data_7HFC
# 
_entry.id   7HFC 
# 
_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   7HFC         pdb_00007hfc 10.2210/pdb7hfc/pdb 
WWPDB D_1001407402 ?            ?                   
# 
_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                        7HFC 
_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 '2-[(2R)-3,3-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' 274.361   1   ? ? ? ? 
3 non-polymer syn '2-[(2S)-3,3-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' 274.361   1   ? ? ? ? 
4 water       nat water                                                                                 18.015    423 ? ? ? ? 
# 
_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 '2-[(2R)-3,3-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' A1BAY 
3 '2-[(2S)-3,3-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' A1BAZ 
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 
A1BAY non-polymer         . '2-[(2R)-3,3-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' ? 'C15 H22 N4 O' 
274.361 
A1BAZ non-polymer         . '2-[(2S)-3,3-dimethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' ? 'C15 H22 N4 O' 
274.361 
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 A1BAY 1   201 201  A1BAY LA1 A . 
D 3 A1BAZ 1   202 301  A1BAZ LA2 A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 625  HOH   HOH A . 
E 4 HOH   3   303 9    HOH   HOH A . 
E 4 HOH   4   304 209  HOH   HOH A . 
E 4 HOH   5   305 109  HOH   HOH A . 
E 4 HOH   6   306 196  HOH   HOH A . 
E 4 HOH   7   307 964  HOH   HOH A . 
E 4 HOH   8   308 661  HOH   HOH A . 
E 4 HOH   9   309 74   HOH   HOH A . 
E 4 HOH   10  310 1283 HOH   HOH A . 
E 4 HOH   11  311 236  HOH   HOH A . 
E 4 HOH   12  312 57   HOH   HOH A . 
E 4 HOH   13  313 105  HOH   HOH A . 
E 4 HOH   14  314 76   HOH   HOH A . 
E 4 HOH   15  315 337  HOH   HOH A . 
E 4 HOH   16  316 662  HOH   HOH A . 
E 4 HOH   17  317 136  HOH   HOH A . 
E 4 HOH   18  318 153  HOH   HOH A . 
E 4 HOH   19  319 151  HOH   HOH A . 
E 4 HOH   20  320 124  HOH   HOH A . 
E 4 HOH   21  321 1    HOH   HOH A . 
E 4 HOH   22  322 247  HOH   HOH A . 
E 4 HOH   23  323 1295 HOH   HOH A . 
E 4 HOH   24  324 393  HOH   HOH A . 
E 4 HOH   25  325 15   HOH   HOH A . 
E 4 HOH   26  326 49   HOH   HOH A . 
E 4 HOH   27  327 192  HOH   HOH A . 
E 4 HOH   28  328 68   HOH   HOH A . 
E 4 HOH   29  329 493  HOH   HOH A . 
E 4 HOH   30  330 86   HOH   HOH A . 
E 4 HOH   31  331 241  HOH   HOH A . 
E 4 HOH   32  332 630  HOH   HOH A . 
E 4 HOH   33  333 225  HOH   HOH A . 
E 4 HOH   34  334 140  HOH   HOH A . 
E 4 HOH   35  335 93   HOH   HOH A . 
E 4 HOH   36  336 16   HOH   HOH A . 
E 4 HOH   37  337 36   HOH   HOH A . 
E 4 HOH   38  338 164  HOH   HOH A . 
E 4 HOH   39  339 396  HOH   HOH A . 
E 4 HOH   40  340 6    HOH   HOH A . 
E 4 HOH   41  341 42   HOH   HOH A . 
E 4 HOH   42  342 4    HOH   HOH A . 
E 4 HOH   43  343 139  HOH   HOH A . 
E 4 HOH   44  344 39   HOH   HOH A . 
E 4 HOH   45  345 26   HOH   HOH A . 
E 4 HOH   46  346 469  HOH   HOH A . 
E 4 HOH   47  347 320  HOH   HOH A . 
E 4 HOH   48  348 17   HOH   HOH A . 
E 4 HOH   49  349 122  HOH   HOH A . 
E 4 HOH   50  350 92   HOH   HOH A . 
E 4 HOH   51  351 33   HOH   HOH A . 
E 4 HOH   52  352 165  HOH   HOH A . 
E 4 HOH   53  353 66   HOH   HOH A . 
E 4 HOH   54  354 1300 HOH   HOH A . 
E 4 HOH   55  355 2    HOH   HOH A . 
E 4 HOH   56  356 199  HOH   HOH A . 
E 4 HOH   57  357 354  HOH   HOH A . 
E 4 HOH   58  358 27   HOH   HOH A . 
E 4 HOH   59  359 18   HOH   HOH A . 
E 4 HOH   60  360 5    HOH   HOH A . 
E 4 HOH   61  361 162  HOH   HOH A . 
E 4 HOH   62  362 70   HOH   HOH A . 
E 4 HOH   63  363 56   HOH   HOH A . 
E 4 HOH   64  364 169  HOH   HOH A . 
E 4 HOH   65  365 19   HOH   HOH A . 
E 4 HOH   66  366 102  HOH   HOH A . 
E 4 HOH   67  367 186  HOH   HOH A . 
E 4 HOH   68  368 81   HOH   HOH A . 
E 4 HOH   69  369 148  HOH   HOH A . 
E 4 HOH   70  370 138  HOH   HOH A . 
E 4 HOH   71  371 229  HOH   HOH A . 
E 4 HOH   72  372 12   HOH   HOH A . 
E 4 HOH   73  373 1315 HOH   HOH A . 
E 4 HOH   74  374 46   HOH   HOH A . 
E 4 HOH   75  375 21   HOH   HOH A . 
E 4 HOH   76  376 45   HOH   HOH A . 
E 4 HOH   77  377 939  HOH   HOH A . 
E 4 HOH   78  378 159  HOH   HOH A . 
E 4 HOH   79  379 461  HOH   HOH A . 
E 4 HOH   80  380 155  HOH   HOH A . 
E 4 HOH   81  381 78   HOH   HOH A . 
E 4 HOH   82  382 409  HOH   HOH A . 
E 4 HOH   83  383 14   HOH   HOH A . 
E 4 HOH   84  384 34   HOH   HOH A . 
E 4 HOH   85  385 218  HOH   HOH A . 
E 4 HOH   86  386 35   HOH   HOH A . 
E 4 HOH   87  387 8    HOH   HOH A . 
E 4 HOH   88  388 366  HOH   HOH A . 
E 4 HOH   89  389 24   HOH   HOH A . 
E 4 HOH   90  390 134  HOH   HOH A . 
E 4 HOH   91  391 711  HOH   HOH A . 
E 4 HOH   92  392 1290 HOH   HOH A . 
E 4 HOH   93  393 405  HOH   HOH A . 
E 4 HOH   94  394 154  HOH   HOH A . 
E 4 HOH   95  395 58   HOH   HOH A . 
E 4 HOH   96  396 303  HOH   HOH A . 
E 4 HOH   97  397 10   HOH   HOH A . 
E 4 HOH   98  398 3    HOH   HOH A . 
E 4 HOH   99  399 1301 HOH   HOH A . 
E 4 HOH   100 400 116  HOH   HOH A . 
E 4 HOH   101 401 1309 HOH   HOH A . 
E 4 HOH   102 402 67   HOH   HOH A . 
E 4 HOH   103 403 132  HOH   HOH A . 
E 4 HOH   104 404 296  HOH   HOH A . 
E 4 HOH   105 405 83   HOH   HOH A . 
E 4 HOH   106 406 1275 HOH   HOH A . 
E 4 HOH   107 407 6    HOH   HOH A . 
E 4 HOH   108 408 25   HOH   HOH A . 
E 4 HOH   109 409 115  HOH   HOH A . 
E 4 HOH   110 410 1068 HOH   HOH A . 
E 4 HOH   111 411 582  HOH   HOH A . 
E 4 HOH   112 412 212  HOH   HOH A . 
E 4 HOH   113 413 121  HOH   HOH A . 
E 4 HOH   114 414 7    HOH   HOH A . 
E 4 HOH   115 415 96   HOH   HOH A . 
E 4 HOH   116 416 195  HOH   HOH A . 
E 4 HOH   117 417 156  HOH   HOH A . 
E 4 HOH   118 418 281  HOH   HOH A . 
E 4 HOH   119 419 85   HOH   HOH A . 
E 4 HOH   120 420 397  HOH   HOH A . 
E 4 HOH   121 421 333  HOH   HOH A . 
E 4 HOH   122 422 51   HOH   HOH A . 
E 4 HOH   123 423 123  HOH   HOH A . 
E 4 HOH   124 424 8    HOH   HOH A . 
E 4 HOH   125 425 125  HOH   HOH A . 
E 4 HOH   126 426 278  HOH   HOH A . 
E 4 HOH   127 427 53   HOH   HOH A . 
E 4 HOH   128 428 95   HOH   HOH A . 
E 4 HOH   129 429 7    HOH   HOH A . 
E 4 HOH   130 430 1189 HOH   HOH A . 
E 4 HOH   131 431 1310 HOH   HOH A . 
E 4 HOH   132 432 4    HOH   HOH A . 
E 4 HOH   133 433 5    HOH   HOH A . 
E 4 HOH   134 434 1308 HOH   HOH A . 
E 4 HOH   135 435 381  HOH   HOH A . 
E 4 HOH   136 436 351  HOH   HOH A . 
E 4 HOH   137 437 16   HOH   HOH A . 
E 4 HOH   138 438 1222 HOH   HOH A . 
E 4 HOH   139 439 73   HOH   HOH A . 
E 4 HOH   140 440 1279 HOH   HOH A . 
E 4 HOH   141 441 1289 HOH   HOH A . 
E 4 HOH   142 442 12   HOH   HOH A . 
E 4 HOH   143 443 1313 HOH   HOH A . 
E 4 HOH   144 444 71   HOH   HOH A . 
E 4 HOH   145 445 1286 HOH   HOH A . 
E 4 HOH   146 446 80   HOH   HOH A . 
E 4 HOH   147 447 1238 HOH   HOH A . 
E 4 HOH   148 448 944  HOH   HOH A . 
E 4 HOH   149 449 188  HOH   HOH A . 
E 4 HOH   150 450 94   HOH   HOH A . 
E 4 HOH   151 451 952  HOH   HOH A . 
E 4 HOH   152 452 104  HOH   HOH A . 
E 4 HOH   153 453 15   HOH   HOH A . 
E 4 HOH   154 454 97   HOH   HOH A . 
E 4 HOH   155 455 40   HOH   HOH A . 
E 4 HOH   156 456 330  HOH   HOH A . 
E 4 HOH   157 457 11   HOH   HOH A . 
E 4 HOH   158 458 1296 HOH   HOH A . 
E 4 HOH   159 459 576  HOH   HOH A . 
E 4 HOH   160 460 1134 HOH   HOH A . 
E 4 HOH   161 461 79   HOH   HOH A . 
E 4 HOH   162 462 267  HOH   HOH A . 
E 4 HOH   163 463 1119 HOH   HOH A . 
E 4 HOH   164 464 1276 HOH   HOH A . 
E 4 HOH   165 465 107  HOH   HOH A . 
E 4 HOH   166 466 726  HOH   HOH A . 
E 4 HOH   167 467 509  HOH   HOH A . 
E 4 HOH   168 468 163  HOH   HOH A . 
E 4 HOH   169 469 756  HOH   HOH A . 
E 4 HOH   170 470 361  HOH   HOH A . 
E 4 HOH   171 471 1094 HOH   HOH A . 
E 4 HOH   172 472 408  HOH   HOH A . 
E 4 HOH   173 473 342  HOH   HOH A . 
E 4 HOH   174 474 63   HOH   HOH A . 
E 4 HOH   175 475 319  HOH   HOH A . 
E 4 HOH   176 476 280  HOH   HOH A . 
E 4 HOH   177 477 801  HOH   HOH A . 
E 4 HOH   178 478 126  HOH   HOH A . 
E 4 HOH   179 479 556  HOH   HOH A . 
E 4 HOH   180 480 17   HOH   HOH A . 
E 4 HOH   181 481 1307 HOH   HOH A . 
E 4 HOH   182 482 326  HOH   HOH A . 
E 4 HOH   183 483 370  HOH   HOH A . 
E 4 HOH   184 484 250  HOH   HOH A . 
E 4 HOH   185 485 521  HOH   HOH A . 
E 4 HOH   186 486 1306 HOH   HOH A . 
E 4 HOH   187 487 695  HOH   HOH A . 
E 4 HOH   188 488 1287 HOH   HOH A . 
E 4 HOH   189 489 135  HOH   HOH A . 
E 4 HOH   190 490 674  HOH   HOH A . 
E 4 HOH   191 491 224  HOH   HOH A . 
E 4 HOH   192 492 919  HOH   HOH A . 
E 4 HOH   193 493 1314 HOH   HOH A . 
E 4 HOH   194 494 315  HOH   HOH A . 
E 4 HOH   195 495 202  HOH   HOH A . 
E 4 HOH   196 496 309  HOH   HOH A . 
E 4 HOH   197 497 208  HOH   HOH A . 
E 4 HOH   198 498 318  HOH   HOH A . 
E 4 HOH   199 499 1299 HOH   HOH A . 
E 4 HOH   200 500 331  HOH   HOH A . 
E 4 HOH   201 501 263  HOH   HOH A . 
E 4 HOH   202 502 152  HOH   HOH A . 
E 4 HOH   203 503 805  HOH   HOH A . 
E 4 HOH   204 504 356  HOH   HOH A . 
E 4 HOH   205 505 941  HOH   HOH A . 
E 4 HOH   206 506 1071 HOH   HOH A . 
E 4 HOH   207 507 180  HOH   HOH A . 
E 4 HOH   208 508 350  HOH   HOH A . 
E 4 HOH   209 509 3    HOH   HOH A . 
E 4 HOH   210 510 363  HOH   HOH A . 
E 4 HOH   211 511 313  HOH   HOH A . 
E 4 HOH   212 512 371  HOH   HOH A . 
E 4 HOH   213 513 1284 HOH   HOH A . 
E 4 HOH   214 514 185  HOH   HOH A . 
E 4 HOH   215 515 429  HOH   HOH A . 
E 4 HOH   216 516 13   HOH   HOH A . 
E 4 HOH   217 517 772  HOH   HOH A . 
E 4 HOH   218 518 376  HOH   HOH A . 
E 4 HOH   219 519 1074 HOH   HOH A . 
E 4 HOH   220 520 346  HOH   HOH A . 
E 4 HOH   221 521 1292 HOH   HOH A . 
E 4 HOH   222 522 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 358  HOH   HOH B . 
F 4 HOH   3   203 654  HOH   HOH B . 
F 4 HOH   4   204 1249 HOH   HOH B . 
F 4 HOH   5   205 398  HOH   HOH B . 
F 4 HOH   6   206 758  HOH   HOH B . 
F 4 HOH   7   207 743  HOH   HOH B . 
F 4 HOH   8   208 364  HOH   HOH B . 
F 4 HOH   9   209 900  HOH   HOH B . 
F 4 HOH   10  210 240  HOH   HOH B . 
F 4 HOH   11  211 282  HOH   HOH B . 
F 4 HOH   12  212 531  HOH   HOH B . 
F 4 HOH   13  213 549  HOH   HOH B . 
F 4 HOH   14  214 264  HOH   HOH B . 
F 4 HOH   15  215 50   HOH   HOH B . 
F 4 HOH   16  216 343  HOH   HOH B . 
F 4 HOH   17  217 120  HOH   HOH B . 
F 4 HOH   18  218 353  HOH   HOH B . 
F 4 HOH   19  219 452  HOH   HOH B . 
F 4 HOH   20  220 272  HOH   HOH B . 
F 4 HOH   21  221 276  HOH   HOH B . 
F 4 HOH   22  222 332  HOH   HOH B . 
F 4 HOH   23  223 444  HOH   HOH B . 
F 4 HOH   24  224 1278 HOH   HOH B . 
F 4 HOH   25  225 131  HOH   HOH B . 
F 4 HOH   26  226 166  HOH   HOH B . 
F 4 HOH   27  227 723  HOH   HOH B . 
F 4 HOH   28  228 75   HOH   HOH B . 
F 4 HOH   29  229 1140 HOH   HOH B . 
F 4 HOH   30  230 54   HOH   HOH B . 
F 4 HOH   31  231 232  HOH   HOH B . 
F 4 HOH   32  232 252  HOH   HOH B . 
F 4 HOH   33  233 181  HOH   HOH B . 
F 4 HOH   34  234 205  HOH   HOH B . 
F 4 HOH   35  235 69   HOH   HOH B . 
F 4 HOH   36  236 60   HOH   HOH B . 
F 4 HOH   37  237 1    HOH   HOH B . 
F 4 HOH   38  238 110  HOH   HOH B . 
F 4 HOH   39  239 14   HOH   HOH B . 
F 4 HOH   40  240 129  HOH   HOH B . 
F 4 HOH   41  241 72   HOH   HOH B . 
F 4 HOH   42  242 128  HOH   HOH B . 
F 4 HOH   43  243 9    HOH   HOH B . 
F 4 HOH   44  244 127  HOH   HOH B . 
F 4 HOH   45  245 82   HOH   HOH B . 
F 4 HOH   46  246 133  HOH   HOH B . 
F 4 HOH   47  247 30   HOH   HOH B . 
F 4 HOH   48  248 1312 HOH   HOH B . 
F 4 HOH   49  249 231  HOH   HOH B . 
F 4 HOH   50  250 325  HOH   HOH B . 
F 4 HOH   51  251 20   HOH   HOH B . 
F 4 HOH   52  252 31   HOH   HOH B . 
F 4 HOH   53  253 143  HOH   HOH B . 
F 4 HOH   54  254 391  HOH   HOH B . 
F 4 HOH   55  255 300  HOH   HOH B . 
F 4 HOH   56  256 144  HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 10   HOH   HOH B . 
F 4 HOH   59  259 52   HOH   HOH B . 
F 4 HOH   60  260 302  HOH   HOH B . 
F 4 HOH   61  261 221  HOH   HOH B . 
F 4 HOH   62  262 62   HOH   HOH B . 
F 4 HOH   63  263 41   HOH   HOH B . 
F 4 HOH   64  264 59   HOH   HOH B . 
F 4 HOH   65  265 61   HOH   HOH B . 
F 4 HOH   66  266 77   HOH   HOH B . 
F 4 HOH   67  267 1277 HOH   HOH B . 
F 4 HOH   68  268 103  HOH   HOH B . 
F 4 HOH   69  269 84   HOH   HOH B . 
F 4 HOH   70  270 11   HOH   HOH B . 
F 4 HOH   71  271 175  HOH   HOH B . 
F 4 HOH   72  272 150  HOH   HOH B . 
F 4 HOH   73  273 172  HOH   HOH B . 
F 4 HOH   74  274 117  HOH   HOH B . 
F 4 HOH   75  275 387  HOH   HOH B . 
F 4 HOH   76  276 347  HOH   HOH B . 
F 4 HOH   77  277 271  HOH   HOH B . 
F 4 HOH   78  278 242  HOH   HOH B . 
F 4 HOH   79  279 114  HOH   HOH B . 
F 4 HOH   80  280 1106 HOH   HOH B . 
F 4 HOH   81  281 141  HOH   HOH B . 
F 4 HOH   82  282 235  HOH   HOH B . 
F 4 HOH   83  283 43   HOH   HOH B . 
F 4 HOH   84  284 22   HOH   HOH B . 
F 4 HOH   85  285 243  HOH   HOH B . 
F 4 HOH   86  286 88   HOH   HOH B . 
F 4 HOH   87  287 147  HOH   HOH B . 
F 4 HOH   88  288 89   HOH   HOH B . 
F 4 HOH   89  289 1126 HOH   HOH B . 
F 4 HOH   90  290 13   HOH   HOH B . 
F 4 HOH   91  291 1066 HOH   HOH B . 
F 4 HOH   92  292 106  HOH   HOH B . 
F 4 HOH   93  293 99   HOH   HOH B . 
F 4 HOH   94  294 220  HOH   HOH B . 
F 4 HOH   95  295 287  HOH   HOH B . 
F 4 HOH   96  296 299  HOH   HOH B . 
F 4 HOH   97  297 137  HOH   HOH B . 
F 4 HOH   98  298 297  HOH   HOH B . 
F 4 HOH   99  299 112  HOH   HOH B . 
F 4 HOH   100 300 316  HOH   HOH B . 
F 4 HOH   101 301 635  HOH   HOH B . 
F 4 HOH   102 302 339  HOH   HOH B . 
F 4 HOH   103 303 215  HOH   HOH B . 
F 4 HOH   104 304 160  HOH   HOH B . 
F 4 HOH   105 305 32   HOH   HOH B . 
F 4 HOH   106 306 38   HOH   HOH B . 
F 4 HOH   107 307 142  HOH   HOH B . 
F 4 HOH   108 308 1305 HOH   HOH B . 
F 4 HOH   109 309 311  HOH   HOH B . 
F 4 HOH   110 310 101  HOH   HOH B . 
F 4 HOH   111 311 416  HOH   HOH B . 
F 4 HOH   112 312 216  HOH   HOH B . 
F 4 HOH   113 313 341  HOH   HOH B . 
F 4 HOH   114 314 37   HOH   HOH B . 
F 4 HOH   115 315 48   HOH   HOH B . 
F 4 HOH   116 316 1291 HOH   HOH B . 
F 4 HOH   117 317 91   HOH   HOH B . 
F 4 HOH   118 318 118  HOH   HOH B . 
F 4 HOH   119 319 170  HOH   HOH B . 
F 4 HOH   120 320 23   HOH   HOH B . 
F 4 HOH   121 321 334  HOH   HOH B . 
F 4 HOH   122 322 704  HOH   HOH B . 
F 4 HOH   123 323 44   HOH   HOH B . 
F 4 HOH   124 324 100  HOH   HOH B . 
F 4 HOH   125 325 28   HOH   HOH B . 
F 4 HOH   126 326 1274 HOH   HOH B . 
F 4 HOH   127 327 161  HOH   HOH B . 
F 4 HOH   128 328 182  HOH   HOH B . 
F 4 HOH   129 329 177  HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 717  HOH   HOH B . 
F 4 HOH   132 332 1285 HOH   HOH B . 
F 4 HOH   133 333 197  HOH   HOH B . 
F 4 HOH   134 334 234  HOH   HOH B . 
F 4 HOH   135 335 207  HOH   HOH B . 
F 4 HOH   136 336 98   HOH   HOH B . 
F 4 HOH   137 337 1294 HOH   HOH B . 
F 4 HOH   138 338 55   HOH   HOH B . 
F 4 HOH   139 339 65   HOH   HOH B . 
F 4 HOH   140 340 445  HOH   HOH B . 
F 4 HOH   141 341 619  HOH   HOH B . 
F 4 HOH   142 342 1293 HOH   HOH B . 
F 4 HOH   143 343 178  HOH   HOH B . 
F 4 HOH   144 344 90   HOH   HOH B . 
F 4 HOH   145 345 362  HOH   HOH B . 
F 4 HOH   146 346 463  HOH   HOH B . 
F 4 HOH   147 347 1304 HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 304  HOH   HOH B . 
F 4 HOH   150 350 960  HOH   HOH B . 
F 4 HOH   151 351 203  HOH   HOH B . 
F 4 HOH   152 352 1280 HOH   HOH B . 
F 4 HOH   153 353 623  HOH   HOH B . 
F 4 HOH   154 354 335  HOH   HOH B . 
F 4 HOH   155 355 541  HOH   HOH B . 
F 4 HOH   156 356 290  HOH   HOH B . 
F 4 HOH   157 357 1046 HOH   HOH B . 
F 4 HOH   158 358 1077 HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 87   HOH   HOH B . 
F 4 HOH   161 361 283  HOH   HOH B . 
F 4 HOH   162 362 389  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 718  HOH   HOH B . 
F 4 HOH   165 365 615  HOH   HOH B . 
F 4 HOH   166 366 898  HOH   HOH B . 
F 4 HOH   167 367 340  HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 1316 HOH   HOH B . 
F 4 HOH   170 370 667  HOH   HOH B . 
F 4 HOH   171 371 291  HOH   HOH B . 
F 4 HOH   172 372 190  HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 183  HOH   HOH B . 
F 4 HOH   175 375 149  HOH   HOH B . 
F 4 HOH   176 376 1303 HOH   HOH B . 
F 4 HOH   177 377 431  HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 1163 HOH   HOH B . 
F 4 HOH   180 380 418  HOH   HOH B . 
F 4 HOH   181 381 176  HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 1000 HOH   HOH B . 
F 4 HOH   185 385 470  HOH   HOH B . 
F 4 HOH   186 386 981  HOH   HOH B . 
F 4 HOH   187 387 265  HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 491  HOH   HOH B . 
F 4 HOH   190 390 1298 HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 792  HOH   HOH B . 
F 4 HOH   197 397 274  HOH   HOH B . 
F 4 HOH   198 398 314  HOH   HOH B . 
F 4 HOH   199 399 157  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFC 
_cell.length_a           88.713 
_cell.length_b           88.713 
_cell.length_c           39.599 
_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                         7HFC 
_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          7HFC 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.7 
_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   2023-08-11 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HFC 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.010 
_reflns.number_obs                   159714 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.100 
_reflns.pdbx_Rmerge_I_obs            0.050 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.300 
_reflns.B_iso_Wilson_estimate        12.100 
_reflns.pdbx_redundancy              6.600 
_reflns.pdbx_Rrim_I_all              0.055 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1057483 
_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 1.010 1.030  ? 49351 7834 ? 1.848 ? ? ? 6.300 ? 0.900  ? ? ? ? ? ? 98.800 2.015 0.790 0.644 
1 2 5.530 44.360 ? 7479  1067 ? 0.037 ? ? ? 7.000 ? 55.300 ? ? ? ? ? ? 99.800 0.040 0.015 0.997 
# 
_refine.entry_id                                 7HFC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0100 
_refine.ls_d_res_low                             39.6700 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.9500 
_refine.ls_number_reflns_obs                     159621 
_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                          0.1501 
_refine.ls_R_factor_R_work                       0.1493 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1649 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8100 
_refine.ls_number_reflns_R_free                  7680 
_refine.ls_number_reflns_R_work                  151941 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.1776 
_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                                65.010 
_refine.B_iso_min                                9.280 
_refine.pdbx_overall_phase_error                 19.4400 
_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                       1.0100 
_refine_hist.d_res_low                        39.6700 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             423 
_refine_hist.number_atoms_total               3049 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.12 
_refine_hist.pdbx_B_iso_mean_solvent          30.83 
_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 
1.0100 1.0200  30 98.0000  5034 . 0.3728 0.3850 . 234 0.0000 5268 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5089 . 0.3295 0.3386 . 222 0.0000 5311 . 'X-RAY DIFFRACTION' 
1.0300 1.0500  30 100.0000 5048 . 0.3114 0.3070 . 275 0.0000 5323 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5006 . 0.2864 0.2769 . 293 0.0000 5299 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 99.0000  5051 . 0.2707 0.2824 . 269 0.0000 5320 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 99.0000  5036 . 0.2437 0.2564 . 244 0.0000 5280 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 98.0000  4987 . 0.2299 0.2379 . 258 0.0000 5245 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 97.0000  4864 . 0.2038 0.2305 . 258 0.0000 5122 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5155 . 0.1851 0.1949 . 221 0.0000 5376 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5109 . 0.1731 0.1847 . 256 0.0000 5365 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5075 . 0.1600 0.1850 . 257 0.0000 5332 . 'X-RAY DIFFRACTION' 
1.1800 1.2000  30 100.0000 5135 . 0.1524 0.1841 . 255 0.0000 5390 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 99.0000  4959 . 0.1434 0.1721 . 284 0.0000 5243 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 99.0000  5083 . 0.1402 0.1583 . 230 0.0000 5313 . 'X-RAY DIFFRACTION' 
1.2500 1.2700  30 95.0000  4865 . 0.1416 0.1754 . 229 0.0000 5094 . 'X-RAY DIFFRACTION' 
1.2700 1.3000  30 97.0000  4989 . 0.1325 0.1546 . 248 0.0000 5237 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5069 . 0.1327 0.1490 . 285 0.0000 5354 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5085 . 0.1314 0.1510 . 274 0.0000 5359 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5141 . 0.1273 0.1675 . 223 0.0000 5364 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5082 . 0.1252 0.1435 . 267 0.0000 5349 . 'X-RAY DIFFRACTION' 
1.4600 1.5100  30 100.0000 5117 . 0.1198 0.1398 . 253 0.0000 5370 . 'X-RAY DIFFRACTION' 
1.5100 1.5700  30 96.0000  4902 . 0.1214 0.1316 . 254 0.0000 5156 . 'X-RAY DIFFRACTION' 
1.5700 1.6400  30 98.0000  5007 . 0.1190 0.1329 . 263 0.0000 5270 . 'X-RAY DIFFRACTION' 
1.6400 1.7300  30 100.0000 5164 . 0.1256 0.1476 . 231 0.0000 5395 . 'X-RAY DIFFRACTION' 
1.7300 1.8400  30 100.0000 5100 . 0.1336 0.1323 . 263 0.0000 5363 . 'X-RAY DIFFRACTION' 
1.8400 1.9800  30 100.0000 5142 . 0.1361 0.1342 . 279 0.0000 5421 . 'X-RAY DIFFRACTION' 
1.9800 2.1800  30 99.0000  5074 . 0.1392 0.1600 . 283 0.0000 5357 . 'X-RAY DIFFRACTION' 
2.1800 2.4900  30 99.0000  5105 . 0.1396 0.1411 . 255 0.0000 5360 . 'X-RAY DIFFRACTION' 
2.4900 3.1400  30 100.0000 5182 . 0.1507 0.1647 . 259 0.0000 5441 . 'X-RAY DIFFRACTION' 
3.1400 39.6700 30 99.0000  5286 . 0.1530 0.1811 . 258 0.0000 5544 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFC 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004126' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFC 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HFC A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFC 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 7HFC SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFC MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFC SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFC MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N 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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HFC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A ASP 66  ? ? 1_555 HG B SER 1   ? B 2_655 1.58 
2 1 OD1 A ASN 159 ? B 1_555 O  A HOH 471 ? ? 3_554 2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.45   -133.10 
2 1 ILE A 131 ? B -147.37 -21.84  
3 1 ALA A 134 ? B 39.66   33.62   
4 1 ASP A 157 ? B -166.24 108.34  
5 1 HIS B 86  ? ? 57.26   -127.50 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 520 ? 5.90 . 
2 1 O ? A HOH 521 ? 6.07 . 
3 1 O ? A HOH 522 ? 7.55 . 
4 1 O ? B HOH 401 ? 6.26 . 
# 
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 
A1BAY N2   N Y N 1   
A1BAY C3   C N N 2   
A1BAY C6   C Y N 3   
A1BAY C9   C Y N 4   
A1BAY C12  C N N 5   
A1BAY C14  C N N 6   
A1BAY C1   C N N 7   
A1BAY C10  C Y N 8   
A1BAY C11  C N N 9   
A1BAY C13  C N N 10  
A1BAY C15  C N N 11  
A1BAY C2   C N N 12  
A1BAY C4   C N R 13  
A1BAY C5   C Y N 14  
A1BAY C7   C Y N 15  
A1BAY C8   C Y N 16  
A1BAY N1   N N N 17  
A1BAY N3   N Y N 18  
A1BAY N4   N Y N 19  
A1BAY O1   O N N 20  
A1BAY H7   H N N 21  
A1BAY H5   H N N 22  
A1BAY H6   H N N 23  
A1BAY H9   H N N 24  
A1BAY H10  H N N 25  
A1BAY H15  H N N 26  
A1BAY H16  H N N 27  
A1BAY H17  H N N 28  
A1BAY H18  H N N 29  
A1BAY H19  H N N 30  
A1BAY H4   H N N 31  
A1BAY H3   H N N 32  
A1BAY H2   H N N 33  
A1BAY H11  H N N 34  
A1BAY H13  H N N 35  
A1BAY H14  H N N 36  
A1BAY H20  H N N 37  
A1BAY H21  H N N 38  
A1BAY H22  H N N 39  
A1BAY H1   H N N 40  
A1BAY H12  H N N 41  
A1BAY H8   H N N 42  
A1BAZ O1   O N N 43  
A1BAZ C1   C N N 44  
A1BAZ C2   C N N 45  
A1BAZ C3   C N N 46  
A1BAZ C4   C N S 47  
A1BAZ C5   C Y N 48  
A1BAZ C6   C Y N 49  
A1BAZ C7   C Y N 50  
A1BAZ C8   C Y N 51  
A1BAZ C10  C Y N 52  
A1BAZ C11  C N N 53  
A1BAZ C12  C N N 54  
A1BAZ C13  C N N 55  
A1BAZ C14  C N N 56  
A1BAZ C15  C N N 57  
A1BAZ C9   C Y N 58  
A1BAZ N1   N N N 59  
A1BAZ N2   N Y N 60  
A1BAZ N3   N Y N 61  
A1BAZ N4   N Y N 62  
A1BAZ H8   H N N 63  
A1BAZ H2   H N N 64  
A1BAZ H3   H N N 65  
A1BAZ H4   H N N 66  
A1BAZ H6   H N N 67  
A1BAZ H5   H N N 68  
A1BAZ H7   H N N 69  
A1BAZ H1   H N N 70  
A1BAZ H9   H N N 71  
A1BAZ H11  H N N 72  
A1BAZ H13  H N N 73  
A1BAZ H14  H N N 74  
A1BAZ H15  H N N 75  
A1BAZ H16  H N N 76  
A1BAZ H18  H N N 77  
A1BAZ H17  H N N 78  
A1BAZ H19  H N N 79  
A1BAZ H20  H N N 80  
A1BAZ H21  H N N 81  
A1BAZ H22  H N N 82  
A1BAZ H10  H N N 83  
A1BAZ H12  H N N 84  
ALA   N    N N N 85  
ALA   CA   C N S 86  
ALA   C    C N N 87  
ALA   O    O N N 88  
ALA   CB   C N N 89  
ALA   OXT  O N N 90  
ALA   H    H N N 91  
ALA   H2   H N N 92  
ALA   HA   H N N 93  
ALA   HB1  H N N 94  
ALA   HB2  H N N 95  
ALA   HB3  H N N 96  
ALA   HXT  H N N 97  
ARG   N    N N N 98  
ARG   CA   C N S 99  
ARG   C    C N N 100 
ARG   O    O N N 101 
ARG   CB   C N N 102 
ARG   CG   C N N 103 
ARG   CD   C N N 104 
ARG   NE   N N N 105 
ARG   CZ   C N N 106 
ARG   NH1  N N N 107 
ARG   NH2  N N N 108 
ARG   OXT  O N N 109 
ARG   H    H N N 110 
ARG   H2   H N N 111 
ARG   HA   H N N 112 
ARG   HB2  H N N 113 
ARG   HB3  H N N 114 
ARG   HG2  H N N 115 
ARG   HG3  H N N 116 
ARG   HD2  H N N 117 
ARG   HD3  H N N 118 
ARG   HE   H N N 119 
ARG   HH11 H N N 120 
ARG   HH12 H N N 121 
ARG   HH21 H N N 122 
ARG   HH22 H N N 123 
ARG   HXT  H N N 124 
ASN   N    N N N 125 
ASN   CA   C N S 126 
ASN   C    C N N 127 
ASN   O    O N N 128 
ASN   CB   C N N 129 
ASN   CG   C N N 130 
ASN   OD1  O N N 131 
ASN   ND2  N N N 132 
ASN   OXT  O N N 133 
ASN   H    H N N 134 
ASN   H2   H N N 135 
ASN   HA   H N N 136 
ASN   HB2  H N N 137 
ASN   HB3  H N N 138 
ASN   HD21 H N N 139 
ASN   HD22 H N N 140 
ASN   HXT  H N N 141 
ASP   N    N N N 142 
ASP   CA   C N S 143 
ASP   C    C N N 144 
ASP   O    O N N 145 
ASP   CB   C N N 146 
ASP   CG   C N N 147 
ASP   OD1  O N N 148 
ASP   OD2  O N N 149 
ASP   OXT  O N N 150 
ASP   H    H N N 151 
ASP   H2   H N N 152 
ASP   HA   H N N 153 
ASP   HB2  H N N 154 
ASP   HB3  H N N 155 
ASP   HD2  H N N 156 
ASP   HXT  H N N 157 
CYS   N    N N N 158 
CYS   CA   C N R 159 
CYS   C    C N N 160 
CYS   O    O N N 161 
CYS   CB   C N N 162 
CYS   SG   S N N 163 
CYS   OXT  O N N 164 
CYS   H    H N N 165 
CYS   H2   H N N 166 
CYS   HA   H N N 167 
CYS   HB2  H N N 168 
CYS   HB3  H N N 169 
CYS   HG   H N N 170 
CYS   HXT  H N N 171 
GLN   N    N N N 172 
GLN   CA   C N S 173 
GLN   C    C N N 174 
GLN   O    O N N 175 
GLN   CB   C N N 176 
GLN   CG   C N N 177 
GLN   CD   C N N 178 
GLN   OE1  O N N 179 
GLN   NE2  N N N 180 
GLN   OXT  O N N 181 
GLN   H    H N N 182 
GLN   H2   H N N 183 
GLN   HA   H N N 184 
GLN   HB2  H N N 185 
GLN   HB3  H N N 186 
GLN   HG2  H N N 187 
GLN   HG3  H N N 188 
GLN   HE21 H N N 189 
GLN   HE22 H N N 190 
GLN   HXT  H N N 191 
GLU   N    N N N 192 
GLU   CA   C N S 193 
GLU   C    C N N 194 
GLU   O    O N N 195 
GLU   CB   C N N 196 
GLU   CG   C N N 197 
GLU   CD   C N N 198 
GLU   OE1  O N N 199 
GLU   OE2  O N N 200 
GLU   OXT  O N N 201 
GLU   H    H N N 202 
GLU   H2   H N N 203 
GLU   HA   H N N 204 
GLU   HB2  H N N 205 
GLU   HB3  H N N 206 
GLU   HG2  H N N 207 
GLU   HG3  H N N 208 
GLU   HE2  H N N 209 
GLU   HXT  H N N 210 
GLY   N    N N N 211 
GLY   CA   C N N 212 
GLY   C    C N N 213 
GLY   O    O N N 214 
GLY   OXT  O N N 215 
GLY   H    H N N 216 
GLY   H2   H N N 217 
GLY   HA2  H N N 218 
GLY   HA3  H N N 219 
GLY   HXT  H N N 220 
HIS   N    N N N 221 
HIS   CA   C N S 222 
HIS   C    C N N 223 
HIS   O    O N N 224 
HIS   CB   C N N 225 
HIS   CG   C Y N 226 
HIS   ND1  N Y N 227 
HIS   CD2  C Y N 228 
HIS   CE1  C Y N 229 
HIS   NE2  N Y N 230 
HIS   OXT  O N N 231 
HIS   H    H N N 232 
HIS   H2   H N N 233 
HIS   HA   H N N 234 
HIS   HB2  H N N 235 
HIS   HB3  H N N 236 
HIS   HD1  H N N 237 
HIS   HD2  H N N 238 
HIS   HE1  H N N 239 
HIS   HE2  H N N 240 
HIS   HXT  H N N 241 
HOH   O    O N N 242 
HOH   H1   H N N 243 
HOH   H2   H N N 244 
ILE   N    N N N 245 
ILE   CA   C N S 246 
ILE   C    C N N 247 
ILE   O    O N N 248 
ILE   CB   C N S 249 
ILE   CG1  C N N 250 
ILE   CG2  C N N 251 
ILE   CD1  C N N 252 
ILE   OXT  O N N 253 
ILE   H    H N N 254 
ILE   H2   H N N 255 
ILE   HA   H N N 256 
ILE   HB   H N N 257 
ILE   HG12 H N N 258 
ILE   HG13 H N N 259 
ILE   HG21 H N N 260 
ILE   HG22 H N N 261 
ILE   HG23 H N N 262 
ILE   HD11 H N N 263 
ILE   HD12 H N N 264 
ILE   HD13 H N N 265 
ILE   HXT  H N N 266 
LEU   N    N N N 267 
LEU   CA   C N S 268 
LEU   C    C N N 269 
LEU   O    O N N 270 
LEU   CB   C N N 271 
LEU   CG   C N N 272 
LEU   CD1  C N N 273 
LEU   CD2  C N N 274 
LEU   OXT  O N N 275 
LEU   H    H N N 276 
LEU   H2   H N N 277 
LEU   HA   H N N 278 
LEU   HB2  H N N 279 
LEU   HB3  H N N 280 
LEU   HG   H N N 281 
LEU   HD11 H N N 282 
LEU   HD12 H N N 283 
LEU   HD13 H N N 284 
LEU   HD21 H N N 285 
LEU   HD22 H N N 286 
LEU   HD23 H N N 287 
LEU   HXT  H N N 288 
LYS   N    N N N 289 
LYS   CA   C N S 290 
LYS   C    C N N 291 
LYS   O    O N N 292 
LYS   CB   C N N 293 
LYS   CG   C N N 294 
LYS   CD   C N N 295 
LYS   CE   C N N 296 
LYS   NZ   N N N 297 
LYS   OXT  O N N 298 
LYS   H    H N N 299 
LYS   H2   H N N 300 
LYS   HA   H N N 301 
LYS   HB2  H N N 302 
LYS   HB3  H N N 303 
LYS   HG2  H N N 304 
LYS   HG3  H N N 305 
LYS   HD2  H N N 306 
LYS   HD3  H N N 307 
LYS   HE2  H N N 308 
LYS   HE3  H N N 309 
LYS   HZ1  H N N 310 
LYS   HZ2  H N N 311 
LYS   HZ3  H N N 312 
LYS   HXT  H N N 313 
MET   N    N N N 314 
MET   CA   C N S 315 
MET   C    C N N 316 
MET   O    O N N 317 
MET   CB   C N N 318 
MET   CG   C N N 319 
MET   SD   S N N 320 
MET   CE   C N N 321 
MET   OXT  O N N 322 
MET   H    H N N 323 
MET   H2   H N N 324 
MET   HA   H N N 325 
MET   HB2  H N N 326 
MET   HB3  H N N 327 
MET   HG2  H N N 328 
MET   HG3  H N N 329 
MET   HE1  H N N 330 
MET   HE2  H N N 331 
MET   HE3  H N N 332 
MET   HXT  H N N 333 
PHE   N    N N N 334 
PHE   CA   C N S 335 
PHE   C    C N N 336 
PHE   O    O N N 337 
PHE   CB   C N N 338 
PHE   CG   C Y N 339 
PHE   CD1  C Y N 340 
PHE   CD2  C Y N 341 
PHE   CE1  C Y N 342 
PHE   CE2  C Y N 343 
PHE   CZ   C Y N 344 
PHE   OXT  O N N 345 
PHE   H    H N N 346 
PHE   H2   H N N 347 
PHE   HA   H N N 348 
PHE   HB2  H N N 349 
PHE   HB3  H N N 350 
PHE   HD1  H N N 351 
PHE   HD2  H N N 352 
PHE   HE1  H N N 353 
PHE   HE2  H N N 354 
PHE   HZ   H N N 355 
PHE   HXT  H N N 356 
PRO   N    N N N 357 
PRO   CA   C N S 358 
PRO   C    C N N 359 
PRO   O    O N N 360 
PRO   CB   C N N 361 
PRO   CG   C N N 362 
PRO   CD   C N N 363 
PRO   OXT  O N N 364 
PRO   H    H N N 365 
PRO   HA   H N N 366 
PRO   HB2  H N N 367 
PRO   HB3  H N N 368 
PRO   HG2  H N N 369 
PRO   HG3  H N N 370 
PRO   HD2  H N N 371 
PRO   HD3  H N N 372 
PRO   HXT  H N N 373 
SER   N    N N N 374 
SER   CA   C N S 375 
SER   C    C N N 376 
SER   O    O N N 377 
SER   CB   C N N 378 
SER   OG   O N N 379 
SER   OXT  O N N 380 
SER   H    H N N 381 
SER   H2   H N N 382 
SER   HA   H N N 383 
SER   HB2  H N N 384 
SER   HB3  H N N 385 
SER   HG   H N N 386 
SER   HXT  H N N 387 
THR   N    N N N 388 
THR   CA   C N S 389 
THR   C    C N N 390 
THR   O    O N N 391 
THR   CB   C N R 392 
THR   OG1  O N N 393 
THR   CG2  C N N 394 
THR   OXT  O N N 395 
THR   H    H N N 396 
THR   H2   H N N 397 
THR   HA   H N N 398 
THR   HB   H N N 399 
THR   HG1  H N N 400 
THR   HG21 H N N 401 
THR   HG22 H N N 402 
THR   HG23 H N N 403 
THR   HXT  H N N 404 
TYR   N    N N N 405 
TYR   CA   C N S 406 
TYR   C    C N N 407 
TYR   O    O N N 408 
TYR   CB   C N N 409 
TYR   CG   C Y N 410 
TYR   CD1  C Y N 411 
TYR   CD2  C Y N 412 
TYR   CE1  C Y N 413 
TYR   CE2  C Y N 414 
TYR   CZ   C Y N 415 
TYR   OH   O N N 416 
TYR   OXT  O N N 417 
TYR   H    H N N 418 
TYR   H2   H N N 419 
TYR   HA   H N N 420 
TYR   HB2  H N N 421 
TYR   HB3  H N N 422 
TYR   HD1  H N N 423 
TYR   HD2  H N N 424 
TYR   HE1  H N N 425 
TYR   HE2  H N N 426 
TYR   HH   H N N 427 
TYR   HXT  H N N 428 
VAL   N    N N N 429 
VAL   CA   C N S 430 
VAL   C    C N N 431 
VAL   O    O N N 432 
VAL   CB   C N N 433 
VAL   CG1  C N N 434 
VAL   CG2  C N N 435 
VAL   OXT  O N N 436 
VAL   H    H N N 437 
VAL   H2   H N N 438 
VAL   HA   H N N 439 
VAL   HB   H N N 440 
VAL   HG11 H N N 441 
VAL   HG12 H N N 442 
VAL   HG13 H N N 443 
VAL   HG21 H N N 444 
VAL   HG22 H N N 445 
VAL   HG23 H N N 446 
VAL   HXT  H N N 447 
# 
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 
A1BAY C15 C13  sing N N 1   
A1BAY C13 C12  sing N N 2   
A1BAY C13 C14  sing N N 3   
A1BAY C13 C4   sing N N 4   
A1BAY C12 C11  sing N N 5   
A1BAY C1  C2   sing N N 6   
A1BAY C4  C2   sing N N 7   
A1BAY C4  N1   sing N N 8   
A1BAY C2  O1   sing N N 9   
A1BAY C2  C3   sing N N 10  
A1BAY C11 N1   sing N N 11  
A1BAY N1  C5   sing N N 12  
A1BAY C5  N2   doub Y N 13  
A1BAY C5  C8   sing Y N 14  
A1BAY C9  C8   sing Y N 15  
A1BAY C9  C10  doub Y N 16  
A1BAY N2  C6   sing Y N 17  
A1BAY C8  C7   doub Y N 18  
A1BAY C10 N4   sing Y N 19  
A1BAY C6  N3   doub Y N 20  
A1BAY C7  N4   sing Y N 21  
A1BAY C7  N3   sing Y N 22  
A1BAY C3  H7   sing N N 23  
A1BAY C3  H5   sing N N 24  
A1BAY C3  H6   sing N N 25  
A1BAY C6  H9   sing N N 26  
A1BAY C9  H10  sing N N 27  
A1BAY C12 H15  sing N N 28  
A1BAY C12 H16  sing N N 29  
A1BAY C14 H17  sing N N 30  
A1BAY C14 H18  sing N N 31  
A1BAY C14 H19  sing N N 32  
A1BAY C1  H4   sing N N 33  
A1BAY C1  H3   sing N N 34  
A1BAY C1  H2   sing N N 35  
A1BAY C10 H11  sing N N 36  
A1BAY C11 H13  sing N N 37  
A1BAY C11 H14  sing N N 38  
A1BAY C15 H20  sing N N 39  
A1BAY C15 H21  sing N N 40  
A1BAY C15 H22  sing N N 41  
A1BAY C4  H1   sing N N 42  
A1BAY N4  H12  sing N N 43  
A1BAY O1  H8   sing N N 44  
A1BAZ C14 C13  sing N N 45  
A1BAZ C1  C2   sing N N 46  
A1BAZ C3  C2   sing N N 47  
A1BAZ C12 C13  sing N N 48  
A1BAZ C12 C11  sing N N 49  
A1BAZ C2  C4   sing N N 50  
A1BAZ C2  O1   sing N N 51  
A1BAZ C13 C4   sing N N 52  
A1BAZ C13 C15  sing N N 53  
A1BAZ C11 N1   sing N N 54  
A1BAZ C4  N1   sing N N 55  
A1BAZ N1  C5   sing N N 56  
A1BAZ C5  N2   doub Y N 57  
A1BAZ C5  C8   sing Y N 58  
A1BAZ C9  C8   sing Y N 59  
A1BAZ C9  C10  doub Y N 60  
A1BAZ N2  C6   sing Y N 61  
A1BAZ C8  C7   doub Y N 62  
A1BAZ C10 N4   sing Y N 63  
A1BAZ C6  N3   doub Y N 64  
A1BAZ C7  N4   sing Y N 65  
A1BAZ C7  N3   sing Y N 66  
A1BAZ O1  H8   sing N N 67  
A1BAZ C1  H2   sing N N 68  
A1BAZ C1  H3   sing N N 69  
A1BAZ C1  H4   sing N N 70  
A1BAZ C3  H6   sing N N 71  
A1BAZ C3  H5   sing N N 72  
A1BAZ C3  H7   sing N N 73  
A1BAZ C4  H1   sing N N 74  
A1BAZ C6  H9   sing N N 75  
A1BAZ C10 H11  sing N N 76  
A1BAZ C11 H13  sing N N 77  
A1BAZ C11 H14  sing N N 78  
A1BAZ C12 H15  sing N N 79  
A1BAZ C12 H16  sing N N 80  
A1BAZ C14 H18  sing N N 81  
A1BAZ C14 H17  sing N N 82  
A1BAZ C14 H19  sing N N 83  
A1BAZ C15 H20  sing N N 84  
A1BAZ C15 H21  sing N N 85  
A1BAZ C15 H22  sing N N 86  
A1BAZ C9  H10  sing N N 87  
A1BAZ N4  H12  sing N N 88  
ALA   N   CA   sing N N 89  
ALA   N   H    sing N N 90  
ALA   N   H2   sing N N 91  
ALA   CA  C    sing N N 92  
ALA   CA  CB   sing N N 93  
ALA   CA  HA   sing N N 94  
ALA   C   O    doub N N 95  
ALA   C   OXT  sing N N 96  
ALA   CB  HB1  sing N N 97  
ALA   CB  HB2  sing N N 98  
ALA   CB  HB3  sing N N 99  
ALA   OXT HXT  sing N N 100 
ARG   N   CA   sing N N 101 
ARG   N   H    sing N N 102 
ARG   N   H2   sing N N 103 
ARG   CA  C    sing N N 104 
ARG   CA  CB   sing N N 105 
ARG   CA  HA   sing N N 106 
ARG   C   O    doub N N 107 
ARG   C   OXT  sing N N 108 
ARG   CB  CG   sing N N 109 
ARG   CB  HB2  sing N N 110 
ARG   CB  HB3  sing N N 111 
ARG   CG  CD   sing N N 112 
ARG   CG  HG2  sing N N 113 
ARG   CG  HG3  sing N N 114 
ARG   CD  NE   sing N N 115 
ARG   CD  HD2  sing N N 116 
ARG   CD  HD3  sing N N 117 
ARG   NE  CZ   sing N N 118 
ARG   NE  HE   sing N N 119 
ARG   CZ  NH1  sing N N 120 
ARG   CZ  NH2  doub N N 121 
ARG   NH1 HH11 sing N N 122 
ARG   NH1 HH12 sing N N 123 
ARG   NH2 HH21 sing N N 124 
ARG   NH2 HH22 sing N N 125 
ARG   OXT HXT  sing N N 126 
ASN   N   CA   sing N N 127 
ASN   N   H    sing N N 128 
ASN   N   H2   sing N N 129 
ASN   CA  C    sing N N 130 
ASN   CA  CB   sing N N 131 
ASN   CA  HA   sing N N 132 
ASN   C   O    doub N N 133 
ASN   C   OXT  sing N N 134 
ASN   CB  CG   sing N N 135 
ASN   CB  HB2  sing N N 136 
ASN   CB  HB3  sing N N 137 
ASN   CG  OD1  doub N N 138 
ASN   CG  ND2  sing N N 139 
ASN   ND2 HD21 sing N N 140 
ASN   ND2 HD22 sing N N 141 
ASN   OXT HXT  sing N N 142 
ASP   N   CA   sing N N 143 
ASP   N   H    sing N N 144 
ASP   N   H2   sing N N 145 
ASP   CA  C    sing N N 146 
ASP   CA  CB   sing N N 147 
ASP   CA  HA   sing N N 148 
ASP   C   O    doub N N 149 
ASP   C   OXT  sing N N 150 
ASP   CB  CG   sing N N 151 
ASP   CB  HB2  sing N N 152 
ASP   CB  HB3  sing N N 153 
ASP   CG  OD1  doub N N 154 
ASP   CG  OD2  sing N N 155 
ASP   OD2 HD2  sing N N 156 
ASP   OXT HXT  sing N N 157 
CYS   N   CA   sing N N 158 
CYS   N   H    sing N N 159 
CYS   N   H2   sing N N 160 
CYS   CA  C    sing N N 161 
CYS   CA  CB   sing N N 162 
CYS   CA  HA   sing N N 163 
CYS   C   O    doub N N 164 
CYS   C   OXT  sing N N 165 
CYS   CB  SG   sing N N 166 
CYS   CB  HB2  sing N N 167 
CYS   CB  HB3  sing N N 168 
CYS   SG  HG   sing N N 169 
CYS   OXT HXT  sing N N 170 
GLN   N   CA   sing N N 171 
GLN   N   H    sing N N 172 
GLN   N   H2   sing N N 173 
GLN   CA  C    sing N N 174 
GLN   CA  CB   sing N N 175 
GLN   CA  HA   sing N N 176 
GLN   C   O    doub N N 177 
GLN   C   OXT  sing N N 178 
GLN   CB  CG   sing N N 179 
GLN   CB  HB2  sing N N 180 
GLN   CB  HB3  sing N N 181 
GLN   CG  CD   sing N N 182 
GLN   CG  HG2  sing N N 183 
GLN   CG  HG3  sing N N 184 
GLN   CD  OE1  doub N N 185 
GLN   CD  NE2  sing N N 186 
GLN   NE2 HE21 sing N N 187 
GLN   NE2 HE22 sing N N 188 
GLN   OXT HXT  sing N N 189 
GLU   N   CA   sing N N 190 
GLU   N   H    sing N N 191 
GLU   N   H2   sing N N 192 
GLU   CA  C    sing N N 193 
GLU   CA  CB   sing N N 194 
GLU   CA  HA   sing N N 195 
GLU   C   O    doub N N 196 
GLU   C   OXT  sing N N 197 
GLU   CB  CG   sing N N 198 
GLU   CB  HB2  sing N N 199 
GLU   CB  HB3  sing N N 200 
GLU   CG  CD   sing N N 201 
GLU   CG  HG2  sing N N 202 
GLU   CG  HG3  sing N N 203 
GLU   CD  OE1  doub N N 204 
GLU   CD  OE2  sing N N 205 
GLU   OE2 HE2  sing N N 206 
GLU   OXT HXT  sing N N 207 
GLY   N   CA   sing N N 208 
GLY   N   H    sing N N 209 
GLY   N   H2   sing N N 210 
GLY   CA  C    sing N N 211 
GLY   CA  HA2  sing N N 212 
GLY   CA  HA3  sing N N 213 
GLY   C   O    doub N N 214 
GLY   C   OXT  sing N N 215 
GLY   OXT HXT  sing N N 216 
HIS   N   CA   sing N N 217 
HIS   N   H    sing N N 218 
HIS   N   H2   sing N N 219 
HIS   CA  C    sing N N 220 
HIS   CA  CB   sing N N 221 
HIS   CA  HA   sing N N 222 
HIS   C   O    doub N N 223 
HIS   C   OXT  sing N N 224 
HIS   CB  CG   sing N N 225 
HIS   CB  HB2  sing N N 226 
HIS   CB  HB3  sing N N 227 
HIS   CG  ND1  sing Y N 228 
HIS   CG  CD2  doub Y N 229 
HIS   ND1 CE1  doub Y N 230 
HIS   ND1 HD1  sing N N 231 
HIS   CD2 NE2  sing Y N 232 
HIS   CD2 HD2  sing N N 233 
HIS   CE1 NE2  sing Y N 234 
HIS   CE1 HE1  sing N N 235 
HIS   NE2 HE2  sing N N 236 
HIS   OXT HXT  sing N N 237 
HOH   O   H1   sing N N 238 
HOH   O   H2   sing N N 239 
ILE   N   CA   sing N N 240 
ILE   N   H    sing N N 241 
ILE   N   H2   sing N N 242 
ILE   CA  C    sing N N 243 
ILE   CA  CB   sing N N 244 
ILE   CA  HA   sing N N 245 
ILE   C   O    doub N N 246 
ILE   C   OXT  sing N N 247 
ILE   CB  CG1  sing N N 248 
ILE   CB  CG2  sing N N 249 
ILE   CB  HB   sing N N 250 
ILE   CG1 CD1  sing N N 251 
ILE   CG1 HG12 sing N N 252 
ILE   CG1 HG13 sing N N 253 
ILE   CG2 HG21 sing N N 254 
ILE   CG2 HG22 sing N N 255 
ILE   CG2 HG23 sing N N 256 
ILE   CD1 HD11 sing N N 257 
ILE   CD1 HD12 sing N N 258 
ILE   CD1 HD13 sing N N 259 
ILE   OXT HXT  sing N N 260 
LEU   N   CA   sing N N 261 
LEU   N   H    sing N N 262 
LEU   N   H2   sing N N 263 
LEU   CA  C    sing N N 264 
LEU   CA  CB   sing N N 265 
LEU   CA  HA   sing N N 266 
LEU   C   O    doub N N 267 
LEU   C   OXT  sing N N 268 
LEU   CB  CG   sing N N 269 
LEU   CB  HB2  sing N N 270 
LEU   CB  HB3  sing N N 271 
LEU   CG  CD1  sing N N 272 
LEU   CG  CD2  sing N N 273 
LEU   CG  HG   sing N N 274 
LEU   CD1 HD11 sing N N 275 
LEU   CD1 HD12 sing N N 276 
LEU   CD1 HD13 sing N N 277 
LEU   CD2 HD21 sing N N 278 
LEU   CD2 HD22 sing N N 279 
LEU   CD2 HD23 sing N N 280 
LEU   OXT HXT  sing N N 281 
LYS   N   CA   sing N N 282 
LYS   N   H    sing N N 283 
LYS   N   H2   sing N N 284 
LYS   CA  C    sing N N 285 
LYS   CA  CB   sing N N 286 
LYS   CA  HA   sing N N 287 
LYS   C   O    doub N N 288 
LYS   C   OXT  sing N N 289 
LYS   CB  CG   sing N N 290 
LYS   CB  HB2  sing N N 291 
LYS   CB  HB3  sing N N 292 
LYS   CG  CD   sing N N 293 
LYS   CG  HG2  sing N N 294 
LYS   CG  HG3  sing N N 295 
LYS   CD  CE   sing N N 296 
LYS   CD  HD2  sing N N 297 
LYS   CD  HD3  sing N N 298 
LYS   CE  NZ   sing N N 299 
LYS   CE  HE2  sing N N 300 
LYS   CE  HE3  sing N N 301 
LYS   NZ  HZ1  sing N N 302 
LYS   NZ  HZ2  sing N N 303 
LYS   NZ  HZ3  sing N N 304 
LYS   OXT HXT  sing N N 305 
MET   N   CA   sing N N 306 
MET   N   H    sing N N 307 
MET   N   H2   sing N N 308 
MET   CA  C    sing N N 309 
MET   CA  CB   sing N N 310 
MET   CA  HA   sing N N 311 
MET   C   O    doub N N 312 
MET   C   OXT  sing N N 313 
MET   CB  CG   sing N N 314 
MET   CB  HB2  sing N N 315 
MET   CB  HB3  sing N N 316 
MET   CG  SD   sing N N 317 
MET   CG  HG2  sing N N 318 
MET   CG  HG3  sing N N 319 
MET   SD  CE   sing N N 320 
MET   CE  HE1  sing N N 321 
MET   CE  HE2  sing N N 322 
MET   CE  HE3  sing N N 323 
MET   OXT HXT  sing N N 324 
PHE   N   CA   sing N N 325 
PHE   N   H    sing N N 326 
PHE   N   H2   sing N N 327 
PHE   CA  C    sing N N 328 
PHE   CA  CB   sing N N 329 
PHE   CA  HA   sing N N 330 
PHE   C   O    doub N N 331 
PHE   C   OXT  sing N N 332 
PHE   CB  CG   sing N N 333 
PHE   CB  HB2  sing N N 334 
PHE   CB  HB3  sing N N 335 
PHE   CG  CD1  doub Y N 336 
PHE   CG  CD2  sing Y N 337 
PHE   CD1 CE1  sing Y N 338 
PHE   CD1 HD1  sing N N 339 
PHE   CD2 CE2  doub Y N 340 
PHE   CD2 HD2  sing N N 341 
PHE   CE1 CZ   doub Y N 342 
PHE   CE1 HE1  sing N N 343 
PHE   CE2 CZ   sing Y N 344 
PHE   CE2 HE2  sing N N 345 
PHE   CZ  HZ   sing N N 346 
PHE   OXT HXT  sing N N 347 
PRO   N   CA   sing N N 348 
PRO   N   CD   sing N N 349 
PRO   N   H    sing N N 350 
PRO   CA  C    sing N N 351 
PRO   CA  CB   sing N N 352 
PRO   CA  HA   sing N N 353 
PRO   C   O    doub N N 354 
PRO   C   OXT  sing N N 355 
PRO   CB  CG   sing N N 356 
PRO   CB  HB2  sing N N 357 
PRO   CB  HB3  sing N N 358 
PRO   CG  CD   sing N N 359 
PRO   CG  HG2  sing N N 360 
PRO   CG  HG3  sing N N 361 
PRO   CD  HD2  sing N N 362 
PRO   CD  HD3  sing N N 363 
PRO   OXT HXT  sing N N 364 
SER   N   CA   sing N N 365 
SER   N   H    sing N N 366 
SER   N   H2   sing N N 367 
SER   CA  C    sing N N 368 
SER   CA  CB   sing N N 369 
SER   CA  HA   sing N N 370 
SER   C   O    doub N N 371 
SER   C   OXT  sing N N 372 
SER   CB  OG   sing N N 373 
SER   CB  HB2  sing N N 374 
SER   CB  HB3  sing N N 375 
SER   OG  HG   sing N N 376 
SER   OXT HXT  sing N N 377 
THR   N   CA   sing N N 378 
THR   N   H    sing N N 379 
THR   N   H2   sing N N 380 
THR   CA  C    sing N N 381 
THR   CA  CB   sing N N 382 
THR   CA  HA   sing N N 383 
THR   C   O    doub N N 384 
THR   C   OXT  sing N N 385 
THR   CB  OG1  sing N N 386 
THR   CB  CG2  sing N N 387 
THR   CB  HB   sing N N 388 
THR   OG1 HG1  sing N N 389 
THR   CG2 HG21 sing N N 390 
THR   CG2 HG22 sing N N 391 
THR   CG2 HG23 sing N N 392 
THR   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_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                    7HFC 
_atom_sites.fract_transf_matrix[1][1]   0.011272 
_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]   0.011272 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025253 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
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   ? 19.714 -16.356 22.297  0.60 48.36 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.649 -16.334 22.361  0.40 48.01 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.748 -15.276 22.459  0.60 48.10 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.720 -15.227 22.555  0.40 47.77 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.408 -13.930 22.174  0.60 46.79 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.393 -13.904 22.214  0.40 46.62 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.524 -13.667 22.623  0.60 47.09 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.507 -13.632 22.662  0.40 46.93 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.102 -15.308 23.860  0.60 48.88 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.156 -15.213 23.990  0.40 48.42 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.083 -14.185 24.007  0.60 49.14 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.177 -14.059 24.168  0.40 48.64 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.449 -16.660 24.111  0.60 49.13 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.485 -16.540 24.310  0.40 48.63 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.038 -15.391 21.812  0.60 57.70 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.971 -15.335 21.951  0.40 57.30 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.788 -15.179 24.532  0.60 58.63 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.884 -15.087 24.618  0.40 58.08 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.566 -14.331 24.815  0.60 58.94 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.698 -14.178 25.003  0.40 58.34 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.550 -13.337 24.063  0.60 58.94 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.670 -13.224 24.187  0.40 58.34 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.494 -14.190 23.236  0.60 58.94 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.552 -14.059 23.427  0.40 58.34 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.989 -16.635 24.965  0.60 58.93 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.079 -16.485 25.189  0.40 58.33 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.816 -16.841 23.399  0.60 58.93 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.805 -16.718 23.642  0.40 58.33 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.136 -17.345 24.125  0.60 58.93 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.153 -17.243 24.298  0.40 58.33 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.713 -13.086 21.413  1.00 44.83 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.173 -11.743 21.084  1.00 40.86 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.033 -10.758 21.329  1.00 37.37 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.912 -11.144 21.677  1.00 36.93 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.718 -11.658 19.651  1.00 40.14 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.683 -12.012 18.606  1.00 39.39 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.588 -11.450 18.583  1.00 39.17 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.028 -12.950 17.728  1.00 39.06 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.951 -13.279 21.063  0.60 53.77 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.966 -13.294 21.041  0.40 53.77 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.897 -11.509 21.680  1.00 49.01 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.015 -10.749 19.480  1.00 48.14 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.461 -12.272 19.558  1.00 48.14 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.479 -13.189 17.110  1.00 46.85 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.803 -13.320 17.777  1.00 46.85 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.323 -9.472  21.134  1.00 34.19 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.423 -8.399  21.535  1.00 31.15 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.513 -7.909  20.412  1.00 27.05 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.777 -6.938  20.612  1.00 27.41 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.219 -7.230  22.123  1.00 32.18 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.160 -6.735  21.189  1.00 32.78 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.045 -9.196  20.756  1.00 41.00 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.852 -8.731  22.241  1.00 37.36 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.605 -6.516  22.361  1.00 38.59 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.692 -7.535  22.914  1.00 38.59 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.590 -6.092  21.525  1.00 39.31 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.550 -8.552  19.246  0.60 24.37 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.532 -8.547  19.247  0.40 25.10 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.651 -8.193  18.157  0.60 22.18 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.619 -8.147  18.184  0.40 23.38 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.223 -8.576  18.527  0.60 22.35 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.187 -8.482  18.582  0.40 23.38 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.976 -9.681  19.016  0.60 23.03 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.893 -9.609  18.990  0.40 23.77 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.068 -8.918  16.879  0.60 20.33 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 15.990 -8.836  16.874  0.40 21.98 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.347 -8.400  16.271  0.60 19.02 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.266 -8.324  16.269  0.40 20.93 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.359 -7.215  15.555  0.60 18.62 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.291 -7.116  15.591  0.40 20.57 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.531 -9.109  16.402  0.60 19.32 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.440 -9.047  16.384  0.40 20.94 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.530 -6.739  14.990  0.60 18.50 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.465 -6.640  15.036  0.40 20.48 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.703 -8.640  15.839  0.60 19.30 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.615 -8.578  15.831  0.40 20.84 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.702 -7.452  15.132  0.60 18.96 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.628 -7.372  15.156  0.40 20.66 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.085 -9.200  19.066  0.60 29.22 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.053 -9.201  19.050  0.40 30.10 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.686 -7.240  18.002  0.60 26.59 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.679 -7.191  18.055  0.40 28.04 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.196 -9.861  17.082  0.60 24.37 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.095 -9.787  17.039  0.40 26.35 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.365 -8.820  16.220  0.60 24.37 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.275 -8.692  16.234  0.40 26.35 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.569 -6.734  15.459  0.60 22.31 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.507 -6.619  15.509  0.40 24.66 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.536 -9.910  16.879  0.60 23.16 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.435 -9.859  16.839  0.40 25.10 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.525 -5.941  14.514  0.60 22.17 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.470 -5.828  14.582  0.40 24.55 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.494 -9.121  15.937  0.60 23.13 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.399 -9.072  15.915  0.40 24.98 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.490 -7.132  14.752  0.60 22.73 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.419 -7.054  14.784  0.40 24.77 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.278 -7.667  18.284  0.60 21.78 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.295 -7.501  18.458  0.40 22.94 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.903 -7.827  18.745  0.60 22.36 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.951 -7.581  19.015  0.40 23.00 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.918 -7.522  17.624  0.60 21.21 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.916 -7.450  17.908  0.40 21.79 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.145 -6.623  16.810  0.60 21.38 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.021 -6.567  17.051  0.40 21.79 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.628 -6.889  19.928  0.60 24.06 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.736 -6.474  20.051  0.40 24.03 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.269 -6.953  20.322  0.60 25.57 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.424 -6.516  20.575  0.40 25.01 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.414 -6.940  17.849  0.60 26.11 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.448 -6.763  18.041  0.40 27.50 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.759 -8.739  19.040  0.60 26.81 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.825 -8.437  19.450  0.40 27.57 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.182 -7.154  20.680  0.60 28.84 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.369 -6.595  20.776  0.40 28.82 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.845 -5.978  19.667  0.60 28.84 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 11.873 -5.613  19.630  0.40 28.82 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.132 -6.424  20.963  0.60 30.66 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.318 -5.911  21.148  0.40 29.99 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.817  -8.273  17.591  0.60 20.84 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.916  -8.328  17.933  0.40 21.04 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.741  -7.980  16.664  0.60 20.09 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.792  -8.220  17.032  0.40 20.37 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.942  -8.468  15.247  0.60 18.81 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 9.029  -8.725  15.632  0.40 19.36 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.245  -7.998  14.341  0.60 18.76 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.202  -8.457  14.752  0.40 19.67 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.676  -8.956  18.095  0.60 24.99 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.876  -9.003  18.461  0.40 25.23 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.922  -8.374  17.008  0.60 24.08 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 8.045  -8.713  17.397  0.40 24.42 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.614  -7.019  16.631  0.60 24.08 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.536  -7.291  16.953  0.40 24.42 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.867  -9.398  15.022  0.60 17.01 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 10.121 -9.444  15.390  0.40 18.13 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.114 -9.941  13.694  0.60 15.30 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.403 -9.940  14.053  0.40 17.06 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.231  -11.154 13.420  0.60 14.86 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.570  -11.177 13.745  0.40 16.38 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.853  -11.902 14.331  0.60 16.18 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 9.497  -12.116 14.547  0.40 16.78 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.580 -10.361 13.539  0.60 14.76 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.895 -10.232 13.892  0.40 16.69 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.524 -9.195  13.397  0.60 15.20 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.700 -8.980  13.633  0.40 15.91 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.883 -8.436  14.501  0.60 15.80 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.952 -8.075  14.653  0.40 16.07 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.039 -8.842  12.158  0.60 14.84 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.182 -8.689  12.362  0.40 15.21 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.733 -7.356  14.380  0.60 16.23 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.672 -6.921  14.420  0.40 15.85 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.891 -7.761  12.025  0.60 15.42 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.903 -7.535  12.119  0.40 15.13 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.230 -7.023  13.140  0.60 15.99 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.141 -6.657  13.151  0.40 15.22 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 15.074 -5.950  13.021  0.60 16.88 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 14.856 -5.512  12.907  0.40 15.44 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.366 -9.733  15.631  0.60 20.39 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.719 -9.655  15.979  0.40 21.73 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.920  -9.260  13.026  0.60 18.34 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 10.171 -9.258  13.407  0.40 20.45 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.845 -10.870 14.320  0.60 17.69 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 12.238 -10.656 14.696  0.40 20.01 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.659 -10.910 12.743  0.60 17.69 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 12.005 -10.820 13.132  0.40 20.01 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.540 -8.659  15.337  0.60 18.94 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.633 -8.252  15.509  0.40 19.26 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.804 -9.342  11.404  0.60 17.78 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 13.021 -9.282  11.664  0.40 18.23 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.968 -6.861  15.129  0.60 19.45 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 13.837 -6.325  15.114  0.40 19.00 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.238 -7.539  11.188  0.60 18.48 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.227 -7.353  11.264  0.40 18.14 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.202 -5.605  13.776  0.60 20.23 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.021 -5.111  13.627  0.40 18.50 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.916  -11.337 12.140  0.60 14.29 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.929  -11.161 12.581  0.40 15.49 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.311  -12.560 11.636  0.60 14.30 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.285  -12.351 12.055  0.40 15.04 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.430  -13.492 11.186  0.60 13.55 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.365  -13.301 11.552  0.40 13.90 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.401 -13.055 10.562  0.60 14.05 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.259 -12.900 10.801  0.40 13.71 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.426  -12.229 10.434  0.60 15.54 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.351  -11.957 10.912  0.40 16.13 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.661  -13.394 9.795   0.60 17.37 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.962  -13.094 9.960   0.40 17.86 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.579  -13.921 10.729  0.60 18.82 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.952  -14.033 10.598  0.40 18.64 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.065  -12.988 8.455   0.60 18.30 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 6.445  -12.525 8.666   0.40 18.44 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 9.059  -10.755 11.517  0.60 17.13 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 8.864  -10.472 12.070  0.40 18.56 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.781  -12.992 12.329  0.60 17.14 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.763  -12.790 12.749  0.40 18.03 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.770  -11.579 10.715  0.60 18.62 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.525  -11.597 11.291  0.40 19.34 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.989  -11.849 9.745   0.60 18.62 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.781  -11.265 10.383  0.40 19.34 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.281  -14.122 9.629   0.60 20.83 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 7.742  -13.620 9.735   0.40 21.40 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.144  -14.681 10.311  0.60 22.56 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 5.919  -14.851 10.079  0.40 22.34 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.988  -14.192 11.565  0.60 22.56 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 6.227  -14.227 11.508  0.40 22.34 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.932  -13.216 10.890  0.60 22.56 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 5.083  -13.605 10.602  0.40 22.34 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.589  -13.745 8.081   0.60 21.94 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 6.193  -13.260 8.089   0.40 22.11 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.460  -12.246 8.593   0.60 21.94 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 5.681  -11.966 8.856   0.40 22.11 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.786  -12.724 7.861   0.60 21.94 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 7.152  -12.004 8.255   0.40 22.11 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.288  -14.776 11.497  0.60 13.24 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.298  -14.553 11.982  0.40 13.15 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.303 -15.775 11.194  0.60 13.44 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.234 -15.569 11.525  0.40 12.98 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.970  -16.388 9.840   0.60 13.35 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.824  -16.047 10.137  0.40 12.11 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.912  -17.002 9.685   0.60 14.93 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.698  -16.514 9.945   0.40 12.31 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.304 -16.831 12.302  0.60 13.65 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.253 -16.730 12.514  0.40 13.56 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.349 -17.920 12.180  0.60 14.44 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.246 -17.824 12.171  0.40 14.31 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.486 -18.671 13.508  0.60 14.49 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.240 -18.917 13.234  0.40 14.81 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.431 -19.862 13.398  0.60 14.24 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.368 -19.925 13.038  0.40 14.69 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.793 -19.478 12.936  0.60 14.30 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.724 -19.319 13.186  0.40 14.45 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.577  -15.110 11.851  0.60 15.87 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.720  -14.829 12.551  0.40 15.75 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.177 -15.365 11.150  0.60 16.11 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.119 -15.183 11.467  0.40 15.56 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.457 -16.381 13.150  0.60 16.36 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.485 -16.377 13.389  0.40 16.25 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.436  -17.262 12.321  0.60 16.36 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.367  -17.121 12.545  0.40 16.25 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.073 -18.555 11.499  0.60 17.30 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.000 -18.224 11.321  0.40 17.15 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.203 -17.528 11.958  0.60 17.30 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 12.135 -17.446 12.122  0.40 17.15 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.837 -18.064 14.181  0.60 17.37 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.344 -18.509 14.107  0.40 17.75 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.614 -19.000 13.782  0.60 17.37 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.395 -19.396 13.190  0.40 17.75 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.519 -20.278 14.269  0.60 17.06 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.281 -20.627 13.700  0.40 17.61 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.068 -20.496 12.762  0.60 17.06 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.304 -20.299 12.146  0.40 17.61 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.311 -20.201 12.887  0.60 17.14 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 14.344 -19.894 12.911  0.40 17.32 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.746 -19.102 12.131  0.60 17.14 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.781 -18.576 12.699  0.40 17.32 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.156 -18.900 13.506  0.60 17.14 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.874 -19.119 14.039  0.40 17.32 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.851 -16.212 8.854   0.60 12.29 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.718 -15.905 9.162   0.40 12.16 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.599 -16.799 7.538   0.60 12.75 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.467 -16.440 7.828   0.40 12.44 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.188 -18.194 7.382   0.60 12.98 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 11.020 -17.851 7.669   0.40 12.01 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.562 -19.058 6.762   0.60 12.96 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.340 -18.730 7.128   0.40 11.95 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.151 -15.907 6.423   0.60 13.23 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.061 -15.518 6.760   0.40 12.92 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.504 -14.537 6.236   0.60 13.97 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.395 -14.148 6.641   0.40 13.05 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.265 -13.757 5.174   0.60 14.59 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 11.013 -13.329 5.508   0.40 13.61 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 9.035  -14.672 5.859   0.60 14.66 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 8.900  -14.311 6.433   0.40 13.14 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.586 -15.757 8.915   0.60 14.72 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.459 -15.476 9.242   0.40 14.57 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.643  -16.868 7.413   0.60 15.27 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.509  -16.486 7.683   0.40 14.91 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.094 -15.758 6.594   0.60 15.85 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 11.999 -15.368 6.965   0.40 15.48 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 11.053 -16.386 5.583   0.60 15.85 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 10.985 -15.953 5.897   0.40 15.48 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.560 -14.045 7.068   0.60 16.74 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.534 -13.657 7.467   0.40 15.64 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.850 -12.890 5.059   0.60 17.48 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.576 -12.462 5.466   0.40 16.31 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.187 -13.647 5.464   0.60 17.48 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 11.962 -13.208 5.681   0.40 16.31 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.241 -14.251 4.339   0.60 17.48 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 10.889 -13.801 4.669   0.40 16.31 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.680  -13.794 5.653   0.60 17.57 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.538  -13.483 6.088   0.40 15.75 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.960  -15.249 5.082   0.60 17.57 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.750  -15.031 5.801   0.40 15.75 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.551  -15.059 6.605   0.60 17.57 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.488  -14.526 7.284   0.40 15.75 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.399 -18.410 7.889   0.60 13.28 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.250 -18.075 8.121   0.40 11.88 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 13.088 -19.692 7.803   0.60 13.56 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 12.898 -19.376 8.031   0.40 12.25 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.866 -19.898 9.097   0.60 13.40 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.661 -19.622 9.328   0.40 12.52 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.760 -19.117 10.047  0.60 13.31 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.580 -18.847 10.286  0.40 12.93 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 14.055 -19.747 6.612   0.60 14.46 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.854 -19.447 6.831   0.40 12.67 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.138 -18.843 6.853   0.60 14.63 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 14.915 -18.508 7.022   0.40 12.50 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.380 -19.365 5.310   0.60 15.65 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.136 -19.162 5.511   0.40 13.64 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.860 -17.808 8.285   0.60 15.91 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.742 -17.469 8.485   0.40 14.23 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.441 -20.413 7.710   0.60 16.25 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.222 -20.062 7.923   0.40 14.68 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.406 -20.650 6.520   0.60 17.33 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.235 -20.332 6.779   0.40 15.19 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.678 -18.865 6.206   0.60 17.53 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.440 -18.523 6.364   0.40 14.97 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.970 -19.558 4.564   0.60 18.76 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.757 -19.263 4.768   0.40 16.34 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.561 -19.870 5.203   0.60 18.76 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.406 -19.791 5.391   0.40 16.34 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.171 -18.418 5.313   0.60 18.76 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.784 -18.262 5.505   0.40 16.34 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.694 -20.944 9.113   0.60 13.54 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.424 -20.712 9.346   0.40 12.81 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.512 -21.223 10.284  0.60 14.15 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.293 -20.992 10.481  0.40 13.76 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.333 -20.015 10.722  0.60 13.82 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.183 -19.796 10.799  0.40 13.39 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.588 -19.848 11.919  0.60 14.20 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.404 -19.472 11.972  0.40 13.87 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.446 -22.397 9.995   0.60 16.72 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.161 -22.206 10.159  0.40 15.83 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.383 -22.679 11.143  0.60 20.38 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 17.034 -22.633 11.326  0.40 18.28 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.905 -23.193 12.178  0.60 21.96 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.486 -22.946 12.405  0.40 18.85 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.587 -22.369 11.007  0.60 22.75 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.268 -22.681 11.156  0.40 20.05 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.807 -21.499 8.463   0.60 16.22 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.453 -21.286 8.716   0.40 15.35 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.943 -21.475 11.025  0.60 16.96 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.741 -21.196 11.257  0.40 16.48 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.908 -23.197 9.826   0.60 20.04 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.579 -22.939 9.900   0.40 18.98 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.988 -22.200 9.218   0.60 20.04 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.748 -21.974 9.424   0.40 18.98 ?  14  ASP   A HB3  1 
ATOM   347  N N    A ASN   A 1 15  ? 16.768 -19.170 9.780   0.60 13.60 ?  15  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 15  ? 16.686 -19.112 9.765   0.40 13.23 ?  15  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 15  ? 17.720 -18.107 10.095  0.60 13.82 ?  15  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 15  ? 17.741 -18.114 9.933   0.40 13.57 ?  15  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 15  ? 17.332 -16.722 9.600   0.60 13.08 ?  15  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 15  ? 17.400 -16.728 9.389   0.40 13.77 ?  15  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 15  ? 18.030 -15.762 9.951   0.60 12.55 ?  15  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 15  ? 18.291 -15.871 9.339   0.40 13.92 ?  15  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 15  ? 19.109 -18.430 9.517   0.60 14.03 ?  15  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 15  ? 19.069 -18.612 9.334   0.40 13.34 ?  15  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 15  ? 19.090 -18.542 8.010   0.60 13.90 ?  15  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 15  ? 19.057 -18.669 7.813   0.40 13.67 ?  15  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 15  ? 18.347 -19.346 7.450   0.60 14.78 ?  15  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 15  ? 18.345 -19.476 7.219   0.40 14.31 ?  15  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 15  ? 19.870 -17.705 7.340   0.60 14.01 ?  15  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 15  ? 19.872 -17.828 7.177   0.40 13.76 ?  15  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 15  ? 16.528 -19.192 8.956   0.60 16.29 ?  15  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 15  ? 16.425 -19.215 8.960   0.40 15.86 ?  15  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 15  ? 17.820 -18.051 11.062  0.60 16.56 ?  15  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 15  ? 17.894 -18.007 10.881  0.40 16.26 ?  15  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 15  ? 19.729 -17.715 9.763   0.60 16.81 ?  15  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 15  ? 19.782 -18.011 9.603   0.40 15.98 ?  15  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 15  ? 19.421 -19.271 9.884   0.60 16.81 ?  15  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 15  ? 19.252 -19.507 9.662   0.40 15.98 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 15  ? 19.882 -17.730 6.481   0.60 16.79 ?  15  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 15  ? 19.915 -17.828 6.315   0.40 16.49 ?  15  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 15  ? 20.379 -17.152 7.761   0.60 16.79 ?  15  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 15  ? 20.366 -17.285 7.626   0.40 16.49 ?  15  ASN   A HD22 1 
ATOM   375  N N    A VAL   A 1 16  ? 16.286 -16.585 8.779   0.60 12.80 ?  16  VAL   A N    1 
ATOM   376  N N    B VAL   A 1 16  ? 16.149 -16.460 9.011   0.40 13.48 ?  16  VAL   A N    1 
ATOM   377  C CA   A VAL   A 1 16  ? 15.876 -15.306 8.202   0.60 12.85 ?  16  VAL   A CA   1 
ATOM   378  C CA   B VAL   A 1 16  ? 15.768 -15.169 8.443   0.40 13.05 ?  16  VAL   A CA   1 
ATOM   379  C C    A VAL   A 1 16  ? 14.591 -14.823 8.865   0.60 12.63 ?  16  VAL   A C    1 
ATOM   380  C C    B VAL   A 1 16  ? 14.532 -14.644 9.162   0.40 12.74 ?  16  VAL   A C    1 
ATOM   381  O O    A VAL   A 1 16  ? 13.584 -15.544 8.912   0.60 12.26 ?  16  VAL   A O    1 
ATOM   382  O O    B VAL   A 1 16  ? 13.539 -15.365 9.318   0.40 12.92 ?  16  VAL   A O    1 
ATOM   383  C CB   A VAL   A 1 16  ? 15.706 -15.378 6.674   0.60 13.80 ?  16  VAL   A CB   1 
ATOM   384  C CB   B VAL   A 1 16  ? 15.543 -15.246 6.919   0.40 13.44 ?  16  VAL   A CB   1 
ATOM   385  C CG1  A VAL   A 1 16  ? 15.286 -14.012 6.127   0.60 14.27 ?  16  VAL   A CG1  1 
ATOM   386  C CG1  B VAL   A 1 16  ? 15.102 -13.894 6.362   0.40 13.82 ?  16  VAL   A CG1  1 
ATOM   387  C CG2  A VAL   A 1 16  ? 16.987 -15.847 6.006   0.60 14.61 ?  16  VAL   A CG2  1 
ATOM   388  C CG2  B VAL   A 1 16  ? 16.809 -15.726 6.215   0.40 14.26 ?  16  VAL   A CG2  1 
ATOM   389  H H    A VAL   A 1 16  ? 15.801 -17.249 8.533   0.60 15.33 ?  16  VAL   A H    1 
ATOM   390  H H    B VAL   A 1 16  ? 15.491 -17.009 9.081   0.40 16.15 ?  16  VAL   A H    1 
ATOM   391  H HA   A VAL   A 1 16  ? 16.573 -14.654 8.384   0.60 15.39 ?  16  VAL   A HA   1 
ATOM   392  H HA   B VAL   A 1 16  ? 16.480 -14.529 8.599   0.40 15.64 ?  16  VAL   A HA   1 
ATOM   393  H HB   A VAL   A 1 16  ? 15.009 -16.021 6.465   0.60 16.53 ?  16  VAL   A HB   1 
ATOM   394  H HB   B VAL   A 1 16  ? 14.843 -15.888 6.737   0.40 16.11 ?  16  VAL   A HB   1 
ATOM   395  H HG11 A VAL   A 1 16  ? 15.370 -14.021 5.163   0.60 17.10 ?  16  VAL   A HG11 1 
ATOM   396  H HG11 B VAL   A 1 16  ? 15.164 -13.922 5.393   0.40 16.56 ?  16  VAL   A HG11 1 
ATOM   397  H HG12 A VAL   A 1 16  ? 14.362 -13.844 6.376   0.60 17.10 ?  16  VAL   A HG12 1 
ATOM   398  H HG12 B VAL   A 1 16  ? 14.185 -13.728 6.628   0.40 16.56 ?  16  VAL   A HG12 1 
ATOM   399  H HG13 A VAL   A 1 16  ? 15.861 -13.331 6.506   0.60 17.10 ?  16  VAL   A HG13 1 
ATOM   400  H HG13 B VAL   A 1 16  ? 15.684 -13.204 6.711   0.40 16.56 ?  16  VAL   A HG13 1 
ATOM   401  H HG21 A VAL   A 1 16  ? 16.879 -15.785 5.044   0.60 17.50 ?  16  VAL   A HG21 1 
ATOM   402  H HG21 B VAL   A 1 16  ? 16.658 -15.727 5.257   0.40 17.08 ?  16  VAL   A HG21 1 
ATOM   403  H HG22 A VAL   A 1 16  ? 17.718 -15.277 6.294   0.60 17.50 ?  16  VAL   A HG22 1 
ATOM   404  H HG22 B VAL   A 1 16  ? 17.541 -15.127 6.433   0.40 17.08 ?  16  VAL   A HG22 1 
ATOM   405  H HG23 A VAL   A 1 16  ? 17.162 -16.765 6.263   0.60 17.50 ?  16  VAL   A HG23 1 
ATOM   406  H HG23 B VAL   A 1 16  ? 17.019 -16.624 6.518   0.40 17.08 ?  16  VAL   A HG23 1 
ATOM   407  N N    A TYR   A 1 17  ? 14.624 -13.570 9.313   0.60 12.91 ?  17  TYR   A N    1 
ATOM   408  N N    B TYR   A 1 17  ? 14.598 -13.379 9.582   0.40 12.25 ?  17  TYR   A N    1 
ATOM   409  C CA   A TYR   A 1 17  ? 13.536 -12.889 9.991   0.60 12.66 ?  17  TYR   A CA   1 
ATOM   410  C CA   B TYR   A 1 17  ? 13.559 -12.707 10.345  0.40 11.92 ?  17  TYR   A CA   1 
ATOM   411  C C    A TYR   A 1 17  ? 13.274 -11.570 9.270   0.60 12.73 ?  17  TYR   A C    1 
ATOM   412  C C    B TYR   A 1 17  ? 13.288 -11.359 9.698   0.40 11.52 ?  17  TYR   A C    1 
ATOM   413  O O    A TYR   A 1 17  ? 14.166 -11.017 8.625   0.60 12.31 ?  17  TYR   A O    1 
ATOM   414  O O    B TYR   A 1 17  ? 14.193 -10.750 9.127   0.40 11.28 ?  17  TYR   A O    1 
ATOM   415  C CB   A TYR   A 1 17  ? 13.933 -12.622 11.448  0.60 13.14 ?  17  TYR   A CB   1 
ATOM   416  C CB   B TYR   A 1 17  ? 14.036 -12.493 11.781  0.40 12.60 ?  17  TYR   A CB   1 
ATOM   417  C CG   A TYR   A 1 17  ? 14.154 -13.883 12.263  0.60 14.36 ?  17  TYR   A CG   1 
ATOM   418  C CG   B TYR   A 1 17  ? 14.178 -13.780 12.558  0.40 13.34 ?  17  TYR   A CG   1 
ATOM   419  C CD1  A TYR   A 1 17  ? 15.338 -14.608 12.174  0.60 15.29 ?  17  TYR   A CD1  1 
ATOM   420  C CD1  B TYR   A 1 17  ? 15.320 -14.567 12.449  0.40 13.89 ?  17  TYR   A CD1  1 
ATOM   421  C CD2  A TYR   A 1 17  ? 13.168 -14.356 13.118  0.60 14.71 ?  17  TYR   A CD2  1 
ATOM   422  C CD2  B TYR   A 1 17  ? 13.161 -14.218 13.390  0.40 13.60 ?  17  TYR   A CD2  1 
ATOM   423  C CE1  A TYR   A 1 17  ? 15.529 -15.769 12.919  0.60 16.10 ?  17  TYR   A CE1  1 
ATOM   424  C CE1  B TYR   A 1 17  ? 15.440 -15.753 13.159  0.40 14.30 ?  17  TYR   A CE1  1 
ATOM   425  C CE2  A TYR   A 1 17  ? 13.351 -15.512 13.865  0.60 15.74 ?  17  TYR   A CE2  1 
ATOM   426  C CE2  B TYR   A 1 17  ? 13.272 -15.397 14.100  0.40 14.13 ?  17  TYR   A CE2  1 
ATOM   427  C CZ   A TYR   A 1 17  ? 14.533 -16.211 13.762  0.60 16.13 ?  17  TYR   A CZ   1 
ATOM   428  C CZ   B TYR   A 1 17  ? 14.410 -16.160 13.984  0.40 14.11 ?  17  TYR   A CZ   1 
ATOM   429  O OH   A TYR   A 1 17  ? 14.714 -17.356 14.505  0.60 17.05 ?  17  TYR   A OH   1 
ATOM   430  O OH   B TYR   A 1 17  ? 14.506 -17.332 14.696  0.40 14.66 ?  17  TYR   A OH   1 
ATOM   431  H H    A TYR   A 1 17  ? 15.318 -13.074 9.217   0.60 15.47 ?  17  TYR   A H    1 
ATOM   432  H H    B TYR   A 1 17  ? 15.270 -12.858 9.420   0.40 14.68 ?  17  TYR   A H    1 
ATOM   433  H HA   A TYR   A 1 17  ? 12.740 -13.442 9.968   0.60 15.17 ?  17  TYR   A HA   1 
ATOM   434  H HA   B TYR   A 1 17  ? 12.742 -13.223 10.346  0.40 14.28 ?  17  TYR   A HA   1 
ATOM   435  H HB2  A TYR   A 1 17  ? 14.759 -12.114 11.460  0.60 15.75 ?  17  TYR   A HB2  1 
ATOM   436  H HB2  B TYR   A 1 17  ? 14.901 -12.057 11.760  0.40 15.10 ?  17  TYR   A HB2  1 
ATOM   437  H HB3  A TYR   A 1 17  ? 13.227 -12.116 11.872  0.60 15.75 ?  17  TYR   A HB3  1 
ATOM   438  H HB3  B TYR   A 1 17  ? 13.401 -11.933 12.246  0.40 15.10 ?  17  TYR   A HB3  1 
ATOM   439  H HD1  A TYR   A 1 17  ? 16.015 -14.317 11.609  0.60 18.32 ?  17  TYR   A HD1  1 
ATOM   440  H HD1  B TYR   A 1 17  ? 16.017 -14.293 11.892  0.40 16.64 ?  17  TYR   A HD1  1 
ATOM   441  H HD2  A TYR   A 1 17  ? 12.367 -13.890 13.194  0.60 17.63 ?  17  TYR   A HD2  1 
ATOM   442  H HD2  B TYR   A 1 17  ? 12.391 -13.706 13.474  0.40 16.30 ?  17  TYR   A HD2  1 
ATOM   443  H HE1  A TYR   A 1 17  ? 16.328 -16.247 12.856  0.60 19.29 ?  17  TYR   A HE1  1 
ATOM   444  H HE1  B TYR   A 1 17  ? 16.213 -16.270 13.079  0.40 17.13 ?  17  TYR   A HE1  1 
ATOM   445  H HE2  A TYR   A 1 17  ? 12.678 -15.811 14.437  0.60 18.86 ?  17  TYR   A HE2  1 
ATOM   446  H HE2  B TYR   A 1 17  ? 12.582 -15.671 14.656  0.40 16.93 ?  17  TYR   A HE2  1 
ATOM   447  H HH   A TYR   A 1 17  ? 15.479 -17.678 14.371  0.60 20.44 ?  17  TYR   A HH   1 
ATOM   448  H HH   B TYR   A 1 17  ? 13.756 -17.532 15.014  0.40 17.57 ?  17  TYR   A HH   1 
ATOM   449  N N    A ILE   A 1 18  ? 12.051 -11.047 9.381   0.60 12.99 ?  18  ILE   A N    1 
ATOM   450  N N    B ILE   A 1 18  ? 12.045 -10.882 9.782   0.40 11.30 ?  18  ILE   A N    1 
ATOM   451  C CA   A ILE   A 1 18  ? 11.667 -9.859  8.617   0.60 13.22 ?  18  ILE   A CA   1 
ATOM   452  C CA   B ILE   A 1 18  ? 11.663 -9.661  9.082   0.40 11.23 ?  18  ILE   A CA   1 
ATOM   453  C C    A ILE   A 1 18  ? 10.685 -9.014  9.422   0.60 13.85 ?  18  ILE   A C    1 
ATOM   454  C C    B ILE   A 1 18  ? 10.747 -8.810  9.949   0.40 11.57 ?  18  ILE   A C    1 
ATOM   455  O O    A ILE   A 1 18  ? 9.857  -9.540  10.171  0.60 14.05 ?  18  ILE   A O    1 
ATOM   456  O O    B ILE   A 1 18  ? 9.930  -9.322  10.722  0.40 11.80 ?  18  ILE   A O    1 
ATOM   457  C CB   A ILE   A 1 18  ? 11.117 -10.262 7.228   0.60 13.08 ?  18  ILE   A CB   1 
ATOM   458  C CB   B ILE   A 1 18  ? 11.028 -9.970  7.709   0.40 10.72 ?  18  ILE   A CB   1 
ATOM   459  C CG1  A ILE   A 1 18  ? 11.020 -9.049  6.306   0.60 13.55 ?  18  ILE   A CG1  1 
ATOM   460  C CG1  B ILE   A 1 18  ? 10.957 -8.712  6.843   0.40 11.16 ?  18  ILE   A CG1  1 
ATOM   461  C CG2  A ILE   A 1 18  ? 9.779  -11.001 7.365   0.60 13.02 ?  18  ILE   A CG2  1 
ATOM   462  C CG2  B ILE   A 1 18  ? 9.652  -10.612 7.885   0.40 11.45 ?  18  ILE   A CG2  1 
ATOM   463  C CD1  A ILE   A 1 18  ? 10.739 -9.416  4.866   0.60 15.06 ?  18  ILE   A CD1  1 
ATOM   464  C CD1  B ILE   A 1 18  ? 10.725 -9.010  5.380   0.40 12.35 ?  18  ILE   A CD1  1 
ATOM   465  H H    A ILE   A 1 18  ? 11.441 -11.367 9.892   0.60 15.57 ?  18  ILE   A H    1 
ATOM   466  H H    B ILE   A 1 18  ? 11.409 -11.247 10.235  0.40 13.54 ?  18  ILE   A H    1 
ATOM   467  H HA   A ILE   A 1 18  ? 12.462 -9.328  8.470   0.60 15.84 ?  18  ILE   A HA   1 
ATOM   468  H HA   B ILE   A 1 18  ? 12.467 -9.143  8.918   0.40 13.45 ?  18  ILE   A HA   1 
ATOM   469  H HB   A ILE   A 1 18  ? 11.751 -10.884 6.829   0.60 15.67 ?  18  ILE   A HB   1 
ATOM   470  H HB   B ILE   A 1 18  ? 11.598 -10.606 7.259   0.40 12.84 ?  18  ILE   A HB   1 
ATOM   471  H HG12 A ILE   A 1 18  ? 10.304 -8.478  6.614   0.60 16.24 ?  18  ILE   A HG12 1 
ATOM   472  H HG12 B ILE   A 1 18  ? 10.227 -8.152  7.151   0.40 13.37 ?  18  ILE   A HG12 1 
ATOM   473  H HG13 A ILE   A 1 18  ? 11.864 -8.571  6.329   0.60 16.24 ?  18  ILE   A HG13 1 
ATOM   474  H HG13 B ILE   A 1 18  ? 11.796 -8.228  6.916   0.40 13.37 ?  18  ILE   A HG13 1 
ATOM   475  H HG21 A ILE   A 1 18  ? 9.537  -11.380 6.502   0.60 15.60 ?  18  ILE   A HG21 1 
ATOM   476  H HG21 B ILE   A 1 18  ? 9.323  -10.892 7.017   0.40 13.72 ?  18  ILE   A HG21 1 
ATOM   477  H HG22 A ILE   A 1 18  ? 9.875  -11.713 8.018   0.60 15.60 ?  18  ILE   A HG22 1 
ATOM   478  H HG22 B ILE   A 1 18  ? 9.736  -11.379 8.470   0.40 13.72 ?  18  ILE   A HG22 1 
ATOM   479  H HG23 A ILE   A 1 18  ? 9.099  -10.376 7.653   0.60 15.60 ?  18  ILE   A HG23 1 
ATOM   480  H HG23 B ILE   A 1 18  ? 9.042  -9.965  8.275   0.40 13.72 ?  18  ILE   A HG23 1 
ATOM   481  H HD11 A ILE   A 1 18  ? 10.752 -8.608  4.328   0.60 18.04 ?  18  ILE   A HD11 1 
ATOM   482  H HD11 B ILE   A 1 18  ? 10.725 -8.179  4.880   0.40 14.80 ?  18  ILE   A HD11 1 
ATOM   483  H HD12 A ILE   A 1 18  ? 11.420 -10.031 4.556   0.60 18.04 ?  18  ILE   A HD12 1 
ATOM   484  H HD12 B ILE   A 1 18  ? 11.436 -9.589  5.058   0.40 14.80 ?  18  ILE   A HD12 1 
ATOM   485  H HD13 A ILE   A 1 18  ? 9.865  -9.833  4.812   0.60 18.04 ?  18  ILE   A HD13 1 
ATOM   486  H HD13 B ILE   A 1 18  ? 9.869  -9.456  5.280   0.40 14.80 ?  18  ILE   A HD13 1 
ATOM   487  N N    A LYS   A 1 19  ? 10.766 -7.691  9.241   0.60 14.20 ?  19  LYS   A N    1 
ATOM   488  N N    B LYS   A 1 19  ? 10.884 -7.492  9.799   0.40 11.98 ?  19  LYS   A N    1 
ATOM   489  C CA   A LYS   A 1 19  ? 9.964  -6.742  10.009  0.60 14.90 ?  19  LYS   A CA   1 
ATOM   490  C CA   B LYS   A 1 19  ? 10.093 -6.537  10.559  0.40 13.29 ?  19  LYS   A CA   1 
ATOM   491  C C    A LYS   A 1 19  ? 9.751  -5.468  9.200   0.60 15.14 ?  19  LYS   A C    1 
ATOM   492  C C    B LYS   A 1 19  ? 9.880  -5.297  9.705   0.40 14.03 ?  19  LYS   A C    1 
ATOM   493  O O    A LYS   A 1 19  ? 10.623 -5.055  8.431   0.60 14.66 ?  19  LYS   A O    1 
ATOM   494  O O    B LYS   A 1 19  ? 10.778 -4.889  8.965   0.40 14.02 ?  19  LYS   A O    1 
ATOM   495  C CB   A LYS   A 1 19  ? 10.686 -6.386  11.317  0.60 15.74 ?  19  LYS   A CB   1 
ATOM   496  C CB   B LYS   A 1 19  ? 10.817 -6.158  11.856  0.40 13.67 ?  19  LYS   A CB   1 
ATOM   497  C CG   A LYS   A 1 19  ? 9.950  -5.463  12.287  0.60 16.99 ?  19  LYS   A CG   1 
ATOM   498  C CG   B LYS   A 1 19  ? 10.067 -5.206  12.752  0.40 15.01 ?  19  LYS   A CG   1 
ATOM   499  C CD   A LYS   A 1 19  ? 10.816 -5.230  13.532  0.60 17.96 ?  19  LYS   A CD   1 
ATOM   500  C CD   B LYS   A 1 19  ? 10.917 -4.852  13.954  0.40 16.29 ?  19  LYS   A CD   1 
ATOM   501  C CE   A LYS   A 1 19  ? 10.193 -4.261  14.530  0.60 18.65 ?  19  LYS   A CE   1 
ATOM   502  C CE   B LYS   A 1 19  ? 10.177 -3.940  14.907  0.40 17.28 ?  19  LYS   A CE   1 
ATOM   503  N NZ   A LYS   A 1 19  ? 11.069 -4.055  15.730  0.60 18.84 ?  19  LYS   A NZ   1 
ATOM   504  N NZ   B LYS   A 1 19  ? 10.982 -3.687  16.128  0.40 17.66 ?  19  LYS   A NZ   1 
ATOM   505  H H    A LYS   A 1 19  ? 11.296 -7.323  8.671   0.60 17.01 ?  19  LYS   A H    1 
ATOM   506  H H    B LYS   A 1 19  ? 11.447 -7.115  9.256   0.40 14.35 ?  19  LYS   A H    1 
ATOM   507  H HA   A LYS   A 1 19  ? 9.104  -7.144  10.216  0.60 17.86 ?  19  LYS   A HA   1 
ATOM   508  H HA   B LYS   A 1 19  ? 9.235  -6.920  10.781  0.40 15.92 ?  19  LYS   A HA   1 
ATOM   509  H HB2  A LYS   A 1 19  ? 10.866 -7.210  11.788  0.60 18.86 ?  19  LYS   A HB2  1 
ATOM   510  H HB2  B LYS   A 1 19  ? 10.980 -6.964  12.371  0.40 16.38 ?  19  LYS   A HB2  1 
ATOM   511  H HB3  A LYS   A 1 19  ? 11.522 -5.954  11.085  0.60 18.86 ?  19  LYS   A HB3  1 
ATOM   512  H HB3  B LYS   A 1 19  ? 11.663 -5.737  11.636  0.40 16.38 ?  19  LYS   A HB3  1 
ATOM   513  H HG2  A LYS   A 1 19  ? 9.782  -4.606  11.862  0.60 20.37 ?  19  LYS   A HG2  1 
ATOM   514  H HG2  B LYS   A 1 19  ? 9.865  -4.390  12.269  0.40 17.99 ?  19  LYS   A HG2  1 
ATOM   515  H HG3  A LYS   A 1 19  ? 9.115  -5.875  12.562  0.60 20.37 ?  19  LYS   A HG3  1 
ATOM   516  H HG3  B LYS   A 1 19  ? 9.251  -5.628  13.065  0.40 17.99 ?  19  LYS   A HG3  1 
ATOM   517  H HD2  A LYS   A 1 19  ? 10.949 -6.078  13.986  0.60 21.52 ?  19  LYS   A HD2  1 
ATOM   518  H HD2  B LYS   A 1 19  ? 11.150 -5.665  14.429  0.40 19.52 ?  19  LYS   A HD2  1 
ATOM   519  H HD3  A LYS   A 1 19  ? 11.672 -4.866  13.258  0.60 21.52 ?  19  LYS   A HD3  1 
ATOM   520  H HD3  B LYS   A 1 19  ? 11.719 -4.396  13.654  0.40 19.52 ?  19  LYS   A HD3  1 
ATOM   521  H HE2  A LYS   A 1 19  ? 10.064 -3.398  14.104  0.60 22.36 ?  19  LYS   A HE2  1 
ATOM   522  H HE2  B LYS   A 1 19  ? 10.005 -3.091  14.469  0.40 20.72 ?  19  LYS   A HE2  1 
ATOM   523  H HE3  A LYS   A 1 19  ? 9.344  -4.613  14.837  0.60 22.36 ?  19  LYS   A HE3  1 
ATOM   524  H HE3  B LYS   A 1 19  ? 9.342  -4.360  15.168  0.40 20.72 ?  19  LYS   A HE3  1 
ATOM   525  H HZ1  A LYS   A 1 19  ? 10.688 -3.480  16.293  0.60 22.59 ?  19  LYS   A HZ1  1 
ATOM   526  H HZ1  B LYS   A 1 19  ? 10.535 -3.151  16.678  0.40 21.17 ?  19  LYS   A HZ1  1 
ATOM   527  H HZ2  A LYS   A 1 19  ? 11.196 -4.830  16.151  0.60 22.59 ?  19  LYS   A HZ2  1 
ATOM   528  H HZ2  B LYS   A 1 19  ? 11.150 -4.456  16.543  0.40 21.17 ?  19  LYS   A HZ2  1 
ATOM   529  H HZ3  A LYS   A 1 19  ? 11.859 -3.732  15.479  0.60 22.59 ?  19  LYS   A HZ3  1 
ATOM   530  H HZ3  B LYS   A 1 19  ? 11.753 -3.302  15.907  0.40 21.17 ?  19  LYS   A HZ3  1 
ATOM   531  N N    A ASN   A 1 20  ? 8.582  -4.847  9.380   0.60 16.46 ?  20  ASN   A N    1 
ATOM   532  N N    B ASN   A 1 20  ? 8.686  -4.716  9.792   0.40 15.28 ?  20  ASN   A N    1 
ATOM   533  C CA   A ASN   A 1 20  ? 8.321  -3.516  8.838   0.60 18.04 ?  20  ASN   A CA   1 
ATOM   534  C CA   B ASN   A 1 20  ? 8.417  -3.420  9.174   0.40 16.55 ?  20  ASN   A CA   1 
ATOM   535  C C    A ASN   A 1 20  ? 8.940  -2.510  9.798   0.60 18.78 ?  20  ASN   A C    1 
ATOM   536  C C    B ASN   A 1 20  ? 9.036  -2.364  10.076  0.40 17.24 ?  20  ASN   A C    1 
ATOM   537  O O    A ASN   A 1 20  ? 8.422  -2.290  10.897  0.60 19.67 ?  20  ASN   A O    1 
ATOM   538  O O    B ASN   A 1 20  ? 8.479  -2.013  11.118  0.40 17.93 ?  20  ASN   A O    1 
ATOM   539  C CB   A ASN   A 1 20  ? 6.815  -3.296  8.691   0.60 19.32 ?  20  ASN   A CB   1 
ATOM   540  C CB   B ASN   A 1 20  ? 6.916  -3.204  9.018   0.40 17.42 ?  20  ASN   A CB   1 
ATOM   541  C CG   A ASN   A 1 20  ? 6.457  -1.882  8.238   0.60 20.63 ?  20  ASN   A CG   1 
ATOM   542  C CG   B ASN   A 1 20  ? 6.552  -1.749  8.763   0.40 18.11 ?  20  ASN   A CG   1 
ATOM   543  O OD1  A ASN   A 1 20  ? 5.423  -1.332  8.642   0.60 22.06 ?  20  ASN   A OD1  1 
ATOM   544  O OD1  B ASN   A 1 20  ? 5.791  -1.146  9.523   0.40 18.62 ?  20  ASN   A OD1  1 
ATOM   545  N ND2  A ASN   A 1 20  ? 7.299  -1.291  7.395   0.60 21.23 ?  20  ASN   A ND2  1 
ATOM   546  N ND2  B ASN   A 1 20  ? 7.094  -1.179  7.691   0.40 18.30 ?  20  ASN   A ND2  1 
ATOM   547  H H    A ASN   A 1 20  ? 7.920  -5.182  9.821   0.60 19.73 ?  20  ASN   A H    1 
ATOM   548  H H    B ASN   A 1 20  ? 8.012  -5.057  10.199  0.40 18.32 ?  20  ASN   A H    1 
ATOM   549  H HA   A ASN   A 1 20  ? 8.738  -3.430  7.968   0.60 21.62 ?  20  ASN   A HA   1 
ATOM   550  H HA   B ASN   A 1 20  ? 8.836  -3.377  8.298   0.40 19.83 ?  20  ASN   A HA   1 
ATOM   551  H HB2  A ASN   A 1 20  ? 6.464  -3.913  8.033   0.60 23.16 ?  20  ASN   A HB2  1 
ATOM   552  H HB2  B ASN   A 1 20  ? 6.597  -3.729  8.268   0.40 20.89 ?  20  ASN   A HB2  1 
ATOM   553  H HB3  A ASN   A 1 20  ? 6.390  -3.453  9.549   0.60 23.16 ?  20  ASN   A HB3  1 
ATOM   554  H HB3  B ASN   A 1 20  ? 6.471  -3.485  9.833   0.40 20.89 ?  20  ASN   A HB3  1 
ATOM   555  H HD21 A ASN   A 1 20  ? 7.138  -0.495  7.117   0.60 25.46 ?  20  ASN   A HD21 1 
ATOM   556  H HD21 B ASN   A 1 20  ? 6.920  -0.358  7.502   0.40 21.93 ?  20  ASN   A HD21 1 
ATOM   557  H HD22 A ASN   A 1 20  ? 8.006  -1.703  7.130   0.60 25.46 ?  20  ASN   A HD22 1 
ATOM   558  H HD22 B ASN   A 1 20  ? 7.624  -1.632  7.185   0.40 21.93 ?  20  ASN   A HD22 1 
ATOM   559  N N    A ALA   A 1 21  ? 10.070 -1.926  9.409   0.60 18.79 ?  21  ALA   A N    1 
ATOM   560  N N    B ALA   A 1 21  ? 10.208 -1.868  9.689   0.40 17.62 ?  21  ALA   A N    1 
ATOM   561  C CA   A ALA   A 1 21  ? 10.787 -1.040  10.314  0.60 18.59 ?  21  ALA   A CA   1 
ATOM   562  C CA   B ALA   A 1 21  ? 10.898 -0.890  10.514  0.40 17.66 ?  21  ALA   A CA   1 
ATOM   563  C C    A ALA   A 1 21  ? 11.754 -0.168  9.529   0.60 17.97 ?  21  ALA   A C    1 
ATOM   564  C C    B ALA   A 1 21  ? 11.985 -0.213  9.698   0.40 16.98 ?  21  ALA   A C    1 
ATOM   565  O O    A ALA   A 1 21  ? 12.181 -0.525  8.429   0.60 17.78 ?  21  ALA   A O    1 
ATOM   566  O O    B ALA   A 1 21  ? 12.490 -0.769  8.721   0.40 16.90 ?  21  ALA   A O    1 
ATOM   567  C CB   A ALA   A 1 21  ? 11.547 -1.832  11.384  0.60 19.41 ?  21  ALA   A CB   1 
ATOM   568  C CB   B ALA   A 1 21  ? 11.507 -1.538  11.762  0.40 18.67 ?  21  ALA   A CB   1 
ATOM   569  H H    A ALA   A 1 21  ? 10.434 -2.025  8.635   0.60 22.52 ?  21  ALA   A H    1 
ATOM   570  H H    B ALA   A 1 21  ? 10.621 -2.080  8.962   0.40 21.12 ?  21  ALA   A H    1 
ATOM   571  H HA   A ALA   A 1 21  ? 10.149 -0.461  10.760  0.60 22.29 ?  21  ALA   A HA   1 
ATOM   572  H HA   B ALA   A 1 21  ? 10.267 -0.213  10.800  0.40 21.17 ?  21  ALA   A HA   1 
ATOM   573  H HB1  A ALA   A 1 21  ? 11.983 -1.206  11.981  0.60 23.27 ?  21  ALA   A HB1  1 
ATOM   574  H HB1  B ALA   A 1 21  ? 11.955 -0.855  12.284  0.40 22.38 ?  21  ALA   A HB1  1 
ATOM   575  H HB2  A ALA   A 1 21  ? 10.911 -2.374  11.882  0.60 23.27 ?  21  ALA   A HB2  1 
ATOM   576  H HB2  B ALA   A 1 21  ? 10.796 -1.941  12.286  0.40 22.38 ?  21  ALA   A HB2  1 
ATOM   577  H HB3  A ALA   A 1 21  ? 12.200 -2.399  10.953  0.60 23.27 ?  21  ALA   A HB3  1 
ATOM   578  H HB3  B ALA   A 1 21  ? 12.142 -2.217  11.488  0.40 22.38 ?  21  ALA   A HB3  1 
ATOM   579  N N    A ASP   A 1 22  ? 12.064 0.991   10.111  0.60 18.02 ?  22  ASP   A N    1 
ATOM   580  N N    B ASP   A 1 22  ? 12.315 1.007   10.110  0.40 16.86 ?  22  ASP   A N    1 
ATOM   581  C CA   A ASP   A 1 22  ? 13.118 1.869   9.623   0.60 17.62 ?  22  ASP   A CA   1 
ATOM   582  C CA   B ASP   A 1 22  ? 13.479 1.705   9.591   0.40 16.63 ?  22  ASP   A CA   1 
ATOM   583  C C    A ASP   A 1 22  ? 14.438 1.379   10.199  0.60 16.38 ?  22  ASP   A C    1 
ATOM   584  C C    B ASP   A 1 22  ? 14.729 1.048   10.163  0.40 15.00 ?  22  ASP   A C    1 
ATOM   585  O O    A ASP   A 1 22  ? 14.624 1.380   11.420  0.60 16.72 ?  22  ASP   A O    1 
ATOM   586  O O    B ASP   A 1 22  ? 14.857 0.900   11.382  0.40 14.93 ?  22  ASP   A O    1 
ATOM   587  C CB   A ASP   A 1 22  ? 12.829 3.299   10.081  0.60 18.76 ?  22  ASP   A CB   1 
ATOM   588  C CB   B ASP   A 1 22  ? 13.409 3.165   10.044  0.40 17.75 ?  22  ASP   A CB   1 
ATOM   589  C CG   A ASP   A 1 22  ? 13.908 4.299   9.661   0.60 19.55 ?  22  ASP   A CG   1 
ATOM   590  C CG   B ASP   A 1 22  ? 14.406 4.060   9.337   0.40 18.51 ?  22  ASP   A CG   1 
ATOM   591  O OD1  A ASP   A 1 22  ? 14.972 3.894   9.146   0.60 19.50 ?  22  ASP   A OD1  1 
ATOM   592  O OD1  B ASP   A 1 22  ? 15.430 3.546   8.847   0.40 18.08 ?  22  ASP   A OD1  1 
ATOM   593  O OD2  A ASP   A 1 22  ? 13.679 5.514   9.859   0.60 20.91 -1 22  ASP   A OD2  1 
ATOM   594  O OD2  B ASP   A 1 22  ? 14.175 5.287   9.284   0.40 19.72 -1 22  ASP   A OD2  1 
ATOM   595  H H    A ASP   A 1 22  ? 11.656 1.295   10.806  0.60 21.60 ?  22  ASP   A H    1 
ATOM   596  H H    B ASP   A 1 22  ? 11.868 1.454   10.694  0.40 20.21 ?  22  ASP   A H    1 
ATOM   597  H HA   A ASP   A 1 22  ? 13.156 1.841   8.653   0.60 21.12 ?  22  ASP   A HA   1 
ATOM   598  H HA   B ASP   A 1 22  ? 13.494 1.656   8.618   0.40 19.93 ?  22  ASP   A HA   1 
ATOM   599  H HB2  A ASP   A 1 22  ? 11.975 3.581   9.707   0.60 22.48 ?  22  ASP   A HB2  1 
ATOM   600  H HB2  B ASP   A 1 22  ? 12.518 3.501   9.879   0.40 21.27 ?  22  ASP   A HB2  1 
ATOM   601  H HB3  A ASP   A 1 22  ? 12.780 3.312   11.049  0.60 22.48 ?  22  ASP   A HB3  1 
ATOM   602  H HB3  B ASP   A 1 22  ? 13.619 3.205   10.986  0.40 21.27 ?  22  ASP   A HB3  1 
ATOM   603  N N    A ILE   A 1 23  ? 15.345 0.945   9.322   0.60 15.75 ?  23  ILE   A N    1 
ATOM   604  N N    B ILE   A 1 23  ? 15.644 0.629   9.283   0.40 14.37 ?  23  ILE   A N    1 
ATOM   605  C CA   A ILE   A 1 23  ? 16.604 0.362   9.773   0.60 14.71 ?  23  ILE   A CA   1 
ATOM   606  C CA   B ILE   A 1 23  ? 16.871 -0.021  9.738   0.40 14.19 ?  23  ILE   A CA   1 
ATOM   607  C C    A ILE   A 1 23  ? 17.382 1.335   10.647  0.60 14.48 ?  23  ILE   A C    1 
ATOM   608  C C    B ILE   A 1 23  ? 17.635 0.884   10.696  0.40 14.50 ?  23  ILE   A C    1 
ATOM   609  O O    A ILE   A 1 23  ? 18.101 0.917   11.562  0.60 14.13 ?  23  ILE   A O    1 
ATOM   610  O O    B ILE   A 1 23  ? 18.312 0.406   11.614  0.40 14.29 ?  23  ILE   A O    1 
ATOM   611  C CB   A ILE   A 1 23  ? 17.422 -0.136  8.563   0.60 14.48 ?  23  ILE   A CB   1 
ATOM   612  C CB   B ILE   A 1 23  ? 17.736 -0.480  8.541   0.40 13.53 ?  23  ILE   A CB   1 
ATOM   613  C CG1  A ILE   A 1 23  ? 18.553 -1.053  9.028   0.60 14.42 ?  23  ILE   A CG1  1 
ATOM   614  C CG1  B ILE   A 1 23  ? 18.787 -1.492  9.011   0.40 13.30 ?  23  ILE   A CG1  1 
ATOM   615  C CG2  A ILE   A 1 23  ? 17.950 1.042   7.740   0.60 14.45 ?  23  ILE   A CG2  1 
ATOM   616  C CG2  B ILE   A 1 23  ? 18.400 0.713   7.844   0.40 13.74 ?  23  ILE   A CG2  1 
ATOM   617  C CD1  A ILE   A 1 23  ? 19.284 -1.736  7.893   0.60 14.05 ?  23  ILE   A CD1  1 
ATOM   618  C CD1  B ILE   A 1 23  ? 19.658 -2.056  7.903   0.40 13.16 ?  23  ILE   A CD1  1 
ATOM   619  H H    A ILE   A 1 23  ? 15.248 0.976   8.472   0.60 18.88 ?  23  ILE   A H    1 
ATOM   620  H H    B ILE   A 1 23  ? 15.578 0.708   8.437   0.40 17.22 ?  23  ILE   A H    1 
ATOM   621  H HA   A ILE   A 1 23  ? 16.403 -0.409  10.319  0.60 17.63 ?  23  ILE   A HA   1 
ATOM   622  H HA   B ILE   A 1 23  ? 16.623 -0.818  10.226  0.40 17.00 ?  23  ILE   A HA   1 
ATOM   623  H HB   A ILE   A 1 23  ? 16.831 -0.654  7.997   0.60 17.35 ?  23  ILE   A HB   1 
ATOM   624  H HB   B ILE   A 1 23  ? 17.159 -0.924  7.897   0.40 16.21 ?  23  ILE   A HB   1 
ATOM   625  H HG12 A ILE   A 1 23  ? 19.200 -0.530  9.524   0.60 17.28 ?  23  ILE   A HG12 1 
ATOM   626  H HG12 B ILE   A 1 23  ? 19.370 -1.060  9.652   0.40 15.93 ?  23  ILE   A HG12 1 
ATOM   627  H HG13 A ILE   A 1 23  ? 18.181 -1.745  9.598   0.60 17.28 ?  23  ILE   A HG13 1 
ATOM   628  H HG13 B ILE   A 1 23  ? 18.330 -2.237  9.432   0.40 15.93 ?  23  ILE   A HG13 1 
ATOM   629  H HG21 A ILE   A 1 23  ? 18.294 0.707   6.894   0.60 17.32 ?  23  ILE   A HG21 1 
ATOM   630  H HG21 B ILE   A 1 23  ? 18.758 0.420   6.987   0.40 16.47 ?  23  ILE   A HG21 1 
ATOM   631  H HG22 A ILE   A 1 23  ? 17.223 1.663   7.574   0.60 17.32 ?  23  ILE   A HG22 1 
ATOM   632  H HG22 B ILE   A 1 23  ? 17.736 1.404   7.700   0.40 16.47 ?  23  ILE   A HG22 1 
ATOM   633  H HG23 A ILE   A 1 23  ? 18.658 1.485   8.231   0.60 17.32 ?  23  ILE   A HG23 1 
ATOM   634  H HG23 B ILE   A 1 23  ? 19.117 1.050   8.401   0.40 16.47 ?  23  ILE   A HG23 1 
ATOM   635  H HD11 A ILE   A 1 23  ? 19.933 -2.353  8.262   0.60 16.83 ?  23  ILE   A HD11 1 
ATOM   636  H HD11 B ILE   A 1 23  ? 20.226 -2.754  8.273   0.40 15.76 ?  23  ILE   A HD11 1 
ATOM   637  H HD12 A ILE   A 1 23  ? 18.639 -2.218  7.350   0.60 16.83 ?  23  ILE   A HD12 1 
ATOM   638  H HD12 B ILE   A 1 23  ? 19.091 -2.428  7.210   0.40 15.76 ?  23  ILE   A HD12 1 
ATOM   639  H HD13 A ILE   A 1 23  ? 19.731 -1.064  7.356   0.60 16.83 ?  23  ILE   A HD13 1 
ATOM   640  H HD13 B ILE   A 1 23  ? 20.207 -1.346  7.536   0.40 15.76 ?  23  ILE   A HD13 1 
ATOM   641  N N    A VAL   A 1 24  ? 17.239 2.638   10.400  0.60 15.31 ?  24  VAL   A N    1 
ATOM   642  N N    B VAL   A 1 24  ? 17.524 2.200   10.514  0.40 15.41 ?  24  VAL   A N    1 
ATOM   643  C CA   A VAL   A 1 24  ? 17.911 3.633   11.232  0.60 16.40 ?  24  VAL   A CA   1 
ATOM   644  C CA   B VAL   A 1 24  ? 18.201 3.139   11.404  0.40 16.52 ?  24  VAL   A CA   1 
ATOM   645  C C    A VAL   A 1 24  ? 17.401 3.553   12.663  0.60 17.09 ?  24  VAL   A C    1 
ATOM   646  C C    B VAL   A 1 24  ? 17.632 3.040   12.814  0.40 17.16 ?  24  VAL   A C    1 
ATOM   647  O O    A VAL   A 1 24  ? 18.182 3.500   13.620  0.60 17.12 ?  24  VAL   A O    1 
ATOM   648  O O    B VAL   A 1 24  ? 18.375 3.049   13.803  0.40 17.52 ?  24  VAL   A O    1 
ATOM   649  C CB   A VAL   A 1 24  ? 17.717 5.042   10.645  0.60 17.35 ?  24  VAL   A CB   1 
ATOM   650  C CB   B VAL   A 1 24  ? 18.096 4.565   10.833  0.40 16.76 ?  24  VAL   A CB   1 
ATOM   651  C CG1  A VAL   A 1 24  ? 18.238 6.102   11.612  0.60 17.85 ?  24  VAL   A CG1  1 
ATOM   652  C CG1  B VAL   A 1 24  ? 18.764 5.559   11.760  0.40 17.31 ?  24  VAL   A CG1  1 
ATOM   653  C CG2  A VAL   A 1 24  ? 18.406 5.153   9.298   0.60 18.04 ?  24  VAL   A CG2  1 
ATOM   654  C CG2  B VAL   A 1 24  ? 18.710 4.623   9.439   0.40 16.67 ?  24  VAL   A CG2  1 
ATOM   655  H H    A VAL   A 1 24  ? 16.765 2.971   9.766   0.60 18.35 ?  24  VAL   A H    1 
ATOM   656  H H    B VAL   A 1 24  ? 17.068 2.567   9.890   0.40 18.47 ?  24  VAL   A H    1 
ATOM   657  H HA   A VAL   A 1 24  ? 18.859 3.447   11.248  0.60 19.66 ?  24  VAL   A HA   1 
ATOM   658  H HA   B VAL   A 1 24  ? 19.142 2.906   11.446  0.40 19.80 ?  24  VAL   A HA   1 
ATOM   659  H HB   A VAL   A 1 24  ? 16.770 5.203   10.509  0.60 20.80 ?  24  VAL   A HB   1 
ATOM   660  H HB   B VAL   A 1 24  ? 17.160 4.805   10.756  0.40 20.09 ?  24  VAL   A HB   1 
ATOM   661  H HG11 A VAL   A 1 24  ? 18.364 6.933   11.129  0.60 21.40 ?  24  VAL   A HG11 1 
ATOM   662  H HG11 B VAL   A 1 24  ? 19.002 6.349   11.252  0.40 20.75 ?  24  VAL   A HG11 1 
ATOM   663  H HG12 A VAL   A 1 24  ? 17.591 6.229   12.324  0.60 21.40 ?  24  VAL   A HG12 1 
ATOM   664  H HG12 B VAL   A 1 24  ? 18.138 5.793   12.459  0.40 20.75 ?  24  VAL   A HG12 1 
ATOM   665  H HG13 A VAL   A 1 24  ? 19.084 5.802   11.980  0.60 21.40 ?  24  VAL   A HG13 1 
ATOM   666  H HG13 B VAL   A 1 24  ? 19.559 5.155   12.139  0.40 20.75 ?  24  VAL   A HG13 1 
ATOM   667  H HG21 A VAL   A 1 24  ? 18.195 6.015   8.908   0.60 21.62 ?  24  VAL   A HG21 1 
ATOM   668  H HG21 B VAL   A 1 24  ? 18.677 5.537   9.118   0.40 19.98 ?  24  VAL   A HG21 1 
ATOM   669  H HG22 A VAL   A 1 24  ? 19.363 5.074   9.428   0.60 21.62 ?  24  VAL   A HG22 1 
ATOM   670  H HG22 B VAL   A 1 24  ? 19.630 4.323   9.487   0.40 19.98 ?  24  VAL   A HG22 1 
ATOM   671  H HG23 A VAL   A 1 24  ? 18.087 4.442   8.721   0.60 21.62 ?  24  VAL   A HG23 1 
ATOM   672  H HG23 B VAL   A 1 24  ? 18.206 4.046   8.843   0.40 19.98 ?  24  VAL   A HG23 1 
ATOM   673  N N    A GLU   A 1 25  ? 16.076 3.555   12.829  0.60 18.07 ?  25  GLU   A N    1 
ATOM   674  N N    B GLU   A 1 25  ? 16.306 2.926   12.926  0.40 17.56 ?  25  GLU   A N    1 
ATOM   675  C CA   A GLU   A 1 25  ? 15.504 3.503   14.170  0.60 19.37 ?  25  GLU   A CA   1 
ATOM   676  C CA   B GLU   A 1 25  ? 15.670 2.826   14.235  0.40 18.44 ?  25  GLU   A CA   1 
ATOM   677  C C    A GLU   A 1 25  ? 15.738 2.145   14.816  0.60 18.29 ?  25  GLU   A C    1 
ATOM   678  C C    B GLU   A 1 25  ? 15.962 1.483   14.895  0.40 17.47 ?  25  GLU   A C    1 
ATOM   679  O O    A GLU   A 1 25  ? 15.969 2.060   16.027  0.60 18.89 ?  25  GLU   A O    1 
ATOM   680  O O    B GLU   A 1 25  ? 16.194 1.421   16.108  0.40 17.63 ?  25  GLU   A O    1 
ATOM   681  C CB   A GLU   A 1 25  ? 14.015 3.854   14.122  0.60 21.54 ?  25  GLU   A CB   1 
ATOM   682  C CB   B GLU   A 1 25  ? 14.165 3.061   14.096  0.40 19.79 ?  25  GLU   A CB   1 
ATOM   683  C CG   A GLU   A 1 25  ? 13.752 5.307   13.757  0.60 24.06 ?  25  GLU   A CG   1 
ATOM   684  C CG   B GLU   A 1 25  ? 13.811 4.464   13.628  0.40 21.61 ?  25  GLU   A CG   1 
ATOM   685  C CD   A GLU   A 1 25  ? 14.543 6.270   14.617  0.60 26.07 ?  25  GLU   A CD   1 
ATOM   686  C CD   B GLU   A 1 25  ? 14.244 5.535   14.614  0.40 23.26 ?  25  GLU   A CD   1 
ATOM   687  O OE1  A GLU   A 1 25  ? 14.576 6.078   15.850  0.60 26.60 ?  25  GLU   A OE1  1 
ATOM   688  O OE1  B GLU   A 1 25  ? 14.190 5.282   15.837  0.40 23.67 ?  25  GLU   A OE1  1 
ATOM   689  O OE2  A GLU   A 1 25  ? 15.155 7.202   14.054  0.60 27.03 -1 25  GLU   A OE2  1 
ATOM   690  O OE2  B GLU   A 1 25  ? 14.650 6.629   14.166  0.40 24.33 -1 25  GLU   A OE2  1 
ATOM   691  H H    A GLU   A 1 25  ? 15.497 3.593   12.191  0.60 21.67 ?  25  GLU   A H    1 
ATOM   692  H H    B GLU   A 1 25  ? 15.763 2.901   12.264  0.40 21.04 ?  25  GLU   A H    1 
ATOM   693  H HA   A GLU   A 1 25  ? 15.948 4.160   14.723  0.60 23.22 ?  25  GLU   A HA   1 
ATOM   694  H HA   B GLU   A 1 25  ? 16.026 3.517   14.810  0.40 22.10 ?  25  GLU   A HA   1 
ATOM   695  H HB2  A GLU   A 1 25  ? 13.576 3.302   13.455  0.60 25.82 ?  25  GLU   A HB2  1 
ATOM   696  H HB2  B GLU   A 1 25  ? 13.806 2.434   13.447  0.40 23.72 ?  25  GLU   A HB2  1 
ATOM   697  H HB3  A GLU   A 1 25  ? 13.620 3.694   14.994  0.60 25.82 ?  25  GLU   A HB3  1 
ATOM   698  H HB3  B GLU   A 1 25  ? 13.742 2.921   14.956  0.40 23.72 ?  25  GLU   A HB3  1 
ATOM   699  H HG2  A GLU   A 1 25  ? 14.017 5.459   12.838  0.60 28.85 ?  25  GLU   A HG2  1 
ATOM   700  H HG2  B GLU   A 1 25  ? 14.264 4.643   12.790  0.40 25.90 ?  25  GLU   A HG2  1 
ATOM   701  H HG3  A GLU   A 1 25  ? 12.806 5.500   13.869  0.60 28.85 ?  25  GLU   A HG3  1 
ATOM   702  H HG3  B GLU   A 1 25  ? 12.848 4.521   13.502  0.40 25.90 ?  25  GLU   A HG3  1 
ATOM   703  N N    A GLU   A 1 26  ? 15.688 1.072   14.025  0.60 17.64 ?  26  GLU   A N    1 
ATOM   704  N N    B GLU   A 1 26  ? 15.959 0.396   14.118  0.40 16.92 ?  26  GLU   A N    1 
ATOM   705  C CA   A GLU   A 1 26  ? 16.015 -0.250  14.549  0.60 17.75 ?  26  GLU   A CA   1 
ATOM   706  C CA   B GLU   A 1 26  ? 16.356 -0.895  14.672  0.40 16.45 ?  26  GLU   A CA   1 
ATOM   707  C C    A GLU   A 1 26  ? 17.448 -0.286  15.066  0.60 17.13 ?  26  GLU   A C    1 
ATOM   708  C C    B GLU   A 1 26  ? 17.781 -0.842  15.205  0.40 16.12 ?  26  GLU   A C    1 
ATOM   709  O O    A GLU   A 1 26  ? 17.714 -0.787  16.164  0.60 16.85 ?  26  GLU   A O    1 
ATOM   710  O O    B GLU   A 1 26  ? 18.064 -1.351  16.296  0.40 15.92 ?  26  GLU   A O    1 
ATOM   711  C CB   A GLU   A 1 26  ? 15.828 -1.299  13.454  0.60 19.35 ?  26  GLU   A CB   1 
ATOM   712  C CB   B GLU   A 1 26  ? 16.228 -1.993  13.613  0.40 17.48 ?  26  GLU   A CB   1 
ATOM   713  C CG   A GLU   A 1 26  ? 14.432 -1.863  13.345  0.60 21.24 ?  26  GLU   A CG   1 
ATOM   714  C CG   B GLU   A 1 26  ? 14.807 -2.302  13.204  0.40 18.23 ?  26  GLU   A CG   1 
ATOM   715  C CD   A GLU   A 1 26  ? 14.054 -2.696  14.555  0.60 22.57 ?  26  GLU   A CD   1 
ATOM   716  C CD   B GLU   A 1 26  ? 13.990 -2.852  14.355  0.40 18.70 ?  26  GLU   A CD   1 
ATOM   717  O OE1  A GLU   A 1 26  ? 14.525 -3.852  14.673  0.60 23.45 ?  26  GLU   A OE1  1 
ATOM   718  O OE1  B GLU   A 1 26  ? 14.432 -3.838  14.993  0.40 19.35 ?  26  GLU   A OE1  1 
ATOM   719  O OE2  A GLU   A 1 26  ? 13.294 -2.184  15.397  0.60 22.86 -1 26  GLU   A OE2  1 
ATOM   720  O OE2  B GLU   A 1 26  ? 12.914 -2.285  14.631  0.40 18.12 -1 26  GLU   A OE2  1 
ATOM   721  H H    A GLU   A 1 26  ? 15.466 1.087   13.196  0.60 21.14 ?  26  GLU   A H    1 
ATOM   722  H H    B GLU   A 1 26  ? 15.735 0.378   13.289  0.40 20.29 ?  26  GLU   A H    1 
ATOM   723  H HA   A GLU   A 1 26  ? 15.419 -0.460  15.285  0.60 21.28 ?  26  GLU   A HA   1 
ATOM   724  H HA   B GLU   A 1 26  ? 15.772 -1.122  15.411  0.40 19.71 ?  26  GLU   A HA   1 
ATOM   725  H HB2  A GLU   A 1 26  ? 16.050 -0.894  12.601  0.60 23.19 ?  26  GLU   A HB2  1 
ATOM   726  H HB2  B GLU   A 1 26  ? 16.711 -1.719  12.818  0.40 20.95 ?  26  GLU   A HB2  1 
ATOM   727  H HB3  A GLU   A 1 26  ? 16.428 -2.036  13.632  0.60 23.19 ?  26  GLU   A HB3  1 
ATOM   728  H HB3  B GLU   A 1 26  ? 16.616 -2.813  13.963  0.40 20.95 ?  26  GLU   A HB3  1 
ATOM   729  H HG2  A GLU   A 1 26  ? 13.803 -1.126  13.260  0.60 25.47 ?  26  GLU   A HG2  1 
ATOM   730  H HG2  B GLU   A 1 26  ? 14.383 -1.486  12.894  0.40 21.85 ?  26  GLU   A HG2  1 
ATOM   731  H HG3  A GLU   A 1 26  ? 14.381 -2.430  12.559  0.60 25.47 ?  26  GLU   A HG3  1 
ATOM   732  H HG3  B GLU   A 1 26  ? 14.820 -2.959  12.486  0.40 21.85 ?  26  GLU   A HG3  1 
ATOM   733  N N    A ALA   A 1 27  ? 18.388 0.247   14.280  0.60 16.37 ?  27  ALA   A N    1 
ATOM   734  N N    B ALA   A 1 27  ? 18.693 -0.217  14.455  0.40 16.14 ?  27  ALA   A N    1 
ATOM   735  C CA   A ALA   A 1 27  ? 19.791 0.221   14.681  0.60 16.86 ?  27  ALA   A CA   1 
ATOM   736  C CA   B ALA   A 1 27  ? 20.069 -0.108  14.926  0.40 16.71 ?  27  ALA   A CA   1 
ATOM   737  C C    A ALA   A 1 27  ? 20.005 0.967   15.994  0.60 18.28 ?  27  ALA   A C    1 
ATOM   738  C C    B ALA   A 1 27  ? 20.156 0.790   16.154  0.40 18.41 ?  27  ALA   A C    1 
ATOM   739  O O    A ALA   A 1 27  ? 20.672 0.464   16.905  0.60 18.34 ?  27  ALA   A O    1 
ATOM   740  O O    B ALA   A 1 27  ? 20.884 0.482   17.105  0.40 18.49 ?  27  ALA   A O    1 
ATOM   741  C CB   A ALA   A 1 27  ? 20.667 0.803   13.567  0.60 16.54 ?  27  ALA   A CB   1 
ATOM   742  C CB   B ALA   A 1 27  ? 20.975 0.400   13.802  0.40 16.43 ?  27  ALA   A CB   1 
ATOM   743  H H    A ALA   A 1 27  ? 18.234 0.628   13.520  0.60 19.62 ?  27  ALA   A H    1 
ATOM   744  H H    B ALA   A 1 27  ? 18.544 0.137   13.685  0.40 19.35 ?  27  ALA   A H    1 
ATOM   745  H HA   A ALA   A 1 27  ? 20.054 -0.697  14.813  0.60 20.21 ?  27  ALA   A HA   1 
ATOM   746  H HA   B ALA   A 1 27  ? 20.381 -0.989  15.179  0.40 20.02 ?  27  ALA   A HA   1 
ATOM   747  H HB1  A ALA   A 1 27  ? 21.593 0.777   13.849  0.60 19.82 ?  27  ALA   A HB1  1 
ATOM   748  H HB1  B ALA   A 1 27  ? 21.889 0.443   14.127  0.40 19.69 ?  27  ALA   A HB1  1 
ATOM   749  H HB2  A ALA   A 1 27  ? 20.550 0.272   12.762  0.60 19.82 ?  27  ALA   A HB2  1 
ATOM   750  H HB2  B ALA   A 1 27  ? 20.924 -0.217  13.053  0.40 19.69 ?  27  ALA   A HB2  1 
ATOM   751  H HB3  A ALA   A 1 27  ? 20.398 1.721   13.396  0.60 19.82 ?  27  ALA   A HB3  1 
ATOM   752  H HB3  B ALA   A 1 27  ? 20.680 1.279   13.528  0.40 19.69 ?  27  ALA   A HB3  1 
ATOM   753  N N    A LYS   A 1 28  ? 19.426 2.165   16.121  0.60 20.15 ?  28  LYS   A N    1 
ATOM   754  N N    B LYS   A 1 28  ? 19.402 1.892   16.163  0.40 20.24 ?  28  LYS   A N    1 
ATOM   755  C CA   A LYS   A 1 28  ? 19.624 2.950   17.338  0.60 22.80 ?  28  LYS   A CA   1 
ATOM   756  C CA   B LYS   A 1 28  ? 19.395 2.773   17.327  0.40 22.60 ?  28  LYS   A CA   1 
ATOM   757  C C    A LYS   A 1 28  ? 19.075 2.245   18.574  0.60 23.98 ?  28  LYS   A C    1 
ATOM   758  C C    B LYS   A 1 28  ? 18.948 2.027   18.579  0.40 24.01 ?  28  LYS   A C    1 
ATOM   759  O O    A LYS   A 1 28  ? 19.542 2.501   19.689  0.60 25.19 ?  28  LYS   A O    1 
ATOM   760  O O    B LYS   A 1 28  ? 19.573 2.142   19.639  0.40 24.64 ?  28  LYS   A O    1 
ATOM   761  C CB   A LYS   A 1 28  ? 18.999 4.338   17.188  0.60 24.53 ?  28  LYS   A CB   1 
ATOM   762  C CB   B LYS   A 1 28  ? 18.514 3.997   17.061  0.40 23.63 ?  28  LYS   A CB   1 
ATOM   763  C CG   A LYS   A 1 28  ? 19.792 5.260   16.275  0.60 26.39 ?  28  LYS   A CG   1 
ATOM   764  C CG   B LYS   A 1 28  ? 19.247 5.122   16.350  0.40 25.03 ?  28  LYS   A CG   1 
ATOM   765  C CD   A LYS   A 1 28  ? 19.283 6.691   16.322  0.60 28.33 ?  28  LYS   A CD   1 
ATOM   766  C CD   B LYS   A 1 28  ? 18.537 6.462   16.490  0.40 26.81 ?  28  LYS   A CD   1 
ATOM   767  C CE   A LYS   A 1 28  ? 17.959 6.835   15.599  0.60 29.63 ?  28  LYS   A CE   1 
ATOM   768  C CE   B LYS   A 1 28  ? 17.701 6.780   15.266  0.40 28.25 ?  28  LYS   A CE   1 
ATOM   769  N NZ   A LYS   A 1 28  ? 17.495 8.251   15.590  0.60 30.43 ?  28  LYS   A NZ   1 
ATOM   770  N NZ   B LYS   A 1 28  ? 17.611 8.246   15.025  0.40 29.00 ?  28  LYS   A NZ   1 
ATOM   771  H H    A LYS   A 1 28  ? 18.925 2.539   15.529  0.60 24.15 ?  28  LYS   A H    1 
ATOM   772  H H    B LYS   A 1 28  ? 18.891 2.141   15.521  0.40 24.27 ?  28  LYS   A H    1 
ATOM   773  H HA   A LYS   A 1 28  ? 20.573 3.073   17.475  0.60 27.34 ?  28  LYS   A HA   1 
ATOM   774  H HA   B LYS   A 1 28  ? 20.293 3.088   17.488  0.40 27.10 ?  28  LYS   A HA   1 
ATOM   775  H HB2  A LYS   A 1 28  ? 18.108 4.246   16.819  0.60 29.41 ?  28  LYS   A HB2  1 
ATOM   776  H HB2  B LYS   A 1 28  ? 17.765 3.735   16.501  0.40 28.34 ?  28  LYS   A HB2  1 
ATOM   777  H HB3  A LYS   A 1 28  ? 18.951 4.758   18.064  0.60 29.41 ?  28  LYS   A HB3  1 
ATOM   778  H HB3  B LYS   A 1 28  ? 18.189 4.342   17.906  0.40 28.34 ?  28  LYS   A HB3  1 
ATOM   779  H HG2  A LYS   A 1 28  ? 20.721 5.261   16.552  0.60 31.65 ?  28  LYS   A HG2  1 
ATOM   780  H HG2  B LYS   A 1 28  ? 20.130 5.217   16.733  0.40 30.02 ?  28  LYS   A HG2  1 
ATOM   781  H HG3  A LYS   A 1 28  ? 19.715 4.942   15.362  0.60 31.65 ?  28  LYS   A HG3  1 
ATOM   782  H HG3  B LYS   A 1 28  ? 19.318 4.908   15.406  0.40 30.02 ?  28  LYS   A HG3  1 
ATOM   783  H HD2  A LYS   A 1 28  ? 19.153 6.955   17.246  0.60 33.97 ?  28  LYS   A HD2  1 
ATOM   784  H HD2  B LYS   A 1 28  ? 17.948 6.439   17.263  0.40 32.15 ?  28  LYS   A HD2  1 
ATOM   785  H HD3  A LYS   A 1 28  ? 19.928 7.274   15.894  0.60 33.97 ?  28  LYS   A HD3  1 
ATOM   786  H HD3  B LYS   A 1 28  ? 19.198 7.165   16.598  0.40 32.15 ?  28  LYS   A HD3  1 
ATOM   787  H HE2  A LYS   A 1 28  ? 18.063 6.544   14.679  0.60 35.53 ?  28  LYS   A HE2  1 
ATOM   788  H HE2  B LYS   A 1 28  ? 18.107 6.374   14.487  0.40 33.87 ?  28  LYS   A HE2  1 
ATOM   789  H HE3  A LYS   A 1 28  ? 17.287 6.298   16.047  0.60 35.53 ?  28  LYS   A HE3  1 
ATOM   790  H HE3  B LYS   A 1 28  ? 16.804 6.435   15.394  0.40 33.87 ?  28  LYS   A HE3  1 
ATOM   791  H HZ1  A LYS   A 1 28  ? 16.719 8.314   15.161  0.60 36.49 ?  28  LYS   A HZ1  1 
ATOM   792  H HZ1  B LYS   A 1 28  ? 17.119 8.407   14.302  0.40 34.78 ?  28  LYS   A HZ1  1 
ATOM   793  H HZ2  A LYS   A 1 28  ? 17.390 8.541   16.425  0.60 36.49 ?  28  LYS   A HZ2  1 
ATOM   794  H HZ2  B LYS   A 1 28  ? 17.238 8.648   15.726  0.40 34.78 ?  28  LYS   A HZ2  1 
ATOM   795  H HZ3  A LYS   A 1 28  ? 18.096 8.765   15.179  0.60 36.49 ?  28  LYS   A HZ3  1 
ATOM   796  H HZ3  B LYS   A 1 28  ? 18.427 8.584   14.900  0.40 34.78 ?  28  LYS   A HZ3  1 
ATOM   797  N N    A LYS   A 1 29  ? 18.090 1.361   18.403  0.60 24.40 ?  29  LYS   A N    1 
ATOM   798  N N    B LYS   A 1 29  ? 17.879 1.235   18.471  0.40 25.14 ?  29  LYS   A N    1 
ATOM   799  C CA   A LYS   A 1 29  ? 17.499 0.662   19.542  0.60 25.95 ?  29  LYS   A CA   1 
ATOM   800  C CA   B LYS   A 1 29  ? 17.350 0.558   19.651  0.40 26.52 ?  29  LYS   A CA   1 
ATOM   801  C C    A LYS   A 1 29  ? 18.326 -0.557  19.940  0.60 25.60 ?  29  LYS   A C    1 
ATOM   802  C C    B LYS   A 1 29  ? 18.146 -0.698  19.988  0.40 25.71 ?  29  LYS   A C    1 
ATOM   803  O O    A LYS   A 1 29  ? 18.704 -0.710  21.108  0.60 26.17 ?  29  LYS   A O    1 
ATOM   804  O O    B LYS   A 1 29  ? 18.345 -1.006  21.169  0.40 25.73 ?  29  LYS   A O    1 
ATOM   805  C CB   A LYS   A 1 29  ? 16.066 0.244   19.194  0.60 28.06 ?  29  LYS   A CB   1 
ATOM   806  C CB   B LYS   A 1 29  ? 15.868 0.224   19.454  0.40 28.82 ?  29  LYS   A CB   1 
ATOM   807  C CG   A LYS   A 1 29  ? 15.302 -0.422  20.329  0.60 30.46 ?  29  LYS   A CG   1 
ATOM   808  C CG   B LYS   A 1 29  ? 15.199 -0.466  20.646  0.40 30.88 ?  29  LYS   A CG   1 
ATOM   809  C CD   A LYS   A 1 29  ? 14.861 0.590   21.370  0.60 32.77 ?  29  LYS   A CD   1 
ATOM   810  C CD   B LYS   A 1 29  ? 15.010 0.476   21.828  0.40 32.61 ?  29  LYS   A CD   1 
ATOM   811  C CE   A LYS   A 1 29  ? 13.990 -0.054  22.437  0.60 34.32 ?  29  LYS   A CE   1 
ATOM   812  C CE   B LYS   A 1 29  ? 14.202 -0.187  22.937  0.40 33.83 ?  29  LYS   A CE   1 
ATOM   813  N NZ   A LYS   A 1 29  ? 13.481 0.947   23.413  0.60 35.26 ?  29  LYS   A NZ   1 
ATOM   814  N NZ   B LYS   A 1 29  ? 13.952 0.728   24.087  0.40 34.56 ?  29  LYS   A NZ   1 
ATOM   815  H H    A LYS   A 1 29  ? 17.744 1.153   17.645  0.60 29.26 ?  29  LYS   A H    1 
ATOM   816  H H    B LYS   A 1 29  ? 17.454 1.067   17.741  0.40 30.14 ?  29  LYS   A H    1 
ATOM   817  H HA   A LYS   A 1 29  ? 17.460 1.260   20.303  0.60 31.12 ?  29  LYS   A HA   1 
ATOM   818  H HA   B LYS   A 1 29  ? 17.415 1.155   20.410  0.40 31.79 ?  29  LYS   A HA   1 
ATOM   819  H HB2  A LYS   A 1 29  ? 15.568 1.037   18.935  0.60 33.65 ?  29  LYS   A HB2  1 
ATOM   820  H HB2  B LYS   A 1 29  ? 15.387 1.051   19.291  0.40 34.56 ?  29  LYS   A HB2  1 
ATOM   821  H HB3  A LYS   A 1 29  ? 16.094 -0.380  18.454  0.60 33.65 ?  29  LYS   A HB3  1 
ATOM   822  H HB3  B LYS   A 1 29  ? 15.779 -0.362  18.690  0.40 34.56 ?  29  LYS   A HB3  1 
ATOM   823  H HG2  A LYS   A 1 29  ? 14.509 -0.851  19.970  0.60 36.53 ?  29  LYS   A HG2  1 
ATOM   824  H HG2  B LYS   A 1 29  ? 14.323 -0.784  20.376  0.40 37.04 ?  29  LYS   A HG2  1 
ATOM   825  H HG3  A LYS   A 1 29  ? 15.867 -1.080  20.764  0.60 36.53 ?  29  LYS   A HG3  1 
ATOM   826  H HG3  B LYS   A 1 29  ? 15.744 -1.213  20.941  0.40 37.04 ?  29  LYS   A HG3  1 
ATOM   827  H HD2  A LYS   A 1 29  ? 15.643 0.968   21.802  0.60 39.31 ?  29  LYS   A HD2  1 
ATOM   828  H HD2  B LYS   A 1 29  ? 15.877 0.721   22.188  0.40 39.11 ?  29  LYS   A HD2  1 
ATOM   829  H HD3  A LYS   A 1 29  ? 14.346 1.290   20.939  0.60 39.31 ?  29  LYS   A HD3  1 
ATOM   830  H HD3  B LYS   A 1 29  ? 14.531 1.268   21.535  0.40 39.11 ?  29  LYS   A HD3  1 
ATOM   831  H HE2  A LYS   A 1 29  ? 13.228 -0.480  22.013  0.60 41.16 ?  29  LYS   A HE2  1 
ATOM   832  H HE2  B LYS   A 1 29  ? 13.342 -0.466  22.582  0.40 40.57 ?  29  LYS   A HE2  1 
ATOM   833  H HE3  A LYS   A 1 29  ? 14.513 -0.712  22.922  0.60 41.16 ?  29  LYS   A HE3  1 
ATOM   834  H HE3  B LYS   A 1 29  ? 14.689 -0.958  23.268  0.40 40.57 ?  29  LYS   A HE3  1 
ATOM   835  H HZ1  A LYS   A 1 29  ? 12.975 0.545   24.025  0.60 42.29 ?  29  LYS   A HZ1  1 
ATOM   836  H HZ1  B LYS   A 1 29  ? 13.478 0.308   24.713  0.40 41.45 ?  29  LYS   A HZ1  1 
ATOM   837  H HZ2  A LYS   A 1 29  ? 14.163 1.349   23.819  0.60 42.29 ?  29  LYS   A HZ2  1 
ATOM   838  H HZ2  B LYS   A 1 29  ? 14.725 0.994   24.438  0.40 41.45 ?  29  LYS   A HZ2  1 
ATOM   839  H HZ3  A LYS   A 1 29  ? 12.993 1.561   22.992  0.60 42.29 ?  29  LYS   A HZ3  1 
ATOM   840  H HZ3  B LYS   A 1 29  ? 13.497 1.443   23.813  0.40 41.45 ?  29  LYS   A HZ3  1 
ATOM   841  N N    . VAL   A 1 30  ? 18.607 -1.435  18.979  1.00 24.84 ?  30  VAL   A N    1 
ATOM   842  C CA   . VAL   A 1 30  ? 19.296 -2.692  19.254  1.00 24.39 ?  30  VAL   A CA   1 
ATOM   843  C C    . VAL   A 1 30  ? 20.803 -2.515  19.438  1.00 23.52 ?  30  VAL   A C    1 
ATOM   844  O O    . VAL   A 1 30  ? 21.419 -3.242  20.224  1.00 24.00 ?  30  VAL   A O    1 
ATOM   845  C CB   . VAL   A 1 30  ? 18.982 -3.697  18.131  1.00 25.32 ?  30  VAL   A CB   1 
ATOM   846  C CG1  . VAL   A 1 30  ? 19.763 -4.984  18.320  1.00 25.80 ?  30  VAL   A CG1  1 
ATOM   847  C CG2  . VAL   A 1 30  ? 17.487 -3.983  18.076  1.00 26.04 ?  30  VAL   A CG2  1 
ATOM   848  H H    A VAL   A 1 30  ? 18.400 -1.328  18.151  0.60 29.79 ?  30  VAL   A H    1 
ATOM   849  H H    B VAL   A 1 30  ? 18.524 -1.242  18.146  0.40 29.79 ?  30  VAL   A H    1 
ATOM   850  H HA   . VAL   A 1 30  ? 18.940 -3.063  20.075  1.00 29.25 ?  30  VAL   A HA   1 
ATOM   851  H HB   . VAL   A 1 30  ? 19.242 -3.315  17.281  1.00 30.36 ?  30  VAL   A HB   1 
ATOM   852  H HG11 . VAL   A 1 30  ? 19.377 -5.671  17.752  1.00 30.94 ?  30  VAL   A HG11 1 
ATOM   853  H HG12 . VAL   A 1 30  ? 20.686 -4.834  18.075  1.00 30.94 ?  30  VAL   A HG12 1 
ATOM   854  H HG13 . VAL   A 1 30  ? 19.701 -5.256  19.249  1.00 30.94 ?  30  VAL   A HG13 1 
ATOM   855  H HG21 . VAL   A 1 30  ? 17.319 -4.658  17.399  1.00 31.22 ?  30  VAL   A HG21 1 
ATOM   856  H HG22 . VAL   A 1 30  ? 17.195 -4.306  18.943  1.00 31.22 ?  30  VAL   A HG22 1 
ATOM   857  H HG23 . VAL   A 1 30  ? 17.017 -3.166  17.852  1.00 31.22 ?  30  VAL   A HG23 1 
ATOM   858  N N    . LYS   A 1 31  ? 21.411 -1.560  18.741  1.00 21.77 ?  31  LYS   A N    1 
ATOM   859  C CA   . LYS   A 1 31  ? 22.862 -1.441  18.650  1.00 22.36 ?  31  LYS   A CA   1 
ATOM   860  C C    . LYS   A 1 31  ? 23.475 -2.797  18.290  1.00 20.46 ?  31  LYS   A C    1 
ATOM   861  O O    . LYS   A 1 31  ? 24.267 -3.355  19.058  1.00 20.93 ?  31  LYS   A O    1 
ATOM   862  C CB   . LYS   A 1 31  ? 23.476 -0.880  19.925  1.00 27.02 ?  31  LYS   A CB   1 
ATOM   863  C CG   . LYS   A 1 31  ? 22.772 0.367   20.445  1.00 32.44 ?  31  LYS   A CG   1 
ATOM   864  C CD   . LYS   A 1 31  ? 23.750 1.496   20.737  1.00 36.80 ?  31  LYS   A CD   1 
ATOM   865  C CE   . LYS   A 1 31  ? 23.149 2.523   21.691  1.00 39.80 ?  31  LYS   A CE   1 
ATOM   866  N NZ   . LYS   A 1 31  ? 21.903 3.153   21.173  1.00 41.39 ?  31  LYS   A NZ   1 
ATOM   867  H H    . LYS   A 1 31  ? 20.994 -0.953  18.302  1.00 26.10 ?  31  LYS   A H    1 
ATOM   868  H HA   . LYS   A 1 31  ? 23.075 -0.827  17.937  1.00 26.80 ?  31  LYS   A HA   1 
ATOM   869  H HB2  . LYS   A 1 31  ? 23.424 -1.560  20.604  1.00 32.40 ?  31  LYS   A HB2  1 
ATOM   870  H HB3  . LYS   A 1 31  ? 24.408 -0.655  19.751  1.00 32.40 ?  31  LYS   A HB3  1 
ATOM   871  H HG2  . LYS   A 1 31  ? 22.141 0.680   19.778  1.00 38.91 ?  31  LYS   A HG2  1 
ATOM   872  H HG3  . LYS   A 1 31  ? 22.308 0.148   21.268  1.00 38.91 ?  31  LYS   A HG3  1 
ATOM   873  H HD2  . LYS   A 1 31  ? 24.550 1.132   21.147  1.00 44.14 ?  31  LYS   A HD2  1 
ATOM   874  H HD3  . LYS   A 1 31  ? 23.975 1.948   19.907  1.00 44.14 ?  31  LYS   A HD3  1 
ATOM   875  H HE2  . LYS   A 1 31  ? 22.930 2.082   22.526  1.00 47.73 ?  31  LYS   A HE2  1 
ATOM   876  H HE3  . LYS   A 1 31  ? 23.798 3.227   21.849  1.00 47.73 ?  31  LYS   A HE3  1 
ATOM   877  H HZ1  . LYS   A 1 31  ? 21.592 3.743   21.764  1.00 49.65 ?  31  LYS   A HZ1  1 
ATOM   878  H HZ2  . LYS   A 1 31  ? 22.069 3.572   20.407  1.00 49.65 ?  31  LYS   A HZ2  1 
ATOM   879  H HZ3  . LYS   A 1 31  ? 21.282 2.530   21.035  1.00 49.65 ?  31  LYS   A HZ3  1 
ATOM   880  N N    . PRO   A 1 32  ? 23.120 -3.349  17.137  1.00 17.99 ?  32  PRO   A N    1 
ATOM   881  C CA   . PRO   A 1 32  ? 23.597 -4.682  16.772  1.00 17.93 ?  32  PRO   A CA   1 
ATOM   882  C C    . PRO   A 1 32  ? 25.095 -4.687  16.545  1.00 17.83 ?  32  PRO   A C    1 
ATOM   883  O O    . PRO   A 1 32  ? 25.727 -3.653  16.324  1.00 17.52 ?  32  PRO   A O    1 
ATOM   884  C CB   . PRO   A 1 32  ? 22.850 -4.966  15.466  1.00 17.89 ?  32  PRO   A CB   1 
ATOM   885  C CG   . PRO   A 1 32  ? 22.660 -3.602  14.868  1.00 17.24 ?  32  PRO   A CG   1 
ATOM   886  C CD   . PRO   A 1 32  ? 22.388 -2.705  16.037  1.00 17.46 ?  32  PRO   A CD   1 
ATOM   887  H HA   . PRO   A 1 32  ? 23.361 -5.343  17.440  1.00 21.49 ?  32  PRO   A HA   1 
ATOM   888  H HB2  . PRO   A 1 32  ? 23.388 -5.530  14.885  1.00 21.44 ?  32  PRO   A HB2  1 
ATOM   889  H HB3  . PRO   A 1 32  ? 21.993 -5.384  15.656  1.00 21.44 ?  32  PRO   A HB3  1 
ATOM   890  H HG2  . PRO   A 1 32  ? 23.469 -3.338  14.402  1.00 20.66 ?  32  PRO   A HG2  1 
ATOM   891  H HG3  . PRO   A 1 32  ? 21.903 -3.618  14.258  1.00 20.66 ?  32  PRO   A HG3  1 
ATOM   892  H HD2  . PRO   A 1 32  ? 22.747 -1.820  15.861  1.00 20.93 ?  32  PRO   A HD2  1 
ATOM   893  H HD3  . PRO   A 1 32  ? 21.442 -2.681  16.225  1.00 20.93 ?  32  PRO   A HD3  1 
ATOM   894  N N    . THR   A 1 33  ? 25.662 -5.892  16.585  1.00 17.80 ?  33  THR   A N    1 
ATOM   895  C CA   . THR   A 1 33  ? 27.069 -6.043  16.249  1.00 17.93 ?  33  THR   A CA   1 
ATOM   896  C C    . THR   A 1 33  ? 27.338 -5.582  14.823  1.00 16.27 ?  33  THR   A C    1 
ATOM   897  O O    . THR   A 1 33  ? 28.362 -4.940  14.557  1.00 16.20 ?  33  THR   A O    1 
ATOM   898  C CB   . THR   A 1 33  ? 27.489 -7.499  16.450  1.00 19.34 ?  33  THR   A CB   1 
ATOM   899  O OG1  . THR   A 1 33  ? 27.216 -7.880  17.801  1.00 20.65 ?  33  THR   A OG1  1 
ATOM   900  C CG2  . THR   A 1 33  ? 28.976 -7.684  16.171  1.00 20.21 ?  33  THR   A CG2  1 
ATOM   901  H H    . THR   A 1 33  ? 25.262 -6.623  16.791  1.00 21.34 ?  33  THR   A H    1 
ATOM   902  H HA   . THR   A 1 33  ? 27.602 -5.495  16.843  1.00 21.49 ?  33  THR   A HA   1 
ATOM   903  H HB   . THR   A 1 33  ? 26.992 -8.073  15.846  1.00 23.18 ?  33  THR   A HB   1 
ATOM   904  H HG1  . THR   A 1 33  ? 27.649 -7.390  18.333  1.00 24.76 ?  33  THR   A HG1  1 
ATOM   905  H HG21 . THR   A 1 33  ? 29.259 -8.569  16.451  1.00 24.22 ?  33  THR   A HG21 1 
ATOM   906  H HG22 . THR   A 1 33  ? 29.152 -7.584  15.223  1.00 24.22 ?  33  THR   A HG22 1 
ATOM   907  H HG23 . THR   A 1 33  ? 29.488 -7.021  16.660  1.00 24.22 ?  33  THR   A HG23 1 
ATOM   908  N N    . VAL   A 1 34  ? 26.427 -5.886  13.898  1.00 14.57 ?  34  VAL   A N    1 
ATOM   909  C CA   . VAL   A 1 34  ? 26.592 -5.539  12.490  1.00 13.32 ?  34  VAL   A CA   1 
ATOM   910  C C    . VAL   A 1 34  ? 25.284 -4.980  11.943  1.00 12.83 ?  34  VAL   A C    1 
ATOM   911  O O    . VAL   A 1 34  ? 24.248 -5.653  11.993  1.00 13.35 ?  34  VAL   A O    1 
ATOM   912  C CB   . VAL   A 1 34  ? 27.041 -6.734  11.628  1.00 13.91 ?  34  VAL   A CB   1 
ATOM   913  C CG1  . VAL   A 1 34  ? 27.217 -6.298  10.185  1.00 13.95 ?  34  VAL   A CG1  1 
ATOM   914  C CG2  . VAL   A 1 34  ? 28.334 -7.350  12.167  1.00 15.47 ?  34  VAL   A CG2  1 
ATOM   915  H H    . VAL   A 1 34  ? 25.694 -6.303  14.065  1.00 17.46 ?  34  VAL   A H    1 
ATOM   916  H HA   . VAL   A 1 34  ? 27.263 -4.843  12.408  1.00 15.96 ?  34  VAL   A HA   1 
ATOM   917  H HB   . VAL   A 1 34  ? 26.349 -7.414  11.649  1.00 16.67 ?  34  VAL   A HB   1 
ATOM   918  H HG11 . VAL   A 1 34  ? 27.715 -6.980  9.708   1.00 16.72 ?  34  VAL   A HG11 1 
ATOM   919  H HG12 . VAL   A 1 34  ? 26.349 -6.175  9.774   1.00 16.72 ?  34  VAL   A HG12 1 
ATOM   920  H HG13 . VAL   A 1 34  ? 27.714 -5.460  10.166  1.00 16.72 ?  34  VAL   A HG13 1 
ATOM   921  H HG21 . VAL   A 1 34  ? 28.604 -8.076  11.583  1.00 18.54 ?  34  VAL   A HG21 1 
ATOM   922  H HG22 . VAL   A 1 34  ? 29.023 -6.668  12.189  1.00 18.54 ?  34  VAL   A HG22 1 
ATOM   923  H HG23 . VAL   A 1 34  ? 28.172 -7.688  13.062  1.00 18.54 ?  34  VAL   A HG23 1 
ATOM   924  N N    . VAL   A 1 35  ? 25.335 -3.764  11.396  1.00 12.02 ?  35  VAL   A N    1 
ATOM   925  C CA   . VAL   A 1 35  ? 24.288 -3.240  10.528  1.00 11.72 ?  35  VAL   A CA   1 
ATOM   926  C C    . VAL   A 1 35  ? 24.831 -3.232  9.107   1.00 10.86 ?  35  VAL   A C    1 
ATOM   927  O O    . VAL   A 1 35  ? 25.975 -2.825  8.875   1.00 11.57 ?  35  VAL   A O    1 
ATOM   928  C CB   . VAL   A 1 35  ? 23.763 -1.851  10.957  1.00 12.33 ?  35  VAL   A CB   1 
ATOM   929  C CG1  . VAL   A 1 35  ? 24.833 -0.759  10.822  1.00 13.21 ?  35  VAL   A CG1  1 
ATOM   930  C CG2  . VAL   A 1 35  ? 22.510 -1.481  10.152  1.00 12.87 ?  35  VAL   A CG2  1 
ATOM   931  H H    . VAL   A 1 35  ? 25.980 -3.211  11.515  1.00 14.40 ?  35  VAL   A H    1 
ATOM   932  H HA   . VAL   A 1 35  ? 23.529 -3.850  10.550  1.00 14.04 ?  35  VAL   A HA   1 
ATOM   933  H HB   . VAL   A 1 35  ? 23.502 -1.889  11.886  1.00 14.78 ?  35  VAL   A HB   1 
ATOM   934  H HG11 . VAL   A 1 35  ? 24.494 0.071   11.202  1.00 15.82 ?  35  VAL   A HG11 1 
ATOM   935  H HG12 . VAL   A 1 35  ? 25.631 -1.034  11.302  1.00 15.82 ?  35  VAL   A HG12 1 
ATOM   936  H HG13 . VAL   A 1 35  ? 25.044 -0.623  9.884   1.00 15.82 ?  35  VAL   A HG13 1 
ATOM   937  H HG21 . VAL   A 1 35  ? 22.168 -0.629  10.463  1.00 15.42 ?  35  VAL   A HG21 1 
ATOM   938  H HG22 . VAL   A 1 35  ? 22.743 -1.416  9.208   1.00 15.42 ?  35  VAL   A HG22 1 
ATOM   939  H HG23 . VAL   A 1 35  ? 21.839 -2.171  10.274  1.00 15.42 ?  35  VAL   A HG23 1 
ATOM   940  N N    . VAL   A 1 36  ? 24.015 -3.689  8.163   1.00 10.49 ?  36  VAL   A N    1 
ATOM   941  C CA   . VAL   A 1 36  ? 24.384 -3.693  6.756   1.00 10.27 ?  36  VAL   A CA   1 
ATOM   942  C C    . VAL   A 1 36  ? 23.918 -2.402  6.102   1.00 10.80 ?  36  VAL   A C    1 
ATOM   943  O O    . VAL   A 1 36  ? 22.762 -1.990  6.264   1.00 11.50 ?  36  VAL   A O    1 
ATOM   944  C CB   . VAL   A 1 36  ? 23.770 -4.903  6.038   1.00 10.25 ?  36  VAL   A CB   1 
ATOM   945  C CG1  . VAL   A 1 36  ? 24.008 -4.813  4.549   1.00 10.85 ?  36  VAL   A CG1  1 
ATOM   946  C CG2  . VAL   A 1 36  ? 24.326 -6.200  6.594   1.00 11.12 ?  36  VAL   A CG2  1 
ATOM   947  H H    . VAL   A 1 36  ? 23.221 -3.998  8.315   1.00 12.56 ?  36  VAL   A H    1 
ATOM   948  H HA   . VAL   A 1 36  ? 25.352 -3.753  6.680   1.00 12.31 ?  36  VAL   A HA   1 
ATOM   949  H HB   . VAL   A 1 36  ? 22.812 -4.901  6.188   1.00 12.28 ?  36  VAL   A HB   1 
ATOM   950  H HG11 . VAL   A 1 36  ? 23.878 -5.692  4.156   1.00 12.99 ?  36  VAL   A HG11 1 
ATOM   951  H HG12 . VAL   A 1 36  ? 23.377 -4.186  4.160   1.00 12.99 ?  36  VAL   A HG12 1 
ATOM   952  H HG13 . VAL   A 1 36  ? 24.916 -4.515  4.390   1.00 12.99 ?  36  VAL   A HG13 1 
ATOM   953  H HG21 . VAL   A 1 36  ? 23.924 -6.949  6.122   1.00 13.33 ?  36  VAL   A HG21 1 
ATOM   954  H HG22 . VAL   A 1 36  ? 25.290 -6.215  6.468   1.00 13.33 ?  36  VAL   A HG22 1 
ATOM   955  H HG23 . VAL   A 1 36  ? 24.118 -6.261  7.540   1.00 13.33 ?  36  VAL   A HG23 1 
ATOM   956  N N    A ASN   A 1 37  ? 24.822 -1.766  5.366   0.60 10.52 ?  37  ASN   A N    1 
ATOM   957  N N    B ASN   A 1 37  ? 24.808 -1.775  5.337   0.40 10.13 ?  37  ASN   A N    1 
ATOM   958  C CA   A ASN   A 1 37  ? 24.490 -0.619  4.539   0.60 10.19 ?  37  ASN   A CA   1 
ATOM   959  C CA   B ASN   A 1 37  ? 24.441 -0.676  4.456   0.40 9.45  ?  37  ASN   A CA   1 
ATOM   960  C C    A ASN   A 1 37  ? 24.319 -1.056  3.092   0.60 10.01 ?  37  ASN   A C    1 
ATOM   961  C C    B ASN   A 1 37  ? 24.349 -1.172  3.019   0.40 9.67  ?  37  ASN   A C    1 
ATOM   962  O O    A ASN   A 1 37  ? 25.056 -1.915  2.597   0.60 10.61 ?  37  ASN   A O    1 
ATOM   963  O O    B ASN   A 1 37  ? 25.190 -1.952  2.562   0.40 9.92  ?  37  ASN   A O    1 
ATOM   964  C CB   A ASN   A 1 37  ? 25.591 0.439   4.617   0.60 10.31 ?  37  ASN   A CB   1 
ATOM   965  C CB   B ASN   A 1 37  ? 25.468 0.455   4.529   0.40 9.60  ?  37  ASN   A CB   1 
ATOM   966  C CG   A ASN   A 1 37  ? 25.237 1.690   3.852   0.60 10.12 ?  37  ASN   A CG   1 
ATOM   967  C CG   B ASN   A 1 37  ? 25.159 1.585   3.555   0.40 9.93  ?  37  ASN   A CG   1 
ATOM   968  O OD1  A ASN   A 1 37  ? 24.059 2.035   3.723   0.60 9.66  ?  37  ASN   A OD1  1 
ATOM   969  O OD1  B ASN   A 1 37  ? 23.995 1.892   3.284   0.40 10.12 ?  37  ASN   A OD1  1 
ATOM   970  N ND2  A ASN   A 1 37  ? 26.250 2.373   3.329   0.60 9.79  ?  37  ASN   A ND2  1 
ATOM   971  N ND2  B ASN   A 1 37  ? 26.204 2.195   3.015   0.40 10.09 ?  37  ASN   A ND2  1 
ATOM   972  H H    A ASN   A 1 37  ? 25.654 -1.989  5.329   0.60 12.60 ?  37  ASN   A H    1 
ATOM   973  H H    B ASN   A 1 37  ? 25.647 -1.974  5.316   0.40 12.14 ?  37  ASN   A H    1 
ATOM   974  H HA   A ASN   A 1 37  ? 23.661 -0.226  4.846   0.60 12.20 ?  37  ASN   A HA   1 
ATOM   975  H HA   B ASN   A 1 37  ? 23.579 -0.325  4.722   0.40 11.31 ?  37  ASN   A HA   1 
ATOM   976  H HB2  A ASN   A 1 37  ? 25.723 0.687   5.548   0.60 12.35 ?  37  ASN   A HB2  1 
ATOM   977  H HB2  B ASN   A 1 37  ? 25.474 0.821   5.432   0.40 11.50 ?  37  ASN   A HB2  1 
ATOM   978  H HB3  A ASN   A 1 37  ? 26.415 0.074   4.253   0.60 12.35 ?  37  ASN   A HB3  1 
ATOM   979  H HB3  B ASN   A 1 37  ? 26.347 0.102   4.314   0.40 11.50 ?  37  ASN   A HB3  1 
ATOM   980  H HD21 A ASN   A 1 37  ? 26.101 3.090   2.879   0.60 11.72 ?  37  ASN   A HD21 1 
ATOM   981  H HD21 B ASN   A 1 37  ? 26.082 2.835   2.459   0.40 12.08 ?  37  ASN   A HD21 1 
ATOM   982  H HD22 A ASN   A 1 37  ? 27.057 2.104   3.433   0.60 11.72 ?  37  ASN   A HD22 1 
ATOM   983  H HD22 B ASN   A 1 37  ? 26.999 1.948   3.219   0.40 12.08 ?  37  ASN   A HD22 1 
ATOM   984  N N    A ALA   A 1 38  ? 23.330 -0.463  2.426   0.60 10.22 ?  38  ALA   A N    1 
ATOM   985  N N    B ALA   A 1 38  ? 23.312 -0.718  2.317   0.40 10.18 ?  38  ALA   A N    1 
ATOM   986  C CA   A ALA   A 1 38  ? 23.117 -0.618  0.988   0.60 9.87  ?  38  ALA   A CA   1 
ATOM   987  C CA   B ALA   A 1 38  ? 23.145 -0.964  0.885   0.40 11.15 ?  38  ALA   A CA   1 
ATOM   988  C C    A ALA   A 1 38  ? 24.041 0.363   0.266   0.60 9.97  ?  38  ALA   A C    1 
ATOM   989  C C    B ALA   A 1 38  ? 23.929 0.108   0.141   0.40 11.14 ?  38  ALA   A C    1 
ATOM   990  O O    A ALA   A 1 38  ? 23.648 1.454   -0.154  0.60 10.18 ?  38  ALA   A O    1 
ATOM   991  O O    B ALA   A 1 38  ? 23.406 1.168   -0.210  0.40 11.62 ?  38  ALA   A O    1 
ATOM   992  C CB   A ALA   A 1 38  ? 21.649 -0.372  0.651   0.60 10.71 ?  38  ALA   A CB   1 
ATOM   993  C CB   B ALA   A 1 38  ? 21.671 -0.928  0.514   0.40 12.08 ?  38  ALA   A CB   1 
ATOM   994  H H    A ALA   A 1 38  ? 22.755 0.048   2.802   0.60 12.24 ?  38  ALA   A H    1 
ATOM   995  H H    B ALA   A 1 38  ? 22.678 -0.255  2.664   0.40 12.19 ?  38  ALA   A H    1 
ATOM   996  H HA   A ALA   A 1 38  ? 23.350 -1.518  0.717   0.60 11.82 ?  38  ALA   A HA   1 
ATOM   997  H HA   B ALA   A 1 38  ? 23.509 -1.839  0.658   0.40 13.35 ?  38  ALA   A HA   1 
ATOM   998  H HB1  A ALA   A 1 38  ? 21.516 -0.491  -0.300  0.60 12.83 ?  38  ALA   A HB1  1 
ATOM   999  H HB1  B ALA   A 1 38  ? 21.587 -1.092  -0.435  0.40 14.47 ?  38  ALA   A HB1  1 
ATOM   1000 H HB2  A ALA   A 1 38  ? 21.101 -1.009  1.144   0.60 12.83 ?  38  ALA   A HB2  1 
ATOM   1001 H HB2  B ALA   A 1 38  ? 21.202 -1.611  1.017   0.40 14.47 ?  38  ALA   A HB2  1 
ATOM   1002 H HB3  A ALA   A 1 38  ? 21.411 0.532   0.911   0.60 12.83 ?  38  ALA   A HB3  1 
ATOM   1003 H HB3  B ALA   A 1 38  ? 21.319 -0.051  0.736   0.40 14.47 ?  38  ALA   A HB3  1 
ATOM   1004 N N    A ALA   A 1 39  ? 25.303 -0.034  0.143   0.60 10.19 ?  39  ALA   A N    1 
ATOM   1005 N N    B ALA   A 1 39  ? 25.199 -0.175  -0.108  0.40 11.22 ?  39  ALA   A N    1 
ATOM   1006 C CA   A ALA   A 1 39  ? 26.372 0.828   -0.334  0.60 10.32 ?  39  ALA   A CA   1 
ATOM   1007 C CA   B ALA   A 1 39  ? 26.141 0.819   -0.589  0.40 10.93 ?  39  ALA   A CA   1 
ATOM   1008 C C    A ALA   A 1 39  ? 26.496 0.783   -1.854  0.60 9.89  ?  39  ALA   A C    1 
ATOM   1009 C C    B ALA   A 1 39  ? 26.291 0.752   -2.106  0.40 10.53 ?  39  ALA   A C    1 
ATOM   1010 O O    A ALA   A 1 39  ? 26.009 -0.133  -2.518  0.60 10.26 ?  39  ALA   A O    1 
ATOM   1011 O O    B ALA   A 1 39  ? 25.816 -0.169  -2.774  0.40 11.17 ?  39  ALA   A O    1 
ATOM   1012 C CB   A ALA   A 1 39  ? 27.693 0.382   0.296   0.60 10.57 ?  39  ALA   A CB   1 
ATOM   1013 C CB   B ALA   A 1 39  ? 27.497 0.605   0.087   0.40 11.29 ?  39  ALA   A CB   1 
ATOM   1014 H H    A ALA   A 1 39  ? 25.574 -0.828  0.339   0.60 12.21 ?  39  ALA   A H    1 
ATOM   1015 H H    B ALA   A 1 39  ? 25.540 -0.958  0.003   0.40 13.44 ?  39  ALA   A H    1 
ATOM   1016 H HA   A ALA   A 1 39  ? 26.200 1.744   -0.071  0.60 12.37 ?  39  ALA   A HA   1 
ATOM   1017 H HA   B ALA   A 1 39  ? 25.816 1.701   -0.343  0.40 13.10 ?  39  ALA   A HA   1 
ATOM   1018 H HB1  A ALA   A 1 39  ? 28.406 0.959   -0.022  0.60 12.66 ?  39  ALA   A HB1  1 
ATOM   1019 H HB1  B ALA   A 1 39  ? 28.117 1.272   -0.240  0.40 13.53 ?  39  ALA   A HB1  1 
ATOM   1020 H HB2  A ALA   A 1 39  ? 27.617 0.457   1.262   0.60 12.66 ?  39  ALA   A HB2  1 
ATOM   1021 H HB2  B ALA   A 1 39  ? 27.390 0.693   1.049   0.40 13.53 ?  39  ALA   A HB2  1 
ATOM   1022 H HB3  A ALA   A 1 39  ? 27.869 -0.535  0.047   0.60 12.66 ?  39  ALA   A HB3  1 
ATOM   1023 H HB3  B ALA   A 1 39  ? 27.818 -0.284  -0.128  0.40 13.53 ?  39  ALA   A HB3  1 
ATOM   1024 N N    A ASN   A 1 40  ? 27.188 1.787   -2.398  0.60 10.09 ?  40  ASN   A N    1 
ATOM   1025 N N    B ASN   A 1 40  ? 26.951 1.769   -2.649  0.40 10.58 ?  40  ASN   A N    1 
ATOM   1026 C CA   A ASN   A 1 40  ? 27.709 1.740   -3.758  0.60 10.49 ?  40  ASN   A CA   1 
ATOM   1027 C CA   B ASN   A 1 40  ? 27.482 1.728   -4.001  0.40 10.86 ?  40  ASN   A CA   1 
ATOM   1028 C C    A ASN   A 1 40  ? 29.231 1.615   -3.716  0.60 10.31 ?  40  ASN   A C    1 
ATOM   1029 C C    B ASN   A 1 40  ? 29.006 1.632   -3.924  0.40 10.47 ?  40  ASN   A C    1 
ATOM   1030 O O    A ASN   A 1 40  ? 29.850 1.737   -2.656  0.60 10.75 ?  40  ASN   A O    1 
ATOM   1031 O O    B ASN   A 1 40  ? 29.597 1.698   -2.844  0.40 10.16 ?  40  ASN   A O    1 
ATOM   1032 C CB   A ASN   A 1 40  ? 27.238 2.936   -4.603  0.60 11.36 ?  40  ASN   A CB   1 
ATOM   1033 C CB   B ASN   A 1 40  ? 27.015 2.943   -4.818  0.40 11.28 ?  40  ASN   A CB   1 
ATOM   1034 C CG   A ASN   A 1 40  ? 27.653 4.280   -4.028  0.60 12.48 ?  40  ASN   A CG   1 
ATOM   1035 C CG   B ASN   A 1 40  ? 27.335 4.264   -4.144  0.40 11.45 ?  40  ASN   A CG   1 
ATOM   1036 O OD1  A ASN   A 1 40  ? 28.827 4.507   -3.729  0.60 12.96 ?  40  ASN   A OD1  1 
ATOM   1037 O OD1  B ASN   A 1 40  ? 28.494 4.562   -3.856  0.40 12.65 ?  40  ASN   A OD1  1 
ATOM   1038 N ND2  A ASN   A 1 40  ? 26.684 5.184   -3.883  0.60 12.88 ?  40  ASN   A ND2  1 
ATOM   1039 N ND2  B ASN   A 1 40  ? 26.305 5.070   -3.904  0.40 10.89 ?  40  ASN   A ND2  1 
ATOM   1040 H H    A ASN   A 1 40  ? 27.384 2.515   -1.989  0.60 12.08 ?  40  ASN   A H    1 
ATOM   1041 H H    B ASN   A 1 40  ? 27.104 2.503   -2.238  0.40 12.67 ?  40  ASN   A H    1 
ATOM   1042 H HA   A ASN   A 1 40  ? 27.381 0.940   -4.189  0.60 12.57 ?  40  ASN   A HA   1 
ATOM   1043 H HA   B ASN   A 1 40  ? 27.142 0.925   -4.443  0.40 13.01 ?  40  ASN   A HA   1 
ATOM   1044 H HB2  A ASN   A 1 40  ? 27.612 2.858   -5.500  0.60 13.60 ?  40  ASN   A HB2  1 
ATOM   1045 H HB2  B ASN   A 1 40  ? 27.456 2.925   -5.679  0.40 13.51 ?  40  ASN   A HB2  1 
ATOM   1046 H HB3  A ASN   A 1 40  ? 26.270 2.918   -4.653  0.60 13.60 ?  40  ASN   A HB3  1 
ATOM   1047 H HB3  B ASN   A 1 40  ? 26.050 2.887   -4.944  0.40 13.51 ?  40  ASN   A HB3  1 
ATOM   1048 H HD21 A ASN   A 1 40  ? 26.865 5.969   -3.576  0.60 15.43 ?  40  ASN   A HD21 1 
ATOM   1049 H HD21 B ASN   A 1 40  ? 26.435 5.830   -3.527  0.40 13.04 ?  40  ASN   A HD21 1 
ATOM   1050 H HD22 A ASN   A 1 40  ? 25.875 4.988   -4.100  0.60 15.43 ?  40  ASN   A HD22 1 
ATOM   1051 H HD22 B ASN   A 1 40  ? 25.505 4.830   -4.121  0.40 13.04 ?  40  ASN   A HD22 1 
ATOM   1052 N N    A VAL   A 1 41  ? 29.827 1.336   -4.881  0.60 10.75 ?  41  VAL   A N    1 
ATOM   1053 N N    B VAL   A 1 41  ? 29.640 1.450   -5.084  0.40 10.77 ?  41  VAL   A N    1 
ATOM   1054 C CA   A VAL   A 1 41  ? 31.262 1.057   -4.929  0.60 11.54 ?  41  VAL   A CA   1 
ATOM   1055 C CA   B VAL   A 1 41  ? 31.067 1.110   -5.117  0.40 11.51 ?  41  VAL   A CA   1 
ATOM   1056 C C    A VAL   A 1 41  ? 32.076 2.246   -4.470  0.60 11.70 ?  41  VAL   A C    1 
ATOM   1057 C C    B VAL   A 1 41  ? 31.985 2.209   -4.576  0.40 11.32 ?  41  VAL   A C    1 
ATOM   1058 O O    A VAL   A 1 41  ? 33.217 2.074   -4.028  0.60 12.54 ?  41  VAL   A O    1 
ATOM   1059 O O    B VAL   A 1 41  ? 33.124 1.922   -4.187  0.40 11.28 ?  41  VAL   A O    1 
ATOM   1060 C CB   A VAL   A 1 41  ? 31.757 0.574   -6.317  0.60 11.72 ?  41  VAL   A CB   1 
ATOM   1061 C CB   B VAL   A 1 41  ? 31.497 0.693   -6.537  0.40 12.46 ?  41  VAL   A CB   1 
ATOM   1062 C CG1  A VAL   A 1 41  ? 31.017 -0.685  -6.747  0.60 13.03 ?  41  VAL   A CG1  1 
ATOM   1063 C CG1  B VAL   A 1 41  ? 30.914 -0.671  -6.887  0.40 13.43 ?  41  VAL   A CG1  1 
ATOM   1064 C CG2  A VAL   A 1 41  ? 31.662 1.682   -7.376  0.60 10.80 ?  41  VAL   A CG2  1 
ATOM   1065 C CG2  B VAL   A 1 41  ? 31.091 1.750   -7.563  0.40 12.95 ?  41  VAL   A CG2  1 
ATOM   1066 H H    A VAL   A 1 41  ? 29.441 1.303   -5.646  0.60 12.87 ?  41  VAL   A H    1 
ATOM   1067 H H    B VAL   A 1 41  ? 29.254 1.491   -5.854  0.40 12.91 ?  41  VAL   A H    1 
ATOM   1068 H HA   A VAL   A 1 41  ? 31.456 0.339   -4.309  0.60 13.83 ?  41  VAL   A HA   1 
ATOM   1069 H HA   B VAL   A 1 41  ? 31.190 0.338   -4.549  0.40 13.79 ?  41  VAL   A HA   1 
ATOM   1070 H HB   A VAL   A 1 41  ? 32.699 0.338   -6.243  0.60 14.04 ?  41  VAL   A HB   1 
ATOM   1071 H HB   B VAL   A 1 41  ? 32.460 0.614   -6.558  0.40 14.93 ?  41  VAL   A HB   1 
ATOM   1072 H HG11 A VAL   A 1 41  ? 31.360 -0.978  -7.606  0.60 15.61 ?  41  VAL   A HG11 1 
ATOM   1073 H HG11 B VAL   A 1 41  ? 31.239 -0.939  -7.760  0.40 16.10 ?  41  VAL   A HG11 1 
ATOM   1074 H HG12 A VAL   A 1 41  ? 31.159 -1.376  -6.081  0.60 15.61 ?  41  VAL   A HG12 1 
ATOM   1075 H HG12 B VAL   A 1 41  ? 31.197 -1.315  -6.217  0.40 16.10 ?  41  VAL   A HG12 1 
ATOM   1076 H HG13 A VAL   A 1 41  ? 30.072 -0.483  -6.819  0.60 15.61 ?  41  VAL   A HG13 1 
ATOM   1077 H HG13 B VAL   A 1 41  ? 29.946 -0.609  -6.897  0.40 16.10 ?  41  VAL   A HG13 1 
ATOM   1078 H HG21 A VAL   A 1 41  ? 31.836 1.298   -8.253  0.60 12.94 ?  41  VAL   A HG21 1 
ATOM   1079 H HG21 B VAL   A 1 41  ? 31.542 1.563   -8.400  0.40 15.52 ?  41  VAL   A HG21 1 
ATOM   1080 H HG22 A VAL   A 1 41  ? 30.775 2.065   -7.352  0.60 12.94 ?  41  VAL   A HG22 1 
ATOM   1081 H HG22 B VAL   A 1 41  ? 30.129 1.716   -7.695  0.40 15.52 ?  41  VAL   A HG22 1 
ATOM   1082 H HG23 A VAL   A 1 41  ? 32.326 2.364   -7.183  0.60 12.94 ?  41  VAL   A HG23 1 
ATOM   1083 H HG23 B VAL   A 1 41  ? 31.351 2.623   -7.234  0.40 15.52 ?  41  VAL   A HG23 1 
ATOM   1084 N N    . TYR   A 1 42  ? 31.530 3.461   -4.570  1.00 11.87 ?  42  TYR   A N    1 
ATOM   1085 C CA   . TYR   A 1 42  ? 32.279 4.641   -4.147  1.00 11.68 ?  42  TYR   A CA   1 
ATOM   1086 C C    . TYR   A 1 42  ? 32.013 5.008   -2.699  1.00 11.77 ?  42  TYR   A C    1 
ATOM   1087 O O    . TYR   A 1 42  ? 32.581 5.992   -2.205  1.00 12.09 ?  42  TYR   A O    1 
ATOM   1088 C CB   . TYR   A 1 42  ? 31.948 5.836   -5.064  1.00 12.59 ?  42  TYR   A CB   1 
ATOM   1089 C CG   . TYR   A 1 42  ? 32.132 5.529   -6.534  1.00 13.65 ?  42  TYR   A CG   1 
ATOM   1090 C CD1  . TYR   A 1 42  ? 33.396 5.336   -7.068  1.00 14.33 ?  42  TYR   A CD1  1 
ATOM   1091 C CD2  . TYR   A 1 42  ? 31.044 5.414   -7.386  1.00 15.13 ?  42  TYR   A CD2  1 
ATOM   1092 C CE1  . TYR   A 1 42  ? 33.571 5.030   -8.408  1.00 14.94 ?  42  TYR   A CE1  1 
ATOM   1093 C CE2  . TYR   A 1 42  ? 31.215 5.124   -8.733  1.00 16.02 ?  42  TYR   A CE2  1 
ATOM   1094 C CZ   . TYR   A 1 42  ? 32.481 4.934   -9.235  1.00 15.91 ?  42  TYR   A CZ   1 
ATOM   1095 O OH   . TYR   A 1 42  ? 32.651 4.636   -10.566 1.00 17.69 ?  42  TYR   A OH   1 
ATOM   1096 H H    A TYR   A 1 42  ? 30.742 3.620   -4.876  0.60 14.22 ?  42  TYR   A H    1 
ATOM   1097 H H    B TYR   A 1 42  ? 30.739 3.662   -4.841  0.40 14.22 ?  42  TYR   A H    1 
ATOM   1098 H HA   . TYR   A 1 42  ? 33.224 4.465   -4.240  1.00 13.99 ?  42  TYR   A HA   1 
ATOM   1099 H HB2  . TYR   A 1 42  ? 31.022 6.097   -4.930  1.00 15.09 ?  42  TYR   A HB2  1 
ATOM   1100 H HB3  . TYR   A 1 42  ? 32.533 6.580   -4.841  1.00 15.09 ?  42  TYR   A HB3  1 
ATOM   1101 H HD1  . TYR   A 1 42  ? 34.139 5.392   -6.514  1.00 17.17 ?  42  TYR   A HD1  1 
ATOM   1102 H HD2  . TYR   A 1 42  ? 30.189 5.551   -7.053  1.00 18.13 ?  42  TYR   A HD2  1 
ATOM   1103 H HE1  . TYR   A 1 42  ? 34.426 4.902   -8.750  1.00 17.90 ?  42  TYR   A HE1  1 
ATOM   1104 H HE2  . TYR   A 1 42  ? 30.477 5.061   -9.296  1.00 19.20 ?  42  TYR   A HE2  1 
ATOM   1105 H HH   . TYR   A 1 42  ? 33.470 4.539   -10.737 1.00 21.20 ?  42  TYR   A HH   1 
ATOM   1106 N N    A LEU   A 1 43  ? 31.171 4.244   -2.004  0.60 11.36 ?  43  LEU   A N    1 
ATOM   1107 N N    B LEU   A 1 43  ? 31.147 4.254   -2.021  0.40 11.35 ?  43  LEU   A N    1 
ATOM   1108 C CA   A LEU   A 1 43  ? 30.752 4.564   -0.638  0.60 11.21 ?  43  LEU   A CA   1 
ATOM   1109 C CA   B LEU   A 1 43  ? 30.678 4.583   -0.676  0.40 11.19 ?  43  LEU   A CA   1 
ATOM   1110 C C    A LEU   A 1 43  ? 30.284 6.013   -0.520  0.60 11.19 ?  43  LEU   A C    1 
ATOM   1111 C C    B LEU   A 1 43  ? 30.172 6.020   -0.591  0.40 11.26 ?  43  LEU   A C    1 
ATOM   1112 O O    A LEU   A 1 43  ? 30.571 6.702   0.461   0.60 12.02 ?  43  LEU   A O    1 
ATOM   1113 O O    B LEU   A 1 43  ? 30.397 6.722   0.396   0.40 11.63 ?  43  LEU   A O    1 
ATOM   1114 C CB   A LEU   A 1 43  ? 31.837 4.250   0.394   0.60 11.54 ?  43  LEU   A CB   1 
ATOM   1115 C CB   B LEU   A 1 43  ? 31.732 4.285   0.390   0.40 11.03 ?  43  LEU   A CB   1 
ATOM   1116 C CG   A LEU   A 1 43  ? 32.370 2.812   0.466   0.60 11.56 ?  43  LEU   A CG   1 
ATOM   1117 C CG   B LEU   A 1 43  ? 32.175 2.820   0.476   0.40 11.12 ?  43  LEU   A CG   1 
ATOM   1118 C CD1  A LEU   A 1 43  ? 33.432 2.720   1.547   0.60 12.29 ?  43  LEU   A CD1  1 
ATOM   1119 C CD1  B LEU   A 1 43  ? 33.214 2.651   1.567   0.40 11.79 ?  43  LEU   A CD1  1 
ATOM   1120 C CD2  A LEU   A 1 43  ? 31.263 1.801   0.722   0.60 11.92 ?  43  LEU   A CD2  1 
ATOM   1121 C CD2  B LEU   A 1 43  ? 30.988 1.882   0.706   0.40 11.50 ?  43  LEU   A CD2  1 
ATOM   1122 H H    A LEU   A 1 43  ? 30.819 3.511   -2.307  0.60 13.61 ?  43  LEU   A H    1 
ATOM   1123 H H    B LEU   A 1 43  ? 30.805 3.520   -2.329  0.40 13.60 ?  43  LEU   A H    1 
ATOM   1124 H HA   A LEU   A 1 43  ? 29.990 4.000   -0.423  0.60 13.43 ?  43  LEU   A HA   1 
ATOM   1125 H HA   B LEU   A 1 43  ? 29.916 4.013   -0.485  0.40 13.41 ?  43  LEU   A HA   1 
ATOM   1126 H HB2  A LEU   A 1 43  ? 32.594 4.826   0.216   0.60 13.83 ?  43  LEU   A HB2  1 
ATOM   1127 H HB2  B LEU   A 1 43  ? 32.519 4.819   0.204   0.40 13.21 ?  43  LEU   A HB2  1 
ATOM   1128 H HB3  A LEU   A 1 43  ? 31.476 4.457   1.270   0.60 13.83 ?  43  LEU   A HB3  1 
ATOM   1129 H HB3  B LEU   A 1 43  ? 31.368 4.530   1.255   0.40 13.21 ?  43  LEU   A HB3  1 
ATOM   1130 H HG   A LEU   A 1 43  ? 32.789 2.589   -0.380  0.60 13.85 ?  43  LEU   A HG   1 
ATOM   1131 H HG   B LEU   A 1 43  ? 32.586 2.572   -0.366  0.40 13.32 ?  43  LEU   A HG   1 
ATOM   1132 H HD11 A LEU   A 1 43  ? 33.764 1.808   1.585   0.60 14.73 ?  43  LEU   A HD11 1 
ATOM   1133 H HD11 B LEU   A 1 43  ? 33.484 1.720   1.603   0.40 14.12 ?  43  LEU   A HD11 1 
ATOM   1134 H HD12 A LEU   A 1 43  ? 34.156 3.327   1.333   0.60 14.73 ?  43  LEU   A HD12 1 
ATOM   1135 H HD12 B LEU   A 1 43  ? 33.980 3.210   1.362   0.40 14.12 ?  43  LEU   A HD12 1 
ATOM   1136 H HD13 A LEU   A 1 43  ? 33.036 2.961   2.400   0.60 14.73 ?  43  LEU   A HD13 1 
ATOM   1137 H HD13 B LEU   A 1 43  ? 32.827 2.917   2.416   0.40 14.12 ?  43  LEU   A HD13 1 
ATOM   1138 H HD21 A LEU   A 1 43  ? 31.657 0.921   0.819   0.60 14.28 ?  43  LEU   A HD21 1 
ATOM   1139 H HD21 B LEU   A 1 43  ? 31.322 0.999   0.922   0.40 13.77 ?  43  LEU   A HD21 1 
ATOM   1140 H HD22 A LEU   A 1 43  ? 30.795 2.048   1.535   0.60 14.28 ?  43  LEU   A HD22 1 
ATOM   1141 H HD22 B LEU   A 1 43  ? 30.453 2.224   1.439   0.40 13.77 ?  43  LEU   A HD22 1 
ATOM   1142 H HD23 A LEU   A 1 43  ? 30.650 1.811   -0.029  0.60 14.28 ?  43  LEU   A HD23 1 
ATOM   1143 H HD23 B LEU   A 1 43  ? 30.453 1.845   -0.103  0.40 13.77 ?  43  LEU   A HD23 1 
ATOM   1144 N N    A LYS   A 1 44  ? 29.554 6.476   -1.536  0.60 11.11 ?  44  LYS   A N    1 
ATOM   1145 N N    B LYS   A 1 44  ? 29.467 6.454   -1.636  0.40 11.32 ?  44  LYS   A N    1 
ATOM   1146 C CA   A LYS   A 1 44  ? 28.931 7.798   -1.515  0.60 11.60 ?  44  LYS   A CA   1 
ATOM   1147 C CA   B LYS   A 1 44  ? 28.776 7.742   -1.636  0.40 12.06 ?  44  LYS   A CA   1 
ATOM   1148 C C    A LYS   A 1 44  ? 27.504 7.613   -1.018  0.60 10.61 ?  44  LYS   A C    1 
ATOM   1149 C C    B LYS   A 1 44  ? 27.370 7.500   -1.107  0.40 11.84 ?  44  LYS   A C    1 
ATOM   1150 O O    A LYS   A 1 44  ? 26.636 7.120   -1.742  0.60 11.97 ?  44  LYS   A O    1 
ATOM   1151 O O    B LYS   A 1 44  ? 26.508 6.968   -1.810  0.40 12.33 ?  44  LYS   A O    1 
ATOM   1152 C CB   A LYS   A 1 44  ? 28.983 8.445   -2.894  0.60 13.76 ?  44  LYS   A CB   1 
ATOM   1153 C CB   B LYS   A 1 44  ? 28.758 8.351   -3.033  0.40 14.29 ?  44  LYS   A CB   1 
ATOM   1154 C CG   A LYS   A 1 44  ? 30.379 8.871   -3.324  0.60 16.97 ?  44  LYS   A CG   1 
ATOM   1155 C CG   B LYS   A 1 44  ? 30.113 8.841   -3.512  0.40 17.41 ?  44  LYS   A CG   1 
ATOM   1156 C CD   A LYS   A 1 44  ? 31.049 9.784   -2.299  0.60 21.72 ?  44  LYS   A CD   1 
ATOM   1157 C CD   B LYS   A 1 44  ? 30.789 9.739   -2.483  0.40 21.09 ?  44  LYS   A CD   1 
ATOM   1158 C CE   A LYS   A 1 44  ? 32.384 10.301  -2.803  0.60 24.50 ?  44  LYS   A CE   1 
ATOM   1159 C CE   B LYS   A 1 44  ? 32.095 10.294  -3.018  0.40 23.34 ?  44  LYS   A CE   1 
ATOM   1160 N NZ   A LYS   A 1 44  ? 33.157 10.982  -1.732  0.60 26.05 ?  44  LYS   A NZ   1 
ATOM   1161 N NZ   B LYS   A 1 44  ? 32.901 10.966  -1.963  0.40 24.65 ?  44  LYS   A NZ   1 
ATOM   1162 H H    A LYS   A 1 44  ? 29.407 6.037   -2.262  0.60 13.31 ?  44  LYS   A H    1 
ATOM   1163 H H    B LYS   A 1 44  ? 29.370 6.013   -2.369  0.40 13.56 ?  44  LYS   A H    1 
ATOM   1164 H HA   A LYS   A 1 44  ? 29.396 8.365   -0.878  0.60 13.90 ?  44  LYS   A HA   1 
ATOM   1165 H HA   B LYS   A 1 44  ? 29.216 8.349   -1.021  0.40 14.45 ?  44  LYS   A HA   1 
ATOM   1166 H HB2  A LYS   A 1 44  ? 28.655 7.812   -3.551  0.60 16.49 ?  44  LYS   A HB2  1 
ATOM   1167 H HB2  B LYS   A 1 44  ? 28.449 7.682   -3.664  0.40 17.13 ?  44  LYS   A HB2  1 
ATOM   1168 H HB3  A LYS   A 1 44  ? 28.424 9.237   -2.891  0.60 16.49 ?  44  LYS   A HB3  1 
ATOM   1169 H HB3  B LYS   A 1 44  ? 28.155 9.111   -3.038  0.40 17.13 ?  44  LYS   A HB3  1 
ATOM   1170 H HG2  A LYS   A 1 44  ? 30.935 8.083   -3.434  0.60 20.34 ?  44  LYS   A HG2  1 
ATOM   1171 H HG2  B LYS   A 1 44  ? 30.690 8.078   -3.675  0.40 20.87 ?  44  LYS   A HG2  1 
ATOM   1172 H HG3  A LYS   A 1 44  ? 30.322 9.357   -4.164  0.60 20.34 ?  44  LYS   A HG3  1 
ATOM   1173 H HG3  B LYS   A 1 44  ? 30.000 9.353   -4.330  0.40 20.87 ?  44  LYS   A HG3  1 
ATOM   1174 H HD2  A LYS   A 1 44  ? 30.465 10.538  -2.120  0.60 26.04 ?  44  LYS   A HD2  1 
ATOM   1175 H HD2  B LYS   A 1 44  ? 30.200 10.477  -2.260  0.40 25.29 ?  44  LYS   A HD2  1 
ATOM   1176 H HD3  A LYS   A 1 44  ? 31.210 9.282   -1.484  0.60 26.04 ?  44  LYS   A HD3  1 
ATOM   1177 H HD3  B LYS   A 1 44  ? 30.998 9.221   -1.687  0.40 25.29 ?  44  LYS   A HD3  1 
ATOM   1178 H HE2  A LYS   A 1 44  ? 32.910 9.552   -3.127  0.60 29.38 ?  44  LYS   A HE2  1 
ATOM   1179 H HE2  B LYS   A 1 44  ? 32.623 9.564   -3.381  0.40 27.98 ?  44  LYS   A HE2  1 
ATOM   1180 H HE3  A LYS   A 1 44  ? 32.227 10.934  -3.519  0.60 29.38 ?  44  LYS   A HE3  1 
ATOM   1181 H HE3  B LYS   A 1 44  ? 31.902 10.942  -3.710  0.40 27.98 ?  44  LYS   A HE3  1 
ATOM   1182 H HZ1  A LYS   A 1 44  ? 33.932 11.270  -2.055  0.60 31.23 ?  44  LYS   A HZ1  1 
ATOM   1183 H HZ1  B LYS   A 1 44  ? 33.659 11.278  -2.313  0.40 29.56 ?  44  LYS   A HZ1  1 
ATOM   1184 H HZ2  A LYS   A 1 44  ? 32.694 11.679  -1.423  0.60 31.23 ?  44  LYS   A HZ2  1 
ATOM   1185 H HZ2  B LYS   A 1 44  ? 32.442 11.644  -1.615  0.40 29.56 ?  44  LYS   A HZ2  1 
ATOM   1186 H HZ3  A LYS   A 1 44  ? 33.310 10.419  -1.062  0.60 31.23 ?  44  LYS   A HZ3  1 
ATOM   1187 H HZ3  B LYS   A 1 44  ? 33.099 10.388  -1.315  0.40 29.56 ?  44  LYS   A HZ3  1 
ATOM   1188 N N    A HIS   A 1 45  ? 27.267 7.996   0.232   0.60 10.03 ?  45  HIS   A N    1 
ATOM   1189 N N    B HIS   A 1 45  ? 27.145 7.882   0.148   0.40 11.84 ?  45  HIS   A N    1 
ATOM   1190 C CA   A HIS   A 1 45  ? 26.034 7.633   0.930   0.60 10.39 ?  45  HIS   A CA   1 
ATOM   1191 C CA   B HIS   A 1 45  ? 25.894 7.585   0.842   0.40 11.98 ?  45  HIS   A CA   1 
ATOM   1192 C C    A HIS   A 1 45  ? 24.990 8.743   0.790   0.60 11.24 ?  45  HIS   A C    1 
ATOM   1193 C C    B HIS   A 1 45  ? 24.923 8.741   0.623   0.40 12.13 ?  45  HIS   A C    1 
ATOM   1194 O O    A HIS   A 1 45  ? 24.588 9.395   1.754   0.60 11.91 ?  45  HIS   A O    1 
ATOM   1195 O O    B HIS   A 1 45  ? 24.782 9.646   1.448   0.40 13.10 ?  45  HIS   A O    1 
ATOM   1196 C CB   A HIS   A 1 45  ? 26.340 7.336   2.387   0.60 9.89  ?  45  HIS   A CB   1 
ATOM   1197 C CB   B HIS   A 1 45  ? 26.169 7.362   2.319   0.40 11.58 ?  45  HIS   A CB   1 
ATOM   1198 C CG   A HIS   A 1 45  ? 27.453 6.356   2.577   0.60 10.01 ?  45  HIS   A CG   1 
ATOM   1199 C CG   B HIS   A 1 45  ? 27.313 6.435   2.580   0.40 10.83 ?  45  HIS   A CG   1 
ATOM   1200 N ND1  A HIS   A 1 45  ? 27.422 5.078   2.058   0.60 10.69 ?  45  HIS   A ND1  1 
ATOM   1201 N ND1  B HIS   A 1 45  ? 27.346 5.141   2.105   0.40 10.77 ?  45  HIS   A ND1  1 
ATOM   1202 C CD2  A HIS   A 1 45  ? 28.637 6.478   3.220   0.60 11.02 ?  45  HIS   A CD2  1 
ATOM   1203 C CD2  B HIS   A 1 45  ? 28.471 6.622   3.255   0.40 10.38 ?  45  HIS   A CD2  1 
ATOM   1204 C CE1  A HIS   A 1 45  ? 28.538 4.453   2.388   0.60 10.76 ?  45  HIS   A CE1  1 
ATOM   1205 C CE1  B HIS   A 1 45  ? 28.474 4.569   2.487   0.40 9.96  ?  45  HIS   A CE1  1 
ATOM   1206 N NE2  A HIS   A 1 45  ? 29.294 5.280   3.090   0.60 11.23 ?  45  HIS   A NE2  1 
ATOM   1207 N NE2  B HIS   A 1 45  ? 29.176 5.446   3.184   0.40 9.71  ?  45  HIS   A NE2  1 
ATOM   1208 H H    A HIS   A 1 45  ? 27.809 8.474   0.706   0.60 12.01 ?  45  HIS   A H    1 
ATOM   1209 H H    B HIS   A 1 45  ? 27.708 8.321   0.627   0.40 14.19 ?  45  HIS   A H    1 
ATOM   1210 H HA   A HIS   A 1 45  ? 25.668 6.836   0.529   0.60 12.44 ?  45  HIS   A HA   1 
ATOM   1211 H HA   B HIS   A 1 45  ? 25.503 6.775   0.475   0.40 14.35 ?  45  HIS   A HA   1 
ATOM   1212 H HB2  A HIS   A 1 45  ? 26.588 8.162   2.832   0.60 11.84 ?  45  HIS   A HB2  1 
ATOM   1213 H HB2  B HIS   A 1 45  ? 26.378 8.215   2.730   0.40 13.87 ?  45  HIS   A HB2  1 
ATOM   1214 H HB3  A HIS   A 1 45  ? 25.544 6.966   2.802   0.60 11.84 ?  45  HIS   A HB3  1 
ATOM   1215 H HB3  B HIS   A 1 45  ? 25.377 6.983   2.733   0.40 13.87 ?  45  HIS   A HB3  1 
ATOM   1216 H HD2  A HIS   A 1 45  ? 28.949 7.233   3.667   0.60 13.20 ?  45  HIS   A HD2  1 
ATOM   1217 H HD2  B HIS   A 1 45  ? 28.739 7.402   3.687   0.40 12.43 ?  45  HIS   A HD2  1 
ATOM   1218 H HE1  A HIS   A 1 45  ? 28.756 3.576   2.165   0.60 12.88 ?  45  HIS   A HE1  1 
ATOM   1219 H HE1  B HIS   A 1 45  ? 28.730 3.696   2.296   0.40 11.93 ?  45  HIS   A HE1  1 
ATOM   1220 H HE2  A HIS   A 1 45  ? 30.069 5.097   3.414   0.60 13.45 ?  45  HIS   A HE2  1 
ATOM   1221 H HE2  B HIS   A 1 45  ? 29.946 5.303   3.536   0.40 11.63 ?  45  HIS   A HE2  1 
ATOM   1222 N N    A GLY   A 1 46  ? 24.532 8.935   -0.444  0.60 12.32 ?  46  GLY   A N    1 
ATOM   1223 N N    B GLY   A 1 46  ? 24.238 8.702   -0.516  0.40 12.11 ?  46  GLY   A N    1 
ATOM   1224 C CA   A GLY   A 1 46  ? 23.734 10.104  -0.763  0.60 13.08 ?  46  GLY   A CA   1 
ATOM   1225 C CA   B GLY   A 1 46  ? 23.382 9.806   -0.902  0.40 12.33 ?  46  GLY   A CA   1 
ATOM   1226 C C    A GLY   A 1 46  ? 22.238 9.980   -0.548  0.60 13.25 ?  46  GLY   A C    1 
ATOM   1227 C C    B GLY   A 1 46  ? 21.927 9.678   -0.497  0.40 12.47 ?  46  GLY   A C    1 
ATOM   1228 O O    A GLY   A 1 46  ? 21.564 10.989  -0.311  0.60 14.11 ?  46  GLY   A O    1 
ATOM   1229 O O    B GLY   A 1 46  ? 21.313 10.663  -0.071  0.40 13.00 ?  46  GLY   A O    1 
ATOM   1230 H H    A GLY   A 1 46  ? 24.659 8.404   -1.106  0.60 14.76 ?  46  GLY   A H    1 
ATOM   1231 H H    B GLY   A 1 46  ? 24.259 8.052   -1.080  0.40 14.51 ?  46  GLY   A H    1 
ATOM   1232 H HA2  A GLY   A 1 46  ? 24.045 10.852  -0.225  0.60 15.67 ?  46  GLY   A HA2  1 
ATOM   1233 H HA2  B GLY   A 1 46  ? 23.717 10.621  -0.500  0.40 14.77 ?  46  GLY   A HA2  1 
ATOM   1234 H HA3  A GLY   A 1 46  ? 23.870 10.335  -1.694  0.60 15.67 ?  46  GLY   A HA3  1 
ATOM   1235 H HA3  B GLY   A 1 46  ? 23.418 9.909   -1.864  0.40 14.77 ?  46  GLY   A HA3  1 
ATOM   1236 N N    A GLY   A 1 47  ? 21.703 8.768   -0.643  0.60 13.07 ?  47  GLY   A N    1 
ATOM   1237 N N    B GLY   A 1 47  ? 21.353 8.483   -0.624  0.40 12.48 ?  47  GLY   A N    1 
ATOM   1238 C CA   A GLY   A 1 47  ? 20.265 8.579   -0.628  0.60 13.58 ?  47  GLY   A CA   1 
ATOM   1239 C CA   B GLY   A 1 47  ? 19.935 8.312   -0.387  0.40 12.32 ?  47  GLY   A CA   1 
ATOM   1240 C C    A GLY   A 1 47  ? 19.932 7.139   -0.305  0.60 12.50 ?  47  GLY   A C    1 
ATOM   1241 C C    B GLY   A 1 47  ? 19.607 6.908   0.068   0.40 11.55 ?  47  GLY   A C    1 
ATOM   1242 O O    A GLY   A 1 47  ? 20.815 6.309   -0.080  0.60 12.38 ?  47  GLY   A O    1 
ATOM   1243 O O    B GLY   A 1 47  ? 20.493 6.080   0.288   0.40 11.54 ?  47  GLY   A O    1 
ATOM   1244 H H    A GLY   A 1 47  ? 22.156 8.043   -0.703  0.60 15.66 ?  47  GLY   A H    1 
ATOM   1245 H H    B GLY   A 1 47  ? 21.768 7.756   -0.839  0.40 14.95 ?  47  GLY   A H    1 
ATOM   1246 H HA2  A GLY   A 1 47  ? 19.859 9.154   0.039   0.60 16.27 ?  47  GLY   A HA2  1 
ATOM   1247 H HA2  B GLY   A 1 47  ? 19.644 8.925   0.302   0.40 14.76 ?  47  GLY   A HA2  1 
ATOM   1248 H HA3  A GLY   A 1 47  ? 19.900 8.802   -1.501  0.60 16.27 ?  47  GLY   A HA3  1 
ATOM   1249 H HA3  B GLY   A 1 47  ? 19.443 8.503   -1.201  0.40 14.76 ?  47  GLY   A HA3  1 
ATOM   1250 N N    A GLY   A 1 48  ? 18.638 6.842   -0.297  0.60 12.09 ?  48  GLY   A N    1 
ATOM   1251 N N    B GLY   A 1 48  ? 18.309 6.644   0.209   0.40 11.67 ?  48  GLY   A N    1 
ATOM   1252 C CA   A GLY   A 1 48  ? 18.195 5.517   0.075   0.60 11.94 ?  48  GLY   A CA   1 
ATOM   1253 C CA   B GLY   A 1 48  ? 17.876 5.339   0.674   0.40 11.18 ?  48  GLY   A CA   1 
ATOM   1254 C C    A GLY   A 1 48  ? 18.604 5.175   1.493   0.60 11.35 ?  48  GLY   A C    1 
ATOM   1255 C C    B GLY   A 1 48  ? 18.480 4.998   2.023   0.40 11.04 ?  48  GLY   A C    1 
ATOM   1256 O O    A GLY   A 1 48  ? 18.771 6.048   2.355   0.60 12.01 ?  48  GLY   A O    1 
ATOM   1257 O O    B GLY   A 1 48  ? 18.620 5.851   2.908   0.40 11.29 ?  48  GLY   A O    1 
ATOM   1258 H H    A GLY   A 1 48  ? 18.013 7.387   -0.500  0.60 14.48 ?  48  GLY   A H    1 
ATOM   1259 H H    B GLY   A 1 48  ? 17.664 7.200   0.049   0.40 13.98 ?  48  GLY   A H    1 
ATOM   1260 H HA2  A GLY   A 1 48  ? 17.230 5.465   0.004   0.60 14.31 ?  48  GLY   A HA2  1 
ATOM   1261 H HA2  B GLY   A 1 48  ? 16.905 5.320   0.746   0.40 13.39 ?  48  GLY   A HA2  1 
ATOM   1262 H HA3  A GLY   A 1 48  ? 18.588 4.857   -0.516  0.60 14.31 ?  48  GLY   A HA3  1 
ATOM   1263 H HA3  B GLY   A 1 48  ? 18.145 4.660   0.035   0.40 13.39 ?  48  GLY   A HA3  1 
ATOM   1264 N N    A VAL   A 1 49  ? 18.781 3.874   1.736   0.60 11.79 ?  49  VAL   A N    1 
ATOM   1265 N N    B VAL   A 1 49  ? 18.839 3.723   2.182   0.40 10.25 ?  49  VAL   A N    1 
ATOM   1266 C CA   A VAL   A 1 49  ? 19.250 3.406   3.038   0.60 12.10 ?  49  VAL   A CA   1 
ATOM   1267 C CA   B VAL   A 1 49  ? 19.419 3.242   3.435   0.40 10.28 ?  49  VAL   A CA   1 
ATOM   1268 C C    A VAL   A 1 49  ? 20.572 4.072   3.397   0.60 10.66 ?  49  VAL   A C    1 
ATOM   1269 C C    B VAL   A 1 49  ? 20.715 3.978   3.750   0.40 9.90  ?  49  VAL   A C    1 
ATOM   1270 O O    A VAL   A 1 49  ? 20.776 4.510   4.534   0.60 10.77 ?  49  VAL   A O    1 
ATOM   1271 O O    B VAL   A 1 49  ? 20.962 4.367   4.898   0.40 9.36  ?  49  VAL   A O    1 
ATOM   1272 C CB   A VAL   A 1 49  ? 19.377 1.868   3.044   0.60 13.18 ?  49  VAL   A CB   1 
ATOM   1273 C CB   B VAL   A 1 49  ? 19.637 1.719   3.362   0.40 10.66 ?  49  VAL   A CB   1 
ATOM   1274 C CG1  A VAL   A 1 49  ? 20.089 1.399   4.312   0.60 13.39 ?  49  VAL   A CG1  1 
ATOM   1275 C CG1  B VAL   A 1 49  ? 20.604 1.275   4.441   0.40 10.88 ?  49  VAL   A CG1  1 
ATOM   1276 C CG2  A VAL   A 1 49  ? 18.009 1.204   2.914   0.60 14.34 ?  49  VAL   A CG2  1 
ATOM   1277 C CG2  B VAL   A 1 49  ? 18.309 0.977   3.485   0.40 11.27 ?  49  VAL   A CG2  1 
ATOM   1278 H H    A VAL   A 1 49  ? 18.637 3.247   1.168   0.60 14.12 ?  49  VAL   A H    1 
ATOM   1279 H H    B VAL   A 1 49  ? 18.749 3.114   1.581   0.40 12.28 ?  49  VAL   A H    1 
ATOM   1280 H HA   A VAL   A 1 49  ? 18.602 3.643   3.718   0.60 14.50 ?  49  VAL   A HA   1 
ATOM   1281 H HA   B VAL   A 1 49  ? 18.799 3.417   4.160   0.40 12.31 ?  49  VAL   A HA   1 
ATOM   1282 H HB   A VAL   A 1 49  ? 19.916 1.587   2.286   0.60 15.80 ?  49  VAL   A HB   1 
ATOM   1283 H HB   B VAL   A 1 49  ? 20.024 1.494   2.500   0.40 12.77 ?  49  VAL   A HB   1 
ATOM   1284 H HG11 A VAL   A 1 49  ? 19.910 0.453   4.445   0.60 16.05 ?  49  VAL   A HG11 1 
ATOM   1285 H HG11 B VAL   A 1 49  ? 20.510 0.318   4.572   0.40 13.03 ?  49  VAL   A HG11 1 
ATOM   1286 H HG12 A VAL   A 1 49  ? 21.042 1.541   4.217   0.60 16.05 ?  49  VAL   A HG12 1 
ATOM   1287 H HG12 B VAL   A 1 49  ? 21.512 1.476   4.159   0.40 13.03 ?  49  VAL   A HG12 1 
ATOM   1288 H HG13 A VAL   A 1 49  ? 19.749 1.903   5.069   0.60 16.05 ?  49  VAL   A HG13 1 
ATOM   1289 H HG13 B VAL   A 1 49  ? 20.398 1.740   5.265   0.40 13.03 ?  49  VAL   A HG13 1 
ATOM   1290 H HG21 A VAL   A 1 49  ? 18.121 0.238   2.921   0.60 17.18 ?  49  VAL   A HG21 1 
ATOM   1291 H HG21 B VAL   A 1 49  ? 18.421 0.072   3.155   0.40 13.50 ?  49  VAL   A HG21 1 
ATOM   1292 H HG22 A VAL   A 1 49  ? 17.455 1.476   3.662   0.60 17.18 ?  49  VAL   A HG22 1 
ATOM   1293 H HG22 B VAL   A 1 49  ? 18.044 0.959   4.418   0.40 13.50 ?  49  VAL   A HG22 1 
ATOM   1294 H HG23 A VAL   A 1 49  ? 17.602 1.483   2.080   0.60 17.18 ?  49  VAL   A HG23 1 
ATOM   1295 H HG23 B VAL   A 1 49  ? 17.640 1.441   2.959   0.40 13.50 ?  49  VAL   A HG23 1 
ATOM   1296 N N    A ALA   A 1 50  ? 21.504 4.115   2.444   0.60 10.48 ?  50  ALA   A N    1 
ATOM   1297 N N    B ALA   A 1 50  ? 21.581 4.141   2.747   0.40 9.66  ?  50  ALA   A N    1 
ATOM   1298 C CA   A ALA   A 1 50  ? 22.832 4.651   2.727   0.60 10.39 ?  50  ALA   A CA   1 
ATOM   1299 C CA   B ALA   A 1 50  ? 22.897 4.719   2.998   0.40 9.51  ?  50  ALA   A CA   1 
ATOM   1300 C C    A ALA   A 1 50  ? 22.755 6.108   3.152   0.60 10.16 ?  50  ALA   A C    1 
ATOM   1301 C C    B ALA   A 1 50  ? 22.781 6.159   3.472   0.40 9.44  ?  50  ALA   A C    1 
ATOM   1302 O O    A ALA   A 1 50  ? 23.404 6.517   4.120   0.60 10.66 ?  50  ALA   A O    1 
ATOM   1303 O O    B ALA   A 1 50  ? 23.431 6.559   4.445   0.40 9.28  ?  50  ALA   A O    1 
ATOM   1304 C CB   A ALA   A 1 50  ? 23.725 4.507   1.497   0.60 10.55 ?  50  ALA   A CB   1 
ATOM   1305 C CB   B ALA   A 1 50  ? 23.762 4.631   1.741   0.40 9.83  ?  50  ALA   A CB   1 
ATOM   1306 H H    A ALA   A 1 50  ? 21.394 3.843   1.641   0.60 12.56 ?  50  ALA   A H    1 
ATOM   1307 H H    B ALA   A 1 50  ? 21.432 3.931   1.926   0.40 11.57 ?  50  ALA   A H    1 
ATOM   1308 H HA   A ALA   A 1 50  ? 23.232 4.158   3.458   0.60 12.45 ?  50  ALA   A HA   1 
ATOM   1309 H HA   B ALA   A 1 50  ? 23.336 4.217   3.698   0.40 11.39 ?  50  ALA   A HA   1 
ATOM   1310 H HB1  A ALA   A 1 50  ? 24.600 4.874   1.701   0.60 12.64 ?  50  ALA   A HB1  1 
ATOM   1311 H HB1  B ALA   A 1 50  ? 24.642 4.996   1.934   0.40 11.77 ?  50  ALA   A HB1  1 
ATOM   1312 H HB2  A ALA   A 1 50  ? 23.799 3.569   1.275   0.60 12.64 ?  50  ALA   A HB2  1 
ATOM   1313 H HB2  B ALA   A 1 50  ? 23.842 3.701   1.481   0.40 11.77 ?  50  ALA   A HB2  1 
ATOM   1314 H HB3  A ALA   A 1 50  ? 23.325 4.996   0.762   0.60 12.64 ?  50  ALA   A HB3  1 
ATOM   1315 H HB3  B ALA   A 1 50  ? 23.343 5.140   1.030   0.40 11.77 ?  50  ALA   A HB3  1 
ATOM   1316 N N    A GLY   A 1 51  ? 21.977 6.915   2.431   0.60 10.12 ?  51  GLY   A N    1 
ATOM   1317 N N    B GLY   A 1 51  ? 21.954 6.956   2.795   0.40 10.00 ?  51  GLY   A N    1 
ATOM   1318 C CA   A GLY   A 1 51  ? 21.851 8.314   2.802   0.60 10.26 ?  51  GLY   A CA   1 
ATOM   1319 C CA   B GLY   A 1 51  ? 21.753 8.326   3.233   0.40 10.30 ?  51  GLY   A CA   1 
ATOM   1320 C C    A GLY   A 1 51  ? 21.244 8.494   4.178   0.60 9.79  ?  51  GLY   A C    1 
ATOM   1321 C C    B GLY   A 1 51  ? 21.179 8.397   4.634   0.40 10.88 ?  51  GLY   A C    1 
ATOM   1322 O O    A GLY   A 1 51  ? 21.633 9.394   4.927   0.60 10.22 ?  51  GLY   A O    1 
ATOM   1323 O O    B GLY   A 1 51  ? 21.586 9.237   5.443   0.40 11.34 ?  51  GLY   A O    1 
ATOM   1324 H H    A GLY   A 1 51  ? 21.527 6.682   1.740   0.60 12.12 ?  51  GLY   A H    1 
ATOM   1325 H H    B GLY   A 1 51  ? 21.512 6.731   2.090   0.40 11.98 ?  51  GLY   A H    1 
ATOM   1326 H HA2  A GLY   A 1 51  ? 22.722 8.732   2.808   0.60 12.29 ?  51  GLY   A HA2  1 
ATOM   1327 H HA2  B GLY   A 1 51  ? 22.601 8.798   3.221   0.40 12.34 ?  51  GLY   A HA2  1 
ATOM   1328 H HA3  A GLY   A 1 51  ? 21.292 8.777   2.154   0.60 12.29 ?  51  GLY   A HA3  1 
ATOM   1329 H HA3  B GLY   A 1 51  ? 21.145 8.776   2.621   0.40 12.34 ?  51  GLY   A HA3  1 
ATOM   1330 N N    A ALA   A 1 52  ? 20.275 7.644   4.527   0.60 10.19 ?  52  ALA   A N    1 
ATOM   1331 N N    B ALA   A 1 52  ? 20.230 7.508   4.942   0.40 11.40 ?  52  ALA   A N    1 
ATOM   1332 C CA   A ALA   A 1 52  ? 19.627 7.742   5.831   0.60 10.57 ?  52  ALA   A CA   1 
ATOM   1333 C CA   B ALA   A 1 52  ? 19.623 7.493   6.268   0.40 11.14 ?  52  ALA   A CA   1 
ATOM   1334 C C    A ALA   A 1 52  ? 20.559 7.306   6.959   0.60 10.37 ?  52  ALA   A C    1 
ATOM   1335 C C    B ALA   A 1 52  ? 20.635 7.085   7.333   0.40 10.57 ?  52  ALA   A C    1 
ATOM   1336 O O    A ALA   A 1 52  ? 20.635 7.969   7.999   0.60 11.16 ?  52  ALA   A O    1 
ATOM   1337 O O    B ALA   A 1 52  ? 20.726 7.715   8.394   0.40 10.92 ?  52  ALA   A O    1 
ATOM   1338 C CB   A ALA   A 1 52  ? 18.342 6.912   5.834   0.60 12.00 ?  52  ALA   A CB   1 
ATOM   1339 C CB   B ALA   A 1 52  ? 18.413 6.557   6.277   0.40 12.22 ?  52  ALA   A CB   1 
ATOM   1340 H H    A ALA   A 1 52  ? 19.983 7.002   4.033   0.60 12.21 ?  52  ALA   A H    1 
ATOM   1341 H H    B ALA   A 1 52  ? 19.929 6.902   4.400   0.40 13.65 ?  52  ALA   A H    1 
ATOM   1342 H HA   A ALA   A 1 52  ? 19.376 8.663   5.988   0.60 12.66 ?  52  ALA   A HA   1 
ATOM   1343 H HA   B ALA   A 1 52  ? 19.314 8.382   6.478   0.40 13.34 ?  52  ALA   A HA   1 
ATOM   1344 H HB1  A ALA   A 1 52  ? 17.916 6.983   6.706   0.60 14.37 ?  52  ALA   A HB1  1 
ATOM   1345 H HB1  B ALA   A 1 52  ? 18.012 6.571   7.161   0.40 14.64 ?  52  ALA   A HB1  1 
ATOM   1346 H HB2  A ALA   A 1 52  ? 17.741 7.248   5.149   0.60 14.37 ?  52  ALA   A HB2  1 
ATOM   1347 H HB2  B ALA   A 1 52  ? 17.767 6.869   5.620   0.40 14.64 ?  52  ALA   A HB2  1 
ATOM   1348 H HB3  A ALA   A 1 52  ? 18.559 5.983   5.652   0.60 14.37 ?  52  ALA   A HB3  1 
ATOM   1349 H HB3  B ALA   A 1 52  ? 18.700 5.659   6.056   0.40 14.64 ?  52  ALA   A HB3  1 
ATOM   1350 N N    A LEU   A 1 53  ? 21.267 6.190   6.784   0.60 10.27 ?  53  LEU   A N    1 
ATOM   1351 N N    B LEU   A 1 53  ? 21.394 6.017   7.077   0.40 10.43 ?  53  LEU   A N    1 
ATOM   1352 C CA   A LEU   A 1 53  ? 22.203 5.751   7.814   0.60 10.82 ?  53  LEU   A CA   1 
ATOM   1353 C CA   B LEU   A 1 53  ? 22.450 5.634   8.009   0.40 10.30 ?  53  LEU   A CA   1 
ATOM   1354 C C    A LEU   A 1 53  ? 23.272 6.805   8.042   0.60 10.94 ?  53  LEU   A C    1 
ATOM   1355 C C    B LEU   A 1 53  ? 23.463 6.759   8.169   0.40 10.70 ?  53  LEU   A C    1 
ATOM   1356 O O    A LEU   A 1 53  ? 23.579 7.163   9.183   0.60 12.03 ?  53  LEU   A O    1 
ATOM   1357 O O    B LEU   A 1 53  ? 23.836 7.121   9.289   0.40 11.61 ?  53  LEU   A O    1 
ATOM   1358 C CB   A LEU   A 1 53  ? 22.843 4.416   7.419   0.60 11.37 ?  53  LEU   A CB   1 
ATOM   1359 C CB   B LEU   A 1 53  ? 23.143 4.355   7.529   0.40 9.93  ?  53  LEU   A CB   1 
ATOM   1360 C CG   A LEU   A 1 53  ? 21.974 3.154   7.482   0.60 11.75 ?  53  LEU   A CG   1 
ATOM   1361 C CG   B LEU   A 1 53  ? 22.387 3.029   7.644   0.40 10.25 ?  53  LEU   A CG   1 
ATOM   1362 C CD1  A LEU   A 1 53  ? 22.706 1.966   6.874   0.60 12.22 ?  53  LEU   A CD1  1 
ATOM   1363 C CD1  B LEU   A 1 53  ? 23.208 1.924   6.989   0.40 10.85 ?  53  LEU   A CD1  1 
ATOM   1364 C CD2  A LEU   A 1 53  ? 21.571 2.845   8.905   0.60 12.94 ?  53  LEU   A CD2  1 
ATOM   1365 C CD2  B LEU   A 1 53  ? 22.103 2.686   9.088   0.40 10.20 ?  53  LEU   A CD2  1 
ATOM   1366 H H    A LEU   A 1 53  ? 21.222 5.681   6.093   0.60 12.30 ?  53  LEU   A H    1 
ATOM   1367 H H    B LEU   A 1 53  ? 21.312 5.496   6.388   0.40 12.49 ?  53  LEU   A H    1 
ATOM   1368 H HA   A LEU   A 1 53  ? 21.727 5.627   8.649   0.60 12.96 ?  53  LEU   A HA   1 
ATOM   1369 H HA   B LEU   A 1 53  ? 22.054 5.453   8.876   0.40 12.34 ?  53  LEU   A HA   1 
ATOM   1370 H HB2  A LEU   A 1 53  ? 23.162 4.498   6.506   0.60 13.62 ?  53  LEU   A HB2  1 
ATOM   1371 H HB2  B LEU   A 1 53  ? 23.368 4.466   6.593   0.40 11.89 ?  53  LEU   A HB2  1 
ATOM   1372 H HB3  A LEU   A 1 53  ? 23.602 4.265   8.005   0.60 13.62 ?  53  LEU   A HB3  1 
ATOM   1373 H HB3  B LEU   A 1 53  ? 23.962 4.250   8.039   0.40 11.89 ?  53  LEU   A HB3  1 
ATOM   1374 H HG   A LEU   A 1 53  ? 21.169 3.305   6.961   0.60 14.08 ?  53  LEU   A HG   1 
ATOM   1375 H HG   B LEU   A 1 53  ? 21.544 3.092   7.169   0.40 12.28 ?  53  LEU   A HG   1 
ATOM   1376 H HD11 A LEU   A 1 53  ? 22.136 1.184   6.930   0.60 14.64 ?  53  LEU   A HD11 1 
ATOM   1377 H HD11 B LEU   A 1 53  ? 22.728 1.083   7.065   0.40 12.99 ?  53  LEU   A HD11 1 
ATOM   1378 H HD12 A LEU   A 1 53  ? 22.913 2.160   5.946   0.60 14.64 ?  53  LEU   A HD12 1 
ATOM   1379 H HD12 B LEU   A 1 53  ? 23.346 2.142   6.054   0.40 12.99 ?  53  LEU   A HD12 1 
ATOM   1380 H HD13 A LEU   A 1 53  ? 23.526 1.814   7.371   0.60 14.64 ?  53  LEU   A HD13 1 
ATOM   1381 H HD13 B LEU   A 1 53  ? 24.064 1.855   7.443   0.40 12.99 ?  53  LEU   A HD13 1 
ATOM   1382 H HD21 A LEU   A 1 53  ? 21.071 2.016   8.915   0.60 15.50 ?  53  LEU   A HD21 1 
ATOM   1383 H HD21 B LEU   A 1 53  ? 21.584 1.868   9.124   0.40 12.22 ?  53  LEU   A HD21 1 
ATOM   1384 H HD22 A LEU   A 1 53  ? 22.370 2.760   9.446   0.60 15.50 ?  53  LEU   A HD22 1 
ATOM   1385 H HD22 B LEU   A 1 53  ? 22.944 2.566   9.555   0.40 12.22 ?  53  LEU   A HD22 1 
ATOM   1386 H HD23 A LEU   A 1 53  ? 21.020 3.570   9.240   0.60 15.50 ?  53  LEU   A HD23 1 
ATOM   1387 H HD23 B LEU   A 1 53  ? 21.602 3.411   9.493   0.40 12.22 ?  53  LEU   A HD23 1 
ATOM   1388 N N    A ASN   A 1 54  ? 23.834 7.333   6.959   0.60 10.51 ?  54  ASN   A N    1 
ATOM   1389 N N    B ASN   A 1 54  ? 23.918 7.330   7.053   0.40 10.89 ?  54  ASN   A N    1 
ATOM   1390 C CA   A ASN   A 1 54  ? 24.894 8.318   7.113   0.60 10.42 ?  54  ASN   A CA   1 
ATOM   1391 C CA   B ASN   A 1 54  ? 24.948 8.361   7.141   0.40 11.00 ?  54  ASN   A CA   1 
ATOM   1392 C C    A ASN   A 1 54  ? 24.395 9.551   7.858   0.60 11.38 ?  54  ASN   A C    1 
ATOM   1393 C C    B ASN   A 1 54  ? 24.424 9.614   7.830   0.40 11.54 ?  54  ASN   A C    1 
ATOM   1394 O O    A ASN   A 1 54  ? 25.079 10.069  8.748   0.60 11.72 ?  54  ASN   A O    1 
ATOM   1395 O O    B ASN   A 1 54  ? 25.128 10.215  8.650   0.40 11.85 ?  54  ASN   A O    1 
ATOM   1396 C CB   A ASN   A 1 54  ? 25.447 8.704   5.756   0.60 10.29 ?  54  ASN   A CB   1 
ATOM   1397 C CB   B ASN   A 1 54  ? 25.500 8.696   5.761   0.40 11.21 ?  54  ASN   A CB   1 
ATOM   1398 C CG   A ASN   A 1 54  ? 26.501 9.765   5.871   0.60 10.33 ?  54  ASN   A CG   1 
ATOM   1399 C CG   B ASN   A 1 54  ? 26.470 9.858   5.807   0.40 11.41 ?  54  ASN   A CG   1 
ATOM   1400 O OD1  A ASN   A 1 54  ? 27.449 9.629   6.657   0.60 9.44  ?  54  ASN   A OD1  1 
ATOM   1401 O OD1  B ASN   A 1 54  ? 27.583 9.718   6.315   0.40 12.65 ?  54  ASN   A OD1  1 
ATOM   1402 N ND2  A ASN   A 1 54  ? 26.332 10.849  5.129   0.60 11.39 ?  54  ASN   A ND2  1 
ATOM   1403 N ND2  B ASN   A 1 54  ? 26.052 11.014  5.295   0.40 10.63 ?  54  ASN   A ND2  1 
ATOM   1404 H H    A ASN   A 1 54  ? 23.619 7.148   6.146   0.60 12.59 ?  54  ASN   A H    1 
ATOM   1405 H H    B ASN   A 1 54  ? 23.652 7.141   6.258   0.40 13.05 ?  54  ASN   A H    1 
ATOM   1406 H HA   A ASN   A 1 54  ? 25.613 7.926   7.630   0.60 12.49 ?  54  ASN   A HA   1 
ATOM   1407 H HA   B ASN   A 1 54  ? 25.674 8.021   7.680   0.40 13.17 ?  54  ASN   A HA   1 
ATOM   1408 H HB2  A ASN   A 1 54  ? 25.836 7.914   5.337   0.60 12.32 ?  54  ASN   A HB2  1 
ATOM   1409 H HB2  B ASN   A 1 54  ? 25.974 7.920   5.417   0.40 13.42 ?  54  ASN   A HB2  1 
ATOM   1410 H HB3  A ASN   A 1 54  ? 24.726 9.046   5.202   0.60 12.32 ?  54  ASN   A HB3  1 
ATOM   1411 H HB3  B ASN   A 1 54  ? 24.770 8.931   5.172   0.40 13.42 ?  54  ASN   A HB3  1 
ATOM   1412 H HD21 A ASN   A 1 54  ? 26.911 11.480  5.164   0.60 13.64 ?  54  ASN   A HD21 1 
ATOM   1413 H HD21 B ASN   A 1 54  ? 26.571 11.702  5.304   0.40 12.74 ?  54  ASN   A HD21 1 
ATOM   1414 H HD22 A ASN   A 1 54  ? 25.656 10.906  4.605   0.60 13.64 ?  54  ASN   A HD22 1 
ATOM   1415 H HD22 B ASN   A 1 54  ? 25.270 11.071  4.946   0.40 12.74 ?  54  ASN   A HD22 1 
ATOM   1416 N N    . LYS   A 1 55  ? 23.193 10.027  7.511   1.00 11.87 ?  55  LYS   A N    1 
ATOM   1417 C CA   . LYS   A 1 55  ? 22.611 11.179  8.188   1.00 12.57 ?  55  LYS   A CA   1 
ATOM   1418 C C    . LYS   A 1 55  ? 22.525 10.935  9.688   1.00 12.54 ?  55  LYS   A C    1 
ATOM   1419 O O    . LYS   A 1 55  ? 22.810 11.832  10.491  1.00 13.40 ?  55  LYS   A O    1 
ATOM   1420 C CB   . LYS   A 1 55  ? 21.240 11.490  7.581   1.00 13.55 ?  55  LYS   A CB   1 
ATOM   1421 C CG   . LYS   A 1 55  ? 20.488 12.637  8.222   1.00 15.45 ?  55  LYS   A CG   1 
ATOM   1422 C CD   . LYS   A 1 55  ? 19.183 12.919  7.453   1.00 16.66 ?  55  LYS   A CD   1 
ATOM   1423 C CE   . LYS   A 1 55  ? 18.348 14.015  8.099   1.00 18.10 ?  55  LYS   A CE   1 
ATOM   1424 N NZ   . LYS   A 1 55  ? 17.033 14.208  7.407   1.00 19.08 ?  55  LYS   A NZ   1 
ATOM   1425 H H    A LYS   A 1 55  ? 22.694 9.695   6.890   0.60 14.22 ?  55  LYS   A H    1 
ATOM   1426 H H    B LYS   A 1 55  ? 22.680 9.657   6.924   0.40 14.22 ?  55  LYS   A H    1 
ATOM   1427 H HA   . LYS   A 1 55  ? 23.179 11.948  8.046   1.00 15.06 ?  55  LYS   A HA   1 
ATOM   1428 H HB2  . LYS   A 1 55  ? 21.361 11.717  6.645   1.00 16.24 ?  55  LYS   A HB2  1 
ATOM   1429 H HB3  . LYS   A 1 55  ? 20.679 10.702  7.652   1.00 16.24 ?  55  LYS   A HB3  1 
ATOM   1430 H HG2  . LYS   A 1 55  ? 20.255 12.400  9.136   1.00 18.51 ?  55  LYS   A HG2  1 
ATOM   1431 H HG3  . LYS   A 1 55  ? 21.033 13.435  8.206   1.00 18.51 ?  55  LYS   A HG3  1 
ATOM   1432 H HD2  . LYS   A 1 55  ? 19.405 13.201  6.552   1.00 19.97 ?  55  LYS   A HD2  1 
ATOM   1433 H HD3  . LYS   A 1 55  ? 18.650 12.109  7.426   1.00 19.97 ?  55  LYS   A HD3  1 
ATOM   1434 H HE2  . LYS   A 1 55  ? 18.170 13.775  9.023   1.00 21.70 ?  55  LYS   A HE2  1 
ATOM   1435 H HE3  . LYS   A 1 55  ? 18.836 14.851  8.060   1.00 21.70 ?  55  LYS   A HE3  1 
ATOM   1436 H HZ1  . LYS   A 1 55  ? 16.457 14.608  7.956   1.00 22.88 ?  55  LYS   A HZ1  1 
ATOM   1437 H HZ2  . LYS   A 1 55  ? 17.140 14.716  6.685   1.00 22.88 ?  55  LYS   A HZ2  1 
ATOM   1438 H HZ3  . LYS   A 1 55  ? 16.697 13.420  7.163   1.00 22.88 ?  55  LYS   A HZ3  1 
ATOM   1439 N N    . ALA   A 1 56  ? 22.148 9.716   10.086  1.00 13.20 ?  56  ALA   A N    1 
ATOM   1440 C CA   . ALA   A 1 56  ? 22.040 9.382   11.500  1.00 14.07 ?  56  ALA   A CA   1 
ATOM   1441 C C    . ALA   A 1 56  ? 23.387 9.407   12.215  1.00 13.58 ?  56  ALA   A C    1 
ATOM   1442 O O    . ALA   A 1 56  ? 23.416 9.588   13.435  1.00 15.14 ?  56  ALA   A O    1 
ATOM   1443 C CB   . ALA   A 1 56  ? 21.352 8.021   11.669  1.00 14.61 ?  56  ALA   A CB   1 
ATOM   1444 H H    . ALA   A 1 56  ? 21.946 9.072   9.552   1.00 15.82 ?  56  ALA   A H    1 
ATOM   1445 H HA   . ALA   A 1 56  ? 21.478 10.040  11.927  1.00 16.86 ?  56  ALA   A HA   1 
ATOM   1446 H HB1  . ALA   A 1 56  ? 21.290 7.812   12.615  1.00 17.50 ?  56  ALA   A HB1  1 
ATOM   1447 H HB2  . ALA   A 1 56  ? 20.460 8.069   11.285  1.00 17.50 ?  56  ALA   A HB2  1 
ATOM   1448 H HB3  . ALA   A 1 56  ? 21.869 7.340   11.213  1.00 17.50 ?  56  ALA   A HB3  1 
ATOM   1449 N N    . THR   A 1 57  ? 24.496 9.234   11.489  1.00 12.53 ?  57  THR   A N    1 
ATOM   1450 C CA   . THR   A 1 57  ? 25.837 9.364   12.062  1.00 12.53 ?  57  THR   A CA   1 
ATOM   1451 C C    . THR   A 1 57  ? 26.383 10.784  11.984  1.00 13.04 ?  57  THR   A C    1 
ATOM   1452 O O    . THR   A 1 57  ? 27.566 10.997  12.272  1.00 13.52 ?  57  THR   A O    1 
ATOM   1453 C CB   . THR   A 1 57  ? 26.848 8.418   11.388  1.00 12.55 ?  57  THR   A CB   1 
ATOM   1454 O OG1  . THR   A 1 57  ? 27.221 8.925   10.096  1.00 12.33 ?  57  THR   A OG1  1 
ATOM   1455 C CG2  . THR   A 1 57  ? 26.310 7.004   11.273  1.00 12.76 ?  57  THR   A CG2  1 
ATOM   1456 H H    . THR   A 1 57  ? 24.495 9.025   10.649  1.00 15.01 ?  57  THR   A H    1 
ATOM   1457 H HA   . THR   A 1 57  ? 25.791 9.108   12.998  1.00 15.01 ?  57  THR   A HA   1 
ATOM   1458 H HB   . THR   A 1 57  ? 27.644 8.369   11.945  1.00 15.03 ?  57  THR   A HB   1 
ATOM   1459 H HG1  . THR   A 1 57  ? 26.546 8.987   9.608   1.00 14.78 ?  57  THR   A HG1  1 
ATOM   1460 H HG21 . THR   A 1 57  ? 26.899 6.466   10.719  1.00 15.29 ?  57  THR   A HG21 1 
ATOM   1461 H HG22 . THR   A 1 57  ? 26.253 6.596   12.153  1.00 15.29 ?  57  THR   A HG22 1 
ATOM   1462 H HG23 . THR   A 1 57  ? 25.428 7.007   10.876  1.00 15.29 ?  57  THR   A HG23 1 
ATOM   1463 N N    . ASN   A 1 58  ? 25.561 11.753  11.589  1.00 13.80 ?  58  ASN   A N    1 
ATOM   1464 C CA   . ASN   A 1 58  ? 26.013 13.136  11.492  1.00 14.74 ?  58  ASN   A CA   1 
ATOM   1465 C C    . ASN   A 1 58  ? 27.155 13.275  10.481  1.00 13.16 ?  58  ASN   A C    1 
ATOM   1466 O O    . ASN   A 1 58  ? 28.046 14.114  10.640  1.00 13.85 ?  58  ASN   A O    1 
ATOM   1467 C CB   . ASN   A 1 58  ? 26.394 13.671  12.886  1.00 17.35 ?  58  ASN   A CB   1 
ATOM   1468 C CG   . ASN   A 1 58  ? 26.795 15.129  12.885  1.00 20.93 ?  58  ASN   A CG   1 
ATOM   1469 O OD1  . ASN   A 1 58  ? 26.159 15.952  12.236  1.00 22.55 ?  58  ASN   A OD1  1 
ATOM   1470 N ND2  . ASN   A 1 58  ? 27.851 15.459  13.634  1.00 22.18 ?  58  ASN   A ND2  1 
ATOM   1471 H H    . ASN   A 1 58  ? 24.739 11.623  11.360  1.00 16.54 ?  58  ASN   A H    1 
ATOM   1472 H HA   . ASN   A 1 58  ? 25.268 13.665  11.169  1.00 17.66 ?  58  ASN   A HA   1 
ATOM   1473 H HB2  . ASN   A 1 58  ? 25.627 13.572  13.478  1.00 20.79 ?  58  ASN   A HB2  1 
ATOM   1474 H HB3  . ASN   A 1 58  ? 27.139 13.160  13.229  1.00 20.79 ?  58  ASN   A HB3  1 
ATOM   1475 H HD21 . ASN   A 1 58  ? 28.117 16.276  13.672  1.00 26.60 ?  58  ASN   A HD21 1 
ATOM   1476 H HD22 . ASN   A 1 58  ? 28.264 14.851  14.079  1.00 26.60 ?  58  ASN   A HD22 1 
ATOM   1477 N N    . ASN   A 1 59  ? 27.131 12.462  9.424   1.00 12.23 ?  59  ASN   A N    1 
ATOM   1478 C CA   . ASN   A 1 59  ? 28.099 12.442  8.325   1.00 12.03 ?  59  ASN   A CA   1 
ATOM   1479 C C    . ASN   A 1 59  ? 29.417 11.760  8.701   1.00 11.54 ?  59  ASN   A C    1 
ATOM   1480 O O    . ASN   A 1 59  ? 30.329 11.723  7.869   1.00 11.57 ?  59  ASN   A O    1 
ATOM   1481 C CB   . ASN   A 1 59  ? 28.380 13.830  7.722   1.00 12.25 ?  59  ASN   A CB   1 
ATOM   1482 C CG   . ASN   A 1 59  ? 28.730 13.771  6.252   1.00 12.48 ?  59  ASN   A CG   1 
ATOM   1483 O OD1  . ASN   A 1 59  ? 28.030 13.144  5.461   1.00 12.98 ?  59  ASN   A OD1  1 
ATOM   1484 N ND2  . ASN   A 1 59  ? 29.810 14.434  5.870   1.00 13.09 ?  59  ASN   A ND2  1 
ATOM   1485 H H    . ASN   A 1 59  ? 26.515 11.873  9.309   1.00 14.65 ?  59  ASN   A H    1 
ATOM   1486 H HA   . ASN   A 1 59  ? 27.715 11.911  7.611   1.00 14.41 ?  59  ASN   A HA   1 
ATOM   1487 H HB2  . ASN   A 1 59  ? 27.591 14.386  7.811   1.00 14.68 ?  59  ASN   A HB2  1 
ATOM   1488 H HB3  . ASN   A 1 59  ? 29.129 14.238  8.181   1.00 14.68 ?  59  ASN   A HB3  1 
ATOM   1489 H HD21 . ASN   A 1 59  ? 30.050 14.433  5.040   1.00 15.69 ?  59  ASN   A HD21 1 
ATOM   1490 H HD22 . ASN   A 1 59  ? 30.282 14.866  6.446   1.00 15.69 ?  59  ASN   A HD22 1 
ATOM   1491 N N    . ALA   A 1 60  ? 29.558 11.224  9.911   1.00 11.48 ?  60  ALA   A N    1 
ATOM   1492 C CA   . ALA   A 1 60  ? 30.800 10.535  10.255  1.00 11.69 ?  60  ALA   A CA   1 
ATOM   1493 C C    . ALA   A 1 60  ? 31.022 9.306   9.381   1.00 11.87 ?  60  ALA   A C    1 
ATOM   1494 O O    . ALA   A 1 60  ? 32.164 8.983   9.037   1.00 12.25 ?  60  ALA   A O    1 
ATOM   1495 C CB   . ALA   A 1 60  ? 30.811 10.155  11.733  1.00 12.20 ?  60  ALA   A CB   1 
ATOM   1496 H H    . ALA   A 1 60  ? 28.967 11.241  10.533  1.00 13.75 ?  60  ALA   A H    1 
ATOM   1497 H HA   . ALA   A 1 60  ? 31.545 11.141  10.100  1.00 14.01 ?  60  ALA   A HA   1 
ATOM   1498 H HB1  . ALA   A 1 60  ? 31.644 9.704   11.938  1.00 14.62 ?  60  ALA   A HB1  1 
ATOM   1499 H HB2  . ALA   A 1 60  ? 30.734 10.964  12.267  1.00 14.62 ?  60  ALA   A HB2  1 
ATOM   1500 H HB3  . ALA   A 1 60  ? 30.061 9.569   11.913  1.00 14.62 ?  60  ALA   A HB3  1 
ATOM   1501 N N    . MET   A 1 61  ? 29.949 8.605   9.014   1.00 11.23 ?  61  MET   A N    1 
ATOM   1502 C CA   . MET   A 1 61  ? 30.087 7.471   8.104   1.00 11.36 ?  61  MET   A CA   1 
ATOM   1503 C C    . MET   A 1 61  ? 30.707 7.905   6.778   1.00 11.25 ?  61  MET   A C    1 
ATOM   1504 O O    . MET   A 1 61  ? 31.594 7.225   6.246   1.00 11.49 ?  61  MET   A O    1 
ATOM   1505 C CB   . MET   A 1 61  ? 28.726 6.811   7.897   1.00 11.40 ?  61  MET   A CB   1 
ATOM   1506 C CG   . MET   A 1 61  ? 28.730 5.641   6.921   1.00 11.86 ?  61  MET   A CG   1 
ATOM   1507 S SD   . MET   A 1 61  ? 27.116 4.888   6.732   1.00 12.40 ?  61  MET   A SD   1 
ATOM   1508 C CE   . MET   A 1 61  ? 26.985 4.004   8.285   1.00 13.75 ?  61  MET   A CE   1 
ATOM   1509 H H    . MET   A 1 61  ? 29.141 8.769   9.265   1.00 13.45 ?  61  MET   A H    1 
ATOM   1510 H HA   . MET   A 1 61  ? 30.671 6.820   8.516   1.00 13.60 ?  61  MET   A HA   1 
ATOM   1511 H HB2  . MET   A 1 61  ? 28.414 6.478   8.750   1.00 13.65 ?  61  MET   A HB2  1 
ATOM   1512 H HB3  . MET   A 1 61  ? 28.107 7.474   7.557   1.00 13.65 ?  61  MET   A HB3  1 
ATOM   1513 H HG2  . MET   A 1 61  ? 29.011 5.956   6.046   1.00 14.20 ?  61  MET   A HG2  1 
ATOM   1514 H HG3  . MET   A 1 61  ? 29.340 4.962   7.241   1.00 14.20 ?  61  MET   A HG3  1 
ATOM   1515 H HE1  . MET   A 1 61  ? 26.153 3.501   8.294   1.00 16.48 ?  61  MET   A HE1  1 
ATOM   1516 H HE2  . MET   A 1 61  ? 27.737 3.398   8.367   1.00 16.48 ?  61  MET   A HE2  1 
ATOM   1517 H HE3  . MET   A 1 61  ? 26.991 4.643   9.014   1.00 16.48 ?  61  MET   A HE3  1 
ATOM   1518 N N    . GLN   A 1 62  ? 30.257 9.038   6.229   1.00 11.22 ?  62  GLN   A N    1 
ATOM   1519 C CA   . GLN   A 1 62  ? 30.810 9.509   4.962   1.00 11.32 ?  62  GLN   A CA   1 
ATOM   1520 C C    . GLN   A 1 62  ? 32.279 9.885   5.097   1.00 11.42 ?  62  GLN   A C    1 
ATOM   1521 O O    . GLN   A 1 62  ? 33.081 9.578   4.210   1.00 11.65 ?  62  GLN   A O    1 
ATOM   1522 C CB   . GLN   A 1 62  ? 30.013 10.700  4.434   1.00 11.37 ?  62  GLN   A CB   1 
ATOM   1523 C CG   . GLN   A 1 62  ? 30.368 11.057  3.006   1.00 11.11 ?  62  GLN   A CG   1 
ATOM   1524 C CD   . GLN   A 1 62  ? 30.028 9.926   2.063   1.00 11.45 ?  62  GLN   A CD   1 
ATOM   1525 O OE1  . GLN   A 1 62  ? 28.848 9.619   1.859   1.00 11.93 ?  62  GLN   A OE1  1 
ATOM   1526 N NE2  . GLN   A 1 62  ? 31.046 9.257   1.524   1.00 12.14 ?  62  GLN   A NE2  1 
ATOM   1527 H H    . GLN   A 1 62  ? 29.648 9.540   6.565   1.00 13.44 ?  62  GLN   A H    1 
ATOM   1528 H HA   . GLN   A 1 62  ? 30.747 8.791   4.310   1.00 13.56 ?  62  GLN   A HA   1 
ATOM   1529 H HB2  . GLN   A 1 62  ? 29.068 10.489  4.465   1.00 13.62 ?  62  GLN   A HB2  1 
ATOM   1530 H HB3  . GLN   A 1 62  ? 30.200 11.475  4.988   1.00 13.62 ?  62  GLN   A HB3  1 
ATOM   1531 H HG2  . GLN   A 1 62  ? 29.858 11.834  2.735   1.00 13.31 ?  62  GLN   A HG2  1 
ATOM   1532 H HG3  . GLN   A 1 62  ? 31.316 11.231  2.940   1.00 13.31 ?  62  GLN   A HG3  1 
ATOM   1533 H HE21 . GLN   A 1 62  ? 31.855 9.491   1.699   1.00 14.54 ?  62  GLN   A HE21 1 
ATOM   1534 H HE22 . GLN   A 1 62  ? 30.898 8.600   0.986   1.00 14.54 ?  62  GLN   A HE22 1 
ATOM   1535 N N    . VAL   A 1 63  ? 32.643 10.574  6.180   1.00 11.79 ?  63  VAL   A N    1 
ATOM   1536 C CA   . VAL   A 1 63  ? 34.034 10.969  6.390   1.00 12.42 ?  63  VAL   A CA   1 
ATOM   1537 C C    . VAL   A 1 63  ? 34.934 9.737   6.441   1.00 11.60 ?  63  VAL   A C    1 
ATOM   1538 O O    . VAL   A 1 63  ? 35.980 9.676   5.779   1.00 11.87 ?  63  VAL   A O    1 
ATOM   1539 C CB   . VAL   A 1 63  ? 34.146 11.830  7.660   1.00 14.05 ?  63  VAL   A CB   1 
ATOM   1540 C CG1  . VAL   A 1 63  ? 35.599 12.067  8.014   1.00 15.67 ?  63  VAL   A CG1  1 
ATOM   1541 C CG2  . VAL   A 1 63  ? 33.410 13.156  7.466   1.00 14.29 ?  63  VAL   A CG2  1 
ATOM   1542 H H    . VAL   A 1 63  ? 32.100 10.819  6.803   1.00 14.13 ?  63  VAL   A H    1 
ATOM   1543 H HA   . VAL   A 1 63  ? 34.315 11.512  5.640   1.00 14.88 ?  63  VAL   A HA   1 
ATOM   1544 H HB   . VAL   A 1 63  ? 33.725 11.362  8.400   1.00 16.84 ?  63  VAL   A HB   1 
ATOM   1545 H HG11 . VAL   A 1 63  ? 35.652 12.807  8.638   1.00 18.78 ?  63  VAL   A HG11 1 
ATOM   1546 H HG12 . VAL   A 1 63  ? 35.960 11.265  8.420   1.00 18.78 ?  63  VAL   A HG12 1 
ATOM   1547 H HG13 . VAL   A 1 63  ? 36.087 12.282  7.204   1.00 18.78 ?  63  VAL   A HG13 1 
ATOM   1548 H HG21 . VAL   A 1 63  ? 33.502 13.689  8.273   1.00 17.12 ?  63  VAL   A HG21 1 
ATOM   1549 H HG22 . VAL   A 1 63  ? 33.802 13.628  6.714   1.00 17.12 ?  63  VAL   A HG22 1 
ATOM   1550 H HG23 . VAL   A 1 63  ? 32.473 12.979  7.294   1.00 17.12 ?  63  VAL   A HG23 1 
ATOM   1551 N N    . GLU   A 1 64  ? 34.523 8.725   7.210   1.00 12.01 ?  64  GLU   A N    1 
ATOM   1552 C CA   . GLU   A 1 64  ? 35.291 7.491   7.298   1.00 11.63 ?  64  GLU   A CA   1 
ATOM   1553 C C    . GLU   A 1 64  ? 35.370 6.805   5.941   1.00 11.30 ?  64  GLU   A C    1 
ATOM   1554 O O    . GLU   A 1 64  ? 36.422 6.264   5.555   1.00 11.68 ?  64  GLU   A O    1 
ATOM   1555 C CB   . GLU   A 1 64  ? 34.616 6.577   8.319   1.00 12.39 ?  64  GLU   A CB   1 
ATOM   1556 C CG   . GLU   A 1 64  ? 35.270 5.225   8.457   1.00 12.82 ?  64  GLU   A CG   1 
ATOM   1557 C CD   . GLU   A 1 64  ? 34.391 4.223   9.181   1.00 13.60 ?  64  GLU   A CD   1 
ATOM   1558 O OE1  . GLU   A 1 64  ? 33.155 4.305   9.043   1.00 13.88 ?  64  GLU   A OE1  1 
ATOM   1559 O OE2  . GLU   A 1 64  ? 34.934 3.326   9.866   1.00 13.60 -1 64  GLU   A OE2  1 
ATOM   1560 H H    . GLU   A 1 64  ? 33.800 8.723   7.677   1.00 14.39 ?  64  GLU   A H    1 
ATOM   1561 H HA   . GLU   A 1 64  ? 36.194 7.693   7.605   1.00 13.94 ?  64  GLU   A HA   1 
ATOM   1562 H HB2  . GLU   A 1 64  ? 34.650 7.015   9.192   1.00 14.84 ?  64  GLU   A HB2  1 
ATOM   1563 H HB3  . GLU   A 1 64  ? 33.697 6.450   8.056   1.00 14.84 ?  64  GLU   A HB3  1 
ATOM   1564 H HG2  . GLU   A 1 64  ? 35.470 4.867   7.577   1.00 15.37 ?  64  GLU   A HG2  1 
ATOM   1565 H HG3  . GLU   A 1 64  ? 36.091 5.322   8.964   1.00 15.37 ?  64  GLU   A HG3  1 
ATOM   1566 N N    . SER   A 1 65  ? 34.250 6.799   5.216   1.00 11.40 ?  65  SER   A N    1 
ATOM   1567 C CA   . SER   A 1 65  ? 34.191 6.144   3.918   1.00 10.93 ?  65  SER   A CA   1 
ATOM   1568 C C    . SER   A 1 65  ? 35.101 6.815   2.907   1.00 11.15 ?  65  SER   A C    1 
ATOM   1569 O O    . SER   A 1 65  ? 35.736 6.140   2.092   1.00 11.98 ?  65  SER   A O    1 
ATOM   1570 C CB   . SER   A 1 65  ? 32.755 6.152   3.391   1.00 11.18 ?  65  SER   A CB   1 
ATOM   1571 O OG   . SER   A 1 65  ? 31.906 5.328   4.179   1.00 11.76 ?  65  SER   A OG   1 
ATOM   1572 H H    . SER   A 1 65  ? 33.514 7.166   5.464   1.00 13.66 ?  65  SER   A H    1 
ATOM   1573 H HA   . SER   A 1 65  ? 34.477 5.224   4.010   1.00 13.09 ?  65  SER   A HA   1 
ATOM   1574 H HB2  . SER   A 1 65  ? 32.419 7.062   3.414   1.00 13.39 ?  65  SER   A HB2  1 
ATOM   1575 H HB3  . SER   A 1 65  ? 32.760 5.826   2.479   1.00 13.39 ?  65  SER   A HB3  1 
ATOM   1576 H HG   . SER   A 1 65  ? 31.896 5.600   4.976   1.00 14.09 ?  65  SER   A HG   1 
ATOM   1577 N N    . ASP   A 1 66  ? 35.172 8.147   2.930   1.00 11.43 ?  66  ASP   A N    1 
ATOM   1578 C CA   . ASP   A 1 66  ? 36.022 8.847   1.976   1.00 12.65 ?  66  ASP   A CA   1 
ATOM   1579 C C    . ASP   A 1 66  ? 37.487 8.499   2.200   1.00 12.33 ?  66  ASP   A C    1 
ATOM   1580 O O    . ASP   A 1 66  ? 38.254 8.336   1.241   1.00 13.48 ?  66  ASP   A O    1 
ATOM   1581 C CB   . ASP   A 1 66  ? 35.801 10.356  2.093   1.00 13.85 ?  66  ASP   A CB   1 
ATOM   1582 C CG   . ASP   A 1 66  ? 34.467 10.821  1.493   1.00 15.25 ?  66  ASP   A CG   1 
ATOM   1583 O OD1  . ASP   A 1 66  ? 33.749 10.028  0.840   1.00 15.32 ?  66  ASP   A OD1  1 
ATOM   1584 O OD2  . ASP   A 1 66  ? 34.168 12.017  1.660   1.00 18.18 -1 66  ASP   A OD2  1 
ATOM   1585 H H    . ASP   A 1 66  ? 34.739 8.664   3.473   1.00 13.69 ?  66  ASP   A H    1 
ATOM   1586 H HA   . ASP   A 1 66  ? 35.779 8.578   1.077   1.00 15.16 ?  66  ASP   A HA   1 
ATOM   1587 H HB2  . ASP   A 1 66  ? 35.814 10.605  3.031   1.00 16.60 ?  66  ASP   A HB2  1 
ATOM   1588 H HB3  . ASP   A 1 66  ? 36.517 10.815  1.622   1.00 16.60 ?  66  ASP   A HB3  1 
ATOM   1589 N N    . ASP   A 1 67  ? 37.893 8.369   3.463   1.00 12.69 ?  67  ASP   A N    1 
ATOM   1590 C CA   . ASP   A 1 67  ? 39.247 7.918   3.752   1.00 13.31 ?  67  ASP   A CA   1 
ATOM   1591 C C    . ASP   A 1 67  ? 39.465 6.486   3.271   1.00 13.14 ?  67  ASP   A C    1 
ATOM   1592 O O    . ASP   A 1 67  ? 40.519 6.167   2.710   1.00 14.12 ?  67  ASP   A O    1 
ATOM   1593 C CB   . ASP   A 1 67  ? 39.528 8.051   5.245   1.00 14.72 ?  67  ASP   A CB   1 
ATOM   1594 C CG   . ASP   A 1 67  ? 40.827 7.389   5.651   1.00 15.63 ?  67  ASP   A CG   1 
ATOM   1595 O OD1  . ASP   A 1 67  ? 41.898 8.016   5.485   1.00 18.47 ?  67  ASP   A OD1  1 
ATOM   1596 O OD2  . ASP   A 1 67  ? 40.781 6.228   6.121   1.00 15.42 -1 67  ASP   A OD2  1 
ATOM   1597 H H    . ASP   A 1 67  ? 37.414 8.540   4.152   1.00 15.20 ?  67  ASP   A H    1 
ATOM   1598 H HA   . ASP   A 1 67  ? 39.875 8.487   3.279   1.00 15.95 ?  67  ASP   A HA   1 
ATOM   1599 H HB2  . ASP   A 1 67  ? 39.585 8.990   5.469   1.00 17.64 ?  67  ASP   A HB2  1 
ATOM   1600 H HB3  . ASP   A 1 67  ? 38.804 7.631   5.737   1.00 17.64 ?  67  ASP   A HB3  1 
ATOM   1601 N N    A TYR   A 1 68  ? 38.473 5.614   3.458   0.60 12.44 ?  68  TYR   A N    1 
ATOM   1602 N N    B TYR   A 1 68  ? 38.480 5.600   3.487   0.40 12.53 ?  68  TYR   A N    1 
ATOM   1603 C CA   A TYR   A 1 68  ? 38.611 4.235   3.001   0.60 12.80 ?  68  TYR   A CA   1 
ATOM   1604 C CA   B TYR   A 1 68  ? 38.592 4.226   2.989   0.40 12.59 ?  68  TYR   A CA   1 
ATOM   1605 C C    A TYR   A 1 68  ? 38.820 4.169   1.489   0.60 12.70 ?  68  TYR   A C    1 
ATOM   1606 C C    B TYR   A 1 68  ? 38.858 4.211   1.489   0.40 12.41 ?  68  TYR   A C    1 
ATOM   1607 O O    A TYR   A 1 68  ? 39.667 3.407   1.005   0.60 13.06 ?  68  TYR   A O    1 
ATOM   1608 O O    B TYR   A 1 68  ? 39.770 3.525   1.012   0.40 12.54 ?  68  TYR   A O    1 
ATOM   1609 C CB   A TYR   A 1 68  ? 37.390 3.405   3.422   0.60 13.09 ?  68  TYR   A CB   1 
ATOM   1610 C CB   B TYR   A 1 68  ? 37.326 3.405   3.306   0.40 12.72 ?  68  TYR   A CB   1 
ATOM   1611 C CG   A TYR   A 1 68  ? 37.460 2.003   2.873   0.60 14.08 ?  68  TYR   A CG   1 
ATOM   1612 C CG   B TYR   A 1 68  ? 37.325 2.052   2.593   0.40 13.16 ?  68  TYR   A CG   1 
ATOM   1613 C CD1  A TYR   A 1 68  ? 37.001 1.725   1.595   0.60 15.33 ?  68  TYR   A CD1  1 
ATOM   1614 C CD1  B TYR   A 1 68  ? 36.842 1.929   1.289   0.40 13.37 ?  68  TYR   A CD1  1 
ATOM   1615 C CD2  A TYR   A 1 68  ? 38.048 0.977   3.598   0.60 15.44 ?  68  TYR   A CD2  1 
ATOM   1616 C CD2  B TYR   A 1 68  ? 37.846 0.915   3.204   0.40 13.46 ?  68  TYR   A CD2  1 
ATOM   1617 C CE1  A TYR   A 1 68  ? 37.105 0.471   1.058   0.60 16.51 ?  68  TYR   A CE1  1 
ATOM   1618 C CE1  B TYR   A 1 68  ? 36.875 0.714   0.623   0.40 13.00 ?  68  TYR   A CE1  1 
ATOM   1619 C CE2  A TYR   A 1 68  ? 38.152 -0.298  3.063   0.60 16.11 ?  68  TYR   A CE2  1 
ATOM   1620 C CE2  B TYR   A 1 68  ? 37.876 -0.307  2.545   0.40 12.80 ?  68  TYR   A CE2  1 
ATOM   1621 C CZ   A TYR   A 1 68  ? 37.680 -0.532  1.793   0.60 16.72 ?  68  TYR   A CZ   1 
ATOM   1622 C CZ   B TYR   A 1 68  ? 37.396 -0.395  1.260   0.40 12.56 ?  68  TYR   A CZ   1 
ATOM   1623 O OH   A TYR   A 1 68  ? 37.786 -1.777  1.233   0.60 18.70 ?  68  TYR   A OH   1 
ATOM   1624 O OH   B TYR   A 1 68  ? 37.446 -1.612  0.624   0.40 12.84 ?  68  TYR   A OH   1 
ATOM   1625 H H    A TYR   A 1 68  ? 37.719 5.795   3.834   0.60 14.90 ?  68  TYR   A H    1 
ATOM   1626 H H    B TYR   A 1 68  ? 37.749 5.769   3.914   0.40 15.01 ?  68  TYR   A H    1 
ATOM   1627 H HA   A TYR   A 1 68  ? 39.391 3.846   3.419   0.60 15.33 ?  68  TYR   A HA   1 
ATOM   1628 H HA   B TYR   A 1 68  ? 39.337 3.795   3.429   0.40 15.09 ?  68  TYR   A HA   1 
ATOM   1629 H HB2  A TYR   A 1 68  ? 37.362 3.353   4.390   0.60 15.68 ?  68  TYR   A HB2  1 
ATOM   1630 H HB2  B TYR   A 1 68  ? 37.281 3.240   4.262   0.40 15.24 ?  68  TYR   A HB2  1 
ATOM   1631 H HB3  A TYR   A 1 68  ? 36.584 3.826   3.083   0.60 15.68 ?  68  TYR   A HB3  1 
ATOM   1632 H HB3  B TYR   A 1 68  ? 36.541 3.899   3.018   0.40 15.24 ?  68  TYR   A HB3  1 
ATOM   1633 H HD1  A TYR   A 1 68  ? 36.621 2.408   1.088   0.60 18.37 ?  68  TYR   A HD1  1 
ATOM   1634 H HD1  B TYR   A 1 68  ? 36.495 2.674   0.853   0.40 16.02 ?  68  TYR   A HD1  1 
ATOM   1635 H HD2  A TYR   A 1 68  ? 38.387 1.148   4.447   0.60 18.51 ?  68  TYR   A HD2  1 
ATOM   1636 H HD2  B TYR   A 1 68  ? 38.181 0.974   4.067   0.40 16.13 ?  68  TYR   A HD2  1 
ATOM   1637 H HE1  A TYR   A 1 68  ? 36.787 0.305   0.201   0.60 19.79 ?  68  TYR   A HE1  1 
ATOM   1638 H HE1  B TYR   A 1 68  ? 36.546 0.641   -0.248  0.40 15.58 ?  68  TYR   A HE1  1 
ATOM   1639 H HE2  A TYR   A 1 68  ? 38.554 -0.983  3.548   0.60 19.31 ?  68  TYR   A HE2  1 
ATOM   1640 H HE2  B TYR   A 1 68  ? 38.230 -1.063  2.961   0.40 15.34 ?  68  TYR   A HE2  1 
ATOM   1641 H HH   A TYR   A 1 68  ? 38.146 -2.307  1.771   0.60 22.42 ?  68  TYR   A HH   1 
ATOM   1642 H HH   B TYR   A 1 68  ? 37.213 -1.527  -0.186  0.40 15.38 ?  68  TYR   A HH   1 
ATOM   1643 N N    . ILE   A 1 69  ? 38.051 4.951   0.725   1.00 11.91 ?  69  ILE   A N    1 
ATOM   1644 C CA   . ILE   A 1 69  ? 38.177 4.935   -0.730  1.00 12.07 ?  69  ILE   A CA   1 
ATOM   1645 C C    . ILE   A 1 69  ? 39.505 5.545   -1.164  1.00 12.21 ?  69  ILE   A C    1 
ATOM   1646 O O    . ILE   A 1 69  ? 40.146 5.071   -2.107  1.00 12.52 ?  69  ILE   A O    1 
ATOM   1647 C CB   . ILE   A 1 69  ? 36.977 5.651   -1.386  1.00 13.28 ?  69  ILE   A CB   1 
ATOM   1648 C CG1  . ILE   A 1 69  ? 35.664 4.908   -1.118  1.00 13.69 ?  69  ILE   A CG1  1 
ATOM   1649 C CG2  . ILE   A 1 69  ? 37.209 5.849   -2.887  1.00 14.93 ?  69  ILE   A CG2  1 
ATOM   1650 C CD1  . ILE   A 1 69  ? 35.516 3.602   -1.870  1.00 14.22 ?  69  ILE   A CD1  1 
ATOM   1651 H H    A ILE   A 1 69  ? 37.455 5.495   1.025   0.60 14.27 ?  69  ILE   A H    1 
ATOM   1652 H H    B ILE   A 1 69  ? 37.429 5.466   1.022   0.40 14.27 ?  69  ILE   A H    1 
ATOM   1653 H HA   . ILE   A 1 69  ? 38.169 4.013   -1.031  1.00 14.46 ?  69  ILE   A HA   1 
ATOM   1654 H HB   . ILE   A 1 69  ? 36.904 6.526   -0.984  1.00 15.92 ?  69  ILE   A HB   1 
ATOM   1655 H HG12 . ILE   A 1 69  ? 35.610 4.711   -0.169  1.00 16.40 ?  69  ILE   A HG12 1 
ATOM   1656 H HG13 . ILE   A 1 69  ? 34.928 5.485   -1.374  1.00 16.40 ?  69  ILE   A HG13 1 
ATOM   1657 H HG21 . ILE   A 1 69  ? 36.359 6.056   -3.312  1.00 17.90 ?  69  ILE   A HG21 1 
ATOM   1658 H HG22 . ILE   A 1 69  ? 37.824 6.592   -3.018  1.00 17.90 ?  69  ILE   A HG22 1 
ATOM   1659 H HG23 . ILE   A 1 69  ? 37.578 5.040   -3.266  1.00 17.90 ?  69  ILE   A HG23 1 
ATOM   1660 H HD11 . ILE   A 1 69  ? 34.698 3.167   -1.582  1.00 17.04 ?  69  ILE   A HD11 1 
ATOM   1661 H HD12 . ILE   A 1 69  ? 35.470 3.787   -2.822  1.00 17.04 ?  69  ILE   A HD12 1 
ATOM   1662 H HD13 . ILE   A 1 69  ? 36.277 3.035   -1.678  1.00 17.04 ?  69  ILE   A HD13 1 
ATOM   1663 N N    . ALA   A 1 70  ? 39.922 6.626   -0.509  1.00 12.41 ?  70  ALA   A N    1 
ATOM   1664 C CA   . ALA   A 1 70  ? 41.195 7.237   -0.868  1.00 13.21 ?  70  ALA   A CA   1 
ATOM   1665 C C    . ALA   A 1 70  ? 42.343 6.249   -0.703  1.00 13.36 ?  70  ALA   A C    1 
ATOM   1666 O O    . ALA   A 1 70  ? 43.303 6.275   -1.479  1.00 15.43 ?  70  ALA   A O    1 
ATOM   1667 C CB   . ALA   A 1 70  ? 41.426 8.487   -0.021  1.00 14.02 ?  70  ALA   A CB   1 
ATOM   1668 H H    . ALA   A 1 70  ? 39.496 7.013   0.126   1.00 14.87 ?  70  ALA   A H    1 
ATOM   1669 H HA   . ALA   A 1 70  ? 41.163 7.511   -1.800  1.00 15.82 ?  70  ALA   A HA   1 
ATOM   1670 H HB1  . ALA   A 1 70  ? 42.279 8.880   -0.269  1.00 16.80 ?  70  ALA   A HB1  1 
ATOM   1671 H HB2  . ALA   A 1 70  ? 40.710 9.118   -0.184  1.00 16.80 ?  70  ALA   A HB2  1 
ATOM   1672 H HB3  . ALA   A 1 70  ? 41.440 8.233   0.915   1.00 16.80 ?  70  ALA   A HB3  1 
ATOM   1673 N N    . THR   A 1 71  ? 42.254 5.358   0.282   1.00 12.93 ?  71  THR   A N    1 
ATOM   1674 C CA   . THR   A 1 71  ? 43.310 4.381   0.517   1.00 14.43 ?  71  THR   A CA   1 
ATOM   1675 C C    . THR   A 1 71  ? 43.183 3.169   -0.394  1.00 14.39 ?  71  THR   A C    1 
ATOM   1676 O O    . THR   A 1 71  ? 44.187 2.675   -0.920  1.00 16.34 ?  71  THR   A O    1 
ATOM   1677 C CB   . THR   A 1 71  ? 43.255 3.924   1.971   1.00 16.28 ?  71  THR   A CB   1 
ATOM   1678 O OG1  . THR   A 1 71  ? 43.511 5.049   2.822   1.00 17.72 ?  71  THR   A OG1  1 
ATOM   1679 C CG2  . THR   A 1 71  ? 44.273 2.812   2.241   1.00 17.61 ?  71  THR   A CG2  1 
ATOM   1680 H H    . THR   A 1 71  ? 41.587 5.292   0.820   1.00 15.49 ?  71  THR   A H    1 
ATOM   1681 H HA   . THR   A 1 71  ? 44.172 4.793   0.353   1.00 17.30 ?  71  THR   A HA   1 
ATOM   1682 H HB   . THR   A 1 71  ? 42.372 3.569   2.160   1.00 19.51 ?  71  THR   A HB   1 
ATOM   1683 H HG1  . THR   A 1 71  ? 43.485 4.799   3.627   1.00 21.24 ?  71  THR   A HG1  1 
ATOM   1684 H HG21 . THR   A 1 71  ? 44.413 2.718   3.197   1.00 21.11 ?  71  THR   A HG21 1 
ATOM   1685 H HG22 . THR   A 1 71  ? 43.954 1.967   1.887   1.00 21.11 ?  71  THR   A HG22 1 
ATOM   1686 H HG23 . THR   A 1 71  ? 45.122 3.030   1.822   1.00 21.11 ?  71  THR   A HG23 1 
ATOM   1687 N N    . ASN   A 1 72  ? 41.963 2.660   -0.573  1.00 13.55 ?  72  ASN   A N    1 
ATOM   1688 C CA   . ASN   A 1 72  ? 41.752 1.336   -1.139  1.00 13.86 ?  72  ASN   A CA   1 
ATOM   1689 C C    . ASN   A 1 72  ? 41.120 1.332   -2.519  1.00 14.21 ?  72  ASN   A C    1 
ATOM   1690 O O    . ASN   A 1 72  ? 41.121 0.282   -3.172  1.00 15.31 ?  72  ASN   A O    1 
ATOM   1691 C CB   . ASN   A 1 72  ? 40.867 0.515   -0.196  1.00 14.64 ?  72  ASN   A CB   1 
ATOM   1692 C CG   . ASN   A 1 72  ? 41.485 0.361   1.165   1.00 15.50 ?  72  ASN   A CG   1 
ATOM   1693 O OD1  . ASN   A 1 72  ? 41.031 0.957   2.138   1.00 17.60 ?  72  ASN   A OD1  1 
ATOM   1694 N ND2  . ASN   A 1 72  ? 42.538 -0.420  1.239   1.00 15.95 ?  72  ASN   A ND2  1 
ATOM   1695 H H    . ASN   A 1 72  ? 41.229 3.071   -0.372  1.00 16.24 ?  72  ASN   A H    1 
ATOM   1696 H HA   . ASN   A 1 72  ? 42.603 0.886   -1.207  1.00 16.61 ?  72  ASN   A HA   1 
ATOM   1697 H HB2  . ASN   A 1 72  ? 40.009 0.958   -0.089  1.00 17.54 ?  72  ASN   A HB2  1 
ATOM   1698 H HB3  . ASN   A 1 72  ? 40.738 -0.373  -0.565  1.00 17.54 ?  72  ASN   A HB3  1 
ATOM   1699 H HD21 . ASN   A 1 72  ? 42.936 -0.534  1.995   1.00 19.11 ?  72  ASN   A HD21 1 
ATOM   1700 H HD22 . ASN   A 1 72  ? 42.835 -0.806  0.534   1.00 19.11 ?  72  ASN   A HD22 1 
ATOM   1701 N N    . GLY   A 1 73  ? 40.556 2.445   -2.967  1.00 13.64 ?  73  GLY   A N    1 
ATOM   1702 C CA   . GLY   A 1 73  ? 39.828 2.460   -4.212  1.00 13.44 ?  73  GLY   A CA   1 
ATOM   1703 C C    . GLY   A 1 73  ? 38.437 1.883   -4.039  1.00 12.64 ?  73  GLY   A C    1 
ATOM   1704 O O    . GLY   A 1 73  ? 38.062 1.416   -2.958  1.00 13.31 ?  73  GLY   A O    1 
ATOM   1705 H H    . GLY   A 1 73  ? 40.580 3.210   -2.567  1.00 16.34 ?  73  GLY   A H    1 
ATOM   1706 H HA2  . GLY   A 1 73  ? 39.750 3.375   -4.531  1.00 16.10 ?  73  GLY   A HA2  1 
ATOM   1707 H HA3  . GLY   A 1 73  ? 40.303 1.939   -4.876  1.00 16.10 ?  73  GLY   A HA3  1 
ATOM   1708 N N    . PRO   A 1 74  ? 37.648 1.907   -5.114  1.00 13.06 ?  74  PRO   A N    1 
ATOM   1709 C CA   . PRO   A 1 74  ? 36.252 1.467   -5.024  1.00 13.14 ?  74  PRO   A CA   1 
ATOM   1710 C C    . PRO   A 1 74  ? 36.113 -0.015  -4.717  1.00 12.41 ?  74  PRO   A C    1 
ATOM   1711 O O    . PRO   A 1 74  ? 36.990 -0.837  -5.007  1.00 13.49 ?  74  PRO   A O    1 
ATOM   1712 C CB   . PRO   A 1 74  ? 35.688 1.788   -6.415  1.00 15.25 ?  74  PRO   A CB   1 
ATOM   1713 C CG   . PRO   A 1 74  ? 36.625 2.803   -7.003  1.00 17.23 ?  74  PRO   A CG   1 
ATOM   1714 C CD   . PRO   A 1 74  ? 37.972 2.452   -6.442  1.00 14.66 ?  74  PRO   A CD   1 
ATOM   1715 H HA   . PRO   A 1 74  ? 35.772 1.983   -4.355  1.00 15.75 ?  74  PRO   A HA   1 
ATOM   1716 H HB2  . PRO   A 1 74  ? 35.665 0.983   -6.953  1.00 18.28 ?  74  PRO   A HB2  1 
ATOM   1717 H HB3  . PRO   A 1 74  ? 34.791 2.161   -6.326  1.00 18.28 ?  74  PRO   A HB3  1 
ATOM   1718 H HG2  . PRO   A 1 74  ? 36.627 2.728   -7.970  1.00 20.65 ?  74  PRO   A HG2  1 
ATOM   1719 H HG3  . PRO   A 1 74  ? 36.361 3.695   -6.728  1.00 20.65 ?  74  PRO   A HG3  1 
ATOM   1720 H HD2  . PRO   A 1 74  ? 38.405 1.780   -6.990  1.00 17.57 ?  74  PRO   A HD2  1 
ATOM   1721 H HD3  . PRO   A 1 74  ? 38.519 3.254   -6.367  1.00 17.57 ?  74  PRO   A HD3  1 
ATOM   1722 N N    . LEU   A 1 75  ? 34.971 -0.346  -4.126  1.00 12.15 ?  75  LEU   A N    1 
ATOM   1723 C CA   . LEU   A 1 75  ? 34.588 -1.738  -3.974  1.00 11.77 ?  75  LEU   A CA   1 
ATOM   1724 C C    . LEU   A 1 75  ? 34.204 -2.325  -5.331  1.00 12.07 ?  75  LEU   A C    1 
ATOM   1725 O O    . LEU   A 1 75  ? 34.054 -1.617  -6.329  1.00 13.60 ?  75  LEU   A O    1 
ATOM   1726 C CB   . LEU   A 1 75  ? 33.398 -1.871  -3.026  1.00 11.53 ?  75  LEU   A CB   1 
ATOM   1727 C CG   . LEU   A 1 75  ? 33.614 -1.459  -1.576  1.00 13.43 ?  75  LEU   A CG   1 
ATOM   1728 C CD1  . LEU   A 1 75  ? 32.326 -1.625  -0.776  1.00 15.27 ?  75  LEU   A CD1  1 
ATOM   1729 C CD2  . LEU   A 1 75  ? 34.741 -2.223  -0.940  1.00 17.01 ?  75  LEU   A CD2  1 
ATOM   1730 H H    . LEU   A 1 75  ? 34.399 0.214   -3.812  1.00 14.56 ?  75  LEU   A H    1 
ATOM   1731 H HA   . LEU   A 1 75  ? 35.334 -2.244  -3.621  1.00 14.10 ?  75  LEU   A HA   1 
ATOM   1732 H HB2  . LEU   A 1 75  ? 32.672 -1.331  -3.373  1.00 13.81 ?  75  LEU   A HB2  1 
ATOM   1733 H HB3  . LEU   A 1 75  ? 33.124 -2.804  -3.018  1.00 13.81 ?  75  LEU   A HB3  1 
ATOM   1734 H HG   . LEU   A 1 75  ? 33.860 -0.517  -1.560  1.00 16.10 ?  75  LEU   A HG   1 
ATOM   1735 H HD11 . LEU   A 1 75  ? 32.489 -1.351  0.141   1.00 18.30 ?  75  LEU   A HD11 1 
ATOM   1736 H HD12 . LEU   A 1 75  ? 31.640 -1.062  -1.171  1.00 18.30 ?  75  LEU   A HD12 1 
ATOM   1737 H HD13 . LEU   A 1 75  ? 32.056 -2.552  -0.805  1.00 18.30 ?  75  LEU   A HD13 1 
ATOM   1738 H HD21 . LEU   A 1 75  ? 34.805 -1.969  -0.007  1.00 20.39 ?  75  LEU   A HD21 1 
ATOM   1739 H HD22 . LEU   A 1 75  ? 34.560 -3.171  -1.017  1.00 20.39 ?  75  LEU   A HD22 1 
ATOM   1740 H HD23 . LEU   A 1 75  ? 35.571 -2.006  -1.397  1.00 20.39 ?  75  LEU   A HD23 1 
ATOM   1741 N N    . LYS   A 1 76  ? 34.049 -3.645  -5.351  1.00 12.37 ?  76  LYS   A N    1 
ATOM   1742 C CA   . LYS   A 1 76  ? 33.448 -4.364  -6.468  1.00 12.94 ?  76  LYS   A CA   1 
ATOM   1743 C C    . LYS   A 1 76  ? 31.937 -4.445  -6.273  1.00 11.53 ?  76  LYS   A C    1 
ATOM   1744 O O    . LYS   A 1 76  ? 31.455 -4.563  -5.148  1.00 11.81 ?  76  LYS   A O    1 
ATOM   1745 C CB   . LYS   A 1 76  ? 33.987 -5.804  -6.523  1.00 14.66 ?  76  LYS   A CB   1 
ATOM   1746 C CG   . LYS   A 1 76  ? 35.495 -5.919  -6.717  1.00 15.87 ?  76  LYS   A CG   1 
ATOM   1747 C CD   . LYS   A 1 76  ? 36.000 -7.327  -6.509  1.00 16.91 ?  76  LYS   A CD   1 
ATOM   1748 C CE   . LYS   A 1 76  ? 37.493 -7.412  -6.731  1.00 19.36 ?  76  LYS   A CE   1 
ATOM   1749 N NZ   . LYS   A 1 76  ? 38.017 -8.764  -6.480  1.00 20.27 ?  76  LYS   A NZ   1 
ATOM   1750 H H    . LYS   A 1 76  ? 34.297 -4.163  -4.708  1.00 14.83 ?  76  LYS   A H    1 
ATOM   1751 H HA   . LYS   A 1 76  ? 33.645 -3.913  -7.305  1.00 15.51 ?  76  LYS   A HA   1 
ATOM   1752 H HB2  . LYS   A 1 76  ? 33.764 -6.246  -5.690  1.00 17.56 ?  76  LYS   A HB2  1 
ATOM   1753 H HB3  . LYS   A 1 76  ? 33.561 -6.261  -7.263  1.00 17.56 ?  76  LYS   A HB3  1 
ATOM   1754 H HG2  . LYS   A 1 76  ? 35.720 -5.645  -7.621  1.00 19.02 ?  76  LYS   A HG2  1 
ATOM   1755 H HG3  . LYS   A 1 76  ? 35.942 -5.340  -6.077  1.00 19.02 ?  76  LYS   A HG3  1 
ATOM   1756 H HD2  . LYS   A 1 76  ? 35.807 -7.607  -5.601  1.00 20.27 ?  76  LYS   A HD2  1 
ATOM   1757 H HD3  . LYS   A 1 76  ? 35.562 -7.920  -7.143  1.00 20.27 ?  76  LYS   A HD3  1 
ATOM   1758 H HE2  . LYS   A 1 76  ? 37.691 -7.177  -7.649  1.00 23.20 ?  76  LYS   A HE2  1 
ATOM   1759 H HE3  . LYS   A 1 76  ? 37.937 -6.801  -6.124  1.00 23.20 ?  76  LYS   A HE3  1 
ATOM   1760 H HZ1  . LYS   A 1 76  ? 38.893 -8.788  -6.618  1.00 24.30 ?  76  LYS   A HZ1  1 
ATOM   1761 H HZ2  . LYS   A 1 76  ? 37.848 -9.011  -5.639  1.00 24.30 ?  76  LYS   A HZ2  1 
ATOM   1762 H HZ3  . LYS   A 1 76  ? 37.624 -9.353  -7.029  1.00 24.30 ?  76  LYS   A HZ3  1 
ATOM   1763 N N    . VAL   A 1 77  ? 31.189 -4.415  -7.380  1.00 12.07 ?  77  VAL   A N    1 
ATOM   1764 C CA   . VAL   A 1 77  ? 29.781 -4.792  -7.296  1.00 12.28 ?  77  VAL   A CA   1 
ATOM   1765 C C    . VAL   A 1 77  ? 29.718 -6.243  -6.849  1.00 12.04 ?  77  VAL   A C    1 
ATOM   1766 O O    . VAL   A 1 77  ? 30.385 -7.114  -7.420  1.00 12.20 ?  77  VAL   A O    1 
ATOM   1767 C CB   . VAL   A 1 77  ? 29.070 -4.577  -8.639  1.00 13.68 ?  77  VAL   A CB   1 
ATOM   1768 C CG1  . VAL   A 1 77  ? 27.618 -5.015  -8.538  1.00 14.65 ?  77  VAL   A CG1  1 
ATOM   1769 C CG2  . VAL   A 1 77  ? 29.153 -3.123  -9.060  1.00 15.34 ?  77  VAL   A CG2  1 
ATOM   1770 H H    . VAL   A 1 77  ? 31.468 -4.182  -8.157  1.00 14.46 ?  77  VAL   A H    1 
ATOM   1771 H HA   . VAL   A 1 77  ? 29.345 -4.244  -6.624  1.00 14.71 ?  77  VAL   A HA   1 
ATOM   1772 H HB   . VAL   A 1 77  ? 29.508 -5.114  -9.318  1.00 16.39 ?  77  VAL   A HB   1 
ATOM   1773 H HG11 . VAL   A 1 77  ? 27.148 -4.708  -9.324  1.00 17.56 ?  77  VAL   A HG11 1 
ATOM   1774 H HG12 . VAL   A 1 77  ? 27.584 -5.982  -8.483  1.00 17.56 ?  77  VAL   A HG12 1 
ATOM   1775 H HG13 . VAL   A 1 77  ? 27.230 -4.621  -7.741  1.00 17.56 ?  77  VAL   A HG13 1 
ATOM   1776 H HG21 . VAL   A 1 77  ? 28.674 -3.012  -9.896  1.00 18.38 ?  77  VAL   A HG21 1 
ATOM   1777 H HG22 . VAL   A 1 77  ? 28.749 -2.572  -8.371  1.00 18.38 ?  77  VAL   A HG22 1 
ATOM   1778 H HG23 . VAL   A 1 77  ? 30.084 -2.877  -9.177  1.00 18.38 ?  77  VAL   A HG23 1 
ATOM   1779 N N    . GLY   A 1 78  ? 28.927 -6.510  -5.811  1.00 11.30 ?  78  GLY   A N    1 
ATOM   1780 C CA   . GLY   A 1 78  ? 28.900 -7.798  -5.156  1.00 11.49 ?  78  GLY   A CA   1 
ATOM   1781 C C    . GLY   A 1 78  ? 29.821 -7.899  -3.964  1.00 10.83 ?  78  GLY   A C    1 
ATOM   1782 O O    . GLY   A 1 78  ? 29.769 -8.906  -3.245  1.00 11.70 ?  78  GLY   A O    1 
ATOM   1783 H H    . GLY   A 1 78  ? 28.371 -5.939  -5.474  1.00 13.54 ?  78  GLY   A H    1 
ATOM   1784 H HA2  . GLY   A 1 78  ? 27.994 -7.981  -4.854  1.00 13.77 ?  78  GLY   A HA2  1 
ATOM   1785 H HA3  . GLY   A 1 78  ? 29.149 -8.483  -5.793  1.00 13.77 ?  78  GLY   A HA3  1 
ATOM   1786 N N    . GLY   A 1 79  ? 30.678 -6.899  -3.743  1.00 11.23 ?  79  GLY   A N    1 
ATOM   1787 C CA   . GLY   A 1 79  ? 31.643 -6.920  -2.669  1.00 11.41 ?  79  GLY   A CA   1 
ATOM   1788 C C    . GLY   A 1 79  ? 31.195 -6.129  -1.454  1.00 10.91 ?  79  GLY   A C    1 
ATOM   1789 O O    . GLY   A 1 79  ? 30.071 -5.631  -1.371  1.00 11.27 ?  79  GLY   A O    1 
ATOM   1790 H H    . GLY   A 1 79  ? 30.722 -6.186  -4.225  1.00 13.45 ?  79  GLY   A H    1 
ATOM   1791 H HA2  . GLY   A 1 79  ? 31.800 -7.845  -2.399  1.00 13.66 ?  79  GLY   A HA2  1 
ATOM   1792 H HA3  . GLY   A 1 79  ? 32.484 -6.554  -2.982  1.00 13.66 ?  79  GLY   A HA3  1 
ATOM   1793 N N    . SER   A 1 80  ? 32.099 -6.034  -0.485  1.00 11.68 ?  80  SER   A N    1 
ATOM   1794 C CA   . SER   A 1 80  ? 31.787 -5.406  0.789   1.00 11.03 ?  80  SER   A CA   1 
ATOM   1795 C C    . SER   A 1 80  ? 33.061 -4.957  1.484   1.00 10.89 ?  80  SER   A C    1 
ATOM   1796 O O    . SER   A 1 80  ? 34.173 -5.382  1.147   1.00 12.24 ?  80  SER   A O    1 
ATOM   1797 C CB   . SER   A 1 80  ? 31.036 -6.375  1.711   1.00 12.07 ?  80  SER   A CB   1 
ATOM   1798 O OG   . SER   A 1 80  ? 31.867 -7.430  2.168   1.00 13.52 ?  80  SER   A OG   1 
ATOM   1799 H H    . SER   A 1 80  ? 32.906 -6.319  -0.546  1.00 13.99 ?  80  SER   A H    1 
ATOM   1800 H HA   . SER   A 1 80  ? 31.231 -4.629  0.622   1.00 13.21 ?  80  SER   A HA   1 
ATOM   1801 H HB2  . SER   A 1 80  ? 30.705 -5.883  2.478   1.00 14.46 ?  80  SER   A HB2  1 
ATOM   1802 H HB3  . SER   A 1 80  ? 30.290 -6.756  1.219   1.00 14.46 ?  80  SER   A HB3  1 
ATOM   1803 H HG   . SER   A 1 80  ? 32.163 -7.859  1.506   1.00 16.20 ?  80  SER   A HG   1 
ATOM   1804 N N    . CYS   A 1 81  ? 32.873 -4.110  2.493   1.00 10.54 ?  81  CYS   A N    1 
ATOM   1805 C CA   . CYS   A 1 81  ? 33.928 -3.829  3.451   1.00 10.81 ?  81  CYS   A CA   1 
ATOM   1806 C C    . CYS   A 1 81  ? 33.294 -3.606  4.813   1.00 10.64 ?  81  CYS   A C    1 
ATOM   1807 O O    . CYS   A 1 81  ? 32.128 -3.210  4.908   1.00 11.97 ?  81  CYS   A O    1 
ATOM   1808 C CB   . CYS   A 1 81  ? 34.793 -2.630  3.034   1.00 11.86 ?  81  CYS   A CB   1 
ATOM   1809 S SG   . CYS   A 1 81  ? 33.888 -1.061  3.059   1.00 11.95 ?  81  CYS   A SG   1 
ATOM   1810 H H    . CYS   A 1 81  ? 32.142 -3.673  2.643   1.00 12.62 ?  81  CYS   A H    1 
ATOM   1811 H HA   . CYS   A 1 81  ? 34.511 -4.599  3.509   1.00 12.95 ?  81  CYS   A HA   1 
ATOM   1812 H HB2  . CYS   A 1 81  ? 35.547 -2.554  3.645   1.00 14.20 ?  81  CYS   A HB2  1 
ATOM   1813 H HB3  . CYS   A 1 81  ? 35.124 -2.777  2.130   1.00 14.20 ?  81  CYS   A HB3  1 
ATOM   1814 H HG   . CYS   A 1 81  ? 34.625 -0.173  2.720   1.00 14.31 ?  81  CYS   A HG   1 
ATOM   1815 N N    . VAL   A 1 82  ? 34.070 -3.867  5.864   1.00 11.33 ?  82  VAL   A N    1 
ATOM   1816 C CA   . VAL   A 1 82  ? 33.650 -3.634  7.239   1.00 11.76 ?  82  VAL   A CA   1 
ATOM   1817 C C    . VAL   A 1 82  ? 34.249 -2.320  7.709   1.00 11.86 ?  82  VAL   A C    1 
ATOM   1818 O O    . VAL   A 1 82  ? 35.472 -2.138  7.684   1.00 12.97 ?  82  VAL   A O    1 
ATOM   1819 C CB   . VAL   A 1 82  ? 34.083 -4.776  8.171   1.00 13.40 ?  82  VAL   A CB   1 
ATOM   1820 C CG1  . VAL   A 1 82  ? 33.633 -4.482  9.595   1.00 14.69 ?  82  VAL   A CG1  1 
ATOM   1821 C CG2  . VAL   A 1 82  ? 33.534 -6.114  7.696   1.00 14.29 ?  82  VAL   A CG2  1 
ATOM   1822 H H    . VAL   A 1 82  ? 34.868 -4.208  5.802   1.00 13.58 ?  82  VAL   A H    1 
ATOM   1823 H HA   . VAL   A 1 82  ? 32.682 -3.566  7.267   1.00 14.09 ?  82  VAL   A HA   1 
ATOM   1824 H HB   . VAL   A 1 82  ? 35.049 -4.829  8.175   1.00 16.05 ?  82  VAL   A HB   1 
ATOM   1825 H HG11 . VAL   A 1 82  ? 33.715 -5.287  10.126  1.00 17.61 ?  82  VAL   A HG11 1 
ATOM   1826 H HG12 . VAL   A 1 82  ? 34.189 -3.780  9.970   1.00 17.61 ?  82  VAL   A HG12 1 
ATOM   1827 H HG13 . VAL   A 1 82  ? 32.704 -4.192  9.580   1.00 17.61 ?  82  VAL   A HG13 1 
ATOM   1828 H HG21 . VAL   A 1 82  ? 33.791 -6.800  8.331   1.00 17.13 ?  82  VAL   A HG21 1 
ATOM   1829 H HG22 . VAL   A 1 82  ? 32.569 -6.055  7.640   1.00 17.13 ?  82  VAL   A HG22 1 
ATOM   1830 H HG23 . VAL   A 1 82  ? 33.908 -6.310  6.824   1.00 17.13 ?  82  VAL   A HG23 1 
ATOM   1831 N N    . LEU   A 1 83  ? 33.390 -1.405  8.135   1.00 11.47 ?  83  LEU   A N    1 
ATOM   1832 C CA   . LEU   A 1 83  ? 33.811 -0.141  8.717   1.00 11.59 ?  83  LEU   A CA   1 
ATOM   1833 C C    . LEU   A 1 83  ? 33.104 0.026   10.055  1.00 11.83 ?  83  LEU   A C    1 
ATOM   1834 O O    . LEU   A 1 83  ? 32.396 -0.870  10.524  1.00 12.54 ?  83  LEU   A O    1 
ATOM   1835 C CB   . LEU   A 1 83  ? 33.551 1.023   7.750   1.00 12.01 ?  83  LEU   A CB   1 
ATOM   1836 C CG   . LEU   A 1 83  ? 34.448 1.028   6.506   1.00 12.67 ?  83  LEU   A CG   1 
ATOM   1837 C CD1  . LEU   A 1 83  ? 34.005 2.081   5.511   1.00 12.89 ?  83  LEU   A CD1  1 
ATOM   1838 C CD2  . LEU   A 1 83  ? 35.918 1.240   6.882   1.00 13.71 ?  83  LEU   A CD2  1 
ATOM   1839 H H    . LEU   A 1 83  ? 32.532 -1.494  8.085   1.00 13.75 ?  83  LEU   A H    1 
ATOM   1840 H HA   . LEU   A 1 83  ? 34.763 -0.175  8.884   1.00 13.88 ?  83  LEU   A HA   1 
ATOM   1841 H HB2  . LEU   A 1 83  ? 32.632 0.983   7.444   1.00 14.39 ?  83  LEU   A HB2  1 
ATOM   1842 H HB3  . LEU   A 1 83  ? 33.700 1.860   8.219   1.00 14.39 ?  83  LEU   A HB3  1 
ATOM   1843 H HG   . LEU   A 1 83  ? 34.382 0.164   6.072   1.00 15.18 ?  83  LEU   A HG   1 
ATOM   1844 H HD11 . LEU   A 1 83  ? 34.593 2.047   4.736   1.00 15.44 ?  83  LEU   A HD11 1 
ATOM   1845 H HD12 . LEU   A 1 83  ? 33.094 1.893   5.241   1.00 15.44 ?  83  LEU   A HD12 1 
ATOM   1846 H HD13 . LEU   A 1 83  ? 34.059 2.953   5.927   1.00 15.44 ?  83  LEU   A HD13 1 
ATOM   1847 H HD21 . LEU   A 1 83  ? 36.433 1.405   6.073   1.00 16.43 ?  83  LEU   A HD21 1 
ATOM   1848 H HD22 . LEU   A 1 83  ? 35.988 2.005   7.475   1.00 16.43 ?  83  LEU   A HD22 1 
ATOM   1849 H HD23 . LEU   A 1 83  ? 36.254 0.446   7.326   1.00 16.43 ?  83  LEU   A HD23 1 
ATOM   1850 N N    . SER   A 1 84  ? 33.316 1.175   10.689  1.00 12.20 ?  84  SER   A N    1 
ATOM   1851 C CA   . SER   A 1 84  ? 32.672 1.433   11.966  1.00 12.42 ?  84  SER   A CA   1 
ATOM   1852 C C    . SER   A 1 84  ? 31.155 1.518   11.820  1.00 12.23 ?  84  SER   A C    1 
ATOM   1853 O O    . SER   A 1 84  ? 30.631 1.981   10.810  1.00 12.64 ?  84  SER   A O    1 
ATOM   1854 C CB   . SER   A 1 84  ? 33.169 2.758   12.533  1.00 13.69 ?  84  SER   A CB   1 
ATOM   1855 O OG   . SER   A 1 84  ? 32.562 3.017   13.783  1.00 14.55 ?  84  SER   A OG   1 
ATOM   1856 H H    . SER   A 1 84  ? 33.822 1.814   10.399  1.00 14.62 ?  84  SER   A H    1 
ATOM   1857 H HA   . SER   A 1 84  ? 32.890 0.725   12.585  1.00 14.88 ?  84  SER   A HA   1 
ATOM   1858 H HB2  . SER   A 1 84  ? 34.129 2.716   12.650  1.00 16.40 ?  84  SER   A HB2  1 
ATOM   1859 H HB3  . SER   A 1 84  ? 32.942 3.475   11.914  1.00 16.40 ?  84  SER   A HB3  1 
ATOM   1860 H HG   . SER   A 1 84  ? 32.834 3.754   14.091  1.00 17.44 ?  84  SER   A HG   1 
ATOM   1861 N N    . GLY   A 1 85  ? 30.449 1.095   12.866  1.00 13.52 ?  85  GLY   A N    1 
ATOM   1862 C CA   . GLY   A 1 85  ? 29.028 1.338   12.972  1.00 14.33 ?  85  GLY   A CA   1 
ATOM   1863 C C    . GLY   A 1 85  ? 28.679 2.643   13.642  1.00 14.28 ?  85  GLY   A C    1 
ATOM   1864 O O    . GLY   A 1 85  ? 27.495 2.957   13.789  1.00 14.47 ?  85  GLY   A O    1 
ATOM   1865 H H    . GLY   A 1 85  ? 30.784 0.667   13.530  1.00 16.20 ?  85  GLY   A H    1 
ATOM   1866 H HA2  . GLY   A 1 85  ? 28.640 1.337   12.082  1.00 17.18 ?  85  GLY   A HA2  1 
ATOM   1867 H HA3  . GLY   A 1 85  ? 28.622 0.627   13.482  1.00 17.18 ?  85  GLY   A HA3  1 
ATOM   1868 N N    . HIS   A 1 86  ? 29.677 3.408   14.070  1.00 13.81 ?  86  HIS   A N    1 
ATOM   1869 C CA   . HIS   A 1 86  ? 29.467 4.739   14.651  1.00 14.06 ?  86  HIS   A CA   1 
ATOM   1870 C C    . HIS   A 1 86  ? 28.498 4.605   15.819  1.00 15.16 ?  86  HIS   A C    1 
ATOM   1871 O O    . HIS   A 1 86  ? 28.695 3.721   16.669  1.00 16.20 ?  86  HIS   A O    1 
ATOM   1872 C CB   . HIS   A 1 86  ? 29.079 5.734   13.569  1.00 13.97 ?  86  HIS   A CB   1 
ATOM   1873 C CG   . HIS   A 1 86  ? 30.117 5.842   12.515  1.00 13.54 ?  86  HIS   A CG   1 
ATOM   1874 N ND1  . HIS   A 1 86  ? 31.198 6.689   12.629  1.00 14.60 ?  86  HIS   A ND1  1 
ATOM   1875 C CD2  . HIS   A 1 86  ? 30.297 5.144   11.373  1.00 13.00 ?  86  HIS   A CD2  1 
ATOM   1876 C CE1  . HIS   A 1 86  ? 31.979 6.531   11.577  1.00 14.16 ?  86  HIS   A CE1  1 
ATOM   1877 N NE2  . HIS   A 1 86  ? 31.462 5.591   10.807  1.00 13.38 ?  86  HIS   A NE2  1 
ATOM   1878 H H    . HIS   A 1 86  ? 30.500 3.180   14.046  1.00 16.54 ?  86  HIS   A H    1 
ATOM   1879 H HA   . HIS   A 1 86  ? 30.311 5.049   15.013  1.00 16.85 ?  86  HIS   A HA   1 
ATOM   1880 H HB2  . HIS   A 1 86  ? 28.249 5.453   13.149  1.00 16.74 ?  86  HIS   A HB2  1 
ATOM   1881 H HB3  . HIS   A 1 86  ? 28.960 6.619   13.964  1.00 16.74 ?  86  HIS   A HB3  1 
ATOM   1882 H HD2  . HIS   A 1 86  ? 29.739 4.476   11.037  1.00 15.58 ?  86  HIS   A HD2  1 
ATOM   1883 H HE1  . HIS   A 1 86  ? 32.763 7.001   11.398  1.00 16.97 ?  86  HIS   A HE1  1 
ATOM   1884 H HE2  . HIS   A 1 86  ? 31.793 5.313   10.056  1.00 16.04 ?  86  HIS   A HE2  1 
ATOM   1885 N N    . ASN   A 1 87  ? 27.487 5.455   15.914  1.00 16.04 ?  87  ASN   A N    1 
ATOM   1886 C CA   . ASN   A 1 87  ? 26.532 5.434   17.006  1.00 16.80 ?  87  ASN   A CA   1 
ATOM   1887 C C    . ASN   A 1 87  ? 25.408 4.433   16.784  1.00 17.89 ?  87  ASN   A C    1 
ATOM   1888 O O    . ASN   A 1 87  ? 24.517 4.337   17.632  1.00 20.09 ?  87  ASN   A O    1 
ATOM   1889 C CB   . ASN   A 1 87  ? 25.935 6.837   17.186  1.00 18.06 ?  87  ASN   A CB   1 
ATOM   1890 C CG   . ASN   A 1 87  ? 25.405 7.420   15.881  1.00 18.99 ?  87  ASN   A CG   1 
ATOM   1891 O OD1  . ASN   A 1 87  ? 26.048 7.335   14.838  1.00 19.34 ?  87  ASN   A OD1  1 
ATOM   1892 N ND2  . ASN   A 1 87  ? 24.232 8.024   15.942  1.00 20.49 ?  87  ASN   A ND2  1 
ATOM   1893 H H    . ASN   A 1 87  ? 27.330 6.074   15.343  1.00 19.23 ?  87  ASN   A H    1 
ATOM   1894 H HA   . ASN   A 1 87  ? 26.983 5.190   17.833  1.00 20.14 ?  87  ASN   A HA   1 
ATOM   1895 H HB2  . ASN   A 1 87  ? 25.197 6.786   17.821  1.00 21.65 ?  87  ASN   A HB2  1 
ATOM   1896 H HB3  . ASN   A 1 87  ? 26.621 7.429   17.527  1.00 21.65 ?  87  ASN   A HB3  1 
ATOM   1897 H HD21 . ASN   A 1 87  ? 23.892 8.364   15.233  1.00 24.57 ?  87  ASN   A HD21 1 
ATOM   1898 H HD22 . ASN   A 1 87  ? 23.809 8.072   16.691  1.00 24.57 ?  87  ASN   A HD22 1 
ATOM   1899 N N    A LEU   A 1 88  ? 25.438 3.680   15.684  0.60 17.18 ?  88  LEU   A N    1 
ATOM   1900 N N    B LEU   A 1 88  ? 25.433 3.677   15.689  0.40 17.37 ?  88  LEU   A N    1 
ATOM   1901 C CA   A LEU   A 1 88  ? 24.323 2.823   15.294  0.60 16.99 ?  88  LEU   A CA   1 
ATOM   1902 C CA   B LEU   A 1 88  ? 24.314 2.821   15.314  0.40 17.18 ?  88  LEU   A CA   1 
ATOM   1903 C C    A LEU   A 1 88  ? 24.551 1.348   15.588  0.60 16.66 ?  88  LEU   A C    1 
ATOM   1904 C C    B LEU   A 1 88  ? 24.549 1.341   15.566  0.40 16.77 ?  88  LEU   A C    1 
ATOM   1905 O O    A LEU   A 1 88  ? 23.581 0.618   15.814  0.60 17.85 ?  88  LEU   A O    1 
ATOM   1906 O O    B LEU   A 1 88  ? 23.582 0.600   15.750  0.40 17.64 ?  88  LEU   A O    1 
ATOM   1907 C CB   A LEU   A 1 88  ? 24.054 2.973   13.794  0.60 17.74 ?  88  LEU   A CB   1 
ATOM   1908 C CB   B LEU   A 1 88  ? 23.982 3.018   13.830  0.40 17.83 ?  88  LEU   A CB   1 
ATOM   1909 C CG   A LEU   A 1 88  ? 23.747 4.374   13.264  0.60 19.25 ?  88  LEU   A CG   1 
ATOM   1910 C CG   B LEU   A 1 88  ? 23.673 4.459   13.415  0.40 18.77 ?  88  LEU   A CG   1 
ATOM   1911 C CD1  A LEU   A 1 88  ? 23.549 4.324   11.758  0.60 19.68 ?  88  LEU   A CD1  1 
ATOM   1912 C CD1  B LEU   A 1 88  ? 23.475 4.557   11.910  0.40 18.83 ?  88  LEU   A CD1  1 
ATOM   1913 C CD2  A LEU   A 1 88  ? 22.524 4.964   13.949  0.60 20.57 ?  88  LEU   A CD2  1 
ATOM   1914 C CD2  B LEU   A 1 88  ? 22.451 4.986   14.156  0.40 19.70 ?  88  LEU   A CD2  1 
ATOM   1915 H H    A LEU   A 1 88  ? 26.106 3.650   15.145  0.60 20.59 ?  88  LEU   A H    1 
ATOM   1916 H H    B LEU   A 1 88  ? 26.098 3.643   15.145  0.40 20.82 ?  88  LEU   A H    1 
ATOM   1917 H HA   A LEU   A 1 88  ? 23.528 3.104   15.769  0.60 20.37 ?  88  LEU   A HA   1 
ATOM   1918 H HA   B LEU   A 1 88  ? 23.536 3.086   15.826  0.40 20.60 ?  88  LEU   A HA   1 
ATOM   1919 H HB2  A LEU   A 1 88  ? 24.832 2.656   13.313  0.60 21.26 ?  88  LEU   A HB2  1 
ATOM   1920 H HB2  B LEU   A 1 88  ? 24.737 2.719   13.302  0.40 21.37 ?  88  LEU   A HB2  1 
ATOM   1921 H HB3  A LEU   A 1 88  ? 23.291 2.418   13.569  0.60 21.26 ?  88  LEU   A HB3  1 
ATOM   1922 H HB3  B LEU   A 1 88  ? 23.202 2.483   13.617  0.40 21.37 ?  88  LEU   A HB3  1 
ATOM   1923 H HG   A LEU   A 1 88  ? 24.503 4.955   13.443  0.60 23.07 ?  88  LEU   A HG   1 
ATOM   1924 H HG   B LEU   A 1 88  ? 24.429 5.021   13.647  0.40 22.50 ?  88  LEU   A HG   1 
ATOM   1925 H HD11 A LEU   A 1 88  ? 23.358 5.219   11.433  0.60 23.59 ?  88  LEU   A HD11 1 
ATOM   1926 H HD11 B LEU   A 1 88  ? 23.286 5.480   11.676  0.40 22.57 ?  88  LEU   A HD11 1 
ATOM   1927 H HD12 A LEU   A 1 88  ? 24.358 3.987   11.343  0.60 23.59 ?  88  LEU   A HD12 1 
ATOM   1928 H HD12 B LEU   A 1 88  ? 24.285 4.263   11.464  0.40 22.57 ?  88  LEU   A HD12 1 
ATOM   1929 H HD13 A LEU   A 1 88  ? 22.804 3.735   11.557  0.60 23.59 ?  88  LEU   A HD13 1 
ATOM   1930 H HD13 B LEU   A 1 88  ? 22.730 3.992   11.652  0.40 22.57 ?  88  LEU   A HD13 1 
ATOM   1931 H HD21 A LEU   A 1 88  ? 22.313 5.817   13.538  0.60 24.66 ?  88  LEU   A HD21 1 
ATOM   1932 H HD21 B LEU   A 1 88  ? 22.210 5.851   13.789  0.40 23.62 ?  88  LEU   A HD21 1 
ATOM   1933 H HD22 A LEU   A 1 88  ? 21.779 4.352   13.844  0.60 24.66 ?  88  LEU   A HD22 1 
ATOM   1934 H HD22 B LEU   A 1 88  ? 21.720 4.361   14.041  0.40 23.62 ?  88  LEU   A HD22 1 
ATOM   1935 H HD23 A LEU   A 1 88  ? 22.722 5.089   14.890  0.60 24.66 ?  88  LEU   A HD23 1 
ATOM   1936 H HD23 B LEU   A 1 88  ? 22.669 5.074   15.096  0.40 23.62 ?  88  LEU   A HD23 1 
ATOM   1937 N N    . ALA   A 1 89  ? 25.801 0.896   15.578  1.00 16.03 ?  89  ALA   A N    1 
ATOM   1938 C CA   . ALA   A 1 89  ? 26.135 -0.517  15.685  1.00 15.72 ?  89  ALA   A CA   1 
ATOM   1939 C C    . ALA   A 1 89  ? 27.623 -0.580  15.978  1.00 16.06 ?  89  ALA   A C    1 
ATOM   1940 O O    . ALA   A 1 89  ? 28.329 0.421   15.863  1.00 16.76 ?  89  ALA   A O    1 
ATOM   1941 C CB   . ALA   A 1 89  ? 25.843 -1.234  14.367  1.00 15.41 ?  89  ALA   A CB   1 
ATOM   1942 H H    A ALA   A 1 89  ? 26.490 1.406   15.505  0.60 19.21 ?  89  ALA   A H    1 
ATOM   1943 H H    B ALA   A 1 89  ? 26.490 1.408   15.516  0.40 19.21 ?  89  ALA   A H    1 
ATOM   1944 H HA   . ALA   A 1 89  ? 25.636 -0.932  16.406  1.00 18.84 ?  89  ALA   A HA   1 
ATOM   1945 H HB1  . ALA   A 1 89  ? 26.107 -2.165  14.449  1.00 18.46 ?  89  ALA   A HB1  1 
ATOM   1946 H HB2  . ALA   A 1 89  ? 24.892 -1.178  14.178  1.00 18.46 ?  89  ALA   A HB2  1 
ATOM   1947 H HB3  . ALA   A 1 89  ? 26.348 -0.811  13.657  1.00 18.46 ?  89  ALA   A HB3  1 
ATOM   1948 N N    . LYS   A 1 90  ? 28.112 -1.764  16.342  1.00 16.30 ?  90  LYS   A N    1 
ATOM   1949 C CA   . LYS   A 1 90  ? 29.557 -1.906  16.482  1.00 17.14 ?  90  LYS   A CA   1 
ATOM   1950 C C    . LYS   A 1 90  ? 30.248 -1.724  15.134  1.00 16.00 ?  90  LYS   A C    1 
ATOM   1951 O O    . LYS   A 1 90  ? 31.183 -0.922  14.997  1.00 17.13 ?  90  LYS   A O    1 
ATOM   1952 C CB   . LYS   A 1 90  ? 29.906 -3.259  17.104  1.00 20.00 ?  90  LYS   A CB   1 
ATOM   1953 C CG   . LYS   A 1 90  ? 31.387 -3.404  17.417  1.00 24.64 ?  90  LYS   A CG   1 
ATOM   1954 C CD   . LYS   A 1 90  ? 31.644 -4.608  18.307  1.00 29.12 ?  90  LYS   A CD   1 
ATOM   1955 C CE   . LYS   A 1 90  ? 33.065 -4.615  18.851  1.00 32.46 ?  90  LYS   A CE   1 
ATOM   1956 N NZ   . LYS   A 1 90  ? 34.071 -4.953  17.810  1.00 34.40 ?  90  LYS   A NZ   1 
ATOM   1957 H H    . LYS   A 1 90  ? 27.648 -2.468  16.506  1.00 19.54 ?  90  LYS   A H    1 
ATOM   1958 H HA   . LYS   A 1 90  ? 29.882 -1.215  17.077  1.00 20.55 ?  90  LYS   A HA   1 
ATOM   1959 H HB2  . LYS   A 1 90  ? 29.411 -3.359  17.936  1.00 23.98 ?  90  LYS   A HB2  1 
ATOM   1960 H HB3  . LYS   A 1 90  ? 29.657 -3.965  16.488  1.00 23.98 ?  90  LYS   A HB3  1 
ATOM   1961 H HG2  . LYS   A 1 90  ? 31.877 -3.522  16.590  1.00 29.55 ?  90  LYS   A HG2  1 
ATOM   1962 H HG3  . LYS   A 1 90  ? 31.694 -2.608  17.881  1.00 29.55 ?  90  LYS   A HG3  1 
ATOM   1963 H HD2  . LYS   A 1 90  ? 31.031 -4.587  19.059  1.00 34.93 ?  90  LYS   A HD2  1 
ATOM   1964 H HD3  . LYS   A 1 90  ? 31.512 -5.419  17.791  1.00 34.93 ?  90  LYS   A HD3  1 
ATOM   1965 H HE2  . LYS   A 1 90  ? 33.276 -3.734  19.198  1.00 38.93 ?  90  LYS   A HE2  1 
ATOM   1966 H HE3  . LYS   A 1 90  ? 33.130 -5.275  19.559  1.00 38.93 ?  90  LYS   A HE3  1 
ATOM   1967 H HZ1  . LYS   A 1 90  ? 33.905 -5.762  17.478  1.00 41.26 ?  90  LYS   A HZ1  1 
ATOM   1968 H HZ2  . LYS   A 1 90  ? 34.040 -4.357  17.151  1.00 41.26 ?  90  LYS   A HZ2  1 
ATOM   1969 H HZ3  . LYS   A 1 90  ? 34.888 -4.950  18.166  1.00 41.26 ?  90  LYS   A HZ3  1 
ATOM   1970 N N    . HIS   A 1 91  ? 29.771 -2.440  14.118  1.00 14.02 ?  91  HIS   A N    1 
ATOM   1971 C CA   . HIS   A 1 91  ? 30.329 -2.405  12.780  1.00 13.46 ?  91  HIS   A CA   1 
ATOM   1972 C C    . HIS   A 1 91  ? 29.228 -2.128  11.772  1.00 11.92 ?  91  HIS   A C    1 
ATOM   1973 O O    . HIS   A 1 91  ? 28.065 -2.495  11.975  1.00 13.05 ?  91  HIS   A O    1 
ATOM   1974 C CB   . HIS   A 1 91  ? 30.932 -3.762  12.393  1.00 16.14 ?  91  HIS   A CB   1 
ATOM   1975 C CG   . HIS   A 1 91  ? 31.937 -4.281  13.371  1.00 20.42 ?  91  HIS   A CG   1 
ATOM   1976 N ND1  . HIS   A 1 91  ? 33.210 -3.766  13.473  1.00 22.49 ?  91  HIS   A ND1  1 
ATOM   1977 C CD2  . HIS   A 1 91  ? 31.859 -5.275  14.286  1.00 22.25 ?  91  HIS   A CD2  1 
ATOM   1978 C CE1  . HIS   A 1 91  ? 33.875 -4.420  14.409  1.00 23.35 ?  91  HIS   A CE1  1 
ATOM   1979 N NE2  . HIS   A 1 91  ? 33.076 -5.340  14.921  1.00 23.65 ?  91  HIS   A NE2  1 
ATOM   1980 H H    . HIS   A 1 91  ? 29.104 -2.986  14.190  1.00 16.80 ?  91  HIS   A H    1 
ATOM   1981 H HA   . HIS   A 1 91  ? 31.014 -1.725  12.714  1.00 16.12 ?  91  HIS   A HA   1 
ATOM   1982 H HB2  . HIS   A 1 91  ? 30.219 -4.420  12.333  1.00 19.34 ?  91  HIS   A HB2  1 
ATOM   1983 H HB3  . HIS   A 1 91  ? 31.373 -3.679  11.534  1.00 19.34 ?  91  HIS   A HB3  1 
ATOM   1984 H HD1  . HIS   A 1 91  ? 33.527 -3.122  12.997  1.00 26.97 ?  91  HIS   A HD1  1 
ATOM   1985 H HD2  . HIS   A 1 91  ? 31.124 -5.815  14.457  1.00 26.67 ?  91  HIS   A HD2  1 
ATOM   1986 H HE1  . HIS   A 1 91  ? 34.758 -4.256  14.667  1.00 28.00 ?  91  HIS   A HE1  1 
ATOM   1987 N N    . CYS   A 1 92  ? 29.620 -1.519  10.659  1.00 11.55 ?  92  CYS   A N    1 
ATOM   1988 C CA   . CYS   A 1 92  ? 28.775 -1.442  9.476   1.00 11.71 ?  92  CYS   A CA   1 
ATOM   1989 C C    . CYS   A 1 92  ? 29.420 -2.254  8.364   1.00 11.11 ?  92  CYS   A C    1 
ATOM   1990 O O    . CYS   A 1 92  ? 30.574 -1.997  7.990   1.00 11.89 ?  92  CYS   A O    1 
ATOM   1991 C CB   . CYS   A 1 92  ? 28.554 0.001   9.020   1.00 11.97 ?  92  CYS   A CB   1 
ATOM   1992 S SG   . CYS   A 1 92  ? 27.522 0.113   7.530   1.00 11.64 ?  92  CYS   A SG   1 
ATOM   1993 H H    . CYS   A 1 92  ? 30.385 -1.132  10.566  1.00 13.84 ?  92  CYS   A H    1 
ATOM   1994 H HA   . CYS   A 1 92  ? 27.911 -1.828  9.680   1.00 14.03 ?  92  CYS   A HA   1 
ATOM   1995 H HB2  . CYS   A 1 92  ? 28.112 0.498   9.728   1.00 14.34 ?  92  CYS   A HB2  1 
ATOM   1996 H HB3  . CYS   A 1 92  ? 29.413 0.407   8.818   1.00 14.34 ?  92  CYS   A HB3  1 
ATOM   1997 H HG   . CYS   A 1 92  ? 27.379 1.267   7.234   1.00 13.94 ?  92  CYS   A HG   1 
ATOM   1998 N N    . LEU   A 1 93  ? 28.679 -3.236  7.856   1.00 10.65 ?  93  LEU   A N    1 
ATOM   1999 C CA   . LEU   A 1 93  ? 29.078 -3.989  6.675   1.00 10.32 ?  93  LEU   A CA   1 
ATOM   2000 C C    . LEU   A 1 93  ? 28.472 -3.296  5.462   1.00 10.21 ?  93  LEU   A C    1 
ATOM   2001 O O    . LEU   A 1 93  ? 27.255 -3.359  5.250   1.00 10.32 ?  93  LEU   A O    1 
ATOM   2002 C CB   . LEU   A 1 93  ? 28.599 -5.434  6.776   1.00 11.03 ?  93  LEU   A CB   1 
ATOM   2003 C CG   . LEU   A 1 93  ? 28.981 -6.329  5.599   1.00 11.19 ?  93  LEU   A CG   1 
ATOM   2004 C CD1  . LEU   A 1 93  ? 30.487 -6.579  5.558   1.00 12.11 ?  93  LEU   A CD1  1 
ATOM   2005 C CD2  . LEU   A 1 93  ? 28.220 -7.663  5.634   1.00 11.87 ?  93  LEU   A CD2  1 
ATOM   2006 H H    . LEU   A 1 93  ? 27.923 -3.487  8.196   1.00 12.76 ?  93  LEU   A H    1 
ATOM   2007 H HA   . LEU   A 1 93  ? 30.039 -3.977  6.598   1.00 12.36 ?  93  LEU   A HA   1 
ATOM   2008 H HB2  . LEU   A 1 93  ? 28.979 -5.828  7.578   1.00 13.21 ?  93  LEU   A HB2  1 
ATOM   2009 H HB3  . LEU   A 1 93  ? 27.632 -5.436  6.842   1.00 13.21 ?  93  LEU   A HB3  1 
ATOM   2010 H HG   . LEU   A 1 93  ? 28.740 -5.883  4.778   1.00 13.40 ?  93  LEU   A HG   1 
ATOM   2011 H HD11 . LEU   A 1 93  ? 30.693 -7.188  4.831   1.00 14.51 ?  93  LEU   A HD11 1 
ATOM   2012 H HD12 . LEU   A 1 93  ? 30.948 -5.735  5.420   1.00 14.51 ?  93  LEU   A HD12 1 
ATOM   2013 H HD13 . LEU   A 1 93  ? 30.772 -6.971  6.403   1.00 14.51 ?  93  LEU   A HD13 1 
ATOM   2014 H HD21 . LEU   A 1 93  ? 28.495 -8.203  4.872   1.00 14.22 ?  93  LEU   A HD21 1 
ATOM   2015 H HD22 . LEU   A 1 93  ? 28.430 -8.130  6.458   1.00 14.22 ?  93  LEU   A HD22 1 
ATOM   2016 H HD23 . LEU   A 1 93  ? 27.269 -7.487  5.585   1.00 14.22 ?  93  LEU   A HD23 1 
ATOM   2017 N N    . HIS   A 1 94  ? 29.313 -2.595  4.699   1.00 9.95  ?  94  HIS   A N    1 
ATOM   2018 C CA   . HIS   A 1 94  ? 28.880 -1.922  3.479   1.00 10.29 ?  94  HIS   A CA   1 
ATOM   2019 C C    . HIS   A 1 94  ? 28.881 -2.949  2.364   1.00 10.22 ?  94  HIS   A C    1 
ATOM   2020 O O    . HIS   A 1 94  ? 29.947 -3.457  2.006   1.00 11.21 ?  94  HIS   A O    1 
ATOM   2021 C CB   . HIS   A 1 94  ? 29.825 -0.768  3.146   1.00 10.35 ?  94  HIS   A CB   1 
ATOM   2022 C CG   . HIS   A 1 94  ? 29.814 0.316   4.166   1.00 10.04 ?  94  HIS   A CG   1 
ATOM   2023 N ND1  . HIS   A 1 94  ? 28.938 1.380   4.116   1.00 10.29 ?  94  HIS   A ND1  1 
ATOM   2024 C CD2  . HIS   A 1 94  ? 30.553 0.475   5.285   1.00 10.67 ?  94  HIS   A CD2  1 
ATOM   2025 C CE1  . HIS   A 1 94  ? 29.150 2.154   5.163   1.00 10.24 ?  94  HIS   A CE1  1 
ATOM   2026 N NE2  . HIS   A 1 94  ? 30.127 1.632   5.885   1.00 10.56 ?  94  HIS   A NE2  1 
ATOM   2027 H H    . HIS   A 1 94  ? 30.156 -2.502  4.869   1.00 11.92 ?  94  HIS   A H    1 
ATOM   2028 H HA   . HIS   A 1 94  ? 27.982 -1.579  3.593   1.00 12.33 ?  94  HIS   A HA   1 
ATOM   2029 H HB2  . HIS   A 1 94  ? 30.727 -1.109  3.085   1.00 12.40 ?  94  HIS   A HB2  1 
ATOM   2030 H HB3  . HIS   A 1 94  ? 29.555 -0.381  2.299   1.00 12.40 ?  94  HIS   A HB3  1 
ATOM   2031 H HD2  . HIS   A 1 94  ? 31.226 -0.082  5.589   1.00 12.78 ?  94  HIS   A HD2  1 
ATOM   2032 H HE1  . HIS   A 1 94  ? 28.692 2.943   5.355   1.00 12.27 ?  94  HIS   A HE1  1 
ATOM   2033 H HE2  . HIS   A 1 94  ? 30.443 1.970   6.613   1.00 12.65 ?  94  HIS   A HE2  1 
ATOM   2034 N N    . VAL   A 1 95  ? 27.712 -3.267  1.820   1.00 9.47  ?  95  VAL   A N    1 
ATOM   2035 C CA   . VAL   A 1 95  ? 27.570 -4.301  0.796   1.00 9.79  ?  95  VAL   A CA   1 
ATOM   2036 C C    . VAL   A 1 95  ? 27.018 -3.661  -0.466  1.00 9.43  ?  95  VAL   A C    1 
ATOM   2037 O O    . VAL   A 1 95  ? 26.017 -2.938  -0.404  1.00 10.62 ?  95  VAL   A O    1 
ATOM   2038 C CB   . VAL   A 1 95  ? 26.651 -5.454  1.247   1.00 10.46 ?  95  VAL   A CB   1 
ATOM   2039 C CG1  . VAL   A 1 95  ? 26.560 -6.499  0.152   1.00 11.02 ?  95  VAL   A CG1  1 
ATOM   2040 C CG2  . VAL   A 1 95  ? 27.159 -6.062  2.535   1.00 10.52 ?  95  VAL   A CG2  1 
ATOM   2041 H H    . VAL   A 1 95  ? 26.966 -2.888  2.029   1.00 11.35 ?  95  VAL   A H    1 
ATOM   2042 H HA   . VAL   A 1 95  ? 28.444 -4.670  0.592   1.00 11.73 ?  95  VAL   A HA   1 
ATOM   2043 H HB   . VAL   A 1 95  ? 25.765 -5.105  1.409   1.00 12.53 ?  95  VAL   A HB   1 
ATOM   2044 H HG11 . VAL   A 1 95  ? 26.166 -7.307  0.519   1.00 13.20 ?  95  VAL   A HG11 1 
ATOM   2045 H HG12 . VAL   A 1 95  ? 26.008 -6.162  -0.569  1.00 13.20 ?  95  VAL   A HG12 1 
ATOM   2046 H HG13 . VAL   A 1 95  ? 27.454 -6.695  -0.178  1.00 13.20 ?  95  VAL   A HG13 1 
ATOM   2047 H HG21 . VAL   A 1 95  ? 26.608 -6.825  2.761   1.00 12.60 ?  95  VAL   A HG21 1 
ATOM   2048 H HG22 . VAL   A 1 95  ? 28.080 -6.338  2.415   1.00 12.60 ?  95  VAL   A HG22 1 
ATOM   2049 H HG23 . VAL   A 1 95  ? 27.104 -5.394  3.240   1.00 12.60 ?  95  VAL   A HG23 1 
ATOM   2050 N N    . VAL   A 1 96  ? 27.639 -3.946  -1.607  1.00 9.73  ?  96  VAL   A N    1 
ATOM   2051 C CA   . VAL   A 1 96  ? 27.231 -3.387  -2.887  1.00 10.37 ?  96  VAL   A CA   1 
ATOM   2052 C C    . VAL   A 1 96  ? 26.434 -4.430  -3.659  1.00 10.74 ?  96  VAL   A C    1 
ATOM   2053 O O    . VAL   A 1 96  ? 26.999 -5.364  -4.236  1.00 11.68 ?  96  VAL   A O    1 
ATOM   2054 C CB   . VAL   A 1 96  ? 28.427 -2.905  -3.709  1.00 10.97 ?  96  VAL   A CB   1 
ATOM   2055 C CG1  . VAL   A 1 96  ? 27.919 -2.274  -4.984  1.00 10.68 ?  96  VAL   A CG1  1 
ATOM   2056 C CG2  . VAL   A 1 96  ? 29.290 -1.937  -2.908  1.00 11.77 ?  96  VAL   A CG2  1 
ATOM   2057 H H    . VAL   A 1 96  ? 28.325 -4.470  -1.661  1.00 11.65 ?  96  VAL   A H    1 
ATOM   2058 H HA   . VAL   A 1 96  ? 26.654 -2.627  -2.728  1.00 12.43 ?  96  VAL   A HA   1 
ATOM   2059 H HB   . VAL   A 1 96  ? 28.976 -3.666  -3.947  1.00 13.14 ?  96  VAL   A HB   1 
ATOM   2060 H HG11 . VAL   A 1 96  ? 28.647 -1.775  -5.396  1.00 12.79 ?  96  VAL   A HG11 1 
ATOM   2061 H HG12 . VAL   A 1 96  ? 27.617 -2.968  -5.587  1.00 12.79 ?  96  VAL   A HG12 1 
ATOM   2062 H HG13 . VAL   A 1 96  ? 27.191 -1.670  -4.773  1.00 12.79 ?  96  VAL   A HG13 1 
ATOM   2063 H HG21 . VAL   A 1 96  ? 29.994 -1.592  -3.476  1.00 14.10 ?  96  VAL   A HG21 1 
ATOM   2064 H HG22 . VAL   A 1 96  ? 28.734 -1.203  -2.590  1.00 14.10 ?  96  VAL   A HG22 1 
ATOM   2065 H HG23 . VAL   A 1 96  ? 29.675 -2.405  -2.149  1.00 14.10 ?  96  VAL   A HG23 1 
ATOM   2066 N N    A GLY   A 1 97  ? 25.114 -4.301  -3.622  0.60 10.76 ?  97  GLY   A N    1 
ATOM   2067 N N    B GLY   A 1 97  ? 25.117 -4.255  -3.731  0.40 11.27 ?  97  GLY   A N    1 
ATOM   2068 C CA   A GLY   A 1 97  ? 24.274 -5.031  -4.531  0.60 11.16 ?  97  GLY   A CA   1 
ATOM   2069 C CA   B GLY   A 1 97  ? 24.315 -5.047  -4.634  0.40 11.74 ?  97  GLY   A CA   1 
ATOM   2070 C C    A GLY   A 1 97  ? 24.271 -4.336  -5.875  0.60 10.90 ?  97  GLY   A C    1 
ATOM   2071 C C    B GLY   A 1 97  ? 24.357 -4.485  -6.044  0.40 12.29 ?  97  GLY   A C    1 
ATOM   2072 O O    A GLY   A 1 97  ? 24.536 -3.134  -5.968  0.60 11.78 ?  97  GLY   A O    1 
ATOM   2073 O O    B GLY   A 1 97  ? 24.669 -3.308  -6.251  0.40 12.72 ?  97  GLY   A O    1 
ATOM   2074 H H    A GLY   A 1 97  ? 24.683 -3.784  -3.076  0.60 12.89 ?  97  GLY   A H    1 
ATOM   2075 H H    B GLY   A 1 97  ? 24.666 -3.685  -3.260  0.40 13.50 ?  97  GLY   A H    1 
ATOM   2076 H HA2  A GLY   A 1 97  ? 24.614 -5.929  -4.633  0.60 13.36 ?  97  GLY   A HA2  1 
ATOM   2077 H HA2  B GLY   A 1 97  ? 24.653 -5.957  -4.644  0.40 14.07 ?  97  GLY   A HA2  1 
ATOM   2078 H HA3  A GLY   A 1 97  ? 23.365 -5.069  -4.188  0.60 13.36 ?  97  GLY   A HA3  1 
ATOM   2079 H HA3  B GLY   A 1 97  ? 23.394 -5.066  -4.325  0.40 14.07 ?  97  GLY   A HA3  1 
ATOM   2080 N N    A PRO   A 1 98  ? 23.966 -5.066  -6.943  0.60 10.79 ?  98  PRO   A N    1 
ATOM   2081 N N    B PRO   A 1 98  ? 24.046 -5.310  -7.046  0.40 13.16 ?  98  PRO   A N    1 
ATOM   2082 C CA   A PRO   A 1 98  ? 23.862 -4.427  -8.258  0.60 11.18 ?  98  PRO   A CA   1 
ATOM   2083 C CA   B PRO   A 1 98  ? 24.030 -4.810  -8.427  0.40 14.14 ?  98  PRO   A CA   1 
ATOM   2084 C C    A PRO   A 1 98  ? 22.740 -3.402  -8.290  0.60 11.01 ?  98  PRO   A C    1 
ATOM   2085 C C    B PRO   A 1 98  ? 22.930 -3.785  -8.656  0.40 15.04 ?  98  PRO   A C    1 
ATOM   2086 O O    A PRO   A 1 98  ? 21.672 -3.597  -7.704  0.60 11.29 ?  98  PRO   A O    1 
ATOM   2087 O O    B PRO   A 1 98  ? 21.831 -3.879  -8.105  0.40 15.11 ?  98  PRO   A O    1 
ATOM   2088 C CB   A PRO   A 1 98  ? 23.569 -5.601  -9.196  0.60 11.64 ?  98  PRO   A CB   1 
ATOM   2089 C CB   B PRO   A 1 98  ? 23.792 -6.073  -9.265  0.40 13.88 ?  98  PRO   A CB   1 
ATOM   2090 C CG   A PRO   A 1 98  ? 22.922 -6.629  -8.317  0.60 11.74 ?  98  PRO   A CG   1 
ATOM   2091 C CG   B PRO   A 1 98  ? 23.164 -7.045  -8.326  0.40 13.86 ?  98  PRO   A CG   1 
ATOM   2092 C CD   A PRO   A 1 98  ? 23.632 -6.500  -6.995  0.60 11.26 ?  98  PRO   A CD   1 
ATOM   2093 C CD   B PRO   A 1 98  ? 23.783 -6.758  -6.987  0.40 13.25 ?  98  PRO   A CD   1 
ATOM   2094 H HA   A PRO   A 1 98  ? 24.702 -4.007  -8.495  0.60 13.39 ?  98  PRO   A HA   1 
ATOM   2095 H HA   B PRO   A 1 98  ? 24.887 -4.421  -8.657  0.40 16.94 ?  98  PRO   A HA   1 
ATOM   2096 H HB2  A PRO   A 1 98  ? 22.962 -5.315  -9.893  0.60 13.94 ?  98  PRO   A HB2  1 
ATOM   2097 H HB2  B PRO   A 1 98  ? 23.193 -5.865  -10.001 0.40 16.63 ?  98  PRO   A HB2  1 
ATOM   2098 H HB3  A PRO   A 1 98  ? 24.397 -5.935  -9.565  0.60 13.94 ?  98  PRO   A HB3  1 
ATOM   2099 H HB3  B PRO   A 1 98  ? 24.639 -6.408  -9.596  0.40 16.63 ?  98  PRO   A HB3  1 
ATOM   2100 H HG2  A PRO   A 1 98  ? 21.978 -6.433  -8.220  0.60 14.06 ?  98  PRO   A HG2  1 
ATOM   2101 H HG2  B PRO   A 1 98  ? 22.205 -6.898  -8.299  0.40 16.61 ?  98  PRO   A HG2  1 
ATOM   2102 H HG3  A PRO   A 1 98  ? 23.057 -7.511  -8.691  0.60 14.06 ?  98  PRO   A HG3  1 
ATOM   2103 H HG3  B PRO   A 1 98  ? 23.364 -7.949  -8.613  0.40 16.61 ?  98  PRO   A HG3  1 
ATOM   2104 H HD2  A PRO   A 1 98  ? 23.037 -6.744  -6.263  0.60 13.49 ?  98  PRO   A HD2  1 
ATOM   2105 H HD2  B PRO   A 1 98  ? 23.157 -6.963  -6.274  0.40 15.88 ?  98  PRO   A HD2  1 
ATOM   2106 H HD3  A PRO   A 1 98  ? 24.442 -7.031  -6.984  0.60 13.49 ?  98  PRO   A HD3  1 
ATOM   2107 H HD3  B PRO   A 1 98  ? 24.612 -7.253  -6.885  0.40 15.88 ?  98  PRO   A HD3  1 
ATOM   2108 N N    A ASN   A 1 99  ? 22.994 -2.304  -8.991  0.60 11.60 ?  99  ASN   A N    1 
ATOM   2109 N N    B ASN   A 1 99  ? 23.239 -2.804  -9.494  0.40 16.03 ?  99  ASN   A N    1 
ATOM   2110 C CA   A ASN   A 1 99  ? 22.012 -1.247  -9.201  0.60 12.84 ?  99  ASN   A CA   1 
ATOM   2111 C CA   B ASN   A 1 99  ? 22.309 -1.748  -9.881  0.40 17.72 ?  99  ASN   A CA   1 
ATOM   2112 C C    A ASN   A 1 99  ? 21.467 -1.396  -10.618 0.60 13.84 ?  99  ASN   A C    1 
ATOM   2113 C C    B ASN   A 1 99  ? 21.860 -2.053  -11.306 0.40 18.87 ?  99  ASN   A C    1 
ATOM   2114 O O    A ASN   A 1 99  ? 22.164 -1.094  -11.593 0.60 15.24 ?  99  ASN   A O    1 
ATOM   2115 O O    B ASN   A 1 99  ? 22.605 -1.822  -12.261 0.40 18.55 ?  99  ASN   A O    1 
ATOM   2116 C CB   A ASN   A 1 99  ? 22.652 0.126   -8.989  0.60 13.04 ?  99  ASN   A CB   1 
ATOM   2117 C CB   B ASN   A 1 99  ? 23.001 -0.392  -9.802  0.40 18.62 ?  99  ASN   A CB   1 
ATOM   2118 C CG   A ASN   A 1 99  ? 21.635 1.260   -8.988  0.60 13.88 ?  99  ASN   A CG   1 
ATOM   2119 C CG   B ASN   A 1 99  ? 22.080 0.757   -10.149 0.40 19.66 ?  99  ASN   A CG   1 
ATOM   2120 O OD1  A ASN   A 1 99  ? 20.637 1.212   -9.700  0.60 14.52 ?  99  ASN   A OD1  1 
ATOM   2121 O OD1  B ASN   A 1 99  ? 20.958 0.553   -10.609 0.40 19.83 ?  99  ASN   A OD1  1 
ATOM   2122 N ND2  A ASN   A 1 99  ? 21.895 2.288   -8.193  0.60 14.54 ?  99  ASN   A ND2  1 
ATOM   2123 N ND2  B ASN   A 1 99  ? 22.555 1.976   -9.938  0.40 20.52 ?  99  ASN   A ND2  1 
ATOM   2124 H H    A ASN   A 1 99  ? 23.755 -2.144  -9.357  0.60 13.90 ?  99  ASN   A H    1 
ATOM   2125 H H    B ASN   A 1 99  ? 24.011 -2.730  -9.863  0.40 19.21 ?  99  ASN   A H    1 
ATOM   2126 H HA   A ASN   A 1 99  ? 21.283 -1.350  -8.566  0.60 15.38 ?  99  ASN   A HA   1 
ATOM   2127 H HA   B ASN   A 1 99  ? 21.533 -1.753  -9.299  0.40 21.24 ?  99  ASN   A HA   1 
ATOM   2128 H HB2  A ASN   A 1 99  ? 23.115 0.135   -8.136  0.60 15.62 ?  99  ASN   A HB2  1 
ATOM   2129 H HB2  B ASN   A 1 99  ? 23.323 -0.258  -8.899  0.40 22.32 ?  99  ASN   A HB2  1 
ATOM   2130 H HB3  A ASN   A 1 99  ? 23.284 0.291   -9.708  0.60 15.62 ?  99  ASN   A HB3  1 
ATOM   2131 H HB3  B ASN   A 1 99  ? 23.743 -0.383  -10.427 0.40 22.32 ?  99  ASN   A HB3  1 
ATOM   2132 H HD21 A ASN   A 1 99  ? 21.349 2.950   -8.156  0.60 17.43 ?  99  ASN   A HD21 1 
ATOM   2133 H HD21 B ASN   A 1 99  ? 22.072 2.664   -10.123 0.40 24.59 ?  99  ASN   A HD21 1 
ATOM   2134 H HD22 A ASN   A 1 99  ? 22.607 2.288   -7.713  0.60 17.43 ?  99  ASN   A HD22 1 
ATOM   2135 H HD22 B ASN   A 1 99  ? 23.346 2.078   -9.621  0.40 24.59 ?  99  ASN   A HD22 1 
ATOM   2136 N N    A VAL   A 1 100 ? 20.221 -1.871  -10.720 0.60 14.25 ?  100 VAL   A N    1 
ATOM   2137 N N    B VAL   A 1 100 ? 20.640 -2.578  -11.448 0.40 21.23 ?  100 VAL   A N    1 
ATOM   2138 C CA   A VAL   A 1 100 ? 19.591 -2.082  -12.020 0.60 16.10 ?  100 VAL   A CA   1 
ATOM   2139 C CA   B VAL   A 1 100 ? 20.150 -2.956  -12.769 0.40 23.52 ?  100 VAL   A CA   1 
ATOM   2140 C C    A VAL   A 1 100 ? 19.487 -0.772  -12.791 0.60 15.94 ?  100 VAL   A C    1 
ATOM   2141 C C    B VAL   A 1 100 ? 19.899 -1.740  -13.645 0.40 24.66 ?  100 VAL   A C    1 
ATOM   2142 O O    A VAL   A 1 100 ? 19.544 -0.762  -14.026 0.60 17.17 ?  100 VAL   A O    1 
ATOM   2143 O O    B VAL   A 1 100 ? 19.882 -1.862  -14.875 0.40 24.85 ?  100 VAL   A O    1 
ATOM   2144 C CB   A VAL   A 1 100 ? 18.223 -2.777  -11.836 0.60 18.76 ?  100 VAL   A CB   1 
ATOM   2145 C CB   B VAL   A 1 100 ? 18.892 -3.834  -12.662 0.40 24.72 ?  100 VAL   A CB   1 
ATOM   2146 C CG1  A VAL   A 1 100 ? 17.540 -3.002  -13.176 0.60 19.68 ?  100 VAL   A CG1  1 
ATOM   2147 C CG1  B VAL   A 1 100 ? 18.351 -4.164  -14.053 0.40 24.98 ?  100 VAL   A CG1  1 
ATOM   2148 C CG2  A VAL   A 1 100 ? 18.395 -4.101  -11.100 0.60 19.71 ?  100 VAL   A CG2  1 
ATOM   2149 C CG2  B VAL   A 1 100 ? 19.214 -5.099  -11.899 0.40 25.27 ?  100 VAL   A CG2  1 
ATOM   2150 H H    A VAL   A 1 100 ? 19.724 -2.080  -10.043 0.60 17.07 ?  100 VAL   A H    1 
ATOM   2151 H H    B VAL   A 1 100 ? 20.088 -2.719  -10.806 0.40 25.46 ?  100 VAL   A H    1 
ATOM   2152 H HA   A VAL   A 1 100 ? 20.149 -2.681  -12.534 0.60 19.29 ?  100 VAL   A HA   1 
ATOM   2153 H HA   B VAL   A 1 100 ? 20.835 -3.493  -13.202 0.40 28.20 ?  100 VAL   A HA   1 
ATOM   2154 H HB   A VAL   A 1 100 ? 17.649 -2.212  -11.297 0.60 22.49 ?  100 VAL   A HB   1 
ATOM   2155 H HB   B VAL   A 1 100 ? 18.205 -3.344  -12.182 0.40 29.64 ?  100 VAL   A HB   1 
ATOM   2156 H HG11 A VAL   A 1 100 ? 16.767 -3.574  -13.043 0.60 23.60 ?  100 VAL   A HG11 1 
ATOM   2157 H HG11 B VAL   A 1 100 ? 17.621 -4.795  -13.961 0.40 29.95 ?  100 VAL   A HG11 1 
ATOM   2158 H HG12 A VAL   A 1 100 ? 17.260 -2.147  -13.536 0.60 23.60 ?  100 VAL   A HG12 1 
ATOM   2159 H HG12 B VAL   A 1 100 ? 18.028 -3.353  -14.479 0.40 29.95 ?  100 VAL   A HG12 1 
ATOM   2160 H HG13 A VAL   A 1 100 ? 18.166 -3.430  -13.781 0.60 23.60 ?  100 VAL   A HG13 1 
ATOM   2161 H HG13 B VAL   A 1 100 ? 19.061 -4.557  -14.585 0.40 29.95 ?  100 VAL   A HG13 1 
ATOM   2162 H HG21 A VAL   A 1 100 ? 17.544 -4.567  -11.085 0.60 23.63 ?  100 VAL   A HG21 1 
ATOM   2163 H HG21 B VAL   A 1 100 ? 18.432 -5.670  -11.896 0.40 30.30 ?  100 VAL   A HG21 1 
ATOM   2164 H HG22 A VAL   A 1 100 ? 19.058 -4.636  -11.563 0.60 23.63 ?  100 VAL   A HG22 1 
ATOM   2165 H HG22 B VAL   A 1 100 ? 19.954 -5.549  -12.338 0.40 30.30 ?  100 VAL   A HG22 1 
ATOM   2166 H HG23 A VAL   A 1 100 ? 18.689 -3.924  -10.192 0.60 23.63 ?  100 VAL   A HG23 1 
ATOM   2167 H HG23 B VAL   A 1 100 ? 19.461 -4.864  -10.992 0.40 30.30 ?  100 VAL   A HG23 1 
ATOM   2168 N N    A ASN   A 1 101 ? 19.340 0.350   -12.088 0.60 16.87 ?  101 ASN   A N    1 
ATOM   2169 N N    B ASN   A 1 101 ? 19.706 -0.565  -13.048 0.40 25.62 ?  101 ASN   A N    1 
ATOM   2170 C CA   A ASN   A 1 101 ? 19.274 1.643   -12.762 0.60 18.08 ?  101 ASN   A CA   1 
ATOM   2171 C CA   B ASN   A 1 101 ? 19.642 0.681   -13.800 0.40 26.67 ?  101 ASN   A CA   1 
ATOM   2172 C C    A ASN   A 1 101 ? 20.625 2.097   -13.302 0.60 19.79 ?  101 ASN   A C    1 
ATOM   2173 C C    B ASN   A 1 101 ? 21.026 1.209   -14.150 0.40 27.07 ?  101 ASN   A C    1 
ATOM   2174 O O    A ASN   A 1 101 ? 20.692 3.165   -13.925 0.60 21.32 ?  101 ASN   A O    1 
ATOM   2175 O O    B ASN   A 1 101 ? 21.194 2.413   -14.386 0.40 27.47 ?  101 ASN   A O    1 
ATOM   2176 C CB   A ASN   A 1 101 ? 18.661 2.682   -11.824 0.60 17.97 ?  101 ASN   A CB   1 
ATOM   2177 C CB   B ASN   A 1 101 ? 18.820 1.716   -13.028 0.40 27.43 ?  101 ASN   A CB   1 
ATOM   2178 C CG   A ASN   A 1 101 ? 17.291 2.265   -11.327 0.60 18.26 ?  101 ASN   A CG   1 
ATOM   2179 C CG   B ASN   A 1 101 ? 17.381 1.277   -12.831 0.40 28.24 ?  101 ASN   A CG   1 
ATOM   2180 O OD1  A ASN   A 1 101 ? 16.460 1.769   -12.099 0.60 19.02 ?  101 ASN   A OD1  1 
ATOM   2181 O OD1  B ASN   A 1 101 ? 16.828 0.547   -13.653 0.40 28.56 ?  101 ASN   A OD1  1 
ATOM   2182 N ND2  A ASN   A 1 101 ? 17.049 2.444   -10.034 0.60 18.25 ?  101 ASN   A ND2  1 
ATOM   2183 N ND2  B ASN   A 1 101 ? 16.768 1.715   -11.740 0.40 28.58 ?  101 ASN   A ND2  1 
ATOM   2184 H H    A ASN   A 1 101 ? 19.270 0.386   -11.233 0.60 20.22 ?  101 ASN   A H    1 
ATOM   2185 H H    B ASN   A 1 101 ? 19.618 -0.461  -12.198 0.40 30.72 ?  101 ASN   A H    1 
ATOM   2186 H HA   A ASN   A 1 101 ? 18.678 1.555   -13.518 0.60 21.67 ?  101 ASN   A HA   1 
ATOM   2187 H HA   B ASN   A 1 101 ? 19.187 0.517   -14.641 0.40 31.98 ?  101 ASN   A HA   1 
ATOM   2188 H HB2  A ASN   A 1 101 ? 19.242 2.803   -11.057 0.60 21.54 ?  101 ASN   A HB2  1 
ATOM   2189 H HB2  B ASN   A 1 101 ? 19.215 1.846   -12.151 0.40 32.89 ?  101 ASN   A HB2  1 
ATOM   2190 H HB3  A ASN   A 1 101 ? 18.566 3.521   -12.305 0.60 21.54 ?  101 ASN   A HB3  1 
ATOM   2191 H HB3  B ASN   A 1 101 ? 18.812 2.553   -13.518 0.40 32.89 ?  101 ASN   A HB3  1 
ATOM   2192 H HD21 A ASN   A 1 101 ? 16.287 2.221   -9.705  0.60 21.88 ?  101 ASN   A HD21 1 
ATOM   2193 H HD21 B ASN   A 1 101 ? 15.951 1.490   -11.587 0.40 34.27 ?  101 ASN   A HD21 1 
ATOM   2194 H HD22 A ASN   A 1 101 ? 17.651 2.791   -9.527  0.60 21.88 ?  101 ASN   A HD22 1 
ATOM   2195 H HD22 B ASN   A 1 101 ? 17.184 2.224   -11.188 0.40 34.27 ?  101 ASN   A HD22 1 
ATOM   2196 N N    A LYS   A 1 102 ? 21.688 1.316   -13.083 0.60 21.27 ?  102 LYS   A N    1 
ATOM   2197 N N    B LYS   A 1 102 ? 22.013 0.310   -14.187 0.40 27.25 ?  102 LYS   A N    1 
ATOM   2198 C CA   A LYS   A 1 102 ? 22.967 1.491   -13.758 0.60 22.85 ?  102 LYS   A CA   1 
ATOM   2199 C CA   B LYS   A 1 102 ? 23.378 0.651   -14.558 0.40 27.48 ?  102 LYS   A CA   1 
ATOM   2200 C C    A LYS   A 1 102 ? 23.251 0.389   -14.770 0.60 23.64 ?  102 LYS   A C    1 
ATOM   2201 C C    B LYS   A 1 102 ? 24.012 -0.423  -15.436 0.40 26.77 ?  102 LYS   A C    1 
ATOM   2202 O O    A LYS   A 1 102 ? 24.322 0.399   -15.386 0.60 24.61 ?  102 LYS   A O    1 
ATOM   2203 O O    B LYS   A 1 102 ? 25.221 -0.354  -15.693 0.40 27.12 ?  102 LYS   A O    1 
ATOM   2204 C CB   A LYS   A 1 102 ? 24.114 1.538   -12.738 0.60 23.52 ?  102 LYS   A CB   1 
ATOM   2205 C CB   B LYS   A 1 102 ? 24.245 0.834   -13.310 0.40 28.48 ?  102 LYS   A CB   1 
ATOM   2206 C CG   A LYS   A 1 102 ? 23.994 2.635   -11.698 0.60 23.96 ?  102 LYS   A CG   1 
ATOM   2207 C CG   B LYS   A 1 102 ? 24.956 2.170   -13.237 0.40 29.45 ?  102 LYS   A CG   1 
ATOM   2208 C CD   A LYS   A 1 102 ? 25.166 2.595   -10.728 0.60 24.73 ?  102 LYS   A CD   1 
ATOM   2209 C CD   B LYS   A 1 102 ? 26.194 2.080   -12.361 0.40 30.29 ?  102 LYS   A CD   1 
ATOM   2210 C CE   A LYS   A 1 102 ? 25.064 3.688   -9.675  0.60 25.43 ?  102 LYS   A CE   1 
ATOM   2211 C CE   B LYS   A 1 102 ? 27.326 2.915   -12.934 0.40 30.96 ?  102 LYS   A CE   1 
ATOM   2212 N NZ   A LYS   A 1 102 ? 26.182 3.610   -8.688  0.60 25.81 ?  102 LYS   A NZ   1 
ATOM   2213 N NZ   B LYS   A 1 102 ? 28.625 2.640   -12.263 0.40 31.45 ?  102 LYS   A NZ   1 
ATOM   2214 H H    A LYS   A 1 102 ? 21.691 0.658   -12.527 0.60 25.50 ?  102 LYS   A H    1 
ATOM   2215 H H    B LYS   A 1 102 ? 21.913 -0.521  -14.001 0.40 32.68 ?  102 LYS   A H    1 
ATOM   2216 H HA   A LYS   A 1 102 ? 22.960 2.330   -14.236 0.60 27.40 ?  102 LYS   A HA   1 
ATOM   2217 H HA   B LYS   A 1 102 ? 23.364 1.489   -15.041 0.40 32.95 ?  102 LYS   A HA   1 
ATOM   2218 H HB2  A LYS   A 1 102 ? 24.146 0.690   -12.269 0.60 28.20 ?  102 LYS   A HB2  1 
ATOM   2219 H HB2  B LYS   A 1 102 ? 23.686 0.752   -12.524 0.40 34.15 ?  102 LYS   A HB2  1 
ATOM   2220 H HB3  A LYS   A 1 102 ? 24.947 1.676   -13.217 0.60 28.20 ?  102 LYS   A HB3  1 
ATOM   2221 H HB3  B LYS   A 1 102 ? 24.920 0.136   -13.307 0.40 34.15 ?  102 LYS   A HB3  1 
ATOM   2222 H HG2  A LYS   A 1 102 ? 23.991 3.498   -12.142 0.60 28.73 ?  102 LYS   A HG2  1 
ATOM   2223 H HG2  B LYS   A 1 102 ? 25.227 2.442   -14.128 0.40 35.31 ?  102 LYS   A HG2  1 
ATOM   2224 H HG3  A LYS   A 1 102 ? 23.174 2.512   -11.195 0.60 28.73 ?  102 LYS   A HG3  1 
ATOM   2225 H HG3  B LYS   A 1 102 ? 24.357 2.831   -12.852 0.40 35.31 ?  102 LYS   A HG3  1 
ATOM   2226 H HD2  A LYS   A 1 102 ? 25.176 1.737   -10.276 0.60 29.66 ?  102 LYS   A HD2  1 
ATOM   2227 H HD2  B LYS   A 1 102 ? 25.982 2.416   -11.476 0.40 36.33 ?  102 LYS   A HD2  1 
ATOM   2228 H HD3  A LYS   A 1 102 ? 25.992 2.724   -11.221 0.60 29.66 ?  102 LYS   A HD3  1 
ATOM   2229 H HD3  B LYS   A 1 102 ? 26.493 1.158   -12.307 0.40 36.33 ?  102 LYS   A HD3  1 
ATOM   2230 H HE2  A LYS   A 1 102 ? 25.102 4.555   -10.110 0.60 30.49 ?  102 LYS   A HE2  1 
ATOM   2231 H HE2  B LYS   A 1 102 ? 27.425 2.711   -13.878 0.40 37.12 ?  102 LYS   A HE2  1 
ATOM   2232 H HE3  A LYS   A 1 102 ? 24.226 3.591   -9.195  0.60 30.49 ?  102 LYS   A HE3  1 
ATOM   2233 H HE3  B LYS   A 1 102 ? 27.115 3.854   -12.817 0.40 37.12 ?  102 LYS   A HE3  1 
ATOM   2234 H HZ1  A LYS   A 1 102 ? 26.099 4.257   -8.085  0.60 30.95 ?  102 LYS   A HZ1  1 
ATOM   2235 H HZ1  B LYS   A 1 102 ? 29.264 3.143   -12.623 0.40 37.72 ?  102 LYS   A HZ1  1 
ATOM   2236 H HZ2  A LYS   A 1 102 ? 26.165 2.822   -8.274  0.60 30.95 ?  102 LYS   A HZ2  1 
ATOM   2237 H HZ2  B LYS   A 1 102 ? 28.563 2.824   -11.395 0.40 37.72 ?  102 LYS   A HZ2  1 
ATOM   2238 H HZ3  A LYS   A 1 102 ? 26.962 3.700   -9.106  0.60 30.95 ?  102 LYS   A HZ3  1 
ATOM   2239 H HZ3  B LYS   A 1 102 ? 28.842 1.782   -12.363 0.40 37.72 ?  102 LYS   A HZ3  1 
ATOM   2240 N N    A GLY   A 1 103 ? 22.333 -0.560  -14.955 0.60 23.94 ?  103 GLY   A N    1 
ATOM   2241 N N    B GLY   A 1 103 ? 23.250 -1.419  -15.885 0.40 26.09 ?  103 GLY   A N    1 
ATOM   2242 C CA   A GLY   A 1 103 ? 22.546 -1.655  -15.881 0.60 24.41 ?  103 GLY   A CA   1 
ATOM   2243 C CA   B GLY   A 1 103 ? 23.803 -2.512  -16.656 0.40 25.49 ?  103 GLY   A CA   1 
ATOM   2244 C C    A GLY   A 1 103 ? 23.362 -2.801  -15.332 0.60 25.14 ?  103 GLY   A C    1 
ATOM   2245 C C    B GLY   A 1 103 ? 24.411 -3.620  -15.832 0.40 24.78 ?  103 GLY   A C    1 
ATOM   2246 O O    A GLY   A 1 103 ? 23.830 -3.640  -16.107 0.60 25.86 ?  103 GLY   A O    1 
ATOM   2247 O O    B GLY   A 1 103 ? 25.013 -4.537  -16.402 0.40 25.18 ?  103 GLY   A O    1 
ATOM   2248 H H    A GLY   A 1 103 ? 21.574 -0.591  -14.553 0.60 28.71 ?  103 GLY   A H    1 
ATOM   2249 H H    B GLY   A 1 103 ? 22.406 -1.483  -15.750 0.40 31.28 ?  103 GLY   A H    1 
ATOM   2250 H HA2  A GLY   A 1 103 ? 21.686 -2.013  -16.154 0.60 29.27 ?  103 GLY   A HA2  1 
ATOM   2251 H HA2  B GLY   A 1 103 ? 23.104 -2.903  -17.203 0.40 30.57 ?  103 GLY   A HA2  1 
ATOM   2252 H HA3  A GLY   A 1 103 ? 22.996 -1.319  -16.672 0.60 29.27 ?  103 GLY   A HA3  1 
ATOM   2253 H HA3  B GLY   A 1 103 ? 24.491 -2.164  -17.249 0.40 30.57 ?  103 GLY   A HA3  1 
ATOM   2254 N N    A GLU   A 1 104 ? 23.530 -2.877  -14.016 0.60 24.48 ?  104 GLU   A N    1 
ATOM   2255 N N    B GLU   A 1 104 ? 24.264 -3.574  -14.513 0.40 23.28 ?  104 GLU   A N    1 
ATOM   2256 C CA   A GLU   A 1 104 ? 24.405 -3.870  -13.412 0.60 24.02 ?  104 GLU   A CA   1 
ATOM   2257 C CA   B GLU   A 1 104 ? 24.916 -4.530  -13.631 0.40 21.76 ?  104 GLU   A CA   1 
ATOM   2258 C C    A GLU   A 1 104 ? 23.721 -5.233  -13.320 0.60 25.01 ?  104 GLU   A C    1 
ATOM   2259 C C    B GLU   A 1 104 ? 24.056 -5.780  -13.488 0.40 21.99 ?  104 GLU   A C    1 
ATOM   2260 O O    A GLU   A 1 104 ? 22.499 -5.338  -13.166 0.60 25.60 ?  104 GLU   A O    1 
ATOM   2261 O O    B GLU   A 1 104 ? 22.843 -5.694  -13.266 0.40 22.44 ?  104 GLU   A O    1 
ATOM   2262 C CB   A GLU   A 1 104 ? 24.892 -3.376  -12.045 0.60 22.87 ?  104 GLU   A CB   1 
ATOM   2263 C CB   B GLU   A 1 104 ? 25.203 -3.882  -12.275 0.40 20.55 ?  104 GLU   A CB   1 
ATOM   2264 C CG   A GLU   A 1 104 ? 25.829 -2.167  -12.189 0.60 22.53 ?  104 GLU   A CG   1 
ATOM   2265 C CG   B GLU   A 1 104 ? 26.039 -2.616  -12.428 0.40 20.04 ?  104 GLU   A CG   1 
ATOM   2266 C CD   A GLU   A 1 104 ? 26.145 -1.435  -10.899 0.60 21.74 ?  104 GLU   A CD   1 
ATOM   2267 C CD   B GLU   A 1 104 ? 26.385 -1.920  -11.129 0.40 19.50 ?  104 GLU   A CD   1 
ATOM   2268 O OE1  A GLU   A 1 104 ? 25.551 -1.747  -9.852  0.60 20.28 ?  104 GLU   A OE1  1 
ATOM   2269 O OE1  B GLU   A 1 104 ? 25.786 -2.233  -10.083 0.40 18.75 ?  104 GLU   A OE1  1 
ATOM   2270 O OE2  A GLU   A 1 104 ? 26.999 -0.522  -10.945 0.60 22.54 -1 104 GLU   A OE2  1 
ATOM   2271 O OE2  B GLU   A 1 104 ? 27.265 -1.033  -11.171 0.40 19.96 -1 104 GLU   A OE2  1 
ATOM   2272 H H    A GLU   A 1 104 ? 23.145 -2.361  -13.450 0.60 29.35 ?  104 GLU   A H    1 
ATOM   2273 H H    B GLU   A 1 104 ? 23.785 -2.988  -14.103 0.40 27.91 ?  104 GLU   A H    1 
ATOM   2274 H HA   A GLU   A 1 104 ? 25.185 -3.975  -13.977 0.60 28.80 ?  104 GLU   A HA   1 
ATOM   2275 H HA   B GLU   A 1 104 ? 25.763 -4.786  -14.025 0.40 26.08 ?  104 GLU   A HA   1 
ATOM   2276 H HB2  A GLU   A 1 104 ? 24.127 -3.113  -11.510 0.60 27.42 ?  104 GLU   A HB2  1 
ATOM   2277 H HB2  B GLU   A 1 104 ? 24.366 -3.645  -11.851 0.40 24.63 ?  104 GLU   A HB2  1 
ATOM   2278 H HB3  A GLU   A 1 104 ? 25.379 -4.091  -11.604 0.60 27.42 ?  104 GLU   A HB3  1 
ATOM   2279 H HB3  B GLU   A 1 104 ? 25.697 -4.509  -11.723 0.40 24.63 ?  104 GLU   A HB3  1 
ATOM   2280 H HG2  A GLU   A 1 104 ? 26.670 -2.471  -12.557 0.60 27.01 ?  104 GLU   A HG2  1 
ATOM   2281 H HG2  B GLU   A 1 104 ? 26.866 -2.845  -12.880 0.40 24.03 ?  104 GLU   A HG2  1 
ATOM   2282 H HG3  A GLU   A 1 104 ? 25.417 -1.527  -12.787 0.60 27.01 ?  104 GLU   A HG3  1 
ATOM   2283 H HG3  B GLU   A 1 104 ? 25.540 -1.977  -12.956 0.40 24.03 ?  104 GLU   A HG3  1 
ATOM   2284 N N    A ASP   A 1 105 ? 24.537 -6.282  -13.426 0.60 25.49 ?  105 ASP   A N    1 
ATOM   2285 N N    B ASP   A 1 105 ? 24.693 -6.937  -13.624 0.40 22.47 ?  105 ASP   A N    1 
ATOM   2286 C CA   A ASP   A 1 105 ? 24.046 -7.648  -13.558 0.60 26.16 ?  105 ASP   A CA   1 
ATOM   2287 C CA   B ASP   A 1 105 ? 23.977 -8.204  -13.698 0.40 23.20 ?  105 ASP   A CA   1 
ATOM   2288 C C    A ASP   A 1 105 ? 23.352 -8.102  -12.279 0.60 24.74 ?  105 ASP   A C    1 
ATOM   2289 C C    B ASP   A 1 105 ? 23.361 -8.542  -12.345 0.40 21.92 ?  105 ASP   A C    1 
ATOM   2290 O O    A ASP   A 1 105 ? 23.940 -8.058  -11.195 0.60 23.38 ?  105 ASP   A O    1 
ATOM   2291 O O    B ASP   A 1 105 ? 24.068 -8.649  -11.338 0.40 20.01 ?  105 ASP   A O    1 
ATOM   2292 C CB   A ASP   A 1 105 ? 25.228 -8.570  -13.857 0.60 28.03 ?  105 ASP   A CB   1 
ATOM   2293 C CB   B ASP   A 1 105 ? 24.942 -9.293  -14.155 0.40 25.03 ?  105 ASP   A CB   1 
ATOM   2294 C CG   A ASP   A 1 105 ? 24.798 -9.970  -14.226 0.60 29.78 ?  105 ASP   A CG   1 
ATOM   2295 C CG   B ASP   A 1 105 ? 24.481 -10.678 -13.798 0.40 26.41 ?  105 ASP   A CG   1 
ATOM   2296 O OD1  A ASP   A 1 105 ? 23.576 -10.203 -14.340 0.60 30.08 ?  105 ASP   A OD1  1 
ATOM   2297 O OD1  B ASP   A 1 105 ? 23.300 -11.007 -14.033 0.40 26.65 ?  105 ASP   A OD1  1 
ATOM   2298 O OD2  A ASP   A 1 105 ? 25.684 -10.832 -14.414 0.60 30.83 -1 105 ASP   A OD2  1 
ATOM   2299 O OD2  B ASP   A 1 105 ? 25.327 -11.446 -13.295 0.40 27.51 -1 105 ASP   A OD2  1 
ATOM   2300 H H    A ASP   A 1 105 ? 25.395 -6.227  -13.425 0.60 30.56 ?  105 ASP   A H    1 
ATOM   2301 H H    B ASP   A 1 105 ? 25.548 -7.012  -13.673 0.40 26.94 ?  105 ASP   A H    1 
ATOM   2302 H HA   A ASP   A 1 105 ? 23.417 -7.711  -14.294 0.60 31.37 ?  105 ASP   A HA   1 
ATOM   2303 H HA   B ASP   A 1 105 ? 23.263 -8.129  -14.349 0.40 27.82 ?  105 ASP   A HA   1 
ATOM   2304 H HB2  A ASP   A 1 105 ? 25.724 -8.221  -14.613 0.60 33.61 ?  105 ASP   A HB2  1 
ATOM   2305 H HB2  B ASP   A 1 105 ? 25.032 -9.251  -15.117 0.40 30.01 ?  105 ASP   A HB2  1 
ATOM   2306 H HB3  A ASP   A 1 105 ? 25.807 -8.611  -13.075 0.60 33.61 ?  105 ASP   A HB3  1 
ATOM   2307 H HB3  B ASP   A 1 105 ? 25.799 -9.156  -13.728 0.40 30.01 ?  105 ASP   A HB3  1 
ATOM   2308 N N    A ILE   A 1 106 ? 22.108 -8.573  -12.411 0.60 24.67 ?  106 ILE   A N    1 
ATOM   2309 N N    B ILE   A 1 106 ? 22.035 -8.701  -12.326 0.40 22.71 ?  106 ILE   A N    1 
ATOM   2310 C CA   A ILE   A 1 106 ? 21.342 -8.992  -11.242 0.60 24.06 ?  106 ILE   A CA   1 
ATOM   2311 C CA   B ILE   A 1 106 ? 21.325 -9.005  -11.090 0.40 23.28 ?  106 ILE   A CA   1 
ATOM   2312 C C    A ILE   A 1 106 ? 21.885 -10.278 -10.642 0.60 22.97 ?  106 ILE   A C    1 
ATOM   2313 C C    B ILE   A 1 106 ? 21.810 -10.308 -10.473 0.40 23.02 ?  106 ILE   A C    1 
ATOM   2314 O O    A ILE   A 1 106 ? 21.683 -10.529 -9.450  0.60 22.07 ?  106 ILE   A O    1 
ATOM   2315 O O    B ILE   A 1 106 ? 21.615 -10.530 -9.273  0.40 22.63 ?  106 ILE   A O    1 
ATOM   2316 C CB   A ILE   A 1 106 ? 19.839 -9.106  -11.575 0.60 25.39 ?  106 ILE   A CB   1 
ATOM   2317 C CB   B ILE   A 1 106 ? 19.796 -8.987  -11.329 0.40 24.65 ?  106 ILE   A CB   1 
ATOM   2318 C CG1  A ILE   A 1 106 ? 19.001 -9.175  -10.294 0.60 25.86 ?  106 ILE   A CG1  1 
ATOM   2319 C CG1  B ILE   A 1 106 ? 19.026 -9.064  -10.004 0.40 25.42 ?  106 ILE   A CG1  1 
ATOM   2320 C CG2  A ILE   A 1 106 ? 19.564 -10.334 -12.425 0.60 25.87 ?  106 ILE   A CG2  1 
ATOM   2321 C CG2  B ILE   A 1 106 ? 19.383 -10.119 -12.257 0.40 25.17 ?  106 ILE   A CG2  1 
ATOM   2322 C CD1  A ILE   A 1 106 ? 19.125 -7.951  -9.414  0.60 26.20 ?  106 ILE   A CD1  1 
ATOM   2323 C CD1  B ILE   A 1 106 ? 19.277 -7.890  -9.075  0.40 25.84 ?  106 ILE   A CD1  1 
ATOM   2324 H H    A ILE   A 1 106 ? 21.696 -8.666  -13.156 0.60 29.58 ?  106 ILE   A H    1 
ATOM   2325 H H    B ILE   A 1 106 ? 21.528 -8.627  -13.013 0.40 27.23 ?  106 ILE   A H    1 
ATOM   2326 H HA   A ILE   A 1 106 ? 21.439 -8.314  -10.565 0.60 28.85 ?  106 ILE   A HA   1 
ATOM   2327 H HA   B ILE   A 1 106 ? 21.524 -8.309  -10.452 0.40 27.91 ?  106 ILE   A HA   1 
ATOM   2328 H HB   A ILE   A 1 106 ? 19.573 -8.319  -12.075 0.60 30.44 ?  106 ILE   A HB   1 
ATOM   2329 H HB   B ILE   A 1 106 ? 19.569 -8.148  -11.759 0.40 29.56 ?  106 ILE   A HB   1 
ATOM   2330 H HG12 A ILE   A 1 106 ? 18.066 -9.267  -10.536 0.60 31.01 ?  106 ILE   A HG12 1 
ATOM   2331 H HG12 B ILE   A 1 106 ? 18.075 -9.084  -10.197 0.40 30.48 ?  106 ILE   A HG12 1 
ATOM   2332 H HG13 A ILE   A 1 106 ? 19.282 -9.943  -9.773  0.60 31.01 ?  106 ILE   A HG13 1 
ATOM   2333 H HG13 B ILE   A 1 106 ? 19.280 -9.873  -9.535  0.40 30.48 ?  106 ILE   A HG13 1 
ATOM   2334 H HG21 A ILE   A 1 106 ? 18.677 -10.256 -12.811 0.60 31.02 ?  106 ILE   A HG21 1 
ATOM   2335 H HG21 B ILE   A 1 106 ? 18.445 -10.015 -12.482 0.40 30.18 ?  106 ILE   A HG21 1 
ATOM   2336 H HG22 A ILE   A 1 106 ? 20.229 -10.383 -13.127 0.60 31.02 ?  106 ILE   A HG22 1 
ATOM   2337 H HG22 B ILE   A 1 106 ? 19.922 -10.077 -13.062 0.40 30.18 ?  106 ILE   A HG22 1 
ATOM   2338 H HG23 A ILE   A 1 106 ? 19.612 -11.124 -11.864 0.60 31.02 ?  106 ILE   A HG23 1 
ATOM   2339 H HG23 B ILE   A 1 106 ? 19.523 -10.966 -11.807 0.40 30.18 ?  106 ILE   A HG23 1 
ATOM   2340 H HD11 A ILE   A 1 106 ? 18.384 -7.934  -8.791  0.60 31.41 ?  106 ILE   A HD11 1 
ATOM   2341 H HD11 B ILE   A 1 106 ? 18.614 -7.902  -8.367  0.40 30.99 ?  106 ILE   A HD11 1 
ATOM   2342 H HD12 A ILE   A 1 106 ? 19.965 -7.994  -8.928  0.60 31.41 ?  106 ILE   A HD12 1 
ATOM   2343 H HD12 B ILE   A 1 106 ? 20.166 -7.971  -8.695  0.40 30.99 ?  106 ILE   A HD12 1 
ATOM   2344 H HD13 A ILE   A 1 106 ? 19.106 -7.158  -9.973  0.60 31.41 ?  106 ILE   A HD13 1 
ATOM   2345 H HD13 B ILE   A 1 106 ? 19.205 -7.066  -9.581  0.40 30.99 ?  106 ILE   A HD13 1 
ATOM   2346 N N    A GLN   A 1 107 ? 22.580 -11.099 -11.437 0.60 23.54 ?  107 GLN   A N    1 
ATOM   2347 N N    B GLN   A 1 107 ? 22.455 -11.176 -11.260 0.40 23.51 ?  107 GLN   A N    1 
ATOM   2348 C CA   A GLN   A 1 107 ? 23.186 -12.320 -10.916 0.60 24.85 ?  107 GLN   A CA   1 
ATOM   2349 C CA   B GLN   A 1 107 ? 23.057 -12.374 -10.686 0.40 24.09 ?  107 GLN   A CA   1 
ATOM   2350 C C    A GLN   A 1 107 ? 24.157 -12.025 -9.783  0.60 22.69 ?  107 GLN   A C    1 
ATOM   2351 C C    B GLN   A 1 107 ? 24.165 -12.034 -9.697  0.40 22.19 ?  107 GLN   A C    1 
ATOM   2352 O O    A GLN   A 1 107 ? 24.386 -12.889 -8.930  0.60 24.15 ?  107 GLN   A O    1 
ATOM   2353 O O    B GLN   A 1 107 ? 24.524 -12.881 -8.871  0.40 23.20 ?  107 GLN   A O    1 
ATOM   2354 C CB   A GLN   A 1 107 ? 23.900 -13.065 -12.050 0.60 27.97 ?  107 GLN   A CB   1 
ATOM   2355 C CB   B GLN   A 1 107 ? 23.567 -13.312 -11.786 0.40 26.37 ?  107 GLN   A CB   1 
ATOM   2356 C CG   A GLN   A 1 107 ? 23.036 -13.276 -13.290 0.60 31.13 ?  107 GLN   A CG   1 
ATOM   2357 C CG   B GLN   A 1 107 ? 22.481 -13.840 -12.712 0.40 28.47 ?  107 GLN   A CG   1 
ATOM   2358 C CD   A GLN   A 1 107 ? 21.766 -14.051 -12.993 0.60 33.76 ?  107 GLN   A CD   1 
ATOM   2359 C CD   B GLN   A 1 107 ? 21.594 -14.869 -12.040 0.40 30.29 ?  107 GLN   A CD   1 
ATOM   2360 O OE1  A GLN   A 1 107 ? 21.809 -15.140 -12.422 0.60 35.02 ?  107 GLN   A OE1  1 
ATOM   2361 O OE1  B GLN   A 1 107 ? 21.951 -15.431 -11.004 0.40 30.86 ?  107 GLN   A OE1  1 
ATOM   2362 N NE2  A GLN   A 1 107 ? 20.626 -13.487 -13.372 0.60 34.61 ?  107 GLN   A NE2  1 
ATOM   2363 N NE2  B GLN   A 1 107 ? 20.430 -15.123 -12.629 0.40 30.90 ?  107 GLN   A NE2  1 
ATOM   2364 H H    A GLN   A 1 107 ? 22.717 -10.968 -12.274 0.60 28.23 ?  107 GLN   A H    1 
ATOM   2365 H H    B GLN   A 1 107 ? 22.555 -11.095 -12.110 0.40 28.19 ?  107 GLN   A H    1 
ATOM   2366 H HA   A GLN   A 1 107 ? 22.494 -12.903 -10.570 0.60 29.80 ?  107 GLN   A HA   1 
ATOM   2367 H HA   B GLN   A 1 107 ? 22.375 -12.857 -10.201 0.40 28.88 ?  107 GLN   A HA   1 
ATOM   2368 H HB2  A GLN   A 1 107 ? 24.682 -12.559 -12.320 0.60 33.55 ?  107 GLN   A HB2  1 
ATOM   2369 H HB2  B GLN   A 1 107 ? 24.222 -12.864 -12.329 0.40 31.62 ?  107 GLN   A HB2  1 
ATOM   2370 H HB3  A GLN   A 1 107 ? 24.171 -13.942 -11.733 0.60 33.55 ?  107 GLN   A HB3  1 
ATOM   2371 H HB3  B GLN   A 1 107 ? 23.981 -14.077 -11.366 0.40 31.62 ?  107 GLN   A HB3  1 
ATOM   2372 H HG2  A GLN   A 1 107 ? 22.785 -12.414 -13.659 0.60 37.33 ?  107 GLN   A HG2  1 
ATOM   2373 H HG2  B GLN   A 1 107 ? 21.920 -13.103 -12.999 0.40 34.14 ?  107 GLN   A HG2  1 
ATOM   2374 H HG3  A GLN   A 1 107 ? 23.545 -13.777 -13.946 0.60 37.33 ?  107 GLN   A HG3  1 
ATOM   2375 H HG3  B GLN   A 1 107 ? 22.897 -14.259 -13.483 0.40 34.14 ?  107 GLN   A HG3  1 
ATOM   2376 H HE21 A GLN   A 1 107 ? 20.635 -12.724 -13.768 0.60 41.51 ?  107 GLN   A HE21 1 
ATOM   2377 H HE21 B GLN   A 1 107 ? 20.215 -14.710 -13.352 0.40 37.05 ?  107 GLN   A HE21 1 
ATOM   2378 H HE22 A GLN   A 1 107 ? 19.880 -13.887 -13.223 0.60 41.51 ?  107 GLN   A HE22 1 
ATOM   2379 H HE22 B GLN   A 1 107 ? 19.891 -15.701 -12.288 0.40 37.05 ?  107 GLN   A HE22 1 
ATOM   2380 N N    . LEU   A 1 108 ? 24.703 -10.810 -9.738  1.00 19.26 ?  108 LEU   A N    1 
ATOM   2381 C CA   . LEU   A 1 108 ? 25.636 -10.403 -8.699  1.00 15.84 ?  108 LEU   A CA   1 
ATOM   2382 C C    . LEU   A 1 108 ? 24.955 -10.235 -7.351  1.00 14.02 ?  108 LEU   A C    1 
ATOM   2383 O O    . LEU   A 1 108 ? 25.653 -10.085 -6.344  1.00 14.18 ?  108 LEU   A O    1 
ATOM   2384 C CB   . LEU   A 1 108 ? 26.358 -9.114  -9.103  1.00 15.63 ?  108 LEU   A CB   1 
ATOM   2385 C CG   . LEU   A 1 108 ? 27.379 -9.320  -10.223 1.00 17.51 ?  108 LEU   A CG   1 
ATOM   2386 C CD1  . LEU   A 1 108 ? 27.899 -7.994  -10.748 1.00 18.17 ?  108 LEU   A CD1  1 
ATOM   2387 C CD2  . LEU   A 1 108 ? 28.539 -10.190 -9.747  1.00 19.59 ?  108 LEU   A CD2  1 
ATOM   2388 H H    A LEU   A 1 108 ? 24.538 -10.193 -10.308 0.60 23.09 ?  108 LEU   A H    1 
ATOM   2389 H H    B LEU   A 1 108 ? 24.548 -10.220 -10.339 0.40 23.09 ?  108 LEU   A H    1 
ATOM   2390 H HA   . LEU   A 1 108 ? 26.300 -11.098 -8.590  1.00 18.98 ?  108 LEU   A HA   1 
ATOM   2391 H HB2  . LEU   A 1 108 ? 25.699 -8.473  -9.415  1.00 18.73 ?  108 LEU   A HB2  1 
ATOM   2392 H HB3  . LEU   A 1 108 ? 26.824 -8.761  -8.331  1.00 18.73 ?  108 LEU   A HB3  1 
ATOM   2393 H HG   . LEU   A 1 108 ? 26.947 -9.784  -10.957 1.00 20.99 ?  108 LEU   A HG   1 
ATOM   2394 H HD11 . LEU   A 1 108 ? 28.513 -8.164  -11.482 1.00 21.78 ?  108 LEU   A HD11 1 
ATOM   2395 H HD12 . LEU   A 1 108 ? 27.152 -7.462  -11.059 1.00 21.78 ?  108 LEU   A HD12 1 
ATOM   2396 H HD13 . LEU   A 1 108 ? 28.363 -7.530  -10.033 1.00 21.78 ?  108 LEU   A HD13 1 
ATOM   2397 H HD21 . LEU   A 1 108 ? 29.265 -10.118 -10.380 1.00 23.48 ?  108 LEU   A HD21 1 
ATOM   2398 H HD22 . LEU   A 1 108 ? 28.823 -9.879  -8.872  1.00 23.48 ?  108 LEU   A HD22 1 
ATOM   2399 H HD23 . LEU   A 1 108 ? 28.238 -11.111 -9.687  1.00 23.48 ?  108 LEU   A HD23 1 
ATOM   2400 N N    . LEU   A 1 109 ? 23.622 -10.284 -7.300  1.00 13.62 ?  109 LEU   A N    1 
ATOM   2401 C CA   . LEU   A 1 109 ? 22.935 -10.162 -6.021  1.00 12.68 ?  109 LEU   A CA   1 
ATOM   2402 C C    . LEU   A 1 109 ? 23.288 -11.315 -5.089  1.00 11.79 ?  109 LEU   A C    1 
ATOM   2403 O O    . LEU   A 1 109 ? 23.422 -11.121 -3.877  1.00 12.21 ?  109 LEU   A O    1 
ATOM   2404 C CB   . LEU   A 1 109 ? 21.424 -10.073 -6.249  1.00 13.74 ?  109 LEU   A CB   1 
ATOM   2405 C CG   . LEU   A 1 109 ? 20.556 -9.804  -5.023  1.00 13.92 ?  109 LEU   A CG   1 
ATOM   2406 C CD1  . LEU   A 1 109 ? 21.022 -8.541  -4.317  1.00 13.87 ?  109 LEU   A CD1  1 
ATOM   2407 C CD2  . LEU   A 1 109 ? 19.094 -9.674  -5.420  1.00 15.18 ?  109 LEU   A CD2  1 
ATOM   2408 H H    . LEU   A 1 109 ? 23.098 -10.382 -7.980  1.00 16.32 ?  109 LEU   A H    1 
ATOM   2409 H HA   . LEU   A 1 109 ? 23.223 -9.339  -5.596  1.00 15.20 ?  109 LEU   A HA   1 
ATOM   2410 H HB2  . LEU   A 1 109 ? 21.253 -9.355  -6.877  1.00 16.47 ?  109 LEU   A HB2  1 
ATOM   2411 H HB3  . LEU   A 1 109 ? 21.123 -10.911 -6.628  1.00 16.47 ?  109 LEU   A HB3  1 
ATOM   2412 H HG   . LEU   A 1 109 ? 20.636 -10.546 -4.404  1.00 16.68 ?  109 LEU   A HG   1 
ATOM   2413 H HD11 . LEU   A 1 109 ? 20.353 -8.266  -3.676  1.00 16.63 ?  109 LEU   A HD11 1 
ATOM   2414 H HD12 . LEU   A 1 109 ? 21.862 -8.723  -3.864  1.00 16.63 ?  109 LEU   A HD12 1 
ATOM   2415 H HD13 . LEU   A 1 109 ? 21.154 -7.839  -4.979  1.00 16.63 ?  109 LEU   A HD13 1 
ATOM   2416 H HD21 . LEU   A 1 109 ? 18.581 -9.373  -4.650  1.00 18.20 ?  109 LEU   A HD21 1 
ATOM   2417 H HD22 . LEU   A 1 109 ? 19.013 -9.028  -6.139  1.00 18.20 ?  109 LEU   A HD22 1 
ATOM   2418 H HD23 . LEU   A 1 109 ? 18.764 -10.539 -5.715  1.00 18.20 ?  109 LEU   A HD23 1 
ATOM   2419 N N    . LYS   A 1 110 ? 23.440 -12.528 -5.628  1.00 11.80 ?  110 LYS   A N    1 
ATOM   2420 C CA   . LYS   A 1 110 ? 23.815 -13.649 -4.773  1.00 11.74 ?  110 LYS   A CA   1 
ATOM   2421 C C    . LYS   A 1 110 ? 25.198 -13.426 -4.167  1.00 10.89 ?  110 LYS   A C    1 
ATOM   2422 O O    . LYS   A 1 110 ? 25.399 -13.627 -2.965  1.00 11.16 ?  110 LYS   A O    1 
ATOM   2423 C CB   . LYS   A 1 110 ? 23.737 -14.973 -5.540  1.00 12.71 ?  110 LYS   A CB   1 
ATOM   2424 C CG   . LYS   A 1 110 ? 23.917 -16.190 -4.633  1.00 13.03 ?  110 LYS   A CG   1 
ATOM   2425 C CD   . LYS   A 1 110 ? 23.694 -17.499 -5.356  1.00 13.46 ?  110 LYS   A CD   1 
ATOM   2426 C CE   . LYS   A 1 110 ? 23.782 -18.686 -4.412  1.00 14.13 ?  110 LYS   A CE   1 
ATOM   2427 N NZ   . LYS   A 1 110 ? 22.615 -18.800 -3.503  1.00 14.15 ?  110 LYS   A NZ   1 
ATOM   2428 H H    . LYS   A 1 110 ? 23.327 -12.724 -6.459  1.00 14.14 ?  110 LYS   A H    1 
ATOM   2429 H HA   . LYS   A 1 110 ? 23.176 -13.704 -4.040  1.00 14.06 ?  110 LYS   A HA   1 
ATOM   2430 H HB2  . LYS   A 1 110 ? 22.869 -15.044 -5.966  1.00 15.22 ?  110 LYS   A HB2  1 
ATOM   2431 H HB3  . LYS   A 1 110 ? 24.439 -14.991 -6.207  1.00 15.22 ?  110 LYS   A HB3  1 
ATOM   2432 H HG2  . LYS   A 1 110 ? 24.821 -16.194 -4.280  1.00 15.61 ?  110 LYS   A HG2  1 
ATOM   2433 H HG3  . LYS   A 1 110 ? 23.279 -16.140 -3.904  1.00 15.61 ?  110 LYS   A HG3  1 
ATOM   2434 H HD2  . LYS   A 1 110 ? 22.812 -17.496 -5.757  1.00 16.13 ?  110 LYS   A HD2  1 
ATOM   2435 H HD3  . LYS   A 1 110 ? 24.374 -17.605 -6.039  1.00 16.13 ?  110 LYS   A HD3  1 
ATOM   2436 H HE2  . LYS   A 1 110 ? 23.836 -19.501 -4.933  1.00 16.93 ?  110 LYS   A HE2  1 
ATOM   2437 H HE3  . LYS   A 1 110 ? 24.577 -18.593 -3.861  1.00 16.93 ?  110 LYS   A HE3  1 
ATOM   2438 H HZ1  . LYS   A 1 110 ? 22.707 -19.506 -2.971  1.00 16.96 ?  110 LYS   A HZ1  1 
ATOM   2439 H HZ2  . LYS   A 1 110 ? 22.543 -18.066 -3.003  1.00 16.96 ?  110 LYS   A HZ2  1 
ATOM   2440 H HZ3  . LYS   A 1 110 ? 21.867 -18.895 -3.981  1.00 16.96 ?  110 LYS   A HZ3  1 
ATOM   2441 N N    . SER   A 1 111 ? 26.156 -12.986 -4.986  1.00 11.06 ?  111 SER   A N    1 
ATOM   2442 C CA   . SER   A 1 111 ? 27.485 -12.667 -4.473  1.00 11.44 ?  111 SER   A CA   1 
ATOM   2443 C C    . SER   A 1 111 ? 27.411 -11.626 -3.363  1.00 10.90 ?  111 SER   A C    1 
ATOM   2444 O O    . SER   A 1 111 ? 28.105 -11.732 -2.345  1.00 11.57 ?  111 SER   A O    1 
ATOM   2445 C CB   . SER   A 1 111 ? 28.371 -12.173 -5.613  1.00 12.91 ?  111 SER   A CB   1 
ATOM   2446 O OG   . SER   A 1 111 ? 28.490 -13.170 -6.615  1.00 14.77 ?  111 SER   A OG   1 
ATOM   2447 H H    . SER   A 1 111 ? 26.052 -12.859 -5.831  1.00 13.25 ?  111 SER   A H    1 
ATOM   2448 H HA   . SER   A 1 111 ? 27.878 -13.473 -4.109  1.00 13.71 ?  111 SER   A HA   1 
ATOM   2449 H HB2  . SER   A 1 111 ? 27.969 -11.388 -6.012  1.00 15.47 ?  111 SER   A HB2  1 
ATOM   2450 H HB3  . SER   A 1 111 ? 29.247 -11.958 -5.259  1.00 15.47 ?  111 SER   A HB3  1 
ATOM   2451 H HG   . SER   A 1 111 ? 29.003 -12.899 -7.234  1.00 17.70 ?  111 SER   A HG   1 
ATOM   2452 N N    . ALA   A 1 112 ? 26.561 -10.614 -3.541  1.00 10.96 ?  112 ALA   A N    1 
ATOM   2453 C CA   . ALA   A 1 112 ? 26.417 -9.577  -2.523  1.00 10.81 ?  112 ALA   A CA   1 
ATOM   2454 C C    . ALA   A 1 112 ? 25.948 -10.183 -1.204  1.00 10.86 ?  112 ALA   A C    1 
ATOM   2455 O O    . ALA   A 1 112 ? 26.508 -9.903  -0.138  1.00 11.09 ?  112 ALA   A O    1 
ATOM   2456 C CB   . ALA   A 1 112 ? 25.447 -8.499  -3.011  1.00 11.22 ?  112 ALA   A CB   1 
ATOM   2457 H H    . ALA   A 1 112 ? 26.068 -10.499 -4.234  1.00 13.13 ?  112 ALA   A H    1 
ATOM   2458 H HA   . ALA   A 1 112 ? 27.276 -9.150  -2.371  1.00 12.95 ?  112 ALA   A HA   1 
ATOM   2459 H HB1  . ALA   A 1 112 ? 25.366 -7.805  -2.327  1.00 13.44 ?  112 ALA   A HB1  1 
ATOM   2460 H HB2  . ALA   A 1 112 ? 25.782 -8.107  -3.830  1.00 13.44 ?  112 ALA   A HB2  1 
ATOM   2461 H HB3  . ALA   A 1 112 ? 24.575 -8.898  -3.167  1.00 13.44 ?  112 ALA   A HB3  1 
ATOM   2462 N N    . TYR   A 1 113 ? 24.913 -11.026 -1.253  1.00 10.98 ?  113 TYR   A N    1 
ATOM   2463 C CA   . TYR   A 1 113 ? 24.401 -11.626 -0.023  1.00 10.74 ?  113 TYR   A CA   1 
ATOM   2464 C C    . TYR   A 1 113 ? 25.400 -12.589 0.620   1.00 10.14 ?  113 TYR   A C    1 
ATOM   2465 O O    . TYR   A 1 113 ? 25.365 -12.780 1.840   1.00 10.90 ?  113 TYR   A O    1 
ATOM   2466 C CB   . TYR   A 1 113 ? 23.081 -12.349 -0.291  1.00 11.23 ?  113 TYR   A CB   1 
ATOM   2467 C CG   . TYR   A 1 113 ? 21.869 -11.448 -0.210  1.00 11.30 ?  113 TYR   A CG   1 
ATOM   2468 C CD1  . TYR   A 1 113 ? 21.531 -10.822 0.979   1.00 11.60 ?  113 TYR   A CD1  1 
ATOM   2469 C CD2  . TYR   A 1 113 ? 21.048 -11.250 -1.312  1.00 11.77 ?  113 TYR   A CD2  1 
ATOM   2470 C CE1  . TYR   A 1 113 ? 20.402 -10.021 1.066   1.00 12.16 ?  113 TYR   A CE1  1 
ATOM   2471 C CE2  . TYR   A 1 113 ? 19.909 -10.438 -1.232  1.00 11.98 ?  113 TYR   A CE2  1 
ATOM   2472 C CZ   . TYR   A 1 113 ? 19.601 -9.837  -0.044  1.00 11.78 ?  113 TYR   A CZ   1 
ATOM   2473 O OH   . TYR   A 1 113 ? 18.478 -9.038  0.053   1.00 12.98 ?  113 TYR   A OH   1 
ATOM   2474 H H    . TYR   A 1 113 ? 24.499 -11.258 -1.972  1.00 13.15 ?  113 TYR   A H    1 
ATOM   2475 H HA   . TYR   A 1 113 ? 24.229 -10.918 0.614   1.00 12.87 ?  113 TYR   A HA   1 
ATOM   2476 H HB2  . TYR   A 1 113 ? 23.106 -12.728 -1.183  1.00 13.45 ?  113 TYR   A HB2  1 
ATOM   2477 H HB3  . TYR   A 1 113 ? 22.973 -13.053 0.365   1.00 13.45 ?  113 TYR   A HB3  1 
ATOM   2478 H HD1  . TYR   A 1 113 ? 22.072 -10.954 1.733   1.00 13.90 ?  113 TYR   A HD1  1 
ATOM   2479 H HD2  . TYR   A 1 113 ? 21.254 -11.667 -2.114  1.00 14.10 ?  113 TYR   A HD2  1 
ATOM   2480 H HE1  . TYR   A 1 113 ? 20.196 -9.608  1.874   1.00 14.57 ?  113 TYR   A HE1  1 
ATOM   2481 H HE2  . TYR   A 1 113 ? 19.365 -10.312 -1.974  1.00 14.36 ?  113 TYR   A HE2  1 
ATOM   2482 H HH   . TYR   A 1 113 ? 18.088 -9.014  -0.696  1.00 15.55 ?  113 TYR   A HH   1 
ATOM   2483 N N    . GLU   A 1 114 ? 26.291 -13.201 -0.172  1.00 10.66 ?  114 GLU   A N    1 
ATOM   2484 C CA   . GLU   A 1 114 ? 27.289 -14.101 0.410   1.00 11.01 ?  114 GLU   A CA   1 
ATOM   2485 C C    . GLU   A 1 114 ? 28.146 -13.396 1.456   1.00 10.90 ?  114 GLU   A C    1 
ATOM   2486 O O    . GLU   A 1 114 ? 28.628 -14.035 2.400   1.00 11.16 ?  114 GLU   A O    1 
ATOM   2487 C CB   . GLU   A 1 114 ? 28.152 -14.721 -0.690  1.00 11.14 ?  114 GLU   A CB   1 
ATOM   2488 C CG   . GLU   A 1 114 ? 27.388 -15.779 -1.464  1.00 11.46 ?  114 GLU   A CG   1 
ATOM   2489 C CD   . GLU   A 1 114 ? 28.098 -16.309 -2.702  1.00 12.06 ?  114 GLU   A CD   1 
ATOM   2490 O OE1  . GLU   A 1 114 ? 29.050 -15.680 -3.202  1.00 11.81 ?  114 GLU   A OE1  1 
ATOM   2491 O OE2  . GLU   A 1 114 ? 27.658 -17.374 -3.191  1.00 13.05 -1 114 GLU   A OE2  1 
ATOM   2492 H H    . GLU   A 1 114 ? 26.338 -13.108 -1.034  1.00 12.77 ?  114 GLU   A H    1 
ATOM   2493 H HA   . GLU   A 1 114 ? 26.820 -14.820 0.849   1.00 13.19 ?  114 GLU   A HA   1 
ATOM   2494 H HB2  . GLU   A 1 114 ? 28.424 -14.030 -1.318  1.00 13.34 ?  114 GLU   A HB2  1 
ATOM   2495 H HB3  . GLU   A 1 114 ? 28.928 -15.138 -0.292  1.00 13.34 ?  114 GLU   A HB3  1 
ATOM   2496 H HG2  . GLU   A 1 114 ? 27.232 -16.537 -0.878  1.00 13.73 ?  114 GLU   A HG2  1 
ATOM   2497 H HG3  . GLU   A 1 114 ? 26.537 -15.408 -1.747  1.00 13.73 ?  114 GLU   A HG3  1 
ATOM   2498 N N    . ASN   A 1 115 ? 28.329 -12.079 1.330   1.00 10.48 ?  115 ASN   A N    1 
ATOM   2499 C CA   . ASN   A 1 115 ? 29.095 -11.351 2.335   1.00 11.07 ?  115 ASN   A CA   1 
ATOM   2500 C C    . ASN   A 1 115 ? 28.486 -11.488 3.725   1.00 10.52 ?  115 ASN   A C    1 
ATOM   2501 O O    . ASN   A 1 115 ? 29.204 -11.411 4.729   1.00 11.16 ?  115 ASN   A O    1 
ATOM   2502 C CB   . ASN   A 1 115 ? 29.192 -9.872  1.958   1.00 10.95 ?  115 ASN   A CB   1 
ATOM   2503 C CG   . ASN   A 1 115 ? 29.992 -9.646  0.701   1.00 11.77 ?  115 ASN   A CG   1 
ATOM   2504 O OD1  . ASN   A 1 115 ? 31.208 -9.758  0.718   1.00 14.96 ?  115 ASN   A OD1  1 
ATOM   2505 N ND2  . ASN   A 1 115 ? 29.324 -9.340  -0.392  1.00 11.40 ?  115 ASN   A ND2  1 
ATOM   2506 H H    . ASN   A 1 115 ? 28.024 -11.590 0.687   1.00 12.55 ?  115 ASN   A H    1 
ATOM   2507 H HA   . ASN   A 1 115 ? 29.994 -11.711 2.367   1.00 13.27 ?  115 ASN   A HA   1 
ATOM   2508 H HB2  . ASN   A 1 115 ? 28.297 -9.521  1.824   1.00 13.12 ?  115 ASN   A HB2  1 
ATOM   2509 H HB3  . ASN   A 1 115 ? 29.626 -9.392  2.686   1.00 13.12 ?  115 ASN   A HB3  1 
ATOM   2510 H HD21 . ASN   A 1 115 ? 29.745 -9.198  -1.126  1.00 13.66 ?  115 ASN   A HD21 1 
ATOM   2511 H HD22 . ASN   A 1 115 ? 28.464 -9.287  -0.372  1.00 13.66 ?  115 ASN   A HD22 1 
ATOM   2512 N N    . PHE   A 1 116 ? 27.160 -11.650 3.807   1.00 10.98 ?  116 PHE   A N    1 
ATOM   2513 C CA   . PHE   A 1 116 ? 26.519 -11.751 5.113   1.00 11.00 ?  116 PHE   A CA   1 
ATOM   2514 C C    . PHE   A 1 116 ? 26.992 -12.989 5.875   1.00 11.02 ?  116 PHE   A C    1 
ATOM   2515 O O    . PHE   A 1 116 ? 26.915 -13.015 7.103   1.00 11.61 ?  116 PHE   A O    1 
ATOM   2516 C CB   . PHE   A 1 116 ? 24.988 -11.876 4.986   1.00 11.31 ?  116 PHE   A CB   1 
ATOM   2517 C CG   . PHE   A 1 116 ? 24.232 -10.631 4.520   1.00 11.05 ?  116 PHE   A CG   1 
ATOM   2518 C CD1  . PHE   A 1 116 ? 24.802 -9.621  3.761   1.00 11.32 ?  116 PHE   A CD1  1 
ATOM   2519 C CD2  . PHE   A 1 116 ? 22.884 -10.519 4.850   1.00 11.87 ?  116 PHE   A CD2  1 
ATOM   2520 C CE1  . PHE   A 1 116 ? 24.032 -8.533  3.347   1.00 11.57 ?  116 PHE   A CE1  1 
ATOM   2521 C CE2  . PHE   A 1 116 ? 22.113 -9.452  4.443   1.00 11.80 ?  116 PHE   A CE2  1 
ATOM   2522 C CZ   . PHE   A 1 116 ? 22.680 -8.454  3.688   1.00 11.59 ?  116 PHE   A CZ   1 
ATOM   2523 H H    . PHE   A 1 116 ? 26.622 -11.692 3.133   1.00 13.15 ?  116 PHE   A H    1 
ATOM   2524 H HA   . PHE   A 1 116 ? 26.722 -10.961 5.639   1.00 13.17 ?  116 PHE   A HA   1 
ATOM   2525 H HB2  . PHE   A 1 116 ? 24.795 -12.582 4.354   1.00 13.55 ?  116 PHE   A HB2  1 
ATOM   2526 H HB3  . PHE   A 1 116 ? 24.636 -12.119 5.857   1.00 13.55 ?  116 PHE   A HB3  1 
ATOM   2527 H HD1  . PHE   A 1 116 ? 25.697 -9.675  3.523   1.00 13.56 ?  116 PHE   A HD1  1 
ATOM   2528 H HD2  . PHE   A 1 116 ? 22.485 -11.204 5.351   1.00 14.22 ?  116 PHE   A HD2  1 
ATOM   2529 H HE1  . PHE   A 1 116 ? 24.419 -7.856  2.841   1.00 13.87 ?  116 PHE   A HE1  1 
ATOM   2530 H HE2  . PHE   A 1 116 ? 21.215 -9.414  4.683   1.00 14.14 ?  116 PHE   A HE2  1 
ATOM   2531 H HZ   . PHE   A 1 116 ? 22.171 -7.725  3.424   1.00 13.88 ?  116 PHE   A HZ   1 
ATOM   2532 N N    . ASN   A 1 117 ? 27.429 -14.035 5.166   1.00 11.06 ?  117 ASN   A N    1 
ATOM   2533 C CA   . ASN   A 1 117 ? 27.799 -15.282 5.824   1.00 11.38 ?  117 ASN   A CA   1 
ATOM   2534 C C    . ASN   A 1 117 ? 29.065 -15.165 6.648   1.00 11.97 ?  117 ASN   A C    1 
ATOM   2535 O O    . ASN   A 1 117 ? 29.365 -16.083 7.415   1.00 13.03 ?  117 ASN   A O    1 
ATOM   2536 C CB   . ASN   A 1 117 ? 27.906 -16.398 4.792   1.00 11.64 ?  117 ASN   A CB   1 
ATOM   2537 C CG   . ASN   A 1 117 ? 26.551 -16.785 4.264   1.00 11.60 ?  117 ASN   A CG   1 
ATOM   2538 O OD1  . ASN   A 1 117 ? 25.579 -16.826 5.023   1.00 12.29 ?  117 ASN   A OD1  1 
ATOM   2539 N ND2  . ASN   A 1 117 ? 26.458 -17.041 2.973   1.00 11.45 ?  117 ASN   A ND2  1 
ATOM   2540 H H    . ASN   A 1 117 ? 27.502 -14.042 4.308   1.00 13.25 ?  117 ASN   A H    1 
ATOM   2541 H HA   . ASN   A 1 117 ? 27.080 -15.517 6.430   1.00 13.63 ?  117 ASN   A HA   1 
ATOM   2542 H HB2  . ASN   A 1 117 ? 28.454 -16.094 4.048   1.00 13.94 ?  117 ASN   A HB2  1 
ATOM   2543 H HB3  . ASN   A 1 117 ? 28.307 -17.174 5.208   1.00 13.94 ?  117 ASN   A HB3  1 
ATOM   2544 H HD21 . ASN   A 1 117 ? 25.702 -17.255 2.633   1.00 13.72 ?  117 ASN   A HD21 1 
ATOM   2545 H HD22 . ASN   A 1 117 ? 27.158 -16.985 2.469   1.00 13.72 ?  117 ASN   A HD22 1 
ATOM   2546 N N    . GLN   A 1 118 ? 29.791 -14.057 6.531   1.00 11.78 ?  118 GLN   A N    1 
ATOM   2547 C CA   . GLN   A 1 118 ? 30.970 -13.832 7.353   1.00 12.26 ?  118 GLN   A CA   1 
ATOM   2548 C C    . GLN   A 1 118 ? 30.633 -13.260 8.723   1.00 12.44 ?  118 GLN   A C    1 
ATOM   2549 O O    . GLN   A 1 118 ? 31.550 -12.966 9.496   1.00 14.18 ?  118 GLN   A O    1 
ATOM   2550 C CB   . GLN   A 1 118 ? 31.954 -12.924 6.616   1.00 12.49 ?  118 GLN   A CB   1 
ATOM   2551 C CG   . GLN   A 1 118 ? 32.427 -13.505 5.293   1.00 12.45 ?  118 GLN   A CG   1 
ATOM   2552 C CD   . GLN   A 1 118 ? 33.256 -14.765 5.468   1.00 12.73 ?  118 GLN   A CD   1 
ATOM   2553 O OE1  . GLN   A 1 118 ? 34.108 -14.837 6.359   1.00 13.72 ?  118 GLN   A OE1  1 
ATOM   2554 N NE2  . GLN   A 1 118 ? 33.008 -15.766 4.625   1.00 12.93 ?  118 GLN   A NE2  1 
ATOM   2555 H H    . GLN   A 1 118 ? 29.614 -13.411 5.982   1.00 14.11 ?  118 GLN   A H    1 
ATOM   2556 H HA   . GLN   A 1 118 ? 31.401 -14.688 7.493   1.00 14.69 ?  118 GLN   A HA   1 
ATOM   2557 H HB2  . GLN   A 1 118 ? 31.524 -12.076 6.437   1.00 14.97 ?  118 GLN   A HB2  1 
ATOM   2558 H HB3  . GLN   A 1 118 ? 32.732 -12.791 7.181   1.00 14.97 ?  118 GLN   A HB3  1 
ATOM   2559 H HG2  . GLN   A 1 118 ? 31.657 -13.723 4.744   1.00 14.92 ?  118 GLN   A HG2  1 
ATOM   2560 H HG3  . GLN   A 1 118 ? 32.981 -12.851 4.840   1.00 14.92 ?  118 GLN   A HG3  1 
ATOM   2561 H HE21 . GLN   A 1 118 ? 32.399 -15.677 4.016   1.00 15.49 ?  118 GLN   A HE21 1 
ATOM   2562 H HE22 . GLN   A 1 118 ? 33.443 -16.504 4.684   1.00 15.49 ?  118 GLN   A HE22 1 
ATOM   2563 N N    . HIS   A 1 119 ? 29.346 -13.113 9.044   1.00 12.15 ?  119 HIS   A N    1 
ATOM   2564 C CA   . HIS   A 1 119 ? 28.901 -12.513 10.296  1.00 12.55 ?  119 HIS   A CA   1 
ATOM   2565 C C    . HIS   A 1 119 ? 27.766 -13.342 10.868  1.00 12.88 ?  119 HIS   A C    1 
ATOM   2566 O O    . HIS   A 1 119 ? 26.811 -13.660 10.158  1.00 13.66 ?  119 HIS   A O    1 
ATOM   2567 C CB   . HIS   A 1 119 ? 28.438 -11.081 10.031  1.00 13.21 ?  119 HIS   A CB   1 
ATOM   2568 C CG   . HIS   A 1 119 ? 29.513 -10.265 9.412   1.00 14.80 ?  119 HIS   A CG   1 
ATOM   2569 N ND1  . HIS   A 1 119 ? 30.498 -9.667  10.162  1.00 16.86 ?  119 HIS   A ND1  1 
ATOM   2570 C CD2  . HIS   A 1 119 ? 29.842 -10.065 8.116   1.00 15.64 ?  119 HIS   A CD2  1 
ATOM   2571 C CE1  . HIS   A 1 119 ? 31.359 -9.078  9.351   1.00 17.10 ?  119 HIS   A CE1  1 
ATOM   2572 N NE2  . HIS   A 1 119 ? 30.994 -9.316  8.104   1.00 16.96 ?  119 HIS   A NE2  1 
ATOM   2573 H H    . HIS   A 1 119 ? 28.688 -13.362 8.540   1.00 14.56 ?  119 HIS   A H    1 
ATOM   2574 H HA   . HIS   A 1 119 ? 29.636 -12.500 10.933  1.00 15.03 ?  119 HIS   A HA   1 
ATOM   2575 H HB2  . HIS   A 1 119 ? 27.680 -11.104 9.426   1.00 15.83 ?  119 HIS   A HB2  1 
ATOM   2576 H HB3  . HIS   A 1 119 ? 28.188 -10.670 10.871  1.00 15.83 ?  119 HIS   A HB3  1 
ATOM   2577 H HD2  . HIS   A 1 119 ? 29.376 -10.375 7.368   1.00 18.74 ?  119 HIS   A HD2  1 
ATOM   2578 H HE1  . HIS   A 1 119 ? 32.101 -8.582  9.609   1.00 20.50 ?  119 HIS   A HE1  1 
ATOM   2579 H HE2  . HIS   A 1 119 ? 31.393 -9.023  7.398   1.00 20.33 ?  119 HIS   A HE2  1 
ATOM   2580 N N    . GLU   A 1 120 ? 27.871 -13.683 12.152  1.00 13.73 ?  120 GLU   A N    1 
ATOM   2581 C CA   . GLU   A 1 120 ? 26.921 -14.632 12.733  1.00 15.77 ?  120 GLU   A CA   1 
ATOM   2582 C C    . GLU   A 1 120 ? 25.508 -14.065 12.827  1.00 14.31 ?  120 GLU   A C    1 
ATOM   2583 O O    . GLU   A 1 120 ? 24.528 -14.822 12.724  1.00 14.73 ?  120 GLU   A O    1 
ATOM   2584 C CB   . GLU   A 1 120 ? 27.405 -15.088 14.112  1.00 20.93 ?  120 GLU   A CB   1 
ATOM   2585 C CG   . GLU   A 1 120 ? 28.596 -16.035 14.079  1.00 28.10 ?  120 GLU   A CG   1 
ATOM   2586 C CD   . GLU   A 1 120 ? 28.806 -16.744 15.403  1.00 34.52 ?  120 GLU   A CD   1 
ATOM   2587 O OE1  . GLU   A 1 120 ? 28.392 -16.196 16.447  1.00 36.92 ?  120 GLU   A OE1  1 
ATOM   2588 O OE2  . GLU   A 1 120 ? 29.381 -17.853 15.397  1.00 39.17 -1 120 GLU   A OE2  1 
ATOM   2589 H H    . GLU   A 1 120 ? 28.473 -13.397 12.698  1.00 16.46 ?  120 GLU   A H    1 
ATOM   2590 H HA   . GLU   A 1 120 ? 26.883 -15.417 12.170  1.00 18.90 ?  120 GLU   A HA   1 
ATOM   2591 H HB2  . GLU   A 1 120 ? 27.668 -14.313 14.630  1.00 25.10 ?  120 GLU   A HB2  1 
ATOM   2592 H HB3  . GLU   A 1 120 ? 26.680 -15.552 14.564  1.00 25.10 ?  120 GLU   A HB3  1 
ATOM   2593 H HG2  . GLU   A 1 120 ? 28.454 -16.705 13.391  1.00 33.70 ?  120 GLU   A HG2  1 
ATOM   2594 H HG3  . GLU   A 1 120 ? 29.402 -15.531 13.896  1.00 33.70 ?  120 GLU   A HG3  1 
ATOM   2595 N N    . VAL   A 1 121 ? 25.384 -12.760 13.072  1.00 13.85 ?  121 VAL   A N    1 
ATOM   2596 C CA   . VAL   A 1 121 ? 24.097 -12.083 13.206  1.00 14.35 ?  121 VAL   A CA   1 
ATOM   2597 C C    . VAL   A 1 121 ? 24.210 -10.700 12.572  1.00 13.29 ?  121 VAL   A C    1 
ATOM   2598 O O    . VAL   A 1 121 ? 25.184 -9.980  12.811  1.00 14.15 ?  121 VAL   A O    1 
ATOM   2599 C CB   . VAL   A 1 121 ? 23.680 -11.938 14.687  1.00 17.23 ?  121 VAL   A CB   1 
ATOM   2600 C CG1  . VAL   A 1 121 ? 22.295 -11.321 14.795  1.00 17.91 ?  121 VAL   A CG1  1 
ATOM   2601 C CG2  . VAL   A 1 121 ? 23.724 -13.269 15.420  1.00 19.17 ?  121 VAL   A CG2  1 
ATOM   2602 H H    . VAL   A 1 121 ? 26.054 -12.228 13.178  1.00 16.60 ?  121 VAL   A H    1 
ATOM   2603 H HA   . VAL   A 1 121 ? 23.415 -12.593 12.744  1.00 17.20 ?  121 VAL   A HA   1 
ATOM   2604 H HB   . VAL   A 1 121 ? 24.299 -11.341 15.130  1.00 20.65 ?  121 VAL   A HB   1 
ATOM   2605 H HG11 . VAL   A 1 121 ? 21.996 -11.373 15.718  1.00 21.47 ?  121 VAL   A HG11 1 
ATOM   2606 H HG12 . VAL   A 1 121 ? 22.338 -10.394 14.516  1.00 21.47 ?  121 VAL   A HG12 1 
ATOM   2607 H HG13 . VAL   A 1 121 ? 21.684 -11.813 14.224  1.00 21.47 ?  121 VAL   A HG13 1 
ATOM   2608 H HG21 . VAL   A 1 121 ? 23.381 -13.147 16.324  1.00 22.98 ?  121 VAL   A HG21 1 
ATOM   2609 H HG22 . VAL   A 1 121 ? 23.169 -13.912 14.948  1.00 22.98 ?  121 VAL   A HG22 1 
ATOM   2610 H HG23 . VAL   A 1 121 ? 24.638 -13.583 15.457  1.00 22.98 ?  121 VAL   A HG23 1 
ATOM   2611 N N    . LEU   A 1 122 ? 23.199 -10.308 11.792  1.00 12.89 ?  122 LEU   A N    1 
ATOM   2612 C CA   . LEU   A 1 122 ? 23.197 -9.005  11.132  1.00 12.91 ?  122 LEU   A CA   1 
ATOM   2613 C C    . LEU   A 1 122 ? 21.799 -8.414  11.107  1.00 12.62 ?  122 LEU   A C    1 
ATOM   2614 O O    . LEU   A 1 122 ? 20.811 -9.135  10.966  1.00 13.86 ?  122 LEU   A O    1 
ATOM   2615 C CB   . LEU   A 1 122 ? 23.599 -9.083  9.655   1.00 14.62 ?  122 LEU   A CB   1 
ATOM   2616 C CG   . LEU   A 1 122 ? 24.796 -9.930  9.262   1.00 14.44 ?  122 LEU   A CG   1 
ATOM   2617 C CD1  . LEU   A 1 122 ? 24.374 -11.379 9.059   1.00 15.43 ?  122 LEU   A CD1  1 
ATOM   2618 C CD2  . LEU   A 1 122 ? 25.437 -9.370  7.999   1.00 13.54 ?  122 LEU   A CD2  1 
ATOM   2619 H H    . LEU   A 1 122 ? 22.497 -10.784 11.629  1.00 15.44 ?  122 LEU   A H    1 
ATOM   2620 H HA   . LEU   A 1 122 ? 23.798 -8.397  11.589  1.00 15.46 ?  122 LEU   A HA   1 
ATOM   2621 H HB2  . LEU   A 1 122 ? 22.846 -9.431  9.157   1.00 17.52 ?  122 LEU   A HB2  1 
ATOM   2622 H HB3  . LEU   A 1 122 ? 23.790 -8.183  9.349   1.00 17.52 ?  122 LEU   A HB3  1 
ATOM   2623 H HG   . LEU   A 1 122 ? 25.466 -9.901  9.964   1.00 17.30 ?  122 LEU   A HG   1 
ATOM   2624 H HD11 . LEU   A 1 122 ? 25.132 -11.892 8.736   1.00 18.49 ?  122 LEU   A HD11 1 
ATOM   2625 H HD12 . LEU   A 1 122 ? 24.073 -11.741 9.908   1.00 18.49 ?  122 LEU   A HD12 1 
ATOM   2626 H HD13 . LEU   A 1 122 ? 23.653 -11.413 8.411   1.00 18.49 ?  122 LEU   A HD13 1 
ATOM   2627 H HD21 . LEU   A 1 122 ? 26.180 -9.939  7.730   1.00 16.22 ?  122 LEU   A HD21 1 
ATOM   2628 H HD22 . LEU   A 1 122 ? 24.774 -9.346  7.288   1.00 16.22 ?  122 LEU   A HD22 1 
ATOM   2629 H HD23 . LEU   A 1 122 ? 25.762 -8.471  8.172   1.00 16.22 ?  122 LEU   A HD23 1 
ATOM   2630 N N    . LEU   A 1 123 ? 21.736 -7.084  11.204  1.00 12.40 ?  123 LEU   A N    1 
ATOM   2631 C CA   . LEU   A 1 123 ? 20.559 -6.293  10.849  1.00 12.00 ?  123 LEU   A CA   1 
ATOM   2632 C C    . LEU   A 1 123 ? 20.791 -5.744  9.449   1.00 11.51 ?  123 LEU   A C    1 
ATOM   2633 O O    . LEU   A 1 123 ? 21.834 -5.144  9.199   1.00 12.26 ?  123 LEU   A O    1 
ATOM   2634 C CB   . LEU   A 1 123 ? 20.435 -5.126  11.826  1.00 12.46 ?  123 LEU   A CB   1 
ATOM   2635 C CG   . LEU   A 1 123 ? 19.394 -4.061  11.495  1.00 13.26 ?  123 LEU   A CG   1 
ATOM   2636 C CD1  . LEU   A 1 123 ? 17.991 -4.638  11.507  1.00 14.45 ?  123 LEU   A CD1  1 
ATOM   2637 C CD2  . LEU   A 1 123 ? 19.524 -2.910  12.478  1.00 14.39 ?  123 LEU   A CD2  1 
ATOM   2638 H H    . LEU   A 1 123 ? 22.398 -6.594  11.475  1.00 14.86 ?  123 LEU   A H    1 
ATOM   2639 H HA   . LEU   A 1 123 ? 19.757 -6.839  10.869  1.00 14.37 ?  123 LEU   A HA   1 
ATOM   2640 H HB2  . LEU   A 1 123 ? 20.206 -5.486  12.697  1.00 14.93 ?  123 LEU   A HB2  1 
ATOM   2641 H HB3  . LEU   A 1 123 ? 21.293 -4.682  11.876  1.00 14.93 ?  123 LEU   A HB3  1 
ATOM   2642 H HG   . LEU   A 1 123 ? 19.565 -3.709  10.606  1.00 15.88 ?  123 LEU   A HG   1 
ATOM   2643 H HD11 . LEU   A 1 123 ? 17.354 -3.929  11.324  1.00 17.31 ?  123 LEU   A HD11 1 
ATOM   2644 H HD12 . LEU   A 1 123 ? 17.924 -5.326  10.825  1.00 17.31 ?  123 LEU   A HD12 1 
ATOM   2645 H HD13 . LEU   A 1 123 ? 17.815 -5.022  12.381  1.00 17.31 ?  123 LEU   A HD13 1 
ATOM   2646 H HD21 . LEU   A 1 123 ? 18.891 -2.221  12.241  1.00 17.25 ?  123 LEU   A HD21 1 
ATOM   2647 H HD22 . LEU   A 1 123 ? 19.341 -3.244  13.371  1.00 17.25 ?  123 LEU   A HD22 1 
ATOM   2648 H HD23 . LEU   A 1 123 ? 20.429 -2.565  12.433  1.00 17.25 ?  123 LEU   A HD23 1 
ATOM   2649 N N    A ALA   A 1 124 ? 19.821 -5.899  8.552   0.60 11.06 ?  124 ALA   A N    1 
ATOM   2650 N N    B ALA   A 1 124 ? 19.851 -5.975  8.534   0.40 11.73 ?  124 ALA   A N    1 
ATOM   2651 C CA   A ALA   A 1 124 ? 20.079 -5.576  7.156   0.60 10.80 ?  124 ALA   A CA   1 
ATOM   2652 C CA   B ALA   A 1 124 ? 20.155 -5.743  7.130   0.40 12.17 ?  124 ALA   A CA   1 
ATOM   2653 C C    A ALA   A 1 124 ? 18.817 -5.085  6.465   0.60 10.52 ?  124 ALA   A C    1 
ATOM   2654 C C    B ALA   A 1 124 ? 18.926 -5.319  6.338   0.40 11.50 ?  124 ALA   A C    1 
ATOM   2655 O O    A ALA   A 1 124 ? 17.698 -5.423  6.875   0.60 11.20 ?  124 ALA   A O    1 
ATOM   2656 O O    B ALA   A 1 124 ? 17.795 -5.667  6.698   0.40 11.88 ?  124 ALA   A O    1 
ATOM   2657 C CB   A ALA   A 1 124 ? 20.611 -6.797  6.401   0.60 10.96 ?  124 ALA   A CB   1 
ATOM   2658 C CB   B ALA   A 1 124 ? 20.771 -6.997  6.492   0.40 12.75 ?  124 ALA   A CB   1 
ATOM   2659 H H    A ALA   A 1 124 ? 19.026 -6.186  8.721   0.60 13.25 ?  124 ALA   A H    1 
ATOM   2660 H H    B ALA   A 1 124 ? 19.057 -6.264  8.692   0.40 14.05 ?  124 ALA   A H    1 
ATOM   2661 H HA   A ALA   A 1 124 ? 20.754 -4.879  7.122   0.60 12.94 ?  124 ALA   A HA   1 
ATOM   2662 H HA   B ALA   A 1 124 ? 20.809 -5.034  7.073   0.40 14.57 ?  124 ALA   A HA   1 
ATOM   2663 H HB1  A ALA   A 1 124 ? 20.775 -6.549  5.478   0.60 13.13 ?  124 ALA   A HB1  1 
ATOM   2664 H HB1  B ALA   A 1 124 ? 20.968 -6.822  5.558   0.40 15.28 ?  124 ALA   A HB1  1 
ATOM   2665 H HB2  A ALA   A 1 124 ? 21.436 -7.092  6.816   0.60 13.13 ?  124 ALA   A HB2  1 
ATOM   2666 H HB2  B ALA   A 1 124 ? 21.594 -7.220  6.964   0.40 15.28 ?  124 ALA   A HB2  1 
ATOM   2667 H HB3  A ALA   A 1 124 ? 19.948 -7.504  6.441   0.60 13.13 ?  124 ALA   A HB3  1 
ATOM   2668 H HB3  B ALA   A 1 124 ? 20.144 -7.734  6.565   0.40 15.28 ?  124 ALA   A HB3  1 
ATOM   2669 N N    A PRO   A 1 125 ? 18.968 -4.312  5.393   0.60 10.81 ?  125 PRO   A N    1 
ATOM   2670 N N    B PRO   A 1 125 ? 19.125 -4.584  5.242   0.40 10.65 ?  125 PRO   A N    1 
ATOM   2671 C CA   A PRO   A 1 125 ? 17.884 -4.079  4.441   0.60 11.73 ?  125 PRO   A CA   1 
ATOM   2672 C CA   B PRO   A 1 125 ? 18.039 -4.297  4.304   0.40 11.16 ?  125 PRO   A CA   1 
ATOM   2673 C C    A PRO   A 1 125 ? 17.945 -5.146  3.351   0.60 11.55 ?  125 PRO   A C    1 
ATOM   2674 C C    B PRO   A 1 125 ? 18.052 -5.296  3.162   0.40 11.39 ?  125 PRO   A C    1 
ATOM   2675 O O    A PRO   A 1 125 ? 18.882 -5.946  3.283   0.60 11.42 ?  125 PRO   A O    1 
ATOM   2676 O O    B PRO   A 1 125 ? 19.058 -5.975  2.935   0.40 10.89 ?  125 PRO   A O    1 
ATOM   2677 C CB   A PRO   A 1 125 ? 18.285 -2.721  3.854   0.60 12.46 ?  125 PRO   A CB   1 
ATOM   2678 C CB   B PRO   A 1 125 ? 18.436 -2.914  3.778   0.40 11.28 ?  125 PRO   A CB   1 
ATOM   2679 C CG   A PRO   A 1 125 ? 19.786 -2.861  3.730   0.60 12.86 ?  125 PRO   A CG   1 
ATOM   2680 C CG   B PRO   A 1 125 ? 19.951 -3.007  3.701   0.40 10.98 ?  125 PRO   A CG   1 
ATOM   2681 C CD   A PRO   A 1 125 ? 20.202 -3.611  4.986   0.60 11.95 ?  125 PRO   A CD   1 
ATOM   2682 C CD   B PRO   A 1 125 ? 20.381 -3.929  4.831   0.40 10.33 ?  125 PRO   A CD   1 
ATOM   2683 H HA   A PRO   A 1 125 ? 17.010 -4.053  4.867   0.60 14.05 ?  125 PRO   A HA   1 
ATOM   2684 H HA   B PRO   A 1 125 ? 17.164 -4.281  4.739   0.40 13.36 ?  125 PRO   A HA   1 
ATOM   2685 H HB2  A PRO   A 1 125 ? 17.864 -2.597  2.990   0.60 14.93 ?  125 PRO   A HB2  1 
ATOM   2686 H HB2  B PRO   A 1 125 ? 18.048 -2.774  2.899   0.40 13.51 ?  125 PRO   A HB2  1 
ATOM   2687 H HB3  A PRO   A 1 125 ? 18.044 -2.011  4.471   0.60 14.93 ?  125 PRO   A HB3  1 
ATOM   2688 H HB3  B PRO   A 1 125 ? 18.154 -2.233  4.402   0.40 13.51 ?  125 PRO   A HB3  1 
ATOM   2689 H HG2  A PRO   A 1 125 ? 20.007 -3.377  2.935   0.60 15.41 ?  125 PRO   A HG2  1 
ATOM   2690 H HG2  B PRO   A 1 125 ? 20.212 -3.380  2.844   0.40 13.15 ?  125 PRO   A HG2  1 
ATOM   2691 H HG3  A PRO   A 1 125 ? 20.198 -1.986  3.696   0.60 15.41 ?  125 PRO   A HG3  1 
ATOM   2692 H HG3  B PRO   A 1 125 ? 20.334 -2.126  3.821   0.40 13.15 ?  125 PRO   A HG3  1 
ATOM   2693 H HD2  A PRO   A 1 125 ? 20.911 -4.241  4.785   0.60 14.31 ?  125 PRO   A HD2  1 
ATOM   2694 H HD2  B PRO   A 1 125 ? 21.019 -4.587  4.509   0.40 12.38 ?  125 PRO   A HD2  1 
ATOM   2695 H HD3  A PRO   A 1 125 ? 20.474 -2.980  5.675   0.60 14.31 ?  125 PRO   A HD3  1 
ATOM   2696 H HD3  B PRO   A 1 125 ? 20.743 -3.412  5.566   0.40 12.38 ?  125 PRO   A HD3  1 
ATOM   2697 N N    A LEU   A 1 126 ? 16.936 -5.130  2.478   0.60 11.90 ?  126 LEU   A N    1 
ATOM   2698 N N    B LEU   A 1 126 ? 16.955 -5.376  2.421   0.40 12.07 ?  126 LEU   A N    1 
ATOM   2699 C CA   A LEU   A 1 126 ? 16.957 -5.989  1.298   0.60 12.03 ?  126 LEU   A CA   1 
ATOM   2700 C CA   B LEU   A 1 126 ? 17.000 -6.049  1.133   0.40 12.87 ?  126 LEU   A CA   1 
ATOM   2701 C C    A LEU   A 1 126 ? 17.846 -5.374  0.221   0.60 11.52 ?  126 LEU   A C    1 
ATOM   2702 C C    B LEU   A 1 126 ? 17.967 -5.310  0.217   0.40 13.32 ?  126 LEU   A C    1 
ATOM   2703 O O    A LEU   A 1 126 ? 17.554 -4.290  -0.299  0.60 11.50 ?  126 LEU   A O    1 
ATOM   2704 O O    B LEU   A 1 126 ? 18.007 -4.077  0.195   0.40 14.33 ?  126 LEU   A O    1 
ATOM   2705 C CB   A LEU   A 1 126 ? 15.552 -6.227  0.752   0.60 13.11 ?  126 LEU   A CB   1 
ATOM   2706 C CB   B LEU   A 1 126 ? 15.615 -6.064  0.499   0.40 12.92 ?  126 LEU   A CB   1 
ATOM   2707 C CG   A LEU   A 1 126 ? 14.718 -7.276  1.484   0.60 13.65 ?  126 LEU   A CG   1 
ATOM   2708 C CG   B LEU   A 1 126 ? 14.533 -6.811  1.270   0.40 13.19 ?  126 LEU   A CG   1 
ATOM   2709 C CD1  A LEU   A 1 126 ? 13.268 -7.160  1.070   0.60 14.41 ?  126 LEU   A CD1  1 
ATOM   2710 C CD1  B LEU   A 1 126 ? 13.236 -6.720  0.492   0.40 13.72 ?  126 LEU   A CD1  1 
ATOM   2711 C CD2  A LEU   A 1 126 ? 15.239 -8.692  1.220   0.60 13.55 ?  126 LEU   A CD2  1 
ATOM   2712 C CD2  B LEU   A 1 126 ? 14.934 -8.259  1.498   0.40 13.51 ?  126 LEU   A CD2  1 
ATOM   2713 H H    A LEU   A 1 126 ? 16.230 -4.642  2.552   0.60 14.26 ?  126 LEU   A H    1 
ATOM   2714 H H    B LEU   A 1 126 ? 16.194 -5.043  2.644   0.40 14.46 ?  126 LEU   A H    1 
ATOM   2715 H HA   A LEU   A 1 126 ? 17.338 -6.842  1.540   0.60 14.41 ?  126 LEU   A HA   1 
ATOM   2716 H HA   B LEU   A 1 126 ? 17.306 -6.961  1.250   0.40 15.42 ?  126 LEU   A HA   1 
ATOM   2717 H HB2  A LEU   A 1 126 ? 15.065 -5.392  0.789   0.60 15.71 ?  126 LEU   A HB2  1 
ATOM   2718 H HB2  B LEU   A 1 126 ? 15.316 -5.147  0.395   0.40 15.48 ?  126 LEU   A HB2  1 
ATOM   2719 H HB3  A LEU   A 1 126 ? 15.632 -6.514  -0.173  0.60 15.71 ?  126 LEU   A HB3  1 
ATOM   2720 H HB3  B LEU   A 1 126 ? 15.685 -6.481  -0.373  0.40 15.48 ?  126 LEU   A HB3  1 
ATOM   2721 H HG   A LEU   A 1 126 ? 14.772 -7.113  2.436   0.60 16.35 ?  126 LEU   A HG   1 
ATOM   2722 H HG   B LEU   A 1 126 ? 14.395 -6.385  2.132   0.40 15.80 ?  126 LEU   A HG   1 
ATOM   2723 H HD11 A LEU   A 1 126 ? 12.754 -7.841  1.535   0.60 17.27 ?  126 LEU   A HD11 1 
ATOM   2724 H HD11 B LEU   A 1 126 ? 12.545 -7.207  0.967   0.40 16.44 ?  126 LEU   A HD11 1 
ATOM   2725 H HD12 A LEU   A 1 126 ? 12.943 -6.280  1.308   0.60 17.27 ?  126 LEU   A HD12 1 
ATOM   2726 H HD12 B LEU   A 1 126 ? 12.981 -5.788  0.401   0.40 16.44 ?  126 LEU   A HD12 1 
ATOM   2727 H HD13 A LEU   A 1 126 ? 13.202 -7.293  0.112   0.60 17.27 ?  126 LEU   A HD13 1 
ATOM   2728 H HD13 B LEU   A 1 126 ? 13.368 -7.111  -0.388  0.40 16.44 ?  126 LEU   A HD13 1 
ATOM   2729 H HD21 A LEU   A 1 126 ? 14.647 -9.331  1.646   0.60 16.23 ?  126 LEU   A HD21 1 
ATOM   2730 H HD21 B LEU   A 1 126 ? 14.173 -8.745  1.847   0.40 16.19 ?  126 LEU   A HD21 1 
ATOM   2731 H HD22 A LEU   A 1 126 ? 15.260 -8.849  0.262   0.60 16.23 ?  126 LEU   A HD22 1 
ATOM   2732 H HD22 B LEU   A 1 126 ? 15.215 -8.640  0.652   0.40 16.19 ?  126 LEU   A HD22 1 
ATOM   2733 H HD23 A LEU   A 1 126 ? 16.134 -8.775  1.586   0.60 16.23 ?  126 LEU   A HD23 1 
ATOM   2734 H HD23 B LEU   A 1 126 ? 15.666 -8.282  2.133   0.40 16.19 ?  126 LEU   A HD23 1 
ATOM   2735 N N    A LEU   A 1 127 ? 18.917 -6.085  -0.125  0.60 11.06 ?  127 LEU   A N    1 
ATOM   2736 N N    B LEU   A 1 127 ? 18.754 -6.066  -0.540  0.40 12.92 ?  127 LEU   A N    1 
ATOM   2737 C CA   A LEU   A 1 127 ? 19.884 -5.589  -1.098  0.60 10.72 ?  127 LEU   A CA   1 
ATOM   2738 C CA   B LEU   A 1 127 ? 19.719 -5.497  -1.470  0.40 13.30 ?  127 LEU   A CA   1 
ATOM   2739 C C    A LEU   A 1 127 ? 19.252 -5.382  -2.469  0.60 9.90  ?  127 LEU   A C    1 
ATOM   2740 C C    B LEU   A 1 127 ? 19.179 -5.591  -2.895  0.40 14.08 ?  127 LEU   A C    1 
ATOM   2741 O O    A LEU   A 1 127 ? 18.381 -6.143  -2.906  0.60 10.19 ?  127 LEU   A O    1 
ATOM   2742 O O    B LEU   A 1 127 ? 18.491 -6.553  -3.247  0.40 13.87 ?  127 LEU   A O    1 
ATOM   2743 C CB   A LEU   A 1 127 ? 21.040 -6.580  -1.235  0.60 11.48 ?  127 LEU   A CB   1 
ATOM   2744 C CB   B LEU   A 1 127 ? 21.074 -6.211  -1.354  0.40 13.67 ?  127 LEU   A CB   1 
ATOM   2745 C CG   A LEU   A 1 127 ? 21.870 -6.809  0.024   0.60 12.23 ?  127 LEU   A CG   1 
ATOM   2746 C CG   B LEU   A 1 127 ? 21.789 -6.181  0.010   0.40 13.80 ?  127 LEU   A CG   1 
ATOM   2747 C CD1  A LEU   A 1 127 ? 22.980 -7.790  -0.260  0.60 12.35 ?  127 LEU   A CD1  1 
ATOM   2748 C CD1  B LEU   A 1 127 ? 23.062 -7.035  0.009   0.40 14.10 ?  127 LEU   A CD1  1 
ATOM   2749 C CD2  A LEU   A 1 127 ? 22.445 -5.500  0.520   0.60 12.64 ?  127 LEU   A CD2  1 
ATOM   2750 C CD2  B LEU   A 1 127 ? 22.115 -4.752  0.428   0.40 14.46 ?  127 LEU   A CD2  1 
ATOM   2751 H H    A LEU   A 1 127 ? 19.118 -6.854  0.202   0.60 13.25 ?  127 LEU   A H    1 
ATOM   2752 H H    B LEU   A 1 127 ? 18.742 -6.927  -0.527  0.40 15.49 ?  127 LEU   A H    1 
ATOM   2753 H HA   A LEU   A 1 127 ? 20.248 -4.739  -0.793  0.60 12.85 ?  127 LEU   A HA   1 
ATOM   2754 H HA   B LEU   A 1 127 ? 19.854 -4.563  -1.254  0.40 15.94 ?  127 LEU   A HA   1 
ATOM   2755 H HB2  A LEU   A 1 127 ? 20.679 -7.440  -1.510  0.60 13.76 ?  127 LEU   A HB2  1 
ATOM   2756 H HB2  B LEU   A 1 127 ? 20.946 -7.144  -1.580  0.40 16.38 ?  127 LEU   A HB2  1 
ATOM   2757 H HB3  A LEU   A 1 127 ? 21.647 -6.256  -1.926  0.60 13.76 ?  127 LEU   A HB3  1 
ATOM   2758 H HB3  B LEU   A 1 127 ? 21.680 -5.807  -1.993  0.40 16.38 ?  127 LEU   A HB3  1 
ATOM   2759 H HG   A LEU   A 1 127 ? 21.300 -7.183  0.717   0.60 14.65 ?  127 LEU   A HG   1 
ATOM   2760 H HG   B LEU   A 1 127 ? 21.199 -6.556  0.680   0.40 16.53 ?  127 LEU   A HG   1 
ATOM   2761 H HD11 A LEU   A 1 127 ? 23.482 -7.940  0.556   0.60 14.80 ?  127 LEU   A HD11 1 
ATOM   2762 H HD11 B LEU   A 1 127 ? 23.479 -6.987  0.887   0.40 16.89 ?  127 LEU   A HD11 1 
ATOM   2763 H HD12 A LEU   A 1 127 ? 22.596 -8.625  -0.571  0.60 14.80 ?  127 LEU   A HD12 1 
ATOM   2764 H HD12 B LEU   A 1 127 ? 22.828 -7.956  -0.191  0.40 16.89 ?  127 LEU   A HD12 1 
ATOM   2765 H HD13 A LEU   A 1 127 ? 23.560 -7.418  -0.942  0.60 14.80 ?  127 LEU   A HD13 1 
ATOM   2766 H HD13 B LEU   A 1 127 ? 23.673 -6.696  -0.663  0.40 16.89 ?  127 LEU   A HD13 1 
ATOM   2767 H HD21 A LEU   A 1 127 ? 23.118 -5.685  1.191   0.60 15.15 ?  127 LEU   A HD21 1 
ATOM   2768 H HD21 B LEU   A 1 127 ? 22.610 -4.772  1.263   0.40 17.33 ?  127 LEU   A HD21 1 
ATOM   2769 H HD22 A LEU   A 1 127 ? 22.844 -5.028  -0.230  0.60 15.15 ?  127 LEU   A HD22 1 
ATOM   2770 H HD22 B LEU   A 1 127 ? 22.649 -4.335  -0.264  0.40 17.33 ?  127 LEU   A HD22 1 
ATOM   2771 H HD23 A LEU   A 1 127 ? 21.732 -4.965  0.902   0.60 15.15 ?  127 LEU   A HD23 1 
ATOM   2772 H HD23 B LEU   A 1 127 ? 21.285 -4.267  0.547   0.40 17.33 ?  127 LEU   A HD23 1 
ATOM   2773 N N    A SER   A 1 128 ? 19.715 -4.341  -3.154  0.60 9.55  ?  128 SER   A N    1 
ATOM   2774 N N    B SER   A 1 128 ? 19.461 -4.568  -3.703  0.40 15.62 ?  128 SER   A N    1 
ATOM   2775 C CA   A SER   A 1 128 ? 19.341 -3.976  -4.515  0.60 9.91  ?  128 SER   A CA   1 
ATOM   2776 C CA   B SER   A 1 128 ? 19.035 -4.536  -5.108  0.40 17.20 ?  128 SER   A CA   1 
ATOM   2777 C C    A SER   A 1 128 ? 17.891 -3.533  -4.658  0.60 10.42 ?  128 SER   A C    1 
ATOM   2778 C C    B SER   A 1 128 ? 17.542 -4.827  -5.251  0.40 19.17 ?  128 SER   A C    1 
ATOM   2779 O O    A SER   A 1 128 ? 17.476 -3.239  -5.777  0.60 12.08 ?  128 SER   A O    1 
ATOM   2780 O O    B SER   A 1 128 ? 17.114 -5.564  -6.143  0.40 19.89 ?  128 SER   A O    1 
ATOM   2781 C CB   A SER   A 1 128 ? 19.650 -5.063  -5.554  0.60 9.95  ?  128 SER   A CB   1 
ATOM   2782 C CB   B SER   A 1 128 ? 19.844 -5.510  -5.966  0.40 16.77 ?  128 SER   A CB   1 
ATOM   2783 O OG   A SER   A 1 128 ? 21.050 -5.264  -5.665  0.60 10.85 ?  128 SER   A OG   1 
ATOM   2784 O OG   B SER   A 1 128 ? 21.229 -5.420  -5.692  0.40 16.38 ?  128 SER   A OG   1 
ATOM   2785 H H    A SER   A 1 128 ? 20.295 -3.795  -2.825  0.60 11.43 ?  128 SER   A H    1 
ATOM   2786 H H    B SER   A 1 128 ? 19.893 -3.871  -3.455  0.40 18.72 ?  128 SER   A H    1 
ATOM   2787 H HA   A SER   A 1 128 ? 19.870 -3.209  -4.755  0.60 11.87 ?  128 SER   A HA   1 
ATOM   2788 H HA   B SER   A 1 128 ? 19.201 -3.645  -5.451  0.40 20.62 ?  128 SER   A HA   1 
ATOM   2789 H HB2  A SER   A 1 128 ? 19.221 -5.886  -5.287  0.60 11.91 ?  128 SER   A HB2  1 
ATOM   2790 H HB2  B SER   A 1 128 ? 19.538 -6.412  -5.786  0.40 20.10 ?  128 SER   A HB2  1 
ATOM   2791 H HB3  A SER   A 1 128 ? 19.307 -4.771  -6.418  0.60 11.91 ?  128 SER   A HB3  1 
ATOM   2792 H HB3  B SER   A 1 128 ? 19.694 -5.294  -6.903  0.40 20.10 ?  128 SER   A HB3  1 
ATOM   2793 H HG   A SER   A 1 128 ? 21.418 -4.528  -5.862  0.60 13.00 ?  128 SER   A HG   1 
ATOM   2794 H HG   B SER   A 1 128 ? 21.493 -4.638  -5.841  0.40 19.63 ?  128 SER   A HG   1 
ATOM   2795 N N    A ALA   A 1 129 ? 17.132 -3.441  -3.568  0.60 11.89 ?  129 ALA   A N    1 
ATOM   2796 N N    B ALA   A 1 129 ? 16.734 -4.242  -4.368  0.40 20.08 ?  129 ALA   A N    1 
ATOM   2797 C CA   A ALA   A 1 129 ? 15.763 -2.947  -3.608  0.60 13.00 ?  129 ALA   A CA   1 
ATOM   2798 C CA   B ALA   A 1 129 ? 15.310 -4.561  -4.312  0.40 20.93 ?  129 ALA   A CA   1 
ATOM   2799 C C    A ALA   A 1 129 ? 15.769 -1.415  -3.568  0.60 12.55 ?  129 ALA   A C    1 
ATOM   2800 C C    B ALA   A 1 129 ? 14.429 -3.472  -4.915  0.40 21.56 ?  129 ALA   A C    1 
ATOM   2801 O O    A ALA   A 1 129 ? 16.819 -0.765  -3.630  0.60 12.64 ?  129 ALA   A O    1 
ATOM   2802 O O    B ALA   A 1 129 ? 13.636 -3.745  -5.821  0.40 22.00 ?  129 ALA   A O    1 
ATOM   2803 C CB   A ALA   A 1 129 ? 14.947 -3.599  -2.491  0.60 15.00 ?  129 ALA   A CB   1 
ATOM   2804 C CB   B ALA   A 1 129 ? 14.898 -4.838  -2.863  0.40 21.16 ?  129 ALA   A CB   1 
ATOM   2805 H H    A ALA   A 1 129 ? 17.400 -3.662  -2.772  0.60 14.25 ?  129 ALA   A H    1 
ATOM   2806 H H    B ALA   A 1 129 ? 16.988 -3.664  -3.782  0.40 24.08 ?  129 ALA   A H    1 
ATOM   2807 H HA   A ALA   A 1 129 ? 15.370 -3.215  -4.444  0.60 15.58 ?  129 ALA   A HA   1 
ATOM   2808 H HA   B ALA   A 1 129 ? 15.157 -5.367  -4.823  0.40 25.10 ?  129 ALA   A HA   1 
ATOM   2809 H HB1  A ALA   A 1 129 ? 14.036 -3.272  -2.529  0.60 17.98 ?  129 ALA   A HB1  1 
ATOM   2810 H HB1  B ALA   A 1 129 ? 13.948 -5.027  -2.841  0.40 25.37 ?  129 ALA   A HB1  1 
ATOM   2811 H HB2  A ALA   A 1 129 ? 14.952 -4.567  -2.617  0.60 17.98 ?  129 ALA   A HB2  1 
ATOM   2812 H HB2  B ALA   A 1 129 ? 15.398 -5.603  -2.540  0.40 25.37 ?  129 ALA   A HB2  1 
ATOM   2813 H HB3  A ALA   A 1 129 ? 15.342 -3.384  -1.631  0.60 17.98 ?  129 ALA   A HB3  1 
ATOM   2814 H HB3  B ALA   A 1 129 ? 15.095 -4.058  -2.325  0.40 25.37 ?  129 ALA   A HB3  1 
ATOM   2815 N N    A GLY   A 1 130 ? 14.584 -0.821  -3.478  0.60 12.60 ?  130 GLY   A N    1 
ATOM   2816 N N    B GLY   A 1 130 ? 14.545 -2.242  -4.424  0.40 21.89 ?  130 GLY   A N    1 
ATOM   2817 C CA   A GLY   A 1 130 ? 14.499 0.628   -3.417  0.60 13.20 ?  130 GLY   A CA   1 
ATOM   2818 C CA   B GLY   A 1 130 ? 13.551 -1.246  -4.775  0.40 22.10 ?  130 GLY   A CA   1 
ATOM   2819 C C    A GLY   A 1 130 ? 15.121 1.250   -4.649  0.60 12.56 ?  130 GLY   A C    1 
ATOM   2820 C C    B GLY   A 1 130 ? 12.241 -1.567  -4.084  0.40 22.30 ?  130 GLY   A C    1 
ATOM   2821 O O    A GLY   A 1 130 ? 14.898 0.807   -5.778  0.60 12.87 ?  130 GLY   A O    1 
ATOM   2822 O O    B GLY   A 1 130 ? 12.210 -2.050  -2.948  0.40 21.21 ?  130 GLY   A O    1 
ATOM   2823 H H    A GLY   A 1 130 ? 13.831 -1.235  -3.445  0.60 15.10 ?  130 GLY   A H    1 
ATOM   2824 H H    B GLY   A 1 130 ? 15.168 -1.966  -3.900  0.40 26.25 ?  130 GLY   A H    1 
ATOM   2825 H HA2  A GLY   A 1 130 ? 13.568 0.894   -3.355  0.60 15.81 ?  130 GLY   A HA2  1 
ATOM   2826 H HA2  B GLY   A 1 130 ? 13.842 -0.368  -4.490  0.40 26.49 ?  130 GLY   A HA2  1 
ATOM   2827 H HA3  A GLY   A 1 130 ? 14.969 0.951   -2.631  0.60 15.81 ?  130 GLY   A HA3  1 
ATOM   2828 H HA3  B GLY   A 1 130 ? 13.409 -1.241  -5.733  0.40 26.49 ?  130 GLY   A HA3  1 
ATOM   2829 N N    A ILE   A 1 131 ? 15.930 2.290   -4.430  0.60 12.11 ?  131 ILE   A N    1 
ATOM   2830 N N    B ILE   A 1 131 ? 11.134 -1.307  -4.766  0.40 24.20 ?  131 ILE   A N    1 
ATOM   2831 C CA   A ILE   A 1 131 ? 16.515 3.045   -5.536  0.60 11.99 ?  131 ILE   A CA   1 
ATOM   2832 C CA   B ILE   A 1 131 ? 9.849  -1.594  -4.147  0.40 26.39 ?  131 ILE   A CA   1 
ATOM   2833 C C    A ILE   A 1 131 ? 17.539 2.255   -6.334  0.60 11.53 ?  131 ILE   A C    1 
ATOM   2834 C C    B ILE   A 1 131 ? 8.830  -2.011  -5.199  0.40 27.92 ?  131 ILE   A C    1 
ATOM   2835 O O    A ILE   A 1 131 ? 17.972 2.732   -7.389  0.60 12.26 ?  131 ILE   A O    1 
ATOM   2836 O O    B ILE   A 1 131 ? 7.845  -2.691  -4.887  0.40 28.13 ?  131 ILE   A O    1 
ATOM   2837 C CB   A ILE   A 1 131 ? 17.077 4.416   -5.094  0.60 13.12 ?  131 ILE   A CB   1 
ATOM   2838 C CB   B ILE   A 1 131 ? 9.392  -0.391  -3.297  0.40 27.29 ?  131 ILE   A CB   1 
ATOM   2839 C CG1  A ILE   A 1 131 ? 18.288 4.253   -4.169  0.60 14.18 ?  131 ILE   A CG1  1 
ATOM   2840 C CG1  B ILE   A 1 131 ? 8.336  -0.810  -2.272  0.40 27.67 ?  131 ILE   A CG1  1 
ATOM   2841 C CG2  A ILE   A 1 131 ? 15.975 5.247   -4.436  0.60 13.91 ?  131 ILE   A CG2  1 
ATOM   2842 C CG2  B ILE   A 1 131 ? 8.923  0.737   -4.181  0.40 27.56 ?  131 ILE   A CG2  1 
ATOM   2843 C CD1  A ILE   A 1 131 ? 18.925 5.578   -3.752  0.60 15.46 ?  131 ILE   A CD1  1 
ATOM   2844 C CD1  B ILE   A 1 131 ? 6.925  -0.734  -2.753  0.40 27.73 ?  131 ILE   A CD1  1 
ATOM   2845 H H    A ILE   A 1 131 ? 16.141 2.574   -3.654  0.60 14.51 ?  131 ILE   A H    1 
ATOM   2846 H H    B ILE   A 1 131 ? 11.104 -0.964  -5.556  0.40 29.02 ?  131 ILE   A H    1 
ATOM   2847 H HA   A ILE   A 1 131 ? 15.798 3.237   -6.155  0.60 14.37 ?  131 ILE   A HA   1 
ATOM   2848 H HA   B ILE   A 1 131 ? 9.962  -2.346  -3.547  0.40 31.64 ?  131 ILE   A HA   1 
ATOM   2849 H HB   A ILE   A 1 131 ? 17.366 4.887   -5.891  0.60 15.72 ?  131 ILE   A HB   1 
ATOM   2850 H HB   B ILE   A 1 131 ? 10.164 -0.074  -2.806  0.40 32.72 ?  131 ILE   A HB   1 
ATOM   2851 H HG12 A ILE   A 1 131 ? 18.007 3.792   -3.365  0.60 17.00 ?  131 ILE   A HG12 1 
ATOM   2852 H HG12 B ILE   A 1 131 ? 8.499  -1.731  -2.027  0.40 33.18 ?  131 ILE   A HG12 1 
ATOM   2853 H HG13 A ILE   A 1 131 ? 18.965 3.733   -4.628  0.60 17.00 ?  131 ILE   A HG13 1 
ATOM   2854 H HG13 B ILE   A 1 131 ? 8.418  -0.242  -1.488  0.40 33.18 ?  131 ILE   A HG13 1 
ATOM   2855 H HG21 A ILE   A 1 131 ? 16.295 6.153   -4.308  0.60 16.67 ?  131 ILE   A HG21 1 
ATOM   2856 H HG21 B ILE   A 1 131 ? 8.593  1.450   -3.617  0.40 33.05 ?  131 ILE   A HG21 1 
ATOM   2857 H HG22 A ILE   A 1 131 ? 15.196 5.253   -5.017  0.60 16.67 ?  131 ILE   A HG22 1 
ATOM   2858 H HG22 B ILE   A 1 131 ? 9.675  1.044   -4.705  0.40 33.05 ?  131 ILE   A HG22 1 
ATOM   2859 H HG23 A ILE   A 1 131 ? 15.746 4.849   -3.583  0.60 16.67 ?  131 ILE   A HG23 1 
ATOM   2860 H HG23 B ILE   A 1 131 ? 8.221  0.423   -4.764  0.40 33.05 ?  131 ILE   A HG23 1 
ATOM   2861 H HD11 A ILE   A 1 131 ? 19.747 5.395   -3.267  0.60 18.53 ?  131 ILE   A HD11 1 
ATOM   2862 H HD11 B ILE   A 1 131 ? 6.419  -1.403  -2.278  0.40 33.25 ?  131 ILE   A HD11 1 
ATOM   2863 H HD12 A ILE   A 1 131 ? 19.123 6.100   -4.547  0.60 18.53 ?  131 ILE   A HD12 1 
ATOM   2864 H HD12 B ILE   A 1 131 ? 6.575  0.150   -2.563  0.40 33.25 ?  131 ILE   A HD12 1 
ATOM   2865 H HD13 A ILE   A 1 131 ? 18.308 6.065   -3.183  0.60 18.53 ?  131 ILE   A HD13 1 
ATOM   2866 H HD13 B ILE   A 1 131 ? 6.892  -0.915  -3.702  0.40 33.25 ?  131 ILE   A HD13 1 
ATOM   2867 N N    A PHE   A 1 132 ? 17.938 1.065   -5.875  0.60 11.28 ?  132 PHE   A N    1 
ATOM   2868 N N    B PHE   A 1 132 ? 9.069  -1.636  -6.452  0.40 29.20 ?  132 PHE   A N    1 
ATOM   2869 C CA   A PHE   A 1 132 ? 18.791 0.209   -6.691  0.60 11.55 ?  132 PHE   A CA   1 
ATOM   2870 C CA   B PHE   A 1 132 ? 8.130  -1.897  -7.531  0.40 30.64 ?  132 PHE   A CA   1 
ATOM   2871 C C    A PHE   A 1 132 ? 18.017 -0.531  -7.778  0.60 12.44 ?  132 PHE   A C    1 
ATOM   2872 C C    B PHE   A 1 132 ? 8.480  -3.179  -8.279  0.40 30.97 ?  132 PHE   A C    1 
ATOM   2873 O O    A PHE   A 1 132 ? 18.639 -1.167  -8.634  0.60 13.14 ?  132 PHE   A O    1 
ATOM   2874 O O    B PHE   A 1 132 ? 9.652  -3.455  -8.557  0.40 30.79 ?  132 PHE   A O    1 
ATOM   2875 C CB   A PHE   A 1 132 ? 19.573 -0.788  -5.821  0.60 10.86 ?  132 PHE   A CB   1 
ATOM   2876 C CB   B PHE   A 1 132 ? 8.116  -0.726  -8.515  0.40 31.73 ?  132 PHE   A CB   1 
ATOM   2877 C CG   A PHE   A 1 132 ? 20.782 -0.197  -5.124  0.60 10.50 ?  132 PHE   A CG   1 
ATOM   2878 C CG   B PHE   A 1 132 ? 7.214  -0.940  -9.694  0.40 32.79 ?  132 PHE   A CG   1 
ATOM   2879 C CD1  A PHE   A 1 132 ? 20.641 0.820   -4.194  0.60 11.41 ?  132 PHE   A CD1  1 
ATOM   2880 C CD1  B PHE   A 1 132 ? 5.869  -0.626  -9.618  0.40 33.24 ?  132 PHE   A CD1  1 
ATOM   2881 C CD2  A PHE   A 1 132 ? 22.054 -0.695  -5.372  0.60 11.30 ?  132 PHE   A CD2  1 
ATOM   2882 C CD2  B PHE   A 1 132 ? 7.712  -1.459  -10.879 0.40 33.32 ?  132 PHE   A CD2  1 
ATOM   2883 C CE1  A PHE   A 1 132 ? 21.746 1.346   -3.546  0.60 11.67 ?  132 PHE   A CE1  1 
ATOM   2884 C CE1  B PHE   A 1 132 ? 5.036  -0.824  -10.702 0.40 33.55 ?  132 PHE   A CE1  1 
ATOM   2885 C CE2  A PHE   A 1 132 ? 23.160 -0.172  -4.727  0.60 11.82 ?  132 PHE   A CE2  1 
ATOM   2886 C CE2  B PHE   A 1 132 ? 6.883  -1.659  -11.966 0.40 33.58 ?  132 PHE   A CE2  1 
ATOM   2887 C CZ   A PHE   A 1 132 ? 23.005 0.849   -3.811  0.60 11.54 ?  132 PHE   A CZ   1 
ATOM   2888 C CZ   B PHE   A 1 132 ? 5.543  -1.340  -11.878 0.40 33.68 ?  132 PHE   A CZ   1 
ATOM   2889 H H    A PHE   A 1 132 ? 17.734 0.739   -5.103  0.60 13.51 ?  132 PHE   A H    1 
ATOM   2890 H H    B PHE   A 1 132 ? 9.774  -1.208  -6.708  0.40 35.02 ?  132 PHE   A H    1 
ATOM   2891 H HA   A PHE   A 1 132 ? 19.447 0.768   -7.132  0.60 13.84 ?  132 PHE   A HA   1 
ATOM   2892 H HA   B PHE   A 1 132 ? 7.239  -1.993  -7.157  0.40 36.74 ?  132 PHE   A HA   1 
ATOM   2893 H HB2  A PHE   A 1 132 ? 18.982 -1.132  -5.133  0.60 13.00 ?  132 PHE   A HB2  1 
ATOM   2894 H HB2  B PHE   A 1 132 ? 7.813  0.069   -8.049  0.40 38.05 ?  132 PHE   A HB2  1 
ATOM   2895 H HB3  A PHE   A 1 132 ? 19.884 -1.520  -6.381  0.60 13.00 ?  132 PHE   A HB3  1 
ATOM   2896 H HB3  B PHE   A 1 132 ? 9.016  -0.590  -8.848  0.40 38.05 ?  132 PHE   A HB3  1 
ATOM   2897 H HD1  A PHE   A 1 132 ? 19.797 1.157   -4.008  0.60 13.67 ?  132 PHE   A HD1  1 
ATOM   2898 H HD1  B PHE   A 1 132 ? 5.522  -0.277  -8.827  0.40 39.87 ?  132 PHE   A HD1  1 
ATOM   2899 H HD2  A PHE   A 1 132 ? 22.163 -1.385  -5.991  0.60 13.54 ?  132 PHE   A HD2  1 
ATOM   2900 H HD2  B PHE   A 1 132 ? 8.614  -1.676  -10.943 0.40 39.96 ?  132 PHE   A HD2  1 
ATOM   2901 H HE1  A PHE   A 1 132 ? 21.641 2.034   -2.929  0.60 13.98 ?  132 PHE   A HE1  1 
ATOM   2902 H HE1  B PHE   A 1 132 ? 4.135  -0.609  -10.640 0.40 40.24 ?  132 PHE   A HE1  1 
ATOM   2903 H HE2  A PHE   A 1 132 ? 24.007 -0.512  -4.914  0.60 14.16 ?  132 PHE   A HE2  1 
ATOM   2904 H HE2  B PHE   A 1 132 ? 7.229  -2.007  -12.756 0.40 40.28 ?  132 PHE   A HE2  1 
ATOM   2905 H HZ   A PHE   A 1 132 ? 23.747 1.203   -3.381  0.60 13.83 ?  132 PHE   A HZ   1 
ATOM   2906 H HZ   B PHE   A 1 132 ? 4.983  -1.474  -12.608 0.40 40.39 ?  132 PHE   A HZ   1 
ATOM   2907 N N    A GLY   A 1 133 ? 16.687 -0.494  -7.755  0.60 12.32 ?  133 GLY   A N    1 
ATOM   2908 N N    B GLY   A 1 133 ? 7.449  -3.965  -8.583  0.40 31.49 ?  133 GLY   A N    1 
ATOM   2909 C CA   A GLY   A 1 133 ? 15.897 -0.844  -8.917  0.60 13.11 ?  133 GLY   A CA   1 
ATOM   2910 C CA   B GLY   A 1 133 ? 7.504  -5.018  -9.582  0.40 31.89 ?  133 GLY   A CA   1 
ATOM   2911 C C    A GLY   A 1 133 ? 15.505 -2.298  -9.086  0.60 13.69 ?  133 GLY   A C    1 
ATOM   2912 C C    B GLY   A 1 133 ? 8.611  -6.054  -9.477  0.40 32.22 ?  133 GLY   A C    1 
ATOM   2913 O O    A GLY   A 1 133 ? 14.787 -2.605  -10.045 0.60 14.95 ?  133 GLY   A O    1 
ATOM   2914 O O    B GLY   A 1 133 ? 9.741  -5.823  -9.918  0.40 32.62 ?  133 GLY   A O    1 
ATOM   2915 H H    A GLY   A 1 133 ? 16.218 -0.256  -7.071  0.60 14.76 ?  133 GLY   A H    1 
ATOM   2916 H H    B GLY   A 1 133 ? 6.679  -3.898  -8.206  0.40 37.76 ?  133 GLY   A H    1 
ATOM   2917 H HA2  A GLY   A 1 133 ? 15.074 -0.333  -8.893  0.60 15.71 ?  133 GLY   A HA2  1 
ATOM   2918 H HA2  B GLY   A 1 133 ? 6.654  -5.491  -9.558  0.40 38.25 ?  133 GLY   A HA2  1 
ATOM   2919 H HA3  A GLY   A 1 133 ? 16.386 -0.580  -9.711  0.60 15.71 ?  133 GLY   A HA3  1 
ATOM   2920 H HA3  B GLY   A 1 133 ? 7.569  -4.596  -10.453 0.40 38.25 ?  133 GLY   A HA3  1 
ATOM   2921 N N    A ALA   A 1 134 ? 15.937 -3.201  -8.207  0.60 12.87 ?  134 ALA   A N    1 
ATOM   2922 N N    B ALA   A 1 134 ? 8.279  -7.206  -8.889  0.40 31.90 ?  134 ALA   A N    1 
ATOM   2923 C CA   A ALA   A 1 134 ? 15.569 -4.601  -8.349  0.60 12.95 ?  134 ALA   A CA   1 
ATOM   2924 C CA   B ALA   A 1 134 ? 9.062  -8.441  -8.954  0.40 31.34 ?  134 ALA   A CA   1 
ATOM   2925 C C    A ALA   A 1 134 ? 14.232 -4.873  -7.657  0.60 13.04 ?  134 ALA   A C    1 
ATOM   2926 C C    B ALA   A 1 134 ? 10.573 -8.255  -8.865  0.40 30.49 ?  134 ALA   A C    1 
ATOM   2927 O O    A ALA   A 1 134 ? 13.735 -4.072  -6.865  0.60 14.01 ?  134 ALA   A O    1 
ATOM   2928 O O    B ALA   A 1 134 ? 11.331 -9.020  -9.471  0.40 31.20 ?  134 ALA   A O    1 
ATOM   2929 C CB   A ALA   A 1 134 ? 16.669 -5.516  -7.806  0.60 13.60 ?  134 ALA   A CB   1 
ATOM   2930 C CB   B ALA   A 1 134 ? 8.695  -9.243  -10.208 0.40 31.53 ?  134 ALA   A CB   1 
ATOM   2931 H H    A ALA   A 1 134 ? 16.445 -3.024  -7.527  0.60 15.42 ?  134 ALA   A H    1 
ATOM   2932 H H    B ALA   A 1 134 ? 7.573  -7.294  -8.413  0.40 38.26 ?  134 ALA   A H    1 
ATOM   2933 H HA   A ALA   A 1 134 ? 15.462 -4.797  -9.291  0.60 15.52 ?  134 ALA   A HA   1 
ATOM   2934 H HA   B ALA   A 1 134 ? 8.815  -8.983  -8.196  0.40 37.59 ?  134 ALA   A HA   1 
ATOM   2935 H HB1  A ALA   A 1 134 ? 16.404 -6.437  -7.940  0.60 16.30 ?  134 ALA   A HB1  1 
ATOM   2936 H HB1  B ALA   A 1 134 ? 9.213  -10.065 -10.222 0.40 37.82 ?  134 ALA   A HB1  1 
ATOM   2937 H HB2  A ALA   A 1 134 ? 17.495 -5.335  -8.288  0.60 16.30 ?  134 ALA   A HB2  1 
ATOM   2938 H HB2  B ALA   A 1 134 ? 7.747  -9.455  -10.180 0.40 37.82 ?  134 ALA   A HB2  1 
ATOM   2939 H HB3  A ALA   A 1 134 ? 16.794 -5.337  -6.862  0.60 16.30 ?  134 ALA   A HB3  1 
ATOM   2940 H HB3  B ALA   A 1 134 ? 8.892  -8.716  -10.997 0.40 37.82 ?  134 ALA   A HB3  1 
ATOM   2941 N N    A ASP   A 1 135 ? 13.658 -6.033  -7.964  0.60 13.41 ?  135 ASP   A N    1 
ATOM   2942 N N    B ASP   A 1 135 ? 11.020 -7.263  -8.104  0.40 28.59 ?  135 ASP   A N    1 
ATOM   2943 C CA   A ASP   A 1 135 ? 12.400 -6.459  -7.357  0.60 14.92 ?  135 ASP   A CA   1 
ATOM   2944 C CA   B ASP   A 1 135 ? 12.437 -7.099  -7.801  0.40 26.53 ?  135 ASP   A CA   1 
ATOM   2945 C C    A ASP   A 1 135 ? 12.654 -6.929  -5.925  0.60 14.35 ?  135 ASP   A C    1 
ATOM   2946 C C    B ASP   A 1 135 ? 12.695 -7.361  -6.318  0.40 22.68 ?  135 ASP   A C    1 
ATOM   2947 O O    A ASP   A 1 135 ? 13.419 -7.884  -5.724  0.60 13.69 ?  135 ASP   A O    1 
ATOM   2948 O O    B ASP   A 1 135 ? 13.612 -8.122  -5.986  0.40 21.84 ?  135 ASP   A O    1 
ATOM   2949 C CB   A ASP   A 1 135 ? 11.822 -7.601  -8.186  0.60 17.19 ?  135 ASP   A CB   1 
ATOM   2950 C CB   B ASP   A 1 135 ? 12.947 -5.721  -8.236  0.40 28.41 ?  135 ASP   A CB   1 
ATOM   2951 C CG   A ASP   A 1 135 ? 10.639 -8.289  -7.522  0.60 19.75 ?  135 ASP   A CG   1 
ATOM   2952 C CG   B ASP   A 1 135 ? 13.536 -5.731  -9.632  0.40 30.05 ?  135 ASP   A CG   1 
ATOM   2953 O OD1  A ASP   A 1 135 ? 9.988  -7.683  -6.647  0.60 19.65 ?  135 ASP   A OD1  1 
ATOM   2954 O OD1  B ASP   A 1 135 ? 12.843 -6.180  -10.569 0.40 30.82 ?  135 ASP   A OD1  1 
ATOM   2955 O OD2  A ASP   A 1 135 ? 10.395 -9.460  -7.870  0.60 22.89 -1 135 ASP   A OD2  1 
ATOM   2956 O OD2  B ASP   A 1 135 ? 14.689 -5.278  -9.795  0.40 30.64 -1 135 ASP   A OD2  1 
ATOM   2957 H H    A ASP   A 1 135 ? 13.975 -6.593  -8.530  0.60 16.07 ?  135 ASP   A H    1 
ATOM   2958 H H    B ASP   A 1 135 ? 10.515 -6.670  -7.756  0.40 34.29 ?  135 ASP   A H    1 
ATOM   2959 H HA   A ASP   A 1 135 ? 11.768 -5.715  -7.363  0.60 17.88 ?  135 ASP   A HA   1 
ATOM   2960 H HA   B ASP   A 1 135 ? 12.942 -7.756  -8.300  0.40 31.82 ?  135 ASP   A HA   1 
ATOM   2961 H HB2  A ASP   A 1 135 ? 11.555 -7.252  -9.052  0.60 20.60 ?  135 ASP   A HB2  1 
ATOM   2962 H HB2  B ASP   A 1 135 ? 12.215 -5.090  -8.248  0.40 34.07 ?  135 ASP   A HB2  1 
ATOM   2963 H HB3  A ASP   A 1 135 ? 12.508 -8.276  -8.301  0.60 20.60 ?  135 ASP   A HB3  1 
ATOM   2964 H HB3  B ASP   A 1 135 ? 13.639 -5.426  -7.625  0.40 34.07 ?  135 ASP   A HB3  1 
ATOM   2965 N N    A PRO   A 1 136 ? 12.062 -6.284  -4.910  0.60 14.14 ?  136 PRO   A N    1 
ATOM   2966 N N    B PRO   A 1 136 ? 11.921 -6.773  -5.395  0.40 19.94 ?  136 PRO   A N    1 
ATOM   2967 C CA   A PRO   A 1 136 ? 12.317 -6.704  -3.518  0.60 14.12 ?  136 PRO   A CA   1 
ATOM   2968 C CA   B PRO   A 1 136 ? 12.135 -7.112  -3.978  0.40 18.29 ?  136 PRO   A CA   1 
ATOM   2969 C C    A PRO   A 1 136 ? 11.872 -8.128  -3.209  0.60 13.70 ?  136 PRO   A C    1 
ATOM   2970 C C    B PRO   A 1 136 ? 11.800 -8.554  -3.657  0.40 16.89 ?  136 PRO   A C    1 
ATOM   2971 O O    A PRO   A 1 136 ? 12.451 -8.777  -2.329  0.60 12.73 ?  136 PRO   A O    1 
ATOM   2972 O O    B PRO   A 1 136 ? 12.493 -9.175  -2.842  0.40 16.54 ?  136 PRO   A O    1 
ATOM   2973 C CB   A PRO   A 1 136 ? 11.540 -5.661  -2.696  0.60 15.14 ?  136 PRO   A CB   1 
ATOM   2974 C CB   B PRO   A 1 136 ? 11.221 -6.131  -3.228  0.40 18.70 ?  136 PRO   A CB   1 
ATOM   2975 C CG   A PRO   A 1 136 ? 10.469 -5.173  -3.636  0.60 15.97 ?  136 PRO   A CG   1 
ATOM   2976 C CG   B PRO   A 1 136 ? 10.930 -5.050  -4.201  0.40 19.02 ?  136 PRO   A CG   1 
ATOM   2977 C CD   A PRO   A 1 136 ? 11.148 -5.125  -4.970  0.60 14.90 ?  136 PRO   A CD   1 
ATOM   2978 C CD   B PRO   A 1 136 ? 10.905 -5.717  -5.539  0.40 19.32 ?  136 PRO   A CD   1 
ATOM   2979 H HA   A PRO   A 1 136 ? 13.265 -6.602  -3.307  0.60 16.92 ?  136 PRO   A HA   1 
ATOM   2980 H HA   B PRO   A 1 136 ? 13.057 -6.943  -3.728  0.40 21.92 ?  136 PRO   A HA   1 
ATOM   2981 H HB2  A PRO   A 1 136 ? 11.148 -6.075  -1.914  0.60 18.14 ?  136 PRO   A HB2  1 
ATOM   2982 H HB2  B PRO   A 1 136 ? 10.406 -6.587  -2.961  0.40 22.41 ?  136 PRO   A HB2  1 
ATOM   2983 H HB3  A PRO   A 1 136 ? 12.125 -4.922  -2.436  0.60 18.14 ?  136 PRO   A HB3  1 
ATOM   2984 H HB3  B PRO   A 1 136 ? 11.687 -5.783  -2.451  0.40 22.41 ?  136 PRO   A HB3  1 
ATOM   2985 H HG2  A PRO   A 1 136 ? 9.736  -5.806  -3.651  0.60 19.14 ?  136 PRO   A HG2  1 
ATOM   2986 H HG2  B PRO   A 1 136 ? 10.068 -4.657  -3.995  0.40 22.79 ?  136 PRO   A HG2  1 
ATOM   2987 H HG3  A PRO   A 1 136 ? 10.164 -4.293  -3.370  0.60 19.14 ?  136 PRO   A HG3  1 
ATOM   2988 H HG3  B PRO   A 1 136 ? 11.632 -4.384  -4.162  0.40 22.79 ?  136 PRO   A HG3  1 
ATOM   2989 H HD2  A PRO   A 1 136 ? 10.496 -5.240  -5.681  0.60 17.85 ?  136 PRO   A HD2  1 
ATOM   2990 H HD2  B PRO   A 1 136 ? 10.031 -6.106  -5.699  0.40 23.16 ?  136 PRO   A HD2  1 
ATOM   2991 H HD3  A PRO   A 1 136 ? 11.637 -4.286  -5.074  0.60 17.85 ?  136 PRO   A HD3  1 
ATOM   2992 H HD3  B PRO   A 1 136 ? 11.152 -5.086  -6.227  0.40 23.16 ?  136 PRO   A HD3  1 
ATOM   2993 N N    A ILE   A 1 137 ? 10.841 -8.627  -3.888  0.60 14.33 ?  137 ILE   A N    1 
ATOM   2994 N N    B ILE   A 1 137 ? 10.740 -9.105  -4.258  0.40 16.26 ?  137 ILE   A N    1 
ATOM   2995 C CA   A ILE   A 1 137 ? 10.449 -10.019 -3.691  0.60 14.69 ?  137 ILE   A CA   1 
ATOM   2996 C CA   B ILE   A 1 137 ? 10.460 -10.527 -4.085  0.40 16.08 ?  137 ILE   A CA   1 
ATOM   2997 C C    A ILE   A 1 137 ? 11.585 -10.947 -4.103  0.60 14.56 ?  137 ILE   A C    1 
ATOM   2998 C C    B ILE   A 1 137 ? 11.693 -11.330 -4.455  0.40 15.52 ?  137 ILE   A C    1 
ATOM   2999 O O    A ILE   A 1 137 ? 11.898 -11.929 -3.414  0.60 14.62 ?  137 ILE   A O    1 
ATOM   3000 O O    B ILE   A 1 137 ? 12.066 -12.291 -3.769  0.40 15.19 ?  137 ILE   A O    1 
ATOM   3001 C CB   A ILE   A 1 137 ? 9.154  -10.313 -4.469  0.60 15.76 ?  137 ILE   A CB   1 
ATOM   3002 C CB   B ILE   A 1 137 ? 9.236  -10.950 -4.922  0.40 16.91 ?  137 ILE   A CB   1 
ATOM   3003 C CG1  A ILE   A 1 137 ? 7.973  -9.531  -3.873  0.60 16.80 ?  137 ILE   A CG1  1 
ATOM   3004 C CG1  B ILE   A 1 137 ? 8.019  -10.067 -4.622  0.40 17.64 ?  137 ILE   A CG1  1 
ATOM   3005 C CG2  A ILE   A 1 137 ? 8.879  -11.805 -4.477  0.60 16.91 ?  137 ILE   A CG2  1 
ATOM   3006 C CG2  B ILE   A 1 137 ? 8.905  -12.419 -4.660  0.40 17.00 ?  137 ILE   A CG2  1 
ATOM   3007 C CD1  A ILE   A 1 137 ? 6.681  -9.681  -4.649  0.60 18.46 ?  137 ILE   A CD1  1 
ATOM   3008 C CD1  B ILE   A 1 137 ? 6.868  -10.261 -5.596  0.40 18.19 ?  137 ILE   A CD1  1 
ATOM   3009 H H    A ILE   A 1 137 ? 10.365 -8.174  -4.449  0.60 17.17 ?  137 ILE   A H    1 
ATOM   3010 H H    B ILE   A 1 137 ? 10.192 -8.689  -4.766  0.40 19.49 ?  137 ILE   A H    1 
ATOM   3011 H HA   A ILE   A 1 137 ? 10.267 -10.148 -2.748  0.60 17.61 ?  137 ILE   A HA   1 
ATOM   3012 H HA   B ILE   A 1 137 ? 10.261 -10.710 -3.157  0.40 19.27 ?  137 ILE   A HA   1 
ATOM   3013 H HB   A ILE   A 1 137 ? 9.274  -10.013 -5.382  0.60 18.88 ?  137 ILE   A HB   1 
ATOM   3014 H HB   B ILE   A 1 137 ? 9.451  -10.855 -5.861  0.40 20.27 ?  137 ILE   A HB   1 
ATOM   3015 H HG12 A ILE   A 1 137 ? 7.808  -9.843  -2.970  0.60 20.13 ?  137 ILE   A HG12 1 
ATOM   3016 H HG12 B ILE   A 1 137 ? 7.693  -10.274 -3.734  0.40 21.14 ?  137 ILE   A HG12 1 
ATOM   3017 H HG13 A ILE   A 1 137 ? 8.191  -8.583  -3.856  0.60 20.13 ?  137 ILE   A HG13 1 
ATOM   3018 H HG13 B ILE   A 1 137 ? 8.279  -9.134  -4.666  0.40 21.14 ?  137 ILE   A HG13 1 
ATOM   3019 H HG21 A ILE   A 1 137 ? 8.017  -11.970 -4.883  0.60 20.27 ?  137 ILE   A HG21 1 
ATOM   3020 H HG21 B ILE   A 1 137 ? 8.081  -12.651 -5.120  0.40 20.38 ?  137 ILE   A HG21 1 
ATOM   3021 H HG22 A ILE   A 1 137 ? 9.565  -12.247 -4.993  0.60 20.27 ?  137 ILE   A HG22 1 
ATOM   3022 H HG22 B ILE   A 1 137 ? 9.628  -12.972 -4.991  0.40 20.38 ?  137 ILE   A HG22 1 
ATOM   3023 H HG23 A ILE   A 1 137 ? 8.883  -12.126 -3.564  0.60 20.27 ?  137 ILE   A HG23 1 
ATOM   3024 H HG23 B ILE   A 1 137 ? 8.795  -12.553 -3.705  0.40 20.38 ?  137 ILE   A HG23 1 
ATOM   3025 H HD11 A ILE   A 1 137 ? 5.997  -9.186  -4.181  0.60 22.12 ?  137 ILE   A HD11 1 
ATOM   3026 H HD11 B ILE   A 1 137 ? 6.206  -9.569  -5.445  0.40 21.80 ?  137 ILE   A HD11 1 
ATOM   3027 H HD12 A ILE   A 1 137 ? 6.800  -9.325  -5.546  0.60 22.12 ?  137 ILE   A HD12 1 
ATOM   3028 H HD12 B ILE   A 1 137 ? 7.208  -10.198 -6.503  0.40 21.80 ?  137 ILE   A HD12 1 
ATOM   3029 H HD13 A ILE   A 1 137 ? 6.428  -10.616 -4.694  0.60 22.12 ?  137 ILE   A HD13 1 
ATOM   3030 H HD13 B ILE   A 1 137 ? 6.473  -11.133 -5.451  0.40 21.80 ?  137 ILE   A HD13 1 
ATOM   3031 N N    A HIS   A 1 138 ? 12.203 -10.660 -5.249  0.60 15.24 ?  138 HIS   A N    1 
ATOM   3032 N N    B HIS   A 1 138 ? 12.349 -10.942 -5.547  0.40 15.65 ?  138 HIS   A N    1 
ATOM   3033 C CA   A HIS   A 1 138 ? 13.316 -11.477 -5.716  0.60 15.30 ?  138 HIS   A CA   1 
ATOM   3034 C CA   B HIS   A 1 138 ? 13.594 -11.594 -5.923  0.40 15.36 ?  138 HIS   A CA   1 
ATOM   3035 C C    A HIS   A 1 138 ? 14.497 -11.387 -4.762  0.60 14.73 ?  138 HIS   A C    1 
ATOM   3036 C C    B HIS   A 1 138 ? 14.674 -11.394 -4.863  0.40 14.70 ?  138 HIS   A C    1 
ATOM   3037 O O    A HIS   A 1 138 ? 15.114 -12.402 -4.418  0.60 14.90 ?  138 HIS   A O    1 
ATOM   3038 O O    B HIS   A 1 138 ? 15.390 -12.343 -4.521  0.40 14.64 ?  138 HIS   A O    1 
ATOM   3039 C CB   A HIS   A 1 138 ? 13.725 -11.026 -7.116  0.60 15.79 ?  138 HIS   A CB   1 
ATOM   3040 C CB   B HIS   A 1 138 ? 14.063 -11.099 -7.289  0.40 16.15 ?  138 HIS   A CB   1 
ATOM   3041 C CG   A HIS   A 1 138 ? 15.006 -11.635 -7.586  0.60 16.81 ?  138 HIS   A CG   1 
ATOM   3042 C CG   B HIS   A 1 138 ? 15.308 -11.775 -7.768  0.40 17.12 ?  138 HIS   A CG   1 
ATOM   3043 N ND1  A HIS   A 1 138 ? 15.148 -12.987 -7.803  0.60 17.94 ?  138 HIS   A ND1  1 
ATOM   3044 N ND1  B HIS   A 1 138 ? 15.341 -13.104 -8.135  0.40 18.04 ?  138 HIS   A ND1  1 
ATOM   3045 C CD2  A HIS   A 1 138 ? 16.210 -11.079 -7.862  0.60 16.66 ?  138 HIS   A CD2  1 
ATOM   3046 C CD2  B HIS   A 1 138 ? 16.570 -11.312 -7.920  0.40 17.27 ?  138 HIS   A CD2  1 
ATOM   3047 C CE1  A HIS   A 1 138 ? 16.381 -13.239 -8.203  0.60 17.86 ?  138 HIS   A CE1  1 
ATOM   3048 C CE1  B HIS   A 1 138 ? 16.568 -13.427 -8.501  0.40 18.14 ?  138 HIS   A CE1  1 
ATOM   3049 N NE2  A HIS   A 1 138 ? 17.047 -12.099 -8.248  0.60 17.21 ?  138 HIS   A NE2  1 
ATOM   3050 N NE2  B HIS   A 1 138 ? 17.334 -12.358 -8.379  0.40 17.56 ?  138 HIS   A NE2  1 
ATOM   3051 H H    A HIS   A 1 138 ? 12.003 -9.991  -5.761  0.60 18.26 ?  138 HIS   A H    1 
ATOM   3052 H H    B HIS   A 1 138 ? 12.091 -10.318 -6.083  0.40 18.76 ?  138 HIS   A H    1 
ATOM   3053 H HA   A HIS   A 1 138 ? 13.029 -12.397 -5.760  0.60 18.34 ?  138 HIS   A HA   1 
ATOM   3054 H HA   B HIS   A 1 138 ? 13.433 -12.545 -6.001  0.40 18.41 ?  138 HIS   A HA   1 
ATOM   3055 H HB2  A HIS   A 1 138 ? 13.024 -11.280 -7.741  0.60 18.93 ?  138 HIS   A HB2  1 
ATOM   3056 H HB2  B HIS   A 1 138 ? 13.363 -11.265 -7.943  0.40 19.36 ?  138 HIS   A HB2  1 
ATOM   3057 H HB3  A HIS   A 1 138 ? 13.828 -10.061 -7.119  0.60 18.93 ?  138 HIS   A HB3  1 
ATOM   3058 H HB3  B HIS   A 1 138 ? 14.243 -10.147 -7.237  0.40 19.36 ?  138 HIS   A HB3  1 
ATOM   3059 H HD1  A HIS   A 1 138 ? 14.527 -13.573 -7.698  0.60 21.51 ?  138 HIS   A HD1  1 
ATOM   3060 H HD2  A HIS   A 1 138 ? 16.420 -10.173 -7.805  0.60 19.97 ?  138 HIS   A HD2  1 
ATOM   3061 H HD2  B HIS   A 1 138 ? 16.865 -10.447 -7.748  0.40 20.70 ?  138 HIS   A HD2  1 
ATOM   3062 H HE1  A HIS   A 1 138 ? 16.723 -14.074 -8.416  0.60 21.40 ?  138 HIS   A HE1  1 
ATOM   3063 H HE1  B HIS   A 1 138 ? 16.842 -14.264 -8.794  0.40 21.74 ?  138 HIS   A HE1  1 
ATOM   3064 H HE2  B HIS   A 1 138 ? 18.172 -12.322 -8.558  0.40 21.04 ?  138 HIS   A HE2  1 
ATOM   3065 N N    . SER   A 1 139 ? 14.816 -10.176 -4.321  1.00 14.70 ?  139 SER   A N    1 
ATOM   3066 C CA   . SER   A 1 139 ? 15.886 -9.975  -3.353  1.00 14.29 ?  139 SER   A CA   1 
ATOM   3067 C C    . SER   A 1 139 ? 15.679 -10.824 -2.105  1.00 13.62 ?  139 SER   A C    1 
ATOM   3068 O O    . SER   A 1 139 ? 16.633 -11.413 -1.582  1.00 13.53 ?  139 SER   A O    1 
ATOM   3069 C CB   . SER   A 1 139 ? 16.004 -8.496  -2.995  1.00 14.41 ?  139 SER   A CB   1 
ATOM   3070 O OG   . SER   A 1 139 ? 17.079 -8.322  -2.096  1.00 14.00 ?  139 SER   A OG   1 
ATOM   3071 H H    A SER   A 1 139 ? 14.418 -9.449  -4.562  0.60 17.61 ?  139 SER   A H    1 
ATOM   3072 H H    B SER   A 1 139 ? 14.332 -9.482  -4.494  0.40 17.61 ?  139 SER   A H    1 
ATOM   3073 H HA   . SER   A 1 139 ? 16.727 -10.242 -3.756  1.00 17.13 ?  139 SER   A HA   1 
ATOM   3074 H HB2  . SER   A 1 139 ? 16.165 -7.975  -3.799  1.00 17.27 ?  139 SER   A HB2  1 
ATOM   3075 H HB3  . SER   A 1 139 ? 15.183 -8.200  -2.565  1.00 17.27 ?  139 SER   A HB3  1 
ATOM   3076 H HG   . SER   A 1 139 ? 17.165 -7.511  -1.892  1.00 16.78 ?  139 SER   A HG   1 
ATOM   3077 N N    . LEU   A 1 140 ? 14.446 -10.881 -1.599  1.00 13.55 ?  140 LEU   A N    1 
ATOM   3078 C CA   . LEU   A 1 140 ? 14.179 -11.701 -0.421  1.00 13.46 ?  140 LEU   A CA   1 
ATOM   3079 C C    . LEU   A 1 140 ? 14.448 -13.174 -0.705  1.00 13.07 ?  140 LEU   A C    1 
ATOM   3080 O O    . LEU   A 1 140 ? 15.000 -13.892 0.140   1.00 13.73 ?  140 LEU   A O    1 
ATOM   3081 C CB   . LEU   A 1 140 ? 12.737 -11.491 0.036   1.00 14.30 ?  140 LEU   A CB   1 
ATOM   3082 C CG   . LEU   A 1 140 ? 12.293 -12.331 1.231   1.00 14.49 ?  140 LEU   A CG   1 
ATOM   3083 C CD1  . LEU   A 1 140 ? 13.208 -12.145 2.431   1.00 14.91 ?  140 LEU   A CD1  1 
ATOM   3084 C CD2  . LEU   A 1 140 ? 10.841 -12.009 1.600   1.00 15.62 ?  140 LEU   A CD2  1 
ATOM   3085 H H    . LEU   A 1 140 ? 13.764 -10.457 -1.907  1.00 16.24 ?  140 LEU   A H    1 
ATOM   3086 H HA   . LEU   A 1 140 ? 14.764 -11.421 0.301   1.00 16.13 ?  140 LEU   A HA   1 
ATOM   3087 H HB2  . LEU   A 1 140 ? 12.621 -10.563 0.278   1.00 17.14 ?  140 LEU   A HB2  1 
ATOM   3088 H HB3  . LEU   A 1 140 ? 12.149 -11.710 -0.705  1.00 17.14 ?  140 LEU   A HB3  1 
ATOM   3089 H HG   . LEU   A 1 140 ? 12.317 -13.271 0.981   1.00 17.36 ?  140 LEU   A HG   1 
ATOM   3090 H HD11 . LEU   A 1 140 ? 12.827 -12.613 3.193   1.00 17.87 ?  140 LEU   A HD11 1 
ATOM   3091 H HD12 . LEU   A 1 140 ? 14.079 -12.520 2.220   1.00 17.87 ?  140 LEU   A HD12 1 
ATOM   3092 H HD13 . LEU   A 1 140 ? 13.286 -11.203 2.624   1.00 17.87 ?  140 LEU   A HD13 1 
ATOM   3093 H HD21 . LEU   A 1 140 ? 10.576 -12.555 2.361   1.00 18.73 ?  140 LEU   A HD21 1 
ATOM   3094 H HD22 . LEU   A 1 140 ? 10.773 -11.070 1.832   1.00 18.73 ?  140 LEU   A HD22 1 
ATOM   3095 H HD23 . LEU   A 1 140 ? 10.266 -12.205 0.842   1.00 18.73 ?  140 LEU   A HD23 1 
ATOM   3096 N N    . ARG   A 1 141 ? 14.050 -13.644 -1.888  1.00 13.72 ?  141 ARG   A N    1 
ATOM   3097 C CA   . ARG   A 1 141 ? 14.287 -15.031 -2.267  1.00 15.06 ?  141 ARG   A CA   1 
ATOM   3098 C C    . ARG   A 1 141 ? 15.781 -15.341 -2.283  1.00 14.06 ?  141 ARG   A C    1 
ATOM   3099 O O    . ARG   A 1 141 ? 16.228 -16.349 -1.722  1.00 13.82 ?  141 ARG   A O    1 
ATOM   3100 C CB   . ARG   A 1 141 ? 13.662 -15.263 -3.643  1.00 17.03 ?  141 ARG   A CB   1 
ATOM   3101 C CG   . ARG   A 1 141 ? 13.694 -16.683 -4.140  1.00 20.22 ?  141 ARG   A CG   1 
ATOM   3102 C CD   . ARG   A 1 141 ? 12.675 -17.505 -3.420  1.00 22.18 ?  141 ARG   A CD   1 
ATOM   3103 N NE   . ARG   A 1 141 ? 13.276 -18.267 -2.338  1.00 22.30 ?  141 ARG   A NE   1 
ATOM   3104 C CZ   . ARG   A 1 141 ? 12.576 -18.856 -1.379  1.00 22.83 ?  141 ARG   A CZ   1 
ATOM   3105 N NH1  . ARG   A 1 141 ? 11.274 -18.663 -1.258  1.00 22.65 ?  141 ARG   A NH1  1 
ATOM   3106 N NH2  . ARG   A 1 141 ? 13.199 -19.649 -0.513  1.00 23.29 ?  141 ARG   A NH2  1 
ATOM   3107 H H    . ARG   A 1 141 ? 13.647 -13.178 -2.487  1.00 16.44 ?  141 ARG   A H    1 
ATOM   3108 H HA   . ARG   A 1 141 ? 13.859 -15.620 -1.628  1.00 18.05 ?  141 ARG   A HA   1 
ATOM   3109 H HB2  . ARG   A 1 141 ? 12.735 -14.978 -3.612  1.00 20.41 ?  141 ARG   A HB2  1 
ATOM   3110 H HB3  . ARG   A 1 141 ? 14.142 -14.720 -4.288  1.00 20.41 ?  141 ARG   A HB3  1 
ATOM   3111 H HG2  . ARG   A 1 141 ? 13.490 -16.699 -5.090  1.00 24.23 ?  141 ARG   A HG2  1 
ATOM   3112 H HG3  . ARG   A 1 141 ? 14.572 -17.068 -3.980  1.00 24.23 ?  141 ARG   A HG3  1 
ATOM   3113 H HD2  . ARG   A 1 141 ? 12.001 -16.921 -3.035  1.00 26.59 ?  141 ARG   A HD2  1 
ATOM   3114 H HD3  . ARG   A 1 141 ? 12.261 -18.123 -4.044  1.00 26.59 ?  141 ARG   A HD3  1 
ATOM   3115 H HE   . ARG   A 1 141 ? 14.110 -18.464 -2.401  1.00 26.74 ?  141 ARG   A HE   1 
ATOM   3116 H HH11 . ARG   A 1 141 ? 10.853 -18.166 -1.820  1.00 27.15 ?  141 ARG   A HH11 1 
ATOM   3117 H HH12 . ARG   A 1 141 ? 10.837 -19.055 -0.628  1.00 27.15 ?  141 ARG   A HH12 1 
ATOM   3118 H HH21 . ARG   A 1 141 ? 14.048 -19.775 -0.580  1.00 27.93 ?  141 ARG   A HH21 1 
ATOM   3119 H HH22 . ARG   A 1 141 ? 12.759 -20.026 0.122   1.00 27.93 ?  141 ARG   A HH22 1 
ATOM   3120 N N    . VAL   A 1 142 ? 16.573 -14.477 -2.924  1.00 13.34 ?  142 VAL   A N    1 
ATOM   3121 C CA   . VAL   A 1 142 ? 18.016 -14.692 -2.960  1.00 13.31 ?  142 VAL   A CA   1 
ATOM   3122 C C    . VAL   A 1 142 ? 18.591 -14.663 -1.554  1.00 12.81 ?  142 VAL   A C    1 
ATOM   3123 O O    . VAL   A 1 142 ? 19.458 -15.473 -1.210  1.00 12.89 ?  142 VAL   A O    1 
ATOM   3124 C CB   . VAL   A 1 142 ? 18.709 -13.676 -3.885  1.00 13.89 ?  142 VAL   A CB   1 
ATOM   3125 C CG1  . VAL   A 1 142 ? 20.220 -13.878 -3.845  1.00 13.84 ?  142 VAL   A CG1  1 
ATOM   3126 C CG2  . VAL   A 1 142 ? 18.197 -13.821 -5.305  1.00 15.27 ?  142 VAL   A CG2  1 
ATOM   3127 H H    . VAL   A 1 142 ? 16.307 -13.764 -3.335  1.00 15.99 ?  142 VAL   A H    1 
ATOM   3128 H HA   . VAL   A 1 142 ? 18.186 -15.568 -3.325  1.00 15.95 ?  142 VAL   A HA   1 
ATOM   3129 H HB   . VAL   A 1 142 ? 18.520 -12.770 -3.581  1.00 16.64 ?  142 VAL   A HB   1 
ATOM   3130 H HG11 . VAL   A 1 142 ? 20.626 -13.392 -4.582  1.00 16.58 ?  142 VAL   A HG11 1 
ATOM   3131 H HG12 . VAL   A 1 142 ? 20.569 -13.537 -3.002  1.00 16.58 ?  142 VAL   A HG12 1 
ATOM   3132 H HG13 . VAL   A 1 142 ? 20.416 -14.822 -3.925  1.00 16.58 ?  142 VAL   A HG13 1 
ATOM   3133 H HG21 . VAL   A 1 142 ? 18.654 -13.178 -5.871  1.00 18.30 ?  142 VAL   A HG21 1 
ATOM   3134 H HG22 . VAL   A 1 142 ? 18.390 -14.723 -5.610  1.00 18.30 ?  142 VAL   A HG22 1 
ATOM   3135 H HG23 . VAL   A 1 142 ? 17.247 -13.661 -5.313  1.00 18.30 ?  142 VAL   A HG23 1 
ATOM   3136 N N    . CYS   A 1 143 ? 18.131 -13.729 -0.721  1.00 12.50 ?  143 CYS   A N    1 
ATOM   3137 C CA   . CYS   A 1 143 ? 18.600 -13.673 0.658   1.00 12.67 ?  143 CYS   A CA   1 
ATOM   3138 C C    . CYS   A 1 143 ? 18.376 -15.008 1.361   1.00 12.55 ?  143 CYS   A C    1 
ATOM   3139 O O    . CYS   A 1 143 ? 19.301 -15.593 1.933   1.00 12.55 ?  143 CYS   A O    1 
ATOM   3140 C CB   . CYS   A 1 143 ? 17.870 -12.558 1.399   1.00 13.21 ?  143 CYS   A CB   1 
ATOM   3141 S SG   . CYS   A 1 143 ? 18.358 -12.377 3.118   1.00 13.27 ?  143 CYS   A SG   1 
ATOM   3142 H H    . CYS   A 1 143 ? 17.553 -13.130 -0.925  1.00 14.98 ?  143 CYS   A H    1 
ATOM   3143 H HA   . CYS   A 1 143 ? 19.548 -13.487 0.671   1.00 15.18 ?  143 CYS   A HA   1 
ATOM   3144 H HB2  . CYS   A 1 143 ? 18.046 -11.718 0.950   1.00 15.83 ?  143 CYS   A HB2  1 
ATOM   3145 H HB3  . CYS   A 1 143 ? 16.920 -12.741 1.384   1.00 15.83 ?  143 CYS   A HB3  1 
ATOM   3146 H HG   . CYS   A 1 143 ? 17.767 -11.448 3.595   1.00 15.90 ?  143 CYS   A HG   1 
ATOM   3147 N N    . VAL   A 1 144 ? 17.145 -15.509 1.324   1.00 12.95 ?  144 VAL   A N    1 
ATOM   3148 C CA   . VAL   A 1 144 ? 16.815 -16.741 2.033   1.00 14.07 ?  144 VAL   A CA   1 
ATOM   3149 C C    . VAL   A 1 144 ? 17.625 -17.910 1.498   1.00 13.95 ?  144 VAL   A C    1 
ATOM   3150 O O    . VAL   A 1 144 ? 18.009 -18.809 2.253   1.00 14.52 ?  144 VAL   A O    1 
ATOM   3151 C CB   . VAL   A 1 144 ? 15.298 -16.991 1.927   1.00 16.82 ?  144 VAL   A CB   1 
ATOM   3152 C CG1  . VAL   A 1 144 ? 14.944 -18.424 2.265   1.00 18.55 ?  144 VAL   A CG1  1 
ATOM   3153 C CG2  . VAL   A 1 144 ? 14.545 -15.990 2.813   1.00 17.14 ?  144 VAL   A CG2  1 
ATOM   3154 H H    . VAL   A 1 144 ? 16.484 -15.155 0.897   1.00 15.52 ?  144 VAL   A H    1 
ATOM   3155 H HA   . VAL   A 1 144 ? 17.026 -16.631 2.969   1.00 16.87 ?  144 VAL   A HA   1 
ATOM   3156 H HB   . VAL   A 1 144 ? 15.017 -16.828 1.010   1.00 20.17 ?  144 VAL   A HB   1 
ATOM   3157 H HG11 . VAL   A 1 144 ? 13.993 -18.475 2.460   1.00 22.24 ?  144 VAL   A HG11 1 
ATOM   3158 H HG12 . VAL   A 1 144 ? 15.152 -18.989 1.506   1.00 22.24 ?  144 VAL   A HG12 1 
ATOM   3159 H HG13 . VAL   A 1 144 ? 15.453 -18.698 3.040   1.00 22.24 ?  144 VAL   A HG13 1 
ATOM   3160 H HG21 . VAL   A 1 144 ? 13.590 -16.161 2.755   1.00 20.54 ?  144 VAL   A HG21 1 
ATOM   3161 H HG22 . VAL   A 1 144 ? 14.842 -16.090 3.731   1.00 20.54 ?  144 VAL   A HG22 1 
ATOM   3162 H HG23 . VAL   A 1 144 ? 14.732 -15.086 2.505   1.00 20.54 ?  144 VAL   A HG23 1 
ATOM   3163 N N    . ASP   A 1 145 ? 17.872 -17.937 0.193   1.00 14.20 ?  145 ASP   A N    1 
ATOM   3164 C CA   . ASP   A 1 145 ? 18.576 -19.042 -0.448  1.00 15.10 ?  145 ASP   A CA   1 
ATOM   3165 C C    . ASP   A 1 145 ? 20.096 -18.894 -0.417  1.00 14.34 ?  145 ASP   A C    1 
ATOM   3166 O O    . ASP   A 1 145 ? 20.799 -19.780 -0.912  1.00 15.95 ?  145 ASP   A O    1 
ATOM   3167 C CB   . ASP   A 1 145 ? 18.126 -19.171 -1.902  1.00 16.67 ?  145 ASP   A CB   1 
ATOM   3168 C CG   . ASP   A 1 145 ? 16.679 -19.613 -2.028  1.00 19.11 ?  145 ASP   A CG   1 
ATOM   3169 O OD1  . ASP   A 1 145 ? 16.122 -20.150 -1.046  1.00 19.75 ?  145 ASP   A OD1  1 
ATOM   3170 O OD2  . ASP   A 1 145 ? 16.102 -19.417 -3.113  1.00 20.57 -1 145 ASP   A OD2  1 
ATOM   3171 H H    . ASP   A 1 145 ? 17.626 -17.318 -0.351  1.00 17.01 ?  145 ASP   A H    1 
ATOM   3172 H HA   . ASP   A 1 145 ? 18.344 -19.864 0.010   1.00 18.09 ?  145 ASP   A HA   1 
ATOM   3173 H HB2  . ASP   A 1 145 ? 18.220 -18.308 -2.339  1.00 19.98 ?  145 ASP   A HB2  1 
ATOM   3174 H HB3  . ASP   A 1 145 ? 18.675 -19.831 -2.344  1.00 19.98 ?  145 ASP   A HB3  1 
ATOM   3175 N N    . THR   A 1 146 ? 20.624 -17.809 0.141   1.00 12.69 ?  146 THR   A N    1 
ATOM   3176 C CA   . THR   A 1 146 ? 22.063 -17.556 0.155   1.00 12.13 ?  146 THR   A CA   1 
ATOM   3177 C C    . THR   A 1 146 ? 22.622 -17.376 1.552   1.00 11.81 ?  146 THR   A C    1 
ATOM   3178 O O    . THR   A 1 146 ? 23.698 -17.907 1.857   1.00 12.80 ?  146 THR   A O    1 
ATOM   3179 C CB   . THR   A 1 146 ? 22.389 -16.304 -0.683  1.00 11.95 ?  146 THR   A CB   1 
ATOM   3180 O OG1  . THR   A 1 146 ? 21.871 -16.466 -2.005  1.00 12.75 ?  146 THR   A OG1  1 
ATOM   3181 C CG2  . THR   A 1 146 ? 23.897 -16.065 -0.752  1.00 12.37 ?  146 THR   A CG2  1 
ATOM   3182 H H    . THR   A 1 146 ? 20.161 -17.188 0.529   1.00 15.20 ?  146 THR   A H    1 
ATOM   3183 H HA   . THR   A 1 146 ? 22.518 -18.301 -0.251  1.00 14.53 ?  146 THR   A HA   1 
ATOM   3184 H HB   . THR   A 1 146 ? 21.984 -15.521 -0.268  1.00 14.31 ?  146 THR   A HB   1 
ATOM   3185 H HG1  . THR   A 1 146 ? 21.035 -16.542 -1.972  1.00 15.27 ?  146 THR   A HG1  1 
ATOM   3186 H HG21 . THR   A 1 146 ? 24.097 -15.400 -1.429  1.00 14.83 ?  146 THR   A HG21 1 
ATOM   3187 H HG22 . THR   A 1 146 ? 24.226 -15.747 0.106   1.00 14.83 ?  146 THR   A HG22 1 
ATOM   3188 H HG23 . THR   A 1 146 ? 24.351 -16.891 -0.977  1.00 14.83 ?  146 THR   A HG23 1 
ATOM   3189 N N    . VAL   A 1 147 ? 21.945 -16.604 2.392   1.00 11.86 ?  147 VAL   A N    1 
ATOM   3190 C CA   . VAL   A 1 147 ? 22.435 -16.312 3.728   1.00 12.18 ?  147 VAL   A CA   1 
ATOM   3191 C C    . VAL   A 1 147 ? 22.115 -17.483 4.640   1.00 12.31 ?  147 VAL   A C    1 
ATOM   3192 O O    . VAL   A 1 147 ? 20.974 -17.954 4.687   1.00 13.22 ?  147 VAL   A O    1 
ATOM   3193 C CB   . VAL   A 1 147 ? 21.817 -15.011 4.256   1.00 12.18 ?  147 VAL   A CB   1 
ATOM   3194 C CG1  . VAL   A 1 147 ? 22.384 -14.703 5.622   1.00 13.14 ?  147 VAL   A CG1  1 
ATOM   3195 C CG2  . VAL   A 1 147 ? 22.068 -13.870 3.287   1.00 12.50 ?  147 VAL   A CG2  1 
ATOM   3196 H H    . VAL   A 1 147 ? 21.182 -16.239 2.215   1.00 14.21 ?  147 VAL   A H    1 
ATOM   3197 H HA   . VAL   A 1 147 ? 23.397 -16.198 3.698   1.00 14.59 ?  147 VAL   A HA   1 
ATOM   3198 H HB   . VAL   A 1 147 ? 20.860 -15.122 4.349   1.00 14.59 ?  147 VAL   A HB   1 
ATOM   3199 H HG11 . VAL   A 1 147 ? 22.155 -13.796 5.864   1.00 15.74 ?  147 VAL   A HG11 1 
ATOM   3200 H HG12 . VAL   A 1 147 ? 22.009 -15.324 6.267   1.00 15.74 ?  147 VAL   A HG12 1 
ATOM   3201 H HG13 . VAL   A 1 147 ? 23.350 -14.805 5.591   1.00 15.74 ?  147 VAL   A HG13 1 
ATOM   3202 H HG21 . VAL   A 1 147 ? 21.755 -13.040 3.686   1.00 14.98 ?  147 VAL   A HG21 1 
ATOM   3203 H HG22 . VAL   A 1 147 ? 23.017 -13.810 3.105   1.00 14.98 ?  147 VAL   A HG22 1 
ATOM   3204 H HG23 . VAL   A 1 147 ? 21.581 -14.042 2.465   1.00 14.98 ?  147 VAL   A HG23 1 
ATOM   3205 N N    . ARG   A 1 148 ? 23.135 -17.963 5.348   1.00 12.46 ?  148 ARG   A N    1 
ATOM   3206 C CA   . ARG   A 1 148 ? 23.003 -19.048 6.303   1.00 12.69 ?  148 ARG   A CA   1 
ATOM   3207 C C    . ARG   A 1 148 ? 23.137 -18.586 7.742   1.00 13.16 ?  148 ARG   A C    1 
ATOM   3208 O O    . ARG   A 1 148 ? 22.734 -19.317 8.654   1.00 14.95 ?  148 ARG   A O    1 
ATOM   3209 C CB   . ARG   A 1 148 ? 24.033 -20.152 6.011   1.00 13.44 ?  148 ARG   A CB   1 
ATOM   3210 C CG   . ARG   A 1 148 ? 23.850 -20.778 4.641   1.00 14.61 ?  148 ARG   A CG   1 
ATOM   3211 C CD   . ARG   A 1 148 ? 24.920 -21.823 4.330   1.00 15.29 ?  148 ARG   A CD   1 
ATOM   3212 N NE   . ARG   A 1 148 ? 26.261 -21.251 4.345   1.00 15.22 ?  148 ARG   A NE   1 
ATOM   3213 C CZ   . ARG   A 1 148 ? 26.766 -20.509 3.369   1.00 14.25 ?  148 ARG   A CZ   1 
ATOM   3214 N NH1  . ARG   A 1 148 ? 26.080 -20.257 2.265   1.00 14.84 ?  148 ARG   A NH1  1 
ATOM   3215 N NH2  . ARG   A 1 148 ? 27.991 -19.999 3.506   1.00 15.09 ?  148 ARG   A NH2  1 
ATOM   3216 H H    . ARG   A 1 148 ? 23.943 -17.659 5.280   1.00 14.93 ?  148 ARG   A H    1 
ATOM   3217 H HA   . ARG   A 1 148 ? 22.124 -19.436 6.203   1.00 15.20 ?  148 ARG   A HA   1 
ATOM   3218 H HB2  . ARG   A 1 148 ? 24.924 -19.780 6.052   1.00 16.10 ?  148 ARG   A HB2  1 
ATOM   3219 H HB3  . ARG   A 1 148 ? 23.934 -20.857 6.673   1.00 16.10 ?  148 ARG   A HB3  1 
ATOM   3220 H HG2  . ARG   A 1 148 ? 22.984 -21.213 4.604   1.00 17.51 ?  148 ARG   A HG2  1 
ATOM   3221 H HG3  . ARG   A 1 148 ? 23.904 -20.084 3.967   1.00 17.51 ?  148 ARG   A HG3  1 
ATOM   3222 H HD2  . ARG   A 1 148 ? 24.887 -22.528 5.000   1.00 18.32 ?  148 ARG   A HD2  1 
ATOM   3223 H HD3  . ARG   A 1 148 ? 24.757 -22.201 3.449   1.00 18.32 ?  148 ARG   A HD3  1 
ATOM   3224 H HE   . ARG   A 1 148 ? 26.762 -21.411 5.022   1.00 18.25 ?  148 ARG   A HE   1 
ATOM   3225 H HH11 . ARG   A 1 148 ? 25.290 -20.572 2.163   1.00 17.78 ?  148 ARG   A HH11 1 
ATOM   3226 H HH12 . ARG   A 1 148 ? 26.427 -19.762 1.647   1.00 17.78 ?  148 ARG   A HH12 1 
ATOM   3227 H HH21 . ARG   A 1 148 ? 28.440 -20.149 4.218   1.00 18.09 ?  148 ARG   A HH21 1 
ATOM   3228 H HH22 . ARG   A 1 148 ? 28.324 -19.505 2.880   1.00 18.09 ?  148 ARG   A HH22 1 
ATOM   3229 N N    . THR   A 1 149 ? 23.705 -17.405 7.961   1.00 13.29 ?  149 THR   A N    1 
ATOM   3230 C CA   . THR   A 1 149 ? 23.788 -16.814 9.281   1.00 13.29 ?  149 THR   A CA   1 
ATOM   3231 C C    . THR   A 1 149 ? 22.466 -16.116 9.598   1.00 12.69 ?  149 THR   A C    1 
ATOM   3232 O O    . THR   A 1 149 ? 21.526 -16.103 8.794   1.00 13.72 ?  149 THR   A O    1 
ATOM   3233 C CB   . THR   A 1 149 ? 24.986 -15.876 9.339   1.00 13.69 ?  149 THR   A CB   1 
ATOM   3234 O OG1  . THR   A 1 149 ? 24.849 -14.930 8.276   1.00 13.90 ?  149 THR   A OG1  1 
ATOM   3235 C CG2  . THR   A 1 149 ? 26.300 -16.666 9.199   1.00 14.63 ?  149 THR   A CG2  1 
ATOM   3236 H H    . THR   A 1 149 ? 24.060 -16.918 7.344   1.00 15.93 ?  149 THR   A H    1 
ATOM   3237 H HA   . THR   A 1 149 ? 23.919 -17.518 9.933   1.00 15.93 ?  149 THR   A HA   1 
ATOM   3238 H HB   . THR   A 1 149 ? 24.988 -15.415 10.191  1.00 16.40 ?  149 THR   A HB   1 
ATOM   3239 H HG1  . THR   A 1 149 ? 25.499 -14.396 8.282   1.00 16.65 ?  149 THR   A HG1  1 
ATOM   3240 H HG21 . THR   A 1 149 ? 27.058 -16.065 9.255   1.00 17.53 ?  149 THR   A HG21 1 
ATOM   3241 H HG22 . THR   A 1 149 ? 26.371 -17.329 9.905   1.00 17.53 ?  149 THR   A HG22 1 
ATOM   3242 H HG23 . THR   A 1 149 ? 26.326 -17.124 8.340   1.00 17.53 ?  149 THR   A HG23 1 
ATOM   3243 N N    . ASN   A 1 150 ? 22.353 -15.585 10.808  1.00 13.11 ?  150 ASN   A N    1 
ATOM   3244 C CA   . ASN   A 1 150 ? 21.075 -15.080 11.310  1.00 13.85 ?  150 ASN   A CA   1 
ATOM   3245 C C    . ASN   A 1 150 ? 20.894 -13.639 10.860  1.00 13.40 ?  150 ASN   A C    1 
ATOM   3246 O O    . ASN   A 1 150 ? 21.634 -12.748 11.293  1.00 14.95 ?  150 ASN   A O    1 
ATOM   3247 C CB   . ASN   A 1 150 ? 21.034 -15.202 12.827  1.00 16.73 ?  150 ASN   A CB   1 
ATOM   3248 C CG   . ASN   A 1 150 ? 20.908 -16.631 13.277  1.00 20.98 ?  150 ASN   A CG   1 
ATOM   3249 O OD1  . ASN   A 1 150 ? 20.298 -17.447 12.590  1.00 22.58 ?  150 ASN   A OD1  1 
ATOM   3250 N ND2  . ASN   A 1 150 ? 21.503 -16.954 14.421  1.00 23.37 ?  150 ASN   A ND2  1 
ATOM   3251 H H    . ASN   A 1 150 ? 23.006 -15.498 11.360  1.00 15.71 ?  150 ASN   A H    1 
ATOM   3252 H HA   . ASN   A 1 150 ? 20.352 -15.615 10.943  1.00 16.60 ?  150 ASN   A HA   1 
ATOM   3253 H HB2  . ASN   A 1 150 ? 21.853 -14.840 13.201  1.00 20.06 ?  150 ASN   A HB2  1 
ATOM   3254 H HB3  . ASN   A 1 150 ? 20.268 -14.715 13.168  1.00 20.06 ?  150 ASN   A HB3  1 
ATOM   3255 H HD21 . ASN   A 1 150 ? 21.461 -17.764 14.721  1.00 28.02 ?  150 ASN   A HD21 1 
ATOM   3256 H HD22 . ASN   A 1 150 ? 21.924 -16.356 14.876  1.00 28.02 ?  150 ASN   A HD22 1 
ATOM   3257 N N    . VAL   A 1 151 ? 19.914 -13.407 9.995   1.00 12.95 ?  151 VAL   A N    1 
ATOM   3258 C CA   . VAL   A 1 151 ? 19.701 -12.093 9.413   1.00 13.10 ?  151 VAL   A CA   1 
ATOM   3259 C C    . VAL   A 1 151 ? 18.315 -11.582 9.782   1.00 13.13 ?  151 VAL   A C    1 
ATOM   3260 O O    . VAL   A 1 151 ? 17.309 -12.297 9.642   1.00 14.21 ?  151 VAL   A O    1 
ATOM   3261 C CB   . VAL   A 1 151 ? 19.996 -12.071 7.899   1.00 14.04 ?  151 VAL   A CB   1 
ATOM   3262 C CG1  . VAL   A 1 151 ? 19.162 -13.077 7.132   1.00 15.32 ?  151 VAL   A CG1  1 
ATOM   3263 C CG2  . VAL   A 1 151 ? 19.834 -10.658 7.344   1.00 14.66 ?  151 VAL   A CG2  1 
ATOM   3264 H H    . VAL   A 1 151 ? 19.359 -14.006 9.723   1.00 15.52 ?  151 VAL   A H    1 
ATOM   3265 H HA   . VAL   A 1 151 ? 20.341 -11.485 9.818   1.00 15.70 ?  151 VAL   A HA   1 
ATOM   3266 H HB   . VAL   A 1 151 ? 20.930 -12.316 7.768   1.00 16.82 ?  151 VAL   A HB   1 
ATOM   3267 H HG11 . VAL   A 1 151 ? 19.376 -13.017 6.186   1.00 18.36 ?  151 VAL   A HG11 1 
ATOM   3268 H HG12 . VAL   A 1 151 ? 19.371 -13.972 7.455   1.00 18.36 ?  151 VAL   A HG12 1 
ATOM   3269 H HG13 . VAL   A 1 151 ? 18.224 -12.887 7.272   1.00 18.36 ?  151 VAL   A HG13 1 
ATOM   3270 H HG21 . VAL   A 1 151 ? 20.154 -10.642 6.425   1.00 17.57 ?  151 VAL   A HG21 1 
ATOM   3271 H HG22 . VAL   A 1 151 ? 18.899 -10.412 7.372   1.00 17.57 ?  151 VAL   A HG22 1 
ATOM   3272 H HG23 . VAL   A 1 151 ? 20.359 -10.044 7.883   1.00 17.57 ?  151 VAL   A HG23 1 
ATOM   3273 N N    . TYR   A 1 152 ? 18.299 -10.338 10.272  1.00 12.89 ?  152 TYR   A N    1 
ATOM   3274 C CA   . TYR   A 1 152 ? 17.107 -9.607  10.673  1.00 12.46 ?  152 TYR   A CA   1 
ATOM   3275 C C    . TYR   A 1 152 ? 16.902 -8.500  9.652   1.00 11.95 ?  152 TYR   A C    1 
ATOM   3276 O O    . TYR   A 1 152 ? 17.680 -7.539  9.602   1.00 12.55 ?  152 TYR   A O    1 
ATOM   3277 C CB   . TYR   A 1 152 ? 17.292 -9.072  12.092  1.00 13.06 ?  152 TYR   A CB   1 
ATOM   3278 C CG   . TYR   A 1 152 ? 17.253 -10.208 13.079  1.00 14.14 ?  152 TYR   A CG   1 
ATOM   3279 C CD1  . TYR   A 1 152 ? 18.379 -10.980 13.324  1.00 15.71 ?  152 TYR   A CD1  1 
ATOM   3280 C CD2  . TYR   A 1 152 ? 16.076 -10.547 13.728  1.00 14.09 ?  152 TYR   A CD2  1 
ATOM   3281 C CE1  . TYR   A 1 152 ? 18.341 -12.048 14.199  1.00 16.32 ?  152 TYR   A CE1  1 
ATOM   3282 C CE2  . TYR   A 1 152 ? 16.024 -11.618 14.607  1.00 15.35 ?  152 TYR   A CE2  1 
ATOM   3283 C CZ   . TYR   A 1 152 ? 17.162 -12.361 14.842  1.00 16.23 ?  152 TYR   A CZ   1 
ATOM   3284 O OH   . TYR   A 1 152 ? 17.109 -13.429 15.716  1.00 18.36 ?  152 TYR   A OH   1 
ATOM   3285 H H    . TYR   A 1 152 ? 19.019 -9.871  10.374  1.00 15.45 ?  152 TYR   A H    1 
ATOM   3286 H HA   . TYR   A 1 152 ? 16.341 -10.204 10.659  1.00 14.93 ?  152 TYR   A HA   1 
ATOM   3287 H HB2  . TYR   A 1 152 ? 18.151 -8.634  12.166  1.00 15.65 ?  152 TYR   A HB2  1 
ATOM   3288 H HB3  . TYR   A 1 152 ? 16.574 -8.457  12.303  1.00 15.65 ?  152 TYR   A HB3  1 
ATOM   3289 H HD1  . TYR   A 1 152 ? 19.172 -10.774 12.889  1.00 18.83 ?  152 TYR   A HD1  1 
ATOM   3290 H HD2  . TYR   A 1 152 ? 15.304 -10.047 13.571  1.00 16.89 ?  152 TYR   A HD2  1 
ATOM   3291 H HE1  . TYR   A 1 152 ? 19.105 -12.552 14.359  1.00 19.57 ?  152 TYR   A HE1  1 
ATOM   3292 H HE2  . TYR   A 1 152 ? 15.228 -11.824 15.044  1.00 18.39 ?  152 TYR   A HE2  1 
ATOM   3293 H HH   . TYR   A 1 152 ? 16.331 -13.496 16.037  1.00 22.01 ?  152 TYR   A HH   1 
ATOM   3294 N N    . LEU   A 1 153 ? 15.887 -8.663  8.811   1.00 12.26 ?  153 LEU   A N    1 
ATOM   3295 C CA   . LEU   A 1 153 ? 15.623 -7.742  7.717   1.00 12.78 ?  153 LEU   A CA   1 
ATOM   3296 C C    . LEU   A 1 153 ? 14.633 -6.672  8.150   1.00 13.35 ?  153 LEU   A C    1 
ATOM   3297 O O    . LEU   A 1 153 ? 13.538 -6.984  8.641   1.00 14.49 ?  153 LEU   A O    1 
ATOM   3298 C CB   . LEU   A 1 153 ? 15.047 -8.494  6.517   1.00 12.96 ?  153 LEU   A CB   1 
ATOM   3299 C CG   . LEU   A 1 153 ? 15.983 -9.502  5.848   1.00 12.90 ?  153 LEU   A CG   1 
ATOM   3300 C CD1  . LEU   A 1 153 ? 15.185 -10.377 4.898   1.00 13.43 ?  153 LEU   A CD1  1 
ATOM   3301 C CD2  . LEU   A 1 153 ? 17.108 -8.791  5.104   1.00 13.60 ?  153 LEU   A CD2  1 
ATOM   3302 H H    . LEU   A 1 153 ? 15.323 -9.322  8.859   1.00 14.69 ?  153 LEU   A H    1 
ATOM   3303 H HA   . LEU   A 1 153 ? 16.449 -7.322  7.460   1.00 15.31 ?  153 LEU   A HA   1 
ATOM   3304 H HB2  . LEU   A 1 153 ? 14.258 -8.972  6.807   1.00 15.53 ?  153 LEU   A HB2  1 
ATOM   3305 H HB3  . LEU   A 1 153 ? 14.799 -7.835  5.846   1.00 15.53 ?  153 LEU   A HB3  1 
ATOM   3306 H HG   . LEU   A 1 153 ? 16.383 -10.066 6.530   1.00 15.45 ?  153 LEU   A HG   1 
ATOM   3307 H HD11 . LEU   A 1 153 ? 15.768 -11.059 4.533   1.00 16.09 ?  153 LEU   A HD11 1 
ATOM   3308 H HD12 . LEU   A 1 153 ? 14.459 -10.790 5.389   1.00 16.09 ?  153 LEU   A HD12 1 
ATOM   3309 H HD13 . LEU   A 1 153 ? 14.831 -9.824  4.184   1.00 16.09 ?  153 LEU   A HD13 1 
ATOM   3310 H HD21 . LEU   A 1 153 ? 17.676 -9.459  4.691   1.00 16.29 ?  153 LEU   A HD21 1 
ATOM   3311 H HD22 . LEU   A 1 153 ? 16.718 -8.221  4.425   1.00 16.29 ?  153 LEU   A HD22 1 
ATOM   3312 H HD23 . LEU   A 1 153 ? 17.619 -8.263  5.733   1.00 16.29 ?  153 LEU   A HD23 1 
ATOM   3313 N N    A ALA   A 1 154 ? 14.995 -5.415  7.902   0.60 13.22 ?  154 ALA   A N    1 
ATOM   3314 N N    B ALA   A 1 154 ? 15.029 -5.412  8.013   0.40 13.29 ?  154 ALA   A N    1 
ATOM   3315 C CA   A ALA   A 1 154 ? 14.113 -4.272  8.105   0.60 13.74 ?  154 ALA   A CA   1 
ATOM   3316 C CA   B ALA   A 1 154 ? 14.182 -4.272  8.341   0.40 13.71 ?  154 ALA   A CA   1 
ATOM   3317 C C    A ALA   A 1 154 ? 13.618 -3.776  6.752   0.60 14.03 ?  154 ALA   A C    1 
ATOM   3318 C C    B ALA   A 1 154 ? 13.737 -3.634  7.032   0.40 13.49 ?  154 ALA   A C    1 
ATOM   3319 O O    A ALA   A 1 154 ? 14.421 -3.391  5.894   0.60 14.27 ?  154 ALA   A O    1 
ATOM   3320 O O    B ALA   A 1 154 ? 14.578 -3.215  6.229   0.40 13.46 ?  154 ALA   A O    1 
ATOM   3321 C CB   A ALA   A 1 154 ? 14.851 -3.146  8.824   0.60 14.03 ?  154 ALA   A CB   1 
ATOM   3322 C CB   B ALA   A 1 154 ? 14.948 -3.265  9.199   0.40 14.02 ?  154 ALA   A CB   1 
ATOM   3323 H H    A ALA   A 1 154 ? 15.776 -5.196  7.611   0.60 15.84 ?  154 ALA   A H    1 
ATOM   3324 H H    B ALA   A 1 154 ? 15.809 -5.186  7.727   0.40 15.92 ?  154 ALA   A H    1 
ATOM   3325 H HA   A ALA   A 1 154 ? 13.349 -4.535  8.638   0.60 16.47 ?  154 ALA   A HA   1 
ATOM   3326 H HA   B ALA   A 1 154 ? 13.401 -4.566  8.838   0.40 16.43 ?  154 ALA   A HA   1 
ATOM   3327 H HB1  A ALA   A 1 154 ? 14.247 -2.396  8.941   0.60 16.81 ?  154 ALA   A HB1  1 
ATOM   3328 H HB1  B ALA   A 1 154 ? 14.369 -2.515  9.407   0.40 16.79 ?  154 ALA   A HB1  1 
ATOM   3329 H HB2  A ALA   A 1 154 ? 15.156 -3.465  9.686   0.60 16.81 ?  154 ALA   A HB2  1 
ATOM   3330 H HB2  B ALA   A 1 154 ? 15.237 -3.695  10.022  0.40 16.79 ?  154 ALA   A HB2  1 
ATOM   3331 H HB3  A ALA   A 1 154 ? 15.613 -2.872  8.285   0.60 16.81 ?  154 ALA   A HB3  1 
ATOM   3332 H HB3  B ALA   A 1 154 ? 15.725 -2.952  8.705   0.40 16.79 ?  154 ALA   A HB3  1 
ATOM   3333 N N    A VAL   A 1 155 ? 12.302 -3.785  6.572   0.60 14.97 ?  155 VAL   A N    1 
ATOM   3334 N N    B VAL   A 1 155 ? 12.426 -3.573  6.813   0.40 13.79 ?  155 VAL   A N    1 
ATOM   3335 C CA   A VAL   A 1 155 ? 11.646 -3.298  5.364   0.60 15.94 ?  155 VAL   A CA   1 
ATOM   3336 C CA   B VAL   A 1 155 ? 11.852 -3.072  5.566   0.40 14.67 ?  155 VAL   A CA   1 
ATOM   3337 C C    A VAL   A 1 155 ? 10.915 -2.016  5.732   0.60 17.33 ?  155 VAL   A C    1 
ATOM   3338 C C    B VAL   A 1 155 ? 10.961 -1.885  5.903   0.40 15.97 ?  155 VAL   A C    1 
ATOM   3339 O O    A VAL   A 1 155 ? 10.031 -2.025  6.598   0.60 17.77 ?  155 VAL   A O    1 
ATOM   3340 O O    B VAL   A 1 155 ? 9.857  -2.059  6.435   0.40 16.69 ?  155 VAL   A O    1 
ATOM   3341 C CB   A VAL   A 1 155 ? 10.678 -4.348  4.796   0.60 15.95 ?  155 VAL   A CB   1 
ATOM   3342 C CB   B VAL   A 1 155 ? 11.068 -4.156  4.813   0.40 14.69 ?  155 VAL   A CB   1 
ATOM   3343 C CG1  A VAL   A 1 155 ? 9.939  -3.793  3.589   0.60 16.68 ?  155 VAL   A CG1  1 
ATOM   3344 C CG1  B VAL   A 1 155 ? 10.444 -3.573  3.551   0.40 14.83 ?  155 VAL   A CG1  1 
ATOM   3345 C CG2  A VAL   A 1 155 ? 11.438 -5.618  4.430   0.60 15.80 ?  155 VAL   A CG2  1 
ATOM   3346 C CG2  B VAL   A 1 155 ? 11.981 -5.323  4.472   0.40 14.38 ?  155 VAL   A CG2  1 
ATOM   3347 H H    A VAL   A 1 155 ? 11.750 -4.086  7.158   0.60 17.94 ?  155 VAL   A H    1 
ATOM   3348 H H    B VAL   A 1 155 ? 11.836 -3.821  7.391   0.40 16.53 ?  155 VAL   A H    1 
ATOM   3349 H HA   A VAL   A 1 155 ? 12.308 -3.093  4.691   0.60 19.10 ?  155 VAL   A HA   1 
ATOM   3350 H HA   B VAL   A 1 155 ? 12.566 -2.758  4.993   0.40 17.58 ?  155 VAL   A HA   1 
ATOM   3351 H HB   A VAL   A 1 155 ? 10.020 -4.573  5.475   0.60 19.12 ?  155 VAL   A HB   1 
ATOM   3352 H HB   B VAL   A 1 155 ? 10.356 -4.485  5.383   0.40 17.61 ?  155 VAL   A HB   1 
ATOM   3353 H HG11 A VAL   A 1 155 ? 9.479  -4.519  3.141   0.60 19.99 ?  155 VAL   A HG11 1 
ATOM   3354 H HG11 B VAL   A 1 155 ? 10.123 -4.299  2.996   0.40 17.77 ?  155 VAL   A HG11 1 
ATOM   3355 H HG12 A VAL   A 1 155 ? 9.296  -3.128  3.885   0.60 19.99 ?  155 VAL   A HG12 1 
ATOM   3356 H HG12 B VAL   A 1 155 ? 9.704  -2.995  3.798   0.40 17.77 ?  155 VAL   A HG12 1 
ATOM   3357 H HG13 A VAL   A 1 155 ? 10.582 -3.387  2.986   0.60 19.99 ?  155 VAL   A HG13 1 
ATOM   3358 H HG13 B VAL   A 1 155 ? 11.115 -3.064  3.072   0.40 17.77 ?  155 VAL   A HG13 1 
ATOM   3359 H HG21 A VAL   A 1 155 ? 10.819 -6.257  4.046   0.60 18.94 ?  155 VAL   A HG21 1 
ATOM   3360 H HG21 B VAL   A 1 155 ? 11.474 -5.980  3.970   0.40 17.24 ?  155 VAL   A HG21 1 
ATOM   3361 H HG22 A VAL   A 1 155 ? 12.129 -5.397  3.786   0.60 18.94 ?  155 VAL   A HG22 1 
ATOM   3362 H HG22 B VAL   A 1 155 ? 12.723 -4.998  3.938   0.40 17.24 ?  155 VAL   A HG22 1 
ATOM   3363 H HG23 A VAL   A 1 155 ? 11.841 -5.989  5.232   0.60 18.94 ?  155 VAL   A HG23 1 
ATOM   3364 H HG23 B VAL   A 1 155 ? 12.313 -5.718  5.294   0.40 17.24 ?  155 VAL   A HG23 1 
ATOM   3365 N N    A PHE   A 1 156 ? 11.273 -0.915  5.065   0.60 18.47 ?  156 PHE   A N    1 
ATOM   3366 N N    B PHE   A 1 156 ? 11.433 -0.679  5.575   0.40 16.34 ?  156 PHE   A N    1 
ATOM   3367 C CA   A PHE   A 1 156 ? 10.780 0.400   5.467   0.60 20.09 ?  156 PHE   A CA   1 
ATOM   3368 C CA   B PHE   A 1 156 ? 10.767 0.571   5.946   0.40 17.82 ?  156 PHE   A CA   1 
ATOM   3369 C C    A PHE   A 1 156 ? 9.328  0.612   5.060   0.60 20.55 ?  156 PHE   A C    1 
ATOM   3370 C C    B PHE   A 1 156 ? 9.638  0.925   4.971   0.40 18.22 ?  156 PHE   A C    1 
ATOM   3371 O O    A PHE   A 1 156 ? 8.555  1.222   5.807   0.60 22.06 ?  156 PHE   A O    1 
ATOM   3372 O O    B PHE   A 1 156 ? 9.615  1.984   4.342   0.40 18.07 ?  156 PHE   A O    1 
ATOM   3373 C CB   A PHE   A 1 156 ? 11.679 1.489   4.873   0.60 21.45 ?  156 PHE   A CB   1 
ATOM   3374 C CB   B PHE   A 1 156 ? 11.806 1.683   6.008   0.40 18.96 ?  156 PHE   A CB   1 
ATOM   3375 C CG   A PHE   A 1 156 ? 11.231 2.893   5.184   0.60 23.24 ?  156 PHE   A CG   1 
ATOM   3376 C CG   B PHE   A 1 156 ? 11.356 2.907   6.750   0.40 20.53 ?  156 PHE   A CG   1 
ATOM   3377 C CD1  A PHE   A 1 156 ? 11.228 3.361   6.489   0.60 24.20 ?  156 PHE   A CD1  1 
ATOM   3378 C CD1  B PHE   A 1 156 ? 10.272 2.868   7.614   0.40 21.06 ?  156 PHE   A CD1  1 
ATOM   3379 C CD2  A PHE   A 1 156 ? 10.833 3.749   4.169   0.60 24.11 ?  156 PHE   A CD2  1 
ATOM   3380 C CD2  B PHE   A 1 156 ? 12.027 4.103   6.580   0.40 21.25 ?  156 PHE   A CD2  1 
ATOM   3381 C CE1  A PHE   A 1 156 ? 10.822 4.651   6.779   0.60 25.13 ?  156 PHE   A CE1  1 
ATOM   3382 C CE1  B PHE   A 1 156 ? 9.871  3.997   8.290   0.40 21.41 ?  156 PHE   A CE1  1 
ATOM   3383 C CE2  A PHE   A 1 156 ? 10.427 5.042   4.451   0.60 24.96 ?  156 PHE   A CE2  1 
ATOM   3384 C CE2  B PHE   A 1 156 ? 11.630 5.235   7.254   0.40 21.68 ?  156 PHE   A CE2  1 
ATOM   3385 C CZ   A PHE   A 1 156 ? 10.425 5.495   5.758   0.60 25.31 ?  156 PHE   A CZ   1 
ATOM   3386 C CZ   B PHE   A 1 156 ? 10.550 5.182   8.111   0.40 21.61 ?  156 PHE   A CZ   1 
ATOM   3387 H H    A PHE   A 1 156 ? 11.781 -0.910  4.369   0.60 22.15 ?  156 PHE   A H    1 
ATOM   3388 H H    B PHE   A 1 156 ? 12.166 -0.552  5.145   0.40 19.58 ?  156 PHE   A H    1 
ATOM   3389 H HA   A PHE   A 1 156 ? 10.828 0.467   6.430   0.60 24.08 ?  156 PHE   A HA   1 
ATOM   3390 H HA   B PHE   A 1 156 ? 10.379 0.447   6.824   0.40 21.36 ?  156 PHE   A HA   1 
ATOM   3391 H HB2  A PHE   A 1 156 ? 12.575 1.379   5.229   0.60 25.71 ?  156 PHE   A HB2  1 
ATOM   3392 H HB2  B PHE   A 1 156 ? 12.600 1.347   6.453   0.40 22.73 ?  156 PHE   A HB2  1 
ATOM   3393 H HB3  A PHE   A 1 156 ? 11.694 1.391   3.909   0.60 25.71 ?  156 PHE   A HB3  1 
ATOM   3394 H HB3  B PHE   A 1 156 ? 12.031 1.955   5.103   0.40 22.73 ?  156 PHE   A HB3  1 
ATOM   3395 H HD1  A PHE   A 1 156 ? 11.495 2.795   7.180   0.60 29.01 ?  156 PHE   A HD1  1 
ATOM   3396 H HD1  B PHE   A 1 156 ? 9.811  2.069   7.740   0.40 25.25 ?  156 PHE   A HD1  1 
ATOM   3397 H HD2  A PHE   A 1 156 ? 10.834 3.448   3.289   0.60 28.91 ?  156 PHE   A HD2  1 
ATOM   3398 H HD2  B PHE   A 1 156 ? 12.756 4.148   6.004   0.40 25.48 ?  156 PHE   A HD2  1 
ATOM   3399 H HE1  A PHE   A 1 156 ? 10.821 4.951   7.660   0.60 30.13 ?  156 PHE   A HE1  1 
ATOM   3400 H HE1  B PHE   A 1 156 ? 9.142  3.955   8.867   0.40 25.67 ?  156 PHE   A HE1  1 
ATOM   3401 H HE2  A PHE   A 1 156 ? 10.159 5.605   3.763   0.60 29.93 ?  156 PHE   A HE2  1 
ATOM   3402 H HE2  B PHE   A 1 156 ? 12.087 6.036   7.132   0.40 26.00 ?  156 PHE   A HE2  1 
ATOM   3403 H HZ   A PHE   A 1 156 ? 10.151 6.362   5.950   0.60 30.35 ?  156 PHE   A HZ   1 
ATOM   3404 H HZ   B PHE   A 1 156 ? 10.279 5.945   8.566   0.40 25.91 ?  156 PHE   A HZ   1 
ATOM   3405 N N    A ASP   A 1 157 ? 8.946  0.115   3.889   0.60 20.21 ?  157 ASP   A N    1 
ATOM   3406 N N    B ASP   A 1 157 ? 8.667  0.021   4.883   0.40 18.84 ?  157 ASP   A N    1 
ATOM   3407 C CA   A ASP   A 1 157 ? 7.632  0.372   3.313   0.60 20.47 ?  157 ASP   A CA   1 
ATOM   3408 C CA   B ASP   A 1 157 ? 7.515  0.194   4.007   0.40 19.91 ?  157 ASP   A CA   1 
ATOM   3409 C C    A ASP   A 1 157 ? 6.645  -0.682  3.811   0.60 20.40 ?  157 ASP   A C    1 
ATOM   3410 C C    B ASP   A 1 157 ? 6.457  -0.827  4.398   0.40 20.59 ?  157 ASP   A C    1 
ATOM   3411 O O    A ASP   A 1 157 ? 6.849  -1.882  3.593   0.60 19.46 ?  157 ASP   A O    1 
ATOM   3412 O O    B ASP   A 1 157 ? 6.628  -2.026  4.157   0.40 20.40 ?  157 ASP   A O    1 
ATOM   3413 C CB   A ASP   A 1 157 ? 7.758  0.314   1.793   0.60 21.41 ?  157 ASP   A CB   1 
ATOM   3414 C CB   B ASP   A 1 157 ? 7.931  -0.005  2.546   0.40 20.07 ?  157 ASP   A CB   1 
ATOM   3415 C CG   A ASP   A 1 157 ? 6.533  0.812   1.087   0.60 22.82 ?  157 ASP   A CG   1 
ATOM   3416 C CG   B ASP   A 1 157 ? 6.810  0.278   1.563   0.40 20.42 ?  157 ASP   A CG   1 
ATOM   3417 O OD1  A ASP   A 1 157 ? 6.423  2.039   0.921   0.60 24.30 ?  157 ASP   A OD1  1 
ATOM   3418 O OD1  B ASP   A 1 157 ? 5.627  0.244   1.956   0.40 20.03 ?  157 ASP   A OD1  1 
ATOM   3419 O OD2  A ASP   A 1 157 ? 5.696  -0.018  0.682   0.60 22.38 -1 157 ASP   A OD2  1 
ATOM   3420 O OD2  B ASP   A 1 157 ? 7.122  0.528   0.380   0.40 21.01 -1 157 ASP   A OD2  1 
ATOM   3421 H H    A ASP   A 1 157 ? 9.445  -0.383  3.394   0.60 24.23 ?  157 ASP   A H    1 
ATOM   3422 H H    B ASP   A 1 157 ? 8.656  -0.707  5.333   0.40 22.58 ?  157 ASP   A H    1 
ATOM   3423 H HA   A ASP   A 1 157 ? 7.319  1.250   3.573   0.60 24.54 ?  157 ASP   A HA   1 
ATOM   3424 H HA   B ASP   A 1 157 ? 7.148  1.088   4.115   0.40 23.86 ?  157 ASP   A HA   1 
ATOM   3425 H HB2  A ASP   A 1 157 ? 8.494  0.879   1.516   0.60 25.67 ?  157 ASP   A HB2  1 
ATOM   3426 H HB2  B ASP   A 1 157 ? 8.650  0.603   2.338   0.40 24.06 ?  157 ASP   A HB2  1 
ATOM   3427 H HB3  A ASP   A 1 157 ? 7.916  -0.597  1.518   0.60 25.67 ?  157 ASP   A HB3  1 
ATOM   3428 H HB3  B ASP   A 1 157 ? 8.220  -0.924  2.425   0.40 24.06 ?  157 ASP   A HB3  1 
ATOM   3429 N N    A LYS   A 1 158 ? 5.574  -0.234  4.479   0.60 21.59 ?  158 LYS   A N    1 
ATOM   3430 N N    B LYS   A 1 158 ? 5.366  -0.367  5.014   0.40 21.36 ?  158 LYS   A N    1 
ATOM   3431 C CA   A LYS   A 1 158 ? 4.625  -1.174  5.076   0.60 22.53 ?  158 LYS   A CA   1 
ATOM   3432 C CA   B LYS   A 1 158 ? 4.355  -1.300  5.500   0.40 22.23 ?  158 LYS   A CA   1 
ATOM   3433 C C    A LYS   A 1 158 ? 3.888  -1.978  4.008   0.60 22.47 ?  158 LYS   A C    1 
ATOM   3434 C C    B LYS   A 1 158 ? 3.733  -2.086  4.352   0.40 22.13 ?  158 LYS   A C    1 
ATOM   3435 O O    A LYS   A 1 158 ? 3.713  -3.194  4.148   0.60 22.13 ?  158 LYS   A O    1 
ATOM   3436 O O    B LYS   A 1 158 ? 3.488  -3.292  4.477   0.40 22.06 ?  158 LYS   A O    1 
ATOM   3437 C CB   A LYS   A 1 158 ? 3.644  -0.426  5.988   0.60 23.67 ?  158 LYS   A CB   1 
ATOM   3438 C CB   B LYS   A 1 158 ? 3.286  -0.544  6.291   0.40 23.35 ?  158 LYS   A CB   1 
ATOM   3439 C CG   A LYS   A 1 158 ? 2.421  -1.240  6.434   0.60 25.13 ?  158 LYS   A CG   1 
ATOM   3440 C CG   B LYS   A 1 158 ? 2.195  -1.422  6.894   0.40 24.35 ?  158 LYS   A CG   1 
ATOM   3441 C CD   A LYS   A 1 158 ? 2.792  -2.488  7.238   0.60 26.28 ?  158 LYS   A CD   1 
ATOM   3442 C CD   B LYS   A 1 158 ? 2.761  -2.480  7.833   0.40 25.05 ?  158 LYS   A CD   1 
ATOM   3443 C CE   A LYS   A 1 158 ? 1.541  -3.249  7.676   0.60 27.03 ?  158 LYS   A CE   1 
ATOM   3444 C CE   B LYS   A 1 158 ? 1.646  -3.177  8.600   0.40 25.48 ?  158 LYS   A CE   1 
ATOM   3445 N NZ   A LYS   A 1 158 ? 1.854  -4.539  8.359   0.60 27.27 ?  158 LYS   A NZ   1 
ATOM   3446 N NZ   B LYS   A 1 158 ? 2.117  -4.412  9.281   0.40 25.69 ?  158 LYS   A NZ   1 
ATOM   3447 H H    A LYS   A 1 158 ? 5.382  0.596   4.600   0.60 25.89 ?  158 LYS   A H    1 
ATOM   3448 H H    B LYS   A 1 158 ? 5.194  0.464   5.159   0.40 25.61 ?  158 LYS   A H    1 
ATOM   3449 H HA   A LYS   A 1 158 ? 5.113  -1.796  5.633   0.60 27.02 ?  158 LYS   A HA   1 
ATOM   3450 H HA   B LYS   A 1 158 ? 4.778  -1.931  6.100   0.40 26.66 ?  158 LYS   A HA   1 
ATOM   3451 H HB2  A LYS   A 1 158 ? 4.113  -0.147  6.794   0.60 28.38 ?  158 LYS   A HB2  1 
ATOM   3452 H HB2  B LYS   A 1 158 ? 3.717  -0.071  7.021   0.40 27.99 ?  158 LYS   A HB2  1 
ATOM   3453 H HB3  A LYS   A 1 158 ? 3.315  0.359   5.522   0.60 28.38 ?  158 LYS   A HB3  1 
ATOM   3454 H HB3  B LYS   A 1 158 ? 2.856  0.094   5.701   0.40 27.99 ?  158 LYS   A HB3  1 
ATOM   3455 H HG2  A LYS   A 1 158 ? 1.863  -0.683  6.999   0.60 30.13 ?  158 LYS   A HG2  1 
ATOM   3456 H HG2  B LYS   A 1 158 ? 1.584  -0.864  7.402   0.40 29.20 ?  158 LYS   A HG2  1 
ATOM   3457 H HG3  A LYS   A 1 158 ? 1.914  -1.521  5.656   0.60 30.13 ?  158 LYS   A HG3  1 
ATOM   3458 H HG3  B LYS   A 1 158 ? 1.718  -1.874  6.181   0.40 29.20 ?  158 LYS   A HG3  1 
ATOM   3459 H HD2  A LYS   A 1 158 ? 3.333  -3.077  6.692   0.60 31.52 ?  158 LYS   A HD2  1 
ATOM   3460 H HD2  B LYS   A 1 158 ? 3.240  -3.147  7.316   0.40 30.04 ?  158 LYS   A HD2  1 
ATOM   3461 H HD3  A LYS   A 1 158 ? 3.279  -2.224  8.035   0.60 31.52 ?  158 LYS   A HD3  1 
ATOM   3462 H HD3  B LYS   A 1 158 ? 3.357  -2.057  8.473   0.40 30.04 ?  158 LYS   A HD3  1 
ATOM   3463 H HE2  A LYS   A 1 158 ? 1.036  -2.699  8.296   0.60 32.41 ?  158 LYS   A HE2  1 
ATOM   3464 H HE2  B LYS   A 1 158 ? 1.300  -2.573  9.278   0.40 30.55 ?  158 LYS   A HE2  1 
ATOM   3465 H HE3  A LYS   A 1 158 ? 1.001  -3.446  6.896   0.60 32.41 ?  158 LYS   A HE3  1 
ATOM   3466 H HE3  B LYS   A 1 158 ? 0.940  -3.422  7.982   0.40 30.55 ?  158 LYS   A HE3  1 
ATOM   3467 H HZ1  A LYS   A 1 158 ? 1.100  -4.950  8.596   0.60 32.70 ?  158 LYS   A HZ1  1 
ATOM   3468 H HZ1  B LYS   A 1 158 ? 1.427  -4.851  9.631   0.40 30.80 ?  158 LYS   A HZ1  1 
ATOM   3469 H HZ2  A LYS   A 1 158 ? 2.312  -5.070  7.810   0.60 32.70 ?  158 LYS   A HZ2  1 
ATOM   3470 H HZ2  B LYS   A 1 158 ? 2.532  -4.942  8.697   0.40 30.80 ?  158 LYS   A HZ2  1 
ATOM   3471 H HZ3  A LYS   A 1 158 ? 2.342  -4.388  9.088   0.60 32.70 ?  158 LYS   A HZ3  1 
ATOM   3472 H HZ3  B LYS   A 1 158 ? 2.685  -4.201  9.932   0.40 30.80 ?  158 LYS   A HZ3  1 
ATOM   3473 N N    A ASN   A 1 159 ? 3.438  -1.317  2.940   0.60 22.94 ?  159 ASN   A N    1 
ATOM   3474 N N    B ASN   A 1 159 ? 3.478  -1.426  3.220   0.40 22.06 ?  159 ASN   A N    1 
ATOM   3475 C CA   A ASN   A 1 159 ? 2.778  -2.039  1.858   0.60 23.33 ?  159 ASN   A CA   1 
ATOM   3476 C CA   B ASN   A 1 159 ? 2.837  -2.112  2.102   0.40 21.92 ?  159 ASN   A CA   1 
ATOM   3477 C C    A ASN   A 1 159 ? 3.701  -3.093  1.255   0.60 22.27 ?  159 ASN   A C    1 
ATOM   3478 C C    B ASN   A 1 159 ? 3.755  -3.170  1.497   0.40 21.06 ?  159 ASN   A C    1 
ATOM   3479 O O    A ASN   A 1 159 ? 3.251  -4.179  0.869   0.60 22.14 ?  159 ASN   A O    1 
ATOM   3480 O O    B ASN   A 1 159 ? 3.345  -4.322  1.304   0.40 20.15 ?  159 ASN   A O    1 
ATOM   3481 C CB   A ASN   A 1 159 ? 2.297  -1.051  0.795   0.60 24.84 ?  159 ASN   A CB   1 
ATOM   3482 C CB   B ASN   A 1 159 ? 2.387  -1.104  1.045   0.40 22.60 ?  159 ASN   A CB   1 
ATOM   3483 C CG   A ASN   A 1 159 ? 1.170  -0.160  1.293   0.60 26.31 ?  159 ASN   A CG   1 
ATOM   3484 C CG   B ASN   A 1 159 ? 1.681  -1.767  -0.119  0.40 23.20 ?  159 ASN   A CG   1 
ATOM   3485 O OD1  A ASN   A 1 159 ? 0.335  -0.593  2.084   0.60 26.91 ?  159 ASN   A OD1  1 
ATOM   3486 O OD1  B ASN   A 1 159 ? 2.288  -2.038  -1.155  0.40 23.49 ?  159 ASN   A OD1  1 
ATOM   3487 N ND2  A ASN   A 1 159 ? 1.145  1.087   0.835   0.60 27.09 ?  159 ASN   A ND2  1 
ATOM   3488 N ND2  B ASN   A 1 159 ? 0.393  -2.051  0.054   0.40 23.63 ?  159 ASN   A ND2  1 
ATOM   3489 H H    A ASN   A 1 159 ? 3.496  -0.468  2.827   0.60 27.50 ?  159 ASN   A H    1 
ATOM   3490 H H    B ASN   A 1 159 ? 3.656  -0.596  3.081   0.40 26.44 ?  159 ASN   A H    1 
ATOM   3491 H HA   A ASN   A 1 159 ? 2.000  -2.497  2.216   0.60 27.98 ?  159 ASN   A HA   1 
ATOM   3492 H HA   B ASN   A 1 159 ? 2.044  -2.561  2.430   0.40 26.28 ?  159 ASN   A HA   1 
ATOM   3493 H HB2  A ASN   A 1 159 ? 3.035  -0.481  0.536   0.60 29.78 ?  159 ASN   A HB2  1 
ATOM   3494 H HB2  B ASN   A 1 159 ? 1.770  -0.469  1.448   0.40 27.10 ?  159 ASN   A HB2  1 
ATOM   3495 H HB3  A ASN   A 1 159 ? 1.970  -1.547  0.029   0.60 29.78 ?  159 ASN   A HB3  1 
ATOM   3496 H HB3  B ASN   A 1 159 ? 3.161  -0.635  0.696   0.40 27.10 ?  159 ASN   A HB3  1 
ATOM   3497 H HD21 A ASN   A 1 159 ? 0.527  1.628   1.091   0.60 32.48 ?  159 ASN   A HD21 1 
ATOM   3498 H HD21 B ASN   A 1 159 ? -0.054 -2.429  -0.576  0.40 28.34 ?  159 ASN   A HD21 1 
ATOM   3499 H HD22 A ASN   A 1 159 ? 1.751  1.354   0.287   0.60 32.48 ?  159 ASN   A HD22 1 
ATOM   3500 H HD22 B ASN   A 1 159 ? 0.002  -1.853  0.795   0.40 28.34 ?  159 ASN   A HD22 1 
ATOM   3501 N N    . LEU   A 1 160 ? 4.999  -2.796  1.177   1.00 21.40 ?  160 LEU   A N    1 
ATOM   3502 C CA   . LEU   A 1 160 ? 5.945  -3.770  0.644   1.00 21.06 ?  160 LEU   A CA   1 
ATOM   3503 C C    . LEU   A 1 160 ? 6.163  -4.909  1.627   1.00 20.23 ?  160 LEU   A C    1 
ATOM   3504 O O    . LEU   A 1 160 ? 6.211  -6.079  1.229   1.00 21.10 ?  160 LEU   A O    1 
ATOM   3505 C CB   . LEU   A 1 160 ? 7.276  -3.097  0.316   1.00 20.93 ?  160 LEU   A CB   1 
ATOM   3506 C CG   . LEU   A 1 160 ? 8.375  -4.075  -0.109  1.00 21.00 ?  160 LEU   A CG   1 
ATOM   3507 C CD1  . LEU   A 1 160 ? 7.949  -4.794  -1.367  1.00 21.74 ?  160 LEU   A CD1  1 
ATOM   3508 C CD2  . LEU   A 1 160 ? 9.691  -3.369  -0.313  1.00 20.84 ?  160 LEU   A CD2  1 
ATOM   3509 H H    A LEU   A 1 160 ? 5.349  -2.052  1.427   0.60 25.65 ?  160 LEU   A H    1 
ATOM   3510 H H    B LEU   A 1 160 ? 5.311  -2.001  1.266   0.40 25.65 ?  160 LEU   A H    1 
ATOM   3511 H HA   . LEU   A 1 160 ? 5.581  -4.147  -0.168  1.00 25.25 ?  160 LEU   A HA   1 
ATOM   3512 H HB2  . LEU   A 1 160 ? 7.134  -2.462  -0.405  1.00 25.10 ?  160 LEU   A HB2  1 
ATOM   3513 H HB3  . LEU   A 1 160 ? 7.587  -2.637  1.108   1.00 25.10 ?  160 LEU   A HB3  1 
ATOM   3514 H HG   . LEU   A 1 160 ? 8.499  -4.739  0.588   1.00 25.18 ?  160 LEU   A HG   1 
ATOM   3515 H HD11 . LEU   A 1 160 ? 8.670  -5.369  -1.651  1.00 26.06 ?  160 LEU   A HD11 1 
ATOM   3516 H HD12 . LEU   A 1 160 ? 7.158  -5.327  -1.180  1.00 26.06 ?  160 LEU   A HD12 1 
ATOM   3517 H HD13 . LEU   A 1 160 ? 7.751  -4.136  -2.051  1.00 26.06 ?  160 LEU   A HD13 1 
ATOM   3518 H HD21 . LEU   A 1 160 ? 10.294 -3.619  0.402   1.00 24.99 ?  160 LEU   A HD21 1 
ATOM   3519 H HD22 . LEU   A 1 160 ? 10.058 -3.633  -1.171  1.00 24.99 ?  160 LEU   A HD22 1 
ATOM   3520 H HD23 . LEU   A 1 160 ? 9.521  -2.422  -0.296  1.00 24.99 ?  160 LEU   A HD23 1 
ATOM   3521 N N    . TYR   A 1 161 ? 6.319  -4.584  2.912   1.00 19.87 ?  161 TYR   A N    1 
ATOM   3522 C CA   . TYR   A 1 161 ? 6.452  -5.624  3.928   1.00 19.70 ?  161 TYR   A CA   1 
ATOM   3523 C C    . TYR   A 1 161 ? 5.297  -6.615  3.850   1.00 20.17 ?  161 TYR   A C    1 
ATOM   3524 O O    . TYR   A 1 161 ? 5.502  -7.834  3.832   1.00 20.17 ?  161 TYR   A O    1 
ATOM   3525 C CB   . TYR   A 1 161 ? 6.534  -4.992  5.320   1.00 19.93 ?  161 TYR   A CB   1 
ATOM   3526 C CG   . TYR   A 1 161 ? 6.428  -6.004  6.432   1.00 19.60 ?  161 TYR   A CG   1 
ATOM   3527 C CD1  . TYR   A 1 161 ? 7.544  -6.702  6.868   1.00 19.31 ?  161 TYR   A CD1  1 
ATOM   3528 C CD2  . TYR   A 1 161 ? 5.208  -6.269  7.041   1.00 20.00 ?  161 TYR   A CD2  1 
ATOM   3529 C CE1  . TYR   A 1 161 ? 7.456  -7.637  7.874   1.00 19.89 ?  161 TYR   A CE1  1 
ATOM   3530 C CE2  . TYR   A 1 161 ? 5.103  -7.203  8.050   1.00 20.24 ?  161 TYR   A CE2  1 
ATOM   3531 C CZ   . TYR   A 1 161 ? 6.233  -7.889  8.466   1.00 20.70 ?  161 TYR   A CZ   1 
ATOM   3532 O OH   . TYR   A 1 161 ? 6.143  -8.824  9.476   1.00 22.38 ?  161 TYR   A OH   1 
ATOM   3533 H H    . TYR   A 1 161 ? 6.346  -3.783  3.219   1.00 23.82 ?  161 TYR   A H    1 
ATOM   3534 H HA   . TYR   A 1 161 ? 7.274  -6.111  3.780   1.00 23.62 ?  161 TYR   A HA   1 
ATOM   3535 H HB2  . TYR   A 1 161 ? 7.387  -4.539  5.414   1.00 23.90 ?  161 TYR   A HB2  1 
ATOM   3536 H HB3  . TYR   A 1 161 ? 5.809  -4.356  5.426   1.00 23.90 ?  161 TYR   A HB3  1 
ATOM   3537 H HD1  . TYR   A 1 161 ? 8.365  -6.537  6.469   1.00 23.15 ?  161 TYR   A HD1  1 
ATOM   3538 H HD2  . TYR   A 1 161 ? 4.443  -5.811  6.763   1.00 23.98 ?  161 TYR   A HD2  1 
ATOM   3539 H HE1  . TYR   A 1 161 ? 8.210  -8.097  8.152   1.00 23.85 ?  161 TYR   A HE1  1 
ATOM   3540 H HE2  . TYR   A 1 161 ? 4.274  -7.371  8.449   1.00 24.26 ?  161 TYR   A HE2  1 
ATOM   3541 H HH   . TYR   A 1 161 ? 5.334  -8.877  9.741   1.00 26.83 ?  161 TYR   A HH   1 
ATOM   3542 N N    A ASP   A 1 162 ? 4.067  -6.114  3.721   0.60 20.58 ?  162 ASP   A N    1 
ATOM   3543 N N    B ASP   A 1 162 ? 4.069  -6.092  3.879   0.40 20.57 ?  162 ASP   A N    1 
ATOM   3544 C CA   A ASP   A 1 162 ? 2.917  -7.015  3.656   0.60 21.28 ?  162 ASP   A CA   1 
ATOM   3545 C CA   B ASP   A 1 162 ? 2.893  -6.943  3.767   0.40 21.15 ?  162 ASP   A CA   1 
ATOM   3546 C C    A ASP   A 1 162 ? 2.972  -7.909  2.419   0.60 21.00 ?  162 ASP   A C    1 
ATOM   3547 C C    B ASP   A 1 162 ? 2.893  -7.698  2.446   0.40 21.05 ?  162 ASP   A C    1 
ATOM   3548 O O    A ASP   A 1 162 ? 2.652  -9.103  2.491   0.60 21.15 ?  162 ASP   A O    1 
ATOM   3549 O O    B ASP   A 1 162 ? 2.444  -8.849  2.384   0.40 21.22 ?  162 ASP   A O    1 
ATOM   3550 C CB   A ASP   A 1 162 ? 1.611  -6.214  3.680   0.60 22.60 ?  162 ASP   A CB   1 
ATOM   3551 C CB   B ASP   A 1 162 ? 1.630  -6.087  3.903   0.40 22.05 ?  162 ASP   A CB   1 
ATOM   3552 C CG   A ASP   A 1 162 ? 1.256  -5.695  5.065   0.60 23.96 ?  162 ASP   A CG   1 
ATOM   3553 C CG   B ASP   A 1 162 ? 1.515  -5.416  5.262   0.40 23.15 ?  162 ASP   A CG   1 
ATOM   3554 O OD1  A ASP   A 1 162 ? 1.885  -6.123  6.053   0.60 25.27 ?  162 ASP   A OD1  1 
ATOM   3555 O OD1  B ASP   A 1 162 ? 2.188  -5.860  6.215   0.40 23.98 ?  162 ASP   A OD1  1 
ATOM   3556 O OD2  A ASP   A 1 162 ? 0.321  -4.867  5.165   0.60 24.08 -1 162 ASP   A OD2  1 
ATOM   3557 O OD2  B ASP   A 1 162 ? 0.730  -4.449  5.381   0.40 23.91 -1 162 ASP   A OD2  1 
ATOM   3558 H H    A ASP   A 1 162 ? 3.874  -5.280  3.666   0.60 24.67 ?  162 ASP   A H    1 
ATOM   3559 H H    B ASP   A 1 162 ? 3.896  -5.252  3.967   0.40 24.66 ?  162 ASP   A H    1 
ATOM   3560 H HA   A ASP   A 1 162 ? 2.923  -7.596  4.429   0.60 25.51 ?  162 ASP   A HA   1 
ATOM   3561 H HA   B ASP   A 1 162 ? 2.897  -7.587  4.487   0.40 25.36 ?  162 ASP   A HA   1 
ATOM   3562 H HB2  A ASP   A 1 162 ? 1.691  -5.457  3.084   0.60 27.09 ?  162 ASP   A HB2  1 
ATOM   3563 H HB2  B ASP   A 1 162 ? 1.646  -5.390  3.230   0.40 26.43 ?  162 ASP   A HB2  1 
ATOM   3564 H HB3  A ASP   A 1 162 ? 0.881  -6.788  3.399   0.60 27.09 ?  162 ASP   A HB3  1 
ATOM   3565 H HB3  B ASP   A 1 162 ? 0.847  -6.641  3.787   0.40 26.43 ?  162 ASP   A HB3  1 
ATOM   3566 N N    A LYS   A 1 163 ? 3.361  -7.350  1.271   0.60 21.47 ?  163 LYS   A N    1 
ATOM   3567 N N    B LYS   A 1 163 ? 3.396  -7.070  1.383   0.40 21.33 ?  163 LYS   A N    1 
ATOM   3568 C CA   A LYS   A 1 163 ? 3.449  -8.144  0.047   0.60 21.80 ?  163 LYS   A CA   1 
ATOM   3569 C CA   B LYS   A 1 163 ? 3.485  -7.748  0.095   0.40 21.43 ?  163 LYS   A CA   1 
ATOM   3570 C C    A LYS   A 1 163 ? 4.564  -9.178  0.139   0.60 21.12 ?  163 LYS   A C    1 
ATOM   3571 C C    B LYS   A 1 163 ? 4.497  -8.888  0.132   0.40 20.89 ?  163 LYS   A C    1 
ATOM   3572 O O    A LYS   A 1 163 ? 4.418  -10.305 -0.347  0.60 22.04 ?  163 LYS   A O    1 
ATOM   3573 O O    B LYS   A 1 163 ? 4.261  -9.949  -0.456  0.40 20.88 ?  163 LYS   A O    1 
ATOM   3574 C CB   A LYS   A 1 163 ? 3.668  -7.212  -1.146  0.60 23.71 ?  163 LYS   A CB   1 
ATOM   3575 C CB   B LYS   A 1 163 ? 3.862  -6.745  -0.993  0.40 22.69 ?  163 LYS   A CB   1 
ATOM   3576 C CG   A LYS   A 1 163 ? 3.691  -7.894  -2.503  0.60 25.95 ?  163 LYS   A CG   1 
ATOM   3577 C CG   B LYS   A 1 163 ? 3.986  -7.352  -2.381  0.40 24.00 ?  163 LYS   A CG   1 
ATOM   3578 C CD   A LYS   A 1 163 ? 4.060  -6.901  -3.596  0.60 27.85 ?  163 LYS   A CD   1 
ATOM   3579 C CD   B LYS   A 1 163 ? 5.155  -6.740  -3.125  0.40 25.20 ?  163 LYS   A CD   1 
ATOM   3580 C CE   A LYS   A 1 163 ? 3.911  -7.510  -4.981  0.60 29.16 ?  163 LYS   A CE   1 
ATOM   3581 C CE   B LYS   A 1 163 ? 5.002  -6.885  -4.627  0.40 26.07 ?  163 LYS   A CE   1 
ATOM   3582 N NZ   A LYS   A 1 163 ? 4.532  -6.664  -6.036  0.60 30.17 ?  163 LYS   A NZ   1 
ATOM   3583 N NZ   B LYS   A 1 163 ? 6.102  -6.185  -5.344  0.40 26.53 ?  163 LYS   A NZ   1 
ATOM   3584 H H    A LYS   A 1 163 ? 3.580  -6.527  1.174   0.60 25.74 ?  163 LYS   A H    1 
ATOM   3585 H H    B LYS   A 1 163 ? 3.679  -6.256  1.381   0.40 25.57 ?  163 LYS   A H    1 
ATOM   3586 H HA   A LYS   A 1 163 ? 2.613  -8.616  -0.092  0.60 26.13 ?  163 LYS   A HA   1 
ATOM   3587 H HA   B LYS   A 1 163 ? 2.618  -8.119  -0.125  0.40 25.70 ?  163 LYS   A HA   1 
ATOM   3588 H HB2  A LYS   A 1 163 ? 2.950  -6.559  -1.164  0.60 28.43 ?  163 LYS   A HB2  1 
ATOM   3589 H HB2  B LYS   A 1 163 ? 3.177  -6.056  -1.034  0.40 27.21 ?  163 LYS   A HB2  1 
ATOM   3590 H HB3  A LYS   A 1 163 ? 4.517  -6.758  -1.034  0.60 28.43 ?  163 LYS   A HB3  1 
ATOM   3591 H HB3  B LYS   A 1 163 ? 4.715  -6.344  -0.768  0.40 27.21 ?  163 LYS   A HB3  1 
ATOM   3592 H HG2  A LYS   A 1 163 ? 4.355  -8.600  -2.501  0.60 31.12 ?  163 LYS   A HG2  1 
ATOM   3593 H HG2  B LYS   A 1 163 ? 4.127  -8.311  -2.319  0.40 28.78 ?  163 LYS   A HG2  1 
ATOM   3594 H HG3  A LYS   A 1 163 ? 2.813  -8.254  -2.700  0.60 31.12 ?  163 LYS   A HG3  1 
ATOM   3595 H HG3  B LYS   A 1 163 ? 3.176  -7.169  -2.881  0.40 28.78 ?  163 LYS   A HG3  1 
ATOM   3596 H HD2  A LYS   A 1 163 ? 3.468  -6.133  -3.540  0.60 33.39 ?  163 LYS   A HD2  1 
ATOM   3597 H HD2  B LYS   A 1 163 ? 5.208  -5.796  -2.914  0.40 30.22 ?  163 LYS   A HD2  1 
ATOM   3598 H HD3  A LYS   A 1 163 ? 4.981  -6.624  -3.479  0.60 33.39 ?  163 LYS   A HD3  1 
ATOM   3599 H HD3  B LYS   A 1 163 ? 5.973  -7.190  -2.857  0.40 30.22 ?  163 LYS   A HD3  1 
ATOM   3600 H HE2  A LYS   A 1 163 ? 4.323  -8.386  -5.004  0.60 34.97 ?  163 LYS   A HE2  1 
ATOM   3601 H HE2  B LYS   A 1 163 ? 5.026  -7.825  -4.864  0.40 31.26 ?  163 LYS   A HE2  1 
ATOM   3602 H HE3  A LYS   A 1 163 ? 2.970  -7.589  -5.182  0.60 34.97 ?  163 LYS   A HE3  1 
ATOM   3603 H HE3  B LYS   A 1 163 ? 4.159  -6.492  -4.901  0.40 31.26 ?  163 LYS   A HE3  1 
ATOM   3604 H HZ1  A LYS   A 1 163 ? 4.431  -7.050  -6.832  0.60 36.18 ?  163 LYS   A HZ1  1 
ATOM   3605 H HZ1  B LYS   A 1 163 ? 5.999  -6.277  -6.223  0.40 31.81 ?  163 LYS   A HZ1  1 
ATOM   3606 H HZ2  A LYS   A 1 163 ? 4.142  -5.864  -6.050  0.60 36.18 ?  163 LYS   A HZ2  1 
ATOM   3607 H HZ2  B LYS   A 1 163 ? 6.093  -5.317  -5.141  0.40 31.81 ?  163 LYS   A HZ2  1 
ATOM   3608 H HZ3  A LYS   A 1 163 ? 5.401  -6.560  -5.874  0.60 36.18 ?  163 LYS   A HZ3  1 
ATOM   3609 H HZ3  B LYS   A 1 163 ? 6.888  -6.528  -5.107  0.40 31.81 ?  163 LYS   A HZ3  1 
ATOM   3610 N N    A LEU   A 1 164 ? 5.693  -8.803  0.744   0.60 19.21 ?  164 LEU   A N    1 
ATOM   3611 N N    B LEU   A 1 164 ? 5.641  -8.684  0.790   0.40 20.10 ?  164 LEU   A N    1 
ATOM   3612 C CA   A LEU   A 1 164 ? 6.795  -9.741  0.949   0.60 17.97 ?  164 LEU   A CA   1 
ATOM   3613 C CA   B LEU   A 1 164 ? 6.674  -9.718  0.785   0.40 19.71 ?  164 LEU   A CA   1 
ATOM   3614 C C    A LEU   A 1 164 ? 6.353  -10.924 1.795   0.60 18.25 ?  164 LEU   A C    1 
ATOM   3615 C C    B LEU   A 1 164 ? 6.279  -10.909 1.649   0.40 19.99 ?  164 LEU   A C    1 
ATOM   3616 O O    A LEU   A 1 164 ? 6.673  -12.078 1.490   0.60 18.63 ?  164 LEU   A O    1 
ATOM   3617 O O    B LEU   A 1 164 ? 6.502  -12.060 1.259   0.40 20.02 ?  164 LEU   A O    1 
ATOM   3618 C CB   A LEU   A 1 164 ? 7.955  -9.018  1.634   0.60 16.48 ?  164 LEU   A CB   1 
ATOM   3619 C CB   B LEU   A 1 164 ? 8.012  -9.144  1.246   0.40 19.02 ?  164 LEU   A CB   1 
ATOM   3620 C CG   A LEU   A 1 164 ? 8.718  -7.989  0.796   0.60 16.02 ?  164 LEU   A CG   1 
ATOM   3621 C CG   B LEU   A 1 164 ? 8.725  -8.196  0.280   0.40 18.51 ?  164 LEU   A CG   1 
ATOM   3622 C CD1  A LEU   A 1 164 ? 9.632  -7.123  1.661   0.60 15.58 ?  164 LEU   A CD1  1 
ATOM   3623 C CD1  B LEU   A 1 164 ? 9.774  -7.401  1.028   0.40 18.00 ?  164 LEU   A CD1  1 
ATOM   3624 C CD2  A LEU   A 1 164 ? 9.518  -8.677  -0.301  0.60 16.39 ?  164 LEU   A CD2  1 
ATOM   3625 C CD2  B LEU   A 1 164 ? 9.357  -8.952  -0.880  0.40 18.72 ?  164 LEU   A CD2  1 
ATOM   3626 H H    A LEU   A 1 164 ? 5.849  -8.013  1.034   0.60 23.03 ?  164 LEU   A H    1 
ATOM   3627 H H    B LEU   A 1 164 ? 5.842  -7.969  1.230   0.40 24.09 ?  164 LEU   A H    1 
ATOM   3628 H HA   A LEU   A 1 164 ? 7.105  -10.080 0.096   0.60 21.54 ?  164 LEU   A HA   1 
ATOM   3629 H HA   B LEU   A 1 164 ? 6.787  -10.037 -0.122  0.40 23.63 ?  164 LEU   A HA   1 
ATOM   3630 H HB2  A LEU   A 1 164 ? 7.605  -8.551  2.410   0.60 19.76 ?  164 LEU   A HB2  1 
ATOM   3631 H HB2  B LEU   A 1 164 ? 7.867  -8.658  2.069   0.40 22.81 ?  164 LEU   A HB2  1 
ATOM   3632 H HB3  A LEU   A 1 164 ? 8.599  -9.681  1.926   0.60 19.76 ?  164 LEU   A HB3  1 
ATOM   3633 H HB3  B LEU   A 1 164 ? 8.615  -9.887  1.412   0.40 22.81 ?  164 LEU   A HB3  1 
ATOM   3634 H HG   A LEU   A 1 164 ? 8.080  -7.397  0.371   0.60 19.20 ?  164 LEU   A HG   1 
ATOM   3635 H HG   B LEU   A 1 164 ? 8.080  -7.572  -0.086  0.40 22.18 ?  164 LEU   A HG   1 
ATOM   3636 H HD11 A LEU   A 1 164 ? 10.080 -6.471  1.097   0.60 18.67 ?  164 LEU   A HD11 1 
ATOM   3637 H HD11 B LEU   A 1 164 ? 10.242 -6.828  0.401   0.40 21.58 ?  164 LEU   A HD11 1 
ATOM   3638 H HD12 A LEU   A 1 164 ? 9.096  -6.664  2.330   0.60 18.67 ?  164 LEU   A HD12 1 
ATOM   3639 H HD12 B LEU   A 1 164 ? 9.337  -6.864  1.706   0.40 21.58 ?  164 LEU   A HD12 1 
ATOM   3640 H HD13 A LEU   A 1 164 ? 10.288 -7.688  2.098   0.60 18.67 ?  164 LEU   A HD13 1 
ATOM   3641 H HD13 B LEU   A 1 164 ? 10.398 -8.017  1.444   0.40 21.58 ?  164 LEU   A HD13 1 
ATOM   3642 H HD21 A LEU   A 1 164 ? 10.046 -8.011  -0.770  0.60 19.64 ?  164 LEU   A HD21 1 
ATOM   3643 H HD21 B LEU   A 1 164 ? 9.811  -8.319  -1.459  0.40 22.44 ?  164 LEU   A HD21 1 
ATOM   3644 H HD22 A LEU   A 1 164 ? 10.099 -9.339  0.100   0.60 19.64 ?  164 LEU   A HD22 1 
ATOM   3645 H HD22 B LEU   A 1 164 ? 9.993  -9.595  -0.530  0.40 22.44 ?  164 LEU   A HD22 1 
ATOM   3646 H HD23 A LEU   A 1 164 ? 8.901  -9.103  -0.916  0.60 19.64 ?  164 LEU   A HD23 1 
ATOM   3647 H HD23 B LEU   A 1 164 ? 8.660  -9.411  -1.375  0.40 22.44 ?  164 LEU   A HD23 1 
ATOM   3648 N N    A VAL   A 1 165 ? 5.635  -10.650 2.882   0.60 18.31 ?  165 VAL   A N    1 
ATOM   3649 N N    B VAL   A 1 165 ? 5.707  -10.658 2.828   0.40 20.29 ?  165 VAL   A N    1 
ATOM   3650 C CA   A VAL   A 1 165 ? 5.150  -11.721 3.745   0.60 18.08 ?  165 VAL   A CA   1 
ATOM   3651 C CA   B VAL   A 1 165 ? 5.282  -11.769 3.677   0.40 20.61 ?  165 VAL   A CA   1 
ATOM   3652 C C    A VAL   A 1 165 ? 4.146  -12.593 3.001   0.60 18.57 ?  165 VAL   A C    1 
ATOM   3653 C C    B VAL   A 1 165 ? 4.142  -12.539 3.022   0.40 20.92 ?  165 VAL   A C    1 
ATOM   3654 O O    A VAL   A 1 165 ? 4.291  -13.819 2.936   0.60 18.48 ?  165 VAL   A O    1 
ATOM   3655 O O    B VAL   A 1 165 ? 4.118  -13.776 3.043   0.40 20.94 ?  165 VAL   A O    1 
ATOM   3656 C CB   A VAL   A 1 165 ? 4.560  -11.127 5.037   0.60 17.64 ?  165 VAL   A CB   1 
ATOM   3657 C CB   B VAL   A 1 165 ? 4.926  -11.290 5.099   0.40 20.87 ?  165 VAL   A CB   1 
ATOM   3658 C CG1  A VAL   A 1 165 ? 3.816  -12.195 5.829   0.60 17.65 ?  165 VAL   A CG1  1 
ATOM   3659 C CG1  B VAL   A 1 165 ? 3.936  -10.155 5.056   0.40 21.46 ?  165 VAL   A CG1  1 
ATOM   3660 C CG2  A VAL   A 1 165 ? 5.665  -10.491 5.878   0.60 17.74 ?  165 VAL   A CG2  1 
ATOM   3661 C CG2  B VAL   A 1 165 ? 4.349  -12.440 5.913   0.40 20.94 ?  165 VAL   A CG2  1 
ATOM   3662 H H    A VAL   A 1 165 ? 5.408  -9.864  3.141   0.60 21.95 ?  165 VAL   A H    1 
ATOM   3663 H H    B VAL   A 1 165 ? 5.556  -9.872  3.148   0.40 24.32 ?  165 VAL   A H    1 
ATOM   3664 H HA   A VAL   A 1 165 ? 5.892  -12.286 4.003   0.60 21.67 ?  165 VAL   A HA   1 
ATOM   3665 H HA   B VAL   A 1 165 ? 6.026  -12.378 3.764   0.40 24.71 ?  165 VAL   A HA   1 
ATOM   3666 H HB   A VAL   A 1 165 ? 3.917  -10.434 4.806   0.60 21.15 ?  165 VAL   A HB   1 
ATOM   3667 H HB   B VAL   A 1 165 ? 5.731  -10.977 5.546   0.40 25.02 ?  165 VAL   A HB   1 
ATOM   3668 H HG11 A VAL   A 1 165 ? 3.692  -11.883 6.740   0.60 21.16 ?  165 VAL   A HG11 1 
ATOM   3669 H HG11 B VAL   A 1 165 ? 4.331  -9.381  5.483   0.40 25.73 ?  165 VAL   A HG11 1 
ATOM   3670 H HG12 A VAL   A 1 165 ? 2.949  -12.353 5.418   0.60 21.16 ?  165 VAL   A HG12 1 
ATOM   3671 H HG12 B VAL   A 1 165 ? 3.721  -9.955  4.135   0.40 25.73 ?  165 VAL   A HG12 1 
ATOM   3672 H HG13 A VAL   A 1 165 ? 4.339  -13.009 5.827   0.60 21.16 ?  165 VAL   A HG13 1 
ATOM   3673 H HG13 B VAL   A 1 165 ? 3.136  -10.425 5.530   0.40 25.73 ?  165 VAL   A HG13 1 
ATOM   3674 H HG21 A VAL   A 1 165 ? 5.274  -10.120 6.686   0.60 21.27 ?  165 VAL   A HG21 1 
ATOM   3675 H HG21 B VAL   A 1 165 ? 4.315  -12.178 6.846   0.40 25.11 ?  165 VAL   A HG21 1 
ATOM   3676 H HG22 A VAL   A 1 165 ? 6.316  -11.170 6.105   0.60 21.27 ?  165 VAL   A HG22 1 
ATOM   3677 H HG22 B VAL   A 1 165 ? 3.454  -12.639 5.595   0.40 25.11 ?  165 VAL   A HG22 1 
ATOM   3678 H HG23 A VAL   A 1 165 ? 6.083  -9.786  5.360   0.60 21.27 ?  165 VAL   A HG23 1 
ATOM   3679 H HG23 B VAL   A 1 165 ? 4.919  -13.216 5.808   0.40 25.11 ?  165 VAL   A HG23 1 
ATOM   3680 N N    A SER   A 1 166 ? 3.125  -11.971 2.411   0.60 19.03 ?  166 SER   A N    1 
ATOM   3681 N N    B SER   A 1 166 ? 3.184  -11.827 2.428   0.40 21.16 ?  166 SER   A N    1 
ATOM   3682 C CA   A SER   A 1 166 ? 2.029  -12.736 1.823   0.60 19.62 ?  166 SER   A CA   1 
ATOM   3683 C CA   B SER   A 1 166 ? 2.037  -12.473 1.803   0.40 21.84 ?  166 SER   A CA   1 
ATOM   3684 C C    A SER   A 1 166 ? 2.484  -13.563 0.633   0.60 20.01 ?  166 SER   A C    1 
ATOM   3685 C C    B SER   A 1 166 ? 2.396  -13.223 0.529   0.40 22.12 ?  166 SER   A C    1 
ATOM   3686 O O    A SER   A 1 166 ? 1.915  -14.632 0.372   0.60 21.22 ?  166 SER   A O    1 
ATOM   3687 O O    B SER   A 1 166 ? 1.540  -13.938 -0.006  0.40 22.21 ?  166 SER   A O    1 
ATOM   3688 C CB   A SER   A 1 166 ? 0.901  -11.796 1.389   0.60 20.74 ?  166 SER   A CB   1 
ATOM   3689 C CB   B SER   A 1 166 ? 0.937  -11.444 1.523   0.40 22.60 ?  166 SER   A CB   1 
ATOM   3690 O OG   A SER   A 1 166 ? 0.279  -11.178 2.503   0.60 22.59 ?  166 SER   A OG   1 
ATOM   3691 O OG   B SER   A 1 166 ? 0.492  -10.836 2.723   0.40 23.62 ?  166 SER   A OG   1 
ATOM   3692 H H    A SER   A 1 166 ? 3.030  -11.127 2.353   0.60 22.81 ?  166 SER   A H    1 
ATOM   3693 H H    B SER   A 1 166 ? 3.171  -10.974 2.385   0.40 25.36 ?  166 SER   A H    1 
ATOM   3694 H HA   A SER   A 1 166 ? 1.660  -13.351 2.483   0.60 23.52 ?  166 SER   A HA   1 
ATOM   3695 H HA   B SER   A 1 166 ? 1.670  -13.119 2.417   0.40 26.18 ?  166 SER   A HA   1 
ATOM   3696 H HB2  A SER   A 1 166 ? 1.268  -11.107 0.815   0.60 24.86 ?  166 SER   A HB2  1 
ATOM   3697 H HB2  B SER   A 1 166 ? 1.282  -10.755 0.939   0.40 27.10 ?  166 SER   A HB2  1 
ATOM   3698 H HB3  A SER   A 1 166 ? 0.228  -12.304 0.902   0.60 24.86 ?  166 SER   A HB3  1 
ATOM   3699 H HB3  B SER   A 1 166 ? 0.182  -11.889 1.103   0.40 27.10 ?  166 SER   A HB3  1 
ATOM   3700 H HG   A SER   A 1 166 ? 0.848  -10.735 2.936   0.60 27.09 ?  166 SER   A HG   1 
ATOM   3701 H HG   B SER   A 1 166 ? 1.130  -10.449 3.107   0.40 28.32 ?  166 SER   A HG   1 
ATOM   3702 N N    A SER   A 1 167 ? 3.489  -13.089 -0.101  0.60 19.89 ?  167 SER   A N    1 
ATOM   3703 N N    B SER   A 1 167 ? 3.631  -13.095 0.040   0.40 22.62 ?  167 SER   A N    1 
ATOM   3704 C CA   A SER   A 1 167 ? 3.973  -13.782 -1.283  0.60 20.40 ?  167 SER   A CA   1 
ATOM   3705 C CA   B SER   A 1 167 ? 4.074  -13.823 -1.144  0.40 23.44 ?  167 SER   A CA   1 
ATOM   3706 C C    A SER   A 1 167 ? 5.136  -14.715 -0.983  0.60 20.13 ?  167 SER   A C    1 
ATOM   3707 C C    B SER   A 1 167 ? 5.231  -14.770 -0.850  0.40 23.96 ?  167 SER   A C    1 
ATOM   3708 O O    A SER   A 1 167 ? 5.632  -15.375 -1.902  0.60 21.56 ?  167 SER   A O    1 
ATOM   3709 O O    B SER   A 1 167 ? 5.800  -15.341 -1.788  0.40 24.53 ?  167 SER   A O    1 
ATOM   3710 C CB   A SER   A 1 167 ? 4.390  -12.773 -2.362  0.60 21.18 ?  167 SER   A CB   1 
ATOM   3711 C CB   B SER   A 1 167 ? 4.446  -12.860 -2.278  0.40 23.95 ?  167 SER   A CB   1 
ATOM   3712 O OG   A SER   A 1 167 ? 5.397  -11.897 -1.881  0.60 21.22 ?  167 SER   A OG   1 
ATOM   3713 O OG   B SER   A 1 167 ? 5.786  -12.421 -2.163  0.40 24.02 ?  167 SER   A OG   1 
ATOM   3714 H H    A SER   A 1 167 ? 3.898  -12.350 0.067   0.60 23.84 ?  167 SER   A H    1 
ATOM   3715 H H    B SER   A 1 167 ? 4.237  -12.588 0.385   0.40 27.13 ?  167 SER   A H    1 
ATOM   3716 H HA   A SER   A 1 167 ? 3.250  -14.315 -1.647  0.60 24.45 ?  167 SER   A HA   1 
ATOM   3717 H HA   B SER   A 1 167 ? 3.341  -14.366 -1.462  0.40 28.11 ?  167 SER   A HA   1 
ATOM   3718 H HB2  A SER   A 1 167 ? 4.735  -13.259 -3.128  0.60 25.39 ?  167 SER   A HB2  1 
ATOM   3719 H HB2  B SER   A 1 167 ? 4.335  -13.317 -3.128  0.40 28.71 ?  167 SER   A HB2  1 
ATOM   3720 H HB3  A SER   A 1 167 ? 3.607  -12.258 -2.630  0.60 25.39 ?  167 SER   A HB3  1 
ATOM   3721 H HB3  B SER   A 1 167 ? 3.862  -12.085 -2.243  0.40 28.71 ?  167 SER   A HB3  1 
ATOM   3722 H HG   A SER   A 1 167 ? 5.128  -11.518 -1.178  0.60 25.45 ?  167 SER   A HG   1 
ATOM   3723 H HG   B SER   A 1 167 ? 5.900  -12.029 -1.432  0.40 28.80 ?  167 SER   A HG   1 
ATOM   3724 N N    A PHE   A 1 168 ? 5.586  -14.786 0.267   0.60 18.68 ?  168 PHE   A N    1 
ATOM   3725 N N    B PHE   A 1 168 ? 5.592  -14.956 0.420   0.40 23.98 ?  168 PHE   A N    1 
ATOM   3726 C CA   A PHE   A 1 168 ? 6.755  -15.598 0.578   0.60 18.21 ?  168 PHE   A CA   1 
ATOM   3727 C CA   B PHE   A 1 168 ? 6.656  -15.880 0.798   0.40 24.45 ?  168 PHE   A CA   1 
ATOM   3728 C C    A PHE   A 1 168 ? 6.420  -17.075 0.451   0.60 18.96 ?  168 PHE   A C    1 
ATOM   3729 C C    B PHE   A 1 168 ? 6.159  -17.007 1.689   0.40 25.85 ?  168 PHE   A C    1 
ATOM   3730 O O    A PHE   A 1 168 ? 5.427  -17.552 1.010   0.60 20.53 ?  168 PHE   A O    1 
ATOM   3731 O O    B PHE   A 1 168 ? 6.433  -18.179 1.405   0.40 25.98 ?  168 PHE   A O    1 
ATOM   3732 C CB   A PHE   A 1 168 ? 7.266  -15.319 1.987   0.60 17.60 ?  168 PHE   A CB   1 
ATOM   3733 C CB   B PHE   A 1 168 ? 7.818  -15.135 1.484   0.40 23.91 ?  168 PHE   A CB   1 
ATOM   3734 C CG   A PHE   A 1 168 ? 8.531  -16.066 2.306   0.60 16.75 ?  168 PHE   A CG   1 
ATOM   3735 C CG   B PHE   A 1 168 ? 8.939  -16.040 1.929   0.40 23.20 ?  168 PHE   A CG   1 
ATOM   3736 C CD1  A PHE   A 1 168 ? 9.725  -15.679 1.730   0.60 17.02 ?  168 PHE   A CD1  1 
ATOM   3737 C CD1  B PHE   A 1 168 ? 8.930  -16.613 3.192   0.40 22.95 ?  168 PHE   A CD1  1 
ATOM   3738 C CD2  A PHE   A 1 168 ? 8.525  -17.177 3.140   0.60 16.30 ?  168 PHE   A CD2  1 
ATOM   3739 C CD2  B PHE   A 1 168 ? 10.000 -16.320 1.082   0.40 22.98 ?  168 PHE   A CD2  1 
ATOM   3740 C CE1  A PHE   A 1 168 ? 10.888 -16.365 1.990   0.60 16.74 ?  168 PHE   A CE1  1 
ATOM   3741 C CE1  B PHE   A 1 168 ? 9.956  -17.447 3.601   0.40 22.72 ?  168 PHE   A CE1  1 
ATOM   3742 C CE2  A PHE   A 1 168 ? 9.701  -17.865 3.409   0.60 16.51 ?  168 PHE   A CE2  1 
ATOM   3743 C CE2  B PHE   A 1 168 ? 11.030 -17.153 1.486   0.40 22.89 ?  168 PHE   A CE2  1 
ATOM   3744 C CZ   A PHE   A 1 168 ? 10.881 -17.453 2.830   0.60 16.73 ?  168 PHE   A CZ   1 
ATOM   3745 C CZ   B PHE   A 1 168 ? 11.007 -17.716 2.747   0.40 22.85 ?  168 PHE   A CZ   1 
ATOM   3746 H H    A PHE   A 1 168 ? 5.247  -14.369 0.937   0.60 22.40 ?  168 PHE   A H    1 
ATOM   3747 H H    B PHE   A 1 168 ? 5.228  -14.554 1.089   0.40 28.76 ?  168 PHE   A H    1 
ATOM   3748 H HA   A PHE   A 1 168 ? 7.467  -15.388 -0.051  0.60 21.83 ?  168 PHE   A HA   1 
ATOM   3749 H HA   B PHE   A 1 168 ? 7.013  -16.283 -0.006  0.40 29.32 ?  168 PHE   A HA   1 
ATOM   3750 H HB2  A PHE   A 1 168 ? 7.449  -14.370 2.075   0.60 21.10 ?  168 PHE   A HB2  1 
ATOM   3751 H HB2  B PHE   A 1 168 ? 8.191  -14.490 0.859   0.40 28.67 ?  168 PHE   A HB2  1 
ATOM   3752 H HB3  A PHE   A 1 168 ? 6.587  -15.587 2.625   0.60 21.10 ?  168 PHE   A HB3  1 
ATOM   3753 H HB3  B PHE   A 1 168 ? 7.482  -14.675 2.267   0.40 28.67 ?  168 PHE   A HB3  1 
ATOM   3754 H HD1  A PHE   A 1 168 ? 9.743  -14.942 1.163   0.60 20.40 ?  168 PHE   A HD1  1 
ATOM   3755 H HD1  B PHE   A 1 168 ? 8.226  -16.435 3.772   0.40 27.51 ?  168 PHE   A HD1  1 
ATOM   3756 H HD2  A PHE   A 1 168 ? 7.723  -17.458 3.529   0.60 19.54 ?  168 PHE   A HD2  1 
ATOM   3757 H HD2  B PHE   A 1 168 ? 10.023 -15.945 0.231   0.40 27.56 ?  168 PHE   A HD2  1 
ATOM   3758 H HE1  A PHE   A 1 168 ? 11.688 -16.087 1.604   0.60 20.07 ?  168 PHE   A HE1  1 
ATOM   3759 H HE1  B PHE   A 1 168 ? 9.938  -17.824 4.452   0.40 27.24 ?  168 PHE   A HE1  1 
ATOM   3760 H HE2  A PHE   A 1 168 ? 9.683  -18.608 3.972   0.60 19.79 ?  168 PHE   A HE2  1 
ATOM   3761 H HE2  B PHE   A 1 168 ? 11.737 -17.334 0.909   0.40 27.45 ?  168 PHE   A HE2  1 
ATOM   3762 H HZ   A PHE   A 1 168 ? 11.668 -17.915 3.005   0.60 20.05 ?  168 PHE   A HZ   1 
ATOM   3763 H HZ   B PHE   A 1 168 ? 11.698 -18.277 3.021   0.40 27.39 ?  168 PHE   A HZ   1 
ATOM   3764 N N    A LEU   A 1 169 ? 7.269  -17.802 -0.268  0.60 19.86 ?  169 LEU   A N    1 
ATOM   3765 N N    B LEU   A 1 169 ? 5.430  -16.691 2.756   0.40 27.09 ?  169 LEU   A N    1 
ATOM   3766 C CA   A LEU   A 1 169 ? 7.078  -19.228 -0.432  0.60 22.50 ?  169 LEU   A CA   1 
ATOM   3767 C CA   B LEU   A 1 169 ? 4.976  -17.708 3.702   0.40 28.20 ?  169 LEU   A CA   1 
ATOM   3768 C C    A LEU   A 1 169 ? 7.958  -19.966 0.561   0.60 22.90 ?  169 LEU   A C    1 
ATOM   3769 C C    B LEU   A 1 169 ? 4.118  -18.776 3.029   0.40 29.16 ?  169 LEU   A C    1 
ATOM   3770 O O    A LEU   A 1 169 ? 7.471  -20.419 1.599   0.60 22.85 ?  169 LEU   A O    1 
ATOM   3771 O O    B LEU   A 1 169 ? 4.187  -19.952 3.391   0.40 29.66 ?  169 LEU   A O    1 
ATOM   3772 C CB   A LEU   A 1 169 ? 7.397  -19.655 -1.866  0.60 24.27 ?  169 LEU   A CB   1 
ATOM   3773 C CB   B LEU   A 1 169 ? 4.198  -17.069 4.858   0.40 28.33 ?  169 LEU   A CB   1 
ATOM   3774 C CG   A LEU   A 1 169 ? 7.063  -21.107 -2.219  0.60 25.80 ?  169 LEU   A CG   1 
ATOM   3775 C CG   B LEU   A 1 169 ? 4.972  -16.361 5.973   0.40 28.46 ?  169 LEU   A CG   1 
ATOM   3776 C CD1  A LEU   A 1 169 ? 5.630  -21.439 -1.832  0.60 26.40 ?  169 LEU   A CD1  1 
ATOM   3777 C CD1  B LEU   A 1 169 ? 4.016  -16.004 7.102   0.40 28.70 ?  169 LEU   A CD1  1 
ATOM   3778 C CD2  A LEU   A 1 169 ? 7.286  -21.367 -3.701  0.60 26.24 ?  169 LEU   A CD2  1 
ATOM   3779 C CD2  B LEU   A 1 169 ? 6.113  -17.220 6.495   0.40 28.41 ?  169 LEU   A CD2  1 
ATOM   3780 O OXT  A LEU   A 1 169 ? 9.163  -20.103 0.355   0.60 23.17 -1 169 LEU   A OXT  1 
ATOM   3781 O OXT  B LEU   A 1 169 ? 3.343  -18.498 2.113   0.40 29.58 -1 169 LEU   A OXT  1 
ATOM   3782 H H    A LEU   A 1 169 ? 7.965  -17.491 -0.668  0.60 23.80 ?  169 LEU   A H    1 
ATOM   3783 H H    B LEU   A 1 169 ? 5.185  -15.891 2.953   0.40 32.48 ?  169 LEU   A H    1 
ATOM   3784 H HA   A LEU   A 1 169 ? 6.156  -19.449 -0.239  0.60 26.97 ?  169 LEU   A HA   1 
ATOM   3785 H HA   B LEU   A 1 169 ? 5.747  -18.156 4.070   0.40 33.82 ?  169 LEU   A HA   1 
ATOM   3786 H HB2  A LEU   A 1 169 ? 6.891  -19.090 -2.470  0.60 29.10 ?  169 LEU   A HB2  1 
ATOM   3787 H HB2  B LEU   A 1 169 ? 3.596  -16.409 4.483   0.40 33.97 ?  169 LEU   A HB2  1 
ATOM   3788 H HB3  A LEU   A 1 169 ? 8.344  -19.532 -2.022  0.60 29.10 ?  169 LEU   A HB3  1 
ATOM   3789 H HB3  B LEU   A 1 169 ? 3.678  -17.764 5.285   0.40 33.97 ?  169 LEU   A HB3  1 
ATOM   3790 H HG   A LEU   A 1 169 ? 7.650  -21.698 -1.723  0.60 30.93 ?  169 LEU   A HG   1 
ATOM   3791 H HG   B LEU   A 1 169 ? 5.349  -15.535 5.629   0.40 34.13 ?  169 LEU   A HG   1 
ATOM   3792 H HD11 A LEU   A 1 169 ? 5.367  -22.265 -2.265  0.60 31.65 ?  169 LEU   A HD11 1 
ATOM   3793 H HD11 B LEU   A 1 169 ? 4.507  -15.547 7.801   0.40 34.42 ?  169 LEU   A HD11 1 
ATOM   3794 H HD12 A LEU   A 1 169 ? 5.578  -21.541 -0.868  0.60 31.65 ?  169 LEU   A HD12 1 
ATOM   3795 H HD12 B LEU   A 1 169 ? 3.318  -15.427 6.754   0.40 34.42 ?  169 LEU   A HD12 1 
ATOM   3796 H HD13 A LEU   A 1 169 ? 5.049  -20.716 -2.121  0.60 31.65 ?  169 LEU   A HD13 1 
ATOM   3797 H HD13 B LEU   A 1 169 ? 3.624  -16.821 7.452   0.40 34.42 ?  169 LEU   A HD13 1 
ATOM   3798 H HD21 A LEU   A 1 169 ? 7.075  -22.295 -3.895  0.60 31.47 ?  169 LEU   A HD21 1 
ATOM   3799 H HD21 B LEU   A 1 169 ? 6.449  -16.834 7.318   0.40 34.07 ?  169 LEU   A HD21 1 
ATOM   3800 H HD22 A LEU   A 1 169 ? 6.706  -20.783 -4.215  0.60 31.47 ?  169 LEU   A HD22 1 
ATOM   3801 H HD22 B LEU   A 1 169 ? 5.780  -18.116 6.662   0.40 34.07 ?  169 LEU   A HD22 1 
ATOM   3802 H HD23 A LEU   A 1 169 ? 8.213  -21.187 -3.917  0.60 31.47 ?  169 LEU   A HD23 1 
ATOM   3803 H HD23 B LEU   A 1 169 ? 6.817  -17.247 5.829   0.40 34.07 ?  169 LEU   A HD23 1 
ATOM   3804 N N    A SER   B 1 1   ? 50.701 -9.158  -23.680 0.60 30.09 ?  1   SER   B N    1 
ATOM   3805 N N    B SER   B 1 1   ? 50.764 -9.284  -23.768 0.40 28.28 ?  1   SER   B N    1 
ATOM   3806 C CA   A SER   B 1 1   ? 51.222 -10.250 -22.835 0.60 29.48 ?  1   SER   B CA   1 
ATOM   3807 C CA   B SER   B 1 1   ? 51.201 -10.285 -22.771 0.40 28.08 ?  1   SER   B CA   1 
ATOM   3808 C C    A SER   B 1 1   ? 50.153 -11.301 -22.580 0.60 27.49 ?  1   SER   B C    1 
ATOM   3809 C C    B SER   B 1 1   ? 50.112 -11.322 -22.531 0.40 27.24 ?  1   SER   B C    1 
ATOM   3810 O O    A SER   B 1 1   ? 48.957 -11.090 -22.826 0.60 26.85 ?  1   SER   B O    1 
ATOM   3811 O O    B SER   B 1 1   ? 48.950 -11.138 -22.910 0.40 26.54 ?  1   SER   B O    1 
ATOM   3812 C CB   A SER   B 1 1   ? 51.734 -9.709  -21.503 0.60 30.51 ?  1   SER   B CB   1 
ATOM   3813 C CB   B SER   B 1 1   ? 51.560 -9.609  -21.452 0.40 28.57 ?  1   SER   B CB   1 
ATOM   3814 O OG   A SER   B 1 1   ? 50.659 -9.339  -20.662 0.60 32.08 ?  1   SER   B OG   1 
ATOM   3815 O OG   B SER   B 1 1   ? 50.418 -9.497  -20.621 0.40 29.41 ?  1   SER   B OG   1 
ATOM   3816 H H1   A SER   B 1 1   ? 50.429 -9.496  -24.454 0.60 36.08 ?  1   SER   B H1   1 
ATOM   3817 H H1   B SER   B 1 1   ? 51.481 -8.877  -24.101 0.40 33.91 ?  1   SER   B H1   1 
ATOM   3818 H H2   A SER   B 1 1   ? 50.025 -8.768  -23.263 0.60 36.08 ?  1   SER   B H2   1 
ATOM   3819 H H2   B SER   B 1 1   ? 50.322 -9.695  -24.418 0.40 33.91 ?  1   SER   B H2   1 
ATOM   3820 H H3   A SER   B 1 1   ? 51.352 -8.571  -23.820 0.60 36.08 ?  1   SER   B H3   1 
ATOM   3821 H H3   B SER   B 1 1   ? 50.239 -8.691  -23.370 0.40 33.91 ?  1   SER   B H3   1 
ATOM   3822 H HA   A SER   B 1 1   ? 51.960 -10.666 -23.301 0.60 35.35 ?  1   SER   B HA   1 
ATOM   3823 H HA   B SER   B 1 1   ? 51.988 -10.729 -23.115 0.40 33.67 ?  1   SER   B HA   1 
ATOM   3824 H HB2  A SER   B 1 1   ? 52.254 -10.402 -21.069 0.60 36.59 ?  1   SER   B HB2  1 
ATOM   3825 H HB2  B SER   B 1 1   ? 52.231 -10.146 -21.006 0.40 34.26 ?  1   SER   B HB2  1 
ATOM   3826 H HB3  A SER   B 1 1   ? 52.286 -8.931  -21.668 0.60 36.59 ?  1   SER   B HB3  1 
ATOM   3827 H HB3  B SER   B 1 1   ? 51.907 -8.722  -21.633 0.40 34.26 ?  1   SER   B HB3  1 
ATOM   3828 H HG   A SER   B 1 1   ? 50.932 -8.811  -20.068 0.60 38.47 ?  1   SER   B HG   1 
ATOM   3829 H HG   B SER   B 1 1   ? 50.558 -8.919  -20.028 0.40 35.27 ?  1   SER   B HG   1 
ATOM   3830 N N    A MET   B 1 2   ? 50.609 -12.434 -22.065 0.60 26.44 ?  2   MET   B N    1 
ATOM   3831 N N    B MET   B 1 2   ? 50.503 -12.408 -21.874 0.40 27.19 ?  2   MET   B N    1 
ATOM   3832 C CA   A MET   B 1 2   ? 49.790 -13.625 -21.887 0.60 26.33 ?  2   MET   B CA   1 
ATOM   3833 C CA   B MET   B 1 2   ? 49.680 -13.606 -21.731 0.40 27.20 ?  2   MET   B CA   1 
ATOM   3834 C C    A MET   B 1 2   ? 49.565 -13.823 -20.395 0.60 23.60 ?  2   MET   B C    1 
ATOM   3835 C C    B MET   B 1 2   ? 49.408 -13.852 -20.250 0.40 25.22 ?  2   MET   B C    1 
ATOM   3836 O O    A MET   B 1 2   ? 50.517 -14.061 -19.645 0.60 23.24 ?  2   MET   B O    1 
ATOM   3837 O O    B MET   B 1 2   ? 50.260 -14.390 -19.536 0.40 25.70 ?  2   MET   B O    1 
ATOM   3838 C CB   A MET   B 1 2   ? 50.513 -14.821 -22.494 0.60 30.14 ?  2   MET   B CB   1 
ATOM   3839 C CB   B MET   B 1 2   ? 50.414 -14.785 -22.351 0.40 29.67 ?  2   MET   B CB   1 
ATOM   3840 C CG   A MET   B 1 2   ? 49.666 -16.070 -22.653 0.60 33.57 ?  2   MET   B CG   1 
ATOM   3841 C CG   B MET   B 1 2   ? 49.542 -15.967 -22.728 0.40 31.88 ?  2   MET   B CG   1 
ATOM   3842 S SD   A MET   B 1 2   ? 50.523 -17.317 -23.634 0.60 36.75 ?  2   MET   B SD   1 
ATOM   3843 S SD   B MET   B 1 2   ? 50.428 -17.143 -23.765 0.40 33.91 ?  2   MET   B SD   1 
ATOM   3844 C CE   A MET   B 1 2   ? 51.050 -16.308 -25.014 0.60 36.92 ?  2   MET   B CE   1 
ATOM   3845 C CE   B MET   B 1 2   ? 51.258 -16.019 -24.878 0.40 34.05 ?  2   MET   B CE   1 
ATOM   3846 H H    A MET   B 1 2   ? 51.419 -12.543 -21.801 0.60 31.70 ?  2   MET   B H    1 
ATOM   3847 H H    B MET   B 1 2   ? 51.274 -12.478 -21.503 0.40 32.61 ?  2   MET   B H    1 
ATOM   3848 H HA   A MET   B 1 2   ? 48.940 -13.520 -22.340 0.60 31.57 ?  2   MET   B HA   1 
ATOM   3849 H HA   B MET   B 1 2   ? 48.844 -13.486 -22.206 0.40 32.62 ?  2   MET   B HA   1 
ATOM   3850 H HB2  A MET   B 1 2   ? 50.828 -14.544 -23.364 0.60 36.14 ?  2   MET   B HB2  1 
ATOM   3851 H HB2  B MET   B 1 2   ? 50.851 -14.445 -23.141 0.40 35.59 ?  2   MET   B HB2  1 
ATOM   3852 H HB3  A MET   B 1 2   ? 51.266 -15.060 -21.935 0.60 36.14 ?  2   MET   B HB3  1 
ATOM   3853 H HB3  B MET   B 1 2   ? 51.080 -15.115 -21.731 0.40 35.59 ?  2   MET   B HB3  1 
ATOM   3854 H HG2  A MET   B 1 2   ? 49.481 -16.442 -21.774 0.60 40.26 ?  2   MET   B HG2  1 
ATOM   3855 H HG2  B MET   B 1 2   ? 49.263 -16.422 -21.916 0.40 38.24 ?  2   MET   B HG2  1 
ATOM   3856 H HG3  A MET   B 1 2   ? 48.839 -15.848 -23.107 0.60 40.26 ?  2   MET   B HG3  1 
ATOM   3857 H HG3  B MET   B 1 2   ? 48.769 -15.664 -23.223 0.40 38.24 ?  2   MET   B HG3  1 
ATOM   3858 H HE1  A MET   B 1 2   ? 51.210 -16.879 -25.770 0.60 44.28 ?  2   MET   B HE1  1 
ATOM   3859 H HE1  B MET   B 1 2   ? 51.510 -16.503 -25.665 0.40 40.83 ?  2   MET   B HE1  1 
ATOM   3860 H HE2  A MET   B 1 2   ? 50.344 -15.670 -25.217 0.60 44.28 ?  2   MET   B HE2  1 
ATOM   3861 H HE2  B MET   B 1 2   ? 50.644 -15.299 -25.107 0.40 40.83 ?  2   MET   B HE2  1 
ATOM   3862 H HE3  A MET   B 1 2   ? 51.864 -15.829 -24.775 0.60 44.28 ?  2   MET   B HE3  1 
ATOM   3863 H HE3  B MET   B 1 2   ? 52.047 -15.653 -24.439 0.40 40.83 ?  2   MET   B HE3  1 
ATOM   3864 N N    A VAL   B 1 3   ? 48.312 -13.693 -19.966 0.60 21.60 ?  3   VAL   B N    1 
ATOM   3865 N N    B VAL   B 1 3   ? 48.218 -13.469 -19.795 0.40 22.94 ?  3   VAL   B N    1 
ATOM   3866 C CA   A VAL   B 1 3   ? 47.913 -13.935 -18.588 0.60 20.42 ?  3   VAL   B CA   1 
ATOM   3867 C CA   B VAL   B 1 3   ? 47.783 -13.721 -18.426 0.40 21.07 ?  3   VAL   B CA   1 
ATOM   3868 C C    A VAL   B 1 3   ? 46.676 -14.822 -18.602 0.60 18.37 ?  3   VAL   B C    1 
ATOM   3869 C C    B VAL   B 1 3   ? 46.533 -14.588 -18.462 0.40 18.80 ?  3   VAL   B C    1 
ATOM   3870 O O    A VAL   B 1 3   ? 45.972 -14.930 -19.608 0.60 18.53 ?  3   VAL   B O    1 
ATOM   3871 O O    B VAL   B 1 3   ? 45.700 -14.479 -19.367 0.40 18.65 ?  3   VAL   B O    1 
ATOM   3872 C CB   A VAL   B 1 3   ? 47.635 -12.624 -17.817 0.60 21.96 ?  3   VAL   B CB   1 
ATOM   3873 C CB   B VAL   B 1 3   ? 47.536 -12.427 -17.616 0.40 21.66 ?  3   VAL   B CB   1 
ATOM   3874 C CG1  A VAL   B 1 3   ? 48.900 -11.772 -17.735 0.60 22.40 ?  3   VAL   B CG1  1 
ATOM   3875 C CG1  B VAL   B 1 3   ? 48.818 -11.610 -17.506 0.40 21.92 ?  3   VAL   B CG1  1 
ATOM   3876 C CG2  A VAL   B 1 3   ? 46.496 -11.851 -18.471 0.60 22.63 ?  3   VAL   B CG2  1 
ATOM   3877 C CG2  B VAL   B 1 3   ? 46.413 -11.606 -18.232 0.40 21.81 ?  3   VAL   B CG2  1 
ATOM   3878 H H    A VAL   B 1 3   ? 47.657 -13.467 -20.475 0.60 25.89 ?  3   VAL   B H    1 
ATOM   3879 H H    B VAL   B 1 3   ? 47.630 -13.067 -20.277 0.40 27.50 ?  3   VAL   B H    1 
ATOM   3880 H HA   A VAL   B 1 3   ? 48.624 -14.410 -18.127 0.60 24.48 ?  3   VAL   B HA   1 
ATOM   3881 H HA   B VAL   B 1 3   ? 48.472 -14.222 -17.969 0.40 25.26 ?  3   VAL   B HA   1 
ATOM   3882 H HB   A VAL   B 1 3   ? 47.368 -12.844 -16.911 0.60 26.33 ?  3   VAL   B HB   1 
ATOM   3883 H HB   B VAL   B 1 3   ? 47.268 -12.670 -16.717 0.40 25.97 ?  3   VAL   B HB   1 
ATOM   3884 H HG11 A VAL   B 1 3   ? 48.704 -10.963 -17.237 0.60 26.85 ?  3   VAL   B HG11 1 
ATOM   3885 H HG11 B VAL   B 1 3   ? 48.640 -10.813 -16.980 0.40 26.28 ?  3   VAL   B HG11 1 
ATOM   3886 H HG12 A VAL   B 1 3   ? 49.594 -12.278 -17.284 0.60 26.85 ?  3   VAL   B HG12 1 
ATOM   3887 H HG12 B VAL   B 1 3   ? 49.499 -12.147 -17.071 0.40 26.28 ?  3   VAL   B HG12 1 
ATOM   3888 H HG13 A VAL   B 1 3   ? 49.188 -11.546 -18.634 0.60 26.85 ?  3   VAL   B HG13 1 
ATOM   3889 H HG13 B VAL   B 1 3   ? 49.111 -11.360 -18.396 0.40 26.28 ?  3   VAL   B HG13 1 
ATOM   3890 H HG21 A VAL   B 1 3   ? 46.440 -10.974 -18.065 0.60 27.14 ?  3   VAL   B HG21 1 
ATOM   3891 H HG21 B VAL   B 1 3   ? 46.383 -10.739 -17.800 0.40 26.15 ?  3   VAL   B HG21 1 
ATOM   3892 H HG22 A VAL   B 1 3   ? 46.676 -11.767 -19.419 0.60 27.14 ?  3   VAL   B HG22 1 
ATOM   3893 H HG22 B VAL   B 1 3   ? 46.583 -11.499 -19.180 0.40 26.15 ?  3   VAL   B HG22 1 
ATOM   3894 H HG23 A VAL   B 1 3   ? 45.667 -12.335 -18.332 0.60 27.14 ?  3   VAL   B HG23 1 
ATOM   3895 H HG23 B VAL   B 1 3   ? 45.572 -12.071 -18.097 0.40 26.15 ?  3   VAL   B HG23 1 
ATOM   3896 N N    . ASN   B 1 4   ? 46.412 -15.459 -17.463 1.00 16.94 ?  4   ASN   B N    1 
ATOM   3897 C CA   . ASN   B 1 4   ? 45.283 -16.383 -17.349 1.00 16.10 ?  4   ASN   B CA   1 
ATOM   3898 C C    . ASN   B 1 4   ? 45.233 -17.352 -18.530 1.00 16.49 ?  4   ASN   B C    1 
ATOM   3899 O O    . ASN   B 1 4   ? 44.169 -17.629 -19.084 1.00 17.26 ?  4   ASN   B O    1 
ATOM   3900 C CB   . ASN   B 1 4   ? 43.952 -15.641 -17.183 1.00 15.70 ?  4   ASN   B CB   1 
ATOM   3901 C CG   . ASN   B 1 4   ? 43.907 -14.824 -15.914 1.00 14.55 ?  4   ASN   B CG   1 
ATOM   3902 O OD1  . ASN   B 1 4   ? 44.195 -15.328 -14.834 1.00 14.18 ?  4   ASN   B OD1  1 
ATOM   3903 N ND2  . ASN   B 1 4   ? 43.563 -13.546 -16.039 1.00 15.27 ?  4   ASN   B ND2  1 
ATOM   3904 H H    A ASN   B 1 4   ? 46.869 -15.368 -16.741 0.60 20.31 ?  4   ASN   B H    1 
ATOM   3905 H H    B ASN   B 1 4   ? 46.987 -15.536 -16.830 0.40 20.31 ?  4   ASN   B H    1 
ATOM   3906 H HA   . ASN   B 1 4   ? 45.417 -16.915 -16.549 1.00 19.30 ?  4   ASN   B HA   1 
ATOM   3907 H HB2  . ASN   B 1 4   ? 43.819 -15.045 -17.931 1.00 18.81 ?  4   ASN   B HB2  1 
ATOM   3908 H HB3  . ASN   B 1 4   ? 43.233 -16.295 -17.144 1.00 18.81 ?  4   ASN   B HB3  1 
ATOM   3909 H HD21 . ASN   B 1 4   ? 43.522 -13.036 -15.345 1.00 18.30 ?  4   ASN   B HD21 1 
ATOM   3910 H HD22 . ASN   B 1 4   ? 43.372 -13.225 -16.815 1.00 18.30 ?  4   ASN   B HD22 1 
ATOM   3911 N N    . SER   B 1 5   ? 46.398 -17.869 -18.925 1.00 17.91 ?  5   SER   B N    1 
ATOM   3912 C CA   . SER   B 1 5   ? 46.497 -18.793 -20.056 1.00 20.58 ?  5   SER   B CA   1 
ATOM   3913 C C    . SER   B 1 5   ? 46.494 -20.216 -19.511 1.00 21.87 ?  5   SER   B C    1 
ATOM   3914 O O    . SER   B 1 5   ? 47.517 -20.895 -19.449 1.00 23.71 ?  5   SER   B O    1 
ATOM   3915 C CB   . SER   B 1 5   ? 47.742 -18.505 -20.889 1.00 22.51 ?  5   SER   B CB   1 
ATOM   3916 O OG   . SER   B 1 5   ? 48.931 -18.740 -20.149 1.00 25.42 ?  5   SER   B OG   1 
ATOM   3917 H H    . SER   B 1 5   ? 47.158 -17.692 -18.552 1.00 21.47 ?  5   SER   B H    1 
ATOM   3918 H HA   . SER   B 1 5   ? 45.722 -18.686 -20.624 1.00 24.67 ?  5   SER   B HA   1 
ATOM   3919 H HB2  . SER   B 1 5   ? 47.735 -19.076 -21.674 1.00 26.98 ?  5   SER   B HB2  1 
ATOM   3920 H HB3  . SER   B 1 5   ? 47.709 -17.575 -21.160 1.00 26.98 ?  5   SER   B HB3  1 
ATOM   3921 H HG   . SER   B 1 5   ? 48.980 -19.552 -19.941 1.00 30.48 ?  5   SER   B HG   1 
ATOM   3922 N N    . PHE   B 1 6   ? 45.312 -20.663 -19.107 1.00 21.66 ?  6   PHE   B N    1 
ATOM   3923 C CA   . PHE   B 1 6   ? 45.148 -22.011 -18.588 1.00 20.83 ?  6   PHE   B CA   1 
ATOM   3924 C C    . PHE   B 1 6   ? 45.093 -22.993 -19.747 1.00 23.99 ?  6   PHE   B C    1 
ATOM   3925 O O    . PHE   B 1 6   ? 44.438 -22.738 -20.761 1.00 26.12 ?  6   PHE   B O    1 
ATOM   3926 C CB   . PHE   B 1 6   ? 43.863 -22.095 -17.768 1.00 18.54 ?  6   PHE   B CB   1 
ATOM   3927 C CG   . PHE   B 1 6   ? 43.862 -21.216 -16.547 1.00 16.84 ?  6   PHE   B CG   1 
ATOM   3928 C CD1  . PHE   B 1 6   ? 44.376 -21.678 -15.352 1.00 15.76 ?  6   PHE   B CD1  1 
ATOM   3929 C CD2  . PHE   B 1 6   ? 43.355 -19.925 -16.598 1.00 16.39 ?  6   PHE   B CD2  1 
ATOM   3930 C CE1  . PHE   B 1 6   ? 44.369 -20.876 -14.218 1.00 15.50 ?  6   PHE   B CE1  1 
ATOM   3931 C CE2  . PHE   B 1 6   ? 43.357 -19.115 -15.477 1.00 16.40 ?  6   PHE   B CE2  1 
ATOM   3932 C CZ   . PHE   B 1 6   ? 43.864 -19.587 -14.287 1.00 15.77 ?  6   PHE   B CZ   1 
ATOM   3933 H H    . PHE   B 1 6   ? 44.585 -20.205 -19.133 1.00 25.97 ?  6   PHE   B H    1 
ATOM   3934 H HA   . PHE   B 1 6   ? 45.897 -22.241 -18.021 1.00 24.97 ?  6   PHE   B HA   1 
ATOM   3935 H HB2  . PHE   B 1 6   ? 43.115 -21.827 -18.325 1.00 22.22 ?  6   PHE   B HB2  1 
ATOM   3936 H HB3  . PHE   B 1 6   ? 43.739 -23.011 -17.472 1.00 22.22 ?  6   PHE   B HB3  1 
ATOM   3937 H HD1  . PHE   B 1 6   ? 44.721 -22.541 -15.300 1.00 18.89 ?  6   PHE   B HD1  1 
ATOM   3938 H HD2  . PHE   B 1 6   ? 43.007 -19.601 -17.397 1.00 19.64 ?  6   PHE   B HD2  1 
ATOM   3939 H HE1  . PHE   B 1 6   ? 44.725 -21.194 -13.418 1.00 18.58 ?  6   PHE   B HE1  1 
ATOM   3940 H HE2  . PHE   B 1 6   ? 43.008 -18.252 -15.524 1.00 19.65 ?  6   PHE   B HE2  1 
ATOM   3941 H HZ   . PHE   B 1 6   ? 43.865 -19.045 -13.531 1.00 18.90 ?  6   PHE   B HZ   1 
ATOM   3942 N N    A SER   B 1 7   ? 45.788 -24.119 -19.597 0.60 24.15 ?  7   SER   B N    1 
ATOM   3943 N N    B SER   B 1 7   ? 45.800 -24.112 -19.596 0.40 24.43 ?  7   SER   B N    1 
ATOM   3944 C CA   A SER   B 1 7   ? 45.861 -25.118 -20.654 0.60 25.72 ?  7   SER   B CA   1 
ATOM   3945 C CA   B SER   B 1 7   ? 45.926 -25.107 -20.651 0.40 25.63 ?  7   SER   B CA   1 
ATOM   3946 C C    A SER   B 1 7   ? 45.844 -26.516 -20.054 0.60 25.17 ?  7   SER   B C    1 
ATOM   3947 C C    B SER   B 1 7   ? 45.885 -26.503 -20.049 0.40 25.19 ?  7   SER   B C    1 
ATOM   3948 O O    A SER   B 1 7   ? 46.424 -26.757 -18.992 0.60 25.81 ?  7   SER   B O    1 
ATOM   3949 O O    B SER   B 1 7   ? 46.470 -26.751 -18.990 0.40 25.63 ?  7   SER   B O    1 
ATOM   3950 C CB   A SER   B 1 7   ? 47.127 -24.930 -21.501 0.60 27.79 ?  7   SER   B CB   1 
ATOM   3951 C CB   B SER   B 1 7   ? 47.242 -24.923 -21.419 0.40 27.19 ?  7   SER   B CB   1 
ATOM   3952 O OG   A SER   B 1 7   ? 47.091 -25.744 -22.658 0.60 29.67 ?  7   SER   B OG   1 
ATOM   3953 O OG   B SER   B 1 7   ? 47.396 -25.915 -22.419 0.40 28.52 ?  7   SER   B OG   1 
ATOM   3954 H H    A SER   B 1 7   ? 46.232 -24.324 -18.888 0.60 28.96 ?  7   SER   B H    1 
ATOM   3955 H H    B SER   B 1 7   ? 46.227 -24.316 -18.877 0.40 29.30 ?  7   SER   B H    1 
ATOM   3956 H HA   A SER   B 1 7   ? 45.091 -25.030 -21.234 0.60 30.84 ?  7   SER   B HA   1 
ATOM   3957 H HA   B SER   B 1 7   ? 45.189 -25.018 -21.274 0.40 30.73 ?  7   SER   B HA   1 
ATOM   3958 H HB2  A SER   B 1 7   ? 47.186 -24.001 -21.776 0.60 33.33 ?  7   SER   B HB2  1 
ATOM   3959 H HB2  B SER   B 1 7   ? 47.241 -24.048 -21.839 0.40 32.60 ?  7   SER   B HB2  1 
ATOM   3960 H HB3  A SER   B 1 7   ? 47.902 -25.166 -20.968 0.60 33.33 ?  7   SER   B HB3  1 
ATOM   3961 H HB3  B SER   B 1 7   ? 47.983 -24.991 -20.797 0.40 32.60 ?  7   SER   B HB3  1 
ATOM   3962 H HG   A SER   B 1 7   ? 47.792 -25.636 -23.110 0.60 35.58 ?  7   SER   B HG   1 
ATOM   3963 H HG   B SER   B 1 7   ? 48.117 -25.797 -22.833 0.40 34.20 ?  7   SER   B HG   1 
ATOM   3964 N N    A GLY   B 1 8   ? 45.170 -27.435 -20.744 0.60 24.68 ?  8   GLY   B N    1 
ATOM   3965 N N    B GLY   B 1 8   ? 45.189 -27.410 -20.730 0.40 24.67 ?  8   GLY   B N    1 
ATOM   3966 C CA   A GLY   B 1 8   ? 45.139 -28.824 -20.339 0.60 24.19 ?  8   GLY   B CA   1 
ATOM   3967 C CA   B GLY   B 1 8   ? 45.158 -28.798 -20.316 0.40 24.03 ?  8   GLY   B CA   1 
ATOM   3968 C C    A GLY   B 1 8   ? 44.137 -29.163 -19.261 0.60 23.17 ?  8   GLY   B C    1 
ATOM   3969 C C    B GLY   B 1 8   ? 44.197 -29.116 -19.197 0.40 22.96 ?  8   GLY   B C    1 
ATOM   3970 O O    A GLY   B 1 8   ? 44.208 -30.264 -18.699 0.60 24.16 ?  8   GLY   B O    1 
ATOM   3971 O O    B GLY   B 1 8   ? 44.356 -30.149 -18.537 0.40 23.44 ?  8   GLY   B O    1 
ATOM   3972 H H    A GLY   B 1 8   ? 44.722 -27.269 -21.458 0.60 29.59 ?  8   GLY   B H    1 
ATOM   3973 H H    B GLY   B 1 8   ? 44.729 -27.242 -21.436 0.40 29.59 ?  8   GLY   B H    1 
ATOM   3974 H HA2  A GLY   B 1 8   ? 44.933 -29.372 -21.113 0.60 29.00 ?  8   GLY   B HA2  1 
ATOM   3975 H HA2  B GLY   B 1 8   ? 44.919 -29.347 -21.078 0.40 28.81 ?  8   GLY   B HA2  1 
ATOM   3976 H HA3  A GLY   B 1 8   ? 46.017 -29.079 -20.017 0.60 29.00 ?  8   GLY   B HA3  1 
ATOM   3977 H HA3  B GLY   B 1 8   ? 46.045 -29.059 -20.025 0.40 28.81 ?  8   GLY   B HA3  1 
ATOM   3978 N N    . TYR   B 1 9   ? 43.199 -28.269 -18.958 1.00 21.81 ?  9   TYR   B N    1 
ATOM   3979 C CA   . TYR   B 1 9   ? 42.217 -28.529 -17.918 1.00 19.32 ?  9   TYR   B CA   1 
ATOM   3980 C C    . TYR   B 1 9   ? 41.033 -29.309 -18.461 1.00 18.93 ?  9   TYR   B C    1 
ATOM   3981 O O    . TYR   B 1 9   ? 40.631 -29.156 -19.618 1.00 20.92 ?  9   TYR   B O    1 
ATOM   3982 C CB   . TYR   B 1 9   ? 41.707 -27.235 -17.291 1.00 18.66 ?  9   TYR   B CB   1 
ATOM   3983 C CG   . TYR   B 1 9   ? 42.717 -26.616 -16.362 1.00 18.22 ?  9   TYR   B CG   1 
ATOM   3984 C CD1  . TYR   B 1 9   ? 43.836 -25.969 -16.864 1.00 18.94 ?  9   TYR   B CD1  1 
ATOM   3985 C CD2  . TYR   B 1 9   ? 42.567 -26.698 -14.988 1.00 17.34 ?  9   TYR   B CD2  1 
ATOM   3986 C CE1  . TYR   B 1 9   ? 44.777 -25.423 -16.024 1.00 19.16 ?  9   TYR   B CE1  1 
ATOM   3987 C CE2  . TYR   B 1 9   ? 43.503 -26.149 -14.137 1.00 17.92 ?  9   TYR   B CE2  1 
ATOM   3988 C CZ   . TYR   B 1 9   ? 44.607 -25.507 -14.663 1.00 18.91 ?  9   TYR   B CZ   1 
ATOM   3989 O OH   . TYR   B 1 9   ? 45.549 -24.962 -13.828 1.00 19.46 ?  9   TYR   B OH   1 
ATOM   3990 H H    A TYR   B 1 9   ? 43.105 -27.510 -19.350 0.60 26.14 ?  9   TYR   B H    1 
ATOM   3991 H H    B TYR   B 1 9   ? 43.065 -27.540 -19.393 0.40 26.14 ?  9   TYR   B H    1 
ATOM   3992 H HA   . TYR   B 1 9   ? 42.626 -29.057 -17.218 1.00 23.16 ?  9   TYR   B HA   1 
ATOM   3993 H HB2  . TYR   B 1 9   ? 41.503 -26.592 -17.989 1.00 22.37 ?  9   TYR   B HB2  1 
ATOM   3994 H HB3  . TYR   B 1 9   ? 40.914 -27.436 -16.777 1.00 22.37 ?  9   TYR   B HB3  1 
ATOM   3995 H HD1  . TYR   B 1 9   ? 43.955 -25.914 -17.784 1.00 22.70 ?  9   TYR   B HD1  1 
ATOM   3996 H HD2  . TYR   B 1 9   ? 41.820 -27.133 -14.633 1.00 20.79 ?  9   TYR   B HD2  1 
ATOM   3997 H HE1  . TYR   B 1 9   ? 45.519 -24.993 -16.376 1.00 22.96 ?  9   TYR   B HE1  1 
ATOM   3998 H HE2  . TYR   B 1 9   ? 43.384 -26.211 -13.214 1.00 21.48 ?  9   TYR   B HE2  1 
ATOM   3999 H HH   . TYR   B 1 9   ? 46.159 -24.612 -14.282 1.00 23.33 ?  9   TYR   B HH   1 
ATOM   4000 N N    . LEU   B 1 10  ? 40.478 -30.147 -17.598 1.00 17.05 ?  10  LEU   B N    1 
ATOM   4001 C CA   . LEU   B 1 10  ? 39.275 -30.908 -17.879 1.00 16.96 ?  10  LEU   B CA   1 
ATOM   4002 C C    . LEU   B 1 10  ? 38.085 -30.139 -17.323 1.00 16.11 ?  10  LEU   B C    1 
ATOM   4003 O O    . LEU   B 1 10  ? 38.090 -29.732 -16.158 1.00 16.06 ?  10  LEU   B O    1 
ATOM   4004 C CB   . LEU   B 1 10  ? 39.375 -32.274 -17.205 1.00 18.01 ?  10  LEU   B CB   1 
ATOM   4005 C CG   . LEU   B 1 10  ? 38.227 -33.216 -17.540 1.00 19.22 ?  10  LEU   B CG   1 
ATOM   4006 C CD1  . LEU   B 1 10  ? 38.367 -33.722 -18.968 1.00 20.52 ?  10  LEU   B CD1  1 
ATOM   4007 C CD2  . LEU   B 1 10  ? 38.173 -34.363 -16.551 1.00 20.24 ?  10  LEU   B CD2  1 
ATOM   4008 H H    . LEU   B 1 10  ? 40.791 -30.291 -16.806 1.00 20.44 ?  10  LEU   B H    1 
ATOM   4009 H HA   . LEU   B 1 10  ? 39.165 -31.026 -18.831 1.00 20.33 ?  10  LEU   B HA   1 
ATOM   4010 H HB2  . LEU   B 1 10  ? 40.202 -32.704 -17.487 1.00 21.59 ?  10  LEU   B HB2  1 
ATOM   4011 H HB3  . LEU   B 1 10  ? 39.387 -32.152 -16.241 1.00 21.59 ?  10  LEU   B HB3  1 
ATOM   4012 H HG   . LEU   B 1 10  ? 37.392 -32.727 -17.477 1.00 23.04 ?  10  LEU   B HG   1 
ATOM   4013 H HD11 . LEU   B 1 10  ? 37.671 -34.373 -19.136 1.00 24.60 ?  10  LEU   B HD11 1 
ATOM   4014 H HD12 . LEU   B 1 10  ? 38.275 -32.972 -19.578 1.00 24.60 ?  10  LEU   B HD12 1 
ATOM   4015 H HD13 . LEU   B 1 10  ? 39.239 -34.130 -19.072 1.00 24.60 ?  10  LEU   B HD13 1 
ATOM   4016 H HD21 . LEU   B 1 10  ? 37.438 -34.945 -16.792 1.00 24.26 ?  10  LEU   B HD21 1 
ATOM   4017 H HD22 . LEU   B 1 10  ? 39.010 -34.845 -16.585 1.00 24.26 ?  10  LEU   B HD22 1 
ATOM   4018 H HD23 . LEU   B 1 10  ? 38.032 -34.000 -15.662 1.00 24.26 ?  10  LEU   B HD23 1 
ATOM   4019 N N    . LYS   B 1 11  ? 37.070 -29.948 -18.152 1.00 17.31 ?  11  LYS   B N    1 
ATOM   4020 C CA   . LYS   B 1 11  ? 35.874 -29.229 -17.738 1.00 19.01 ?  11  LYS   B CA   1 
ATOM   4021 C C    . LYS   B 1 11  ? 34.979 -30.157 -16.922 1.00 18.50 ?  11  LYS   B C    1 
ATOM   4022 O O    . LYS   B 1 11  ? 34.581 -31.226 -17.400 1.00 20.46 ?  11  LYS   B O    1 
ATOM   4023 C CB   . LYS   B 1 11  ? 35.142 -28.727 -18.981 1.00 22.60 ?  11  LYS   B CB   1 
ATOM   4024 C CG   . LYS   B 1 11  ? 33.949 -27.832 -18.711 1.00 25.99 ?  11  LYS   B CG   1 
ATOM   4025 C CD   . LYS   B 1 11  ? 33.176 -27.566 -20.000 1.00 28.72 ?  11  LYS   B CD   1 
ATOM   4026 C CE   . LYS   B 1 11  ? 32.152 -26.460 -19.826 1.00 30.88 ?  11  LYS   B CE   1 
ATOM   4027 N NZ   . LYS   B 1 11  ? 32.810 -25.146 -19.605 1.00 32.15 ?  11  LYS   B NZ   1 
ATOM   4028 H H    . LYS   B 1 11  ? 37.044 -30.235 -18.960 1.00 20.75 ?  11  LYS   B H    1 
ATOM   4029 H HA   . LYS   B 1 11  ? 36.120 -28.469 -17.188 1.00 22.79 ?  11  LYS   B HA   1 
ATOM   4030 H HB2  . LYS   B 1 11  ? 35.770 -28.221 -19.522 1.00 27.09 ?  11  LYS   B HB2  1 
ATOM   4031 H HB3  . LYS   B 1 11  ? 34.826 -29.493 -19.483 1.00 27.09 ?  11  LYS   B HB3  1 
ATOM   4032 H HG2  . LYS   B 1 11  ? 33.351 -28.267 -18.084 1.00 31.16 ?  11  LYS   B HG2  1 
ATOM   4033 H HG3  . LYS   B 1 11  ? 34.254 -26.983 -18.357 1.00 31.16 ?  11  LYS   B HG3  1 
ATOM   4034 H HD2  . LYS   B 1 11  ? 33.798 -27.297 -20.696 1.00 34.45 ?  11  LYS   B HD2  1 
ATOM   4035 H HD3  . LYS   B 1 11  ? 32.709 -28.375 -20.266 1.00 34.45 ?  11  LYS   B HD3  1 
ATOM   4036 H HE2  . LYS   B 1 11  ? 31.607 -26.399 -20.626 1.00 37.04 ?  11  LYS   B HE2  1 
ATOM   4037 H HE3  . LYS   B 1 11  ? 31.598 -26.659 -19.055 1.00 37.04 ?  11  LYS   B HE3  1 
ATOM   4038 H HZ1  . LYS   B 1 11  ? 32.197 -24.504 -19.551 1.00 38.56 ?  11  LYS   B HZ1  1 
ATOM   4039 H HZ2  . LYS   B 1 11  ? 33.280 -25.163 -18.850 1.00 38.56 ?  11  LYS   B HZ2  1 
ATOM   4040 H HZ3  . LYS   B 1 11  ? 33.359 -24.964 -20.283 1.00 38.56 ?  11  LYS   B HZ3  1 
ATOM   4041 N N    . LEU   B 1 12  ? 34.653 -29.752 -15.695 1.00 17.07 ?  12  LEU   B N    1 
ATOM   4042 C CA   . LEU   B 1 12  ? 33.688 -30.461 -14.861 1.00 16.74 ?  12  LEU   B CA   1 
ATOM   4043 C C    . LEU   B 1 12  ? 32.296 -29.857 -14.956 1.00 16.90 ?  12  LEU   B C    1 
ATOM   4044 O O    . LEU   B 1 12  ? 31.314 -30.576 -15.137 1.00 17.35 ?  12  LEU   B O    1 
ATOM   4045 C CB   . LEU   B 1 12  ? 34.137 -30.475 -13.396 1.00 16.07 ?  12  LEU   B CB   1 
ATOM   4046 C CG   . LEU   B 1 12  ? 35.466 -31.165 -13.103 1.00 16.26 ?  12  LEU   B CG   1 
ATOM   4047 C CD1  . LEU   B 1 12  ? 35.771 -31.118 -11.620 1.00 16.50 ?  12  LEU   B CD1  1 
ATOM   4048 C CD2  . LEU   B 1 12  ? 35.464 -32.601 -13.610 1.00 17.28 ?  12  LEU   B CD2  1 
ATOM   4049 H H    . LEU   B 1 12  ? 34.986 -29.054 -15.318 1.00 20.46 ?  12  LEU   B H    1 
ATOM   4050 H HA   . LEU   B 1 12  ? 33.626 -31.378 -15.168 1.00 20.07 ?  12  LEU   B HA   1 
ATOM   4051 H HB2  . LEU   B 1 12  ? 34.214 -29.559 -13.095 1.00 19.25 ?  12  LEU   B HB2  1 
ATOM   4052 H HB3  . LEU   B 1 12  ? 33.454 -30.930 -12.878 1.00 19.25 ?  12  LEU   B HB3  1 
ATOM   4053 H HG   . LEU   B 1 12  ? 36.171 -30.692 -13.567 1.00 19.48 ?  12  LEU   B HG   1 
ATOM   4054 H HD11 . LEU   B 1 12  ? 36.620 -31.560 -11.457 1.00 19.78 ?  12  LEU   B HD11 1 
ATOM   4055 H HD12 . LEU   B 1 12  ? 35.823 -30.191 -11.338 1.00 19.78 ?  12  LEU   B HD12 1 
ATOM   4056 H HD13 . LEU   B 1 12  ? 35.064 -31.572 -11.134 1.00 19.78 ?  12  LEU   B HD13 1 
ATOM   4057 H HD21 . LEU   B 1 12  ? 36.257 -33.054 -13.284 1.00 20.72 ?  12  LEU   B HD21 1 
ATOM   4058 H HD22 . LEU   B 1 12  ? 34.668 -33.052 -13.285 1.00 20.72 ?  12  LEU   B HD22 1 
ATOM   4059 H HD23 . LEU   B 1 12  ? 35.464 -32.596 -14.582 1.00 20.72 ?  12  LEU   B HD23 1 
ATOM   4060 N N    . THR   B 1 13  ? 32.198 -28.541 -14.824 1.00 16.93 ?  13  THR   B N    1 
ATOM   4061 C CA   . THR   B 1 13  ? 30.964 -27.798 -15.024 1.00 16.81 ?  13  THR   B CA   1 
ATOM   4062 C C    . THR   B 1 13  ? 31.287 -26.589 -15.897 1.00 18.63 ?  13  THR   B C    1 
ATOM   4063 O O    . THR   B 1 13  ? 32.429 -26.385 -16.322 1.00 19.73 ?  13  THR   B O    1 
ATOM   4064 C CB   . THR   B 1 13  ? 30.366 -27.336 -13.690 1.00 17.02 ?  13  THR   B CB   1 
ATOM   4065 O OG1  . THR   B 1 13  ? 31.204 -26.306 -13.147 1.00 16.41 ?  13  THR   B OG1  1 
ATOM   4066 C CG2  . THR   B 1 13  ? 30.268 -28.493 -12.700 1.00 17.61 ?  13  THR   B CG2  1 
ATOM   4067 H H    . THR   B 1 13  ? 32.860 -28.039 -14.607 1.00 20.29 ?  13  THR   B H    1 
ATOM   4068 H HA   . THR   B 1 13  ? 30.315 -28.354 -15.478 1.00 20.15 ?  13  THR   B HA   1 
ATOM   4069 H HB   . THR   B 1 13  ? 29.469 -26.987 -13.839 1.00 20.39 ?  13  THR   B HB   1 
ATOM   4070 H HG1  . THR   B 1 13  ? 30.875 -25.549 -13.327 1.00 19.67 ?  13  THR   B HG1  1 
ATOM   4071 H HG21 . THR   B 1 13  ? 29.719 -28.238 -11.941 1.00 21.11 ?  13  THR   B HG21 1 
ATOM   4072 H HG22 . THR   B 1 13  ? 29.862 -29.264 -13.131 1.00 21.11 ?  13  THR   B HG22 1 
ATOM   4073 H HG23 . THR   B 1 13  ? 31.150 -28.738 -12.385 1.00 21.11 ?  13  THR   B HG23 1 
ATOM   4074 N N    A ASP   B 1 14  ? 30.267 -25.768 -16.152 0.60 19.54 ?  14  ASP   B N    1 
ATOM   4075 N N    B ASP   B 1 14  ? 30.270 -25.763 -16.151 0.40 19.52 ?  14  ASP   B N    1 
ATOM   4076 C CA   A ASP   B 1 14  ? 30.470 -24.598 -16.999 0.60 20.95 ?  14  ASP   B CA   1 
ATOM   4077 C CA   B ASP   B 1 14  ? 30.467 -24.596 -17.005 0.40 20.60 ?  14  ASP   B CA   1 
ATOM   4078 C C    A ASP   B 1 14  ? 31.572 -23.692 -16.463 0.60 19.55 ?  14  ASP   B C    1 
ATOM   4079 C C    B ASP   B 1 14  ? 31.489 -23.617 -16.445 0.40 19.28 ?  14  ASP   B C    1 
ATOM   4080 O O    A ASP   B 1 14  ? 32.236 -22.998 -17.244 0.60 20.72 ?  14  ASP   B O    1 
ATOM   4081 O O    B ASP   B 1 14  ? 31.985 -22.767 -17.194 0.40 20.13 ?  14  ASP   B O    1 
ATOM   4082 C CB   A ASP   B 1 14  ? 29.161 -23.823 -17.154 0.60 23.93 ?  14  ASP   B CB   1 
ATOM   4083 C CB   B ASP   B 1 14  ? 29.145 -23.864 -17.233 0.40 23.08 ?  14  ASP   B CB   1 
ATOM   4084 C CG   A ASP   B 1 14  ? 28.206 -24.469 -18.140 0.60 26.93 ?  14  ASP   B CG   1 
ATOM   4085 C CG   B ASP   B 1 14  ? 28.277 -24.539 -18.277 0.40 25.47 ?  14  ASP   B CG   1 
ATOM   4086 O OD1  A ASP   B 1 14  ? 28.572 -25.486 -18.772 0.60 28.06 ?  14  ASP   B OD1  1 
ATOM   4087 O OD1  B ASP   B 1 14  ? 28.838 -25.153 -19.210 0.40 26.33 ?  14  ASP   B OD1  1 
ATOM   4088 O OD2  A ASP   B 1 14  ? 27.081 -23.949 -18.281 0.60 28.31 -1 14  ASP   B OD2  1 
ATOM   4089 O OD2  B ASP   B 1 14  ? 27.036 -24.457 -18.171 0.40 26.52 -1 14  ASP   B OD2  1 
ATOM   4090 H H    A ASP   B 1 14  ? 29.469 -25.861 -15.844 0.60 23.43 ?  14  ASP   B H    1 
ATOM   4091 H H    B ASP   B 1 14  ? 29.471 -25.856 -15.844 0.40 23.40 ?  14  ASP   B H    1 
ATOM   4092 H HA   A ASP   B 1 14  ? 30.745 -24.892 -17.877 0.60 25.12 ?  14  ASP   B HA   1 
ATOM   4093 H HA   B ASP   B 1 14  ? 30.789 -24.900 -17.866 0.40 24.69 ?  14  ASP   B HA   1 
ATOM   4094 H HB2  A ASP   B 1 14  ? 28.709 -23.777 -16.298 0.60 28.69 ?  14  ASP   B HB2  1 
ATOM   4095 H HB2  B ASP   B 1 14  ? 28.654 -23.832 -16.397 0.40 27.67 ?  14  ASP   B HB2  1 
ATOM   4096 H HB3  A ASP   B 1 14  ? 29.352 -22.932 -17.481 0.60 28.69 ?  14  ASP   B HB3  1 
ATOM   4097 H HB3  B ASP   B 1 14  ? 29.337 -22.960 -17.537 0.40 27.67 ?  14  ASP   B HB3  1 
ATOM   4098 N N    . ASN   B 1 15  ? 31.800 -23.691 -15.147 1.00 17.27 ?  15  ASN   B N    1 
ATOM   4099 C CA   . ASN   B 1 15  ? 32.764 -22.773 -14.546 1.00 15.18 ?  15  ASN   B CA   1 
ATOM   4100 C C    . ASN   B 1 15  ? 33.861 -23.428 -13.716 1.00 14.24 ?  15  ASN   B C    1 
ATOM   4101 O O    . ASN   B 1 15  ? 34.703 -22.702 -13.182 1.00 14.44 ?  15  ASN   B O    1 
ATOM   4102 C CB   . ASN   B 1 15  ? 32.055 -21.714 -13.685 1.00 15.52 ?  15  ASN   B CB   1 
ATOM   4103 C CG   . ASN   B 1 15  ? 31.421 -22.311 -12.448 1.00 14.99 ?  15  ASN   B CG   1 
ATOM   4104 O OD1  . ASN   B 1 15  ? 30.483 -23.109 -12.537 1.00 16.35 ?  15  ASN   B OD1  1 
ATOM   4105 N ND2  . ASN   B 1 15  ? 31.942 -21.964 -11.289 1.00 14.62 ?  15  ASN   B ND2  1 
ATOM   4106 H H    A ASN   B 1 15  ? 31.411 -24.215 -14.583 0.60 20.70 ?  15  ASN   B H    1 
ATOM   4107 H H    B ASN   B 1 15  ? 31.443 -24.244 -14.590 0.40 20.70 ?  15  ASN   B H    1 
ATOM   4108 H HA   . ASN   B 1 15  ? 33.210 -22.296 -15.255 1.00 18.19 ?  15  ASN   B HA   1 
ATOM   4109 H HB2  . ASN   B 1 15  ? 32.711 -21.047 -13.402 1.00 18.60 ?  15  ASN   B HB2  1 
ATOM   4110 H HB3  . ASN   B 1 15  ? 31.360 -21.283 -14.208 1.00 18.60 ?  15  ASN   B HB3  1 
ATOM   4111 H HD21 . ASN   B 1 15  ? 31.612 -22.277 -10.558 1.00 17.53 ?  15  ASN   B HD21 1 
ATOM   4112 H HD22 . ASN   B 1 15  ? 32.600 -21.407 -11.254 1.00 17.53 ?  15  ASN   B HD22 1 
ATOM   4113 N N    . VAL   B 1 16  ? 33.881 -24.752 -13.580 1.00 13.91 ?  16  VAL   B N    1 
ATOM   4114 C CA   . VAL   B 1 16  ? 34.878 -25.442 -12.769 1.00 13.61 ?  16  VAL   B CA   1 
ATOM   4115 C C    . VAL   B 1 16  ? 35.678 -26.378 -13.662 1.00 13.79 ?  16  VAL   B C    1 
ATOM   4116 O O    . VAL   B 1 16  ? 35.104 -27.251 -14.331 1.00 14.92 ?  16  VAL   B O    1 
ATOM   4117 C CB   . VAL   B 1 16  ? 34.245 -26.203 -11.590 1.00 13.93 ?  16  VAL   B CB   1 
ATOM   4118 C CG1  . VAL   B 1 16  ? 35.321 -26.931 -10.791 1.00 14.29 ?  16  VAL   B CG1  1 
ATOM   4119 C CG2  . VAL   B 1 16  ? 33.451 -25.253 -10.705 1.00 14.71 ?  16  VAL   B CG2  1 
ATOM   4120 H H    . VAL   B 1 16  ? 33.314 -25.288 -13.950 1.00 16.67 ?  16  VAL   B H    1 
ATOM   4121 H HA   . VAL   B 1 16  ? 35.491 -24.787 -12.397 1.00 16.31 ?  16  VAL   B HA   1 
ATOM   4122 H HB   . VAL   B 1 16  ? 33.632 -26.870 -11.940 1.00 16.70 ?  16  VAL   B HB   1 
ATOM   4123 H HG11 . VAL   B 1 16  ? 34.938 -27.225 -9.951  1.00 17.12 ?  16  VAL   B HG11 1 
ATOM   4124 H HG12 . VAL   B 1 16  ? 35.636 -27.691 -11.299 1.00 17.12 ?  16  VAL   B HG12 1 
ATOM   4125 H HG13 . VAL   B 1 16  ? 36.052 -26.314 -10.621 1.00 17.12 ?  16  VAL   B HG13 1 
ATOM   4126 H HG21 . VAL   B 1 16  ? 33.113 -25.742 -9.941  1.00 17.62 ?  16  VAL   B HG21 1 
ATOM   4127 H HG22 . VAL   B 1 16  ? 34.035 -24.537 -10.409 1.00 17.62 ?  16  VAL   B HG22 1 
ATOM   4128 H HG23 . VAL   B 1 16  ? 32.714 -24.886 -11.218 1.00 17.62 ?  16  VAL   B HG23 1 
ATOM   4129 N N    . TYR   B 1 17  ? 37.004 -26.211 -13.631 1.00 13.90 ?  17  TYR   B N    1 
ATOM   4130 C CA   . TYR   B 1 17  ? 37.953 -26.959 -14.439 1.00 14.32 ?  17  TYR   B CA   1 
ATOM   4131 C C    . TYR   B 1 17  ? 38.996 -27.570 -13.516 1.00 13.48 ?  17  TYR   B C    1 
ATOM   4132 O O    . TYR   B 1 17  ? 39.264 -27.041 -12.432 1.00 13.81 ?  17  TYR   B O    1 
ATOM   4133 C CB   . TYR   B 1 17  ? 38.671 -26.016 -15.413 1.00 16.24 ?  17  TYR   B CB   1 
ATOM   4134 C CG   . TYR   B 1 17  ? 37.751 -25.247 -16.325 1.00 18.83 ?  17  TYR   B CG   1 
ATOM   4135 C CD1  . TYR   B 1 17  ? 37.138 -24.071 -15.904 1.00 19.95 ?  17  TYR   B CD1  1 
ATOM   4136 C CD2  . TYR   B 1 17  ? 37.490 -25.697 -17.609 1.00 20.66 ?  17  TYR   B CD2  1 
ATOM   4137 C CE1  . TYR   B 1 17  ? 36.288 -23.367 -16.742 1.00 21.49 ?  17  TYR   B CE1  1 
ATOM   4138 C CE2  . TYR   B 1 17  ? 36.648 -25.002 -18.455 1.00 22.07 ?  17  TYR   B CE2  1 
ATOM   4139 C CZ   . TYR   B 1 17  ? 36.048 -23.839 -18.016 1.00 22.42 ?  17  TYR   B CZ   1 
ATOM   4140 O OH   . TYR   B 1 17  ? 35.210 -23.151 -18.860 1.00 23.82 ?  17  TYR   B OH   1 
ATOM   4141 H H    . TYR   B 1 17  ? 37.399 -25.634 -13.119 1.00 16.66 ?  17  TYR   B H    1 
ATOM   4142 H HA   . TYR   B 1 17  ? 37.500 -27.662 -14.935 1.00 17.16 ?  17  TYR   B HA   1 
ATOM   4143 H HB2  . TYR   B 1 17  ? 39.192 -25.375 -14.905 1.00 19.46 ?  17  TYR   B HB2  1 
ATOM   4144 H HB3  . TYR   B 1 17  ? 39.256 -26.542 -15.976 1.00 19.46 ?  17  TYR   B HB3  1 
ATOM   4145 H HD1  . TYR   B 1 17  ? 37.301 -23.752 -15.046 1.00 23.92 ?  17  TYR   B HD1  1 
ATOM   4146 H HD2  . TYR   B 1 17  ? 37.891 -26.481 -17.909 1.00 24.77 ?  17  TYR   B HD2  1 
ATOM   4147 H HE1  . TYR   B 1 17  ? 35.886 -22.580 -16.449 1.00 25.77 ?  17  TYR   B HE1  1 
ATOM   4148 H HE2  . TYR   B 1 17  ? 36.481 -25.317 -19.314 1.00 26.46 ?  17  TYR   B HE2  1 
ATOM   4149 H HH   . TYR   B 1 17  ? 35.153 -23.548 -19.598 1.00 28.56 ?  17  TYR   B HH   1 
ATOM   4150 N N    . ILE   B 1 18  ? 39.612 -28.670 -13.948 1.00 13.26 ?  18  ILE   B N    1 
ATOM   4151 C CA   . ILE   B 1 18  ? 40.539 -29.389 -13.081 1.00 13.17 ?  18  ILE   B CA   1 
ATOM   4152 C C    . ILE   B 1 18  ? 41.704 -29.940 -13.894 1.00 13.49 ?  18  ILE   B C    1 
ATOM   4153 O O    . ILE   B 1 18  ? 41.550 -30.340 -15.052 1.00 15.05 ?  18  ILE   B O    1 
ATOM   4154 C CB   . ILE   B 1 18  ? 39.785 -30.486 -12.287 1.00 13.85 ?  18  ILE   B CB   1 
ATOM   4155 C CG1  . ILE   B 1 18  ? 40.640 -31.035 -11.143 1.00 14.40 ?  18  ILE   B CG1  1 
ATOM   4156 C CG2  . ILE   B 1 18  ? 39.289 -31.601 -13.215 1.00 14.32 ?  18  ILE   B CG2  1 
ATOM   4157 C CD1  . ILE   B 1 18  ? 39.823 -31.840 -10.135 1.00 15.79 ?  18  ILE   B CD1  1 
ATOM   4158 H H    . ILE   B 1 18  ? 39.516 -29.016 -14.729 1.00 15.88 ?  18  ILE   B H    1 
ATOM   4159 H HA   . ILE   B 1 18  ? 40.900 -28.768 -12.430 1.00 15.78 ?  18  ILE   B HA   1 
ATOM   4160 H HB   . ILE   B 1 18  ? 38.998 -30.078 -11.886 1.00 16.60 ?  18  ILE   B HB   1 
ATOM   4161 H HG12 . ILE   B 1 18  ? 41.321 -31.616 -11.506 1.00 17.26 ?  18  ILE   B HG12 1 
ATOM   4162 H HG13 . ILE   B 1 18  ? 41.046 -30.292 -10.669 1.00 17.26 ?  18  ILE   B HG13 1 
ATOM   4163 H HG21 . ILE   B 1 18  ? 38.694 -32.185 -12.716 1.00 17.16 ?  18  ILE   B HG21 1 
ATOM   4164 H HG22 . ILE   B 1 18  ? 38.812 -31.200 -13.955 1.00 17.16 ?  18  ILE   B HG22 1 
ATOM   4165 H HG23 . ILE   B 1 18  ? 40.051 -32.102 -13.538 1.00 17.16 ?  18  ILE   B HG23 1 
ATOM   4166 H HD11 . ILE   B 1 18  ? 40.403 -32.116 -9.408  1.00 18.93 ?  18  ILE   B HD11 1 
ATOM   4167 H HD12 . ILE   B 1 18  ? 39.105 -31.284 -9.792  1.00 18.93 ?  18  ILE   B HD12 1 
ATOM   4168 H HD13 . ILE   B 1 18  ? 39.453 -32.620 -10.578 1.00 18.93 ?  18  ILE   B HD13 1 
ATOM   4169 N N    . LYS   B 1 19  ? 42.883 -29.967 -13.269 1.00 14.14 ?  19  LYS   B N    1 
ATOM   4170 C CA   . LYS   B 1 19  ? 44.092 -30.451 -13.920 1.00 14.87 ?  19  LYS   B CA   1 
ATOM   4171 C C    . LYS   B 1 19  ? 44.987 -31.124 -12.893 1.00 14.64 ?  19  LYS   B C    1 
ATOM   4172 O O    . LYS   B 1 19  ? 45.067 -30.689 -11.744 1.00 14.06 ?  19  LYS   B O    1 
ATOM   4173 C CB   . LYS   B 1 19  ? 44.866 -29.291 -14.560 1.00 16.30 ?  19  LYS   B CB   1 
ATOM   4174 C CG   . LYS   B 1 19  ? 46.089 -29.698 -15.363 1.00 17.61 ?  19  LYS   B CG   1 
ATOM   4175 C CD   . LYS   B 1 19  ? 46.807 -28.466 -15.899 1.00 19.13 ?  19  LYS   B CD   1 
ATOM   4176 C CE   . LYS   B 1 19  ? 47.990 -28.840 -16.772 1.00 20.87 ?  19  LYS   B CE   1 
ATOM   4177 N NZ   . LYS   B 1 19  ? 48.737 -27.643 -17.238 1.00 21.92 ?  19  LYS   B NZ   1 
ATOM   4178 H H    . LYS   B 1 19  ? 42.998 -29.705 -12.456 1.00 16.94 ?  19  LYS   B H    1 
ATOM   4179 H HA   . LYS   B 1 19  ? 43.856 -31.096 -14.606 1.00 17.83 ?  19  LYS   B HA   1 
ATOM   4180 H HB2  . LYS   B 1 19  ? 44.266 -28.819 -15.161 1.00 19.53 ?  19  LYS   B HB2  1 
ATOM   4181 H HB3  . LYS   B 1 19  ? 45.157 -28.690 -13.855 1.00 19.53 ?  19  LYS   B HB3  1 
ATOM   4182 H HG2  . LYS   B 1 19  ? 46.700 -30.188 -14.792 1.00 21.11 ?  19  LYS   B HG2  1 
ATOM   4183 H HG3  . LYS   B 1 19  ? 45.812 -30.246 -16.114 1.00 21.11 ?  19  LYS   B HG3  1 
ATOM   4184 H HD2  . LYS   B 1 19  ? 46.188 -27.941 -16.431 1.00 22.93 ?  19  LYS   B HD2  1 
ATOM   4185 H HD3  . LYS   B 1 19  ? 47.136 -27.938 -15.152 1.00 22.93 ?  19  LYS   B HD3  1 
ATOM   4186 H HE2  . LYS   B 1 19  ? 48.595 -29.401 -16.262 1.00 25.02 ?  19  LYS   B HE2  1 
ATOM   4187 H HE3  . LYS   B 1 19  ? 47.666 -29.322 -17.551 1.00 25.02 ?  19  LYS   B HE3  1 
ATOM   4188 H HZ1  . LYS   B 1 19  ? 49.355 -27.886 -17.831 1.00 26.28 ?  19  LYS   B HZ1  1 
ATOM   4189 H HZ2  . LYS   B 1 19  ? 48.179 -27.067 -17.621 1.00 26.28 ?  19  LYS   B HZ2  1 
ATOM   4190 H HZ3  . LYS   B 1 19  ? 49.136 -27.249 -16.549 1.00 26.28 ?  19  LYS   B HZ3  1 
ATOM   4191 N N    . ASN   B 1 20  ? 45.675 -32.176 -13.323 1.00 15.29 ?  20  ASN   B N    1 
ATOM   4192 C CA   . ASN   B 1 20  ? 46.708 -32.800 -12.504 1.00 16.28 ?  20  ASN   B CA   1 
ATOM   4193 C C    . ASN   B 1 20  ? 47.980 -31.984 -12.692 1.00 16.71 ?  20  ASN   B C    1 
ATOM   4194 O O    . ASN   B 1 20  ? 48.618 -32.052 -13.749 1.00 18.50 ?  20  ASN   B O    1 
ATOM   4195 C CB   . ASN   B 1 20  ? 46.884 -34.253 -12.945 1.00 17.71 ?  20  ASN   B CB   1 
ATOM   4196 C CG   . ASN   B 1 20  ? 48.045 -34.960 -12.264 1.00 18.87 ?  20  ASN   B CG   1 
ATOM   4197 O OD1  . ASN   B 1 20  ? 48.700 -35.817 -12.871 1.00 21.29 ?  20  ASN   B OD1  1 
ATOM   4198 N ND2  . ASN   B 1 20  ? 48.290 -34.639 -11.003 1.00 18.25 ?  20  ASN   B ND2  1 
ATOM   4199 H H    . ASN   B 1 20  ? 45.568 -32.539 -14.092 1.00 18.33 ?  20  ASN   B H    1 
ATOM   4200 H HA   . ASN   B 1 20  ? 46.437 -32.783 -11.571 1.00 19.52 ?  20  ASN   B HA   1 
ATOM   4201 H HB2  . ASN   B 1 20  ? 46.074 -34.745 -12.730 1.00 21.23 ?  20  ASN   B HB2  1 
ATOM   4202 H HB3  . ASN   B 1 20  ? 47.038 -34.271 -13.899 1.00 21.23 ?  20  ASN   B HB3  1 
ATOM   4203 H HD21 . ASN   B 1 20  ? 48.941 -35.006 -10.584 1.00 21.88 ?  20  ASN   B HD21 1 
ATOM   4204 H HD22 . ASN   B 1 20  ? 47.804 -34.045 -10.601 1.00 21.88 ?  20  ASN   B HD22 1 
ATOM   4205 N N    . ALA   B 1 21  ? 48.331 -31.183 -11.685 1.00 16.48 ?  21  ALA   B N    1 
ATOM   4206 C CA   . ALA   B 1 21  ? 49.427 -30.238 -11.838 1.00 17.54 ?  21  ALA   B CA   1 
ATOM   4207 C C    . ALA   B 1 21  ? 49.888 -29.753 -10.473 1.00 16.52 ?  21  ALA   B C    1 
ATOM   4208 O O    . ALA   B 1 21  ? 49.151 -29.805 -9.486  1.00 16.33 ?  21  ALA   B O    1 
ATOM   4209 C CB   . ALA   B 1 21  ? 49.013 -29.054 -12.714 1.00 19.04 ?  21  ALA   B CB   1 
ATOM   4210 H H    . ALA   B 1 21  ? 47.948 -31.170 -10.908 1.00 19.75 ?  21  ALA   B H    1 
ATOM   4211 H HA   . ALA   B 1 21  ? 50.168 -30.689 -12.261 1.00 21.03 ?  21  ALA   B HA   1 
ATOM   4212 H HB1  . ALA   B 1 21  ? 49.791 -28.508 -12.877 1.00 22.83 ?  21  ALA   B HB1  1 
ATOM   4213 H HB2  . ALA   B 1 21  ? 48.664 -29.399 -13.551 1.00 22.83 ?  21  ALA   B HB2  1 
ATOM   4214 H HB3  . ALA   B 1 21  ? 48.326 -28.546 -12.255 1.00 22.83 ?  21  ALA   B HB3  1 
ATOM   4215 N N    . ASP   B 1 22  ? 51.147 -29.319 -10.448 1.00 16.02 ?  22  ASP   B N    1 
ATOM   4216 C CA   . ASP   B 1 22  ? 51.760 -28.620 -9.324  1.00 15.38 ?  22  ASP   B CA   1 
ATOM   4217 C C    . ASP   B 1 22  ? 51.346 -27.153 -9.416  1.00 13.87 ?  22  ASP   B C    1 
ATOM   4218 O O    . ASP   B 1 22  ? 51.653 -26.481 -10.405 1.00 14.31 ?  22  ASP   B O    1 
ATOM   4219 C CB   . ASP   B 1 22  ? 53.278 -28.793 -9.477  1.00 16.41 ?  22  ASP   B CB   1 
ATOM   4220 C CG   . ASP   B 1 22  ? 54.097 -28.036 -8.440  1.00 17.91 ?  22  ASP   B CG   1 
ATOM   4221 O OD1  . ASP   B 1 22  ? 53.733 -26.915 -8.046  1.00 18.01 ?  22  ASP   B OD1  1 
ATOM   4222 O OD2  . ASP   B 1 22  ? 55.165 -28.559 -8.050  1.00 20.42 -1 22  ASP   B OD2  1 
ATOM   4223 H H    . ASP   B 1 22  ? 51.695 -29.432 -11.104 1.00 19.20 ?  22  ASP   B H    1 
ATOM   4224 H HA   . ASP   B 1 22  ? 51.472 -29.003 -8.477  1.00 18.44 ?  22  ASP   B HA   1 
ATOM   4225 H HB2  . ASP   B 1 22  ? 53.503 -29.729 -9.403  1.00 19.67 ?  22  ASP   B HB2  1 
ATOM   4226 H HB3  . ASP   B 1 22  ? 53.543 -28.455 -10.347 1.00 19.67 ?  22  ASP   B HB3  1 
ATOM   4227 N N    . ILE   B 1 23  ? 50.629 -26.664 -8.398  1.00 13.51 ?  23  ILE   B N    1 
ATOM   4228 C CA   . ILE   B 1 23  ? 50.035 -25.327 -8.471  1.00 13.05 ?  23  ILE   B CA   1 
ATOM   4229 C C    . ILE   B 1 23  ? 51.087 -24.233 -8.610  1.00 12.47 ?  23  ILE   B C    1 
ATOM   4230 O O    . ILE   B 1 23  ? 50.811 -23.187 -9.209  1.00 12.55 ?  23  ILE   B O    1 
ATOM   4231 C CB   . ILE   B 1 23  ? 49.090 -25.090 -7.276  1.00 13.50 ?  23  ILE   B CB   1 
ATOM   4232 C CG1  . ILE   B 1 23  ? 48.253 -23.828 -7.488  1.00 14.15 ?  23  ILE   B CG1  1 
ATOM   4233 C CG2  . ILE   B 1 23  ? 49.856 -25.046 -5.969  1.00 14.89 ?  23  ILE   B CG2  1 
ATOM   4234 C CD1  . ILE   B 1 23  ? 47.138 -23.658 -6.472  1.00 15.07 ?  23  ILE   B CD1  1 
ATOM   4235 H H    . ILE   B 1 23  ? 50.476 -27.086 -7.664  1.00 16.19 ?  23  ILE   B H    1 
ATOM   4236 H HA   . ILE   B 1 23  ? 49.490 -25.292 -9.268  1.00 15.63 ?  23  ILE   B HA   1 
ATOM   4237 H HB   . ILE   B 1 23  ? 48.478 -25.843 -7.233  1.00 16.18 ?  23  ILE   B HB   1 
ATOM   4238 H HG12 . ILE   B 1 23  ? 48.837 -23.054 -7.426  1.00 16.96 ?  23  ILE   B HG12 1 
ATOM   4239 H HG13 . ILE   B 1 23  ? 47.853 -23.864 -8.374  1.00 16.96 ?  23  ILE   B HG13 1 
ATOM   4240 H HG21 . ILE   B 1 23  ? 49.228 -25.044 -5.232  1.00 17.85 ?  23  ILE   B HG21 1 
ATOM   4241 H HG22 . ILE   B 1 23  ? 50.431 -25.825 -5.912  1.00 17.85 ?  23  ILE   B HG22 1 
ATOM   4242 H HG23 . ILE   B 1 23  ? 50.395 -24.238 -5.946  1.00 17.85 ?  23  ILE   B HG23 1 
ATOM   4243 H HD11 . ILE   B 1 23  ? 46.606 -22.886 -6.716  1.00 18.06 ?  23  ILE   B HD11 1 
ATOM   4244 H HD12 . ILE   B 1 23  ? 46.584 -24.457 -6.481  1.00 18.06 ?  23  ILE   B HD12 1 
ATOM   4245 H HD13 . ILE   B 1 23  ? 47.527 -23.533 -5.595  1.00 18.06 ?  23  ILE   B HD13 1 
ATOM   4246 N N    . VAL   B 1 24  ? 52.283 -24.428 -8.046  1.00 13.10 ?  24  VAL   B N    1 
ATOM   4247 C CA   . VAL   B 1 24  ? 53.356 -23.447 -8.216  1.00 13.35 ?  24  VAL   B CA   1 
ATOM   4248 C C    . VAL   B 1 24  ? 53.806 -23.405 -9.668  1.00 13.73 ?  24  VAL   B C    1 
ATOM   4249 O O    . VAL   B 1 24  ? 53.946 -22.331 -10.268 1.00 14.11 ?  24  VAL   B O    1 
ATOM   4250 C CB   . VAL   B 1 24  ? 54.536 -23.763 -7.276  1.00 14.33 ?  24  VAL   B CB   1 
ATOM   4251 C CG1  . VAL   B 1 24  ? 55.733 -22.866 -7.602  1.00 14.80 ?  24  VAL   B CG1  1 
ATOM   4252 C CG2  . VAL   B 1 24  ? 54.120 -23.605 -5.832  1.00 15.51 ?  24  VAL   B CG2  1 
ATOM   4253 H H    . VAL   B 1 24  ? 52.493 -25.111 -7.565  1.00 15.69 ?  24  VAL   B H    1 
ATOM   4254 H HA   . VAL   B 1 24  ? 53.017 -22.571 -7.982  1.00 16.00 ?  24  VAL   B HA   1 
ATOM   4255 H HB   . VAL   B 1 24  ? 54.808 -24.685 -7.406  1.00 17.18 ?  24  VAL   B HB   1 
ATOM   4256 H HG11 . VAL   B 1 24  ? 56.311 -22.818 -6.824  1.00 17.74 ?  24  VAL   B HG11 1 
ATOM   4257 H HG12 . VAL   B 1 24  ? 56.219 -23.254 -8.347  1.00 17.74 ?  24  VAL   B HG12 1 
ATOM   4258 H HG13 . VAL   B 1 24  ? 55.414 -21.981 -7.833  1.00 17.74 ?  24  VAL   B HG13 1 
ATOM   4259 H HG21 . VAL   B 1 24  ? 54.850 -23.885 -5.260  1.00 18.59 ?  24  VAL   B HG21 1 
ATOM   4260 H HG22 . VAL   B 1 24  ? 53.910 -22.672 -5.667  1.00 18.59 ?  24  VAL   B HG22 1 
ATOM   4261 H HG23 . VAL   B 1 24  ? 53.338 -24.155 -5.665  1.00 18.59 ?  24  VAL   B HG23 1 
ATOM   4262 N N    . GLU   B 1 25  ? 54.066 -24.578 -10.247 1.00 15.08 ?  25  GLU   B N    1 
ATOM   4263 C CA   . GLU   B 1 25  ? 54.451 -24.629 -11.651 1.00 16.29 ?  25  GLU   B CA   1 
ATOM   4264 C C    . GLU   B 1 25  ? 53.346 -24.075 -12.537 1.00 15.27 ?  25  GLU   B C    1 
ATOM   4265 O O    . GLU   B 1 25  ? 53.616 -23.360 -13.511 1.00 15.98 ?  25  GLU   B O    1 
ATOM   4266 C CB   . GLU   B 1 25  ? 54.825 -26.061 -12.035 1.00 19.95 ?  25  GLU   B CB   1 
ATOM   4267 C CG   . GLU   B 1 25  ? 56.124 -26.522 -11.388 1.00 25.14 ?  25  GLU   B CG   1 
ATOM   4268 C CD   . GLU   B 1 25  ? 57.237 -25.480 -11.454 1.00 30.43 ?  25  GLU   B CD   1 
ATOM   4269 O OE1  . GLU   B 1 25  ? 57.623 -25.080 -12.573 1.00 31.86 ?  25  GLU   B OE1  1 
ATOM   4270 O OE2  . GLU   B 1 25  ? 57.717 -25.045 -10.380 1.00 31.84 -1 25  GLU   B OE2  1 
ATOM   4271 H H    . GLU   B 1 25  ? 54.023 -25.345 -9.853  1.00 18.08 ?  25  GLU   B H    1 
ATOM   4272 H HA   . GLU   B 1 25  ? 55.214 -24.058 -11.781 1.00 19.52 ?  25  GLU   B HA   1 
ATOM   4273 H HB2  . GLU   B 1 25  ? 54.119 -26.666 -11.743 1.00 23.92 ?  25  GLU   B HB2  1 
ATOM   4274 H HB3  . GLU   B 1 25  ? 54.928 -26.116 -12.997 1.00 23.92 ?  25  GLU   B HB3  1 
ATOM   4275 H HG2  . GLU   B 1 25  ? 55.970 -26.697 -10.454 1.00 30.15 ?  25  GLU   B HG2  1 
ATOM   4276 H HG3  . GLU   B 1 25  ? 56.434 -27.321 -11.841 1.00 30.15 ?  25  GLU   B HG3  1 
ATOM   4277 N N    . GLU   B 1 26  ? 52.094 -24.383 -12.203 1.00 14.33 ?  26  GLU   B N    1 
ATOM   4278 C CA   . GLU   B 1 26  ? 50.972 -23.844 -12.961 1.00 15.16 ?  26  GLU   B CA   1 
ATOM   4279 C C    . GLU   B 1 26  ? 50.933 -22.328 -12.872 1.00 14.35 ?  26  GLU   B C    1 
ATOM   4280 O O    . GLU   B 1 26  ? 50.748 -21.647 -13.885 1.00 15.77 ?  26  GLU   B O    1 
ATOM   4281 C CB   . GLU   B 1 26  ? 49.655 -24.429 -12.448 1.00 16.73 ?  26  GLU   B CB   1 
ATOM   4282 C CG   . GLU   B 1 26  ? 49.256 -25.732 -13.093 1.00 19.58 ?  26  GLU   B CG   1 
ATOM   4283 C CD   . GLU   B 1 26  ? 49.019 -25.611 -14.595 1.00 21.32 ?  26  GLU   B CD   1 
ATOM   4284 O OE1  . GLU   B 1 26  ? 48.062 -24.931 -15.023 1.00 21.14 ?  26  GLU   B OE1  1 
ATOM   4285 O OE2  . GLU   B 1 26  ? 49.784 -26.228 -15.346 1.00 23.76 -1 26  GLU   B OE2  1 
ATOM   4286 H H    . GLU   B 1 26  ? 51.865 -24.901 -11.548 1.00 17.17 ?  26  GLU   B H    1 
ATOM   4287 H HA   . GLU   B 1 26  ? 51.070 -24.086 -13.890 1.00 18.17 ?  26  GLU   B HA   1 
ATOM   4288 H HB2  . GLU   B 1 26  ? 49.730 -24.586 -11.493 1.00 20.05 ?  26  GLU   B HB2  1 
ATOM   4289 H HB3  . GLU   B 1 26  ? 48.942 -23.789 -12.616 1.00 20.05 ?  26  GLU   B HB3  1 
ATOM   4290 H HG2  . GLU   B 1 26  ? 49.965 -26.372 -12.946 1.00 23.47 ?  26  GLU   B HG2  1 
ATOM   4291 H HG3  . GLU   B 1 26  ? 48.431 -26.046 -12.691 1.00 23.47 ?  26  GLU   B HG3  1 
ATOM   4292 N N    . ALA   B 1 27  ? 51.081 -21.782 -11.661 1.00 13.80 ?  27  ALA   B N    1 
ATOM   4293 C CA   . ALA   B 1 27  ? 51.052 -20.332 -11.507 1.00 13.92 ?  27  ALA   B CA   1 
ATOM   4294 C C    . ALA   B 1 27  ? 52.117 -19.670 -12.368 1.00 14.90 ?  27  ALA   B C    1 
ATOM   4295 O O    . ALA   B 1 27  ? 51.852 -18.662 -13.038 1.00 15.62 ?  27  ALA   B O    1 
ATOM   4296 C CB   . ALA   B 1 27  ? 51.218 -19.955 -10.035 1.00 14.24 ?  27  ALA   B CB   1 
ATOM   4297 H H    . ALA   B 1 27  ? 51.186 -22.221 -10.925 1.00 16.54 ?  27  ALA   B H    1 
ATOM   4298 H HA   . ALA   B 1 27  ? 50.192 -19.999 -11.795 1.00 16.67 ?  27  ALA   B HA   1 
ATOM   4299 H HB1  . ALA   B 1 27  ? 51.197 -18.989 -9.949  1.00 17.06 ?  27  ALA   B HB1  1 
ATOM   4300 H HB2  . ALA   B 1 27  ? 50.490 -20.347 -9.524  1.00 17.06 ?  27  ALA   B HB2  1 
ATOM   4301 H HB3  . ALA   B 1 27  ? 52.067 -20.297 -9.712  1.00 17.06 ?  27  ALA   B HB3  1 
ATOM   4302 N N    . LYS   B 1 28  ? 53.331 -20.223 -12.368 1.00 16.38 ?  28  LYS   B N    1 
ATOM   4303 C CA   . LYS   B 1 28  ? 54.409 -19.602 -13.128 1.00 18.58 ?  28  LYS   B CA   1 
ATOM   4304 C C    . LYS   B 1 28  ? 54.157 -19.676 -14.630 1.00 19.39 ?  28  LYS   B C    1 
ATOM   4305 O O    . LYS   B 1 28  ? 54.567 -18.774 -15.370 1.00 20.63 ?  28  LYS   B O    1 
ATOM   4306 C CB   . LYS   B 1 28  ? 55.760 -20.217 -12.740 1.00 21.63 ?  28  LYS   B CB   1 
ATOM   4307 C CG   . LYS   B 1 28  ? 56.154 -19.926 -11.291 1.00 25.28 ?  28  LYS   B CG   1 
ATOM   4308 C CD   . LYS   B 1 28  ? 57.586 -20.332 -10.965 1.00 29.43 ?  28  LYS   B CD   1 
ATOM   4309 C CE   . LYS   B 1 28  ? 57.688 -21.801 -10.635 1.00 32.79 ?  28  LYS   B CE   1 
ATOM   4310 N NZ   . LYS   B 1 28  ? 59.042 -22.143 -10.113 1.00 34.90 ?  28  LYS   B NZ   1 
ATOM   4311 H H    . LYS   B 1 28  ? 53.555 -20.937 -11.940 1.00 19.63 ?  28  LYS   B H    1 
ATOM   4312 H HA   . LYS   B 1 28  ? 54.449 -18.662 -12.889 1.00 22.27 ?  28  LYS   B HA   1 
ATOM   4313 H HB2  . LYS   B 1 28  ? 55.717 -21.178 -12.845 1.00 25.93 ?  28  LYS   B HB2  1 
ATOM   4314 H HB3  . LYS   B 1 28  ? 56.454 -19.850 -13.312 1.00 25.93 ?  28  LYS   B HB3  1 
ATOM   4315 H HG2  . LYS   B 1 28  ? 56.068 -18.972 -11.129 1.00 30.32 ?  28  LYS   B HG2  1 
ATOM   4316 H HG3  . LYS   B 1 28  ? 55.561 -20.415 -10.701 1.00 30.32 ?  28  LYS   B HG3  1 
ATOM   4317 H HD2  . LYS   B 1 28  ? 58.148 -20.149 -11.733 1.00 35.29 ?  28  LYS   B HD2  1 
ATOM   4318 H HD3  . LYS   B 1 28  ? 57.889 -19.822 -10.198 1.00 35.29 ?  28  LYS   B HD3  1 
ATOM   4319 H HE2  . LYS   B 1 28  ? 57.034 -22.023 -9.954  1.00 39.32 ?  28  LYS   B HE2  1 
ATOM   4320 H HE3  . LYS   B 1 28  ? 57.528 -22.324 -11.436 1.00 39.32 ?  28  LYS   B HE3  1 
ATOM   4321 H HZ1  . LYS   B 1 28  ? 59.085 -23.012 -9.924  1.00 41.86 ?  28  LYS   B HZ1  1 
ATOM   4322 H HZ2  . LYS   B 1 28  ? 59.660 -21.949 -10.723 1.00 41.86 ?  28  LYS   B HZ2  1 
ATOM   4323 H HZ3  . LYS   B 1 28  ? 59.209 -21.677 -9.373  1.00 41.86 ?  28  LYS   B HZ3  1 
ATOM   4324 N N    . LYS   B 1 29  ? 53.457 -20.713 -15.092 1.00 20.51 ?  29  LYS   B N    1 
ATOM   4325 C CA   . LYS   B 1 29  ? 53.161 -20.848 -16.515 1.00 23.11 ?  29  LYS   B CA   1 
ATOM   4326 C C    . LYS   B 1 29  ? 51.926 -20.051 -16.928 1.00 21.98 ?  29  LYS   B C    1 
ATOM   4327 O O    . LYS   B 1 29  ? 51.940 -19.387 -17.969 1.00 23.02 ?  29  LYS   B O    1 
ATOM   4328 C CB   . LYS   B 1 29  ? 52.964 -22.322 -16.867 1.00 27.81 ?  29  LYS   B CB   1 
ATOM   4329 C CG   . LYS   B 1 29  ? 52.902 -22.594 -18.362 1.00 32.13 ?  29  LYS   B CG   1 
ATOM   4330 C CD   . LYS   B 1 29  ? 53.179 -24.058 -18.683 1.00 35.59 ?  29  LYS   B CD   1 
ATOM   4331 C CE   . LYS   B 1 29  ? 52.111 -24.976 -18.108 1.00 37.82 ?  29  LYS   B CE   1 
ATOM   4332 N NZ   . LYS   B 1 29  ? 52.360 -26.406 -18.456 1.00 38.97 ?  29  LYS   B NZ   1 
ATOM   4333 H H    . LYS   B 1 29  ? 53.152 -21.347 -14.598 1.00 24.59 ?  29  LYS   B H    1 
ATOM   4334 H HA   . LYS   B 1 29  ? 53.915 -20.512 -17.022 1.00 27.71 ?  29  LYS   B HA   1 
ATOM   4335 H HB2  . LYS   B 1 29  ? 53.705 -22.829 -16.502 1.00 33.35 ?  29  LYS   B HB2  1 
ATOM   4336 H HB3  . LYS   B 1 29  ? 52.131 -22.626 -16.475 1.00 33.35 ?  29  LYS   B HB3  1 
ATOM   4337 H HG2  . LYS   B 1 29  ? 52.016 -22.374 -18.690 1.00 38.53 ?  29  LYS   B HG2  1 
ATOM   4338 H HG3  . LYS   B 1 29  ? 53.569 -22.052 -18.813 1.00 38.53 ?  29  LYS   B HG3  1 
ATOM   4339 H HD2  . LYS   B 1 29  ? 53.195 -24.178 -19.646 1.00 42.68 ?  29  LYS   B HD2  1 
ATOM   4340 H HD3  . LYS   B 1 29  ? 54.035 -24.313 -18.301 1.00 42.68 ?  29  LYS   B HD3  1 
ATOM   4341 H HE2  . LYS   B 1 29  ? 52.107 -24.897 -17.141 1.00 45.36 ?  29  LYS   B HE2  1 
ATOM   4342 H HE3  . LYS   B 1 29  ? 51.247 -24.722 -18.468 1.00 45.36 ?  29  LYS   B HE3  1 
ATOM   4343 H HZ1  . LYS   B 1 29  ? 51.721 -26.919 -18.108 1.00 46.74 ?  29  LYS   B HZ1  1 
ATOM   4344 H HZ2  . LYS   B 1 29  ? 52.363 -26.508 -19.340 1.00 46.74 ?  29  LYS   B HZ2  1 
ATOM   4345 H HZ3  . LYS   B 1 29  ? 53.148 -26.665 -18.132 1.00 46.74 ?  29  LYS   B HZ3  1 
ATOM   4346 N N    . VAL   B 1 30  ? 50.851 -20.123 -16.136 1.00 20.47 ?  30  VAL   B N    1 
ATOM   4347 C CA   . VAL   B 1 30  ? 49.557 -19.547 -16.514 1.00 20.57 ?  30  VAL   B CA   1 
ATOM   4348 C C    . VAL   B 1 30  ? 49.548 -18.034 -16.361 1.00 19.46 ?  30  VAL   B C    1 
ATOM   4349 O O    . VAL   B 1 30  ? 48.807 -17.332 -17.064 1.00 20.46 ?  30  VAL   B O    1 
ATOM   4350 C CB   . VAL   B 1 30  ? 48.457 -20.170 -15.632 1.00 21.54 ?  30  VAL   B CB   1 
ATOM   4351 C CG1  . VAL   B 1 30  ? 47.165 -19.365 -15.711 1.00 21.77 ?  30  VAL   B CG1  1 
ATOM   4352 C CG2  . VAL   B 1 30  ? 48.221 -21.626 -16.012 1.00 22.11 ?  30  VAL   B CG2  1 
ATOM   4353 H H    . VAL   B 1 30  ? 50.843 -20.519 -15.362 1.00 24.54 ?  30  VAL   B H    1 
ATOM   4354 H HA   . VAL   B 1 30  ? 49.366 -19.789 -17.438 1.00 24.66 ?  30  VAL   B HA   1 
ATOM   4355 H HB   . VAL   B 1 30  ? 48.750 -20.160 -14.708 1.00 25.83 ?  30  VAL   B HB   1 
ATOM   4356 H HG11 . VAL   B 1 30  ? 46.424 -19.945 -15.469 1.00 26.11 ?  30  VAL   B HG11 1 
ATOM   4357 H HG12 . VAL   B 1 30  ? 47.210 -18.623 -15.089 1.00 26.11 ?  30  VAL   B HG12 1 
ATOM   4358 H HG13 . VAL   B 1 30  ? 47.040 -19.047 -16.614 1.00 26.11 ?  30  VAL   B HG13 1 
ATOM   4359 H HG21 . VAL   B 1 30  ? 47.530 -21.999 -15.437 1.00 26.51 ?  30  VAL   B HG21 1 
ATOM   4360 H HG22 . VAL   B 1 30  ? 47.932 -21.669 -16.938 1.00 26.51 ?  30  VAL   B HG22 1 
ATOM   4361 H HG23 . VAL   B 1 30  ? 49.045 -22.120 -15.899 1.00 26.51 ?  30  VAL   B HG23 1 
ATOM   4362 N N    . LYS   B 1 31  ? 50.319 -17.527 -15.420 1.00 18.97 ?  31  LYS   B N    1 
ATOM   4363 C CA   . LYS   B 1 31  ? 50.350 -16.121 -15.056 1.00 19.35 ?  31  LYS   B CA   1 
ATOM   4364 C C    . LYS   B 1 31  ? 48.952 -15.655 -14.661 1.00 17.18 ?  31  LYS   B C    1 
ATOM   4365 O O    . LYS   B 1 31  ? 48.403 -14.738 -15.283 1.00 18.52 ?  31  LYS   B O    1 
ATOM   4366 C CB   . LYS   B 1 31  ? 50.972 -15.298 -16.192 1.00 22.61 ?  31  LYS   B CB   1 
ATOM   4367 C CG   . LYS   B 1 31  ? 52.387 -15.766 -16.587 1.00 25.99 ?  31  LYS   B CG   1 
ATOM   4368 C CD   . LYS   B 1 31  ? 52.978 -14.909 -17.699 1.00 28.70 ?  31  LYS   B CD   1 
ATOM   4369 C CE   . LYS   B 1 31  ? 54.456 -15.189 -17.907 1.00 30.93 ?  31  LYS   B CE   1 
ATOM   4370 N NZ   . LYS   B 1 31  ? 55.221 -14.924 -16.658 1.00 31.95 ?  31  LYS   B NZ   1 
ATOM   4371 H H    . LYS   B 1 31  ? 50.854 -18.011 -14.967 1.00 22.74 ?  31  LYS   B H    1 
ATOM   4372 H HA   . LYS   B 1 31  ? 50.910 -16.037 -14.285 1.00 23.20 ?  31  LYS   B HA   1 
ATOM   4373 H HB2  . LYS   B 1 31  ? 50.411 -15.359 -16.979 1.00 27.11 ?  31  LYS   B HB2  1 
ATOM   4374 H HB3  . LYS   B 1 31  ? 51.038 -14.377 -15.901 1.00 27.11 ?  31  LYS   B HB3  1 
ATOM   4375 H HG2  . LYS   B 1 31  ? 52.961 -15.713 -15.808 1.00 31.17 ?  31  LYS   B HG2  1 
ATOM   4376 H HG3  . LYS   B 1 31  ? 52.338 -16.686 -16.901 1.00 31.17 ?  31  LYS   B HG3  1 
ATOM   4377 H HD2  . LYS   B 1 31  ? 52.513 -15.101 -18.526 1.00 34.42 ?  31  LYS   B HD2  1 
ATOM   4378 H HD3  . LYS   B 1 31  ? 52.875 -13.975 -17.463 1.00 34.42 ?  31  LYS   B HD3  1 
ATOM   4379 H HE2  . LYS   B 1 31  ? 54.586 -16.120 -18.153 1.00 37.09 ?  31  LYS   B HE2  1 
ATOM   4380 H HE3  . LYS   B 1 31  ? 54.804 -14.607 -18.606 1.00 37.09 ?  31  LYS   B HE3  1 
ATOM   4381 H HZ1  . LYS   B 1 31  ? 56.095 -14.954 -16.821 1.00 38.32 ?  31  LYS   B HZ1  1 
ATOM   4382 H HZ2  . LYS   B 1 31  ? 55.014 -14.118 -16.342 1.00 38.32 ?  31  LYS   B HZ2  1 
ATOM   4383 H HZ3  . LYS   B 1 31  ? 55.020 -15.536 -16.044 1.00 38.32 ?  31  LYS   B HZ3  1 
ATOM   4384 N N    . PRO   B 1 32  ? 48.346 -16.261 -13.631 1.00 14.66 ?  32  PRO   B N    1 
ATOM   4385 C CA   . PRO   B 1 32  ? 46.966 -15.909 -13.277 1.00 13.85 ?  32  PRO   B CA   1 
ATOM   4386 C C    . PRO   B 1 32  ? 46.874 -14.564 -12.580 1.00 13.87 ?  32  PRO   B C    1 
ATOM   4387 O O    . PRO   B 1 32  ? 47.796 -14.130 -11.883 1.00 15.25 ?  32  PRO   B O    1 
ATOM   4388 C CB   . PRO   B 1 32  ? 46.567 -17.027 -12.308 1.00 13.95 ?  32  PRO   B CB   1 
ATOM   4389 C CG   . PRO   B 1 32  ? 47.862 -17.357 -11.624 1.00 14.57 ?  32  PRO   B CG   1 
ATOM   4390 C CD   . PRO   B 1 32  ? 48.903 -17.265 -12.704 1.00 14.85 ?  32  PRO   B CD   1 
ATOM   4391 H HA   . PRO   B 1 32  ? 46.381 -15.924 -14.056 1.00 16.59 ?  32  PRO   B HA   1 
ATOM   4392 H HB2  . PRO   B 1 32  ? 45.907 -16.702 -11.671 1.00 16.72 ?  32  PRO   B HB2  1 
ATOM   4393 H HB3  . PRO   B 1 32  ? 46.226 -17.793 -12.798 1.00 16.72 ?  32  PRO   B HB3  1 
ATOM   4394 H HG2  . PRO   B 1 32  ? 48.037 -16.706 -10.923 1.00 17.46 ?  32  PRO   B HG2  1 
ATOM   4395 H HG3  . PRO   B 1 32  ? 47.824 -18.253 -11.256 1.00 17.46 ?  32  PRO   B HG3  1 
ATOM   4396 H HD2  . PRO   B 1 32  ? 49.740 -16.953 -12.333 1.00 17.80 ?  32  PRO   B HD2  1 
ATOM   4397 H HD3  . PRO   B 1 32  ? 48.998 -18.122 -13.143 1.00 17.80 ?  32  PRO   B HD3  1 
ATOM   4398 N N    . THR   B 1 33  ? 45.721 -13.913 -12.754 1.00 13.50 ?  33  THR   B N    1 
ATOM   4399 C CA   . THR   B 1 33  ? 45.415 -12.739 -11.947 1.00 13.41 ?  33  THR   B CA   1 
ATOM   4400 C C    . THR   B 1 33  ? 45.370 -13.091 -10.469 1.00 13.15 ?  33  THR   B C    1 
ATOM   4401 O O    . THR   B 1 33  ? 45.837 -12.311 -9.626  1.00 14.24 ?  33  THR   B O    1 
ATOM   4402 C CB   . THR   B 1 33  ? 44.093 -12.119 -12.401 1.00 14.15 ?  33  THR   B CB   1 
ATOM   4403 O OG1  . THR   B 1 33  ? 44.157 -11.855 -13.802 1.00 14.20 ?  33  THR   B OG1  1 
ATOM   4404 C CG2  . THR   B 1 33  ? 43.823 -10.822 -11.651 1.00 15.32 ?  33  THR   B CG2  1 
ATOM   4405 H H    . THR   B 1 33  ? 45.108 -14.131 -13.320 1.00 16.17 ?  33  THR   B H    1 
ATOM   4406 H HA   . THR   B 1 33  ? 46.109 -12.082 -12.072 1.00 16.07 ?  33  THR   B HA   1 
ATOM   4407 H HB   . THR   B 1 33  ? 43.362 -12.735 -12.216 1.00 16.96 ?  33  THR   B HB   1 
ATOM   4408 H HG1  . THR   B 1 33  ? 43.431 -11.497 -14.061 1.00 17.02 ?  33  THR   B HG1  1 
ATOM   4409 H HG21 . THR   B 1 33  ? 43.068 -10.364 -12.044 1.00 18.37 ?  33  THR   B HG21 1 
ATOM   4410 H HG22 . THR   B 1 33  ? 43.631 -11.010 -10.718 1.00 18.37 ?  33  THR   B HG22 1 
ATOM   4411 H HG23 . THR   B 1 33  ? 44.604 -10.248 -11.701 1.00 18.37 ?  33  THR   B HG23 1 
ATOM   4412 N N    . VAL   B 1 34  ? 44.827 -14.265 -10.131 1.00 12.26 ?  34  VAL   B N    1 
ATOM   4413 C CA   . VAL   B 1 34  ? 44.637 -14.661 -8.741  1.00 11.69 ?  34  VAL   B CA   1 
ATOM   4414 C C    . VAL   B 1 34  ? 45.067 -16.105 -8.580  1.00 11.07 ?  34  VAL   B C    1 
ATOM   4415 O O    . VAL   B 1 34  ? 44.553 -16.991 -9.272  1.00 11.85 ?  34  VAL   B O    1 
ATOM   4416 C CB   . VAL   B 1 34  ? 43.165 -14.527 -8.300  1.00 13.03 ?  34  VAL   B CB   1 
ATOM   4417 C CG1  . VAL   B 1 34  ? 42.999 -14.968 -6.861  1.00 13.68 ?  34  VAL   B CG1  1 
ATOM   4418 C CG2  . VAL   B 1 34  ? 42.665 -13.099 -8.486  1.00 14.14 ?  34  VAL   B CG2  1 
ATOM   4419 H H    . VAL   B 1 34  ? 44.564 -14.863 -10.695 1.00 14.69 ?  34  VAL   B H    1 
ATOM   4420 H HA   . VAL   B 1 34  ? 45.183 -14.108 -8.160  1.00 14.00 ?  34  VAL   B HA   1 
ATOM   4421 H HB   . VAL   B 1 34  ? 42.616 -15.106 -8.854  1.00 15.62 ?  34  VAL   B HB   1 
ATOM   4422 H HG11 . VAL   B 1 34  ? 42.137 -14.655 -6.532  1.00 16.40 ?  34  VAL   B HG11 1 
ATOM   4423 H HG12 . VAL   B 1 34  ? 43.026 -15.939 -6.819  1.00 16.40 ?  34  VAL   B HG12 1 
ATOM   4424 H HG13 . VAL   B 1 34  ? 43.710 -14.590 -6.328  1.00 16.40 ?  34  VAL   B HG13 1 
ATOM   4425 H HG21 . VAL   B 1 34  ? 41.744 -13.041 -8.178  1.00 16.95 ?  34  VAL   B HG21 1 
ATOM   4426 H HG22 . VAL   B 1 34  ? 43.223 -12.498 -7.971  1.00 16.95 ?  34  VAL   B HG22 1 
ATOM   4427 H HG23 . VAL   B 1 34  ? 42.709 -12.868 -9.428  1.00 16.95 ?  34  VAL   B HG23 1 
ATOM   4428 N N    . VAL   B 1 35  ? 45.967 -16.352 -7.634  1.00 10.74 ?  35  VAL   B N    1 
ATOM   4429 C CA   . VAL   B 1 35  ? 46.214 -17.693 -7.121  1.00 10.69 ?  35  VAL   B CA   1 
ATOM   4430 C C    . VAL   B 1 35  ? 45.671 -17.754 -5.701  1.00 10.35 ?  35  VAL   B C    1 
ATOM   4431 O O    . VAL   B 1 35  ? 45.883 -16.829 -4.907  1.00 10.61 ?  35  VAL   B O    1 
ATOM   4432 C CB   . VAL   B 1 35  ? 47.699 -18.105 -7.199  1.00 11.37 ?  35  VAL   B CB   1 
ATOM   4433 C CG1  . VAL   B 1 35  ? 48.590 -17.269 -6.273  1.00 12.48 ?  35  VAL   B CG1  1 
ATOM   4434 C CG2  . VAL   B 1 35  ? 47.841 -19.608 -6.883  1.00 12.33 ?  35  VAL   B CG2  1 
ATOM   4435 H H    . VAL   B 1 35  ? 46.463 -15.748 -7.270  1.00 12.87 ?  35  VAL   B H    1 
ATOM   4436 H HA   . VAL   B 1 35  ? 45.708 -18.327 -7.654  1.00 12.80 ?  35  VAL   B HA   1 
ATOM   4437 H HB   . VAL   B 1 35  ? 48.011 -17.975 -8.110  1.00 13.62 ?  35  VAL   B HB   1 
ATOM   4438 H HG11 . VAL   B 1 35  ? 49.518 -17.487 -6.450  1.00 14.95 ?  35  VAL   B HG11 1 
ATOM   4439 H HG12 . VAL   B 1 35  ? 48.425 -16.333 -6.445  1.00 14.95 ?  35  VAL   B HG12 1 
ATOM   4440 H HG13 . VAL   B 1 35  ? 48.371 -17.484 -5.351  1.00 14.95 ?  35  VAL   B HG13 1 
ATOM   4441 H HG21 . VAL   B 1 35  ? 48.766 -19.874 -6.990  1.00 14.77 ?  35  VAL   B HG21 1 
ATOM   4442 H HG22 . VAL   B 1 35  ? 47.555 -19.770 -5.967  1.00 14.77 ?  35  VAL   B HG22 1 
ATOM   4443 H HG23 . VAL   B 1 35  ? 47.279 -20.120 -7.493  1.00 14.77 ?  35  VAL   B HG23 1 
ATOM   4444 N N    . VAL   B 1 36  ? 44.953 -18.836 -5.389  1.00 10.22 ?  36  VAL   B N    1 
ATOM   4445 C CA   . VAL   B 1 36  ? 44.407 -19.043 -4.061  1.00 10.05 ?  36  VAL   B CA   1 
ATOM   4446 C C    . VAL   B 1 36  ? 45.413 -19.803 -3.209  1.00 10.03 ?  36  VAL   B C    1 
ATOM   4447 O O    . VAL   B 1 36  ? 45.950 -20.838 -3.629  1.00 10.90 ?  36  VAL   B O    1 
ATOM   4448 C CB   . VAL   B 1 36  ? 43.075 -19.804 -4.138  1.00 10.55 ?  36  VAL   B CB   1 
ATOM   4449 C CG1  . VAL   B 1 36  ? 42.575 -20.166 -2.749  1.00 11.51 ?  36  VAL   B CG1  1 
ATOM   4450 C CG2  . VAL   B 1 36  ? 42.045 -18.967 -4.871  1.00 10.93 ?  36  VAL   B CG2  1 
ATOM   4451 H H    . VAL   B 1 36  ? 44.775 -19.474 -5.942  1.00 12.24 ?  36  VAL   B H    1 
ATOM   4452 H HA   . VAL   B 1 36  ? 44.243 -18.183 -3.644  1.00 12.04 ?  36  VAL   B HA   1 
ATOM   4453 H HB   . VAL   B 1 36  ? 43.205 -20.627 -4.635  1.00 12.63 ?  36  VAL   B HB   1 
ATOM   4454 H HG11 . VAL   B 1 36  ? 41.634 -20.401 -2.806  1.00 13.79 ?  36  VAL   B HG11 1 
ATOM   4455 H HG12 . VAL   B 1 36  ? 43.083 -20.915 -2.410  1.00 13.79 ?  36  VAL   B HG12 1 
ATOM   4456 H HG13 . VAL   B 1 36  ? 42.684 -19.396 -2.166  1.00 13.79 ?  36  VAL   B HG13 1 
ATOM   4457 H HG21 . VAL   B 1 36  ? 41.203 -19.446 -4.896  1.00 13.09 ?  36  VAL   B HG21 1 
ATOM   4458 H HG22 . VAL   B 1 36  ? 41.933 -18.123 -4.406  1.00 13.09 ?  36  VAL   B HG22 1 
ATOM   4459 H HG23 . VAL   B 1 36  ? 42.357 -18.803 -5.778  1.00 13.09 ?  36  VAL   B HG23 1 
ATOM   4460 N N    . ASN   B 1 37  ? 45.630 -19.315 -1.994  1.00 10.04 ?  37  ASN   B N    1 
ATOM   4461 C CA   . ASN   B 1 37  ? 46.387 -20.040 -0.990  1.00 10.69 ?  37  ASN   B CA   1 
ATOM   4462 C C    . ASN   B 1 37  ? 45.444 -20.715 -0.000  1.00 10.63 ?  37  ASN   B C    1 
ATOM   4463 O O    . ASN   B 1 37  ? 44.434 -20.138 0.415   1.00 10.96 ?  37  ASN   B O    1 
ATOM   4464 C CB   . ASN   B 1 37  ? 47.324 -19.096 -0.239  1.00 10.64 ?  37  ASN   B CB   1 
ATOM   4465 C CG   . ASN   B 1 37  ? 48.168 -19.815 0.779   1.00 10.85 ?  37  ASN   B CG   1 
ATOM   4466 O OD1  . ASN   B 1 37  ? 48.513 -20.986 0.598   1.00 11.46 ?  37  ASN   B OD1  1 
ATOM   4467 N ND2  . ASN   B 1 37  ? 48.515 -19.120 1.857   1.00 11.10 ?  37  ASN   B ND2  1 
ATOM   4468 H H    . ASN   B 1 37  ? 45.340 -18.554 -1.717  1.00 12.03 ?  37  ASN   B H    1 
ATOM   4469 H HA   . ASN   B 1 37  ? 46.924 -20.729 -1.413  1.00 12.80 ?  37  ASN   B HA   1 
ATOM   4470 H HB2  . ASN   B 1 37  ? 47.923 -18.675 -0.875  1.00 12.74 ?  37  ASN   B HB2  1 
ATOM   4471 H HB3  . ASN   B 1 37  ? 46.802 -18.427 0.225   1.00 12.74 ?  37  ASN   B HB3  1 
ATOM   4472 H HD21 . ASN   B 1 37  ? 48.994 -19.492 2.471   1.00 13.29 ?  37  ASN   B HD21 1 
ATOM   4473 H HD22 . ASN   B 1 37  ? 48.255 -18.314 1.953   1.00 13.29 ?  37  ASN   B HD22 1 
ATOM   4474 N N    . ALA   B 1 38  ? 45.800 -21.943 0.376   1.00 10.52 ?  38  ALA   B N    1 
ATOM   4475 C CA   . ALA   B 1 38  ? 45.141 -22.691 1.445   1.00 11.12 ?  38  ALA   B CA   1 
ATOM   4476 C C    . ALA   B 1 38  ? 45.720 -22.209 2.772   1.00 10.96 ?  38  ALA   B C    1 
ATOM   4477 O O    . ALA   B 1 38  ? 46.622 -22.818 3.355   1.00 11.87 ?  38  ALA   B O    1 
ATOM   4478 C CB   . ALA   B 1 38  ? 45.356 -24.188 1.254   1.00 12.20 ?  38  ALA   B CB   1 
ATOM   4479 H H    . ALA   B 1 38  ? 46.450 -22.378 0.020   1.00 12.60 ?  38  ALA   B H    1 
ATOM   4480 H HA   . ALA   B 1 38  ? 44.187 -22.509 1.437   1.00 13.32 ?  38  ALA   B HA   1 
ATOM   4481 H HB1  . ALA   B 1 38  ? 44.903 -24.668 1.975   1.00 14.62 ?  38  ALA   B HB1  1 
ATOM   4482 H HB2  . ALA   B 1 38  ? 44.974 -24.457 0.402   1.00 14.62 ?  38  ALA   B HB2  1 
ATOM   4483 H HB3  . ALA   B 1 38  ? 46.300 -24.383 1.274   1.00 14.62 ?  38  ALA   B HB3  1 
ATOM   4484 N N    . ALA   B 1 39  ? 45.203 -21.069 3.230   1.00 10.52 ?  39  ALA   B N    1 
ATOM   4485 C CA   . ALA   B 1 39  ? 45.744 -20.335 4.362   1.00 11.04 ?  39  ALA   B CA   1 
ATOM   4486 C C    . ALA   B 1 39  ? 45.130 -20.787 5.684   1.00 11.04 ?  39  ALA   B C    1 
ATOM   4487 O O    . ALA   B 1 39  ? 44.106 -21.470 5.731   1.00 11.82 ?  39  ALA   B O    1 
ATOM   4488 C CB   . ALA   B 1 39  ? 45.493 -18.836 4.169   1.00 11.63 ?  39  ALA   B CB   1 
ATOM   4489 H H    . ALA   B 1 39  ? 44.506 -20.692 2.883   1.00 12.60 ?  39  ALA   B H    1 
ATOM   4490 H HA   . ALA   B 1 39  ? 46.695 -20.477 4.407   1.00 13.22 ?  39  ALA   B HA   1 
ATOM   4491 H HB1  . ALA   B 1 39  ? 45.858 -18.354 4.928   1.00 13.93 ?  39  ALA   B HB1  1 
ATOM   4492 H HB2  . ALA   B 1 39  ? 45.932 -18.544 3.352   1.00 13.93 ?  39  ALA   B HB2  1 
ATOM   4493 H HB3  . ALA   B 1 39  ? 44.538 -18.675 4.105   1.00 13.93 ?  39  ALA   B HB3  1 
ATOM   4494 N N    . ASN   B 1 40  ? 45.765 -20.359 6.772   1.00 12.06 ?  40  ASN   B N    1 
ATOM   4495 C CA   . ASN   B 1 40  ? 45.203 -20.417 8.110   1.00 12.50 ?  40  ASN   B CA   1 
ATOM   4496 C C    . ASN   B 1 40  ? 45.029 -18.994 8.641   1.00 12.14 ?  40  ASN   B C    1 
ATOM   4497 O O    . ASN   B 1 40  ? 45.443 -18.010 8.014   1.00 12.25 ?  40  ASN   B O    1 
ATOM   4498 C CB   . ASN   B 1 40  ? 46.051 -21.298 9.045   1.00 13.69 ?  40  ASN   B CB   1 
ATOM   4499 C CG   . ASN   B 1 40  ? 47.508 -20.895 9.070   1.00 14.52 ?  40  ASN   B CG   1 
ATOM   4500 O OD1  . ASN   B 1 40  ? 47.833 -19.715 9.119   1.00 16.41 ?  40  ASN   B OD1  1 
ATOM   4501 N ND2  . ASN   B 1 40  ? 48.400 -21.875 9.040   1.00 14.74 ?  40  ASN   B ND2  1 
ATOM   4502 H H    . ASN   B 1 40  ? 46.553 -20.018 6.748   1.00 14.45 ?  40  ASN   B H    1 
ATOM   4503 H HA   . ASN   B 1 40  ? 44.321 -20.814 8.061   1.00 14.98 ?  40  ASN   B HA   1 
ATOM   4504 H HB2  . ASN   B 1 40  ? 45.705 -21.223 9.950   1.00 16.41 ?  40  ASN   B HB2  1 
ATOM   4505 H HB3  . ASN   B 1 40  ? 46.001 -22.217 8.746   1.00 16.41 ?  40  ASN   B HB3  1 
ATOM   4506 H HD21 . ASN   B 1 40  ? 49.243 -21.694 9.055   1.00 17.66 ?  40  ASN   B HD21 1 
ATOM   4507 H HD22 . ASN   B 1 40  ? 48.141 -22.694 9.004   1.00 17.66 ?  40  ASN   B HD22 1 
ATOM   4508 N N    . VAL   B 1 41  ? 44.370 -18.875 9.794   1.00 12.73 ?  41  VAL   B N    1 
ATOM   4509 C CA   . VAL   B 1 41  ? 43.919 -17.553 10.237  1.00 13.69 ?  41  VAL   B CA   1 
ATOM   4510 C C    . VAL   B 1 41  ? 45.074 -16.607 10.544  1.00 13.58 ?  41  VAL   B C    1 
ATOM   4511 O O    . VAL   B 1 41  ? 44.899 -15.386 10.482  1.00 13.84 ?  41  VAL   B O    1 
ATOM   4512 C CB   . VAL   B 1 41  ? 42.932 -17.619 11.418  1.00 14.85 ?  41  VAL   B CB   1 
ATOM   4513 C CG1  . VAL   B 1 41  ? 41.632 -18.300 11.000  1.00 15.46 ?  41  VAL   B CG1  1 
ATOM   4514 C CG2  . VAL   B 1 41  ? 43.561 -18.296 12.624  1.00 15.74 ?  41  VAL   B CG2  1 
ATOM   4515 H H    . VAL   B 1 41  ? 44.179 -19.518 10.324  1.00 15.25 ?  41  VAL   B H    1 
ATOM   4516 H HA   . VAL   B 1 41  ? 43.432 -17.152 9.502   1.00 16.41 ?  41  VAL   B HA   1 
ATOM   4517 H HB   . VAL   B 1 41  ? 42.710 -16.710 11.682  1.00 17.80 ?  41  VAL   B HB   1 
ATOM   4518 H HG11 . VAL   B 1 41  ? 41.015 -18.291 11.749  1.00 18.53 ?  41  VAL   B HG11 1 
ATOM   4519 H HG12 . VAL   B 1 41  ? 41.249 -17.818 10.250  1.00 18.53 ?  41  VAL   B HG12 1 
ATOM   4520 H HG13 . VAL   B 1 41  ? 41.825 -19.214 10.741  1.00 18.53 ?  41  VAL   B HG13 1 
ATOM   4521 H HG21 . VAL   B 1 41  ? 42.909 -18.332 13.340  1.00 18.86 ?  41  VAL   B HG21 1 
ATOM   4522 H HG22 . VAL   B 1 41  ? 43.829 -19.195 12.376  1.00 18.86 ?  41  VAL   B HG22 1 
ATOM   4523 H HG23 . VAL   B 1 41  ? 44.335 -17.785 12.906  1.00 18.86 ?  41  VAL   B HG23 1 
ATOM   4524 N N    . TYR   B 1 42  ? 46.240 -17.126 10.921  1.00 13.75 ?  42  TYR   B N    1 
ATOM   4525 C CA   . TYR   B 1 42  ? 47.394 -16.278 11.197  1.00 14.32 ?  42  TYR   B CA   1 
ATOM   4526 C C    . TYR   B 1 42  ? 48.361 -16.199 10.019  1.00 13.64 ?  42  TYR   B C    1 
ATOM   4527 O O    . TYR   B 1 42  ? 49.454 -15.635 10.160  1.00 14.69 ?  42  TYR   B O    1 
ATOM   4528 C CB   . TYR   B 1 42  ? 48.090 -16.685 12.505  1.00 16.43 ?  42  TYR   B CB   1 
ATOM   4529 C CG   . TYR   B 1 42  ? 47.486 -16.007 13.730  1.00 17.24 ?  42  TYR   B CG   1 
ATOM   4530 C CD1  . TYR   B 1 42  ? 47.712 -14.655 13.976  1.00 16.67 ?  42  TYR   B CD1  1 
ATOM   4531 C CD2  . TYR   B 1 42  ? 46.687 -16.706 14.625  1.00 19.14 ?  42  TYR   B CD2  1 
ATOM   4532 C CE1  . TYR   B 1 42  ? 47.163 -14.021 15.077  1.00 17.60 ?  42  TYR   B CE1  1 
ATOM   4533 C CE2  . TYR   B 1 42  ? 46.135 -16.081 15.733  1.00 19.00 ?  42  TYR   B CE2  1 
ATOM   4534 C CZ   . TYR   B 1 42  ? 46.377 -14.736 15.952  1.00 19.34 ?  42  TYR   B CZ   1 
ATOM   4535 O OH   . TYR   B 1 42  ? 45.835 -14.104 17.052  1.00 21.99 ?  42  TYR   B OH   1 
ATOM   4536 H H    . TYR   B 1 42  ? 46.386 -17.971 11.016  1.00 16.48 ?  42  TYR   B H    1 
ATOM   4537 H HA   . TYR   B 1 42  ? 47.065 -15.381 11.336  1.00 17.16 ?  42  TYR   B HA   1 
ATOM   4538 H HB2  . TYR   B 1 42  ? 48.009 -17.645 12.622  1.00 19.69 ?  42  TYR   B HB2  1 
ATOM   4539 H HB3  . TYR   B 1 42  ? 49.027 -16.436 12.453  1.00 19.69 ?  42  TYR   B HB3  1 
ATOM   4540 H HD1  . TYR   B 1 42  ? 48.246 -14.168 13.383  1.00 19.98 ?  42  TYR   B HD1  1 
ATOM   4541 H HD2  . TYR   B 1 42  ? 46.520 -17.610 14.477  1.00 22.95 ?  42  TYR   B HD2  1 
ATOM   4542 H HE1  . TYR   B 1 42  ? 47.330 -13.117 15.225  1.00 21.10 ?  42  TYR   B HE1  1 
ATOM   4543 H HE2  . TYR   B 1 42  ? 45.602 -16.561 16.324  1.00 22.78 ?  42  TYR   B HE2  1 
ATOM   4544 H HH   . TYR   B 1 42  ? 46.062 -13.295 17.057  1.00 26.37 ?  42  TYR   B HH   1 
ATOM   4545 N N    . LEU   B 1 43  ? 47.961 -16.706 8.855   1.00 12.57 ?  43  LEU   B N    1 
ATOM   4546 C CA   . LEU   B 1 43  ? 48.775 -16.633 7.646   1.00 12.32 ?  43  LEU   B CA   1 
ATOM   4547 C C    . LEU   B 1 43  ? 50.186 -17.139 7.908   1.00 12.64 ?  43  LEU   B C    1 
ATOM   4548 O O    . LEU   B 1 43  ? 51.169 -16.539 7.473   1.00 13.48 ?  43  LEU   B O    1 
ATOM   4549 C CB   . LEU   B 1 43  ? 48.795 -15.229 7.039   1.00 12.68 ?  43  LEU   B CB   1 
ATOM   4550 C CG   . LEU   B 1 43  ? 47.437 -14.613 6.671   1.00 13.03 ?  43  LEU   B CG   1 
ATOM   4551 C CD1  . LEU   B 1 43  ? 47.644 -13.211 6.101   1.00 14.05 ?  43  LEU   B CD1  1 
ATOM   4552 C CD2  . LEU   B 1 43  ? 46.669 -15.500 5.693   1.00 13.09 ?  43  LEU   B CD2  1 
ATOM   4553 H H    . LEU   B 1 43  ? 47.214 -17.115 8.735   1.00 15.06 ?  43  LEU   B H    1 
ATOM   4554 H HA   . LEU   B 1 43  ? 48.381 -17.219 6.980   1.00 14.76 ?  43  LEU   B HA   1 
ATOM   4555 H HB2  . LEU   B 1 43  ? 49.219 -14.628 7.670   1.00 15.19 ?  43  LEU   B HB2  1 
ATOM   4556 H HB3  . LEU   B 1 43  ? 49.323 -15.259 6.223   1.00 15.19 ?  43  LEU   B HB3  1 
ATOM   4557 H HG   . LEU   B 1 43  ? 46.906 -14.529 7.473   1.00 15.62 ?  43  LEU   B HG   1 
ATOM   4558 H HD11 . LEU   B 1 43  ? 46.780 -12.832 5.873   1.00 16.83 ?  43  LEU   B HD11 1 
ATOM   4559 H HD12 . LEU   B 1 43  ? 48.079 -12.659 6.771   1.00 16.83 ?  43  LEU   B HD12 1 
ATOM   4560 H HD13 . LEU   B 1 43  ? 48.200 -13.267 5.308   1.00 16.83 ?  43  LEU   B HD13 1 
ATOM   4561 H HD21 . LEU   B 1 43  ? 45.863 -15.038 5.409   1.00 15.68 ?  43  LEU   B HD21 1 
ATOM   4562 H HD22 . LEU   B 1 43  ? 47.228 -15.686 4.921   1.00 15.68 ?  43  LEU   B HD22 1 
ATOM   4563 H HD23 . LEU   B 1 43  ? 46.433 -16.331 6.135   1.00 15.68 ?  43  LEU   B HD23 1 
ATOM   4564 N N    . LYS   B 1 44  ? 50.282 -18.265 8.619   1.00 12.57 ?  44  LYS   B N    1 
ATOM   4565 C CA   . LYS   B 1 44  ? 51.547 -18.943 8.861   1.00 13.48 ?  44  LYS   B CA   1 
ATOM   4566 C C    . LYS   B 1 44  ? 51.666 -20.056 7.831   1.00 12.77 ?  44  LYS   B C    1 
ATOM   4567 O O    . LYS   B 1 44  ? 50.963 -21.070 7.908   1.00 13.64 ?  44  LYS   B O    1 
ATOM   4568 C CB   . LYS   B 1 44  ? 51.602 -19.461 10.298  1.00 15.04 ?  44  LYS   B CB   1 
ATOM   4569 C CG   . LYS   B 1 44  ? 51.798 -18.348 11.322  1.00 17.76 ?  44  LYS   B CG   1 
ATOM   4570 C CD   . LYS   B 1 44  ? 53.025 -17.513 10.955  1.00 20.62 ?  44  LYS   B CD   1 
ATOM   4571 C CE   . LYS   B 1 44  ? 53.435 -16.551 12.038  1.00 23.24 ?  44  LYS   B CE   1 
ATOM   4572 N NZ   . LYS   B 1 44  ? 54.659 -15.787 11.672  1.00 24.53 ?  44  LYS   B NZ   1 
ATOM   4573 H H    . LYS   B 1 44  ? 49.607 -18.654 8.984   1.00 15.06 ?  44  LYS   B H    1 
ATOM   4574 H HA   . LYS   B 1 44  ? 52.279 -18.329 8.703   1.00 16.15 ?  44  LYS   B HA   1 
ATOM   4575 H HB2  . LYS   B 1 44  ? 50.763 -19.909 10.504  1.00 18.02 ?  44  LYS   B HB2  1 
ATOM   4576 H HB3  . LYS   B 1 44  ? 52.338 -20.081 10.386  1.00 18.02 ?  44  LYS   B HB3  1 
ATOM   4577 H HG2  . LYS   B 1 44  ? 51.019 -17.773 11.331  1.00 21.29 ?  44  LYS   B HG2  1 
ATOM   4578 H HG3  . LYS   B 1 44  ? 51.942 -18.741 12.201  1.00 21.29 ?  44  LYS   B HG3  1 
ATOM   4579 H HD2  . LYS   B 1 44  ? 53.766 -18.118 10.765  1.00 24.72 ?  44  LYS   B HD2  1 
ATOM   4580 H HD3  . LYS   B 1 44  ? 52.819 -16.989 10.165  1.00 24.72 ?  44  LYS   B HD3  1 
ATOM   4581 H HE2  . LYS   B 1 44  ? 52.717 -15.918 12.175  1.00 27.86 ?  44  LYS   B HE2  1 
ATOM   4582 H HE3  . LYS   B 1 44  ? 53.616 -17.046 12.847  1.00 27.86 ?  44  LYS   B HE3  1 
ATOM   4583 H HZ1  . LYS   B 1 44  ? 54.871 -15.223 12.327  1.00 29.41 ?  44  LYS   B HZ1  1 
ATOM   4584 H HZ2  . LYS   B 1 44  ? 55.341 -16.343 11.537  1.00 29.41 ?  44  LYS   B HZ2  1 
ATOM   4585 H HZ3  . LYS   B 1 44  ? 54.518 -15.319 10.925  1.00 29.41 ?  44  LYS   B HZ3  1 
ATOM   4586 N N    . HIS   B 1 45  ? 52.520 -19.838 6.836   1.00 12.30 ?  45  HIS   B N    1 
ATOM   4587 C CA   . HIS   B 1 45  ? 52.542 -20.668 5.633   1.00 12.55 ?  45  HIS   B CA   1 
ATOM   4588 C C    . HIS   B 1 45  ? 53.558 -21.790 5.798   1.00 14.67 ?  45  HIS   B C    1 
ATOM   4589 O O    . HIS   B 1 45  ? 54.626 -21.800 5.195   1.00 16.83 ?  45  HIS   B O    1 
ATOM   4590 C CB   . HIS   B 1 45  ? 52.858 -19.816 4.417   1.00 12.39 ?  45  HIS   B CB   1 
ATOM   4591 C CG   . HIS   B 1 45  ? 51.987 -18.614 4.304   1.00 12.28 ?  45  HIS   B CG   1 
ATOM   4592 N ND1  . HIS   B 1 45  ? 50.609 -18.689 4.259   1.00 12.66 ?  45  HIS   B ND1  1 
ATOM   4593 C CD2  . HIS   B 1 45  ? 52.306 -17.300 4.249   1.00 13.28 ?  45  HIS   B CD2  1 
ATOM   4594 C CE1  . HIS   B 1 45  ? 50.126 -17.465 4.159   1.00 12.41 ?  45  HIS   B CE1  1 
ATOM   4595 N NE2  . HIS   B 1 45  ? 51.131 -16.605 4.152   1.00 12.98 ?  45  HIS   B NE2  1 
ATOM   4596 H H    . HIS   B 1 45  ? 53.099 -19.201 6.828   1.00 14.74 ?  45  HIS   B H    1 
ATOM   4597 H HA   . HIS   B 1 45  ? 51.663 -21.063 5.503   1.00 15.04 ?  45  HIS   B HA   1 
ATOM   4598 H HB2  . HIS   B 1 45  ? 53.778 -19.521 4.467   1.00 14.84 ?  45  HIS   B HB2  1 
ATOM   4599 H HB3  . HIS   B 1 45  ? 52.731 -20.357 3.614   1.00 14.84 ?  45  HIS   B HB3  1 
ATOM   4600 H HD2  . HIS   B 1 45  ? 53.165 -16.938 4.264   1.00 15.91 ?  45  HIS   B HD2  1 
ATOM   4601 H HE1  . HIS   B 1 45  ? 49.225 -17.246 4.096   1.00 14.87 ?  45  HIS   B HE1  1 
ATOM   4602 H HE2  . HIS   B 1 45  ? 51.057 -15.751 4.099   1.00 15.55 ?  45  HIS   B HE2  1 
ATOM   4603 N N    A GLY   B 1 46  ? 53.190 -22.760 6.629   0.60 15.94 ?  46  GLY   B N    1 
ATOM   4604 N N    B GLY   B 1 46  ? 53.196 -22.748 6.643   0.40 15.81 ?  46  GLY   B N    1 
ATOM   4605 C CA   A GLY   B 1 46  ? 54.109 -23.821 6.995   0.60 17.46 ?  46  GLY   B CA   1 
ATOM   4606 C CA   B GLY   B 1 46  ? 54.106 -23.822 6.979   0.40 17.05 ?  46  GLY   B CA   1 
ATOM   4607 C C    A GLY   B 1 46  ? 54.153 -25.032 6.085   0.60 19.18 ?  46  GLY   B C    1 
ATOM   4608 C C    B GLY   B 1 46  ? 54.138 -24.969 5.990   0.40 18.45 ?  46  GLY   B C    1 
ATOM   4609 O O    A GLY   B 1 46  ? 55.232 -25.450 5.655   0.60 21.91 ?  46  GLY   B O    1 
ATOM   4610 O O    B GLY   B 1 46  ? 55.180 -25.259 5.394   0.40 19.89 ?  46  GLY   B O    1 
ATOM   4611 H H    A GLY   B 1 46  ? 52.419 -22.812 7.011   0.60 19.11 ?  46  GLY   B H    1 
ATOM   4612 H H    B GLY   B 1 46  ? 52.433 -22.787 7.045   0.40 18.95 ?  46  GLY   B H    1 
ATOM   4613 H HA2  A GLY   B 1 46  ? 55.005 -23.453 7.039   0.60 20.93 ?  46  GLY   B HA2  1 
ATOM   4614 H HA2  B GLY   B 1 46  ? 55.003 -23.462 7.046   0.40 20.43 ?  46  GLY   B HA2  1 
ATOM   4615 H HA3  A GLY   B 1 46  ? 53.876 -24.143 7.878   0.60 20.93 ?  46  GLY   B HA3  1 
ATOM   4616 H HA3  B GLY   B 1 46  ? 53.861 -24.183 7.844   0.40 20.43 ?  46  GLY   B HA3  1 
ATOM   4617 N N    . GLY   B 1 47  ? 52.998 -25.631 5.800   1.00 18.63 ?  47  GLY   B N    1 
ATOM   4618 C CA   . GLY   B 1 47  ? 52.946 -26.893 5.092   1.00 16.01 ?  47  GLY   B CA   1 
ATOM   4619 C C    . GLY   B 1 47  ? 52.038 -26.864 3.880   1.00 14.23 ?  47  GLY   B C    1 
ATOM   4620 O O    . GLY   B 1 47  ? 51.394 -25.857 3.584   1.00 13.98 ?  47  GLY   B O    1 
ATOM   4621 H H    A GLY   B 1 47  ? 52.226 -25.329 6.029   0.60 22.33 ?  47  GLY   B H    1 
ATOM   4622 H H    B GLY   B 1 47  ? 52.232 -25.362 6.083   0.40 22.33 ?  47  GLY   B H    1 
ATOM   4623 H HA2  . GLY   B 1 47  ? 53.835 -27.140 4.793   1.00 19.19 ?  47  GLY   B HA2  1 
ATOM   4624 H HA3  . GLY   B 1 47  ? 52.627 -27.582 5.694   1.00 19.19 ?  47  GLY   B HA3  1 
ATOM   4625 N N    . GLY   B 1 48  ? 51.991 -28.003 3.190   1.00 12.93 ?  48  GLY   B N    1 
ATOM   4626 C CA   . GLY   B 1 48  ? 51.076 -28.147 2.077   1.00 12.87 ?  48  GLY   B CA   1 
ATOM   4627 C C    . GLY   B 1 48  ? 51.217 -27.037 1.066   1.00 12.30 ?  48  GLY   B C    1 
ATOM   4628 O O    . GLY   B 1 48  ? 52.323 -26.568 0.765   1.00 12.88 ?  48  GLY   B O    1 
ATOM   4629 H H    . GLY   B 1 48  ? 52.480 -28.691 3.340   1.00 15.49 ?  48  GLY   B H    1 
ATOM   4630 H HA2  . GLY   B 1 48  ? 51.240 -28.992 1.629   1.00 15.42 ?  48  GLY   B HA2  1 
ATOM   4631 H HA3  . GLY   B 1 48  ? 50.164 -28.144 2.403   1.00 15.42 ?  48  GLY   B HA3  1 
ATOM   4632 N N    . VAL   B 1 49  ? 50.070 -26.604 0.537   1.00 12.22 ?  49  VAL   B N    1 
ATOM   4633 C CA   . VAL   B 1 49  ? 50.047 -25.581 -0.503  1.00 12.16 ?  49  VAL   B CA   1 
ATOM   4634 C C    . VAL   B 1 49  ? 50.699 -24.292 -0.015  1.00 11.81 ?  49  VAL   B C    1 
ATOM   4635 O O    . VAL   B 1 49  ? 51.495 -23.676 -0.731  1.00 12.69 ?  49  VAL   B O    1 
ATOM   4636 C CB   . VAL   B 1 49  ? 48.604 -25.333 -0.982  1.00 13.52 ?  49  VAL   B CB   1 
ATOM   4637 C CG1  . VAL   B 1 49  ? 48.529 -24.069 -1.838  1.00 13.69 ?  49  VAL   B CG1  1 
ATOM   4638 C CG2  . VAL   B 1 49  ? 48.076 -26.534 -1.751  1.00 14.90 ?  49  VAL   B CG2  1 
ATOM   4639 H H    . VAL   B 1 49  ? 49.286 -26.889 0.758   1.00 14.64 ?  49  VAL   B H    1 
ATOM   4640 H HA   . VAL   B 1 49  ? 50.553 -25.891 -1.267  1.00 14.56 ?  49  VAL   B HA   1 
ATOM   4641 H HB   . VAL   B 1 49  ? 48.032 -25.197 -0.211  1.00 16.20 ?  49  VAL   B HB   1 
ATOM   4642 H HG11 . VAL   B 1 49  ? 47.704 -24.084 -2.350  1.00 16.40 ?  49  VAL   B HG11 1 
ATOM   4643 H HG12 . VAL   B 1 49  ? 48.538 -23.289 -1.259  1.00 16.40 ?  49  VAL   B HG12 1 
ATOM   4644 H HG13 . VAL   B 1 49  ? 49.288 -24.047 -2.439  1.00 16.40 ?  49  VAL   B HG13 1 
ATOM   4645 H HG21 . VAL   B 1 49  ? 47.167 -26.354 -2.037  1.00 17.86 ?  49  VAL   B HG21 1 
ATOM   4646 H HG22 . VAL   B 1 49  ? 48.642 -26.683 -2.527  1.00 17.86 ?  49  VAL   B HG22 1 
ATOM   4647 H HG23 . VAL   B 1 49  ? 48.096 -27.309 -1.172  1.00 17.86 ?  49  VAL   B HG23 1 
ATOM   4648 N N    . ALA   B 1 50  ? 50.368 -23.858 1.203   1.00 11.53 ?  50  ALA   B N    1 
ATOM   4649 C CA   . ALA   B 1 50  ? 50.884 -22.578 1.679   1.00 11.62 ?  50  ALA   B CA   1 
ATOM   4650 C C    . ALA   B 1 50  ? 52.401 -22.605 1.794   1.00 11.79 ?  50  ALA   B C    1 
ATOM   4651 O O    . ALA   B 1 50  ? 53.075 -21.628 1.443   1.00 11.75 ?  50  ALA   B O    1 
ATOM   4652 C CB   . ALA   B 1 50  ? 50.252 -22.218 3.020   1.00 12.31 ?  50  ALA   B CB   1 
ATOM   4653 H H    . ALA   B 1 50  ? 49.863 -24.277 1.761   1.00 13.81 ?  50  ALA   B H    1 
ATOM   4654 H HA   . ALA   B 1 50  ? 50.652 -21.886 1.046   1.00 13.92 ?  50  ALA   B HA   1 
ATOM   4655 H HB1  . ALA   B 1 50  ? 50.604 -21.363 3.321   1.00 14.74 ?  50  ALA   B HB1  1 
ATOM   4656 H HB2  . ALA   B 1 50  ? 49.289 -22.154 2.910   1.00 14.74 ?  50  ALA   B HB2  1 
ATOM   4657 H HB3  . ALA   B 1 50  ? 50.463 -22.907 3.671   1.00 14.74 ?  50  ALA   B HB3  1 
ATOM   4658 N N    . GLY   B 1 51  ? 52.954 -23.700 2.311   1.00 12.36 ?  51  GLY   B N    1 
ATOM   4659 C CA   . GLY   B 1 51  ? 54.398 -23.801 2.380   1.00 12.89 ?  51  GLY   B CA   1 
ATOM   4660 C C    . GLY   B 1 51  ? 55.039 -23.740 1.009   1.00 12.63 ?  51  GLY   B C    1 
ATOM   4661 O O    . GLY   B 1 51  ? 56.072 -23.095 0.826   1.00 13.74 ?  51  GLY   B O    1 
ATOM   4662 H H    . GLY   B 1 51  ? 52.529 -24.384 2.614   1.00 14.81 ?  51  GLY   B H    1 
ATOM   4663 H HA2  . GLY   B 1 51  ? 54.750 -23.068 2.914   1.00 15.45 ?  51  GLY   B HA2  1 
ATOM   4664 H HA3  . GLY   B 1 51  ? 54.650 -24.636 2.804   1.00 15.45 ?  51  GLY   B HA3  1 
ATOM   4665 N N    . ALA   B 1 52  ? 54.437 -24.405 0.025   1.00 12.52 ?  52  ALA   B N    1 
ATOM   4666 C CA   . ALA   B 1 52  ? 55.006 -24.405 -1.315  1.00 12.71 ?  52  ALA   B CA   1 
ATOM   4667 C C    . ALA   B 1 52  ? 54.918 -23.029 -1.962  1.00 12.34 ?  52  ALA   B C    1 
ATOM   4668 O O    . ALA   B 1 52  ? 55.887 -22.569 -2.583  1.00 13.00 ?  52  ALA   B O    1 
ATOM   4669 C CB   . ALA   B 1 52  ? 54.318 -25.452 -2.183  1.00 13.68 ?  52  ALA   B CB   1 
ATOM   4670 H H    . ALA   B 1 52  ? 53.702 -24.849 0.106   1.00 15.00 ?  52  ALA   B H    1 
ATOM   4671 H HA   . ALA   B 1 52  ? 55.946 -24.640 -1.249  1.00 15.23 ?  52  ALA   B HA   1 
ATOM   4672 H HB1  . ALA   B 1 52  ? 54.720 -25.436 -3.068  1.00 16.39 ?  52  ALA   B HB1  1 
ATOM   4673 H HB2  . ALA   B 1 52  ? 54.448 -26.327 -1.780  1.00 16.39 ?  52  ALA   B HB2  1 
ATOM   4674 H HB3  . ALA   B 1 52  ? 53.377 -25.247 -2.240  1.00 16.39 ?  52  ALA   B HB3  1 
ATOM   4675 N N    . LEU   B 1 53  ? 53.769 -22.358 -1.841  1.00 12.10 ?  53  LEU   B N    1 
ATOM   4676 C CA   . LEU   B 1 53  ? 53.654 -21.017 -2.408  1.00 11.82 ?  53  LEU   B CA   1 
ATOM   4677 C C    . LEU   B 1 53  ? 54.658 -20.076 -1.760  1.00 11.87 ?  53  LEU   B C    1 
ATOM   4678 O O    . LEU   B 1 53  ? 55.355 -19.316 -2.444  1.00 12.98 ?  53  LEU   B O    1 
ATOM   4679 C CB   . LEU   B 1 53  ? 52.234 -20.478 -2.233  1.00 12.69 ?  53  LEU   B CB   1 
ATOM   4680 C CG   . LEU   B 1 53  ? 51.111 -21.203 -2.971  1.00 12.99 ?  53  LEU   B CG   1 
ATOM   4681 C CD1  . LEU   B 1 53  ? 49.771 -20.573 -2.627  1.00 14.31 ?  53  LEU   B CD1  1 
ATOM   4682 C CD2  . LEU   B 1 53  ? 51.330 -21.210 -4.474  1.00 14.64 ?  53  LEU   B CD2  1 
ATOM   4683 H H    . LEU   B 1 53  ? 53.064 -22.652 -1.446  1.00 14.49 ?  53  LEU   B H    1 
ATOM   4684 H HA   . LEU   B 1 53  ? 53.848 -21.064 -3.362  1.00 14.16 ?  53  LEU   B HA   1 
ATOM   4685 H HB2  . LEU   B 1 53  ? 52.017 -20.512 -1.291  1.00 15.20 ?  53  LEU   B HB2  1 
ATOM   4686 H HB3  . LEU   B 1 53  ? 52.223 -19.563 -2.538  1.00 15.20 ?  53  LEU   B HB3  1 
ATOM   4687 H HG   . LEU   B 1 53  ? 51.079 -22.127 -2.673  1.00 15.57 ?  53  LEU   B HG   1 
ATOM   4688 H HD11 . LEU   B 1 53  ? 49.065 -21.047 -3.098  1.00 17.15 ?  53  LEU   B HD11 1 
ATOM   4689 H HD12 . LEU   B 1 53  ? 49.626 -20.642 -1.668  1.00 17.15 ?  53  LEU   B HD12 1 
ATOM   4690 H HD13 . LEU   B 1 53  ? 49.780 -19.643 -2.893  1.00 17.15 ?  53  LEU   B HD13 1 
ATOM   4691 H HD21 . LEU   B 1 53  ? 50.572 -21.639 -4.906  1.00 17.55 ?  53  LEU   B HD21 1 
ATOM   4692 H HD22 . LEU   B 1 53  ? 51.409 -20.295 -4.787  1.00 17.55 ?  53  LEU   B HD22 1 
ATOM   4693 H HD23 . LEU   B 1 53  ? 52.141 -21.700 -4.674  1.00 17.55 ?  53  LEU   B HD23 1 
ATOM   4694 N N    . ASN   B 1 54  ? 54.747 -20.105 -0.434  1.00 11.85 ?  54  ASN   B N    1 
ATOM   4695 C CA   . ASN   B 1 54  ? 55.662 -19.194 0.238   1.00 12.53 ?  54  ASN   B CA   1 
ATOM   4696 C C    . ASN   B 1 54  ? 57.106 -19.469 -0.159  1.00 12.88 ?  54  ASN   B C    1 
ATOM   4697 O O    . ASN   B 1 54  ? 57.882 -18.532 -0.386  1.00 13.19 ?  54  ASN   B O    1 
ATOM   4698 C CB   . ASN   B 1 54  ? 55.493 -19.271 1.748   1.00 13.07 ?  54  ASN   B CB   1 
ATOM   4699 C CG   . ASN   B 1 54  ? 56.472 -18.364 2.464   1.00 13.23 ?  54  ASN   B CG   1 
ATOM   4700 O OD1  . ASN   B 1 54  ? 56.492 -17.150 2.228   1.00 13.98 ?  54  ASN   B OD1  1 
ATOM   4701 N ND2  . ASN   B 1 54  ? 57.322 -18.948 3.304   1.00 15.02 ?  54  ASN   B ND2  1 
ATOM   4702 H H    . ASN   B 1 54  ? 54.303 -20.632 0.081   1.00 14.20 ?  54  ASN   B H    1 
ATOM   4703 H HA   . ASN   B 1 54  ? 55.446 -18.289 -0.038  1.00 15.01 ?  54  ASN   B HA   1 
ATOM   4704 H HB2  . ASN   B 1 54  ? 54.592 -18.988 1.982   1.00 15.66 ?  54  ASN   B HB2  1 
ATOM   4705 H HB3  . ASN   B 1 54  ? 55.645 -20.180 2.041   1.00 15.66 ?  54  ASN   B HB3  1 
ATOM   4706 H HD21 . ASN   B 1 54  ? 57.901 -18.479 3.728   1.00 18.00 ?  54  ASN   B HD21 1 
ATOM   4707 H HD22 . ASN   B 1 54  ? 57.285 -19.802 3.431   1.00 18.00 ?  54  ASN   B HD22 1 
ATOM   4708 N N    . LYS   B 1 55  ? 57.494 -20.743 -0.225  1.00 13.52 ?  55  LYS   B N    1 
ATOM   4709 C CA   . LYS   B 1 55  ? 58.849 -21.078 -0.641  1.00 14.58 ?  55  LYS   B CA   1 
ATOM   4710 C C    . LYS   B 1 55  ? 59.141 -20.540 -2.034  1.00 14.25 ?  55  LYS   B C    1 
ATOM   4711 O O    . LYS   B 1 55  ? 60.240 -20.039 -2.292  1.00 14.74 ?  55  LYS   B O    1 
ATOM   4712 C CB   . LYS   B 1 55  ? 59.045 -22.592 -0.587  1.00 15.94 ?  55  LYS   B CB   1 
ATOM   4713 C CG   . LYS   B 1 55  ? 60.429 -23.061 -0.990  1.00 19.87 ?  55  LYS   B CG   1 
ATOM   4714 C CD   . LYS   B 1 55  ? 60.579 -24.567 -0.826  1.00 22.90 ?  55  LYS   B CD   1 
ATOM   4715 C CE   . LYS   B 1 55  ? 60.657 -24.977 0.645   1.00 25.50 ?  55  LYS   B CE   1 
ATOM   4716 N NZ   . LYS   B 1 55  ? 61.005 -26.411 0.804   1.00 26.86 ?  55  LYS   B NZ   1 
ATOM   4717 H H    . LYS   B 1 55  ? 56.997 -21.415 -0.036  1.00 16.20 ?  55  LYS   B H    1 
ATOM   4718 H HA   . LYS   B 1 55  ? 59.481 -20.668 -0.026  1.00 17.48 ?  55  LYS   B HA   1 
ATOM   4719 H HB2  . LYS   B 1 55  ? 58.884 -22.887 0.323   1.00 19.10 ?  55  LYS   B HB2  1 
ATOM   4720 H HB3  . LYS   B 1 55  ? 58.406 -23.006 -1.185  1.00 19.10 ?  55  LYS   B HB3  1 
ATOM   4721 H HG2  . LYS   B 1 55  ? 60.582 -22.841 -1.922  1.00 23.82 ?  55  LYS   B HG2  1 
ATOM   4722 H HG3  . LYS   B 1 55  ? 61.090 -22.624 -0.430  1.00 23.82 ?  55  LYS   B HG3  1 
ATOM   4723 H HD2  . LYS   B 1 55  ? 59.812 -25.012 -1.221  1.00 27.45 ?  55  LYS   B HD2  1 
ATOM   4724 H HD3  . LYS   B 1 55  ? 61.396 -24.858 -1.261  1.00 27.45 ?  55  LYS   B HD3  1 
ATOM   4725 H HE2  . LYS   B 1 55  ? 61.339 -24.443 1.085   1.00 30.57 ?  55  LYS   B HE2  1 
ATOM   4726 H HE3  . LYS   B 1 55  ? 59.793 -24.821 1.063   1.00 30.57 ?  55  LYS   B HE3  1 
ATOM   4727 H HZ1  . LYS   B 1 55  ? 60.991 -26.631 1.666   1.00 32.21 ?  55  LYS   B HZ1  1 
ATOM   4728 H HZ2  . LYS   B 1 55  ? 60.413 -26.913 0.367   1.00 32.21 ?  55  LYS   B HZ2  1 
ATOM   4729 H HZ3  . LYS   B 1 55  ? 61.814 -26.564 0.475   1.00 32.21 ?  55  LYS   B HZ3  1 
ATOM   4730 N N    . ALA   B 1 56  ? 58.171 -20.626 -2.947  1.00 13.66 ?  56  ALA   B N    1 
ATOM   4731 C CA   . ALA   B 1 56  ? 58.392 -20.110 -4.295  1.00 14.53 ?  56  ALA   B CA   1 
ATOM   4732 C C    . ALA   B 1 56  ? 58.672 -18.614 -4.284  1.00 14.53 ?  56  ALA   B C    1 
ATOM   4733 O O    . ALA   B 1 56  ? 59.420 -18.115 -5.138  1.00 15.69 ?  56  ALA   B O    1 
ATOM   4734 C CB   . ALA   B 1 56  ? 57.196 -20.433 -5.187  1.00 15.39 ?  56  ALA   B CB   1 
ATOM   4735 H H    . ALA   B 1 56  ? 57.391 -20.967 -2.815  1.00 16.37 ?  56  ALA   B H    1 
ATOM   4736 H HA   . ALA   B 1 56  ? 59.169 -20.547 -4.671  1.00 17.41 ?  56  ALA   B HA   1 
ATOM   4737 H HB1  . ALA   B 1 56  ? 57.368 -20.094 -6.082  1.00 18.44 ?  56  ALA   B HB1  1 
ATOM   4738 H HB2  . ALA   B 1 56  ? 57.078 -21.395 -5.216  1.00 18.44 ?  56  ALA   B HB2  1 
ATOM   4739 H HB3  . ALA   B 1 56  ? 56.403 -20.012 -4.821  1.00 18.44 ?  56  ALA   B HB3  1 
ATOM   4740 N N    . THR   B 1 57  ? 58.093 -17.885 -3.330  1.00 14.13 ?  57  THR   B N    1 
ATOM   4741 C CA   . THR   B 1 57  ? 58.335 -16.451 -3.207  1.00 14.14 ?  57  THR   B CA   1 
ATOM   4742 C C    . THR   B 1 57  ? 59.582 -16.133 -2.395  1.00 14.78 ?  57  THR   B C    1 
ATOM   4743 O O    . THR   B 1 57  ? 59.810 -14.961 -2.071  1.00 15.10 ?  57  THR   B O    1 
ATOM   4744 C CB   . THR   B 1 57  ? 57.137 -15.726 -2.570  1.00 13.51 ?  57  THR   B CB   1 
ATOM   4745 O OG1  . THR   B 1 57  ? 57.117 -15.943 -1.150  1.00 13.68 ?  57  THR   B OG1  1 
ATOM   4746 C CG2  . THR   B 1 57  ? 55.811 -16.152 -3.212  1.00 13.66 ?  57  THR   B CG2  1 
ATOM   4747 H H    . THR   B 1 57  ? 57.538 -18.195 -2.748  1.00 16.93 ?  57  THR   B H    1 
ATOM   4748 H HA   . THR   B 1 57  ? 58.457 -16.080 -4.096  1.00 16.94 ?  57  THR   B HA   1 
ATOM   4749 H HB   . THR   B 1 57  ? 57.235 -14.774 -2.735  1.00 16.19 ?  57  THR   B HB   1 
ATOM   4750 H HG1  . THR   B 1 57  ? 57.044 -16.762 -0.988  1.00 16.39 ?  57  THR   B HG1  1 
ATOM   4751 H HG21 . THR   B 1 57  ? 55.082 -15.609 -2.870  1.00 16.36 ?  57  THR   B HG21 1 
ATOM   4752 H HG22 . THR   B 1 57  ? 55.854 -16.044 -4.177  1.00 16.36 ?  57  THR   B HG22 1 
ATOM   4753 H HG23 . THR   B 1 57  ? 55.625 -17.083 -3.012  1.00 16.36 ?  57  THR   B HG23 1 
ATOM   4754 N N    . ASN   B 1 58  ? 60.380 -17.135 -2.042  1.00 15.38 ?  58  ASN   B N    1 
ATOM   4755 C CA   . ASN   B 1 58  ? 61.578 -16.915 -1.239  1.00 17.95 ?  58  ASN   B CA   1 
ATOM   4756 C C    . ASN   B 1 58  ? 61.238 -16.215 0.075   1.00 16.05 ?  58  ASN   B C    1 
ATOM   4757 O O    . ASN   B 1 58  ? 61.973 -15.345 0.548   1.00 16.63 ?  58  ASN   B O    1 
ATOM   4758 C CB   . ASN   B 1 58  ? 62.653 -16.147 -2.017  1.00 23.97 ?  58  ASN   B CB   1 
ATOM   4759 C CG   . ASN   B 1 58  ? 64.024 -16.260 -1.382  1.00 30.62 ?  58  ASN   B CG   1 
ATOM   4760 O OD1  . ASN   B 1 58  ? 64.344 -17.267 -0.749  1.00 33.73 ?  58  ASN   B OD1  1 
ATOM   4761 N ND2  . ASN   B 1 58  ? 64.842 -15.224 -1.545  1.00 34.07 ?  58  ASN   B ND2  1 
ATOM   4762 H H    . ASN   B 1 58  ? 60.250 -17.962 -2.251  1.00 18.44 ?  58  ASN   B H    1 
ATOM   4763 H HA   . ASN   B 1 58  ? 61.957 -17.782 -1.019  1.00 21.52 ?  58  ASN   B HA   1 
ATOM   4764 H HB2  . ASN   B 1 58  ? 62.710 -16.502 -2.920  1.00 28.75 ?  58  ASN   B HB2  1 
ATOM   4765 H HB3  . ASN   B 1 58  ? 62.417 -15.207 -2.046  1.00 28.75 ?  58  ASN   B HB3  1 
ATOM   4766 H HD21 . ASN   B 1 58  ? 65.634 -15.241 -1.206  1.00 40.86 ?  58  ASN   B HD21 1 
ATOM   4767 H HD22 . ASN   B 1 58  ? 64.583 -14.536 -1.992  1.00 40.86 ?  58  ASN   B HD22 1 
ATOM   4768 N N    . ASN   B 1 59  ? 60.111 -16.602 0.672   1.00 15.01 ?  59  ASN   B N    1 
ATOM   4769 C CA   . ASN   B 1 59  ? 59.637 -16.143 1.978   1.00 15.13 ?  59  ASN   B CA   1 
ATOM   4770 C C    . ASN   B 1 59  ? 59.044 -14.735 1.933   1.00 14.55 ?  59  ASN   B C    1 
ATOM   4771 O O    . ASN   B 1 59  ? 58.621 -14.232 2.982   1.00 14.47 ?  59  ASN   B O    1 
ATOM   4772 C CB   . ASN   B 1 59  ? 60.711 -16.208 3.080   1.00 16.34 ?  59  ASN   B CB   1 
ATOM   4773 C CG   . ASN   B 1 59  ? 60.124 -16.381 4.456   1.00 17.44 ?  59  ASN   B CG   1 
ATOM   4774 O OD1  . ASN   B 1 59  ? 59.288 -17.258 4.672   1.00 17.78 ?  59  ASN   B OD1  1 
ATOM   4775 N ND2  . ASN   B 1 59  ? 60.553 -15.548 5.398   1.00 18.34 ?  59  ASN   B ND2  1 
ATOM   4776 H H    . ASN   B 1 59  ? 59.574 -17.175 0.317   1.00 17.99 ?  59  ASN   B H    1 
ATOM   4777 H HA   . ASN   B 1 59  ? 58.925 -16.740 2.254   1.00 18.14 ?  59  ASN   B HA   1 
ATOM   4778 H HB2  . ASN   B 1 59  ? 61.294 -16.966 2.917   1.00 19.58 ?  59  ASN   B HB2  1 
ATOM   4779 H HB3  . ASN   B 1 59  ? 61.220 -15.387 3.081   1.00 19.58 ?  59  ASN   B HB3  1 
ATOM   4780 H HD21 . ASN   B 1 59  ? 60.244 -15.602 6.202   1.00 21.99 ?  59  ASN   B HD21 1 
ATOM   4781 H HD22 . ASN   B 1 59  ? 61.136 -14.947 5.205   1.00 21.99 ?  59  ASN   B HD22 1 
ATOM   4782 N N    . ALA   B 1 60  ? 58.985 -14.083 0.768   1.00 14.25 ?  60  ALA   B N    1 
ATOM   4783 C CA   . ALA   B 1 60  ? 58.395 -12.748 0.709   1.00 14.39 ?  60  ALA   B CA   1 
ATOM   4784 C C    . ALA   B 1 60  ? 56.928 -12.775 1.110   1.00 13.81 ?  60  ALA   B C    1 
ATOM   4785 O O    . ALA   B 1 60  ? 56.427 -11.823 1.727   1.00 14.37 ?  60  ALA   B O    1 
ATOM   4786 C CB   . ALA   B 1 60  ? 58.555 -12.169 -0.696  1.00 15.60 ?  60  ALA   B CB   1 
ATOM   4787 H H    . ALA   B 1 60  ? 59.274 -14.389 0.019   1.00 17.07 ?  60  ALA   B H    1 
ATOM   4788 H HA   . ALA   B 1 60  ? 58.865 -12.170 1.328   1.00 17.25 ?  60  ALA   B HA   1 
ATOM   4789 H HB1  . ALA   B 1 60  ? 58.160 -11.286 -0.719  1.00 18.70 ?  60  ALA   B HB1  1 
ATOM   4790 H HB2  . ALA   B 1 60  ? 59.500 -12.117 -0.912  1.00 18.70 ?  60  ALA   B HB2  1 
ATOM   4791 H HB3  . ALA   B 1 60  ? 58.105 -12.751 -1.330  1.00 18.70 ?  60  ALA   B HB3  1 
ATOM   4792 N N    . MET   B 1 61  ? 56.224 -13.853 0.767   1.00 13.15 ?  61  MET   B N    1 
ATOM   4793 C CA   . MET   B 1 61  ? 54.828 -13.975 1.158   1.00 12.80 ?  61  MET   B CA   1 
ATOM   4794 C C    . MET   B 1 61  ? 54.690 -13.991 2.675   1.00 12.80 ?  61  MET   B C    1 
ATOM   4795 O O    . MET   B 1 61  ? 53.791 -13.346 3.230   1.00 12.50 ?  61  MET   B O    1 
ATOM   4796 C CB   . MET   B 1 61  ? 54.247 -15.235 0.520   1.00 12.58 ?  61  MET   B CB   1 
ATOM   4797 C CG   . MET   B 1 61  ? 52.806 -15.526 0.926   1.00 12.34 ?  61  MET   B CG   1 
ATOM   4798 S SD   . MET   B 1 61  ? 52.164 -17.038 0.166   1.00 12.75 ?  61  MET   B SD   1 
ATOM   4799 C CE   . MET   B 1 61  ? 51.908 -16.461 -1.506  1.00 14.26 ?  61  MET   B CE   1 
ATOM   4800 H H    . MET   B 1 61  ? 56.530 -14.521 0.313   1.00 15.75 ?  61  MET   B H    1 
ATOM   4801 H HA   . MET   B 1 61  ? 54.336 -13.221 0.804   1.00 15.34 ?  61  MET   B HA   1 
ATOM   4802 H HB2  . MET   B 1 61  ? 54.263 -15.140 -0.448  1.00 15.07 ?  61  MET   B HB2  1 
ATOM   4803 H HB3  . MET   B 1 61  ? 54.785 -16.001 0.779   1.00 15.07 ?  61  MET   B HB3  1 
ATOM   4804 H HG2  . MET   B 1 61  ? 52.758 -15.641 1.889   1.00 14.78 ?  61  MET   B HG2  1 
ATOM   4805 H HG3  . MET   B 1 61  ? 52.240 -14.790 0.650   1.00 14.78 ?  61  MET   B HG3  1 
ATOM   4806 H HE1  . MET   B 1 61  ? 51.531 -17.182 -2.035  1.00 17.09 ?  61  MET   B HE1  1 
ATOM   4807 H HE2  . MET   B 1 61  ? 51.297 -15.707 -1.492  1.00 17.09 ?  61  MET   B HE2  1 
ATOM   4808 H HE3  . MET   B 1 61  ? 52.761 -16.188 -1.880  1.00 17.09 ?  61  MET   B HE3  1 
ATOM   4809 N N    . GLN   B 1 62  ? 55.573 -14.708 3.370   1.00 12.75 ?  62  GLN   B N    1 
ATOM   4810 C CA   . GLN   B 1 62  ? 55.466 -14.775 4.823   1.00 12.89 ?  62  GLN   B CA   1 
ATOM   4811 C C    . GLN   B 1 62  ? 55.752 -13.425 5.462   1.00 13.44 ?  62  GLN   B C    1 
ATOM   4812 O O    . GLN   B 1 62  ? 55.071 -13.031 6.416   1.00 14.07 ?  62  GLN   B O    1 
ATOM   4813 C CB   . GLN   B 1 62  ? 56.422 -15.824 5.382   1.00 13.12 ?  62  GLN   B CB   1 
ATOM   4814 C CG   . GLN   B 1 62  ? 56.201 -16.106 6.858   1.00 13.53 ?  62  GLN   B CG   1 
ATOM   4815 C CD   . GLN   B 1 62  ? 54.826 -16.701 7.095   1.00 13.24 ?  62  GLN   B CD   1 
ATOM   4816 O OE1  . GLN   B 1 62  ? 54.567 -17.845 6.729   1.00 13.44 ?  62  GLN   B OE1  1 
ATOM   4817 N NE2  . GLN   B 1 62  ? 53.924 -15.915 7.674   1.00 13.62 ?  62  GLN   B NE2  1 
ATOM   4818 H H    . GLN   B 1 62  ? 56.227 -15.159 3.028   1.00 15.28 ?  62  GLN   B H    1 
ATOM   4819 H HA   . GLN   B 1 62  ? 54.564 -15.035 5.055   1.00 15.45 ?  62  GLN   B HA   1 
ATOM   4820 H HB2  . GLN   B 1 62  ? 56.305 -16.657 4.897   1.00 15.72 ?  62  GLN   B HB2  1 
ATOM   4821 H HB3  . GLN   B 1 62  ? 57.338 -15.510 5.274   1.00 15.72 ?  62  GLN   B HB3  1 
ATOM   4822 H HG2  . GLN   B 1 62  ? 56.866 -16.744 7.167   1.00 16.21 ?  62  GLN   B HG2  1 
ATOM   4823 H HG3  . GLN   B 1 62  ? 56.269 -15.282 7.361   1.00 16.21 ?  62  GLN   B HG3  1 
ATOM   4824 H HE21 . GLN   B 1 62  ? 54.135 -15.116 7.905   1.00 16.32 ?  62  GLN   B HE21 1 
ATOM   4825 H HE22 . GLN   B 1 62  ? 53.129 -16.211 7.822   1.00 16.32 ?  62  GLN   B HE22 1 
ATOM   4826 N N    . VAL   B 1 63  ? 56.771 -12.713 4.975   1.00 13.82 ?  63  VAL   B N    1 
ATOM   4827 C CA   . VAL   B 1 63  ? 57.077 -11.400 5.534   1.00 14.55 ?  63  VAL   B CA   1 
ATOM   4828 C C    . VAL   B 1 63  ? 55.886 -10.463 5.356   1.00 13.88 ?  63  VAL   B C    1 
ATOM   4829 O O    . VAL   B 1 63  ? 55.474 -9.766  6.292   1.00 14.50 ?  63  VAL   B O    1 
ATOM   4830 C CB   . VAL   B 1 63  ? 58.368 -10.838 4.914   1.00 16.43 ?  63  VAL   B CB   1 
ATOM   4831 C CG1  . VAL   B 1 63  ? 58.598 -9.399  5.363   1.00 17.26 ?  63  VAL   B CG1  1 
ATOM   4832 C CG2  . VAL   B 1 63  ? 59.551 -11.710 5.311   1.00 16.92 ?  63  VAL   B CG2  1 
ATOM   4833 H H    . VAL   B 1 63  ? 57.292 -12.966 4.334   1.00 16.56 ?  63  VAL   B H    1 
ATOM   4834 H HA   . VAL   B 1 63  ? 57.235 -11.501 6.485   1.00 17.44 ?  63  VAL   B HA   1 
ATOM   4835 H HB   . VAL   B 1 63  ? 58.301 -10.852 3.948   1.00 19.69 ?  63  VAL   B HB   1 
ATOM   4836 H HG11 . VAL   B 1 63  ? 59.514 -9.148  5.165   1.00 20.69 ?  63  VAL   B HG11 1 
ATOM   4837 H HG12 . VAL   B 1 63  ? 57.986 -8.819  4.887   1.00 20.69 ?  63  VAL   B HG12 1 
ATOM   4838 H HG13 . VAL   B 1 63  ? 58.441 -9.339  6.319   1.00 20.69 ?  63  VAL   B HG13 1 
ATOM   4839 H HG21 . VAL   B 1 63  ? 60.366 -11.336 4.937   1.00 20.28 ?  63  VAL   B HG21 1 
ATOM   4840 H HG22 . VAL   B 1 63  ? 59.619 -11.730 6.283   1.00 20.28 ?  63  VAL   B HG22 1 
ATOM   4841 H HG23 . VAL   B 1 63  ? 59.416 -12.608 4.974   1.00 20.28 ?  63  VAL   B HG23 1 
ATOM   4842 N N    . GLU   B 1 64  ? 55.319 -10.438 4.147   1.00 13.46 ?  64  GLU   B N    1 
ATOM   4843 C CA   . GLU   B 1 64  ? 54.149 -9.608  3.873   1.00 13.12 ?  64  GLU   B CA   1 
ATOM   4844 C C    . GLU   B 1 64  ? 52.971 -10.014 4.753   1.00 12.88 ?  64  GLU   B C    1 
ATOM   4845 O O    . GLU   B 1 64  ? 52.230 -9.158  5.262   1.00 13.35 ?  64  GLU   B O    1 
ATOM   4846 C CB   . GLU   B 1 64  ? 53.786 -9.761  2.396   1.00 13.07 ?  64  GLU   B CB   1 
ATOM   4847 C CG   . GLU   B 1 64  ? 52.522 -9.020  1.966   1.00 13.14 ?  64  GLU   B CG   1 
ATOM   4848 C CD   . GLU   B 1 64  ? 51.970 -9.516  0.643   1.00 13.90 ?  64  GLU   B CD   1 
ATOM   4849 O OE1  . GLU   B 1 64  ? 52.140 -10.725 0.334   1.00 14.64 ?  64  GLU   B OE1  1 
ATOM   4850 O OE2  . GLU   B 1 64  ? 51.346 -8.702  -0.081  1.00 14.40 -1 64  GLU   B OE2  1 
ATOM   4851 H H    . GLU   B 1 64  ? 55.600 -10.895 3.468   1.00 16.13 ?  64  GLU   B H    1 
ATOM   4852 H HA   . GLU   B 1 64  ? 54.364 -8.682  4.047   1.00 15.72 ?  64  GLU   B HA   1 
ATOM   4853 H HB2  . GLU   B 1 64  ? 54.521 -9.416  1.858   1.00 15.66 ?  64  GLU   B HB2  1 
ATOM   4854 H HB3  . GLU   B 1 64  ? 53.658 -10.700 2.202   1.00 15.66 ?  64  GLU   B HB3  1 
ATOM   4855 H HG2  . GLU   B 1 64  ? 51.828 -9.140  2.633   1.00 15.75 ?  64  GLU   B HG2  1 
ATOM   4856 H HG3  . GLU   B 1 64  ? 52.726 -8.075  1.872   1.00 15.75 ?  64  GLU   B HG3  1 
ATOM   4857 N N    . SER   B 1 65  ? 52.790 -11.322 4.941   1.00 12.61 ?  65  SER   B N    1 
ATOM   4858 C CA   . SER   B 1 65  ? 51.680 -11.828 5.738   1.00 12.68 ?  65  SER   B CA   1 
ATOM   4859 C C    . SER   B 1 65  ? 51.815 -11.438 7.203   1.00 12.85 ?  65  SER   B C    1 
ATOM   4860 O O    . SER   B 1 65  ? 50.816 -11.071 7.844   1.00 13.43 ?  65  SER   B O    1 
ATOM   4861 C CB   . SER   B 1 65  ? 51.592 -13.349 5.599   1.00 12.97 ?  65  SER   B CB   1 
ATOM   4862 O OG   . SER   B 1 65  ? 51.257 -13.740 4.276   1.00 13.02 ?  65  SER   B OG   1 
ATOM   4863 H H    . SER   B 1 65  ? 53.301 -11.942 4.620   1.00 15.11 ?  65  SER   B H    1 
ATOM   4864 H HA   . SER   B 1 65  ? 50.852 -11.454 5.403   1.00 15.19 ?  65  SER   B HA   1 
ATOM   4865 H HB2  . SER   B 1 65  ? 52.448 -13.739 5.832   1.00 15.54 ?  65  SER   B HB2  1 
ATOM   4866 H HB3  . SER   B 1 65  ? 50.906 -13.681 6.203   1.00 15.54 ?  65  SER   B HB3  1 
ATOM   4867 H HG   . SER   B 1 65  ? 51.844 -13.454 3.736   1.00 15.60 ?  65  SER   B HG   1 
ATOM   4868 N N    . ASP   B 1 66  ? 53.026 -11.538 7.763   1.00 13.14 ?  66  ASP   B N    1 
ATOM   4869 C CA   . ASP   B 1 66  ? 53.216 -11.157 9.158   1.00 13.59 ?  66  ASP   B CA   1 
ATOM   4870 C C    . ASP   B 1 66  ? 52.900 -9.681  9.368   1.00 13.99 ?  66  ASP   B C    1 
ATOM   4871 O O    . ASP   B 1 66  ? 52.318 -9.299  10.390  1.00 14.32 ?  66  ASP   B O    1 
ATOM   4872 C CB   . ASP   B 1 66  ? 54.652 -11.460 9.592   1.00 15.04 ?  66  ASP   B CB   1 
ATOM   4873 C CG   . ASP   B 1 66  ? 54.929 -12.947 9.746   1.00 16.82 ?  66  ASP   B CG   1 
ATOM   4874 O OD1  . ASP   B 1 66  ? 53.982 -13.762 9.661   1.00 17.44 ?  66  ASP   B OD1  1 
ATOM   4875 O OD2  . ASP   B 1 66  ? 56.111 -13.305 9.964   1.00 19.38 -1 66  ASP   B OD2  1 
ATOM   4876 H H    . ASP   B 1 66  ? 53.732 -11.830 7.365   1.00 15.74 ?  66  ASP   B H    1 
ATOM   4877 H HA   . ASP   B 1 66  ? 52.620 -11.673 9.719   1.00 16.28 ?  66  ASP   B HA   1 
ATOM   4878 H HB2  . ASP   B 1 66  ? 55.268 -11.117 8.925   1.00 18.03 ?  66  ASP   B HB2  1 
ATOM   4879 H HB3  . ASP   B 1 66  ? 54.824 -11.034 10.449  1.00 18.03 ?  66  ASP   B HB3  1 
ATOM   4880 N N    . ASP   B 1 67  ? 53.275 -8.832  8.410   1.00 13.53 ?  67  ASP   B N    1 
ATOM   4881 C CA   . ASP   B 1 67  ? 52.930 -7.421  8.510   1.00 14.33 ?  67  ASP   B CA   1 
ATOM   4882 C C    . ASP   B 1 67  ? 51.419 -7.213  8.425   1.00 14.31 ?  67  ASP   B C    1 
ATOM   4883 O O    . ASP   B 1 67  ? 50.853 -6.410  9.178   1.00 14.96 ?  67  ASP   B O    1 
ATOM   4884 C CB   . ASP   B 1 67  ? 53.652 -6.641  7.418   1.00 15.42 ?  67  ASP   B CB   1 
ATOM   4885 C CG   . ASP   B 1 67  ? 53.235 -5.205  7.382   1.00 16.91 ?  67  ASP   B CG   1 
ATOM   4886 O OD1  . ASP   B 1 67  ? 53.740 -4.413  8.207   1.00 18.06 ?  67  ASP   B OD1  1 
ATOM   4887 O OD2  . ASP   B 1 67  ? 52.379 -4.882  6.546   1.00 17.85 -1 67  ASP   B OD2  1 
ATOM   4888 H H    . ASP   B 1 67  ? 53.733 -9.046  7.710   1.00 16.21 ?  67  ASP   B H    1 
ATOM   4889 H HA   . ASP   B 1 67  ? 53.233 -7.082  9.367   1.00 17.18 ?  67  ASP   B HA   1 
ATOM   4890 H HB2  . ASP   B 1 67  ? 54.608 -6.670  7.583   1.00 18.48 ?  67  ASP   B HB2  1 
ATOM   4891 H HB3  . ASP   B 1 67  ? 53.453 -7.044  6.556   1.00 18.48 ?  67  ASP   B HB3  1 
ATOM   4892 N N    . TYR   B 1 68  ? 50.746 -7.941  7.527   1.00 13.98 ?  68  TYR   B N    1 
ATOM   4893 C CA   . TYR   B 1 68  ? 49.288 -7.864  7.454   1.00 14.89 ?  68  TYR   B CA   1 
ATOM   4894 C C    . TYR   B 1 68  ? 48.653 -8.207  8.797   1.00 14.05 ?  68  TYR   B C    1 
ATOM   4895 O O    . TYR   B 1 68  ? 47.721 -7.530  9.252   1.00 14.68 ?  68  TYR   B O    1 
ATOM   4896 C CB   . TYR   B 1 68  ? 48.754 -8.797  6.361   1.00 15.98 ?  68  TYR   B CB   1 
ATOM   4897 C CG   . TYR   B 1 68  ? 47.243 -8.943  6.423   1.00 16.98 ?  68  TYR   B CG   1 
ATOM   4898 C CD1  . TYR   B 1 68  ? 46.646 -9.897  7.248   1.00 17.42 ?  68  TYR   B CD1  1 
ATOM   4899 C CD2  . TYR   B 1 68  ? 46.415 -8.107  5.694   1.00 17.89 ?  68  TYR   B CD2  1 
ATOM   4900 C CE1  . TYR   B 1 68  ? 45.279 -10.018 7.336   1.00 18.71 ?  68  TYR   B CE1  1 
ATOM   4901 C CE2  . TYR   B 1 68  ? 45.031 -8.230  5.771   1.00 18.36 ?  68  TYR   B CE2  1 
ATOM   4902 C CZ   . TYR   B 1 68  ? 44.483 -9.184  6.597   1.00 18.65 ?  68  TYR   B CZ   1 
ATOM   4903 O OH   . TYR   B 1 68  ? 43.118 -9.305  6.695   1.00 19.71 ?  68  TYR   B OH   1 
ATOM   4904 H H    . TYR   B 1 68  ? 51.106 -8.482  6.957   1.00 16.76 ?  68  TYR   B H    1 
ATOM   4905 H HA   . TYR   B 1 68  ? 49.034 -6.959  7.225   1.00 17.85 ?  68  TYR   B HA   1 
ATOM   4906 H HB2  . TYR   B 1 68  ? 48.980 -8.434  5.492   1.00 19.16 ?  68  TYR   B HB2  1 
ATOM   4907 H HB3  . TYR   B 1 68  ? 49.147 -9.677  6.469   1.00 19.16 ?  68  TYR   B HB3  1 
ATOM   4908 H HD1  . TYR   B 1 68  ? 47.186 -10.467 7.753   1.00 20.88 ?  68  TYR   B HD1  1 
ATOM   4909 H HD2  . TYR   B 1 68  ? 46.789 -7.462  5.147   1.00 21.45 ?  68  TYR   B HD2  1 
ATOM   4910 H HE1  . TYR   B 1 68  ? 44.897 -10.669 7.887   1.00 22.43 ?  68  TYR   B HE1  1 
ATOM   4911 H HE2  . TYR   B 1 68  ? 44.479 -7.666  5.280   1.00 22.01 ?  68  TYR   B HE2  1 
ATOM   4912 H HH   . TYR   B 1 68  ? 42.730 -8.750  6.191   1.00 23.63 ?  68  TYR   B HH   1 
ATOM   4913 N N    . ILE   B 1 69  ? 49.127 -9.281  9.433   1.00 13.89 ?  69  ILE   B N    1 
ATOM   4914 C CA   . ILE   B 1 69  ? 48.567 -9.712  10.710  1.00 14.60 ?  69  ILE   B CA   1 
ATOM   4915 C C    . ILE   B 1 69  ? 48.829 -8.677  11.795  1.00 14.44 ?  69  ILE   B C    1 
ATOM   4916 O O    . ILE   B 1 69  ? 47.963 -8.403  12.632  1.00 14.66 ?  69  ILE   B O    1 
ATOM   4917 C CB   . ILE   B 1 69  ? 49.132 -11.093 11.089  1.00 15.41 ?  69  ILE   B CB   1 
ATOM   4918 C CG1  . ILE   B 1 69  ? 48.611 -12.182 10.138  1.00 15.88 ?  69  ILE   B CG1  1 
ATOM   4919 C CG2  . ILE   B 1 69  ? 48.832 -11.423 12.544  1.00 16.94 ?  69  ILE   B CG2  1 
ATOM   4920 C CD1  . ILE   B 1 69  ? 47.139 -12.508 10.291  1.00 15.95 ?  69  ILE   B CD1  1 
ATOM   4921 H H    . ILE   B 1 69  ? 49.769 -9.778  9.144   1.00 16.64 ?  69  ILE   B H    1 
ATOM   4922 H HA   . ILE   B 1 69  ? 47.609 -9.800  10.614  1.00 17.50 ?  69  ILE   B HA   1 
ATOM   4923 H HB   . ILE   B 1 69  ? 50.096 -11.057 10.990  1.00 18.46 ?  69  ILE   B HB   1 
ATOM   4924 H HG12 . ILE   B 1 69  ? 48.752 -11.885 9.223   1.00 19.03 ?  69  ILE   B HG12 1 
ATOM   4925 H HG13 . ILE   B 1 69  ? 49.113 -12.997 10.294  1.00 19.03 ?  69  ILE   B HG13 1 
ATOM   4926 H HG21 . ILE   B 1 69  ? 48.971 -12.374 12.682  1.00 20.30 ?  69  ILE   B HG21 1 
ATOM   4927 H HG22 . ILE   B 1 69  ? 49.429 -10.919 13.115  1.00 20.30 ?  69  ILE   B HG22 1 
ATOM   4928 H HG23 . ILE   B 1 69  ? 47.910 -11.195 12.736  1.00 20.30 ?  69  ILE   B HG23 1 
ATOM   4929 H HD11 . ILE   B 1 69  ? 46.903 -13.192 9.643   1.00 19.12 ?  69  ILE   B HD11 1 
ATOM   4930 H HD12 . ILE   B 1 69  ? 46.981 -12.840 11.189  1.00 19.12 ?  69  ILE   B HD12 1 
ATOM   4931 H HD13 . ILE   B 1 69  ? 46.617 -11.710 10.133  1.00 19.12 ?  69  ILE   B HD13 1 
ATOM   4932 N N    . ALA   B 1 70  ? 50.025 -8.095  11.816  1.00 14.27 ?  70  ALA   B N    1 
ATOM   4933 C CA   . ALA   B 1 70  ? 50.308 -7.058  12.803  1.00 14.24 ?  70  ALA   B CA   1 
ATOM   4934 C C    . ALA   B 1 70  ? 49.314 -5.910  12.698  1.00 14.67 ?  70  ALA   B C    1 
ATOM   4935 O O    . ALA   B 1 70  ? 48.876 -5.364  13.714  1.00 14.89 ?  70  ALA   B O    1 
ATOM   4936 C CB   . ALA   B 1 70  ? 51.735 -6.546  12.622  1.00 14.69 ?  70  ALA   B CB   1 
ATOM   4937 H H    . ALA   B 1 70  ? 50.674 -8.280  11.288  1.00 17.10 ?  70  ALA   B H    1 
ATOM   4938 H HA   . ALA   B 1 70  ? 50.242 -7.437  13.695  1.00 17.07 ?  70  ALA   B HA   1 
ATOM   4939 H HB1  . ALA   B 1 70  ? 51.930 -5.889  13.309  1.00 17.60 ?  70  ALA   B HB1  1 
ATOM   4940 H HB2  . ALA   B 1 70  ? 52.354 -7.292  12.698  1.00 17.60 ?  70  ALA   B HB2  1 
ATOM   4941 H HB3  . ALA   B 1 70  ? 51.820 -6.140  11.743  1.00 17.60 ?  70  ALA   B HB3  1 
ATOM   4942 N N    . THR   B 1 71  ? 48.939 -5.541  11.476  1.00 15.21 ?  71  THR   B N    1 
ATOM   4943 C CA   . THR   B 1 71  ? 48.050 -4.403  11.272  1.00 15.78 ?  71  THR   B CA   1 
ATOM   4944 C C    . THR   B 1 71  ? 46.584 -4.770  11.476  1.00 16.47 ?  71  THR   B C    1 
ATOM   4945 O O    . THR   B 1 71  ? 45.806 -3.955  11.986  1.00 17.68 ?  71  THR   B O    1 
ATOM   4946 C CB   . THR   B 1 71  ? 48.272 -3.835  9.869   1.00 17.35 ?  71  THR   B CB   1 
ATOM   4947 O OG1  . THR   B 1 71  ? 49.600 -3.306  9.775   1.00 19.33 ?  71  THR   B OG1  1 
ATOM   4948 C CG2  . THR   B 1 71  ? 47.261 -2.744  9.546   1.00 18.45 ?  71  THR   B CG2  1 
ATOM   4949 H H    . THR   B 1 71  ? 49.194 -5.927  10.754  1.00 18.22 ?  71  THR   B H    1 
ATOM   4950 H HA   . THR   B 1 71  ? 48.275 -3.708  11.911  1.00 18.91 ?  71  THR   B HA   1 
ATOM   4951 H HB   . THR   B 1 71  ? 48.174 -4.544  9.215   1.00 20.79 ?  71  THR   B HB   1 
ATOM   4952 H HG1  . THR   B 1 71  ? 49.730 -2.979  9.009   1.00 23.17 ?  71  THR   B HG1  1 
ATOM   4953 H HG21 . THR   B 1 71  ? 47.565 -2.224  8.784   1.00 22.12 ?  71  THR   B HG21 1 
ATOM   4954 H HG22 . THR   B 1 71  ? 46.401 -3.137  9.333   1.00 22.12 ?  71  THR   B HG22 1 
ATOM   4955 H HG23 . THR   B 1 71  ? 47.159 -2.150  10.307  1.00 22.12 ?  71  THR   B HG23 1 
ATOM   4956 N N    . ASN   B 1 72  ? 46.187 -5.980  11.078  1.00 15.99 ?  72  ASN   B N    1 
ATOM   4957 C CA   . ASN   B 1 72  ? 44.783 -6.337  10.949  1.00 16.47 ?  72  ASN   B CA   1 
ATOM   4958 C C    . ASN   B 1 72  ? 44.306 -7.436  11.886  1.00 16.87 ?  72  ASN   B C    1 
ATOM   4959 O O    . ASN   B 1 72  ? 43.090 -7.592  12.048  1.00 18.04 ?  72  ASN   B O    1 
ATOM   4960 C CB   . ASN   B 1 72  ? 44.482 -6.756  9.503   1.00 17.27 ?  72  ASN   B CB   1 
ATOM   4961 C CG   . ASN   B 1 72  ? 44.733 -5.637  8.522   1.00 18.57 ?  72  ASN   B CG   1 
ATOM   4962 O OD1  . ASN   B 1 72  ? 45.736 -5.623  7.808   1.00 19.75 ?  72  ASN   B OD1  1 
ATOM   4963 N ND2  . ASN   B 1 72  ? 43.841 -4.671  8.507   1.00 20.24 ?  72  ASN   B ND2  1 
ATOM   4964 H H    . ASN   B 1 72  ? 46.731 -6.620  10.867  1.00 19.16 ?  72  ASN   B H    1 
ATOM   4965 H HA   . ASN   B 1 72  ? 44.255 -5.550  11.133  1.00 19.74 ?  72  ASN   B HA   1 
ATOM   4966 H HB2  . ASN   B 1 72  ? 45.056 -7.506  9.262   1.00 20.70 ?  72  ASN   B HB2  1 
ATOM   4967 H HB3  . ASN   B 1 72  ? 43.553 -7.016  9.435   1.00 20.70 ?  72  ASN   B HB3  1 
ATOM   4968 H HD21 . ASN   B 1 72  ? 43.932 -4.009  7.966   1.00 24.26 ?  72  ASN   B HD21 1 
ATOM   4969 H HD22 . ASN   B 1 72  ? 43.152 -4.713  9.021   1.00 24.26 ?  72  ASN   B HD22 1 
ATOM   4970 N N    . GLY   B 1 73  ? 45.206 -8.197  12.500  1.00 16.39 ?  73  GLY   B N    1 
ATOM   4971 C CA   . GLY   B 1 73  ? 44.804 -9.336  13.286  1.00 15.99 ?  73  GLY   B CA   1 
ATOM   4972 C C    . GLY   B 1 73  ? 44.438 -10.516 12.413  1.00 14.77 ?  73  GLY   B C    1 
ATOM   4973 O O    . GLY   B 1 73  ? 44.426 -10.429 11.182  1.00 14.72 ?  73  GLY   B O    1 
ATOM   4974 H H    . GLY   B 1 73  ? 46.061 -8.068  12.470  1.00 19.64 ?  73  GLY   B H    1 
ATOM   4975 H HA2  . GLY   B 1 73  ? 45.531 -9.593  13.878  1.00 19.16 ?  73  GLY   B HA2  1 
ATOM   4976 H HA3  . GLY   B 1 73  ? 44.036 -9.097  13.829  1.00 19.16 ?  73  GLY   B HA3  1 
ATOM   4977 N N    . PRO   B 1 74  ? 44.132 -11.645 13.045  1.00 14.85 ?  74  PRO   B N    1 
ATOM   4978 C CA   . PRO   B 1 74  ? 43.888 -12.876 12.292  1.00 14.32 ?  74  PRO   B CA   1 
ATOM   4979 C C    . PRO   B 1 74  ? 42.581 -12.828 11.513  1.00 13.46 ?  74  PRO   B C    1 
ATOM   4980 O O    . PRO   B 1 74  ? 41.640 -12.094 11.841  1.00 15.07 ?  74  PRO   B O    1 
ATOM   4981 C CB   . PRO   B 1 74  ? 43.827 -13.945 13.389  1.00 15.41 ?  74  PRO   B CB   1 
ATOM   4982 C CG   . PRO   B 1 74  ? 43.359 -13.205 14.597  1.00 17.04 ?  74  PRO   B CG   1 
ATOM   4983 C CD   . PRO   B 1 74  ? 44.022 -11.856 14.497  1.00 16.13 ?  74  PRO   B CD   1 
ATOM   4984 H HA   . PRO   B 1 74  ? 44.634 -13.057 11.688  1.00 17.16 ?  74  PRO   B HA   1 
ATOM   4985 H HB2  . PRO   B 1 74  ? 43.195 -14.633 13.133  1.00 18.46 ?  74  PRO   B HB2  1 
ATOM   4986 H HB3  . PRO   B 1 74  ? 44.711 -14.319 13.530  1.00 18.46 ?  74  PRO   B HB3  1 
ATOM   4987 H HG2  . PRO   B 1 74  ? 42.393 -13.117 14.572  1.00 20.42 ?  74  PRO   B HG2  1 
ATOM   4988 H HG3  . PRO   B 1 74  ? 43.645 -13.671 15.396  1.00 20.42 ?  74  PRO   B HG3  1 
ATOM   4989 H HD2  . PRO   B 1 74  ? 43.460 -11.173 14.903  1.00 19.33 ?  74  PRO   B HD2  1 
ATOM   4990 H HD3  . PRO   B 1 74  ? 44.902 -11.878 14.902  1.00 19.33 ?  74  PRO   B HD3  1 
ATOM   4991 N N    . LEU   B 1 75  ? 42.550 -13.627 10.449  1.00 12.94 ?  75  LEU   B N    1 
ATOM   4992 C CA   . LEU   B 1 75  ? 41.334 -13.845 9.687   1.00 12.70 ?  75  LEU   B CA   1 
ATOM   4993 C C    . LEU   B 1 75  ? 40.368 -14.711 10.493  1.00 13.08 ?  75  LEU   B C    1 
ATOM   4994 O O    . LEU   B 1 75  ? 40.708 -15.251 11.546  1.00 14.03 ?  75  LEU   B O    1 
ATOM   4995 C CB   . LEU   B 1 75  ? 41.649 -14.554 8.370   1.00 13.10 ?  75  LEU   B CB   1 
ATOM   4996 C CG   . LEU   B 1 75  ? 42.503 -13.812 7.339   1.00 15.39 ?  75  LEU   B CG   1 
ATOM   4997 C CD1  . LEU   B 1 75  ? 42.672 -14.629 6.058   1.00 16.58 ?  75  LEU   B CD1  1 
ATOM   4998 C CD2  . LEU   B 1 75  ? 41.951 -12.451 7.022   1.00 18.68 ?  75  LEU   B CD2  1 
ATOM   4999 H H    . LEU   B 1 75  ? 43.229 -14.065 10.144  1.00 15.51 ?  75  LEU   B H    1 
ATOM   5000 H HA   . LEU   B 1 75  ? 40.906 -12.997 9.493   1.00 15.21 ?  75  LEU   B HA   1 
ATOM   5001 H HB2  . LEU   B 1 75  ? 42.116 -15.381 8.576   1.00 15.69 ?  75  LEU   B HB2  1 
ATOM   5002 H HB3  . LEU   B 1 75  ? 40.809 -14.770 7.932   1.00 15.69 ?  75  LEU   B HB3  1 
ATOM   5003 H HG   . LEU   B 1 75  ? 43.388 -13.685 7.710   1.00 18.45 ?  75  LEU   B HG   1 
ATOM   5004 H HD11 . LEU   B 1 75  ? 43.225 -14.126 5.430   1.00 19.87 ?  75  LEU   B HD11 1 
ATOM   5005 H HD12 . LEU   B 1 75  ? 43.107 -15.471 6.269   1.00 19.87 ?  75  LEU   B HD12 1 
ATOM   5006 H HD13 . LEU   B 1 75  ? 41.803 -14.794 5.664   1.00 19.87 ?  75  LEU   B HD13 1 
ATOM   5007 H HD21 . LEU   B 1 75  ? 42.470 -12.055 6.307   1.00 22.39 ?  75  LEU   B HD21 1 
ATOM   5008 H HD22 . LEU   B 1 75  ? 41.025 -12.544 6.749   1.00 22.39 ?  75  LEU   B HD22 1 
ATOM   5009 H HD23 . LEU   B 1 75  ? 42.006 -11.898 7.817   1.00 22.39 ?  75  LEU   B HD23 1 
ATOM   5010 N N    . LYS   B 1 76  ? 39.144 -14.834 9.977   1.00 14.46 ?  76  LYS   B N    1 
ATOM   5011 C CA   . LYS   B 1 76  ? 38.158 -15.793 10.460  1.00 15.87 ?  76  LYS   B CA   1 
ATOM   5012 C C    . LYS   B 1 76  ? 38.241 -17.056 9.609   1.00 14.45 ?  76  LYS   B C    1 
ATOM   5013 O O    . LYS   B 1 76  ? 38.507 -16.985 8.410   1.00 14.05 ?  76  LYS   B O    1 
ATOM   5014 C CB   . LYS   B 1 76  ? 36.737 -15.223 10.293  1.00 19.05 ?  76  LYS   B CB   1 
ATOM   5015 C CG   . LYS   B 1 76  ? 36.472 -13.821 10.874  1.00 21.52 ?  76  LYS   B CG   1 
ATOM   5016 C CD   . LYS   B 1 76  ? 35.053 -13.303 10.546  1.00 23.43 ?  76  LYS   B CD   1 
ATOM   5017 C CE   . LYS   B 1 76  ? 34.795 -11.932 11.163  1.00 25.66 ?  76  LYS   B CE   1 
ATOM   5018 N NZ   . LYS   B 1 76  ? 33.521 -11.313 10.694  1.00 26.21 ?  76  LYS   B NZ   1 
ATOM   5019 H H    . LYS   B 1 76  ? 38.854 -14.361 9.324   1.00 17.33 ?  76  LYS   B H    1 
ATOM   5020 H HA   . LYS   B 1 76  ? 38.314 -16.018 11.394  1.00 19.02 ?  76  LYS   B HA   1 
ATOM   5021 H HB2  . LYS   B 1 76  ? 36.542 -15.178 9.343   1.00 22.84 ?  76  LYS   B HB2  1 
ATOM   5022 H HB3  . LYS   B 1 76  ? 36.113 -15.830 10.718  1.00 22.84 ?  76  LYS   B HB3  1 
ATOM   5023 H HG2  . LYS   B 1 76  ? 36.566 -13.855 11.839  1.00 25.80 ?  76  LYS   B HG2  1 
ATOM   5024 H HG3  . LYS   B 1 76  ? 37.115 -13.196 10.500  1.00 25.80 ?  76  LYS   B HG3  1 
ATOM   5025 H HD2  . LYS   B 1 76  ? 34.956 -13.225 9.583   1.00 28.09 ?  76  LYS   B HD2  1 
ATOM   5026 H HD3  . LYS   B 1 76  ? 34.397 -13.924 10.899  1.00 28.09 ?  76  LYS   B HD3  1 
ATOM   5027 H HE2  . LYS   B 1 76  ? 34.747 -12.026 12.127  1.00 30.76 ?  76  LYS   B HE2  1 
ATOM   5028 H HE3  . LYS   B 1 76  ? 35.524 -11.338 10.924  1.00 30.76 ?  76  LYS   B HE3  1 
ATOM   5029 H HZ1  . LYS   B 1 76  ? 33.409 -10.516 11.078  1.00 31.43 ?  76  LYS   B HZ1  1 
ATOM   5030 H HZ2  . LYS   B 1 76  ? 33.539 -11.205 9.811   1.00 31.43 ?  76  LYS   B HZ2  1 
ATOM   5031 H HZ3  . LYS   B 1 76  ? 32.830 -11.833 10.907  1.00 31.43 ?  76  LYS   B HZ3  1 
ATOM   5032 N N    . VAL   B 1 77  ? 37.992 -18.219 10.226  1.00 14.49 ?  77  VAL   B N    1 
ATOM   5033 C CA   . VAL   B 1 77  ? 37.776 -19.421 9.424   1.00 14.27 ?  77  VAL   B CA   1 
ATOM   5034 C C    . VAL   B 1 77  ? 36.584 -19.171 8.510   1.00 13.55 ?  77  VAL   B C    1 
ATOM   5035 O O    . VAL   B 1 77  ? 35.521 -18.719 8.958   1.00 13.53 ?  77  VAL   B O    1 
ATOM   5036 C CB   . VAL   B 1 77  ? 37.571 -20.662 10.306  1.00 15.57 ?  77  VAL   B CB   1 
ATOM   5037 C CG1  . VAL   B 1 77  ? 37.293 -21.880 9.424   1.00 16.13 ?  77  VAL   B CG1  1 
ATOM   5038 C CG2  . VAL   B 1 77  ? 38.793 -20.918 11.191  1.00 17.37 ?  77  VAL   B CG2  1 
ATOM   5039 H H    . VAL   B 1 77  ? 37.959 -18.335 11.076  1.00 17.36 ?  77  VAL   B H    1 
ATOM   5040 H HA   . VAL   B 1 77  ? 38.551 -19.572 8.865   1.00 17.10 ?  77  VAL   B HA   1 
ATOM   5041 H HB   . VAL   B 1 77  ? 36.799 -20.521 10.882  1.00 18.66 ?  77  VAL   B HB   1 
ATOM   5042 H HG11 . VAL   B 1 77  ? 37.356 -22.681 9.966   1.00 19.33 ?  77  VAL   B HG11 1 
ATOM   5043 H HG12 . VAL   B 1 77  ? 36.398 -21.806 9.051   1.00 19.33 ?  77  VAL   B HG12 1 
ATOM   5044 H HG13 . VAL   B 1 77  ? 37.948 -21.908 8.711   1.00 19.33 ?  77  VAL   B HG13 1 
ATOM   5045 H HG21 . VAL   B 1 77  ? 38.636 -21.722 11.709  1.00 20.82 ?  77  VAL   B HG21 1 
ATOM   5046 H HG22 . VAL   B 1 77  ? 39.567 -21.029 10.624  1.00 20.82 ?  77  VAL   B HG22 1 
ATOM   5047 H HG23 . VAL   B 1 77  ? 38.913 -20.159 11.781  1.00 20.82 ?  77  VAL   B HG23 1 
ATOM   5048 N N    . GLY   B 1 78  ? 36.760 -19.450 7.222   1.00 12.80 ?  78  GLY   B N    1 
ATOM   5049 C CA   . GLY   B 1 78  ? 35.783 -19.118 6.210   1.00 12.50 ?  78  GLY   B CA   1 
ATOM   5050 C C    . GLY   B 1 78  ? 36.036 -17.801 5.512   1.00 12.09 ?  78  GLY   B C    1 
ATOM   5051 O O    . GLY   B 1 78  ? 35.365 -17.513 4.514   1.00 12.49 ?  78  GLY   B O    1 
ATOM   5052 H H    . GLY   B 1 78  ? 37.460 -19.839 6.911   1.00 15.34 ?  78  GLY   B H    1 
ATOM   5053 H HA2  . GLY   B 1 78  ? 35.772 -19.817 5.541   1.00 14.97 ?  78  GLY   B HA2  1 
ATOM   5054 H HA3  . GLY   B 1 78  ? 34.905 -19.073 6.619   1.00 14.97 ?  78  GLY   B HA3  1 
ATOM   5055 N N    . GLY   B 1 79  ? 36.996 -17.007 5.996   1.00 12.36 ?  79  GLY   B N    1 
ATOM   5056 C CA   . GLY   B 1 79  ? 37.293 -15.707 5.435   1.00 11.82 ?  79  GLY   B CA   1 
ATOM   5057 C C    . GLY   B 1 79  ? 38.528 -15.714 4.544   1.00 11.61 ?  79  GLY   B C    1 
ATOM   5058 O O    . GLY   B 1 79  ? 39.148 -16.743 4.290   1.00 12.19 ?  79  GLY   B O    1 
ATOM   5059 H H    . GLY   B 1 79  ? 37.502 -17.212 6.654   1.00 14.81 ?  79  GLY   B H    1 
ATOM   5060 H HA2  . GLY   B 1 79  ? 36.536 -15.399 4.903   1.00 14.16 ?  79  GLY   B HA2  1 
ATOM   5061 H HA3  . GLY   B 1 79  ? 37.437 -15.070 6.150   1.00 14.16 ?  79  GLY   B HA3  1 
ATOM   5062 N N    . SER   B 1 80  ? 38.887 -14.519 4.072   1.00 11.99 ?  80  SER   B N    1 
ATOM   5063 C CA   . SER   B 1 80  ? 39.997 -14.381 3.141   1.00 11.85 ?  80  SER   B CA   1 
ATOM   5064 C C    . SER   B 1 80  ? 40.575 -12.974 3.212   1.00 12.08 ?  80  SER   B C    1 
ATOM   5065 O O    . SER   B 1 80  ? 39.954 -12.043 3.733   1.00 13.21 ?  80  SER   B O    1 
ATOM   5066 C CB   . SER   B 1 80  ? 39.554 -14.664 1.702   1.00 11.99 ?  80  SER   B CB   1 
ATOM   5067 O OG   . SER   B 1 80  ? 38.714 -13.638 1.206   1.00 12.93 ?  80  SER   B OG   1 
ATOM   5068 H H    . SER   B 1 80  ? 38.504 -13.775 4.276   1.00 14.37 ?  80  SER   B H    1 
ATOM   5069 H HA   . SER   B 1 80  ? 40.687 -15.011 3.385   1.00 14.20 ?  80  SER   B HA   1 
ATOM   5070 H HB2  . SER   B 1 80  ? 40.337 -14.721 1.134   1.00 14.36 ?  80  SER   B HB2  1 
ATOM   5071 H HB3  . SER   B 1 80  ? 39.067 -15.502 1.680   1.00 14.36 ?  80  SER   B HB3  1 
ATOM   5072 H HG   . SER   B 1 80  ? 38.025 -13.574 1.691   1.00 15.50 ?  80  SER   B HG   1 
ATOM   5073 N N    . CYS   B 1 81  ? 41.757 -12.822 2.620   1.00 11.75 ?  81  CYS   B N    1 
ATOM   5074 C CA   . CYS   B 1 81  ? 42.300 -11.505 2.329   1.00 11.68 ?  81  CYS   B CA   1 
ATOM   5075 C C    . CYS   B 1 81  ? 43.078 -11.585 1.026   1.00 11.25 ?  81  CYS   B C    1 
ATOM   5076 O O    . CYS   B 1 81  ? 43.587 -12.650 0.653   1.00 12.27 ?  81  CYS   B O    1 
ATOM   5077 C CB   . CYS   B 1 81  ? 43.184 -10.968 3.464   1.00 12.65 ?  81  CYS   B CB   1 
ATOM   5078 S SG   . CYS   B 1 81  ? 44.711 -11.903 3.696   1.00 12.90 ?  81  CYS   B SG   1 
ATOM   5079 H H    . CYS   B 1 81  ? 42.263 -13.470 2.365   1.00 14.08 ?  81  CYS   B H    1 
ATOM   5080 H HA   . CYS   B 1 81  ? 41.569 -10.878 2.208   1.00 13.99 ?  81  CYS   B HA   1 
ATOM   5081 H HB2  . CYS   B 1 81  ? 43.429 -10.054 3.273   1.00 15.15 ?  81  CYS   B HB2  1 
ATOM   5082 H HB3  . CYS   B 1 81  ? 42.684 -11.009 4.298   1.00 15.15 ?  81  CYS   B HB3  1 
ATOM   5083 H HG   . CYS   B 1 81  ? 45.333 -11.422 4.607   1.00 15.46 ?  81  CYS   B HG   1 
ATOM   5084 N N    . VAL   B 1 82  ? 43.176 -10.442 0.352   1.00 11.87 ?  82  VAL   B N    1 
ATOM   5085 C CA   . VAL   B 1 82  ? 43.935 -10.312 -0.886  1.00 11.64 ?  82  VAL   B CA   1 
ATOM   5086 C C    . VAL   B 1 82  ? 45.274 -9.671  -0.565  1.00 12.08 ?  82  VAL   B C    1 
ATOM   5087 O O    . VAL   B 1 82  ? 45.321 -8.559  -0.021  1.00 13.03 ?  82  VAL   B O    1 
ATOM   5088 C CB   . VAL   B 1 82  ? 43.185 -9.470  -1.928  1.00 12.79 ?  82  VAL   B CB   1 
ATOM   5089 C CG1  . VAL   B 1 82  ? 44.030 -9.312  -3.181  1.00 14.19 ?  82  VAL   B CG1  1 
ATOM   5090 C CG2  . VAL   B 1 82  ? 41.841 -10.087 -2.249  1.00 13.73 ?  82  VAL   B CG2  1 
ATOM   5091 H H    . VAL   B 1 82  ? 42.792 -9.705  0.596   1.00 14.22 ?  82  VAL   B H    1 
ATOM   5092 H HA   . VAL   B 1 82  ? 44.094 -11.192 -1.257  1.00 13.94 ?  82  VAL   B HA   1 
ATOM   5093 H HB   . VAL   B 1 82  ? 43.025 -8.588  -1.564  1.00 15.32 ?  82  VAL   B HB   1 
ATOM   5094 H HG11 . VAL   B 1 82  ? 43.465 -9.002  -3.904  1.00 17.01 ?  82  VAL   B HG11 1 
ATOM   5095 H HG12 . VAL   B 1 82  ? 44.733 -8.664  -3.010  1.00 17.01 ?  82  VAL   B HG12 1 
ATOM   5096 H HG13 . VAL   B 1 82  ? 44.419 -10.171 -3.410  1.00 17.01 ?  82  VAL   B HG13 1 
ATOM   5097 H HG21 . VAL   B 1 82  ? 41.403 -9.559  -2.937  1.00 16.46 ?  82  VAL   B HG21 1 
ATOM   5098 H HG22 . VAL   B 1 82  ? 41.973 -10.996 -2.567  1.00 16.46 ?  82  VAL   B HG22 1 
ATOM   5099 H HG23 . VAL   B 1 82  ? 41.293 -10.097 -1.447  1.00 16.46 ?  82  VAL   B HG23 1 
ATOM   5100 N N    . LEU   B 1 83  ? 46.356 -10.350 -0.934  1.00 11.43 ?  83  LEU   B N    1 
ATOM   5101 C CA   . LEU   B 1 83  ? 47.709 -9.833  -0.810  1.00 11.47 ?  83  LEU   B CA   1 
ATOM   5102 C C    . LEU   B 1 83  ? 48.410 -9.968  -2.161  1.00 11.24 ?  83  LEU   B C    1 
ATOM   5103 O O    . LEU   B 1 83  ? 47.807 -10.379 -3.157  1.00 11.51 ?  83  LEU   B O    1 
ATOM   5104 C CB   . LEU   B 1 83  ? 48.462 -10.522 0.333   1.00 12.09 ?  83  LEU   B CB   1 
ATOM   5105 C CG   . LEU   B 1 83  ? 47.954 -10.162 1.733   1.00 13.64 ?  83  LEU   B CG   1 
ATOM   5106 C CD1  . LEU   B 1 83  ? 48.570 -11.046 2.798   1.00 13.88 ?  83  LEU   B CD1  1 
ATOM   5107 C CD2  . LEU   B 1 83  ? 48.187 -8.686  2.074   1.00 14.41 ?  83  LEU   B CD2  1 
ATOM   5108 H H    . LEU   B 1 83  ? 46.321 -11.141 -1.280  1.00 13.69 ?  83  LEU   B H    1 
ATOM   5109 H HA   . LEU   B 1 83  ? 47.654 -8.890  -0.602  1.00 13.74 ?  83  LEU   B HA   1 
ATOM   5110 H HB2  . LEU   B 1 83  ? 48.381 -11.480 0.230   1.00 14.49 ?  83  LEU   B HB2  1 
ATOM   5111 H HB3  . LEU   B 1 83  ? 49.397 -10.264 0.285   1.00 14.49 ?  83  LEU   B HB3  1 
ATOM   5112 H HG   . LEU   B 1 83  ? 47.002 -10.312 1.757   1.00 16.35 ?  83  LEU   B HG   1 
ATOM   5113 H HD11 . LEU   B 1 83  ? 48.218 -10.794 3.666   1.00 16.63 ?  83  LEU   B HD11 1 
ATOM   5114 H HD12 . LEU   B 1 83  ? 48.342 -11.974 2.609   1.00 16.63 ?  83  LEU   B HD12 1 
ATOM   5115 H HD13 . LEU   B 1 83  ? 49.535 -10.940 2.789   1.00 16.63 ?  83  LEU   B HD13 1 
ATOM   5116 H HD21 . LEU   B 1 83  ? 47.982 -8.541  3.012   1.00 17.27 ?  83  LEU   B HD21 1 
ATOM   5117 H HD22 . LEU   B 1 83  ? 49.118 -8.463  1.904   1.00 17.27 ?  83  LEU   B HD22 1 
ATOM   5118 H HD23 . LEU   B 1 83  ? 47.610 -8.139  1.520   1.00 17.27 ?  83  LEU   B HD23 1 
ATOM   5119 N N    . SER   B 1 84  ? 49.687 -9.597  -2.208  1.00 12.71 ?  84  SER   B N    1 
ATOM   5120 C CA   . SER   B 1 84  ? 50.424 -9.709  -3.456  1.00 12.87 ?  84  SER   B CA   1 
ATOM   5121 C C    . SER   B 1 84  ? 50.577 -11.168 -3.876  1.00 12.10 ?  84  SER   B C    1 
ATOM   5122 O O    . SER   B 1 84  ? 50.687 -12.072 -3.047  1.00 11.75 ?  84  SER   B O    1 
ATOM   5123 C CB   . SER   B 1 84  ? 51.816 -9.108  -3.301  1.00 14.73 ?  84  SER   B CB   1 
ATOM   5124 O OG   . SER   B 1 84  ? 52.562 -9.312  -4.484  1.00 16.57 ?  84  SER   B OG   1 
ATOM   5125 H H    . SER   B 1 84  ? 50.135 -9.275  -1.548  1.00 15.23 ?  84  SER   B H    1 
ATOM   5126 H HA   . SER   B 1 84  ? 49.957 -9.236  -4.158  1.00 15.42 ?  84  SER   B HA   1 
ATOM   5127 H HB2  . SER   B 1 84  ? 51.734 -8.151  -3.136  1.00 17.65 ?  84  SER   B HB2  1 
ATOM   5128 H HB3  . SER   B 1 84  ? 52.274 -9.533  -2.562  1.00 17.65 ?  84  SER   B HB3  1 
ATOM   5129 H HG   . SER   B 1 84  ? 53.330 -8.970  -4.405  1.00 19.86 ?  84  SER   B HG   1 
ATOM   5130 N N    . GLY   B 1 85  ? 50.637 -11.383 -5.184  1.00 13.08 ?  85  GLY   B N    1 
ATOM   5131 C CA   . GLY   B 1 85  ? 50.988 -12.672 -5.729  1.00 13.72 ?  85  GLY   B CA   1 
ATOM   5132 C C    . GLY   B 1 85  ? 52.457 -12.855 -6.033  1.00 13.04 ?  85  GLY   B C    1 
ATOM   5133 O O    . GLY   B 1 85  ? 52.834 -13.927 -6.504  1.00 13.54 ?  85  GLY   B O    1 
ATOM   5134 H H    . GLY   B 1 85  ? 50.486 -10.790 -5.777  1.00 15.67 ?  85  GLY   B H    1 
ATOM   5135 H HA2  . GLY   B 1 85  ? 50.727 -13.367 -5.098  1.00 16.44 ?  85  GLY   B HA2  1 
ATOM   5136 H HA3  . GLY   B 1 85  ? 50.496 -12.815 -6.547  1.00 16.44 ?  85  GLY   B HA3  1 
ATOM   5137 N N    . HIS   B 1 86  ? 53.305 -11.854 -5.800  1.00 12.86 ?  86  HIS   B N    1 
ATOM   5138 C CA   . HIS   B 1 86  ? 54.765 -12.019 -5.878  1.00 12.71 ?  86  HIS   B CA   1 
ATOM   5139 C C    . HIS   B 1 86  ? 55.136 -12.528 -7.269  1.00 13.16 ?  86  HIS   B C    1 
ATOM   5140 O O    . HIS   B 1 86  ? 54.755 -11.904 -8.271  1.00 13.95 ?  86  HIS   B O    1 
ATOM   5141 C CB   . HIS   B 1 86  ? 55.249 -12.871 -4.706  1.00 13.34 ?  86  HIS   B CB   1 
ATOM   5142 C CG   . HIS   B 1 86  ? 54.937 -12.269 -3.379  1.00 13.26 ?  86  HIS   B CG   1 
ATOM   5143 N ND1  . HIS   B 1 86  ? 55.761 -11.352 -2.762  1.00 15.05 ?  86  HIS   B ND1  1 
ATOM   5144 C CD2  . HIS   B 1 86  ? 53.862 -12.420 -2.571  1.00 13.51 ?  86  HIS   B CD2  1 
ATOM   5145 C CE1  . HIS   B 1 86  ? 55.204 -10.968 -1.627  1.00 14.52 ?  86  HIS   B CE1  1 
ATOM   5146 N NE2  . HIS   B 1 86  ? 54.050 -11.597 -1.489  1.00 13.60 ?  86  HIS   B NE2  1 
ATOM   5147 H H    . HIS   B 1 86  ? 53.060 -11.059 -5.596  1.00 15.41 ?  86  HIS   B H    1 
ATOM   5148 H HA   . HIS   B 1 86  ? 55.174 -11.147 -5.778  1.00 15.23 ?  86  HIS   B HA   1 
ATOM   5149 H HB2  . HIS   B 1 86  ? 54.827 -13.742 -4.751  1.00 15.99 ?  86  HIS   B HB2  1 
ATOM   5150 H HB3  . HIS   B 1 86  ? 56.216 -12.972 -4.767  1.00 15.99 ?  86  HIS   B HB3  1 
ATOM   5151 H HD2  . HIS   B 1 86  ? 53.125 -12.967 -2.727  1.00 16.19 ?  86  HIS   B HD2  1 
ATOM   5152 H HE1  . HIS   B 1 86  ? 55.573 -10.367 -1.020  1.00 17.41 ?  86  HIS   B HE1  1 
ATOM   5153 H HE2  . HIS   B 1 86  ? 53.515 -11.518 -0.821  1.00 16.29 ?  86  HIS   B HE2  1 
ATOM   5154 N N    . ASN   B 1 87  ? 55.894 -13.615 -7.378  1.00 13.43 ?  87  ASN   B N    1 
ATOM   5155 C CA   . ASN   B 1 87  ? 56.299 -14.185 -8.654  1.00 14.53 ?  87  ASN   B CA   1 
ATOM   5156 C C    . ASN   B 1 87  ? 55.322 -15.229 -9.162  1.00 13.97 ?  87  ASN   B C    1 
ATOM   5157 O O    . ASN   B 1 87  ? 55.642 -15.941 -10.117 1.00 15.62 ?  87  ASN   B O    1 
ATOM   5158 C CB   . ASN   B 1 87  ? 57.697 -14.808 -8.535  1.00 16.16 ?  87  ASN   B CB   1 
ATOM   5159 C CG   . ASN   B 1 87  ? 57.753 -15.929 -7.511  1.00 16.95 ?  87  ASN   B CG   1 
ATOM   5160 O OD1  . ASN   B 1 87  ? 57.112 -15.859 -6.461  1.00 15.98 ?  87  ASN   B OD1  1 
ATOM   5161 N ND2  . ASN   B 1 87  ? 58.505 -16.987 -7.826  1.00 19.08 ?  87  ASN   B ND2  1 
ATOM   5162 H H    . ASN   B 1 87  ? 56.196 -14.056 -6.701  1.00 16.10 ?  87  ASN   B H    1 
ATOM   5163 H HA   . ASN   B 1 87  ? 56.347 -13.477 -9.310  1.00 17.42 ?  87  ASN   B HA   1 
ATOM   5164 H HB2  . ASN   B 1 87  ? 57.956 -15.171 -9.397  1.00 19.36 ?  87  ASN   B HB2  1 
ATOM   5165 H HB3  . ASN   B 1 87  ? 58.328 -14.121 -8.263  1.00 19.36 ?  87  ASN   B HB3  1 
ATOM   5166 H HD21 . ASN   B 1 87  ? 58.570 -17.645 -7.280  1.00 22.87 ?  87  ASN   B HD21 1 
ATOM   5167 H HD22 . ASN   B 1 87  ? 58.935 -17.002 -8.573  1.00 22.87 ?  87  ASN   B HD22 1 
ATOM   5168 N N    . LEU   B 1 88  ? 54.140 -15.324 -8.555  1.00 12.85 ?  88  LEU   B N    1 
ATOM   5169 C CA   . LEU   B 1 88  ? 53.164 -16.358 -8.880  1.00 13.19 ?  88  LEU   B CA   1 
ATOM   5170 C C    . LEU   B 1 88  ? 51.934 -15.839 -9.602  1.00 13.05 ?  88  LEU   B C    1 
ATOM   5171 O O    . LEU   B 1 88  ? 51.327 -16.587 -10.379 1.00 14.76 ?  88  LEU   B O    1 
ATOM   5172 C CB   . LEU   B 1 88  ? 52.693 -17.039 -7.592  1.00 14.28 ?  88  LEU   B CB   1 
ATOM   5173 C CG   . LEU   B 1 88  ? 53.798 -17.689 -6.778  1.00 16.39 ?  88  LEU   B CG   1 
ATOM   5174 C CD1  . LEU   B 1 88  ? 53.280 -18.034 -5.395  1.00 18.17 ?  88  LEU   B CD1  1 
ATOM   5175 C CD2  . LEU   B 1 88  ? 54.291 -18.923 -7.500  1.00 19.29 ?  88  LEU   B CD2  1 
ATOM   5176 H H    . LEU   B 1 88  ? 53.878 -14.792 -7.928  1.00 15.40 ?  88  LEU   B H    1 
ATOM   5177 H HA   . LEU   B 1 88  ? 53.580 -17.025 -9.441  1.00 15.81 ?  88  LEU   B HA   1 
ATOM   5178 H HB2  . LEU   B 1 88  ? 52.260 -16.381 -7.027  1.00 17.11 ?  88  LEU   B HB2  1 
ATOM   5179 H HB3  . LEU   B 1 88  ? 52.056 -17.736 -7.826  1.00 17.11 ?  88  LEU   B HB3  1 
ATOM   5180 H HG   . LEU   B 1 88  ? 54.541 -17.068 -6.682  1.00 19.65 ?  88  LEU   B HG   1 
ATOM   5181 H HD11 . LEU   B 1 88  ? 53.903 -18.636 -4.964  1.00 21.78 ?  88  LEU   B HD11 1 
ATOM   5182 H HD12 . LEU   B 1 88  ? 53.192 -17.218 -4.878  1.00 21.78 ?  88  LEU   B HD12 1 
ATOM   5183 H HD13 . LEU   B 1 88  ? 52.413 -18.461 -5.487  1.00 21.78 ?  88  LEU   B HD13 1 
ATOM   5184 H HD21 . LEU   B 1 88  ? 54.944 -19.374 -6.943  1.00 23.12 ?  88  LEU   B HD21 1 
ATOM   5185 H HD22 . LEU   B 1 88  ? 53.538 -19.509 -7.669  1.00 23.12 ?  88  LEU   B HD22 1 
ATOM   5186 H HD23 . LEU   B 1 88  ? 54.699 -18.657 -8.339  1.00 23.12 ?  88  LEU   B HD23 1 
ATOM   5187 N N    . ALA   B 1 89  ? 51.534 -14.601 -9.340  1.00 12.80 ?  89  ALA   B N    1 
ATOM   5188 C CA   . ALA   B 1 89  ? 50.235 -14.118 -9.780  1.00 12.08 ?  89  ALA   B CA   1 
ATOM   5189 C C    . ALA   B 1 89  ? 50.203 -12.628 -9.510  1.00 12.19 ?  89  ALA   B C    1 
ATOM   5190 O O    . ALA   B 1 89  ? 51.045 -12.104 -8.781  1.00 13.16 ?  89  ALA   B O    1 
ATOM   5191 C CB   . ALA   B 1 89  ? 49.111 -14.793 -8.997  1.00 11.97 ?  89  ALA   B CB   1 
ATOM   5192 H H    . ALA   B 1 89  ? 51.989 -14.017 -8.892  1.00 15.33 ?  89  ALA   B H    1 
ATOM   5193 H HA   . ALA   B 1 89  ? 50.115 -14.278 -10.728 1.00 14.48 ?  89  ALA   B HA   1 
ATOM   5194 H HB1  . ALA   B 1 89  ? 48.257 -14.464 -9.319  1.00 14.34 ?  89  ALA   B HB1  1 
ATOM   5195 H HB2  . ALA   B 1 89  ? 49.166 -15.754 -9.134  1.00 14.34 ?  89  ALA   B HB2  1 
ATOM   5196 H HB3  . ALA   B 1 89  ? 49.212 -14.588 -8.056  1.00 14.34 ?  89  ALA   B HB3  1 
ATOM   5197 N N    . LYS   B 1 90  ? 49.203 -11.947 -10.067 1.00 13.05 ?  90  LYS   B N    1 
ATOM   5198 C CA   . LYS   B 1 90  ? 49.010 -10.558 -9.668  1.00 13.56 ?  90  LYS   B CA   1 
ATOM   5199 C C    . LYS   B 1 90  ? 48.691 -10.480 -8.178  1.00 13.22 ?  90  LYS   B C    1 
ATOM   5200 O O    . LYS   B 1 90  ? 49.331 -9.733  -7.425  1.00 14.57 ?  90  LYS   B O    1 
ATOM   5201 C CB   . LYS   B 1 90  ? 47.931 -9.901  -10.525 1.00 15.08 ?  90  LYS   B CB   1 
ATOM   5202 C CG   . LYS   B 1 90  ? 47.635 -8.466  -10.139 1.00 15.97 ?  90  LYS   B CG   1 
ATOM   5203 C CD   . LYS   B 1 90  ? 48.841 -7.565  -10.218 1.00 19.06 ?  90  LYS   B CD   1 
ATOM   5204 C CE   . LYS   B 1 90  ? 48.396 -6.138  -10.001 1.00 21.25 ?  90  LYS   B CE   1 
ATOM   5205 N NZ   . LYS   B 1 90  ? 49.536 -5.192  -9.943  1.00 21.08 ?  90  LYS   B NZ   1 
ATOM   5206 H H    . LYS   B 1 90  ? 48.643 -12.249 -10.648 1.00 15.64 ?  90  LYS   B H    1 
ATOM   5207 H HA   . LYS   B 1 90  ? 49.837 -10.079 -9.817  1.00 16.24 ?  90  LYS   B HA   1 
ATOM   5208 H HB2  . LYS   B 1 90  ? 48.223 -9.904  -11.452 1.00 18.08 ?  90  LYS   B HB2  1 
ATOM   5209 H HB3  . LYS   B 1 90  ? 47.108 -10.409 -10.441 1.00 18.08 ?  90  LYS   B HB3  1 
ATOM   5210 H HG2  . LYS   B 1 90  ? 46.959 -8.115  -10.741 1.00 19.14 ?  90  LYS   B HG2  1 
ATOM   5211 H HG3  . LYS   B 1 90  ? 47.300 -8.446  -9.227  1.00 19.14 ?  90  LYS   B HG3  1 
ATOM   5212 H HD2  . LYS   B 1 90  ? 49.475 -7.803  -9.522  1.00 22.85 ?  90  LYS   B HD2  1 
ATOM   5213 H HD3  . LYS   B 1 90  ? 49.249 -7.638  -11.094 1.00 22.85 ?  90  LYS   B HD3  1 
ATOM   5214 H HE2  . LYS   B 1 90  ? 47.822 -5.867  -10.736 1.00 25.48 ?  90  LYS   B HE2  1 
ATOM   5215 H HE3  . LYS   B 1 90  ? 47.914 -6.074  -9.163  1.00 25.48 ?  90  LYS   B HE3  1 
ATOM   5216 H HZ1  . LYS   B 1 90  ? 49.241 -4.360  -9.817  1.00 25.27 ?  90  LYS   B HZ1  1 
ATOM   5217 H HZ2  . LYS   B 1 90  ? 50.081 -5.408  -9.273  1.00 25.27 ?  90  LYS   B HZ2  1 
ATOM   5218 H HZ3  . LYS   B 1 90  ? 49.997 -5.218  -10.707 1.00 25.27 ?  90  LYS   B HZ3  1 
ATOM   5219 N N    . HIS   B 1 91  ? 47.738 -11.299 -7.729  1.00 11.72 ?  91  HIS   B N    1 
ATOM   5220 C CA   . HIS   B 1 91  ? 47.271 -11.321 -6.357  1.00 11.86 ?  91  HIS   B CA   1 
ATOM   5221 C C    . HIS   B 1 91  ? 47.278 -12.749 -5.843  1.00 11.13 ?  91  HIS   B C    1 
ATOM   5222 O O    . HIS   B 1 91  ? 47.050 -13.703 -6.598  1.00 11.43 ?  91  HIS   B O    1 
ATOM   5223 C CB   . HIS   B 1 91  ? 45.814 -10.852 -6.239  1.00 13.52 ?  91  HIS   B CB   1 
ATOM   5224 C CG   . HIS   B 1 91  ? 45.591 -9.451  -6.689  1.00 16.83 ?  91  HIS   B CG   1 
ATOM   5225 N ND1  . HIS   B 1 91  ? 46.170 -8.366  -6.064  1.00 19.19 ?  91  HIS   B ND1  1 
ATOM   5226 C CD2  . HIS   B 1 91  ? 44.830 -8.950  -7.687  1.00 19.11 ?  91  HIS   B CD2  1 
ATOM   5227 C CE1  . HIS   B 1 91  ? 45.787 -7.255  -6.669  1.00 20.19 ?  91  HIS   B CE1  1 
ATOM   5228 N NE2  . HIS   B 1 91  ? 44.968 -7.583  -7.655  1.00 20.44 ?  91  HIS   B NE2  1 
ATOM   5229 H H    . HIS   B 1 91  ? 47.336 -11.873 -8.226  1.00 14.04 ?  91  HIS   B H    1 
ATOM   5230 H HA   . HIS   B 1 91  ? 47.836 -10.765 -5.791  1.00 14.21 ?  91  HIS   B HA   1 
ATOM   5231 H HB2  . HIS   B 1 91  ? 45.256 -11.429 -6.783  1.00 16.20 ?  91  HIS   B HB2  1 
ATOM   5232 H HB3  . HIS   B 1 91  ? 45.538 -10.914 -5.309  1.00 16.20 ?  91  HIS   B HB3  1 
ATOM   5233 H HD1  . HIS   B 1 91  ? 46.700 -8.408  -5.385  1.00 23.00 ?  91  HIS   B HD1  1 
ATOM   5234 H HD2  . HIS   B 1 91  ? 44.316 -9.431  -8.288  1.00 22.91 ?  91  HIS   B HD2  1 
ATOM   5235 H HE1  . HIS   B 1 91  ? 46.047 -6.392  -6.432  1.00 24.20 ?  91  HIS   B HE1  1 
ATOM   5236 N N    . CYS   B 1 92  ? 47.480 -12.885 -4.541  1.00 10.79 ?  92  CYS   B N    1 
ATOM   5237 C CA   . CYS   B 1 92  ? 47.183 -14.121 -3.832  1.00 10.67 ?  92  CYS   B CA   1 
ATOM   5238 C C    . CYS   B 1 92  ? 45.965 -13.890 -2.947  1.00 10.29 ?  92  CYS   B C    1 
ATOM   5239 O O    . CYS   B 1 92  ? 45.962 -12.990 -2.097  1.00 11.41 ?  92  CYS   B O    1 
ATOM   5240 C CB   . CYS   B 1 92  ? 48.365 -14.577 -2.982  1.00 11.36 ?  92  CYS   B CB   1 
ATOM   5241 S SG   . CYS   B 1 92  ? 48.009 -16.117 -2.087  1.00 11.37 ?  92  CYS   B SG   1 
ATOM   5242 H H    . CYS   B 1 92  ? 47.812 -12.268 -4.036  1.00 12.92 ?  92  CYS   B H    1 
ATOM   5243 H HA   . CYS   B 1 92  ? 46.984 -14.819 -4.474  1.00 12.78 ?  92  CYS   B HA   1 
ATOM   5244 H HB2  . CYS   B 1 92  ? 49.130 -14.732 -3.554  1.00 13.60 ?  92  CYS   B HB2  1 
ATOM   5245 H HB3  . CYS   B 1 92  ? 48.567 -13.890 -2.328  1.00 13.60 ?  92  CYS   B HB3  1 
ATOM   5246 H HG   . CYS   B 1 92  ? 48.983 -16.434 -1.462  1.00 13.62 ?  92  CYS   B HG   1 
ATOM   5247 N N    . LEU   B 1 93  ? 44.931 -14.697 -3.166  1.00 10.12 ?  93  LEU   B N    1 
ATOM   5248 C CA   . LEU   B 1 93  ? 43.757 -14.722 -2.306  1.00 10.36 ?  93  LEU   B CA   1 
ATOM   5249 C C    . LEU   B 1 93  ? 43.982 -15.789 -1.242  1.00 9.83  ?  93  LEU   B C    1 
ATOM   5250 O O    . LEU   B 1 93  ? 43.942 -16.992 -1.537  1.00 10.48 ?  93  LEU   B O    1 
ATOM   5251 C CB   . LEU   B 1 93  ? 42.495 -15.004 -3.118  1.00 10.92 ?  93  LEU   B CB   1 
ATOM   5252 C CG   . LEU   B 1 93  ? 41.204 -15.041 -2.307  1.00 11.53 ?  93  LEU   B CG   1 
ATOM   5253 C CD1  . LEU   B 1 93  ? 40.842 -13.657 -1.795  1.00 11.72 ?  93  LEU   B CD1  1 
ATOM   5254 C CD2  . LEU   B 1 93  ? 40.082 -15.614 -3.153  1.00 11.92 ?  93  LEU   B CD2  1 
ATOM   5255 H H    . LEU   B 1 93  ? 44.889 -15.265 -3.825  1.00 12.12 ?  93  LEU   B H    1 
ATOM   5256 H HA   . LEU   B 1 93  ? 43.661 -13.863 -1.873  1.00 12.41 ?  93  LEU   B HA   1 
ATOM   5257 H HB2  . LEU   B 1 93  ? 42.399 -14.306 -3.790  1.00 13.08 ?  93  LEU   B HB2  1 
ATOM   5258 H HB3  . LEU   B 1 93  ? 42.592 -15.862 -3.556  1.00 13.08 ?  93  LEU   B HB3  1 
ATOM   5259 H HG   . LEU   B 1 93  ? 41.325 -15.619 -1.542  1.00 13.81 ?  93  LEU   B HG   1 
ATOM   5260 H HD11 . LEU   B 1 93  ? 39.990 -13.702 -1.336  1.00 14.04 ?  93  LEU   B HD11 1 
ATOM   5261 H HD12 . LEU   B 1 93  ? 41.533 -13.354 -1.184  1.00 14.04 ?  93  LEU   B HD12 1 
ATOM   5262 H HD13 . LEU   B 1 93  ? 40.779 -13.047 -2.549  1.00 14.04 ?  93  LEU   B HD13 1 
ATOM   5263 H HD21 . LEU   B 1 93  ? 39.265 -15.622 -2.631  1.00 14.28 ?  93  LEU   B HD21 1 
ATOM   5264 H HD22 . LEU   B 1 93  ? 39.964 -15.058 -3.942  1.00 14.28 ?  93  LEU   B HD22 1 
ATOM   5265 H HD23 . LEU   B 1 93  ? 40.315 -16.517 -3.419  1.00 14.28 ?  93  LEU   B HD23 1 
ATOM   5266 N N    . HIS   B 1 94  ? 44.252 -15.359 -0.017  1.00 9.94  ?  94  HIS   B N    1 
ATOM   5267 C CA   . HIS   B 1 94  ? 44.477 -16.270 1.099   1.00 10.19 ?  94  HIS   B CA   1 
ATOM   5268 C C    . HIS   B 1 94  ? 43.117 -16.627 1.680   1.00 10.76 ?  94  HIS   B C    1 
ATOM   5269 O O    . HIS   B 1 94  ? 42.453 -15.758 2.249   1.00 12.05 ?  94  HIS   B O    1 
ATOM   5270 C CB   . HIS   B 1 94  ? 45.348 -15.592 2.153   1.00 10.49 ?  94  HIS   B CB   1 
ATOM   5271 C CG   . HIS   B 1 94  ? 46.730 -15.291 1.683   1.00 10.52 ?  94  HIS   B CG   1 
ATOM   5272 N ND1  . HIS   B 1 94  ? 47.761 -16.201 1.771   1.00 11.15 ?  94  HIS   B ND1  1 
ATOM   5273 C CD2  . HIS   B 1 94  ? 47.236 -14.185 1.084   1.00 10.73 ?  94  HIS   B CD2  1 
ATOM   5274 C CE1  . HIS   B 1 94  ? 48.849 -15.651 1.259   1.00 11.14 ?  94  HIS   B CE1  1 
ATOM   5275 N NE2  . HIS   B 1 94  ? 48.562 -14.428 0.843   1.00 11.00 ?  94  HIS   B NE2  1 
ATOM   5276 H H    . HIS   B 1 94  ? 44.306 -14.524 0.196   1.00 11.91 ?  94  HIS   B H    1 
ATOM   5277 H HA   . HIS   B 1 94  ? 44.915 -17.076 0.788   1.00 12.21 ?  94  HIS   B HA   1 
ATOM   5278 H HB2  . HIS   B 1 94  ? 44.936 -14.753 2.407   1.00 12.56 ?  94  HIS   B HB2  1 
ATOM   5279 H HB3  . HIS   B 1 94  ? 45.422 -16.174 2.921   1.00 12.56 ?  94  HIS   B HB3  1 
ATOM   5280 H HD2  . HIS   B 1 94  ? 46.782 -13.401 0.884   1.00 12.85 ?  94  HIS   B HD2  1 
ATOM   5281 H HE1  . HIS   B 1 94  ? 49.688 -16.064 1.205   1.00 13.35 ?  94  HIS   B HE1  1 
ATOM   5282 H HE2  . HIS   B 1 94  ? 49.121 -13.888 0.470   1.00 13.17 ?  94  HIS   B HE2  1 
ATOM   5283 N N    . VAL   B 1 95  ? 42.686 -17.882 1.521   1.00 10.59 ?  95  VAL   B N    1 
ATOM   5284 C CA   . VAL   B 1 95  ? 41.361 -18.323 1.954   1.00 10.34 ?  95  VAL   B CA   1 
ATOM   5285 C C    . VAL   B 1 95  ? 41.530 -19.361 3.049   1.00 10.55 ?  95  VAL   B C    1 
ATOM   5286 O O    . VAL   B 1 95  ? 42.304 -20.313 2.889   1.00 11.10 ?  95  VAL   B O    1 
ATOM   5287 C CB   . VAL   B 1 95  ? 40.545 -18.921 0.796   1.00 10.75 ?  95  VAL   B CB   1 
ATOM   5288 C CG1  . VAL   B 1 95  ? 39.165 -19.365 1.280   1.00 11.93 ?  95  VAL   B CG1  1 
ATOM   5289 C CG2  . VAL   B 1 95  ? 40.435 -17.934 -0.345  1.00 11.07 ?  95  VAL   B CG2  1 
ATOM   5290 H H    . VAL   B 1 95  ? 43.150 -18.506 1.158   1.00 12.69 ?  95  VAL   B H    1 
ATOM   5291 H HA   . VAL   B 1 95  ? 40.866 -17.571 2.321   1.00 12.39 ?  95  VAL   B HA   1 
ATOM   5292 H HB   . VAL   B 1 95  ? 41.004 -19.706 0.465   1.00 12.88 ?  95  VAL   B HB   1 
ATOM   5293 H HG11 . VAL   B 1 95  ? 38.602 -19.565 0.506   1.00 14.29 ?  95  VAL   B HG11 1 
ATOM   5294 H HG12 . VAL   B 1 95  ? 39.249 -20.164 1.827   1.00 14.29 ?  95  VAL   B HG12 1 
ATOM   5295 H HG13 . VAL   B 1 95  ? 38.755 -18.653 1.798   1.00 14.29 ?  95  VAL   B HG13 1 
ATOM   5296 H HG21 . VAL   B 1 95  ? 39.853 -18.305 -1.026  1.00 13.26 ?  95  VAL   B HG21 1 
ATOM   5297 H HG22 . VAL   B 1 95  ? 40.066 -17.104 -0.008  1.00 13.26 ?  95  VAL   B HG22 1 
ATOM   5298 H HG23 . VAL   B 1 95  ? 41.319 -17.782 -0.710  1.00 13.26 ?  95  VAL   B HG23 1 
ATOM   5299 N N    . VAL   B 1 96  ? 40.799 -19.194 4.145   1.00 11.12 ?  96  VAL   B N    1 
ATOM   5300 C CA   . VAL   B 1 96  ? 40.881 -20.114 5.277   1.00 11.45 ?  96  VAL   B CA   1 
ATOM   5301 C C    . VAL   B 1 96  ? 39.692 -21.071 5.224   1.00 12.02 ?  96  VAL   B C    1 
ATOM   5302 O O    . VAL   B 1 96  ? 38.569 -20.716 5.595   1.00 12.47 ?  96  VAL   B O    1 
ATOM   5303 C CB   . VAL   B 1 96  ? 40.935 -19.372 6.615   1.00 12.20 ?  96  VAL   B CB   1 
ATOM   5304 C CG1  . VAL   B 1 96  ? 41.120 -20.360 7.757   1.00 12.65 ?  96  VAL   B CG1  1 
ATOM   5305 C CG2  . VAL   B 1 96  ? 42.040 -18.326 6.624   1.00 13.13 ?  96  VAL   B CG2  1 
ATOM   5306 H H    . VAL   B 1 96  ? 40.240 -18.551 4.263   1.00 13.32 ?  96  VAL   B H    1 
ATOM   5307 H HA   . VAL   B 1 96  ? 41.693 -20.640 5.201   1.00 13.71 ?  96  VAL   B HA   1 
ATOM   5308 H HB   . VAL   B 1 96  ? 40.092 -18.913 6.756   1.00 14.61 ?  96  VAL   B HB   1 
ATOM   5309 H HG11 . VAL   B 1 96  ? 41.296 -19.867 8.578   1.00 15.15 ?  96  VAL   B HG11 1 
ATOM   5310 H HG12 . VAL   B 1 96  ? 40.317 -20.889 7.859   1.00 15.15 ?  96  VAL   B HG12 1 
ATOM   5311 H HG13 . VAL   B 1 96  ? 41.877 -20.937 7.559   1.00 15.15 ?  96  VAL   B HG13 1 
ATOM   5312 H HG21 . VAL   B 1 96  ? 42.091 -17.921 7.508   1.00 15.73 ?  96  VAL   B HG21 1 
ATOM   5313 H HG22 . VAL   B 1 96  ? 42.884 -18.748 6.406   1.00 15.73 ?  96  VAL   B HG22 1 
ATOM   5314 H HG23 . VAL   B 1 96  ? 41.834 -17.639 5.966   1.00 15.73 ?  96  VAL   B HG23 1 
ATOM   5315 N N    . GLY   B 1 97  ? 39.930 -22.301 4.783   1.00 12.08 ?  97  GLY   B N    1 
ATOM   5316 C CA   . GLY   B 1 97  ? 38.956 -23.360 4.939   1.00 12.42 ?  97  GLY   B CA   1 
ATOM   5317 C C    . GLY   B 1 97  ? 39.060 -23.965 6.324   1.00 13.00 ?  97  GLY   B C    1 
ATOM   5318 O O    . GLY   B 1 97  ? 40.098 -23.851 6.989   1.00 13.67 ?  97  GLY   B O    1 
ATOM   5319 H H    . GLY   B 1 97  ? 40.661 -22.541 4.386   1.00 14.47 ?  97  GLY   B H    1 
ATOM   5320 H HA2  . GLY   B 1 97  ? 38.065 -22.995 4.808   1.00 14.89 ?  97  GLY   B HA2  1 
ATOM   5321 H HA3  . GLY   B 1 97  ? 39.112 -24.047 4.270   1.00 14.89 ?  97  GLY   B HA3  1 
ATOM   5322 N N    . PRO   B 1 98  ? 38.010 -24.649 6.779   1.00 13.37 ?  98  PRO   B N    1 
ATOM   5323 C CA   . PRO   B 1 98  ? 38.096 -25.345 8.066   1.00 14.36 ?  98  PRO   B CA   1 
ATOM   5324 C C    . PRO   B 1 98  ? 39.121 -26.464 8.019   1.00 14.13 ?  98  PRO   B C    1 
ATOM   5325 O O    . PRO   B 1 98  ? 39.230 -27.194 7.032   1.00 14.18 ?  98  PRO   B O    1 
ATOM   5326 C CB   . PRO   B 1 98  ? 36.680 -25.895 8.266   1.00 14.55 ?  98  PRO   B CB   1 
ATOM   5327 C CG   . PRO   B 1 98  ? 36.137 -26.025 6.885   1.00 14.14 ?  98  PRO   B CG   1 
ATOM   5328 C CD   . PRO   B 1 98  ? 36.698 -24.843 6.137   1.00 13.28 ?  98  PRO   B CD   1 
ATOM   5329 H HA   . PRO   B 1 98  ? 38.317 -24.725 8.774   1.00 17.21 ?  98  PRO   B HA   1 
ATOM   5330 H HB2  . PRO   B 1 98  ? 36.725 -26.761 8.702   1.00 17.43 ?  98  PRO   B HB2  1 
ATOM   5331 H HB3  . PRO   B 1 98  ? 36.157 -25.270 8.784   1.00 17.43 ?  98  PRO   B HB3  1 
ATOM   5332 H HG2  . PRO   B 1 98  ? 36.446 -26.860 6.493   1.00 16.94 ?  98  PRO   B HG2  1 
ATOM   5333 H HG3  . PRO   B 1 98  ? 35.172 -25.993 6.912   1.00 16.94 ?  98  PRO   B HG3  1 
ATOM   5334 H HD2  . PRO   B 1 98  ? 36.804 -25.057 5.193   1.00 15.91 ?  98  PRO   B HD2  1 
ATOM   5335 H HD3  . PRO   B 1 98  ? 36.140 -24.062 6.263   1.00 15.91 ?  98  PRO   B HD3  1 
ATOM   5336 N N    . ASN   B 1 99  ? 39.864 -26.598 9.106   1.00 14.78 ?  99  ASN   B N    1 
ATOM   5337 C CA   . ASN   B 1 99  ? 40.841 -27.669 9.265   1.00 15.53 ?  99  ASN   B CA   1 
ATOM   5338 C C    . ASN   B 1 99  ? 40.201 -28.752 10.132  1.00 17.35 ?  99  ASN   B C    1 
ATOM   5339 O O    . ASN   B 1 99  ? 40.093 -28.602 11.351  1.00 18.11 ?  99  ASN   B O    1 
ATOM   5340 C CB   . ASN   B 1 99  ? 42.112 -27.114 9.894   1.00 15.89 ?  99  ASN   B CB   1 
ATOM   5341 C CG   . ASN   B 1 99  ? 43.242 -28.118 9.899   1.00 16.56 ?  99  ASN   B CG   1 
ATOM   5342 O OD1  . ASN   B 1 99  ? 43.014 -29.309 10.066  1.00 17.42 ?  99  ASN   B OD1  1 
ATOM   5343 N ND2  . ASN   B 1 99  ? 44.464 -27.645 9.711   1.00 16.99 ?  99  ASN   B ND2  1 
ATOM   5344 H H    . ASN   B 1 99  ? 39.824 -26.070 9.782   1.00 17.71 ?  99  ASN   B H    1 
ATOM   5345 H HA   . ASN   B 1 99  ? 41.062 -28.056 8.403   1.00 18.61 ?  99  ASN   B HA   1 
ATOM   5346 H HB2  . ASN   B 1 99  ? 42.402 -26.344 9.394   1.00 19.05 ?  99  ASN   B HB2  1 
ATOM   5347 H HB3  . ASN   B 1 99  ? 41.921 -26.864 10.817  1.00 19.05 ?  99  ASN   B HB3  1 
ATOM   5348 H HD21 . ASN   B 1 99  ? 45.136 -28.179 9.714   1.00 20.37 ?  99  ASN   B HD21 1 
ATOM   5349 H HD22 . ASN   B 1 99  ? 44.579 -26.803 9.594   1.00 20.37 ?  99  ASN   B HD22 1 
ATOM   5350 N N    A VAL   B 1 100 ? 39.754 -29.835 9.489   0.60 18.97 ?  100 VAL   B N    1 
ATOM   5351 N N    B VAL   B 1 100 ? 39.765 -29.840 9.490   0.40 18.96 ?  100 VAL   B N    1 
ATOM   5352 C CA   A VAL   B 1 100 ? 39.138 -30.940 10.222  0.60 21.38 ?  100 VAL   B CA   1 
ATOM   5353 C CA   B VAL   B 1 100 ? 39.143 -30.947 10.214  0.40 21.13 ?  100 VAL   B CA   1 
ATOM   5354 C C    A VAL   B 1 100 ? 40.139 -31.595 11.165  0.60 21.87 ?  100 VAL   B C    1 
ATOM   5355 C C    B VAL   B 1 100 ? 40.138 -31.605 11.158  0.40 21.72 ?  100 VAL   B C    1 
ATOM   5356 O O    A VAL   B 1 100 ? 39.761 -32.097 12.230  0.60 22.54 ?  100 VAL   B O    1 
ATOM   5357 O O    B VAL   B 1 100 ? 39.756 -32.118 12.217  0.40 22.16 ?  100 VAL   B O    1 
ATOM   5358 C CB   A VAL   B 1 100 ? 38.510 -31.952 9.240   0.60 23.80 ?  100 VAL   B CB   1 
ATOM   5359 C CB   B VAL   B 1 100 ? 38.532 -31.956 9.220   0.40 23.02 ?  100 VAL   B CB   1 
ATOM   5360 C CG1  A VAL   B 1 100 ? 38.039 -33.200 9.974   0.60 24.78 ?  100 VAL   B CG1  1 
ATOM   5361 C CG1  B VAL   B 1 100 ? 38.016 -33.193 9.948   0.40 23.80 ?  100 VAL   B CG1  1 
ATOM   5362 C CG2  A VAL   B 1 100 ? 37.352 -31.314 8.485   0.60 24.53 ?  100 VAL   B CG2  1 
ATOM   5363 C CG2  B VAL   B 1 100 ? 37.416 -31.300 8.426   0.40 23.54 ?  100 VAL   B CG2  1 
ATOM   5364 H H    A VAL   B 1 100 ? 39.783 -29.949 8.637   0.60 22.74 ?  100 VAL   B H    1 
ATOM   5365 H H    B VAL   B 1 100 ? 39.814 -29.959 8.640   0.40 22.73 ?  100 VAL   B H    1 
ATOM   5366 H HA   A VAL   B 1 100 ? 38.418 -30.587 10.765  0.60 25.64 ?  100 VAL   B HA   1 
ATOM   5367 H HA   B VAL   B 1 100 ? 38.417 -30.600 10.754  0.40 25.34 ?  100 VAL   B HA   1 
ATOM   5368 H HB   A VAL   B 1 100 ? 39.175 -32.224 8.592   0.60 28.54 ?  100 VAL   B HB   1 
ATOM   5369 H HB   B VAL   B 1 100 ? 39.217 -32.244 8.597   0.40 27.59 ?  100 VAL   B HB   1 
ATOM   5370 H HG11 A VAL   B 1 100 ? 37.453 -33.709 9.389   0.60 29.72 ?  100 VAL   B HG11 1 
ATOM   5371 H HG11 B VAL   B 1 100 ? 37.448 -33.700 9.345   0.40 28.53 ?  100 VAL   B HG11 1 
ATOM   5372 H HG12 A VAL   B 1 100 ? 38.809 -33.739 10.214  0.60 29.72 ?  100 VAL   B HG12 1 
ATOM   5373 H HG12 B VAL   B 1 100 ? 38.768 -33.740 10.225  0.40 28.53 ?  100 VAL   B HG12 1 
ATOM   5374 H HG13 A VAL   B 1 100 ? 37.556 -32.936 10.773  0.60 29.72 ?  100 VAL   B HG13 1 
ATOM   5375 H HG13 B VAL   B 1 100 ? 37.504 -32.914 10.723  0.40 28.53 ?  100 VAL   B HG13 1 
ATOM   5376 H HG21 A VAL   B 1 100 ? 36.972 -31.970 7.878   0.60 29.42 ?  100 VAL   B HG21 1 
ATOM   5377 H HG21 B VAL   B 1 100 ? 37.025 -31.957 7.829   0.40 28.23 ?  100 VAL   B HG21 1 
ATOM   5378 H HG22 A VAL   B 1 100 ? 36.679 -31.026 9.122   0.60 29.42 ?  100 VAL   B HG22 1 
ATOM   5379 H HG22 B VAL   B 1 100 ? 36.743 -30.972 9.043   0.40 28.23 ?  100 VAL   B HG22 1 
ATOM   5380 H HG23 A VAL   B 1 100 ? 37.684 -30.554 7.985   0.60 29.42 ?  100 VAL   B HG23 1 
ATOM   5381 H HG23 B VAL   B 1 100 ? 37.785 -30.565 7.915   0.40 28.23 ?  100 VAL   B HG23 1 
ATOM   5382 N N    . ASN   B 1 101 ? 41.423 -31.613 10.795  1.00 22.23 ?  101 ASN   B N    1 
ATOM   5383 C CA   . ASN   B 1 101 ? 42.443 -32.156 11.689  1.00 24.90 ?  101 ASN   B CA   1 
ATOM   5384 C C    . ASN   B 1 101 ? 42.589 -31.329 12.962  1.00 27.34 ?  101 ASN   B C    1 
ATOM   5385 O O    . ASN   B 1 101 ? 43.159 -31.821 13.943  1.00 28.50 ?  101 ASN   B O    1 
ATOM   5386 C CB   . ASN   B 1 101 ? 43.784 -32.276 10.962  1.00 25.35 ?  101 ASN   B CB   1 
ATOM   5387 C CG   . ASN   B 1 101 ? 43.788 -33.393 9.934   1.00 25.45 ?  101 ASN   B CG   1 
ATOM   5388 O OD1  . ASN   B 1 101 ? 43.132 -34.418 10.114  1.00 26.38 ?  101 ASN   B OD1  1 
ATOM   5389 N ND2  . ASN   B 1 101 ? 44.525 -33.198 8.849   1.00 25.55 ?  101 ASN   B ND2  1 
ATOM   5390 H H    A ASN   B 1 101 ? 41.719 -31.326 10.038  0.60 26.66 ?  101 ASN   B H    1 
ATOM   5391 H H    B ASN   B 1 101 ? 41.721 -31.313 10.044  0.40 26.66 ?  101 ASN   B H    1 
ATOM   5392 H HA   . ASN   B 1 101 ? 42.176 -33.045 11.952  1.00 29.85 ?  101 ASN   B HA   1 
ATOM   5393 H HB2  . ASN   B 1 101 ? 43.980 -31.445 10.501  1.00 30.40 ?  101 ASN   B HB2  1 
ATOM   5394 H HB3  . ASN   B 1 101 ? 44.480 -32.465 11.611  1.00 30.40 ?  101 ASN   B HB3  1 
ATOM   5395 H HD21 . ASN   B 1 101 ? 44.557 -33.801 8.237   1.00 30.64 ?  101 ASN   B HD21 1 
ATOM   5396 H HD22 . ASN   B 1 101 ? 44.969 -32.466 8.755   1.00 30.64 ?  101 ASN   B HD22 1 
ATOM   5397 N N    A LYS   B 1 102 ? 42.114 -30.083 12.957  0.60 28.57 ?  102 LYS   B N    1 
ATOM   5398 N N    B LYS   B 1 102 ? 42.076 -30.097 12.969  0.40 28.50 ?  102 LYS   B N    1 
ATOM   5399 C CA   A LYS   B 1 102 ? 42.110 -29.225 14.134  0.60 30.57 ?  102 LYS   B CA   1 
ATOM   5400 C CA   B LYS   B 1 102 ? 41.995 -29.276 14.169  0.40 30.11 ?  102 LYS   B CA   1 
ATOM   5401 C C    A LYS   B 1 102 ? 40.744 -29.175 14.809  0.60 29.96 ?  102 LYS   B C    1 
ATOM   5402 C C    B LYS   B 1 102 ? 40.602 -29.278 14.788  0.40 29.59 ?  102 LYS   B C    1 
ATOM   5403 O O    A LYS   B 1 102 ? 40.541 -28.360 15.713  0.60 30.45 ?  102 LYS   B O    1 
ATOM   5404 O O    B LYS   B 1 102 ? 40.368 -28.547 15.755  0.40 29.90 ?  102 LYS   B O    1 
ATOM   5405 C CB   A LYS   B 1 102 ? 42.531 -27.801 13.762  0.60 33.27 ?  102 LYS   B CB   1 
ATOM   5406 C CB   B LYS   B 1 102 ? 42.397 -27.831 13.856  0.40 32.30 ?  102 LYS   B CB   1 
ATOM   5407 C CG   A LYS   B 1 102 ? 43.998 -27.624 13.406  0.60 35.82 ?  102 LYS   B CG   1 
ATOM   5408 C CG   B LYS   B 1 102 ? 43.849 -27.642 13.448  0.40 34.36 ?  102 LYS   B CG   1 
ATOM   5409 C CD   A LYS   B 1 102 ? 44.290 -26.166 13.071  0.60 38.04 ?  102 LYS   B CD   1 
ATOM   5410 C CD   B LYS   B 1 102 ? 44.112 -26.193 13.066  0.40 36.08 ?  102 LYS   B CD   1 
ATOM   5411 C CE   A LYS   B 1 102 ? 45.759 -25.933 12.763  0.60 39.71 ?  102 LYS   B CE   1 
ATOM   5412 C CE   B LYS   B 1 102 ? 45.573 -25.955 12.731  0.40 37.35 ?  102 LYS   B CE   1 
ATOM   5413 N NZ   A LYS   B 1 102 ? 46.029 -24.511 12.394  0.60 40.71 ?  102 LYS   B NZ   1 
ATOM   5414 N NZ   B LYS   B 1 102 ? 45.824 -24.547 12.313  0.40 38.08 ?  102 LYS   B NZ   1 
ATOM   5415 H H    A LYS   B 1 102 ? 41.775 -29.704 12.262  0.60 34.26 ?  102 LYS   B H    1 
ATOM   5416 H H    B LYS   B 1 102 ? 41.762 -29.707 12.269  0.40 34.17 ?  102 LYS   B H    1 
ATOM   5417 H HA   A LYS   B 1 102 ? 42.759 -29.567 14.770  0.60 36.66 ?  102 LYS   B HA   1 
ATOM   5418 H HA   B LYS   B 1 102 ? 42.618 -29.621 14.826  0.40 36.11 ?  102 LYS   B HA   1 
ATOM   5419 H HB2  A LYS   B 1 102 ? 42.009 -27.516 12.996  0.60 39.90 ?  102 LYS   B HB2  1 
ATOM   5420 H HB2  B LYS   B 1 102 ? 41.844 -27.505 13.129  0.40 38.74 ?  102 LYS   B HB2  1 
ATOM   5421 H HB3  A LYS   B 1 102 ? 42.343 -27.218 14.515  0.60 39.90 ?  102 LYS   B HB3  1 
ATOM   5422 H HB3  B LYS   B 1 102 ? 42.243 -27.290 14.648  0.40 38.74 ?  102 LYS   B HB3  1 
ATOM   5423 H HG2  A LYS   B 1 102 ? 44.549 -27.880 14.162  0.60 42.95 ?  102 LYS   B HG2  1 
ATOM   5424 H HG2  B LYS   B 1 102 ? 44.429 -27.871 14.192  0.40 41.20 ?  102 LYS   B HG2  1 
ATOM   5425 H HG3  A LYS   B 1 102 ? 44.212 -28.165 12.631  0.60 42.95 ?  102 LYS   B HG3  1 
ATOM   5426 H HG3  B LYS   B 1 102 ? 44.047 -28.201 12.681  0.40 41.20 ?  102 LYS   B HG3  1 
ATOM   5427 H HD2  A LYS   B 1 102 ? 43.773 -25.909 12.291  0.60 45.63 ?  102 LYS   B HD2  1 
ATOM   5428 H HD2  B LYS   B 1 102 ? 43.581 -25.967 12.285  0.40 43.27 ?  102 LYS   B HD2  1 
ATOM   5429 H HD3  A LYS   B 1 102 ? 44.047 -25.610 13.829  0.60 45.63 ?  102 LYS   B HD3  1 
ATOM   5430 H HD3  B LYS   B 1 102 ? 43.873 -25.617 13.810  0.40 43.27 ?  102 LYS   B HD3  1 
ATOM   5431 H HE2  A LYS   B 1 102 ? 46.288 -26.147 13.547  0.60 47.62 ?  102 LYS   B HE2  1 
ATOM   5432 H HE2  B LYS   B 1 102 ? 46.113 -26.139 13.516  0.40 44.80 ?  102 LYS   B HE2  1 
ATOM   5433 H HE3  A LYS   B 1 102 ? 46.023 -26.494 12.017  0.60 47.62 ?  102 LYS   B HE3  1 
ATOM   5434 H HE3  B LYS   B 1 102 ? 45.832 -26.539 12.002  0.40 44.80 ?  102 LYS   B HE3  1 
ATOM   5435 H HZ1  A LYS   B 1 102 ? 46.895 -24.401 12.219  0.60 48.83 ?  102 LYS   B HZ1  1 
ATOM   5436 H HZ1  B LYS   B 1 102 ? 46.686 -24.435 12.123  0.40 45.67 ?  102 LYS   B HZ1  1 
ATOM   5437 H HZ2  A LYS   B 1 102 ? 45.558 -24.290 11.672  0.60 48.83 ?  102 LYS   B HZ2  1 
ATOM   5438 H HZ2  B LYS   B 1 102 ? 45.342 -24.354 11.590  0.40 45.67 ?  102 LYS   B HZ2  1 
ATOM   5439 H HZ3  A LYS   B 1 102 ? 45.799 -23.974 13.065  0.60 48.83 ?  102 LYS   B HZ3  1 
ATOM   5440 H HZ3  B LYS   B 1 102 ? 45.598 -23.990 12.969  0.40 45.67 ?  102 LYS   B HZ3  1 
ATOM   5441 N N    A GLY   B 1 103 ? 39.801 -30.008 14.376  0.60 29.09 ?  103 GLY   B N    1 
ATOM   5442 N N    B GLY   B 1 103 ? 39.673 -30.067 14.253  0.40 28.80 ?  103 GLY   B N    1 
ATOM   5443 C CA   A GLY   B 1 103 ? 38.475 -30.032 14.958  0.60 28.72 ?  103 GLY   B CA   1 
ATOM   5444 C CA   B GLY   B 1 103 ? 38.333 -30.137 14.804  0.40 28.16 ?  103 GLY   B CA   1 
ATOM   5445 C C    A GLY   B 1 103 ? 37.532 -28.962 14.455  0.60 27.81 ?  103 GLY   B C    1 
ATOM   5446 C C    B GLY   B 1 103 ? 37.399 -29.029 14.376  0.40 27.16 ?  103 GLY   B C    1 
ATOM   5447 O O    A GLY   B 1 103 ? 36.416 -28.848 14.975  0.60 28.57 ?  103 GLY   B O    1 
ATOM   5448 O O    B GLY   B 1 103 ? 36.344 -28.852 14.994  0.40 27.70 ?  103 GLY   B O    1 
ATOM   5449 H H    A GLY   B 1 103 ? 39.912 -30.571 13.739  0.60 34.89 ?  103 GLY   B H    1 
ATOM   5450 H H    B GLY   B 1 103 ? 39.799 -30.575 13.572  0.40 34.53 ?  103 GLY   B H    1 
ATOM   5451 H HA2  A GLY   B 1 103 ? 38.073 -30.896 14.776  0.60 34.45 ?  103 GLY   B HA2  1 
ATOM   5452 H HA2  B GLY   B 1 103 ? 37.932 -30.980 14.541  0.40 33.76 ?  103 GLY   B HA2  1 
ATOM   5453 H HA3  A GLY   B 1 103 ? 38.554 -29.938 15.922  0.60 34.45 ?  103 GLY   B HA3  1 
ATOM   5454 H HA3  B GLY   B 1 103 ? 38.392 -30.125 15.773  0.40 33.76 ?  103 GLY   B HA3  1 
ATOM   5455 N N    A GLU   B 1 104 ? 37.935 -28.177 13.460  0.60 26.04 ?  104 GLU   B N    1 
ATOM   5456 N N    B GLU   B 1 104 ? 37.742 -28.280 13.333  0.40 25.47 ?  104 GLU   B N    1 
ATOM   5457 C CA   A GLU   B 1 104 ? 37.091 -27.094 12.982  0.60 24.50 ?  104 GLU   B CA   1 
ATOM   5458 C CA   B GLU   B 1 104 ? 36.912 -27.166 12.900  0.40 23.92 ?  104 GLU   B CA   1 
ATOM   5459 C C    A GLU   B 1 104 ? 35.920 -27.643 12.167  0.60 24.91 ?  104 GLU   B C    1 
ATOM   5460 C C    B GLU   B 1 104 ? 35.755 -27.662 12.040  0.40 23.86 ?  104 GLU   B C    1 
ATOM   5461 O O    A GLU   B 1 104 ? 35.970 -28.744 11.611  0.60 25.68 ?  104 GLU   B O    1 
ATOM   5462 O O    B GLU   B 1 104 ? 35.842 -28.699 11.375  0.40 24.30 ?  104 GLU   B O    1 
ATOM   5463 C CB   A GLU   B 1 104 ? 37.927 -26.094 12.183  0.60 22.95 ?  104 GLU   B CB   1 
ATOM   5464 C CB   B GLU   B 1 104 ? 37.761 -26.144 12.144  0.40 22.59 ?  104 GLU   B CB   1 
ATOM   5465 C CG   A GLU   B 1 104 ? 39.038 -25.484 13.029  0.60 21.67 ?  104 GLU   B CG   1 
ATOM   5466 C CG   B GLU   B 1 104 ? 38.871 -25.573 13.014  0.40 21.49 ?  104 GLU   B CG   1 
ATOM   5467 C CD   A GLU   B 1 104 ? 39.989 -24.592 12.256  0.60 20.49 ?  104 GLU   B CD   1 
ATOM   5468 C CD   B GLU   B 1 104 ? 39.834 -24.669 12.270  0.40 20.56 ?  104 GLU   B CD   1 
ATOM   5469 O OE1  A GLU   B 1 104 ? 39.995 -24.624 11.007  0.60 18.81 ?  104 GLU   B OE1  1 
ATOM   5470 O OE1  B GLU   B 1 104 ? 39.822 -24.643 11.021  0.40 19.89 ?  104 GLU   B OE1  1 
ATOM   5471 O OE2  A GLU   B 1 104 ? 40.744 -23.851 12.920  0.60 21.78 -1 104 GLU   B OE2  1 
ATOM   5472 O OE2  B GLU   B 1 104 ? 40.614 -23.979 12.957  0.40 20.62 -1 104 GLU   B OE2  1 
ATOM   5473 H H    A GLU   B 1 104 ? 38.690 -28.248 13.057  0.60 31.22 ?  104 GLU   B H    1 
ATOM   5474 H H    B GLU   B 1 104 ? 38.451 -28.395 12.862  0.40 30.55 ?  104 GLU   B H    1 
ATOM   5475 H HA   A GLU   B 1 104 ? 36.726 -26.626 13.749  0.60 29.37 ?  104 GLU   B HA   1 
ATOM   5476 H HA   B GLU   B 1 104 ? 36.540 -26.727 13.681  0.40 28.68 ?  104 GLU   B HA   1 
ATOM   5477 H HB2  A GLU   B 1 104 ? 38.334 -26.548 11.429  0.60 27.51 ?  104 GLU   B HB2  1 
ATOM   5478 H HB2  B GLU   B 1 104 ? 38.166 -26.573 11.375  0.40 27.09 ?  104 GLU   B HB2  1 
ATOM   5479 H HB3  A GLU   B 1 104 ? 37.353 -25.377 11.874  0.60 27.51 ?  104 GLU   B HB3  1 
ATOM   5480 H HB3  B GLU   B 1 104 ? 37.193 -25.411 11.857  0.40 27.09 ?  104 GLU   B HB3  1 
ATOM   5481 H HG2  A GLU   B 1 104 ? 38.639 -24.945 13.730  0.60 25.99 ?  104 GLU   B HG2  1 
ATOM   5482 H HG2  B GLU   B 1 104 ? 38.472 -25.050 13.727  0.40 25.77 ?  104 GLU   B HG2  1 
ATOM   5483 H HG3  A GLU   B 1 104 ? 39.564 -26.197 13.423  0.60 25.99 ?  104 GLU   B HG3  1 
ATOM   5484 H HG3  B GLU   B 1 104 ? 39.382 -26.305 13.393  0.40 25.77 ?  104 GLU   B HG3  1 
ATOM   5485 N N    A ASP   B 1 105 ? 34.849 -26.853 12.115  0.60 25.12 ?  105 ASP   B N    1 
ATOM   5486 N N    B ASP   B 1 105 ? 34.660 -26.905 12.063  0.40 23.72 ?  105 ASP   B N    1 
ATOM   5487 C CA   A ASP   B 1 105 ? 33.570 -27.313 11.590  0.60 26.02 ?  105 ASP   B CA   1 
ATOM   5488 C CA   B ASP   B 1 105 ? 33.402 -27.370 11.491  0.40 24.09 ?  105 ASP   B CA   1 
ATOM   5489 C C    A ASP   B 1 105 ? 33.608 -27.351 10.066  0.60 24.52 ?  105 ASP   B C    1 
ATOM   5490 C C    B ASP   B 1 105 ? 33.484 -27.385 9.969   0.40 23.18 ?  105 ASP   B C    1 
ATOM   5491 O O    A ASP   B 1 105 ? 33.760 -26.312 9.414   0.60 23.88 ?  105 ASP   B O    1 
ATOM   5492 O O    B ASP   B 1 105 ? 33.660 -26.339 9.335   0.40 22.36 ?  105 ASP   B O    1 
ATOM   5493 C CB   A ASP   B 1 105 ? 32.457 -26.388 12.076  0.60 28.69 ?  105 ASP   B CB   1 
ATOM   5494 C CB   B ASP   B 1 105 ? 32.259 -26.472 11.959  0.40 25.35 ?  105 ASP   B CB   1 
ATOM   5495 C CG   A ASP   B 1 105 ? 31.084 -26.833 11.616  0.60 30.94 ?  105 ASP   B CG   1 
ATOM   5496 C CG   B ASP   B 1 105 ? 30.893 -27.057 11.643  0.40 26.28 ?  105 ASP   B CG   1 
ATOM   5497 O OD1  A ASP   B 1 105 ? 30.968 -27.954 11.075  0.60 31.35 ?  105 ASP   B OD1  1 
ATOM   5498 O OD1  B ASP   B 1 105 ? 30.823 -28.006 10.834  0.40 26.39 ?  105 ASP   B OD1  1 
ATOM   5499 O OD2  A ASP   B 1 105 ? 30.121 -26.055 11.789  0.60 32.38 -1 105 ASP   B OD2  1 
ATOM   5500 O OD2  B ASP   B 1 105 ? 29.891 -26.579 12.217  0.40 26.35 -1 105 ASP   B OD2  1 
ATOM   5501 H H    A ASP   B 1 105 ? 34.842 -26.036 12.379  0.60 30.12 ?  105 ASP   B H    1 
ATOM   5502 H H    B ASP   B 1 105 ? 34.621 -26.117 12.402  0.40 28.44 ?  105 ASP   B H    1 
ATOM   5503 H HA   A ASP   B 1 105 ? 33.387 -28.209 11.917  0.60 31.21 ?  105 ASP   B HA   1 
ATOM   5504 H HA   B ASP   B 1 105 ? 33.221 -28.273 11.795  0.40 28.89 ?  105 ASP   B HA   1 
ATOM   5505 H HB2  A ASP   B 1 105 ? 32.478 -26.353 13.049  0.60 34.41 ?  105 ASP   B HB2  1 
ATOM   5506 H HB2  B ASP   B 1 105 ? 32.321 -26.355 12.921  0.40 30.40 ?  105 ASP   B HB2  1 
ATOM   5507 H HB3  A ASP   B 1 105 ? 32.600 -25.502 11.713  0.60 34.41 ?  105 ASP   B HB3  1 
ATOM   5508 H HB3  B ASP   B 1 105 ? 32.334 -25.609 11.518  0.40 30.40 ?  105 ASP   B HB3  1 
ATOM   5509 N N    A ILE   B 1 106 ? 33.452 -28.553 9.503   0.60 23.86 ?  106 ILE   B N    1 
ATOM   5510 N N    B ILE   B 1 106 ? 33.346 -28.579 9.386   0.40 23.01 ?  106 ILE   B N    1 
ATOM   5511 C CA   A ILE   B 1 106 ? 33.448 -28.725 8.054   0.60 22.76 ?  106 ILE   B CA   1 
ATOM   5512 C CA   B ILE   B 1 106 ? 33.360 -28.729 7.936   0.40 22.68 ?  106 ILE   B CA   1 
ATOM   5513 C C    A ILE   B 1 106 ? 32.349 -27.902 7.385   0.60 21.55 ?  106 ILE   B C    1 
ATOM   5514 C C    B ILE   B 1 106 ? 32.265 -27.902 7.276   0.40 22.06 ?  106 ILE   B C    1 
ATOM   5515 O O    A ILE   B 1 106 ? 32.456 -27.573 6.200   0.60 20.63 ?  106 ILE   B O    1 
ATOM   5516 O O    B ILE   B 1 106 ? 32.361 -27.584 6.085   0.40 21.34 ?  106 ILE   B O    1 
ATOM   5517 C CB   A ILE   B 1 106 ? 33.352 -30.233 7.715   0.60 23.66 ?  106 ILE   B CB   1 
ATOM   5518 C CB   B ILE   B 1 106 ? 33.260 -30.229 7.570   0.40 23.22 ?  106 ILE   B CB   1 
ATOM   5519 C CG1  A ILE   B 1 106 ? 33.601 -30.477 6.226   0.60 24.14 ?  106 ILE   B CG1  1 
ATOM   5520 C CG1  B ILE   B 1 106 ? 33.558 -30.452 6.086   0.40 23.52 ?  106 ILE   B CG1  1 
ATOM   5521 C CG2  A ILE   B 1 106 ? 32.001 -30.797 8.133   0.60 24.40 ?  106 ILE   B CG2  1 
ATOM   5522 C CG2  B ILE   B 1 106 ? 31.885 -30.780 7.926   0.40 23.75 ?  106 ILE   B CG2  1 
ATOM   5523 C CD1  A ILE   B 1 106 ? 34.949 -29.985 5.753   0.60 24.30 ?  106 ILE   B CD1  1 
ATOM   5524 C CD1  B ILE   B 1 106 ? 34.930 -29.976 5.669   0.40 23.71 ?  106 ILE   B CD1  1 
ATOM   5525 H H    A ILE   B 1 106 ? 33.359 -29.284 9.946   0.60 28.61 ?  106 ILE   B H    1 
ATOM   5526 H H    B ILE   B 1 106 ? 33.253 -29.316 9.813   0.40 27.59 ?  106 ILE   B H    1 
ATOM   5527 H HA   A ILE   B 1 106 ? 34.295 -28.406 7.716   0.60 27.29 ?  106 ILE   B HA   1 
ATOM   5528 H HA   B ILE   B 1 106 ? 34.206 -28.398 7.608   0.40 27.19 ?  106 ILE   B HA   1 
ATOM   5529 H HB   A ILE   B 1 106 ? 34.039 -30.703 8.216   0.60 28.37 ?  106 ILE   B HB   1 
ATOM   5530 H HB   B ILE   B 1 106 ? 33.922 -30.713 8.088   0.40 27.84 ?  106 ILE   B HB   1 
ATOM   5531 H HG12 A ILE   B 1 106 ? 33.560 -31.434 6.054   0.60 28.94 ?  106 ILE   B HG12 1 
ATOM   5532 H HG12 B ILE   B 1 106 ? 33.506 -31.404 5.896   0.40 28.20 ?  106 ILE   B HG12 1 
ATOM   5533 H HG13 A ILE   B 1 106 ? 32.919 -30.022 5.712   0.60 28.94 ?  106 ILE   B HG13 1 
ATOM   5534 H HG13 B ILE   B 1 106 ? 32.903 -29.975 5.556   0.40 28.20 ?  106 ILE   B HG13 1 
ATOM   5535 H HG21 A ILE   B 1 106 ? 32.017 -31.762 8.030   0.60 29.26 ?  106 ILE   B HG21 1 
ATOM   5536 H HG21 B ILE   B 1 106 ? 31.904 -31.747 7.849   0.40 28.48 ?  106 ILE   B HG21 1 
ATOM   5537 H HG22 A ILE   B 1 106 ? 31.837 -30.567 9.061   0.60 29.26 ?  106 ILE   B HG22 1 
ATOM   5538 H HG22 B ILE   B 1 106 ? 31.671 -30.525 8.837   0.40 28.48 ?  106 ILE   B HG22 1 
ATOM   5539 H HG23 A ILE   B 1 106 ? 31.311 -30.417 7.569   0.60 29.26 ?  106 ILE   B HG23 1 
ATOM   5540 H HG23 B ILE   B 1 106 ? 31.228 -30.412 7.316   0.40 28.48 ?  106 ILE   B HG23 1 
ATOM   5541 H HD11 A ILE   B 1 106 ? 35.152 -30.395 4.899   0.60 29.13 ?  106 ILE   B HD11 1 
ATOM   5542 H HD11 B ILE   B 1 106 ? 35.160 -30.383 4.821   0.40 28.43 ?  106 ILE   B HD11 1 
ATOM   5543 H HD12 A ILE   B 1 106 ? 34.917 -29.020 5.657   0.60 29.13 ?  106 ILE   B HD12 1 
ATOM   5544 H HD12 B ILE   B 1 106 ? 34.917 -29.010 5.581   0.40 28.43 ?  106 ILE   B HD12 1 
ATOM   5545 H HD13 A ILE   B 1 106 ? 35.623 -30.233 6.406   0.60 29.13 ?  106 ILE   B HD13 1 
ATOM   5546 H HD13 B ILE   B 1 106 ? 35.574 -30.239 6.347   0.40 28.43 ?  106 ILE   B HD13 1 
ATOM   5547 N N    A GLN   B 1 107 ? 31.292 -27.552 8.118   0.60 22.25 ?  107 GLN   B N    1 
ATOM   5548 N N    B GLN   B 1 107 ? 31.223 -27.535 8.024   0.40 22.60 ?  107 GLN   B N    1 
ATOM   5549 C CA   A GLN   B 1 107 ? 30.213 -26.756 7.540   0.60 22.96 ?  107 GLN   B CA   1 
ATOM   5550 C CA   B GLN   B 1 107 ? 30.161 -26.706 7.468   0.40 23.21 ?  107 GLN   B CA   1 
ATOM   5551 C C    A GLN   B 1 107 ? 30.695 -25.406 7.012   0.60 21.15 ?  107 GLN   B C    1 
ATOM   5552 C C    B GLN   B 1 107 ? 30.672 -25.346 7.008   0.40 21.28 ?  107 GLN   B C    1 
ATOM   5553 O O    A GLN   B 1 107 ? 30.054 -24.840 6.121   0.60 21.81 ?  107 GLN   B O    1 
ATOM   5554 O O    B GLN   B 1 107 ? 30.031 -24.712 6.164   0.40 21.88 ?  107 GLN   B O    1 
ATOM   5555 C CB   A GLN   B 1 107 ? 29.106 -26.558 8.580   0.60 26.53 ?  107 GLN   B CB   1 
ATOM   5556 C CB   B GLN   B 1 107 ? 29.044 -26.533 8.500   0.40 26.15 ?  107 GLN   B CB   1 
ATOM   5557 C CG   A GLN   B 1 107 ? 27.788 -26.038 8.022   0.60 30.40 ?  107 GLN   B CG   1 
ATOM   5558 C CG   B GLN   B 1 107 ? 27.715 -26.062 7.926   0.40 29.12 ?  107 GLN   B CG   1 
ATOM   5559 C CD   A GLN   B 1 107 ? 27.743 -24.523 7.918   0.60 33.19 ?  107 GLN   B CD   1 
ATOM   5560 C CD   B GLN   B 1 107 ? 27.603 -24.550 7.851   0.40 31.39 ?  107 GLN   B CD   1 
ATOM   5561 O OE1  A GLN   B 1 107 ? 28.578 -23.821 8.493   0.60 34.27 ?  107 GLN   B OE1  1 
ATOM   5562 O OE1  B GLN   B 1 107 ? 28.422 -23.824 8.417   0.40 32.27 ?  107 GLN   B OE1  1 
ATOM   5563 N NE2  A GLN   B 1 107 ? 26.760 -24.009 7.181   0.60 34.28 ?  107 GLN   B NE2  1 
ATOM   5564 N NE2  B GLN   B 1 107 ? 26.581 -24.068 7.153   0.40 32.18 ?  107 GLN   B NE2  1 
ATOM   5565 H H    A GLN   B 1 107 ? 31.177 -27.769 8.938   0.60 26.68 ?  107 GLN   B H    1 
ATOM   5566 H H    B GLN   B 1 107 ? 31.106 -27.756 8.845   0.40 27.10 ?  107 GLN   B H    1 
ATOM   5567 H HA   A GLN   B 1 107 ? 29.831 -27.249 6.794   0.60 27.52 ?  107 GLN   B HA   1 
ATOM   5568 H HA   B GLN   B 1 107 ? 29.782 -27.159 6.698   0.40 27.82 ?  107 GLN   B HA   1 
ATOM   5569 H HB2  A GLN   B 1 107 ? 28.926 -27.410 9.005   0.60 31.82 ?  107 GLN   B HB2  1 
ATOM   5570 H HB2  B GLN   B 1 107 ? 28.888 -27.385 8.931   0.40 31.35 ?  107 GLN   B HB2  1 
ATOM   5571 H HB3  A GLN   B 1 107 ? 29.418 -25.924 9.244   0.60 31.82 ?  107 GLN   B HB3  1 
ATOM   5572 H HB3  B GLN   B 1 107 ? 29.328 -25.881 9.160   0.40 31.35 ?  107 GLN   B HB3  1 
ATOM   5573 H HG2  A GLN   B 1 107 ? 27.653 -26.400 7.134   0.60 36.46 ?  107 GLN   B HG2  1 
ATOM   5574 H HG2  B GLN   B 1 107 ? 27.615 -26.413 7.028   0.40 34.92 ?  107 GLN   B HG2  1 
ATOM   5575 H HG3  A GLN   B 1 107 ? 27.065 -26.324 8.607   0.60 36.46 ?  107 GLN   B HG3  1 
ATOM   5576 H HG3  B GLN   B 1 107 ? 26.995 -26.392 8.490   0.40 34.92 ?  107 GLN   B HG3  1 
ATOM   5577 H HE21 A GLN   B 1 107 ? 26.195 -24.530 6.791   0.60 41.11 ?  107 GLN   B HE21 1 
ATOM   5578 H HE21 B GLN   B 1 107 ? 26.029 -24.605 6.769   0.40 38.60 ?  107 GLN   B HE21 1 
ATOM   5579 H HE22 A GLN   B 1 107 ? 26.686 -23.156 7.094   0.60 41.11 ?  107 GLN   B HE22 1 
ATOM   5580 H HE22 B GLN   B 1 107 ? 26.471 -23.218 7.084   0.40 38.60 ?  107 GLN   B HE22 1 
ATOM   5581 N N    . LEU   B 1 108 ? 31.813 -24.885 7.528   1.00 18.95 ?  108 LEU   B N    1 
ATOM   5582 C CA   . LEU   B 1 108 ? 32.363 -23.591 7.120   1.00 16.99 ?  108 LEU   B CA   1 
ATOM   5583 C C    . LEU   B 1 108 ? 33.012 -23.615 5.745   1.00 15.03 ?  108 LEU   B C    1 
ATOM   5584 O O    . LEU   B 1 108 ? 33.444 -22.558 5.258   1.00 14.95 ?  108 LEU   B O    1 
ATOM   5585 C CB   . LEU   B 1 108 ? 33.371 -23.106 8.159   1.00 17.95 ?  108 LEU   B CB   1 
ATOM   5586 C CG   . LEU   B 1 108 ? 32.744 -22.669 9.481   1.00 19.10 ?  108 LEU   B CG   1 
ATOM   5587 C CD1  . LEU   B 1 108 ? 33.784 -22.557 10.584  1.00 19.52 ?  108 LEU   B CD1  1 
ATOM   5588 C CD2  . LEU   B 1 108 ? 32.031 -21.340 9.295   1.00 20.53 ?  108 LEU   B CD2  1 
ATOM   5589 H H    A LEU   B 1 108 ? 32.277 -25.275 8.136   0.60 22.72 ?  108 LEU   B H    1 
ATOM   5590 H H    B LEU   B 1 108 ? 32.276 -25.299 8.120   0.40 22.72 ?  108 LEU   B H    1 
ATOM   5591 H HA   . LEU   B 1 108 ? 31.638 -22.952 7.084   1.00 20.37 ?  108 LEU   B HA   1 
ATOM   5592 H HB2  . LEU   B 1 108 ? 33.987 -23.827 8.352   1.00 21.52 ?  108 LEU   B HB2  1 
ATOM   5593 H HB3  . LEU   B 1 108 ? 33.848 -22.349 7.794   1.00 21.52 ?  108 LEU   B HB3  1 
ATOM   5594 H HG   . LEU   B 1 108 ? 32.082 -23.325 9.757   1.00 22.90 ?  108 LEU   B HG   1 
ATOM   5595 H HD11 . LEU   B 1 108 ? 33.345 -22.294 11.410  1.00 23.40 ?  108 LEU   B HD11 1 
ATOM   5596 H HD12 . LEU   B 1 108 ? 34.215 -23.417 10.700  1.00 23.40 ?  108 LEU   B HD12 1 
ATOM   5597 H HD13 . LEU   B 1 108 ? 34.440 -21.888 10.333  1.00 23.40 ?  108 LEU   B HD13 1 
ATOM   5598 H HD21 . LEU   B 1 108 ? 31.740 -21.013 10.160  1.00 24.62 ?  108 LEU   B HD21 1 
ATOM   5599 H HD22 . LEU   B 1 108 ? 32.645 -20.708 8.891   1.00 24.62 ?  108 LEU   B HD22 1 
ATOM   5600 H HD23 . LEU   B 1 108 ? 31.263 -21.470 8.716   1.00 24.62 ?  108 LEU   B HD23 1 
ATOM   5601 N N    . LEU   B 1 109 ? 33.085 -24.784 5.112   1.00 14.25 ?  109 LEU   B N    1 
ATOM   5602 C CA   . LEU   B 1 109 ? 33.714 -24.884 3.804   1.00 13.58 ?  109 LEU   B CA   1 
ATOM   5603 C C    . LEU   B 1 109 ? 32.947 -24.100 2.746   1.00 12.74 ?  109 LEU   B C    1 
ATOM   5604 O O    . LEU   B 1 109 ? 33.559 -23.507 1.851   1.00 12.66 ?  109 LEU   B O    1 
ATOM   5605 C CB   . LEU   B 1 109 ? 33.843 -26.358 3.417   1.00 13.61 ?  109 LEU   B CB   1 
ATOM   5606 C CG   . LEU   B 1 109 ? 34.622 -26.688 2.148   1.00 13.47 ?  109 LEU   B CG   1 
ATOM   5607 C CD1  . LEU   B 1 109 ? 36.008 -26.042 2.168   1.00 13.92 ?  109 LEU   B CD1  1 
ATOM   5608 C CD2  . LEU   B 1 109 ? 34.745 -28.198 1.997   1.00 14.25 ?  109 LEU   B CD2  1 
ATOM   5609 H H    . LEU   B 1 109 ? 32.781 -25.529 5.409   1.00 17.08 ?  109 LEU   B H    1 
ATOM   5610 H HA   . LEU   B 1 109 ? 34.607 -24.511 3.852   1.00 16.28 ?  109 LEU   B HA   1 
ATOM   5611 H HB2  . LEU   B 1 109 ? 34.287 -26.820 4.144   1.00 16.30 ?  109 LEU   B HB2  1 
ATOM   5612 H HB3  . LEU   B 1 109 ? 32.953 -26.722 3.303   1.00 16.30 ?  109 LEU   B HB3  1 
ATOM   5613 H HG   . LEU   B 1 109 ? 34.138 -26.348 1.376   1.00 16.14 ?  109 LEU   B HG   1 
ATOM   5614 H HD11 . LEU   B 1 109 ? 36.533 -26.394 1.429   1.00 16.69 ?  109 LEU   B HD11 1 
ATOM   5615 H HD12 . LEU   B 1 109 ? 35.913 -25.082 2.075   1.00 16.69 ?  109 LEU   B HD12 1 
ATOM   5616 H HD13 . LEU   B 1 109 ? 36.443 -26.255 3.009   1.00 16.69 ?  109 LEU   B HD13 1 
ATOM   5617 H HD21 . LEU   B 1 109 ? 35.331 -28.395 1.248   1.00 17.08 ?  109 LEU   B HD21 1 
ATOM   5618 H HD22 . LEU   B 1 109 ? 35.117 -28.568 2.812   1.00 17.08 ?  109 LEU   B HD22 1 
ATOM   5619 H HD23 . LEU   B 1 109 ? 33.865 -28.575 1.834   1.00 17.08 ?  109 LEU   B HD23 1 
ATOM   5620 N N    . LYS   B 1 110 ? 31.613 -24.071 2.825   1.00 12.57 ?  110 LYS   B N    1 
ATOM   5621 C CA   . LYS   B 1 110 ? 30.863 -23.303 1.839   1.00 12.83 ?  110 LYS   B CA   1 
ATOM   5622 C C    . LYS   B 1 110 ? 31.212 -21.816 1.932   1.00 12.48 ?  110 LYS   B C    1 
ATOM   5623 O O    . LYS   B 1 110 ? 31.475 -21.165 0.917   1.00 12.14 ?  110 LYS   B O    1 
ATOM   5624 C CB   . LYS   B 1 110 ? 29.359 -23.547 1.987   1.00 13.66 ?  110 LYS   B CB   1 
ATOM   5625 C CG   . LYS   B 1 110 ? 28.570 -22.911 0.854   1.00 14.06 ?  110 LYS   B CG   1 
ATOM   5626 C CD   . LYS   B 1 110 ? 27.111 -23.350 0.855   1.00 14.27 ?  110 LYS   B CD   1 
ATOM   5627 C CE   . LYS   B 1 110 ? 26.344 -22.808 -0.354  1.00 14.85 ?  110 LYS   B CE   1 
ATOM   5628 N NZ   . LYS   B 1 110 ? 26.674 -23.525 -1.617  1.00 14.82 ?  110 LYS   B NZ   1 
ATOM   5629 H H    . LYS   B 1 110 ? 31.140 -24.482 3.409   1.00 15.06 ?  110 LYS   B H    1 
ATOM   5630 H HA   . LYS   B 1 110 ? 31.118 -23.605 0.950   1.00 15.37 ?  110 LYS   B HA   1 
ATOM   5631 H HB2  . LYS   B 1 110 ? 29.188 -24.505 1.971   1.00 16.37 ?  110 LYS   B HB2  1 
ATOM   5632 H HB3  . LYS   B 1 110 ? 29.053 -23.167 2.822   1.00 16.37 ?  110 LYS   B HB3  1 
ATOM   5633 H HG2  . LYS   B 1 110 ? 28.586 -21.946 0.953   1.00 16.85 ?  110 LYS   B HG2  1 
ATOM   5634 H HG3  . LYS   B 1 110 ? 28.956 -23.166 0.003   1.00 16.85 ?  110 LYS   B HG3  1 
ATOM   5635 H HD2  . LYS   B 1 110 ? 27.071 -24.323 0.826   1.00 17.10 ?  110 LYS   B HD2  1 
ATOM   5636 H HD3  . LYS   B 1 110 ? 26.677 -23.026 1.660   1.00 17.10 ?  110 LYS   B HD3  1 
ATOM   5637 H HE2  . LYS   B 1 110 ? 25.393 -22.901 -0.197  1.00 17.80 ?  110 LYS   B HE2  1 
ATOM   5638 H HE3  . LYS   B 1 110 ? 26.571 -21.871 -0.475  1.00 17.80 ?  110 LYS   B HE3  1 
ATOM   5639 H HZ1  . LYS   B 1 110 ? 26.212 -23.178 -2.294  1.00 17.76 ?  110 LYS   B HZ1  1 
ATOM   5640 H HZ2  . LYS   B 1 110 ? 27.544 -23.449 -1.792  1.00 17.76 ?  110 LYS   B HZ2  1 
ATOM   5641 H HZ3  . LYS   B 1 110 ? 26.470 -24.388 -1.538  1.00 17.76 ?  110 LYS   B HZ3  1 
ATOM   5642 N N    . SER   B 1 111 ? 31.223 -21.263 3.150   1.00 12.86 ?  111 SER   B N    1 
ATOM   5643 C CA   . SER   B 1 111 ? 31.614 -19.865 3.331   1.00 12.79 ?  111 SER   B CA   1 
ATOM   5644 C C    . SER   B 1 111 ? 32.997 -19.604 2.752   1.00 12.10 ?  111 SER   B C    1 
ATOM   5645 O O    . SER   B 1 111 ? 33.223 -18.570 2.110   1.00 12.26 ?  111 SER   B O    1 
ATOM   5646 C CB   . SER   B 1 111 ? 31.594 -19.510 4.813   1.00 13.97 ?  111 SER   B CB   1 
ATOM   5647 O OG   . SER   B 1 111 ? 30.283 -19.537 5.331   1.00 15.84 ?  111 SER   B OG   1 
ATOM   5648 H H    . SER   B 1 111 ? 31.013 -21.673 3.875   1.00 15.41 ?  111 SER   B H    1 
ATOM   5649 H HA   . SER   B 1 111 ? 30.981 -19.294 2.870   1.00 15.33 ?  111 SER   B HA   1 
ATOM   5650 H HB2  . SER   B 1 111 ? 32.129 -20.158 5.297   1.00 16.73 ?  111 SER   B HB2  1 
ATOM   5651 H HB3  . SER   B 1 111 ? 31.959 -18.623 4.928   1.00 16.73 ?  111 SER   B HB3  1 
ATOM   5652 H HG   . SER   B 1 111 ? 30.291 -19.335 6.151   1.00 18.98 ?  111 SER   B HG   1 
ATOM   5653 N N    . ALA   B 1 112 ? 33.935 -20.525 2.978   1.00 12.06 ?  112 ALA   B N    1 
ATOM   5654 C CA   . ALA   B 1 112 ? 35.282 -20.358 2.440   1.00 11.94 ?  112 ALA   B CA   1 
ATOM   5655 C C    . ALA   B 1 112 ? 35.254 -20.256 0.919   1.00 11.32 ?  112 ALA   B C    1 
ATOM   5656 O O    . ALA   B 1 112 ? 35.887 -19.370 0.330   1.00 11.85 ?  112 ALA   B O    1 
ATOM   5657 C CB   . ALA   B 1 112 ? 36.183 -21.502 2.912   1.00 12.63 ?  112 ALA   B CB   1 
ATOM   5658 H H    . ALA   B 1 112 ? 33.823 -21.245 3.440   1.00 14.45 ?  112 ALA   B H    1 
ATOM   5659 H HA   . ALA   B 1 112 ? 35.655 -19.531 2.786   1.00 14.30 ?  112 ALA   B HA   1 
ATOM   5660 H HB1  . ALA   B 1 112 ? 37.077 -21.370 2.554   1.00 15.13 ?  112 ALA   B HB1  1 
ATOM   5661 H HB2  . ALA   B 1 112 ? 36.220 -21.495 3.886   1.00 15.13 ?  112 ALA   B HB2  1 
ATOM   5662 H HB3  . ALA   B 1 112 ? 35.822 -22.343 2.603   1.00 15.13 ?  112 ALA   B HB3  1 
ATOM   5663 N N    . TYR   B 1 113 ? 34.518 -21.155 0.260   1.00 11.47 ?  113 TYR   B N    1 
ATOM   5664 C CA   . TYR   B 1 113 ? 34.446 -21.106 -1.194  1.00 11.16 ?  113 TYR   B CA   1 
ATOM   5665 C C    . TYR   B 1 113 ? 33.749 -19.851 -1.709  1.00 11.18 ?  113 TYR   B C    1 
ATOM   5666 O O    . TYR   B 1 113 ? 34.016 -19.427 -2.838  1.00 11.28 ?  113 TYR   B O    1 
ATOM   5667 C CB   . TYR   B 1 113 ? 33.767 -22.359 -1.750  1.00 11.47 ?  113 TYR   B CB   1 
ATOM   5668 C CG   . TYR   B 1 113 ? 34.732 -23.512 -2.022  1.00 11.76 ?  113 TYR   B CG   1 
ATOM   5669 C CD1  . TYR   B 1 113 ? 35.727 -23.404 -2.990  1.00 12.28 ?  113 TYR   B CD1  1 
ATOM   5670 C CD2  . TYR   B 1 113 ? 34.645 -24.696 -1.312  1.00 11.94 ?  113 TYR   B CD2  1 
ATOM   5671 C CE1  . TYR   B 1 113 ? 36.605 -24.436 -3.240  1.00 12.17 ?  113 TYR   B CE1  1 
ATOM   5672 C CE2  . TYR   B 1 113 ? 35.512 -25.747 -1.564  1.00 12.11 ?  113 TYR   B CE2  1 
ATOM   5673 C CZ   . TYR   B 1 113 ? 36.480 -25.610 -2.533  1.00 12.20 ?  113 TYR   B CZ   1 
ATOM   5674 O OH   . TYR   B 1 113 ? 37.365 -26.623 -2.815  1.00 12.88 ?  113 TYR   B OH   1 
ATOM   5675 H H    . TYR   B 1 113 ? 34.058 -21.789 0.633   1.00 13.75 ?  113 TYR   B H    1 
ATOM   5676 H HA   . TYR   B 1 113 ? 35.344 -21.089 -1.531  1.00 13.37 ?  113 TYR   B HA   1 
ATOM   5677 H HB2  . TYR   B 1 113 ? 33.106 -22.676 -1.110  1.00 13.74 ?  113 TYR   B HB2  1 
ATOM   5678 H HB3  . TYR   B 1 113 ? 33.329 -22.133 -2.585  1.00 13.74 ?  113 TYR   B HB3  1 
ATOM   5679 H HD1  . TYR   B 1 113 ? 35.803 -22.608 -3.478  1.00 14.71 ?  113 TYR   B HD1  1 
ATOM   5680 H HD2  . TYR   B 1 113 ? 33.981 -24.793 -0.670  1.00 14.31 ?  113 TYR   B HD2  1 
ATOM   5681 H HE1  . TYR   B 1 113 ? 37.256 -24.347 -3.903  1.00 14.58 ?  113 TYR   B HE1  1 
ATOM   5682 H HE2  . TYR   B 1 113 ? 35.435 -26.541 -1.093  1.00 14.51 ?  113 TYR   B HE2  1 
ATOM   5683 H HH   . TYR   B 1 113 ? 37.189 -27.293 -2.339  1.00 15.43 ?  113 TYR   B HH   1 
ATOM   5684 N N    . GLU   B 1 114 ? 32.820 -19.277 -0.936  1.00 11.11 ?  114 GLU   B N    1 
ATOM   5685 C CA   . GLU   B 1 114 ? 32.136 -18.070 -1.395  1.00 11.14 ?  114 GLU   B CA   1 
ATOM   5686 C C    . GLU   B 1 114 ? 33.120 -16.946 -1.685  1.00 10.91 ?  114 GLU   B C    1 
ATOM   5687 O O    . GLU   B 1 114 ? 32.849 -16.086 -2.526  1.00 11.62 ?  114 GLU   B O    1 
ATOM   5688 C CB   . GLU   B 1 114 ? 31.072 -17.643 -0.381  1.00 11.65 ?  114 GLU   B CB   1 
ATOM   5689 C CG   . GLU   B 1 114 ? 29.860 -18.562 -0.443  1.00 11.88 ?  114 GLU   B CG   1 
ATOM   5690 C CD   . GLU   B 1 114 ? 28.845 -18.371 0.663   1.00 11.86 ?  114 GLU   B CD   1 
ATOM   5691 O OE1  . GLU   B 1 114 ? 29.135 -17.759 1.712   1.00 12.10 ?  114 GLU   B OE1  1 
ATOM   5692 O OE2  . GLU   B 1 114 ? 27.720 -18.900 0.494   1.00 12.72 -1 114 GLU   B OE2  1 
ATOM   5693 H H    . GLU   B 1 114 ? 32.560 -19.567 -0.160  1.00 13.31 ?  114 GLU   B H    1 
ATOM   5694 H HA   . GLU   B 1 114 ? 31.679 -18.273 -2.220  1.00 13.35 ?  114 GLU   B HA   1 
ATOM   5695 H HB2  . GLU   B 1 114 ? 31.443 -17.688 0.516   1.00 13.95 ?  114 GLU   B HB2  1 
ATOM   5696 H HB3  . GLU   B 1 114 ? 30.780 -16.742 -0.580  1.00 13.95 ?  114 GLU   B HB3  1 
ATOM   5697 H HG2  . GLU   B 1 114 ? 29.408 -18.416 -1.285  1.00 14.23 ?  114 GLU   B HG2  1 
ATOM   5698 H HG3  . GLU   B 1 114 ? 30.172 -19.482 -0.396  1.00 14.23 ?  114 GLU   B HG3  1 
ATOM   5699 N N    . ASN   B 1 115 ? 34.282 -16.943 -1.027  1.00 10.84 ?  115 ASN   B N    1 
ATOM   5700 C CA   . ASN   B 1 115 ? 35.278 -15.912 -1.320  1.00 10.92 ?  115 ASN   B CA   1 
ATOM   5701 C C    . ASN   B 1 115 ? 35.688 -15.925 -2.785  1.00 10.73 ?  115 ASN   B C    1 
ATOM   5702 O O    . ASN   B 1 115 ? 36.071 -14.882 -3.333  1.00 11.56 ?  115 ASN   B O    1 
ATOM   5703 C CB   . ASN   B 1 115 ? 36.519 -16.093 -0.441  1.00 11.77 ?  115 ASN   B CB   1 
ATOM   5704 C CG   . ASN   B 1 115 ? 36.255 -15.833 1.019   1.00 12.20 ?  115 ASN   B CG   1 
ATOM   5705 O OD1  . ASN   B 1 115 ? 36.257 -14.687 1.464   1.00 14.04 ?  115 ASN   B OD1  1 
ATOM   5706 N ND2  . ASN   B 1 115 ? 36.085 -16.902 1.793   1.00 12.30 ?  115 ASN   B ND2  1 
ATOM   5707 H H    . ASN   B 1 115 ? 34.512 -17.508 -0.416  1.00 12.98 ?  115 ASN   B H    1 
ATOM   5708 H HA   . ASN   B 1 115 ? 34.899 -15.043 -1.125  1.00 13.08 ?  115 ASN   B HA   1 
ATOM   5709 H HB2  . ASN   B 1 115 ? 36.844 -16.999 -0.531  1.00 14.10 ?  115 ASN   B HB2  1 
ATOM   5710 H HB3  . ASN   B 1 115 ? 37.202 -15.465 -0.729  1.00 14.10 ?  115 ASN   B HB3  1 
ATOM   5711 H HD21 . ASN   B 1 115 ? 35.943 -16.806 2.639   1.00 14.74 ?  115 ASN   B HD21 1 
ATOM   5712 H HD22 . ASN   B 1 115 ? 36.105 -17.692 1.452   1.00 14.74 ?  115 ASN   B HD22 1 
ATOM   5713 N N    . PHE   B 1 116 ? 35.665 -17.099 -3.428  1.00 10.78 ?  116 PHE   B N    1 
ATOM   5714 C CA   . PHE   B 1 116 ? 36.098 -17.188 -4.816  1.00 11.12 ?  116 PHE   B CA   1 
ATOM   5715 C C    . PHE   B 1 116 ? 35.197 -16.360 -5.726  1.00 11.09 ?  116 PHE   B C    1 
ATOM   5716 O O    . PHE   B 1 116 ? 35.632 -15.932 -6.798  1.00 11.32 ?  116 PHE   B O    1 
ATOM   5717 C CB   . PHE   B 1 116 ? 36.069 -18.635 -5.343  1.00 10.73 ?  116 PHE   B CB   1 
ATOM   5718 C CG   . PHE   B 1 116 ? 37.138 -19.589 -4.791  1.00 10.55 ?  116 PHE   B CG   1 
ATOM   5719 C CD1  . PHE   B 1 116 ? 37.791 -19.399 -3.585  1.00 11.42 ?  116 PHE   B CD1  1 
ATOM   5720 C CD2  . PHE   B 1 116 ? 37.441 -20.726 -5.527  1.00 11.07 ?  116 PHE   B CD2  1 
ATOM   5721 C CE1  . PHE   B 1 116 ? 38.723 -20.335 -3.132  1.00 11.63 ?  116 PHE   B CE1  1 
ATOM   5722 C CE2  . PHE   B 1 116 ? 38.362 -21.660 -5.083  1.00 11.06 ?  116 PHE   B CE2  1 
ATOM   5723 C CZ   . PHE   B 1 116 ? 39.001 -21.467 -3.888  1.00 11.11 ?  116 PHE   B CZ   1 
ATOM   5724 H H    . PHE   B 1 116 ? 35.402 -17.851 -3.088  1.00 12.91 ?  116 PHE   B H    1 
ATOM   5725 H HA   . PHE   B 1 116 ? 37.002 -16.855 -4.895  1.00 13.32 ?  116 PHE   B HA   1 
ATOM   5726 H HB2  . PHE   B 1 116 ? 35.200 -19.018 -5.131  1.00 12.85 ?  116 PHE   B HB2  1 
ATOM   5727 H HB3  . PHE   B 1 116 ? 36.174 -18.610 -6.308  1.00 12.85 ?  116 PHE   B HB3  1 
ATOM   5728 H HD1  . PHE   B 1 116 ? 37.597 -18.649 -3.068  1.00 13.68 ?  116 PHE   B HD1  1 
ATOM   5729 H HD2  . PHE   B 1 116 ? 36.999 -20.876 -6.332  1.00 13.26 ?  116 PHE   B HD2  1 
ATOM   5730 H HE1  . PHE   B 1 116 ? 39.165 -20.199 -2.323  1.00 13.94 ?  116 PHE   B HE1  1 
ATOM   5731 H HE2  . PHE   B 1 116 ? 38.553 -22.413 -5.594  1.00 13.25 ?  116 PHE   B HE2  1 
ATOM   5732 H HZ   . PHE   B 1 116 ? 39.637 -22.078 -3.590  1.00 13.31 ?  116 PHE   B HZ   1 
ATOM   5733 N N    . ASN   B 1 117 ? 33.928 -16.162 -5.344  1.00 11.23 ?  117 ASN   B N    1 
ATOM   5734 C CA   . ASN   B 1 117 ? 32.983 -15.464 -6.213  1.00 11.13 ?  117 ASN   B CA   1 
ATOM   5735 C C    . ASN   B 1 117 ? 33.298 -13.987 -6.366  1.00 11.87 ?  117 ASN   B C    1 
ATOM   5736 O O    . ASN   B 1 117 ? 32.706 -13.330 -7.226  1.00 12.76 ?  117 ASN   B O    1 
ATOM   5737 C CB   . ASN   B 1 117 ? 31.559 -15.687 -5.716  1.00 11.27 ?  117 ASN   B CB   1 
ATOM   5738 C CG   . ASN   B 1 117 ? 31.104 -17.093 -5.969  1.00 11.49 ?  117 ASN   B CG   1 
ATOM   5739 O OD1  . ASN   B 1 117 ? 31.457 -17.684 -6.996  1.00 12.72 ?  117 ASN   B OD1  1 
ATOM   5740 N ND2  . ASN   B 1 117 ? 30.369 -17.662 -5.029  1.00 11.38 ?  117 ASN   B ND2  1 
ATOM   5741 H H    . ASN   B 1 117 ? 33.601 -16.416 -4.586  1.00 13.45 ?  117 ASN   B H    1 
ATOM   5742 H HA   . ASN   B 1 117 ? 33.039 -15.865 -7.089  1.00 13.33 ?  117 ASN   B HA   1 
ATOM   5743 H HB2  . ASN   B 1 117 ? 31.521 -15.523 -4.755  1.00 13.50 ?  117 ASN   B HB2  1 
ATOM   5744 H HB3  . ASN   B 1 117 ? 30.960 -15.076 -6.176  1.00 13.50 ?  117 ASN   B HB3  1 
ATOM   5745 H HD21 . ASN   B 1 117 ? 30.087 -18.464 -5.128  1.00 13.64 ?  117 ASN   B HD21 1 
ATOM   5746 H HD22 . ASN   B 1 117 ? 30.150 -17.214 -4.322  1.00 13.64 ?  117 ASN   B HD22 1 
ATOM   5747 N N    . GLN   B 1 118 ? 34.229 -13.465 -5.584  1.00 11.66 ?  118 GLN   B N    1 
ATOM   5748 C CA   . GLN   B 1 118 ? 34.657 -12.077 -5.708  1.00 11.98 ?  118 GLN   B CA   1 
ATOM   5749 C C    . GLN   B 1 118 ? 35.725 -11.880 -6.779  1.00 12.23 ?  118 GLN   B C    1 
ATOM   5750 O O    . GLN   B 1 118 ? 36.197 -10.751 -6.952  1.00 13.42 ?  118 GLN   B O    1 
ATOM   5751 C CB   . GLN   B 1 118 ? 35.133 -11.556 -4.348  1.00 12.51 ?  118 GLN   B CB   1 
ATOM   5752 C CG   . GLN   B 1 118 ? 34.047 -11.591 -3.278  1.00 12.56 ?  118 GLN   B CG   1 
ATOM   5753 C CD   . GLN   B 1 118 ? 32.880 -10.670 -3.606  1.00 12.85 ?  118 GLN   B CD   1 
ATOM   5754 O OE1  . GLN   B 1 118 ? 33.069 -9.529  -4.052  1.00 13.37 ?  118 GLN   B OE1  1 
ATOM   5755 N NE2  . GLN   B 1 118 ? 31.664 -11.158 -3.396  1.00 13.27 ?  118 GLN   B NE2  1 
ATOM   5756 H H    . GLN   B 1 118 ? 34.642 -13.896 -4.963  1.00 13.97 ?  118 GLN   B H    1 
ATOM   5757 H HA   . GLN   B 1 118 ? 33.889 -11.545 -5.968  1.00 14.35 ?  118 GLN   B HA   1 
ATOM   5758 H HB2  . GLN   B 1 118 ? 35.872 -12.099 -4.040  1.00 14.99 ?  118 GLN   B HB2  1 
ATOM   5759 H HB3  . GLN   B 1 118 ? 35.419 -10.632 -4.445  1.00 14.99 ?  118 GLN   B HB3  1 
ATOM   5760 H HG2  . GLN   B 1 118 ? 33.707 -12.497 -3.200  1.00 15.05 ?  118 GLN   B HG2  1 
ATOM   5761 H HG3  . GLN   B 1 118 ? 34.428 -11.308 -2.430  1.00 15.05 ?  118 GLN   B HG3  1 
ATOM   5762 H HE21 . GLN   B 1 118 ? 31.570 -11.957 -3.083  1.00 15.90 ?  118 GLN   B HE21 1 
ATOM   5763 H HE22 . GLN   B 1 118 ? 30.979 -10.677 -3.565  1.00 15.90 ?  118 GLN   B HE22 1 
ATOM   5764 N N    . HIS   B 1 119 ? 36.076 -12.937 -7.518  1.00 11.47 ?  119 HIS   B N    1 
ATOM   5765 C CA   . HIS   B 1 119 ? 37.120 -12.887 -8.533  1.00 11.76 ?  119 HIS   B CA   1 
ATOM   5766 C C    . HIS   B 1 119 ? 36.643 -13.621 -9.771  1.00 11.95 ?  119 HIS   B C    1 
ATOM   5767 O O    . HIS   B 1 119 ? 36.126 -14.734 -9.666  1.00 12.50 ?  119 HIS   B O    1 
ATOM   5768 C CB   . HIS   B 1 119 ? 38.406 -13.512 -7.989  1.00 12.43 ?  119 HIS   B CB   1 
ATOM   5769 C CG   . HIS   B 1 119 ? 38.890 -12.815 -6.765  1.00 13.89 ?  119 HIS   B CG   1 
ATOM   5770 N ND1  . HIS   B 1 119 ? 39.698 -11.698 -6.819  1.00 15.42 ?  119 HIS   B ND1  1 
ATOM   5771 C CD2  . HIS   B 1 119 ? 38.597 -13.008 -5.458  1.00 15.12 ?  119 HIS   B CD2  1 
ATOM   5772 C CE1  . HIS   B 1 119 ? 39.906 -11.256 -5.593  1.00 16.42 ?  119 HIS   B CE1  1 
ATOM   5773 N NE2  . HIS   B 1 119 ? 39.243 -12.026 -4.751  1.00 16.61 ?  119 HIS   B NE2  1 
ATOM   5774 H H    . HIS   B 1 119 ? 35.705 -13.712 -7.449  1.00 13.74 ?  119 HIS   B H    1 
ATOM   5775 H HA   . HIS   B 1 119 ? 37.297 -11.961 -8.771  1.00 14.09 ?  119 HIS   B HA   1 
ATOM   5776 H HB2  . HIS   B 1 119 ? 38.234 -14.440 -7.768  1.00 14.89 ?  119 HIS   B HB2  1 
ATOM   5777 H HB3  . HIS   B 1 119 ? 39.095 -13.453 -8.670  1.00 14.89 ?  119 HIS   B HB3  1 
ATOM   5778 H HD2  . HIS   B 1 119 ? 38.052 -13.678 -5.110  1.00 18.12 ?  119 HIS   B HD2  1 
ATOM   5779 H HE1  . HIS   B 1 119 ? 40.441 -10.534 -5.362  1.00 19.68 ?  119 HIS   B HE1  1 
ATOM   5780 H HE2  . HIS   B 1 119 ? 39.243 -11.947 -3.895  1.00 19.91 ?  119 HIS   B HE2  1 
ATOM   5781 N N    . GLU   B 1 120 ? 36.803 -13.011 -10.944 1.00 12.28 ?  120 GLU   B N    1 
ATOM   5782 C CA   . GLU   B 1 120 ? 36.204 -13.594 -12.137 1.00 13.69 ?  120 GLU   B CA   1 
ATOM   5783 C C    . GLU   B 1 120 ? 36.883 -14.892 -12.552 1.00 12.91 ?  120 GLU   B C    1 
ATOM   5784 O O    . GLU   B 1 120 ? 36.226 -15.765 -13.128 1.00 12.86 ?  120 GLU   B O    1 
ATOM   5785 C CB   . GLU   B 1 120 ? 36.203 -12.586 -13.283 1.00 17.52 ?  120 GLU   B CB   1 
ATOM   5786 C CG   . GLU   B 1 120 ? 35.293 -11.402 -13.020 1.00 23.07 ?  120 GLU   B CG   1 
ATOM   5787 C CD   . GLU   B 1 120 ? 35.063 -10.537 -14.237 1.00 28.40 ?  120 GLU   B CD   1 
ATOM   5788 O OE1  . GLU   B 1 120 ? 36.029 -10.303 -14.993 1.00 30.45 ?  120 GLU   B OE1  1 
ATOM   5789 O OE2  . GLU   B 1 120 ? 33.913 -10.090 -14.429 1.00 31.25 -1 120 GLU   B OE2  1 
ATOM   5790 H H    . GLU   B 1 120 ? 37.242 -12.279 -11.075 1.00 14.72 ?  120 GLU   B H    1 
ATOM   5791 H HA   . GLU   B 1 120 ? 35.282 -13.809 -11.941 1.00 16.40 ?  120 GLU   B HA   1 
ATOM   5792 H HB2  . GLU   B 1 120 ? 37.101 -12.250 -13.414 1.00 21.00 ?  120 GLU   B HB2  1 
ATOM   5793 H HB3  . GLU   B 1 120 ? 35.891 -13.025 -14.091 1.00 21.00 ?  120 GLU   B HB3  1 
ATOM   5794 H HG2  . GLU   B 1 120 ? 34.426 -11.723 -12.734 1.00 27.66 ?  120 GLU   B HG2  1 
ATOM   5795 H HG3  . GLU   B 1 120 ? 35.688 -10.847 -12.330 1.00 27.66 ?  120 GLU   B HG3  1 
ATOM   5796 N N    . VAL   B 1 121 ? 38.182 -15.030 -12.284 1.00 12.50 ?  121 VAL   B N    1 
ATOM   5797 C CA   . VAL   B 1 121 ? 38.928 -16.238 -12.633 1.00 11.99 ?  121 VAL   B CA   1 
ATOM   5798 C C    . VAL   B 1 121 ? 40.038 -16.442 -11.612 1.00 11.82 ?  121 VAL   B C    1 
ATOM   5799 O O    . VAL   B 1 121 ? 40.719 -15.486 -11.224 1.00 12.63 ?  121 VAL   B O    1 
ATOM   5800 C CB   . VAL   B 1 121 ? 39.445 -16.194 -14.090 1.00 13.75 ?  121 VAL   B CB   1 
ATOM   5801 C CG1  . VAL   B 1 121 ? 40.320 -14.972 -14.336 1.00 15.18 ?  121 VAL   B CG1  1 
ATOM   5802 C CG2  . VAL   B 1 121 ? 40.180 -17.477 -14.443 1.00 15.31 ?  121 VAL   B CG2  1 
ATOM   5803 H H    . VAL   B 1 121 ? 38.665 -14.426 -11.901 1.00 14.97 ?  121 VAL   B H    1 
ATOM   5804 H HA   . VAL   B 1 121 ? 38.319 -16.990 -12.566 1.00 14.36 ?  121 VAL   B HA   1 
ATOM   5805 H HB   . VAL   B 1 121 ? 38.679 -16.126 -14.685 1.00 16.48 ?  121 VAL   B HB   1 
ATOM   5806 H HG11 . VAL   B 1 121 ? 40.623 -14.982 -15.258 1.00 18.19 ?  121 VAL   B HG11 1 
ATOM   5807 H HG12 . VAL   B 1 121 ? 39.798 -14.170 -14.171 1.00 18.19 ?  121 VAL   B HG12 1 
ATOM   5808 H HG13 . VAL   B 1 121 ? 41.080 -15.001 -13.737 1.00 18.19 ?  121 VAL   B HG13 1 
ATOM   5809 H HG21 . VAL   B 1 121 ? 40.382 -17.472 -15.393 1.00 18.34 ?  121 VAL   B HG21 1 
ATOM   5810 H HG22 . VAL   B 1 121 ? 41.004 -17.520 -13.933 1.00 18.34 ?  121 VAL   B HG22 1 
ATOM   5811 H HG23 . VAL   B 1 121 ? 39.615 -18.234 -14.230 1.00 18.34 ?  121 VAL   B HG23 1 
ATOM   5812 N N    . LEU   B 1 122 ? 40.226 -17.694 -11.180 1.00 11.21 ?  122 LEU   B N    1 
ATOM   5813 C CA   . LEU   B 1 122 ? 41.212 -18.037 -10.159 1.00 11.19 ?  122 LEU   B CA   1 
ATOM   5814 C C    . LEU   B 1 122 ? 41.868 -19.367 -10.484 1.00 10.90 ?  122 LEU   B C    1 
ATOM   5815 O O    . LEU   B 1 122 ? 41.208 -20.287 -10.984 1.00 12.19 ?  122 LEU   B O    1 
ATOM   5816 C CB   . LEU   B 1 122 ? 40.562 -18.264 -8.782  1.00 12.98 ?  122 LEU   B CB   1 
ATOM   5817 C CG   . LEU   B 1 122 ? 39.527 -17.246 -8.300  1.00 13.21 ?  122 LEU   B CG   1 
ATOM   5818 C CD1  . LEU   B 1 122 ? 38.128 -17.595 -8.787  1.00 13.99 ?  122 LEU   B CD1  1 
ATOM   5819 C CD2  . LEU   B 1 122 ? 39.569 -17.135 -6.792  1.00 13.00 ?  122 LEU   B CD2  1 
ATOM   5820 H H    . LEU   B 1 122 ? 39.788 -18.376 -11.468 1.00 13.42 ?  122 LEU   B H    1 
ATOM   5821 H HA   . LEU   B 1 122 ? 41.888 -17.343 -10.082 1.00 13.40 ?  122 LEU   B HA   1 
ATOM   5822 H HB2  . LEU   B 1 122 ? 40.120 -19.127 -8.800  1.00 15.55 ?  122 LEU   B HB2  1 
ATOM   5823 H HB3  . LEU   B 1 122 ? 41.269 -18.286 -8.116  1.00 15.55 ?  122 LEU   B HB3  1 
ATOM   5824 H HG   . LEU   B 1 122 ? 39.759 -16.377 -8.662  1.00 15.83 ?  122 LEU   B HG   1 
ATOM   5825 H HD11 . LEU   B 1 122 ? 37.500 -16.962 -8.408  1.00 16.76 ?  122 LEU   B HD11 1 
ATOM   5826 H HD12 . LEU   B 1 122 ? 38.110 -17.538 -9.756  1.00 16.76 ?  122 LEU   B HD12 1 
ATOM   5827 H HD13 . LEU   B 1 122 ? 37.911 -18.493 -8.502  1.00 16.76 ?  122 LEU   B HD13 1 
ATOM   5828 H HD21 . LEU   B 1 122 ? 38.888 -16.512 -6.499  1.00 15.58 ?  122 LEU   B HD21 1 
ATOM   5829 H HD22 . LEU   B 1 122 ? 39.410 -18.010 -6.404  1.00 15.58 ?  122 LEU   B HD22 1 
ATOM   5830 H HD23 . LEU   B 1 122 ? 40.448 -16.813 -6.521  1.00 15.58 ?  122 LEU   B HD23 1 
ATOM   5831 N N    . LEU   B 1 123 ? 43.155 -19.470 -10.133 1.00 10.74 ?  123 LEU   B N    1 
ATOM   5832 C CA   . LEU   B 1 123 ? 43.867 -20.741 -10.010 1.00 11.24 ?  123 LEU   B CA   1 
ATOM   5833 C C    . LEU   B 1 123 ? 43.839 -21.132 -8.538  1.00 10.71 ?  123 LEU   B C    1 
ATOM   5834 O O    . LEU   B 1 123 ? 44.187 -20.304 -7.685  1.00 11.30 ?  123 LEU   B O    1 
ATOM   5835 C CB   . LEU   B 1 123 ? 45.316 -20.560 -10.465 1.00 11.45 ?  123 LEU   B CB   1 
ATOM   5836 C CG   . LEU   B 1 123 ? 46.262 -21.733 -10.213 1.00 11.63 ?  123 LEU   B CG   1 
ATOM   5837 C CD1  . LEU   B 1 123 ? 45.843 -22.980 -10.987 1.00 12.31 ?  123 LEU   B CD1  1 
ATOM   5838 C CD2  . LEU   B 1 123 ? 47.687 -21.338 -10.566 1.00 12.61 ?  123 LEU   B CD2  1 
ATOM   5839 H H    . LEU   B 1 123 ? 43.652 -18.788 -9.941  1.00 12.87 ?  123 LEU   B H    1 
ATOM   5840 H HA   . LEU   B 1 123 ? 43.434 -21.427 -10.540 1.00 13.47 ?  123 LEU   B HA   1 
ATOM   5841 H HB2  . LEU   B 1 123 ? 45.313 -20.396 -11.423 1.00 13.71 ?  123 LEU   B HB2  1 
ATOM   5842 H HB3  . LEU   B 1 123 ? 45.686 -19.790 -10.010 1.00 13.71 ?  123 LEU   B HB3  1 
ATOM   5843 H HG   . LEU   B 1 123 ? 46.248 -21.958 -9.268  1.00 13.93 ?  123 LEU   B HG   1 
ATOM   5844 H HD11 . LEU   B 1 123 ? 46.479 -23.690 -10.811 1.00 14.75 ?  123 LEU   B HD11 1 
ATOM   5845 H HD12 . LEU   B 1 123 ? 44.957 -23.249 -10.695 1.00 14.75 ?  123 LEU   B HD12 1 
ATOM   5846 H HD13 . LEU   B 1 123 ? 45.830 -22.772 -11.933 1.00 14.75 ?  123 LEU   B HD13 1 
ATOM   5847 H HD21 . LEU   B 1 123 ? 48.276 -22.090 -10.401 1.00 15.11 ?  123 LEU   B HD21 1 
ATOM   5848 H HD22 . LEU   B 1 123 ? 47.721 -21.088 -11.503 1.00 15.11 ?  123 LEU   B HD22 1 
ATOM   5849 H HD23 . LEU   B 1 123 ? 47.950 -20.584 -10.014 1.00 15.11 ?  123 LEU   B HD23 1 
ATOM   5850 N N    . ALA   B 1 124 ? 43.408 -22.364 -8.230  1.00 10.88 ?  124 ALA   B N    1 
ATOM   5851 C CA   . ALA   B 1 124 ? 43.144 -22.687 -6.836  1.00 11.02 ?  124 ALA   B CA   1 
ATOM   5852 C C    . ALA   B 1 124 ? 43.415 -24.147 -6.509  1.00 10.61 ?  124 ALA   B C    1 
ATOM   5853 O O    . ALA   B 1 124 ? 43.292 -25.019 -7.381  1.00 11.09 ?  124 ALA   B O    1 
ATOM   5854 C CB   . ALA   B 1 124 ? 41.685 -22.378 -6.475  1.00 11.71 ?  124 ALA   B CB   1 
ATOM   5855 H H    . ALA   B 1 124 ? 43.255 -23.004 -8.789  1.00 13.03 ?  124 ALA   B H    1 
ATOM   5856 H HA   . ALA   B 1 124 ? 43.712 -22.131 -6.281  1.00 13.20 ?  124 ALA   B HA   1 
ATOM   5857 H HB1  . ALA   B 1 124 ? 41.529 -22.596 -5.543  1.00 14.02 ?  124 ALA   B HB1  1 
ATOM   5858 H HB2  . ALA   B 1 124 ? 41.515 -21.431 -6.623  1.00 14.02 ?  124 ALA   B HB2  1 
ATOM   5859 H HB3  . ALA   B 1 124 ? 41.098 -22.906 -7.040  1.00 14.02 ?  124 ALA   B HB3  1 
ATOM   5860 N N    . PRO   B 1 125 ? 43.709 -24.442 -5.248  1.00 10.55 ?  125 PRO   B N    1 
ATOM   5861 C CA   . PRO   B 1 125 ? 43.650 -25.808 -4.731  1.00 11.16 ?  125 PRO   B CA   1 
ATOM   5862 C C    . PRO   B 1 125 ? 42.246 -26.079 -4.191  1.00 11.62 ?  125 PRO   B C    1 
ATOM   5863 O O    . PRO   B 1 125 ? 41.448 -25.165 -3.980  1.00 11.99 ?  125 PRO   B O    1 
ATOM   5864 C CB   . PRO   B 1 125 ? 44.636 -25.734 -3.562  1.00 12.38 ?  125 PRO   B CB   1 
ATOM   5865 C CG   . PRO   B 1 125 ? 44.376 -24.346 -2.985  1.00 12.68 ?  125 PRO   B CG   1 
ATOM   5866 C CD   . PRO   B 1 125 ? 44.025 -23.473 -4.182  1.00 11.37 ?  125 PRO   B CD   1 
ATOM   5867 H HA   . PRO   B 1 125 ? 43.924 -26.470 -5.383  1.00 13.37 ?  125 PRO   B HA   1 
ATOM   5868 H HB2  . PRO   B 1 125 ? 44.438 -26.423 -2.908  1.00 14.83 ?  125 PRO   B HB2  1 
ATOM   5869 H HB3  . PRO   B 1 125 ? 45.547 -25.808 -3.884  1.00 14.83 ?  125 PRO   B HB3  1 
ATOM   5870 H HG2  . PRO   B 1 125 ? 43.630 -24.380 -2.359  1.00 15.20 ?  125 PRO   B HG2  1 
ATOM   5871 H HG3  . PRO   B 1 125 ? 45.174 -24.016 -2.535  1.00 15.20 ?  125 PRO   B HG3  1 
ATOM   5872 H HD2  . PRO   B 1 125 ? 43.259 -22.911 -3.988  1.00 13.63 ?  125 PRO   B HD2  1 
ATOM   5873 H HD3  . PRO   B 1 125 ? 44.798 -22.928 -4.438  1.00 13.63 ?  125 PRO   B HD3  1 
ATOM   5874 N N    . LEU   B 1 126 ? 41.971 -27.356 -3.923  1.00 12.16 ?  126 LEU   B N    1 
ATOM   5875 C CA   . LEU   B 1 126 ? 40.748 -27.723 -3.216  1.00 12.84 ?  126 LEU   B CA   1 
ATOM   5876 C C    . LEU   B 1 126 ? 40.861 -27.324 -1.752  1.00 12.60 ?  126 LEU   B C    1 
ATOM   5877 O O    . LEU   B 1 126 ? 41.758 -27.779 -1.036  1.00 14.32 ?  126 LEU   B O    1 
ATOM   5878 C CB   . LEU   B 1 126 ? 40.492 -29.221 -3.331  1.00 13.94 ?  126 LEU   B CB   1 
ATOM   5879 C CG   . LEU   B 1 126 ? 39.977 -29.706 -4.685  1.00 14.51 ?  126 LEU   B CG   1 
ATOM   5880 C CD1  . LEU   B 1 126 ? 40.019 -31.221 -4.773  1.00 16.11 ?  126 LEU   B CD1  1 
ATOM   5881 C CD2  . LEU   B 1 126 ? 38.562 -29.191 -4.946  1.00 14.56 ?  126 LEU   B CD2  1 
ATOM   5882 H H    . LEU   B 1 126 ? 42.481 -28.022 -4.122  1.00 14.57 ?  126 LEU   B H    1 
ATOM   5883 H HA   . LEU   B 1 126 ? 40.002 -27.245 -3.604  1.00 15.39 ?  126 LEU   B HA   1 
ATOM   5884 H HB2  . LEU   B 1 126 ? 41.318 -29.686 -3.149  1.00 16.70 ?  126 LEU   B HB2  1 
ATOM   5885 H HB3  . LEU   B 1 126 ? 39.827 -29.464 -2.666  1.00 16.70 ?  126 LEU   B HB3  1 
ATOM   5886 H HG   . LEU   B 1 126 ? 40.555 -29.352 -5.381  1.00 17.39 ?  126 LEU   B HG   1 
ATOM   5887 H HD11 . LEU   B 1 126 ? 39.686 -31.497 -5.642  1.00 19.31 ?  126 LEU   B HD11 1 
ATOM   5888 H HD12 . LEU   B 1 126 ? 40.931 -31.523 -4.656  1.00 19.31 ?  126 LEU   B HD12 1 
ATOM   5889 H HD13 . LEU   B 1 126 ? 39.455 -31.593 -4.073  1.00 19.31 ?  126 LEU   B HD13 1 
ATOM   5890 H HD21 . LEU   B 1 126 ? 38.217 -29.606 -5.751  1.00 17.45 ?  126 LEU   B HD21 1 
ATOM   5891 H HD22 . LEU   B 1 126 ? 37.999 -29.412 -4.190  1.00 17.45 ?  126 LEU   B HD22 1 
ATOM   5892 H HD23 . LEU   B 1 126 ? 38.590 -28.225 -5.063  1.00 17.45 ?  126 LEU   B HD23 1 
ATOM   5893 N N    . LEU   B 1 127 ? 39.930 -26.495 -1.297  1.00 12.40 ?  127 LEU   B N    1 
ATOM   5894 C CA   . LEU   B 1 127 ? 39.976 -26.009 0.068   1.00 12.34 ?  127 LEU   B CA   1 
ATOM   5895 C C    . LEU   B 1 127 ? 39.712 -27.132 1.057   1.00 12.36 ?  127 LEU   B C    1 
ATOM   5896 O O    . LEU   B 1 127 ? 38.889 -28.025 0.827   1.00 12.76 ?  127 LEU   B O    1 
ATOM   5897 C CB   . LEU   B 1 127 ? 38.948 -24.894 0.274   1.00 13.11 ?  127 LEU   B CB   1 
ATOM   5898 C CG   . LEU   B 1 127 ? 39.137 -23.627 -0.565  1.00 13.64 ?  127 LEU   B CG   1 
ATOM   5899 C CD1  . LEU   B 1 127 ? 38.007 -22.657 -0.248  1.00 14.15 ?  127 LEU   B CD1  1 
ATOM   5900 C CD2  . LEU   B 1 127 ? 40.499 -22.979 -0.328  1.00 14.44 ?  127 LEU   B CD2  1 
ATOM   5901 H H    . LEU   B 1 127 ? 39.258 -26.200 -1.756  1.00 14.86 ?  127 LEU   B H    1 
ATOM   5902 H HA   . LEU   B 1 127 ? 40.859 -25.639 0.246   1.00 14.78 ?  127 LEU   B HA   1 
ATOM   5903 H HB2  . LEU   B 1 127 ? 38.068 -25.249 0.066   1.00 15.71 ?  127 LEU   B HB2  1 
ATOM   5904 H HB3  . LEU   B 1 127 ? 38.969 -24.625 1.208   1.00 15.71 ?  127 LEU   B HB3  1 
ATOM   5905 H HG   . LEU   B 1 127 ? 39.062 -23.851 -1.502  1.00 16.34 ?  127 LEU   B HG   1 
ATOM   5906 H HD11 . LEU   B 1 127 ? 38.123 -21.845 -0.773  1.00 16.95 ?  127 LEU   B HD11 1 
ATOM   5907 H HD12 . LEU   B 1 127 ? 37.155 -23.067 -0.464  1.00 16.95 ?  127 LEU   B HD12 1 
ATOM   5908 H HD13 . LEU   B 1 127 ? 38.031 -22.434 0.700   1.00 16.95 ?  127 LEU   B HD13 1 
ATOM   5909 H HD21 . LEU   B 1 127 ? 40.533 -22.125 -0.791  1.00 17.31 ?  127 LEU   B HD21 1 
ATOM   5910 H HD22 . LEU   B 1 127 ? 40.625 -22.839 0.625   1.00 17.31 ?  127 LEU   B HD22 1 
ATOM   5911 H HD23 . LEU   B 1 127 ? 41.188 -23.567 -0.670  1.00 17.31 ?  127 LEU   B HD23 1 
ATOM   5912 N N    . SER   B 1 128 ? 40.396 -27.046 2.185   1.00 12.25 ?  128 SER   B N    1 
ATOM   5913 C CA   . SER   B 1 128 ? 40.294 -27.966 3.304   1.00 12.93 ?  128 SER   B CA   1 
ATOM   5914 C C    . SER   B 1 128 ? 40.789 -29.371 2.976   1.00 13.41 ?  128 SER   B C    1 
ATOM   5915 O O    . SER   B 1 128 ? 40.695 -30.256 3.826   1.00 15.17 ?  128 SER   B O    1 
ATOM   5916 C CB   . SER   B 1 128 ? 38.898 -27.986 3.937   1.00 13.22 ?  128 SER   B CB   1 
ATOM   5917 O OG   . SER   B 1 128 ? 38.574 -26.709 4.483   1.00 14.06 ?  128 SER   B OG   1 
ATOM   5918 H H    . SER   B 1 128 ? 40.962 -26.414 2.335   1.00 14.68 ?  128 SER   B H    1 
ATOM   5919 H HA   . SER   B 1 128 ? 40.883 -27.634 3.987   1.00 15.49 ?  128 SER   B HA   1 
ATOM   5920 H HB2  . SER   B 1 128 ? 38.238 -28.223 3.265   1.00 15.84 ?  128 SER   B HB2  1 
ATOM   5921 H HB3  . SER   B 1 128 ? 38.885 -28.654 4.652   1.00 15.84 ?  128 SER   B HB3  1 
ATOM   5922 H HG   . SER   B 1 128 ? 39.139 -26.507 5.074   1.00 16.85 ?  128 SER   B HG   1 
ATOM   5923 N N    . ALA   B 1 129 ? 41.360 -29.589 1.789   1.00 14.40 ?  129 ALA   B N    1 
ATOM   5924 C CA   . ALA   B 1 129 ? 41.906 -30.887 1.429   1.00 15.48 ?  129 ALA   B CA   1 
ATOM   5925 C C    . ALA   B 1 129 ? 43.293 -31.068 2.033   1.00 14.57 ?  129 ALA   B C    1 
ATOM   5926 O O    . ALA   B 1 129 ? 43.858 -30.166 2.669   1.00 14.64 ?  129 ALA   B O    1 
ATOM   5927 C CB   . ALA   B 1 129 ? 41.958 -31.046 -0.088  1.00 17.52 ?  129 ALA   B CB   1 
ATOM   5928 H H    . ALA   B 1 129 ? 41.438 -28.994 1.171   1.00 17.26 ?  129 ALA   B H    1 
ATOM   5929 H HA   . ALA   B 1 129 ? 41.333 -31.579 1.784   1.00 18.55 ?  129 ALA   B HA   1 
ATOM   5930 H HB1  . ALA   B 1 129 ? 42.320 -31.922 -0.299  1.00 21.00 ?  129 ALA   B HB1  1 
ATOM   5931 H HB2  . ALA   B 1 129 ? 41.060 -30.964 -0.442  1.00 21.00 ?  129 ALA   B HB2  1 
ATOM   5932 H HB3  . ALA   B 1 129 ? 42.527 -30.355 -0.460  1.00 21.00 ?  129 ALA   B HB3  1 
ATOM   5933 N N    . GLY   B 1 130 ? 43.846 -32.264 1.821   1.00 14.87 ?  130 GLY   B N    1 
ATOM   5934 C CA   . GLY   B 1 130 ? 45.229 -32.512 2.174   1.00 15.76 ?  130 GLY   B CA   1 
ATOM   5935 C C    . GLY   B 1 130 ? 45.443 -32.407 3.666   1.00 15.57 ?  130 GLY   B C    1 
ATOM   5936 O O    . GLY   B 1 130 ? 44.748 -33.046 4.470   1.00 16.48 ?  130 GLY   B O    1 
ATOM   5937 H H    . GLY   B 1 130 ? 43.439 -32.934 1.467   1.00 17.82 ?  130 GLY   B H    1 
ATOM   5938 H HA2  . GLY   B 1 130 ? 45.480 -33.405 1.886   1.00 18.89 ?  130 GLY   B HA2  1 
ATOM   5939 H HA3  . GLY   B 1 130 ? 45.801 -31.870 1.729   1.00 18.89 ?  130 GLY   B HA3  1 
ATOM   5940 N N    . ILE   B 1 131 ? 46.411 -31.569 4.047   1.00 15.61 ?  131 ILE   B N    1 
ATOM   5941 C CA   . ILE   B 1 131 ? 46.768 -31.428 5.453   1.00 16.43 ?  131 ILE   B CA   1 
ATOM   5942 C C    . ILE   B 1 131 ? 45.647 -30.832 6.288   1.00 15.58 ?  131 ILE   B C    1 
ATOM   5943 O O    . ILE   B 1 131 ? 45.714 -30.903 7.518   1.00 17.27 ?  131 ILE   B O    1 
ATOM   5944 C CB   . ILE   B 1 131 ? 48.087 -30.648 5.646   1.00 18.31 ?  131 ILE   B CB   1 
ATOM   5945 C CG1  . ILE   B 1 131 ? 47.929 -29.176 5.236   1.00 19.20 ?  131 ILE   B CG1  1 
ATOM   5946 C CG2  . ILE   B 1 131 ? 49.214 -31.314 4.865   1.00 19.33 ?  131 ILE   B CG2  1 
ATOM   5947 C CD1  . ILE   B 1 131 ? 49.133 -28.310 5.576   1.00 20.47 ?  131 ILE   B CD1  1 
ATOM   5948 H H    . ILE   B 1 131 ? 46.873 -31.080 3.513   1.00 18.71 ?  131 ILE   B H    1 
ATOM   5949 H HA   . ILE   B 1 131 ? 46.917 -32.316 5.804   1.00 19.70 ?  131 ILE   B HA   1 
ATOM   5950 H HB   . ILE   B 1 131 ? 48.312 -30.675 6.589   1.00 21.94 ?  131 ILE   B HB   1 
ATOM   5951 H HG12 . ILE   B 1 131 ? 47.791 -29.131 4.278   1.00 23.01 ?  131 ILE   B HG12 1 
ATOM   5952 H HG13 . ILE   B 1 131 ? 47.160 -28.795 5.694   1.00 23.01 ?  131 ILE   B HG13 1 
ATOM   5953 H HG21 . ILE   B 1 131 ? 50.054 -30.911 5.125   1.00 23.17 ?  131 ILE   B HG21 1 
ATOM   5954 H HG22 . ILE   B 1 131 ? 49.217 -32.260 5.071   1.00 23.17 ?  131 ILE   B HG22 1 
ATOM   5955 H HG23 . ILE   B 1 131 ? 49.057 -31.181 3.917   1.00 23.17 ?  131 ILE   B HG23 1 
ATOM   5956 H HD11 . ILE   B 1 131 ? 48.926 -27.386 5.362   1.00 24.54 ?  131 ILE   B HD11 1 
ATOM   5957 H HD12 . ILE   B 1 131 ? 49.323 -28.394 6.524   1.00 24.54 ?  131 ILE   B HD12 1 
ATOM   5958 H HD13 . ILE   B 1 131 ? 49.893 -28.609 5.057   1.00 24.54 ?  131 ILE   B HD13 1 
ATOM   5959 N N    . PHE   B 1 132 ? 44.619 -30.251 5.656   1.00 14.26 ?  132 PHE   B N    1 
ATOM   5960 C CA   . PHE   B 1 132 ? 43.455 -29.749 6.381   1.00 14.84 ?  132 PHE   B CA   1 
ATOM   5961 C C    . PHE   B 1 132 ? 42.434 -30.840 6.700   1.00 16.02 ?  132 PHE   B C    1 
ATOM   5962 O O    . PHE   B 1 132 ? 41.522 -30.591 7.493   1.00 17.63 ?  132 PHE   B O    1 
ATOM   5963 C CB   . PHE   B 1 132 ? 42.782 -28.610 5.602   1.00 14.05 ?  132 PHE   B CB   1 
ATOM   5964 C CG   . PHE   B 1 132 ? 43.479 -27.271 5.729   1.00 14.58 ?  132 PHE   B CG   1 
ATOM   5965 C CD1  . PHE   B 1 132 ? 44.778 -27.088 5.275   1.00 15.94 ?  132 PHE   B CD1  1 
ATOM   5966 C CD2  . PHE   B 1 132 ? 42.803 -26.180 6.255   1.00 13.86 ?  132 PHE   B CD2  1 
ATOM   5967 C CE1  . PHE   B 1 132 ? 45.401 -25.853 5.379   1.00 16.45 ?  132 PHE   B CE1  1 
ATOM   5968 C CE2  . PHE   B 1 132 ? 43.416 -24.939 6.359   1.00 14.35 ?  132 PHE   B CE2  1 
ATOM   5969 C CZ   . PHE   B 1 132 ? 44.714 -24.778 5.919   1.00 15.82 ?  132 PHE   B CZ   1 
ATOM   5970 H H    . PHE   B 1 132 ? 44.574 -30.133 4.801   1.00 17.09 ?  132 PHE   B H    1 
ATOM   5971 H HA   . PHE   B 1 132 ? 43.760 -29.375 7.220   1.00 17.79 ?  132 PHE   B HA   1 
ATOM   5972 H HB2  . PHE   B 1 132 ? 42.771 -28.842 4.663   1.00 16.83 ?  132 PHE   B HB2  1 
ATOM   5973 H HB3  . PHE   B 1 132 ? 41.874 -28.502 5.927   1.00 16.83 ?  132 PHE   B HB3  1 
ATOM   5974 H HD1  . PHE   B 1 132 ? 45.243 -27.811 4.917   1.00 19.10 ?  132 PHE   B HD1  1 
ATOM   5975 H HD2  . PHE   B 1 132 ? 41.927 -26.283 6.550   1.00 16.60 ?  132 PHE   B HD2  1 
ATOM   5976 H HE1  . PHE   B 1 132 ? 46.277 -25.745 5.085   1.00 19.72 ?  132 PHE   B HE1  1 
ATOM   5977 H HE2  . PHE   B 1 132 ? 42.951 -24.216 6.722   1.00 17.20 ?  132 PHE   B HE2  1 
ATOM   5978 H HZ   . PHE   B 1 132 ? 45.127 -23.943 5.992   1.00 18.96 ?  132 PHE   B HZ   1 
ATOM   5979 N N    . GLY   B 1 133 ? 42.544 -32.031 6.098   1.00 15.52 ?  133 GLY   B N    1 
ATOM   5980 C CA   . GLY   B 1 133 ? 41.838 -33.207 6.582   1.00 16.20 ?  133 GLY   B CA   1 
ATOM   5981 C C    . GLY   B 1 133 ? 40.436 -33.456 6.062   1.00 16.44 ?  133 GLY   B C    1 
ATOM   5982 O O    . GLY   B 1 133 ? 39.839 -34.467 6.445   1.00 18.13 ?  133 GLY   B O    1 
ATOM   5983 H H    . GLY   B 1 133 ? 43.033 -32.175 5.403   1.00 18.60 ?  133 GLY   B H    1 
ATOM   5984 H HA2  . GLY   B 1 133 ? 42.368 -33.987 6.362   1.00 19.42 ?  133 GLY   B HA2  1 
ATOM   5985 H HA3  . GLY   B 1 133 ? 41.789 -33.150 7.549   1.00 19.42 ?  133 GLY   B HA3  1 
ATOM   5986 N N    . ALA   B 1 134 ? 39.883 -32.593 5.218   1.00 15.63 ?  134 ALA   B N    1 
ATOM   5987 C CA   . ALA   B 1 134 ? 38.552 -32.864 4.695   1.00 16.03 ?  134 ALA   B CA   1 
ATOM   5988 C C    . ALA   B 1 134 ? 38.630 -33.858 3.540   1.00 15.82 ?  134 ALA   B C    1 
ATOM   5989 O O    . ALA   B 1 134 ? 39.683 -34.057 2.928   1.00 17.20 ?  134 ALA   B O    1 
ATOM   5990 C CB   . ALA   B 1 134 ? 37.869 -31.576 4.239   1.00 16.32 ?  134 ALA   B CB   1 
ATOM   5991 H H    . ALA   B 1 134 ? 40.247 -31.858 4.941   1.00 18.74 ?  134 ALA   B H    1 
ATOM   5992 H HA   . ALA   B 1 134 ? 38.012 -33.255 5.400   1.00 19.21 ?  134 ALA   B HA   1 
ATOM   5993 H HB1  . ALA   B 1 134 ? 36.981 -31.791 3.910   1.00 19.56 ?  134 ALA   B HB1  1 
ATOM   5994 H HB2  . ALA   B 1 134 ? 37.801 -30.968 4.994   1.00 19.56 ?  134 ALA   B HB2  1 
ATOM   5995 H HB3  . ALA   B 1 134 ? 38.394 -31.170 3.534   1.00 19.56 ?  134 ALA   B HB3  1 
ATOM   5996 N N    . ASP   B 1 135 ? 37.494 -34.484 3.250   1.00 15.69 ?  135 ASP   B N    1 
ATOM   5997 C CA   . ASP   B 1 135 ? 37.398 -35.387 2.112   1.00 16.68 ?  135 ASP   B CA   1 
ATOM   5998 C C    . ASP   B 1 135 ? 37.501 -34.552 0.843   1.00 15.61 ?  135 ASP   B C    1 
ATOM   5999 O O    . ASP   B 1 135 ? 36.649 -33.680 0.620   1.00 15.65 ?  135 ASP   B O    1 
ATOM   6000 C CB   . ASP   B 1 135 ? 36.051 -36.112 2.170   1.00 18.32 ?  135 ASP   B CB   1 
ATOM   6001 C CG   . ASP   B 1 135 ? 35.853 -37.099 1.032   1.00 20.12 ?  135 ASP   B CG   1 
ATOM   6002 O OD1  . ASP   B 1 135 ? 36.712 -37.165 0.128   1.00 20.20 ?  135 ASP   B OD1  1 
ATOM   6003 O OD2  . ASP   B 1 135 ? 34.833 -37.830 1.058   1.00 23.20 -1 135 ASP   B OD2  1 
ATOM   6004 H H    . ASP   B 1 135 ? 36.765 -34.399 3.698   1.00 18.81 ?  135 ASP   B H    1 
ATOM   6005 H HA   . ASP   B 1 135 ? 38.115 -36.041 2.149   1.00 20.00 ?  135 ASP   B HA   1 
ATOM   6006 H HB2  . ASP   B 1 135 ? 35.998 -36.602 3.003   1.00 21.96 ?  135 ASP   B HB2  1 
ATOM   6007 H HB3  . ASP   B 1 135 ? 35.344 -35.455 2.119   1.00 21.96 ?  135 ASP   B HB3  1 
ATOM   6008 N N    . PRO   B 1 136 ? 38.516 -34.758 -0.000  1.00 16.20 ?  136 PRO   B N    1 
ATOM   6009 C CA   . PRO   B 1 136 ? 38.621 -33.934 -1.214  1.00 15.25 ?  136 PRO   B CA   1 
ATOM   6010 C C    . PRO   B 1 136 ? 37.439 -34.092 -2.152  1.00 14.82 ?  136 PRO   B C    1 
ATOM   6011 O O    . PRO   B 1 136 ? 37.123 -33.148 -2.885  1.00 14.18 ?  136 PRO   B O    1 
ATOM   6012 C CB   . PRO   B 1 136 ? 39.943 -34.396 -1.846  1.00 16.26 ?  136 PRO   B CB   1 
ATOM   6013 C CG   . PRO   B 1 136 ? 40.150 -35.785 -1.310  1.00 17.45 ?  136 PRO   B CG   1 
ATOM   6014 C CD   . PRO   B 1 136 ? 39.586 -35.768 0.081   1.00 17.09 ?  136 PRO   B CD   1 
ATOM   6015 H HA   . PRO   B 1 136 ? 38.698 -32.996 -0.974  1.00 18.28 ?  136 PRO   B HA   1 
ATOM   6016 H HB2  . PRO   B 1 136 ? 39.859 -34.407 -2.814  1.00 19.49 ?  136 PRO   B HB2  1 
ATOM   6017 H HB3  . PRO   B 1 136 ? 40.661 -33.805 -1.571  1.00 19.49 ?  136 PRO   B HB3  1 
ATOM   6018 H HG2  . PRO   B 1 136 ? 39.678 -36.427 -1.862  1.00 20.92 ?  136 PRO   B HG2  1 
ATOM   6019 H HG3  . PRO   B 1 136 ? 41.100 -35.989 -1.287  1.00 20.92 ?  136 PRO   B HG3  1 
ATOM   6020 H HD2  . PRO   B 1 136 ? 39.210 -36.633 0.310   1.00 20.49 ?  136 PRO   B HD2  1 
ATOM   6021 H HD3  . PRO   B 1 136 ? 40.258 -35.491 0.726   1.00 20.49 ?  136 PRO   B HD3  1 
ATOM   6022 N N    . ILE   B 1 137 ? 36.773 -35.251 -2.147  1.00 15.02 ?  137 ILE   B N    1 
ATOM   6023 C CA   . ILE   B 1 137 ? 35.565 -35.417 -2.951  1.00 15.72 ?  137 ILE   B CA   1 
ATOM   6024 C C    . ILE   B 1 137 ? 34.487 -34.452 -2.481  1.00 15.44 ?  137 ILE   B C    1 
ATOM   6025 O O    . ILE   B 1 137 ? 33.776 -33.846 -3.291  1.00 14.97 ?  137 ILE   B O    1 
ATOM   6026 C CB   . ILE   B 1 137 ? 35.095 -36.886 -2.904  1.00 17.40 ?  137 ILE   B CB   1 
ATOM   6027 C CG1  . ILE   B 1 137 ? 36.098 -37.781 -3.639  1.00 19.98 ?  137 ILE   B CG1  1 
ATOM   6028 C CG2  . ILE   B 1 137 ? 33.692 -37.037 -3.497  1.00 17.92 ?  137 ILE   B CG2  1 
ATOM   6029 C CD1  . ILE   B 1 137 ? 35.802 -39.267 -3.523  1.00 22.59 ?  137 ILE   B CD1  1 
ATOM   6030 H H    . ILE   B 1 137 ? 36.992 -35.947 -1.692  1.00 18.01 ?  137 ILE   B H    1 
ATOM   6031 H HA   . ILE   B 1 137 ? 35.771 -35.204 -3.876  1.00 18.84 ?  137 ILE   B HA   1 
ATOM   6032 H HB   . ILE   B 1 137 ? 35.059 -37.164 -1.979  1.00 20.86 ?  137 ILE   B HB   1 
ATOM   6033 H HG12 . ILE   B 1 137 ? 36.090 -37.552 -4.581  1.00 23.95 ?  137 ILE   B HG12 1 
ATOM   6034 H HG13 . ILE   B 1 137 ? 36.979 -37.626 -3.270  1.00 23.95 ?  137 ILE   B HG13 1 
ATOM   6035 H HG21 . ILE   B 1 137 ? 33.487 -37.978 -3.599  1.00 21.48 ?  137 ILE   B HG21 1 
ATOM   6036 H HG22 . ILE   B 1 137 ? 33.048 -36.629 -2.899  1.00 21.48 ?  137 ILE   B HG22 1 
ATOM   6037 H HG23 . ILE   B 1 137 ? 33.667 -36.599 -4.362  1.00 21.48 ?  137 ILE   B HG23 1 
ATOM   6038 H HD11 . ILE   B 1 137 ? 36.578 -39.765 -3.827  1.00 27.08 ?  137 ILE   B HD11 1 
ATOM   6039 H HD12 . ILE   B 1 137 ? 35.615 -39.484 -2.595  1.00 27.08 ?  137 ILE   B HD12 1 
ATOM   6040 H HD13 . ILE   B 1 137 ? 35.034 -39.487 -4.074  1.00 27.08 ?  137 ILE   B HD13 1 
ATOM   6041 N N    . HIS   B 1 138 ? 34.348 -34.299 -1.167  1.00 15.12 ?  138 HIS   B N    1 
ATOM   6042 C CA   . HIS   B 1 138 ? 33.395 -33.331 -0.638  1.00 15.36 ?  138 HIS   B CA   1 
ATOM   6043 C C    . HIS   B 1 138 ? 33.820 -31.904 -0.953  1.00 14.60 ?  138 HIS   B C    1 
ATOM   6044 O O    . HIS   B 1 138 ? 32.978 -31.057 -1.264  1.00 15.12 ?  138 HIS   B O    1 
ATOM   6045 C CB   . HIS   B 1 138 ? 33.262 -33.515 0.864   1.00 16.63 ?  138 HIS   B CB   1 
ATOM   6046 C CG   . HIS   B 1 138 ? 32.319 -32.544 1.493   1.00 17.17 ?  138 HIS   B CG   1 
ATOM   6047 N ND1  . HIS   B 1 138 ? 30.979 -32.488 1.168   1.00 18.40 ?  138 HIS   B ND1  1 
ATOM   6048 C CD2  . HIS   B 1 138 ? 32.527 -31.564 2.403   1.00 17.74 ?  138 HIS   B CD2  1 
ATOM   6049 C CE1  . HIS   B 1 138 ? 30.401 -31.524 1.862   1.00 18.51 ?  138 HIS   B CE1  1 
ATOM   6050 N NE2  . HIS   B 1 138 ? 31.317 -30.953 2.624   1.00 18.07 ?  138 HIS   B NE2  1 
ATOM   6051 H H    . HIS   B 1 138 ? 34.785 -34.738 -0.575  1.00 18.12 ?  138 HIS   B H    1 
ATOM   6052 H HA   . HIS   B 1 138 ? 32.525 -33.490 -1.043  1.00 18.41 ?  138 HIS   B HA   1 
ATOM   6053 H HB2  . HIS   B 1 138 ? 32.930 -34.406 1.044   1.00 19.93 ?  138 HIS   B HB2  1 
ATOM   6054 H HB3  . HIS   B 1 138 ? 34.131 -33.391 1.272   1.00 19.93 ?  138 HIS   B HB3  1 
ATOM   6055 H HD1  . HIS   B 1 138 ? 30.585 -33.005 0.602   1.00 22.06 ?  138 HIS   B HD1  1 
ATOM   6056 H HD2  . HIS   B 1 138 ? 33.329 -31.347 2.814   1.00 21.27 ?  138 HIS   B HD2  1 
ATOM   6057 H HE1  . HIS   B 1 138 ? 29.495 -31.302 1.826   1.00 22.18 ?  138 HIS   B HE1  1 
ATOM   6058 N N    . SER   B 1 139 ? 35.115 -31.607 -0.869  1.00 14.38 ?  139 SER   B N    1 
ATOM   6059 C CA   . SER   B 1 139 ? 35.557 -30.257 -1.185  1.00 13.67 ?  139 SER   B CA   1 
ATOM   6060 C C    . SER   B 1 139 ? 35.225 -29.903 -2.625  1.00 12.69 ?  139 SER   B C    1 
ATOM   6061 O O    . SER   B 1 139 ? 34.786 -28.786 -2.907  1.00 12.97 ?  139 SER   B O    1 
ATOM   6062 C CB   . SER   B 1 139 ? 37.050 -30.125 -0.919  1.00 13.95 ?  139 SER   B CB   1 
ATOM   6063 O OG   . SER   B 1 139 ? 37.470 -28.790 -1.188  1.00 14.16 ?  139 SER   B OG   1 
ATOM   6064 H H    . SER   B 1 139 ? 35.730 -32.153 -0.640  1.00 17.24 ?  139 SER   B H    1 
ATOM   6065 H HA   . SER   B 1 139 ? 35.091 -29.631 -0.615  1.00 16.38 ?  139 SER   B HA   1 
ATOM   6066 H HB2  . SER   B 1 139 ? 37.227 -30.343 0.011   1.00 16.72 ?  139 SER   B HB2  1 
ATOM   6067 H HB3  . SER   B 1 139 ? 37.536 -30.729 -1.502  1.00 16.72 ?  139 SER   B HB3  1 
ATOM   6068 H HG   . SER   B 1 139 ? 38.295 -28.709 -1.024  1.00 16.96 ?  139 SER   B HG   1 
ATOM   6069 N N    . LEU   B 1 140 ? 35.413 -30.844 -3.548  1.00 12.59 ?  140 LEU   B N    1 
ATOM   6070 C CA   . LEU   B 1 140 ? 35.054 -30.594 -4.937  1.00 12.88 ?  140 LEU   B CA   1 
ATOM   6071 C C    . LEU   B 1 140 ? 33.551 -30.368 -5.078  1.00 12.95 ?  140 LEU   B C    1 
ATOM   6072 O O    . LEU   B 1 140 ? 33.116 -29.484 -5.823  1.00 12.99 ?  140 LEU   B O    1 
ATOM   6073 C CB   . LEU   B 1 140 ? 35.528 -31.760 -5.806  1.00 13.21 ?  140 LEU   B CB   1 
ATOM   6074 C CG   . LEU   B 1 140 ? 35.184 -31.649 -7.286  1.00 13.42 ?  140 LEU   B CG   1 
ATOM   6075 C CD1  . LEU   B 1 140 ? 35.758 -30.373 -7.884  1.00 14.38 ?  140 LEU   B CD1  1 
ATOM   6076 C CD2  . LEU   B 1 140 ? 35.650 -32.872 -8.054  1.00 14.43 ?  140 LEU   B CD2  1 
ATOM   6077 H H    . LEU   B 1 140 ? 35.737 -31.626 -3.400  1.00 15.09 ?  140 LEU   B H    1 
ATOM   6078 H HA   . LEU   B 1 140 ? 35.509 -29.793 -5.240  1.00 15.43 ?  140 LEU   B HA   1 
ATOM   6079 H HB2  . LEU   B 1 140 ? 36.496 -31.824 -5.739  1.00 15.82 ?  140 LEU   B HB2  1 
ATOM   6080 H HB3  . LEU   B 1 140 ? 35.126 -32.578 -5.478  1.00 15.82 ?  140 LEU   B HB3  1 
ATOM   6081 H HG   . LEU   B 1 140 ? 34.220 -31.595 -7.372  1.00 16.08 ?  140 LEU   B HG   1 
ATOM   6082 H HD11 . LEU   B 1 140 ? 35.645 -30.399 -8.845  1.00 17.24 ?  140 LEU   B HD11 1 
ATOM   6083 H HD12 . LEU   B 1 140 ? 35.283 -29.608 -7.517  1.00 17.24 ?  140 LEU   B HD12 1 
ATOM   6084 H HD13 . LEU   B 1 140 ? 36.700 -30.315 -7.661  1.00 17.24 ?  140 LEU   B HD13 1 
ATOM   6085 H HD21 . LEU   B 1 140 ? 35.403 -32.760 -8.989  1.00 17.29 ?  140 LEU   B HD21 1 
ATOM   6086 H HD22 . LEU   B 1 140 ? 36.605 -32.953 -7.968  1.00 17.29 ?  140 LEU   B HD22 1 
ATOM   6087 H HD23 . LEU   B 1 140 ? 35.206 -33.652 -7.689  1.00 17.29 ?  140 LEU   B HD23 1 
ATOM   6088 N N    . ARG   B 1 141 ? 32.748 -31.156 -4.361  1.00 13.16 ?  141 ARG   B N    1 
ATOM   6089 C CA   . ARG   B 1 141 ? 31.299 -30.984 -4.353  1.00 14.46 ?  141 ARG   B CA   1 
ATOM   6090 C C    . ARG   B 1 141 ? 30.915 -29.574 -3.924  1.00 13.67 ?  141 ARG   B C    1 
ATOM   6091 O O    . ARG   B 1 141 ? 30.121 -28.894 -4.593  1.00 13.81 ?  141 ARG   B O    1 
ATOM   6092 C CB   . ARG   B 1 141 ? 30.721 -32.017 -3.377  1.00 16.34 ?  141 ARG   B CB   1 
ATOM   6093 C CG   . ARG   B 1 141 ? 29.264 -31.915 -3.038  1.00 18.90 ?  141 ARG   B CG   1 
ATOM   6094 C CD   . ARG   B 1 141 ? 28.461 -32.544 -4.102  1.00 21.28 ?  141 ARG   B CD   1 
ATOM   6095 N NE   . ARG   B 1 141 ? 28.210 -31.628 -5.202  1.00 21.73 ?  141 ARG   B NE   1 
ATOM   6096 C CZ   . ARG   B 1 141 ? 28.208 -31.970 -6.483  1.00 21.62 ?  141 ARG   B CZ   1 
ATOM   6097 N NH1  . ARG   B 1 141 ? 28.655 -33.150 -6.889  1.00 22.00 ?  141 ARG   B NH1  1 
ATOM   6098 N NH2  . ARG   B 1 141 ? 27.743 -31.104 -7.380  1.00 22.07 ?  141 ARG   B NH2  1 
ATOM   6099 H H    . ARG   B 1 141 ? 33.026 -31.801 -3.866  1.00 15.77 ?  141 ARG   B H    1 
ATOM   6100 H HA   . ARG   B 1 141 ? 30.942 -31.151 -5.238  1.00 17.33 ?  141 ARG   B HA   1 
ATOM   6101 H HB2  . ARG   B 1 141 ? 30.878 -32.902 -3.752  1.00 19.59 ?  141 ARG   B HB2  1 
ATOM   6102 H HB3  . ARG   B 1 141 ? 31.210 -31.947 -2.545  1.00 19.59 ?  141 ARG   B HB3  1 
ATOM   6103 H HG2  . ARG   B 1 141 ? 29.099 -32.382 -2.204  1.00 22.66 ?  141 ARG   B HG2  1 
ATOM   6104 H HG3  . ARG   B 1 141 ? 29.003 -30.984 -2.958  1.00 22.66 ?  141 ARG   B HG3  1 
ATOM   6105 H HD2  . ARG   B 1 141 ? 28.933 -33.326 -4.441  1.00 25.52 ?  141 ARG   B HD2  1 
ATOM   6106 H HD3  . ARG   B 1 141 ? 27.612 -32.821 -3.730  1.00 25.52 ?  141 ARG   B HD3  1 
ATOM   6107 H HE   . ARG   B 1 141 ? 28.015 -30.814 -5.003  1.00 26.06 ?  141 ARG   B HE   1 
ATOM   6108 H HH11 . ARG   B 1 141 ? 28.949 -33.722 -6.321  1.00 26.37 ?  141 ARG   B HH11 1 
ATOM   6109 H HH12 . ARG   B 1 141 ? 28.652 -33.338 -7.725  1.00 26.37 ?  141 ARG   B HH12 1 
ATOM   6110 H HH21 . ARG   B 1 141 ? 27.451 -30.333 -7.126  1.00 26.46 ?  141 ARG   B HH21 1 
ATOM   6111 H HH22 . ARG   B 1 141 ? 27.752 -31.303 -8.216  1.00 26.46 ?  141 ARG   B HH22 1 
ATOM   6112 N N    . VAL   B 1 142 ? 31.464 -29.126 -2.795  1.00 13.10 ?  142 VAL   B N    1 
ATOM   6113 C CA   . VAL   B 1 142 ? 31.136 -27.795 -2.302  1.00 13.27 ?  142 VAL   B CA   1 
ATOM   6114 C C    . VAL   B 1 142 ? 31.614 -26.735 -3.283  1.00 13.19 ?  142 VAL   B C    1 
ATOM   6115 O O    . VAL   B 1 142 ? 30.916 -25.751 -3.540  1.00 13.62 ?  142 VAL   B O    1 
ATOM   6116 C CB   . VAL   B 1 142 ? 31.682 -27.577 -0.879  1.00 13.92 ?  142 VAL   B CB   1 
ATOM   6117 C CG1  . VAL   B 1 142 ? 31.364 -26.158 -0.401  1.00 13.87 ?  142 VAL   B CG1  1 
ATOM   6118 C CG2  . VAL   B 1 142 ? 31.105 -28.602 0.082   1.00 14.73 ?  142 VAL   B CG2  1 
ATOM   6119 H H    . VAL   B 1 142 ? 32.018 -29.570 -2.303  1.00 15.69 ?  142 VAL   B H    1 
ATOM   6120 H HA   . VAL   B 1 142 ? 30.176 -27.722 -2.249  1.00 15.91 ?  142 VAL   B HA   1 
ATOM   6121 H HB   . VAL   B 1 142 ? 32.647 -27.681 -0.886  1.00 16.68 ?  142 VAL   B HB   1 
ATOM   6122 H HG11 . VAL   B 1 142 ? 31.543 -26.096 0.549   1.00 16.62 ?  142 VAL   B HG11 1 
ATOM   6123 H HG12 . VAL   B 1 142 ? 31.928 -25.527 -0.882  1.00 16.62 ?  142 VAL   B HG12 1 
ATOM   6124 H HG13 . VAL   B 1 142 ? 30.431 -25.967 -0.577  1.00 16.62 ?  142 VAL   B HG13 1 
ATOM   6125 H HG21 . VAL   B 1 142 ? 31.436 -28.415 0.974   1.00 17.66 ?  142 VAL   B HG21 1 
ATOM   6126 H HG22 . VAL   B 1 142 ? 30.140 -28.539 0.063   1.00 17.66 ?  142 VAL   B HG22 1 
ATOM   6127 H HG23 . VAL   B 1 142 ? 31.388 -29.486 -0.198  1.00 17.66 ?  142 VAL   B HG23 1 
ATOM   6128 N N    . CYS   B 1 143 ? 32.792 -26.938 -3.873  1.00 12.52 ?  143 CYS   B N    1 
ATOM   6129 C CA   . CYS   B 1 143 ? 33.288 -26.002 -4.877  1.00 12.40 ?  143 CYS   B CA   1 
ATOM   6130 C C    . CYS   B 1 143 ? 32.289 -25.853 -6.017  1.00 12.55 ?  143 CYS   B C    1 
ATOM   6131 O O    . CYS   B 1 143 ? 31.880 -24.742 -6.365  1.00 12.81 ?  143 CYS   B O    1 
ATOM   6132 C CB   . CYS   B 1 143 ? 34.641 -26.486 -5.406  1.00 12.89 ?  143 CYS   B CB   1 
ATOM   6133 S SG   . CYS   B 1 143 ? 35.397 -25.384 -6.609  1.00 13.30 ?  143 CYS   B SG   1 
ATOM   6134 H H    . CYS   B 1 143 ? 33.320 -27.595 -3.710  1.00 15.00 ?  143 CYS   B H    1 
ATOM   6135 H HA   . CYS   B 1 143 ? 33.420 -25.131 -4.473  1.00 14.85 ?  143 CYS   B HA   1 
ATOM   6136 H HB2  . CYS   B 1 143 ? 35.261 -26.578 -4.664  1.00 15.45 ?  143 CYS   B HB2  1 
ATOM   6137 H HB3  . CYS   B 1 143 ? 34.522 -27.347 -5.833  1.00 15.45 ?  143 CYS   B HB3  1 
ATOM   6138 H HG   . CYS   B 1 143 ? 36.470 -25.821 -6.929  1.00 15.94 ?  143 CYS   B HG   1 
ATOM   6139 N N    . VAL   B 1 144 ? 31.884 -26.971 -6.618  1.00 13.22 ?  144 VAL   B N    1 
ATOM   6140 C CA   . VAL   B 1 144 ? 30.981 -26.898 -7.765  1.00 14.16 ?  144 VAL   B CA   1 
ATOM   6141 C C    . VAL   B 1 144 ? 29.636 -26.293 -7.390  1.00 13.89 ?  144 VAL   B C    1 
ATOM   6142 O O    . VAL   B 1 144 ? 29.012 -25.592 -8.200  1.00 15.18 ?  144 VAL   B O    1 
ATOM   6143 C CB   . VAL   B 1 144 ? 30.835 -28.302 -8.367  1.00 17.11 ?  144 VAL   B CB   1 
ATOM   6144 C CG1  . VAL   B 1 144 ? 29.571 -28.423 -9.221  1.00 19.89 ?  144 VAL   B CG1  1 
ATOM   6145 C CG2  . VAL   B 1 144 ? 32.089 -28.686 -9.144  1.00 17.56 ?  144 VAL   B CG2  1 
ATOM   6146 H H    . VAL   B 1 144 ? 32.112 -27.769 -6.387  1.00 15.84 ?  144 VAL   B H    1 
ATOM   6147 H HA   . VAL   B 1 144 ? 31.378 -26.331 -8.441  1.00 16.97 ?  144 VAL   B HA   1 
ATOM   6148 H HB   . VAL   B 1 144 ? 30.748 -28.941 -7.642  1.00 20.50 ?  144 VAL   B HB   1 
ATOM   6149 H HG11 . VAL   B 1 144 ? 29.660 -29.197 -9.803  1.00 23.85 ?  144 VAL   B HG11 1 
ATOM   6150 H HG12 . VAL   B 1 144 ? 28.809 -28.538 -8.636  1.00 23.85 ?  144 VAL   B HG12 1 
ATOM   6151 H HG13 . VAL   B 1 144 ? 29.473 -27.621 -9.754  1.00 23.85 ?  144 VAL   B HG13 1 
ATOM   6152 H HG21 . VAL   B 1 144 ? 31.976 -29.577 -9.508  1.00 21.04 ?  144 VAL   B HG21 1 
ATOM   6153 H HG22 . VAL   B 1 144 ? 32.217 -28.048 -9.865  1.00 21.04 ?  144 VAL   B HG22 1 
ATOM   6154 H HG23 . VAL   B 1 144 ? 32.848 -28.665 -8.543  1.00 21.04 ?  144 VAL   B HG23 1 
ATOM   6155 N N    . ASP   B 1 145 ? 29.174 -26.536 -6.169  1.00 14.06 ?  145 ASP   B N    1 
ATOM   6156 C CA   . ASP   B 1 145 ? 27.868 -26.072 -5.729  1.00 14.52 ?  145 ASP   B CA   1 
ATOM   6157 C C    . ASP   B 1 145 ? 27.898 -24.654 -5.176  1.00 14.41 ?  145 ASP   B C    1 
ATOM   6158 O O    . ASP   B 1 145 ? 26.834 -24.115 -4.846  1.00 16.07 ?  145 ASP   B O    1 
ATOM   6159 C CB   . ASP   B 1 145 ? 27.300 -27.001 -4.647  1.00 16.11 ?  145 ASP   B CB   1 
ATOM   6160 C CG   . ASP   B 1 145 ? 26.920 -28.367 -5.168  1.00 17.64 ?  145 ASP   B CG   1 
ATOM   6161 O OD1  . ASP   B 1 145 ? 26.825 -28.555 -6.400  1.00 18.08 ?  145 ASP   B OD1  1 
ATOM   6162 O OD2  . ASP   B 1 145 ? 26.718 -29.260 -4.320  1.00 20.12 -1 145 ASP   B OD2  1 
ATOM   6163 H H    . ASP   B 1 145 ? 29.614 -26.963 -5.567  1.00 16.85 ?  145 ASP   B H    1 
ATOM   6164 H HA   . ASP   B 1 145 ? 27.265 -26.066 -6.486  1.00 17.40 ?  145 ASP   B HA   1 
ATOM   6165 H HB2  . ASP   B 1 145 ? 27.965 -27.123 -3.961  1.00 19.31 ?  145 ASP   B HB2  1 
ATOM   6166 H HB3  . ASP   B 1 145 ? 26.503 -26.585 -4.276  1.00 19.31 ?  145 ASP   B HB3  1 
ATOM   6167 N N    . THR   B 1 146 ? 29.072 -24.039 -5.060  1.00 12.79 ?  146 THR   B N    1 
ATOM   6168 C CA   . THR   B 1 146 ? 29.203 -22.718 -4.452  1.00 12.60 ?  146 THR   B CA   1 
ATOM   6169 C C    . THR   B 1 146 ? 29.844 -21.689 -5.366  1.00 12.39 ?  146 THR   B C    1 
ATOM   6170 O O    . THR   B 1 146 ? 29.391 -20.534 -5.410  1.00 12.94 ?  146 THR   B O    1 
ATOM   6171 C CB   . THR   B 1 146 ? 30.029 -22.830 -3.161  1.00 12.86 ?  146 THR   B CB   1 
ATOM   6172 O OG1  . THR   B 1 146 ? 29.455 -23.828 -2.308  1.00 13.06 ?  146 THR   B OG1  1 
ATOM   6173 C CG2  . THR   B 1 146 ? 30.097 -21.496 -2.430  1.00 13.20 ?  146 THR   B CG2  1 
ATOM   6174 H H    . THR   B 1 146 ? 29.824 -24.368 -5.330  1.00 15.32 ?  146 THR   B H    1 
ATOM   6175 H HA   . THR   B 1 146 ? 28.328 -22.393 -4.212  1.00 15.09 ?  146 THR   B HA   1 
ATOM   6176 H HB   . THR   B 1 146 ? 30.935 -23.088 -3.386  1.00 15.41 ?  146 THR   B HB   1 
ATOM   6177 H HG1  . THR   B 1 146 ? 29.493 -24.584 -2.690  1.00 15.64 ?  146 THR   B HG1  1 
ATOM   6178 H HG21 . THR   B 1 146 ? 30.454 -21.627 -1.539  1.00 15.81 ?  146 THR   B HG21 1 
ATOM   6179 H HG22 . THR   B 1 146 ? 30.677 -20.882 -2.912  1.00 15.81 ?  146 THR   B HG22 1 
ATOM   6180 H HG23 . THR   B 1 146 ? 29.212 -21.109 -2.364  1.00 15.81 ?  146 THR   B HG23 1 
ATOM   6181 N N    . VAL   B 1 147 ? 30.913 -22.062 -6.061  1.00 12.45 ?  147 VAL   B N    1 
ATOM   6182 C CA   . VAL   B 1 147 ? 31.639 -21.119 -6.894  1.00 12.23 ?  147 VAL   B CA   1 
ATOM   6183 C C    . VAL   B 1 147 ? 30.908 -20.979 -8.214  1.00 12.20 ?  147 VAL   B C    1 
ATOM   6184 O O    . VAL   B 1 147 ? 30.542 -21.979 -8.847  1.00 13.28 ?  147 VAL   B O    1 
ATOM   6185 C CB   . VAL   B 1 147 ? 33.089 -21.582 -7.101  1.00 12.35 ?  147 VAL   B CB   1 
ATOM   6186 C CG1  . VAL   B 1 147 ? 33.840 -20.551 -7.919  1.00 12.47 ?  147 VAL   B CG1  1 
ATOM   6187 C CG2  . VAL   B 1 147 ? 33.771 -21.796 -5.760  1.00 12.57 ?  147 VAL   B CG2  1 
ATOM   6188 H H    . VAL   B 1 147 ? 31.243 -22.863 -6.060  1.00 14.92 ?  147 VAL   B H    1 
ATOM   6189 H HA   . VAL   B 1 147 ? 31.657 -20.257 -6.457  1.00 14.65 ?  147 VAL   B HA   1 
ATOM   6190 H HB   . VAL   B 1 147 ? 33.096 -22.424 -7.588  1.00 14.80 ?  147 VAL   B HB   1 
ATOM   6191 H HG11 . VAL   B 1 147 ? 34.787 -20.765 -7.902  1.00 14.94 ?  147 VAL   B HG11 1 
ATOM   6192 H HG12 . VAL   B 1 147 ? 33.515 -20.568 -8.832  1.00 14.94 ?  147 VAL   B HG12 1 
ATOM   6193 H HG13 . VAL   B 1 147 ? 33.694 -19.675 -7.530  1.00 14.94 ?  147 VAL   B HG13 1 
ATOM   6194 H HG21 . VAL   B 1 147 ? 34.712 -21.995 -5.911  1.00 15.06 ?  147 VAL   B HG21 1 
ATOM   6195 H HG22 . VAL   B 1 147 ? 33.689 -20.988 -5.230  1.00 15.06 ?  147 VAL   B HG22 1 
ATOM   6196 H HG23 . VAL   B 1 147 ? 33.350 -22.539 -5.301  1.00 15.06 ?  147 VAL   B HG23 1 
ATOM   6197 N N    . ARG   B 1 148 ? 30.698 -19.732 -8.629  1.00 12.29 ?  148 ARG   B N    1 
ATOM   6198 C CA   . ARG   B 1 148 ? 30.071 -19.416 -9.899  1.00 12.85 ?  148 ARG   B CA   1 
ATOM   6199 C C    . ARG   B 1 148 ? 31.028 -18.746 -10.872 1.00 12.96 ?  148 ARG   B C    1 
ATOM   6200 O O    . ARG   B 1 148 ? 30.751 -18.734 -12.073 1.00 14.19 ?  148 ARG   B O    1 
ATOM   6201 C CB   . ARG   B 1 148 ? 28.838 -18.525 -9.674  1.00 13.43 ?  148 ARG   B CB   1 
ATOM   6202 C CG   . ARG   B 1 148 ? 27.753 -19.227 -8.864  1.00 14.04 ?  148 ARG   B CG   1 
ATOM   6203 C CD   . ARG   B 1 148 ? 26.552 -18.334 -8.579  1.00 14.47 ?  148 ARG   B CD   1 
ATOM   6204 N NE   . ARG   B 1 148 ? 26.939 -17.137 -7.841  1.00 14.15 ?  148 ARG   B NE   1 
ATOM   6205 C CZ   . ARG   B 1 148 ? 27.233 -17.110 -6.546  1.00 13.36 ?  148 ARG   B CZ   1 
ATOM   6206 N NH1  . ARG   B 1 148 ? 27.173 -18.199 -5.797  1.00 13.50 ?  148 ARG   B NH1  1 
ATOM   6207 N NH2  . ARG   B 1 148 ? 27.630 -15.964 -5.996  1.00 13.75 ?  148 ARG   B NH2  1 
ATOM   6208 H H    . ARG   B 1 148 ? 30.924 -19.036 -8.170  1.00 14.72 ?  148 ARG   B H    1 
ATOM   6209 H HA   . ARG   B 1 148 ? 29.764 -20.239 -10.303 1.00 15.40 ?  148 ARG   B HA   1 
ATOM   6210 H HB2  . ARG   B 1 148 ? 29.107 -17.725 -9.188  1.00 16.10 ?  148 ARG   B HB2  1 
ATOM   6211 H HB3  . ARG   B 1 148 ? 28.463 -18.279 -10.532 1.00 16.10 ?  148 ARG   B HB3  1 
ATOM   6212 H HG2  . ARG   B 1 148 ? 27.440 -19.998 -9.359  1.00 16.82 ?  148 ARG   B HG2  1 
ATOM   6213 H HG3  . ARG   B 1 148 ? 28.125 -19.507 -8.012  1.00 16.82 ?  148 ARG   B HG3  1 
ATOM   6214 H HD2  . ARG   B 1 148 ? 26.153 -18.054 -9.416  1.00 17.34 ?  148 ARG   B HD2  1 
ATOM   6215 H HD3  . ARG   B 1 148 ? 25.905 -18.824 -8.046  1.00 17.34 ?  148 ARG   B HD3  1 
ATOM   6216 H HE   . ARG   B 1 148 ? 26.974 -16.395 -8.269  1.00 16.96 ?  148 ARG   B HE   1 
ATOM   6217 H HH11 . ARG   B 1 148 ? 26.917 -18.948 -6.135  1.00 16.18 ?  148 ARG   B HH11 1 
ATOM   6218 H HH12 . ARG   B 1 148 ? 27.367 -18.158 -4.957  1.00 16.18 ?  148 ARG   B HH12 1 
ATOM   6219 H HH21 . ARG   B 1 148 ? 27.678 -15.252 -6.472  1.00 16.48 ?  148 ARG   B HH21 1 
ATOM   6220 H HH22 . ARG   B 1 148 ? 27.826 -15.932 -5.157  1.00 16.48 ?  148 ARG   B HH22 1 
ATOM   6221 N N    . THR   B 1 149 ? 32.133 -18.192 -10.384 1.00 12.66 ?  149 THR   B N    1 
ATOM   6222 C CA   . THR   B 1 149 ? 33.171 -17.632 -11.233 1.00 12.72 ?  149 THR   B CA   1 
ATOM   6223 C C    . THR   B 1 149 ? 34.056 -18.769 -11.738 1.00 12.42 ?  149 THR   B C    1 
ATOM   6224 O O    . THR   B 1 149 ? 33.864 -19.938 -11.395 1.00 12.76 ?  149 THR   B O    1 
ATOM   6225 C CB   . THR   B 1 149 ? 33.942 -16.578 -10.451 1.00 12.66 ?  149 THR   B CB   1 
ATOM   6226 O OG1  . THR   B 1 149 ? 34.393 -17.178 -9.237  1.00 12.70 ?  149 THR   B OG1  1 
ATOM   6227 C CG2  . THR   B 1 149 ? 33.045 -15.373 -10.153 1.00 13.76 ?  149 THR   B CG2  1 
ATOM   6228 H H    . THR   B 1 149 ? 32.299 -18.118 -9.544  1.00 15.17 ?  149 THR   B H    1 
ATOM   6229 H HA   . THR   B 1 149 ? 32.760 -17.202 -12.000 1.00 15.24 ?  149 THR   B HA   1 
ATOM   6230 H HB   . THR   B 1 149 ? 34.701 -16.278 -10.971 1.00 15.17 ?  149 THR   B HB   1 
ATOM   6231 H HG1  . THR   B 1 149 ? 34.810 -16.604 -8.777  1.00 15.21 ?  149 THR   B HG1  1 
ATOM   6232 H HG21 . THR   B 1 149 ? 33.549 -14.697 -9.673  1.00 16.49 ?  149 THR   B HG21 1 
ATOM   6233 H HG22 . THR   B 1 149 ? 32.717 -14.989 -10.983 1.00 16.49 ?  149 THR   B HG22 1 
ATOM   6234 H HG23 . THR   B 1 149 ? 32.289 -15.646 -9.612  1.00 16.49 ?  149 THR   B HG23 1 
ATOM   6235 N N    . ASN   B 1 150 ? 35.018 -18.447 -12.589 1.00 12.71 ?  150 ASN   B N    1 
ATOM   6236 C CA   . ASN   B 1 150 ? 35.786 -19.474 -13.282 1.00 13.16 ?  150 ASN   B CA   1 
ATOM   6237 C C    . ASN   B 1 150 ? 36.950 -19.922 -12.407 1.00 12.90 ?  150 ASN   B C    1 
ATOM   6238 O O    . ASN   B 1 150 ? 37.878 -19.151 -12.147 1.00 13.36 ?  150 ASN   B O    1 
ATOM   6239 C CB   . ASN   B 1 150 ? 36.261 -18.946 -14.625 1.00 15.19 ?  150 ASN   B CB   1 
ATOM   6240 C CG   . ASN   B 1 150 ? 35.117 -18.729 -15.573 1.00 17.43 ?  150 ASN   B CG   1 
ATOM   6241 O OD1  . ASN   B 1 150 ? 34.249 -19.583 -15.698 1.00 18.50 ?  150 ASN   B OD1  1 
ATOM   6242 N ND2  . ASN   B 1 150 ? 35.083 -17.575 -16.216 1.00 18.70 ?  150 ASN   B ND2  1 
ATOM   6243 H H    . ASN   B 1 150 ? 35.256 -17.640 -12.777 1.00 15.23 ?  150 ASN   B H    1 
ATOM   6244 H HA   . ASN   B 1 150 ? 35.208 -20.241 -13.447 1.00 15.77 ?  150 ASN   B HA   1 
ATOM   6245 H HB2  . ASN   B 1 150 ? 36.708 -18.094 -14.490 1.00 18.20 ?  150 ASN   B HB2  1 
ATOM   6246 H HB3  . ASN   B 1 150 ? 36.872 -19.585 -15.022 1.00 18.20 ?  150 ASN   B HB3  1 
ATOM   6247 H HD21 . ASN   B 1 150 ? 34.445 -17.409 -16.772 1.00 22.42 ?  150 ASN   B HD21 1 
ATOM   6248 H HD22 . ASN   B 1 150 ? 35.703 -16.991 -16.093 1.00 22.42 ?  150 ASN   B HD22 1 
ATOM   6249 N N    . VAL   B 1 151 ? 36.912 -21.172 -11.962 1.00 12.39 ?  151 VAL   B N    1 
ATOM   6250 C CA   . VAL   B 1 151 ? 37.932 -21.702 -11.073 1.00 12.43 ?  151 VAL   B CA   1 
ATOM   6251 C C    . VAL   B 1 151 ? 38.643 -22.868 -11.748 1.00 12.17 ?  151 VAL   B C    1 
ATOM   6252 O O    . VAL   B 1 151 ? 38.004 -23.799 -12.260 1.00 13.31 ?  151 VAL   B O    1 
ATOM   6253 C CB   . VAL   B 1 151 ? 37.373 -22.041 -9.676  1.00 13.79 ?  151 VAL   B CB   1 
ATOM   6254 C CG1  . VAL   B 1 151 ? 36.196 -23.023 -9.750  1.00 14.39 ?  151 VAL   B CG1  1 
ATOM   6255 C CG2  . VAL   B 1 151 ? 38.490 -22.548 -8.772  1.00 14.26 ?  151 VAL   B CG2  1 
ATOM   6256 H H    . VAL   B 1 151 ? 36.292 -21.741 -12.163 1.00 14.84 ?  151 VAL   B H    1 
ATOM   6257 H HA   . VAL   B 1 151 ? 38.598 -21.005 -10.943 1.00 14.89 ?  151 VAL   B HA   1 
ATOM   6258 H HB   . VAL   B 1 151 ? 37.040 -21.218 -9.278  1.00 16.53 ?  151 VAL   B HB   1 
ATOM   6259 H HG11 . VAL   B 1 151 ? 35.890 -23.219 -8.849  1.00 17.25 ?  151 VAL   B HG11 1 
ATOM   6260 H HG12 . VAL   B 1 151 ? 35.476 -22.621 -10.261 1.00 17.25 ?  151 VAL   B HG12 1 
ATOM   6261 H HG13 . VAL   B 1 151 ? 36.491 -23.841 -10.181 1.00 17.25 ?  151 VAL   B HG13 1 
ATOM   6262 H HG21 . VAL   B 1 151 ? 38.153 -22.611 -7.864  1.00 17.09 ?  151 VAL   B HG21 1 
ATOM   6263 H HG22 . VAL   B 1 151 ? 38.775 -23.421 -9.080  1.00 17.09 ?  151 VAL   B HG22 1 
ATOM   6264 H HG23 . VAL   B 1 151 ? 39.233 -21.925 -8.803  1.00 17.09 ?  151 VAL   B HG23 1 
ATOM   6265 N N    . TYR   B 1 152 ? 39.971 -22.782 -11.763 1.00 11.79 ?  152 TYR   B N    1 
ATOM   6266 C CA   . TYR   B 1 152 ? 40.877 -23.759 -12.349 1.00 11.94 ?  152 TYR   B CA   1 
ATOM   6267 C C    . TYR   B 1 152 ? 41.596 -24.434 -11.186 1.00 11.36 ?  152 TYR   B C    1 
ATOM   6268 O O    . TYR   B 1 152 ? 42.432 -23.814 -10.520 1.00 11.88 ?  152 TYR   B O    1 
ATOM   6269 C CB   . TYR   B 1 152 ? 41.848 -23.041 -13.291 1.00 12.53 ?  152 TYR   B CB   1 
ATOM   6270 C CG   . TYR   B 1 152 ? 41.165 -22.583 -14.559 1.00 13.11 ?  152 TYR   B CG   1 
ATOM   6271 C CD1  . TYR   B 1 152 ? 40.485 -21.372 -14.619 1.00 13.54 ?  152 TYR   B CD1  1 
ATOM   6272 C CD2  . TYR   B 1 152 ? 41.179 -23.383 -15.686 1.00 14.16 ?  152 TYR   B CD2  1 
ATOM   6273 C CE1  . TYR   B 1 152 ? 39.845 -20.975 -15.771 1.00 14.65 ?  152 TYR   B CE1  1 
ATOM   6274 C CE2  . TYR   B 1 152 ? 40.546 -23.000 -16.841 1.00 15.09 ?  152 TYR   B CE2  1 
ATOM   6275 C CZ   . TYR   B 1 152 ? 39.878 -21.793 -16.884 1.00 15.14 ?  152 TYR   B CZ   1 
ATOM   6276 O OH   . TYR   B 1 152 ? 39.248 -21.427 -18.047 1.00 17.85 ?  152 TYR   B OH   1 
ATOM   6277 H H    . TYR   B 1 152 ? 40.400 -22.115 -11.414 1.00 14.12 ?  152 TYR   B H    1 
ATOM   6278 H HA   . TYR   B 1 152 ? 40.374 -24.422 -12.849 1.00 14.30 ?  152 TYR   B HA   1 
ATOM   6279 H HB2  . TYR   B 1 152 ? 42.207 -22.260 -12.835 1.00 15.01 ?  152 TYR   B HB2  1 
ATOM   6280 H HB3  . TYR   B 1 152 ? 42.568 -23.645 -13.527 1.00 15.01 ?  152 TYR   B HB3  1 
ATOM   6281 H HD1  . TYR   B 1 152 ? 40.457 -20.826 -13.863 1.00 16.22 ?  152 TYR   B HD1  1 
ATOM   6282 H HD2  . TYR   B 1 152 ? 41.630 -24.201 -15.656 1.00 16.96 ?  152 TYR   B HD2  1 
ATOM   6283 H HE1  . TYR   B 1 152 ? 39.392 -20.164 -15.801 1.00 17.55 ?  152 TYR   B HE1  1 
ATOM   6284 H HE2  . TYR   B 1 152 ? 40.572 -23.549 -17.590 1.00 18.09 ?  152 TYR   B HE2  1 
ATOM   6285 H HH   . TYR   B 1 152 ? 38.880 -20.679 -17.949 1.00 21.40 ?  152 TYR   B HH   1 
ATOM   6286 N N    . LEU   B 1 153 ? 41.236 -25.694 -10.927 1.00 11.74 ?  153 LEU   B N    1 
ATOM   6287 C CA   . LEU   B 1 153 ? 41.737 -26.440 -9.784  1.00 11.43 ?  153 LEU   B CA   1 
ATOM   6288 C C    . LEU   B 1 153 ? 42.974 -27.237 -10.172 1.00 11.59 ?  153 LEU   B C    1 
ATOM   6289 O O    . LEU   B 1 153 ? 42.967 -27.963 -11.168 1.00 12.59 ?  153 LEU   B O    1 
ATOM   6290 C CB   . LEU   B 1 153 ? 40.654 -27.391 -9.271  1.00 11.90 ?  153 LEU   B CB   1 
ATOM   6291 C CG   . LEU   B 1 153 ? 39.401 -26.730 -8.701  1.00 12.52 ?  153 LEU   B CG   1 
ATOM   6292 C CD1  . LEU   B 1 153 ? 38.309 -27.775 -8.553  1.00 13.48 ?  153 LEU   B CD1  1 
ATOM   6293 C CD2  . LEU   B 1 153 ? 39.692 -26.074 -7.361  1.00 13.02 ?  153 LEU   B CD2  1 
ATOM   6294 H H    . LEU   B 1 153 ? 40.679 -26.144 -11.412 1.00 14.07 ?  153 LEU   B H    1 
ATOM   6295 H HA   . LEU   B 1 153 ? 41.963 -25.822 -9.074  1.00 13.69 ?  153 LEU   B HA   1 
ATOM   6296 H HB2  . LEU   B 1 153 ? 40.367 -27.960 -9.998  1.00 14.26 ?  153 LEU   B HB2  1 
ATOM   6297 H HB3  . LEU   B 1 153 ? 41.031 -27.935 -8.560  1.00 14.26 ?  153 LEU   B HB3  1 
ATOM   6298 H HG   . LEU   B 1 153 ? 39.084 -26.037 -9.311  1.00 15.00 ?  153 LEU   B HG   1 
ATOM   6299 H HD11 . LEU   B 1 153 ? 37.506 -27.345 -8.216  1.00 16.16 ?  153 LEU   B HD11 1 
ATOM   6300 H HD12 . LEU   B 1 153 ? 38.138 -28.167 -9.418  1.00 16.16 ?  153 LEU   B HD12 1 
ATOM   6301 H HD13 . LEU   B 1 153 ? 38.612 -28.448 -7.928  1.00 16.16 ?  153 LEU   B HD13 1 
ATOM   6302 H HD21 . LEU   B 1 153 ? 38.877 -25.692 -7.003  1.00 15.60 ?  153 LEU   B HD21 1 
ATOM   6303 H HD22 . LEU   B 1 153 ? 40.039 -26.746 -6.753  1.00 15.60 ?  153 LEU   B HD22 1 
ATOM   6304 H HD23 . LEU   B 1 153 ? 40.356 -25.374 -7.489  1.00 15.60 ?  153 LEU   B HD23 1 
ATOM   6305 N N    . ALA   B 1 154 ? 44.017 -27.126 -9.363  1.00 11.79 ?  154 ALA   B N    1 
ATOM   6306 C CA   . ALA   B 1 154 ? 45.244 -27.888 -9.548  1.00 12.82 ?  154 ALA   B CA   1 
ATOM   6307 C C    . ALA   B 1 154 ? 45.308 -28.966 -8.475  1.00 13.11 ?  154 ALA   B C    1 
ATOM   6308 O O    . ALA   B 1 154 ? 45.231 -28.670 -7.277  1.00 14.44 ?  154 ALA   B O    1 
ATOM   6309 C CB   . ALA   B 1 154 ? 46.469 -26.980 -9.484  1.00 13.98 ?  154 ALA   B CB   1 
ATOM   6310 H H    . ALA   B 1 154 ? 44.033 -26.601 -8.678  1.00 14.13 ?  154 ALA   B H    1 
ATOM   6311 H HA   . ALA   B 1 154 ? 45.228 -28.319 -10.413 1.00 15.35 ?  154 ALA   B HA   1 
ATOM   6312 H HB1  . ALA   B 1 154 ? 47.266 -27.513 -9.609  1.00 16.75 ?  154 ALA   B HB1  1 
ATOM   6313 H HB2  . ALA   B 1 154 ? 46.402 -26.310 -10.185 1.00 16.75 ?  154 ALA   B HB2  1 
ATOM   6314 H HB3  . ALA   B 1 154 ? 46.494 -26.542 -8.616  1.00 16.75 ?  154 ALA   B HB3  1 
ATOM   6315 N N    . VAL   B 1 155 ? 45.430 -30.211 -8.911  1.00 12.34 ?  155 VAL   B N    1 
ATOM   6316 C CA   . VAL   B 1 155 ? 45.535 -31.360 -8.022  1.00 12.51 ?  155 VAL   B CA   1 
ATOM   6317 C C    . VAL   B 1 155 ? 46.877 -32.033 -8.291  1.00 12.53 ?  155 VAL   B C    1 
ATOM   6318 O O    . VAL   B 1 155 ? 47.120 -32.525 -9.400  1.00 13.99 ?  155 VAL   B O    1 
ATOM   6319 C CB   . VAL   B 1 155 ? 44.378 -32.351 -8.228  1.00 14.20 ?  155 VAL   B CB   1 
ATOM   6320 C CG1  . VAL   B 1 155 ? 44.547 -33.558 -7.316  1.00 14.27 ?  155 VAL   B CG1  1 
ATOM   6321 C CG2  . VAL   B 1 155 ? 43.031 -31.665 -7.982  1.00 15.50 ?  155 VAL   B CG2  1 
ATOM   6322 H H    . VAL   B 1 155 ? 45.457 -30.425 -9.745  1.00 14.79 ?  155 VAL   B H    1 
ATOM   6323 H HA   . VAL   B 1 155 ? 45.517 -31.066 -7.101  1.00 14.99 ?  155 VAL   B HA   1 
ATOM   6324 H HB   . VAL   B 1 155 ? 44.387 -32.668 -9.147  1.00 17.02 ?  155 VAL   B HB   1 
ATOM   6325 H HG11 . VAL   B 1 155 ? 43.717 -34.064 -7.300  1.00 17.11 ?  155 VAL   B HG11 1 
ATOM   6326 H HG12 . VAL   B 1 155 ? 45.264 -34.119 -7.655  1.00 17.11 ?  155 VAL   B HG12 1 
ATOM   6327 H HG13 . VAL   B 1 155 ? 44.761 -33.252 -6.421  1.00 17.11 ?  155 VAL   B HG13 1 
ATOM   6328 H HG21 . VAL   B 1 155 ? 42.323 -32.322 -8.071  1.00 18.57 ?  155 VAL   B HG21 1 
ATOM   6329 H HG22 . VAL   B 1 155 ? 43.030 -31.295 -7.086  1.00 18.57 ?  155 VAL   B HG22 1 
ATOM   6330 H HG23 . VAL   B 1 155 ? 42.915 -30.959 -8.635  1.00 18.57 ?  155 VAL   B HG23 1 
ATOM   6331 N N    . PHE   B 1 156 ? 47.737 -32.065 -7.274  1.00 13.15 ?  156 PHE   B N    1 
ATOM   6332 C CA   . PHE   B 1 156 ? 49.116 -32.523 -7.462  1.00 14.41 ?  156 PHE   B CA   1 
ATOM   6333 C C    . PHE   B 1 156 ? 49.221 -34.023 -7.745  1.00 14.96 ?  156 PHE   B C    1 
ATOM   6334 O O    . PHE   B 1 156 ? 49.954 -34.444 -8.650  1.00 16.61 ?  156 PHE   B O    1 
ATOM   6335 C CB   . PHE   B 1 156 ? 49.937 -32.157 -6.229  1.00 14.61 ?  156 PHE   B CB   1 
ATOM   6336 C CG   . PHE   B 1 156 ? 51.358 -32.616 -6.288  1.00 15.36 ?  156 PHE   B CG   1 
ATOM   6337 C CD1  . PHE   B 1 156 ? 52.247 -32.055 -7.183  1.00 17.12 ?  156 PHE   B CD1  1 
ATOM   6338 C CD2  . PHE   B 1 156 ? 51.808 -33.598 -5.432  1.00 15.42 ?  156 PHE   B CD2  1 
ATOM   6339 C CE1  . PHE   B 1 156 ? 53.571 -32.467 -7.228  1.00 18.11 ?  156 PHE   B CE1  1 
ATOM   6340 C CE2  . PHE   B 1 156 ? 53.127 -34.018 -5.471  1.00 16.94 ?  156 PHE   B CE2  1 
ATOM   6341 C CZ   . PHE   B 1 156 ? 54.001 -33.455 -6.375  1.00 17.79 ?  156 PHE   B CZ   1 
ATOM   6342 H H    . PHE   B 1 156 ? 47.550 -31.818 -6.469  1.00 15.76 ?  156 PHE   B H    1 
ATOM   6343 H HA   . PHE   B 1 156 ? 49.496 -32.054 -8.216  1.00 17.27 ?  156 PHE   B HA   1 
ATOM   6344 H HB2  . PHE   B 1 156 ? 49.945 -31.191 -6.136  1.00 17.51 ?  156 PHE   B HB2  1 
ATOM   6345 H HB3  . PHE   B 1 156 ? 49.530 -32.559 -5.447  1.00 17.51 ?  156 PHE   B HB3  1 
ATOM   6346 H HD1  . PHE   B 1 156 ? 51.959 -31.383 -7.763  1.00 20.52 ?  156 PHE   B HD1  1 
ATOM   6347 H HD2  . PHE   B 1 156 ? 51.216 -33.983 -4.825  1.00 18.48 ?  156 PHE   B HD2  1 
ATOM   6348 H HE1  . PHE   B 1 156 ? 54.161 -32.083 -7.839  1.00 21.71 ?  156 PHE   B HE1  1 
ATOM   6349 H HE2  . PHE   B 1 156 ? 53.417 -34.688 -4.895  1.00 20.30 ?  156 PHE   B HE2  1 
ATOM   6350 H HZ   . PHE   B 1 156 ? 54.887 -33.738 -6.403  1.00 21.33 ?  156 PHE   B HZ   1 
ATOM   6351 N N    . ASP   B 1 157 ? 48.561 -34.848 -6.945  1.00 15.11 ?  157 ASP   B N    1 
ATOM   6352 C CA   . ASP   B 1 157 ? 48.704 -36.295 -7.049  1.00 16.35 ?  157 ASP   B CA   1 
ATOM   6353 C C    . ASP   B 1 157 ? 47.786 -36.829 -8.142  1.00 16.66 ?  157 ASP   B C    1 
ATOM   6354 O O    . ASP   B 1 157 ? 46.559 -36.723 -8.030  1.00 15.98 ?  157 ASP   B O    1 
ATOM   6355 C CB   . ASP   B 1 157 ? 48.337 -36.907 -5.706  1.00 17.89 ?  157 ASP   B CB   1 
ATOM   6356 C CG   . ASP   B 1 157 ? 48.468 -38.419 -5.692  1.00 19.97 ?  157 ASP   B CG   1 
ATOM   6357 O OD1  . ASP   B 1 157 ? 48.816 -39.023 -6.734  1.00 20.43 ?  157 ASP   B OD1  1 
ATOM   6358 O OD2  . ASP   B 1 157 ? 48.236 -39.008 -4.620  1.00 21.95 -1 157 ASP   B OD2  1 
ATOM   6359 H H    . ASP   B 1 157 ? 48.026 -34.598 -6.324  1.00 18.11 ?  157 ASP   B H    1 
ATOM   6360 H HA   . ASP   B 1 157 ? 49.627 -36.531 -7.264  1.00 19.59 ?  157 ASP   B HA   1 
ATOM   6361 H HB2  . ASP   B 1 157 ? 48.920 -36.539 -5.025  1.00 21.45 ?  157 ASP   B HB2  1 
ATOM   6362 H HB3  . ASP   B 1 157 ? 47.414 -36.685 -5.506  1.00 21.45 ?  157 ASP   B HB3  1 
ATOM   6363 N N    . LYS   B 1 158 ? 48.381 -37.438 -9.176  1.00 17.82 ?  158 LYS   B N    1 
ATOM   6364 C CA   . LYS   B 1 158 ? 47.605 -38.053 -10.256 1.00 18.60 ?  158 LYS   B CA   1 
ATOM   6365 C C    . LYS   B 1 158 ? 46.548 -39.019 -9.726  1.00 18.15 ?  158 LYS   B C    1 
ATOM   6366 O O    . LYS   B 1 158 ? 45.449 -39.116 -10.283 1.00 18.44 ?  158 LYS   B O    1 
ATOM   6367 C CB   . LYS   B 1 158 ? 48.546 -38.773 -11.230 1.00 20.74 ?  158 LYS   B CB   1 
ATOM   6368 C CG   . LYS   B 1 158 ? 47.849 -39.667 -12.249 1.00 22.95 ?  158 LYS   B CG   1 
ATOM   6369 C CD   . LYS   B 1 158 ? 47.014 -38.881 -13.236 1.00 25.27 ?  158 LYS   B CD   1 
ATOM   6370 C CE   . LYS   B 1 158 ? 46.431 -39.800 -14.298 1.00 27.31 ?  158 LYS   B CE   1 
ATOM   6371 N NZ   . LYS   B 1 158 ? 45.361 -39.131 -15.091 1.00 26.82 ?  158 LYS   B NZ   1 
ATOM   6372 H H    . LYS   B 1 158 ? 49.238 -37.508 -9.280  1.00 21.36 ?  158 LYS   B H    1 
ATOM   6373 H HA   . LYS   B 1 158 ? 47.151 -37.352 -10.755 1.00 22.29 ?  158 LYS   B HA   1 
ATOM   6374 H HB2  . LYS   B 1 158 ? 49.050 -38.107 -11.730 1.00 24.87 ?  158 LYS   B HB2  1 
ATOM   6375 H HB3  . LYS   B 1 158 ? 49.156 -39.327 -10.723 1.00 24.87 ?  158 LYS   B HB3  1 
ATOM   6376 H HG2  . LYS   B 1 158 ? 48.525 -40.146 -12.753 1.00 27.52 ?  158 LYS   B HG2  1 
ATOM   6377 H HG3  . LYS   B 1 158 ? 47.273 -40.306 -11.798 1.00 27.52 ?  158 LYS   B HG3  1 
ATOM   6378 H HD2  . LYS   B 1 158 ? 46.282 -38.448 -12.771 1.00 30.30 ?  158 LYS   B HD2  1 
ATOM   6379 H HD3  . LYS   B 1 158 ? 47.571 -38.221 -13.678 1.00 30.30 ?  158 LYS   B HD3  1 
ATOM   6380 H HE2  . LYS   B 1 158 ? 47.132 -40.070 -14.909 1.00 32.74 ?  158 LYS   B HE2  1 
ATOM   6381 H HE3  . LYS   B 1 158 ? 46.043 -40.580 -13.869 1.00 32.74 ?  158 LYS   B HE3  1 
ATOM   6382 H HZ1  . LYS   B 1 158 ? 45.037 -39.691 -15.702 1.00 32.17 ?  158 LYS   B HZ1  1 
ATOM   6383 H HZ2  . LYS   B 1 158 ? 44.698 -38.875 -14.554 1.00 32.17 ?  158 LYS   B HZ2  1 
ATOM   6384 H HZ3  . LYS   B 1 158 ? 45.691 -38.413 -15.502 1.00 32.17 ?  158 LYS   B HZ3  1 
ATOM   6385 N N    . ASN   B 1 159 ? 46.870 -39.773 -8.675  1.00 18.41 ?  159 ASN   B N    1 
ATOM   6386 C CA   . ASN   B 1 159 ? 45.918 -40.759 -8.177  1.00 19.25 ?  159 ASN   B CA   1 
ATOM   6387 C C    . ASN   B 1 159 ? 44.718 -40.094 -7.506  1.00 18.06 ?  159 ASN   B C    1 
ATOM   6388 O O    . ASN   B 1 159 ? 43.590 -40.588 -7.631  1.00 18.10 ?  159 ASN   B O    1 
ATOM   6389 C CB   . ASN   B 1 159 ? 46.624 -41.735 -7.246  1.00 20.92 ?  159 ASN   B CB   1 
ATOM   6390 C CG   . ASN   B 1 159 ? 47.660 -42.573 -7.972  1.00 23.20 ?  159 ASN   B CG   1 
ATOM   6391 O OD1  . ASN   B 1 159 ? 47.409 -43.081 -9.071  1.00 24.56 ?  159 ASN   B OD1  1 
ATOM   6392 N ND2  . ASN   B 1 159 ? 48.832 -42.723 -7.365  1.00 23.91 ?  159 ASN   B ND2  1 
ATOM   6393 H H    . ASN   B 1 159 ? 47.612 -39.720 -8.244  1.00 22.07 ?  159 ASN   B H    1 
ATOM   6394 H HA   . ASN   B 1 159 ? 45.589 -41.263 -8.937  1.00 23.07 ?  159 ASN   B HA   1 
ATOM   6395 H HB2  . ASN   B 1 159 ? 47.076 -41.242 -6.548  1.00 25.08 ?  159 ASN   B HB2  1 
ATOM   6396 H HB3  . ASN   B 1 159 ? 45.969 -42.338 -6.868  1.00 25.08 ?  159 ASN   B HB3  1 
ATOM   6397 H HD21 . ASN   B 1 159 ? 49.455 -43.191 -7.737  1.00 28.67 ?  159 ASN   B HD21 1 
ATOM   6398 H HD22 . ASN   B 1 159 ? 48.966 -42.369 -6.596  1.00 28.67 ?  159 ASN   B HD22 1 
ATOM   6399 N N    . LEU   B 1 160 ? 44.921 -38.961 -6.823  1.00 17.22 ?  160 LEU   B N    1 
ATOM   6400 C CA   . LEU   B 1 160 ? 43.786 -38.224 -6.283  1.00 16.32 ?  160 LEU   B CA   1 
ATOM   6401 C C    . LEU   B 1 160 ? 43.003 -37.557 -7.399  1.00 15.39 ?  160 LEU   B C    1 
ATOM   6402 O O    . LEU   B 1 160 ? 41.767 -37.564 -7.389  1.00 15.11 ?  160 LEU   B O    1 
ATOM   6403 C CB   . LEU   B 1 160 ? 44.246 -37.189 -5.257  1.00 15.99 ?  160 LEU   B CB   1 
ATOM   6404 C CG   . LEU   B 1 160 ? 43.120 -36.292 -4.722  1.00 15.75 ?  160 LEU   B CG   1 
ATOM   6405 C CD1  . LEU   B 1 160 ? 41.990 -37.125 -4.122  1.00 16.48 ?  160 LEU   B CD1  1 
ATOM   6406 C CD2  . LEU   B 1 160 ? 43.666 -35.300 -3.703  1.00 15.91 ?  160 LEU   B CD2  1 
ATOM   6407 H H    . LEU   B 1 160 ? 45.693 -38.603 -6.678  1.00 20.64 ?  160 LEU   B H    1 
ATOM   6408 H HA   . LEU   B 1 160 ? 43.197 -38.847 -5.841  1.00 19.57 ?  160 LEU   B HA   1 
ATOM   6409 H HB2  . LEU   B 1 160 ? 44.641 -37.657 -4.503  1.00 19.17 ?  160 LEU   B HB2  1 
ATOM   6410 H HB3  . LEU   B 1 160 ? 44.916 -36.616 -5.669  1.00 19.17 ?  160 LEU   B HB3  1 
ATOM   6411 H HG   . LEU   B 1 160 ? 42.754 -35.780 -5.457  1.00 18.87 ?  160 LEU   B HG   1 
ATOM   6412 H HD11 . LEU   B 1 160 ? 41.364 -36.533 -3.682  1.00 19.75 ?  160 LEU   B HD11 1 
ATOM   6413 H HD12 . LEU   B 1 160 ? 41.542 -37.611 -4.833  1.00 19.75 ?  160 LEU   B HD12 1 
ATOM   6414 H HD13 . LEU   B 1 160 ? 42.364 -37.750 -3.480  1.00 19.75 ?  160 LEU   B HD13 1 
ATOM   6415 H HD21 . LEU   B 1 160 ? 42.941 -34.729 -3.404  1.00 19.07 ?  160 LEU   B HD21 1 
ATOM   6416 H HD22 . LEU   B 1 160 ? 44.036 -35.788 -2.952  1.00 19.07 ?  160 LEU   B HD22 1 
ATOM   6417 H HD23 . LEU   B 1 160 ? 44.357 -34.763 -4.123  1.00 19.07 ?  160 LEU   B HD23 1 
ATOM   6418 N N    . TYR   B 1 161 ? 43.706 -36.982 -8.374  1.00 15.54 ?  161 TYR   B N    1 
ATOM   6419 C CA   . TYR   B 1 161 ? 43.039 -36.419 -9.540  1.00 15.46 ?  161 TYR   B CA   1 
ATOM   6420 C C    . TYR   B 1 161 ? 42.099 -37.442 -10.162 1.00 15.46 ?  161 TYR   B C    1 
ATOM   6421 O O    . TYR   B 1 161 ? 40.928 -37.147 -10.421 1.00 15.27 ?  161 TYR   B O    1 
ATOM   6422 C CB   . TYR   B 1 161 ? 44.089 -35.941 -10.547 1.00 15.89 ?  161 TYR   B CB   1 
ATOM   6423 C CG   . TYR   B 1 161 ? 43.518 -35.470 -11.860 1.00 16.43 ?  161 TYR   B CG   1 
ATOM   6424 C CD1  . TYR   B 1 161 ? 43.131 -34.147 -12.032 1.00 16.27 ?  161 TYR   B CD1  1 
ATOM   6425 C CD2  . TYR   B 1 161 ? 43.343 -36.350 -12.926 1.00 17.09 ?  161 TYR   B CD2  1 
ATOM   6426 C CE1  . TYR   B 1 161 ? 42.604 -33.714 -13.218 1.00 17.22 ?  161 TYR   B CE1  1 
ATOM   6427 C CE2  . TYR   B 1 161 ? 42.811 -35.922 -14.117 1.00 18.21 ?  161 TYR   B CE2  1 
ATOM   6428 C CZ   . TYR   B 1 161 ? 42.445 -34.602 -14.258 1.00 17.82 ?  161 TYR   B CZ   1 
ATOM   6429 O OH   . TYR   B 1 161 ? 41.911 -34.159 -15.439 1.00 19.62 ?  161 TYR   B OH   1 
ATOM   6430 H H    . TYR   B 1 161 ? 44.562 -36.908 -8.387  1.00 18.63 ?  161 TYR   B H    1 
ATOM   6431 H HA   . TYR   B 1 161 ? 42.512 -35.652 -9.270  1.00 18.53 ?  161 TYR   B HA   1 
ATOM   6432 H HB2  . TYR   B 1 161 ? 44.580 -35.198 -10.158 1.00 19.04 ?  161 TYR   B HB2  1 
ATOM   6433 H HB3  . TYR   B 1 161 ? 44.698 -36.670 -10.738 1.00 19.04 ?  161 TYR   B HB3  1 
ATOM   6434 H HD1  . TYR   B 1 161 ? 43.245 -33.537 -11.337 1.00 19.50 ?  161 TYR   B HD1  1 
ATOM   6435 H HD2  . TYR   B 1 161 ? 43.586 -37.240 -12.833 1.00 20.49 ?  161 TYR   B HD2  1 
ATOM   6436 H HE1  . TYR   B 1 161 ? 42.362 -32.818 -13.319 1.00 20.64 ?  161 TYR   B HE1  1 
ATOM   6437 H HE2  . TYR   B 1 161 ? 42.697 -36.514 -14.825 1.00 21.83 ?  161 TYR   B HE2  1 
ATOM   6438 H HH   . TYR   B 1 161 ? 41.868 -34.795 -15.988 1.00 23.52 ?  161 TYR   B HH   1 
ATOM   6439 N N    . ASP   B 1 162 ? 42.596 -38.662 -10.386 1.00 15.97 ?  162 ASP   B N    1 
ATOM   6440 C CA   . ASP   B 1 162 ? 41.767 -39.693 -11.005 1.00 16.24 ?  162 ASP   B CA   1 
ATOM   6441 C C    . ASP   B 1 162 ? 40.559 -40.027 -10.139 1.00 15.52 ?  162 ASP   B C    1 
ATOM   6442 O O    . ASP   B 1 162 ? 39.457 -40.244 -10.659 1.00 15.96 ?  162 ASP   B O    1 
ATOM   6443 C CB   . ASP   B 1 162 ? 42.593 -40.955 -11.263 1.00 17.98 ?  162 ASP   B CB   1 
ATOM   6444 C CG   . ASP   B 1 162 ? 43.597 -40.789 -12.391 1.00 19.11 ?  162 ASP   B CG   1 
ATOM   6445 O OD1  . ASP   B 1 162 ? 43.464 -39.839 -13.186 1.00 18.98 ?  162 ASP   B OD1  1 
ATOM   6446 O OD2  . ASP   B 1 162 ? 44.509 -41.634 -12.496 1.00 21.02 -1 162 ASP   B OD2  1 
ATOM   6447 H H    . ASP   B 1 162 ? 43.396 -38.914 -10.193 1.00 19.13 ?  162 ASP   B H    1 
ATOM   6448 H HA   . ASP   B 1 162 ? 41.440 -39.367 -11.856 1.00 19.46 ?  162 ASP   B HA   1 
ATOM   6449 H HB2  . ASP   B 1 162 ? 43.081 -41.182 -10.457 1.00 21.55 ?  162 ASP   B HB2  1 
ATOM   6450 H HB3  . ASP   B 1 162 ? 41.994 -41.678 -11.504 1.00 21.55 ?  162 ASP   B HB3  1 
ATOM   6451 N N    . LYS   B 1 163 ? 40.748 -40.101 -8.821  1.00 15.03 ?  163 LYS   B N    1 
ATOM   6452 C CA   . LYS   B 1 163 ? 39.622 -40.380 -7.934  1.00 15.75 ?  163 LYS   B CA   1 
ATOM   6453 C C    . LYS   B 1 163 ? 38.573 -39.275 -8.000  1.00 14.72 ?  163 LYS   B C    1 
ATOM   6454 O O    . LYS   B 1 163 ? 37.366 -39.551 -8.010  1.00 15.77 ?  163 LYS   B O    1 
ATOM   6455 C CB   . LYS   B 1 163 ? 40.104 -40.565 -6.498  1.00 19.50 ?  163 LYS   B CB   1 
ATOM   6456 C CG   . LYS   B 1 163 ? 38.996 -41.020 -5.568  1.00 25.99 ?  163 LYS   B CG   1 
ATOM   6457 C CD   . LYS   B 1 163 ? 39.484 -41.314 -4.163  1.00 31.82 ?  163 LYS   B CD   1 
ATOM   6458 C CE   . LYS   B 1 163 ? 38.387 -42.001 -3.360  1.00 36.44 ?  163 LYS   B CE   1 
ATOM   6459 N NZ   . LYS   B 1 163 ? 38.402 -41.618 -1.922  1.00 39.65 ?  163 LYS   B NZ   1 
ATOM   6460 H H    . LYS   B 1 163 ? 41.502 -39.990 -8.422  1.00 18.01 ?  163 LYS   B H    1 
ATOM   6461 H HA   . LYS   B 1 163 ? 39.201 -41.205 -8.216  1.00 18.87 ?  163 LYS   B HA   1 
ATOM   6462 H HB2  . LYS   B 1 163 ? 40.803 -41.240 -6.483  1.00 23.38 ?  163 LYS   B HB2  1 
ATOM   6463 H HB3  . LYS   B 1 163 ? 40.448 -39.723 -6.166  1.00 23.38 ?  163 LYS   B HB3  1 
ATOM   6464 H HG2  . LYS   B 1 163 ? 38.324 -40.323 -5.510  1.00 31.16 ?  163 LYS   B HG2  1 
ATOM   6465 H HG3  . LYS   B 1 163 ? 38.599 -41.832 -5.924  1.00 31.16 ?  163 LYS   B HG3  1 
ATOM   6466 H HD2  . LYS   B 1 163 ? 40.252 -41.906 -4.203  1.00 38.16 ?  163 LYS   B HD2  1 
ATOM   6467 H HD3  . LYS   B 1 163 ? 39.716 -40.484 -3.719  1.00 38.16 ?  163 LYS   B HD3  1 
ATOM   6468 H HE2  . LYS   B 1 163 ? 37.523 -41.760 -3.731  1.00 43.70 ?  163 LYS   B HE2  1 
ATOM   6469 H HE3  . LYS   B 1 163 ? 38.511 -42.962 -3.416  1.00 43.70 ?  163 LYS   B HE3  1 
ATOM   6470 H HZ1  . LYS   B 1 163 ? 37.747 -42.038 -1.489  1.00 47.55 ?  163 LYS   B HZ1  1 
ATOM   6471 H HZ2  . LYS   B 1 163 ? 39.181 -41.841 -1.556  1.00 47.55 ?  163 LYS   B HZ2  1 
ATOM   6472 H HZ3  . LYS   B 1 163 ? 38.284 -40.739 -1.840  1.00 47.55 ?  163 LYS   B HZ3  1 
ATOM   6473 N N    . LEU   B 1 164 ? 39.020 -38.019 -8.048  1.00 13.64 ?  164 LEU   B N    1 
ATOM   6474 C CA   . LEU   B 1 164 ? 38.106 -36.884 -8.103  1.00 13.59 ?  164 LEU   B CA   1 
ATOM   6475 C C    . LEU   B 1 164 ? 37.329 -36.866 -9.413  1.00 13.98 ?  164 LEU   B C    1 
ATOM   6476 O O    . LEU   B 1 164 ? 36.107 -36.675 -9.419  1.00 14.81 ?  164 LEU   B O    1 
ATOM   6477 C CB   . LEU   B 1 164 ? 38.915 -35.595 -7.941  1.00 13.54 ?  164 LEU   B CB   1 
ATOM   6478 C CG   . LEU   B 1 164 ? 39.443 -35.324 -6.537  1.00 14.31 ?  164 LEU   B CG   1 
ATOM   6479 C CD1  . LEU   B 1 164 ? 40.527 -34.255 -6.579  1.00 14.65 ?  164 LEU   B CD1  1 
ATOM   6480 C CD2  . LEU   B 1 164 ? 38.329 -34.894 -5.614  1.00 15.90 ?  164 LEU   B CD2  1 
ATOM   6481 H H    . LEU   B 1 164 ? 39.855 -37.799 -8.044  1.00 16.35 ?  164 LEU   B H    1 
ATOM   6482 H HA   . LEU   B 1 164 ? 37.476 -36.941 -7.372  1.00 16.29 ?  164 LEU   B HA   1 
ATOM   6483 H HB2  . LEU   B 1 164 ? 39.686 -35.635 -8.532  1.00 16.22 ?  164 LEU   B HB2  1 
ATOM   6484 H HB3  . LEU   B 1 164 ? 38.357 -34.844 -8.189  1.00 16.22 ?  164 LEU   B HB3  1 
ATOM   6485 H HG   . LEU   B 1 164 ? 39.838 -36.131 -6.180  1.00 17.14 ?  164 LEU   B HG   1 
ATOM   6486 H HD11 . LEU   B 1 164 ? 40.845 -34.083 -5.676  1.00 17.55 ?  164 LEU   B HD11 1 
ATOM   6487 H HD12 . LEU   B 1 164 ? 41.263 -34.566 -7.131  1.00 17.55 ?  164 LEU   B HD12 1 
ATOM   6488 H HD13 . LEU   B 1 164 ? 40.159 -33.438 -6.956  1.00 17.55 ?  164 LEU   B HD13 1 
ATOM   6489 H HD21 . LEU   B 1 164 ? 38.699 -34.664 -4.748  1.00 19.05 ?  164 LEU   B HD21 1 
ATOM   6490 H HD22 . LEU   B 1 164 ? 37.876 -34.124 -5.994  1.00 19.05 ?  164 LEU   B HD22 1 
ATOM   6491 H HD23 . LEU   B 1 164 ? 37.699 -35.628 -5.517  1.00 19.05 ?  164 LEU   B HD23 1 
ATOM   6492 N N    . VAL   B 1 165 ? 38.025 -37.035 -10.538 1.00 14.99 ?  165 VAL   B N    1 
ATOM   6493 C CA   . VAL   B 1 165 ? 37.373 -36.972 -11.841 1.00 15.72 ?  165 VAL   B CA   1 
ATOM   6494 C C    . VAL   B 1 165 ? 36.461 -38.174 -12.031 1.00 17.74 ?  165 VAL   B C    1 
ATOM   6495 O O    . VAL   B 1 165 ? 35.304 -38.042 -12.448 1.00 18.36 ?  165 VAL   B O    1 
ATOM   6496 C CB   . VAL   B 1 165 ? 38.423 -36.876 -12.963 1.00 17.04 ?  165 VAL   B CB   1 
ATOM   6497 C CG1  . VAL   B 1 165 ? 37.762 -36.959 -14.321 1.00 18.20 ?  165 VAL   B CG1  1 
ATOM   6498 C CG2  . VAL   B 1 165 ? 39.221 -35.593 -12.833 1.00 17.61 ?  165 VAL   B CG2  1 
ATOM   6499 H H    . VAL   B 1 165 ? 38.874 -37.179 -10.570 1.00 17.97 ?  165 VAL   B H    1 
ATOM   6500 H HA   . VAL   B 1 165 ? 36.824 -36.176 -11.881 1.00 18.84 ?  165 VAL   B HA   1 
ATOM   6501 H HB   . VAL   B 1 165 ? 39.045 -37.616 -12.881 1.00 20.43 ?  165 VAL   B HB   1 
ATOM   6502 H HG11 . VAL   B 1 165 ? 38.388 -36.655 -14.994 1.00 21.81 ?  165 VAL   B HG11 1 
ATOM   6503 H HG12 . VAL   B 1 165 ? 37.517 -37.881 -14.493 1.00 21.81 ?  165 VAL   B HG12 1 
ATOM   6504 H HG13 . VAL   B 1 165 ? 36.973 -36.398 -14.322 1.00 21.81 ?  165 VAL   B HG13 1 
ATOM   6505 H HG21 . VAL   B 1 165 ? 39.855 -35.536 -13.566 1.00 21.11 ?  165 VAL   B HG21 1 
ATOM   6506 H HG22 . VAL   B 1 165 ? 38.612 -34.836 -12.867 1.00 21.11 ?  165 VAL   B HG22 1 
ATOM   6507 H HG23 . VAL   B 1 165 ? 39.695 -35.593 -11.986 1.00 21.11 ?  165 VAL   B HG23 1 
ATOM   6508 N N    . SER   B 1 166 ? 36.972 -39.369 -11.723 1.00 18.41 ?  166 SER   B N    1 
ATOM   6509 C CA   . SER   B 1 166 ? 36.218 -40.582 -12.004 1.00 19.77 ?  166 SER   B CA   1 
ATOM   6510 C C    . SER   B 1 166 ? 34.958 -40.671 -11.155 1.00 20.02 ?  166 SER   B C    1 
ATOM   6511 O O    . SER   B 1 166 ? 33.986 -41.296 -11.579 1.00 21.25 ?  166 SER   B O    1 
ATOM   6512 C CB   . SER   B 1 166 ? 37.091 -41.835 -11.836 1.00 20.73 ?  166 SER   B CB   1 
ATOM   6513 O OG   . SER   B 1 166 ? 37.455 -42.045 -10.483 1.00 20.58 ?  166 SER   B OG   1 
ATOM   6514 H H    . SER   B 1 166 ? 37.749 -39.501 -11.362 1.00 22.07 ?  166 SER   B H    1 
ATOM   6515 H HA   . SER   B 1 166 ? 35.944 -40.560 -12.932 1.00 23.71 ?  166 SER   B HA   1 
ATOM   6516 H HB2  . SER   B 1 166 ? 36.597 -42.608 -12.149 1.00 24.85 ?  166 SER   B HB2  1 
ATOM   6517 H HB3  . SER   B 1 166 ? 37.900 -41.730 -12.369 1.00 24.85 ?  166 SER   B HB3  1 
ATOM   6518 H HG   . SER   B 1 166 ? 37.905 -41.393 -10.203 1.00 24.67 ?  166 SER   B HG   1 
ATOM   6519 N N    . SER   B 1 167 ? 34.941 -40.067 -9.969  1.00 18.81 ?  167 SER   B N    1 
ATOM   6520 C CA   . SER   B 1 167 ? 33.780 -40.125 -9.089  1.00 18.32 ?  167 SER   B CA   1 
ATOM   6521 C C    . SER   B 1 167 ? 32.864 -38.906 -9.200  1.00 17.92 ?  167 SER   B C    1 
ATOM   6522 O O    . SER   B 1 167 ? 31.784 -38.902 -8.593  1.00 18.37 ?  167 SER   B O    1 
ATOM   6523 C CB   . SER   B 1 167 ? 34.215 -40.298 -7.627  1.00 18.34 ?  167 SER   B CB   1 
ATOM   6524 O OG   . SER   B 1 167 ? 34.893 -39.141 -7.158  1.00 18.04 ?  167 SER   B OG   1 
ATOM   6525 H H    . SER   B 1 167 ? 35.598 -39.615 -9.651  1.00 22.54 ?  167 SER   B H    1 
ATOM   6526 H HA   . SER   B 1 167 ? 33.258 -40.907 -9.329  1.00 21.96 ?  167 SER   B HA   1 
ATOM   6527 H HB2  . SER   B 1 167 ? 33.425 -40.448 -7.082  1.00 21.98 ?  167 SER   B HB2  1 
ATOM   6528 H HB3  . SER   B 1 167 ? 34.805 -41.071 -7.564  1.00 21.98 ?  167 SER   B HB3  1 
ATOM   6529 H HG   . SER   B 1 167 ? 35.585 -39.019 -7.620  1.00 21.62 ?  167 SER   B HG   1 
ATOM   6530 N N    . PHE   B 1 168 ? 33.242 -37.881 -9.970  1.00 17.65 ?  168 PHE   B N    1 
ATOM   6531 C CA   . PHE   B 1 168 ? 32.418 -36.676 -10.034 1.00 17.12 ?  168 PHE   B CA   1 
ATOM   6532 C C    . PHE   B 1 168 ? 31.089 -36.936 -10.737 1.00 15.17 ?  168 PHE   B C    1 
ATOM   6533 O O    . PHE   B 1 168 ? 30.061 -36.319 -10.392 1.00 16.08 ?  168 PHE   B O    1 
ATOM   6534 C CB   . PHE   B 1 168 ? 33.177 -35.552 -10.738 1.00 17.79 ?  168 PHE   B CB   1 
ATOM   6535 C CG   . PHE   B 1 168 ? 32.382 -34.299 -10.856 1.00 17.86 ?  168 PHE   B CG   1 
ATOM   6536 C CD1  . PHE   B 1 168 ? 32.079 -33.560 -9.722  1.00 19.22 ?  168 PHE   B CD1  1 
ATOM   6537 C CD2  . PHE   B 1 168 ? 31.908 -33.870 -12.080 1.00 17.13 ?  168 PHE   B CD2  1 
ATOM   6538 C CE1  . PHE   B 1 168 ? 31.323 -32.409 -9.805  1.00 19.92 ?  168 PHE   B CE1  1 
ATOM   6539 C CE2  . PHE   B 1 168 ? 31.165 -32.700 -12.178 1.00 18.55 ?  168 PHE   B CE2  1 
ATOM   6540 C CZ   . PHE   B 1 168 ? 30.865 -31.974 -11.037 1.00 19.03 ?  168 PHE   B CZ   1 
ATOM   6541 H H    . PHE   B 1 168 ? 33.956 -37.864 -10.453 1.00 21.15 ?  168 PHE   B H    1 
ATOM   6542 H HA   . PHE   B 1 168 ? 32.225 -36.387 -9.134  1.00 20.52 ?  168 PHE   B HA   1 
ATOM   6543 H HB2  . PHE   B 1 168 ? 33.981 -35.349 -10.230 1.00 21.32 ?  168 PHE   B HB2  1 
ATOM   6544 H HB3  . PHE   B 1 168 ? 33.417 -35.839 -11.632 1.00 21.32 ?  168 PHE   B HB3  1 
ATOM   6545 H HD1  . PHE   B 1 168 ? 32.382 -33.856 -8.893  1.00 23.04 ?  168 PHE   B HD1  1 
ATOM   6546 H HD2  . PHE   B 1 168 ? 32.110 -34.354 -12.848 1.00 20.53 ?  168 PHE   B HD2  1 
ATOM   6547 H HE1  . PHE   B 1 168 ? 31.126 -31.923 -9.036  1.00 23.88 ?  168 PHE   B HE1  1 
ATOM   6548 H HE2  . PHE   B 1 168 ? 30.851 -32.417 -13.009 1.00 22.24 ?  168 PHE   B HE2  1 
ATOM   6549 H HZ   . PHE   B 1 168 ? 30.355 -31.195 -11.102 1.00 22.81 ?  168 PHE   B HZ   1 
ATOM   6550 N N    . LEU   B 1 169 ? 31.099 -37.827 -11.724 1.00 15.30 ?  169 LEU   B N    1 
ATOM   6551 C CA   . LEU   B 1 169 ? 29.917 -38.116 -12.518 1.00 17.40 ?  169 LEU   B CA   1 
ATOM   6552 C C    . LEU   B 1 169 ? 29.914 -39.547 -13.030 1.00 20.06 ?  169 LEU   B C    1 
ATOM   6553 O O    . LEU   B 1 169 ? 29.004 -39.960 -13.748 1.00 22.77 ?  169 LEU   B O    1 
ATOM   6554 C CB   . LEU   B 1 169 ? 29.838 -37.152 -13.702 1.00 19.47 ?  169 LEU   B CB   1 
ATOM   6555 C CG   . LEU   B 1 169 ? 28.570 -36.297 -13.792 1.00 22.87 ?  169 LEU   B CG   1 
ATOM   6556 C CD1  . LEU   B 1 169 ? 28.536 -35.558 -15.117 1.00 24.20 ?  169 LEU   B CD1  1 
ATOM   6557 C CD2  . LEU   B 1 169 ? 27.313 -37.130 -13.606 1.00 23.10 ?  169 LEU   B CD2  1 
ATOM   6558 O OXT  . LEU   B 1 169 ? 30.829 -40.311 -12.742 1.00 21.11 -1 169 LEU   B OXT  1 
ATOM   6559 H H    . LEU   B 1 169 ? 31.796 -38.276 -11.967 1.00 18.33 ?  169 LEU   B H    1 
ATOM   6560 H HA   . LEU   B 1 169 ? 29.134 -37.994 -11.966 1.00 20.86 ?  169 LEU   B HA   1 
ATOM   6561 H HB2  . LEU   B 1 169 ? 30.590 -36.542 -13.653 1.00 23.35 ?  169 LEU   B HB2  1 
ATOM   6562 H HB3  . LEU   B 1 169 ? 29.892 -37.665 -14.523 1.00 23.35 ?  169 LEU   B HB3  1 
ATOM   6563 H HG   . LEU   B 1 169 ? 28.592 -35.631 -13.087 1.00 27.42 ?  169 LEU   B HG   1 
ATOM   6564 H HD11 . LEU   B 1 169 ? 27.739 -35.006 -15.149 1.00 29.02 ?  169 LEU   B HD11 1 
ATOM   6565 H HD12 . LEU   B 1 169 ? 29.328 -35.003 -15.188 1.00 29.02 ?  169 LEU   B HD12 1 
ATOM   6566 H HD13 . LEU   B 1 169 ? 28.520 -36.207 -15.837 1.00 29.02 ?  169 LEU   B HD13 1 
ATOM   6567 H HD21 . LEU   B 1 169 ? 26.558 -36.660 -13.991 1.00 27.69 ?  169 LEU   B HD21 1 
ATOM   6568 H HD22 . LEU   B 1 169 ? 27.432 -37.986 -14.049 1.00 27.69 ?  169 LEU   B HD22 1 
ATOM   6569 H HD23 . LEU   B 1 169 ? 27.168 -37.269 -12.657 1.00 27.69 ?  169 LEU   B HD23 1 
HETATM 6570 N N2   B A1BAY C 2 .   ? 14.704 -0.018  4.267   0.20 12.36 ?  201 A1BAY A N2   1 
HETATM 6571 C C3   B A1BAY C 2 .   ? 11.704 0.300   2.185   0.20 17.57 ?  201 A1BAY A C3   1 
HETATM 6572 C C6   B A1BAY C 2 .   ? 14.961 -0.051  5.612   0.20 12.02 ?  201 A1BAY A C6   1 
HETATM 6573 C C9   B A1BAY C 2 .   ? 15.220 3.773   4.149   0.20 11.74 ?  201 A1BAY A C9   1 
HETATM 6574 C C12  B A1BAY C 2 .   ? 14.857 2.072   0.037   0.20 13.95 ?  201 A1BAY A C12  1 
HETATM 6575 C C14  B A1BAY C 2 .   ? 16.540 0.277   0.062   0.20 15.54 ?  201 A1BAY A C14  1 
HETATM 6576 C C1   B A1BAY C 2 .   ? 12.006 -0.857  0.047   0.20 17.68 ?  201 A1BAY A C1   1 
HETATM 6577 C C10  B A1BAY C 2 .   ? 15.543 4.369   5.338   0.20 11.29 ?  201 A1BAY A C10  1 
HETATM 6578 C C11  B A1BAY C 2 .   ? 14.307 2.421   1.413   0.20 13.69 ?  201 A1BAY A C11  1 
HETATM 6579 C C13  B A1BAY C 2 .   ? 15.038 0.551   -0.009  0.20 14.76 ?  201 A1BAY A C13  1 
HETATM 6580 C C15  B A1BAY C 2 .   ? 14.692 0.014   -1.406  0.20 14.78 ?  201 A1BAY A C15  1 
HETATM 6581 C C2   B A1BAY C 2 .   ? 12.700 -0.564  1.389   0.20 17.22 ?  201 A1BAY A C2   1 
HETATM 6582 C C4   B A1BAY C 2 .   ? 14.227 0.022   1.333   0.20 15.24 ?  201 A1BAY A C4   1 
HETATM 6583 C C5   B A1BAY C 2 .   ? 14.739 1.171   3.607   0.20 12.13 ?  201 A1BAY A C5   1 
HETATM 6584 C C7   B A1BAY C 2 .   ? 15.304 2.168   5.741   0.20 11.33 ?  201 A1BAY A C7   1 
HETATM 6585 C C8   B A1BAY C 2 .   ? 15.061 2.365   4.349   0.20 11.50 ?  201 A1BAY A C8   1 
HETATM 6586 N N1   B A1BAY C 2 .   ? 14.462 1.181   2.196   0.20 13.45 ?  201 A1BAY A N1   1 
HETATM 6587 N N3   B A1BAY C 2 .   ? 15.265 0.982   6.400   0.20 11.53 ?  201 A1BAY A N3   1 
HETATM 6588 N N4   B A1BAY C 2 .   ? 15.589 3.395   6.332   0.20 11.50 ?  201 A1BAY A N4   1 
HETATM 6589 O O1   B A1BAY C 2 .   ? 12.826 -1.712  2.166   0.20 17.78 ?  201 A1BAY A O1   1 
HETATM 6590 H H7   B A1BAY C 2 .   ? 11.581 1.294   1.769   0.20 21.06 ?  201 A1BAY A H7   1 
HETATM 6591 H H5   B A1BAY C 2 .   ? 11.993 0.373   3.240   0.20 21.06 ?  201 A1BAY A H5   1 
HETATM 6592 H H6   B A1BAY C 2 .   ? 10.690 -0.154  2.221   0.20 21.06 ?  201 A1BAY A H6   1 
HETATM 6593 H H9   B A1BAY C 2 .   ? 14.917 -1.024  6.134   0.20 14.40 ?  201 A1BAY A H9   1 
HETATM 6594 H H10  B A1BAY C 2 .   ? 15.111 4.297   3.210   0.20 14.07 ?  201 A1BAY A H10  1 
HETATM 6595 H H15  B A1BAY C 2 .   ? 14.222 2.466   -0.776  0.20 16.72 ?  201 A1BAY A H15  1 
HETATM 6596 H H16  B A1BAY C 2 .   ? 15.825 2.605   -0.116  0.20 16.72 ?  201 A1BAY A H16  1 
HETATM 6597 H H17  B A1BAY C 2 .   ? 17.109 0.647   -0.779  0.20 18.63 ?  201 A1BAY A H17  1 
HETATM 6598 H H18  B A1BAY C 2 .   ? 16.757 -0.802  0.076   0.20 18.63 ?  201 A1BAY A H18  1 
HETATM 6599 H H19  B A1BAY C 2 .   ? 17.028 0.652   0.974   0.20 18.63 ?  201 A1BAY A H19  1 
HETATM 6600 H H4   B A1BAY C 2 .   ? 12.374 -1.742  -0.482  0.20 21.19 ?  201 A1BAY A H4   1 
HETATM 6601 H H3   B A1BAY C 2 .   ? 12.058 -0.040  -0.646  0.20 21.19 ?  201 A1BAY A H3   1 
HETATM 6602 H H2   B A1BAY C 2 .   ? 10.921 -1.030  0.166   0.20 21.19 ?  201 A1BAY A H2   1 
HETATM 6603 H H11  B A1BAY C 2 .   ? 15.739 5.414   5.576   0.20 13.52 ?  201 A1BAY A H11  1 
HETATM 6604 H H13  B A1BAY C 2 .   ? 13.264 2.790   1.412   0.20 16.40 ?  201 A1BAY A H13  1 
HETATM 6605 H H14  B A1BAY C 2 .   ? 14.878 3.269   1.772   0.20 16.40 ?  201 A1BAY A H14  1 
HETATM 6606 H H20  B A1BAY C 2 .   ? 15.448 0.371   -2.156  0.20 17.72 ?  201 A1BAY A H20  1 
HETATM 6607 H H21  B A1BAY C 2 .   ? 13.747 0.333   -1.800  0.20 17.72 ?  201 A1BAY A H21  1 
HETATM 6608 H H22  B A1BAY C 2 .   ? 14.750 -1.076  -1.463  0.20 17.72 ?  201 A1BAY A H22  1 
HETATM 6609 H H1   B A1BAY C 2 .   ? 14.814 -0.782  1.807   0.20 18.26 ?  201 A1BAY A H1   1 
HETATM 6610 H H12  B A1BAY C 2 .   ? 15.811 3.532   7.314   0.20 13.77 ?  201 A1BAY A H12  1 
HETATM 6611 H H8   B A1BAY C 2 .   ? 13.415 -2.322  1.720   0.20 21.31 ?  201 A1BAY A H8   1 
HETATM 6612 O O1   C A1BAZ D 3 .   ? 16.006 -1.040  1.691   0.20 14.82 ?  202 A1BAZ A O1   1 
HETATM 6613 C C1   C A1BAZ D 3 .   ? 15.571 -0.021  -0.477  0.20 13.20 ?  202 A1BAZ A C1   1 
HETATM 6614 C C2   C A1BAZ D 3 .   ? 14.996 -0.817  0.735   0.20 13.50 ?  202 A1BAZ A C2   1 
HETATM 6615 C C3   C A1BAZ D 3 .   ? 14.614 -2.239  0.318   0.20 13.77 ?  202 A1BAZ A C3   1 
HETATM 6616 C C4   C A1BAZ D 3 .   ? 13.842 -0.027  1.549   0.20 12.84 ?  202 A1BAZ A C4   1 
HETATM 6617 C C5   C A1BAZ D 3 .   ? 14.734 1.194   3.591   0.20 11.18 ?  202 A1BAZ A C5   1 
HETATM 6618 C C6   C A1BAZ D 3 .   ? 14.879 -0.049  5.593   0.20 11.53 ?  202 A1BAZ A C6   1 
HETATM 6619 C C7   C A1BAZ D 3 .   ? 15.306 2.142   5.749   0.20 10.84 ?  202 A1BAZ A C7   1 
HETATM 6620 C C8   C A1BAZ D 3 .   ? 15.094 2.356   4.351   0.20 10.74 ?  202 A1BAZ A C8   1 
HETATM 6621 C C10  C A1BAZ D 3 .   ? 15.641 4.346   5.379   0.20 10.82 ?  202 A1BAZ A C10  1 
HETATM 6622 C C11  C A1BAZ D 3 .   ? 14.030 2.387   1.494   0.20 12.92 ?  202 A1BAZ A C11  1 
HETATM 6623 C C12  C A1BAZ D 3 .   ? 12.750 2.044   0.727   0.20 13.49 ?  202 A1BAZ A C12  1 
HETATM 6624 C C13  C A1BAZ D 3 .   ? 12.523 0.520   0.784   0.20 13.41 ?  202 A1BAZ A C13  1 
HETATM 6625 C C14  C A1BAZ D 3 .   ? 12.221 -0.005  -0.632  0.20 13.61 ?  202 A1BAZ A C14  1 
HETATM 6626 C C15  C A1BAZ D 3 .   ? 11.225 0.216   1.549   0.20 14.28 ?  202 A1BAZ A C15  1 
HETATM 6627 C C9   C A1BAZ D 3 .   ? 15.313 3.776   4.157   0.20 11.16 ?  202 A1BAZ A C9   1 
HETATM 6628 N N1   C A1BAZ D 3 .   ? 14.459 1.159   2.215   0.20 12.03 ?  202 A1BAZ A N1   1 
HETATM 6629 N N2   C A1BAZ D 3 .   ? 14.632 -0.022  4.251   0.20 11.80 ?  202 A1BAZ A N2   1 
HETATM 6630 N N3   C A1BAZ D 3 .   ? 15.214 0.950   6.416   0.20 11.15 ?  202 A1BAZ A N3   1 
HETATM 6631 N N4   C A1BAZ D 3 .   ? 15.631 3.344   6.356   0.20 11.15 ?  202 A1BAZ A N4   1 
HETATM 6632 H H8   C A1BAZ D 3 .   ? 16.652 -1.650  1.325   0.20 17.76 ?  202 A1BAZ A H8   1 
HETATM 6633 H H2   C A1BAZ D 3 .   ? 14.952 0.806   -0.797  0.20 15.81 ?  202 A1BAZ A H2   1 
HETATM 6634 H H3   C A1BAZ D 3 .   ? 15.735 -0.644  -1.381  0.20 15.81 ?  202 A1BAZ A H3   1 
HETATM 6635 H H4   C A1BAZ D 3 .   ? 16.562 0.433   -0.279  0.20 15.81 ?  202 A1BAZ A H4   1 
HETATM 6636 H H6   C A1BAZ D 3 .   ? 13.657 -2.262  -0.196  0.20 16.50 ?  202 A1BAZ A H6   1 
HETATM 6637 H H5   C A1BAZ D 3 .   ? 14.500 -2.893  1.199   0.20 16.50 ?  202 A1BAZ A H5   1 
HETATM 6638 H H7   C A1BAZ D 3 .   ? 15.363 -2.701  -0.339  0.20 16.50 ?  202 A1BAZ A H7   1 
HETATM 6639 H H1   C A1BAZ D 3 .   ? 13.496 -0.734  2.312   0.20 15.38 ?  202 A1BAZ A H1   1 
HETATM 6640 H H9   C A1BAZ D 3 .   ? 14.789 -1.028  6.096   0.20 13.82 ?  202 A1BAZ A H9   1 
HETATM 6641 H H11  C A1BAZ D 3 .   ? 15.875 5.371   5.643   0.20 12.96 ?  202 A1BAZ A H11  1 
HETATM 6642 H H13  C A1BAZ D 3 .   ? 13.835 3.234   2.170   0.20 15.48 ?  202 A1BAZ A H13  1 
HETATM 6643 H H14  C A1BAZ D 3 .   ? 14.829 2.741   0.808   0.20 15.48 ?  202 A1BAZ A H14  1 
HETATM 6644 H H15  C A1BAZ D 3 .   ? 11.880 2.602   1.150   0.20 16.16 ?  202 A1BAZ A H15  1 
HETATM 6645 H H16  C A1BAZ D 3 .   ? 12.789 2.419   -0.310  0.20 16.16 ?  202 A1BAZ A H16  1 
HETATM 6646 H H18  C A1BAZ D 3 .   ? 13.067 -0.036  -1.295  0.20 16.31 ?  202 A1BAZ A H18  1 
HETATM 6647 H H17  C A1BAZ D 3 .   ? 11.475 0.652   -1.147  0.20 16.31 ?  202 A1BAZ A H17  1 
HETATM 6648 H H19  C A1BAZ D 3 .   ? 11.755 -0.992  -0.626  0.20 16.31 ?  202 A1BAZ A H19  1 
HETATM 6649 H H20  C A1BAZ D 3 .   ? 10.378 0.880   1.318   0.20 17.11 ?  202 A1BAZ A H20  1 
HETATM 6650 H H21  C A1BAZ D 3 .   ? 11.322 0.310   2.641   0.20 17.11 ?  202 A1BAZ A H21  1 
HETATM 6651 H H22  C A1BAZ D 3 .   ? 10.870 -0.807  1.403   0.20 17.11 ?  202 A1BAZ A H22  1 
HETATM 6652 H H10  C A1BAZ D 3 .   ? 15.240 4.332   3.244   0.20 13.37 ?  202 A1BAZ A H10  1 
HETATM 6653 H H12  C A1BAZ D 3 .   ? 15.840 3.461   7.340   0.20 13.36 ?  202 A1BAZ A H12  1 
HETATM 6654 O O    . HOH   E 4 .   ? 14.811 -4.700  20.590  1.00 46.31 ?  301 HOH   A O    1 
HETATM 6655 O O    . HOH   E 4 .   ? 34.444 -1.880  12.497  1.00 41.30 ?  302 HOH   A O    1 
HETATM 6656 O O    B HOH   E 4 .   ? 19.092 -1.959  -0.521  0.40 29.59 ?  303 HOH   A O    1 
HETATM 6657 O O    . HOH   E 4 .   ? 15.234 -12.284 18.751  1.00 34.89 ?  304 HOH   A O    1 
HETATM 6658 O O    . HOH   E 4 .   ? 28.903 0.494   -9.673  1.00 21.90 ?  305 HOH   A O    1 
HETATM 6659 O O    . HOH   E 4 .   ? 4.804  3.954   0.828   1.00 26.01 ?  306 HOH   A O    1 
HETATM 6660 O O    . HOH   E 4 .   ? 28.394 -0.261  -13.330 1.00 37.16 ?  307 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 9.060  -10.204 19.481  1.00 45.39 ?  308 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 15.240 -21.631 14.242  1.00 18.55 ?  309 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 15.032 3.682   17.810  1.00 40.87 ?  310 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 36.135 -5.049  -0.507  1.00 28.69 ?  311 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 9.840  -21.342 5.766   1.00 20.64 ?  312 HOH   A O    1 
HETATM 6666 O O    . HOH   E 4 .   ? 8.011  -12.582 -0.838  1.00 24.10 ?  313 HOH   A O    1 
HETATM 6667 O O    . HOH   E 4 .   ? 42.421 10.544  5.221   1.00 19.88 ?  314 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 18.880 -21.995 6.860   1.00 32.27 ?  315 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 7.976  -21.413 3.951   1.00 45.11 ?  316 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 14.771 -13.996 16.741  1.00 23.08 ?  317 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 17.155 -18.090 15.097  1.00 28.41 ?  318 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 19.897 -12.476 -8.930  1.00 26.21 ?  319 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 30.249 -13.291 -8.562  1.00 19.84 ?  320 HOH   A O    1 
HETATM 6674 O O    B HOH   E 4 .   ? 15.042 -3.076  3.640   0.40 17.83 ?  321 HOH   A O    1 
HETATM 6675 O O    A HOH   E 4 .   ? 0.719  -4.633  0.298   0.60 28.47 ?  322 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 28.239 -6.324  19.669  1.00 45.81 ?  323 HOH   A O    1 
HETATM 6677 O O    A HOH   E 4 .   ? 3.594  -9.510  9.769   0.60 30.07 ?  324 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 26.478 -19.324 -1.823  1.00 13.59 ?  325 HOH   A O    1 
HETATM 6679 O O    . HOH   E 4 .   ? 17.039 -19.292 4.901   1.00 15.20 ?  326 HOH   A O    1 
HETATM 6680 O O    A HOH   E 4 .   ? 14.047 -4.570  -11.690 0.60 24.33 ?  327 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 38.070 -1.314  -1.953  1.00 18.99 ?  328 HOH   A O    1 
HETATM 6682 O O    A HOH   E 4 .   ? 7.693  -6.330  -6.467  0.60 31.14 ?  329 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 7.025  -8.200  11.973  1.00 23.51 ?  330 HOH   A O    1 
HETATM 6684 O O    . HOH   E 4 .   ? 27.288 13.745  2.965   1.00 33.76 ?  331 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 18.649 -19.436 13.570  1.00 34.36 ?  332 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 33.920 -1.020  -8.933  1.00 28.14 ?  333 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 31.024 -18.157 7.749   1.00 20.66 ?  334 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 26.804 11.385  1.720   1.00 17.31 ?  335 HOH   A O    1 
HETATM 6689 O O    B HOH   E 4 .   ? 11.948 -2.458  -7.596  0.40 34.46 ?  336 HOH   A O    1 
HETATM 6690 O O    A HOH   E 4 .   ? 17.480 -1.728  0.490   0.60 23.18 ?  337 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 37.534 2.751   10.198  1.00 27.68 ?  338 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 22.357 -19.320 11.312  1.00 34.82 ?  339 HOH   A O    1 
HETATM 6693 O O    B HOH   E 4 .   ? 7.026  1.514   7.603   0.40 26.15 ?  340 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 38.554 4.967   6.967   1.00 16.29 ?  341 HOH   A O    1 
HETATM 6695 O O    B HOH   E 4 .   ? 14.754 7.288   7.566   0.40 21.76 ?  342 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 17.160 -17.840 -5.033  1.00 27.62 ?  343 HOH   A O    1 
HETATM 6697 O O    A HOH   E 4 .   ? 13.286 -1.433  -6.471  0.60 18.86 ?  344 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 25.689 -0.776  -7.329  1.00 18.07 ?  345 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 38.257 10.076  7.196   1.00 37.73 ?  346 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? 20.643 -19.663 -5.154  1.00 28.14 ?  347 HOH   A O    1 
HETATM 6701 O O    A HOH   E 4 .   ? 21.228 -2.402  -2.008  0.60 12.81 ?  348 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 23.971 3.915   -4.675  1.00 26.77 ?  349 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 39.701 -0.982  -5.191  1.00 21.34 ?  350 HOH   A O    1 
HETATM 6704 O O    A HOH   E 4 .   ? 14.263 0.540   6.857   0.60 30.08 ?  351 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 44.241 7.053   6.485   1.00 26.98 ?  352 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 35.763 -12.719 6.801   1.00 16.20 ?  353 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 22.352 5.283   19.003  1.00 45.05 ?  354 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 24.006 -2.121  -2.072  1.00 11.69 ?  355 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 23.990 -15.668 -9.192  1.00 32.57 ?  356 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 42.516 4.267   5.314   1.00 30.83 ?  357 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 24.323 3.600   -1.720  1.00 17.31 ?  358 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 22.745 12.480  1.665   1.00 16.68 ?  359 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 30.797 3.040   8.282   1.00 12.50 ?  360 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 37.321 11.925  4.950   1.00 35.92 ?  361 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 11.799 -10.791 17.097  1.00 28.15 ?  362 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 18.554 9.410   9.068   1.00 23.94 ?  363 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 14.377 -21.206 -4.289  1.00 30.48 ?  364 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 31.061 -13.939 -2.500  1.00 13.49 ?  365 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 31.702 8.174   14.890  1.00 23.56 ?  366 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 16.510 -22.000 0.957   1.00 28.57 ?  367 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 31.877 -9.296  -6.643  1.00 22.34 ?  368 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 14.000 -5.015  17.502  1.00 24.27 ?  369 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 21.903 -21.927 8.342   1.00 30.55 ?  370 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 12.092 0.334   14.901  1.00 36.10 ?  371 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 23.446 11.352  4.180   1.00 13.23 ?  372 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 27.586 2.238   18.732  1.00 33.47 ?  373 HOH   A O    1 
HETATM 6727 O O    . HOH   E 4 .   ? 27.566 -10.711 14.027  1.00 17.40 ?  374 HOH   A O    1 
HETATM 6728 O O    A HOH   E 4 .   ? 14.622 -3.677  3.143   0.60 15.37 ?  375 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 33.669 -7.164  4.259   1.00 16.61 ?  376 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 37.251 -2.943  9.654   1.00 42.81 ?  377 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 43.855 8.457   -3.108  1.00 26.77 ?  378 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 22.627 -12.014 21.870  1.00 45.57 ?  379 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 13.564 -15.248 -7.484  1.00 27.96 ?  380 HOH   A O    1 
HETATM 6734 O O    A HOH   E 4 .   ? 20.072 4.551   -7.482  0.60 17.01 ?  381 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? -0.562 -3.150  3.165   1.00 47.01 ?  382 HOH   A O    1 
HETATM 6736 O O    B HOH   E 4 .   ? 16.107 -8.333  -7.195  0.40 23.28 ?  383 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 14.066 -23.072 7.435   1.00 19.54 ?  384 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 43.298 7.825   2.666   1.00 24.80 ?  385 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 24.385 -7.885  14.478  1.00 17.72 ?  386 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 27.859 0.856   -7.156  1.00 14.16 ?  387 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 21.308 10.197  15.174  1.00 32.65 ?  388 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 6.516  -5.658  11.290  1.00 21.77 ?  389 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 31.803 -7.306  -9.828  1.00 21.71 ?  390 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 16.060 -6.679  -11.797 1.00 47.73 ?  391 HOH   A O    1 
HETATM 6745 O O    A HOH   E 4 .   ? -0.645 -8.525  2.447   0.60 45.41 ?  392 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 8.808  -12.028 17.274  1.00 42.13 ?  393 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 24.730 -17.638 12.655  1.00 24.45 ?  394 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 32.773 -9.279  5.907   1.00 20.16 ?  395 HOH   A O    1 
HETATM 6749 O O    A HOH   E 4 .   ? 15.787 -0.974  5.322   0.60 33.88 ?  396 HOH   A O    1 
HETATM 6750 O O    B HOH   E 4 .   ? 21.015 2.576   0.441   0.40 29.41 ?  397 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 26.905 4.138   -0.585  1.00 13.36 ?  398 HOH   A O    1 
HETATM 6752 O O    A HOH   E 4 .   ? 11.712 -10.771 -10.036 0.60 38.03 ?  399 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 37.541 -2.035  5.719   1.00 25.92 ?  400 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 10.461 -22.138 -1.171  1.00 47.92 ?  401 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 20.578 -20.000 2.730   1.00 17.59 ?  402 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 11.030 1.604   12.705  1.00 25.11 ?  403 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 15.498 11.859  7.971   1.00 32.54 ?  404 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 30.787 1.756   16.694  1.00 22.59 ?  405 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 14.361 -24.720 11.644  1.00 40.68 ?  406 HOH   A O    1 
HETATM 6760 O O    A HOH   E 4 .   ? 21.329 3.145   -0.290  0.60 12.51 ?  407 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 23.915 -20.270 -1.398  1.00 15.96 ?  408 HOH   A O    1 
HETATM 6762 O O    A HOH   E 4 .   ? 11.051 -0.402  1.991   0.60 40.73 ?  409 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 40.849 -8.256  -6.745  1.00 36.98 ?  410 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 16.243 -14.206 20.407  1.00 41.25 ?  411 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 27.141 -3.404  19.384  1.00 37.83 ?  412 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 30.140 -10.215 12.984  1.00 21.50 ?  413 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 15.957 6.994   3.006   1.00 17.16 ?  414 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 15.162 -8.142  -9.616  1.00 29.09 ?  415 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 14.529 -0.413  -12.120 1.00 33.81 ?  416 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 32.551 -10.642 3.149   1.00 30.69 ?  417 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 30.900 6.209   -12.285 1.00 29.06 ?  418 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 24.523 1.978   -6.933  1.00 21.95 ?  419 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 41.567 1.594   4.933   1.00 36.73 ?  420 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 21.737 -13.804 -8.110  1.00 40.75 ?  421 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 10.439 -13.771 -1.670  1.00 19.15 ?  422 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 30.404 -12.996 13.453  1.00 20.02 ?  423 HOH   A O    1 
HETATM 6777 O O    B HOH   E 4 .   ? 21.190 -2.310  -2.997  0.40 18.03 ?  424 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 32.673 -4.316  -9.909  1.00 28.46 ?  425 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 16.306 16.739  8.702   1.00 30.56 ?  426 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 35.055 -5.219  -3.086  1.00 18.76 ?  427 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 36.730 -4.981  5.308   1.00 24.89 ?  428 HOH   A O    1 
HETATM 6782 O O    B HOH   E 4 .   ? 10.936 4.222   2.971   0.40 32.17 ?  429 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 20.592 -17.765 24.759  1.00 52.65 ?  430 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 28.600 -10.617 -14.017 1.00 48.82 ?  431 HOH   A O    1 
HETATM 6785 O O    A HOH   E 4 .   ? 18.940 -0.677  -1.576  0.60 14.47 ?  432 HOH   A O    1 
HETATM 6786 O O    B HOH   E 4 .   ? 12.113 6.355   11.114  0.40 28.76 ?  433 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 27.549 -6.273  -14.007 1.00 40.44 ?  434 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 5.112  2.606   5.182   1.00 33.84 ?  435 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 6.760  -3.453  13.062  1.00 32.68 ?  436 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 18.794 2.146   -0.679  1.00 16.09 ?  437 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 22.682 7.928   18.477  1.00 49.11 ?  438 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 37.715 -8.847  -3.521  1.00 26.13 ?  439 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 44.975 -0.620  2.952   1.00 42.67 ?  440 HOH   A O    1 
HETATM 6794 O O    A HOH   E 4 .   ? 18.543 -2.431  -16.293 0.60 31.97 ?  441 HOH   A O    1 
HETATM 6795 O O    B HOH   E 4 .   ? 9.384  1.945   -1.026  0.40 29.59 ?  442 HOH   A O    1 
HETATM 6796 O O    A HOH   E 4 .   ? 15.864 2.124   24.847  0.60 40.63 ?  443 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 23.703 -8.147  17.048  1.00 22.22 ?  444 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 21.340 -9.326  21.338  1.00 43.78 ?  445 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 23.295 -20.959 1.262   1.00 17.04 ?  446 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 18.501 4.949   -15.059 1.00 51.61 ?  447 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 18.493 -16.096 16.397  1.00 36.48 ?  448 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 23.203 7.535   -3.189  1.00 33.97 ?  449 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 34.421 -8.079  -0.557  1.00 28.55 ?  450 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 9.472  -16.279 -2.068  1.00 49.36 ?  451 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 31.311 -12.776 -0.019  1.00 18.47 ?  452 HOH   A O    1 
HETATM 6806 O O    B HOH   E 4 .   ? 18.832 -2.849  -8.931  0.40 38.15 ?  453 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 30.542 14.749  2.857   1.00 19.71 ?  454 HOH   A O    1 
HETATM 6808 O O    A HOH   E 4 .   ? 16.238 2.938   -1.379  0.60 14.91 ?  455 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 29.804 -16.041 10.524  1.00 37.09 ?  456 HOH   A O    1 
HETATM 6810 O O    B HOH   E 4 .   ? 20.155 4.059   -2.111  0.40 32.65 ?  457 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 19.368 -11.091 24.151  1.00 65.01 ?  458 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 21.617 -14.735 18.051  1.00 49.91 ?  459 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 29.847 -2.057  -12.713 1.00 49.05 ?  460 HOH   A O    1 
HETATM 6814 O O    A HOH   E 4 .   ? 14.013 -0.363  3.517   0.60 43.66 ?  461 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 13.943 -10.285 -10.854 1.00 36.56 ?  462 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 27.780 7.059   -6.344  1.00 36.47 ?  463 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 11.958 -13.427 16.351  1.00 48.01 ?  464 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 25.428 8.239   -4.742  1.00 34.03 ?  465 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 24.855 5.526   20.818  1.00 54.12 ?  466 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 32.445 -15.990 10.845  1.00 41.51 ?  467 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 19.931 -17.319 -5.102  1.00 25.23 ?  468 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 24.645 14.533  7.862   1.00 36.02 ?  469 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 26.890 11.564  -1.254  1.00 31.30 ?  470 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? -1.784 -4.347  8.303   1.00 52.61 ?  471 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 23.224 -22.399 -3.390  1.00 33.75 ?  472 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 11.076 -14.983 -6.067  1.00 36.32 ?  473 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 23.467 13.699  5.576   1.00 20.63 ?  474 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 18.841 10.788  11.471  1.00 33.95 ?  475 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 21.944 5.211   -5.821  1.00 32.80 ?  476 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 27.569 -11.425 16.524  1.00 35.98 ?  477 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 15.760 -21.517 3.733   1.00 22.83 ?  478 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 39.593 -7.006  -3.477  1.00 47.54 ?  479 HOH   A O    1 
HETATM 6833 O O    B HOH   E 4 .   ? 14.968 0.938   -6.499  0.40 35.36 ?  480 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 12.388 1.573   17.370  1.00 42.73 ?  481 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 20.542 -16.124 -7.397  1.00 28.70 ?  482 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 18.198 -16.216 -8.745  1.00 42.53 ?  483 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 25.820 10.814  -3.704  1.00 25.66 ?  484 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 28.570 -4.710  -12.240 1.00 42.46 ?  485 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 35.186 7.432   12.342  1.00 51.52 ?  486 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 17.447 -18.728 19.857  1.00 48.66 ?  487 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 28.875 8.978   17.514  1.00 36.40 ?  488 HOH   A O    1 
HETATM 6842 O O    . HOH   E 4 .   ? 23.156 11.799  -4.018  1.00 21.35 ?  489 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 40.933 -4.015  -0.263  1.00 39.16 ?  490 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 15.730 -17.098 -7.009  1.00 33.43 ?  491 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 30.916 0.609   19.172  1.00 40.48 ?  492 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 28.648 -7.958  -15.267 1.00 49.98 ?  493 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 31.448 -0.566  -10.559 1.00 26.09 ?  494 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 16.891 -20.610 16.183  1.00 28.82 ?  495 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 41.600 9.218   -4.146  1.00 32.63 ?  496 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 16.144 -23.347 5.761   1.00 31.20 ?  497 HOH   A O    1 
HETATM 6851 O O    . HOH   E 4 .   ? 44.459 10.506  -1.565  1.00 32.90 ?  498 HOH   A O    1 
HETATM 6852 O O    . HOH   E 4 .   ? 23.359 -12.911 19.347  1.00 43.19 ?  499 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 39.158 2.368   7.552   1.00 34.71 ?  500 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 40.401 -0.231  -7.849  1.00 35.86 ?  501 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 20.013 -22.326 4.101   1.00 29.05 ?  502 HOH   A O    1 
HETATM 6856 O O    . HOH   E 4 .   ? 18.424 -23.242 1.911   1.00 41.53 ?  503 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 30.690 5.852   -14.633 1.00 43.79 ?  504 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 14.059 -25.390 8.894   1.00 31.59 ?  505 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 30.732 -5.790  -11.840 1.00 49.56 ?  506 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 37.426 -6.656  7.419   1.00 23.93 ?  507 HOH   A O    1 
HETATM 6861 O O    . HOH   E 4 .   ? 23.061 -23.731 1.668   1.00 30.34 ?  508 HOH   A O    1 
HETATM 6862 O O    B HOH   E 4 .   ? 14.605 7.774   4.985   0.40 28.33 ?  509 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 39.578 0.016   6.593   1.00 30.52 ?  510 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 37.992 13.890  6.773   1.00 56.24 ?  511 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 28.941 14.367  0.932   1.00 47.28 ?  512 HOH   A O    1 
HETATM 6866 O O    A HOH   E 4 .   ? 8.227  -3.078  -5.619  0.60 36.53 ?  513 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 22.030 -24.057 4.441   1.00 25.80 ?  514 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 36.470 -6.577  10.074  1.00 45.71 ?  515 HOH   A O    1 
HETATM 6869 O O    B HOH   E 4 .   ? 2.474  4.344   1.860   0.40 28.19 ?  516 HOH   A O    1 
HETATM 6870 O O    . HOH   E 4 .   ? 17.115 -7.119  -14.106 1.00 45.43 ?  517 HOH   A O    1 
HETATM 6871 O O    A HOH   E 4 .   ? 14.832 8.623   4.968   0.60 39.86 ?  518 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? 24.024 9.015   -7.174  1.00 37.50 ?  519 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 16.294 -21.232 18.740  1.00 44.19 ?  520 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 15.970 -12.423 27.539  1.00 43.74 ?  521 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 14.653 -22.804 19.898  1.00 40.65 ?  522 HOH   A O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 29.790 -22.429 5.404   1.00 21.25 ?  201 HOH   B O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 48.147 -6.863  15.580  1.00 39.09 ?  202 HOH   B O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 47.391 -7.508  -4.033  1.00 39.83 ?  203 HOH   B O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 37.904 -39.412 -0.186  1.00 38.45 ?  204 HOH   B O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 27.855 -41.853 -15.080 1.00 35.01 ?  205 HOH   B O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 41.450 -7.717  5.488   1.00 38.09 ?  206 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 56.282 -19.678 7.419   1.00 34.27 ?  207 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 59.114 -18.708 6.831   1.00 37.77 ?  208 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 49.390 -22.692 -19.724 1.00 51.47 ?  209 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 27.703 -29.206 -1.897  1.00 33.95 ?  210 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 35.940 -43.184 -8.650  1.00 28.03 ?  211 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 52.955 -13.377 -20.382 1.00 37.31 ?  212 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 41.939 -35.880 -17.438 1.00 30.18 ?  213 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 58.212 -13.019 8.386   1.00 34.48 ?  214 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 30.215 -41.003 -8.198  1.00 15.85 ?  215 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 55.392 -16.481 -14.319 1.00 35.32 ?  216 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 54.440 -9.326  -8.819  1.00 19.07 ?  217 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 50.267 -3.404  7.205   1.00 34.57 ?  218 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 57.685 -24.459 5.014   1.00 35.44 ?  219 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 39.327 -10.963 6.087   1.00 24.68 ?  220 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 29.678 -34.163 -0.451  1.00 34.82 ?  221 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 56.690 -30.751 -7.836  1.00 35.21 ?  222 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 44.401 -7.279  2.145   1.00 35.58 ?  223 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 37.196 -19.693 -18.092 1.00 37.48 ?  224 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 50.672 -6.119  0.231   1.00 26.50 ?  225 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 44.963 -43.466 -10.568 1.00 26.42 ?  226 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 45.175 -34.877 6.839   1.00 39.32 ?  227 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 34.535 -36.334 -7.244  1.00 17.07 ?  228 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 57.173 -26.809 -7.555  1.00 40.32 ?  229 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 57.384 -16.219 -12.180 1.00 19.48 ?  230 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 29.812 -26.324 3.855   1.00 28.84 ?  231 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 48.107 -24.506 -17.710 1.00 29.96 ?  232 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 28.416 -19.690 -13.095 1.00 25.54 ?  233 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 30.782 -28.742 4.190   1.00 24.25 ?  234 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 32.839 -43.767 -11.371 1.00 19.44 ?  235 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 51.684 -6.511  4.464   1.00 20.56 ?  236 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 50.691 -12.965 -0.463  1.00 12.48 ?  237 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 35.108 -8.005  -3.045  1.00 18.18 ?  238 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 42.528 -25.372 2.580   1.00 14.77 ?  239 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 43.108 -43.213 -8.262  1.00 28.92 ?  240 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 41.820 -23.543 9.268   1.00 16.09 ?  241 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 40.636 -15.991 14.188  1.00 25.81 ?  242 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 42.606 -22.879 3.831   1.00 11.91 ?  243 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 41.365 -9.643  13.063  1.00 23.01 ?  244 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 41.476 -39.093 -14.941 1.00 21.00 ?  245 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 44.496 -27.729 -0.732  1.00 23.14 ?  246 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 39.452 -11.128 0.328   1.00 17.38 ?  247 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 48.505 -36.494 -15.540 1.00 42.74 ?  248 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 51.541 -13.854 10.956  1.00 29.21 ?  249 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 46.377 -1.593  13.305  1.00 28.91 ?  250 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 49.346 -28.695 -6.956  1.00 15.15 ?  251 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 40.324 -12.764 -11.553 1.00 15.12 ?  252 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 43.227 -32.322 -17.120 1.00 21.93 ?  253 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 50.969 -39.936 -8.225  1.00 31.12 ?  254 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 25.437 -26.002 -1.413  1.00 30.77 ?  255 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 34.179 -18.555 11.383  1.00 23.19 ?  256 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 29.738 -25.216 -10.864 1.00 16.03 ?  257 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 30.867 -15.768 2.614   1.00 13.30 ?  258 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 57.563 -24.407 -3.845  1.00 22.18 ?  259 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 49.774 -0.574  10.320  1.00 30.01 ?  260 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 30.674 -42.173 -10.664 1.00 27.40 ?  261 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 33.485 -17.038 8.024   1.00 19.53 ?  262 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 38.430 -11.064 -2.246  1.00 19.32 ?  263 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 47.973 -22.771 5.812   1.00 17.59 ?  264 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 57.479 -9.234  1.462   1.00 20.29 ?  265 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 28.280 -34.338 -9.496  1.00 22.38 ?  266 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 34.911 -33.319 -19.247 1.00 28.17 ?  267 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 27.149 -31.813 -10.036 1.00 24.04 ?  268 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 56.929 -8.653  8.428   1.00 20.51 ?  269 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 43.361 -15.793 -12.186 1.00 14.15 ?  270 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 34.461 -12.810 2.552   1.00 22.72 ?  271 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 58.133 -10.565 -4.062  1.00 20.78 ?  272 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 34.851 -24.658 13.891  1.00 28.35 ?  273 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 42.311 -9.899  9.382   1.00 22.48 ?  274 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 42.196 -10.168 -14.947 1.00 35.10 ?  275 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 38.865 -12.036 12.389  1.00 33.66 ?  276 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 31.824 -17.988 -14.584 1.00 33.38 ?  277 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 56.182 -23.461 -14.702 1.00 26.67 ?  278 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 46.595 -31.264 -4.803  1.00 19.20 ?  279 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 57.145 -12.103 12.327  1.00 38.88 ?  280 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 57.617 -22.139 3.019   1.00 27.63 ?  281 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 27.621 -26.723 -15.683 1.00 33.66 ?  282 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 27.950 -22.868 -8.045  1.00 17.36 ?  283 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 48.384 -25.047 3.072   1.00 13.47 ?  284 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 28.484 -30.761 -14.805 1.00 30.05 ?  285 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 52.546 -10.472 12.985  1.00 22.61 ?  286 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 42.355 -34.687 3.724   1.00 24.97 ?  287 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 47.071 -34.000 -4.654  1.00 16.41 ?  288 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 41.156 -24.408 15.741  1.00 41.69 ?  289 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 48.690 -20.051 5.900   1.00 14.13 ?  290 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 36.790 -12.760 -1.536  1.00 26.88 ?  291 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 33.514 -15.325 -13.968 1.00 20.72 ?  292 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 45.432 -33.390 -15.919 1.00 21.97 ?  293 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 49.937 -24.667 5.764   1.00 34.50 ?  294 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 46.815 -29.531 9.802   1.00 30.48 ?  295 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 45.896 -40.400 -3.666  1.00 28.28 ?  296 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 51.239 -37.586 -9.551  1.00 25.00 ?  297 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 35.028 -33.563 4.434   1.00 26.10 ?  298 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 44.592 -27.468 1.948   1.00 14.92 ?  299 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 52.586 -35.637 -8.538  1.00 30.26 ?  300 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 37.311 -35.699 7.124   1.00 34.57 ?  301 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 39.408 -23.277 -20.275 1.00 33.22 ?  302 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 53.208 -16.111 -12.717 1.00 30.89 ?  303 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 42.680 -12.280 -18.504 1.00 31.24 ?  304 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 40.237 -10.822 -9.540  1.00 17.15 ?  305 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 25.958 -21.482 -3.570  1.00 15.98 ?  306 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 44.033 -29.333 -4.701  1.00 24.88 ?  307 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 41.122 -5.485  11.563  1.00 47.46 ?  308 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 37.529 -18.275 13.113  1.00 27.95 ?  309 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 53.416 -30.190 4.510   1.00 19.73 ?  310 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 42.878 -20.262 -20.781 1.00 39.16 ?  311 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 59.731 -15.375 8.209   1.00 31.42 ?  312 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 43.507 -15.419 18.265  1.00 32.75 ?  313 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 37.824 -10.264 -10.752 1.00 17.59 ?  314 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 32.799 -34.594 -5.959  1.00 16.34 ?  315 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 48.145 -32.639 -16.591 1.00 46.14 ?  316 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 41.639 -8.140  1.344   1.00 24.50 ?  317 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 52.570 -29.193 -13.018 1.00 22.71 ?  318 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 62.672 -13.604 4.705   1.00 27.47 ?  319 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 43.173 -21.447 10.654  1.00 15.93 ?  320 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 28.001 -14.810 -9.353  1.00 32.86 ?  321 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 62.861 -20.168 -0.888  1.00 40.27 ?  322 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 38.352 -12.847 7.884   1.00 18.87 ?  323 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 44.520 -24.654 9.558   1.00 18.81 ?  324 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 26.327 -21.031 -6.292  1.00 16.71 ?  325 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 51.418 -32.840 -10.717 1.00 36.58 ?  326 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 59.928 -17.162 -10.475 1.00 36.23 ?  327 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 38.317 -9.372  -13.254 1.00 27.60 ?  328 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 37.234 -30.571 -21.104 1.00 30.29 ?  329 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 36.691 -12.453 4.281   1.00 18.70 ?  330 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 33.592 -31.176 11.019  1.00 36.62 ?  331 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 51.648 -5.957  -7.890  1.00 48.99 ?  332 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 53.637 -12.527 -22.371 1.00 34.23 ?  333 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 42.947 -43.458 -14.383 1.00 43.31 ?  334 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 48.582 -11.892 -13.838 1.00 25.93 ?  335 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 47.071 -24.511 8.167   1.00 27.25 ?  336 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 44.191 -1.760  7.561   1.00 46.56 ?  337 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 43.065 -34.666 0.023   1.00 19.57 ?  338 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 47.444 -27.447 1.976   1.00 14.96 ?  339 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 45.787 -36.233 -16.183 1.00 34.74 ?  340 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 46.803 -19.913 12.234  1.00 31.87 ?  341 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 36.997 -15.011 -16.473 1.00 38.28 ?  342 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 37.085 -45.239 -9.832  1.00 36.43 ?  343 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 32.972 -14.678 0.993   1.00 17.30 ?  344 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 28.875 -42.946 -12.300 1.00 34.66 ?  345 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 39.797 -44.311 -11.235 1.00 37.14 ?  346 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 38.508 -22.383 15.049  1.00 41.45 ?  347 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 40.361 -43.432 -9.160  1.00 27.07 ?  348 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 55.575 -8.248  10.826  1.00 24.78 ?  349 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 38.479 -12.327 -16.228 1.00 42.29 ?  350 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 23.210 -23.697 6.774   1.00 36.94 ?  351 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 44.194 -37.364 -17.769 1.00 32.88 ?  352 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 33.784 -9.167  -8.809  1.00 31.61 ?  353 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 27.743 -26.646 -0.663  1.00 29.78 ?  354 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 36.196 -8.525  -9.669  1.00 33.61 ?  355 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 56.540 -7.274  3.115   1.00 30.24 ?  356 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 62.579 -20.151 -4.979  1.00 47.84 ?  357 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 34.070 -7.829  11.465  1.00 42.22 ?  358 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 43.055 -12.782 -21.233 1.00 39.75 ?  359 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 34.706 -10.304 7.382   1.00 24.69 ?  360 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 40.330 -8.725  9.910   1.00 46.88 ?  361 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 61.481 -19.893 1.592   1.00 33.23 ?  362 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 27.150 -26.052 -11.416 1.00 34.71 ?  363 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 56.916 -21.493 -16.437 1.00 45.34 ?  364 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 48.261 -26.583 8.868   1.00 38.90 ?  365 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 32.415 -23.641 14.062  1.00 42.99 ?  366 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 36.238 -8.806  8.935   1.00 37.60 ?  367 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 59.023 -10.505 9.167   1.00 44.05 ?  368 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 54.206 -5.740  2.920   1.00 36.72 ?  369 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 39.859 -6.992  7.900   1.00 45.22 ?  370 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 39.945 -11.436 -14.009 1.00 35.24 ?  371 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 56.038 -7.810  -0.521  1.00 35.65 ?  372 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 51.989 -12.981 13.363  1.00 32.50 ?  373 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 36.533 -22.789 13.291  1.00 24.76 ?  374 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 38.045 -10.642 10.043  1.00 31.45 ?  375 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 41.778 -9.911  -17.432 1.00 53.15 ?  376 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 62.980 -12.411 7.026   1.00 38.22 ?  377 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 41.777 -6.788  -4.871  1.00 48.84 ?  378 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 44.040 -5.608  -3.479  1.00 45.96 ?  379 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 40.180 -7.623  3.175   1.00 36.20 ?  380 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 52.811 -29.883 7.161   1.00 24.75 ?  381 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 39.740 -14.098 15.779  1.00 48.39 ?  382 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 60.450 -22.405 2.767   1.00 45.68 ?  383 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 42.576 -16.940 -23.272 1.00 42.66 ?  384 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 35.303 -33.719 7.165   1.00 39.13 ?  385 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 25.804 -18.784 -11.979 1.00 38.62 ?  386 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 35.296 -20.295 13.329  1.00 28.18 ?  387 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 23.909 -20.779 -7.772  1.00 28.18 ?  388 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 46.738 -5.399  3.024   1.00 42.87 ?  389 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 40.910 -9.795  15.808  1.00 46.50 ?  390 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 40.688 -6.637  -0.871  1.00 25.07 ?  391 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 43.966 -31.744 -3.892  1.00 28.77 ?  392 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 27.904 -27.057 2.218   1.00 35.34 ?  393 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 26.671 -27.990 -13.619 1.00 36.76 ?  394 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 34.403 -33.423 9.620   1.00 32.68 ?  395 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 45.717 -20.340 15.135  1.00 55.02 ?  396 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 24.593 -20.708 -10.451 1.00 40.71 ?  397 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 50.592 -30.736 8.634   1.00 26.53 ?  398 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 26.847 -30.651 -12.681 1.00 30.13 ?  399 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 57.537 -6.403  -2.363  1.00 34.49 ?  400 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 40.843 -11.850 -22.319 1.00 44.79 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6020 0.5927 0.6426 0.0212  -0.0143 0.0986  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6005 0.5928 0.6309 0.0172  -0.0116 0.0856  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5999 0.5910 0.6367 0.0198  -0.0136 0.0982  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5983 0.5910 0.6256 0.0163  -0.0113 0.0865  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5872 0.5826 0.6079 0.0141  -0.0146 0.1020  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5867 0.5828 0.6019 0.0120  -0.0131 0.0952  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5890 0.5841 0.6161 0.0164  -0.0161 0.1038  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5888 0.5845 0.6098 0.0137  -0.0143 0.0959  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6079 0.5958 0.6535 0.0228  -0.0111 0.0955  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6053 0.5957 0.6386 0.0187  -0.0089 0.0805  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6107 0.5974 0.6590 0.0234  -0.0102 0.0944  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6078 0.5973 0.6430 0.0192  -0.0081 0.0781  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6105 0.5974 0.6587 0.0239  -0.0095 0.0955  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6077 0.5973 0.6426 0.0196  -0.0076 0.0791  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5705 0.5710 0.5617 0.0058  -0.0131 0.1035  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5359 0.5449 0.4718 -0.0101 -0.0097 0.1105  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4906 0.5116 0.4179 -0.0258 0.0030  0.0919  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4901 0.5130 0.4000 -0.0270 0.0021  0.1012  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5442 0.5503 0.4307 -0.0099 -0.0185 0.1337  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5503 0.5521 0.3942 -0.0106 -0.0254 0.1555  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5542 0.5523 0.3819 -0.0111 -0.0271 0.1618  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5505 0.5518 0.3818 -0.0096 -0.0279 0.1669  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4437 0.4749 0.3803 -0.0406 0.0137  0.0623  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3959 0.4429 0.3448 -0.0544 0.0296  0.0301  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3414 0.3923 0.2940 -0.0599 0.0492  0.0039  5   SER   A C   
49   O O   . SER   A 5   ? 0.3474 0.4017 0.2924 -0.0470 0.0518  -0.0125 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4043 0.4530 0.3654 -0.0607 0.0261  0.0245  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4106 0.4585 0.3764 -0.0646 0.0286  0.0220  5   SER   A OG  
57   N N   A PHE   A 6   ? 0.3035 0.3561 0.2664 -0.0709 0.0642  0.0036  6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3145 0.3637 0.2755 -0.0681 0.0536  0.0022  6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2722 0.3227 0.2479 -0.0768 0.0719  0.0149  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.2912 0.3372 0.2601 -0.0729 0.0544  0.0081  6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2647 0.3201 0.2646 -0.0839 0.0828  0.0173  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.2844 0.3312 0.2726 -0.0782 0.0636  0.0057  6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2659 0.3272 0.2818 -0.0896 0.0761  0.0271  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.2853 0.3349 0.2831 -0.0829 0.0586  0.0124  6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2532 0.2955 0.2238 -0.0684 0.0690  0.0206  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2778 0.3182 0.2390 -0.0691 0.0475  0.0150  6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2375 0.2735 0.2117 -0.0600 0.0622  0.0163  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2664 0.3021 0.2266 -0.0658 0.0378  0.0160  6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2318 0.2645 0.2110 -0.0551 0.0524  0.0158  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2623 0.2954 0.2237 -0.0622 0.0302  0.0175  6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2378 0.2689 0.2273 -0.0482 0.0530  0.0029  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2651 0.2980 0.2324 -0.0606 0.0308  0.0114  6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2285 0.2594 0.2149 -0.0549 0.0516  0.0147  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2602 0.2918 0.2262 -0.0617 0.0275  0.0183  6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2353 0.2647 0.2332 -0.0467 0.0504  0.0031  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2626 0.2947 0.2345 -0.0589 0.0274  0.0121  6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2340 0.2614 0.2251 -0.0506 0.0497  0.0072  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2622 0.2923 0.2304 -0.0599 0.0262  0.0141  6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2573 0.3114 0.2586 -0.0787 0.0997  0.0115  7   SER   A N   
98   N N   B SER   A 7   ? 0.2769 0.3217 0.2731 -0.0745 0.0761  -0.0019 7   SER   A N   
99   C CA  A SER   A 7   ? 0.2623 0.3136 0.2737 -0.0646 0.0977  -0.0022 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2754 0.3167 0.2816 -0.0666 0.0811  -0.0123 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2424 0.2891 0.2743 -0.0587 0.1020  0.0048  7   SER   A C   
102  C C   B SER   A 7   ? 0.2570 0.3007 0.2704 -0.0621 0.0939  -0.0088 7   SER   A C   
103  O O   A SER   A 7   ? 0.2486 0.2806 0.2832 -0.0591 0.0985  0.0099  7   SER   A O   
104  O O   B SER   A 7   ? 0.2553 0.2959 0.2767 -0.0643 0.1008  -0.0078 7   SER   A O   
105  C CB  A SER   A 7   ? 0.2854 0.3349 0.2938 -0.0526 0.0927  -0.0100 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2892 0.3252 0.2987 -0.0649 0.0764  -0.0194 7   SER   A CB  
107  O OG  A SER   A 7   ? 0.3030 0.3484 0.3203 -0.0440 0.0855  -0.0157 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2988 0.3317 0.3198 -0.0617 0.0725  -0.0272 7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2282 0.2756 0.2881 -0.0521 0.0844  -0.0013 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2455 0.2917 0.2624 -0.0554 0.0930  -0.0067 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.2150 0.2584 0.2898 -0.0418 0.0748  0.0080  8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2340 0.2803 0.2597 -0.0474 0.0858  0.0043  8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1976 0.2422 0.2748 -0.0303 0.0544  0.0102  8   GLY   A C   
124  C C   B GLY   A 8   ? 0.2189 0.2669 0.2496 -0.0406 0.0747  0.0159  8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1972 0.2400 0.2756 -0.0118 0.0557  0.0030  8   GLY   A O   
126  O O   B GLY   A 8   ? 0.2194 0.2669 0.2612 -0.0374 0.0750  0.0208  8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1762 0.2253 0.2450 -0.0280 0.0483  0.0207  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.2031 0.2495 0.2361 -0.0338 0.0629  0.0239  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1534 0.2024 0.2256 -0.0317 0.0364  0.0221  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1917 0.2289 0.2277 -0.0267 0.0436  0.0264  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1454 0.1897 0.2296 -0.0282 0.0373  0.0437  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1896 0.2107 0.2222 -0.0247 0.0283  0.0381  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1491 0.2149 0.2507 -0.0282 0.0429  0.0445  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1935 0.2175 0.2268 -0.0185 0.0083  0.0560  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1431 0.1964 0.2215 -0.0279 0.0266  0.0023  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1841 0.2274 0.2228 -0.0186 0.0412  0.0175  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1528 0.1892 0.2354 -0.0154 0.0402  -0.0070 9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1747 0.2198 0.2099 -0.0162 0.0476  0.0136  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1619 0.1861 0.2523 -0.0194 0.0470  -0.0111 9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.1789 0.2164 0.2154 -0.0200 0.0525  0.0123  9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1565 0.1776 0.2297 -0.0096 0.0387  0.0018  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1697 0.2114 0.1969 -0.0096 0.0482  0.0196  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1644 0.1861 0.2662 -0.0127 0.0472  -0.0119 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.1749 0.2085 0.2190 -0.0195 0.0539  0.0085  9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1601 0.1800 0.2456 -0.0077 0.0430  -0.0081 9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1653 0.2083 0.2014 -0.0081 0.0536  0.0136  9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1631 0.1802 0.2642 -0.0208 0.0530  -0.0041 9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1624 0.2049 0.2109 -0.0141 0.0634  0.0134  9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1757 0.1820 0.2837 -0.0217 0.0534  -0.0053 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.1586 0.2049 0.2231 -0.0145 0.0667  0.0210  9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1466 0.1712 0.2253 -0.0245 0.0342  0.0386  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1819 0.1947 0.2119 -0.0280 0.0334  0.0277  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1407 0.1672 0.2355 -0.0237 0.0267  0.0522  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1748 0.1881 0.2088 -0.0300 0.0306  0.0178  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1340 0.1617 0.2192 -0.0181 0.0208  0.0453  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1623 0.1732 0.1928 -0.0314 0.0245  0.0178  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1404 0.1614 0.2320 -0.0177 0.0428  0.0498  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1642 0.1683 0.1883 -0.0307 0.0438  0.0229  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1415 0.1743 0.2745 -0.0297 0.0077  0.0660  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1825 0.1956 0.2349 -0.0359 0.0229  0.0260  10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1553 0.1829 0.3219 -0.0338 -0.0301 0.0726  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1973 0.2103 0.2708 -0.0306 0.0135  0.0310  10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.1686 0.1953 0.3511 -0.0285 -0.0234 0.0691  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.2001 0.2183 0.2898 -0.0243 0.0142  0.0295  10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.1670 0.1936 0.3347 -0.0358 -0.0305 0.0646  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.2039 0.2169 0.2798 -0.0347 0.0157  0.0342  10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1385 0.1574 0.2073 -0.0154 0.0199  0.0331  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1555 0.1611 0.1829 -0.0356 0.0114  0.0194  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1392 0.1528 0.2187 -0.0238 0.0166  0.0329  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1556 0.1499 0.1878 -0.0340 0.0107  0.0270  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1379 0.1523 0.2168 -0.0164 0.0290  0.0183  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1424 0.1355 0.1822 -0.0300 0.0171  0.0179  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1400 0.1730 0.2541 -0.0333 0.0433  -0.0077 11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1336 0.1332 0.2011 -0.0310 0.0232  -0.0087 11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1462 0.1543 0.2183 -0.0249 0.0116  0.0362  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1707 0.1481 0.1964 -0.0305 0.0062  0.0402  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1589 0.1631 0.2265 -0.0248 0.0128  0.0352  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1846 0.1544 0.2048 -0.0263 0.0144  0.0481  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1659 0.1628 0.2220 -0.0310 0.0008  0.0352  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1912 0.1594 0.2122 -0.0235 0.0170  0.0527  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1779 0.1607 0.2024 -0.0259 -0.0064 0.0340  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1963 0.1643 0.1977 -0.0183 0.0206  0.0619  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1798 0.1525 0.2111 -0.0155 -0.0086 0.0150  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1947 0.1640 0.1904 -0.0090 0.0206  0.0629  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1366 0.1374 0.1929 -0.0161 0.0215  0.0164  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1352 0.1465 0.1803 -0.0167 0.0133  0.0173  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1412 0.1444 0.1987 -0.0182 0.0154  0.0236  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1350 0.1562 0.1816 -0.0141 0.0091  0.0148  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1402 0.1496 0.2033 -0.0219 0.0082  0.0234  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1278 0.1530 0.1755 -0.0146 0.0097  0.0124  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1422 0.1502 0.2000 -0.0163 0.0203  0.0180  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1379 0.1527 0.1633 -0.0110 -0.0031 0.0132  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1525 0.1383 0.2119 -0.0186 0.0067  0.0328  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1440 0.1602 0.1865 -0.0119 0.0168  0.0114  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1620 0.1482 0.2206 -0.0048 0.0166  0.0386  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1422 0.1581 0.1955 -0.0127 0.0227  0.0101  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1749 0.1491 0.2302 0.0103  0.0238  0.0460  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1430 0.1618 0.2124 -0.0064 0.0274  0.0134  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1666 0.1622 0.2284 0.0058  0.0143  0.0283  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1418 0.1623 0.1953 -0.0145 0.0148  -0.0057 12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1375 0.1486 0.2185 -0.0216 0.0017  0.0198  13  THR   A N   
296  N N   B THR   A 13  ? 0.1197 0.1460 0.1858 -0.0123 0.0111  0.0035  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1418 0.1491 0.2244 -0.0179 0.0146  0.0198  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1280 0.1457 0.1917 -0.0150 0.0160  0.0094  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1409 0.1435 0.2247 -0.0144 0.0170  0.0209  13  THR   A C   
300  C C   B THR   A 13  ? 0.1354 0.1486 0.1916 -0.0193 0.0210  0.0121  13  THR   A C   
301  O O   A THR   A 13  ? 0.1425 0.1367 0.2264 -0.0103 0.0189  0.0172  13  THR   A O   
302  O O   B THR   A 13  ? 0.1419 0.1493 0.1999 -0.0151 0.0116  0.0085  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1498 0.1571 0.2427 -0.0176 0.0127  0.0213  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1229 0.1573 0.2014 -0.0060 0.0137  0.0112  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1577 0.1403 0.2576 -0.0186 0.0001  0.0297  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1114 0.1551 0.2084 -0.0049 0.0224  0.0209  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1597 0.1783 0.2568 -0.0191 0.0154  0.0118  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1367 0.1730 0.2084 -0.0044 0.0084  0.0054  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1447 0.1440 0.2257 -0.0144 0.0183  0.0219  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1392 0.1506 0.1970 -0.0245 0.0207  0.0228  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1450 0.1576 0.2350 -0.0050 0.0080  0.0372  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1495 0.1596 0.2137 -0.0217 0.0059  0.0367  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1514 0.1535 0.2201 -0.0114 -0.0066 0.0472  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1483 0.1560 0.2044 -0.0224 -0.0055 0.0466  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1640 0.1588 0.2166 -0.0172 -0.0122 0.0483  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1580 0.1569 0.2121 -0.0261 -0.0117 0.0593  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1552 0.1893 0.2908 -0.0092 0.0194  0.0476  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.1653 0.1749 0.2614 -0.0232 0.0002  0.0384  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1796 0.2385 0.3563 -0.0196 0.0211  0.0539  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.1766 0.2100 0.3080 -0.0195 -0.0004 0.0450  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.1978 0.2580 0.3784 -0.0006 0.0099  0.0543  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.1773 0.2191 0.3197 -0.0041 -0.0009 0.0546  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.2042 0.2709 0.3892 -0.0259 0.0229  0.0462  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.1869 0.2385 0.3364 -0.0232 -0.0092 0.0376  14  ASP   A OD2 
347  N N   A ASN   A 15  ? 0.1450 0.1513 0.2204 -0.0195 -0.0010 0.0458  15  ASN   A N   
348  N N   B ASN   A 15  ? 0.1428 0.1555 0.2046 -0.0247 0.0013  0.0403  15  ASN   A N   
349  C CA  A ASN   A 15  ? 0.1440 0.1547 0.2263 -0.0192 -0.0104 0.0369  15  ASN   A CA  
350  C CA  B ASN   A 15  ? 0.1419 0.1598 0.2139 -0.0252 -0.0010 0.0229  15  ASN   A CA  
351  C C   A ASN   A 15  ? 0.1369 0.1503 0.2098 -0.0219 0.0011  0.0317  15  ASN   A C   
352  C C   B ASN   A 15  ? 0.1379 0.1636 0.2216 -0.0200 0.0143  0.0240  15  ASN   A C   
353  O O   A ASN   A 15  ? 0.1305 0.1416 0.2046 -0.0194 0.0099  0.0266  15  ASN   A O   
354  O O   B ASN   A 15  ? 0.1316 0.1671 0.2301 -0.0179 0.0352  0.0164  15  ASN   A O   
355  C CB  A ASN   A 15  ? 0.1430 0.1571 0.2329 -0.0126 -0.0071 0.0446  15  ASN   A CB  
356  C CB  B ASN   A 15  ? 0.1417 0.1569 0.2082 -0.0282 -0.0051 0.0087  15  ASN   A CB  
357  C CG  A ASN   A 15  ? 0.1337 0.1553 0.2394 -0.0056 0.0035  0.0409  15  ASN   A CG  
358  C CG  B ASN   A 15  ? 0.1446 0.1608 0.2140 -0.0262 -0.0039 0.0020  15  ASN   A CG  
359  O OD1 A ASN   A 15  ? 0.1476 0.1637 0.2503 -0.0183 0.0002  0.0422  15  ASN   A OD1 
360  O OD1 B ASN   A 15  ? 0.1546 0.1673 0.2218 -0.0330 -0.0070 -0.0028 15  ASN   A OD1 
361  N ND2 A ASN   A 15  ? 0.1371 0.1609 0.2344 -0.0085 0.0198  0.0450  15  ASN   A ND2 
362  N ND2 B ASN   A 15  ? 0.1464 0.1671 0.2094 -0.0326 -0.0038 0.0017  15  ASN   A ND2 
375  N N   A VAL   A 16  ? 0.1375 0.1434 0.2053 -0.0164 0.0058  0.0336  16  VAL   A N   
376  N N   B VAL   A 16  ? 0.1396 0.1589 0.2137 -0.0116 0.0143  0.0362  16  VAL   A N   
377  C CA  A VAL   A 16  ? 0.1337 0.1438 0.2106 -0.0152 0.0013  0.0305  16  VAL   A CA  
378  C CA  B VAL   A 16  ? 0.1394 0.1588 0.1976 -0.0058 0.0216  0.0416  16  VAL   A CA  
379  C C   A VAL   A 16  ? 0.1287 0.1441 0.2070 -0.0215 0.0031  0.0278  16  VAL   A C   
380  C C   B VAL   A 16  ? 0.1386 0.1589 0.1867 -0.0091 0.0196  0.0400  16  VAL   A C   
381  O O   A VAL   A 16  ? 0.1204 0.1449 0.2007 -0.0236 0.0159  0.0185  16  VAL   A O   
382  O O   B VAL   A 16  ? 0.1377 0.1599 0.1931 -0.0064 0.0254  0.0376  16  VAL   A O   
383  C CB  A VAL   A 16  ? 0.1454 0.1578 0.2211 -0.0042 0.0207  0.0338  16  VAL   A CB  
384  C CB  B VAL   A 16  ? 0.1470 0.1643 0.1995 0.0019  0.0385  0.0414  16  VAL   A CB  
385  C CG1 A VAL   A 16  ? 0.1540 0.1670 0.2211 0.0010  0.0257  0.0474  16  VAL   A CG1 
386  C CG1 B VAL   A 16  ? 0.1574 0.1687 0.1991 0.0111  0.0350  0.0461  16  VAL   A CG1 
387  C CG2 A VAL   A 16  ? 0.1528 0.1714 0.2308 -0.0005 0.0311  0.0233  16  VAL   A CG2 
388  C CG2 B VAL   A 16  ? 0.1482 0.1737 0.2198 -0.0011 0.0490  0.0403  16  VAL   A CG2 
407  N N   A TYR   A 17  ? 0.1321 0.1420 0.2164 -0.0215 0.0063  0.0281  17  TYR   A N   
408  N N   B TYR   A 17  ? 0.1405 0.1517 0.1733 -0.0181 0.0210  0.0322  17  TYR   A N   
409  C CA  A TYR   A 17  ? 0.1349 0.1463 0.1998 -0.0172 0.0082  0.0168  17  TYR   A CA  
410  C CA  B TYR   A 17  ? 0.1432 0.1525 0.1573 -0.0292 0.0120  0.0270  17  TYR   A CA  
411  C C   A TYR   A 17  ? 0.1413 0.1406 0.2019 -0.0145 0.0176  0.0148  17  TYR   A C   
412  C C   B TYR   A 17  ? 0.1378 0.1525 0.1474 -0.0244 0.0092  0.0310  17  TYR   A C   
413  O O   A TYR   A 17  ? 0.1350 0.1355 0.1974 -0.0180 0.0271  0.0190  17  TYR   A O   
414  O O   B TYR   A 17  ? 0.1293 0.1513 0.1481 -0.0274 0.0070  0.0274  17  TYR   A O   
415  C CB  A TYR   A 17  ? 0.1450 0.1623 0.1922 -0.0153 0.0050  0.0271  17  TYR   A CB  
416  C CB  B TYR   A 17  ? 0.1607 0.1545 0.1636 -0.0356 0.0006  0.0284  17  TYR   A CB  
417  C CG  A TYR   A 17  ? 0.1642 0.1758 0.2057 -0.0159 0.0048  0.0222  17  TYR   A CG  
418  C CG  B TYR   A 17  ? 0.1811 0.1590 0.1669 -0.0447 -0.0056 0.0217  17  TYR   A CG  
419  C CD1 A TYR   A 17  ? 0.1759 0.1856 0.2193 -0.0030 -0.0064 0.0205  17  TYR   A CD1 
420  C CD1 B TYR   A 17  ? 0.1915 0.1648 0.1713 -0.0390 -0.0039 0.0299  17  TYR   A CD1 
421  C CD2 A TYR   A 17  ? 0.1712 0.1809 0.2067 -0.0184 0.0170  0.0287  17  TYR   A CD2 
422  C CD2 B TYR   A 17  ? 0.1918 0.1620 0.1630 -0.0520 -0.0038 0.0214  17  TYR   A CD2 
423  C CE1 A TYR   A 17  ? 0.1899 0.1912 0.2305 -0.0056 -0.0014 0.0239  17  TYR   A CE1 
424  C CE1 B TYR   A 17  ? 0.2019 0.1667 0.1746 -0.0430 -0.0080 0.0335  17  TYR   A CE1 
425  C CE2 A TYR   A 17  ? 0.1874 0.1867 0.2238 -0.0153 0.0183  0.0208  17  TYR   A CE2 
426  C CE2 B TYR   A 17  ? 0.2047 0.1654 0.1666 -0.0505 -0.0074 0.0175  17  TYR   A CE2 
427  C CZ  A TYR   A 17  ? 0.1959 0.1894 0.2274 -0.0070 0.0064  0.0276  17  TYR   A CZ  
428  C CZ  B TYR   A 17  ? 0.2101 0.1613 0.1647 -0.0475 -0.0150 0.0353  17  TYR   A CZ  
429  O OH  A TYR   A 17  ? 0.2062 0.1988 0.2429 -0.0035 0.0151  0.0247  17  TYR   A OH  
430  O OH  B TYR   A 17  ? 0.2230 0.1623 0.1717 -0.0469 -0.0242 0.0357  17  TYR   A OH  
449  N N   A ILE   A 18  ? 0.1485 0.1422 0.2030 -0.0138 0.0288  0.0225  18  ILE   A N   
450  N N   B ILE   A 18  ? 0.1327 0.1485 0.1482 -0.0238 0.0178  0.0350  18  ILE   A N   
451  C CA  A ILE   A 18  ? 0.1536 0.1443 0.2045 -0.0160 0.0340  0.0123  18  ILE   A CA  
452  C CA  B ILE   A 18  ? 0.1341 0.1454 0.1471 -0.0165 0.0259  0.0158  18  ILE   A CA  
453  C C   A ILE   A 18  ? 0.1556 0.1527 0.2180 -0.0244 0.0387  0.0176  18  ILE   A C   
454  C C   B ILE   A 18  ? 0.1368 0.1569 0.1457 -0.0164 0.0173  0.0048  18  ILE   A C   
455  O O   A ILE   A 18  ? 0.1527 0.1696 0.2117 -0.0265 0.0523  0.0252  18  ILE   A O   
456  O O   B ILE   A 18  ? 0.1375 0.1685 0.1424 -0.0261 0.0227  0.0039  18  ILE   A O   
457  C CB  A ILE   A 18  ? 0.1636 0.1468 0.1867 -0.0074 0.0262  0.0222  18  ILE   A CB  
458  C CB  B ILE   A 18  ? 0.1392 0.1375 0.1304 -0.0077 0.0292  0.0185  18  ILE   A CB  
459  C CG1 A ILE   A 18  ? 0.1730 0.1521 0.1898 0.0014  0.0077  0.0124  18  ILE   A CG1 
460  C CG1 B ILE   A 18  ? 0.1493 0.1453 0.1295 -0.0148 0.0139  0.0259  18  ILE   A CG1 
461  C CG2 A ILE   A 18  ? 0.1631 0.1422 0.1893 -0.0014 0.0319  0.0063  18  ILE   A CG2 
462  C CG2 B ILE   A 18  ? 0.1483 0.1439 0.1429 -0.0100 0.0393  0.0145  18  ILE   A CG2 
463  C CD1 A ILE   A 18  ? 0.1932 0.1612 0.2176 0.0095  0.0014  0.0068  18  ILE   A CD1 
464  C CD1 B ILE   A 18  ? 0.1695 0.1595 0.1405 -0.0109 0.0018  0.0128  18  ILE   A CD1 
487  N N   A LYS   A 19  ? 0.1577 0.1531 0.2286 -0.0256 0.0516  0.0244  19  LYS   A N   
488  N N   B LYS   A 19  ? 0.1417 0.1601 0.1532 -0.0106 0.0228  0.0032  19  LYS   A N   
489  C CA  A LYS   A 19  ? 0.1593 0.1623 0.2446 -0.0179 0.0472  0.0277  19  LYS   A CA  
490  C CA  B LYS   A 19  ? 0.1559 0.1706 0.1784 -0.0028 0.0373  -0.0032 19  LYS   A CA  
491  C C   A LYS   A 19  ? 0.1459 0.1621 0.2674 -0.0087 0.0461  0.0413  19  LYS   A C   
492  C C   B LYS   A 19  ? 0.1601 0.1710 0.2018 0.0061  0.0415  0.0064  19  LYS   A C   
493  O O   A LYS   A 19  ? 0.1397 0.1623 0.2551 -0.0170 0.0414  0.0361  19  LYS   A O   
494  O O   B LYS   A 19  ? 0.1649 0.1706 0.1972 0.0053  0.0385  0.0124  19  LYS   A O   
495  C CB  A LYS   A 19  ? 0.1754 0.1738 0.2487 -0.0197 0.0454  0.0144  19  LYS   A CB  
496  C CB  B LYS   A 19  ? 0.1633 0.1842 0.1717 -0.0037 0.0518  -0.0163 19  LYS   A CB  
497  C CG  A LYS   A 19  ? 0.2030 0.1886 0.2541 -0.0174 0.0487  -0.0054 19  LYS   A CG  
498  C CG  B LYS   A 19  ? 0.1875 0.1995 0.1834 -0.0054 0.0538  -0.0226 19  LYS   A CG  
499  C CD  A LYS   A 19  ? 0.2233 0.2000 0.2590 -0.0120 0.0569  -0.0138 19  LYS   A CD  
500  C CD  B LYS   A 19  ? 0.2086 0.2098 0.2004 -0.0079 0.0542  -0.0249 19  LYS   A CD  
501  C CE  A LYS   A 19  ? 0.2374 0.2059 0.2653 -0.0069 0.0660  -0.0302 19  LYS   A CE  
502  C CE  B LYS   A 19  ? 0.2223 0.2211 0.2133 -0.0116 0.0517  -0.0248 19  LYS   A CE  
503  N NZ  A LYS   A 19  ? 0.2482 0.2099 0.2579 -0.0083 0.0790  -0.0435 19  LYS   A NZ  
504  N NZ  B LYS   A 19  ? 0.2309 0.2217 0.2184 -0.0169 0.0566  -0.0294 19  LYS   A NZ  
531  N N   A ASN   A 20  ? 0.1507 0.1702 0.3047 -0.0036 0.0557  0.0569  20  ASN   A N   
532  N N   B ASN   A 20  ? 0.1720 0.1791 0.2296 0.0089  0.0551  0.0051  20  ASN   A N   
533  C CA  A ASN   A 20  ? 0.1605 0.1877 0.3372 0.0153  0.0648  0.0531  20  ASN   A CA  
534  C CA  B ASN   A 20  ? 0.1840 0.1944 0.2503 0.0151  0.0631  -0.0006 20  ASN   A CA  
535  C C   A ASN   A 20  ? 0.1775 0.1870 0.3492 0.0118  0.0733  0.0452  20  ASN   A C   
536  C C   B ASN   A 20  ? 0.1976 0.1964 0.2611 0.0089  0.0690  -0.0029 20  ASN   A C   
537  O O   A ASN   A 20  ? 0.1906 0.1901 0.3665 0.0008  0.0777  0.0334  20  ASN   A O   
538  O O   B ASN   A 20  ? 0.2087 0.2024 0.2702 -0.0054 0.0699  -0.0123 20  ASN   A O   
539  C CB  A ASN   A 20  ? 0.1634 0.2077 0.3630 0.0222  0.0633  0.0659  20  ASN   A CB  
540  C CB  B ASN   A 20  ? 0.1890 0.2064 0.2667 0.0216  0.0574  0.0039  20  ASN   A CB  
541  C CG  A ASN   A 20  ? 0.1704 0.2201 0.3933 0.0337  0.0649  0.0701  20  ASN   A CG  
542  C CG  B ASN   A 20  ? 0.1941 0.2123 0.2819 0.0293  0.0520  0.0071  20  ASN   A CG  
543  O OD1 A ASN   A 20  ? 0.1885 0.2320 0.4175 0.0433  0.0712  0.0588  20  ASN   A OD1 
544  O OD1 B ASN   A 20  ? 0.2038 0.2183 0.2855 0.0263  0.0337  0.0061  20  ASN   A OD1 
545  N ND2 A ASN   A 20  ? 0.1787 0.2178 0.4103 0.0290  0.0565  0.0760  20  ASN   A ND2 
546  N ND2 B ASN   A 20  ? 0.1953 0.2116 0.2883 0.0366  0.0550  0.0065  20  ASN   A ND2 
559  N N   A ALA   A 21  ? 0.1795 0.1896 0.3449 0.0070  0.0607  0.0401  21  ALA   A N   
560  N N   B ALA   A 21  ? 0.2014 0.1969 0.2712 0.0097  0.0591  -0.0014 21  ALA   A N   
561  C CA  A ALA   A 21  ? 0.1837 0.1890 0.3336 -0.0021 0.0558  0.0347  21  ALA   A CA  
562  C CA  B ALA   A 21  ? 0.2051 0.1943 0.2717 0.0076  0.0563  -0.0000 21  ALA   A CA  
563  C C   A ALA   A 21  ? 0.1742 0.1893 0.3193 -0.0085 0.0462  0.0409  21  ALA   A C   
564  C C   B ALA   A 21  ? 0.1975 0.1878 0.2598 0.0120  0.0644  0.0036  21  ALA   A C   
565  O O   A ALA   A 21  ? 0.1677 0.1899 0.3179 -0.0066 0.0350  0.0456  21  ALA   A O   
566  O O   B ALA   A 21  ? 0.1993 0.1856 0.2572 0.0187  0.0683  0.0025  21  ALA   A O   
567  C CB  A ALA   A 21  ? 0.2022 0.1974 0.3378 -0.0094 0.0517  0.0354  21  ALA   A CB  
568  C CB  B ALA   A 21  ? 0.2196 0.2034 0.2863 -0.0033 0.0430  0.0050  21  ALA   A CB  
579  N N   A ASP   A 22  ? 0.1762 0.1944 0.3142 -0.0164 0.0428  0.0371  22  ASP   A N   
580  N N   B ASP   A 22  ? 0.1920 0.1854 0.2633 0.0081  0.0644  0.0049  22  ASP   A N   
581  C CA  A ASP   A 22  ? 0.1775 0.1977 0.2943 -0.0136 0.0367  0.0303  22  ASP   A CA  
582  C CA  B ASP   A 22  ? 0.1888 0.1856 0.2575 0.0078  0.0651  -0.0010 22  ASP   A CA  
583  C C   A ASP   A 22  ? 0.1689 0.1972 0.2560 -0.0135 0.0412  0.0343  22  ASP   A C   
584  C C   B ASP   A 22  ? 0.1768 0.1713 0.2218 -0.0017 0.0671  0.0006  22  ASP   A C   
585  O O   A ASP   A 22  ? 0.1774 0.2023 0.2558 -0.0115 0.0535  0.0394  22  ASP   A O   
586  O O   B ASP   A 22  ? 0.1796 0.1690 0.2186 -0.0058 0.0652  -0.0032 22  ASP   A O   
587  C CB  A ASP   A 22  ? 0.1972 0.1982 0.3173 -0.0122 0.0406  0.0171  22  ASP   A CB  
588  C CB  B ASP   A 22  ? 0.1961 0.1956 0.2825 0.0153  0.0784  -0.0061 22  ASP   A CB  
589  C CG  A ASP   A 22  ? 0.2140 0.1948 0.3339 -0.0158 0.0346  0.0128  22  ASP   A CG  
590  C CG  B ASP   A 22  ? 0.2066 0.1988 0.2981 0.0173  0.0913  -0.0002 22  ASP   A CG  
591  O OD1 A ASP   A 22  ? 0.2110 0.1898 0.3400 -0.0342 0.0160  0.0306  22  ASP   A OD1 
592  O OD1 B ASP   A 22  ? 0.2077 0.1898 0.2895 0.0143  0.0987  0.0110  22  ASP   A OD1 
593  O OD2 A ASP   A 22  ? 0.2318 0.2070 0.3557 -0.0084 0.0455  -0.0028 22  ASP   A OD2 
594  O OD2 B ASP   A 22  ? 0.2155 0.2173 0.3163 0.0197  0.0959  -0.0008 22  ASP   A OD2 
603  N N   A ILE   A 23  ? 0.1726 0.1960 0.2300 -0.0125 0.0406  0.0299  23  ILE   A N   
604  N N   B ILE   A 23  ? 0.1687 0.1688 0.2084 0.0021  0.0622  0.0083  23  ILE   A N   
605  C CA  A ILE   A 23  ? 0.1712 0.1883 0.1996 -0.0068 0.0348  0.0314  23  ILE   A CA  
606  C CA  B ILE   A 23  ? 0.1653 0.1696 0.2042 -0.0016 0.0424  0.0122  23  ILE   A CA  
607  C C   A ILE   A 23  ? 0.1687 0.1920 0.1894 0.0026  0.0439  0.0214  23  ILE   A C   
608  C C   B ILE   A 23  ? 0.1668 0.1730 0.2110 -0.0107 0.0430  0.0034  23  ILE   A C   
609  O O   A ILE   A 23  ? 0.1733 0.1824 0.1811 0.0097  0.0422  0.0101  23  ILE   A O   
610  O O   B ILE   A 23  ? 0.1657 0.1688 0.2086 -0.0141 0.0472  -0.0049 23  ILE   A O   
611  C CB  A ILE   A 23  ? 0.1838 0.1804 0.1861 -0.0068 0.0250  0.0225  23  ILE   A CB  
612  C CB  B ILE   A 23  ? 0.1609 0.1639 0.1892 0.0033  0.0383  0.0170  23  ILE   A CB  
613  C CG1 A ILE   A 23  ? 0.1869 0.1821 0.1789 -0.0107 0.0269  0.0121  23  ILE   A CG1 
614  C CG1 B ILE   A 23  ? 0.1632 0.1611 0.1808 0.0001  0.0265  0.0099  23  ILE   A CG1 
615  C CG2 A ILE   A 23  ? 0.1883 0.1776 0.1831 -0.0077 0.0248  0.0241  23  ILE   A CG2 
616  C CG2 B ILE   A 23  ? 0.1609 0.1664 0.1949 0.0110  0.0373  0.0244  23  ILE   A CG2 
617  C CD1 A ILE   A 23  ? 0.1808 0.1777 0.1752 -0.0129 0.0210  0.0041  23  ILE   A CD1 
618  C CD1 B ILE   A 23  ? 0.1595 0.1576 0.1828 0.0018  0.0178  0.0077  23  ILE   A CD1 
641  N N   A VAL   A 24  ? 0.1735 0.2004 0.2078 -0.0021 0.0351  0.0227  24  VAL   A N   
642  N N   B VAL   A 24  ? 0.1712 0.1820 0.2323 -0.0149 0.0385  0.0069  24  VAL   A N   
643  C CA  A VAL   A 24  ? 0.1866 0.2044 0.2322 -0.0079 0.0298  0.0193  24  VAL   A CA  
644  C CA  B VAL   A 24  ? 0.1858 0.1947 0.2471 -0.0127 0.0405  0.0105  24  VAL   A CA  
645  C C   A VAL   A 24  ? 0.1961 0.2171 0.2359 -0.0160 0.0340  0.0147  24  VAL   A C   
646  C C   B VAL   A 24  ? 0.1948 0.2065 0.2508 -0.0138 0.0531  -0.0016 24  VAL   A C   
647  O O   A VAL   A 24  ? 0.2030 0.2163 0.2311 -0.0178 0.0353  0.0193  24  VAL   A O   
648  O O   B VAL   A 24  ? 0.1941 0.2091 0.2624 -0.0080 0.0556  -0.0063 24  VAL   A O   
649  C CB  A VAL   A 24  ? 0.1896 0.2107 0.2589 -0.0115 0.0286  0.0285  24  VAL   A CB  
650  C CB  B VAL   A 24  ? 0.1865 0.1945 0.2559 -0.0111 0.0354  0.0259  24  VAL   A CB  
651  C CG1 A VAL   A 24  ? 0.1942 0.2131 0.2709 -0.0072 0.0217  0.0203  24  VAL   A CG1 
652  C CG1 B VAL   A 24  ? 0.1913 0.1983 0.2682 -0.0107 0.0199  0.0228  24  VAL   A CG1 
653  C CG2 A VAL   A 24  ? 0.1938 0.2182 0.2733 -0.0135 0.0399  0.0363  24  VAL   A CG2 
654  C CG2 B VAL   A 24  ? 0.1885 0.1919 0.2528 -0.0047 0.0412  0.0357  24  VAL   A CG2 
673  N N   A GLU   A 25  ? 0.2048 0.2364 0.2455 -0.0231 0.0479  0.0010  25  GLU   A N   
674  N N   B GLU   A 25  ? 0.2046 0.2139 0.2485 -0.0174 0.0694  -0.0012 25  GLU   A N   
675  C CA  A GLU   A 25  ? 0.2266 0.2554 0.2540 -0.0219 0.0617  0.0024  25  GLU   A CA  
676  C CA  B GLU   A 25  ? 0.2236 0.2271 0.2498 -0.0204 0.0874  -0.0070 25  GLU   A CA  
677  C C   A GLU   A 25  ? 0.2131 0.2536 0.2283 -0.0243 0.0712  0.0026  25  GLU   A C   
678  C C   B GLU   A 25  ? 0.2178 0.2251 0.2211 -0.0194 0.0954  -0.0128 25  GLU   A C   
679  O O   A GLU   A 25  ? 0.2191 0.2595 0.2390 -0.0154 0.0717  -0.0029 25  GLU   A O   
680  O O   B GLU   A 25  ? 0.2232 0.2267 0.2199 -0.0138 0.0969  -0.0185 25  GLU   A O   
681  C CB  A GLU   A 25  ? 0.2548 0.2776 0.2859 -0.0217 0.0663  0.0097  25  GLU   A CB  
682  C CB  B GLU   A 25  ? 0.2435 0.2392 0.2692 -0.0233 0.1014  0.0001  25  GLU   A CB  
683  C CG  A GLU   A 25  ? 0.2840 0.2965 0.3336 -0.0260 0.0557  0.0109  25  GLU   A CG  
684  C CG  B GLU   A 25  ? 0.2660 0.2528 0.3021 -0.0229 0.0988  0.0013  25  GLU   A CG  
685  C CD  A GLU   A 25  ? 0.3033 0.3103 0.3768 -0.0345 0.0506  0.0153  25  GLU   A CD  
686  C CD  B GLU   A 25  ? 0.2850 0.2638 0.3350 -0.0260 0.0940  0.0047  25  GLU   A CD  
687  O OE1 A GLU   A 25  ? 0.3093 0.3137 0.3877 -0.0361 0.0428  0.0129  25  GLU   A OE1 
688  O OE1 B GLU   A 25  ? 0.2914 0.2665 0.3415 -0.0255 0.0919  0.0023  25  GLU   A OE1 
689  O OE2 A GLU   A 25  ? 0.3072 0.3171 0.4027 -0.0422 0.0515  0.0126  25  GLU   A OE2 
690  O OE2 B GLU   A 25  ? 0.2967 0.2696 0.3579 -0.0253 0.0948  0.0086  25  GLU   A OE2 
703  N N   A GLU   A 26  ? 0.2011 0.2466 0.2224 -0.0396 0.0745  0.0022  26  GLU   A N   
704  N N   B GLU   A 26  ? 0.2152 0.2202 0.2077 -0.0235 0.0911  -0.0172 26  GLU   A N   
705  C CA  A GLU   A 26  ? 0.2086 0.2484 0.2175 -0.0497 0.0696  0.0039  26  GLU   A CA  
706  C CA  B GLU   A 26  ? 0.2179 0.2152 0.1918 -0.0301 0.0957  -0.0146 26  GLU   A CA  
707  C C   A GLU   A 26  ? 0.2083 0.2383 0.2042 -0.0491 0.0597  0.0025  26  GLU   A C   
708  C C   B GLU   A 26  ? 0.2201 0.2146 0.1778 -0.0334 0.0897  -0.0162 26  GLU   A C   
709  O O   A GLU   A 26  ? 0.2121 0.2310 0.1970 -0.0487 0.0495  -0.0052 26  GLU   A O   
710  O O   B GLU   A 26  ? 0.2181 0.2119 0.1750 -0.0347 0.0892  -0.0204 26  GLU   A O   
711  C CB  A GLU   A 26  ? 0.2227 0.2568 0.2556 -0.0566 0.0624  0.0046  26  GLU   A CB  
712  C CB  B GLU   A 26  ? 0.2252 0.2234 0.2156 -0.0311 0.0872  -0.0184 26  GLU   A CB  
713  C CG  A GLU   A 26  ? 0.2400 0.2662 0.3009 -0.0606 0.0710  -0.0008 26  GLU   A CG  
714  C CG  B GLU   A 26  ? 0.2309 0.2328 0.2288 -0.0415 0.0956  -0.0152 26  GLU   A CG  
715  C CD  A GLU   A 26  ? 0.2550 0.2725 0.3300 -0.0714 0.0840  0.0043  26  GLU   A CD  
716  C CD  B GLU   A 26  ? 0.2385 0.2393 0.2327 -0.0539 0.1043  -0.0123 26  GLU   A CD  
717  O OE1 A GLU   A 26  ? 0.2537 0.2894 0.3480 -0.0663 0.1079  -0.0083 26  GLU   A OE1 
718  O OE1 B GLU   A 26  ? 0.2411 0.2536 0.2406 -0.0540 0.1154  -0.0182 26  GLU   A OE1 
719  O OE2 A GLU   A 26  ? 0.2709 0.2731 0.3247 -0.0722 0.0725  0.0116  26  GLU   A OE2 
720  O OE2 B GLU   A 26  ? 0.2411 0.2359 0.2116 -0.0589 0.1108  -0.0125 26  GLU   A OE2 
733  N N   A ALA   A 27  ? 0.1963 0.2288 0.1970 -0.0558 0.0532  -0.0026 27  ALA   A N   
734  N N   B ALA   A 27  ? 0.2223 0.2165 0.1746 -0.0370 0.0794  -0.0229 27  ALA   A N   
735  C CA  A ALA   A 27  ? 0.2056 0.2362 0.1987 -0.0566 0.0495  -0.0056 27  ALA   A CA  
736  C CA  B ALA   A 27  ? 0.2315 0.2282 0.1751 -0.0410 0.0762  -0.0284 27  ALA   A CA  
737  C C   A ALA   A 27  ? 0.2262 0.2573 0.2111 -0.0687 0.0578  -0.0224 27  ALA   A C   
738  C C   B ALA   A 27  ? 0.2546 0.2495 0.1953 -0.0439 0.0653  -0.0452 27  ALA   A C   
739  O O   A ALA   A 27  ? 0.2241 0.2544 0.2183 -0.0812 0.0447  -0.0251 27  ALA   A O   
740  O O   B ALA   A 27  ? 0.2579 0.2494 0.1951 -0.0453 0.0584  -0.0532 27  ALA   A O   
741  C CB  A ALA   A 27  ? 0.1985 0.2301 0.1998 -0.0543 0.0363  -0.0051 27  ALA   A CB  
742  C CB  B ALA   A 27  ? 0.2216 0.2234 0.1792 -0.0381 0.0770  -0.0230 27  ALA   A CB  
753  N N   A LYS   A 28  ? 0.2599 0.2817 0.2238 -0.0637 0.0551  -0.0527 28  LYS   A N   
754  N N   B LYS   A 28  ? 0.2799 0.2723 0.2170 -0.0466 0.0517  -0.0611 28  LYS   A N   
755  C CA  A LYS   A 28  ? 0.2979 0.3154 0.2531 -0.0572 0.0530  -0.0685 28  LYS   A CA  
756  C CA  B LYS   A 28  ? 0.3063 0.3041 0.2483 -0.0486 0.0417  -0.0602 28  LYS   A CA  
757  C C   A LYS   A 28  ? 0.3190 0.3463 0.2458 -0.0636 0.0683  -0.0609 28  LYS   A C   
758  C C   B LYS   A 28  ? 0.3247 0.3319 0.2557 -0.0589 0.0458  -0.0500 28  LYS   A C   
759  O O   A LYS   A 28  ? 0.3284 0.3532 0.2756 -0.0598 0.0521  -0.0623 28  LYS   A O   
760  O O   B LYS   A 28  ? 0.3307 0.3356 0.2700 -0.0573 0.0335  -0.0451 28  LYS   A O   
761  C CB  A LYS   A 28  ? 0.3161 0.3249 0.2911 -0.0382 0.0407  -0.0818 28  LYS   A CB  
762  C CB  B LYS   A 28  ? 0.3147 0.3100 0.2732 -0.0400 0.0316  -0.0655 28  LYS   A CB  
763  C CG  A LYS   A 28  ? 0.3322 0.3361 0.3345 -0.0236 0.0323  -0.0830 28  LYS   A CG  
764  C CG  B LYS   A 28  ? 0.3239 0.3179 0.3093 -0.0301 0.0223  -0.0664 28  LYS   A CG  
765  C CD  A LYS   A 28  ? 0.3457 0.3491 0.3814 -0.0145 0.0219  -0.0804 28  LYS   A CD  
766  C CD  B LYS   A 28  ? 0.3355 0.3274 0.3557 -0.0235 0.0114  -0.0637 28  LYS   A CD  
767  C CE  A LYS   A 28  ? 0.3544 0.3585 0.4130 -0.0084 0.0108  -0.0778 28  LYS   A CE  
768  C CE  B LYS   A 28  ? 0.3460 0.3348 0.3925 -0.0200 0.0051  -0.0635 28  LYS   A CE  
769  N NZ  A LYS   A 28  ? 0.3604 0.3627 0.4329 -0.0043 0.0082  -0.0737 28  LYS   A NZ  
770  N NZ  B LYS   A 28  ? 0.3517 0.3371 0.4132 -0.0183 0.0004  -0.0647 28  LYS   A NZ  
797  N N   A LYS   A 29  ? 0.3284 0.3686 0.2301 -0.0749 0.0992  -0.0429 29  LYS   A N   
798  N N   B LYS   A 29  ? 0.3357 0.3561 0.2632 -0.0705 0.0632  -0.0418 29  LYS   A N   
799  C CA  A LYS   A 29  ? 0.3468 0.3933 0.2460 -0.0812 0.1078  -0.0277 29  LYS   A CA  
800  C CA  B LYS   A 29  ? 0.3495 0.3795 0.2785 -0.0818 0.0733  -0.0323 29  LYS   A CA  
801  C C   A LYS   A 29  ? 0.3472 0.3917 0.2339 -0.0924 0.0983  -0.0262 29  LYS   A C   
802  C C   B LYS   A 29  ? 0.3473 0.3825 0.2469 -0.0944 0.0849  -0.0257 29  LYS   A C   
803  O O   A LYS   A 29  ? 0.3517 0.3973 0.2454 -0.0898 0.0932  -0.0233 29  LYS   A O   
804  O O   B LYS   A 29  ? 0.3479 0.3831 0.2468 -0.0963 0.0913  -0.0178 29  LYS   A O   
805  C CB  A LYS   A 29  ? 0.3600 0.4179 0.2883 -0.0749 0.1218  -0.0171 29  LYS   A CB  
806  C CB  B LYS   A 29  ? 0.3637 0.3985 0.3329 -0.0789 0.0704  -0.0286 29  LYS   A CB  
807  C CG  A LYS   A 29  ? 0.3736 0.4378 0.3459 -0.0676 0.1223  -0.0097 29  LYS   A CG  
808  C CG  B LYS   A 29  ? 0.3769 0.4145 0.3821 -0.0747 0.0683  -0.0278 29  LYS   A CG  
809  C CD  A LYS   A 29  ? 0.3873 0.4546 0.4035 -0.0605 0.1132  -0.0093 29  LYS   A CD  
810  C CD  B LYS   A 29  ? 0.3871 0.4281 0.4237 -0.0719 0.0658  -0.0280 29  LYS   A CD  
811  C CE  A LYS   A 29  ? 0.3967 0.4652 0.4422 -0.0547 0.1097  -0.0074 29  LYS   A CE  
812  C CE  B LYS   A 29  ? 0.3949 0.4373 0.4533 -0.0687 0.0654  -0.0281 29  LYS   A CE  
813  N NZ  A LYS   A 29  ? 0.4015 0.4714 0.4669 -0.0511 0.1063  -0.0066 29  LYS   A NZ  
814  N NZ  B LYS   A 29  ? 0.3990 0.4429 0.4714 -0.0671 0.0647  -0.0282 29  LYS   A NZ  
841  N N   . VAL   A 30  ? 0.3417 0.3818 0.2204 -0.1062 0.0982  -0.0209 30  VAL   A N   
842  C CA  . VAL   A 30  ? 0.3439 0.3747 0.2083 -0.1234 0.0831  -0.0105 30  VAL   A CA  
843  C C   . VAL   A 30  ? 0.3504 0.3606 0.1827 -0.1260 0.0702  -0.0034 30  VAL   A C   
844  O O   . VAL   A 30  ? 0.3600 0.3621 0.1897 -0.1280 0.0642  0.0062  30  VAL   A O   
845  C CB  . VAL   A 30  ? 0.3422 0.3771 0.2427 -0.1364 0.0640  -0.0087 30  VAL   A CB  
846  C CG1 . VAL   A 30  ? 0.3475 0.3795 0.2534 -0.1369 0.0487  -0.0020 30  VAL   A CG1 
847  C CG2 . VAL   A 30  ? 0.3418 0.3780 0.2697 -0.1418 0.0668  -0.0092 30  VAL   A CG2 
858  N N   . LYS   A 31  ? 0.3378 0.3374 0.1520 -0.1316 0.0654  -0.0160 31  LYS   A N   
859  C CA  . LYS   A 31  ? 0.3533 0.3327 0.1634 -0.1171 0.0388  -0.0165 31  LYS   A CA  
860  C C   . LYS   A 31  ? 0.3273 0.3075 0.1427 -0.0989 0.0196  0.0111  31  LYS   A C   
861  O O   . LYS   A 31  ? 0.3282 0.3172 0.1498 -0.0944 0.0044  0.0309  31  LYS   A O   
862  C CB  . LYS   A 31  ? 0.3972 0.3611 0.2684 -0.1117 0.0215  -0.0315 31  LYS   A CB  
863  C CG  . LYS   A 31  ? 0.4383 0.3955 0.3989 -0.1015 0.0007  -0.0357 31  LYS   A CG  
864  C CD  . LYS   A 31  ? 0.4728 0.4211 0.5044 -0.0930 -0.0170 -0.0393 31  LYS   A CD  
865  C CE  . LYS   A 31  ? 0.4977 0.4394 0.5750 -0.0850 -0.0311 -0.0431 31  LYS   A CE  
866  N NZ  . LYS   A 31  ? 0.5134 0.4457 0.6137 -0.0817 -0.0384 -0.0447 31  LYS   A NZ  
880  N N   . PRO   A 32  ? 0.2925 0.2714 0.1196 -0.0911 0.0204  0.0127  32  PRO   A N   
881  C CA  . PRO   A 32  ? 0.2812 0.2496 0.1504 -0.0849 0.0024  0.0278  32  PRO   A CA  
882  C C   . PRO   A 32  ? 0.2718 0.2443 0.1613 -0.0715 -0.0071 0.0315  32  PRO   A C   
883  O O   . PRO   A 32  ? 0.2650 0.2354 0.1654 -0.0754 -0.0198 0.0368  32  PRO   A O   
884  C CB  . PRO   A 32  ? 0.2779 0.2528 0.1489 -0.0842 -0.0012 0.0246  32  PRO   A CB  
885  C CG  . PRO   A 32  ? 0.2773 0.2579 0.1198 -0.0780 -0.0051 0.0220  32  PRO   A CG  
886  C CD  . PRO   A 32  ? 0.2853 0.2633 0.1147 -0.0767 0.0107  0.0220  32  PRO   A CD  
894  N N   . THR   A 33  ? 0.2747 0.2412 0.1605 -0.0647 -0.0054 0.0398  33  THR   A N   
895  C CA  . THR   A 33  ? 0.2716 0.2421 0.1674 -0.0476 -0.0203 0.0394  33  THR   A CA  
896  C C   . THR   A 33  ? 0.2391 0.2241 0.1549 -0.0450 -0.0232 0.0309  33  THR   A C   
897  O O   . THR   A 33  ? 0.2265 0.2270 0.1620 -0.0402 -0.0324 0.0302  33  THR   A O   
898  C CB  . THR   A 33  ? 0.2958 0.2583 0.1806 -0.0362 -0.0283 0.0541  33  THR   A CB  
899  O OG1 . THR   A 33  ? 0.3166 0.2643 0.2038 -0.0253 -0.0186 0.0653  33  THR   A OG1 
900  C CG2 . THR   A 33  ? 0.2986 0.2681 0.2010 -0.0272 -0.0374 0.0455  33  THR   A CG2 
908  N N   . VAL   A 34  ? 0.2141 0.2034 0.1361 -0.0491 -0.0270 0.0375  34  VAL   A N   
909  C CA  . VAL   A 34  ? 0.1952 0.1903 0.1205 -0.0388 -0.0144 0.0314  34  VAL   A CA  
910  C C   . VAL   A 34  ? 0.1771 0.1868 0.1235 -0.0321 -0.0132 0.0270  34  VAL   A C   
911  O O   . VAL   A 34  ? 0.1764 0.1849 0.1460 -0.0387 -0.0062 0.0306  34  VAL   A O   
912  C CB  . VAL   A 34  ? 0.1953 0.1851 0.1483 -0.0337 -0.0025 0.0176  34  VAL   A CB  
913  C CG1 . VAL   A 34  ? 0.2001 0.1834 0.1465 -0.0212 0.0141  0.0023  34  VAL   A CG1 
914  C CG2 . VAL   A 34  ? 0.2008 0.1979 0.1891 -0.0247 -0.0198 0.0079  34  VAL   A CG2 
924  N N   . VAL   A 35  ? 0.1633 0.1729 0.1207 -0.0375 -0.0045 0.0213  35  VAL   A N   
925  C CA  . VAL   A 35  ? 0.1540 0.1657 0.1257 -0.0317 -0.0054 0.0182  35  VAL   A CA  
926  C C   . VAL   A 35  ? 0.1440 0.1507 0.1179 -0.0226 0.0012  0.0245  35  VAL   A C   
927  O O   . VAL   A 35  ? 0.1420 0.1600 0.1375 -0.0253 0.0166  0.0072  35  VAL   A O   
928  C CB  . VAL   A 35  ? 0.1625 0.1730 0.1331 -0.0230 0.0191  0.0064  35  VAL   A CB  
929  C CG1 . VAL   A 35  ? 0.1750 0.1721 0.1547 -0.0162 0.0110  -0.0070 35  VAL   A CG1 
930  C CG2 . VAL   A 35  ? 0.1588 0.1670 0.1632 -0.0219 0.0194  -0.0018 35  VAL   A CG2 
940  N N   . VAL   A 36  ? 0.1332 0.1456 0.1197 -0.0207 0.0081  0.0157  36  VAL   A N   
941  C CA  . VAL   A 36  ? 0.1261 0.1360 0.1283 -0.0120 0.0027  0.0044  36  VAL   A CA  
942  C C   . VAL   A 36  ? 0.1201 0.1340 0.1564 -0.0118 0.0117  0.0044  36  VAL   A C   
943  O O   . VAL   A 36  ? 0.1329 0.1347 0.1691 -0.0036 0.0282  0.0090  36  VAL   A O   
944  C CB  . VAL   A 36  ? 0.1310 0.1291 0.1294 -0.0106 0.0067  0.0086  36  VAL   A CB  
945  C CG1 . VAL   A 36  ? 0.1318 0.1377 0.1426 -0.0142 0.0059  -0.0037 36  VAL   A CG1 
946  C CG2 . VAL   A 36  ? 0.1377 0.1379 0.1471 -0.0110 0.0003  0.0113  36  VAL   A CG2 
956  N N   A ASN   A 37  ? 0.1220 0.1309 0.1467 -0.0040 0.0076  0.0101  37  ASN   A N   
957  N N   B ASN   A 37  ? 0.1203 0.1237 0.1411 -0.0043 0.0075  0.0099  37  ASN   A N   
958  C CA  A ASN   A 37  ? 0.1259 0.1292 0.1320 0.0006  0.0089  0.0147  37  ASN   A CA  
959  C CA  B ASN   A 37  ? 0.1184 0.1147 0.1258 -0.0002 0.0053  0.0135  37  ASN   A CA  
960  C C   A ASN   A 37  ? 0.1278 0.1295 0.1229 -0.0066 0.0141  0.0197  37  ASN   A C   
961  C C   B ASN   A 37  ? 0.1187 0.1147 0.1341 -0.0010 0.0174  0.0154  37  ASN   A C   
962  O O   A ASN   A 37  ? 0.1404 0.1399 0.1228 -0.0007 0.0060  0.0071  37  ASN   A O   
963  O O   B ASN   A 37  ? 0.1207 0.1197 0.1364 0.0078  0.0161  0.0027  37  ASN   A O   
964  C CB  A ASN   A 37  ? 0.1230 0.1263 0.1425 0.0048  0.0114  0.0094  37  ASN   A CB  
965  C CB  B ASN   A 37  ? 0.1171 0.1103 0.1375 0.0039  0.0078  0.0086  37  ASN   A CB  
966  C CG  A ASN   A 37  ? 0.1262 0.1294 0.1290 0.0043  0.0094  -0.0013 37  ASN   A CG  
967  C CG  B ASN   A 37  ? 0.1201 0.1109 0.1461 -0.0009 0.0111  0.0021  37  ASN   A CG  
968  O OD1 A ASN   A 37  ? 0.1269 0.1268 0.1135 -0.0008 0.0031  -0.0013 37  ASN   A OD1 
969  O OD1 B ASN   A 37  ? 0.1189 0.1177 0.1478 -0.0041 0.0125  0.0061  37  ASN   A OD1 
970  N ND2 A ASN   A 37  ? 0.1275 0.1295 0.1149 0.0027  0.0001  0.0131  37  ASN   A ND2 
971  N ND2 B ASN   A 37  ? 0.1277 0.1098 0.1458 0.0005  0.0111  0.0063  37  ASN   A ND2 
984  N N   A ALA   A 38  ? 0.1268 0.1356 0.1259 -0.0009 0.0112  0.0102  38  ALA   A N   
985  N N   B ALA   A 38  ? 0.1271 0.1194 0.1401 0.0012  0.0210  0.0122  38  ALA   A N   
986  C CA  A ALA   A 38  ? 0.1287 0.1242 0.1220 0.0037  0.0022  0.0016  38  ALA   A CA  
987  C CA  B ALA   A 38  ? 0.1378 0.1261 0.1596 -0.0056 0.0062  0.0148  38  ALA   A CA  
988  C C   A ALA   A 38  ? 0.1230 0.1285 0.1274 0.0041  -0.0014 -0.0011 38  ALA   A C   
989  C C   B ALA   A 38  ? 0.1374 0.1276 0.1581 0.0013  -0.0031 0.0139  38  ALA   A C   
990  O O   A ALA   A 38  ? 0.1192 0.1186 0.1492 0.0005  -0.0045 0.0009  38  ALA   A O   
991  O O   B ALA   A 38  ? 0.1340 0.1262 0.1812 0.0009  -0.0124 0.0283  38  ALA   A O   
992  C CB  A ALA   A 38  ? 0.1348 0.1348 0.1376 -0.0061 -0.0027 0.0051  38  ALA   A CB  
993  C CB  B ALA   A 38  ? 0.1466 0.1319 0.1806 -0.0078 0.0015  0.0115  38  ALA   A CB  
1004 N N   A ALA   A 39  ? 0.1231 0.1272 0.1369 0.0063  0.0018  -0.0040 39  ALA   A N   
1005 N N   B ALA   A 39  ? 0.1407 0.1378 0.1478 0.0057  0.0034  0.0239  39  ALA   A N   
1006 C CA  A ALA   A 39  ? 0.1286 0.1307 0.1329 0.0073  0.0025  0.0114  39  ALA   A CA  
1007 C CA  B ALA   A 39  ? 0.1434 0.1398 0.1322 0.0014  -0.0043 0.0210  39  ALA   A CA  
1008 C C   A ALA   A 39  ? 0.1311 0.1265 0.1183 0.0064  0.0001  0.0074  39  ALA   A C   
1009 C C   B ALA   A 39  ? 0.1402 0.1257 0.1341 -0.0049 -0.0111 0.0127  39  ALA   A C   
1010 O O   A ALA   A 39  ? 0.1365 0.1293 0.1242 -0.0033 0.0067  0.0094  39  ALA   A O   
1011 O O   B ALA   A 39  ? 0.1555 0.1253 0.1435 -0.0086 -0.0044 0.0064  39  ALA   A O   
1012 C CB  A ALA   A 39  ? 0.1316 0.1351 0.1348 0.0089  -0.0046 0.0162  39  ALA   A CB  
1013 C CB  B ALA   A 39  ? 0.1529 0.1577 0.1184 0.0022  -0.0176 0.0254  39  ALA   A CB  
1024 N N   A ASN   A 40  ? 0.1344 0.1310 0.1180 0.0005  0.0170  0.0129  40  ASN   A N   
1025 N N   B ASN   A 40  ? 0.1404 0.1214 0.1402 -0.0103 -0.0053 0.0071  40  ASN   A N   
1026 C CA  A ASN   A 40  ? 0.1452 0.1316 0.1219 0.0017  0.0067  0.0058  40  ASN   A CA  
1027 C CA  B ASN   A 40  ? 0.1419 0.1162 0.1548 -0.0091 -0.0067 0.0174  40  ASN   A CA  
1028 C C   A ASN   A 40  ? 0.1458 0.1223 0.1237 0.0007  0.0139  0.0071  40  ASN   A C   
1029 C C   B ASN   A 40  ? 0.1428 0.1107 0.1443 -0.0117 0.0066  0.0227  40  ASN   A C   
1030 O O   A ASN   A 40  ? 0.1457 0.1277 0.1351 -0.0004 0.0244  0.0095  40  ASN   A O   
1031 O O   B ASN   A 40  ? 0.1326 0.1054 0.1480 -0.0183 0.0110  0.0239  40  ASN   A O   
1032 C CB  A ASN   A 40  ? 0.1526 0.1425 0.1364 0.0012  -0.0081 -0.0088 40  ASN   A CB  
1033 C CB  B ASN   A 40  ? 0.1446 0.1157 0.1683 -0.0010 -0.0131 0.0110  40  ASN   A CB  
1034 C CG  A ASN   A 40  ? 0.1524 0.1481 0.1737 -0.0035 -0.0072 0.0004  40  ASN   A CG  
1035 C CG  B ASN   A 40  ? 0.1382 0.1106 0.1861 0.0034  -0.0214 0.0092  40  ASN   A CG  
1036 O OD1 A ASN   A 40  ? 0.1547 0.1513 0.1864 -0.0011 0.0004  0.0098  40  ASN   A OD1 
1037 O OD1 B ASN   A 40  ? 0.1435 0.1123 0.2249 0.0114  -0.0228 -0.0059 40  ASN   A OD1 
1038 N ND2 A ASN   A 40  ? 0.1507 0.1587 0.1800 -0.0030 -0.0031 -0.0070 40  ASN   A ND2 
1039 N ND2 B ASN   A 40  ? 0.1247 0.1079 0.1811 -0.0114 -0.0074 0.0067  40  ASN   A ND2 
1052 N N   A VAL   A 41  ? 0.1563 0.1252 0.1268 -0.0031 0.0207  0.0134  41  VAL   A N   
1053 N N   B VAL   A 41  ? 0.1515 0.1135 0.1444 0.0035  0.0095  0.0224  41  VAL   A N   
1054 C CA  A VAL   A 41  ? 0.1575 0.1340 0.1470 -0.0030 0.0236  0.0101  41  VAL   A CA  
1055 C CA  B VAL   A 41  ? 0.1609 0.1238 0.1525 0.0008  0.0259  0.0166  41  VAL   A CA  
1056 C C   A VAL   A 41  ? 0.1547 0.1325 0.1575 -0.0037 0.0205  0.0056  41  VAL   A C   
1057 C C   B VAL   A 41  ? 0.1571 0.1206 0.1525 -0.0031 0.0317  0.0116  41  VAL   A C   
1058 O O   A VAL   A 41  ? 0.1619 0.1300 0.1848 0.0025  0.0227  -0.0078 41  VAL   A O   
1059 O O   B VAL   A 41  ? 0.1654 0.1053 0.1577 -0.0037 0.0407  0.0116  41  VAL   A O   
1060 C CB  A VAL   A 41  ? 0.1606 0.1401 0.1447 -0.0045 0.0302  0.0074  41  VAL   A CB  
1061 C CB  B VAL   A 41  ? 0.1733 0.1358 0.1644 -0.0038 0.0359  0.0117  41  VAL   A CB  
1062 C CG1 A VAL   A 41  ? 0.1763 0.1517 0.1670 -0.0044 0.0305  0.0016  41  VAL   A CG1 
1063 C CG1 B VAL   A 41  ? 0.1837 0.1442 0.1826 -0.0066 0.0463  0.0037  41  VAL   A CG1 
1064 C CG2 A VAL   A 41  ? 0.1524 0.1438 0.1143 -0.0071 0.0361  0.0079  41  VAL   A CG2 
1065 C CG2 B VAL   A 41  ? 0.1759 0.1451 0.1710 -0.0073 0.0284  0.0123  41  VAL   A CG2 
1084 N N   . TYR   A 42  ? 0.1472 0.1260 0.1777 0.0046  0.0322  0.0210  42  TYR   A N   
1085 C CA  . TYR   A 42  ? 0.1487 0.1174 0.1775 -0.0039 0.0337  0.0191  42  TYR   A CA  
1086 C C   . TYR   A 42  ? 0.1410 0.1229 0.1831 -0.0029 0.0300  0.0158  42  TYR   A C   
1087 O O   . TYR   A 42  ? 0.1412 0.1243 0.1939 -0.0110 0.0251  0.0077  42  TYR   A O   
1088 C CB  . TYR   A 42  ? 0.1776 0.1282 0.1726 0.0021  0.0324  0.0254  42  TYR   A CB  
1089 C CG  . TYR   A 42  ? 0.1968 0.1435 0.1784 0.0006  0.0262  0.0327  42  TYR   A CG  
1090 C CD1 . TYR   A 42  ? 0.2044 0.1547 0.1853 -0.0038 0.0354  0.0286  42  TYR   A CD1 
1091 C CD2 . TYR   A 42  ? 0.2089 0.1653 0.2006 0.0092  0.0234  0.0207  42  TYR   A CD2 
1092 C CE1 . TYR   A 42  ? 0.2137 0.1690 0.1848 -0.0110 0.0456  0.0279  42  TYR   A CE1 
1093 C CE2 . TYR   A 42  ? 0.2186 0.1800 0.2100 -0.0132 0.0310  0.0282  42  TYR   A CE2 
1094 C CZ  . TYR   A 42  ? 0.2271 0.1822 0.1950 -0.0157 0.0449  0.0323  42  TYR   A CZ  
1095 O OH  . TYR   A 42  ? 0.2402 0.2109 0.2209 -0.0304 0.0479  0.0225  42  TYR   A OH  
1106 N N   A LEU   A 43  ? 0.1378 0.1250 0.1689 -0.0021 0.0201  0.0078  43  LEU   A N   
1107 N N   B LEU   A 43  ? 0.1370 0.1277 0.1666 -0.0061 0.0188  0.0130  43  LEU   A N   
1108 C CA  A LEU   A 43  ? 0.1320 0.1210 0.1728 -0.0005 0.0160  0.0007  43  LEU   A CA  
1109 C CA  B LEU   A 43  ? 0.1324 0.1289 0.1640 -0.0072 0.0145  0.0101  43  LEU   A CA  
1110 C C   A LEU   A 43  ? 0.1300 0.1255 0.1697 0.0065  0.0120  -0.0061 43  LEU   A C   
1111 C C   B LEU   A 43  ? 0.1385 0.1328 0.1565 -0.0092 0.0092  0.0131  43  LEU   A C   
1112 O O   A LEU   A 43  ? 0.1395 0.1303 0.1867 0.0136  -0.0016 -0.0139 43  LEU   A O   
1113 O O   B LEU   A 43  ? 0.1474 0.1321 0.1625 -0.0111 0.0014  0.0170  43  LEU   A O   
1114 C CB  A LEU   A 43  ? 0.1366 0.1205 0.1815 -0.0018 0.0158  0.0001  43  LEU   A CB  
1115 C CB  B LEU   A 43  ? 0.1264 0.1260 0.1665 -0.0061 0.0210  0.0054  43  LEU   A CB  
1116 C CG  A LEU   A 43  ? 0.1402 0.1188 0.1802 -0.0004 0.0075  0.0025  43  LEU   A CG  
1117 C CG  B LEU   A 43  ? 0.1251 0.1277 0.1695 -0.0018 0.0144  0.0093  43  LEU   A CG  
1118 C CD1 A LEU   A 43  ? 0.1440 0.1255 0.1977 0.0010  0.0029  0.0114  43  LEU   A CD1 
1119 C CD1 B LEU   A 43  ? 0.1247 0.1338 0.1894 -0.0014 0.0106  0.0126  43  LEU   A CD1 
1120 C CD2 A LEU   A 43  ? 0.1487 0.1207 0.1834 0.0061  0.0132  0.0070  43  LEU   A CD2 
1121 C CD2 B LEU   A 43  ? 0.1372 0.1268 0.1729 0.0014  0.0103  0.0204  43  LEU   A CD2 
1144 N N   A LYS   A 44  ? 0.1344 0.1214 0.1664 0.0058  0.0098  0.0038  44  LYS   A N   
1145 N N   B LYS   A 44  ? 0.1411 0.1346 0.1545 -0.0084 0.0025  0.0122  44  LYS   A N   
1146 C CA  A LYS   A 44  ? 0.1389 0.1206 0.1812 -0.0028 0.0109  0.0159  44  LYS   A CA  
1147 C CA  B LYS   A 44  ? 0.1531 0.1384 0.1669 -0.0117 0.0013  0.0157  44  LYS   A CA  
1148 C C   A LYS   A 44  ? 0.1284 0.1165 0.1581 0.0055  0.0014  0.0005  44  LYS   A C   
1149 C C   B LYS   A 44  ? 0.1487 0.1355 0.1657 -0.0134 -0.0037 0.0086  44  LYS   A C   
1150 O O   A LYS   A 44  ? 0.1367 0.1319 0.1863 0.0081  0.0033  -0.0204 44  LYS   A O   
1151 O O   B LYS   A 44  ? 0.1539 0.1389 0.1757 -0.0181 -0.0018 0.0010  44  LYS   A O   
1152 C CB  A LYS   A 44  ? 0.1595 0.1367 0.2266 -0.0019 0.0140  0.0230  44  LYS   A CB  
1153 C CB  B LYS   A 44  ? 0.1755 0.1585 0.2091 -0.0011 0.0105  0.0116  44  LYS   A CB  
1154 C CG  A LYS   A 44  ? 0.1898 0.1646 0.2905 -0.0161 0.0223  0.0302  44  LYS   A CG  
1155 C CG  B LYS   A 44  ? 0.2008 0.1893 0.2714 0.0003  0.0195  0.0135  44  LYS   A CG  
1156 C CD  A LYS   A 44  ? 0.2305 0.2154 0.3795 -0.0228 0.0171  0.0201  44  LYS   A CD  
1157 C CD  B LYS   A 44  ? 0.2296 0.2297 0.3421 -0.0013 0.0099  0.0089  44  LYS   A CD  
1158 C CE  A LYS   A 44  ? 0.2508 0.2454 0.4347 -0.0248 0.0217  0.0131  44  LYS   A CE  
1159 C CE  B LYS   A 44  ? 0.2445 0.2550 0.3871 -0.0048 0.0086  0.0084  44  LYS   A CE  
1160 N NZ  A LYS   A 44  ? 0.2610 0.2701 0.4586 -0.0217 0.0261  0.0115  44  LYS   A NZ  
1161 N NZ  B LYS   A 44  ? 0.2563 0.2714 0.4090 -0.0115 0.0101  0.0053  44  LYS   A NZ  
1188 N N   A HIS   A 45  ? 0.1198 0.1100 0.1514 0.0095  0.0076  0.0092  45  HIS   A N   
1189 N N   B HIS   A 45  ? 0.1466 0.1346 0.1687 -0.0119 -0.0075 0.0105  45  HIS   A N   
1190 C CA  A HIS   A 45  ? 0.1196 0.1211 0.1540 0.0023  0.0021  0.0031  45  HIS   A CA  
1191 C CA  B HIS   A 45  ? 0.1463 0.1406 0.1681 -0.0079 -0.0115 0.0093  45  HIS   A CA  
1192 C C   A HIS   A 45  ? 0.1262 0.1281 0.1728 0.0129  0.0069  0.0053  45  HIS   A C   
1193 C C   B HIS   A 45  ? 0.1495 0.1426 0.1688 -0.0013 -0.0162 0.0102  45  HIS   A C   
1194 O O   A HIS   A 45  ? 0.1413 0.1241 0.1869 0.0080  0.0115  0.0062  45  HIS   A O   
1195 O O   B HIS   A 45  ? 0.1609 0.1503 0.1866 0.0143  -0.0113 0.0122  45  HIS   A O   
1196 C CB  A HIS   A 45  ? 0.1194 0.1192 0.1371 -0.0054 0.0058  -0.0093 45  HIS   A CB  
1197 C CB  B HIS   A 45  ? 0.1407 0.1394 0.1597 -0.0049 -0.0091 0.0035  45  HIS   A CB  
1198 C CG  A HIS   A 45  ? 0.1229 0.1158 0.1417 0.0015  0.0141  -0.0005 45  HIS   A CG  
1199 C CG  B HIS   A 45  ? 0.1309 0.1352 0.1454 -0.0022 0.0089  0.0069  45  HIS   A CG  
1200 N ND1 A HIS   A 45  ? 0.1243 0.1243 0.1576 -0.0021 0.0140  0.0101  45  HIS   A ND1 
1201 N ND1 B HIS   A 45  ? 0.1228 0.1352 0.1511 -0.0019 -0.0022 0.0167  45  HIS   A ND1 
1202 C CD2 A HIS   A 45  ? 0.1265 0.1242 0.1682 -0.0053 0.0064  0.0141  45  HIS   A CD2 
1203 C CD2 B HIS   A 45  ? 0.1254 0.1295 0.1394 -0.0009 0.0131  0.0071  45  HIS   A CD2 
1204 C CE1 A HIS   A 45  ? 0.1243 0.1288 0.1556 -0.0053 0.0075  0.0196  45  HIS   A CE1 
1205 C CE1 B HIS   A 45  ? 0.1195 0.1285 0.1304 -0.0021 -0.0015 0.0082  45  HIS   A CE1 
1206 N NE2 A HIS   A 45  ? 0.1295 0.1340 0.1630 0.0019  0.0042  0.0197  45  HIS   A NE2 
1207 N NE2 B HIS   A 45  ? 0.1240 0.1294 0.1155 0.0012  0.0065  -0.0027 45  HIS   A NE2 
1222 N N   A GLY   A 46  ? 0.1347 0.1442 0.1891 0.0214  -0.0023 0.0193  46  GLY   A N   
1223 N N   B GLY   A 46  ? 0.1496 0.1393 0.1713 -0.0140 -0.0229 0.0120  46  GLY   A N   
1224 C CA  A GLY   A 46  ? 0.1423 0.1487 0.2060 0.0189  -0.0186 0.0305  46  GLY   A CA  
1225 C CA  B GLY   A 46  ? 0.1444 0.1387 0.1854 -0.0127 -0.0143 0.0078  46  GLY   A CA  
1226 C C   A GLY   A 46  ? 0.1477 0.1467 0.2089 0.0243  -0.0153 0.0424  46  GLY   A C   
1227 C C   B GLY   A 46  ? 0.1407 0.1376 0.1954 -0.0053 -0.0041 0.0146  46  GLY   A C   
1228 O O   A GLY   A 46  ? 0.1579 0.1482 0.2299 0.0275  -0.0218 0.0485  46  GLY   A O   
1229 O O   B GLY   A 46  ? 0.1496 0.1423 0.2022 0.0012  -0.0024 0.0125  46  GLY   A O   
1236 N N   A GLY   A 47  ? 0.1454 0.1453 0.2060 0.0216  -0.0199 0.0416  47  GLY   A N   
1237 N N   B GLY   A 47  ? 0.1376 0.1404 0.1962 -0.0046 -0.0101 0.0071  47  GLY   A N   
1238 C CA  A GLY   A 47  ? 0.1488 0.1566 0.2106 0.0217  -0.0228 0.0303  47  GLY   A CA  
1239 C CA  B GLY   A 47  ? 0.1333 0.1450 0.1896 -0.0045 -0.0102 0.0133  47  GLY   A CA  
1240 C C   A GLY   A 47  ? 0.1454 0.1519 0.1775 0.0211  -0.0146 0.0173  47  GLY   A C   
1241 C C   B GLY   A 47  ? 0.1297 0.1366 0.1726 0.0032  -0.0081 0.0132  47  GLY   A C   
1242 O O   A GLY   A 47  ? 0.1439 0.1409 0.1855 0.0227  -0.0102 0.0195  47  GLY   A O   
1243 O O   B GLY   A 47  ? 0.1257 0.1346 0.1781 0.0111  -0.0083 0.0248  47  GLY   A O   
1250 N N   A GLY   A 48  ? 0.1412 0.1630 0.1551 0.0190  -0.0139 0.0169  48  GLY   A N   
1251 N N   B GLY   A 48  ? 0.1358 0.1425 0.1650 0.0029  0.0016  0.0142  48  GLY   A N   
1252 C CA  A GLY   A 48  ? 0.1340 0.1666 0.1532 0.0151  -0.0110 0.0036  48  GLY   A CA  
1253 C CA  B GLY   A 48  ? 0.1349 0.1368 0.1530 0.0009  0.0106  0.0096  48  GLY   A CA  
1254 C C   A GLY   A 48  ? 0.1339 0.1668 0.1305 0.0030  -0.0027 -0.0039 48  GLY   A C   
1255 C C   B GLY   A 48  ? 0.1340 0.1324 0.1530 0.0047  0.0117  0.0088  48  GLY   A C   
1256 O O   A GLY   A 48  ? 0.1449 0.1705 0.1410 0.0085  0.0002  -0.0113 48  GLY   A O   
1257 O O   B GLY   A 48  ? 0.1474 0.1359 0.1455 0.0062  0.0202  0.0076  48  GLY   A O   
1264 N N   A VAL   A 49  ? 0.1307 0.1606 0.1565 -0.0055 -0.0082 -0.0000 49  VAL   A N   
1265 N N   B VAL   A 49  ? 0.1232 0.1242 0.1421 0.0051  -0.0004 0.0032  49  VAL   A N   
1266 C CA  A VAL   A 49  ? 0.1491 0.1539 0.1568 -0.0134 -0.0011 0.0172  49  VAL   A CA  
1267 C CA  B VAL   A 49  ? 0.1232 0.1278 0.1395 -0.0023 0.0007  0.0066  49  VAL   A CA  
1268 C C   A VAL   A 49  ? 0.1393 0.1401 0.1257 -0.0079 -0.0097 0.0185  49  VAL   A C   
1269 C C   B VAL   A 49  ? 0.1217 0.1172 0.1374 -0.0016 0.0057  -0.0165 49  VAL   A C   
1270 O O   A VAL   A 49  ? 0.1461 0.1426 0.1205 -0.0096 -0.0041 0.0134  49  VAL   A O   
1271 O O   B VAL   A 49  ? 0.1186 0.1069 0.1302 0.0021  0.0108  -0.0051 49  VAL   A O   
1272 C CB  A VAL   A 49  ? 0.1707 0.1489 0.1814 -0.0228 -0.0147 0.0252  49  VAL   A CB  
1273 C CB  B VAL   A 49  ? 0.1246 0.1263 0.1541 -0.0002 -0.0203 0.0200  49  VAL   A CB  
1274 C CG1 A VAL   A 49  ? 0.1715 0.1426 0.1947 -0.0131 -0.0117 0.0168  49  VAL   A CG1 
1275 C CG1 B VAL   A 49  ? 0.1115 0.1230 0.1787 0.0003  -0.0194 0.0192  49  VAL   A CG1 
1276 C CG2 A VAL   A 49  ? 0.1804 0.1573 0.2071 -0.0328 -0.0213 0.0282  49  VAL   A CG2 
1277 C CG2 B VAL   A 49  ? 0.1403 0.1335 0.1543 -0.0014 -0.0395 0.0220  49  VAL   A CG2 
1296 N N   A ALA   A 50  ? 0.1319 0.1341 0.1324 -0.0050 -0.0153 0.0165  50  ALA   A N   
1297 N N   B ALA   A 50  ? 0.1258 0.1210 0.1203 0.0017  -0.0036 -0.0170 50  ALA   A N   
1298 C CA  A ALA   A 50  ? 0.1259 0.1301 0.1389 -0.0041 -0.0054 0.0146  50  ALA   A CA  
1299 C CA  B ALA   A 50  ? 0.1228 0.1180 0.1205 0.0062  0.0004  -0.0145 50  ALA   A CA  
1300 C C   A ALA   A 50  ? 0.1191 0.1291 0.1377 -0.0038 -0.0058 0.0050  50  ALA   A C   
1301 C C   B ALA   A 50  ? 0.1243 0.1192 0.1151 -0.0021 0.0019  -0.0109 50  ALA   A C   
1302 O O   A ALA   A 50  ? 0.1195 0.1335 0.1519 0.0005  -0.0162 0.0069  50  ALA   A O   
1303 O O   B ALA   A 50  ? 0.1269 0.1270 0.0985 -0.0038 0.0073  -0.0144 50  ALA   A O   
1304 C CB  A ALA   A 50  ? 0.1279 0.1329 0.1400 -0.0053 -0.0026 0.0060  50  ALA   A CB  
1305 C CB  B ALA   A 50  ? 0.1266 0.1125 0.1344 0.0171  0.0045  -0.0200 50  ALA   A CB  
1316 N N   A GLY   A 51  ? 0.1214 0.1227 0.1406 0.0060  -0.0094 -0.0029 51  GLY   A N   
1317 N N   B GLY   A 51  ? 0.1287 0.1123 0.1390 -0.0005 -0.0050 -0.0020 51  GLY   A N   
1318 C CA  A GLY   A 51  ? 0.1264 0.1233 0.1402 0.0099  -0.0005 -0.0001 51  GLY   A CA  
1319 C CA  B GLY   A 51  ? 0.1368 0.1144 0.1402 -0.0019 -0.0007 -0.0016 51  GLY   A CA  
1320 C C   A GLY   A 51  ? 0.1178 0.1257 0.1284 0.0074  0.0031  -0.0047 51  GLY   A C   
1321 C C   B GLY   A 51  ? 0.1341 0.1237 0.1558 -0.0009 0.0084  -0.0012 51  GLY   A C   
1322 O O   A GLY   A 51  ? 0.1284 0.1285 0.1316 0.0001  -0.0103 0.0063  51  GLY   A O   
1323 O O   B GLY   A 51  ? 0.1469 0.1280 0.1561 0.0005  0.0275  0.0052  51  GLY   A O   
1330 N N   A ALA   A 52  ? 0.1186 0.1362 0.1324 0.0025  0.0034  -0.0080 52  ALA   A N   
1331 N N   B ALA   A 52  ? 0.1349 0.1333 0.1648 -0.0015 0.0105  -0.0065 52  ALA   A N   
1332 C CA  A ALA   A 52  ? 0.1225 0.1406 0.1386 -0.0033 0.0056  -0.0016 52  ALA   A CA  
1333 C CA  B ALA   A 52  ? 0.1311 0.1377 0.1544 0.0015  0.0080  0.0008  52  ALA   A CA  
1334 C C   A ALA   A 52  ? 0.1242 0.1407 0.1290 -0.0045 -0.0033 0.0016  52  ALA   A C   
1335 C C   B ALA   A 52  ? 0.1247 0.1323 0.1448 -0.0029 0.0122  -0.0060 52  ALA   A C   
1336 O O   A ALA   A 52  ? 0.1368 0.1490 0.1381 0.0039  -0.0067 0.0047  52  ALA   A O   
1337 O O   B ALA   A 52  ? 0.1301 0.1287 0.1559 -0.0081 0.0105  -0.0099 52  ALA   A O   
1338 C CB  A ALA   A 52  ? 0.1403 0.1554 0.1602 -0.0041 -0.0069 0.0182  52  ALA   A CB  
1339 C CB  B ALA   A 52  ? 0.1376 0.1550 0.1716 0.0031  0.0011  0.0019  52  ALA   A CB  
1350 N N   A LEU   A 53  ? 0.1245 0.1335 0.1322 -0.0101 -0.0099 0.0015  53  LEU   A N   
1351 N N   B LEU   A 53  ? 0.1234 0.1380 0.1349 0.0052  0.0039  -0.0089 53  LEU   A N   
1352 C CA  A LEU   A 53  ? 0.1283 0.1441 0.1388 -0.0095 -0.0045 0.0030  53  LEU   A CA  
1353 C CA  B LEU   A 53  ? 0.1227 0.1459 0.1228 0.0026  0.0009  -0.0115 53  LEU   A CA  
1354 C C   A LEU   A 53  ? 0.1283 0.1498 0.1374 -0.0032 0.0005  0.0047  53  LEU   A C   
1355 C C   B LEU   A 53  ? 0.1220 0.1491 0.1354 -0.0048 0.0132  -0.0171 53  LEU   A C   
1356 O O   A LEU   A 53  ? 0.1423 0.1598 0.1551 -0.0099 -0.0039 0.0063  53  LEU   A O   
1357 O O   B LEU   A 53  ? 0.1248 0.1548 0.1615 -0.0159 0.0140  -0.0200 53  LEU   A O   
1358 C CB  A LEU   A 53  ? 0.1303 0.1476 0.1542 -0.0079 0.0010  0.0155  53  LEU   A CB  
1359 C CB  B LEU   A 53  ? 0.1201 0.1482 0.1090 0.0029  -0.0116 -0.0145 53  LEU   A CB  
1360 C CG  A LEU   A 53  ? 0.1331 0.1461 0.1674 -0.0038 0.0071  0.0163  53  LEU   A CG  
1361 C CG  B LEU   A 53  ? 0.1151 0.1507 0.1238 0.0014  -0.0076 -0.0163 53  LEU   A CG  
1362 C CD1 A LEU   A 53  ? 0.1352 0.1535 0.1757 0.0038  -0.0029 0.0201  53  LEU   A CD1 
1363 C CD1 B LEU   A 53  ? 0.1195 0.1582 0.1344 0.0050  -0.0120 -0.0228 53  LEU   A CD1 
1364 C CD2 A LEU   A 53  ? 0.1473 0.1561 0.1881 -0.0085 0.0013  0.0137  53  LEU   A CD2 
1365 C CD2 B LEU   A 53  ? 0.1115 0.1489 0.1271 0.0001  -0.0008 -0.0170 53  LEU   A CD2 
1388 N N   A ASN   A 54  ? 0.1267 0.1403 0.1324 -0.0020 -0.0035 0.0032  54  ASN   A N   
1389 N N   B ASN   A 54  ? 0.1240 0.1448 0.1451 -0.0081 0.0104  -0.0161 54  ASN   A N   
1390 C CA  A ASN   A 54  ? 0.1234 0.1330 0.1397 -0.0018 -0.0078 -0.0019 54  ASN   A CA  
1391 C CA  B ASN   A 54  ? 0.1222 0.1414 0.1543 -0.0078 0.0048  -0.0159 54  ASN   A CA  
1392 C C   A ASN   A 54  ? 0.1334 0.1429 0.1563 -0.0077 -0.0013 -0.0073 54  ASN   A C   
1393 C C   B ASN   A 54  ? 0.1300 0.1460 0.1626 -0.0073 -0.0027 -0.0148 54  ASN   A C   
1394 O O   A ASN   A 54  ? 0.1338 0.1485 0.1629 -0.0127 0.0090  -0.0196 54  ASN   A O   
1395 O O   B ASN   A 54  ? 0.1292 0.1508 0.1702 -0.0049 -0.0098 -0.0211 54  ASN   A O   
1396 C CB  A ASN   A 54  ? 0.1175 0.1272 0.1463 -0.0030 -0.0121 -0.0121 54  ASN   A CB  
1397 C CB  B ASN   A 54  ? 0.1224 0.1413 0.1621 -0.0044 0.0087  -0.0154 54  ASN   A CB  
1398 C CG  A ASN   A 54  ? 0.1207 0.1307 0.1409 -0.0008 -0.0099 -0.0161 54  ASN   A CG  
1399 C CG  B ASN   A 54  ? 0.1257 0.1448 0.1629 0.0012  0.0161  -0.0107 54  ASN   A CG  
1400 O OD1 A ASN   A 54  ? 0.1187 0.1224 0.1177 -0.0018 -0.0017 0.0014  54  ASN   A OD1 
1401 O OD1 B ASN   A 54  ? 0.1313 0.1622 0.1873 -0.0057 0.0134  -0.0030 54  ASN   A OD1 
1402 N ND2 A ASN   A 54  ? 0.1163 0.1418 0.1746 -0.0072 -0.0193 0.0000  54  ASN   A ND2 
1403 N ND2 B ASN   A 54  ? 0.1209 0.1329 0.1503 0.0005  0.0217  0.0033  54  ASN   A ND2 
1416 N N   . LYS   A 55  ? 0.1334 0.1481 0.1696 -0.0014 -0.0007 -0.0215 55  LYS   A N   
1417 C CA  . LYS   A 55  ? 0.1403 0.1503 0.1868 0.0028  -0.0029 -0.0283 55  LYS   A CA  
1418 C C   . LYS   A 55  ? 0.1428 0.1583 0.1753 -0.0028 0.0100  -0.0361 55  LYS   A C   
1419 O O   . LYS   A 55  ? 0.1538 0.1672 0.1883 0.0021  0.0031  -0.0390 55  LYS   A O   
1420 C CB  . LYS   A 55  ? 0.1524 0.1618 0.2007 0.0192  -0.0061 -0.0319 55  LYS   A CB  
1421 C CG  . LYS   A 55  ? 0.1714 0.1939 0.2216 0.0250  -0.0132 -0.0381 55  LYS   A CG  
1422 C CD  . LYS   A 55  ? 0.1803 0.2272 0.2255 0.0395  -0.0090 -0.0397 55  LYS   A CD  
1423 C CE  . LYS   A 55  ? 0.2002 0.2582 0.2295 0.0482  -0.0207 -0.0359 55  LYS   A CE  
1424 N NZ  . LYS   A 55  ? 0.2066 0.2902 0.2283 0.0604  -0.0235 -0.0280 55  LYS   A NZ  
1439 N N   . ALA   A 56  ? 0.1489 0.1719 0.1809 -0.0142 0.0162  -0.0377 56  ALA   A N   
1440 C CA  . ALA   A 56  ? 0.1604 0.1905 0.1836 -0.0172 0.0193  -0.0396 56  ALA   A CA  
1441 C C   . ALA   A 56  ? 0.1630 0.2012 0.1516 -0.0188 0.0252  -0.0468 56  ALA   A C   
1442 O O   . ALA   A 56  ? 0.1706 0.2375 0.1672 -0.0095 0.0263  -0.0313 56  ALA   A O   
1443 C CB  . ALA   A 56  ? 0.1593 0.1983 0.1972 -0.0242 0.0201  -0.0279 56  ALA   A CB  
1449 N N   . THR   A 57  ? 0.1460 0.1771 0.1529 -0.0191 0.0181  -0.0365 57  THR   A N   
1450 C CA  . THR   A 57  ? 0.1559 0.1727 0.1474 -0.0162 0.0061  -0.0232 57  THR   A CA  
1451 C C   . THR   A 57  ? 0.1554 0.1776 0.1624 -0.0121 0.0082  -0.0309 57  THR   A C   
1452 O O   . THR   A 57  ? 0.1522 0.1864 0.1752 -0.0151 -0.0012 -0.0399 57  THR   A O   
1453 C CB  . THR   A 57  ? 0.1585 0.1662 0.1521 -0.0089 0.0110  -0.0233 57  THR   A CB  
1454 O OG1 . THR   A 57  ? 0.1471 0.1629 0.1585 -0.0097 0.0087  -0.0212 57  THR   A OG1 
1455 C CG2 . THR   A 57  ? 0.1612 0.1703 0.1535 -0.0120 0.0054  -0.0107 57  THR   A CG2 
1463 N N   . ASN   A 58  ? 0.1616 0.1709 0.1920 -0.0157 0.0151  -0.0511 58  ASN   A N   
1464 C CA  . ASN   A 58  ? 0.1745 0.1668 0.2187 -0.0200 0.0205  -0.0547 58  ASN   A CA  
1465 C C   . ASN   A 58  ? 0.1505 0.1517 0.1979 -0.0043 0.0089  -0.0410 58  ASN   A C   
1466 O O   . ASN   A 58  ? 0.1515 0.1663 0.2083 -0.0157 -0.0003 -0.0454 58  ASN   A O   
1467 C CB  . ASN   A 58  ? 0.2163 0.1863 0.2565 -0.0283 0.0460  -0.0627 58  ASN   A CB  
1468 C CG  . ASN   A 58  ? 0.2599 0.2095 0.3259 -0.0199 0.0530  -0.0465 58  ASN   A CG  
1469 O OD1 . ASN   A 58  ? 0.2879 0.2064 0.3627 0.0117  0.0836  -0.0456 58  ASN   A OD1 
1470 N ND2 . ASN   A 58  ? 0.2720 0.2225 0.3483 -0.0171 0.0351  -0.0460 58  ASN   A ND2 
1477 N N   . ASN   A 59  ? 0.1362 0.1486 0.1798 -0.0117 -0.0003 -0.0307 59  ASN   A N   
1478 C CA  . ASN   A 59  ? 0.1383 0.1369 0.1818 -0.0081 -0.0057 -0.0175 59  ASN   A CA  
1479 C C   . ASN   A 59  ? 0.1339 0.1386 0.1661 -0.0086 -0.0035 -0.0086 59  ASN   A C   
1480 O O   . ASN   A 59  ? 0.1388 0.1444 0.1564 -0.0100 0.0011  -0.0054 59  ASN   A O   
1481 C CB  . ASN   A 59  ? 0.1462 0.1343 0.1851 -0.0020 -0.0149 -0.0318 59  ASN   A CB  
1482 C CG  . ASN   A 59  ? 0.1477 0.1410 0.1854 -0.0001 -0.0254 -0.0090 59  ASN   A CG  
1483 O OD1 . ASN   A 59  ? 0.1645 0.1483 0.1802 -0.0122 -0.0262 -0.0035 59  ASN   A OD1 
1484 N ND2 . ASN   A 59  ? 0.1489 0.1435 0.2050 -0.0095 -0.0192 -0.0016 59  ASN   A ND2 
1491 N N   . ALA   A 60  ? 0.1249 0.1388 0.1725 -0.0040 -0.0014 -0.0081 60  ALA   A N   
1492 C CA  . ALA   A 60  ? 0.1350 0.1452 0.1641 -0.0057 -0.0027 -0.0046 60  ALA   A CA  
1493 C C   . ALA   A 60  ? 0.1367 0.1451 0.1690 -0.0053 -0.0022 -0.0160 60  ALA   A C   
1494 O O   . ALA   A 60  ? 0.1309 0.1444 0.1902 -0.0081 -0.0108 -0.0122 60  ALA   A O   
1495 C CB  . ALA   A 60  ? 0.1482 0.1543 0.1612 -0.0105 -0.0142 -0.0243 60  ALA   A CB  
1501 N N   . MET   A 61  ? 0.1289 0.1377 0.1600 -0.0078 -0.0019 -0.0131 61  MET   A N   
1502 C CA  . MET   A 61  ? 0.1287 0.1300 0.1727 -0.0104 0.0072  -0.0083 61  MET   A CA  
1503 C C   . MET   A 61  ? 0.1301 0.1260 0.1715 -0.0147 0.0022  -0.0076 61  MET   A C   
1504 O O   . MET   A 61  ? 0.1341 0.1301 0.1726 -0.0102 0.0096  -0.0034 61  MET   A O   
1505 C CB  . MET   A 61  ? 0.1388 0.1281 0.1662 -0.0071 0.0042  -0.0101 61  MET   A CB  
1506 C CG  . MET   A 61  ? 0.1421 0.1395 0.1689 -0.0022 0.0078  -0.0081 61  MET   A CG  
1507 S SD  . MET   A 61  ? 0.1381 0.1404 0.1925 -0.0126 0.0038  -0.0235 61  MET   A SD  
1508 C CE  . MET   A 61  ? 0.1526 0.1588 0.2111 -0.0200 0.0183  -0.0152 61  MET   A CE  
1518 N N   . GLN   A 62  ? 0.1302 0.1235 0.1725 -0.0069 -0.0016 -0.0046 62  GLN   A N   
1519 C CA  . GLN   A 62  ? 0.1339 0.1180 0.1782 -0.0034 0.0048  -0.0074 62  GLN   A CA  
1520 C C   . GLN   A 62  ? 0.1322 0.1211 0.1806 -0.0032 0.0087  -0.0011 62  GLN   A C   
1521 O O   . GLN   A 62  ? 0.1333 0.1344 0.1751 -0.0080 0.0078  -0.0057 62  GLN   A O   
1522 C CB  . GLN   A 62  ? 0.1332 0.1220 0.1769 0.0010  -0.0049 -0.0090 62  GLN   A CB  
1523 C CG  . GLN   A 62  ? 0.1389 0.1155 0.1676 -0.0038 -0.0015 0.0062  62  GLN   A CG  
1524 C CD  . GLN   A 62  ? 0.1470 0.1170 0.1712 0.0025  0.0112  0.0087  62  GLN   A CD  
1525 O OE1 . GLN   A 62  ? 0.1464 0.1325 0.1743 -0.0072 0.0053  0.0015  62  GLN   A OE1 
1526 N NE2 . GLN   A 62  ? 0.1546 0.1246 0.1821 0.0018  0.0039  -0.0028 62  GLN   A NE2 
1535 N N   . VAL   A 63  ? 0.1301 0.1288 0.1891 -0.0056 0.0146  -0.0224 63  VAL   A N   
1536 C CA  . VAL   A 63  ? 0.1355 0.1358 0.2006 -0.0157 0.0049  -0.0261 63  VAL   A CA  
1537 C C   . VAL   A 63  ? 0.1214 0.1296 0.1899 -0.0187 -0.0075 -0.0193 63  VAL   A C   
1538 O O   . VAL   A 63  ? 0.1229 0.1355 0.1924 -0.0171 0.0023  -0.0183 63  VAL   A O   
1539 C CB  . VAL   A 63  ? 0.1504 0.1540 0.2295 -0.0195 0.0011  -0.0386 63  VAL   A CB  
1540 C CG1 . VAL   A 63  ? 0.1639 0.1744 0.2571 -0.0165 -0.0126 -0.0599 63  VAL   A CG1 
1541 C CG2 . VAL   A 63  ? 0.1609 0.1428 0.2393 -0.0132 0.0206  -0.0346 63  VAL   A CG2 
1551 N N   . GLU   A 64  ? 0.1290 0.1400 0.1873 -0.0053 0.0023  -0.0179 64  GLU   A N   
1552 C CA  . GLU   A 64  ? 0.1241 0.1371 0.1809 -0.0102 0.0012  -0.0030 64  GLU   A CA  
1553 C C   . GLU   A 64  ? 0.1185 0.1299 0.1811 -0.0103 0.0064  -0.0033 64  GLU   A C   
1554 O O   . GLU   A 64  ? 0.1308 0.1317 0.1811 -0.0011 0.0110  -0.0038 64  GLU   A O   
1555 C CB  . GLU   A 64  ? 0.1368 0.1469 0.1869 -0.0089 0.0052  -0.0114 64  GLU   A CB  
1556 C CG  . GLU   A 64  ? 0.1474 0.1539 0.1860 -0.0144 0.0106  -0.0031 64  GLU   A CG  
1557 C CD  . GLU   A 64  ? 0.1556 0.1626 0.1984 -0.0209 0.0149  -0.0056 64  GLU   A CD  
1558 O OE1 . GLU   A 64  ? 0.1486 0.1667 0.2122 -0.0239 0.0193  -0.0116 64  GLU   A OE1 
1559 O OE2 . GLU   A 64  ? 0.1704 0.1626 0.1836 -0.0277 0.0021  -0.0020 64  GLU   A OE2 
1566 N N   . SER   A 65  ? 0.1155 0.1354 0.1823 -0.0011 0.0070  -0.0031 65  SER   A N   
1567 C CA  . SER   A 65  ? 0.1258 0.1295 0.1600 -0.0068 0.0054  -0.0153 65  SER   A CA  
1568 C C   . SER   A 65  ? 0.1266 0.1359 0.1613 -0.0049 -0.0017 -0.0071 65  SER   A C   
1569 O O   . SER   A 65  ? 0.1384 0.1355 0.1813 0.0006  0.0154  -0.0059 65  SER   A O   
1570 C CB  . SER   A 65  ? 0.1255 0.1290 0.1702 -0.0101 0.0063  0.0067  65  SER   A CB  
1571 O OG  . SER   A 65  ? 0.1282 0.1379 0.1807 -0.0106 -0.0014 0.0082  65  SER   A OG  
1577 N N   . ASP   A 66  ? 0.1257 0.1310 0.1776 -0.0042 0.0128  0.0076  66  ASP   A N   
1578 C CA  . ASP   A 66  ? 0.1385 0.1427 0.1996 0.0011  0.0109  0.0183  66  ASP   A CA  
1579 C C   . ASP   A 66  ? 0.1304 0.1374 0.2006 -0.0018 0.0110  0.0194  66  ASP   A C   
1580 O O   . ASP   A 66  ? 0.1435 0.1471 0.2216 -0.0007 0.0297  0.0207  66  ASP   A O   
1581 C CB  . ASP   A 66  ? 0.1475 0.1506 0.2283 0.0038  0.0126  0.0280  66  ASP   A CB  
1582 C CG  . ASP   A 66  ? 0.1709 0.1575 0.2510 0.0088  -0.0021 0.0414  66  ASP   A CG  
1583 O OD1 . ASP   A 66  ? 0.1687 0.1855 0.2281 -0.0032 -0.0081 0.0494  66  ASP   A OD1 
1584 O OD2 . ASP   A 66  ? 0.1907 0.1706 0.3296 0.0258  -0.0142 0.0178  66  ASP   A OD2 
1589 N N   . ASP   A 67  ? 0.1250 0.1403 0.2168 -0.0006 0.0038  0.0200  67  ASP   A N   
1590 C CA  . ASP   A 67  ? 0.1256 0.1573 0.2228 -0.0008 0.0010  0.0276  67  ASP   A CA  
1591 C C   . ASP   A 67  ? 0.1288 0.1535 0.2170 -0.0039 0.0155  0.0322  67  ASP   A C   
1592 O O   . ASP   A 67  ? 0.1308 0.1689 0.2367 -0.0009 0.0333  0.0388  67  ASP   A O   
1593 C CB  . ASP   A 67  ? 0.1328 0.1697 0.2568 -0.0049 -0.0119 0.0274  67  ASP   A CB  
1594 C CG  . ASP   A 67  ? 0.1315 0.1821 0.2805 -0.0074 -0.0276 0.0316  67  ASP   A CG  
1595 O OD1 . ASP   A 67  ? 0.1424 0.2038 0.3555 -0.0125 -0.0334 0.0431  67  ASP   A OD1 
1596 O OD2 . ASP   A 67  ? 0.1361 0.1775 0.2724 0.0024  -0.0205 0.0241  67  ASP   A OD2 
1601 N N   A TYR   A 68  ? 0.1288 0.1407 0.2031 0.0034  0.0282  0.0268  68  TYR   A N   
1602 N N   B TYR   A 68  ? 0.1335 0.1444 0.1980 0.0044  0.0172  0.0328  68  TYR   A N   
1603 C CA  A TYR   A 68  ? 0.1426 0.1360 0.2076 0.0002  0.0399  0.0217  68  TYR   A CA  
1604 C CA  B TYR   A 68  ? 0.1476 0.1409 0.1900 0.0050  0.0206  0.0327  68  TYR   A CA  
1605 C C   A TYR   A 68  ? 0.1468 0.1329 0.2028 0.0030  0.0310  0.0179  68  TYR   A C   
1606 C C   B TYR   A 68  ? 0.1466 0.1350 0.1898 0.0046  0.0287  0.0193  68  TYR   A C   
1607 O O   A TYR   A 68  ? 0.1493 0.1352 0.2116 0.0049  0.0280  0.0260  68  TYR   A O   
1608 O O   B TYR   A 68  ? 0.1481 0.1372 0.1911 0.0074  0.0405  0.0164  68  TYR   A O   
1609 C CB  A TYR   A 68  ? 0.1428 0.1328 0.2217 0.0019  0.0575  0.0094  68  TYR   A CB  
1610 C CB  B TYR   A 68  ? 0.1555 0.1424 0.1853 0.0100  0.0154  0.0383  68  TYR   A CB  
1611 C CG  A TYR   A 68  ? 0.1453 0.1438 0.2458 -0.0044 0.0759  0.0056  68  TYR   A CG  
1612 C CG  B TYR   A 68  ? 0.1647 0.1504 0.1847 0.0103  0.0111  0.0407  68  TYR   A CG  
1613 C CD1 A TYR   A 68  ? 0.1485 0.1466 0.2872 -0.0314 0.0600  -0.0163 68  TYR   A CD1 
1614 C CD1 B TYR   A 68  ? 0.1723 0.1512 0.1844 0.0106  0.0031  0.0417  68  TYR   A CD1 
1615 C CD2 A TYR   A 68  ? 0.1648 0.1506 0.2712 -0.0000 0.0757  0.0051  68  TYR   A CD2 
1616 C CD2 B TYR   A 68  ? 0.1748 0.1508 0.1860 0.0070  0.0038  0.0385  68  TYR   A CD2 
1617 C CE1 A TYR   A 68  ? 0.1500 0.1600 0.3173 -0.0307 0.0599  -0.0330 68  TYR   A CE1 
1618 C CE1 B TYR   A 68  ? 0.1768 0.1456 0.1717 0.0177  0.0008  0.0587  68  TYR   A CE1 
1619 C CE2 A TYR   A 68  ? 0.1591 0.1558 0.2972 -0.0023 0.0815  -0.0088 68  TYR   A CE2 
1620 C CE2 B TYR   A 68  ? 0.1740 0.1477 0.1648 0.0056  0.0042  0.0375  68  TYR   A CE2 
1621 C CZ  A TYR   A 68  ? 0.1464 0.1558 0.3333 -0.0251 0.0640  -0.0450 68  TYR   A CZ  
1622 C CZ  B TYR   A 68  ? 0.1795 0.1425 0.1550 0.0149  0.0022  0.0579  68  TYR   A CZ  
1623 O OH  A TYR   A 68  ? 0.1634 0.1716 0.3756 -0.0181 0.0434  -0.0813 68  TYR   A OH  
1624 O OH  B TYR   A 68  ? 0.1976 0.1443 0.1459 0.0238  -0.0139 0.0629  68  TYR   A OH  
1643 N N   . ILE   A 69  ? 0.1388 0.1287 0.1852 0.0019  0.0265  0.0122  69  ILE   A N   
1644 C CA  . ILE   A 69  ? 0.1413 0.1354 0.1818 0.0001  0.0209  -0.0031 69  ILE   A CA  
1645 C C   . ILE   A 69  ? 0.1452 0.1413 0.1775 0.0014  0.0168  0.0141  69  ILE   A C   
1646 O O   . ILE   A 69  ? 0.1524 0.1534 0.1698 -0.0013 0.0249  0.0190  69  ILE   A O   
1647 C CB  . ILE   A 69  ? 0.1481 0.1619 0.1947 0.0076  0.0124  -0.0105 69  ILE   A CB  
1648 C CG1 . ILE   A 69  ? 0.1468 0.1766 0.1966 0.0044  0.0175  -0.0257 69  ILE   A CG1 
1649 C CG2 . ILE   A 69  ? 0.1727 0.1839 0.2108 0.0075  0.0066  -0.0143 69  ILE   A CG2 
1650 C CD1 . ILE   A 69  ? 0.1516 0.1864 0.2021 0.0033  0.0145  -0.0329 69  ILE   A CD1 
1663 N N   . ALA   A 70  ? 0.1481 0.1402 0.1834 -0.0018 0.0221  0.0117  70  ALA   A N   
1664 C CA  . ALA   A 70  ? 0.1508 0.1529 0.1981 -0.0157 0.0301  0.0178  70  ALA   A CA  
1665 C C   . ALA   A 70  ? 0.1476 0.1643 0.1958 -0.0116 0.0288  0.0234  70  ALA   A C   
1666 O O   . ALA   A 70  ? 0.1665 0.1992 0.2206 0.0004  0.0470  0.0387  70  ALA   A O   
1667 C CB  . ALA   A 70  ? 0.1505 0.1537 0.2285 -0.0188 0.0299  0.0122  70  ALA   A CB  
1673 N N   . THR   A 71  ? 0.1413 0.1655 0.1845 -0.0051 0.0238  0.0287  71  THR   A N   
1674 C CA  . THR   A 71  ? 0.1513 0.1789 0.2182 0.0061  0.0212  0.0256  71  THR   A CA  
1675 C C   . THR   A 71  ? 0.1436 0.1707 0.2326 0.0131  0.0335  0.0224  71  THR   A C   
1676 O O   . THR   A 71  ? 0.1478 0.2004 0.2726 0.0113  0.0440  -0.0001 71  THR   A O   
1677 C CB  . THR   A 71  ? 0.1771 0.2015 0.2399 0.0149  -0.0094 0.0283  71  THR   A CB  
1678 O OG1 . THR   A 71  ? 0.2035 0.2238 0.2460 0.0053  -0.0272 0.0143  71  THR   A OG1 
1679 C CG2 . THR   A 71  ? 0.1892 0.2155 0.2644 0.0289  -0.0206 0.0442  71  THR   A CG2 
1687 N N   . ASN   A 72  ? 0.1466 0.1538 0.2146 0.0155  0.0273  0.0227  72  ASN   A N   
1688 C CA  . ASN   A 72  ? 0.1533 0.1570 0.2165 0.0151  0.0391  0.0253  72  ASN   A CA  
1689 C C   . ASN   A 72  ? 0.1684 0.1574 0.2144 0.0104  0.0533  0.0170  72  ASN   A C   
1690 O O   . ASN   A 72  ? 0.1833 0.1560 0.2425 0.0155  0.0496  0.0014  72  ASN   A O   
1691 C CB  . ASN   A 72  ? 0.1720 0.1657 0.2186 0.0150  0.0340  0.0173  72  ASN   A CB  
1692 C CG  . ASN   A 72  ? 0.1941 0.1716 0.2234 0.0248  0.0332  0.0225  72  ASN   A CG  
1693 O OD1 . ASN   A 72  ? 0.2132 0.2110 0.2445 0.0211  0.0438  0.0234  72  ASN   A OD1 
1694 N ND2 . ASN   A 72  ? 0.2081 0.1701 0.2277 0.0471  0.0224  0.0140  72  ASN   A ND2 
1701 N N   . GLY   A 73  ? 0.1734 0.1507 0.1940 0.0029  0.0505  0.0067  73  GLY   A N   
1702 C CA  . GLY   A 73  ? 0.1707 0.1527 0.1872 -0.0068 0.0460  0.0125  73  GLY   A CA  
1703 C C   . GLY   A 73  ? 0.1684 0.1441 0.1678 0.0038  0.0487  0.0212  73  GLY   A C   
1704 O O   . GLY   A 73  ? 0.1661 0.1474 0.1924 0.0098  0.0328  0.0245  73  GLY   A O   
1708 N N   . PRO   A 74  ? 0.1816 0.1448 0.1697 -0.0084 0.0426  0.0089  74  PRO   A N   
1709 C CA  . PRO   A 74  ? 0.1750 0.1442 0.1801 -0.0004 0.0382  0.0114  74  PRO   A CA  
1710 C C   . PRO   A 74  ? 0.1698 0.1268 0.1747 0.0028  0.0252  0.0093  74  PRO   A C   
1711 O O   . PRO   A 74  ? 0.1767 0.1338 0.2021 0.0051  0.0371  -0.0062 74  PRO   A O   
1712 C CB  . PRO   A 74  ? 0.1916 0.1727 0.2153 -0.0011 0.0385  0.0232  74  PRO   A CB  
1713 C CG  . PRO   A 74  ? 0.2102 0.2045 0.2400 -0.0154 0.0360  0.0120  74  PRO   A CG  
1714 C CD  . PRO   A 74  ? 0.1902 0.1814 0.1856 -0.0147 0.0403  0.0055  74  PRO   A CD  
1722 N N   . LEU   A 75  ? 0.1650 0.1212 0.1756 0.0027  0.0343  0.0045  75  LEU   A N   
1723 C CA  . LEU   A 75  ? 0.1676 0.1270 0.1526 0.0020  0.0148  0.0038  75  LEU   A CA  
1724 C C   . LEU   A 75  ? 0.1742 0.1374 0.1469 0.0093  0.0192  0.0153  75  LEU   A C   
1725 O O   . LEU   A 75  ? 0.2075 0.1538 0.1555 0.0101  0.0079  0.0129  75  LEU   A O   
1726 C CB  . LEU   A 75  ? 0.1695 0.1312 0.1374 -0.0070 0.0086  0.0148  75  LEU   A CB  
1727 C CG  . LEU   A 75  ? 0.1899 0.1588 0.1617 -0.0419 0.0081  0.0110  75  LEU   A CG  
1728 C CD1 . LEU   A 75  ? 0.1958 0.2102 0.1742 -0.0377 0.0124  -0.0053 75  LEU   A CD1 
1729 C CD2 . LEU   A 75  ? 0.2212 0.2081 0.2171 -0.0178 0.0142  0.0182  75  LEU   A CD2 
1741 N N   . LYS   A 76  ? 0.1766 0.1329 0.1606 -0.0021 0.0187  0.0059  76  LYS   A N   
1742 C CA  . LYS   A 76  ? 0.1711 0.1507 0.1700 -0.0058 0.0134  -0.0103 76  LYS   A CA  
1743 C C   . LYS   A 76  ? 0.1688 0.1352 0.1340 -0.0007 0.0050  0.0062  76  LYS   A C   
1744 O O   . LYS   A 76  ? 0.1697 0.1323 0.1468 -0.0029 0.0116  0.0076  76  LYS   A O   
1745 C CB  . LYS   A 76  ? 0.1713 0.1735 0.2121 0.0040  0.0186  -0.0359 76  LYS   A CB  
1746 C CG  . LYS   A 76  ? 0.1803 0.1672 0.2556 0.0071  0.0071  -0.0289 76  LYS   A CG  
1747 C CD  . LYS   A 76  ? 0.1869 0.1705 0.2851 0.0117  0.0026  -0.0442 76  LYS   A CD  
1748 C CE  . LYS   A 76  ? 0.2027 0.1951 0.3377 -0.0008 0.0092  -0.0538 76  LYS   A CE  
1749 N NZ  . LYS   A 76  ? 0.2008 0.1918 0.3776 -0.0120 0.0109  -0.0656 76  LYS   A NZ  
1763 N N   . VAL   A 77  ? 0.1790 0.1472 0.1325 -0.0018 0.0228  0.0155  77  VAL   A N   
1764 C CA  . VAL   A 77  ? 0.1746 0.1516 0.1403 0.0066  0.0152  0.0201  77  VAL   A CA  
1765 C C   . VAL   A 77  ? 0.1722 0.1451 0.1401 0.0086  0.0136  0.0088  77  VAL   A C   
1766 O O   . VAL   A 77  ? 0.1792 0.1443 0.1401 0.0187  0.0254  0.0018  77  VAL   A O   
1767 C CB  . VAL   A 77  ? 0.1921 0.1706 0.1570 0.0028  0.0073  0.0270  77  VAL   A CB  
1768 C CG1 . VAL   A 77  ? 0.1879 0.1829 0.1859 0.0128  0.0007  0.0119  77  VAL   A CG1 
1769 C CG2 . VAL   A 77  ? 0.2130 0.1806 0.1892 -0.0028 -0.0017 0.0320  77  VAL   A CG2 
1779 N N   . GLY   A 78  ? 0.1626 0.1354 0.1314 0.0100  0.0209  0.0145  78  GLY   A N   
1780 C CA  . GLY   A 78  ? 0.1595 0.1368 0.1404 0.0056  0.0204  0.0164  78  GLY   A CA  
1781 C C   . GLY   A 78  ? 0.1492 0.1278 0.1343 0.0030  0.0141  0.0118  78  GLY   A C   
1782 O O   . GLY   A 78  ? 0.1488 0.1367 0.1589 0.0064  0.0119  0.0250  78  GLY   A O   
1786 N N   . GLY   A 79  ? 0.1533 0.1303 0.1430 0.0035  0.0154  0.0118  79  GLY   A N   
1787 C CA  . GLY   A 79  ? 0.1451 0.1299 0.1584 -0.0004 0.0191  0.0086  79  GLY   A CA  
1788 C C   . GLY   A 79  ? 0.1324 0.1219 0.1601 -0.0025 0.0143  0.0066  79  GLY   A C   
1789 O O   . GLY   A 79  ? 0.1394 0.1365 0.1525 0.0198  0.0103  0.0059  79  GLY   A O   
1793 N N   . SER   A 80  ? 0.1273 0.1381 0.1782 -0.0038 0.0138  0.0001  80  SER   A N   
1794 C CA  . SER   A 80  ? 0.1256 0.1351 0.1583 -0.0059 0.0075  0.0005  80  SER   A CA  
1795 C C   . SER   A 80  ? 0.1268 0.1352 0.1518 -0.0051 0.0150  0.0078  80  SER   A C   
1796 O O   . SER   A 80  ? 0.1250 0.1519 0.1882 0.0077  0.0136  -0.0051 80  SER   A O   
1797 C CB  . SER   A 80  ? 0.1379 0.1372 0.1836 -0.0054 -0.0011 0.0129  80  SER   A CB  
1798 O OG  . SER   A 80  ? 0.1592 0.1336 0.2209 0.0062  -0.0058 0.0178  80  SER   A OG  
1804 N N   . CYS   A 81  ? 0.1214 0.1311 0.1478 -0.0015 0.0030  0.0069  81  CYS   A N   
1805 C CA  . CYS   A 81  ? 0.1189 0.1391 0.1528 -0.0085 -0.0011 0.0190  81  CYS   A CA  
1806 C C   . CYS   A 81  ? 0.1257 0.1328 0.1458 -0.0144 -0.0011 0.0238  81  CYS   A C   
1807 O O   . CYS   A 81  ? 0.1270 0.1598 0.1679 -0.0030 0.0089  0.0227  81  CYS   A O   
1808 C CB  . CYS   A 81  ? 0.1331 0.1462 0.1711 -0.0180 0.0070  0.0146  81  CYS   A CB  
1809 S SG  . CYS   A 81  ? 0.1501 0.1319 0.1718 -0.0152 0.0048  0.0063  81  CYS   A SG  
1815 N N   . VAL   A 82  ? 0.1299 0.1450 0.1557 -0.0050 -0.0142 0.0118  82  VAL   A N   
1816 C CA  . VAL   A 82  ? 0.1424 0.1473 0.1573 -0.0050 -0.0095 0.0223  82  VAL   A CA  
1817 C C   . VAL   A 82  ? 0.1392 0.1500 0.1615 -0.0092 -0.0128 0.0221  82  VAL   A C   
1818 O O   . VAL   A 82  ? 0.1355 0.1630 0.1943 -0.0086 -0.0024 0.0001  82  VAL   A O   
1819 C CB  . VAL   A 82  ? 0.1714 0.1618 0.1759 -0.0032 -0.0020 0.0225  82  VAL   A CB  
1820 C CG1 . VAL   A 82  ? 0.1862 0.1781 0.1939 0.0030  0.0080  0.0197  82  VAL   A CG1 
1821 C CG2 . VAL   A 82  ? 0.1801 0.1631 0.1999 -0.0043 -0.0070 0.0241  82  VAL   A CG2 
1831 N N   . LEU   A 83  ? 0.1379 0.1411 0.1570 -0.0107 -0.0090 0.0098  83  LEU   A N   
1832 C CA  . LEU   A 83  ? 0.1402 0.1518 0.1483 -0.0118 -0.0068 0.0004  83  LEU   A CA  
1833 C C   . LEU   A 83  ? 0.1453 0.1551 0.1492 -0.0176 -0.0095 -0.0008 83  LEU   A C   
1834 O O   . LEU   A 83  ? 0.1552 0.1583 0.1631 -0.0218 0.0008  0.0089  83  LEU   A O   
1835 C CB  . LEU   A 83  ? 0.1456 0.1583 0.1523 -0.0115 -0.0059 0.0160  83  LEU   A CB  
1836 C CG  . LEU   A 83  ? 0.1554 0.1675 0.1585 -0.0139 0.0037  0.0094  83  LEU   A CG  
1837 C CD1 . LEU   A 83  ? 0.1728 0.1623 0.1546 -0.0230 0.0004  0.0231  83  LEU   A CD1 
1838 C CD2 . LEU   A 83  ? 0.1551 0.1810 0.1848 -0.0168 0.0200  0.0144  83  LEU   A CD2 
1850 N N   . SER   A 84  ? 0.1575 0.1603 0.1458 -0.0183 -0.0079 0.0035  84  SER   A N   
1851 C CA  . SER   A 84  ? 0.1696 0.1716 0.1306 -0.0150 -0.0086 -0.0028 84  SER   A CA  
1852 C C   . SER   A 84  ? 0.1682 0.1641 0.1323 -0.0232 0.0012  0.0024  84  SER   A C   
1853 O O   . SER   A 84  ? 0.1647 0.1788 0.1367 -0.0215 -0.0110 0.0012  84  SER   A O   
1854 C CB  . SER   A 84  ? 0.1827 0.1909 0.1465 -0.0144 -0.0040 -0.0039 84  SER   A CB  
1855 O OG  . SER   A 84  ? 0.1866 0.2075 0.1589 -0.0126 -0.0114 -0.0227 84  SER   A OG  
1861 N N   . GLY   A 85  ? 0.1859 0.1814 0.1462 -0.0288 0.0168  -0.0051 85  GLY   A N   
1862 C CA  . GLY   A 85  ? 0.1876 0.1902 0.1668 -0.0364 0.0172  -0.0129 85  GLY   A CA  
1863 C C   . GLY   A 85  ? 0.1882 0.1977 0.1568 -0.0263 0.0060  -0.0197 85  GLY   A C   
1864 O O   . GLY   A 85  ? 0.1831 0.2073 0.1595 -0.0322 0.0206  -0.0222 85  GLY   A O   
1868 N N   . HIS   A 86  ? 0.1917 0.1856 0.1472 -0.0288 0.0045  -0.0117 86  HIS   A N   
1869 C CA  . HIS   A 86  ? 0.2033 0.1985 0.1326 -0.0356 0.0119  -0.0101 86  HIS   A CA  
1870 C C   . HIS   A 86  ? 0.2260 0.2060 0.1442 -0.0401 0.0123  -0.0121 86  HIS   A C   
1871 O O   . HIS   A 86  ? 0.2407 0.2261 0.1487 -0.0292 0.0170  -0.0108 86  HIS   A O   
1872 C CB  . HIS   A 86  ? 0.1996 0.1899 0.1414 -0.0276 0.0116  -0.0090 86  HIS   A CB  
1873 C CG  . HIS   A 86  ? 0.1875 0.1834 0.1436 -0.0170 0.0095  0.0010  86  HIS   A CG  
1874 N ND1 . HIS   A 86  ? 0.1925 0.1816 0.1805 -0.0293 -0.0019 0.0024  86  HIS   A ND1 
1875 C CD2 . HIS   A 86  ? 0.1798 0.1715 0.1427 -0.0089 0.0044  -0.0022 86  HIS   A CD2 
1876 C CE1 . HIS   A 86  ? 0.1822 0.1782 0.1776 -0.0247 0.0156  0.0059  86  HIS   A CE1 
1877 N NE2 . HIS   A 86  ? 0.1785 0.1713 0.1587 -0.0070 0.0150  0.0156  86  HIS   A NE2 
1885 N N   . ASN   A 87  ? 0.2395 0.2159 0.1540 -0.0334 0.0367  -0.0281 87  ASN   A N   
1886 C CA  . ASN   A 87  ? 0.2526 0.2274 0.1582 -0.0235 0.0575  -0.0322 87  ASN   A CA  
1887 C C   . ASN   A 87  ? 0.2439 0.2425 0.1933 -0.0261 0.0686  -0.0154 87  ASN   A C   
1888 O O   . ASN   A 87  ? 0.2632 0.2603 0.2400 -0.0351 0.0968  -0.0175 87  ASN   A O   
1889 C CB  . ASN   A 87  ? 0.2716 0.2357 0.1788 -0.0142 0.0638  -0.0331 87  ASN   A CB  
1890 C CG  . ASN   A 87  ? 0.2840 0.2464 0.1911 -0.0025 0.0723  -0.0200 87  ASN   A CG  
1891 O OD1 . ASN   A 87  ? 0.2963 0.2462 0.1923 0.0158  0.0627  -0.0106 87  ASN   A OD1 
1892 N ND2 . ASN   A 87  ? 0.2921 0.2693 0.2173 -0.0027 0.0712  -0.0131 87  ASN   A ND2 
1899 N N   A LEU   A 88  ? 0.2271 0.2359 0.1897 -0.0320 0.0479  -0.0039 88  LEU   A N   
1900 N N   B LEU   A 88  ? 0.2304 0.2380 0.1917 -0.0312 0.0546  -0.0108 88  LEU   A N   
1901 C CA  A LEU   A 88  ? 0.2120 0.2335 0.2001 -0.0365 0.0385  0.0010  88  LEU   A CA  
1902 C CA  B LEU   A 88  ? 0.2178 0.2360 0.1991 -0.0348 0.0484  -0.0097 88  LEU   A CA  
1903 C C   A LEU   A 88  ? 0.2078 0.2339 0.1913 -0.0393 0.0410  0.0150  88  LEU   A C   
1904 C C   B LEU   A 88  ? 0.2121 0.2339 0.1913 -0.0373 0.0452  0.0079  88  LEU   A C   
1905 O O   A LEU   A 88  ? 0.2137 0.2407 0.2238 -0.0399 0.0474  0.0285  88  LEU   A O   
1906 O O   B LEU   A 88  ? 0.2164 0.2392 0.2148 -0.0368 0.0514  0.0204  88  LEU   A O   
1907 C CB  A LEU   A 88  ? 0.2098 0.2390 0.2251 -0.0396 0.0071  0.0067  88  LEU   A CB  
1908 C CB  B LEU   A 88  ? 0.2168 0.2420 0.2187 -0.0362 0.0328  -0.0165 88  LEU   A CB  
1909 C CG  A LEU   A 88  ? 0.2236 0.2485 0.2592 -0.0352 -0.0062 0.0095  88  LEU   A CG  
1910 C CG  B LEU   A 88  ? 0.2240 0.2494 0.2398 -0.0325 0.0281  -0.0258 88  LEU   A CG  
1911 C CD1 A LEU   A 88  ? 0.2325 0.2558 0.2593 -0.0318 -0.0076 0.0059  88  LEU   A CD1 
1912 C CD1 B LEU   A 88  ? 0.2287 0.2531 0.2336 -0.0297 0.0300  -0.0387 88  LEU   A CD1 
1913 C CD2 A LEU   A 88  ? 0.2333 0.2580 0.2901 -0.0293 -0.0078 0.0065  88  LEU   A CD2 
1914 C CD2 B LEU   A 88  ? 0.2295 0.2561 0.2629 -0.0285 0.0266  -0.0262 88  LEU   A CD2 
1937 N N   . ALA   A 89  ? 0.2106 0.2236 0.1748 -0.0374 0.0359  0.0072  89  ALA   A N   
1938 C CA  . ALA   A 89  ? 0.2206 0.2216 0.1550 -0.0363 0.0240  0.0110  89  ALA   A CA  
1939 C C   . ALA   A 89  ? 0.2216 0.2252 0.1633 -0.0374 0.0070  0.0060  89  ALA   A C   
1940 O O   . ALA   A 89  ? 0.2241 0.2262 0.1863 -0.0431 -0.0090 -0.0152 89  ALA   A O   
1941 C CB  . ALA   A 89  ? 0.2151 0.2235 0.1468 -0.0293 0.0203  0.0106  89  ALA   A CB  
1948 N N   . LYS   A 90  ? 0.2296 0.2345 0.1553 -0.0462 -0.0089 0.0150  90  LYS   A N   
1949 C CA  . LYS   A 90  ? 0.2388 0.2484 0.1642 -0.0443 -0.0179 0.0136  90  LYS   A CA  
1950 C C   . LYS   A 90  ? 0.2144 0.2337 0.1600 -0.0424 -0.0206 0.0110  90  LYS   A C   
1951 O O   . LYS   A 90  ? 0.2108 0.2498 0.1903 -0.0428 -0.0362 -0.0020 90  LYS   A O   
1952 C CB  . LYS   A 90  ? 0.2674 0.2827 0.2100 -0.0407 -0.0192 0.0211  90  LYS   A CB  
1953 C CG  . LYS   A 90  ? 0.3077 0.3174 0.3113 -0.0409 -0.0118 0.0250  90  LYS   A CG  
1954 C CD  . LYS   A 90  ? 0.3438 0.3513 0.4114 -0.0426 0.0033  0.0291  90  LYS   A CD  
1955 C CE  . LYS   A 90  ? 0.3712 0.3751 0.4871 -0.0438 0.0125  0.0245  90  LYS   A CE  
1956 N NZ  . LYS   A 90  ? 0.3839 0.3878 0.5354 -0.0417 0.0163  0.0207  90  LYS   A NZ  
1970 N N   . HIS   A 91  ? 0.2011 0.2047 0.1270 -0.0345 -0.0284 0.0091  91  HIS   A N   
1971 C CA  . HIS   A 91  ? 0.1920 0.1866 0.1327 -0.0267 -0.0265 0.0151  91  HIS   A CA  
1972 C C   . HIS   A 91  ? 0.1678 0.1735 0.1118 -0.0200 -0.0134 0.0219  91  HIS   A C   
1973 O O   . HIS   A 91  ? 0.1616 0.1851 0.1492 -0.0249 0.0049  0.0179  91  HIS   A O   
1974 C CB  . HIS   A 91  ? 0.2096 0.2165 0.1871 -0.0038 -0.0409 0.0083  91  HIS   A CB  
1975 C CG  . HIS   A 91  ? 0.2478 0.2643 0.2638 0.0070  -0.0649 -0.0003 91  HIS   A CG  
1976 N ND1 . HIS   A 91  ? 0.2571 0.2911 0.3064 0.0148  -0.0720 -0.0180 91  HIS   A ND1 
1977 C CD2 . HIS   A 91  ? 0.2679 0.2821 0.2953 0.0191  -0.0734 0.0097  91  HIS   A CD2 
1978 C CE1 . HIS   A 91  ? 0.2688 0.2958 0.3228 0.0236  -0.0695 -0.0027 91  HIS   A CE1 
1979 N NE2 . HIS   A 91  ? 0.2802 0.2948 0.3234 0.0293  -0.0744 0.0047  91  HIS   A NE2 
1987 N N   . CYS   A 92  ? 0.1532 0.1633 0.1223 -0.0161 -0.0056 0.0137  92  CYS   A N   
1988 C CA  . CYS   A 92  ? 0.1488 0.1578 0.1384 -0.0159 -0.0004 0.0105  92  CYS   A CA  
1989 C C   . CYS   A 92  ? 0.1369 0.1472 0.1380 -0.0199 -0.0039 0.0073  92  CYS   A C   
1990 O O   . CYS   A 92  ? 0.1410 0.1579 0.1528 -0.0242 -0.0002 0.0062  92  CYS   A O   
1991 C CB  . CYS   A 92  ? 0.1512 0.1529 0.1508 -0.0105 0.0018  0.0023  92  CYS   A CB  
1992 S SG  . CYS   A 92  ? 0.1460 0.1434 0.1528 -0.0131 0.0026  0.0067  92  CYS   A SG  
1998 N N   . LEU   A 93  ? 0.1374 0.1308 0.1366 -0.0126 0.0077  0.0039  93  LEU   A N   
1999 C CA  . LEU   A 93  ? 0.1279 0.1265 0.1378 -0.0075 -0.0002 0.0106  93  LEU   A CA  
2000 C C   . LEU   A 93  ? 0.1260 0.1188 0.1430 -0.0063 0.0110  0.0063  93  LEU   A C   
2001 O O   . LEU   A 93  ? 0.1214 0.1312 0.1397 -0.0057 0.0045  0.0125  93  LEU   A O   
2002 C CB  . LEU   A 93  ? 0.1334 0.1258 0.1600 -0.0058 -0.0028 0.0230  93  LEU   A CB  
2003 C CG  . LEU   A 93  ? 0.1382 0.1298 0.1570 -0.0036 0.0003  0.0183  93  LEU   A CG  
2004 C CD1 . LEU   A 93  ? 0.1481 0.1376 0.1746 -0.0019 0.0083  0.0145  93  LEU   A CD1 
2005 C CD2 . LEU   A 93  ? 0.1483 0.1270 0.1756 -0.0100 -0.0017 0.0156  93  LEU   A CD2 
2017 N N   . HIS   A 94  ? 0.1192 0.1183 0.1407 -0.0047 0.0080  0.0153  94  HIS   A N   
2018 C CA  . HIS   A 94  ? 0.1205 0.1237 0.1468 -0.0077 0.0065  0.0126  94  HIS   A CA  
2019 C C   . HIS   A 94  ? 0.1182 0.1171 0.1529 -0.0084 0.0095  0.0098  94  HIS   A C   
2020 O O   . HIS   A 94  ? 0.1189 0.1366 0.1704 0.0009  0.0058  -0.0117 94  HIS   A O   
2021 C CB  . HIS   A 94  ? 0.1211 0.1235 0.1487 -0.0081 -0.0014 0.0173  94  HIS   A CB  
2022 C CG  . HIS   A 94  ? 0.1254 0.1206 0.1355 -0.0084 -0.0002 0.0126  94  HIS   A CG  
2023 N ND1 . HIS   A 94  ? 0.1268 0.1201 0.1442 -0.0015 0.0110  0.0055  94  HIS   A ND1 
2024 C CD2 . HIS   A 94  ? 0.1280 0.1393 0.1381 -0.0093 0.0000  0.0025  94  HIS   A CD2 
2025 C CE1 . HIS   A 94  ? 0.1294 0.1255 0.1342 -0.0113 -0.0053 0.0054  94  HIS   A CE1 
2026 N NE2 . HIS   A 94  ? 0.1326 0.1292 0.1395 -0.0119 -0.0065 0.0016  94  HIS   A NE2 
2034 N N   . VAL   A 95  ? 0.1147 0.1103 0.1349 -0.0044 0.0124  0.0029  95  VAL   A N   
2035 C CA  . VAL   A 95  ? 0.1241 0.1231 0.1248 -0.0017 0.0146  0.0118  95  VAL   A CA  
2036 C C   . VAL   A 95  ? 0.1256 0.1167 0.1162 -0.0121 0.0041  0.0051  95  VAL   A C   
2037 O O   . VAL   A 95  ? 0.1313 0.1303 0.1418 0.0103  0.0042  0.0064  95  VAL   A O   
2038 C CB  . VAL   A 95  ? 0.1275 0.1249 0.1451 -0.0137 0.0053  0.0059  95  VAL   A CB  
2039 C CG1 . VAL   A 95  ? 0.1404 0.1254 0.1530 -0.0110 0.0012  -0.0008 95  VAL   A CG1 
2040 C CG2 . VAL   A 95  ? 0.1352 0.1252 0.1392 -0.0171 0.0016  0.0230  95  VAL   A CG2 
2050 N N   . VAL   A 96  ? 0.1265 0.1220 0.1212 -0.0061 0.0025  0.0136  96  VAL   A N   
2051 C CA  . VAL   A 96  ? 0.1400 0.1245 0.1296 -0.0027 0.0054  0.0195  96  VAL   A CA  
2052 C C   . VAL   A 96  ? 0.1378 0.1298 0.1405 0.0018  0.0068  0.0203  96  VAL   A C   
2053 O O   . VAL   A 96  ? 0.1468 0.1345 0.1623 -0.0003 0.0122  0.0011  96  VAL   A O   
2054 C CB  . VAL   A 96  ? 0.1443 0.1277 0.1448 -0.0016 0.0192  0.0173  96  VAL   A CB  
2055 C CG1 . VAL   A 96  ? 0.1485 0.1373 0.1199 0.0043  0.0178  0.0181  96  VAL   A CG1 
2056 C CG2 . VAL   A 96  ? 0.1431 0.1392 0.1650 -0.0131 0.0112  0.0170  96  VAL   A CG2 
2066 N N   A GLY   A 97  ? 0.1347 0.1315 0.1427 -0.0019 0.0109  0.0208  97  GLY   A N   
2067 N N   B GLY   A 97  ? 0.1422 0.1389 0.1470 -0.0003 0.0065  0.0203  97  GLY   A N   
2068 C CA  A GLY   A 97  ? 0.1370 0.1394 0.1475 -0.0038 0.0055  0.0151  97  GLY   A CA  
2069 C CA  B GLY   A 97  ? 0.1481 0.1477 0.1504 -0.0039 0.0078  0.0238  97  GLY   A CA  
2070 C C   A GLY   A 97  ? 0.1375 0.1497 0.1269 -0.0021 0.0031  0.0079  97  GLY   A C   
2071 C C   B GLY   A 97  ? 0.1559 0.1568 0.1541 -0.0020 0.0066  0.0282  97  GLY   A C   
2072 O O   A GLY   A 97  ? 0.1551 0.1546 0.1379 -0.0013 0.0105  0.0052  97  GLY   A O   
2073 O O   B GLY   A 97  ? 0.1658 0.1560 0.1617 -0.0028 0.0081  0.0279  97  GLY   A O   
2080 N N   A PRO   A 98  ? 0.1467 0.1481 0.1150 0.0024  -0.0049 0.0153  98  PRO   A N   
2081 N N   B PRO   A 98  ? 0.1719 0.1659 0.1623 0.0012  0.0013  0.0345  98  PRO   A N   
2082 C CA  A PRO   A 98  ? 0.1514 0.1600 0.1134 0.0075  -0.0041 0.0044  98  PRO   A CA  
2083 C CA  B PRO   A 98  ? 0.1880 0.1762 0.1730 0.0008  -0.0049 0.0234  98  PRO   A CA  
2084 C C   A PRO   A 98  ? 0.1522 0.1654 0.1009 -0.0025 0.0121  0.0082  98  PRO   A C   
2085 C C   B PRO   A 98  ? 0.2125 0.1824 0.1766 -0.0013 -0.0094 0.0386  98  PRO   A C   
2086 O O   A PRO   A 98  ? 0.1543 0.1540 0.1208 -0.0052 0.0065  0.0052  98  PRO   A O   
2087 O O   B PRO   A 98  ? 0.2073 0.1793 0.1873 0.0002  -0.0063 0.0409  98  PRO   A O   
2088 C CB  A PRO   A 98  ? 0.1632 0.1659 0.1132 0.0187  -0.0063 -0.0073 98  PRO   A CB  
2089 C CB  B PRO   A 98  ? 0.1889 0.1751 0.1632 0.0080  -0.0095 0.0196  98  PRO   A CB  
2090 C CG  A PRO   A 98  ? 0.1626 0.1570 0.1264 0.0202  -0.0148 -0.0085 98  PRO   A CG  
2091 C CG  B PRO   A 98  ? 0.1904 0.1702 0.1661 0.0080  -0.0093 0.0266  98  PRO   A CG  
2092 C CD  A PRO   A 98  ? 0.1548 0.1466 0.1263 0.0126  -0.0111 0.0100  98  PRO   A CD  
2093 C CD  B PRO   A 98  ? 0.1781 0.1641 0.1612 0.0072  -0.0066 0.0336  98  PRO   A CD  
2108 N N   A ASN   A 99  ? 0.1600 0.1867 0.0942 0.0040  0.0173  0.0247  99  ASN   A N   
2109 N N   B ASN   A 99  ? 0.2458 0.1912 0.1721 0.0034  -0.0180 0.0551  99  ASN   A N   
2110 C CA  A ASN   A 99  ? 0.1802 0.2041 0.1034 0.0067  0.0096  0.0342  99  ASN   A CA  
2111 C CA  B ASN   A 99  ? 0.2804 0.2040 0.1889 0.0129  -0.0231 0.0697  99  ASN   A CA  
2112 C C   A ASN   A 99  ? 0.1942 0.2367 0.0950 0.0060  0.0145  0.0411  99  ASN   A C   
2113 C C   B ASN   A 99  ? 0.3003 0.2191 0.1976 0.0170  -0.0281 0.0777  99  ASN   A C   
2114 O O   A ASN   A 99  ? 0.2013 0.2582 0.1197 0.0145  0.0132  0.0373  99  ASN   A O   
2115 O O   B ASN   A 99  ? 0.3031 0.2146 0.1872 0.0206  -0.0212 0.0840  99  ASN   A O   
2116 C CB  A ASN   A 99  ? 0.1828 0.1954 0.1171 0.0069  -0.0027 0.0326  99  ASN   A CB  
2117 C CB  B ASN   A 99  ? 0.2922 0.2037 0.2116 0.0188  -0.0256 0.0685  99  ASN   A CB  
2118 C CG  A ASN   A 99  ? 0.1837 0.1916 0.1521 0.0145  -0.0068 0.0251  99  ASN   A CG  
2119 C CG  B ASN   A 99  ? 0.3033 0.2078 0.2361 0.0212  -0.0301 0.0647  99  ASN   A CG  
2120 O OD1 A ASN   A 99  ? 0.1929 0.1982 0.1604 0.0252  -0.0011 0.0063  99  ASN   A OD1 
2121 O OD1 B ASN   A 99  ? 0.3065 0.2105 0.2367 0.0293  -0.0395 0.0644  99  ASN   A OD1 
2122 N ND2 A ASN   A 99  ? 0.1816 0.1859 0.1850 0.0105  -0.0140 0.0412  99  ASN   A ND2 
2123 N ND2 B ASN   A 99  ? 0.3075 0.2115 0.2605 0.0190  -0.0335 0.0627  99  ASN   A ND2 
2136 N N   A VAL   A 100 ? 0.2073 0.2445 0.0896 -0.0057 -0.0106 0.0293  100 VAL   A N   
2137 N N   B VAL   A 100 ? 0.3209 0.2502 0.2357 0.0183  -0.0318 0.0721  100 VAL   A N   
2138 C CA  A VAL   A 100 ? 0.2289 0.2630 0.1197 -0.0091 -0.0209 0.0284  100 VAL   A CA  
2139 C CA  B VAL   A 100 ? 0.3422 0.2764 0.2749 0.0179  -0.0334 0.0599  100 VAL   A CA  
2140 C C   A VAL   A 100 ? 0.2350 0.2712 0.0996 -0.0167 -0.0276 0.0444  100 VAL   A C   
2141 C C   B VAL   A 100 ? 0.3556 0.2902 0.2910 0.0237  -0.0301 0.0520  100 VAL   A C   
2142 O O   A VAL   A 100 ? 0.2466 0.2786 0.1271 -0.0172 -0.0117 0.0395  100 VAL   A O   
2143 O O   B VAL   A 100 ? 0.3590 0.2901 0.2951 0.0208  -0.0350 0.0503  100 VAL   A O   
2144 C CB  A VAL   A 100 ? 0.2507 0.2715 0.1906 -0.0186 -0.0274 0.0184  100 VAL   A CB  
2145 C CB  B VAL   A 100 ? 0.3488 0.2889 0.3014 0.0117  -0.0327 0.0518  100 VAL   A CB  
2146 C CG1 A VAL   A 100 ? 0.2515 0.2802 0.2162 -0.0262 -0.0207 0.0219  100 VAL   A CG1 
2147 C CG1 B VAL   A 100 ? 0.3491 0.2923 0.3078 0.0107  -0.0370 0.0500  100 VAL   A CG1 
2148 C CG2 A VAL   A 100 ? 0.2610 0.2770 0.2109 -0.0198 -0.0301 0.0153  100 VAL   A CG2 
2149 C CG2 B VAL   A 100 ? 0.3533 0.2937 0.3133 0.0087  -0.0329 0.0518  100 VAL   A CG2 
2168 N N   A ASN   A 101 ? 0.2365 0.2764 0.1281 -0.0167 -0.0274 0.0641  101 ASN   A N   
2169 N N   B ASN   A 101 ? 0.3660 0.3083 0.2992 0.0309  -0.0211 0.0397  101 ASN   A N   
2170 C CA  A ASN   A 101 ? 0.2506 0.2838 0.1525 -0.0186 -0.0235 0.0791  101 ASN   A CA  
2171 C CA  B ASN   A 101 ? 0.3754 0.3258 0.3121 0.0398  -0.0075 0.0324  101 ASN   A CA  
2172 C C   A ASN   A 101 ? 0.2645 0.3102 0.1773 -0.0193 0.0031  0.1044  101 ASN   A C   
2173 C C   B ASN   A 101 ? 0.3783 0.3351 0.3152 0.0354  -0.0044 0.0369  101 ASN   A C   
2174 O O   A ASN   A 101 ? 0.2765 0.3117 0.2218 -0.0143 0.0100  0.0942  101 ASN   A O   
2175 O O   B ASN   A 101 ? 0.3816 0.3359 0.3263 0.0359  0.0029  0.0354  101 ASN   A O   
2176 C CB  A ASN   A 101 ? 0.2520 0.2709 0.1597 -0.0167 -0.0458 0.0608  101 ASN   A CB  
2177 C CB  B ASN   A 101 ? 0.3819 0.3347 0.3255 0.0496  0.0046  0.0212  101 ASN   A CB  
2178 C CG  A ASN   A 101 ? 0.2574 0.2646 0.1717 -0.0224 -0.0550 0.0302  101 ASN   A CG  
2179 C CG  B ASN   A 101 ? 0.3875 0.3438 0.3418 0.0557  0.0181  0.0085  101 ASN   A CG  
2180 O OD1 A ASN   A 101 ? 0.2613 0.2742 0.1871 -0.0095 -0.0518 -0.0031 101 ASN   A OD1 
2181 O OD1 B ASN   A 101 ? 0.3881 0.3463 0.3507 0.0574  0.0234  0.0032  101 ASN   A OD1 
2182 N ND2 A ASN   A 101 ? 0.2629 0.2579 0.1727 -0.0334 -0.0594 0.0369  101 ASN   A ND2 
2183 N ND2 B ASN   A 101 ? 0.3909 0.3484 0.3465 0.0580  0.0234  0.0035  101 ASN   A ND2 
2196 N N   A LYS   A 102 ? 0.2636 0.3399 0.2048 -0.0242 0.0136  0.1090  102 LYS   A N   
2197 N N   B LYS   A 102 ? 0.3766 0.3436 0.3154 0.0310  -0.0081 0.0400  102 LYS   A N   
2198 C CA  A LYS   A 102 ? 0.2722 0.3695 0.2266 -0.0222 0.0208  0.1004  102 LYS   A CA  
2199 C CA  B LYS   A 102 ? 0.3737 0.3525 0.3178 0.0228  -0.0051 0.0459  102 LYS   A CA  
2200 C C   A LYS   A 102 ? 0.2827 0.3967 0.2189 -0.0122 0.0275  0.0893  102 LYS   A C   
2201 C C   B LYS   A 102 ? 0.3674 0.3510 0.2987 0.0208  -0.0038 0.0502  102 LYS   A C   
2202 O O   A LYS   A 102 ? 0.2876 0.4090 0.2384 -0.0079 0.0279  0.0797  102 LYS   A O   
2203 O O   B LYS   A 102 ? 0.3678 0.3542 0.3084 0.0261  0.0020  0.0516  102 LYS   A O   
2204 C CB  A LYS   A 102 ? 0.2725 0.3693 0.2519 -0.0315 0.0240  0.1036  102 LYS   A CB  
2205 C CB  B LYS   A 102 ? 0.3757 0.3603 0.3460 0.0161  -0.0052 0.0447  102 LYS   A CB  
2206 C CG  A LYS   A 102 ? 0.2734 0.3668 0.2702 -0.0374 0.0207  0.0984  102 LYS   A CG  
2207 C CG  B LYS   A 102 ? 0.3767 0.3676 0.3745 0.0099  -0.0056 0.0457  102 LYS   A CG  
2208 C CD  A LYS   A 102 ? 0.2820 0.3665 0.2913 -0.0373 0.0122  0.0827  102 LYS   A CD  
2209 C CD  B LYS   A 102 ? 0.3774 0.3739 0.3996 0.0042  -0.0049 0.0469  102 LYS   A CD  
2210 C CE  A LYS   A 102 ? 0.2919 0.3659 0.3084 -0.0361 0.0049  0.0729  102 LYS   A CE  
2211 C CE  B LYS   A 102 ? 0.3775 0.3783 0.4204 0.0011  -0.0056 0.0478  102 LYS   A CE  
2212 N NZ  A LYS   A 102 ? 0.2998 0.3647 0.3163 -0.0391 0.0035  0.0644  102 LYS   A NZ  
2213 N NZ  B LYS   A 102 ? 0.3777 0.3809 0.4364 -0.0000 -0.0061 0.0473  102 LYS   A NZ  
2240 N N   A GLY   A 103 ? 0.2842 0.4137 0.2118 -0.0043 0.0287  0.0655  103 GLY   A N   
2241 N N   B GLY   A 103 ? 0.3604 0.3498 0.2809 0.0166  -0.0089 0.0439  103 GLY   A N   
2242 C CA  A GLY   A 103 ? 0.2899 0.4264 0.2111 -0.0004 0.0294  0.0509  103 GLY   A CA  
2243 C CA  B GLY   A 103 ? 0.3527 0.3443 0.2717 0.0129  -0.0131 0.0443  103 GLY   A CA  
2244 C C   A GLY   A 103 ? 0.2919 0.4387 0.2246 0.0005  0.0356  0.0337  103 GLY   A C   
2245 C C   B GLY   A 103 ? 0.3443 0.3395 0.2577 0.0086  -0.0205 0.0442  103 GLY   A C   
2246 O O   A GLY   A 103 ? 0.2975 0.4459 0.2390 0.0035  0.0341  0.0212  103 GLY   A O   
2247 O O   B GLY   A 103 ? 0.3481 0.3430 0.2655 0.0129  -0.0177 0.0420  103 GLY   A O   
2254 N N   A GLU   A 104 ? 0.2860 0.4395 0.2045 -0.0071 0.0431  0.0293  104 GLU   A N   
2255 N N   B GLU   A 104 ? 0.3302 0.3268 0.2275 -0.0040 -0.0278 0.0518  104 GLU   A N   
2256 C CA  A GLU   A 104 ? 0.2765 0.4366 0.1995 -0.0209 0.0474  0.0277  104 GLU   A CA  
2257 C CA  B GLU   A 104 ? 0.3155 0.3137 0.1974 -0.0198 -0.0385 0.0516  104 GLU   A CA  
2258 C C   A GLU   A 104 ? 0.2836 0.4507 0.2159 -0.0363 0.0432  0.0055  104 GLU   A C   
2259 C C   B GLU   A 104 ? 0.3146 0.3200 0.2008 -0.0272 -0.0333 0.0350  104 GLU   A C   
2260 O O   A GLU   A 104 ? 0.2815 0.4553 0.2360 -0.0379 0.0324  -0.0019 104 GLU   A O   
2261 O O   B GLU   A 104 ? 0.3172 0.3168 0.2185 -0.0258 -0.0356 0.0330  104 GLU   A O   
2262 C CB  A GLU   A 104 ? 0.2581 0.4199 0.1911 -0.0217 0.0573  0.0486  104 GLU   A CB  
2263 C CB  B GLU   A 104 ? 0.3030 0.2975 0.1802 -0.0279 -0.0498 0.0622  104 GLU   A CB  
2264 C CG  A GLU   A 104 ? 0.2452 0.4036 0.2071 -0.0215 0.0530  0.0640  104 GLU   A CG  
2265 C CG  B GLU   A 104 ? 0.2937 0.2852 0.1826 -0.0334 -0.0544 0.0671  104 GLU   A CG  
2266 C CD  A GLU   A 104 ? 0.2290 0.3859 0.2111 -0.0205 0.0476  0.0820  104 GLU   A CD  
2267 C CD  B GLU   A 104 ? 0.2860 0.2745 0.1804 -0.0370 -0.0588 0.0720  104 GLU   A CD  
2268 O OE1 A GLU   A 104 ? 0.2126 0.3728 0.1852 -0.0251 0.0525  0.0904  104 GLU   A OE1 
2269 O OE1 B GLU   A 104 ? 0.2811 0.2708 0.1605 -0.0396 -0.0621 0.0751  104 GLU   A OE1 
2270 O OE2 A GLU   A 104 ? 0.2376 0.3834 0.2355 -0.0163 0.0373  0.0926  104 GLU   A OE2 
2271 O OE2 B GLU   A 104 ? 0.2879 0.2662 0.2043 -0.0360 -0.0510 0.0791  104 GLU   A OE2 
2284 N N   A ASP   A 105 ? 0.2925 0.4571 0.2189 -0.0461 0.0431  -0.0151 105 ASP   A N   
2285 N N   B ASP   A 105 ? 0.3156 0.3302 0.2080 -0.0402 -0.0248 0.0185  105 ASP   A N   
2286 C CA  A ASP   A 105 ? 0.2994 0.4629 0.2315 -0.0566 0.0366  -0.0365 105 ASP   A CA  
2287 C CA  B ASP   A 105 ? 0.3156 0.3411 0.2249 -0.0458 -0.0090 -0.0031 105 ASP   A CA  
2288 C C   A ASP   A 105 ? 0.2753 0.4531 0.2115 -0.0650 0.0147  -0.0538 105 ASP   A C   
2289 C C   B ASP   A 105 ? 0.2968 0.3421 0.1938 -0.0526 -0.0047 -0.0148 105 ASP   A C   
2290 O O   A ASP   A 105 ? 0.2636 0.4500 0.1749 -0.0685 0.0097  -0.0793 105 ASP   A O   
2291 O O   B ASP   A 105 ? 0.2872 0.3345 0.1385 -0.0540 0.0009  -0.0232 105 ASP   A O   
2292 C CB  A ASP   A 105 ? 0.3260 0.4749 0.2641 -0.0553 0.0458  -0.0441 105 ASP   A CB  
2293 C CB  B ASP   A 105 ? 0.3323 0.3500 0.2686 -0.0429 0.0019  -0.0091 105 ASP   A CB  
2294 C CG  A ASP   A 105 ? 0.3480 0.4854 0.2983 -0.0518 0.0508  -0.0506 105 ASP   A CG  
2295 C CG  B ASP   A 105 ? 0.3443 0.3565 0.3028 -0.0372 0.0102  -0.0124 105 ASP   A CG  
2296 O OD1 A ASP   A 105 ? 0.3554 0.4894 0.2979 -0.0542 0.0468  -0.0629 105 ASP   A OD1 
2297 O OD1 B ASP   A 105 ? 0.3502 0.3536 0.3089 -0.0395 0.0167  -0.0116 105 ASP   A OD1 
2298 O OD2 A ASP   A 105 ? 0.3557 0.4899 0.3259 -0.0493 0.0593  -0.0459 105 ASP   A OD2 
2299 O OD2 B ASP   A 105 ? 0.3519 0.3646 0.3289 -0.0341 0.0112  -0.0167 105 ASP   A OD2 
2308 N N   A ILE   A 106 ? 0.2610 0.4423 0.2341 -0.0711 -0.0177 -0.0521 106 ILE   A N   
2309 N N   B ILE   A 106 ? 0.2887 0.3522 0.2220 -0.0555 -0.0124 -0.0187 106 ILE   A N   
2310 C CA  A ILE   A 106 ? 0.2404 0.4234 0.2505 -0.0795 -0.0385 -0.0638 106 ILE   A CA  
2311 C CA  B ILE   A 106 ? 0.2787 0.3570 0.2486 -0.0589 -0.0171 -0.0310 106 ILE   A CA  
2312 C C   A ILE   A 106 ? 0.2245 0.3940 0.2543 -0.0944 -0.0355 -0.0860 106 ILE   A C   
2313 C C   B ILE   A 106 ? 0.2723 0.3422 0.2600 -0.0636 -0.0163 -0.0463 106 ILE   A C   
2314 O O   A ILE   A 106 ? 0.2035 0.3852 0.2497 -0.1020 -0.0159 -0.0895 106 ILE   A O   
2315 O O   B ILE   A 106 ? 0.2660 0.3373 0.2567 -0.0638 -0.0105 -0.0591 106 ILE   A O   
2316 C CB  A ILE   A 106 ? 0.2435 0.4346 0.2865 -0.0647 -0.0592 -0.0427 106 ILE   A CB  
2317 C CB  B ILE   A 106 ? 0.2794 0.3751 0.2822 -0.0531 -0.0215 -0.0220 106 ILE   A CB  
2318 C CG1 A ILE   A 106 ? 0.2357 0.4378 0.3090 -0.0511 -0.0690 -0.0257 106 ILE   A CG1 
2319 C CG1 B ILE   A 106 ? 0.2778 0.3817 0.3063 -0.0472 -0.0228 -0.0125 106 ILE   A CG1 
2320 C CG2 A ILE   A 106 ? 0.2477 0.4389 0.2963 -0.0625 -0.0632 -0.0417 106 ILE   A CG2 
2321 C CG2 B ILE   A 106 ? 0.2804 0.3816 0.2945 -0.0521 -0.0237 -0.0218 106 ILE   A CG2 
2322 C CD1 A ILE   A 106 ? 0.2356 0.4373 0.3224 -0.0393 -0.0652 -0.0181 106 ILE   A CD1 
2323 C CD1 B ILE   A 106 ? 0.2787 0.3838 0.3194 -0.0417 -0.0206 -0.0075 106 ILE   A CD1 
2346 N N   A GLN   A 107 ? 0.2410 0.3726 0.2809 -0.0937 -0.0183 -0.0967 107 GLN   A N   
2347 N N   B GLN   A 107 ? 0.2780 0.3305 0.2847 -0.0652 -0.0097 -0.0443 107 GLN   A N   
2348 C CA  A GLN   A 107 ? 0.2592 0.3486 0.3364 -0.0800 0.0039  -0.0950 107 GLN   A CA  
2349 C CA  B GLN   A 107 ? 0.2810 0.3162 0.3179 -0.0614 0.0012  -0.0453 107 GLN   A CA  
2350 C C   A GLN   A 107 ? 0.2423 0.2995 0.3204 -0.0670 0.0234  -0.0730 107 GLN   A C   
2351 C C   B GLN   A 107 ? 0.2548 0.2841 0.3041 -0.0601 0.0161  -0.0502 107 GLN   A C   
2352 O O   A GLN   A 107 ? 0.2484 0.2954 0.3739 -0.0573 0.0374  -0.0688 107 GLN   A O   
2353 O O   B GLN   A 107 ? 0.2616 0.2809 0.3391 -0.0570 0.0201  -0.0506 107 GLN   A O   
2354 C CB  A GLN   A 107 ? 0.2878 0.3683 0.4068 -0.0856 0.0021  -0.1008 107 GLN   A CB  
2355 C CB  B GLN   A 107 ? 0.3070 0.3305 0.3645 -0.0622 -0.0064 -0.0282 107 GLN   A CB  
2356 C CG  A GLN   A 107 ? 0.3166 0.3883 0.4779 -0.0877 -0.0034 -0.0986 107 GLN   A CG  
2357 C CG  B GLN   A 107 ? 0.3280 0.3438 0.4098 -0.0646 -0.0121 -0.0104 107 GLN   A CG  
2358 C CD  A GLN   A 107 ? 0.3397 0.4042 0.5386 -0.0885 -0.0045 -0.0900 107 GLN   A CD  
2359 C CD  B GLN   A 107 ? 0.3469 0.3557 0.4482 -0.0638 -0.0157 0.0051  107 GLN   A CD  
2360 O OE1 A GLN   A 107 ? 0.3535 0.4127 0.5644 -0.0857 -0.0045 -0.0868 107 GLN   A OE1 
2361 O OE1 B GLN   A 107 ? 0.3540 0.3604 0.4580 -0.0634 -0.0158 0.0158  107 GLN   A OE1 
2362 N NE2 A GLN   A 107 ? 0.3481 0.4090 0.5580 -0.0920 -0.0032 -0.0892 107 GLN   A NE2 
2363 N NE2 B GLN   A 107 ? 0.3532 0.3596 0.4612 -0.0637 -0.0191 0.0093  107 GLN   A NE2 
2380 N N   . LEU   A 108 ? 0.2217 0.2542 0.2560 -0.0612 0.0247  -0.0610 108 LEU   A N   
2381 C CA  . LEU   A 108 ? 0.1974 0.1994 0.2051 -0.0289 0.0247  -0.0167 108 LEU   A CA  
2382 C C   . LEU   A 108 ? 0.1687 0.1539 0.2101 -0.0118 0.0146  0.0084  108 LEU   A C   
2383 O O   . LEU   A 108 ? 0.1619 0.1544 0.2226 -0.0037 0.0186  0.0078  108 LEU   A O   
2384 C CB  . LEU   A 108 ? 0.2043 0.2096 0.1798 -0.0278 0.0275  -0.0042 108 LEU   A CB  
2385 C CG  . LEU   A 108 ? 0.2177 0.2311 0.2166 -0.0246 0.0336  -0.0076 108 LEU   A CG  
2386 C CD1 . LEU   A 108 ? 0.2319 0.2373 0.2212 -0.0335 0.0405  -0.0059 108 LEU   A CD1 
2387 C CD2 . LEU   A 108 ? 0.2208 0.2550 0.2685 -0.0189 0.0356  -0.0012 108 LEU   A CD2 
2400 N N   . LEU   A 109 ? 0.1539 0.1508 0.2126 -0.0031 0.0077  0.0205  109 LEU   A N   
2401 C CA  . LEU   A 109 ? 0.1512 0.1459 0.1848 -0.0072 -0.0028 0.0278  109 LEU   A CA  
2402 C C   . LEU   A 109 ? 0.1379 0.1366 0.1733 -0.0107 -0.0037 0.0100  109 LEU   A C   
2403 O O   . LEU   A 109 ? 0.1477 0.1303 0.1860 -0.0079 -0.0090 0.0077  109 LEU   A O   
2404 C CB  . LEU   A 109 ? 0.1629 0.1585 0.2009 -0.0009 -0.0152 0.0362  109 LEU   A CB  
2405 C CG  . LEU   A 109 ? 0.1541 0.1626 0.2123 -0.0064 -0.0095 0.0318  109 LEU   A CG  
2406 C CD1 . LEU   A 109 ? 0.1605 0.1531 0.2136 -0.0042 -0.0083 0.0081  109 LEU   A CD1 
2407 C CD2 . LEU   A 109 ? 0.1546 0.1795 0.2428 -0.0033 -0.0154 0.0293  109 LEU   A CD2 
2419 N N   . LYS   A 110 ? 0.1383 0.1340 0.1761 -0.0098 -0.0088 0.0093  110 LYS   A N   
2420 C CA  . LYS   A 110 ? 0.1400 0.1297 0.1763 -0.0099 -0.0122 0.0149  110 LYS   A CA  
2421 C C   . LYS   A 110 ? 0.1420 0.1193 0.1525 -0.0093 -0.0027 0.0054  110 LYS   A C   
2422 O O   . LYS   A 110 ? 0.1345 0.1275 0.1621 -0.0037 0.0035  -0.0013 110 LYS   A O   
2423 C CB  . LYS   A 110 ? 0.1509 0.1387 0.1931 -0.0065 -0.0208 0.0004  110 LYS   A CB  
2424 C CG  . LYS   A 110 ? 0.1504 0.1355 0.2090 -0.0056 -0.0184 -0.0088 110 LYS   A CG  
2425 C CD  . LYS   A 110 ? 0.1518 0.1405 0.2192 -0.0113 -0.0148 -0.0076 110 LYS   A CD  
2426 C CE  . LYS   A 110 ? 0.1584 0.1445 0.2340 -0.0057 0.0021  -0.0033 110 LYS   A CE  
2427 N NZ  . LYS   A 110 ? 0.1592 0.1441 0.2343 -0.0184 0.0075  0.0001  110 LYS   A NZ  
2441 N N   . SER   A 111 ? 0.1426 0.1236 0.1541 -0.0023 -0.0004 0.0126  111 SER   A N   
2442 C CA  . SER   A 111 ? 0.1330 0.1287 0.1730 0.0025  0.0072  0.0038  111 SER   A CA  
2443 C C   . SER   A 111 ? 0.1249 0.1217 0.1673 -0.0064 -0.0007 0.0033  111 SER   A C   
2444 O O   . SER   A 111 ? 0.1421 0.1178 0.1798 -0.0016 -0.0034 0.0087  111 SER   A O   
2445 C CB  . SER   A 111 ? 0.1524 0.1512 0.1871 -0.0040 0.0222  -0.0097 111 SER   A CB  
2446 O OG  . SER   A 111 ? 0.2022 0.1743 0.1845 -0.0016 0.0255  -0.0096 111 SER   A OG  
2452 N N   . ALA   A 112 ? 0.1294 0.1168 0.1702 -0.0028 0.0036  0.0011  112 ALA   A N   
2453 C CA  . ALA   A 112 ? 0.1298 0.1202 0.1608 -0.0065 0.0112  0.0010  112 ALA   A CA  
2454 C C   . ALA   A 112 ? 0.1223 0.1167 0.1737 -0.0003 0.0019  0.0055  112 ALA   A C   
2455 O O   . ALA   A 112 ? 0.1318 0.1178 0.1719 -0.0107 0.0082  0.0075  112 ALA   A O   
2456 C CB  . ALA   A 112 ? 0.1407 0.1199 0.1658 -0.0056 0.0050  0.0073  112 ALA   A CB  
2462 N N   . TYR   A 113 ? 0.1222 0.1212 0.1736 -0.0045 0.0041  0.0088  113 TYR   A N   
2463 C CA  . TYR   A 113 ? 0.1176 0.1210 0.1695 -0.0019 0.0089  0.0115  113 TYR   A CA  
2464 C C   . TYR   A 113 ? 0.1194 0.1201 0.1459 -0.0105 0.0124  0.0064  113 TYR   A C   
2465 O O   . TYR   A 113 ? 0.1239 0.1262 0.1640 -0.0042 0.0155  0.0083  113 TYR   A O   
2466 C CB  . TYR   A 113 ? 0.1174 0.1289 0.1802 -0.0085 -0.0050 0.0181  113 TYR   A CB  
2467 C CG  . TYR   A 113 ? 0.1267 0.1287 0.1741 -0.0105 0.0024  0.0138  113 TYR   A CG  
2468 C CD1 . TYR   A 113 ? 0.1250 0.1343 0.1814 0.0005  0.0007  0.0154  113 TYR   A CD1 
2469 C CD2 . TYR   A 113 ? 0.1353 0.1369 0.1748 -0.0107 -0.0015 0.0180  113 TYR   A CD2 
2470 C CE1 . TYR   A 113 ? 0.1376 0.1457 0.1789 -0.0068 0.0030  0.0154  113 TYR   A CE1 
2471 C CE2 . TYR   A 113 ? 0.1281 0.1485 0.1787 -0.0109 -0.0064 0.0224  113 TYR   A CE2 
2472 C CZ  . TYR   A 113 ? 0.1298 0.1397 0.1781 -0.0037 0.0004  0.0290  113 TYR   A CZ  
2473 O OH  . TYR   A 113 ? 0.1304 0.1460 0.2167 0.0051  -0.0020 0.0280  113 TYR   A OH  
2483 N N   . GLU   A 114 ? 0.1233 0.1191 0.1627 -0.0034 0.0098  0.0089  114 GLU   A N   
2484 C CA  . GLU   A 114 ? 0.1296 0.1136 0.1752 -0.0005 0.0047  0.0100  114 GLU   A CA  
2485 C C   . GLU   A 114 ? 0.1233 0.1216 0.1694 0.0035  0.0101  0.0116  114 GLU   A C   
2486 O O   . GLU   A 114 ? 0.1320 0.1219 0.1701 -0.0055 0.0045  0.0080  114 GLU   A O   
2487 C CB  . GLU   A 114 ? 0.1276 0.1192 0.1764 -0.0054 0.0076  0.0108  114 GLU   A CB  
2488 C CG  . GLU   A 114 ? 0.1302 0.1210 0.1843 -0.0025 0.0068  0.0011  114 GLU   A CG  
2489 C CD  . GLU   A 114 ? 0.1459 0.1251 0.1871 -0.0020 -0.0017 -0.0020 114 GLU   A CD  
2490 O OE1 . GLU   A 114 ? 0.1418 0.1249 0.1820 -0.0049 0.0101  -0.0039 114 GLU   A OE1 
2491 O OE2 . GLU   A 114 ? 0.1606 0.1296 0.2055 -0.0079 0.0086  -0.0144 114 GLU   A OE2 
2498 N N   . ASN   A 115 ? 0.1190 0.1223 0.1569 -0.0057 0.0039  0.0023  115 ASN   A N   
2499 C CA  . ASN   A 115 ? 0.1257 0.1250 0.1701 -0.0076 0.0103  0.0084  115 ASN   A CA  
2500 C C   . ASN   A 115 ? 0.1251 0.1152 0.1595 -0.0081 0.0030  0.0043  115 ASN   A C   
2501 O O   . ASN   A 115 ? 0.1273 0.1358 0.1610 -0.0105 0.0046  0.0104  115 ASN   A O   
2502 C CB  . ASN   A 115 ? 0.1342 0.1298 0.1521 -0.0165 0.0002  0.0016  115 ASN   A CB  
2503 C CG  . ASN   A 115 ? 0.1298 0.1543 0.1629 -0.0182 0.0083  0.0075  115 ASN   A CG  
2504 O OD1 . ASN   A 115 ? 0.1353 0.2509 0.1820 -0.0185 0.0176  0.0275  115 ASN   A OD1 
2505 N ND2 . ASN   A 115 ? 0.1363 0.1332 0.1637 -0.0152 0.0143  0.0149  115 ASN   A ND2 
2512 N N   . PHE   A 116 ? 0.1198 0.1251 0.1723 -0.0034 0.0091  0.0118  116 PHE   A N   
2513 C CA  . PHE   A 116 ? 0.1231 0.1358 0.1589 -0.0009 0.0061  0.0116  116 PHE   A CA  
2514 C C   . PHE   A 116 ? 0.1227 0.1369 0.1593 -0.0087 0.0076  0.0194  116 PHE   A C   
2515 O O   . PHE   A 116 ? 0.1308 0.1460 0.1644 -0.0013 0.0080  0.0194  116 PHE   A O   
2516 C CB  . PHE   A 116 ? 0.1271 0.1246 0.1780 -0.0032 0.0134  0.0129  116 PHE   A CB  
2517 C CG  . PHE   A 116 ? 0.1267 0.1211 0.1721 -0.0049 0.0172  0.0096  116 PHE   A CG  
2518 C CD1 . PHE   A 116 ? 0.1288 0.1285 0.1727 -0.0049 0.0076  0.0149  116 PHE   A CD1 
2519 C CD2 . PHE   A 116 ? 0.1313 0.1272 0.1925 -0.0120 0.0149  0.0119  116 PHE   A CD2 
2520 C CE1 . PHE   A 116 ? 0.1286 0.1250 0.1861 -0.0159 0.0000  0.0113  116 PHE   A CE1 
2521 C CE2 . PHE   A 116 ? 0.1333 0.1229 0.1923 0.0004  0.0113  0.0136  116 PHE   A CE2 
2522 C CZ  . PHE   A 116 ? 0.1339 0.1165 0.1898 -0.0010 0.0004  0.0095  116 PHE   A CZ  
2532 N N   . ASN   A 117 ? 0.1233 0.1296 0.1673 -0.0085 0.0103  0.0183  117 ASN   A N   
2533 C CA  . ASN   A 117 ? 0.1267 0.1270 0.1786 -0.0042 0.0137  0.0265  117 ASN   A CA  
2534 C C   . ASN   A 117 ? 0.1271 0.1379 0.1900 -0.0017 0.0079  0.0246  117 ASN   A C   
2535 O O   . ASN   A 117 ? 0.1367 0.1439 0.2143 -0.0062 -0.0098 0.0402  117 ASN   A O   
2536 C CB  . ASN   A 117 ? 0.1301 0.1307 0.1814 -0.0079 0.0072  0.0305  117 ASN   A CB  
2537 C CG  . ASN   A 117 ? 0.1291 0.1278 0.1840 -0.0081 0.0120  0.0200  117 ASN   A CG  
2538 O OD1 . ASN   A 117 ? 0.1310 0.1504 0.1856 -0.0121 0.0058  0.0199  117 ASN   A OD1 
2539 N ND2 . ASN   A 117 ? 0.1237 0.1312 0.1802 -0.0034 0.0116  0.0171  117 ASN   A ND2 
2546 N N   . GLN   A 118 ? 0.1243 0.1337 0.1896 -0.0082 0.0016  0.0251  118 GLN   A N   
2547 C CA  . GLN   A 118 ? 0.1350 0.1521 0.1789 -0.0110 -0.0030 0.0210  118 GLN   A CA  
2548 C C   . GLN   A 118 ? 0.1354 0.1558 0.1817 -0.0102 -0.0018 0.0198  118 GLN   A C   
2549 O O   . GLN   A 118 ? 0.1349 0.1898 0.2141 -0.0029 -0.0127 0.0079  118 GLN   A O   
2550 C CB  . GLN   A 118 ? 0.1319 0.1518 0.1911 -0.0061 -0.0009 0.0231  118 GLN   A CB  
2551 C CG  . GLN   A 118 ? 0.1287 0.1547 0.1897 -0.0035 0.0024  0.0221  118 GLN   A CG  
2552 C CD  . GLN   A 118 ? 0.1299 0.1567 0.1972 0.0008  -0.0008 0.0146  118 GLN   A CD  
2553 O OE1 . GLN   A 118 ? 0.1368 0.1645 0.2200 0.0071  -0.0131 0.0076  118 GLN   A OE1 
2554 N NE2 . GLN   A 118 ? 0.1402 0.1550 0.1961 0.0047  -0.0037 0.0186  118 GLN   A NE2 
2563 N N   . HIS   A 119 ? 0.1386 0.1563 0.1667 -0.0079 0.0024  0.0253  119 HIS   A N   
2564 C CA  . HIS   A 119 ? 0.1450 0.1657 0.1660 -0.0075 -0.0030 0.0298  119 HIS   A CA  
2565 C C   . HIS   A 119 ? 0.1556 0.1690 0.1648 -0.0116 0.0046  0.0297  119 HIS   A C   
2566 O O   . HIS   A 119 ? 0.1602 0.1784 0.1806 -0.0292 -0.0054 0.0318  119 HIS   A O   
2567 C CB  . HIS   A 119 ? 0.1515 0.1643 0.1861 -0.0047 0.0146  0.0353  119 HIS   A CB  
2568 C CG  . HIS   A 119 ? 0.1586 0.1666 0.2371 0.0024  0.0121  0.0409  119 HIS   A CG  
2569 N ND1 . HIS   A 119 ? 0.1708 0.1793 0.2908 -0.0089 0.0131  0.0296  119 HIS   A ND1 
2570 C CD2 . HIS   A 119 ? 0.1699 0.1702 0.2540 0.0105  0.0303  0.0556  119 HIS   A CD2 
2571 C CE1 . HIS   A 119 ? 0.1684 0.1754 0.3060 -0.0166 0.0291  0.0451  119 HIS   A CE1 
2572 N NE2 . HIS   A 119 ? 0.1784 0.1737 0.2923 0.0023  0.0509  0.0600  119 HIS   A NE2 
2580 N N   . GLU   A 120 ? 0.1658 0.1914 0.1646 -0.0072 -0.0024 0.0454  120 GLU   A N   
2581 C CA  . GLU   A 120 ? 0.1902 0.2185 0.1904 0.0057  -0.0051 0.0729  120 GLU   A CA  
2582 C C   . GLU   A 120 ? 0.1658 0.2046 0.1734 -0.0061 -0.0047 0.0642  120 GLU   A C   
2583 O O   . GLU   A 120 ? 0.1703 0.2022 0.1870 -0.0146 -0.0029 0.0659  120 GLU   A O   
2584 C CB  . GLU   A 120 ? 0.2525 0.2865 0.2564 0.0232  0.0072  0.1274  120 GLU   A CB  
2585 C CG  . GLU   A 120 ? 0.3430 0.3529 0.3718 0.0357  0.0138  0.1359  120 GLU   A CG  
2586 C CD  . GLU   A 120 ? 0.4081 0.4134 0.4901 0.0440  0.0261  0.1300  120 GLU   A CD  
2587 O OE1 . GLU   A 120 ? 0.4472 0.4354 0.5203 0.0443  0.0258  0.1262  120 GLU   A OE1 
2588 O OE2 . GLU   A 120 ? 0.4694 0.4694 0.5497 0.0465  0.0323  0.1286  120 GLU   A OE2 
2595 N N   . VAL   A 121 ? 0.1638 0.2086 0.1540 -0.0167 0.0046  0.0506  121 VAL   A N   
2596 C CA  . VAL   A 121 ? 0.1730 0.2136 0.1587 -0.0134 0.0178  0.0509  121 VAL   A CA  
2597 C C   . VAL   A 121 ? 0.1598 0.1959 0.1494 -0.0254 0.0073  0.0382  121 VAL   A C   
2598 O O   . VAL   A 121 ? 0.1565 0.2070 0.1741 -0.0354 -0.0024 0.0302  121 VAL   A O   
2599 C CB  . VAL   A 121 ? 0.2152 0.2475 0.1921 -0.0035 0.0352  0.0576  121 VAL   A CB  
2600 C CG1 . VAL   A 121 ? 0.2224 0.2612 0.1970 -0.0009 0.0410  0.0587  121 VAL   A CG1 
2601 C CG2 . VAL   A 121 ? 0.2296 0.2650 0.2340 -0.0135 0.0316  0.0447  121 VAL   A CG2 
2611 N N   . LEU   A 122 ? 0.1519 0.1736 0.1642 -0.0287 0.0094  0.0360  122 LEU   A N   
2612 C CA  . LEU   A 122 ? 0.1585 0.1647 0.1671 -0.0278 0.0294  0.0295  122 LEU   A CA  
2613 C C   . LEU   A 122 ? 0.1554 0.1624 0.1619 -0.0245 0.0199  0.0245  122 LEU   A C   
2614 O O   . LEU   A 122 ? 0.1553 0.1676 0.2035 -0.0315 0.0133  0.0289  122 LEU   A O   
2615 C CB  . LEU   A 122 ? 0.1835 0.1659 0.2059 -0.0190 0.0246  0.0374  122 LEU   A CB  
2616 C CG  . LEU   A 122 ? 0.1887 0.1681 0.1918 -0.0166 0.0288  0.0151  122 LEU   A CG  
2617 C CD1 . LEU   A 122 ? 0.2086 0.1673 0.2105 -0.0326 0.0319  0.0129  122 LEU   A CD1 
2618 C CD2 . LEU   A 122 ? 0.1850 0.1537 0.1758 -0.0069 0.0335  0.0247  122 LEU   A CD2 
2630 N N   . LEU   A 123 ? 0.1520 0.1593 0.1599 -0.0269 0.0093  0.0290  123 LEU   A N   
2631 C CA  . LEU   A 123 ? 0.1488 0.1580 0.1490 -0.0212 0.0136  0.0276  123 LEU   A CA  
2632 C C   . LEU   A 123 ? 0.1432 0.1498 0.1443 -0.0155 0.0114  0.0238  123 LEU   A C   
2633 O O   . LEU   A 123 ? 0.1379 0.1651 0.1628 -0.0300 0.0055  0.0271  123 LEU   A O   
2634 C CB  . LEU   A 123 ? 0.1565 0.1676 0.1494 -0.0259 0.0346  0.0215  123 LEU   A CB  
2635 C CG  . LEU   A 123 ? 0.1627 0.1785 0.1626 -0.0191 0.0285  0.0172  123 LEU   A CG  
2636 C CD1 . LEU   A 123 ? 0.1699 0.1861 0.1928 -0.0147 0.0208  0.0122  123 LEU   A CD1 
2637 C CD2 . LEU   A 123 ? 0.1816 0.1882 0.1771 -0.0201 0.0249  0.0086  123 LEU   A CD2 
2649 N N   A ALA   A 124 ? 0.1394 0.1399 0.1410 -0.0177 0.0118  0.0161  124 ALA   A N   
2650 N N   B ALA   A 124 ? 0.1461 0.1451 0.1545 -0.0205 0.0056  0.0183  124 ALA   A N   
2651 C CA  A ALA   A 124 ? 0.1280 0.1326 0.1497 -0.0098 0.0085  0.0191  124 ALA   A CA  
2652 C CA  B ALA   A 124 ? 0.1467 0.1426 0.1729 -0.0249 -0.0002 0.0225  124 ALA   A CA  
2653 C C   A ALA   A 124 ? 0.1249 0.1280 0.1470 -0.0125 0.0219  0.0165  124 ALA   A C   
2654 C C   B ALA   A 124 ? 0.1374 0.1267 0.1728 -0.0172 0.0063  0.0171  124 ALA   A C   
2655 O O   A ALA   A 124 ? 0.1244 0.1402 0.1610 -0.0086 0.0334  0.0276  124 ALA   A O   
2656 O O   B ALA   A 124 ? 0.1316 0.1249 0.1949 -0.0072 0.0100  0.0099  124 ALA   A O   
2657 C CB  A ALA   A 124 ? 0.1198 0.1252 0.1715 -0.0037 0.0028  0.0211  124 ALA   A CB  
2658 C CB  B ALA   A 124 ? 0.1560 0.1443 0.1843 -0.0327 -0.0040 0.0305  124 ALA   A CB  
2669 N N   A PRO   A 125 ? 0.1240 0.1329 0.1540 -0.0021 0.0199  0.0226  125 PRO   A N   
2670 N N   B PRO   A 125 ? 0.1268 0.1236 0.1541 -0.0053 0.0158  0.0228  125 PRO   A N   
2671 C CA  A PRO   A 125 ? 0.1367 0.1426 0.1664 -0.0027 0.0117  0.0161  125 PRO   A CA  
2672 C CA  B PRO   A 125 ? 0.1305 0.1267 0.1666 0.0020  0.0204  0.0294  125 PRO   A CA  
2673 C C   A PRO   A 125 ? 0.1295 0.1545 0.1548 -0.0111 0.0135  0.0083  125 PRO   A C   
2674 C C   B PRO   A 125 ? 0.1227 0.1345 0.1757 -0.0024 0.0242  0.0272  125 PRO   A C   
2675 O O   A PRO   A 125 ? 0.1409 0.1493 0.1436 -0.0076 0.0150  0.0124  125 PRO   A O   
2676 O O   B PRO   A 125 ? 0.1172 0.1253 0.1713 0.0035  0.0276  0.0278  125 PRO   A O   
2677 C CB  A PRO   A 125 ? 0.1532 0.1450 0.1751 -0.0026 0.0154  0.0169  125 PRO   A CB  
2678 C CB  B PRO   A 125 ? 0.1370 0.1236 0.1679 0.0029  0.0191  0.0305  125 PRO   A CB  
2679 C CG  A PRO   A 125 ? 0.1569 0.1454 0.1864 -0.0052 0.0104  0.0205  125 PRO   A CG  
2680 C CG  B PRO   A 125 ? 0.1338 0.1191 0.1641 0.0004  0.0199  0.0249  125 PRO   A CG  
2681 C CD  A PRO   A 125 ? 0.1398 0.1427 0.1715 -0.0050 0.0149  0.0197  125 PRO   A CD  
2682 C CD  B PRO   A 125 ? 0.1275 0.1098 0.1553 -0.0015 0.0188  0.0207  125 PRO   A CD  
2697 N N   A LEU   A 126 ? 0.1264 0.1610 0.1647 -0.0089 0.0010  0.0057  126 LEU   A N   
2698 N N   B LEU   A 126 ? 0.1252 0.1432 0.1903 -0.0020 0.0192  0.0300  126 LEU   A N   
2699 C CA  A LEU   A 126 ? 0.1273 0.1552 0.1746 -0.0173 -0.0008 0.0191  126 LEU   A CA  
2700 C CA  B LEU   A 126 ? 0.1370 0.1559 0.1962 -0.0069 0.0096  0.0385  126 LEU   A CA  
2701 C C   A LEU   A 126 ? 0.1263 0.1416 0.1699 -0.0023 -0.0026 0.0122  126 LEU   A C   
2702 C C   B LEU   A 126 ? 0.1440 0.1519 0.2100 0.0029  0.0063  0.0441  126 LEU   A C   
2703 O O   A LEU   A 126 ? 0.1257 0.1353 0.1760 -0.0032 -0.0030 0.0054  126 LEU   A O   
2704 O O   B LEU   A 126 ? 0.1527 0.1470 0.2448 0.0031  0.0187  0.0447  126 LEU   A O   
2705 C CB  A LEU   A 126 ? 0.1417 0.1611 0.1953 -0.0179 -0.0123 0.0341  126 LEU   A CB  
2706 C CB  B LEU   A 126 ? 0.1431 0.1682 0.1795 -0.0109 0.0084  0.0380  126 LEU   A CB  
2707 C CG  A LEU   A 126 ? 0.1386 0.1664 0.2134 -0.0121 -0.0087 0.0520  126 LEU   A CG  
2708 C CG  B LEU   A 126 ? 0.1371 0.1708 0.1931 -0.0056 0.0056  0.0432  126 LEU   A CG  
2709 C CD1 A LEU   A 126 ? 0.1466 0.1849 0.2162 -0.0151 -0.0110 0.0590  126 LEU   A CD1 
2710 C CD1 B LEU   A 126 ? 0.1383 0.1746 0.2086 -0.0049 -0.0085 0.0508  126 LEU   A CD1 
2711 C CD2 A LEU   A 126 ? 0.1455 0.1609 0.2083 -0.0154 0.0047  0.0443  126 LEU   A CD2 
2712 C CD2 B LEU   A 126 ? 0.1325 0.1730 0.2078 -0.0071 0.0116  0.0330  126 LEU   A CD2 
2735 N N   A LEU   A 127 ? 0.1200 0.1390 0.1613 -0.0015 0.0002  0.0141  127 LEU   A N   
2736 N N   B LEU   A 127 ? 0.1425 0.1581 0.1905 0.0041  0.0028  0.0519  127 LEU   A N   
2737 C CA  A LEU   A 127 ? 0.1203 0.1374 0.1498 -0.0052 -0.0030 0.0144  127 LEU   A CA  
2738 C CA  B LEU   A 127 ? 0.1456 0.1657 0.1940 -0.0014 0.0019  0.0506  127 LEU   A CA  
2739 C C   A LEU   A 127 ? 0.1165 0.1212 0.1385 0.0007  -0.0004 0.0086  127 LEU   A C   
2740 C C   B LEU   A 127 ? 0.1573 0.1754 0.2023 -0.0021 -0.0055 0.0396  127 LEU   A C   
2741 O O   A LEU   A 127 ? 0.1219 0.1143 0.1509 0.0030  0.0084  0.0146  127 LEU   A O   
2742 O O   B LEU   A 127 ? 0.1587 0.1681 0.2002 -0.0056 -0.0012 0.0236  127 LEU   A O   
2743 C CB  A LEU   A 127 ? 0.1315 0.1492 0.1556 0.0024  0.0020  0.0121  127 LEU   A CB  
2744 C CB  B LEU   A 127 ? 0.1459 0.1693 0.2040 -0.0021 0.0083  0.0448  127 LEU   A CB  
2745 C CG  A LEU   A 127 ? 0.1382 0.1616 0.1646 0.0082  -0.0060 0.0177  127 LEU   A CG  
2746 C CG  B LEU   A 127 ? 0.1456 0.1748 0.2037 -0.0028 0.0156  0.0487  127 LEU   A CG  
2747 C CD1 A LEU   A 127 ? 0.1452 0.1496 0.1744 0.0061  -0.0125 0.0186  127 LEU   A CD1 
2748 C CD1 B LEU   A 127 ? 0.1423 0.1856 0.2077 -0.0024 0.0129  0.0431  127 LEU   A CD1 
2749 C CD2 A LEU   A 127 ? 0.1435 0.1705 0.1664 0.0185  -0.0312 0.0180  127 LEU   A CD2 
2750 C CD2 B LEU   A 127 ? 0.1586 0.1794 0.2113 0.0038  0.0061  0.0420  127 LEU   A CD2 
2773 N N   A SER   A 128 ? 0.1226 0.1162 0.1241 -0.0065 -0.0030 0.0035  128 SER   A N   
2774 N N   B SER   A 128 ? 0.1698 0.2000 0.2237 -0.0045 -0.0182 0.0361  128 SER   A N   
2775 C CA  A SER   A 128 ? 0.1310 0.1216 0.1241 -0.0062 -0.0169 0.0152  128 SER   A CA  
2776 C CA  B SER   A 128 ? 0.1847 0.2282 0.2407 -0.0016 -0.0227 0.0352  128 SER   A CA  
2777 C C   A SER   A 128 ? 0.1353 0.1128 0.1477 -0.0052 -0.0252 0.0281  128 SER   A C   
2778 C C   B SER   A 128 ? 0.2035 0.2536 0.2712 0.0010  -0.0266 0.0294  128 SER   A C   
2779 O O   A SER   A 128 ? 0.1482 0.1241 0.1868 -0.0072 -0.0299 0.0110  128 SER   A O   
2780 O O   B SER   A 128 ? 0.2121 0.2588 0.2846 -0.0001 -0.0182 0.0279  128 SER   A O   
2781 C CB  A SER   A 128 ? 0.1333 0.1307 0.1140 -0.0051 -0.0117 0.0192  128 SER   A CB  
2782 C CB  B SER   A 128 ? 0.1781 0.2311 0.2280 -0.0020 -0.0260 0.0368  128 SER   A CB  
2783 O OG  A SER   A 128 ? 0.1350 0.1435 0.1339 -0.0108 -0.0084 0.0244  128 SER   A OG  
2784 O OG  B SER   A 128 ? 0.1678 0.2328 0.2217 -0.0060 -0.0271 0.0355  128 SER   A OG  
2795 N N   A ALA   A 129 ? 0.1281 0.1256 0.1981 -0.0007 -0.0291 0.0313  129 ALA   A N   
2796 N N   B ALA   A 129 ? 0.2078 0.2701 0.2852 0.0096  -0.0369 0.0327  129 ALA   A N   
2797 C CA  A ALA   A 129 ? 0.1244 0.1324 0.2372 0.0069  -0.0106 0.0287  129 ALA   A CA  
2798 C CA  B ALA   A 129 ? 0.2164 0.2846 0.2943 0.0047  -0.0413 0.0330  129 ALA   A CA  
2799 C C   A ALA   A 129 ? 0.1267 0.1329 0.2174 0.0114  -0.0161 0.0084  129 ALA   A C   
2800 C C   B ALA   A 129 ? 0.2275 0.2950 0.2968 0.0001  -0.0465 0.0314  129 ALA   A C   
2801 O O   A ALA   A 129 ? 0.1337 0.1341 0.2123 0.0052  -0.0094 0.0137  129 ALA   A O   
2802 O O   B ALA   A 129 ? 0.2369 0.3007 0.2985 0.0012  -0.0543 0.0331  129 ALA   A O   
2803 C CB  A ALA   A 129 ? 0.1390 0.1524 0.2786 0.0084  0.0058  0.0415  129 ALA   A CB  
2804 C CB  B ALA   A 129 ? 0.2162 0.2875 0.3004 0.0049  -0.0353 0.0340  129 ALA   A CB  
2815 N N   A GLY   A 130 ? 0.1366 0.1338 0.2084 0.0085  -0.0105 0.0011  130 GLY   A N   
2816 N N   B GLY   A 130 ? 0.2331 0.3014 0.2975 -0.0018 -0.0376 0.0335  130 GLY   A N   
2817 C CA  A GLY   A 130 ? 0.1591 0.1389 0.2034 0.0083  -0.0093 -0.0019 130 GLY   A CA  
2818 C CA  B GLY   A 130 ? 0.2375 0.3083 0.2938 -0.0077 -0.0322 0.0348  130 GLY   A CA  
2819 C C   A GLY   A 130 ? 0.1630 0.1322 0.1819 0.0148  -0.0174 -0.0004 130 GLY   A C   
2820 C C   B GLY   A 130 ? 0.2409 0.3143 0.2921 -0.0136 -0.0312 0.0419  130 GLY   A C   
2821 O O   A GLY   A 130 ? 0.1790 0.1242 0.1858 0.0172  -0.0258 0.0080  130 GLY   A O   
2822 O O   B GLY   A 130 ? 0.2170 0.3022 0.2866 -0.0390 -0.0047 0.0497  130 GLY   A O   
2829 N N   A ILE   A 131 ? 0.1710 0.1250 0.1642 0.0081  -0.0229 0.0131  131 ILE   A N   
2830 N N   B ILE   A 131 ? 0.2802 0.3340 0.3054 -0.0050 -0.0316 0.0468  131 ILE   A N   
2831 C CA  A ILE   A 131 ? 0.1800 0.1306 0.1451 -0.0046 -0.0267 0.0086  131 ILE   A CA  
2832 C CA  B ILE   A 131 ? 0.3192 0.3569 0.3266 0.0024  -0.0355 0.0415  131 ILE   A CA  
2833 C C   A ILE   A 131 ? 0.1664 0.1327 0.1389 -0.0152 -0.0267 0.0162  131 ILE   A C   
2834 C C   B ILE   A 131 ? 0.3428 0.3752 0.3427 0.0036  -0.0390 0.0302  131 ILE   A C   
2835 O O   A ILE   A 131 ? 0.1741 0.1379 0.1539 -0.0082 -0.0236 0.0256  131 ILE   A O   
2836 O O   B ILE   A 131 ? 0.3474 0.3754 0.3462 0.0004  -0.0373 0.0326  131 ILE   A O   
2837 C CB  A ILE   A 131 ? 0.2044 0.1394 0.1545 -0.0094 -0.0278 -0.0032 131 ILE   A CB  
2838 C CB  B ILE   A 131 ? 0.3335 0.3645 0.3388 0.0057  -0.0301 0.0412  131 ILE   A CB  
2839 C CG1 A ILE   A 131 ? 0.2123 0.1657 0.1610 -0.0186 -0.0316 -0.0120 131 ILE   A CG1 
2840 C CG1 B ILE   A 131 ? 0.3410 0.3667 0.3436 0.0081  -0.0305 0.0456  131 ILE   A CG1 
2841 C CG2 A ILE   A 131 ? 0.2174 0.1301 0.1811 0.0004  -0.0221 -0.0051 131 ILE   A CG2 
2842 C CG2 B ILE   A 131 ? 0.3372 0.3667 0.3432 0.0079  -0.0280 0.0373  131 ILE   A CG2 
2843 C CD1 A ILE   A 131 ? 0.2215 0.1793 0.1867 -0.0227 -0.0398 -0.0186 131 ILE   A CD1 
2844 C CD1 B ILE   A 131 ? 0.3436 0.3668 0.3431 0.0109  -0.0300 0.0476  131 ILE   A CD1 
2867 N N   A PHE   A 132 ? 0.1629 0.1346 0.1310 -0.0020 -0.0272 0.0179  132 PHE   A N   
2868 N N   B PHE   A 132 ? 0.3603 0.3925 0.3567 0.0069  -0.0442 0.0154  132 PHE   A N   
2869 C CA  A PHE   A 132 ? 0.1665 0.1420 0.1304 -0.0034 -0.0165 0.0136  132 PHE   A CA  
2870 C CA  B PHE   A 132 ? 0.3788 0.4098 0.3755 0.0112  -0.0494 -0.0031 132 PHE   A CA  
2871 C C   A PHE   A 132 ? 0.1765 0.1618 0.1342 0.0024  -0.0197 0.0120  132 PHE   A C   
2872 C C   B PHE   A 132 ? 0.3851 0.4075 0.3840 0.0046  -0.0537 -0.0005 132 PHE   A C   
2873 O O   A PHE   A 132 ? 0.1792 0.1749 0.1452 0.0082  -0.0282 0.0053  132 PHE   A O   
2874 O O   B PHE   A 132 ? 0.3842 0.4065 0.3794 0.0026  -0.0594 -0.0005 132 PHE   A O   
2875 C CB  A PHE   A 132 ? 0.1627 0.1276 0.1222 -0.0077 -0.0167 0.0198  132 PHE   A CB  
2876 C CB  B PHE   A 132 ? 0.3892 0.4289 0.3875 0.0210  -0.0470 -0.0243 132 PHE   A CB  
2877 C CG  A PHE   A 132 ? 0.1611 0.1230 0.1148 -0.0021 -0.0210 0.0167  132 PHE   A CG  
2878 C CG  B PHE   A 132 ? 0.3982 0.4458 0.4020 0.0304  -0.0451 -0.0425 132 PHE   A CG  
2879 C CD1 A PHE   A 132 ? 0.1637 0.1396 0.1303 0.0119  -0.0204 -0.0051 132 PHE   A CD1 
2880 C CD1 B PHE   A 132 ? 0.4018 0.4531 0.4082 0.0346  -0.0439 -0.0503 132 PHE   A CD1 
2881 C CD2 A PHE   A 132 ? 0.1653 0.1397 0.1245 -0.0018 -0.0141 0.0061  132 PHE   A CD2 
2882 C CD2 B PHE   A 132 ? 0.4024 0.4529 0.4105 0.0339  -0.0425 -0.0503 132 PHE   A CD2 
2883 C CE1 A PHE   A 132 ? 0.1675 0.1455 0.1306 0.0157  -0.0277 -0.0135 132 PHE   A CE1 
2884 C CE1 B PHE   A 132 ? 0.4037 0.4579 0.4133 0.0372  -0.0433 -0.0536 132 PHE   A CE1 
2885 C CE2 A PHE   A 132 ? 0.1638 0.1445 0.1407 0.0045  -0.0183 0.0032  132 PHE   A CE2 
2886 C CE2 B PHE   A 132 ? 0.4043 0.4574 0.4143 0.0374  -0.0415 -0.0535 132 PHE   A CE2 
2887 C CZ  A PHE   A 132 ? 0.1627 0.1436 0.1324 0.0033  -0.0257 0.0018  132 PHE   A CZ  
2888 C CZ  B PHE   A 132 ? 0.4046 0.4592 0.4159 0.0377  -0.0424 -0.0546 132 PHE   A CZ  
2907 N N   A GLY   A 133 ? 0.1804 0.1592 0.1285 -0.0009 -0.0386 0.0184  133 GLY   A N   
2908 N N   B GLY   A 133 ? 0.3913 0.4068 0.3982 0.0008  -0.0519 0.0028  133 GLY   A N   
2909 C CA  A GLY   A 133 ? 0.1870 0.1675 0.1438 -0.0015 -0.0401 0.0029  133 GLY   A CA  
2910 C CA  B GLY   A 133 ? 0.3956 0.4025 0.4137 -0.0039 -0.0454 0.0060  133 GLY   A CA  
2911 C C   A GLY   A 133 ? 0.1871 0.1775 0.1555 -0.0036 -0.0471 -0.0154 133 GLY   A C   
2912 C C   B GLY   A 133 ? 0.3973 0.3981 0.4289 -0.0088 -0.0392 0.0099  133 GLY   A C   
2913 O O   A GLY   A 133 ? 0.2018 0.1939 0.1724 -0.0015 -0.0483 -0.0277 133 GLY   A O   
2914 O O   B GLY   A 133 ? 0.4002 0.4014 0.4379 -0.0102 -0.0395 0.0123  133 GLY   A O   
2921 N N   A ALA   A 134 ? 0.1782 0.1660 0.1449 -0.0089 -0.0373 -0.0187 134 ALA   A N   
2922 N N   B ALA   A 134 ? 0.3942 0.3878 0.4301 -0.0108 -0.0312 0.0120  134 ALA   A N   
2923 C CA  A ALA   A 134 ? 0.1683 0.1614 0.1624 -0.0027 -0.0345 -0.0217 134 ALA   A CA  
2924 C CA  B ALA   A 134 ? 0.3880 0.3756 0.4273 -0.0132 -0.0209 0.0098  134 ALA   A CA  
2925 C C   A ALA   A 134 ? 0.1651 0.1652 0.1651 -0.0040 -0.0326 -0.0043 134 ALA   A C   
2926 C C   B ALA   A 134 ? 0.3749 0.3614 0.4221 -0.0136 -0.0111 0.0056  134 ALA   A C   
2927 O O   A ALA   A 134 ? 0.1804 0.1743 0.1778 -0.0029 -0.0152 0.0060  134 ALA   A O   
2928 O O   B ALA   A 134 ? 0.3821 0.3651 0.4384 -0.0123 -0.0100 0.0022  134 ALA   A O   
2929 C CB  A ALA   A 134 ? 0.1700 0.1554 0.1916 -0.0009 -0.0228 -0.0215 134 ALA   A CB  
2930 C CB  B ALA   A 134 ? 0.3929 0.3775 0.4277 -0.0142 -0.0213 0.0105  134 ALA   A CB  
2941 N N   A ASP   A 135 ? 0.1676 0.1704 0.1717 -0.0130 -0.0342 0.0071  135 ASP   A N   
2942 N N   B ASP   A 135 ? 0.3513 0.3419 0.3933 -0.0174 -0.0018 0.0068  135 ASP   A N   
2943 C CA  A ASP   A 135 ? 0.1664 0.1920 0.2085 -0.0227 -0.0426 0.0304  135 ASP   A CA  
2944 C CA  B ASP   A 135 ? 0.3246 0.3231 0.3605 -0.0209 0.0104  0.0090  135 ASP   A CA  
2945 C C   A ASP   A 135 ? 0.1563 0.1830 0.2058 -0.0118 -0.0364 0.0452  135 ASP   A C   
2946 C C   B ASP   A 135 ? 0.2823 0.2896 0.2897 -0.0192 0.0035  0.0173  135 ASP   A C   
2947 O O   A ASP   A 135 ? 0.1473 0.1644 0.2084 -0.0229 -0.0371 0.0472  135 ASP   A O   
2948 O O   B ASP   A 135 ? 0.2747 0.2835 0.2715 -0.0205 0.0020  0.0176  135 ASP   A O   
2949 C CB  A ASP   A 135 ? 0.1826 0.2214 0.2491 -0.0421 -0.0513 0.0261  135 ASP   A CB  
2950 C CB  B ASP   A 135 ? 0.3393 0.3378 0.4024 -0.0251 0.0278  0.0018  135 ASP   A CB  
2951 C CG  A ASP   A 135 ? 0.1991 0.2527 0.2985 -0.0468 -0.0478 0.0288  135 ASP   A CG  
2952 C CG  B ASP   A 135 ? 0.3501 0.3509 0.4409 -0.0279 0.0449  -0.0039 135 ASP   A CG  
2953 O OD1 A ASP   A 135 ? 0.1834 0.2657 0.2977 -0.0476 -0.0707 0.0439  135 ASP   A OD1 
2954 O OD1 B ASP   A 135 ? 0.3555 0.3585 0.4571 -0.0260 0.0494  -0.0044 135 ASP   A OD1 
2955 O OD2 A ASP   A 135 ? 0.2419 0.2715 0.3561 -0.0337 -0.0103 0.0376  135 ASP   A OD2 
2956 O OD2 B ASP   A 135 ? 0.3533 0.3552 0.4555 -0.0306 0.0532  -0.0029 135 ASP   A OD2 
2965 N N   A PRO   A 136 ? 0.1485 0.1821 0.2065 0.0095  -0.0252 0.0588  136 PRO   A N   
2966 N N   B PRO   A 136 ? 0.2463 0.2629 0.2485 -0.0102 0.0041  0.0246  136 PRO   A N   
2967 C CA  A PRO   A 136 ? 0.1406 0.1795 0.2164 0.0076  -0.0100 0.0421  136 PRO   A CA  
2968 C CA  B PRO   A 136 ? 0.2200 0.2455 0.2293 -0.0094 0.0068  0.0229  136 PRO   A CA  
2969 C C   A PRO   A 136 ? 0.1221 0.1750 0.2233 0.0018  -0.0124 0.0320  136 PRO   A C   
2970 C C   B PRO   A 136 ? 0.1880 0.2337 0.2203 -0.0084 -0.0009 0.0181  136 PRO   A C   
2971 O O   A PRO   A 136 ? 0.1156 0.1595 0.2084 0.0006  0.0026  0.0261  136 PRO   A O   
2972 O O   B PRO   A 136 ? 0.1824 0.2365 0.2093 -0.0028 0.0008  0.0152  136 PRO   A O   
2973 C CB  A PRO   A 136 ? 0.1596 0.1826 0.2330 0.0122  -0.0054 0.0354  136 PRO   A CB  
2974 C CB  B PRO   A 136 ? 0.2318 0.2476 0.2311 -0.0062 0.0117  0.0260  136 PRO   A CB  
2975 C CG  A PRO   A 136 ? 0.1736 0.1901 0.2430 0.0182  0.0002  0.0482  136 PRO   A CG  
2976 C CG  B PRO   A 136 ? 0.2406 0.2520 0.2299 -0.0036 0.0187  0.0282  136 PRO   A CG  
2977 C CD  A PRO   A 136 ? 0.1651 0.1874 0.2135 0.0206  -0.0116 0.0704  136 PRO   A CD  
2978 C CD  B PRO   A 136 ? 0.2433 0.2547 0.2362 -0.0069 0.0096  0.0274  136 PRO   A CD  
2993 N N   A ILE   A 137 ? 0.1272 0.1801 0.2371 -0.0012 -0.0222 0.0216  137 ILE   A N   
2994 N N   B ILE   A 137 ? 0.1674 0.2267 0.2238 -0.0137 -0.0117 0.0215  137 ILE   A N   
2995 C CA  A ILE   A 137 ? 0.1313 0.1899 0.2371 -0.0061 -0.0348 0.0094  137 ILE   A CA  
2996 C CA  B ILE   A 137 ? 0.1574 0.2267 0.2268 -0.0192 -0.0213 0.0248  137 ILE   A CA  
2997 C C   A ILE   A 137 ? 0.1343 0.1908 0.2282 -0.0099 -0.0276 0.0194  137 ILE   A C   
2998 C C   B ILE   A 137 ? 0.1490 0.2208 0.2199 -0.0159 -0.0246 0.0281  137 ILE   A C   
2999 O O   A ILE   A 137 ? 0.1368 0.1862 0.2324 -0.0139 -0.0181 0.0136  137 ILE   A O   
3000 O O   B ILE   A 137 ? 0.1461 0.2108 0.2202 -0.0196 -0.0210 0.0224  137 ILE   A O   
3001 C CB  A ILE   A 137 ? 0.1371 0.2037 0.2579 -0.0036 -0.0534 -0.0011 137 ILE   A CB  
3002 C CB  B ILE   A 137 ? 0.1629 0.2365 0.2430 -0.0228 -0.0258 0.0154  137 ILE   A CB  
3003 C CG1 A ILE   A 137 ? 0.1464 0.2200 0.2719 0.0077  -0.0510 -0.0091 137 ILE   A CG1 
3004 C CG1 B ILE   A 137 ? 0.1713 0.2461 0.2528 -0.0236 -0.0269 0.0009  137 ILE   A CG1 
3005 C CG2 A ILE   A 137 ? 0.1498 0.2049 0.2879 -0.0086 -0.0610 0.0009  137 ILE   A CG2 
3006 C CG2 B ILE   A 137 ? 0.1630 0.2340 0.2490 -0.0266 -0.0301 0.0131  137 ILE   A CG2 
3007 C CD1 A ILE   A 137 ? 0.1664 0.2366 0.2983 0.0168  -0.0421 -0.0133 137 ILE   A CD1 
3008 C CD1 B ILE   A 137 ? 0.1822 0.2500 0.2589 -0.0199 -0.0271 -0.0125 137 ILE   A CD1 
3031 N N   A HIS   A 138 ? 0.1375 0.2087 0.2326 -0.0057 -0.0100 0.0196  138 HIS   A N   
3032 N N   B HIS   A 138 ? 0.1444 0.2267 0.2236 -0.0143 -0.0241 0.0323  138 HIS   A N   
3033 C CA  A HIS   A 138 ? 0.1424 0.2146 0.2244 -0.0114 -0.0101 0.0313  138 HIS   A CA  
3034 C CA  B HIS   A 138 ? 0.1402 0.2284 0.2151 -0.0197 -0.0277 0.0327  138 HIS   A CA  
3035 C C   A HIS   A 138 ? 0.1399 0.2056 0.2142 -0.0105 -0.0109 0.0390  138 HIS   A C   
3036 C C   B HIS   A 138 ? 0.1336 0.2135 0.2117 -0.0179 -0.0257 0.0389  138 HIS   A C   
3037 O O   A HIS   A 138 ? 0.1498 0.2016 0.2146 -0.0169 -0.0060 0.0344  138 HIS   A O   
3038 O O   B HIS   A 138 ? 0.1349 0.2123 0.2091 -0.0225 -0.0250 0.0353  138 HIS   A O   
3039 C CB  A HIS   A 138 ? 0.1475 0.2279 0.2246 -0.0094 -0.0108 0.0203  138 HIS   A CB  
3040 C CB  B HIS   A 138 ? 0.1538 0.2405 0.2193 -0.0253 -0.0335 0.0246  138 HIS   A CB  
3041 C CG  A HIS   A 138 ? 0.1668 0.2384 0.2336 -0.0066 -0.0206 0.0048  138 HIS   A CG  
3042 C CG  B HIS   A 138 ? 0.1709 0.2517 0.2280 -0.0241 -0.0278 0.0142  138 HIS   A CG  
3043 N ND1 A HIS   A 138 ? 0.1861 0.2495 0.2461 -0.0063 -0.0256 0.0003  138 HIS   A ND1 
3044 N ND1 B HIS   A 138 ? 0.1832 0.2621 0.2401 -0.0236 -0.0244 0.0049  138 HIS   A ND1 
3045 C CD2 A HIS   A 138 ? 0.1667 0.2382 0.2281 0.0011  -0.0202 0.0051  138 HIS   A CD2 
3046 C CD2 B HIS   A 138 ? 0.1752 0.2564 0.2248 -0.0216 -0.0284 0.0113  138 HIS   A CD2 
3047 C CE1 A HIS   A 138 ? 0.1892 0.2476 0.2416 -0.0023 -0.0278 -0.0039 138 HIS   A CE1 
3048 C CE1 B HIS   A 138 ? 0.1869 0.2634 0.2388 -0.0216 -0.0240 0.0010  138 HIS   A CE1 
3049 N NE2 A HIS   A 138 ? 0.1807 0.2436 0.2298 -0.0001 -0.0158 -0.0031 138 HIS   A NE2 
3050 N NE2 B HIS   A 138 ? 0.1800 0.2606 0.2264 -0.0187 -0.0233 0.0049  138 HIS   A NE2 
3065 N N   . SER   A 139 ? 0.1389 0.2001 0.2194 -0.0075 -0.0153 0.0532  139 SER   A N   
3066 C CA  . SER   A 139 ? 0.1368 0.1871 0.2192 -0.0071 -0.0081 0.0572  139 SER   A CA  
3067 C C   . SER   A 139 ? 0.1288 0.1729 0.2158 -0.0112 -0.0041 0.0406  139 SER   A C   
3068 O O   . SER   A 139 ? 0.1283 0.1648 0.2211 -0.0117 -0.0027 0.0441  139 SER   A O   
3069 C CB  . SER   A 139 ? 0.1346 0.1801 0.2329 -0.0106 -0.0101 0.0594  139 SER   A CB  
3070 O OG  . SER   A 139 ? 0.1411 0.1726 0.2184 -0.0085 -0.0130 0.0605  139 SER   A OG  
3077 N N   . LEU   A 140 ? 0.1245 0.1763 0.2143 -0.0073 -0.0021 0.0503  140 LEU   A N   
3078 C CA  . LEU   A 140 ? 0.1250 0.1742 0.2123 -0.0103 -0.0030 0.0432  140 LEU   A CA  
3079 C C   . LEU   A 140 ? 0.1174 0.1757 0.2035 -0.0145 -0.0005 0.0368  140 LEU   A C   
3080 O O   . LEU   A 140 ? 0.1249 0.1749 0.2217 -0.0059 -0.0092 0.0382  140 LEU   A O   
3081 C CB  . LEU   A 140 ? 0.1225 0.1819 0.2389 -0.0067 0.0046  0.0463  140 LEU   A CB  
3082 C CG  . LEU   A 140 ? 0.1275 0.1897 0.2332 -0.0210 0.0066  0.0492  140 LEU   A CG  
3083 C CD1 . LEU   A 140 ? 0.1352 0.1907 0.2407 -0.0165 0.0019  0.0482  140 LEU   A CD1 
3084 C CD2 . LEU   A 140 ? 0.1399 0.2068 0.2469 -0.0153 0.0071  0.0528  140 LEU   A CD2 
3096 N N   . ARG   A 141 ? 0.1261 0.1782 0.2169 -0.0193 -0.0156 0.0355  141 ARG   A N   
3097 C CA  . ARG   A 141 ? 0.1372 0.1978 0.2374 -0.0290 -0.0273 0.0124  141 ARG   A CA  
3098 C C   . ARG   A 141 ? 0.1383 0.1748 0.2210 -0.0202 -0.0205 0.0162  141 ARG   A C   
3099 O O   . ARG   A 141 ? 0.1373 0.1653 0.2225 -0.0232 -0.0028 0.0137  141 ARG   A O   
3100 C CB  . ARG   A 141 ? 0.1549 0.2258 0.2663 -0.0353 -0.0377 -0.0047 141 ARG   A CB  
3101 C CG  . ARG   A 141 ? 0.1960 0.2615 0.3106 -0.0351 -0.0294 -0.0104 141 ARG   A CG  
3102 C CD  . ARG   A 141 ? 0.2188 0.2834 0.3404 -0.0402 -0.0263 -0.0031 141 ARG   A CD  
3103 N NE  . ARG   A 141 ? 0.2069 0.2939 0.3466 -0.0510 -0.0293 0.0024  141 ARG   A NE  
3104 C CZ  . ARG   A 141 ? 0.2033 0.3113 0.3526 -0.0599 -0.0195 0.0050  141 ARG   A CZ  
3105 N NH1 . ARG   A 141 ? 0.1948 0.3181 0.3475 -0.0663 -0.0052 -0.0017 141 ARG   A NH1 
3106 N NH2 . ARG   A 141 ? 0.2063 0.3181 0.3606 -0.0559 -0.0337 0.0110  141 ARG   A NH2 
3120 N N   . VAL   A 142 ? 0.1330 0.1693 0.2047 -0.0154 -0.0100 0.0147  142 VAL   A N   
3121 C CA  . VAL   A 142 ? 0.1344 0.1657 0.2057 -0.0088 0.0058  0.0124  142 VAL   A CA  
3122 C C   . VAL   A 142 ? 0.1301 0.1567 0.1999 -0.0183 0.0012  0.0176  142 VAL   A C   
3123 O O   . VAL   A 142 ? 0.1332 0.1547 0.2019 -0.0062 -0.0043 0.0166  142 VAL   A O   
3124 C CB  . VAL   A 142 ? 0.1456 0.1753 0.2069 -0.0121 0.0013  0.0248  142 VAL   A CB  
3125 C CG1 . VAL   A 142 ? 0.1453 0.1703 0.2102 -0.0194 0.0028  0.0238  142 VAL   A CG1 
3126 C CG2 . VAL   A 142 ? 0.1579 0.1949 0.2273 -0.0057 -0.0056 0.0230  142 VAL   A CG2 
3136 N N   . CYS   A 143 ? 0.1287 0.1516 0.1947 -0.0131 -0.0057 0.0154  143 CYS   A N   
3137 C CA  . CYS   A 143 ? 0.1292 0.1490 0.2032 -0.0158 -0.0003 0.0141  143 CYS   A CA  
3138 C C   . CYS   A 143 ? 0.1289 0.1448 0.2032 -0.0144 -0.0028 0.0266  143 CYS   A C   
3139 O O   . CYS   A 143 ? 0.1305 0.1411 0.2053 -0.0121 -0.0029 0.0281  143 CYS   A O   
3140 C CB  . CYS   A 143 ? 0.1418 0.1476 0.2125 -0.0101 0.0121  0.0269  143 CYS   A CB  
3141 S SG  . CYS   A 143 ? 0.1527 0.1553 0.1963 0.0017  0.0077  0.0145  143 CYS   A SG  
3147 N N   . VAL   A 144 ? 0.1259 0.1479 0.2182 -0.0059 0.0015  0.0309  144 VAL   A N   
3148 C CA  . VAL   A 144 ? 0.1364 0.1555 0.2428 -0.0098 0.0110  0.0366  144 VAL   A CA  
3149 C C   . VAL   A 144 ? 0.1389 0.1470 0.2442 -0.0243 -0.0200 0.0308  144 VAL   A C   
3150 O O   . VAL   A 144 ? 0.1488 0.1518 0.2512 -0.0131 -0.0105 0.0356  144 VAL   A O   
3151 C CB  . VAL   A 144 ? 0.1610 0.1796 0.2987 -0.0082 0.0268  0.0380  144 VAL   A CB  
3152 C CG1 . VAL   A 144 ? 0.1716 0.1980 0.3353 -0.0226 0.0109  0.0355  144 VAL   A CG1 
3153 C CG2 . VAL   A 144 ? 0.1564 0.1859 0.3087 -0.0082 0.0335  0.0396  144 VAL   A CG2 
3163 N N   . ASP   A 145 ? 0.1446 0.1430 0.2518 -0.0217 -0.0182 0.0186  145 ASP   A N   
3164 C CA  . ASP   A 145 ? 0.1511 0.1529 0.2695 -0.0241 -0.0175 0.0046  145 ASP   A CA  
3165 C C   . ASP   A 145 ? 0.1538 0.1400 0.2510 -0.0191 -0.0078 0.0017  145 ASP   A C   
3166 O O   . ASP   A 145 ? 0.1638 0.1512 0.2911 -0.0167 -0.0070 -0.0391 145 ASP   A O   
3167 C CB  . ASP   A 145 ? 0.1627 0.1795 0.2913 -0.0269 -0.0230 0.0017  145 ASP   A CB  
3168 C CG  . ASP   A 145 ? 0.1852 0.2145 0.3262 -0.0456 -0.0395 0.0129  145 ASP   A CG  
3169 O OD1 . ASP   A 145 ? 0.1832 0.2236 0.3436 -0.0612 -0.0308 0.0192  145 ASP   A OD1 
3170 O OD2 . ASP   A 145 ? 0.2030 0.2390 0.3394 -0.0564 -0.0649 0.0073  145 ASP   A OD2 
3175 N N   . THR   A 146 ? 0.1369 0.1346 0.2105 -0.0123 0.0010  0.0109  146 THR   A N   
3176 C CA  . THR   A 146 ? 0.1366 0.1346 0.1895 -0.0089 -0.0028 0.0049  146 THR   A CA  
3177 C C   . THR   A 146 ? 0.1259 0.1332 0.1898 -0.0065 0.0081  0.0153  146 THR   A C   
3178 O O   . THR   A 146 ? 0.1350 0.1472 0.2042 -0.0015 -0.0001 0.0111  146 THR   A O   
3179 C CB  . THR   A 146 ? 0.1396 0.1347 0.1796 -0.0050 0.0004  0.0085  146 THR   A CB  
3180 O OG1 . THR   A 146 ? 0.1323 0.1554 0.1966 -0.0024 -0.0032 0.0052  146 THR   A OG1 
3181 C CG2 . THR   A 146 ? 0.1360 0.1341 0.2000 -0.0129 -0.0016 0.0124  146 THR   A CG2 
3189 N N   . VAL   A 147 ? 0.1254 0.1359 0.1894 -0.0042 0.0033  0.0172  147 VAL   A N   
3190 C CA  . VAL   A 147 ? 0.1302 0.1366 0.1959 -0.0080 0.0154  0.0223  147 VAL   A CA  
3191 C C   . VAL   A 147 ? 0.1328 0.1338 0.2012 -0.0136 0.0138  0.0232  147 VAL   A C   
3192 O O   . VAL   A 147 ? 0.1320 0.1378 0.2325 -0.0127 0.0090  0.0272  147 VAL   A O   
3193 C CB  . VAL   A 147 ? 0.1440 0.1342 0.1846 -0.0138 0.0166  0.0261  147 VAL   A CB  
3194 C CG1 . VAL   A 147 ? 0.1699 0.1458 0.1835 -0.0051 0.0111  0.0242  147 VAL   A CG1 
3195 C CG2 . VAL   A 147 ? 0.1485 0.1395 0.1871 -0.0166 0.0101  0.0217  147 VAL   A CG2 
3205 N N   . ARG   A 148 ? 0.1342 0.1407 0.1986 -0.0131 0.0107  0.0348  148 ARG   A N   
3206 C CA  . ARG   A 148 ? 0.1432 0.1412 0.1978 -0.0083 0.0062  0.0443  148 ARG   A CA  
3207 C C   . ARG   A 148 ? 0.1566 0.1434 0.2001 -0.0177 0.0082  0.0516  148 ARG   A C   
3208 O O   . ARG   A 148 ? 0.1849 0.1567 0.2265 -0.0167 0.0170  0.0459  148 ARG   A O   
3209 C CB  . ARG   A 148 ? 0.1475 0.1463 0.2169 -0.0053 0.0242  0.0379  148 ARG   A CB  
3210 C CG  . ARG   A 148 ? 0.1619 0.1486 0.2446 -0.0031 0.0312  0.0226  148 ARG   A CG  
3211 C CD  . ARG   A 148 ? 0.1750 0.1445 0.2613 -0.0030 0.0379  0.0416  148 ARG   A CD  
3212 N NE  . ARG   A 148 ? 0.1676 0.1508 0.2601 0.0067  0.0456  0.0437  148 ARG   A NE  
3213 C CZ  . ARG   A 148 ? 0.1658 0.1371 0.2384 0.0003  0.0425  0.0412  148 ARG   A CZ  
3214 N NH1 . ARG   A 148 ? 0.1705 0.1351 0.2583 -0.0065 0.0360  0.0148  148 ARG   A NH1 
3215 N NH2 . ARG   A 148 ? 0.1598 0.1574 0.2563 0.0074  0.0372  0.0424  148 ARG   A NH2 
3229 N N   . THR   A 149 ? 0.1513 0.1558 0.1980 -0.0178 0.0008  0.0421  149 THR   A N   
3230 C CA  . THR   A 149 ? 0.1492 0.1626 0.1934 -0.0190 0.0090  0.0415  149 THR   A CA  
3231 C C   . THR   A 149 ? 0.1491 0.1556 0.1775 -0.0235 0.0078  0.0500  149 THR   A C   
3232 O O   . THR   A 149 ? 0.1480 0.1634 0.2097 -0.0229 0.0009  0.0387  149 THR   A O   
3233 C CB  . THR   A 149 ? 0.1464 0.1733 0.2005 -0.0181 0.0059  0.0392  149 THR   A CB  
3234 O OG1 . THR   A 149 ? 0.1563 0.1606 0.2111 -0.0244 0.0012  0.0350  149 THR   A OG1 
3235 C CG2 . THR   A 149 ? 0.1475 0.1867 0.2216 -0.0078 -0.0035 0.0339  149 THR   A CG2 
3243 N N   . ASN   A 150 ? 0.1495 0.1603 0.1884 -0.0140 -0.0047 0.0427  150 ASN   A N   
3244 C CA  . ASN   A 150 ? 0.1592 0.1732 0.1940 -0.0151 0.0150  0.0422  150 ASN   A CA  
3245 C C   . ASN   A 150 ? 0.1442 0.1634 0.2014 -0.0187 0.0007  0.0384  150 ASN   A C   
3246 O O   . ASN   A 150 ? 0.1549 0.1775 0.2357 -0.0238 -0.0185 0.0387  150 ASN   A O   
3247 C CB  . ASN   A 150 ? 0.2071 0.2013 0.2273 -0.0180 0.0402  0.0581  150 ASN   A CB  
3248 C CG  . ASN   A 150 ? 0.2640 0.2363 0.2966 -0.0139 0.0258  0.0682  150 ASN   A CG  
3249 O OD1 . ASN   A 150 ? 0.2902 0.2479 0.3199 -0.0223 0.0226  0.0834  150 ASN   A OD1 
3250 N ND2 . ASN   A 150 ? 0.2938 0.2611 0.3331 -0.0066 0.0158  0.0677  150 ASN   A ND2 
3257 N N   . VAL   A 151 ? 0.1407 0.1521 0.1993 -0.0176 0.0072  0.0448  151 VAL   A N   
3258 C CA  . VAL   A 151 ? 0.1445 0.1560 0.1972 -0.0199 0.0149  0.0358  151 VAL   A CA  
3259 C C   . VAL   A 151 ? 0.1398 0.1499 0.2094 -0.0260 0.0189  0.0395  151 VAL   A C   
3260 O O   . VAL   A 151 ? 0.1497 0.1583 0.2319 -0.0217 0.0180  0.0398  151 VAL   A O   
3261 C CB  . VAL   A 151 ? 0.1690 0.1677 0.1967 -0.0090 0.0142  0.0403  151 VAL   A CB  
3262 C CG1 . VAL   A 151 ? 0.1657 0.1924 0.2239 -0.0094 0.0017  0.0343  151 VAL   A CG1 
3263 C CG2 . VAL   A 151 ? 0.1809 0.1706 0.2056 -0.0072 0.0288  0.0312  151 VAL   A CG2 
3273 N N   . TYR   A 152 ? 0.1412 0.1514 0.1973 -0.0219 0.0108  0.0395  152 TYR   A N   
3274 C CA  . TYR   A 152 ? 0.1406 0.1561 0.1768 -0.0242 0.0102  0.0314  152 TYR   A CA  
3275 C C   . TYR   A 152 ? 0.1355 0.1545 0.1640 -0.0229 0.0188  0.0322  152 TYR   A C   
3276 O O   . TYR   A 152 ? 0.1471 0.1508 0.1788 -0.0263 0.0251  0.0230  152 TYR   A O   
3277 C CB  . TYR   A 152 ? 0.1527 0.1674 0.1762 -0.0174 0.0189  0.0318  152 TYR   A CB  
3278 C CG  . TYR   A 152 ? 0.1711 0.1844 0.1819 -0.0248 0.0297  0.0364  152 TYR   A CG  
3279 C CD1 . TYR   A 152 ? 0.1821 0.2061 0.2087 -0.0208 0.0243  0.0465  152 TYR   A CD1 
3280 C CD2 . TYR   A 152 ? 0.1722 0.1947 0.1685 -0.0315 0.0231  0.0320  152 TYR   A CD2 
3281 C CE1 . TYR   A 152 ? 0.1992 0.2172 0.2039 -0.0147 0.0099  0.0566  152 TYR   A CE1 
3282 C CE2 . TYR   A 152 ? 0.1953 0.2132 0.1747 -0.0329 0.0199  0.0428  152 TYR   A CE2 
3283 C CZ  . TYR   A 152 ? 0.2144 0.2193 0.1831 -0.0256 0.0126  0.0607  152 TYR   A CZ  
3284 O OH  . TYR   A 152 ? 0.2420 0.2404 0.2153 -0.0162 0.0225  0.0720  152 TYR   A OH  
3294 N N   . LEU   A 153 ? 0.1370 0.1520 0.1767 -0.0270 0.0203  0.0411  153 LEU   A N   
3295 C CA  . LEU   A 153 ? 0.1377 0.1509 0.1969 -0.0115 0.0234  0.0394  153 LEU   A CA  
3296 C C   . LEU   A 153 ? 0.1416 0.1540 0.2115 -0.0071 0.0407  0.0424  153 LEU   A C   
3297 O O   . LEU   A 153 ? 0.1454 0.1611 0.2440 -0.0139 0.0412  0.0350  153 LEU   A O   
3298 C CB  . LEU   A 153 ? 0.1296 0.1576 0.2054 -0.0125 0.0111  0.0411  153 LEU   A CB  
3299 C CG  . LEU   A 153 ? 0.1381 0.1581 0.1939 -0.0123 0.0143  0.0325  153 LEU   A CG  
3300 C CD1 . LEU   A 153 ? 0.1458 0.1641 0.2004 -0.0095 -0.0022 0.0295  153 LEU   A CD1 
3301 C CD2 . LEU   A 153 ? 0.1474 0.1655 0.2037 -0.0147 0.0324  0.0104  153 LEU   A CD2 
3313 N N   A ALA   A 154 ? 0.1394 0.1490 0.2141 -0.0046 0.0349  0.0431  154 ALA   A N   
3314 N N   B ALA   A 154 ? 0.1441 0.1532 0.2076 -0.0024 0.0311  0.0411  154 ALA   A N   
3315 C CA  A ALA   A 154 ? 0.1475 0.1522 0.2226 -0.0045 0.0371  0.0356  154 ALA   A CA  
3316 C CA  B ALA   A 154 ? 0.1525 0.1579 0.2106 -0.0010 0.0289  0.0389  154 ALA   A CA  
3317 C C   A ALA   A 154 ? 0.1481 0.1446 0.2405 -0.0011 0.0382  0.0333  154 ALA   A C   
3318 C C   B ALA   A 154 ? 0.1524 0.1540 0.2064 -0.0004 0.0289  0.0378  154 ALA   A C   
3319 O O   A ALA   A 154 ? 0.1544 0.1459 0.2417 -0.0077 0.0339  0.0253  154 ALA   A O   
3320 O O   B ALA   A 154 ? 0.1540 0.1543 0.2030 -0.0041 0.0263  0.0419  154 ALA   A O   
3321 C CB  A ALA   A 154 ? 0.1548 0.1596 0.2187 -0.0011 0.0244  0.0231  154 ALA   A CB  
3322 C CB  B ALA   A 154 ? 0.1598 0.1615 0.2112 -0.0004 0.0176  0.0351  154 ALA   A CB  
3333 N N   A VAL   A 155 ? 0.1553 0.1529 0.2607 0.0033  0.0344  0.0458  155 VAL   A N   
3334 N N   B VAL   A 155 ? 0.1557 0.1579 0.2105 -0.0039 0.0284  0.0393  155 VAL   A N   
3335 C CA  A VAL   A 155 ? 0.1629 0.1624 0.2803 0.0004  0.0303  0.0632  155 VAL   A CA  
3336 C CA  B VAL   A 155 ? 0.1622 0.1664 0.2289 -0.0034 0.0225  0.0452  155 VAL   A CA  
3337 C C   A VAL   A 155 ? 0.1707 0.1737 0.3142 0.0163  0.0222  0.0655  155 VAL   A C   
3338 C C   B VAL   A 155 ? 0.1644 0.1745 0.2680 0.0025  0.0294  0.0444  155 VAL   A C   
3339 O O   A VAL   A 155 ? 0.1668 0.1797 0.3288 0.0279  0.0217  0.0576  155 VAL   A O   
3340 O O   B VAL   A 155 ? 0.1610 0.1792 0.2938 0.0058  0.0369  0.0465  155 VAL   A O   
3341 C CB  A VAL   A 155 ? 0.1586 0.1684 0.2791 0.0008  0.0139  0.0563  155 VAL   A CB  
3342 C CB  B VAL   A 155 ? 0.1571 0.1757 0.2255 -0.0035 0.0041  0.0362  155 VAL   A CB  
3343 C CG1 A VAL   A 155 ? 0.1709 0.1814 0.2814 -0.0042 0.0113  0.0574  155 VAL   A CG1 
3344 C CG1 B VAL   A 155 ? 0.1530 0.1838 0.2266 -0.0046 -0.0023 0.0316  155 VAL   A CG1 
3345 C CG2 A VAL   A 155 ? 0.1557 0.1723 0.2724 0.0171  0.0021  0.0586  155 VAL   A CG2 
3346 C CG2 B VAL   A 155 ? 0.1562 0.1718 0.2185 -0.0099 -0.0004 0.0350  155 VAL   A CG2 
3365 N N   A PHE   A 156 ? 0.1882 0.1775 0.3362 0.0201  0.0145  0.0766  156 PHE   A N   
3366 N N   B PHE   A 156 ? 0.1721 0.1787 0.2700 0.0089  0.0333  0.0383  156 PHE   A N   
3367 C CA  A PHE   A 156 ? 0.2147 0.1848 0.3637 0.0260  -0.0042 0.0745  156 PHE   A CA  
3368 C CA  B PHE   A 156 ? 0.1910 0.1944 0.2918 0.0184  0.0362  0.0304  156 PHE   A CA  
3369 C C   A PHE   A 156 ? 0.2087 0.1893 0.3829 0.0356  -0.0104 0.0715  156 PHE   A C   
3370 C C   B PHE   A 156 ? 0.1990 0.2051 0.2881 0.0223  0.0345  0.0467  156 PHE   A C   
3371 O O   A PHE   A 156 ? 0.2192 0.2083 0.4105 0.0334  -0.0074 0.0280  156 PHE   A O   
3372 O O   B PHE   A 156 ? 0.2027 0.1974 0.2863 0.0270  0.0291  0.0417  156 PHE   A O   
3373 C CB  A PHE   A 156 ? 0.2524 0.1937 0.3688 0.0272  -0.0216 0.0757  156 PHE   A CB  
3374 C CB  B PHE   A 156 ? 0.2071 0.2078 0.3055 0.0204  0.0354  0.0115  156 PHE   A CB  
3375 C CG  A PHE   A 156 ? 0.2910 0.2106 0.3813 0.0394  -0.0417 0.0651  156 PHE   A CG  
3376 C CG  B PHE   A 156 ? 0.2284 0.2262 0.3253 0.0223  0.0308  -0.0096 156 PHE   A CG  
3377 C CD1 A PHE   A 156 ? 0.3102 0.2212 0.3879 0.0448  -0.0471 0.0574  156 PHE   A CD1 
3378 C CD1 B PHE   A 156 ? 0.2369 0.2312 0.3320 0.0254  0.0311  -0.0211 156 PHE   A CD1 
3379 C CD2 A PHE   A 156 ? 0.3070 0.2214 0.3877 0.0469  -0.0492 0.0562  156 PHE   A CD2 
3380 C CD2 B PHE   A 156 ? 0.2345 0.2358 0.3373 0.0161  0.0249  -0.0171 156 PHE   A CD2 
3381 C CE1 A PHE   A 156 ? 0.3224 0.2319 0.4006 0.0448  -0.0437 0.0422  156 PHE   A CE1 
3382 C CE1 B PHE   A 156 ? 0.2403 0.2359 0.3373 0.0251  0.0293  -0.0283 156 PHE   A CE1 
3383 C CE2 A PHE   A 156 ? 0.3213 0.2322 0.3948 0.0465  -0.0453 0.0438  156 PHE   A CE2 
3384 C CE2 B PHE   A 156 ? 0.2404 0.2387 0.3449 0.0186  0.0217  -0.0261 156 PHE   A CE2 
3385 C CZ  A PHE   A 156 ? 0.3249 0.2357 0.4012 0.0487  -0.0422 0.0340  156 PHE   A CZ  
3386 C CZ  B PHE   A 156 ? 0.2410 0.2383 0.3420 0.0239  0.0270  -0.0323 156 PHE   A CZ  
3405 N N   A ASP   A 157 ? 0.2013 0.1933 0.3734 0.0295  -0.0125 0.1004  157 ASP   A N   
3406 N N   B ASP   A 157 ? 0.2013 0.2241 0.2903 0.0210  0.0269  0.0596  157 ASP   A N   
3407 C CA  A ASP   A 157 ? 0.1957 0.1981 0.3839 0.0294  -0.0108 0.1054  157 ASP   A CA  
3408 C CA  B ASP   A 157 ? 0.2057 0.2474 0.3032 0.0128  0.0263  0.0726  157 ASP   A CA  
3409 C C   A ASP   A 157 ? 0.1872 0.2053 0.3824 0.0331  0.0074  0.1078  157 ASP   A C   
3410 C C   B ASP   A 157 ? 0.2017 0.2596 0.3210 0.0087  0.0325  0.0734  157 ASP   A C   
3411 O O   A ASP   A 157 ? 0.1741 0.1918 0.3734 0.0286  0.0228  0.1158  157 ASP   A O   
3412 O O   B ASP   A 157 ? 0.2012 0.2566 0.3173 0.0050  0.0256  0.0733  157 ASP   A O   
3413 C CB  A ASP   A 157 ? 0.2038 0.2047 0.4050 0.0279  -0.0204 0.1104  157 ASP   A CB  
3414 C CB  B ASP   A 157 ? 0.2092 0.2532 0.3003 0.0071  0.0240  0.0905  157 ASP   A CB  
3415 C CG  A ASP   A 157 ? 0.2203 0.2197 0.4270 0.0236  -0.0267 0.1083  157 ASP   A CG  
3416 C CG  B ASP   A 157 ? 0.2168 0.2581 0.3010 0.0088  0.0210  0.1052  157 ASP   A CG  
3417 O OD1 A ASP   A 157 ? 0.2424 0.2308 0.4501 0.0107  -0.0438 0.1009  157 ASP   A OD1 
3418 O OD1 B ASP   A 157 ? 0.2168 0.2543 0.2901 0.0107  0.0158  0.1177  157 ASP   A OD1 
3419 O OD2 A ASP   A 157 ? 0.2095 0.2110 0.4296 0.0212  -0.0163 0.1113  157 ASP   A OD2 
3420 O OD2 B ASP   A 157 ? 0.2185 0.2678 0.3121 0.0070  0.0222  0.1063  157 ASP   A OD2 
3429 N N   A LYS   A 158 ? 0.1905 0.2299 0.3999 0.0373  0.0168  0.0890  158 LYS   A N   
3430 N N   B LYS   A 158 ? 0.2007 0.2719 0.3389 0.0064  0.0437  0.0762  158 LYS   A N   
3431 C CA  A LYS   A 158 ? 0.1888 0.2573 0.4101 0.0393  0.0315  0.0796  158 LYS   A CA  
3432 C CA  B LYS   A 158 ? 0.2006 0.2884 0.3559 0.0047  0.0457  0.0735  158 LYS   A CA  
3433 C C   A LYS   A 158 ? 0.1773 0.2670 0.4094 0.0435  0.0278  0.0927  158 LYS   A C   
3434 C C   B LYS   A 158 ? 0.1917 0.2905 0.3586 0.0023  0.0288  0.0817  158 LYS   A C   
3435 O O   A LYS   A 158 ? 0.1683 0.2670 0.4057 0.0415  0.0369  0.0965  158 LYS   A O   
3436 O O   B LYS   A 158 ? 0.1878 0.2887 0.3616 -0.0078 0.0326  0.0812  158 LYS   A O   
3437 C CB  A LYS   A 158 ? 0.2069 0.2731 0.4194 0.0387  0.0518  0.0727  158 LYS   A CB  
3438 C CB  B LYS   A 158 ? 0.2130 0.3008 0.3733 0.0104  0.0572  0.0663  158 LYS   A CB  
3439 C CG  A LYS   A 158 ? 0.2284 0.2956 0.4309 0.0347  0.0657  0.0696  158 LYS   A CG  
3440 C CG  B LYS   A 158 ? 0.2246 0.3127 0.3880 0.0114  0.0665  0.0655  158 LYS   A CG  
3441 C CD  A LYS   A 158 ? 0.2418 0.3163 0.4406 0.0321  0.0789  0.0721  158 LYS   A CD  
3442 C CD  B LYS   A 158 ? 0.2343 0.3235 0.3942 0.0082  0.0774  0.0676  158 LYS   A CD  
3443 C CE  A LYS   A 158 ? 0.2472 0.3314 0.4484 0.0291  0.0841  0.0797  158 LYS   A CE  
3444 C CE  B LYS   A 158 ? 0.2390 0.3319 0.3971 0.0068  0.0844  0.0712  158 LYS   A CE  
3445 N NZ  A LYS   A 158 ? 0.2483 0.3380 0.4498 0.0239  0.0830  0.0875  158 LYS   A NZ  
3446 N NZ  B LYS   A 158 ? 0.2432 0.3354 0.3974 0.0028  0.0922  0.0768  158 LYS   A NZ  
3473 N N   A ASN   A 159 ? 0.1772 0.2779 0.4165 0.0484  0.0103  0.1004  159 ASN   A N   
3474 N N   B ASN   A 159 ? 0.1850 0.2958 0.3572 0.0104  0.0097  0.0911  159 ASN   A N   
3475 C CA  A ASN   A 159 ? 0.1852 0.2888 0.4125 0.0446  -0.0056 0.1078  159 ASN   A CA  
3476 C CA  B ASN   A 159 ? 0.1801 0.2981 0.3546 0.0181  -0.0099 0.1014  159 ASN   A CA  
3477 C C   A ASN   A 159 ? 0.1712 0.2860 0.3891 0.0263  -0.0063 0.1120  159 ASN   A C   
3478 C C   B ASN   A 159 ? 0.1620 0.2851 0.3532 0.0168  -0.0151 0.1209  159 ASN   A C   
3479 O O   A ASN   A 159 ? 0.1662 0.2958 0.3791 0.0273  -0.0227 0.1027  159 ASN   A O   
3480 O O   B ASN   A 159 ? 0.1457 0.2860 0.3338 0.0203  -0.0305 0.1290  159 ASN   A O   
3481 C CB  A ASN   A 159 ? 0.2110 0.3028 0.4299 0.0487  -0.0118 0.1109  159 ASN   A CB  
3482 C CB  B ASN   A 159 ? 0.1955 0.3111 0.3523 0.0195  -0.0149 0.0974  159 ASN   A CB  
3483 C CG  A ASN   A 159 ? 0.2362 0.3137 0.4497 0.0464  -0.0063 0.1066  159 ASN   A CG  
3484 C CG  B ASN   A 159 ? 0.2101 0.3201 0.3512 0.0177  -0.0110 0.0935  159 ASN   A CG  
3485 O OD1 A ASN   A 159 ? 0.2437 0.3189 0.4597 0.0416  0.0039  0.1032  159 ASN   A OD1 
3486 O OD1 B ASN   A 159 ? 0.2169 0.3205 0.3552 0.0169  -0.0079 0.1000  159 ASN   A OD1 
3487 N ND2 A ASN   A 159 ? 0.2478 0.3201 0.4613 0.0401  -0.0077 0.1007  159 ASN   A ND2 
3488 N ND2 B ASN   A 159 ? 0.2162 0.3270 0.3548 0.0152  -0.0107 0.0839  159 ASN   A ND2 
3501 N N   . LEU   A 160 ? 0.1601 0.2747 0.3782 0.0137  -0.0194 0.1192  160 LEU   A N   
3502 C CA  . LEU   A 160 ? 0.1624 0.2608 0.3771 0.0065  -0.0126 0.1210  160 LEU   A CA  
3503 C C   . LEU   A 160 ? 0.1417 0.2553 0.3718 0.0000  0.0110  0.1146  160 LEU   A C   
3504 O O   . LEU   A 160 ? 0.1458 0.2608 0.3950 -0.0031 0.0087  0.1103  160 LEU   A O   
3505 C CB  . LEU   A 160 ? 0.1737 0.2596 0.3621 -0.0000 -0.0082 0.1210  160 LEU   A CB  
3506 C CG  . LEU   A 160 ? 0.1785 0.2618 0.3577 -0.0148 0.0026  0.0990  160 LEU   A CG  
3507 C CD1 . LEU   A 160 ? 0.1958 0.2700 0.3602 -0.0117 0.0025  0.0836  160 LEU   A CD1 
3508 C CD2 . LEU   A 160 ? 0.1789 0.2583 0.3547 -0.0236 0.0157  0.0893  160 LEU   A CD2 
3521 N N   . TYR   A 161 ? 0.1425 0.2458 0.3666 0.0027  0.0207  0.1078  161 TYR   A N   
3522 C CA  . TYR   A 161 ? 0.1506 0.2354 0.3625 0.0050  0.0325  0.1014  161 TYR   A CA  
3523 C C   . TYR   A 161 ? 0.1470 0.2483 0.3709 0.0021  0.0297  0.0923  161 TYR   A C   
3524 O O   . TYR   A 161 ? 0.1380 0.2462 0.3820 -0.0062 0.0245  0.0858  161 TYR   A O   
3525 C CB  . TYR   A 161 ? 0.1631 0.2218 0.3726 0.0083  0.0337  0.0895  161 TYR   A CB  
3526 C CG  . TYR   A 161 ? 0.1579 0.2135 0.3734 0.0019  0.0305  0.0799  161 TYR   A CG  
3527 C CD1 . TYR   A 161 ? 0.1552 0.2047 0.3738 -0.0003 0.0266  0.0798  161 TYR   A CD1 
3528 C CD2 . TYR   A 161 ? 0.1585 0.2247 0.3769 0.0027  0.0203  0.0725  161 TYR   A CD2 
3529 C CE1 . TYR   A 161 ? 0.1690 0.2039 0.3830 -0.0048 0.0148  0.0820  161 TYR   A CE1 
3530 C CE2 . TYR   A 161 ? 0.1628 0.2195 0.3866 -0.0011 0.0097  0.0792  161 TYR   A CE2 
3531 C CZ  . TYR   A 161 ? 0.1778 0.2118 0.3967 -0.0110 0.0028  0.0898  161 TYR   A CZ  
3532 O OH  . TYR   A 161 ? 0.2051 0.2215 0.4237 -0.0219 -0.0054 0.0984  161 TYR   A OH  
3542 N N   A ASP   A 162 ? 0.1385 0.2580 0.3852 0.0021  0.0341  0.0931  162 ASP   A N   
3543 N N   B ASP   A 162 ? 0.1564 0.2604 0.3647 0.0044  0.0299  0.0775  162 ASP   A N   
3544 C CA  A ASP   A 162 ? 0.1334 0.2748 0.4003 -0.0078 0.0362  0.0907  162 ASP   A CA  
3545 C CA  B ASP   A 162 ? 0.1666 0.2760 0.3610 0.0002  0.0332  0.0623  162 ASP   A CA  
3546 C C   A ASP   A 162 ? 0.1254 0.2719 0.4005 -0.0091 0.0219  0.0934  162 ASP   A C   
3547 C C   B ASP   A 162 ? 0.1740 0.2810 0.3448 0.0036  0.0236  0.0496  162 ASP   A C   
3548 O O   A ASP   A 162 ? 0.1221 0.2607 0.4208 -0.0125 0.0225  0.0929  162 ASP   A O   
3549 O O   B ASP   A 162 ? 0.1733 0.2814 0.3515 0.0043  0.0191  0.0412  162 ASP   A O   
3550 C CB  A ASP   A 162 ? 0.1384 0.2940 0.4262 -0.0023 0.0462  0.0736  162 ASP   A CB  
3551 C CB  B ASP   A 162 ? 0.1699 0.2860 0.3817 -0.0007 0.0417  0.0548  162 ASP   A CB  
3552 C CG  A ASP   A 162 ? 0.1467 0.3145 0.4492 -0.0002 0.0519  0.0585  162 ASP   A CG  
3553 C CG  B ASP   A 162 ? 0.1768 0.2976 0.4054 -0.0046 0.0460  0.0495  162 ASP   A CG  
3554 O OD1 A ASP   A 162 ? 0.1592 0.3329 0.4679 -0.0079 0.0589  0.0504  162 ASP   A OD1 
3555 O OD1 B ASP   A 162 ? 0.1860 0.3092 0.4160 -0.0135 0.0534  0.0454  162 ASP   A OD1 
3556 O OD2 A ASP   A 162 ? 0.1422 0.3162 0.4567 0.0006  0.0514  0.0508  162 ASP   A OD2 
3557 O OD2 B ASP   A 162 ? 0.1816 0.3002 0.4265 -0.0031 0.0434  0.0434  162 ASP   A OD2 
3566 N N   A LYS   A 163 ? 0.1378 0.2866 0.3913 -0.0084 -0.0146 0.0879  163 LYS   A N   
3567 N N   B LYS   A 163 ? 0.1883 0.2922 0.3300 0.0051  0.0079  0.0454  163 LYS   A N   
3568 C CA  A LYS   A 163 ? 0.1522 0.3016 0.3744 -0.0113 -0.0292 0.0854  163 LYS   A CA  
3569 C CA  B LYS   A 163 ? 0.1988 0.3033 0.3122 0.0017  -0.0022 0.0490  163 LYS   A CA  
3570 C C   A LYS   A 163 ? 0.1446 0.2922 0.3656 -0.0121 -0.0125 0.0858  163 LYS   A C   
3571 C C   B LYS   A 163 ? 0.1927 0.2996 0.3013 -0.0003 0.0014  0.0528  163 LYS   A C   
3572 O O   A LYS   A 163 ? 0.1458 0.3044 0.3871 -0.0141 -0.0239 0.0826  163 LYS   A O   
3573 O O   B LYS   A 163 ? 0.1871 0.3022 0.3041 0.0018  -0.0078 0.0504  163 LYS   A O   
3574 C CB  A LYS   A 163 ? 0.1886 0.3264 0.3859 -0.0109 -0.0455 0.0795  163 LYS   A CB  
3575 C CB  B LYS   A 163 ? 0.2228 0.3172 0.3224 0.0041  -0.0151 0.0497  163 LYS   A CB  
3576 C CG  A LYS   A 163 ? 0.2236 0.3502 0.4123 -0.0170 -0.0431 0.0709  163 LYS   A CG  
3577 C CG  B LYS   A 163 ? 0.2436 0.3298 0.3387 0.0018  -0.0150 0.0510  163 LYS   A CG  
3578 C CD  A LYS   A 163 ? 0.2509 0.3713 0.4358 -0.0199 -0.0458 0.0606  163 LYS   A CD  
3579 C CD  B LYS   A 163 ? 0.2600 0.3402 0.3573 0.0006  -0.0168 0.0502  163 LYS   A CD  
3580 C CE  A LYS   A 163 ? 0.2664 0.3863 0.4553 -0.0232 -0.0457 0.0521  163 LYS   A CE  
3581 C CE  B LYS   A 163 ? 0.2689 0.3459 0.3758 0.0016  -0.0216 0.0501  163 LYS   A CE  
3582 N NZ  A LYS   A 163 ? 0.2799 0.3958 0.4706 -0.0247 -0.0447 0.0490  163 LYS   A NZ  
3583 N NZ  B LYS   A 163 ? 0.2716 0.3484 0.3880 0.0032  -0.0246 0.0470  163 LYS   A NZ  
3610 N N   A LEU   A 164 ? 0.1271 0.2672 0.3358 -0.0172 -0.0083 0.0815  164 LEU   A N   
3611 N N   B LEU   A 164 ? 0.1856 0.2885 0.2894 -0.0074 0.0028  0.0524  164 LEU   A N   
3612 C CA  A LEU   A 164 ? 0.1298 0.2495 0.3034 -0.0202 0.0102  0.0754  164 LEU   A CA  
3613 C CA  B LEU   A 164 ? 0.1874 0.2814 0.2801 -0.0154 0.0108  0.0515  164 LEU   A CA  
3614 C C   A LEU   A 164 ? 0.1361 0.2469 0.3105 -0.0206 0.0189  0.0744  164 LEU   A C   
3615 C C   B LEU   A 164 ? 0.1897 0.2834 0.2862 -0.0155 0.0116  0.0534  164 LEU   A C   
3616 O O   A LEU   A 164 ? 0.1440 0.2498 0.3140 -0.0213 0.0310  0.0538  164 LEU   A O   
3617 O O   B LEU   A 164 ? 0.1898 0.2840 0.2869 -0.0153 0.0168  0.0440  164 LEU   A O   
3618 C CB  A LEU   A 164 ? 0.1269 0.2358 0.2636 -0.0206 0.0250  0.0715  164 LEU   A CB  
3619 C CB  B LEU   A 164 ? 0.1849 0.2729 0.2650 -0.0207 0.0177  0.0530  164 LEU   A CB  
3620 C CG  A LEU   A 164 ? 0.1333 0.2284 0.2469 -0.0113 0.0097  0.0554  164 LEU   A CG  
3621 C CG  B LEU   A 164 ? 0.1827 0.2671 0.2533 -0.0191 0.0177  0.0468  164 LEU   A CG  
3622 C CD1 A LEU   A 164 ? 0.1252 0.2300 0.2368 0.0004  0.0106  0.0372  164 LEU   A CD1 
3623 C CD1 B LEU   A 164 ? 0.1756 0.2666 0.2417 -0.0171 0.0245  0.0423  164 LEU   A CD1 
3624 C CD2 A LEU   A 164 ? 0.1496 0.2231 0.2500 -0.0171 0.0105  0.0469  164 LEU   A CD2 
3625 C CD2 B LEU   A 164 ? 0.1897 0.2670 0.2545 -0.0166 0.0070  0.0378  164 LEU   A CD2 
3648 N N   A VAL   A 165 ? 0.1400 0.2449 0.3107 -0.0248 0.0246  0.0780  165 VAL   A N   
3649 N N   B VAL   A 165 ? 0.1938 0.2866 0.2906 -0.0190 0.0135  0.0573  165 VAL   A N   
3650 C CA  A VAL   A 165 ? 0.1412 0.2429 0.3027 -0.0267 0.0382  0.0786  165 VAL   A CA  
3651 C CA  B VAL   A 165 ? 0.1962 0.2911 0.2960 -0.0201 0.0163  0.0594  165 VAL   A CA  
3652 C C   A VAL   A 165 ? 0.1396 0.2557 0.3102 -0.0285 0.0437  0.0804  165 VAL   A C   
3653 C C   B VAL   A 165 ? 0.1993 0.2935 0.3020 -0.0183 0.0176  0.0530  165 VAL   A C   
3654 O O   A VAL   A 165 ? 0.1407 0.2561 0.3055 -0.0293 0.0412  0.0809  165 VAL   A O   
3655 O O   B VAL   A 165 ? 0.1992 0.2924 0.3039 -0.0187 0.0140  0.0452  165 VAL   A O   
3656 C CB  A VAL   A 165 ? 0.1491 0.2270 0.2942 -0.0172 0.0445  0.0663  165 VAL   A CB  
3657 C CB  B VAL   A 165 ? 0.1963 0.2941 0.3027 -0.0208 0.0143  0.0623  165 VAL   A CB  
3658 C CG1 A VAL   A 165 ? 0.1435 0.2271 0.3000 -0.0073 0.0490  0.0563  165 VAL   A CG1 
3659 C CG1 B VAL   A 165 ? 0.2027 0.2993 0.3133 -0.0206 0.0109  0.0601  165 VAL   A CG1 
3660 C CG2 A VAL   A 165 ? 0.1659 0.2198 0.2885 -0.0175 0.0421  0.0671  165 VAL   A CG2 
3661 C CG2 B VAL   A 165 ? 0.1964 0.2953 0.3041 -0.0201 0.0152  0.0661  165 VAL   A CG2 
3680 N N   A SER   A 166 ? 0.1344 0.2682 0.3205 -0.0201 0.0348  0.0731  166 SER   A N   
3681 N N   B SER   A 166 ? 0.2003 0.2971 0.3064 -0.0152 0.0201  0.0496  166 SER   A N   
3682 C CA  A SER   A 166 ? 0.1316 0.2818 0.3320 -0.0288 0.0274  0.0658  166 SER   A CA  
3683 C CA  B SER   A 166 ? 0.2100 0.3041 0.3157 -0.0122 0.0143  0.0414  166 SER   A CA  
3684 C C   A SER   A 166 ? 0.1244 0.2928 0.3431 -0.0315 0.0010  0.0513  166 SER   A C   
3685 C C   B SER   A 166 ? 0.2144 0.3116 0.3144 -0.0043 -0.0041 0.0391  166 SER   A C   
3686 O O   A SER   A 166 ? 0.1444 0.2949 0.3671 -0.0313 -0.0028 0.0382  166 SER   A O   
3687 O O   B SER   A 166 ? 0.2158 0.3161 0.3121 -0.0004 -0.0076 0.0388  166 SER   A O   
3688 C CB  A SER   A 166 ? 0.1541 0.2894 0.3446 -0.0223 0.0316  0.0608  166 SER   A CB  
3689 C CB  B SER   A 166 ? 0.2192 0.3065 0.3330 -0.0100 0.0219  0.0300  166 SER   A CB  
3690 O OG  A SER   A 166 ? 0.1941 0.2980 0.3662 -0.0214 0.0336  0.0621  166 SER   A OG  
3691 O OG  B SER   A 166 ? 0.2375 0.3099 0.3501 -0.0119 0.0285  0.0279  166 SER   A OG  
3702 N N   A SER   A 167 ? 0.1322 0.3011 0.3224 -0.0136 -0.0107 0.0493  167 SER   A N   
3703 N N   B SER   A 167 ? 0.2252 0.3196 0.3148 0.0003  -0.0137 0.0355  167 SER   A N   
3704 C CA  A SER   A 167 ? 0.1552 0.3102 0.3095 0.0007  -0.0125 0.0380  167 SER   A CA  
3705 C CA  B SER   A 167 ? 0.2445 0.3266 0.3196 0.0038  -0.0192 0.0265  167 SER   A CA  
3706 C C   A SER   A 167 ? 0.1593 0.3079 0.2975 0.0096  0.0004  0.0337  167 SER   A C   
3707 C C   B SER   A 167 ? 0.2607 0.3277 0.3218 0.0046  -0.0162 0.0270  167 SER   A C   
3708 O O   A SER   A 167 ? 0.1778 0.3181 0.3233 0.0138  -0.0137 0.0278  167 SER   A O   
3709 O O   B SER   A 167 ? 0.2641 0.3317 0.3361 0.0021  -0.0198 0.0220  167 SER   A O   
3710 C CB  A SER   A 167 ? 0.1708 0.3226 0.3113 0.0105  -0.0038 0.0349  167 SER   A CB  
3711 C CB  B SER   A 167 ? 0.2475 0.3345 0.3279 0.0067  -0.0165 0.0183  167 SER   A CB  
3712 O OG  A SER   A 167 ? 0.1712 0.3251 0.3101 0.0191  0.0092  0.0304  167 SER   A OG  
3713 O OG  B SER   A 167 ? 0.2454 0.3376 0.3295 0.0088  -0.0123 0.0117  167 SER   A OG  
3724 N N   A PHE   A 168 ? 0.1507 0.2964 0.2628 0.0114  0.0148  0.0374  168 PHE   A N   
3725 N N   B PHE   A 168 ? 0.2746 0.3256 0.3111 0.0067  -0.0115 0.0352  168 PHE   A N   
3726 C CA  A PHE   A 168 ? 0.1516 0.2899 0.2505 0.0036  0.0173  0.0346  168 PHE   A CA  
3727 C CA  B PHE   A 168 ? 0.2921 0.3255 0.3116 0.0063  -0.0072 0.0379  168 PHE   A CA  
3728 C C   A PHE   A 168 ? 0.1546 0.3018 0.2638 -0.0041 0.0312  0.0213  168 PHE   A C   
3729 C C   B PHE   A 168 ? 0.3156 0.3342 0.3325 0.0023  -0.0103 0.0348  168 PHE   A C   
3730 O O   A PHE   A 168 ? 0.1650 0.3074 0.3077 -0.0119 0.0351  0.0205  168 PHE   A O   
3731 O O   B PHE   A 168 ? 0.3195 0.3339 0.3337 0.0031  -0.0075 0.0321  168 PHE   A O   
3732 C CB  A PHE   A 168 ? 0.1557 0.2800 0.2332 0.0020  0.0041  0.0428  168 PHE   A CB  
3733 C CB  B PHE   A 168 ? 0.2884 0.3195 0.3006 0.0067  0.0003  0.0414  168 PHE   A CB  
3734 C CG  A PHE   A 168 ? 0.1521 0.2706 0.2137 -0.0117 -0.0092 0.0479  168 PHE   A CG  
3735 C CG  B PHE   A 168 ? 0.2824 0.3141 0.2852 0.0073  0.0047  0.0412  168 PHE   A CG  
3736 C CD1 A PHE   A 168 ? 0.1540 0.2737 0.2189 -0.0202 -0.0168 0.0529  168 PHE   A CD1 
3737 C CD1 B PHE   A 168 ? 0.2790 0.3127 0.2802 0.0100  0.0068  0.0428  168 PHE   A CD1 
3738 C CD2 A PHE   A 168 ? 0.1508 0.2640 0.2046 -0.0106 -0.0038 0.0427  168 PHE   A CD2 
3739 C CD2 B PHE   A 168 ? 0.2803 0.3122 0.2807 0.0079  0.0067  0.0382  168 PHE   A CD2 
3740 C CE1 A PHE   A 168 ? 0.1472 0.2754 0.2136 -0.0229 -0.0165 0.0509  168 PHE   A CE1 
3741 C CE1 B PHE   A 168 ? 0.2769 0.3108 0.2755 0.0099  0.0059  0.0453  168 PHE   A CE1 
3742 C CE2 A PHE   A 168 ? 0.1505 0.2649 0.2120 -0.0132 -0.0011 0.0456  168 PHE   A CE2 
3743 C CE2 B PHE   A 168 ? 0.2781 0.3115 0.2803 0.0065  0.0046  0.0388  168 PHE   A CE2 
3744 C CZ  A PHE   A 168 ? 0.1486 0.2735 0.2134 -0.0169 -0.0092 0.0491  168 PHE   A CZ  
3745 C CZ  B PHE   A 168 ? 0.2780 0.3121 0.2780 0.0076  0.0053  0.0424  168 PHE   A CZ  
3764 N N   A LEU   A 169 ? 0.1749 0.3078 0.2717 -0.0069 0.0301  -0.0005 169 LEU   A N   
3765 N N   B LEU   A 169 ? 0.3357 0.3433 0.3503 -0.0057 -0.0166 0.0342  169 LEU   A N   
3766 C CA  A LEU   A 169 ? 0.2133 0.3218 0.3197 0.0042  0.0065  -0.0106 169 LEU   A CA  
3767 C CA  B LEU   A 169 ? 0.3544 0.3544 0.3628 -0.0135 -0.0215 0.0360  169 LEU   A CA  
3768 C C   A LEU   A 169 ? 0.2131 0.3220 0.3349 0.0062  0.0064  0.0012  169 LEU   A C   
3769 C C   B LEU   A 169 ? 0.3641 0.3624 0.3815 -0.0165 -0.0329 0.0324  169 LEU   A C   
3770 O O   A LEU   A 169 ? 0.2167 0.3215 0.3302 0.0096  0.0064  0.0021  169 LEU   A O   
3771 O O   B LEU   A 169 ? 0.3697 0.3661 0.3911 -0.0181 -0.0341 0.0308  169 LEU   A O   
3772 C CB  A LEU   A 169 ? 0.2401 0.3358 0.3463 0.0089  -0.0093 -0.0237 169 LEU   A CB  
3773 C CB  B LEU   A 169 ? 0.3619 0.3575 0.3568 -0.0185 -0.0127 0.0418  169 LEU   A CB  
3774 C CG  A LEU   A 169 ? 0.2645 0.3470 0.3686 0.0065  -0.0230 -0.0381 169 LEU   A CG  
3775 C CG  B LEU   A 169 ? 0.3671 0.3600 0.3543 -0.0225 -0.0059 0.0455  169 LEU   A CG  
3776 C CD1 A LEU   A 169 ? 0.2748 0.3500 0.3781 0.0072  -0.0290 -0.0389 169 LEU   A CD1 
3777 C CD1 B LEU   A 169 ? 0.3717 0.3630 0.3558 -0.0218 -0.0051 0.0433  169 LEU   A CD1 
3778 C CD2 A LEU   A 169 ? 0.2717 0.3519 0.3735 0.0034  -0.0241 -0.0418 169 LEU   A CD2 
3779 C CD2 B LEU   A 169 ? 0.3665 0.3589 0.3540 -0.0252 -0.0007 0.0474  169 LEU   A CD2 
3780 O OXT A LEU   A 169 ? 0.2089 0.3250 0.3463 0.0077  0.0068  0.0038  169 LEU   A OXT 
3781 O OXT B LEU   A 169 ? 0.3668 0.3668 0.3903 -0.0185 -0.0379 0.0301  169 LEU   A OXT 
3804 N N   A SER   B 1   ? 0.3768 0.3700 0.3965 -0.1152 -0.0783 0.0518  1   SER   B N   
3805 N N   B SER   B 1   ? 0.3666 0.3501 0.3579 -0.0938 -0.0647 0.0266  1   SER   B N   
3806 C CA  A SER   B 1   ? 0.3652 0.3676 0.3871 -0.1185 -0.0810 0.0537  1   SER   B CA  
3807 C CA  B SER   B 1   ? 0.3601 0.3523 0.3545 -0.0944 -0.0667 0.0263  1   SER   B CA  
3808 C C   A SER   B 1   ? 0.3294 0.3576 0.3575 -0.1212 -0.0855 0.0745  1   SER   B C   
3809 C C   B SER   B 1   ? 0.3428 0.3531 0.3392 -0.0881 -0.0717 0.0418  1   SER   B C   
3810 O O   A SER   B 1   ? 0.3376 0.3540 0.3287 -0.1160 -0.0834 0.0689  1   SER   B O   
3811 O O   B SER   B 1   ? 0.3425 0.3493 0.3168 -0.0876 -0.0763 0.0378  1   SER   B O   
3812 C CB  A SER   B 1   ? 0.3820 0.3716 0.4057 -0.1166 -0.0739 0.0390  1   SER   B CB  
3813 C CB  B SER   B 1   ? 0.3681 0.3510 0.3664 -0.0981 -0.0600 0.0119  1   SER   B CB  
3814 O OG  A SER   B 1   ? 0.3979 0.3818 0.4390 -0.1106 -0.0647 0.0315  1   SER   B OG  
3815 O OG  B SER   B 1   ? 0.3757 0.3547 0.3872 -0.0989 -0.0541 0.0039  1   SER   B OG  
3830 N N   A MET   B 2   ? 0.2985 0.3486 0.3573 -0.1219 -0.0844 0.1131  2   MET   B N   
3831 N N   B MET   B 2   ? 0.3308 0.3568 0.3455 -0.0779 -0.0678 0.0671  2   MET   B N   
3832 C CA  A MET   B 2   ? 0.2807 0.3450 0.3747 -0.1015 -0.0850 0.1293  2   MET   B CA  
3833 C CA  B MET   B 2   ? 0.3211 0.3580 0.3545 -0.0619 -0.0614 0.0844  2   MET   B CA  
3834 C C   A MET   B 2   ? 0.2394 0.3206 0.3367 -0.0879 -0.0981 0.1491  2   MET   B C   
3835 C C   B MET   B 2   ? 0.2973 0.3377 0.3231 -0.0531 -0.0545 0.1004  2   MET   B C   
3836 O O   A MET   B 2   ? 0.2243 0.3271 0.3315 -0.0854 -0.1103 0.1560  2   MET   B O   
3837 O O   B MET   B 2   ? 0.3000 0.3451 0.3315 -0.0495 -0.0473 0.1057  2   MET   B O   
3838 C CB  A MET   B 2   ? 0.3123 0.3758 0.4570 -0.0789 -0.0676 0.1054  2   MET   B CB  
3839 C CB  B MET   B 2   ? 0.3383 0.3807 0.4085 -0.0498 -0.0616 0.0792  2   MET   B CB  
3840 C CG  A MET   B 2   ? 0.3409 0.4023 0.5323 -0.0580 -0.0497 0.0911  2   MET   B CG  
3841 C CG  B MET   B 2   ? 0.3526 0.3998 0.4591 -0.0393 -0.0603 0.0791  2   MET   B CG  
3842 S SD  A MET   B 2   ? 0.3681 0.4276 0.6008 -0.0394 -0.0339 0.0766  2   MET   B SD  
3843 S SD  B MET   B 2   ? 0.3664 0.4178 0.5043 -0.0298 -0.0587 0.0769  2   MET   B SD  
3844 C CE  A MET   B 2   ? 0.3708 0.4311 0.6009 -0.0375 -0.0270 0.0774  2   MET   B CE  
3845 C CE  B MET   B 2   ? 0.3665 0.4197 0.5074 -0.0304 -0.0556 0.0756  2   MET   B CE  
3864 N N   A VAL   B 3   ? 0.2204 0.2821 0.3180 -0.0896 -0.0859 0.1554  3   VAL   B N   
3865 N N   B VAL   B 3   ? 0.2711 0.3080 0.2924 -0.0513 -0.0513 0.1039  3   VAL   B N   
3866 C CA  A VAL   B 3   ? 0.2167 0.2539 0.3053 -0.0762 -0.0776 0.1343  3   VAL   B CA  
3867 C CA  B VAL   B 3   ? 0.2503 0.2796 0.2707 -0.0448 -0.0496 0.0946  3   VAL   B CA  
3868 C C   A VAL   B 3   ? 0.2005 0.2368 0.2608 -0.0644 -0.0715 0.1151  3   VAL   B C   
3869 C C   B VAL   B 3   ? 0.2215 0.2570 0.2358 -0.0424 -0.0515 0.0894  3   VAL   B C   
3870 O O   A VAL   B 3   ? 0.1958 0.2349 0.2733 -0.0635 -0.0725 0.1200  3   VAL   B O   
3871 O O   B VAL   B 3   ? 0.2184 0.2621 0.2280 -0.0305 -0.0502 0.0857  3   VAL   B O   
3872 C CB  A VAL   B 3   ? 0.2337 0.2527 0.3480 -0.0731 -0.0751 0.1147  3   VAL   B CB  
3873 C CB  B VAL   B 3   ? 0.2592 0.2763 0.2877 -0.0416 -0.0465 0.0892  3   VAL   B CB  
3874 C CG1 A VAL   B 3   ? 0.2400 0.2482 0.3627 -0.0715 -0.0749 0.1114  3   VAL   B CG1 
3875 C CG1 B VAL   B 3   ? 0.2624 0.2744 0.2960 -0.0423 -0.0442 0.0886  3   VAL   B CG1 
3876 C CG2 A VAL   B 3   ? 0.2403 0.2572 0.3625 -0.0706 -0.0692 0.1144  3   VAL   B CG2 
3877 C CG2 B VAL   B 3   ? 0.2629 0.2753 0.2906 -0.0399 -0.0458 0.0904  3   VAL   B CG2 
3896 N N   . ASN   B 4   ? 0.1988 0.2282 0.2168 -0.0513 -0.0614 0.0911  4   ASN   B N   
3897 C CA  . ASN   B 4   ? 0.1978 0.2210 0.1929 -0.0545 -0.0452 0.0464  4   ASN   B CA  
3898 C C   . ASN   B 4   ? 0.2119 0.2282 0.1866 -0.0565 -0.0323 0.0289  4   ASN   B C   
3899 O O   . ASN   B 4   ? 0.2133 0.2325 0.2099 -0.0544 -0.0270 0.0155  4   ASN   B O   
3900 C CB  . ASN   B 4   ? 0.1936 0.2115 0.1913 -0.0467 -0.0547 0.0410  4   ASN   B CB  
3901 C CG  . ASN   B 4   ? 0.1909 0.1900 0.1718 -0.0471 -0.0506 0.0326  4   ASN   B CG  
3902 O OD1 . ASN   B 4   ? 0.1899 0.1744 0.1747 -0.0427 -0.0498 0.0254  4   ASN   B OD1 
3903 N ND2 . ASN   B 4   ? 0.2115 0.1954 0.1732 -0.0299 -0.0304 0.0365  4   ASN   B ND2 
3911 N N   . SER   B 5   ? 0.2300 0.2437 0.2068 -0.0559 -0.0025 0.0296  5   SER   B N   
3912 C CA  . SER   B 5   ? 0.2597 0.2770 0.2453 -0.0410 0.0186  0.0348  5   SER   B CA  
3913 C C   . SER   B 5   ? 0.2745 0.2779 0.2784 -0.0526 0.0459  0.0363  5   SER   B C   
3914 O O   . SER   B 5   ? 0.2868 0.2771 0.3367 -0.0457 0.0672  0.0373  5   SER   B O   
3915 C CB  . SER   B 5   ? 0.2707 0.3040 0.2805 -0.0352 0.0211  0.0411  5   SER   B CB  
3916 O OG  . SER   B 5   ? 0.2984 0.3332 0.3340 -0.0223 0.0279  0.0478  5   SER   B OG  
3922 N N   . PHE   B 6   ? 0.2878 0.2893 0.2460 -0.0579 0.0563  0.0307  6   PHE   B N   
3923 C CA  . PHE   B 6   ? 0.2961 0.2852 0.2101 -0.0768 0.0522  0.0134  6   PHE   B CA  
3924 C C   . PHE   B 6   ? 0.3539 0.3102 0.2475 -0.0780 0.0752  -0.0132 6   PHE   B C   
3925 O O   . PHE   B 6   ? 0.3684 0.3426 0.2813 -0.0674 0.0539  -0.0322 6   PHE   B O   
3926 C CB  . PHE   B 6   ? 0.2575 0.2645 0.1825 -0.0728 0.0231  0.0141  6   PHE   B CB  
3927 C CG  . PHE   B 6   ? 0.2199 0.2351 0.1850 -0.0676 0.0092  0.0152  6   PHE   B CG  
3928 C CD1 . PHE   B 6   ? 0.2176 0.2115 0.1698 -0.0602 -0.0026 0.0161  6   PHE   B CD1 
3929 C CD2 . PHE   B 6   ? 0.1955 0.2344 0.1929 -0.0531 0.0021  0.0394  6   PHE   B CD2 
3930 C CE1 . PHE   B 6   ? 0.2088 0.2013 0.1788 -0.0415 -0.0111 0.0068  6   PHE   B CE1 
3931 C CE2 . PHE   B 6   ? 0.1905 0.2214 0.2112 -0.0411 0.0024  0.0394  6   PHE   B CE2 
3932 C CZ  . PHE   B 6   ? 0.1978 0.2046 0.1966 -0.0387 -0.0097 0.0094  6   PHE   B CZ  
3942 N N   A SER   B 7   ? 0.3776 0.2951 0.2450 -0.0920 0.1009  -0.0256 7   SER   B N   
3943 N N   B SER   B 7   ? 0.3715 0.3021 0.2548 -0.0857 0.0918  -0.0200 7   SER   B N   
3944 C CA  A SER   B 7   ? 0.4005 0.2990 0.2779 -0.0911 0.1151  -0.0330 7   SER   B CA  
3945 C CA  B SER   B 7   ? 0.3876 0.3040 0.2822 -0.0837 0.1012  -0.0225 7   SER   B CA  
3946 C C   A SER   B 7   ? 0.3969 0.2886 0.2711 -0.0961 0.1227  -0.0385 7   SER   B C   
3947 C C   B SER   B 7   ? 0.3860 0.2940 0.2770 -0.0865 0.1049  -0.0287 7   SER   B C   
3948 O O   A SER   B 7   ? 0.4013 0.2914 0.2879 -0.0992 0.1222  -0.0340 7   SER   B O   
3949 O O   B SER   B 7   ? 0.3898 0.2965 0.2877 -0.0879 0.1045  -0.0244 7   SER   B O   
3950 C CB  A SER   B 7   ? 0.4192 0.3099 0.3268 -0.0863 0.1225  -0.0350 7   SER   B CB  
3951 C CB  B SER   B 7   ? 0.4002 0.3133 0.3194 -0.0791 0.1062  -0.0211 7   SER   B CB  
3952 O OG  A SER   B 7   ? 0.4326 0.3217 0.3729 -0.0829 0.1217  -0.0325 7   SER   B OG  
3953 O OG  B SER   B 7   ? 0.4090 0.3222 0.3523 -0.0755 0.1047  -0.0200 7   SER   B OG  
3964 N N   A GLY   B 8   ? 0.3917 0.2762 0.2699 -0.0867 0.1225  -0.0519 8   GLY   B N   
3965 N N   B GLY   B 8   ? 0.3818 0.2816 0.2742 -0.0807 0.1052  -0.0410 8   GLY   B N   
3966 C CA  A GLY   B 8   ? 0.3797 0.2642 0.2750 -0.0832 0.1217  -0.0553 8   GLY   B CA  
3967 C CA  B GLY   B 8   ? 0.3726 0.2684 0.2720 -0.0787 0.1061  -0.0480 8   GLY   B CA  
3968 C C   A GLY   B 8   ? 0.3646 0.2476 0.2683 -0.0813 0.1219  -0.0506 8   GLY   B C   
3969 C C   B GLY   B 8   ? 0.3608 0.2518 0.2599 -0.0774 0.1072  -0.0519 8   GLY   B C   
3970 O O   A GLY   B 8   ? 0.3686 0.2516 0.2977 -0.0775 0.1283  -0.0461 8   GLY   B O   
3971 O O   B GLY   B 8   ? 0.3637 0.2572 0.2696 -0.0728 0.1066  -0.0548 8   GLY   B O   
3978 N N   . TYR   B 9   ? 0.3489 0.2361 0.2435 -0.0716 0.1032  -0.0523 9   TYR   B N   
3979 C CA  . TYR   B 9   ? 0.3194 0.2028 0.2119 -0.0489 0.0769  -0.0408 9   TYR   B CA  
3980 C C   . TYR   B 9   ? 0.3092 0.2054 0.2047 -0.0401 0.0390  -0.0293 9   TYR   B C   
3981 O O   . TYR   B 9   ? 0.3229 0.2332 0.2387 -0.0453 0.0344  -0.0132 9   TYR   B O   
3982 C CB  . TYR   B 9   ? 0.3114 0.1746 0.2231 -0.0382 0.0748  -0.0345 9   TYR   B CB  
3983 C CG  . TYR   B 9   ? 0.3023 0.1614 0.2287 -0.0487 0.0653  -0.0359 9   TYR   B CG  
3984 C CD1 . TYR   B 9   ? 0.3040 0.1630 0.2524 -0.0632 0.0701  -0.0272 9   TYR   B CD1 
3985 C CD2 . TYR   B 9   ? 0.2853 0.1585 0.2152 -0.0423 0.0565  -0.0472 9   TYR   B CD2 
3986 C CE1 . TYR   B 9   ? 0.2951 0.1753 0.2574 -0.0696 0.0711  -0.0378 9   TYR   B CE1 
3987 C CE2 . TYR   B 9   ? 0.2828 0.1641 0.2340 -0.0436 0.0561  -0.0382 9   TYR   B CE2 
3988 C CZ  . TYR   B 9   ? 0.2861 0.1776 0.2547 -0.0557 0.0584  -0.0555 9   TYR   B CZ  
3989 O OH  . TYR   B 9   ? 0.2766 0.1881 0.2747 -0.0693 0.0568  -0.0639 9   TYR   B OH  
4000 N N   . LEU   B 10  ? 0.2815 0.1815 0.1849 -0.0366 0.0164  -0.0270 10  LEU   B N   
4001 C CA  . LEU   B 10  ? 0.2712 0.1805 0.1927 -0.0519 -0.0117 -0.0281 10  LEU   B CA  
4002 C C   . LEU   B 10  ? 0.2513 0.1760 0.1850 -0.0555 -0.0314 -0.0245 10  LEU   B C   
4003 O O   . LEU   B 10  ? 0.2446 0.1778 0.1878 -0.0380 -0.0216 -0.0210 10  LEU   B O   
4004 C CB  . LEU   B 10  ? 0.2849 0.1827 0.2167 -0.0547 -0.0262 -0.0156 10  LEU   B CB  
4005 C CG  . LEU   B 10  ? 0.2986 0.1894 0.2423 -0.0478 -0.0531 -0.0013 10  LEU   B CG  
4006 C CD1 . LEU   B 10  ? 0.3076 0.1984 0.2737 -0.0490 -0.0509 -0.0007 10  LEU   B CD1 
4007 C CD2 . LEU   B 10  ? 0.3052 0.1948 0.2689 -0.0464 -0.0479 0.0155  10  LEU   B CD2 
4019 N N   . LYS   B 11  ? 0.2634 0.2013 0.1932 -0.0463 -0.0305 -0.0231 11  LYS   B N   
4020 C CA  . LYS   B 11  ? 0.2794 0.2344 0.2085 -0.0271 -0.0396 -0.0272 11  LYS   B CA  
4021 C C   . LYS   B 11  ? 0.2643 0.2157 0.2229 -0.0493 -0.0362 -0.0363 11  LYS   B C   
4022 O O   . LYS   B 11  ? 0.2776 0.2399 0.2597 -0.0637 -0.0395 -0.0682 11  LYS   B O   
4023 C CB  . LYS   B 11  ? 0.3109 0.2891 0.2586 -0.0033 -0.0413 -0.0194 11  LYS   B CB  
4024 C CG  . LYS   B 11  ? 0.3416 0.3269 0.3189 0.0146  -0.0386 -0.0167 11  LYS   B CG  
4025 C CD  . LYS   B 11  ? 0.3640 0.3526 0.3748 0.0223  -0.0344 -0.0208 11  LYS   B CD  
4026 C CE  . LYS   B 11  ? 0.3790 0.3708 0.4236 0.0245  -0.0280 -0.0201 11  LYS   B CE  
4027 N NZ  . LYS   B 11  ? 0.3881 0.3821 0.4514 0.0239  -0.0232 -0.0171 11  LYS   B NZ  
4041 N N   . LEU   B 12  ? 0.2343 0.1896 0.2246 -0.0483 -0.0326 -0.0358 12  LEU   B N   
4042 C CA  . LEU   B 12  ? 0.2226 0.1758 0.2378 -0.0461 -0.0256 -0.0304 12  LEU   B CA  
4043 C C   . LEU   B 12  ? 0.2132 0.1724 0.2567 -0.0471 -0.0390 -0.0251 12  LEU   B C   
4044 O O   . LEU   B 12  ? 0.2131 0.1773 0.2689 -0.0567 -0.0439 -0.0189 12  LEU   B O   
4045 C CB  . LEU   B 12  ? 0.2260 0.1555 0.2289 -0.0355 -0.0154 -0.0361 12  LEU   B CB  
4046 C CG  . LEU   B 12  ? 0.2271 0.1537 0.2369 -0.0371 -0.0133 -0.0257 12  LEU   B CG  
4047 C CD1 . LEU   B 12  ? 0.2361 0.1569 0.2340 -0.0231 -0.0169 -0.0201 12  LEU   B CD1 
4048 C CD2 . LEU   B 12  ? 0.2354 0.1652 0.2562 -0.0412 -0.0142 -0.0306 12  LEU   B CD2 
4060 N N   . THR   B 13  ? 0.2062 0.1762 0.2608 -0.0444 -0.0471 -0.0261 13  THR   B N   
4061 C CA  . THR   B 13  ? 0.2083 0.1830 0.2474 -0.0511 -0.0629 -0.0232 13  THR   B CA  
4062 C C   . THR   B 13  ? 0.2430 0.1959 0.2689 -0.0553 -0.0732 -0.0229 13  THR   B C   
4063 O O   . THR   B 13  ? 0.2602 0.1947 0.2948 -0.0530 -0.0440 -0.0257 13  THR   B O   
4064 C CB  . THR   B 13  ? 0.1958 0.1934 0.2574 -0.0439 -0.0594 -0.0125 13  THR   B CB  
4065 O OG1 . THR   B 13  ? 0.1849 0.1842 0.2544 -0.0442 -0.0472 -0.0179 13  THR   B OG1 
4066 C CG2 . THR   B 13  ? 0.2070 0.1958 0.2664 -0.0410 -0.0480 -0.0137 13  THR   B CG2 
4074 N N   A ASP   B 14  ? 0.2538 0.2102 0.2786 -0.0585 -0.0954 -0.0162 14  ASP   B N   
4075 N N   B ASP   B 14  ? 0.2539 0.2098 0.2779 -0.0521 -0.0842 -0.0142 14  ASP   B N   
4076 C CA  A ASP   B 14  ? 0.2619 0.2300 0.3043 -0.0584 -0.0994 0.0073  14  ASP   B CA  
4077 C CA  B ASP   B 14  ? 0.2612 0.2260 0.2954 -0.0480 -0.0851 0.0048  14  ASP   B CA  
4078 C C   A ASP   B 14  ? 0.2516 0.2161 0.2750 -0.0595 -0.0836 0.0131  14  ASP   B C   
4079 C C   B ASP   B 14  ? 0.2487 0.2116 0.2722 -0.0493 -0.0794 0.0093  14  ASP   B C   
4080 O O   A ASP   B 14  ? 0.2730 0.2314 0.2827 -0.0630 -0.0823 0.0191  14  ASP   B O   
4081 O O   B ASP   B 14  ? 0.2644 0.2184 0.2822 -0.0468 -0.0774 0.0093  14  ASP   B O   
4082 C CB  A ASP   B 14  ? 0.2800 0.2588 0.3705 -0.0544 -0.1108 0.0124  14  ASP   B CB  
4083 C CB  B ASP   B 14  ? 0.2804 0.2530 0.3434 -0.0405 -0.0858 0.0108  14  ASP   B CB  
4084 C CG  A ASP   B 14  ? 0.3036 0.2839 0.4357 -0.0504 -0.1069 0.0054  14  ASP   B CG  
4085 C CG  B ASP   B 14  ? 0.3023 0.2768 0.3888 -0.0337 -0.0777 0.0080  14  ASP   B CG  
4086 O OD1 A ASP   B 14  ? 0.3189 0.2949 0.4525 -0.0568 -0.1036 -0.0058 14  ASP   B OD1 
4087 O OD1 B ASP   B 14  ? 0.3113 0.2900 0.3992 -0.0328 -0.0698 0.0032  14  ASP   B OD1 
4088 O OD2 A ASP   B 14  ? 0.3090 0.2971 0.4694 -0.0487 -0.1004 0.0100  14  ASP   B OD2 
4089 O OD2 B ASP   B 14  ? 0.3105 0.2854 0.4117 -0.0354 -0.0759 0.0110  14  ASP   B OD2 
4098 N N   . ASN   B 15  ? 0.2212 0.1886 0.2463 -0.0447 -0.0834 0.0122  15  ASN   B N   
4099 C CA  . ASN   B 15  ? 0.1838 0.1613 0.2317 -0.0313 -0.0561 0.0016  15  ASN   B CA  
4100 C C   . ASN   B 15  ? 0.1679 0.1525 0.2205 -0.0171 -0.0438 -0.0041 15  ASN   B C   
4101 O O   . ASN   B 15  ? 0.1657 0.1485 0.2346 -0.0192 -0.0534 -0.0134 15  ASN   B O   
4102 C CB  . ASN   B 15  ? 0.1784 0.1594 0.2518 -0.0143 -0.0488 0.0010  15  ASN   B CB  
4103 C CG  . ASN   B 15  ? 0.1624 0.1537 0.2534 -0.0216 -0.0286 0.0055  15  ASN   B CG  
4104 O OD1 . ASN   B 15  ? 0.1689 0.1824 0.2699 -0.0402 -0.0343 0.0114  15  ASN   B OD1 
4105 N ND2 . ASN   B 15  ? 0.1696 0.1351 0.2509 -0.0170 -0.0005 -0.0147 15  ASN   B ND2 
4113 N N   . VAL   B 16  ? 0.1735 0.1422 0.2128 -0.0244 -0.0493 0.0025  16  VAL   B N   
4114 C CA  . VAL   B 16  ? 0.1749 0.1470 0.1954 -0.0233 -0.0357 -0.0131 16  VAL   B CA  
4115 C C   . VAL   B 16  ? 0.1741 0.1540 0.1960 -0.0294 -0.0381 -0.0114 16  VAL   B C   
4116 O O   . VAL   B 16  ? 0.1780 0.1670 0.2220 -0.0283 -0.0327 -0.0227 16  VAL   B O   
4117 C CB  . VAL   B 16  ? 0.1764 0.1479 0.2050 -0.0126 -0.0247 -0.0140 16  VAL   B CB  
4118 C CG1 . VAL   B 16  ? 0.1884 0.1497 0.2048 0.0006  -0.0212 -0.0089 16  VAL   B CG1 
4119 C CG2 . VAL   B 16  ? 0.1772 0.1544 0.2271 -0.0097 -0.0156 -0.0159 16  VAL   B CG2 
4129 N N   . TYR   B 17  ? 0.1777 0.1599 0.1907 -0.0296 -0.0316 -0.0176 17  TYR   B N   
4130 C CA  . TYR   B 17  ? 0.1839 0.1767 0.1836 -0.0304 -0.0239 -0.0033 17  TYR   B CA  
4131 C C   . TYR   B 17  ? 0.1745 0.1519 0.1857 -0.0355 -0.0205 -0.0104 17  TYR   B C   
4132 O O   . TYR   B 17  ? 0.1746 0.1528 0.1973 -0.0236 -0.0310 -0.0356 17  TYR   B O   
4133 C CB  . TYR   B 17  ? 0.2063 0.2118 0.1990 -0.0199 -0.0227 0.0309  17  TYR   B CB  
4134 C CG  . TYR   B 17  ? 0.2320 0.2537 0.2297 -0.0125 -0.0291 0.0350  17  TYR   B CG  
4135 C CD1 . TYR   B 17  ? 0.2522 0.2686 0.2373 -0.0061 -0.0427 0.0437  17  TYR   B CD1 
4136 C CD2 . TYR   B 17  ? 0.2533 0.2834 0.2483 -0.0030 -0.0350 0.0343  17  TYR   B CD2 
4137 C CE1 . TYR   B 17  ? 0.2712 0.2943 0.2511 0.0025  -0.0462 0.0386  17  TYR   B CE1 
4138 C CE2 . TYR   B 17  ? 0.2692 0.3018 0.2677 0.0089  -0.0482 0.0360  17  TYR   B CE2 
4139 C CZ  . TYR   B 17  ? 0.2799 0.3091 0.2630 0.0114  -0.0565 0.0416  17  TYR   B CZ  
4140 O OH  . TYR   B 17  ? 0.2979 0.3258 0.2815 0.0197  -0.0627 0.0408  17  TYR   B OH  
4150 N N   . ILE   B 18  ? 0.1857 0.1482 0.1697 -0.0280 -0.0069 -0.0178 18  ILE   B N   
4151 C CA  . ILE   B 18  ? 0.1870 0.1465 0.1669 -0.0249 -0.0100 -0.0109 18  ILE   B CA  
4152 C C   . ILE   B 18  ? 0.1970 0.1524 0.1631 -0.0373 -0.0073 -0.0253 18  ILE   B C   
4153 O O   . ILE   B 18  ? 0.2176 0.1658 0.1884 -0.0322 0.0030  -0.0323 18  ILE   B O   
4154 C CB  . ILE   B 18  ? 0.1878 0.1487 0.1897 -0.0304 -0.0123 -0.0149 18  ILE   B CB  
4155 C CG1 . ILE   B 18  ? 0.1849 0.1554 0.2068 -0.0327 -0.0058 -0.0032 18  ILE   B CG1 
4156 C CG2 . ILE   B 18  ? 0.1939 0.1612 0.1889 -0.0364 -0.0141 -0.0131 18  ILE   B CG2 
4157 C CD1 . ILE   B 18  ? 0.1936 0.1837 0.2228 -0.0322 -0.0222 0.0161  18  ILE   B CD1 
4169 N N   . LYS   B 19  ? 0.1953 0.1509 0.1911 -0.0195 0.0255  -0.0254 19  LYS   B N   
4170 C CA  . LYS   B 19  ? 0.2073 0.1542 0.2037 -0.0255 0.0238  -0.0202 19  LYS   B CA  
4171 C C   . LYS   B 19  ? 0.1915 0.1543 0.2104 -0.0217 0.0256  -0.0304 19  LYS   B C   
4172 O O   . LYS   B 19  ? 0.1847 0.1576 0.1920 -0.0094 0.0119  -0.0284 19  LYS   B O   
4173 C CB  . LYS   B 19  ? 0.2278 0.1772 0.2142 -0.0190 0.0280  -0.0158 19  LYS   B CB  
4174 C CG  . LYS   B 19  ? 0.2498 0.1956 0.2236 -0.0253 0.0340  -0.0236 19  LYS   B CG  
4175 C CD  . LYS   B 19  ? 0.2756 0.2247 0.2266 -0.0338 0.0430  -0.0125 19  LYS   B CD  
4176 C CE  . LYS   B 19  ? 0.2942 0.2479 0.2508 -0.0359 0.0403  -0.0129 19  LYS   B CE  
4177 N NZ  . LYS   B 19  ? 0.3076 0.2624 0.2627 -0.0388 0.0428  -0.0085 19  LYS   B NZ  
4191 N N   . ASN   B 20  ? 0.1889 0.1618 0.2305 -0.0187 0.0251  -0.0420 20  ASN   B N   
4192 C CA  . ASN   B 20  ? 0.1895 0.1776 0.2516 -0.0081 0.0304  -0.0483 20  ASN   B CA  
4193 C C   . ASN   B 20  ? 0.1820 0.1942 0.2586 -0.0170 0.0350  -0.0576 20  ASN   B C   
4194 O O   . ASN   B 20  ? 0.1989 0.2247 0.2793 -0.0276 0.0288  -0.0558 20  ASN   B O   
4195 C CB  . ASN   B 20  ? 0.2157 0.1811 0.2762 0.0047  0.0181  -0.0535 20  ASN   B CB  
4196 C CG  . ASN   B 20  ? 0.2442 0.1842 0.2884 0.0280  0.0265  -0.0685 20  ASN   B CG  
4197 O OD1 . ASN   B 20  ? 0.2741 0.2125 0.3226 0.0503  0.0271  -0.0714 20  ASN   B OD1 
4198 N ND2 . ASN   B 20  ? 0.2382 0.1840 0.2714 0.0261  0.0185  -0.0658 20  ASN   B ND2 
4205 N N   . ALA   B 21  ? 0.1844 0.1804 0.2612 -0.0211 0.0374  -0.0511 21  ALA   B N   
4206 C CA  . ALA   B 21  ? 0.1936 0.1888 0.2843 -0.0298 0.0347  -0.0409 21  ALA   B CA  
4207 C C   . ALA   B 21  ? 0.1940 0.1626 0.2712 -0.0192 0.0354  -0.0304 21  ALA   B C   
4208 O O   . ALA   B 21  ? 0.1969 0.1554 0.2683 -0.0265 0.0296  -0.0239 21  ALA   B O   
4209 C CB  . ALA   B 21  ? 0.2134 0.2149 0.2953 -0.0419 0.0243  -0.0302 21  ALA   B CB  
4215 N N   . ASP   B 22  ? 0.1878 0.1567 0.2641 -0.0234 0.0287  -0.0220 22  ASP   B N   
4216 C CA  . ASP   B 22  ? 0.1857 0.1525 0.2462 -0.0124 0.0217  -0.0171 22  ASP   B CA  
4217 C C   . ASP   B 22  ? 0.1781 0.1519 0.1968 -0.0124 0.0126  -0.0050 22  ASP   B C   
4218 O O   . ASP   B 22  ? 0.1788 0.1554 0.2094 -0.0075 0.0145  -0.0025 22  ASP   B O   
4219 C CB  . ASP   B 22  ? 0.1902 0.1547 0.2788 -0.0101 0.0283  -0.0032 22  ASP   B CB  
4220 C CG  . ASP   B 22  ? 0.1895 0.1759 0.3153 -0.0070 0.0019  -0.0067 22  ASP   B CG  
4221 O OD1 . ASP   B 22  ? 0.2088 0.1684 0.3070 -0.0022 -0.0284 -0.0086 22  ASP   B OD1 
4222 O OD2 . ASP   B 22  ? 0.1949 0.2073 0.3736 0.0022  -0.0161 -0.0292 22  ASP   B OD2 
4227 N N   . ILE   B 23  ? 0.1787 0.1460 0.1886 -0.0138 0.0092  0.0187  23  ILE   B N   
4228 C CA  . ILE   B 23  ? 0.1693 0.1459 0.1805 -0.0106 -0.0025 0.0082  23  ILE   B CA  
4229 C C   . ILE   B 23  ? 0.1605 0.1457 0.1678 -0.0063 -0.0078 0.0033  23  ILE   B C   
4230 O O   . ILE   B 23  ? 0.1613 0.1453 0.1702 -0.0063 -0.0075 0.0037  23  ILE   B O   
4231 C CB  . ILE   B 23  ? 0.1663 0.1483 0.1985 -0.0177 -0.0051 0.0180  23  ILE   B CB  
4232 C CG1 . ILE   B 23  ? 0.1702 0.1523 0.2152 -0.0175 -0.0001 0.0271  23  ILE   B CG1 
4233 C CG2 . ILE   B 23  ? 0.1823 0.1712 0.2124 -0.0200 -0.0027 0.0118  23  ILE   B CG2 
4234 C CD1 . ILE   B 23  ? 0.1771 0.1630 0.2324 -0.0136 0.0058  0.0176  23  ILE   B CD1 
4246 N N   . VAL   B 24  ? 0.1667 0.1483 0.1826 -0.0077 -0.0004 0.0009  24  VAL   B N   
4247 C CA  . VAL   B 24  ? 0.1555 0.1504 0.2013 -0.0045 -0.0136 0.0033  24  VAL   B CA  
4248 C C   . VAL   B 24  ? 0.1552 0.1485 0.2179 -0.0079 -0.0131 0.0023  24  VAL   B C   
4249 O O   . VAL   B 24  ? 0.1565 0.1538 0.2259 -0.0102 -0.0038 0.0081  24  VAL   B O   
4250 C CB  . VAL   B 24  ? 0.1675 0.1708 0.2063 0.0004  -0.0187 0.0013  24  VAL   B CB  
4251 C CG1 . VAL   B 24  ? 0.1681 0.1717 0.2226 -0.0121 -0.0179 0.0013  24  VAL   B CG1 
4252 C CG2 . VAL   B 24  ? 0.1742 0.1979 0.2171 0.0048  -0.0175 -0.0077 24  VAL   B CG2 
4262 N N   . GLU   B 25  ? 0.1807 0.1623 0.2301 -0.0098 -0.0036 0.0094  25  GLU   B N   
4263 C CA  . GLU   B 25  ? 0.1933 0.1849 0.2408 -0.0015 0.0067  0.0063  25  GLU   B CA  
4264 C C   . GLU   B 25  ? 0.1927 0.1739 0.2136 -0.0071 0.0099  0.0130  25  GLU   B C   
4265 O O   . GLU   B 25  ? 0.1945 0.1882 0.2246 -0.0086 0.0179  0.0163  25  GLU   B O   
4266 C CB  . GLU   B 25  ? 0.2267 0.2359 0.2956 0.0105  0.0161  0.0055  25  GLU   B CB  
4267 C CG  . GLU   B 25  ? 0.2669 0.2975 0.3910 0.0134  0.0177  -0.0034 25  GLU   B CG  
4268 C CD  . GLU   B 25  ? 0.3231 0.3572 0.4757 0.0091  0.0203  -0.0109 25  GLU   B CD  
4269 O OE1 . GLU   B 25  ? 0.3258 0.3776 0.5073 0.0145  0.0262  -0.0107 25  GLU   B OE1 
4270 O OE2 . GLU   B 25  ? 0.3239 0.3751 0.5109 0.0083  0.0171  -0.0176 25  GLU   B OE2 
4277 N N   . GLU   B 26  ? 0.1852 0.1691 0.1900 -0.0221 0.0118  0.0124  26  GLU   B N   
4278 C CA  . GLU   B 26  ? 0.1870 0.1857 0.2034 -0.0313 -0.0109 0.0095  26  GLU   B CA  
4279 C C   . GLU   B 26  ? 0.1701 0.1824 0.1927 -0.0252 -0.0014 0.0186  26  GLU   B C   
4280 O O   . GLU   B 26  ? 0.1898 0.2094 0.2000 -0.0189 -0.0031 0.0299  26  GLU   B O   
4281 C CB  . GLU   B 26  ? 0.2156 0.2042 0.2159 -0.0407 -0.0077 0.0176  26  GLU   B CB  
4282 C CG  . GLU   B 26  ? 0.2567 0.2338 0.2534 -0.0490 -0.0014 0.0011  26  GLU   B CG  
4283 C CD  . GLU   B 26  ? 0.2835 0.2528 0.2739 -0.0691 0.0154  -0.0297 26  GLU   B CD  
4284 O OE1 . GLU   B 26  ? 0.3033 0.2270 0.2730 -0.0763 0.0550  -0.0235 26  GLU   B OE1 
4285 O OE2 . GLU   B 26  ? 0.2836 0.2995 0.3195 -0.0665 0.0145  -0.0213 26  GLU   B OE2 
4292 N N   . ALA   B 27  ? 0.1546 0.1708 0.1990 -0.0228 0.0020  0.0238  27  ALA   B N   
4293 C CA  . ALA   B 27  ? 0.1594 0.1609 0.2084 -0.0126 0.0010  0.0350  27  ALA   B CA  
4294 C C   . ALA   B 27  ? 0.1678 0.1749 0.2234 -0.0092 0.0100  0.0391  27  ALA   B C   
4295 O O   . ALA   B 27  ? 0.1749 0.1781 0.2404 0.0015  0.0102  0.0437  27  ALA   B O   
4296 C CB  . ALA   B 27  ? 0.1786 0.1439 0.2185 -0.0182 0.0001  0.0281  27  ALA   B CB  
4302 N N   . LYS   B 28  ? 0.1611 0.1956 0.2656 -0.0145 0.0194  0.0680  28  LYS   B N   
4303 C CA  . LYS   B 28  ? 0.1732 0.2307 0.3018 -0.0038 0.0506  0.0962  28  LYS   B CA  
4304 C C   . LYS   B 28  ? 0.1987 0.2484 0.2895 0.0035  0.0600  0.0888  28  LYS   B C   
4305 O O   . LYS   B 28  ? 0.2289 0.2537 0.3014 0.0028  0.0578  0.0862  28  LYS   B O   
4306 C CB  . LYS   B 28  ? 0.1929 0.2685 0.3605 0.0132  0.0704  0.1265  28  LYS   B CB  
4307 C CG  . LYS   B 28  ? 0.2241 0.3233 0.4132 0.0308  0.0774  0.1413  28  LYS   B CG  
4308 C CD  . LYS   B 28  ? 0.2660 0.3830 0.4693 0.0382  0.0982  0.1436  28  LYS   B CD  
4309 C CE  . LYS   B 28  ? 0.3011 0.4272 0.5175 0.0483  0.0994  0.1463  28  LYS   B CE  
4310 N NZ  . LYS   B 28  ? 0.3315 0.4549 0.5398 0.0608  0.0998  0.1533  28  LYS   B NZ  
4324 N N   . LYS   B 29  ? 0.2160 0.2732 0.2902 0.0220  0.0621  0.0780  29  LYS   B N   
4325 C CA  . LYS   B 29  ? 0.2586 0.3036 0.3158 0.0221  0.0535  0.0770  29  LYS   B CA  
4326 C C   . LYS   B 29  ? 0.2477 0.3044 0.2831 0.0208  0.0434  0.0860  29  LYS   B C   
4327 O O   . LYS   B 29  ? 0.2637 0.3262 0.2847 0.0300  0.0435  0.0807  29  LYS   B O   
4328 C CB  . LYS   B 29  ? 0.3174 0.3417 0.3976 0.0202  0.0472  0.0584  29  LYS   B CB  
4329 C CG  . LYS   B 29  ? 0.3701 0.3749 0.4757 0.0153  0.0447  0.0560  29  LYS   B CG  
4330 C CD  . LYS   B 29  ? 0.4090 0.4011 0.5420 0.0094  0.0476  0.0485  29  LYS   B CD  
4331 C CE  . LYS   B 29  ? 0.4365 0.4134 0.5871 0.0044  0.0542  0.0449  29  LYS   B CE  
4332 N NZ  . LYS   B 29  ? 0.4464 0.4207 0.6135 0.0022  0.0563  0.0435  29  LYS   B NZ  
4346 N N   . VAL   B 30  ? 0.2197 0.2850 0.2730 0.0042  0.0358  0.0853  30  VAL   B N   
4347 C CA  . VAL   B 30  ? 0.2080 0.2731 0.3003 -0.0055 0.0079  0.0844  30  VAL   B CA  
4348 C C   . VAL   B 30  ? 0.1856 0.2684 0.2855 -0.0030 0.0224  0.1011  30  VAL   B C   
4349 O O   . VAL   B 30  ? 0.2007 0.2865 0.2902 0.0065  0.0270  0.1188  30  VAL   B O   
4350 C CB  . VAL   B 30  ? 0.2157 0.2636 0.3393 -0.0209 -0.0234 0.0787  30  VAL   B CB  
4351 C CG1 . VAL   B 30  ? 0.2213 0.2659 0.3402 -0.0216 -0.0174 0.0772  30  VAL   B CG1 
4352 C CG2 . VAL   B 30  ? 0.2266 0.2629 0.3507 -0.0255 -0.0421 0.0639  30  VAL   B CG2 
4362 N N   . LYS   B 31  ? 0.1716 0.2345 0.3147 -0.0122 0.0218  0.1027  31  LYS   B N   
4363 C CA  . LYS   B 31  ? 0.1624 0.2295 0.3434 -0.0326 0.0072  0.1063  31  LYS   B CA  
4364 C C   . LYS   B 31  ? 0.1619 0.1944 0.2965 -0.0337 -0.0196 0.0882  31  LYS   B C   
4365 O O   . LYS   B 31  ? 0.1698 0.2170 0.3171 -0.0243 -0.0068 0.1155  31  LYS   B O   
4366 C CB  . LYS   B 31  ? 0.1785 0.2772 0.4034 -0.0263 0.0284  0.1264  31  LYS   B CB  
4367 C CG  . LYS   B 31  ? 0.2118 0.3253 0.4504 -0.0172 0.0409  0.1281  31  LYS   B CG  
4368 C CD  . LYS   B 31  ? 0.2356 0.3644 0.4907 -0.0067 0.0396  0.1210  31  LYS   B CD  
4369 C CE  . LYS   B 31  ? 0.2571 0.3942 0.5238 -0.0008 0.0294  0.1109  31  LYS   B CE  
4370 N NZ  . LYS   B 31  ? 0.2721 0.4050 0.5370 0.0059  0.0142  0.0992  31  LYS   B NZ  
4384 N N   . PRO   B 32  ? 0.1690 0.1626 0.2256 -0.0315 -0.0433 0.0504  32  PRO   B N   
4385 C CA  . PRO   B 32  ? 0.1769 0.1580 0.1913 -0.0299 -0.0297 0.0332  32  PRO   B CA  
4386 C C   . PRO   B 32  ? 0.1876 0.1445 0.1950 -0.0307 -0.0454 0.0349  32  PRO   B C   
4387 O O   . PRO   B 32  ? 0.2004 0.1530 0.2259 -0.0387 -0.0718 0.0306  32  PRO   B O   
4388 C CB  . PRO   B 32  ? 0.1890 0.1496 0.1915 -0.0310 -0.0262 0.0210  32  PRO   B CB  
4389 C CG  . PRO   B 32  ? 0.2080 0.1433 0.2023 -0.0254 -0.0473 0.0334  32  PRO   B CG  
4390 C CD  . PRO   B 32  ? 0.1947 0.1499 0.2197 -0.0201 -0.0616 0.0346  32  PRO   B CD  
4398 N N   . THR   B 33  ? 0.1911 0.1384 0.1833 -0.0280 -0.0435 0.0278  33  THR   B N   
4399 C CA  . THR   B 33  ? 0.1966 0.1410 0.1721 -0.0311 -0.0441 0.0261  33  THR   B CA  
4400 C C   . THR   B 33  ? 0.1964 0.1332 0.1701 -0.0277 -0.0448 0.0221  33  THR   B C   
4401 O O   . THR   B 33  ? 0.2196 0.1358 0.1857 -0.0386 -0.0554 0.0197  33  THR   B O   
4402 C CB  . THR   B 33  ? 0.2065 0.1534 0.1779 -0.0163 -0.0514 0.0273  33  THR   B CB  
4403 O OG1 . THR   B 33  ? 0.1948 0.1636 0.1812 -0.0207 -0.0450 0.0400  33  THR   B OG1 
4404 C CG2 . THR   B 33  ? 0.2288 0.1577 0.1958 -0.0110 -0.0470 0.0213  33  THR   B CG2 
4412 N N   . VAL   B 34  ? 0.1812 0.1347 0.1498 -0.0287 -0.0362 0.0163  34  VAL   B N   
4413 C CA  . VAL   B 34  ? 0.1636 0.1297 0.1508 -0.0296 -0.0396 0.0093  34  VAL   B CA  
4414 C C   . VAL   B 34  ? 0.1548 0.1302 0.1355 -0.0298 -0.0288 0.0000  34  VAL   B C   
4415 O O   . VAL   B 34  ? 0.1756 0.1291 0.1457 -0.0234 -0.0400 0.0100  34  VAL   B O   
4416 C CB  . VAL   B 34  ? 0.1729 0.1423 0.1800 -0.0121 -0.0360 0.0015  34  VAL   B CB  
4417 C CG1 . VAL   B 34  ? 0.1737 0.1597 0.1864 -0.0112 -0.0206 -0.0113 34  VAL   B CG1 
4418 C CG2 . VAL   B 34  ? 0.1829 0.1520 0.2024 -0.0043 -0.0259 0.0033  34  VAL   B CG2 
4428 N N   . VAL   B 35  ? 0.1489 0.1288 0.1304 -0.0270 -0.0172 0.0047  35  VAL   B N   
4429 C CA  . VAL   B 35  ? 0.1492 0.1220 0.1350 -0.0206 -0.0102 0.0080  35  VAL   B CA  
4430 C C   . VAL   B 35  ? 0.1388 0.1217 0.1329 -0.0182 -0.0161 0.0108  35  VAL   B C   
4431 O O   . VAL   B 35  ? 0.1412 0.1287 0.1332 -0.0241 -0.0080 -0.0050 35  VAL   B O   
4432 C CB  . VAL   B 35  ? 0.1422 0.1436 0.1461 -0.0197 -0.0043 0.0048  35  VAL   B CB  
4433 C CG1 . VAL   B 35  ? 0.1375 0.1555 0.1812 -0.0139 -0.0070 -0.0026 35  VAL   B CG1 
4434 C CG2 . VAL   B 35  ? 0.1494 0.1464 0.1727 -0.0082 -0.0005 -0.0038 35  VAL   B CG2 
4444 N N   . VAL   B 36  ? 0.1350 0.1197 0.1335 -0.0118 -0.0159 0.0087  36  VAL   B N   
4445 C CA  . VAL   B 36  ? 0.1320 0.1174 0.1325 -0.0113 -0.0086 0.0067  36  VAL   B CA  
4446 C C   . VAL   B 36  ? 0.1296 0.1181 0.1332 -0.0129 -0.0097 0.0047  36  VAL   B C   
4447 O O   . VAL   B 36  ? 0.1389 0.1292 0.1462 -0.0087 -0.0044 -0.0080 36  VAL   B O   
4448 C CB  . VAL   B 36  ? 0.1347 0.1303 0.1357 -0.0160 -0.0100 0.0084  36  VAL   B CB  
4449 C CG1 . VAL   B 36  ? 0.1349 0.1446 0.1578 -0.0214 -0.0102 0.0073  36  VAL   B CG1 
4450 C CG2 . VAL   B 36  ? 0.1408 0.1345 0.1400 -0.0168 -0.0176 0.0121  36  VAL   B CG2 
4460 N N   . ASN   B 37  ? 0.1303 0.1209 0.1303 -0.0019 -0.0138 0.0053  37  ASN   B N   
4461 C CA  . ASN   B 37  ? 0.1310 0.1239 0.1513 -0.0012 -0.0211 0.0072  37  ASN   B CA  
4462 C C   . ASN   B 37  ? 0.1278 0.1299 0.1460 0.0013  -0.0133 -0.0024 37  ASN   B C   
4463 O O   . ASN   B 37  ? 0.1412 0.1351 0.1400 -0.0006 -0.0040 0.0042  37  ASN   B O   
4464 C CB  . ASN   B 37  ? 0.1320 0.1309 0.1412 -0.0013 -0.0240 0.0040  37  ASN   B CB  
4465 C CG  . ASN   B 37  ? 0.1344 0.1232 0.1546 -0.0061 -0.0170 0.0071  37  ASN   B CG  
4466 O OD1 . ASN   B 37  ? 0.1397 0.1311 0.1648 0.0086  -0.0135 0.0030  37  ASN   B OD1 
4467 N ND2 . ASN   B 37  ? 0.1430 0.1228 0.1558 0.0005  -0.0232 0.0100  37  ASN   B ND2 
4474 N N   . ALA   B 38  ? 0.1361 0.1205 0.1430 0.0047  -0.0020 0.0034  38  ALA   B N   
4475 C CA  . ALA   B 38  ? 0.1413 0.1257 0.1554 0.0005  0.0010  0.0047  38  ALA   B CA  
4476 C C   . ALA   B 38  ? 0.1432 0.1209 0.1523 -0.0017 -0.0018 0.0062  38  ALA   B C   
4477 O O   . ALA   B 38  ? 0.1538 0.1334 0.1639 0.0091  -0.0009 0.0097  38  ALA   B O   
4478 C CB  . ALA   B 38  ? 0.1653 0.1373 0.1610 -0.0091 0.0096  0.0023  38  ALA   B CB  
4484 N N   . ALA   B 39  ? 0.1451 0.1272 0.1275 0.0069  -0.0059 0.0012  39  ALA   B N   
4485 C CA  . ALA   B 39  ? 0.1518 0.1373 0.1303 0.0080  -0.0020 0.0045  39  ALA   B CA  
4486 C C   . ALA   B 39  ? 0.1589 0.1395 0.1211 0.0057  -0.0076 0.0005  39  ALA   B C   
4487 O O   . ALA   B 39  ? 0.1599 0.1436 0.1454 0.0018  -0.0020 0.0092  39  ALA   B O   
4488 C CB  . ALA   B 39  ? 0.1573 0.1384 0.1461 -0.0059 -0.0069 0.0031  39  ALA   B CB  
4494 N N   . ASN   B 40  ? 0.1644 0.1650 0.1289 -0.0081 -0.0035 -0.0056 40  ASN   B N   
4495 C CA  . ASN   B 40  ? 0.1690 0.1682 0.1378 -0.0012 0.0002  -0.0035 40  ASN   B CA  
4496 C C   . ASN   B 40  ? 0.1643 0.1698 0.1273 -0.0007 -0.0122 -0.0052 40  ASN   B C   
4497 O O   . ASN   B 40  ? 0.1645 0.1609 0.1400 0.0058  -0.0173 -0.0062 40  ASN   B O   
4498 C CB  . ASN   B 40  ? 0.1810 0.1668 0.1724 0.0056  -0.0171 0.0098  40  ASN   B CB  
4499 C CG  . ASN   B 40  ? 0.1821 0.1680 0.2014 0.0036  -0.0290 0.0085  40  ASN   B CG  
4500 O OD1 . ASN   B 40  ? 0.1812 0.1666 0.2757 0.0013  -0.0331 0.0144  40  ASN   B OD1 
4501 N ND2 . ASN   B 40  ? 0.1880 0.1683 0.2036 0.0072  -0.0183 0.0105  40  ASN   B ND2 
4508 N N   . VAL   B 41  ? 0.1750 0.1713 0.1374 0.0123  0.0027  0.0010  41  VAL   B N   
4509 C CA  . VAL   B 41  ? 0.1854 0.1842 0.1506 0.0128  0.0005  -0.0077 41  VAL   B CA  
4510 C C   . VAL   B 41  ? 0.1848 0.1858 0.1452 0.0194  -0.0105 -0.0116 41  VAL   B C   
4511 O O   . VAL   B 41  ? 0.1776 0.1842 0.1642 0.0138  -0.0200 -0.0137 41  VAL   B O   
4512 C CB  . VAL   B 41  ? 0.1963 0.1992 0.1689 -0.0026 0.0116  -0.0224 41  VAL   B CB  
4513 C CG1 . VAL   B 41  ? 0.1969 0.2034 0.1870 -0.0090 0.0160  -0.0317 41  VAL   B CG1 
4514 C CG2 . VAL   B 41  ? 0.1967 0.2171 0.1841 -0.0084 0.0136  -0.0148 41  VAL   B CG2 
4524 N N   . TYR   B 42  ? 0.1918 0.1852 0.1455 0.0184  -0.0238 -0.0012 42  TYR   B N   
4525 C CA  . TYR   B 42  ? 0.1966 0.1940 0.1534 0.0179  -0.0330 -0.0120 42  TYR   B CA  
4526 C C   . TYR   B 42  ? 0.1795 0.1742 0.1646 0.0174  -0.0231 -0.0219 42  TYR   B C   
4527 O O   . TYR   B 42  ? 0.1794 0.1787 0.1999 0.0142  -0.0353 -0.0272 42  TYR   B O   
4528 C CB  . TYR   B 42  ? 0.2253 0.2261 0.1728 0.0070  -0.0415 -0.0094 42  TYR   B CB  
4529 C CG  . TYR   B 42  ? 0.2319 0.2490 0.1741 0.0017  -0.0356 0.0052  42  TYR   B CG  
4530 C CD1 . TYR   B 42  ? 0.2302 0.2470 0.1562 0.0007  -0.0197 0.0009  42  TYR   B CD1 
4531 C CD2 . TYR   B 42  ? 0.2491 0.2646 0.2136 0.0011  -0.0232 0.0138  42  TYR   B CD2 
4532 C CE1 . TYR   B 42  ? 0.2395 0.2568 0.1725 0.0051  -0.0130 -0.0016 42  TYR   B CE1 
4533 C CE2 . TYR   B 42  ? 0.2523 0.2658 0.2040 0.0032  -0.0008 0.0265  42  TYR   B CE2 
4534 C CZ  . TYR   B 42  ? 0.2619 0.2734 0.1996 0.0186  0.0070  0.0171  42  TYR   B CZ  
4535 O OH  . TYR   B 42  ? 0.2933 0.2936 0.2488 0.0337  0.0244  0.0311  42  TYR   B OH  
4545 N N   . LEU   B 43  ? 0.1687 0.1575 0.1514 0.0139  -0.0176 -0.0211 43  LEU   B N   
4546 C CA  . LEU   B 43  ? 0.1667 0.1540 0.1473 0.0086  -0.0168 -0.0052 43  LEU   B CA  
4547 C C   . LEU   B 43  ? 0.1733 0.1555 0.1514 0.0039  -0.0180 -0.0045 43  LEU   B C   
4548 O O   . LEU   B 43  ? 0.1699 0.1635 0.1788 0.0016  -0.0279 0.0019  43  LEU   B O   
4549 C CB  . LEU   B 43  ? 0.1630 0.1493 0.1693 0.0030  -0.0325 -0.0105 43  LEU   B CB  
4550 C CG  . LEU   B 43  ? 0.1677 0.1520 0.1754 0.0012  -0.0330 -0.0035 43  LEU   B CG  
4551 C CD1 . LEU   B 43  ? 0.1740 0.1535 0.2062 -0.0062 -0.0413 -0.0009 43  LEU   B CD1 
4552 C CD2 . LEU   B 43  ? 0.1661 0.1531 0.1780 -0.0075 -0.0338 -0.0055 43  LEU   B CD2 
4564 N N   . LYS   B 44  ? 0.1664 0.1519 0.1591 0.0073  -0.0084 -0.0082 44  LYS   B N   
4565 C CA  . LYS   B 44  ? 0.1814 0.1658 0.1648 0.0080  -0.0169 0.0091  44  LYS   B CA  
4566 C C   . LYS   B 44  ? 0.1653 0.1599 0.1599 0.0088  -0.0202 0.0009  44  LYS   B C   
4567 O O   . LYS   B 44  ? 0.1788 0.1585 0.1809 0.0048  -0.0061 -0.0030 44  LYS   B O   
4568 C CB  . LYS   B 44  ? 0.2036 0.1852 0.1825 0.0137  -0.0269 0.0039  44  LYS   B CB  
4569 C CG  . LYS   B 44  ? 0.2428 0.2136 0.2184 0.0074  -0.0461 0.0020  44  LYS   B CG  
4570 C CD  . LYS   B 44  ? 0.2814 0.2363 0.2659 -0.0060 -0.0596 0.0030  44  LYS   B CD  
4571 C CE  . LYS   B 44  ? 0.3107 0.2615 0.3108 -0.0116 -0.0630 0.0108  44  LYS   B CE  
4572 N NZ  . LYS   B 44  ? 0.3234 0.2735 0.3350 -0.0066 -0.0702 0.0248  44  LYS   B NZ  
4586 N N   . HIS   B 45  ? 0.1604 0.1620 0.1448 0.0076  -0.0192 0.0058  45  HIS   B N   
4587 C CA  . HIS   B 45  ? 0.1647 0.1576 0.1546 0.0087  -0.0114 0.0039  45  HIS   B CA  
4588 C C   . HIS   B 45  ? 0.1912 0.1795 0.1868 0.0187  -0.0266 -0.0026 45  HIS   B C   
4589 O O   . HIS   B 45  ? 0.2016 0.2083 0.2295 0.0472  0.0097  0.0052  45  HIS   B O   
4590 C CB  . HIS   B 45  ? 0.1551 0.1573 0.1584 0.0013  -0.0119 0.0003  45  HIS   B CB  
4591 C CG  . HIS   B 45  ? 0.1578 0.1548 0.1541 -0.0062 -0.0146 0.0008  45  HIS   B CG  
4592 N ND1 . HIS   B 45  ? 0.1642 0.1480 0.1687 -0.0003 -0.0224 -0.0091 45  HIS   B ND1 
4593 C CD2 . HIS   B 45  ? 0.1735 0.1563 0.1749 -0.0066 -0.0201 0.0043  45  HIS   B CD2 
4594 C CE1 . HIS   B 45  ? 0.1770 0.1414 0.1532 -0.0031 -0.0345 -0.0045 45  HIS   B CE1 
4595 N NE2 . HIS   B 45  ? 0.1801 0.1490 0.1641 -0.0012 -0.0255 0.0032  45  HIS   B NE2 
4603 N N   A GLY   B 46  ? 0.2048 0.1804 0.2205 0.0204  -0.0465 0.0080  46  GLY   B N   
4604 N N   B GLY   B 46  ? 0.2040 0.1847 0.2121 0.0206  -0.0407 0.0090  46  GLY   B N   
4605 C CA  A GLY   B 46  ? 0.2125 0.1866 0.2642 0.0171  -0.0518 0.0080  46  GLY   B CA  
4606 C CA  B GLY   B 46  ? 0.2122 0.1919 0.2436 0.0188  -0.0458 0.0139  46  GLY   B CA  
4607 C C   A GLY   B 46  ? 0.2142 0.2010 0.3133 0.0238  -0.0439 0.0006  46  GLY   B C   
4608 C C   B GLY   B 46  ? 0.2160 0.2035 0.2817 0.0232  -0.0401 0.0134  46  GLY   B C   
4609 O O   A GLY   B 46  ? 0.2243 0.2168 0.3914 0.0297  -0.0245 -0.0214 46  GLY   B O   
4610 O O   B GLY   B 46  ? 0.2266 0.2142 0.3151 0.0293  -0.0305 0.0211  46  GLY   B O   
4617 N N   . GLY   B 47  ? 0.2111 0.2095 0.2873 0.0111  -0.0285 -0.0000 47  GLY   B N   
4618 C CA  . GLY   B 47  ? 0.1968 0.1766 0.2349 0.0072  -0.0178 -0.0032 47  GLY   B CA  
4619 C C   . GLY   B 47  ? 0.1775 0.1582 0.2050 0.0052  -0.0055 0.0064  47  GLY   B C   
4620 O O   . GLY   B 47  ? 0.1831 0.1433 0.2047 -0.0003 -0.0106 0.0130  47  GLY   B O   
4625 N N   . GLY   B 48  ? 0.1575 0.1461 0.1878 0.0057  -0.0124 0.0167  48  GLY   B N   
4626 C CA  . GLY   B 48  ? 0.1641 0.1396 0.1853 -0.0012 -0.0063 0.0079  48  GLY   B CA  
4627 C C   . GLY   B 48  ? 0.1534 0.1402 0.1737 0.0037  0.0038  0.0039  48  GLY   B C   
4628 O O   . GLY   B 48  ? 0.1485 0.1391 0.2017 0.0063  -0.0133 0.0066  48  GLY   B O   
4632 N N   . VAL   B 49  ? 0.1527 0.1488 0.1629 0.0074  0.0057  0.0090  49  VAL   B N   
4633 C CA  . VAL   B 49  ? 0.1527 0.1528 0.1565 0.0099  -0.0157 -0.0004 49  VAL   B CA  
4634 C C   . VAL   B 49  ? 0.1442 0.1471 0.1576 0.0121  -0.0026 0.0033  49  VAL   B C   
4635 O O   . VAL   B 49  ? 0.1512 0.1505 0.1805 0.0070  -0.0103 0.0082  49  VAL   B O   
4636 C CB  . VAL   B 49  ? 0.1554 0.1648 0.1935 0.0099  -0.0248 0.0017  49  VAL   B CB  
4637 C CG1 . VAL   B 49  ? 0.1527 0.1742 0.1931 0.0043  -0.0356 0.0036  49  VAL   B CG1 
4638 C CG2 . VAL   B 49  ? 0.1701 0.1789 0.2171 -0.0005 -0.0418 -0.0057 49  VAL   B CG2 
4648 N N   . ALA   B 50  ? 0.1409 0.1386 0.1585 0.0029  0.0030  0.0088  50  ALA   B N   
4649 C CA  . ALA   B 50  ? 0.1432 0.1331 0.1651 0.0092  0.0016  0.0065  50  ALA   B CA  
4650 C C   . ALA   B 50  ? 0.1501 0.1365 0.1616 0.0043  -0.0048 0.0041  50  ALA   B C   
4651 O O   . ALA   B 50  ? 0.1464 0.1415 0.1586 0.0088  -0.0061 0.0002  50  ALA   B O   
4652 C CB  . ALA   B 50  ? 0.1515 0.1413 0.1748 0.0040  -0.0018 0.0110  50  ALA   B CB  
4658 N N   . GLY   B 51  ? 0.1461 0.1475 0.1762 0.0121  -0.0133 0.0076  51  GLY   B N   
4659 C CA  . GLY   B 51  ? 0.1486 0.1558 0.1854 0.0138  -0.0129 0.0118  51  GLY   B CA  
4660 C C   . GLY   B 51  ? 0.1511 0.1474 0.1813 0.0205  -0.0120 0.0167  51  GLY   B C   
4661 O O   . GLY   B 51  ? 0.1488 0.1644 0.2091 0.0100  -0.0137 0.0029  51  GLY   B O   
4665 N N   . ALA   B 52  ? 0.1531 0.1437 0.1788 0.0161  -0.0062 0.0120  52  ALA   B N   
4666 C CA  . ALA   B 52  ? 0.1515 0.1540 0.1774 0.0200  -0.0034 -0.0024 52  ALA   B CA  
4667 C C   . ALA   B 52  ? 0.1437 0.1552 0.1699 0.0141  0.0030  -0.0003 52  ALA   B C   
4668 O O   . ALA   B 52  ? 0.1515 0.1541 0.1883 0.0138  0.0077  0.0056  52  ALA   B O   
4669 C CB  . ALA   B 52  ? 0.1694 0.1625 0.1878 0.0118  0.0005  -0.0053 52  ALA   B CB  
4675 N N   . LEU   B 53  ? 0.1393 0.1524 0.1680 0.0177  0.0014  0.0034  53  LEU   B N   
4676 C CA  . LEU   B 53  ? 0.1346 0.1585 0.1559 0.0108  -0.0060 0.0010  53  LEU   B CA  
4677 C C   . LEU   B 53  ? 0.1455 0.1478 0.1578 0.0108  -0.0009 0.0083  53  LEU   B C   
4678 O O   . LEU   B 53  ? 0.1556 0.1602 0.1776 0.0018  0.0036  0.0155  53  LEU   B O   
4679 C CB  . LEU   B 53  ? 0.1412 0.1675 0.1734 0.0117  0.0020  0.0114  53  LEU   B CB  
4680 C CG  . LEU   B 53  ? 0.1375 0.1819 0.1744 0.0040  -0.0002 0.0246  53  LEU   B CG  
4681 C CD1 . LEU   B 53  ? 0.1506 0.2052 0.1880 0.0154  0.0012  -0.0007 53  LEU   B CD1 
4682 C CD2 . LEU   B 53  ? 0.1463 0.2078 0.2022 -0.0061 -0.0080 -0.0144 53  LEU   B CD2 
4694 N N   . ASN   B 54  ? 0.1483 0.1392 0.1628 0.0037  -0.0093 0.0064  54  ASN   B N   
4695 C CA  . ASN   B 54  ? 0.1478 0.1584 0.1698 0.0041  -0.0073 0.0030  54  ASN   B CA  
4696 C C   . ASN   B 54  ? 0.1450 0.1563 0.1882 0.0009  -0.0065 0.0094  54  ASN   B C   
4697 O O   . ASN   B 54  ? 0.1421 0.1650 0.1939 -0.0017 -0.0084 0.0082  54  ASN   B O   
4698 C CB  . ASN   B 54  ? 0.1504 0.1691 0.1771 0.0046  -0.0013 0.0054  54  ASN   B CB  
4699 C CG  . ASN   B 54  ? 0.1478 0.1779 0.1769 0.0057  -0.0140 0.0017  54  ASN   B CG  
4700 O OD1 . ASN   B 54  ? 0.1433 0.1811 0.2069 0.0002  -0.0201 -0.0072 54  ASN   B OD1 
4701 N ND2 . ASN   B 54  ? 0.1571 0.2008 0.2128 -0.0040 -0.0308 0.0221  54  ASN   B ND2 
4708 N N   . LYS   B 55  ? 0.1439 0.1643 0.2056 0.0087  0.0020  0.0062  55  LYS   B N   
4709 C CA  . LYS   B 55  ? 0.1530 0.1774 0.2238 0.0154  -0.0009 0.0047  55  LYS   B CA  
4710 C C   . LYS   B 55  ? 0.1439 0.1754 0.2221 0.0117  -0.0023 -0.0008 55  LYS   B C   
4711 O O   . LYS   B 55  ? 0.1365 0.1839 0.2396 0.0122  -0.0044 0.0024  55  LYS   B O   
4712 C CB  . LYS   B 55  ? 0.1662 0.1874 0.2519 0.0286  0.0044  0.0165  55  LYS   B CB  
4713 C CG  . LYS   B 55  ? 0.2100 0.2103 0.3346 0.0315  0.0235  0.0309  55  LYS   B CG  
4714 C CD  . LYS   B 55  ? 0.2424 0.2319 0.3957 0.0450  0.0481  0.0339  55  LYS   B CD  
4715 C CE  . LYS   B 55  ? 0.2670 0.2519 0.4499 0.0471  0.0696  0.0255  55  LYS   B CE  
4716 N NZ  . LYS   B 55  ? 0.2778 0.2656 0.4773 0.0439  0.0638  0.0260  55  LYS   B NZ  
4730 N N   . ALA   B 56  ? 0.1422 0.1772 0.1997 0.0100  -0.0024 -0.0063 56  ALA   B N   
4731 C CA  . ALA   B 56  ? 0.1570 0.1921 0.2030 -0.0007 0.0044  0.0049  56  ALA   B CA  
4732 C C   . ALA   B 56  ? 0.1618 0.1911 0.1991 -0.0010 0.0094  0.0124  56  ALA   B C   
4733 O O   . ALA   B 56  ? 0.1674 0.2033 0.2255 0.0021  0.0289  0.0181  56  ALA   B O   
4734 C CB  . ALA   B 56  ? 0.1652 0.2140 0.2055 -0.0196 0.0054  -0.0023 56  ALA   B CB  
4740 N N   . THR   B 57  ? 0.1592 0.1792 0.1985 0.0066  0.0126  0.0124  57  THR   B N   
4741 C CA  . THR   B 57  ? 0.1584 0.1765 0.2023 0.0037  0.0164  0.0183  57  THR   B CA  
4742 C C   . THR   B 57  ? 0.1628 0.1841 0.2148 0.0030  0.0141  0.0145  57  THR   B C   
4743 O O   . THR   B 57  ? 0.1696 0.1818 0.2223 -0.0094 0.0082  0.0080  57  THR   B O   
4744 C CB  . THR   B 57  ? 0.1643 0.1631 0.1859 0.0024  0.0164  0.0143  57  THR   B CB  
4745 O OG1 . THR   B 57  ? 0.1618 0.1608 0.1971 -0.0014 0.0085  0.0114  57  THR   B OG1 
4746 C CG2 . THR   B 57  ? 0.1606 0.1650 0.1933 -0.0036 0.0097  0.0008  57  THR   B CG2 
4754 N N   . ASN   B 58  ? 0.1456 0.1991 0.2398 -0.0082 -0.0030 -0.0013 58  ASN   B N   
4755 C CA  . ASN   B 58  ? 0.1601 0.2400 0.2820 -0.0156 0.0138  0.0064  58  ASN   B CA  
4756 C C   . ASN   B 58  ? 0.1479 0.2220 0.2401 -0.0134 -0.0081 0.0058  58  ASN   B C   
4757 O O   . ASN   B 58  ? 0.1517 0.2328 0.2474 -0.0190 -0.0033 -0.0031 58  ASN   B O   
4758 C CB  . ASN   B 58  ? 0.2232 0.2977 0.3900 -0.0252 0.0496  0.0095  58  ASN   B CB  
4759 C CG  . ASN   B 58  ? 0.3005 0.3425 0.5203 -0.0266 0.0750  0.0367  58  ASN   B CG  
4760 O OD1 . ASN   B 58  ? 0.3498 0.3627 0.5692 -0.0283 0.0780  0.0474  58  ASN   B OD1 
4761 N ND2 . ASN   B 58  ? 0.3653 0.3653 0.5639 -0.0307 0.0880  0.0447  58  ASN   B ND2 
4768 N N   . ASN   B 59  ? 0.1479 0.2071 0.2155 -0.0147 -0.0089 0.0145  59  ASN   B N   
4769 C CA  . ASN   B 59  ? 0.1503 0.2089 0.2158 -0.0141 -0.0168 0.0222  59  ASN   B CA  
4770 C C   . ASN   B 59  ? 0.1448 0.1996 0.2084 -0.0202 -0.0212 0.0099  59  ASN   B C   
4771 O O   . ASN   B 59  ? 0.1460 0.2035 0.2002 -0.0135 -0.0136 0.0053  59  ASN   B O   
4772 C CB  . ASN   B 59  ? 0.1637 0.2268 0.2303 -0.0108 -0.0344 0.0153  59  ASN   B CB  
4773 C CG  . ASN   B 59  ? 0.1730 0.2459 0.2438 -0.0044 -0.0486 0.0112  59  ASN   B CG  
4774 O OD1 . ASN   B 59  ? 0.1820 0.2494 0.2440 -0.0070 -0.0386 0.0290  59  ASN   B OD1 
4775 N ND2 . ASN   B 59  ? 0.1807 0.2559 0.2605 -0.0098 -0.0474 0.0162  59  ASN   B ND2 
4782 N N   . ALA   B 60  ? 0.1455 0.1846 0.2111 -0.0170 -0.0165 0.0153  60  ALA   B N   
4783 C CA  . ALA   B 60  ? 0.1544 0.1775 0.2149 -0.0211 -0.0101 0.0173  60  ALA   B CA  
4784 C C   . ALA   B 60  ? 0.1540 0.1632 0.2075 -0.0122 -0.0139 0.0147  60  ALA   B C   
4785 O O   . ALA   B 60  ? 0.1600 0.1680 0.2180 -0.0156 -0.0115 -0.0017 60  ALA   B O   
4786 C CB  . ALA   B 60  ? 0.1668 0.1820 0.2441 -0.0186 -0.0104 0.0144  60  ALA   B CB  
4792 N N   . MET   B 61  ? 0.1428 0.1576 0.1991 -0.0067 -0.0082 0.0160  61  MET   B N   
4793 C CA  . MET   B 61  ? 0.1435 0.1526 0.1903 -0.0049 -0.0165 0.0092  61  MET   B CA  
4794 C C   . MET   B 61  ? 0.1505 0.1537 0.1824 -0.0133 -0.0179 0.0080  61  MET   B C   
4795 O O   . MET   B 61  ? 0.1552 0.1526 0.1672 -0.0082 -0.0145 -0.0076 61  MET   B O   
4796 C CB  . MET   B 61  ? 0.1416 0.1537 0.1826 -0.0004 -0.0192 -0.0003 61  MET   B CB  
4797 C CG  . MET   B 61  ? 0.1424 0.1504 0.1761 0.0010  -0.0135 -0.0001 61  MET   B CG  
4798 S SD  . MET   B 61  ? 0.1437 0.1544 0.1862 -0.0011 -0.0093 -0.0085 61  MET   B SD  
4799 C CE  . MET   B 61  ? 0.1484 0.1723 0.2212 -0.0034 -0.0042 -0.0199 61  MET   B CE  
4809 N N   . GLN   B 62  ? 0.1531 0.1579 0.1734 -0.0089 -0.0255 0.0134  62  GLN   B N   
4810 C CA  . GLN   B 62  ? 0.1507 0.1568 0.1823 -0.0024 -0.0223 0.0005  62  GLN   B CA  
4811 C C   . GLN   B 62  ? 0.1510 0.1651 0.1947 -0.0048 -0.0284 -0.0027 62  GLN   B C   
4812 O O   . GLN   B 62  ? 0.1658 0.1654 0.2034 -0.0002 -0.0331 -0.0075 62  GLN   B O   
4813 C CB  . GLN   B 62  ? 0.1536 0.1617 0.1832 -0.0027 -0.0145 0.0017  62  GLN   B CB  
4814 C CG  . GLN   B 62  ? 0.1564 0.1702 0.1875 -0.0004 -0.0319 -0.0076 62  GLN   B CG  
4815 C CD  . GLN   B 62  ? 0.1592 0.1614 0.1826 0.0043  -0.0308 0.0100  62  GLN   B CD  
4816 O OE1 . GLN   B 62  ? 0.1598 0.1583 0.1924 0.0028  -0.0328 -0.0039 62  GLN   B OE1 
4817 N NE2 . GLN   B 62  ? 0.1595 0.1672 0.1908 -0.0002 -0.0257 -0.0035 62  GLN   B NE2 
4826 N N   . VAL   B 63  ? 0.1506 0.1687 0.2059 -0.0109 -0.0298 -0.0095 63  VAL   B N   
4827 C CA  . VAL   B 63  ? 0.1618 0.1763 0.2148 -0.0116 -0.0368 -0.0003 63  VAL   B CA  
4828 C C   . VAL   B 63  ? 0.1630 0.1621 0.2021 -0.0190 -0.0353 -0.0077 63  VAL   B C   
4829 O O   . VAL   B 63  ? 0.1763 0.1617 0.2130 -0.0118 -0.0445 -0.0099 63  VAL   B O   
4830 C CB  . VAL   B 63  ? 0.1673 0.1937 0.2633 -0.0155 -0.0313 -0.0025 63  VAL   B CB  
4831 C CG1 . VAL   B 63  ? 0.1804 0.2028 0.2727 -0.0255 -0.0261 -0.0024 63  VAL   B CG1 
4832 C CG2 . VAL   B 63  ? 0.1608 0.2103 0.2717 -0.0091 -0.0368 -0.0074 63  VAL   B CG2 
4842 N N   . GLU   B 64  ? 0.1639 0.1535 0.1941 -0.0107 -0.0367 -0.0059 64  GLU   B N   
4843 C CA  . GLU   B 64  ? 0.1650 0.1479 0.1855 -0.0097 -0.0384 -0.0066 64  GLU   B CA  
4844 C C   . GLU   B 64  ? 0.1609 0.1506 0.1779 -0.0017 -0.0315 -0.0195 64  GLU   B C   
4845 O O   . GLU   B 64  ? 0.1740 0.1570 0.1762 -0.0084 -0.0333 -0.0197 64  GLU   B O   
4846 C CB  . GLU   B 64  ? 0.1573 0.1596 0.1799 -0.0101 -0.0269 0.0055  64  GLU   B CB  
4847 C CG  . GLU   B 64  ? 0.1663 0.1614 0.1717 -0.0205 -0.0289 -0.0087 64  GLU   B CG  
4848 C CD  . GLU   B 64  ? 0.1729 0.1694 0.1859 -0.0253 -0.0331 -0.0038 64  GLU   B CD  
4849 O OE1 . GLU   B 64  ? 0.1787 0.1877 0.1898 -0.0336 -0.0310 -0.0237 64  GLU   B OE1 
4850 O OE2 . GLU   B 64  ? 0.1864 0.1712 0.1894 -0.0318 -0.0471 -0.0042 64  GLU   B OE2 
4857 N N   . SER   B 65  ? 0.1585 0.1429 0.1777 -0.0068 -0.0195 -0.0139 65  SER   B N   
4858 C CA  . SER   B 65  ? 0.1589 0.1452 0.1777 0.0002  -0.0226 -0.0183 65  SER   B CA  
4859 C C   . SER   B 65  ? 0.1616 0.1502 0.1763 -0.0023 -0.0290 -0.0134 65  SER   B C   
4860 O O   . SER   B 65  ? 0.1641 0.1594 0.1868 -0.0022 -0.0315 -0.0216 65  SER   B O   
4861 C CB  . SER   B 65  ? 0.1614 0.1500 0.1814 -0.0059 -0.0190 -0.0181 65  SER   B CB  
4862 O OG  . SER   B 65  ? 0.1660 0.1488 0.1797 -0.0071 -0.0213 -0.0216 65  SER   B OG  
4868 N N   . ASP   B 66  ? 0.1701 0.1498 0.1794 -0.0056 -0.0413 -0.0168 66  ASP   B N   
4869 C CA  . ASP   B 66  ? 0.1793 0.1627 0.1742 -0.0015 -0.0381 -0.0182 66  ASP   B CA  
4870 C C   . ASP   B 66  ? 0.1831 0.1714 0.1769 -0.0048 -0.0273 -0.0226 66  ASP   B C   
4871 O O   . ASP   B 66  ? 0.1810 0.1759 0.1870 0.0017  -0.0329 -0.0245 66  ASP   B O   
4872 C CB  . ASP   B 66  ? 0.1960 0.1791 0.1964 0.0078  -0.0442 -0.0182 66  ASP   B CB  
4873 C CG  . ASP   B 66  ? 0.2239 0.1891 0.2260 0.0145  -0.0596 -0.0034 66  ASP   B CG  
4874 O OD1 . ASP   B 66  ? 0.2448 0.1879 0.2298 0.0069  -0.0641 0.0024  66  ASP   B OD1 
4875 O OD2 . ASP   B 66  ? 0.2422 0.2127 0.2814 0.0359  -0.0569 -0.0032 66  ASP   B OD2 
4880 N N   . ASP   B 67  ? 0.1721 0.1613 0.1806 -0.0083 -0.0264 -0.0257 67  ASP   B N   
4881 C CA  . ASP   B 67  ? 0.1928 0.1610 0.1908 -0.0096 -0.0242 -0.0195 67  ASP   B CA  
4882 C C   . ASP   B 67  ? 0.1851 0.1559 0.2026 0.0011  -0.0229 -0.0234 67  ASP   B C   
4883 O O   . ASP   B 67  ? 0.1870 0.1624 0.2189 -0.0012 -0.0159 -0.0259 67  ASP   B O   
4884 C CB  . ASP   B 67  ? 0.2126 0.1663 0.2070 -0.0130 -0.0427 -0.0172 67  ASP   B CB  
4885 C CG  . ASP   B 67  ? 0.2513 0.1771 0.2142 -0.0082 -0.0734 -0.0176 67  ASP   B CG  
4886 O OD1 . ASP   B 67  ? 0.2733 0.1830 0.2300 -0.0148 -0.0814 -0.0103 67  ASP   B OD1 
4887 O OD2 . ASP   B 67  ? 0.2711 0.1839 0.2231 0.0087  -0.0783 -0.0168 67  ASP   B OD2 
4892 N N   . TYR   B 68  ? 0.1785 0.1581 0.1948 0.0004  -0.0417 -0.0241 68  TYR   B N   
4893 C CA  . TYR   B 68  ? 0.1806 0.1764 0.2089 0.0051  -0.0460 -0.0360 68  TYR   B CA  
4894 C C   . TYR   B 68  ? 0.1702 0.1698 0.1939 0.0051  -0.0400 -0.0466 68  TYR   B C   
4895 O O   . TYR   B 68  ? 0.1777 0.1831 0.1971 0.0099  -0.0365 -0.0587 68  TYR   B O   
4896 C CB  . TYR   B 68  ? 0.1879 0.2025 0.2170 0.0077  -0.0526 -0.0495 68  TYR   B CB  
4897 C CG  . TYR   B 68  ? 0.1978 0.2213 0.2260 0.0179  -0.0417 -0.0662 68  TYR   B CG  
4898 C CD1 . TYR   B 68  ? 0.1975 0.2248 0.2394 -0.0055 -0.0432 -0.0829 68  TYR   B CD1 
4899 C CD2 . TYR   B 68  ? 0.2020 0.2356 0.2422 0.0291  -0.0542 -0.0586 68  TYR   B CD2 
4900 C CE1 . TYR   B 68  ? 0.2053 0.2388 0.2668 -0.0002 -0.0329 -0.0842 68  TYR   B CE1 
4901 C CE2 . TYR   B 68  ? 0.2043 0.2398 0.2534 0.0231  -0.0491 -0.0745 68  TYR   B CE2 
4902 C CZ  . TYR   B 68  ? 0.2004 0.2424 0.2659 0.0122  -0.0386 -0.0814 68  TYR   B CZ  
4903 O OH  . TYR   B 68  ? 0.1944 0.2570 0.2974 0.0131  -0.0351 -0.0640 68  TYR   B OH  
4913 N N   . ILE   B 69  ? 0.1696 0.1564 0.2016 0.0024  -0.0316 -0.0335 69  ILE   B N   
4914 C CA  . ILE   B 69  ? 0.1753 0.1691 0.2103 -0.0020 -0.0288 -0.0385 69  ILE   B CA  
4915 C C   . ILE   B 69  ? 0.1777 0.1666 0.2045 0.0055  -0.0373 -0.0289 69  ILE   B C   
4916 O O   . ILE   B 69  ? 0.1870 0.1722 0.1978 0.0053  -0.0350 -0.0288 69  ILE   B O   
4917 C CB  . ILE   B 69  ? 0.1843 0.1731 0.2279 -0.0038 -0.0001 -0.0358 69  ILE   B CB  
4918 C CG1 . ILE   B 69  ? 0.1864 0.1747 0.2422 -0.0087 0.0070  -0.0367 69  ILE   B CG1 
4919 C CG2 . ILE   B 69  ? 0.2055 0.1876 0.2504 0.0068  -0.0013 -0.0243 69  ILE   B CG2 
4920 C CD1 . ILE   B 69  ? 0.1782 0.1814 0.2465 -0.0178 0.0080  -0.0379 69  ILE   B CD1 
4932 N N   . ALA   B 70  ? 0.1755 0.1666 0.2000 0.0139  -0.0422 -0.0275 70  ALA   B N   
4933 C CA  . ALA   B 70  ? 0.1819 0.1749 0.1844 0.0068  -0.0445 -0.0374 70  ALA   B CA  
4934 C C   . ALA   B 70  ? 0.1880 0.1749 0.1948 0.0021  -0.0515 -0.0410 70  ALA   B C   
4935 O O   . ALA   B 70  ? 0.1937 0.1786 0.1936 0.0061  -0.0430 -0.0375 70  ALA   B O   
4936 C CB  . ALA   B 70  ? 0.1822 0.1923 0.1837 0.0023  -0.0405 -0.0330 70  ALA   B CB  
4942 N N   . THR   B 71  ? 0.1996 0.1744 0.2038 0.0038  -0.0676 -0.0353 71  THR   B N   
4943 C CA  . THR   B 71  ? 0.2108 0.1719 0.2168 0.0084  -0.0692 -0.0348 71  THR   B CA  
4944 C C   . THR   B 71  ? 0.2084 0.1744 0.2432 0.0228  -0.0628 -0.0518 71  THR   B C   
4945 O O   . THR   B 71  ? 0.2147 0.1842 0.2729 0.0242  -0.0584 -0.0663 71  THR   B O   
4946 C CB  . THR   B 71  ? 0.2266 0.1985 0.2340 0.0046  -0.0788 -0.0151 71  THR   B CB  
4947 O OG1 . THR   B 71  ? 0.2452 0.2266 0.2624 -0.0166 -0.0734 0.0025  71  THR   B OG1 
4948 C CG2 . THR   B 71  ? 0.2456 0.1954 0.2600 0.0104  -0.0650 0.0009  71  THR   B CG2 
4956 N N   . ASN   B 72  ? 0.1898 0.1802 0.2374 0.0156  -0.0654 -0.0667 72  ASN   B N   
4957 C CA  . ASN   B 72  ? 0.1947 0.1949 0.2362 0.0169  -0.0581 -0.0700 72  ASN   B CA  
4958 C C   . ASN   B 72  ? 0.1947 0.2049 0.2412 0.0033  -0.0351 -0.0701 72  ASN   B C   
4959 O O   . ASN   B 72  ? 0.1997 0.2249 0.2610 0.0055  -0.0060 -0.0707 72  ASN   B O   
4960 C CB  . ASN   B 72  ? 0.2024 0.2084 0.2451 0.0147  -0.0773 -0.0636 72  ASN   B CB  
4961 C CG  . ASN   B 72  ? 0.2217 0.2254 0.2583 0.0320  -0.0759 -0.0391 72  ASN   B CG  
4962 O OD1 . ASN   B 72  ? 0.2420 0.2441 0.2644 0.0205  -0.0608 -0.0383 72  ASN   B OD1 
4963 N ND2 . ASN   B 72  ? 0.2358 0.2344 0.2986 0.0469  -0.0675 -0.0060 72  ASN   B ND2 
4970 N N   . GLY   B 73  ? 0.1995 0.2004 0.2228 0.0021  -0.0358 -0.0715 73  GLY   B N   
4971 C CA  . GLY   B 73  ? 0.1988 0.2061 0.2026 -0.0041 -0.0341 -0.0597 73  GLY   B CA  
4972 C C   . GLY   B 73  ? 0.1880 0.2084 0.1650 0.0007  -0.0255 -0.0565 73  GLY   B C   
4973 O O   . GLY   B 73  ? 0.1809 0.2009 0.1776 0.0057  -0.0272 -0.0454 73  GLY   B O   
4977 N N   . PRO   B 74  ? 0.1866 0.2191 0.1587 0.0075  -0.0290 -0.0441 74  PRO   B N   
4978 C CA  . PRO   B 74  ? 0.1808 0.2161 0.1472 0.0113  -0.0327 -0.0278 74  PRO   B CA  
4979 C C   . PRO   B 74  ? 0.1673 0.2015 0.1425 0.0046  -0.0226 -0.0228 74  PRO   B C   
4980 O O   . PRO   B 74  ? 0.1712 0.2038 0.1974 0.0077  -0.0166 -0.0382 74  PRO   B O   
4981 C CB  . PRO   B 74  ? 0.1965 0.2309 0.1581 0.0108  -0.0288 -0.0261 74  PRO   B CB  
4982 C CG  . PRO   B 74  ? 0.2123 0.2429 0.1921 0.0094  -0.0134 -0.0205 74  PRO   B CG  
4983 C CD  . PRO   B 74  ? 0.2072 0.2344 0.1711 0.0089  -0.0149 -0.0404 74  PRO   B CD  
4991 N N   . LEU   B 75  ? 0.1617 0.1959 0.1341 0.0144  -0.0178 -0.0298 75  LEU   B N   
4992 C CA  . LEU   B 75  ? 0.1624 0.1901 0.1300 0.0078  -0.0156 -0.0094 75  LEU   B CA  
4993 C C   . LEU   B 75  ? 0.1725 0.1979 0.1266 0.0034  -0.0130 -0.0096 75  LEU   B C   
4994 O O   . LEU   B 75  ? 0.1856 0.2099 0.1378 -0.0013 -0.0081 -0.0073 75  LEU   B O   
4995 C CB  . LEU   B 75  ? 0.1661 0.1920 0.1394 -0.0068 -0.0175 0.0024  75  LEU   B CB  
4996 C CG  . LEU   B 75  ? 0.1997 0.2087 0.1763 -0.0350 -0.0142 -0.0105 75  LEU   B CG  
4997 C CD1 . LEU   B 75  ? 0.2298 0.2257 0.1743 -0.0492 0.0002  -0.0158 75  LEU   B CD1 
4998 C CD2 . LEU   B 75  ? 0.2346 0.2314 0.2438 -0.0206 -0.0109 -0.0053 75  LEU   B CD2 
5010 N N   . LYS   B 76  ? 0.1730 0.2185 0.1579 -0.0010 -0.0081 -0.0071 76  LYS   B N   
5011 C CA  . LYS   B 76  ? 0.1766 0.2259 0.2006 -0.0003 0.0154  -0.0081 76  LYS   B CA  
5012 C C   . LYS   B 76  ? 0.1720 0.2078 0.1691 0.0060  -0.0006 0.0122  76  LYS   B C   
5013 O O   . LYS   B 76  ? 0.1663 0.1899 0.1776 0.0033  -0.0024 0.0155  76  LYS   B O   
5014 C CB  . LYS   B 76  ? 0.1975 0.2411 0.2854 -0.0075 0.0400  -0.0375 76  LYS   B CB  
5015 C CG  . LYS   B 76  ? 0.2093 0.2629 0.3456 0.0003  0.0257  -0.0454 76  LYS   B CG  
5016 C CD  . LYS   B 76  ? 0.2085 0.2776 0.4040 0.0103  0.0075  -0.0560 76  LYS   B CD  
5017 C CE  . LYS   B 76  ? 0.2167 0.2959 0.4622 0.0129  -0.0041 -0.0676 76  LYS   B CE  
5018 N NZ  . LYS   B 76  ? 0.2114 0.3007 0.4838 0.0109  -0.0215 -0.0857 76  LYS   B NZ  
5032 N N   . VAL   B 77  ? 0.1822 0.2152 0.1530 0.0126  0.0003  0.0112  77  VAL   B N   
5033 C CA  . VAL   B 77  ? 0.1817 0.2048 0.1556 0.0206  0.0009  0.0342  77  VAL   B CA  
5034 C C   . VAL   B 77  ? 0.1662 0.1858 0.1628 0.0204  0.0073  0.0246  77  VAL   B C   
5035 O O   . VAL   B 77  ? 0.1686 0.1816 0.1636 0.0265  0.0216  0.0179  77  VAL   B O   
5036 C CB  . VAL   B 77  ? 0.1916 0.2172 0.1828 0.0216  0.0148  0.0431  77  VAL   B CB  
5037 C CG1 . VAL   B 77  ? 0.1987 0.2088 0.2052 0.0146  0.0253  0.0566  77  VAL   B CG1 
5038 C CG2 . VAL   B 77  ? 0.2100 0.2396 0.2104 0.0226  -0.0020 0.0528  77  VAL   B CG2 
5048 N N   . GLY   B 78  ? 0.1591 0.1732 0.1541 0.0148  0.0019  0.0194  78  GLY   B N   
5049 C CA  . GLY   B 78  ? 0.1570 0.1717 0.1461 0.0140  0.0107  0.0070  78  GLY   B CA  
5050 C C   . GLY   B 78  ? 0.1555 0.1665 0.1372 0.0104  0.0089  0.0189  78  GLY   B C   
5051 O O   . GLY   B 78  ? 0.1572 0.1603 0.1571 0.0128  0.0078  0.0180  78  GLY   B O   
5055 N N   . GLY   B 79  ? 0.1515 0.1684 0.1499 0.0105  0.0105  0.0029  79  GLY   B N   
5056 C CA  . GLY   B 79  ? 0.1528 0.1558 0.1405 0.0122  0.0013  0.0036  79  GLY   B CA  
5057 C C   . GLY   B 79  ? 0.1480 0.1417 0.1516 0.0112  -0.0019 0.0020  79  GLY   B C   
5058 O O   . GLY   B 79  ? 0.1583 0.1476 0.1574 0.0107  0.0125  0.0160  79  GLY   B O   
5062 N N   . SER   B 80  ? 0.1476 0.1369 0.1712 0.0138  0.0109  -0.0032 80  SER   B N   
5063 C CA  . SER   B 80  ? 0.1419 0.1424 0.1660 0.0041  0.0003  -0.0091 80  SER   B CA  
5064 C C   . SER   B 80  ? 0.1455 0.1422 0.1713 0.0085  -0.0167 -0.0071 80  SER   B C   
5065 O O   . SER   B 80  ? 0.1568 0.1405 0.2045 0.0124  -0.0080 -0.0146 80  SER   B O   
5066 C CB  . SER   B 80  ? 0.1443 0.1438 0.1673 -0.0025 -0.0080 0.0005  80  SER   B CB  
5067 O OG  . SER   B 80  ? 0.1560 0.1526 0.1828 -0.0012 -0.0192 0.0037  80  SER   B OG  
5073 N N   . CYS   B 81  ? 0.1454 0.1263 0.1749 0.0043  -0.0065 -0.0050 81  CYS   B N   
5074 C CA  . CYS   B 81  ? 0.1462 0.1261 0.1714 0.0067  -0.0187 -0.0120 81  CYS   B CA  
5075 C C   . CYS   B 81  ? 0.1490 0.1242 0.1544 0.0017  -0.0196 -0.0060 81  CYS   B C   
5076 O O   . CYS   B 81  ? 0.1698 0.1293 0.1672 0.0079  -0.0104 -0.0096 81  CYS   B O   
5077 C CB  . CYS   B 81  ? 0.1616 0.1376 0.1813 -0.0037 -0.0216 -0.0050 81  CYS   B CB  
5078 S SG  . CYS   B 81  ? 0.1607 0.1605 0.1691 -0.0003 -0.0301 -0.0141 81  CYS   B SG  
5084 N N   . VAL   B 82  ? 0.1518 0.1282 0.1710 0.0041  -0.0172 -0.0100 82  VAL   B N   
5085 C CA  . VAL   B 82  ? 0.1518 0.1246 0.1658 -0.0047 -0.0105 -0.0032 82  VAL   B CA  
5086 C C   . VAL   B 82  ? 0.1572 0.1212 0.1807 -0.0021 -0.0082 -0.0017 82  VAL   B C   
5087 O O   . VAL   B 82  ? 0.1677 0.1258 0.2016 -0.0028 -0.0140 -0.0188 82  VAL   B O   
5088 C CB  . VAL   B 82  ? 0.1643 0.1436 0.1780 -0.0019 -0.0173 0.0101  82  VAL   B CB  
5089 C CG1 . VAL   B 82  ? 0.1848 0.1630 0.1915 0.0084  -0.0230 0.0199  82  VAL   B CG1 
5090 C CG2 . VAL   B 82  ? 0.1745 0.1549 0.1925 -0.0034 -0.0299 0.0127  82  VAL   B CG2 
5100 N N   . LEU   B 83  ? 0.1432 0.1229 0.1682 -0.0124 -0.0212 -0.0082 83  LEU   B N   
5101 C CA  . LEU   B 83  ? 0.1491 0.1287 0.1581 -0.0098 -0.0169 -0.0027 83  LEU   B CA  
5102 C C   . LEU   B 83  ? 0.1488 0.1206 0.1578 -0.0181 -0.0159 -0.0029 83  LEU   B C   
5103 O O   . LEU   B 83  ? 0.1514 0.1374 0.1486 -0.0209 -0.0182 0.0006  83  LEU   B O   
5104 C CB  . LEU   B 83  ? 0.1553 0.1377 0.1665 -0.0117 -0.0218 -0.0147 83  LEU   B CB  
5105 C CG  . LEU   B 83  ? 0.1729 0.1616 0.1840 -0.0102 -0.0163 -0.0123 83  LEU   B CG  
5106 C CD1 . LEU   B 83  ? 0.1850 0.1652 0.1773 -0.0011 -0.0292 0.0020  83  LEU   B CD1 
5107 C CD2 . LEU   B 83  ? 0.1932 0.1610 0.1934 -0.0048 -0.0105 -0.0264 83  LEU   B CD2 
5119 N N   . SER   B 84  ? 0.1533 0.1352 0.1946 -0.0265 -0.0180 0.0116  84  SER   B N   
5120 C CA  . SER   B 84  ? 0.1517 0.1568 0.1804 -0.0261 -0.0201 0.0226  84  SER   B CA  
5121 C C   . SER   B 84  ? 0.1462 0.1777 0.1360 -0.0178 -0.0288 0.0236  84  SER   B C   
5122 O O   . SER   B 84  ? 0.1529 0.1574 0.1360 -0.0170 -0.0201 0.0030  84  SER   B O   
5123 C CB  . SER   B 84  ? 0.1684 0.1637 0.2277 -0.0252 0.0023  0.0217  84  SER   B CB  
5124 O OG  . SER   B 84  ? 0.1708 0.1774 0.2814 -0.0297 0.0092  0.0265  84  SER   B OG  
5130 N N   . GLY   B 85  ? 0.1498 0.2015 0.1456 -0.0260 -0.0131 0.0244  85  GLY   B N   
5131 C CA  . GLY   B 85  ? 0.1540 0.2109 0.1564 -0.0333 -0.0021 -0.0023 85  GLY   B CA  
5132 C C   . GLY   B 85  ? 0.1483 0.1910 0.1564 -0.0389 -0.0104 0.0086  85  GLY   B C   
5133 O O   . GLY   B 85  ? 0.1606 0.1925 0.1615 -0.0580 0.0076  -0.0032 85  GLY   B O   
5137 N N   . HIS   B 86  ? 0.1480 0.1723 0.1684 -0.0282 -0.0293 0.0231  86  HIS   B N   
5138 C CA  . HIS   B 86  ? 0.1490 0.1680 0.1660 -0.0267 -0.0223 0.0182  86  HIS   B CA  
5139 C C   . HIS   B 86  ? 0.1541 0.1794 0.1663 -0.0381 -0.0162 0.0360  86  HIS   B C   
5140 O O   . HIS   B 86  ? 0.1668 0.1894 0.1738 -0.0297 -0.0001 0.0400  86  HIS   B O   
5141 C CB  . HIS   B 86  ? 0.1596 0.1687 0.1788 -0.0180 -0.0319 0.0153  86  HIS   B CB  
5142 C CG  . HIS   B 86  ? 0.1641 0.1740 0.1658 -0.0148 -0.0297 0.0222  86  HIS   B CG  
5143 N ND1 . HIS   B 86  ? 0.1773 0.1945 0.2000 -0.0261 -0.0347 0.0019  86  HIS   B ND1 
5144 C CD2 . HIS   B 86  ? 0.1644 0.1727 0.1763 -0.0112 -0.0264 0.0190  86  HIS   B CD2 
5145 C CE1 . HIS   B 86  ? 0.1775 0.1866 0.1878 -0.0186 -0.0210 -0.0153 86  HIS   B CE1 
5146 N NE2 . HIS   B 86  ? 0.1713 0.1772 0.1681 -0.0052 -0.0220 0.0014  86  HIS   B NE2 
5154 N N   . ASN   B 87  ? 0.1534 0.1767 0.1802 -0.0353 -0.0126 0.0453  87  ASN   B N   
5155 C CA  . ASN   B 87  ? 0.1622 0.1958 0.1942 -0.0296 0.0173  0.0260  87  ASN   B CA  
5156 C C   . ASN   B 87  ? 0.1730 0.1815 0.1763 -0.0305 0.0278  0.0148  87  ASN   B C   
5157 O O   . ASN   B 87  ? 0.1980 0.1887 0.2068 -0.0236 0.0423  0.0096  87  ASN   B O   
5158 C CB  . ASN   B 87  ? 0.1629 0.2301 0.2208 -0.0312 0.0184  0.0165  87  ASN   B CB  
5159 C CG  . ASN   B 87  ? 0.1719 0.2508 0.2212 0.0058  0.0210  0.0335  87  ASN   B CG  
5160 O OD1 . ASN   B 87  ? 0.1715 0.2360 0.1999 0.0165  0.0370  0.0491  87  ASN   B OD1 
5161 N ND2 . ASN   B 87  ? 0.2093 0.2632 0.2524 0.0091  0.0297  0.0307  87  ASN   B ND2 
5168 N N   . LEU   B 88  ? 0.1633 0.1770 0.1479 -0.0337 0.0075  0.0142  88  LEU   B N   
5169 C CA  . LEU   B 88  ? 0.1760 0.1679 0.1573 -0.0318 0.0006  0.0044  88  LEU   B CA  
5170 C C   . LEU   B 88  ? 0.1725 0.1564 0.1668 -0.0326 -0.0032 0.0038  88  LEU   B C   
5171 O O   . LEU   B 88  ? 0.1940 0.1657 0.2010 -0.0168 -0.0246 -0.0089 88  LEU   B O   
5172 C CB  . LEU   B 88  ? 0.1854 0.1751 0.1821 -0.0467 -0.0151 0.0297  88  LEU   B CB  
5173 C CG  . LEU   B 88  ? 0.2213 0.2050 0.1966 -0.0387 -0.0359 0.0442  88  LEU   B CG  
5174 C CD1 . LEU   B 88  ? 0.2350 0.2419 0.2135 -0.0446 -0.0212 0.0545  88  LEU   B CD1 
5175 C CD2 . LEU   B 88  ? 0.2556 0.2301 0.2470 0.0022  -0.0544 0.0237  88  LEU   B CD2 
5187 N N   . ALA   B 89  ? 0.1649 0.1556 0.1657 -0.0344 0.0115  0.0057  89  ALA   B N   
5188 C CA  . ALA   B 89  ? 0.1607 0.1533 0.1451 -0.0333 0.0020  0.0145  89  ALA   B CA  
5189 C C   . ALA   B 89  ? 0.1637 0.1537 0.1456 -0.0318 0.0084  -0.0014 89  ALA   B C   
5190 O O   . ALA   B 89  ? 0.1522 0.1651 0.1828 -0.0360 0.0050  -0.0208 89  ALA   B O   
5191 C CB  . ALA   B 89  ? 0.1560 0.1505 0.1484 -0.0389 0.0003  0.0167  89  ALA   B CB  
5197 N N   . LYS   B 90  ? 0.1963 0.1428 0.1567 -0.0359 -0.0103 0.0040  90  LYS   B N   
5198 C CA  . LYS   B 90  ? 0.2123 0.1430 0.1598 -0.0378 -0.0087 -0.0005 90  LYS   B CA  
5199 C C   . LYS   B 90  ? 0.2053 0.1349 0.1621 -0.0381 -0.0067 -0.0137 90  LYS   B C   
5200 O O   . LYS   B 90  ? 0.2188 0.1591 0.1755 -0.0582 0.0101  -0.0074 90  LYS   B O   
5201 C CB  . LYS   B 90  ? 0.2387 0.1441 0.1903 -0.0293 0.0050  0.0169  90  LYS   B CB  
5202 C CG  . LYS   B 90  ? 0.2410 0.1652 0.2006 -0.0205 0.0349  0.0183  90  LYS   B CG  
5203 C CD  . LYS   B 90  ? 0.2692 0.1987 0.2564 -0.0154 0.0549  0.0024  90  LYS   B CD  
5204 C CE  . LYS   B 90  ? 0.2847 0.2205 0.3022 -0.0196 0.0656  -0.0107 90  LYS   B CE  
5205 N NZ  . LYS   B 90  ? 0.2873 0.2132 0.3003 -0.0322 0.0817  -0.0115 90  LYS   B NZ  
5219 N N   . HIS   B 91  ? 0.1836 0.1252 0.1366 -0.0304 -0.0195 0.0029  91  HIS   B N   
5220 C CA  . HIS   B 91  ? 0.1666 0.1331 0.1510 -0.0235 -0.0177 0.0029  91  HIS   B CA  
5221 C C   . HIS   B 91  ? 0.1571 0.1379 0.1279 -0.0329 -0.0100 0.0007  91  HIS   B C   
5222 O O   . HIS   B 91  ? 0.1740 0.1356 0.1248 -0.0292 -0.0209 -0.0005 91  HIS   B O   
5223 C CB  . HIS   B 91  ? 0.1813 0.1381 0.1942 -0.0056 -0.0136 0.0195  91  HIS   B CB  
5224 C CG  . HIS   B 91  ? 0.2207 0.1519 0.2670 0.0024  0.0192  0.0208  91  HIS   B CG  
5225 N ND1 . HIS   B 91  ? 0.2553 0.1551 0.3187 -0.0016 0.0324  0.0075  91  HIS   B ND1 
5226 C CD2 . HIS   B 91  ? 0.2361 0.1781 0.3121 0.0160  0.0147  0.0560  91  HIS   B CD2 
5227 C CE1 . HIS   B 91  ? 0.2584 0.1707 0.3379 0.0150  0.0311  0.0145  91  HIS   B CE1 
5228 N NE2 . HIS   B 91  ? 0.2493 0.1860 0.3414 0.0247  0.0286  0.0566  91  HIS   B NE2 
5236 N N   . CYS   B 92  ? 0.1519 0.1335 0.1244 -0.0294 -0.0122 -0.0016 92  CYS   B N   
5237 C CA  . CYS   B 92  ? 0.1477 0.1310 0.1268 -0.0225 -0.0116 0.0054  92  CYS   B CA  
5238 C C   . CYS   B 92  ? 0.1358 0.1201 0.1352 -0.0094 -0.0126 0.0063  92  CYS   B C   
5239 O O   . CYS   B 92  ? 0.1474 0.1287 0.1574 -0.0129 -0.0082 -0.0047 92  CYS   B O   
5240 C CB  . CYS   B 92  ? 0.1498 0.1372 0.1446 -0.0152 -0.0089 0.0066  92  CYS   B CB  
5241 S SG  . CYS   B 92  ? 0.1438 0.1393 0.1489 -0.0119 -0.0138 0.0044  92  CYS   B SG  
5247 N N   . LEU   B 93  ? 0.1336 0.1251 0.1256 -0.0156 -0.0065 0.0027  93  LEU   B N   
5248 C CA  . LEU   B 93  ? 0.1378 0.1261 0.1299 -0.0045 -0.0109 0.0038  93  LEU   B CA  
5249 C C   . LEU   B 93  ? 0.1275 0.1271 0.1188 0.0009  -0.0109 0.0033  93  LEU   B C   
5250 O O   . LEU   B 93  ? 0.1339 0.1209 0.1432 -0.0051 -0.0071 -0.0020 93  LEU   B O   
5251 C CB  . LEU   B 93  ? 0.1381 0.1276 0.1491 -0.0009 -0.0150 0.0006  93  LEU   B CB  
5252 C CG  . LEU   B 93  ? 0.1336 0.1396 0.1649 -0.0006 -0.0077 0.0140  93  LEU   B CG  
5253 C CD1 . LEU   B 93  ? 0.1405 0.1505 0.1545 0.0050  -0.0113 0.0035  93  LEU   B CD1 
5254 C CD2 . LEU   B 93  ? 0.1345 0.1426 0.1758 -0.0040 -0.0126 0.0076  93  LEU   B CD2 
5266 N N   . HIS   B 94  ? 0.1306 0.1250 0.1222 -0.0026 -0.0196 0.0023  94  HIS   B N   
5267 C CA  . HIS   B 94  ? 0.1371 0.1246 0.1256 -0.0012 -0.0134 0.0027  94  HIS   B CA  
5268 C C   . HIS   B 94  ? 0.1312 0.1239 0.1536 -0.0009 -0.0056 0.0060  94  HIS   B C   
5269 O O   . HIS   B 94  ? 0.1336 0.1346 0.1897 -0.0034 0.0106  -0.0155 94  HIS   B O   
5270 C CB  . HIS   B 94  ? 0.1330 0.1308 0.1347 -0.0001 -0.0170 0.0019  94  HIS   B CB  
5271 C CG  . HIS   B 94  ? 0.1361 0.1252 0.1386 -0.0067 -0.0270 0.0084  94  HIS   B CG  
5272 N ND1 . HIS   B 94  ? 0.1420 0.1332 0.1484 -0.0048 -0.0262 -0.0016 94  HIS   B ND1 
5273 C CD2 . HIS   B 94  ? 0.1409 0.1272 0.1394 -0.0019 -0.0216 0.0036  94  HIS   B CD2 
5274 C CE1 . HIS   B 94  ? 0.1408 0.1319 0.1506 -0.0096 -0.0224 0.0020  94  HIS   B CE1 
5275 N NE2 . HIS   B 94  ? 0.1374 0.1380 0.1424 -0.0127 -0.0201 -0.0009 94  HIS   B NE2 
5283 N N   . VAL   B 95  ? 0.1310 0.1167 0.1548 0.0012  -0.0045 0.0065  95  VAL   B N   
5284 C CA  . VAL   B 95  ? 0.1297 0.1286 0.1346 0.0000  -0.0046 0.0139  95  VAL   B CA  
5285 C C   . VAL   B 95  ? 0.1354 0.1316 0.1340 -0.0018 0.0086  0.0078  95  VAL   B C   
5286 O O   . VAL   B 95  ? 0.1361 0.1330 0.1524 0.0083  0.0042  0.0145  95  VAL   B O   
5287 C CB  . VAL   B 95  ? 0.1353 0.1314 0.1418 -0.0024 -0.0117 0.0034  95  VAL   B CB  
5288 C CG1 . VAL   B 95  ? 0.1448 0.1447 0.1636 -0.0077 -0.0115 0.0094  95  VAL   B CG1 
5289 C CG2 . VAL   B 95  ? 0.1451 0.1286 0.1468 0.0060  -0.0181 0.0020  95  VAL   B CG2 
5299 N N   . VAL   B 96  ? 0.1439 0.1358 0.1427 0.0078  0.0041  0.0122  96  VAL   B N   
5300 C CA  . VAL   B 96  ? 0.1490 0.1494 0.1365 0.0065  -0.0012 0.0112  96  VAL   B CA  
5301 C C   . VAL   B 96  ? 0.1507 0.1540 0.1520 0.0077  0.0058  0.0155  96  VAL   B C   
5302 O O   . VAL   B 96  ? 0.1517 0.1550 0.1671 0.0040  0.0110  0.0052  96  VAL   B O   
5303 C CB  . VAL   B 96  ? 0.1546 0.1692 0.1396 0.0091  0.0041  0.0028  96  VAL   B CB  
5304 C CG1 . VAL   B 96  ? 0.1530 0.1820 0.1456 0.0150  0.0073  0.0037  96  VAL   B CG1 
5305 C CG2 . VAL   B 96  ? 0.1682 0.1708 0.1598 0.0038  0.0065  -0.0020 96  VAL   B CG2 
5315 N N   . GLY   B 97  ? 0.1586 0.1503 0.1500 0.0054  -0.0005 0.0155  97  GLY   B N   
5316 C CA  . GLY   B 97  ? 0.1669 0.1571 0.1481 0.0060  0.0031  0.0168  97  GLY   B CA  
5317 C C   . GLY   B 97  ? 0.1765 0.1589 0.1585 0.0109  0.0028  0.0121  97  GLY   B C   
5318 O O   . GLY   B 97  ? 0.1843 0.1712 0.1639 0.0024  -0.0033 0.0127  97  GLY   B O   
5322 N N   . PRO   B 98  ? 0.1861 0.1588 0.1633 0.0104  0.0225  0.0236  98  PRO   B N   
5323 C CA  . PRO   B 98  ? 0.1974 0.1715 0.1768 0.0189  0.0362  0.0227  98  PRO   B CA  
5324 C C   . PRO   B 98  ? 0.2076 0.1742 0.1549 0.0282  0.0297  0.0350  98  PRO   B C   
5325 O O   . PRO   B 98  ? 0.1991 0.1723 0.1672 0.0259  0.0321  0.0337  98  PRO   B O   
5326 C CB  . PRO   B 98  ? 0.1873 0.1767 0.1887 0.0100  0.0514  0.0218  98  PRO   B CB  
5327 C CG  . PRO   B 98  ? 0.1860 0.1699 0.1814 0.0121  0.0344  0.0308  98  PRO   B CG  
5328 C CD  . PRO   B 98  ? 0.1667 0.1611 0.1768 0.0141  0.0232  0.0224  98  PRO   B CD  
5336 N N   . ASN   B 99  ? 0.2139 0.1887 0.1590 0.0339  0.0296  0.0220  99  ASN   B N   
5337 C CA  . ASN   B 99  ? 0.2356 0.1916 0.1628 0.0365  0.0235  0.0366  99  ASN   B CA  
5338 C C   . ASN   B 99  ? 0.2602 0.2224 0.1767 0.0319  0.0355  0.0580  99  ASN   B C   
5339 O O   . ASN   B 99  ? 0.2732 0.2269 0.1878 0.0287  0.0277  0.0571  99  ASN   B O   
5340 C CB  . ASN   B 99  ? 0.2400 0.1887 0.1752 0.0408  0.0207  0.0330  99  ASN   B CB  
5341 C CG  . ASN   B 99  ? 0.2394 0.1950 0.1949 0.0309  0.0038  0.0394  99  ASN   B CG  
5342 O OD1 . ASN   B 99  ? 0.2407 0.1959 0.2255 0.0345  -0.0074 0.0418  99  ASN   B OD1 
5343 N ND2 . ASN   B 99  ? 0.2408 0.2022 0.2026 0.0281  -0.0123 0.0332  99  ASN   B ND2 
5350 N N   A VAL   B 100 ? 0.2742 0.2369 0.2096 0.0225  0.0343  0.0665  100 VAL   B N   
5351 N N   B VAL   B 100 ? 0.2771 0.2358 0.2075 0.0239  0.0324  0.0669  100 VAL   B N   
5352 C CA  A VAL   B 100 ? 0.3026 0.2541 0.2558 0.0141  0.0388  0.0747  100 VAL   B CA  
5353 C CA  B VAL   B 100 ? 0.3036 0.2508 0.2486 0.0166  0.0331  0.0751  100 VAL   B CA  
5354 C C   A VAL   B 100 ? 0.3251 0.2557 0.2503 0.0232  0.0370  0.0874  100 VAL   B C   
5355 C C   B VAL   B 100 ? 0.3247 0.2541 0.2465 0.0248  0.0316  0.0876  100 VAL   B C   
5356 O O   A VAL   B 100 ? 0.3313 0.2631 0.2621 0.0203  0.0456  0.0758  100 VAL   B O   
5357 O O   B VAL   B 100 ? 0.3290 0.2590 0.2538 0.0221  0.0370  0.0793  100 VAL   B O   
5358 C CB  A VAL   B 100 ? 0.3109 0.2693 0.3242 -0.0067 0.0378  0.0740  100 VAL   B CB  
5359 C CB  B VAL   B 100 ? 0.3104 0.2625 0.3016 -0.0009 0.0314  0.0729  100 VAL   B CB  
5360 C CG1 A VAL   B 100 ? 0.3152 0.2748 0.3516 -0.0125 0.0389  0.0718  100 VAL   B CG1 
5361 C CG1 B VAL   B 100 ? 0.3139 0.2670 0.3234 -0.0058 0.0316  0.0707  100 VAL   B CG1 
5362 C CG2 A VAL   B 100 ? 0.3142 0.2744 0.3435 -0.0124 0.0405  0.0772  100 VAL   B CG2 
5363 C CG2 B VAL   B 100 ? 0.3129 0.2659 0.3158 -0.0064 0.0331  0.0753  100 VAL   B CG2 
5382 N N   . ASN   B 101 ? 0.3412 0.2577 0.2459 0.0377  0.0236  0.1009  101 ASN   B N   
5383 C CA  . ASN   B 101 ? 0.3852 0.2793 0.2815 0.0487  0.0008  0.1111  101 ASN   B CA  
5384 C C   . ASN   B 101 ? 0.4302 0.3190 0.2896 0.0466  -0.0134 0.1195  101 ASN   B C   
5385 O O   . ASN   B 101 ? 0.4384 0.3324 0.3121 0.0536  -0.0200 0.0989  101 ASN   B O   
5386 C CB  . ASN   B 101 ? 0.3872 0.2725 0.3035 0.0477  0.0058  0.0945  101 ASN   B CB  
5387 C CG  . ASN   B 101 ? 0.3869 0.2642 0.3157 0.0458  0.0073  0.0958  101 ASN   B CG  
5388 O OD1 . ASN   B 101 ? 0.3910 0.2659 0.3455 0.0396  0.0285  0.0875  101 ASN   B OD1 
5389 N ND2 . ASN   B 101 ? 0.3847 0.2691 0.3170 0.0450  -0.0024 0.0853  101 ASN   B ND2 
5397 N N   A LYS   B 102 ? 0.4543 0.3386 0.2926 0.0398  -0.0068 0.1190  102 LYS   B N   
5398 N N   B LYS   B 102 ? 0.4415 0.3370 0.3042 0.0356  -0.0084 0.1080  102 LYS   B N   
5399 C CA  A LYS   B 102 ? 0.4792 0.3682 0.3141 0.0292  0.0062  0.1024  102 LYS   B CA  
5400 C CA  B LYS   B 102 ? 0.4532 0.3606 0.3305 0.0223  0.0016  0.0867  102 LYS   B CA  
5401 C C   A LYS   B 102 ? 0.4786 0.3683 0.2915 0.0316  0.0194  0.1088  102 LYS   B C   
5402 C C   B LYS   B 102 ? 0.4475 0.3587 0.3180 0.0180  0.0092  0.0875  102 LYS   B C   
5403 O O   A LYS   B 102 ? 0.4871 0.3735 0.2963 0.0320  0.0142  0.1042  102 LYS   B O   
5404 O O   B LYS   B 102 ? 0.4527 0.3621 0.3211 0.0184  0.0082  0.0853  102 LYS   B O   
5405 C CB  A LYS   B 102 ? 0.5012 0.3945 0.3683 0.0182  0.0138  0.0706  102 LYS   B CB  
5406 C CB  B LYS   B 102 ? 0.4690 0.3842 0.3742 0.0145  0.0080  0.0588  102 LYS   B CB  
5407 C CG  A LYS   B 102 ? 0.5181 0.4164 0.4263 0.0108  0.0211  0.0383  102 LYS   B CG  
5408 C CG  B LYS   B 102 ? 0.4817 0.4044 0.4192 0.0095  0.0141  0.0310  102 LYS   B CG  
5409 C CD  A LYS   B 102 ? 0.5331 0.4343 0.4782 0.0050  0.0270  0.0135  102 LYS   B CD  
5410 C CD  B LYS   B 102 ? 0.4921 0.4200 0.4587 0.0054  0.0186  0.0097  102 LYS   B CD  
5411 C CE  A LYS   B 102 ? 0.5431 0.4462 0.5194 0.0001  0.0313  -0.0031 102 LYS   B CE  
5412 C CE  B LYS   B 102 ? 0.4991 0.4306 0.4893 0.0019  0.0224  -0.0049 102 LYS   B CE  
5413 N NZ  A LYS   B 102 ? 0.5495 0.4539 0.5434 -0.0030 0.0334  -0.0118 102 LYS   B NZ  
5414 N NZ  B LYS   B 102 ? 0.5029 0.4368 0.5070 0.0001  0.0246  -0.0121 102 LYS   B NZ  
5441 N N   A GLY   B 103 ? 0.4653 0.3612 0.2789 0.0335  0.0398  0.1124  103 GLY   B N   
5442 N N   B GLY   B 103 ? 0.4337 0.3511 0.3093 0.0129  0.0188  0.0874  103 GLY   B N   
5443 C CA  A GLY   B 103 ? 0.4504 0.3550 0.2860 0.0368  0.0609  0.1005  103 GLY   B CA  
5444 C CA  B GLY   B 103 ? 0.4189 0.3432 0.3077 0.0074  0.0271  0.0779  103 GLY   B CA  
5445 C C   A GLY   B 103 ? 0.4310 0.3443 0.2814 0.0378  0.0798  0.0859  103 GLY   B C   
5446 C C   B GLY   B 103 ? 0.4009 0.3323 0.2987 -0.0013 0.0334  0.0652  103 GLY   B C   
5447 O O   A GLY   B 103 ? 0.4366 0.3510 0.2979 0.0347  0.0778  0.0837  103 GLY   B O   
5448 O O   B GLY   B 103 ? 0.4043 0.3368 0.3112 -0.0004 0.0325  0.0634  103 GLY   B O   
5455 N N   A GLU   B 104 ? 0.4043 0.3241 0.2609 0.0423  0.0961  0.0643  104 GLU   B N   
5456 N N   B GLU   B 104 ? 0.3786 0.3140 0.2753 -0.0128 0.0362  0.0489  104 GLU   B N   
5457 C CA  A GLU   B 104 ? 0.3780 0.3086 0.2442 0.0460  0.1049  0.0430  104 GLU   B CA  
5458 C CA  B GLU   B 104 ? 0.3572 0.2984 0.2533 -0.0259 0.0347  0.0342  104 GLU   B CA  
5459 C C   A GLU   B 104 ? 0.3821 0.3089 0.2557 0.0287  0.1260  0.0379  104 GLU   B C   
5460 C C   B GLU   B 104 ? 0.3543 0.2958 0.2565 -0.0306 0.0544  0.0278  104 GLU   B C   
5461 O O   A GLU   B 104 ? 0.3854 0.3107 0.2795 0.0251  0.1190  0.0287  104 GLU   B O   
5462 O O   B GLU   B 104 ? 0.3568 0.2972 0.2693 -0.0299 0.0530  0.0199  104 GLU   B O   
5463 C CB  A GLU   B 104 ? 0.3536 0.2929 0.2254 0.0648  0.0833  0.0238  104 GLU   B CB  
5464 C CB  B GLU   B 104 ? 0.3423 0.2846 0.2315 -0.0360 0.0102  0.0245  104 GLU   B CB  
5465 C CG  A GLU   B 104 ? 0.3351 0.2829 0.2055 0.0785  0.0594  0.0010  104 GLU   B CG  
5466 C CG  B GLU   B 104 ? 0.3320 0.2730 0.2117 -0.0461 -0.0127 0.0114  104 GLU   B CG  
5467 C CD  A GLU   B 104 ? 0.3180 0.2737 0.1869 0.0894  0.0367  -0.0025 104 GLU   B CD  
5468 C CD  B GLU   B 104 ? 0.3222 0.2613 0.1977 -0.0598 -0.0279 0.0102  104 GLU   B CD  
5469 O OE1 A GLU   B 104 ? 0.2956 0.2615 0.1578 0.0999  0.0461  0.0047  104 GLU   B OE1 
5470 O OE1 B GLU   B 104 ? 0.3106 0.2509 0.1942 -0.0736 -0.0202 0.0134  104 GLU   B OE1 
5471 O OE2 A GLU   B 104 ? 0.3252 0.2876 0.2147 0.0831  0.0071  -0.0110 104 GLU   B OE2 
5472 O OE2 B GLU   B 104 ? 0.3232 0.2659 0.1943 -0.0630 -0.0480 0.0035  104 GLU   B OE2 
5485 N N   A ASP   B 105 ? 0.3806 0.3127 0.2610 0.0114  0.1492  0.0433  105 ASP   B N   
5486 N N   B ASP   B 105 ? 0.3482 0.2961 0.2570 -0.0381 0.0748  0.0289  105 ASP   B N   
5487 C CA  A ASP   B 105 ? 0.3842 0.3157 0.2889 0.0005  0.1648  0.0254  105 ASP   B CA  
5488 C CA  B ASP   B 105 ? 0.3454 0.2971 0.2728 -0.0418 0.0899  0.0181  105 ASP   B CA  
5489 C C   A ASP   B 105 ? 0.3704 0.2868 0.2744 -0.0025 0.1665  0.0141  105 ASP   B C   
5490 C C   B ASP   B 105 ? 0.3372 0.2821 0.2614 -0.0431 0.0833  0.0051  105 ASP   B C   
5491 O O   A ASP   B 105 ? 0.3597 0.2795 0.2680 0.0021  0.1733  0.0111  105 ASP   B O   
5492 O O   B ASP   B 105 ? 0.3287 0.2748 0.2463 -0.0461 0.0797  0.0001  105 ASP   B O   
5493 C CB  A ASP   B 105 ? 0.3996 0.3412 0.3495 -0.0001 0.1644  0.0088  105 ASP   B CB  
5494 C CB  B ASP   B 105 ? 0.3491 0.3101 0.3040 -0.0420 0.1064  0.0164  105 ASP   B CB  
5495 C CG  A ASP   B 105 ? 0.4096 0.3583 0.4075 -0.0041 0.1670  -0.0017 105 ASP   B CG  
5496 C CG  B ASP   B 105 ? 0.3508 0.3171 0.3308 -0.0456 0.1234  0.0212  105 ASP   B CG  
5497 O OD1 A ASP   B 105 ? 0.4112 0.3653 0.4144 -0.0099 0.1732  0.0023  105 ASP   B OD1 
5498 O OD1 B ASP   B 105 ? 0.3502 0.3193 0.3332 -0.0524 0.1292  0.0260  105 ASP   B OD1 
5499 O OD2 A ASP   B 105 ? 0.4154 0.3662 0.4489 -0.0037 0.1533  -0.0126 105 ASP   B OD2 
5500 O OD2 B ASP   B 105 ? 0.3480 0.3206 0.3325 -0.0491 0.1384  0.0285  105 ASP   B OD2 
5509 N N   A ILE   B 106 ? 0.3640 0.2613 0.2814 -0.0058 0.1551  0.0107  106 ILE   B N   
5510 N N   B ILE   B 106 ? 0.3346 0.2727 0.2671 -0.0406 0.0788  -0.0007 106 ILE   B N   
5511 C CA  A ILE   B 106 ? 0.3435 0.2343 0.2872 -0.0110 0.1616  0.0091  106 ILE   B CA  
5512 C CA  B ILE   B 106 ? 0.3244 0.2628 0.2745 -0.0404 0.0823  -0.0048 106 ILE   B CA  
5513 C C   A ILE   B 106 ? 0.3115 0.2287 0.2785 -0.0076 0.1550  -0.0053 106 ILE   B C   
5514 C C   B ILE   B 106 ? 0.3040 0.2622 0.2719 -0.0385 0.0740  -0.0202 106 ILE   B C   
5515 O O   A ILE   B 106 ? 0.3018 0.2040 0.2779 -0.0115 0.1443  -0.0020 106 ILE   B O   
5516 O O   B ILE   B 106 ? 0.2955 0.2520 0.2632 -0.0480 0.0602  -0.0294 106 ILE   B O   
5517 C CB  A ILE   B 106 ? 0.3609 0.2245 0.3135 -0.0183 0.1552  0.0173  106 ILE   B CB  
5518 C CB  B ILE   B 106 ? 0.3361 0.2591 0.2870 -0.0403 0.0871  0.0030  106 ILE   B CB  
5519 C CG1 A ILE   B 106 ? 0.3677 0.2231 0.3263 -0.0131 0.1448  0.0162  106 ILE   B CG1 
5520 C CG1 B ILE   B 106 ? 0.3410 0.2585 0.2939 -0.0337 0.0835  0.0048  106 ILE   B CG1 
5521 C CG2 A ILE   B 106 ? 0.3675 0.2287 0.3310 -0.0246 0.1581  0.0164  106 ILE   B CG2 
5522 C CG2 B ILE   B 106 ? 0.3409 0.2626 0.2990 -0.0427 0.0917  0.0014  106 ILE   B CG2 
5523 C CD1 A ILE   B 106 ? 0.3706 0.2247 0.3280 -0.0061 0.1431  0.0207  106 ILE   B CD1 
5524 C CD1 B ILE   B 106 ? 0.3434 0.2597 0.2977 -0.0282 0.0837  0.0101  106 ILE   B CD1 
5547 N N   A GLN   B 107 ? 0.2957 0.2535 0.2963 -0.0111 0.1410  -0.0070 107 GLN   B N   
5548 N N   B GLN   B 107 ? 0.2943 0.2745 0.2900 -0.0306 0.0730  -0.0210 107 GLN   B N   
5549 C CA  A GLN   B 107 ? 0.2808 0.2740 0.3174 -0.0098 0.1271  -0.0034 107 GLN   B CA  
5550 C CA  B GLN   B 107 ? 0.2855 0.2835 0.3128 -0.0181 0.0735  -0.0161 107 GLN   B CA  
5551 C C   A GLN   B 107 ? 0.2539 0.2544 0.2954 0.0040  0.0857  -0.0137 107 GLN   B C   
5552 C C   B GLN   B 107 ? 0.2580 0.2620 0.2885 -0.0032 0.0638  -0.0187 107 GLN   B C   
5553 O O   A GLN   B 107 ? 0.2467 0.2567 0.3252 0.0177  0.0636  -0.0253 107 GLN   B O   
5554 O O   B GLN   B 107 ? 0.2556 0.2676 0.3083 0.0022  0.0510  -0.0275 107 GLN   B O   
5555 C CB  A GLN   B 107 ? 0.3059 0.3185 0.3837 -0.0130 0.1230  0.0042  107 GLN   B CB  
5556 C CB  B GLN   B 107 ? 0.3093 0.3140 0.3701 -0.0157 0.0690  -0.0104 107 GLN   B CB  
5557 C CG  A GLN   B 107 ? 0.3359 0.3604 0.4589 -0.0058 0.0975  0.0082  107 GLN   B CG  
5558 C CG  B GLN   B 107 ? 0.3340 0.3410 0.4315 -0.0082 0.0552  -0.0053 107 GLN   B CG  
5559 C CD  A GLN   B 107 ? 0.3557 0.3877 0.5175 -0.0024 0.0798  0.0147  107 GLN   B CD  
5560 C CD  B GLN   B 107 ? 0.3513 0.3608 0.4804 -0.0039 0.0441  0.0002  107 GLN   B CD  
5561 O OE1 A GLN   B 107 ? 0.3623 0.4016 0.5381 0.0013  0.0814  0.0136  107 GLN   B OE1 
5562 O OE1 B GLN   B 107 ? 0.3577 0.3693 0.4990 -0.0012 0.0463  -0.0004 107 GLN   B OE1 
5563 N NE2 A GLN   B 107 ? 0.3646 0.3991 0.5387 0.0011  0.0701  0.0200  107 GLN   B NE2 
5564 N NE2 B GLN   B 107 ? 0.3593 0.3668 0.4967 -0.0006 0.0382  0.0047  107 GLN   B NE2 
5581 N N   . LEU   B 108 ? 0.2308 0.2356 0.2536 0.0084  0.0680  -0.0132 108 LEU   B N   
5582 C CA  . LEU   B 108 ? 0.2207 0.2128 0.2122 0.0231  0.0404  0.0018  108 LEU   B CA  
5583 C C   . LEU   B 108 ? 0.1911 0.1782 0.2018 0.0193  0.0245  0.0219  108 LEU   B C   
5584 O O   . LEU   B 108 ? 0.1971 0.1692 0.2018 0.0225  0.0199  0.0158  108 LEU   B O   
5585 C CB  . LEU   B 108 ? 0.2394 0.2362 0.2064 0.0181  0.0387  0.0008  108 LEU   B CB  
5586 C CG  . LEU   B 108 ? 0.2517 0.2628 0.2113 0.0197  0.0332  -0.0286 108 LEU   B CG  
5587 C CD1 . LEU   B 108 ? 0.2558 0.2803 0.2054 0.0084  0.0353  -0.0277 108 LEU   B CD1 
5588 C CD2 . LEU   B 108 ? 0.2716 0.2737 0.2349 0.0274  0.0245  -0.0394 108 LEU   B CD2 
5601 N N   . LEU   B 109 ? 0.1811 0.1656 0.1947 0.0176  0.0336  0.0219  109 LEU   B N   
5602 C CA  . LEU   B 109 ? 0.1689 0.1456 0.2016 0.0102  0.0246  0.0204  109 LEU   B CA  
5603 C C   . LEU   B 109 ? 0.1515 0.1303 0.2022 0.0058  0.0255  0.0138  109 LEU   B C   
5604 O O   . LEU   B 109 ? 0.1431 0.1317 0.2064 0.0076  0.0210  0.0272  109 LEU   B O   
5605 C CB  . LEU   B 109 ? 0.1773 0.1408 0.1989 0.0083  0.0151  0.0245  109 LEU   B CB  
5606 C CG  . LEU   B 109 ? 0.1702 0.1418 0.1998 0.0075  0.0078  0.0222  109 LEU   B CG  
5607 C CD1 . LEU   B 109 ? 0.1678 0.1518 0.2095 0.0113  0.0216  0.0150  109 LEU   B CD1 
5608 C CD2 . LEU   B 109 ? 0.1761 0.1447 0.2206 0.0106  0.0051  0.0123  109 LEU   B CD2 
5620 N N   . LYS   B 110 ? 0.1494 0.1304 0.1976 0.0021  0.0297  0.0283  110 LYS   B N   
5621 C CA  . LYS   B 110 ? 0.1505 0.1295 0.2073 0.0033  0.0165  0.0132  110 LYS   B CA  
5622 C C   . LYS   B 110 ? 0.1422 0.1309 0.2011 0.0048  0.0235  0.0058  110 LYS   B C   
5623 O O   . LYS   B 110 ? 0.1378 0.1354 0.1881 -0.0067 0.0076  0.0030  110 LYS   B O   
5624 C CB  . LYS   B 110 ? 0.1530 0.1351 0.2311 -0.0027 0.0208  0.0138  110 LYS   B CB  
5625 C CG  . LYS   B 110 ? 0.1538 0.1337 0.2467 -0.0057 0.0049  0.0123  110 LYS   B CG  
5626 C CD  . LYS   B 110 ? 0.1556 0.1300 0.2565 -0.0105 0.0017  0.0134  110 LYS   B CD  
5627 C CE  . LYS   B 110 ? 0.1469 0.1421 0.2753 -0.0052 0.0065  -0.0027 110 LYS   B CE  
5628 N NZ  . LYS   B 110 ? 0.1476 0.1531 0.2624 -0.0016 0.0059  -0.0003 110 LYS   B NZ  
5642 N N   . SER   B 111 ? 0.1524 0.1344 0.2018 -0.0008 0.0341  0.0137  111 SER   B N   
5643 C CA  . SER   B 111 ? 0.1552 0.1351 0.1957 0.0047  0.0165  0.0193  111 SER   B CA  
5644 C C   . SER   B 111 ? 0.1526 0.1272 0.1798 0.0051  0.0092  0.0047  111 SER   B C   
5645 O O   . SER   B 111 ? 0.1428 0.1339 0.1890 0.0003  0.0044  0.0062  111 SER   B O   
5646 C CB  . SER   B 111 ? 0.1660 0.1519 0.2127 0.0047  0.0302  0.0297  111 SER   B CB  
5647 O OG  . SER   B 111 ? 0.1857 0.1952 0.2208 0.0087  0.0425  0.0275  111 SER   B OG  
5653 N N   . ALA   B 112 ? 0.1431 0.1325 0.1827 0.0085  0.0145  0.0162  112 ALA   B N   
5654 C CA  . ALA   B 112 ? 0.1385 0.1421 0.1730 0.0034  0.0019  0.0034  112 ALA   B CA  
5655 C C   . ALA   B 112 ? 0.1311 0.1364 0.1625 0.0062  0.0058  -0.0040 112 ALA   B C   
5656 O O   . ALA   B 112 ? 0.1315 0.1362 0.1825 -0.0023 0.0098  0.0014  112 ALA   B O   
5657 C CB  . ALA   B 112 ? 0.1445 0.1508 0.1844 0.0122  -0.0017 0.0140  112 ALA   B CB  
5663 N N   . TYR   B 113 ? 0.1277 0.1287 0.1795 0.0035  -0.0018 0.0022  113 TYR   B N   
5664 C CA  . TYR   B 113 ? 0.1275 0.1201 0.1764 -0.0006 0.0036  -0.0007 113 TYR   B CA  
5665 C C   . TYR   B 113 ? 0.1250 0.1206 0.1794 -0.0040 0.0008  0.0051  113 TYR   B C   
5666 O O   . TYR   B 113 ? 0.1307 0.1196 0.1781 -0.0041 -0.0015 -0.0014 113 TYR   B O   
5667 C CB  . TYR   B 113 ? 0.1326 0.1115 0.1918 -0.0000 0.0109  0.0035  113 TYR   B CB  
5668 C CG  . TYR   B 113 ? 0.1375 0.1179 0.1912 -0.0082 -0.0008 0.0069  113 TYR   B CG  
5669 C CD1 . TYR   B 113 ? 0.1477 0.1189 0.1999 -0.0024 0.0065  0.0216  113 TYR   B CD1 
5670 C CD2 . TYR   B 113 ? 0.1444 0.1239 0.1856 -0.0078 -0.0043 0.0123  113 TYR   B CD2 
5671 C CE1 . TYR   B 113 ? 0.1436 0.1283 0.1904 -0.0008 0.0098  0.0081  113 TYR   B CE1 
5672 C CE2 . TYR   B 113 ? 0.1525 0.1101 0.1976 0.0046  0.0062  0.0132  113 TYR   B CE2 
5673 C CZ  . TYR   B 113 ? 0.1462 0.1197 0.1976 0.0069  0.0051  0.0055  113 TYR   B CZ  
5674 O OH  . TYR   B 113 ? 0.1498 0.1200 0.2196 0.0072  0.0100  0.0092  113 TYR   B OH  
5684 N N   . GLU   B 114 ? 0.1227 0.1152 0.1844 -0.0018 -0.0008 0.0057  114 GLU   B N   
5685 C CA  . GLU   B 114 ? 0.1250 0.1161 0.1822 0.0017  -0.0028 -0.0025 114 GLU   B CA  
5686 C C   . GLU   B 114 ? 0.1170 0.1123 0.1852 0.0049  0.0090  -0.0037 114 GLU   B C   
5687 O O   . GLU   B 114 ? 0.1208 0.1200 0.2007 0.0062  0.0003  0.0119  114 GLU   B O   
5688 C CB  . GLU   B 114 ? 0.1292 0.1230 0.1902 -0.0028 -0.0029 0.0067  114 GLU   B CB  
5689 C CG  . GLU   B 114 ? 0.1339 0.1223 0.1952 -0.0052 0.0052  0.0118  114 GLU   B CG  
5690 C CD  . GLU   B 114 ? 0.1282 0.1305 0.1918 -0.0091 0.0002  0.0041  114 GLU   B CD  
5691 O OE1 . GLU   B 114 ? 0.1229 0.1450 0.1918 -0.0055 0.0121  0.0079  114 GLU   B OE1 
5692 O OE2 . GLU   B 114 ? 0.1279 0.1458 0.2097 -0.0144 0.0013  0.0088  114 GLU   B OE2 
5699 N N   . ASN   B 115 ? 0.1238 0.1098 0.1782 -0.0016 -0.0028 -0.0009 115 ASN   B N   
5700 C CA  . ASN   B 115 ? 0.1276 0.1226 0.1647 -0.0059 0.0003  0.0006  115 ASN   B CA  
5701 C C   . ASN   B 115 ? 0.1233 0.1196 0.1648 -0.0066 -0.0057 0.0015  115 ASN   B C   
5702 O O   . ASN   B 115 ? 0.1330 0.1236 0.1825 -0.0079 -0.0033 0.0012  115 ASN   B O   
5703 C CB  . ASN   B 115 ? 0.1356 0.1381 0.1734 -0.0038 0.0047  0.0054  115 ASN   B CB  
5704 C CG  . ASN   B 115 ? 0.1445 0.1421 0.1770 0.0058  0.0025  0.0012  115 ASN   B CG  
5705 O OD1 . ASN   B 115 ? 0.1877 0.1515 0.1943 0.0049  0.0073  -0.0165 115 ASN   B OD1 
5706 N ND2 . ASN   B 115 ? 0.1413 0.1507 0.1754 -0.0044 -0.0014 0.0070  115 ASN   B ND2 
5713 N N   . PHE   B 116 ? 0.1241 0.1164 0.1692 -0.0022 0.0053  0.0029  116 PHE   B N   
5714 C CA  . PHE   B 116 ? 0.1333 0.1213 0.1680 -0.0079 -0.0029 0.0065  116 PHE   B CA  
5715 C C   . PHE   B 116 ? 0.1344 0.1105 0.1764 -0.0097 -0.0110 0.0093  116 PHE   B C   
5716 O O   . PHE   B 116 ? 0.1378 0.1171 0.1754 -0.0005 -0.0111 -0.0011 116 PHE   B O   
5717 C CB  . PHE   B 116 ? 0.1276 0.1187 0.1613 -0.0028 -0.0059 0.0028  116 PHE   B CB  
5718 C CG  . PHE   B 116 ? 0.1218 0.1202 0.1590 -0.0023 -0.0042 0.0065  116 PHE   B CG  
5719 C CD1 . PHE   B 116 ? 0.1314 0.1270 0.1754 0.0030  -0.0094 0.0089  116 PHE   B CD1 
5720 C CD2 . PHE   B 116 ? 0.1299 0.1262 0.1646 -0.0024 -0.0036 -0.0043 116 PHE   B CD2 
5721 C CE1 . PHE   B 116 ? 0.1377 0.1300 0.1744 -0.0034 -0.0171 0.0022  116 PHE   B CE1 
5722 C CE2 . PHE   B 116 ? 0.1275 0.1256 0.1672 0.0024  -0.0029 0.0104  116 PHE   B CE2 
5723 C CZ  . PHE   B 116 ? 0.1253 0.1279 0.1688 -0.0085 -0.0165 0.0056  116 PHE   B CZ  
5733 N N   . ASN   B 117 ? 0.1313 0.1165 0.1789 -0.0036 -0.0141 0.0058  117 ASN   B N   
5734 C CA  . ASN   B 117 ? 0.1364 0.1177 0.1687 0.0030  -0.0006 -0.0010 117 ASN   B CA  
5735 C C   . ASN   B 117 ? 0.1413 0.1182 0.1916 0.0012  -0.0006 0.0034  117 ASN   B C   
5736 O O   . ASN   B 117 ? 0.1513 0.1239 0.2095 -0.0052 -0.0287 0.0127  117 ASN   B O   
5737 C CB  . ASN   B 117 ? 0.1393 0.1230 0.1658 0.0005  -0.0096 -0.0014 117 ASN   B CB  
5738 C CG  . ASN   B 117 ? 0.1328 0.1225 0.1813 0.0027  -0.0136 -0.0097 117 ASN   B CG  
5739 O OD1 . ASN   B 117 ? 0.1587 0.1215 0.2030 -0.0113 -0.0015 -0.0019 117 ASN   B OD1 
5740 N ND2 . ASN   B 117 ? 0.1341 0.1267 0.1716 -0.0026 -0.0020 -0.0038 117 ASN   B ND2 
5747 N N   . GLN   B 118 ? 0.1386 0.1104 0.1940 -0.0053 -0.0156 -0.0022 118 GLN   B N   
5748 C CA  . GLN   B 118 ? 0.1423 0.1173 0.1954 0.0044  -0.0115 -0.0044 118 GLN   B CA  
5749 C C   . GLN   B 118 ? 0.1445 0.1219 0.1984 -0.0005 -0.0070 -0.0025 118 GLN   B C   
5750 O O   . GLN   B 118 ? 0.1615 0.1182 0.2303 -0.0123 0.0032  0.0009  118 GLN   B O   
5751 C CB  . GLN   B 118 ? 0.1508 0.1236 0.2010 0.0022  -0.0077 0.0022  118 GLN   B CB  
5752 C CG  . GLN   B 118 ? 0.1561 0.1257 0.1955 0.0083  -0.0096 -0.0120 118 GLN   B CG  
5753 C CD  . GLN   B 118 ? 0.1638 0.1211 0.2033 0.0040  -0.0088 -0.0145 118 GLN   B CD  
5754 O OE1 . GLN   B 118 ? 0.1678 0.1203 0.2199 0.0072  0.0126  0.0046  118 GLN   B OE1 
5755 N NE2 . GLN   B 118 ? 0.1689 0.1197 0.2157 0.0005  -0.0179 0.0016  118 GLN   B NE2 
5764 N N   . HIS   B 119 ? 0.1455 0.1249 0.1655 -0.0068 -0.0119 0.0010  119 HIS   B N   
5765 C CA  . HIS   B 119 ? 0.1526 0.1364 0.1577 -0.0031 -0.0120 0.0074  119 HIS   B CA  
5766 C C   . HIS   B 119 ? 0.1569 0.1363 0.1608 -0.0041 -0.0297 0.0110  119 HIS   B C   
5767 O O   . HIS   B 119 ? 0.1616 0.1343 0.1791 -0.0230 -0.0153 0.0087  119 HIS   B O   
5768 C CB  . HIS   B 119 ? 0.1558 0.1512 0.1653 -0.0023 -0.0127 0.0005  119 HIS   B CB  
5769 C CG  . HIS   B 119 ? 0.1647 0.1716 0.1916 0.0132  -0.0315 -0.0191 119 HIS   B CG  
5770 N ND1 . HIS   B 119 ? 0.1799 0.1831 0.2230 0.0060  -0.0510 -0.0429 119 HIS   B ND1 
5771 C CD2 . HIS   B 119 ? 0.1820 0.1889 0.2036 0.0362  -0.0438 -0.0213 119 HIS   B CD2 
5772 C CE1 . HIS   B 119 ? 0.1997 0.1947 0.2294 0.0184  -0.0571 -0.0495 119 HIS   B CE1 
5773 N NE2 . HIS   B 119 ? 0.2021 0.2108 0.2182 0.0345  -0.0523 -0.0407 119 HIS   B NE2 
5781 N N   . GLU   B 120 ? 0.1718 0.1345 0.1605 -0.0108 -0.0310 0.0090  120 GLU   B N   
5782 C CA  . GLU   B 120 ? 0.2004 0.1476 0.1721 -0.0041 -0.0397 0.0212  120 GLU   B CA  
5783 C C   . GLU   B 120 ? 0.1840 0.1392 0.1674 -0.0119 -0.0323 0.0188  120 GLU   B C   
5784 O O   . GLU   B 120 ? 0.1786 0.1498 0.1602 -0.0128 -0.0332 0.0092  120 GLU   B O   
5785 C CB  . GLU   B 120 ? 0.2572 0.1779 0.2305 0.0223  -0.0685 0.0386  120 GLU   B CB  
5786 C CG  . GLU   B 120 ? 0.3090 0.2427 0.3248 0.0315  -0.0841 0.0570  120 GLU   B CG  
5787 C CD  . GLU   B 120 ? 0.3471 0.3077 0.4241 0.0267  -0.0857 0.0707  120 GLU   B CD  
5788 O OE1 . GLU   B 120 ? 0.3700 0.3273 0.4598 0.0186  -0.0767 0.0850  120 GLU   B OE1 
5789 O OE2 . GLU   B 120 ? 0.3733 0.3329 0.4811 0.0236  -0.0858 0.0576  120 GLU   B OE2 
5796 N N   . VAL   B 121 ? 0.1706 0.1323 0.1720 -0.0151 -0.0186 0.0144  121 VAL   B N   
5797 C CA  . VAL   B 121 ? 0.1642 0.1423 0.1490 -0.0185 -0.0203 0.0122  121 VAL   B CA  
5798 C C   . VAL   B 121 ? 0.1610 0.1400 0.1480 -0.0233 -0.0230 0.0100  121 VAL   B C   
5799 O O   . VAL   B 121 ? 0.1720 0.1371 0.1708 -0.0274 -0.0308 0.0053  121 VAL   B O   
5800 C CB  . VAL   B 121 ? 0.1807 0.1812 0.1605 -0.0011 -0.0226 0.0199  121 VAL   B CB  
5801 C CG1 . VAL   B 121 ? 0.1871 0.1919 0.1978 -0.0121 -0.0085 0.0120  121 VAL   B CG1 
5802 C CG2 . VAL   B 121 ? 0.2080 0.2093 0.1642 0.0068  -0.0186 0.0139  121 VAL   B CG2 
5812 N N   . LEU   B 122 ? 0.1497 0.1330 0.1431 -0.0195 -0.0284 0.0092  122 LEU   B N   
5813 C CA  . LEU   B 122 ? 0.1448 0.1446 0.1357 -0.0188 -0.0195 0.0105  122 LEU   B CA  
5814 C C   . LEU   B 122 ? 0.1364 0.1301 0.1476 -0.0263 -0.0112 0.0115  122 LEU   B C   
5815 O O   . LEU   B 122 ? 0.1513 0.1377 0.1739 -0.0285 -0.0229 0.0003  122 LEU   B O   
5816 C CB  . LEU   B 122 ? 0.1635 0.1542 0.1755 0.0028  -0.0269 0.0096  122 LEU   B CB  
5817 C CG  . LEU   B 122 ? 0.1531 0.1601 0.1888 -0.0091 -0.0139 0.0017  122 LEU   B CG  
5818 C CD1 . LEU   B 122 ? 0.1561 0.1768 0.1986 -0.0096 -0.0181 0.0007  122 LEU   B CD1 
5819 C CD2 . LEU   B 122 ? 0.1560 0.1621 0.1758 -0.0082 -0.0064 0.0045  122 LEU   B CD2 
5831 N N   . LEU   B 123 ? 0.1438 0.1176 0.1469 -0.0227 -0.0105 0.0049  123 LEU   B N   
5832 C CA  . LEU   B 123 ? 0.1494 0.1236 0.1542 -0.0225 -0.0154 -0.0035 123 LEU   B CA  
5833 C C   . LEU   B 123 ? 0.1421 0.1181 0.1466 -0.0186 -0.0059 0.0031  123 LEU   B C   
5834 O O   . LEU   B 123 ? 0.1584 0.1246 0.1464 -0.0249 -0.0107 -0.0004 123 LEU   B O   
5835 C CB  . LEU   B 123 ? 0.1559 0.1288 0.1503 -0.0231 -0.0116 -0.0007 123 LEU   B CB  
5836 C CG  . LEU   B 123 ? 0.1503 0.1324 0.1591 -0.0121 -0.0056 0.0121  123 LEU   B CG  
5837 C CD1 . LEU   B 123 ? 0.1602 0.1415 0.1662 -0.0157 0.0039  -0.0028 123 LEU   B CD1 
5838 C CD2 . LEU   B 123 ? 0.1604 0.1440 0.1748 -0.0116 -0.0042 0.0191  123 LEU   B CD2 
5850 N N   . ALA   B 124 ? 0.1442 0.1233 0.1459 -0.0187 -0.0050 -0.0089 124 ALA   B N   
5851 C CA  . ALA   B 124 ? 0.1333 0.1264 0.1589 -0.0167 -0.0078 -0.0126 124 ALA   B CA  
5852 C C   . ALA   B 124 ? 0.1292 0.1231 0.1507 -0.0192 -0.0075 -0.0048 124 ALA   B C   
5853 O O   . ALA   B 124 ? 0.1473 0.1213 0.1527 -0.0149 -0.0138 0.0009  124 ALA   B O   
5854 C CB  . ALA   B 124 ? 0.1444 0.1324 0.1679 -0.0076 0.0083  -0.0019 124 ALA   B CB  
5860 N N   . PRO   B 125 ? 0.1438 0.1249 0.1322 -0.0161 -0.0161 0.0060  125 PRO   B N   
5861 C CA  . PRO   B 125 ? 0.1456 0.1250 0.1533 -0.0105 -0.0184 0.0193  125 PRO   B CA  
5862 C C   . PRO   B 125 ? 0.1443 0.1187 0.1786 -0.0087 -0.0136 0.0075  125 PRO   B C   
5863 O O   . PRO   B 125 ? 0.1437 0.1176 0.1941 -0.0062 -0.0044 0.0090  125 PRO   B O   
5864 C CB  . PRO   B 125 ? 0.1561 0.1444 0.1697 -0.0213 -0.0170 0.0264  125 PRO   B CB  
5865 C CG  . PRO   B 125 ? 0.1648 0.1495 0.1676 -0.0324 -0.0144 0.0192  125 PRO   B CG  
5866 C CD  . PRO   B 125 ? 0.1548 0.1331 0.1443 -0.0312 -0.0110 0.0130  125 PRO   B CD  
5874 N N   . LEU   B 126 ? 0.1455 0.1195 0.1970 -0.0115 0.0071  0.0162  126 LEU   B N   
5875 C CA  . LEU   B 126 ? 0.1546 0.1290 0.2043 -0.0094 0.0169  0.0141  126 LEU   B CA  
5876 C C   . LEU   B 126 ? 0.1523 0.1304 0.1962 0.0029  0.0212  0.0146  126 LEU   B C   
5877 O O   . LEU   B 126 ? 0.1661 0.1615 0.2164 0.0212  -0.0023 -0.0027 126 LEU   B O   
5878 C CB  . LEU   B 126 ? 0.1730 0.1344 0.2221 -0.0134 0.0220  0.0071  126 LEU   B CB  
5879 C CG  . LEU   B 126 ? 0.1879 0.1398 0.2238 -0.0166 0.0183  -0.0113 126 LEU   B CG  
5880 C CD1 . LEU   B 126 ? 0.2010 0.1470 0.2642 -0.0229 0.0152  -0.0256 126 LEU   B CD1 
5881 C CD2 . LEU   B 126 ? 0.1823 0.1510 0.2199 -0.0327 0.0032  -0.0175 126 LEU   B CD2 
5893 N N   . LEU   B 127 ? 0.1480 0.1211 0.2022 0.0027  0.0132  0.0078  127 LEU   B N   
5894 C CA  . LEU   B 127 ? 0.1452 0.1334 0.1902 -0.0041 0.0160  0.0124  127 LEU   B CA  
5895 C C   . LEU   B 127 ? 0.1443 0.1292 0.1960 0.0010  0.0109  0.0152  127 LEU   B C   
5896 O O   . LEU   B 127 ? 0.1505 0.1334 0.2009 -0.0083 0.0051  0.0174  127 LEU   B O   
5897 C CB  . LEU   B 127 ? 0.1565 0.1368 0.2049 -0.0009 0.0175  0.0161  127 LEU   B CB  
5898 C CG  . LEU   B 127 ? 0.1717 0.1306 0.2157 0.0023  0.0191  0.0139  127 LEU   B CG  
5899 C CD1 . LEU   B 127 ? 0.1808 0.1263 0.2304 0.0033  0.0071  0.0058  127 LEU   B CD1 
5900 C CD2 . LEU   B 127 ? 0.1755 0.1414 0.2319 -0.0028 0.0149  0.0284  127 LEU   B CD2 
5912 N N   . SER   B 128 ? 0.1464 0.1332 0.1860 -0.0006 -0.0052 0.0135  128 SER   B N   
5913 C CA  . SER   B 128 ? 0.1574 0.1437 0.1901 0.0098  -0.0058 0.0165  128 SER   B CA  
5914 C C   . SER   B 128 ? 0.1678 0.1420 0.1998 0.0165  -0.0187 0.0187  128 SER   B C   
5915 O O   . SER   B 128 ? 0.1842 0.1421 0.2502 0.0086  -0.0205 0.0281  128 SER   B O   
5916 C CB  . SER   B 128 ? 0.1652 0.1448 0.1921 0.0094  0.0059  0.0248  128 SER   B CB  
5917 O OG  . SER   B 128 ? 0.1768 0.1547 0.2028 0.0124  0.0082  0.0299  128 SER   B OG  
5923 N N   . ALA   B 129 ? 0.1781 0.1466 0.2225 0.0264  -0.0086 0.0064  129 ALA   B N   
5924 C CA  . ALA   B 129 ? 0.1926 0.1578 0.2376 0.0283  -0.0155 -0.0068 129 ALA   B CA  
5925 C C   . ALA   B 129 ? 0.1820 0.1551 0.2164 0.0202  0.0042  0.0035  129 ALA   B C   
5926 O O   . ALA   B 129 ? 0.1686 0.1567 0.2309 0.0139  -0.0084 0.0188  129 ALA   B O   
5927 C CB  . ALA   B 129 ? 0.2144 0.1764 0.2749 0.0324  -0.0138 -0.0111 129 ALA   B CB  
5933 N N   . GLY   B 130 ? 0.1804 0.1488 0.2357 0.0258  0.0068  -0.0018 130 GLY   B N   
5934 C CA  . GLY   B 130 ? 0.1871 0.1590 0.2527 0.0214  0.0284  -0.0023 130 GLY   B CA  
5935 C C   . GLY   B 130 ? 0.1904 0.1594 0.2417 0.0185  0.0146  0.0029  130 GLY   B C   
5936 O O   . GLY   B 130 ? 0.2087 0.1696 0.2477 0.0181  0.0011  0.0122  130 GLY   B O   
5940 N N   . ILE   B 131 ? 0.1792 0.1693 0.2446 0.0345  0.0141  0.0068  131 ILE   B N   
5941 C CA  . ILE   B 131 ? 0.2018 0.1845 0.2382 0.0303  0.0003  0.0167  131 ILE   B CA  
5942 C C   . ILE   B 131 ? 0.2097 0.1763 0.2059 0.0215  -0.0031 0.0200  131 ILE   B C   
5943 O O   . ILE   B 131 ? 0.2349 0.1963 0.2250 0.0283  -0.0166 0.0210  131 ILE   B O   
5944 C CB  . ILE   B 131 ? 0.2039 0.2236 0.2681 0.0286  -0.0074 0.0236  131 ILE   B CB  
5945 C CG1 . ILE   B 131 ? 0.2092 0.2417 0.2786 0.0062  0.0024  0.0219  131 ILE   B CG1 
5946 C CG2 . ILE   B 131 ? 0.2040 0.2414 0.2890 0.0338  -0.0020 0.0212  131 ILE   B CG2 
5947 C CD1 . ILE   B 131 ? 0.2208 0.2645 0.2924 -0.0063 -0.0024 0.0222  131 ILE   B CD1 
5959 N N   . PHE   B 132 ? 0.1927 0.1557 0.1935 0.0209  0.0165  0.0185  132 PHE   B N   
5960 C CA  . PHE   B 132 ? 0.2031 0.1643 0.1966 0.0086  0.0234  0.0118  132 PHE   B CA  
5961 C C   . PHE   B 132 ? 0.2197 0.1761 0.2128 0.0091  0.0269  0.0150  132 PHE   B C   
5962 O O   . PHE   B 132 ? 0.2381 0.1996 0.2320 0.0050  0.0428  0.0204  132 PHE   B O   
5963 C CB  . PHE   B 132 ? 0.1864 0.1607 0.1866 0.0114  0.0126  0.0196  132 PHE   B CB  
5964 C CG  . PHE   B 132 ? 0.1880 0.1631 0.2028 0.0159  0.0192  0.0102  132 PHE   B CG  
5965 C CD1 . PHE   B 132 ? 0.1968 0.1611 0.2475 0.0146  0.0283  0.0182  132 PHE   B CD1 
5966 C CD2 . PHE   B 132 ? 0.1895 0.1607 0.1762 0.0216  0.0123  0.0209  132 PHE   B CD2 
5967 C CE1 . PHE   B 132 ? 0.1987 0.1658 0.2607 0.0034  0.0269  0.0257  132 PHE   B CE1 
5968 C CE2 . PHE   B 132 ? 0.1956 0.1651 0.1847 0.0163  0.0144  0.0126  132 PHE   B CE2 
5969 C CZ  . PHE   B 132 ? 0.1996 0.1680 0.2336 0.0097  0.0091  0.0304  132 PHE   B CZ  
5979 N N   . GLY   B 133 ? 0.2145 0.1609 0.2143 0.0116  0.0134  0.0305  133 GLY   B N   
5980 C CA  . GLY   B 133 ? 0.2287 0.1708 0.2161 -0.0134 0.0115  0.0354  133 GLY   B CA  
5981 C C   . GLY   B 133 ? 0.2322 0.1733 0.2191 -0.0231 0.0210  0.0343  133 GLY   B C   
5982 O O   . GLY   B 133 ? 0.2512 0.1885 0.2490 -0.0321 0.0229  0.0525  133 GLY   B O   
5986 N N   . ALA   B 134 ? 0.2178 0.1730 0.2032 -0.0229 0.0203  0.0142  134 ALA   B N   
5987 C CA  . ALA   B 134 ? 0.2147 0.1713 0.2229 -0.0186 0.0310  0.0030  134 ALA   B CA  
5988 C C   . ALA   B 134 ? 0.2165 0.1645 0.2201 -0.0098 0.0264  0.0199  134 ALA   B C   
5989 O O   . ALA   B 134 ? 0.2242 0.1811 0.2481 -0.0026 0.0264  0.0104  134 ALA   B O   
5990 C CB  . ALA   B 134 ? 0.2172 0.1644 0.2383 -0.0081 0.0317  -0.0080 134 ALA   B CB  
5996 N N   . ASP   B 135 ? 0.2249 0.1635 0.2079 -0.0067 0.0158  0.0232  135 ASP   B N   
5997 C CA  . ASP   B 135 ? 0.2382 0.1608 0.2349 -0.0021 -0.0019 0.0242  135 ASP   B CA  
5998 C C   . ASP   B 135 ? 0.2197 0.1479 0.2256 -0.0012 -0.0005 0.0187  135 ASP   B C   
5999 O O   . ASP   B 135 ? 0.2143 0.1418 0.2384 -0.0014 0.0052  0.0219  135 ASP   B O   
6000 C CB  . ASP   B 135 ? 0.2689 0.1712 0.2560 -0.0258 0.0009  0.0298  135 ASP   B CB  
6001 C CG  . ASP   B 135 ? 0.2980 0.1695 0.2970 -0.0496 -0.0021 0.0246  135 ASP   B CG  
6002 O OD1 . ASP   B 135 ? 0.3128 0.1564 0.2985 -0.0368 -0.0098 0.0217  135 ASP   B OD1 
6003 O OD2 . ASP   B 135 ? 0.3198 0.2062 0.3556 -0.0660 -0.0066 0.0085  135 ASP   B OD2 
6008 N N   . PRO   B 136 ? 0.2216 0.1556 0.2384 0.0211  -0.0171 0.0162  136 PRO   B N   
6009 C CA  . PRO   B 136 ? 0.1992 0.1421 0.2381 0.0208  -0.0167 0.0083  136 PRO   B CA  
6010 C C   . PRO   B 136 ? 0.1818 0.1318 0.2496 0.0177  -0.0073 0.0048  136 PRO   B C   
6011 O O   . PRO   B 136 ? 0.1678 0.1272 0.2439 0.0102  -0.0023 0.0131  136 PRO   B O   
6012 C CB  . PRO   B 136 ? 0.2054 0.1636 0.2488 0.0332  -0.0183 -0.0050 136 PRO   B CB  
6013 C CG  . PRO   B 136 ? 0.2246 0.1737 0.2648 0.0340  -0.0143 -0.0023 136 PRO   B CG  
6014 C CD  . PRO   B 136 ? 0.2280 0.1694 0.2521 0.0406  -0.0076 0.0019  136 PRO   B CD  
6022 N N   . ILE   B 137 ? 0.1905 0.1228 0.2575 0.0146  -0.0072 0.0032  137 ILE   B N   
6023 C CA  . ILE   B 137 ? 0.2021 0.1234 0.2718 0.0008  -0.0000 -0.0000 137 ILE   B CA  
6024 C C   . ILE   B 137 ? 0.1922 0.1327 0.2619 -0.0047 0.0129  0.0110  137 ILE   B C   
6025 O O   . ILE   B 137 ? 0.1759 0.1371 0.2557 -0.0066 0.0107  0.0088  137 ILE   B O   
6026 C CB  . ILE   B 137 ? 0.2249 0.1295 0.3068 0.0009  -0.0068 0.0048  137 ILE   B CB  
6027 C CG1 . ILE   B 137 ? 0.2507 0.1479 0.3604 0.0038  -0.0027 -0.0060 137 ILE   B CG1 
6028 C CG2 . ILE   B 137 ? 0.2294 0.1416 0.3098 -0.0173 -0.0117 0.0088  137 ILE   B CG2 
6029 C CD1 . ILE   B 137 ? 0.2761 0.1774 0.4048 0.0168  -0.0132 0.0031  137 ILE   B CD1 
6041 N N   . HIS   B 138 ? 0.1933 0.1266 0.2545 -0.0064 0.0201  0.0130  138 HIS   B N   
6042 C CA  . HIS   B 138 ? 0.2019 0.1375 0.2441 -0.0027 0.0327  0.0170  138 HIS   B CA  
6043 C C   . HIS   B 138 ? 0.1869 0.1374 0.2305 -0.0026 0.0323  0.0223  138 HIS   B C   
6044 O O   . HIS   B 138 ? 0.1783 0.1406 0.2555 0.0061  0.0269  0.0312  138 HIS   B O   
6045 C CB  . HIS   B 138 ? 0.2188 0.1556 0.2573 -0.0011 0.0437  0.0111  138 HIS   B CB  
6046 C CG  . HIS   B 138 ? 0.2276 0.1682 0.2566 -0.0000 0.0445  0.0249  138 HIS   B CG  
6047 N ND1 . HIS   B 138 ? 0.2323 0.1835 0.2834 -0.0058 0.0559  0.0177  138 HIS   B ND1 
6048 C CD2 . HIS   B 138 ? 0.2385 0.1787 0.2569 -0.0092 0.0454  0.0135  138 HIS   B CD2 
6049 C CE1 . HIS   B 138 ? 0.2362 0.1880 0.2789 -0.0028 0.0533  0.0174  138 HIS   B CE1 
6050 N NE2 . HIS   B 138 ? 0.2450 0.1762 0.2656 0.0048  0.0514  0.0101  138 HIS   B NE2 
6058 N N   . SER   B 139 ? 0.1818 0.1311 0.2337 0.0045  0.0219  0.0102  139 SER   B N   
6059 C CA  . SER   B 139 ? 0.1782 0.1190 0.2221 -0.0017 0.0169  -0.0024 139 SER   B CA  
6060 C C   . SER   B 139 ? 0.1530 0.1135 0.2156 -0.0087 0.0130  -0.0018 139 SER   B C   
6061 O O   . SER   B 139 ? 0.1546 0.1174 0.2208 -0.0020 0.0088  0.0104  139 SER   B O   
6062 C CB  . SER   B 139 ? 0.1840 0.1201 0.2261 0.0042  0.0056  -0.0013 139 SER   B CB  
6063 O OG  . SER   B 139 ? 0.1824 0.1274 0.2280 -0.0012 -0.0142 0.0086  139 SER   B OG  
6069 N N   . LEU   B 140 ? 0.1555 0.1124 0.2105 -0.0053 0.0071  -0.0041 140 LEU   B N   
6070 C CA  . LEU   B 140 ? 0.1476 0.1193 0.2225 -0.0023 0.0086  0.0029  140 LEU   B CA  
6071 C C   . LEU   B 140 ? 0.1424 0.1191 0.2307 -0.0067 0.0064  -0.0006 140 LEU   B C   
6072 O O   . LEU   B 140 ? 0.1448 0.1233 0.2253 -0.0003 -0.0016 0.0048  140 LEU   B O   
6073 C CB  . LEU   B 140 ? 0.1437 0.1248 0.2333 -0.0066 0.0160  -0.0066 140 LEU   B CB  
6074 C CG  . LEU   B 140 ? 0.1579 0.1251 0.2269 -0.0090 0.0010  0.0076  140 LEU   B CG  
6075 C CD1 . LEU   B 140 ? 0.1723 0.1352 0.2390 -0.0081 0.0081  0.0088  140 LEU   B CD1 
6076 C CD2 . LEU   B 140 ? 0.1739 0.1338 0.2405 -0.0020 -0.0102 -0.0097 140 LEU   B CD2 
6088 N N   . ARG   B 141 ? 0.1376 0.1210 0.2415 -0.0093 0.0076  -0.0016 141 ARG   B N   
6089 C CA  . ARG   B 141 ? 0.1458 0.1176 0.2860 -0.0103 0.0244  0.0027  141 ARG   B CA  
6090 C C   . ARG   B 141 ? 0.1379 0.1251 0.2563 -0.0148 0.0119  0.0048  141 ARG   B C   
6091 O O   . ARG   B 141 ? 0.1459 0.1265 0.2523 -0.0158 0.0005  -0.0071 141 ARG   B O   
6092 C CB  . ARG   B 141 ? 0.1626 0.1313 0.3270 -0.0177 0.0466  -0.0034 141 ARG   B CB  
6093 C CG  . ARG   B 141 ? 0.1999 0.1469 0.3714 -0.0286 0.0480  0.0072  141 ARG   B CG  
6094 C CD  . ARG   B 141 ? 0.2456 0.1765 0.3866 -0.0256 0.0327  -0.0067 141 ARG   B CD  
6095 N NE  . ARG   B 141 ? 0.2652 0.1824 0.3781 -0.0434 0.0435  -0.0162 141 ARG   B NE  
6096 C CZ  . ARG   B 141 ? 0.2908 0.1636 0.3672 -0.0442 0.0633  -0.0266 141 ARG   B CZ  
6097 N NH1 . ARG   B 141 ? 0.3041 0.1585 0.3731 -0.0434 0.0563  -0.0338 141 ARG   B NH1 
6098 N NH2 . ARG   B 141 ? 0.2888 0.1790 0.3706 -0.0260 0.0623  -0.0177 141 ARG   B NH2 
6112 N N   . VAL   B 142 ? 0.1393 0.1184 0.2399 -0.0074 0.0125  -0.0034 142 VAL   B N   
6113 C CA  . VAL   B 142 ? 0.1397 0.1233 0.2414 -0.0045 0.0107  -0.0030 142 VAL   B CA  
6114 C C   . VAL   B 142 ? 0.1430 0.1198 0.2384 -0.0033 0.0114  -0.0046 142 VAL   B C   
6115 O O   . VAL   B 142 ? 0.1508 0.1162 0.2507 0.0033  0.0040  -0.0023 142 VAL   B O   
6116 C CB  . VAL   B 142 ? 0.1518 0.1381 0.2388 0.0023  0.0172  0.0131  142 VAL   B CB  
6117 C CG1 . VAL   B 142 ? 0.1514 0.1293 0.2463 0.0068  0.0136  0.0070  142 VAL   B CG1 
6118 C CG2 . VAL   B 142 ? 0.1766 0.1391 0.2440 0.0017  0.0128  0.0103  142 VAL   B CG2 
6128 N N   . CYS   B 143 ? 0.1377 0.1166 0.2213 -0.0072 0.0043  -0.0031 143 CYS   B N   
6129 C CA  . CYS   B 143 ? 0.1333 0.1174 0.2203 -0.0071 0.0030  -0.0020 143 CYS   B CA  
6130 C C   . CYS   B 143 ? 0.1287 0.1225 0.2256 -0.0090 0.0048  -0.0037 143 CYS   B C   
6131 O O   . CYS   B 143 ? 0.1413 0.1277 0.2178 -0.0057 -0.0029 0.0026  143 CYS   B O   
6132 C CB  . CYS   B 143 ? 0.1374 0.1306 0.2219 -0.0055 0.0006  -0.0049 143 CYS   B CB  
6133 S SG  . CYS   B 143 ? 0.1430 0.1445 0.2179 -0.0046 0.0042  0.0043  143 CYS   B SG  
6139 N N   . VAL   B 144 ? 0.1375 0.1243 0.2403 -0.0066 -0.0039 -0.0153 144 VAL   B N   
6140 C CA  . VAL   B 144 ? 0.1446 0.1325 0.2609 -0.0153 -0.0056 -0.0246 144 VAL   B CA  
6141 C C   . VAL   B 144 ? 0.1343 0.1365 0.2571 -0.0086 -0.0100 -0.0066 144 VAL   B C   
6142 O O   . VAL   B 144 ? 0.1504 0.1565 0.2697 -0.0002 -0.0125 0.0120  144 VAL   B O   
6143 C CB  . VAL   B 144 ? 0.1718 0.1469 0.3313 -0.0085 -0.0089 -0.0360 144 VAL   B CB  
6144 C CG1 . VAL   B 144 ? 0.2000 0.1884 0.3673 -0.0094 -0.0214 -0.0297 144 VAL   B CG1 
6145 C CG2 . VAL   B 144 ? 0.1854 0.1503 0.3314 -0.0027 -0.0194 -0.0459 144 VAL   B CG2 
6155 N N   . ASP   B 145 ? 0.1372 0.1311 0.2660 -0.0067 -0.0118 -0.0128 145 ASP   B N   
6156 C CA  . ASP   B 145 ? 0.1367 0.1347 0.2804 -0.0066 0.0026  -0.0141 145 ASP   B CA  
6157 C C   . ASP   B 145 ? 0.1369 0.1428 0.2677 -0.0058 0.0087  -0.0091 145 ASP   B C   
6158 O O   . ASP   B 145 ? 0.1325 0.1560 0.3222 -0.0080 0.0072  -0.0334 145 ASP   B O   
6159 C CB  . ASP   B 145 ? 0.1526 0.1448 0.3148 -0.0129 0.0119  -0.0088 145 ASP   B CB  
6160 C CG  . ASP   B 145 ? 0.1717 0.1444 0.3542 -0.0195 0.0200  -0.0100 145 ASP   B CG  
6161 O OD1 . ASP   B 145 ? 0.1784 0.1435 0.3651 -0.0261 -0.0079 -0.0224 145 ASP   B OD1 
6162 O OD2 . ASP   B 145 ? 0.2028 0.1586 0.4032 -0.0227 0.0455  -0.0004 145 ASP   B OD2 
6167 N N   . THR   B 146 ? 0.1312 0.1306 0.2241 -0.0072 0.0068  -0.0067 146 THR   B N   
6168 C CA  . THR   B 146 ? 0.1408 0.1247 0.2131 -0.0042 0.0063  -0.0030 146 THR   B CA  
6169 C C   . THR   B 146 ? 0.1405 0.1250 0.2054 -0.0023 0.0011  0.0043  146 THR   B C   
6170 O O   . THR   B 146 ? 0.1464 0.1243 0.2207 -0.0034 -0.0118 0.0031  146 THR   B O   
6171 C CB  . THR   B 146 ? 0.1422 0.1241 0.2223 0.0018  0.0134  -0.0016 146 THR   B CB  
6172 O OG1 . THR   B 146 ? 0.1456 0.1230 0.2275 -0.0064 0.0094  0.0107  146 THR   B OG1 
6173 C CG2 . THR   B 146 ? 0.1672 0.1235 0.2108 -0.0035 0.0058  -0.0019 146 THR   B CG2 
6181 N N   . VAL   B 147 ? 0.1423 0.1300 0.2007 -0.0034 0.0114  0.0024  147 VAL   B N   
6182 C CA  . VAL   B 147 ? 0.1421 0.1242 0.1983 -0.0098 -0.0024 0.0019  147 VAL   B CA  
6183 C C   . VAL   B 147 ? 0.1346 0.1220 0.2068 -0.0158 -0.0135 -0.0126 147 VAL   B C   
6184 O O   . VAL   B 147 ? 0.1478 0.1380 0.2187 -0.0181 -0.0370 -0.0080 147 VAL   B O   
6185 C CB  . VAL   B 147 ? 0.1403 0.1384 0.1905 -0.0030 -0.0040 0.0054  147 VAL   B CB  
6186 C CG1 . VAL   B 147 ? 0.1363 0.1546 0.1831 -0.0049 -0.0061 0.0004  147 VAL   B CG1 
6187 C CG2 . VAL   B 147 ? 0.1487 0.1354 0.1934 -0.0070 -0.0040 -0.0002 147 VAL   B CG2 
6197 N N   . ARG   B 148 ? 0.1411 0.1246 0.2011 -0.0081 -0.0163 -0.0085 148 ARG   B N   
6198 C CA  . ARG   B 148 ? 0.1505 0.1340 0.2037 -0.0044 -0.0238 -0.0137 148 ARG   B CA  
6199 C C   . ARG   B 148 ? 0.1547 0.1469 0.1906 -0.0101 -0.0288 -0.0048 148 ARG   B C   
6200 O O   . ARG   B 148 ? 0.1750 0.1715 0.1929 -0.0274 -0.0384 0.0015  148 ARG   B O   
6201 C CB  . ARG   B 148 ? 0.1550 0.1451 0.2103 -0.0034 -0.0317 -0.0214 148 ARG   B CB  
6202 C CG  . ARG   B 148 ? 0.1545 0.1590 0.2199 -0.0080 -0.0237 -0.0331 148 ARG   B CG  
6203 C CD  . ARG   B 148 ? 0.1578 0.1697 0.2224 0.0088  -0.0277 -0.0303 148 ARG   B CD  
6204 N NE  . ARG   B 148 ? 0.1605 0.1673 0.2099 0.0220  -0.0281 -0.0283 148 ARG   B NE  
6205 C CZ  . ARG   B 148 ? 0.1538 0.1613 0.1927 0.0117  -0.0235 -0.0202 148 ARG   B CZ  
6206 N NH1 . ARG   B 148 ? 0.1493 0.1606 0.2032 -0.0054 -0.0147 -0.0198 148 ARG   B NH1 
6207 N NH2 . ARG   B 148 ? 0.1769 0.1502 0.1955 0.0173  -0.0249 -0.0095 148 ARG   B NH2 
6221 N N   . THR   B 149 ? 0.1513 0.1385 0.1914 -0.0103 -0.0207 -0.0053 149 THR   B N   
6222 C CA  . THR   B 149 ? 0.1563 0.1363 0.1908 -0.0126 -0.0251 0.0030  149 THR   B CA  
6223 C C   . THR   B 149 ? 0.1534 0.1344 0.1839 -0.0128 -0.0253 0.0013  149 THR   B C   
6224 O O   . THR   B 149 ? 0.1603 0.1378 0.1868 -0.0210 -0.0111 -0.0035 149 THR   B O   
6225 C CB  . THR   B 149 ? 0.1634 0.1346 0.1833 -0.0167 -0.0245 -0.0047 149 THR   B CB  
6226 O OG1 . THR   B 149 ? 0.1642 0.1440 0.1743 -0.0214 -0.0301 -0.0011 149 THR   B OG1 
6227 C CG2 . THR   B 149 ? 0.1738 0.1389 0.2101 -0.0048 -0.0171 -0.0037 149 THR   B CG2 
6235 N N   . ASN   B 150 ? 0.1611 0.1349 0.1870 -0.0151 -0.0308 0.0027  150 ASN   B N   
6236 C CA  . ASN   B 150 ? 0.1685 0.1514 0.1801 -0.0131 -0.0255 -0.0023 150 ASN   B CA  
6237 C C   . ASN   B 150 ? 0.1563 0.1486 0.1854 -0.0107 -0.0262 -0.0007 150 ASN   B C   
6238 O O   . ASN   B 150 ? 0.1684 0.1460 0.1934 -0.0229 -0.0436 -0.0049 150 ASN   B O   
6239 C CB  . ASN   B 150 ? 0.1901 0.1860 0.2010 -0.0142 -0.0385 0.0077  150 ASN   B CB  
6240 C CG  . ASN   B 150 ? 0.2119 0.2258 0.2244 -0.0185 -0.0414 0.0274  150 ASN   B CG  
6241 O OD1 . ASN   B 150 ? 0.2260 0.2466 0.2302 -0.0289 -0.0582 0.0250  150 ASN   B OD1 
6242 N ND2 . ASN   B 150 ? 0.2223 0.2451 0.2432 -0.0109 -0.0442 0.0581  150 ASN   B ND2 
6249 N N   . VAL   B 151 ? 0.1486 0.1455 0.1765 -0.0159 -0.0305 0.0049  151 VAL   B N   
6250 C CA  . VAL   B 151 ? 0.1535 0.1450 0.1738 -0.0183 -0.0264 -0.0021 151 VAL   B CA  
6251 C C   . VAL   B 151 ? 0.1573 0.1389 0.1661 -0.0287 -0.0365 -0.0047 151 VAL   B C   
6252 O O   . VAL   B 151 ? 0.1673 0.1478 0.1905 -0.0266 -0.0194 -0.0131 151 VAL   B O   
6253 C CB  . VAL   B 151 ? 0.1744 0.1642 0.1854 -0.0031 -0.0211 -0.0047 151 VAL   B CB  
6254 C CG1 . VAL   B 151 ? 0.1781 0.1579 0.2108 -0.0149 -0.0075 -0.0209 151 VAL   B CG1 
6255 C CG2 . VAL   B 151 ? 0.1871 0.1813 0.1734 0.0058  -0.0228 0.0034  151 VAL   B CG2 
6265 N N   . TYR   B 152 ? 0.1488 0.1248 0.1742 -0.0210 -0.0214 -0.0056 152 TYR   B N   
6266 C CA  . TYR   B 152 ? 0.1500 0.1393 0.1644 -0.0253 -0.0137 -0.0064 152 TYR   B CA  
6267 C C   . TYR   B 152 ? 0.1476 0.1323 0.1518 -0.0180 -0.0146 -0.0040 152 TYR   B C   
6268 O O   . TYR   B 152 ? 0.1548 0.1342 0.1623 -0.0231 -0.0140 0.0016  152 TYR   B O   
6269 C CB  . TYR   B 152 ? 0.1611 0.1533 0.1616 -0.0275 -0.0103 0.0040  152 TYR   B CB  
6270 C CG  . TYR   B 152 ? 0.1785 0.1600 0.1594 -0.0351 -0.0168 0.0052  152 TYR   B CG  
6271 C CD1 . TYR   B 152 ? 0.1874 0.1722 0.1547 -0.0247 -0.0239 0.0078  152 TYR   B CD1 
6272 C CD2 . TYR   B 152 ? 0.1970 0.1746 0.1664 -0.0314 -0.0133 0.0019  152 TYR   B CD2 
6273 C CE1 . TYR   B 152 ? 0.2033 0.1875 0.1656 -0.0205 -0.0235 0.0213  152 TYR   B CE1 
6274 C CE2 . TYR   B 152 ? 0.2064 0.1950 0.1720 -0.0299 -0.0198 -0.0014 152 TYR   B CE2 
6275 C CZ  . TYR   B 152 ? 0.2091 0.2055 0.1605 -0.0284 -0.0489 0.0171  152 TYR   B CZ  
6276 O OH  . TYR   B 152 ? 0.2334 0.2405 0.2044 -0.0122 -0.0419 0.0227  152 TYR   B OH  
6286 N N   . LEU   B 153 ? 0.1516 0.1311 0.1635 -0.0216 -0.0170 -0.0037 153 LEU   B N   
6287 C CA  . LEU   B 153 ? 0.1560 0.1287 0.1497 -0.0199 -0.0066 -0.0116 153 LEU   B CA  
6288 C C   . LEU   B 153 ? 0.1522 0.1238 0.1644 -0.0201 -0.0073 -0.0174 153 LEU   B C   
6289 O O   . LEU   B 153 ? 0.1617 0.1448 0.1718 -0.0114 -0.0137 -0.0308 153 LEU   B O   
6290 C CB  . LEU   B 153 ? 0.1572 0.1302 0.1647 -0.0260 0.0016  -0.0102 153 LEU   B CB  
6291 C CG  . LEU   B 153 ? 0.1484 0.1419 0.1855 -0.0242 0.0004  -0.0030 153 LEU   B CG  
6292 C CD1 . LEU   B 153 ? 0.1602 0.1620 0.1901 -0.0293 -0.0002 0.0029  153 LEU   B CD1 
6293 C CD2 . LEU   B 153 ? 0.1505 0.1544 0.1897 -0.0223 0.0072  -0.0020 153 LEU   B CD2 
6305 N N   . ALA   B 154 ? 0.1500 0.1268 0.1712 -0.0086 -0.0132 -0.0102 154 ALA   B N   
6306 C CA  . ALA   B 154 ? 0.1626 0.1351 0.1892 0.0004  -0.0169 -0.0194 154 ALA   B CA  
6307 C C   . ALA   B 154 ? 0.1712 0.1418 0.1852 0.0058  -0.0227 -0.0270 154 ALA   B C   
6308 O O   . ALA   B 154 ? 0.2008 0.1442 0.2035 0.0062  -0.0172 -0.0129 154 ALA   B O   
6309 C CB  . ALA   B 154 ? 0.1527 0.1522 0.2263 -0.0018 -0.0060 -0.0262 154 ALA   B CB  
6315 N N   . VAL   B 155 ? 0.1421 0.1301 0.1966 0.0019  -0.0033 -0.0123 155 VAL   B N   
6316 C CA  . VAL   B 155 ? 0.1363 0.1344 0.2048 0.0006  -0.0173 -0.0037 155 VAL   B CA  
6317 C C   . VAL   B 155 ? 0.1392 0.1371 0.1996 -0.0009 -0.0112 -0.0165 155 VAL   B C   
6318 O O   . VAL   B 155 ? 0.1582 0.1491 0.2242 0.0005  -0.0154 -0.0272 155 VAL   B O   
6319 C CB  . VAL   B 155 ? 0.1418 0.1498 0.2481 -0.0053 -0.0142 0.0083  155 VAL   B CB  
6320 C CG1 . VAL   B 155 ? 0.1471 0.1459 0.2494 -0.0087 -0.0079 0.0068  155 VAL   B CG1 
6321 C CG2 . VAL   B 155 ? 0.1413 0.1650 0.2826 -0.0004 -0.0161 0.0289  155 VAL   B CG2 
6331 N N   . PHE   B 156 ? 0.1329 0.1393 0.2275 0.0048  0.0024  -0.0137 156 PHE   B N   
6332 C CA  . PHE   B 156 ? 0.1392 0.1501 0.2584 0.0052  -0.0099 -0.0128 156 PHE   B CA  
6333 C C   . PHE   B 156 ? 0.1338 0.1601 0.2747 0.0111  -0.0116 -0.0296 156 PHE   B C   
6334 O O   . PHE   B 156 ? 0.1595 0.1763 0.2954 0.0216  0.0006  -0.0300 156 PHE   B O   
6335 C CB  . PHE   B 156 ? 0.1450 0.1429 0.2671 0.0010  -0.0226 -0.0007 156 PHE   B CB  
6336 C CG  . PHE   B 156 ? 0.1458 0.1506 0.2872 -0.0029 -0.0224 0.0063  156 PHE   B CG  
6337 C CD1 . PHE   B 156 ? 0.1536 0.1789 0.3180 0.0049  -0.0171 0.0437  156 PHE   B CD1 
6338 C CD2 . PHE   B 156 ? 0.1506 0.1629 0.2724 0.0047  -0.0335 0.0100  156 PHE   B CD2 
6339 C CE1 . PHE   B 156 ? 0.1604 0.1959 0.3319 0.0036  -0.0125 0.0486  156 PHE   B CE1 
6340 C CE2 . PHE   B 156 ? 0.1629 0.1861 0.2946 0.0080  -0.0294 0.0181  156 PHE   B CE2 
6341 C CZ  . PHE   B 156 ? 0.1626 0.1947 0.3188 0.0124  -0.0240 0.0333  156 PHE   B CZ  
6351 N N   . ASP   B 157 ? 0.1332 0.1452 0.2958 0.0128  -0.0217 -0.0177 157 ASP   B N   
6352 C CA  . ASP   B 157 ? 0.1453 0.1459 0.3300 0.0053  -0.0215 -0.0235 157 ASP   B CA  
6353 C C   . ASP   B 157 ? 0.1492 0.1450 0.3387 0.0047  -0.0229 -0.0376 157 ASP   B C   
6354 O O   . ASP   B 157 ? 0.1393 0.1432 0.3247 0.0019  -0.0225 -0.0344 157 ASP   B O   
6355 C CB  . ASP   B 157 ? 0.1651 0.1648 0.3500 0.0047  -0.0360 -0.0131 157 ASP   B CB  
6356 C CG  . ASP   B 157 ? 0.2048 0.1770 0.3772 0.0020  -0.0288 -0.0124 157 ASP   B CG  
6357 O OD1 . ASP   B 157 ? 0.2125 0.1654 0.3983 0.0071  -0.0289 -0.0051 157 ASP   B OD1 
6358 O OD2 . ASP   B 157 ? 0.2425 0.1893 0.4021 -0.0017 -0.0094 -0.0124 157 ASP   B OD2 
6363 N N   . LYS   B 158 ? 0.1515 0.1726 0.3530 0.0031  -0.0075 -0.0607 158 LYS   B N   
6364 C CA  . LYS   B 158 ? 0.1639 0.1858 0.3570 0.0032  0.0015  -0.0746 158 LYS   B CA  
6365 C C   . LYS   B 158 ? 0.1632 0.1706 0.3556 0.0081  -0.0058 -0.0666 158 LYS   B C   
6366 O O   . LYS   B 158 ? 0.1682 0.1733 0.3593 -0.0026 -0.0064 -0.0743 158 LYS   B O   
6367 C CB  . LYS   B 158 ? 0.1890 0.2299 0.3692 0.0015  0.0148  -0.0989 158 LYS   B CB  
6368 C CG  . LYS   B 158 ? 0.2188 0.2720 0.3813 0.0103  0.0267  -0.1110 158 LYS   B CG  
6369 C CD  . LYS   B 158 ? 0.2399 0.3164 0.4038 0.0091  0.0344  -0.1098 158 LYS   B CD  
6370 C CE  . LYS   B 158 ? 0.2613 0.3522 0.4241 0.0104  0.0364  -0.1065 158 LYS   B CE  
6371 N NZ  . LYS   B 158 ? 0.2418 0.3558 0.4217 0.0096  0.0472  -0.1096 158 LYS   B NZ  
6385 N N   . ASN   B 159 ? 0.1661 0.1589 0.3747 0.0052  -0.0224 -0.0552 159 ASN   B N   
6386 C CA  . ASN   B 159 ? 0.1818 0.1547 0.3948 0.0164  -0.0388 -0.0355 159 ASN   B CA  
6387 C C   . ASN   B 159 ? 0.1640 0.1447 0.3775 0.0187  -0.0405 -0.0268 159 ASN   B C   
6388 O O   . ASN   B 159 ? 0.1651 0.1400 0.3828 -0.0000 -0.0337 -0.0242 159 ASN   B O   
6389 C CB  . ASN   B 159 ? 0.2015 0.1630 0.4304 0.0199  -0.0439 -0.0295 159 ASN   B CB  
6390 C CG  . ASN   B 159 ? 0.2292 0.1831 0.4692 0.0186  -0.0564 -0.0435 159 ASN   B CG  
6391 O OD1 . ASN   B 159 ? 0.2510 0.1996 0.4826 0.0295  -0.0531 -0.0544 159 ASN   B OD1 
6392 N ND2 . ASN   B 159 ? 0.2301 0.1908 0.4876 0.0269  -0.0610 -0.0413 159 ASN   B ND2 
6399 N N   . LEU   B 160 ? 0.1575 0.1403 0.3565 0.0091  -0.0396 -0.0251 160 LEU   B N   
6400 C CA  . LEU   B 160 ? 0.1567 0.1489 0.3147 0.0106  -0.0290 -0.0157 160 LEU   B CA  
6401 C C   . LEU   B 160 ? 0.1488 0.1421 0.2939 -0.0012 -0.0258 -0.0229 160 LEU   B C   
6402 O O   . LEU   B 160 ? 0.1388 0.1422 0.2932 -0.0044 -0.0232 -0.0118 160 LEU   B O   
6403 C CB  . LEU   B 160 ? 0.1563 0.1576 0.2938 0.0119  -0.0295 -0.0122 160 LEU   B CB  
6404 C CG  . LEU   B 160 ? 0.1528 0.1730 0.2726 0.0125  -0.0301 -0.0008 160 LEU   B CG  
6405 C CD1 . LEU   B 160 ? 0.1610 0.1879 0.2772 0.0014  -0.0138 -0.0005 160 LEU   B CD1 
6406 C CD2 . LEU   B 160 ? 0.1571 0.1734 0.2740 0.0118  -0.0361 -0.0155 160 LEU   B CD2 
6418 N N   . TYR   B 161 ? 0.1430 0.1521 0.2953 -0.0027 -0.0089 -0.0269 161 TYR   B N   
6419 C CA  . TYR   B 161 ? 0.1520 0.1513 0.2841 -0.0098 0.0089  -0.0463 161 TYR   B CA  
6420 C C   . TYR   B 161 ? 0.1588 0.1503 0.2783 -0.0107 0.0099  -0.0362 161 TYR   B C   
6421 O O   . TYR   B 161 ? 0.1653 0.1491 0.2658 -0.0136 -0.0001 -0.0303 161 TYR   B O   
6422 C CB  . TYR   B 161 ? 0.1620 0.1584 0.2833 -0.0139 0.0209  -0.0428 161 TYR   B CB  
6423 C CG  . TYR   B 161 ? 0.1829 0.1615 0.2797 -0.0150 0.0246  -0.0477 161 TYR   B CG  
6424 C CD1 . TYR   B 161 ? 0.1867 0.1559 0.2755 -0.0316 0.0232  -0.0440 161 TYR   B CD1 
6425 C CD2 . TYR   B 161 ? 0.2023 0.1655 0.2816 -0.0123 0.0253  -0.0416 161 TYR   B CD2 
6426 C CE1 . TYR   B 161 ? 0.2020 0.1704 0.2817 -0.0333 0.0253  -0.0443 161 TYR   B CE1 
6427 C CE2 . TYR   B 161 ? 0.2221 0.1817 0.2882 -0.0233 0.0311  -0.0347 161 TYR   B CE2 
6428 C CZ  . TYR   B 161 ? 0.2180 0.1813 0.2779 -0.0341 0.0305  -0.0319 161 TYR   B CZ  
6429 O OH  . TYR   B 161 ? 0.2456 0.2046 0.2951 -0.0381 0.0271  -0.0336 161 TYR   B OH  
6439 N N   . ASP   B 162 ? 0.1614 0.1470 0.2982 -0.0079 0.0016  -0.0454 162 ASP   B N   
6440 C CA  . ASP   B 162 ? 0.1706 0.1526 0.2937 -0.0048 -0.0032 -0.0468 162 ASP   B CA  
6441 C C   . ASP   B 162 ? 0.1656 0.1396 0.2846 -0.0103 -0.0084 -0.0492 162 ASP   B C   
6442 O O   . ASP   B 162 ? 0.1724 0.1502 0.2837 -0.0140 -0.0230 -0.0376 162 ASP   B O   
6443 C CB  . ASP   B 162 ? 0.1903 0.1720 0.3208 0.0053  -0.0010 -0.0557 162 ASP   B CB  
6444 C CG  . ASP   B 162 ? 0.1928 0.1933 0.3400 0.0071  -0.0104 -0.0763 162 ASP   B CG  
6445 O OD1 . ASP   B 162 ? 0.1891 0.2084 0.3238 0.0083  -0.0084 -0.0766 162 ASP   B OD1 
6446 O OD2 . ASP   B 162 ? 0.2072 0.2180 0.3735 0.0220  0.0048  -0.0742 162 ASP   B OD2 
6451 N N   . LYS   B 163 ? 0.1613 0.1286 0.2810 -0.0155 -0.0218 -0.0229 163 LYS   B N   
6452 C CA  . LYS   B 163 ? 0.1750 0.1392 0.2842 -0.0170 -0.0193 -0.0060 163 LYS   B CA  
6453 C C   . LYS   B 163 ? 0.1497 0.1357 0.2739 -0.0111 -0.0167 -0.0074 163 LYS   B C   
6454 O O   . LYS   B 163 ? 0.1484 0.1440 0.3068 -0.0195 -0.0142 -0.0051 163 LYS   B O   
6455 C CB  . LYS   B 163 ? 0.2277 0.1809 0.3324 -0.0075 -0.0265 0.0098  163 LYS   B CB  
6456 C CG  . LYS   B 163 ? 0.3101 0.2690 0.4083 -0.0074 -0.0160 0.0221  163 LYS   B CG  
6457 C CD  . LYS   B 163 ? 0.3756 0.3464 0.4871 -0.0135 -0.0105 0.0211  163 LYS   B CD  
6458 C CE  . LYS   B 163 ? 0.4458 0.3981 0.5405 -0.0203 -0.0033 0.0237  163 LYS   B CE  
6459 N NZ  . LYS   B 163 ? 0.4667 0.4667 0.5729 -0.0239 0.0000  0.0219  163 LYS   B NZ  
6473 N N   . LEU   B 164 ? 0.1427 0.1268 0.2490 -0.0142 -0.0133 -0.0062 164 LEU   B N   
6474 C CA  . LEU   B 164 ? 0.1400 0.1296 0.2468 -0.0064 -0.0199 -0.0090 164 LEU   B CA  
6475 C C   . LEU   B 164 ? 0.1463 0.1338 0.2513 -0.0119 -0.0239 -0.0048 164 LEU   B C   
6476 O O   . LEU   B 164 ? 0.1461 0.1537 0.2630 -0.0139 -0.0250 -0.0022 164 LEU   B O   
6477 C CB  . LEU   B 164 ? 0.1403 0.1291 0.2450 -0.0042 -0.0183 -0.0037 164 LEU   B CB  
6478 C CG  . LEU   B 164 ? 0.1451 0.1507 0.2478 -0.0058 -0.0127 -0.0026 164 LEU   B CG  
6479 C CD1 . LEU   B 164 ? 0.1551 0.1528 0.2487 -0.0174 -0.0305 -0.0031 164 LEU   B CD1 
6480 C CD2 . LEU   B 164 ? 0.1665 0.1827 0.2547 -0.0062 0.0086  -0.0198 164 LEU   B CD2 
6492 N N   . VAL   B 165 ? 0.1698 0.1422 0.2577 -0.0160 -0.0282 -0.0173 165 VAL   B N   
6493 C CA  . VAL   B 165 ? 0.1956 0.1436 0.2580 -0.0244 -0.0424 -0.0111 165 VAL   B CA  
6494 C C   . VAL   B 165 ? 0.2285 0.1595 0.2861 -0.0316 -0.0677 -0.0159 165 VAL   B C   
6495 O O   . VAL   B 165 ? 0.2423 0.1696 0.2856 -0.0391 -0.0665 -0.0030 165 VAL   B O   
6496 C CB  . VAL   B 165 ? 0.2185 0.1681 0.2610 -0.0068 -0.0191 -0.0188 165 VAL   B CB  
6497 C CG1 . VAL   B 165 ? 0.2331 0.1739 0.2845 -0.0044 -0.0085 -0.0117 165 VAL   B CG1 
6498 C CG2 . VAL   B 165 ? 0.2174 0.1775 0.2742 -0.0076 -0.0139 -0.0112 165 VAL   B CG2 
6508 N N   . SER   B 166 ? 0.2359 0.1498 0.3139 -0.0274 -0.0784 -0.0352 166 SER   B N   
6509 C CA  . SER   B 166 ? 0.2307 0.1571 0.3636 -0.0326 -0.0634 -0.0363 166 SER   B CA  
6510 C C   . SER   B 166 ? 0.2175 0.1620 0.3811 -0.0346 -0.0633 -0.0127 166 SER   B C   
6511 O O   . SER   B 166 ? 0.2190 0.1829 0.4057 -0.0488 -0.0834 -0.0283 166 SER   B O   
6512 C CB  . SER   B 166 ? 0.2317 0.1642 0.3915 -0.0210 -0.0469 -0.0403 166 SER   B CB  
6513 O OG  . SER   B 166 ? 0.2224 0.1592 0.4005 -0.0170 -0.0441 -0.0264 166 SER   B OG  
6519 N N   . SER   B 167 ? 0.2030 0.1590 0.3525 -0.0328 -0.0649 0.0158  167 SER   B N   
6520 C CA  . SER   B 167 ? 0.1945 0.1633 0.3381 -0.0241 -0.0522 0.0111  167 SER   B CA  
6521 C C   . SER   B 167 ? 0.1882 0.1698 0.3227 -0.0327 -0.0492 0.0258  167 SER   B C   
6522 O O   . SER   B 167 ? 0.1898 0.1800 0.3283 -0.0358 -0.0441 0.0266  167 SER   B O   
6523 C CB  . SER   B 167 ? 0.1866 0.1728 0.3373 -0.0280 -0.0254 0.0117  167 SER   B CB  
6524 O OG  . SER   B 167 ? 0.1829 0.1761 0.3263 -0.0156 -0.0134 0.0071  167 SER   B OG  
6530 N N   . PHE   B 168 ? 0.1886 0.1652 0.3166 -0.0315 -0.0288 0.0341  168 PHE   B N   
6531 C CA  . PHE   B 168 ? 0.1958 0.1613 0.2933 -0.0399 -0.0334 0.0237  168 PHE   B CA  
6532 C C   . PHE   B 168 ? 0.1731 0.1487 0.2547 -0.0238 -0.0119 0.0101  168 PHE   B C   
6533 O O   . PHE   B 168 ? 0.2040 0.1438 0.2630 -0.0013 -0.0197 -0.0026 168 PHE   B O   
6534 C CB  . PHE   B 168 ? 0.2117 0.1691 0.2950 -0.0470 -0.0498 0.0370  168 PHE   B CB  
6535 C CG  . PHE   B 168 ? 0.2408 0.1545 0.2832 -0.0454 -0.0519 0.0202  168 PHE   B CG  
6536 C CD1 . PHE   B 168 ? 0.2740 0.1619 0.2943 -0.0373 -0.0617 0.0173  168 PHE   B CD1 
6537 C CD2 . PHE   B 168 ? 0.2255 0.1431 0.2823 -0.0422 -0.0528 0.0157  168 PHE   B CD2 
6538 C CE1 . PHE   B 168 ? 0.2872 0.1723 0.2974 -0.0225 -0.0621 0.0155  168 PHE   B CE1 
6539 C CE2 . PHE   B 168 ? 0.2536 0.1573 0.2941 -0.0252 -0.0605 0.0167  168 PHE   B CE2 
6540 C CZ  . PHE   B 168 ? 0.2707 0.1534 0.2988 -0.0125 -0.0696 0.0278  168 PHE   B CZ  
6550 N N   . LEU   B 169 ? 0.1717 0.1590 0.2505 -0.0086 -0.0036 0.0015  169 LEU   B N   
6551 C CA  . LEU   B 169 ? 0.1896 0.1850 0.2866 -0.0173 -0.0022 -0.0320 169 LEU   B CA  
6552 C C   . LEU   B 169 ? 0.2134 0.2150 0.3339 -0.0018 -0.0067 -0.0609 169 LEU   B C   
6553 O O   . LEU   B 169 ? 0.2319 0.2356 0.3976 0.0038  -0.0161 -0.0815 169 LEU   B O   
6554 C CB  . LEU   B 169 ? 0.2080 0.2301 0.3019 -0.0293 -0.0110 0.0025  169 LEU   B CB  
6555 C CG  . LEU   B 169 ? 0.2470 0.2744 0.3475 -0.0102 -0.0001 0.0167  169 LEU   B CG  
6556 C CD1 . LEU   B 169 ? 0.2599 0.3007 0.3588 -0.0045 -0.0063 0.0365  169 LEU   B CD1 
6557 C CD2 . LEU   B 169 ? 0.2445 0.2822 0.3509 0.0103  0.0243  -0.0001 169 LEU   B CD2 
6558 O OXT . LEU   B 169 ? 0.2390 0.2397 0.3233 0.0275  -0.0029 -0.0603 169 LEU   B OXT 
6570 N N2  B A1BAY C .   ? 0.1662 0.1338 0.1695 0.0031  0.0071  0.0241  201 A1BAY A N2  
6571 C C3  B A1BAY C .   ? 0.2286 0.2043 0.2346 -0.0171 0.0067  0.0212  201 A1BAY A C3  
6572 C C6  B A1BAY C .   ? 0.1508 0.1369 0.1691 0.0048  0.0120  0.0265  201 A1BAY A C6  
6573 C C9  B A1BAY C .   ? 0.1460 0.1355 0.1647 -0.0053 0.0113  0.0243  201 A1BAY A C9  
6574 C C12 B A1BAY C .   ? 0.2081 0.1384 0.1836 -0.0080 -0.0116 0.0357  201 A1BAY A C12 
6575 C C14 B A1BAY C .   ? 0.2155 0.1714 0.2036 -0.0147 -0.0113 0.0148  201 A1BAY A C14 
6576 C C1  B A1BAY C .   ? 0.2314 0.2022 0.2382 -0.0091 0.0037  0.0203  201 A1BAY A C1  
6577 C C10 B A1BAY C .   ? 0.1350 0.1311 0.1627 -0.0064 0.0110  0.0202  201 A1BAY A C10 
6578 C C11 B A1BAY C .   ? 0.2015 0.1304 0.1881 -0.0138 -0.0123 0.0377  201 A1BAY A C11 
6579 C C13 B A1BAY C .   ? 0.2130 0.1569 0.1909 -0.0119 -0.0086 0.0264  201 A1BAY A C13 
6580 C C15 B A1BAY C .   ? 0.2161 0.1628 0.1828 -0.0137 0.0003  0.0232  201 A1BAY A C15 
6581 C C2  B A1BAY C .   ? 0.2294 0.1937 0.2311 -0.0131 0.0102  0.0278  201 A1BAY A C2  
6582 C C4  B A1BAY C .   ? 0.2149 0.1626 0.2016 -0.0130 -0.0029 0.0296  201 A1BAY A C4  
6583 C C5  B A1BAY C .   ? 0.1626 0.1288 0.1696 -0.0055 0.0073  0.0293  201 A1BAY A C5  
6584 C C7  B A1BAY C .   ? 0.1381 0.1313 0.1611 -0.0028 0.0146  0.0230  201 A1BAY A C7  
6585 C C8  B A1BAY C .   ? 0.1437 0.1308 0.1624 -0.0036 0.0108  0.0216  201 A1BAY A C8  
6586 N N1  B A1BAY C .   ? 0.1906 0.1323 0.1881 -0.0123 -0.0004 0.0325  201 A1BAY A N1  
6587 N N3  B A1BAY C .   ? 0.1414 0.1339 0.1626 -0.0028 0.0207  0.0299  201 A1BAY A N3  
6588 N N4  B A1BAY C .   ? 0.1354 0.1327 0.1688 -0.0028 0.0062  0.0186  201 A1BAY A N4  
6589 O O1  B A1BAY C .   ? 0.2336 0.1974 0.2446 -0.0071 0.0321  0.0448  201 A1BAY A O1  
6612 O O1  C A1BAZ D .   ? 0.1792 0.1911 0.1929 0.0370  -0.0328 0.0346  202 A1BAZ A O1  
6613 C C1  C A1BAZ D .   ? 0.1575 0.1867 0.1572 0.0331  -0.0132 0.0338  202 A1BAZ A C1  
6614 C C2  C A1BAZ D .   ? 0.1640 0.1782 0.1710 0.0361  -0.0214 0.0393  202 A1BAZ A C2  
6615 C C3  C A1BAZ D .   ? 0.1685 0.1775 0.1773 0.0441  -0.0261 0.0316  202 A1BAZ A C3  
6616 C C4  C A1BAZ D .   ? 0.1596 0.1566 0.1716 0.0288  -0.0120 0.0427  202 A1BAZ A C4  
6617 C C5  C A1BAZ D .   ? 0.1354 0.1209 0.1686 0.0224  0.0140  0.0347  202 A1BAZ A C5  
6618 C C6  C A1BAZ D .   ? 0.1368 0.1275 0.1740 0.0260  0.0198  0.0269  202 A1BAZ A C6  
6619 C C7  C A1BAZ D .   ? 0.1213 0.1221 0.1686 0.0113  0.0240  0.0208  202 A1BAZ A C7  
6620 C C8  C A1BAZ D .   ? 0.1210 0.1221 0.1649 0.0160  0.0206  0.0237  202 A1BAZ A C8  
6621 C C10 C A1BAZ D .   ? 0.1174 0.1231 0.1706 -0.0003 0.0256  0.0202  202 A1BAZ A C10 
6622 C C11 C A1BAZ D .   ? 0.1622 0.1338 0.1949 0.0226  -0.0121 0.0443  202 A1BAZ A C11 
6623 C C12 C A1BAZ D .   ? 0.1689 0.1480 0.1955 0.0217  -0.0138 0.0346  202 A1BAZ A C12 
6624 C C13 C A1BAZ D .   ? 0.1673 0.1632 0.1789 0.0231  -0.0075 0.0331  202 A1BAZ A C13 
6625 C C14 C A1BAZ D .   ? 0.1700 0.1650 0.1821 0.0189  -0.0015 0.0224  202 A1BAZ A C14 
6626 C C15 C A1BAZ D .   ? 0.1730 0.1827 0.1869 0.0176  -0.0034 0.0232  202 A1BAZ A C15 
6627 C C9  C A1BAZ D .   ? 0.1270 0.1282 0.1688 0.0065  0.0241  0.0281  202 A1BAZ A C9  
6628 N N1  C A1BAZ D .   ? 0.1499 0.1271 0.1802 0.0253  0.0001  0.0410  202 A1BAZ A N1  
6629 N N2  C A1BAZ D .   ? 0.1505 0.1251 0.1726 0.0268  0.0170  0.0262  202 A1BAZ A N2  
6630 N N3  C A1BAZ D .   ? 0.1265 0.1251 0.1720 0.0132  0.0272  0.0275  202 A1BAZ A N3  
6631 N N4  C A1BAZ D .   ? 0.1215 0.1238 0.1785 0.0045  0.0199  0.0156  202 A1BAZ A N4  
6654 O O   . HOH   E .   ? 0.4235 0.8845 0.4515 -0.1234 0.0425  0.0855  301 HOH   A O   
6655 O O   . HOH   E .   ? 0.7218 0.5081 0.3394 0.2524  -0.0896 0.0705  302 HOH   A O   
6656 O O   B HOH   E .   ? 0.4472 0.2508 0.4263 -0.0931 -0.1137 -0.0236 303 HOH   A O   
6657 O O   . HOH   E .   ? 0.4601 0.3425 0.5229 -0.0616 0.1079  0.1052  304 HOH   A O   
6658 O O   . HOH   E .   ? 0.3029 0.3364 0.1927 -0.0380 0.0557  0.0526  305 HOH   A O   
6659 O O   . HOH   E .   ? 0.3493 0.2350 0.4038 -0.0295 -0.1008 0.0610  306 HOH   A O   
6660 O O   . HOH   E .   ? 0.4854 0.5931 0.3337 -0.1559 0.1192  0.1119  307 HOH   A O   
6661 O O   . HOH   E .   ? 0.8363 0.4808 0.4075 -0.1433 0.0930  0.1280  308 HOH   A O   
6662 O O   . HOH   E .   ? 0.1945 0.2264 0.2837 -0.0106 -0.0094 0.0754  309 HOH   A O   
6663 O O   . HOH   E .   ? 0.4535 0.6046 0.4948 0.1854  0.1593  -0.0721 310 HOH   A O   
6664 O O   . HOH   E .   ? 0.3528 0.3099 0.4275 -0.0371 0.1711  0.0193  311 HOH   A O   
6665 O O   . HOH   E .   ? 0.2743 0.2408 0.2692 -0.0565 0.0288  -0.0207 312 HOH   A O   
6666 O O   . HOH   E .   ? 0.1573 0.4321 0.3264 0.0003  0.0153  0.1386  313 HOH   A O   
6667 O O   . HOH   E .   ? 0.2008 0.1826 0.3721 -0.0351 0.0133  -0.0126 314 HOH   A O   
6668 O O   . HOH   E .   ? 0.5674 0.2162 0.4423 0.0876  0.0133  -0.0009 315 HOH   A O   
6669 O O   . HOH   E .   ? 0.7948 0.3508 0.5684 -0.0770 -0.1341 0.0652  316 HOH   A O   
6670 O O   . HOH   E .   ? 0.2957 0.2951 0.2862 -0.0618 0.0374  0.0851  317 HOH   A O   
6671 O O   . HOH   E .   ? 0.2696 0.2455 0.5642 -0.0256 -0.1340 0.1138  318 HOH   A O   
6672 O O   . HOH   E .   ? 0.2032 0.3377 0.4549 -0.0380 0.0342  -0.1078 319 HOH   A O   
6673 O O   . HOH   E .   ? 0.1830 0.3018 0.2692 0.0274  -0.0199 -0.0018 320 HOH   A O   
6674 O O   B HOH   E .   ? 0.1510 0.3543 0.1722 0.0318  -0.0291 0.0140  321 HOH   A O   
6675 O O   A HOH   E .   ? 0.2208 0.4732 0.3878 -0.0149 -0.0480 0.1154  322 HOH   A O   
6676 O O   . HOH   E .   ? 0.7939 0.6020 0.3447 0.0078  -0.0924 0.1327  323 HOH   A O   
6677 O O   A HOH   E .   ? 0.2419 0.4320 0.4686 -0.0545 0.0879  0.1722  324 HOH   A O   
6678 O O   . HOH   E .   ? 0.1498 0.1514 0.2150 -0.0149 0.0042  -0.0022 325 HOH   A O   
6679 O O   . HOH   E .   ? 0.1757 0.1695 0.2324 -0.0213 0.0031  0.0368  326 HOH   A O   
6680 O O   A HOH   E .   ? 0.3270 0.3361 0.2614 -0.0139 -0.0382 -0.0218 327 HOH   A O   
6681 O O   . HOH   E .   ? 0.2639 0.1985 0.2591 -0.0525 0.0085  0.0492  328 HOH   A O   
6682 O O   A HOH   E .   ? 0.2122 0.4494 0.5216 0.0137  -0.0510 0.1574  329 HOH   A O   
6683 O O   . HOH   E .   ? 0.2425 0.2507 0.4000 -0.0131 0.0666  0.0712  330 HOH   A O   
6684 O O   . HOH   E .   ? 0.5906 0.2043 0.4880 0.0128  -0.1547 0.0605  331 HOH   A O   
6685 O O   . HOH   E .   ? 0.4648 0.4265 0.4142 -0.1925 -0.0916 0.2021  332 HOH   A O   
6686 O O   . HOH   E .   ? 0.3428 0.4362 0.2902 -0.0257 0.0612  0.0618  333 HOH   A O   
6687 O O   . HOH   E .   ? 0.2753 0.2325 0.2771 0.0521  0.0340  0.0448  334 HOH   A O   
6688 O O   . HOH   E .   ? 0.2170 0.1756 0.2650 0.0215  -0.0305 -0.0039 335 HOH   A O   
6689 O O   B HOH   E .   ? 0.5623 0.3238 0.4232 0.1430  0.0668  0.1483  336 HOH   A O   
6690 O O   A HOH   E .   ? 0.4974 0.1607 0.2228 -0.0045 0.0501  -0.0023 337 HOH   A O   
6691 O O   . HOH   E .   ? 0.2425 0.4216 0.3874 -0.0100 -0.0344 0.1725  338 HOH   A O   
6692 O O   . HOH   E .   ? 0.6493 0.3758 0.2978 0.0562  0.1154  0.1078  339 HOH   A O   
6693 O O   B HOH   E .   ? 0.3619 0.2954 0.3364 -0.0008 0.0543  0.0378  340 HOH   A O   
6694 O O   . HOH   E .   ? 0.1587 0.2245 0.2356 0.0060  -0.0030 0.0523  341 HOH   A O   
6695 O O   B HOH   E .   ? 0.3663 0.2293 0.2312 -0.0309 -0.0383 -0.0046 342 HOH   A O   
6696 O O   . HOH   E .   ? 0.2652 0.4441 0.3402 -0.0541 0.0302  0.0123  343 HOH   A O   
6697 O O   A HOH   E .   ? 0.2080 0.1651 0.3436 0.0107  -0.0595 -0.0428 344 HOH   A O   
6698 O O   . HOH   E .   ? 0.1886 0.2484 0.2496 -0.0342 -0.0053 0.0936  345 HOH   A O   
6699 O O   . HOH   E .   ? 0.6672 0.4126 0.3536 -0.0882 -0.0871 -0.0762 346 HOH   A O   
6700 O O   . HOH   E .   ? 0.3214 0.3903 0.3575 -0.1151 -0.0836 -0.0280 347 HOH   A O   
6701 O O   A HOH   E .   ? 0.1427 0.1474 0.1965 0.0095  -0.0302 -0.0166 348 HOH   A O   
6702 O O   . HOH   E .   ? 0.2217 0.2548 0.5408 0.0250  -0.1011 -0.0885 349 HOH   A O   
6703 O O   . HOH   E .   ? 0.2098 0.1971 0.4039 0.0018  0.0976  -0.0201 350 HOH   A O   
6704 O O   A HOH   E .   ? 0.2849 0.5513 0.3067 0.1634  -0.0845 -0.0901 351 HOH   A O   
6705 O O   . HOH   E .   ? 0.2329 0.3848 0.4075 0.0668  -0.0831 -0.0107 352 HOH   A O   
6706 O O   . HOH   E .   ? 0.1492 0.1925 0.2740 0.0111  -0.0098 0.0031  353 HOH   A O   
6707 O O   . HOH   E .   ? 0.6363 0.4833 0.5922 0.0652  0.2566  -0.1034 354 HOH   A O   
6708 O O   . HOH   E .   ? 0.1449 0.1372 0.1620 -0.0033 0.0165  0.0134  355 HOH   A O   
6709 O O   . HOH   E .   ? 0.5825 0.2967 0.3582 0.1154  -0.1060 -0.0701 356 HOH   A O   
6710 O O   . HOH   E .   ? 0.3634 0.4586 0.3493 0.1939  0.0791  0.0987  357 HOH   A O   
6711 O O   . HOH   E .   ? 0.2385 0.1995 0.2195 -0.0008 0.0089  0.0197  358 HOH   A O   
6712 O O   . HOH   E .   ? 0.1900 0.1728 0.2710 0.0123  -0.0264 0.0258  359 HOH   A O   
6713 O O   . HOH   E .   ? 0.1522 0.1566 0.1660 -0.0099 -0.0043 -0.0099 360 HOH   A O   
6714 O O   . HOH   E .   ? 0.6353 0.2848 0.4447 -0.1622 0.2610  -0.0941 361 HOH   A O   
6715 O O   . HOH   E .   ? 0.4965 0.2755 0.2976 -0.0700 0.0549  0.0425  362 HOH   A O   
6716 O O   . HOH   E .   ? 0.2112 0.2965 0.4021 0.0338  0.0874  -0.0644 363 HOH   A O   
6717 O O   . HOH   E .   ? 0.2988 0.3561 0.5032 -0.0616 -0.1066 -0.0897 364 HOH   A O   
6718 O O   . HOH   E .   ? 0.1576 0.1386 0.2165 -0.0144 0.0114  -0.0012 365 HOH   A O   
6719 O O   . HOH   E .   ? 0.2802 0.3609 0.2540 -0.0839 -0.0217 -0.0787 366 HOH   A O   
6720 O O   . HOH   E .   ? 0.3350 0.2238 0.5269 -0.0570 -0.0319 0.0182  367 HOH   A O   
6721 O O   . HOH   E .   ? 0.4114 0.2082 0.2293 0.1186  0.0405  0.0131  368 HOH   A O   
6722 O O   . HOH   E .   ? 0.2703 0.2957 0.3561 -0.0358 0.0887  0.0116  369 HOH   A O   
6723 O O   . HOH   E .   ? 0.3939 0.2393 0.5275 -0.1219 0.0696  0.0344  370 HOH   A O   
6724 O O   . HOH   E .   ? 0.4439 0.3699 0.5578 -0.0205 0.1283  -0.0430 371 HOH   A O   
6725 O O   . HOH   E .   ? 0.1480 0.1508 0.2037 0.0055  -0.0106 0.0092  372 HOH   A O   
6726 O O   . HOH   E .   ? 0.5471 0.5255 0.1990 -0.1229 0.0949  0.0078  373 HOH   A O   
6727 O O   . HOH   E .   ? 0.2041 0.2451 0.2117 -0.0299 -0.0336 0.0294  374 HOH   A O   
6728 O O   A HOH   E .   ? 0.1345 0.2446 0.2049 0.0338  0.0175  0.0522  375 HOH   A O   
6729 O O   . HOH   E .   ? 0.2010 0.1956 0.2345 -0.0394 0.0045  0.0239  376 HOH   A O   
6730 O O   . HOH   E .   ? 0.3784 0.7495 0.4986 -0.0520 -0.1354 -0.0114 377 HOH   A O   
6731 O O   . HOH   E .   ? 0.2564 0.4432 0.3176 0.0537  0.0631  0.1656  378 HOH   A O   
6732 O O   . HOH   E .   ? 0.6433 0.5036 0.5844 -0.1178 -0.0383 0.1181  379 HOH   A O   
6733 O O   . HOH   E .   ? 0.3554 0.3214 0.3854 -0.0992 -0.0674 0.0133  380 HOH   A O   
6734 O O   A HOH   E .   ? 0.2203 0.2216 0.2043 0.0331  0.0075  0.0580  381 HOH   A O   
6735 O O   . HOH   E .   ? 0.3765 0.6807 0.7290 0.1520  0.1305  0.1179  382 HOH   A O   
6736 O O   B HOH   E .   ? 0.2757 0.3676 0.2411 -0.0631 -0.0093 -0.0220 383 HOH   A O   
6737 O O   . HOH   E .   ? 0.2642 0.1903 0.2880 -0.0152 0.0052  0.0329  384 HOH   A O   
6738 O O   . HOH   E .   ? 0.2412 0.3788 0.3224 0.0193  0.0178  0.0186  385 HOH   A O   
6739 O O   . HOH   E .   ? 0.2640 0.2090 0.2002 -0.0629 0.0184  0.0207  386 HOH   A O   
6740 O O   . HOH   E .   ? 0.2061 0.1682 0.1637 -0.0004 0.0244  0.0137  387 HOH   A O   
6741 O O   . HOH   E .   ? 0.3103 0.5646 0.3656 0.0577  0.0725  -0.1049 388 HOH   A O   
6742 O O   . HOH   E .   ? 0.1738 0.2593 0.3941 -0.0220 0.0763  0.0675  389 HOH   A O   
6743 O O   . HOH   E .   ? 0.3241 0.2845 0.2163 0.0298  0.0690  0.0055  390 HOH   A O   
6744 O O   . HOH   E .   ? 0.7429 0.6158 0.4550 -0.0621 -0.0413 -0.1207 391 HOH   A O   
6745 O O   A HOH   E .   ? 0.6078 0.5802 0.5373 0.0454  0.0319  0.1429  392 HOH   A O   
6746 O O   . HOH   E .   ? 0.5640 0.4257 0.6111 -0.1339 0.0637  0.1442  393 HOH   A O   
6747 O O   . HOH   E .   ? 0.2988 0.2804 0.3497 0.0056  -0.0306 0.0895  394 HOH   A O   
6748 O O   . HOH   E .   ? 0.1875 0.1893 0.3892 0.0340  0.1011  0.0838  395 HOH   A O   
6749 O O   A HOH   E .   ? 0.3687 0.4391 0.4795 -0.1683 -0.0439 -0.0231 396 HOH   A O   
6750 O O   B HOH   E .   ? 0.3238 0.4973 0.2963 0.0196  -0.0793 -0.1201 397 HOH   A O   
6751 O O   . HOH   E .   ? 0.1814 0.1383 0.1879 -0.0167 0.0106  0.0054  398 HOH   A O   
6752 O O   A HOH   E .   ? 0.5584 0.5199 0.3667 -0.0687 -0.1145 -0.0825 399 HOH   A O   
6753 O O   . HOH   E .   ? 0.2587 0.4120 0.3141 -0.0641 0.0857  -0.0722 400 HOH   A O   
6754 O O   . HOH   E .   ? 0.5924 0.6337 0.5945 -0.1147 0.0697  0.0793  401 HOH   A O   
6755 O O   . HOH   E .   ? 0.2075 0.1596 0.3012 0.0002  -0.0270 0.0108  402 HOH   A O   
6756 O O   . HOH   E .   ? 0.2721 0.3103 0.3715 -0.0191 0.1044  -0.0231 403 HOH   A O   
6757 O O   . HOH   E .   ? 0.3027 0.4949 0.4390 0.1281  0.0174  0.0469  404 HOH   A O   
6758 O O   . HOH   E .   ? 0.3178 0.2909 0.2496 -0.0918 -0.0656 0.0013  405 HOH   A O   
6759 O O   . HOH   E .   ? 0.6158 0.4360 0.4939 0.1648  0.1408  -0.1092 406 HOH   A O   
6760 O O   A HOH   E .   ? 0.1317 0.1885 0.1553 0.0196  -0.0243 -0.0468 407 HOH   A O   
6761 O O   . HOH   E .   ? 0.1542 0.1588 0.2933 -0.0028 -0.0086 0.0040  408 HOH   A O   
6762 O O   A HOH   E .   ? 0.6620 0.4223 0.4633 0.0754  0.0990  0.0234  409 HOH   A O   
6763 O O   . HOH   E .   ? 0.2410 0.3848 0.7791 -0.0365 0.0902  -0.0464 410 HOH   A O   
6764 O O   . HOH   E .   ? 0.5492 0.5625 0.4558 -0.0885 0.0049  -0.0939 411 HOH   A O   
6765 O O   . HOH   E .   ? 0.5544 0.4832 0.3996 -0.0432 -0.1488 0.0219  412 HOH   A O   
6766 O O   . HOH   E .   ? 0.2058 0.2753 0.3359 -0.0213 -0.0246 0.0206  413 HOH   A O   
6767 O O   . HOH   E .   ? 0.1910 0.1825 0.2785 0.0205  -0.0415 0.0319  414 HOH   A O   
6768 O O   . HOH   E .   ? 0.4821 0.3238 0.2993 0.0648  -0.1010 -0.0186 415 HOH   A O   
6769 O O   . HOH   E .   ? 0.3597 0.5881 0.3367 -0.1171 -0.0970 -0.0324 416 HOH   A O   
6770 O O   . HOH   E .   ? 0.3936 0.2208 0.5518 -0.0769 -0.2277 0.1070  417 HOH   A O   
6771 O O   . HOH   E .   ? 0.4308 0.3408 0.3325 -0.1256 0.0509  0.0373  418 HOH   A O   
6772 O O   . HOH   E .   ? 0.2301 0.2292 0.3749 -0.0001 -0.0458 0.0436  419 HOH   A O   
6773 O O   . HOH   E .   ? 0.5001 0.5428 0.3526 -0.1159 -0.0357 0.0978  420 HOH   A O   
6774 O O   . HOH   E .   ? 0.3036 0.7576 0.4869 0.1773  0.0353  0.0886  421 HOH   A O   
6775 O O   . HOH   E .   ? 0.1719 0.2300 0.3255 -0.0345 -0.0137 0.0538  422 HOH   A O   
6776 O O   . HOH   E .   ? 0.2285 0.2729 0.2593 -0.0062 -0.0481 0.0497  423 HOH   A O   
6777 O O   B HOH   E .   ? 0.2031 0.2262 0.2559 -0.0061 0.0300  0.1012  424 HOH   A O   
6778 O O   . HOH   E .   ? 0.2893 0.6164 0.1756 -0.0592 0.0367  0.0124  425 HOH   A O   
6779 O O   . HOH   E .   ? 0.3383 0.4182 0.4048 0.1190  -0.0841 -0.1527 426 HOH   A O   
6780 O O   . HOH   E .   ? 0.3492 0.1269 0.2366 0.0073  -0.0592 0.0063  427 HOH   A O   
6781 O O   . HOH   E .   ? 0.2214 0.4478 0.2763 0.1555  -0.0261 -0.0196 428 HOH   A O   
6782 O O   B HOH   E .   ? 0.3722 0.5501 0.3000 -0.0169 0.1003  0.0259  429 HOH   A O   
6783 O O   . HOH   E .   ? 0.6703 0.7030 0.6271 0.0886  -0.1054 0.0040  430 HOH   A O   
6784 O O   . HOH   E .   ? 0.7461 0.6769 0.4321 0.2860  -0.0657 -0.0572 431 HOH   A O   
6785 O O   A HOH   E .   ? 0.1390 0.1464 0.2642 0.0155  -0.0342 -0.0092 432 HOH   A O   
6786 O O   B HOH   E .   ? 0.3677 0.2774 0.4476 0.0324  0.1444  -0.0627 433 HOH   A O   
6787 O O   . HOH   E .   ? 0.4453 0.6961 0.3950 -0.1025 0.0066  0.1123  434 HOH   A O   
6788 O O   . HOH   E .   ? 0.3804 0.2595 0.6460 0.0694  0.0420  0.0024  435 HOH   A O   
6789 O O   . HOH   E .   ? 0.3147 0.3614 0.5654 -0.0334 0.1798  -0.0180 436 HOH   A O   
6790 O O   . HOH   E .   ? 0.1979 0.2124 0.2010 -0.0081 -0.0180 -0.0160 437 HOH   A O   
6791 O O   . HOH   E .   ? 0.6226 0.7879 0.4555 0.0435  0.2941  -0.0430 438 HOH   A O   
6792 O O   . HOH   E .   ? 0.1901 0.2136 0.5892 -0.0234 -0.0972 0.0846  439 HOH   A O   
6793 O O   . HOH   E .   ? 0.7078 0.4050 0.5083 0.2205  -0.0895 0.1297  440 HOH   A O   
6794 O O   A HOH   E .   ? 0.5248 0.3870 0.3030 -0.1185 -0.0567 0.1270  441 HOH   A O   
6795 O O   B HOH   E .   ? 0.2802 0.2507 0.5934 -0.0025 0.0277  0.0513  442 HOH   A O   
6796 O O   A HOH   E .   ? 0.4214 0.6250 0.4973 0.0105  -0.0125 0.0994  443 HOH   A O   
6797 O O   . HOH   E .   ? 0.3733 0.2775 0.1935 -0.0816 0.0385  0.0267  444 HOH   A O   
6798 O O   . HOH   E .   ? 0.4759 0.6237 0.5637 -0.1653 0.0363  -0.1095 445 HOH   A O   
6799 O O   . HOH   E .   ? 0.2159 0.1703 0.2613 0.0023  0.0054  0.0187  446 HOH   A O   
6800 O O   . HOH   E .   ? 0.7239 0.7887 0.4483 0.3185  -0.0432 0.1883  447 HOH   A O   
6801 O O   . HOH   E .   ? 0.4348 0.4286 0.5227 -0.1114 -0.0994 -0.1143 448 HOH   A O   
6802 O O   . HOH   E .   ? 0.3639 0.3685 0.5584 0.0131  0.1535  -0.1277 449 HOH   A O   
6803 O O   . HOH   E .   ? 0.3953 0.3404 0.3491 0.2014  -0.0306 -0.0437 450 HOH   A O   
6804 O O   . HOH   E .   ? 0.6809 0.5096 0.6848 0.2124  -0.0803 -0.0865 451 HOH   A O   
6805 O O   . HOH   E .   ? 0.2103 0.2634 0.2281 0.0012  -0.0035 -0.0480 452 HOH   A O   
6806 O O   B HOH   E .   ? 0.4098 0.6153 0.4245 -0.1310 0.0651  0.0942  453 HOH   A O   
6807 O O   . HOH   E .   ? 0.2359 0.2028 0.3103 0.0173  0.0377  0.0075  454 HOH   A O   
6808 O O   A HOH   E .   ? 0.1976 0.1561 0.2129 -0.0014 -0.0242 -0.0410 455 HOH   A O   
6809 O O   . HOH   E .   ? 0.6444 0.3052 0.4598 0.0204  -0.0516 0.1510  456 HOH   A O   
6810 O O   B HOH   E .   ? 0.4583 0.3382 0.4440 0.1792  0.0171  -0.0390 457 HOH   A O   
6811 O O   . HOH   E .   ? 0.8522 0.9340 0.6840 -0.0664 -0.1025 -0.0541 458 HOH   A O   
6812 O O   . HOH   E .   ? 0.5585 0.5729 0.7649 0.0085  -0.1410 0.1925  459 HOH   A O   
6813 O O   . HOH   E .   ? 0.6797 0.6314 0.5526 -0.0874 0.1306  0.1430  460 HOH   A O   
6814 O O   A HOH   E .   ? 0.6420 0.4901 0.5269 0.2625  0.1444  0.2221  461 HOH   A O   
6815 O O   . HOH   E .   ? 0.4745 0.5490 0.3656 -0.0699 -0.0379 0.0112  462 HOH   A O   
6816 O O   . HOH   E .   ? 0.4613 0.4610 0.4633 0.0120  -0.0346 0.1252  463 HOH   A O   
6817 O O   . HOH   E .   ? 0.6172 0.5984 0.6087 0.2241  0.3032  0.2856  464 HOH   A O   
6818 O O   . HOH   E .   ? 0.3595 0.4273 0.5063 0.1568  -0.0388 0.1468  465 HOH   A O   
6819 O O   . HOH   E .   ? 0.6404 0.9056 0.5105 -0.0062 -0.0495 -0.0534 466 HOH   A O   
6820 O O   . HOH   E .   ? 0.6302 0.3448 0.6020 0.0892  0.1238  0.0593  467 HOH   A O   
6821 O O   . HOH   E .   ? 0.2902 0.3021 0.3663 -0.0688 0.0311  -0.0787 468 HOH   A O   
6822 O O   . HOH   E .   ? 0.3238 0.5341 0.5106 0.0567  -0.0816 0.1541  469 HOH   A O   
6823 O O   . HOH   E .   ? 0.2973 0.4452 0.4466 0.0255  -0.0557 -0.0101 470 HOH   A O   
6824 O O   . HOH   E .   ? 0.6449 0.7930 0.5610 -0.1456 0.1067  0.2040  471 HOH   A O   
6825 O O   . HOH   E .   ? 0.3027 0.4823 0.4975 -0.1533 0.0639  -0.1922 472 HOH   A O   
6826 O O   . HOH   E .   ? 0.3960 0.5673 0.4169 0.0223  -0.0923 -0.0738 473 HOH   A O   
6827 O O   . HOH   E .   ? 0.3235 0.1923 0.2681 0.0501  -0.0918 -0.0303 474 HOH   A O   
6828 O O   . HOH   E .   ? 0.2956 0.4070 0.5874 0.0620  0.0358  -0.1904 475 HOH   A O   
6829 O O   . HOH   E .   ? 0.3439 0.2919 0.6104 0.0925  -0.1749 -0.0475 476 HOH   A O   
6830 O O   . HOH   E .   ? 0.4395 0.5648 0.3626 -0.0659 -0.0700 0.1802  477 HOH   A O   
6831 O O   . HOH   E .   ? 0.2615 0.2648 0.3413 -0.0822 0.0344  -0.0337 478 HOH   A O   
6832 O O   . HOH   E .   ? 0.6710 0.3335 0.8017 -0.0951 0.0060  0.1848  479 HOH   A O   
6833 O O   B HOH   E .   ? 0.3624 0.5340 0.4469 -0.0757 -0.0757 0.0475  480 HOH   A O   
6834 O O   . HOH   E .   ? 0.5981 0.5233 0.5022 0.0227  0.1599  0.0769  481 HOH   A O   
6835 O O   . HOH   E .   ? 0.3088 0.4205 0.3610 -0.0375 -0.0411 -0.0457 482 HOH   A O   
6836 O O   . HOH   E .   ? 0.5600 0.5602 0.4957 0.1368  -0.1368 -0.1093 483 HOH   A O   
6837 O O   . HOH   E .   ? 0.3137 0.2806 0.3805 0.0177  0.0449  -0.0024 484 HOH   A O   
6838 O O   . HOH   E .   ? 0.7152 0.3922 0.5058 0.0059  0.2204  0.0494  485 HOH   A O   
6839 O O   . HOH   E .   ? 0.5269 0.7666 0.6640 -0.1574 -0.1211 0.0341  486 HOH   A O   
6840 O O   . HOH   E .   ? 0.6602 0.4971 0.6918 -0.0769 0.1365  -0.0142 487 HOH   A O   
6841 O O   . HOH   E .   ? 0.4236 0.4218 0.5376 -0.2073 -0.0116 0.0040  488 HOH   A O   
6842 O O   . HOH   E .   ? 0.2648 0.2559 0.2904 0.0334  -0.0036 -0.0236 489 HOH   A O   
6843 O O   . HOH   E .   ? 0.6746 0.4421 0.3714 -0.0113 0.0148  -0.1180 490 HOH   A O   
6844 O O   . HOH   E .   ? 0.4441 0.5301 0.2959 -0.0333 -0.0415 0.0347  491 HOH   A O   
6845 O O   . HOH   E .   ? 0.8634 0.3455 0.3292 -0.0370 -0.1167 -0.0156 492 HOH   A O   
6846 O O   . HOH   E .   ? 0.5985 0.6726 0.6281 0.1099  0.1769  -0.1295 493 HOH   A O   
6847 O O   . HOH   E .   ? 0.3663 0.3445 0.2803 -0.0713 0.1059  -0.0481 494 HOH   A O   
6848 O O   . HOH   E .   ? 0.4634 0.2830 0.3485 -0.0582 -0.0856 0.0601  495 HOH   A O   
6849 O O   . HOH   E .   ? 0.2800 0.5799 0.3800 0.1248  0.0955  0.2573  496 HOH   A O   
6850 O O   . HOH   E .   ? 0.2593 0.3295 0.5965 -0.0363 0.0963  -0.0691 497 HOH   A O   
6851 O O   . HOH   E .   ? 0.2743 0.4355 0.5401 -0.0072 0.0925  0.1455  498 HOH   A O   
6852 O O   . HOH   E .   ? 0.6097 0.6045 0.4268 0.0232  0.1530  0.0831  499 HOH   A O   
6853 O O   . HOH   E .   ? 0.2662 0.2534 0.7990 -0.0110 -0.1633 0.0298  500 HOH   A O   
6854 O O   . HOH   E .   ? 0.5453 0.3350 0.4820 -0.0240 0.2789  0.0220  501 HOH   A O   
6855 O O   . HOH   E .   ? 0.2659 0.2061 0.6319 0.0022  0.0516  0.1059  502 HOH   A O   
6856 O O   . HOH   E .   ? 0.6197 0.4681 0.4901 -0.0409 -0.1024 -0.0040 503 HOH   A O   
6857 O O   . HOH   E .   ? 0.8068 0.2967 0.5604 0.0181  0.0103  0.1077  504 HOH   A O   
6858 O O   . HOH   E .   ? 0.5027 0.2821 0.4155 -0.1076 0.1014  0.0418  505 HOH   A O   
6859 O O   . HOH   E .   ? 0.4080 0.9262 0.5488 -0.1135 -0.0491 0.3157  506 HOH   A O   
6860 O O   . HOH   E .   ? 0.2244 0.3123 0.3724 0.0384  -0.0348 0.0535  507 HOH   A O   
6861 O O   . HOH   E .   ? 0.4528 0.2234 0.4766 -0.1018 0.0402  0.0295  508 HOH   A O   
6862 O O   B HOH   E .   ? 0.2819 0.3956 0.3987 0.0959  0.0976  0.0843  509 HOH   A O   
6863 O O   . HOH   E .   ? 0.3168 0.3736 0.4692 0.0718  0.0246  0.0148  510 HOH   A O   
6864 O O   . HOH   E .   ? 0.8582 0.6773 0.6013 -0.0691 0.0790  -0.0391 511 HOH   A O   
6865 O O   . HOH   E .   ? 0.4748 0.7307 0.5910 0.1247  -0.0769 0.1248  512 HOH   A O   
6866 O O   A HOH   E .   ? 0.5569 0.3886 0.4427 0.1893  -0.1294 -0.0038 513 HOH   A O   
6867 O O   . HOH   E .   ? 0.3249 0.2092 0.4460 0.0029  0.0700  0.0416  514 HOH   A O   
6868 O O   . HOH   E .   ? 0.4512 0.7484 0.5373 0.2937  -0.0301 0.0882  515 HOH   A O   
6869 O O   B HOH   E .   ? 0.4033 0.3398 0.3280 -0.0248 0.0191  0.0902  516 HOH   A O   
6870 O O   . HOH   E .   ? 0.4311 0.7651 0.5300 -0.0387 -0.0791 -0.0989 517 HOH   A O   
6871 O O   A HOH   E .   ? 0.3720 0.6983 0.4441 0.0035  0.1420  -0.0413 518 HOH   A O   
6872 O O   . HOH   E .   ? 0.2994 0.7164 0.4092 0.1086  0.0023  -0.0027 519 HOH   A O   
6873 O O   . HOH   E .   ? 0.5327 0.5956 0.5506 0.1505  -0.0918 0.0811  520 HOH   A O   
6874 O O   . HOH   E .   ? 0.4891 0.6249 0.5478 -0.0610 -0.0452 0.0251  521 HOH   A O   
6875 O O   . HOH   E .   ? 0.4151 0.4928 0.6368 -0.0365 -0.1199 0.3140  522 HOH   A O   
6876 O O   . HOH   F .   ? 0.2500 0.2395 0.3179 0.0315  0.0837  0.0232  201 HOH   B O   
6877 O O   . HOH   F .   ? 0.6404 0.5225 0.3221 0.0955  -0.1010 -0.1569 202 HOH   B O   
6878 O O   . HOH   F .   ? 0.5172 0.3996 0.5965 0.0684  -0.0765 0.2544  203 HOH   B O   
6879 O O   . HOH   F .   ? 0.7183 0.2526 0.4901 0.0716  0.1211  0.0222  204 HOH   B O   
6880 O O   . HOH   F .   ? 0.2543 0.5246 0.5513 -0.0167 0.1257  -0.2116 205 HOH   B O   
6881 O O   . HOH   F .   ? 0.4852 0.5882 0.3737 0.2975  -0.0815 -0.0054 206 HOH   B O   
6882 O O   . HOH   F .   ? 0.2987 0.2983 0.7050 0.0731  -0.1407 0.0497  207 HOH   B O   
6883 O O   . HOH   F .   ? 0.3612 0.7211 0.3526 0.1057  0.0246  0.2524  208 HOH   B O   
6884 O O   . HOH   F .   ? 0.7019 0.6044 0.6494 0.1681  0.0868  -0.0038 209 HOH   B O   
6885 O O   . HOH   F .   ? 0.3410 0.3183 0.6307 -0.0092 0.0172  -0.0329 210 HOH   B O   
6886 O O   . HOH   F .   ? 0.2656 0.2590 0.5404 -0.0069 0.0741  0.0198  211 HOH   B O   
6887 O O   . HOH   F .   ? 0.3724 0.4822 0.5632 -0.0919 0.0026  -0.1598 212 HOH   B O   
6888 O O   . HOH   F .   ? 0.5190 0.2601 0.3674 -0.0058 -0.0265 -0.0907 213 HOH   B O   
6889 O O   . HOH   F .   ? 0.4284 0.4714 0.4102 -0.0855 -0.1367 0.1215  214 HOH   B O   
6890 O O   . HOH   F .   ? 0.1635 0.1818 0.2568 -0.0206 0.0024  -0.0038 215 HOH   B O   
6891 O O   . HOH   F .   ? 0.6038 0.3309 0.4074 -0.2022 -0.0000 0.0139  216 HOH   B O   
6892 O O   . HOH   F .   ? 0.1932 0.2265 0.3048 -0.0035 0.0272  -0.0141 217 HOH   B O   
6893 O O   . HOH   F .   ? 0.4320 0.5028 0.3788 0.2367  -0.0957 -0.0040 218 HOH   B O   
6894 O O   . HOH   F .   ? 0.3522 0.5378 0.4564 0.2307  -0.0102 -0.0704 219 HOH   B O   
6895 O O   . HOH   F .   ? 0.2639 0.3509 0.3230 -0.0646 0.0342  -0.0609 220 HOH   B O   
6896 O O   . HOH   F .   ? 0.3735 0.4162 0.5333 -0.1738 0.0243  0.1122  221 HOH   B O   
6897 O O   . HOH   F .   ? 0.3408 0.3372 0.6597 0.0886  0.0031  0.0096  222 HOH   B O   
6898 O O   . HOH   F .   ? 0.5617 0.4057 0.3843 0.0179  0.0705  -0.1441 223 HOH   B O   
6899 O O   . HOH   F .   ? 0.4383 0.7188 0.2670 0.2820  0.0181  0.0151  224 HOH   B O   
6900 O O   . HOH   F .   ? 0.4753 0.1897 0.3419 0.0010  -0.0971 0.0121  225 HOH   B O   
6901 O O   . HOH   F .   ? 0.3335 0.2516 0.4186 0.0738  -0.0603 -0.0756 226 HOH   B O   
6902 O O   . HOH   F .   ? 0.4896 0.6976 0.3067 -0.0003 -0.0546 0.1206  227 HOH   B O   
6903 O O   . HOH   F .   ? 0.1728 0.2040 0.2717 -0.0102 -0.0076 -0.0099 228 HOH   B O   
6904 O O   . HOH   F .   ? 0.4859 0.3977 0.6485 -0.0631 -0.1644 -0.0654 229 HOH   B O   
6905 O O   . HOH   F .   ? 0.2503 0.1958 0.2941 -0.0310 0.0876  0.0061  230 HOH   B O   
6906 O O   . HOH   F .   ? 0.3150 0.2111 0.5699 0.0220  0.1756  0.1024  231 HOH   B O   
6907 O O   . HOH   F .   ? 0.4433 0.3213 0.3738 -0.0948 0.0490  -0.0572 232 HOH   B O   
6908 O O   . HOH   F .   ? 0.2379 0.3913 0.3411 -0.0382 -0.0641 -0.0685 233 HOH   B O   
6909 O O   . HOH   F .   ? 0.3075 0.2080 0.4057 0.0019  0.1236  0.0048  234 HOH   B O   
6910 O O   . HOH   F .   ? 0.2111 0.2242 0.3033 -0.0500 0.0100  -0.0359 235 HOH   B O   
6911 O O   . HOH   F .   ? 0.3743 0.1859 0.2209 0.0122  -0.0921 -0.0138 236 HOH   B O   
6912 O O   . HOH   F .   ? 0.1488 0.1414 0.1840 -0.0145 -0.0060 0.0022  237 HOH   B O   
6913 O O   . HOH   F .   ? 0.2107 0.1318 0.3484 0.0096  -0.0649 -0.0212 238 HOH   B O   
6914 O O   . HOH   F .   ? 0.1605 0.1527 0.2479 -0.0047 -0.0060 -0.0200 239 HOH   B O   
6915 O O   . HOH   F .   ? 0.2991 0.1749 0.6250 -0.0182 -0.1094 -0.0335 240 HOH   B O   
6916 O O   . HOH   F .   ? 0.2171 0.2101 0.1841 0.0097  -0.0046 0.0081  241 HOH   B O   
6917 O O   . HOH   F .   ? 0.3650 0.3782 0.2375 0.0517  0.0586  0.0506  242 HOH   B O   
6918 O O   . HOH   F .   ? 0.1500 0.1315 0.1711 0.0004  -0.0059 0.0063  243 HOH   B O   
6919 O O   . HOH   F .   ? 0.2855 0.2707 0.3179 0.0390  0.0033  -0.0969 244 HOH   B O   
6920 O O   . HOH   F .   ? 0.2056 0.2139 0.3786 -0.0297 -0.0226 -0.0607 245 HOH   B O   
6921 O O   . HOH   F .   ? 0.2238 0.4345 0.2208 -0.0607 -0.0224 0.0798  246 HOH   B O   
6922 O O   . HOH   F .   ? 0.2350 0.2049 0.2202 -0.0363 -0.0655 0.0096  247 HOH   B O   
6923 O O   . HOH   F .   ? 0.6297 0.4561 0.5380 0.1676  0.0504  -0.0881 248 HOH   B O   
6924 O O   . HOH   F .   ? 0.2858 0.4627 0.3612 -0.1185 -0.0331 -0.0674 249 HOH   B O   
6925 O O   . HOH   F .   ? 0.3628 0.3068 0.4287 0.0495  -0.0889 -0.1478 250 HOH   B O   
6926 O O   . HOH   F .   ? 0.1937 0.1611 0.2209 -0.0260 -0.0195 0.0121  251 HOH   B O   
6927 O O   . HOH   F .   ? 0.2139 0.1516 0.2088 -0.0270 -0.0347 0.0235  252 HOH   B O   
6928 O O   . HOH   F .   ? 0.2910 0.2461 0.2959 -0.0316 0.0262  -0.0533 253 HOH   B O   
6929 O O   . HOH   F .   ? 0.2321 0.3613 0.5890 0.0949  -0.0654 -0.1396 254 HOH   B O   
6930 O O   . HOH   F .   ? 0.4470 0.3099 0.4124 -0.2089 0.0047  0.0116  255 HOH   B O   
6931 O O   . HOH   F .   ? 0.3245 0.3271 0.2295 0.0599  0.0638  0.0349  256 HOH   B O   
6932 O O   . HOH   F .   ? 0.1650 0.1708 0.2731 -0.0120 -0.0186 0.0093  257 HOH   B O   
6933 O O   . HOH   F .   ? 0.1344 0.1693 0.2018 -0.0082 0.0060  0.0173  258 HOH   B O   
6934 O O   . HOH   F .   ? 0.3043 0.2535 0.2849 0.1025  0.0756  0.0294  259 HOH   B O   
6935 O O   . HOH   F .   ? 0.4253 0.3001 0.4149 -0.0551 -0.0878 -0.0530 260 HOH   B O   
6936 O O   . HOH   F .   ? 0.4656 0.3145 0.2610 0.0879  -0.0316 -0.0811 261 HOH   B O   
6937 O O   . HOH   F .   ? 0.1894 0.2650 0.2875 0.0542  0.0471  0.0988  262 HOH   B O   
6938 O O   . HOH   F .   ? 0.2370 0.2390 0.2580 0.0935  -0.0767 -0.0691 263 HOH   B O   
6939 O O   . HOH   F .   ? 0.2187 0.2244 0.2254 0.0203  -0.0220 -0.0053 264 HOH   B O   
6940 O O   . HOH   F .   ? 0.2702 0.2030 0.2976 -0.0621 0.0084  -0.0048 265 HOH   B O   
6941 O O   . HOH   F .   ? 0.1718 0.1408 0.5377 -0.0044 -0.0321 -0.0239 266 HOH   B O   
6942 O O   . HOH   F .   ? 0.2769 0.3070 0.4866 -0.0405 0.0108  -0.1563 267 HOH   B O   
6943 O O   . HOH   F .   ? 0.2570 0.1856 0.4710 0.0118  -0.1203 -0.0464 268 HOH   B O   
6944 O O   . HOH   F .   ? 0.2503 0.2715 0.2573 -0.0478 -0.0727 -0.0403 269 HOH   B O   
6945 O O   . HOH   F .   ? 0.1863 0.1776 0.1737 -0.0370 -0.0359 0.0068  270 HOH   B O   
6946 O O   . HOH   F .   ? 0.2425 0.2662 0.3545 -0.0296 0.0441  -0.0711 271 HOH   B O   
6947 O O   . HOH   F .   ? 0.2449 0.3173 0.2275 -0.0642 0.0328  0.0467  272 HOH   B O   
6948 O O   . HOH   F .   ? 0.5268 0.2786 0.2719 0.0575  0.0971  -0.0134 273 HOH   B O   
6949 O O   . HOH   F .   ? 0.2947 0.2741 0.2851 -0.0329 -0.1061 -0.0009 274 HOH   B O   
6950 O O   . HOH   F .   ? 0.3810 0.6606 0.2919 0.2338  -0.1047 -0.1151 275 HOH   B O   
6951 O O   . HOH   F .   ? 0.2788 0.4315 0.5689 0.0362  0.0835  -0.0720 276 HOH   B O   
6952 O O   . HOH   F .   ? 0.3118 0.5215 0.4352 -0.0815 -0.1302 0.1778  277 HOH   B O   
6953 O O   . HOH   F .   ? 0.2548 0.3990 0.3597 0.0197  0.0879  0.0162  278 HOH   B O   
6954 O O   . HOH   F .   ? 0.2123 0.2991 0.2182 0.0673  -0.0255 -0.0089 279 HOH   B O   
6955 O O   . HOH   F .   ? 0.4219 0.5410 0.5143 -0.0102 -0.1119 -0.0863 280 HOH   B O   
6956 O O   . HOH   F .   ? 0.2574 0.3586 0.4338 -0.0415 -0.1328 0.1189  281 HOH   B O   
6957 O O   . HOH   F .   ? 0.2618 0.5276 0.4895 -0.1249 -0.1392 0.1345  282 HOH   B O   
6958 O O   . HOH   F .   ? 0.1600 0.1568 0.3426 -0.0146 0.0085  -0.0099 283 HOH   B O   
6959 O O   . HOH   F .   ? 0.1644 0.1598 0.1876 -0.0054 0.0004  -0.0024 284 HOH   B O   
6960 O O   . HOH   F .   ? 0.2164 0.4561 0.4693 -0.0572 -0.0172 -0.1439 285 HOH   B O   
6961 O O   . HOH   F .   ? 0.3785 0.2457 0.2349 0.0357  -0.0803 -0.0156 286 HOH   B O   
6962 O O   . HOH   F .   ? 0.2991 0.2331 0.4163 0.0379  0.0399  0.0675  287 HOH   B O   
6963 O O   . HOH   F .   ? 0.1636 0.1903 0.2695 0.0144  -0.0160 0.0035  288 HOH   B O   
6964 O O   . HOH   F .   ? 0.6287 0.5171 0.4381 -0.1081 0.0082  0.0955  289 HOH   B O   
6965 O O   . HOH   F .   ? 0.1622 0.2071 0.1674 -0.0098 -0.0208 0.0073  290 HOH   B O   
6966 O O   . HOH   F .   ? 0.3803 0.2109 0.4301 -0.0760 -0.2249 0.0616  291 HOH   B O   
6967 O O   . HOH   F .   ? 0.2441 0.2591 0.2841 0.0147  -0.0625 0.0324  292 HOH   B O   
6968 O O   . HOH   F .   ? 0.2887 0.2904 0.2557 -0.0105 -0.0016 -0.0974 293 HOH   B O   
6969 O O   . HOH   F .   ? 0.6013 0.4064 0.3031 0.2775  0.1073  0.0827  294 HOH   B O   
6970 O O   . HOH   F .   ? 0.3636 0.3577 0.4367 0.1076  -0.0794 -0.0967 295 HOH   B O   
6971 O O   . HOH   F .   ? 0.2837 0.2740 0.5167 -0.0052 -0.0470 0.1193  296 HOH   B O   
6972 O O   . HOH   F .   ? 0.1688 0.3107 0.4706 0.0098  0.0031  -0.1212 297 HOH   B O   
6973 O O   . HOH   F .   ? 0.2724 0.2813 0.4380 -0.0773 0.1277  -0.0653 298 HOH   B O   
6974 O O   . HOH   F .   ? 0.1725 0.1540 0.2405 0.0155  0.0005  0.0109  299 HOH   B O   
6975 O O   . HOH   F .   ? 0.2151 0.2786 0.6559 0.0340  -0.0678 -0.1243 300 HOH   B O   
6976 O O   . HOH   F .   ? 0.4388 0.3482 0.5266 -0.0784 -0.0107 0.1563  301 HOH   B O   
6977 O O   . HOH   F .   ? 0.5015 0.4544 0.3063 0.0132  -0.0664 0.0411  302 HOH   B O   
6978 O O   . HOH   F .   ? 0.5772 0.3189 0.2774 -0.2041 0.1095  -0.0325 303 HOH   B O   
6979 O O   . HOH   F .   ? 0.4862 0.4290 0.2719 0.1643  -0.1046 0.0576  304 HOH   B O   
6980 O O   . HOH   F .   ? 0.2124 0.1688 0.2704 -0.0304 -0.0238 -0.0035 305 HOH   B O   
6981 O O   . HOH   F .   ? 0.1595 0.1498 0.2980 -0.0006 -0.0079 -0.0020 306 HOH   B O   
6982 O O   . HOH   F .   ? 0.3592 0.1872 0.3991 0.0782  0.1422  0.0695  307 HOH   B O   
6983 O O   . HOH   F .   ? 0.2793 0.6707 0.8533 0.1366  -0.0261 -0.1171 308 HOH   B O   
6984 O O   . HOH   F .   ? 0.4496 0.4145 0.1977 -0.0193 0.0482  0.0027  309 HOH   B O   
6985 O O   . HOH   F .   ? 0.2222 0.1576 0.3697 0.0328  -0.1172 -0.0088 310 HOH   B O   
6986 O O   . HOH   F .   ? 0.5173 0.6793 0.2912 0.0591  -0.0381 0.2027  311 HOH   B O   
6987 O O   . HOH   F .   ? 0.2490 0.6798 0.2651 0.0447  -0.0080 -0.0417 312 HOH   B O   
6988 O O   . HOH   F .   ? 0.5511 0.4491 0.2441 0.1648  -0.1026 -0.0416 313 HOH   B O   
6989 O O   . HOH   F .   ? 0.2302 0.1546 0.2835 -0.0193 -0.0235 0.0298  314 HOH   B O   
6990 O O   . HOH   F .   ? 0.1605 0.1867 0.2738 -0.0215 -0.0111 0.0143  315 HOH   B O   
6991 O O   . HOH   F .   ? 0.6899 0.4798 0.5835 0.2276  0.1242  0.0677  316 HOH   B O   
6992 O O   . HOH   F .   ? 0.4078 0.2162 0.3067 0.1424  0.0880  0.0148  317 HOH   B O   
6993 O O   . HOH   F .   ? 0.2565 0.2907 0.3158 -0.0366 0.0777  -0.0623 318 HOH   B O   
6994 O O   . HOH   F .   ? 0.2315 0.3468 0.4656 -0.0288 -0.0613 0.0114  319 HOH   B O   
6995 O O   . HOH   F .   ? 0.2206 0.2003 0.1844 -0.0042 0.0047  0.0209  320 HOH   B O   
6996 O O   . HOH   F .   ? 0.7623 0.1992 0.2870 -0.0400 -0.0780 0.0133  321 HOH   B O   
6997 O O   . HOH   F .   ? 0.4856 0.3930 0.6515 0.1116  0.0023  0.0985  322 HOH   B O   
6998 O O   . HOH   F .   ? 0.1665 0.2888 0.2619 -0.0153 -0.0338 0.0728  323 HOH   B O   
6999 O O   . HOH   F .   ? 0.2574 0.2100 0.2471 0.0096  -0.0265 0.0089  324 HOH   B O   
7000 O O   . HOH   F .   ? 0.1638 0.1564 0.3146 -0.0164 -0.0158 -0.0180 325 HOH   B O   
7001 O O   . HOH   F .   ? 0.2991 0.3453 0.7455 -0.0136 -0.0441 0.2023  326 HOH   B O   
7002 O O   . HOH   F .   ? 0.4352 0.3357 0.6057 0.1319  0.2356  0.2090  327 HOH   B O   
7003 O O   . HOH   F .   ? 0.5146 0.2391 0.2949 0.0565  0.0460  0.0818  328 HOH   B O   
7004 O O   . HOH   F .   ? 0.4380 0.4781 0.2347 0.0812  -0.0094 -0.0633 329 HOH   B O   
7005 O O   . HOH   F .   ? 0.2000 0.2070 0.3034 0.0378  0.0312  0.0159  330 HOH   B O   
7006 O O   . HOH   F .   ? 0.7435 0.3193 0.3285 -0.0329 0.1166  0.0937  331 HOH   B O   
7007 O O   . HOH   F .   ? 0.7061 0.6077 0.5478 0.3117  0.0192  -0.0171 332 HOH   B O   
7008 O O   . HOH   F .   ? 0.2426 0.5443 0.5137 -0.0719 -0.0005 -0.0701 333 HOH   B O   
7009 O O   . HOH   F .   ? 0.5324 0.4583 0.6548 -0.0459 -0.0588 -0.1429 334 HOH   B O   
7010 O O   . HOH   F .   ? 0.2379 0.2194 0.5278 -0.0474 0.0074  0.1251  335 HOH   B O   
7011 O O   . HOH   F .   ? 0.2658 0.2024 0.5673 -0.0105 -0.0027 0.0200  336 HOH   B O   
7012 O O   . HOH   F .   ? 0.5222 0.5755 0.6714 0.1261  -0.1284 0.2616  337 HOH   B O   
7013 O O   . HOH   F .   ? 0.1667 0.2868 0.2901 0.0245  -0.0136 -0.0628 338 HOH   B O   
7014 O O   . HOH   F .   ? 0.1682 0.1567 0.2436 0.0072  -0.0224 0.0055  339 HOH   B O   
7015 O O   . HOH   F .   ? 0.5680 0.3527 0.3995 0.0579  0.0294  -0.1569 340 HOH   B O   
7016 O O   . HOH   F .   ? 0.5599 0.3580 0.2929 0.1096  -0.1459 -0.0682 341 HOH   B O   
7017 O O   . HOH   F .   ? 0.4228 0.7204 0.3111 0.0676  -0.0276 0.1419  342 HOH   B O   
7018 O O   . HOH   F .   ? 0.3898 0.6027 0.3918 -0.0469 -0.1253 -0.0705 343 HOH   B O   
7019 O O   . HOH   F .   ? 0.2076 0.1956 0.2540 -0.0074 0.0370  -0.0097 344 HOH   B O   
7020 O O   . HOH   F .   ? 0.1654 0.5589 0.5927 -0.0139 -0.0148 0.0515  345 HOH   B O   
7021 O O   . HOH   F .   ? 0.4456 0.4637 0.5020 -0.0011 -0.0780 0.1204  346 HOH   B O   
7022 O O   . HOH   F .   ? 0.5160 0.5613 0.4977 -0.1236 -0.0324 0.1138  347 HOH   B O   
7023 O O   . HOH   F .   ? 0.2612 0.2230 0.5443 -0.0233 -0.0852 -0.0602 348 HOH   B O   
7024 O O   . HOH   F .   ? 0.3838 0.2079 0.3500 -0.0387 -0.0297 -0.0617 349 HOH   B O   
7025 O O   . HOH   F .   ? 0.6634 0.6569 0.2866 0.0844  -0.0442 0.1747  350 HOH   B O   
7026 O O   . HOH   F .   ? 0.5857 0.2516 0.5661 -0.0805 0.2493  -0.0054 351 HOH   B O   
7027 O O   . HOH   F .   ? 0.3339 0.4352 0.4802 -0.1558 0.0269  0.0477  352 HOH   B O   
7028 O O   . HOH   F .   ? 0.2335 0.6091 0.3583 0.1463  -0.0566 -0.1303 353 HOH   B O   
7029 O O   . HOH   F .   ? 0.2319 0.4121 0.4873 0.0244  0.0249  0.0197  354 HOH   B O   
7030 O O   . HOH   F .   ? 0.5283 0.3652 0.3833 0.0789  0.1342  -0.0486 355 HOH   B O   
7031 O O   . HOH   F .   ? 0.4062 0.2671 0.4756 -0.0852 -0.0115 -0.0614 356 HOH   B O   
7032 O O   . HOH   F .   ? 0.5235 0.6341 0.6602 0.0790  0.0547  -0.0564 357 HOH   B O   
7033 O O   . HOH   F .   ? 0.4721 0.5861 0.5461 0.1770  -0.1292 0.2008  358 HOH   B O   
7034 O O   . HOH   F .   ? 0.4697 0.5211 0.5194 -0.0002 -0.0115 0.0452  359 HOH   B O   
7035 O O   . HOH   F .   ? 0.3150 0.2006 0.4226 0.0630  -0.1261 -0.0701 360 HOH   B O   
7036 O O   . HOH   F .   ? 0.6469 0.7654 0.3691 0.3712  0.0243  0.0930  361 HOH   B O   
7037 O O   . HOH   F .   ? 0.4442 0.3468 0.4718 0.0312  -0.1928 -0.0022 362 HOH   B O   
7038 O O   . HOH   F .   ? 0.2313 0.3595 0.7279 -0.0493 -0.0889 -0.0856 363 HOH   B O   
7039 O O   . HOH   F .   ? 0.5330 0.4292 0.7605 -0.0159 0.0910  0.1158  364 HOH   B O   
7040 O O   . HOH   F .   ? 0.4809 0.5851 0.4121 -0.0095 -0.0809 -0.1334 365 HOH   B O   
7041 O O   . HOH   F .   ? 0.7061 0.4742 0.4532 0.1339  0.1112  0.0591  366 HOH   B O   
7042 O O   . HOH   F .   ? 0.5004 0.3811 0.5472 0.0728  -0.1686 0.0121  367 HOH   B O   
7043 O O   . HOH   F .   ? 0.5940 0.6684 0.4113 0.2334  -0.1573 0.0844  368 HOH   B O   
7044 O O   . HOH   F .   ? 0.5236 0.3249 0.5466 -0.1343 -0.0657 0.0196  369 HOH   B O   
7045 O O   . HOH   F .   ? 0.5344 0.6164 0.5676 0.3275  0.0590  0.1295  370 HOH   B O   
7046 O O   . HOH   F .   ? 0.6112 0.2083 0.5193 0.0096  0.0545  0.0520  371 HOH   B O   
7047 O O   . HOH   F .   ? 0.6721 0.4075 0.2751 -0.1406 -0.0684 -0.0419 372 HOH   B O   
7048 O O   . HOH   F .   ? 0.4563 0.3480 0.4307 0.0566  -0.1631 -0.0184 373 HOH   B O   
7049 O O   . HOH   F .   ? 0.3353 0.3728 0.2327 0.0911  0.0191  0.0212  374 HOH   B O   
7050 O O   . HOH   F .   ? 0.2632 0.4155 0.5163 0.0489  -0.0973 -0.0572 375 HOH   B O   
7051 O O   . HOH   F .   ? 0.7210 0.7851 0.5132 0.2616  -0.1429 0.1430  376 HOH   B O   
7052 O O   . HOH   F .   ? 0.4132 0.4997 0.5392 -0.1046 -0.0938 0.0350  377 HOH   B O   
7053 O O   . HOH   F .   ? 0.4919 0.7190 0.6450 0.1761  0.0773  0.3096  378 HOH   B O   
7054 O O   . HOH   F .   ? 0.7801 0.3308 0.6353 -0.0704 0.0089  -0.0532 379 HOH   B O   
7055 O O   . HOH   F .   ? 0.3504 0.4304 0.5947 0.1175  -0.0912 0.0931  380 HOH   B O   
7056 O O   . HOH   F .   ? 0.3113 0.2627 0.3666 0.0031  -0.0015 0.0413  381 HOH   B O   
7057 O O   . HOH   F .   ? 0.5154 0.6987 0.6244 0.0475  0.2127  0.1911  382 HOH   B O   
7058 O O   . HOH   F .   ? 0.3382 0.8315 0.5661 0.0992  0.1620  0.1200  383 HOH   B O   
7059 O O   . HOH   F .   ? 0.5346 0.6828 0.4035 -0.1336 0.0308  -0.1486 384 HOH   B O   
7060 O O   . HOH   F .   ? 0.5972 0.3918 0.4978 -0.0294 -0.0554 0.0159  385 HOH   B O   
7061 O O   . HOH   F .   ? 0.5689 0.4913 0.4074 -0.0480 -0.0595 -0.0454 386 HOH   B O   
7062 O O   . HOH   F .   ? 0.4483 0.3408 0.2818 0.0275  0.0307  -0.0073 387 HOH   B O   
7063 O O   . HOH   F .   ? 0.2363 0.4420 0.3924 -0.0649 -0.0972 -0.0386 388 HOH   B O   
7064 O O   . HOH   F .   ? 0.7776 0.3579 0.4933 0.0415  0.1177  -0.1326 389 HOH   B O   
7065 O O   . HOH   F .   ? 0.7322 0.6234 0.4112 0.3090  0.0207  0.1320  390 HOH   B O   
7066 O O   . HOH   F .   ? 0.3919 0.2204 0.3400 0.0827  -0.0332 0.0193  391 HOH   B O   
7067 O O   . HOH   F .   ? 0.3386 0.4287 0.3260 -0.0380 -0.0099 0.0624  392 HOH   B O   
7068 O O   . HOH   F .   ? 0.4972 0.2224 0.6232 -0.0845 0.1014  0.0523  393 HOH   B O   
7069 O O   . HOH   F .   ? 0.2572 0.5062 0.6333 -0.1651 -0.0619 0.0452  394 HOH   B O   
7070 O O   . HOH   F .   ? 0.4049 0.4134 0.4235 -0.0118 0.0695  0.0850  395 HOH   B O   
7071 O O   . HOH   F .   ? 0.5776 0.7213 0.7915 0.2018  -0.0608 0.2344  396 HOH   B O   
7072 O O   . HOH   F .   ? 0.4756 0.7075 0.3636 0.1652  -0.0044 -0.1107 397 HOH   B O   
7073 O O   . HOH   F .   ? 0.3090 0.3665 0.3324 0.0574  0.0113  -0.0277 398 HOH   B O   
7074 O O   . HOH   F .   ? 0.2219 0.2911 0.6318 -0.0532 -0.1065 0.0209  399 HOH   B O   
7075 O O   . HOH   F .   ? 0.5697 0.4211 0.3197 -0.2310 -0.0438 0.1039  400 HOH   B O   
7076 O O   . HOH   F .   ? 0.6664 0.6429 0.3926 0.1453  -0.0635 0.0854  401 HOH   B O   
# 
