.3049 -0.0100 -0.0177 0.0218  155 VAL   B CG2 
6097 N N   . PHE   B 156 ? 0.1312 0.1414 0.2655 0.0009  -0.0082 -0.0188 156 PHE   B N   
6098 C CA  . PHE   B 156 ? 0.1354 0.1461 0.2937 0.0054  -0.0068 -0.0193 156 PHE   B CA  
6099 C C   . PHE   B 156 ? 0.1393 0.1573 0.3253 0.0079  -0.0134 -0.0382 156 PHE   B C   
6100 O O   . PHE   B 156 ? 0.1638 0.1809 0.3468 0.0214  -0.0004 -0.0473 156 PHE   B O   
6101 C CB  . PHE   B 156 ? 0.1447 0.1479 0.2920 0.0015  -0.0131 -0.0133 156 PHE   B CB  
6102 C CG  . PHE   B 156 ? 0.1461 0.1591 0.3049 0.0022  -0.0099 0.0055  156 PHE   B CG  
6103 C CD1 . PHE   B 156 ? 0.1487 0.1843 0.3242 0.0039  -0.0012 0.0331  156 PHE   B CD1 
6104 C CD2 . PHE   B 156 ? 0.1552 0.1689 0.2970 0.0098  -0.0147 0.0094  156 PHE   B CD2 
6105 C CE1 . PHE   B 156 ? 0.1543 0.1992 0.3308 0.0046  -0.0002 0.0379  156 PHE   B CE1 
6106 C CE2 . PHE   B 156 ? 0.1622 0.1901 0.3080 0.0129  -0.0095 0.0129  156 PHE   B CE2 
6107 C CZ  . PHE   B 156 ? 0.1516 0.1967 0.3262 0.0138  -0.0160 0.0218  156 PHE   B CZ  
6117 N N   . ASP   B 157 ? 0.1375 0.1432 0.3525 0.0087  -0.0210 -0.0196 157 ASP   B N   
6118 C CA  . ASP   B 157 ? 0.1538 0.1508 0.3706 0.0107  -0.0290 -0.0240 157 ASP   B CA  
6119 C C   . ASP   B 157 ? 0.1567 0.1484 0.3823 0.0102  -0.0253 -0.0434 157 ASP   B C   
6120 O O   . ASP   B 157 ? 0.1451 0.1502 0.3705 0.0051  -0.0223 -0.0333 157 ASP   B O   
6121 C CB  . ASP   B 157 ? 0.1856 0.1714 0.3754 0.0086  -0.0509 -0.0066 157 ASP   B CB  
6122 C CG  . ASP   B 157 ? 0.2301 0.1840 0.3972 0.0051  -0.0496 -0.0140 157 ASP   B CG  
6123 O OD1 . ASP   B 157 ? 0.2386 0.1755 0.4168 0.0126  -0.0396 -0.0160 157 ASP   B OD1 
6124 O OD2 . ASP   B 157 ? 0.2668 0.2034 0.4171 0.0039  -0.0300 -0.0112 157 ASP   B OD2 
6129 N N   . LYS   B 158 ? 0.1593 0.1798 0.3935 0.0058  -0.0157 -0.0738 158 LYS   B N   
6130 C CA  . LYS   B 158 ? 0.1800 0.1993 0.4000 0.0063  -0.0036 -0.1012 158 LYS   B CA  
6131 C C   . LYS   B 158 ? 0.1753 0.1847 0.4109 0.0094  -0.0140 -0.0861 158 LYS   B C   
6132 O O   . LYS   B 158 ? 0.1778 0.1839 0.4186 -0.0030 -0.0132 -0.0935 158 LYS   B O   
6133 C CB  . LYS   B 158 ? 0.2102 0.2468 0.3983 0.0059  0.0055  -0.1295 158 LYS   B CB  
6134 C CG  . LYS   B 158 ? 0.2483 0.2971 0.4061 0.0109  0.0183  -0.1419 158 LYS   B CG  
6135 C CD  . LYS   B 158 ? 0.2775 0.3519 0.4263 0.0117  0.0243  -0.1364 158 LYS   B CD  
6136 C CE  . LYS   B 158 ? 0.3016 0.3924 0.4383 0.0151  0.0228  -0.1324 158 LYS   B CE  
6137 N NZ  . LYS   B 158 ? 0.2975 0.4121 0.4366 0.0149  0.0261  -0.1325 158 LYS   B NZ  
6151 N N   . ASN   B 159 ? 0.1738 0.1747 0.4295 0.0079  -0.0246 -0.0681 159 ASN   B N   
6152 C CA  . ASN   B 159 ? 0.1897 0.1664 0.4457 0.0194  -0.0395 -0.0563 159 ASN   B CA  
6153 C C   . ASN   B 159 ? 0.1750 0.1468 0.4356 0.0174  -0.0512 -0.0471 159 ASN   B C   
6154 O O   . ASN   B 159 ? 0.1796 0.1454 0.4576 -0.0005 -0.0628 -0.0342 159 ASN   B O   
6155 C CB  . ASN   B 159 ? 0.2142 0.1822 0.4662 0.0291  -0.0484 -0.0499 159 ASN   B CB  
6156 C CG  . ASN   B 159 ? 0.2424 0.2044 0.4857 0.0315  -0.0655 -0.0618 159 ASN   B CG  
6157 O OD1 . ASN   B 159 ? 0.2565 0.2156 0.4912 0.0423  -0.0607 -0.0687 159 ASN   B OD1 
6158 N ND2 . ASN   B 159 ? 0.2391 0.2168 0.4999 0.0355  -0.0703 -0.0608 159 ASN   B ND2 
6165 N N   . LEU   B 160 ? 0.1616 0.1482 0.4138 0.0116  -0.0475 -0.0410 160 LEU   B N   
6166 C CA  . LEU   B 160 ? 0.1591 0.1530 0.3723 0.0093  -0.0418 -0.0257 160 LEU   B CA  
6167 C C   . LEU   B 160 ? 0.1525 0.1441 0.3631 -0.0011 -0.0266 -0.0309 160 LEU   B C   
6168 O O   . LEU   B 160 ? 0.1396 0.1484 0.3613 -0.0052 -0.0273 -0.0181 160 LEU   B O   
6169 C CB  . LEU   B 160 ? 0.1497 0.1628 0.3502 0.0046  -0.0403 -0.0138 160 LEU   B CB  
6170 C CG  . LEU   B 160 ? 0.1545 0.1754 0.3217 0.0068  -0.0342 -0.0004 160 LEU   B CG  
6171 C CD1 . LEU   B 160 ? 0.1695 0.1876 0.3255 0.0025  -0.0142 -0.0029 160 LEU   B CD1 
6172 C CD2 . LEU   B 160 ? 0.1594 0.1810 0.3146 0.0205  -0.0267 -0.0087 160 LEU   B CD2 
6184 N N   . TYR   B 161 ? 0.1500 0.1450 0.3573 -0.0097 -0.0003 -0.0435 161 TYR   B N   
6185 C CA  . TYR   B 161 ? 0.1591 0.1502 0.3357 -0.0180 0.0148  -0.0422 161 TYR   B CA  
6186 C C   . TYR   B 161 ? 0.1609 0.1458 0.3312 -0.0113 0.0205  -0.0425 161 TYR   B C   
6187 O O   . TYR   B 161 ? 0.1637 0.1486 0.3279 -0.0214 0.0105  -0.0398 161 TYR   B O   
6188 C CB  . TYR   B 161 ? 0.1779 0.1597 0.3310 -0.0276 0.0310  -0.0510 161 TYR   B CB  
6189 C CG  . TYR   B 161 ? 0.2049 0.1581 0.3256 -0.0344 0.0411  -0.0569 161 TYR   B CG  
6190 C CD1 . TYR   B 161 ? 0.2147 0.1582 0.3243 -0.0450 0.0444  -0.0531 161 TYR   B CD1 
6191 C CD2 . TYR   B 161 ? 0.2273 0.1636 0.3132 -0.0278 0.0377  -0.0588 161 TYR   B CD2 
6192 C CE1 . TYR   B 161 ? 0.2295 0.1782 0.3213 -0.0488 0.0478  -0.0503 161 TYR   B CE1 
6193 C CE2 . TYR   B 161 ? 0.2484 0.1824 0.3206 -0.0351 0.0372  -0.0511 161 TYR   B CE2 
6194 C CZ  . TYR   B 161 ? 0.2488 0.1889 0.3163 -0.0510 0.0322  -0.0452 161 TYR   B CZ  
6195 O OH  . TYR   B 161 ? 0.2781 0.2173 0.3355 -0.0518 0.0249  -0.0456 161 TYR   B OH  
6205 N N   . ASP   B 162 ? 0.1672 0.1455 0.3506 -0.0104 0.0053  -0.0566 162 ASP   B N   
6206 C CA  . ASP   B 162 ? 0.1776 0.1506 0.3487 -0.0123 -0.0017 -0.0506 162 ASP   B CA  
6207 C C   . ASP   B 162 ? 0.1702 0.1410 0.3390 -0.0150 -0.0120 -0.0444 162 ASP   B C   
6208 O O   . ASP   B 162 ? 0.1761 0.1474 0.3404 -0.0175 -0.0231 -0.0288 162 ASP   B O   
6209 C CB  . ASP   B 162 ? 0.1998 0.1675 0.3723 -0.0032 -0.0050 -0.0688 162 ASP   B CB  
6210 C CG  . ASP   B 162 ? 0.2047 0.1939 0.3967 0.0055  -0.0059 -0.0839 162 ASP   B CG  
6211 O OD1 . ASP   B 162 ? 0.2014 0.2188 0.3846 -0.0058 0.0128  -0.0773 162 ASP   B OD1 
6212 O OD2 . ASP   B 162 ? 0.2219 0.2152 0.4210 0.0268  -0.0078 -0.0847 162 ASP   B OD2 
6217 N N   . LYS   B 163 ? 0.1694 0.1319 0.3342 -0.0187 -0.0260 -0.0335 163 LYS   B N   
6218 C CA  . LYS   B 163 ? 0.1799 0.1405 0.3427 -0.0215 -0.0204 -0.0116 163 LYS   B CA  
6219 C C   . LYS   B 163 ? 0.1510 0.1359 0.3351 -0.0170 -0.0192 -0.0015 163 LYS   B C   
6220 O O   . LYS   B 163 ? 0.1542 0.1433 0.3625 -0.0248 -0.0170 0.0080  163 LYS   B O   
6221 C CB  . LYS   B 163 ? 0.2233 0.1774 0.3823 -0.0102 -0.0249 0.0056  163 LYS   B CB  
6222 C CG  . LYS   B 163 ? 0.3031 0.2652 0.4439 -0.0178 -0.0116 0.0128  163 LYS   B CG  
6223 C CD  . LYS   B 163 ? 0.3785 0.3392 0.5079 -0.0286 -0.0072 0.0152  163 LYS   B CD  
6224 C CE  . LYS   B 163 ? 0.4396 0.4068 0.5499 -0.0366 -0.0003 0.0197  163 LYS   B CE  
6225 N NZ  . LYS   B 163 ? 0.4698 0.4356 0.5771 -0.0408 0.0030  0.0178  163 LYS   B NZ  
6239 N N   . LEU   B 164 ? 0.1409 0.1328 0.3091 -0.0117 -0.0120 0.0007  164 LEU   B N   
6240 C CA  . LEU   B 164 ? 0.1438 0.1355 0.2897 -0.0108 -0.0220 -0.0032 164 LEU   B CA  
6241 C C   . LEU   B 164 ? 0.1553 0.1344 0.2862 -0.0206 -0.0302 0.0059  164 LEU   B C   
6242 O O   . LEU   B 164 ? 0.1587 0.1566 0.3099 -0.0193 -0.0314 0.0043  164 LEU   B O   
6243 C CB  . LEU   B 164 ? 0.1438 0.1309 0.2753 -0.0109 -0.0163 0.0002  164 LEU   B CB  
6244 C CG  . LEU   B 164 ? 0.1528 0.1433 0.2818 -0.0128 -0.0040 0.0044  164 LEU   B CG  
6245 C CD1 . LEU   B 164 ? 0.1583 0.1409 0.2813 -0.0115 -0.0160 -0.0121 164 LEU   B CD1 
6246 C CD2 . LEU   B 164 ? 0.1690 0.1811 0.2965 -0.0131 0.0063  -0.0071 164 LEU   B CD2 
6258 N N   . VAL   B 165 ? 0.1905 0.1407 0.3064 -0.0283 -0.0333 -0.0033 165 VAL   B N   
6259 C CA  . VAL   B 165 ? 0.2222 0.1500 0.3114 -0.0366 -0.0562 -0.0029 165 VAL   B CA  
6260 C C   . VAL   B 165 ? 0.2530 0.1652 0.3363 -0.0423 -0.0811 0.0002  165 VAL   B C   
6261 O O   . VAL   B 165 ? 0.2749 0.1827 0.3412 -0.0453 -0.0842 0.0023  165 VAL   B O   
6262 C CB  . VAL   B 165 ? 0.2455 0.1731 0.3158 -0.0198 -0.0282 -0.0182 165 VAL   B CB  
6263 C CG1 . VAL   B 165 ? 0.2617 0.1808 0.3331 -0.0251 -0.0118 -0.0185 165 VAL   B CG1 
6264 C CG2 . VAL   B 165 ? 0.2413 0.1806 0.3009 -0.0188 -0.0121 -0.0152 165 VAL   B CG2 
6274 N N   . SER   B 166 ? 0.2602 0.1538 0.3741 -0.0387 -0.0937 -0.0206 166 SER   B N   
6275 C CA  . SER   B 166 ? 0.2533 0.1571 0.4271 -0.0387 -0.0765 -0.0285 166 SER   B CA  
6276 C C   . SER   B 166 ? 0.2321 0.1651 0.4362 -0.0412 -0.0753 -0.0065 166 SER   B C   
6277 O O   . SER   B 166 ? 0.2343 0.1875 0.4632 -0.0513 -0.0868 -0.0269 166 SER   B O   
6278 C CB  . SER   B 166 ? 0.2542 0.1700 0.4620 -0.0353 -0.0739 -0.0402 166 SER   B CB  
6279 O OG  . SER   B 166 ? 0.2429 0.1704 0.4827 -0.0240 -0.0773 -0.0250 166 SER   B OG  
6285 N N   . SER   B 167 ? 0.2126 0.1550 0.4075 -0.0406 -0.0770 0.0316  167 SER   B N   
6286 C CA  . SER   B 167 ? 0.2085 0.1675 0.3896 -0.0399 -0.0506 0.0301  167 SER   B CA  
6287 C C   . SER   B 167 ? 0.2020 0.1758 0.3736 -0.0531 -0.0431 0.0502  167 SER   B C   
6288 O O   . SER   B 167 ? 0.2030 0.1891 0.3718 -0.0543 -0.0406 0.0494  167 SER   B O   
6289 C CB  . SER   B 167 ? 0.1969 0.1792 0.3902 -0.0372 -0.0250 0.0224  167 SER   B CB  
6290 O OG  . SER   B 167 ? 0.1877 0.1860 0.3832 -0.0246 -0.0113 0.0240  167 SER   B OG  
6296 N N   . PHE   B 168 ? 0.1999 0.1746 0.3665 -0.0494 -0.0332 0.0540  168 PHE   B N   
6297 C CA  . PHE   B 168 ? 0.2045 0.1750 0.3417 -0.0466 -0.0303 0.0353  168 PHE   B CA  
6298 C C   . PHE   B 168 ? 0.1728 0.1636 0.2869 -0.0294 -0.0201 0.0206  168 PHE   B C   
6299 O O   . PHE   B 168 ? 0.2068 0.1543 0.2861 -0.0037 -0.0197 0.0015  168 PHE   B O   
6300 C CB  . PHE   B 168 ? 0.2159 0.1795 0.3390 -0.0557 -0.0493 0.0463  168 PHE   B CB  
6301 C CG  . PHE   B 168 ? 0.2439 0.1639 0.3198 -0.0537 -0.0438 0.0253  168 PHE   B CG  
6302 C CD1 . PHE   B 168 ? 0.2724 0.1659 0.3308 -0.0539 -0.0455 0.0174  168 PHE   B CD1 
6303 C CD2 . PHE   B 168 ? 0.2350 0.1596 0.3152 -0.0470 -0.0408 0.0298  168 PHE   B CD2 
6304 C CE1 . PHE   B 168 ? 0.2845 0.1769 0.3167 -0.0396 -0.0363 0.0209  168 PHE   B CE1 
6305 C CE2 . PHE   B 168 ? 0.2593 0.1678 0.3182 -0.0342 -0.0398 0.0223  168 PHE   B CE2 
6306 C CZ  . PHE   B 168 ? 0.2744 0.1637 0.3209 -0.0260 -0.0428 0.0309  168 PHE   B CZ  
6316 N N   . LEU   B 169 ? 0.1850 0.1731 0.2839 -0.0013 -0.0080 0.0045  169 LEU   B N   
6317 C CA  . LEU   B 169 ? 0.2149 0.2005 0.3115 -0.0075 -0.0076 -0.0240 169 LEU   B CA  
6318 C C   . LEU   B 169 ? 0.2473 0.2272 0.3636 0.0040  -0.0087 -0.0503 169 LEU   B C   
6319 O O   . LEU   B 169 ? 0.2663 0.2486 0.4135 -0.0031 -0.0055 -0.0735 169 LEU   B O   
6320 C CB  . LEU   B 169 ? 0.2345 0.2419 0.3208 -0.0177 -0.0212 0.0019  169 LEU   B CB  
6321 C CG  . LEU   B 169 ? 0.2782 0.2867 0.3566 -0.0053 -0.0220 0.0067  169 LEU   B CG  
6322 C CD1 . LEU   B 169 ? 0.2909 0.3064 0.3590 -0.0019 -0.0316 0.0202  169 LEU   B CD1 
6323 C CD2 . LEU   B 169 ? 0.2755 0.2937 0.3601 0.0055  -0.0076 -0.0096 169 LEU   B CD2 
6324 O OXT . LEU   B 169 ? 0.2691 0.2448 0.3648 0.0326  -0.0021 -0.0476 169 LEU   B OXT 
6336 O O1  B A1A8F C .   ? 0.1758 0.2149 0.2121 0.0170  -0.0131 -0.0216 201 A1A8F A O1  
6337 C C1  B A1A8F C .   ? 0.1908 0.2127 0.2320 0.0031  -0.0021 -0.0009 201 A1A8F A C1  
6338 C C2  B A1A8F C .   ? 0.1894 0.2103 0.2265 0.0066  -0.0037 -0.0029 201 A1A8F A C2  
6339 C C3  B A1A8F C .   ? 0.1886 0.2092 0.2300 0.0056  -0.0041 -0.0049 201 A1A8F A C3  
6340 C C4  B A1A8F C .   ? 0.1913 0.2126 0.2249 0.0067  -0.0033 -0.0045 201 A1A8F A C4  
6341 C C5  B A1A8F C .   ? 0.1913 0.2117 0.2224 0.0080  -0.0011 -0.0031 201 A1A8F A C5  
6342 C C6  B A1A8F C .   ? 0.1869 0.2068 0.2149 0.0107  -0.0021 -0.0028 201 A1A8F A C6  
6343 C C7  B A1A8F C .   ? 0.1818 0.2111 0.2129 0.0143  -0.0081 -0.0134 201 A1A8F A C7  
6344 C C8  B A1A8F C .   ? 0.1799 0.1769 0.1746 0.0132  -0.0025 0.0125  201 A1A8F A C8  
6345 C C10 B A1A8F C .   ? 0.1616 0.1601 0.1452 0.0190  -0.0014 0.0212  201 A1A8F A C10 
6346 C C11 B A1A8F C .   ? 0.1657 0.1628 0.1546 0.0180  -0.0016 0.0167  201 A1A8F A C11 
6347 C C12 B A1A8F C .   ? 0.1594 0.1586 0.1434 0.0214  0.0008  0.0163  201 A1A8F A C12 
6348 C C13 B A1A8F C .   ? 0.1553 0.1597 0.1391 0.0192  -0.0032 0.0172  201 A1A8F A C13 
6349 C C14 B A1A8F C .   ? 0.1875 0.2052 0.2164 0.0105  -0.0038 -0.0018 201 A1A8F A C14 
6350 C C9  B A1A8F C .   ? 0.1769 0.1690 0.1576 0.0163  0.0013  0.0196  201 A1A8F A C9  
6351 N N1  B A1A8F C .   ? 0.1884 0.1981 0.2064 0.0110  -0.0050 0.0031  201 A1A8F A N1  
6352 N N2  B A1A8F C .   ? 0.1827 0.1713 0.1679 0.0134  0.0028  0.0169  201 A1A8F A N2  
6353 N N3  B A1A8F C .   ? 0.1681 0.1647 0.1485 0.0151  0.0005  0.0248  201 A1A8F A N3  
6354 N N4  B A1A8F C .   ? 0.1562 0.1596 0.1392 0.0196  -0.0042 0.0161  201 A1A8F A N4  
6375 O O1  C A1A8F D .   ? 0.1600 0.1904 0.1586 0.0036  -0.0047 0.0207  202 A1A8F A O1  
6376 C C1  C A1A8F D .   ? 0.1814 0.2026 0.2005 -0.0080 -0.0143 0.0086  202 A1A8F A C1  
6377 C C2  C A1A8F D .   ? 0.1817 0.2028 0.2012 -0.0069 -0.0086 0.0104  202 A1A8F A C2  
6378 C C3  C A1A8F D .   ? 0.1829 0.2041 0.2048 -0.0084 -0.0029 0.0107  202 A1A8F A C3  
6379 C C4  C A1A8F D .   ? 0.1795 0.2035 0.2023 -0.0040 -0.0083 0.0111  202 A1A8F A C4  
6380 C C5  C A1A8F D .   ? 0.1795 0.2026 0.1975 -0.0036 -0.0039 0.0126  202 A1A8F A C5  
6381 C C6  C A1A8F D .   ? 0.1783 0.1989 0.1868 -0.0053 -0.0012 0.0152  202 A1A8F A C6  
6382 C C7  C A1A8F D .   ? 0.1704 0.1954 0.1731 -0.0019 -0.0019 0.0153  202 A1A8F A C7  
6383 C C8  C A1A8F D .   ? 0.1786 0.1774 0.1651 -0.0046 0.0002  0.0217  202 A1A8F A C8  
6384 C C10 C A1A8F D .   ? 0.1637 0.1648 0.1488 0.0039  -0.0004 0.0232  202 A1A8F A C10 
6385 C C11 C A1A8F D .   ? 0.1667 0.1652 0.1511 0.0017  0.0011  0.0235  202 A1A8F A C11 
6386 C C12 C A1A8F D .   ? 0.1613 0.1619 0.1413 0.0059  0.0037  0.0218  202 A1A8F A C12 
6387 C C13 C A1A8F D .   ? 0.1570 0.1637 0.1392 0.0054  -0.0004 0.0203  202 A1A8F A C13 
6388 C C14 C A1A8F D .   ? 0.1830 0.1999 0.1968 -0.0075 -0.0067 0.0112  202 A1A8F A C14 
6389 C C9  C A1A8F D .   ? 0.1781 0.1726 0.1583 -0.0009 0.0014  0.0230  202 A1A8F A C9  
6390 N N1  C A1A8F D .   ? 0.1841 0.1951 0.1893 -0.0073 -0.0033 0.0152  202 A1A8F A N1  
6391 N N2  C A1A8F D .   ? 0.1820 0.1726 0.1590 -0.0041 0.0042  0.0237  202 A1A8F A N2  
6392 N N3  C A1A8F D .   ? 0.1705 0.1697 0.1547 -0.0003 -0.0003 0.0250  202 A1A8F A N3  
6393 N N4  C A1A8F D .   ? 0.1580 0.1640 0.1418 0.0059  -0.0024 0.0185  202 A1A8F A N4  
6414 C C1  D A1A8E E .   ? 0.2111 0.1893 0.2431 -0.0004 -0.0094 -0.0006 203 A1A8E A C1  
6415 C C2  D A1A8E E .   ? 0.2090 0.1851 0.2387 0.0060  -0.0103 0.0004  203 A1A8E A C2  
6416 C C3  D A1A8E E .   ? 0.2096 0.1900 0.2421 0.0057  -0.0080 0.0009  203 A1A8E A C3  
6417 C C4  D A1A8E E .   ? 0.2098 0.1856 0.2385 0.0075  -0.0121 -0.0013 203 A1A8E A C4  
6418 C C5  D A1A8E E .   ? 0.2071 0.1769 0.2285 0.0086  -0.0100 0.0049  203 A1A8E A C5  
6419 C C6  D A1A8E E .   ? 0.2008 0.1678 0.2200 0.0119  -0.0091 0.0055  203 A1A8E A C6  
6420 C C7  D A1A8E E .   ? 0.2049 0.1836 0.2278 0.0086  -0.0064 0.0038  203 A1A8E A C7  
6421 C C8  D A1A8E E .   ? 0.1707 0.1073 0.1737 0.0150  -0.0131 0.0114  203 A1A8E A C8  
6422 C C9  D A1A8E E .   ? 0.1548 0.0867 0.1501 0.0124  0.0026  0.0124  203 A1A8E A C9  
6423 C C10 D A1A8E E .   ? 0.1316 0.0768 0.1321 0.0131  0.0023  0.0190  203 A1A8E A C10 
6424 C C11 D A1A8E E .   ? 0.1429 0.0896 0.1479 0.0171  -0.0060 0.0135  203 A1A8E A C11 
6425 C C12 D A1A8E E .   ? 0.1321 0.0942 0.1307 0.0194  -0.0026 0.0213  203 A1A8E A C12 
6426 C C13 D A1A8E E .   ? 0.1213 0.0918 0.1186 0.0118  -0.0059 0.0326  203 A1A8E A C13 
6427 C C14 D A1A8E E .   ? 0.2047 0.1671 0.2242 0.0117  -0.0122 0.0035  203 A1A8E A C14 
6428 N N1  D A1A8E E .   ? 0.1946 0.1429 0.2038 0.0147  -0.0155 0.0090  203 A1A8E A N1  
6429 N N2  D A1A8E E .   ? 0.1736 0.0960 0.1750 0.0142  -0.0045 0.0127  203 A1A8E A N2  
6430 N N3  D A1A8E E .   ? 0.1340 0.0735 0.1365 0.0076  0.0137  0.0179  203 A1A8E A N3  
6431 N N4  D A1A8E E .   ? 0.1242 0.0811 0.1127 0.0100  -0.0062 0.0296  203 A1A8E A N4  
6432 O O1  D A1A8E E .   ? 0.2075 0.1941 0.2338 0.0065  -0.0070 0.0011  203 A1A8E A O1  
6453 O O   . HOH   F .   ? 0.5171 0.2401 0.4353 -0.0159 -0.0899 0.0601  301 HOH   A O   
6454 O O   . HOH   F .   ? 0.4387 0.8532 0.4942 -0.1236 0.0879  0.0525  302 HOH   A O   
6455 O O   . HOH   F .   ? 0.5496 0.5211 0.4461 -0.1176 -0.1435 -0.0368 303 HOH   A O   
6456 O O   . HOH   F .   ? 0.2724 0.2582 0.3877 -0.0151 0.0964  0.0793  304 HOH   A O   
6457 O O   . HOH   F .   ? 0.6674 0.4985 0.3406 0.2396  -0.1263 0.0536  305 HOH   A O   
6458 O O   . HOH   F .   ? 0.3004 0.3559 0.1976 -0.0327 0.0526  0.0675  306 HOH   A O   
6459 O O   . HOH   F .   ? 0.2217 0.1710 0.2469 0.0313  -0.0476 -0.0075 307 HOH   A O   
6460 O O   . HOH   F .   ? 0.3416 0.7052 0.5775 -0.0632 -0.0920 0.2044  308 HOH   A O   
6461 O O   . HOH   F .   ? 0.2833 0.6505 0.4311 0.0285  -0.0449 0.0855  309 HOH   A O   
6462 O O   . HOH   F .   ? 0.7057 0.7576 0.5519 -0.1000 -0.1278 -0.1219 310 HOH   A O   
6463 O O   . HOH   F .   ? 0.4445 0.3675 0.5781 -0.0204 0.1442  -0.0179 311 HOH   A O   
6464 O O   . HOH   F .   ? 0.6207 0.4366 0.6204 -0.0685 0.1883  0.1793  312 HOH   A O   
6465 O O   . HOH   F .   ? 0.4446 0.5965 0.4797 0.1588  0.0819  -0.0823 313 HOH   A O   
6466 O O   . HOH   F .   ? 0.3268 0.5409 0.5742 -0.0310 0.1130  0.2608  314 HOH   A O   
6467 O O   . HOH   F .   ? 0.6794 0.4753 0.5978 -0.1144 0.1861  0.2035  315 HOH   A O   
6468 O O   . HOH   F .   ? 0.1790 0.4318 0.3221 0.0541  -0.0208 0.0240  316 HOH   A O   
6469 O O   . HOH   F .   ? 0.2060 0.1896 0.3755 -0.0424 0.0174  -0.0191 317 HOH   A O   
6470 O O   . HOH   F .   ? 0.6707 0.6352 0.3915 -0.0681 0.0392  0.1317  318 HOH   A O   
6471 O O   . HOH   F .   ? 0.3714 0.3354 0.3731 -0.1286 0.0207  0.0871  319 HOH   A O   
6472 O O   . HOH   F .   ? 0.7244 0.5483 0.5685 -0.0037 -0.0436 0.0411  320 HOH   A O   
6473 O O   . HOH   F .   ? 0.1648 0.4710 0.3330 -0.0118 0.0169  0.0755  321 HOH   A O   
6474 O O   A HOH   F .   ? 0.4095 0.4526 0.2616 -0.1179 0.0900  0.0477  322 HOH   A O   
6475 O O   . HOH   F .   ? 0.5033 0.2986 0.2760 -0.1293 0.0063  0.0449  323 HOH   A O   
6476 O O   B HOH   F .   ? 0.2299 0.2181 0.1690 -0.0181 -0.0428 0.0725  324 HOH   A O   
6477 O O   . HOH   F .   ? 0.3761 0.3375 0.3934 -0.1118 -0.0309 -0.0165 325 HOH   A O   
6478 O O   . HOH   F .   ? 0.6100 0.6442 0.6571 -0.0514 0.1305  -0.0346 326 HOH   A O   
6479 O O   . HOH   F .   ? 0.2117 0.2937 0.2715 -0.0572 -0.0283 0.1175  327 HOH   A O   
6480 O O   . HOH   F .   ? 0.1567 0.1532 0.2513 -0.0239 0.0084  0.0108  328 HOH   A O   
6481 O O   . HOH   F .   ? 0.5756 0.4051 0.3233 0.0369  0.0749  0.1542  329 HOH   A O   
6482 O O   . HOH   F .   ? 0.5097 0.3429 0.5137 0.1486  -0.0564 -0.0072 330 HOH   A O   
6483 O O   . HOH   F .   ? 0.5899 0.5141 0.5546 0.0236  0.2437  -0.1329 331 HOH   A O   
6484 O O   . HOH   F .   ? 0.2186 0.4400 0.3765 -0.0253 -0.0538 0.1587  332 HOH   A O   
6485 O O   . HOH   F .   ? 0.2459 0.2242 0.2919 0.0452  0.0434  0.0475  333 HOH   A O   
6486 O O   . HOH   F .   ? 0.6460 0.7128 0.7049 0.1028  0.0811  0.0028  334 HOH   A O   
6487 O O   . HOH   F .   ? 0.3757 0.3957 0.4071 -0.0052 0.1817  0.0870  335 HOH   A O   
6488 O O   B HOH   F .   ? 0.1945 0.1877 0.2640 0.0405  -0.0878 -0.0355 336 HOH   A O   
6489 O O   . HOH   F .   ? 0.6331 0.6403 0.4380 0.1100  0.0388  -0.0735 337 HOH   A O   
6490 O O   . HOH   F .   ? 0.2473 0.4383 0.3605 0.1068  -0.0653 -0.0275 338 HOH   A O   
6491 O O   . HOH   F .   ? 0.2192 0.1689 0.1815 -0.0154 0.0116  0.0195  339 HOH   A O   
6492 O O   . HOH   F .   ? 0.5637 0.1961 0.5329 0.0775  -0.0667 -0.0263 340 HOH   A O   
6493 O O   . HOH   F .   ? 0.2230 0.3666 0.4506 -0.0630 0.0499  -0.0966 341 HOH   A O   
6494 O O   . HOH   F .   ? 0.3248 0.2980 0.5289 -0.0368 -0.1153 0.1422  342 HOH   A O   
6495 O O   A HOH   F .   ? 0.4960 0.1679 0.2167 -0.0033 0.0270  -0.0010 343 HOH   A O   
6496 O O   B HOH   F .   ? 0.4140 0.4160 0.4456 0.0389  -0.0398 -0.0974 344 HOH   A O   
6497 O O   A HOH   F .   ? 0.2773 0.4883 0.3748 0.1465  -0.0120 -0.0927 345 HOH   A O   
6498 O O   . HOH   F .   ? 0.4719 0.1943 0.4041 0.0372  -0.1019 0.0410  346 HOH   A O   
6499 O O   . HOH   F .   ? 0.3206 0.4253 0.2549 -0.0243 0.0400  0.0409  347 HOH   A O   
6500 O O   . HOH   F .   ? 0.4727 0.3787 0.4872 -0.1640 -0.0182 0.1959  348 HOH   A O   
6501 O O   . HOH   F .   ? 0.1763 0.1731 0.2344 0.0150  -0.0271 0.0236  349 HOH   A O   
6502 O O   . HOH   F .   ? 0.6381 0.6007 0.7500 -0.1315 -0.0852 0.1714  350 HOH   A O   
6503 O O   . HOH   F .   ? 0.1486 0.2172 0.2351 0.0023  -0.0086 0.0595  351 HOH   A O   
6504 O O   . HOH   F .   ? 0.2859 0.4714 0.3569 -0.0734 0.0559  -0.0148 352 HOH   A O   
6505 O O   . HOH   F .   ? 0.1809 0.2874 0.4063 -0.0178 0.0857  0.0918  353 HOH   A O   
6506 O O   . HOH   F .   ? 0.3577 0.5235 0.4121 0.2036  0.0734  0.0591  354 HOH   A O   
6507 O O   . HOH   F .   ? 0.3482 0.3802 0.2192 -0.1113 -0.0217 -0.0830 355 HOH   A O   
6508 O O   . HOH   F .   ? 0.3121 0.4084 0.3745 -0.1040 -0.1004 -0.0247 356 HOH   A O   
6509 O O   . HOH   F .   ? 0.7877 0.5056 0.6414 -0.0282 -0.1329 0.1165  357 HOH   A O   
6510 O O   A HOH   F .   ? 0.1894 0.3428 0.3036 0.0910  0.0721  0.1365  358 HOH   A O   
6511 O O   . HOH   F .   ? 0.3248 0.3718 0.4554 -0.0819 -0.0874 -0.0770 359 HOH   A O   
6512 O O   . HOH   F .   ? 0.2062 0.1999 0.3615 0.0167  0.0875  -0.0089 360 HOH   A O   
6513 O O   . HOH   F .   ? 0.1488 0.1516 0.1723 -0.0035 -0.0118 -0.0036 361 HOH   A O   
6514 O O   . HOH   F .   ? 0.1526 0.1931 0.2567 0.0061  -0.0046 0.0040  362 HOH   A O   
6515 O O   . HOH   F .   ? 0.1578 0.1331 0.2472 -0.0127 0.0178  -0.0107 363 HOH   A O   
6516 O O   . HOH   F .   ? 0.1356 0.1321 0.1773 -0.0042 0.0082  0.0158  364 HOH   A O   
6517 O O   A HOH   F .   ? 0.1430 0.1670 0.2142 0.0069  -0.0363 -0.0263 365 HOH   A O   
6518 O O   A HOH   F .   ? 0.2883 0.5146 0.4907 0.0721  0.0556  0.0797  366 HOH   A O   
6519 O O   . HOH   F .   ? 0.4359 0.2417 0.4163 -0.1367 0.1656  -0.0646 367 HOH   A O   
6520 O O   . HOH   F .   ? 0.4147 0.2419 0.4450 -0.1232 0.0578  0.0466  368 HOH   A O   
6521 O O   . HOH   F .   ? 0.4274 0.2035 0.2540 0.1180  0.0515  0.0180  369 HOH   A O   
6522 O O   . HOH   F .   ? 0.2657 0.4640 0.3338 0.0684  0.0864  0.1843  370 HOH   A O   
6523 O O   . HOH   F .   ? 0.3516 0.4209 0.3138 -0.0425 -0.0639 0.0968  371 HOH   A O   
6524 O O   . HOH   F .   ? 0.4871 0.6881 0.4035 0.2089  -0.0528 -0.0699 372 HOH   A O   
6525 O O   . HOH   F .   ? 0.3073 0.2433 0.2872 -0.0443 0.0523  -0.0020 373 HOH   A O   
6526 O O   . HOH   F .   ? 0.2134 0.2345 0.2358 -0.0228 -0.0317 0.0472  374 HOH   A O   
6527 O O   . HOH   F .   ? 0.1847 0.1935 0.2644 -0.0315 0.0110  0.0364  375 HOH   A O   
6528 O O   . HOH   F .   ? 0.4295 0.6835 0.6034 -0.0800 -0.1413 -0.0421 376 HOH   A O   
6529 O O   . HOH   F .   ? 0.1895 0.2876 0.3641 0.0390  0.0729  -0.0570 377 HOH   A O   
6530 O O   A HOH   F .   ? 0.2486 0.2197 0.2774 -0.0052 -0.0217 0.0544  378 HOH   A O   
6531 O O   . HOH   F .   ? 0.2576 0.2092 0.4219 -0.0002 -0.0723 -0.0147 379 HOH   A O   
6532 O O   . HOH   F .   ? 0.4050 0.3572 0.3500 0.0296  -0.0696 -0.0336 380 HOH   A O   
6533 O O   . HOH   F .   ? 0.3765 0.2491 0.5444 -0.0912 0.0118  -0.0044 381 HOH   A O   
6534 O O   . HOH   F .   ? 0.2127 0.2023 0.2092 -0.0026 0.0147  0.0055  382 HOH   A O   
6535 O O   . HOH   F .   ? 0.1788 0.1800 0.2631 -0.0307 0.0145  0.0435  383 HOH   A O   
6536 O O   . HOH   F .   ? 0.2324 0.2574 0.4363 0.0148  -0.0492 -0.0416 384 HOH   A O   
6537 O O   . HOH   F .   ? 0.4229 0.6104 0.3743 0.1335  0.1638  -0.0556 385 HOH   A O   
6538 O O   . HOH   F .   ? 0.1856 0.2703 0.3001 0.0442  0.0500  0.1038  386 HOH   A O   
6539 O O   . HOH   F .   ? 0.1397 0.1501 0.1996 0.0035  -0.0203 0.0025  387 HOH   A O   
6540 O O   . HOH   F .   ? 0.2482 0.2078 0.2064 -0.0478 0.0251  0.0334  388 HOH   A O   
6541 O O   . HOH   F .   ? 0.2601 0.3886 0.4047 -0.0284 0.0967  -0.0512 389 HOH   A O   
6542 O O   . HOH   F .   ? 0.3251 0.3105 0.2090 0.0275  0.0561  0.0065  390 HOH   A O   
6543 O O   . HOH   F .   ? 0.3323 0.2758 0.3391 -0.0039 -0.0208 0.1062  391 HOH   A O   
6544 O O   . HOH   F .   ? 0.1698 0.1408 0.1760 -0.0178 0.0117  0.0062  392 HOH   A O   
6545 O O   . HOH   F .   ? 0.1870 0.1863 0.3970 0.0361  0.1042  0.0957  393 HOH   A O   
6546 O O   . HOH   F .   ? 0.3193 0.2694 0.2472 -0.0617 -0.0837 0.0258  394 HOH   A O   
6547 O O   . HOH   F .   ? 0.4107 0.6758 0.4156 -0.1107 -0.0275 0.1614  395 HOH   A O   
6548 O O   A HOH   F .   ? 0.2176 0.1933 0.2971 0.0124  -0.0696 0.0182  396 HOH   A O   
6549 O O   A HOH   F .   ? 0.5508 0.4538 0.3186 -0.1327 -0.0038 0.1213  397 HOH   A O   
6550 O O   . HOH   F .   ? 0.4230 0.5062 0.5774 0.0794  -0.0917 0.0983  398 HOH   A O   
6551 O O   . HOH   F .   ? 0.2451 0.3968 0.3672 -0.0459 0.1141  -0.0829 399 HOH   A O   
6552 O O   . HOH   F .   ? 0.5240 0.5420 0.2119 0.0120  0.0831  0.0708  400 HOH   A O   
6553 O O   A HOH   F .   ? 0.1451 0.1544 0.1617 0.0114  -0.0138 -0.0154 401 HOH   A O   
6554 O O   . HOH   F .   ? 0.2222 0.1777 0.3380 0.0005  -0.0379 0.0169  402 HOH   A O   
6555 O O   . HOH   F .   ? 0.2000 0.2712 0.3963 -0.0131 -0.0084 0.0325  403 HOH   A O   
6556 O O   . HOH   F .   ? 0.4220 0.5322 0.4397 0.1191  -0.1041 -0.1453 404 HOH   A O   
6557 O O   . HOH   F .   ? 0.2221 0.2228 0.2836 -0.0377 -0.0260 0.0810  405 HOH   A O   
6558 O O   . HOH   F .   ? 0.3003 0.3613 0.3905 -0.1009 0.1101  -0.0005 406 HOH   A O   
6559 O O   A HOH   F .   ? 0.1525 0.1603 0.2167 0.0053  -0.0383 -0.0064 407 HOH   A O   
6560 O O   . HOH   F .   ? 0.5905 0.4987 0.5716 -0.1532 0.0093  0.1156  408 HOH   A O   
6561 O O   . HOH   F .   ? 0.2489 0.2057 0.2663 -0.0538 -0.0011 0.0566  409 HOH   A O   
6562 O O   . HOH   F .   ? 0.6731 0.6369 0.5190 -0.0871 0.1761  0.1053  410 HOH   A O   
6563 O O   . HOH   F .   ? 0.5043 0.5884 0.3476 -0.1133 -0.0653 -0.0733 411 HOH   A O   
6564 O O   . HOH   F .   ? 0.2518 0.3606 0.7382 -0.0298 0.0537  -0.0490 412 HOH   A O   
6565 O O   . HOH   F .   ? 0.2242 0.2796 0.2779 -0.0115 -0.0532 0.0569  413 HOH   A O   
6566 O O   . HOH   F .   ? 0.2152 0.2025 0.3454 0.0276  -0.0696 0.0447  414 HOH   A O   
6567 O O   . HOH   F .   ? 0.3527 0.3332 0.5841 0.1056  0.0602  0.0416  415 HOH   A O   
6568 O O   . HOH   F .   ? 0.2772 0.2033 0.2880 -0.0039 0.0312  0.0385  416 HOH   A O   
6569 O O   . HOH   F .   ? 0.3526 0.1350 0.2168 -0.0047 -0.0524 0.0100  417 HOH   A O   
6570 O O   . HOH   F .   ? 0.1771 0.2545 0.3294 -0.0236 -0.0089 0.0574  418 HOH   A O   
6571 O O   A HOH   F .   ? 0.4469 0.5729 0.4865 -0.1530 0.0371  0.0454  419 HOH   A O   
6572 O O   . HOH   F .   ? 0.4241 0.6560 0.3475 -0.0862 -0.0255 0.1695  420 HOH   A O   
6573 O O   . HOH   F .   ? 0.1579 0.1657 0.3509 -0.0051 0.0080  0.0263  421 HOH   A O   
6574 O O   . HOH   F .   ? 0.3972 0.2267 0.5536 -0.0692 -0.2301 0.1022  422 HOH   A O   
6575 O O   . HOH   F .   ? 0.2875 0.6137 0.1828 -0.0353 0.0459  0.0421  423 HOH   A O   
6576 O O   . HOH   F .   ? 0.6619 0.7833 0.4361 0.0700  0.2890  -0.0730 424 HOH   A O   
6577 O O   . HOH   F .   ? 0.6493 0.7779 0.6837 -0.0767 -0.0635 -0.0497 425 HOH   A O   
6578 O O   A HOH   F .   ? 0.5023 0.3446 0.3804 0.1354  0.0950  0.1081  426 HOH   A O   
6579 O O   . HOH   F .   ? 0.2601 0.4138 0.2829 0.1726  0.0087  0.0230  427 HOH   A O   
6580 O O   . HOH   F .   ? 0.3192 0.4150 0.5235 -0.0360 0.1268  -0.0253 428 HOH   A O   
6581 O O   . HOH   F .   ? 0.3659 0.4459 0.5723 0.0745  0.1450  -0.1299 429 HOH   A O   
6582 O O   . HOH   F .   ? 0.5921 0.5007 0.3643 -0.0193 -0.1495 0.0269  430 HOH   A O   
6583 O O   . HOH   F .   ? 0.6513 0.3742 0.4838 0.1670  -0.0756 0.1056  431 HOH   A O   
6584 O O   . HOH   F .   ? 1.0961 1.0340 0.8856 -0.0755 -0.0949 0.0375  432 HOH   A O   
6585 O O   . HOH   F .   ? 0.4512 0.6734 0.5724 0.2156  0.0701  0.1190  433 HOH   A O   
6586 O O   A HOH   F .   ? 0.1571 0.1830 0.1764 0.0174  0.0145  -0.0147 434 HOH   A O   
6587 O O   . HOH   F .   ? 0.6242 0.6280 0.6497 -0.1402 0.0717  -0.1207 435 HOH   A O   
6588 O O   . HOH   F .   ? 0.7719 0.6734 0.7172 0.1210  -0.0606 -0.0179 436 HOH   A O   
6589 O O   . HOH   F .   ? 0.7684 0.8397 0.5790 0.2373  -0.1019 0.2598  437 HOH   A O   
6590 O O   . HOH   F .   ? 0.5545 0.5997 0.5116 -0.0994 0.0255  0.2716  438 HOH   A O   
6591 O O   . HOH   F .   ? 0.2578 0.1691 0.3084 0.0075  0.0059  0.0105  439 HOH   A O   
6592 O O   . HOH   F .   ? 0.5916 0.4984 0.7388 0.0944  0.0300  -0.1199 440 HOH   A O   
6593 O O   . HOH   F .   ? 0.4719 0.3576 0.3293 -0.0997 0.0610  0.0220  441 HOH   A O   
6594 O O   A HOH   F .   ? 0.4241 0.1791 0.3258 -0.0091 -0.1252 -0.0291 442 HOH   A O   
6595 O O   . HOH   F .   ? 0.3781 0.2888 0.1963 -0.0768 0.0376  0.0446  443 HOH   A O   
6596 O O   . HOH   F .   ? 0.1920 0.2204 0.5059 -0.0229 -0.0857 0.0558  444 HOH   A O   
6597 O O   . HOH   F .   ? 0.5145 0.5062 0.4624 -0.0450 -0.0954 -0.1240 445 HOH   A O   
6598 O O   . HOH   F .   ? 0.4645 0.3411 0.3452 0.2319  -0.0277 -0.0123 446 HOH   A O   
6599 O O   . HOH   F .   ? 0.3167 0.4435 0.5684 0.0191  0.1233  -0.1611 447 HOH   A O   
6600 O O   . HOH   F .   ? 0.2461 0.2058 0.2750 0.0087  0.0252  0.0280  448 HOH   A O   
6601 O O   . HOH   F .   ? 0.2093 0.2853 0.2592 -0.0027 0.0049  -0.0389 449 HOH   A O   
6602 O O   A HOH   F .   ? 0.5153 0.3210 0.5307 0.0153  0.1555  0.1525  450 HOH   A O   
6603 O O   B HOH   F .   ? 0.4611 0.2226 0.3540 0.0667  -0.0068 -0.0370 451 HOH   A O   
6604 O O   . HOH   F .   ? 0.6891 0.6260 0.7691 0.0259  -0.1177 0.1989  452 HOH   A O   
6605 O O   . HOH   F .   ? 0.5109 0.4023 0.4295 0.0658  0.1178  0.1147  453 HOH   A O   
6606 O O   B HOH   F .   ? 0.2033 0.1066 0.2602 -0.0030 0.0449  -0.0241 454 HOH   A O   
6607 O O   . HOH   F .   ? 0.3607 0.3957 0.4207 0.1355  -0.0738 0.0782  455 HOH   A O   
6608 O O   B HOH   F .   ? 0.4995 0.4232 0.3066 0.1225  -0.1101 0.0292  456 HOH   A O   
6609 O O   . HOH   F .   ? 0.4922 0.3298 0.4563 0.0382  0.1007  0.0412  457 HOH   A O   
6610 O O   . HOH   F .   ? 0.4769 0.5130 0.5087 0.0167  -0.0270 0.1295  458 HOH   A O   
6611 O O   . HOH   F .   ? 0.3263 0.2892 0.3925 -0.0722 -0.0101 -0.0692 459 HOH   A O   
6612 O O   . HOH   F .   ? 0.8425 0.7743 0.5116 0.0096  -0.0691 -0.0506 460 HOH   A O   
6613 O O   . HOH   F .   ? 0.3622 0.4893 0.5043 0.0596  -0.1140 0.1392  461 HOH   A O   
6614 O O   . HOH   F .   ? 0.3153 0.5099 0.5070 -0.1433 0.0905  -0.1263 462 HOH   A O   
6615 O O   . HOH   F .   ? 0.2766 0.4111 0.5712 0.0701  0.0017  -0.1693 463 HOH   A O   
6616 O O   . HOH   F .   ? 0.5958 0.6011 0.4663 0.1058  -0.0583 -0.0539 464 HOH   A O   
6617 O O   . HOH   F .   ? 0.6354 0.3417 0.7890 0.0125  0.0427  0.2518  465 HOH   A O   
6618 O O   . HOH   F .   ? 0.3943 0.4755 0.4311 -0.0988 0.0111  0.0017  466 HOH   A O   
6619 O O   . HOH   F .   ? 0.2849 0.1758 0.2745 0.0340  -0.0945 -0.0340 467 HOH   A O   
6620 O O   . HOH   F .   ? 0.2649 0.3115 0.3312 -0.0952 0.0387  -0.0253 468 HOH   A O   
6621 O O   . HOH   F .   ? 0.4396 0.5691 0.3839 0.0293  -0.0850 -0.0687 469 HOH   A O   
6622 O O   . HOH   F .   ? 0.6100 0.4762 0.4720 0.0047  0.1567  0.0528  470 HOH   A O   
6623 O O   . HOH   F .   ? 0.4261 0.6527 0.4288 -0.0887 -0.0932 0.2295  471 HOH   A O   
6624 O O   . HOH   F .   ? 0.7151 0.4097 0.5042 -0.0388 0.1122  0.0026  472 HOH   A O   
6625 O O   . HOH   F .   ? 0.3414 0.2857 0.4039 0.0032  0.0850  0.0328  473 HOH   A O   
6626 O O   . HOH   F .   ? 0.6797 0.5915 0.6569 0.1281  0.1924  0.2896  474 HOH   A O   
6627 O O   A HOH   F .   ? 0.2796 0.2142 0.5729 0.0554  -0.1417 -0.0191 475 HOH   A O   
6628 O O   . HOH   F .   ? 0.2746 0.2888 0.2724 0.0472  0.0085  0.0299  476 HOH   A O   
6629 O O   . HOH   F .   ? 0.6443 0.6841 0.6778 -0.1469 -0.1214 0.0221  477 HOH   A O   
6630 O O   . HOH   F .   ? 0.4374 0.4506 0.4880 -0.1830 -0.0175 -0.0106 478 HOH   A O   
6631 O O   . HOH   F .   ? 0.4483 0.5474 0.3208 -0.0064 -0.0173 0.0277  479 HOH   A O   
6632 O O   . HOH   F .   ? 0.7118 0.5361 0.6080 -0.1174 -0.0903 -0.1055 480 HOH   A O   
6633 O O   . HOH   F .   ? 0.5316 0.2794 0.3482 -0.0586 -0.1046 0.0579  481 HOH   A O   
6634 O O   . HOH   F .   ? 0.5421 0.4302 0.4676 0.0243  -0.0137 -0.1225 482 HOH   A O   
6635 O O   . HOH   F .   ? 0.7851 0.3906 0.3322 -0.0244 -0.1284 -0.0242 483 HOH   A O   
6636 O O   . HOH   F .   ? 0.6348 0.6032 0.6479 -0.0548 0.0925  -0.0382 484 HOH   A O   
6637 O O   . HOH   F .   ? 0.4960 0.4783 0.3709 -0.0323 -0.0453 0.0236  485 HOH   A O   
6638 O O   . HOH   F .   ? 0.3056 0.4392 0.4825 0.0116  0.1284  0.1311  486 HOH   A O   
6639 O O   . HOH   F .   ? 0.4421 0.3511 0.2471 -0.0914 0.1082  -0.0467 487 HOH   A O   
6640 O O   . HOH   F .   ? 0.6149 0.5326 0.6983 0.0651  0.1866  -0.1137 488 HOH   A O   
6641 O O   . HOH   F .   ? 0.7425 0.6936 0.5072 -0.0950 0.1637  0.1157  489 HOH   A O   
6642 O O   . HOH   F .   ? 0.2870 0.5287 0.4144 0.1231  0.1158  0.2607  490 HOH   A O   
6643 O O   . HOH   F .   ? 0.5325 0.5498 0.5742 0.0344  -0.1221 0.0730  491 HOH   A O   
6644 O O   . HOH   F .   ? 0.2880 0.2503 0.6724 0.0068  -0.1424 0.0076  492 HOH   A O   
6645 O O   . HOH   F .   ? 0.3219 0.4798 0.3798 -0.0201 -0.0394 -0.0501 493 HOH   A O   
6646 O O   . HOH   F .   ? 0.6719 0.2494 0.4529 -0.0409 0.0745  0.0511  494 HOH   A O   
6647 O O   . HOH   F .   ? 0.4491 0.3820 0.4544 -0.0969 0.0924  0.0536  495 HOH   A O   
6648 O O   . HOH   F .   ? 0.4899 0.3011 0.4389 -0.0187 0.2010  0.0185  496 HOH   A O   
6649 O O   . HOH   F .   ? 0.5329 0.5309 0.4418 -0.0381 -0.0640 -0.0065 497 HOH   A O   
6650 O O   . HOH   F .   ? 0.6968 0.7688 0.5904 0.1991  -0.1438 0.0321  498 HOH   A O   
6651 O O   . HOH   F .   ? 0.2648 0.2859 0.5861 -0.0119 0.0939  -0.0394 499 HOH   A O   
6652 O O   . HOH   F .   ? 0.3120 0.2033 0.6755 -0.0054 0.0675  0.0802  500 HOH   A O   
6653 O O   . HOH   F .   ? 0.4368 0.9002 0.6455 -0.1134 -0.0725 0.2212  501 HOH   A O   
6654 O O   . HOH   F .   ? 0.2424 0.3362 0.3332 0.0430  -0.0381 0.0616  502 HOH   A O   
6655 O O   . HOH   F .   ? 0.4748 0.2849 0.4469 -0.1589 0.0058  0.0264  503 HOH   A O   
6656 O O   . HOH   F .   ? 0.2892 0.3933 0.4291 0.0152  -0.0632 0.0115  504 HOH   A O   
6657 O O   . HOH   F .   ? 0.5687 0.7612 0.5210 0.1199  -0.0419 0.0979  505 HOH   A O   
6658 O O   . HOH   F .   ? 0.7439 0.5562 0.5642 0.1298  -0.0451 0.0240  506 HOH   A O   
6659 O O   . HOH   F .   ? 0.2455 0.9034 0.3678 0.0307  0.0399  -0.0010 507 HOH   A O   
6660 O O   . HOH   F .   ? 0.3138 0.2309 0.4581 -0.0128 0.0169  0.0519  508 HOH   A O   
6661 O O   . HOH   F .   ? 0.5364 0.6934 0.4721 0.2977  -0.0386 0.1217  509 HOH   A O   
6662 O O   . HOH   F .   ? 0.6157 0.7079 0.4755 -0.0538 -0.1276 -0.1150 510 HOH   A O   
6663 O O   . HOH   F .   ? 0.3397 0.7167 0.4846 0.0656  0.0232  -0.0710 511 HOH   A O   
6664 O O   . HOH   F .   ? 0.4640 0.4721 0.4536 0.1241  0.0077  0.0804  512 HOH   A O   
6665 O O   . HOH   F .   ? 0.5035 0.6619 0.5944 -0.0416 -0.0609 0.0864  513 HOH   A O   
6666 O O   . HOH   F .   ? 0.3455 0.4665 0.5738 -0.0578 -0.1140 0.2683  514 HOH   A O   
6667 O O   . HOH   G .   ? 0.2345 0.2092 0.3376 0.0183  0.0771  0.0317  201 HOH   B O   
6668 O O   . HOH   G .   ? 0.4591 0.3546 0.4191 -0.0157 0.0082  -0.1498 202 HOH   B O   
6669 O O   . HOH   G .   ? 0.3288 0.3083 0.6775 -0.0365 0.0370  -0.0322 203 HOH   B O   
6670 O O   . HOH   G .   ? 0.3084 0.1985 0.5540 0.0234  0.1892  0.0866  204 HOH   B O   
6671 O O   . HOH   G .   ? 0.4468 0.5478 0.2596 0.0531  -0.0450 -0.1337 205 HOH   B O   
6672 O O   . HOH   G .   ? 0.2007 0.2287 0.2864 0.0020  0.0318  -0.0259 206 HOH   B O   
6673 O O   . HOH   G .   ? 0.3200 0.7212 0.3990 0.1222  0.0287  0.2530  207 HOH   B O   
6674 O O   . HOH   G .   ? 0.7332 0.3050 0.4745 0.0408  0.1182  0.0146  208 HOH   B O   
6675 O O   . HOH   G .   ? 0.2996 0.5559 0.5190 -0.0301 0.1718  -0.1831 209 HOH   B O   
6676 O O   . HOH   G .   ? 0.6674 0.6379 0.5475 0.2005  0.0410  -0.0060 210 HOH   B O   
6677 O O   . HOH   G .   ? 0.4717 0.4440 0.3517 -0.0310 -0.1278 0.1139  211 HOH   B O   
6678 O O   . HOH   G .   ? 0.5246 0.4060 0.6289 0.0374  -0.1078 0.2623  212 HOH   B O   
6679 O O   . HOH   G .   ? 0.1552 0.1959 0.2953 -0.0196 -0.0122 -0.0036 213 HOH   B O   
6680 O O   . HOH   G .   ? 0.3902 0.5115 0.3911 0.1869  -0.0433 -0.0274 214 HOH   B O   
6681 O O   . HOH   G .   ? 0.4802 0.6038 0.3502 0.2901  -0.0853 0.0004  215 HOH   B O   
6682 O O   . HOH   G .   ? 0.3000 0.2770 0.6589 0.0700  -0.1114 0.0587  216 HOH   B O   
6683 O O   . HOH   G .   ? 0.3987 0.3970 0.5674 -0.1126 0.0070  -0.1285 217 HOH   B O   
6684 O O   . HOH   G .   ? 0.4442 0.4508 0.4164 0.0398  0.0571  -0.1269 218 HOH   B O   
6685 O O   . HOH   G .   ? 0.3939 0.5570 0.5520 0.2620  0.0200  -0.0726 219 HOH   B O   
6686 O O   . HOH   G .   ? 0.3157 0.2332 0.5216 -0.0055 0.1884  0.0059  220 HOH   B O   
6687 O O   . HOH   G .   ? 0.4159 0.3692 0.5502 -0.1504 -0.0132 0.0679  221 HOH   B O   
6688 O O   . HOH   G .   ? 0.3122 0.3258 0.4665 0.0539  -0.0846 -0.0231 222 HOH   B O   
6689 O O   . HOH   G .   ? 0.6359 0.2971 0.4314 -0.1947 0.0203  -0.0025 223 HOH   B O   
6690 O O   . HOH   G .   ? 0.1828 0.2038 0.3125 -0.0142 0.0080  -0.0078 224 HOH   B O   
6691 O O   . HOH   G .   ? 0.5443 0.6157 0.3136 0.0761  0.0452  0.0299  225 HOH   B O   
6692 O O   . HOH   G .   ? 0.5129 0.1986 0.2987 -0.0058 -0.0777 0.0032  226 HOH   B O   
6693 O O   . HOH   G .   ? 0.3807 0.2497 0.4265 0.0650  -0.0150 -0.0474 227 HOH   B O   
6694 O O   . HOH   G .   ? 0.5012 0.6563 0.3872 0.2724  0.0673  0.0662  228 HOH   B O   
6695 O O   . HOH   G .   ? 0.5515 0.3288 0.2814 0.0191  0.1050  -0.0172 229 HOH   B O   
6696 O O   . HOH   G .   ? 0.2356 0.1735 0.2838 -0.0237 0.0905  -0.0034 230 HOH   B O   
6697 O O   . HOH   G .   ? 0.2728 0.3533 0.3282 -0.0855 0.0460  -0.0605 231 HOH   B O   
6698 O O   . HOH   G .   ? 0.2264 0.2215 0.3913 -0.0315 -0.0114 -0.0424 232 HOH   B O   
6699 O O   . HOH   G .   ? 0.3848 0.2544 0.3969 0.0461  -0.1053 -0.1122 233 HOH   B O   
6700 O O   . HOH   G .   ? 0.2777 0.2698 0.3022 0.0277  0.0225  -0.0788 234 HOH   B O   
6701 O O   . HOH   G .   ? 0.3631 0.3188 0.2360 0.0304  0.0722  0.0466  235 HOH   B O   
6702 O O   . HOH   G .   ? 0.4600 0.4595 0.6658 0.0344  -0.1602 -0.1312 236 HOH   B O   
6703 O O   . HOH   G .   ? 0.2204 0.1316 0.3455 0.0072  -0.0531 -0.0158 237 HOH   B O   
6704 O O   . HOH   G .   ? 0.4835 0.3269 0.4399 -0.2285 0.0011  0.0170  238 HOH   B O   
6705 O O   . HOH   G .   ? 0.3681 0.1860 0.2082 0.0284  -0.0829 -0.0192 239 HOH   B O   
6706 O O   . HOH   G .   ? 0.2060 0.4079 0.2368 -0.0426 -0.0178 0.0512  240 HOH   B O   
6707 O O   . HOH   G .   ? 0.2252 0.2605 0.3083 -0.0568 0.0183  -0.0432 241 HOH   B O   
6708 O O   . HOH   G .   ? 0.2220 0.1937 0.2311 -0.0296 -0.0410 0.0047  242 HOH   B O   
6709 O O   . HOH   G .   ? 0.1480 0.1412 0.1624 -0.0117 -0.0105 -0.0040 243 HOH   B O   
6710 O O   . HOH   G .   ? 0.2365 0.2129 0.2809 0.0682  -0.0806 -0.0588 244 HOH   B O   
6711 O O   . HOH   G .   ? 0.1584 0.1496 0.2762 -0.0073 0.0024  -0.0104 245 HOH   B O   
6712 O O   . HOH   G .   ? 0.3367 0.3820 0.6301 0.0240  0.1182  0.0871  246 HOH   B O   
6713 O O   . HOH   G .   ? 0.2991 0.1786 0.5978 -0.0086 -0.1222 -0.0327 247 HOH   B O   
6714 O O   . HOH   G .   ? 0.2692 0.2162 0.2058 0.0228  -0.0104 -0.0040 248 HOH   B O   
6715 O O   . HOH   G .   ? 0.2320 0.3385 0.3588 -0.0446 -0.0677 -0.0554 249 HOH   B O   
6716 O O   . HOH   G .   ? 0.1508 0.1334 0.1765 -0.0015 -0.0007 0.0085  250 HOH   B O   
6717 O O   . HOH   G .   ? 0.7004 0.5025 0.5108 0.1502  -0.0097 -0.0703 251 HOH   B O   
6718 O O   . HOH   G .   ? 0.2831 0.2430 0.2829 0.0815  0.0695  -0.0012 252 HOH   B O   
6719 O O   . HOH   G .   ? 0.3263 0.5126 0.3394 -0.0169 -0.1068 0.0669  253 HOH   B O   
6720 O O   . HOH   G .   ? 0.2201 0.1532 0.2164 -0.0295 -0.0442 0.0272  254 HOH   B O   
6721 O O   . HOH   G .   ? 0.2302 0.3061 0.2323 -0.0557 0.0319  0.0445  255 HOH   B O   
6722 O O   . HOH   G .   ? 0.1606 0.1721 0.3074 -0.0186 -0.0124 -0.0020 256 HOH   B O   
6723 O O   . HOH   G .   ? 0.3390 0.4073 0.2291 0.0274  0.0840  0.0113  257 HOH   B O   
6724 O O   . HOH   G .   ? 0.3432 0.2645 0.3175 -0.0543 0.0332  -0.0523 258 HOH   B O   
6725 O O   . HOH   G .   ? 0.4721 0.3567 0.3731 -0.1191 0.0877  -0.0705 259 HOH   B O   
6726 O O   . HOH   G .   ? 0.2167 0.1883 0.3935 -0.0065 -0.0411 -0.0450 260 HOH   B O   
6727 O O   . HOH   G .   ? 0.1416 0.1640 0.2163 -0.0082 0.0074  0.0158  261 HOH   B O   
6728 O O   . HOH   G .   ? 0.2783 0.4281 0.3325 -0.0992 -0.0281 -0.0828 262 HOH   B O   
6729 O O   . HOH   G .   ? 0.2563 0.5222 0.4832 0.1618  -0.0328 -0.0872 263 HOH   B O   
6730 O O   . HOH   G .   ? 0.4540 0.3691 0.2983 0.0384  -0.0006 -0.0813 264 HOH   B O   
6731 O O   . HOH   G .   ? 0.2064 0.5066 0.4533 -0.0592 -0.0249 -0.1274 265 HOH   B O   
6732 O O   . HOH   G .   ? 0.2275 0.2776 0.2398 -0.0369 -0.0628 -0.0441 266 HOH   B O   
6733 O O   . HOH   G .   ? 0.3550 0.3750 0.4512 0.1333  -0.0519 -0.0891 267 HOH   B O   
6734 O O   . HOH   G .   ? 0.2454 0.2121 0.2083 0.0214  -0.0045 -0.0051 268 HOH   B O   
6735 O O   . HOH   G .   ? 0.2159 0.1485 0.2406 -0.0274 -0.0162 0.0113  269 HOH   B O   
6736 O O   . HOH   G .   ? 0.2651 0.2086 0.2650 -0.0572 0.0228  -0.0175 270 HOH   B O   
6737 O O   . HOH   G .   ? 0.2603 0.4734 0.5301 0.0242  -0.0038 -0.1314 271 HOH   B O   
6738 O O   . HOH   G .   ? 0.2638 0.3903 0.3894 0.0157  0.1167  0.0096  272 HOH   B O   
6739 O O   . HOH   G .   ? 0.2727 0.2704 0.2551 -0.0450 -0.0838 0.0245  273 HOH   B O   
6740 O O   . HOH   G .   ? 0.5071 0.3460 0.4850 0.0179  -0.0045 -0.0616 274 HOH   B O   
6741 O O   . HOH   G .   ? 0.1966 0.1735 0.1847 -0.0459 -0.0459 0.0103  275 HOH   B O   
6742 O O   . HOH   G .   ? 0.3975 0.2821 0.4431 -0.0364 -0.0855 -0.0621 276 HOH   B O   
6743 O O   . HOH   G .   ? 0.4294 0.4816 0.4405 0.0083  -0.1389 0.0139  277 HOH   B O   
6744 O O   . HOH   G .   ? 0.2300 0.3131 0.2400 0.0868  -0.0317 -0.0250 278 HOH   B O   
6745 O O   . HOH   G .   ? 0.1801 0.1451 0.3872 -0.0065 -0.0232 -0.0150 279 HOH   B O   
6746 O O   . HOH   G .   ? 0.1660 0.1602 0.3447 -0.0135 0.0095  -0.0099 280 HOH   B O   
6747 O O   . HOH   G .   ? 0.2202 0.3658 0.3361 -0.0375 0.0322  -0.1321 281 HOH   B O   
6748 O O   . HOH   G .   ? 0.2982 0.2164 0.5172 0.0299  0.0588  0.0545  282 HOH   B O   
6749 O O   . HOH   G .   ? 0.1650 0.1611 0.1961 0.0004  0.0085  0.0005  283 HOH   B O   
6750 O O   . HOH   G .   ? 0.1687 0.2003 0.1698 -0.0106 -0.0196 0.0069  284 HOH   B O   
6751 O O   . HOH   G .   ? 0.1761 0.2029 0.3030 0.0160  -0.0138 -0.0109 285 HOH   B O   
6752 O O   . HOH   G .   ? 0.3937 0.6407 0.2938 0.1887  -0.0449 0.0342  286 HOH   B O   
6753 O O   . HOH   G .   ? 0.5427 0.6955 0.2700 0.0369  -0.1272 0.0666  287 HOH   B O   
6754 O O   . HOH   G .   ? 0.3708 0.2214 0.3801 -0.0861 -0.1729 0.0665  288 HOH   B O   
6755 O O   . HOH   G .   ? 0.2633 0.2845 0.2911 0.0163  -0.0837 0.0174  289 HOH   B O   
6756 O O   . HOH   G .   ? 0.3809 0.2781 0.2145 0.0415  -0.0850 -0.0033 290 HOH   B O   
6757 O O   . HOH   G .   ? 0.2732 0.4707 0.4868 -0.0952 -0.1224 0.0790  291 HOH   B O   
6758 O O   . HOH   G .   ? 0.2997 0.6933 0.7492 0.1103  -0.0811 -0.1231 292 HOH   B O   
6759 O O   . HOH   G .   ? 0.4384 0.4970 0.2293 0.0103  0.0711  0.0670  293 HOH   B O   
6760 O O   . HOH   G .   ? 0.3235 0.3013 0.2902 -0.0311 0.0215  -0.1309 294 HOH   B O   
6761 O O   . HOH   G .   ? 0.2137 0.3171 0.5888 0.0509  -0.0586 -0.1426 295 HOH   B O   
6762 O O   . HOH   G .   ? 0.1804 0.1653 0.2441 0.0116  0.0165  0.0209  296 HOH   B O   
6763 O O   . HOH   G .   ? 0.2702 0.7194 0.2577 0.0764  -0.0415 -0.0685 297 HOH   B O   
6764 O O   . HOH   G .   ? 0.6130 0.3937 0.3228 0.2716  0.1186  0.0834  298 HOH   B O   
6765 O O   . HOH   G .   ? 0.4455 0.4026 0.2472 0.0922  -0.0797 0.0734  299 HOH   B O   
6766 O O   . HOH   G .   ? 0.1715 0.3317 0.5067 0.0317  -0.0142 -0.1301 300 HOH   B O   
6767 O O   . HOH   G .   ? 0.2246 0.3515 0.5250 -0.0237 -0.0577 -0.0474 301 HOH   B O   
6768 O O   . HOH   G .   ? 0.3804 0.4122 0.3961 -0.1779 0.1256  -0.0549 302 HOH   B O   
6769 O O   . HOH   G .   ? 0.4302 0.4202 0.5881 0.0700  0.0155  0.0729  303 HOH   B O   
6770 O O   . HOH   G .   ? 0.4465 0.3471 0.5052 -0.0871 0.0317  0.1552  304 HOH   B O   
6771 O O   . HOH   G .   ? 0.3039 0.2911 0.5371 -0.0286 -0.0651 0.1310  305 HOH   B O   
6772 O O   . HOH   G .   ? 0.3599 0.1937 0.3519 0.0800  0.1249  0.0550  306 HOH   B O   
6773 O O   . HOH   G .   ? 0.1651 0.1544 0.3368 0.0047  0.0029  -0.0031 307 HOH   B O   
6774 O O   . HOH   G .   ? 0.1659 0.1906 0.2916 -0.0281 -0.0108 0.0131  308 HOH   B O   
6775 O O   . HOH   G .   ? 0.2180 0.1663 0.2908 -0.0281 -0.0262 -0.0014 309 HOH   B O   
6776 O O   . HOH   G .   ? 0.5803 0.5905 0.5338 0.2709  0.0029  0.0091  310 HOH   B O   
6777 O O   . HOH   G .   ? 0.2097 0.1604 0.3547 0.0364  -0.0934 -0.0007 311 HOH   B O   
6778 O O   . HOH   G .   ? 0.1722 0.2975 0.2419 -0.0164 -0.0301 0.0665  312 HOH   B O   
6779 O O   . HOH   G .   ? 0.2507 0.1504 0.2649 -0.0238 -0.0279 0.0341  313 HOH   B O   
6780 O O   . HOH   G .   ? 0.5383 0.4175 0.2965 0.0252  -0.0728 -0.0823 314 HOH   B O   
6781 O O   . HOH   G .   ? 0.4835 0.2818 0.2687 -0.1686 0.0803  -0.0286 315 HOH   B O   
6782 O O   . HOH   G .   ? 0.4200 0.2282 0.2875 0.1498  0.0959  0.0354  316 HOH   B O   
6783 O O   . HOH   G .   ? 0.2867 0.3003 0.3602 -0.0421 0.0988  -0.0949 317 HOH   B O   
6784 O O   . HOH   G .   ? 0.5020 0.4093 0.2319 0.1223  -0.0937 -0.0333 318 HOH   B O   
6785 O O   . HOH   G .   ? 0.5803 0.4636 0.5220 0.1379  0.1407  0.0337  319 HOH   B O   
6786 O O   . HOH   G .   ? 0.2258 0.1970 0.2017 -0.0090 0.0216  0.0153  320 HOH   B O   
6787 O O   . HOH   G .   ? 0.1553 0.1604 0.3313 -0.0099 -0.0188 -0.0138 321 HOH   B O   
6788 O O   . HOH   G .   ? 0.2259 0.5752 0.5216 -0.0598 -0.0131 -0.0044 322 HOH   B O   
6789 O O   . HOH   G .   ? 0.3140 0.2298 0.2498 0.0325  -0.0336 0.0266  323 HOH   B O   
6790 O O   . HOH   G .   ? 0.6223 0.3569 0.3956 0.0367  0.1490  0.1440  324 HOH   B O   
6791 O O   . HOH   G .   ? 0.2336 0.2405 0.5512 -0.0556 -0.0012 0.1410  325 HOH   B O   
6792 O O   . HOH   G .   ? 0.6010 0.5036 0.6275 0.0808  -0.0634 0.2314  326 HOH   B O   
6793 O O   . HOH   G .   ? 0.3689 0.3628 0.7642 -0.0249 -0.1011 0.1920  327 HOH   B O   
6794 O O   . HOH   G .   ? 0.4672 0.3467 0.5186 0.1417  0.1924  0.1737  328 HOH   B O   
6795 O O   . HOH   G .   ? 0.1975 0.2031 0.2937 0.0310  0.0409  0.0230  329 HOH   B O   
6796 O O   . HOH   G .   ? 0.5031 0.2601 0.3000 0.0602  0.0571  0.0809  330 HOH   B O   
6797 O O   . HOH   G .   ? 0.2839 0.3656 0.5440 -0.0680 -0.1693 0.1652  331 HOH   B O   
6798 O O   . HOH   G .   ? 0.1908 0.3117 0.3330 0.0418  -0.0103 -0.0796 332 HOH   B O   
6799 O O   . HOH   G .   ? 0.2639 0.2068 0.5582 0.0031  0.0050  0.0301  333 HOH   B O   
6800 O O   . HOH   G .   ? 0.5791 0.6084 0.5371 -0.1095 -0.0331 0.1930  334 HOH   B O   
6801 O O   . HOH   G .   ? 0.5653 0.3960 0.4541 -0.0164 0.1469  -0.1770 335 HOH   B O   
6802 O O   . HOH   G .   ? 0.5655 0.4393 0.6045 -0.1077 -0.1008 -0.1454 336 HOH   B O   
6803 O O   . HOH   G .   ? 0.7613 0.2386 0.3451 0.0456  -0.0989 -0.0146 337 HOH   B O   
6804 O O   . HOH   G .   ? 0.1837 0.1524 0.2340 0.0091  -0.0198 0.0098  338 HOH   B O   
6805 O O   . HOH   G .   ? 0.5283 0.5251 0.3404 0.0046  -0.1093 0.0208  339 HOH   B O   
6806 O O   . HOH   G .   ? 0.5472 0.3669 0.3198 0.0758  -0.1299 -0.0830 340 HOH   B O   
6807 O O   . HOH   G .   ? 0.4437 0.6411 0.3548 -0.0240 -0.0663 0.1759  341 HOH   B O   
6808 O O   . HOH   G .   ? 0.3458 0.5339 0.6675 -0.0816 -0.0966 0.1051  342 HOH   B O   
6809 O O   . HOH   G .   ? 0.6614 0.6661 0.3223 0.0040  -0.0466 0.1394  343 HOH   B O   
6810 O O   . HOH   G .   ? 0.4654 0.5818 0.4265 -0.1283 -0.0857 -0.0754 344 HOH   B O   
6811 O O   . HOH   G .   ? 0.2098 0.1991 0.3351 -0.0094 0.0657  0.0094  345 HOH   B O   
6812 O O   . HOH   G .   ? 0.4362 0.5898 0.5371 -0.0190 -0.1141 0.0654  346 HOH   B O   
6813 O O   . HOH   G .   ? 0.3111 0.1909 0.4019 0.0414  -0.1279 -0.0550 347 HOH   B O   
6814 O O   . HOH   G .   ? 0.2891 0.2208 0.4891 -0.0223 -0.0641 -0.0474 348 HOH   B O   
6815 O O   . HOH   G .   ? 0.2337 0.5978 0.3517 0.1516  -0.0469 -0.1369 349 HOH   B O   
6816 O O   . HOH   G .   ? 0.2351 0.4128 0.5242 0.0172  0.0269  0.0305  350 HOH   B O   
6817 O O   . HOH   G .   ? 0.4844 0.2864 0.5411 -0.0965 0.0905  0.0871  351 HOH   B O   
6818 O O   . HOH   G .   ? 0.3914 0.2231 0.3134 -0.0518 -0.0092 -0.0737 352 HOH   B O   
6819 O O   . HOH   G .   ? 0.5475 0.5802 0.5278 -0.1245 0.0402  0.0574  353 HOH   B O   
6820 O O   . HOH   G .   ? 0.3555 0.4600 0.4938 -0.1613 0.0167  -0.0603 354 HOH   B O   
6821 O O   . HOH   G .   ? 0.4661 0.6538 0.7083 0.0879  0.0562  -0.0853 355 HOH   B O   
6822 O O   . HOH   G .   ? 0.4819 0.5203 0.4904 0.1875  -0.1148 0.1425  356 HOH   B O   
6823 O O   . HOH   G .   ? 0.3967 0.2673 0.4262 -0.0864 -0.0068 -0.0737 357 HOH   B O   
6824 O O   . HOH   G .   ? 0.5157 0.3485 0.4256 0.0357  0.1341  -0.0431 358 HOH   B O   
6825 O O   . HOH   G .   ? 0.4943 0.3289 0.4950 0.0344  -0.1697 -0.0448 359 HOH   B O   
6826 O O   . HOH   G .   ? 0.5801 0.4046 0.5062 0.0288  0.1179  0.1089  360 HOH   B O   
6827 O O   . HOH   G .   ? 0.2182 0.4067 0.6712 -0.0804 -0.0596 -0.0755 361 HOH   B O   
6828 O O   . HOH   G .   ? 0.4952 0.6989 0.3083 0.2610  -0.0151 0.0224  362 HOH   B O   
6829 O O   . HOH   G .   ? 0.5138 0.5163 0.4977 0.0742  0.0457  0.0286  363 HOH   B O   
6830 O O   . HOH   G .   ? 0.5662 0.2413 0.4372 0.0183  -0.0121 0.0699  364 HOH   B O   
6831 O O   . HOH   G .   ? 0.6591 0.4467 0.4304 0.1383  0.0684  0.0619  365 HOH   B O   
6832 O O   . HOH   G .   ? 0.5764 0.5979 0.3445 0.1911  -0.1619 0.0523  366 HOH   B O   
6833 O O   . HOH   G .   ? 0.6165 0.5879 0.4634 -0.0721 -0.0826 -0.1200 367 HOH   B O   
6834 O O   . HOH   G .   ? 0.4527 0.3531 0.5215 0.0529  -0.1659 0.0082  368 HOH   B O   
6835 O O   . HOH   G .   ? 0.4306 0.6021 0.5040 0.2761  0.0530  0.1335  369 HOH   B O   
6836 O O   . HOH   G .   ? 0.5288 0.3052 0.5426 -0.1260 -0.0550 0.0241  370 HOH   B O   
6837 O O   . HOH   G .   ? 0.6131 0.3952 0.2793 -0.0752 -0.0994 -0.0402 371 HOH   B O   
6838 O O   . HOH   G .   ? 0.7947 0.7453 0.5284 0.2830  -0.1255 0.0989  372 HOH   B O   
6839 O O   . HOH   G .   ? 0.3927 0.3103 0.3333 0.0640  -0.0967 -0.0343 373 HOH   B O   
6840 O O   . HOH   G .   ? 0.4413 0.4910 0.4990 -0.0809 -0.0605 0.0411  374 HOH   B O   
6841 O O   . HOH   G .   ? 0.2420 0.4295 0.4062 0.0125  -0.0433 -0.0809 375 HOH   B O   
6842 O O   . HOH   G .   ? 0.3553 0.5095 0.2196 -0.0064 0.0333  0.0041  376 HOH   B O   
6843 O O   . HOH   G .   ? 0.5144 0.6785 0.6170 0.1719  0.0348  0.2764  377 HOH   B O   
6844 O O   . HOH   G .   ? 0.3435 0.5919 0.5919 0.0519  -0.0535 0.0050  378 HOH   B O   
6845 O O   . HOH   G .   ? 0.6840 0.3325 0.5219 -0.0668 -0.0739 0.0005  379 HOH   B O   
6846 O O   . HOH   G .   ? 0.5234 0.7364 0.3894 -0.1325 0.0181  -0.1473 380 HOH   B O   
6847 O O   . HOH   G .   ? 0.3038 0.2619 0.3284 0.0164  0.0365  0.0231  381 HOH   B O   
6848 O O   . HOH   G .   ? 0.6667 0.3841 0.4207 0.0381  0.0790  -0.0737 382 HOH   B O   
6849 O O   . HOH   G .   ? 0.5445 0.6618 0.6190 0.0117  0.1350  0.1719  383 HOH   B O   
6850 O O   . HOH   G .   ? 0.4268 0.7679 0.5516 0.1550  0.1366  0.0777  384 HOH   B O   
6851 O O   . HOH   G .   ? 0.2509 0.4294 0.4081 -0.0709 -0.1029 -0.0409 385 HOH   B O   
6852 O O   . HOH   G .   ? 0.5066 0.4041 0.3014 0.0157  0.0643  -0.0288 386 HOH   B O   
6853 O O   . HOH   G .   ? 0.7712 0.6367 0.4602 0.2771  -0.0034 -0.0274 387 HOH   B O   
6854 O O   . HOH   G .   ? 0.6417 0.4326 0.5345 -0.0873 0.0590  0.0234  388 HOH   B O   
6855 O O   . HOH   G .   ? 0.4383 0.2367 0.3136 0.1014  -0.0196 0.0128  389 HOH   B O   
6856 O O   . HOH   G .   ? 0.4830 0.4573 0.4094 0.0365  0.0535  0.0835  390 HOH   B O   
6857 O O   . HOH   G .   ? 0.4306 0.2477 0.5164 -0.0699 0.0208  0.0795  391 HOH   B O   
6858 O O   . HOH   G .   ? 0.2467 0.4559 0.6962 -0.1293 -0.0645 -0.0091 392 HOH   B O   
6859 O O   . HOH   G .   ? 0.5050 0.6326 0.4308 0.1607  0.0220  -0.1077 393 HOH   B O   
6860 O O   . HOH   G .   ? 0.3255 0.4085 0.3677 0.0290  0.0159  -0.0931 394 HOH   B O   
6861 O O   . HOH   G .   ? 0.4690 0.4155 0.4161 0.0039  0.1016  0.0980  395 HOH   B O   
6862 O O   . HOH   G .   ? 0.2154 0.2803 0.5849 -0.0539 -0.0821 -0.0052 396 HOH   B O   
6863 O O   . HOH   G .   ? 0.5784 0.4022 0.3027 -0.2107 -0.0421 0.0750  397 HOH   B O   
6864 O O   . HOH   G .   ? 0.5591 0.6228 0.5804 0.0103  -0.1247 0.2929  398 HOH   B O   
6865 O O   . HOH   G .   ? 0.6177 0.5923 0.3864 0.0949  -0.0543 0.0113  399 HOH   B O   
# 
