data_7HEY
# 
_entry.id   7HEY 
# 
_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   7HEY         pdb_00007hey 10.2210/pdb7hey/pdb 
WWPDB D_1001407388 ?            ?                   
# 
_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                        7HEY 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                      18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                          114.023   1   ?                      ? ? ? 
3 non-polymer syn '(2S,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' 220.271   1   ?                      ? ? ? 
4 non-polymer syn '(2R,3S)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' 220.271   1   ?                      ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                  35.453    1   ?                      ? ? ? 
6 water       nat water                                                           18.015    422 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                          TFA   
3 '(2S,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' A1BAI 
4 '(2R,3S)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' A1BAJ 
5 'CHLORIDE ION'                                                  CL    
6 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 
A1BAI non-polymer         . '(2S,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' ? 'C11 H16 N4 O'   220.271 
A1BAJ non-polymer         . '(2R,3S)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' ? 'C11 H16 N4 O'   220.271 
ALA   'L-peptide linking' y ALANINE                                                         ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                        ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                      ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                 ? 'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                  ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                           ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'     105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                          ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1BAI 1   202 201  A1BAI LA1 A . 
E 4 A1BAJ 1   203 301  A1BAJ LA2 A . 
F 5 CL    1   204 1    CL    CL  A . 
G 6 HOH   1   301 196  HOH   HOH A . 
G 6 HOH   2   302 405  HOH   HOH A . 
G 6 HOH   3   303 153  HOH   HOH A . 
G 6 HOH   4   304 292  HOH   HOH A . 
G 6 HOH   5   305 13   HOH   HOH A . 
G 6 HOH   6   306 86   HOH   HOH A . 
G 6 HOH   7   307 625  HOH   HOH A . 
G 6 HOH   8   308 1289 HOH   HOH A . 
G 6 HOH   9   309 229  HOH   HOH A . 
G 6 HOH   10  310 493  HOH   HOH A . 
G 6 HOH   11  311 209  HOH   HOH A . 
G 6 HOH   12  312 18   HOH   HOH A . 
G 6 HOH   13  313 5    HOH   HOH A . 
G 6 HOH   14  314 109  HOH   HOH A . 
G 6 HOH   15  315 76   HOH   HOH A . 
G 6 HOH   16  316 1301 HOH   HOH A . 
G 6 HOH   17  317 136  HOH   HOH A . 
G 6 HOH   18  318 1295 HOH   HOH A . 
G 6 HOH   19  319 630  HOH   HOH A . 
G 6 HOH   20  320 236  HOH   HOH A . 
G 6 HOH   21  321 247  HOH   HOH A . 
G 6 HOH   22  322 124  HOH   HOH A . 
G 6 HOH   23  323 148  HOH   HOH A . 
G 6 HOH   24  324 1290 HOH   HOH A . 
G 6 HOH   25  325 70   HOH   HOH A . 
G 6 HOH   26  326 17   HOH   HOH A . 
G 6 HOH   27  327 1094 HOH   HOH A . 
G 6 HOH   28  328 1283 HOH   HOH A . 
G 6 HOH   29  329 21   HOH   HOH A . 
G 6 HOH   30  330 151  HOH   HOH A . 
G 6 HOH   31  331 320  HOH   HOH A . 
G 6 HOH   32  332 8    HOH   HOH A . 
G 6 HOH   33  333 1275 HOH   HOH A . 
G 6 HOH   34  334 164  HOH   HOH A . 
G 6 HOH   35  335 15   HOH   HOH A . 
G 6 HOH   36  336 1300 HOH   HOH A . 
G 6 HOH   37  337 39   HOH   HOH A . 
G 6 HOH   38  338 192  HOH   HOH A . 
G 6 HOH   39  339 140  HOH   HOH A . 
G 6 HOH   40  340 225  HOH   HOH A . 
G 6 HOH   41  341 964  HOH   HOH A . 
G 6 HOH   42  342 409  HOH   HOH A . 
G 6 HOH   43  343 393  HOH   HOH A . 
G 6 HOH   44  344 661  HOH   HOH A . 
G 6 HOH   45  345 469  HOH   HOH A . 
G 6 HOH   46  346 105  HOH   HOH A . 
G 6 HOH   47  347 241  HOH   HOH A . 
G 6 HOH   48  348 165  HOH   HOH A . 
G 6 HOH   49  349 281  HOH   HOH A . 
G 6 HOH   50  350 155  HOH   HOH A . 
G 6 HOH   51  351 92   HOH   HOH A . 
G 6 HOH   52  352 42   HOH   HOH A . 
G 6 HOH   53  353 57   HOH   HOH A . 
G 6 HOH   54  354 33   HOH   HOH A . 
G 6 HOH   55  355 93   HOH   HOH A . 
G 6 HOH   56  356 102  HOH   HOH A . 
G 6 HOH   57  357 2    HOH   HOH A . 
G 6 HOH   58  358 337  HOH   HOH A . 
G 6 HOH   59  359 169  HOH   HOH A . 
G 6 HOH   60  360 4    HOH   HOH A . 
G 6 HOH   61  361 36   HOH   HOH A . 
G 6 HOH   62  362 354  HOH   HOH A . 
G 6 HOH   63  363 139  HOH   HOH A . 
G 6 HOH   64  364 396  HOH   HOH A . 
G 6 HOH   65  365 5    HOH   HOH A . 
G 6 HOH   66  366 45   HOH   HOH A . 
G 6 HOH   67  367 12   HOH   HOH A . 
G 6 HOH   68  368 66   HOH   HOH A . 
G 6 HOH   69  369 81   HOH   HOH A . 
G 6 HOH   70  370 662  HOH   HOH A . 
G 6 HOH   71  371 27   HOH   HOH A . 
G 6 HOH   72  372 19   HOH   HOH A . 
G 6 HOH   73  373 115  HOH   HOH A . 
G 6 HOH   74  374 159  HOH   HOH A . 
G 6 HOH   75  375 162  HOH   HOH A . 
G 6 HOH   76  376 939  HOH   HOH A . 
G 6 HOH   77  377 24   HOH   HOH A . 
G 6 HOH   78  378 138  HOH   HOH A . 
G 6 HOH   79  379 85   HOH   HOH A . 
G 6 HOH   80  380 56   HOH   HOH A . 
G 6 HOH   81  381 46   HOH   HOH A . 
G 6 HOH   82  382 186  HOH   HOH A . 
G 6 HOH   83  383 62   HOH   HOH A . 
G 6 HOH   84  384 1310 HOH   HOH A . 
G 6 HOH   85  385 49   HOH   HOH A . 
G 6 HOH   86  386 26   HOH   HOH A . 
G 6 HOH   87  387 154  HOH   HOH A . 
G 6 HOH   88  388 1    HOH   HOH A . 
G 6 HOH   89  389 134  HOH   HOH A . 
G 6 HOH   90  390 366  HOH   HOH A . 
G 6 HOH   91  391 140  HOH   HOH A . 
G 6 HOH   92  392 35   HOH   HOH A . 
G 6 HOH   93  393 195  HOH   HOH A . 
G 6 HOH   94  394 6    HOH   HOH A . 
G 6 HOH   95  395 296  HOH   HOH A . 
G 6 HOH   96  396 218  HOH   HOH A . 
G 6 HOH   97  397 96   HOH   HOH A . 
G 6 HOH   98  398 74   HOH   HOH A . 
G 6 HOH   99  399 58   HOH   HOH A . 
G 6 HOH   100 400 461  HOH   HOH A . 
G 6 HOH   101 401 116  HOH   HOH A . 
G 6 HOH   102 402 34   HOH   HOH A . 
G 6 HOH   103 403 12   HOH   HOH A . 
G 6 HOH   104 404 121  HOH   HOH A . 
G 6 HOH   105 405 1308 HOH   HOH A . 
G 6 HOH   106 406 199  HOH   HOH A . 
G 6 HOH   107 407 351  HOH   HOH A . 
G 6 HOH   108 408 303  HOH   HOH A . 
G 6 HOH   109 409 83   HOH   HOH A . 
G 6 HOH   110 410 333  HOH   HOH A . 
G 6 HOH   111 411 11   HOH   HOH A . 
G 6 HOH   112 412 1315 HOH   HOH A . 
G 6 HOH   113 413 1068 HOH   HOH A . 
G 6 HOH   114 414 67   HOH   HOH A . 
G 6 HOH   115 415 3    HOH   HOH A . 
G 6 HOH   116 416 7    HOH   HOH A . 
G 6 HOH   117 417 25   HOH   HOH A . 
G 6 HOH   118 418 68   HOH   HOH A . 
G 6 HOH   119 419 1313 HOH   HOH A . 
G 6 HOH   120 420 156  HOH   HOH A . 
G 6 HOH   121 421 1279 HOH   HOH A . 
G 6 HOH   122 422 125  HOH   HOH A . 
G 6 HOH   123 423 123  HOH   HOH A . 
G 6 HOH   124 424 278  HOH   HOH A . 
G 6 HOH   125 425 381  HOH   HOH A . 
G 6 HOH   126 426 397  HOH   HOH A . 
G 6 HOH   127 427 4    HOH   HOH A . 
G 6 HOH   128 428 51   HOH   HOH A . 
G 6 HOH   129 429 78   HOH   HOH A . 
G 6 HOH   130 430 53   HOH   HOH A . 
G 6 HOH   131 431 122  HOH   HOH A . 
G 6 HOH   132 432 95   HOH   HOH A . 
G 6 HOH   133 433 132  HOH   HOH A . 
G 6 HOH   134 434 1296 HOH   HOH A . 
G 6 HOH   135 435 1222 HOH   HOH A . 
G 6 HOH   136 436 582  HOH   HOH A . 
G 6 HOH   137 437 71   HOH   HOH A . 
G 6 HOH   138 438 212  HOH   HOH A . 
G 6 HOH   139 439 80   HOH   HOH A . 
G 6 HOH   140 440 188  HOH   HOH A . 
G 6 HOH   141 441 73   HOH   HOH A . 
G 6 HOH   142 442 1309 HOH   HOH A . 
G 6 HOH   143 443 1238 HOH   HOH A . 
G 6 HOH   144 444 16   HOH   HOH A . 
G 6 HOH   145 445 952  HOH   HOH A . 
G 6 HOH   146 446 1189 HOH   HOH A . 
G 6 HOH   147 447 40   HOH   HOH A . 
G 6 HOH   148 448 94   HOH   HOH A . 
G 6 HOH   149 449 1286 HOH   HOH A . 
G 6 HOH   150 450 79   HOH   HOH A . 
G 6 HOH   151 451 97   HOH   HOH A . 
G 6 HOH   152 452 944  HOH   HOH A . 
G 6 HOH   153 453 14   HOH   HOH A . 
G 6 HOH   154 454 104  HOH   HOH A . 
G 6 HOH   155 455 576  HOH   HOH A . 
G 6 HOH   156 456 10   HOH   HOH A . 
G 6 HOH   157 457 1119 HOH   HOH A . 
G 6 HOH   158 458 330  HOH   HOH A . 
G 6 HOH   159 459 7    HOH   HOH A . 
G 6 HOH   160 460 1134 HOH   HOH A . 
G 6 HOH   161 461 509  HOH   HOH A . 
G 6 HOH   162 462 3    HOH   HOH A . 
G 6 HOH   163 463 107  HOH   HOH A . 
G 6 HOH   164 464 8    HOH   HOH A . 
G 6 HOH   165 465 408  HOH   HOH A . 
G 6 HOH   166 466 726  HOH   HOH A . 
G 6 HOH   167 467 163  HOH   HOH A . 
G 6 HOH   168 468 756  HOH   HOH A . 
G 6 HOH   169 469 361  HOH   HOH A . 
G 6 HOH   170 470 1276 HOH   HOH A . 
G 6 HOH   171 471 126  HOH   HOH A . 
G 6 HOH   172 472 319  HOH   HOH A . 
G 6 HOH   173 473 556  HOH   HOH A . 
G 6 HOH   174 474 801  HOH   HOH A . 
G 6 HOH   175 475 280  HOH   HOH A . 
G 6 HOH   176 476 1307 HOH   HOH A . 
G 6 HOH   177 477 342  HOH   HOH A . 
G 6 HOH   178 478 63   HOH   HOH A . 
G 6 HOH   179 479 250  HOH   HOH A . 
G 6 HOH   180 480 370  HOH   HOH A . 
G 6 HOH   181 481 267  HOH   HOH A . 
G 6 HOH   182 482 6    HOH   HOH A . 
G 6 HOH   183 483 1287 HOH   HOH A . 
G 6 HOH   184 484 224  HOH   HOH A . 
G 6 HOH   185 485 202  HOH   HOH A . 
G 6 HOH   186 486 695  HOH   HOH A . 
G 6 HOH   187 487 1306 HOH   HOH A . 
G 6 HOH   188 488 326  HOH   HOH A . 
G 6 HOH   189 489 674  HOH   HOH A . 
G 6 HOH   190 490 135  HOH   HOH A . 
G 6 HOH   191 491 919  HOH   HOH A . 
G 6 HOH   192 492 309  HOH   HOH A . 
G 6 HOH   193 493 318  HOH   HOH A . 
G 6 HOH   194 494 1299 HOH   HOH A . 
G 6 HOH   195 495 315  HOH   HOH A . 
G 6 HOH   196 496 1314 HOH   HOH A . 
G 6 HOH   197 497 521  HOH   HOH A . 
G 6 HOH   198 498 711  HOH   HOH A . 
G 6 HOH   199 499 331  HOH   HOH A . 
G 6 HOH   200 500 805  HOH   HOH A . 
G 6 HOH   201 501 941  HOH   HOH A . 
G 6 HOH   202 502 263  HOH   HOH A . 
G 6 HOH   203 503 152  HOH   HOH A . 
G 6 HOH   204 504 208  HOH   HOH A . 
G 6 HOH   205 505 356  HOH   HOH A . 
G 6 HOH   206 506 1284 HOH   HOH A . 
G 6 HOH   207 507 180  HOH   HOH A . 
G 6 HOH   208 508 1071 HOH   HOH A . 
G 6 HOH   209 509 350  HOH   HOH A . 
G 6 HOH   210 510 363  HOH   HOH A . 
G 6 HOH   211 511 371  HOH   HOH A . 
G 6 HOH   212 512 313  HOH   HOH A . 
G 6 HOH   213 513 9    HOH   HOH A . 
G 6 HOH   214 514 185  HOH   HOH A . 
G 6 HOH   215 515 429  HOH   HOH A . 
G 6 HOH   216 516 70   HOH   HOH A . 
G 6 HOH   217 517 772  HOH   HOH A . 
G 6 HOH   218 518 376  HOH   HOH A . 
G 6 HOH   219 519 1074 HOH   HOH A . 
G 6 HOH   220 520 346  HOH   HOH A . 
G 6 HOH   221 521 1292 HOH   HOH A . 
G 6 HOH   222 522 1078 HOH   HOH A . 
H 6 HOH   1   201 64   HOH   HOH B . 
H 6 HOH   2   202 900  HOH   HOH B . 
H 6 HOH   3   203 358  HOH   HOH B . 
H 6 HOH   4   204 549  HOH   HOH B . 
H 6 HOH   5   205 758  HOH   HOH B . 
H 6 HOH   6   206 531  HOH   HOH B . 
H 6 HOH   7   207 364  HOH   HOH B . 
H 6 HOH   8   208 240  HOH   HOH B . 
H 6 HOH   9   209 1249 HOH   HOH B . 
H 6 HOH   10  210 353  HOH   HOH B . 
H 6 HOH   11  211 452  HOH   HOH B . 
H 6 HOH   12  212 50   HOH   HOH B . 
H 6 HOH   13  213 120  HOH   HOH B . 
H 6 HOH   14  214 654  HOH   HOH B . 
H 6 HOH   15  215 743  HOH   HOH B . 
H 6 HOH   16  216 398  HOH   HOH B . 
H 6 HOH   17  217 264  HOH   HOH B . 
H 6 HOH   18  218 1140 HOH   HOH B . 
H 6 HOH   19  219 343  HOH   HOH B . 
H 6 HOH   20  220 131  HOH   HOH B . 
H 6 HOH   21  221 444  HOH   HOH B . 
H 6 HOH   22  222 332  HOH   HOH B . 
H 6 HOH   23  223 282  HOH   HOH B . 
H 6 HOH   24  224 1278 HOH   HOH B . 
H 6 HOH   25  225 54   HOH   HOH B . 
H 6 HOH   26  226 232  HOH   HOH B . 
H 6 HOH   27  227 82   HOH   HOH B . 
H 6 HOH   28  228 276  HOH   HOH B . 
H 6 HOH   29  229 75   HOH   HOH B . 
H 6 HOH   30  230 1312 HOH   HOH B . 
H 6 HOH   31  231 272  HOH   HOH B . 
H 6 HOH   32  232 60   HOH   HOH B . 
H 6 HOH   33  233 205  HOH   HOH B . 
H 6 HOH   34  234 300  HOH   HOH B . 
H 6 HOH   35  235 127  HOH   HOH B . 
H 6 HOH   36  236 128  HOH   HOH B . 
H 6 HOH   37  237 723  HOH   HOH B . 
H 6 HOH   38  238 1    HOH   HOH B . 
H 6 HOH   39  239 181  HOH   HOH B . 
H 6 HOH   40  240 69   HOH   HOH B . 
H 6 HOH   41  241 143  HOH   HOH B . 
H 6 HOH   42  242 252  HOH   HOH B . 
H 6 HOH   43  243 52   HOH   HOH B . 
H 6 HOH   44  244 14   HOH   HOH B . 
H 6 HOH   45  245 110  HOH   HOH B . 
H 6 HOH   46  246 133  HOH   HOH B . 
H 6 HOH   47  247 144  HOH   HOH B . 
H 6 HOH   48  248 129  HOH   HOH B . 
H 6 HOH   49  249 9    HOH   HOH B . 
H 6 HOH   50  250 325  HOH   HOH B . 
H 6 HOH   51  251 172  HOH   HOH B . 
H 6 HOH   52  252 30   HOH   HOH B . 
H 6 HOH   53  253 166  HOH   HOH B . 
H 6 HOH   54  254 391  HOH   HOH B . 
H 6 HOH   55  255 31   HOH   HOH B . 
H 6 HOH   56  256 271  HOH   HOH B . 
H 6 HOH   57  257 242  HOH   HOH B . 
H 6 HOH   58  258 72   HOH   HOH B . 
H 6 HOH   59  259 41   HOH   HOH B . 
H 6 HOH   60  260 231  HOH   HOH B . 
H 6 HOH   61  261 150  HOH   HOH B . 
H 6 HOH   62  262 47   HOH   HOH B . 
H 6 HOH   63  263 59   HOH   HOH B . 
H 6 HOH   64  264 103  HOH   HOH B . 
H 6 HOH   65  265 347  HOH   HOH B . 
H 6 HOH   66  266 10   HOH   HOH B . 
H 6 HOH   67  267 61   HOH   HOH B . 
H 6 HOH   68  268 11   HOH   HOH B . 
H 6 HOH   69  269 243  HOH   HOH B . 
H 6 HOH   70  270 20   HOH   HOH B . 
H 6 HOH   71  271 175  HOH   HOH B . 
H 6 HOH   72  272 221  HOH   HOH B . 
H 6 HOH   73  273 117  HOH   HOH B . 
H 6 HOH   74  274 77   HOH   HOH B . 
H 6 HOH   75  275 84   HOH   HOH B . 
H 6 HOH   76  276 1277 HOH   HOH B . 
H 6 HOH   77  277 302  HOH   HOH B . 
H 6 HOH   78  278 147  HOH   HOH B . 
H 6 HOH   79  279 114  HOH   HOH B . 
H 6 HOH   80  280 43   HOH   HOH B . 
H 6 HOH   81  281 287  HOH   HOH B . 
H 6 HOH   82  282 387  HOH   HOH B . 
H 6 HOH   83  283 22   HOH   HOH B . 
H 6 HOH   84  284 220  HOH   HOH B . 
H 6 HOH   85  285 235  HOH   HOH B . 
H 6 HOH   86  286 137  HOH   HOH B . 
H 6 HOH   87  287 1305 HOH   HOH B . 
H 6 HOH   88  288 1106 HOH   HOH B . 
H 6 HOH   89  289 106  HOH   HOH B . 
H 6 HOH   90  290 89   HOH   HOH B . 
H 6 HOH   91  291 88   HOH   HOH B . 
H 6 HOH   92  292 13   HOH   HOH B . 
H 6 HOH   93  293 341  HOH   HOH B . 
H 6 HOH   94  294 216  HOH   HOH B . 
H 6 HOH   95  295 1066 HOH   HOH B . 
H 6 HOH   96  296 99   HOH   HOH B . 
H 6 HOH   97  297 635  HOH   HOH B . 
H 6 HOH   98  298 416  HOH   HOH B . 
H 6 HOH   99  299 141  HOH   HOH B . 
H 6 HOH   100 300 142  HOH   HOH B . 
H 6 HOH   101 301 299  HOH   HOH B . 
H 6 HOH   102 302 160  HOH   HOH B . 
H 6 HOH   103 303 32   HOH   HOH B . 
H 6 HOH   104 304 1285 HOH   HOH B . 
H 6 HOH   105 305 112  HOH   HOH B . 
H 6 HOH   106 306 297  HOH   HOH B . 
H 6 HOH   107 307 311  HOH   HOH B . 
H 6 HOH   108 308 316  HOH   HOH B . 
H 6 HOH   109 309 215  HOH   HOH B . 
H 6 HOH   110 310 118  HOH   HOH B . 
H 6 HOH   111 311 101  HOH   HOH B . 
H 6 HOH   112 312 48   HOH   HOH B . 
H 6 HOH   113 313 1274 HOH   HOH B . 
H 6 HOH   114 314 38   HOH   HOH B . 
H 6 HOH   115 315 161  HOH   HOH B . 
H 6 HOH   116 316 37   HOH   HOH B . 
H 6 HOH   117 317 170  HOH   HOH B . 
H 6 HOH   118 318 23   HOH   HOH B . 
H 6 HOH   119 319 177  HOH   HOH B . 
H 6 HOH   120 320 704  HOH   HOH B . 
H 6 HOH   121 321 197  HOH   HOH B . 
H 6 HOH   122 322 28   HOH   HOH B . 
H 6 HOH   123 323 91   HOH   HOH B . 
H 6 HOH   124 324 44   HOH   HOH B . 
H 6 HOH   125 325 100  HOH   HOH B . 
H 6 HOH   126 326 1291 HOH   HOH B . 
H 6 HOH   127 327 182  HOH   HOH B . 
H 6 HOH   128 328 1126 HOH   HOH B . 
H 6 HOH   129 329 1294 HOH   HOH B . 
H 6 HOH   130 330 29   HOH   HOH B . 
H 6 HOH   131 331 334  HOH   HOH B . 
H 6 HOH   132 332 55   HOH   HOH B . 
H 6 HOH   133 333 98   HOH   HOH B . 
H 6 HOH   134 334 717  HOH   HOH B . 
H 6 HOH   135 335 207  HOH   HOH B . 
H 6 HOH   136 336 1293 HOH   HOH B . 
H 6 HOH   137 337 234  HOH   HOH B . 
H 6 HOH   138 338 65   HOH   HOH B . 
H 6 HOH   139 339 445  HOH   HOH B . 
H 6 HOH   140 340 619  HOH   HOH B . 
H 6 HOH   141 341 339  HOH   HOH B . 
H 6 HOH   142 342 178  HOH   HOH B . 
H 6 HOH   143 343 362  HOH   HOH B . 
H 6 HOH   144 344 960  HOH   HOH B . 
H 6 HOH   145 345 90   HOH   HOH B . 
H 6 HOH   146 346 463  HOH   HOH B . 
H 6 HOH   147 347 623  HOH   HOH B . 
H 6 HOH   148 348 191  HOH   HOH B . 
H 6 HOH   149 349 335  HOH   HOH B . 
H 6 HOH   150 350 1304 HOH   HOH B . 
H 6 HOH   151 351 1046 HOH   HOH B . 
H 6 HOH   152 352 87   HOH   HOH B . 
H 6 HOH   153 353 304  HOH   HOH B . 
H 6 HOH   154 354 1280 HOH   HOH B . 
H 6 HOH   155 355 203  HOH   HOH B . 
H 6 HOH   156 356 541  HOH   HOH B . 
H 6 HOH   157 357 290  HOH   HOH B . 
H 6 HOH   158 358 479  HOH   HOH B . 
H 6 HOH   159 359 389  HOH   HOH B . 
H 6 HOH   160 360 1077 HOH   HOH B . 
H 6 HOH   161 361 718  HOH   HOH B . 
H 6 HOH   162 362 1072 HOH   HOH B . 
H 6 HOH   163 363 283  HOH   HOH B . 
H 6 HOH   164 364 1316 HOH   HOH B . 
H 6 HOH   165 365 898  HOH   HOH B . 
H 6 HOH   166 366 340  HOH   HOH B . 
H 6 HOH   167 367 373  HOH   HOH B . 
H 6 HOH   168 368 615  HOH   HOH B . 
H 6 HOH   169 369 1303 HOH   HOH B . 
H 6 HOH   170 370 291  HOH   HOH B . 
H 6 HOH   171 371 667  HOH   HOH B . 
H 6 HOH   172 372 190  HOH   HOH B . 
H 6 HOH   173 373 310  HOH   HOH B . 
H 6 HOH   174 374 431  HOH   HOH B . 
H 6 HOH   175 375 149  HOH   HOH B . 
H 6 HOH   176 376 1163 HOH   HOH B . 
H 6 HOH   177 377 183  HOH   HOH B . 
H 6 HOH   178 378 1173 HOH   HOH B . 
H 6 HOH   179 379 1000 HOH   HOH B . 
H 6 HOH   180 380 418  HOH   HOH B . 
H 6 HOH   181 381 1311 HOH   HOH B . 
H 6 HOH   182 382 176  HOH   HOH B . 
H 6 HOH   183 383 424  HOH   HOH B . 
H 6 HOH   184 384 491  HOH   HOH B . 
H 6 HOH   185 385 981  HOH   HOH B . 
H 6 HOH   186 386 470  HOH   HOH B . 
H 6 HOH   187 387 1298 HOH   HOH B . 
H 6 HOH   188 388 248  HOH   HOH B . 
H 6 HOH   189 389 265  HOH   HOH B . 
H 6 HOH   190 390 184  HOH   HOH B . 
H 6 HOH   191 391 360  HOH   HOH B . 
H 6 HOH   192 392 355  HOH   HOH B . 
H 6 HOH   193 393 410  HOH   HOH B . 
H 6 HOH   194 394 274  HOH   HOH B . 
H 6 HOH   195 395 566  HOH   HOH B . 
H 6 HOH   196 396 314  HOH   HOH B . 
H 6 HOH   197 397 157  HOH   HOH B . 
H 6 HOH   198 398 321  HOH   HOH B . 
H 6 HOH   199 399 792  HOH   HOH B . 
H 6 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEY 
_cell.length_a           88.766 
_cell.length_b           88.766 
_cell.length_c           39.531 
_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                         7HEY 
_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          7HEY 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.68 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-28 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HEY 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156162 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.047 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.500 
_reflns.B_iso_Wilson_estimate        12.130 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.051 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1006780 
_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 1.020 1.040  ? 41347 7431 ? 1.309 ? ? ? 5.600 ? 0.900  ? ? ? ? ? ? 96.400 1.447 0.601 0.611 
1 2 5.590 44.380 ? 7126  1039 ? 0.026 ? ? ? 6.900 ? 51.600 ? ? ? ? ? ? 99.800 0.029 0.011 0.999 
# 
_refine.entry_id                                 7HEY 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7200 
_refine.ls_number_reflns_obs                     156084 
_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                          0.1446 
_refine.ls_R_factor_R_work                       0.1439 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1583 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7528 
_refine.ls_number_reflns_R_work                  148556 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.9711 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1000 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                66.360 
_refine.B_iso_min                                8.480 
_refine.pdbx_overall_phase_error                 17.1700 
_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                       1.0200 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         72 
_refine_hist.number_atoms_solvent             422 
_refine_hist.number_atoms_total               3036 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           17.69 
_refine_hist.pdbx_B_iso_mean_solvent          30.13 
_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 
1.0200 1.0300  30 94.0000  4689 . 0.3695 0.3832 . 193 0.0000 4882 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4954 . 0.3067 0.3109 . 278 0.0000 5232 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4852 . 0.2609 0.2735 . 277 0.0000 5129 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4931 . 0.2408 0.2574 . 279 0.0000 5210 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4914 . 0.2319 0.2418 . 237 0.0000 5151 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4976 . 0.2070 0.2503 . 236 0.0000 5212 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4882 . 0.1901 0.2061 . 268 0.0000 5150 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4984 . 0.1815 0.1964 . 214 0.0000 5198 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4947 . 0.1636 0.1817 . 243 0.0000 5190 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4967 . 0.1488 0.1665 . 262 0.0000 5229 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4906 . 0.1420 0.1670 . 246 0.0000 5152 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4906 . 0.1323 0.1609 . 270 0.0000 5176 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5038 . 0.1272 0.1555 . 219 0.0000 5257 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4904 . 0.1264 0.1454 . 250 0.0000 5154 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4956 . 0.1266 0.1557 . 249 0.0000 5205 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4921 . 0.1268 0.1389 . 267 0.0000 5188 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4964 . 0.1303 0.1461 . 251 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4944 . 0.1287 0.1518 . 256 0.0000 5200 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4969 . 0.1272 0.1493 . 246 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4957 . 0.1242 0.1408 . 244 0.0000 5201 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4991 . 0.1181 0.1381 . 235 0.0000 5226 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4945 . 0.1178 0.1290 . 265 0.0000 5210 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4954 . 0.1195 0.1319 . 260 0.0000 5214 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5016 . 0.1278 0.1436 . 206 0.0000 5222 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4951 . 0.1305 0.1429 . 294 0.0000 5245 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4986 . 0.1342 0.1413 . 242 0.0000 5228 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4943 . 0.1367 0.1419 . 286 0.0000 5229 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5013 . 0.1375 0.1403 . 255 0.0000 5268 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5022 . 0.1498 0.1649 . 249 0.0000 5271 . 'X-RAY DIFFRACTION' 
3.1700 44.3800 30 100.0000 5174 . 0.1506 0.1732 . 251 0.0000 5425 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEY 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003635' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEY 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_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 7HEY A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEY 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 7HEY SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEY MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEY SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEY MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEY 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.84  -133.42 
2 1 SER A 128 ? B 70.83  -8.07   
3 1 PHE A 156 ? B -97.16 50.29   
4 1 HIS B 86  ? ? 57.05  -128.29 
# 
_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 ? 5.86 . 
2 1 O ? A HOH 521 ? 6.00 . 
3 1 O ? A HOH 522 ? 7.50 . 
4 1 O ? B HOH 400 ? 6.22 . 
# 
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 
A1BAI N2   N  Y N 1   
A1BAI C3   C  N R 2   
A1BAI C6   C  Y N 3   
A1BAI C9   C  Y N 4   
A1BAI C1   C  N N 5   
A1BAI C10  C  N S 6   
A1BAI C11  C  N N 7   
A1BAI C2   C  N N 8   
A1BAI C4   C  Y N 9   
A1BAI C5   C  Y N 10  
A1BAI C7   C  Y N 11  
A1BAI C8   C  Y N 12  
A1BAI N1   N  N N 13  
A1BAI N3   N  Y N 14  
A1BAI N4   N  Y N 15  
A1BAI O1   O  N N 16  
A1BAI H1   H  N N 17  
A1BAI H11  H  N N 18  
A1BAI H5   H  N N 19  
A1BAI H3   H  N N 20  
A1BAI H4   H  N N 21  
A1BAI H2   H  N N 22  
A1BAI H14  H  N N 23  
A1BAI H13  H  N N 24  
A1BAI H15  H  N N 25  
A1BAI H6   H  N N 26  
A1BAI H7   H  N N 27  
A1BAI H9   H  N N 28  
A1BAI H10  H  N N 29  
A1BAI H8   H  N N 30  
A1BAI H12  H  N N 31  
A1BAI H16  H  N N 32  
A1BAJ O1   O  N N 33  
A1BAJ C1   C  N N 34  
A1BAJ C2   C  N N 35  
A1BAJ C3   C  N S 36  
A1BAJ C4   C  Y N 37  
A1BAJ C5   C  Y N 38  
A1BAJ C6   C  Y N 39  
A1BAJ C7   C  Y N 40  
A1BAJ C8   C  Y N 41  
A1BAJ C10  C  N R 42  
A1BAJ C11  C  N N 43  
A1BAJ C9   C  Y N 44  
A1BAJ N1   N  N N 45  
A1BAJ N2   N  Y N 46  
A1BAJ N3   N  Y N 47  
A1BAJ N4   N  Y N 48  
A1BAJ H16  H  N N 49  
A1BAJ H3   H  N N 50  
A1BAJ H5   H  N N 51  
A1BAJ H4   H  N N 52  
A1BAJ H6   H  N N 53  
A1BAJ H7   H  N N 54  
A1BAJ H1   H  N N 55  
A1BAJ H9   H  N N 56  
A1BAJ H10  H  N N 57  
A1BAJ H2   H  N N 58  
A1BAJ H15  H  N N 59  
A1BAJ H14  H  N N 60  
A1BAJ H13  H  N N 61  
A1BAJ H11  H  N N 62  
A1BAJ H8   H  N N 63  
A1BAJ H12  H  N N 64  
ALA   N    N  N N 65  
ALA   CA   C  N S 66  
ALA   C    C  N N 67  
ALA   O    O  N N 68  
ALA   CB   C  N N 69  
ALA   OXT  O  N N 70  
ALA   H    H  N N 71  
ALA   H2   H  N N 72  
ALA   HA   H  N N 73  
ALA   HB1  H  N N 74  
ALA   HB2  H  N N 75  
ALA   HB3  H  N N 76  
ALA   HXT  H  N N 77  
ARG   N    N  N N 78  
ARG   CA   C  N S 79  
ARG   C    C  N N 80  
ARG   O    O  N N 81  
ARG   CB   C  N N 82  
ARG   CG   C  N N 83  
ARG   CD   C  N N 84  
ARG   NE   N  N N 85  
ARG   CZ   C  N N 86  
ARG   NH1  N  N N 87  
ARG   NH2  N  N N 88  
ARG   OXT  O  N N 89  
ARG   H    H  N N 90  
ARG   H2   H  N N 91  
ARG   HA   H  N N 92  
ARG   HB2  H  N N 93  
ARG   HB3  H  N N 94  
ARG   HG2  H  N N 95  
ARG   HG3  H  N N 96  
ARG   HD2  H  N N 97  
ARG   HD3  H  N N 98  
ARG   HE   H  N N 99  
ARG   HH11 H  N N 100 
ARG   HH12 H  N N 101 
ARG   HH21 H  N N 102 
ARG   HH22 H  N N 103 
ARG   HXT  H  N N 104 
ASN   N    N  N N 105 
ASN   CA   C  N S 106 
ASN   C    C  N N 107 
ASN   O    O  N N 108 
ASN   CB   C  N N 109 
ASN   CG   C  N N 110 
ASN   OD1  O  N N 111 
ASN   ND2  N  N N 112 
ASN   OXT  O  N N 113 
ASN   H    H  N N 114 
ASN   H2   H  N N 115 
ASN   HA   H  N N 116 
ASN   HB2  H  N N 117 
ASN   HB3  H  N N 118 
ASN   HD21 H  N N 119 
ASN   HD22 H  N N 120 
ASN   HXT  H  N N 121 
ASP   N    N  N N 122 
ASP   CA   C  N S 123 
ASP   C    C  N N 124 
ASP   O    O  N N 125 
ASP   CB   C  N N 126 
ASP   CG   C  N N 127 
ASP   OD1  O  N N 128 
ASP   OD2  O  N N 129 
ASP   OXT  O  N N 130 
ASP   H    H  N N 131 
ASP   H2   H  N N 132 
ASP   HA   H  N N 133 
ASP   HB2  H  N N 134 
ASP   HB3  H  N N 135 
ASP   HD2  H  N N 136 
ASP   HXT  H  N N 137 
CL    CL   CL N N 138 
CYS   N    N  N N 139 
CYS   CA   C  N R 140 
CYS   C    C  N N 141 
CYS   O    O  N N 142 
CYS   CB   C  N N 143 
CYS   SG   S  N N 144 
CYS   OXT  O  N N 145 
CYS   H    H  N N 146 
CYS   H2   H  N N 147 
CYS   HA   H  N N 148 
CYS   HB2  H  N N 149 
CYS   HB3  H  N N 150 
CYS   HG   H  N N 151 
CYS   HXT  H  N N 152 
GLN   N    N  N N 153 
GLN   CA   C  N S 154 
GLN   C    C  N N 155 
GLN   O    O  N N 156 
GLN   CB   C  N N 157 
GLN   CG   C  N N 158 
GLN   CD   C  N N 159 
GLN   OE1  O  N N 160 
GLN   NE2  N  N N 161 
GLN   OXT  O  N N 162 
GLN   H    H  N N 163 
GLN   H2   H  N N 164 
GLN   HA   H  N N 165 
GLN   HB2  H  N N 166 
GLN   HB3  H  N N 167 
GLN   HG2  H  N N 168 
GLN   HG3  H  N N 169 
GLN   HE21 H  N N 170 
GLN   HE22 H  N N 171 
GLN   HXT  H  N N 172 
GLU   N    N  N N 173 
GLU   CA   C  N S 174 
GLU   C    C  N N 175 
GLU   O    O  N N 176 
GLU   CB   C  N N 177 
GLU   CG   C  N N 178 
GLU   CD   C  N N 179 
GLU   OE1  O  N N 180 
GLU   OE2  O  N N 181 
GLU   OXT  O  N N 182 
GLU   H    H  N N 183 
GLU   H2   H  N N 184 
GLU   HA   H  N N 185 
GLU   HB2  H  N N 186 
GLU   HB3  H  N N 187 
GLU   HG2  H  N N 188 
GLU   HG3  H  N N 189 
GLU   HE2  H  N N 190 
GLU   HXT  H  N N 191 
GLY   N    N  N N 192 
GLY   CA   C  N N 193 
GLY   C    C  N N 194 
GLY   O    O  N N 195 
GLY   OXT  O  N N 196 
GLY   H    H  N N 197 
GLY   H2   H  N N 198 
GLY   HA2  H  N N 199 
GLY   HA3  H  N N 200 
GLY   HXT  H  N N 201 
HIS   N    N  N N 202 
HIS   CA   C  N S 203 
HIS   C    C  N N 204 
HIS   O    O  N N 205 
HIS   CB   C  N N 206 
HIS   CG   C  Y N 207 
HIS   ND1  N  Y N 208 
HIS   CD2  C  Y N 209 
HIS   CE1  C  Y N 210 
HIS   NE2  N  Y N 211 
HIS   OXT  O  N N 212 
HIS   H    H  N N 213 
HIS   H2   H  N N 214 
HIS   HA   H  N N 215 
HIS   HB2  H  N N 216 
HIS   HB3  H  N N 217 
HIS   HD1  H  N N 218 
HIS   HD2  H  N N 219 
HIS   HE1  H  N N 220 
HIS   HE2  H  N N 221 
HIS   HXT  H  N N 222 
HOH   O    O  N N 223 
HOH   H1   H  N N 224 
HOH   H2   H  N N 225 
ILE   N    N  N N 226 
ILE   CA   C  N S 227 
ILE   C    C  N N 228 
ILE   O    O  N N 229 
ILE   CB   C  N S 230 
ILE   CG1  C  N N 231 
ILE   CG2  C  N N 232 
ILE   CD1  C  N N 233 
ILE   OXT  O  N N 234 
ILE   H    H  N N 235 
ILE   H2   H  N N 236 
ILE   HA   H  N N 237 
ILE   HB   H  N N 238 
ILE   HG12 H  N N 239 
ILE   HG13 H  N N 240 
ILE   HG21 H  N N 241 
ILE   HG22 H  N N 242 
ILE   HG23 H  N N 243 
ILE   HD11 H  N N 244 
ILE   HD12 H  N N 245 
ILE   HD13 H  N N 246 
ILE   HXT  H  N N 247 
LEU   N    N  N N 248 
LEU   CA   C  N S 249 
LEU   C    C  N N 250 
LEU   O    O  N N 251 
LEU   CB   C  N N 252 
LEU   CG   C  N N 253 
LEU   CD1  C  N N 254 
LEU   CD2  C  N N 255 
LEU   OXT  O  N N 256 
LEU   H    H  N N 257 
LEU   H2   H  N N 258 
LEU   HA   H  N N 259 
LEU   HB2  H  N N 260 
LEU   HB3  H  N N 261 
LEU   HG   H  N N 262 
LEU   HD11 H  N N 263 
LEU   HD12 H  N N 264 
LEU   HD13 H  N N 265 
LEU   HD21 H  N N 266 
LEU   HD22 H  N N 267 
LEU   HD23 H  N N 268 
LEU   HXT  H  N N 269 
LYS   N    N  N N 270 
LYS   CA   C  N S 271 
LYS   C    C  N N 272 
LYS   O    O  N N 273 
LYS   CB   C  N N 274 
LYS   CG   C  N N 275 
LYS   CD   C  N N 276 
LYS   CE   C  N N 277 
LYS   NZ   N  N N 278 
LYS   OXT  O  N N 279 
LYS   H    H  N N 280 
LYS   H2   H  N N 281 
LYS   HA   H  N N 282 
LYS   HB2  H  N N 283 
LYS   HB3  H  N N 284 
LYS   HG2  H  N N 285 
LYS   HG3  H  N N 286 
LYS   HD2  H  N N 287 
LYS   HD3  H  N N 288 
LYS   HE2  H  N N 289 
LYS   HE3  H  N N 290 
LYS   HZ1  H  N N 291 
LYS   HZ2  H  N N 292 
LYS   HZ3  H  N N 293 
LYS   HXT  H  N N 294 
MET   N    N  N N 295 
MET   CA   C  N S 296 
MET   C    C  N N 297 
MET   O    O  N N 298 
MET   CB   C  N N 299 
MET   CG   C  N N 300 
MET   SD   S  N N 301 
MET   CE   C  N N 302 
MET   OXT  O  N N 303 
MET   H    H  N N 304 
MET   H2   H  N N 305 
MET   HA   H  N N 306 
MET   HB2  H  N N 307 
MET   HB3  H  N N 308 
MET   HG2  H  N N 309 
MET   HG3  H  N N 310 
MET   HE1  H  N N 311 
MET   HE2  H  N N 312 
MET   HE3  H  N N 313 
MET   HXT  H  N N 314 
PHE   N    N  N N 315 
PHE   CA   C  N S 316 
PHE   C    C  N N 317 
PHE   O    O  N N 318 
PHE   CB   C  N N 319 
PHE   CG   C  Y N 320 
PHE   CD1  C  Y N 321 
PHE   CD2  C  Y N 322 
PHE   CE1  C  Y N 323 
PHE   CE2  C  Y N 324 
PHE   CZ   C  Y N 325 
PHE   OXT  O  N N 326 
PHE   H    H  N N 327 
PHE   H2   H  N N 328 
PHE   HA   H  N N 329 
PHE   HB2  H  N N 330 
PHE   HB3  H  N N 331 
PHE   HD1  H  N N 332 
PHE   HD2  H  N N 333 
PHE   HE1  H  N N 334 
PHE   HE2  H  N N 335 
PHE   HZ   H  N N 336 
PHE   HXT  H  N N 337 
PRO   N    N  N N 338 
PRO   CA   C  N S 339 
PRO   C    C  N N 340 
PRO   O    O  N N 341 
PRO   CB   C  N N 342 
PRO   CG   C  N N 343 
PRO   CD   C  N N 344 
PRO   OXT  O  N N 345 
PRO   H    H  N N 346 
PRO   HA   H  N N 347 
PRO   HB2  H  N N 348 
PRO   HB3  H  N N 349 
PRO   HG2  H  N N 350 
PRO   HG3  H  N N 351 
PRO   HD2  H  N N 352 
PRO   HD3  H  N N 353 
PRO   HXT  H  N N 354 
SER   N    N  N N 355 
SER   CA   C  N S 356 
SER   C    C  N N 357 
SER   O    O  N N 358 
SER   CB   C  N N 359 
SER   OG   O  N N 360 
SER   OXT  O  N N 361 
SER   H    H  N N 362 
SER   H2   H  N N 363 
SER   HA   H  N N 364 
SER   HB2  H  N N 365 
SER   HB3  H  N N 366 
SER   HG   H  N N 367 
SER   HXT  H  N N 368 
TFA   C1   C  N N 369 
TFA   C2   C  N N 370 
TFA   O    O  N N 371 
TFA   F1   F  N N 372 
TFA   F2   F  N N 373 
TFA   F3   F  N N 374 
TFA   OXT  O  N N 375 
TFA   HXT  H  N N 376 
THR   N    N  N N 377 
THR   CA   C  N S 378 
THR   C    C  N N 379 
THR   O    O  N N 380 
THR   CB   C  N R 381 
THR   OG1  O  N N 382 
THR   CG2  C  N N 383 
THR   OXT  O  N N 384 
THR   H    H  N N 385 
THR   H2   H  N N 386 
THR   HA   H  N N 387 
THR   HB   H  N N 388 
THR   HG1  H  N N 389 
THR   HG21 H  N N 390 
THR   HG22 H  N N 391 
THR   HG23 H  N N 392 
THR   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
# 
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 
A1BAI C2  C1   sing N N 1   
A1BAI C2  C3   sing N N 2   
A1BAI O1  C10  sing N N 3   
A1BAI C10 C3   sing N N 4   
A1BAI C10 C11  sing N N 5   
A1BAI C3  N1   sing N N 6   
A1BAI N1  C4   sing N N 7   
A1BAI C4  C7   doub Y N 8   
A1BAI C4  N2   sing Y N 9   
A1BAI C8  C7   sing Y N 10  
A1BAI C8  C9   doub Y N 11  
A1BAI C7  C6   sing Y N 12  
A1BAI N2  C5   doub Y N 13  
A1BAI C9  N4   sing Y N 14  
A1BAI C6  N4   sing Y N 15  
A1BAI C6  N3   doub Y N 16  
A1BAI C5  N3   sing Y N 17  
A1BAI C3  H1   sing N N 18  
A1BAI C9  H11  sing N N 19  
A1BAI C1  H5   sing N N 20  
A1BAI C1  H3   sing N N 21  
A1BAI C1  H4   sing N N 22  
A1BAI C10 H2   sing N N 23  
A1BAI C11 H14  sing N N 24  
A1BAI C11 H13  sing N N 25  
A1BAI C11 H15  sing N N 26  
A1BAI C2  H6   sing N N 27  
A1BAI C2  H7   sing N N 28  
A1BAI C5  H9   sing N N 29  
A1BAI C8  H10  sing N N 30  
A1BAI N1  H8   sing N N 31  
A1BAI N4  H12  sing N N 32  
A1BAI O1  H16  sing N N 33  
A1BAJ C11 C10  sing N N 34  
A1BAJ C10 O1   sing N N 35  
A1BAJ C10 C3   sing N N 36  
A1BAJ C1  C2   sing N N 37  
A1BAJ C2  C3   sing N N 38  
A1BAJ C3  N1   sing N N 39  
A1BAJ N1  C4   sing N N 40  
A1BAJ C4  C7   doub Y N 41  
A1BAJ C4  N2   sing Y N 42  
A1BAJ C8  C7   sing Y N 43  
A1BAJ C8  C9   doub Y N 44  
A1BAJ C7  C6   sing Y N 45  
A1BAJ N2  C5   doub Y N 46  
A1BAJ C9  N4   sing Y N 47  
A1BAJ C6  N4   sing Y N 48  
A1BAJ C6  N3   doub Y N 49  
A1BAJ C5  N3   sing Y N 50  
A1BAJ O1  H16  sing N N 51  
A1BAJ C1  H3   sing N N 52  
A1BAJ C1  H5   sing N N 53  
A1BAJ C1  H4   sing N N 54  
A1BAJ C2  H6   sing N N 55  
A1BAJ C2  H7   sing N N 56  
A1BAJ C3  H1   sing N N 57  
A1BAJ C5  H9   sing N N 58  
A1BAJ C8  H10  sing N N 59  
A1BAJ C10 H2   sing N N 60  
A1BAJ C11 H15  sing N N 61  
A1BAJ C11 H14  sing N N 62  
A1BAJ C11 H13  sing N N 63  
A1BAJ C9  H11  sing N N 64  
A1BAJ N1  H8   sing N N 65  
A1BAJ N4  H12  sing N N 66  
ALA   N   CA   sing N N 67  
ALA   N   H    sing N N 68  
ALA   N   H2   sing N N 69  
ALA   CA  C    sing N N 70  
ALA   CA  CB   sing N N 71  
ALA   CA  HA   sing N N 72  
ALA   C   O    doub N N 73  
ALA   C   OXT  sing N N 74  
ALA   CB  HB1  sing N N 75  
ALA   CB  HB2  sing N N 76  
ALA   CB  HB3  sing N N 77  
ALA   OXT HXT  sing N N 78  
ARG   N   CA   sing N N 79  
ARG   N   H    sing N N 80  
ARG   N   H2   sing N N 81  
ARG   CA  C    sing N N 82  
ARG   CA  CB   sing N N 83  
ARG   CA  HA   sing N N 84  
ARG   C   O    doub N N 85  
ARG   C   OXT  sing N N 86  
ARG   CB  CG   sing N N 87  
ARG   CB  HB2  sing N N 88  
ARG   CB  HB3  sing N N 89  
ARG   CG  CD   sing N N 90  
ARG   CG  HG2  sing N N 91  
ARG   CG  HG3  sing N N 92  
ARG   CD  NE   sing N N 93  
ARG   CD  HD2  sing N N 94  
ARG   CD  HD3  sing N N 95  
ARG   NE  CZ   sing N N 96  
ARG   NE  HE   sing N N 97  
ARG   CZ  NH1  sing N N 98  
ARG   CZ  NH2  doub N N 99  
ARG   NH1 HH11 sing N N 100 
ARG   NH1 HH12 sing N N 101 
ARG   NH2 HH21 sing N N 102 
ARG   NH2 HH22 sing N N 103 
ARG   OXT HXT  sing N N 104 
ASN   N   CA   sing N N 105 
ASN   N   H    sing N N 106 
ASN   N   H2   sing N N 107 
ASN   CA  C    sing N N 108 
ASN   CA  CB   sing N N 109 
ASN   CA  HA   sing N N 110 
ASN   C   O    doub N N 111 
ASN   C   OXT  sing N N 112 
ASN   CB  CG   sing N N 113 
ASN   CB  HB2  sing N N 114 
ASN   CB  HB3  sing N N 115 
ASN   CG  OD1  doub N N 116 
ASN   CG  ND2  sing N N 117 
ASN   ND2 HD21 sing N N 118 
ASN   ND2 HD22 sing N N 119 
ASN   OXT HXT  sing N N 120 
ASP   N   CA   sing N N 121 
ASP   N   H    sing N N 122 
ASP   N   H2   sing N N 123 
ASP   CA  C    sing N N 124 
ASP   CA  CB   sing N N 125 
ASP   CA  HA   sing N N 126 
ASP   C   O    doub N N 127 
ASP   C   OXT  sing N N 128 
ASP   CB  CG   sing N N 129 
ASP   CB  HB2  sing N N 130 
ASP   CB  HB3  sing N N 131 
ASP   CG  OD1  doub N N 132 
ASP   CG  OD2  sing N N 133 
ASP   OD2 HD2  sing N N 134 
ASP   OXT HXT  sing N N 135 
CYS   N   CA   sing N N 136 
CYS   N   H    sing N N 137 
CYS   N   H2   sing N N 138 
CYS   CA  C    sing N N 139 
CYS   CA  CB   sing N N 140 
CYS   CA  HA   sing N N 141 
CYS   C   O    doub N N 142 
CYS   C   OXT  sing N N 143 
CYS   CB  SG   sing N N 144 
CYS   CB  HB2  sing N N 145 
CYS   CB  HB3  sing N N 146 
CYS   SG  HG   sing N N 147 
CYS   OXT HXT  sing N N 148 
GLN   N   CA   sing N N 149 
GLN   N   H    sing N N 150 
GLN   N   H2   sing N N 151 
GLN   CA  C    sing N N 152 
GLN   CA  CB   sing N N 153 
GLN   CA  HA   sing N N 154 
GLN   C   O    doub N N 155 
GLN   C   OXT  sing N N 156 
GLN   CB  CG   sing N N 157 
GLN   CB  HB2  sing N N 158 
GLN   CB  HB3  sing N N 159 
GLN   CG  CD   sing N N 160 
GLN   CG  HG2  sing N N 161 
GLN   CG  HG3  sing N N 162 
GLN   CD  OE1  doub N N 163 
GLN   CD  NE2  sing N N 164 
GLN   NE2 HE21 sing N N 165 
GLN   NE2 HE22 sing N N 166 
GLN   OXT HXT  sing N N 167 
GLU   N   CA   sing N N 168 
GLU   N   H    sing N N 169 
GLU   N   H2   sing N N 170 
GLU   CA  C    sing N N 171 
GLU   CA  CB   sing N N 172 
GLU   CA  HA   sing N N 173 
GLU   C   O    doub N N 174 
GLU   C   OXT  sing N N 175 
GLU   CB  CG   sing N N 176 
GLU   CB  HB2  sing N N 177 
GLU   CB  HB3  sing N N 178 
GLU   CG  CD   sing N N 179 
GLU   CG  HG2  sing N N 180 
GLU   CG  HG3  sing N N 181 
GLU   CD  OE1  doub N N 182 
GLU   CD  OE2  sing N N 183 
GLU   OE2 HE2  sing N N 184 
GLU   OXT HXT  sing N N 185 
GLY   N   CA   sing N N 186 
GLY   N   H    sing N N 187 
GLY   N   H2   sing N N 188 
GLY   CA  C    sing N N 189 
GLY   CA  HA2  sing N N 190 
GLY   CA  HA3  sing N N 191 
GLY   C   O    doub N N 192 
GLY   C   OXT  sing N N 193 
GLY   OXT HXT  sing N N 194 
HIS   N   CA   sing N N 195 
HIS   N   H    sing N N 196 
HIS   N   H2   sing N N 197 
HIS   CA  C    sing N N 198 
HIS   CA  CB   sing N N 199 
HIS   CA  HA   sing N N 200 
HIS   C   O    doub N N 201 
HIS   C   OXT  sing N N 202 
HIS   CB  CG   sing N N 203 
HIS   CB  HB2  sing N N 204 
HIS   CB  HB3  sing N N 205 
HIS   CG  ND1  sing Y N 206 
HIS   CG  CD2  doub Y N 207 
HIS   ND1 CE1  doub Y N 208 
HIS   ND1 HD1  sing N N 209 
HIS   CD2 NE2  sing Y N 210 
HIS   CD2 HD2  sing N N 211 
HIS   CE1 NE2  sing Y N 212 
HIS   CE1 HE1  sing N N 213 
HIS   NE2 HE2  sing N N 214 
HIS   OXT HXT  sing N N 215 
HOH   O   H1   sing N N 216 
HOH   O   H2   sing N N 217 
ILE   N   CA   sing N N 218 
ILE   N   H    sing N N 219 
ILE   N   H2   sing N N 220 
ILE   CA  C    sing N N 221 
ILE   CA  CB   sing N N 222 
ILE   CA  HA   sing N N 223 
ILE   C   O    doub N N 224 
ILE   C   OXT  sing N N 225 
ILE   CB  CG1  sing N N 226 
ILE   CB  CG2  sing N N 227 
ILE   CB  HB   sing N N 228 
ILE   CG1 CD1  sing N N 229 
ILE   CG1 HG12 sing N N 230 
ILE   CG1 HG13 sing N N 231 
ILE   CG2 HG21 sing N N 232 
ILE   CG2 HG22 sing N N 233 
ILE   CG2 HG23 sing N N 234 
ILE   CD1 HD11 sing N N 235 
ILE   CD1 HD12 sing N N 236 
ILE   CD1 HD13 sing N N 237 
ILE   OXT HXT  sing N N 238 
LEU   N   CA   sing N N 239 
LEU   N   H    sing N N 240 
LEU   N   H2   sing N N 241 
LEU   CA  C    sing N N 242 
LEU   CA  CB   sing N N 243 
LEU   CA  HA   sing N N 244 
LEU   C   O    doub N N 245 
LEU   C   OXT  sing N N 246 
LEU   CB  CG   sing N N 247 
LEU   CB  HB2  sing N N 248 
LEU   CB  HB3  sing N N 249 
LEU   CG  CD1  sing N N 250 
LEU   CG  CD2  sing N N 251 
LEU   CG  HG   sing N N 252 
LEU   CD1 HD11 sing N N 253 
LEU   CD1 HD12 sing N N 254 
LEU   CD1 HD13 sing N N 255 
LEU   CD2 HD21 sing N N 256 
LEU   CD2 HD22 sing N N 257 
LEU   CD2 HD23 sing N N 258 
LEU   OXT HXT  sing N N 259 
LYS   N   CA   sing N N 260 
LYS   N   H    sing N N 261 
LYS   N   H2   sing N N 262 
LYS   CA  C    sing N N 263 
LYS   CA  CB   sing N N 264 
LYS   CA  HA   sing N N 265 
LYS   C   O    doub N N 266 
LYS   C   OXT  sing N N 267 
LYS   CB  CG   sing N N 268 
LYS   CB  HB2  sing N N 269 
LYS   CB  HB3  sing N N 270 
LYS   CG  CD   sing N N 271 
LYS   CG  HG2  sing N N 272 
LYS   CG  HG3  sing N N 273 
LYS   CD  CE   sing N N 274 
LYS   CD  HD2  sing N N 275 
LYS   CD  HD3  sing N N 276 
LYS   CE  NZ   sing N N 277 
LYS   CE  HE2  sing N N 278 
LYS   CE  HE3  sing N N 279 
LYS   NZ  HZ1  sing N N 280 
LYS   NZ  HZ2  sing N N 281 
LYS   NZ  HZ3  sing N N 282 
LYS   OXT HXT  sing N N 283 
MET   N   CA   sing N N 284 
MET   N   H    sing N N 285 
MET   N   H2   sing N N 286 
MET   CA  C    sing N N 287 
MET   CA  CB   sing N N 288 
MET   CA  HA   sing N N 289 
MET   C   O    doub N N 290 
MET   C   OXT  sing N N 291 
MET   CB  CG   sing N N 292 
MET   CB  HB2  sing N N 293 
MET   CB  HB3  sing N N 294 
MET   CG  SD   sing N N 295 
MET   CG  HG2  sing N N 296 
MET   CG  HG3  sing N N 297 
MET   SD  CE   sing N N 298 
MET   CE  HE1  sing N N 299 
MET   CE  HE2  sing N N 300 
MET   CE  HE3  sing N N 301 
MET   OXT HXT  sing N N 302 
PHE   N   CA   sing N N 303 
PHE   N   H    sing N N 304 
PHE   N   H2   sing N N 305 
PHE   CA  C    sing N N 306 
PHE   CA  CB   sing N N 307 
PHE   CA  HA   sing N N 308 
PHE   C   O    doub N N 309 
PHE   C   OXT  sing N N 310 
PHE   CB  CG   sing N N 311 
PHE   CB  HB2  sing N N 312 
PHE   CB  HB3  sing N N 313 
PHE   CG  CD1  doub Y N 314 
PHE   CG  CD2  sing Y N 315 
PHE   CD1 CE1  sing Y N 316 
PHE   CD1 HD1  sing N N 317 
PHE   CD2 CE2  doub Y N 318 
PHE   CD2 HD2  sing N N 319 
PHE   CE1 CZ   doub Y N 320 
PHE   CE1 HE1  sing N N 321 
PHE   CE2 CZ   sing Y N 322 
PHE   CE2 HE2  sing N N 323 
PHE   CZ  HZ   sing N N 324 
PHE   OXT HXT  sing N N 325 
PRO   N   CA   sing N N 326 
PRO   N   CD   sing N N 327 
PRO   N   H    sing N N 328 
PRO   CA  C    sing N N 329 
PRO   CA  CB   sing N N 330 
PRO   CA  HA   sing N N 331 
PRO   C   O    doub N N 332 
PRO   C   OXT  sing N N 333 
PRO   CB  CG   sing N N 334 
PRO   CB  HB2  sing N N 335 
PRO   CB  HB3  sing N N 336 
PRO   CG  CD   sing N N 337 
PRO   CG  HG2  sing N N 338 
PRO   CG  HG3  sing N N 339 
PRO   CD  HD2  sing N N 340 
PRO   CD  HD3  sing N N 341 
PRO   OXT HXT  sing N N 342 
SER   N   CA   sing N N 343 
SER   N   H    sing N N 344 
SER   N   H2   sing N N 345 
SER   CA  C    sing N N 346 
SER   CA  CB   sing N N 347 
SER   CA  HA   sing N N 348 
SER   C   O    doub N N 349 
SER   C   OXT  sing N N 350 
SER   CB  OG   sing N N 351 
SER   CB  HB2  sing N N 352 
SER   CB  HB3  sing N N 353 
SER   OG  HG   sing N N 354 
SER   OXT HXT  sing N N 355 
TFA   C1  C2   sing N N 356 
TFA   C1  O    doub N N 357 
TFA   C1  OXT  sing N N 358 
TFA   C2  F1   sing N N 359 
TFA   C2  F2   sing N N 360 
TFA   C2  F3   sing N N 361 
TFA   OXT HXT  sing N N 362 
THR   N   CA   sing N N 363 
THR   N   H    sing N N 364 
THR   N   H2   sing N N 365 
THR   CA  C    sing N N 366 
THR   CA  CB   sing N N 367 
THR   CA  HA   sing N N 368 
THR   C   O    doub N N 369 
THR   C   OXT  sing N N 370 
THR   CB  OG1  sing N N 371 
THR   CB  CG2  sing N N 372 
THR   CB  HB   sing N N 373 
THR   OG1 HG1  sing N N 374 
THR   CG2 HG21 sing N N 375 
THR   CG2 HG22 sing N N 376 
THR   CG2 HG23 sing N N 377 
THR   OXT HXT  sing N N 378 
TYR   N   CA   sing N N 379 
TYR   N   H    sing N N 380 
TYR   N   H2   sing N N 381 
TYR   CA  C    sing N N 382 
TYR   CA  CB   sing N N 383 
TYR   CA  HA   sing N N 384 
TYR   C   O    doub N N 385 
TYR   C   OXT  sing N N 386 
TYR   CB  CG   sing N N 387 
TYR   CB  HB2  sing N N 388 
TYR   CB  HB3  sing N N 389 
TYR   CG  CD1  doub Y N 390 
TYR   CG  CD2  sing Y N 391 
TYR   CD1 CE1  sing Y N 392 
TYR   CD1 HD1  sing N N 393 
TYR   CD2 CE2  doub Y N 394 
TYR   CD2 HD2  sing N N 395 
TYR   CE1 CZ   doub Y N 396 
TYR   CE1 HE1  sing N N 397 
TYR   CE2 CZ   sing Y N 398 
TYR   CE2 HE2  sing N N 399 
TYR   CZ  OH   sing N N 400 
TYR   OH  HH   sing N N 401 
TYR   OXT HXT  sing N N 402 
VAL   N   CA   sing N N 403 
VAL   N   H    sing N N 404 
VAL   N   H2   sing N N 405 
VAL   CA  C    sing N N 406 
VAL   CA  CB   sing N N 407 
VAL   CA  HA   sing N N 408 
VAL   C   O    doub N N 409 
VAL   C   OXT  sing N N 410 
VAL   CB  CG1  sing N N 411 
VAL   CB  CG2  sing N N 412 
VAL   CB  HB   sing N N 413 
VAL   CG1 HG11 sing N N 414 
VAL   CG1 HG12 sing N N 415 
VAL   CG1 HG13 sing N N 416 
VAL   CG2 HG21 sing N N 417 
VAL   CG2 HG22 sing N N 418 
VAL   CG2 HG23 sing N N 419 
VAL   OXT HXT  sing N N 420 
# 
_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                    7HEY 
_atom_sites.fract_transf_matrix[1][1]   0.011266 
_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]   0.011266 
_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]   0.025297 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.623 -16.195 22.199  0.72 52.26 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.556 -16.169 22.318  0.28 51.35 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.656 -15.121 22.392  0.72 51.85 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.609 -15.074 22.486  0.28 51.06 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.306 -13.771 22.109  0.72 50.45 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.277 -13.744 22.164  0.28 50.01 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.431 -13.512 22.537  0.72 50.87 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.390 -13.472 22.616  0.28 50.41 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.040 -15.171 23.805  0.72 52.53 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.007 -15.066 23.904  0.28 51.58 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.007 -14.065 23.980  0.72 52.70 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 16.987 -13.943 24.044  0.28 51.72 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.416 -16.535 24.063  0.72 52.71 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.372 -16.411 24.218  0.28 51.72 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.934 -15.233 21.759  0.72 62.19 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.877 -15.190 21.863  0.28 61.24 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.739 -15.034 24.463  0.72 63.01 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.715 -14.911 24.549  0.28 61.87 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.516 -14.219 24.803  0.72 63.21 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.505 -14.058 24.878  0.28 62.03 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.461 -13.209 24.023  0.72 63.21 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.450 -13.091 24.046  0.28 62.03 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.397 -14.081 23.225  0.72 63.21 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.369 -13.984 23.298  0.28 62.03 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.965 -16.519 24.922  0.72 63.22 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.921 -16.355 25.075  0.28 62.03 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.778 -16.728 23.358  0.72 63.22 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.732 -16.628 23.522  0.28 62.03 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.115 -17.207 24.069  0.72 63.22 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.065 -17.088 24.253  0.28 62.03 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.593 -12.919 21.374  1.00 48.29 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.052 -11.574 21.047  1.00 44.13 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.910 -10.591 21.288  1.00 40.58 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.799 -10.976 21.668  1.00 40.43 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.613 -11.491 19.619  1.00 43.26 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.602 -11.886 18.565  1.00 42.33 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.484 -11.370 18.535  1.00 41.90 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 18.991 -12.808 17.689  1.00 42.05 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.820 -13.106 21.043  0.72 57.92 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.838 -13.121 21.013  0.28 57.92 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.773 -11.341 21.647  1.00 52.93 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.890 -10.577 19.440  1.00 51.89 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.375 -12.087 19.544  1.00 51.89 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.456 -13.067 17.068  1.00 50.43 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.782 -13.146 17.743  1.00 50.43 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.187 -9.306  21.062  1.00 36.97 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.283 -8.232  21.453  1.00 33.41 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.392 -7.740  20.314  1.00 28.92 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.678 -6.747  20.487  1.00 29.73 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.070 -7.065  22.056  1.00 34.60 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 18.972 -6.514  21.114  1.00 35.34 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 18.903 -9.032  20.671  1.00 44.33 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.700 -8.565  22.148  1.00 40.06 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.448 -6.374  22.336  1.00 41.49 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.573 -7.384  22.824  1.00 41.49 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.399 -5.874  21.461  1.00 42.37 ?  5   SER   A HG   1 
ATOM   57   N  N    A PHE   A 1 6   ? 16.399 -8.412  19.166  0.72 25.52 ?  6   PHE   A N    1 
ATOM   58   N  N    B PHE   A 1 6   ? 16.431 -8.396  19.158  0.28 26.65 ?  6   PHE   A N    1 
ATOM   59   C  CA   A PHE   A 1 6   ? 15.484 -8.049  18.090  0.72 22.13 ?  6   PHE   A CA   1 
ATOM   60   C  CA   B PHE   A 1 6   ? 15.592 -7.998  18.034  0.28 24.22 ?  6   PHE   A CA   1 
ATOM   61   C  C    A PHE   A 1 6   ? 14.057 -8.432  18.466  0.72 21.70 ?  6   PHE   A C    1 
ATOM   62   C  C    B PHE   A 1 6   ? 14.134 -8.250  18.396  0.28 23.61 ?  6   PHE   A C    1 
ATOM   63   O  O    A PHE   A 1 6   ? 13.818 -9.498  19.037  0.72 22.82 ?  6   PHE   A O    1 
ATOM   64   O  O    B PHE   A 1 6   ? 13.687 -9.401  18.449  0.28 23.30 ?  6   PHE   A O    1 
ATOM   65   C  CB   A PHE   A 1 6   ? 15.884 -8.754  16.797  0.72 20.10 ?  6   PHE   A CB   1 
ATOM   66   C  CB   B PHE   A 1 6   ? 16.001 -8.771  16.784  0.28 22.76 ?  6   PHE   A CB   1 
ATOM   67   C  CG   A PHE   A 1 6   ? 17.164 -8.236  16.195  0.72 18.83 ?  6   PHE   A CG   1 
ATOM   68   C  CG   B PHE   A 1 6   ? 17.291 -8.292  16.172  0.28 21.60 ?  6   PHE   A CG   1 
ATOM   69   C  CD1  A PHE   A 1 6   ? 17.177 -7.053  15.476  0.72 18.57 ?  6   PHE   A CD1  1 
ATOM   70   C  CD1  B PHE   A 1 6   ? 17.331 -7.108  15.455  0.28 21.15 ?  6   PHE   A CD1  1 
ATOM   71   C  CD2  A PHE   A 1 6   ? 18.349 -8.937  16.344  0.72 19.63 ?  6   PHE   A CD2  1 
ATOM   72   C  CD2  B PHE   A 1 6   ? 18.461 -9.023  16.310  0.28 21.37 ?  6   PHE   A CD2  1 
ATOM   73   C  CE1  A PHE   A 1 6   ? 18.349 -6.576  14.922  0.72 18.92 ?  6   PHE   A CE1  1 
ATOM   74   C  CE1  B PHE   A 1 6   ? 18.510 -6.660  14.890  0.28 21.01 ?  6   PHE   A CE1  1 
ATOM   75   C  CE2  A PHE   A 1 6   ? 19.521 -8.468  15.788  0.72 19.90 ?  6   PHE   A CE2  1 
ATOM   76   C  CE2  B PHE   A 1 6   ? 19.644 -8.581  15.744  0.28 21.20 ?  6   PHE   A CE2  1 
ATOM   77   C  CZ   A PHE   A 1 6   ? 19.522 -7.284  15.078  0.72 19.34 ?  6   PHE   A CZ   1 
ATOM   78   C  CZ   B PHE   A 1 6   ? 19.668 -7.397  15.033  0.28 20.98 ?  6   PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 16.916 -9.077  18.990  0.72 30.59 ?  6   PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 16.929 -9.077  19.002  0.28 31.95 ?  6   PHE   A H    1 
ATOM   81   H  HA   A PHE   A 1 6   ? 15.514 -7.096  17.950  0.72 26.53 ?  6   PHE   A HA   1 
ATOM   82   H  HA   B PHE   A 1 6   ? 15.707 -7.051  17.863  0.28 29.04 ?  6   PHE   A HA   1 
ATOM   83   H  HB2  A PHE   A 1 6   ? 15.998 -9.702  16.982  0.72 24.08 ?  6   PHE   A HB2  1 
ATOM   84   H  HB2  B PHE   A 1 6   ? 16.111 -9.706  17.019  0.28 27.29 ?  6   PHE   A HB2  1 
ATOM   85   H  HB3  A PHE   A 1 6   ? 15.173 -8.633  16.148  0.72 24.08 ?  6   PHE   A HB3  1 
ATOM   86   H  HB3  B PHE   A 1 6   ? 15.303 -8.679  16.118  0.28 27.29 ?  6   PHE   A HB3  1 
ATOM   87   H  HD1  A PHE   A 1 6   ? 16.386 -6.573  15.370  0.72 22.26 ?  6   PHE   A HD1  1 
ATOM   88   H  HD1  B PHE   A 1 6   ? 16.556 -6.606  15.356  0.28 25.35 ?  6   PHE   A HD1  1 
ATOM   89   H  HD2  A PHE   A 1 6   ? 18.351 -9.737  16.826  0.72 23.52 ?  6   PHE   A HD2  1 
ATOM   90   H  HD2  B PHE   A 1 6   ? 18.451 -9.821  16.788  0.28 25.62 ?  6   PHE   A HD2  1 
ATOM   91   H  HE1  A PHE   A 1 6   ? 18.346 -5.779  14.441  0.72 22.67 ?  6   PHE   A HE1  1 
ATOM   92   H  HE1  B PHE   A 1 6   ? 18.523 -5.862  14.411  0.28 25.18 ?  6   PHE   A HE1  1 
ATOM   93   H  HE2  A PHE   A 1 6   ? 20.311 -8.944  15.898  0.72 23.85 ?  6   PHE   A HE2  1 
ATOM   94   H  HE2  B PHE   A 1 6   ? 20.425 -9.079  15.842  0.28 25.41 ?  6   PHE   A HE2  1 
ATOM   95   H  HZ   A PHE   A 1 6   ? 20.310 -6.964  14.704  0.72 23.18 ?  6   PHE   A HZ   1 
ATOM   96   H  HZ   B PHE   A 1 6   ? 20.462 -7.096  14.652  0.28 25.15 ?  6   PHE   A HZ   1 
ATOM   97   N  N    A SER   A 1 7   ? 13.101 -7.561  18.139  0.72 20.28 ?  7   SER   A N    1 
ATOM   98   N  N    B SER   A 1 7   ? 13.396 -7.175  18.651  0.28 23.30 ?  7   SER   A N    1 
ATOM   99   C  CA   A SER   A 1 7   ? 11.727 -7.719  18.605  0.72 20.39 ?  7   SER   A CA   1 
ATOM   100  C  CA   B SER   A 1 7   ? 12.051 -7.249  19.202  0.28 23.26 ?  7   SER   A CA   1 
ATOM   101  C  C    A SER   A 1 7   ? 10.731 -7.433  17.489  0.72 18.13 ?  7   SER   A C    1 
ATOM   102  C  C    B SER   A 1 7   ? 11.027 -7.113  18.085  0.28 22.30 ?  7   SER   A C    1 
ATOM   103  O  O    A SER   A 1 7   ? 10.945 -6.541  16.665  0.72 18.35 ?  7   SER   A O    1 
ATOM   104  O  O    B SER   A 1 7   ? 11.158 -6.243  17.217  0.28 22.44 ?  7   SER   A O    1 
ATOM   105  C  CB   A SER   A 1 7   ? 11.448 -6.778  19.784  0.72 22.81 ?  7   SER   A CB   1 
ATOM   106  C  CB   B SER   A 1 7   ? 11.845 -6.129  20.223  0.28 23.94 ?  7   SER   A CB   1 
ATOM   107  O  OG   A SER   A 1 7   ? 10.112 -6.901  20.231  0.72 24.49 ?  7   SER   A OG   1 
ATOM   108  O  OG   B SER   A 1 7   ? 10.636 -6.302  20.941  0.28 24.66 ?  7   SER   A OG   1 
ATOM   109  H  H    A SER   A 1 7   ? 13.223 -6.877  17.637  0.72 24.31 ?  7   SER   A H    1 
ATOM   110  H  H    B SER   A 1 7   ? 13.660 -6.368  18.506  0.28 27.93 ?  7   SER   A H    1 
ATOM   111  H  HA   A SER   A 1 7   ? 11.589 -8.631  18.907  0.72 24.44 ?  7   SER   A HA   1 
ATOM   112  H  HA   B SER   A 1 7   ? 11.922 -8.103  19.644  0.28 27.88 ?  7   SER   A HA   1 
ATOM   113  H  HB2  A SER   A 1 7   ? 12.042 -7.005  20.515  0.72 27.34 ?  7   SER   A HB2  1 
ATOM   114  H  HB2  B SER   A 1 7   ? 12.590 -6.131  20.844  0.28 28.70 ?  7   SER   A HB2  1 
ATOM   115  H  HB3  A SER   A 1 7   ? 11.605 -5.864  19.501  0.72 27.34 ?  7   SER   A HB3  1 
ATOM   116  H  HB3  B SER   A 1 7   ? 11.808 -5.281  19.753  0.28 28.70 ?  7   SER   A HB3  1 
ATOM   117  H  HG   A SER   A 1 7   ? 9.971  -6.376  20.872  0.72 29.35 ?  7   SER   A HG   1 
ATOM   118  H  HG   B SER   A 1 7   ? 10.546 -5.680  21.502  0.28 29.56 ?  7   SER   A HG   1 
ATOM   119  N  N    A GLY   A 1 8   ? 9.627  -8.185  17.480  0.72 16.68 ?  8   GLY   A N    1 
ATOM   120  N  N    B GLY   A 1 8   ? 10.014 -7.976  18.107  0.28 21.39 ?  8   GLY   A N    1 
ATOM   121  C  CA   A GLY   A 1 8   ? 8.545  -7.940  16.544  0.72 15.92 ?  8   GLY   A CA   1 
ATOM   122  C  CA   B GLY   A 1 8   ? 8.881  -7.829  17.220  0.28 20.33 ?  8   GLY   A CA   1 
ATOM   123  C  C    A GLY   A 1 8   ? 8.769  -8.450  15.140  0.72 14.50 ?  8   GLY   A C    1 
ATOM   124  C  C    B GLY   A 1 8   ? 9.068  -8.357  15.819  0.28 19.19 ?  8   GLY   A C    1 
ATOM   125  O  O    A GLY   A 1 8   ? 8.033  -8.052  14.229  0.72 15.04 ?  8   GLY   A O    1 
ATOM   126  O  O    B GLY   A 1 8   ? 8.264  -8.019  14.942  0.28 19.10 ?  8   GLY   A O    1 
ATOM   127  H  H    A GLY   A 1 8   ? 9.480  -8.848  18.017  0.72 19.99 ?  8   GLY   A H    1 
ATOM   128  H  H    B GLY   A 1 8   ? 9.965  -8.659  18.630  0.28 25.63 ?  8   GLY   A H    1 
ATOM   129  H  HA2  A GLY   A 1 8   ? 7.733  -8.352  16.886  0.72 19.08 ?  8   GLY   A HA2  1 
ATOM   130  H  HA2  B GLY   A 1 8   ? 8.122  -8.291  17.599  0.28 24.36 ?  8   GLY   A HA2  1 
ATOM   131  H  HA3  A GLY   A 1 8   ? 8.391  -6.984  16.491  0.72 19.08 ?  8   GLY   A HA3  1 
ATOM   132  H  HA3  B GLY   A 1 8   ? 8.660  -6.886  17.154  0.28 24.36 ?  8   GLY   A HA3  1 
ATOM   133  N  N    A TYR   A 1 9   ? 9.756  -9.314  14.929  0.72 13.60 ?  9   TYR   A N    1 
ATOM   134  N  N    B TYR   A 1 9   ? 10.089 -9.169  15.570  0.28 18.21 ?  9   TYR   A N    1 
ATOM   135  C  CA   A TYR   A 1 9   ? 10.029 -9.861  13.608  0.72 12.46 ?  9   TYR   A CA   1 
ATOM   136  C  CA   B TYR   A 1 9   ? 10.297 -9.681  14.224  0.28 17.39 ?  9   TYR   A CA   1 
ATOM   137  C  C    A TYR   A 1 9   ? 9.172  -11.086 13.334  0.72 12.12 ?  9   TYR   A C    1 
ATOM   138  C  C    B TYR   A 1 9   ? 9.424  -10.899 13.952  0.28 16.95 ?  9   TYR   A C    1 
ATOM   139  O  O    A TYR   A 1 9   ? 8.931  -11.912 14.217  0.72 13.58 ?  9   TYR   A O    1 
ATOM   140  O  O    B TYR   A 1 9   ? 9.068  -11.658 14.858  0.28 17.64 ?  9   TYR   A O    1 
ATOM   141  C  CB   A TYR   A 1 9   ? 11.506 -10.252 13.460  0.72 13.15 ?  9   TYR   A CB   1 
ATOM   142  C  CB   B TYR   A 1 9   ? 11.764 -10.039 13.990  0.28 17.04 ?  9   TYR   A CB   1 
ATOM   143  C  CG   A TYR   A 1 9   ? 12.430 -9.065  13.307  0.72 13.70 ?  9   TYR   A CG   1 
ATOM   144  C  CG   B TYR   A 1 9   ? 12.617 -8.832  13.696  0.28 16.38 ?  9   TYR   A CG   1 
ATOM   145  C  CD1  A TYR   A 1 9   ? 12.760 -8.282  14.401  0.72 14.48 ?  9   TYR   A CD1  1 
ATOM   146  C  CD1  B TYR   A 1 9   ? 12.931 -7.927  14.696  0.28 16.44 ?  9   TYR   A CD1  1 
ATOM   147  C  CD2  A TYR   A 1 9   ? 12.954 -8.718  12.067  0.72 13.60 ?  9   TYR   A CD2  1 
ATOM   148  C  CD2  B TYR   A 1 9   ? 13.094 -8.589  12.414  0.28 15.87 ?  9   TYR   A CD2  1 
ATOM   149  C  CE1  A TYR   A 1 9   ? 13.578 -7.183  14.273  0.72 15.63 ?  9   TYR   A CE1  1 
ATOM   150  C  CE1  B TYR   A 1 9   ? 13.701 -6.815  14.435  0.28 16.40 ?  9   TYR   A CE1  1 
ATOM   151  C  CE2  A TYR   A 1 9   ? 13.775 -7.618  11.926  0.72 14.48 ?  9   TYR   A CE2  1 
ATOM   152  C  CE2  B TYR   A 1 9   ? 13.865 -7.475  12.141  0.28 15.89 ?  9   TYR   A CE2  1 
ATOM   153  C  CZ   A TYR   A 1 9   ? 14.087 -6.857  13.032  0.72 15.78 ?  9   TYR   A CZ   1 
ATOM   154  C  CZ   B TYR   A 1 9   ? 14.166 -6.593  13.156  0.28 16.25 ?  9   TYR   A CZ   1 
ATOM   155  O  OH   A TYR   A 1 9   ? 14.900 -5.764  12.895  0.72 17.27 ?  9   TYR   A OH   1 
ATOM   156  O  OH   B TYR   A 1 9   ? 14.931 -5.483  12.891  0.28 16.76 ?  9   TYR   A OH   1 
ATOM   157  H  H    A TYR   A 1 9   ? 10.281 -9.605  15.540  0.72 16.28 ?  9   TYR   A H    1 
ATOM   158  H  H    B TYR   A 1 9   ? 10.674 -9.427  16.152  0.28 21.82 ?  9   TYR   A H    1 
ATOM   159  H  HA   A TYR   A 1 9   ? 9.825  -9.192  12.935  0.72 14.92 ?  9   TYR   A HA   1 
ATOM   160  H  HA   B TYR   A 1 9   ? 10.058 -8.985  13.592  0.28 20.84 ?  9   TYR   A HA   1 
ATOM   161  H  HB2  A TYR   A 1 9   ? 11.780 -10.752 14.244  0.72 15.75 ?  9   TYR   A HB2  1 
ATOM   162  H  HB2  B TYR   A 1 9   ? 12.121 -10.479 14.775  0.28 20.42 ?  9   TYR   A HB2  1 
ATOM   163  H  HB3  A TYR   A 1 9   ? 11.593 -10.807 12.667  0.72 15.75 ?  9   TYR   A HB3  1 
ATOM   164  H  HB3  B TYR   A 1 9   ? 11.814 -10.634 13.226  0.28 20.42 ?  9   TYR   A HB3  1 
ATOM   165  H  HD1  A TYR   A 1 9   ? 12.407 -8.501  15.237  0.72 17.35 ?  9   TYR   A HD1  1 
ATOM   166  H  HD1  B TYR   A 1 9   ? 12.616 -8.075  15.560  0.28 19.70 ?  9   TYR   A HD1  1 
ATOM   167  H  HD2  A TYR   A 1 9   ? 12.738 -9.232  11.316  0.72 16.29 ?  9   TYR   A HD2  1 
ATOM   168  H  HD2  B TYR   A 1 9   ? 12.891 -9.185  11.729  0.28 19.01 ?  9   TYR   A HD2  1 
ATOM   169  H  HE1  A TYR   A 1 9   ? 13.792 -6.672  15.017  0.72 18.73 ?  9   TYR   A HE1  1 
ATOM   170  H  HE1  B TYR   A 1 9   ? 13.905 -6.218  15.117  0.28 19.65 ?  9   TYR   A HE1  1 
ATOM   171  H  HE2  A TYR   A 1 9   ? 14.127 -7.399  11.091  0.72 17.35 ?  9   TYR   A HE2  1 
ATOM   172  H  HE2  B TYR   A 1 9   ? 14.184 -7.325  11.279  0.28 19.03 ?  9   TYR   A HE2  1 
ATOM   173  H  HH   A TYR   A 1 9   ? 15.026 -5.403  13.643  0.72 20.69 ?  9   TYR   A HH   1 
ATOM   174  H  HH   B TYR   A 1 9   ? 15.053 -5.046  13.598  0.28 20.08 ?  9   TYR   A HH   1 
ATOM   175  N  N    A LEU   A 1 10  ? 8.725  -11.196 12.092  0.72 11.52 ?  10  LEU   A N    1 
ATOM   176  N  N    B LEU   A 1 10  ? 9.076  -11.068 12.681  0.28 16.34 ?  10  LEU   A N    1 
ATOM   177  C  CA   A LEU   A 1 10  ? 8.143  -12.428 11.587  0.72 11.30 ?  10  LEU   A CA   1 
ATOM   178  C  CA   B LEU   A 1 10  ? 8.371  -12.241 12.190  0.28 16.14 ?  10  LEU   A CA   1 
ATOM   179  C  C    A LEU   A 1 10  ? 9.267  -13.370 11.147  0.72 11.70 ?  10  LEU   A C    1 
ATOM   180  C  C    B LEU   A 1 10  ? 9.399  -13.223 11.650  0.28 14.83 ?  10  LEU   A C    1 
ATOM   181  O  O    A LEU   A 1 10  ? 10.224 -12.952 10.484  0.72 12.15 ?  10  LEU   A O    1 
ATOM   182  O  O    B LEU   A 1 10  ? 10.267 -12.846 10.854  0.28 14.68 ?  10  LEU   A O    1 
ATOM   183  C  CB   A LEU   A 1 10  ? 7.249  -12.090 10.399  0.72 12.67 ?  10  LEU   A CB   1 
ATOM   184  C  CB   B LEU   A 1 10  ? 7.407  -11.836 11.076  0.28 16.94 ?  10  LEU   A CB   1 
ATOM   185  C  CG   A LEU   A 1 10  ? 6.533  -13.272 9.749   0.72 15.08 ?  10  LEU   A CG   1 
ATOM   186  C  CG   B LEU   A 1 10  ? 6.984  -12.890 10.052  0.28 17.92 ?  10  LEU   A CG   1 
ATOM   187  C  CD1  A LEU   A 1 10  ? 5.469  -13.844 10.673  0.72 17.11 ?  10  LEU   A CD1  1 
ATOM   188  C  CD1  B LEU   A 1 10  ? 6.199  -14.021 10.682  0.28 18.34 ?  10  LEU   A CD1  1 
ATOM   189  C  CD2  A LEU   A 1 10  ? 5.946  -12.875 8.398   0.72 16.89 ?  10  LEU   A CD2  1 
ATOM   190  C  CD2  B LEU   A 1 10  ? 6.159  -12.206 9.008   0.28 18.42 ?  10  LEU   A CD2  1 
ATOM   191  H  H    A LEU   A 1 10  ? 8.750  -10.560 11.504  0.72 13.79 ?  10  LEU   A H    1 
ATOM   192  H  H    B LEU   A 1 10  ? 9.253  -10.494 12.066  0.28 19.57 ?  10  LEU   A H    1 
ATOM   193  H  HA   A LEU   A 1 10  ? 7.608  -12.855 12.276  0.72 13.53 ?  10  LEU   A HA   1 
ATOM   194  H  HA   B LEU   A 1 10  ? 7.868  -12.658 12.909  0.28 19.33 ?  10  LEU   A HA   1 
ATOM   195  H  HB2  A LEU   A 1 10  ? 6.558  -11.472 10.692  0.72 15.17 ?  10  LEU   A HB2  1 
ATOM   196  H  HB2  B LEU   A 1 10  ? 6.594  -11.509 11.490  0.28 20.30 ?  10  LEU   A HB2  1 
ATOM   197  H  HB3  A LEU   A 1 10  ? 7.785  -11.672 9.713   0.72 15.17 ?  10  LEU   A HB3  1 
ATOM   198  H  HB3  B LEU   A 1 10  ? 7.821  -11.113 10.579  0.28 20.30 ?  10  LEU   A HB3  1 
ATOM   199  H  HG   A LEU   A 1 10  ? 7.179  -13.976 9.584   0.72 18.07 ?  10  LEU   A HG   1 
ATOM   200  H  HG   B LEU   A 1 10  ? 7.770  -13.262 9.617   0.28 21.48 ?  10  LEU   A HG   1 
ATOM   201  H  HD11 A LEU   A 1 10  ? 5.022  -14.581 10.225  0.72 20.50 ?  10  LEU   A HD11 1 
ATOM   202  H  HD11 B LEU   A 1 10  ? 5.508  -14.302 10.061  0.28 21.98 ?  10  LEU   A HD11 1 
ATOM   203  H  HD12 A LEU   A 1 10  ? 5.891  -14.161 11.486  0.72 20.50 ?  10  LEU   A HD12 1 
ATOM   204  H  HD12 B LEU   A 1 10  ? 6.802  -14.758 10.860  0.28 21.98 ?  10  LEU   A HD12 1 
ATOM   205  H  HD13 A LEU   A 1 10  ? 4.825  -13.149 10.883  0.72 20.50 ?  10  LEU   A HD13 1 
ATOM   206  H  HD13 B LEU   A 1 10  ? 5.797  -13.706 11.505  0.28 21.98 ?  10  LEU   A HD13 1 
ATOM   207  H  HD21 A LEU   A 1 10  ? 5.498  -13.647 8.011   0.72 20.23 ?  10  LEU   A HD21 1 
ATOM   208  H  HD21 B LEU   A 1 10  ? 5.994  -12.829 8.289   0.28 22.07 ?  10  LEU   A HD21 1 
ATOM   209  H  HD22 A LEU   A 1 10  ? 5.310  -12.157 8.529   0.72 20.23 ?  10  LEU   A HD22 1 
ATOM   210  H  HD22 B LEU   A 1 10  ? 5.324  -11.932 9.415   0.28 22.07 ?  10  LEU   A HD22 1 
ATOM   211  H  HD23 A LEU   A 1 10  ? 6.664  -12.585 7.816   0.72 20.23 ?  10  LEU   A HD23 1 
ATOM   212  H  HD23 B LEU   A 1 10  ? 6.645  -11.435 8.682   0.28 22.07 ?  10  LEU   A HD23 1 
ATOM   213  N  N    A LYS   A 1 11  ? 9.154  -14.647 11.519  0.72 11.75 ?  11  LYS   A N    1 
ATOM   214  N  N    B LYS   A 1 11  ? 9.315  -14.472 12.094  0.28 14.11 ?  11  LYS   A N    1 
ATOM   215  C  CA   A LYS   A 1 11  ? 10.162 -15.649 11.191  0.72 12.29 ?  11  LYS   A CA   1 
ATOM   216  C  CA   B LYS   A 1 11  ? 10.230 -15.502 11.625  0.28 13.63 ?  11  LYS   A CA   1 
ATOM   217  C  C    A LYS   A 1 11  ? 9.834  -16.257 9.832   0.72 12.38 ?  11  LYS   A C    1 
ATOM   218  C  C    B LYS   A 1 11  ? 9.785  -15.970 10.244  0.28 12.87 ?  11  LYS   A C    1 
ATOM   219  O  O    A LYS   A 1 11  ? 8.767  -16.853 9.665   0.72 14.38 ?  11  LYS   A O    1 
ATOM   220  O  O    B LYS   A 1 11  ? 8.644  -16.411 10.069  0.28 12.98 ?  11  LYS   A O    1 
ATOM   221  C  CB   A LYS   A 1 11  ? 10.181 -16.722 12.279  0.72 12.37 ?  11  LYS   A CB   1 
ATOM   222  C  CB   B LYS   A 1 11  ? 10.259 -16.666 12.615  0.28 13.70 ?  11  LYS   A CB   1 
ATOM   223  C  CG   A LYS   A 1 11  ? 11.179 -17.843 12.080  0.72 12.52 ?  11  LYS   A CG   1 
ATOM   224  C  CG   B LYS   A 1 11  ? 11.406 -17.664 12.422  0.28 13.56 ?  11  LYS   A CG   1 
ATOM   225  C  CD   A LYS   A 1 11  ? 11.221 -18.711 13.333  0.72 13.13 ?  11  LYS   A CD   1 
ATOM   226  C  CD   B LYS   A 1 11  ? 11.513 -18.619 13.619  0.28 13.53 ?  11  LYS   A CD   1 
ATOM   227  C  CE   A LYS   A 1 11  ? 12.228 -19.850 13.234  0.72 12.89 ?  11  LYS   A CE   1 
ATOM   228  C  CE   B LYS   A 1 11  ? 12.566 -19.713 13.421  0.28 13.76 ?  11  LYS   A CE   1 
ATOM   229  N  NZ   A LYS   A 1 11  ? 13.614 -19.381 12.964  0.72 12.91 ?  11  LYS   A NZ   1 
ATOM   230  N  NZ   B LYS   A 1 11  ? 13.946 -19.169 13.287  0.28 13.96 ?  11  LYS   A NZ   1 
ATOM   231  H  H    A LYS   A 1 11  ? 8.485  -14.964 11.962  0.72 14.07 ?  11  LYS   A H    1 
ATOM   232  H  H    B LYS   A 1 11  ? 8.740  -14.737 12.677  0.28 16.90 ?  11  LYS   A H    1 
ATOM   233  H  HA   A LYS   A 1 11  ? 11.037 -15.229 11.145  0.72 14.72 ?  11  LYS   A HA   1 
ATOM   234  H  HA   B LYS   A 1 11  ? 11.120 -15.125 11.550  0.28 16.33 ?  11  LYS   A HA   1 
ATOM   235  H  HB2  A LYS   A 1 11  ? 10.392 -16.292 13.124  0.72 14.81 ?  11  LYS   A HB2  1 
ATOM   236  H  HB2  B LYS   A 1 11  ? 10.333 -16.299 13.509  0.28 16.41 ?  11  LYS   A HB2  1 
ATOM   237  H  HB3  A LYS   A 1 11  ? 9.301  -17.120 12.330  0.72 14.81 ?  11  LYS   A HB3  1 
ATOM   238  H  HB3  B LYS   A 1 11  ? 9.427  -17.153 12.531  0.28 16.41 ?  11  LYS   A HB3  1 
ATOM   239  H  HG2  A LYS   A 1 11  ? 10.907 -18.396 11.331  0.72 14.99 ?  11  LYS   A HG2  1 
ATOM   240  H  HG2  B LYS   A 1 11  ? 11.242 -18.191 11.626  0.28 16.24 ?  11  LYS   A HG2  1 
ATOM   241  H  HG3  A LYS   A 1 11  ? 12.063 -17.475 11.933  0.72 14.99 ?  11  LYS   A HG3  1 
ATOM   242  H  HG3  B LYS   A 1 11  ? 12.245 -17.183 12.339  0.28 16.24 ?  11  LYS   A HG3  1 
ATOM   243  H  HD2  A LYS   A 1 11  ? 11.459 -18.159 14.093  0.72 15.72 ?  11  LYS   A HD2  1 
ATOM   244  H  HD2  B LYS   A 1 11  ? 11.756 -18.111 14.410  0.28 16.20 ?  11  LYS   A HD2  1 
ATOM   245  H  HD3  A LYS   A 1 11  ? 10.338 -19.100 13.474  0.72 15.72 ?  11  LYS   A HD3  1 
ATOM   246  H  HD3  B LYS   A 1 11  ? 10.655 -19.051 13.756  0.28 16.20 ?  11  LYS   A HD3  1 
ATOM   247  H  HE2  A LYS   A 1 11  ? 12.235 -20.338 14.074  0.72 15.44 ?  11  LYS   A HE2  1 
ATOM   248  H  HE2  B LYS   A 1 11  ? 12.555 -20.311 14.188  0.28 16.48 ?  11  LYS   A HE2  1 
ATOM   249  H  HE3  A LYS   A 1 11  ? 11.966 -20.442 12.511  0.72 15.44 ?  11  LYS   A HE3  1 
ATOM   250  H  HE3  B LYS   A 1 11  ? 12.361 -20.212 12.614  0.28 16.48 ?  11  LYS   A HE3  1 
ATOM   251  H  HZ1  A LYS   A 1 11  ? 14.165 -20.075 12.890  0.72 15.46 ?  11  LYS   A HZ1  1 
ATOM   252  H  HZ1  B LYS   A 1 11  ? 14.526 -19.833 13.154  0.28 16.72 ?  11  LYS   A HZ1  1 
ATOM   253  H  HZ2  A LYS   A 1 11  ? 13.637 -18.913 12.206  0.72 15.46 ?  11  LYS   A HZ2  1 
ATOM   254  H  HZ2  B LYS   A 1 11  ? 13.986 -18.609 12.597  0.28 16.72 ?  11  LYS   A HZ2  1 
ATOM   255  H  HZ3  A LYS   A 1 11  ? 13.896 -18.859 13.630  0.72 15.46 ?  11  LYS   A HZ3  1 
ATOM   256  H  HZ3  B LYS   A 1 11  ? 14.173 -18.733 14.028  0.28 16.72 ?  11  LYS   A HZ3  1 
ATOM   257  N  N    A LEU   A 1 12  ? 10.742 -16.124 8.863   0.72 11.31 ?  12  LEU   A N    1 
ATOM   258  N  N    B LEU   A 1 12  ? 10.670 -15.840 9.258   0.28 12.66 ?  12  LEU   A N    1 
ATOM   259  C  CA   A LEU   A 1 12  ? 10.497 -16.715 7.549   0.72 11.63 ?  12  LEU   A CA   1 
ATOM   260  C  CA   B LEU   A 1 12  ? 10.411 -16.335 7.911   0.28 12.50 ?  12  LEU   A CA   1 
ATOM   261  C  C    A LEU   A 1 12  ? 11.086 -18.115 7.411   0.72 11.87 ?  12  LEU   A C    1 
ATOM   262  C  C    B LEU   A 1 12  ? 10.988 -17.723 7.678   0.28 12.20 ?  12  LEU   A C    1 
ATOM   263  O  O    A LEU   A 1 12  ? 10.451 -18.994 6.815   0.72 12.51 ?  12  LEU   A O    1 
ATOM   264  O  O    B LEU   A 1 12  ? 10.336 -18.563 7.048   0.28 12.29 ?  12  LEU   A O    1 
ATOM   265  C  CB   A LEU   A 1 12  ? 11.056 -15.822 6.436   0.72 11.99 ?  12  LEU   A CB   1 
ATOM   266  C  CB   B LEU   A 1 12  ? 10.981 -15.370 6.864   0.28 13.21 ?  12  LEU   A CB   1 
ATOM   267  C  CG   A LEU   A 1 12  ? 10.407 -14.450 6.256   0.72 12.84 ?  12  LEU   A CG   1 
ATOM   268  C  CG   B LEU   A 1 12  ? 10.281 -14.015 6.746   0.28 13.96 ?  12  LEU   A CG   1 
ATOM   269  C  CD1  A LEU   A 1 12  ? 11.170 -13.664 5.212   0.72 13.16 ?  12  LEU   A CD1  1 
ATOM   270  C  CD1  B LEU   A 1 12  ? 10.802 -13.228 5.547   0.28 14.52 ?  12  LEU   A CD1  1 
ATOM   271  C  CD2  A LEU   A 1 12  ? 8.933  -14.576 5.873   0.72 13.68 ?  12  LEU   A CD2  1 
ATOM   272  C  CD2  B LEU   A 1 12  ? 8.777  -14.206 6.650   0.28 14.24 ?  12  LEU   A CD2  1 
ATOM   273  H  H    A LEU   A 1 12  ? 11.504 -15.712 8.939   0.72 13.54 ?  12  LEU   A H    1 
ATOM   274  H  H    B LEU   A 1 12  ? 11.438 -15.457 9.347   0.28 15.17 ?  12  LEU   A H    1 
ATOM   275  H  HA   A LEU   A 1 12  ? 9.542  -16.792 7.421   0.72 13.93 ?  12  LEU   A HA   1 
ATOM   276  H  HA   B LEU   A 1 12  ? 9.450  -16.391 7.782   0.28 14.97 ?  12  LEU   A HA   1 
ATOM   277  H  HB2  A LEU   A 1 12  ? 11.995 -15.677 6.611   0.72 14.35 ?  12  LEU   A HB2  1 
ATOM   278  H  HB2  B LEU   A 1 12  ? 11.911 -15.197 7.082   0.28 15.83 ?  12  LEU   A HB2  1 
ATOM   279  H  HB3  A LEU   A 1 12  ? 10.956 -16.301 5.596   0.72 14.35 ?  12  LEU   A HB3  1 
ATOM   280  H  HB3  B LEU   A 1 12  ? 10.929 -15.797 5.995   0.28 15.83 ?  12  LEU   A HB3  1 
ATOM   281  H  HG   A LEU   A 1 12  ? 10.458 -13.968 7.093   0.72 15.38 ?  12  LEU   A HG   1 
ATOM   282  H  HG   B LEU   A 1 12  ? 10.467 -13.493 7.544   0.28 16.73 ?  12  LEU   A HG   1 
ATOM   283  H  HD11 A LEU   A 1 12  ? 10.752 -12.799 5.099   0.72 15.77 ?  12  LEU   A HD11 1 
ATOM   284  H  HD11 B LEU   A 1 12  ? 10.343 -12.372 5.507   0.28 17.39 ?  12  LEU   A HD11 1 
ATOM   285  H  HD12 A LEU   A 1 12  ? 12.089 -13.554 5.510   0.72 15.77 ?  12  LEU   A HD12 1 
ATOM   286  H  HD12 B LEU   A 1 12  ? 11.755 -13.086 5.649   0.28 17.39 ?  12  LEU   A HD12 1 
ATOM   287  H  HD13 A LEU   A 1 12  ? 11.156 -14.153 4.373   0.72 15.77 ?  12  LEU   A HD13 1 
ATOM   288  H  HD13 B LEU   A 1 12  ? 10.626 -13.733 4.737   0.28 17.39 ?  12  LEU   A HD13 1 
ATOM   289  H  HD21 A LEU   A 1 12  ? 8.581  -13.695 5.678   0.72 16.39 ?  12  LEU   A HD21 1 
ATOM   290  H  HD21 B LEU   A 1 12  ? 8.374  -13.396 6.307   0.28 17.05 ?  12  LEU   A HD21 1 
ATOM   291  H  HD22 A LEU   A 1 12  ? 8.856  -15.144 5.088   0.72 16.39 ?  12  LEU   A HD22 1 
ATOM   292  H  HD22 B LEU   A 1 12  ? 8.592  -14.949 6.054   0.28 17.05 ?  12  LEU   A HD22 1 
ATOM   293  H  HD23 A LEU   A 1 12  ? 8.444  -14.972 6.613   0.72 16.39 ?  12  LEU   A HD23 1 
ATOM   294  H  HD23 B LEU   A 1 12  ? 8.427  -14.401 7.536   0.28 17.05 ?  12  LEU   A HD23 1 
ATOM   295  N  N    A THR   A 1 13  ? 12.297 -18.326 7.919   0.72 12.02 ?  13  THR   A N    1 
ATOM   296  N  N    B THR   A 1 13  ? 12.198 -17.976 8.168   0.28 11.97 ?  13  THR   A N    1 
ATOM   297  C  CA   A THR   A 1 13  ? 12.993 -19.607 7.843   0.72 12.69 ?  13  THR   A CA   1 
ATOM   298  C  CA   B THR   A 1 13  ? 12.849 -19.273 8.043   0.28 12.25 ?  13  THR   A CA   1 
ATOM   299  C  C    A THR   A 1 13  ? 13.762 -19.804 9.144   0.72 12.89 ?  13  THR   A C    1 
ATOM   300  C  C    B THR   A 1 13  ? 13.616 -19.560 9.328   0.28 12.64 ?  13  THR   A C    1 
ATOM   301  O  O    A THR   A 1 13  ? 13.661 -19.004 10.080  0.72 13.24 ?  13  THR   A O    1 
ATOM   302  O  O    B THR   A 1 13  ? 13.510 -18.839 10.325  0.28 12.64 ?  13  THR   A O    1 
ATOM   303  C  CB   A THR   A 1 13  ? 13.967 -19.663 6.656   0.72 13.43 ?  13  THR   A CB   1 
ATOM   304  C  CB   B THR   A 1 13  ? 13.818 -19.304 6.852   0.28 12.13 ?  13  THR   A CB   1 
ATOM   305  O  OG1  A THR   A 1 13  ? 15.040 -18.751 6.890   0.72 13.67 ?  13  THR   A OG1  1 
ATOM   306  O  OG1  B THR   A 1 13  ? 14.858 -18.346 7.073   0.28 11.76 ?  13  THR   A OG1  1 
ATOM   307  C  CG2  A THR   A 1 13  ? 13.290 -19.314 5.343   0.72 14.54 ?  13  THR   A CG2  1 
ATOM   308  C  CG2  B THR   A 1 13  ? 13.109 -19.008 5.537   0.28 12.44 ?  13  THR   A CG2  1 
ATOM   309  H  H    A THR   A 1 13  ? 12.759 -17.720 8.311   0.72 14.40 ?  13  THR   A H    1 
ATOM   310  H  H    B THR   A 1 13  ? 12.672 -17.387 8.573   0.28 14.33 ?  13  THR   A H    1 
ATOM   311  H  HA   A THR   A 1 13  ? 12.352 -20.328 7.740   0.72 15.19 ?  13  THR   A HA   1 
ATOM   312  H  HA   B THR   A 1 13  ? 12.180 -19.962 7.919   0.28 14.67 ?  13  THR   A HA   1 
ATOM   313  H  HB   A THR   A 1 13  ? 14.335 -20.556 6.574   0.72 16.09 ?  13  THR   A HB   1 
ATOM   314  H  HB   B THR   A 1 13  ? 14.212 -20.185 6.785   0.28 14.53 ?  13  THR   A HB   1 
ATOM   315  H  HG1  A THR   A 1 13  ? 15.581 -18.759 6.234   0.72 16.38 ?  13  THR   A HG1  1 
ATOM   316  H  HG1  B THR   A 1 13  ? 15.397 -18.350 6.427   0.28 14.09 ?  13  THR   A HG1  1 
ATOM   317  H  HG21 A THR   A 1 13  ? 13.899 -19.469 4.602   0.72 17.42 ?  13  THR   A HG21 1 
ATOM   318  H  HG21 B THR   A 1 13  ? 13.735 -19.087 4.798   0.28 14.90 ?  13  THR   A HG21 1 
ATOM   319  H  HG22 A THR   A 1 13  ? 12.504 -19.871 5.223   0.72 17.42 ?  13  THR   A HG22 1 
ATOM   320  H  HG22 B THR   A 1 13  ? 12.387 -19.646 5.401   0.28 14.90 ?  13  THR   A HG22 1 
ATOM   321  H  HG23 A THR   A 1 13  ? 13.022 -18.384 5.343   0.72 17.42 ?  13  THR   A HG23 1 
ATOM   322  H  HG23 B THR   A 1 13  ? 12.742 -18.114 5.546   0.28 14.90 ?  13  THR   A HG23 1 
ATOM   323  N  N    A ASP   A 1 14  ? 14.571 -20.865 9.191   0.72 13.62 ?  14  ASP   A N    1 
ATOM   324  N  N    B ASP   A 1 14  ? 14.414 -20.626 9.275   0.28 13.49 ?  14  ASP   A N    1 
ATOM   325  C  CA   A ASP   A 1 14  ? 15.406 -21.100 10.361  0.72 14.83 ?  14  ASP   A CA   1 
ATOM   326  C  CA   B ASP   A 1 14  ? 15.269 -21.002 10.394  0.28 14.27 ?  14  ASP   A CA   1 
ATOM   327  C  C    A ASP   A 1 14  ? 16.187 -19.849 10.754  0.72 13.84 ?  14  ASP   A C    1 
ATOM   328  C  C    B ASP   A 1 14  ? 16.266 -19.904 10.743  0.28 13.39 ?  14  ASP   A C    1 
ATOM   329  O  O    A ASP   A 1 14  ? 16.346 -19.554 11.944  0.72 14.91 ?  14  ASP   A O    1 
ATOM   330  O  O    B ASP   A 1 14  ? 16.685 -19.799 11.902  0.28 13.40 ?  14  ASP   A O    1 
ATOM   331  C  CB   A ASP   A 1 14  ? 16.373 -22.248 10.082  0.72 17.63 ?  14  ASP   A CB   1 
ATOM   332  C  CB   B ASP   A 1 14  ? 16.014 -22.288 10.039  0.28 16.03 ?  14  ASP   A CB   1 
ATOM   333  C  CG   A ASP   A 1 14  ? 17.309 -22.494 11.238  0.72 21.94 ?  14  ASP   A CG   1 
ATOM   334  C  CG   B ASP   A 1 14  ? 16.982 -22.720 11.121  0.28 17.46 ?  14  ASP   A CG   1 
ATOM   335  O  OD1  A ASP   A 1 14  ? 16.820 -22.879 12.319  0.72 23.79 ?  14  ASP   A OD1  1 
ATOM   336  O  OD1  B ASP   A 1 14  ? 16.519 -23.131 12.208  0.28 17.86 ?  14  ASP   A OD1  1 
ATOM   337  O  OD2  A ASP   A 1 14  ? 18.523 -22.266 11.068  0.72 24.68 -1 14  ASP   A OD2  1 
ATOM   338  O  OD2  B ASP   A 1 14  ? 18.204 -22.663 10.879  0.28 18.44 -1 14  ASP   A OD2  1 
ATOM   339  H  H    A ASP   A 1 14  ? 14.662 -21.454 8.564   0.72 16.32 ?  14  ASP   A H    1 
ATOM   340  H  H    B ASP   A 1 14  ? 14.467 -21.142 8.599   0.28 16.16 ?  14  ASP   A H    1 
ATOM   341  H  HA   A ASP   A 1 14  ? 14.845 -21.359 11.110  0.72 17.76 ?  14  ASP   A HA   1 
ATOM   342  H  HA   B ASP   A 1 14  ? 14.719 -21.171 11.173  0.28 17.09 ?  14  ASP   A HA   1 
ATOM   343  H  HB2  A ASP   A 1 14  ? 15.860 -23.061 9.902   0.72 21.12 ?  14  ASP   A HB2  1 
ATOM   344  H  HB2  B ASP   A 1 14  ? 15.370 -23.003 9.923   0.28 19.21 ?  14  ASP   A HB2  1 
ATOM   345  H  HB3  A ASP   A 1 14  ? 16.917 -22.032 9.310   0.72 21.12 ?  14  ASP   A HB3  1 
ATOM   346  H  HB3  B ASP   A 1 14  ? 16.504 -22.146 9.210   0.28 19.21 ?  14  ASP   A HB3  1 
ATOM   347  N  N    . ASN   A 1 15  ? 16.672 -19.089 9.765   1.00 13.16 ?  15  ASN   A N    1 
ATOM   348  C  CA   . ASN   A 1 15  ? 17.655 -18.041 10.016  1.00 13.66 ?  15  ASN   A CA   1 
ATOM   349  C  C    . ASN   A 1 15  ? 17.285 -16.647 9.527   1.00 13.84 ?  15  ASN   A C    1 
ATOM   350  O  O    . ASN   A 1 15  ? 18.063 -15.719 9.763   1.00 15.33 ?  15  ASN   A O    1 
ATOM   351  C  CB   . ASN   A 1 15  ? 19.026 -18.438 9.431   1.00 13.30 ?  15  ASN   A CB   1 
ATOM   352  C  CG   . ASN   A 1 15  ? 19.011 -18.535 7.924   1.00 13.88 ?  15  ASN   A CG   1 
ATOM   353  O  OD1  . ASN   A 1 15  ? 18.290 -19.356 7.354   1.00 14.96 ?  15  ASN   A OD1  1 
ATOM   354  N  ND2  . ASN   A 1 15  ? 19.809 -17.697 7.264   1.00 13.91 ?  15  ASN   A ND2  1 
ATOM   355  H  H    A ASN   A 1 15  ? 16.442 -19.165 8.943   0.72 15.76 ?  15  ASN   A H    1 
ATOM   356  H  H    B ASN   A 1 15  ? 16.389 -19.121 8.957   0.28 15.76 ?  15  ASN   A H    1 
ATOM   357  H  HA   . ASN   A 1 15  ? 17.786 -17.971 10.971  1.00 16.36 ?  15  ASN   A HA   1 
ATOM   358  H  HB2  . ASN   A 1 15  ? 19.689 -17.766 9.682   1.00 15.93 ?  15  ASN   A HB2  1 
ATOM   359  H  HB3  . ASN   A 1 15  ? 19.295 -19.302 9.784   1.00 15.93 ?  15  ASN   A HB3  1 
ATOM   360  H  HD21 . ASN   A 1 15  ? 19.836 -17.715 6.403   1.00 16.66 ?  15  ASN   A HD21 1 
ATOM   361  H  HD22 . ASN   A 1 15  ? 20.301 -17.132 7.692   1.00 16.66 ?  15  ASN   A HD22 1 
ATOM   362  N  N    A VAL   A 1 16  ? 16.169 -16.485 8.819   0.72 13.48 ?  16  VAL   A N    1 
ATOM   363  N  N    B VAL   A 1 16  ? 16.109 -16.442 8.938   0.28 13.69 ?  16  VAL   A N    1 
ATOM   364  C  CA   A VAL   A 1 16  ? 15.776 -15.213 8.227   0.72 12.98 ?  16  VAL   A CA   1 
ATOM   365  C  CA   B VAL   A 1 16  ? 15.721 -15.137 8.408   0.28 13.11 ?  16  VAL   A CA   1 
ATOM   366  C  C    A VAL   A 1 16  ? 14.490 -14.722 8.878   0.72 12.16 ?  16  VAL   A C    1 
ATOM   367  C  C    B VAL   A 1 16  ? 14.498 -14.612 9.155   0.28 12.98 ?  16  VAL   A C    1 
ATOM   368  O  O    A VAL   A 1 16  ? 13.481 -15.438 8.920   0.72 11.61 ?  16  VAL   A O    1 
ATOM   369  O  O    B VAL   A 1 16  ? 13.557 -15.363 9.437   0.28 13.00 ?  16  VAL   A O    1 
ATOM   370  C  CB   A VAL   A 1 16  ? 15.626 -15.307 6.698   0.72 13.76 ?  16  VAL   A CB   1 
ATOM   371  C  CB   B VAL   A 1 16  ? 15.477 -15.196 6.884   0.28 13.01 ?  16  VAL   A CB   1 
ATOM   372  C  CG1  A VAL   A 1 16  ? 15.200 -13.958 6.123   0.72 14.79 ?  16  VAL   A CG1  1 
ATOM   373  C  CG1  B VAL   A 1 16  ? 15.081 -13.826 6.344   0.28 13.38 ?  16  VAL   A CG1  1 
ATOM   374  C  CG2  A VAL   A 1 16  ? 16.926 -15.776 6.058   0.72 14.36 ?  16  VAL   A CG2  1 
ATOM   375  C  CG2  B VAL   A 1 16  ? 16.719 -15.721 6.164   0.28 13.44 ?  16  VAL   A CG2  1 
ATOM   376  H  H    A VAL   A 1 16  ? 15.613 -17.124 8.665   0.72 16.14 ?  16  VAL   A H    1 
ATOM   377  H  H    B VAL   A 1 16  ? 15.509 -17.050 8.843   0.28 16.40 ?  16  VAL   A H    1 
ATOM   378  H  HA   A VAL   A 1 16  ? 16.472 -14.562 8.408   0.72 15.54 ?  16  VAL   A HA   1 
ATOM   379  H  HA   B VAL   A 1 16  ? 16.443 -14.510 8.559   0.28 15.70 ?  16  VAL   A HA   1 
ATOM   380  H  HB   A VAL   A 1 16  ? 14.940 -15.959 6.487   0.72 16.48 ?  16  VAL   A HB   1 
ATOM   381  H  HB   B VAL   A 1 16  ? 14.752 -15.811 6.706   0.28 15.58 ?  16  VAL   A HB   1 
ATOM   382  H  HG11 A VAL   A 1 16  ? 15.308 -13.980 5.161   0.72 17.72 ?  16  VAL   A HG11 1 
ATOM   383  H  HG11 B VAL   A 1 16  ? 15.107 -13.853 5.374   0.28 16.03 ?  16  VAL   A HG11 1 
ATOM   384  H  HG12 A VAL   A 1 16  ? 14.269 -13.802 6.348   0.72 17.72 ?  16  VAL   A HG12 1 
ATOM   385  H  HG12 B VAL   A 1 16  ? 14.183 -13.615 6.643   0.28 16.03 ?  16  VAL   A HG12 1 
ATOM   386  H  HG13 A VAL   A 1 16  ? 15.757 -13.265 6.505   0.72 17.72 ?  16  VAL   A HG13 1 
ATOM   387  H  HG13 B VAL   A 1 16  ? 15.707 -13.163 6.672   0.28 16.03 ?  16  VAL   A HG13 1 
ATOM   388  H  HG21 A VAL   A 1 16  ? 16.832 -15.742 5.094   0.72 17.20 ?  16  VAL   A HG21 1 
ATOM   389  H  HG21 B VAL   A 1 16  ? 16.570 -15.681 5.207   0.28 16.10 ?  16  VAL   A HG21 1 
ATOM   390  H  HG22 A VAL   A 1 16  ? 17.645 -15.192 6.342   0.72 17.20 ?  16  VAL   A HG22 1 
ATOM   391  H  HG22 B VAL   A 1 16  ? 17.482 -15.171 6.403   0.28 16.10 ?  16  VAL   A HG22 1 
ATOM   392  H  HG23 A VAL   A 1 16  ? 17.108 -16.686 6.343   0.72 17.20 ?  16  VAL   A HG23 1 
ATOM   393  H  HG23 B VAL   A 1 16  ? 16.879 -16.640 6.435   0.28 16.10 ?  16  VAL   A HG23 1 
ATOM   394  N  N    A TYR   A 1 17  ? 14.531 -13.474 9.335   0.72 12.51 ?  17  TYR   A N    1 
ATOM   395  N  N    B TYR   A 1 17  ? 14.519 -13.309 9.466   0.28 12.86 ?  17  TYR   A N    1 
ATOM   396  C  CA   A TYR   A 1 17  ? 13.440 -12.788 10.003  0.72 12.30 ?  17  TYR   A CA   1 
ATOM   397  C  CA   B TYR   A 1 17  ? 13.466 -12.630 10.215  0.28 12.40 ?  17  TYR   A CA   1 
ATOM   398  C  C    A TYR   A 1 17  ? 13.168 -11.477 9.277   0.72 12.37 ?  17  TYR   A C    1 
ATOM   399  C  C    B TYR   A 1 17  ? 13.196 -11.275 9.572   0.28 12.08 ?  17  TYR   A C    1 
ATOM   400  O  O    A TYR   A 1 17  ? 14.066 -10.922 8.645   0.72 12.33 ?  17  TYR   A O    1 
ATOM   401  O  O    B TYR   A 1 17  ? 14.097 -10.682 8.977   0.28 12.00 ?  17  TYR   A O    1 
ATOM   402  C  CB   A TYR   A 1 17  ? 13.852 -12.503 11.446  0.72 13.02 ?  17  TYR   A CB   1 
ATOM   403  C  CB   B TYR   A 1 17  ? 13.885 -12.423 11.679  0.28 12.97 ?  17  TYR   A CB   1 
ATOM   404  C  CG   A TYR   A 1 17  ? 14.018 -13.757 12.276  0.72 14.08 ?  17  TYR   A CG   1 
ATOM   405  C  CG   B TYR   A 1 17  ? 14.177 -13.702 12.443  0.28 13.32 ?  17  TYR   A CG   1 
ATOM   406  C  CD1  A TYR   A 1 17  ? 15.180 -14.522 12.213  0.72 14.99 ?  17  TYR   A CD1  1 
ATOM   407  C  CD1  B TYR   A 1 17  ? 15.395 -14.362 12.307  0.28 13.73 ?  17  TYR   A CD1  1 
ATOM   408  C  CD2  A TYR   A 1 17  ? 13.002 -14.186 13.114  0.72 14.35 ?  17  TYR   A CD2  1 
ATOM   409  C  CD2  B TYR   A 1 17  ? 13.238 -14.240 13.313  0.28 13.58 ?  17  TYR   A CD2  1 
ATOM   410  C  CE1  A TYR   A 1 17  ? 15.320 -15.683 12.966  0.72 15.14 ?  17  TYR   A CE1  1 
ATOM   411  C  CE1  B TYR   A 1 17  ? 15.660 -15.531 13.008  0.28 14.31 ?  17  TYR   A CE1  1 
ATOM   412  C  CE2  A TYR   A 1 17  ? 13.129 -15.347 13.872  0.72 14.96 ?  17  TYR   A CE2  1 
ATOM   413  C  CE2  B TYR   A 1 17  ? 13.495 -15.406 14.019  0.28 14.10 ?  17  TYR   A CE2  1 
ATOM   414  C  CZ   A TYR   A 1 17  ? 14.292 -16.091 13.797  0.72 15.17 ?  17  TYR   A CZ   1 
ATOM   415  C  CZ   B TYR   A 1 17  ? 14.707 -16.047 13.863  0.28 14.42 ?  17  TYR   A CZ   1 
ATOM   416  O  OH   A TYR   A 1 17  ? 14.429 -17.244 14.547  0.72 15.94 ?  17  TYR   A OH   1 
ATOM   417  O  OH   B TYR   A 1 17  ? 14.959 -17.204 14.566  0.28 14.92 ?  17  TYR   A OH   1 
ATOM   418  H  H    A TYR   A 1 17  ? 15.235 -12.983 9.258   0.72 14.98 ?  17  TYR   A H    1 
ATOM   419  H  H    B TYR   A 1 17  ? 15.164 -12.775 9.242   0.28 15.40 ?  17  TYR   A H    1 
ATOM   420  H  HA   A TYR   A 1 17  ? 12.643 -13.348 9.987   0.72 14.72 ?  17  TYR   A HA   1 
ATOM   421  H  HA   B TYR   A 1 17  ? 12.652 -13.145 10.188  0.28 14.85 ?  17  TYR   A HA   1 
ATOM   422  H  HB2  A TYR   A 1 17  ? 14.698 -12.036 11.441  0.72 15.59 ?  17  TYR   A HB2  1 
ATOM   423  H  HB2  B TYR   A 1 17  ? 14.688 -11.883 11.696  0.28 15.54 ?  17  TYR   A HB2  1 
ATOM   424  H  HB3  A TYR   A 1 17  ? 13.170 -11.961 11.857  0.72 15.59 ?  17  TYR   A HB3  1 
ATOM   425  H  HB3  B TYR   A 1 17  ? 13.170 -11.961 12.143  0.28 15.54 ?  17  TYR   A HB3  1 
ATOM   426  H  HD1  A TYR   A 1 17  ? 15.875 -14.259 11.652  0.72 17.96 ?  17  TYR   A HD1  1 
ATOM   427  H  HD1  B TYR   A 1 17  ? 16.039 -14.022 11.731  0.28 16.44 ?  17  TYR   A HD1  1 
ATOM   428  H  HD2  A TYR   A 1 17  ? 12.213 -13.696 13.168  0.72 17.20 ?  17  TYR   A HD2  1 
ATOM   429  H  HD2  B TYR   A 1 17  ? 12.419 -13.813 13.421  0.28 16.26 ?  17  TYR   A HD2  1 
ATOM   430  H  HE1  A TYR   A 1 17  ? 16.106 -16.186 12.915  0.72 18.13 ?  17  TYR   A HE1  1 
ATOM   431  H  HE1  B TYR   A 1 17  ? 16.477 -15.965 12.907  0.28 17.14 ?  17  TYR   A HE1  1 
ATOM   432  H  HE2  A TYR   A 1 17  ? 12.435 -15.618 14.432  0.72 17.92 ?  17  TYR   A HE2  1 
ATOM   433  H  HE2  B TYR   A 1 17  ? 12.853 -15.753 14.596  0.28 16.88 ?  17  TYR   A HE2  1 
ATOM   434  H  HH   A TYR   A 1 17  ? 13.694 -17.446 14.896  0.72 19.10 ?  17  TYR   A HH   1 
ATOM   435  H  HH   B TYR   A 1 17  ? 15.689 -17.539 14.319  0.28 17.87 ?  17  TYR   A HH   1 
ATOM   436  N  N    A ILE   A 1 18  ? 11.939 -10.963 9.370   0.72 12.17 ?  18  ILE   A N    1 
ATOM   437  N  N    B ILE   A 1 18  ? 11.964 -10.768 9.701   0.28 11.66 ?  18  ILE   A N    1 
ATOM   438  C  CA   A ILE   A 1 18  ? 11.555 -9.775  8.604   0.72 11.96 ?  18  ILE   A CA   1 
ATOM   439  C  CA   B ILE   A 1 18  ? 11.568 -9.549  8.993   0.28 11.12 ?  18  ILE   A CA   1 
ATOM   440  C  C    A ILE   A 1 18  ? 10.580 -8.912  9.399   0.72 11.95 ?  18  ILE   A C    1 
ATOM   441  C  C    B ILE   A 1 18  ? 10.668 -8.678  9.864   0.28 11.24 ?  18  ILE   A C    1 
ATOM   442  O  O    A ILE   A 1 18  ? 9.753  -9.420  10.159  0.72 12.44 ?  18  ILE   A O    1 
ATOM   443  O  O    B ILE   A 1 18  ? 9.852  -9.183  10.643  0.28 11.81 ?  18  ILE   A O    1 
ATOM   444  C  CB   A ILE   A 1 18  ? 11.009 -10.178 7.216   0.72 11.74 ?  18  ILE   A CB   1 
ATOM   445  C  CB   B ILE   A 1 18  ? 10.918 -9.868  7.629   0.28 10.59 ?  18  ILE   A CB   1 
ATOM   446  C  CG1  A ILE   A 1 18  ? 10.972 -8.977  6.277   0.72 12.07 ?  18  ILE   A CG1  1 
ATOM   447  C  CG1  B ILE   A 1 18  ? 10.851 -8.614  6.754   0.28 11.39 ?  18  ILE   A CG1  1 
ATOM   448  C  CG2  A ILE   A 1 18  ? 9.658  -10.883 7.338   0.72 11.83 ?  18  ILE   A CG2  1 
ATOM   449  C  CG2  B ILE   A 1 18  ? 9.532  -10.475 7.812   0.28 10.84 ?  18  ILE   A CG2  1 
ATOM   450  C  CD1  A ILE   A 1 18  ? 10.740 -9.361  4.852   0.72 13.52 ?  18  ILE   A CD1  1 
ATOM   451  C  CD1  B ILE   A 1 18  ? 10.428 -8.901  5.332   0.28 12.34 ?  18  ILE   A CD1  1 
ATOM   452  H  H    A ILE   A 1 18  ? 11.324 -11.297 9.863   0.72 14.58 ?  18  ILE   A H    1 
ATOM   453  H  H    B ILE   A 1 18  ? 11.342 -11.107 10.196  0.28 13.96 ?  18  ILE   A H    1 
ATOM   454  H  HA   A ILE   A 1 18  ? 12.355 -9.254  8.453   0.72 14.33 ?  18  ILE   A HA   1 
ATOM   455  H  HA   B ILE   A 1 18  ? 12.367 -9.028  8.818   0.28 13.32 ?  18  ILE   A HA   1 
ATOM   456  H  HB   A ILE   A 1 18  ? 11.631 -10.821 6.835   0.72 14.05 ?  18  ILE   A HB   1 
ATOM   457  H  HB   B ILE   A 1 18  ? 11.476 -10.516 7.181   0.28 12.68 ?  18  ILE   A HB   1 
ATOM   458  H  HG12 A ILE   A 1 18  ? 10.260 -8.384  6.550   0.72 14.45 ?  18  ILE   A HG12 1 
ATOM   459  H  HG12 B ILE   A 1 18  ? 10.212 -7.992  7.135   0.28 13.63 ?  18  ILE   A HG12 1 
ATOM   460  H  HG13 A ILE   A 1 18  ? 11.827 -8.515  6.324   0.72 14.45 ?  18  ILE   A HG13 1 
ATOM   461  H  HG13 B ILE   A 1 18  ? 11.732 -8.203  6.724   0.28 13.63 ?  18  ILE   A HG13 1 
ATOM   462  H  HG21 A ILE   A 1 18  ? 9.422  -11.267 6.475   0.72 14.17 ?  18  ILE   A HG21 1 
ATOM   463  H  HG21 B ILE   A 1 18  ? 9.234  -10.842 6.963   0.28 12.97 ?  18  ILE   A HG21 1 
ATOM   464  H  HG22 A ILE   A 1 18  ? 9.727  -11.591 8.000   0.72 14.17 ?  18  ILE   A HG22 1 
ATOM   465  H  HG22 B ILE   A 1 18  ? 9.581  -11.179 8.476   0.28 12.97 ?  18  ILE   A HG22 1 
ATOM   466  H  HG23 A ILE   A 1 18  ? 8.986  -10.242 7.608   0.72 14.17 ?  18  ILE   A HG23 1 
ATOM   467  H  HG23 B ILE   A 1 18  ? 8.915  -9.785  8.106   0.28 12.97 ?  18  ILE   A HG23 1 
ATOM   468  H  HD11 A ILE   A 1 18  ? 10.800 -8.564  4.299   0.72 16.19 ?  18  ILE   A HD11 1 
ATOM   469  H  HD11 B ILE   A 1 18  ? 10.493 -8.085  4.812   0.28 14.78 ?  18  ILE   A HD11 1 
ATOM   470  H  HD12 A ILE   A 1 18  ? 11.412 -10.002 4.582   0.72 16.19 ?  18  ILE   A HD12 1 
ATOM   471  H  HD12 B ILE   A 1 18  ? 11.016 -9.578  4.960   0.28 14.78 ?  18  ILE   A HD12 1 
ATOM   472  H  HD13 A ILE   A 1 18  ? 9.855  -9.750  4.772   0.72 16.19 ?  18  ILE   A HD13 1 
ATOM   473  H  HD13 B ILE   A 1 18  ? 9.513  -9.221  5.333   0.28 14.78 ?  18  ILE   A HD13 1 
ATOM   474  N  N    A LYS   A 1 19  ? 10.669 -7.593  9.194   0.72 12.06 ?  19  LYS   A N    1 
ATOM   475  N  N    B LYS   A 1 19  ? 10.821 -7.358  9.718   0.28 11.32 ?  19  LYS   A N    1 
ATOM   476  C  CA   A LYS   A 1 19  ? 9.847  -6.632  9.923   0.72 12.59 ?  19  LYS   A CA   1 
ATOM   477  C  CA   B LYS   A 1 19  ? 10.065 -6.381  10.491  0.28 12.61 ?  19  LYS   A CA   1 
ATOM   478  C  C    A LYS   A 1 19  ? 9.678  -5.368  9.087   0.72 12.27 ?  19  LYS   A C    1 
ATOM   479  C  C    B LYS   A 1 19  ? 9.842  -5.144  9.635   0.28 13.30 ?  19  LYS   A C    1 
ATOM   480  O  O    A LYS   A 1 19  ? 10.581 -4.984  8.341   0.72 12.77 ?  19  LYS   A O    1 
ATOM   481  O  O    B LYS   A 1 19  ? 10.720 -4.753  8.864   0.28 13.27 ?  19  LYS   A O    1 
ATOM   482  C  CB   A LYS   A 1 19  ? 10.529 -6.283  11.254  0.72 14.05 ?  19  LYS   A CB   1 
ATOM   483  C  CB   B LYS   A 1 19  ? 10.834 -5.978  11.756  0.28 13.05 ?  19  LYS   A CB   1 
ATOM   484  C  CG   A LYS   A 1 19  ? 9.788  -5.300  12.147  0.72 15.24 ?  19  LYS   A CG   1 
ATOM   485  C  CG   B LYS   A 1 19  ? 10.080 -5.102  12.742  0.28 14.01 ?  19  LYS   A CG   1 
ATOM   486  C  CD   A LYS   A 1 19  ? 10.623 -5.005  13.386  0.72 17.24 ?  19  LYS   A CD   1 
ATOM   487  C  CD   B LYS   A 1 19  ? 10.993 -4.745  13.909  0.28 14.80 ?  19  LYS   A CD   1 
ATOM   488  C  CE   A LYS   A 1 19  ? 9.928  -4.056  14.344  0.72 18.54 ?  19  LYS   A CE   1 
ATOM   489  C  CE   B LYS   A 1 19  ? 10.295 -3.918  14.969  0.28 15.38 ?  19  LYS   A CE   1 
ATOM   490  N  NZ   A LYS   A 1 19  ? 10.796 -3.766  15.520  0.72 19.22 ?  19  LYS   A NZ   1 
ATOM   491  N  NZ   B LYS   A 1 19  ? 11.180 -3.722  16.153  0.28 15.72 ?  19  LYS   A NZ   1 
ATOM   492  H  H    A LYS   A 1 19  ? 11.211 -7.236  8.627   0.72 14.44 ?  19  LYS   A H    1 
ATOM   493  H  H    B LYS   A 1 19  ? 11.379 -6.991  9.166   0.28 13.55 ?  19  LYS   A H    1 
ATOM   494  H  HA   A LYS   A 1 19  ? 8.976  -7.028  10.101  0.72 15.07 ?  19  LYS   A HA   1 
ATOM   495  H  HA   B LYS   A 1 19  ? 9.208  -6.746  10.748  0.28 15.10 ?  19  LYS   A HA   1 
ATOM   496  H  HB2  A LYS   A 1 19  ? 10.642 -7.105  11.760  0.72 16.83 ?  19  LYS   A HB2  1 
ATOM   497  H  HB2  B LYS   A 1 19  ? 11.086 -6.780  12.234  0.28 15.63 ?  19  LYS   A HB2  1 
ATOM   498  H  HB3  A LYS   A 1 19  ? 11.395 -5.905  11.055  0.72 16.83 ?  19  LYS   A HB3  1 
ATOM   499  H  HB3  B LYS   A 1 19  ? 11.632 -5.489  11.497  0.28 15.63 ?  19  LYS   A HB3  1 
ATOM   500  H  HG2  A LYS   A 1 19  ? 9.642  -4.470  11.665  0.72 18.26 ?  19  LYS   A HG2  1 
ATOM   501  H  HG2  B LYS   A 1 19  ? 9.801  -4.280  12.310  0.28 16.78 ?  19  LYS   A HG2  1 
ATOM   502  H  HG3  A LYS   A 1 19  ? 8.942  -5.685  12.425  0.72 18.26 ?  19  LYS   A HG3  1 
ATOM   503  H  HG3  B LYS   A 1 19  ? 9.312  -5.583  13.090  0.28 16.78 ?  19  LYS   A HG3  1 
ATOM   504  H  HD2  A LYS   A 1 19  ? 10.796 -5.835  13.858  0.72 20.65 ?  19  LYS   A HD2  1 
ATOM   505  H  HD2  B LYS   A 1 19  ? 11.299 -5.565  14.329  0.28 17.73 ?  19  LYS   A HD2  1 
ATOM   506  H  HD3  A LYS   A 1 19  ? 11.462 -4.598  13.114  0.72 20.65 ?  19  LYS   A HD3  1 
ATOM   507  H  HD3  B LYS   A 1 19  ? 11.750 -4.238  13.577  0.28 17.73 ?  19  LYS   A HD3  1 
ATOM   508  H  HE2  A LYS   A 1 19  ? 9.741  -3.218  13.888  0.72 22.22 ?  19  LYS   A HE2  1 
ATOM   509  H  HE2  B LYS   A 1 19  ? 10.075 -3.046  14.605  0.28 18.43 ?  19  LYS   A HE2  1 
ATOM   510  H  HE3  A LYS   A 1 19  ? 9.106  -4.459  14.660  0.72 22.22 ?  19  LYS   A HE3  1 
ATOM   511  H  HE3  B LYS   A 1 19  ? 9.491  -4.376  15.260  0.28 18.43 ?  19  LYS   A HE3  1 
ATOM   512  H  HZ1  A LYS   A 1 19  ? 10.375 -3.217  16.079  0.72 23.03 ?  19  LYS   A HZ1  1 
ATOM   513  H  HZ1  B LYS   A 1 19  ? 10.757 -3.244  16.774  0.28 18.84 ?  19  LYS   A HZ1  1 
ATOM   514  H  HZ2  A LYS   A 1 19  ? 10.987 -4.523  15.947  0.72 23.03 ?  19  LYS   A HZ2  1 
ATOM   515  H  HZ2  B LYS   A 1 19  ? 11.403 -4.511  16.500  0.28 18.84 ?  19  LYS   A HZ2  1 
ATOM   516  H  HZ3  A LYS   A 1 19  ? 11.553 -3.385  15.252  0.72 23.03 ?  19  LYS   A HZ3  1 
ATOM   517  H  HZ3  B LYS   A 1 19  ? 11.921 -3.292  15.912  0.28 18.84 ?  19  LYS   A HZ3  1 
ATOM   518  N  N    A ASN   A 1 20  ? 8.513  -4.725  9.212   0.72 13.22 ?  20  ASN   A N    1 
ATOM   519  N  N    B ASN   A 1 20  ? 8.668  -4.532  9.774   0.28 14.35 ?  20  ASN   A N    1 
ATOM   520  C  CA   A ASN   A 1 20  ? 8.305  -3.396  8.635   0.72 14.71 ?  20  ASN   A CA   1 
ATOM   521  C  CA   B ASN   A 1 20  ? 8.383  -3.256  9.121   0.28 15.56 ?  20  ASN   A CA   1 
ATOM   522  C  C    A ASN   A 1 20  ? 8.928  -2.385  9.594   0.72 15.63 ?  20  ASN   A C    1 
ATOM   523  C  C    B ASN   A 1 20  ? 8.952  -2.138  9.983   0.28 15.74 ?  20  ASN   A C    1 
ATOM   524  O  O    A ASN   A 1 20  ? 8.416  -2.169  10.698  0.72 17.29 ?  20  ASN   A O    1 
ATOM   525  O  O    B ASN   A 1 20  ? 8.312  -1.678  10.932  0.28 16.12 ?  20  ASN   A O    1 
ATOM   526  C  CB   A ASN   A 1 20  ? 6.811  -3.153  8.417   0.72 15.69 ?  20  ASN   A CB   1 
ATOM   527  C  CB   B ASN   A 1 20  ? 6.884  -3.076  8.920   0.28 16.59 ?  20  ASN   A CB   1 
ATOM   528  C  CG   A ASN   A 1 20  ? 6.487  -1.726  7.986   0.72 17.34 ?  20  ASN   A CG   1 
ATOM   529  C  CG   B ASN   A 1 20  ? 6.511  -1.645  8.581   0.28 17.79 ?  20  ASN   A CG   1 
ATOM   530  O  OD1  A ASN   A 1 20  ? 5.435  -1.197  8.341   0.72 19.59 ?  20  ASN   A OD1  1 
ATOM   531  O  OD1  B ASN   A 1 20  ? 5.820  -0.974  9.347   0.28 18.40 ?  20  ASN   A OD1  1 
ATOM   532  N  ND2  A ASN   A 1 20  ? 7.379  -1.103  7.214   0.72 17.55 ?  20  ASN   A ND2  1 
ATOM   533  N  ND2  B ASN   A 1 20  ? 6.987  -1.165  7.439   0.28 18.15 ?  20  ASN   A ND2  1 
ATOM   534  H  H    A ASN   A 1 20  ? 7.828  -5.047  9.627   0.72 15.83 ?  20  ASN   A H    1 
ATOM   535  H  H    B ASN   A 1 20  ? 8.018  -4.842  10.235  0.28 17.19 ?  20  ASN   A H    1 
ATOM   536  H  HA   A ASN   A 1 20  ? 8.762  -3.348  7.782   0.72 17.62 ?  20  ASN   A HA   1 
ATOM   537  H  HA   B ASN   A 1 20  ? 8.819  -3.227  8.256   0.28 18.64 ?  20  ASN   A HA   1 
ATOM   538  H  HB2  A ASN   A 1 20  ? 6.495  -3.749  7.721   0.72 18.80 ?  20  ASN   A HB2  1 
ATOM   539  H  HB2  B ASN   A 1 20  ? 6.596  -3.646  8.190   0.28 19.88 ?  20  ASN   A HB2  1 
ATOM   540  H  HB3  A ASN   A 1 20  ? 6.342  -3.337  9.245   0.72 18.80 ?  20  ASN   A HB3  1 
ATOM   541  H  HB3  B ASN   A 1 20  ? 6.424  -3.324  9.737   0.28 19.88 ?  20  ASN   A HB3  1 
ATOM   542  H  HD21 A ASN   A 1 20  ? 7.231  -0.296  6.963   0.72 21.03 ?  20  ASN   A HD21 1 
ATOM   543  H  HD21 B ASN   A 1 20  ? 6.806  -0.359  7.204   0.28 21.75 ?  20  ASN   A HD21 1 
ATOM   544  H  HD22 A ASN   A 1 20  ? 8.101  -1.504  6.976   0.72 21.03 ?  20  ASN   A HD22 1 
ATOM   545  H  HD22 B ASN   A 1 20  ? 7.475  -1.662  6.933   0.28 21.75 ?  20  ASN   A HD22 1 
ATOM   546  N  N    A ALA   A 1 21  ? 10.060 -1.799  9.204   0.72 15.59 ?  21  ALA   A N    1 
ATOM   547  N  N    B ALA   A 1 21  ? 10.160 -1.692  9.651   0.28 15.85 ?  21  ALA   A N    1 
ATOM   548  C  CA   A ALA   A 1 21  ? 10.761 -0.911  10.122  0.72 15.59 ?  21  ALA   A CA   1 
ATOM   549  C  CA   B ALA   A 1 21  ? 10.790 -0.610  10.389  0.28 15.93 ?  21  ALA   A CA   1 
ATOM   550  C  C    A ALA   A 1 21  ? 11.735 -0.020  9.370   0.72 15.01 ?  21  ALA   A C    1 
ATOM   551  C  C    B ALA   A 1 21  ? 11.913 -0.033  9.545   0.28 15.41 ?  21  ALA   A C    1 
ATOM   552  O  O    A ALA   A 1 21  ? 12.205 -0.364  8.281   0.72 15.27 ?  21  ALA   A O    1 
ATOM   553  O  O    B ALA   A 1 21  ? 12.501 -0.727  8.713   0.28 15.72 ?  21  ALA   A O    1 
ATOM   554  C  CB   A ALA   A 1 21  ? 11.510 -1.696  11.202  0.72 16.27 ?  21  ALA   A CB   1 
ATOM   555  C  CB   B ALA   A 1 21  ? 11.338 -1.092  11.737  0.28 16.68 ?  21  ALA   A CB   1 
ATOM   556  H  H    A ALA   A 1 21  ? 10.433 -1.900  8.436   0.72 18.67 ?  21  ALA   A H    1 
ATOM   557  H  H    B ALA   A 1 21  ? 10.636 -2.000  9.002   0.28 18.98 ?  21  ALA   A H    1 
ATOM   558  H  HA   A ALA   A 1 21  ? 10.105 -0.349  10.565  0.72 18.67 ?  21  ALA   A HA   1 
ATOM   559  H  HA   B ALA   A 1 21  ? 10.141 0.090   10.556  0.28 19.08 ?  21  ALA   A HA   1 
ATOM   560  H  HB1  A ALA   A 1 21  ? 11.938 -1.070  11.803  0.72 19.49 ?  21  ALA   A HB1  1 
ATOM   561  H  HB1  B ALA   A 1 21  ? 11.749 -0.342  12.198  0.28 19.98 ?  21  ALA   A HB1  1 
ATOM   562  H  HB2  A ALA   A 1 21  ? 10.872 -2.242  11.697  0.72 19.49 ?  21  ALA   A HB2  1 
ATOM   563  H  HB2  B ALA   A 1 21  ? 10.607 -1.444  12.268  0.28 19.98 ?  21  ALA   A HB2  1 
ATOM   564  H  HB3  A ALA   A 1 21  ? 12.170 -2.264  10.781  0.72 19.49 ?  21  ALA   A HB3  1 
ATOM   565  H  HB3  B ALA   A 1 21  ? 11.999 -1.784  11.581  0.28 19.98 ?  21  ALA   A HB3  1 
ATOM   566  N  N    A ASP   A 1 22  ? 12.014 1.133   9.982   0.72 15.61 ?  22  ASP   A N    1 
ATOM   567  N  N    B ASP   A 1 22  ? 12.180 1.254   9.754   0.28 15.19 ?  22  ASP   A N    1 
ATOM   568  C  CA   A ASP   A 1 22  ? 13.051 2.058   9.538   0.72 15.83 ?  22  ASP   A CA   1 
ATOM   569  C  CA   B ASP   A 1 22  ? 13.384 1.869   9.215   0.28 15.27 ?  22  ASP   A CA   1 
ATOM   570  C  C    A ASP   A 1 22  ? 14.378 1.572   10.110  0.72 14.90 ?  22  ASP   A C    1 
ATOM   571  C  C    B ASP   A 1 22  ? 14.601 1.201   9.846   0.28 14.15 ?  22  ASP   A C    1 
ATOM   572  O  O    A ASP   A 1 22  ? 14.570 1.566   11.330  0.72 15.28 ?  22  ASP   A O    1 
ATOM   573  O  O    B ASP   A 1 22  ? 14.687 1.073   11.071  0.28 14.30 ?  22  ASP   A O    1 
ATOM   574  C  CB   A ASP   A 1 22  ? 12.709 3.457   10.046  0.72 18.23 ?  22  ASP   A CB   1 
ATOM   575  C  CB   B ASP   A 1 22  ? 13.368 3.363   9.550   0.28 16.58 ?  22  ASP   A CB   1 
ATOM   576  C  CG   A ASP   A 1 22  ? 13.725 4.508   9.628   0.72 20.58 ?  22  ASP   A CG   1 
ATOM   577  C  CG   B ASP   A 1 22  ? 14.435 4.150   8.817   0.28 17.47 ?  22  ASP   A CG   1 
ATOM   578  O  OD1  A ASP   A 1 22  ? 14.856 4.153   9.245   0.72 21.09 ?  22  ASP   A OD1  1 
ATOM   579  O  OD1  B ASP   A 1 22  ? 15.363 3.534   8.256   0.28 17.64 ?  22  ASP   A OD1  1 
ATOM   580  O  OD2  A ASP   A 1 22  ? 13.391 5.709   9.695   0.72 22.56 -1 22  ASP   A OD2  1 
ATOM   581  O  OD2  B ASP   A 1 22  ? 14.342 5.397   8.808   0.28 18.01 -1 22  ASP   A OD2  1 
ATOM   582  H  H    A ASP   A 1 22  ? 11.581 1.407   10.677  0.72 18.71 ?  22  ASP   A H    1 
ATOM   583  H  H    B ASP   A 1 22  ? 11.670 1.793   10.192  0.28 18.20 ?  22  ASP   A H    1 
ATOM   584  H  HA   A ASP   A 1 22  ? 13.096 2.066   8.569   0.72 18.96 ?  22  ASP   A HA   1 
ATOM   585  H  HA   B ASP   A 1 22  ? 13.413 1.755   8.248   0.28 18.30 ?  22  ASP   A HA   1 
ATOM   586  H  HB2  A ASP   A 1 22  ? 11.837 3.715   9.697   0.72 21.84 ?  22  ASP   A HB2  1 
ATOM   587  H  HB2  B ASP   A 1 22  ? 12.505 3.733   9.313   0.28 19.87 ?  22  ASP   A HB2  1 
ATOM   588  H  HB3  A ASP   A 1 22  ? 12.672 3.434   11.018  0.72 21.84 ?  22  ASP   A HB3  1 
ATOM   589  H  HB3  B ASP   A 1 22  ? 13.531 3.473   10.497  0.28 19.87 ?  22  ASP   A HB3  1 
ATOM   590  N  N    A ILE   A 1 23  ? 15.289 1.152   9.229   0.72 14.22 ?  23  ILE   A N    1 
ATOM   591  N  N    B ILE   A 1 23  ? 15.536 0.752   9.003   0.28 13.47 ?  23  ILE   A N    1 
ATOM   592  C  CA   A ILE   A 1 23  ? 16.541 0.539   9.673   0.72 13.75 ?  23  ILE   A CA   1 
ATOM   593  C  CA   B ILE   A 1 23  ? 16.742 0.100   9.508   0.28 12.84 ?  23  ILE   A CA   1 
ATOM   594  C  C    A ILE   A 1 23  ? 17.340 1.485   10.561  0.72 13.78 ?  23  ILE   A C    1 
ATOM   595  C  C    B ILE   A 1 23  ? 17.509 1.038   10.426  0.28 13.48 ?  23  ILE   A C    1 
ATOM   596  O  O    A ILE   A 1 23  ? 18.066 1.038   11.459  0.72 14.30 ?  23  ILE   A O    1 
ATOM   597  O  O    B ILE   A 1 23  ? 18.178 0.594   11.368  0.28 13.35 ?  23  ILE   A O    1 
ATOM   598  C  CB   A ILE   A 1 23  ? 17.348 0.033   8.459   0.72 13.31 ?  23  ILE   A CB   1 
ATOM   599  C  CB   B ILE   A 1 23  ? 17.614 -0.429  8.348   0.28 12.12 ?  23  ILE   A CB   1 
ATOM   600  C  CG1  A ILE   A 1 23  ? 18.477 -0.894  8.917   0.72 13.04 ?  23  ILE   A CG1  1 
ATOM   601  C  CG1  B ILE   A 1 23  ? 18.698 -1.371  8.883   0.28 11.77 ?  23  ILE   A CG1  1 
ATOM   602  C  CG2  A ILE   A 1 23  ? 17.864 1.205   7.627   0.72 13.62 ?  23  ILE   A CG2  1 
ATOM   603  C  CG2  B ILE   A 1 23  ? 18.235 0.723   7.558   0.28 12.10 ?  23  ILE   A CG2  1 
ATOM   604  C  CD1  A ILE   A 1 23  ? 19.183 -1.599  7.780   0.72 13.13 ?  23  ILE   A CD1  1 
ATOM   605  C  CD1  B ILE   A 1 23  ? 19.568 -1.996  7.804   0.28 11.94 ?  23  ILE   A CD1  1 
ATOM   606  H  H    A ILE   A 1 23  ? 15.194 1.199   8.381   0.72 17.04 ?  23  ILE   A H    1 
ATOM   607  H  H    B ILE   A 1 23  ? 15.496 0.810   8.155   0.28 16.14 ?  23  ILE   A H    1 
ATOM   608  H  HA   A ILE   A 1 23  ? 16.322 -0.236  10.213  0.72 16.46 ?  23  ILE   A HA   1 
ATOM   609  H  HA   B ILE   A 1 23  ? 16.469 -0.666  10.033  0.28 15.38 ?  23  ILE   A HA   1 
ATOM   610  H  HB   A ILE   A 1 23  ? 16.748 -0.484  7.902   0.72 15.95 ?  23  ILE   A HB   1 
ATOM   611  H  HB   B ILE   A 1 23  ? 17.048 -0.935  7.748   0.28 14.51 ?  23  ILE   A HB   1 
ATOM   612  H  HG12 A ILE   A 1 23  ? 19.138 -0.369  9.396   0.72 15.62 ?  23  ILE   A HG12 1 
ATOM   613  H  HG12 B ILE   A 1 23  ? 19.282 -0.877  9.480   0.28 14.09 ?  23  ILE   A HG12 1 
ATOM   614  H  HG13 A ILE   A 1 23  ? 18.107 -1.572  9.503   0.72 15.62 ?  23  ILE   A HG13 1 
ATOM   615  H  HG13 B ILE   A 1 23  ? 18.270 -2.094  9.369   0.28 14.09 ?  23  ILE   A HG13 1 
ATOM   616  H  HG21 A ILE   A 1 23  ? 18.219 0.868   6.790   0.72 16.31 ?  23  ILE   A HG21 1 
ATOM   617  H  HG21 B ILE   A 1 23  ? 18.611 0.372   6.732   0.28 14.49 ?  23  ILE   A HG21 1 
ATOM   618  H  HG22 A ILE   A 1 23  ? 17.126 1.815   7.446   0.72 16.31 ?  23  ILE   A HG22 1 
ATOM   619  H  HG22 B ILE   A 1 23  ? 17.547 1.373   7.355   0.28 14.49 ?  23  ILE   A HG22 1 
ATOM   620  H  HG23 A ILE   A 1 23  ? 18.558 1.669   8.120   0.72 16.31 ?  23  ILE   A HG23 1 
ATOM   621  H  HG23 B ILE   A 1 23  ? 18.935 1.133   8.089   0.28 14.49 ?  23  ILE   A HG23 1 
ATOM   622  H  HD11 A ILE   A 1 23  ? 19.839 -2.207  8.150   0.72 15.73 ?  23  ILE   A HD11 1 
ATOM   623  H  HD11 B ILE   A 1 23  ? 20.153 -2.657  8.213   0.28 14.30 ?  23  ILE   A HD11 1 
ATOM   624  H  HD12 A ILE   A 1 23  ? 18.527 -2.089  7.262   0.72 15.73 ?  23  ILE   A HD12 1 
ATOM   625  H  HD12 B ILE   A 1 23  ? 18.998 -2.424  7.147   0.28 14.30 ?  23  ILE   A HD12 1 
ATOM   626  H  HD13 A ILE   A 1 23  ? 19.618 -0.936  7.223   0.72 15.73 ?  23  ILE   A HD13 1 
ATOM   627  H  HD13 B ILE   A 1 23  ? 20.100 -1.303  7.383   0.28 14.30 ?  23  ILE   A HD13 1 
ATOM   628  N  N    A VAL   A 1 24  ? 17.217 2.798   10.340  0.72 14.25 ?  24  VAL   A N    1 
ATOM   629  N  N    B VAL   A 1 24  ? 17.426 2.344   10.171  0.28 14.83 ?  24  VAL   A N    1 
ATOM   630  C  CA   A VAL   A 1 24  ? 17.902 3.762   11.199  0.72 15.92 ?  24  VAL   A CA   1 
ATOM   631  C  CA   B VAL   A 1 24  ? 18.070 3.322   11.041  0.28 15.89 ?  24  VAL   A CA   1 
ATOM   632  C  C    A VAL   A 1 24  ? 17.370 3.674   12.622  0.72 16.51 ?  24  VAL   A C    1 
ATOM   633  C  C    B VAL   A 1 24  ? 17.460 3.275   12.436  0.28 16.37 ?  24  VAL   A C    1 
ATOM   634  O  O    A VAL   A 1 24  ? 18.135 3.593   13.592  0.72 16.95 ?  24  VAL   A O    1 
ATOM   635  O  O    B VAL   A 1 24  ? 18.175 3.303   13.445  0.28 16.84 ?  24  VAL   A O    1 
ATOM   636  C  CB   A VAL   A 1 24  ? 17.764 5.185   10.629  0.72 16.86 ?  24  VAL   A CB   1 
ATOM   637  C  CB   B VAL   A 1 24  ? 17.977 4.725   10.411  0.28 16.55 ?  24  VAL   A CB   1 
ATOM   638  C  CG1  A VAL   A 1 24  ? 18.241 6.226   11.644  0.72 17.75 ?  24  VAL   A CG1  1 
ATOM   639  C  CG1  B VAL   A 1 24  ? 18.614 5.760   11.318  0.28 17.15 ?  24  VAL   A CG1  1 
ATOM   640  C  CG2  A VAL   A 1 24  ? 18.535 5.304   9.327   0.72 17.57 ?  24  VAL   A CG2  1 
ATOM   641  C  CG2  B VAL   A 1 24  ? 18.634 4.730   9.034   0.28 16.57 ?  24  VAL   A CG2  1 
ATOM   642  H  H    A VAL   A 1 24  ? 16.747 3.148   9.709   0.72 17.07 ?  24  VAL   A H    1 
ATOM   643  H  H    B VAL   A 1 24  ? 17.004 2.685   9.508   0.28 17.76 ?  24  VAL   A H    1 
ATOM   644  H  HA   A VAL   A 1 24  ? 18.843 3.544   11.222  0.72 19.08 ?  24  VAL   A HA   1 
ATOM   645  H  HA   B VAL   A 1 24  ? 19.008 3.098   11.124  0.28 19.04 ?  24  VAL   A HA   1 
ATOM   646  H  HB   A VAL   A 1 24  ? 16.830 5.360   10.433  0.72 20.21 ?  24  VAL   A HB   1 
ATOM   647  H  HB   B VAL   A 1 24  ? 17.043 4.961   10.295  0.28 19.83 ?  24  VAL   A HB   1 
ATOM   648  H  HG11 A VAL   A 1 24  ? 18.403 7.063   11.182  0.72 21.27 ?  24  VAL   A HG11 1 
ATOM   649  H  HG11 B VAL   A 1 24  ? 18.720 6.587   10.823  0.28 20.55 ?  24  VAL   A HG11 1 
ATOM   650  H  HG12 A VAL   A 1 24  ? 17.555 6.348   12.317  0.72 21.27 ?  24  VAL   A HG12 1 
ATOM   651  H  HG12 B VAL   A 1 24  ? 18.037 5.906   12.084  0.28 20.55 ?  24  VAL   A HG12 1 
ATOM   652  H  HG13 A VAL   A 1 24  ? 19.061 5.911   12.055  0.72 21.27 ?  24  VAL   A HG13 1 
ATOM   653  H  HG13 B VAL   A 1 24  ? 19.478 5.433   11.608  0.28 20.55 ?  24  VAL   A HG13 1 
ATOM   654  H  HG21 A VAL   A 1 24  ? 18.307 6.145   8.898   0.72 21.05 ?  24  VAL   A HG21 1 
ATOM   655  H  HG21 B VAL   A 1 24  ? 18.637 5.636   8.688   0.28 19.86 ?  24  VAL   A HG21 1 
ATOM   656  H  HG22 A VAL   A 1 24  ? 19.487 5.285   9.520   0.72 21.05 ?  24  VAL   A HG22 1 
ATOM   657  H  HG22 B VAL   A 1 24  ? 19.545 4.406   9.118   0.28 19.86 ?  24  VAL   A HG22 1 
ATOM   658  H  HG23 A VAL   A 1 24  ? 18.301 4.564   8.744   0.72 21.05 ?  24  VAL   A HG23 1 
ATOM   659  H  HG23 B VAL   A 1 24  ? 18.132 4.151   8.439   0.28 19.86 ?  24  VAL   A HG23 1 
ATOM   660  N  N    A GLU   A 1 25  ? 16.044 3.702   12.766  0.72 16.94 ?  25  GLU   A N    1 
ATOM   661  N  N    B GLU   A 1 25  ? 16.129 3.182   12.516  0.28 16.43 ?  25  GLU   A N    1 
ATOM   662  C  CA   A GLU   A 1 25  ? 15.450 3.646   14.096  0.72 18.04 ?  25  GLU   A CA   1 
ATOM   663  C  CA   B GLU   A 1 25  ? 15.469 3.112   13.816  0.28 17.22 ?  25  GLU   A CA   1 
ATOM   664  C  C    A GLU   A 1 25  ? 15.681 2.288   14.746  0.72 17.06 ?  25  GLU   A C    1 
ATOM   665  C  C    B GLU   A 1 25  ? 15.737 1.775   14.501  0.28 16.78 ?  25  GLU   A C    1 
ATOM   666  O  O    A GLU   A 1 25  ? 15.911 2.204   15.959  0.72 18.17 ?  25  GLU   A O    1 
ATOM   667  O  O    B GLU   A 1 25  ? 15.930 1.726   15.721  0.28 16.82 ?  25  GLU   A O    1 
ATOM   668  C  CB   A GLU   A 1 25  ? 13.961 3.987   14.016  0.72 20.84 ?  25  GLU   A CB   1 
ATOM   669  C  CB   B GLU   A 1 25  ? 13.969 3.374   13.658  0.28 18.34 ?  25  GLU   A CB   1 
ATOM   670  C  CG   A GLU   A 1 25  ? 13.702 5.448   13.665  0.72 24.29 ?  25  GLU   A CG   1 
ATOM   671  C  CG   B GLU   A 1 25  ? 13.647 4.774   13.150  0.28 20.15 ?  25  GLU   A CG   1 
ATOM   672  C  CD   A GLU   A 1 25  ? 14.515 6.410   14.520  0.72 26.98 ?  25  GLU   A CD   1 
ATOM   673  C  CD   B GLU   A 1 25  ? 14.050 5.859   14.130  0.28 21.72 ?  25  GLU   A CD   1 
ATOM   674  O  OE1  A GLU   A 1 25  ? 14.585 6.206   15.751  0.72 27.90 ?  25  GLU   A OE1  1 
ATOM   675  O  OE1  B GLU   A 1 25  ? 13.986 5.610   15.353  0.28 22.29 ?  25  GLU   A OE1  1 
ATOM   676  O  OE2  A GLU   A 1 25  ? 15.108 7.354   13.955  0.72 28.08 -1 25  GLU   A OE2  1 
ATOM   677  O  OE2  B GLU   A 1 25  ? 14.429 6.960   13.678  0.28 22.51 -1 25  GLU   A OE2  1 
ATOM   678  H  H    A GLU   A 1 25  ? 15.476 3.770   12.120  0.72 20.29 ?  25  GLU   A H    1 
ATOM   679  H  H    B GLU   A 1 25  ? 15.597 3.156   11.841  0.28 19.68 ?  25  GLU   A H    1 
ATOM   680  H  HA   A GLU   A 1 25  ? 15.879 4.307   14.658  0.72 21.61 ?  25  GLU   A HA   1 
ATOM   681  H  HA   B GLU   A 1 25  ? 15.830 3.806   14.384  0.28 20.64 ?  25  GLU   A HA   1 
ATOM   682  H  HB2  A GLU   A 1 25  ? 13.543 3.443   13.327  0.72 24.97 ?  25  GLU   A HB2  1 
ATOM   683  H  HB2  B GLU   A 1 25  ? 13.601 2.738   13.025  0.28 21.98 ?  25  GLU   A HB2  1 
ATOM   684  H  HB3  A GLU   A 1 25  ? 13.542 3.811   14.873  0.72 24.97 ?  25  GLU   A HB3  1 
ATOM   685  H  HB3  B GLU   A 1 25  ? 13.539 3.267   14.521  0.28 21.98 ?  25  GLU   A HB3  1 
ATOM   686  H  HG2  A GLU   A 1 25  ? 13.954 5.602   12.744  0.72 29.12 ?  25  GLU   A HG2  1 
ATOM   687  H  HG2  B GLU   A 1 25  ? 14.126 4.928   12.319  0.28 24.15 ?  25  GLU   A HG2  1 
ATOM   688  H  HG3  A GLU   A 1 25  ? 12.756 5.641   13.788  0.72 29.12 ?  25  GLU   A HG3  1 
ATOM   689  H  HG3  B GLU   A 1 25  ? 12.692 4.848   13.001  0.28 24.15 ?  25  GLU   A HG3  1 
ATOM   690  N  N    A GLU   A 1 26  ? 15.647 1.216   13.953  0.72 16.62 ?  26  GLU   A N    1 
ATOM   691  N  N    B GLU   A 1 26  ? 15.764 0.681   13.734  0.28 16.42 ?  26  GLU   A N    1 
ATOM   692  C  CA   A GLU   A 1 26  ? 15.944 -0.110  14.488  0.72 16.51 ?  26  GLU   A CA   1 
ATOM   693  C  CA   B GLU   A 1 26  ? 16.138 -0.609  14.310  0.28 16.58 ?  26  GLU   A CA   1 
ATOM   694  C  C    A GLU   A 1 26  ? 17.372 -0.179  15.015  0.72 15.97 ?  26  GLU   A C    1 
ATOM   695  C  C    B GLU   A 1 26  ? 17.559 -0.573  14.858  0.28 16.39 ?  26  GLU   A C    1 
ATOM   696  O  O    A GLU   A 1 26  ? 17.620 -0.692  16.112  0.72 16.73 ?  26  GLU   A O    1 
ATOM   697  O  O    B GLU   A 1 26  ? 17.844 -1.162  15.908  0.28 16.07 ?  26  GLU   A O    1 
ATOM   698  C  CB   A GLU   A 1 26  ? 15.739 -1.163  13.401  0.72 18.22 ?  26  GLU   A CB   1 
ATOM   699  C  CB   B GLU   A 1 26  ? 15.996 -1.720  13.265  0.28 17.21 ?  26  GLU   A CB   1 
ATOM   700  C  CG   A GLU   A 1 26  ? 14.315 -1.628  13.227  0.72 21.91 ?  26  GLU   A CG   1 
ATOM   701  C  CG   B GLU   A 1 26  ? 14.576 -2.198  13.050  0.28 17.32 ?  26  GLU   A CG   1 
ATOM   702  C  CD   A GLU   A 1 26  ? 13.805 -2.411  14.416  0.72 24.09 ?  26  GLU   A CD   1 
ATOM   703  C  CD   B GLU   A 1 26  ? 13.974 -2.801  14.299  0.28 16.99 ?  26  GLU   A CD   1 
ATOM   704  O  OE1  A GLU   A 1 26  ? 14.462 -3.399  14.810  0.72 24.37 ?  26  GLU   A OE1  1 
ATOM   705  O  OE1  B GLU   A 1 26  ? 14.332 -3.946  14.676  0.28 16.71 ?  26  GLU   A OE1  1 
ATOM   706  O  OE2  A GLU   A 1 26  ? 12.752 -2.021  14.957  0.72 25.98 -1 26  GLU   A OE2  1 
ATOM   707  O  OE2  B GLU   A 1 26  ? 13.140 -2.112  14.905  0.28 16.74 -1 26  GLU   A OE2  1 
ATOM   708  H  H    A GLU   A 1 26  ? 15.452 1.237   13.115  0.72 19.92 ?  26  GLU   A H    1 
ATOM   709  H  H    B GLU   A 1 26  ? 15.573 0.658   12.897  0.28 19.68 ?  26  GLU   A H    1 
ATOM   710  H  HA   A GLU   A 1 26  ? 15.336 -0.297  15.217  0.72 19.78 ?  26  GLU   A HA   1 
ATOM   711  H  HA   B GLU   A 1 26  ? 15.546 -0.810  15.048  0.28 19.87 ?  26  GLU   A HA   1 
ATOM   712  H  HB2  A GLU   A 1 26  ? 16.030 -0.791  12.551  0.72 21.83 ?  26  GLU   A HB2  1 
ATOM   713  H  HB2  B GLU   A 1 26  ? 16.323 -1.397  12.412  0.28 20.62 ?  26  GLU   A HB2  1 
ATOM   714  H  HB3  A GLU   A 1 26  ? 16.282 -1.934  13.619  0.72 21.83 ?  26  GLU   A HB3  1 
ATOM   715  H  HB3  B GLU   A 1 26  ? 16.517 -2.489  13.547  0.28 20.62 ?  26  GLU   A HB3  1 
ATOM   716  H  HG2  A GLU   A 1 26  ? 13.739 -0.860  13.141  0.72 26.26 ?  26  GLU   A HG2  1 
ATOM   717  H  HG2  B GLU   A 1 26  ? 14.028 -1.446  12.758  0.28 20.75 ?  26  GLU   A HG2  1 
ATOM   718  H  HG3  A GLU   A 1 26  ? 14.260 -2.181  12.430  0.72 26.26 ?  26  GLU   A HG3  1 
ATOM   719  H  HG3  B GLU   A 1 26  ? 14.563 -2.895  12.382  0.28 20.75 ?  26  GLU   A HG3  1 
ATOM   720  N  N    A ALA   A 1 27  ? 18.332 0.323   14.234  0.72 15.25 ?  27  ALA   A N    1 
ATOM   721  N  N    B ALA   A 1 27  ? 18.467 0.112   14.161  0.28 16.60 ?  27  ALA   A N    1 
ATOM   722  C  CA   A ALA   A 1 27  ? 19.723 0.284   14.670  0.72 15.77 ?  27  ALA   A CA   1 
ATOM   723  C  CA   B ALA   A 1 27  ? 19.849 0.171   14.626  0.28 17.24 ?  27  ALA   A CA   1 
ATOM   724  C  C    A ALA   A 1 27  ? 19.917 1.076   15.956  0.72 17.05 ?  27  ALA   A C    1 
ATOM   725  C  C    B ALA   A 1 27  ? 19.971 1.009   15.894  0.28 18.52 ?  27  ALA   A C    1 
ATOM   726  O  O    A ALA   A 1 27  ? 20.587 0.611   16.885  0.72 17.26 ?  27  ALA   A O    1 
ATOM   727  O  O    B ALA   A 1 27  ? 20.668 0.617   16.837  0.28 18.55 ?  27  ALA   A O    1 
ATOM   728  C  CB   A ALA   A 1 27  ? 20.640 0.810   13.562  0.72 15.18 ?  27  ALA   A CB   1 
ATOM   729  C  CB   B ALA   A 1 27  ? 20.756 0.715   13.521  0.28 16.91 ?  27  ALA   A CB   1 
ATOM   730  H  H    A ALA   A 1 27  ? 18.203 0.685   13.462  0.72 18.27 ?  27  ALA   A H    1 
ATOM   731  H  H    B ALA   A 1 27  ? 18.310 0.539   13.431  0.28 19.89 ?  27  ALA   A H    1 
ATOM   732  H  HA   A ALA   A 1 27  ? 19.966 -0.634  14.846  0.72 18.90 ?  27  ALA   A HA   1 
ATOM   733  H  HA   B ALA   A 1 27  ? 20.146 -0.728  14.832  0.28 20.66 ?  27  ALA   A HA   1 
ATOM   734  H  HB1  A ALA   A 1 27  ? 21.559 0.775   13.871  0.72 18.18 ?  27  ALA   A HB1  1 
ATOM   735  H  HB1  B ALA   A 1 27  ? 21.669 0.746   13.851  0.28 20.26 ?  27  ALA   A HB1  1 
ATOM   736  H  HB2  A ALA   A 1 27  ? 20.536 0.252   12.774  0.72 18.18 ?  27  ALA   A HB2  1 
ATOM   737  H  HB2  B ALA   A 1 27  ? 20.705 0.126   12.750  0.28 20.26 ?  27  ALA   A HB2  1 
ATOM   738  H  HB3  A ALA   A 1 27  ? 20.396 1.725   13.353  0.72 18.18 ?  27  ALA   A HB3  1 
ATOM   739  H  HB3  B ALA   A 1 27  ? 20.462 1.605   13.277  0.28 20.26 ?  27  ALA   A HB3  1 
ATOM   740  N  N    A LYS   A 1 28  ? 19.323 2.268   16.037  0.72 18.97 ?  28  LYS   A N    1 
ATOM   741  N  N    B LYS   A 1 28  ? 19.295 2.159   15.940  0.28 20.09 ?  28  LYS   A N    1 
ATOM   742  C  CA   A LYS   A 1 28  ? 19.475 3.079   17.240  0.72 21.71 ?  28  LYS   A CA   1 
ATOM   743  C  CA   B LYS   A 1 28  ? 19.379 3.015   17.120  0.28 21.97 ?  28  LYS   A CA   1 
ATOM   744  C  C    A LYS   A 1 28  ? 18.900 2.383   18.465  0.72 22.80 ?  28  LYS   A C    1 
ATOM   745  C  C    B LYS   A 1 28  ? 18.870 2.296   18.364  0.28 23.44 ?  28  LYS   A C    1 
ATOM   746  O  O    A LYS   A 1 28  ? 19.406 2.571   19.577  0.72 24.39 ?  28  LYS   A O    1 
ATOM   747  O  O    B LYS   A 1 28  ? 19.448 2.433   19.448  0.28 23.94 ?  28  LYS   A O    1 
ATOM   748  C  CB   A LYS   A 1 28  ? 18.846 4.459   17.039  0.72 24.01 ?  28  LYS   A CB   1 
ATOM   749  C  CB   B LYS   A 1 28  ? 18.607 4.317   16.889  0.28 22.67 ?  28  LYS   A CB   1 
ATOM   750  C  CG   A LYS   A 1 28  ? 19.714 5.390   16.208  0.72 26.36 ?  28  LYS   A CG   1 
ATOM   751  C  CG   B LYS   A 1 28  ? 19.255 5.242   15.866  0.28 23.60 ?  28  LYS   A CG   1 
ATOM   752  C  CD   A LYS   A 1 28  ? 19.231 6.828   16.262  0.72 29.18 ?  28  LYS   A CD   1 
ATOM   753  C  CD   B LYS   A 1 28  ? 18.696 6.657   15.933  0.28 24.88 ?  28  LYS   A CD   1 
ATOM   754  C  CE   A LYS   A 1 28  ? 17.963 7.012   15.457  0.72 31.15 ?  28  LYS   A CE   1 
ATOM   755  C  CE   B LYS   A 1 28  ? 17.257 6.726   15.450  0.28 25.88 ?  28  LYS   A CE   1 
ATOM   756  N  NZ   A LYS   A 1 28  ? 17.562 8.444   15.395  0.72 32.42 ?  28  LYS   A NZ   1 
ATOM   757  N  NZ   B LYS   A 1 28  ? 16.789 8.135   15.315  0.28 26.35 ?  28  LYS   A NZ   1 
ATOM   758  H  H    A LYS   A 1 28  ? 18.838 2.623   15.423  0.72 22.74 ?  28  LYS   A H    1 
ATOM   759  H  H    B LYS   A 1 28  ? 18.792 2.459   15.312  0.28 24.07 ?  28  LYS   A H    1 
ATOM   760  H  HA   A LYS   A 1 28  ? 20.418 3.213   17.409  0.72 26.02 ?  28  LYS   A HA   1 
ATOM   761  H  HA   B LYS   A 1 28  ? 20.306 3.245   17.273  0.28 26.33 ?  28  LYS   A HA   1 
ATOM   762  H  HB2  A LYS   A 1 28  ? 17.997 4.360   16.581  0.72 28.78 ?  28  LYS   A HB2  1 
ATOM   763  H  HB2  B LYS   A 1 28  ? 17.716 4.102   16.571  0.28 27.17 ?  28  LYS   A HB2  1 
ATOM   764  H  HB3  A LYS   A 1 28  ? 18.709 4.877   17.904  0.72 28.78 ?  28  LYS   A HB3  1 
ATOM   765  H  HB3  B LYS   A 1 28  ? 18.549 4.800   17.728  0.28 27.17 ?  28  LYS   A HB3  1 
ATOM   766  H  HG2  A LYS   A 1 28  ? 20.622 5.367   16.547  0.72 31.60 ?  28  LYS   A HG2  1 
ATOM   767  H  HG2  B LYS   A 1 28  ? 20.208 5.286   16.036  0.28 28.29 ?  28  LYS   A HG2  1 
ATOM   768  H  HG3  A LYS   A 1 28  ? 19.695 5.102   15.283  0.72 31.60 ?  28  LYS   A HG3  1 
ATOM   769  H  HG3  B LYS   A 1 28  ? 19.092 4.897   14.974  0.28 28.29 ?  28  LYS   A HG3  1 
ATOM   770  H  HD2  A LYS   A 1 28  ? 19.045 7.070   17.183  0.72 34.99 ?  28  LYS   A HD2  1 
ATOM   771  H  HD2  B LYS   A 1 28  ? 18.722 6.967   16.852  0.28 29.83 ?  28  LYS   A HD2  1 
ATOM   772  H  HD3  A LYS   A 1 28  ? 19.913 7.410   15.892  0.72 34.99 ?  28  LYS   A HD3  1 
ATOM   773  H  HD3  B LYS   A 1 28  ? 19.232 7.239   15.370  0.28 29.83 ?  28  LYS   A HD3  1 
ATOM   774  H  HE2  A LYS   A 1 28  ? 18.110 6.697   14.551  0.72 37.34 ?  28  LYS   A HE2  1 
ATOM   775  H  HE2  B LYS   A 1 28  ? 17.191 6.299   14.582  0.28 31.03 ?  28  LYS   A HE2  1 
ATOM   776  H  HE3  A LYS   A 1 28  ? 17.244 6.511   15.874  0.72 37.34 ?  28  LYS   A HE3  1 
ATOM   777  H  HE3  B LYS   A 1 28  ? 16.683 6.276   16.090  0.28 31.03 ?  28  LYS   A HE3  1 
ATOM   778  H  HZ1  A LYS   A 1 28  ? 16.816 8.530   14.918  0.72 38.87 ?  28  LYS   A HZ1  1 
ATOM   779  H  HZ1  B LYS   A 1 28  ? 15.946 8.151   15.031  0.28 31.59 ?  28  LYS   A HZ1  1 
ATOM   780  H  HZ2  A LYS   A 1 28  ? 17.418 8.755   16.216  0.72 38.87 ?  28  LYS   A HZ2  1 
ATOM   781  H  HZ2  B LYS   A 1 28  ? 16.838 8.549   16.101  0.28 31.59 ?  28  LYS   A HZ2  1 
ATOM   782  H  HZ3  A LYS   A 1 28  ? 18.207 8.924   15.013  0.72 38.87 ?  28  LYS   A HZ3  1 
ATOM   783  H  HZ3  B LYS   A 1 28  ? 17.300 8.570   14.728  0.28 31.59 ?  28  LYS   A HZ3  1 
ATOM   784  N  N    A LYS   A 1 29  ? 17.857 1.571   18.285  0.72 23.33 ?  29  LYS   A N    1 
ATOM   785  N  N    B LYS   A 1 29  ? 17.798 1.514   18.225  0.28 24.72 ?  29  LYS   A N    1 
ATOM   786  C  CA   A LYS   A 1 29  ? 17.256 0.859   19.409  0.72 25.25 ?  29  LYS   A CA   1 
ATOM   787  C  CA   B LYS   A 1 29  ? 17.208 0.837   19.375  0.28 26.26 ?  29  LYS   A CA   1 
ATOM   788  C  C    A LYS   A 1 29  ? 18.072 -0.372  19.793  0.72 24.85 ?  29  LYS   A C    1 
ATOM   789  C  C    B LYS   A 1 29  ? 18.015 -0.391  19.782  0.28 25.43 ?  29  LYS   A C    1 
ATOM   790  O  O    A LYS   A 1 29  ? 18.366 -0.588  20.976  0.72 26.00 ?  29  LYS   A O    1 
ATOM   791  O  O    B LYS   A 1 29  ? 18.255 -0.613  20.975  0.28 25.96 ?  29  LYS   A O    1 
ATOM   792  C  CB   A LYS   A 1 29  ? 15.821 0.456   19.060  0.72 27.99 ?  29  LYS   A CB   1 
ATOM   793  C  CB   B LYS   A 1 29  ? 15.770 0.430   19.048  0.28 28.49 ?  29  LYS   A CB   1 
ATOM   794  C  CG   A LYS   A 1 29  ? 15.073 -0.235  20.191  0.72 30.93 ?  29  LYS   A CG   1 
ATOM   795  C  CG   B LYS   A 1 29  ? 15.012 -0.203  20.205  0.28 30.54 ?  29  LYS   A CG   1 
ATOM   796  C  CD   A LYS   A 1 29  ? 14.745 0.738   21.312  0.72 33.74 ?  29  LYS   A CD   1 
ATOM   797  C  CD   B LYS   A 1 29  ? 14.658 0.827   21.264  0.28 32.32 ?  29  LYS   A CD   1 
ATOM   798  C  CE   A LYS   A 1 29  ? 13.879 0.086   22.377  0.72 35.65 ?  29  LYS   A CE   1 
ATOM   799  C  CE   B LYS   A 1 29  ? 13.774 0.227   22.346  0.28 33.59 ?  29  LYS   A CE   1 
ATOM   800  N  NZ   A LYS   A 1 29  ? 13.469 1.057   23.427  0.72 36.82 ?  29  LYS   A NZ   1 
ATOM   801  N  NZ   B LYS   A 1 29  ? 13.381 1.241   23.362  0.28 34.32 ?  29  LYS   A NZ   1 
ATOM   802  H  H    A LYS   A 1 29  ? 17.477 1.422   17.526  0.72 27.97 ?  29  LYS   A H    1 
ATOM   803  H  H    B LYS   A 1 29  ? 17.397 1.361   17.480  0.28 29.64 ?  29  LYS   A H    1 
ATOM   804  H  HA   A LYS   A 1 29  ? 17.222 1.448   20.176  0.72 30.27 ?  29  LYS   A HA   1 
ATOM   805  H  HA   B LYS   A 1 29  ? 17.186 1.447   20.127  0.28 31.49 ?  29  LYS   A HA   1 
ATOM   806  H  HB2  A LYS   A 1 29  ? 15.321 1.253   18.823  0.72 33.56 ?  29  LYS   A HB2  1 
ATOM   807  H  HB2  B LYS   A 1 29  ? 15.279 1.220   18.775  0.28 34.16 ?  29  LYS   A HB2  1 
ATOM   808  H  HB3  A LYS   A 1 29  ? 15.841 -0.154  18.307  0.72 33.56 ?  29  LYS   A HB3  1 
ATOM   809  H  HB3  B LYS   A 1 29  ? 15.785 -0.213  18.322  0.28 34.16 ?  29  LYS   A HB3  1 
ATOM   810  H  HG2  A LYS   A 1 29  ? 14.239 -0.594  19.850  0.72 37.08 ?  29  LYS   A HG2  1 
ATOM   811  H  HG2  B LYS   A 1 29  ? 14.187 -0.590  19.872  0.28 36.61 ?  29  LYS   A HG2  1 
ATOM   812  H  HG3  A LYS   A 1 29  ? 15.618 -0.950  20.558  0.72 37.08 ?  29  LYS   A HG3  1 
ATOM   813  H  HG3  B LYS   A 1 29  ? 15.559 -0.890  20.618  0.28 36.61 ?  29  LYS   A HG3  1 
ATOM   814  H  HD2  A LYS   A 1 29  ? 15.569 1.035   21.729  0.72 40.45 ?  29  LYS   A HD2  1 
ATOM   815  H  HD2  B LYS   A 1 29  ? 15.471 1.152   21.680  0.28 38.75 ?  29  LYS   A HD2  1 
ATOM   816  H  HD3  A LYS   A 1 29  ? 14.262 1.495   20.946  0.72 40.45 ?  29  LYS   A HD3  1 
ATOM   817  H  HD3  B LYS   A 1 29  ? 14.177 1.560   20.848  0.28 38.75 ?  29  LYS   A HD3  1 
ATOM   818  H  HE2  A LYS   A 1 29  ? 13.077 -0.269  21.961  0.72 42.75 ?  29  LYS   A HE2  1 
ATOM   819  H  HE2  B LYS   A 1 29  ? 12.966 -0.125  21.939  0.28 40.27 ?  29  LYS   A HE2  1 
ATOM   820  H  HE3  A LYS   A 1 29  ? 14.379 -0.629  22.802  0.72 42.75 ?  29  LYS   A HE3  1 
ATOM   821  H  HE3  B LYS   A 1 29  ? 14.258 -0.483  22.796  0.28 40.27 ?  29  LYS   A HE3  1 
ATOM   822  H  HZ1  A LYS   A 1 29  ? 12.964 0.650   24.037  0.72 44.15 ?  29  LYS   A HZ1  1 
ATOM   823  H  HZ1  B LYS   A 1 29  ? 12.865 0.866   23.983  0.28 41.15 ?  29  LYS   A HZ1  1 
ATOM   824  H  HZ2  A LYS   A 1 29  ? 14.189 1.394   23.827  0.72 44.15 ?  29  LYS   A HZ2  1 
ATOM   825  H  HZ2  B LYS   A 1 29  ? 14.107 1.576   23.753  0.28 41.15 ?  29  LYS   A HZ2  1 
ATOM   826  H  HZ3  A LYS   A 1 29  ? 13.003 1.721   23.061  0.72 44.15 ?  29  LYS   A HZ3  1 
ATOM   827  H  HZ3  B LYS   A 1 29  ? 12.930 1.902   22.973  0.28 41.15 ?  29  LYS   A HZ3  1 
ATOM   828  N  N    . VAL   A 1 30  ? 18.430 -1.200  18.810  1.00 24.11 ?  30  VAL   A N    1 
ATOM   829  C  CA   . VAL   A 1 30  ? 19.089 -2.467  19.111  1.00 22.92 ?  30  VAL   A CA   1 
ATOM   830  C  C    . VAL   A 1 30  ? 20.592 -2.316  19.341  1.00 21.73 ?  30  VAL   A C    1 
ATOM   831  O  O    . VAL   A 1 30  ? 21.172 -3.050  20.149  1.00 22.22 ?  30  VAL   A O    1 
ATOM   832  C  CB   . VAL   A 1 30  ? 18.791 -3.467  17.978  1.00 23.66 ?  30  VAL   A CB   1 
ATOM   833  C  CG1  . VAL   A 1 30  ? 19.549 -4.770  18.184  1.00 24.16 ?  30  VAL   A CG1  1 
ATOM   834  C  CG2  . VAL   A 1 30  ? 17.291 -3.730  17.878  1.00 24.21 ?  30  VAL   A CG2  1 
ATOM   835  H  H    A VAL   A 1 30  ? 18.297 -1.056  17.972  0.72 28.90 ?  30  VAL   A H    1 
ATOM   836  H  H    B VAL   A 1 30  ? 18.330 -1.043  17.969  0.28 28.90 ?  30  VAL   A H    1 
ATOM   837  H  HA   . VAL   A 1 30  ? 18.701 -2.830  19.919  1.00 27.47 ?  30  VAL   A HA   1 
ATOM   838  H  HB   . VAL   A 1 30  ? 19.080 -3.087  17.135  1.00 28.37 ?  30  VAL   A HB   1 
ATOM   839  H  HG11 . VAL   A 1 30  ? 19.174 -5.447  17.597  1.00 28.96 ?  30  VAL   A HG11 1 
ATOM   840  H  HG12 . VAL   A 1 30  ? 20.483 -4.630  17.971  1.00 28.96 ?  30  VAL   A HG12 1 
ATOM   841  H  HG13 . VAL   A 1 30  ? 19.453 -5.047  19.108  1.00 28.96 ?  30  VAL   A HG13 1 
ATOM   842  H  HG21 . VAL   A 1 30  ? 17.131 -4.401  17.195  1.00 29.03 ?  30  VAL   A HG21 1 
ATOM   843  H  HG22 . VAL   A 1 30  ? 16.968 -4.050  18.736  1.00 29.03 ?  30  VAL   A HG22 1 
ATOM   844  H  HG23 . VAL   A 1 30  ? 16.840 -2.905  17.642  1.00 29.03 ?  30  VAL   A HG23 1 
ATOM   845  N  N    . LYS   A 1 31  ? 21.240 -1.380  18.657  1.00 20.66 ?  31  LYS   A N    1 
ATOM   846  C  CA   . LYS   A 1 31  ? 22.696 -1.289  18.617  1.00 21.43 ?  31  LYS   A CA   1 
ATOM   847  C  C    . LYS   A 1 31  ? 23.299 -2.653  18.269  1.00 19.44 ?  31  LYS   A C    1 
ATOM   848  O  O    . LYS   A 1 31  ? 24.073 -3.218  19.048  1.00 20.87 ?  31  LYS   A O    1 
ATOM   849  C  CB   . LYS   A 1 31  ? 23.271 -0.751  19.920  1.00 26.13 ?  31  LYS   A CB   1 
ATOM   850  C  CG   . LYS   A 1 31  ? 22.572 0.501   20.423  1.00 32.33 ?  31  LYS   A CG   1 
ATOM   851  C  CD   . LYS   A 1 31  ? 23.567 1.557   20.881  1.00 37.19 ?  31  LYS   A CD   1 
ATOM   852  C  CE   . LYS   A 1 31  ? 22.895 2.610   21.751  1.00 40.57 ?  31  LYS   A CE   1 
ATOM   853  N  NZ   . LYS   A 1 31  ? 21.738 3.263   21.080  1.00 42.06 ?  31  LYS   A NZ   1 
ATOM   854  H  H    . LYS   A 1 31  ? 20.849 -0.768  18.191  1.00 24.76 ?  31  LYS   A H    1 
ATOM   855  H  HA   . LYS   A 1 31  ? 22.940 -0.670  17.911  1.00 25.69 ?  31  LYS   A HA   1 
ATOM   856  H  HB2  . LYS   A 1 31  ? 23.192 -1.433  20.601  1.00 31.33 ?  31  LYS   A HB2  1 
ATOM   857  H  HB3  . LYS   A 1 31  ? 24.207 -0.532  19.778  1.00 31.33 ?  31  LYS   A HB3  1 
ATOM   858  H  HG2  . LYS   A 1 31  ? 22.037 0.880   19.708  1.00 38.76 ?  31  LYS   A HG2  1 
ATOM   859  H  HG3  . LYS   A 1 31  ? 22.008 0.269   21.177  1.00 38.76 ?  31  LYS   A HG3  1 
ATOM   860  H  HD2  . LYS   A 1 31  ? 24.270 1.134   21.400  1.00 44.59 ?  31  LYS   A HD2  1 
ATOM   861  H  HD3  . LYS   A 1 31  ? 23.946 2.000   20.104  1.00 44.59 ?  31  LYS   A HD3  1 
ATOM   862  H  HE2  . LYS   A 1 31  ? 22.569 2.186   22.559  1.00 48.65 ?  31  LYS   A HE2  1 
ATOM   863  H  HE3  . LYS   A 1 31  ? 23.542 3.298   21.975  1.00 48.65 ?  31  LYS   A HE3  1 
ATOM   864  H  HZ1  . LYS   A 1 31  ? 21.384 3.881   21.615  1.00 50.44 ?  31  LYS   A HZ1  1 
ATOM   865  H  HZ2  . LYS   A 1 31  ? 22.003 3.652   20.325  1.00 50.44 ?  31  LYS   A HZ2  1 
ATOM   866  H  HZ3  . LYS   A 1 31  ? 21.115 2.656   20.889  1.00 50.44 ?  31  LYS   A HZ3  1 
ATOM   867  N  N    . PRO   A 1 32  ? 22.960 -3.202  17.107  1.00 17.09 ?  32  PRO   A N    1 
ATOM   868  C  CA   . PRO   A 1 32  ? 23.432 -4.540  16.753  1.00 17.26 ?  32  PRO   A CA   1 
ATOM   869  C  C    . PRO   A 1 32  ? 24.934 -4.554  16.547  1.00 17.26 ?  32  PRO   A C    1 
ATOM   870  O  O    . PRO   A 1 32  ? 25.576 -3.522  16.338  1.00 17.41 ?  32  PRO   A O    1 
ATOM   871  C  CB   . PRO   A 1 32  ? 22.705 -4.823  15.434  1.00 17.45 ?  32  PRO   A CB   1 
ATOM   872  C  CG   . PRO   A 1 32  ? 22.523 -3.460  14.830  1.00 15.99 ?  32  PRO   A CG   1 
ATOM   873  C  CD   . PRO   A 1 32  ? 22.228 -2.569  15.998  1.00 16.14 ?  32  PRO   A CD   1 
ATOM   874  H  HA   . PRO   A 1 32  ? 23.177 -5.192  17.425  1.00 20.68 ?  32  PRO   A HA   1 
ATOM   875  H  HB2  . PRO   A 1 32  ? 23.255 -5.389  14.866  1.00 20.91 ?  32  PRO   A HB2  1 
ATOM   876  H  HB3  . PRO   A 1 32  ? 21.848 -5.247  15.613  1.00 20.91 ?  32  PRO   A HB3  1 
ATOM   877  H  HG2  . PRO   A 1 32  ? 23.337 -3.195  14.381  1.00 19.15 ?  32  PRO   A HG2  1 
ATOM   878  H  HG3  . PRO   A 1 32  ? 21.775 -3.481  14.210  1.00 19.15 ?  32  PRO   A HG3  1 
ATOM   879  H  HD2  . PRO   A 1 32  ? 22.571 -1.679  15.822  1.00 19.34 ?  32  PRO   A HD2  1 
ATOM   880  H  HD3  . PRO   A 1 32  ? 21.278 -2.559  16.178  1.00 19.34 ?  32  PRO   A HD3  1 
ATOM   881  N  N    . THR   A 1 33  ? 25.490 -5.763  16.578  1.00 17.21 ?  33  THR   A N    1 
ATOM   882  C  CA   . THR   A 1 33  ? 26.902 -5.922  16.260  1.00 17.37 ?  33  THR   A CA   1 
ATOM   883  C  C    . THR   A 1 33  ? 27.198 -5.461  14.839  1.00 15.90 ?  33  THR   A C    1 
ATOM   884  O  O    . THR   A 1 33  ? 28.228 -4.819  14.589  1.00 16.06 ?  33  THR   A O    1 
ATOM   885  C  CB   . THR   A 1 33  ? 27.318 -7.379  16.461  1.00 19.20 ?  33  THR   A CB   1 
ATOM   886  O  OG1  . THR   A 1 33  ? 27.025 -7.774  17.805  1.00 21.03 ?  33  THR   A OG1  1 
ATOM   887  C  CG2  . THR   A 1 33  ? 28.805 -7.554  16.201  1.00 20.04 ?  33  THR   A CG2  1 
ATOM   888  H  H    . THR   A 1 33  ? 25.078 -6.497  16.768  1.00 20.62 ?  33  THR   A H    1 
ATOM   889  H  HA   . THR   A 1 33  ? 27.425 -5.378  16.868  1.00 20.81 ?  33  THR   A HA   1 
ATOM   890  H  HB   . THR   A 1 33  ? 26.829 -7.950  15.842  1.00 23.01 ?  33  THR   A HB   1 
ATOM   891  H  HG1  . THR   A 1 33  ? 27.449 -7.288  18.346  1.00 25.20 ?  33  THR   A HG1  1 
ATOM   892  H  HG21 . THR   A 1 33  ? 29.090 -8.436  16.491  1.00 24.02 ?  33  THR   A HG21 1 
ATOM   893  H  HG22 . THR   A 1 33  ? 28.994 -7.459  15.256  1.00 24.02 ?  33  THR   A HG22 1 
ATOM   894  H  HG23 . THR   A 1 33  ? 29.305 -6.886  16.695  1.00 24.02 ?  33  THR   A HG23 1 
ATOM   895  N  N    . VAL   A 1 34  ? 26.307 -5.780  13.898  1.00 14.09 ?  34  VAL   A N    1 
ATOM   896  C  CA   . VAL   A 1 34  ? 26.491 -5.439  12.492  1.00 12.99 ?  34  VAL   A CA   1 
ATOM   897  C  C    . VAL   A 1 34  ? 25.190 -4.882  11.928  1.00 12.13 ?  34  VAL   A C    1 
ATOM   898  O  O    . VAL   A 1 34  ? 24.152 -5.556  11.967  1.00 13.10 ?  34  VAL   A O    1 
ATOM   899  C  CB   . VAL   A 1 34  ? 26.940 -6.643  11.644  1.00 13.71 ?  34  VAL   A CB   1 
ATOM   900  C  CG1  . VAL   A 1 34  ? 27.095 -6.237  10.183  1.00 13.71 ?  34  VAL   A CG1  1 
ATOM   901  C  CG2  . VAL   A 1 34  ? 28.224 -7.256  12.196  1.00 15.17 ?  34  VAL   A CG2  1 
ATOM   902  H  H    . VAL   A 1 34  ? 25.576 -6.206  14.053  1.00 16.87 ?  34  VAL   A H    1 
ATOM   903  H  HA   . VAL   A 1 34  ? 27.167 -4.746  12.411  1.00 15.56 ?  34  VAL   A HA   1 
ATOM   904  H  HB   . VAL   A 1 34  ? 26.246 -7.322  11.690  1.00 16.42 ?  34  VAL   A HB   1 
ATOM   905  H  HG11 . VAL   A 1 34  ? 27.602 -6.923  9.722   1.00 16.42 ?  34  VAL   A HG11 1 
ATOM   906  H  HG12 . VAL   A 1 34  ? 26.217 -6.148  9.782   1.00 16.42 ?  34  VAL   A HG12 1 
ATOM   907  H  HG13 . VAL   A 1 34  ? 27.569 -5.392  10.142  1.00 16.42 ?  34  VAL   A HG13 1 
ATOM   908  H  HG21 . VAL   A 1 34  ? 28.492 -7.990  11.620  1.00 18.18 ?  34  VAL   A HG21 1 
ATOM   909  H  HG22 . VAL   A 1 34  ? 28.914 -6.579  12.214  1.00 18.18 ?  34  VAL   A HG22 1 
ATOM   910  H  HG23 . VAL   A 1 34  ? 28.057 -7.586  13.094  1.00 18.18 ?  34  VAL   A HG23 1 
ATOM   911  N  N    . VAL   A 1 35  ? 25.250 -3.668  11.377  1.00 11.77 ?  35  VAL   A N    1 
ATOM   912  C  CA   . VAL   A 1 35  ? 24.216 -3.158  10.487  1.00 11.32 ?  35  VAL   A CA   1 
ATOM   913  C  C    . VAL   A 1 35  ? 24.772 -3.160  9.072   1.00 10.69 ?  35  VAL   A C    1 
ATOM   914  O  O    . VAL   A 1 35  ? 25.914 -2.743  8.844   1.00 11.19 ?  35  VAL   A O    1 
ATOM   915  C  CB   . VAL   A 1 35  ? 23.693 -1.762  10.892  1.00 11.75 ?  35  VAL   A CB   1 
ATOM   916  C  CG1  . VAL   A 1 35  ? 24.770 -0.666  10.771  1.00 12.61 ?  35  VAL   A CG1  1 
ATOM   917  C  CG2  . VAL   A 1 35  ? 22.457 -1.409  10.064  1.00 12.70 ?  35  VAL   A CG2  1 
ATOM   918  H  H    . VAL   A 1 35  ? 25.886 -3.107  11.509  1.00 14.10 ?  35  VAL   A H    1 
ATOM   919  H  HA   . VAL   A 1 35  ? 23.457 -3.765  10.504  1.00 13.56 ?  35  VAL   A HA   1 
ATOM   920  H  HB   . VAL   A 1 35  ? 23.409 -1.795  11.817  1.00 14.07 ?  35  VAL   A HB   1 
ATOM   921  H  HG11 . VAL   A 1 35  ? 24.419 0.166   11.130  1.00 15.11 ?  35  VAL   A HG11 1 
ATOM   922  H  HG12 . VAL   A 1 35  ? 25.552 -0.938  11.274  1.00 15.11 ?  35  VAL   A HG12 1 
ATOM   923  H  HG13 . VAL   A 1 35  ? 25.002 -0.546  9.836   1.00 15.11 ?  35  VAL   A HG13 1 
ATOM   924  H  HG21 . VAL   A 1 35  ? 22.096 -0.565  10.370  1.00 15.22 ?  35  VAL   A HG21 1 
ATOM   925  H  HG22 . VAL   A 1 35  ? 22.713 -1.335  9.126   1.00 15.22 ?  35  VAL   A HG22 1 
ATOM   926  H  HG23 . VAL   A 1 35  ? 21.794 -2.111  10.164  1.00 15.22 ?  35  VAL   A HG23 1 
ATOM   927  N  N    . VAL   A 1 36  ? 23.963 -3.627  8.122   1.00 10.17 ?  36  VAL   A N    1 
ATOM   928  C  CA   . VAL   A 1 36  ? 24.342 -3.635  6.715   1.00 9.89  ?  36  VAL   A CA   1 
ATOM   929  C  C    . VAL   A 1 36  ? 23.880 -2.344  6.052   1.00 10.21 ?  36  VAL   A C    1 
ATOM   930  O  O    . VAL   A 1 36  ? 22.717 -1.941  6.190   1.00 10.72 ?  36  VAL   A O    1 
ATOM   931  C  CB   . VAL   A 1 36  ? 23.736 -4.850  5.994   1.00 10.20 ?  36  VAL   A CB   1 
ATOM   932  C  CG1  . VAL   A 1 36  ? 23.992 -4.763  4.504   1.00 10.45 ?  36  VAL   A CG1  1 
ATOM   933  C  CG2  . VAL   A 1 36  ? 24.284 -6.145  6.574   1.00 11.08 ?  36  VAL   A CG2  1 
ATOM   934  H  H    . VAL   A 1 36  ? 23.177 -3.957  8.268   1.00 12.18 ?  36  VAL   A H    1 
ATOM   935  H  HA   . VAL   A 1 36  ? 25.310 -3.692  6.643   1.00 11.84 ?  36  VAL   A HA   1 
ATOM   936  H  HB   . VAL   A 1 36  ? 22.778 -4.844  6.130   1.00 12.22 ?  36  VAL   A HB   1 
ATOM   937  H  HG11 . VAL   A 1 36  ? 23.861 -5.640  4.111   1.00 12.51 ?  36  VAL   A HG11 1 
ATOM   938  H  HG12 . VAL   A 1 36  ? 23.367 -4.132  4.109   1.00 12.51 ?  36  VAL   A HG12 1 
ATOM   939  H  HG13 . VAL   A 1 36  ? 24.902 -4.466  4.355   1.00 12.51 ?  36  VAL   A HG13 1 
ATOM   940  H  HG21 . VAL   A 1 36  ? 23.900 -6.897  6.090   1.00 13.27 ?  36  VAL   A HG21 1 
ATOM   941  H  HG22 . VAL   A 1 36  ? 25.251 -6.154  6.473   1.00 13.27 ?  36  VAL   A HG22 1 
ATOM   942  H  HG23 . VAL   A 1 36  ? 24.049 -6.203  7.511   1.00 13.27 ?  36  VAL   A HG23 1 
ATOM   943  N  N    . ASN   A 1 37  ? 24.791 -1.709  5.316   1.00 9.48  ?  37  ASN   A N    1 
ATOM   944  C  CA   . ASN   A 1 37  ? 24.464 -0.592  4.447   1.00 9.38  ?  37  ASN   A CA   1 
ATOM   945  C  C    . ASN   A 1 37  ? 24.321 -1.064  3.010   1.00 9.41  ?  37  ASN   A C    1 
ATOM   946  O  O    . ASN   A 1 37  ? 25.103 -1.892  2.528   1.00 10.07 ?  37  ASN   A O    1 
ATOM   947  C  CB   . ASN   A 1 37  ? 25.542 0.485   4.522   1.00 9.91  ?  37  ASN   A CB   1 
ATOM   948  C  CG   . ASN   A 1 37  ? 25.213 1.688   3.672   1.00 9.99  ?  37  ASN   A CG   1 
ATOM   949  O  OD1  . ASN   A 1 37  ? 24.038 2.025   3.486   1.00 10.56 ?  37  ASN   A OD1  1 
ATOM   950  N  ND2  . ASN   A 1 37  ? 26.244 2.343   3.151   1.00 10.18 ?  37  ASN   A ND2  1 
ATOM   951  H  H    . ASN   A 1 37  ? 25.630 -1.904  5.321   1.00 11.35 ?  37  ASN   A H    1 
ATOM   952  H  HA   . ASN   A 1 37  ? 23.627 -0.197  4.732   1.00 11.22 ?  37  ASN   A HA   1 
ATOM   953  H  HB2  . ASN   A 1 37  ? 25.634 0.783   5.443   1.00 11.87 ?  37  ASN   A HB2  1 
ATOM   954  H  HB3  . ASN   A 1 37  ? 26.387 0.114   4.212   1.00 11.87 ?  37  ASN   A HB3  1 
ATOM   955  H  HD21 . ASN   A 1 37  ? 26.109 3.033   2.655   1.00 12.18 ?  37  ASN   A HD21 1 
ATOM   956  H  HD22 . ASN   A 1 37  ? 27.045 2.081   3.300   1.00 12.18 ?  37  ASN   A HD22 1 
ATOM   957  N  N    A ALA   A 1 38  ? 23.310 -0.513  2.334   0.72 9.72  ?  38  ALA   A N    1 
ATOM   958  N  N    B ALA   A 1 38  ? 23.309 -0.537  2.320   0.28 9.89  ?  38  ALA   A N    1 
ATOM   959  C  CA   A ALA   A 1 38  ? 23.109 -0.659  0.893   0.72 9.84  ?  38  ALA   A CA   1 
ATOM   960  C  CA   B ALA   A 1 38  ? 23.144 -0.786  0.888   0.28 10.45 ?  38  ALA   A CA   1 
ATOM   961  C  C    A ALA   A 1 38  ? 24.028 0.331   0.178   0.72 9.60  ?  38  ALA   A C    1 
ATOM   962  C  C    B ALA   A 1 38  ? 23.965 0.256   0.130   0.28 10.36 ?  38  ALA   A C    1 
ATOM   963  O  O    A ALA   A 1 38  ? 23.629 1.429   -0.218  0.72 9.61  ?  38  ALA   A O    1 
ATOM   964  O  O    B ALA   A 1 38  ? 23.455 1.252   -0.389  0.28 10.43 ?  38  ALA   A O    1 
ATOM   965  C  CB   A ALA   A 1 38  ? 21.642 -0.413  0.552   0.72 10.56 ?  38  ALA   A CB   1 
ATOM   966  C  CB   B ALA   A 1 38  ? 21.670 -0.758  0.507   0.28 11.06 ?  38  ALA   A CB   1 
ATOM   967  H  H    A ALA   A 1 38  ? 22.714 -0.016  2.710   0.72 11.63 ?  38  ALA   A H    1 
ATOM   968  H  H    B ALA   A 1 38  ? 22.702 -0.028  2.664   0.28 11.84 ?  38  ALA   A H    1 
ATOM   969  H  HA   A ALA   A 1 38  ? 23.349 -1.554  0.623   0.72 11.78 ?  38  ALA   A HA   1 
ATOM   970  H  HA   B ALA   A 1 38  ? 23.496 -1.665  0.679   0.28 12.51 ?  38  ALA   A HA   1 
ATOM   971  H  HB1  A ALA   A 1 38  ? 21.518 -0.514  -0.403  0.72 12.65 ?  38  ALA   A HB1  1 
ATOM   972  H  HB1  B ALA   A 1 38  ? 21.593 -0.890  -0.450  0.28 13.25 ?  38  ALA   A HB1  1 
ATOM   973  H  HB2  A ALA   A 1 38  ? 21.094 -1.059  1.028   0.72 12.65 ?  38  ALA   A HB2  1 
ATOM   974  H  HB2  B ALA   A 1 38  ? 21.204 -1.468  0.978   0.28 13.25 ?  38  ALA   A HB2  1 
ATOM   975  H  HB3  A ALA   A 1 38  ? 21.398 0.487   0.824   0.72 12.65 ?  38  ALA   A HB3  1 
ATOM   976  H  HB3  B ALA   A 1 38  ? 21.296 0.102   0.751   0.28 13.25 ?  38  ALA   A HB3  1 
ATOM   977  N  N    A ALA   A 1 39  ? 25.291 -0.066  0.028   0.72 9.89  ?  39  ALA   A N    1 
ATOM   978  N  N    B ALA   A 1 39  ? 25.272 0.015   0.079   0.28 10.44 ?  39  ALA   A N    1 
ATOM   979  C  CA   A ALA   A 1 39  ? 26.346 0.811   -0.453  0.72 9.83  ?  39  ALA   A CA   1 
ATOM   980  C  CA   B ALA   A 1 39  ? 26.221 0.982   -0.445  0.28 10.70 ?  39  ALA   A CA   1 
ATOM   981  C  C    A ALA   A 1 39  ? 26.454 0.783   -1.979  0.72 10.07 ?  39  ALA   A C    1 
ATOM   982  C  C    B ALA   A 1 39  ? 26.418 0.810   -1.947  0.28 10.01 ?  39  ALA   A C    1 
ATOM   983  O  O    A ALA   A 1 39  ? 25.918 -0.097  -2.660  0.72 10.68 ?  39  ALA   A O    1 
ATOM   984  O  O    B ALA   A 1 39  ? 26.091 -0.226  -2.532  0.28 9.51  ?  39  ALA   A O    1 
ATOM   985  C  CB   A ALA   A 1 39  ? 27.679 0.396   0.181   0.72 10.07 ?  39  ALA   A CB   1 
ATOM   986  C  CB   B ALA   A 1 39  ? 27.567 0.815   0.258   0.28 11.73 ?  39  ALA   A CB   1 
ATOM   987  H  H    A ALA   A 1 39  ? 25.559 -0.866  0.205   0.72 11.84 ?  39  ALA   A H    1 
ATOM   988  H  H    B ALA   A 1 39  ? 25.636 -0.719  0.347   0.28 12.50 ?  39  ALA   A H    1 
ATOM   989  H  HA   A ALA   A 1 39  ? 26.148 1.720   -0.179  0.72 11.77 ?  39  ALA   A HA   1 
ATOM   990  H  HA   B ALA   A 1 39  ? 25.891 1.879   -0.276  0.28 12.81 ?  39  ALA   A HA   1 
ATOM   991  H  HB1  A ALA   A 1 39  ? 28.375 0.990   -0.141  0.72 12.05 ?  39  ALA   A HB1  1 
ATOM   992  H  HB1  B ALA   A 1 39  ? 28.189 1.468   -0.098  0.28 14.04 ?  39  ALA   A HB1  1 
ATOM   993  H  HB2  A ALA   A 1 39  ? 27.604 0.474   1.149   0.72 12.05 ?  39  ALA   A HB2  1 
ATOM   994  H  HB2  B ALA   A 1 39  ? 27.445 0.956   1.209   0.28 14.04 ?  39  ALA   A HB2  1 
ATOM   995  H  HB3  A ALA   A 1 39  ? 27.876 -0.517  -0.063  0.72 12.05 ?  39  ALA   A HB3  1 
ATOM   996  H  HB3  B ALA   A 1 39  ? 27.897 -0.082  0.095   0.28 14.04 ?  39  ALA   A HB3  1 
ATOM   997  N  N    A ASN   A 1 40  ? 27.177 1.768   -2.513  0.72 10.37 ?  40  ASN   A N    1 
ATOM   998  N  N    B ASN   A 1 40  ? 26.975 1.848   -2.566  0.28 10.06 ?  40  ASN   A N    1 
ATOM   999  C  CA   A ASN   A 1 40  ? 27.718 1.721   -3.866  0.72 10.17 ?  40  ASN   A CA   1 
ATOM   1000 C  CA   B ASN   A 1 40  ? 27.450 1.781   -3.940  0.28 10.29 ?  40  ASN   A CA   1 
ATOM   1001 C  C    A ASN   A 1 40  ? 29.242 1.614   -3.796  0.72 9.51  ?  40  ASN   A C    1 
ATOM   1002 C  C    B ASN   A 1 40  ? 28.973 1.645   -3.944  0.28 10.21 ?  40  ASN   A C    1 
ATOM   1003 O  O    A ASN   A 1 40  ? 29.841 1.722   -2.724  0.72 9.82  ?  40  ASN   A O    1 
ATOM   1004 O  O    B ASN   A 1 40  ? 29.628 1.710   -2.903  0.28 10.26 ?  40  ASN   A O    1 
ATOM   1005 C  CB   A ASN   A 1 40  ? 27.233 2.903   -4.727  0.72 11.31 ?  40  ASN   A CB   1 
ATOM   1006 C  CB   B ASN   A 1 40  ? 26.990 3.010   -4.735  0.28 11.05 ?  40  ASN   A CB   1 
ATOM   1007 C  CG   A ASN   A 1 40  ? 27.616 4.259   -4.163  0.72 11.80 ?  40  ASN   A CG   1 
ATOM   1008 C  CG   B ASN   A 1 40  ? 27.355 4.317   -4.060  0.28 11.77 ?  40  ASN   A CG   1 
ATOM   1009 O  OD1  A ASN   A 1 40  ? 28.788 4.511   -3.847  0.72 12.77 ?  40  ASN   A OD1  1 
ATOM   1010 O  OD1  B ASN   A 1 40  ? 28.532 4.628   -3.875  0.28 12.86 ?  40  ASN   A OD1  1 
ATOM   1011 N  ND2  A ASN   A 1 40  ? 26.620 5.144   -4.035  0.72 12.36 ?  40  ASN   A ND2  1 
ATOM   1012 N  ND2  B ASN   A 1 40  ? 26.341 5.094   -3.696  0.28 11.99 ?  40  ASN   A ND2  1 
ATOM   1013 H  H    A ASN   A 1 40  ? 27.379 2.484   -2.092  0.72 12.41 ?  40  ASN   A H    1 
ATOM   1014 H  H    B ASN   A 1 40  ? 27.093 2.618   -2.198  0.28 12.04 ?  40  ASN   A H    1 
ATOM   1015 H  HA   A ASN   A 1 40  ? 27.403 0.909   -4.291  0.72 12.18 ?  40  ASN   A HA   1 
ATOM   1016 H  HA   B ASN   A 1 40  ? 27.076 0.991   -4.364  0.28 12.31 ?  40  ASN   A HA   1 
ATOM   1017 H  HB2  A ASN   A 1 40  ? 27.623 2.824   -5.612  0.72 13.54 ?  40  ASN   A HB2  1 
ATOM   1018 H  HB2  B ASN   A 1 40  ? 27.408 2.993   -5.607  0.28 13.23 ?  40  ASN   A HB2  1 
ATOM   1019 H  HB3  A ASN   A 1 40  ? 26.266 2.863   -4.789  0.72 13.54 ?  40  ASN   A HB3  1 
ATOM   1020 H  HB3  B ASN   A 1 40  ? 26.022 2.976   -4.828  0.28 13.23 ?  40  ASN   A HB3  1 
ATOM   1021 H  HD21 A ASN   A 1 40  ? 26.777 5.930   -3.722  0.72 14.80 ?  40  ASN   A HD21 1 
ATOM   1022 H  HD21 B ASN   A 1 40  ? 26.496 5.843   -3.307  0.28 14.36 ?  40  ASN   A HD21 1 
ATOM   1023 H  HD22 A ASN   A 1 40  ? 25.818 4.927   -4.264  0.72 14.80 ?  40  ASN   A HD22 1 
ATOM   1024 H  HD22 B ASN   A 1 40  ? 25.530 4.845   -3.844  0.28 14.36 ?  40  ASN   A HD22 1 
ATOM   1025 N  N    A VAL   A 1 41  ? 29.864 1.352   -4.949  0.72 9.92  ?  41  VAL   A N    1 
ATOM   1026 N  N    B VAL   A 1 41  ? 29.538 1.447   -5.138  0.28 10.28 ?  41  VAL   A N    1 
ATOM   1027 C  CA   A VAL   A 1 41  ? 31.293 1.050   -4.969  0.72 10.17 ?  41  VAL   A CA   1 
ATOM   1028 C  CA   B VAL   A 1 41  ? 30.963 1.121   -5.229  0.28 10.58 ?  41  VAL   A CA   1 
ATOM   1029 C  C    A VAL   A 1 41  ? 32.145 2.213   -4.503  0.72 10.82 ?  41  VAL   A C    1 
ATOM   1030 C  C    B VAL   A 1 41  ? 31.839 2.246   -4.696  0.28 10.84 ?  41  VAL   A C    1 
ATOM   1031 O  O    A VAL   A 1 41  ? 33.297 2.002   -4.102  0.72 11.02 ?  41  VAL   A O    1 
ATOM   1032 O  O    B VAL   A 1 41  ? 32.968 1.999   -4.250  0.28 11.28 ?  41  VAL   A O    1 
ATOM   1033 C  CB   A VAL   A 1 41  ? 31.781 0.564   -6.351  0.72 10.80 ?  41  VAL   A CB   1 
ATOM   1034 C  CB   B VAL   A 1 41  ? 31.367 0.716   -6.661  0.28 11.34 ?  41  VAL   A CB   1 
ATOM   1035 C  CG1  A VAL   A 1 41  ? 31.097 -0.741  -6.746  0.72 11.70 ?  41  VAL   A CG1  1 
ATOM   1036 C  CG1  B VAL   A 1 41  ? 30.724 -0.607  -7.041  0.28 11.96 ?  41  VAL   A CG1  1 
ATOM   1037 C  CG2  A VAL   A 1 41  ? 31.622 1.640   -7.430  0.72 10.56 ?  41  VAL   A CG2  1 
ATOM   1038 C  CG2  B VAL   A 1 41  ? 31.011 1.809   -7.661  0.28 11.84 ?  41  VAL   A CG2  1 
ATOM   1039 H  H    A VAL   A 1 41  ? 29.488 1.338   -5.718  0.72 11.87 ?  41  VAL   A H    1 
ATOM   1040 H  H    B VAL   A 1 41  ? 29.124 1.490   -5.891  0.28 12.30 ?  41  VAL   A H    1 
ATOM   1041 H  HA   A VAL   A 1 41  ? 31.457 0.327   -4.346  0.72 12.17 ?  41  VAL   A HA   1 
ATOM   1042 H  HA   B VAL   A 1 41  ? 31.123 0.353   -4.665  0.28 12.67 ?  41  VAL   A HA   1 
ATOM   1043 H  HB   A VAL   A 1 41  ? 32.730 0.370   -6.286  0.72 12.92 ?  41  VAL   A HB   1 
ATOM   1044 H  HB   B VAL   A 1 41  ? 32.328 0.593   -6.689  0.28 13.57 ?  41  VAL   A HB   1 
ATOM   1045 H  HG11 A VAL   A 1 41  ? 31.435 -1.033  -7.606  0.72 14.01 ?  41  VAL   A HG11 1 
ATOM   1046 H  HG11 B VAL   A 1 41  ? 30.931 -0.803  -7.967  0.28 14.32 ?  41  VAL   A HG11 1 
ATOM   1047 H  HG12 A VAL   A 1 41  ? 31.282 -1.414  -6.071  0.72 14.01 ?  41  VAL   A HG12 1 
ATOM   1048 H  HG12 B VAL   A 1 41  ? 31.081 -1.305  -6.468  0.28 14.32 ?  41  VAL   A HG12 1 
ATOM   1049 H  HG13 A VAL   A 1 41  ? 30.138 -0.590  -6.803  0.72 14.01 ?  41  VAL   A HG13 1 
ATOM   1050 H  HG13 B VAL   A 1 41  ? 29.766 -0.541  -6.922  0.28 14.32 ?  41  VAL   A HG13 1 
ATOM   1051 H  HG21 A VAL   A 1 41  ? 31.845 1.255   -8.294  0.72 12.64 ?  41  VAL   A HG21 1 
ATOM   1052 H  HG21 B VAL   A 1 41  ? 31.344 1.554   -8.537  0.28 14.18 ?  41  VAL   A HG21 1 
ATOM   1053 H  HG22 A VAL   A 1 41  ? 30.707 1.951   -7.431  0.72 12.64 ?  41  VAL   A HG22 1 
ATOM   1054 H  HG22 B VAL   A 1 41  ? 30.046 1.910   -7.694  0.28 14.18 ?  41  VAL   A HG22 1 
ATOM   1055 H  HG23 A VAL   A 1 41  ? 32.225 2.374   -7.232  0.72 12.64 ?  41  VAL   A HG23 1 
ATOM   1056 H  HG23 B VAL   A 1 41  ? 31.422 2.640   -7.381  0.28 14.18 ?  41  VAL   A HG23 1 
ATOM   1057 N  N    A TYR   A 1 42  ? 31.627 3.443   -4.578  0.72 10.64 ?  42  TYR   A N    1 
ATOM   1058 N  N    B TYR   A 1 42  ? 31.358 3.489   -4.740  0.28 10.92 ?  42  TYR   A N    1 
ATOM   1059 C  CA   A TYR   A 1 42  ? 32.356 4.639   -4.167  0.72 10.80 ?  42  TYR   A CA   1 
ATOM   1060 C  CA   B TYR   A 1 42  ? 32.145 4.638   -4.304  0.28 11.39 ?  42  TYR   A CA   1 
ATOM   1061 C  C    A TYR   A 1 42  ? 32.101 5.006   -2.716  0.72 10.61 ?  42  TYR   A C    1 
ATOM   1062 C  C    B TYR   A 1 42  ? 31.881 5.033   -2.857  0.28 11.02 ?  42  TYR   A C    1 
ATOM   1063 O  O    A TYR   A 1 42  ? 32.676 5.988   -2.224  0.72 11.36 ?  42  TYR   A O    1 
ATOM   1064 O  O    B TYR   A 1 42  ? 32.454 6.022   -2.386  0.28 11.34 ?  42  TYR   A O    1 
ATOM   1065 C  CB   A TYR   A 1 42  ? 31.992 5.821   -5.085  0.72 11.44 ?  42  TYR   A CB   1 
ATOM   1066 C  CB   B TYR   A 1 42  ? 31.879 5.843   -5.213  0.28 12.25 ?  42  TYR   A CB   1 
ATOM   1067 C  CG   A TYR   A 1 42  ? 32.182 5.503   -6.555  0.72 12.35 ?  42  TYR   A CG   1 
ATOM   1068 C  CG   B TYR   A 1 42  ? 32.080 5.554   -6.680  0.28 13.03 ?  42  TYR   A CG   1 
ATOM   1069 C  CD1  A TYR   A 1 42  ? 33.447 5.314   -7.083  0.72 13.23 ?  42  TYR   A CD1  1 
ATOM   1070 C  CD1  B TYR   A 1 42  ? 33.348 5.335   -7.198  0.28 13.52 ?  42  TYR   A CD1  1 
ATOM   1071 C  CD2  A TYR   A 1 42  ? 31.093 5.359   -7.406  0.72 14.06 ?  42  TYR   A CD2  1 
ATOM   1072 C  CD2  B TYR   A 1 42  ? 31.000 5.502   -7.548  0.28 13.68 ?  42  TYR   A CD2  1 
ATOM   1073 C  CE1  A TYR   A 1 42  ? 33.629 4.998   -8.417  0.72 14.21 ?  42  TYR   A CE1  1 
ATOM   1074 C  CE1  B TYR   A 1 42  ? 33.532 5.067   -8.542  0.28 14.20 ?  42  TYR   A CE1  1 
ATOM   1075 C  CE2  A TYR   A 1 42  ? 31.266 5.050   -8.746  0.72 15.22 ?  42  TYR   A CE2  1 
ATOM   1076 C  CE2  B TYR   A 1 42  ? 31.174 5.240   -8.888  0.28 14.45 ?  42  TYR   A CE2  1 
ATOM   1077 C  CZ   A TYR   A 1 42  ? 32.538 4.871   -9.245  0.72 15.19 ?  42  TYR   A CZ   1 
ATOM   1078 C  CZ   B TYR   A 1 42  ? 32.439 5.022   -9.382  0.28 14.85 ?  42  TYR   A CZ   1 
ATOM   1079 O  OH   A TYR   A 1 42  ? 32.716 4.553   -10.572 0.72 16.59 ?  42  TYR   A OH   1 
ATOM   1080 O  OH   B TYR   A 1 42  ? 32.605 4.760   -10.721 0.28 15.92 ?  42  TYR   A OH   1 
ATOM   1081 H  H    A TYR   A 1 42  ? 30.837 3.613   -4.874  0.72 12.73 ?  42  TYR   A H    1 
ATOM   1082 H  H    B TYR   A 1 42  ? 30.569 3.692   -5.026  0.28 13.07 ?  42  TYR   A H    1 
ATOM   1083 H  HA   A TYR   A 1 42  ? 33.306 4.481   -4.271  0.72 12.93 ?  42  TYR   A HA   1 
ATOM   1084 H  HA   B TYR   A 1 42  ? 33.083 4.418   -4.385  0.28 13.63 ?  42  TYR   A HA   1 
ATOM   1085 H  HB2  A TYR   A 1 42  ? 31.057 6.056   -4.945  0.72 13.70 ?  42  TYR   A HB2  1 
ATOM   1086 H  HB2  B TYR   A 1 42  ? 30.961 6.132   -5.091  0.28 14.67 ?  42  TYR   A HB2  1 
ATOM   1087 H  HB3  A TYR   A 1 42  ? 32.556 6.582   -4.867  0.72 13.70 ?  42  TYR   A HB3  1 
ATOM   1088 H  HB3  B TYR   A 1 42  ? 32.485 6.559   -4.968  0.28 14.67 ?  42  TYR   A HB3  1 
ATOM   1089 H  HD1  A TYR   A 1 42  ? 34.189 5.396   -6.528  0.72 15.85 ?  42  TYR   A HD1  1 
ATOM   1090 H  HD1  B TYR   A 1 42  ? 34.085 5.364   -6.630  0.28 16.20 ?  42  TYR   A HD1  1 
ATOM   1091 H  HD2  A TYR   A 1 42  ? 30.231 5.480   -7.071  0.72 16.84 ?  42  TYR   A HD2  1 
ATOM   1092 H  HD2  B TYR   A 1 42  ? 30.142 5.648   -7.217  0.28 16.38 ?  42  TYR   A HD2  1 
ATOM   1093 H  HE1  A TYR   A 1 42  ? 34.487 4.880   -8.756  0.72 17.02 ?  42  TYR   A HE1  1 
ATOM   1094 H  HE1  B TYR   A 1 42  ? 34.388 4.921   -8.875  0.28 17.01 ?  42  TYR   A HE1  1 
ATOM   1095 H  HE2  A TYR   A 1 42  ? 30.527 4.963   -9.307  0.72 18.23 ?  42  TYR   A HE2  1 
ATOM   1096 H  HE2  B TYR   A 1 42  ? 30.439 5.207   -9.456  0.28 17.31 ?  42  TYR   A HE2  1 
ATOM   1097 H  HH   A TYR   A 1 42  ? 33.538 4.472   -10.743 0.72 19.88 ?  42  TYR   A HH   1 
ATOM   1098 H  HH   B TYR   A 1 42  ? 33.420 4.641   -10.890 0.28 19.08 ?  42  TYR   A HH   1 
ATOM   1099 N  N    A LEU   A 1 43  ? 31.258 4.238   -2.027  0.72 10.19 ?  43  LEU   A N    1 
ATOM   1100 N  N    B LEU   A 1 43  ? 31.029 4.290   -2.152  0.28 10.62 ?  43  LEU   A N    1 
ATOM   1101 C  CA   A LEU   A 1 43  ? 30.800 4.582   -0.685  0.72 9.99  ?  43  LEU   A CA   1 
ATOM   1102 C  CA   B LEU   A 1 43  ? 30.644 4.604   -0.775  0.28 10.68 ?  43  LEU   A CA   1 
ATOM   1103 C  C    A LEU   A 1 43  ? 30.321 6.032   -0.611  0.72 10.26 ?  43  LEU   A C    1 
ATOM   1104 C  C    B LEU   A 1 43  ? 30.158 6.044   -0.629  0.28 10.88 ?  43  LEU   A C    1 
ATOM   1105 O  O    A LEU   A 1 43  ? 30.596 6.754   0.351   0.72 11.60 ?  43  LEU   A O    1 
ATOM   1106 O  O    B LEU   A 1 43  ? 30.410 6.711   0.377   0.28 10.99 ?  43  LEU   A O    1 
ATOM   1107 C  CB   A LEU   A 1 43  ? 31.849 4.281   0.385   0.72 10.65 ?  43  LEU   A CB   1 
ATOM   1108 C  CB   B LEU   A 1 43  ? 31.752 4.278   0.227   0.28 10.68 ?  43  LEU   A CB   1 
ATOM   1109 C  CG   A LEU   A 1 43  ? 32.358 2.836   0.487   0.72 10.75 ?  43  LEU   A CG   1 
ATOM   1110 C  CG   B LEU   A 1 43  ? 32.194 2.813   0.289   0.28 10.59 ?  43  LEU   A CG   1 
ATOM   1111 C  CD1  A LEU   A 1 43  ? 33.402 2.737   1.591   0.72 11.98 ?  43  LEU   A CD1  1 
ATOM   1112 C  CD1  B LEU   A 1 43  ? 33.219 2.629   1.393   0.28 10.82 ?  43  LEU   A CD1  1 
ATOM   1113 C  CD2  A LEU   A 1 43  ? 31.233 1.850   0.733   0.72 11.18 ?  43  LEU   A CD2  1 
ATOM   1114 C  CD2  B LEU   A 1 43  ? 31.006 1.877   0.489   0.28 10.89 ?  43  LEU   A CD2  1 
ATOM   1115 H  H    A LEU   A 1 43  ? 30.936 3.487   -2.319  0.72 12.20 ?  43  LEU   A H    1 
ATOM   1116 H  H    B LEU   A 1 43  ? 30.654 3.579   -2.454  0.28 12.72 ?  43  LEU   A H    1 
ATOM   1117 H  HA   A LEU   A 1 43  ? 30.032 4.024   -0.485  0.72 11.96 ?  43  LEU   A HA   1 
ATOM   1118 H  HA   B LEU   A 1 43  ? 29.889 4.045   -0.550  0.28 12.79 ?  43  LEU   A HA   1 
ATOM   1119 H  HB2  A LEU   A 1 43  ? 32.620 4.849   0.223   0.72 12.75 ?  43  LEU   A HB2  1 
ATOM   1120 H  HB2  B LEU   A 1 43  ? 32.533 4.807   0.005   0.28 12.79 ?  43  LEU   A HB2  1 
ATOM   1121 H  HB3  A LEU   A 1 43  ? 31.465 4.505   1.247   0.72 12.75 ?  43  LEU   A HB3  1 
ATOM   1122 H  HB3  B LEU   A 1 43  ? 31.439 4.521   1.114   0.28 12.79 ?  43  LEU   A HB3  1 
ATOM   1123 H  HG   A LEU   A 1 43  ? 32.792 2.601   -0.349  0.72 12.87 ?  43  LEU   A HG   1 
ATOM   1124 H  HG   B LEU   A 1 43  ? 32.618 2.580   -0.551  0.28 12.68 ?  43  LEU   A HG   1 
ATOM   1125 H  HD11 A LEU   A 1 43  ? 33.717 1.821   1.644   0.72 14.34 ?  43  LEU   A HD11 1 
ATOM   1126 H  HD11 B LEU   A 1 43  ? 33.491 1.699   1.418   0.28 12.95 ?  43  LEU   A HD11 1 
ATOM   1127 H  HD12 A LEU   A 1 43  ? 34.140 3.331   1.386   0.72 14.34 ?  43  LEU   A HD12 1 
ATOM   1128 H  HD12 B LEU   A 1 43  ? 33.985 3.195   1.211   0.28 12.95 ?  43  LEU   A HD12 1 
ATOM   1129 H  HD13 A LEU   A 1 43  ? 32.993 2.995   2.433   0.72 14.34 ?  43  LEU   A HD13 1 
ATOM   1130 H  HD13 B LEU   A 1 43  ? 32.817 2.879   2.241   0.28 12.95 ?  43  LEU   A HD13 1 
ATOM   1131 H  HD21 A LEU   A 1 43  ? 31.617 0.968   0.864   0.72 13.39 ?  43  LEU   A HD21 1 
ATOM   1132 H  HD21 B LEU   A 1 43  ? 31.338 0.989   0.693   0.28 13.03 ?  43  LEU   A HD21 1 
ATOM   1133 H  HD22 A LEU   A 1 43  ? 30.745 2.122   1.522   0.72 13.39 ?  43  LEU   A HD22 1 
ATOM   1134 H  HD22 B LEU   A 1 43  ? 30.465 2.206   1.222   0.28 13.03 ?  43  LEU   A HD22 1 
ATOM   1135 H  HD23 A LEU   A 1 43  ? 30.648 1.846   -0.040  0.72 13.39 ?  43  LEU   A HD23 1 
ATOM   1136 H  HD23 B LEU   A 1 43  ? 30.481 1.855   -0.327  0.28 13.03 ?  43  LEU   A HD23 1 
ATOM   1137 N  N    A LYS   A 1 44  ? 29.596 6.462   -1.646  0.72 10.27 ?  44  LYS   A N    1 
ATOM   1138 N  N    B LYS   A 1 44  ? 29.433 6.521   -1.639  0.28 11.30 ?  44  LYS   A N    1 
ATOM   1139 C  CA   A LYS   A 1 44  ? 28.949 7.770   -1.654  0.72 10.39 ?  44  LYS   A CA   1 
ATOM   1140 C  CA   B LYS   A 1 44  ? 28.783 7.828   -1.584  0.28 11.98 ?  44  LYS   A CA   1 
ATOM   1141 C  C    A LYS   A 1 44  ? 27.521 7.583   -1.154  0.72 10.03 ?  44  LYS   A C    1 
ATOM   1142 C  C    B LYS   A 1 44  ? 27.367 7.619   -1.065  0.28 11.18 ?  44  LYS   A C    1 
ATOM   1143 O  O    A LYS   A 1 44  ? 26.665 7.053   -1.870  0.72 11.15 ?  44  LYS   A O    1 
ATOM   1144 O  O    B LYS   A 1 44  ? 26.480 7.170   -1.795  0.28 11.20 ?  44  LYS   A O    1 
ATOM   1145 C  CB   A LYS   A 1 44  ? 28.989 8.388   -3.047  0.72 12.79 ?  44  LYS   A CB   1 
ATOM   1146 C  CB   B LYS   A 1 44  ? 28.812 8.501   -2.954  0.28 13.82 ?  44  LYS   A CB   1 
ATOM   1147 C  CG   A LYS   A 1 44  ? 30.367 8.871   -3.467  0.72 16.44 ?  44  LYS   A CG   1 
ATOM   1148 C  CG   B LYS   A 1 44  ? 30.205 8.934   -3.407  0.28 15.81 ?  44  LYS   A CG   1 
ATOM   1149 C  CD   A LYS   A 1 44  ? 30.991 9.826   -2.447  0.72 21.27 ?  44  LYS   A CD   1 
ATOM   1150 C  CD   B LYS   A 1 44  ? 30.982 9.595   -2.266  0.28 18.61 ?  44  LYS   A CD   1 
ATOM   1151 C  CE   A LYS   A 1 44  ? 32.346 10.323  -2.909  0.72 23.73 ?  44  LYS   A CE   1 
ATOM   1152 C  CE   B LYS   A 1 44  ? 31.642 10.886  -2.691  0.28 19.86 ?  44  LYS   A CE   1 
ATOM   1153 N  NZ   A LYS   A 1 44  ? 33.171 10.815  -1.775  0.72 24.84 ?  44  LYS   A NZ   1 
ATOM   1154 N  NZ   B LYS   A 1 44  ? 32.220 11.605  -1.520  0.28 20.57 ?  44  LYS   A NZ   1 
ATOM   1155 H  H    A LYS   A 1 44  ? 29.467 6.003   -2.367  0.72 12.29 ?  44  LYS   A H    1 
ATOM   1156 H  H    B LYS   A 1 44  ? 29.301 6.106   -2.380  0.28 13.54 ?  44  LYS   A H    1 
ATOM   1157 H  HA   A LYS   A 1 44  ? 29.400 8.351   -1.027  0.72 12.43 ?  44  LYS   A HA   1 
ATOM   1158 H  HA   B LYS   A 1 44  ? 29.235 8.381   -0.928  0.28 14.35 ?  44  LYS   A HA   1 
ATOM   1159 H  HB2  A LYS   A 1 44  ? 28.699 7.730   -3.695  0.72 15.32 ?  44  LYS   A HB2  1 
ATOM   1160 H  HB2  B LYS   A 1 44  ? 28.470 7.880   -3.619  0.28 16.56 ?  44  LYS   A HB2  1 
ATOM   1161 H  HB3  A LYS   A 1 44  ? 28.393 9.154   -3.065  0.72 15.32 ?  44  LYS   A HB3  1 
ATOM   1162 H  HB3  B LYS   A 1 44  ? 28.255 9.296   -2.935  0.28 16.56 ?  44  LYS   A HB3  1 
ATOM   1163 H  HG2  A LYS   A 1 44  ? 30.959 8.109   -3.568  0.72 19.70 ?  44  LYS   A HG2  1 
ATOM   1164 H  HG2  B LYS   A 1 44  ? 30.702 8.156   -3.711  0.28 18.94 ?  44  LYS   A HG2  1 
ATOM   1165 H  HG3  A LYS   A 1 44  ? 30.296 9.349   -4.313  0.72 19.70 ?  44  LYS   A HG3  1 
ATOM   1166 H  HG3  B LYS   A 1 44  ? 30.127 9.580   -4.131  0.28 18.94 ?  44  LYS   A HG3  1 
ATOM   1167 H  HD2  A LYS   A 1 44  ? 30.401 10.582  -2.317  0.72 25.49 ?  44  LYS   A HD2  1 
ATOM   1168 H  HD2  B LYS   A 1 44  ? 30.376 9.834   -1.551  0.28 22.30 ?  44  LYS   A HD2  1 
ATOM   1169 H  HD3  A LYS   A 1 44  ? 31.124 9.352   -1.608  0.72 25.49 ?  44  LYS   A HD3  1 
ATOM   1170 H  HD3  B LYS   A 1 44  ? 31.658 8.973   -1.942  0.28 22.30 ?  44  LYS   A HD3  1 
ATOM   1171 H  HE2  A LYS   A 1 44  ? 32.824 9.595   -3.337  0.72 28.44 ?  44  LYS   A HE2  1 
ATOM   1172 H  HE2  B LYS   A 1 44  ? 32.353 10.689  -3.314  0.28 23.80 ?  44  LYS   A HE2  1 
ATOM   1173 H  HE3  A LYS   A 1 44  ? 32.219 11.053  -3.532  0.72 28.44 ?  44  LYS   A HE3  1 
ATOM   1174 H  HE3  B LYS   A 1 44  ? 30.976 11.460  -3.103  0.28 23.80 ?  44  LYS   A HE3  1 
ATOM   1175 H  HZ1  A LYS   A 1 44  ? 33.958 11.102  -2.074  0.72 29.78 ?  44  LYS   A HZ1  1 
ATOM   1176 H  HZ1  B LYS   A 1 44  ? 32.600 12.361  -1.788  0.28 24.66 ?  44  LYS   A HZ1  1 
ATOM   1177 H  HZ2  A LYS   A 1 44  ? 32.755 11.487  -1.365  0.72 29.78 ?  44  LYS   A HZ2  1 
ATOM   1178 H  HZ2  B LYS   A 1 44  ? 31.578 11.796  -0.932  0.28 24.66 ?  44  LYS   A HZ2  1 
ATOM   1179 H  HZ3  A LYS   A 1 44  ? 33.306 10.159  -1.188  0.72 29.78 ?  44  LYS   A HZ3  1 
ATOM   1180 H  HZ3  B LYS   A 1 44  ? 32.831 11.095  -1.122  0.28 24.66 ?  44  LYS   A HZ3  1 
ATOM   1181 N  N    A HIS   A 1 45  ? 27.271 8.004   0.084   0.72 9.72  ?  45  HIS   A N    1 
ATOM   1182 N  N    B HIS   A 1 45  ? 27.157 7.942   0.210   0.28 11.10 ?  45  HIS   A N    1 
ATOM   1183 C  CA   A HIS   A 1 45  ? 26.043 7.641   0.790   0.72 10.11 ?  45  HIS   A CA   1 
ATOM   1184 C  CA   B HIS   A 1 45  ? 25.895 7.645   0.887   0.28 11.26 ?  45  HIS   A CA   1 
ATOM   1185 C  C    A HIS   A 1 45  ? 24.997 8.737   0.610   0.72 10.76 ?  45  HIS   A C    1 
ATOM   1186 C  C    B HIS   A 1 45  ? 24.942 8.832   0.751   0.28 11.60 ?  45  HIS   A C    1 
ATOM   1187 O  O    A HIS   A 1 45  ? 24.704 9.512   1.518   0.72 12.65 ?  45  HIS   A O    1 
ATOM   1188 O  O    B HIS   A 1 45  ? 24.667 9.570   1.697   0.28 12.52 ?  45  HIS   A O    1 
ATOM   1189 C  CB   A HIS   A 1 45  ? 26.348 7.405   2.258   0.72 9.69  ?  45  HIS   A CB   1 
ATOM   1190 C  CB   B HIS   A 1 45  ? 26.150 7.310   2.347   0.28 11.15 ?  45  HIS   A CB   1 
ATOM   1191 C  CG   A HIS   A 1 45  ? 27.450 6.423   2.493   0.72 9.70  ?  45  HIS   A CG   1 
ATOM   1192 C  CG   B HIS   A 1 45  ? 27.331 6.420   2.564   0.28 10.64 ?  45  HIS   A CG   1 
ATOM   1193 N  ND1  A HIS   A 1 45  ? 27.425 5.134   1.996   0.72 10.37 ?  45  HIS   A ND1  1 
ATOM   1194 N  ND1  B HIS   A 1 45  ? 27.404 5.140   2.058   0.28 10.92 ?  45  HIS   A ND1  1 
ATOM   1195 C  CD2  A HIS   A 1 45  ? 28.622 6.556   3.162   0.72 9.94  ?  45  HIS   A CD2  1 
ATOM   1196 C  CD2  B HIS   A 1 45  ? 28.488 6.631   3.235   0.28 10.40 ?  45  HIS   A CD2  1 
ATOM   1197 C  CE1  A HIS   A 1 45  ? 28.536 4.517   2.366   0.72 10.11 ?  45  HIS   A CE1  1 
ATOM   1198 C  CE1  B HIS   A 1 45  ? 28.558 4.601   2.411   0.28 10.40 ?  45  HIS   A CE1  1 
ATOM   1199 N  NE2  A HIS   A 1 45  ? 29.277 5.353   3.075   0.72 10.19 ?  45  HIS   A NE2  1 
ATOM   1200 N  NE2  B HIS   A 1 45  ? 29.233 5.483   3.127   0.28 10.35 ?  45  HIS   A NE2  1 
ATOM   1201 H  H    A HIS   A 1 45  ? 27.803 8.508   0.539   0.72 11.63 ?  45  HIS   A H    1 
ATOM   1202 H  H    B HIS   A 1 45  ? 27.740 8.337   0.708   0.28 13.29 ?  45  HIS   A H    1 
ATOM   1203 H  HA   A HIS   A 1 45  ? 25.692 6.821   0.417   0.72 12.10 ?  45  HIS   A HA   1 
ATOM   1204 H  HA   B HIS   A 1 45  ? 25.487 6.874   0.462   0.28 13.48 ?  45  HIS   A HA   1 
ATOM   1205 H  HB2  A HIS   A 1 45  ? 26.607 8.249   2.665   0.72 11.60 ?  45  HIS   A HB2  1 
ATOM   1206 H  HB2  B HIS   A 1 45  ? 26.306 8.135   2.832   0.28 13.35 ?  45  HIS   A HB2  1 
ATOM   1207 H  HB3  A HIS   A 1 45  ? 25.550 7.065   2.692   0.72 11.60 ?  45  HIS   A HB3  1 
ATOM   1208 H  HB3  B HIS   A 1 45  ? 25.371 6.860   2.701   0.28 13.35 ?  45  HIS   A HB3  1 
ATOM   1209 H  HD2  A HIS   A 1 45  ? 28.926 7.320   3.606   0.72 11.90 ?  45  HIS   A HD2  1 
ATOM   1210 H  HD2  B HIS   A 1 45  ? 28.732 7.409   3.687   0.28 12.45 ?  45  HIS   A HD2  1 
ATOM   1211 H  HE1  A HIS   A 1 45  ? 28.758 3.636   2.172   0.72 12.11 ?  45  HIS   A HE1  1 
ATOM   1212 H  HE1  B HIS   A 1 45  ? 28.843 3.744   2.197   0.28 12.45 ?  45  HIS   A HE1  1 
ATOM   1213 H  HE2  A HIS   A 1 45  ? 30.046 5.176   3.423   0.72 12.19 ?  45  HIS   A HE2  1 
ATOM   1214 H  HE2  B HIS   A 1 45  ? 30.011 5.360   3.469   0.28 12.39 ?  45  HIS   A HE2  1 
ATOM   1215 N  N    A GLY   A 1 46  ? 24.404 8.778   -0.579  0.72 11.77 ?  46  GLY   A N    1 
ATOM   1216 N  N    B GLY   A 1 46  ? 24.421 8.995   -0.459  0.28 11.93 ?  46  GLY   A N    1 
ATOM   1217 C  CA   A GLY   A 1 46  ? 23.573 9.908   -0.948  0.72 12.60 ?  46  GLY   A CA   1 
ATOM   1218 C  CA   B GLY   A 1 46  ? 23.591 10.144  -0.758  0.28 11.88 ?  46  GLY   A CA   1 
ATOM   1219 C  C    A GLY   A 1 46  ? 22.090 9.776   -0.673  0.72 12.74 ?  46  GLY   A C    1 
ATOM   1220 C  C    B GLY   A 1 46  ? 22.121 9.985   -0.416  0.28 11.26 ?  46  GLY   A C    1 
ATOM   1221 O  O    A GLY   A 1 46  ? 21.431 10.765  -0.330  0.72 14.03 ?  46  GLY   A O    1 
ATOM   1222 O  O    B GLY   A 1 46  ? 21.471 10.957  -0.016  0.28 11.73 ?  46  GLY   A O    1 
ATOM   1223 H  H    A GLY   A 1 46  ? 24.452 8.164   -1.179  0.72 14.09 ?  46  GLY   A H    1 
ATOM   1224 H  H    B GLY   A 1 46  ? 24.538 8.456   -1.118  0.28 14.28 ?  46  GLY   A H    1 
ATOM   1225 H  HA2  A GLY   A 1 46  ? 23.880 10.695  -0.471  0.72 15.09 ?  46  GLY   A HA2  1 
ATOM   1226 H  HA2  B GLY   A 1 46  ? 23.934 10.911  -0.267  0.28 14.22 ?  46  GLY   A HA2  1 
ATOM   1227 H  HA3  A GLY   A 1 46  ? 23.669 10.076  -1.895  0.72 15.09 ?  46  GLY   A HA3  1 
ATOM   1228 H  HA3  B GLY   A 1 46  ? 23.662 10.340  -1.704  0.28 14.22 ?  46  GLY   A HA3  1 
ATOM   1229 N  N    A GLY   A 1 47  ? 21.546 8.574   -0.845  0.72 12.25 ?  47  GLY   A N    1 
ATOM   1230 N  N    B GLY   A 1 47  ? 21.576 8.781   -0.576  0.28 11.28 ?  47  GLY   A N    1 
ATOM   1231 C  CA   A GLY   A 1 47  ? 20.116 8.367   -0.767  0.72 12.46 ?  47  GLY   A CA   1 
ATOM   1232 C  CA   B GLY   A 1 47  ? 20.154 8.576   -0.370  0.28 11.52 ?  47  GLY   A CA   1 
ATOM   1233 C  C    A GLY   A 1 47  ? 19.794 6.945   -0.361  0.72 12.28 ?  47  GLY   A C    1 
ATOM   1234 C  C    B GLY   A 1 47  ? 19.840 7.124   -0.070  0.28 11.27 ?  47  GLY   A C    1 
ATOM   1235 O  O    A GLY   A 1 47  ? 20.684 6.125   -0.125  0.72 12.42 ?  47  GLY   A O    1 
ATOM   1236 O  O    B GLY   A 1 47  ? 20.734 6.284   0.060   0.28 11.24 ?  47  GLY   A O    1 
ATOM   1237 H  H    A GLY   A 1 47  ? 21.992 7.853   -0.999  0.72 14.67 ?  47  GLY   A H    1 
ATOM   1238 H  H    B GLY   A 1 47  ? 22.010 8.072   -0.800  0.28 13.51 ?  47  GLY   A H    1 
ATOM   1239 H  HA2  A GLY   A 1 47  ? 19.724 8.971   -0.117  0.72 14.92 ?  47  GLY   A HA2  1 
ATOM   1240 H  HA2  B GLY   A 1 47  ? 19.848 9.125   0.369   0.28 13.80 ?  47  GLY   A HA2  1 
ATOM   1241 H  HA3  A GLY   A 1 47  ? 19.711 8.536   -1.633  0.72 14.92 ?  47  GLY   A HA3  1 
ATOM   1242 H  HA3  B GLY   A 1 47  ? 19.671 8.836   -1.170  0.28 13.80 ?  47  GLY   A HA3  1 
ATOM   1243 N  N    A GLY   A 1 48  ? 18.498 6.649   -0.304  0.72 12.18 ?  48  GLY   A N    1 
ATOM   1244 N  N    B GLY   A 1 48  ? 18.542 6.836   0.043   0.28 12.14 ?  48  GLY   A N    1 
ATOM   1245 C  CA   A GLY   A 1 48  ? 18.070 5.347   0.148   0.72 12.22 ?  48  GLY   A CA   1 
ATOM   1246 C  CA   B GLY   A 1 48  ? 18.116 5.473   0.328   0.28 11.94 ?  48  GLY   A CA   1 
ATOM   1247 C  C    A GLY   A 1 48  ? 18.571 5.070   1.549   0.72 11.35 ?  48  GLY   A C    1 
ATOM   1248 C  C    B GLY   A 1 48  ? 18.579 5.029   1.703   0.28 11.52 ?  48  GLY   A C    1 
ATOM   1249 O  O    A GLY   A 1 48  ? 18.765 5.982   2.365   0.72 11.54 ?  48  GLY   A O    1 
ATOM   1250 O  O    B GLY   A 1 48  ? 18.632 5.819   2.654   0.28 11.68 ?  48  GLY   A O    1 
ATOM   1251 H  H    A GLY   A 1 48  ? 17.854 7.185   -0.502  0.72 14.59 ?  48  GLY   A H    1 
ATOM   1252 H  H    B GLY   A 1 48  ? 17.896 7.403   -0.033  0.28 14.53 ?  48  GLY   A H    1 
ATOM   1253 H  HA2  A GLY   A 1 48  ? 17.101 5.293   0.151   0.72 14.64 ?  48  GLY   A HA2  1 
ATOM   1254 H  HA2  B GLY   A 1 48  ? 17.147 5.412   0.286   0.28 14.30 ?  48  GLY   A HA2  1 
ATOM   1255 H  HA3  A GLY   A 1 48  ? 18.421 4.662   -0.439  0.72 14.64 ?  48  GLY   A HA3  1 
ATOM   1256 H  HA3  B GLY   A 1 48  ? 18.491 4.868   -0.333  0.28 14.30 ?  48  GLY   A HA3  1 
ATOM   1257 N  N    A VAL   A 1 49  ? 18.787 3.783   1.830   0.72 10.98 ?  49  VAL   A N    1 
ATOM   1258 N  N    B VAL   A 1 49  ? 18.918 3.742   1.813   0.28 10.98 ?  49  VAL   A N    1 
ATOM   1259 C  CA   A VAL   A 1 49  ? 19.302 3.364   3.131   0.72 11.26 ?  49  VAL   A CA   1 
ATOM   1260 C  CA   B VAL   A 1 49  ? 19.465 3.219   3.062   0.28 10.46 ?  49  VAL   A CA   1 
ATOM   1261 C  C    A VAL   A 1 49  ? 20.612 4.077   3.455   0.72 9.99  ?  49  VAL   A C    1 
ATOM   1262 C  C    B VAL   A 1 49  ? 20.759 3.937   3.418   0.28 9.62  ?  49  VAL   A C    1 
ATOM   1263 O  O    A VAL   A 1 49  ? 20.816 4.535   4.583   0.72 10.54 ?  49  VAL   A O    1 
ATOM   1264 O  O    B VAL   A 1 49  ? 20.990 4.294   4.578   0.28 9.27  ?  49  VAL   A O    1 
ATOM   1265 C  CB   A VAL   A 1 49  ? 19.460 1.830   3.168   0.72 12.21 ?  49  VAL   A CB   1 
ATOM   1266 C  CB   B VAL   A 1 49  ? 19.682 1.697   2.953   0.28 9.99  ?  49  VAL   A CB   1 
ATOM   1267 C  CG1  A VAL   A 1 49  ? 20.278 1.399   4.375   0.72 12.23 ?  49  VAL   A CG1  1 
ATOM   1268 C  CG1  B VAL   A 1 49  ? 20.549 1.193   4.106   0.28 9.51  ?  49  VAL   A CG1  1 
ATOM   1269 C  CG2  A VAL   A 1 49  ? 18.094 1.156   3.183   0.72 14.03 ?  49  VAL   A CG2  1 
ATOM   1270 C  CG2  B VAL   A 1 49  ? 18.351 0.962   2.914   0.28 10.18 ?  49  VAL   A CG2  1 
ATOM   1271 H  H    A VAL   A 1 49  ? 18.642 3.132   1.287   0.72 13.14 ?  49  VAL   A H    1 
ATOM   1272 H  H    B VAL   A 1 49  ? 18.851 3.161   1.183   0.28 13.14 ?  49  VAL   A H    1 
ATOM   1273 H  HA   A VAL   A 1 49  ? 18.664 3.605   3.817   0.72 13.48 ?  49  VAL   A HA   1 
ATOM   1274 H  HA   B VAL   A 1 49  ? 18.830 3.378   3.776   0.28 12.52 ?  49  VAL   A HA   1 
ATOM   1275 H  HB   A VAL   A 1 49  ? 19.931 1.537   2.370   0.72 14.62 ?  49  VAL   A HB   1 
ATOM   1276 H  HB   B VAL   A 1 49  ? 20.153 1.509   2.128   0.28 11.96 ?  49  VAL   A HB   1 
ATOM   1277 H  HG11 A VAL   A 1 49  ? 20.130 0.454   4.537   0.72 14.64 ?  49  VAL   A HG11 1 
ATOM   1278 H  HG11 B VAL   A 1 49  ? 20.435 0.234   4.188   0.28 11.38 ?  49  VAL   A HG11 1 
ATOM   1279 H  HG12 A VAL   A 1 49  ? 21.219 1.559   4.200   0.72 14.64 ?  49  VAL   A HG12 1 
ATOM   1280 H  HG12 B VAL   A 1 49  ? 21.481 1.397   3.920   0.28 11.38 ?  49  VAL   A HG12 1 
ATOM   1281 H  HG13 A VAL   A 1 49  ? 19.993 1.912   5.149   0.72 14.64 ?  49  VAL   A HG13 1 
ATOM   1282 H  HG13 B VAL   A 1 49  ? 20.272 1.630   4.927   0.28 11.38 ?  49  VAL   A HG13 1 
ATOM   1283 H  HG21 A VAL   A 1 49  ? 18.217 0.194   3.198   0.72 16.80 ?  49  VAL   A HG21 1 
ATOM   1284 H  HG21 B VAL   A 1 49  ? 18.519 0.010   2.833   0.28 12.18 ?  49  VAL   A HG21 1 
ATOM   1285 H  HG22 A VAL   A 1 49  ? 17.614 1.440   3.976   0.72 16.80 ?  49  VAL   A HG22 1 
ATOM   1286 H  HG22 B VAL   A 1 49  ? 17.866 1.143   3.735   0.28 12.18 ?  49  VAL   A HG22 1 
ATOM   1287 H  HG23 A VAL   A 1 49  ? 17.607 1.417   2.388   0.72 16.80 ?  49  VAL   A HG23 1 
ATOM   1288 H  HG23 B VAL   A 1 49  ? 17.841 1.275   2.152   0.28 12.18 ?  49  VAL   A HG23 1 
ATOM   1289 N  N    A ALA   A 1 50  ? 21.529 4.147   2.484   0.72 9.84  ?  50  ALA   A N    1 
ATOM   1290 N  N    B ALA   A 1 50  ? 21.633 4.130   2.429   0.28 9.44  ?  50  ALA   A N    1 
ATOM   1291 C  CA   A ALA   A 1 50  ? 22.854 4.705   2.760   0.72 9.98  ?  50  ALA   A CA   1 
ATOM   1292 C  CA   B ALA   A 1 50  ? 22.938 4.727   2.687   0.28 9.59  ?  50  ALA   A CA   1 
ATOM   1293 C  C    A ALA   A 1 50  ? 22.764 6.167   3.175   0.72 9.53  ?  50  ALA   A C    1 
ATOM   1294 C  C    B ALA   A 1 50  ? 22.804 6.174   3.140   0.28 9.54  ?  50  ALA   A C    1 
ATOM   1295 O  O    A ALA   A 1 50  ? 23.397 6.592   4.150   0.72 10.20 ?  50  ALA   A O    1 
ATOM   1296 O  O    B ALA   A 1 50  ? 23.440 6.593   4.116   0.28 9.65  ?  50  ALA   A O    1 
ATOM   1297 C  CB   A ALA   A 1 50  ? 23.749 4.554   1.531   0.72 9.89  ?  50  ALA   A CB   1 
ATOM   1298 C  CB   B ALA   A 1 50  ? 23.801 4.631   1.428   0.28 9.68  ?  50  ALA   A CB   1 
ATOM   1299 H  H    A ALA   A 1 50  ? 21.415 3.886   1.670   0.72 11.77 ?  50  ALA   A H    1 
ATOM   1300 H  H    B ALA   A 1 50  ? 21.489 3.922   1.610   0.28 11.30 ?  50  ALA   A H    1 
ATOM   1301 H  HA   A ALA   A 1 50  ? 23.260 4.215   3.490   0.72 11.95 ?  50  ALA   A HA   1 
ATOM   1302 H  HA   B ALA   A 1 50  ? 23.380 4.238   3.394   0.28 11.48 ?  50  ALA   A HA   1 
ATOM   1303 H  HB1  A ALA   A 1 50  ? 24.622 4.931   1.730   0.72 11.84 ?  50  ALA   A HB1  1 
ATOM   1304 H  HB1  B ALA   A 1 50  ? 24.676 5.002   1.615   0.28 11.59 ?  50  ALA   A HB1  1 
ATOM   1305 H  HB2  A ALA   A 1 50  ? 23.835 3.615   1.314   0.72 11.84 ?  50  ALA   A HB2  1 
ATOM   1306 H  HB2  B ALA   A 1 50  ? 23.884 3.698   1.174   0.28 11.59 ?  50  ALA   A HB2  1 
ATOM   1307 H  HB3  A ALA   A 1 50  ? 23.347 5.033   0.788   0.72 11.84 ?  50  ALA   A HB3  1 
ATOM   1308 H  HB3  B ALA   A 1 50  ? 23.373 5.130   0.713   0.28 11.59 ?  50  ALA   A HB3  1 
ATOM   1309 N  N    . GLY   A 1 51  ? 21.985 6.957   2.439   1.00 10.08 ?  51  GLY   A N    1 
ATOM   1310 C  CA   . GLY   A 1 51  ? 21.818 8.350   2.815   1.00 10.67 ?  51  GLY   A CA   1 
ATOM   1311 C  C    . GLY   A 1 51  ? 21.221 8.489   4.199   1.00 10.41 ?  51  GLY   A C    1 
ATOM   1312 O  O    . GLY   A 1 51  ? 21.615 9.371   4.966   1.00 11.17 ?  51  GLY   A O    1 
ATOM   1313 H  H    A GLY   A 1 51  ? 21.558 6.714   1.729   0.72 12.06 ?  51  GLY   A H    1 
ATOM   1314 H  H    B GLY   A 1 51  ? 21.529 6.705   1.752   0.28 12.06 ?  51  GLY   A H    1 
ATOM   1315 H  HA2  . GLY   A 1 51  ? 22.676 8.794   2.804   1.00 12.78 ?  51  GLY   A HA2  1 
ATOM   1316 H  HA3  . GLY   A 1 51  ? 21.232 8.789   2.176   1.00 12.78 ?  51  GLY   A HA3  1 
ATOM   1317 N  N    . ALA   A 1 52  ? 20.258 7.621   4.535   1.00 10.48 ?  52  ALA   A N    1 
ATOM   1318 C  CA   . ALA   A 1 52  ? 19.618 7.677   5.845   1.00 11.17 ?  52  ALA   A CA   1 
ATOM   1319 C  C    . ALA   A 1 52  ? 20.580 7.272   6.961   1.00 10.60 ?  52  ALA   A C    1 
ATOM   1320 O  O    . ALA   A 1 52  ? 20.655 7.937   7.999   1.00 11.53 ?  52  ALA   A O    1 
ATOM   1321 C  CB   . ALA   A 1 52  ? 18.365 6.797   5.850   1.00 12.88 ?  52  ALA   A CB   1 
ATOM   1322 H  H    . ALA   A 1 52  ? 19.970 6.981   4.024   1.00 12.55 ?  52  ALA   A H    1 
ATOM   1323 H  HA   . ALA   A 1 52  ? 19.338 8.584   6.011   1.00 13.38 ?  52  ALA   A HA   1 
ATOM   1324 H  HB1  . ALA   A 1 52  ? 17.941 6.856   6.722   1.00 15.43 ?  52  ALA   A HB1  1 
ATOM   1325 H  HB2  . ALA   A 1 52  ? 17.751 7.118   5.167   1.00 15.43 ?  52  ALA   A HB2  1 
ATOM   1326 H  HB3  . ALA   A 1 52  ? 18.614 5.880   5.664   1.00 15.43 ?  52  ALA   A HB3  1 
ATOM   1327 N  N    A LEU   A 1 53  ? 21.313 6.174   6.781   0.72 10.33 ?  53  LEU   A N    1 
ATOM   1328 N  N    B LEU   A 1 53  ? 21.318 6.173   6.764   0.28 10.34 ?  53  LEU   A N    1 
ATOM   1329 C  CA   A LEU   A 1 53  ? 22.282 5.784   7.803   0.72 10.98 ?  53  LEU   A CA   1 
ATOM   1330 C  CA   B LEU   A 1 53  ? 22.292 5.742   7.765   0.28 10.42 ?  53  LEU   A CA   1 
ATOM   1331 C  C    A LEU   A 1 53  ? 23.321 6.877   7.990   0.72 10.20 ?  53  LEU   A C    1 
ATOM   1332 C  C    B LEU   A 1 53  ? 23.363 6.804   7.975   0.28 10.03 ?  53  LEU   A C    1 
ATOM   1333 O  O    A LEU   A 1 53  ? 23.631 7.269   9.119   0.72 11.25 ?  53  LEU   A O    1 
ATOM   1334 O  O    B LEU   A 1 53  ? 23.751 7.090   9.113   0.28 10.29 ?  53  LEU   A O    1 
ATOM   1335 C  CB   A LEU   A 1 53  ? 22.962 4.461   7.439   0.72 11.31 ?  53  LEU   A CB   1 
ATOM   1336 C  CB   B LEU   A 1 53  ? 22.947 4.423   7.340   0.28 10.28 ?  53  LEU   A CB   1 
ATOM   1337 C  CG   A LEU   A 1 53  ? 22.076 3.209   7.455   0.72 12.20 ?  53  LEU   A CG   1 
ATOM   1338 C  CG   B LEU   A 1 53  ? 22.214 3.088   7.513   0.28 9.75  ?  53  LEU   A CG   1 
ATOM   1339 C  CD1  A LEU   A 1 53  ? 22.843 2.015   6.930   0.72 12.71 ?  53  LEU   A CD1  1 
ATOM   1340 C  CD1  B LEU   A 1 53  ? 22.971 1.996   6.769   0.28 10.36 ?  53  LEU   A CD1  1 
ATOM   1341 C  CD2  A LEU   A 1 53  ? 21.535 2.925   8.845   0.72 12.84 ?  53  LEU   A CD2  1 
ATOM   1342 C  CD2  B LEU   A 1 53  ? 22.057 2.711   8.978   0.28 9.32  ?  53  LEU   A CD2  1 
ATOM   1343 H  H    A LEU   A 1 53  ? 21.266 5.647   6.099   0.72 12.37 ?  53  LEU   A H    1 
ATOM   1344 H  H    B LEU   A 1 53  ? 21.275 5.668   6.067   0.28 12.37 ?  53  LEU   A H    1 
ATOM   1345 H  HA   A LEU   A 1 53  ? 21.821 5.662   8.644   0.72 13.14 ?  53  LEU   A HA   1 
ATOM   1346 H  HA   B LEU   A 1 53  ? 21.840 5.595   8.610   0.28 12.48 ?  53  LEU   A HA   1 
ATOM   1347 H  HB2  A LEU   A 1 53  ? 23.330 4.540   6.543   0.72 13.55 ?  53  LEU   A HB2  1 
ATOM   1348 H  HB2  B LEU   A 1 53  ? 23.154 4.494   6.396   0.28 12.30 ?  53  LEU   A HB2  1 
ATOM   1349 H  HB3  A LEU   A 1 53  ? 23.685 4.304   8.067   0.72 13.55 ?  53  LEU   A HB3  1 
ATOM   1350 H  HB3  B LEU   A 1 53  ? 23.775 4.337   7.834   0.28 12.30 ?  53  LEU   A HB3  1 
ATOM   1351 H  HG   A LEU   A 1 53  ? 21.322 3.355   6.861   0.72 14.61 ?  53  LEU   A HG   1 
ATOM   1352 H  HG   B LEU   A 1 53  ? 21.331 3.152   7.119   0.28 11.67 ?  53  LEU   A HG   1 
ATOM   1353 H  HD11 A LEU   A 1 53  ? 22.262 1.238   6.945   0.72 15.22 ?  53  LEU   A HD11 1 
ATOM   1354 H  HD11 B LEU   A 1 53  ? 22.512 1.150   6.892   0.28 12.41 ?  53  LEU   A HD11 1 
ATOM   1355 H  HD12 A LEU   A 1 53  ? 23.128 2.196   6.020   0.72 15.22 ?  53  LEU   A HD12 1 
ATOM   1356 H  HD12 B LEU   A 1 53  ? 23.004 2.219   5.825   0.28 12.41 ?  53  LEU   A HD12 1 
ATOM   1357 H  HD13 A LEU   A 1 53  ? 23.615 1.864   7.495   0.72 15.22 ?  53  LEU   A HD13 1 
ATOM   1358 H  HD13 B LEU   A 1 53  ? 23.872 1.937   7.125   0.28 12.41 ?  53  LEU   A HD13 1 
ATOM   1359 H  HD21 A LEU   A 1 53  ? 21.057 2.081   8.830   0.72 15.38 ?  53  LEU   A HD21 1 
ATOM   1360 H  HD21 B LEU   A 1 53  ? 21.548 1.886   9.040   0.28 11.15 ?  53  LEU   A HD21 1 
ATOM   1361 H  HD22 A LEU   A 1 53  ? 22.275 2.878   9.466   0.72 15.38 ?  53  LEU   A HD22 1 
ATOM   1362 H  HD22 B LEU   A 1 53  ? 22.936 2.587   9.368   0.28 11.15 ?  53  LEU   A HD22 1 
ATOM   1363 H  HD23 A LEU   A 1 53  ? 20.932 3.641   9.099   0.72 15.38 ?  53  LEU   A HD23 1 
ATOM   1364 H  HD23 B LEU   A 1 53  ? 21.588 3.425   9.435   0.28 11.15 ?  53  LEU   A HD23 1 
ATOM   1365 N  N    . ASN   A 1 54  ? 23.858 7.395   6.888   1.00 9.90  ?  54  ASN   A N    1 
ATOM   1366 C  CA   . ASN   A 1 54  ? 24.910 8.391   7.013   1.00 10.12 ?  54  ASN   A CA   1 
ATOM   1367 C  C    . ASN   A 1 54  ? 24.404 9.640   7.733   1.00 10.24 ?  54  ASN   A C    1 
ATOM   1368 O  O    . ASN   A 1 54  ? 25.095 10.190  8.603   1.00 10.80 ?  54  ASN   A O    1 
ATOM   1369 C  CB   . ASN   A 1 54  ? 25.481 8.740   5.651   1.00 10.18 ?  54  ASN   A CB   1 
ATOM   1370 C  CG   . ASN   A 1 54  ? 26.485 9.851   5.757   1.00 10.56 ?  54  ASN   A CG   1 
ATOM   1371 O  OD1  . ASN   A 1 54  ? 27.495 9.713   6.461   1.00 10.64 ?  54  ASN   A OD1  1 
ATOM   1372 N  ND2  . ASN   A 1 54  ? 26.219 10.968  5.096   1.00 11.32 ?  54  ASN   A ND2  1 
ATOM   1373 H  H    A ASN   A 1 54  ? 23.637 7.188   6.083   0.72 11.85 ?  54  ASN   A H    1 
ATOM   1374 H  H    B ASN   A 1 54  ? 23.594 7.242   6.084   0.28 11.85 ?  54  ASN   A H    1 
ATOM   1375 H  HA   . ASN   A 1 54  ? 25.623 8.018   7.546   1.00 12.12 ?  54  ASN   A HA   1 
ATOM   1376 H  HB2  . ASN   A 1 54  ? 25.929 7.955   5.284   1.00 12.18 ?  54  ASN   A HB2  1 
ATOM   1377 H  HB3  . ASN   A 1 54  ? 24.767 9.021   5.061   1.00 12.18 ?  54  ASN   A HB3  1 
ATOM   1378 H  HD21 . ASN   A 1 54  ? 26.761 11.631  5.141   1.00 13.55 ?  54  ASN   A HD21 1 
ATOM   1379 H  HD22 . ASN   A 1 54  ? 25.498 11.027  4.630   1.00 13.55 ?  54  ASN   A HD22 1 
ATOM   1380 N  N    . LYS   A 1 55  ? 23.195 10.097  7.389   1.00 10.71 ?  55  LYS   A N    1 
ATOM   1381 C  CA   . LYS   A 1 55  ? 22.610 11.251  8.060   1.00 11.23 ?  55  LYS   A CA   1 
ATOM   1382 C  C    . LYS   A 1 55  ? 22.515 11.018  9.561   1.00 11.15 ?  55  LYS   A C    1 
ATOM   1383 O  O    . LYS   A 1 55  ? 22.801 11.919  10.359  1.00 12.22 ?  55  LYS   A O    1 
ATOM   1384 C  CB   . LYS   A 1 55  ? 21.240 11.548  7.449   1.00 12.26 ?  55  LYS   A CB   1 
ATOM   1385 C  CG   . LYS   A 1 55  ? 20.478 12.683  8.094   1.00 13.88 ?  55  LYS   A CG   1 
ATOM   1386 C  CD   . LYS   A 1 55  ? 19.158 12.917  7.359   1.00 15.48 ?  55  LYS   A CD   1 
ATOM   1387 C  CE   . LYS   A 1 55  ? 18.316 14.001  8.015   1.00 17.51 ?  55  LYS   A CE   1 
ATOM   1388 N  NZ   . LYS   A 1 55  ? 16.973 14.137  7.375   1.00 18.36 ?  55  LYS   A NZ   1 
ATOM   1389 H  H    . LYS   A 1 55  ? 22.688 9.748   6.781   1.00 12.82 ?  55  LYS   A H    1 
ATOM   1390 H  HA   . LYS   A 1 55  ? 23.176 12.023  7.911   1.00 13.44 ?  55  LYS   A HA   1 
ATOM   1391 H  HB2  . LYS   A 1 55  ? 21.361 11.779  6.515   1.00 14.68 ?  55  LYS   A HB2  1 
ATOM   1392 H  HB3  . LYS   A 1 55  ? 20.689 10.753  7.519   1.00 14.68 ?  55  LYS   A HB3  1 
ATOM   1393 H  HG2  . LYS   A 1 55  ? 20.271 12.458  9.017   1.00 16.63 ?  55  LYS   A HG2  1 
ATOM   1394 H  HG3  . LYS   A 1 55  ? 20.999 13.497  8.050   1.00 16.63 ?  55  LYS   A HG3  1 
ATOM   1395 H  HD2  . LYS   A 1 55  ? 19.348 13.189  6.446   1.00 18.55 ?  55  LYS   A HD2  1 
ATOM   1396 H  HD3  . LYS   A 1 55  ? 18.644 12.092  7.358   1.00 18.55 ?  55  LYS   A HD3  1 
ATOM   1397 H  HE2  . LYS   A 1 55  ? 18.186 13.777  8.951   1.00 20.99 ?  55  LYS   A HE2  1 
ATOM   1398 H  HE3  . LYS   A 1 55  ? 18.778 14.850  7.937   1.00 20.99 ?  55  LYS   A HE3  1 
ATOM   1399 H  HZ1  . LYS   A 1 55  ? 16.419 14.567  7.923   1.00 22.01 ?  55  LYS   A HZ1  1 
ATOM   1400 H  HZ2  . LYS   A 1 55  ? 17.042 14.597  6.617   1.00 22.01 ?  55  LYS   A HZ2  1 
ATOM   1401 H  HZ3  . LYS   A 1 55  ? 16.636 13.332  7.198   1.00 22.01 ?  55  LYS   A HZ3  1 
ATOM   1402 N  N    . ALA   A 1 56  ? 22.128 9.807   9.966   1.00 11.80 ?  56  ALA   A N    1 
ATOM   1403 C  CA   . ALA   A 1 56  ? 22.007 9.489   11.382  1.00 12.78 ?  56  ALA   A CA   1 
ATOM   1404 C  C    . ALA   A 1 56  ? 23.349 9.513   12.106  1.00 12.44 ?  56  ALA   A C    1 
ATOM   1405 O  O    . ALA   A 1 56  ? 23.368 9.697   13.324  1.00 13.87 ?  56  ALA   A O    1 
ATOM   1406 C  CB   . ALA   A 1 56  ? 21.309 8.138   11.572  1.00 13.64 ?  56  ALA   A CB   1 
ATOM   1407 H  H    . ALA   A 1 56  ? 21.931 9.161   9.438   1.00 14.13 ?  56  ALA   A H    1 
ATOM   1408 H  HA   . ALA   A 1 56  ? 21.451 10.154  11.801  1.00 15.31 ?  56  ALA   A HA   1 
ATOM   1409 H  HB1  . ALA   A 1 56  ? 21.241 7.945   12.524  1.00 16.34 ?  56  ALA   A HB1  1 
ATOM   1410 H  HB2  . ALA   A 1 56  ? 20.421 8.184   11.185  1.00 16.34 ?  56  ALA   A HB2  1 
ATOM   1411 H  HB3  . ALA   A 1 56  ? 21.825 7.442   11.134  1.00 16.34 ?  56  ALA   A HB3  1 
ATOM   1412 N  N    . THR   A 1 57  ? 24.464 9.325   11.393  1.00 11.77 ?  57  THR   A N    1 
ATOM   1413 C  CA   . THR   A 1 57  ? 25.806 9.456   11.968  1.00 11.84 ?  57  THR   A CA   1 
ATOM   1414 C  C    . THR   A 1 57  ? 26.353 10.875  11.887  1.00 12.17 ?  57  THR   A C    1 
ATOM   1415 O  O    . THR   A 1 57  ? 27.538 11.084  12.179  1.00 12.80 ?  57  THR   A O    1 
ATOM   1416 C  CB   . THR   A 1 57  ? 26.819 8.503   11.302  1.00 11.79 ?  57  THR   A CB   1 
ATOM   1417 O  OG1  . THR   A 1 57  ? 27.200 8.997   10.004  1.00 11.43 ?  57  THR   A OG1  1 
ATOM   1418 C  CG2  . THR   A 1 57  ? 26.288 7.083   11.204  1.00 11.97 ?  57  THR   A CG2  1 
ATOM   1419 H  H    . THR   A 1 57  ? 24.472 9.091   10.565  1.00 14.09 ?  57  THR   A H    1 
ATOM   1420 H  HA   . THR   A 1 57  ? 25.762 9.206   12.910  1.00 14.17 ?  57  THR   A HA   1 
ATOM   1421 H  HB   . THR   A 1 57  ? 27.618 8.470   11.859  1.00 14.12 ?  57  THR   A HB   1 
ATOM   1422 H  HG1  . THR   A 1 57  ? 26.519 9.055   9.514   1.00 13.69 ?  57  THR   A HG1  1 
ATOM   1423 H  HG21 . THR   A 1 57  ? 26.931 6.515   10.747  1.00 14.34 ?  57  THR   A HG21 1 
ATOM   1424 H  HG22 . THR   A 1 57  ? 26.129 6.721   12.091  1.00 14.34 ?  57  THR   A HG22 1 
ATOM   1425 H  HG23 . THR   A 1 57  ? 25.456 7.069   10.708  1.00 14.34 ?  57  THR   A HG23 1 
ATOM   1426 N  N    . ASN   A 1 58  ? 25.540 11.847  11.477  1.00 12.62 ?  58  ASN   A N    1 
ATOM   1427 C  CA   . ASN   A 1 58  ? 26.006 13.227  11.374  1.00 13.39 ?  58  ASN   A CA   1 
ATOM   1428 C  C    . ASN   A 1 58  ? 27.155 13.347  10.368  1.00 12.55 ?  58  ASN   A C    1 
ATOM   1429 O  O    . ASN   A 1 58  ? 28.057 14.177  10.527  1.00 13.13 ?  58  ASN   A O    1 
ATOM   1430 C  CB   . ASN   A 1 58  ? 26.384 13.769  12.763  1.00 16.29 ?  58  ASN   A CB   1 
ATOM   1431 C  CG   . ASN   A 1 58  ? 26.766 15.231  12.753  1.00 20.71 ?  58  ASN   A CG   1 
ATOM   1432 O  OD1  . ASN   A 1 58  ? 26.131 16.039  12.088  1.00 22.45 ?  58  ASN   A OD1  1 
ATOM   1433 N  ND2  . ASN   A 1 58  ? 27.813 15.582  13.502  1.00 22.43 ?  58  ASN   A ND2  1 
ATOM   1434 H  H    . ASN   A 1 58  ? 24.718 11.724  11.239  1.00 15.11 ?  58  ASN   A H    1 
ATOM   1435 H  HA   . ASN   A 1 58  ? 25.272 13.762  11.044  1.00 16.04 ?  58  ASN   A HA   1 
ATOM   1436 H  HB2  . ASN   A 1 58  ? 25.619 13.660  13.363  1.00 19.51 ?  58  ASN   A HB2  1 
ATOM   1437 H  HB3  . ASN   A 1 58  ? 27.137 13.274  13.109  1.00 19.51 ?  58  ASN   A HB3  1 
ATOM   1438 H  HD21 . ASN   A 1 58  ? 28.060 16.408  13.535  1.00 26.89 ?  58  ASN   A HD21 1 
ATOM   1439 H  HD22 . ASN   A 1 58  ? 28.229 14.989  13.956  1.00 26.89 ?  58  ASN   A HD22 1 
ATOM   1440 N  N    . ASN   A 1 59  ? 27.128 12.525  9.316   1.00 11.60 ?  59  ASN   A N    1 
ATOM   1441 C  CA   . ASN   A 1 59  ? 28.107 12.500  8.225   1.00 11.00 ?  59  ASN   A CA   1 
ATOM   1442 C  C    . ASN   A 1 59  ? 29.423 11.812  8.613   1.00 10.96 ?  59  ASN   A C    1 
ATOM   1443 O  O    . ASN   A 1 59  ? 30.344 11.776  7.789   1.00 11.20 ?  59  ASN   A O    1 
ATOM   1444 C  CB   . ASN   A 1 59  ? 28.403 13.888  7.623   1.00 11.42 ?  59  ASN   A CB   1 
ATOM   1445 C  CG   . ASN   A 1 59  ? 28.757 13.820  6.154   1.00 11.63 ?  59  ASN   A CG   1 
ATOM   1446 O  OD1  . ASN   A 1 59  ? 28.047 13.197  5.361   1.00 11.89 ?  59  ASN   A OD1  1 
ATOM   1447 N  ND2  . ASN   A 1 59  ? 29.845 14.478  5.774   1.00 12.30 ?  59  ASN   A ND2  1 
ATOM   1448 H  H    . ASN   A 1 59  ? 26.513 11.934  9.203   1.00 13.90 ?  59  ASN   A H    1 
ATOM   1449 H  HA   . ASN   A 1 59  ? 27.730 11.974  7.511   1.00 13.17 ?  59  ASN   A HA   1 
ATOM   1450 H  HB2  . ASN   A 1 59  ? 27.619 14.451  7.710   1.00 13.67 ?  59  ASN   A HB2  1 
ATOM   1451 H  HB3  . ASN   A 1 59  ? 29.153 14.292  8.090   1.00 13.67 ?  59  ASN   A HB3  1 
ATOM   1452 H  HD21 . ASN   A 1 59  ? 30.095 14.471  4.950   1.00 14.73 ?  59  ASN   A HD21 1 
ATOM   1453 H  HD22 . ASN   A 1 59  ? 30.325 14.904  6.357   1.00 14.73 ?  59  ASN   A HD22 1 
ATOM   1454 N  N    . ALA   A 1 60  ? 29.552 11.269  9.823   1.00 11.27 ?  60  ALA   A N    1 
ATOM   1455 C  CA   . ALA   A 1 60  ? 30.791 10.588  10.180  1.00 11.16 ?  60  ALA   A CA   1 
ATOM   1456 C  C    . ALA   A 1 60  ? 31.012 9.354   9.316   1.00 11.36 ?  60  ALA   A C    1 
ATOM   1457 O  O    . ALA   A 1 60  ? 32.157 9.026   8.985   1.00 11.48 ?  60  ALA   A O    1 
ATOM   1458 C  CB   . ALA   A 1 60  ? 30.783 10.230  11.664  1.00 12.06 ?  60  ALA   A CB   1 
ATOM   1459 H  H    . ALA   A 1 60  ? 28.955 11.280  10.441  1.00 13.49 ?  60  ALA   A H    1 
ATOM   1460 H  HA   . ALA   A 1 60  ? 31.537 11.194  10.028  1.00 13.36 ?  60  ALA   A HA   1 
ATOM   1461 H  HB1  . ALA   A 1 60  ? 31.613 9.781   11.886  1.00 14.45 ?  60  ALA   A HB1  1 
ATOM   1462 H  HB2  . ALA   A 1 60  ? 30.702 11.048  12.184  1.00 14.45 ?  60  ALA   A HB2  1 
ATOM   1463 H  HB3  . ALA   A 1 60  ? 30.030 9.649   11.844  1.00 14.45 ?  60  ALA   A HB3  1 
ATOM   1464 N  N    . MET   A 1 61  ? 29.937 8.665   8.929   1.00 10.78 ?  61  MET   A N    1 
ATOM   1465 C  CA   . MET   A 1 61  ? 30.077 7.528   8.024   1.00 10.33 ?  61  MET   A CA   1 
ATOM   1466 C  C    . MET   A 1 61  ? 30.714 7.952   6.703   1.00 10.29 ?  61  MET   A C    1 
ATOM   1467 O  O    . MET   A 1 61  ? 31.598 7.264   6.180   1.00 10.85 ?  61  MET   A O    1 
ATOM   1468 C  CB   . MET   A 1 61  ? 28.712 6.874   7.809   1.00 10.51 ?  61  MET   A CB   1 
ATOM   1469 C  CG   . MET   A 1 61  ? 28.721 5.705   6.832   1.00 11.26 ?  61  MET   A CG   1 
ATOM   1470 S  SD   . MET   A 1 61  ? 27.100 4.946   6.642   1.00 12.03 ?  61  MET   A SD   1 
ATOM   1471 C  CE   . MET   A 1 61  ? 26.987 4.078   8.214   1.00 13.45 ?  61  MET   A CE   1 
ATOM   1472 H  H    . MET   A 1 61  ? 29.132 8.838   9.169   1.00 12.91 ?  61  MET   A H    1 
ATOM   1473 H  HA   . MET   A 1 61  ? 30.651 6.871   8.445   1.00 12.36 ?  61  MET   A HA   1 
ATOM   1474 H  HB2  . MET   A 1 61  ? 28.387 6.545   8.660   1.00 12.59 ?  61  MET   A HB2  1 
ATOM   1475 H  HB3  . MET   A 1 61  ? 28.097 7.543   7.463   1.00 12.59 ?  61  MET   A HB3  1 
ATOM   1476 H  HG2  . MET   A 1 61  ? 28.993 6.019   5.955   1.00 13.49 ?  61  MET   A HG2  1 
ATOM   1477 H  HG3  . MET   A 1 61  ? 29.331 5.026   7.150   1.00 13.49 ?  61  MET   A HG3  1 
ATOM   1478 H  HE1  . MET   A 1 61  ? 26.158 3.576   8.243   1.00 16.11 ?  61  MET   A HE1  1 
ATOM   1479 H  HE2  . MET   A 1 61  ? 27.743 3.476   8.300   1.00 16.11 ?  61  MET   A HE2  1 
ATOM   1480 H  HE3  . MET   A 1 61  ? 27.002 4.727   8.941   1.00 16.11 ?  61  MET   A HE3  1 
ATOM   1481 N  N    . GLN   A 1 62  ? 30.263 9.078   6.142   1.00 10.41 ?  62  GLN   A N    1 
ATOM   1482 C  CA   . GLN   A 1 62  ? 30.826 9.559   4.884   1.00 10.65 ?  62  GLN   A CA   1 
ATOM   1483 C  C    . GLN   A 1 62  ? 32.296 9.937   5.028   1.00 10.46 ?  62  GLN   A C    1 
ATOM   1484 O  O    . GLN   A 1 62  ? 33.105 9.624   4.148   1.00 11.08 ?  62  GLN   A O    1 
ATOM   1485 C  CB   . GLN   A 1 62  ? 30.020 10.740  4.355   1.00 10.66 ?  62  GLN   A CB   1 
ATOM   1486 C  CG   . GLN   A 1 62  ? 30.401 11.110  2.933   1.00 10.67 ?  62  GLN   A CG   1 
ATOM   1487 C  CD   . GLN   A 1 62  ? 30.075 9.975   1.982   1.00 11.06 ?  62  GLN   A CD   1 
ATOM   1488 O  OE1  . GLN   A 1 62  ? 28.896 9.660   1.780   1.00 11.47 ?  62  GLN   A OE1  1 
ATOM   1489 N  NE2  . GLN   A 1 62  ? 31.098 9.306   1.458   1.00 11.73 ?  62  GLN   A NE2  1 
ATOM   1490 H  H    . GLN   A 1 62  ? 29.634 9.564   6.465   1.00 12.47 ?  62  GLN   A H    1 
ATOM   1491 H  HA   . GLN   A 1 62  ? 30.773 8.841   4.233   1.00 12.75 ?  62  GLN   A HA   1 
ATOM   1492 H  HB2  . GLN   A 1 62  ? 29.077 10.517  4.368   1.00 12.77 ?  62  GLN   A HB2  1 
ATOM   1493 H  HB3  . GLN   A 1 62  ? 30.185 11.515  4.921   1.00 12.77 ?  62  GLN   A HB3  1 
ATOM   1494 H  HG2  . GLN   A 1 62  ? 29.896 11.890  2.658   1.00 12.78 ?  62  GLN   A HG2  1 
ATOM   1495 H  HG3  . GLN   A 1 62  ? 31.352 11.288  2.887   1.00 12.78 ?  62  GLN   A HG3  1 
ATOM   1496 H  HE21 . GLN   A 1 62  ? 31.905 9.543   1.639   1.00 14.05 ?  62  GLN   A HE21 1 
ATOM   1497 H  HE22 . GLN   A 1 62  ? 30.952 8.649   0.923   1.00 14.05 ?  62  GLN   A HE22 1 
ATOM   1498 N  N    . VAL   A 1 63  ? 32.661 10.610  6.123   1.00 11.28 ?  63  VAL   A N    1 
ATOM   1499 C  CA   . VAL   A 1 63  ? 34.058 11.003  6.332   1.00 11.83 ?  63  VAL   A CA   1 
ATOM   1500 C  C    . VAL   A 1 63  ? 34.953 9.767   6.391   1.00 11.37 ?  63  VAL   A C    1 
ATOM   1501 O  O    . VAL   A 1 63  ? 36.002 9.698   5.732   1.00 12.02 ?  63  VAL   A O    1 
ATOM   1502 C  CB   . VAL   A 1 63  ? 34.175 11.873  7.596   1.00 13.66 ?  63  VAL   A CB   1 
ATOM   1503 C  CG1  . VAL   A 1 63  ? 35.624 12.113  7.953   1.00 15.35 ?  63  VAL   A CG1  1 
ATOM   1504 C  CG2  . VAL   A 1 63  ? 33.439 13.203  7.393   1.00 14.23 ?  63  VAL   A CG2  1 
ATOM   1505 H  H    . VAL   A 1 63  ? 32.121 10.852  6.757   1.00 13.50 ?  63  VAL   A H    1 
ATOM   1506 H  HA   . VAL   A 1 63  ? 34.340 11.539  5.580   1.00 14.16 ?  63  VAL   A HA   1 
ATOM   1507 H  HB   . VAL   A 1 63  ? 33.758 11.411  8.342   1.00 16.36 ?  63  VAL   A HB   1 
ATOM   1508 H  HG11 . VAL   A 1 63  ? 35.673 12.848  8.582   1.00 18.39 ?  63  VAL   A HG11 1 
ATOM   1509 H  HG12 . VAL   A 1 63  ? 35.990 11.309  8.351   1.00 18.39 ?  63  VAL   A HG12 1 
ATOM   1510 H  HG13 . VAL   A 1 63  ? 36.110 12.337  7.144   1.00 18.39 ?  63  VAL   A HG13 1 
ATOM   1511 H  HG21 . VAL   A 1 63  ? 33.537 13.744  8.194   1.00 17.04 ?  63  VAL   A HG21 1 
ATOM   1512 H  HG22 . VAL   A 1 63  ? 33.826 13.665  6.634   1.00 17.04 ?  63  VAL   A HG22 1 
ATOM   1513 H  HG23 . VAL   A 1 63  ? 32.500 13.024  7.229   1.00 17.04 ?  63  VAL   A HG23 1 
ATOM   1514 N  N    . GLU   A 1 64  ? 34.534 8.760   7.161   1.00 11.25 ?  64  GLU   A N    1 
ATOM   1515 C  CA   . GLU   A 1 64  ? 35.295 7.519   7.258   1.00 11.22 ?  64  GLU   A CA   1 
ATOM   1516 C  C    . GLU   A 1 64  ? 35.384 6.829   5.903   1.00 10.92 ?  64  GLU   A C    1 
ATOM   1517 O  O    . GLU   A 1 64  ? 36.434 6.283   5.530   1.00 11.54 ?  64  GLU   A O    1 
ATOM   1518 C  CB   . GLU   A 1 64  ? 34.607 6.617   8.280   1.00 12.06 ?  64  GLU   A CB   1 
ATOM   1519 C  CG   . GLU   A 1 64  ? 35.247 5.268   8.427   1.00 12.59 ?  64  GLU   A CG   1 
ATOM   1520 C  CD   . GLU   A 1 64  ? 34.373 4.274   9.160   1.00 13.18 ?  64  GLU   A CD   1 
ATOM   1521 O  OE1  . GLU   A 1 64  ? 33.131 4.364   9.034   1.00 14.08 ?  64  GLU   A OE1  1 
ATOM   1522 O  OE2  . GLU   A 1 64  ? 34.924 3.385   9.851   1.00 13.62 -1 64  GLU   A OE2  1 
ATOM   1523 H  H    . GLU   A 1 64  ? 33.807 8.766   7.625   1.00 13.47 ?  64  GLU   A H    1 
ATOM   1524 H  HA   . GLU   A 1 64  ? 36.194 7.718   7.573   1.00 13.44 ?  64  GLU   A HA   1 
ATOM   1525 H  HB2  . GLU   A 1 64  ? 34.634 7.057   9.151   1.00 14.45 ?  64  GLU   A HB2  1 
ATOM   1526 H  HB3  . GLU   A 1 64  ? 33.685 6.492   8.010   1.00 14.45 ?  64  GLU   A HB3  1 
ATOM   1527 H  HG2  . GLU   A 1 64  ? 35.435 4.901   7.547   1.00 15.08 ?  64  GLU   A HG2  1 
ATOM   1528 H  HG3  . GLU   A 1 64  ? 36.072 5.366   8.923   1.00 15.08 ?  64  GLU   A HG3  1 
ATOM   1529 N  N    . SER   A 1 65  ? 34.265 6.820   5.171   1.00 10.79 ?  65  SER   A N    1 
ATOM   1530 C  CA   . SER   A 1 65  ? 34.209 6.166   3.869   1.00 10.73 ?  65  SER   A CA   1 
ATOM   1531 C  C    . SER   A 1 65  ? 35.132 6.835   2.862   1.00 10.70 ?  65  SER   A C    1 
ATOM   1532 O  O    . SER   A 1 65  ? 35.768 6.156   2.049   1.00 11.64 ?  65  SER   A O    1 
ATOM   1533 C  CB   . SER   A 1 65  ? 32.773 6.176   3.339   1.00 10.86 ?  65  SER   A CB   1 
ATOM   1534 O  OG   . SER   A 1 65  ? 31.921 5.363   4.135   1.00 11.24 ?  65  SER   A OG   1 
ATOM   1535 H  H    . SER   A 1 65  ? 33.531 7.193   5.410   1.00 12.92 ?  65  SER   A H    1 
ATOM   1536 H  HA   . SER   A 1 65  ? 34.492 5.245   3.963   1.00 12.85 ?  65  SER   A HA   1 
ATOM   1537 H  HB2  . SER   A 1 65  ? 32.438 7.082   3.348   1.00 13.01 ?  65  SER   A HB2  1 
ATOM   1538 H  HB3  . SER   A 1 65  ? 32.777 5.832   2.431   1.00 13.01 ?  65  SER   A HB3  1 
ATOM   1539 H  HG   . SER   A 1 65  ? 31.915 5.644   4.932   1.00 13.46 ?  65  SER   A HG   1 
ATOM   1540 N  N    . ASP   A 1 66  ? 35.207 8.170   2.884   1.00 10.78 ?  66  ASP   A N    1 
ATOM   1541 C  CA   . ASP   A 1 66  ? 36.066 8.865   1.932   1.00 11.75 ?  66  ASP   A CA   1 
ATOM   1542 C  C    . ASP   A 1 66  ? 37.529 8.510   2.165   1.00 11.93 ?  66  ASP   A C    1 
ATOM   1543 O  O    . ASP   A 1 66  ? 38.297 8.336   1.211   1.00 12.75 ?  66  ASP   A O    1 
ATOM   1544 C  CB   . ASP   A 1 66  ? 35.854 10.373  2.039   1.00 13.20 ?  66  ASP   A CB   1 
ATOM   1545 C  CG   . ASP   A 1 66  ? 34.512 10.835  1.459   1.00 15.00 ?  66  ASP   A CG   1 
ATOM   1546 O  OD1  . ASP   A 1 66  ? 33.795 10.050  0.804   1.00 15.08 ?  66  ASP   A OD1  1 
ATOM   1547 O  OD2  . ASP   A 1 66  ? 34.198 12.029  1.632   1.00 17.94 -1 66  ASP   A OD2  1 
ATOM   1548 H  H    . ASP   A 1 66  ? 34.772 8.686   3.423   1.00 12.91 ?  66  ASP   A H    1 
ATOM   1549 H  HA   . ASP   A 1 66  ? 35.828 8.593   1.034   1.00 14.07 ?  66  ASP   A HA   1 
ATOM   1550 H  HB2  . ASP   A 1 66  ? 35.878 10.633  2.973   1.00 15.81 ?  66  ASP   A HB2  1 
ATOM   1551 H  HB3  . ASP   A 1 66  ? 36.567 10.826  1.554   1.00 15.81 ?  66  ASP   A HB3  1 
ATOM   1552 N  N    . ASP   A 1 67  ? 37.934 8.379   3.428   1.00 12.03 ?  67  ASP   A N    1 
ATOM   1553 C  CA   . ASP   A 1 67  ? 39.291 7.932   3.719   1.00 12.82 ?  67  ASP   A CA   1 
ATOM   1554 C  C    . ASP   A 1 67  ? 39.508 6.492   3.259   1.00 12.67 ?  67  ASP   A C    1 
ATOM   1555 O  O    . ASP   A 1 67  ? 40.567 6.163   2.710   1.00 13.21 ?  67  ASP   A O    1 
ATOM   1556 C  CB   . ASP   A 1 67  ? 39.571 8.074   5.213   1.00 14.14 ?  67  ASP   A CB   1 
ATOM   1557 C  CG   . ASP   A 1 67  ? 40.864 7.404   5.630   1.00 15.50 ?  67  ASP   A CG   1 
ATOM   1558 O  OD1  . ASP   A 1 67  ? 41.936 8.029   5.487   1.00 18.49 ?  67  ASP   A OD1  1 
ATOM   1559 O  OD2  . ASP   A 1 67  ? 40.802 6.246   6.104   1.00 15.17 -1 67  ASP   A OD2  1 
ATOM   1560 H  H    . ASP   A 1 67  ? 37.451 8.538   4.117   1.00 14.41 ?  67  ASP   A H    1 
ATOM   1561 H  HA   . ASP   A 1 67  ? 39.919 8.495   3.239   1.00 15.35 ?  67  ASP   A HA   1 
ATOM   1562 H  HB2  . ASP   A 1 67  ? 39.637 9.011   5.432   1.00 16.93 ?  67  ASP   A HB2  1 
ATOM   1563 H  HB3  . ASP   A 1 67  ? 38.846 7.659   5.708   1.00 16.93 ?  67  ASP   A HB3  1 
ATOM   1564 N  N    . TYR   A 1 68  ? 38.515 5.617   3.466   1.00 12.36 ?  68  TYR   A N    1 
ATOM   1565 C  CA   . TYR   A 1 68  ? 38.628 4.239   2.988   1.00 12.31 ?  68  TYR   A CA   1 
ATOM   1566 C  C    . TYR   A 1 68  ? 38.868 4.195   1.480   1.00 12.10 ?  68  TYR   A C    1 
ATOM   1567 O  O    . TYR   A 1 68  ? 39.743 3.460   1.003   1.00 12.65 ?  68  TYR   A O    1 
ATOM   1568 C  CB   . TYR   A 1 68  ? 37.378 3.421   3.364   1.00 12.48 ?  68  TYR   A CB   1 
ATOM   1569 C  CG   . TYR   A 1 68  ? 37.403 2.032   2.738   1.00 13.90 ?  68  TYR   A CG   1 
ATOM   1570 C  CD1  . TYR   A 1 68  ? 36.941 1.835   1.439   1.00 15.53 ?  68  TYR   A CD1  1 
ATOM   1571 C  CD2  . TYR   A 1 68  ? 37.935 0.944   3.410   1.00 15.82 ?  68  TYR   A CD2  1 
ATOM   1572 C  CE1  . TYR   A 1 68  ? 37.006 0.618   0.827   1.00 17.12 ?  68  TYR   A CE1  1 
ATOM   1573 C  CE2  . TYR   A 1 68  ? 38.000 -0.317  2.795   1.00 16.59 ?  68  TYR   A CE2  1 
ATOM   1574 C  CZ   . TYR   A 1 68  ? 37.536 -0.453  1.504   1.00 17.54 ?  68  TYR   A CZ   1 
ATOM   1575 O  OH   . TYR   A 1 68  ? 37.607 -1.666  0.873   1.00 18.93 ?  68  TYR   A OH   1 
ATOM   1576 H  H    . TYR   A 1 68  ? 37.775 5.794   3.872   1.00 14.80 ?  68  TYR   A H    1 
ATOM   1577 H  HA   . TYR   A 1 68  ? 39.388 3.823   3.420   1.00 14.75 ?  68  TYR   A HA   1 
ATOM   1578 H  HB2  . TYR   A 1 68  ? 37.342 3.316   4.326   1.00 14.95 ?  68  TYR   A HB2  1 
ATOM   1579 H  HB3  . TYR   A 1 68  ? 36.586 3.883   3.045   1.00 14.95 ?  68  TYR   A HB3  1 
ATOM   1580 H  HD1  . TYR   A 1 68  ? 36.594 2.563   0.968   1.00 18.61 ?  68  TYR   A HD1  1 
ATOM   1581 H  HD2  . TYR   A 1 68  ? 38.270 1.054   4.268   1.00 18.95 ?  68  TYR   A HD2  1 
ATOM   1582 H  HE1  . TYR   A 1 68  ? 36.684 0.516   -0.041  1.00 20.51 ?  68  TYR   A HE1  1 
ATOM   1583 H  HE2  . TYR   A 1 68  ? 38.363 -1.046  3.238   1.00 19.87 ?  68  TYR   A HE2  1 
ATOM   1584 H  HH   . TYR   A 1 68  ? 37.937 -2.236  1.392   1.00 22.69 ?  68  TYR   A HH   1 
ATOM   1585 N  N    . ILE   A 1 69  ? 38.082 4.955   0.709   1.00 11.64 ?  69  ILE   A N    1 
ATOM   1586 C  CA   . ILE   A 1 69  ? 38.217 4.940   -0.747  1.00 11.83 ?  69  ILE   A CA   1 
ATOM   1587 C  C    . ILE   A 1 69  ? 39.548 5.547   -1.180  1.00 11.72 ?  69  ILE   A C    1 
ATOM   1588 O  O    . ILE   A 1 69  ? 40.192 5.059   -2.117  1.00 12.02 ?  69  ILE   A O    1 
ATOM   1589 C  CB   . ILE   A 1 69  ? 37.017 5.646   -1.411  1.00 12.94 ?  69  ILE   A CB   1 
ATOM   1590 C  CG1  . ILE   A 1 69  ? 35.704 4.912   -1.135  1.00 13.10 ?  69  ILE   A CG1  1 
ATOM   1591 C  CG2  . ILE   A 1 69  ? 37.264 5.842   -2.917  1.00 14.55 ?  69  ILE   A CG2  1 
ATOM   1592 C  CD1  . ILE   A 1 69  ? 35.538 3.629   -1.921  1.00 13.84 ?  69  ILE   A CD1  1 
ATOM   1593 H  H    . ILE   A 1 69  ? 37.476 5.488   1.008   1.00 13.94 ?  69  ILE   A H    1 
ATOM   1594 H  HA   . ILE   A 1 69  ? 38.212 4.019   -1.039  1.00 14.17 ?  69  ILE   A HA   1 
ATOM   1595 H  HB   . ILE   A 1 69  ? 36.943 6.526   -1.015  1.00 15.49 ?  69  ILE   A HB   1 
ATOM   1596 H  HG12 . ILE   A 1 69  ? 35.669 4.685   -0.192  1.00 15.69 ?  69  ILE   A HG12 1 
ATOM   1597 H  HG13 . ILE   A 1 69  ? 34.968 5.497   -1.360  1.00 15.69 ?  69  ILE   A HG13 1 
ATOM   1598 H  HG21 . ILE   A 1 69  ? 36.418 6.051   -3.350  1.00 17.43 ?  69  ILE   A HG21 1 
ATOM   1599 H  HG22 . ILE   A 1 69  ? 37.882 6.584   -3.045  1.00 17.43 ?  69  ILE   A HG22 1 
ATOM   1600 H  HG23 . ILE   A 1 69  ? 37.635 5.033   -3.291  1.00 17.43 ?  69  ILE   A HG23 1 
ATOM   1601 H  HD11 . ILE   A 1 69  ? 34.748 3.169   -1.602  1.00 16.58 ?  69  ILE   A HD11 1 
ATOM   1602 H  HD12 . ILE   A 1 69  ? 35.435 3.849   -2.862  1.00 16.58 ?  69  ILE   A HD12 1 
ATOM   1603 H  HD13 . ILE   A 1 69  ? 36.321 3.074   -1.794  1.00 16.58 ?  69  ILE   A HD13 1 
ATOM   1604 N  N    . ALA   A 1 70  ? 39.976 6.624   -0.519  1.00 12.15 ?  70  ALA   A N    1 
ATOM   1605 C  CA   . ALA   A 1 70  ? 41.253 7.235   -0.871  1.00 13.05 ?  70  ALA   A CA   1 
ATOM   1606 C  C    . ALA   A 1 70  ? 42.405 6.255   -0.695  1.00 13.20 ?  70  ALA   A C    1 
ATOM   1607 O  O    . ALA   A 1 70  ? 43.374 6.293   -1.456  1.00 15.28 ?  70  ALA   A O    1 
ATOM   1608 C  CB   . ALA   A 1 70  ? 41.488 8.492   -0.030  1.00 13.74 ?  70  ALA   A CB   1 
ATOM   1609 H  H    . ALA   A 1 70  ? 39.546 7.014   0.117   1.00 14.56 ?  70  ALA   A H    1 
ATOM   1610 H  HA   . ALA   A 1 70  ? 41.222 7.508   -1.803  1.00 15.63 ?  70  ALA   A HA   1 
ATOM   1611 H  HB1  . ALA   A 1 70  ? 42.344 8.879   -0.280  1.00 16.46 ?  70  ALA   A HB1  1 
ATOM   1612 H  HB2  . ALA   A 1 70  ? 40.777 9.126   -0.195  1.00 16.46 ?  70  ALA   A HB2  1 
ATOM   1613 H  HB3  . ALA   A 1 70  ? 41.503 8.243   0.909   1.00 16.46 ?  70  ALA   A HB3  1 
ATOM   1614 N  N    . THR   A 1 71  ? 42.301 5.358   0.284   1.00 12.91 ?  71  THR   A N    1 
ATOM   1615 C  CA   . THR   A 1 71  ? 43.351 4.376   0.532   1.00 14.33 ?  71  THR   A CA   1 
ATOM   1616 C  C    . THR   A 1 71  ? 43.231 3.154   -0.373  1.00 14.41 ?  71  THR   A C    1 
ATOM   1617 O  O    . THR   A 1 71  ? 44.244 2.645   -0.874  1.00 16.44 ?  71  THR   A O    1 
ATOM   1618 C  CB   . THR   A 1 71  ? 43.277 3.926   1.987   1.00 16.16 ?  71  THR   A CB   1 
ATOM   1619 O  OG1  . THR   A 1 71  ? 43.538 5.047   2.836   1.00 17.54 ?  71  THR   A OG1  1 
ATOM   1620 C  CG2  . THR   A 1 71  ? 44.279 2.817   2.271   1.00 17.76 ?  71  THR   A CG2  1 
ATOM   1621 H  H    . THR   A 1 71  ? 41.626 5.294   0.813   1.00 15.46 ?  71  THR   A H    1 
ATOM   1622 H  HA   . THR   A 1 71  ? 44.214 4.783   0.375   1.00 17.17 ?  71  THR   A HA   1 
ATOM   1623 H  HB   . THR   A 1 71  ? 42.385 3.574   2.163   1.00 19.37 ?  71  THR   A HB   1 
ATOM   1624 H  HG1  . THR   A 1 71  ? 43.486 4.800   3.639   1.00 21.02 ?  71  THR   A HG1  1 
ATOM   1625 H  HG21 . THR   A 1 71  ? 44.412 2.733   3.227   1.00 21.28 ?  71  THR   A HG21 1 
ATOM   1626 H  HG22 . THR   A 1 71  ? 43.958 1.970   1.923   1.00 21.28 ?  71  THR   A HG22 1 
ATOM   1627 H  HG23 . THR   A 1 71  ? 45.130 3.028   1.854   1.00 21.28 ?  71  THR   A HG23 1 
ATOM   1628 N  N    . ASN   A 1 72  ? 42.007 2.643   -0.563  1.00 13.29 ?  72  ASN   A N    1 
ATOM   1629 C  CA   . ASN   A 1 72  ? 41.790 1.317   -1.127  1.00 13.91 ?  72  ASN   A CA   1 
ATOM   1630 C  C    . ASN   A 1 72  ? 41.161 1.308   -2.508  1.00 13.86 ?  72  ASN   A C    1 
ATOM   1631 O  O    . ASN   A 1 72  ? 41.171 0.255   -3.161  1.00 15.12 ?  72  ASN   A O    1 
ATOM   1632 C  CB   . ASN   A 1 72  ? 40.905 0.496   -0.183  1.00 14.69 ?  72  ASN   A CB   1 
ATOM   1633 C  CG   . ASN   A 1 72  ? 41.520 0.350   1.180   1.00 15.60 ?  72  ASN   A CG   1 
ATOM   1634 O  OD1  . ASN   A 1 72  ? 41.063 0.939   2.156   1.00 17.47 ?  72  ASN   A OD1  1 
ATOM   1635 N  ND2  . ASN   A 1 72  ? 42.578 -0.424  1.252   1.00 16.25 ?  72  ASN   A ND2  1 
ATOM   1636 H  H    . ASN   A 1 72  ? 41.274 3.058   -0.375  1.00 15.92 ?  72  ASN   A H    1 
ATOM   1637 H  HA   . ASN   A 1 72  ? 42.648 0.870   -1.201  1.00 16.66 ?  72  ASN   A HA   1 
ATOM   1638 H  HB2  . ASN   A 1 72  ? 40.052 0.936   -0.087  1.00 17.59 ?  72  ASN   A HB2  1 
ATOM   1639 H  HB3  . ASN   A 1 72  ? 40.790 -0.393  -0.557  1.00 17.59 ?  72  ASN   A HB3  1 
ATOM   1640 H  HD21 . ASN   A 1 72  ? 42.980 -0.534  2.006   1.00 19.47 ?  72  ASN   A HD21 1 
ATOM   1641 H  HD22 . ASN   A 1 72  ? 42.882 -0.813  0.546   1.00 19.47 ?  72  ASN   A HD22 1 
ATOM   1642 N  N    . GLY   A 1 73  ? 40.603 2.423   -2.962  1.00 13.24 ?  73  GLY   A N    1 
ATOM   1643 C  CA   . GLY   A 1 73  ? 39.872 2.446   -4.200  1.00 12.96 ?  73  GLY   A CA   1 
ATOM   1644 C  C    . GLY   A 1 73  ? 38.483 1.862   -4.033  1.00 12.63 ?  73  GLY   A C    1 
ATOM   1645 O  O    . GLY   A 1 73  ? 38.096 1.396   -2.952  1.00 13.34 ?  73  GLY   A O    1 
ATOM   1646 H  H    . GLY   A 1 73  ? 40.647 3.191   -2.570  1.00 15.86 ?  73  GLY   A H    1 
ATOM   1647 H  HA2  . GLY   A 1 73  ? 39.793 3.365   -4.514  1.00 15.52 ?  73  GLY   A HA2  1 
ATOM   1648 H  HA3  . GLY   A 1 73  ? 40.350 1.936   -4.875  1.00 15.52 ?  73  GLY   A HA3  1 
ATOM   1649 N  N    . PRO   A 1 74  ? 37.710 1.873   -5.117  1.00 12.87 ?  74  PRO   A N    1 
ATOM   1650 C  CA   . PRO   A 1 74  ? 36.311 1.445   -5.035  1.00 13.27 ?  74  PRO   A CA   1 
ATOM   1651 C  C    . PRO   A 1 74  ? 36.163 -0.036  -4.719  1.00 12.51 ?  74  PRO   A C    1 
ATOM   1652 O  O    . PRO   A 1 74  ? 37.032 -0.862  -5.008  1.00 13.53 ?  74  PRO   A O    1 
ATOM   1653 C  CB   . PRO   A 1 74  ? 35.764 1.751   -6.435  1.00 14.73 ?  74  PRO   A CB   1 
ATOM   1654 C  CG   . PRO   A 1 74  ? 36.709 2.737   -7.031  1.00 17.47 ?  74  PRO   A CG   1 
ATOM   1655 C  CD   . PRO   A 1 74  ? 38.049 2.399   -6.449  1.00 14.76 ?  74  PRO   A CD   1 
ATOM   1656 H  HA   . PRO   A 1 74  ? 35.830 1.973   -4.375  1.00 15.89 ?  74  PRO   A HA   1 
ATOM   1657 H  HB2  . PRO   A 1 74  ? 35.741 0.936   -6.957  1.00 17.64 ?  74  PRO   A HB2  1 
ATOM   1658 H  HB3  . PRO   A 1 74  ? 34.875 2.135   -6.358  1.00 17.64 ?  74  PRO   A HB3  1 
ATOM   1659 H  HG2  . PRO   A 1 74  ? 36.727 2.638   -7.996  1.00 20.93 ?  74  PRO   A HG2  1 
ATOM   1660 H  HG3  . PRO   A 1 74  ? 36.453 3.637   -6.783  1.00 20.93 ?  74  PRO   A HG3  1 
ATOM   1661 H  HD2  . PRO   A 1 74  ? 38.494 1.716   -6.981  1.00 17.68 ?  74  PRO   A HD2  1 
ATOM   1662 H  HD3  . PRO   A 1 74  ? 38.598 3.201   -6.381  1.00 17.68 ?  74  PRO   A HD3  1 
ATOM   1663 N  N    . LEU   A 1 75  ? 35.021 -0.364  -4.126  1.00 11.83 ?  75  LEU   A N    1 
ATOM   1664 C  CA   . LEU   A 1 75  ? 34.620 -1.753  -3.977  1.00 11.50 ?  75  LEU   A CA   1 
ATOM   1665 C  C    . LEU   A 1 75  ? 34.230 -2.327  -5.334  1.00 12.07 ?  75  LEU   A C    1 
ATOM   1666 O  O    . LEU   A 1 75  ? 34.100 -1.610  -6.331  1.00 13.42 ?  75  LEU   A O    1 
ATOM   1667 C  CB   . LEU   A 1 75  ? 33.426 -1.872  -3.027  1.00 11.56 ?  75  LEU   A CB   1 
ATOM   1668 C  CG   . LEU   A 1 75  ? 33.634 -1.455  -1.574  1.00 13.27 ?  75  LEU   A CG   1 
ATOM   1669 C  CD1  . LEU   A 1 75  ? 32.349 -1.655  -0.778  1.00 15.09 ?  75  LEU   A CD1  1 
ATOM   1670 C  CD2  . LEU   A 1 75  ? 34.787 -2.166  -0.916  1.00 16.66 ?  75  LEU   A CD2  1 
ATOM   1671 H  H    . LEU   A 1 75  ? 34.457 0.205   -3.808  1.00 14.17 ?  75  LEU   A H    1 
ATOM   1672 H  HA   . LEU   A 1 75  ? 35.358 -2.265  -3.623  1.00 13.77 ?  75  LEU   A HA   1 
ATOM   1673 H  HB2  . LEU   A 1 75  ? 32.704 -1.331  -3.377  1.00 13.84 ?  75  LEU   A HB2  1 
ATOM   1674 H  HB3  . LEU   A 1 75  ? 33.149 -2.804  -3.015  1.00 13.84 ?  75  LEU   A HB3  1 
ATOM   1675 H  HG   . LEU   A 1 75  ? 33.843 -0.506  -1.561  1.00 15.89 ?  75  LEU   A HG   1 
ATOM   1676 H  HD11 . LEU   A 1 75  ? 32.502 -1.379  0.139   1.00 18.08 ?  75  LEU   A HD11 1 
ATOM   1677 H  HD12 . LEU   A 1 75  ? 31.651 -1.108  -1.176  1.00 18.08 ?  75  LEU   A HD12 1 
ATOM   1678 H  HD13 . LEU   A 1 75  ? 32.101 -2.588  -0.811  1.00 18.08 ?  75  LEU   A HD13 1 
ATOM   1679 H  HD21 . LEU   A 1 75  ? 34.835 -1.898  0.016   1.00 19.97 ?  75  LEU   A HD21 1 
ATOM   1680 H  HD22 . LEU   A 1 75  ? 34.653 -3.120  -0.982  1.00 19.97 ?  75  LEU   A HD22 1 
ATOM   1681 H  HD23 . LEU   A 1 75  ? 35.615 -1.916  -1.367  1.00 19.97 ?  75  LEU   A HD23 1 
ATOM   1682 N  N    . LYS   A 1 76  ? 34.036 -3.647  -5.353  1.00 12.32 ?  76  LYS   A N    1 
ATOM   1683 C  CA   . LYS   A 1 76  ? 33.437 -4.358  -6.476  1.00 13.10 ?  76  LYS   A CA   1 
ATOM   1684 C  C    . LYS   A 1 76  ? 31.925 -4.446  -6.280  1.00 11.77 ?  76  LYS   A C    1 
ATOM   1685 O  O    . LYS   A 1 76  ? 31.446 -4.564  -5.156  1.00 11.70 ?  76  LYS   A O    1 
ATOM   1686 C  CB   . LYS   A 1 76  ? 33.979 -5.796  -6.538  1.00 14.92 ?  76  LYS   A CB   1 
ATOM   1687 C  CG   . LYS   A 1 76  ? 35.492 -5.909  -6.724  1.00 16.42 ?  76  LYS   A CG   1 
ATOM   1688 C  CD   . LYS   A 1 76  ? 36.000 -7.319  -6.511  1.00 17.85 ?  76  LYS   A CD   1 
ATOM   1689 C  CE   . LYS   A 1 76  ? 37.500 -7.389  -6.717  1.00 20.32 ?  76  LYS   A CE   1 
ATOM   1690 N  NZ   . LYS   A 1 76  ? 38.037 -8.739  -6.461  1.00 20.86 ?  76  LYS   A NZ   1 
ATOM   1691 H  H    . LYS   A 1 76  ? 34.253 -4.168  -4.700  1.00 14.75 ?  76  LYS   A H    1 
ATOM   1692 H  HA   . LYS   A 1 76  ? 33.634 -3.901  -7.310  1.00 15.68 ?  76  LYS   A HA   1 
ATOM   1693 H  HB2  . LYS   A 1 76  ? 33.750 -6.244  -5.709  1.00 17.87 ?  76  LYS   A HB2  1 
ATOM   1694 H  HB3  . LYS   A 1 76  ? 33.556 -6.250  -7.282  1.00 17.87 ?  76  LYS   A HB3  1 
ATOM   1695 H  HG2  . LYS   A 1 76  ? 35.719 -5.638  -7.626  1.00 19.67 ?  76  LYS   A HG2  1 
ATOM   1696 H  HG3  . LYS   A 1 76  ? 35.933 -5.330  -6.082  1.00 19.67 ?  76  LYS   A HG3  1 
ATOM   1697 H  HD2  . LYS   A 1 76  ? 35.797 -7.599  -5.604  1.00 21.39 ?  76  LYS   A HD2  1 
ATOM   1698 H  HD3  . LYS   A 1 76  ? 35.572 -7.912  -7.150  1.00 21.39 ?  76  LYS   A HD3  1 
ATOM   1699 H  HE2  . LYS   A 1 76  ? 37.704 -7.149  -7.633  1.00 24.35 ?  76  LYS   A HE2  1 
ATOM   1700 H  HE3  . LYS   A 1 76  ? 37.930 -6.772  -6.105  1.00 24.35 ?  76  LYS   A HE3  1 
ATOM   1701 H  HZ1  . LYS   A 1 76  ? 38.916 -8.751  -6.590  1.00 25.00 ?  76  LYS   A HZ1  1 
ATOM   1702 H  HZ2  . LYS   A 1 76  ? 37.863 -8.986  -5.622  1.00 25.00 ?  76  LYS   A HZ2  1 
ATOM   1703 H  HZ3  . LYS   A 1 76  ? 37.657 -9.330  -7.014  1.00 25.00 ?  76  LYS   A HZ3  1 
ATOM   1704 N  N    . VAL   A 1 77  ? 31.171 -4.415  -7.384  1.00 12.16 ?  77  VAL   A N    1 
ATOM   1705 C  CA   . VAL   A 1 77  ? 29.765 -4.804  -7.297  1.00 12.15 ?  77  VAL   A CA   1 
ATOM   1706 C  C    . VAL   A 1 77  ? 29.703 -6.258  -6.856  1.00 11.80 ?  77  VAL   A C    1 
ATOM   1707 O  O    . VAL   A 1 77  ? 30.361 -7.127  -7.440  1.00 12.07 ?  77  VAL   A O    1 
ATOM   1708 C  CB   . VAL   A 1 77  ? 29.040 -4.585  -8.633  1.00 12.82 ?  77  VAL   A CB   1 
ATOM   1709 C  CG1  . VAL   A 1 77  ? 27.578 -5.023  -8.522  1.00 13.90 ?  77  VAL   A CG1  1 
ATOM   1710 C  CG2  . VAL   A 1 77  ? 29.130 -3.126  -9.062  1.00 14.65 ?  77  VAL   A CG2  1 
ATOM   1711 H  H    . VAL   A 1 77  ? 31.447 -4.177  -8.165  1.00 14.57 ?  77  VAL   A H    1 
ATOM   1712 H  HA   . VAL   A 1 77  ? 29.329 -4.259  -6.622  1.00 14.55 ?  77  VAL   A HA   1 
ATOM   1713 H  HB   . VAL   A 1 77  ? 29.468 -5.123  -9.316  1.00 15.35 ?  77  VAL   A HB   1 
ATOM   1714 H  HG11 . VAL   A 1 77  ? 27.101 -4.723  -9.310  1.00 16.65 ?  77  VAL   A HG11 1 
ATOM   1715 H  HG12 . VAL   A 1 77  ? 27.542 -5.989  -8.459  1.00 16.65 ?  77  VAL   A HG12 1 
ATOM   1716 H  HG13 . VAL   A 1 77  ? 27.191 -4.622  -7.727  1.00 16.65 ?  77  VAL   A HG13 1 
ATOM   1717 H  HG21 . VAL   A 1 77  ? 28.618 -3.007  -9.878  1.00 17.55 ?  77  VAL   A HG21 1 
ATOM   1718 H  HG22 . VAL   A 1 77  ? 28.765 -2.567  -8.359  1.00 17.55 ?  77  VAL   A HG22 1 
ATOM   1719 H  HG23 . VAL   A 1 77  ? 30.059 -2.897  -9.219  1.00 17.55 ?  77  VAL   A HG23 1 
ATOM   1720 N  N    . GLY   A 1 78  ? 28.927 -6.528  -5.807  1.00 11.60 ?  78  GLY   A N    1 
ATOM   1721 C  CA   . GLY   A 1 78  ? 28.910 -7.820  -5.154  1.00 11.57 ?  78  GLY   A CA   1 
ATOM   1722 C  C    . GLY   A 1 78  ? 29.817 -7.903  -3.947  1.00 11.28 ?  78  GLY   A C    1 
ATOM   1723 O  O    . GLY   A 1 78  ? 29.755 -8.902  -3.214  1.00 11.84 ?  78  GLY   A O    1 
ATOM   1724 H  H    . GLY   A 1 78  ? 28.384 -5.953  -5.458  1.00 13.89 ?  78  GLY   A H    1 
ATOM   1725 H  HA2  . GLY   A 1 78  ? 28.006 -8.013  -4.872  1.00 13.86 ?  78  GLY   A HA2  1 
ATOM   1726 H  HA3  . GLY   A 1 78  ? 29.184 -8.495  -5.794  1.00 13.86 ?  78  GLY   A HA3  1 
ATOM   1727 N  N    . GLY   A 1 79  ? 30.678 -6.900  -3.737  1.00 11.03 ?  79  GLY   A N    1 
ATOM   1728 C  CA   . GLY   A 1 79  ? 31.639 -6.914  -2.659  1.00 11.40 ?  79  GLY   A CA   1 
ATOM   1729 C  C    . GLY   A 1 79  ? 31.191 -6.118  -1.443  1.00 10.59 ?  79  GLY   A C    1 
ATOM   1730 O  O    . GLY   A 1 79  ? 30.077 -5.602  -1.366  1.00 11.55 ?  79  GLY   A O    1 
ATOM   1731 H  H    . GLY   A 1 79  ? 30.717 -6.185  -4.220  1.00 13.20 ?  79  GLY   A H    1 
ATOM   1732 H  HA2  . GLY   A 1 79  ? 31.796 -7.836  -2.388  1.00 13.65 ?  79  GLY   A HA2  1 
ATOM   1733 H  HA3  . GLY   A 1 79  ? 32.482 -6.550  -2.979  1.00 13.65 ?  79  GLY   A HA3  1 
ATOM   1734 N  N    . SER   A 1 80  ? 32.098 -6.028  -0.474  1.00 11.46 ?  80  SER   A N    1 
ATOM   1735 C  CA   . SER   A 1 80  ? 31.780 -5.396  0.796   1.00 10.90 ?  80  SER   A CA   1 
ATOM   1736 C  C    . SER   A 1 80  ? 33.055 -4.946  1.497   1.00 10.91 ?  80  SER   A C    1 
ATOM   1737 O  O    . SER   A 1 80  ? 34.165 -5.390  1.174   1.00 12.65 ?  80  SER   A O    1 
ATOM   1738 C  CB   . SER   A 1 80  ? 31.026 -6.362  1.719   1.00 12.07 ?  80  SER   A CB   1 
ATOM   1739 O  OG   . SER   A 1 80  ? 31.862 -7.407  2.191   1.00 14.06 ?  80  SER   A OG   1 
ATOM   1740 H  H    . SER   A 1 80  ? 32.908 -6.318  -0.532  1.00 13.72 ?  80  SER   A H    1 
ATOM   1741 H  HA   . SER   A 1 80  ? 31.224 -4.614  0.619   1.00 13.05 ?  80  SER   A HA   1 
ATOM   1742 H  HB2  . SER   A 1 80  ? 30.687 -5.861  2.474   1.00 14.45 ?  80  SER   A HB2  1 
ATOM   1743 H  HB3  . SER   A 1 80  ? 30.287 -6.747  1.220   1.00 14.45 ?  80  SER   A HB3  1 
ATOM   1744 H  HG   . SER   A 1 80  ? 32.165 -7.843  1.535   1.00 16.84 ?  80  SER   A HG   1 
ATOM   1745 N  N    . CYS   A 1 81  ? 32.868 -4.092  2.501   1.00 10.81 ?  81  CYS   A N    1 
ATOM   1746 C  CA   . CYS   A 1 81  ? 33.919 -3.815  3.466   1.00 10.75 ?  81  CYS   A CA   1 
ATOM   1747 C  C    . CYS   A 1 81  ? 33.278 -3.579  4.825   1.00 10.74 ?  81  CYS   A C    1 
ATOM   1748 O  O    . CYS   A 1 81  ? 32.114 -3.181  4.911   1.00 11.95 ?  81  CYS   A O    1 
ATOM   1749 C  CB   . CYS   A 1 81  ? 34.786 -2.619  3.050   1.00 11.79 ?  81  CYS   A CB   1 
ATOM   1750 S  SG   . CYS   A 1 81  ? 33.896 -1.046  3.065   1.00 11.75 ?  81  CYS   A SG   1 
ATOM   1751 H  H    . CYS   A 1 81  ? 32.137 -3.657  2.645   1.00 12.94 ?  81  CYS   A H    1 
ATOM   1752 H  HA   . CYS   A 1 81  ? 34.496 -4.592  3.535   1.00 12.87 ?  81  CYS   A HA   1 
ATOM   1753 H  HB2  . CYS   A 1 81  ? 35.540 -2.550  3.663   1.00 14.12 ?  81  CYS   A HB2  1 
ATOM   1754 H  HB3  . CYS   A 1 81  ? 35.119 -2.773  2.147   1.00 14.12 ?  81  CYS   A HB3  1 
ATOM   1755 H  HG   . CYS   A 1 81  ? 34.640 -0.166  2.729   1.00 14.07 ?  81  CYS   A HG   1 
ATOM   1756 N  N    . VAL   A 1 82  ? 34.043 -3.834  5.881   1.00 11.05 ?  82  VAL   A N    1 
ATOM   1757 C  CA   . VAL   A 1 82  ? 33.617 -3.591  7.251   1.00 11.53 ?  82  VAL   A CA   1 
ATOM   1758 C  C    . VAL   A 1 82  ? 34.212 -2.272  7.718   1.00 11.98 ?  82  VAL   A C    1 
ATOM   1759 O  O    . VAL   A 1 82  ? 35.437 -2.098  7.701   1.00 12.58 ?  82  VAL   A O    1 
ATOM   1760 C  CB   . VAL   A 1 82  ? 34.052 -4.730  8.186   1.00 13.01 ?  82  VAL   A CB   1 
ATOM   1761 C  CG1  . VAL   A 1 82  ? 33.606 -4.447  9.610   1.00 14.56 ?  82  VAL   A CG1  1 
ATOM   1762 C  CG2  . VAL   A 1 82  ? 33.493 -6.060  7.707   1.00 14.18 ?  82  VAL   A CG2  1 
ATOM   1763 H  H    . VAL   A 1 82  ? 34.841 -4.169  5.828   1.00 13.23 ?  82  VAL   A H    1 
ATOM   1764 H  HA   . VAL   A 1 82  ? 32.650 -3.517  7.277   1.00 13.81 ?  82  VAL   A HA   1 
ATOM   1765 H  HB   . VAL   A 1 82  ? 35.016 -4.786  8.186   1.00 15.58 ?  82  VAL   A HB   1 
ATOM   1766 H  HG11 . VAL   A 1 82  ? 33.709 -5.253  10.139  1.00 17.45 ?  82  VAL   A HG11 1 
ATOM   1767 H  HG12 . VAL   A 1 82  ? 34.150 -3.735  9.983   1.00 17.45 ?  82  VAL   A HG12 1 
ATOM   1768 H  HG13 . VAL   A 1 82  ? 32.671 -4.177  9.604   1.00 17.45 ?  82  VAL   A HG13 1 
ATOM   1769 H  HG21 . VAL   A 1 82  ? 33.737 -6.751  8.342   1.00 16.99 ?  82  VAL   A HG21 1 
ATOM   1770 H  HG22 . VAL   A 1 82  ? 32.527 -5.995  7.643   1.00 16.99 ?  82  VAL   A HG22 1 
ATOM   1771 H  HG23 . VAL   A 1 82  ? 33.869 -6.263  6.836   1.00 16.99 ?  82  VAL   A HG23 1 
ATOM   1772 N  N    . LEU   A 1 83  ? 33.358 -1.350  8.142   1.00 11.49 ?  83  LEU   A N    1 
ATOM   1773 C  CA   . LEU   A 1 83  ? 33.785 -0.087  8.720   1.00 11.40 ?  83  LEU   A CA   1 
ATOM   1774 C  C    . LEU   A 1 83  ? 33.065 0.094   10.050  1.00 11.64 ?  83  LEU   A C    1 
ATOM   1775 O  O    . LEU   A 1 83  ? 32.344 -0.798  10.515  1.00 12.07 ?  83  LEU   A O    1 
ATOM   1776 C  CB   . LEU   A 1 83  ? 33.535 1.072   7.744   1.00 11.86 ?  83  LEU   A CB   1 
ATOM   1777 C  CG   . LEU   A 1 83  ? 34.429 1.064   6.499   1.00 12.78 ?  83  LEU   A CG   1 
ATOM   1778 C  CD1  . LEU   A 1 83  ? 33.980 2.112   5.496   1.00 13.38 ?  83  LEU   A CD1  1 
ATOM   1779 C  CD2  . LEU   A 1 83  ? 35.902 1.280   6.871   1.00 13.30 ?  83  LEU   A CD2  1 
ATOM   1780 H  H    . LEU   A 1 83  ? 32.502 -1.438  8.104   1.00 13.76 ?  83  LEU   A H    1 
ATOM   1781 H  HA   . LEU   A 1 83  ? 34.735 -0.121  8.898   1.00 13.65 ?  83  LEU   A HA   1 
ATOM   1782 H  HB2  . LEU   A 1 83  ? 32.615 1.039   7.438   1.00 14.20 ?  83  LEU   A HB2  1 
ATOM   1783 H  HB3  . LEU   A 1 83  ? 33.690 1.914   8.205   1.00 14.20 ?  83  LEU   A HB3  1 
ATOM   1784 H  HG   . LEU   A 1 83  ? 34.360 0.198   6.072   1.00 15.30 ?  83  LEU   A HG   1 
ATOM   1785 H  HD11 . LEU   A 1 83  ? 34.566 2.074   4.721   1.00 16.02 ?  83  LEU   A HD11 1 
ATOM   1786 H  HD12 . LEU   A 1 83  ? 33.069 1.920   5.232   1.00 16.02 ?  83  LEU   A HD12 1 
ATOM   1787 H  HD13 . LEU   A 1 83  ? 34.034 2.985   5.909   1.00 16.02 ?  83  LEU   A HD13 1 
ATOM   1788 H  HD21 . LEU   A 1 83  ? 36.417 1.422   6.060   1.00 15.93 ?  83  LEU   A HD21 1 
ATOM   1789 H  HD22 . LEU   A 1 83  ? 35.973 2.059   7.446   1.00 15.93 ?  83  LEU   A HD22 1 
ATOM   1790 H  HD23 . LEU   A 1 83  ? 36.231 0.496   7.337   1.00 15.93 ?  83  LEU   A HD23 1 
ATOM   1791 N  N    . SER   A 1 84  ? 33.282 1.245   10.682  1.00 11.93 ?  84  SER   A N    1 
ATOM   1792 C  CA   . SER   A 1 84  ? 32.640 1.508   11.960  1.00 11.99 ?  84  SER   A CA   1 
ATOM   1793 C  C    . SER   A 1 84  ? 31.122 1.590   11.812  1.00 12.01 ?  84  SER   A C    1 
ATOM   1794 O  O    . SER   A 1 84  ? 30.595 2.049   10.800  1.00 12.29 ?  84  SER   A O    1 
ATOM   1795 C  CB   . SER   A 1 84  ? 33.141 2.830   12.533  1.00 13.00 ?  84  SER   A CB   1 
ATOM   1796 O  OG   . SER   A 1 84  ? 32.499 3.105   13.762  1.00 14.01 ?  84  SER   A OG   1 
ATOM   1797 H  H    . SER   A 1 84  ? 33.784 1.886   10.388  1.00 14.29 ?  84  SER   A H    1 
ATOM   1798 H  HA   . SER   A 1 84  ? 32.857 0.798   12.577  1.00 14.36 ?  84  SER   A HA   1 
ATOM   1799 H  HB2  . SER   A 1 84  ? 34.100 2.774   12.672  1.00 15.57 ?  84  SER   A HB2  1 
ATOM   1800 H  HB3  . SER   A 1 84  ? 32.941 3.546   11.904  1.00 15.57 ?  84  SER   A HB3  1 
ATOM   1801 H  HG   . SER   A 1 84  ? 32.783 3.832   14.075  1.00 16.79 ?  84  SER   A HG   1 
ATOM   1802 N  N    . GLY   A 1 85  ? 30.414 1.181   12.861  1.00 12.78 ?  85  GLY   A N    1 
ATOM   1803 C  CA   . GLY   A 1 85  ? 28.991 1.414   12.949  1.00 13.62 ?  85  GLY   A CA   1 
ATOM   1804 C  C    . GLY   A 1 85  ? 28.622 2.727   13.598  1.00 13.07 ?  85  GLY   A C    1 
ATOM   1805 O  O    . GLY   A 1 85  ? 27.431 3.042   13.710  1.00 13.72 ?  85  GLY   A O    1 
ATOM   1806 H  H    . GLY   A 1 85  ? 30.750 0.763   13.538  1.00 15.31 ?  85  GLY   A H    1 
ATOM   1807 H  HA2  . GLY   A 1 85  ? 28.618 1.398   12.052  1.00 16.32 ?  85  GLY   A HA2  1 
ATOM   1808 H  HA3  . GLY   A 1 85  ? 28.586 0.701   13.456  1.00 16.32 ?  85  GLY   A HA3  1 
ATOM   1809 N  N    . HIS   A 1 86  ? 29.611 3.500   14.037  1.00 12.71 ?  86  HIS   A N    1 
ATOM   1810 C  CA   . HIS   A 1 86  ? 29.386 4.836   14.596  1.00 13.39 ?  86  HIS   A CA   1 
ATOM   1811 C  C    . HIS   A 1 86  ? 28.402 4.715   15.751  1.00 13.96 ?  86  HIS   A C    1 
ATOM   1812 O  O    . HIS   A 1 86  ? 28.591 3.843   16.614  1.00 15.10 ?  86  HIS   A O    1 
ATOM   1813 C  CB   . HIS   A 1 86  ? 29.007 5.808   13.489  1.00 13.28 ?  86  HIS   A CB   1 
ATOM   1814 C  CG   . HIS   A 1 86  ? 30.065 5.913   12.452  1.00 13.07 ?  86  HIS   A CG   1 
ATOM   1815 N  ND1  . HIS   A 1 86  ? 31.157 6.746   12.592  1.00 14.22 ?  86  HIS   A ND1  1 
ATOM   1816 C  CD2  . HIS   A 1 86  ? 30.250 5.229   11.301  1.00 13.01 ?  86  HIS   A CD2  1 
ATOM   1817 C  CE1  . HIS   A 1 86  ? 31.950 6.590   11.547  1.00 13.70 ?  86  HIS   A CE1  1 
ATOM   1818 N  NE2  . HIS   A 1 86  ? 31.430 5.669   10.757  1.00 13.41 ?  86  HIS   A NE2  1 
ATOM   1819 H  H    . HIS   A 1 86  ? 30.436 3.271   14.030  1.00 15.22 ?  86  HIS   A H    1 
ATOM   1820 H  HA   . HIS   A 1 86  ? 30.224 5.151   14.965  1.00 16.04 ?  86  HIS   A HA   1 
ATOM   1821 H  HB2  . HIS   A 1 86  ? 28.190 5.511   13.057  1.00 15.91 ?  86  HIS   A HB2  1 
ATOM   1822 H  HB3  . HIS   A 1 86  ? 28.875 6.696   13.866  1.00 15.91 ?  86  HIS   A HB3  1 
ATOM   1823 H  HD2  . HIS   A 1 86  ? 29.687 4.571   10.946  1.00 15.58 ?  86  HIS   A HD2  1 
ATOM   1824 H  HE1  . HIS   A 1 86  ? 32.740 7.049   11.378  1.00 16.40 ?  86  HIS   A HE1  1 
ATOM   1825 H  HE2  . HIS   A 1 86  ? 31.765 5.395   10.003  1.00 16.06 ?  86  HIS   A HE2  1 
ATOM   1826 N  N    . ASN   A 1 87  ? 27.391 5.566   15.821  1.00 15.11 ?  87  ASN   A N    1 
ATOM   1827 C  CA   . ASN   A 1 87  ? 26.419 5.562   16.895  1.00 16.00 ?  87  ASN   A CA   1 
ATOM   1828 C  C    . ASN   A 1 87  ? 25.293 4.567   16.668  1.00 17.31 ?  87  ASN   A C    1 
ATOM   1829 O  O    . ASN   A 1 87  ? 24.381 4.498   17.496  1.00 19.77 ?  87  ASN   A O    1 
ATOM   1830 C  CB   . ASN   A 1 87  ? 25.834 6.973   17.050  1.00 16.71 ?  87  ASN   A CB   1 
ATOM   1831 C  CG   . ASN   A 1 87  ? 25.307 7.537   15.736  1.00 17.50 ?  87  ASN   A CG   1 
ATOM   1832 O  OD1  . ASN   A 1 87  ? 25.942 7.420   14.690  1.00 18.12 ?  87  ASN   A OD1  1 
ATOM   1833 N  ND2  . ASN   A 1 87  ? 24.139 8.148   15.788  1.00 18.51 ?  87  ASN   A ND2  1 
ATOM   1834 H  H    . ASN   A 1 87  ? 27.245 6.178   15.239  1.00 18.10 ?  87  ASN   A H    1 
ATOM   1835 H  HA   . ASN   A 1 87  ? 26.860 5.322   17.730  1.00 19.17 ?  87  ASN   A HA   1 
ATOM   1836 H  HB2  . ASN   A 1 87  ? 25.099 6.940   17.688  1.00 20.03 ?  87  ASN   A HB2  1 
ATOM   1837 H  HB3  . ASN   A 1 87  ? 26.527 7.566   17.377  1.00 20.03 ?  87  ASN   A HB3  1 
ATOM   1838 H  HD21 . ASN   A 1 87  ? 23.800 8.476   15.073  1.00 22.18 ?  87  ASN   A HD21 1 
ATOM   1839 H  HD22 . ASN   A 1 87  ? 23.723 8.220   16.538  1.00 22.18 ?  87  ASN   A HD22 1 
ATOM   1840 N  N    . LEU   A 1 88  ? 25.338 3.787   15.590  1.00 16.13 ?  88  LEU   A N    1 
ATOM   1841 C  CA   . LEU   A 1 88  ? 24.224 2.925   15.206  1.00 16.04 ?  88  LEU   A CA   1 
ATOM   1842 C  C    . LEU   A 1 88  ? 24.440 1.447   15.505  1.00 15.50 ?  88  LEU   A C    1 
ATOM   1843 O  O    . LEU   A 1 88  ? 23.462 0.717   15.690  1.00 16.96 ?  88  LEU   A O    1 
ATOM   1844 C  CB   . LEU   A 1 88  ? 23.957 3.078   13.708  1.00 16.68 ?  88  LEU   A CB   1 
ATOM   1845 C  CG   . LEU   A 1 88  ? 23.667 4.499   13.224  1.00 18.11 ?  88  LEU   A CG   1 
ATOM   1846 C  CD1  . LEU   A 1 88  ? 23.529 4.509   11.714  1.00 18.50 ?  88  LEU   A CD1  1 
ATOM   1847 C  CD2  . LEU   A 1 88  ? 22.420 5.074   13.886  1.00 19.82 ?  88  LEU   A CD2  1 
ATOM   1848 H  H    . LEU   A 1 88  ? 26.014 3.743   15.062  1.00 19.33 ?  88  LEU   A H    1 
ATOM   1849 H  HA   . LEU   A 1 88  ? 23.430 3.215   15.680  1.00 19.22 ?  88  LEU   A HA   1 
ATOM   1850 H  HB2  . LEU   A 1 88  ? 24.728 2.762   13.219  1.00 19.99 ?  88  LEU   A HB2  1 
ATOM   1851 H  HB3  . LEU   A 1 88  ? 23.182 2.538   13.479  1.00 19.99 ?  88  LEU   A HB3  1 
ATOM   1852 H  HG   . LEU   A 1 88  ? 24.415 5.070   13.455  1.00 21.70 ?  88  LEU   A HG   1 
ATOM   1853 H  HD11 . LEU   A 1 88  ? 23.363 5.419   11.416  1.00 22.17 ?  88  LEU   A HD11 1 
ATOM   1854 H  HD12 . LEU   A 1 88  ? 24.351 4.178   11.319  1.00 22.17 ?  88  LEU   A HD12 1 
ATOM   1855 H  HD13 . LEU   A 1 88  ? 22.787 3.939   11.460  1.00 22.17 ?  88  LEU   A HD13 1 
ATOM   1856 H  HD21 . LEU   A 1 88  ? 22.220 5.935   13.486  1.00 23.76 ?  88  LEU   A HD21 1 
ATOM   1857 H  HD22 . LEU   A 1 88  ? 21.681 4.463   13.747  1.00 23.76 ?  88  LEU   A HD22 1 
ATOM   1858 H  HD23 . LEU   A 1 88  ? 22.591 5.181   14.834  1.00 23.76 ?  88  LEU   A HD23 1 
ATOM   1859 N  N    . ALA   A 1 89  ? 25.688 0.994   15.528  1.00 14.69 ?  89  ALA   A N    1 
ATOM   1860 C  CA   . ALA   A 1 89  ? 26.029 -0.418  15.624  1.00 14.59 ?  89  ALA   A CA   1 
ATOM   1861 C  C    . ALA   A 1 89  ? 27.515 -0.483  15.940  1.00 15.03 ?  89  ALA   A C    1 
ATOM   1862 O  O    . ALA   A 1 89  ? 28.228 0.514   15.822  1.00 15.78 ?  89  ALA   A O    1 
ATOM   1863 C  CB   . ALA   A 1 89  ? 25.750 -1.124  14.300  1.00 14.04 ?  89  ALA   A CB   1 
ATOM   1864 H  H    . ALA   A 1 89  ? 26.373 1.509   15.479  1.00 17.59 ?  89  ALA   A H    1 
ATOM   1865 H  HA   . ALA   A 1 89  ? 25.519 -0.838  16.336  1.00 17.48 ?  89  ALA   A HA   1 
ATOM   1866 H  HB1  . ALA   A 1 89  ? 25.992 -2.061  14.387  1.00 16.82 ?  89  ALA   A HB1  1 
ATOM   1867 H  HB2  . ALA   A 1 89  ? 24.804 -1.048  14.088  1.00 16.82 ?  89  ALA   A HB2  1 
ATOM   1868 H  HB3  . ALA   A 1 89  ? 26.279 -0.710  13.602  1.00 16.82 ?  89  ALA   A HB3  1 
ATOM   1869 N  N    . LYS   A 1 90  ? 27.990 -1.660  16.334  1.00 15.85 ?  90  LYS   A N    1 
ATOM   1870 C  CA   . LYS   A 1 90  ? 29.434 -1.816  16.481  1.00 16.32 ?  90  LYS   A CA   1 
ATOM   1871 C  C    . LYS   A 1 90  ? 30.135 -1.626  15.139  1.00 15.08 ?  90  LYS   A C    1 
ATOM   1872 O  O    . LYS   A 1 90  ? 31.073 -0.818  15.013  1.00 16.64 ?  90  LYS   A O    1 
ATOM   1873 C  CB   . LYS   A 1 90  ? 29.764 -3.178  17.093  1.00 19.16 ?  90  LYS   A CB   1 
ATOM   1874 C  CG   . LYS   A 1 90  ? 31.240 -3.335  17.431  1.00 24.01 ?  90  LYS   A CG   1 
ATOM   1875 C  CD   . LYS   A 1 90  ? 31.490 -4.578  18.272  1.00 29.20 ?  90  LYS   A CD   1 
ATOM   1876 C  CE   . LYS   A 1 90  ? 32.907 -4.606  18.831  1.00 33.32 ?  90  LYS   A CE   1 
ATOM   1877 N  NZ   . LYS   A 1 90  ? 33.927 -4.997  17.818  1.00 35.42 ?  90  LYS   A NZ   1 
ATOM   1878 H  H    . LYS   A 1 90  ? 27.513 -2.349  16.527  1.00 18.99 ?  90  LYS   A H    1 
ATOM   1879 H  HA   . LYS   A 1 90  ? 29.760 -1.134  17.084  1.00 19.55 ?  90  LYS   A HA   1 
ATOM   1880 H  HB2  . LYS   A 1 90  ? 29.254 -3.289  17.914  1.00 22.97 ?  90  LYS   A HB2  1 
ATOM   1881 H  HB3  . LYS   A 1 90  ? 29.524 -3.877  16.463  1.00 22.97 ?  90  LYS   A HB3  1 
ATOM   1882 H  HG2  . LYS   A 1 90  ? 31.749 -3.416  16.610  1.00 28.78 ?  90  LYS   A HG2  1 
ATOM   1883 H  HG3  . LYS   A 1 90  ? 31.536 -2.561  17.936  1.00 28.78 ?  90  LYS   A HG3  1 
ATOM   1884 H  HD2  . LYS   A 1 90  ? 30.870 -4.591  19.018  1.00 35.00 ?  90  LYS   A HD2  1 
ATOM   1885 H  HD3  . LYS   A 1 90  ? 31.366 -5.367  17.721  1.00 35.00 ?  90  LYS   A HD3  1 
ATOM   1886 H  HE2  . LYS   A 1 90  ? 33.135 -3.721  19.157  1.00 39.95 ?  90  LYS   A HE2  1 
ATOM   1887 H  HE3  . LYS   A 1 90  ? 32.947 -5.247  19.558  1.00 39.95 ?  90  LYS   A HE3  1 
ATOM   1888 H  HZ1  . LYS   A 1 90  ? 34.736 -5.015  18.191  1.00 42.47 ?  90  LYS   A HZ1  1 
ATOM   1889 H  HZ2  . LYS   A 1 90  ? 33.741 -5.806  17.496  1.00 42.47 ?  90  LYS   A HZ2  1 
ATOM   1890 H  HZ3  . LYS   A 1 90  ? 33.931 -4.413  17.148  1.00 42.47 ?  90  LYS   A HZ3  1 
ATOM   1891 N  N    . HIS   A 1 91  ? 29.663 -2.341  14.115  1.00 13.45 ?  91  HIS   A N    1 
ATOM   1892 C  CA   . HIS   A 1 91  ? 30.239 -2.327  12.786  1.00 13.03 ?  91  HIS   A CA   1 
ATOM   1893 C  C    . HIS   A 1 91  ? 29.154 -2.050  11.762  1.00 11.74 ?  91  HIS   A C    1 
ATOM   1894 O  O    . HIS   A 1 91  ? 27.991 -2.417  11.953  1.00 12.43 ?  91  HIS   A O    1 
ATOM   1895 C  CB   . HIS   A 1 91  ? 30.835 -3.693  12.422  1.00 15.42 ?  91  HIS   A CB   1 
ATOM   1896 C  CG   . HIS   A 1 91  ? 31.834 -4.208  13.407  1.00 20.01 ?  91  HIS   A CG   1 
ATOM   1897 N  ND1  . HIS   A 1 91  ? 33.113 -3.706  13.503  1.00 22.16 ?  91  HIS   A ND1  1 
ATOM   1898 C  CD2  . HIS   A 1 91  ? 31.750 -5.201  14.324  1.00 21.81 ?  91  HIS   A CD2  1 
ATOM   1899 C  CE1  . HIS   A 1 91  ? 33.772 -4.358  14.445  1.00 22.98 ?  91  HIS   A CE1  1 
ATOM   1900 N  NE2  . HIS   A 1 91  ? 32.967 -5.273  14.958  1.00 23.15 ?  91  HIS   A NE2  1 
ATOM   1901 H  H    . HIS   A 1 91  ? 28.981 -2.879  14.181  1.00 16.11 ?  91  HIS   A H    1 
ATOM   1902 H  HA   . HIS   A 1 91  ? 30.927 -1.649  12.726  1.00 15.60 ?  91  HIS   A HA   1 
ATOM   1903 H  HB2  . HIS   A 1 91  ? 30.117 -4.342  12.366  1.00 18.47 ?  91  HIS   A HB2  1 
ATOM   1904 H  HB3  . HIS   A 1 91  ? 31.279 -3.618  11.563  1.00 18.47 ?  91  HIS   A HB3  1 
ATOM   1905 H  HD1  . HIS   A 1 91  ? 33.434 -3.065  13.024  1.00 26.57 ?  91  HIS   A HD1  1 
ATOM   1906 H  HD2  . HIS   A 1 91  ? 31.010 -5.729  14.499  1.00 26.15 ?  91  HIS   A HD2  1 
ATOM   1907 H  HE1  . HIS   A 1 91  ? 34.656 -4.199  14.700  1.00 27.54 ?  91  HIS   A HE1  1 
ATOM   1908 N  N    . CYS   A 1 92  ? 29.562 -1.458  10.645  1.00 11.50 ?  92  CYS   A N    1 
ATOM   1909 C  CA   . CYS   A 1 92  ? 28.727 -1.379  9.457   1.00 10.87 ?  92  CYS   A CA   1 
ATOM   1910 C  C    . CYS   A 1 92  ? 29.373 -2.201  8.351   1.00 10.57 ?  92  CYS   A C    1 
ATOM   1911 O  O    . CYS   A 1 92  ? 30.533 -1.955  7.988   1.00 11.61 ?  92  CYS   A O    1 
ATOM   1912 C  CB   . CYS   A 1 92  ? 28.520 0.064   8.996   1.00 11.88 ?  92  CYS   A CB   1 
ATOM   1913 S  SG   . CYS   A 1 92  ? 27.502 0.174   7.493   1.00 11.21 ?  92  CYS   A SG   1 
ATOM   1914 H  H    . CYS   A 1 92  ? 30.335 -1.080  10.554  1.00 13.77 ?  92  CYS   A H    1 
ATOM   1915 H  HA   . CYS   A 1 92  ? 27.862 -1.763  9.650   1.00 13.01 ?  92  CYS   A HA   1 
ATOM   1916 H  HB2  . CYS   A 1 92  ? 28.068 0.560   9.697   1.00 14.23 ?  92  CYS   A HB2  1 
ATOM   1917 H  HB3  . CYS   A 1 92  ? 29.379 0.466   8.802   1.00 14.23 ?  92  CYS   A HB3  1 
ATOM   1918 H  HG   . CYS   A 1 92  ? 27.365 1.322   7.198   1.00 13.42 ?  92  CYS   A HG   1 
ATOM   1919 N  N    . LEU   A 1 93  ? 28.636 -3.187  7.848   1.00 10.72 ?  93  LEU   A N    1 
ATOM   1920 C  CA   . LEU   A 1 93  ? 29.043 -3.948  6.674   1.00 10.18 ?  93  LEU   A CA   1 
ATOM   1921 C  C    . LEU   A 1 93  ? 28.445 -3.256  5.455   1.00 9.79  ?  93  LEU   A C    1 
ATOM   1922 O  O    . LEU   A 1 93  ? 27.229 -3.315  5.229   1.00 9.94  ?  93  LEU   A O    1 
ATOM   1923 C  CB   . LEU   A 1 93  ? 28.562 -5.394  6.783   1.00 10.80 ?  93  LEU   A CB   1 
ATOM   1924 C  CG   . LEU   A 1 93  ? 28.951 -6.290  5.609   1.00 11.23 ?  93  LEU   A CG   1 
ATOM   1925 C  CD1  . LEU   A 1 93  ? 30.457 -6.555  5.587   1.00 12.23 ?  93  LEU   A CD1  1 
ATOM   1926 C  CD2  . LEU   A 1 93  ? 28.178 -7.608  5.646   1.00 12.11 ?  93  LEU   A CD2  1 
ATOM   1927 H  H    . LEU   A 1 93  ? 27.881 -3.438  8.179   1.00 12.83 ?  93  LEU   A H    1 
ATOM   1928 H  HA   . LEU   A 1 93  ? 30.005 -3.939  6.598   1.00 12.19 ?  93  LEU   A HA   1 
ATOM   1929 H  HB2  . LEU   A 1 93  ? 28.943 -5.781  7.591   1.00 12.93 ?  93  LEU   A HB2  1 
ATOM   1930 H  HB3  . LEU   A 1 93  ? 27.597 -5.399  6.847   1.00 12.93 ?  93  LEU   A HB3  1 
ATOM   1931 H  HG   . LEU   A 1 93  ? 28.732 -5.843  4.785   1.00 13.45 ?  93  LEU   A HG   1 
ATOM   1932 H  HD11 . LEU   A 1 93  ? 30.664 -7.165  4.863   1.00 14.64 ?  93  LEU   A HD11 1 
ATOM   1933 H  HD12 . LEU   A 1 93  ? 30.928 -5.719  5.463   1.00 14.64 ?  93  LEU   A HD12 1 
ATOM   1934 H  HD13 . LEU   A 1 93  ? 30.723 -6.958  6.436   1.00 14.64 ?  93  LEU   A HD13 1 
ATOM   1935 H  HD21 . LEU   A 1 93  ? 28.451 -8.156  4.890   1.00 14.50 ?  93  LEU   A HD21 1 
ATOM   1936 H  HD22 . LEU   A 1 93  ? 28.372 -8.072  6.475   1.00 14.50 ?  93  LEU   A HD22 1 
ATOM   1937 H  HD23 . LEU   A 1 93  ? 27.229 -7.416  5.587   1.00 14.50 ?  93  LEU   A HD23 1 
ATOM   1938 N  N    . HIS   A 1 94  ? 29.293 -2.563  4.697   1.00 9.62  ?  94  HIS   A N    1 
ATOM   1939 C  CA   . HIS   A 1 94  ? 28.872 -1.890  3.472   1.00 9.76  ?  94  HIS   A CA   1 
ATOM   1940 C  C    . HIS   A 1 94  ? 28.884 -2.923  2.358   1.00 10.03 ?  94  HIS   A C    1 
ATOM   1941 O  O    . HIS   A 1 94  ? 29.952 -3.442  2.017   1.00 11.40 ?  94  HIS   A O    1 
ATOM   1942 C  CB   . HIS   A 1 94  ? 29.835 -0.749  3.142   1.00 10.09 ?  94  HIS   A CB   1 
ATOM   1943 C  CG   . HIS   A 1 94  ? 29.820 0.345   4.154   1.00 9.94  ?  94  HIS   A CG   1 
ATOM   1944 N  ND1  . HIS   A 1 94  ? 28.946 1.410   4.090   1.00 9.84  ?  94  HIS   A ND1  1 
ATOM   1945 C  CD2  . HIS   A 1 94  ? 30.548 0.514   5.279   1.00 10.92 ?  94  HIS   A CD2  1 
ATOM   1946 C  CE1  . HIS   A 1 94  ? 29.152 2.193   5.132   1.00 10.19 ?  94  HIS   A CE1  1 
ATOM   1947 N  NE2  . HIS   A 1 94  ? 30.118 1.674   5.868   1.00 10.61 ?  94  HIS   A NE2  1 
ATOM   1948 H  H    . HIS   A 1 94  ? 30.132 -2.464  4.871   1.00 11.52 ?  94  HIS   A H    1 
ATOM   1949 H  HA   . HIS   A 1 94  ? 27.972 -1.537  3.571   1.00 11.69 ?  94  HIS   A HA   1 
ATOM   1950 H  HB2  . HIS   A 1 94  ? 30.733 -1.102  3.097   1.00 12.08 ?  94  HIS   A HB2  1 
ATOM   1951 H  HB3  . HIS   A 1 94  ? 29.583 -0.366  2.285   1.00 12.08 ?  94  HIS   A HB3  1 
ATOM   1952 H  HD2  . HIS   A 1 94  ? 31.215 -0.044  5.595   1.00 13.08 ?  94  HIS   A HD2  1 
ATOM   1953 H  HE1  . HIS   A 1 94  ? 28.685 2.983   5.308   1.00 12.20 ?  94  HIS   A HE1  1 
ATOM   1954 H  HE2  . HIS   A 1 94  ? 30.421 2.017   6.592   1.00 12.70 ?  94  HIS   A HE2  1 
ATOM   1955 N  N    . VAL   A 1 95  ? 27.713 -3.246  1.809   1.00 9.14  ?  95  VAL   A N    1 
ATOM   1956 C  CA   . VAL   A 1 95  ? 27.570 -4.280  0.788   1.00 9.86  ?  95  VAL   A CA   1 
ATOM   1957 C  C    . VAL   A 1 95  ? 27.019 -3.643  -0.475  1.00 9.12  ?  95  VAL   A C    1 
ATOM   1958 O  O    . VAL   A 1 95  ? 26.009 -2.928  -0.424  1.00 10.09 ?  95  VAL   A O    1 
ATOM   1959 C  CB   . VAL   A 1 95  ? 26.645 -5.424  1.240   1.00 10.16 ?  95  VAL   A CB   1 
ATOM   1960 C  CG1  . VAL   A 1 95  ? 26.548 -6.475  0.139   1.00 10.89 ?  95  VAL   A CG1  1 
ATOM   1961 C  CG2  . VAL   A 1 95  ? 27.147 -6.034  2.526   1.00 10.35 ?  95  VAL   A CG2  1 
ATOM   1962 H  H    . VAL   A 1 95  ? 26.962 -2.877  2.020   1.00 10.94 ?  95  VAL   A H    1 
ATOM   1963 H  HA   . VAL   A 1 95  ? 28.437 -4.655  0.582   1.00 11.81 ?  95  VAL   A HA   1 
ATOM   1964 H  HB   . VAL   A 1 95  ? 25.757 -5.078  1.400   1.00 12.17 ?  95  VAL   A HB   1 
ATOM   1965 H  HG11 . VAL   A 1 95  ? 26.162 -7.288  0.508   1.00 13.04 ?  95  VAL   A HG11 1 
ATOM   1966 H  HG12 . VAL   A 1 95  ? 25.987 -6.141  -0.576  1.00 13.04 ?  95  VAL   A HG12 1 
ATOM   1967 H  HG13 . VAL   A 1 95  ? 27.440 -6.665  -0.199  1.00 13.04 ?  95  VAL   A HG13 1 
ATOM   1968 H  HG21 . VAL   A 1 95  ? 26.591 -6.796  2.753   1.00 12.39 ?  95  VAL   A HG21 1 
ATOM   1969 H  HG22 . VAL   A 1 95  ? 28.065 -6.316  2.407   1.00 12.39 ?  95  VAL   A HG22 1 
ATOM   1970 H  HG23 . VAL   A 1 95  ? 27.092 -5.367  3.230   1.00 12.39 ?  95  VAL   A HG23 1 
ATOM   1971 N  N    . VAL   A 1 96  ? 27.650 -3.937  -1.612  1.00 9.28  ?  96  VAL   A N    1 
ATOM   1972 C  CA   . VAL   A 1 96  ? 27.239 -3.387  -2.898  1.00 10.03 ?  96  VAL   A CA   1 
ATOM   1973 C  C    . VAL   A 1 96  ? 26.435 -4.442  -3.650  1.00 10.40 ?  96  VAL   A C    1 
ATOM   1974 O  O    . VAL   A 1 96  ? 26.993 -5.380  -4.224  1.00 11.39 ?  96  VAL   A O    1 
ATOM   1975 C  CB   . VAL   A 1 96  ? 28.431 -2.905  -3.724  1.00 10.65 ?  96  VAL   A CB   1 
ATOM   1976 C  CG1  . VAL   A 1 96  ? 27.924 -2.263  -4.996  1.00 10.62 ?  96  VAL   A CG1  1 
ATOM   1977 C  CG2  . VAL   A 1 96  ? 29.292 -1.946  -2.928  1.00 11.08 ?  96  VAL   A CG2  1 
ATOM   1978 H  H    . VAL   A 1 96  ? 28.339 -4.457  -1.664  1.00 11.11 ?  96  VAL   A H    1 
ATOM   1979 H  HA   . VAL   A 1 96  ? 26.663 -2.624  -2.741  1.00 12.01 ?  96  VAL   A HA   1 
ATOM   1980 H  HB   . VAL   A 1 96  ? 28.976 -3.667  -3.970  1.00 12.75 ?  96  VAL   A HB   1 
ATOM   1981 H  HG11 . VAL   A 1 96  ? 28.662 -1.797  -5.426  1.00 12.72 ?  96  VAL   A HG11 1 
ATOM   1982 H  HG12 . VAL   A 1 96  ? 27.580 -2.946  -5.588  1.00 12.72 ?  96  VAL   A HG12 1 
ATOM   1983 H  HG13 . VAL   A 1 96  ? 27.225 -1.627  -4.774  1.00 12.72 ?  96  VAL   A HG13 1 
ATOM   1984 H  HG21 . VAL   A 1 96  ? 29.991 -1.593  -3.500  1.00 13.26 ?  96  VAL   A HG21 1 
ATOM   1985 H  HG22 . VAL   A 1 96  ? 28.738 -1.219  -2.598  1.00 13.26 ?  96  VAL   A HG22 1 
ATOM   1986 H  HG23 . VAL   A 1 96  ? 29.689 -2.421  -2.179  1.00 13.26 ?  96  VAL   A HG23 1 
ATOM   1987 N  N    . GLY   A 1 97  ? 25.117 -4.277  -3.681  1.00 10.39 ?  97  GLY   A N    1 
ATOM   1988 C  CA   . GLY   A 1 97  ? 24.303 -5.037  -4.591  1.00 10.91 ?  97  GLY   A CA   1 
ATOM   1989 C  C    . GLY   A 1 97  ? 24.304 -4.384  -5.958  1.00 11.12 ?  97  GLY   A C    1 
ATOM   1990 O  O    . GLY   A 1 97  ? 24.580 -3.188  -6.092  1.00 11.98 ?  97  GLY   A O    1 
ATOM   1991 H  H    . GLY   A 1 97  ? 24.677 -3.727  -3.174  1.00 12.43 ?  97  GLY   A H    1 
ATOM   1992 H  HA2  . GLY   A 1 97  ? 24.654 -5.936  -4.656  1.00 13.07 ?  97  GLY   A HA2  1 
ATOM   1993 H  HA3  . GLY   A 1 97  ? 23.391 -5.079  -4.254  1.00 13.07 ?  97  GLY   A HA3  1 
ATOM   1994 N  N    . PRO   A 1 98  ? 23.978 -5.142  -6.996  1.00 10.99 ?  98  PRO   A N    1 
ATOM   1995 C  CA   . PRO   A 1 98  ? 23.869 -4.547  -8.329  1.00 12.44 ?  98  PRO   A CA   1 
ATOM   1996 C  C    . PRO   A 1 98  ? 22.750 -3.520  -8.400  1.00 12.64 ?  98  PRO   A C    1 
ATOM   1997 O  O    . PRO   A 1 98  ? 21.674 -3.690  -7.817  1.00 12.70 ?  98  PRO   A O    1 
ATOM   1998 C  CB   . PRO   A 1 98  ? 23.578 -5.751  -9.234  1.00 13.03 ?  98  PRO   A CB   1 
ATOM   1999 C  CG   . PRO   A 1 98  ? 22.944 -6.760  -8.325  1.00 12.92 ?  98  PRO   A CG   1 
ATOM   2000 C  CD   . PRO   A 1 98  ? 23.668 -6.583  -7.006  1.00 11.64 ?  98  PRO   A CD   1 
ATOM   2001 H  HA   . PRO   A 1 98  ? 24.709 -4.139  -8.583  1.00 14.89 ?  98  PRO   A HA   1 
ATOM   2002 H  HB2  . PRO   A 1 98  ? 22.965 -5.486  -9.937  1.00 15.60 ?  98  PRO   A HB2  1 
ATOM   2003 H  HB3  . PRO   A 1 98  ? 24.406 -6.090  -9.603  1.00 15.60 ?  98  PRO   A HB3  1 
ATOM   2004 H  HG2  . PRO   A 1 98  ? 21.999 -6.566  -8.231  1.00 15.47 ?  98  PRO   A HG2  1 
ATOM   2005 H  HG3  . PRO   A 1 98  ? 23.083 -7.650  -8.682  1.00 15.47 ?  98  PRO   A HG3  1 
ATOM   2006 H  HD2  . PRO   A 1 98  ? 23.082 -6.819  -6.267  1.00 13.94 ?  98  PRO   A HD2  1 
ATOM   2007 H  HD3  . PRO   A 1 98  ? 24.483 -7.111  -6.993  1.00 13.94 ?  98  PRO   A HD3  1 
ATOM   2008 N  N    A ASN   A 1 99  ? 23.028 -2.403  -9.079  0.72 13.62 ?  99  ASN   A N    1 
ATOM   2009 N  N    B ASN   A 1 99  ? 23.019 -2.475  -9.172  0.28 13.92 ?  99  ASN   A N    1 
ATOM   2010 C  CA   A ASN   A 1 99  ? 22.049 -1.334  -9.278  0.72 14.38 ?  99  ASN   A CA   1 
ATOM   2011 C  CA   B ASN   A 1 99  ? 22.035 -1.468  -9.531  0.28 15.04 ?  99  ASN   A CA   1 
ATOM   2012 C  C    A ASN   A 1 99  ? 21.492 -1.467  -10.692 0.72 15.31 ?  99  ASN   A C    1 
ATOM   2013 C  C    B ASN   A 1 99  ? 21.393 -1.883  -10.850 0.28 15.90 ?  99  ASN   A C    1 
ATOM   2014 O  O    A ASN   A 1 99  ? 22.184 -1.172  -11.673 0.72 16.42 ?  99  ASN   A O    1 
ATOM   2015 O  O    B ASN   A 1 99  ? 22.057 -1.914  -11.891 0.28 15.57 ?  99  ASN   A O    1 
ATOM   2016 C  CB   A ASN   A 1 99  ? 22.672 0.047   -9.052  0.72 14.54 ?  99  ASN   A CB   1 
ATOM   2017 C  CB   B ASN   A 1 99  ? 22.739 -0.127  -9.681  0.28 15.66 ?  99  ASN   A CB   1 
ATOM   2018 C  CG   A ASN   A 1 99  ? 21.631 1.183   -9.041  0.72 14.77 ?  99  ASN   A CG   1 
ATOM   2019 C  CG   B ASN   A 1 99  ? 21.778 1.011   -9.880  0.28 16.17 ?  99  ASN   A CG   1 
ATOM   2020 O  OD1  A ASN   A 1 99  ? 20.620 1.124   -9.743  0.72 15.36 ?  99  ASN   A OD1  1 
ATOM   2021 O  OD1  B ASN   A 1 99  ? 20.780 0.878   -10.583 0.28 16.36 ?  99  ASN   A OD1  1 
ATOM   2022 N  ND2  A ASN   A 1 99  ? 21.892 2.221   -8.250  0.72 15.18 ?  99  ASN   A ND2  1 
ATOM   2023 N  ND2  B ASN   A 1 99  ? 22.069 2.143   -9.252  0.28 16.90 ?  99  ASN   A ND2  1 
ATOM   2024 H  H    A ASN   A 1 99  ? 23.796 -2.238  -9.430  0.72 16.32 ?  99  ASN   A H    1 
ATOM   2025 H  H    B ASN   A 1 99  ? 23.800 -2.320  -9.500  0.28 16.67 ?  99  ASN   A H    1 
ATOM   2026 H  HA   A ASN   A 1 99  ? 21.319 -1.446  -8.643  0.72 17.23 ?  99  ASN   A HA   1 
ATOM   2027 H  HA   B ASN   A 1 99  ? 21.352 -1.410  -8.842  0.28 18.02 ?  99  ASN   A HA   1 
ATOM   2028 H  HB2  A ASN   A 1 99  ? 23.132 0.054   -8.199  0.72 17.42 ?  99  ASN   A HB2  1 
ATOM   2029 H  HB2  B ASN   A 1 99  ? 23.257 0.048   -8.883  0.28 18.76 ?  99  ASN   A HB2  1 
ATOM   2030 H  HB3  A ASN   A 1 99  ? 23.302 0.225   -9.769  0.72 17.42 ?  99  ASN   A HB3  1 
ATOM   2031 H  HB3  B ASN   A 1 99  ? 23.323 -0.169  -10.455 0.28 18.76 ?  99  ASN   A HB3  1 
ATOM   2032 H  HD21 A ASN   A 1 99  ? 21.342 2.882   -8.210  0.72 18.18 ?  99  ASN   A HD21 1 
ATOM   2033 H  HD21 B ASN   A 1 99  ? 21.553 2.824   -9.330  0.28 20.25 ?  99  ASN   A HD21 1 
ATOM   2034 H  HD22 A ASN   A 1 99  ? 22.609 2.229   -7.775  0.72 18.18 ?  99  ASN   A HD22 1 
ATOM   2035 H  HD22 B ASN   A 1 99  ? 22.778 2.194   -8.768  0.28 20.25 ?  99  ASN   A HD22 1 
ATOM   2036 N  N    A VAL   A 1 100 ? 20.242 -1.927  -10.787 0.72 16.37 ?  100 VAL   A N    1 
ATOM   2037 N  N    B VAL   A 1 100 ? 20.098 -2.199  -10.800 0.28 17.21 ?  100 VAL   A N    1 
ATOM   2038 C  CA   A VAL   A 1 100 ? 19.608 -2.123  -12.086 0.72 18.15 ?  100 VAL   A CA   1 
ATOM   2039 C  CA   B VAL   A 1 100 ? 19.369 -2.600  -12.001 0.28 18.47 ?  100 VAL   A CA   1 
ATOM   2040 C  C    A VAL   A 1 100 ? 19.483 -0.803  -12.832 0.72 18.34 ?  100 VAL   A C    1 
ATOM   2041 C  C    B VAL   A 1 100 ? 19.343 -1.467  -13.015 0.28 18.82 ?  100 VAL   A C    1 
ATOM   2042 O  O    A VAL   A 1 100 ? 19.538 -0.771  -14.067 0.72 19.32 ?  100 VAL   A O    1 
ATOM   2043 O  O    B VAL   A 1 100 ? 19.495 -1.691  -14.223 0.28 18.51 ?  100 VAL   A O    1 
ATOM   2044 C  CB   A VAL   A 1 100 ? 18.254 -2.841  -11.914 0.72 19.81 ?  100 VAL   A CB   1 
ATOM   2045 C  CB   B VAL   A 1 100 ? 17.950 -3.060  -11.621 0.28 19.48 ?  100 VAL   A CB   1 
ATOM   2046 C  CG1  A VAL   A 1 100 ? 17.567 -3.042  -13.259 0.72 20.62 ?  100 VAL   A CG1  1 
ATOM   2047 C  CG1  B VAL   A 1 100 ? 17.063 -3.176  -12.853 0.28 19.89 ?  100 VAL   A CG1  1 
ATOM   2048 C  CG2  A VAL   A 1 100 ? 18.469 -4.175  -11.224 0.72 20.71 ?  100 VAL   A CG2  1 
ATOM   2049 C  CG2  B VAL   A 1 100 ? 18.009 -4.375  -10.870 0.28 20.11 ?  100 VAL   A CG2  1 
ATOM   2050 H  H    A VAL   A 1 100 ? 19.739 -2.132  -10.113 0.72 19.61 ?  100 VAL   A H    1 
ATOM   2051 H  H    B VAL   A 1 100 ? 19.623 -2.192  -10.087 0.28 20.62 ?  100 VAL   A H    1 
ATOM   2052 H  HA   A VAL   A 1 100 ? 20.172 -2.696  -12.620 0.72 21.75 ?  100 VAL   A HA   1 
ATOM   2053 H  HA   B VAL   A 1 100 ? 19.824 -3.346  -12.414 0.28 22.14 ?  100 VAL   A HA   1 
ATOM   2054 H  HB   A VAL   A 1 100 ? 17.671 -2.303  -11.356 0.72 23.74 ?  100 VAL   A HB   1 
ATOM   2055 H  HB   B VAL   A 1 100 ? 17.558 -2.400  -11.033 0.28 23.35 ?  100 VAL   A HB   1 
ATOM   2056 H  HG11 A VAL   A 1 100 ? 16.805 -3.632  -13.140 0.72 24.71 ?  100 VAL   A HG11 1 
ATOM   2057 H  HG11 B VAL   A 1 100 ? 16.288 -3.715  -12.629 0.28 23.84 ?  100 VAL   A HG11 1 
ATOM   2058 H  HG12 A VAL   A 1 100 ? 17.267 -2.184  -13.596 0.72 24.71 ?  100 VAL   A HG12 1 
ATOM   2059 H  HG12 B VAL   A 1 100 ? 16.778 -2.289  -13.127 0.28 23.84 ?  100 VAL   A HG12 1 
ATOM   2060 H  HG13 A VAL   A 1 100 ? 18.197 -3.442  -13.879 0.72 24.71 ?  100 VAL   A HG13 1 
ATOM   2061 H  HG13 B VAL   A 1 100 ? 17.565 -3.600  -13.564 0.28 23.84 ?  100 VAL   A HG13 1 
ATOM   2062 H  HG21 A VAL   A 1 100 ? 17.635 -4.669  -11.221 0.72 24.82 ?  100 VAL   A HG21 1 
ATOM   2063 H  HG21 B VAL   A 1 100 ? 17.108 -4.643  -10.635 0.28 24.10 ?  100 VAL   A HG21 1 
ATOM   2064 H  HG22 A VAL   A 1 100 ? 19.148 -4.673  -11.707 0.72 24.82 ?  100 VAL   A HG22 1 
ATOM   2065 H  HG22 B VAL   A 1 100 ? 18.418 -5.043  -11.441 0.28 24.10 ?  100 VAL   A HG22 1 
ATOM   2066 H  HG23 A VAL   A 1 100 ? 18.763 -4.016  -10.313 0.72 24.82 ?  100 VAL   A HG23 1 
ATOM   2067 H  HG23 B VAL   A 1 100 ? 18.540 -4.255  -10.067 0.28 24.10 ?  100 VAL   A HG23 1 
ATOM   2068 N  N    A ASN   A 1 101 ? 19.316 0.303   -12.111 0.72 19.64 ?  101 ASN   A N    1 
ATOM   2069 N  N    B ASN   A 1 101 ? 19.143 -0.234  -12.541 0.28 19.41 ?  101 ASN   A N    1 
ATOM   2070 C  CA   A ASN   A 1 101 ? 19.244 1.594   -12.782 0.72 21.26 ?  101 ASN   A CA   1 
ATOM   2071 C  CA   B ASN   A 1 101 ? 19.046 0.909   -13.443 0.28 19.75 ?  101 ASN   A CA   1 
ATOM   2072 C  C    A ASN   A 1 101 ? 20.595 2.044   -13.341 0.72 23.37 ?  101 ASN   A C    1 
ATOM   2073 C  C    B ASN   A 1 101 ? 20.337 1.115   -14.223 0.28 20.49 ?  101 ASN   A C    1 
ATOM   2074 O  O    A ASN   A 1 101 ? 20.652 3.097   -13.989 0.72 25.25 ?  101 ASN   A O    1 
ATOM   2075 O  O    B ASN   A 1 101 ? 20.307 1.627   -15.348 0.28 20.19 ?  101 ASN   A O    1 
ATOM   2076 C  CB   A ASN   A 1 101 ? 18.604 2.626   -11.848 0.72 21.03 ?  101 ASN   A CB   1 
ATOM   2077 C  CB   B ASN   A 1 101 ? 18.700 2.164   -12.641 0.28 19.24 ?  101 ASN   A CB   1 
ATOM   2078 C  CG   A ASN   A 1 101 ? 17.205 2.203   -11.396 0.72 21.24 ?  101 ASN   A CG   1 
ATOM   2079 C  CG   B ASN   A 1 101 ? 17.543 1.939   -11.681 0.28 18.99 ?  101 ASN   A CG   1 
ATOM   2080 O  OD1  A ASN   A 1 101 ? 16.407 1.702   -12.195 0.72 22.26 ?  101 ASN   A OD1  1 
ATOM   2081 O  OD1  B ASN   A 1 101 ? 16.484 1.439   -12.067 0.28 18.93 ?  101 ASN   A OD1  1 
ATOM   2082 N  ND2  A ASN   A 1 101 ? 16.912 2.381   -10.113 0.72 20.91 ?  101 ASN   A ND2  1 
ATOM   2083 N  ND2  B ASN   A 1 101 ? 17.748 2.286   -10.416 0.28 18.94 ?  101 ASN   A ND2  1 
ATOM   2084 H  H    A ASN   A 1 101 ? 19.234 0.334   -11.255 0.72 23.54 ?  101 ASN   A H    1 
ATOM   2085 H  H    B ASN   A 1 101 ? 19.062 -0.032  -11.708 0.28 23.26 ?  101 ASN   A H    1 
ATOM   2086 H  HA   A ASN   A 1 101 ? 18.654 1.503   -13.541 0.72 25.48 ?  101 ASN   A HA   1 
ATOM   2087 H  HA   B ASN   A 1 101 ? 18.330 0.761   -14.080 0.28 23.67 ?  101 ASN   A HA   1 
ATOM   2088 H  HB2  A ASN   A 1 101 ? 19.156 2.738   -11.060 0.72 25.20 ?  101 ASN   A HB2  1 
ATOM   2089 H  HB2  B ASN   A 1 101 ? 19.474 2.437   -12.121 0.28 23.06 ?  101 ASN   A HB2  1 
ATOM   2090 H  HB3  A ASN   A 1 101 ? 18.525 3.476   -12.320 0.72 25.20 ?  101 ASN   A HB3  1 
ATOM   2091 H  HB3  B ASN   A 1 101 ? 18.449 2.880   -13.252 0.28 23.06 ?  101 ASN   A HB3  1 
ATOM   2092 H  HD21 A ASN   A 1 101 ? 16.135 2.157   -9.817  0.72 25.06 ?  101 ASN   A HD21 1 
ATOM   2093 H  HD21 B ASN   A 1 101 ? 17.124 2.177   -9.836  0.28 22.70 ?  101 ASN   A HD21 1 
ATOM   2094 H  HD22 A ASN   A 1 101 ? 17.489 2.732   -9.584  0.72 25.06 ?  101 ASN   A HD22 1 
ATOM   2095 H  HD22 B ASN   A 1 101 ? 18.501 2.629   -10.179 0.28 22.70 ?  101 ASN   A HD22 1 
ATOM   2096 N  N    A LYS   A 1 102 ? 21.659 1.255   -13.137 0.72 24.73 ?  102 LYS   A N    1 
ATOM   2097 N  N    B LYS   A 1 102 ? 21.474 0.742   -13.641 0.28 21.86 ?  102 LYS   A N    1 
ATOM   2098 C  CA   A LYS   A 1 102 ? 22.952 1.453   -13.783 0.72 25.70 ?  102 LYS   A CA   1 
ATOM   2099 C  CA   B LYS   A 1 102 ? 22.757 0.800   -14.327 0.28 22.67 ?  102 LYS   A CA   1 
ATOM   2100 C  C    A LYS   A 1 102 ? 23.282 0.365   -14.797 0.72 25.91 ?  102 LYS   A C    1 
ATOM   2101 C  C    B LYS   A 1 102 ? 23.032 -0.445  -15.159 0.28 21.85 ?  102 LYS   A C    1 
ATOM   2102 O  O    A LYS   A 1 102 ? 24.352 0.420   -15.408 0.72 26.65 ?  102 LYS   A O    1 
ATOM   2103 O  O    B LYS   A 1 102 ? 24.130 -0.576  -15.709 0.28 20.92 ?  102 LYS   A O    1 
ATOM   2104 C  CB   A LYS   A 1 102 ? 24.076 1.496   -12.740 0.72 27.03 ?  102 LYS   A CB   1 
ATOM   2105 C  CB   B LYS   A 1 102 ? 23.892 0.992   -13.316 0.28 24.48 ?  102 LYS   A CB   1 
ATOM   2106 C  CG   A LYS   A 1 102 ? 23.956 2.600   -11.713 0.72 28.31 ?  102 LYS   A CG   1 
ATOM   2107 C  CG   B LYS   A 1 102 ? 23.960 2.386   -12.718 0.28 26.07 ?  102 LYS   A CG   1 
ATOM   2108 C  CD   A LYS   A 1 102 ? 25.121 2.545   -10.735 0.72 29.71 ?  102 LYS   A CD   1 
ATOM   2109 C  CD   B LYS   A 1 102 ? 24.968 2.462   -11.581 0.28 27.52 ?  102 LYS   A CD   1 
ATOM   2110 C  CE   A LYS   A 1 102 ? 25.039 3.655   -9.703  0.72 30.97 ?  102 LYS   A CE   1 
ATOM   2111 C  CE   B LYS   A 1 102 ? 25.101 3.885   -11.058 0.28 28.58 ?  102 LYS   A CE   1 
ATOM   2112 N  NZ   A LYS   A 1 102 ? 26.140 3.551   -8.702  0.72 31.51 ?  102 LYS   A NZ   1 
ATOM   2113 N  NZ   B LYS   A 1 102 ? 25.732 3.938   -9.710  0.28 29.18 ?  102 LYS   A NZ   1 
ATOM   2114 H  H    A LYS   A 1 102 ? 21.651 0.565   -12.621 0.72 29.65 ?  102 LYS   A H    1 
ATOM   2115 H  H    B LYS   A 1 102 ? 21.524 0.452   -12.833 0.28 26.20 ?  102 LYS   A H    1 
ATOM   2116 H  HA   A LYS   A 1 102 ? 22.948 2.296   -14.252 0.72 30.82 ?  102 LYS   A HA   1 
ATOM   2117 H  HA   B LYS   A 1 102 ? 22.758 1.572   -14.914 0.28 27.17 ?  102 LYS   A HA   1 
ATOM   2118 H  HB2  A LYS   A 1 102 ? 24.086 0.651   -12.263 0.72 32.40 ?  102 LYS   A HB2  1 
ATOM   2119 H  HB2  B LYS   A 1 102 ? 23.771 0.363   -12.589 0.28 29.34 ?  102 LYS   A HB2  1 
ATOM   2120 H  HB3  A LYS   A 1 102 ? 24.921 1.616   -13.203 0.72 32.40 ?  102 LYS   A HB3  1 
ATOM   2121 H  HB3  B LYS   A 1 102 ? 24.736 0.820   -13.761 0.28 29.34 ?  102 LYS   A HB3  1 
ATOM   2122 H  HG2  A LYS   A 1 102 ? 23.969 3.459   -12.163 0.72 33.94 ?  102 LYS   A HG2  1 
ATOM   2123 H  HG2  B LYS   A 1 102 ? 24.232 3.016   -13.405 0.28 31.26 ?  102 LYS   A HG2  1 
ATOM   2124 H  HG3  A LYS   A 1 102 ? 23.130 2.488   -11.218 0.72 33.94 ?  102 LYS   A HG3  1 
ATOM   2125 H  HG3  B LYS   A 1 102 ? 23.089 2.628   -12.367 0.28 31.26 ?  102 LYS   A HG3  1 
ATOM   2126 H  HD2  A LYS   A 1 102 ? 25.107 1.694   -10.269 0.72 35.62 ?  102 LYS   A HD2  1 
ATOM   2127 H  HD2  B LYS   A 1 102 ? 24.673 1.894   -10.851 0.28 32.99 ?  102 LYS   A HD2  1 
ATOM   2128 H  HD3  A LYS   A 1 102 ? 25.953 2.644   -11.225 0.72 35.62 ?  102 LYS   A HD3  1 
ATOM   2129 H  HD3  B LYS   A 1 102 ? 25.837 2.172   -11.902 0.28 32.99 ?  102 LYS   A HD3  1 
ATOM   2130 H  HE2  A LYS   A 1 102 ? 25.114 4.513   -10.152 0.72 37.14 ?  102 LYS   A HE2  1 
ATOM   2131 H  HE2  B LYS   A 1 102 ? 25.654 4.397   -11.670 0.28 34.27 ?  102 LYS   A HE2  1 
ATOM   2132 H  HE3  A LYS   A 1 102 ? 24.191 3.594   -9.236  0.72 37.14 ?  102 LYS   A HE3  1 
ATOM   2133 H  HE3  B LYS   A 1 102 ? 24.219 4.283   -10.995 0.28 34.27 ?  102 LYS   A HE3  1 
ATOM   2134 H  HZ1  A LYS   A 1 102 ? 26.073 4.209   -8.109  0.72 37.78 ?  102 LYS   A HZ1  1 
ATOM   2135 H  HZ1  B LYS   A 1 102 ? 25.793 4.783   -9.435  0.28 34.99 ?  102 LYS   A HZ1  1 
ATOM   2136 H  HZ2  A LYS   A 1 102 ? 26.089 2.770   -8.277  0.72 37.78 ?  102 LYS   A HZ2  1 
ATOM   2137 H  HZ2  B LYS   A 1 102 ? 25.240 3.480   -9.126  0.28 34.99 ?  102 LYS   A HZ2  1 
ATOM   2138 H  HZ3  A LYS   A 1 102 ? 26.928 3.607   -9.111  0.72 37.78 ?  102 LYS   A HZ3  1 
ATOM   2139 H  HZ3  B LYS   A 1 102 ? 26.548 3.584   -9.741  0.28 34.99 ?  102 LYS   A HZ3  1 
ATOM   2140 N  N    A GLY   A 1 103 ? 22.413 -0.629  -14.975 0.72 26.46 ?  103 GLY   A N    1 
ATOM   2141 N  N    B GLY   A 1 103 ? 22.076 -1.368  -15.248 0.28 21.97 ?  103 GLY   A N    1 
ATOM   2142 C  CA   A GLY   A 1 103 ? 22.669 -1.705  -15.916 0.72 26.28 ?  103 GLY   A CA   1 
ATOM   2143 C  CA   B GLY   A 1 103 ? 22.279 -2.566  -16.035 0.28 21.70 ?  103 GLY   A CA   1 
ATOM   2144 C  C    A GLY   A 1 103 ? 23.513 -2.843  -15.387 0.72 26.66 ?  103 GLY   A C    1 
ATOM   2145 C  C    B GLY   A 1 103 ? 23.230 -3.568  -15.426 0.28 21.21 ?  103 GLY   A C    1 
ATOM   2146 O  O    A GLY   A 1 103 ? 24.129 -3.559  -16.182 0.72 27.81 ?  103 GLY   A O    1 
ATOM   2147 O  O    B GLY   A 1 103 ? 23.675 -4.484  -16.125 0.28 21.00 ?  103 GLY   A O    1 
ATOM   2148 H  H    A GLY   A 1 103 ? 21.669 -0.709  -14.557 0.72 31.72 ?  103 GLY   A H    1 
ATOM   2149 H  H    B GLY   A 1 103 ? 21.308 -1.324  -14.855 0.28 26.34 ?  103 GLY   A H    1 
ATOM   2150 H  HA2  A GLY   A 1 103 ? 21.820 -2.071  -16.220 0.72 31.51 ?  103 GLY   A HA2  1 
ATOM   2151 H  HA2  B GLY   A 1 103 ? 21.428 -3.005  -16.167 0.28 26.00 ?  103 GLY   A HA2  1 
ATOM   2152 H  HA3  A GLY   A 1 103 ? 23.129 -1.348  -16.691 0.72 31.51 ?  103 GLY   A HA3  1 
ATOM   2153 H  HA3  B GLY   A 1 103 ? 22.626 -2.311  -16.905 0.28 26.00 ?  103 GLY   A HA3  1 
ATOM   2154 N  N    A GLU   A 1 104 ? 23.559 -3.044  -14.074 0.72 25.08 ?  104 GLU   A N    1 
ATOM   2155 N  N    B GLU   A 1 104 ? 23.557 -3.426  -14.145 0.28 21.10 ?  104 GLU   A N    1 
ATOM   2156 C  CA   A GLU   A 1 104 ? 24.431 -4.050  -13.482 0.72 23.45 ?  104 GLU   A CA   1 
ATOM   2157 C  CA   B GLU   A 1 104 ? 24.492 -4.340  -13.505 0.28 20.98 ?  104 GLU   A CA   1 
ATOM   2158 C  C    A GLU   A 1 104 ? 23.738 -5.409  -13.388 0.72 23.64 ?  104 GLU   A C    1 
ATOM   2159 C  C    B GLU   A 1 104 ? 23.845 -5.707  -13.295 0.28 21.24 ?  104 GLU   A C    1 
ATOM   2160 O  O    A GLU   A 1 104 ? 22.511 -5.503  -13.289 0.72 23.97 ?  104 GLU   A O    1 
ATOM   2161 O  O    B GLU   A 1 104 ? 22.672 -5.813  -12.922 0.28 20.90 ?  104 GLU   A O    1 
ATOM   2162 C  CB   A GLU   A 1 104 ? 24.934 -3.568  -12.118 0.72 21.31 ?  104 GLU   A CB   1 
ATOM   2163 C  CB   B GLU   A 1 104 ? 24.979 -3.740  -12.185 0.28 20.77 ?  104 GLU   A CB   1 
ATOM   2164 C  CG   A GLU   A 1 104 ? 25.864 -2.359  -12.277 0.72 20.37 ?  104 GLU   A CG   1 
ATOM   2165 C  CG   B GLU   A 1 104 ? 25.739 -2.427  -12.381 0.28 20.95 ?  104 GLU   A CG   1 
ATOM   2166 C  CD   A GLU   A 1 104 ? 26.214 -1.609  -10.997 0.72 19.33 ?  104 GLU   A CD   1 
ATOM   2167 C  CD   B GLU   A 1 104 ? 26.050 -1.711  -11.080 0.28 21.02 ?  104 GLU   A CD   1 
ATOM   2168 O  OE1  A GLU   A 1 104 ? 25.599 -1.849  -9.935  0.72 17.59 ?  104 GLU   A OE1  1 
ATOM   2169 O  OE1  B GLU   A 1 104 ? 25.696 -2.231  -10.002 0.28 21.22 ?  104 GLU   A OE1  1 
ATOM   2170 O  OE2  A GLU   A 1 104 ? 27.119 -0.743  -11.082 0.72 20.10 -1 104 GLU   A OE2  1 
ATOM   2171 O  OE2  B GLU   A 1 104 ? 26.644 -0.613  -11.139 0.28 21.00 -1 104 GLU   A OE2  1 
ATOM   2172 H  H    A GLU   A 1 104 ? 23.094 -2.601  -13.500 0.72 30.06 ?  104 GLU   A H    1 
ATOM   2173 H  H    B GLU   A 1 104 ? 23.254 -2.804  -13.629 0.28 25.29 ?  104 GLU   A H    1 
ATOM   2174 H  HA   A GLU   A 1 104 ? 25.202 -4.156  -14.058 0.72 28.11 ?  104 GLU   A HA   1 
ATOM   2175 H  HA   B GLU   A 1 104 ? 25.266 -4.454  -14.081 0.28 25.15 ?  104 GLU   A HA   1 
ATOM   2176 H  HB2  A GLU   A 1 104 ? 24.177 -3.308  -11.573 0.72 25.54 ?  104 GLU   A HB2  1 
ATOM   2177 H  HB2  B GLU   A 1 104 ? 24.216 -3.555  -11.614 0.28 24.90 ?  104 GLU   A HB2  1 
ATOM   2178 H  HB3  A GLU   A 1 104 ? 25.429 -4.285  -11.693 0.72 25.54 ?  104 GLU   A HB3  1 
ATOM   2179 H  HB3  B GLU   A 1 104 ? 25.578 -4.365  -11.748 0.28 24.90 ?  104 GLU   A HB3  1 
ATOM   2180 H  HG2  A GLU   A 1 104 ? 26.697 -2.665  -12.661 0.72 24.42 ?  104 GLU   A HG2  1 
ATOM   2181 H  HG2  B GLU   A 1 104 ? 26.579 -2.611  -12.836 0.28 25.11 ?  104 GLU   A HG2  1 
ATOM   2182 H  HG3  A GLU   A 1 104 ? 25.440 -1.725  -12.875 0.72 24.42 ?  104 GLU   A HG3  1 
ATOM   2183 H  HG3  B GLU   A 1 104 ? 25.203 -1.825  -12.922 0.28 25.11 ?  104 GLU   A HG3  1 
ATOM   2184 N  N    A ASP   A 1 105 ? 24.551 -6.466  -13.419 0.72 24.54 ?  105 ASP   A N    1 
ATOM   2185 N  N    B ASP   A 1 105 ? 24.626 -6.755  -13.548 0.28 22.09 ?  105 ASP   A N    1 
ATOM   2186 C  CA   A ASP   A 1 105 ? 24.060 -7.832  -13.574 0.72 25.74 ?  105 ASP   A CA   1 
ATOM   2187 C  CA   B ASP   A 1 105 ? 24.149 -8.134  -13.545 0.28 22.97 ?  105 ASP   A CA   1 
ATOM   2188 C  C    A ASP   A 1 105 ? 23.383 -8.312  -12.292 0.72 23.41 ?  105 ASP   A C    1 
ATOM   2189 C  C    B ASP   A 1 105 ? 23.441 -8.475  -12.242 0.28 22.74 ?  105 ASP   A C    1 
ATOM   2190 O  O    A ASP   A 1 105 ? 24.018 -8.388  -11.238 0.72 21.08 ?  105 ASP   A O    1 
ATOM   2191 O  O    B ASP   A 1 105 ? 24.056 -8.485  -11.172 0.28 22.24 ?  105 ASP   A O    1 
ATOM   2192 C  CB   A ASP   A 1 105 ? 25.237 -8.742  -13.923 0.72 29.12 ?  105 ASP   A CB   1 
ATOM   2193 C  CB   B ASP   A 1 105 ? 25.357 -9.054  -13.742 0.28 24.01 ?  105 ASP   A CB   1 
ATOM   2194 C  CG   A ASP   A 1 105 ? 24.810 -10.158 -14.235 0.72 31.91 ?  105 ASP   A CG   1 
ATOM   2195 C  CG   B ASP   A 1 105 ? 24.993 -10.527 -13.731 0.28 24.80 ?  105 ASP   A CG   1 
ATOM   2196 O  OD1  A ASP   A 1 105 ? 23.590 -10.404 -14.311 0.72 32.67 ?  105 ASP   A OD1  1 
ATOM   2197 O  OD1  B ASP   A 1 105 ? 23.793 -10.857 -13.836 0.28 24.69 ?  105 ASP   A OD1  1 
ATOM   2198 O  OD2  A ASP   A 1 105 ? 25.698 -11.021 -14.411 0.72 33.35 -1 105 ASP   A OD2  1 
ATOM   2199 O  OD2  B ASP   A 1 105 ? 25.920 -11.359 -13.611 0.28 25.46 -1 105 ASP   A OD2  1 
ATOM   2200 H  H    A ASP   A 1 105 ? 25.408 -6.415  -13.349 0.72 29.42 ?  105 ASP   A H    1 
ATOM   2201 H  H    B ASP   A 1 105 ? 25.458 -6.681  -13.732 0.28 26.47 ?  105 ASP   A H    1 
ATOM   2202 H  HA   A ASP   A 1 105 ? 23.415 -7.872  -14.296 0.72 30.86 ?  105 ASP   A HA   1 
ATOM   2203 H  HA   B ASP   A 1 105 ? 23.529 -8.265  -14.278 0.28 27.54 ?  105 ASP   A HA   1 
ATOM   2204 H  HB2  A ASP   A 1 105 ? 25.686 -8.394  -14.710 0.72 34.91 ?  105 ASP   A HB2  1 
ATOM   2205 H  HB2  B ASP   A 1 105 ? 25.769 -8.850  -14.595 0.28 28.79 ?  105 ASP   A HB2  1 
ATOM   2206 H  HB3  A ASP   A 1 105 ? 25.855 -8.764  -13.174 0.72 34.91 ?  105 ASP   A HB3  1 
ATOM   2207 H  HB3  B ASP   A 1 105 ? 25.987 -8.901  -13.022 0.28 28.79 ?  105 ASP   A HB3  1 
ATOM   2208 N  N    A ILE   A 1 106 ? 22.101 -8.672  -12.391 0.72 23.14 ?  106 ILE   A N    1 
ATOM   2209 N  N    B ILE   A 1 106 ? 22.143 -8.776  -12.339 0.28 22.92 ?  106 ILE   A N    1 
ATOM   2210 C  CA   A ILE   A 1 106 ? 21.339 -9.075  -11.215 0.72 22.45 ?  106 ILE   A CA   1 
ATOM   2211 C  CA   B ILE   A 1 106 ? 21.375 -9.138  -11.154 0.28 23.12 ?  106 ILE   A CA   1 
ATOM   2212 C  C    A ILE   A 1 106 ? 21.881 -10.352 -10.593 0.72 21.29 ?  106 ILE   A C    1 
ATOM   2213 C  C    B ILE   A 1 106 ? 21.884 -10.429 -10.532 0.28 22.79 ?  106 ILE   A C    1 
ATOM   2214 O  O    A ILE   A 1 106 ? 21.677 -10.585 -9.398  0.72 20.48 ?  106 ILE   A O    1 
ATOM   2215 O  O    B ILE   A 1 106 ? 21.675 -10.660 -9.336  0.28 22.61 ?  106 ILE   A O    1 
ATOM   2216 C  CB   A ILE   A 1 106 ? 19.832 -9.184  -11.551 0.72 23.99 ?  106 ILE   A CB   1 
ATOM   2217 C  CB   B ILE   A 1 106 ? 19.863 -9.198  -11.472 0.28 24.03 ?  106 ILE   A CB   1 
ATOM   2218 C  CG1  A ILE   A 1 106 ? 18.992 -9.244  -10.272 0.72 24.39 ?  106 ILE   A CG1  1 
ATOM   2219 C  CG1  B ILE   A 1 106 ? 19.039 -9.255  -10.182 0.28 24.40 ?  106 ILE   A CG1  1 
ATOM   2220 C  CG2  A ILE   A 1 106 ? 19.555 -10.407 -12.408 0.72 24.67 ?  106 ILE   A CG2  1 
ATOM   2221 C  CG2  B ILE   A 1 106 ? 19.543 -10.399 -12.346 0.28 24.35 ?  106 ILE   A CG2  1 
ATOM   2222 C  CD1  A ILE   A 1 106 ? 19.081 -7.997  -9.420  0.72 24.76 ?  106 ILE   A CD1  1 
ATOM   2223 C  CD1  B ILE   A 1 106 ? 19.246 -8.067  -9.265  0.28 24.55 ?  106 ILE   A CD1  1 
ATOM   2224 H  H    A ILE   A 1 106 ? 21.661 -8.688  -13.123 0.72 27.74 ?  106 ILE   A H    1 
ATOM   2225 H  H    B ILE   A 1 106 ? 21.692 -8.770  -13.069 0.28 27.47 ?  106 ILE   A H    1 
ATOM   2226 H  HA   A ILE   A 1 106 ? 21.439 -8.389  -10.548 0.72 26.90 ?  106 ILE   A HA   1 
ATOM   2227 H  HA   B ILE   A 1 106 ? 21.507 -8.444  -10.496 0.28 27.71 ?  106 ILE   A HA   1 
ATOM   2228 H  HB   A ILE   A 1 106 ? 19.575 -8.394  -12.050 0.72 28.76 ?  106 ILE   A HB   1 
ATOM   2229 H  HB   B ILE   A 1 106 ? 19.619 -8.393  -11.955 0.28 28.81 ?  106 ILE   A HB   1 
ATOM   2230 H  HG12 A ILE   A 1 106 ? 18.061 -9.365  -10.517 0.72 29.24 ?  106 ILE   A HG12 1 
ATOM   2231 H  HG12 B ILE   A 1 106 ? 18.097 -9.284  -10.414 0.28 29.26 ?  106 ILE   A HG12 1 
ATOM   2232 H  HG13 A ILE   A 1 106 ? 19.290 -9.993  -9.734  0.72 29.24 ?  106 ILE   A HG13 1 
ATOM   2233 H  HG13 B ILE   A 1 106 ? 19.279 -10.054 -9.689  0.28 29.26 ?  106 ILE   A HG13 1 
ATOM   2234 H  HG21 A ILE   A 1 106 ? 18.661 -10.334 -12.776 0.72 29.57 ?  106 ILE   A HG21 1 
ATOM   2235 H  HG21 B ILE   A 1 106 ? 18.639 -10.306 -12.687 0.28 29.19 ?  106 ILE   A HG21 1 
ATOM   2236 H  HG22 A ILE   A 1 106 ? 20.207 -10.441 -13.123 0.72 29.57 ?  106 ILE   A HG22 1 
ATOM   2237 H  HG22 B ILE   A 1 106 ? 20.173 -10.427 -13.081 0.28 29.19 ?  106 ILE   A HG22 1 
ATOM   2238 H  HG23 A ILE   A 1 106 ? 19.623 -11.201 -11.856 0.72 29.57 ?  106 ILE   A HG23 1 
ATOM   2239 H  HG23 B ILE   A 1 106 ? 19.615 -11.206 -11.814 0.28 29.19 ?  106 ILE   A HG23 1 
ATOM   2240 H  HD11 A ILE   A 1 106 ? 18.355 -8.002  -8.779  0.72 29.68 ?  106 ILE   A HD11 1 
ATOM   2241 H  HD11 B ILE   A 1 106 ? 18.517 -8.031  -8.629  0.28 29.44 ?  106 ILE   A HD11 1 
ATOM   2242 H  HD12 A ILE   A 1 106 ? 19.933 -7.992  -8.953  0.72 29.68 ?  106 ILE   A HD12 1 
ATOM   2243 H  HD12 B ILE   A 1 106 ? 20.089 -8.173  -8.796  0.28 29.44 ?  106 ILE   A HD12 1 
ATOM   2244 H  HD13 A ILE   A 1 106 ? 19.013 -7.217  -9.993  0.72 29.68 ?  106 ILE   A HD13 1 
ATOM   2245 H  HD13 B ILE   A 1 106 ? 19.261 -7.257  -9.798  0.28 29.44 ?  106 ILE   A HD13 1 
ATOM   2246 N  N    A GLN   A 1 107 ? 22.581 -11.184 -11.376 0.72 21.86 ?  107 GLN   A N    1 
ATOM   2247 N  N    B GLN   A 1 107 ? 22.560 -11.279 -11.312 0.28 22.85 ?  107 GLN   A N    1 
ATOM   2248 C  CA   A GLN   A 1 107 ? 23.198 -12.388 -10.825 0.72 24.34 ?  107 GLN   A CA   1 
ATOM   2249 C  CA   B GLN   A 1 107 ? 23.195 -12.456 -10.733 0.28 23.22 ?  107 GLN   A CA   1 
ATOM   2250 C  C    A GLN   A 1 107 ? 24.168 -12.054 -9.698  0.72 22.07 ?  107 GLN   A C    1 
ATOM   2251 C  C    B GLN   A 1 107 ? 24.234 -12.082 -9.686  0.28 21.21 ?  107 GLN   A C    1 
ATOM   2252 O  O    A GLN   A 1 107 ? 24.382 -12.874 -8.797  0.72 23.65 ?  107 GLN   A O    1 
ATOM   2253 O  O    B GLN   A 1 107 ? 24.580 -12.920 -8.846  0.28 22.12 ?  107 GLN   A O    1 
ATOM   2254 C  CB   A GLN   A 1 107 ? 23.909 -13.160 -11.943 0.72 28.81 ?  107 GLN   A CB   1 
ATOM   2255 C  CB   B GLN   A 1 107 ? 23.827 -13.316 -11.832 0.28 25.45 ?  107 GLN   A CB   1 
ATOM   2256 C  CG   A GLN   A 1 107 ? 23.062 -13.347 -13.202 0.72 33.57 ?  107 GLN   A CG   1 
ATOM   2257 C  CG   B GLN   A 1 107 ? 22.816 -13.882 -12.814 0.28 27.63 ?  107 GLN   A CG   1 
ATOM   2258 C  CD   A GLN   A 1 107 ? 21.773 -14.099 -12.935 0.72 37.43 ?  107 GLN   A CD   1 
ATOM   2259 C  CD   B GLN   A 1 107 ? 21.709 -14.655 -12.124 0.28 29.59 ?  107 GLN   A CD   1 
ATOM   2260 O  OE1  A GLN   A 1 107 ? 21.779 -15.166 -12.321 0.72 38.91 ?  107 GLN   A OE1  1 
ATOM   2261 O  OE1  B GLN   A 1 107 ? 21.962 -15.447 -11.216 0.28 30.19 ?  107 GLN   A OE1  1 
ATOM   2262 N  NE2  A GLN   A 1 107 ? 20.656 -13.542 -13.390 0.72 38.69 ?  107 GLN   A NE2  1 
ATOM   2263 N  NE2  B GLN   A 1 107 ? 20.472 -14.414 -12.541 0.28 30.16 ?  107 GLN   A NE2  1 
ATOM   2264 H  H    A GLN   A 1 107 ? 22.710 -11.072 -12.216 0.72 26.20 ?  107 GLN   A H    1 
ATOM   2265 H  H    B GLN   A 1 107 ? 22.662 -11.198 -12.163 0.28 27.39 ?  107 GLN   A H    1 
ATOM   2266 H  HA   A GLN   A 1 107 ? 22.516 -12.968 -10.460 0.72 29.18 ?  107 GLN   A HA   1 
ATOM   2267 H  HA   B GLN   A 1 107 ? 22.519 -12.988 -10.292 0.28 27.83 ?  107 GLN   A HA   1 
ATOM   2268 H  HB2  A GLN   A 1 107 ? 24.714 -12.683 -12.201 0.72 34.55 ?  107 GLN   A HB2  1 
ATOM   2269 H  HB2  B GLN   A 1 107 ? 24.458 -12.777 -12.334 0.28 30.51 ?  107 GLN   A HB2  1 
ATOM   2270 H  HB3  A GLN   A 1 107 ? 24.144 -14.046 -11.621 0.72 34.55 ?  107 GLN   A HB3  1 
ATOM   2271 H  HB3  B GLN   A 1 107 ? 24.290 -14.064 -11.421 0.28 30.51 ?  107 GLN   A HB3  1 
ATOM   2272 H  HG2  A GLN   A 1 107 ? 22.833 -12.480 -13.573 0.72 40.25 ?  107 GLN   A HG2  1 
ATOM   2273 H  HG2  B GLN   A 1 107 ? 22.413 -13.151 -13.308 0.28 33.13 ?  107 GLN   A HG2  1 
ATOM   2274 H  HG3  A GLN   A 1 107 ? 23.573 -13.853 -13.851 0.72 40.25 ?  107 GLN   A HG3  1 
ATOM   2275 H  HG3  B GLN   A 1 107 ? 23.269 -14.486 -13.422 0.28 33.13 ?  107 GLN   A HG3  1 
ATOM   2276 H  HE21 A GLN   A 1 107 ? 20.688 -12.795 -13.815 0.72 46.39 ?  107 GLN   A HE21 1 
ATOM   2277 H  HE21 B GLN   A 1 107 ? 20.334 -13.851 -13.176 0.28 36.16 ?  107 GLN   A HE21 1 
ATOM   2278 H  HE22 A GLN   A 1 107 ? 19.900 -13.932 -13.262 0.72 46.39 ?  107 GLN   A HE22 1 
ATOM   2279 H  HE22 B GLN   A 1 107 ? 19.809 -14.823 -12.177 0.28 36.16 ?  107 GLN   A HE22 1 
ATOM   2280 N  N    . LEU   A 1 108 ? 24.730 -10.842 -9.704  1.00 18.52 ?  108 LEU   A N    1 
ATOM   2281 C  CA   . LEU   A 1 108 ? 25.648 -10.412 -8.663  1.00 15.68 ?  108 LEU   A CA   1 
ATOM   2282 C  C    . LEU   A 1 108 ? 24.952 -10.237 -7.323  1.00 13.76 ?  108 LEU   A C    1 
ATOM   2283 O  O    . LEU   A 1 108 ? 25.635 -10.069 -6.311  1.00 14.25 ?  108 LEU   A O    1 
ATOM   2284 C  CB   . LEU   A 1 108 ? 26.363 -9.118  -9.076  1.00 15.29 ?  108 LEU   A CB   1 
ATOM   2285 C  CG   . LEU   A 1 108 ? 27.362 -9.317  -10.217 1.00 17.14 ?  108 LEU   A CG   1 
ATOM   2286 C  CD1  . LEU   A 1 108 ? 27.826 -7.983  -10.780 1.00 17.78 ?  108 LEU   A CD1  1 
ATOM   2287 C  CD2  . LEU   A 1 108 ? 28.562 -10.127 -9.752  1.00 19.08 ?  108 LEU   A CD2  1 
ATOM   2288 H  H    A LEU   A 1 108 ? 24.580 -10.247 -10.300 0.72 22.20 ?  108 LEU   A H    1 
ATOM   2289 H  H    B LEU   A 1 108 ? 24.558 -10.253 -10.300 0.28 22.20 ?  108 LEU   A H    1 
ATOM   2290 H  HA   . LEU   A 1 108 ? 26.324 -11.095 -8.542  1.00 18.79 ?  108 LEU   A HA   1 
ATOM   2291 H  HB2  . LEU   A 1 108 ? 25.702 -8.473  -9.371  1.00 18.32 ?  108 LEU   A HB2  1 
ATOM   2292 H  HB3  . LEU   A 1 108 ? 26.848 -8.770  -8.314  1.00 18.32 ?  108 LEU   A HB3  1 
ATOM   2293 H  HG   . LEU   A 1 108 ? 26.933 -9.811  -10.934 1.00 20.54 ?  108 LEU   A HG   1 
ATOM   2294 H  HD11 . LEU   A 1 108 ? 28.436 -8.144  -11.523 1.00 21.30 ?  108 LEU   A HD11 1 
ATOM   2295 H  HD12 . LEU   A 1 108 ? 27.057 -7.483  -11.092 1.00 21.30 ?  108 LEU   A HD12 1 
ATOM   2296 H  HD13 . LEU   A 1 108 ? 28.286 -7.485  -10.085 1.00 21.30 ?  108 LEU   A HD13 1 
ATOM   2297 H  HD21 . LEU   A 1 108 ? 29.251 -10.090 -10.432 1.00 22.87 ?  108 LEU   A HD21 1 
ATOM   2298 H  HD22 . LEU   A 1 108 ? 28.894 -9.748  -8.923  1.00 22.87 ?  108 LEU   A HD22 1 
ATOM   2299 H  HD23 . LEU   A 1 108 ? 28.287 -11.046 -9.607  1.00 22.87 ?  108 LEU   A HD23 1 
ATOM   2300 N  N    . LEU   A 1 109 ? 23.619 -10.294 -7.283  1.00 13.25 ?  109 LEU   A N    1 
ATOM   2301 C  CA   . LEU   A 1 109 ? 22.925 -10.166 -6.010  1.00 12.57 ?  109 LEU   A CA   1 
ATOM   2302 C  C    . LEU   A 1 109 ? 23.268 -11.319 -5.076  1.00 11.75 ?  109 LEU   A C    1 
ATOM   2303 O  O    . LEU   A 1 109 ? 23.407 -11.126 -3.864  1.00 12.21 ?  109 LEU   A O    1 
ATOM   2304 C  CB   . LEU   A 1 109 ? 21.419 -10.087 -6.257  1.00 13.35 ?  109 LEU   A CB   1 
ATOM   2305 C  CG   . LEU   A 1 109 ? 20.532 -9.795  -5.048  1.00 13.67 ?  109 LEU   A CG   1 
ATOM   2306 C  CD1  . LEU   A 1 109 ? 20.991 -8.527  -4.338  1.00 13.78 ?  109 LEU   A CD1  1 
ATOM   2307 C  CD2  . LEU   A 1 109 ? 19.068 -9.677  -5.471  1.00 14.60 ?  109 LEU   A CD2  1 
ATOM   2308 H  H    . LEU   A 1 109 ? 23.104 -10.402 -7.963  1.00 15.87 ?  109 LEU   A H    1 
ATOM   2309 H  HA   . LEU   A 1 109 ? 23.206 -9.341  -5.582  1.00 15.05 ?  109 LEU   A HA   1 
ATOM   2310 H  HB2  . LEU   A 1 109 ? 21.258 -9.382  -6.903  1.00 15.99 ?  109 LEU   A HB2  1 
ATOM   2311 H  HB3  . LEU   A 1 109 ? 21.128 -10.933 -6.622  1.00 15.99 ?  109 LEU   A HB3  1 
ATOM   2312 H  HG   . LEU   A 1 109 ? 20.601 -10.526 -4.417  1.00 16.38 ?  109 LEU   A HG   1 
ATOM   2313 H  HD11 . LEU   A 1 109 ? 20.312 -8.250  -3.704  1.00 16.51 ?  109 LEU   A HD11 1 
ATOM   2314 H  HD12 . LEU   A 1 109 ? 21.825 -8.701  -3.878  1.00 16.51 ?  109 LEU   A HD12 1 
ATOM   2315 H  HD13 . LEU   A 1 109 ? 21.122 -7.823  -5.002  1.00 16.51 ?  109 LEU   A HD13 1 
ATOM   2316 H  HD21 . LEU   A 1 109 ? 18.543 -9.372  -4.715  1.00 17.49 ?  109 LEU   A HD21 1 
ATOM   2317 H  HD22 . LEU   A 1 109 ? 18.999 -9.043  -6.201  1.00 17.49 ?  109 LEU   A HD22 1 
ATOM   2318 H  HD23 . LEU   A 1 109 ? 18.754 -10.550 -5.761  1.00 17.49 ?  109 LEU   A HD23 1 
ATOM   2319 N  N    . LYS   A 1 110 ? 23.408 -12.532 -5.614  1.00 11.84 ?  110 LYS   A N    1 
ATOM   2320 C  CA   . LYS   A 1 110 ? 23.781 -13.647 -4.754  1.00 11.95 ?  110 LYS   A CA   1 
ATOM   2321 C  C    . LYS   A 1 110 ? 25.165 -13.426 -4.155  1.00 11.35 ?  110 LYS   A C    1 
ATOM   2322 O  O    . LYS   A 1 110 ? 25.368 -13.629 -2.955  1.00 11.78 ?  110 LYS   A O    1 
ATOM   2323 C  CB   . LYS   A 1 110 ? 23.695 -14.972 -5.515  1.00 12.69 ?  110 LYS   A CB   1 
ATOM   2324 C  CG   . LYS   A 1 110 ? 23.910 -16.192 -4.614  1.00 13.19 ?  110 LYS   A CG   1 
ATOM   2325 C  CD   . LYS   A 1 110 ? 23.658 -17.515 -5.332  1.00 13.61 ?  110 LYS   A CD   1 
ATOM   2326 C  CE   . LYS   A 1 110 ? 23.773 -18.708 -4.389  1.00 14.58 ?  110 LYS   A CE   1 
ATOM   2327 N  NZ   . LYS   A 1 110 ? 22.596 -18.824 -3.481  1.00 14.69 ?  110 LYS   A NZ   1 
ATOM   2328 H  H    . LYS   A 1 110 ? 23.294 -12.729 -6.440  1.00 14.17 ?  110 LYS   A H    1 
ATOM   2329 H  HA   . LYS   A 1 110 ? 23.147 -13.695 -4.017  1.00 14.31 ?  110 LYS   A HA   1 
ATOM   2330 H  HB2  . LYS   A 1 110 ? 22.814 -15.049 -5.915  1.00 15.19 ?  110 LYS   A HB2  1 
ATOM   2331 H  HB3  . LYS   A 1 110 ? 24.376 -14.985 -6.202  1.00 15.19 ?  110 LYS   A HB3  1 
ATOM   2332 H  HG2  . LYS   A 1 110 ? 24.825 -16.187 -4.295  1.00 15.80 ?  110 LYS   A HG2  1 
ATOM   2333 H  HG3  . LYS   A 1 110 ? 23.297 -16.134 -3.861  1.00 15.80 ?  110 LYS   A HG3  1 
ATOM   2334 H  HD2  . LYS   A 1 110 ? 22.765 -17.509 -5.706  1.00 16.30 ?  110 LYS   A HD2  1 
ATOM   2335 H  HD3  . LYS   A 1 110 ? 24.317 -17.621 -6.036  1.00 16.30 ?  110 LYS   A HD3  1 
ATOM   2336 H  HE2  . LYS   A 1 110 ? 23.833 -19.522 -4.909  1.00 17.47 ?  110 LYS   A HE2  1 
ATOM   2337 H  HE3  . LYS   A 1 110 ? 24.566 -18.603 -3.837  1.00 17.47 ?  110 LYS   A HE3  1 
ATOM   2338 H  HZ1  . LYS   A 1 110 ? 22.688 -19.525 -2.946  1.00 17.60 ?  110 LYS   A HZ1  1 
ATOM   2339 H  HZ2  . LYS   A 1 110 ? 22.519 -18.086 -2.985  1.00 17.60 ?  110 LYS   A HZ2  1 
ATOM   2340 H  HZ3  . LYS   A 1 110 ? 21.851 -18.922 -3.962  1.00 17.60 ?  110 LYS   A HZ3  1 
ATOM   2341 N  N    . SER   A 1 111 ? 26.123 -12.992 -4.976  1.00 11.49 ?  111 SER   A N    1 
ATOM   2342 C  CA   . SER   A 1 111 ? 27.457 -12.679 -4.466  1.00 11.56 ?  111 SER   A CA   1 
ATOM   2343 C  C    . SER   A 1 111 ? 27.397 -11.633 -3.357  1.00 11.18 ?  111 SER   A C    1 
ATOM   2344 O  O    . SER   A 1 111 ? 28.092 -11.744 -2.342  1.00 11.89 ?  111 SER   A O    1 
ATOM   2345 C  CB   . SER   A 1 111 ? 28.344 -12.190 -5.610  1.00 13.05 ?  111 SER   A CB   1 
ATOM   2346 O  OG   . SER   A 1 111 ? 28.439 -13.183 -6.621  1.00 14.89 ?  111 SER   A OG   1 
ATOM   2347 H  H    . SER   A 1 111 ? 26.019 -12.871 -5.820  1.00 13.76 ?  111 SER   A H    1 
ATOM   2348 H  HA   . SER   A 1 111 ? 27.852 -13.487 -4.104  1.00 13.85 ?  111 SER   A HA   1 
ATOM   2349 H  HB2  . SER   A 1 111 ? 27.949 -11.393 -5.998  1.00 15.62 ?  111 SER   A HB2  1 
ATOM   2350 H  HB3  . SER   A 1 111 ? 29.225 -11.991 -5.265  1.00 15.62 ?  111 SER   A HB3  1 
ATOM   2351 H  HG   . SER   A 1 111 ? 28.944 -12.905 -7.244  1.00 17.84 ?  111 SER   A HG   1 
ATOM   2352 N  N    . ALA   A 1 112 ? 26.556 -10.612 -3.533  1.00 11.16 ?  112 ALA   A N    1 
ATOM   2353 C  CA   . ALA   A 1 112 ? 26.409 -9.576  -2.513  1.00 11.26 ?  112 ALA   A CA   1 
ATOM   2354 C  C    . ALA   A 1 112 ? 25.931 -10.175 -1.193  1.00 10.89 ?  112 ALA   A C    1 
ATOM   2355 O  O    . ALA   A 1 112 ? 26.479 -9.880  -0.123  1.00 11.38 ?  112 ALA   A O    1 
ATOM   2356 C  CB   . ALA   A 1 112 ? 25.444 -8.496  -3.007  1.00 11.75 ?  112 ALA   A CB   1 
ATOM   2357 H  H    . ALA   A 1 112 ? 26.072 -10.489 -4.233  1.00 13.36 ?  112 ALA   A H    1 
ATOM   2358 H  HA   . ALA   A 1 112 ? 27.266 -9.152  -2.356  1.00 13.48 ?  112 ALA   A HA   1 
ATOM   2359 H  HB1  . ALA   A 1 112 ? 25.368 -7.800  -2.327  1.00 14.07 ?  112 ALA   A HB1  1 
ATOM   2360 H  HB2  . ALA   A 1 112 ? 25.788 -8.109  -3.827  1.00 14.07 ?  112 ALA   A HB2  1 
ATOM   2361 H  HB3  . ALA   A 1 112 ? 24.573 -8.890  -3.166  1.00 14.07 ?  112 ALA   A HB3  1 
ATOM   2362 N  N    . TYR   A 1 113 ? 24.897 -11.015 -1.245  1.00 11.19 ?  113 TYR   A N    1 
ATOM   2363 C  CA   . TYR   A 1 113 ? 24.384 -11.624 -0.020  1.00 10.92 ?  113 TYR   A CA   1 
ATOM   2364 C  C    . TYR   A 1 113 ? 25.385 -12.577 0.631   1.00 10.70 ?  113 TYR   A C    1 
ATOM   2365 O  O    . TYR   A 1 113 ? 25.343 -12.759 1.852   1.00 11.39 ?  113 TYR   A O    1 
ATOM   2366 C  CB   . TYR   A 1 113 ? 23.062 -12.348 -0.294  1.00 11.57 ?  113 TYR   A CB   1 
ATOM   2367 C  CG   . TYR   A 1 113 ? 21.843 -11.453 -0.203  1.00 11.40 ?  113 TYR   A CG   1 
ATOM   2368 C  CD1  . TYR   A 1 113 ? 21.484 -10.854 1.000   1.00 11.51 ?  113 TYR   A CD1  1 
ATOM   2369 C  CD2  . TYR   A 1 113 ? 21.038 -11.222 -1.311  1.00 11.35 ?  113 TYR   A CD2  1 
ATOM   2370 C  CE1  . TYR   A 1 113 ? 20.355 -10.060 1.099   1.00 11.64 ?  113 TYR   A CE1  1 
ATOM   2371 C  CE2  . TYR   A 1 113 ? 19.891 -10.422 -1.219  1.00 11.68 ?  113 TYR   A CE2  1 
ATOM   2372 C  CZ   . TYR   A 1 113 ? 19.562 -9.849  -0.006  1.00 11.42 ?  113 TYR   A CZ   1 
ATOM   2373 O  OH   . TYR   A 1 113 ? 18.442 -9.057  0.128   1.00 12.17 ?  113 TYR   A OH   1 
ATOM   2374 H  H    . TYR   A 1 113 ? 24.485 -11.243 -1.965  1.00 13.40 ?  113 TYR   A H    1 
ATOM   2375 H  HA   . TYR   A 1 113 ? 24.206 -10.917 0.617   1.00 13.08 ?  113 TYR   A HA   1 
ATOM   2376 H  HB2  . TYR   A 1 113 ? 23.085 -12.720 -1.188  1.00 13.85 ?  113 TYR   A HB2  1 
ATOM   2377 H  HB3  . TYR   A 1 113 ? 22.954 -13.058 0.357   1.00 13.85 ?  113 TYR   A HB3  1 
ATOM   2378 H  HD1  . TYR   A 1 113 ? 22.009 -11.001 1.758   1.00 13.78 ?  113 TYR   A HD1  1 
ATOM   2379 H  HD2  . TYR   A 1 113 ? 21.253 -11.621 -2.120  1.00 13.59 ?  113 TYR   A HD2  1 
ATOM   2380 H  HE1  . TYR   A 1 113 ? 20.132 -9.670  1.914   1.00 13.93 ?  113 TYR   A HE1  1 
ATOM   2381 H  HE2  . TYR   A 1 113 ? 19.353 -10.274 -1.963  1.00 13.98 ?  113 TYR   A HE2  1 
ATOM   2382 H  HH   . TYR   A 1 113 ? 18.047 -9.003  -0.617  1.00 14.57 ?  113 TYR   A HH   1 
ATOM   2383 N  N    . GLU   A 1 114 ? 26.277 -13.203 -0.151  1.00 10.88 ?  114 GLU   A N    1 
ATOM   2384 C  CA   . GLU   A 1 114 ? 27.281 -14.089 0.442   1.00 11.17 ?  114 GLU   A CA   1 
ATOM   2385 C  C    . GLU   A 1 114 ? 28.124 -13.379 1.492   1.00 11.12 ?  114 GLU   A C    1 
ATOM   2386 O  O    . GLU   A 1 114 ? 28.603 -14.011 2.442   1.00 11.45 ?  114 GLU   A O    1 
ATOM   2387 C  CB   . GLU   A 1 114 ? 28.151 -14.729 -0.651  1.00 11.41 ?  114 GLU   A CB   1 
ATOM   2388 C  CG   . GLU   A 1 114 ? 27.385 -15.781 -1.433  1.00 11.77 ?  114 GLU   A CG   1 
ATOM   2389 C  CD   . GLU   A 1 114 ? 28.089 -16.315 -2.671  1.00 12.10 ?  114 GLU   A CD   1 
ATOM   2390 O  OE1  . GLU   A 1 114 ? 29.039 -15.685 -3.177  1.00 12.33 ?  114 GLU   A OE1  1 
ATOM   2391 O  OE2  . GLU   A 1 114 ? 27.646 -17.383 -3.159  1.00 13.41 -1 114 GLU   A OE2  1 
ATOM   2392 H  H    . GLU   A 1 114 ? 26.325 -13.123 -1.014  1.00 13.03 ?  114 GLU   A H    1 
ATOM   2393 H  HA   . GLU   A 1 114 ? 26.817 -14.806 0.886   1.00 13.37 ?  114 GLU   A HA   1 
ATOM   2394 H  HB2  . GLU   A 1 114 ? 28.439 -14.044 -1.279  1.00 13.66 ?  114 GLU   A HB2  1 
ATOM   2395 H  HB3  . GLU   A 1 114 ? 28.916 -15.156 -0.246  1.00 13.66 ?  114 GLU   A HB3  1 
ATOM   2396 H  HG2  . GLU   A 1 114 ? 27.211 -16.536 -0.850  1.00 14.09 ?  114 GLU   A HG2  1 
ATOM   2397 H  HG3  . GLU   A 1 114 ? 26.537 -15.400 -1.724  1.00 14.09 ?  114 GLU   A HG3  1 
ATOM   2398 N  N    . ASN   A 1 115 ? 28.306 -12.062 1.359   1.00 10.97 ?  115 ASN   A N    1 
ATOM   2399 C  CA   . ASN   A 1 115 ? 29.074 -11.332 2.364   1.00 11.29 ?  115 ASN   A CA   1 
ATOM   2400 C  C    . ASN   A 1 115 ? 28.458 -11.466 3.751   1.00 11.00 ?  115 ASN   A C    1 
ATOM   2401 O  O    . ASN   A 1 115 ? 29.171 -11.391 4.757   1.00 11.39 ?  115 ASN   A O    1 
ATOM   2402 C  CB   . ASN   A 1 115 ? 29.183 -9.856  1.987   1.00 11.71 ?  115 ASN   A CB   1 
ATOM   2403 C  CG   . ASN   A 1 115 ? 29.981 -9.642  0.730   1.00 12.29 ?  115 ASN   A CG   1 
ATOM   2404 O  OD1  . ASN   A 1 115 ? 31.199 -9.757  0.748   1.00 15.63 ?  115 ASN   A OD1  1 
ATOM   2405 N  ND2  . ASN   A 1 115 ? 29.312 -9.333  -0.366  1.00 12.02 ?  115 ASN   A ND2  1 
ATOM   2406 H  H    . ASN   A 1 115 ? 27.995 -11.574 0.715   1.00 13.14 ?  115 ASN   A H    1 
ATOM   2407 H  HA   . ASN   A 1 115 ? 29.967 -11.698 2.400   1.00 13.52 ?  115 ASN   A HA   1 
ATOM   2408 H  HB2  . ASN   A 1 115 ? 28.289 -9.496  1.855   1.00 14.03 ?  115 ASN   A HB2  1 
ATOM   2409 H  HB3  . ASN   A 1 115 ? 29.620 -9.379  2.716   1.00 14.03 ?  115 ASN   A HB3  1 
ATOM   2410 H  HD21 . ASN   A 1 115 ? 29.734 -9.201  -1.101  1.00 14.40 ?  115 ASN   A HD21 1 
ATOM   2411 H  HD22 . ASN   A 1 115 ? 28.453 -9.288  -0.347  1.00 14.40 ?  115 ASN   A HD22 1 
ATOM   2412 N  N    . PHE   A 1 116 ? 27.131 -11.632 3.832   1.00 10.95 ?  116 PHE   A N    1 
ATOM   2413 C  CA   . PHE   A 1 116 ? 26.484 -11.730 5.137   1.00 11.16 ?  116 PHE   A CA   1 
ATOM   2414 C  C    . PHE   A 1 116 ? 26.957 -12.961 5.907   1.00 11.47 ?  116 PHE   A C    1 
ATOM   2415 O  O    . PHE   A 1 116 ? 26.877 -12.988 7.136   1.00 12.10 ?  116 PHE   A O    1 
ATOM   2416 C  CB   . PHE   A 1 116 ? 24.957 -11.854 5.004   1.00 11.10 ?  116 PHE   A CB   1 
ATOM   2417 C  CG   . PHE   A 1 116 ? 24.204 -10.610 4.541   1.00 10.93 ?  116 PHE   A CG   1 
ATOM   2418 C  CD1  . PHE   A 1 116 ? 24.785 -9.583  3.805   1.00 10.94 ?  116 PHE   A CD1  1 
ATOM   2419 C  CD2  . PHE   A 1 116 ? 22.842 -10.512 4.844   1.00 11.69 ?  116 PHE   A CD2  1 
ATOM   2420 C  CE1  . PHE   A 1 116 ? 24.016 -8.504  3.386   1.00 11.53 ?  116 PHE   A CE1  1 
ATOM   2421 C  CE2  . PHE   A 1 116 ? 22.076 -9.438  4.428   1.00 11.87 ?  116 PHE   A CE2  1 
ATOM   2422 C  CZ   . PHE   A 1 116 ? 22.658 -8.433  3.698   1.00 11.25 ?  116 PHE   A CZ   1 
ATOM   2423 H  H    . PHE   A 1 116 ? 26.593 -11.676 3.158   1.00 13.11 ?  116 PHE   A H    1 
ATOM   2424 H  HA   . PHE   A 1 116 ? 26.683 -10.940 5.663   1.00 13.36 ?  116 PHE   A HA   1 
ATOM   2425 H  HB2  . PHE   A 1 116 ? 24.767 -12.561 4.367   1.00 13.29 ?  116 PHE   A HB2  1 
ATOM   2426 H  HB3  . PHE   A 1 116 ? 24.599 -12.104 5.872   1.00 13.29 ?  116 PHE   A HB3  1 
ATOM   2427 H  HD1  . PHE   A 1 116 ? 25.681 -9.636  3.585   1.00 13.10 ?  116 PHE   A HD1  1 
ATOM   2428 H  HD2  . PHE   A 1 116 ? 22.434 -11.206 5.329   1.00 14.00 ?  116 PHE   A HD2  1 
ATOM   2429 H  HE1  . PHE   A 1 116 ? 24.412 -7.821  2.900   1.00 13.81 ?  116 PHE   A HE1  1 
ATOM   2430 H  HE2  . PHE   A 1 116 ? 21.170 -9.404  4.649   1.00 14.22 ?  116 PHE   A HE2  1 
ATOM   2431 H  HZ   . PHE   A 1 116 ? 22.150 -7.701  3.431   1.00 13.47 ?  116 PHE   A HZ   1 
ATOM   2432 N  N    . ASN   A 1 117 ? 27.407 -14.004 5.203   1.00 11.55 ?  117 ASN   A N    1 
ATOM   2433 C  CA   . ASN   A 1 117 ? 27.769 -15.252 5.871   1.00 12.11 ?  117 ASN   A CA   1 
ATOM   2434 C  C    . ASN   A 1 117 ? 29.036 -15.137 6.699   1.00 12.45 ?  117 ASN   A C    1 
ATOM   2435 O  O    . ASN   A 1 117 ? 29.338 -16.058 7.467   1.00 13.36 ?  117 ASN   A O    1 
ATOM   2436 C  CB   . ASN   A 1 117 ? 27.881 -16.376 4.847   1.00 12.18 ?  117 ASN   A CB   1 
ATOM   2437 C  CG   . ASN   A 1 117 ? 26.526 -16.768 4.314   1.00 11.97 ?  117 ASN   A CG   1 
ATOM   2438 O  OD1  . ASN   A 1 117 ? 25.552 -16.795 5.064   1.00 12.99 ?  117 ASN   A OD1  1 
ATOM   2439 N  ND2  . ASN   A 1 117 ? 26.440 -17.032 3.026   1.00 11.83 ?  117 ASN   A ND2  1 
ATOM   2440 H  H    . ASN   A 1 117 ? 27.492 -14.018 4.341   1.00 13.83 ?  117 ASN   A H    1 
ATOM   2441 H  HA   . ASN   A 1 117 ? 27.045 -15.483 6.477   1.00 14.50 ?  117 ASN   A HA   1 
ATOM   2442 H  HB2  . ASN   A 1 117 ? 28.427 -16.077 4.104   1.00 14.59 ?  117 ASN   A HB2  1 
ATOM   2443 H  HB3  . ASN   A 1 117 ? 28.273 -17.150 5.270   1.00 14.59 ?  117 ASN   A HB3  1 
ATOM   2444 H  HD21 . ASN   A 1 117 ? 25.688 -17.253 2.687   1.00 14.17 ?  117 ASN   A HD21 1 
ATOM   2445 H  HD22 . ASN   A 1 117 ? 27.147 -16.994 2.536   1.00 14.17 ?  117 ASN   A HD22 1 
ATOM   2446 N  N    . GLN   A 1 118 ? 29.761 -14.027 6.584   1.00 12.27 ?  118 GLN   A N    1 
ATOM   2447 C  CA   . GLN   A 1 118 ? 30.939 -13.797 7.406   1.00 13.11 ?  118 GLN   A CA   1 
ATOM   2448 C  C    . GLN   A 1 118 ? 30.596 -13.216 8.773   1.00 12.94 ?  118 GLN   A C    1 
ATOM   2449 O  O    . GLN   A 1 118 ? 31.509 -12.916 9.553   1.00 14.61 ?  118 GLN   A O    1 
ATOM   2450 C  CB   . GLN   A 1 118 ? 31.931 -12.896 6.667   1.00 13.16 ?  118 GLN   A CB   1 
ATOM   2451 C  CG   . GLN   A 1 118 ? 32.401 -13.474 5.347   1.00 12.93 ?  118 GLN   A CG   1 
ATOM   2452 C  CD   . GLN   A 1 118 ? 33.234 -14.732 5.520   1.00 13.40 ?  118 GLN   A CD   1 
ATOM   2453 O  OE1  . GLN   A 1 118 ? 34.092 -14.803 6.408   1.00 14.23 ?  118 GLN   A OE1  1 
ATOM   2454 N  NE2  . GLN   A 1 118 ? 32.988 -15.727 4.670   1.00 13.61 ?  118 GLN   A NE2  1 
ATOM   2455 H  H    . GLN   A 1 118 ? 29.579 -13.382 6.035   1.00 14.70 ?  118 GLN   A H    1 
ATOM   2456 H  HA   . GLN   A 1 118 ? 31.367 -14.654 7.552   1.00 15.71 ?  118 GLN   A HA   1 
ATOM   2457 H  HB2  . GLN   A 1 118 ? 31.509 -12.044 6.490   1.00 15.76 ?  118 GLN   A HB2  1 
ATOM   2458 H  HB3  . GLN   A 1 118 ? 32.711 -12.771 7.232   1.00 15.76 ?  118 GLN   A HB3  1 
ATOM   2459 H  HG2  . GLN   A 1 118 ? 31.629 -13.691 4.800   1.00 15.48 ?  118 GLN   A HG2  1 
ATOM   2460 H  HG3  . GLN   A 1 118 ? 32.950 -12.813 4.892   1.00 15.48 ?  118 GLN   A HG3  1 
ATOM   2461 H  HE21 . GLN   A 1 118 ? 32.379 -15.635 4.058   1.00 16.30 ?  118 GLN   A HE21 1 
ATOM   2462 H  HE22 . GLN   A 1 118 ? 33.427 -16.463 4.718   1.00 16.30 ?  118 GLN   A HE22 1 
ATOM   2463 N  N    . HIS   A 1 119 ? 29.306 -13.058 9.080   1.00 12.51 ?  119 HIS   A N    1 
ATOM   2464 C  CA   . HIS   A 1 119 ? 28.851 -12.456 10.327  1.00 12.87 ?  119 HIS   A CA   1 
ATOM   2465 C  C    . HIS   A 1 119 ? 27.707 -13.272 10.902  1.00 13.14 ?  119 HIS   A C    1 
ATOM   2466 O  O    . HIS   A 1 119 ? 26.759 -13.610 10.188  1.00 13.70 ?  119 HIS   A O    1 
ATOM   2467 C  CB   . HIS   A 1 119 ? 28.404 -11.021 10.065  1.00 13.36 ?  119 HIS   A CB   1 
ATOM   2468 C  CG   . HIS   A 1 119 ? 29.483 -10.211 9.445   1.00 14.39 ?  119 HIS   A CG   1 
ATOM   2469 N  ND1  . HIS   A 1 119 ? 30.461 -9.600  10.194  1.00 16.97 ?  119 HIS   A ND1  1 
ATOM   2470 C  CD2  . HIS   A 1 119 ? 29.814 -10.013 8.148   1.00 15.61 ?  119 HIS   A CD2  1 
ATOM   2471 C  CE1  . HIS   A 1 119 ? 31.319 -9.008  9.383   1.00 17.19 ?  119 HIS   A CE1  1 
ATOM   2472 N  NE2  . HIS   A 1 119 ? 30.963 -9.261  8.136   1.00 17.19 ?  119 HIS   A NE2  1 
ATOM   2473 H  H    . HIS   A 1 119 ? 28.653 -13.307 8.570   1.00 14.99 ?  119 HIS   A H    1 
ATOM   2474 H  HA   . HIS   A 1 119 ? 29.583 -12.450 10.967  1.00 15.41 ?  119 HIS   A HA   1 
ATOM   2475 H  HB2  . HIS   A 1 119 ? 27.643 -11.037 9.464   1.00 16.00 ?  119 HIS   A HB2  1 
ATOM   2476 H  HB3  . HIS   A 1 119 ? 28.158 -10.613 10.909  1.00 16.00 ?  119 HIS   A HB3  1 
ATOM   2477 H  HD1  . HIS   A 1 119 ? 30.494 -9.586  11.050  1.00 20.33 ?  119 HIS   A HD1  1 
ATOM   2478 H  HD2  . HIS   A 1 119 ? 29.346 -10.330 7.406   1.00 18.70 ?  119 HIS   A HD2  1 
ATOM   2479 H  HE1  . HIS   A 1 119 ? 32.057 -8.510  9.642   1.00 20.59 ?  119 HIS   A HE1  1 
ATOM   2480 N  N    . GLU   A 1 120 ? 27.793 -13.573 12.199  1.00 14.14 ?  120 GLU   A N    1 
ATOM   2481 C  CA   . GLU   A 1 120 ? 26.839 -14.504 12.797  1.00 16.60 ?  120 GLU   A CA   1 
ATOM   2482 C  C    . GLU   A 1 120 ? 25.422 -13.941 12.855  1.00 14.85 ?  120 GLU   A C    1 
ATOM   2483 O  O    . GLU   A 1 120 ? 24.450 -14.704 12.736  1.00 15.08 ?  120 GLU   A O    1 
ATOM   2484 C  CB   . GLU   A 1 120 ? 27.306 -14.909 14.197  1.00 22.16 ?  120 GLU   A CB   1 
ATOM   2485 C  CG   . GLU   A 1 120 ? 28.497 -15.856 14.197  1.00 30.43 ?  120 GLU   A CG   1 
ATOM   2486 C  CD   . GLU   A 1 120 ? 28.686 -16.555 15.528  1.00 38.09 ?  120 GLU   A CD   1 
ATOM   2487 O  OE1  . GLU   A 1 120 ? 28.210 -16.025 16.555  1.00 40.01 ?  120 GLU   A OE1  1 
ATOM   2488 O  OE2  . GLU   A 1 120 ? 29.311 -17.636 15.547  1.00 43.06 -1 120 GLU   A OE2  1 
ATOM   2489 H  H    . GLU   A 1 120 ? 28.382 -13.258 12.746  1.00 16.93 ?  120 GLU   A H    1 
ATOM   2490 H  HA   . GLU   A 1 120 ? 26.816 -15.309 12.263  1.00 19.89 ?  120 GLU   A HA   1 
ATOM   2491 H  HB2  . GLU   A 1 120 ? 27.568 -14.118 14.691  1.00 26.56 ?  120 GLU   A HB2  1 
ATOM   2492 H  HB3  . GLU   A 1 120 ? 26.579 -15.359 14.659  1.00 26.56 ?  120 GLU   A HB3  1 
ATOM   2493 H  HG2  . GLU   A 1 120 ? 28.375 -16.524 13.503  1.00 36.49 ?  120 GLU   A HG2  1 
ATOM   2494 H  HG3  . GLU   A 1 120 ? 29.308 -15.353 14.039  1.00 36.49 ?  120 GLU   A HG3  1 
ATOM   2495 N  N    . VAL   A 1 121 ? 25.286 -12.632 13.076  1.00 14.24 ?  121 VAL   A N    1 
ATOM   2496 C  CA   . VAL   A 1 121 ? 23.990 -11.966 13.185  1.00 14.24 ?  121 VAL   A CA   1 
ATOM   2497 C  C    . VAL   A 1 121 ? 24.103 -10.583 12.549  1.00 12.99 ?  121 VAL   A C    1 
ATOM   2498 O  O    . VAL   A 1 121 ? 25.069 -9.854  12.801  1.00 13.55 ?  121 VAL   A O    1 
ATOM   2499 C  CB   . VAL   A 1 121 ? 23.540 -11.817 14.656  1.00 17.39 ?  121 VAL   A CB   1 
ATOM   2500 C  CG1  . VAL   A 1 121 ? 22.143 -11.210 14.731  1.00 17.95 ?  121 VAL   A CG1  1 
ATOM   2501 C  CG2  . VAL   A 1 121 ? 23.576 -13.144 15.401  1.00 19.71 ?  121 VAL   A CG2  1 
ATOM   2502 H  H    . VAL   A 1 121 ? 25.949 -12.094 13.173  1.00 17.06 ?  121 VAL   A H    1 
ATOM   2503 H  HA   . VAL   A 1 121 ? 23.320 -12.481 12.709  1.00 17.06 ?  121 VAL   A HA   1 
ATOM   2504 H  HB   . VAL   A 1 121 ? 24.142 -11.212 15.109  1.00 20.84 ?  121 VAL   A HB   1 
ATOM   2505 H  HG11 . VAL   A 1 121 ? 21.821 -11.263 15.647  1.00 21.52 ?  121 VAL   A HG11 1 
ATOM   2506 H  HG12 . VAL   A 1 121 ? 22.181 -10.283 14.451  1.00 21.52 ?  121 VAL   A HG12 1 
ATOM   2507 H  HG13 . VAL   A 1 121 ? 21.547 -11.708 14.147  1.00 21.52 ?  121 VAL   A HG13 1 
ATOM   2508 H  HG21 . VAL   A 1 121 ? 23.219 -13.014 16.299  1.00 23.62 ?  121 VAL   A HG21 1 
ATOM   2509 H  HG22 . VAL   A 1 121 ? 23.028 -13.791 14.927  1.00 23.62 ?  121 VAL   A HG22 1 
ATOM   2510 H  HG23 . VAL   A 1 121 ? 24.489 -13.455 15.453  1.00 23.62 ?  121 VAL   A HG23 1 
ATOM   2511 N  N    . LEU   A 1 122 ? 23.093 -10.199 11.763  1.00 12.51 ?  122 LEU   A N    1 
ATOM   2512 C  CA   . LEU   A 1 122 ? 23.092 -8.902  11.090  1.00 12.16 ?  122 LEU   A CA   1 
ATOM   2513 C  C    . LEU   A 1 122 ? 21.691 -8.309  11.060  1.00 11.86 ?  122 LEU   A C    1 
ATOM   2514 O  O    . LEU   A 1 122 ? 20.702 -9.029  10.921  1.00 13.19 ?  122 LEU   A O    1 
ATOM   2515 C  CB   . LEU   A 1 122 ? 23.527 -8.994  9.621   1.00 13.46 ?  122 LEU   A CB   1 
ATOM   2516 C  CG   . LEU   A 1 122 ? 24.736 -9.846  9.273   1.00 13.24 ?  122 LEU   A CG   1 
ATOM   2517 C  CD1  . LEU   A 1 122 ? 24.335 -11.300 9.054   1.00 14.46 ?  122 LEU   A CD1  1 
ATOM   2518 C  CD2  . LEU   A 1 122 ? 25.420 -9.286  8.037   1.00 12.77 ?  122 LEU   A CD2  1 
ATOM   2519 H  H    . LEU   A 1 122 ? 22.389 -10.672 11.604  1.00 14.98 ?  122 LEU   A H    1 
ATOM   2520 H  HA   . LEU   A 1 122 ? 23.684 -8.287  11.553  1.00 14.57 ?  122 LEU   A HA   1 
ATOM   2521 H  HB2  . LEU   A 1 122 ? 22.789 -9.352  9.111   1.00 16.12 ?  122 LEU   A HB2  1 
ATOM   2522 H  HB3  . LEU   A 1 122 ? 23.727 -8.100  9.311   1.00 16.12 ?  122 LEU   A HB3  1 
ATOM   2523 H  HG   . LEU   A 1 122 ? 25.383 -9.819  10.000  1.00 15.86 ?  122 LEU   A HG   1 
ATOM   2524 H  HD11 . LEU   A 1 122 ? 25.113 -11.813 8.777   1.00 17.33 ?  122 LEU   A HD11 1 
ATOM   2525 H  HD12 . LEU   A 1 122 ? 23.985 -11.660 9.885   1.00 17.33 ?  122 LEU   A HD12 1 
ATOM   2526 H  HD13 . LEU   A 1 122 ? 23.654 -11.340 8.364   1.00 17.33 ?  122 LEU   A HD13 1 
ATOM   2527 H  HD21 . LEU   A 1 122 ? 26.167 -9.859  7.788   1.00 15.29 ?  122 LEU   A HD21 1 
ATOM   2528 H  HD22 . LEU   A 1 122 ? 24.780 -9.250  7.308   1.00 15.29 ?  122 LEU   A HD22 1 
ATOM   2529 H  HD23 . LEU   A 1 122 ? 25.747 -8.391  8.229   1.00 15.29 ?  122 LEU   A HD23 1 
ATOM   2530 N  N    . LEU   A 1 123 ? 21.631 -6.978  11.167  1.00 11.64 ?  123 LEU   A N    1 
ATOM   2531 C  CA   . LEU   A 1 123 ? 20.460 -6.180  10.800  1.00 11.47 ?  123 LEU   A CA   1 
ATOM   2532 C  C    . LEU   A 1 123 ? 20.709 -5.661  9.391   1.00 10.88 ?  123 LEU   A C    1 
ATOM   2533 O  O    . LEU   A 1 123 ? 21.759 -5.066  9.143   1.00 11.85 ?  123 LEU   A O    1 
ATOM   2534 C  CB   . LEU   A 1 123 ? 20.329 -5.005  11.770  1.00 12.21 ?  123 LEU   A CB   1 
ATOM   2535 C  CG   . LEU   A 1 123 ? 19.283 -3.943  11.430  1.00 12.87 ?  123 LEU   A CG   1 
ATOM   2536 C  CD1  . LEU   A 1 123 ? 17.883 -4.536  11.425  1.00 13.46 ?  123 LEU   A CD1  1 
ATOM   2537 C  CD2  . LEU   A 1 123 ? 19.382 -2.767  12.396  1.00 13.45 ?  123 LEU   A CD2  1 
ATOM   2538 H  H    . LEU   A 1 123 ? 22.282 -6.498  11.468  1.00 13.93 ?  123 LEU   A H    1 
ATOM   2539 H  HA   . LEU   A 1 123 ? 19.653 -6.720  10.824  1.00 13.74 ?  123 LEU   A HA   1 
ATOM   2540 H  HB2  . LEU   A 1 123 ? 20.090 -5.356  12.649  1.00 14.62 ?  123 LEU   A HB2  1 
ATOM   2541 H  HB3  . LEU   A 1 123 ? 21.181 -4.555  11.830  1.00 14.62 ?  123 LEU   A HB3  1 
ATOM   2542 H  HG   . LEU   A 1 123 ? 19.460 -3.598  10.540  1.00 15.41 ?  123 LEU   A HG   1 
ATOM   2543 H  HD11 . LEU   A 1 123 ? 17.237 -3.839  11.251  1.00 16.12 ?  123 LEU   A HD11 1 
ATOM   2544 H  HD12 . LEU   A 1 123 ? 17.833 -5.217  10.733  1.00 16.12 ?  123 LEU   A HD12 1 
ATOM   2545 H  HD13 . LEU   A 1 123 ? 17.710 -4.941  12.293  1.00 16.12 ?  123 LEU   A HD13 1 
ATOM   2546 H  HD21 . LEU   A 1 123 ? 18.712 -2.106  12.163  1.00 16.11 ?  123 LEU   A HD21 1 
ATOM   2547 H  HD22 . LEU   A 1 123 ? 19.223 -3.092  13.300  1.00 16.11 ?  123 LEU   A HD22 1 
ATOM   2548 H  HD23 . LEU   A 1 123 ? 20.267 -2.382  12.336  1.00 16.11 ?  123 LEU   A HD23 1 
ATOM   2549 N  N    A ALA   A 1 124 ? 19.739 -5.816  8.489   0.72 10.40 ?  124 ALA   A N    1 
ATOM   2550 N  N    B ALA   A 1 124 ? 19.808 -5.957  8.460   0.28 10.95 ?  124 ALA   A N    1 
ATOM   2551 C  CA   A ALA   A 1 124 ? 20.019 -5.517  7.091   0.72 10.17 ?  124 ALA   A CA   1 
ATOM   2552 C  CA   B ALA   A 1 124 ? 20.125 -5.752  7.055   0.28 11.30 ?  124 ALA   A CA   1 
ATOM   2553 C  C    A ALA   A 1 124 ? 18.767 -5.059  6.354   0.72 9.78  ?  124 ALA   A C    1 
ATOM   2554 C  C    B ALA   A 1 124 ? 18.915 -5.277  6.262   0.28 11.06 ?  124 ALA   A C    1 
ATOM   2555 O  O    A ALA   A 1 124 ? 17.639 -5.410  6.735   0.72 10.86 ?  124 ALA   A O    1 
ATOM   2556 O  O    B ALA   A 1 124 ? 17.772 -5.615  6.597   0.28 11.53 ?  124 ALA   A O    1 
ATOM   2557 C  CB   A ALA   A 1 124 ? 20.599 -6.741  6.378   0.72 10.57 ?  124 ALA   A CB   1 
ATOM   2558 C  CB   B ALA   A 1 124 ? 20.679 -7.038  6.417   0.28 11.68 ?  124 ALA   A CB   1 
ATOM   2559 H  H    A ALA   A 1 124 ? 18.939 -6.088  8.659   0.72 12.45 ?  124 ALA   A H    1 
ATOM   2560 H  H    B ALA   A 1 124 ? 19.026 -6.281  8.613   0.28 13.10 ?  124 ALA   A H    1 
ATOM   2561 H  HA   A ALA   A 1 124 ? 20.677 -4.807  7.061   0.72 12.17 ?  124 ALA   A HA   1 
ATOM   2562 H  HA   B ALA   A 1 124 ? 20.813 -5.075  6.996   0.28 13.53 ?  124 ALA   A HA   1 
ATOM   2563 H  HB1  A ALA   A 1 124 ? 20.779 -6.510  5.453   0.72 12.65 ?  124 ALA   A HB1  1 
ATOM   2564 H  HB1  B ALA   A 1 124 ? 20.886 -6.868  5.482   0.28 13.98 ?  124 ALA   A HB1  1 
ATOM   2565 H  HB2  A ALA   A 1 124 ? 21.428 -6.998  6.819   0.72 12.65 ?  124 ALA   A HB2  1 
ATOM   2566 H  HB2  B ALA   A 1 124 ? 21.490 -7.307  6.885   0.28 13.98 ?  124 ALA   A HB2  1 
ATOM   2567 H  HB3  A ALA   A 1 124 ? 19.963 -7.467  6.424   0.72 12.65 ?  124 ALA   A HB3  1 
ATOM   2568 H  HB3  B ALA   A 1 124 ? 20.015 -7.741  6.485   0.28 13.98 ?  124 ALA   A HB3  1 
ATOM   2569 N  N    A PRO   A 1 125 ? 18.944 -4.323  5.258   0.72 10.37 ?  125 PRO   A N    1 
ATOM   2570 N  N    B PRO   A 1 125 ? 19.138 -4.514  5.196   0.28 9.78  ?  125 PRO   A N    1 
ATOM   2571 C  CA   A PRO   A 1 125 ? 17.887 -4.121  4.268   0.72 11.36 ?  125 PRO   A CA   1 
ATOM   2572 C  CA   B PRO   A 1 125 ? 18.046 -4.116  4.309   0.28 9.98  ?  125 PRO   A CA   1 
ATOM   2573 C  C    A PRO   A 1 125 ? 17.969 -5.193  3.184   0.72 10.86 ?  125 PRO   A C    1 
ATOM   2574 C  C    B PRO   A 1 125 ? 17.957 -5.107  3.152   0.28 10.77 ?  125 PRO   A C    1 
ATOM   2575 O  O    A PRO   A 1 125 ? 18.947 -5.936  3.076   0.72 11.12 ?  125 PRO   A O    1 
ATOM   2576 O  O    B PRO   A 1 125 ? 18.795 -5.998  2.998   0.28 11.31 ?  125 PRO   A O    1 
ATOM   2577 C  CB   A PRO   A 1 125 ? 18.290 -2.767  3.667   0.72 11.86 ?  125 PRO   A CB   1 
ATOM   2578 C  CB   B PRO   A 1 125 ? 18.533 -2.754  3.805   0.28 9.19  ?  125 PRO   A CB   1 
ATOM   2579 C  CG   A PRO   A 1 125 ? 19.797 -2.889  3.592   0.72 11.84 ?  125 PRO   A CG   1 
ATOM   2580 C  CG   B PRO   A 1 125 ? 20.020 -2.982  3.628   0.28 8.77  ?  125 PRO   A CG   1 
ATOM   2581 C  CD   A PRO   A 1 125 ? 20.182 -3.609  4.877   0.72 11.08 ?  125 PRO   A CD   1 
ATOM   2582 C  CD   B PRO   A 1 125 ? 20.428 -3.973  4.720   0.28 8.48  ?  125 PRO   A CD   1 
ATOM   2583 H  HA   A PRO   A 1 125 ? 17.004 -4.088  4.668   0.72 13.61 ?  125 PRO   A HA   1 
ATOM   2584 H  HA   B PRO   A 1 125 ? 17.209 -4.026  4.796   0.28 11.94 ?  125 PRO   A HA   1 
ATOM   2585 H  HB2  A PRO   A 1 125 ? 17.896 -2.661  2.785   0.72 14.20 ?  125 PRO   A HB2  1 
ATOM   2586 H  HB2  B PRO   A 1 125 ? 18.103 -2.537  2.962   0.28 11.00 ?  125 PRO   A HB2  1 
ATOM   2587 H  HB3  A PRO   A 1 125 ? 18.021 -2.047  4.260   0.72 14.20 ?  125 PRO   A HB3  1 
ATOM   2588 H  HB3  B PRO   A 1 125 ? 18.358 -2.065  4.472   0.28 11.00 ?  125 PRO   A HB3  1 
ATOM   2589 H  HG2  A PRO   A 1 125 ? 20.048 -3.416  2.816   0.72 14.18 ?  125 PRO   A HG2  1 
ATOM   2590 H  HG2  B PRO   A 1 125 ? 20.185 -3.358  2.748   0.28 10.50 ?  125 PRO   A HG2  1 
ATOM   2591 H  HG3  A PRO   A 1 125 ? 20.197 -2.007  3.553   0.72 14.18 ?  125 PRO   A HG3  1 
ATOM   2592 H  HG3  B PRO   A 1 125 ? 20.494 -2.144  3.734   0.28 10.50 ?  125 PRO   A HG3  1 
ATOM   2593 H  HD2  A PRO   A 1 125 ? 20.903 -4.230  4.716   0.72 13.27 ?  125 PRO   A HD2  1 
ATOM   2594 H  HD2  B PRO   A 1 125 ? 20.987 -4.678  4.341   0.28 10.14 ?  125 PRO   A HD2  1 
ATOM   2595 H  HD3  A PRO   A 1 125 ? 20.417 -2.959  5.565   0.72 13.27 ?  125 PRO   A HD3  1 
ATOM   2596 H  HD3  B PRO   A 1 125 ? 20.891 -3.509  5.435   0.28 10.14 ?  125 PRO   A HD3  1 
ATOM   2597 N  N    A LEU   A 1 126 ? 16.928 -5.236  2.357   0.72 10.76 ?  126 LEU   A N    1 
ATOM   2598 N  N    B LEU   A 1 126 ? 16.926 -4.931  2.323   0.28 11.34 ?  126 LEU   A N    1 
ATOM   2599 C  CA   A LEU   A 1 126 ? 16.946 -6.066  1.161   0.72 11.15 ?  126 LEU   A CA   1 
ATOM   2600 C  CA   B LEU   A 1 126 ? 16.805 -5.746  1.115   0.28 11.33 ?  126 LEU   A CA   1 
ATOM   2601 C  C    A LEU   A 1 126 ? 17.872 -5.450  0.118   0.72 10.95 ?  126 LEU   A C    1 
ATOM   2602 C  C    B LEU   A 1 126 ? 17.750 -5.182  0.062   0.28 11.03 ?  126 LEU   A C    1 
ATOM   2603 O  O    A LEU   A 1 126 ? 17.648 -4.328  -0.346  0.72 11.92 ?  126 LEU   A O    1 
ATOM   2604 O  O    B LEU   A 1 126 ? 17.468 -4.153  -0.557  0.28 11.28 ?  126 LEU   A O    1 
ATOM   2605 C  CB   A LEU   A 1 126 ? 15.533 -6.216  0.606   0.72 11.34 ?  126 LEU   A CB   1 
ATOM   2606 C  CB   B LEU   A 1 126 ? 15.368 -5.745  0.610   0.28 12.24 ?  126 LEU   A CB   1 
ATOM   2607 C  CG   A LEU   A 1 126 ? 14.619 -7.151  1.399   0.72 12.01 ?  126 LEU   A CG   1 
ATOM   2608 C  CG   B LEU   A 1 126 ? 14.379 -6.573  1.425   0.28 12.58 ?  126 LEU   A CG   1 
ATOM   2609 C  CD1  A LEU   A 1 126 ? 13.186 -7.033  0.919   0.72 13.70 ?  126 LEU   A CD1  1 
ATOM   2610 C  CD1  B LEU   A 1 126 ? 12.984 -6.423  0.843   0.28 12.65 ?  126 LEU   A CD1  1 
ATOM   2611 C  CD2  A LEU   A 1 126 ? 15.109 -8.593  1.277   0.72 12.31 ?  126 LEU   A CD2  1 
ATOM   2612 C  CD2  B LEU   A 1 126 ? 14.787 -8.035  1.459   0.28 12.78 ?  126 LEU   A CD2  1 
ATOM   2613 H  H    A LEU   A 1 126 ? 16.205 -4.784  2.461   0.72 12.89 ?  126 LEU   A H    1 
ATOM   2614 H  H    B LEU   A 1 126 ? 16.277 -4.358  2.424   0.28 13.58 ?  126 LEU   A H    1 
ATOM   2615 H  HA   A LEU   A 1 126 ? 17.283 -6.944  1.383   0.72 13.35 ?  126 LEU   A HA   1 
ATOM   2616 H  HA   B LEU   A 1 126 ? 17.069 -6.660  1.320   0.28 13.56 ?  126 LEU   A HA   1 
ATOM   2617 H  HB2  A LEU   A 1 126 ? 15.107 -5.344  0.594   0.72 13.58 ?  126 LEU   A HB2  1 
ATOM   2618 H  HB2  B LEU   A 1 126 ? 15.047 -4.829  0.608   0.28 14.65 ?  126 LEU   A HB2  1 
ATOM   2619 H  HB3  A LEU   A 1 126 ? 15.586 -6.564  -0.297  0.72 13.58 ?  126 LEU   A HB3  1 
ATOM   2620 H  HB3  B LEU   A 1 126 ? 15.362 -6.094  -0.292  0.28 14.65 ?  126 LEU   A HB3  1 
ATOM   2621 H  HG   A LEU   A 1 126 ? 14.641 -6.905  2.338   0.72 14.39 ?  126 LEU   A HG   1 
ATOM   2622 H  HG   B LEU   A 1 126 ? 14.358 -6.241  2.338   0.28 15.07 ?  126 LEU   A HG   1 
ATOM   2623 H  HD11 A LEU   A 1 126 ? 12.627 -7.637  1.434   0.72 16.41 ?  126 LEU   A HD11 1 
ATOM   2624 H  HD11 B LEU   A 1 126 ? 12.364 -6.953  1.367   0.28 15.15 ?  126 LEU   A HD11 1 
ATOM   2625 H  HD12 A LEU   A 1 126 ? 12.888 -6.120  1.040   0.72 16.41 ?  126 LEU   A HD12 1 
ATOM   2626 H  HD12 B LEU   A 1 126 ? 12.728 -5.487  0.873   0.28 15.15 ?  126 LEU   A HD12 1 
ATOM   2627 H  HD13 A LEU   A 1 126 ? 13.150 -7.273  -0.022  0.72 16.41 ?  126 LEU   A HD13 1 
ATOM   2628 H  HD13 B LEU   A 1 126 ? 12.992 -6.734  -0.076  0.28 15.15 ?  126 LEU   A HD13 1 
ATOM   2629 H  HD21 A LEU   A 1 126 ? 14.438 -9.190  1.640   0.72 14.74 ?  126 LEU   A HD21 1 
ATOM   2630 H  HD21 B LEU   A 1 126 ? 14.043 -8.563  1.787   0.28 15.31 ?  126 LEU   A HD21 1 
ATOM   2631 H  HD22 A LEU   A 1 126 ? 15.262 -8.795  0.341   0.72 14.74 ?  126 LEU   A HD22 1 
ATOM   2632 H  HD22 B LEU   A 1 126 ? 15.023 -8.314  0.561   0.28 15.31 ?  126 LEU   A HD22 1 
ATOM   2633 H  HD23 A LEU   A 1 126 ? 15.938 -8.688  1.775   0.72 14.74 ?  126 LEU   A HD23 1 
ATOM   2634 H  HD23 B LEU   A 1 126 ? 15.550 -8.134  2.048   0.28 15.31 ?  126 LEU   A HD23 1 
ATOM   2635 N  N    A LEU   A 1 127 ? 18.914 -6.186  -0.249  0.72 10.91 ?  127 LEU   A N    1 
ATOM   2636 N  N    B LEU   A 1 127 ? 18.875 -5.859  -0.155  0.28 10.45 ?  127 LEU   A N    1 
ATOM   2637 C  CA   A LEU   A 1 127 ? 19.898 -5.682  -1.194  0.72 10.61 ?  127 LEU   A CA   1 
ATOM   2638 C  CA   B LEU   A 1 127 ? 19.870 -5.344  -1.084  0.28 10.47 ?  127 LEU   A CA   1 
ATOM   2639 C  C    A LEU   A 1 127 ? 19.283 -5.509  -2.573  0.72 10.35 ?  127 LEU   A C    1 
ATOM   2640 C  C    B LEU   A 1 127 ? 19.302 -5.270  -2.495  0.28 10.83 ?  127 LEU   A C    1 
ATOM   2641 O  O    A LEU   A 1 127 ? 18.469 -6.318  -3.023  0.72 10.66 ?  127 LEU   A O    1 
ATOM   2642 O  O    B LEU   A 1 127 ? 18.465 -6.080  -2.901  0.28 10.93 ?  127 LEU   A O    1 
ATOM   2643 C  CB   A LEU   A 1 127 ? 21.080 -6.647  -1.283  0.72 11.14 ?  127 LEU   A CB   1 
ATOM   2644 C  CB   B LEU   A 1 127 ? 21.112 -6.232  -1.088  0.28 10.80 ?  127 LEU   A CB   1 
ATOM   2645 C  CG   A LEU   A 1 127 ? 21.874 -6.870  0.000   0.72 11.55 ?  127 LEU   A CG   1 
ATOM   2646 C  CG   B LEU   A 1 127 ? 21.913 -6.241  0.215   0.28 11.13 ?  127 LEU   A CG   1 
ATOM   2647 C  CD1  A LEU   A 1 127 ? 22.981 -7.862  -0.266  0.72 11.92 ?  127 LEU   A CD1  1 
ATOM   2648 C  CD1  B LEU   A 1 127 ? 23.061 -7.230  0.130   0.28 11.47 ?  127 LEU   A CD1  1 
ATOM   2649 C  CD2  A LEU   A 1 127 ? 22.463 -5.573  0.511   0.72 12.42 ?  127 LEU   A CD2  1 
ATOM   2650 C  CD2  B LEU   A 1 127 ? 22.430 -4.847  0.556   0.28 11.67 ?  127 LEU   A CD2  1 
ATOM   2651 H  H    A LEU   A 1 127 ? 19.075 -6.980  0.044   0.72 13.06 ?  127 LEU   A H    1 
ATOM   2652 H  H    B LEU   A 1 127 ? 19.082 -6.609  0.221   0.28 12.51 ?  127 LEU   A H    1 
ATOM   2653 H  HA   A LEU   A 1 127 ? 20.225 -4.824  -0.892  0.72 12.70 ?  127 LEU   A HA   1 
ATOM   2654 H  HA   B LEU   A 1 127 ? 20.125 -4.451  -0.800  0.28 12.53 ?  127 LEU   A HA   1 
ATOM   2655 H  HB2  A LEU   A 1 127 ? 20.746 -7.512  -1.567  0.72 13.34 ?  127 LEU   A HB2  1 
ATOM   2656 H  HB2  B LEU   A 1 127 ? 20.832 -7.142  -1.275  0.28 12.93 ?  127 LEU   A HB2  1 
ATOM   2657 H  HB3  A LEU   A 1 127 ? 21.699 -6.307  -1.945  0.72 13.34 ?  127 LEU   A HB3  1 
ATOM   2658 H  HB3  B LEU   A 1 127 ? 21.698 -5.922  -1.798  0.28 12.93 ?  127 LEU   A HB3  1 
ATOM   2659 H  HG   A LEU   A 1 127 ? 21.289 -7.238  0.687   0.72 13.83 ?  127 LEU   A HG   1 
ATOM   2660 H  HG   B LEU   A 1 127 ? 21.329 -6.526  0.933   0.28 13.33 ?  127 LEU   A HG   1 
ATOM   2661 H  HD11 A LEU   A 1 127 ? 23.470 -8.021  0.558   0.72 14.28 ?  127 LEU   A HD11 1 
ATOM   2662 H  HD11 B LEU   A 1 127 ? 23.582 -7.172  0.945   0.28 13.74 ?  127 LEU   A HD11 1 
ATOM   2663 H  HD12 A LEU   A 1 127 ? 22.596 -8.693  -0.587  0.72 14.28 ?  127 LEU   A HD12 1 
ATOM   2664 H  HD12 B LEU   A 1 127 ? 22.701 -8.124  0.028   0.28 13.74 ?  127 LEU   A HD12 1 
ATOM   2665 H  HD13 A LEU   A 1 127 ? 23.578 -7.494  -0.937  0.72 14.28 ?  127 LEU   A HD13 1 
ATOM   2666 H  HD13 B LEU   A 1 127 ? 23.614 -7.005  -0.634  0.28 13.74 ?  127 LEU   A HD13 1 
ATOM   2667 H  HD21 A LEU   A 1 127 ? 23.058 -5.767  1.252   0.72 14.88 ?  127 LEU   A HD21 1 
ATOM   2668 H  HD21 B LEU   A 1 127 ? 23.063 -4.918  1.289   0.28 13.97 ?  127 LEU   A HD21 1 
ATOM   2669 H  HD22 A LEU   A 1 127 ? 22.963 -5.153  -0.210  0.72 14.88 ?  127 LEU   A HD22 1 
ATOM   2670 H  HD22 B LEU   A 1 127 ? 22.870 -4.473  -0.224  0.28 13.97 ?  127 LEU   A HD22 1 
ATOM   2671 H  HD23 A LEU   A 1 127 ? 21.748 -4.990  0.801   0.72 14.88 ?  127 LEU   A HD23 1 
ATOM   2672 H  HD23 B LEU   A 1 127 ? 21.684 -4.286  0.817   0.28 13.97 ?  127 LEU   A HD23 1 
ATOM   2673 N  N    A SER   A 1 128 ? 19.703 -4.447  -3.249  0.72 10.44 ?  128 SER   A N    1 
ATOM   2674 N  N    B SER   A 1 128 ? 19.769 -4.271  -3.239  0.28 11.00 ?  128 SER   A N    1 
ATOM   2675 C  CA   A SER   A 1 128 ? 19.284 -4.044  -4.585  0.72 10.61 ?  128 SER   A CA   1 
ATOM   2676 C  CA   B SER   A 1 128 ? 19.407 -4.067  -4.638  0.28 10.53 ?  128 SER   A CA   1 
ATOM   2677 C  C    A SER   A 1 128 ? 17.821 -3.614  -4.678  0.72 11.13 ?  128 SER   A C    1 
ATOM   2678 C  C    B SER   A 1 128 ? 17.967 -3.599  -4.830  0.28 10.03 ?  128 SER   A C    1 
ATOM   2679 O  O    A SER   A 1 128 ? 17.362 -3.314  -5.779  0.72 12.59 ?  128 SER   A O    1 
ATOM   2680 O  O    B SER   A 1 128 ? 17.587 -3.220  -5.942  0.28 9.96  ?  128 SER   A O    1 
ATOM   2681 C  CB   A SER   A 1 128 ? 19.637 -5.066  -5.678  0.72 11.27 ?  128 SER   A CB   1 
ATOM   2682 C  CB   B SER   A 1 128 ? 19.707 -5.307  -5.487  0.28 10.62 ?  128 SER   A CB   1 
ATOM   2683 O  OG   A SER   A 1 128 ? 21.042 -5.295  -5.716  0.72 11.95 ?  128 SER   A OG   1 
ATOM   2684 O  OG   B SER   A 1 128 ? 21.105 -5.442  -5.689  0.28 10.90 ?  128 SER   A OG   1 
ATOM   2685 H  H    A SER   A 1 128 ? 20.307 -3.913  -2.929  0.72 12.50 ?  128 SER   A H    1 
ATOM   2686 H  H    B SER   A 1 128 ? 20.325 -3.679  -2.943  0.28 13.17 ?  128 SER   A H    1 
ATOM   2687 H  HA   A SER   A 1 128 ? 19.803 -3.255  -4.799  0.72 12.70 ?  128 SER   A HA   1 
ATOM   2688 H  HA   B SER   A 1 128 ? 19.974 -3.362  -4.974  0.28 12.61 ?  128 SER   A HA   1 
ATOM   2689 H  HB2  A SER   A 1 128 ? 19.176 -5.897  -5.494  0.72 13.50 ?  128 SER   A HB2  1 
ATOM   2690 H  HB2  B SER   A 1 128 ? 19.369 -6.098  -5.043  0.28 12.72 ?  128 SER   A HB2  1 
ATOM   2691 H  HB3  A SER   A 1 128 ? 19.349 -4.710  -6.539  0.72 13.50 ?  128 SER   A HB3  1 
ATOM   2692 H  HB3  B SER   A 1 128 ? 19.272 -5.201  -6.351  0.28 12.72 ?  128 SER   A HB3  1 
ATOM   2693 H  HG   A SER   A 1 128 ? 21.440 -4.575  -5.870  0.72 14.31 ?  128 SER   A HG   1 
ATOM   2694 H  HG   B SER   A 1 128 ? 21.399 -4.752  -6.071  0.28 13.04 ?  128 SER   A HG   1 
ATOM   2695 N  N    A ALA   A 1 129 ? 17.090 -3.546  -3.564  0.72 11.94 ?  129 ALA   A N    1 
ATOM   2696 N  N    B ALA   A 1 129 ? 17.175 -3.591  -3.760  0.28 10.42 ?  129 ALA   A N    1 
ATOM   2697 C  CA   A ALA   A 1 129 ? 15.718 -3.054  -3.561  0.72 12.56 ?  129 ALA   A CA   1 
ATOM   2698 C  CA   B ALA   A 1 129 ? 15.813 -3.078  -3.815  0.28 10.93 ?  129 ALA   A CA   1 
ATOM   2699 C  C    A ALA   A 1 129 ? 15.697 -1.524  -3.545  0.72 12.28 ?  129 ALA   A C    1 
ATOM   2700 C  C    B ALA   A 1 129 ? 15.848 -1.562  -3.616  0.28 11.39 ?  129 ALA   A C    1 
ATOM   2701 O  O    A ALA   A 1 129 ? 16.732 -0.855  -3.639  0.72 12.27 ?  129 ALA   A O    1 
ATOM   2702 O  O    B ALA   A 1 129 ? 16.915 -0.942  -3.572  0.28 11.48 ?  129 ALA   A O    1 
ATOM   2703 C  CB   A ALA   A 1 129 ? 14.944 -3.641  -2.379  0.72 14.08 ?  129 ALA   A CB   1 
ATOM   2704 C  CB   B ALA   A 1 129 ? 14.929 -3.807  -2.805  0.28 11.00 ?  129 ALA   A CB   1 
ATOM   2705 H  H    A ALA   A 1 129 ? 17.371 -3.795  -2.786  0.72 14.29 ?  129 ALA   A H    1 
ATOM   2706 H  H    B ALA   A 1 129 ? 17.406 -3.869  -2.982  0.28 12.47 ?  129 ALA   A H    1 
ATOM   2707 H  HA   A ALA   A 1 129 ? 15.283 -3.339  -4.373  0.72 15.04 ?  129 ALA   A HA   1 
ATOM   2708 H  HA   B ALA   A 1 129 ? 15.460 -3.250  -4.695  0.28 13.09 ?  129 ALA   A HA   1 
ATOM   2709 H  HB1  A ALA   A 1 129 ? 14.031 -3.312  -2.405  0.72 16.87 ?  129 ALA   A HB1  1 
ATOM   2710 H  HB1  B ALA   A 1 129 ? 14.031 -3.449  -2.862  0.28 13.17 ?  129 ALA   A HB1  1 
ATOM   2711 H  HB2  A ALA   A 1 129 ? 14.949 -4.607  -2.447  0.72 16.87 ?  129 ALA   A HB2  1 
ATOM   2712 H  HB2  B ALA   A 1 129 ? 14.926 -4.751  -3.017  0.28 13.17 ?  129 ALA   A HB2  1 
ATOM   2713 H  HB3  A ALA   A 1 129 ? 15.369 -3.366  -1.550  0.72 16.87 ?  129 ALA   A HB3  1 
ATOM   2714 H  HB3  B ALA   A 1 129 ? 15.286 -3.668  -1.913  0.28 13.17 ?  129 ALA   A HB3  1 
ATOM   2715 N  N    A GLY   A 1 130 ? 14.495 -0.964  -3.450  0.72 12.53 ?  130 GLY   A N    1 
ATOM   2716 N  N    B GLY   A 1 130 ? 14.678 -0.942  -3.500  0.28 11.96 ?  130 GLY   A N    1 
ATOM   2717 C  CA   A GLY   A 1 130 ? 14.356 0.481   -3.405  0.72 13.01 ?  130 GLY   A CA   1 
ATOM   2718 C  CA   B GLY   A 1 130 ? 14.642 0.505   -3.368  0.28 12.55 ?  130 GLY   A CA   1 
ATOM   2719 C  C    A GLY   A 1 130 ? 14.975 1.121   -4.627  0.72 12.15 ?  130 GLY   A C    1 
ATOM   2720 C  C    B GLY   A 1 130 ? 15.232 1.164   -4.597  0.28 12.78 ?  130 GLY   A C    1 
ATOM   2721 O  O    A GLY   A 1 130 ? 14.757 0.674   -5.758  0.72 12.21 ?  130 GLY   A O    1 
ATOM   2722 O  O    B GLY   A 1 130 ? 14.952 0.771   -5.734  0.28 13.28 ?  130 GLY   A O    1 
ATOM   2723 H  H    A GLY   A 1 130 ? 13.755 -1.397  -3.418  0.72 15.01 ?  130 GLY   A H    1 
ATOM   2724 H  H    B GLY   A 1 130 ? 13.911 -1.328  -3.493  0.28 14.33 ?  130 GLY   A H    1 
ATOM   2725 H  HA2  A GLY   A 1 130 ? 13.414 0.717   -3.372  0.72 15.58 ?  130 GLY   A HA2  1 
ATOM   2726 H  HA2  B GLY   A 1 130 ? 13.724 0.806   -3.243  0.28 15.03 ?  130 GLY   A HA2  1 
ATOM   2727 H  HA3  A GLY   A 1 130 ? 14.794 0.832   -2.619  0.72 15.58 ?  130 GLY   A HA3  1 
ATOM   2728 H  HA3  B GLY   A 1 130 ? 15.165 0.775   -2.602  0.28 15.03 ?  130 GLY   A HA3  1 
ATOM   2729 N  N    A ILE   A 1 131 ? 15.749 2.191   -4.402  0.72 12.53 ?  131 ILE   A N    1 
ATOM   2730 N  N    B ILE   A 1 131 ? 16.084 2.169   -4.372  0.28 12.56 ?  131 ILE   A N    1 
ATOM   2731 C  CA   A ILE   A 1 131 ? 16.318 2.972   -5.499  0.72 12.31 ?  131 ILE   A CA   1 
ATOM   2732 C  CA   B ILE   A 1 131 ? 16.642 2.953   -5.470  0.28 12.47 ?  131 ILE   A CA   1 
ATOM   2733 C  C    A ILE   A 1 131 ? 17.372 2.219   -6.301  0.72 12.17 ?  131 ILE   A C    1 
ATOM   2734 C  C    B ILE   A 1 131 ? 17.597 2.166   -6.355  0.28 12.37 ?  131 ILE   A C    1 
ATOM   2735 O  O    A ILE   A 1 131 ? 17.803 2.724   -7.346  0.72 13.19 ?  131 ILE   A O    1 
ATOM   2736 O  O    B ILE   A 1 131 ? 17.962 2.657   -7.430  0.28 12.85 ?  131 ILE   A O    1 
ATOM   2737 C  CB   A ILE   A 1 131 ? 16.837 4.356   -5.044  0.72 13.54 ?  131 ILE   A CB   1 
ATOM   2738 C  CB   B ILE   A 1 131 ? 17.306 4.251   -4.958  0.28 12.51 ?  131 ILE   A CB   1 
ATOM   2739 C  CG1  A ILE   A 1 131 ? 18.055 4.232   -4.120  0.72 14.64 ?  131 ILE   A CG1  1 
ATOM   2740 C  CG1  B ILE   A 1 131 ? 18.536 3.940   -4.098  0.28 12.76 ?  131 ILE   A CG1  1 
ATOM   2741 C  CG2  A ILE   A 1 131 ? 15.718 5.150   -4.378  0.72 14.28 ?  131 ILE   A CG2  1 
ATOM   2742 C  CG2  B ILE   A 1 131 ? 16.304 5.081   -4.170  0.28 12.26 ?  131 ILE   A CG2  1 
ATOM   2743 C  CD1  A ILE   A 1 131 ? 18.699 5.577   -3.766  0.72 15.79 ?  131 ILE   A CD1  1 
ATOM   2744 C  CD1  B ILE   A 1 131 ? 19.218 5.184   -3.530  0.28 12.93 ?  131 ILE   A CD1  1 
ATOM   2745 H  H    A ILE   A 1 131 ? 15.941 2.492   -3.617  0.72 15.01 ?  131 ILE   A H    1 
ATOM   2746 H  H    B ILE   A 1 131 ? 16.347 2.416   -3.592  0.28 15.05 ?  131 ILE   A H    1 
ATOM   2747 H  HA   A ILE   A 1 131 ? 15.601 3.153   -6.116  0.72 14.74 ?  131 ILE   A HA   1 
ATOM   2748 H  HA   B ILE   A 1 131 ? 15.909 3.225   -6.037  0.28 14.93 ?  131 ILE   A HA   1 
ATOM   2749 H  HB   A ILE   A 1 131 ? 17.113 4.843   -5.833  0.72 16.22 ?  131 ILE   A HB   1 
ATOM   2750 H  HB   B ILE   A 1 131 ? 17.593 4.769   -5.727  0.28 14.98 ?  131 ILE   A HB   1 
ATOM   2751 H  HG12 A ILE   A 1 131 ? 17.782 3.808   -3.291  0.72 17.54 ?  131 ILE   A HG12 1 
ATOM   2752 H  HG12 B ILE   A 1 131 ? 18.264 3.386   -3.351  0.28 15.29 ?  131 ILE   A HG12 1 
ATOM   2753 H  HG13 A ILE   A 1 131 ? 18.733 3.692   -4.557  0.72 17.54 ?  131 ILE   A HG13 1 
ATOM   2754 H  HG13 B ILE   A 1 131 ? 19.189 3.470   -4.638  0.28 15.29 ?  131 ILE   A HG13 1 
ATOM   2755 H  HG21 A ILE   A 1 131 ? 16.017 6.061   -4.231  0.72 17.11 ?  131 ILE   A HG21 1 
ATOM   2756 H  HG21 B ILE   A 1 131 ? 16.665 5.971   -4.033  0.28 14.68 ?  131 ILE   A HG21 1 
ATOM   2757 H  HG22 A ILE   A 1 131 ? 14.942 5.148   -4.962  0.72 17.11 ?  131 ILE   A HG22 1 
ATOM   2758 H  HG22 B ILE   A 1 131 ? 15.476 5.135   -4.673  0.28 14.68 ?  131 ILE   A HG22 1 
ATOM   2759 H  HG23 A ILE   A 1 131 ? 15.493 4.733   -3.531  0.72 17.11 ?  131 ILE   A HG23 1 
ATOM   2760 H  HG23 B ILE   A 1 131 ? 16.143 4.652   -3.315  0.28 14.68 ?  131 ILE   A HG23 1 
ATOM   2761 H  HD11 A ILE   A 1 131 ? 19.517 5.418   -3.268  0.72 18.91 ?  131 ILE   A HD11 1 
ATOM   2762 H  HD11 B ILE   A 1 131 ? 20.076 4.932   -3.152  0.28 15.48 ?  131 ILE   A HD11 1 
ATOM   2763 H  HD12 A ILE   A 1 131 ? 18.900 6.059   -4.585  0.72 18.91 ?  131 ILE   A HD12 1 
ATOM   2764 H  HD12 B ILE   A 1 131 ? 19.350 5.830   -4.243  0.28 15.48 ?  131 ILE   A HD12 1 
ATOM   2765 H  HD13 A ILE   A 1 131 ? 18.080 6.094   -3.224  0.72 18.91 ?  131 ILE   A HD13 1 
ATOM   2766 H  HD13 B ILE   A 1 131 ? 18.655 5.570   -2.839  0.28 15.48 ?  131 ILE   A HD13 1 
ATOM   2767 N  N    A PHE   A 1 132 ? 17.798 1.025   -5.859  0.72 12.02 ?  132 PHE   A N    1 
ATOM   2768 N  N    B PHE   A 1 132 ? 18.009 0.959   -5.950  0.28 12.07 ?  132 PHE   A N    1 
ATOM   2769 C  CA   A PHE   A 1 132 ? 18.664 0.185   -6.684  0.72 11.67 ?  132 PHE   A CA   1 
ATOM   2770 C  CA   B PHE   A 1 132 ? 18.920 0.169   -6.773  0.28 12.44 ?  132 PHE   A CA   1 
ATOM   2771 C  C    A PHE   A 1 132 ? 17.898 -0.581  -7.765  0.72 11.91 ?  132 PHE   A C    1 
ATOM   2772 C  C    B PHE   A 1 132 ? 18.225 -0.552  -7.927  0.28 13.27 ?  132 PHE   A C    1 
ATOM   2773 O  O    A PHE   A 1 132 ? 18.524 -1.236  -8.605  0.72 12.77 ?  132 PHE   A O    1 
ATOM   2774 O  O    B PHE   A 1 132 ? 18.914 -1.044  -8.828  0.28 14.01 ?  132 PHE   A O    1 
ATOM   2775 C  CB   A PHE   A 1 132 ? 19.474 -0.787  -5.816  0.72 11.30 ?  132 PHE   A CB   1 
ATOM   2776 C  CB   B PHE   A 1 132 ? 19.726 -0.814  -5.914  0.28 11.73 ?  132 PHE   A CB   1 
ATOM   2777 C  CG   A PHE   A 1 132 ? 20.711 -0.187  -5.173  0.72 11.48 ?  132 PHE   A CG   1 
ATOM   2778 C  CG   B PHE   A 1 132 ? 20.906 -0.187  -5.204  0.28 11.41 ?  132 PHE   A CG   1 
ATOM   2779 C  CD1  A PHE   A 1 132 ? 20.621 0.877   -4.291  0.72 12.55 ?  132 PHE   A CD1  1 
ATOM   2780 C  CD1  B PHE   A 1 132 ? 20.718 0.715   -4.168  0.28 11.76 ?  132 PHE   A CD1  1 
ATOM   2781 C  CD2  A PHE   A 1 132 ? 21.961 -0.754  -5.398  0.72 11.98 ?  132 PHE   A CD2  1 
ATOM   2782 C  CD2  B PHE   A 1 132 ? 22.205 -0.525  -5.559  0.28 11.30 ?  132 PHE   A CD2  1 
ATOM   2783 C  CE1  A PHE   A 1 132 ? 21.762 1.393   -3.685  0.72 13.23 ?  132 PHE   A CE1  1 
ATOM   2784 C  CE1  B PHE   A 1 132 ? 21.804 1.279   -3.512  0.28 11.72 ?  132 PHE   A CE1  1 
ATOM   2785 C  CE2  A PHE   A 1 132 ? 23.098 -0.246  -4.793  0.72 12.51 ?  132 PHE   A CE2  1 
ATOM   2786 C  CE2  B PHE   A 1 132 ? 23.292 0.037   -4.905  0.28 11.53 ?  132 PHE   A CE2  1 
ATOM   2787 C  CZ   A PHE   A 1 132 ? 22.994 0.831   -3.933  0.72 12.94 ?  132 PHE   A CZ   1 
ATOM   2788 C  CZ   B PHE   A 1 132 ? 23.088 0.938   -3.880  0.28 11.64 ?  132 PHE   A CZ   1 
ATOM   2789 H  H    A PHE   A 1 132 ? 17.596 0.684   -5.090  0.72 14.39 ?  132 PHE   A H    1 
ATOM   2790 H  H    B PHE   A 1 132 ? 17.781 0.581   -5.208  0.28 14.45 ?  132 PHE   A H    1 
ATOM   2791 H  HA   A PHE   A 1 132 ? 19.301 0.762   -7.126  0.72 13.98 ?  132 PHE   A HA   1 
ATOM   2792 H  HA   B PHE   A 1 132 ? 19.559 0.779   -7.166  0.28 14.90 ?  132 PHE   A HA   1 
ATOM   2793 H  HB2  A PHE   A 1 132 ? 18.906 -1.116  -5.099  0.72 13.53 ?  132 PHE   A HB2  1 
ATOM   2794 H  HB2  B PHE   A 1 132 ? 19.145 -1.190  -5.236  0.28 14.05 ?  132 PHE   A HB2  1 
ATOM   2795 H  HB3  A PHE   A 1 132 ? 19.763 -1.531  -6.367  0.72 13.53 ?  132 PHE   A HB3  1 
ATOM   2796 H  HB3  B PHE   A 1 132 ? 20.068 -1.524  -6.483  0.28 14.05 ?  132 PHE   A HB3  1 
ATOM   2797 H  HD1  A PHE   A 1 132 ? 19.796 1.260   -4.114  0.72 15.04 ?  132 PHE   A HD1  1 
ATOM   2798 H  HD1  B PHE   A 1 132 ? 19.857 0.950   -3.913  0.28 14.08 ?  132 PHE   A HD1  1 
ATOM   2799 H  HD2  A PHE   A 1 132 ? 22.039 -1.481  -5.975  0.72 14.34 ?  132 PHE   A HD2  1 
ATOM   2800 H  HD2  B PHE   A 1 132 ? 22.349 -1.134  -6.248  0.28 13.53 ?  132 PHE   A HD2  1 
ATOM   2801 H  HE1  A PHE   A 1 132 ? 21.695 2.120   -3.105  0.72 15.85 ?  132 PHE   A HE1  1 
ATOM   2802 H  HE1  B PHE   A 1 132 ? 21.666 1.889   -2.822  0.28 14.03 ?  132 PHE   A HE1  1 
ATOM   2803 H  HE2  A PHE   A 1 132 ? 23.932 -0.626  -4.969  0.72 14.99 ?  132 PHE   A HE2  1 
ATOM   2804 H  HE2  B PHE   A 1 132 ? 24.158 -0.196  -5.159  0.28 13.80 ?  132 PHE   A HE2  1 
ATOM   2805 H  HZ   A PHE   A 1 132 ? 23.758 1.182   -3.531  0.72 15.50 ?  132 PHE   A HZ   1 
ATOM   2806 H  HZ   B PHE   A 1 132 ? 23.818 1.318   -3.444  0.28 13.94 ?  132 PHE   A HZ   1 
ATOM   2807 N  N    A GLY   A 1 133 ? 16.567 -0.543  -7.753  0.72 11.91 ?  133 GLY   A N    1 
ATOM   2808 N  N    B GLY   A 1 133 ? 16.893 -0.642  -7.925  0.28 13.15 ?  133 GLY   A N    1 
ATOM   2809 C  CA   A GLY   A 1 133 ? 15.780 -0.910  -8.914  0.72 12.96 ?  133 GLY   A CA   1 
ATOM   2810 C  CA   B GLY   A 1 133 ? 16.132 -1.001  -9.105  0.28 13.30 ?  133 GLY   A CA   1 
ATOM   2811 C  C    A GLY   A 1 133 ? 15.513 -2.386  -9.150  0.72 13.61 ?  133 GLY   A C    1 
ATOM   2812 C  C    B GLY   A 1 133 ? 15.463 -2.362  -9.076  0.28 13.33 ?  133 GLY   A C    1 
ATOM   2813 O  O    A GLY   A 1 133 ? 14.918 -2.717  -10.181 0.72 14.77 ?  133 GLY   A O    1 
ATOM   2814 O  O    B GLY   A 1 133 ? 14.558 -2.601  -9.887  0.28 13.47 ?  133 GLY   A O    1 
ATOM   2815 H  H    A GLY   A 1 133 ? 16.096 -0.302  -7.075  0.72 14.26 ?  133 GLY   A H    1 
ATOM   2816 H  H    B GLY   A 1 133 ? 16.407 -0.501  -7.231  0.28 15.74 ?  133 GLY   A H    1 
ATOM   2817 H  HA2  A GLY   A 1 133 ? 14.917 -0.475  -8.846  0.72 15.52 ?  133 GLY   A HA2  1 
ATOM   2818 H  HA2  B GLY   A 1 133 ? 15.435 -0.349  -9.234  0.28 15.93 ?  133 GLY   A HA2  1 
ATOM   2819 H  HA3  A GLY   A 1 133 ? 16.222 -0.562  -9.706  0.72 15.52 ?  133 GLY   A HA3  1 
ATOM   2820 H  HA3  B GLY   A 1 133 ? 16.714 -0.957  -9.879  0.28 15.93 ?  133 GLY   A HA3  1 
ATOM   2821 N  N    A ALA   A 1 134 ? 15.927 -3.287  -8.261  0.72 13.21 ?  134 ALA   A N    1 
ATOM   2822 N  N    B ALA   A 1 134 ? 15.860 -3.254  -8.176  0.28 13.21 ?  134 ALA   A N    1 
ATOM   2823 C  CA   A ALA   A 1 134 ? 15.596 -4.694  -8.446  0.72 13.61 ?  134 ALA   A CA   1 
ATOM   2824 C  CA   B ALA   A 1 134 ? 15.399 -4.634  -8.233  0.28 13.30 ?  134 ALA   A CA   1 
ATOM   2825 C  C    A ALA   A 1 134 ? 14.229 -5.014  -7.834  0.72 13.37 ?  134 ALA   A C    1 
ATOM   2826 C  C    B ALA   A 1 134 ? 14.111 -4.833  -7.440  0.28 13.16 ?  134 ALA   A C    1 
ATOM   2827 O  O    A ALA   A 1 134 ? 13.656 -4.232  -7.071  0.72 14.41 ?  134 ALA   A O    1 
ATOM   2828 O  O    B ALA   A 1 134 ? 13.771 -4.058  -6.543  0.28 13.48 ?  134 ALA   A O    1 
ATOM   2829 C  CB   A ALA   A 1 134 ? 16.680 -5.594  -7.852  0.72 14.61 ?  134 ALA   A CB   1 
ATOM   2830 C  CB   B ALA   A 1 134 ? 16.470 -5.583  -7.703  0.28 13.40 ?  134 ALA   A CB   1 
ATOM   2831 H  H    A ALA   A 1 134 ? 16.404 -3.109  -7.561  0.72 15.82 ?  134 ALA   A H    1 
ATOM   2832 H  H    B ALA   A 1 134 ? 16.389 -3.079  -7.524  0.28 15.82 ?  134 ALA   A H    1 
ATOM   2833 H  HA   A ALA   A 1 134 ? 15.552 -4.877  -9.398  0.72 16.30 ?  134 ALA   A HA   1 
ATOM   2834 H  HA   B ALA   A 1 134 ? 15.219 -4.861  -9.158  0.28 15.92 ?  134 ALA   A HA   1 
ATOM   2835 H  HB1  A ALA   A 1 134 ? 16.436 -6.519  -8.005  0.72 17.50 ?  134 ALA   A HB1  1 
ATOM   2836 H  HB1  B ALA   A 1 134 ? 16.137 -6.490  -7.766  0.28 16.05 ?  134 ALA   A HB1  1 
ATOM   2837 H  HB2  A ALA   A 1 134 ? 17.528 -5.400  -8.287  0.72 17.50 ?  134 ALA   A HB2  1 
ATOM   2838 H  HB2  B ALA   A 1 134 ? 17.268 -5.479  -8.242  0.28 16.05 ?  134 ALA   A HB2  1 
ATOM   2839 H  HB3  A ALA   A 1 134 ? 16.751 -5.420  -6.902  0.72 17.50 ?  134 ALA   A HB3  1 
ATOM   2840 H  HB3  B ALA   A 1 134 ? 16.657 -5.358  -6.780  0.28 16.05 ?  134 ALA   A HB3  1 
ATOM   2841 N  N    A ASP   A 1 135 ? 13.708 -6.189  -8.186  0.72 13.59 ?  135 ASP   A N    1 
ATOM   2842 N  N    B ASP   A 1 135 ? 13.403 -5.904  -7.784  0.28 13.31 ?  135 ASP   A N    1 
ATOM   2843 C  CA   A ASP   A 1 135 ? 12.444 -6.672  -7.634  0.72 14.62 ?  135 ASP   A CA   1 
ATOM   2844 C  CA   B ASP   A 1 135 ? 12.165 -6.274  -7.111  0.28 13.30 ?  135 ASP   A CA   1 
ATOM   2845 C  C    A ASP   A 1 135 ? 12.670 -7.104  -6.191  0.72 13.83 ?  135 ASP   A C    1 
ATOM   2846 C  C    B ASP   A 1 135 ? 12.488 -6.786  -5.712  0.28 12.58 ?  135 ASP   A C    1 
ATOM   2847 O  O    A ASP   A 1 135 ? 13.467 -8.021  -5.951  0.72 14.03 ?  135 ASP   A O    1 
ATOM   2848 O  O    B ASP   A 1 135 ? 13.225 -7.772  -5.580  0.28 12.77 ?  135 ASP   A O    1 
ATOM   2849 C  CB   A ASP   A 1 135 ? 11.968 -7.859  -8.467  0.72 17.26 ?  135 ASP   A CB   1 
ATOM   2850 C  CB   B ASP   A 1 135 ? 11.500 -7.379  -7.923  0.28 14.05 ?  135 ASP   A CB   1 
ATOM   2851 C  CG   A ASP   A 1 135 ? 10.666 -8.473  -7.956  0.72 19.70 ?  135 ASP   A CG   1 
ATOM   2852 C  CG   B ASP   A 1 135 ? 10.099 -7.708  -7.442  0.28 15.21 ?  135 ASP   A CG   1 
ATOM   2853 O  OD1  A ASP   A 1 135 ? 10.136 -8.033  -6.916  0.72 20.04 ?  135 ASP   A OD1  1 
ATOM   2854 O  OD1  B ASP   A 1 135 ? 9.779  -7.417  -6.270  0.28 15.08 ?  135 ASP   A OD1  1 
ATOM   2855 O  OD2  A ASP   A 1 135 ? 10.168 -9.409  -8.615  0.72 22.29 -1 135 ASP   A OD2  1 
ATOM   2856 O  OD2  B ASP   A 1 135 ? 9.321  -8.279  -8.239  0.28 16.29 -1 135 ASP   A OD2  1 
ATOM   2857 H  H    A ASP   A 1 135 ? 14.075 -6.729  -8.746  0.72 16.27 ?  135 ASP   A H    1 
ATOM   2858 H  H    B ASP   A 1 135 ? 13.619 -6.439  -8.417  0.28 15.94 ?  135 ASP   A H    1 
ATOM   2859 H  HA   A ASP   A 1 135 ? 11.780 -5.966  -7.676  0.72 17.51 ?  135 ASP   A HA   1 
ATOM   2860 H  HA   B ASP   A 1 135 ? 11.566 -5.507  -7.069  0.28 15.93 ?  135 ASP   A HA   1 
ATOM   2861 H  HB2  A ASP   A 1 135 ? 11.814 -7.563  -9.376  0.72 20.68 ?  135 ASP   A HB2  1 
ATOM   2862 H  HB2  B ASP   A 1 135 ? 11.462 -7.101  -8.851  0.28 16.83 ?  135 ASP   A HB2  1 
ATOM   2863 H  HB3  A ASP   A 1 135 ? 12.656 -8.545  -8.454  0.72 20.68 ?  135 ASP   A HB3  1 
ATOM   2864 H  HB3  B ASP   A 1 135 ? 12.025 -8.185  -7.836  0.28 16.83 ?  135 ASP   A HB3  1 
ATOM   2865 N  N    A PRO   A 1 136 ? 12.017 -6.481  -5.208  0.72 13.84 ?  136 PRO   A N    1 
ATOM   2866 N  N    B PRO   A 1 136 ? 11.973 -6.159  -4.651  0.28 11.93 ?  136 PRO   A N    1 
ATOM   2867 C  CA   A PRO   A 1 136 ? 12.250 -6.888  -3.812  0.72 13.87 ?  136 PRO   A CA   1 
ATOM   2868 C  CA   B PRO   A 1 136 ? 12.281 -6.644  -3.296  0.28 12.17 ?  136 PRO   A CA   1 
ATOM   2869 C  C    A PRO   A 1 136 ? 11.830 -8.315  -3.504  0.72 13.32 ?  136 PRO   A C    1 
ATOM   2870 C  C    B PRO   A 1 136 ? 11.850 -8.078  -3.043  0.28 11.73 ?  136 PRO   A C    1 
ATOM   2871 O  O    A PRO   A 1 136 ? 12.434 -8.944  -2.629  0.72 13.27 ?  136 PRO   A O    1 
ATOM   2872 O  O    B PRO   A 1 136 ? 12.439 -8.748  -2.187  0.28 10.71 ?  136 PRO   A O    1 
ATOM   2873 C  CB   A PRO   A 1 136 ? 11.443 -5.859  -3.009  0.72 14.65 ?  136 PRO   A CB   1 
ATOM   2874 C  CB   B PRO   A 1 136 ? 11.549 -5.643  -2.388  0.28 12.83 ?  136 PRO   A CB   1 
ATOM   2875 C  CG   A PRO   A 1 136 ? 10.402 -5.369  -3.965  0.72 15.37 ?  136 PRO   A CG   1 
ATOM   2876 C  CG   B PRO   A 1 136 ? 10.503 -5.024  -3.259  0.28 12.67 ?  136 PRO   A CG   1 
ATOM   2877 C  CD   A PRO   A 1 136 ? 11.045 -5.378  -5.312  0.72 14.68 ?  136 PRO   A CD   1 
ATOM   2878 C  CD   B PRO   A 1 136 ? 11.112 -4.966  -4.626  0.28 11.98 ?  136 PRO   A CD   1 
ATOM   2879 H  HA   A PRO   A 1 136 ? 13.193 -6.784  -3.588  0.72 16.62 ?  136 PRO   A HA   1 
ATOM   2880 H  HA   B PRO   A 1 136 ? 13.233 -6.570  -3.127  0.28 14.58 ?  136 PRO   A HA   1 
ATOM   2881 H  HB2  A PRO   A 1 136 ? 11.034 -6.289  -2.242  0.72 17.54 ?  136 PRO   A HB2  1 
ATOM   2882 H  HB2  B PRO   A 1 136 ? 11.140 -6.107  -1.643  0.28 15.36 ?  136 PRO   A HB2  1 
ATOM   2883 H  HB3  A PRO   A 1 136 ? 12.025 -5.133  -2.727  0.72 17.54 ?  136 PRO   A HB3  1 
ATOM   2884 H  HB3  B PRO   A 1 136 ? 12.170 -4.965  -2.072  0.28 15.36 ?  136 PRO   A HB3  1 
ATOM   2885 H  HG2  A PRO   A 1 136 ? 9.641  -5.966  -3.947  0.72 18.41 ?  136 PRO   A HG2  1 
ATOM   2886 H  HG2  B PRO   A 1 136 ? 9.709  -5.583  -3.265  0.28 15.17 ?  136 PRO   A HG2  1 
ATOM   2887 H  HG3  A PRO   A 1 136 ? 10.140 -4.468  -3.723  0.72 18.41 ?  136 PRO   A HG3  1 
ATOM   2888 H  HG3  B PRO   A 1 136 ? 10.290 -4.133  -2.942  0.28 15.17 ?  136 PRO   A HG3  1 
ATOM   2889 H  HD2  A PRO   A 1 136 ? 10.387 -5.578  -5.999  0.72 17.59 ?  136 PRO   A HD2  1 
ATOM   2890 H  HD2  B PRO   A 1 136 ? 10.421 -5.029  -5.306  0.28 14.34 ?  136 PRO   A HD2  1 
ATOM   2891 H  HD3  A PRO   A 1 136 ? 11.498 -4.539  -5.486  0.72 17.59 ?  136 PRO   A HD3  1 
ATOM   2892 H  HD3  B PRO   A 1 136 ? 11.643 -4.159  -4.732  0.28 14.34 ?  136 PRO   A HD3  1 
ATOM   2893 N  N    A ILE   A 1 137 ? 10.799 -8.840  -4.170  0.72 13.41 ?  137 ILE   A N    1 
ATOM   2894 N  N    B ILE   A 1 137 ? 10.833 -8.571  -3.754  0.28 12.39 ?  137 ILE   A N    1 
ATOM   2895 C  CA   A ILE   A 1 137 ? 10.432 -10.240 -3.968  0.72 13.97 ?  137 ILE   A CA   1 
ATOM   2896 C  CA   B ILE   A 1 137 ? 10.428 -9.967  -3.598  0.28 12.69 ?  137 ILE   A CA   1 
ATOM   2897 C  C    A ILE   A 1 137 ? 11.597 -11.139 -4.350  0.72 13.58 ?  137 ILE   A C    1 
ATOM   2898 C  C    B ILE   A 1 137 ? 11.559 -10.896 -4.028  0.28 12.46 ?  137 ILE   A C    1 
ATOM   2899 O  O    A ILE   A 1 137 ? 11.904 -12.123 -3.663  0.72 13.79 ?  137 ILE   A O    1 
ATOM   2900 O  O    B ILE   A 1 137 ? 11.895 -11.863 -3.333  0.28 12.33 ?  137 ILE   A O    1 
ATOM   2901 C  CB   A ILE   A 1 137 ? 9.151  -10.577 -4.757  0.72 15.52 ?  137 ILE   A CB   1 
ATOM   2902 C  CB   B ILE   A 1 137 ? 9.137  -10.245 -4.390  0.28 13.34 ?  137 ILE   A CB   1 
ATOM   2903 C  CG1  A ILE   A 1 137 ? 7.966  -9.755  -4.234  0.72 17.65 ?  137 ILE   A CG1  1 
ATOM   2904 C  CG1  B ILE   A 1 137 ? 8.026  -9.266  -3.997  0.28 14.60 ?  137 ILE   A CG1  1 
ATOM   2905 C  CG2  A ILE   A 1 137 ? 8.850  -12.077 -4.674  0.72 15.82 ?  137 ILE   A CG2  1 
ATOM   2906 C  CG2  B ILE   A 1 137 ? 8.683  -11.687 -4.178  0.28 13.52 ?  137 ILE   A CG2  1 
ATOM   2907 C  CD1  A ILE   A 1 137 ? 6.696  -9.909  -5.045  0.72 18.73 ?  137 ILE   A CD1  1 
ATOM   2908 C  CD1  B ILE   A 1 137 ? 7.043  -9.023  -5.111  0.28 15.37 ?  137 ILE   A CD1  1 
ATOM   2909 H  H    A ILE   A 1 137 ? 10.313 -8.415  -4.733  0.72 16.06 ?  137 ILE   A H    1 
ATOM   2910 H  H    B ILE   A 1 137 ? 10.364 -8.117  -4.319  0.28 14.84 ?  137 ILE   A H    1 
ATOM   2911 H  HA   A ILE   A 1 137 ? 10.253 -10.386 -3.031  0.72 16.73 ?  137 ILE   A HA   1 
ATOM   2912 H  HA   B ILE   A 1 137 ? 10.238 -10.133 -2.660  0.28 15.19 ?  137 ILE   A HA   1 
ATOM   2913 H  HB   A ILE   A 1 137 ? 9.295  -10.349 -5.688  0.72 18.59 ?  137 ILE   A HB   1 
ATOM   2914 H  HB   B ILE   A 1 137 ? 9.324  -10.123 -5.331  0.28 15.98 ?  137 ILE   A HB   1 
ATOM   2915 H  HG12 A ILE   A 1 137 ? 7.779  -10.030 -3.323  0.72 21.15 ?  137 ILE   A HG12 1 
ATOM   2916 H  HG12 B ILE   A 1 137 ? 7.536  -9.632  -3.245  0.28 17.50 ?  137 ILE   A HG12 1 
ATOM   2917 H  HG13 A ILE   A 1 137 ? 8.215  -8.815  -4.246  0.72 21.15 ?  137 ILE   A HG13 1 
ATOM   2918 H  HG13 B ILE   A 1 137 ? 8.410  -8.409  -3.750  0.28 17.50 ?  137 ILE   A HG13 1 
ATOM   2919 H  HG21 A ILE   A 1 137 ? 7.958  -12.252 -5.010  0.72 18.96 ?  137 ILE   A HG21 1 
ATOM   2920 H  HG21 B ILE   A 1 137 ? 7.794  -11.797 -4.551  0.28 16.20 ?  137 ILE   A HG21 1 
ATOM   2921 H  HG22 A ILE   A 1 137 ? 9.498  -12.561 -5.209  0.72 18.96 ?  137 ILE   A HG22 1 
ATOM   2922 H  HG22 B ILE   A 1 137 ? 9.304  -12.284 -4.623  0.28 16.20 ?  137 ILE   A HG22 1 
ATOM   2923 H  HG23 A ILE   A 1 137 ? 8.910  -12.357 -3.747  0.72 18.96 ?  137 ILE   A HG23 1 
ATOM   2924 H  HG23 B ILE   A 1 137 ? 8.665  -11.877 -3.226  0.28 16.20 ?  137 ILE   A HG23 1 
ATOM   2925 H  HD11 A ILE   A 1 137 ? 5.974  -10.158 -4.450  0.72 22.44 ?  137 ILE   A HD11 1 
ATOM   2926 H  HD11 B ILE   A 1 137 ? 6.422  -8.332  -4.838  0.28 18.41 ?  137 ILE   A HD11 1 
ATOM   2927 H  HD12 A ILE   A 1 137 ? 6.505  -9.065  -5.474  0.72 22.44 ?  137 ILE   A HD12 1 
ATOM   2928 H  HD12 B ILE   A 1 137 ? 7.532  -8.734  -5.900  0.28 18.41 ?  137 ILE   A HD12 1 
ATOM   2929 H  HD13 A ILE   A 1 137 ? 6.826  -10.595 -5.719  0.72 22.44 ?  137 ILE   A HD13 1 
ATOM   2930 H  HD13 B ILE   A 1 137 ? 6.571  -9.846  -5.297  0.28 18.41 ?  137 ILE   A HD13 1 
ATOM   2931 N  N    A HIS   A 1 138 ? 12.274 -10.801 -5.447  0.72 14.03 ?  138 HIS   A N    1 
ATOM   2932 N  N    B HIS   A 1 138 ? 12.162 -10.614 -5.187  0.28 12.85 ?  138 HIS   A N    1 
ATOM   2933 C  CA   A HIS   A 1 138 ? 13.471 -11.535 -5.835  0.72 13.81 ?  138 HIS   A CA   1 
ATOM   2934 C  CA   B HIS   A 1 138 ? 13.266 -11.438 -5.677  0.28 13.04 ?  138 HIS   A CA   1 
ATOM   2935 C  C    A HIS   A 1 138 ? 14.590 -11.367 -4.809  0.72 13.42 ?  138 HIS   A C    1 
ATOM   2936 C  C    B HIS   A 1 138 ? 14.462 -11.358 -4.737  0.28 12.90 ?  138 HIS   A C    1 
ATOM   2937 O  O    A HIS   A 1 138 ? 15.272 -12.341 -4.463  0.72 13.63 ?  138 HIS   A O    1 
ATOM   2938 O  O    B HIS   A 1 138 ? 15.082 -12.376 -4.405  0.28 13.13 ?  138 HIS   A O    1 
ATOM   2939 C  CB   A HIS   A 1 138 ? 13.915 -11.101 -7.230  0.72 14.98 ?  138 HIS   A CB   1 
ATOM   2940 C  CB   B HIS   A 1 138 ? 13.656 -10.993 -7.088  0.28 13.31 ?  138 HIS   A CB   1 
ATOM   2941 C  CG   A HIS   A 1 138 ? 15.160 -11.786 -7.695  0.72 15.79 ?  138 HIS   A CG   1 
ATOM   2942 C  CG   B HIS   A 1 138 ? 14.965 -11.549 -7.558  0.28 13.68 ?  138 HIS   A CG   1 
ATOM   2943 N  ND1  A HIS   A 1 138 ? 15.238 -13.152 -7.868  0.72 17.26 ?  138 HIS   A ND1  1 
ATOM   2944 N  ND1  B HIS   A 1 138 ? 15.103 -12.840 -8.019  0.28 14.70 ?  138 HIS   A ND1  1 
ATOM   2945 C  CD2  A HIS   A 1 138 ? 16.383 -11.295 -8.002  0.72 15.73 ?  138 HIS   A CD2  1 
ATOM   2946 C  CD2  B HIS   A 1 138 ? 16.197 -10.989 -7.635  0.28 13.51 ?  138 HIS   A CD2  1 
ATOM   2947 C  CE1  A HIS   A 1 138 ? 16.453 -13.470 -8.276  0.72 17.41 ?  138 HIS   A CE1  1 
ATOM   2948 C  CE1  B HIS   A 1 138 ? 16.362 -13.051 -8.361  0.28 14.60 ?  138 HIS   A CE1  1 
ATOM   2949 N  NE2  A HIS   A 1 138 ? 17.168 -12.362 -8.364  0.72 16.48 ?  138 HIS   A NE2  1 
ATOM   2950 N  NE2  B HIS   A 1 138 ? 17.046 -11.943 -8.139  0.28 14.04 ?  138 HIS   A NE2  1 
ATOM   2951 H  H    A HIS   A 1 138 ? 12.057 -10.158 -5.985  0.72 16.81 ?  138 HIS   A H    1 
ATOM   2952 H  H    B HIS   A 1 138 ? 11.952 -9.953  -5.698  0.28 15.39 ?  138 HIS   A H    1 
ATOM   2953 H  HA   A HIS   A 1 138 ? 13.251 -12.474 -5.883  0.72 16.54 ?  138 HIS   A HA   1 
ATOM   2954 H  HA   B HIS   A 1 138 ? 12.975 -12.359 -5.719  0.28 15.62 ?  138 HIS   A HA   1 
ATOM   2955 H  HB2  A HIS   A 1 138 ? 13.203 -11.308 -7.866  0.72 17.95 ?  138 HIS   A HB2  1 
ATOM   2956 H  HB2  B HIS   A 1 138 ? 12.967 -11.289 -7.709  0.28 15.94 ?  138 HIS   A HB2  1 
ATOM   2957 H  HB3  A HIS   A 1 138 ? 14.080 -10.146 -7.230  0.72 17.95 ?  138 HIS   A HB3  1 
ATOM   2958 H  HB3  B HIS   A 1 138 ? 13.718 -10.026 -7.109  0.28 15.94 ?  138 HIS   A HB3  1 
ATOM   2959 H  HD1  A HIS   A 1 138 ? 14.589 -13.707 -7.740  0.72 20.69 ?  138 HIS   A HD1  1 
ATOM   2960 H  HD1  B HIS   A 1 138 ? 14.467 -13.418 -8.075  0.28 17.60 ?  138 HIS   A HD1  1 
ATOM   2961 H  HD2  A HIS   A 1 138 ? 16.632 -10.401 -7.977  0.72 18.85 ?  138 HIS   A HD2  1 
ATOM   2962 H  HD2  B HIS   A 1 138 ? 16.419 -10.119 -7.393  0.28 16.18 ?  138 HIS   A HD2  1 
ATOM   2963 H  HE1  A HIS   A 1 138 ? 16.751 -14.327 -8.464  0.72 20.87 ?  138 HIS   A HE1  1 
ATOM   2964 H  HE1  B HIS   A 1 138 ? 16.706 -13.843 -8.700  0.28 17.48 ?  138 HIS   A HE1  1 
ATOM   2965 N  N    . SER   A 1 139 ? 14.804 -10.145 -4.309  1.00 12.85 ?  139 SER   A N    1 
ATOM   2966 C  CA   . SER   A 1 139 ? 15.874 -9.957  -3.341  1.00 12.86 ?  139 SER   A CA   1 
ATOM   2967 C  C    . SER   A 1 139 ? 15.654 -10.799 -2.090  1.00 12.46 ?  139 SER   A C    1 
ATOM   2968 O  O    . SER   A 1 139 ? 16.604 -11.387 -1.559  1.00 12.57 ?  139 SER   A O    1 
ATOM   2969 C  CB   . SER   A 1 139 ? 15.998 -8.479  -2.984  1.00 12.60 ?  139 SER   A CB   1 
ATOM   2970 O  OG   . SER   A 1 139 ? 17.074 -8.311  -2.081  1.00 12.86 ?  139 SER   A OG   1 
ATOM   2971 H  H    A SER   A 1 139 ? 14.363 -9.435  -4.509  0.72 15.39 ?  139 SER   A H    1 
ATOM   2972 H  H    B SER   A 1 139 ? 14.425 -9.414  -4.558  0.28 15.39 ?  139 SER   A H    1 
ATOM   2973 H  HA   . SER   A 1 139 ? 16.715 -10.233 -3.738  1.00 15.41 ?  139 SER   A HA   1 
ATOM   2974 H  HB2  . SER   A 1 139 ? 16.174 -7.961  -3.787  1.00 15.10 ?  139 SER   A HB2  1 
ATOM   2975 H  HB3  . SER   A 1 139 ? 15.174 -8.174  -2.565  1.00 15.10 ?  139 SER   A HB3  1 
ATOM   2976 H  HG   . SER   A 1 139 ? 17.154 -7.498  -1.865  1.00 15.40 ?  139 SER   A HG   1 
ATOM   2977 N  N    . LEU   A 1 140 ? 14.412 -10.863 -1.602  1.00 12.43 ?  140 LEU   A N    1 
ATOM   2978 C  CA   . LEU   A 1 140 ? 14.134 -11.678 -0.424  1.00 12.53 ?  140 LEU   A CA   1 
ATOM   2979 C  C    . LEU   A 1 140 ? 14.402 -13.156 -0.702  1.00 12.43 ?  140 LEU   A C    1 
ATOM   2980 O  O    . LEU   A 1 140 ? 14.953 -13.868 0.150   1.00 13.17 ?  140 LEU   A O    1 
ATOM   2981 C  CB   . LEU   A 1 140 ? 12.693 -11.457 0.029   1.00 13.03 ?  140 LEU   A CB   1 
ATOM   2982 C  CG   . LEU   A 1 140 ? 12.233 -12.310 1.212   1.00 13.20 ?  140 LEU   A CG   1 
ATOM   2983 C  CD1  . LEU   A 1 140 ? 13.135 -12.141 2.431   1.00 13.75 ?  140 LEU   A CD1  1 
ATOM   2984 C  CD2  . LEU   A 1 140 ? 10.776 -12.001 1.568   1.00 14.31 ?  140 LEU   A CD2  1 
ATOM   2985 H  H    . LEU   A 1 140 ? 13.729 -10.450 -1.925  1.00 14.88 ?  140 LEU   A H    1 
ATOM   2986 H  HA   . LEU   A 1 140 ? 14.717 -11.403 0.297   1.00 15.01 ?  140 LEU   A HA   1 
ATOM   2987 H  HB2  . LEU   A 1 140 ? 12.589 -10.533 0.284   1.00 15.60 ?  140 LEU   A HB2  1 
ATOM   2988 H  HB3  . LEU   A 1 140 ? 12.104 -11.662 -0.714  1.00 15.60 ?  140 LEU   A HB3  1 
ATOM   2989 H  HG   . LEU   A 1 140 ? 12.264 -13.246 0.955   1.00 15.81 ?  140 LEU   A HG   1 
ATOM   2990 H  HD11 . LEU   A 1 140 ? 12.756 -12.634 3.178   1.00 16.47 ?  140 LEU   A HD11 1 
ATOM   2991 H  HD12 . LEU   A 1 140 ? 14.015 -12.501 2.220   1.00 16.47 ?  140 LEU   A HD12 1 
ATOM   2992 H  HD13 . LEU   A 1 140 ? 13.203 -11.204 2.650   1.00 16.47 ?  140 LEU   A HD13 1 
ATOM   2993 H  HD21 . LEU   A 1 140 ? 10.501 -12.578 2.306   1.00 17.14 ?  140 LEU   A HD21 1 
ATOM   2994 H  HD22 . LEU   A 1 140 ? 10.703 -11.074 1.835   1.00 17.14 ?  140 LEU   A HD22 1 
ATOM   2995 H  HD23 . LEU   A 1 140 ? 10.216 -12.173 0.796   1.00 17.14 ?  140 LEU   A HD23 1 
ATOM   2996 N  N    . ARG   A 1 141 ? 14.009 -13.635 -1.888  1.00 12.64 ?  141 ARG   A N    1 
ATOM   2997 C  CA   . ARG   A 1 141 ? 14.254 -15.027 -2.255  1.00 13.85 ?  141 ARG   A CA   1 
ATOM   2998 C  C    . ARG   A 1 141 ? 15.752 -15.328 -2.271  1.00 13.00 ?  141 ARG   A C    1 
ATOM   2999 O  O    . ARG   A 1 141 ? 16.207 -16.337 -1.718  1.00 13.36 ?  141 ARG   A O    1 
ATOM   3000 C  CB   . ARG   A 1 141 ? 13.633 -15.287 -3.630  1.00 15.59 ?  141 ARG   A CB   1 
ATOM   3001 C  CG   . ARG   A 1 141 ? 13.615 -16.736 -4.069  1.00 18.31 ?  141 ARG   A CG   1 
ATOM   3002 C  CD   . ARG   A 1 141 ? 12.575 -17.487 -3.305  1.00 20.89 ?  141 ARG   A CD   1 
ATOM   3003 N  NE   . ARG   A 1 141 ? 13.187 -18.264 -2.243  1.00 21.70 ?  141 ARG   A NE   1 
ATOM   3004 C  CZ   . ARG   A 1 141 ? 12.513 -18.835 -1.255  1.00 22.84 ?  141 ARG   A CZ   1 
ATOM   3005 N  NH1  . ARG   A 1 141 ? 11.224 -18.598 -1.069  1.00 22.20 ?  141 ARG   A NH1  1 
ATOM   3006 N  NH2  . ARG   A 1 141 ? 13.150 -19.655 -0.425  1.00 24.08 ?  141 ARG   A NH2  1 
ATOM   3007 H  H    . ARG   A 1 141 ? 13.602 -13.175 -2.494  1.00 15.14 ?  141 ARG   A H    1 
ATOM   3008 H  HA   . ARG   A 1 141 ? 13.833 -15.611 -1.611  1.00 16.60 ?  141 ARG   A HA   1 
ATOM   3009 H  HB2  . ARG   A 1 141 ? 12.717 -14.967 -3.623  1.00 18.67 ?  141 ARG   A HB2  1 
ATOM   3010 H  HB3  . ARG   A 1 141 ? 14.139 -14.791 -4.293  1.00 18.67 ?  141 ARG   A HB3  1 
ATOM   3011 H  HG2  . ARG   A 1 141 ? 13.404 -16.790 -5.016  1.00 21.95 ?  141 ARG   A HG2  1 
ATOM   3012 H  HG3  . ARG   A 1 141 ? 14.482 -17.144 -3.895  1.00 21.95 ?  141 ARG   A HG3  1 
ATOM   3013 H  HD2  . ARG   A 1 141 ? 11.950 -16.862 -2.901  1.00 25.04 ?  141 ARG   A HD2  1 
ATOM   3014 H  HD3  . ARG   A 1 141 ? 12.103 -18.089 -3.904  1.00 25.04 ?  141 ARG   A HD3  1 
ATOM   3015 H  HE   . ARG   A 1 141 ? 14.021 -18.448 -2.313  1.00 26.01 ?  141 ARG   A HE   1 
ATOM   3016 H  HH11 . ARG   A 1 141 ? 10.793 -18.080 -1.606  1.00 26.61 ?  141 ARG   A HH11 1 
ATOM   3017 H  HH12 . ARG   A 1 141 ? 10.802 -18.977 -0.419  1.00 26.61 ?  141 ARG   A HH12 1 
ATOM   3018 H  HH21 . ARG   A 1 141 ? 13.988 -19.810 -0.533  1.00 28.86 ?  141 ARG   A HH21 1 
ATOM   3019 H  HH22 . ARG   A 1 141 ? 12.727 -20.021 0.230   1.00 28.86 ?  141 ARG   A HH22 1 
ATOM   3020 N  N    . VAL   A 1 142 ? 16.541 -14.458 -2.905  1.00 12.47 ?  142 VAL   A N    1 
ATOM   3021 C  CA   . VAL   A 1 142 ? 17.988 -14.669 -2.938  1.00 12.74 ?  142 VAL   A CA   1 
ATOM   3022 C  C    . VAL   A 1 142 ? 18.559 -14.651 -1.527  1.00 12.05 ?  142 VAL   A C    1 
ATOM   3023 O  O    . VAL   A 1 142 ? 19.422 -15.465 -1.182  1.00 12.61 ?  142 VAL   A O    1 
ATOM   3024 C  CB   . VAL   A 1 142 ? 18.684 -13.652 -3.860  1.00 12.73 ?  142 VAL   A CB   1 
ATOM   3025 C  CG1  . VAL   A 1 142 ? 20.201 -13.852 -3.808  1.00 12.84 ?  142 VAL   A CG1  1 
ATOM   3026 C  CG2  . VAL   A 1 142 ? 18.185 -13.790 -5.285  1.00 14.08 ?  142 VAL   A CG2  1 
ATOM   3027 H  H    . VAL   A 1 142 ? 16.273 -13.739 -3.309  1.00 14.94 ?  142 VAL   A H    1 
ATOM   3028 H  HA   . VAL   A 1 142 ? 18.157 -15.542 -3.307  1.00 15.26 ?  142 VAL   A HA   1 
ATOM   3029 H  HB   . VAL   A 1 142 ? 18.492 -12.745 -3.558  1.00 15.25 ?  142 VAL   A HB   1 
ATOM   3030 H  HG11 . VAL   A 1 142 ? 20.611 -13.366 -4.543  1.00 15.38 ?  142 VAL   A HG11 1 
ATOM   3031 H  HG12 . VAL   A 1 142 ? 20.540 -13.508 -2.963  1.00 15.38 ?  142 VAL   A HG12 1 
ATOM   3032 H  HG13 . VAL   A 1 142 ? 20.397 -14.795 -3.886  1.00 15.38 ?  142 VAL   A HG13 1 
ATOM   3033 H  HG21 . VAL   A 1 142 ? 18.658 -13.151 -5.847  1.00 16.86 ?  142 VAL   A HG21 1 
ATOM   3034 H  HG22 . VAL   A 1 142 ? 18.366 -14.692 -5.589  1.00 16.86 ?  142 VAL   A HG22 1 
ATOM   3035 H  HG23 . VAL   A 1 142 ? 17.238 -13.611 -5.303  1.00 16.86 ?  142 VAL   A HG23 1 
ATOM   3036 N  N    . CYS   A 1 143 ? 18.090 -13.729 -0.688  1.00 11.89 ?  143 CYS   A N    1 
ATOM   3037 C  CA   . CYS   A 1 143 ? 18.553 -13.686 0.695   1.00 12.32 ?  143 CYS   A CA   1 
ATOM   3038 C  C    . CYS   A 1 143 ? 18.327 -15.028 1.382   1.00 12.11 ?  143 CYS   A C    1 
ATOM   3039 O  O    . CYS   A 1 143 ? 19.247 -15.617 1.957   1.00 12.15 ?  143 CYS   A O    1 
ATOM   3040 C  CB   . CYS   A 1 143 ? 17.818 -12.579 1.444   1.00 12.70 ?  143 CYS   A CB   1 
ATOM   3041 S  SG   . CYS   A 1 143 ? 18.320 -12.389 3.162   1.00 12.97 ?  143 CYS   A SG   1 
ATOM   3042 H  H    . CYS   A 1 143 ? 17.511 -13.129 -0.893  1.00 14.24 ?  143 CYS   A H    1 
ATOM   3043 H  HA   . CYS   A 1 143 ? 19.503 -13.495 0.708   1.00 14.75 ?  143 CYS   A HA   1 
ATOM   3044 H  HB2  . CYS   A 1 143 ? 17.977 -11.736 0.991   1.00 15.21 ?  143 CYS   A HB2  1 
ATOM   3045 H  HB3  . CYS   A 1 143 ? 16.870 -12.777 1.435   1.00 15.21 ?  143 CYS   A HB3  1 
ATOM   3046 H  HG   . CYS   A 1 143 ? 17.755 -11.442 3.622   1.00 15.53 ?  143 CYS   A HG   1 
ATOM   3047 N  N    . VAL   A 1 144 ? 17.094 -15.525 1.329   1.00 12.70 ?  144 VAL   A N    1 
ATOM   3048 C  CA   . VAL   A 1 144 ? 16.754 -16.763 2.024   1.00 14.15 ?  144 VAL   A CA   1 
ATOM   3049 C  C    . VAL   A 1 144 ? 17.571 -17.932 1.495   1.00 13.94 ?  144 VAL   A C    1 
ATOM   3050 O  O    . VAL   A 1 144 ? 17.941 -18.838 2.253   1.00 14.53 ?  144 VAL   A O    1 
ATOM   3051 C  CB   . VAL   A 1 144 ? 15.235 -16.999 1.911   1.00 16.93 ?  144 VAL   A CB   1 
ATOM   3052 C  CG1  . VAL   A 1 144 ? 14.872 -18.430 2.228   1.00 18.95 ?  144 VAL   A CG1  1 
ATOM   3053 C  CG2  . VAL   A 1 144 ? 14.490 -16.006 2.816   1.00 17.21 ?  144 VAL   A CG2  1 
ATOM   3054 H  H    . VAL   A 1 144 ? 16.436 -15.157 0.903   1.00 15.20 ?  144 VAL   A H    1 
ATOM   3055 H  HA   . VAL   A 1 144 ? 16.960 -16.652 2.960   1.00 16.95 ?  144 VAL   A HA   1 
ATOM   3056 H  HB   . VAL   A 1 144 ? 14.954 -16.815 0.996   1.00 20.29 ?  144 VAL   A HB   1 
ATOM   3057 H  HG11 . VAL   A 1 144 ? 13.919 -18.479 2.415   1.00 22.71 ?  144 VAL   A HG11 1 
ATOM   3058 H  HG12 . VAL   A 1 144 ? 15.084 -18.987 1.464   1.00 22.71 ?  144 VAL   A HG12 1 
ATOM   3059 H  HG13 . VAL   A 1 144 ? 15.374 -18.715 3.004   1.00 22.71 ?  144 VAL   A HG13 1 
ATOM   3060 H  HG21 . VAL   A 1 144 ? 13.534 -16.167 2.754   1.00 20.62 ?  144 VAL   A HG21 1 
ATOM   3061 H  HG22 . VAL   A 1 144 ? 14.785 -16.126 3.731   1.00 20.62 ?  144 VAL   A HG22 1 
ATOM   3062 H  HG23 . VAL   A 1 144 ? 14.685 -15.096 2.526   1.00 20.62 ?  144 VAL   A HG23 1 
ATOM   3063 N  N    . ASP   A 1 145 ? 17.843 -17.950 0.192   1.00 13.97 ?  145 ASP   A N    1 
ATOM   3064 C  CA   . ASP   A 1 145 ? 18.553 -19.056 -0.438  1.00 14.67 ?  145 ASP   A CA   1 
ATOM   3065 C  C    . ASP   A 1 145 ? 20.074 -18.910 -0.395  1.00 14.33 ?  145 ASP   A C    1 
ATOM   3066 O  O    . ASP   A 1 145 ? 20.779 -19.798 -0.886  1.00 16.27 ?  145 ASP   A O    1 
ATOM   3067 C  CB   . ASP   A 1 145 ? 18.105 -19.198 -1.895  1.00 16.22 ?  145 ASP   A CB   1 
ATOM   3068 C  CG   . ASP   A 1 145 ? 16.655 -19.626 -2.025  1.00 18.46 ?  145 ASP   A CG   1 
ATOM   3069 O  OD1  . ASP   A 1 145 ? 16.087 -20.163 -1.052  1.00 18.97 ?  145 ASP   A OD1  1 
ATOM   3070 O  OD2  . ASP   A 1 145 ? 16.083 -19.419 -3.111  1.00 19.93 -1 145 ASP   A OD2  1 
ATOM   3071 H  H    . ASP   A 1 145 ? 17.605 -17.331 -0.361  1.00 16.74 ?  145 ASP   A H    1 
ATOM   3072 H  HA   . ASP   A 1 145 ? 18.315 -19.878 0.022   1.00 17.58 ?  145 ASP   A HA   1 
ATOM   3073 H  HB2  . ASP   A 1 145 ? 18.214 -18.344 -2.342  1.00 19.44 ?  145 ASP   A HB2  1 
ATOM   3074 H  HB3  . ASP   A 1 145 ? 18.654 -19.871 -2.327  1.00 19.44 ?  145 ASP   A HB3  1 
ATOM   3075 N  N    . THR   A 1 146 ? 20.597 -17.819 0.157   1.00 12.77 ?  146 THR   A N    1 
ATOM   3076 C  CA   . THR   A 1 146 ? 22.034 -17.565 0.171   1.00 12.24 ?  146 THR   A CA   1 
ATOM   3077 C  C    . THR   A 1 146 ? 22.597 -17.372 1.565   1.00 12.23 ?  146 THR   A C    1 
ATOM   3078 O  O    . THR   A 1 146 ? 23.664 -17.915 1.874   1.00 13.32 ?  146 THR   A O    1 
ATOM   3079 C  CB   . THR   A 1 146 ? 22.355 -16.319 -0.672  1.00 12.38 ?  146 THR   A CB   1 
ATOM   3080 O  OG1  . THR   A 1 146 ? 21.826 -16.484 -1.988  1.00 12.89 ?  146 THR   A OG1  1 
ATOM   3081 C  CG2  . THR   A 1 146 ? 23.861 -16.090 -0.770  1.00 12.99 ?  146 THR   A CG2  1 
ATOM   3082 H  H    . THR   A 1 146 ? 20.133 -17.196 0.529   1.00 15.29 ?  146 THR   A H    1 
ATOM   3083 H  HA   . THR   A 1 146 ? 22.494 -18.314 -0.229  1.00 14.66 ?  146 THR   A HA   1 
ATOM   3084 H  HB   . THR   A 1 146 ? 21.959 -15.536 -0.256  1.00 14.82 ?  146 THR   A HB   1 
ATOM   3085 H  HG1  . THR   A 1 146 ? 20.989 -16.555 -1.944  1.00 15.43 ?  146 THR   A HG1  1 
ATOM   3086 H  HG21 . THR   A 1 146 ? 24.047 -15.424 -1.448  1.00 15.56 ?  146 THR   A HG21 1 
ATOM   3087 H  HG22 . THR   A 1 146 ? 24.209 -15.784 0.079   1.00 15.56 ?  146 THR   A HG22 1 
ATOM   3088 H  HG23 . THR   A 1 146 ? 24.302 -16.920 -1.015  1.00 15.56 ?  146 THR   A HG23 1 
ATOM   3089 N  N    . VAL   A 1 147 ? 21.919 -16.601 2.407   1.00 11.91 ?  147 VAL   A N    1 
ATOM   3090 C  CA   . VAL   A 1 147 ? 22.408 -16.303 3.745   1.00 12.36 ?  147 VAL   A CA   1 
ATOM   3091 C  C    . VAL   A 1 147 ? 22.084 -17.471 4.663   1.00 12.91 ?  147 VAL   A C    1 
ATOM   3092 O  O    . VAL   A 1 147 ? 20.940 -17.941 4.715   1.00 13.39 ?  147 VAL   A O    1 
ATOM   3093 C  CB   . VAL   A 1 147 ? 21.791 -14.997 4.266   1.00 12.61 ?  147 VAL   A CB   1 
ATOM   3094 C  CG1  . VAL   A 1 147 ? 22.328 -14.684 5.643   1.00 13.51 ?  147 VAL   A CG1  1 
ATOM   3095 C  CG2  . VAL   A 1 147 ? 22.045 -13.852 3.293   1.00 12.45 ?  147 VAL   A CG2  1 
ATOM   3096 H  H    . VAL   A 1 147 ? 21.154 -16.241 2.232   1.00 14.26 ?  147 VAL   A H    1 
ATOM   3097 H  HA   . VAL   A 1 147 ? 23.370 -16.195 3.714   1.00 14.80 ?  147 VAL   A HA   1 
ATOM   3098 H  HB   . VAL   A 1 147 ? 20.832 -15.115 4.344   1.00 15.10 ?  147 VAL   A HB   1 
ATOM   3099 H  HG11 . VAL   A 1 147 ? 22.080 -13.780 5.882   1.00 16.18 ?  147 VAL   A HG11 1 
ATOM   3100 H  HG12 . VAL   A 1 147 ? 21.951 -15.311 6.283   1.00 16.18 ?  147 VAL   A HG12 1 
ATOM   3101 H  HG13 . VAL   A 1 147 ? 23.296 -14.770 5.632   1.00 16.18 ?  147 VAL   A HG13 1 
ATOM   3102 H  HG21 . VAL   A 1 147 ? 21.720 -13.028 3.690   1.00 14.91 ?  147 VAL   A HG21 1 
ATOM   3103 H  HG22 . VAL   A 1 147 ? 22.996 -13.787 3.125   1.00 14.91 ?  147 VAL   A HG22 1 
ATOM   3104 H  HG23 . VAL   A 1 147 ? 21.570 -14.031 2.467   1.00 14.91 ?  147 VAL   A HG23 1 
ATOM   3105 N  N    . ARG   A 1 148 ? 23.104 -17.948 5.376   1.00 13.08 ?  148 ARG   A N    1 
ATOM   3106 C  CA   . ARG   A 1 148 ? 22.969 -19.024 6.342   1.00 13.19 ?  148 ARG   A CA   1 
ATOM   3107 C  C    . ARG   A 1 148 ? 23.097 -18.546 7.776   1.00 13.42 ?  148 ARG   A C    1 
ATOM   3108 O  O    . ARG   A 1 148 ? 22.683 -19.264 8.694   1.00 15.32 ?  148 ARG   A O    1 
ATOM   3109 C  CB   . ARG   A 1 148 ? 24.004 -20.126 6.064   1.00 14.14 ?  148 ARG   A CB   1 
ATOM   3110 C  CG   . ARG   A 1 148 ? 23.842 -20.761 4.693   1.00 15.32 ?  148 ARG   A CG   1 
ATOM   3111 C  CD   . ARG   A 1 148 ? 24.931 -21.794 4.394   1.00 16.18 ?  148 ARG   A CD   1 
ATOM   3112 N  NE   . ARG   A 1 148 ? 26.270 -21.212 4.428   1.00 16.01 ?  148 ARG   A NE   1 
ATOM   3113 C  CZ   . ARG   A 1 148 ? 26.787 -20.469 3.459   1.00 14.90 ?  148 ARG   A CZ   1 
ATOM   3114 N  NH1  . ARG   A 1 148 ? 26.113 -20.222 2.347   1.00 15.42 ?  148 ARG   A NH1  1 
ATOM   3115 N  NH2  . ARG   A 1 148 ? 28.007 -19.953 3.613   1.00 15.56 ?  148 ARG   A NH2  1 
ATOM   3116 H  H    . ARG   A 1 148 ? 23.909 -17.649 5.304   1.00 15.66 ?  148 ARG   A H    1 
ATOM   3117 H  HA   . ARG   A 1 148 ? 22.093 -19.420 6.241   1.00 15.79 ?  148 ARG   A HA   1 
ATOM   3118 H  HB2  . ARG   A 1 148 ? 24.895 -19.756 6.112   1.00 16.94 ?  148 ARG   A HB2  1 
ATOM   3119 H  HB3  . ARG   A 1 148 ? 23.900 -20.834 6.723   1.00 16.94 ?  148 ARG   A HB3  1 
ATOM   3120 H  HG2  . ARG   A 1 148 ? 22.980 -21.202 4.650   1.00 18.35 ?  148 ARG   A HG2  1 
ATOM   3121 H  HG3  . ARG   A 1 148 ? 23.892 -20.063 4.020   1.00 18.35 ?  148 ARG   A HG3  1 
ATOM   3122 H  HD2  . ARG   A 1 148 ? 24.889 -22.500 5.057   1.00 19.38 ?  148 ARG   A HD2  1 
ATOM   3123 H  HD3  . ARG   A 1 148 ? 24.778 -22.166 3.507   1.00 19.38 ?  148 ARG   A HD3  1 
ATOM   3124 H  HE   . ARG   A 1 148 ? 26.757 -21.373 5.113   1.00 19.18 ?  148 ARG   A HE   1 
ATOM   3125 H  HH11 . ARG   A 1 148 ? 25.323 -20.540 2.237   1.00 18.47 ?  148 ARG   A HH11 1 
ATOM   3126 H  HH12 . ARG   A 1 148 ? 26.464 -19.728 1.733   1.00 18.47 ?  148 ARG   A HH12 1 
ATOM   3127 H  HH21 . ARG   A 1 148 ? 28.451 -20.107 4.333   1.00 18.64 ?  148 ARG   A HH21 1 
ATOM   3128 H  HH22 . ARG   A 1 148 ? 28.351 -19.463 2.993   1.00 18.64 ?  148 ARG   A HH22 1 
ATOM   3129 N  N    . THR   A 1 149 ? 23.644 -17.353 7.986   1.00 13.40 ?  149 THR   A N    1 
ATOM   3130 C  CA   . THR   A 1 149 ? 23.718 -16.748 9.302   1.00 13.64 ?  149 THR   A CA   1 
ATOM   3131 C  C    . THR   A 1 149 ? 22.391 -16.052 9.607   1.00 12.86 ?  149 THR   A C    1 
ATOM   3132 O  O    . THR   A 1 149 ? 21.455 -16.050 8.796   1.00 14.14 ?  149 THR   A O    1 
ATOM   3133 C  CB   . THR   A 1 149 ? 24.918 -15.808 9.363   1.00 14.38 ?  149 THR   A CB   1 
ATOM   3134 O  OG1  . THR   A 1 149 ? 24.796 -14.878 8.287   1.00 14.28 ?  149 THR   A OG1  1 
ATOM   3135 C  CG2  . THR   A 1 149 ? 26.231 -16.600 9.254   1.00 14.86 ?  149 THR   A CG2  1 
ATOM   3136 H  H    . THR   A 1 149 ? 23.989 -16.861 7.362   1.00 16.05 ?  149 THR   A H    1 
ATOM   3137 H  HA   . THR   A 1 149 ? 23.846 -17.450 9.959   1.00 16.34 ?  149 THR   A HA   1 
ATOM   3138 H  HB   . THR   A 1 149 ? 24.903 -15.332 10.207  1.00 17.22 ?  149 THR   A HB   1 
ATOM   3139 H  HG1  . THR   A 1 149 ? 25.448 -14.347 8.290   1.00 17.10 ?  149 THR   A HG1  1 
ATOM   3140 H  HG21 . THR   A 1 149 ? 26.985 -15.997 9.309   1.00 17.80 ?  149 THR   A HG21 1 
ATOM   3141 H  HG22 . THR   A 1 149 ? 26.290 -17.248 9.976   1.00 17.80 ?  149 THR   A HG22 1 
ATOM   3142 H  HG23 . THR   A 1 149 ? 26.265 -17.074 8.407   1.00 17.80 ?  149 THR   A HG23 1 
ATOM   3143 N  N    . ASN   A 1 150 ? 22.276 -15.508 10.811  1.00 13.27 ?  150 ASN   A N    1 
ATOM   3144 C  CA   . ASN   A 1 150 ? 20.995 -14.994 11.299  1.00 13.88 ?  150 ASN   A CA   1 
ATOM   3145 C  C    . ASN   A 1 150 ? 20.814 -13.555 10.836  1.00 13.17 ?  150 ASN   A C    1 
ATOM   3146 O  O    . ASN   A 1 150 ? 21.562 -12.659 11.248  1.00 14.56 ?  150 ASN   A O    1 
ATOM   3147 C  CB   . ASN   A 1 150 ? 20.940 -15.104 12.818  1.00 16.62 ?  150 ASN   A CB   1 
ATOM   3148 C  CG   . ASN   A 1 150 ? 20.815 -16.535 13.280  1.00 20.73 ?  150 ASN   A CG   1 
ATOM   3149 O  OD1  . ASN   A 1 150 ? 20.214 -17.360 12.596  1.00 22.09 ?  150 ASN   A OD1  1 
ATOM   3150 N  ND2  . ASN   A 1 150 ? 21.396 -16.845 14.434  1.00 23.16 ?  150 ASN   A ND2  1 
ATOM   3151 H  H    . ASN   A 1 150 ? 22.922 -15.429 11.370  1.00 15.89 ?  150 ASN   A H    1 
ATOM   3152 H  HA   . ASN   A 1 150 ? 20.272 -15.534 10.932  1.00 16.63 ?  150 ASN   A HA   1 
ATOM   3153 H  HB2  . ASN   A 1 150 ? 21.754 -14.737 13.194  1.00 19.91 ?  150 ASN   A HB2  1 
ATOM   3154 H  HB3  . ASN   A 1 150 ? 20.169 -14.618 13.146  1.00 19.91 ?  150 ASN   A HB3  1 
ATOM   3155 H  HD21 . ASN   A 1 150 ? 21.354 -17.653 14.739  1.00 27.76 ?  150 ASN   A HD21 1 
ATOM   3156 H  HD22 . ASN   A 1 150 ? 21.808 -16.242 14.889  1.00 27.76 ?  150 ASN   A HD22 1 
ATOM   3157 N  N    . VAL   A 1 151 ? 19.822 -13.328 9.982   1.00 13.06 ?  151 VAL   A N    1 
ATOM   3158 C  CA   . VAL   A 1 151 ? 19.605 -12.021 9.379   1.00 13.14 ?  151 VAL   A CA   1 
ATOM   3159 C  C    . VAL   A 1 151 ? 18.218 -11.507 9.744   1.00 12.59 ?  151 VAL   A C    1 
ATOM   3160 O  O    . VAL   A 1 151 ? 17.212 -12.222 9.600   1.00 13.98 ?  151 VAL   A O    1 
ATOM   3161 C  CB   . VAL   A 1 151 ? 19.892 -12.019 7.862   1.00 14.46 ?  151 VAL   A CB   1 
ATOM   3162 C  CG1  . VAL   A 1 151 ? 19.061 -13.044 7.118   1.00 15.61 ?  151 VAL   A CG1  1 
ATOM   3163 C  CG2  . VAL   A 1 151 ? 19.721 -10.614 7.279   1.00 14.50 ?  151 VAL   A CG2  1 
ATOM   3164 H  H    . VAL   A 1 151 ? 19.250 -13.925 9.736   1.00 15.64 ?  151 VAL   A H    1 
ATOM   3165 H  HA   . VAL   A 1 151 ? 20.244 -11.407 9.772   1.00 15.74 ?  151 VAL   A HA   1 
ATOM   3166 H  HB   . VAL   A 1 151 ? 20.824 -12.265 7.730   1.00 17.32 ?  151 VAL   A HB   1 
ATOM   3167 H  HG11 . VAL   A 1 151 ? 19.263 -12.998 6.169   1.00 18.70 ?  151 VAL   A HG11 1 
ATOM   3168 H  HG12 . VAL   A 1 151 ? 19.275 -13.933 7.453   1.00 18.70 ?  151 VAL   A HG12 1 
ATOM   3169 H  HG13 . VAL   A 1 151 ? 18.119 -12.860 7.263   1.00 18.70 ?  151 VAL   A HG13 1 
ATOM   3170 H  HG21 . VAL   A 1 151 ? 20.028 -10.615 6.355   1.00 17.37 ?  151 VAL   A HG21 1 
ATOM   3171 H  HG22 . VAL   A 1 151 ? 18.786 -10.366 7.313   1.00 17.37 ?  151 VAL   A HG22 1 
ATOM   3172 H  HG23 . VAL   A 1 151 ? 20.251 -9.989  7.797   1.00 17.37 ?  151 VAL   A HG23 1 
ATOM   3173 N  N    . TYR   A 1 152 ? 18.200 -10.262 10.232  1.00 12.83 ?  152 TYR   A N    1 
ATOM   3174 C  CA   . TYR   A 1 152 ? 17.006 -9.523  10.614  1.00 12.53 ?  152 TYR   A CA   1 
ATOM   3175 C  C    . TYR   A 1 152 ? 16.820 -8.422  9.583   1.00 12.03 ?  152 TYR   A C    1 
ATOM   3176 O  O    . TYR   A 1 152 ? 17.599 -7.462  9.537   1.00 12.28 ?  152 TYR   A O    1 
ATOM   3177 C  CB   . TYR   A 1 152 ? 17.176 -8.976  12.028  1.00 13.46 ?  152 TYR   A CB   1 
ATOM   3178 C  CG   . TYR   A 1 152 ? 17.134 -10.096 13.023  1.00 14.03 ?  152 TYR   A CG   1 
ATOM   3179 C  CD1  . TYR   A 1 152 ? 18.262 -10.862 13.294  1.00 15.25 ?  152 TYR   A CD1  1 
ATOM   3180 C  CD2  . TYR   A 1 152 ? 15.950 -10.438 13.653  1.00 14.45 ?  152 TYR   A CD2  1 
ATOM   3181 C  CE1  . TYR   A 1 152 ? 18.216 -11.921 14.181  1.00 16.85 ?  152 TYR   A CE1  1 
ATOM   3182 C  CE2  . TYR   A 1 152 ? 15.891 -11.504 14.545  1.00 16.16 ?  152 TYR   A CE2  1 
ATOM   3183 C  CZ   . TYR   A 1 152 ? 17.030 -12.238 14.805  1.00 16.96 ?  152 TYR   A CZ   1 
ATOM   3184 O  OH   . TYR   A 1 152 ? 16.984 -13.303 15.685  1.00 19.16 ?  152 TYR   A OH   1 
ATOM   3185 H  H    . TYR   A 1 152 ? 18.922 -9.797  10.343  1.00 15.37 ?  152 TYR   A H    1 
ATOM   3186 H  HA   . TYR   A 1 152 ? 16.238 -10.111 10.594  1.00 15.00 ?  152 TYR   A HA   1 
ATOM   3187 H  HB2  . TYR   A 1 152 ? 18.037 -8.535  12.102  1.00 16.13 ?  152 TYR   A HB2  1 
ATOM   3188 H  HB3  . TYR   A 1 152 ? 16.460 -8.359  12.228  1.00 16.13 ?  152 TYR   A HB3  1 
ATOM   3189 H  HD1  . TYR   A 1 152 ? 19.064 -10.653 12.870  1.00 18.27 ?  152 TYR   A HD1  1 
ATOM   3190 H  HD2  . TYR   A 1 152 ? 15.178 -9.946  13.476  1.00 17.32 ?  152 TYR   A HD2  1 
ATOM   3191 H  HE1  . TYR   A 1 152 ? 18.983 -12.414 14.356  1.00 20.19 ?  152 TYR   A HE1  1 
ATOM   3192 H  HE2  . TYR   A 1 152 ? 15.087 -11.712 14.969  1.00 19.37 ?  152 TYR   A HE2  1 
ATOM   3193 H  HH   . TYR   A 1 152 ? 16.210 -13.377 16.002  1.00 22.96 ?  152 TYR   A HH   1 
ATOM   3194 N  N    A LEU   A 1 153 ? 15.817 -8.601  8.724   0.72 12.20 ?  153 LEU   A N    1 
ATOM   3195 N  N    B LEU   A 1 153 ? 15.774 -8.534  8.776   0.28 12.13 ?  153 LEU   A N    1 
ATOM   3196 C  CA   A LEU   A 1 153 ? 15.552 -7.722  7.592   0.72 12.05 ?  153 LEU   A CA   1 
ATOM   3197 C  CA   B LEU   A 1 153 ? 15.532 -7.573  7.709   0.28 11.85 ?  153 LEU   A CA   1 
ATOM   3198 C  C    A LEU   A 1 153 ? 14.544 -6.643  7.964   0.72 12.13 ?  153 LEU   A C    1 
ATOM   3199 C  C    B LEU   A 1 153 ? 14.575 -6.488  8.185   0.28 11.84 ?  153 LEU   A C    1 
ATOM   3200 O  O    A LEU   A 1 153 ? 13.442 -6.945  8.437   0.72 13.41 ?  153 LEU   A O    1 
ATOM   3201 O  O    B LEU   A 1 153 ? 13.464 -6.784  8.641   0.28 12.48 ?  153 LEU   A O    1 
ATOM   3202 C  CB   A LEU   A 1 153 ? 14.993 -8.529  6.419   0.72 11.78 ?  153 LEU   A CB   1 
ATOM   3203 C  CB   B LEU   A 1 153 ? 14.973 -8.278  6.476   0.28 11.73 ?  153 LEU   A CB   1 
ATOM   3204 C  CG   A LEU   A 1 153 ? 15.944 -9.516  5.742   0.72 12.08 ?  153 LEU   A CG   1 
ATOM   3205 C  CG   B LEU   A 1 153 ? 15.876 -9.365  5.891   0.28 12.21 ?  153 LEU   A CG   1 
ATOM   3206 C  CD1  A LEU   A 1 153 ? 15.164 -10.437 4.814   0.72 12.62 ?  153 LEU   A CD1  1 
ATOM   3207 C  CD1  B LEU   A 1 153 ? 15.132 -10.116 4.798   0.28 12.78 ?  153 LEU   A CD1  1 
ATOM   3208 C  CD2  A LEU   A 1 153 ? 17.005 -8.759  4.966   0.72 11.90 ?  153 LEU   A CD2  1 
ATOM   3209 C  CD2  B LEU   A 1 153 ? 17.186 -8.782  5.362   0.28 12.42 ?  153 LEU   A CD2  1 
ATOM   3210 H  H    A LEU   A 1 153 ? 15.250 -9.252  8.789   0.72 14.61 ?  153 LEU   A H    1 
ATOM   3211 H  H    B LEU   A 1 153 ? 15.181 -9.158  8.830   0.28 14.53 ?  153 LEU   A H    1 
ATOM   3212 H  HA   A LEU   A 1 153 ? 16.375 -7.304  7.314   0.72 14.43 ?  153 LEU   A HA   1 
ATOM   3213 H  HA   B LEU   A 1 153 ? 16.368 -7.155  7.474   0.28 14.19 ?  153 LEU   A HA   1 
ATOM   3214 H  HB2  A LEU   A 1 153 ? 14.229 -9.043  6.736   0.72 14.11 ?  153 LEU   A HB2  1 
ATOM   3215 H  HB2  B LEU   A 1 153 ? 14.131 -8.692  6.718   0.28 14.05 ?  153 LEU   A HB2  1 
ATOM   3216 H  HB3  A LEU   A 1 153 ? 14.696 -7.910  5.736   0.72 14.11 ?  153 LEU   A HB3  1 
ATOM   3217 H  HB3  B LEU   A 1 153 ? 14.825 -7.612  5.789   0.28 14.05 ?  153 LEU   A HB3  1 
ATOM   3218 H  HG   A LEU   A 1 153 ? 16.385 -10.062 6.418   0.72 14.47 ?  153 LEU   A HG   1 
ATOM   3219 H  HG   B LEU   A 1 153 ? 16.097 -9.998  6.592   0.28 14.63 ?  153 LEU   A HG   1 
ATOM   3220 H  HD11 A LEU   A 1 153 ? 15.752 -11.143 4.504   0.72 15.11 ?  153 LEU   A HD11 1 
ATOM   3221 H  HD11 B LEU   A 1 153 ? 15.702 -10.820 4.456   0.28 15.31 ?  153 LEU   A HD11 1 
ATOM   3222 H  HD12 A LEU   A 1 153 ? 14.419 -10.815 5.300   0.72 15.11 ?  153 LEU   A HD12 1 
ATOM   3223 H  HD12 B LEU   A 1 153 ? 14.323 -10.496 5.174   0.28 15.31 ?  153 LEU   A HD12 1 
ATOM   3224 H  HD13 A LEU   A 1 153 ? 14.844 -9.917  4.060   0.72 15.11 ?  153 LEU   A HD13 1 
ATOM   3225 H  HD13 B LEU   A 1 153 ? 14.907 -9.496  4.087   0.28 15.31 ?  153 LEU   A HD13 1 
ATOM   3226 H  HD21 A LEU   A 1 153 ? 17.582 -9.396  4.525   0.72 14.25 ?  153 LEU   A HD21 1 
ATOM   3227 H  HD21 B LEU   A 1 153 ? 17.691 -9.487  4.929   0.28 14.87 ?  153 LEU   A HD21 1 
ATOM   3228 H  HD22 A LEU   A 1 153 ? 16.562 -8.197  4.313   0.72 14.25 ?  153 LEU   A HD22 1 
ATOM   3229 H  HD22 B LEU   A 1 153 ? 16.985 -8.079  4.727   0.28 14.87 ?  153 LEU   A HD22 1 
ATOM   3230 H  HD23 A LEU   A 1 153 ? 17.513 -8.217  5.586   0.72 14.25 ?  153 LEU   A HD23 1 
ATOM   3231 H  HD23 B LEU   A 1 153 ? 17.696 -8.421  6.106   0.28 14.87 ?  153 LEU   A HD23 1 
ATOM   3232 N  N    A ALA   A 1 154 ? 14.915 -5.391  7.711   0.72 11.70 ?  154 ALA   A N    1 
ATOM   3233 N  N    B ALA   A 1 154 ? 15.009 -5.234  8.075   0.28 11.32 ?  154 ALA   A N    1 
ATOM   3234 C  CA   A ALA   A 1 154 ? 14.054 -4.233  7.921   0.72 11.81 ?  154 ALA   A CA   1 
ATOM   3235 C  CA   B ALA   A 1 154 ? 14.175 -4.074  8.354   0.28 11.50 ?  154 ALA   A CA   1 
ATOM   3236 C  C    A ALA   A 1 154 ? 13.565 -3.745  6.564   0.72 11.39 ?  154 ALA   A C    1 
ATOM   3237 C  C    B ALA   A 1 154 ? 13.685 -3.517  7.024   0.28 11.05 ?  154 ALA   A C    1 
ATOM   3238 O  O    A ALA   A 1 154 ? 14.372 -3.381  5.703   0.72 12.26 ?  154 ALA   A O    1 
ATOM   3239 O  O    B ALA   A 1 154 ? 14.492 -3.134  6.171   0.28 10.70 ?  154 ALA   A O    1 
ATOM   3240 C  CB   A ALA   A 1 154 ? 14.820 -3.118  8.632   0.72 12.62 ?  154 ALA   A CB   1 
ATOM   3241 C  CB   B ALA   A 1 154 ? 14.968 -3.014  9.121   0.28 11.76 ?  154 ALA   A CB   1 
ATOM   3242 H  H    A ALA   A 1 154 ? 15.690 -5.187  7.400   0.72 14.01 ?  154 ALA   A H    1 
ATOM   3243 H  H    B ALA   A 1 154 ? 15.807 -5.024  7.827   0.28 13.55 ?  154 ALA   A H    1 
ATOM   3244 H  HA   A ALA   A 1 154 ? 13.288 -4.487  8.460   0.72 14.14 ?  154 ALA   A HA   1 
ATOM   3245 H  HA   B ALA   A 1 154 ? 13.409 -4.334  8.887   0.28 13.77 ?  154 ALA   A HA   1 
ATOM   3246 H  HB1  A ALA   A 1 154 ? 14.227 -2.363  8.759   0.72 15.12 ?  154 ALA   A HB1  1 
ATOM   3247 H  HB1  B ALA   A 1 154 ? 14.391 -2.255  9.302   0.28 14.08 ?  154 ALA   A HB1  1 
ATOM   3248 H  HB2  A ALA   A 1 154 ? 15.130 -3.447  9.490   0.72 15.12 ?  154 ALA   A HB2  1 
ATOM   3249 H  HB2  B ALA   A 1 154 ? 15.280 -3.397  9.957   0.28 14.08 ?  154 ALA   A HB2  1 
ATOM   3250 H  HB3  A ALA   A 1 154 ? 15.577 -2.859  8.083   0.72 15.12 ?  154 ALA   A HB3  1 
ATOM   3251 H  HB3  B ALA   A 1 154 ? 15.725 -2.734  8.583   0.28 14.08 ?  154 ALA   A HB3  1 
ATOM   3252 N  N    A VAL   A 1 155 ? 12.247 -3.741  6.379   0.42 9.39  ?  155 VAL   A N    1 
ATOM   3253 N  N    B VAL   A 1 155 ? 12.368 -3.492  6.840   0.28 11.21 ?  155 VAL   A N    1 
ATOM   3254 C  CA   A VAL   A 1 155 ? 11.600 -3.293  5.149   0.42 11.43 ?  155 VAL   A CA   1 
ATOM   3255 C  CA   B VAL   A 1 155 ? 11.741 -2.993  5.621   0.28 12.86 ?  155 VAL   A CA   1 
ATOM   3256 C  CA   T VAL   A 1 155 ? 11.627 -3.309  5.220   0.30 12.81 ?  155 VAL   A CA   1 
ATOM   3257 C  C    A VAL   A 1 155 ? 10.870 -1.994  5.473   0.42 12.78 ?  155 VAL   A C    1 
ATOM   3258 C  C    B VAL   A 1 155 ? 10.969 -1.727  5.971   0.28 14.73 ?  155 VAL   A C    1 
ATOM   3259 C  C    T VAL   A 1 155 ? 11.024 -1.936  5.532   0.30 12.78 ?  155 VAL   A C    1 
ATOM   3260 O  O    A VAL   A 1 155 ? 9.860  -2.009  6.186   0.42 13.39 ?  155 VAL   A O    1 
ATOM   3261 O  O    B VAL   A 1 155 ? 10.049 -1.764  6.798   0.28 14.54 ?  155 VAL   A O    1 
ATOM   3262 O  O    T VAL   A 1 155 ? 10.194 -1.801  6.431   0.30 12.61 ?  155 VAL   A O    1 
ATOM   3263 C  CB   A VAL   A 1 155 ? 10.629 -4.352  4.604   0.42 12.49 ?  155 VAL   A CB   1 
ATOM   3264 C  CB   B VAL   A 1 155 ? 10.819 -4.049  4.994   0.28 13.04 ?  155 VAL   A CB   1 
ATOM   3265 C  CB   T VAL   A 1 155 ? 10.566 -4.329  4.746   0.30 13.36 ?  155 VAL   A CB   1 
ATOM   3266 C  CG1  A VAL   A 1 155 ? 9.970  -3.871  3.316   0.42 13.00 ?  155 VAL   A CG1  1 
ATOM   3267 C  CG1  B VAL   A 1 155 ? 10.055 -3.460  3.821   0.28 13.30 ?  155 VAL   A CG1  1 
ATOM   3268 C  CG1  T VAL   A 1 155 ? 9.836  -3.816  3.515   0.30 13.73 ?  155 VAL   A CG1  1 
ATOM   3269 C  CG2  A VAL   A 1 155 ? 11.345 -5.681  4.374   0.42 13.65 ?  155 VAL   A CG2  1 
ATOM   3270 C  CG2  B VAL   A 1 155 ? 11.633 -5.260  4.559   0.28 13.40 ?  155 VAL   A CG2  1 
ATOM   3271 C  CG2  T VAL   A 1 155 ? 11.210 -5.681  4.455   0.30 13.92 ?  155 VAL   A CG2  1 
ATOM   3272 H  H    A VAL   A 1 155 ? 11.686 -4.021  6.970   0.42 11.23 ?  155 VAL   A H    1 
ATOM   3273 H  H    B VAL   A 1 155 ? 11.803 -3.770  7.426   0.28 13.42 ?  155 VAL   A H    1 
ATOM   3274 H  HA   A VAL   A 1 155 ? 12.271 -3.120  4.471   0.42 13.69 ?  155 VAL   A HA   1 
ATOM   3275 H  HA   B VAL   A 1 155 ? 12.428 -2.764  4.976   0.28 15.40 ?  155 VAL   A HA   1 
ATOM   3276 H  HB   A VAL   A 1 155 ? 9.927  -4.506  5.258   0.42 14.96 ?  155 VAL   A HB   1 
ATOM   3277 H  HB   B VAL   A 1 155 ? 10.175 -4.339  5.660   0.28 15.61 ?  155 VAL   A HB   1 
ATOM   3278 H  HB   T VAL   A 1 155 ? 9.914  -4.457  5.453   0.30 16.01 ?  155 VAL   A HB   1 
ATOM   3279 H  HG11 A VAL   A 1 155 ? 9.459  -4.603  2.932   0.42 15.57 ?  155 VAL   A HG11 1 
ATOM   3280 H  HG11 B VAL   A 1 155 ? 9.666  -4.184  3.309   0.28 15.92 ?  155 VAL   A HG11 1 
ATOM   3281 H  HG11 T VAL   A 1 155 ? 9.292  -4.533  3.150   0.30 16.44 ?  155 VAL   A HG11 1 
ATOM   3282 H  HG12 A VAL   A 1 155 ? 9.379  -3.131  3.520   0.42 15.57 ?  155 VAL   A HG12 1 
ATOM   3283 H  HG12 B VAL   A 1 155 ? 9.354  -2.879  4.157   0.28 15.92 ?  155 VAL   A HG12 1 
ATOM   3284 H  HG12 T VAL   A 1 155 ? 9.273  -3.071  3.769   0.30 16.44 ?  155 VAL   A HG12 1 
ATOM   3285 H  HG13 A VAL   A 1 155 ? 10.659 -3.590  2.697   0.42 15.57 ?  155 VAL   A HG13 1 
ATOM   3286 H  HG13 B VAL   A 1 155 ? 10.669 -2.955  3.268   0.28 15.92 ?  155 VAL   A HG13 1 
ATOM   3287 H  HG13 T VAL   A 1 155 ? 10.491 -3.533  2.857   0.30 16.44 ?  155 VAL   A HG13 1 
ATOM   3288 H  HG21 A VAL   A 1 155 ? 10.733 -6.302  3.948   0.42 16.35 ?  155 VAL   A HG21 1 
ATOM   3289 H  HG21 B VAL   A 1 155 ? 11.040 -5.904  4.140   0.28 16.05 ?  155 VAL   A HG21 1 
ATOM   3290 H  HG21 T VAL   A 1 155 ? 10.525 -6.304  4.167   0.30 16.67 ?  155 VAL   A HG21 1 
ATOM   3291 H  HG22 A VAL   A 1 155 ? 12.113 -5.529  3.801   0.42 16.35 ?  155 VAL   A HG22 1 
ATOM   3292 H  HG22 B VAL   A 1 155 ? 12.310 -4.975  3.927   0.28 16.05 ?  155 VAL   A HG22 1 
ATOM   3293 H  HG22 T VAL   A 1 155 ? 11.872 -5.570  3.753   0.30 16.67 ?  155 VAL   A HG22 1 
ATOM   3294 H  HG23 A VAL   A 1 155 ? 11.635 -6.037  5.229   0.42 16.35 ?  155 VAL   A HG23 1 
ATOM   3295 H  HG23 B VAL   A 1 155 ? 12.054 -5.657  5.338   0.28 16.05 ?  155 VAL   A HG23 1 
ATOM   3296 H  HG23 T VAL   A 1 155 ? 11.637 -6.009  5.262   0.30 16.67 ?  155 VAL   A HG23 1 
ATOM   3297 N  N    A PHE   A 1 156 ? 11.369 -0.869  4.946   0.42 14.40 ?  156 PHE   A N    1 
ATOM   3298 N  N    B PHE   A 1 156 ? 11.335 -0.614  5.342   0.28 16.53 ?  156 PHE   A N    1 
ATOM   3299 N  N    T PHE   A 1 156 ? 11.458 -0.922  4.778   0.30 13.49 ?  156 PHE   A N    1 
ATOM   3300 C  CA   A PHE   A 1 156 ? 10.839 0.441   5.338   0.42 16.10 ?  156 PHE   A CA   1 
ATOM   3301 C  CA   B PHE   A 1 156 ? 10.730 0.690   5.631   0.28 18.77 ?  156 PHE   A CA   1 
ATOM   3302 C  CA   T PHE   A 1 156 ? 11.051 0.455   5.058   0.30 14.07 ?  156 PHE   A CA   1 
ATOM   3303 C  C    A PHE   A 1 156 ? 9.375  0.605   4.942   0.42 15.68 ?  156 PHE   A C    1 
ATOM   3304 C  C    B PHE   A 1 156 ? 9.624  1.032   4.636   0.28 19.95 ?  156 PHE   A C    1 
ATOM   3305 C  C    T PHE   A 1 156 ? 9.587  0.687   4.716   0.30 14.49 ?  156 PHE   A C    1 
ATOM   3306 O  O    A PHE   A 1 156 ? 8.555  1.106   5.724   0.42 16.30 ?  156 PHE   A O    1 
ATOM   3307 O  O    B PHE   A 1 156 ? 9.612  2.119   4.058   0.28 20.40 ?  156 PHE   A O    1 
ATOM   3308 O  O    T PHE   A 1 156 ? 8.862  1.350   5.468   0.30 14.67 ?  156 PHE   A O    1 
ATOM   3309 C  CB   A PHE   A 1 156 ? 11.684 1.559   4.720   0.42 17.26 ?  156 PHE   A CB   1 
ATOM   3310 C  CB   B PHE   A 1 156 ? 11.808 1.772   5.644   0.28 19.85 ?  156 PHE   A CB   1 
ATOM   3311 C  CB   T PHE   A 1 156 ? 11.926 1.415   4.252   0.30 13.52 ?  156 PHE   A CB   1 
ATOM   3312 C  CG   A PHE   A 1 156 ? 11.164 2.943   5.021   0.42 18.34 ?  156 PHE   A CG   1 
ATOM   3313 C  CG   B PHE   A 1 156 ? 11.340 3.108   6.169   0.28 20.90 ?  156 PHE   A CG   1 
ATOM   3314 C  CG   T PHE   A 1 156 ? 11.587 2.872   4.452   0.30 13.13 ?  156 PHE   A CG   1 
ATOM   3315 C  CD1  A PHE   A 1 156 ? 11.068 3.383   6.331   0.42 18.76 ?  156 PHE   A CD1  1 
ATOM   3316 C  CD1  B PHE   A 1 156 ? 10.282 3.201   7.059   0.28 21.40 ?  156 PHE   A CD1  1 
ATOM   3317 C  CD1  T PHE   A 1 156 ? 11.969 3.527   5.612   0.30 13.96 ?  156 PHE   A CD1  1 
ATOM   3318 C  CD2  A PHE   A 1 156 ? 10.779 3.802   4.001   0.42 19.19 ?  156 PHE   A CD2  1 
ATOM   3319 C  CD2  B PHE   A 1 156 ? 11.970 4.274   5.764   0.28 21.24 ?  156 PHE   A CD2  1 
ATOM   3320 C  CD2  T PHE   A 1 156 ? 10.909 3.587   3.475   0.30 13.44 ?  156 PHE   A CD2  1 
ATOM   3321 C  CE1  A PHE   A 1 156 ? 10.596 4.646   6.623   0.42 19.33 ?  156 PHE   A CE1  1 
ATOM   3322 C  CE1  B PHE   A 1 156 ? 9.862  4.431   7.534   0.28 21.59 ?  156 PHE   A CE1  1 
ATOM   3323 C  CE1  T PHE   A 1 156 ? 11.669 4.863   5.805   0.30 14.19 ?  156 PHE   A CE1  1 
ATOM   3324 C  CE2  A PHE   A 1 156 ? 10.301 5.071   4.288   0.42 19.81 ?  156 PHE   A CE2  1 
ATOM   3325 C  CE2  B PHE   A 1 156 ? 11.555 5.504   6.234   0.28 21.53 ?  156 PHE   A CE2  1 
ATOM   3326 C  CE2  T PHE   A 1 156 ? 10.607 4.928   3.661   0.30 13.78 ?  156 PHE   A CE2  1 
ATOM   3327 C  CZ   A PHE   A 1 156 ? 10.214 5.494   5.600   0.42 19.83 ?  156 PHE   A CZ   1 
ATOM   3328 C  CZ   B PHE   A 1 156 ? 10.501 5.584   7.120   0.28 21.61 ?  156 PHE   A CZ   1 
ATOM   3329 C  CZ   T PHE   A 1 156 ? 10.990 5.564   4.830   0.30 13.81 ?  156 PHE   A CZ   1 
ATOM   3330 H  H    A PHE   A 1 156 ? 12.017 -0.846  4.374   0.42 17.25 ?  156 PHE   A H    1 
ATOM   3331 H  H    B PHE   A 1 156 ? 11.942 -0.584  4.731   0.28 19.81 ?  156 PHE   A H    1 
ATOM   3332 H  H    T PHE   A 1 156 ? 11.989 -1.010  4.108   0.30 16.16 ?  156 PHE   A H    1 
ATOM   3333 H  HA   A PHE   A 1 156 ? 10.905 0.522   6.301   0.42 19.28 ?  156 PHE   A HA   1 
ATOM   3334 H  HA   B PHE   A 1 156 ? 10.342 0.644   6.517   0.28 22.49 ?  156 PHE   A HA   1 
ATOM   3335 H  HA   T PHE   A 1 156 ? 11.176 0.634   6.002   0.30 16.85 ?  156 PHE   A HA   1 
ATOM   3336 H  HB2  A PHE   A 1 156 ? 12.594 1.497   5.065   0.42 20.68 ?  156 PHE   A HB2  1 
ATOM   3337 H  HB2  B PHE   A 1 156 ? 12.542 1.478   6.202   0.28 23.79 ?  156 PHE   A HB2  1 
ATOM   3338 H  HB2  T PHE   A 1 156 ? 12.848 1.283   4.518   0.30 16.19 ?  156 PHE   A HB2  1 
ATOM   3339 H  HB3  A PHE   A 1 156 ? 11.699 1.446   3.755   0.42 20.68 ?  156 PHE   A HB3  1 
ATOM   3340 H  HB3  B PHE   A 1 156 ? 12.122 1.914   4.737   0.28 23.79 ?  156 PHE   A HB3  1 
ATOM   3341 H  HB3  T PHE   A 1 156 ? 11.820 1.210   3.311   0.30 16.19 ?  156 PHE   A HB3  1 
ATOM   3342 H  HD1  A PHE   A 1 156 ? 11.328 2.814   7.025   0.42 22.48 ?  156 PHE   A HD1  1 
ATOM   3343 H  HD1  B PHE   A 1 156 ? 9.848  2.429   7.343   0.28 25.65 ?  156 PHE   A HD1  1 
ATOM   3344 H  HD1  T PHE   A 1 156 ? 12.422 3.054   6.278   0.30 16.72 ?  156 PHE   A HD1  1 
ATOM   3345 H  HD2  A PHE   A 1 156 ? 10.841 3.519   3.117   0.42 22.99 ?  156 PHE   A HD2  1 
ATOM   3346 H  HD2  B PHE   A 1 156 ? 12.681 4.228   5.167   0.28 25.46 ?  156 PHE   A HD2  1 
ATOM   3347 H  HD2  T PHE   A 1 156 ? 10.648 3.158   2.693   0.30 16.10 ?  156 PHE   A HD2  1 
ATOM   3348 H  HE1  A PHE   A 1 156 ? 10.538 4.926   7.509   0.42 23.17 ?  156 PHE   A HE1  1 
ATOM   3349 H  HE1  B PHE   A 1 156 ? 9.151  4.481   8.132   0.28 25.88 ?  156 PHE   A HE1  1 
ATOM   3350 H  HE1  T PHE   A 1 156 ? 11.924 5.285   6.593   0.30 17.00 ?  156 PHE   A HE1  1 
ATOM   3351 H  HE2  A PHE   A 1 156 ? 10.048 5.637   3.599   0.42 23.75 ?  156 PHE   A HE2  1 
ATOM   3352 H  HE2  B PHE   A 1 156 ? 11.988 6.278   5.953   0.28 25.81 ?  156 PHE   A HE2  1 
ATOM   3353 H  HE2  T PHE   A 1 156 ? 10.147 5.395   3.007   0.30 16.51 ?  156 PHE   A HE2  1 
ATOM   3354 H  HZ   A PHE   A 1 156 ? 9.895  6.344   5.798   0.42 23.76 ?  156 PHE   A HZ   1 
ATOM   3355 H  HZ   B PHE   A 1 156 ? 10.221 6.411   7.438   0.28 25.91 ?  156 PHE   A HZ   1 
ATOM   3356 H  HZ   T PHE   A 1 156 ? 10.786 6.460   4.961   0.30 16.54 ?  156 PHE   A HZ   1 
ATOM   3357 N  N    A ASP   A 1 157 ? 9.037  0.228   3.715   0.42 15.54 ?  157 ASP   A N    1 
ATOM   3358 N  N    B ASP   A 1 157 ? 8.681  0.115   4.414   0.28 20.23 ?  157 ASP   A N    1 
ATOM   3359 N  N    T ASP   A 1 157 ? 9.147  0.170   3.577   0.30 14.83 ?  157 ASP   A N    1 
ATOM   3360 C  CA   A ASP   A 1 157 ? 7.717  0.505   3.167   0.42 16.92 ?  157 ASP   A CA   1 
ATOM   3361 C  CA   B ASP   A 1 157 ? 7.534  0.400   3.558   0.28 20.94 ?  157 ASP   A CA   1 
ATOM   3362 C  CA   T ASP   A 1 157 ? 7.840  0.480   3.023   0.30 15.47 ?  157 ASP   A CA   1 
ATOM   3363 C  C    A ASP   A 1 157 ? 6.722  -0.521  3.698   0.42 17.40 ?  157 ASP   A C    1 
ATOM   3364 C  C    B ASP   A 1 157 ? 6.464  -0.650  3.817   0.28 20.83 ?  157 ASP   A C    1 
ATOM   3365 C  C    T ASP   A 1 157 ? 6.810  -0.492  3.587   0.30 16.36 ?  157 ASP   A C    1 
ATOM   3366 O  O    A ASP   A 1 157 ? 6.851  -1.720  3.420   0.42 17.21 ?  157 ASP   A O    1 
ATOM   3367 O  O    B ASP   A 1 157 ? 6.742  -1.852  3.748   0.28 20.77 ?  157 ASP   A O    1 
ATOM   3368 O  O    T ASP   A 1 157 ? 6.912  -1.705  3.370   0.30 16.25 ?  157 ASP   A O    1 
ATOM   3369 C  CB   A ASP   A 1 157 ? 7.794  0.450   1.644   0.42 18.55 ?  157 ASP   A CB   1 
ATOM   3370 C  CB   B ASP   A 1 157 ? 7.937  0.413   2.080   0.28 21.83 ?  157 ASP   A CB   1 
ATOM   3371 C  CB   T ASP   A 1 157 ? 7.929  0.346   1.508   0.30 15.47 ?  157 ASP   A CB   1 
ATOM   3372 C  CG   A ASP   A 1 157 ? 6.519  0.914   0.979   0.42 19.73 ?  157 ASP   A CG   1 
ATOM   3373 C  CG   B ASP   A 1 157 ? 7.171  1.450   1.278   0.28 22.52 ?  157 ASP   A CG   1 
ATOM   3374 C  CG   T ASP   A 1 157 ? 6.764  0.963   0.810   0.30 14.62 ?  157 ASP   A CG   1 
ATOM   3375 O  OD1  A ASP   A 1 157 ? 6.239  2.130   1.007   0.42 20.98 ?  157 ASP   A OD1  1 
ATOM   3376 O  OD1  B ASP   A 1 157 ? 5.951  1.606   1.512   0.28 23.03 ?  157 ASP   A OD1  1 
ATOM   3377 O  OD1  T ASP   A 1 157 ? 5.665  0.392   0.927   0.30 14.27 ?  157 ASP   A OD1  1 
ATOM   3378 O  OD2  A ASP   A 1 157 ? 5.795  0.058   0.428   0.42 19.40 -1 157 ASP   A OD2  1 
ATOM   3379 O  OD2  B ASP   A 1 157 ? 7.789  2.114   0.419   0.28 22.81 -1 157 ASP   A OD2  1 
ATOM   3380 O  OD2  T ASP   A 1 157 ? 6.935  2.020   0.170   0.30 13.68 -1 157 ASP   A OD2  1 
ATOM   3381 H  H    A ASP   A 1 157 ? 9.570  -0.188  3.172   0.42 18.61 ?  157 ASP   A H    1 
ATOM   3382 H  H    B ASP   A 1 157 ? 8.681  -0.681  4.745   0.28 24.24 ?  157 ASP   A H    1 
ATOM   3383 H  H    T ASP   A 1 157 ? 9.608  -0.363  3.083   0.30 17.77 ?  157 ASP   A H    1 
ATOM   3384 H  HA   A ASP   A 1 157 ? 7.438  1.395   3.439   0.42 20.28 ?  157 ASP   A HA   1 
ATOM   3385 H  HA   B ASP   A 1 157 ? 7.167  1.271   3.776   0.28 25.10 ?  157 ASP   A HA   1 
ATOM   3386 H  HA   T ASP   A 1 157 ? 7.585  1.391   3.245   0.30 18.53 ?  157 ASP   A HA   1 
ATOM   3387 H  HB2  A ASP   A 1 157 ? 8.548  0.991   1.349   0.42 22.22 ?  157 ASP   A HB2  1 
ATOM   3388 H  HB2  B ASP   A 1 157 ? 8.889  0.594   2.015   0.28 26.16 ?  157 ASP   A HB2  1 
ATOM   3389 H  HB2  T ASP   A 1 157 ? 8.740  0.762   1.192   0.30 18.53 ?  157 ASP   A HB2  1 
ATOM   3390 H  HB3  A ASP   A 1 157 ? 7.931  -0.470  1.375   0.42 22.22 ?  157 ASP   A HB3  1 
ATOM   3391 H  HB3  B ASP   A 1 157 ? 7.739  -0.447  1.685   0.28 26.16 ?  157 ASP   A HB3  1 
ATOM   3392 H  HB3  T ASP   A 1 157 ? 7.941  -0.598  1.288   0.30 18.53 ?  157 ASP   A HB3  1 
ATOM   3393 N  N    A LYS   A 1 158 ? 5.734  -0.055  4.473   0.42 18.65 ?  158 LYS   A N    1 
ATOM   3394 N  N    B LYS   A 1 158 ? 5.245  -0.191  4.109   0.28 20.62 ?  158 LYS   A N    1 
ATOM   3395 N  N    T LYS   A 1 158 ? 5.817  0.040   4.309   0.30 17.73 ?  158 LYS   A N    1 
ATOM   3396 C  CA   A LYS   A 1 158 ? 4.756  -0.976  5.049   0.42 19.64 ?  158 LYS   A CA   1 
ATOM   3397 C  CA   B LYS   A 1 158 ? 4.183  -1.090  4.552   0.28 20.60 ?  158 LYS   A CA   1 
ATOM   3398 C  CA   T LYS   A 1 158 ? 4.827  -0.829  4.939   0.30 19.22 ?  158 LYS   A CA   1 
ATOM   3399 C  C    A LYS   A 1 158 ? 3.998  -1.714  3.958   0.42 18.98 ?  158 LYS   A C    1 
ATOM   3400 C  C    B LYS   A 1 158 ? 3.691  -1.982  3.415   0.28 19.06 ?  158 LYS   A C    1 
ATOM   3401 C  C    T LYS   A 1 158 ? 4.047  -1.621  3.900   0.30 19.04 ?  158 LYS   A C    1 
ATOM   3402 O  O    A LYS   A 1 158 ? 3.764  -2.923  4.063   0.42 19.26 ?  158 LYS   A O    1 
ATOM   3403 O  O    B LYS   A 1 158 ? 3.671  -3.213  3.538   0.28 18.26 ?  158 LYS   A O    1 
ATOM   3404 O  O    T LYS   A 1 158 ? 3.777  -2.812  4.092   0.30 19.14 ?  158 LYS   A O    1 
ATOM   3405 C  CB   A LYS   A 1 158 ? 3.778  -0.234  5.963   0.42 21.69 ?  158 LYS   A CB   1 
ATOM   3406 C  CB   B LYS   A 1 158 ? 3.025  -0.264  5.124   0.28 22.01 ?  158 LYS   A CB   1 
ATOM   3407 C  CB   T LYS   A 1 158 ? 3.873  -0.018  5.820   0.30 21.29 ?  158 LYS   A CB   1 
ATOM   3408 C  CG   A LYS   A 1 158 ? 2.533  -1.050  6.372   0.42 23.79 ?  158 LYS   A CG   1 
ATOM   3409 C  CG   B LYS   A 1 158 ? 2.476  -0.747  6.463   0.28 23.41 ?  158 LYS   A CG   1 
ATOM   3410 C  CG   T LYS   A 1 158 ? 2.647  -0.803  6.300   0.30 23.21 ?  158 LYS   A CG   1 
ATOM   3411 C  CD   A LYS   A 1 158 ? 2.872  -2.354  7.109   0.42 25.32 ?  158 LYS   A CD   1 
ATOM   3412 C  CD   B LYS   A 1 158 ? 2.370  -2.262  6.532   0.28 24.57 ?  158 LYS   A CD   1 
ATOM   3413 C  CD   T LYS   A 1 158 ? 3.031  -2.020  7.139   0.30 24.83 ?  158 LYS   A CD   1 
ATOM   3414 C  CE   A LYS   A 1 158 ? 1.616  -3.027  7.668   0.42 26.34 ?  158 LYS   A CE   1 
ATOM   3415 C  CE   B LYS   A 1 158 ? 1.412  -2.701  7.626   0.28 25.38 ?  158 LYS   A CE   1 
ATOM   3416 C  CE   T LYS   A 1 158 ? 1.802  -2.841  7.525   0.30 26.05 ?  158 LYS   A CE   1 
ATOM   3417 N  NZ   A LYS   A 1 158 ? 1.889  -4.368  8.272   0.42 26.84 ?  158 LYS   A NZ   1 
ATOM   3418 N  NZ   B LYS   A 1 158 ? 1.585  -4.139  7.979   0.28 25.82 ?  158 LYS   A NZ   1 
ATOM   3419 N  NZ   T LYS   A 1 158 ? 2.143  -4.055  8.324   0.30 26.68 ?  158 LYS   A NZ   1 
ATOM   3420 H  H    A LYS   A 1 158 ? 5.620  0.773   4.676   0.42 22.35 ?  158 LYS   A H    1 
ATOM   3421 H  H    B LYS   A 1 158 ? 5.010  0.636   4.073   0.28 24.72 ?  158 LYS   A H    1 
ATOM   3422 H  H    T LYS   A 1 158 ? 5.701  0.882   4.446   0.30 21.24 ?  158 LYS   A H    1 
ATOM   3423 H  HA   A LYS   A 1 158 ? 5.223  -1.634  5.587   0.42 23.53 ?  158 LYS   A HA   1 
ATOM   3424 H  HA   B LYS   A 1 158 ? 4.535  -1.659  5.253   0.28 24.69 ?  158 LYS   A HA   1 
ATOM   3425 H  HA   T LYS   A 1 158 ? 5.288  -1.461  5.512   0.30 23.03 ?  158 LYS   A HA   1 
ATOM   3426 H  HB2  A LYS   A 1 158 ? 4.239  0.029   6.775   0.42 26.00 ?  158 LYS   A HB2  1 
ATOM   3427 H  HB2  B LYS   A 1 158 ? 3.328  0.649   5.251   0.28 26.38 ?  158 LYS   A HB2  1 
ATOM   3428 H  HB2  T LYS   A 1 158 ? 4.355  0.283   6.608   0.30 25.52 ?  158 LYS   A HB2  1 
ATOM   3429 H  HB3  A LYS   A 1 158 ? 3.466  0.559   5.500   0.42 26.00 ?  158 LYS   A HB3  1 
ATOM   3430 H  HB3  B LYS   A 1 158 ? 2.292  -0.277  4.491   0.28 26.38 ?  158 LYS   A HB3  1 
ATOM   3431 H  HB3  T LYS   A 1 158 ? 3.556  0.747   5.318   0.30 25.52 ?  158 LYS   A HB3  1 
ATOM   3432 H  HG2  A LYS   A 1 158 ? 1.992  -0.510  6.966   0.42 28.52 ?  158 LYS   A HG2  1 
ATOM   3433 H  HG2  B LYS   A 1 158 ? 3.066  -0.451  7.175   0.28 28.06 ?  158 LYS   A HG2  1 
ATOM   3434 H  HG2  T LYS   A 1 158 ? 2.102  -0.224  6.852   0.30 27.83 ?  158 LYS   A HG2  1 
ATOM   3435 H  HG3  A LYS   A 1 158 ? 2.018  -1.276  5.580   0.42 28.52 ?  158 LYS   A HG3  1 
ATOM   3436 H  HG3  B LYS   A 1 158 ? 1.587  -0.377  6.594   0.28 28.06 ?  158 LYS   A HG3  1 
ATOM   3437 H  HG3  T LYS   A 1 158 ? 2.129  -1.109  5.537   0.30 27.83 ?  158 LYS   A HG3  1 
ATOM   3438 H  HD2  A LYS   A 1 158 ? 3.302  -2.971  6.496   0.42 30.35 ?  158 LYS   A HD2  1 
ATOM   3439 H  HD2  B LYS   A 1 158 ? 2.046  -2.598  5.682   0.28 29.45 ?  158 LYS   A HD2  1 
ATOM   3440 H  HD2  T LYS   A 1 158 ? 3.627  -2.592  6.631   0.30 29.76 ?  158 LYS   A HD2  1 
ATOM   3441 H  HD3  A LYS   A 1 158 ? 3.456  -2.158  7.855   0.42 30.35 ?  158 LYS   A HD3  1 
ATOM   3442 H  HD3  B LYS   A 1 158 ? 3.245  -2.635  6.729   0.28 29.45 ?  158 LYS   A HD3  1 
ATOM   3443 H  HD3  T LYS   A 1 158 ? 3.465  -1.723  7.955   0.30 29.76 ?  158 LYS   A HD3  1 
ATOM   3444 H  HE2  A LYS   A 1 158 ? 1.233  -2.461  8.357   0.42 31.58 ?  158 LYS   A HE2  1 
ATOM   3445 H  HE2  B LYS   A 1 158 ? 1.575  -2.170  8.421   0.28 30.42 ?  158 LYS   A HE2  1 
ATOM   3446 H  HE2  T LYS   A 1 158 ? 1.205  -2.290  8.055   0.30 31.23 ?  158 LYS   A HE2  1 
ATOM   3447 H  HE3  A LYS   A 1 158 ? 0.978  -3.149  6.950   0.42 31.58 ?  158 LYS   A HE3  1 
ATOM   3448 H  HE3  B LYS   A 1 158 ? 0.502  -2.571  7.318   0.28 30.42 ?  158 LYS   A HE3  1 
ATOM   3449 H  HE3  T LYS   A 1 158 ? 1.351  -3.133  6.717   0.30 31.23 ?  158 LYS   A HE3  1 
ATOM   3450 H  HZ1  A LYS   A 1 158 ? 1.134  -4.721  8.584   0.42 32.18 ?  158 LYS   A HZ1  1 
ATOM   3451 H  HZ1  B LYS   A 1 158 ? 0.796  -4.505  8.164   0.28 30.95 ?  158 LYS   A HZ1  1 
ATOM   3452 H  HZ1  T LYS   A 1 158 ? 1.402  -4.505  8.527   0.30 31.98 ?  158 LYS   A HZ1  1 
ATOM   3453 H  HZ2  A LYS   A 1 158 ? 2.231  -4.913  7.657   0.42 32.18 ?  158 LYS   A HZ2  1 
ATOM   3454 H  HZ2  B LYS   A 1 158 ? 1.957  -4.576  7.299   0.28 30.95 ?  158 LYS   A HZ2  1 
ATOM   3455 H  HZ2  T LYS   A 1 158 ? 2.683  -4.586  7.855   0.30 31.98 ?  158 LYS   A HZ2  1 
ATOM   3456 H  HZ3  A LYS   A 1 158 ? 2.469  -4.288  8.942   0.42 32.18 ?  158 LYS   A HZ3  1 
ATOM   3457 H  HZ3  B LYS   A 1 158 ? 2.115  -4.214  8.690   0.28 30.95 ?  158 LYS   A HZ3  1 
ATOM   3458 H  HZ3  T LYS   A 1 158 ? 2.553  -3.818  9.077   0.30 31.98 ?  158 LYS   A HZ3  1 
ATOM   3459 N  N    A ASN   A 1 159 ? 3.589  -1.003  2.909   0.42 18.53 ?  159 ASN   A N    1 
ATOM   3460 N  N    B ASN   A 1 159 ? 3.271  -1.376  2.300   0.28 18.60 ?  159 ASN   A N    1 
ATOM   3461 N  N    T ASN   A 1 159 ? 3.658  -0.980  2.806   0.30 19.27 ?  159 ASN   A N    1 
ATOM   3462 C  CA   A ASN   A 1 159 ? 2.886  -1.676  1.827   0.42 18.43 ?  159 ASN   A CA   1 
ATOM   3463 C  CA   B ASN   A 1 159 ? 2.695  -2.161  1.212   0.28 18.34 ?  159 ASN   A CA   1 
ATOM   3464 C  CA   T ASN   A 1 159 ? 2.910  -1.675  1.768   0.30 19.79 ?  159 ASN   A CA   1 
ATOM   3465 C  C    A ASN   A 1 159 ? 3.755  -2.761  1.208   0.42 17.68 ?  159 ASN   A C    1 
ATOM   3466 C  C    B ASN   A 1 159 ? 3.668  -3.233  0.735   0.28 17.83 ?  159 ASN   A C    1 
ATOM   3467 C  C    T ASN   A 1 159 ? 3.739  -2.780  1.123   0.30 20.09 ?  159 ASN   A C    1 
ATOM   3468 O  O    A ASN   A 1 159 ? 3.275  -3.865  0.930   0.42 17.18 ?  159 ASN   A O    1 
ATOM   3469 O  O    B ASN   A 1 159 ? 3.278  -4.388  0.516   0.28 18.01 ?  159 ASN   A O    1 
ATOM   3470 O  O    T ASN   A 1 159 ? 3.212  -3.840  0.798   0.30 20.03 ?  159 ASN   A O    1 
ATOM   3471 C  CB   A ASN   A 1 159 ? 2.402  -0.660  0.792   0.42 19.36 ?  159 ASN   A CB   1 
ATOM   3472 C  CB   B ASN   A 1 159 ? 2.264  -1.240  0.065   0.28 18.90 ?  159 ASN   A CB   1 
ATOM   3473 C  CB   T ASN   A 1 159 ? 2.399  -0.689  0.714   0.30 20.28 ?  159 ASN   A CB   1 
ATOM   3474 C  CG   A ASN   A 1 159 ? 1.174  0.103   1.262   0.42 20.89 ?  159 ASN   A CG   1 
ATOM   3475 C  CG   B ASN   A 1 159 ? 0.814  -0.800  0.181   0.28 19.62 ?  159 ASN   A CG   1 
ATOM   3476 C  CG   T ASN   A 1 159 ? 1.197  0.104   1.195   0.30 21.12 ?  159 ASN   A CG   1 
ATOM   3477 O  OD1  A ASN   A 1 159 ? 0.369  -0.419  2.030   0.42 21.99 ?  159 ASN   A OD1  1 
ATOM   3478 O  OD1  B ASN   A 1 159 ? 0.254  -0.764  1.275   0.28 19.94 ?  159 ASN   A OD1  1 
ATOM   3479 O  OD1  T ASN   A 1 159 ? 0.416  -0.373  2.017   0.30 21.82 ?  159 ASN   A OD1  1 
ATOM   3480 N  ND2  A ASN   A 1 159 ? 1.026  1.338   0.804   0.42 21.40 ?  159 ASN   A ND2  1 
ATOM   3481 N  ND2  B ASN   A 1 159 ? 0.198  -0.467  -0.952  0.28 19.85 ?  159 ASN   A ND2  1 
ATOM   3482 N  ND2  T ASN   A 1 159 ? 1.042  1.318   0.685   0.30 21.39 ?  159 ASN   A ND2  1 
ATOM   3483 H  H    A ASN   A 1 159 ? 3.707  -0.159  2.803   0.42 22.21 ?  159 ASN   A H    1 
ATOM   3484 H  H    B ASN   A 1 159 ? 3.321  -0.530  2.151   0.28 22.29 ?  159 ASN   A H    1 
ATOM   3485 H  H    T ASN   A 1 159 ? 3.806  -0.150  2.645   0.30 23.10 ?  159 ASN   A H    1 
ATOM   3486 H  HA   A ASN   A 1 159 ? 2.105  -2.116  2.194   0.42 22.09 ?  159 ASN   A HA   1 
ATOM   3487 H  HA   B ASN   A 1 159 ? 1.896  -2.604  1.533   0.28 21.98 ?  159 ASN   A HA   1 
ATOM   3488 H  HA   T ASN   A 1 159 ? 2.139  -2.100  2.171   0.30 23.72 ?  159 ASN   A HA   1 
ATOM   3489 H  HB2  A ASN   A 1 159 ? 3.103  -0.015  0.624   0.42 23.21 ?  159 ASN   A HB2  1 
ATOM   3490 H  HB2  B ASN   A 1 159 ? 2.815  -0.435  0.070   0.28 22.65 ?  159 ASN   A HB2  1 
ATOM   3491 H  HB2  T ASN   A 1 159 ? 3.103  -0.062  0.497   0.30 24.31 ?  159 ASN   A HB2  1 
ATOM   3492 H  HB3  A ASN   A 1 159 ? 2.173  -1.127  -0.029  0.42 23.21 ?  159 ASN   A HB3  1 
ATOM   3493 H  HB3  B ASN   A 1 159 ? 2.359  -1.699  -0.778  0.28 22.65 ?  159 ASN   A HB3  1 
ATOM   3494 H  HB3  T ASN   A 1 159 ? 2.138  -1.184  -0.082  0.30 24.31 ?  159 ASN   A HB3  1 
ATOM   3495 H  HD21 A ASN   A 1 159 ? 0.343  1.803   1.042   0.42 25.65 ?  159 ASN   A HD21 1 
ATOM   3496 H  HD21 B ASN   A 1 159 ? -0.625 -0.205  -0.941  0.28 23.79 ?  159 ASN   A HD21 1 
ATOM   3497 H  HD21 T ASN   A 1 159 ? 0.372  1.800   0.926   0.30 25.63 ?  159 ASN   A HD21 1 
ATOM   3498 H  HD22 A ASN   A 1 159 ? 1.612  1.671   0.275   0.42 25.65 ?  159 ASN   A HD22 1 
ATOM   3499 H  HD22 B ASN   A 1 159 ? 0.619  -0.510  -1.701  0.28 23.79 ?  159 ASN   A HD22 1 
ATOM   3500 H  HD22 T ASN   A 1 159 ? 1.610  1.618   0.117   0.30 25.63 ?  159 ASN   A HD22 1 
ATOM   3501 N  N    A LEU   A 1 160 ? 5.048  -2.489  1.025   0.42 16.92 ?  160 LEU   A N    1 
ATOM   3502 N  N    B LEU   A 1 160 ? 4.945  -2.877  0.592   0.28 17.15 ?  160 LEU   A N    1 
ATOM   3503 N  N    T LEU   A 1 160 ? 5.036  -2.546  0.954   0.30 20.25 ?  160 LEU   A N    1 
ATOM   3504 C  CA   A LEU   A 1 160 ? 5.920  -3.518  0.466   0.42 16.12 ?  160 LEU   A CA   1 
ATOM   3505 C  CA   B LEU   A 1 160 ? 5.937  -3.868  0.188   0.28 16.76 ?  160 LEU   A CA   1 
ATOM   3506 C  CA   T LEU   A 1 160 ? 5.893  -3.534  0.306   0.30 20.43 ?  160 LEU   A CA   1 
ATOM   3507 C  C    A LEU   A 1 160 ? 6.089  -4.684  1.431   0.42 15.22 ?  160 LEU   A C    1 
ATOM   3508 C  C    B LEU   A 1 160 ? 6.154  -4.910  1.282   0.28 16.01 ?  160 LEU   A C    1 
ATOM   3509 O  O    A LEU   A 1 160 ? 6.072  -5.848  1.015   0.42 14.97 ?  160 LEU   A O    1 
ATOM   3510 O  O    B LEU   A 1 160 ? 6.246  -6.109  0.994   0.28 15.67 ?  160 LEU   A O    1 
ATOM   3511 C  CB   A LEU   A 1 160 ? 7.273  -2.927  0.077   0.42 15.77 ?  160 LEU   A CB   1 
ATOM   3512 C  CB   B LEU   A 1 160 ? 7.252  -3.178  -0.183  0.28 17.15 ?  160 LEU   A CB   1 
ATOM   3513 C  CB   T LEU   A 1 160 ? 7.346  -3.064  0.295   0.30 20.53 ?  160 LEU   A CB   1 
ATOM   3514 C  CG   A LEU   A 1 160 ? 8.279  -3.973  -0.407  0.42 15.85 ?  160 LEU   A CG   1 
ATOM   3515 C  CG   B LEU   A 1 160 ? 7.278  -2.375  -1.490  0.28 18.04 ?  160 LEU   A CG   1 
ATOM   3516 C  CG   T LEU   A 1 160 ? 8.216  -3.574  -0.856  0.30 20.67 ?  160 LEU   A CG   1 
ATOM   3517 C  CD1  A LEU   A 1 160 ? 7.757  -4.712  -1.625  0.42 16.43 ?  160 LEU   A CD1  1 
ATOM   3518 C  CD1  B LEU   A 1 160 ? 8.614  -1.662  -1.686  0.28 18.32 ?  160 LEU   A CD1  1 
ATOM   3519 C  CD1  T LEU   A 1 160 ? 9.681  -3.468  -0.482  0.30 20.33 ?  160 LEU   A CD1  1 
ATOM   3520 C  CD2  A LEU   A 1 160 ? 9.589  -3.292  -0.728  0.42 16.07 ?  160 LEU   A CD2  1 
ATOM   3521 C  CD2  B LEU   A 1 160 ? 6.975  -3.278  -2.677  0.28 18.32 ?  160 LEU   A CD2  1 
ATOM   3522 C  CD2  T LEU   A 1 160 ? 7.857  -4.996  -1.242  0.30 20.60 ?  160 LEU   A CD2  1 
ATOM   3523 H  H    A LEU   A 1 160 ? 5.436  -1.742  1.219   0.42 20.27 ?  160 LEU   A H    1 
ATOM   3524 H  H    B LEU   A 1 160 ? 5.253  -2.082  0.727   0.28 20.56 ?  160 LEU   A H    1 
ATOM   3525 H  H    T LEU   A 1 160 ? 5.446  -1.830  1.208   0.30 24.27 ?  160 LEU   A H    1 
ATOM   3526 H  HA   A LEU   A 1 160 ? 5.513  -3.858  -0.339  0.42 19.31 ?  160 LEU   A HA   1 
ATOM   3527 H  HA   B LEU   A 1 160 ? 5.606  -4.324  -0.600  0.28 20.08 ?  160 LEU   A HA   1 
ATOM   3528 H  HB2  A LEU   A 1 160 ? 7.150  -2.276  -0.639  0.42 18.89 ?  160 LEU   A HB2  1 
ATOM   3529 H  HB2  B LEU   A 1 160 ? 7.482  -2.564  0.532   0.28 20.55 ?  160 LEU   A HB2  1 
ATOM   3530 H  HB2  T LEU   A 1 160 ? 7.338  -2.103  0.213   0.30 24.60 ?  160 LEU   A HB2  1 
ATOM   3531 H  HB3  A LEU   A 1 160 ? 7.662  -2.491  0.850   0.42 18.89 ?  160 LEU   A HB3  1 
ATOM   3532 H  HB3  B LEU   A 1 160 ? 7.935  -3.861  -0.252  0.28 20.55 ?  160 LEU   A HB3  1 
ATOM   3533 H  HB3  T LEU   A 1 160 ? 7.769  -3.321  1.135   0.30 24.60 ?  160 LEU   A HB3  1 
ATOM   3534 H  HG   A LEU   A 1 160 ? 8.447  -4.616  0.296   0.42 18.99 ?  160 LEU   A HG   1 
ATOM   3535 H  HG   B LEU   A 1 160 ? 6.591  -1.695  -1.452  0.28 21.62 ?  160 LEU   A HG   1 
ATOM   3536 H  HG   T LEU   A 1 160 ? 8.071  -3.007  -1.631  0.30 24.78 ?  160 LEU   A HG   1 
ATOM   3537 H  HD11 A LEU   A 1 160 ? 8.464  -5.271  -1.980  0.42 19.69 ?  160 LEU   A HD11 1 
ATOM   3538 H  HD11 B LEU   A 1 160 ? 8.588  -1.166  -2.521  0.28 21.95 ?  160 LEU   A HD11 1 
ATOM   3539 H  HD11 T LEU   A 1 160 ? 10.220 -3.752  -1.236  0.30 24.37 ?  160 LEU   A HD11 1 
ATOM   3540 H  HD12 A LEU   A 1 160 ? 7.002  -5.260  -1.362  0.42 19.69 ?  160 LEU   A HD12 1 
ATOM   3541 H  HD12 B LEU   A 1 160 ? 8.759  -1.053  -0.945  0.28 21.95 ?  160 LEU   A HD12 1 
ATOM   3542 H  HD12 T LEU   A 1 160 ? 9.883  -2.547  -0.258  0.30 24.37 ?  160 LEU   A HD12 1 
ATOM   3543 H  HD13 A LEU   A 1 160 ? 7.481  -4.064  -2.293  0.42 19.69 ?  160 LEU   A HD13 1 
ATOM   3544 H  HD13 B LEU   A 1 160 ? 9.325  -2.321  -1.716  0.28 21.95 ?  160 LEU   A HD13 1 
ATOM   3545 H  HD13 T LEU   A 1 160 ? 9.851  -4.040  0.282   0.30 24.37 ?  160 LEU   A HD13 1 
ATOM   3546 H  HD21 A LEU   A 1 160 ? 10.227 -3.958  -1.032  0.42 19.25 ?  160 LEU   A HD21 1 
ATOM   3547 H  HD21 B LEU   A 1 160 ? 7.169  -2.798  -3.497  0.28 21.95 ?  160 LEU   A HD21 1 
ATOM   3548 H  HD21 T LEU   A 1 160 ? 8.550  -5.349  -1.821  0.30 24.69 ?  160 LEU   A HD21 1 
ATOM   3549 H  HD22 A LEU   A 1 160 ? 9.444  -2.634  -1.427  0.42 19.25 ?  160 LEU   A HD22 1 
ATOM   3550 H  HD22 B LEU   A 1 160 ? 7.531  -4.072  -2.619  0.28 21.95 ?  160 LEU   A HD22 1 
ATOM   3551 H  HD22 T LEU   A 1 160 ? 7.791  -5.531  -0.437  0.30 24.69 ?  160 LEU   A HD22 1 
ATOM   3552 H  HD23 A LEU   A 1 160 ? 9.926  -2.856  0.071   0.42 19.25 ?  160 LEU   A HD23 1 
ATOM   3553 H  HD23 B LEU   A 1 160 ? 6.039  -3.528  -2.653  0.28 21.95 ?  160 LEU   A HD23 1 
ATOM   3554 H  HD23 T LEU   A 1 160 ? 7.006  -4.990  -1.708  0.30 24.69 ?  160 LEU   A HD23 1 
ATOM   3555 N  N    A TYR   A 1 161 ? 6.259  -4.394  2.721   0.72 15.90 ?  161 TYR   A N    1 
ATOM   3556 N  N    B TYR   A 1 161 ? 6.238  -4.475  2.543   0.28 15.97 ?  161 TYR   A N    1 
ATOM   3557 C  CA   A TYR   A 1 161 ? 6.370  -5.460  3.711   0.72 16.32 ?  161 TYR   A CA   1 
ATOM   3558 C  CA   B TYR   A 1 161 ? 6.407  -5.422  3.643   0.28 16.14 ?  161 TYR   A CA   1 
ATOM   3559 C  C    A TYR   A 1 161 ? 5.200  -6.433  3.614   0.72 17.09 ?  161 TYR   A C    1 
ATOM   3560 C  C    B TYR   A 1 161 ? 5.262  -6.427  3.688   0.28 16.85 ?  161 TYR   A C    1 
ATOM   3561 O  O    A TYR   A 1 161 ? 5.388  -7.654  3.583   0.72 16.39 ?  161 TYR   A O    1 
ATOM   3562 O  O    B TYR   A 1 161 ? 5.488  -7.639  3.780   0.28 16.79 ?  161 TYR   A O    1 
ATOM   3563 C  CB   A TYR   A 1 161 ? 6.456  -4.862  5.114   0.72 16.08 ?  161 TYR   A CB   1 
ATOM   3564 C  CB   B TYR   A 1 161 ? 6.528  -4.684  4.981   0.28 15.75 ?  161 TYR   A CB   1 
ATOM   3565 C  CG   A TYR   A 1 161 ? 6.359  -5.904  6.190   0.72 15.32 ?  161 TYR   A CG   1 
ATOM   3566 C  CG   B TYR   A 1 161 ? 6.413  -5.607  6.180   0.28 15.23 ?  161 TYR   A CG   1 
ATOM   3567 C  CD1  A TYR   A 1 161 ? 7.477  -6.623  6.582   0.72 15.23 ?  161 TYR   A CD1  1 
ATOM   3568 C  CD1  B TYR   A 1 161 ? 7.511  -6.324  6.641   0.28 15.38 ?  161 TYR   A CD1  1 
ATOM   3569 C  CD2  A TYR   A 1 161 ? 5.145  -6.183  6.807   0.72 15.22 ?  161 TYR   A CD2  1 
ATOM   3570 C  CD2  B TYR   A 1 161 ? 5.202  -5.769  6.845   0.28 15.34 ?  161 TYR   A CD2  1 
ATOM   3571 C  CE1  A TYR   A 1 161 ? 7.393  -7.584  7.553   0.72 14.78 ?  161 TYR   A CE1  1 
ATOM   3572 C  CE1  B TYR   A 1 161 ? 7.407  -7.174  7.730   0.28 15.63 ?  161 TYR   A CE1  1 
ATOM   3573 C  CE2  A TYR   A 1 161 ? 5.051  -7.144  7.784   0.72 14.65 ?  161 TYR   A CE2  1 
ATOM   3574 C  CE2  B TYR   A 1 161 ? 5.089  -6.618  7.933   0.28 15.69 ?  161 TYR   A CE2  1 
ATOM   3575 C  CZ   A TYR   A 1 161 ? 6.180  -7.844  8.151   0.72 14.52 ?  161 TYR   A CZ   1 
ATOM   3576 C  CZ   B TYR   A 1 161 ? 6.194  -7.317  8.372   0.28 16.13 ?  161 TYR   A CZ   1 
ATOM   3577 O  OH   A TYR   A 1 161 ? 6.124  -8.809  9.124   0.72 14.91 ?  161 TYR   A OH   1 
ATOM   3578 O  OH   B TYR   A 1 161 ? 6.086  -8.160  9.454   0.28 17.32 ?  161 TYR   A OH   1 
ATOM   3579 H  H    A TYR   A 1 161 ? 6.305  -3.597  3.047   0.72 19.06 ?  161 TYR   A H    1 
ATOM   3580 H  H    B TYR   A 1 161 ? 6.204  -3.649  2.779   0.28 19.14 ?  161 TYR   A H    1 
ATOM   3581 H  HA   A TYR   A 1 161 ? 7.187  -5.955  3.549   0.72 19.55 ?  161 TYR   A HA   1 
ATOM   3582 H  HA   B TYR   A 1 161 ? 7.224  -5.917  3.504   0.28 19.34 ?  161 TYR   A HA   1 
ATOM   3583 H  HB2  A TYR   A 1 161 ? 7.309  -4.407  5.215   0.72 19.27 ?  161 TYR   A HB2  1 
ATOM   3584 H  HB2  B TYR   A 1 161 ? 7.396  -4.249  5.020   0.28 18.87 ?  161 TYR   A HB2  1 
ATOM   3585 H  HB3  A TYR   A 1 161 ? 5.729  -4.233  5.239   0.72 19.27 ?  161 TYR   A HB3  1 
ATOM   3586 H  HB3  B TYR   A 1 161 ? 5.824  -4.021  5.043   0.28 18.87 ?  161 TYR   A HB3  1 
ATOM   3587 H  HD1  A TYR   A 1 161 ? 8.297  -6.453  6.178   0.72 18.25 ?  161 TYR   A HD1  1 
ATOM   3588 H  HD1  B TYR   A 1 161 ? 8.331  -6.231  6.212   0.28 18.42 ?  161 TYR   A HD1  1 
ATOM   3589 H  HD2  A TYR   A 1 161 ? 4.381  -5.716  6.558   0.72 18.24 ?  161 TYR   A HD2  1 
ATOM   3590 H  HD2  B TYR   A 1 161 ? 4.454  -5.299  6.554   0.28 18.37 ?  161 TYR   A HD2  1 
ATOM   3591 H  HE1  A TYR   A 1 161 ? 8.152  -8.062  7.807   0.72 17.71 ?  161 TYR   A HE1  1 
ATOM   3592 H  HE1  B TYR   A 1 161 ? 8.152  -7.646  8.030   0.28 18.73 ?  161 TYR   A HE1  1 
ATOM   3593 H  HE2  A TYR   A 1 161 ? 4.230  -7.328  8.191   0.72 17.55 ?  161 TYR   A HE2  1 
ATOM   3594 H  HE2  B TYR   A 1 161 ? 4.271  -6.712  8.369   0.28 18.79 ?  161 TYR   A HE2  1 
ATOM   3595 H  HH   A TYR   A 1 161 ? 6.878  -9.158  9.241   0.72 17.86 ?  161 TYR   A HH   1 
ATOM   3596 H  HH   B TYR   A 1 161 ? 6.824  -8.520  9.619   0.28 20.75 ?  161 TYR   A HH   1 
ATOM   3597 N  N    A ASP   A 1 162 ? 3.974  -5.907  3.584   0.72 18.28 ?  162 ASP   A N    1 
ATOM   3598 N  N    B ASP   A 1 162 ? 4.020  -5.943  3.632   0.28 17.66 ?  162 ASP   A N    1 
ATOM   3599 C  CA   A ASP   A 1 162 ? 2.805  -6.778  3.487   0.72 18.86 ?  162 ASP   A CA   1 
ATOM   3600 C  CA   B ASP   A 1 162 ? 2.881  -6.851  3.737   0.28 18.37 ?  162 ASP   A CA   1 
ATOM   3601 C  C    A ASP   A 1 162 ? 2.858  -7.615  2.217   0.72 18.36 ?  162 ASP   A C    1 
ATOM   3602 C  C    B ASP   A 1 162 ? 2.856  -7.857  2.594   0.28 18.41 ?  162 ASP   A C    1 
ATOM   3603 O  O    A ASP   A 1 162 ? 2.528  -8.809  2.235   0.72 18.21 ?  162 ASP   A O    1 
ATOM   3604 O  O    B ASP   A 1 162 ? 2.413  -8.996  2.780   0.28 18.18 ?  162 ASP   A O    1 
ATOM   3605 C  CB   A ASP   A 1 162 ? 1.513  -5.956  3.522   0.72 20.59 ?  162 ASP   A CB   1 
ATOM   3606 C  CB   B ASP   A 1 162 ? 1.571  -6.063  3.812   0.28 19.16 ?  162 ASP   A CB   1 
ATOM   3607 C  CG   A ASP   A 1 162 ? 1.237  -5.337  4.876   0.72 22.38 ?  162 ASP   A CG   1 
ATOM   3608 C  CG   B ASP   A 1 162 ? 1.152  -5.754  5.234   0.28 20.06 ?  162 ASP   A CG   1 
ATOM   3609 O  OD1  A ASP   A 1 162 ? 1.844  -5.765  5.875   0.72 23.43 ?  162 ASP   A OD1  1 
ATOM   3610 O  OD1  B ASP   A 1 162 ? 1.891  -6.113  6.175   0.28 20.63 ?  162 ASP   A OD1  1 
ATOM   3611 O  OD2  A ASP   A 1 162 ? 0.379  -4.429  4.942   0.72 23.55 -1 162 ASP   A OD2  1 
ATOM   3612 O  OD2  B ASP   A 1 162 ? 0.073  -5.148  5.408   0.28 20.49 -1 162 ASP   A OD2  1 
ATOM   3613 H  H    A ASP   A 1 162 ? 3.797  -5.066  3.616   0.72 21.91 ?  162 ASP   A H    1 
ATOM   3614 H  H    B ASP   A 1 162 ? 3.814  -5.111  3.532   0.28 21.17 ?  162 ASP   A H    1 
ATOM   3615 H  HA   A ASP   A 1 162 ? 2.800  -7.387  4.238   0.72 22.60 ?  162 ASP   A HA   1 
ATOM   3616 H  HA   B ASP   A 1 162 ? 2.968  -7.356  4.553   0.28 22.02 ?  162 ASP   A HA   1 
ATOM   3617 H  HB2  A ASP   A 1 162 ? 1.581  -5.232  2.888   0.72 24.68 ?  162 ASP   A HB2  1 
ATOM   3618 H  HB2  B ASP   A 1 162 ? 1.676  -5.213  3.359   0.28 22.96 ?  162 ASP   A HB2  1 
ATOM   3619 H  HB3  A ASP   A 1 162 ? 0.769  -6.534  3.300   0.72 24.68 ?  162 ASP   A HB3  1 
ATOM   3620 H  HB3  B ASP   A 1 162 ? 0.862  -6.578  3.400   0.28 22.96 ?  162 ASP   A HB3  1 
ATOM   3621 N  N    A LYS   A 1 163 ? 3.272  -7.008  1.102   0.72 18.71 ?  163 LYS   A N    1 
ATOM   3622 N  N    B LYS   A 1 163 ? 3.340  -7.467  1.416   0.28 18.65 ?  163 LYS   A N    1 
ATOM   3623 C  CA   A LYS   A 1 163 ? 3.381  -7.770  -0.135  0.72 19.21 ?  163 LYS   A CA   1 
ATOM   3624 C  CA   B LYS   A 1 163 ? 3.352  -8.381  0.282   0.28 18.91 ?  163 LYS   A CA   1 
ATOM   3625 C  C    A LYS   A 1 163 ? 4.448  -8.849  -0.023  0.72 18.52 ?  163 LYS   A C    1 
ATOM   3626 C  C    B LYS   A 1 163 ? 4.530  -9.348  0.333   0.28 17.83 ?  163 LYS   A C    1 
ATOM   3627 O  O    A LYS   A 1 163 ? 4.275  -9.960  -0.538  0.72 18.26 ?  163 LYS   A O    1 
ATOM   3628 O  O    B LYS   A 1 163 ? 4.413  -10.487 -0.136  0.28 17.87 ?  163 LYS   A O    1 
ATOM   3629 C  CB   A LYS   A 1 163 ? 3.675  -6.844  -1.315  0.72 21.55 ?  163 LYS   A CB   1 
ATOM   3630 C  CB   B LYS   A 1 163 ? 3.368  -7.569  -1.008  0.28 20.62 ?  163 LYS   A CB   1 
ATOM   3631 C  CG   A LYS   A 1 163 ? 3.742  -7.583  -2.642  0.72 24.40 ?  163 LYS   A CG   1 
ATOM   3632 C  CG   B LYS   A 1 163 ? 2.219  -7.886  -1.961  0.28 22.35 ?  163 LYS   A CG   1 
ATOM   3633 C  CD   A LYS   A 1 163 ? 4.171  -6.674  -3.776  0.72 27.18 ?  163 LYS   A CD   1 
ATOM   3634 C  CD   B LYS   A 1 163 ? 2.626  -8.907  -2.999  0.28 23.54 ?  163 LYS   A CD   1 
ATOM   3635 C  CE   A LYS   A 1 163 ? 4.110  -7.401  -5.111  0.72 29.02 ?  163 LYS   A CE   1 
ATOM   3636 C  CE   B LYS   A 1 163 ? 3.954  -8.535  -3.644  0.28 24.54 ?  163 LYS   A CE   1 
ATOM   3637 N  NZ   A LYS   A 1 163 ? 4.765  -6.627  -6.201  0.72 30.19 ?  163 LYS   A NZ   1 
ATOM   3638 N  NZ   B LYS   A 1 163 ? 3.980  -7.132  -4.155  0.28 25.29 ?  163 LYS   A NZ   1 
ATOM   3639 H  H    A LYS   A 1 163 ? 3.486  -6.169  1.038   0.72 22.43 ?  163 LYS   A H    1 
ATOM   3640 H  H    B LYS   A 1 163 ? 3.659  -6.686  1.246   0.28 22.35 ?  163 LYS   A H    1 
ATOM   3641 H  HA   A LYS   A 1 163 ? 2.532  -8.203  -0.306  0.72 23.02 ?  163 LYS   A HA   1 
ATOM   3642 H  HA   B LYS   A 1 163 ? 2.540  -8.907  0.292   0.28 22.66 ?  163 LYS   A HA   1 
ATOM   3643 H  HB2  A LYS   A 1 163 ? 2.968  -6.177  -1.384  0.72 25.83 ?  163 LYS   A HB2  1 
ATOM   3644 H  HB2  B LYS   A 1 163 ? 3.264  -6.645  -0.782  0.28 24.71 ?  163 LYS   A HB2  1 
ATOM   3645 H  HB3  A LYS   A 1 163 ? 4.527  -6.405  -1.174  0.72 25.83 ?  163 LYS   A HB3  1 
ATOM   3646 H  HB3  B LYS   A 1 163 ? 4.233  -7.679  -1.428  0.28 24.71 ?  163 LYS   A HB3  1 
ATOM   3647 H  HG2  A LYS   A 1 163 ? 4.387  -8.304  -2.578  0.72 29.25 ?  163 LYS   A HG2  1 
ATOM   3648 H  HG2  B LYS   A 1 163 ? 1.464  -8.240  -1.454  0.28 26.79 ?  163 LYS   A HG2  1 
ATOM   3649 H  HG3  A LYS   A 1 163 ? 2.864  -7.939  -2.852  0.72 29.25 ?  163 LYS   A HG3  1 
ATOM   3650 H  HG3  B LYS   A 1 163 ? 1.949  -7.072  -2.418  0.28 26.79 ?  163 LYS   A HG3  1 
ATOM   3651 H  HD2  A LYS   A 1 163 ? 3.576  -5.910  -3.817  0.72 32.58 ?  163 LYS   A HD2  1 
ATOM   3652 H  HD2  B LYS   A 1 163 ? 2.716  -9.775  -2.576  0.28 28.22 ?  163 LYS   A HD2  1 
ATOM   3653 H  HD3  A LYS   A 1 163 ? 5.084  -6.385  -3.626  0.72 32.58 ?  163 LYS   A HD3  1 
ATOM   3654 H  HD3  B LYS   A 1 163 ? 1.949  -8.941  -3.697  0.28 28.22 ?  163 LYS   A HD3  1 
ATOM   3655 H  HE2  A LYS   A 1 163 ? 4.557  -8.258  -5.029  0.72 34.79 ?  163 LYS   A HE2  1 
ATOM   3656 H  HE2  B LYS   A 1 163 ? 4.694  -8.670  -3.021  0.28 29.42 ?  163 LYS   A HE2  1 
ATOM   3657 H  HE3  A LYS   A 1 163 ? 3.182  -7.537  -5.355  0.72 34.79 ?  163 LYS   A HE3  1 
ATOM   3658 H  HE3  B LYS   A 1 163 ? 4.076  -9.105  -4.393  0.28 29.42 ?  163 LYS   A HE3  1 
ATOM   3659 H  HZ1  A LYS   A 1 163 ? 4.714  -7.077  -6.967  0.72 36.20 ?  163 LYS   A HZ1  1 
ATOM   3660 H  HZ1  B LYS   A 1 163 ? 4.765  -6.967  -4.542  0.28 30.32 ?  163 LYS   A HZ1  1 
ATOM   3661 H  HZ2  A LYS   A 1 163 ? 4.360  -5.841  -6.300  0.72 36.20 ?  163 LYS   A HZ2  1 
ATOM   3662 H  HZ2  B LYS   A 1 163 ? 3.334  -7.021  -4.758  0.28 30.32 ?  163 LYS   A HZ2  1 
ATOM   3663 H  HZ3  A LYS   A 1 163 ? 5.622  -6.488  -6.004  0.72 36.20 ?  163 LYS   A HZ3  1 
ATOM   3664 H  HZ3  B LYS   A 1 163 ? 3.858  -6.549  -3.493  0.28 30.32 ?  163 LYS   A HZ3  1 
ATOM   3665 N  N    A LEU   A 1 164 ? 5.564  -8.541  0.639   0.72 17.02 ?  164 LEU   A N    1 
ATOM   3666 N  N    B LEU   A 1 164 ? 5.663  -8.917  0.894   0.28 16.57 ?  164 LEU   A N    1 
ATOM   3667 C  CA   A LEU   A 1 164 ? 6.630  -9.530  0.773   0.72 16.31 ?  164 LEU   A CA   1 
ATOM   3668 C  CA   B LEU   A 1 164 ? 6.803  -9.813  1.066   0.28 15.36 ?  164 LEU   A CA   1 
ATOM   3669 C  C    A LEU   A 1 164 ? 6.188  -10.705 1.633   0.72 16.24 ?  164 LEU   A C    1 
ATOM   3670 C  C    B LEU   A 1 164 ? 6.429  -11.009 1.932   0.28 15.48 ?  164 LEU   A C    1 
ATOM   3671 O  O    A LEU   A 1 164 ? 6.481  -11.862 1.310   0.72 16.68 ?  164 LEU   A O    1 
ATOM   3672 O  O    B LEU   A 1 164 ? 6.788  -12.151 1.622   0.28 15.26 ?  164 LEU   A O    1 
ATOM   3673 C  CB   A LEU   A 1 164 ? 7.872  -8.875  1.367   0.72 16.11 ?  164 LEU   A CB   1 
ATOM   3674 C  CB   B LEU   A 1 164 ? 7.966  -9.046  1.702   0.28 14.51 ?  164 LEU   A CB   1 
ATOM   3675 C  CG   A LEU   A 1 164 ? 8.640  -7.958  0.417   0.72 16.10 ?  164 LEU   A CG   1 
ATOM   3676 C  CG   B LEU   A 1 164 ? 8.732  -8.038  0.840   0.28 14.32 ?  164 LEU   A CG   1 
ATOM   3677 C  CD1  A LEU   A 1 164 ? 9.608  -7.104  1.210   0.72 15.65 ?  164 LEU   A CD1  1 
ATOM   3678 C  CD1  B LEU   A 1 164 ? 9.505  -7.052  1.713   0.28 14.27 ?  164 LEU   A CD1  1 
ATOM   3679 C  CD2  A LEU   A 1 164 ? 9.382  -8.753  -0.646  0.72 16.49 ?  164 LEU   A CD2  1 
ATOM   3680 C  CD2  B LEU   A 1 164 ? 9.681  -8.755  -0.106  0.28 14.03 ?  164 LEU   A CD2  1 
ATOM   3681 H  H    A LEU   A 1 164 ? 5.729  -7.774  1.014   0.72 20.39 ?  164 LEU   A H    1 
ATOM   3682 H  H    B LEU   A 1 164 ? 5.791  -8.122  1.183   0.28 19.86 ?  164 LEU   A H    1 
ATOM   3683 H  HA   A LEU   A 1 164 ? 6.859  -9.863  -0.106  0.72 19.55 ?  164 LEU   A HA   1 
ATOM   3684 H  HA   B LEU   A 1 164 ? 7.091  -10.144 0.203   0.28 18.40 ?  164 LEU   A HA   1 
ATOM   3685 H  HB2  A LEU   A 1 164 ? 7.608  -8.338  2.131   0.72 19.30 ?  164 LEU   A HB2  1 
ATOM   3686 H  HB2  B LEU   A 1 164 ? 7.619  -8.555  2.462   0.28 17.38 ?  164 LEU   A HB2  1 
ATOM   3687 H  HB3  A LEU   A 1 164 ? 8.483  -9.569  1.652   0.72 19.30 ?  164 LEU   A HB3  1 
ATOM   3688 H  HB3  B LEU   A 1 164 ? 8.616  -9.693  2.014   0.28 17.38 ?  164 LEU   A HB3  1 
ATOM   3689 H  HG   A LEU   A 1 164 ? 8.016  -7.365  -0.030  0.72 19.29 ?  164 LEU   A HG   1 
ATOM   3690 H  HG   B LEU   A 1 164 ? 8.104  -7.529  0.307   0.28 17.16 ?  164 LEU   A HG   1 
ATOM   3691 H  HD11 A LEU   A 1 164 ? 10.084 -6.516  0.605   0.72 18.75 ?  164 LEU   A HD11 1 
ATOM   3692 H  HD11 B LEU   A 1 164 ? 10.079 -6.510  1.149   0.28 17.09 ?  164 LEU   A HD11 1 
ATOM   3693 H  HD12 A LEU   A 1 164 ? 9.110  -6.582  1.859   0.72 18.75 ?  164 LEU   A HD12 1 
ATOM   3694 H  HD12 B LEU   A 1 164 ? 8.874  -6.481  2.182   0.28 17.09 ?  164 LEU   A HD12 1 
ATOM   3695 H  HD13 A LEU   A 1 164 ? 10.237 -7.685  1.669   0.72 18.75 ?  164 LEU   A HD13 1 
ATOM   3696 H  HD13 B LEU   A 1 164 ? 10.042 -7.545  2.353   0.28 17.09 ?  164 LEU   A HD13 1 
ATOM   3697 H  HD21 A LEU   A 1 164 ? 9.914  -8.144  -1.184  0.72 19.75 ?  164 LEU   A HD21 1 
ATOM   3698 H  HD21 B LEU   A 1 164 ? 10.140 -8.097  -0.653  0.28 16.81 ?  164 LEU   A HD21 1 
ATOM   3699 H  HD22 A LEU   A 1 164 ? 9.960  -9.399  -0.211  0.72 19.75 ?  164 LEU   A HD22 1 
ATOM   3700 H  HD22 B LEU   A 1 164 ? 10.326 -9.259  0.414   0.28 16.81 ?  164 LEU   A HD22 1 
ATOM   3701 H  HD23 A LEU   A 1 164 ? 8.737  -9.211  -1.207  0.72 19.75 ?  164 LEU   A HD23 1 
ATOM   3702 H  HD23 B LEU   A 1 164 ? 9.168  -9.353  -0.669  0.28 16.81 ?  164 LEU   A HD23 1 
ATOM   3703 N  N    A VAL   A 1 165 ? 5.508  -10.425 2.744   0.72 15.60 ?  165 VAL   A N    1 
ATOM   3704 N  N    B VAL   A 1 165 ? 5.712  -10.761 3.027   0.28 15.64 ?  165 VAL   A N    1 
ATOM   3705 C  CA   A VAL   A 1 165 ? 5.020  -11.498 3.607   0.72 15.60 ?  165 VAL   A CA   1 
ATOM   3706 C  CA   B VAL   A 1 165 ? 5.285  -11.845 3.905   0.28 15.85 ?  165 VAL   A CA   1 
ATOM   3707 C  C    A VAL   A 1 165 ? 3.997  -12.349 2.868   0.72 15.86 ?  165 VAL   A C    1 
ATOM   3708 C  C    B VAL   A 1 165 ? 4.216  -12.688 3.224   0.28 15.86 ?  165 VAL   A C    1 
ATOM   3709 O  O    A VAL   A 1 165 ? 4.097  -13.582 2.827   0.72 15.85 ?  165 VAL   A O    1 
ATOM   3710 O  O    B VAL   A 1 165 ? 4.281  -13.923 3.223   0.28 15.37 ?  165 VAL   A O    1 
ATOM   3711 C  CB   A VAL   A 1 165 ? 4.443  -10.915 4.909   0.72 16.03 ?  165 VAL   A CB   1 
ATOM   3712 C  CB   B VAL   A 1 165 ? 4.784  -11.270 5.242   0.28 15.98 ?  165 VAL   A CB   1 
ATOM   3713 C  CG1  A VAL   A 1 165 ? 3.693  -11.987 5.694   0.72 15.78 ?  165 VAL   A CG1  1 
ATOM   3714 C  CG1  B VAL   A 1 165 ? 4.189  -12.370 6.112   0.28 16.09 ?  165 VAL   A CG1  1 
ATOM   3715 C  CG2  A VAL   A 1 165 ? 5.547  -10.302 5.752   0.72 16.41 ?  165 VAL   A CG2  1 
ATOM   3716 C  CG2  B VAL   A 1 165 ? 5.914  -10.546 5.961   0.28 16.37 ?  165 VAL   A CG2  1 
ATOM   3717 H  H    A VAL   A 1 165 ? 5.319  -9.631  3.020   0.72 18.68 ?  165 VAL   A H    1 
ATOM   3718 H  H    B VAL   A 1 165 ? 5.465  -9.981  3.283   0.28 18.74 ?  165 VAL   A H    1 
ATOM   3719 H  HA   A VAL   A 1 165 ? 5.762  -12.069 3.846   0.72 18.69 ?  165 VAL   A HA   1 
ATOM   3720 H  HA   B VAL   A 1 165 ? 6.044  -12.420 4.097   0.28 18.99 ?  165 VAL   A HA   1 
ATOM   3721 H  HB   A VAL   A 1 165 ? 3.812  -10.210 4.692   0.72 19.20 ?  165 VAL   A HB   1 
ATOM   3722 H  HB   B VAL   A 1 165 ? 4.086  -10.623 5.064   0.28 19.14 ?  165 VAL   A HB   1 
ATOM   3723 H  HG11 A VAL   A 1 165 ? 3.585  -11.690 6.612   0.72 18.90 ?  165 VAL   A HG11 1 
ATOM   3724 H  HG11 B VAL   A 1 165 ? 4.111  -12.043 7.022   0.28 19.28 ?  165 VAL   A HG11 1 
ATOM   3725 H  HG12 A VAL   A 1 165 ? 2.821  -12.126 5.291   0.72 18.90 ?  165 VAL   A HG12 1 
ATOM   3726 H  HG12 B VAL   A 1 165 ? 3.312  -12.604 5.771   0.28 19.28 ?  165 VAL   A HG12 1 
ATOM   3727 H  HG13 A VAL   A 1 165 ? 4.205  -12.810 5.674   0.72 18.90 ?  165 VAL   A HG13 1 
ATOM   3728 H  HG13 B VAL   A 1 165 ? 4.774  -13.142 6.088   0.28 19.28 ?  165 VAL   A HG13 1 
ATOM   3729 H  HG21 A VAL   A 1 165 ? 5.167  -9.964  6.579   0.72 19.66 ?  165 VAL   A HG21 1 
ATOM   3730 H  HG21 B VAL   A 1 165 ? 5.591  -10.226 6.817   0.28 19.61 ?  165 VAL   A HG21 1 
ATOM   3731 H  HG22 A VAL   A 1 165 ? 6.212  -10.981 5.948   0.72 19.66 ?  165 VAL   A HG22 1 
ATOM   3732 H  HG22 B VAL   A 1 165 ? 6.651  -11.162 6.093   0.28 19.61 ?  165 VAL   A HG22 1 
ATOM   3733 H  HG23 A VAL   A 1 165 ? 5.957  -9.574  5.256   0.72 19.66 ?  165 VAL   A HG23 1 
ATOM   3734 H  HG23 B VAL   A 1 165 ? 6.203  -9.796  5.416   0.28 19.61 ?  165 VAL   A HG23 1 
ATOM   3735 N  N    A SER   A 1 166 ? 2.992  -11.703 2.276   0.72 16.27 ?  166 SER   A N    1 
ATOM   3736 N  N    B SER   A 1 166 ? 3.217  -12.032 2.629   0.28 16.19 ?  166 SER   A N    1 
ATOM   3737 C  CA   A SER   A 1 166 ? 1.887  -12.443 1.681   0.72 17.12 ?  166 SER   A CA   1 
ATOM   3738 C  CA   B SER   A 1 166 ? 2.056  -12.758 2.125   0.28 16.24 ?  166 SER   A CA   1 
ATOM   3739 C  C    A SER   A 1 166 ? 2.323  -13.265 0.482   0.72 17.67 ?  166 SER   A C    1 
ATOM   3740 C  C    B SER   A 1 166 ? 2.433  -13.746 1.025   0.28 16.07 ?  166 SER   A C    1 
ATOM   3741 O  O    A SER   A 1 166 ? 1.649  -14.245 0.142   0.72 19.11 ?  166 SER   A O    1 
ATOM   3742 O  O    B SER   A 1 166 ? 1.815  -14.809 0.908   0.28 15.97 ?  166 SER   A O    1 
ATOM   3743 C  CB   A SER   A 1 166 ? 0.767  -11.486 1.268   0.72 18.25 ?  166 SER   A CB   1 
ATOM   3744 C  CB   B SER   A 1 166 ? 0.970  -11.773 1.665   0.28 16.98 ?  166 SER   A CB   1 
ATOM   3745 O  OG   A SER   A 1 166 ? 0.152  -10.899 2.402   0.72 20.10 ?  166 SER   A OG   1 
ATOM   3746 O  OG   B SER   A 1 166 ? 1.333  -11.079 0.483   0.28 17.72 ?  166 SER   A OG   1 
ATOM   3747 H  H    A SER   A 1 166 ? 2.923  -10.850 2.216   0.72 19.50 ?  166 SER   A H    1 
ATOM   3748 H  H    B SER   A 1 166 ? 3.193  -11.184 2.513   0.28 19.40 ?  166 SER   A H    1 
ATOM   3749 H  HA   A SER   A 1 166 ? 1.521  -13.054 2.341   0.72 20.52 ?  166 SER   A HA   1 
ATOM   3750 H  HA   B SER   A 1 166 ? 1.679  -13.267 2.857   0.28 19.46 ?  166 SER   A HA   1 
ATOM   3751 H  HB2  A SER   A 1 166 ? 1.136  -10.791 0.703   0.72 21.87 ?  166 SER   A HB2  1 
ATOM   3752 H  HB2  B SER   A 1 166 ? 0.158  -12.263 1.481   0.28 20.34 ?  166 SER   A HB2  1 
ATOM   3753 H  HB3  A SER   A 1 166 ? 0.087  -11.981 0.786   0.72 21.87 ?  166 SER   A HB3  1 
ATOM   3754 H  HB3  B SER   A 1 166 ? 0.809  -11.130 2.380   0.28 20.34 ?  166 SER   A HB3  1 
ATOM   3755 H  HG   A SER   A 1 166 ? -0.444 -10.358 2.161   0.72 24.09 ?  166 SER   A HG   1 
ATOM   3756 H  HG   B SER   A 1 166 ? 0.736  -10.529 0.274   0.28 21.23 ?  166 SER   A HG   1 
ATOM   3757 N  N    A SER   A 1 167 ? 3.427  -12.897 -0.165  0.72 16.57 ?  167 SER   A N    1 
ATOM   3758 N  N    B SER   A 1 167 ? 3.467  -13.445 0.241   0.28 16.55 ?  167 SER   A N    1 
ATOM   3759 C  CA   A SER   A 1 167 ? 3.902  -13.612 -1.338  0.72 17.54 ?  167 SER   A CA   1 
ATOM   3760 C  CA   B SER   A 1 167 ? 3.824  -14.261 -0.912  0.28 16.68 ?  167 SER   A CA   1 
ATOM   3761 C  C    A SER   A 1 167 ? 5.046  -14.569 -1.035  0.72 17.73 ?  167 SER   A C    1 
ATOM   3762 C  C    B SER   A 1 167 ? 5.008  -15.188 -0.644  0.28 16.67 ?  167 SER   A C    1 
ATOM   3763 O  O    A SER   A 1 167 ? 5.554  -15.210 -1.960  0.72 19.20 ?  167 SER   A O    1 
ATOM   3764 O  O    B SER   A 1 167 ? 5.616  -15.693 -1.595  0.28 17.11 ?  167 SER   A O    1 
ATOM   3765 C  CB   A SER   A 1 167 ? 4.338  -12.623 -2.429  0.72 18.08 ?  167 SER   A CB   1 
ATOM   3766 C  CB   B SER   A 1 167 ? 4.112  -13.370 -2.122  0.28 17.23 ?  167 SER   A CB   1 
ATOM   3767 O  OG   A SER   A 1 167 ? 5.389  -11.785 -1.971  0.72 18.08 ?  167 SER   A OG   1 
ATOM   3768 O  OG   B SER   A 1 167 ? 5.336  -12.668 -1.973  0.28 17.93 ?  167 SER   A OG   1 
ATOM   3769 H  H    A SER   A 1 167 ? 3.918  -12.221 0.063   0.72 19.85 ?  167 SER   A H    1 
ATOM   3770 H  H    B SER   A 1 167 ? 3.984  -12.773 0.370   0.28 19.83 ?  167 SER   A H    1 
ATOM   3771 H  HA   A SER   A 1 167 ? 3.168  -14.125 -1.698  0.72 21.02 ?  167 SER   A HA   1 
ATOM   3772 H  HA   B SER   A 1 167 ? 3.067  -14.823 -1.134  0.28 19.99 ?  167 SER   A HA   1 
ATOM   3773 H  HB2  A SER   A 1 167 ? 4.651  -13.125 -3.198  0.72 21.67 ?  167 SER   A HB2  1 
ATOM   3774 H  HB2  B SER   A 1 167 ? 4.160  -13.928 -2.912  0.28 20.65 ?  167 SER   A HB2  1 
ATOM   3775 H  HB3  A SER   A 1 167 ? 3.576  -12.074 -2.685  0.72 21.67 ?  167 SER   A HB3  1 
ATOM   3776 H  HB3  B SER   A 1 167 ? 3.391  -12.728 -2.210  0.28 20.65 ?  167 SER   A HB3  1 
ATOM   3777 H  HG   A SER   A 1 167 ? 5.118  -11.330 -1.313  0.72 21.66 ?  167 SER   A HG   1 
ATOM   3778 H  HG   B SER   A 1 167 ? 5.308  -12.186 -1.285  0.28 21.48 ?  167 SER   A HG   1 
ATOM   3779 N  N    A PHE   A 1 168 ? 5.471  -14.680 0.224   0.72 17.19 ?  168 PHE   A N    1 
ATOM   3780 N  N    B PHE   A 1 168 ? 5.328  -15.453 0.623   0.28 16.35 ?  168 PHE   A N    1 
ATOM   3781 C  CA   A PHE   A 1 168 ? 6.648  -15.485 0.527   0.72 17.73 ?  168 PHE   A CA   1 
ATOM   3782 C  CA   B PHE   A 1 168 ? 6.593  -16.113 0.933   0.28 16.16 ?  168 PHE   A CA   1 
ATOM   3783 C  C    A PHE   A 1 168 ? 6.330  -16.966 0.405   0.72 19.36 ?  168 PHE   A C    1 
ATOM   3784 C  C    B PHE   A 1 168 ? 6.518  -17.629 0.781   0.28 16.27 ?  168 PHE   A C    1 
ATOM   3785 O  O    A PHE   A 1 168 ? 5.339  -17.451 0.962   0.72 21.09 ?  168 PHE   A O    1 
ATOM   3786 O  O    B PHE   A 1 168 ? 7.338  -18.229 0.075   0.28 15.56 ?  168 PHE   A O    1 
ATOM   3787 C  CB   A PHE   A 1 168 ? 7.163  -15.213 1.935   0.72 16.89 ?  168 PHE   A CB   1 
ATOM   3788 C  CB   B PHE   A 1 168 ? 7.067  -15.738 2.338   0.28 16.28 ?  168 PHE   A CB   1 
ATOM   3789 C  CG   A PHE   A 1 168 ? 8.422  -15.968 2.246   0.72 16.14 ?  168 PHE   A CG   1 
ATOM   3790 C  CG   B PHE   A 1 168 ? 8.388  -16.347 2.700   0.28 16.55 ?  168 PHE   A CG   1 
ATOM   3791 C  CD1  A PHE   A 1 168 ? 9.618  -15.580 1.673   0.72 16.32 ?  168 PHE   A CD1  1 
ATOM   3792 C  CD1  B PHE   A 1 168 ? 9.547  -15.929 2.070   0.28 16.98 ?  168 PHE   A CD1  1 
ATOM   3793 C  CD2  A PHE   A 1 168 ? 8.414  -17.086 3.070   0.72 15.86 ?  168 PHE   A CD2  1 
ATOM   3794 C  CD2  B PHE   A 1 168 ? 8.473  -17.346 3.654   0.28 16.46 ?  168 PHE   A CD2  1 
ATOM   3795 C  CE1  A PHE   A 1 168 ? 10.783 -16.271 1.931   0.72 15.84 ?  168 PHE   A CE1  1 
ATOM   3796 C  CE1  B PHE   A 1 168 ? 10.766 -16.489 2.389   0.28 17.08 ?  168 PHE   A CE1  1 
ATOM   3797 C  CE2  A PHE   A 1 168 ? 9.586  -17.779 3.332   0.72 16.11 ?  168 PHE   A CE2  1 
ATOM   3798 C  CE2  B PHE   A 1 168 ? 9.693  -17.907 3.980   0.28 16.73 ?  168 PHE   A CE2  1 
ATOM   3799 C  CZ   A PHE   A 1 168 ? 10.768 -17.369 2.760   0.72 15.92 ?  168 PHE   A CZ   1 
ATOM   3800 C  CZ   B PHE   A 1 168 ? 10.840 -17.478 3.345   0.28 17.03 ?  168 PHE   A CZ   1 
ATOM   3801 H  H    A PHE   A 1 168 ? 5.109  -14.292 0.904   0.72 20.59 ?  168 PHE   A H    1 
ATOM   3802 H  H    B PHE   A 1 168 ? 4.841  -15.272 1.310   0.28 19.59 ?  168 PHE   A H    1 
ATOM   3803 H  HA   A PHE   A 1 168 ? 7.352  -15.264 -0.105  0.72 21.24 ?  168 PHE   A HA   1 
ATOM   3804 H  HA   B PHE   A 1 168 ? 7.264  -15.800 0.311   0.28 19.36 ?  168 PHE   A HA   1 
ATOM   3805 H  HB2  A PHE   A 1 168 ? 7.346  -14.266 2.028   0.72 20.24 ?  168 PHE   A HB2  1 
ATOM   3806 H  HB2  B PHE   A 1 168 ? 7.164  -14.774 2.389   0.28 19.50 ?  168 PHE   A HB2  1 
ATOM   3807 H  HB3  A PHE   A 1 168 ? 6.483  -15.483 2.574   0.72 20.24 ?  168 PHE   A HB3  1 
ATOM   3808 H  HB3  B PHE   A 1 168 ? 6.415  -16.041 2.987   0.28 19.50 ?  168 PHE   A HB3  1 
ATOM   3809 H  HD1  A PHE   A 1 168 ? 9.640  -14.837 1.113   0.72 19.55 ?  168 PHE   A HD1  1 
ATOM   3810 H  HD1  B PHE   A 1 168 ? 9.504  -15.262 1.424   0.28 20.34 ?  168 PHE   A HD1  1 
ATOM   3811 H  HD2  A PHE   A 1 168 ? 7.617  -17.367 3.458   0.72 19.00 ?  168 PHE   A HD2  1 
ATOM   3812 H  HD2  B PHE   A 1 168 ? 7.703  -17.637 4.086   0.28 19.72 ?  168 PHE   A HD2  1 
ATOM   3813 H  HE1  A PHE   A 1 168 ? 11.586 -15.994 1.546   0.72 18.98 ?  168 PHE   A HE1  1 
ATOM   3814 H  HE1  B PHE   A 1 168 ? 11.539 -16.197 1.960   0.28 20.46 ?  168 PHE   A HE1  1 
ATOM   3815 H  HE2  A PHE   A 1 168 ? 9.572  -18.525 3.889   0.72 19.30 ?  168 PHE   A HE2  1 
ATOM   3816 H  HE2  B PHE   A 1 168 ? 9.741  -18.576 4.625   0.28 20.05 ?  168 PHE   A HE2  1 
ATOM   3817 H  HZ   A PHE   A 1 168 ? 11.558 -17.835 2.933   0.72 19.08 ?  168 PHE   A HZ   1 
ATOM   3818 H  HZ   B PHE   A 1 168 ? 11.663 -17.855 3.561   0.28 20.41 ?  168 PHE   A HZ   1 
ATOM   3819 N  N    A LEU   A 1 169 ? 7.198  -17.693 -0.291  0.72 21.17 ?  169 LEU   A N    1 
ATOM   3820 N  N    B LEU   A 1 169 ? 5.576  -18.271 1.467   0.28 17.69 ?  169 LEU   A N    1 
ATOM   3821 C  CA   A LEU   A 1 169 ? 6.999  -19.124 -0.453  0.72 23.62 ?  169 LEU   A CA   1 
ATOM   3822 C  CA   B LEU   A 1 169 ? 5.531  -19.731 1.485   0.28 19.45 ?  169 LEU   A CA   1 
ATOM   3823 C  C    A LEU   A 1 169 ? 7.831  -19.890 0.570   0.72 23.55 ?  169 LEU   A C    1 
ATOM   3824 C  C    B LEU   A 1 169 ? 4.879  -20.290 0.223   0.28 20.90 ?  169 LEU   A C    1 
ATOM   3825 O  O    A LEU   A 1 169 ? 7.278  -20.414 1.541   0.72 24.13 ?  169 LEU   A O    1 
ATOM   3826 O  O    B LEU   A 1 169 ? 5.184  -21.407 -0.194  0.28 21.77 ?  169 LEU   A O    1 
ATOM   3827 C  CB   A LEU   A 1 169 ? 7.343  -19.561 -1.880  0.72 25.19 ?  169 LEU   A CB   1 
ATOM   3828 C  CB   B LEU   A 1 169 ? 4.797  -20.241 2.731   0.28 19.77 ?  169 LEU   A CB   1 
ATOM   3829 C  CG   A LEU   A 1 169 ? 7.059  -21.031 -2.205  0.72 26.64 ?  169 LEU   A CG   1 
ATOM   3830 C  CG   B LEU   A 1 169 ? 4.981  -21.732 3.034   0.28 19.98 ?  169 LEU   A CG   1 
ATOM   3831 C  CD1  A LEU   A 1 169 ? 5.640  -21.416 -1.813  0.72 27.28 ?  169 LEU   A CD1  1 
ATOM   3832 C  CD1  B LEU   A 1 169 ? 6.449  -22.050 3.269   0.28 20.35 ?  169 LEU   A CD1  1 
ATOM   3833 C  CD2  A LEU   A 1 169 ? 7.296  -21.315 -3.682  0.72 27.01 ?  169 LEU   A CD2  1 
ATOM   3834 C  CD2  B LEU   A 1 169 ? 4.141  -22.157 4.231   0.28 20.29 ?  169 LEU   A CD2  1 
ATOM   3835 O  OXT  A LEU   A 1 169 ? 9.056  -19.993 0.464   0.72 22.99 -1 169 LEU   A OXT  1 
ATOM   3836 O  OXT  B LEU   A 1 169 ? 4.036  -19.650 -0.407  0.28 21.24 -1 169 LEU   A OXT  1 
ATOM   3837 H  H    A LEU   A 1 169 ? 7.908  -17.382 -0.668  0.72 25.37 ?  169 LEU   A H    1 
ATOM   3838 H  H    B LEU   A 1 169 ? 4.961  -17.890 1.933   0.28 21.19 ?  169 LEU   A H    1 
ATOM   3839 H  HA   A LEU   A 1 169 ? 6.069  -19.328 -0.288  0.72 28.31 ?  169 LEU   A HA   1 
ATOM   3840 H  HA   B LEU   A 1 169 ? 6.440  -20.063 1.519   0.28 23.31 ?  169 LEU   A HA   1 
ATOM   3841 H  HB2  A LEU   A 1 169 ? 6.823  -19.023 -2.498  0.72 30.20 ?  169 LEU   A HB2  1 
ATOM   3842 H  HB2  B LEU   A 1 169 ? 5.118  -19.749 3.503   0.28 23.69 ?  169 LEU   A HB2  1 
ATOM   3843 H  HB3  A LEU   A 1 169 ? 8.287  -19.408 -2.033  0.72 30.20 ?  169 LEU   A HB3  1 
ATOM   3844 H  HB3  B LEU   A 1 169 ? 3.848  -20.085 2.618   0.28 23.69 ?  169 LEU   A HB3  1 
ATOM   3845 H  HG   A LEU   A 1 169 ? 7.668  -21.588 -1.697  0.72 31.94 ?  169 LEU   A HG   1 
ATOM   3846 H  HG   B LEU   A 1 169 ? 4.686  -22.247 2.268   0.28 23.95 ?  169 LEU   A HG   1 
ATOM   3847 H  HD11 A LEU   A 1 169 ? 5.423  -22.273 -2.211  0.72 32.71 ?  169 LEU   A HD11 1 
ATOM   3848 H  HD11 B LEU   A 1 169 ? 6.520  -22.922 3.687   0.28 24.39 ?  169 LEU   A HD11 1 
ATOM   3849 H  HD12 A LEU   A 1 169 ? 5.584  -21.477 -0.847  0.72 32.71 ?  169 LEU   A HD12 1 
ATOM   3850 H  HD12 B LEU   A 1 169 ? 6.914  -22.053 2.417   0.28 24.39 ?  169 LEU   A HD12 1 
ATOM   3851 H  HD13 A LEU   A 1 169 ? 5.027  -20.737 -2.139  0.72 32.71 ?  169 LEU   A HD13 1 
ATOM   3852 H  HD13 B LEU   A 1 169 ? 6.829  -21.373 3.852   0.28 24.39 ?  169 LEU   A HD13 1 
ATOM   3853 H  HD21 A LEU   A 1 169 ? 7.116  -22.252 -3.857  0.72 32.38 ?  169 LEU   A HD21 1 
ATOM   3854 H  HD21 B LEU   A 1 169 ? 4.274  -23.105 4.390   0.28 24.32 ?  169 LEU   A HD21 1 
ATOM   3855 H  HD22 A LEU   A 1 169 ? 6.699  -20.761 -4.210  0.72 32.38 ?  169 LEU   A HD22 1 
ATOM   3856 H  HD22 B LEU   A 1 169 ? 4.423  -21.650 5.010   0.28 24.32 ?  169 LEU   A HD22 1 
ATOM   3857 H  HD23 A LEU   A 1 169 ? 8.218  -21.108 -3.900  0.72 32.38 ?  169 LEU   A HD23 1 
ATOM   3858 H  HD23 B LEU   A 1 169 ? 3.208  -21.980 4.040   0.28 24.32 ?  169 LEU   A HD23 1 
ATOM   3859 N  N    A SER   B 1 1   ? 50.790 -9.253  -23.751 0.72 28.84 ?  1   SER   B N    1 
ATOM   3860 N  N    B SER   B 1 1   ? 50.683 -9.207  -23.701 0.28 26.93 ?  1   SER   B N    1 
ATOM   3861 C  CA   A SER   B 1 1   ? 51.273 -10.298 -22.827 0.72 28.97 ?  1   SER   B CA   1 
ATOM   3862 C  CA   B SER   B 1 1   ? 51.192 -10.229 -22.763 0.28 26.73 ?  1   SER   B CA   1 
ATOM   3863 C  C    A SER   B 1 1   ? 50.190 -11.334 -22.559 0.72 27.70 ?  1   SER   B C    1 
ATOM   3864 C  C    B SER   B 1 1   ? 50.134 -11.296 -22.517 0.28 25.88 ?  1   SER   B C    1 
ATOM   3865 O  O    A SER   B 1 1   ? 48.996 -11.116 -22.812 0.72 27.33 ?  1   SER   B O    1 
ATOM   3866 O  O    B SER   B 1 1   ? 48.970 -11.145 -22.899 0.28 25.54 ?  1   SER   B O    1 
ATOM   3867 C  CB   A SER   B 1 1   ? 51.743 -9.688  -21.509 0.72 29.86 ?  1   SER   B CB   1 
ATOM   3868 C  CB   B SER   B 1 1   ? 51.598 -9.588  -21.441 0.28 27.09 ?  1   SER   B CB   1 
ATOM   3869 O  OG   A SER   B 1 1   ? 50.642 -9.364  -20.681 0.72 31.69 ?  1   SER   B OG   1 
ATOM   3870 O  OG   B SER   B 1 1   ? 50.492 -9.513  -20.561 0.28 27.84 ?  1   SER   B OG   1 
ATOM   3871 H  H1   A SER   B 1 1   ? 50.706 -9.601  -24.563 0.72 34.58 ?  1   SER   B H1   1 
ATOM   3872 H  H1   B SER   B 1 1   ? 51.369 -8.740  -24.017 0.28 32.29 ?  1   SER   B H1   1 
ATOM   3873 H  H2   A SER   B 1 1   ? 50.008 -8.954  -23.465 0.72 34.58 ?  1   SER   B H2   1 
ATOM   3874 H  H2   B SER   B 1 1   ? 50.261 -9.612  -24.369 0.28 32.29 ?  1   SER   B H2   1 
ATOM   3875 H  H3   A SER   B 1 1   ? 51.382 -8.591  -23.767 0.72 34.58 ?  1   SER   B H3   1 
ATOM   3876 H  H3   B SER   B 1 1   ? 50.125 -8.671  -23.270 0.28 32.29 ?  1   SER   B H3   1 
ATOM   3877 H  HA   A SER   B 1 1   ? 52.025 -10.741 -23.243 0.72 34.73 ?  1   SER   B HA   1 
ATOM   3878 H  HA   B SER   B 1 1   ? 51.970 -10.645 -23.158 0.28 32.04 ?  1   SER   B HA   1 
ATOM   3879 H  HB2  A SER   B 1 1   ? 52.304 -10.333 -21.053 0.72 35.80 ?  1   SER   B HB2  1 
ATOM   3880 H  HB2  B SER   B 1 1   ? 52.296 -10.127 -21.039 0.28 32.48 ?  1   SER   B HB2  1 
ATOM   3881 H  HB3  A SER   B 1 1   ? 52.247 -8.880  -21.694 0.72 35.80 ?  1   SER   B HB3  1 
ATOM   3882 H  HB3  B SER   B 1 1   ? 51.927 -8.691  -21.610 0.28 32.48 ?  1   SER   B HB3  1 
ATOM   3883 H  HG   A SER   B 1 1   ? 50.891 -8.840  -20.072 0.72 38.00 ?  1   SER   B HG   1 
ATOM   3884 H  HG   B SER   B 1 1   ? 50.569 -8.838  -20.068 0.28 33.38 ?  1   SER   B HG   1 
ATOM   3885 N  N    A MET   B 1 2   ? 50.634 -12.464 -22.030 0.72 26.57 ?  2   MET   B N    1 
ATOM   3886 N  N    B MET   B 1 2   ? 50.553 -12.373 -21.860 0.28 25.21 ?  2   MET   B N    1 
ATOM   3887 C  CA   A MET   B 1 2   ? 49.809 -13.652 -21.862 0.72 26.55 ?  2   MET   B CA   1 
ATOM   3888 C  CA   B MET   B 1 2   ? 49.741 -13.571 -21.690 0.28 24.75 ?  2   MET   B CA   1 
ATOM   3889 C  C    A MET   B 1 2   ? 49.575 -13.858 -20.373 0.72 24.11 ?  2   MET   B C    1 
ATOM   3890 C  C    B MET   B 1 2   ? 49.475 -13.766 -20.204 0.28 23.20 ?  2   MET   B C    1 
ATOM   3891 O  O    A MET   B 1 2   ? 50.514 -14.146 -19.625 0.72 24.17 ?  2   MET   B O    1 
ATOM   3892 O  O    B MET   B 1 2   ? 50.376 -14.156 -19.453 0.28 23.46 ?  2   MET   B O    1 
ATOM   3893 C  CB   A MET   B 1 2   ? 50.535 -14.846 -22.470 0.72 30.52 ?  2   MET   B CB   1 
ATOM   3894 C  CB   B MET   B 1 2   ? 50.487 -14.765 -22.270 0.28 26.30 ?  2   MET   B CB   1 
ATOM   3895 C  CG   A MET   B 1 2   ? 49.688 -16.094 -22.637 0.72 33.98 ?  2   MET   B CG   1 
ATOM   3896 C  CG   B MET   B 1 2   ? 49.609 -15.908 -22.752 0.28 27.48 ?  2   MET   B CG   1 
ATOM   3897 S  SD   A MET   B 1 2   ? 50.550 -17.331 -23.625 0.72 37.41 ?  2   MET   B SD   1 
ATOM   3898 S  SD   B MET   B 1 2   ? 50.518 -16.998 -23.855 0.28 28.62 ?  2   MET   B SD   1 
ATOM   3899 C  CE   A MET   B 1 2   ? 51.102 -16.305 -24.981 0.72 37.68 ?  2   MET   B CE   1 
ATOM   3900 C  CE   B MET   B 1 2   ? 51.410 -15.798 -24.823 0.28 28.85 ?  2   MET   B CE   1 
ATOM   3901 H  H    A MET   B 1 2   ? 51.441 -12.577 -21.754 0.72 31.85 ?  2   MET   B H    1 
ATOM   3902 H  H    B MET   B 1 2   ? 51.333 -12.439 -21.503 0.28 30.22 ?  2   MET   B H    1 
ATOM   3903 H  HA   A MET   B 1 2   ? 48.964 -13.543 -22.321 0.72 31.83 ?  2   MET   B HA   1 
ATOM   3904 H  HA   B MET   B 1 2   ? 48.909 -13.481 -22.177 0.28 29.67 ?  2   MET   B HA   1 
ATOM   3905 H  HB2  A MET   B 1 2   ? 50.854 -14.563 -23.337 0.72 36.60 ?  2   MET   B HB2  1 
ATOM   3906 H  HB2  B MET   B 1 2   ? 51.012 -14.415 -23.001 0.28 31.53 ?  2   MET   B HB2  1 
ATOM   3907 H  HB3  A MET   B 1 2   ? 51.287 -15.088 -21.910 0.72 36.60 ?  2   MET   B HB3  1 
ATOM   3908 H  HB3  B MET   B 1 2   ? 51.076 -15.140 -21.608 0.28 31.53 ?  2   MET   B HB3  1 
ATOM   3909 H  HG2  A MET   B 1 2   ? 49.501 -16.473 -21.761 0.72 40.75 ?  2   MET   B HG2  1 
ATOM   3910 H  HG2  B MET   B 1 2   ? 49.310 -16.430 -21.987 0.28 32.95 ?  2   MET   B HG2  1 
ATOM   3911 H  HG3  A MET   B 1 2   ? 48.862 -15.870 -23.092 0.72 40.75 ?  2   MET   B HG3  1 
ATOM   3912 H  HG3  B MET   B 1 2   ? 48.848 -15.565 -23.239 0.28 32.95 ?  2   MET   B HG3  1 
ATOM   3913 H  HE1  A MET   B 1 2   ? 51.270 -16.867 -25.742 0.72 45.18 ?  2   MET   B HE1  1 
ATOM   3914 H  HE1  B MET   B 1 2   ? 51.634 -16.211 -25.649 0.28 34.59 ?  2   MET   B HE1  1 
ATOM   3915 H  HE2  A MET   B 1 2   ? 50.401 -15.662 -25.186 0.72 45.18 ?  2   MET   B HE2  1 
ATOM   3916 H  HE2  B MET   B 1 2   ? 50.837 -15.027 -24.982 0.28 34.59 ?  2   MET   B HE2  1 
ATOM   3917 H  HE3  A MET   B 1 2   ? 51.914 -15.833 -24.724 0.72 45.18 ?  2   MET   B HE3  1 
ATOM   3918 H  HE3  B MET   B 1 2   ? 52.216 -15.527 -24.345 0.28 34.59 ?  2   MET   B HE3  1 
ATOM   3919 N  N    A VAL   B 1 3   ? 48.328 -13.682 -19.942 0.72 21.46 ?  3   VAL   B N    1 
ATOM   3920 N  N    B VAL   B 1 3   ? 48.247 -13.481 -19.779 0.28 21.27 ?  3   VAL   B N    1 
ATOM   3921 C  CA   A VAL   B 1 3   ? 47.921 -13.940 -18.569 0.72 20.25 ?  3   VAL   B CA   1 
ATOM   3922 C  CA   B VAL   B 1 3   ? 47.811 -13.751 -18.416 0.28 19.81 ?  3   VAL   B CA   1 
ATOM   3923 C  C    A VAL   B 1 3   ? 46.678 -14.820 -18.591 0.72 18.49 ?  3   VAL   B C    1 
ATOM   3924 C  C    B VAL   B 1 3   ? 46.554 -14.607 -18.457 0.28 18.17 ?  3   VAL   B C    1 
ATOM   3925 O  O    A VAL   B 1 3   ? 45.961 -14.903 -19.591 0.72 18.93 ?  3   VAL   B O    1 
ATOM   3926 O  O    B VAL   B 1 3   ? 45.714 -14.475 -19.353 0.28 18.08 ?  3   VAL   B O    1 
ATOM   3927 C  CB   A VAL   B 1 3   ? 47.653 -12.637 -17.783 0.72 21.78 ?  3   VAL   B CB   1 
ATOM   3928 C  CB   B VAL   B 1 3   ? 47.567 -12.464 -17.597 0.28 20.23 ?  3   VAL   B CB   1 
ATOM   3929 C  CG1  A VAL   B 1 3   ? 48.927 -11.795 -17.683 0.72 22.29 ?  3   VAL   B CG1  1 
ATOM   3930 C  CG1  B VAL   B 1 3   ? 48.849 -11.651 -17.485 0.28 20.41 ?  3   VAL   B CG1  1 
ATOM   3931 C  CG2  A VAL   B 1 3   ? 46.533 -11.845 -18.438 0.72 22.61 ?  3   VAL   B CG2  1 
ATOM   3932 C  CG2  B VAL   B 1 3   ? 46.448 -11.641 -18.212 0.28 20.45 ?  3   VAL   B CG2  1 
ATOM   3933 H  H    A VAL   B 1 3   ? 47.687 -13.410 -20.444 0.72 25.72 ?  3   VAL   B H    1 
ATOM   3934 H  H    B VAL   B 1 3   ? 47.646 -13.118 -20.277 0.28 25.49 ?  3   VAL   B H    1 
ATOM   3935 H  HA   A VAL   B 1 3   ? 48.627 -14.426 -18.111 0.72 24.27 ?  3   VAL   B HA   1 
ATOM   3936 H  HA   B VAL   B 1 3   ? 48.500 -14.261 -17.967 0.28 23.74 ?  3   VAL   B HA   1 
ATOM   3937 H  HB   A VAL   B 1 3   ? 47.377 -12.865 -16.882 0.72 26.10 ?  3   VAL   B HB   1 
ATOM   3938 H  HB   B VAL   B 1 3   ? 47.294 -12.716 -16.702 0.28 24.24 ?  3   VAL   B HB   1 
ATOM   3939 H  HG11 A VAL   B 1 3   ? 48.732 -10.992 -17.175 0.72 26.72 ?  3   VAL   B HG11 1 
ATOM   3940 H  HG11 B VAL   B 1 3   ? 48.673 -10.861 -16.952 0.28 24.46 ?  3   VAL   B HG11 1 
ATOM   3941 H  HG12 A VAL   B 1 3   ? 49.613 -12.314 -17.233 0.72 26.72 ?  3   VAL   B HG12 1 
ATOM   3942 H  HG12 B VAL   B 1 3   ? 49.530 -12.195 -17.059 0.28 24.46 ?  3   VAL   B HG12 1 
ATOM   3943 H  HG13 A VAL   B 1 3   ? 49.220 -11.561 -18.576 0.72 26.72 ?  3   VAL   B HG13 1 
ATOM   3944 H  HG13 B VAL   B 1 3   ? 49.138 -11.394 -18.374 0.28 24.46 ?  3   VAL   B HG13 1 
ATOM   3945 H  HG21 A VAL   B 1 3   ? 46.477 -10.976 -18.016 0.72 27.11 ?  3   VAL   B HG21 1 
ATOM   3946 H  HG21 B VAL   B 1 3   ? 46.415 -10.780 -17.771 0.28 24.51 ?  3   VAL   B HG21 1 
ATOM   3947 H  HG22 A VAL   B 1 3   ? 46.727 -11.746 -19.382 0.72 27.11 ?  3   VAL   B HG22 1 
ATOM   3948 H  HG22 B VAL   B 1 3   ? 46.626 -11.524 -19.158 0.28 24.51 ?  3   VAL   B HG22 1 
ATOM   3949 H  HG23 A VAL   B 1 3   ? 45.698 -12.326 -18.320 0.72 27.11 ?  3   VAL   B HG23 1 
ATOM   3950 H  HG23 B VAL   B 1 3   ? 45.606 -12.109 -18.090 0.28 24.51 ?  3   VAL   B HG23 1 
ATOM   3951 N  N    . ASN   B 1 4   ? 46.428 -15.486 -17.466 1.00 16.95 ?  4   ASN   B N    1 
ATOM   3952 C  CA   . ASN   B 1 4   ? 45.288 -16.397 -17.355 1.00 15.99 ?  4   ASN   B CA   1 
ATOM   3953 C  C    . ASN   B 1 4   ? 45.236 -17.364 -18.537 1.00 16.59 ?  4   ASN   B C    1 
ATOM   3954 O  O    . ASN   B 1 4   ? 44.175 -17.629 -19.101 1.00 17.40 ?  4   ASN   B O    1 
ATOM   3955 C  CB   . ASN   B 1 4   ? 43.965 -15.640 -17.193 1.00 15.35 ?  4   ASN   B CB   1 
ATOM   3956 C  CG   . ASN   B 1 4   ? 43.923 -14.819 -15.920 1.00 14.61 ?  4   ASN   B CG   1 
ATOM   3957 O  OD1  . ASN   B 1 4   ? 44.216 -15.329 -14.836 1.00 14.43 ?  4   ASN   B OD1  1 
ATOM   3958 N  ND2  . ASN   B 1 4   ? 43.580 -13.538 -16.043 1.00 15.73 ?  4   ASN   B ND2  1 
ATOM   3959 H  H    A ASN   B 1 4   ? 46.905 -15.432 -16.755 0.72 20.31 ?  4   ASN   B H    1 
ATOM   3960 H  H    B ASN   B 1 4   ? 47.001 -15.574 -16.833 0.28 20.31 ?  4   ASN   B H    1 
ATOM   3961 H  HA   . ASN   B 1 4   ? 45.412 -16.930 -16.552 1.00 19.16 ?  4   ASN   B HA   1 
ATOM   3962 H  HB2  . ASN   B 1 4   ? 43.844 -15.041 -17.945 1.00 18.39 ?  4   ASN   B HB2  1 
ATOM   3963 H  HB3  . ASN   B 1 4   ? 43.236 -16.283 -17.163 1.00 18.39 ?  4   ASN   B HB3  1 
ATOM   3964 H  HD21 . ASN   B 1 4   ? 43.545 -13.030 -15.347 1.00 18.84 ?  4   ASN   B HD21 1 
ATOM   3965 H  HD22 . ASN   B 1 4   ? 43.389 -13.211 -16.817 1.00 18.84 ?  4   ASN   B HD22 1 
ATOM   3966 N  N    . SER   B 1 5   ? 46.396 -17.897 -18.915 1.00 17.32 ?  5   SER   B N    1 
ATOM   3967 C  CA   . SER   B 1 5   ? 46.493 -18.815 -20.050 1.00 19.95 ?  5   SER   B CA   1 
ATOM   3968 C  C    . SER   B 1 5   ? 46.485 -20.250 -19.531 1.00 21.35 ?  5   SER   B C    1 
ATOM   3969 O  O    . SER   B 1 5   ? 47.497 -20.944 -19.493 1.00 23.70 ?  5   SER   B O    1 
ATOM   3970 C  CB   . SER   B 1 5   ? 47.745 -18.518 -20.870 1.00 21.88 ?  5   SER   B CB   1 
ATOM   3971 O  OG   . SER   B 1 5   ? 48.918 -18.663 -20.084 1.00 24.58 ?  5   SER   B OG   1 
ATOM   3972 H  H    . SER   B 1 5   ? 47.148 -17.750 -18.525 1.00 20.75 ?  5   SER   B H    1 
ATOM   3973 H  HA   . SER   B 1 5   ? 45.722 -18.697 -20.626 1.00 23.91 ?  5   SER   B HA   1 
ATOM   3974 H  HB2  . SER   B 1 5   ? 47.779 -19.133 -21.622 1.00 26.23 ?  5   SER   B HB2  1 
ATOM   3975 H  HB3  . SER   B 1 5   ? 47.684 -17.608 -21.194 1.00 26.23 ?  5   SER   B HB3  1 
ATOM   3976 H  HG   . SER   B 1 5   ? 48.993 -19.456 -19.822 1.00 29.47 ?  5   SER   B HG   1 
ATOM   3977 N  N    . PHE   B 1 6   ? 45.300 -20.674 -19.108 1.00 21.56 ?  6   PHE   B N    1 
ATOM   3978 C  CA   . PHE   B 1 6   ? 45.107 -22.016 -18.584 1.00 20.92 ?  6   PHE   B CA   1 
ATOM   3979 C  C    . PHE   B 1 6   ? 45.033 -23.006 -19.737 1.00 24.22 ?  6   PHE   B C    1 
ATOM   3980 O  O    . PHE   B 1 6   ? 44.368 -22.752 -20.743 1.00 26.43 ?  6   PHE   B O    1 
ATOM   3981 C  CB   . PHE   B 1 6   ? 43.813 -22.066 -17.771 1.00 18.83 ?  6   PHE   B CB   1 
ATOM   3982 C  CG   . PHE   B 1 6   ? 43.835 -21.207 -16.539 1.00 17.04 ?  6   PHE   B CG   1 
ATOM   3983 C  CD1  . PHE   B 1 6   ? 44.353 -21.694 -15.354 1.00 15.78 ?  6   PHE   B CD1  1 
ATOM   3984 C  CD2  . PHE   B 1 6   ? 43.340 -19.911 -16.567 1.00 16.53 ?  6   PHE   B CD2  1 
ATOM   3985 C  CE1  . PHE   B 1 6   ? 44.369 -20.910 -14.212 1.00 15.25 ?  6   PHE   B CE1  1 
ATOM   3986 C  CE2  . PHE   B 1 6   ? 43.364 -19.115 -15.432 1.00 16.85 ?  6   PHE   B CE2  1 
ATOM   3987 C  CZ   . PHE   B 1 6   ? 43.883 -19.610 -14.256 1.00 16.01 ?  6   PHE   B CZ   1 
ATOM   3988 H  H    . PHE   B 1 6   ? 44.584 -20.202 -19.121 1.00 25.85 ?  6   PHE   B H    1 
ATOM   3989 H  HA   . PHE   B 1 6   ? 45.847 -22.259 -18.007 1.00 25.08 ?  6   PHE   B HA   1 
ATOM   3990 H  HB2  . PHE   B 1 6   ? 43.081 -21.760 -18.329 1.00 22.57 ?  6   PHE   B HB2  1 
ATOM   3991 H  HB3  . PHE   B 1 6   ? 43.653 -22.980 -17.489 1.00 22.57 ?  6   PHE   B HB3  1 
ATOM   3992 H  HD1  . PHE   B 1 6   ? 44.694 -22.557 -15.320 1.00 18.91 ?  6   PHE   B HD1  1 
ATOM   3993 H  HD2  . PHE   B 1 6   ? 42.989 -19.572 -17.356 1.00 19.80 ?  6   PHE   B HD2  1 
ATOM   3994 H  HE1  . PHE   B 1 6   ? 44.734 -21.243 -13.421 1.00 18.28 ?  6   PHE   B HE1  1 
ATOM   3995 H  HE2  . PHE   B 1 6   ? 43.024 -18.248 -15.462 1.00 20.19 ?  6   PHE   B HE2  1 
ATOM   3996 H  HZ   . PHE   B 1 6   ? 43.897 -19.082 -13.489 1.00 19.19 ?  6   PHE   B HZ   1 
ATOM   3997 N  N    . SER   B 1 7   ? 45.736 -24.131 -19.593 1.00 24.98 ?  7   SER   B N    1 
ATOM   3998 C  CA   . SER   B 1 7   ? 45.821 -25.130 -20.649 1.00 27.59 ?  7   SER   B CA   1 
ATOM   3999 C  C    . SER   B 1 7   ? 45.785 -26.528 -20.052 1.00 26.62 ?  7   SER   B C    1 
ATOM   4000 O  O    . SER   B 1 7   ? 46.377 -26.782 -18.999 1.00 27.67 ?  7   SER   B O    1 
ATOM   4001 C  CB   . SER   B 1 7   ? 47.108 -24.953 -21.466 1.00 30.63 ?  7   SER   B CB   1 
ATOM   4002 O  OG   . SER   B 1 7   ? 47.100 -25.780 -22.615 1.00 32.67 ?  7   SER   B OG   1 
ATOM   4003 H  H    . SER   B 1 7   ? 46.183 -24.338 -18.883 1.00 29.95 ?  7   SER   B H    1 
ATOM   4004 H  HA   . SER   B 1 7   ? 45.065 -25.038 -21.245 1.00 33.08 ?  7   SER   B HA   1 
ATOM   4005 H  HB2  . SER   B 1 7   ? 47.177 -24.027 -21.746 1.00 36.73 ?  7   SER   B HB2  1 
ATOM   4006 H  HB3  . SER   B 1 7   ? 47.870 -25.188 -20.911 1.00 36.73 ?  7   SER   B HB3  1 
ATOM   4007 H  HG   . SER   B 1 7   ? 47.811 -25.676 -23.051 1.00 39.17 ?  7   SER   B HG   1 
ATOM   4008 N  N    . GLY   B 1 8   ? 45.091 -27.435 -20.737 1.00 26.40 ?  8   GLY   B N    1 
ATOM   4009 C  CA   . GLY   B 1 8   ? 45.062 -28.824 -20.337 1.00 25.82 ?  8   GLY   B CA   1 
ATOM   4010 C  C    . GLY   B 1 8   ? 44.097 -29.149 -19.226 1.00 24.21 ?  8   GLY   B C    1 
ATOM   4011 O  O    . GLY   B 1 8   ? 44.222 -30.214 -18.607 1.00 25.66 ?  8   GLY   B O    1 
ATOM   4012 H  H    . GLY   B 1 8   ? 44.627 -27.260 -21.436 1.00 31.66 ?  8   GLY   B H    1 
ATOM   4013 H  HA2  . GLY   B 1 8   ? 44.820 -29.366 -21.101 1.00 30.96 ?  8   GLY   B HA2  1 
ATOM   4014 H  HA3  . GLY   B 1 8   ? 45.945 -29.089 -20.044 1.00 30.96 ?  8   GLY   B HA3  1 
ATOM   4015 N  N    . TYR   B 1 9   ? 43.118 -28.285 -18.963 1.00 22.35 ?  9   TYR   B N    1 
ATOM   4016 C  CA   . TYR   B 1 9   ? 42.152 -28.552 -17.910 1.00 20.53 ?  9   TYR   B CA   1 
ATOM   4017 C  C    . TYR   B 1 9   ? 40.970 -29.345 -18.438 1.00 19.92 ?  9   TYR   B C    1 
ATOM   4018 O  O    . TYR   B 1 9   ? 40.563 -29.209 -19.595 1.00 21.93 ?  9   TYR   B O    1 
ATOM   4019 C  CB   . TYR   B 1 9   ? 41.642 -27.263 -17.273 1.00 20.10 ?  9   TYR   B CB   1 
ATOM   4020 C  CG   . TYR   B 1 9   ? 42.663 -26.634 -16.358 1.00 19.36 ?  9   TYR   B CG   1 
ATOM   4021 C  CD1  . TYR   B 1 9   ? 43.762 -25.965 -16.876 1.00 19.67 ?  9   TYR   B CD1  1 
ATOM   4022 C  CD2  . TYR   B 1 9   ? 42.544 -26.730 -14.980 1.00 18.44 ?  9   TYR   B CD2  1 
ATOM   4023 C  CE1  . TYR   B 1 9   ? 44.710 -25.405 -16.048 1.00 19.61 ?  9   TYR   B CE1  1 
ATOM   4024 C  CE2  . TYR   B 1 9   ? 43.489 -26.170 -14.142 1.00 18.71 ?  9   TYR   B CE2  1 
ATOM   4025 C  CZ   . TYR   B 1 9   ? 44.570 -25.504 -14.684 1.00 19.59 ?  9   TYR   B CZ   1 
ATOM   4026 O  OH   . TYR   B 1 9   ? 45.520 -24.950 -13.865 1.00 20.16 ?  9   TYR   B OH   1 
ATOM   4027 H  H    . TYR   B 1 9   ? 42.973 -27.557 -19.397 1.00 26.79 ?  9   TYR   B H    1 
ATOM   4028 H  HA   . TYR   B 1 9   ? 42.571 -29.078 -17.218 1.00 24.60 ?  9   TYR   B HA   1 
ATOM   4029 H  HB2  . TYR   B 1 9   ? 41.419 -26.622 -17.968 1.00 24.09 ?  9   TYR   B HB2  1 
ATOM   4030 H  HB3  . TYR   B 1 9   ? 40.857 -27.470 -16.746 1.00 24.09 ?  9   TYR   B HB3  1 
ATOM   4031 H  HD1  . TYR   B 1 9   ? 43.859 -25.898 -17.800 1.00 23.58 ?  9   TYR   B HD1  1 
ATOM   4032 H  HD2  . TYR   B 1 9   ? 41.814 -27.182 -14.615 1.00 22.09 ?  9   TYR   B HD2  1 
ATOM   4033 H  HE1  . TYR   B 1 9   ? 45.436 -24.960 -16.411 1.00 23.51 ?  9   TYR   B HE1  1 
ATOM   4034 H  HE2  . TYR   B 1 9   ? 43.389 -26.244 -13.218 1.00 22.42 ?  9   TYR   B HE2  1 
ATOM   4035 H  HH   . TYR   B 1 9   ? 46.110 -24.579 -14.326 1.00 24.16 ?  9   TYR   B HH   1 
ATOM   4036 N  N    . LEU   B 1 10  ? 40.425 -30.181 -17.564 1.00 18.07 ?  10  LEU   B N    1 
ATOM   4037 C  CA   . LEU   B 1 10  ? 39.221 -30.943 -17.836 1.00 17.95 ?  10  LEU   B CA   1 
ATOM   4038 C  C    . LEU   B 1 10  ? 38.033 -30.176 -17.270 1.00 17.57 ?  10  LEU   B C    1 
ATOM   4039 O  O    . LEU   B 1 10  ? 38.050 -29.766 -16.105 1.00 17.47 ?  10  LEU   B O    1 
ATOM   4040 C  CB   . LEU   B 1 10  ? 39.334 -32.314 -17.173 1.00 19.00 ?  10  LEU   B CB   1 
ATOM   4041 C  CG   . LEU   B 1 10  ? 38.182 -33.264 -17.467 1.00 20.79 ?  10  LEU   B CG   1 
ATOM   4042 C  CD1  . LEU   B 1 10  ? 38.254 -33.773 -18.902 1.00 22.34 ?  10  LEU   B CD1  1 
ATOM   4043 C  CD2  . LEU   B 1 10  ? 38.177 -34.412 -16.473 1.00 22.04 ?  10  LEU   B CD2  1 
ATOM   4044 H  H    . LEU   B 1 10  ? 40.740 -30.323 -16.769 1.00 21.65 ?  10  LEU   B H    1 
ATOM   4045 H  HA   . LEU   B 1 10  ? 39.104 -31.059 -18.790 1.00 21.51 ?  10  LEU   B HA   1 
ATOM   4046 H  HB2  . LEU   B 1 10  ? 40.153 -32.740 -17.481 1.00 22.77 ?  10  LEU   B HB2  1 
ATOM   4047 H  HB3  . LEU   B 1 10  ? 39.377 -32.193 -16.211 1.00 22.77 ?  10  LEU   B HB3  1 
ATOM   4048 H  HG   . LEU   B 1 10  ? 37.346 -32.785 -17.367 1.00 24.91 ?  10  LEU   B HG   1 
ATOM   4049 H  HD11 . LEU   B 1 10  ? 37.538 -34.410 -19.046 1.00 26.78 ?  10  LEU   B HD11 1 
ATOM   4050 H  HD12 . LEU   B 1 10  ? 38.155 -33.021 -19.508 1.00 26.78 ?  10  LEU   B HD12 1 
ATOM   4051 H  HD13 . LEU   B 1 10  ? 39.112 -34.201 -19.043 1.00 26.78 ?  10  LEU   B HD13 1 
ATOM   4052 H  HD21 . LEU   B 1 10  ? 37.443 -35.004 -16.686 1.00 26.42 ?  10  LEU   B HD21 1 
ATOM   4053 H  HD22 . LEU   B 1 10  ? 39.020 -34.882 -16.537 1.00 26.42 ?  10  LEU   B HD22 1 
ATOM   4054 H  HD23 . LEU   B 1 10  ? 38.064 -34.046 -15.581 1.00 26.42 ?  10  LEU   B HD23 1 
ATOM   4055 N  N    . LYS   B 1 11  ? 37.011 -29.983 -18.095 1.00 18.84 ?  11  LYS   B N    1 
ATOM   4056 C  CA   . LYS   B 1 11  ? 35.817 -29.264 -17.678 1.00 20.77 ?  11  LYS   B CA   1 
ATOM   4057 C  C    . LYS   B 1 11  ? 34.932 -30.190 -16.851 1.00 19.92 ?  11  LYS   B C    1 
ATOM   4058 O  O    . LYS   B 1 11  ? 34.550 -31.270 -17.315 1.00 21.90 ?  11  LYS   B O    1 
ATOM   4059 C  CB   . LYS   B 1 11  ? 35.076 -28.779 -18.923 1.00 24.76 ?  11  LYS   B CB   1 
ATOM   4060 C  CG   . LYS   B 1 11  ? 33.907 -27.847 -18.661 1.00 28.13 ?  11  LYS   B CG   1 
ATOM   4061 C  CD   . LYS   B 1 11  ? 33.173 -27.540 -19.961 1.00 31.05 ?  11  LYS   B CD   1 
ATOM   4062 C  CE   . LYS   B 1 11  ? 32.139 -26.444 -19.782 1.00 33.15 ?  11  LYS   B CE   1 
ATOM   4063 N  NZ   . LYS   B 1 11  ? 32.774 -25.116 -19.564 1.00 34.35 ?  11  LYS   B NZ   1 
ATOM   4064 H  H    . LYS   B 1 11  ? 36.982 -30.268 -18.906 1.00 22.57 ?  11  LYS   B H    1 
ATOM   4065 H  HA   . LYS   B 1 11  ? 36.066 -28.498 -17.139 1.00 24.90 ?  11  LYS   B HA   1 
ATOM   4066 H  HB2  . LYS   B 1 11  ? 35.705 -28.302 -19.489 1.00 29.68 ?  11  LYS   B HB2  1 
ATOM   4067 H  HB3  . LYS   B 1 11  ? 34.733 -29.550 -19.399 1.00 29.68 ?  11  LYS   B HB3  1 
ATOM   4068 H  HG2  . LYS   B 1 11  ? 33.284 -28.272 -18.051 1.00 33.73 ?  11  LYS   B HG2  1 
ATOM   4069 H  HG3  . LYS   B 1 11  ? 34.232 -27.013 -18.289 1.00 33.73 ?  11  LYS   B HG3  1 
ATOM   4070 H  HD2  . LYS   B 1 11  ? 33.815 -27.246 -20.627 1.00 37.23 ?  11  LYS   B HD2  1 
ATOM   4071 H  HD3  . LYS   B 1 11  ? 32.718 -28.341 -20.266 1.00 37.23 ?  11  LYS   B HD3  1 
ATOM   4072 H  HE2  . LYS   B 1 11  ? 31.589 -26.392 -20.580 1.00 39.75 ?  11  LYS   B HE2  1 
ATOM   4073 H  HE3  . LYS   B 1 11  ? 31.590 -26.652 -19.010 1.00 39.75 ?  11  LYS   B HE3  1 
ATOM   4074 H  HZ1  . LYS   B 1 11  ? 32.147 -24.489 -19.486 1.00 41.19 ?  11  LYS   B HZ1  1 
ATOM   4075 H  HZ2  . LYS   B 1 11  ? 33.264 -25.131 -18.822 1.00 41.19 ?  11  LYS   B HZ2  1 
ATOM   4076 H  HZ3  . LYS   B 1 11  ? 33.299 -24.914 -20.254 1.00 41.19 ?  11  LYS   B HZ3  1 
ATOM   4077 N  N    . LEU   B 1 12  ? 34.605 -29.774 -15.628 1.00 18.22 ?  12  LEU   B N    1 
ATOM   4078 C  CA   . LEU   B 1 12  ? 33.642 -30.484 -14.792 1.00 17.74 ?  12  LEU   B CA   1 
ATOM   4079 C  C    . LEU   B 1 12  ? 32.252 -29.873 -14.881 1.00 17.68 ?  12  LEU   B C    1 
ATOM   4080 O  O    . LEU   B 1 12  ? 31.263 -30.587 -15.057 1.00 18.22 ?  12  LEU   B O    1 
ATOM   4081 C  CB   . LEU   B 1 12  ? 34.105 -30.504 -13.331 1.00 17.32 ?  12  LEU   B CB   1 
ATOM   4082 C  CG   . LEU   B 1 12  ? 35.446 -31.181 -13.059 1.00 17.04 ?  12  LEU   B CG   1 
ATOM   4083 C  CD1  . LEU   B 1 12  ? 35.777 -31.126 -11.582 1.00 17.37 ?  12  LEU   B CD1  1 
ATOM   4084 C  CD2  . LEU   B 1 12  ? 35.451 -32.622 -13.559 1.00 17.68 ?  12  LEU   B CD2  1 
ATOM   4085 H  H    . LEU   B 1 12  ? 34.935 -29.072 -15.257 1.00 21.83 ?  12  LEU   B H    1 
ATOM   4086 H  HA   . LEU   B 1 12  ? 33.574 -31.398 -15.100 1.00 21.26 ?  12  LEU   B HA   1 
ATOM   4087 H  HB2  . LEU   B 1 12  ? 34.175 -29.590 -13.021 1.00 20.76 ?  12  LEU   B HB2  1 
ATOM   4088 H  HB3  . LEU   B 1 12  ? 33.434 -30.972 -12.809 1.00 20.76 ?  12  LEU   B HB3  1 
ATOM   4089 H  HG   . LEU   B 1 12  ? 36.138 -30.702 -13.537 1.00 20.41 ?  12  LEU   B HG   1 
ATOM   4090 H  HD11 . LEU   B 1 12  ? 36.634 -31.562 -11.434 1.00 20.82 ?  12  LEU   B HD11 1 
ATOM   4091 H  HD12 . LEU   B 1 12  ? 35.826 -30.200 -11.302 1.00 20.82 ?  12  LEU   B HD12 1 
ATOM   4092 H  HD13 . LEU   B 1 12  ? 35.085 -31.588 -11.082 1.00 20.82 ?  12  LEU   B HD13 1 
ATOM   4093 H  HD21 . LEU   B 1 12  ? 36.261 -33.058 -13.256 1.00 21.18 ?  12  LEU   B HD21 1 
ATOM   4094 H  HD22 . LEU   B 1 12  ? 34.674 -33.082 -13.204 1.00 21.18 ?  12  LEU   B HD22 1 
ATOM   4095 H  HD23 . LEU   B 1 12  ? 35.418 -32.621 -14.529 1.00 21.18 ?  12  LEU   B HD23 1 
ATOM   4096 N  N    . THR   B 1 13  ? 32.165 -28.554 -14.757 1.00 17.67 ?  13  THR   B N    1 
ATOM   4097 C  CA   . THR   B 1 13  ? 30.938 -27.807 -14.960 1.00 17.61 ?  13  THR   B CA   1 
ATOM   4098 C  C    . THR   B 1 13  ? 31.269 -26.610 -15.841 1.00 19.44 ?  13  THR   B C    1 
ATOM   4099 O  O    . THR   B 1 13  ? 32.412 -26.421 -16.270 1.00 20.15 ?  13  THR   B O    1 
ATOM   4100 C  CB   . THR   B 1 13  ? 30.340 -27.333 -13.631 1.00 17.34 ?  13  THR   B CB   1 
ATOM   4101 O  OG1  . THR   B 1 13  ? 31.181 -26.312 -13.083 1.00 17.20 ?  13  THR   B OG1  1 
ATOM   4102 C  CG2  . THR   B 1 13  ? 30.229 -28.487 -12.639 1.00 17.86 ?  13  THR   B CG2  1 
ATOM   4103 H  H    . THR   B 1 13  ? 32.831 -28.049 -14.547 1.00 21.17 ?  13  THR   B H    1 
ATOM   4104 H  HA   . THR   B 1 13  ? 30.283 -28.367 -15.409 1.00 21.10 ?  13  THR   B HA   1 
ATOM   4105 H  HB   . THR   B 1 13  ? 29.449 -26.969 -13.785 1.00 20.77 ?  13  THR   B HB   1 
ATOM   4106 H  HG1  . THR   B 1 13  ? 30.865 -25.548 -13.262 1.00 20.61 ?  13  THR   B HG1  1 
ATOM   4107 H  HG21 . THR   B 1 13  ? 29.737 -28.204 -11.852 1.00 21.40 ?  13  THR   B HG21 1 
ATOM   4108 H  HG22 . THR   B 1 13  ? 29.766 -29.233 -13.049 1.00 21.40 ?  13  THR   B HG22 1 
ATOM   4109 H  HG23 . THR   B 1 13  ? 31.116 -28.777 -12.368 1.00 21.40 ?  13  THR   B HG23 1 
ATOM   4110 N  N    A ASP   B 1 14  ? 30.256 -25.783 -16.099 0.72 20.68 ?  14  ASP   B N    1 
ATOM   4111 N  N    B ASP   B 1 14  ? 30.261 -25.771 -16.092 0.28 20.37 ?  14  ASP   B N    1 
ATOM   4112 C  CA   A ASP   B 1 14  ? 30.465 -24.621 -16.954 0.72 22.07 ?  14  ASP   B CA   1 
ATOM   4113 C  CA   B ASP   B 1 14  ? 30.460 -24.616 -16.962 0.28 21.21 ?  14  ASP   B CA   1 
ATOM   4114 C  C    A ASP   B 1 14  ? 31.566 -23.713 -16.421 0.72 20.11 ?  14  ASP   B C    1 
ATOM   4115 C  C    B ASP   B 1 14  ? 31.455 -23.613 -16.395 0.28 19.51 ?  14  ASP   B C    1 
ATOM   4116 O  O    A ASP   B 1 14  ? 32.230 -23.026 -17.206 0.72 21.33 ?  14  ASP   B O    1 
ATOM   4117 O  O    B ASP   B 1 14  ? 31.904 -22.728 -17.132 0.28 19.84 ?  14  ASP   B O    1 
ATOM   4118 C  CB   A ASP   B 1 14  ? 29.158 -23.845 -17.116 0.72 25.68 ?  14  ASP   B CB   1 
ATOM   4119 C  CB   B ASP   B 1 14  ? 29.133 -23.904 -17.223 0.28 23.69 ?  14  ASP   B CB   1 
ATOM   4120 C  CG   A ASP   B 1 14  ? 28.196 -24.510 -18.077 0.72 29.40 ?  14  ASP   B CG   1 
ATOM   4121 C  CG   B ASP   B 1 14  ? 28.253 -24.656 -18.205 0.28 25.95 ?  14  ASP   B CG   1 
ATOM   4122 O  OD1  A ASP   B 1 14  ? 28.582 -25.496 -18.746 0.72 30.77 ?  14  ASP   B OD1  1 
ATOM   4123 O  OD1  B ASP   B 1 14  ? 28.805 -25.307 -19.117 0.28 26.82 ?  14  ASP   B OD1  1 
ATOM   4124 O  OD2  A ASP   B 1 14  ? 27.042 -24.046 -18.158 0.72 30.84 -1 14  ASP   B OD2  1 
ATOM   4125 O  OD2  B ASP   B 1 14  ? 27.014 -24.604 -18.063 0.28 26.63 -1 14  ASP   B OD2  1 
ATOM   4126 H  H    A ASP   B 1 14  ? 29.458 -25.864 -15.785 0.72 24.78 ?  14  ASP   B H    1 
ATOM   4127 H  H    B ASP   B 1 14  ? 29.465 -25.846 -15.773 0.28 24.41 ?  14  ASP   B H    1 
ATOM   4128 H  HA   A ASP   B 1 14  ? 30.742 -24.921 -17.829 0.72 26.45 ?  14  ASP   B HA   1 
ATOM   4129 H  HA   B ASP   B 1 14  ? 30.803 -24.926 -17.813 0.28 25.43 ?  14  ASP   B HA   1 
ATOM   4130 H  HB2  A ASP   B 1 14  ? 28.709 -23.787 -16.259 0.72 30.79 ?  14  ASP   B HB2  1 
ATOM   4131 H  HB2  B ASP   B 1 14  ? 28.650 -23.821 -16.386 0.28 28.40 ?  14  ASP   B HB2  1 
ATOM   4132 H  HB3  A ASP   B 1 14  ? 29.350 -22.958 -17.454 0.72 30.79 ?  14  ASP   B HB3  1 
ATOM   4133 H  HB3  B ASP   B 1 14  ? 29.320 -23.018 -17.583 0.28 28.40 ?  14  ASP   B HB3  1 
ATOM   4134 N  N    . ASN   B 1 15  ? 31.787 -23.704 -15.104 1.00 17.73 ?  15  ASN   B N    1 
ATOM   4135 C  CA   . ASN   B 1 15  ? 32.745 -22.782 -14.499 1.00 15.46 ?  15  ASN   B CA   1 
ATOM   4136 C  C    . ASN   B 1 15  ? 33.837 -23.436 -13.664 1.00 14.05 ?  15  ASN   B C    1 
ATOM   4137 O  O    . ASN   B 1 15  ? 34.688 -22.710 -13.138 1.00 14.72 ?  15  ASN   B O    1 
ATOM   4138 C  CB   . ASN   B 1 15  ? 32.029 -21.731 -13.639 1.00 15.54 ?  15  ASN   B CB   1 
ATOM   4139 C  CG   . ASN   B 1 15  ? 31.403 -22.330 -12.401 1.00 15.03 ?  15  ASN   B CG   1 
ATOM   4140 O  OD1  . ASN   B 1 15  ? 30.460 -23.121 -12.491 1.00 16.81 ?  15  ASN   B OD1  1 
ATOM   4141 N  ND2  . ASN   B 1 15  ? 31.919 -21.976 -11.242 1.00 14.30 ?  15  ASN   B ND2  1 
ATOM   4142 H  H    A ASN   B 1 15  ? 31.394 -24.226 -14.542 0.72 21.24 ?  15  ASN   B H    1 
ATOM   4143 H  H    B ASN   B 1 15  ? 31.445 -24.271 -14.554 0.28 21.24 ?  15  ASN   B H    1 
ATOM   4144 H  HA   . ASN   B 1 15  ? 33.194 -22.303 -15.203 1.00 18.52 ?  15  ASN   B HA   1 
ATOM   4145 H  HB2  . ASN   B 1 15  ? 32.677 -21.054 -13.359 1.00 18.61 ?  15  ASN   B HB2  1 
ATOM   4146 H  HB3  . ASN   B 1 15  ? 31.327 -21.306 -14.162 1.00 18.61 ?  15  ASN   B HB3  1 
ATOM   4147 H  HD21 . ASN   B 1 15  ? 31.590 -22.286 -10.510 1.00 17.13 ?  15  ASN   B HD21 1 
ATOM   4148 H  HD22 . ASN   B 1 15  ? 32.584 -21.424 -11.208 1.00 17.13 ?  15  ASN   B HD22 1 
ATOM   4149 N  N    . VAL   B 1 16  ? 33.852 -24.760 -13.517 1.00 14.25 ?  16  VAL   B N    1 
ATOM   4150 C  CA   . VAL   B 1 16  ? 34.853 -25.451 -12.710 1.00 13.85 ?  16  VAL   B CA   1 
ATOM   4151 C  C    . VAL   B 1 16  ? 35.644 -26.388 -13.606 1.00 14.10 ?  16  VAL   B C    1 
ATOM   4152 O  O    . VAL   B 1 16  ? 35.065 -27.261 -14.270 1.00 15.37 ?  16  VAL   B O    1 
ATOM   4153 C  CB   . VAL   B 1 16  ? 34.225 -26.216 -11.531 1.00 14.37 ?  16  VAL   B CB   1 
ATOM   4154 C  CG1  . VAL   B 1 16  ? 35.304 -26.959 -10.739 1.00 14.41 ?  16  VAL   B CG1  1 
ATOM   4155 C  CG2  . VAL   B 1 16  ? 33.426 -25.276 -10.632 1.00 15.00 ?  16  VAL   B CG2  1 
ATOM   4156 H  H    . VAL   B 1 16  ? 33.274 -25.292 -13.877 1.00 17.06 ?  16  VAL   B H    1 
ATOM   4157 H  HA   . VAL   B 1 16  ? 35.466 -24.796 -12.340 1.00 16.59 ?  16  VAL   B HA   1 
ATOM   4158 H  HB   . VAL   B 1 16  ? 33.611 -26.881 -11.884 1.00 17.21 ?  16  VAL   B HB   1 
ATOM   4159 H  HG11 . VAL   B 1 16  ? 34.924 -27.263 -9.900  1.00 17.26 ?  16  VAL   B HG11 1 
ATOM   4160 H  HG12 . VAL   B 1 16  ? 35.615 -27.717 -11.255 1.00 17.26 ?  16  VAL   B HG12 1 
ATOM   4161 H  HG13 . VAL   B 1 16  ? 36.039 -26.349 -10.564 1.00 17.26 ?  16  VAL   B HG13 1 
ATOM   4162 H  HG21 . VAL   B 1 16  ? 33.087 -25.777 -9.874  1.00 17.97 ?  16  VAL   B HG21 1 
ATOM   4163 H  HG22 . VAL   B 1 16  ? 34.006 -24.564 -10.327 1.00 17.97 ?  16  VAL   B HG22 1 
ATOM   4164 H  HG23 . VAL   B 1 16  ? 32.686 -24.907 -11.141 1.00 17.97 ?  16  VAL   B HG23 1 
ATOM   4165 N  N    . TYR   B 1 17  ? 36.968 -26.229 -13.580 1.00 14.59 ?  17  TYR   B N    1 
ATOM   4166 C  CA   . TYR   B 1 17  ? 37.910 -26.980 -14.395 1.00 14.75 ?  17  TYR   B CA   1 
ATOM   4167 C  C    . TYR   B 1 17  ? 38.963 -27.589 -13.481 1.00 14.11 ?  17  TYR   B C    1 
ATOM   4168 O  O    . TYR   B 1 17  ? 39.243 -27.056 -12.403 1.00 14.42 ?  17  TYR   B O    1 
ATOM   4169 C  CB   . TYR   B 1 17  ? 38.615 -26.045 -15.388 1.00 17.34 ?  17  TYR   B CB   1 
ATOM   4170 C  CG   . TYR   B 1 17  ? 37.688 -25.277 -16.296 1.00 20.39 ?  17  TYR   B CG   1 
ATOM   4171 C  CD1  . TYR   B 1 17  ? 37.098 -24.089 -15.882 1.00 21.84 ?  17  TYR   B CD1  1 
ATOM   4172 C  CD2  . TYR   B 1 17  ? 37.409 -25.738 -17.573 1.00 22.59 ?  17  TYR   B CD2  1 
ATOM   4173 C  CE1  . TYR   B 1 17  ? 36.247 -23.385 -16.715 1.00 23.44 ?  17  TYR   B CE1  1 
ATOM   4174 C  CE2  . TYR   B 1 17  ? 36.564 -25.043 -18.414 1.00 24.14 ?  17  TYR   B CE2  1 
ATOM   4175 C  CZ   . TYR   B 1 17  ? 35.985 -23.869 -17.980 1.00 24.67 ?  17  TYR   B CZ   1 
ATOM   4176 O  OH   . TYR   B 1 17  ? 35.146 -23.175 -18.818 1.00 26.19 ?  17  TYR   B OH   1 
ATOM   4177 H  H    . TYR   B 1 17  ? 37.368 -25.658 -13.067 1.00 17.47 ?  17  TYR   B H    1 
ATOM   4178 H  HA   . TYR   B 1 17  ? 37.448 -27.687 -14.883 1.00 17.67 ?  17  TYR   B HA   1 
ATOM   4179 H  HB2  . TYR   B 1 17  ? 39.142 -25.405 -14.891 1.00 20.78 ?  17  TYR   B HB2  1 
ATOM   4180 H  HB3  . TYR   B 1 17  ? 39.188 -26.579 -15.953 1.00 20.78 ?  17  TYR   B HB3  1 
ATOM   4181 H  HD1  . TYR   B 1 17  ? 37.272 -23.765 -15.029 1.00 26.17 ?  17  TYR   B HD1  1 
ATOM   4182 H  HD2  . TYR   B 1 17  ? 37.791 -26.531 -17.869 1.00 27.07 ?  17  TYR   B HD2  1 
ATOM   4183 H  HE1  . TYR   B 1 17  ? 35.855 -22.590 -16.428 1.00 28.10 ?  17  TYR   B HE1  1 
ATOM   4184 H  HE2  . TYR   B 1 17  ? 36.381 -25.366 -19.269 1.00 28.94 ?  17  TYR   B HE2  1 
ATOM   4185 H  HH   . TYR   B 1 17  ? 35.068 -23.573 -19.555 1.00 31.40 ?  17  TYR   B HH   1 
ATOM   4186 N  N    . ILE   B 1 18  ? 39.583 -28.689 -13.920 1.00 14.10 ?  18  ILE   B N    1 
ATOM   4187 C  CA   . ILE   B 1 18  ? 40.512 -29.416 -13.059 1.00 14.04 ?  18  ILE   B CA   1 
ATOM   4188 C  C    . ILE   B 1 18  ? 41.679 -29.962 -13.875 1.00 14.29 ?  18  ILE   B C    1 
ATOM   4189 O  O    . ILE   B 1 18  ? 41.525 -30.356 -15.035 1.00 15.68 ?  18  ILE   B O    1 
ATOM   4190 C  CB   . ILE   B 1 18  ? 39.764 -30.520 -12.261 1.00 14.72 ?  18  ILE   B CB   1 
ATOM   4191 C  CG1  . ILE   B 1 18  ? 40.624 -31.057 -11.114 1.00 14.93 ?  18  ILE   B CG1  1 
ATOM   4192 C  CG2  . ILE   B 1 18  ? 39.271 -31.641 -13.184 1.00 14.88 ?  18  ILE   B CG2  1 
ATOM   4193 C  CD1  . ILE   B 1 18  ? 39.811 -31.857 -10.099 1.00 16.23 ?  18  ILE   B CD1  1 
ATOM   4194 H  H    . ILE   B 1 18  ? 39.483 -29.033 -14.704 1.00 16.89 ?  18  ILE   B H    1 
ATOM   4195 H  HA   . ILE   B 1 18  ? 40.876 -28.796 -12.408 1.00 16.82 ?  18  ILE   B HA   1 
ATOM   4196 H  HB   . ILE   B 1 18  ? 38.979 -30.115 -11.862 1.00 17.63 ?  18  ILE   B HB   1 
ATOM   4197 H  HG12 . ILE   B 1 18  ? 41.309 -31.637 -11.473 1.00 17.89 ?  18  ILE   B HG12 1 
ATOM   4198 H  HG13 . ILE   B 1 18  ? 41.028 -30.308 -10.647 1.00 17.89 ?  18  ILE   B HG13 1 
ATOM   4199 H  HG21 . ILE   B 1 18  ? 38.685 -32.228 -12.681 1.00 17.83 ?  18  ILE   B HG21 1 
ATOM   4200 H  HG22 . ILE   B 1 18  ? 38.784 -31.243 -13.922 1.00 17.83 ?  18  ILE   B HG22 1 
ATOM   4201 H  HG23 . ILE   B 1 18  ? 40.034 -32.136 -13.515 1.00 17.83 ?  18  ILE   B HG23 1 
ATOM   4202 H  HD11 . ILE   B 1 18  ? 40.392 -32.129 -9.371  1.00 19.44 ?  18  ILE   B HD11 1 
ATOM   4203 H  HD12 . ILE   B 1 18  ? 39.092 -31.301 -9.756  1.00 19.44 ?  18  ILE   B HD12 1 
ATOM   4204 H  HD13 . ILE   B 1 18  ? 39.440 -32.641 -10.535 1.00 19.44 ?  18  ILE   B HD13 1 
ATOM   4205 N  N    . LYS   B 1 19  ? 42.856 -29.999 -13.247 1.00 14.75 ?  19  LYS   B N    1 
ATOM   4206 C  CA   . LYS   B 1 19  ? 44.069 -30.470 -13.899 1.00 15.36 ?  19  LYS   B CA   1 
ATOM   4207 C  C    . LYS   B 1 19  ? 44.959 -31.155 -12.873 1.00 15.25 ?  19  LYS   B C    1 
ATOM   4208 O  O    . LYS   B 1 19  ? 45.041 -30.722 -11.723 1.00 14.95 ?  19  LYS   B O    1 
ATOM   4209 C  CB   . LYS   B 1 19  ? 44.844 -29.301 -14.523 1.00 16.99 ?  19  LYS   B CB   1 
ATOM   4210 C  CG   . LYS   B 1 19  ? 46.031 -29.709 -15.383 1.00 18.95 ?  19  LYS   B CG   1 
ATOM   4211 C  CD   . LYS   B 1 19  ? 46.788 -28.478 -15.864 1.00 20.59 ?  19  LYS   B CD   1 
ATOM   4212 C  CE   . LYS   B 1 19  ? 47.903 -28.838 -16.826 1.00 22.48 ?  19  LYS   B CE   1 
ATOM   4213 N  NZ   . LYS   B 1 19  ? 48.660 -27.641 -17.278 1.00 23.60 ?  19  LYS   B NZ   1 
ATOM   4214 H  H    . LYS   B 1 19  ? 42.968 -29.753 -12.426 1.00 17.67 ?  19  LYS   B H    1 
ATOM   4215 H  HA   . LYS   B 1 19  ? 43.838 -31.104 -14.593 1.00 18.41 ?  19  LYS   B HA   1 
ATOM   4216 H  HB2  . LYS   B 1 19  ? 44.235 -28.796 -15.084 1.00 20.36 ?  19  LYS   B HB2  1 
ATOM   4217 H  HB3  . LYS   B 1 19  ? 45.172 -28.730 -13.806 1.00 20.36 ?  19  LYS   B HB3  1 
ATOM   4218 H  HG2  . LYS   B 1 19  ? 46.632 -30.260 -14.860 1.00 22.71 ?  19  LYS   B HG2  1 
ATOM   4219 H  HG3  . LYS   B 1 19  ? 45.708 -30.197 -16.157 1.00 22.71 ?  19  LYS   B HG3  1 
ATOM   4220 H  HD2  . LYS   B 1 19  ? 46.172 -27.882 -16.318 1.00 24.68 ?  19  LYS   B HD2  1 
ATOM   4221 H  HD3  . LYS   B 1 19  ? 47.181 -28.028 -15.097 1.00 24.68 ?  19  LYS   B HD3  1 
ATOM   4222 H  HE2  . LYS   B 1 19  ? 48.520 -29.441 -16.383 1.00 26.94 ?  19  LYS   B HE2  1 
ATOM   4223 H  HE3  . LYS   B 1 19  ? 47.518 -29.269 -17.606 1.00 26.94 ?  19  LYS   B HE3  1 
ATOM   4224 H  HZ1  . LYS   B 1 19  ? 49.279 -27.880 -17.872 1.00 28.29 ?  19  LYS   B HZ1  1 
ATOM   4225 H  HZ2  . LYS   B 1 19  ? 48.107 -27.056 -17.659 1.00 28.29 ?  19  LYS   B HZ2  1 
ATOM   4226 H  HZ3  . LYS   B 1 19  ? 49.059 -27.253 -16.585 1.00 28.29 ?  19  LYS   B HZ3  1 
ATOM   4227 N  N    . ASN   B 1 20  ? 45.647 -32.207 -13.305 1.00 16.56 ?  20  ASN   B N    1 
ATOM   4228 C  CA   . ASN   B 1 20  ? 46.679 -32.837 -12.486 1.00 17.63 ?  20  ASN   B CA   1 
ATOM   4229 C  C    . ASN   B 1 20  ? 47.953 -32.021 -12.677 1.00 17.98 ?  20  ASN   B C    1 
ATOM   4230 O  O    . ASN   B 1 20  ? 48.605 -32.107 -13.723 1.00 19.87 ?  20  ASN   B O    1 
ATOM   4231 C  CB   . ASN   B 1 20  ? 46.847 -34.293 -12.914 1.00 19.09 ?  20  ASN   B CB   1 
ATOM   4232 C  CG   . ASN   B 1 20  ? 48.025 -34.987 -12.252 1.00 20.81 ?  20  ASN   B CG   1 
ATOM   4233 O  OD1  . ASN   B 1 20  ? 48.695 -35.817 -12.875 1.00 23.45 ?  20  ASN   B OD1  1 
ATOM   4234 N  ND2  . ASN   B 1 20  ? 48.271 -34.679 -10.990 1.00 20.26 ?  20  ASN   B ND2  1 
ATOM   4235 H  H    . ASN   B 1 20  ? 45.534 -32.574 -14.074 1.00 19.84 ?  20  ASN   B H    1 
ATOM   4236 H  HA   . ASN   B 1 20  ? 46.406 -32.809 -11.552 1.00 21.12 ?  20  ASN   B HA   1 
ATOM   4237 H  HB2  . ASN   B 1 20  ? 46.040 -34.782 -12.678 1.00 22.87 ?  20  ASN   B HB2  1 
ATOM   4238 H  HB3  . ASN   B 1 20  ? 46.978 -34.319 -13.872 1.00 22.87 ?  20  ASN   B HB3  1 
ATOM   4239 H  HD21 . ASN   B 1 20  ? 48.931 -35.043 -10.581 1.00 24.29 ?  20  ASN   B HD21 1 
ATOM   4240 H  HD22 . ASN   B 1 20  ? 47.777 -34.102 -10.578 1.00 24.29 ?  20  ASN   B HD22 1 
ATOM   4241 N  N    . ALA   B 1 21  ? 48.304 -31.209 -11.676 1.00 17.70 ?  21  ALA   B N    1 
ATOM   4242 C  CA   . ALA   B 1 21  ? 49.414 -30.283 -11.830 1.00 18.59 ?  21  ALA   B CA   1 
ATOM   4243 C  C    . ALA   B 1 21  ? 49.874 -29.788 -10.467 1.00 17.52 ?  21  ALA   B C    1 
ATOM   4244 O  O    . ALA   B 1 21  ? 49.131 -29.823 -9.481  1.00 17.22 ?  21  ALA   B O    1 
ATOM   4245 C  CB   . ALA   B 1 21  ? 49.022 -29.103 -12.720 1.00 20.02 ?  21  ALA   B CB   1 
ATOM   4246 H  H    . ALA   B 1 21  ? 47.912 -31.181 -10.904 1.00 21.21 ?  21  ALA   B H    1 
ATOM   4247 H  HA   . ALA   B 1 21  ? 50.152 -30.752 -12.247 1.00 22.28 ?  21  ALA   B HA   1 
ATOM   4248 H  HB1  . ALA   B 1 21  ? 49.807 -28.558 -12.864 1.00 24.00 ?  21  ALA   B HB1  1 
ATOM   4249 H  HB2  . ALA   B 1 21  ? 48.694 -29.447 -13.564 1.00 24.00 ?  21  ALA   B HB2  1 
ATOM   4250 H  HB3  . ALA   B 1 21  ? 48.330 -28.591 -12.277 1.00 24.00 ?  21  ALA   B HB3  1 
ATOM   4251 N  N    . ASP   B 1 22  ? 51.131 -29.343 -10.445 1.00 16.64 ?  22  ASP   B N    1 
ATOM   4252 C  CA   . ASP   B 1 22  ? 51.741 -28.651 -9.315  1.00 15.89 ?  22  ASP   B CA   1 
ATOM   4253 C  C    . ASP   B 1 22  ? 51.333 -27.182 -9.394  1.00 14.92 ?  22  ASP   B C    1 
ATOM   4254 O  O    . ASP   B 1 22  ? 51.641 -26.507 -10.380 1.00 14.93 ?  22  ASP   B O    1 
ATOM   4255 C  CB   . ASP   B 1 22  ? 53.259 -28.821 -9.468  1.00 17.58 ?  22  ASP   B CB   1 
ATOM   4256 C  CG   . ASP   B 1 22  ? 54.082 -28.064 -8.434  1.00 19.45 ?  22  ASP   B CG   1 
ATOM   4257 O  OD1  . ASP   B 1 22  ? 53.711 -26.951 -8.025  1.00 19.77 ?  22  ASP   B OD1  1 
ATOM   4258 O  OD2  . ASP   B 1 22  ? 55.156 -28.580 -8.057  1.00 21.47 -1 22  ASP   B OD2  1 
ATOM   4259 H  H    . ASP   B 1 22  ? 51.672 -29.433 -11.111 1.00 19.94 ?  22  ASP   B H    1 
ATOM   4260 H  HA   . ASP   B 1 22  ? 51.446 -29.038 -8.475  1.00 19.04 ?  22  ASP   B HA   1 
ATOM   4261 H  HB2  . ASP   B 1 22  ? 53.481 -29.759 -9.387  1.00 21.06 ?  22  ASP   B HB2  1 
ATOM   4262 H  HB3  . ASP   B 1 22  ? 53.522 -28.491 -10.340 1.00 21.06 ?  22  ASP   B HB3  1 
ATOM   4263 N  N    . ILE   B 1 23  ? 50.624 -26.690 -8.370  1.00 14.03 ?  23  ILE   B N    1 
ATOM   4264 C  CA   . ILE   B 1 23  ? 50.033 -25.348 -8.438  1.00 13.05 ?  23  ILE   B CA   1 
ATOM   4265 C  C    . ILE   B 1 23  ? 51.089 -24.259 -8.582  1.00 12.91 ?  23  ILE   B C    1 
ATOM   4266 O  O    . ILE   B 1 23  ? 50.824 -23.217 -9.190  1.00 12.57 ?  23  ILE   B O    1 
ATOM   4267 C  CB   . ILE   B 1 23  ? 49.095 -25.098 -7.242  1.00 13.89 ?  23  ILE   B CB   1 
ATOM   4268 C  CG1  . ILE   B 1 23  ? 48.266 -23.831 -7.460  1.00 14.33 ?  23  ILE   B CG1  1 
ATOM   4269 C  CG2  . ILE   B 1 23  ? 49.865 -25.035 -5.940  1.00 14.66 ?  23  ILE   B CG2  1 
ATOM   4270 C  CD1  . ILE   B 1 23  ? 47.137 -23.666 -6.458  1.00 15.13 ?  23  ILE   B CD1  1 
ATOM   4271 H  H    . ILE   B 1 23  ? 50.476 -27.110 -7.635  1.00 16.80 ?  23  ILE   B H    1 
ATOM   4272 H  HA   . ILE   B 1 23  ? 49.487 -25.309 -9.236  1.00 15.62 ?  23  ILE   B HA   1 
ATOM   4273 H  HB   . ILE   B 1 23  ? 48.478 -25.846 -7.189  1.00 16.64 ?  23  ILE   B HB   1 
ATOM   4274 H  HG12 . ILE   B 1 23  ? 48.852 -23.058 -7.381  1.00 17.16 ?  23  ILE   B HG12 1 
ATOM   4275 H  HG13 . ILE   B 1 23  ? 47.879 -23.856 -8.351  1.00 17.16 ?  23  ILE   B HG13 1 
ATOM   4276 H  HG21 . ILE   B 1 23  ? 49.238 -25.037 -5.202  1.00 17.57 ?  23  ILE   B HG21 1 
ATOM   4277 H  HG22 . ILE   B 1 23  ? 50.450 -25.805 -5.883  1.00 17.57 ?  23  ILE   B HG22 1 
ATOM   4278 H  HG23 . ILE   B 1 23  ? 50.391 -24.218 -5.926  1.00 17.57 ?  23  ILE   B HG23 1 
ATOM   4279 H  HD11 . ILE   B 1 23  ? 46.613 -22.889 -6.701  1.00 18.13 ?  23  ILE   B HD11 1 
ATOM   4280 H  HD12 . ILE   B 1 23  ? 46.582 -24.462 -6.484  1.00 18.13 ?  23  ILE   B HD12 1 
ATOM   4281 H  HD13 . ILE   B 1 23  ? 47.514 -23.553 -5.575  1.00 18.13 ?  23  ILE   B HD13 1 
ATOM   4282 N  N    . VAL   B 1 24  ? 52.285 -24.465 -8.026  1.00 13.45 ?  24  VAL   B N    1 
ATOM   4283 C  CA   . VAL   B 1 24  ? 53.358 -23.483 -8.197  1.00 13.84 ?  24  VAL   B CA   1 
ATOM   4284 C  C    . VAL   B 1 24  ? 53.809 -23.439 -9.650  1.00 14.07 ?  24  VAL   B C    1 
ATOM   4285 O  O    . VAL   B 1 24  ? 53.958 -22.364 -10.244 1.00 14.57 ?  24  VAL   B O    1 
ATOM   4286 C  CB   . VAL   B 1 24  ? 54.536 -23.795 -7.252  1.00 14.81 ?  24  VAL   B CB   1 
ATOM   4287 C  CG1  . VAL   B 1 24  ? 55.746 -22.919 -7.589  1.00 15.89 ?  24  VAL   B CG1  1 
ATOM   4288 C  CG2  . VAL   B 1 24  ? 54.124 -23.595 -5.813  1.00 15.67 ?  24  VAL   B CG2  1 
ATOM   4289 H  H    . VAL   B 1 24  ? 52.499 -25.152 -7.553  1.00 16.11 ?  24  VAL   B H    1 
ATOM   4290 H  HA   . VAL   B 1 24  ? 53.021 -22.608 -7.964  1.00 16.58 ?  24  VAL   B HA   1 
ATOM   4291 H  HB   . VAL   B 1 24  ? 54.799 -24.725 -7.357  1.00 17.74 ?  24  VAL   B HB   1 
ATOM   4292 H  HG11 . VAL   B 1 24  ? 56.341 -22.898 -6.824  1.00 19.04 ?  24  VAL   B HG11 1 
ATOM   4293 H  HG12 . VAL   B 1 24  ? 56.203 -23.298 -8.354  1.00 19.04 ?  24  VAL   B HG12 1 
ATOM   4294 H  HG13 . VAL   B 1 24  ? 55.436 -22.023 -7.792  1.00 19.04 ?  24  VAL   B HG13 1 
ATOM   4295 H  HG21 . VAL   B 1 24  ? 54.843 -23.883 -5.232  1.00 18.78 ?  24  VAL   B HG21 1 
ATOM   4296 H  HG22 . VAL   B 1 24  ? 53.939 -22.653 -5.670  1.00 18.78 ?  24  VAL   B HG22 1 
ATOM   4297 H  HG23 . VAL   B 1 24  ? 53.326 -24.119 -5.637  1.00 18.78 ?  24  VAL   B HG23 1 
ATOM   4298 N  N    . GLU   B 1 25  ? 54.065 -24.611 -10.238 1.00 14.97 ?  25  GLU   B N    1 
ATOM   4299 C  CA   . GLU   B 1 25  ? 54.464 -24.643 -11.639 1.00 16.49 ?  25  GLU   B CA   1 
ATOM   4300 C  C    . GLU   B 1 25  ? 53.360 -24.092 -12.526 1.00 15.44 ?  25  GLU   B C    1 
ATOM   4301 O  O    . GLU   B 1 25  ? 53.628 -23.377 -13.499 1.00 16.27 ?  25  GLU   B O    1 
ATOM   4302 C  CB   . GLU   B 1 25  ? 54.849 -26.064 -12.043 1.00 20.40 ?  25  GLU   B CB   1 
ATOM   4303 C  CG   . GLU   B 1 25  ? 56.134 -26.532 -11.381 1.00 26.03 ?  25  GLU   B CG   1 
ATOM   4304 C  CD   . GLU   B 1 25  ? 57.257 -25.509 -11.473 1.00 31.15 ?  25  GLU   B CD   1 
ATOM   4305 O  OE1  . GLU   B 1 25  ? 57.649 -25.152 -12.605 1.00 33.01 ?  25  GLU   B OE1  1 
ATOM   4306 O  OE2  . GLU   B 1 25  ? 57.739 -25.044 -10.413 1.00 32.84 -1 25  GLU   B OE2  1 
ATOM   4307 H  H    . GLU   B 1 25  ? 54.016 -25.383 -9.855  1.00 17.94 ?  25  GLU   B H    1 
ATOM   4308 H  HA   . GLU   B 1 25  ? 55.228 -24.064 -11.759 1.00 19.76 ?  25  GLU   B HA   1 
ATOM   4309 H  HB2  . GLU   B 1 25  ? 54.140 -26.675 -11.779 1.00 24.45 ?  25  GLU   B HB2  1 
ATOM   4310 H  HB3  . GLU   B 1 25  ? 54.973 -26.100 -13.004 1.00 24.45 ?  25  GLU   B HB3  1 
ATOM   4311 H  HG2  . GLU   B 1 25  ? 55.969 -26.686 -10.443 1.00 31.20 ?  25  GLU   B HG2  1 
ATOM   4312 H  HG3  . GLU   B 1 25  ? 56.432 -27.347 -11.813 1.00 31.20 ?  25  GLU   B HG3  1 
ATOM   4313 N  N    . GLU   B 1 26  ? 52.108 -24.410 -12.198 1.00 14.73 ?  26  GLU   B N    1 
ATOM   4314 C  CA   . GLU   B 1 26  ? 50.982 -23.879 -12.957 1.00 14.90 ?  26  GLU   B CA   1 
ATOM   4315 C  C    . GLU   B 1 26  ? 50.934 -22.361 -12.876 1.00 13.77 ?  26  GLU   B C    1 
ATOM   4316 O  O    . GLU   B 1 26  ? 50.733 -21.685 -13.888 1.00 15.38 ?  26  GLU   B O    1 
ATOM   4317 C  CB   . GLU   B 1 26  ? 49.670 -24.464 -12.433 1.00 16.99 ?  26  GLU   B CB   1 
ATOM   4318 C  CG   . GLU   B 1 26  ? 49.227 -25.746 -13.105 1.00 20.69 ?  26  GLU   B CG   1 
ATOM   4319 C  CD   . GLU   B 1 26  ? 48.987 -25.601 -14.605 1.00 22.26 ?  26  GLU   B CD   1 
ATOM   4320 O  OE1  . GLU   B 1 26  ? 48.023 -24.926 -15.031 1.00 22.48 ?  26  GLU   B OE1  1 
ATOM   4321 O  OE2  . GLU   B 1 26  ? 49.767 -26.198 -15.358 1.00 24.39 -1 26  GLU   B OE2  1 
ATOM   4322 H  H    . GLU   B 1 26  ? 51.882 -24.938 -11.552 1.00 17.65 ?  26  GLU   B H    1 
ATOM   4323 H  HA   . GLU   B 1 26  ? 51.078 -24.127 -13.887 1.00 17.85 ?  26  GLU   B HA   1 
ATOM   4324 H  HB2  . GLU   B 1 26  ? 49.768 -24.648 -11.485 1.00 20.36 ?  26  GLU   B HB2  1 
ATOM   4325 H  HB3  . GLU   B 1 26  ? 48.966 -23.806 -12.562 1.00 20.36 ?  26  GLU   B HB3  1 
ATOM   4326 H  HG2  . GLU   B 1 26  ? 49.923 -26.402 -12.989 1.00 24.80 ?  26  GLU   B HG2  1 
ATOM   4327 H  HG3  . GLU   B 1 26  ? 48.403 -26.044 -12.692 1.00 24.80 ?  26  GLU   B HG3  1 
ATOM   4328 N  N    . ALA   B 1 27  ? 51.083 -21.809 -11.669 1.00 13.13 ?  27  ALA   B N    1 
ATOM   4329 C  CA   . ALA   B 1 27  ? 51.043 -20.359 -11.522 1.00 13.61 ?  27  ALA   B CA   1 
ATOM   4330 C  C    . ALA   B 1 27  ? 52.118 -19.695 -12.372 1.00 14.48 ?  27  ALA   B C    1 
ATOM   4331 O  O    . ALA   B 1 27  ? 51.860 -18.691 -13.052 1.00 15.29 ?  27  ALA   B O    1 
ATOM   4332 C  CB   . ALA   B 1 27  ? 51.188 -19.980 -10.048 1.00 13.71 ?  27  ALA   B CB   1 
ATOM   4333 H  H    . ALA   B 1 27  ? 51.194 -22.244 -10.931 1.00 15.72 ?  27  ALA   B H    1 
ATOM   4334 H  HA   . ALA   B 1 27  ? 50.182 -20.033 -11.823 1.00 16.30 ?  27  ALA   B HA   1 
ATOM   4335 H  HB1  . ALA   B 1 27  ? 51.153 -19.012 -9.964  1.00 16.42 ?  27  ALA   B HB1  1 
ATOM   4336 H  HB2  . ALA   B 1 27  ? 50.454 -20.376 -9.546  1.00 16.42 ?  27  ALA   B HB2  1 
ATOM   4337 H  HB3  . ALA   B 1 27  ? 52.032 -20.311 -9.713  1.00 16.42 ?  27  ALA   B HB3  1 
ATOM   4338 N  N    . LYS   B 1 28  ? 53.329 -20.249 -12.362 1.00 15.99 ?  28  LYS   B N    1 
ATOM   4339 C  CA   . LYS   B 1 28  ? 54.405 -19.638 -13.133 1.00 18.27 ?  28  LYS   B CA   1 
ATOM   4340 C  C    . LYS   B 1 28  ? 54.146 -19.722 -14.634 1.00 18.94 ?  28  LYS   B C    1 
ATOM   4341 O  O    . LYS   B 1 28  ? 54.555 -18.825 -15.382 1.00 20.20 ?  28  LYS   B O    1 
ATOM   4342 C  CB   . LYS   B 1 28  ? 55.756 -20.245 -12.742 1.00 21.14 ?  28  LYS   B CB   1 
ATOM   4343 C  CG   . LYS   B 1 28  ? 56.172 -19.897 -11.315 1.00 24.73 ?  28  LYS   B CG   1 
ATOM   4344 C  CD   . LYS   B 1 28  ? 57.597 -20.319 -10.991 1.00 29.74 ?  28  LYS   B CD   1 
ATOM   4345 C  CE   . LYS   B 1 28  ? 57.684 -21.794 -10.680 1.00 33.59 ?  28  LYS   B CE   1 
ATOM   4346 N  NZ   . LYS   B 1 28  ? 59.037 -22.166 -10.178 1.00 35.47 ?  28  LYS   B NZ   1 
ATOM   4347 H  H    . LYS   B 1 28  ? 53.550 -20.955 -11.921 1.00 19.16 ?  28  LYS   B H    1 
ATOM   4348 H  HA   . LYS   B 1 28  ? 54.445 -18.696 -12.903 1.00 21.90 ?  28  LYS   B HA   1 
ATOM   4349 H  HB2  . LYS   B 1 28  ? 55.706 -21.210 -12.808 1.00 25.34 ?  28  LYS   B HB2  1 
ATOM   4350 H  HB3  . LYS   B 1 28  ? 56.442 -19.906 -13.340 1.00 25.34 ?  28  LYS   B HB3  1 
ATOM   4351 H  HG2  . LYS   B 1 28  ? 56.107 -18.936 -11.195 1.00 29.65 ?  28  LYS   B HG2  1 
ATOM   4352 H  HG3  . LYS   B 1 28  ? 55.577 -20.348 -10.697 1.00 29.65 ?  28  LYS   B HG3  1 
ATOM   4353 H  HD2  . LYS   B 1 28  ? 58.165 -20.133 -11.756 1.00 35.66 ?  28  LYS   B HD2  1 
ATOM   4354 H  HD3  . LYS   B 1 28  ? 57.906 -19.823 -10.216 1.00 35.66 ?  28  LYS   B HD3  1 
ATOM   4355 H  HE2  . LYS   B 1 28  ? 57.033 -22.015 -9.995  1.00 40.28 ?  28  LYS   B HE2  1 
ATOM   4356 H  HE3  . LYS   B 1 28  ? 57.507 -22.303 -11.487 1.00 40.28 ?  28  LYS   B HE3  1 
ATOM   4357 H  HZ1  . LYS   B 1 28  ? 59.067 -23.037 -10.001 1.00 42.53 ?  28  LYS   B HZ1  1 
ATOM   4358 H  HZ2  . LYS   B 1 28  ? 59.652 -21.973 -10.792 1.00 42.53 ?  28  LYS   B HZ2  1 
ATOM   4359 H  HZ3  . LYS   B 1 28  ? 59.220 -21.712 -9.434  1.00 42.53 ?  28  LYS   B HZ3  1 
ATOM   4360 N  N    . LYS   B 1 29  ? 53.445 -20.763 -15.088 1.00 20.00 ?  29  LYS   B N    1 
ATOM   4361 C  CA   . LYS   B 1 29  ? 53.159 -20.902 -16.513 1.00 22.75 ?  29  LYS   B CA   1 
ATOM   4362 C  C    . LYS   B 1 29  ? 51.916 -20.122 -16.937 1.00 21.64 ?  29  LYS   B C    1 
ATOM   4363 O  O    . LYS   B 1 29  ? 51.908 -19.500 -18.005 1.00 23.12 ?  29  LYS   B O    1 
ATOM   4364 C  CB   . LYS   B 1 29  ? 52.999 -22.379 -16.871 1.00 27.27 ?  29  LYS   B CB   1 
ATOM   4365 C  CG   . LYS   B 1 29  ? 52.943 -22.648 -18.367 1.00 31.51 ?  29  LYS   B CG   1 
ATOM   4366 C  CD   . LYS   B 1 29  ? 53.201 -24.116 -18.683 1.00 34.88 ?  29  LYS   B CD   1 
ATOM   4367 C  CE   . LYS   B 1 29  ? 52.083 -25.009 -18.171 1.00 37.22 ?  29  LYS   B CE   1 
ATOM   4368 N  NZ   . LYS   B 1 29  ? 52.337 -26.447 -18.472 1.00 38.39 ?  29  LYS   B NZ   1 
ATOM   4369 H  H    . LYS   B 1 29  ? 53.134 -21.395 -14.591 1.00 23.96 ?  29  LYS   B H    1 
ATOM   4370 H  HA   . LYS   B 1 29  ? 53.908 -20.552 -17.012 1.00 27.27 ?  29  LYS   B HA   1 
ATOM   4371 H  HB2  . LYS   B 1 29  ? 53.755 -22.869 -16.511 1.00 32.70 ?  29  LYS   B HB2  1 
ATOM   4372 H  HB3  . LYS   B 1 29  ? 52.176 -22.709 -16.480 1.00 32.70 ?  29  LYS   B HB3  1 
ATOM   4373 H  HG2  . LYS   B 1 29  ? 52.062 -22.415 -18.700 1.00 37.78 ?  29  LYS   B HG2  1 
ATOM   4374 H  HG3  . LYS   B 1 29  ? 53.621 -22.116 -18.814 1.00 37.78 ?  29  LYS   B HG3  1 
ATOM   4375 H  HD2  . LYS   B 1 29  ? 53.264 -24.231 -19.644 1.00 41.83 ?  29  LYS   B HD2  1 
ATOM   4376 H  HD3  . LYS   B 1 29  ? 54.029 -24.394 -18.259 1.00 41.83 ?  29  LYS   B HD3  1 
ATOM   4377 H  HE2  . LYS   B 1 29  ? 52.010 -24.911 -17.209 1.00 44.63 ?  29  LYS   B HE2  1 
ATOM   4378 H  HE3  . LYS   B 1 29  ? 51.250 -24.753 -18.598 1.00 44.63 ?  29  LYS   B HE3  1 
ATOM   4379 H  HZ1  . LYS   B 1 29  ? 51.668 -26.946 -18.162 1.00 46.04 ?  29  LYS   B HZ1  1 
ATOM   4380 H  HZ2  . LYS   B 1 29  ? 52.403 -26.567 -19.351 1.00 46.04 ?  29  LYS   B HZ2  1 
ATOM   4381 H  HZ3  . LYS   B 1 29  ? 53.095 -26.710 -18.087 1.00 46.04 ?  29  LYS   B HZ3  1 
ATOM   4382 N  N    . VAL   B 1 30  ? 50.856 -20.164 -16.125 1.00 19.99 ?  30  VAL   B N    1 
ATOM   4383 C  CA   . VAL   B 1 30  ? 49.565 -19.577 -16.496 1.00 20.12 ?  30  VAL   B CA   1 
ATOM   4384 C  C    . VAL   B 1 30  ? 49.563 -18.062 -16.344 1.00 19.49 ?  30  VAL   B C    1 
ATOM   4385 O  O    . VAL   B 1 30  ? 48.819 -17.356 -17.045 1.00 20.53 ?  30  VAL   B O    1 
ATOM   4386 C  CB   . VAL   B 1 30  ? 48.461 -20.201 -15.617 1.00 20.85 ?  30  VAL   B CB   1 
ATOM   4387 C  CG1  . VAL   B 1 30  ? 47.181 -19.381 -15.671 1.00 20.95 ?  30  VAL   B CG1  1 
ATOM   4388 C  CG2  . VAL   B 1 30  ? 48.206 -21.645 -16.023 1.00 21.70 ?  30  VAL   B CG2  1 
ATOM   4389 H  H    . VAL   B 1 30  ? 50.850 -20.549 -15.346 1.00 23.96 ?  30  VAL   B H    1 
ATOM   4390 H  HA   . VAL   B 1 30  ? 49.368 -19.804 -17.418 1.00 24.11 ?  30  VAL   B HA   1 
ATOM   4391 H  HB   . VAL   B 1 30  ? 48.761 -20.216 -14.694 1.00 24.99 ?  30  VAL   B HB   1 
ATOM   4392 H  HG11 . VAL   B 1 30  ? 46.437 -19.956 -15.424 1.00 25.11 ?  30  VAL   B HG11 1 
ATOM   4393 H  HG12 . VAL   B 1 30  ? 47.245 -18.647 -15.043 1.00 25.11 ?  30  VAL   B HG12 1 
ATOM   4394 H  HG13 . VAL   B 1 30  ? 47.048 -19.055 -16.569 1.00 25.11 ?  30  VAL   B HG13 1 
ATOM   4395 H  HG21 . VAL   B 1 30  ? 47.517 -22.023 -15.447 1.00 26.01 ?  30  VAL   B HG21 1 
ATOM   4396 H  HG22 . VAL   B 1 30  ? 47.903 -21.666 -16.946 1.00 26.01 ?  30  VAL   B HG22 1 
ATOM   4397 H  HG23 . VAL   B 1 30  ? 49.024 -22.153 -15.930 1.00 26.01 ?  30  VAL   B HG23 1 
ATOM   4398 N  N    . LYS   B 1 31  ? 50.342 -17.557 -15.403 1.00 19.21 ?  31  LYS   B N    1 
ATOM   4399 C  CA   . LYS   B 1 31  ? 50.365 -16.146 -15.041 1.00 19.60 ?  31  LYS   B CA   1 
ATOM   4400 C  C    . LYS   B 1 31  ? 48.961 -15.673 -14.659 1.00 17.11 ?  31  LYS   B C    1 
ATOM   4401 O  O    . LYS   B 1 31  ? 48.423 -14.744 -15.275 1.00 18.27 ?  31  LYS   B O    1 
ATOM   4402 C  CB   . LYS   B 1 31  ? 50.996 -15.329 -16.173 1.00 22.87 ?  31  LYS   B CB   1 
ATOM   4403 C  CG   . LYS   B 1 31  ? 52.410 -15.806 -16.523 1.00 26.22 ?  31  LYS   B CG   1 
ATOM   4404 C  CD   . LYS   B 1 31  ? 52.992 -15.047 -17.703 1.00 29.62 ?  31  LYS   B CD   1 
ATOM   4405 C  CE   . LYS   B 1 31  ? 54.469 -15.341 -17.886 1.00 32.29 ?  31  LYS   B CE   1 
ATOM   4406 N  NZ   . LYS   B 1 31  ? 55.225 -15.003 -16.651 1.00 33.25 ?  31  LYS   B NZ   1 
ATOM   4407 H  H    . LYS   B 1 31  ? 50.890 -18.050 -14.957 1.00 23.02 ?  31  LYS   B H    1 
ATOM   4408 H  HA   . LYS   B 1 31  ? 50.918 -16.058 -14.261 1.00 23.49 ?  31  LYS   B HA   1 
ATOM   4409 H  HB2  . LYS   B 1 31  ? 50.449 -15.407 -16.972 1.00 27.41 ?  31  LYS   B HB2  1 
ATOM   4410 H  HB3  . LYS   B 1 31  ? 51.052 -14.405 -15.895 1.00 27.41 ?  31  LYS   B HB3  1 
ATOM   4411 H  HG2  . LYS   B 1 31  ? 52.978 -15.673 -15.748 1.00 31.44 ?  31  LYS   B HG2  1 
ATOM   4412 H  HG3  . LYS   B 1 31  ? 52.377 -16.751 -16.751 1.00 31.44 ?  31  LYS   B HG3  1 
ATOM   4413 H  HD2  . LYS   B 1 31  ? 52.523 -15.314 -18.508 1.00 35.52 ?  31  LYS   B HD2  1 
ATOM   4414 H  HD3  . LYS   B 1 31  ? 52.883 -14.098 -17.548 1.00 35.52 ?  31  LYS   B HD3  1 
ATOM   4415 H  HE2  . LYS   B 1 31  ? 54.596 -16.285 -18.074 1.00 38.72 ?  31  LYS   B HE2  1 
ATOM   4416 H  HE3  . LYS   B 1 31  ? 54.818 -14.802 -18.615 1.00 38.72 ?  31  LYS   B HE3  1 
ATOM   4417 H  HZ1  . LYS   B 1 31  ? 56.099 -15.022 -16.813 1.00 39.87 ?  31  LYS   B HZ1  1 
ATOM   4418 H  HZ2  . LYS   B 1 31  ? 55.000 -14.188 -16.372 1.00 39.87 ?  31  LYS   B HZ2  1 
ATOM   4419 H  HZ3  . LYS   B 1 31  ? 55.036 -15.590 -16.009 1.00 39.87 ?  31  LYS   B HZ3  1 
ATOM   4420 N  N    . PRO   B 1 32  ? 48.348 -16.283 -13.637 1.00 14.67 ?  32  PRO   B N    1 
ATOM   4421 C  CA   . PRO   B 1 32  ? 46.970 -15.929 -13.281 1.00 13.59 ?  32  PRO   B CA   1 
ATOM   4422 C  C    . PRO   B 1 32  ? 46.887 -14.580 -12.583 1.00 13.81 ?  32  PRO   B C    1 
ATOM   4423 O  O    . PRO   B 1 32  ? 47.806 -14.156 -11.877 1.00 15.09 ?  32  PRO   B O    1 
ATOM   4424 C  CB   . PRO   B 1 32  ? 46.573 -17.044 -12.311 1.00 13.78 ?  32  PRO   B CB   1 
ATOM   4425 C  CG   . PRO   B 1 32  ? 47.881 -17.389 -11.636 1.00 14.41 ?  32  PRO   B CG   1 
ATOM   4426 C  CD   . PRO   B 1 32  ? 48.921 -17.276 -12.707 1.00 14.62 ?  32  PRO   B CD   1 
ATOM   4427 H  HA   . PRO   B 1 32  ? 46.391 -15.944 -14.063 1.00 16.28 ?  32  PRO   B HA   1 
ATOM   4428 H  HB2  . PRO   B 1 32  ? 45.928 -16.708 -11.669 1.00 16.50 ?  32  PRO   B HB2  1 
ATOM   4429 H  HB3  . PRO   B 1 32  ? 46.222 -17.802 -12.799 1.00 16.50 ?  32  PRO   B HB3  1 
ATOM   4430 H  HG2  . PRO   B 1 32  ? 48.062 -16.753 -10.922 1.00 17.27 ?  32  PRO   B HG2  1 
ATOM   4431 H  HG3  . PRO   B 1 32  ? 47.847 -18.291 -11.289 1.00 17.27 ?  32  PRO   B HG3  1 
ATOM   4432 H  HD2  . PRO   B 1 32  ? 49.753 -16.947 -12.336 1.00 17.52 ?  32  PRO   B HD2  1 
ATOM   4433 H  HD3  . PRO   B 1 32  ? 49.036 -18.127 -13.152 1.00 17.52 ?  32  PRO   B HD3  1 
ATOM   4434 N  N    . THR   B 1 33  ? 45.736 -13.926 -12.753 1.00 13.14 ?  33  THR   B N    1 
ATOM   4435 C  CA   . THR   B 1 33  ? 45.442 -12.744 -11.947 1.00 13.44 ?  33  THR   B CA   1 
ATOM   4436 C  C    . THR   B 1 33  ? 45.396 -13.097 -10.467 1.00 12.97 ?  33  THR   B C    1 
ATOM   4437 O  O    . THR   B 1 33  ? 45.869 -12.320 -9.625  1.00 14.12 ?  33  THR   B O    1 
ATOM   4438 C  CB   . THR   B 1 33  ? 44.119 -12.120 -12.398 1.00 14.12 ?  33  THR   B CB   1 
ATOM   4439 O  OG1  . THR   B 1 33  ? 44.169 -11.853 -13.802 1.00 14.05 ?  33  THR   B OG1  1 
ATOM   4440 C  CG2  . THR   B 1 33  ? 43.830 -10.836 -11.634 1.00 15.71 ?  33  THR   B CG2  1 
ATOM   4441 H  H    . THR   B 1 33  ? 45.122 -14.141 -13.322 1.00 15.74 ?  33  THR   B H    1 
ATOM   4442 H  HA   . THR   B 1 33  ? 46.141 -12.087 -12.082 1.00 16.10 ?  33  THR   B HA   1 
ATOM   4443 H  HB   . THR   B 1 33  ? 43.394 -12.747 -12.230 1.00 16.92 ?  33  THR   B HB   1 
ATOM   4444 H  HG1  . THR   B 1 33  ? 43.451 -11.488 -14.056 1.00 16.83 ?  33  THR   B HG1  1 
ATOM   4445 H  HG21 . THR   B 1 33  ? 43.076 -10.377 -12.029 1.00 18.82 ?  33  THR   B HG21 1 
ATOM   4446 H  HG22 . THR   B 1 33  ? 43.625 -11.043 -10.708 1.00 18.82 ?  33  THR   B HG22 1 
ATOM   4447 H  HG23 . THR   B 1 33  ? 44.607 -10.256 -11.663 1.00 18.82 ?  33  THR   B HG23 1 
ATOM   4448 N  N    . VAL   B 1 34  ? 44.846 -14.268 -10.130 1.00 12.48 ?  34  VAL   B N    1 
ATOM   4449 C  CA   . VAL   B 1 34  ? 44.645 -14.669 -8.740  1.00 12.09 ?  34  VAL   B CA   1 
ATOM   4450 C  C    . VAL   B 1 34  ? 45.075 -16.119 -8.577  1.00 11.13 ?  34  VAL   B C    1 
ATOM   4451 O  O    . VAL   B 1 34  ? 44.551 -17.007 -9.261  1.00 11.61 ?  34  VAL   B O    1 
ATOM   4452 C  CB   . VAL   B 1 34  ? 43.175 -14.526 -8.297  1.00 13.06 ?  34  VAL   B CB   1 
ATOM   4453 C  CG1  . VAL   B 1 34  ? 43.012 -14.977 -6.850  1.00 13.58 ?  34  VAL   B CG1  1 
ATOM   4454 C  CG2  . VAL   B 1 34  ? 42.672 -13.098 -8.495  1.00 14.26 ?  34  VAL   B CG2  1 
ATOM   4455 H  H    . VAL   B 1 34  ? 44.580 -14.860 -10.698 1.00 14.95 ?  34  VAL   B H    1 
ATOM   4456 H  HA   . VAL   B 1 34  ? 45.201 -14.116 -8.161  1.00 14.48 ?  34  VAL   B HA   1 
ATOM   4457 H  HB   . VAL   B 1 34  ? 42.634 -15.105 -8.851  1.00 15.64 ?  34  VAL   B HB   1 
ATOM   4458 H  HG11 . VAL   B 1 34  ? 42.154 -14.667 -6.518  1.00 16.26 ?  34  VAL   B HG11 1 
ATOM   4459 H  HG12 . VAL   B 1 34  ? 43.044 -15.948 -6.812  1.00 16.26 ?  34  VAL   B HG12 1 
ATOM   4460 H  HG13 . VAL   B 1 34  ? 43.727 -14.601 -6.314  1.00 16.26 ?  34  VAL   B HG13 1 
ATOM   4461 H  HG21 . VAL   B 1 34  ? 41.755 -13.041 -8.184  1.00 17.08 ?  34  VAL   B HG21 1 
ATOM   4462 H  HG22 . VAL   B 1 34  ? 43.232 -12.489 -7.992  1.00 17.08 ?  34  VAL   B HG22 1 
ATOM   4463 H  HG23 . VAL   B 1 34  ? 42.711 -12.877 -9.442  1.00 17.08 ?  34  VAL   B HG23 1 
ATOM   4464 N  N    . VAL   B 1 35  ? 45.985 -16.367 -7.637  1.00 10.68 ?  35  VAL   B N    1 
ATOM   4465 C  CA   . VAL   B 1 35  ? 46.224 -17.709 -7.118  1.00 10.34 ?  35  VAL   B CA   1 
ATOM   4466 C  C    . VAL   B 1 35  ? 45.686 -17.764 -5.697  1.00 10.27 ?  35  VAL   B C    1 
ATOM   4467 O  O    . VAL   B 1 35  ? 45.904 -16.837 -4.908  1.00 10.62 ?  35  VAL   B O    1 
ATOM   4468 C  CB   . VAL   B 1 35  ? 47.707 -18.128 -7.203  1.00 11.31 ?  35  VAL   B CB   1 
ATOM   4469 C  CG1  . VAL   B 1 35  ? 48.606 -17.286 -6.286  1.00 12.27 ?  35  VAL   B CG1  1 
ATOM   4470 C  CG2  . VAL   B 1 35  ? 47.852 -19.622 -6.891  1.00 11.59 ?  35  VAL   B CG2  1 
ATOM   4471 H  H    . VAL   B 1 35  ? 46.490 -15.765 -7.280  1.00 12.79 ?  35  VAL   B H    1 
ATOM   4472 H  HA   . VAL   B 1 35  ? 45.708 -18.339 -7.644  1.00 12.37 ?  35  VAL   B HA   1 
ATOM   4473 H  HB   . VAL   B 1 35  ? 48.008 -17.996 -8.118  1.00 13.55 ?  35  VAL   B HB   1 
ATOM   4474 H  HG11 . VAL   B 1 35  ? 49.528 -17.509 -6.468  1.00 14.69 ?  35  VAL   B HG11 1 
ATOM   4475 H  HG12 . VAL   B 1 35  ? 48.440 -16.352 -6.464  1.00 14.69 ?  35  VAL   B HG12 1 
ATOM   4476 H  HG13 . VAL   B 1 35  ? 48.386 -17.496 -5.363  1.00 14.69 ?  35  VAL   B HG13 1 
ATOM   4477 H  HG21 . VAL   B 1 35  ? 48.776 -19.886 -7.000  1.00 13.88 ?  35  VAL   B HG21 1 
ATOM   4478 H  HG22 . VAL   B 1 35  ? 47.565 -19.787 -5.976  1.00 13.88 ?  35  VAL   B HG22 1 
ATOM   4479 H  HG23 . VAL   B 1 35  ? 47.290 -20.136 -7.502  1.00 13.88 ?  35  VAL   B HG23 1 
ATOM   4480 N  N    . VAL   B 1 36  ? 44.960 -18.838 -5.382  1.00 10.10 ?  36  VAL   B N    1 
ATOM   4481 C  CA   . VAL   B 1 36  ? 44.420 -19.042 -4.050  1.00 9.81  ?  36  VAL   B CA   1 
ATOM   4482 C  C    . VAL   B 1 36  ? 45.432 -19.804 -3.203  1.00 9.79  ?  36  VAL   B C    1 
ATOM   4483 O  O    . VAL   B 1 36  ? 45.970 -20.837 -3.626  1.00 10.93 ?  36  VAL   B O    1 
ATOM   4484 C  CB   . VAL   B 1 36  ? 43.084 -19.800 -4.119  1.00 10.32 ?  36  VAL   B CB   1 
ATOM   4485 C  CG1  . VAL   B 1 36  ? 42.593 -20.157 -2.724  1.00 11.13 ?  36  VAL   B CG1  1 
ATOM   4486 C  CG2  . VAL   B 1 36  ? 42.058 -18.974 -4.874  1.00 11.20 ?  36  VAL   B CG2  1 
ATOM   4487 H  H    . VAL   B 1 36  ? 44.781 -19.477 -5.928  1.00 12.09 ?  36  VAL   B H    1 
ATOM   4488 H  HA   . VAL   B 1 36  ? 44.259 -18.182 -3.631  1.00 11.74 ?  36  VAL   B HA   1 
ATOM   4489 H  HB   . VAL   B 1 36  ? 43.218 -20.629 -4.605  1.00 12.36 ?  36  VAL   B HB   1 
ATOM   4490 H  HG11 . VAL   B 1 36  ? 41.651 -20.379 -2.771  1.00 13.32 ?  36  VAL   B HG11 1 
ATOM   4491 H  HG12 . VAL   B 1 36  ? 43.096 -20.913 -2.391  1.00 13.32 ?  36  VAL   B HG12 1 
ATOM   4492 H  HG13 . VAL   B 1 36  ? 42.720 -19.389 -2.142  1.00 13.32 ?  36  VAL   B HG13 1 
ATOM   4493 H  HG21 . VAL   B 1 36  ? 41.214 -19.453 -4.884  1.00 13.40 ?  36  VAL   B HG21 1 
ATOM   4494 H  HG22 . VAL   B 1 36  ? 41.952 -18.121 -4.430  1.00 13.40 ?  36  VAL   B HG22 1 
ATOM   4495 H  HG23 . VAL   B 1 36  ? 42.371 -18.839 -5.783  1.00 13.40 ?  36  VAL   B HG23 1 
ATOM   4496 N  N    . ASN   B 1 37  ? 45.661 -19.309 -1.988  1.00 10.15 ?  37  ASN   B N    1 
ATOM   4497 C  CA   . ASN   B 1 37  ? 46.407 -20.034 -0.973  1.00 10.43 ?  37  ASN   B CA   1 
ATOM   4498 C  C    . ASN   B 1 37  ? 45.459 -20.707 0.012   1.00 10.44 ?  37  ASN   B C    1 
ATOM   4499 O  O    . ASN   B 1 37  ? 44.445 -20.131 0.418   1.00 10.97 ?  37  ASN   B O    1 
ATOM   4500 C  CB   . ASN   B 1 37  ? 47.337 -19.089 -0.218  1.00 10.29 ?  37  ASN   B CB   1 
ATOM   4501 C  CG   . ASN   B 1 37  ? 48.187 -19.810 0.795   1.00 10.81 ?  37  ASN   B CG   1 
ATOM   4502 O  OD1  . ASN   B 1 37  ? 48.521 -20.991 0.618   1.00 11.40 ?  37  ASN   B OD1  1 
ATOM   4503 N  ND2  . ASN   B 1 37  ? 48.547 -19.110 1.870   1.00 10.97 ?  37  ASN   B ND2  1 
ATOM   4504 H  H    . ASN   B 1 37  ? 45.385 -18.535 -1.720  1.00 12.14 ?  37  ASN   B H    1 
ATOM   4505 H  HA   . ASN   B 1 37  ? 46.940 -20.724 -1.394  1.00 12.49 ?  37  ASN   B HA   1 
ATOM   4506 H  HB2  . ASN   B 1 37  ? 47.929 -18.663 -0.852  1.00 12.32 ?  37  ASN   B HB2  1 
ATOM   4507 H  HB3  . ASN   B 1 37  ? 46.809 -18.429 0.251   1.00 12.32 ?  37  ASN   B HB3  1 
ATOM   4508 H  HD21 . ASN   B 1 37  ? 49.039 -19.477 2.478   1.00 13.13 ?  37  ASN   B HD21 1 
ATOM   4509 H  HD22 . ASN   B 1 37  ? 48.299 -18.298 1.963   1.00 13.13 ?  37  ASN   B HD22 1 
ATOM   4510 N  N    . ALA   B 1 38  ? 45.802 -21.943 0.384   1.00 10.58 ?  38  ALA   B N    1 
ATOM   4511 C  CA   . ALA   B 1 38  ? 45.154 -22.682 1.466   1.00 11.04 ?  38  ALA   B CA   1 
ATOM   4512 C  C    . ALA   B 1 38  ? 45.742 -22.196 2.789   1.00 10.86 ?  38  ALA   B C    1 
ATOM   4513 O  O    . ALA   B 1 38  ? 46.648 -22.802 3.373   1.00 11.75 ?  38  ALA   B O    1 
ATOM   4514 C  CB   . ALA   B 1 38  ? 45.375 -24.177 1.277   1.00 12.33 ?  38  ALA   B CB   1 
ATOM   4515 H  H    . ALA   B 1 38  ? 46.446 -22.383 0.022   1.00 12.67 ?  38  ALA   B H    1 
ATOM   4516 H  HA   . ALA   B 1 38  ? 44.199 -22.501 1.462   1.00 13.22 ?  38  ALA   B HA   1 
ATOM   4517 H  HB1  . ALA   B 1 38  ? 44.930 -24.656 2.001   1.00 14.76 ?  38  ALA   B HB1  1 
ATOM   4518 H  HB2  . ALA   B 1 38  ? 44.990 -24.448 0.427   1.00 14.76 ?  38  ALA   B HB2  1 
ATOM   4519 H  HB3  . ALA   B 1 38  ? 46.321 -24.365 1.291   1.00 14.76 ?  38  ALA   B HB3  1 
ATOM   4520 N  N    . ALA   B 1 39  ? 45.222 -21.057 3.249   1.00 10.86 ?  39  ALA   B N    1 
ATOM   4521 C  CA   . ALA   B 1 39  ? 45.772 -20.321 4.375   1.00 10.83 ?  39  ALA   B CA   1 
ATOM   4522 C  C    . ALA   B 1 39  ? 45.152 -20.762 5.698   1.00 11.12 ?  39  ALA   B C    1 
ATOM   4523 O  O    . ALA   B 1 39  ? 44.122 -21.434 5.747   1.00 12.13 ?  39  ALA   B O    1 
ATOM   4524 C  CB   . ALA   B 1 39  ? 45.530 -18.822 4.174   1.00 11.65 ?  39  ALA   B CB   1 
ATOM   4525 H  H    . ALA   B 1 39  ? 44.526 -20.686 2.906   1.00 13.01 ?  39  ALA   B H    1 
ATOM   4526 H  HA   . ALA   B 1 39  ? 46.723 -20.473 4.422   1.00 12.97 ?  39  ALA   B HA   1 
ATOM   4527 H  HB1  . ALA   B 1 39  ? 45.899 -18.338 4.929   1.00 13.95 ?  39  ALA   B HB1  1 
ATOM   4528 H  HB2  . ALA   B 1 39  ? 45.971 -18.539 3.355   1.00 13.95 ?  39  ALA   B HB2  1 
ATOM   4529 H  HB3  . ALA   B 1 39  ? 44.577 -18.656 4.108   1.00 13.95 ?  39  ALA   B HB3  1 
ATOM   4530 N  N    . ASN   B 1 40  ? 45.790 -20.338 6.786   1.00 11.70 ?  40  ASN   B N    1 
ATOM   4531 C  CA   . ASN   B 1 40  ? 45.231 -20.389 8.126   1.00 12.49 ?  40  ASN   B CA   1 
ATOM   4532 C  C    . ASN   B 1 40  ? 45.053 -18.962 8.649   1.00 12.29 ?  40  ASN   B C    1 
ATOM   4533 O  O    . ASN   B 1 40  ? 45.459 -17.982 8.017   1.00 12.16 ?  40  ASN   B O    1 
ATOM   4534 C  CB   . ASN   B 1 40  ? 46.081 -21.266 9.061   1.00 13.56 ?  40  ASN   B CB   1 
ATOM   4535 C  CG   . ASN   B 1 40  ? 47.538 -20.860 9.089   1.00 14.42 ?  40  ASN   B CG   1 
ATOM   4536 O  OD1  . ASN   B 1 40  ? 47.856 -19.680 9.140   1.00 16.47 ?  40  ASN   B OD1  1 
ATOM   4537 N  ND2  . ASN   B 1 40  ? 48.430 -21.835 9.062   1.00 14.63 ?  40  ASN   B ND2  1 
ATOM   4538 H  H    . ASN   B 1 40  ? 46.581 -20.005 6.761   1.00 14.01 ?  40  ASN   B H    1 
ATOM   4539 H  HA   . ASN   B 1 40  ? 44.348 -20.782 8.079   1.00 14.96 ?  40  ASN   B HA   1 
ATOM   4540 H  HB2  . ASN   B 1 40  ? 45.729 -21.195 9.962   1.00 16.24 ?  40  ASN   B HB2  1 
ATOM   4541 H  HB3  . ASN   B 1 40  ? 46.032 -22.184 8.755   1.00 16.24 ?  40  ASN   B HB3  1 
ATOM   4542 H  HD21 . ASN   B 1 40  ? 49.269 -21.650 9.083   1.00 17.52 ?  40  ASN   B HD21 1 
ATOM   4543 H  HD22 . ASN   B 1 40  ? 48.169 -22.653 9.030   1.00 17.52 ?  40  ASN   B HD22 1 
ATOM   4544 N  N    . VAL   B 1 41  ? 44.404 -18.837 9.807   1.00 12.84 ?  41  VAL   B N    1 
ATOM   4545 C  CA   . VAL   B 1 41  ? 43.949 -17.517 10.250  1.00 13.55 ?  41  VAL   B CA   1 
ATOM   4546 C  C    . VAL   B 1 41  ? 45.101 -16.569 10.552  1.00 13.25 ?  41  VAL   B C    1 
ATOM   4547 O  O    . VAL   B 1 41  ? 44.921 -15.350 10.477  1.00 13.71 ?  41  VAL   B O    1 
ATOM   4548 C  CB   . VAL   B 1 41  ? 42.966 -17.594 11.434  1.00 15.06 ?  41  VAL   B CB   1 
ATOM   4549 C  CG1  . VAL   B 1 41  ? 41.670 -18.287 11.026  1.00 15.56 ?  41  VAL   B CG1  1 
ATOM   4550 C  CG2  . VAL   B 1 41  ? 43.611 -18.269 12.629  1.00 16.05 ?  41  VAL   B CG2  1 
ATOM   4551 H  H    . VAL   B 1 41  ? 44.219 -19.478 10.335  1.00 15.38 ?  41  VAL   B H    1 
ATOM   4552 H  HA   . VAL   B 1 41  ? 43.458 -17.114 9.517   1.00 16.23 ?  41  VAL   B HA   1 
ATOM   4553 H  HB   . VAL   B 1 41  ? 42.735 -16.690 11.703  1.00 18.05 ?  41  VAL   B HB   1 
ATOM   4554 H  HG11 . VAL   B 1 41  ? 41.061 -18.288 11.781  1.00 18.64 ?  41  VAL   B HG11 1 
ATOM   4555 H  HG12 . VAL   B 1 41  ? 41.275 -17.805 10.283  1.00 18.64 ?  41  VAL   B HG12 1 
ATOM   4556 H  HG13 . VAL   B 1 41  ? 41.871 -19.198 10.761  1.00 18.64 ?  41  VAL   B HG13 1 
ATOM   4557 H  HG21 . VAL   B 1 41  ? 42.968 -18.315 13.350  1.00 19.22 ?  41  VAL   B HG21 1 
ATOM   4558 H  HG22 . VAL   B 1 41  ? 43.888 -19.164 12.373  1.00 19.22 ?  41  VAL   B HG22 1 
ATOM   4559 H  HG23 . VAL   B 1 41  ? 44.383 -17.751 12.904  1.00 19.22 ?  41  VAL   B HG23 1 
ATOM   4560 N  N    . TYR   B 1 42  ? 46.272 -17.086 10.928  1.00 13.49 ?  42  TYR   B N    1 
ATOM   4561 C  CA   . TYR   B 1 42  ? 47.431 -16.240 11.195  1.00 13.84 ?  42  TYR   B CA   1 
ATOM   4562 C  C    . TYR   B 1 42  ? 48.393 -16.169 10.012  1.00 13.02 ?  42  TYR   B C    1 
ATOM   4563 O  O    . TYR   B 1 42  ? 49.484 -15.601 10.142  1.00 14.44 ?  42  TYR   B O    1 
ATOM   4564 C  CB   . TYR   B 1 42  ? 48.128 -16.644 12.501  1.00 15.85 ?  42  TYR   B CB   1 
ATOM   4565 C  CG   . TYR   B 1 42  ? 47.511 -15.969 13.724  1.00 16.73 ?  42  TYR   B CG   1 
ATOM   4566 C  CD1  . TYR   B 1 42  ? 47.717 -14.612 13.963  1.00 16.05 ?  42  TYR   B CD1  1 
ATOM   4567 C  CD2  . TYR   B 1 42  ? 46.721 -16.674 14.619  1.00 18.53 ?  42  TYR   B CD2  1 
ATOM   4568 C  CE1  . TYR   B 1 42  ? 47.157 -13.981 15.059  1.00 17.10 ?  42  TYR   B CE1  1 
ATOM   4569 C  CE2  . TYR   B 1 42  ? 46.163 -16.050 15.725  1.00 18.83 ?  42  TYR   B CE2  1 
ATOM   4570 C  CZ   . TYR   B 1 42  ? 46.382 -14.699 15.937  1.00 19.04 ?  42  TYR   B CZ   1 
ATOM   4571 O  OH   . TYR   B 1 42  ? 45.835 -14.064 17.035  1.00 21.85 ?  42  TYR   B OH   1 
ATOM   4572 H  H    . TYR   B 1 42  ? 46.421 -17.932 11.025  1.00 16.16 ?  42  TYR   B H    1 
ATOM   4573 H  HA   . TYR   B 1 42  ? 47.104 -15.341 11.329  1.00 16.58 ?  42  TYR   B HA   1 
ATOM   4574 H  HB2  . TYR   B 1 42  ? 48.055 -17.603 12.617  1.00 18.99 ?  42  TYR   B HB2  1 
ATOM   4575 H  HB3  . TYR   B 1 42  ? 49.063 -16.385 12.451  1.00 18.99 ?  42  TYR   B HB3  1 
ATOM   4576 H  HD1  . TYR   B 1 42  ? 48.243 -14.120 13.366  1.00 19.23 ?  42  TYR   B HD1  1 
ATOM   4577 H  HD2  . TYR   B 1 42  ? 46.569 -17.582 14.474  1.00 22.20 ?  42  TYR   B HD2  1 
ATOM   4578 H  HE1  . TYR   B 1 42  ? 47.312 -13.075 15.200  1.00 20.49 ?  42  TYR   B HE1  1 
ATOM   4579 H  HE2  . TYR   B 1 42  ? 45.634 -16.538 16.314  1.00 22.57 ?  42  TYR   B HE2  1 
ATOM   4580 H  HH   . TYR   B 1 42  ? 46.053 -13.254 17.027  1.00 26.19 ?  42  TYR   B HH   1 
ATOM   4581 N  N    . LEU   B 1 43  ? 47.988 -16.681 8.854   1.00 12.08 ?  43  LEU   B N    1 
ATOM   4582 C  CA   . LEU   B 1 43  ? 48.798 -16.614 7.644   1.00 11.95 ?  43  LEU   B CA   1 
ATOM   4583 C  C    . LEU   B 1 43  ? 50.211 -17.123 7.903   1.00 12.23 ?  43  LEU   B C    1 
ATOM   4584 O  O    . LEU   B 1 43  ? 51.194 -16.529 7.459   1.00 13.12 ?  43  LEU   B O    1 
ATOM   4585 C  CB   . LEU   B 1 43  ? 48.815 -15.211 7.033   1.00 12.52 ?  43  LEU   B CB   1 
ATOM   4586 C  CG   . LEU   B 1 43  ? 47.459 -14.593 6.667   1.00 12.55 ?  43  LEU   B CG   1 
ATOM   4587 C  CD1  . LEU   B 1 43  ? 47.670 -13.188 6.097   1.00 13.82 ?  43  LEU   B CD1  1 
ATOM   4588 C  CD2  . LEU   B 1 43  ? 46.683 -15.470 5.691   1.00 12.76 ?  43  LEU   B CD2  1 
ATOM   4589 H  H    . LEU   B 1 43  ? 47.239 -17.091 8.742   1.00 14.47 ?  43  LEU   B H    1 
ATOM   4590 H  HA   . LEU   B 1 43  ? 48.397 -17.207 6.980   1.00 14.31 ?  43  LEU   B HA   1 
ATOM   4591 H  HB2  . LEU   B 1 43  ? 49.242 -14.616 7.666   1.00 14.99 ?  43  LEU   B HB2  1 
ATOM   4592 H  HB3  . LEU   B 1 43  ? 49.342 -15.246 6.218   1.00 14.99 ?  43  LEU   B HB3  1 
ATOM   4593 H  HG   . LEU   B 1 43  ? 46.930 -14.506 7.472   1.00 15.03 ?  43  LEU   B HG   1 
ATOM   4594 H  HD11 . LEU   B 1 43  ? 46.806 -12.807 5.871   1.00 16.56 ?  43  LEU   B HD11 1 
ATOM   4595 H  HD12 . LEU   B 1 43  ? 48.107 -12.638 6.767   1.00 16.56 ?  43  LEU   B HD12 1 
ATOM   4596 H  HD13 . LEU   B 1 43  ? 48.223 -13.246 5.304   1.00 16.56 ?  43  LEU   B HD13 1 
ATOM   4597 H  HD21 . LEU   B 1 43  ? 45.875 -15.004 5.421   1.00 15.28 ?  43  LEU   B HD21 1 
ATOM   4598 H  HD22 . LEU   B 1 43  ? 47.236 -15.648 4.914   1.00 15.28 ?  43  LEU   B HD22 1 
ATOM   4599 H  HD23 . LEU   B 1 43  ? 46.452 -16.303 6.130   1.00 15.28 ?  43  LEU   B HD23 1 
ATOM   4600 N  N    . LYS   B 1 44  ? 50.311 -18.239 8.625   1.00 12.33 ?  44  LYS   B N    1 
ATOM   4601 C  CA   . LYS   B 1 44  ? 51.578 -18.916 8.867   1.00 13.11 ?  44  LYS   B CA   1 
ATOM   4602 C  C    . LYS   B 1 44  ? 51.701 -20.032 7.839   1.00 12.56 ?  44  LYS   B C    1 
ATOM   4603 O  O    . LYS   B 1 44  ? 51.000 -21.047 7.921   1.00 14.06 ?  44  LYS   B O    1 
ATOM   4604 C  CB   . LYS   B 1 44  ? 51.632 -19.437 10.301  1.00 14.79 ?  44  LYS   B CB   1 
ATOM   4605 C  CG   . LYS   B 1 44  ? 51.819 -18.336 11.330  1.00 17.58 ?  44  LYS   B CG   1 
ATOM   4606 C  CD   . LYS   B 1 44  ? 53.017 -17.466 10.944  1.00 20.80 ?  44  LYS   B CD   1 
ATOM   4607 C  CE   . LYS   B 1 44  ? 53.522 -16.609 12.074  1.00 23.53 ?  44  LYS   B CE   1 
ATOM   4608 N  NZ   . LYS   B 1 44  ? 54.684 -15.778 11.675  1.00 24.83 ?  44  LYS   B NZ   1 
ATOM   4609 H  H    . LYS   B 1 44  ? 49.638 -18.626 8.997   1.00 14.76 ?  44  LYS   B H    1 
ATOM   4610 H  HA   . LYS   B 1 44  ? 52.308 -18.299 8.709   1.00 15.71 ?  44  LYS   B HA   1 
ATOM   4611 H  HB2  . LYS   B 1 44  ? 50.794 -19.890 10.503  1.00 17.72 ?  44  LYS   B HB2  1 
ATOM   4612 H  HB3  . LYS   B 1 44  ? 52.370 -20.054 10.386  1.00 17.72 ?  44  LYS   B HB3  1 
ATOM   4613 H  HG2  . LYS   B 1 44  ? 51.026 -17.782 11.365  1.00 21.07 ?  44  LYS   B HG2  1 
ATOM   4614 H  HG3  . LYS   B 1 44  ? 51.995 -18.736 12.200  1.00 21.07 ?  44  LYS   B HG3  1 
ATOM   4615 H  HD2  . LYS   B 1 44  ? 53.736 -18.047 10.639  1.00 24.93 ?  44  LYS   B HD2  1 
ATOM   4616 H  HD3  . LYS   B 1 44  ? 52.745 -16.874 10.223  1.00 24.93 ?  44  LYS   B HD3  1 
ATOM   4617 H  HE2  . LYS   B 1 44  ? 52.820 -15.999 12.318  1.00 28.21 ?  44  LYS   B HE2  1 
ATOM   4618 H  HE3  . LYS   B 1 44  ? 53.775 -17.172 12.824  1.00 28.21 ?  44  LYS   B HE3  1 
ATOM   4619 H  HZ1  . LYS   B 1 44  ? 54.954 -15.284 12.365  1.00 29.77 ?  44  LYS   B HZ1  1 
ATOM   4620 H  HZ2  . LYS   B 1 44  ? 55.356 -16.295 11.408  1.00 29.77 ?  44  LYS   B HZ2  1 
ATOM   4621 H  HZ3  . LYS   B 1 44  ? 54.454 -15.235 11.006  1.00 29.77 ?  44  LYS   B HZ3  1 
ATOM   4622 N  N    . HIS   B 1 45  ? 52.556 -19.814 6.842   1.00 12.08 ?  45  HIS   B N    1 
ATOM   4623 C  CA   . HIS   B 1 45  ? 52.576 -20.647 5.640   1.00 12.60 ?  45  HIS   B CA   1 
ATOM   4624 C  C    . HIS   B 1 45  ? 53.592 -21.772 5.803   1.00 14.59 ?  45  HIS   B C    1 
ATOM   4625 O  O    . HIS   B 1 45  ? 54.653 -21.793 5.187   1.00 16.97 ?  45  HIS   B O    1 
ATOM   4626 C  CB   . HIS   B 1 45  ? 52.889 -19.800 4.420   1.00 12.72 ?  45  HIS   B CB   1 
ATOM   4627 C  CG   . HIS   B 1 45  ? 52.017 -18.597 4.304   1.00 12.54 ?  45  HIS   B CG   1 
ATOM   4628 N  ND1  . HIS   B 1 45  ? 50.639 -18.673 4.265   1.00 12.47 ?  45  HIS   B ND1  1 
ATOM   4629 C  CD2  . HIS   B 1 45  ? 52.332 -17.283 4.228   1.00 13.04 ?  45  HIS   B CD2  1 
ATOM   4630 C  CE1  . HIS   B 1 45  ? 50.150 -17.450 4.156   1.00 12.14 ?  45  HIS   B CE1  1 
ATOM   4631 N  NE2  . HIS   B 1 45  ? 51.153 -16.590 4.132   1.00 12.75 ?  45  HIS   B NE2  1 
ATOM   4632 H  H    . HIS   B 1 45  ? 53.129 -19.173 6.829   1.00 14.47 ?  45  HIS   B H    1 
ATOM   4633 H  HA   . HIS   B 1 45  ? 51.697 -21.044 5.513   1.00 15.09 ?  45  HIS   B HA   1 
ATOM   4634 H  HB2  . HIS   B 1 45  ? 53.807 -19.502 4.467   1.00 15.23 ?  45  HIS   B HB2  1 
ATOM   4635 H  HB3  . HIS   B 1 45  ? 52.759 -20.343 3.620   1.00 15.23 ?  45  HIS   B HB3  1 
ATOM   4636 H  HD2  . HIS   B 1 45  ? 53.186 -16.916 4.239   1.00 15.62 ?  45  HIS   B HD2  1 
ATOM   4637 H  HE1  . HIS   B 1 45  ? 49.246 -17.235 4.097   1.00 14.54 ?  45  HIS   B HE1  1 
ATOM   4638 H  HE2  . HIS   B 1 45  ? 51.075 -15.736 4.076   1.00 15.27 ?  45  HIS   B HE2  1 
ATOM   4639 N  N    A GLY   B 1 46  ? 53.221 -22.742 6.632   0.72 15.69 ?  46  GLY   B N    1 
ATOM   4640 N  N    B GLY   B 1 46  ? 53.234 -22.725 6.654   0.28 15.50 ?  46  GLY   B N    1 
ATOM   4641 C  CA   A GLY   B 1 46  ? 54.142 -23.798 7.012   0.72 17.36 ?  46  GLY   B CA   1 
ATOM   4642 C  CA   B GLY   B 1 46  ? 54.150 -23.795 6.987   0.28 16.55 ?  46  GLY   B CA   1 
ATOM   4643 C  C    A GLY   B 1 46  ? 54.196 -25.015 6.109   0.72 19.02 ?  46  GLY   B C    1 
ATOM   4644 C  C    B GLY   B 1 46  ? 54.174 -24.928 5.980   0.28 17.67 ?  46  GLY   B C    1 
ATOM   4645 O  O    A GLY   B 1 46  ? 55.277 -25.443 5.691   0.72 21.99 ?  46  GLY   B O    1 
ATOM   4646 O  O    B GLY   B 1 46  ? 55.196 -25.178 5.331   0.28 18.06 ?  46  GLY   B O    1 
ATOM   4647 H  H    A GLY   B 1 46  ? 52.443 -22.794 7.007   0.72 18.80 ?  46  GLY   B H    1 
ATOM   4648 H  H    B GLY   B 1 46  ? 52.469 -22.767 7.053   0.28 18.56 ?  46  GLY   B H    1 
ATOM   4649 H  HA2  A GLY   B 1 46  ? 55.034 -23.423 7.063   0.72 20.80 ?  46  GLY   B HA2  1 
ATOM   4650 H  HA2  B GLY   B 1 46  ? 55.046 -23.430 7.053   0.28 19.84 ?  46  GLY   B HA2  1 
ATOM   4651 H  HA3  A GLY   B 1 46  ? 53.902 -24.113 7.897   0.72 20.80 ?  46  GLY   B HA3  1 
ATOM   4652 H  HA3  B GLY   B 1 46  ? 53.908 -24.154 7.856   0.28 19.84 ?  46  GLY   B HA3  1 
ATOM   4653 N  N    . GLY   B 1 47  ? 53.042 -25.611 5.819   1.00 18.47 ?  47  GLY   B N    1 
ATOM   4654 C  CA   . GLY   B 1 47  ? 52.988 -26.871 5.107   1.00 16.33 ?  47  GLY   B CA   1 
ATOM   4655 C  C    . GLY   B 1 47  ? 52.069 -26.841 3.901   1.00 14.14 ?  47  GLY   B C    1 
ATOM   4656 O  O    . GLY   B 1 47  ? 51.409 -25.841 3.615   1.00 14.21 ?  47  GLY   B O    1 
ATOM   4657 H  H    A GLY   B 1 47  ? 52.269 -25.310 6.053   0.72 22.13 ?  47  GLY   B H    1 
ATOM   4658 H  H    B GLY   B 1 47  ? 52.277 -25.349 6.119   0.28 22.13 ?  47  GLY   B H    1 
ATOM   4659 H  HA2  . GLY   B 1 47  ? 53.877 -27.114 4.804   1.00 19.57 ?  47  GLY   B HA2  1 
ATOM   4660 H  HA3  . GLY   B 1 47  ? 52.678 -27.564 5.713   1.00 19.57 ?  47  GLY   B HA3  1 
ATOM   4661 N  N    . GLY   B 1 48  ? 52.021 -27.982 3.215   1.00 13.62 ?  48  GLY   B N    1 
ATOM   4662 C  CA   . GLY   B 1 48  ? 51.100 -28.141 2.107   1.00 13.28 ?  48  GLY   B CA   1 
ATOM   4663 C  C    . GLY   B 1 48  ? 51.237 -27.035 1.087   1.00 12.53 ?  48  GLY   B C    1 
ATOM   4664 O  O    . GLY   B 1 48  ? 52.340 -26.573 0.771   1.00 13.08 ?  48  GLY   B O    1 
ATOM   4665 H  H    . GLY   B 1 48  ? 52.517 -28.665 3.367   1.00 16.31 ?  48  GLY   B H    1 
ATOM   4666 H  HA2  . GLY   B 1 48  ? 51.263 -28.990 1.669   1.00 15.91 ?  48  GLY   B HA2  1 
ATOM   4667 H  HA3  . GLY   B 1 48  ? 50.189 -28.136 2.440   1.00 15.91 ?  48  GLY   B HA3  1 
ATOM   4668 N  N    . VAL   B 1 49  ? 50.091 -26.601 0.561   1.00 12.40 ?  49  VAL   B N    1 
ATOM   4669 C  CA   . VAL   B 1 49  ? 50.073 -25.577 -0.479  1.00 12.30 ?  49  VAL   B CA   1 
ATOM   4670 C  C    . VAL   B 1 49  ? 50.730 -24.289 0.008   1.00 11.33 ?  49  VAL   B C    1 
ATOM   4671 O  O    . VAL   B 1 49  ? 51.520 -23.668 -0.714  1.00 12.36 ?  49  VAL   B O    1 
ATOM   4672 C  CB   . VAL   B 1 49  ? 48.628 -25.324 -0.954  1.00 13.84 ?  49  VAL   B CB   1 
ATOM   4673 C  CG1  . VAL   B 1 49  ? 48.557 -24.074 -1.827  1.00 13.84 ?  49  VAL   B CG1  1 
ATOM   4674 C  CG2  . VAL   B 1 49  ? 48.082 -26.534 -1.703  1.00 15.33 ?  49  VAL   B CG2  1 
ATOM   4675 H  H    . VAL   B 1 49  ? 49.306 -26.890 0.784   1.00 14.85 ?  49  VAL   B H    1 
ATOM   4676 H  HA   . VAL   B 1 49  ? 50.575 -25.896 -1.243  1.00 14.74 ?  49  VAL   B HA   1 
ATOM   4677 H  HB   . VAL   B 1 49  ? 48.064 -25.176 -0.181  1.00 16.58 ?  49  VAL   B HB   1 
ATOM   4678 H  HG11 . VAL   B 1 49  ? 47.728 -24.086 -2.332  1.00 16.58 ?  49  VAL   B HG11 1 
ATOM   4679 H  HG12 . VAL   B 1 49  ? 48.579 -23.285 -1.258  1.00 16.58 ?  49  VAL   B HG12 1 
ATOM   4680 H  HG13 . VAL   B 1 49  ? 49.312 -24.064 -2.434  1.00 16.58 ?  49  VAL   B HG13 1 
ATOM   4681 H  HG21 . VAL   B 1 49  ? 47.172 -26.347 -1.988  1.00 18.37 ?  49  VAL   B HG21 1 
ATOM   4682 H  HG22 . VAL   B 1 49  ? 48.640 -26.705 -2.479  1.00 18.37 ?  49  VAL   B HG22 1 
ATOM   4683 H  HG23 . VAL   B 1 49  ? 48.092 -27.302 -1.113  1.00 18.37 ?  49  VAL   B HG23 1 
ATOM   4684 N  N    . ALA   B 1 50  ? 50.384 -23.842 1.218   1.00 11.53 ?  50  ALA   B N    1 
ATOM   4685 C  CA   . ALA   B 1 50  ? 50.902 -22.561 1.692   1.00 11.46 ?  50  ALA   B CA   1 
ATOM   4686 C  C    . ALA   B 1 50  ? 52.423 -22.589 1.802   1.00 11.59 ?  50  ALA   B C    1 
ATOM   4687 O  O    . ALA   B 1 50  ? 53.105 -21.628 1.425   1.00 11.55 ?  50  ALA   B O    1 
ATOM   4688 C  CB   . ALA   B 1 50  ? 50.266 -22.200 3.031   1.00 11.89 ?  50  ALA   B CB   1 
ATOM   4689 H  H    . ALA   B 1 50  ? 49.865 -24.248 1.769   1.00 13.81 ?  50  ALA   B H    1 
ATOM   4690 H  HA   . ALA   B 1 50  ? 50.671 -21.870 1.057   1.00 13.72 ?  50  ALA   B HA   1 
ATOM   4691 H  HB1  . ALA   B 1 50  ? 50.620 -21.346 3.332   1.00 14.23 ?  50  ALA   B HB1  1 
ATOM   4692 H  HB2  . ALA   B 1 50  ? 49.304 -22.133 2.916   1.00 14.23 ?  50  ALA   B HB2  1 
ATOM   4693 H  HB3  . ALA   B 1 50  ? 50.474 -22.890 3.680   1.00 14.23 ?  50  ALA   B HB3  1 
ATOM   4694 N  N    . GLY   B 1 51  ? 52.975 -23.681 2.321   1.00 12.24 ?  51  GLY   B N    1 
ATOM   4695 C  CA   . GLY   B 1 51  ? 54.421 -23.789 2.392   1.00 12.71 ?  51  GLY   B CA   1 
ATOM   4696 C  C    . GLY   B 1 51  ? 55.069 -23.738 1.023   1.00 12.53 ?  51  GLY   B C    1 
ATOM   4697 O  O    . GLY   B 1 51  ? 56.113 -23.105 0.842   1.00 13.43 ?  51  GLY   B O    1 
ATOM   4698 H  H    . GLY   B 1 51  ? 52.547 -24.360 2.632   1.00 14.66 ?  51  GLY   B H    1 
ATOM   4699 H  HA2  . GLY   B 1 51  ? 54.777 -23.056 2.923   1.00 15.22 ?  51  GLY   B HA2  1 
ATOM   4700 H  HA3  . GLY   B 1 51  ? 54.668 -24.624 2.817   1.00 15.22 ?  51  GLY   B HA3  1 
ATOM   4701 N  N    . ALA   B 1 52  ? 54.464 -24.405 0.043   1.00 12.38 ?  52  ALA   B N    1 
ATOM   4702 C  CA   . ALA   B 1 52  ? 55.023 -24.416 -1.301  1.00 12.72 ?  52  ALA   B CA   1 
ATOM   4703 C  C    . ALA   B 1 52  ? 54.939 -23.039 -1.956  1.00 11.84 ?  52  ALA   B C    1 
ATOM   4704 O  O    . ALA   B 1 52  ? 55.906 -22.589 -2.591  1.00 12.77 ?  52  ALA   B O    1 
ATOM   4705 C  CB   . ALA   B 1 52  ? 54.317 -25.466 -2.151  1.00 13.61 ?  52  ALA   B CB   1 
ATOM   4706 H  H    . ALA   B 1 52  ? 53.732 -24.852 0.129   1.00 14.83 ?  52  ALA   B H    1 
ATOM   4707 H  HA   . ALA   B 1 52  ? 55.960 -24.655 -1.245  1.00 15.24 ?  52  ALA   B HA   1 
ATOM   4708 H  HB1  . ALA   B 1 52  ? 54.705 -25.461 -3.042  1.00 16.31 ?  52  ALA   B HB1  1 
ATOM   4709 H  HB2  . ALA   B 1 52  ? 54.448 -26.337 -1.742  1.00 16.31 ?  52  ALA   B HB2  1 
ATOM   4710 H  HB3  . ALA   B 1 52  ? 53.375 -25.257 -2.197  1.00 16.31 ?  52  ALA   B HB3  1 
ATOM   4711 N  N    . LEU   B 1 53  ? 53.796 -22.357 -1.835  1.00 11.71 ?  53  LEU   B N    1 
ATOM   4712 C  CA   . LEU   B 1 53  ? 53.690 -21.020 -2.411  1.00 11.87 ?  53  LEU   B CA   1 
ATOM   4713 C  C    . LEU   B 1 53  ? 54.696 -20.079 -1.761  1.00 11.63 ?  53  LEU   B C    1 
ATOM   4714 O  O    . LEU   B 1 53  ? 55.398 -19.326 -2.448  1.00 12.41 ?  53  LEU   B O    1 
ATOM   4715 C  CB   . LEU   B 1 53  ? 52.266 -20.477 -2.251  1.00 12.59 ?  53  LEU   B CB   1 
ATOM   4716 C  CG   . LEU   B 1 53  ? 51.128 -21.204 -2.976  1.00 12.85 ?  53  LEU   B CG   1 
ATOM   4717 C  CD1  . LEU   B 1 53  ? 49.779 -20.589 -2.622  1.00 14.52 ?  53  LEU   B CD1  1 
ATOM   4718 C  CD2  . LEU   B 1 53  ? 51.338 -21.218 -4.487  1.00 14.64 ?  53  LEU   B CD2  1 
ATOM   4719 H  H    . LEU   B 1 53  ? 53.089 -22.636 -1.432  1.00 14.03 ?  53  LEU   B H    1 
ATOM   4720 H  HA   . LEU   B 1 53  ? 53.893 -21.070 -3.364  1.00 14.21 ?  53  LEU   B HA   1 
ATOM   4721 H  HB2  . LEU   B 1 53  ? 52.050 -20.491 -1.311  1.00 15.08 ?  53  LEU   B HB2  1 
ATOM   4722 H  HB3  . LEU   B 1 53  ? 52.260 -19.565 -2.572  1.00 15.08 ?  53  LEU   B HB3  1 
ATOM   4723 H  HG   . LEU   B 1 53  ? 51.110 -22.127 -2.679  1.00 15.39 ?  53  LEU   B HG   1 
ATOM   4724 H  HD11 . LEU   B 1 53  ? 49.077 -21.071 -3.091  1.00 17.40 ?  53  LEU   B HD11 1 
ATOM   4725 H  HD12 . LEU   B 1 53  ? 49.642 -20.664 -1.662  1.00 17.40 ?  53  LEU   B HD12 1 
ATOM   4726 H  HD13 . LEU   B 1 53  ? 49.775 -19.658 -2.885  1.00 17.40 ?  53  LEU   B HD13 1 
ATOM   4727 H  HD21 . LEU   B 1 53  ? 50.619 -21.723 -4.902  1.00 17.54 ?  53  LEU   B HD21 1 
ATOM   4728 H  HD22 . LEU   B 1 53  ? 51.332 -20.308 -4.817  1.00 17.54 ?  53  LEU   B HD22 1 
ATOM   4729 H  HD23 . LEU   B 1 53  ? 52.189 -21.640 -4.686  1.00 17.54 ?  53  LEU   B HD23 1 
ATOM   4730 N  N    . ASN   B 1 54  ? 54.785 -20.108 -0.433  1.00 11.32 ?  54  ASN   B N    1 
ATOM   4731 C  CA   . ASN   B 1 54  ? 55.696 -19.194 0.235   1.00 12.22 ?  54  ASN   B CA   1 
ATOM   4732 C  C    . ASN   B 1 54  ? 57.140 -19.471 -0.164  1.00 12.61 ?  54  ASN   B C    1 
ATOM   4733 O  O    . ASN   B 1 54  ? 57.911 -18.533 -0.403  1.00 13.17 ?  54  ASN   B O    1 
ATOM   4734 C  CB   . ASN   B 1 54  ? 55.539 -19.269 1.744   1.00 12.93 ?  54  ASN   B CB   1 
ATOM   4735 C  CG   . ASN   B 1 54  ? 56.523 -18.364 2.448   1.00 12.86 ?  54  ASN   B CG   1 
ATOM   4736 O  OD1  . ASN   B 1 54  ? 56.548 -17.151 2.206   1.00 13.22 ?  54  ASN   B OD1  1 
ATOM   4737 N  ND2  . ASN   B 1 54  ? 57.363 -18.944 3.296   1.00 14.76 ?  54  ASN   B ND2  1 
ATOM   4738 H  H    . ASN   B 1 54  ? 54.338 -20.633 0.083   1.00 13.56 ?  54  ASN   B H    1 
ATOM   4739 H  HA   . ASN   B 1 54  ? 55.480 -18.290 -0.041  1.00 14.64 ?  54  ASN   B HA   1 
ATOM   4740 H  HB2  . ASN   B 1 54  ? 54.643 -18.989 1.989   1.00 15.49 ?  54  ASN   B HB2  1 
ATOM   4741 H  HB3  . ASN   B 1 54  ? 55.699 -20.178 2.039   1.00 15.49 ?  54  ASN   B HB3  1 
ATOM   4742 H  HD21 . ASN   B 1 54  ? 57.949 -18.470 3.716   1.00 17.68 ?  54  ASN   B HD21 1 
ATOM   4743 H  HD22 . ASN   B 1 54  ? 57.327 -19.793 3.428   1.00 17.68 ?  54  ASN   B HD22 1 
ATOM   4744 N  N    . LYS   B 1 55  ? 57.528 -20.750 -0.226  1.00 13.10 ?  55  LYS   B N    1 
ATOM   4745 C  CA   . LYS   B 1 55  ? 58.886 -21.091 -0.642  1.00 14.24 ?  55  LYS   B CA   1 
ATOM   4746 C  C    . LYS   B 1 55  ? 59.184 -20.554 -2.035  1.00 13.84 ?  55  LYS   B C    1 
ATOM   4747 O  O    . LYS   B 1 55  ? 60.283 -20.047 -2.288  1.00 14.64 ?  55  LYS   B O    1 
ATOM   4748 C  CB   . LYS   B 1 55  ? 59.094 -22.606 -0.588  1.00 15.98 ?  55  LYS   B CB   1 
ATOM   4749 C  CG   . LYS   B 1 55  ? 60.480 -23.062 -1.011  1.00 19.84 ?  55  LYS   B CG   1 
ATOM   4750 C  CD   . LYS   B 1 55  ? 60.647 -24.561 -0.829  1.00 23.13 ?  55  LYS   B CD   1 
ATOM   4751 C  CE   . LYS   B 1 55  ? 60.689 -24.952 0.647   1.00 26.34 ?  55  LYS   B CE   1 
ATOM   4752 N  NZ   . LYS   B 1 55  ? 61.061 -26.375 0.837   1.00 28.05 ?  55  LYS   B NZ   1 
ATOM   4753 H  H    . LYS   B 1 55  ? 57.026 -21.424 -0.041  1.00 15.69 ?  55  LYS   B H    1 
ATOM   4754 H  HA   . LYS   B 1 55  ? 59.512 -20.681 -0.031  1.00 17.06 ?  55  LYS   B HA   1 
ATOM   4755 H  HB2  . LYS   B 1 55  ? 58.947 -22.899 0.323   1.00 19.15 ?  55  LYS   B HB2  1 
ATOM   4756 H  HB3  . LYS   B 1 55  ? 58.453 -23.030 -1.178  1.00 19.15 ?  55  LYS   B HB3  1 
ATOM   4757 H  HG2  . LYS   B 1 55  ? 60.618 -22.855 -1.949  1.00 23.77 ?  55  LYS   B HG2  1 
ATOM   4758 H  HG3  . LYS   B 1 55  ? 61.147 -22.613 -0.467  1.00 23.77 ?  55  LYS   B HG3  1 
ATOM   4759 H  HD2  . LYS   B 1 55  ? 59.899 -25.024 -1.241  1.00 27.72 ?  55  LYS   B HD2  1 
ATOM   4760 H  HD3  . LYS   B 1 55  ? 61.481 -24.848 -1.237  1.00 27.72 ?  55  LYS   B HD3  1 
ATOM   4761 H  HE2  . LYS   B 1 55  ? 61.345 -24.397 1.101   1.00 31.58 ?  55  LYS   B HE2  1 
ATOM   4762 H  HE3  . LYS   B 1 55  ? 59.810 -24.810 1.036   1.00 31.58 ?  55  LYS   B HE3  1 
ATOM   4763 H  HZ1  . LYS   B 1 55  ? 61.052 -26.575 1.705   1.00 33.63 ?  55  LYS   B HZ1  1 
ATOM   4764 H  HZ2  . LYS   B 1 55  ? 60.478 -26.898 0.414   1.00 33.63 ?  55  LYS   B HZ2  1 
ATOM   4765 H  HZ3  . LYS   B 1 55  ? 61.874 -26.521 0.512   1.00 33.63 ?  55  LYS   B HZ3  1 
ATOM   4766 N  N    . ALA   B 1 56  ? 58.215 -20.636 -2.950  1.00 13.48 ?  56  ALA   B N    1 
ATOM   4767 C  CA   . ALA   B 1 56  ? 58.437 -20.134 -4.300  1.00 14.30 ?  56  ALA   B CA   1 
ATOM   4768 C  C    . ALA   B 1 56  ? 58.711 -18.638 -4.300  1.00 13.89 ?  56  ALA   B C    1 
ATOM   4769 O  O    . ALA   B 1 56  ? 59.423 -18.141 -5.183  1.00 15.16 ?  56  ALA   B O    1 
ATOM   4770 C  CB   . ALA   B 1 56  ? 57.238 -20.460 -5.192  1.00 15.30 ?  56  ALA   B CB   1 
ATOM   4771 H  H    . ALA   B 1 56  ? 57.426 -20.956 -2.814  1.00 16.14 ?  56  ALA   B H    1 
ATOM   4772 H  HA   . ALA   B 1 56  ? 59.212 -20.570 -4.675  1.00 17.13 ?  56  ALA   B HA   1 
ATOM   4773 H  HB1  . ALA   B 1 56  ? 57.409 -20.125 -6.092  1.00 18.33 ?  56  ALA   B HB1  1 
ATOM   4774 H  HB2  . ALA   B 1 56  ? 57.119 -21.422 -5.222  1.00 18.33 ?  56  ALA   B HB2  1 
ATOM   4775 H  HB3  . ALA   B 1 56  ? 56.443 -20.039 -4.833  1.00 18.33 ?  56  ALA   B HB3  1 
ATOM   4776 N  N    . THR   B 1 57  ? 58.148 -17.902 -3.338  1.00 13.79 ?  57  THR   B N    1 
ATOM   4777 C  CA   . THR   B 1 57  ? 58.385 -16.467 -3.215  1.00 14.07 ?  57  THR   B CA   1 
ATOM   4778 C  C    . THR   B 1 57  ? 59.635 -16.143 -2.403  1.00 14.89 ?  57  THR   B C    1 
ATOM   4779 O  O    . THR   B 1 57  ? 59.868 -14.969 -2.089  1.00 15.22 ?  57  THR   B O    1 
ATOM   4780 C  CB   . THR   B 1 57  ? 57.181 -15.739 -2.582  1.00 13.19 ?  57  THR   B CB   1 
ATOM   4781 O  OG1  . THR   B 1 57  ? 57.160 -15.957 -1.164  1.00 13.53 ?  57  THR   B OG1  1 
ATOM   4782 C  CG2  . THR   B 1 57  ? 55.861 -16.160 -3.224  1.00 13.43 ?  57  THR   B CG2  1 
ATOM   4783 H  H    . THR   B 1 57  ? 57.605 -18.214 -2.747  1.00 16.52 ?  57  THR   B H    1 
ATOM   4784 H  HA   . THR   B 1 57  ? 58.507 -16.100 -4.105  1.00 16.85 ?  57  THR   B HA   1 
ATOM   4785 H  HB   . THR   B 1 57  ? 57.286 -14.785 -2.746  1.00 15.79 ?  57  THR   B HB   1 
ATOM   4786 H  HG1  . THR   B 1 57  ? 57.085 -16.776 -1.005  1.00 16.20 ?  57  THR   B HG1  1 
ATOM   4787 H  HG21 . THR   B 1 57  ? 55.134 -15.625 -2.871  1.00 16.08 ?  57  THR   B HG21 1 
ATOM   4788 H  HG22 . THR   B 1 57  ? 55.904 -16.037 -4.186  1.00 16.08 ?  57  THR   B HG22 1 
ATOM   4789 H  HG23 . THR   B 1 57  ? 55.685 -17.094 -3.036  1.00 16.08 ?  57  THR   B HG23 1 
ATOM   4790 N  N    . ASN   B 1 58  ? 60.432 -17.147 -2.049  1.00 15.23 ?  58  ASN   B N    1 
ATOM   4791 C  CA   . ASN   B 1 58  ? 61.628 -16.930 -1.240  1.00 18.16 ?  58  ASN   B CA   1 
ATOM   4792 C  C    . ASN   B 1 58  ? 61.287 -16.221 0.072   1.00 15.94 ?  58  ASN   B C    1 
ATOM   4793 O  O    . ASN   B 1 58  ? 62.020 -15.344 0.538   1.00 16.68 ?  58  ASN   B O    1 
ATOM   4794 C  CB   . ASN   B 1 58  ? 62.709 -16.175 -2.020  1.00 26.37 ?  58  ASN   B CB   1 
ATOM   4795 C  CG   . ASN   B 1 58  ? 64.085 -16.324 -1.398  1.00 35.52 ?  58  ASN   B CG   1 
ATOM   4796 O  OD1  . ASN   B 1 58  ? 64.385 -17.337 -0.766  1.00 38.29 ?  58  ASN   B OD1  1 
ATOM   4797 N  ND2  . ASN   B 1 58  ? 64.927 -15.312 -1.571  1.00 41.12 ?  58  ASN   B ND2  1 
ATOM   4798 H  H    . ASN   B 1 58  ? 60.299 -17.974 -2.265  1.00 18.24 ?  58  ASN   B H    1 
ATOM   4799 H  HA   . ASN   B 1 58  ? 61.995 -17.800 -1.018  1.00 21.76 ?  58  ASN   B HA   1 
ATOM   4800 H  HB2  . ASN   B 1 58  ? 62.750 -16.522 -2.928  1.00 31.61 ?  58  ASN   B HB2  1 
ATOM   4801 H  HB3  . ASN   B 1 58  ? 62.490 -15.232 -2.037  1.00 31.61 ?  58  ASN   B HB3  1 
ATOM   4802 H  HD21 . ASN   B 1 58  ? 65.719 -15.350 -1.238  1.00 49.32 ?  58  ASN   B HD21 1 
ATOM   4803 H  HD22 . ASN   B 1 58  ? 64.680 -14.619 -2.016  1.00 49.32 ?  58  ASN   B HD22 1 
ATOM   4804 N  N    . ASN   B 1 59  ? 60.161 -16.605 0.674   1.00 14.97 ?  59  ASN   B N    1 
ATOM   4805 C  CA   . ASN   B 1 59  ? 59.684 -16.128 1.973   1.00 14.83 ?  59  ASN   B CA   1 
ATOM   4806 C  C    . ASN   B 1 59  ? 59.093 -14.721 1.921   1.00 14.01 ?  59  ASN   B C    1 
ATOM   4807 O  O    . ASN   B 1 59  ? 58.664 -14.215 2.969   1.00 14.17 ?  59  ASN   B O    1 
ATOM   4808 C  CB   . ASN   B 1 59  ? 60.756 -16.186 3.077   1.00 15.98 ?  59  ASN   B CB   1 
ATOM   4809 C  CG   . ASN   B 1 59  ? 60.167 -16.363 4.458   1.00 17.40 ?  59  ASN   B CG   1 
ATOM   4810 O  OD1  . ASN   B 1 59  ? 59.342 -17.252 4.683   1.00 17.38 ?  59  ASN   B OD1  1 
ATOM   4811 N  ND2  . ASN   B 1 59  ? 60.593 -15.526 5.396   1.00 18.05 ?  59  ASN   B ND2  1 
ATOM   4812 H  H    . ASN   B 1 59  ? 59.619 -17.185 0.326   1.00 17.94 ?  59  ASN   B H    1 
ATOM   4813 H  HA   . ASN   B 1 59  ? 58.974 -16.723 2.257   1.00 17.77 ?  59  ASN   B HA   1 
ATOM   4814 H  HB2  . ASN   B 1 59  ? 61.349 -16.936 2.912   1.00 19.14 ?  59  ASN   B HB2  1 
ATOM   4815 H  HB3  . ASN   B 1 59  ? 61.259 -15.358 3.079   1.00 19.14 ?  59  ASN   B HB3  1 
ATOM   4816 H  HD21 . ASN   B 1 59  ? 60.288 -15.589 6.200   1.00 21.62 ?  59  ASN   B HD21 1 
ATOM   4817 H  HD22 . ASN   B 1 59  ? 61.169 -14.921 5.202   1.00 21.62 ?  59  ASN   B HD22 1 
ATOM   4818 N  N    . ALA   B 1 60  ? 59.028 -14.078 0.750   1.00 14.05 ?  60  ALA   B N    1 
ATOM   4819 C  CA   . ALA   B 1 60  ? 58.434 -12.744 0.679   1.00 13.77 ?  60  ALA   B CA   1 
ATOM   4820 C  C    . ALA   B 1 60  ? 56.966 -12.770 1.080   1.00 13.03 ?  60  ALA   B C    1 
ATOM   4821 O  O    . ALA   B 1 60  ? 56.464 -11.823 1.699   1.00 13.79 ?  60  ALA   B O    1 
ATOM   4822 C  CB   . ALA   B 1 60  ? 58.597 -12.169 -0.726  1.00 14.87 ?  60  ALA   B CB   1 
ATOM   4823 H  H    . ALA   B 1 60  ? 59.316 -14.391 0.004   1.00 16.84 ?  60  ALA   B H    1 
ATOM   4824 H  HA   . ALA   B 1 60  ? 58.898 -12.165 1.300   1.00 16.49 ?  60  ALA   B HA   1 
ATOM   4825 H  HB1  . ALA   B 1 60  ? 58.199 -11.287 -0.750  1.00 17.81 ?  60  ALA   B HB1  1 
ATOM   4826 H  HB2  . ALA   B 1 60  ? 59.544 -12.112 -0.934  1.00 17.81 ?  60  ALA   B HB2  1 
ATOM   4827 H  HB3  . ALA   B 1 60  ? 58.155 -12.753 -1.361  1.00 17.81 ?  60  ALA   B HB3  1 
ATOM   4828 N  N    . MET   B 1 61  ? 56.260 -13.847 0.734   1.00 12.67 ?  61  MET   B N    1 
ATOM   4829 C  CA   . MET   B 1 61  ? 54.862 -13.972 1.127   1.00 12.53 ?  61  MET   B CA   1 
ATOM   4830 C  C    . MET   B 1 61  ? 54.722 -13.981 2.650   1.00 12.55 ?  61  MET   B C    1 
ATOM   4831 O  O    . MET   B 1 61  ? 53.820 -13.336 3.202   1.00 12.45 ?  61  MET   B O    1 
ATOM   4832 C  CB   . MET   B 1 61  ? 54.281 -15.242 0.499   1.00 12.41 ?  61  MET   B CB   1 
ATOM   4833 C  CG   . MET   B 1 61  ? 52.832 -15.529 0.897   1.00 11.92 ?  61  MET   B CG   1 
ATOM   4834 S  SD   . MET   B 1 61  ? 52.197 -17.039 0.143   1.00 12.74 ?  61  MET   B SD   1 
ATOM   4835 C  CE   . MET   B 1 61  ? 51.928 -16.438 -1.522  1.00 13.86 ?  61  MET   B CE   1 
ATOM   4836 H  H    . MET   B 1 61  ? 56.562 -14.517 0.277   1.00 15.18 ?  61  MET   B H    1 
ATOM   4837 H  HA   . MET   B 1 61  ? 54.367 -13.218 0.765   1.00 15.00 ?  61  MET   B HA   1 
ATOM   4838 H  HB2  . MET   B 1 61  ? 54.306 -15.157 -0.470  1.00 14.86 ?  61  MET   B HB2  1 
ATOM   4839 H  HB3  . MET   B 1 61  ? 54.817 -16.002 0.773   1.00 14.86 ?  61  MET   B HB3  1 
ATOM   4840 H  HG2  . MET   B 1 61  ? 52.780 -15.634 1.862   1.00 14.27 ?  61  MET   B HG2  1 
ATOM   4841 H  HG3  . MET   B 1 61  ? 52.272 -14.787 0.617   1.00 14.27 ?  61  MET   B HG3  1 
ATOM   4842 H  HE1  . MET   B 1 61  ? 51.546 -17.151 -2.059  1.00 16.60 ?  61  MET   B HE1  1 
ATOM   4843 H  HE2  . MET   B 1 61  ? 51.313 -15.684 -1.494  1.00 16.60 ?  61  MET   B HE2  1 
ATOM   4844 H  HE3  . MET   B 1 61  ? 52.774 -16.156 -1.899  1.00 16.60 ?  61  MET   B HE3  1 
ATOM   4845 N  N    . GLN   B 1 62  ? 55.602 -14.703 3.350   1.00 12.28 ?  62  GLN   B N    1 
ATOM   4846 C  CA   . GLN   B 1 62  ? 55.498 -14.760 4.805   1.00 12.74 ?  62  GLN   B CA   1 
ATOM   4847 C  C    . GLN   B 1 62  ? 55.783 -13.405 5.439   1.00 12.77 ?  62  GLN   B C    1 
ATOM   4848 O  O    . GLN   B 1 62  ? 55.102 -13.007 6.390   1.00 13.47 ?  62  GLN   B O    1 
ATOM   4849 C  CB   . GLN   B 1 62  ? 56.451 -15.815 5.365   1.00 13.01 ?  62  GLN   B CB   1 
ATOM   4850 C  CG   . GLN   B 1 62  ? 56.231 -16.090 6.841   1.00 13.29 ?  62  GLN   B CG   1 
ATOM   4851 C  CD   . GLN   B 1 62  ? 54.855 -16.672 7.089   1.00 12.70 ?  62  GLN   B CD   1 
ATOM   4852 O  OE1  . GLN   B 1 62  ? 54.591 -17.825 6.740   1.00 13.34 ?  62  GLN   B OE1  1 
ATOM   4853 N  NE2  . GLN   B 1 62  ? 53.951 -15.870 7.649   1.00 13.32 ?  62  GLN   B NE2  1 
ATOM   4854 H  H    . GLN   B 1 62  ? 56.251 -15.158 3.007   1.00 14.70 ?  62  GLN   B H    1 
ATOM   4855 H  HA   . GLN   B 1 62  ? 54.593 -15.017 5.036   1.00 15.25 ?  62  GLN   B HA   1 
ATOM   4856 H  HB2  . GLN   B 1 62  ? 56.326 -16.646 4.882   1.00 15.58 ?  62  GLN   B HB2  1 
ATOM   4857 H  HB3  . GLN   B 1 62  ? 57.366 -15.503 5.252   1.00 15.58 ?  62  GLN   B HB3  1 
ATOM   4858 H  HG2  . GLN   B 1 62  ? 56.890 -16.731 7.146   1.00 15.92 ?  62  GLN   B HG2  1 
ATOM   4859 H  HG3  . GLN   B 1 62  ? 56.310 -15.262 7.338   1.00 15.92 ?  62  GLN   B HG3  1 
ATOM   4860 H  HE21 . GLN   B 1 62  ? 54.166 -15.064 7.867   1.00 15.95 ?  62  GLN   B HE21 1 
ATOM   4861 H  HE22 . GLN   B 1 62  ? 53.156 -16.157 7.798   1.00 15.95 ?  62  GLN   B HE22 1 
ATOM   4862 N  N    . VAL   B 1 63  ? 56.799 -12.695 4.949   1.00 13.45 ?  63  VAL   B N    1 
ATOM   4863 C  CA   . VAL   B 1 63  ? 57.107 -11.378 5.502   1.00 14.37 ?  63  VAL   B CA   1 
ATOM   4864 C  C    . VAL   B 1 63  ? 55.917 -10.441 5.321   1.00 13.53 ?  63  VAL   B C    1 
ATOM   4865 O  O    . VAL   B 1 63  ? 55.498 -9.744  6.257   1.00 14.57 ?  63  VAL   B O    1 
ATOM   4866 C  CB   . VAL   B 1 63  ? 58.402 -10.823 4.880   1.00 15.79 ?  63  VAL   B CB   1 
ATOM   4867 C  CG1  . VAL   B 1 63  ? 58.632 -9.380  5.311   1.00 16.45 ?  63  VAL   B CG1  1 
ATOM   4868 C  CG2  . VAL   B 1 63  ? 59.586 -11.692 5.283   1.00 16.57 ?  63  VAL   B CG2  1 
ATOM   4869 H  H    . VAL   B 1 63  ? 57.309 -12.947 4.301   1.00 16.11 ?  63  VAL   B H    1 
ATOM   4870 H  HA   . VAL   B 1 63  ? 57.261 -11.479 6.452   1.00 17.21 ?  63  VAL   B HA   1 
ATOM   4871 H  HB   . VAL   B 1 63  ? 58.332 -10.848 3.914   1.00 18.92 ?  63  VAL   B HB   1 
ATOM   4872 H  HG11 . VAL   B 1 63  ? 59.548 -9.137  5.114   1.00 19.71 ?  63  VAL   B HG11 1 
ATOM   4873 H  HG12 . VAL   B 1 63  ? 58.023 -8.806  4.824   1.00 19.71 ?  63  VAL   B HG12 1 
ATOM   4874 H  HG13 . VAL   B 1 63  ? 58.468 -9.309  6.265   1.00 19.71 ?  63  VAL   B HG13 1 
ATOM   4875 H  HG21 . VAL   B 1 63  ? 60.396 -11.323 4.899   1.00 19.86 ?  63  VAL   B HG21 1 
ATOM   4876 H  HG22 . VAL   B 1 63  ? 59.656 -11.700 6.254   1.00 19.86 ?  63  VAL   B HG22 1 
ATOM   4877 H  HG23 . VAL   B 1 63  ? 59.446 -12.595 4.957   1.00 19.86 ?  63  VAL   B HG23 1 
ATOM   4878 N  N    . GLU   B 1 64  ? 55.345 -10.425 4.116   1.00 13.24 ?  64  GLU   B N    1 
ATOM   4879 C  CA   . GLU   B 1 64  ? 54.177 -9.590  3.845   1.00 12.72 ?  64  GLU   B CA   1 
ATOM   4880 C  C    . GLU   B 1 64  ? 52.995 -9.993  4.720   1.00 12.56 ?  64  GLU   B C    1 
ATOM   4881 O  O    . GLU   B 1 64  ? 52.250 -9.135  5.225   1.00 13.17 ?  64  GLU   B O    1 
ATOM   4882 C  CB   . GLU   B 1 64  ? 53.811 -9.744  2.368   1.00 13.17 ?  64  GLU   B CB   1 
ATOM   4883 C  CG   . GLU   B 1 64  ? 52.555 -9.005  1.936   1.00 13.54 ?  64  GLU   B CG   1 
ATOM   4884 C  CD   . GLU   B 1 64  ? 52.018 -9.498  0.601   1.00 14.12 ?  64  GLU   B CD   1 
ATOM   4885 O  OE1  . GLU   B 1 64  ? 52.186 -10.707 0.282   1.00 15.10 ?  64  GLU   B OE1  1 
ATOM   4886 O  OE2  . GLU   B 1 64  ? 51.398 -8.684  -0.125  1.00 14.98 -1 64  GLU   B OE2  1 
ATOM   4887 H  H    . GLU   B 1 64  ? 55.620 -10.887 3.437   1.00 15.86 ?  64  GLU   B H    1 
ATOM   4888 H  HA   . GLU   B 1 64  ? 54.395 -8.661  4.018   1.00 15.23 ?  64  GLU   B HA   1 
ATOM   4889 H  HB2  . GLU   B 1 64  ? 54.544 -9.398  1.829   1.00 15.77 ?  64  GLU   B HB2  1 
ATOM   4890 H  HB3  . GLU   B 1 64  ? 53.680 -10.680 2.178   1.00 15.77 ?  64  GLU   B HB3  1 
ATOM   4891 H  HG2  . GLU   B 1 64  ? 51.854 -9.129  2.601   1.00 16.22 ?  64  GLU   B HG2  1 
ATOM   4892 H  HG3  . GLU   B 1 64  ? 52.755 -8.058  1.850   1.00 16.22 ?  64  GLU   B HG3  1 
ATOM   4893 N  N    . SER   B 1 65  ? 52.808 -11.301 4.898   1.00 12.42 ?  65  SER   B N    1 
ATOM   4894 C  CA   . SER   B 1 65  ? 51.702 -11.811 5.700   1.00 12.31 ?  65  SER   B CA   1 
ATOM   4895 C  C    . SER   B 1 65  ? 51.837 -11.409 7.162   1.00 12.48 ?  65  SER   B C    1 
ATOM   4896 O  O    . SER   B 1 65  ? 50.840 -11.039 7.800   1.00 12.96 ?  65  SER   B O    1 
ATOM   4897 C  CB   . SER   B 1 65  ? 51.629 -13.330 5.571   1.00 12.33 ?  65  SER   B CB   1 
ATOM   4898 O  OG   . SER   B 1 65  ? 51.264 -13.722 4.256   1.00 12.79 ?  65  SER   B OG   1 
ATOM   4899 H  H    . SER   B 1 65  ? 53.312 -11.920 4.566   1.00 14.87 ?  65  SER   B H    1 
ATOM   4900 H  HA   . SER   B 1 65  ? 50.871 -11.440 5.363   1.00 14.74 ?  65  SER   B HA   1 
ATOM   4901 H  HB2  . SER   B 1 65  ? 52.493 -13.708 5.782   1.00 14.77 ?  65  SER   B HB2  1 
ATOM   4902 H  HB3  . SER   B 1 65  ? 50.960 -13.665 6.192   1.00 14.77 ?  65  SER   B HB3  1 
ATOM   4903 H  HG   . SER   B 1 65  ? 51.831 -13.431 3.700   1.00 15.32 ?  65  SER   B HG   1 
ATOM   4904 N  N    . ASP   B 1 66  ? 53.048 -11.504 7.725   1.00 12.91 ?  66  ASP   B N    1 
ATOM   4905 C  CA   . ASP   B 1 66  ? 53.228 -11.119 9.123   1.00 13.19 ?  66  ASP   B CA   1 
ATOM   4906 C  C    . ASP   B 1 66  ? 52.916 -9.642  9.325   1.00 13.18 ?  66  ASP   B C    1 
ATOM   4907 O  O    . ASP   B 1 66  ? 52.345 -9.252  10.350  1.00 13.64 ?  66  ASP   B O    1 
ATOM   4908 C  CB   . ASP   B 1 66  ? 54.655 -11.429 9.583   1.00 14.38 ?  66  ASP   B CB   1 
ATOM   4909 C  CG   . ASP   B 1 66  ? 54.922 -12.923 9.736   1.00 16.42 ?  66  ASP   B CG   1 
ATOM   4910 O  OD1  . ASP   B 1 66  ? 53.974 -13.736 9.660   1.00 16.86 ?  66  ASP   B OD1  1 
ATOM   4911 O  OD2  . ASP   B 1 66  ? 56.101 -13.288 9.950   1.00 19.16 -1 66  ASP   B OD2  1 
ATOM   4912 H  H    . ASP   B 1 66  ? 53.756 -11.793 7.332   1.00 15.47 ?  66  ASP   B H    1 
ATOM   4913 H  HA   . ASP   B 1 66  ? 52.621 -11.627 9.678   1.00 15.80 ?  66  ASP   B HA   1 
ATOM   4914 H  HB2  . ASP   B 1 66  ? 55.283 -11.081 8.933   1.00 17.23 ?  66  ASP   B HB2  1 
ATOM   4915 H  HB3  . ASP   B 1 66  ? 54.806 -11.008 10.447  1.00 17.23 ?  66  ASP   B HB3  1 
ATOM   4916 N  N    . ASP   B 1 67  ? 53.290 -8.801  8.361   1.00 12.96 ?  67  ASP   B N    1 
ATOM   4917 C  CA   . ASP   B 1 67  ? 52.949 -7.387  8.454   1.00 13.65 ?  67  ASP   B CA   1 
ATOM   4918 C  C    . ASP   B 1 67  ? 51.438 -7.178  8.373   1.00 13.82 ?  67  ASP   B C    1 
ATOM   4919 O  O    . ASP   B 1 67  ? 50.876 -6.374  9.126   1.00 14.33 ?  67  ASP   B O    1 
ATOM   4920 C  CB   . ASP   B 1 67  ? 53.662 -6.621  7.350   1.00 15.22 ?  67  ASP   B CB   1 
ATOM   4921 C  CG   . ASP   B 1 67  ? 53.247 -5.173  7.308   1.00 16.55 ?  67  ASP   B CG   1 
ATOM   4922 O  OD1  . ASP   B 1 67  ? 53.741 -4.371  8.136   1.00 17.88 ?  67  ASP   B OD1  1 
ATOM   4923 O  OD2  . ASP   B 1 67  ? 52.390 -4.860  6.466   1.00 17.51 -1 67  ASP   B OD2  1 
ATOM   4924 H  H    . ASP   B 1 67  ? 53.741 -9.021  7.659   1.00 15.52 ?  67  ASP   B H    1 
ATOM   4925 H  HA   . ASP   B 1 67  ? 53.258 -7.042  9.304   1.00 16.35 ?  67  ASP   B HA   1 
ATOM   4926 H  HB2  . ASP   B 1 67  ? 54.622 -6.655  7.504   1.00 18.23 ?  67  ASP   B HB2  1 
ATOM   4927 H  HB3  . ASP   B 1 67  ? 53.457 -7.032  6.490   1.00 18.23 ?  67  ASP   B HB3  1 
ATOM   4928 N  N    . TYR   B 1 68  ? 50.758 -7.907  7.481   1.00 13.39 ?  68  TYR   B N    1 
ATOM   4929 C  CA   . TYR   B 1 68  ? 49.301 -7.829  7.409   1.00 14.09 ?  68  TYR   B CA   1 
ATOM   4930 C  C    . TYR   B 1 68  ? 48.665 -8.176  8.750   1.00 13.92 ?  68  TYR   B C    1 
ATOM   4931 O  O    . TYR   B 1 68  ? 47.734 -7.497  9.200   1.00 14.61 ?  68  TYR   B O    1 
ATOM   4932 C  CB   . TYR   B 1 68  ? 48.768 -8.766  6.317   1.00 14.85 ?  68  TYR   B CB   1 
ATOM   4933 C  CG   . TYR   B 1 68  ? 47.263 -8.918  6.373   1.00 15.86 ?  68  TYR   B CG   1 
ATOM   4934 C  CD1  . TYR   B 1 68  ? 46.672 -9.878  7.188   1.00 16.91 ?  68  TYR   B CD1  1 
ATOM   4935 C  CD2  . TYR   B 1 68  ? 46.437 -8.076  5.649   1.00 17.16 ?  68  TYR   B CD2  1 
ATOM   4936 C  CE1  . TYR   B 1 68  ? 45.306 -9.998  7.275   1.00 18.10 ?  68  TYR   B CE1  1 
ATOM   4937 C  CE2  . TYR   B 1 68  ? 45.056 -8.197  5.723   1.00 17.73 ?  68  TYR   B CE2  1 
ATOM   4938 C  CZ   . TYR   B 1 68  ? 44.509 -9.157  6.540   1.00 18.07 ?  68  TYR   B CZ   1 
ATOM   4939 O  OH   . TYR   B 1 68  ? 43.140 -9.269  6.628   1.00 18.96 ?  68  TYR   B OH   1 
ATOM   4940 H  H    . TYR   B 1 68  ? 51.115 -8.458  6.921   1.00 16.03 ?  68  TYR   B H    1 
ATOM   4941 H  HA   . TYR   B 1 68  ? 49.048 -6.924  7.183   1.00 16.88 ?  68  TYR   B HA   1 
ATOM   4942 H  HB2  . TYR   B 1 68  ? 48.996 -8.405  5.450   1.00 17.80 ?  68  TYR   B HB2  1 
ATOM   4943 H  HB3  . TYR   B 1 68  ? 49.161 -9.645  6.431   1.00 17.80 ?  68  TYR   B HB3  1 
ATOM   4944 H  HD1  . TYR   B 1 68  ? 47.209 -10.453 7.689   1.00 20.26 ?  68  TYR   B HD1  1 
ATOM   4945 H  HD2  . TYR   B 1 68  ? 46.814 -7.420  5.115   1.00 20.56 ?  68  TYR   B HD2  1 
ATOM   4946 H  HE1  . TYR   B 1 68  ? 44.921 -10.659 7.812   1.00 21.69 ?  68  TYR   B HE1  1 
ATOM   4947 H  HE2  . TYR   B 1 68  ? 44.506 -7.628  5.237   1.00 21.24 ?  68  TYR   B HE2  1 
ATOM   4948 H  HH   . TYR   B 1 68  ? 42.761 -8.712  6.117   1.00 22.73 ?  68  TYR   B HH   1 
ATOM   4949 N  N    . ILE   B 1 69  ? 49.143 -9.246  9.394   1.00 13.91 ?  69  ILE   B N    1 
ATOM   4950 C  CA   . ILE   B 1 69  ? 48.583 -9.671  10.673  1.00 14.46 ?  69  ILE   B CA   1 
ATOM   4951 C  C    . ILE   B 1 69  ? 48.841 -8.627  11.748  1.00 14.01 ?  69  ILE   B C    1 
ATOM   4952 O  O    . ILE   B 1 69  ? 47.977 -8.353  12.587  1.00 14.41 ?  69  ILE   B O    1 
ATOM   4953 C  CB   . ILE   B 1 69  ? 49.156 -11.047 11.067  1.00 14.95 ?  69  ILE   B CB   1 
ATOM   4954 C  CG1  . ILE   B 1 69  ? 48.629 -12.148 10.139  1.00 15.44 ?  69  ILE   B CG1  1 
ATOM   4955 C  CG2  . ILE   B 1 69  ? 48.860 -11.370 12.530  1.00 16.05 ?  69  ILE   B CG2  1 
ATOM   4956 C  CD1  . ILE   B 1 69  ? 47.155 -12.460 10.298  1.00 15.84 ?  69  ILE   B CD1  1 
ATOM   4957 H  H    . ILE   B 1 69  ? 49.786 -9.740  9.113   1.00 16.67 ?  69  ILE   B H    1 
ATOM   4958 H  HA   . ILE   B 1 69  ? 47.625 -9.767  10.581  1.00 17.33 ?  69  ILE   B HA   1 
ATOM   4959 H  HB   . ILE   B 1 69  ? 50.121 -11.008 10.964  1.00 17.91 ?  69  ILE   B HB   1 
ATOM   4960 H  HG12 . ILE   B 1 69  ? 48.777 -11.872 9.219   1.00 18.50 ?  69  ILE   B HG12 1 
ATOM   4961 H  HG13 . ILE   B 1 69  ? 49.127 -12.964 10.314  1.00 18.50 ?  69  ILE   B HG13 1 
ATOM   4962 H  HG21 . ILE   B 1 69  ? 49.002 -12.319 12.675  1.00 19.22 ?  69  ILE   B HG21 1 
ATOM   4963 H  HG22 . ILE   B 1 69  ? 49.459 -10.860 13.097  1.00 19.22 ?  69  ILE   B HG22 1 
ATOM   4964 H  HG23 . ILE   B 1 69  ? 47.939 -11.141 12.724  1.00 19.22 ?  69  ILE   B HG23 1 
ATOM   4965 H  HD11 . ILE   B 1 69  ? 46.917 -13.164 9.676   1.00 18.98 ?  69  ILE   B HD11 1 
ATOM   4966 H  HD12 . ILE   B 1 69  ? 46.990 -12.755 11.207  1.00 18.98 ?  69  ILE   B HD12 1 
ATOM   4967 H  HD13 . ILE   B 1 69  ? 46.639 -11.663 10.109  1.00 18.98 ?  69  ILE   B HD13 1 
ATOM   4968 N  N    . ALA   B 1 70  ? 50.035 -8.037  11.763  1.00 14.05 ?  70  ALA   B N    1 
ATOM   4969 C  CA   . ALA   B 1 70  ? 50.318 -7.010  12.759  1.00 13.72 ?  70  ALA   B CA   1 
ATOM   4970 C  C    . ALA   B 1 70  ? 49.326 -5.861  12.651  1.00 14.11 ?  70  ALA   B C    1 
ATOM   4971 O  O    . ALA   B 1 70  ? 48.880 -5.317  13.666  1.00 14.56 ?  70  ALA   B O    1 
ATOM   4972 C  CB   . ALA   B 1 70  ? 51.751 -6.508  12.599  1.00 14.44 ?  70  ALA   B CB   1 
ATOM   4973 H  H    . ALA   B 1 70  ? 50.675 -8.209  11.223  1.00 16.83 ?  70  ALA   B H    1 
ATOM   4974 H  HA   . ALA   B 1 70  ? 50.235 -7.393  13.645  1.00 16.43 ?  70  ALA   B HA   1 
ATOM   4975 H  HB1  . ALA   B 1 70  ? 51.937 -5.850  13.289  1.00 17.30 ?  70  ALA   B HB1  1 
ATOM   4976 H  HB2  . ALA   B 1 70  ? 52.362 -7.259  12.691  1.00 17.30 ?  70  ALA   B HB2  1 
ATOM   4977 H  HB3  . ALA   B 1 70  ? 51.854 -6.107  11.722  1.00 17.30 ?  70  ALA   B HB3  1 
ATOM   4978 N  N    . THR   B 1 71  ? 48.954 -5.493  11.428  1.00 14.83 ?  71  THR   B N    1 
ATOM   4979 C  CA   . THR   B 1 71  ? 48.062 -4.357  11.220  1.00 15.59 ?  71  THR   B CA   1 
ATOM   4980 C  C    . THR   B 1 71  ? 46.594 -4.721  11.427  1.00 16.05 ?  71  THR   B C    1 
ATOM   4981 O  O    . THR   B 1 71  ? 45.815 -3.904  11.937  1.00 17.61 ?  71  THR   B O    1 
ATOM   4982 C  CB   . THR   B 1 71  ? 48.282 -3.787  9.816   1.00 17.12 ?  71  THR   B CB   1 
ATOM   4983 O  OG1  . THR   B 1 71  ? 49.609 -3.258  9.719   1.00 19.28 ?  71  THR   B OG1  1 
ATOM   4984 C  CG2  . THR   B 1 71  ? 47.268 -2.696  9.493   1.00 18.28 ?  71  THR   B CG2  1 
ATOM   4985 H  H    . THR   B 1 71  ? 49.209 -5.879  10.704  1.00 17.76 ?  71  THR   B H    1 
ATOM   4986 H  HA   . THR   B 1 71  ? 48.285 -3.660  11.854  1.00 18.68 ?  71  THR   B HA   1 
ATOM   4987 H  HB   . THR   B 1 71  ? 48.184 -4.491  9.157   1.00 20.51 ?  71  THR   B HB   1 
ATOM   4988 H  HG1  . THR   B 1 71  ? 49.740 -2.926  8.955   1.00 23.11 ?  71  THR   B HG1  1 
ATOM   4989 H  HG21 . THR   B 1 71  ? 47.571 -2.171  8.733   1.00 21.90 ?  71  THR   B HG21 1 
ATOM   4990 H  HG22 . THR   B 1 71  ? 46.409 -3.089  9.279   1.00 21.90 ?  71  THR   B HG22 1 
ATOM   4991 H  HG23 . THR   B 1 71  ? 47.164 -2.104  10.256  1.00 21.90 ?  71  THR   B HG23 1 
ATOM   4992 N  N    . ASN   B 1 72  ? 46.199 -5.936  11.038  1.00 15.55 ?  72  ASN   B N    1 
ATOM   4993 C  CA   . ASN   B 1 72  ? 44.794 -6.294  10.908  1.00 16.19 ?  72  ASN   B CA   1 
ATOM   4994 C  C    . ASN   B 1 72  ? 44.321 -7.391  11.852  1.00 16.74 ?  72  ASN   B C    1 
ATOM   4995 O  O    . ASN   B 1 72  ? 43.104 -7.548  12.019  1.00 18.01 ?  72  ASN   B O    1 
ATOM   4996 C  CB   . ASN   B 1 72  ? 44.494 -6.726  9.464   1.00 17.28 ?  72  ASN   B CB   1 
ATOM   4997 C  CG   . ASN   B 1 72  ? 44.765 -5.623  8.471   1.00 18.37 ?  72  ASN   B CG   1 
ATOM   4998 O  OD1  . ASN   B 1 72  ? 45.782 -5.625  7.768   1.00 19.45 ?  72  ASN   B OD1  1 
ATOM   4999 N  ND2  . ASN   B 1 72  ? 43.877 -4.651  8.432   1.00 19.74 ?  72  ASN   B ND2  1 
ATOM   5000 H  H    . ASN   B 1 72  ? 46.738 -6.580  10.839  1.00 18.63 ?  72  ASN   B H    1 
ATOM   5001 H  HA   . ASN   B 1 72  ? 44.259 -5.507  11.091  1.00 19.40 ?  72  ASN   B HA   1 
ATOM   5002 H  HB2  . ASN   B 1 72  ? 45.060 -7.481  9.236   1.00 20.71 ?  72  ASN   B HB2  1 
ATOM   5003 H  HB3  . ASN   B 1 72  ? 43.561 -6.975  9.395   1.00 20.71 ?  72  ASN   B HB3  1 
ATOM   5004 H  HD21 . ASN   B 1 72  ? 43.977 -3.996  7.884   1.00 23.65 ?  72  ASN   B HD21 1 
ATOM   5005 H  HD22 . ASN   B 1 72  ? 43.178 -4.682  8.937   1.00 23.65 ?  72  ASN   B HD22 1 
ATOM   5006 N  N    . GLY   B 1 73  ? 45.224 -8.139  12.477  1.00 16.16 ?  73  GLY   B N    1 
ATOM   5007 C  CA   . GLY   B 1 73  ? 44.835 -9.284  13.263  1.00 15.49 ?  73  GLY   B CA   1 
ATOM   5008 C  C    . GLY   B 1 73  ? 44.468 -10.466 12.392  1.00 14.33 ?  73  GLY   B C    1 
ATOM   5009 O  O    . GLY   B 1 73  ? 44.454 -10.381 11.162  1.00 14.30 ?  73  GLY   B O    1 
ATOM   5010 H  H    . GLY   B 1 73  ? 46.074 -7.994  12.461  1.00 19.36 ?  73  GLY   B H    1 
ATOM   5011 H  HA2  . GLY   B 1 73  ? 45.569 -9.541  13.843  1.00 18.55 ?  73  GLY   B HA2  1 
ATOM   5012 H  HA3  . GLY   B 1 73  ? 44.072 -9.052  13.816  1.00 18.55 ?  73  GLY   B HA3  1 
ATOM   5013 N  N    . PRO   B 1 74  ? 44.159 -11.593 13.029  1.00 14.74 ?  74  PRO   B N    1 
ATOM   5014 C  CA   . PRO   B 1 74  ? 43.904 -12.826 12.282  1.00 14.25 ?  74  PRO   B CA   1 
ATOM   5015 C  C    . PRO   B 1 74  ? 42.604 -12.770 11.489  1.00 13.40 ?  74  PRO   B C    1 
ATOM   5016 O  O    . PRO   B 1 74  ? 41.663 -12.034 11.807  1.00 14.53 ?  74  PRO   B O    1 
ATOM   5017 C  CB   . PRO   B 1 74  ? 43.823 -13.887 13.387  1.00 15.54 ?  74  PRO   B CB   1 
ATOM   5018 C  CG   . PRO   B 1 74  ? 43.382 -13.138 14.593  1.00 16.99 ?  74  PRO   B CG   1 
ATOM   5019 C  CD   . PRO   B 1 74  ? 44.046 -11.795 14.483  1.00 16.09 ?  74  PRO   B CD   1 
ATOM   5020 H  HA   . PRO   B 1 74  ? 44.650 -13.023 11.687  1.00 17.07 ?  74  PRO   B HA   1 
ATOM   5021 H  HB2  . PRO   B 1 74  ? 43.173 -14.563 13.139  1.00 18.61 ?  74  PRO   B HB2  1 
ATOM   5022 H  HB3  . PRO   B 1 74  ? 44.698 -14.282 13.525  1.00 18.61 ?  74  PRO   B HB3  1 
ATOM   5023 H  HG2  . PRO   B 1 74  ? 42.415 -13.048 14.582  1.00 20.36 ?  74  PRO   B HG2  1 
ATOM   5024 H  HG3  . PRO   B 1 74  ? 43.675 -13.604 15.389  1.00 20.36 ?  74  PRO   B HG3  1 
ATOM   5025 H  HD2  . PRO   B 1 74  ? 43.485 -11.106 14.883  1.00 19.28 ?  74  PRO   B HD2  1 
ATOM   5026 H  HD3  . PRO   B 1 74  ? 44.925 -11.814 14.889  1.00 19.28 ?  74  PRO   B HD3  1 
ATOM   5027 N  N    . LEU   B 1 75  ? 42.574 -13.581 10.433  1.00 12.76 ?  75  LEU   B N    1 
ATOM   5028 C  CA   . LEU   B 1 75  ? 41.363 -13.808 9.663   1.00 12.73 ?  75  LEU   B CA   1 
ATOM   5029 C  C    . LEU   B 1 75  ? 40.389 -14.669 10.469  1.00 13.27 ?  75  LEU   B C    1 
ATOM   5030 O  O    . LEU   B 1 75  ? 40.730 -15.218 11.518  1.00 14.42 ?  75  LEU   B O    1 
ATOM   5031 C  CB   . LEU   B 1 75  ? 41.695 -14.519 8.349   1.00 13.02 ?  75  LEU   B CB   1 
ATOM   5032 C  CG   . LEU   B 1 75  ? 42.543 -13.766 7.318   1.00 14.91 ?  75  LEU   B CG   1 
ATOM   5033 C  CD1  . LEU   B 1 75  ? 42.733 -14.579 6.038   1.00 16.13 ?  75  LEU   B CD1  1 
ATOM   5034 C  CD2  . LEU   B 1 75  ? 41.956 -12.419 7.002   1.00 18.16 ?  75  LEU   B CD2  1 
ATOM   5035 H  H    . LEU   B 1 75  ? 43.257 -14.019 10.137  1.00 15.28 ?  75  LEU   B H    1 
ATOM   5036 H  HA   . LEU   B 1 75  ? 40.937 -12.962 9.462   1.00 15.24 ?  75  LEU   B HA   1 
ATOM   5037 H  HB2  . LEU   B 1 75  ? 42.172 -15.337 8.560   1.00 15.59 ?  75  LEU   B HB2  1 
ATOM   5038 H  HB3  . LEU   B 1 75  ? 40.860 -14.745 7.910   1.00 15.59 ?  75  LEU   B HB3  1 
ATOM   5039 H  HG   . LEU   B 1 75  ? 43.426 -13.620 7.694   1.00 17.86 ?  75  LEU   B HG   1 
ATOM   5040 H  HD11 . LEU   B 1 75  ? 43.282 -14.070 5.415   1.00 19.33 ?  75  LEU   B HD11 1 
ATOM   5041 H  HD12 . LEU   B 1 75  ? 43.176 -15.416 6.252   1.00 19.33 ?  75  LEU   B HD12 1 
ATOM   5042 H  HD13 . LEU   B 1 75  ? 41.867 -14.756 5.640   1.00 19.33 ?  75  LEU   B HD13 1 
ATOM   5043 H  HD21 . LEU   B 1 75  ? 42.451 -12.023 6.268   1.00 21.76 ?  75  LEU   B HD21 1 
ATOM   5044 H  HD22 . LEU   B 1 75  ? 41.027 -12.532 6.756   1.00 21.76 ?  75  LEU   B HD22 1 
ATOM   5045 H  HD23 . LEU   B 1 75  ? 42.026 -11.855 7.789   1.00 21.76 ?  75  LEU   B HD23 1 
ATOM   5046 N  N    . LYS   B 1 76  ? 39.155 -14.766 9.971   1.00 14.50 ?  76  LYS   B N    1 
ATOM   5047 C  CA   . LYS   B 1 76  ? 38.173 -15.726 10.456  1.00 15.97 ?  76  LYS   B CA   1 
ATOM   5048 C  C    . LYS   B 1 76  ? 38.258 -16.994 9.613   1.00 14.53 ?  76  LYS   B C    1 
ATOM   5049 O  O    . LYS   B 1 76  ? 38.524 -16.933 8.414   1.00 14.14 ?  76  LYS   B O    1 
ATOM   5050 C  CB   . LYS   B 1 76  ? 36.753 -15.158 10.288  1.00 18.18 ?  76  LYS   B CB   1 
ATOM   5051 C  CG   . LYS   B 1 76  ? 36.487 -13.757 10.870  1.00 20.32 ?  76  LYS   B CG   1 
ATOM   5052 C  CD   . LYS   B 1 76  ? 35.066 -13.248 10.539  1.00 21.59 ?  76  LYS   B CD   1 
ATOM   5053 C  CE   . LYS   B 1 76  ? 34.806 -11.868 11.135  1.00 23.72 ?  76  LYS   B CE   1 
ATOM   5054 N  NZ   . LYS   B 1 76  ? 33.503 -11.282 10.703  1.00 24.38 ?  76  LYS   B NZ   1 
ATOM   5055 H  H    . LYS   B 1 76  ? 38.864 -14.274 9.333   1.00 17.37 ?  76  LYS   B H    1 
ATOM   5056 H  HA   . LYS   B 1 76  ? 38.333 -15.945 11.389  1.00 19.14 ?  76  LYS   B HA   1 
ATOM   5057 H  HB2  . LYS   B 1 76  ? 36.558 -15.118 9.339   1.00 21.79 ?  76  LYS   B HB2  1 
ATOM   5058 H  HB3  . LYS   B 1 76  ? 36.133 -15.769 10.716  1.00 21.79 ?  76  LYS   B HB3  1 
ATOM   5059 H  HG2  . LYS   B 1 76  ? 36.582 -13.791 11.834  1.00 24.35 ?  76  LYS   B HG2  1 
ATOM   5060 H  HG3  . LYS   B 1 76  ? 37.129 -13.132 10.494  1.00 24.35 ?  76  LYS   B HG3  1 
ATOM   5061 H  HD2  . LYS   B 1 76  ? 34.967 -13.187 9.575   1.00 25.88 ?  76  LYS   B HD2  1 
ATOM   5062 H  HD3  . LYS   B 1 76  ? 34.415 -13.866 10.904  1.00 25.88 ?  76  LYS   B HD3  1 
ATOM   5063 H  HE2  . LYS   B 1 76  ? 34.797 -11.941 12.101  1.00 28.43 ?  76  LYS   B HE2  1 
ATOM   5064 H  HE3  . LYS   B 1 76  ? 35.514 -11.266 10.854  1.00 28.43 ?  76  LYS   B HE3  1 
ATOM   5065 H  HZ1  . LYS   B 1 76  ? 33.393 -10.478 11.074  1.00 29.22 ?  76  LYS   B HZ1  1 
ATOM   5066 H  HZ2  . LYS   B 1 76  ? 33.485 -11.194 9.817   1.00 29.22 ?  76  LYS   B HZ2  1 
ATOM   5067 H  HZ3  . LYS   B 1 76  ? 32.832 -11.809 10.955  1.00 29.22 ?  76  LYS   B HZ3  1 
ATOM   5068 N  N    . VAL   B 1 77  ? 38.012 -18.152 10.238  1.00 15.03 ?  77  VAL   B N    1 
ATOM   5069 C  CA   . VAL   B 1 77  ? 37.803 -19.359 9.447   1.00 15.01 ?  77  VAL   B CA   1 
ATOM   5070 C  C    . VAL   B 1 77  ? 36.611 -19.121 8.531   1.00 14.02 ?  77  VAL   B C    1 
ATOM   5071 O  O    . VAL   B 1 77  ? 35.543 -18.681 8.979   1.00 14.06 ?  77  VAL   B O    1 
ATOM   5072 C  CB   . VAL   B 1 77  ? 37.602 -20.585 10.351  1.00 16.55 ?  77  VAL   B CB   1 
ATOM   5073 C  CG1  . VAL   B 1 77  ? 37.323 -21.819 9.503   1.00 17.55 ?  77  VAL   B CG1  1 
ATOM   5074 C  CG2  . VAL   B 1 77  ? 38.830 -20.819 11.236  1.00 17.95 ?  77  VAL   B CG2  1 
ATOM   5075 H  H    . VAL   B 1 77  ? 37.965 -18.261 11.087  1.00 18.00 ?  77  VAL   B H    1 
ATOM   5076 H  HA   . VAL   B 1 77  ? 38.580 -19.519 8.891   1.00 17.99 ?  77  VAL   B HA   1 
ATOM   5077 H  HB   . VAL   B 1 77  ? 36.835 -20.437 10.927  1.00 19.84 ?  77  VAL   B HB   1 
ATOM   5078 H  HG11 . VAL   B 1 77  ? 37.379 -22.608 10.069  1.00 21.03 ?  77  VAL   B HG11 1 
ATOM   5079 H  HG12 . VAL   B 1 77  ? 36.430 -21.753 9.126   1.00 21.03 ?  77  VAL   B HG12 1 
ATOM   5080 H  HG13 . VAL   B 1 77  ? 37.980 -21.874 8.796   1.00 21.03 ?  77  VAL   B HG13 1 
ATOM   5081 H  HG21 . VAL   B 1 77  ? 38.686 -21.619 11.765  1.00 21.51 ?  77  VAL   B HG21 1 
ATOM   5082 H  HG22 . VAL   B 1 77  ? 39.606 -20.929 10.668  1.00 21.51 ?  77  VAL   B HG22 1 
ATOM   5083 H  HG23 . VAL   B 1 77  ? 38.945 -20.052 11.816  1.00 21.51 ?  77  VAL   B HG23 1 
ATOM   5084 N  N    . GLY   B 1 78  ? 36.790 -19.403 7.242   1.00 13.46 ?  78  GLY   B N    1 
ATOM   5085 C  CA   . GLY   B 1 78  ? 35.812 -19.074 6.232   1.00 13.03 ?  78  GLY   B CA   1 
ATOM   5086 C  C    . GLY   B 1 78  ? 36.057 -17.756 5.534   1.00 12.62 ?  78  GLY   B C    1 
ATOM   5087 O  O    . GLY   B 1 78  ? 35.377 -17.468 4.543   1.00 12.93 ?  78  GLY   B O    1 
ATOM   5088 H  H    . GLY   B 1 78  ? 37.492 -19.787 6.927   1.00 16.12 ?  78  GLY   B H    1 
ATOM   5089 H  HA2  . GLY   B 1 78  ? 35.803 -19.769 5.561   1.00 15.61 ?  78  GLY   B HA2  1 
ATOM   5090 H  HA3  . GLY   B 1 78  ? 34.934 -19.032 6.641   1.00 15.61 ?  78  GLY   B HA3  1 
ATOM   5091 N  N    . GLY   B 1 79  ? 37.005 -16.952 6.020   1.00 12.48 ?  79  GLY   B N    1 
ATOM   5092 C  CA   . GLY   B 1 79  ? 37.297 -15.656 5.443   1.00 12.29 ?  79  GLY   B CA   1 
ATOM   5093 C  C    . GLY   B 1 79  ? 38.536 -15.677 4.556   1.00 11.79 ?  79  GLY   B C    1 
ATOM   5094 O  O    . GLY   B 1 79  ? 39.154 -16.710 4.305   1.00 12.63 ?  79  GLY   B O    1 
ATOM   5095 H  H    . GLY   B 1 79  ? 37.507 -17.145 6.691   1.00 14.94 ?  79  GLY   B H    1 
ATOM   5096 H  HA2  . GLY   B 1 79  ? 36.544 -15.359 4.908   1.00 14.72 ?  79  GLY   B HA2  1 
ATOM   5097 H  HA3  . GLY   B 1 79  ? 37.442 -15.010 6.153   1.00 14.72 ?  79  GLY   B HA3  1 
ATOM   5098 N  N    . SER   B 1 80  ? 38.905 -14.484 4.084   1.00 12.00 ?  80  SER   B N    1 
ATOM   5099 C  CA   . SER   B 1 80  ? 40.018 -14.351 3.151   1.00 11.85 ?  80  SER   B CA   1 
ATOM   5100 C  C    . SER   B 1 80  ? 40.597 -12.942 3.206   1.00 11.84 ?  80  SER   B C    1 
ATOM   5101 O  O    . SER   B 1 80  ? 39.976 -12.006 3.715   1.00 12.95 ?  80  SER   B O    1 
ATOM   5102 C  CB   . SER   B 1 80  ? 39.570 -14.641 1.715   1.00 12.32 ?  80  SER   B CB   1 
ATOM   5103 O  OG   . SER   B 1 80  ? 38.729 -13.618 1.210   1.00 13.29 ?  80  SER   B OG   1 
ATOM   5104 H  H    . SER   B 1 80  ? 38.535 -13.739 4.296   1.00 14.37 ?  80  SER   B H    1 
ATOM   5105 H  HA   . SER   B 1 80  ? 40.712 -14.981 3.397   1.00 14.19 ?  80  SER   B HA   1 
ATOM   5106 H  HB2  . SER   B 1 80  ? 40.353 -14.705 1.149   1.00 14.76 ?  80  SER   B HB2  1 
ATOM   5107 H  HB3  . SER   B 1 80  ? 39.087 -15.484 1.705   1.00 14.76 ?  80  SER   B HB3  1 
ATOM   5108 H  HG   . SER   B 1 80  ? 38.033 -13.556 1.690   1.00 15.91 ?  80  SER   B HG   1 
ATOM   5109 N  N    . CYS   B 1 81  ? 41.785 -12.795 2.625   1.00 11.57 ?  81  CYS   B N    1 
ATOM   5110 C  CA   . CYS   B 1 81  ? 42.330 -11.482 2.307   1.00 11.43 ?  81  CYS   B CA   1 
ATOM   5111 C  C    . CYS   B 1 81  ? 43.097 -11.575 0.998   1.00 10.82 ?  81  CYS   B C    1 
ATOM   5112 O  O    . CYS   B 1 81  ? 43.606 -12.635 0.621   1.00 12.01 ?  81  CYS   B O    1 
ATOM   5113 C  CB   . CYS   B 1 81  ? 43.226 -10.930 3.427   1.00 12.59 ?  81  CYS   B CB   1 
ATOM   5114 S  SG   . CYS   B 1 81  ? 44.742 -11.864 3.680   1.00 12.94 ?  81  CYS   B SG   1 
ATOM   5115 H  H    . CYS   B 1 81  ? 42.297 -13.450 2.393   1.00 13.85 ?  81  CYS   B H    1 
ATOM   5116 H  HA   . CYS   B 1 81  ? 41.597 -10.860 2.182   1.00 13.68 ?  81  CYS   B HA   1 
ATOM   5117 H  HB2  . CYS   B 1 81  ? 43.478 -10.017 3.207   1.00 15.07 ?  81  CYS   B HB2  1 
ATOM   5118 H  HB3  . CYS   B 1 81  ? 42.726 -10.934 4.261   1.00 15.07 ?  81  CYS   B HB3  1 
ATOM   5119 H  HG   . CYS   B 1 81  ? 45.372 -11.364 4.581   1.00 15.49 ?  81  CYS   B HG   1 
ATOM   5120 N  N    . VAL   B 1 82  ? 43.207 -10.431 0.327   1.00 11.20 ?  82  VAL   B N    1 
ATOM   5121 C  CA   . VAL   B 1 82  ? 43.974 -10.304 -0.910  1.00 11.43 ?  82  VAL   B CA   1 
ATOM   5122 C  C    . VAL   B 1 82  ? 45.312 -9.660  -0.590  1.00 11.98 ?  82  VAL   B C    1 
ATOM   5123 O  O    . VAL   B 1 82  ? 45.361 -8.545  -0.054  1.00 13.01 ?  82  VAL   B O    1 
ATOM   5124 C  CB   . VAL   B 1 82  ? 43.228 -9.464  -1.956  1.00 12.56 ?  82  VAL   B CB   1 
ATOM   5125 C  CG1  . VAL   B 1 82  ? 44.075 -9.307  -3.218  1.00 13.68 ?  82  VAL   B CG1  1 
ATOM   5126 C  CG2  . VAL   B 1 82  ? 41.868 -10.061 -2.271  1.00 13.56 ?  82  VAL   B CG2  1 
ATOM   5127 H  H    . VAL   B 1 82  ? 42.834 -9.688  0.571   1.00 13.41 ?  82  VAL   B H    1 
ATOM   5128 H  HA   . VAL   B 1 82  ? 44.138 -11.181 -1.281  1.00 13.68 ?  82  VAL   B HA   1 
ATOM   5129 H  HB   . VAL   B 1 82  ? 43.080 -8.578  -1.599  1.00 15.04 ?  82  VAL   B HB   1 
ATOM   5130 H  HG11 . VAL   B 1 82  ? 43.513 -8.991  -3.942  1.00 16.38 ?  82  VAL   B HG11 1 
ATOM   5131 H  HG12 . VAL   B 1 82  ? 44.784 -8.663  -3.048  1.00 16.38 ?  82  VAL   B HG12 1 
ATOM   5132 H  HG13 . VAL   B 1 82  ? 44.461 -10.166 -3.451  1.00 16.38 ?  82  VAL   B HG13 1 
ATOM   5133 H  HG21 . VAL   B 1 82  ? 41.437 -9.532  -2.965  1.00 16.25 ?  82  VAL   B HG21 1 
ATOM   5134 H  HG22 . VAL   B 1 82  ? 41.981 -10.975 -2.583  1.00 16.25 ?  82  VAL   B HG22 1 
ATOM   5135 H  HG23 . VAL   B 1 82  ? 41.322 -10.054 -1.469  1.00 16.25 ?  82  VAL   B HG23 1 
ATOM   5136 N  N    . LEU   B 1 83  ? 46.393 -10.344 -0.957  1.00 11.13 ?  83  LEU   B N    1 
ATOM   5137 C  CA   . LEU   B 1 83  ? 47.749 -9.831  -0.831  1.00 11.13 ?  83  LEU   B CA   1 
ATOM   5138 C  C    . LEU   B 1 83  ? 48.450 -9.970  -2.183  1.00 11.22 ?  83  LEU   B C    1 
ATOM   5139 O  O    . LEU   B 1 83  ? 47.852 -10.384 -3.180  1.00 11.29 ?  83  LEU   B O    1 
ATOM   5140 C  CB   . LEU   B 1 83  ? 48.496 -10.509 0.326   1.00 11.79 ?  83  LEU   B CB   1 
ATOM   5141 C  CG   . LEU   B 1 83  ? 47.980 -10.143 1.722   1.00 13.18 ?  83  LEU   B CG   1 
ATOM   5142 C  CD1  . LEU   B 1 83  ? 48.596 -11.016 2.794   1.00 13.55 ?  83  LEU   B CD1  1 
ATOM   5143 C  CD2  . LEU   B 1 83  ? 48.197 -8.663  2.036   1.00 14.20 ?  83  LEU   B CD2  1 
ATOM   5144 H  H    . LEU   B 1 83  ? 46.358 -11.139 -1.289  1.00 13.32 ?  83  LEU   B H    1 
ATOM   5145 H  HA   . LEU   B 1 83  ? 47.697 -8.889  -0.633  1.00 13.33 ?  83  LEU   B HA   1 
ATOM   5146 H  HB2  . LEU   B 1 83  ? 48.422 -11.470 0.227   1.00 14.11 ?  83  LEU   B HB2  1 
ATOM   5147 H  HB3  . LEU   B 1 83  ? 49.431 -10.249 0.281   1.00 14.11 ?  83  LEU   B HB3  1 
ATOM   5148 H  HG   . LEU   B 1 83  ? 47.027 -10.301 1.739   1.00 15.79 ?  83  LEU   B HG   1 
ATOM   5149 H  HD11 . LEU   B 1 83  ? 48.233 -10.757 3.659   1.00 16.23 ?  83  LEU   B HD11 1 
ATOM   5150 H  HD12 . LEU   B 1 83  ? 48.370 -11.945 2.613   1.00 16.23 ?  83  LEU   B HD12 1 
ATOM   5151 H  HD13 . LEU   B 1 83  ? 49.556 -10.902 2.790   1.00 16.23 ?  83  LEU   B HD13 1 
ATOM   5152 H  HD21 . LEU   B 1 83  ? 48.003 -8.507  2.973   1.00 17.02 ?  83  LEU   B HD21 1 
ATOM   5153 H  HD22 . LEU   B 1 83  ? 49.119 -8.431  1.845   1.00 17.02 ?  83  LEU   B HD22 1 
ATOM   5154 H  HD23 . LEU   B 1 83  ? 47.602 -8.134  1.482   1.00 17.02 ?  83  LEU   B HD23 1 
ATOM   5155 N  N    . SER   B 1 84  ? 49.725 -9.600  -2.233  1.00 12.32 ?  84  SER   B N    1 
ATOM   5156 C  CA   . SER   B 1 84  ? 50.460 -9.711  -3.483  1.00 12.68 ?  84  SER   B CA   1 
ATOM   5157 C  C    . SER   B 1 84  ? 50.617 -11.171 -3.902  1.00 12.02 ?  84  SER   B C    1 
ATOM   5158 O  O    . SER   B 1 84  ? 50.728 -12.073 -3.073  1.00 11.68 ?  84  SER   B O    1 
ATOM   5159 C  CB   . SER   B 1 84  ? 51.850 -9.099  -3.338  1.00 14.50 ?  84  SER   B CB   1 
ATOM   5160 O  OG   . SER   B 1 84  ? 52.594 -9.314  -4.522  1.00 16.20 ?  84  SER   B OG   1 
ATOM   5161 H  H    . SER   B 1 84  ? 50.166 -9.271  -1.575  1.00 14.76 ?  84  SER   B H    1 
ATOM   5162 H  HA   . SER   B 1 84  ? 49.985 -9.241  -4.186  1.00 15.18 ?  84  SER   B HA   1 
ATOM   5163 H  HB2  . SER   B 1 84  ? 51.759 -8.143  -3.174  1.00 17.38 ?  84  SER   B HB2  1 
ATOM   5164 H  HB3  . SER   B 1 84  ? 52.310 -9.520  -2.598  1.00 17.38 ?  84  SER   B HB3  1 
ATOM   5165 H  HG   . SER   B 1 84  ? 53.358 -8.957  -4.453  1.00 19.41 ?  84  SER   B HG   1 
ATOM   5166 N  N    . GLY   B 1 85  ? 50.680 -11.385 -5.212  1.00 13.06 ?  85  GLY   B N    1 
ATOM   5167 C  CA   . GLY   B 1 85  ? 51.022 -12.675 -5.760  1.00 13.49 ?  85  GLY   B CA   1 
ATOM   5168 C  C    . GLY   B 1 85  ? 52.493 -12.873 -6.056  1.00 12.72 ?  85  GLY   B C    1 
ATOM   5169 O  O    . GLY   B 1 85  ? 52.873 -13.949 -6.518  1.00 13.05 ?  85  GLY   B O    1 
ATOM   5170 H  H    . GLY   B 1 85  ? 50.534 -10.787 -5.808  1.00 15.64 ?  85  GLY   B H    1 
ATOM   5171 H  HA2  . GLY   B 1 85  ? 50.751 -13.368 -5.136  1.00 16.16 ?  85  GLY   B HA2  1 
ATOM   5172 H  HA3  . GLY   B 1 85  ? 50.536 -12.810 -6.585  1.00 16.16 ?  85  GLY   B HA3  1 
ATOM   5173 N  N    . HIS   B 1 86  ? 53.348 -11.878 -5.826  1.00 12.59 ?  86  HIS   B N    1 
ATOM   5174 C  CA   . HIS   B 1 86  ? 54.812 -12.046 -5.913  1.00 12.71 ?  86  HIS   B CA   1 
ATOM   5175 C  C    . HIS   B 1 86  ? 55.180 -12.557 -7.305  1.00 12.61 ?  86  HIS   B C    1 
ATOM   5176 O  O    . HIS   B 1 86  ? 54.784 -11.940 -8.306  1.00 13.65 ?  86  HIS   B O    1 
ATOM   5177 C  CB   . HIS   B 1 86  ? 55.306 -12.889 -4.742  1.00 13.05 ?  86  HIS   B CB   1 
ATOM   5178 C  CG   . HIS   B 1 86  ? 54.991 -12.286 -3.417  1.00 13.40 ?  86  HIS   B CG   1 
ATOM   5179 N  ND1  . HIS   B 1 86  ? 55.820 -11.376 -2.798  1.00 14.52 ?  86  HIS   B ND1  1 
ATOM   5180 C  CD2  . HIS   B 1 86  ? 53.917 -12.435 -2.605  1.00 13.63 ?  86  HIS   B CD2  1 
ATOM   5181 C  CE1  . HIS   B 1 86  ? 55.267 -10.991 -1.662  1.00 14.45 ?  86  HIS   B CE1  1 
ATOM   5182 N  NE2  . HIS   B 1 86  ? 54.110 -11.614 -1.523  1.00 13.92 ?  86  HIS   B NE2  1 
ATOM   5183 H  H    . HIS   B 1 86  ? 53.107 -11.084 -5.612  1.00 15.07 ?  86  HIS   B H    1 
ATOM   5184 H  HA   . HIS   B 1 86  ? 55.218 -11.172 -5.818  1.00 15.22 ?  86  HIS   B HA   1 
ATOM   5185 H  HB2  . HIS   B 1 86  ? 54.897 -13.764 -4.780  1.00 15.63 ?  86  HIS   B HB2  1 
ATOM   5186 H  HB3  . HIS   B 1 86  ? 56.276 -12.975 -4.801  1.00 15.63 ?  86  HIS   B HB3  1 
ATOM   5187 H  HD2  . HIS   B 1 86  ? 53.176 -12.978 -2.763  1.00 16.32 ?  86  HIS   B HD2  1 
ATOM   5188 H  HE1  . HIS   B 1 86  ? 55.635 -10.395 -1.048  1.00 17.31 ?  86  HIS   B HE1  1 
ATOM   5189 H  HE2  . HIS   B 1 86  ? 53.572 -11.537 -0.854  1.00 16.68 ?  86  HIS   B HE2  1 
ATOM   5190 N  N    . ASN   B 1 87  ? 55.951 -13.636 -7.417  1.00 13.16 ?  87  ASN   B N    1 
ATOM   5191 C  CA   . ASN   B 1 87  ? 56.345 -14.205 -8.695  1.00 13.82 ?  87  ASN   B CA   1 
ATOM   5192 C  C    . ASN   B 1 87  ? 55.366 -15.256 -9.193  1.00 13.54 ?  87  ASN   B C    1 
ATOM   5193 O  O    . ASN   B 1 87  ? 55.685 -15.970 -10.150 1.00 15.43 ?  87  ASN   B O    1 
ATOM   5194 C  CB   . ASN   B 1 87  ? 57.741 -14.830 -8.580  1.00 15.74 ?  87  ASN   B CB   1 
ATOM   5195 C  CG   . ASN   B 1 87  ? 57.800 -15.950 -7.545  1.00 16.81 ?  87  ASN   B CG   1 
ATOM   5196 O  OD1  . ASN   B 1 87  ? 57.151 -15.882 -6.494  1.00 16.04 ?  87  ASN   B OD1  1 
ATOM   5197 N  ND2  . ASN   B 1 87  ? 58.558 -17.003 -7.853  1.00 19.10 ?  87  ASN   B ND2  1 
ATOM   5198 H  H    . ASN   B 1 87  ? 56.263 -14.071 -6.743  1.00 15.76 ?  87  ASN   B H    1 
ATOM   5199 H  HA   . ASN   B 1 87  ? 56.385 -13.495 -9.355  1.00 16.55 ?  87  ASN   B HA   1 
ATOM   5200 H  HB2  . ASN   B 1 87  ? 57.990 -15.200 -9.444  1.00 18.86 ?  87  ASN   B HB2  1 
ATOM   5201 H  HB3  . ASN   B 1 87  ? 58.372 -14.144 -8.319  1.00 18.86 ?  87  ASN   B HB3  1 
ATOM   5202 H  HD21 . ASN   B 1 87  ? 58.622 -17.659 -7.306  1.00 22.89 ?  87  ASN   B HD21 1 
ATOM   5203 H  HD22 . ASN   B 1 87  ? 58.991 -17.018 -8.599  1.00 22.89 ?  87  ASN   B HD22 1 
ATOM   5204 N  N    . LEU   B 1 88  ? 54.184 -15.356 -8.578  1.00 12.69 ?  88  LEU   B N    1 
ATOM   5205 C  CA   . LEU   B 1 88  ? 53.204 -16.386 -8.903  1.00 12.91 ?  88  LEU   B CA   1 
ATOM   5206 C  C    . LEU   B 1 88  ? 51.974 -15.868 -9.625  1.00 12.64 ?  88  LEU   B C    1 
ATOM   5207 O  O    . LEU   B 1 88  ? 51.374 -16.615 -10.406 1.00 14.29 ?  88  LEU   B O    1 
ATOM   5208 C  CB   . LEU   B 1 88  ? 52.730 -17.075 -7.620  1.00 13.72 ?  88  LEU   B CB   1 
ATOM   5209 C  CG   . LEU   B 1 88  ? 53.847 -17.740 -6.827  1.00 16.16 ?  88  LEU   B CG   1 
ATOM   5210 C  CD1  . LEU   B 1 88  ? 53.340 -18.126 -5.446  1.00 18.02 ?  88  LEU   B CD1  1 
ATOM   5211 C  CD2  . LEU   B 1 88  ? 54.352 -18.952 -7.585  1.00 19.39 ?  88  LEU   B CD2  1 
ATOM   5212 H  H    . LEU   B 1 88  ? 53.922 -14.822 -7.944  1.00 15.20 ?  88  LEU   B H    1 
ATOM   5213 H  HA   . LEU   B 1 88  ? 53.620 -17.046 -9.466  1.00 15.46 ?  88  LEU   B HA   1 
ATOM   5214 H  HB2  . LEU   B 1 88  ? 52.312 -16.419 -7.041  1.00 16.43 ?  88  LEU   B HB2  1 
ATOM   5215 H  HB3  . LEU   B 1 88  ? 52.087 -17.762 -7.854  1.00 16.43 ?  88  LEU   B HB3  1 
ATOM   5216 H  HG   . LEU   B 1 88  ? 54.581 -17.118 -6.719  1.00 19.36 ?  88  LEU   B HG   1 
ATOM   5217 H  HD11 . LEU   B 1 88  ? 53.989 -18.708 -5.022  1.00 21.60 ?  88  LEU   B HD11 1 
ATOM   5218 H  HD12 . LEU   B 1 88  ? 53.219 -17.322 -4.918  1.00 21.60 ?  88  LEU   B HD12 1 
ATOM   5219 H  HD13 . LEU   B 1 88  ? 52.493 -18.590 -5.542  1.00 21.60 ?  88  LEU   B HD13 1 
ATOM   5220 H  HD21 . LEU   B 1 88  ? 54.984 -19.429 -7.026  1.00 23.23 ?  88  LEU   B HD21 1 
ATOM   5221 H  HD22 . LEU   B 1 88  ? 53.601 -19.524 -7.801  1.00 23.23 ?  88  LEU   B HD22 1 
ATOM   5222 H  HD23 . LEU   B 1 88  ? 54.789 -18.655 -8.398  1.00 23.23 ?  88  LEU   B HD23 1 
ATOM   5223 N  N    . ALA   B 1 89  ? 51.561 -14.636 -9.352  1.00 12.00 ?  89  ALA   B N    1 
ATOM   5224 C  CA   . ALA   B 1 89  ? 50.266 -14.143 -9.797  1.00 11.74 ?  89  ALA   B CA   1 
ATOM   5225 C  C    . ALA   B 1 89  ? 50.242 -12.650 -9.522  1.00 12.02 ?  89  ALA   B C    1 
ATOM   5226 O  O    . ALA   B 1 89  ? 51.079 -12.131 -8.784  1.00 12.80 ?  89  ALA   B O    1 
ATOM   5227 C  CB   . ALA   B 1 89  ? 49.130 -14.821 -9.033  1.00 11.86 ?  89  ALA   B CB   1 
ATOM   5228 H  H    . ALA   B 1 89  ? 52.009 -14.054 -8.897  1.00 14.37 ?  89  ALA   B H    1 
ATOM   5229 H  HA   . ALA   B 1 89  ? 50.152 -14.294 -10.749 1.00 14.06 ?  89  ALA   B HA   1 
ATOM   5230 H  HB1  . ALA   B 1 89  ? 48.280 -14.492 -9.371  1.00 14.20 ?  89  ALA   B HB1  1 
ATOM   5231 H  HB2  . ALA   B 1 89  ? 49.189 -15.781 -9.177  1.00 14.20 ?  89  ALA   B HB2  1 
ATOM   5232 H  HB3  . ALA   B 1 89  ? 49.217 -14.620 -8.094  1.00 14.20 ?  89  ALA   B HB3  1 
ATOM   5233 N  N    . LYS   B 1 90  ? 49.245 -11.963 -10.077 1.00 12.80 ?  90  LYS   B N    1 
ATOM   5234 C  CA   . LYS   B 1 90  ? 49.052 -10.574 -9.679  1.00 12.90 ?  90  LYS   B CA   1 
ATOM   5235 C  C    . LYS   B 1 90  ? 48.735 -10.496 -8.191  1.00 12.85 ?  90  LYS   B C    1 
ATOM   5236 O  O    . LYS   B 1 90  ? 49.381 -9.749  -7.442  1.00 14.06 ?  90  LYS   B O    1 
ATOM   5237 C  CB   . LYS   B 1 90  ? 47.971 -9.916  -10.536 1.00 14.66 ?  90  LYS   B CB   1 
ATOM   5238 C  CG   . LYS   B 1 90  ? 47.679 -8.466  -10.168 1.00 15.35 ?  90  LYS   B CG   1 
ATOM   5239 C  CD   . LYS   B 1 90  ? 48.896 -7.583  -10.246 1.00 18.54 ?  90  LYS   B CD   1 
ATOM   5240 C  CE   . LYS   B 1 90  ? 48.477 -6.148  -9.999  1.00 20.88 ?  90  LYS   B CE   1 
ATOM   5241 N  NZ   . LYS   B 1 90  ? 49.645 -5.243  -9.871  1.00 20.90 ?  90  LYS   B NZ   1 
ATOM   5242 H  H    . LYS   B 1 90  ? 48.687 -12.268 -10.657 1.00 15.34 ?  90  LYS   B H    1 
ATOM   5243 H  HA   . LYS   B 1 90  ? 49.876 -10.096 -9.827  1.00 15.45 ?  90  LYS   B HA   1 
ATOM   5244 H  HB2  . LYS   B 1 90  ? 48.260 -9.931  -11.466 1.00 17.56 ?  90  LYS   B HB2  1 
ATOM   5245 H  HB3  . LYS   B 1 90  ? 47.145 -10.419 -10.449 1.00 17.56 ?  90  LYS   B HB3  1 
ATOM   5246 H  HG2  . LYS   B 1 90  ? 47.012 -8.114  -10.780 1.00 18.39 ?  90  LYS   B HG2  1 
ATOM   5247 H  HG3  . LYS   B 1 90  ? 47.337 -8.433  -9.259  1.00 18.39 ?  90  LYS   B HG3  1 
ATOM   5248 H  HD2  . LYS   B 1 90  ? 49.535 -7.839  -9.562  1.00 22.22 ?  90  LYS   B HD2  1 
ATOM   5249 H  HD3  . LYS   B 1 90  ? 49.293 -7.645  -11.128 1.00 22.22 ?  90  LYS   B HD3  1 
ATOM   5250 H  HE2  . LYS   B 1 90  ? 47.941 -5.834  -10.746 1.00 25.03 ?  90  LYS   B HE2  1 
ATOM   5251 H  HE3  . LYS   B 1 90  ? 47.968 -6.093  -9.177  1.00 25.03 ?  90  LYS   B HE3  1 
ATOM   5252 H  HZ1  . LYS   B 1 90  ? 49.376 -4.404  -9.729  1.00 25.05 ?  90  LYS   B HZ1  1 
ATOM   5253 H  HZ2  . LYS   B 1 90  ? 50.159 -5.497  -9.189  1.00 25.05 ?  90  LYS   B HZ2  1 
ATOM   5254 H  HZ3  . LYS   B 1 90  ? 50.134 -5.261  -10.619 1.00 25.05 ?  90  LYS   B HZ3  1 
ATOM   5255 N  N    . HIS   B 1 91  ? 47.780 -11.309 -7.741  1.00 11.32 ?  91  HIS   B N    1 
ATOM   5256 C  CA   . HIS   B 1 91  ? 47.324 -11.330 -6.365  1.00 11.73 ?  91  HIS   B CA   1 
ATOM   5257 C  C    . HIS   B 1 91  ? 47.323 -12.759 -5.845  1.00 10.89 ?  91  HIS   B C    1 
ATOM   5258 O  O    . HIS   B 1 91  ? 47.086 -13.715 -6.596  1.00 11.43 ?  91  HIS   B O    1 
ATOM   5259 C  CB   . HIS   B 1 91  ? 45.872 -10.856 -6.251  1.00 13.29 ?  91  HIS   B CB   1 
ATOM   5260 C  CG   . HIS   B 1 91  ? 45.651 -9.453  -6.702  1.00 16.79 ?  91  HIS   B CG   1 
ATOM   5261 N  ND1  . HIS   B 1 91  ? 46.233 -8.365  -6.086  1.00 19.50 ?  91  HIS   B ND1  1 
ATOM   5262 C  CD2  . HIS   B 1 91  ? 44.882 -8.957  -7.695  1.00 19.02 ?  91  HIS   B CD2  1 
ATOM   5263 C  CE1  . HIS   B 1 91  ? 45.845 -7.257  -6.694  1.00 20.18 ?  91  HIS   B CE1  1 
ATOM   5264 N  NE2  . HIS   B 1 91  ? 45.018 -7.590  -7.670  1.00 20.50 ?  91  HIS   B NE2  1 
ATOM   5265 H  H    . HIS   B 1 91  ? 47.364 -11.882 -8.234  1.00 13.56 ?  91  HIS   B H    1 
ATOM   5266 H  HA   . HIS   B 1 91  ? 47.894 -10.774 -5.802  1.00 14.04 ?  91  HIS   B HA   1 
ATOM   5267 H  HB2  . HIS   B 1 91  ? 45.315 -11.434 -6.791  1.00 15.92 ?  91  HIS   B HB2  1 
ATOM   5268 H  HB3  . HIS   B 1 91  ? 45.598 -10.915 -5.319  1.00 15.92 ?  91  HIS   B HB3  1 
ATOM   5269 H  HD1  . HIS   B 1 91  ? 46.769 -8.402  -5.414  1.00 23.37 ?  91  HIS   B HD1  1 
ATOM   5270 H  HD2  . HIS   B 1 91  ? 44.363 -9.443  -8.290  1.00 22.80 ?  91  HIS   B HD2  1 
ATOM   5271 H  HE1  . HIS   B 1 91  ? 46.105 -6.392  -6.464  1.00 24.18 ?  91  HIS   B HE1  1 
ATOM   5272 N  N    . CYS   B 1 92  ? 47.519 -12.893 -4.540  1.00 10.79 ?  92  CYS   B N    1 
ATOM   5273 C  CA   . CYS   B 1 92  ? 47.219 -14.129 -3.831  1.00 10.62 ?  92  CYS   B CA   1 
ATOM   5274 C  C    . CYS   B 1 92  ? 45.994 -13.897 -2.956  1.00 10.12 ?  92  CYS   B C    1 
ATOM   5275 O  O    . CYS   B 1 92  ? 45.993 -13.003 -2.102  1.00 11.12 ?  92  CYS   B O    1 
ATOM   5276 C  CB   . CYS   B 1 92  ? 48.394 -14.576 -2.969  1.00 11.15 ?  92  CYS   B CB   1 
ATOM   5277 S  SG   . CYS   B 1 92  ? 48.037 -16.130 -2.089  1.00 11.26 ?  92  CYS   B SG   1 
ATOM   5278 H  H    . CYS   B 1 92  ? 47.849 -12.275 -4.032  1.00 12.92 ?  92  CYS   B H    1 
ATOM   5279 H  HA   . CYS   B 1 92  ? 47.023 -14.829 -4.473  1.00 12.72 ?  92  CYS   B HA   1 
ATOM   5280 H  HB2  . CYS   B 1 92  ? 49.168 -14.713 -3.531  1.00 13.35 ?  92  CYS   B HB2  1 
ATOM   5281 H  HB3  . CYS   B 1 92  ? 48.576 -13.887 -2.307  1.00 13.35 ?  92  CYS   B HB3  1 
ATOM   5282 H  HG   . CYS   B 1 92  ? 48.999 -16.444 -1.449  1.00 13.48 ?  92  CYS   B HG   1 
ATOM   5283 N  N    . LEU   B 1 93  ? 44.961 -14.706 -3.168  1.00 10.04 ?  93  LEU   B N    1 
ATOM   5284 C  CA   . LEU   B 1 93  ? 43.785 -14.721 -2.308  1.00 10.43 ?  93  LEU   B CA   1 
ATOM   5285 C  C    . LEU   B 1 93  ? 44.009 -15.784 -1.239  1.00 9.99  ?  93  LEU   B C    1 
ATOM   5286 O  O    . LEU   B 1 93  ? 43.961 -16.986 -1.527  1.00 10.54 ?  93  LEU   B O    1 
ATOM   5287 C  CB   . LEU   B 1 93  ? 42.520 -15.009 -3.115  1.00 11.06 ?  93  LEU   B CB   1 
ATOM   5288 C  CG   . LEU   B 1 93  ? 41.216 -15.026 -2.307  1.00 11.64 ?  93  LEU   B CG   1 
ATOM   5289 C  CD1  . LEU   B 1 93  ? 40.863 -13.636 -1.810  1.00 11.87 ?  93  LEU   B CD1  1 
ATOM   5290 C  CD2  . LEU   B 1 93  ? 40.087 -15.617 -3.132  1.00 11.88 ?  93  LEU   B CD2  1 
ATOM   5291 H  H    . LEU   B 1 93  ? 44.927 -15.285 -3.813  1.00 12.02 ?  93  LEU   B H    1 
ATOM   5292 H  HA   . LEU   B 1 93  ? 43.693 -13.859 -1.878  1.00 12.48 ?  93  LEU   B HA   1 
ATOM   5293 H  HB2  . LEU   B 1 93  ? 42.430 -14.317 -3.795  1.00 13.24 ?  93  LEU   B HB2  1 
ATOM   5294 H  HB3  . LEU   B 1 93  ? 42.615 -15.870 -3.542  1.00 13.24 ?  93  LEU   B HB3  1 
ATOM   5295 H  HG   . LEU   B 1 93  ? 41.340 -15.594 -1.533  1.00 13.93 ?  93  LEU   B HG   1 
ATOM   5296 H  HD11 . LEU   B 1 93  ? 40.014 -13.673 -1.352  1.00 14.21 ?  93  LEU   B HD11 1 
ATOM   5297 H  HD12 . LEU   B 1 93  ? 41.558 -13.333 -1.205  1.00 14.21 ?  93  LEU   B HD12 1 
ATOM   5298 H  HD13 . LEU   B 1 93  ? 40.805 -13.036 -2.573  1.00 14.21 ?  93  LEU   B HD13 1 
ATOM   5299 H  HD21 . LEU   B 1 93  ? 39.275 -15.618 -2.603  1.00 14.23 ?  93  LEU   B HD21 1 
ATOM   5300 H  HD22 . LEU   B 1 93  ? 39.962 -15.082 -3.931  1.00 14.23 ?  93  LEU   B HD22 1 
ATOM   5301 H  HD23 . LEU   B 1 93  ? 40.319 -16.529 -3.381  1.00 14.23 ?  93  LEU   B HD23 1 
ATOM   5302 N  N    . HIS   B 1 94  ? 44.287 -15.345 -0.019  1.00 9.83  ?  94  HIS   B N    1 
ATOM   5303 C  CA   . HIS   B 1 94  ? 44.501 -16.250 1.103   1.00 10.24 ?  94  HIS   B CA   1 
ATOM   5304 C  C    . HIS   B 1 94  ? 43.138 -16.605 1.677   1.00 10.74 ?  94  HIS   B C    1 
ATOM   5305 O  O    . HIS   B 1 94  ? 42.472 -15.733 2.240   1.00 11.87 ?  94  HIS   B O    1 
ATOM   5306 C  CB   . HIS   B 1 94  ? 45.372 -15.573 2.160   1.00 10.74 ?  94  HIS   B CB   1 
ATOM   5307 C  CG   . HIS   B 1 94  ? 46.758 -15.268 1.690   1.00 10.77 ?  94  HIS   B CG   1 
ATOM   5308 N  ND1  . HIS   B 1 94  ? 47.783 -16.185 1.775   1.00 10.88 ?  94  HIS   B ND1  1 
ATOM   5309 C  CD2  . HIS   B 1 94  ? 47.269 -14.161 1.096   1.00 11.02 ?  94  HIS   B CD2  1 
ATOM   5310 C  CE1  . HIS   B 1 94  ? 48.874 -15.638 1.268   1.00 10.84 ?  94  HIS   B CE1  1 
ATOM   5311 N  NE2  . HIS   B 1 94  ? 48.593 -14.415 0.849   1.00 11.11 ?  94  HIS   B NE2  1 
ATOM   5312 H  H    . HIS   B 1 94  ? 44.367 -14.511 0.185   1.00 11.77 ?  94  HIS   B H    1 
ATOM   5313 H  HA   . HIS   B 1 94  ? 44.938 -17.060 0.797   1.00 12.26 ?  94  HIS   B HA   1 
ATOM   5314 H  HB2  . HIS   B 1 94  ? 44.957 -14.736 2.413   1.00 12.86 ?  94  HIS   B HB2  1 
ATOM   5315 H  HB3  . HIS   B 1 94  ? 45.439 -16.158 2.926   1.00 12.86 ?  94  HIS   B HB3  1 
ATOM   5316 H  HD2  . HIS   B 1 94  ? 46.814 -13.381 0.900   1.00 13.19 ?  94  HIS   B HD2  1 
ATOM   5317 H  HE1  . HIS   B 1 94  ? 49.706 -16.056 1.212   1.00 12.98 ?  94  HIS   B HE1  1 
ATOM   5318 H  HE2  . HIS   B 1 94  ? 49.151 -13.876 0.484   1.00 13.30 ?  94  HIS   B HE2  1 
ATOM   5319 N  N    . VAL   B 1 95  ? 42.707 -17.862 1.528   1.00 10.62 ?  95  VAL   B N    1 
ATOM   5320 C  CA   . VAL   B 1 95  ? 41.381 -18.303 1.961   1.00 10.69 ?  95  VAL   B CA   1 
ATOM   5321 C  C    . VAL   B 1 95  ? 41.552 -19.339 3.058   1.00 10.86 ?  95  VAL   B C    1 
ATOM   5322 O  O    . VAL   B 1 95  ? 42.326 -20.289 2.896   1.00 11.48 ?  95  VAL   B O    1 
ATOM   5323 C  CB   . VAL   B 1 95  ? 40.562 -18.906 0.804   1.00 10.87 ?  95  VAL   B CB   1 
ATOM   5324 C  CG1  . VAL   B 1 95  ? 39.179 -19.351 1.287   1.00 11.94 ?  95  VAL   B CG1  1 
ATOM   5325 C  CG2  . VAL   B 1 95  ? 40.435 -17.929 -0.342  1.00 11.10 ?  95  VAL   B CG2  1 
ATOM   5326 H  H    . VAL   B 1 95  ? 43.169 -18.490 1.164   1.00 12.71 ?  95  VAL   B H    1 
ATOM   5327 H  HA   . VAL   B 1 95  ? 40.885 -17.551 2.322   1.00 12.79 ?  95  VAL   B HA   1 
ATOM   5328 H  HB   . VAL   B 1 95  ? 41.020 -19.690 0.469   1.00 13.01 ?  95  VAL   B HB   1 
ATOM   5329 H  HG11 . VAL   B 1 95  ? 38.619 -19.548 0.515   1.00 14.30 ?  95  VAL   B HG11 1 
ATOM   5330 H  HG12 . VAL   B 1 95  ? 39.269 -20.145 1.835   1.00 14.30 ?  95  VAL   B HG12 1 
ATOM   5331 H  HG13 . VAL   B 1 95  ? 38.775 -18.634 1.804   1.00 14.30 ?  95  VAL   B HG13 1 
ATOM   5332 H  HG21 . VAL   B 1 95  ? 39.863 -18.322 -1.025  1.00 13.29 ?  95  VAL   B HG21 1 
ATOM   5333 H  HG22 . VAL   B 1 95  ? 40.035 -17.110 -0.012  1.00 13.29 ?  95  VAL   B HG22 1 
ATOM   5334 H  HG23 . VAL   B 1 95  ? 41.312 -17.755 -0.703  1.00 13.29 ?  95  VAL   B HG23 1 
ATOM   5335 N  N    . VAL   B 1 96  ? 40.822 -19.169 4.157   1.00 11.41 ?  96  VAL   B N    1 
ATOM   5336 C  CA   . VAL   B 1 96  ? 40.903 -20.082 5.297   1.00 11.51 ?  96  VAL   B CA   1 
ATOM   5337 C  C    . VAL   B 1 96  ? 39.715 -21.041 5.247   1.00 12.12 ?  96  VAL   B C    1 
ATOM   5338 O  O    . VAL   B 1 96  ? 38.594 -20.685 5.625   1.00 12.85 ?  96  VAL   B O    1 
ATOM   5339 C  CB   . VAL   B 1 96  ? 40.949 -19.331 6.631   1.00 12.39 ?  96  VAL   B CB   1 
ATOM   5340 C  CG1  . VAL   B 1 96  ? 41.130 -20.320 7.774   1.00 13.32 ?  96  VAL   B CG1  1 
ATOM   5341 C  CG2  . VAL   B 1 96  ? 42.059 -18.295 6.636   1.00 13.25 ?  96  VAL   B CG2  1 
ATOM   5342 H  H    . VAL   B 1 96  ? 40.259 -18.529 4.269   1.00 13.67 ?  96  VAL   B H    1 
ATOM   5343 H  HA   . VAL   B 1 96  ? 41.718 -20.607 5.225   1.00 13.79 ?  96  VAL   B HA   1 
ATOM   5344 H  HB   . VAL   B 1 96  ? 40.105 -18.873 6.767   1.00 14.84 ?  96  VAL   B HB   1 
ATOM   5345 H  HG11 . VAL   B 1 96  ? 41.318 -19.830 8.592   1.00 15.95 ?  96  VAL   B HG11 1 
ATOM   5346 H  HG12 . VAL   B 1 96  ? 40.319 -20.840 7.883   1.00 15.95 ?  96  VAL   B HG12 1 
ATOM   5347 H  HG13 . VAL   B 1 96  ? 41.876 -20.909 7.570   1.00 15.95 ?  96  VAL   B HG13 1 
ATOM   5348 H  HG21 . VAL   B 1 96  ? 42.107 -17.883 7.516   1.00 15.87 ?  96  VAL   B HG21 1 
ATOM   5349 H  HG22 . VAL   B 1 96  ? 42.900 -18.725 6.427   1.00 15.87 ?  96  VAL   B HG22 1 
ATOM   5350 H  HG23 . VAL   B 1 96  ? 41.861 -17.614 5.970   1.00 15.87 ?  96  VAL   B HG23 1 
ATOM   5351 N  N    . GLY   B 1 97  ? 39.950 -22.275 4.811   1.00 11.96 ?  97  GLY   B N    1 
ATOM   5352 C  CA   . GLY   B 1 97  ? 38.969 -23.328 4.969   1.00 12.81 ?  97  GLY   B CA   1 
ATOM   5353 C  C    . GLY   B 1 97  ? 39.094 -23.948 6.344   1.00 13.57 ?  97  GLY   B C    1 
ATOM   5354 O  O    . GLY   B 1 97  ? 40.132 -23.824 7.005   1.00 14.15 ?  97  GLY   B O    1 
ATOM   5355 H  H    . GLY   B 1 97  ? 40.680 -22.525 4.423   1.00 14.32 ?  97  GLY   B H    1 
ATOM   5356 H  HA2  . GLY   B 1 97  ? 38.077 -22.953 4.857   1.00 15.34 ?  97  GLY   B HA2  1 
ATOM   5357 H  HA3  . GLY   B 1 97  ? 39.106 -24.009 4.290   1.00 15.34 ?  97  GLY   B HA3  1 
ATOM   5358 N  N    . PRO   B 1 98  ? 38.045 -24.630 6.806   1.00 14.54 ?  98  PRO   B N    1 
ATOM   5359 C  CA   . PRO   B 1 98  ? 38.136 -25.323 8.094   1.00 15.11 ?  98  PRO   B CA   1 
ATOM   5360 C  C    . PRO   B 1 98  ? 39.162 -26.446 8.054   1.00 14.83 ?  98  PRO   B C    1 
ATOM   5361 O  O    . PRO   B 1 98  ? 39.270 -27.185 7.075   1.00 15.35 ?  98  PRO   B O    1 
ATOM   5362 C  CB   . PRO   B 1 98  ? 36.718 -25.866 8.299   1.00 15.24 ?  98  PRO   B CB   1 
ATOM   5363 C  CG   . PRO   B 1 98  ? 36.163 -26.004 6.922   1.00 14.94 ?  98  PRO   B CG   1 
ATOM   5364 C  CD   . PRO   B 1 98  ? 36.728 -24.825 6.171   1.00 14.42 ?  98  PRO   B CD   1 
ATOM   5365 H  HA   . PRO   B 1 98  ? 38.362 -24.698 8.797   1.00 18.10 ?  98  PRO   B HA   1 
ATOM   5366 H  HB2  . PRO   B 1 98  ? 36.763 -26.731 8.740   1.00 18.26 ?  98  PRO   B HB2  1 
ATOM   5367 H  HB3  . PRO   B 1 98  ? 36.200 -25.238 8.819   1.00 18.26 ?  98  PRO   B HB3  1 
ATOM   5368 H  HG2  . PRO   B 1 98  ? 36.463 -26.841 6.528   1.00 17.90 ?  98  PRO   B HG2  1 
ATOM   5369 H  HG3  . PRO   B 1 98  ? 35.196 -25.965 6.953   1.00 17.90 ?  98  PRO   B HG3  1 
ATOM   5370 H  HD2  . PRO   B 1 98  ? 36.825 -25.039 5.227   1.00 17.27 ?  98  PRO   B HD2  1 
ATOM   5371 H  HD3  . PRO   B 1 98  ? 36.174 -24.041 6.301   1.00 17.27 ?  98  PRO   B HD3  1 
ATOM   5372 N  N    . ASN   B 1 99  ? 39.918 -26.568 9.136   1.00 15.71 ?  99  ASN   B N    1 
ATOM   5373 C  CA   . ASN   B 1 99  ? 40.894 -27.643 9.302   1.00 16.53 ?  99  ASN   B CA   1 
ATOM   5374 C  C    . ASN   B 1 99  ? 40.260 -28.727 10.172  1.00 19.18 ?  99  ASN   B C    1 
ATOM   5375 O  O    . ASN   B 1 99  ? 40.177 -28.587 11.394  1.00 19.97 ?  99  ASN   B O    1 
ATOM   5376 C  CB   . ASN   B 1 99  ? 42.167 -27.089 9.926   1.00 17.20 ?  99  ASN   B CB   1 
ATOM   5377 C  CG   . ASN   B 1 99  ? 43.297 -28.094 9.930   1.00 18.06 ?  99  ASN   B CG   1 
ATOM   5378 O  OD1  . ASN   B 1 99  ? 43.069 -29.285 10.095  1.00 18.87 ?  99  ASN   B OD1  1 
ATOM   5379 N  ND2  . ASN   B 1 99  ? 44.518 -27.619 9.741   1.00 18.01 ?  99  ASN   B ND2  1 
ATOM   5380 H  H    . ASN   B 1 99  ? 39.886 -26.026 9.801   1.00 18.83 ?  99  ASN   B H    1 
ATOM   5381 H  HA   . ASN   B 1 99  ? 41.110 -28.028 8.439   1.00 19.80 ?  99  ASN   B HA   1 
ATOM   5382 H  HB2  . ASN   B 1 99  ? 42.454 -26.315 9.428   1.00 20.60 ?  99  ASN   B HB2  1 
ATOM   5383 H  HB3  . ASN   B 1 99  ? 41.979 -26.843 10.850  1.00 20.60 ?  99  ASN   B HB3  1 
ATOM   5384 H  HD21 . ASN   B 1 99  ? 45.192 -28.152 9.735   1.00 21.58 ?  99  ASN   B HD21 1 
ATOM   5385 H  HD22 . ASN   B 1 99  ? 44.633 -26.776 9.628   1.00 21.58 ?  99  ASN   B HD22 1 
ATOM   5386 N  N    A VAL   B 1 100 ? 39.794 -29.804 9.531   0.72 20.82 ?  100 VAL   B N    1 
ATOM   5387 N  N    B VAL   B 1 100 ? 39.804 -29.806 9.528   0.28 21.17 ?  100 VAL   B N    1 
ATOM   5388 C  CA   A VAL   B 1 100 ? 39.177 -30.906 10.269  0.72 23.58 ?  100 VAL   B CA   1 
ATOM   5389 C  CA   B VAL   B 1 100 ? 39.184 -30.913 10.253  0.28 23.45 ?  100 VAL   B CA   1 
ATOM   5390 C  C    A VAL   B 1 100 ? 40.181 -31.573 11.202  0.72 24.09 ?  100 VAL   B C    1 
ATOM   5391 C  C    B VAL   B 1 100 ? 40.181 -31.571 11.197  0.28 24.19 ?  100 VAL   B C    1 
ATOM   5392 O  O    A VAL   B 1 100 ? 39.808 -32.084 12.265  0.72 24.60 ?  100 VAL   B O    1 
ATOM   5393 O  O    B VAL   B 1 100 ? 39.804 -32.061 12.268  0.28 24.45 ?  100 VAL   B O    1 
ATOM   5394 C  CB   A VAL   B 1 100 ? 38.530 -31.913 9.296   0.72 26.15 ?  100 VAL   B CB   1 
ATOM   5395 C  CB   B VAL   B 1 100 ? 38.570 -31.923 9.261   0.28 25.03 ?  100 VAL   B CB   1 
ATOM   5396 C  CG1  A VAL   B 1 100 ? 38.036 -33.144 10.044  0.72 27.20 ?  100 VAL   B CG1  1 
ATOM   5397 C  CG1  B VAL   B 1 100 ? 38.038 -33.146 9.995   0.28 25.63 ?  100 VAL   B CG1  1 
ATOM   5398 C  CG2  A VAL   B 1 100 ? 37.383 -31.263 8.538   0.72 26.78 ?  100 VAL   B CG2  1 
ATOM   5399 C  CG2  B VAL   B 1 100 ? 37.464 -31.263 8.453   0.28 25.53 ?  100 VAL   B CG2  1 
ATOM   5400 H  H    A VAL   B 1 100 ? 39.812 -29.912 8.676   0.72 24.95 ?  100 VAL   B H    1 
ATOM   5401 H  H    B VAL   B 1 100 ? 39.841 -29.915 8.677   0.28 25.38 ?  100 VAL   B H    1 
ATOM   5402 H  HA   A VAL   B 1 100 ? 38.462 -30.543 10.816  0.72 28.26 ?  100 VAL   B HA   1 
ATOM   5403 H  HA   B VAL   B 1 100 ? 38.459 -30.562 10.792  0.28 28.11 ?  100 VAL   B HA   1 
ATOM   5404 H  HB   A VAL   B 1 100 ? 39.192 -32.202 8.652   0.72 31.35 ?  100 VAL   B HB   1 
ATOM   5405 H  HB   B VAL   B 1 100 ? 39.256 -32.221 8.643   0.28 30.00 ?  100 VAL   B HB   1 
ATOM   5406 H  HG11 A VAL   B 1 100 ? 37.449 -33.653 9.459   0.72 32.61 ?  100 VAL   B HG11 1 
ATOM   5407 H  HG11 B VAL   B 1 100 ? 37.474 -33.656 9.391   0.28 30.72 ?  100 VAL   B HG11 1 
ATOM   5408 H  HG12 A VAL   B 1 100 ? 38.795 -33.690 10.301  0.72 32.61 ?  100 VAL   B HG12 1 
ATOM   5409 H  HG12 B VAL   B 1 100 ? 38.783 -33.693 10.288  0.28 30.72 ?  100 VAL   B HG12 1 
ATOM   5410 H  HG13 A VAL   B 1 100 ? 37.546 -32.862 10.833  0.72 32.61 ?  100 VAL   B HG13 1 
ATOM   5411 H  HG13 B VAL   B 1 100 ? 37.518 -32.854 10.760  0.28 30.72 ?  100 VAL   B HG13 1 
ATOM   5412 H  HG21 A VAL   B 1 100 ? 36.995 -31.917 7.933   0.72 32.10 ?  100 VAL   B HG21 1 
ATOM   5413 H  HG21 B VAL   B 1 100 ? 37.073 -31.921 7.857   0.28 30.61 ?  100 VAL   B HG21 1 
ATOM   5414 H  HG22 A VAL   B 1 100 ? 36.712 -30.965 9.173   0.72 32.10 ?  100 VAL   B HG22 1 
ATOM   5415 H  HG22 B VAL   B 1 100 ? 36.788 -30.926 9.062   0.28 30.61 ?  100 VAL   B HG22 1 
ATOM   5416 H  HG23 A VAL   B 1 100 ? 37.723 -30.509 8.035   0.72 32.10 ?  100 VAL   B HG23 1 
ATOM   5417 H  HG23 B VAL   B 1 100 ? 37.842 -30.533 7.940   0.28 30.61 ?  100 VAL   B HG23 1 
ATOM   5418 N  N    . ASN   B 1 101 ? 41.461 -31.603 10.819  1.00 24.74 ?  101 ASN   B N    1 
ATOM   5419 C  CA   . ASN   B 1 101 ? 42.494 -32.140 11.702  1.00 26.66 ?  101 ASN   B CA   1 
ATOM   5420 C  C    . ASN   B 1 101 ? 42.687 -31.301 12.959  1.00 28.81 ?  101 ASN   B C    1 
ATOM   5421 O  O    . ASN   B 1 101 ? 43.329 -31.774 13.905  1.00 30.15 ?  101 ASN   B O    1 
ATOM   5422 C  CB   . ASN   B 1 101 ? 43.823 -32.270 10.954  1.00 26.82 ?  101 ASN   B CB   1 
ATOM   5423 C  CG   . ASN   B 1 101 ? 43.823 -33.416 9.963   1.00 26.81 ?  101 ASN   B CG   1 
ATOM   5424 O  OD1  . ASN   B 1 101 ? 43.168 -34.427 10.180  1.00 27.65 ?  101 ASN   B OD1  1 
ATOM   5425 N  ND2  . ASN   B 1 101 ? 44.552 -33.259 8.867   1.00 26.19 ?  101 ASN   B ND2  1 
ATOM   5426 H  H    A ASN   B 1 101 ? 41.746 -31.336 10.052  0.72 29.65 ?  101 ASN   B H    1 
ATOM   5427 H  H    B ASN   B 1 101 ? 41.750 -31.326 10.057  0.28 29.65 ?  101 ASN   B H    1 
ATOM   5428 H  HA   . ASN   B 1 101 ? 42.226 -33.025 11.983  1.00 31.96 ?  101 ASN   B HA   1 
ATOM   5429 H  HB2  . ASN   B 1 101 ? 44.002 -31.456 10.462  1.00 32.15 ?  101 ASN   B HB2  1 
ATOM   5430 H  HB3  . ASN   B 1 101 ? 44.533 -32.429 11.599  1.00 32.15 ?  101 ASN   B HB3  1 
ATOM   5431 H  HD21 . ASN   B 1 101 ? 44.584 -33.887 8.279   1.00 31.40 ?  101 ASN   B HD21 1 
ATOM   5432 H  HD22 . ASN   B 1 101 ? 44.990 -32.531 8.745   1.00 31.40 ?  101 ASN   B HD22 1 
ATOM   5433 N  N    . LYS   B 1 102 ? 42.161 -30.075 12.982  1.00 30.95 ?  102 LYS   B N    1 
ATOM   5434 C  CA   . LYS   B 1 102 ? 42.133 -29.234 14.172  1.00 33.55 ?  102 LYS   B CA   1 
ATOM   5435 C  C    . LYS   B 1 102 ? 40.754 -29.190 14.817  1.00 32.85 ?  102 LYS   B C    1 
ATOM   5436 O  O    . LYS   B 1 102 ? 40.536 -28.392 15.733  1.00 33.64 ?  102 LYS   B O    1 
ATOM   5437 C  CB   . LYS   B 1 102 ? 42.565 -27.808 13.827  1.00 37.16 ?  102 LYS   B CB   1 
ATOM   5438 C  CG   . LYS   B 1 102 ? 44.028 -27.643 13.454  1.00 40.55 ?  102 LYS   B CG   1 
ATOM   5439 C  CD   . LYS   B 1 102 ? 44.284 -26.222 12.974  1.00 43.64 ?  102 LYS   B CD   1 
ATOM   5440 C  CE   . LYS   B 1 102 ? 45.758 -25.952 12.737  1.00 46.00 ?  102 LYS   B CE   1 
ATOM   5441 N  NZ   . LYS   B 1 102 ? 45.980 -24.566 12.233  1.00 47.39 ?  102 LYS   B NZ   1 
ATOM   5442 H  H    . LYS   B 1 102 ? 41.801 -29.697 12.297  1.00 37.10 ?  102 LYS   B H    1 
ATOM   5443 H  HA   . LYS   B 1 102 ? 42.761 -29.585 14.820  1.00 40.23 ?  102 LYS   B HA   1 
ATOM   5444 H  HB2  . LYS   B 1 102 ? 42.036 -27.497 13.076  1.00 44.56 ?  102 LYS   B HB2  1 
ATOM   5445 H  HB3  . LYS   B 1 102 ? 42.397 -27.240 14.597  1.00 44.56 ?  102 LYS   B HB3  1 
ATOM   5446 H  HG2  . LYS   B 1 102 ? 44.584 -27.811 14.231  1.00 48.64 ?  102 LYS   B HG2  1 
ATOM   5447 H  HG3  . LYS   B 1 102 ? 44.252 -28.256 12.736  1.00 48.64 ?  102 LYS   B HG3  1 
ATOM   5448 H  HD2  . LYS   B 1 102 ? 43.812 -26.080 12.138  1.00 52.33 ?  102 LYS   B HD2  1 
ATOM   5449 H  HD3  . LYS   B 1 102 ? 43.966 -25.598 13.646  1.00 52.33 ?  102 LYS   B HD3  1 
ATOM   5450 H  HE2  . LYS   B 1 102 ? 46.242 -26.053 13.572  1.00 55.17 ?  102 LYS   B HE2  1 
ATOM   5451 H  HE3  . LYS   B 1 102 ? 46.097 -26.575 12.075  1.00 55.17 ?  102 LYS   B HE3  1 
ATOM   5452 H  HZ1  . LYS   B 1 102 ? 46.849 -24.426 12.100  1.00 56.84 ?  102 LYS   B HZ1  1 
ATOM   5453 H  HZ2  . LYS   B 1 102 ? 45.547 -24.450 11.464  1.00 56.84 ?  102 LYS   B HZ2  1 
ATOM   5454 H  HZ3  . LYS   B 1 102 ? 45.679 -23.975 12.827  1.00 56.84 ?  102 LYS   B HZ3  1 
ATOM   5455 N  N    . GLY   B 1 103 ? 39.815 -30.008 14.348  1.00 31.76 ?  103 GLY   B N    1 
ATOM   5456 C  CA   . GLY   B 1 103 ? 38.487 -30.053 14.924  1.00 31.10 ?  103 GLY   B CA   1 
ATOM   5457 C  C    . GLY   B 1 103 ? 37.546 -28.963 14.466  1.00 29.85 ?  103 GLY   B C    1 
ATOM   5458 O  O    . GLY   B 1 103 ? 36.460 -28.823 15.042  1.00 30.19 ?  103 GLY   B O    1 
ATOM   5459 H  H    . GLY   B 1 103 ? 39.927 -30.547 13.689  1.00 38.08 ?  103 GLY   B H    1 
ATOM   5460 H  HA2  . GLY   B 1 103 ? 38.079 -30.904 14.705  1.00 37.29 ?  103 GLY   B HA2  1 
ATOM   5461 H  HA3  . GLY   B 1 103 ? 38.562 -29.997 15.891  1.00 37.29 ?  103 GLY   B HA3  1 
ATOM   5462 N  N    A GLU   B 1 104 ? 37.923 -28.187 13.454  0.72 28.40 ?  104 GLU   B N    1 
ATOM   5463 N  N    B GLU   B 1 104 ? 37.913 -28.195 13.446  0.28 29.18 ?  104 GLU   B N    1 
ATOM   5464 C  CA   A GLU   B 1 104 ? 37.092 -27.087 12.994  0.72 26.86 ?  104 GLU   B CA   1 
ATOM   5465 C  CA   B GLU   B 1 104 ? 37.064 -27.111 12.978  0.28 28.31 ?  104 GLU   B CA   1 
ATOM   5466 C  C    A GLU   B 1 104 ? 35.910 -27.609 12.178  0.72 27.65 ?  104 GLU   B C    1 
ATOM   5467 C  C    B GLU   B 1 104 ? 35.908 -27.654 12.143  0.28 28.44 ?  104 GLU   B C    1 
ATOM   5468 O  O    A GLU   B 1 104 ? 35.949 -28.697 11.597  0.72 28.43 ?  104 GLU   B O    1 
ATOM   5469 O  O    B GLU   B 1 104 ? 35.998 -28.723 11.532  0.28 28.67 ?  104 GLU   B O    1 
ATOM   5470 C  CB   A GLU   B 1 104 ? 37.935 -26.089 12.196  0.72 25.38 ?  104 GLU   B CB   1 
ATOM   5471 C  CB   B GLU   B 1 104 ? 37.891 -26.101 12.184  0.28 27.42 ?  104 GLU   B CB   1 
ATOM   5472 C  CG   A GLU   B 1 104 ? 39.031 -25.457 13.046  0.72 24.10 ?  104 GLU   B CG   1 
ATOM   5473 C  CG   B GLU   B 1 104 ? 38.973 -25.440 13.031  0.28 26.68 ?  104 GLU   B CG   1 
ATOM   5474 C  CD   A GLU   B 1 104 ? 39.977 -24.566 12.271  0.72 22.61 ?  104 GLU   B CD   1 
ATOM   5475 C  CD   B GLU   B 1 104 ? 39.926 -24.582 12.225  0.28 26.02 ?  104 GLU   B CD   1 
ATOM   5476 O  OE1  A GLU   B 1 104 ? 39.974 -24.597 11.021  0.72 20.61 ?  104 GLU   B OE1  1 
ATOM   5477 O  OE1  B GLU   B 1 104 ? 39.846 -24.596 10.979  0.28 25.44 ?  104 GLU   B OE1  1 
ATOM   5478 O  OE2  A GLU   B 1 104 ? 40.737 -23.830 12.933  0.72 22.98 -1 104 GLU   B OE2  1 
ATOM   5479 O  OE2  B GLU   B 1 104 ? 40.762 -23.892 12.846  0.28 26.06 -1 104 GLU   B OE2  1 
ATOM   5480 H  H    A GLU   B 1 104 ? 38.661 -28.277 13.021  0.72 34.05 ?  104 GLU   B H    1 
ATOM   5481 H  H    B GLU   B 1 104 ? 38.650 -28.279 13.014  0.28 34.99 ?  104 GLU   B H    1 
ATOM   5482 H  HA   A GLU   B 1 104 ? 36.740 -26.618 13.768  0.72 32.20 ?  104 GLU   B HA   1 
ATOM   5483 H  HA   B GLU   B 1 104 ? 36.689 -26.652 13.744  0.28 33.94 ?  104 GLU   B HA   1 
ATOM   5484 H  HB2  A GLU   B 1 104 ? 38.356 -26.548 11.453  0.72 30.43 ?  104 GLU   B HB2  1 
ATOM   5485 H  HB2  B GLU   B 1 104 ? 38.324 -26.556 11.445  0.28 32.88 ?  104 GLU   B HB2  1 
ATOM   5486 H  HB3  A GLU   B 1 104 ? 37.362 -25.378 11.868  0.72 30.43 ?  104 GLU   B HB3  1 
ATOM   5487 H  HB3  B GLU   B 1 104 ? 37.304 -25.405 11.849  0.28 32.88 ?  104 GLU   B HB3  1 
ATOM   5488 H  HG2  A GLU   B 1 104 ? 38.623 -24.915 13.740  0.72 28.89 ?  104 GLU   B HG2  1 
ATOM   5489 H  HG2  B GLU   B 1 104 ? 38.550 -24.873 13.697  0.28 31.99 ?  104 GLU   B HG2  1 
ATOM   5490 H  HG3  A GLU   B 1 104 ? 39.564 -26.159 13.452  0.72 28.89 ?  104 GLU   B HG3  1 
ATOM   5491 H  HG3  B GLU   B 1 104 ? 39.495 -26.129 13.473  0.28 31.99 ?  104 GLU   B HG3  1 
ATOM   5492 N  N    A ASP   B 1 105 ? 34.844 -26.812 12.151  0.72 27.62 ?  105 ASP   B N    1 
ATOM   5493 N  N    B ASP   B 1 105 ? 34.812 -26.898 12.126  0.28 28.19 ?  105 ASP   B N    1 
ATOM   5494 C  CA   A ASP   B 1 105 ? 33.565 -27.263 11.616  0.72 28.26 ?  105 ASP   B CA   1 
ATOM   5495 C  CA   B ASP   B 1 105 ? 33.557 -27.380 11.563  0.28 28.16 ?  105 ASP   B CA   1 
ATOM   5496 C  C    A ASP   B 1 105 ? 33.612 -27.318 10.093  0.72 26.31 ?  105 ASP   B C    1 
ATOM   5497 C  C    B ASP   B 1 105 ? 33.629 -27.393 10.040  0.28 27.32 ?  105 ASP   B C    1 
ATOM   5498 O  O    A ASP   B 1 105 ? 33.755 -26.285 9.430   0.72 25.42 ?  105 ASP   B O    1 
ATOM   5499 O  O    B ASP   B 1 105 ? 33.845 -26.353 9.409   0.28 26.99 ?  105 ASP   B O    1 
ATOM   5500 C  CB   A ASP   B 1 105 ? 32.454 -26.323 12.081  0.72 31.47 ?  105 ASP   B CB   1 
ATOM   5501 C  CB   B ASP   B 1 105 ? 32.407 -26.493 12.036  0.28 28.93 ?  105 ASP   B CB   1 
ATOM   5502 C  CG   A ASP   B 1 105 ? 31.077 -26.787 11.647  0.72 34.23 ?  105 ASP   B CG   1 
ATOM   5503 C  CG   B ASP   B 1 105 ? 31.045 -27.088 11.724  0.28 29.58 ?  105 ASP   B CG   1 
ATOM   5504 O  OD1  A ASP   B 1 105 ? 30.970 -27.897 11.084  0.72 34.57 ?  105 ASP   B OD1  1 
ATOM   5505 O  OD1  B ASP   B 1 105 ? 30.991 -28.094 10.985  0.28 29.69 ?  105 ASP   B OD1  1 
ATOM   5506 O  OD2  A ASP   B 1 105 ? 30.098 -26.039 11.863  0.72 35.81 -1 105 ASP   B OD2  1 
ATOM   5507 O  OD2  B ASP   B 1 105 ? 30.030 -26.560 12.226  0.28 29.66 -1 105 ASP   B OD2  1 
ATOM   5508 H  H    A ASP   B 1 105 ? 34.839 -26.001 12.432  0.72 33.11 ?  105 ASP   B H    1 
ATOM   5509 H  H    B ASP   B 1 105 ? 34.773 -26.099 12.432  0.28 33.80 ?  105 ASP   B H    1 
ATOM   5510 H  HA   A ASP   B 1 105 ? 33.370 -28.153 11.950  0.72 33.88 ?  105 ASP   B HA   1 
ATOM   5511 H  HA   B ASP   B 1 105 ? 33.385 -28.284 11.869  0.28 33.76 ?  105 ASP   B HA   1 
ATOM   5512 H  HB2  A ASP   B 1 105 ? 32.478 -26.258 13.052  0.72 37.73 ?  105 ASP   B HB2  1 
ATOM   5513 H  HB2  B ASP   B 1 105 ? 32.469 -26.377 12.999  0.28 34.69 ?  105 ASP   B HB2  1 
ATOM   5514 H  HB3  A ASP   B 1 105 ? 32.593 -25.447 11.690  0.72 37.73 ?  105 ASP   B HB3  1 
ATOM   5515 H  HB3  B ASP   B 1 105 ? 32.471 -25.627 11.598  0.28 34.69 ?  105 ASP   B HB3  1 
ATOM   5516 N  N    A ILE   B 1 106 ? 33.466 -28.526 9.541   0.72 25.81 ?  106 ILE   B N    1 
ATOM   5517 N  N    B ILE   B 1 106 ? 33.438 -28.577 9.452   0.28 26.78 ?  106 ILE   B N    1 
ATOM   5518 C  CA   A ILE   B 1 106 ? 33.459 -28.712 8.095   0.72 24.86 ?  106 ILE   B CA   1 
ATOM   5519 C  CA   B ILE   B 1 106 ? 33.449 -28.721 8.001   0.28 26.37 ?  106 ILE   B CA   1 
ATOM   5520 C  C    A ILE   B 1 106 ? 32.362 -27.891 7.422   0.72 23.77 ?  106 ILE   B C    1 
ATOM   5521 C  C    B ILE   B 1 106 ? 32.351 -27.897 7.341   0.28 25.77 ?  106 ILE   B C    1 
ATOM   5522 O  O    A ILE   B 1 106 ? 32.467 -27.573 6.233   0.72 22.75 ?  106 ILE   B O    1 
ATOM   5523 O  O    B ILE   B 1 106 ? 32.434 -27.599 6.144   0.28 25.42 ?  106 ILE   B O    1 
ATOM   5524 C  CB   A ILE   B 1 106 ? 33.360 -30.220 7.768   0.72 26.07 ?  106 ILE   B CB   1 
ATOM   5525 C  CB   B ILE   B 1 106 ? 33.354 -30.219 7.628   0.28 26.75 ?  106 ILE   B CB   1 
ATOM   5526 C  CG1  A ILE   B 1 106 ? 33.624 -30.479 6.285   0.72 26.70 ?  106 ILE   B CG1  1 
ATOM   5527 C  CG1  B ILE   B 1 106 ? 33.631 -30.435 6.138   0.28 26.92 ?  106 ILE   B CG1  1 
ATOM   5528 C  CG2  A ILE   B 1 106 ? 31.996 -30.771 8.174   0.72 26.88 ?  106 ILE   B CG2  1 
ATOM   5529 C  CG2  B ILE   B 1 106 ? 31.987 -30.779 8.001   0.28 27.08 ?  106 ILE   B CG2  1 
ATOM   5530 C  CD1  A ILE   B 1 106 ? 34.993 -30.036 5.831   0.72 26.76 ?  106 ILE   B CD1  1 
ATOM   5531 C  CD1  B ILE   B 1 106 ? 34.999 -29.965 5.703   0.28 26.97 ?  106 ILE   B CD1  1 
ATOM   5532 H  H    A ILE   B 1 106 ? 33.373 -29.252 9.991   0.72 30.94 ?  106 ILE   B H    1 
ATOM   5533 H  H    B ILE   B 1 106 ? 33.308 -29.312 9.876   0.28 32.10 ?  106 ILE   B H    1 
ATOM   5534 H  HA   A ILE   B 1 106 ? 34.307 -28.396 7.754   0.72 29.81 ?  106 ILE   B HA   1 
ATOM   5535 H  HA   B ILE   B 1 106 ? 34.296 -28.388 7.673   0.28 31.61 ?  106 ILE   B HA   1 
ATOM   5536 H  HB   A ILE   B 1 106 ? 34.036 -30.689 8.282   0.72 31.26 ?  106 ILE   B HB   1 
ATOM   5537 H  HB   B ILE   B 1 106 ? 34.025 -30.702 8.133   0.28 32.07 ?  106 ILE   B HB   1 
ATOM   5538 H  HG12 A ILE   B 1 106 ? 33.554 -31.433 6.116   0.72 32.00 ?  106 ILE   B HG12 1 
ATOM   5539 H  HG12 B ILE   B 1 106 ? 33.571 -31.385 5.944   0.28 32.27 ?  106 ILE   B HG12 1 
ATOM   5540 H  HG13 A ILE   B 1 106 ? 32.967 -30.004 5.757   0.72 32.00 ?  106 ILE   B HG13 1 
ATOM   5541 H  HG13 B ILE   B 1 106 ? 32.971 -29.953 5.619   0.28 32.27 ?  106 ILE   B HG13 1 
ATOM   5542 H  HG21 A ILE   B 1 106 ? 32.007 -31.737 8.089   0.72 32.23 ?  106 ILE   B HG21 1 
ATOM   5543 H  HG21 B ILE   B 1 106 ? 32.005 -31.744 7.901   0.28 32.47 ?  106 ILE   B HG21 1 
ATOM   5544 H  HG22 A ILE   B 1 106 ? 31.818 -30.524 9.096   0.72 32.23 ?  106 ILE   B HG22 1 
ATOM   5545 H  HG22 B ILE   B 1 106 ? 31.793 -30.546 8.922   0.28 32.47 ?  106 ILE   B HG22 1 
ATOM   5546 H  HG23 A ILE   B 1 106 ? 31.316 -30.395 7.594   0.72 32.23 ?  106 ILE   B HG23 1 
ATOM   5547 H  HG23 B ILE   B 1 106 ? 31.316 -30.398 7.414   0.28 32.47 ?  106 ILE   B HG23 1 
ATOM   5548 H  HD11 A ILE   B 1 106 ? 35.194 -30.449 4.978   0.72 32.08 ?  106 ILE   B HD11 1 
ATOM   5549 H  HD11 B ILE   B 1 106 ? 35.204 -30.354 4.840   0.28 32.34 ?  106 ILE   B HD11 1 
ATOM   5550 H  HD12 A ILE   B 1 106 ? 34.999 -29.069 5.738   0.72 32.08 ?  106 ILE   B HD12 1 
ATOM   5551 H  HD12 B ILE   B 1 106 ? 34.994 -28.997 5.638   0.28 32.34 ?  106 ILE   B HD12 1 
ATOM   5552 H  HD13 A ILE   B 1 106 ? 35.651 -30.308 6.492   0.72 32.08 ?  106 ILE   B HD13 1 
ATOM   5553 H  HD13 B ILE   B 1 106 ? 35.654 -30.252 6.359   0.28 32.34 ?  106 ILE   B HD13 1 
ATOM   5554 N  N    A GLN   B 1 107 ? 31.314 -27.519 8.158   0.72 24.51 ?  107 GLN   B N    1 
ATOM   5555 N  N    B GLN   B 1 107 ? 31.316 -27.514 8.094   0.28 25.79 ?  107 GLN   B N    1 
ATOM   5556 C  CA   A GLN   B 1 107 ? 30.240 -26.718 7.579   0.72 25.05 ?  107 GLN   B CA   1 
ATOM   5557 C  CA   B GLN   B 1 107 ? 30.236 -26.709 7.535   0.28 25.77 ?  107 GLN   B CA   1 
ATOM   5558 C  C    A GLN   B 1 107 ? 30.731 -25.369 7.063   0.72 22.87 ?  107 GLN   B C    1 
ATOM   5559 C  C    B GLN   B 1 107 ? 30.719 -25.342 7.065   0.28 23.39 ?  107 GLN   B C    1 
ATOM   5560 O  O    A GLN   B 1 107 ? 30.094 -24.794 6.176   0.72 23.57 ?  107 GLN   B O    1 
ATOM   5561 O  O    B GLN   B 1 107 ? 30.060 -24.723 6.224   0.28 23.76 ?  107 GLN   B O    1 
ATOM   5562 C  CB   A GLN   B 1 107 ? 29.127 -26.517 8.611   0.72 29.04 ?  107 GLN   B CB   1 
ATOM   5563 C  CB   B GLN   B 1 107 ? 29.118 -26.551 8.570   0.28 28.36 ?  107 GLN   B CB   1 
ATOM   5564 C  CG   A GLN   B 1 107 ? 27.801 -26.021 8.036   0.72 32.97 ?  107 GLN   B CG   1 
ATOM   5565 C  CG   B GLN   B 1 107 ? 27.795 -26.036 8.010   0.28 30.75 ?  107 GLN   B CG   1 
ATOM   5566 C  CD   A GLN   B 1 107 ? 27.726 -24.507 7.931   0.72 36.02 ?  107 GLN   B CD   1 
ATOM   5567 C  CD   B GLN   B 1 107 ? 27.694 -24.521 8.030   0.28 32.63 ?  107 GLN   B CD   1 
ATOM   5568 O  OE1  A GLN   B 1 107 ? 28.558 -23.790 8.489   0.72 37.15 ?  107 GLN   B OE1  1 
ATOM   5569 O  OE1  B GLN   B 1 107 ? 28.547 -23.835 8.594   0.28 33.28 ?  107 GLN   B OE1  1 
ATOM   5570 N  NE2  A GLN   B 1 107 ? 26.719 -24.012 7.214   0.72 37.09 ?  107 GLN   B NE2  1 
ATOM   5571 N  NE2  B GLN   B 1 107 ? 26.641 -23.992 7.415   0.28 33.33 ?  107 GLN   B NE2  1 
ATOM   5572 H  H    A GLN   B 1 107 ? 31.206 -27.713 8.983   0.72 29.38 ?  107 GLN   B H    1 
ATOM   5573 H  H    B GLN   B 1 107 ? 31.217 -27.709 8.923   0.28 30.92 ?  107 GLN   B H    1 
ATOM   5574 H  HA   A GLN   B 1 107 ? 29.861 -27.202 6.828   0.72 30.03 ?  107 GLN   B HA   1 
ATOM   5575 H  HA   B GLN   B 1 107 ? 29.863 -27.174 6.770   0.28 30.89 ?  107 GLN   B HA   1 
ATOM   5576 H  HB2  A GLN   B 1 107 ? 28.957 -27.364 9.046   0.72 34.82 ?  107 GLN   B HB2  1 
ATOM   5577 H  HB2  B GLN   B 1 107 ? 28.945 -27.416 8.969   0.28 34.00 ?  107 GLN   B HB2  1 
ATOM   5578 H  HB3  A GLN   B 1 107 ? 29.427 -25.868 9.266   0.72 34.82 ?  107 GLN   B HB3  1 
ATOM   5579 H  HB3  B GLN   B 1 107 ? 29.412 -25.930 9.254   0.28 34.00 ?  107 GLN   B HB3  1 
ATOM   5580 H  HG2  A GLN   B 1 107 ? 27.683 -26.387 7.146   0.72 39.54 ?  107 GLN   B HG2  1 
ATOM   5581 H  HG2  B GLN   B 1 107 ? 27.704 -26.329 7.090   0.28 36.87 ?  107 GLN   B HG2  1 
ATOM   5582 H  HG3  A GLN   B 1 107 ? 27.077 -26.320 8.613   0.72 39.54 ?  107 GLN   B HG3  1 
ATOM   5583 H  HG3  B GLN   B 1 107 ? 27.066 -26.395 8.544   0.28 36.87 ?  107 GLN   B HG3  1 
ATOM   5584 H  HE21 A GLN   B 1 107 ? 26.155 -24.542 6.836   0.72 44.48 ?  107 GLN   B HE21 1 
ATOM   5585 H  HE21 B GLN   B 1 107 ? 26.064 -24.502 7.031   0.28 39.97 ?  107 GLN   B HE21 1 
ATOM   5586 H  HE22 A GLN   B 1 107 ? 26.629 -23.160 7.127   0.72 44.48 ?  107 GLN   B HE22 1 
ATOM   5587 H  HE22 B GLN   B 1 107 ? 26.535 -23.138 7.401   0.28 39.97 ?  107 GLN   B HE22 1 
ATOM   5588 N  N    . LEU   B 1 108 ? 31.853 -24.860 7.580   1.00 20.90 ?  108 LEU   B N    1 
ATOM   5589 C  CA   . LEU   B 1 108 ? 32.394 -23.562 7.167   1.00 18.51 ?  108 LEU   B CA   1 
ATOM   5590 C  C    . LEU   B 1 108 ? 33.041 -23.588 5.793   1.00 16.13 ?  108 LEU   B C    1 
ATOM   5591 O  O    . LEU   B 1 108 ? 33.478 -22.533 5.308   1.00 15.82 ?  108 LEU   B O    1 
ATOM   5592 C  CB   . LEU   B 1 108 ? 33.399 -23.070 8.205   1.00 19.09 ?  108 LEU   B CB   1 
ATOM   5593 C  CG   . LEU   B 1 108 ? 32.770 -22.624 9.522   1.00 20.50 ?  108 LEU   B CG   1 
ATOM   5594 C  CD1  . LEU   B 1 108 ? 33.798 -22.591 10.635  1.00 20.83 ?  108 LEU   B CD1  1 
ATOM   5595 C  CD2  . LEU   B 1 108 ? 32.140 -21.255 9.346   1.00 21.74 ?  108 LEU   B CD2  1 
ATOM   5596 H  H    A LEU   B 1 108 ? 32.313 -25.250 8.189   0.72 25.05 ?  108 LEU   B H    1 
ATOM   5597 H  H    B LEU   B 1 108 ? 32.316 -25.261 8.179   0.28 25.05 ?  108 LEU   B H    1 
ATOM   5598 H  HA   . LEU   B 1 108 ? 31.666 -22.923 7.135   1.00 22.18 ?  108 LEU   B HA   1 
ATOM   5599 H  HB2  . LEU   B 1 108 ? 34.018 -23.788 8.404   1.00 22.88 ?  108 LEU   B HB2  1 
ATOM   5600 H  HB3  . LEU   B 1 108 ? 33.877 -22.313 7.838   1.00 22.88 ?  108 LEU   B HB3  1 
ATOM   5601 H  HG   . LEU   B 1 108 ? 32.068 -23.250 9.775   1.00 24.58 ?  108 LEU   B HG   1 
ATOM   5602 H  HD11 . LEU   B 1 108 ? 33.363 -22.320 11.461  1.00 24.97 ?  108 LEU   B HD11 1 
ATOM   5603 H  HD12 . LEU   B 1 108 ? 34.181 -23.475 10.739  1.00 24.97 ?  108 LEU   B HD12 1 
ATOM   5604 H  HD13 . LEU   B 1 108 ? 34.490 -21.953 10.404  1.00 24.97 ?  108 LEU   B HD13 1 
ATOM   5605 H  HD21 . LEU   B 1 108 ? 31.790 -20.956 10.200  1.00 26.06 ?  108 LEU   B HD21 1 
ATOM   5606 H  HD22 . LEU   B 1 108 ? 32.816 -20.637 9.030   1.00 26.06 ?  108 LEU   B HD22 1 
ATOM   5607 H  HD23 . LEU   B 1 108 ? 31.420 -21.319 8.698   1.00 26.06 ?  108 LEU   B HD23 1 
ATOM   5608 N  N    . LEU   B 1 109 ? 33.105 -24.757 5.161   1.00 15.19 ?  109 LEU   B N    1 
ATOM   5609 C  CA   . LEU   B 1 109 ? 33.738 -24.865 3.856   1.00 14.53 ?  109 LEU   B CA   1 
ATOM   5610 C  C    . LEU   B 1 109 ? 32.975 -24.082 2.796   1.00 13.60 ?  109 LEU   B C    1 
ATOM   5611 O  O    . LEU   B 1 109 ? 33.593 -23.492 1.902   1.00 13.39 ?  109 LEU   B O    1 
ATOM   5612 C  CB   . LEU   B 1 109 ? 33.860 -26.342 3.480   1.00 14.72 ?  109 LEU   B CB   1 
ATOM   5613 C  CG   . LEU   B 1 109 ? 34.640 -26.684 2.215   1.00 14.44 ?  109 LEU   B CG   1 
ATOM   5614 C  CD1  . LEU   B 1 109 ? 36.017 -26.025 2.221   1.00 14.22 ?  109 LEU   B CD1  1 
ATOM   5615 C  CD2  . LEU   B 1 109 ? 34.761 -28.195 2.079   1.00 15.25 ?  109 LEU   B CD2  1 
ATOM   5616 H  H    . LEU   B 1 109 ? 32.798 -25.499 5.462   1.00 18.20 ?  109 LEU   B H    1 
ATOM   5617 H  HA   . LEU   B 1 109 ? 34.630 -24.498 3.905   1.00 17.40 ?  109 LEU   B HA   1 
ATOM   5618 H  HB2  . LEU   B 1 109 ? 34.301 -26.804 4.210   1.00 17.64 ?  109 LEU   B HB2  1 
ATOM   5619 H  HB3  . LEU   B 1 109 ? 32.968 -26.706 3.366   1.00 17.64 ?  109 LEU   B HB3  1 
ATOM   5620 H  HG   . LEU   B 1 109 ? 34.150 -26.363 1.440   1.00 17.29 ?  109 LEU   B HG   1 
ATOM   5621 H  HD11 . LEU   B 1 109 ? 36.546 -26.388 1.492   1.00 17.03 ?  109 LEU   B HD11 1 
ATOM   5622 H  HD12 . LEU   B 1 109 ? 35.907 -25.070 2.105   1.00 17.03 ?  109 LEU   B HD12 1 
ATOM   5623 H  HD13 . LEU   B 1 109 ? 36.451 -26.213 3.067   1.00 17.03 ?  109 LEU   B HD13 1 
ATOM   5624 H  HD21 . LEU   B 1 109 ? 35.331 -28.405 1.320   1.00 18.28 ?  109 LEU   B HD21 1 
ATOM   5625 H  HD22 . LEU   B 1 109 ? 35.149 -28.559 2.890   1.00 18.28 ?  109 LEU   B HD22 1 
ATOM   5626 H  HD23 . LEU   B 1 109 ? 33.877 -28.578 1.939   1.00 18.28 ?  109 LEU   B HD23 1 
ATOM   5627 N  N    . LYS   B 1 110 ? 31.640 -24.047 2.875   1.00 13.36 ?  110 LYS   B N    1 
ATOM   5628 C  CA   . LYS   B 1 110 ? 30.884 -23.286 1.884   1.00 12.96 ?  110 LYS   B CA   1 
ATOM   5629 C  C    . LYS   B 1 110 ? 31.221 -21.797 1.971   1.00 12.97 ?  110 LYS   B C    1 
ATOM   5630 O  O    . LYS   B 1 110 ? 31.477 -21.148 0.952   1.00 12.72 ?  110 LYS   B O    1 
ATOM   5631 C  CB   . LYS   B 1 110 ? 29.379 -23.536 2.033   1.00 13.69 ?  110 LYS   B CB   1 
ATOM   5632 C  CG   . LYS   B 1 110 ? 28.577 -22.920 0.893   1.00 14.43 ?  110 LYS   B CG   1 
ATOM   5633 C  CD   . LYS   B 1 110 ? 27.109 -23.340 0.923   1.00 14.45 ?  110 LYS   B CD   1 
ATOM   5634 C  CE   . LYS   B 1 110 ? 26.348 -22.809 -0.293  1.00 15.30 ?  110 LYS   B CE   1 
ATOM   5635 N  NZ   . LYS   B 1 110 ? 26.668 -23.534 -1.548  1.00 15.72 ?  110 LYS   B NZ   1 
ATOM   5636 H  H    . LYS   B 1 110 ? 31.166 -24.446 3.470   1.00 16.00 ?  110 LYS   B H    1 
ATOM   5637 H  HA   . LYS   B 1 110 ? 31.142 -23.593 0.996   1.00 15.53 ?  110 LYS   B HA   1 
ATOM   5638 H  HB2  . LYS   B 1 110 ? 29.214 -24.495 2.032   1.00 16.40 ?  110 LYS   B HB2  1 
ATOM   5639 H  HB3  . LYS   B 1 110 ? 29.072 -23.147 2.863   1.00 16.40 ?  110 LYS   B HB3  1 
ATOM   5640 H  HG2  . LYS   B 1 110 ? 28.607 -21.956 0.964   1.00 17.29 ?  110 LYS   B HG2  1 
ATOM   5641 H  HG3  . LYS   B 1 110 ? 28.947 -23.208 0.046   1.00 17.29 ?  110 LYS   B HG3  1 
ATOM   5642 H  HD2  . LYS   B 1 110 ? 27.048 -24.312 0.916   1.00 17.31 ?  110 LYS   B HD2  1 
ATOM   5643 H  HD3  . LYS   B 1 110 ? 26.685 -22.988 1.723   1.00 17.31 ?  110 LYS   B HD3  1 
ATOM   5644 H  HE2  . LYS   B 1 110 ? 25.397 -22.892 -0.136  1.00 18.33 ?  110 LYS   B HE2  1 
ATOM   5645 H  HE3  . LYS   B 1 110 ? 26.583 -21.875 -0.422  1.00 18.33 ?  110 LYS   B HE3  1 
ATOM   5646 H  HZ1  . LYS   B 1 110 ? 26.211 -23.189 -2.225  1.00 18.83 ?  110 LYS   B HZ1  1 
ATOM   5647 H  HZ2  . LYS   B 1 110 ? 27.541 -23.467 -1.722  1.00 18.83 ?  110 LYS   B HZ2  1 
ATOM   5648 H  HZ3  . LYS   B 1 110 ? 26.459 -24.395 -1.461  1.00 18.83 ?  110 LYS   B HZ3  1 
ATOM   5649 N  N    . SER   B 1 111 ? 31.248 -21.246 3.189   1.00 13.36 ?  111 SER   B N    1 
ATOM   5650 C  CA   . SER   B 1 111 ? 31.633 -19.845 3.359   1.00 13.19 ?  111 SER   B CA   1 
ATOM   5651 C  C    . SER   B 1 111 ? 33.017 -19.585 2.777   1.00 12.89 ?  111 SER   B C    1 
ATOM   5652 O  O    . SER   B 1 111 ? 33.244 -18.556 2.126   1.00 12.91 ?  111 SER   B O    1 
ATOM   5653 C  CB   . SER   B 1 111 ? 31.619 -19.467 4.838   1.00 14.32 ?  111 SER   B CB   1 
ATOM   5654 O  OG   . SER   B 1 111 ? 30.314 -19.487 5.371   1.00 16.21 ?  111 SER   B OG   1 
ATOM   5655 H  H    . SER   B 1 111 ? 31.059 -21.661 3.917   1.00 16.00 ?  111 SER   B H    1 
ATOM   5656 H  HA   . SER   B 1 111 ? 31.001 -19.283 2.890   1.00 15.79 ?  111 SER   B HA   1 
ATOM   5657 H  HB2  . SER   B 1 111 ? 32.165 -20.098 5.330   1.00 17.16 ?  111 SER   B HB2  1 
ATOM   5658 H  HB3  . SER   B 1 111 ? 31.976 -18.573 4.936   1.00 17.16 ?  111 SER   B HB3  1 
ATOM   5659 H  HG   . SER   B 1 111 ? 30.327 -19.279 6.190   1.00 19.42 ?  111 SER   B HG   1 
ATOM   5660 N  N    . ALA   B 1 112 ? 33.958 -20.503 3.007   1.00 12.92 ?  112 ALA   B N    1 
ATOM   5661 C  CA   . ALA   B 1 112 ? 35.305 -20.339 2.467   1.00 12.53 ?  112 ALA   B CA   1 
ATOM   5662 C  C    . ALA   B 1 112 ? 35.275 -20.238 0.945   1.00 11.77 ?  112 ALA   B C    1 
ATOM   5663 O  O    . ALA   B 1 112 ? 35.902 -19.349 0.357   1.00 12.28 ?  112 ALA   B O    1 
ATOM   5664 C  CB   . ALA   B 1 112 ? 36.202 -21.486 2.937   1.00 12.98 ?  112 ALA   B CB   1 
ATOM   5665 H  H    . ALA   B 1 112 ? 33.841 -21.226 3.469   1.00 15.47 ?  112 ALA   B H    1 
ATOM   5666 H  HA   . ALA   B 1 112 ? 35.675 -19.514 2.811   1.00 15.01 ?  112 ALA   B HA   1 
ATOM   5667 H  HB1  . ALA   B 1 112 ? 37.095 -21.353 2.575   1.00 15.55 ?  112 ALA   B HB1  1 
ATOM   5668 H  HB2  . ALA   B 1 112 ? 36.240 -21.480 3.908   1.00 15.55 ?  112 ALA   B HB2  1 
ATOM   5669 H  HB3  . ALA   B 1 112 ? 35.839 -22.325 2.624   1.00 15.55 ?  112 ALA   B HB3  1 
ATOM   5670 N  N    . TYR   B 1 113 ? 34.533 -21.135 0.287   1.00 12.02 ?  113 TYR   B N    1 
ATOM   5671 C  CA   . TYR   B 1 113 ? 34.457 -21.094 -1.168  1.00 11.84 ?  113 TYR   B CA   1 
ATOM   5672 C  C    . TYR   B 1 113 ? 33.747 -19.848 -1.685  1.00 11.31 ?  113 TYR   B C    1 
ATOM   5673 O  O    . TYR   B 1 113 ? 34.021 -19.419 -2.809  1.00 11.32 ?  113 TYR   B O    1 
ATOM   5674 C  CB   . TYR   B 1 113 ? 33.791 -22.360 -1.718  1.00 11.95 ?  113 TYR   B CB   1 
ATOM   5675 C  CG   . TYR   B 1 113 ? 34.750 -23.509 -1.977  1.00 12.55 ?  113 TYR   B CG   1 
ATOM   5676 C  CD1  . TYR   B 1 113 ? 35.738 -23.406 -2.945  1.00 13.20 ?  113 TYR   B CD1  1 
ATOM   5677 C  CD2  . TYR   B 1 113 ? 34.653 -24.702 -1.272  1.00 12.77 ?  113 TYR   B CD2  1 
ATOM   5678 C  CE1  . TYR   B 1 113 ? 36.624 -24.435 -3.187  1.00 13.10 ?  113 TYR   B CE1  1 
ATOM   5679 C  CE2  . TYR   B 1 113 ? 35.527 -25.755 -1.514  1.00 12.94 ?  113 TYR   B CE2  1 
ATOM   5680 C  CZ   . TYR   B 1 113 ? 36.506 -25.617 -2.477  1.00 12.91 ?  113 TYR   B CZ   1 
ATOM   5681 O  OH   . TYR   B 1 113 ? 37.389 -26.634 -2.750  1.00 13.69 ?  113 TYR   B OH   1 
ATOM   5682 H  H    . TYR   B 1 113 ? 34.070 -21.765 0.659   1.00 14.40 ?  113 TYR   B H    1 
ATOM   5683 H  HA   . TYR   B 1 113 ? 35.359 -21.074 -1.510  1.00 14.18 ?  113 TYR   B HA   1 
ATOM   5684 H  HB2  . TYR   B 1 113 ? 33.126 -22.672 -1.080  1.00 14.31 ?  113 TYR   B HB2  1 
ATOM   5685 H  HB3  . TYR   B 1 113 ? 33.352 -22.142 -2.558  1.00 14.31 ?  113 TYR   B HB3  1 
ATOM   5686 H  HD1  . TYR   B 1 113 ? 35.823 -22.608 -3.430  1.00 15.81 ?  113 TYR   B HD1  1 
ATOM   5687 H  HD2  . TYR   B 1 113 ? 33.988 -24.797 -0.633  1.00 15.30 ?  113 TYR   B HD2  1 
ATOM   5688 H  HE1  . TYR   B 1 113 ? 37.281 -24.343 -3.848  1.00 15.69 ?  113 TYR   B HE1  1 
ATOM   5689 H  HE2  . TYR   B 1 113 ? 35.444 -26.551 -1.042  1.00 15.50 ?  113 TYR   B HE2  1 
ATOM   5690 H  HH   . TYR   B 1 113 ? 37.213 -27.302 -2.274  1.00 16.39 ?  113 TYR   B HH   1 
ATOM   5691 N  N    . GLU   B 1 114 ? 32.825 -19.272 -0.906  1.00 11.48 ?  114 GLU   B N    1 
ATOM   5692 C  CA   . GLU   B 1 114 ? 32.144 -18.065 -1.362  1.00 11.49 ?  114 GLU   B CA   1 
ATOM   5693 C  C    . GLU   B 1 114 ? 33.129 -16.941 -1.655  1.00 11.18 ?  114 GLU   B C    1 
ATOM   5694 O  O    . GLU   B 1 114 ? 32.851 -16.084 -2.497  1.00 11.52 ?  114 GLU   B O    1 
ATOM   5695 C  CB   . GLU   B 1 114 ? 31.090 -17.636 -0.338  1.00 11.92 ?  114 GLU   B CB   1 
ATOM   5696 C  CG   . GLU   B 1 114 ? 29.862 -18.545 -0.413  1.00 11.83 ?  114 GLU   B CG   1 
ATOM   5697 C  CD   . GLU   B 1 114 ? 28.846 -18.365 0.700   1.00 12.27 ?  114 GLU   B CD   1 
ATOM   5698 O  OE1  . GLU   B 1 114 ? 29.137 -17.750 1.745   1.00 12.57 ?  114 GLU   B OE1  1 
ATOM   5699 O  OE2  . GLU   B 1 114 ? 27.722 -18.901 0.539   1.00 13.20 -1 114 GLU   B OE2  1 
ATOM   5700 H  H    . GLU   B 1 114 ? 32.575 -19.566 -0.133  1.00 13.74 ?  114 GLU   B H    1 
ATOM   5701 H  HA   . GLU   B 1 114 ? 31.683 -18.266 -2.186  1.00 13.76 ?  114 GLU   B HA   1 
ATOM   5702 H  HB2  . GLU   B 1 114 ? 31.465 -17.700 0.557   1.00 14.27 ?  114 GLU   B HB2  1 
ATOM   5703 H  HB3  . GLU   B 1 114 ? 30.813 -16.729 -0.525  1.00 14.27 ?  114 GLU   B HB3  1 
ATOM   5704 H  HG2  . GLU   B 1 114 ? 29.414 -18.379 -1.254  1.00 14.17 ?  114 GLU   B HG2  1 
ATOM   5705 H  HG3  . GLU   B 1 114 ? 30.166 -19.468 -0.385  1.00 14.17 ?  114 GLU   B HG3  1 
ATOM   5706 N  N    . ASN   B 1 115 ? 34.294 -16.936 -0.998  1.00 11.17 ?  115 ASN   B N    1 
ATOM   5707 C  CA   . ASN   B 1 115 ? 35.284 -15.902 -1.298  1.00 11.07 ?  115 ASN   B CA   1 
ATOM   5708 C  C    . ASN   B 1 115 ? 35.692 -15.923 -2.763  1.00 10.86 ?  115 ASN   B C    1 
ATOM   5709 O  O    . ASN   B 1 115 ? 36.086 -14.884 -3.316  1.00 11.65 ?  115 ASN   B O    1 
ATOM   5710 C  CB   . ASN   B 1 115 ? 36.528 -16.073 -0.416  1.00 11.85 ?  115 ASN   B CB   1 
ATOM   5711 C  CG   . ASN   B 1 115 ? 36.260 -15.812 1.044   1.00 12.70 ?  115 ASN   B CG   1 
ATOM   5712 O  OD1  . ASN   B 1 115 ? 36.257 -14.664 1.483   1.00 14.34 ?  115 ASN   B OD1  1 
ATOM   5713 N  ND2  . ASN   B 1 115 ? 36.099 -16.881 1.825   1.00 12.49 ?  115 ASN   B ND2  1 
ATOM   5714 H  H    . ASN   B 1 115 ? 34.529 -17.495 -0.383  1.00 13.37 ?  115 ASN   B H    1 
ATOM   5715 H  HA   . ASN   B 1 115 ? 34.902 -15.032 -1.108  1.00 13.25 ?  115 ASN   B HA   1 
ATOM   5716 H  HB2  . ASN   B 1 115 ? 36.854 -16.981 -0.506  1.00 14.19 ?  115 ASN   B HB2  1 
ATOM   5717 H  HB3  . ASN   B 1 115 ? 37.206 -15.445 -0.706  1.00 14.19 ?  115 ASN   B HB3  1 
ATOM   5718 H  HD21 . ASN   B 1 115 ? 35.953 -16.780 2.668   1.00 14.96 ?  115 ASN   B HD21 1 
ATOM   5719 H  HD22 . ASN   B 1 115 ? 36.125 -17.672 1.487   1.00 14.96 ?  115 ASN   B HD22 1 
ATOM   5720 N  N    . PHE   B 1 116 ? 35.665 -17.103 -3.398  1.00 10.67 ?  116 PHE   B N    1 
ATOM   5721 C  CA   . PHE   B 1 116 ? 36.099 -17.195 -4.785  1.00 11.06 ?  116 PHE   B CA   1 
ATOM   5722 C  C    . PHE   B 1 116 ? 35.200 -16.369 -5.697  1.00 10.72 ?  116 PHE   B C    1 
ATOM   5723 O  O    . PHE   B 1 116 ? 35.636 -15.942 -6.770  1.00 11.35 ?  116 PHE   B O    1 
ATOM   5724 C  CB   . PHE   B 1 116 ? 36.060 -18.643 -5.300  1.00 10.91 ?  116 PHE   B CB   1 
ATOM   5725 C  CG   . PHE   B 1 116 ? 37.131 -19.594 -4.761  1.00 10.89 ?  116 PHE   B CG   1 
ATOM   5726 C  CD1  . PHE   B 1 116 ? 37.787 -19.410 -3.557  1.00 11.87 ?  116 PHE   B CD1  1 
ATOM   5727 C  CD2  . PHE   B 1 116 ? 37.437 -20.729 -5.501  1.00 11.37 ?  116 PHE   B CD2  1 
ATOM   5728 C  CE1  . PHE   B 1 116 ? 38.717 -20.342 -3.105  1.00 11.76 ?  116 PHE   B CE1  1 
ATOM   5729 C  CE2  . PHE   B 1 116 ? 38.364 -21.663 -5.055  1.00 11.18 ?  116 PHE   B CE2  1 
ATOM   5730 C  CZ   . PHE   B 1 116 ? 39.001 -21.469 -3.862  1.00 11.63 ?  116 PHE   B CZ   1 
ATOM   5731 H  H    . PHE   B 1 116 ? 35.399 -17.852 -3.053  1.00 12.77 ?  116 PHE   B H    1 
ATOM   5732 H  HA   . PHE   B 1 116 ? 37.007 -16.870 -4.866  1.00 13.24 ?  116 PHE   B HA   1 
ATOM   5733 H  HB2  . PHE   B 1 116 ? 35.192 -19.026 -5.070  1.00 13.07 ?  116 PHE   B HB2  1 
ATOM   5734 H  HB3  . PHE   B 1 116 ? 36.147 -18.629 -6.267  1.00 13.07 ?  116 PHE   B HB3  1 
ATOM   5735 H  HD1  . PHE   B 1 116 ? 37.583 -18.668 -3.037  1.00 14.22 ?  116 PHE   B HD1  1 
ATOM   5736 H  HD2  . PHE   B 1 116 ? 36.998 -20.882 -6.309  1.00 13.62 ?  116 PHE   B HD2  1 
ATOM   5737 H  HE1  . PHE   B 1 116 ? 39.153 -20.208 -2.297  1.00 14.08 ?  116 PHE   B HE1  1 
ATOM   5738 H  HE2  . PHE   B 1 116 ? 38.560 -22.411 -5.572  1.00 13.39 ?  116 PHE   B HE2  1 
ATOM   5739 H  HZ   . PHE   B 1 116 ? 39.639 -22.079 -3.568  1.00 13.92 ?  116 PHE   B HZ   1 
ATOM   5740 N  N    . ASN   B 1 117 ? 33.931 -16.162 -5.311  1.00 11.31 ?  117 ASN   B N    1 
ATOM   5741 C  CA   . ASN   B 1 117 ? 32.985 -15.461 -6.178  1.00 11.54 ?  117 ASN   B CA   1 
ATOM   5742 C  C    . ASN   B 1 117 ? 33.299 -13.982 -6.333  1.00 11.69 ?  117 ASN   B C    1 
ATOM   5743 O  O    . ASN   B 1 117 ? 32.702 -13.331 -7.192  1.00 13.13 ?  117 ASN   B O    1 
ATOM   5744 C  CB   . ASN   B 1 117 ? 31.555 -15.684 -5.692  1.00 11.57 ?  117 ASN   B CB   1 
ATOM   5745 C  CG   . ASN   B 1 117 ? 31.109 -17.095 -5.939  1.00 11.77 ?  117 ASN   B CG   1 
ATOM   5746 O  OD1  . ASN   B 1 117 ? 31.462 -17.686 -6.962  1.00 12.84 ?  117 ASN   B OD1  1 
ATOM   5747 N  ND2  . ASN   B 1 117 ? 30.375 -17.667 -4.997  1.00 11.94 ?  117 ASN   B ND2  1 
ATOM   5748 H  H    . ASN   B 1 117 ? 33.607 -16.414 -4.549  1.00 13.54 ?  117 ASN   B H    1 
ATOM   5749 H  HA   . ASN   B 1 117 ? 33.050 -15.862 -7.054  1.00 13.81 ?  117 ASN   B HA   1 
ATOM   5750 H  HB2  . ASN   B 1 117 ? 31.509 -15.512 -4.734  1.00 13.86 ?  117 ASN   B HB2  1 
ATOM   5751 H  HB3  . ASN   B 1 117 ? 30.962 -15.080 -6.165  1.00 13.86 ?  117 ASN   B HB3  1 
ATOM   5752 H  HD21 . ASN   B 1 117 ? 30.096 -18.475 -5.098  1.00 14.30 ?  117 ASN   B HD21 1 
ATOM   5753 H  HD22 . ASN   B 1 117 ? 30.155 -17.225 -4.291  1.00 14.30 ?  117 ASN   B HD22 1 
ATOM   5754 N  N    . GLN   B 1 118 ? 34.237 -13.457 -5.561  1.00 11.54 ?  118 GLN   B N    1 
ATOM   5755 C  CA   . GLN   B 1 118 ? 34.655 -12.072 -5.703  1.00 11.98 ?  118 GLN   B CA   1 
ATOM   5756 C  C    . GLN   B 1 118 ? 35.725 -11.883 -6.771  1.00 12.38 ?  118 GLN   B C    1 
ATOM   5757 O  O    . GLN   B 1 118 ? 36.191 -10.757 -6.958  1.00 13.77 ?  118 GLN   B O    1 
ATOM   5758 C  CB   . GLN   B 1 118 ? 35.135 -11.535 -4.355  1.00 12.73 ?  118 GLN   B CB   1 
ATOM   5759 C  CG   . GLN   B 1 118 ? 34.057 -11.581 -3.286  1.00 12.98 ?  118 GLN   B CG   1 
ATOM   5760 C  CD   . GLN   B 1 118 ? 32.885 -10.669 -3.610  1.00 12.90 ?  118 GLN   B CD   1 
ATOM   5761 O  OE1  . GLN   B 1 118 ? 33.073 -9.529  -4.050  1.00 13.49 ?  118 GLN   B OE1  1 
ATOM   5762 N  NE2  . GLN   B 1 118 ? 31.669 -11.161 -3.400  1.00 13.04 ?  118 GLN   B NE2  1 
ATOM   5763 H  H    . GLN   B 1 118 ? 34.669 -13.885 -4.947  1.00 13.82 ?  118 GLN   B H    1 
ATOM   5764 H  HA   . GLN   B 1 118 ? 33.887 -11.547 -5.978  1.00 14.35 ?  118 GLN   B HA   1 
ATOM   5765 H  HB2  . GLN   B 1 118 ? 35.886 -12.059 -4.050  1.00 15.25 ?  118 GLN   B HB2  1 
ATOM   5766 H  HB3  . GLN   B 1 118 ? 35.404 -10.603 -4.463  1.00 15.25 ?  118 GLN   B HB3  1 
ATOM   5767 H  HG2  . GLN   B 1 118 ? 33.724 -12.489 -3.213  1.00 15.55 ?  118 GLN   B HG2  1 
ATOM   5768 H  HG3  . GLN   B 1 118 ? 34.437 -11.297 -2.440  1.00 15.55 ?  118 GLN   B HG3  1 
ATOM   5769 H  HE21 . GLN   B 1 118 ? 31.577 -11.962 -3.095  1.00 15.62 ?  118 GLN   B HE21 1 
ATOM   5770 H  HE22 . GLN   B 1 118 ? 30.979 -10.683 -3.571  1.00 15.62 ?  118 GLN   B HE22 1 
ATOM   5771 N  N    . HIS   B 1 119 ? 36.091 -12.940 -7.498  1.00 11.43 ?  119 HIS   B N    1 
ATOM   5772 C  CA   . HIS   B 1 119 ? 37.129 -12.885 -8.520  1.00 12.01 ?  119 HIS   B CA   1 
ATOM   5773 C  C    . HIS   B 1 119 ? 36.647 -13.620 -9.756  1.00 11.96 ?  119 HIS   B C    1 
ATOM   5774 O  O    . HIS   B 1 119 ? 36.132 -14.733 -9.648  1.00 12.65 ?  119 HIS   B O    1 
ATOM   5775 C  CB   . HIS   B 1 119 ? 38.411 -13.513 -7.980  1.00 12.60 ?  119 HIS   B CB   1 
ATOM   5776 C  CG   . HIS   B 1 119 ? 38.893 -12.814 -6.759  1.00 13.71 ?  119 HIS   B CG   1 
ATOM   5777 N  ND1  . HIS   B 1 119 ? 39.685 -11.687 -6.818  1.00 15.28 ?  119 HIS   B ND1  1 
ATOM   5778 C  CD2  . HIS   B 1 119 ? 38.608 -13.011 -5.452  1.00 14.77 ?  119 HIS   B CD2  1 
ATOM   5779 C  CE1  . HIS   B 1 119 ? 39.897 -11.244 -5.593  1.00 16.53 ?  119 HIS   B CE1  1 
ATOM   5780 N  NE2  . HIS   B 1 119 ? 39.250 -12.024 -4.747  1.00 16.32 ?  119 HIS   B NE2  1 
ATOM   5781 H  H    . HIS   B 1 119 ? 35.736 -13.725 -7.421  1.00 13.69 ?  119 HIS   B H    1 
ATOM   5782 H  HA   . HIS   B 1 119 ? 37.306 -11.962 -8.760  1.00 14.38 ?  119 HIS   B HA   1 
ATOM   5783 H  HB2  . HIS   B 1 119 ? 38.245 -14.437 -7.760  1.00 15.09 ?  119 HIS   B HB2  1 
ATOM   5784 H  HB3  . HIS   B 1 119 ? 39.103 -13.446 -8.662  1.00 15.09 ?  119 HIS   B HB3  1 
ATOM   5785 H  HD2  . HIS   B 1 119 ? 38.082 -13.693 -5.102  1.00 17.69 ?  119 HIS   B HD2  1 
ATOM   5786 H  HE1  . HIS   B 1 119 ? 40.425 -10.512 -5.360  1.00 19.81 ?  119 HIS   B HE1  1 
ATOM   5787 H  HE2  . HIS   B 1 119 ? 39.259 -11.948 -3.890  1.00 19.55 ?  119 HIS   B HE2  1 
ATOM   5788 N  N    . GLU   B 1 120 ? 36.799 -13.010 -10.930 1.00 12.60 ?  120 GLU   B N    1 
ATOM   5789 C  CA   . GLU   B 1 120 ? 36.208 -13.595 -12.129 1.00 13.85 ?  120 GLU   B CA   1 
ATOM   5790 C  C    . GLU   B 1 120 ? 36.888 -14.893 -12.539 1.00 12.81 ?  120 GLU   B C    1 
ATOM   5791 O  O    . GLU   B 1 120 ? 36.228 -15.767 -13.112 1.00 12.95 ?  120 GLU   B O    1 
ATOM   5792 C  CB   . GLU   B 1 120 ? 36.214 -12.593 -13.282 1.00 18.94 ?  120 GLU   B CB   1 
ATOM   5793 C  CG   . GLU   B 1 120 ? 35.268 -11.427 -13.060 1.00 25.30 ?  120 GLU   B CG   1 
ATOM   5794 C  CD   . GLU   B 1 120 ? 35.127 -10.537 -14.280 1.00 31.47 ?  120 GLU   B CD   1 
ATOM   5795 O  OE1  . GLU   B 1 120 ? 36.121 -10.371 -15.018 1.00 33.68 ?  120 GLU   B OE1  1 
ATOM   5796 O  OE2  . GLU   B 1 120 ? 34.017 -10.009 -14.499 1.00 34.46 -1 120 GLU   B OE2  1 
ATOM   5797 H  H    . GLU   B 1 120 ? 37.227 -12.269 -11.061 1.00 15.09 ?  120 GLU   B H    1 
ATOM   5798 H  HA   . GLU   B 1 120 ? 35.288 -13.809 -11.940 1.00 16.59 ?  120 GLU   B HA   1 
ATOM   5799 H  HB2  . GLU   B 1 120 ? 37.106 -12.234 -13.389 1.00 22.69 ?  120 GLU   B HB2  1 
ATOM   5800 H  HB3  . GLU   B 1 120 ? 35.938 -13.046 -14.096 1.00 22.69 ?  120 GLU   B HB3  1 
ATOM   5801 H  HG2  . GLU   B 1 120 ? 34.385 -11.770 -12.847 1.00 30.33 ?  120 GLU   B HG2  1 
ATOM   5802 H  HG3  . GLU   B 1 120 ? 35.598 -10.886 -12.327 1.00 30.33 ?  120 GLU   B HG3  1 
ATOM   5803 N  N    . VAL   B 1 121 ? 38.189 -15.033 -12.276 1.00 12.52 ?  121 VAL   B N    1 
ATOM   5804 C  CA   . VAL   B 1 121 ? 38.935 -16.242 -12.623 1.00 12.42 ?  121 VAL   B CA   1 
ATOM   5805 C  C    . VAL   B 1 121 ? 40.046 -16.450 -11.603 1.00 11.92 ?  121 VAL   B C    1 
ATOM   5806 O  O    . VAL   B 1 121 ? 40.728 -15.494 -11.210 1.00 12.52 ?  121 VAL   B O    1 
ATOM   5807 C  CB   . VAL   B 1 121 ? 39.458 -16.200 -14.079 1.00 14.07 ?  121 VAL   B CB   1 
ATOM   5808 C  CG1  . VAL   B 1 121 ? 40.324 -14.969 -14.333 1.00 15.49 ?  121 VAL   B CG1  1 
ATOM   5809 C  CG2  . VAL   B 1 121 ? 40.200 -17.484 -14.428 1.00 15.66 ?  121 VAL   B CG2  1 
ATOM   5810 H  H    . VAL   B 1 121 ? 38.675 -14.431 -11.898 1.00 14.99 ?  121 VAL   B H    1 
ATOM   5811 H  HA   . VAL   B 1 121 ? 38.330 -16.995 -12.562 1.00 14.88 ?  121 VAL   B HA   1 
ATOM   5812 H  HB   . VAL   B 1 121 ? 38.694 -16.143 -14.679 1.00 16.86 ?  121 VAL   B HB   1 
ATOM   5813 H  HG11 . VAL   B 1 121 ? 40.636 -14.985 -15.252 1.00 18.55 ?  121 VAL   B HG11 1 
ATOM   5814 H  HG12 . VAL   B 1 121 ? 39.793 -14.173 -14.179 1.00 18.55 ?  121 VAL   B HG12 1 
ATOM   5815 H  HG13 . VAL   B 1 121 ? 41.081 -14.986 -13.728 1.00 18.55 ?  121 VAL   B HG13 1 
ATOM   5816 H  HG21 . VAL   B 1 121 ? 40.400 -17.485 -15.380 1.00 18.76 ?  121 VAL   B HG21 1 
ATOM   5817 H  HG22 . VAL   B 1 121 ? 41.026 -17.521 -13.921 1.00 18.76 ?  121 VAL   B HG22 1 
ATOM   5818 H  HG23 . VAL   B 1 121 ? 39.641 -18.244 -14.210 1.00 18.76 ?  121 VAL   B HG23 1 
ATOM   5819 N  N    . LEU   B 1 122 ? 40.225 -17.705 -11.169 1.00 11.45 ?  122 LEU   B N    1 
ATOM   5820 C  CA   . LEU   B 1 122 ? 41.211 -18.056 -10.151 1.00 11.02 ?  122 LEU   B CA   1 
ATOM   5821 C  C    . LEU   B 1 122 ? 41.866 -19.388 -10.472 1.00 10.98 ?  122 LEU   B C    1 
ATOM   5822 O  O    . LEU   B 1 122 ? 41.209 -20.309 -10.974 1.00 12.08 ?  122 LEU   B O    1 
ATOM   5823 C  CB   . LEU   B 1 122 ? 40.569 -18.270 -8.769  1.00 12.83 ?  122 LEU   B CB   1 
ATOM   5824 C  CG   . LEU   B 1 122 ? 39.526 -17.260 -8.278  1.00 12.83 ?  122 LEU   B CG   1 
ATOM   5825 C  CD1  . LEU   B 1 122 ? 38.124 -17.605 -8.763  1.00 14.01 ?  122 LEU   B CD1  1 
ATOM   5826 C  CD2  . LEU   B 1 122 ? 39.563 -17.140 -6.767  1.00 12.27 ?  122 LEU   B CD2  1 
ATOM   5827 H  H    . LEU   B 1 122 ? 39.778 -18.382 -11.459 1.00 13.71 ?  122 LEU   B H    1 
ATOM   5828 H  HA   . LEU   B 1 122 ? 41.890 -17.364 -10.085 1.00 13.19 ?  122 LEU   B HA   1 
ATOM   5829 H  HB2  . LEU   B 1 122 ? 40.133 -19.133 -8.775  1.00 15.37 ?  122 LEU   B HB2  1 
ATOM   5830 H  HB3  . LEU   B 1 122 ? 41.278 -18.275 -8.109  1.00 15.37 ?  122 LEU   B HB3  1 
ATOM   5831 H  HG   . LEU   B 1 122 ? 39.751 -16.387 -8.639  1.00 15.37 ?  122 LEU   B HG   1 
ATOM   5832 H  HD11 . LEU   B 1 122 ? 37.495 -16.972 -8.381  1.00 16.78 ?  122 LEU   B HD11 1 
ATOM   5833 H  HD12 . LEU   B 1 122 ? 38.103 -17.540 -9.733  1.00 16.78 ?  122 LEU   B HD12 1 
ATOM   5834 H  HD13 . LEU   B 1 122 ? 37.905 -18.503 -8.485  1.00 16.78 ?  122 LEU   B HD13 1 
ATOM   5835 H  HD21 . LEU   B 1 122 ? 38.880 -16.515 -6.478  1.00 14.69 ?  122 LEU   B HD21 1 
ATOM   5836 H  HD22 . LEU   B 1 122 ? 39.403 -18.012 -6.375  1.00 14.69 ?  122 LEU   B HD22 1 
ATOM   5837 H  HD23 . LEU   B 1 122 ? 40.440 -16.815 -6.496  1.00 14.69 ?  122 LEU   B HD23 1 
ATOM   5838 N  N    . LEU   B 1 123 ? 43.153 -19.493 -10.118 1.00 10.70 ?  123 LEU   B N    1 
ATOM   5839 C  CA   . LEU   B 1 123 ? 43.868 -20.759 -9.999  1.00 11.08 ?  123 LEU   B CA   1 
ATOM   5840 C  C    . LEU   B 1 123 ? 43.839 -21.146 -8.527  1.00 10.90 ?  123 LEU   B C    1 
ATOM   5841 O  O    . LEU   B 1 123 ? 44.196 -20.322 -7.676  1.00 11.09 ?  123 LEU   B O    1 
ATOM   5842 C  CB   . LEU   B 1 123 ? 45.318 -20.578 -10.457 1.00 11.53 ?  123 LEU   B CB   1 
ATOM   5843 C  CG   . LEU   B 1 123 ? 46.267 -21.755 -10.205 1.00 11.87 ?  123 LEU   B CG   1 
ATOM   5844 C  CD1  . LEU   B 1 123 ? 45.849 -23.009 -10.980 1.00 12.68 ?  123 LEU   B CD1  1 
ATOM   5845 C  CD2  . LEU   B 1 123 ? 47.682 -21.357 -10.570 1.00 12.95 ?  123 LEU   B CD2  1 
ATOM   5846 H  H    . LEU   B 1 123 ? 43.650 -18.812 -9.927  1.00 12.81 ?  123 LEU   B H    1 
ATOM   5847 H  HA   . LEU   B 1 123 ? 43.434 -21.450 -10.526 1.00 13.27 ?  123 LEU   B HA   1 
ATOM   5848 H  HB2  . LEU   B 1 123 ? 45.310 -20.418 -11.414 1.00 13.80 ?  123 LEU   B HB2  1 
ATOM   5849 H  HB3  . LEU   B 1 123 ? 45.686 -19.810 -10.002 1.00 13.80 ?  123 LEU   B HB3  1 
ATOM   5850 H  HG   . LEU   B 1 123 ? 46.260 -21.977 -9.260  1.00 14.21 ?  123 LEU   B HG   1 
ATOM   5851 H  HD11 . LEU   B 1 123 ? 46.487 -23.716 -10.799 1.00 15.19 ?  123 LEU   B HD11 1 
ATOM   5852 H  HD12 . LEU   B 1 123 ? 44.964 -23.276 -10.690 1.00 15.19 ?  123 LEU   B HD12 1 
ATOM   5853 H  HD13 . LEU   B 1 123 ? 45.841 -22.802 -11.927 1.00 15.19 ?  123 LEU   B HD13 1 
ATOM   5854 H  HD21 . LEU   B 1 123 ? 48.274 -22.108 -10.409 1.00 15.51 ?  123 LEU   B HD21 1 
ATOM   5855 H  HD22 . LEU   B 1 123 ? 47.708 -21.112 -11.509 1.00 15.51 ?  123 LEU   B HD22 1 
ATOM   5856 H  HD23 . LEU   B 1 123 ? 47.947 -20.601 -10.024 1.00 15.51 ?  123 LEU   B HD23 1 
ATOM   5857 N  N    . ALA   B 1 124 ? 43.408 -22.377 -8.218  1.00 10.76 ?  124 ALA   B N    1 
ATOM   5858 C  CA   . ALA   B 1 124 ? 43.146 -22.701 -6.823  1.00 10.85 ?  124 ALA   B CA   1 
ATOM   5859 C  C    . ALA   B 1 124 ? 43.412 -24.162 -6.491  1.00 10.75 ?  124 ALA   B C    1 
ATOM   5860 O  O    . ALA   B 1 124 ? 43.286 -25.038 -7.360  1.00 11.36 ?  124 ALA   B O    1 
ATOM   5861 C  CB   . ALA   B 1 124 ? 41.688 -22.382 -6.458  1.00 11.16 ?  124 ALA   B CB   1 
ATOM   5862 H  H    . ALA   B 1 124 ? 43.254 -23.023 -8.778  1.00 12.88 ?  124 ALA   B H    1 
ATOM   5863 H  HA   . ALA   B 1 124 ? 43.719 -22.148 -6.273  1.00 12.99 ?  124 ALA   B HA   1 
ATOM   5864 H  HB1  . ALA   B 1 124 ? 41.536 -22.595 -5.525  1.00 13.36 ?  124 ALA   B HB1  1 
ATOM   5865 H  HB2  . ALA   B 1 124 ? 41.528 -21.432 -6.607  1.00 13.36 ?  124 ALA   B HB2  1 
ATOM   5866 H  HB3  . ALA   B 1 124 ? 41.097 -22.904 -7.020  1.00 13.36 ?  124 ALA   B HB3  1 
ATOM   5867 N  N    . PRO   B 1 125 ? 43.717 -24.453 -5.230  1.00 10.93 ?  125 PRO   B N    1 
ATOM   5868 C  CA   . PRO   B 1 125 ? 43.657 -25.818 -4.709  1.00 11.69 ?  125 PRO   B CA   1 
ATOM   5869 C  C    . PRO   B 1 125 ? 42.258 -26.090 -4.161  1.00 11.45 ?  125 PRO   B C    1 
ATOM   5870 O  O    . PRO   B 1 125 ? 41.464 -25.173 -3.947  1.00 12.26 ?  125 PRO   B O    1 
ATOM   5871 C  CB   . PRO   B 1 125 ? 44.648 -25.742 -3.541  1.00 12.76 ?  125 PRO   B CB   1 
ATOM   5872 C  CG   . PRO   B 1 125 ? 44.396 -24.351 -2.970  1.00 12.63 ?  125 PRO   B CG   1 
ATOM   5873 C  CD   . PRO   B 1 125 ? 44.051 -23.482 -4.170  1.00 11.68 ?  125 PRO   B CD   1 
ATOM   5874 H  HA   . PRO   B 1 125 ? 43.930 -26.484 -5.357  1.00 14.00 ?  125 PRO   B HA   1 
ATOM   5875 H  HB2  . PRO   B 1 125 ? 44.448 -26.425 -2.881  1.00 15.28 ?  125 PRO   B HB2  1 
ATOM   5876 H  HB3  . PRO   B 1 125 ? 45.558 -25.821 -3.862  1.00 15.28 ?  125 PRO   B HB3  1 
ATOM   5877 H  HG2  . PRO   B 1 125 ? 43.652 -24.379 -2.345  1.00 15.12 ?  125 PRO   B HG2  1 
ATOM   5878 H  HG3  . PRO   B 1 125 ? 45.198 -24.026 -2.523  1.00 15.12 ?  125 PRO   B HG3  1 
ATOM   5879 H  HD2  . PRO   B 1 125 ? 43.293 -22.914 -3.974  1.00 13.99 ?  125 PRO   B HD2  1 
ATOM   5880 H  HD3  . PRO   B 1 125 ? 44.830 -22.950 -4.429  1.00 13.99 ?  125 PRO   B HD3  1 
ATOM   5881 N  N    . LEU   B 1 126 ? 41.987 -27.370 -3.882  1.00 12.30 ?  126 LEU   B N    1 
ATOM   5882 C  CA   . LEU   B 1 126 ? 40.768 -27.740 -3.168  1.00 12.80 ?  126 LEU   B CA   1 
ATOM   5883 C  C    . LEU   B 1 126 ? 40.881 -27.337 -1.706  1.00 12.78 ?  126 LEU   B C    1 
ATOM   5884 O  O    . LEU   B 1 126 ? 41.768 -27.803 -0.985  1.00 14.66 ?  126 LEU   B O    1 
ATOM   5885 C  CB   . LEU   B 1 126 ? 40.516 -29.239 -3.274  1.00 14.07 ?  126 LEU   B CB   1 
ATOM   5886 C  CG   . LEU   B 1 126 ? 39.985 -29.721 -4.622  1.00 15.00 ?  126 LEU   B CG   1 
ATOM   5887 C  CD1  . LEU   B 1 126 ? 40.036 -31.232 -4.699  1.00 17.00 ?  126 LEU   B CD1  1 
ATOM   5888 C  CD2  . LEU   B 1 126 ? 38.569 -29.224 -4.868  1.00 15.58 ?  126 LEU   B CD2  1 
ATOM   5889 H  H    . LEU   B 1 126 ? 42.494 -28.035 -4.082  1.00 14.73 ?  126 LEU   B H    1 
ATOM   5890 H  HA   . LEU   B 1 126 ? 40.015 -27.270 -3.556  1.00 15.33 ?  126 LEU   B HA   1 
ATOM   5891 H  HB2  . LEU   B 1 126 ? 41.348 -29.701 -3.102  1.00 16.85 ?  126 LEU   B HB2  1 
ATOM   5892 H  HB3  . LEU   B 1 126 ? 39.861 -29.485 -2.600  1.00 16.85 ?  126 LEU   B HB3  1 
ATOM   5893 H  HG   . LEU   B 1 126 ? 40.555 -29.368 -5.326  1.00 17.96 ?  126 LEU   B HG   1 
ATOM   5894 H  HD11 . LEU   B 1 126 ? 39.696 -31.517 -5.562  1.00 20.37 ?  126 LEU   B HD11 1 
ATOM   5895 H  HD12 . LEU   B 1 126 ? 40.952 -31.527 -4.589  1.00 20.37 ?  126 LEU   B HD12 1 
ATOM   5896 H  HD13 . LEU   B 1 126 ? 39.483 -31.602 -3.990  1.00 20.37 ?  126 LEU   B HD13 1 
ATOM   5897 H  HD21 . LEU   B 1 126 ? 38.220 -29.647 -5.667  1.00 18.66 ?  126 LEU   B HD21 1 
ATOM   5898 H  HD22 . LEU   B 1 126 ? 38.018 -29.452 -4.104  1.00 18.66 ?  126 LEU   B HD22 1 
ATOM   5899 H  HD23 . LEU   B 1 126 ? 38.587 -28.260 -4.986  1.00 18.66 ?  126 LEU   B HD23 1 
ATOM   5900 N  N    . LEU   B 1 127 ? 39.955 -26.501 -1.252  1.00 12.71 ?  127 LEU   B N    1 
ATOM   5901 C  CA   . LEU   B 1 127 ? 40.008 -26.009 0.112   1.00 13.21 ?  127 LEU   B CA   1 
ATOM   5902 C  C    . LEU   B 1 127 ? 39.737 -27.130 1.106   1.00 12.77 ?  127 LEU   B C    1 
ATOM   5903 O  O    . LEU   B 1 127 ? 38.915 -28.024 0.874   1.00 13.11 ?  127 LEU   B O    1 
ATOM   5904 C  CB   . LEU   B 1 127 ? 38.989 -24.890 0.317   1.00 13.54 ?  127 LEU   B CB   1 
ATOM   5905 C  CG   . LEU   B 1 127 ? 39.166 -23.622 -0.520  1.00 14.36 ?  127 LEU   B CG   1 
ATOM   5906 C  CD1  . LEU   B 1 127 ? 38.047 -22.658 -0.184  1.00 14.60 ?  127 LEU   B CD1  1 
ATOM   5907 C  CD2  . LEU   B 1 127 ? 40.524 -22.979 -0.284  1.00 15.23 ?  127 LEU   B CD2  1 
ATOM   5908 H  H    . LEU   B 1 127 ? 39.291 -26.196 -1.713  1.00 15.22 ?  127 LEU   B H    1 
ATOM   5909 H  HA   . LEU   B 1 127 ? 40.894 -25.647 0.288   1.00 15.82 ?  127 LEU   B HA   1 
ATOM   5910 H  HB2  . LEU   B 1 127 ? 38.109 -25.239 0.117   1.00 16.21 ?  127 LEU   B HB2  1 
ATOM   5911 H  HB3  . LEU   B 1 127 ? 39.020 -24.617 1.248   1.00 16.21 ?  127 LEU   B HB3  1 
ATOM   5912 H  HG   . LEU   B 1 127 ? 39.086 -23.838 -1.460  1.00 17.20 ?  127 LEU   B HG   1 
ATOM   5913 H  HD11 . LEU   B 1 127 ? 38.155 -21.846 -0.709  1.00 17.49 ?  127 LEU   B HD11 1 
ATOM   5914 H  HD12 . LEU   B 1 127 ? 37.195 -23.071 -0.389  1.00 17.49 ?  127 LEU   B HD12 1 
ATOM   5915 H  HD13 . LEU   B 1 127 ? 38.090 -22.440 0.763   1.00 17.49 ?  127 LEU   B HD13 1 
ATOM   5916 H  HD21 . LEU   B 1 127 ? 40.559 -22.124 -0.750  1.00 18.24 ?  127 LEU   B HD21 1 
ATOM   5917 H  HD22 . LEU   B 1 127 ? 40.648 -22.835 0.668   1.00 18.24 ?  127 LEU   B HD22 1 
ATOM   5918 H  HD23 . LEU   B 1 127 ? 41.212 -23.566 -0.624  1.00 18.24 ?  127 LEU   B HD23 1 
ATOM   5919 N  N    . SER   B 1 128 ? 40.419 -27.046 2.237   1.00 13.13 ?  128 SER   B N    1 
ATOM   5920 C  CA   . SER   B 1 128 ? 40.312 -27.965 3.358   1.00 13.65 ?  128 SER   B CA   1 
ATOM   5921 C  C    . SER   B 1 128 ? 40.807 -29.372 3.039   1.00 14.51 ?  128 SER   B C    1 
ATOM   5922 O  O    . SER   B 1 128 ? 40.710 -30.251 3.893   1.00 15.98 ?  128 SER   B O    1 
ATOM   5923 C  CB   . SER   B 1 128 ? 38.911 -27.975 3.988   1.00 13.78 ?  128 SER   B CB   1 
ATOM   5924 O  OG   . SER   B 1 128 ? 38.589 -26.696 4.530   1.00 14.56 ?  128 SER   B OG   1 
ATOM   5925 H  H    . SER   B 1 128 ? 40.986 -26.419 2.385   1.00 15.72 ?  128 SER   B H    1 
ATOM   5926 H  HA   . SER   B 1 128 ? 40.896 -27.627 4.043   1.00 16.35 ?  128 SER   B HA   1 
ATOM   5927 H  HB2  . SER   B 1 128 ? 38.251 -28.215 3.316   1.00 16.50 ?  128 SER   B HB2  1 
ATOM   5928 H  HB3  . SER   B 1 128 ? 38.892 -28.642 4.707   1.00 16.50 ?  128 SER   B HB3  1 
ATOM   5929 H  HG   . SER   B 1 128 ? 39.151 -26.493 5.119   1.00 17.44 ?  128 SER   B HG   1 
ATOM   5930 N  N    . ALA   B 1 129 ? 41.375 -29.601 1.853   1.00 15.76 ?  129 ALA   B N    1 
ATOM   5931 C  CA   . ALA   B 1 129 ? 41.914 -30.906 1.507   1.00 16.59 ?  129 ALA   B CA   1 
ATOM   5932 C  C    . ALA   B 1 129 ? 43.312 -31.076 2.093   1.00 15.74 ?  129 ALA   B C    1 
ATOM   5933 O  O    . ALA   B 1 129 ? 43.868 -30.176 2.736   1.00 15.42 ?  129 ALA   B O    1 
ATOM   5934 C  CB   . ALA   B 1 129 ? 41.948 -31.081 -0.009  1.00 18.61 ?  129 ALA   B CB   1 
ATOM   5935 H  H    . ALA   B 1 129 ? 41.455 -29.013 1.227   1.00 18.88 ?  129 ALA   B H    1 
ATOM   5936 H  HA   . ALA   B 1 129 ? 41.343 -31.596 1.877   1.00 19.87 ?  129 ALA   B HA   1 
ATOM   5937 H  HB1  . ALA   B 1 129 ? 42.301 -31.962 -0.216  1.00 22.30 ?  129 ALA   B HB1  1 
ATOM   5938 H  HB2  . ALA   B 1 129 ? 41.050 -30.994 -0.357  1.00 22.30 ?  129 ALA   B HB2  1 
ATOM   5939 H  HB3  . ALA   B 1 129 ? 42.523 -30.398 -0.391  1.00 22.30 ?  129 ALA   B HB3  1 
ATOM   5940 N  N    . GLY   B 1 130 ? 43.885 -32.254 1.852   1.00 15.63 ?  130 GLY   B N    1 
ATOM   5941 C  CA   . GLY   B 1 130 ? 45.270 -32.489 2.213   1.00 16.11 ?  130 GLY   B CA   1 
ATOM   5942 C  C    . GLY   B 1 130 ? 45.475 -32.392 3.705   1.00 16.27 ?  130 GLY   B C    1 
ATOM   5943 O  O    . GLY   B 1 130 ? 44.771 -33.029 4.498   1.00 17.12 ?  130 GLY   B O    1 
ATOM   5944 H  H    . GLY   B 1 130 ? 43.494 -32.924 1.478   1.00 18.72 ?  130 GLY   B H    1 
ATOM   5945 H  HA2  . GLY   B 1 130 ? 45.536 -33.376 1.921   1.00 19.30 ?  130 GLY   B HA2  1 
ATOM   5946 H  HA3  . GLY   B 1 130 ? 45.836 -31.836 1.778   1.00 19.30 ?  130 GLY   B HA3  1 
ATOM   5947 N  N    . ILE   B 1 131 ? 46.450 -31.567 4.097   1.00 16.59 ?  131 ILE   B N    1 
ATOM   5948 C  CA   . ILE   B 1 131 ? 46.806 -31.429 5.499   1.00 17.56 ?  131 ILE   B CA   1 
ATOM   5949 C  C    . ILE   B 1 131 ? 45.688 -30.828 6.332   1.00 16.68 ?  131 ILE   B C    1 
ATOM   5950 O  O    . ILE   B 1 131 ? 45.758 -30.887 7.561   1.00 18.12 ?  131 ILE   B O    1 
ATOM   5951 C  CB   . ILE   B 1 131 ? 48.129 -30.647 5.690   1.00 19.63 ?  131 ILE   B CB   1 
ATOM   5952 C  CG1  . ILE   B 1 131 ? 47.957 -29.163 5.329   1.00 20.63 ?  131 ILE   B CG1  1 
ATOM   5953 C  CG2  . ILE   B 1 131 ? 49.241 -31.281 4.864   1.00 20.90 ?  131 ILE   B CG2  1 
ATOM   5954 C  CD1  . ILE   B 1 131 ? 49.184 -28.310 5.631   1.00 21.67 ?  131 ILE   B CD1  1 
ATOM   5955 H  H    . ILE   B 1 131 ? 46.920 -31.081 3.564   1.00 19.87 ?  131 ILE   B H    1 
ATOM   5956 H  HA   . ILE   B 1 131 ? 46.954 -32.314 5.853   1.00 21.04 ?  131 ILE   B HA   1 
ATOM   5957 H  HB   . ILE   B 1 131 ? 48.372 -30.703 6.629   1.00 23.52 ?  131 ILE   B HB   1 
ATOM   5958 H  HG12 . ILE   B 1 131 ? 47.771 -29.094 4.381   1.00 24.72 ?  131 ILE   B HG12 1 
ATOM   5959 H  HG13 . ILE   B 1 131 ? 47.215 -28.792 5.835   1.00 24.72 ?  131 ILE   B HG13 1 
ATOM   5960 H  HG21 . ILE   B 1 131 ? 50.083 -30.884 5.122   1.00 25.05 ?  131 ILE   B HG21 1 
ATOM   5961 H  HG22 . ILE   B 1 131 ? 49.250 -32.233 5.034   1.00 25.05 ?  131 ILE   B HG22 1 
ATOM   5962 H  HG23 . ILE   B 1 131 ? 49.063 -31.111 3.925   1.00 25.05 ?  131 ILE   B HG23 1 
ATOM   5963 H  HD11 . ILE   B 1 131 ? 48.966 -27.378 5.469   1.00 25.98 ?  131 ILE   B HD11 1 
ATOM   5964 H  HD12 . ILE   B 1 131 ? 49.433 -28.433 6.561   1.00 25.98 ?  131 ILE   B HD12 1 
ATOM   5965 H  HD13 . ILE   B 1 131 ? 49.911 -28.586 5.054   1.00 25.98 ?  131 ILE   B HD13 1 
ATOM   5966 N  N    . PHE   B 1 132 ? 44.660 -30.248 5.699   1.00 15.63 ?  132 PHE   B N    1 
ATOM   5967 C  CA   . PHE   B 1 132 ? 43.500 -29.746 6.428   1.00 15.76 ?  132 PHE   B CA   1 
ATOM   5968 C  C    . PHE   B 1 132 ? 42.480 -30.838 6.760   1.00 17.28 ?  132 PHE   B C    1 
ATOM   5969 O  O    . PHE   B 1 132 ? 41.574 -30.588 7.562   1.00 18.85 ?  132 PHE   B O    1 
ATOM   5970 C  CB   . PHE   B 1 132 ? 42.824 -28.615 5.644   1.00 14.73 ?  132 PHE   B CB   1 
ATOM   5971 C  CG   . PHE   B 1 132 ? 43.522 -27.273 5.758   1.00 14.93 ?  132 PHE   B CG   1 
ATOM   5972 C  CD1  . PHE   B 1 132 ? 44.818 -27.090 5.295   1.00 15.94 ?  132 PHE   B CD1  1 
ATOM   5973 C  CD2  . PHE   B 1 132 ? 42.846 -26.179 6.283   1.00 14.37 ?  132 PHE   B CD2  1 
ATOM   5974 C  CE1  . PHE   B 1 132 ? 45.441 -25.848 5.392   1.00 16.72 ?  132 PHE   B CE1  1 
ATOM   5975 C  CE2  . PHE   B 1 132 ? 43.456 -24.932 6.369   1.00 15.39 ?  132 PHE   B CE2  1 
ATOM   5976 C  CZ   . PHE   B 1 132 ? 44.753 -24.769 5.926   1.00 16.28 ?  132 PHE   B CZ   1 
ATOM   5977 H  H    . PHE   B 1 132 ? 44.610 -30.137 4.845   1.00 18.72 ?  132 PHE   B H    1 
ATOM   5978 H  HA   . PHE   B 1 132 ? 43.806 -29.370 7.266   1.00 18.88 ?  132 PHE   B HA   1 
ATOM   5979 H  HB2  . PHE   B 1 132 ? 42.814 -28.853 4.706   1.00 17.64 ?  132 PHE   B HB2  1 
ATOM   5980 H  HB3  . PHE   B 1 132 ? 41.917 -28.505 5.969   1.00 17.64 ?  132 PHE   B HB3  1 
ATOM   5981 H  HD1  . PHE   B 1 132 ? 45.283 -27.812 4.942   1.00 19.09 ?  132 PHE   B HD1  1 
ATOM   5982 H  HD2  . PHE   B 1 132 ? 41.970 -26.282 6.585   1.00 17.21 ?  132 PHE   B HD2  1 
ATOM   5983 H  HE1  . PHE   B 1 132 ? 46.313 -25.739 5.093   1.00 20.04 ?  132 PHE   B HE1  1 
ATOM   5984 H  HE2  . PHE   B 1 132 ? 42.995 -24.210 6.738   1.00 18.44 ?  132 PHE   B HE2  1 
ATOM   5985 H  HZ   . PHE   B 1 132 ? 45.164 -23.935 5.995   1.00 19.51 ?  132 PHE   B HZ   1 
ATOM   5986 N  N    . GLY   B 1 133 ? 42.581 -32.030 6.158   1.00 16.98 ?  133 GLY   B N    1 
ATOM   5987 C  CA   . GLY   B 1 133 ? 41.867 -33.199 6.645   1.00 17.79 ?  133 GLY   B CA   1 
ATOM   5988 C  C    . GLY   B 1 133 ? 40.470 -33.459 6.110   1.00 18.12 ?  133 GLY   B C    1 
ATOM   5989 O  O    . GLY   B 1 133 ? 39.882 -34.481 6.477   1.00 19.94 ?  133 GLY   B O    1 
ATOM   5990 H  H    . GLY   B 1 133 ? 43.071 -32.177 5.466   1.00 20.35 ?  133 GLY   B H    1 
ATOM   5991 H  HA2  . GLY   B 1 133 ? 42.403 -33.979 6.446   1.00 21.32 ?  133 GLY   B HA2  1 
ATOM   5992 H  HA3  . GLY   B 1 133 ? 41.796 -33.125 7.608   1.00 21.32 ?  133 GLY   B HA3  1 
ATOM   5993 N  N    . ALA   B 1 134 ? 39.907 -32.588 5.278   1.00 17.15 ?  134 ALA   B N    1 
ATOM   5994 C  CA   . ALA   B 1 134 ? 38.582 -32.873 4.745   1.00 17.20 ?  134 ALA   B CA   1 
ATOM   5995 C  C    . ALA   B 1 134 ? 38.671 -33.870 3.594   1.00 17.19 ?  134 ALA   B C    1 
ATOM   5996 O  O    . ALA   B 1 134 ? 39.729 -34.065 2.987   1.00 18.18 ?  134 ALA   B O    1 
ATOM   5997 C  CB   . ALA   B 1 134 ? 37.902 -31.591 4.263   1.00 17.68 ?  134 ALA   B CB   1 
ATOM   5998 H  H    . ALA   B 1 134 ? 40.254 -31.839 5.018   1.00 20.55 ?  134 ALA   B H    1 
ATOM   5999 H  HA   . ALA   B 1 134 ? 38.032 -33.257 5.448   1.00 20.60 ?  134 ALA   B HA   1 
ATOM   6000 H  HB1  . ALA   B 1 134 ? 37.017 -31.812 3.926   1.00 21.18 ?  134 ALA   B HB1  1 
ATOM   6001 H  HB2  . ALA   B 1 134 ? 37.827 -30.971 5.005   1.00 21.18 ?  134 ALA   B HB2  1 
ATOM   6002 H  HB3  . ALA   B 1 134 ? 38.435 -31.198 3.554   1.00 21.18 ?  134 ALA   B HB3  1 
ATOM   6003 N  N    . ASP   B 1 135 ? 37.537 -34.499 3.302   1.00 17.33 ?  135 ASP   B N    1 
ATOM   6004 C  CA   . ASP   B 1 135 ? 37.439 -35.394 2.159   1.00 18.20 ?  135 ASP   B CA   1 
ATOM   6005 C  C    . ASP   B 1 135 ? 37.538 -34.558 0.889   1.00 17.09 ?  135 ASP   B C    1 
ATOM   6006 O  O    . ASP   B 1 135 ? 36.684 -33.687 0.665   1.00 16.83 ?  135 ASP   B O    1 
ATOM   6007 C  CB   . ASP   B 1 135 ? 36.101 -36.133 2.217   1.00 20.02 ?  135 ASP   B CB   1 
ATOM   6008 C  CG   . ASP   B 1 135 ? 35.915 -37.113 1.076   1.00 21.85 ?  135 ASP   B CG   1 
ATOM   6009 O  OD1  . ASP   B 1 135 ? 36.786 -37.173 0.182   1.00 21.51 ?  135 ASP   B OD1  1 
ATOM   6010 O  OD2  . ASP   B 1 135 ? 34.895 -37.841 1.090   1.00 24.98 -1 135 ASP   B OD2  1 
ATOM   6011 H  H    . ASP   B 1 135 ? 36.809 -34.424 3.754   1.00 20.77 ?  135 ASP   B H    1 
ATOM   6012 H  HA   . ASP   B 1 135 ? 38.161 -36.045 2.192   1.00 21.81 ?  135 ASP   B HA   1 
ATOM   6013 H  HB2  . ASP   B 1 135 ? 36.054 -36.630 3.046   1.00 23.99 ?  135 ASP   B HB2  1 
ATOM   6014 H  HB3  . ASP   B 1 135 ? 35.386 -35.486 2.170   1.00 23.99 ?  135 ASP   B HB3  1 
ATOM   6015 N  N    . PRO   B 1 136 ? 38.549 -34.766 0.045   1.00 17.21 ?  136 PRO   B N    1 
ATOM   6016 C  CA   . PRO   B 1 136 ? 38.651 -33.947 -1.172  1.00 16.44 ?  136 PRO   B CA   1 
ATOM   6017 C  C    . PRO   B 1 136 ? 37.461 -34.101 -2.099  1.00 15.87 ?  136 PRO   B C    1 
ATOM   6018 O  O    . PRO   B 1 136 ? 37.134 -33.154 -2.821  1.00 15.17 ?  136 PRO   B O    1 
ATOM   6019 C  CB   . PRO   B 1 136 ? 39.964 -34.420 -1.812  1.00 17.32 ?  136 PRO   B CB   1 
ATOM   6020 C  CG   . PRO   B 1 136 ? 40.166 -35.807 -1.271  1.00 18.55 ?  136 PRO   B CG   1 
ATOM   6021 C  CD   . PRO   B 1 136 ? 39.619 -35.772 0.128   1.00 18.39 ?  136 PRO   B CD   1 
ATOM   6022 H  HA   . PRO   B 1 136 ? 38.736 -33.010 -0.936  1.00 19.70 ?  136 PRO   B HA   1 
ATOM   6023 H  HB2  . PRO   B 1 136 ? 39.872 -34.436 -2.779  1.00 20.75 ?  136 PRO   B HB2  1 
ATOM   6024 H  HB3  . PRO   B 1 136 ? 40.687 -33.834 -1.545  1.00 20.75 ?  136 PRO   B HB3  1 
ATOM   6025 H  HG2  . PRO   B 1 136 ? 39.676 -36.449 -1.810  1.00 22.24 ?  136 PRO   B HG2  1 
ATOM   6026 H  HG3  . PRO   B 1 136 ? 41.113 -36.023 -1.259  1.00 22.24 ?  136 PRO   B HG3  1 
ATOM   6027 H  HD2  . PRO   B 1 136 ? 39.253 -36.637 0.373   1.00 22.04 ?  136 PRO   B HD2  1 
ATOM   6028 H  HD3  . PRO   B 1 136 ? 40.301 -35.485 0.757   1.00 22.04 ?  136 PRO   B HD3  1 
ATOM   6029 N  N    . ILE   B 1 137 ? 36.800 -35.265 -2.097  1.00 16.30 ?  137 ILE   B N    1 
ATOM   6030 C  CA   . ILE   B 1 137 ? 35.582 -35.433 -2.888  1.00 16.48 ?  137 ILE   B CA   1 
ATOM   6031 C  C    . ILE   B 1 137 ? 34.510 -34.459 -2.415  1.00 16.15 ?  137 ILE   B C    1 
ATOM   6032 O  O    . ILE   B 1 137 ? 33.800 -33.840 -3.221  1.00 15.77 ?  137 ILE   B O    1 
ATOM   6033 C  CB   . ILE   B 1 137 ? 35.108 -36.900 -2.823  1.00 18.45 ?  137 ILE   B CB   1 
ATOM   6034 C  CG1  . ILE   B 1 137 ? 36.109 -37.808 -3.543  1.00 20.92 ?  137 ILE   B CG1  1 
ATOM   6035 C  CG2  . ILE   B 1 137 ? 33.716 -37.045 -3.426  1.00 19.00 ?  137 ILE   B CG2  1 
ATOM   6036 C  CD1  . ILE   B 1 137 ? 35.792 -39.290 -3.443  1.00 23.25 ?  137 ILE   B CD1  1 
ATOM   6037 H  H    . ILE   B 1 137 ? 37.031 -35.966 -1.653  1.00 19.53 ?  137 ILE   B H    1 
ATOM   6038 H  HA   . ILE   B 1 137 ? 35.777 -35.232 -3.817  1.00 19.75 ?  137 ILE   B HA   1 
ATOM   6039 H  HB   . ILE   B 1 137 ? 35.062 -37.169 -1.895  1.00 22.11 ?  137 ILE   B HB   1 
ATOM   6040 H  HG12 . ILE   B 1 137 ? 36.124 -37.576 -4.484  1.00 25.07 ?  137 ILE   B HG12 1 
ATOM   6041 H  HG13 . ILE   B 1 137 ? 36.986 -37.671 -3.156  1.00 25.07 ?  137 ILE   B HG13 1 
ATOM   6042 H  HG21 . ILE   B 1 137 ? 33.477 -37.984 -3.473  1.00 22.77 ?  137 ILE   B HG21 1 
ATOM   6043 H  HG22 . ILE   B 1 137 ? 33.074 -36.582 -2.867  1.00 22.77 ?  137 ILE   B HG22 1 
ATOM   6044 H  HG23 . ILE   B 1 137 ? 33.716 -36.663 -4.318  1.00 22.77 ?  137 ILE   B HG23 1 
ATOM   6045 H  HD11 . ILE   B 1 137 ? 36.501 -39.781 -3.882  1.00 27.87 ?  137 ILE   B HD11 1 
ATOM   6046 H  HD12 . ILE   B 1 137 ? 35.740 -39.542 -2.508  1.00 27.87 ?  137 ILE   B HD12 1 
ATOM   6047 H  HD13 . ILE   B 1 137 ? 34.949 -39.472 -3.885  1.00 27.87 ?  137 ILE   B HD13 1 
ATOM   6048 N  N    . HIS   B 1 138 ? 34.378 -34.304 -1.103  1.00 16.25 ?  138 HIS   B N    1 
ATOM   6049 C  CA   . HIS   B 1 138 ? 33.426 -33.338 -0.574  1.00 16.66 ?  138 HIS   B CA   1 
ATOM   6050 C  C    . HIS   B 1 138 ? 33.847 -31.910 -0.891  1.00 15.79 ?  138 HIS   B C    1 
ATOM   6051 O  O    . HIS   B 1 138 ? 33.002 -31.064 -1.198  1.00 15.98 ?  138 HIS   B O    1 
ATOM   6052 C  CB   . HIS   B 1 138 ? 33.298 -33.515 0.930   1.00 18.10 ?  138 HIS   B CB   1 
ATOM   6053 C  CG   . HIS   B 1 138 ? 32.365 -32.532 1.560   1.00 18.92 ?  138 HIS   B CG   1 
ATOM   6054 N  ND1  . HIS   B 1 138 ? 31.029 -32.463 1.227   1.00 20.22 ?  138 HIS   B ND1  1 
ATOM   6055 C  CD2  . HIS   B 1 138 ? 32.576 -31.561 2.479   1.00 19.38 ?  138 HIS   B CD2  1 
ATOM   6056 C  CE1  . HIS   B 1 138 ? 30.453 -31.503 1.926   1.00 20.06 ?  138 HIS   B CE1  1 
ATOM   6057 N  NE2  . HIS   B 1 138 ? 31.369 -30.942 2.697   1.00 19.36 ?  138 HIS   B NE2  1 
ATOM   6058 H  H    . HIS   B 1 138 ? 34.822 -34.739 -0.512  1.00 19.47 ?  138 HIS   B H    1 
ATOM   6059 H  HA   . HIS   B 1 138 ? 32.553 -33.502 -0.976  1.00 19.96 ?  138 HIS   B HA   1 
ATOM   6060 H  HB2  . HIS   B 1 138 ? 32.961 -34.405 1.116   1.00 21.69 ?  138 HIS   B HB2  1 
ATOM   6061 H  HB3  . HIS   B 1 138 ? 34.169 -33.397 1.334   1.00 21.69 ?  138 HIS   B HB3  1 
ATOM   6062 H  HD1  . HIS   B 1 138 ? 30.629 -32.974 0.657   1.00 24.24 ?  138 HIS   B HD1  1 
ATOM   6063 H  HD2  . HIS   B 1 138 ? 33.373 -31.359 2.899   1.00 23.22 ?  138 HIS   B HD2  1 
ATOM   6064 H  HE1  . HIS   B 1 138 ? 29.547 -31.271 1.884   1.00 24.04 ?  138 HIS   B HE1  1 
ATOM   6065 N  N    . SER   B 1 139 ? 35.142 -31.612 -0.812  1.00 15.56 ?  139 SER   B N    1 
ATOM   6066 C  CA   . SER   B 1 139 ? 35.583 -30.263 -1.131  1.00 14.47 ?  139 SER   B CA   1 
ATOM   6067 C  C    . SER   B 1 139 ? 35.244 -29.913 -2.570  1.00 14.00 ?  139 SER   B C    1 
ATOM   6068 O  O    . SER   B 1 139 ? 34.790 -28.799 -2.849  1.00 13.97 ?  139 SER   B O    1 
ATOM   6069 C  CB   . SER   B 1 139 ? 37.078 -30.127 -0.865  1.00 15.04 ?  139 SER   B CB   1 
ATOM   6070 O  OG   . SER   B 1 139 ? 37.487 -28.791 -1.115  1.00 14.95 ?  139 SER   B OG   1 
ATOM   6071 H  H    . SER   B 1 139 ? 35.757 -32.159 -0.588  1.00 18.64 ?  139 SER   B H    1 
ATOM   6072 H  HA   . SER   B 1 139 ? 35.114 -29.638 -0.562  1.00 17.33 ?  139 SER   B HA   1 
ATOM   6073 H  HB2  . SER   B 1 139 ? 37.253 -30.346 0.065   1.00 18.02 ?  139 SER   B HB2  1 
ATOM   6074 H  HB3  . SER   B 1 139 ? 37.564 -30.732 -1.447  1.00 18.02 ?  139 SER   B HB3  1 
ATOM   6075 H  HG   . SER   B 1 139 ? 38.316 -28.715 -0.970  1.00 17.91 ?  139 SER   B HG   1 
ATOM   6076 N  N    . LEU   B 1 140 ? 35.438 -30.856 -3.497  1.00 13.62 ?  140 LEU   B N    1 
ATOM   6077 C  CA   . LEU   B 1 140 ? 35.071 -30.612 -4.885  1.00 13.85 ?  140 LEU   B CA   1 
ATOM   6078 C  C    . LEU   B 1 140 ? 33.570 -30.383 -5.017  1.00 13.74 ?  140 LEU   B C    1 
ATOM   6079 O  O    . LEU   B 1 140 ? 33.134 -29.498 -5.758  1.00 13.77 ?  140 LEU   B O    1 
ATOM   6080 C  CB   . LEU   B 1 140 ? 35.542 -31.774 -5.762  1.00 13.85 ?  140 LEU   B CB   1 
ATOM   6081 C  CG   . LEU   B 1 140 ? 35.174 -31.676 -7.235  1.00 13.99 ?  140 LEU   B CG   1 
ATOM   6082 C  CD1  . LEU   B 1 140 ? 35.714 -30.387 -7.841  1.00 14.85 ?  140 LEU   B CD1  1 
ATOM   6083 C  CD2  . LEU   B 1 140 ? 35.661 -32.898 -7.987  1.00 15.27 ?  140 LEU   B CD2  1 
ATOM   6084 H  H    . LEU   B 1 140 ? 35.769 -31.633 -3.351  1.00 16.31 ?  140 LEU   B H    1 
ATOM   6085 H  HA   . LEU   B 1 140 ? 35.522 -29.807 -5.192  1.00 16.59 ?  140 LEU   B HA   1 
ATOM   6086 H  HB2  . LEU   B 1 140 ? 36.509 -31.829 -5.709  1.00 16.59 ?  140 LEU   B HB2  1 
ATOM   6087 H  HB3  . LEU   B 1 140 ? 35.151 -32.593 -5.422  1.00 16.59 ?  140 LEU   B HB3  1 
ATOM   6088 H  HG   . LEU   B 1 140 ? 34.208 -31.649 -7.312  1.00 16.76 ?  140 LEU   B HG   1 
ATOM   6089 H  HD11 . LEU   B 1 140 ? 35.588 -30.419 -8.802  1.00 17.79 ?  140 LEU   B HD11 1 
ATOM   6090 H  HD12 . LEU   B 1 140 ? 35.223 -29.634 -7.470  1.00 17.79 ?  140 LEU   B HD12 1 
ATOM   6091 H  HD13 . LEU   B 1 140 ? 36.654 -30.309 -7.630  1.00 17.79 ?  140 LEU   B HD13 1 
ATOM   6092 H  HD21 . LEU   B 1 140 ? 35.410 -32.806 -8.920  1.00 18.29 ?  140 LEU   B HD21 1 
ATOM   6093 H  HD22 . LEU   B 1 140 ? 36.621 -32.954 -7.902  1.00 18.29 ?  140 LEU   B HD22 1 
ATOM   6094 H  HD23 . LEU   B 1 140 ? 35.241 -33.682 -7.606  1.00 18.29 ?  140 LEU   B HD23 1 
ATOM   6095 N  N    . ARG   B 1 141 ? 32.767 -31.174 -4.299  1.00 13.85 ?  141 ARG   B N    1 
ATOM   6096 C  CA   . ARG   B 1 141 ? 31.317 -30.996 -4.281  1.00 14.84 ?  141 ARG   B CA   1 
ATOM   6097 C  C    . ARG   B 1 141 ? 30.940 -29.586 -3.849  1.00 14.27 ?  141 ARG   B C    1 
ATOM   6098 O  O    . ARG   B 1 141 ? 30.138 -28.906 -4.508  1.00 14.65 ?  141 ARG   B O    1 
ATOM   6099 C  CB   . ARG   B 1 141 ? 30.732 -32.030 -3.309  1.00 16.47 ?  141 ARG   B CB   1 
ATOM   6100 C  CG   . ARG   B 1 141 ? 29.264 -31.913 -2.966  1.00 18.59 ?  141 ARG   B CG   1 
ATOM   6101 C  CD   . ARG   B 1 141 ? 28.448 -32.545 -4.024  1.00 20.30 ?  141 ARG   B CD   1 
ATOM   6102 N  NE   . ARG   B 1 141 ? 28.207 -31.639 -5.136  1.00 20.84 ?  141 ARG   B NE   1 
ATOM   6103 C  CZ   . ARG   B 1 141 ? 28.210 -31.995 -6.413  1.00 20.30 ?  141 ARG   B CZ   1 
ATOM   6104 N  NH1  . ARG   B 1 141 ? 28.631 -33.191 -6.798  1.00 20.10 ?  141 ARG   B NH1  1 
ATOM   6105 N  NH2  . ARG   B 1 141 ? 27.779 -31.131 -7.326  1.00 21.04 ?  141 ARG   B NH2  1 
ATOM   6106 H  H    . ARG   B 1 141 ? 33.047 -31.823 -3.811  1.00 16.59 ?  141 ARG   B H    1 
ATOM   6107 H  HA   . ARG   B 1 141 ? 30.955 -31.159 -5.162  1.00 17.78 ?  141 ARG   B HA   1 
ATOM   6108 H  HB2  . ARG   B 1 141 ? 30.875 -32.914 -3.689  1.00 19.74 ?  141 ARG   B HB2  1 
ATOM   6109 H  HB3  . ARG   B 1 141 ? 31.223 -31.971 -2.475  1.00 19.74 ?  141 ARG   B HB3  1 
ATOM   6110 H  HG2  . ARG   B 1 141 ? 29.099 -32.366 -2.126  1.00 22.27 ?  141 ARG   B HG2  1 
ATOM   6111 H  HG3  . ARG   B 1 141 ? 29.014 -30.975 -2.894  1.00 22.27 ?  141 ARG   B HG3  1 
ATOM   6112 H  HD2  . ARG   B 1 141 ? 28.908 -33.337 -4.350  1.00 24.33 ?  141 ARG   B HD2  1 
ATOM   6113 H  HD3  . ARG   B 1 141 ? 27.595 -32.799 -3.648  1.00 24.33 ?  141 ARG   B HD3  1 
ATOM   6114 H  HE   . ARG   B 1 141 ? 28.035 -30.817 -4.949  1.00 24.97 ?  141 ARG   B HE   1 
ATOM   6115 H  HH11 . ARG   B 1 141 ? 28.901 -33.769 -6.220  1.00 24.09 ?  141 ARG   B HH11 1 
ATOM   6116 H  HH12 . ARG   B 1 141 ? 28.630 -33.397 -7.632  1.00 24.09 ?  141 ARG   B HH12 1 
ATOM   6117 H  HH21 . ARG   B 1 141 ? 27.513 -30.346 -7.087  1.00 25.22 ?  141 ARG   B HH21 1 
ATOM   6118 H  HH22 . ARG   B 1 141 ? 27.795 -31.339 -8.161  1.00 25.22 ?  141 ARG   B HH22 1 
ATOM   6119 N  N    . VAL   B 1 142 ? 31.486 -29.142 -2.720  1.00 14.16 ?  142 VAL   B N    1 
ATOM   6120 C  CA   . VAL   B 1 142 ? 31.146 -27.808 -2.236  1.00 13.71 ?  142 VAL   B CA   1 
ATOM   6121 C  C    . VAL   B 1 142 ? 31.620 -26.748 -3.223  1.00 13.65 ?  142 VAL   B C    1 
ATOM   6122 O  O    . VAL   B 1 142 ? 30.919 -25.759 -3.478  1.00 14.23 ?  142 VAL   B O    1 
ATOM   6123 C  CB   . VAL   B 1 142 ? 31.689 -27.584 -0.813  1.00 14.65 ?  142 VAL   B CB   1 
ATOM   6124 C  CG1  . VAL   B 1 142 ? 31.381 -26.157 -0.351  1.00 14.59 ?  142 VAL   B CG1  1 
ATOM   6125 C  CG2  . VAL   B 1 142 ? 31.095 -28.599 0.147   1.00 15.51 ?  142 VAL   B CG2  1 
ATOM   6126 H  H    . VAL   B 1 142 ? 32.047 -29.580 -2.228  1.00 16.96 ?  142 VAL   B H    1 
ATOM   6127 H  HA   . VAL   B 1 142 ? 30.188 -27.744 -2.184  1.00 16.43 ?  142 VAL   B HA   1 
ATOM   6128 H  HB   . VAL   B 1 142 ? 32.654 -27.699 -0.812  1.00 17.55 ?  142 VAL   B HB   1 
ATOM   6129 H  HG11 . VAL   B 1 142 ? 31.552 -26.088 0.600   1.00 17.48 ?  142 VAL   B HG11 1 
ATOM   6130 H  HG12 . VAL   B 1 142 ? 31.954 -25.536 -0.833  1.00 17.48 ?  142 VAL   B HG12 1 
ATOM   6131 H  HG13 . VAL   B 1 142 ? 30.451 -25.959 -0.537  1.00 17.48 ?  142 VAL   B HG13 1 
ATOM   6132 H  HG21 . VAL   B 1 142 ? 31.411 -28.408 1.043   1.00 18.59 ?  142 VAL   B HG21 1 
ATOM   6133 H  HG22 . VAL   B 1 142 ? 30.128 -28.529 0.115   1.00 18.59 ?  142 VAL   B HG22 1 
ATOM   6134 H  HG23 . VAL   B 1 142 ? 31.373 -29.487 -0.122  1.00 18.59 ?  142 VAL   B HG23 1 
ATOM   6135 N  N    . CYS   B 1 143 ? 32.804 -26.948 -3.809  1.00 13.27 ?  143 CYS   B N    1 
ATOM   6136 C  CA   . CYS   B 1 143 ? 33.300 -26.009 -4.811  1.00 13.38 ?  143 CYS   B CA   1 
ATOM   6137 C  C    . CYS   B 1 143 ? 32.298 -25.860 -5.950  1.00 13.16 ?  143 CYS   B C    1 
ATOM   6138 O  O    . CYS   B 1 143 ? 31.894 -24.744 -6.307  1.00 13.68 ?  143 CYS   B O    1 
ATOM   6139 C  CB   . CYS   B 1 143 ? 34.658 -26.490 -5.333  1.00 13.70 ?  143 CYS   B CB   1 
ATOM   6140 S  SG   . CYS   B 1 143 ? 35.405 -25.393 -6.562  1.00 13.77 ?  143 CYS   B SG   1 
ATOM   6141 H  H    . CYS   B 1 143 ? 33.338 -27.602 -3.640  1.00 15.90 ?  143 CYS   B H    1 
ATOM   6142 H  HA   . CYS   B 1 143 ? 33.430 -25.138 -4.403  1.00 16.02 ?  143 CYS   B HA   1 
ATOM   6143 H  HB2  . CYS   B 1 143 ? 35.278 -26.561 -4.588  1.00 16.42 ?  143 CYS   B HB2  1 
ATOM   6144 H  HB3  . CYS   B 1 143 ? 34.545 -27.356 -5.742  1.00 16.42 ?  143 CYS   B HB3  1 
ATOM   6145 H  HG   . CYS   B 1 143 ? 36.482 -25.826 -6.877  1.00 16.50 ?  143 CYS   B HG   1 
ATOM   6146 N  N    . VAL   B 1 144 ? 31.891 -26.981 -6.541  1.00 13.66 ?  144 VAL   B N    1 
ATOM   6147 C  CA   . VAL   B 1 144 ? 30.987 -26.921 -7.682  1.00 14.44 ?  144 VAL   B CA   1 
ATOM   6148 C  C    . VAL   B 1 144 ? 29.648 -26.304 -7.304  1.00 14.66 ?  144 VAL   B C    1 
ATOM   6149 O  O    . VAL   B 1 144 ? 29.033 -25.597 -8.111  1.00 16.01 ?  144 VAL   B O    1 
ATOM   6150 C  CB   . VAL   B 1 144 ? 30.823 -28.337 -8.254  1.00 17.40 ?  144 VAL   B CB   1 
ATOM   6151 C  CG1  . VAL   B 1 144 ? 29.541 -28.467 -9.077  1.00 19.70 ?  144 VAL   B CG1  1 
ATOM   6152 C  CG2  . VAL   B 1 144 ? 32.061 -28.735 -9.051  1.00 17.40 ?  144 VAL   B CG2  1 
ATOM   6153 H  H    . VAL   B 1 144 ? 32.125 -27.773 -6.306  1.00 16.36 ?  144 VAL   B H    1 
ATOM   6154 H  HA   . VAL   B 1 144 ? 31.381 -26.372 -8.374  1.00 17.30 ?  144 VAL   B HA   1 
ATOM   6155 H  HB   . VAL   B 1 144 ? 30.751 -28.962 -7.515  1.00 20.85 ?  144 VAL   B HB   1 
ATOM   6156 H  HG11 . VAL   B 1 144 ? 29.608 -29.260 -9.636  1.00 23.61 ?  144 VAL   B HG11 1 
ATOM   6157 H  HG12 . VAL   B 1 144 ? 28.787 -28.558 -8.474  1.00 23.61 ?  144 VAL   B HG12 1 
ATOM   6158 H  HG13 . VAL   B 1 144 ? 29.439 -27.683 -9.632  1.00 23.61 ?  144 VAL   B HG13 1 
ATOM   6159 H  HG21 . VAL   B 1 144 ? 31.941 -29.633 -9.399  1.00 20.84 ?  144 VAL   B HG21 1 
ATOM   6160 H  HG22 . VAL   B 1 144 ? 32.176 -28.110 -9.786  1.00 20.84 ?  144 VAL   B HG22 1 
ATOM   6161 H  HG23 . VAL   B 1 144 ? 32.834 -28.706 -8.468  1.00 20.84 ?  144 VAL   B HG23 1 
ATOM   6162 N  N    . ASP   B 1 145 ? 29.177 -26.555 -6.088  1.00 14.53 ?  145 ASP   B N    1 
ATOM   6163 C  CA   . ASP   B 1 145 ? 27.866 -26.087 -5.656  1.00 15.58 ?  145 ASP   B CA   1 
ATOM   6164 C  C    . ASP   B 1 145 ? 27.893 -24.661 -5.116  1.00 14.93 ?  145 ASP   B C    1 
ATOM   6165 O  O    . ASP   B 1 145 ? 26.833 -24.117 -4.785  1.00 16.84 ?  145 ASP   B O    1 
ATOM   6166 C  CB   . ASP   B 1 145 ? 27.296 -27.010 -4.571  1.00 16.83 ?  145 ASP   B CB   1 
ATOM   6167 C  CG   . ASP   B 1 145 ? 26.918 -28.383 -5.084  1.00 18.66 ?  145 ASP   B CG   1 
ATOM   6168 O  OD1  . ASP   B 1 145 ? 26.811 -28.585 -6.311  1.00 19.06 ?  145 ASP   B OD1  1 
ATOM   6169 O  OD2  . ASP   B 1 145 ? 26.724 -29.269 -4.233  1.00 20.94 -1 145 ASP   B OD2  1 
ATOM   6170 H  H    . ASP   B 1 145 ? 29.608 -26.989 -5.489  1.00 17.40 ?  145 ASP   B H    1 
ATOM   6171 H  HA   . ASP   B 1 145 ? 27.266 -26.090 -6.415  1.00 18.66 ?  145 ASP   B HA   1 
ATOM   6172 H  HB2  . ASP   B 1 145 ? 27.960 -27.132 -3.884  1.00 20.17 ?  145 ASP   B HB2  1 
ATOM   6173 H  HB3  . ASP   B 1 145 ? 26.499 -26.598 -4.204  1.00 20.17 ?  145 ASP   B HB3  1 
ATOM   6174 N  N    . THR   B 1 146 ? 29.068 -24.048 -5.008  1.00 13.41 ?  146 THR   B N    1 
ATOM   6175 C  CA   . THR   B 1 146 ? 29.203 -22.724 -4.402  1.00 13.17 ?  146 THR   B CA   1 
ATOM   6176 C  C    . THR   B 1 146 ? 29.840 -21.696 -5.319  1.00 12.93 ?  146 THR   B C    1 
ATOM   6177 O  O    . THR   B 1 146 ? 29.387 -20.537 -5.362  1.00 13.26 ?  146 THR   B O    1 
ATOM   6178 C  CB   . THR   B 1 146 ? 30.037 -22.825 -3.115  1.00 13.51 ?  146 THR   B CB   1 
ATOM   6179 O  OG1  . THR   B 1 146 ? 29.468 -23.810 -2.247  1.00 13.70 ?  146 THR   B OG1  1 
ATOM   6180 C  CG2  . THR   B 1 146 ? 30.109 -21.474 -2.406  1.00 13.82 ?  146 THR   B CG2  1 
ATOM   6181 H  H    . THR   B 1 146 ? 29.820 -24.375 -5.285  1.00 16.06 ?  146 THR   B H    1 
ATOM   6182 H  HA   . THR   B 1 146 ? 28.329 -22.392 -4.164  1.00 15.77 ?  146 THR   B HA   1 
ATOM   6183 H  HB   . THR   B 1 146 ? 30.946 -23.082 -3.344  1.00 16.18 ?  146 THR   B HB   1 
ATOM   6184 H  HG1  . THR   B 1 146 ? 29.496 -24.566 -2.626  1.00 16.41 ?  146 THR   B HG1  1 
ATOM   6185 H  HG21 . THR   B 1 146 ? 30.448 -21.588 -1.507  1.00 16.55 ?  146 THR   B HG21 1 
ATOM   6186 H  HG22 . THR   B 1 146 ? 30.706 -20.873 -2.889  1.00 16.55 ?  146 THR   B HG22 1 
ATOM   6187 H  HG23 . THR   B 1 146 ? 29.228 -21.073 -2.365  1.00 16.55 ?  146 THR   B HG23 1 
ATOM   6188 N  N    . VAL   B 1 147 ? 30.900 -22.073 -6.020  1.00 12.85 ?  147 VAL   B N    1 
ATOM   6189 C  CA   . VAL   B 1 147 ? 31.624 -21.128 -6.856  1.00 12.57 ?  147 VAL   B CA   1 
ATOM   6190 C  C    . VAL   B 1 147 ? 30.894 -20.993 -8.180  1.00 12.77 ?  147 VAL   B C    1 
ATOM   6191 O  O    . VAL   B 1 147 ? 30.520 -21.995 -8.808  1.00 13.59 ?  147 VAL   B O    1 
ATOM   6192 C  CB   . VAL   B 1 147 ? 33.078 -21.580 -7.057  1.00 12.71 ?  147 VAL   B CB   1 
ATOM   6193 C  CG1  . VAL   B 1 147 ? 33.836 -20.549 -7.868  1.00 12.55 ?  147 VAL   B CG1  1 
ATOM   6194 C  CG2  . VAL   B 1 147 ? 33.758 -21.785 -5.717  1.00 13.11 ?  147 VAL   B CG2  1 
ATOM   6195 H  H    . VAL   B 1 147 ? 31.228 -22.875 -6.036  1.00 15.39 ?  147 VAL   B H    1 
ATOM   6196 H  HA   . VAL   B 1 147 ? 31.643 -20.263 -6.424  1.00 15.05 ?  147 VAL   B HA   1 
ATOM   6197 H  HB   . VAL   B 1 147 ? 33.097 -22.424 -7.543  1.00 15.22 ?  147 VAL   B HB   1 
ATOM   6198 H  HG11 . VAL   B 1 147 ? 34.782 -20.764 -7.852  1.00 15.03 ?  147 VAL   B HG11 1 
ATOM   6199 H  HG12 . VAL   B 1 147 ? 33.511 -20.556 -8.780  1.00 15.03 ?  147 VAL   B HG12 1 
ATOM   6200 H  HG13 . VAL   B 1 147 ? 33.693 -19.673 -7.471  1.00 15.03 ?  147 VAL   B HG13 1 
ATOM   6201 H  HG21 . VAL   B 1 147 ? 34.699 -21.978 -5.864  1.00 15.70 ?  147 VAL   B HG21 1 
ATOM   6202 H  HG22 . VAL   B 1 147 ? 33.664 -20.976 -5.192  1.00 15.70 ?  147 VAL   B HG22 1 
ATOM   6203 H  HG23 . VAL   B 1 147 ? 33.338 -22.529 -5.259  1.00 15.70 ?  147 VAL   B HG23 1 
ATOM   6204 N  N    . ARG   B 1 148 ? 30.676 -19.743 -8.593  1.00 12.70 ?  148 ARG   B N    1 
ATOM   6205 C  CA   . ARG   B 1 148 ? 30.055 -19.425 -9.866  1.00 13.01 ?  148 ARG   B CA   1 
ATOM   6206 C  C    . ARG   B 1 148 ? 31.010 -18.752 -10.840 1.00 12.86 ?  148 ARG   B C    1 
ATOM   6207 O  O    . ARG   B 1 148 ? 30.721 -18.722 -12.038 1.00 14.21 ?  148 ARG   B O    1 
ATOM   6208 C  CB   . ARG   B 1 148 ? 28.813 -18.543 -9.650  1.00 13.27 ?  148 ARG   B CB   1 
ATOM   6209 C  CG   . ARG   B 1 148 ? 27.738 -19.249 -8.826  1.00 14.23 ?  148 ARG   B CG   1 
ATOM   6210 C  CD   . ARG   B 1 148 ? 26.531 -18.363 -8.518  1.00 15.04 ?  148 ARG   B CD   1 
ATOM   6211 N  NE   . ARG   B 1 148 ? 26.921 -17.162 -7.792  1.00 14.78 ?  148 ARG   B NE   1 
ATOM   6212 C  CZ   . ARG   B 1 148 ? 27.228 -17.128 -6.503  1.00 13.99 ?  148 ARG   B CZ   1 
ATOM   6213 N  NH1  . ARG   B 1 148 ? 27.154 -18.211 -5.745  1.00 14.23 ?  148 ARG   B NH1  1 
ATOM   6214 N  NH2  . ARG   B 1 148 ? 27.625 -15.978 -5.960  1.00 13.95 ?  148 ARG   B NH2  1 
ATOM   6215 H  H    . ARG   B 1 148 ? 30.895 -19.040 -8.131  1.00 15.21 ?  148 ARG   B H    1 
ATOM   6216 H  HA   . ARG   B 1 148 ? 29.760 -20.250 -10.271 1.00 15.58 ?  148 ARG   B HA   1 
ATOM   6217 H  HB2  . ARG   B 1 148 ? 29.071 -17.738 -9.177  1.00 15.89 ?  148 ARG   B HB2  1 
ATOM   6218 H  HB3  . ARG   B 1 148 ? 28.432 -18.319 -10.511 1.00 15.89 ?  148 ARG   B HB3  1 
ATOM   6219 H  HG2  . ARG   B 1 148 ? 27.420 -20.022 -9.320  1.00 17.05 ?  148 ARG   B HG2  1 
ATOM   6220 H  HG3  . ARG   B 1 148 ? 28.121 -19.533 -7.982  1.00 17.05 ?  148 ARG   B HG3  1 
ATOM   6221 H  HD2  . ARG   B 1 148 ? 26.112 -18.093 -9.349  1.00 18.01 ?  148 ARG   B HD2  1 
ATOM   6222 H  HD3  . ARG   B 1 148 ? 25.899 -18.861 -7.972  1.00 18.01 ?  148 ARG   B HD3  1 
ATOM   6223 H  HE   . ARG   B 1 148 ? 26.957 -16.425 -8.227  1.00 17.71 ?  148 ARG   B HE   1 
ATOM   6224 H  HH11 . ARG   B 1 148 ? 26.895 -18.962 -6.080  1.00 17.05 ?  148 ARG   B HH11 1 
ATOM   6225 H  HH12 . ARG   B 1 148 ? 27.353 -18.168 -4.907  1.00 17.05 ?  148 ARG   B HH12 1 
ATOM   6226 H  HH21 . ARG   B 1 148 ? 27.680 -15.272 -6.445  1.00 16.71 ?  148 ARG   B HH21 1 
ATOM   6227 H  HH22 . ARG   B 1 148 ? 27.828 -15.943 -5.124  1.00 16.71 ?  148 ARG   B HH22 1 
ATOM   6228 N  N    . THR   B 1 149 ? 32.118 -18.199 -10.356 1.00 12.80 ?  149 THR   B N    1 
ATOM   6229 C  CA   . THR   B 1 149 ? 33.157 -17.642 -11.206 1.00 12.92 ?  149 THR   B CA   1 
ATOM   6230 C  C    . THR   B 1 149 ? 34.045 -18.781 -11.710 1.00 12.78 ?  149 THR   B C    1 
ATOM   6231 O  O    . THR   B 1 149 ? 33.851 -19.951 -11.367 1.00 13.32 ?  149 THR   B O    1 
ATOM   6232 C  CB   . THR   B 1 149 ? 33.933 -16.586 -10.425 1.00 12.74 ?  149 THR   B CB   1 
ATOM   6233 O  OG1  . THR   B 1 149 ? 34.390 -17.179 -9.210  1.00 12.91 ?  149 THR   B OG1  1 
ATOM   6234 C  CG2  . THR   B 1 149 ? 33.039 -15.387 -10.127 1.00 13.73 ?  149 THR   B CG2  1 
ATOM   6235 H  H    . THR   B 1 149 ? 32.286 -18.126 -9.519  1.00 15.33 ?  149 THR   B H    1 
ATOM   6236 H  HA   . THR   B 1 149 ? 32.750 -17.208 -11.974 1.00 15.47 ?  149 THR   B HA   1 
ATOM   6237 H  HB   . THR   B 1 149 ? 34.693 -16.290 -10.942 1.00 15.25 ?  149 THR   B HB   1 
ATOM   6238 H  HG1  . THR   B 1 149 ? 34.808 -16.608 -8.750  1.00 15.47 ?  149 THR   B HG1  1 
ATOM   6239 H  HG21 . THR   B 1 149 ? 33.540 -14.710 -9.648  1.00 16.45 ?  149 THR   B HG21 1 
ATOM   6240 H  HG22 . THR   B 1 149 ? 32.710 -15.005 -10.958 1.00 16.45 ?  149 THR   B HG22 1 
ATOM   6241 H  HG23 . THR   B 1 149 ? 32.280 -15.660 -9.587  1.00 16.45 ?  149 THR   B HG23 1 
ATOM   6242 N  N    . ASN   B 1 150 ? 35.016 -18.456 -12.553 1.00 12.73 ?  150 ASN   B N    1 
ATOM   6243 C  CA   . ASN   B 1 150 ? 35.780 -19.481 -13.253 1.00 13.42 ?  150 ASN   B CA   1 
ATOM   6244 C  C    . ASN   B 1 150 ? 36.948 -19.931 -12.384 1.00 12.68 ?  150 ASN   B C    1 
ATOM   6245 O  O    . ASN   B 1 150 ? 37.881 -19.160 -12.135 1.00 13.26 ?  150 ASN   B O    1 
ATOM   6246 C  CB   . ASN   B 1 150 ? 36.254 -18.949 -14.596 1.00 15.16 ?  150 ASN   B CB   1 
ATOM   6247 C  CG   . ASN   B 1 150 ? 35.108 -18.726 -15.541 1.00 17.75 ?  150 ASN   B CG   1 
ATOM   6248 O  OD1  . ASN   B 1 150 ? 34.220 -19.561 -15.643 1.00 18.85 ?  150 ASN   B OD1  1 
ATOM   6249 N  ND2  . ASN   B 1 150 ? 35.091 -17.583 -16.203 1.00 19.50 ?  150 ASN   B ND2  1 
ATOM   6250 H  H    . ASN   B 1 150 ? 35.261 -17.647 -12.732 1.00 15.25 ?  150 ASN   B H    1 
ATOM   6251 H  HA   . ASN   B 1 150 ? 35.201 -20.247 -13.416 1.00 16.08 ?  150 ASN   B HA   1 
ATOM   6252 H  HB2  . ASN   B 1 150 ? 36.702 -18.099 -14.460 1.00 18.17 ?  150 ASN   B HB2  1 
ATOM   6253 H  HB3  . ASN   B 1 150 ? 36.857 -19.589 -14.998 1.00 18.17 ?  150 ASN   B HB3  1 
ATOM   6254 H  HD21 . ASN   B 1 150 ? 34.452 -17.413 -16.755 1.00 23.37 ?  150 ASN   B HD21 1 
ATOM   6255 H  HD22 . ASN   B 1 150 ? 35.727 -17.015 -16.095 1.00 23.37 ?  150 ASN   B HD22 1 
ATOM   6256 N  N    . VAL   B 1 151 ? 36.904 -21.179 -11.929 1.00 12.66 ?  151 VAL   B N    1 
ATOM   6257 C  CA   . VAL   B 1 151 ? 37.922 -21.713 -11.039 1.00 12.55 ?  151 VAL   B CA   1 
ATOM   6258 C  C    . VAL   B 1 151 ? 38.631 -22.877 -11.717 1.00 12.25 ?  151 VAL   B C    1 
ATOM   6259 O  O    . VAL   B 1 151 ? 37.993 -23.816 -12.219 1.00 13.28 ?  151 VAL   B O    1 
ATOM   6260 C  CB   . VAL   B 1 151 ? 37.361 -22.055 -9.644  1.00 13.97 ?  151 VAL   B CB   1 
ATOM   6261 C  CG1  . VAL   B 1 151 ? 36.184 -23.036 -9.728  1.00 15.19 ?  151 VAL   B CG1  1 
ATOM   6262 C  CG2  . VAL   B 1 151 ? 38.463 -22.566 -8.738  1.00 14.25 ?  151 VAL   B CG2  1 
ATOM   6263 H  H    . VAL   B 1 151 ? 36.280 -21.746 -12.130 1.00 15.16 ?  151 VAL   B H    1 
ATOM   6264 H  HA   . VAL   B 1 151 ? 38.584 -21.021 -10.905 1.00 15.03 ?  151 VAL   B HA   1 
ATOM   6265 H  HB   . VAL   B 1 151 ? 37.020 -21.238 -9.247  1.00 16.73 ?  151 VAL   B HB   1 
ATOM   6266 H  HG11 . VAL   B 1 151 ? 35.869 -23.237 -8.831  1.00 18.20 ?  151 VAL   B HG11 1 
ATOM   6267 H  HG12 . VAL   B 1 151 ? 35.463 -22.632 -10.243 1.00 18.20 ?  151 VAL   B HG12 1 
ATOM   6268 H  HG13 . VAL   B 1 151 ? 36.476 -23.853 -10.164 1.00 18.20 ?  151 VAL   B HG13 1 
ATOM   6269 H  HG21 . VAL   B 1 151 ? 38.117 -22.639 -7.832  1.00 17.07 ?  151 VAL   B HG21 1 
ATOM   6270 H  HG22 . VAL   B 1 151 ? 38.754 -23.438 -9.048  1.00 17.07 ?  151 VAL   B HG22 1 
ATOM   6271 H  HG23 . VAL   B 1 151 ? 39.204 -21.941 -8.755  1.00 17.07 ?  151 VAL   B HG23 1 
ATOM   6272 N  N    . TYR   B 1 152 ? 39.958 -22.790 -11.734 1.00 11.88 ?  152 TYR   B N    1 
ATOM   6273 C  CA   . TYR   B 1 152 ? 40.865 -23.768 -12.316 1.00 12.01 ?  152 TYR   B CA   1 
ATOM   6274 C  C    . TYR   B 1 152 ? 41.585 -24.449 -11.157 1.00 11.33 ?  152 TYR   B C    1 
ATOM   6275 O  O    . TYR   B 1 152 ? 42.430 -23.833 -10.500 1.00 12.01 ?  152 TYR   B O    1 
ATOM   6276 C  CB   . TYR   B 1 152 ? 41.837 -23.063 -13.262 1.00 12.92 ?  152 TYR   B CB   1 
ATOM   6277 C  CG   . TYR   B 1 152 ? 41.155 -22.603 -14.527 1.00 13.52 ?  152 TYR   B CG   1 
ATOM   6278 C  CD1  . TYR   B 1 152 ? 40.485 -21.384 -14.586 1.00 13.68 ?  152 TYR   B CD1  1 
ATOM   6279 C  CD2  . TYR   B 1 152 ? 41.152 -23.406 -15.653 1.00 14.69 ?  152 TYR   B CD2  1 
ATOM   6280 C  CE1  . TYR   B 1 152 ? 39.840 -20.978 -15.743 1.00 15.18 ?  152 TYR   B CE1  1 
ATOM   6281 C  CE2  . TYR   B 1 152 ? 40.513 -23.016 -16.809 1.00 15.69 ?  152 TYR   B CE2  1 
ATOM   6282 C  CZ   . TYR   B 1 152 ? 39.856 -21.803 -16.855 1.00 15.72 ?  152 TYR   B CZ   1 
ATOM   6283 O  OH   . TYR   B 1 152 ? 39.226 -21.431 -18.018 1.00 18.25 ?  152 TYR   B OH   1 
ATOM   6284 H  H    . TYR   B 1 152 ? 40.384 -22.128 -11.378 1.00 14.22 ?  152 TYR   B H    1 
ATOM   6285 H  HA   . TYR   B 1 152 ? 40.360 -24.434 -12.811 1.00 14.38 ?  152 TYR   B HA   1 
ATOM   6286 H  HB2  . TYR   B 1 152 ? 42.206 -22.285 -12.812 1.00 15.47 ?  152 TYR   B HB2  1 
ATOM   6287 H  HB3  . TYR   B 1 152 ? 42.549 -23.675 -13.502 1.00 15.47 ?  152 TYR   B HB3  1 
ATOM   6288 H  HD1  . TYR   B 1 152 ? 40.472 -20.833 -13.834 1.00 16.38 ?  152 TYR   B HD1  1 
ATOM   6289 H  HD2  . TYR   B 1 152 ? 41.589 -24.229 -15.626 1.00 17.59 ?  152 TYR   B HD2  1 
ATOM   6290 H  HE1  . TYR   B 1 152 ? 39.402 -20.161 -15.772 1.00 18.19 ?  152 TYR   B HE1  1 
ATOM   6291 H  HE2  . TYR   B 1 152 ? 40.529 -23.570 -17.556 1.00 18.80 ?  152 TYR   B HE2  1 
ATOM   6292 H  HH   . TYR   B 1 152 ? 38.874 -20.675 -17.917 1.00 21.87 ?  152 TYR   B HH   1 
ATOM   6293 N  N    . LEU   B 1 153 ? 41.213 -25.702 -10.886 1.00 11.71 ?  153 LEU   B N    1 
ATOM   6294 C  CA   . LEU   B 1 153 ? 41.725 -26.447 -9.747  1.00 11.86 ?  153 LEU   B CA   1 
ATOM   6295 C  C    . LEU   B 1 153 ? 42.958 -27.248 -10.144 1.00 12.14 ?  153 LEU   B C    1 
ATOM   6296 O  O    . LEU   B 1 153 ? 42.938 -27.974 -11.141 1.00 13.10 ?  153 LEU   B O    1 
ATOM   6297 C  CB   . LEU   B 1 153 ? 40.649 -27.406 -9.234  1.00 11.89 ?  153 LEU   B CB   1 
ATOM   6298 C  CG   . LEU   B 1 153 ? 39.388 -26.755 -8.666  1.00 13.01 ?  153 LEU   B CG   1 
ATOM   6299 C  CD1  . LEU   B 1 153 ? 38.288 -27.794 -8.515  1.00 13.77 ?  153 LEU   B CD1  1 
ATOM   6300 C  CD2  . LEU   B 1 153 ? 39.685 -26.093 -7.332  1.00 13.37 ?  153 LEU   B CD2  1 
ATOM   6301 H  H    . LEU   B 1 153 ? 40.637 -26.148 -11.359 1.00 14.02 ?  153 LEU   B H    1 
ATOM   6302 H  HA   . LEU   B 1 153 ? 41.952 -25.830 -9.038  1.00 14.20 ?  153 LEU   B HA   1 
ATOM   6303 H  HB2  . LEU   B 1 153 ? 40.373 -27.981 -9.965  1.00 14.23 ?  153 LEU   B HB2  1 
ATOM   6304 H  HB3  . LEU   B 1 153 ? 41.038 -27.950 -8.527  1.00 14.23 ?  153 LEU   B HB3  1 
ATOM   6305 H  HG   . LEU   B 1 153 ? 39.079 -26.067 -9.277  1.00 15.58 ?  153 LEU   B HG   1 
ATOM   6306 H  HD11 . LEU   B 1 153 ? 37.483 -27.351 -8.197  1.00 16.50 ?  153 LEU   B HD11 1 
ATOM   6307 H  HD12 . LEU   B 1 153 ? 38.125 -28.200 -9.376  1.00 16.50 ?  153 LEU   B HD12 1 
ATOM   6308 H  HD13 . LEU   B 1 153 ? 38.574 -28.460 -7.874  1.00 16.50 ?  153 LEU   B HD13 1 
ATOM   6309 H  HD21 . LEU   B 1 153 ? 38.868 -25.725 -6.968  1.00 16.01 ?  153 LEU   B HD21 1 
ATOM   6310 H  HD22 . LEU   B 1 153 ? 40.049 -26.759 -6.724  1.00 16.01 ?  153 LEU   B HD22 1 
ATOM   6311 H  HD23 . LEU   B 1 153 ? 40.337 -25.384 -7.466  1.00 16.01 ?  153 LEU   B HD23 1 
ATOM   6312 N  N    . ALA   B 1 154 ? 44.013 -27.139 -9.345  1.00 12.35 ?  154 ALA   B N    1 
ATOM   6313 C  CA   . ALA   B 1 154 ? 45.239 -27.906 -9.533  1.00 13.42 ?  154 ALA   B CA   1 
ATOM   6314 C  C    . ALA   B 1 154 ? 45.307 -28.979 -8.455  1.00 13.92 ?  154 ALA   B C    1 
ATOM   6315 O  O    . ALA   B 1 154 ? 45.227 -28.673 -7.257  1.00 14.91 ?  154 ALA   B O    1 
ATOM   6316 C  CB   . ALA   B 1 154 ? 46.466 -26.997 -9.476  1.00 14.47 ?  154 ALA   B CB   1 
ATOM   6317 H  H    . ALA   B 1 154 ? 44.039 -26.606 -8.668  1.00 14.79 ?  154 ALA   B H    1 
ATOM   6318 H  HA   . ALA   B 1 154 ? 45.223 -28.336 -10.399 1.00 16.08 ?  154 ALA   B HA   1 
ATOM   6319 H  HB1  . ALA   B 1 154 ? 47.266 -27.529 -9.602  1.00 17.34 ?  154 ALA   B HB1  1 
ATOM   6320 H  HB2  . ALA   B 1 154 ? 46.402 -26.327 -10.180 1.00 17.34 ?  154 ALA   B HB2  1 
ATOM   6321 H  HB3  . ALA   B 1 154 ? 46.498 -26.554 -8.611  1.00 17.34 ?  154 ALA   B HB3  1 
ATOM   6322 N  N    . VAL   B 1 155 ? 45.426 -30.231 -8.881  1.00 13.12 ?  155 VAL   B N    1 
ATOM   6323 C  CA   . VAL   B 1 155 ? 45.534 -31.376 -7.987  1.00 13.32 ?  155 VAL   B CA   1 
ATOM   6324 C  C    . VAL   B 1 155 ? 46.876 -32.044 -8.261  1.00 13.11 ?  155 VAL   B C    1 
ATOM   6325 O  O    . VAL   B 1 155 ? 47.115 -32.538 -9.369  1.00 14.98 ?  155 VAL   B O    1 
ATOM   6326 C  CB   . VAL   B 1 155 ? 44.379 -32.370 -8.188  1.00 14.64 ?  155 VAL   B CB   1 
ATOM   6327 C  CG1  . VAL   B 1 155 ? 44.559 -33.564 -7.270  1.00 14.56 ?  155 VAL   B CG1  1 
ATOM   6328 C  CG2  . VAL   B 1 155 ? 43.038 -31.680 -7.937  1.00 15.63 ?  155 VAL   B CG2  1 
ATOM   6329 H  H    . VAL   B 1 155 ? 45.459 -30.450 -9.715  1.00 15.71 ?  155 VAL   B H    1 
ATOM   6330 H  HA   . VAL   B 1 155 ? 45.522 -31.073 -7.066  1.00 15.95 ?  155 VAL   B HA   1 
ATOM   6331 H  HB   . VAL   B 1 155 ? 44.386 -32.684 -9.106  1.00 17.54 ?  155 VAL   B HB   1 
ATOM   6332 H  HG11 . VAL   B 1 155 ? 43.731 -34.064 -7.233  1.00 17.45 ?  155 VAL   B HG11 1 
ATOM   6333 H  HG12 . VAL   B 1 155 ? 45.270 -34.129 -7.618  1.00 17.45 ?  155 VAL   B HG12 1 
ATOM   6334 H  HG13 . VAL   B 1 155 ? 44.795 -33.248 -6.382  1.00 17.45 ?  155 VAL   B HG13 1 
ATOM   6335 H  HG21 . VAL   B 1 155 ? 42.327 -32.333 -8.028  1.00 18.72 ?  155 VAL   B HG21 1 
ATOM   6336 H  HG22 . VAL   B 1 155 ? 43.037 -31.312 -7.039  1.00 18.72 ?  155 VAL   B HG22 1 
ATOM   6337 H  HG23 . VAL   B 1 155 ? 42.919 -30.969 -8.586  1.00 18.72 ?  155 VAL   B HG23 1 
ATOM   6338 N  N    . PHE   B 1 156 ? 47.740 -32.080 -7.246  1.00 13.74 ?  156 PHE   B N    1 
ATOM   6339 C  CA   . PHE   B 1 156 ? 49.118 -32.539 -7.443  1.00 14.81 ?  156 PHE   B CA   1 
ATOM   6340 C  C    . PHE   B 1 156 ? 49.209 -34.040 -7.730  1.00 15.86 ?  156 PHE   B C    1 
ATOM   6341 O  O    . PHE   B 1 156 ? 49.931 -34.465 -8.642  1.00 17.86 ?  156 PHE   B O    1 
ATOM   6342 C  CB   . PHE   B 1 156 ? 49.947 -32.170 -6.214  1.00 15.19 ?  156 PHE   B CB   1 
ATOM   6343 C  CG   . PHE   B 1 156 ? 51.372 -32.633 -6.274  1.00 15.67 ?  156 PHE   B CG   1 
ATOM   6344 C  CD1  . PHE   B 1 156 ? 52.248 -32.093 -7.196  1.00 17.31 ?  156 PHE   B CD1  1 
ATOM   6345 C  CD2  . PHE   B 1 156 ? 51.838 -33.582 -5.388  1.00 15.96 ?  156 PHE   B CD2  1 
ATOM   6346 C  CE1  . PHE   B 1 156 ? 53.569 -32.506 -7.244  1.00 18.29 ?  156 PHE   B CE1  1 
ATOM   6347 C  CE2  . PHE   B 1 156 ? 53.159 -33.999 -5.430  1.00 17.61 ?  156 PHE   B CE2  1 
ATOM   6348 C  CZ   . PHE   B 1 156 ? 54.015 -33.462 -6.364  1.00 18.01 ?  156 PHE   B CZ   1 
ATOM   6349 H  H    . PHE   B 1 156 ? 47.555 -31.855 -6.439  1.00 16.45 ?  156 PHE   B H    1 
ATOM   6350 H  HA   . PHE   B 1 156 ? 49.493 -32.072 -8.201  1.00 17.75 ?  156 PHE   B HA   1 
ATOM   6351 H  HB2  . PHE   B 1 156 ? 49.955 -31.203 -6.126  1.00 18.20 ?  156 PHE   B HB2  1 
ATOM   6352 H  HB3  . PHE   B 1 156 ? 49.541 -32.567 -5.429  1.00 18.20 ?  156 PHE   B HB3  1 
ATOM   6353 H  HD1  . PHE   B 1 156 ? 51.951 -31.445 -7.797  1.00 20.75 ?  156 PHE   B HD1  1 
ATOM   6354 H  HD2  . PHE   B 1 156 ? 51.257 -33.950 -4.760  1.00 19.13 ?  156 PHE   B HD2  1 
ATOM   6355 H  HE1  . PHE   B 1 156 ? 54.154 -32.142 -7.873  1.00 21.92 ?  156 PHE   B HE1  1 
ATOM   6356 H  HE2  . PHE   B 1 156 ? 53.462 -34.650 -4.834  1.00 21.10 ?  156 PHE   B HE2  1 
ATOM   6357 H  HZ   . PHE   B 1 156 ? 54.903 -33.743 -6.394  1.00 21.58 ?  156 PHE   B HZ   1 
ATOM   6358 N  N    . ASP   B 1 157 ? 48.540 -34.861 -6.932  1.00 16.19 ?  157 ASP   B N    1 
ATOM   6359 C  CA   . ASP   B 1 157 ? 48.687 -36.309 -7.029  1.00 17.56 ?  157 ASP   B CA   1 
ATOM   6360 C  C    . ASP   B 1 157 ? 47.776 -36.853 -8.124  1.00 17.96 ?  157 ASP   B C    1 
ATOM   6361 O  O    . ASP   B 1 157 ? 46.548 -36.740 -8.027  1.00 17.38 ?  157 ASP   B O    1 
ATOM   6362 C  CB   . ASP   B 1 157 ? 48.325 -36.922 -5.683  1.00 19.32 ?  157 ASP   B CB   1 
ATOM   6363 C  CG   . ASP   B 1 157 ? 48.472 -38.427 -5.666  1.00 21.29 ?  157 ASP   B CG   1 
ATOM   6364 O  OD1  . ASP   B 1 157 ? 48.805 -39.025 -6.717  1.00 21.58 ?  157 ASP   B OD1  1 
ATOM   6365 O  OD2  . ASP   B 1 157 ? 48.265 -39.009 -4.584  1.00 23.37 -1 157 ASP   B OD2  1 
ATOM   6366 H  H    . ASP   B 1 157 ? 47.995 -34.607 -6.325  1.00 19.40 ?  157 ASP   B H    1 
ATOM   6367 H  HA   . ASP   B 1 157 ? 49.609 -36.540 -7.240  1.00 21.05 ?  157 ASP   B HA   1 
ATOM   6368 H  HB2  . ASP   B 1 157 ? 48.895 -36.538 -5.001  1.00 23.15 ?  157 ASP   B HB2  1 
ATOM   6369 H  HB3  . ASP   B 1 157 ? 47.395 -36.711 -5.488  1.00 23.15 ?  157 ASP   B HB3  1 
ATOM   6370 N  N    . LYS   B 1 158 ? 48.374 -37.466 -9.153  1.00 19.12 ?  158 LYS   B N    1 
ATOM   6371 C  CA   . LYS   B 1 158 ? 47.597 -38.081 -10.234 1.00 20.14 ?  158 LYS   B CA   1 
ATOM   6372 C  C    . LYS   B 1 158 ? 46.541 -39.050 -9.700  1.00 19.78 ?  158 LYS   B C    1 
ATOM   6373 O  O    . LYS   B 1 158 ? 45.435 -39.144 -10.250 1.00 19.86 ?  158 LYS   B O    1 
ATOM   6374 C  CB   . LYS   B 1 158 ? 48.543 -38.794 -11.212 1.00 21.86 ?  158 LYS   B CB   1 
ATOM   6375 C  CG   . LYS   B 1 158 ? 47.858 -39.698 -12.230 1.00 23.98 ?  158 LYS   B CG   1 
ATOM   6376 C  CD   . LYS   B 1 158 ? 47.013 -38.916 -13.214 1.00 26.17 ?  158 LYS   B CD   1 
ATOM   6377 C  CE   . LYS   B 1 158 ? 46.416 -39.838 -14.264 1.00 27.88 ?  158 LYS   B CE   1 
ATOM   6378 N  NZ   . LYS   B 1 158 ? 45.334 -39.175 -15.043 1.00 28.27 ?  158 LYS   B NZ   1 
ATOM   6379 H  H    . LYS   B 1 158 ? 49.229 -37.539 -9.251  1.00 22.91 ?  158 LYS   B H    1 
ATOM   6380 H  HA   . LYS   B 1 158 ? 47.142 -37.381 -10.731 1.00 24.14 ?  158 LYS   B HA   1 
ATOM   6381 H  HB2  . LYS   B 1 158 ? 49.041 -38.123 -11.712 1.00 26.20 ?  158 LYS   B HB2  1 
ATOM   6382 H  HB3  . LYS   B 1 158 ? 49.162 -39.340 -10.705 1.00 26.20 ?  158 LYS   B HB3  1 
ATOM   6383 H  HG2  . LYS   B 1 158 ? 48.538 -40.170 -12.736 1.00 28.75 ?  158 LYS   B HG2  1 
ATOM   6384 H  HG3  . LYS   B 1 158 ? 47.288 -40.342 -11.778 1.00 28.75 ?  158 LYS   B HG3  1 
ATOM   6385 H  HD2  . LYS   B 1 158 ? 46.288 -38.477 -12.742 1.00 31.37 ?  158 LYS   B HD2  1 
ATOM   6386 H  HD3  . LYS   B 1 158 ? 47.568 -38.259 -13.665 1.00 31.37 ?  158 LYS   B HD3  1 
ATOM   6387 H  HE2  . LYS   B 1 158 ? 47.110 -40.109 -14.884 1.00 33.43 ?  158 LYS   B HE2  1 
ATOM   6388 H  HE3  . LYS   B 1 158 ? 46.038 -40.618 -13.826 1.00 33.43 ?  158 LYS   B HE3  1 
ATOM   6389 H  HZ1  . LYS   B 1 158 ? 45.003 -39.738 -15.647 1.00 33.89 ?  158 LYS   B HZ1  1 
ATOM   6390 H  HZ2  . LYS   B 1 158 ? 44.678 -38.919 -14.497 1.00 33.89 ?  158 LYS   B HZ2  1 
ATOM   6391 H  HZ3  . LYS   B 1 158 ? 45.656 -38.458 -15.462 1.00 33.89 ?  158 LYS   B HZ3  1 
ATOM   6392 N  N    . ASN   B 1 159 ? 46.865 -39.801 -8.646  1.00 19.81 ?  159 ASN   B N    1 
ATOM   6393 C  CA   . ASN   B 1 159 ? 45.912 -40.788 -8.142  1.00 20.32 ?  159 ASN   B CA   1 
ATOM   6394 C  C    . ASN   B 1 159 ? 44.709 -40.121 -7.470  1.00 19.13 ?  159 ASN   B C    1 
ATOM   6395 O  O    . ASN   B 1 159 ? 43.577 -40.612 -7.586  1.00 19.49 ?  159 ASN   B O    1 
ATOM   6396 C  CB   . ASN   B 1 159 ? 46.620 -41.765 -7.209  1.00 22.00 ?  159 ASN   B CB   1 
ATOM   6397 C  CG   . ASN   B 1 159 ? 47.647 -42.611 -7.931  1.00 24.32 ?  159 ASN   B CG   1 
ATOM   6398 O  OD1  . ASN   B 1 159 ? 47.394 -43.115 -9.034  1.00 24.86 ?  159 ASN   B OD1  1 
ATOM   6399 N  ND2  . ASN   B 1 159 ? 48.815 -42.775 -7.316  1.00 25.15 ?  159 ASN   B ND2  1 
ATOM   6400 H  H    . ASN   B 1 159 ? 47.613 -39.754 -8.225  1.00 23.75 ?  159 ASN   B H    1 
ATOM   6401 H  HA   . ASN   B 1 159 ? 45.582 -41.295 -8.901  1.00 24.35 ?  159 ASN   B HA   1 
ATOM   6402 H  HB2  . ASN   B 1 159 ? 47.074 -41.268 -6.513  1.00 26.37 ?  159 ASN   B HB2  1 
ATOM   6403 H  HB3  . ASN   B 1 159 ? 45.964 -42.363 -6.827  1.00 26.37 ?  159 ASN   B HB3  1 
ATOM   6404 H  HD21 . ASN   B 1 159 ? 49.437 -43.245 -7.685  1.00 30.15 ?  159 ASN   B HD21 1 
ATOM   6405 H  HD22 . ASN   B 1 159 ? 48.949 -42.424 -6.541  1.00 30.15 ?  159 ASN   B HD22 1 
ATOM   6406 N  N    . LEU   B 1 160 ? 44.923 -38.998 -6.774  1.00 18.36 ?  160 LEU   B N    1 
ATOM   6407 C  CA   . LEU   B 1 160 ? 43.791 -38.254 -6.233  1.00 17.32 ?  160 LEU   B CA   1 
ATOM   6408 C  C    . LEU   B 1 160 ? 43.004 -37.587 -7.349  1.00 16.57 ?  160 LEU   B C    1 
ATOM   6409 O  O    . LEU   B 1 160 ? 41.766 -37.598 -7.338  1.00 16.06 ?  160 LEU   B O    1 
ATOM   6410 C  CB   . LEU   B 1 160 ? 44.260 -37.222 -5.207  1.00 17.04 ?  160 LEU   B CB   1 
ATOM   6411 C  CG   . LEU   B 1 160 ? 43.128 -36.328 -4.672  1.00 16.87 ?  160 LEU   B CG   1 
ATOM   6412 C  CD1  . LEU   B 1 160 ? 42.019 -37.170 -4.058  1.00 17.66 ?  160 LEU   B CD1  1 
ATOM   6413 C  CD2  . LEU   B 1 160 ? 43.658 -35.329 -3.654  1.00 16.89 ?  160 LEU   B CD2  1 
ATOM   6414 H  H    . LEU   B 1 160 ? 45.701 -38.657 -6.609  1.00 22.00 ?  160 LEU   B H    1 
ATOM   6415 H  HA   . LEU   B 1 160 ? 43.203 -38.876 -5.787  1.00 20.76 ?  160 LEU   B HA   1 
ATOM   6416 H  HB2  . LEU   B 1 160 ? 44.659 -37.691 -4.454  1.00 20.42 ?  160 LEU   B HB2  1 
ATOM   6417 H  HB3  . LEU   B 1 160 ? 44.928 -36.648 -5.621  1.00 20.42 ?  160 LEU   B HB3  1 
ATOM   6418 H  HG   . LEU   B 1 160 ? 42.749 -35.828 -5.408  1.00 20.21 ?  160 LEU   B HG   1 
ATOM   6419 H  HD11 . LEU   B 1 160 ? 41.396 -36.585 -3.605  1.00 21.16 ?  160 LEU   B HD11 1 
ATOM   6420 H  HD12 . LEU   B 1 160 ? 41.562 -37.662 -4.759  1.00 21.16 ?  160 LEU   B HD12 1 
ATOM   6421 H  HD13 . LEU   B 1 160 ? 42.409 -37.794 -3.421  1.00 21.16 ?  160 LEU   B HD13 1 
ATOM   6422 H  HD21 . LEU   B 1 160 ? 42.927 -34.763 -3.365  1.00 20.23 ?  160 LEU   B HD21 1 
ATOM   6423 H  HD22 . LEU   B 1 160 ? 44.023 -35.814 -2.897  1.00 20.23 ?  160 LEU   B HD22 1 
ATOM   6424 H  HD23 . LEU   B 1 160 ? 44.350 -34.793 -4.071  1.00 20.23 ?  160 LEU   B HD23 1 
ATOM   6425 N  N    . TYR   B 1 161 ? 43.702 -37.014 -8.330  1.00 16.72 ?  161 TYR   B N    1 
ATOM   6426 C  CA   . TYR   B 1 161 ? 43.030 -36.445 -9.494  1.00 16.49 ?  161 TYR   B CA   1 
ATOM   6427 C  C    . TYR   B 1 161 ? 42.086 -37.468 -10.119 1.00 16.72 ?  161 TYR   B C    1 
ATOM   6428 O  O    . TYR   B 1 161 ? 40.913 -37.175 -10.378 1.00 16.57 ?  161 TYR   B O    1 
ATOM   6429 C  CB   . TYR   B 1 161 ? 44.072 -35.967 -10.512 1.00 17.13 ?  161 TYR   B CB   1 
ATOM   6430 C  CG   . TYR   B 1 161 ? 43.495 -35.503 -11.826 1.00 17.84 ?  161 TYR   B CG   1 
ATOM   6431 C  CD1  . TYR   B 1 161 ? 43.098 -34.181 -11.996 1.00 18.02 ?  161 TYR   B CD1  1 
ATOM   6432 C  CD2  . TYR   B 1 161 ? 43.328 -36.381 -12.892 1.00 18.42 ?  161 TYR   B CD2  1 
ATOM   6433 C  CE1  . TYR   B 1 161 ? 42.570 -33.746 -13.181 1.00 19.08 ?  161 TYR   B CE1  1 
ATOM   6434 C  CE2  . TYR   B 1 161 ? 42.791 -35.952 -14.087 1.00 19.58 ?  161 TYR   B CE2  1 
ATOM   6435 C  CZ   . TYR   B 1 161 ? 42.416 -34.630 -14.225 1.00 19.69 ?  161 TYR   B CZ   1 
ATOM   6436 O  OH   . TYR   B 1 161 ? 41.877 -34.185 -15.408 1.00 21.59 ?  161 TYR   B OH   1 
ATOM   6437 H  H    . TYR   B 1 161 ? 44.558 -36.950 -8.353  1.00 20.04 ?  161 TYR   B H    1 
ATOM   6438 H  HA   . TYR   B 1 161 ? 42.505 -35.679 -9.220  1.00 19.76 ?  161 TYR   B HA   1 
ATOM   6439 H  HB2  . TYR   B 1 161 ? 44.563 -35.218 -10.131 1.00 20.53 ?  161 TYR   B HB2  1 
ATOM   6440 H  HB3  . TYR   B 1 161 ? 44.685 -36.692 -10.705 1.00 20.53 ?  161 TYR   B HB3  1 
ATOM   6441 H  HD1  . TYR   B 1 161 ? 43.206 -33.571 -11.298 1.00 21.60 ?  161 TYR   B HD1  1 
ATOM   6442 H  HD2  . TYR   B 1 161 ? 43.580 -37.270 -12.799 1.00 22.08 ?  161 TYR   B HD2  1 
ATOM   6443 H  HE1  . TYR   B 1 161 ? 42.314 -32.852 -13.277 1.00 22.87 ?  161 TYR   B HE1  1 
ATOM   6444 H  HE2  . TYR   B 1 161 ? 42.681 -36.548 -14.793 1.00 23.46 ?  161 TYR   B HE2  1 
ATOM   6445 H  HH   . TYR   B 1 161 ? 41.827 -34.820 -15.958 1.00 25.87 ?  161 TYR   B HH   1 
ATOM   6446 N  N    . ASP   B 1 162 ? 42.581 -38.687 -10.348 1.00 17.18 ?  162 ASP   B N    1 
ATOM   6447 C  CA   . ASP   B 1 162 ? 41.752 -39.719 -10.964 1.00 18.03 ?  162 ASP   B CA   1 
ATOM   6448 C  C    . ASP   B 1 162 ? 40.544 -40.059 -10.096 1.00 17.42 ?  162 ASP   B C    1 
ATOM   6449 O  O    . ASP   B 1 162 ? 39.439 -40.273 -10.612 1.00 17.69 ?  162 ASP   B O    1 
ATOM   6450 C  CB   . ASP   B 1 162 ? 42.578 -40.983 -11.224 1.00 19.45 ?  162 ASP   B CB   1 
ATOM   6451 C  CG   . ASP   B 1 162 ? 43.584 -40.818 -12.352 1.00 20.93 ?  162 ASP   B CG   1 
ATOM   6452 O  OD1  . ASP   B 1 162 ? 43.451 -39.875 -13.155 1.00 21.33 ?  162 ASP   B OD1  1 
ATOM   6453 O  OD2  . ASP   B 1 162 ? 44.498 -41.665 -12.455 1.00 22.56 -1 162 ASP   B OD2  1 
ATOM   6454 H  H    . ASP   B 1 162 ? 43.382 -38.935 -10.160 1.00 20.59 ?  162 ASP   B H    1 
ATOM   6455 H  HA   . ASP   B 1 162 ? 41.423 -39.396 -11.815 1.00 21.60 ?  162 ASP   B HA   1 
ATOM   6456 H  HB2  . ASP   B 1 162 ? 43.074 -41.210 -10.424 1.00 23.31 ?  162 ASP   B HB2  1 
ATOM   6457 H  HB3  . ASP   B 1 162 ? 41.982 -41.707 -11.466 1.00 23.31 ?  162 ASP   B HB3  1 
ATOM   6458 N  N    . LYS   B 1 163 ? 40.736 -40.137 -8.777  1.00 16.72 ?  163 LYS   B N    1 
ATOM   6459 C  CA   . LYS   B 1 163 ? 39.613 -40.415 -7.887  1.00 17.45 ?  163 LYS   B CA   1 
ATOM   6460 C  C    . LYS   B 1 163 ? 38.569 -39.304 -7.947  1.00 15.94 ?  163 LYS   B C    1 
ATOM   6461 O  O    . LYS   B 1 163 ? 37.362 -39.575 -7.954  1.00 16.89 ?  163 LYS   B O    1 
ATOM   6462 C  CB   . LYS   B 1 163 ? 40.105 -40.602 -6.454  1.00 20.60 ?  163 LYS   B CB   1 
ATOM   6463 C  CG   . LYS   B 1 163 ? 39.019 -41.090 -5.522  1.00 26.52 ?  163 LYS   B CG   1 
ATOM   6464 C  CD   . LYS   B 1 163 ? 39.502 -41.264 -4.095  1.00 32.05 ?  163 LYS   B CD   1 
ATOM   6465 C  CE   . LYS   B 1 163 ? 38.419 -41.911 -3.241  1.00 35.94 ?  163 LYS   B CE   1 
ATOM   6466 N  NZ   . LYS   B 1 163 ? 38.616 -41.663 -1.785  1.00 38.71 ?  163 LYS   B NZ   1 
ATOM   6467 H  H    . LYS   B 1 163 ? 41.496 -40.025 -8.381  1.00 20.03 ?  163 LYS   B H    1 
ATOM   6468 H  HA   . LYS   B 1 163 ? 39.193 -41.241 -8.169  1.00 20.90 ?  163 LYS   B HA   1 
ATOM   6469 H  HB2  . LYS   B 1 163 ? 40.822 -41.258 -6.446  1.00 24.69 ?  163 LYS   B HB2  1 
ATOM   6470 H  HB3  . LYS   B 1 163 ? 40.430 -39.754 -6.116  1.00 24.69 ?  163 LYS   B HB3  1 
ATOM   6471 H  HG2  . LYS   B 1 163 ? 38.293 -40.448 -5.515  1.00 31.79 ?  163 LYS   B HG2  1 
ATOM   6472 H  HG3  . LYS   B 1 163 ? 38.697 -41.951 -5.837  1.00 31.79 ?  163 LYS   B HG3  1 
ATOM   6473 H  HD2  . LYS   B 1 163 ? 40.284 -41.840 -4.086  1.00 38.43 ?  163 LYS   B HD2  1 
ATOM   6474 H  HD3  . LYS   B 1 163 ? 39.716 -40.397 -3.719  1.00 38.43 ?  163 LYS   B HD3  1 
ATOM   6475 H  HE2  . LYS   B 1 163 ? 37.553 -41.558 -3.498  1.00 43.10 ?  163 LYS   B HE2  1 
ATOM   6476 H  HE3  . LYS   B 1 163 ? 38.436 -42.869 -3.386  1.00 43.10 ?  163 LYS   B HE3  1 
ATOM   6477 H  HZ1  . LYS   B 1 163 ? 37.964 -42.053 -1.320  1.00 46.43 ?  163 LYS   B HZ1  1 
ATOM   6478 H  HZ2  . LYS   B 1 163 ? 39.398 -41.997 -1.524  1.00 46.43 ?  163 LYS   B HZ2  1 
ATOM   6479 H  HZ3  . LYS   B 1 163 ? 38.604 -40.788 -1.621  1.00 46.43 ?  163 LYS   B HZ3  1 
ATOM   6480 N  N    . LEU   B 1 164 ? 39.017 -38.048 -7.993  1.00 14.88 ?  164 LEU   B N    1 
ATOM   6481 C  CA   . LEU   B 1 164 ? 38.103 -36.912 -8.051  1.00 14.41 ?  164 LEU   B CA   1 
ATOM   6482 C  C    . LEU   B 1 164 ? 37.326 -36.893 -9.362  1.00 14.66 ?  164 LEU   B C    1 
ATOM   6483 O  O    . LEU   B 1 164 ? 36.102 -36.695 -9.368  1.00 15.80 ?  164 LEU   B O    1 
ATOM   6484 C  CB   . LEU   B 1 164 ? 38.904 -35.621 -7.886  1.00 13.96 ?  164 LEU   B CB   1 
ATOM   6485 C  CG   . LEU   B 1 164 ? 39.441 -35.341 -6.486  1.00 15.06 ?  164 LEU   B CG   1 
ATOM   6486 C  CD1  . LEU   B 1 164 ? 40.528 -34.280 -6.558  1.00 15.33 ?  164 LEU   B CD1  1 
ATOM   6487 C  CD2  . LEU   B 1 164 ? 38.330 -34.900 -5.547  1.00 17.07 ?  164 LEU   B CD2  1 
ATOM   6488 H  H    . LEU   B 1 164 ? 39.857 -37.829 -7.995  1.00 17.83 ?  164 LEU   B H    1 
ATOM   6489 H  HA   . LEU   B 1 164 ? 37.476 -36.973 -7.325  1.00 17.26 ?  164 LEU   B HA   1 
ATOM   6490 H  HB2  . LEU   B 1 164 ? 39.668 -35.651 -8.488  1.00 16.73 ?  164 LEU   B HB2  1 
ATOM   6491 H  HB3  . LEU   B 1 164 ? 38.336 -34.875 -8.132  1.00 16.73 ?  164 LEU   B HB3  1 
ATOM   6492 H  HG   . LEU   B 1 164 ? 39.842 -36.146 -6.132  1.00 18.04 ?  164 LEU   B HG   1 
ATOM   6493 H  HD11 . LEU   B 1 164 ? 40.860 -34.094 -5.663  1.00 18.37 ?  164 LEU   B HD11 1 
ATOM   6494 H  HD12 . LEU   B 1 164 ? 41.261 -34.603 -7.114  1.00 18.37 ?  164 LEU   B HD12 1 
ATOM   6495 H  HD13 . LEU   B 1 164 ? 40.164 -33.466 -6.946  1.00 18.37 ?  164 LEU   B HD13 1 
ATOM   6496 H  HD21 . LEU   B 1 164 ? 38.712 -34.685 -4.683  1.00 20.46 ?  164 LEU   B HD21 1 
ATOM   6497 H  HD22 . LEU   B 1 164 ? 37.890 -34.121 -5.919  1.00 20.46 ?  164 LEU   B HD22 1 
ATOM   6498 H  HD23 . LEU   B 1 164 ? 37.694 -35.627 -5.455  1.00 20.46 ?  164 LEU   B HD23 1 
ATOM   6499 N  N    . VAL   B 1 165 ? 38.020 -37.075 -10.487 1.00 16.10 ?  165 VAL   B N    1 
ATOM   6500 C  CA   . VAL   B 1 165 ? 37.367 -37.012 -11.790 1.00 17.67 ?  165 VAL   B CA   1 
ATOM   6501 C  C    . VAL   B 1 165 ? 36.437 -38.204 -11.975 1.00 19.48 ?  165 VAL   B C    1 
ATOM   6502 O  O    . VAL   B 1 165 ? 35.276 -38.056 -12.379 1.00 20.76 ?  165 VAL   B O    1 
ATOM   6503 C  CB   . VAL   B 1 165 ? 38.414 -36.938 -12.916 1.00 18.93 ?  165 VAL   B CB   1 
ATOM   6504 C  CG1  . VAL   B 1 165 ? 37.753 -37.049 -14.271 1.00 20.37 ?  165 VAL   B CG1  1 
ATOM   6505 C  CG2  . VAL   B 1 165 ? 39.209 -35.650 -12.824 1.00 18.45 ?  165 VAL   B CG2  1 
ATOM   6506 H  H    . VAL   B 1 165 ? 38.873 -37.225 -10.523 1.00 19.29 ?  165 VAL   B H    1 
ATOM   6507 H  HA   . VAL   B 1 165 ? 36.834 -36.207 -11.836 1.00 21.17 ?  165 VAL   B HA   1 
ATOM   6508 H  HB   . VAL   B 1 165 ? 39.039 -37.676 -12.823 1.00 22.68 ?  165 VAL   B HB   1 
ATOM   6509 H  HG11 . VAL   B 1 165 ? 38.379 -36.764 -14.953 1.00 24.42 ?  165 VAL   B HG11 1 
ATOM   6510 H  HG12 . VAL   B 1 165 ? 37.506 -37.977 -14.423 1.00 24.42 ?  165 VAL   B HG12 1 
ATOM   6511 H  HG13 . VAL   B 1 165 ? 36.965 -36.490 -14.284 1.00 24.42 ?  165 VAL   B HG13 1 
ATOM   6512 H  HG21 . VAL   B 1 165 ? 39.850 -35.615 -13.555 1.00 22.12 ?  165 VAL   B HG21 1 
ATOM   6513 H  HG22 . VAL   B 1 165 ? 38.601 -34.895 -12.888 1.00 22.12 ?  165 VAL   B HG22 1 
ATOM   6514 H  HG23 . VAL   B 1 165 ? 39.679 -35.623 -11.975 1.00 22.12 ?  165 VAL   B HG23 1 
ATOM   6515 N  N    . SER   B 1 166 ? 36.945 -39.409 -11.692 1.00 20.24 ?  166 SER   B N    1 
ATOM   6516 C  CA   . SER   B 1 166 ? 36.186 -40.620 -11.968 1.00 21.37 ?  166 SER   B CA   1 
ATOM   6517 C  C    . SER   B 1 166 ? 34.931 -40.703 -11.116 1.00 21.66 ?  166 SER   B C    1 
ATOM   6518 O  O    . SER   B 1 166 ? 33.959 -41.324 -11.540 1.00 22.90 ?  166 SER   B O    1 
ATOM   6519 C  CB   . SER   B 1 166 ? 37.051 -41.874 -11.795 1.00 22.52 ?  166 SER   B CB   1 
ATOM   6520 O  OG   . SER   B 1 166 ? 37.421 -42.073 -10.441 1.00 22.64 ?  166 SER   B OG   1 
ATOM   6521 H  H    . SER   B 1 166 ? 37.726 -39.545 -11.354 1.00 24.25 ?  166 SER   B H    1 
ATOM   6522 H  HA   . SER   B 1 166 ? 35.902 -40.595 -12.894 1.00 25.61 ?  166 SER   B HA   1 
ATOM   6523 H  HB2  . SER   B 1 166 ? 36.543 -42.644 -12.098 1.00 26.99 ?  166 SER   B HB2  1 
ATOM   6524 H  HB3  . SER   B 1 166 ? 37.850 -41.777 -12.337 1.00 26.99 ?  166 SER   B HB3  1 
ATOM   6525 H  HG   . SER   B 1 166 ? 37.877 -41.424 -10.172 1.00 27.14 ?  166 SER   B HG   1 
ATOM   6526 N  N    . SER   B 1 167 ? 34.913 -40.095 -9.932  1.00 20.14 ?  167 SER   B N    1 
ATOM   6527 C  CA   . SER   B 1 167 ? 33.759 -40.150 -9.042  1.00 19.89 ?  167 SER   B CA   1 
ATOM   6528 C  C    . SER   B 1 167 ? 32.845 -38.930 -9.140  1.00 19.38 ?  167 SER   B C    1 
ATOM   6529 O  O    . SER   B 1 167 ? 31.770 -38.933 -8.529  1.00 19.69 ?  167 SER   B O    1 
ATOM   6530 C  CB   . SER   B 1 167 ? 34.208 -40.330 -7.585  1.00 19.67 ?  167 SER   B CB   1 
ATOM   6531 O  OG   . SER   B 1 167 ? 34.880 -39.165 -7.116  1.00 19.45 ?  167 SER   B OG   1 
ATOM   6532 H  H    . SER   B 1 167 ? 35.566 -39.639 -9.620  1.00 24.14 ?  167 SER   B H    1 
ATOM   6533 H  HA   . SER   B 1 167 ? 33.225 -40.928 -9.276  1.00 23.84 ?  167 SER   B HA   1 
ATOM   6534 H  HB2  . SER   B 1 167 ? 33.427 -40.495 -7.030  1.00 23.58 ?  167 SER   B HB2  1 
ATOM   6535 H  HB3  . SER   B 1 167 ? 34.809 -41.097 -7.535  1.00 23.58 ?  167 SER   B HB3  1 
ATOM   6536 H  HG   . SER   B 1 167 ? 35.561 -39.030 -7.589  1.00 23.31 ?  167 SER   B HG   1 
ATOM   6537 N  N    . PHE   B 1 168 ? 33.225 -37.894 -9.893  1.00 19.07 ?  168 PHE   B N    1 
ATOM   6538 C  CA   . PHE   B 1 168 ? 32.394 -36.692 -9.962  1.00 18.40 ?  168 PHE   B CA   1 
ATOM   6539 C  C    . PHE   B 1 168 ? 31.078 -36.957 -10.689 1.00 16.17 ?  168 PHE   B C    1 
ATOM   6540 O  O    . PHE   B 1 168 ? 30.034 -36.367 -10.342 1.00 16.85 ?  168 PHE   B O    1 
ATOM   6541 C  CB   . PHE   B 1 168 ? 33.156 -35.557 -10.645 1.00 19.17 ?  168 PHE   B CB   1 
ATOM   6542 C  CG   . PHE   B 1 168 ? 32.353 -34.306 -10.773 1.00 19.16 ?  168 PHE   B CG   1 
ATOM   6543 C  CD1  . PHE   B 1 168 ? 32.021 -33.575 -9.644  1.00 20.21 ?  168 PHE   B CD1  1 
ATOM   6544 C  CD2  . PHE   B 1 168 ? 31.902 -33.871 -12.006 1.00 18.52 ?  168 PHE   B CD2  1 
ATOM   6545 C  CE1  . PHE   B 1 168 ? 31.257 -32.427 -9.737  1.00 20.74 ?  168 PHE   B CE1  1 
ATOM   6546 C  CE2  . PHE   B 1 168 ? 31.151 -32.706 -12.115 1.00 19.61 ?  168 PHE   B CE2  1 
ATOM   6547 C  CZ   . PHE   B 1 168 ? 30.822 -31.982 -10.975 1.00 19.93 ?  168 PHE   B CZ   1 
ATOM   6548 H  H    . PHE   B 1 168 ? 33.942 -37.870 -10.365 1.00 22.86 ?  168 PHE   B H    1 
ATOM   6549 H  HA   . PHE   B 1 168 ? 32.177 -36.411 -9.064  1.00 22.06 ?  168 PHE   B HA   1 
ATOM   6550 H  HB2  . PHE   B 1 168 ? 33.944 -35.350 -10.122 1.00 22.98 ?  168 PHE   B HB2  1 
ATOM   6551 H  HB3  . PHE   B 1 168 ? 33.411 -35.837 -11.536 1.00 22.98 ?  168 PHE   B HB3  1 
ATOM   6552 H  HD1  . PHE   B 1 168 ? 32.307 -33.872 -8.811  1.00 24.22 ?  168 PHE   B HD1  1 
ATOM   6553 H  HD2  . PHE   B 1 168 ? 32.120 -34.347 -12.773 1.00 22.19 ?  168 PHE   B HD2  1 
ATOM   6554 H  HE1  . PHE   B 1 168 ? 31.043 -31.946 -8.970  1.00 24.86 ?  168 PHE   B HE1  1 
ATOM   6555 H  HE2  . PHE   B 1 168 ? 30.852 -32.415 -12.949 1.00 23.50 ?  168 PHE   B HE2  1 
ATOM   6556 H  HZ   . PHE   B 1 168 ? 30.309 -31.207 -11.043 1.00 23.89 ?  168 PHE   B HZ   1 
ATOM   6557 N  N    . LEU   B 1 169 ? 31.113 -37.830 -11.694 1.00 16.76 ?  169 LEU   B N    1 
ATOM   6558 C  CA   . LEU   B 1 169 ? 29.939 -38.144 -12.499 1.00 18.87 ?  169 LEU   B CA   1 
ATOM   6559 C  C    . LEU   B 1 169 ? 29.936 -39.581 -12.995 1.00 21.70 ?  169 LEU   B C    1 
ATOM   6560 O  O    . LEU   B 1 169 ? 29.038 -39.986 -13.733 1.00 24.17 ?  169 LEU   B O    1 
ATOM   6561 C  CB   . LEU   B 1 169 ? 29.856 -37.205 -13.701 1.00 20.70 ?  169 LEU   B CB   1 
ATOM   6562 C  CG   . LEU   B 1 169 ? 28.599 -36.339 -13.794 1.00 23.71 ?  169 LEU   B CG   1 
ATOM   6563 C  CD1  . LEU   B 1 169 ? 28.556 -35.654 -15.144 1.00 24.73 ?  169 LEU   B CD1  1 
ATOM   6564 C  CD2  . LEU   B 1 169 ? 27.333 -37.145 -13.559 1.00 23.78 ?  169 LEU   B CD2  1 
ATOM   6565 O  OXT  . LEU   B 1 169 ? 30.832 -40.354 -12.678 1.00 22.49 -1 169 LEU   B OXT  1 
ATOM   6566 H  H    . LEU   B 1 169 ? 31.821 -38.253 -11.946 1.00 20.08 ?  169 LEU   B H    1 
ATOM   6567 H  HA   . LEU   B 1 169 ? 29.152 -38.013 -11.956 1.00 22.62 ?  169 LEU   B HA   1 
ATOM   6568 H  HB2  . LEU   B 1 169 ? 30.616 -36.602 -13.678 1.00 24.81 ?  169 LEU   B HB2  1 
ATOM   6569 H  HB3  . LEU   B 1 169 ? 29.894 -37.735 -14.514 1.00 24.81 ?  169 LEU   B HB3  1 
ATOM   6570 H  HG   . LEU   B 1 169 ? 28.643 -35.647 -13.115 1.00 28.42 ?  169 LEU   B HG   1 
ATOM   6571 H  HD11 . LEU   B 1 169 ? 27.771 -35.086 -15.182 1.00 29.65 ?  169 LEU   B HD11 1 
ATOM   6572 H  HD12 . LEU   B 1 169 ? 29.357 -35.121 -15.251 1.00 29.65 ?  169 LEU   B HD12 1 
ATOM   6573 H  HD13 . LEU   B 1 169 ? 28.510 -36.331 -15.836 1.00 29.65 ?  169 LEU   B HD13 1 
ATOM   6574 H  HD21 . LEU   B 1 169 ? 26.584 -36.693 -13.974 1.00 28.50 ?  169 LEU   B HD21 1 
ATOM   6575 H  HD22 . LEU   B 1 169 ? 27.446 -38.028 -13.951 1.00 28.50 ?  169 LEU   B HD22 1 
ATOM   6576 H  HD23 . LEU   B 1 169 ? 27.186 -37.227 -12.605 1.00 28.50 ?  169 LEU   B HD23 1 
HETATM 6577 C  C1   T TFA   C 2 .   ? 12.125 -1.294  1.456   0.30 10.28 ?  201 TFA   A C1   1 
HETATM 6578 C  C2   T TFA   C 2 .   ? 12.741 -1.735  0.106   0.30 12.82 ?  201 TFA   A C2   1 
HETATM 6579 O  O    T TFA   C 2 .   ? 12.839 -1.560  2.429   0.30 8.85  ?  201 TFA   A O    1 
HETATM 6580 F  F1   T TFA   C 2 .   ? 12.780 -3.079  0.057   0.30 14.40 ?  201 TFA   A F1   1 
HETATM 6581 F  F2   T TFA   C 2 .   ? 12.036 -1.341  -0.965  0.30 13.08 ?  201 TFA   A F2   1 
HETATM 6582 F  F3   T TFA   C 2 .   ? 13.980 -1.267  -0.080  0.30 14.31 ?  201 TFA   A F3   1 
HETATM 6583 O  OXT  T TFA   C 2 .   ? 11.026 -0.747  1.374   0.30 10.99 ?  201 TFA   A OXT  1 
HETATM 6584 N  N2   B A1BAI D 3 .   ? 14.614 -0.193  4.089   0.14 16.44 ?  202 A1BAI A N2   1 
HETATM 6585 C  C3   B A1BAI D 3 .   ? 13.876 -0.483  1.231   0.14 18.82 ?  202 A1BAI A C3   1 
HETATM 6586 C  C6   B A1BAI D 3 .   ? 15.301 2.100   5.268   0.14 15.10 ?  202 A1BAI A C6   1 
HETATM 6587 C  C9   B A1BAI D 3 .   ? 15.750 4.230   4.686   0.14 14.70 ?  202 A1BAI A C9   1 
HETATM 6588 C  C1   B A1BAI D 3 .   ? 16.121 -1.249  0.148   0.14 19.16 ?  202 A1BAI A C1   1 
HETATM 6589 C  C10  B A1BAI D 3 .   ? 12.326 -0.231  0.876   0.14 19.56 ?  202 A1BAI A C10  1 
HETATM 6590 C  C11  B A1BAI D 3 .   ? 11.580 0.348   2.093   0.14 19.72 ?  202 A1BAI A C11  1 
HETATM 6591 C  C2   B A1BAI D 3 .   ? 14.615 -0.993  -0.071  0.14 19.01 ?  202 A1BAI A C2   1 
HETATM 6592 C  C4   B A1BAI D 3 .   ? 14.788 0.898   3.244   0.14 16.59 ?  202 A1BAI A C4   1 
HETATM 6593 C  C5   B A1BAI D 3 .   ? 14.803 -0.053  5.447   0.14 15.90 ?  202 A1BAI A C5   1 
HETATM 6594 C  C7   B A1BAI D 3 .   ? 15.157 2.166   3.859   0.14 15.61 ?  202 A1BAI A C7   1 
HETATM 6595 C  C8   B A1BAI D 3 .   ? 15.452 3.538   3.523   0.14 15.27 ?  202 A1BAI A C8   1 
HETATM 6596 N  N1   B A1BAI D 3 .   ? 14.574 0.697   1.860   0.14 17.86 ?  202 A1BAI A N1   1 
HETATM 6597 N  N3   B A1BAI D 3 .   ? 15.144 1.050   6.132   0.14 15.38 ?  202 A1BAI A N3   1 
HETATM 6598 N  N4   B A1BAI D 3 .   ? 15.666 3.354   5.811   0.14 14.34 ?  202 A1BAI A N4   1 
HETATM 6599 O  O1   B A1BAI D 3 .   ? 11.756 -1.448  0.499   0.14 20.04 ?  202 A1BAI A O1   1 
HETATM 6600 H  H1   B A1BAI D 3 .   ? 13.903 -1.335  1.954   0.14 22.55 ?  202 A1BAI A H1   1 
HETATM 6601 H  H11  B A1BAI D 3 .   ? 16.025 5.215   5.018   0.14 17.61 ?  202 A1BAI A H11  1 
HETATM 6602 H  H5   B A1BAI D 3 .   ? 16.685 -1.460  -0.785  0.14 22.96 ?  202 A1BAI A H5   1 
HETATM 6603 H  H3   B A1BAI D 3 .   ? 16.304 -2.121  0.801   0.14 22.96 ?  202 A1BAI A H3   1 
HETATM 6604 H  H4   B A1BAI D 3 .   ? 16.642 -0.394  0.616   0.14 22.96 ?  202 A1BAI A H4   1 
HETATM 6605 H  H2   B A1BAI D 3 .   ? 12.250 0.493   0.029   0.14 23.44 ?  202 A1BAI A H2   1 
HETATM 6606 H  H14  B A1BAI D 3 .   ? 10.950 -0.403  2.595   0.14 23.63 ?  202 A1BAI A H14  1 
HETATM 6607 H  H13  B A1BAI D 3 .   ? 10.930 1.186   1.812   0.14 23.63 ?  202 A1BAI A H13  1 
HETATM 6608 H  H15  B A1BAI D 3 .   ? 12.245 0.735   2.872   0.14 23.63 ?  202 A1BAI A H15  1 
HETATM 6609 H  H6   B A1BAI D 3 .   ? 14.132 -1.926  -0.441  0.14 22.78 ?  202 A1BAI A H6   1 
HETATM 6610 H  H7   B A1BAI D 3 .   ? 14.483 -0.272  -0.901  0.14 22.78 ?  202 A1BAI A H7   1 
HETATM 6611 H  H9   B A1BAI D 3 .   ? 14.654 -0.962  6.093   0.14 19.05 ?  202 A1BAI A H9   1 
HETATM 6612 H  H10  B A1BAI D 3 .   ? 15.460 4.043   2.561   0.14 18.29 ?  202 A1BAI A H10  1 
HETATM 6613 H  H8   B A1BAI D 3 .   ? 14.905 1.394   1.174   0.14 21.41 ?  202 A1BAI A H8   1 
HETATM 6614 H  H12  B A1BAI D 3 .   ? 15.830 3.609   6.704   0.14 17.17 ?  202 A1BAI A H12  1 
HETATM 6615 H  H16  B A1BAI D 3 .   ? 10.817 -1.487  0.723   0.14 24.02 ?  202 A1BAI A H16  1 
HETATM 6616 O  O1   C A1BAJ E 4 .   ? 16.052 -1.502  0.586   0.14 19.36 ?  203 A1BAJ A O1   1 
HETATM 6617 C  C1   C A1BAJ E 4 .   ? 11.795 -1.889  0.417   0.14 19.54 ?  203 A1BAJ A C1   1 
HETATM 6618 C  C2   C A1BAJ E 4 .   ? 12.386 -0.503  0.767   0.14 19.24 ?  203 A1BAJ A C2   1 
HETATM 6619 C  C3   C A1BAJ E 4 .   ? 13.889 -0.575  1.284   0.14 18.73 ?  203 A1BAJ A C3   1 
HETATM 6620 C  C4   C A1BAJ E 4 .   ? 14.621 0.863   3.338   0.14 16.53 ?  203 A1BAJ A C4   1 
HETATM 6621 C  C5   C A1BAJ E 4 .   ? 14.791 -0.091  5.543   0.14 15.86 ?  203 A1BAJ A C5   1 
HETATM 6622 C  C6   C A1BAJ E 4 .   ? 15.318 2.048   5.323   0.14 15.17 ?  203 A1BAJ A C6   1 
HETATM 6623 C  C7   C A1BAJ E 4 .   ? 15.067 2.116   3.923   0.14 15.65 ?  203 A1BAJ A C7   1 
HETATM 6624 C  C8   C A1BAJ E 4 .   ? 15.362 3.483   3.553   0.14 15.48 ?  203 A1BAJ A C8   1 
HETATM 6625 C  C10  C A1BAJ E 4 .   ? 14.855 -1.003  0.059   0.14 19.11 ?  203 A1BAJ A C10  1 
HETATM 6626 C  C11  C A1BAJ E 4 .   ? 15.129 0.216   -0.859  0.14 19.24 ?  203 A1BAJ A C11  1 
HETATM 6627 C  C9   C A1BAJ E 4 .   ? 15.762 4.173   4.683   0.14 14.94 ?  203 A1BAJ A C9   1 
HETATM 6628 N  N1   C A1BAJ E 4 .   ? 14.308 0.693   1.965   0.14 17.74 ?  203 A1BAJ A N1   1 
HETATM 6629 N  N2   C A1BAJ E 4 .   ? 14.494 -0.224  4.196   0.14 16.33 ?  203 A1BAJ A N2   1 
HETATM 6630 N  N3   C A1BAJ E 4 .   ? 15.210 1.000   6.217   0.14 15.41 ?  203 A1BAJ A N3   1 
HETATM 6631 N  N4   C A1BAJ E 4 .   ? 15.747 3.302   5.815   0.14 14.52 ?  203 A1BAJ A N4   1 
HETATM 6632 H  H16  C A1BAJ E 4 .   ? 16.415 -2.213  0.039   0.14 23.21 ?  203 A1BAJ A H16  1 
HETATM 6633 H  H3   C A1BAJ E 4 .   ? 10.752 -1.820  0.073   0.14 23.42 ?  203 A1BAJ A H3   1 
HETATM 6634 H  H5   C A1BAJ E 4 .   ? 11.777 -2.596  1.273   0.14 23.42 ?  203 A1BAJ A H5   1 
HETATM 6635 H  H4   C A1BAJ E 4 .   ? 12.348 -2.415  -0.380  0.14 23.42 ?  203 A1BAJ A H4   1 
HETATM 6636 H  H6   C A1BAJ E 4 .   ? 11.747 -0.015  1.540   0.14 23.06 ?  203 A1BAJ A H6   1 
HETATM 6637 H  H7   C A1BAJ E 4 .   ? 12.300 0.168   -0.125  0.14 23.06 ?  203 A1BAJ A H7   1 
HETATM 6638 H  H1   C A1BAJ E 4 .   ? 13.915 -1.408  2.038   0.14 22.45 ?  203 A1BAJ A H1   1 
HETATM 6639 H  H9   C A1BAJ E 4 .   ? 14.671 -1.003  6.180   0.14 19.00 ?  203 A1BAJ A H9   1 
HETATM 6640 H  H10  C A1BAJ E 4 .   ? 15.310 3.989   2.584   0.14 18.54 ?  203 A1BAJ A H10  1 
HETATM 6641 H  H2   C A1BAJ E 4 .   ? 14.352 -1.805  -0.553  0.14 22.90 ?  203 A1BAJ A H2   1 
HETATM 6642 H  H15  C A1BAJ E 4 .   ? 15.538 1.089   -0.313  0.14 23.05 ?  203 A1BAJ A H15  1 
HETATM 6643 H  H14  C A1BAJ E 4 .   ? 14.218 0.586   -1.367  0.14 23.05 ?  203 A1BAJ A H14  1 
HETATM 6644 H  H13  C A1BAJ E 4 .   ? 15.859 -0.019  -1.651  0.14 23.05 ?  203 A1BAJ A H13  1 
HETATM 6645 H  H11  C A1BAJ E 4 .   ? 16.083 5.157   4.986   0.14 17.90 ?  203 A1BAJ A H11  1 
HETATM 6646 H  H8   C A1BAJ E 4 .   ? 14.359 1.498   1.317   0.14 21.26 ?  203 A1BAJ A H8   1 
HETATM 6647 H  H12  C A1BAJ E 4 .   ? 15.985 3.558   6.689   0.14 17.39 ?  203 A1BAJ A H12  1 
HETATM 6648 CL CL   B CL    F 5 .   ? 15.983 2.676   -1.145  0.28 20.57 ?  204 CL    A CL   1 
HETATM 6649 O  O    . HOH   G 6 .   ? 4.747  3.762   0.582   1.00 24.17 ?  301 HOH   A O    1 
HETATM 6650 O  O    . HOH   G 6 .   ? 8.863  -12.036 17.114  1.00 45.41 ?  302 HOH   A O    1 
HETATM 6651 O  O    . HOH   G 6 .   ? 17.094 -17.966 15.019  1.00 26.16 ?  303 HOH   A O    1 
HETATM 6652 O  O    . HOH   G 6 .   ? 14.758 -4.600  20.524  1.00 43.35 ?  304 HOH   A O    1 
HETATM 6653 O  O    B HOH   G 6 .   ? 0.852  -9.515  4.550   0.28 21.07 ?  305 HOH   A O    1 
HETATM 6654 O  O    . HOH   G 6 .   ? 6.809  -8.000  11.786  1.00 18.87 ?  306 HOH   A O    1 
HETATM 6655 O  O    . HOH   G 6 .   ? 34.316 -1.839  12.462  1.00 36.58 ?  307 HOH   A O    1 
HETATM 6656 O  O    . HOH   G 6 .   ? 18.566 -2.409  -16.427 1.00 45.67 ?  308 HOH   A O    1 
HETATM 6657 O  O    . HOH   G 6 .   ? 11.966 0.355   14.734  1.00 33.87 ?  309 HOH   A O    1 
HETATM 6658 O  O    . HOH   G 6 .   ? 7.589  -6.182  -6.672  1.00 41.57 ?  310 HOH   A O    1 
HETATM 6659 O  O    . HOH   G 6 .   ? 15.075 -12.205 18.613  1.00 38.86 ?  311 HOH   A O    1 
HETATM 6660 O  O    . HOH   G 6 .   ? 22.697 12.483  1.623   1.00 14.86 ?  312 HOH   A O    1 
HETATM 6661 O  O    B HOH   G 6 .   ? 13.488 -1.100  -6.669  0.28 28.44 ?  313 HOH   A O    1 
HETATM 6662 O  O    . HOH   G 6 .   ? 28.894 0.499   -9.725  1.00 21.15 ?  314 HOH   A O    1 
HETATM 6663 O  O    . HOH   G 6 .   ? 42.446 10.550  5.203   1.00 20.86 ?  315 HOH   A O    1 
HETATM 6664 O  O    . HOH   G 6 .   ? 11.694 -10.863 -10.125 1.00 45.13 ?  316 HOH   A O    1 
HETATM 6665 O  O    . HOH   G 6 .   ? 14.674 -13.926 16.687  1.00 24.86 ?  317 HOH   A O    1 
HETATM 6666 O  O    . HOH   G 6 .   ? 28.127 -6.281  19.629  1.00 41.19 ?  318 HOH   A O    1 
HETATM 6667 O  O    . HOH   G 6 .   ? 18.652 -19.332 13.543  1.00 34.12 ?  319 HOH   A O    1 
HETATM 6668 O  O    . HOH   G 6 .   ? 36.114 -5.062  -0.532  1.00 30.50 ?  320 HOH   A O    1 
HETATM 6669 O  O    . HOH   G 6 .   ? 0.700  -4.374  0.089   1.00 32.23 ?  321 HOH   A O    1 
HETATM 6670 O  O    . HOH   G 6 .   ? 30.209 -13.326 -8.549  1.00 20.71 ?  322 HOH   A O    1 
HETATM 6671 O  O    . HOH   G 6 .   ? 13.938 -4.924  17.422  1.00 26.77 ?  323 HOH   A O    1 
HETATM 6672 O  O    . HOH   G 6 .   ? -0.600 -8.404  2.059   1.00 45.25 ?  324 HOH   A O    1 
HETATM 6673 O  O    . HOH   G 6 .   ? 11.645 -10.704 17.031  1.00 25.20 ?  325 HOH   A O    1 
HETATM 6674 O  O    . HOH   G 6 .   ? 21.256 -2.283  -2.354  1.00 16.04 ?  326 HOH   A O    1 
HETATM 6675 O  O    . HOH   G 6 .   ? -1.338 -4.436  7.520   1.00 51.55 ?  327 HOH   A O    1 
HETATM 6676 O  O    . HOH   G 6 .   ? 15.037 4.017   17.668  1.00 40.62 ?  328 HOH   A O    1 
HETATM 6677 O  O    A HOH   G 6 .   ? 14.617 -3.641  3.076   0.72 13.86 ?  329 HOH   A O    1 
HETATM 6678 O  O    . HOH   G 6 .   ? 19.871 -12.543 -8.857  1.00 25.54 ?  330 HOH   A O    1 
HETATM 6679 O  O    . HOH   G 6 .   ? 20.652 -19.721 -5.045  1.00 27.71 ?  331 HOH   A O    1 
HETATM 6680 O  O    . HOH   G 6 .   ? 27.897 0.833   -7.131  1.00 14.25 ?  332 HOH   A O    1 
HETATM 6681 O  O    . HOH   G 6 .   ? 14.442 -24.687 11.620  1.00 36.99 ?  333 HOH   A O    1 
HETATM 6682 O  O    . HOH   G 6 .   ? 37.499 2.799   10.194  1.00 29.15 ?  334 HOH   A O    1 
HETATM 6683 O  O    . HOH   G 6 .   ? 26.460 -19.342 -1.781  1.00 14.36 ?  335 HOH   A O    1 
HETATM 6684 O  O    . HOH   G 6 .   ? 22.326 5.430   18.936  1.00 39.07 ?  336 HOH   A O    1 
HETATM 6685 O  O    A HOH   G 6 .   ? 13.292 -1.424  -6.546  0.72 15.17 ?  337 HOH   A O    1 
HETATM 6686 O  O    . HOH   G 6 .   ? 14.079 -4.589  -11.903 1.00 33.48 ?  338 HOH   A O    1 
HETATM 6687 O  O    . HOH   G 6 .   ? 31.021 -18.118 7.781   1.00 20.22 ?  339 HOH   A O    1 
HETATM 6688 O  O    . HOH   G 6 .   ? 33.987 -1.026  -8.947  1.00 26.91 ?  340 HOH   A O    1 
HETATM 6689 O  O    . HOH   G 6 .   ? 28.337 -0.141  -13.398 1.00 32.05 ?  341 HOH   A O    1 
HETATM 6690 O  O    . HOH   G 6 .   ? -0.420 -2.849  2.923   1.00 36.85 ?  342 HOH   A O    1 
HETATM 6691 O  O    A HOH   G 6 .   ? 3.581  -9.448  9.709   0.72 24.09 ?  343 HOH   A O    1 
HETATM 6692 O  O    . HOH   G 6 .   ? 9.137  -10.146 19.434  1.00 36.43 ?  344 HOH   A O    1 
HETATM 6693 O  O    . HOH   G 6 .   ? 38.247 10.109  7.164   1.00 33.13 ?  345 HOH   A O    1 
HETATM 6694 O  O    . HOH   G 6 .   ? 7.907  -12.569 -0.868  1.00 21.47 ?  346 HOH   A O    1 
HETATM 6695 O  O    . HOH   G 6 .   ? 27.306 13.791  2.836   1.00 28.78 ?  347 HOH   A O    1 
HETATM 6696 O  O    . HOH   G 6 .   ? 44.300 7.098   6.399   1.00 26.84 ?  348 HOH   A O    1 
HETATM 6697 O  O    . HOH   G 6 .   ? 30.959 6.212   -12.304 1.00 29.33 ?  349 HOH   A O    1 
HETATM 6698 O  O    . HOH   G 6 .   ? 13.531 -15.216 -7.471  1.00 26.54 ?  350 HOH   A O    1 
HETATM 6699 O  O    . HOH   G 6 .   ? 39.734 -1.023  -5.185  1.00 20.14 ?  351 HOH   A O    1 
HETATM 6700 O  O    . HOH   G 6 .   ? 38.548 4.986   6.941   1.00 15.85 ?  352 HOH   A O    1 
HETATM 6701 O  O    . HOH   G 6 .   ? 9.846  -21.384 5.678   1.00 19.30 ?  353 HOH   A O    1 
HETATM 6702 O  O    A HOH   G 6 .   ? 14.257 0.587   6.777   0.72 18.08 ?  354 HOH   A O    1 
HETATM 6703 O  O    . HOH   G 6 .   ? 26.814 11.401  1.654   1.00 16.68 ?  355 HOH   A O    1 
HETATM 6704 O  O    . HOH   G 6 .   ? 31.677 8.219   14.817  1.00 24.13 ?  356 HOH   A O    1 
HETATM 6705 O  O    . HOH   G 6 .   ? 24.014 -2.102  -2.087  1.00 10.78 ?  357 HOH   A O    1 
HETATM 6706 O  O    . HOH   G 6 .   ? 18.899 -21.989 6.996   1.00 32.86 ?  358 HOH   A O    1 
HETATM 6707 O  O    . HOH   G 6 .   ? 14.331 -21.186 -4.250  1.00 29.48 ?  359 HOH   A O    1 
HETATM 6708 O  O    . HOH   G 6 .   ? 18.860 -0.732  -1.652  1.00 14.30 ?  360 HOH   A O    1 
HETATM 6709 O  O    A HOH   G 6 .   ? 17.478 -1.701  0.420   0.72 17.89 ?  361 HOH   A O    1 
HETATM 6710 O  O    . HOH   G 6 .   ? 42.528 4.260   5.324   1.00 30.21 ?  362 HOH   A O    1 
HETATM 6711 O  O    . HOH   G 6 .   ? 17.121 -17.744 -5.024  1.00 26.81 ?  363 HOH   A O    1 
HETATM 6712 O  O    . HOH   G 6 .   ? 22.147 -19.273 11.394  1.00 34.10 ?  364 HOH   A O    1 
HETATM 6713 O  O    . HOH   G 6 .   ? 30.785 3.104   8.261   1.00 11.99 ?  365 HOH   A O    1 
HETATM 6714 O  O    . HOH   G 6 .   ? 33.643 -7.143  4.279   1.00 16.71 ?  366 HOH   A O    1 
HETATM 6715 O  O    B HOH   G 6 .   ? 10.919 2.498   11.867  0.28 24.40 ?  367 HOH   A O    1 
HETATM 6716 O  O    . HOH   G 6 .   ? 35.765 -12.652 6.839   1.00 15.82 ?  368 HOH   A O    1 
HETATM 6717 O  O    . HOH   G 6 .   ? 31.821 -9.339  -6.660  1.00 22.30 ?  369 HOH   A O    1 
HETATM 6718 O  O    A HOH   G 6 .   ? 8.170  -21.383 3.973   0.72 35.21 ?  370 HOH   A O    1 
HETATM 6719 O  O    . HOH   G 6 .   ? 24.370 3.572   -1.803  1.00 14.96 ?  371 HOH   A O    1 
HETATM 6720 O  O    . HOH   G 6 .   ? 31.063 -13.934 -2.475  1.00 14.08 ?  372 HOH   A O    1 
HETATM 6721 O  O    A HOH   G 6 .   ? 11.049 -0.367  1.911   0.42 19.02 ?  373 HOH   A O    1 
HETATM 6722 O  O    . HOH   G 6 .   ? 43.951 8.462   -3.076  1.00 26.03 ?  374 HOH   A O    1 
HETATM 6723 O  O    . HOH   G 6 .   ? 37.355 11.981  4.943   1.00 31.53 ?  375 HOH   A O    1 
HETATM 6724 O  O    . HOH   G 6 .   ? 37.234 -2.789  9.698   1.00 40.23 ?  376 HOH   A O    1 
HETATM 6725 O  O    . HOH   G 6 .   ? 6.398  -5.459  11.073  1.00 19.09 ?  377 HOH   A O    1 
HETATM 6726 O  O    . HOH   G 6 .   ? 21.846 -21.895 8.404   1.00 28.49 ?  378 HOH   A O    1 
HETATM 6727 O  O    . HOH   G 6 .   ? 24.556 1.975   -7.047  1.00 19.74 ?  379 HOH   A O    1 
HETATM 6728 O  O    . HOH   G 6 .   ? 18.550 9.446   9.012   1.00 21.54 ?  380 HOH   A O    1 
HETATM 6729 O  O    . HOH   G 6 .   ? 27.450 -10.605 14.033  1.00 17.86 ?  381 HOH   A O    1 
HETATM 6730 O  O    . HOH   G 6 .   ? 16.510 -22.046 0.955   1.00 28.53 ?  382 HOH   A O    1 
HETATM 6731 O  O    . HOH   G 6 .   ? 33.496 -16.964 8.066   1.00 19.50 ?  383 HOH   A O    1 
HETATM 6732 O  O    . HOH   G 6 .   ? 28.574 -10.616 -14.039 1.00 42.23 ?  384 HOH   A O    1 
HETATM 6733 O  O    . HOH   G 6 .   ? 16.984 -19.270 4.890   1.00 15.12 ?  385 HOH   A O    1 
HETATM 6734 O  O    . HOH   G 6 .   ? 25.683 -0.796  -7.352  1.00 15.26 ?  386 HOH   A O    1 
HETATM 6735 O  O    . HOH   G 6 .   ? 24.664 -17.488 12.710  1.00 25.03 ?  387 HOH   A O    1 
HETATM 6736 O  O    B HOH   G 6 .   ? 14.962 -2.947  3.423   0.28 19.61 ?  388 HOH   A O    1 
HETATM 6737 O  O    . HOH   G 6 .   ? 31.763 -7.303  -9.853  1.00 21.65 ?  389 HOH   A O    1 
HETATM 6738 O  O    . HOH   G 6 .   ? 21.201 10.311  14.985  1.00 36.04 ?  390 HOH   A O    1 
HETATM 6739 O  O    T HOH   G 6 .   ? 15.390 -0.408  2.364   0.30 11.56 ?  391 HOH   A O    1 
HETATM 6740 O  O    . HOH   G 6 .   ? 24.180 -7.739  14.408  1.00 17.21 ?  392 HOH   A O    1 
HETATM 6741 O  O    . HOH   G 6 .   ? 14.510 -0.550  -12.158 1.00 24.23 ?  393 HOH   A O    1 
HETATM 6742 O  O    . HOH   G 6 .   ? 21.301 3.047   -0.303  1.00 13.29 ?  394 HOH   A O    1 
HETATM 6743 O  O    . HOH   G 6 .   ? 15.499 11.811  7.912   1.00 38.12 ?  395 HOH   A O    1 
HETATM 6744 O  O    . HOH   G 6 .   ? 43.359 7.845   2.669   1.00 26.23 ?  396 HOH   A O    1 
HETATM 6745 O  O    . HOH   G 6 .   ? 15.115 -8.115  -9.697  1.00 23.31 ?  397 HOH   A O    1 
HETATM 6746 O  O    . HOH   G 6 .   ? 15.188 -21.526 14.237  1.00 18.23 ?  398 HOH   A O    1 
HETATM 6747 O  O    . HOH   G 6 .   ? 32.761 -9.238  5.952   1.00 20.45 ?  399 HOH   A O    1 
HETATM 6748 O  O    . HOH   G 6 .   ? 22.640 -11.900 21.811  1.00 44.96 ?  400 HOH   A O    1 
HETATM 6749 O  O    . HOH   G 6 .   ? 37.514 -2.022  5.764   1.00 26.99 ?  401 HOH   A O    1 
HETATM 6750 O  O    . HOH   G 6 .   ? 14.024 -23.042 7.441   1.00 18.45 ?  402 HOH   A O    1 
HETATM 6751 O  O    . HOH   G 6 .   ? 23.441 11.368  4.068   1.00 12.53 ?  403 HOH   A O    1 
HETATM 6752 O  O    . HOH   G 6 .   ? 30.021 -10.093 12.970  1.00 22.23 ?  404 HOH   A O    1 
HETATM 6753 O  O    . HOH   G 6 .   ? 27.366 -6.086  -14.002 1.00 37.03 ?  405 HOH   A O    1 
HETATM 6754 O  O    . HOH   G 6 .   ? 23.908 -15.719 -9.135  1.00 37.10 ?  406 HOH   A O    1 
HETATM 6755 O  O    . HOH   G 6 .   ? 6.659  -3.170  12.731  1.00 29.72 ?  407 HOH   A O    1 
HETATM 6756 O  O    A HOH   G 6 .   ? 15.782 -0.931  5.248   0.72 17.27 ?  408 HOH   A O    1 
HETATM 6757 O  O    . HOH   G 6 .   ? 30.692 1.896   16.679  1.00 20.75 ?  409 HOH   A O    1 
HETATM 6758 O  O    . HOH   G 6 .   ? 21.743 -13.801 -8.176  1.00 41.72 ?  410 HOH   A O    1 
HETATM 6759 O  O    B HOH   G 6 .   ? 12.173 6.851   9.988   0.28 27.12 ?  411 HOH   A O    1 
HETATM 6760 O  O    . HOH   G 6 .   ? 27.298 2.337   18.694  1.00 29.30 ?  412 HOH   A O    1 
HETATM 6761 O  O    . HOH   G 6 .   ? 40.860 -8.268  -6.738  1.00 36.49 ?  413 HOH   A O    1 
HETATM 6762 O  O    . HOH   G 6 .   ? 20.553 -20.021 2.759   1.00 18.58 ?  414 HOH   A O    1 
HETATM 6763 O  O    . HOH   G 6 .   ? 26.910 4.164   -0.680  1.00 12.50 ?  415 HOH   A O    1 
HETATM 6764 O  O    . HOH   G 6 .   ? 15.952 6.844   3.027   1.00 17.38 ?  416 HOH   A O    1 
HETATM 6765 O  O    . HOH   G 6 .   ? 23.907 -20.270 -1.340  1.00 16.56 ?  417 HOH   A O    1 
HETATM 6766 O  O    . HOH   G 6 .   ? 38.116 -1.350  -1.966  1.00 18.96 ?  418 HOH   A O    1 
HETATM 6767 O  O    . HOH   G 6 .   ? 15.860 2.101   24.699  1.00 45.75 ?  419 HOH   A O    1 
HETATM 6768 O  O    . HOH   G 6 .   ? 32.507 -10.648 3.184   1.00 31.28 ?  420 HOH   A O    1 
HETATM 6769 O  O    . HOH   G 6 .   ? 44.872 -0.669  3.022   1.00 41.11 ?  421 HOH   A O    1 
HETATM 6770 O  O    . HOH   G 6 .   ? 32.627 -4.331  -9.903  1.00 28.41 ?  422 HOH   A O    1 
HETATM 6771 O  O    . HOH   G 6 .   ? 30.308 -12.900 13.504  1.00 20.35 ?  423 HOH   A O    1 
HETATM 6772 O  O    . HOH   G 6 .   ? 16.156 16.621  8.658   1.00 32.68 ?  424 HOH   A O    1 
HETATM 6773 O  O    . HOH   G 6 .   ? 5.418  2.868   4.895   1.00 36.05 ?  425 HOH   A O    1 
HETATM 6774 O  O    . HOH   G 6 .   ? 41.585 1.544   4.965   1.00 36.88 ?  426 HOH   A O    1 
HETATM 6775 O  O    B HOH   G 6 .   ? 11.897 -1.749  -3.092  0.28 15.78 ?  427 HOH   A O    1 
HETATM 6776 O  O    . HOH   G 6 .   ? 10.346 -13.720 -1.685  1.00 16.83 ?  428 HOH   A O    1 
HETATM 6777 O  O    A HOH   G 6 .   ? 20.082 4.554   -7.568  0.72 16.74 ?  429 HOH   A O    1 
HETATM 6778 O  O    . HOH   G 6 .   ? 35.040 -5.213  -3.085  1.00 18.02 ?  430 HOH   A O    1 
HETATM 6779 O  O    A HOH   G 6 .   ? 24.075 3.970   -4.938  0.72 20.20 ?  431 HOH   A O    1 
HETATM 6780 O  O    . HOH   G 6 .   ? 36.716 -4.951  5.351   1.00 24.13 ?  432 HOH   A O    1 
HETATM 6781 O  O    A HOH   G 6 .   ? 11.017 1.567   12.728  0.72 21.98 ?  433 HOH   A O    1 
HETATM 6782 O  O    . HOH   G 6 .   ? 19.435 -11.084 24.074  1.00 66.36 ?  434 HOH   A O    1 
HETATM 6783 O  O    . HOH   G 6 .   ? 22.582 8.143   18.336  1.00 44.31 ?  435 HOH   A O    1 
HETATM 6784 O  O    . HOH   G 6 .   ? 16.144 -14.161 20.140  1.00 49.92 ?  436 HOH   A O    1 
HETATM 6785 O  O    . HOH   G 6 .   ? 23.538 -8.015  17.074  1.00 21.84 ?  437 HOH   A O    1 
HETATM 6786 O  O    . HOH   G 6 .   ? 27.090 -3.172  19.332  1.00 36.70 ?  438 HOH   A O    1 
HETATM 6787 O  O    . HOH   G 6 .   ? 23.318 -20.917 1.328   1.00 18.76 ?  439 HOH   A O    1 
HETATM 6788 O  O    . HOH   G 6 .   ? 23.155 7.518   -3.218  1.00 29.34 ?  440 HOH   A O    1 
HETATM 6789 O  O    . HOH   G 6 .   ? 37.710 -8.823  -3.420  1.00 24.32 ?  441 HOH   A O    1 
HETATM 6790 O  O    . HOH   G 6 .   ? 10.374 -22.196 -1.202  1.00 50.06 ?  442 HOH   A O    1 
HETATM 6791 O  O    . HOH   G 6 .   ? 18.475 4.903   -15.162 1.00 45.81 ?  443 HOH   A O    1 
HETATM 6792 O  O    . HOH   G 6 .   ? 18.824 1.945   -0.667  1.00 13.20 ?  444 HOH   A O    1 
HETATM 6793 O  O    . HOH   G 6 .   ? 9.438  -16.268 -1.955  1.00 39.82 ?  445 HOH   A O    1 
HETATM 6794 O  O    . HOH   G 6 .   ? 20.556 -17.735 24.765  1.00 50.80 ?  446 HOH   A O    1 
HETATM 6795 O  O    A HOH   G 6 .   ? 16.241 2.960   -1.463  0.72 15.93 ?  447 HOH   A O    1 
HETATM 6796 O  O    . HOH   G 6 .   ? 34.389 -8.088  -0.560  1.00 28.33 ?  448 HOH   A O    1 
HETATM 6797 O  O    . HOH   G 6 .   ? 21.260 -9.173  21.318  1.00 48.49 ?  449 HOH   A O    1 
HETATM 6798 O  O    A HOH   G 6 .   ? 14.010 -0.325  3.439   0.42 36.30 ?  450 HOH   A O    1 
HETATM 6799 O  O    . HOH   G 6 .   ? 30.575 14.774  2.772   1.00 18.99 ?  451 HOH   A O    1 
HETATM 6800 O  O    . HOH   G 6 .   ? 18.405 -16.007 16.349  1.00 37.30 ?  452 HOH   A O    1 
HETATM 6801 O  O    B HOH   G 6 .   ? 10.019 3.954   -0.787  0.28 27.49 ?  453 HOH   A O    1 
HETATM 6802 O  O    . HOH   G 6 .   ? 31.328 -12.798 0.004   1.00 20.13 ?  454 HOH   A O    1 
HETATM 6803 O  O    . HOH   G 6 .   ? 21.510 -14.658 17.944  1.00 53.33 ?  455 HOH   A O    1 
HETATM 6804 O  O    B HOH   G 6 .   ? 7.245  1.939   6.990   0.28 28.95 ?  456 HOH   A O    1 
HETATM 6805 O  O    . HOH   G 6 .   ? 27.719 7.026   -6.436  1.00 34.93 ?  457 HOH   A O    1 
HETATM 6806 O  O    . HOH   G 6 .   ? 29.784 -16.081 10.702  1.00 34.08 ?  458 HOH   A O    1 
HETATM 6807 O  O    C HOH   G 6 .   ? 11.432 2.346   1.970   0.14 20.40 ?  459 HOH   A O    1 
HETATM 6808 O  O    . HOH   G 6 .   ? 29.741 -1.984  -12.748 1.00 46.24 ?  460 HOH   A O    1 
HETATM 6809 O  O    . HOH   G 6 .   ? 32.489 -15.881 10.825  1.00 32.43 ?  461 HOH   A O    1 
HETATM 6810 O  O    B HOH   G 6 .   ? 11.319 0.576   -2.203  0.28 23.03 ?  462 HOH   A O    1 
HETATM 6811 O  O    . HOH   G 6 .   ? 25.400 8.222   -4.859  1.00 29.40 ?  463 HOH   A O    1 
HETATM 6812 O  O    B HOH   G 6 .   ? 12.804 2.525   -0.480  0.28 24.62 ?  464 HOH   A O    1 
HETATM 6813 O  O    . HOH   G 6 .   ? 23.112 -22.247 -3.458  1.00 35.86 ?  465 HOH   A O    1 
HETATM 6814 O  O    . HOH   G 6 .   ? 24.795 5.661   20.738  1.00 50.79 ?  466 HOH   A O    1 
HETATM 6815 O  O    . HOH   G 6 .   ? 19.850 -17.346 -5.056  1.00 24.99 ?  467 HOH   A O    1 
HETATM 6816 O  O    . HOH   G 6 .   ? 24.613 14.595  7.794   1.00 34.76 ?  468 HOH   A O    1 
HETATM 6817 O  O    . HOH   G 6 .   ? 26.885 11.631  -1.347  1.00 31.76 ?  469 HOH   A O    1 
HETATM 6818 O  O    . HOH   G 6 .   ? 12.004 -13.413 16.364  1.00 53.85 ?  470 HOH   A O    1 
HETATM 6819 O  O    . HOH   G 6 .   ? 15.732 -21.538 3.697   1.00 23.90 ?  471 HOH   A O    1 
HETATM 6820 O  O    . HOH   G 6 .   ? 18.758 10.881  11.296  1.00 32.40 ?  472 HOH   A O    1 
HETATM 6821 O  O    . HOH   G 6 .   ? 39.619 -6.993  -3.442  1.00 43.75 ?  473 HOH   A O    1 
HETATM 6822 O  O    . HOH   G 6 .   ? 27.520 -11.402 16.541  1.00 37.77 ?  474 HOH   A O    1 
HETATM 6823 O  O    A HOH   G 6 .   ? 21.948 5.278   -5.858  0.72 28.45 ?  475 HOH   A O    1 
HETATM 6824 O  O    . HOH   G 6 .   ? 12.295 1.615   17.297  1.00 39.50 ?  476 HOH   A O    1 
HETATM 6825 O  O    . HOH   G 6 .   ? 11.001 -15.065 -6.098  1.00 34.79 ?  477 HOH   A O    1 
HETATM 6826 O  O    . HOH   G 6 .   ? 23.453 13.725  5.490   1.00 18.98 ?  478 HOH   A O    1 
HETATM 6827 O  O    . HOH   G 6 .   ? 25.784 10.764  -3.736  1.00 25.70 ?  479 HOH   A O    1 
HETATM 6828 O  O    . HOH   G 6 .   ? 18.105 -16.207 -8.830  1.00 43.37 ?  480 HOH   A O    1 
HETATM 6829 O  O    . HOH   G 6 .   ? 13.915 -10.328 -10.889 1.00 32.54 ?  481 HOH   A O    1 
HETATM 6830 O  O    B HOH   G 6 .   ? 10.711 -1.514  -5.646  0.28 17.61 ?  482 HOH   A O    1 
HETATM 6831 O  O    . HOH   G 6 .   ? 28.840 9.026   17.437  1.00 38.07 ?  483 HOH   A O    1 
HETATM 6832 O  O    . HOH   G 6 .   ? 15.659 -17.136 -6.999  1.00 30.21 ?  484 HOH   A O    1 
HETATM 6833 O  O    . HOH   G 6 .   ? 16.829 -20.519 16.110  1.00 30.67 ?  485 HOH   A O    1 
HETATM 6834 O  O    . HOH   G 6 .   ? 17.358 -18.693 19.815  1.00 51.73 ?  486 HOH   A O    1 
HETATM 6835 O  O    . HOH   G 6 .   ? 35.221 7.439   12.244  1.00 42.51 ?  487 HOH   A O    1 
HETATM 6836 O  O    . HOH   G 6 .   ? 20.504 -16.075 -7.359  1.00 29.32 ?  488 HOH   A O    1 
HETATM 6837 O  O    . HOH   G 6 .   ? 40.895 -3.998  -0.355  1.00 37.43 ?  489 HOH   A O    1 
HETATM 6838 O  O    . HOH   G 6 .   ? 23.117 11.825  -4.067  1.00 19.47 ?  490 HOH   A O    1 
HETATM 6839 O  O    . HOH   G 6 .   ? 30.854 0.698   19.142  1.00 38.86 ?  491 HOH   A O    1 
HETATM 6840 O  O    . HOH   G 6 .   ? 41.706 9.282   -4.103  1.00 30.92 ?  492 HOH   A O    1 
HETATM 6841 O  O    . HOH   G 6 .   ? 44.519 10.466  -1.580  1.00 30.95 ?  493 HOH   A O    1 
HETATM 6842 O  O    . HOH   G 6 .   ? 23.238 -12.826 19.307  1.00 43.11 ?  494 HOH   A O    1 
HETATM 6843 O  O    . HOH   G 6 .   ? 31.430 -0.572  -10.557 1.00 29.83 ?  495 HOH   A O    1 
HETATM 6844 O  O    . HOH   G 6 .   ? 28.654 -7.932  -15.316 1.00 47.40 ?  496 HOH   A O    1 
HETATM 6845 O  O    . HOH   G 6 .   ? 28.591 -4.694  -12.276 1.00 36.89 ?  497 HOH   A O    1 
HETATM 6846 O  O    . HOH   G 6 .   ? 15.975 -6.820  -11.888 1.00 40.93 ?  498 HOH   A O    1 
HETATM 6847 O  O    . HOH   G 6 .   ? 39.142 2.416   7.514   1.00 32.61 ?  499 HOH   A O    1 
HETATM 6848 O  O    . HOH   G 6 .   ? 18.409 -23.207 1.883   1.00 42.89 ?  500 HOH   A O    1 
HETATM 6849 O  O    . HOH   G 6 .   ? 13.946 -25.243 8.893   1.00 33.14 ?  501 HOH   A O    1 
HETATM 6850 O  O    . HOH   G 6 .   ? 40.517 -0.269  -7.847  1.00 33.61 ?  502 HOH   A O    1 
HETATM 6851 O  O    . HOH   G 6 .   ? 20.021 -22.321 4.166   1.00 28.00 ?  503 HOH   A O    1 
HETATM 6852 O  O    . HOH   G 6 .   ? 16.162 -23.384 5.735   1.00 27.88 ?  504 HOH   A O    1 
HETATM 6853 O  O    . HOH   G 6 .   ? 30.682 5.840   -14.746 1.00 35.44 ?  505 HOH   A O    1 
HETATM 6854 O  O    . HOH   G 6 .   ? 8.105  -3.122  -5.815  1.00 48.70 ?  506 HOH   A O    1 
HETATM 6855 O  O    . HOH   G 6 .   ? 37.367 -6.632  7.542   1.00 26.70 ?  507 HOH   A O    1 
HETATM 6856 O  O    . HOH   G 6 .   ? 30.746 -5.814  -11.893 1.00 46.17 ?  508 HOH   A O    1 
HETATM 6857 O  O    . HOH   G 6 .   ? 23.090 -23.757 1.666   1.00 29.85 ?  509 HOH   A O    1 
HETATM 6858 O  O    . HOH   G 6 .   ? 39.540 0.024   6.588   1.00 29.15 ?  510 HOH   A O    1 
HETATM 6859 O  O    . HOH   G 6 .   ? 28.971 14.363  0.821   1.00 47.43 ?  511 HOH   A O    1 
HETATM 6860 O  O    . HOH   G 6 .   ? 38.009 13.935  6.745   1.00 43.58 ?  512 HOH   A O    1 
HETATM 6861 O  O    B HOH   G 6 .   ? 14.895 8.162   4.897   0.28 22.60 ?  513 HOH   A O    1 
HETATM 6862 O  O    . HOH   G 6 .   ? 22.009 -24.007 4.510   1.00 27.26 ?  514 HOH   A O    1 
HETATM 6863 O  O    . HOH   G 6 .   ? 36.459 -6.519  10.124  1.00 44.94 ?  515 HOH   A O    1 
HETATM 6864 O  O    T HOH   G 6 .   ? 11.905 -2.136  -3.676  0.30 11.61 ?  516 HOH   A O    1 
HETATM 6865 O  O    . HOH   G 6 .   ? 17.332 -6.568  -14.181 1.00 39.31 ?  517 HOH   A O    1 
HETATM 6866 O  O    A HOH   G 6 .   ? 14.833 8.665   4.865   0.72 44.94 ?  518 HOH   A O    1 
HETATM 6867 O  O    . HOH   G 6 .   ? 24.068 8.982   -7.282  1.00 34.88 ?  519 HOH   A O    1 
HETATM 6868 O  O    . HOH   G 6 .   ? 16.342 -21.087 18.734  1.00 39.28 ?  520 HOH   A O    1 
HETATM 6869 O  O    . HOH   G 6 .   ? 15.832 -12.238 27.457  1.00 44.60 ?  521 HOH   A O    1 
HETATM 6870 O  O    . HOH   G 6 .   ? 14.720 -22.759 19.828  1.00 34.72 ?  522 HOH   A O    1 
HETATM 6871 O  O    . HOH   H 6 .   ? 29.813 -22.424 5.503   1.00 21.12 ?  201 HOH   B O    1 
HETATM 6872 O  O    . HOH   H 6 .   ? 49.353 -22.664 -19.734 1.00 47.25 ?  202 HOH   B O    1 
HETATM 6873 O  O    . HOH   H 6 .   ? 48.142 -6.889  15.526  1.00 33.94 ?  203 HOH   B O    1 
HETATM 6874 O  O    . HOH   H 6 .   ? 41.833 -35.981 -17.225 1.00 30.26 ?  204 HOH   B O    1 
HETATM 6875 O  O    . HOH   H 6 .   ? 41.355 -7.807  5.492   1.00 39.11 ?  205 HOH   B O    1 
HETATM 6876 O  O    . HOH   H 6 .   ? 52.897 -13.437 -20.296 1.00 34.62 ?  206 HOH   B O    1 
HETATM 6877 O  O    . HOH   H 6 .   ? 59.160 -18.722 6.796   1.00 37.76 ?  207 HOH   B O    1 
HETATM 6878 O  O    . HOH   H 6 .   ? 27.733 -29.173 -1.829  1.00 37.35 ?  208 HOH   B O    1 
HETATM 6879 O  O    . HOH   H 6 .   ? 38.036 -39.452 -0.164  1.00 39.33 ?  209 HOH   B O    1 
HETATM 6880 O  O    . HOH   H 6 .   ? 50.248 -3.369  7.172   1.00 36.91 ?  210 HOH   B O    1 
HETATM 6881 O  O    . HOH   H 6 .   ? 57.706 -24.463 5.013   1.00 34.34 ?  211 HOH   B O    1 
HETATM 6882 O  O    . HOH   H 6 .   ? 30.211 -41.012 -8.117  1.00 17.00 ?  212 HOH   B O    1 
HETATM 6883 O  O    . HOH   H 6 .   ? 54.497 -9.367  -8.776  1.00 18.57 ?  213 HOH   B O    1 
HETATM 6884 O  O    . HOH   H 6 .   ? 47.363 -7.399  -3.914  1.00 39.06 ?  214 HOH   B O    1 
HETATM 6885 O  O    . HOH   H 6 .   ? 56.366 -19.712 7.206   1.00 31.85 ?  215 HOH   B O    1 
HETATM 6886 O  O    . HOH   H 6 .   ? 27.843 -41.844 -15.165 1.00 35.67 ?  216 HOH   B O    1 
HETATM 6887 O  O    . HOH   H 6 .   ? 58.228 -12.943 8.412   1.00 31.89 ?  217 HOH   B O    1 
HETATM 6888 O  O    . HOH   H 6 .   ? 57.164 -26.892 -7.690  1.00 42.74 ?  218 HOH   B O    1 
HETATM 6889 O  O    . HOH   H 6 .   ? 55.429 -16.544 -14.350 1.00 34.87 ?  219 HOH   B O    1 
HETATM 6890 O  O    . HOH   H 6 .   ? 50.766 -6.119  0.149   1.00 27.09 ?  220 HOH   B O    1 
HETATM 6891 O  O    . HOH   H 6 .   ? 44.421 -7.233  2.070   1.00 35.13 ?  221 HOH   B O    1 
HETATM 6892 O  O    . HOH   H 6 .   ? 56.671 -30.762 -7.735  1.00 30.29 ?  222 HOH   B O    1 
HETATM 6893 O  O    . HOH   H 6 .   ? 35.969 -43.268 -8.535  1.00 32.13 ?  223 HOH   B O    1 
HETATM 6894 O  O    . HOH   H 6 .   ? 37.077 -19.831 -18.096 1.00 37.79 ?  224 HOH   B O    1 
HETATM 6895 O  O    . HOH   H 6 .   ? 57.414 -16.264 -12.179 1.00 19.18 ?  225 HOH   B O    1 
HETATM 6896 O  O    . HOH   H 6 .   ? 29.887 -26.323 3.980   1.00 28.64 ?  226 HOH   B O    1 
HETATM 6897 O  O    . HOH   H 6 .   ? 41.513 -39.155 -14.883 1.00 23.20 ?  227 HOH   B O    1 
HETATM 6898 O  O    . HOH   H 6 .   ? 29.826 -34.219 -0.442  1.00 34.60 ?  228 HOH   B O    1 
HETATM 6899 O  O    . HOH   H 6 .   ? 34.536 -36.382 -7.184  1.00 18.40 ?  229 HOH   B O    1 
HETATM 6900 O  O    . HOH   H 6 .   ? 48.599 -36.465 -15.507 1.00 42.79 ?  230 HOH   B O    1 
HETATM 6901 O  O    . HOH   H 6 .   ? 39.311 -10.925 6.115   1.00 25.19 ?  231 HOH   B O    1 
HETATM 6902 O  O    . HOH   H 6 .   ? 51.672 -6.461  4.393   1.00 20.25 ?  232 HOH   B O    1 
HETATM 6903 O  O    . HOH   H 6 .   ? 30.849 -28.777 4.279   1.00 27.05 ?  233 HOH   B O    1 
HETATM 6904 O  O    . HOH   H 6 .   ? 25.441 -25.947 -1.313  1.00 32.43 ?  234 HOH   B O    1 
HETATM 6905 O  O    . HOH   H 6 .   ? 41.385 -9.640  13.070  1.00 22.73 ?  235 HOH   B O    1 
HETATM 6906 O  O    . HOH   H 6 .   ? 40.648 -16.033 14.116  1.00 24.92 ?  236 HOH   B O    1 
HETATM 6907 O  O    . HOH   H 6 .   ? 45.106 -35.010 6.844   1.00 39.30 ?  237 HOH   B O    1 
HETATM 6908 O  O    . HOH   H 6 .   ? 50.726 -12.966 -0.490  1.00 12.17 ?  238 HOH   B O    1 
HETATM 6909 O  O    . HOH   H 6 .   ? 28.400 -19.679 -13.131 1.00 24.37 ?  239 HOH   B O    1 
HETATM 6910 O  O    . HOH   H 6 .   ? 32.803 -43.798 -11.309 1.00 20.66 ?  240 HOH   B O    1 
HETATM 6911 O  O    . HOH   H 6 .   ? 43.182 -32.400 -17.034 1.00 23.76 ?  241 HOH   B O    1 
HETATM 6912 O  O    . HOH   H 6 .   ? 48.038 -24.504 -17.743 1.00 29.64 ?  242 HOH   B O    1 
HETATM 6913 O  O    . HOH   H 6 .   ? 57.596 -24.379 -3.813  1.00 21.63 ?  243 HOH   B O    1 
HETATM 6914 O  O    . HOH   H 6 .   ? 42.556 -25.366 2.648   1.00 15.44 ?  244 HOH   B O    1 
HETATM 6915 O  O    . HOH   H 6 .   ? 35.101 -7.987  -3.004  1.00 18.23 ?  245 HOH   B O    1 
HETATM 6916 O  O    . HOH   H 6 .   ? 44.515 -27.741 -0.721  1.00 22.74 ?  246 HOH   B O    1 
HETATM 6917 O  O    . HOH   H 6 .   ? 34.236 -18.473 11.402  1.00 25.48 ?  247 HOH   B O    1 
HETATM 6918 O  O    . HOH   H 6 .   ? 43.092 -43.256 -8.224  1.00 28.95 ?  248 HOH   B O    1 
HETATM 6919 O  O    . HOH   H 6 .   ? 42.629 -22.865 3.855   1.00 11.88 ?  249 HOH   B O    1 
HETATM 6920 O  O    . HOH   H 6 .   ? 46.435 -1.549  13.255  1.00 29.32 ?  250 HOH   B O    1 
HETATM 6921 O  O    . HOH   H 6 .   ? 34.897 -24.641 13.872  1.00 31.45 ?  251 HOH   B O    1 
HETATM 6922 O  O    . HOH   H 6 .   ? 39.468 -11.094 0.325   1.00 16.88 ?  252 HOH   B O    1 
HETATM 6923 O  O    . HOH   H 6 .   ? 44.929 -43.574 -10.479 1.00 27.91 ?  253 HOH   B O    1 
HETATM 6924 O  O    . HOH   H 6 .   ? 50.954 -39.948 -8.224  1.00 32.39 ?  254 HOH   B O    1 
HETATM 6925 O  O    . HOH   H 6 .   ? 40.307 -12.755 -11.504 1.00 15.28 ?  255 HOH   B O    1 
HETATM 6926 O  O    . HOH   H 6 .   ? 31.793 -17.904 -14.479 1.00 30.54 ?  256 HOH   B O    1 
HETATM 6927 O  O    . HOH   H 6 .   ? 56.130 -23.539 -14.722 1.00 26.26 ?  257 HOH   B O    1 
HETATM 6928 O  O    . HOH   H 6 .   ? 41.864 -23.505 9.282   1.00 17.59 ?  258 HOH   B O    1 
HETATM 6929 O  O    . HOH   H 6 .   ? 38.457 -11.064 -2.248  1.00 19.64 ?  259 HOH   B O    1 
HETATM 6930 O  O    . HOH   H 6 .   ? 51.559 -13.837 11.060  1.00 25.77 ?  260 HOH   B O    1 
HETATM 6931 O  O    . HOH   H 6 .   ? 58.183 -10.640 -4.096  1.00 20.96 ?  261 HOH   B O    1 
HETATM 6932 O  O    . HOH   H 6 .   ? 29.712 -25.225 -10.807 1.00 16.75 ?  262 HOH   B O    1 
HETATM 6933 O  O    . HOH   H 6 .   ? 47.988 -22.781 5.831   1.00 17.67 ?  263 HOH   B O    1 
HETATM 6934 O  O    . HOH   H 6 .   ? 27.133 -31.824 -9.961  1.00 20.30 ?  264 HOH   B O    1 
HETATM 6935 O  O    . HOH   H 6 .   ? 38.910 -11.959 12.318  1.00 34.96 ?  265 HOH   B O    1 
HETATM 6936 O  O    . HOH   H 6 .   ? 30.854 -15.733 2.665   1.00 13.92 ?  266 HOH   B O    1 
HETATM 6937 O  O    . HOH   H 6 .   ? 57.505 -9.232  1.433   1.00 20.25 ?  267 HOH   B O    1 
HETATM 6938 O  O    . HOH   H 6 .   ? 43.351 -15.783 -12.165 1.00 14.69 ?  268 HOH   B O    1 
HETATM 6939 O  O    . HOH   H 6 .   ? 28.486 -30.883 -14.741 1.00 30.03 ?  269 HOH   B O    1 
HETATM 6940 O  O    . HOH   H 6 .   ? 49.305 -28.693 -6.901  1.00 15.62 ?  270 HOH   B O    1 
HETATM 6941 O  O    . HOH   H 6 .   ? 34.476 -12.796 2.606   1.00 26.08 ?  271 HOH   B O    1 
HETATM 6942 O  O    . HOH   H 6 .   ? 30.535 -42.235 -10.604 1.00 30.79 ?  272 HOH   B O    1 
HETATM 6943 O  O    . HOH   H 6 .   ? 42.339 -9.916  9.361   1.00 21.23 ?  273 HOH   B O    1 
HETATM 6944 O  O    . HOH   H 6 .   ? 28.274 -34.356 -9.452  1.00 19.34 ?  274 HOH   B O    1 
HETATM 6945 O  O    . HOH   H 6 .   ? 56.964 -8.656  8.411   1.00 19.82 ?  275 HOH   B O    1 
HETATM 6946 O  O    . HOH   H 6 .   ? 34.941 -33.384 -19.147 1.00 31.41 ?  276 HOH   B O    1 
HETATM 6947 O  O    . HOH   H 6 .   ? 49.768 -0.481  10.212  1.00 30.24 ?  277 HOH   B O    1 
HETATM 6948 O  O    . HOH   H 6 .   ? 42.361 -34.727 3.775   1.00 26.50 ?  278 HOH   B O    1 
HETATM 6949 O  O    . HOH   H 6 .   ? 46.596 -31.277 -4.784  1.00 25.08 ?  279 HOH   B O    1 
HETATM 6950 O  O    . HOH   H 6 .   ? 27.960 -22.897 -7.993  1.00 17.89 ?  280 HOH   B O    1 
HETATM 6951 O  O    . HOH   H 6 .   ? 46.830 -29.580 9.845   1.00 32.25 ?  281 HOH   B O    1 
HETATM 6952 O  O    . HOH   H 6 .   ? 42.258 -10.029 -14.894 1.00 38.48 ?  282 HOH   B O    1 
HETATM 6953 O  O    . HOH   H 6 .   ? 48.411 -25.039 3.105   1.00 13.68 ?  283 HOH   B O    1 
HETATM 6954 O  O    . HOH   H 6 .   ? 49.972 -24.638 5.780   1.00 32.80 ?  284 HOH   B O    1 
HETATM 6955 O  O    . HOH   H 6 .   ? 27.578 -26.699 -15.622 1.00 32.70 ?  285 HOH   B O    1 
HETATM 6956 O  O    . HOH   H 6 .   ? 51.211 -37.598 -9.608  1.00 26.14 ?  286 HOH   B O    1 
HETATM 6957 O  O    . HOH   H 6 .   ? 41.137 -5.519  11.481  1.00 42.12 ?  287 HOH   B O    1 
HETATM 6958 O  O    . HOH   H 6 .   ? 57.121 -12.066 12.349  1.00 36.68 ?  288 HOH   B O    1 
HETATM 6959 O  O    . HOH   H 6 .   ? 33.505 -15.313 -13.936 1.00 20.95 ?  289 HOH   B O    1 
HETATM 6960 O  O    . HOH   H 6 .   ? 47.079 -33.969 -4.611  1.00 17.74 ?  290 HOH   B O    1 
HETATM 6961 O  O    . HOH   H 6 .   ? 52.527 -10.391 12.996  1.00 22.49 ?  291 HOH   B O    1 
HETATM 6962 O  O    . HOH   H 6 .   ? 48.703 -20.014 5.934   1.00 14.23 ?  292 HOH   B O    1 
HETATM 6963 O  O    . HOH   H 6 .   ? 43.535 -15.367 18.195  1.00 30.21 ?  293 HOH   B O    1 
HETATM 6964 O  O    . HOH   H 6 .   ? 59.771 -15.321 8.156   1.00 31.61 ?  294 HOH   B O    1 
HETATM 6965 O  O    . HOH   H 6 .   ? 36.815 -12.765 -1.490  1.00 26.12 ?  295 HOH   B O    1 
HETATM 6966 O  O    . HOH   H 6 .   ? 45.340 -33.382 -15.931 1.00 23.82 ?  296 HOH   B O    1 
HETATM 6967 O  O    . HOH   H 6 .   ? 37.341 -35.663 7.200   1.00 33.44 ?  297 HOH   B O    1 
HETATM 6968 O  O    . HOH   H 6 .   ? 42.865 -20.277 -20.790 1.00 33.16 ?  298 HOH   B O    1 
HETATM 6969 O  O    . HOH   H 6 .   ? 57.643 -22.096 3.089   1.00 28.68 ?  299 HOH   B O    1 
HETATM 6970 O  O    . HOH   H 6 .   ? 44.031 -29.351 -4.703  1.00 23.74 ?  300 HOH   B O    1 
HETATM 6971 O  O    . HOH   H 6 .   ? 45.919 -40.420 -3.621  1.00 29.10 ?  301 HOH   B O    1 
HETATM 6972 O  O    . HOH   H 6 .   ? 42.642 -12.313 -18.502 1.00 30.10 ?  302 HOH   B O    1 
HETATM 6973 O  O    . HOH   H 6 .   ? 40.240 -10.839 -9.546  1.00 17.17 ?  303 HOH   B O    1 
HETATM 6974 O  O    . HOH   H 6 .   ? 51.719 -5.974  -7.956  1.00 47.11 ?  304 HOH   B O    1 
HETATM 6975 O  O    . HOH   H 6 .   ? 44.618 -27.451 2.001   1.00 15.93 ?  305 HOH   B O    1 
HETATM 6976 O  O    . HOH   H 6 .   ? 35.054 -33.558 4.533   1.00 29.31 ?  306 HOH   B O    1 
HETATM 6977 O  O    . HOH   H 6 .   ? 37.501 -18.172 13.124  1.00 29.14 ?  307 HOH   B O    1 
HETATM 6978 O  O    . HOH   H 6 .   ? 52.605 -35.666 -8.569  1.00 28.79 ?  308 HOH   B O    1 
HETATM 6979 O  O    . HOH   H 6 .   ? 53.153 -16.071 -12.744 1.00 27.88 ?  309 HOH   B O    1 
HETATM 6980 O  O    . HOH   H 6 .   ? 52.527 -29.253 -13.030 1.00 25.26 ?  310 HOH   B O    1 
HETATM 6981 O  O    . HOH   H 6 .   ? 53.473 -30.203 4.486   1.00 19.18 ?  311 HOH   B O    1 
HETATM 6982 O  O    . HOH   H 6 .   ? 32.801 -34.591 -5.889  1.00 17.24 ?  312 HOH   B O    1 
HETATM 6983 O  O    . HOH   H 6 .   ? 51.354 -32.967 -10.744 1.00 38.79 ?  313 HOH   B O    1 
HETATM 6984 O  O    . HOH   H 6 .   ? 25.931 -21.482 -3.539  1.00 17.01 ?  314 HOH   B O    1 
HETATM 6985 O  O    . HOH   H 6 .   ? 59.957 -17.109 -10.462 1.00 33.37 ?  315 HOH   B O    1 
HETATM 6986 O  O    . HOH   H 6 .   ? 37.854 -10.233 -10.751 1.00 17.33 ?  316 HOH   B O    1 
HETATM 6987 O  O    . HOH   H 6 .   ? 62.723 -13.558 4.727   1.00 27.27 ?  317 HOH   B O    1 
HETATM 6988 O  O    . HOH   H 6 .   ? 43.200 -21.421 10.665  1.00 16.48 ?  318 HOH   B O    1 
HETATM 6989 O  O    . HOH   H 6 .   ? 37.142 -30.571 -21.015 1.00 31.85 ?  319 HOH   B O    1 
HETATM 6990 O  O    . HOH   H 6 .   ? 62.879 -20.131 -0.822  1.00 38.77 ?  320 HOH   B O    1 
HETATM 6991 O  O    . HOH   H 6 .   ? 53.609 -12.613 -22.221 1.00 32.88 ?  321 HOH   B O    1 
HETATM 6992 O  O    . HOH   H 6 .   ? 26.335 -21.041 -6.231  1.00 16.73 ?  322 HOH   B O    1 
HETATM 6993 O  O    . HOH   H 6 .   ? 41.696 -8.060  1.337   1.00 24.49 ?  323 HOH   B O    1 
HETATM 6994 O  O    . HOH   H 6 .   ? 38.339 -12.752 7.917   1.00 18.70 ?  324 HOH   B O    1 
HETATM 6995 O  O    . HOH   H 6 .   ? 44.599 -24.592 9.580   1.00 20.07 ?  325 HOH   B O    1 
HETATM 6996 O  O    . HOH   H 6 .   ? 48.067 -32.644 -16.619 1.00 42.97 ?  326 HOH   B O    1 
HETATM 6997 O  O    . HOH   H 6 .   ? 38.367 -9.374  -13.282 1.00 26.64 ?  327 HOH   B O    1 
HETATM 6998 O  O    . HOH   H 6 .   ? 41.210 -24.468 15.840  1.00 43.63 ?  328 HOH   B O    1 
HETATM 6999 O  O    . HOH   H 6 .   ? 44.176 -1.772  7.570   1.00 44.98 ?  329 HOH   B O    1 
HETATM 7000 O  O    . HOH   H 6 .   ? 36.704 -12.418 4.295   1.00 18.27 ?  330 HOH   B O    1 
HETATM 7001 O  O    . HOH   H 6 .   ? 27.879 -14.788 -9.445  1.00 35.36 ?  331 HOH   B O    1 
HETATM 7002 O  O    . HOH   H 6 .   ? 43.113 -34.655 0.102   1.00 20.49 ?  332 HOH   B O    1 
HETATM 7003 O  O    . HOH   H 6 .   ? 47.165 -24.499 8.178   1.00 25.82 ?  333 HOH   B O    1 
HETATM 7004 O  O    . HOH   H 6 .   ? 33.620 -31.212 11.054  1.00 33.93 ?  334 HOH   B O    1 
HETATM 7005 O  O    . HOH   H 6 .   ? 48.602 -11.948 -13.891 1.00 26.81 ?  335 HOH   B O    1 
HETATM 7006 O  O    . HOH   H 6 .   ? 36.992 -15.149 -16.519 1.00 40.37 ?  336 HOH   B O    1 
HETATM 7007 O  O    . HOH   H 6 .   ? 42.817 -43.485 -14.332 1.00 43.05 ?  337 HOH   B O    1 
HETATM 7008 O  O    . HOH   H 6 .   ? 47.462 -27.424 2.015   1.00 15.22 ?  338 HOH   B O    1 
HETATM 7009 O  O    . HOH   H 6 .   ? 45.720 -36.261 -16.107 1.00 34.09 ?  339 HOH   B O    1 
HETATM 7010 O  O    . HOH   H 6 .   ? 46.809 -19.890 12.251  1.00 30.26 ?  340 HOH   B O    1 
HETATM 7011 O  O    . HOH   H 6 .   ? 39.424 -23.569 -20.326 1.00 36.44 ?  341 HOH   B O    1 
HETATM 7012 O  O    . HOH   H 6 .   ? 37.087 -45.184 -9.785  1.00 37.54 ?  342 HOH   B O    1 
HETATM 7013 O  O    . HOH   H 6 .   ? 28.895 -42.934 -12.358 1.00 37.97 ?  343 HOH   B O    1 
HETATM 7014 O  O    . HOH   H 6 .   ? 38.425 -12.301 -16.292 1.00 41.05 ?  344 HOH   B O    1 
HETATM 7015 O  O    . HOH   H 6 .   ? 32.999 -14.686 1.045   1.00 19.60 ?  345 HOH   B O    1 
HETATM 7016 O  O    . HOH   H 6 .   ? 39.816 -44.292 -11.205 1.00 38.98 ?  346 HOH   B O    1 
HETATM 7017 O  O    . HOH   H 6 .   ? 33.697 -9.517  -8.829  1.00 32.08 ?  347 HOH   B O    1 
HETATM 7018 O  O    . HOH   H 6 .   ? 40.420 -43.485 -9.113  1.00 27.59 ?  348 HOH   B O    1 
HETATM 7019 O  O    . HOH   H 6 .   ? 27.733 -26.612 -0.602  1.00 29.78 ?  349 HOH   B O    1 
HETATM 7020 O  O    . HOH   H 6 .   ? 38.522 -22.275 15.045  1.00 38.49 ?  350 HOH   B O    1 
HETATM 7021 O  O    . HOH   H 6 .   ? 62.581 -20.134 -4.854  1.00 44.30 ?  351 HOH   B O    1 
HETATM 7022 O  O    . HOH   H 6 .   ? 34.583 -10.308 7.577   1.00 24.30 ?  352 HOH   B O    1 
HETATM 7023 O  O    . HOH   H 6 .   ? 55.648 -8.266  10.819  1.00 25.47 ?  353 HOH   B O    1 
HETATM 7024 O  O    . HOH   H 6 .   ? 44.165 -37.301 -17.766 1.00 33.38 ?  354 HOH   B O    1 
HETATM 7025 O  O    . HOH   H 6 .   ? 23.198 -23.651 6.843   1.00 34.58 ?  355 HOH   B O    1 
HETATM 7026 O  O    . HOH   H 6 .   ? 36.078 -8.547  -9.702  1.00 35.19 ?  356 HOH   B O    1 
HETATM 7027 O  O    . HOH   H 6 .   ? 56.593 -7.283  3.105   1.00 27.40 ?  357 HOH   B O    1 
HETATM 7028 O  O    . HOH   H 6 .   ? 43.203 -12.711 -21.218 1.00 39.92 ?  358 HOH   B O    1 
HETATM 7029 O  O    . HOH   H 6 .   ? 61.508 -19.886 1.643   1.00 35.55 ?  359 HOH   B O    1 
HETATM 7030 O  O    . HOH   H 6 .   ? 34.134 -7.728  11.405  1.00 39.80 ?  360 HOH   B O    1 
HETATM 7031 O  O    . HOH   H 6 .   ? 56.928 -21.554 -16.341 1.00 40.98 ?  361 HOH   B O    1 
HETATM 7032 O  O    . HOH   H 6 .   ? 27.141 -25.963 -11.395 1.00 33.72 ?  362 HOH   B O    1 
HETATM 7033 O  O    . HOH   H 6 .   ? 40.205 -8.862  9.861   1.00 36.28 ?  363 HOH   B O    1 
HETATM 7034 O  O    . HOH   H 6 .   ? 54.146 -5.714  3.017   1.00 35.40 ?  364 HOH   B O    1 
HETATM 7035 O  O    . HOH   H 6 .   ? 32.535 -23.645 14.076  1.00 39.28 ?  365 HOH   B O    1 
HETATM 7036 O  O    . HOH   H 6 .   ? 36.188 -8.715  8.958   1.00 37.30 ?  366 HOH   B O    1 
HETATM 7037 O  O    . HOH   H 6 .   ? 58.954 -10.421 9.175   1.00 38.86 ?  367 HOH   B O    1 
HETATM 7038 O  O    . HOH   H 6 .   ? 48.374 -26.504 8.814   1.00 40.73 ?  368 HOH   B O    1 
HETATM 7039 O  O    . HOH   H 6 .   ? 41.827 -10.061 -17.456 1.00 51.76 ?  369 HOH   B O    1 
HETATM 7040 O  O    . HOH   H 6 .   ? 40.030 -11.389 -13.981 1.00 31.56 ?  370 HOH   B O    1 
HETATM 7041 O  O    . HOH   H 6 .   ? 39.879 -6.980  7.888   1.00 39.39 ?  371 HOH   B O    1 
HETATM 7042 O  O    . HOH   H 6 .   ? 56.068 -7.803  -0.597  1.00 35.01 ?  372 HOH   B O    1 
HETATM 7043 O  O    . HOH   H 6 .   ? 52.062 -12.886 13.331  1.00 32.20 ?  373 HOH   B O    1 
HETATM 7044 O  O    . HOH   H 6 .   ? 63.048 -12.395 6.907   1.00 38.55 ?  374 HOH   B O    1 
HETATM 7045 O  O    . HOH   H 6 .   ? 38.016 -10.598 10.084  1.00 30.29 ?  375 HOH   B O    1 
HETATM 7046 O  O    . HOH   H 6 .   ? 44.048 -5.594  -3.572  1.00 41.42 ?  376 HOH   B O    1 
HETATM 7047 O  O    . HOH   H 6 .   ? 36.534 -22.812 13.282  1.00 25.29 ?  377 HOH   B O    1 
HETATM 7048 O  O    . HOH   H 6 .   ? 41.795 -6.672  -4.871  1.00 45.06 ?  378 HOH   B O    1 
HETATM 7049 O  O    . HOH   H 6 .   ? 42.611 -17.066 -23.175 1.00 45.74 ?  379 HOH   B O    1 
HETATM 7050 O  O    . HOH   H 6 .   ? 40.071 -7.589  3.259   1.00 36.06 ?  380 HOH   B O    1 
HETATM 7051 O  O    . HOH   H 6 .   ? 39.659 -14.017 15.676  1.00 49.97 ?  381 HOH   B O    1 
HETATM 7052 O  O    . HOH   H 6 .   ? 52.852 -29.881 7.175   1.00 23.97 ?  382 HOH   B O    1 
HETATM 7053 O  O    . HOH   H 6 .   ? 60.485 -22.244 2.786   1.00 48.33 ?  383 HOH   B O    1 
HETATM 7054 O  O    . HOH   H 6 .   ? 46.805 -5.378  2.897   1.00 40.14 ?  384 HOH   B O    1 
HETATM 7055 O  O    . HOH   H 6 .   ? 25.803 -18.903 -11.873 1.00 37.96 ?  385 HOH   B O    1 
HETATM 7056 O  O    . HOH   H 6 .   ? 35.407 -33.745 7.331   1.00 42.37 ?  386 HOH   B O    1 
HETATM 7057 O  O    . HOH   H 6 .   ? 40.930 -9.783  15.787  1.00 44.92 ?  387 HOH   B O    1 
HETATM 7058 O  O    . HOH   H 6 .   ? 23.902 -20.861 -7.673  1.00 28.38 ?  388 HOH   B O    1 
HETATM 7059 O  O    . HOH   H 6 .   ? 35.321 -20.338 13.298  1.00 31.74 ?  389 HOH   B O    1 
HETATM 7060 O  O    . HOH   H 6 .   ? 40.685 -6.620  -0.881  1.00 25.39 ?  390 HOH   B O    1 
HETATM 7061 O  O    . HOH   H 6 .   ? 44.018 -31.748 -3.803  1.00 34.28 ?  391 HOH   B O    1 
HETATM 7062 O  O    . HOH   H 6 .   ? 26.634 -27.971 -13.474 1.00 34.67 ?  392 HOH   B O    1 
HETATM 7063 O  O    . HOH   H 6 .   ? 27.907 -27.080 2.207   1.00 31.36 ?  393 HOH   B O    1 
HETATM 7064 O  O    . HOH   H 6 .   ? 24.607 -20.652 -10.467 1.00 36.83 ?  394 HOH   B O    1 
HETATM 7065 O  O    . HOH   H 6 .   ? 34.357 -33.478 9.585   1.00 34.56 ?  395 HOH   B O    1 
HETATM 7066 O  O    . HOH   H 6 .   ? 50.629 -30.769 8.676   1.00 28.86 ?  396 HOH   B O    1 
HETATM 7067 O  O    . HOH   H 6 .   ? 26.858 -30.677 -12.655 1.00 29.49 ?  397 HOH   B O    1 
HETATM 7068 O  O    . HOH   H 6 .   ? 57.673 -6.508  -2.362  1.00 35.46 ?  398 HOH   B O    1 
HETATM 7069 O  O    . HOH   H 6 .   ? 45.766 -20.213 15.162  1.00 52.64 ?  399 HOH   B O    1 
HETATM 7070 O  O    . HOH   H 6 .   ? 40.935 -11.821 -22.329 1.00 41.12 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.6419 0.6420 0.7016 0.0014  -0.0225 0.0779  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6380 0.6395 0.6737 -0.0044 -0.0175 0.0534  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6394 0.6396 0.6909 -0.0001 -0.0217 0.0771  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6356 0.6373 0.6671 -0.0053 -0.0177 0.0550  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6257 0.6289 0.6623 -0.0069 -0.0249 0.0788  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6239 0.6277 0.6486 -0.0097 -0.0223 0.0665  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6282 0.6310 0.6736 -0.0054 -0.0267 0.0814  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6268 0.6298 0.6586 -0.0089 -0.0232 0.0669  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6482 0.6461 0.7018 0.0036  -0.0174 0.0748  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6425 0.6430 0.6744 -0.0028 -0.0136 0.0467  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6512 0.6482 0.7031 0.0051  -0.0162 0.0738  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6448 0.6448 0.6755 -0.0020 -0.0122 0.0437  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6507 0.6481 0.7040 0.0049  -0.0155 0.0743  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6445 0.6447 0.6757 -0.0020 -0.0120 0.0440  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6068 0.6139 0.6142 -0.0154 -0.0252 0.0784  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5689 0.5828 0.5251 -0.0309 -0.0270 0.0871  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5216 0.5487 0.4716 -0.0457 -0.0188 0.0675  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5239 0.5509 0.4615 -0.0471 -0.0212 0.0712  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5752 0.5835 0.4851 -0.0319 -0.0372 0.1133  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5791 0.5823 0.4469 -0.0340 -0.0459 0.1387  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5823 0.5808 0.4290 -0.0348 -0.0503 0.1496  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5788 0.5815 0.4374 -0.0341 -0.0484 0.1499  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4707 0.5072 0.4267 -0.0604 -0.0084 0.0437  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4181 0.4643 0.3870 -0.0731 0.0049  0.0180  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3626 0.4121 0.3243 -0.0775 0.0189  -0.0014 5   SER   A C   
49   O  O   . SER   A 5   ? 0.3726 0.4256 0.3312 -0.0650 0.0171  -0.0130 5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4232 0.4752 0.4164 -0.0793 0.0097  0.0111  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4279 0.4822 0.4325 -0.0826 0.0160  0.0081  5   SER   A OG  
57   N  N   A PHE   A 6   ? 0.3181 0.3765 0.2748 -0.0999 0.0323  0.0017  6   PHE   A N   
58   N  N   B PHE   A 6   ? 0.3367 0.3798 0.2960 -0.0728 0.0224  -0.0047 6   PHE   A N   
59   C  CA  A PHE   A 6   ? 0.2768 0.3397 0.2244 -0.1153 0.0411  0.0142  6   PHE   A CA  
60   C  CA  B PHE   A 6   ? 0.3112 0.3460 0.2632 -0.0664 0.0250  -0.0040 6   PHE   A CA  
61   C  C   A PHE   A 6   ? 0.2681 0.3387 0.2179 -0.1224 0.0544  0.0136  6   PHE   A C   
62   C  C   B PHE   A 6   ? 0.3046 0.3343 0.2580 -0.0662 0.0301  -0.0060 6   PHE   A C   
63   O  O   A PHE   A 6   ? 0.2768 0.3464 0.2438 -0.1192 0.0539  0.0305  6   PHE   A O   
64   O  O   B PHE   A 6   ? 0.3064 0.3345 0.2442 -0.0674 0.0239  -0.0014 6   PHE   A O   
65   C  CB  A PHE   A 6   ? 0.2593 0.3091 0.1952 -0.1091 0.0310  0.0286  6   PHE   A CB  
66   C  CB  B PHE   A 6   ? 0.2964 0.3256 0.2429 -0.0568 0.0196  -0.0026 6   PHE   A CB  
67   C  CG  A PHE   A 6   ? 0.2465 0.2879 0.1812 -0.0963 0.0235  0.0408  6   PHE   A CG  
68   C  CG  B PHE   A 6   ? 0.2829 0.3084 0.2294 -0.0477 0.0149  0.0006  6   PHE   A CG  
69   C  CD1 A PHE   A 6   ? 0.2410 0.2791 0.1856 -0.0880 0.0167  0.0456  6   PHE   A CD1 
70   C  CD1 B PHE   A 6   ? 0.2772 0.3010 0.2256 -0.0432 0.0121  0.0030  6   PHE   A CD1 
71   C  CD2 A PHE   A 6   ? 0.2558 0.2847 0.2052 -0.0779 0.0211  0.0400  6   PHE   A CD2 
72   C  CD2 B PHE   A 6   ? 0.2801 0.3018 0.2302 -0.0407 0.0147  0.0009  6   PHE   A CD2 
73   C  CE1 A PHE   A 6   ? 0.2389 0.2759 0.2041 -0.0849 0.0199  0.0429  6   PHE   A CE1 
74   C  CE1 B PHE   A 6   ? 0.2737 0.2967 0.2278 -0.0407 0.0129  0.0033  6   PHE   A CE1 
75   C  CE2 A PHE   A 6   ? 0.2535 0.2814 0.2214 -0.0744 0.0201  0.0365  6   PHE   A CE2 
76   C  CE2 B PHE   A 6   ? 0.2767 0.2976 0.2313 -0.0387 0.0150  0.0007  6   PHE   A CE2 
77   C  CZ  A PHE   A 6   ? 0.2471 0.2749 0.2128 -0.0802 0.0130  0.0347  6   PHE   A CZ  
78   C  CZ  B PHE   A 6   ? 0.2740 0.2952 0.2280 -0.0395 0.0122  0.0007  6   PHE   A CZ  
97   N  N   A SER   A 7   ? 0.2543 0.3274 0.1890 -0.1240 0.0573  -0.0069 7   SER   A N   
98   N  N   B SER   A 7   ? 0.2965 0.3213 0.2675 -0.0636 0.0349  -0.0153 7   SER   A N   
99   C  CA  A SER   A 7   ? 0.2570 0.3258 0.1920 -0.1069 0.0523  -0.0197 7   SER   A CA  
100  C  CA  B SER   A 7   ? 0.2917 0.3113 0.2809 -0.0584 0.0315  -0.0253 7   SER   A CA  
101  C  C   A SER   A 7   ? 0.2426 0.2910 0.1554 -0.0990 0.0584  -0.0171 7   SER   A C   
102  C  C   B SER   A 7   ? 0.2820 0.2995 0.2659 -0.0542 0.0329  -0.0236 7   SER   A C   
103  O  O   A SER   A 7   ? 0.2568 0.2812 0.1592 -0.1009 0.0643  -0.0154 7   SER   A O   
104  O  O   B SER   A 7   ? 0.2854 0.3025 0.2646 -0.0513 0.0275  -0.0248 7   SER   A O   
105  C  CB  A SER   A 7   ? 0.2794 0.3539 0.2334 -0.0910 0.0475  -0.0196 7   SER   A CB  
106  C  CB  B SER   A 7   ? 0.2939 0.3127 0.3029 -0.0596 0.0257  -0.0328 7   SER   A CB  
107  O  OG  A SER   A 7   ? 0.2980 0.3709 0.2614 -0.0813 0.0415  -0.0198 7   SER   A OG  
108  O  OG  B SER   A 7   ? 0.2964 0.3165 0.3239 -0.0572 0.0177  -0.0387 7   SER   A OG  
119  N  N   A GLY   A 8   ? 0.2155 0.2661 0.1522 -0.0869 0.0465  -0.0219 8   GLY   A N   
120  N  N   B GLY   A 8   ? 0.2719 0.2888 0.2518 -0.0516 0.0357  -0.0210 8   GLY   A N   
121  C  CA  A GLY   A 8   ? 0.1978 0.2415 0.1657 -0.0611 0.0358  -0.0133 8   GLY   A CA  
122  C  CA  B GLY   A 8   ? 0.2604 0.2753 0.2366 -0.0475 0.0361  -0.0198 8   GLY   A CA  
123  C  C   A GLY   A 8   ? 0.1705 0.2170 0.1636 -0.0441 0.0316  -0.0044 8   GLY   A C   
124  C  C   B GLY   A 8   ? 0.2478 0.2625 0.2190 -0.0446 0.0396  -0.0181 8   GLY   A C   
125  O  O   A GLY   A 8   ? 0.1785 0.2196 0.1734 -0.0211 0.0277  -0.0261 8   GLY   A O   
126  O  O   B GLY   A 8   ? 0.2466 0.2622 0.2171 -0.0431 0.0459  -0.0210 8   GLY   A O   
133  N  N   A TYR   A 9   ? 0.1478 0.2091 0.1597 -0.0349 0.0292  0.0132  9   TYR   A N   
134  N  N   B TYR   A 9   ? 0.2345 0.2508 0.2065 -0.0399 0.0356  -0.0134 9   TYR   A N   
135  C  CA  A TYR   A 9   ? 0.1458 0.1913 0.1362 -0.0386 0.0241  0.0166  9   TYR   A CA  
136  C  CA  B TYR   A 9   ? 0.2228 0.2382 0.1998 -0.0334 0.0300  -0.0054 9   TYR   A CA  
137  C  C   A TYR   A 9   ? 0.1477 0.1745 0.1384 -0.0302 0.0326  0.0291  9   TYR   A C   
138  C  C   B TYR   A 9   ? 0.2170 0.2289 0.1982 -0.0302 0.0283  -0.0011 9   TYR   A C   
139  O  O   A TYR   A 9   ? 0.1702 0.1889 0.1567 -0.0247 0.0183  0.0220  9   TYR   A O   
140  O  O   B TYR   A 9   ? 0.2211 0.2332 0.2158 -0.0315 0.0288  0.0018  9   TYR   A O   
141  C  CB  A TYR   A 9   ? 0.1468 0.2057 0.1473 -0.0312 0.0200  0.0109  9   TYR   A CB  
142  C  CB  B TYR   A 9   ? 0.2139 0.2327 0.2009 -0.0326 0.0224  -0.0063 9   TYR   A CB  
143  C  CG  A TYR   A 9   ? 0.1434 0.2144 0.1627 -0.0229 0.0231  0.0018  9   TYR   A CG  
144  C  CG  B TYR   A 9   ? 0.2047 0.2262 0.1915 -0.0319 0.0211  -0.0030 9   TYR   A CG  
145  C  CD1 A TYR   A 9   ? 0.1490 0.2214 0.1798 -0.0395 0.0335  -0.0098 9   TYR   A CD1 
146  C  CD1 B TYR   A 9   ? 0.2036 0.2251 0.1959 -0.0359 0.0226  -0.0006 9   TYR   A CD1 
147  C  CD2 A TYR   A 9   ? 0.1385 0.2098 0.1684 -0.0156 0.0195  0.0173  9   TYR   A CD2 
148  C  CD2 B TYR   A 9   ? 0.2003 0.2214 0.1812 -0.0296 0.0164  -0.0015 9   TYR   A CD2 
149  C  CE1 A TYR   A 9   ? 0.1581 0.2253 0.2106 -0.0453 0.0455  -0.0104 9   TYR   A CE1 
150  C  CE1 B TYR   A 9   ? 0.2037 0.2233 0.1962 -0.0386 0.0236  -0.0010 9   TYR   A CE1 
151  C  CE2 A TYR   A 9   ? 0.1459 0.2196 0.1849 -0.0192 0.0274  0.0093  9   TYR   A CE2 
152  C  CE2 B TYR   A 9   ? 0.2005 0.2221 0.1810 -0.0299 0.0220  0.0005  9   TYR   A CE2 
153  C  CZ  A TYR   A 9   ? 0.1554 0.2281 0.2159 -0.0410 0.0551  -0.0023 9   TYR   A CZ  
154  C  CZ  B TYR   A 9   ? 0.2018 0.2232 0.1925 -0.0359 0.0319  0.0024  9   TYR   A CZ  
155  O  OH  A TYR   A 9   ? 0.1688 0.2396 0.2477 -0.0581 0.0600  -0.0064 9   TYR   A OH  
156  O  OH  B TYR   A 9   ? 0.2067 0.2267 0.2034 -0.0389 0.0415  0.0088  9   TYR   A OH  
175  N  N   A LEU   A 10  ? 0.1416 0.1601 0.1358 -0.0313 0.0127  0.0309  10  LEU   A N   
176  N  N   B LEU   A 10  ? 0.2117 0.2183 0.1907 -0.0268 0.0247  0.0034  10  LEU   A N   
177  C  CA  A LEU   A 10  ? 0.1346 0.1572 0.1375 -0.0306 0.0113  0.0331  10  LEU   A CA  
178  C  CA  B LEU   A 10  ? 0.2076 0.2127 0.1928 -0.0246 0.0190  0.0051  10  LEU   A CA  
179  C  C   A LEU   A 10  ? 0.1397 0.1558 0.1492 -0.0332 0.0006  0.0376  10  LEU   A C   
180  C  C   B LEU   A 10  ? 0.1969 0.1983 0.1682 -0.0275 0.0102  0.0079  10  LEU   A C   
181  O  O   A LEU   A 10  ? 0.1477 0.1476 0.1665 -0.0287 0.0225  0.0399  10  LEU   A O   
182  O  O   B LEU   A 10  ? 0.1967 0.1960 0.1653 -0.0306 0.0202  0.0105  10  LEU   A O   
183  C  CB  A LEU   A 10  ? 0.1448 0.1622 0.1743 -0.0303 -0.0055 0.0446  10  LEU   A CB  
184  C  CB  B LEU   A 10  ? 0.2112 0.2173 0.2152 -0.0249 0.0150  0.0083  10  LEU   A CB  
185  C  CG  A LEU   A 10  ? 0.1545 0.1732 0.2453 -0.0132 -0.0295 0.0530  10  LEU   A CG  
186  C  CG  B LEU   A 10  ? 0.2158 0.2238 0.2414 -0.0187 0.0106  0.0104  10  LEU   A CG  
187  C  CD1 A LEU   A 10  ? 0.1698 0.1887 0.2916 -0.0243 -0.0091 0.0563  10  LEU   A CD1 
188  C  CD1 B LEU   A 10  ? 0.2133 0.2299 0.2536 -0.0123 0.0096  0.0111  10  LEU   A CD1 
189  C  CD2 A LEU   A 10  ? 0.1822 0.1913 0.2681 -0.0022 -0.0222 0.0306  10  LEU   A CD2 
190  C  CD2 B LEU   A 10  ? 0.2182 0.2245 0.2572 -0.0227 0.0128  0.0148  10  LEU   A CD2 
213  N  N   A LYS   A 11  ? 0.1449 0.1605 0.1409 -0.0360 0.0022  0.0455  11  LYS   A N   
214  N  N   B LYS   A 11  ? 0.1892 0.1869 0.1600 -0.0305 -0.0027 0.0025  11  LYS   A N   
215  C  CA  A LYS   A 11  ? 0.1488 0.1573 0.1609 -0.0463 0.0046  0.0353  11  LYS   A CA  
216  C  CA  B LYS   A 11  ? 0.1800 0.1731 0.1648 -0.0340 -0.0022 0.0020  11  LYS   A CA  
217  C  C   A LYS   A 11  ? 0.1460 0.1575 0.1670 -0.0391 0.0160  0.0268  11  LYS   A C   
218  C  C   B LYS   A 11  ? 0.1670 0.1590 0.1630 -0.0367 0.0054  -0.0107 11  LYS   A C   
219  O  O   A LYS   A 11  ? 0.1575 0.1897 0.1990 -0.0624 0.0212  0.0010  11  LYS   A O   
220  O  O   B LYS   A 11  ? 0.1666 0.1526 0.1741 -0.0423 0.0145  -0.0299 11  LYS   A O   
221  C  CB  A LYS   A 11  ? 0.1650 0.1525 0.1525 -0.0447 0.0034  0.0281  11  LYS   A CB  
222  C  CB  B LYS   A 11  ? 0.1839 0.1683 0.1682 -0.0321 -0.0026 0.0043  11  LYS   A CB  
223  C  CG  A LYS   A 11  ? 0.1741 0.1540 0.1475 -0.0390 0.0058  0.0288  11  LYS   A CG  
224  C  CG  B LYS   A 11  ? 0.1836 0.1686 0.1631 -0.0298 -0.0098 0.0041  11  LYS   A CG  
225  C  CD  A LYS   A 11  ? 0.1829 0.1578 0.1581 -0.0346 0.0076  0.0349  11  LYS   A CD  
226  C  CD  B LYS   A 11  ? 0.1822 0.1696 0.1621 -0.0294 -0.0153 0.0106  11  LYS   A CD  
227  C  CE  A LYS   A 11  ? 0.1820 0.1529 0.1550 -0.0334 0.0050  0.0389  11  LYS   A CE  
228  C  CE  B LYS   A 11  ? 0.1859 0.1715 0.1654 -0.0234 -0.0119 0.0178  11  LYS   A CE  
229  N  NZ  A LYS   A 11  ? 0.1757 0.1473 0.1674 -0.0210 -0.0095 0.0297  11  LYS   A NZ  
230  N  NZ  B LYS   A 11  ? 0.1874 0.1756 0.1674 -0.0164 -0.0106 0.0246  11  LYS   A NZ  
257  N  N   A LEU   A 12  ? 0.1364 0.1424 0.1509 -0.0269 0.0107  0.0247  12  LEU   A N   
258  N  N   B LEU   A 12  ? 0.1549 0.1608 0.1655 -0.0211 0.0065  -0.0038 12  LEU   A N   
259  C  CA  A LEU   A 12  ? 0.1325 0.1515 0.1581 -0.0156 0.0024  0.0272  12  LEU   A CA  
260  C  CA  B LEU   A 12  ? 0.1473 0.1675 0.1602 -0.0137 0.0142  -0.0028 12  LEU   A CA  
261  C  C   A LEU   A 12  ? 0.1424 0.1431 0.1655 -0.0243 0.0041  0.0243  12  LEU   A C   
262  C  C   B LEU   A 12  ? 0.1466 0.1654 0.1515 -0.0136 0.0235  0.0066  12  LEU   A C   
263  O  O   A LEU   A 12  ? 0.1504 0.1476 0.1772 -0.0219 0.0052  0.0083  12  LEU   A O   
264  O  O   B LEU   A 12  ? 0.1475 0.1657 0.1536 -0.0132 0.0224  0.0118  12  LEU   A O   
265  C  CB  A LEU   A 12  ? 0.1452 0.1465 0.1637 -0.0109 0.0043  0.0276  12  LEU   A CB  
266  C  CB  B LEU   A 12  ? 0.1555 0.1751 0.1715 -0.0108 0.0182  -0.0060 12  LEU   A CB  
267  C  CG  A LEU   A 12  ? 0.1505 0.1571 0.1803 -0.0081 0.0199  0.0213  12  LEU   A CG  
268  C  CG  B LEU   A 12  ? 0.1573 0.1802 0.1930 -0.0041 0.0253  -0.0080 12  LEU   A CG  
269  C  CD1 A LEU   A 12  ? 0.1588 0.1569 0.1845 0.0094  0.0303  0.0354  12  LEU   A CD1 
270  C  CD1 B LEU   A 12  ? 0.1565 0.1856 0.2095 -0.0019 0.0356  -0.0082 12  LEU   A CD1 
271  C  CD2 A LEU   A 12  ? 0.1558 0.1659 0.1980 -0.0136 0.0176  0.0244  12  LEU   A CD2 
272  C  CD2 B LEU   A 12  ? 0.1575 0.1842 0.1992 -0.0023 0.0222  -0.0184 12  LEU   A CD2 
295  N  N   A THR   A 13  ? 0.1393 0.1346 0.1829 -0.0223 0.0080  0.0200  13  THR   A N   
296  N  N   B THR   A 13  ? 0.1447 0.1608 0.1492 -0.0099 0.0171  0.0077  13  THR   A N   
297  C  CA  A THR   A 13  ? 0.1439 0.1427 0.1954 -0.0167 0.0248  0.0209  13  THR   A CA  
298  C  CA  B THR   A 13  ? 0.1451 0.1639 0.1563 -0.0135 0.0152  0.0101  13  THR   A CA  
299  C  C   A THR   A 13  ? 0.1474 0.1403 0.2021 -0.0205 0.0168  0.0422  13  THR   A C   
300  C  C   B THR   A 13  ? 0.1496 0.1677 0.1630 -0.0208 0.0055  0.0138  13  THR   A C   
301  O  O   A THR   A 13  ? 0.1510 0.1486 0.2032 -0.0140 0.0237  0.0316  13  THR   A O   
302  O  O   B THR   A 13  ? 0.1509 0.1720 0.1573 -0.0260 -0.0017 0.0150  13  THR   A O   
303  C  CB  A THR   A 13  ? 0.1450 0.1583 0.2070 -0.0110 0.0222  0.0190  13  THR   A CB  
304  C  CB  B THR   A 13  ? 0.1402 0.1656 0.1552 -0.0112 0.0174  0.0160  13  THR   A CB  
305  O  OG1 A THR   A 13  ? 0.1480 0.1519 0.2196 -0.0181 0.0128  0.0305  13  THR   A OG1 
306  O  OG1 B THR   A 13  ? 0.1292 0.1622 0.1556 -0.0170 0.0323  0.0256  13  THR   A OG1 
307  C  CG2 A THR   A 13  ? 0.1563 0.1761 0.2201 -0.0086 0.0271  0.0144  13  THR   A CG2 
308  C  CG2 B THR   A 13  ? 0.1414 0.1720 0.1592 -0.0056 0.0142  0.0126  13  THR   A CG2 
323  N  N   A ASP   A 14  ? 0.1467 0.1470 0.2240 -0.0281 0.0091  0.0570  14  ASP   A N   
324  N  N   B ASP   A 14  ? 0.1518 0.1702 0.1906 -0.0222 -0.0036 0.0141  14  ASP   A N   
325  C  CA  A ASP   A 14  ? 0.1552 0.1616 0.2466 -0.0204 -0.0022 0.0702  14  ASP   A CA  
326  C  CA  B ASP   A 14  ? 0.1564 0.1764 0.2092 -0.0159 -0.0085 0.0235  14  ASP   A CA  
327  C  C   A ASP   A 14  ? 0.1500 0.1643 0.2114 -0.0255 -0.0057 0.0636  14  ASP   A C   
328  C  C   B ASP   A 14  ? 0.1515 0.1658 0.1913 -0.0143 -0.0108 0.0350  14  ASP   A C   
329  O  O   A ASP   A 14  ? 0.1608 0.1759 0.2299 -0.0312 -0.0160 0.0686  14  ASP   A O   
330  O  O   B ASP   A 14  ? 0.1536 0.1664 0.1890 -0.0055 -0.0214 0.0321  14  ASP   A O   
331  C  CB  A ASP   A 14  ? 0.1671 0.1886 0.3142 -0.0324 0.0036  0.0849  14  ASP   A CB  
332  C  CB  B ASP   A 14  ? 0.1635 0.1955 0.2503 -0.0190 -0.0096 0.0260  14  ASP   A CB  
333  C  CG  A ASP   A 14  ? 0.1944 0.2379 0.4012 -0.0324 0.0097  0.0801  14  ASP   A CG  
334  C  CG  B ASP   A 14  ? 0.1654 0.2153 0.2828 -0.0271 -0.0131 0.0292  14  ASP   A CG  
335  O  OD1 A ASP   A 14  ? 0.2129 0.2594 0.4316 -0.0119 -0.0082 0.0752  14  ASP   A OD1 
336  O  OD1 B ASP   A 14  ? 0.1659 0.2206 0.2922 -0.0280 -0.0119 0.0321  14  ASP   A OD1 
337  O  OD2 A ASP   A 14  ? 0.2201 0.2690 0.4487 -0.0406 0.0046  0.0629  14  ASP   A OD2 
338  O  OD2 B ASP   A 14  ? 0.1671 0.2317 0.3018 -0.0330 -0.0251 0.0237  14  ASP   A OD2 
347  N  N   . ASN   A 15  ? 0.1469 0.1584 0.1945 -0.0257 0.0005  0.0520  15  ASN   A N   
348  C  CA  . ASN   A 15  ? 0.1466 0.1618 0.2107 -0.0206 -0.0044 0.0417  15  ASN   A CA  
349  C  C   . ASN   A 15  ? 0.1471 0.1578 0.2210 -0.0207 0.0060  0.0446  15  ASN   A C   
350  O  O   . ASN   A 15  ? 0.1524 0.1569 0.2732 -0.0259 -0.0193 0.0389  15  ASN   A O   
351  C  CB  . ASN   A 15  ? 0.1453 0.1574 0.2027 -0.0161 -0.0018 0.0416  15  ASN   A CB  
352  C  CG  . ASN   A 15  ? 0.1466 0.1665 0.2142 -0.0154 0.0070  0.0273  15  ASN   A CG  
353  O  OD1 . ASN   A 15  ? 0.1603 0.1718 0.2363 -0.0327 0.0000  0.0345  15  ASN   A OD1 
354  N  ND2 . ASN   A 15  ? 0.1539 0.1783 0.1961 -0.0219 0.0160  0.0237  15  ASN   A ND2 
362  N  N   A VAL   A 16  ? 0.1416 0.1529 0.2175 -0.0156 0.0083  0.0500  16  VAL   A N   
363  N  N   B VAL   A 16  ? 0.1504 0.1655 0.2044 -0.0133 0.0123  0.0420  16  VAL   A N   
364  C  CA  A VAL   A 16  ? 0.1366 0.1513 0.2052 -0.0112 0.0084  0.0448  16  VAL   A CA  
365  C  CA  B VAL   A 16  ? 0.1530 0.1709 0.1741 -0.0078 0.0213  0.0360  16  VAL   A CA  
366  C  C   A VAL   A 16  ? 0.1338 0.1511 0.1770 -0.0212 -0.0041 0.0405  16  VAL   A C   
367  C  C   B VAL   A 16  ? 0.1519 0.1762 0.1652 -0.0170 0.0203  0.0332  16  VAL   A C   
368  O  O   A VAL   A 16  ? 0.1319 0.1444 0.1648 -0.0256 0.0067  0.0281  16  VAL   A O   
369  O  O   B VAL   A 16  ? 0.1530 0.1805 0.1603 -0.0194 0.0264  0.0246  16  VAL   A O   
370  C  CB  A VAL   A 16  ? 0.1437 0.1671 0.2119 0.0041  0.0330  0.0504  16  VAL   A CB  
371  C  CB  B VAL   A 16  ? 0.1595 0.1771 0.1577 0.0047  0.0316  0.0325  16  VAL   A CB  
372  C  CG1 A VAL   A 16  ? 0.1553 0.1765 0.2302 0.0123  0.0373  0.0508  16  VAL   A CG1 
373  C  CG1 B VAL   A 16  ? 0.1647 0.1806 0.1632 0.0110  0.0309  0.0318  16  VAL   A CG1 
374  C  CG2 A VAL   A 16  ? 0.1518 0.1766 0.2173 0.0096  0.0523  0.0535  16  VAL   A CG2 
375  C  CG2 B VAL   A 16  ? 0.1636 0.1819 0.1651 0.0070  0.0360  0.0330  16  VAL   A CG2 
394  N  N   A TYR   A 17  ? 0.1364 0.1456 0.1934 -0.0174 0.0108  0.0441  17  TYR   A N   
395  N  N   B TYR   A 17  ? 0.1487 0.1714 0.1684 -0.0208 0.0142  0.0292  17  TYR   A N   
396  C  CA  A TYR   A 17  ? 0.1430 0.1472 0.1769 -0.0164 0.0113  0.0399  17  TYR   A CA  
397  C  CA  B TYR   A 17  ? 0.1463 0.1660 0.1587 -0.0259 0.0125  0.0252  17  TYR   A CA  
398  C  C   A TYR   A 17  ? 0.1466 0.1393 0.1841 -0.0156 0.0116  0.0322  17  TYR   A C   
399  C  C   B TYR   A 17  ? 0.1435 0.1637 0.1516 -0.0314 0.0160  0.0220  17  TYR   A C   
400  O  O   A TYR   A 17  ? 0.1396 0.1355 0.1934 -0.0163 0.0183  0.0366  17  TYR   A O   
401  O  O   B TYR   A 17  ? 0.1378 0.1640 0.1543 -0.0391 0.0159  0.0248  17  TYR   A O   
402  C  CB  A TYR   A 17  ? 0.1605 0.1516 0.1824 -0.0277 0.0027  0.0378  17  TYR   A CB  
403  C  CB  B TYR   A 17  ? 0.1564 0.1669 0.1697 -0.0197 0.0075  0.0240  17  TYR   A CB  
404  C  CG  A TYR   A 17  ? 0.1785 0.1662 0.1903 -0.0386 -0.0167 0.0374  17  TYR   A CG  
405  C  CG  B TYR   A 17  ? 0.1659 0.1712 0.1690 -0.0133 0.0050  0.0222  17  TYR   A CG  
406  C  CD1 A TYR   A 17  ? 0.1894 0.1759 0.2043 -0.0323 -0.0229 0.0372  17  TYR   A CD1 
407  C  CD1 B TYR   A 17  ? 0.1737 0.1727 0.1752 -0.0042 0.0031  0.0271  17  TYR   A CD1 
408  C  CD2 A TYR   A 17  ? 0.1875 0.1784 0.1796 -0.0509 -0.0208 0.0513  17  TYR   A CD2 
409  C  CD2 B TYR   A 17  ? 0.1693 0.1776 0.1689 -0.0132 0.0046  0.0212  17  TYR   A CD2 
410  C  CE1 A TYR   A 17  ? 0.1905 0.1752 0.2095 -0.0417 -0.0421 0.0346  17  TYR   A CE1 
411  C  CE1 B TYR   A 17  ? 0.1798 0.1775 0.1864 -0.0030 0.0027  0.0342  17  TYR   A CE1 
412  C  CE2 A TYR   A 17  ? 0.1943 0.1791 0.1949 -0.0540 -0.0364 0.0421  17  TYR   A CE2 
413  C  CE2 B TYR   A 17  ? 0.1760 0.1808 0.1787 -0.0080 0.0051  0.0239  17  TYR   A CE2 
414  C  CZ  A TYR   A 17  ? 0.1997 0.1735 0.2031 -0.0524 -0.0404 0.0435  17  TYR   A CZ  
415  C  CZ  B TYR   A 17  ? 0.1783 0.1830 0.1867 -0.0027 0.0013  0.0329  17  TYR   A CZ  
416  O  OH  A TYR   A 17  ? 0.2153 0.1756 0.2149 -0.0478 -0.0395 0.0413  17  TYR   A OH  
417  O  OH  B TYR   A 17  ? 0.1761 0.1894 0.2013 0.0012  0.0014  0.0387  17  TYR   A OH  
436  N  N   A ILE   A 18  ? 0.1473 0.1445 0.1707 -0.0167 0.0142  0.0385  18  ILE   A N   
437  N  N   B ILE   A 18  ? 0.1375 0.1593 0.1460 -0.0352 0.0183  0.0150  18  ILE   A N   
438  C  CA  A ILE   A 18  ? 0.1448 0.1446 0.1652 -0.0153 0.0168  0.0248  18  ILE   A CA  
439  C  CA  B ILE   A 18  ? 0.1299 0.1562 0.1366 -0.0289 0.0271  0.0034  18  ILE   A CA  
440  C  C   A ILE   A 18  ? 0.1496 0.1464 0.1578 -0.0252 0.0182  0.0270  18  ILE   A C   
441  C  C   B ILE   A 18  ? 0.1310 0.1668 0.1293 -0.0296 0.0170  -0.0009 18  ILE   A C   
442  O  O   A ILE   A 18  ? 0.1552 0.1619 0.1558 -0.0294 0.0212  0.0255  18  ILE   A O   
443  O  O   B ILE   A 18  ? 0.1292 0.1756 0.1441 -0.0319 0.0112  0.0007  18  ILE   A O   
444  C  CB  A ILE   A 18  ? 0.1575 0.1431 0.1453 0.0055  0.0229  0.0264  18  ILE   A CB  
445  C  CB  B ILE   A 18  ? 0.1301 0.1458 0.1266 -0.0209 0.0422  0.0014  18  ILE   A CB  
446  C  CG1 A ILE   A 18  ? 0.1629 0.1510 0.1446 0.0186  0.0117  0.0214  18  ILE   A CG1 
447  C  CG1 B ILE   A 18  ? 0.1412 0.1501 0.1413 -0.0246 0.0496  0.0063  18  ILE   A CG1 
448  C  CG2 A ILE   A 18  ? 0.1597 0.1440 0.1458 0.0022  0.0192  0.0175  18  ILE   A CG2 
449  C  CG2 B ILE   A 18  ? 0.1325 0.1480 0.1312 -0.0224 0.0396  -0.0042 18  ILE   A CG2 
450  C  CD1 A ILE   A 18  ? 0.1887 0.1615 0.1633 0.0288  0.0127  0.0215  18  ILE   A CD1 
451  C  CD1 B ILE   A 18  ? 0.1498 0.1600 0.1591 -0.0201 0.0562  -0.0064 18  ILE   A CD1 
474  N  N   A LYS   A 19  ? 0.1477 0.1526 0.1578 -0.0147 0.0294  0.0216  19  LYS   A N   
475  N  N   B LYS   A 19  ? 0.1379 0.1698 0.1224 -0.0240 0.0267  -0.0095 19  LYS   A N   
476  C  CA  A LYS   A 19  ? 0.1653 0.1632 0.1497 -0.0156 0.0328  0.0216  19  LYS   A CA  
477  C  CA  B LYS   A 19  ? 0.1570 0.1820 0.1402 -0.0151 0.0295  -0.0165 19  LYS   A CA  
478  C  C   A LYS   A 19  ? 0.1541 0.1486 0.1636 -0.0089 0.0335  0.0424  19  LYS   A C   
479  C  C   B LYS   A 19  ? 0.1685 0.1840 0.1529 -0.0072 0.0245  -0.0117 19  LYS   A C   
480  O  O   A LYS   A 19  ? 0.1507 0.1567 0.1776 -0.0024 0.0334  0.0449  19  LYS   A O   
481  O  O   B LYS   A 19  ? 0.1652 0.1817 0.1575 -0.0086 0.0210  -0.0038 19  LYS   A O   
482  C  CB  A LYS   A 19  ? 0.1813 0.1894 0.1633 -0.0199 0.0221  0.0100  19  LYS   A CB  
483  C  CB  B LYS   A 19  ? 0.1565 0.1912 0.1481 -0.0129 0.0387  -0.0258 19  LYS   A CB  
484  C  CG  A LYS   A 19  ? 0.2089 0.2035 0.1667 -0.0283 0.0148  -0.0052 19  LYS   A CG  
485  C  CG  B LYS   A 19  ? 0.1732 0.2028 0.1563 -0.0101 0.0361  -0.0205 19  LYS   A CG  
486  C  CD  A LYS   A 19  ? 0.2356 0.2308 0.1885 -0.0351 0.0055  -0.0101 19  LYS   A CD  
487  C  CD  B LYS   A 19  ? 0.1893 0.2131 0.1599 -0.0140 0.0301  -0.0134 19  LYS   A CD  
488  C  CE  A LYS   A 19  ? 0.2595 0.2444 0.2007 -0.0443 0.0087  -0.0062 19  LYS   A CE  
489  C  CE  B LYS   A 19  ? 0.1978 0.2204 0.1663 -0.0174 0.0207  -0.0123 19  LYS   A CE  
490  N  NZ  A LYS   A 19  ? 0.2717 0.2547 0.2037 -0.0500 0.0149  -0.0105 19  LYS   A NZ  
491  N  NZ  B LYS   A 19  ? 0.2036 0.2239 0.1699 -0.0218 0.0194  -0.0143 19  LYS   A NZ  
518  N  N   A ASN   A 20  ? 0.1566 0.1555 0.1902 -0.0123 0.0317  0.0470  20  ASN   A N   
519  N  N   B ASN   A 20  ? 0.1840 0.1920 0.1693 -0.0010 0.0301  -0.0210 20  ASN   A N   
520  C  CA  A ASN   A 20  ? 0.1682 0.1792 0.2116 0.0082  0.0556  0.0379  20  ASN   A CA  
521  C  CA  B ASN   A 20  ? 0.1956 0.2049 0.1906 0.0005  0.0270  -0.0219 20  ASN   A CA  
522  C  C   A ASN   A 20  ? 0.1947 0.1787 0.2203 -0.0055 0.0811  0.0143  20  ASN   A C   
523  C  C   B ASN   A 20  ? 0.2021 0.2023 0.1937 -0.0077 0.0375  -0.0310 20  ASN   A C   
524  O  O   A ASN   A 20  ? 0.2180 0.1871 0.2520 -0.0237 0.0866  -0.0115 20  ASN   A O   
525  O  O   B ASN   A 20  ? 0.2084 0.2039 0.2002 -0.0112 0.0469  -0.0431 20  ASN   A O   
526  C  CB  A ASN   A 20  ? 0.1687 0.2024 0.2250 0.0280  0.0587  0.0588  20  ASN   A CB  
527  C  CB  B ASN   A 20  ? 0.2051 0.2194 0.2059 0.0118  0.0171  -0.0144 20  ASN   A CB  
528  C  CG  A ASN   A 20  ? 0.1792 0.2161 0.2635 0.0456  0.0607  0.0709  20  ASN   A CG  
529  C  CG  B ASN   A 20  ? 0.2155 0.2302 0.2302 0.0215  0.0066  -0.0088 20  ASN   A CG  
530  O  OD1 A ASN   A 20  ? 0.2085 0.2291 0.3067 0.0613  0.0687  0.0565  20  ASN   A OD1 
531  O  OD1 B ASN   A 20  ? 0.2242 0.2355 0.2394 0.0241  -0.0091 -0.0093 20  ASN   A OD1 
532  N  ND2 A ASN   A 20  ? 0.1807 0.2074 0.2789 0.0453  0.0548  0.0879  20  ASN   A ND2 
533  N  ND2 B ASN   A 20  ? 0.2188 0.2305 0.2402 0.0258  0.0063  -0.0039 20  ASN   A ND2 
546  N  N   A ALA   A 21  ? 0.1950 0.1778 0.2194 -0.0031 0.0706  0.0117  21  ALA   A N   
547  N  N   B ALA   A 21  ? 0.2040 0.2005 0.1976 -0.0106 0.0257  -0.0248 21  ALA   A N   
548  C  CA  A ALA   A 21  ? 0.1984 0.1742 0.2197 -0.0054 0.0599  0.0113  21  ALA   A CA  
549  C  CA  B ALA   A 21  ? 0.2055 0.1974 0.2021 -0.0137 0.0252  -0.0147 21  ALA   A CA  
550  C  C   A ALA   A 21  ? 0.1775 0.1732 0.2196 -0.0004 0.0524  0.0274  21  ALA   A C   
551  C  C   B ALA   A 21  ? 0.1970 0.1920 0.1966 -0.0140 0.0376  -0.0060 21  ALA   A C   
552  O  O   A ALA   A 21  ? 0.1765 0.1829 0.2207 0.0138  0.0418  0.0355  21  ALA   A O   
553  O  O   B ALA   A 21  ? 0.1985 0.1902 0.2088 -0.0076 0.0440  -0.0083 21  ALA   A O   
554  C  CB  A ALA   A 21  ? 0.2176 0.1838 0.2167 -0.0137 0.0580  0.0180  21  ALA   A CB  
555  C  CB  B ALA   A 21  ? 0.2128 0.1973 0.2236 -0.0142 0.0184  -0.0100 21  ALA   A CB  
566  N  N   A ASP   A 22  ? 0.1793 0.1676 0.2463 -0.0096 0.0512  0.0351  22  ASP   A N   
567  N  N   B ASP   A 22  ? 0.1925 0.1889 0.1957 -0.0204 0.0425  0.0072  22  ASP   A N   
568  C  CA  A ASP   A 22  ? 0.1830 0.1746 0.2438 -0.0015 0.0429  0.0417  22  ASP   A CA  
569  C  CA  B ASP   A 22  ? 0.1896 0.1905 0.2002 -0.0213 0.0374  0.0189  22  ASP   A CA  
570  C  C   A ASP   A 22  ? 0.1786 0.1841 0.2036 -0.0019 0.0391  0.0290  22  ASP   A C   
571  C  C   B ASP   A 22  ? 0.1767 0.1848 0.1760 -0.0294 0.0463  0.0186  22  ASP   A C   
572  O  O   A ASP   A 22  ? 0.1816 0.1880 0.2109 -0.0036 0.0464  0.0244  22  ASP   A O   
573  O  O   B ASP   A 22  ? 0.1734 0.1860 0.1839 -0.0375 0.0501  0.0105  22  ASP   A O   
574  C  CB  A ASP   A 22  ? 0.2070 0.1801 0.3054 -0.0094 0.0314  0.0418  22  ASP   A CB  
575  C  CB  B ASP   A 22  ? 0.1991 0.1965 0.2345 -0.0143 0.0266  0.0205  22  ASP   A CB  
576  C  CG  A ASP   A 22  ? 0.2266 0.1932 0.3623 -0.0097 0.0029  0.0547  22  ASP   A CG  
577  C  CG  B ASP   A 22  ? 0.2053 0.2000 0.2584 -0.0146 0.0187  0.0245  22  ASP   A CG  
578  O  OD1 A ASP   A 22  ? 0.2213 0.1963 0.3836 -0.0251 -0.0110 0.0644  22  ASP   A OD1 
579  O  OD1 B ASP   A 22  ? 0.2111 0.1986 0.2604 -0.0148 0.0213  0.0239  22  ASP   A OD1 
580  O  OD2 A ASP   A 22  ? 0.2525 0.2055 0.3990 0.0013  -0.0012 0.0453  22  ASP   A OD2 
581  O  OD2 B ASP   A 22  ? 0.2015 0.2057 0.2771 -0.0158 0.0132  0.0213  22  ASP   A OD2 
590  N  N   A ILE   A 23  ? 0.1791 0.1820 0.1793 0.0009  0.0388  0.0213  23  ILE   A N   
591  N  N   B ILE   A 23  ? 0.1725 0.1783 0.1611 -0.0256 0.0422  0.0244  23  ILE   A N   
592  C  CA  A ILE   A 23  ? 0.1807 0.1726 0.1690 -0.0007 0.0369  0.0218  23  ILE   A CA  
593  C  CA  B ILE   A 23  ? 0.1658 0.1733 0.1489 -0.0188 0.0244  0.0239  23  ILE   A CA  
594  C  C   A ILE   A 23  ? 0.1740 0.1775 0.1722 0.0017  0.0596  0.0160  23  ILE   A C   
595  C  C   B ILE   A 23  ? 0.1697 0.1762 0.1664 -0.0229 0.0227  0.0141  23  ILE   A C   
596  O  O   A ILE   A 23  ? 0.1891 0.1838 0.1702 0.0009  0.0558  0.0028  23  ILE   A O   
597  O  O   B ILE   A 23  ? 0.1672 0.1683 0.1719 -0.0219 0.0140  0.0115  23  ILE   A O   
598  C  CB  A ILE   A 23  ? 0.1856 0.1709 0.1494 0.0004  0.0295  0.0197  23  ILE   A CB  
599  C  CB  B ILE   A 23  ? 0.1620 0.1640 0.1345 -0.0088 0.0133  0.0265  23  ILE   A CB  
600  C  CG1 A ILE   A 23  ? 0.1865 0.1662 0.1427 0.0014  0.0229  0.0131  23  ILE   A CG1 
601  C  CG1 B ILE   A 23  ? 0.1612 0.1596 0.1264 -0.0077 0.0083  0.0237  23  ILE   A CG1 
602  C  CG2 A ILE   A 23  ? 0.1842 0.1724 0.1609 0.0029  0.0337  0.0267  23  ILE   A CG2 
603  C  CG2 B ILE   A 23  ? 0.1612 0.1618 0.1367 -0.0026 0.0108  0.0282  23  ILE   A CG2 
604  C  CD1 A ILE   A 23  ? 0.1906 0.1650 0.1434 0.0032  0.0078  -0.0032 23  ILE   A CD1 
605  C  CD1 B ILE   A 23  ? 0.1584 0.1583 0.1371 -0.0026 0.0021  0.0169  23  ILE   A CD1 
628  N  N   A VAL   A 24  ? 0.1760 0.1797 0.1857 -0.0023 0.0576  0.0108  24  VAL   A N   
629  N  N   B VAL   A 24  ? 0.1825 0.1891 0.1919 -0.0254 0.0231  0.0081  24  VAL   A N   
630  C  CA  A VAL   A 24  ? 0.1967 0.1907 0.2176 -0.0148 0.0556  0.0012  24  VAL   A CA  
631  C  CA  B VAL   A 24  ? 0.1965 0.1980 0.2093 -0.0241 0.0276  0.0039  24  VAL   A CA  
632  C  C   A VAL   A 24  ? 0.2030 0.2050 0.2193 -0.0262 0.0438  -0.0046 24  VAL   A C   
633  C  C   B VAL   A 24  ? 0.2013 0.2105 0.2103 -0.0257 0.0340  -0.0075 24  VAL   A C   
634  O  O   A VAL   A 24  ? 0.2170 0.2116 0.2155 -0.0272 0.0499  -0.0151 24  VAL   A O   
635  O  O   B VAL   A 24  ? 0.2067 0.2148 0.2185 -0.0201 0.0347  -0.0047 24  VAL   A O   
636  C  CB  A VAL   A 24  ? 0.2056 0.1898 0.2452 -0.0108 0.0636  0.0022  24  VAL   A CB  
637  C  CB  B VAL   A 24  ? 0.2029 0.1991 0.2269 -0.0193 0.0238  0.0089  24  VAL   A CB  
638  C  CG1 A VAL   A 24  ? 0.2148 0.1995 0.2603 -0.0115 0.0640  -0.0090 24  VAL   A CG1 
639  C  CG1 B VAL   A 24  ? 0.2090 0.2044 0.2382 -0.0134 0.0246  0.0083  24  VAL   A CG1 
640  C  CG2 A VAL   A 24  ? 0.2178 0.1956 0.2542 -0.0066 0.0857  0.0236  24  VAL   A CG2 
641  C  CG2 B VAL   A 24  ? 0.2064 0.1945 0.2288 -0.0217 0.0257  0.0097  24  VAL   A CG2 
660  N  N   A GLU   A 25  ? 0.2057 0.2228 0.2150 -0.0321 0.0546  -0.0108 25  GLU   A N   
661  N  N   B GLU   A 25  ? 0.2031 0.2201 0.2010 -0.0293 0.0527  -0.0155 25  GLU   A N   
662  C  CA  A GLU   A 25  ? 0.2183 0.2462 0.2209 -0.0224 0.0603  -0.0172 25  GLU   A CA  
663  C  CA  B GLU   A 25  ? 0.2127 0.2322 0.2095 -0.0360 0.0563  -0.0169 25  GLU   A CA  
664  C  C   A GLU   A 25  ? 0.2074 0.2478 0.1928 -0.0324 0.0661  -0.0162 25  GLU   A C   
665  C  C   B GLU   A 25  ? 0.2131 0.2313 0.1934 -0.0397 0.0619  -0.0178 25  GLU   A C   
666  O  O   A GLU   A 25  ? 0.2143 0.2574 0.2185 -0.0336 0.0590  -0.0204 25  GLU   A O   
667  O  O   B GLU   A 25  ? 0.2147 0.2315 0.1930 -0.0416 0.0684  -0.0248 25  GLU   A O   
668  C  CB  A GLU   A 25  ? 0.2445 0.2783 0.2689 -0.0124 0.0636  -0.0085 25  GLU   A CB  
669  C  CB  B GLU   A 25  ? 0.2212 0.2407 0.2351 -0.0412 0.0533  -0.0198 25  GLU   A CB  
670  C  CG  A GLU   A 25  ? 0.2783 0.3056 0.3390 -0.0146 0.0412  -0.0098 25  GLU   A CG  
671  C  CG  B GLU   A 25  ? 0.2356 0.2525 0.2773 -0.0454 0.0455  -0.0166 25  GLU   A CG  
672  C  CD  A GLU   A 25  ? 0.3017 0.3274 0.3961 -0.0184 0.0250  -0.0071 25  GLU   A CD  
673  C  CD  B GLU   A 25  ? 0.2445 0.2634 0.3175 -0.0496 0.0347  -0.0123 25  GLU   A CD  
674  O  OE1 A GLU   A 25  ? 0.3130 0.3366 0.4105 -0.0160 0.0118  -0.0128 25  GLU   A OE1 
675  O  OE1 B GLU   A 25  ? 0.2462 0.2662 0.3344 -0.0504 0.0323  -0.0104 25  GLU   A OE1 
676  O  OE2 A GLU   A 25  ? 0.3053 0.3354 0.4263 -0.0233 0.0199  -0.0136 25  GLU   A OE2 
677  O  OE2 B GLU   A 25  ? 0.2504 0.2698 0.3351 -0.0488 0.0355  -0.0069 25  GLU   A OE2 
690  N  N   A GLU   A 26  ? 0.1946 0.2451 0.1919 -0.0483 0.0653  -0.0199 26  GLU   A N   
691  N  N   B GLU   A 26  ? 0.2138 0.2254 0.1847 -0.0427 0.0635  -0.0203 26  GLU   A N   
692  C  CA  A GLU   A 26  ? 0.2070 0.2540 0.1661 -0.0603 0.0678  -0.0179 26  GLU   A CA  
693  C  CA  B GLU   A 26  ? 0.2211 0.2203 0.1887 -0.0430 0.0596  -0.0169 26  GLU   A CA  
694  C  C   A GLU   A 26  ? 0.2099 0.2456 0.1513 -0.0590 0.0551  -0.0154 26  GLU   A C   
695  C  C   B GLU   A 26  ? 0.2242 0.2206 0.1779 -0.0363 0.0501  -0.0092 26  GLU   A C   
696  O  O   A GLU   A 26  ? 0.2220 0.2478 0.1659 -0.0659 0.0536  -0.0097 26  GLU   A O   
697  O  O   B GLU   A 26  ? 0.2231 0.2163 0.1711 -0.0376 0.0526  -0.0055 26  GLU   A O   
698  C  CB  A GLU   A 26  ? 0.2257 0.2709 0.1956 -0.0676 0.0612  -0.0186 26  GLU   A CB  
699  C  CB  B GLU   A 26  ? 0.2293 0.2139 0.2108 -0.0524 0.0594  -0.0252 26  GLU   A CB  
700  C  CG  A GLU   A 26  ? 0.2530 0.3007 0.2787 -0.0661 0.0534  -0.0218 26  GLU   A CG  
701  C  CG  B GLU   A 26  ? 0.2343 0.2015 0.2223 -0.0668 0.0739  -0.0365 26  GLU   A CG  
702  C  CD  A GLU   A 26  ? 0.2657 0.3228 0.3267 -0.0717 0.0638  -0.0224 26  GLU   A CD  
703  C  CD  B GLU   A 26  ? 0.2360 0.1872 0.2225 -0.0930 0.0948  -0.0428 26  GLU   A CD  
704  O  OE1 A GLU   A 26  ? 0.2681 0.3378 0.3200 -0.0747 0.0754  -0.0293 26  GLU   A OE1 
705  O  OE1 B GLU   A 26  ? 0.2345 0.1800 0.2206 -0.0991 0.1092  -0.0722 26  GLU   A OE1 
706  O  OE2 A GLU   A 26  ? 0.2855 0.3347 0.3672 -0.0633 0.0526  -0.0215 26  GLU   A OE2 
707  O  OE2 B GLU   A 26  ? 0.2438 0.1928 0.1995 -0.0862 0.1106  -0.0326 26  GLU   A OE2 
720  N  N   A ALA   A 27  ? 0.1934 0.2310 0.1552 -0.0628 0.0522  -0.0048 27  ALA   A N   
721  N  N   B ALA   A 27  ? 0.2287 0.2264 0.1758 -0.0307 0.0419  -0.0054 27  ALA   A N   
722  C  CA  A ALA   A 27  ? 0.2025 0.2407 0.1561 -0.0598 0.0427  -0.0033 27  ALA   A CA  
723  C  CA  B ALA   A 27  ? 0.2387 0.2386 0.1778 -0.0248 0.0299  -0.0056 27  ALA   A CA  
724  C  C   A ALA   A 27  ? 0.2295 0.2575 0.1607 -0.0701 0.0462  -0.0121 27  ALA   A C   
725  C  C   B ALA   A 27  ? 0.2561 0.2559 0.1917 -0.0243 0.0244  -0.0122 27  ALA   A C   
726  O  O   A ALA   A 27  ? 0.2339 0.2481 0.1740 -0.0768 0.0353  -0.0043 27  ALA   A O   
727  O  O   B ALA   A 27  ? 0.2582 0.2539 0.1929 -0.0252 0.0182  -0.0127 27  ALA   A O   
728  C  CB  A ALA   A 27  ? 0.1839 0.2376 0.1552 -0.0606 0.0314  -0.0004 27  ALA   A CB  
729  C  CB  B ALA   A 27  ? 0.2327 0.2361 0.1737 -0.0243 0.0259  -0.0000 27  ALA   A CB  
740  N  N   A LYS   A 28  ? 0.2614 0.2838 0.1757 -0.0678 0.0396  -0.0428 28  LYS   A N   
741  N  N   B LYS   A 28  ? 0.2749 0.2762 0.2122 -0.0248 0.0208  -0.0210 28  LYS   A N   
742  C  CA  A LYS   A 28  ? 0.3002 0.3190 0.2057 -0.0575 0.0421  -0.0618 28  LYS   A CA  
743  C  CA  B LYS   A 28  ? 0.2960 0.3000 0.2388 -0.0248 0.0190  -0.0249 28  LYS   A CA  
744  C  C   A LYS   A 28  ? 0.3222 0.3492 0.1950 -0.0651 0.0599  -0.0448 28  LYS   A C   
745  C  C   B LYS   A 28  ? 0.3168 0.3261 0.2477 -0.0329 0.0279  -0.0193 28  LYS   A C   
746  O  O   A LYS   A 28  ? 0.3314 0.3587 0.2365 -0.0658 0.0374  -0.0465 28  LYS   A O   
747  O  O   B LYS   A 28  ? 0.3197 0.3303 0.2595 -0.0325 0.0224  -0.0204 28  LYS   A O   
748  C  CB  A LYS   A 28  ? 0.3183 0.3288 0.2650 -0.0396 0.0265  -0.0802 28  LYS   A CB  
749  C  CB  B LYS   A 28  ? 0.2976 0.3000 0.2637 -0.0180 0.0090  -0.0296 28  LYS   A CB  
750  C  CG  A LYS   A 28  ? 0.3360 0.3388 0.3269 -0.0246 0.0151  -0.0842 28  LYS   A CG  
751  C  CG  B LYS   A 28  ? 0.3004 0.3022 0.2940 -0.0123 0.0022  -0.0293 28  LYS   A CG  
752  C  CD  A LYS   A 28  ? 0.3512 0.3555 0.4022 -0.0128 0.0013  -0.0830 28  LYS   A CD  
753  C  CD  B LYS   A 28  ? 0.3051 0.3078 0.3325 -0.0099 -0.0047 -0.0282 28  LYS   A CD  
754  C  CE  A LYS   A 28  ? 0.3609 0.3686 0.4539 -0.0055 -0.0084 -0.0836 28  LYS   A CE  
755  C  CE  B LYS   A 28  ? 0.3092 0.3123 0.3620 -0.0117 -0.0091 -0.0262 28  LYS   A CE  
756  N  NZ  A LYS   A 28  ? 0.3684 0.3758 0.4875 0.0002  -0.0090 -0.0866 28  LYS   A NZ  
757  N  NZ  B LYS   A 28  ? 0.3099 0.3144 0.3769 -0.0126 -0.0117 -0.0269 28  LYS   A NZ  
784  N  N   A LYS   A 29  ? 0.3331 0.3688 0.1845 -0.0729 0.0949  -0.0188 29  LYS   A N   
785  N  N   B LYS   A 29  ? 0.3340 0.3471 0.2583 -0.0424 0.0424  -0.0094 29  LYS   A N   
786  C  CA  A LYS   A 29  ? 0.3544 0.3934 0.2115 -0.0736 0.1098  -0.0032 29  LYS   A CA  
787  C  CA  B LYS   A 29  ? 0.3524 0.3686 0.2770 -0.0512 0.0547  -0.0022 29  LYS   A CA  
788  C  C   A LYS   A 29  ? 0.3610 0.3909 0.1921 -0.0762 0.0942  0.0040  29  LYS   A C   
789  C  C   B LYS   A 29  ? 0.3553 0.3740 0.2368 -0.0666 0.0662  0.0039  29  LYS   A C   
790  O  O   A LYS   A 29  ? 0.3739 0.4060 0.2079 -0.0690 0.0882  0.0009  29  LYS   A O   
791  O  O   B LYS   A 29  ? 0.3604 0.3796 0.2465 -0.0645 0.0651  0.0047  29  LYS   A O   
792  C  CB  A LYS   A 29  ? 0.3698 0.4204 0.2732 -0.0646 0.1234  0.0027  29  LYS   A CB  
793  C  CB  B LYS   A 29  ? 0.3662 0.3837 0.3326 -0.0430 0.0528  -0.0010 29  LYS   A CB  
794  C  CG  A LYS   A 29  ? 0.3877 0.4430 0.3445 -0.0541 0.1242  0.0024  29  LYS   A CG  
795  C  CG  B LYS   A 29  ? 0.3793 0.3966 0.3844 -0.0353 0.0502  -0.0010 29  LYS   A CG  
796  C  CD  A LYS   A 29  ? 0.4046 0.4620 0.4153 -0.0456 0.1184  -0.0008 29  LYS   A CD  
797  C  CD  B LYS   A 29  ? 0.3907 0.4078 0.4294 -0.0295 0.0476  -0.0010 29  LYS   A CD  
798  C  CE  A LYS   A 29  ? 0.4164 0.4755 0.4628 -0.0402 0.1154  -0.0038 29  LYS   A CE  
799  C  CE  B LYS   A 29  ? 0.3988 0.4162 0.4611 -0.0258 0.0460  -0.0013 29  LYS   A CE  
800  N  NZ  A LYS   A 29  ? 0.4217 0.4830 0.4943 -0.0368 0.1131  -0.0068 29  LYS   A NZ  
801  N  NZ  B LYS   A 29  ? 0.4030 0.4208 0.4802 -0.0237 0.0448  -0.0013 29  LYS   A NZ  
828  N  N   . VAL   A 30  ? 0.3502 0.3726 0.1934 -0.0843 0.0798  0.0073  30  VAL   A N   
829  C  CA  . VAL   A 30  ? 0.3444 0.3549 0.1716 -0.1055 0.0499  0.0268  30  VAL   A CA  
830  C  C   . VAL   A 30  ? 0.3482 0.3445 0.1329 -0.1082 0.0337  0.0324  30  VAL   A C   
831  O  O   . VAL   A 30  ? 0.3556 0.3476 0.1409 -0.1100 0.0260  0.0341  30  VAL   A O   
832  C  CB  . VAL   A 30  ? 0.3382 0.3426 0.2183 -0.1206 0.0238  0.0337  30  VAL   A CB  
833  C  CG1 . VAL   A 30  ? 0.3419 0.3410 0.2349 -0.1209 0.0109  0.0381  30  VAL   A CG1 
834  C  CG2 . VAL   A 30  ? 0.3360 0.3422 0.2418 -0.1292 0.0258  0.0326  30  VAL   A CG2 
845  N  N   . LYS   A 31  ? 0.3382 0.3266 0.1203 -0.1095 0.0162  0.0262  31  LYS   A N   
846  C  CA  . LYS   A 31  ? 0.3499 0.3280 0.1364 -0.0968 -0.0172 0.0231  31  LYS   A CA  
847  C  C   . LYS   A 31  ? 0.3179 0.3035 0.1170 -0.0736 -0.0164 0.0586  31  LYS   A C   
848  O  O   . LYS   A 31  ? 0.3260 0.3182 0.1488 -0.0666 -0.0302 0.0749  31  LYS   A O   
849  C  CB  . LYS   A 31  ? 0.3970 0.3603 0.2356 -0.0883 -0.0421 -0.0049 31  LYS   A CB  
850  C  CG  . LYS   A 31  ? 0.4485 0.3961 0.3837 -0.0754 -0.0593 -0.0203 31  LYS   A CG  
851  C  CD  . LYS   A 31  ? 0.4891 0.4293 0.4945 -0.0620 -0.0771 -0.0337 31  LYS   A CD  
852  C  CE  . LYS   A 31  ? 0.5202 0.4564 0.5647 -0.0518 -0.0897 -0.0438 31  LYS   A CE  
853  N  NZ  . LYS   A 31  ? 0.5339 0.4608 0.6034 -0.0468 -0.0969 -0.0513 31  LYS   A NZ  
867  N  N   . PRO   A 32  ? 0.2800 0.2672 0.1022 -0.0763 -0.0067 0.0398  32  PRO   A N   
868  C  CA  . PRO   A 32  ? 0.2658 0.2477 0.1424 -0.0712 -0.0203 0.0538  32  PRO   A CA  
869  C  C   . PRO   A 32  ? 0.2612 0.2432 0.1516 -0.0610 -0.0295 0.0635  32  PRO   A C   
870  O  O   . PRO   A 32  ? 0.2547 0.2392 0.1676 -0.0593 -0.0458 0.0635  32  PRO   A O   
871  C  CB  . PRO   A 32  ? 0.2571 0.2546 0.1515 -0.0636 -0.0184 0.0419  32  PRO   A CB  
872  C  CG  . PRO   A 32  ? 0.2536 0.2555 0.0983 -0.0577 -0.0282 0.0333  32  PRO   A CG  
873  C  CD  . PRO   A 32  ? 0.2598 0.2568 0.0968 -0.0657 -0.0167 0.0359  32  PRO   A CD  
881  N  N   . THR   A 33  ? 0.2685 0.2405 0.1449 -0.0564 -0.0249 0.0631  33  THR   A N   
882  C  CA  . THR   A 33  ? 0.2677 0.2415 0.1507 -0.0481 -0.0375 0.0626  33  THR   A CA  
883  C  C   . THR   A 33  ? 0.2349 0.2217 0.1476 -0.0490 -0.0331 0.0460  33  THR   A C   
884  O  O   . THR   A 33  ? 0.2277 0.2215 0.1612 -0.0441 -0.0493 0.0488  33  THR   A O   
885  C  CB  . THR   A 33  ? 0.2941 0.2652 0.1701 -0.0345 -0.0479 0.0789  33  THR   A CB  
886  O  OG1 . THR   A 33  ? 0.3160 0.2823 0.2006 -0.0169 -0.0370 0.0941  33  THR   A OG1 
887  C  CG2 . THR   A 33  ? 0.3003 0.2733 0.1879 -0.0276 -0.0570 0.0840  33  THR   A CG2 
895  N  N   . VAL   A 34  ? 0.2057 0.2037 0.1259 -0.0466 -0.0245 0.0433  34  VAL   A N   
896  C  CA  . VAL   A 34  ? 0.1873 0.1903 0.1162 -0.0368 -0.0199 0.0395  34  VAL   A CA  
897  C  C   . VAL   A 34  ? 0.1743 0.1807 0.1058 -0.0306 -0.0076 0.0353  34  VAL   A C   
898  O  O   . VAL   A 34  ? 0.1753 0.1858 0.1365 -0.0373 -0.0065 0.0415  34  VAL   A O   
899  C  CB  . VAL   A 34  ? 0.1881 0.1881 0.1448 -0.0329 -0.0099 0.0243  34  VAL   A CB  
900  C  CG1 . VAL   A 34  ? 0.1933 0.1878 0.1396 -0.0345 0.0028  0.0138  34  VAL   A CG1 
901  C  CG2 . VAL   A 34  ? 0.1987 0.2033 0.1746 -0.0177 -0.0225 0.0276  34  VAL   A CG2 
911  N  N   . VAL   A 35  ? 0.1620 0.1689 0.1163 -0.0319 -0.0119 0.0297  35  VAL   A N   
912  C  CA  . VAL   A 35  ? 0.1529 0.1645 0.1127 -0.0269 -0.0027 0.0212  35  VAL   A CA  
913  C  C   . VAL   A 35  ? 0.1435 0.1509 0.1118 -0.0225 0.0000  0.0210  35  VAL   A C   
914  O  O   . VAL   A 35  ? 0.1405 0.1594 0.1254 -0.0289 0.0084  0.0184  35  VAL   A O   
915  C  CB  . VAL   A 35  ? 0.1586 0.1674 0.1205 -0.0187 0.0060  0.0139  35  VAL   A CB  
916  C  CG1 . VAL   A 35  ? 0.1742 0.1745 0.1305 -0.0079 0.0047  0.0160  35  VAL   A CG1 
917  C  CG2 . VAL   A 35  ? 0.1566 0.1684 0.1577 -0.0097 0.0106  0.0072  35  VAL   A CG2 
927  N  N   . VAL   A 36  ? 0.1331 0.1504 0.1030 -0.0191 0.0065  0.0179  36  VAL   A N   
928  C  CA  . VAL   A 36  ? 0.1276 0.1395 0.1086 -0.0130 0.0032  0.0079  36  VAL   A CA  
929  C  C   . VAL   A 36  ? 0.1284 0.1408 0.1186 -0.0128 0.0073  0.0123  36  VAL   A C   
930  O  O   . VAL   A 36  ? 0.1341 0.1392 0.1341 -0.0079 0.0198  0.0145  36  VAL   A O   
931  C  CB  . VAL   A 36  ? 0.1302 0.1306 0.1269 -0.0119 0.0013  0.0152  36  VAL   A CB  
932  C  CG1 . VAL   A 36  ? 0.1347 0.1316 0.1306 -0.0170 0.0038  0.0040  36  VAL   A CG1 
933  C  CG2 . VAL   A 36  ? 0.1408 0.1362 0.1441 -0.0083 -0.0035 0.0238  36  VAL   A CG2 
943  N  N   . ASN   A 37  ? 0.1196 0.1341 0.1065 -0.0044 0.0047  0.0160  37  ASN   A N   
944  C  CA  . ASN   A 37  ? 0.1270 0.1270 0.1024 -0.0044 0.0038  0.0215  37  ASN   A CA  
945  C  C   . ASN   A 37  ? 0.1256 0.1202 0.1117 -0.0068 0.0066  0.0238  37  ASN   A C   
946  O  O   . ASN   A 37  ? 0.1377 0.1334 0.1116 0.0067  0.0097  0.0096  37  ASN   A O   
947  C  CB  . ASN   A 37  ? 0.1297 0.1259 0.1211 0.0018  0.0042  0.0154  37  ASN   A CB  
948  C  CG  . ASN   A 37  ? 0.1319 0.1259 0.1218 -0.0015 0.0039  0.0131  37  ASN   A CG  
949  O  OD1 . ASN   A 37  ? 0.1271 0.1332 0.1411 0.0036  0.0037  0.0144  37  ASN   A OD1 
950  N  ND2 . ASN   A 37  ? 0.1325 0.1277 0.1265 -0.0050 0.0021  0.0225  37  ASN   A ND2 
957  N  N   A ALA   A 38  ? 0.1209 0.1310 0.1175 -0.0032 0.0116  0.0108  38  ALA   A N   
958  N  N   B ALA   A 38  ? 0.1261 0.1297 0.1200 -0.0092 0.0005  0.0197  38  ALA   A N   
959  C  CA  A ALA   A 38  ? 0.1332 0.1345 0.1061 -0.0003 0.0015  0.0037  38  ALA   A CA  
960  C  CA  B ALA   A 38  ? 0.1342 0.1362 0.1267 -0.0102 -0.0107 0.0191  38  ALA   A CA  
961  C  C   A ALA   A 38  ? 0.1275 0.1401 0.0972 0.0061  -0.0019 0.0024  38  ALA   A C   
962  C  C   B ALA   A 38  ? 0.1318 0.1378 0.1240 -0.0112 -0.0101 0.0186  38  ALA   A C   
963  O  O   A ALA   A 38  ? 0.1208 0.1261 0.1180 0.0047  -0.0117 -0.0038 38  ALA   A O   
964  O  O   B ALA   A 38  ? 0.1270 0.1326 0.1366 -0.0162 -0.0116 0.0231  38  ALA   A O   
965  C  CB  A ALA   A 38  ? 0.1291 0.1545 0.1178 -0.0179 0.0018  0.0006  38  ALA   A CB  
966  C  CB  B ALA   A 38  ? 0.1375 0.1429 0.1399 -0.0119 -0.0193 0.0166  38  ALA   A CB  
977  N  N   A ALA   A 39  ? 0.1262 0.1342 0.1154 0.0084  0.0093  0.0080  39  ALA   A N   
978  N  N   B ALA   A 39  ? 0.1349 0.1367 0.1253 -0.0116 -0.0049 0.0197  39  ALA   A N   
979  C  CA  A ALA   A 39  ? 0.1256 0.1318 0.1163 0.0050  0.0129  0.0019  39  ALA   A CA  
980  C  CA  B ALA   A 39  ? 0.1397 0.1413 0.1254 -0.0110 -0.0023 0.0217  39  ALA   A CA  
981  C  C   A ALA   A 39  ? 0.1216 0.1356 0.1255 0.0003  0.0049  -0.0005 39  ALA   A C   
982  C  C   B ALA   A 39  ? 0.1329 0.1375 0.1098 -0.0105 0.0058  0.0232  39  ALA   A C   
983  O  O   A ALA   A 39  ? 0.1381 0.1332 0.1346 -0.0007 -0.0009 0.0024  39  ALA   A O   
984  O  O   B ALA   A 39  ? 0.1345 0.1367 0.0900 -0.0190 0.0104  0.0280  39  ALA   A O   
985  C  CB  A ALA   A 39  ? 0.1307 0.1276 0.1243 0.0005  -0.0018 -0.0031 39  ALA   A CB  
986  C  CB  B ALA   A 39  ? 0.1549 0.1482 0.1425 -0.0094 -0.0133 0.0126  39  ALA   A CB  
997  N  N   A ASN   A 40  ? 0.1267 0.1376 0.1297 -0.0111 0.0155  0.0042  40  ASN   A N   
998  N  N   B ASN   A 40  ? 0.1336 0.1332 0.1154 -0.0064 0.0131  0.0252  40  ASN   A N   
999  C  CA  A ASN   A 40  ? 0.1271 0.1348 0.1247 -0.0011 0.0071  0.0011  40  ASN   A CA  
1000 C  CA  B ASN   A 40  ? 0.1383 0.1291 0.1234 0.0000  0.0026  0.0213  40  ASN   A CA  
1001 C  C   A ASN   A 40  ? 0.1262 0.1265 0.1086 -0.0039 0.0139  0.0097  40  ASN   A C   
1002 C  C   B ASN   A 40  ? 0.1380 0.1316 0.1183 0.0024  0.0046  0.0258  40  ASN   A C   
1003 O  O   A ASN   A 40  ? 0.1275 0.1287 0.1169 -0.0113 0.0163  0.0119  40  ASN   A O   
1004 O  O   B ASN   A 40  ? 0.1349 0.1312 0.1239 0.0012  0.0026  0.0289  40  ASN   A O   
1005 C  CB  A ASN   A 40  ? 0.1426 0.1427 0.1444 0.0073  -0.0109 0.0027  40  ASN   A CB  
1006 C  CB  B ASN   A 40  ? 0.1476 0.1261 0.1461 -0.0008 0.0002  0.0124  40  ASN   A CB  
1007 C  CG  A ASN   A 40  ? 0.1486 0.1419 0.1578 0.0064  -0.0006 0.0137  40  ASN   A CG  
1008 C  CG  B ASN   A 40  ? 0.1563 0.1202 0.1708 -0.0042 -0.0020 0.0089  40  ASN   A CG  
1009 O  OD1 A ASN   A 40  ? 0.1610 0.1433 0.1808 0.0061  0.0090  0.0110  40  ASN   A OD1 
1010 O  OD1 B ASN   A 40  ? 0.1691 0.1222 0.1973 -0.0065 -0.0123 -0.0088 40  ASN   A OD1 
1011 N  ND2 A ASN   A 40  ? 0.1541 0.1536 0.1620 0.0023  0.0144  -0.0062 40  ASN   A ND2 
1012 N  ND2 B ASN   A 40  ? 0.1539 0.1237 0.1781 -0.0128 0.0228  0.0102  40  ASN   A ND2 
1025 N  N   A VAL   A 41  ? 0.1356 0.1277 0.1135 -0.0038 0.0121  0.0096  41  VAL   A N   
1026 N  N   B VAL   A 41  ? 0.1384 0.1361 0.1160 0.0042  0.0098  0.0278  41  VAL   A N   
1027 C  CA  A VAL   A 41  ? 0.1318 0.1295 0.1250 -0.0021 0.0185  0.0097  41  VAL   A CA  
1028 C  CA  B VAL   A 41  ? 0.1400 0.1415 0.1205 0.0043  0.0178  0.0254  41  VAL   A CA  
1029 C  C   A VAL   A 41  ? 0.1331 0.1359 0.1422 0.0056  0.0188  0.0120  41  VAL   A C   
1030 C  C   B VAL   A 41  ? 0.1363 0.1448 0.1309 0.0011  0.0213  0.0241  41  VAL   A C   
1031 O  O   A VAL   A 41  ? 0.1397 0.1275 0.1516 0.0036  0.0185  0.0052  41  VAL   A O   
1032 O  O   B VAL   A 41  ? 0.1398 0.1395 0.1495 -0.0024 0.0146  0.0226  41  VAL   A O   
1033 C  CB  A VAL   A 41  ? 0.1401 0.1383 0.1318 -0.0015 0.0187  0.0112  41  VAL   A CB  
1034 C  CB  B VAL   A 41  ? 0.1435 0.1490 0.1383 0.0094  0.0238  0.0176  41  VAL   A CB  
1035 C  CG1 A VAL   A 41  ? 0.1484 0.1526 0.1435 0.0000  0.0101  0.0020  41  VAL   A CG1 
1036 C  CG1 B VAL   A 41  ? 0.1552 0.1525 0.1467 0.0087  0.0268  0.0081  41  VAL   A CG1 
1037 C  CG2 A VAL   A 41  ? 0.1520 0.1381 0.1110 -0.0043 0.0313  0.0076  41  VAL   A CG2 
1038 C  CG2 B VAL   A 41  ? 0.1429 0.1587 0.1483 0.0106  0.0114  0.0182  41  VAL   A CG2 
1057 N  N   A TYR   A 42  ? 0.1249 0.1295 0.1498 -0.0034 0.0253  0.0160  42  TYR   A N   
1058 N  N   B TYR   A 42  ? 0.1359 0.1455 0.1335 0.0028  0.0189  0.0317  42  TYR   A N   
1059 C  CA  A TYR   A 42  ? 0.1312 0.1248 0.1544 -0.0056 0.0263  0.0181  42  TYR   A CA  
1060 C  CA  B TYR   A 42  ? 0.1436 0.1498 0.1393 0.0028  0.0222  0.0293  42  TYR   A CA  
1061 C  C   A TYR   A 42  ? 0.1225 0.1206 0.1602 -0.0093 0.0186  0.0215  42  TYR   A C   
1062 C  C   B TYR   A 42  ? 0.1427 0.1479 0.1280 0.0009  0.0149  0.0344  42  TYR   A C   
1063 O  O   A TYR   A 42  ? 0.1219 0.1209 0.1889 -0.0179 0.0158  -0.0012 42  TYR   A O   
1064 O  O   B TYR   A 42  ? 0.1422 0.1540 0.1346 -0.0023 0.0141  0.0277  42  TYR   A O   
1065 C  CB  A TYR   A 42  ? 0.1600 0.1333 0.1414 -0.0071 0.0308  0.0303  42  TYR   A CB  
1066 C  CB  B TYR   A 42  ? 0.1584 0.1572 0.1497 0.0020  0.0148  0.0267  42  TYR   A CB  
1067 C  CG  A TYR   A 42  ? 0.1824 0.1417 0.1450 -0.0093 0.0276  0.0402  42  TYR   A CG  
1068 C  CG  B TYR   A 42  ? 0.1715 0.1664 0.1572 0.0032  0.0084  0.0227  42  TYR   A CG  
1069 C  CD1 A TYR   A 42  ? 0.1942 0.1537 0.1548 -0.0168 0.0344  0.0356  42  TYR   A CD1 
1070 C  CD1 B TYR   A 42  ? 0.1777 0.1712 0.1649 0.0030  0.0065  0.0187  42  TYR   A CD1 
1071 C  CD2 A TYR   A 42  ? 0.2001 0.1602 0.1738 -0.0040 0.0320  0.0294  42  TYR   A CD2 
1072 C  CD2 B TYR   A 42  ? 0.1801 0.1769 0.1626 0.0059  0.0100  0.0189  42  TYR   A CD2 
1073 C  CE1 A TYR   A 42  ? 0.2104 0.1672 0.1622 -0.0243 0.0428  0.0219  42  TYR   A CE1 
1074 C  CE1 B TYR   A 42  ? 0.1866 0.1787 0.1742 0.0011  0.0109  0.0109  42  TYR   A CE1 
1075 C  CE2 A TYR   A 42  ? 0.2190 0.1706 0.1885 -0.0174 0.0362  0.0342  42  TYR   A CE2 
1076 C  CE2 B TYR   A 42  ? 0.1909 0.1841 0.1741 0.0022  0.0099  0.0161  42  TYR   A CE2 
1077 C  CZ  A TYR   A 42  ? 0.2296 0.1781 0.1694 -0.0285 0.0451  0.0232  42  TYR   A CZ  
1078 C  CZ  B TYR   A 42  ? 0.1975 0.1879 0.1789 -0.0009 0.0129  0.0075  42  TYR   A CZ  
1079 O  OH  A TYR   A 42  ? 0.2494 0.1981 0.1829 -0.0410 0.0423  0.0126  42  TYR   A OH  
1080 O  OH  B TYR   A 42  ? 0.2095 0.2018 0.1937 -0.0053 0.0108  0.0003  42  TYR   A OH  
1099 N  N   A LEU   A 43  ? 0.1232 0.1179 0.1462 -0.0024 0.0136  0.0067  43  LEU   A N   
1100 N  N   B LEU   A 43  ? 0.1385 0.1394 0.1257 -0.0001 0.0006  0.0324  43  LEU   A N   
1101 C  CA  A LEU   A 43  ? 0.1172 0.1212 0.1413 -0.0068 0.0175  0.0051  43  LEU   A CA  
1102 C  CA  B LEU   A 43  ? 0.1387 0.1350 0.1321 -0.0018 -0.0038 0.0246  43  LEU   A CA  
1103 C  C   A LEU   A 43  ? 0.1242 0.1278 0.1377 -0.0025 0.0058  0.0048  43  LEU   A C   
1104 C  C   B LEU   A 43  ? 0.1436 0.1326 0.1372 -0.0069 -0.0067 0.0164  43  LEU   A C   
1105 O  O   A LEU   A 43  ? 0.1397 0.1354 0.1657 0.0018  -0.0085 -0.0011 43  LEU   A O   
1106 O  O   B LEU   A 43  ? 0.1480 0.1284 0.1413 -0.0160 -0.0115 0.0115  43  LEU   A O   
1107 C  CB  A LEU   A 43  ? 0.1334 0.1216 0.1498 -0.0103 0.0119  0.0090  43  LEU   A CB  
1108 C  CB  B LEU   A 43  ? 0.1368 0.1321 0.1370 -0.0003 -0.0059 0.0248  43  LEU   A CB  
1109 C  CG  A LEU   A 43  ? 0.1354 0.1222 0.1510 -0.0049 0.0073  0.0046  43  LEU   A CG  
1110 C  CG  B LEU   A 43  ? 0.1337 0.1294 0.1394 0.0057  -0.0087 0.0194  43  LEU   A CG  
1111 C  CD1 A LEU   A 43  ? 0.1471 0.1312 0.1768 -0.0065 -0.0053 0.0082  43  LEU   A CD1 
1112 C  CD1 B LEU   A 43  ? 0.1385 0.1315 0.1411 0.0076  -0.0148 0.0254  43  LEU   A CD1 
1113 C  CD2 A LEU   A 43  ? 0.1530 0.1273 0.1445 -0.0019 -0.0006 0.0177  43  LEU   A CD2 
1114 C  CD2 B LEU   A 43  ? 0.1388 0.1287 0.1462 0.0049  -0.0050 0.0307  43  LEU   A CD2 
1137 N  N   A LYS   A 44  ? 0.1284 0.1283 0.1334 -0.0037 0.0170  0.0114  44  LYS   A N   
1138 N  N   B LYS   A 44  ? 0.1502 0.1359 0.1434 -0.0013 -0.0081 0.0190  44  LYS   A N   
1139 C  CA  A LYS   A 44  ? 0.1410 0.1240 0.1296 -0.0059 0.0191  0.0150  44  LYS   A CA  
1140 C  CA  B LYS   A 44  ? 0.1658 0.1411 0.1484 0.0036  -0.0057 0.0196  44  LYS   A CA  
1141 C  C   A LYS   A 44  ? 0.1252 0.1280 0.1277 -0.0028 0.0066  0.0086  44  LYS   A C   
1142 C  C   B LYS   A 44  ? 0.1640 0.1387 0.1221 0.0072  -0.0085 0.0095  44  LYS   A C   
1143 O  O   A LYS   A 44  ? 0.1293 0.1406 0.1537 0.0052  0.0105  -0.0038 44  LYS   A O   
1144 O  O   B LYS   A 44  ? 0.1706 0.1402 0.1147 0.0132  -0.0037 -0.0062 44  LYS   A O   
1145 C  CB  A LYS   A 44  ? 0.1751 0.1344 0.1766 -0.0050 0.0344  0.0217  44  LYS   A CB  
1146 C  CB  B LYS   A 44  ? 0.1840 0.1573 0.1839 0.0059  0.0088  0.0285  44  LYS   A CB  
1147 C  CG  A LYS   A 44  ? 0.2079 0.1692 0.2475 -0.0153 0.0575  0.0289  44  LYS   A CG  
1148 C  CG  B LYS   A 44  ? 0.1985 0.1734 0.2289 0.0086  0.0196  0.0315  44  LYS   A CG  
1149 C  CD  A LYS   A 44  ? 0.2388 0.2204 0.3488 -0.0175 0.0483  0.0258  44  LYS   A CD  
1150 C  CD  B LYS   A 44  ? 0.2152 0.1970 0.2949 0.0106  0.0100  0.0263  44  LYS   A CD  
1151 C  CE  A LYS   A 44  ? 0.2487 0.2489 0.4038 -0.0134 0.0454  0.0276  44  LYS   A CE  
1152 C  CE  B LYS   A 44  ? 0.2168 0.2033 0.3344 0.0116  0.0047  0.0284  44  LYS   A CE  
1153 N  NZ  A LYS   A 44  ? 0.2520 0.2644 0.4273 -0.0191 0.0466  0.0297  44  LYS   A NZ  
1154 N  NZ  B LYS   A 44  ? 0.2170 0.2084 0.3563 0.0102  0.0003  0.0411  44  LYS   A NZ  
1181 N  N   A HIS   A 45  ? 0.1173 0.1226 0.1294 -0.0057 0.0056  0.0191  45  HIS   A N   
1182 N  N   B HIS   A 45  ? 0.1610 0.1371 0.1236 0.0055  -0.0152 0.0188  45  HIS   A N   
1183 C  CA  A HIS   A 45  ? 0.1206 0.1271 0.1363 -0.0038 0.0009  0.0011  45  HIS   A CA  
1184 C  CA  B HIS   A 45  ? 0.1558 0.1410 0.1310 0.0069  -0.0164 0.0153  45  HIS   A CA  
1185 C  C   A HIS   A 45  ? 0.1288 0.1394 0.1407 0.0049  0.0010  0.0043  45  HIS   A C   
1186 C  C   B HIS   A 45  ? 0.1576 0.1460 0.1371 0.0138  -0.0055 0.0132  45  HIS   A C   
1187 O  O   A HIS   A 45  ? 0.1498 0.1518 0.1792 0.0246  -0.0056 -0.0119 45  HIS   A O   
1188 O  O   B HIS   A 45  ? 0.1654 0.1536 0.1568 0.0169  -0.0020 0.0084  45  HIS   A O   
1189 C  CB  A HIS   A 45  ? 0.1161 0.1237 0.1285 -0.0113 0.0026  0.0042  45  HIS   A CB  
1190 C  CB  B HIS   A 45  ? 0.1487 0.1383 0.1366 0.0081  -0.0249 0.0129  45  HIS   A CB  
1191 C  CG  A HIS   A 45  ? 0.1238 0.1245 0.1201 -0.0113 0.0067  0.0080  45  HIS   A CG  
1192 C  CG  B HIS   A 45  ? 0.1414 0.1353 0.1277 0.0055  -0.0088 0.0054  45  HIS   A CG  
1193 N  ND1 A HIS   A 45  ? 0.1193 0.1332 0.1417 -0.0097 0.0031  0.0165  45  HIS   A ND1 
1194 N  ND1 B HIS   A 45  ? 0.1373 0.1369 0.1406 0.0063  -0.0051 0.0052  45  HIS   A ND1 
1195 C  CD2 A HIS   A 45  ? 0.1239 0.1281 0.1257 -0.0181 -0.0019 0.0196  45  HIS   A CD2 
1196 C  CD2 B HIS   A 45  ? 0.1390 0.1345 0.1217 0.0038  -0.0079 -0.0014 45  HIS   A CD2 
1197 C  CE1 A HIS   A 45  ? 0.1176 0.1374 0.1293 -0.0121 -0.0007 0.0255  45  HIS   A CE1 
1198 C  CE1 B HIS   A 45  ? 0.1334 0.1347 0.1269 0.0038  -0.0088 -0.0011 45  HIS   A CE1 
1199 N  NE2 A HIS   A 45  ? 0.1207 0.1372 0.1291 -0.0098 0.0031  0.0303  45  HIS   A NE2 
1200 N  NE2 B HIS   A 45  ? 0.1344 0.1365 0.1224 0.0032  -0.0079 -0.0041 45  HIS   A NE2 
1215 N  N   A GLY   A 46  ? 0.1454 0.1399 0.1617 0.0110  -0.0204 0.0110  46  GLY   A N   
1216 N  N   B GLY   A 46  ? 0.1636 0.1462 0.1434 0.0209  -0.0113 0.0112  46  GLY   A N   
1217 C  CA  A GLY   A 46  ? 0.1547 0.1471 0.1770 0.0149  -0.0207 0.0172  46  GLY   A CA  
1218 C  CA  B GLY   A 46  ? 0.1635 0.1475 0.1403 0.0243  -0.0135 0.0116  46  GLY   A CA  
1219 C  C   A GLY   A 46  ? 0.1562 0.1489 0.1789 0.0212  -0.0222 0.0198  46  GLY   A C   
1220 C  C   B GLY   A 46  ? 0.1589 0.1423 0.1267 0.0261  -0.0211 0.0045  46  GLY   A C   
1221 O  O   A GLY   A 46  ? 0.1623 0.1603 0.2105 0.0186  -0.0374 -0.0073 46  GLY   A O   
1222 O  O   B GLY   A 46  ? 0.1597 0.1501 0.1357 0.0273  -0.0227 -0.0117 46  GLY   A O   
1229 N  N   A GLY   A 47  ? 0.1637 0.1487 0.1530 0.0196  -0.0185 0.0137  47  GLY   A N   
1230 N  N   B GLY   A 47  ? 0.1577 0.1381 0.1328 0.0258  -0.0238 0.0025  47  GLY   A N   
1231 C  CA  A GLY   A 47  ? 0.1657 0.1598 0.1479 0.0124  -0.0309 0.0066  47  GLY   A CA  
1232 C  CA  B GLY   A 47  ? 0.1575 0.1433 0.1370 0.0226  -0.0284 -0.0018 47  GLY   A CA  
1233 C  C   A GLY   A 47  ? 0.1627 0.1450 0.1589 0.0130  -0.0461 -0.0007 47  GLY   A C   
1234 C  C   B GLY   A 47  ? 0.1547 0.1427 0.1306 0.0226  -0.0199 -0.0170 47  GLY   A C   
1235 O  O   A GLY   A 47  ? 0.1596 0.1358 0.1766 0.0192  -0.0516 0.0100  47  GLY   A O   
1236 O  O   B GLY   A 47  ? 0.1563 0.1393 0.1314 0.0299  -0.0091 -0.0028 47  GLY   A O   
1243 N  N   A GLY   A 48  ? 0.1567 0.1446 0.1617 0.0141  -0.0491 -0.0058 48  GLY   A N   
1244 N  N   B GLY   A 48  ? 0.1547 0.1508 0.1557 0.0110  -0.0208 -0.0235 48  GLY   A N   
1245 C  CA  A GLY   A 48  ? 0.1432 0.1396 0.1817 0.0092  -0.0413 -0.0088 48  GLY   A CA  
1246 C  CA  B GLY   A 48  ? 0.1475 0.1484 0.1579 0.0056  -0.0136 -0.0206 48  GLY   A CA  
1247 C  C   A GLY   A 48  ? 0.1326 0.1381 0.1606 0.0060  -0.0105 -0.0038 48  GLY   A C   
1248 C  C   B GLY   A 48  ? 0.1399 0.1488 0.1489 0.0003  -0.0003 -0.0094 48  GLY   A C   
1249 O  O   A GLY   A 48  ? 0.1446 0.1370 0.1570 0.0047  -0.0080 -0.0053 48  GLY   A O   
1250 O  O   B GLY   A 48  ? 0.1452 0.1525 0.1460 -0.0041 0.0059  -0.0101 48  GLY   A O   
1257 N  N   A VAL   A 49  ? 0.1206 0.1337 0.1628 -0.0032 -0.0087 -0.0086 49  VAL   A N   
1258 N  N   B VAL   A 49  ? 0.1298 0.1432 0.1441 -0.0035 -0.0028 -0.0055 49  VAL   A N   
1259 C  CA  A VAL   A 49  ? 0.1402 0.1298 0.1576 -0.0065 0.0150  -0.0023 49  VAL   A CA  
1260 C  CA  B VAL   A 49  ? 0.1223 0.1374 0.1376 -0.0037 0.0015  0.0050  49  VAL   A CA  
1261 C  C   A VAL   A 49  ? 0.1385 0.1179 0.1232 0.0023  0.0131  -0.0005 49  VAL   A C   
1262 C  C   B VAL   A 49  ? 0.1150 0.1277 0.1228 0.0021  0.0103  0.0061  49  VAL   A C   
1263 O  O   A VAL   A 49  ? 0.1424 0.1244 0.1337 -0.0014 0.0090  -0.0073 49  VAL   A O   
1264 O  O   B VAL   A 49  ? 0.1088 0.1197 0.1236 0.0070  0.0178  0.0018  49  VAL   A O   
1265 C  CB  A VAL   A 49  ? 0.1566 0.1330 0.1743 -0.0085 0.0214  -0.0115 49  VAL   A CB  
1266 C  CB  B VAL   A 49  ? 0.1175 0.1324 0.1297 -0.0008 -0.0051 0.0065  49  VAL   A CB  
1267 C  CG1 A VAL   A 49  ? 0.1662 0.1301 0.1682 -0.0007 0.0258  0.0021  49  VAL   A CG1 
1268 C  CG1 B VAL   A 49  ? 0.1132 0.1307 0.1175 0.0101  -0.0051 0.0121  49  VAL   A CG1 
1269 C  CG2 A VAL   A 49  ? 0.1680 0.1420 0.2229 -0.0221 0.0174  -0.0096 49  VAL   A CG2 
1270 C  CG2 B VAL   A 49  ? 0.1194 0.1337 0.1336 -0.0044 -0.0023 0.0124  49  VAL   A CG2 
1289 N  N   A ALA   A 50  ? 0.1339 0.1174 0.1224 -0.0065 -0.0110 0.0074  50  ALA   A N   
1290 N  N   B ALA   A 50  ? 0.1174 0.1262 0.1152 0.0035  0.0086  0.0063  50  ALA   A N   
1291 C  CA  A ALA   A 50  ? 0.1270 0.1236 0.1288 -0.0097 -0.0065 0.0114  50  ALA   A CA  
1292 C  CA  B ALA   A 50  ? 0.1170 0.1293 0.1182 -0.0002 0.0083  0.0088  50  ALA   A CA  
1293 C  C   A ALA   A 50  ? 0.1215 0.1239 0.1168 -0.0133 -0.0033 0.0014  50  ALA   A C   
1294 C  C   B ALA   A 50  ? 0.1173 0.1259 0.1191 0.0044  0.0047  0.0037  50  ALA   A C   
1295 O  O   A ALA   A 50  ? 0.1229 0.1316 0.1332 -0.0098 -0.0077 0.0011  50  ALA   A O   
1296 O  O   B ALA   A 50  ? 0.1149 0.1251 0.1267 0.0168  0.0083  0.0016  50  ALA   A O   
1297 C  CB  A ALA   A 50  ? 0.1309 0.1256 0.1193 -0.0073 -0.0074 -0.0053 50  ALA   A CB  
1298 C  CB  B ALA   A 50  ? 0.1191 0.1334 0.1152 -0.0051 0.0172  -0.0018 50  ALA   A CB  
1309 N  N   . GLY   A 51  ? 0.1219 0.1261 0.1349 0.0060  -0.0061 0.0039  51  GLY   A N   
1310 C  CA  . GLY   A 51  ? 0.1412 0.1227 0.1416 0.0064  -0.0124 0.0055  51  GLY   A CA  
1311 C  C   . GLY   A 51  ? 0.1240 0.1322 0.1393 0.0044  -0.0086 -0.0079 51  GLY   A C   
1312 O  O   . GLY   A 51  ? 0.1285 0.1420 0.1538 0.0020  -0.0113 -0.0089 51  GLY   A O   
1317 N  N   . ALA   A 52  ? 0.1250 0.1419 0.1313 0.0031  -0.0040 -0.0120 52  ALA   A N   
1318 C  CA  . ALA   A 52  ? 0.1296 0.1553 0.1396 -0.0012 0.0018  -0.0133 52  ALA   A CA  
1319 C  C   . ALA   A 52  ? 0.1297 0.1490 0.1240 -0.0100 0.0083  -0.0100 52  ALA   A C   
1320 O  O   . ALA   A 52  ? 0.1360 0.1605 0.1417 -0.0056 0.0065  -0.0141 52  ALA   A O   
1321 C  CB  . ALA   A 52  ? 0.1404 0.1817 0.1673 -0.0036 -0.0021 -0.0066 52  ALA   A CB  
1327 N  N   A LEU   A 53  ? 0.1219 0.1411 0.1295 -0.0060 0.0059  -0.0083 53  LEU   A N   
1328 N  N   B LEU   A 53  ? 0.1267 0.1441 0.1219 -0.0051 0.0082  -0.0057 53  LEU   A N   
1329 C  CA  A LEU   A 53  ? 0.1400 0.1530 0.1241 -0.0054 0.0002  -0.0042 53  LEU   A CA  
1330 C  CA  B LEU   A 53  ? 0.1327 0.1462 0.1172 -0.0015 0.0072  -0.0023 53  LEU   A CA  
1331 C  C   A LEU   A 53  ? 0.1335 0.1489 0.1051 0.0079  0.0063  0.0006  53  LEU   A C   
1332 C  C   B LEU   A 53  ? 0.1336 0.1449 0.1025 0.0016  0.0095  -0.0046 53  LEU   A C   
1333 O  O   A LEU   A 53  ? 0.1486 0.1532 0.1257 -0.0072 0.0016  0.0034  53  LEU   A O   
1334 O  O   B LEU   A 53  ? 0.1424 0.1459 0.1026 -0.0092 0.0120  -0.0076 53  LEU   A O   
1335 C  CB  A LEU   A 53  ? 0.1529 0.1575 0.1195 -0.0141 -0.0041 0.0059  53  LEU   A CB  
1336 C  CB  B LEU   A 53  ? 0.1326 0.1423 0.1156 -0.0007 0.0065  0.0041  53  LEU   A CB  
1337 C  CG  A LEU   A 53  ? 0.1653 0.1591 0.1391 -0.0172 -0.0011 0.0052  53  LEU   A CG  
1338 C  CG  B LEU   A 53  ? 0.1289 0.1346 0.1070 0.0010  0.0045  0.0052  53  LEU   A CG  
1339 C  CD1 A LEU   A 53  ? 0.1810 0.1682 0.1336 -0.0050 0.0047  0.0037  53  LEU   A CD1 
1340 C  CD1 B LEU   A 53  ? 0.1392 0.1404 0.1142 0.0054  0.0065  0.0074  53  LEU   A CD1 
1341 C  CD2 A LEU   A 53  ? 0.1670 0.1717 0.1493 -0.0257 -0.0039 0.0192  53  LEU   A CD2 
1342 C  CD2 B LEU   A 53  ? 0.1250 0.1301 0.0990 0.0046  0.0117  0.0028  53  LEU   A CD2 
1365 N  N   . ASN   A 54  ? 0.1298 0.1394 0.1070 0.0024  -0.0034 0.0020  54  ASN   A N   
1366 C  CA  . ASN   A 54  ? 0.1186 0.1377 0.1282 -0.0026 -0.0038 -0.0043 54  ASN   A CA  
1367 C  C   . ASN   A 54  ? 0.1270 0.1395 0.1224 -0.0033 -0.0022 -0.0057 54  ASN   A C   
1368 O  O   . ASN   A 54  ? 0.1326 0.1434 0.1341 -0.0043 -0.0057 -0.0139 54  ASN   A O   
1369 C  CB  . ASN   A 54  ? 0.1156 0.1355 0.1355 -0.0071 -0.0069 -0.0003 54  ASN   A CB  
1370 C  CG  . ASN   A 54  ? 0.1260 0.1434 0.1318 0.0029  -0.0087 -0.0040 54  ASN   A CG  
1371 O  OD1 . ASN   A 54  ? 0.1233 0.1448 0.1361 -0.0024 -0.0078 0.0020  54  ASN   A OD1 
1372 N  ND2 . ASN   A 54  ? 0.1310 0.1499 0.1491 -0.0079 -0.0091 0.0103  54  ASN   A ND2 
1380 N  N   . LYS   A 55  ? 0.1335 0.1441 0.1293 -0.0023 -0.0040 -0.0113 55  LYS   A N   
1381 C  CA  . LYS   A 55  ? 0.1379 0.1518 0.1368 0.0060  -0.0114 -0.0160 55  LYS   A CA  
1382 C  C   . LYS   A 55  ? 0.1380 0.1572 0.1285 -0.0024 0.0037  -0.0231 55  LYS   A C   
1383 O  O   . LYS   A 55  ? 0.1506 0.1709 0.1429 0.0034  0.0002  -0.0292 55  LYS   A O   
1384 C  CB  . LYS   A 55  ? 0.1473 0.1558 0.1628 0.0124  -0.0093 -0.0192 55  LYS   A CB  
1385 C  CG  . LYS   A 55  ? 0.1636 0.1835 0.1805 0.0280  -0.0190 -0.0250 55  LYS   A CG  
1386 C  CD  . LYS   A 55  ? 0.1791 0.2191 0.1901 0.0390  -0.0077 -0.0252 55  LYS   A CD  
1387 C  CE  . LYS   A 55  ? 0.2015 0.2554 0.2085 0.0540  -0.0186 -0.0239 55  LYS   A CE  
1388 N  NZ  . LYS   A 55  ? 0.2115 0.2656 0.2207 0.0642  -0.0207 -0.0197 55  LYS   A NZ  
1402 N  N   . ALA   A 56  ? 0.1417 0.1651 0.1414 -0.0104 0.0036  -0.0221 56  ALA   A N   
1403 C  CA  . ALA   A 56  ? 0.1565 0.1862 0.1429 -0.0151 0.0013  -0.0256 56  ALA   A CA  
1404 C  C   . ALA   A 56  ? 0.1617 0.1932 0.1177 -0.0158 0.0075  -0.0323 56  ALA   A C   
1405 O  O   . ALA   A 56  ? 0.1674 0.2264 0.1330 -0.0016 0.0113  -0.0217 56  ALA   A O   
1406 C  CB  . ALA   A 56  ? 0.1603 0.2068 0.1512 -0.0208 0.0088  -0.0173 56  ALA   A CB  
1412 N  N   . THR   A 57  ? 0.1508 0.1740 0.1222 -0.0124 0.0116  -0.0219 57  THR   A N   
1413 C  CA  . THR   A 57  ? 0.1484 0.1700 0.1314 -0.0169 -0.0014 -0.0119 57  THR   A CA  
1414 C  C   . THR   A 57  ? 0.1469 0.1697 0.1458 -0.0112 -0.0046 -0.0186 57  THR   A C   
1415 O  O   . THR   A 57  ? 0.1495 0.1754 0.1614 -0.0081 -0.0168 -0.0251 57  THR   A O   
1416 C  CB  . THR   A 57  ? 0.1463 0.1708 0.1309 -0.0117 0.0033  -0.0111 57  THR   A CB  
1417 O  OG1 . THR   A 57  ? 0.1332 0.1611 0.1401 -0.0054 0.0010  -0.0069 57  THR   A OG1 
1418 C  CG2 . THR   A 57  ? 0.1517 0.1736 0.1295 -0.0079 -0.0020 -0.0031 57  THR   A CG2 
1426 N  N   . ASN   A 58  ? 0.1466 0.1703 0.1623 -0.0093 0.0017  -0.0347 58  ASN   A N   
1427 C  CA  . ASN   A 58  ? 0.1716 0.1633 0.1739 -0.0089 0.0129  -0.0455 58  ASN   A CA  
1428 C  C   . ASN   A 58  ? 0.1526 0.1526 0.1717 -0.0007 0.0031  -0.0233 58  ASN   A C   
1429 O  O   . ASN   A 58  ? 0.1537 0.1700 0.1750 -0.0175 -0.0055 -0.0330 58  ASN   A O   
1430 C  CB  . ASN   A 58  ? 0.2229 0.1833 0.2125 -0.0225 0.0411  -0.0610 58  ASN   A CB  
1431 C  CG  . ASN   A 58  ? 0.2725 0.2124 0.3022 -0.0221 0.0448  -0.0466 58  ASN   A CG  
1432 O  OD1 . ASN   A 58  ? 0.3024 0.2006 0.3500 0.0150  0.0811  -0.0345 58  ASN   A OD1 
1433 N  ND2 . ASN   A 58  ? 0.2844 0.2331 0.3347 -0.0280 0.0330  -0.0544 58  ASN   A ND2 
1440 N  N   . ASN   A 59  ? 0.1414 0.1430 0.1565 -0.0037 -0.0057 -0.0196 59  ASN   A N   
1441 C  CA  . ASN   A 59  ? 0.1382 0.1317 0.1480 -0.0016 -0.0077 -0.0125 59  ASN   A CA  
1442 C  C   . ASN   A 59  ? 0.1410 0.1430 0.1326 -0.0048 -0.0084 -0.0097 59  ASN   A C   
1443 O  O   . ASN   A 59  ? 0.1410 0.1436 0.1410 -0.0050 -0.0009 0.0011  59  ASN   A O   
1444 C  CB  . ASN   A 59  ? 0.1401 0.1352 0.1584 0.0028  -0.0203 -0.0183 59  ASN   A CB  
1445 C  CG  . ASN   A 59  ? 0.1415 0.1435 0.1568 -0.0029 -0.0258 -0.0012 59  ASN   A CG  
1446 O  OD1 . ASN   A 59  ? 0.1539 0.1464 0.1514 -0.0114 -0.0201 0.0029  59  ASN   A OD1 
1447 N  ND2 . ASN   A 59  ? 0.1511 0.1490 0.1674 -0.0121 -0.0205 0.0111  59  ASN   A ND2 
1454 N  N   . ALA   A 60  ? 0.1368 0.1475 0.1437 -0.0022 -0.0077 -0.0094 60  ALA   A N   
1455 C  CA  . ALA   A 60  ? 0.1310 0.1436 0.1493 0.0061  -0.0139 -0.0015 60  ALA   A CA  
1456 C  C   . ALA   A 60  ? 0.1352 0.1432 0.1533 -0.0004 -0.0081 -0.0072 60  ALA   A C   
1457 O  O   . ALA   A 60  ? 0.1298 0.1403 0.1662 -0.0034 -0.0155 -0.0102 60  ALA   A O   
1458 C  CB  . ALA   A 60  ? 0.1498 0.1508 0.1578 -0.0009 -0.0162 -0.0128 60  ALA   A CB  
1464 N  N   . MET   A 61  ? 0.1305 0.1360 0.1432 -0.0027 -0.0096 -0.0104 61  MET   A N   
1465 C  CA  . MET   A 61  ? 0.1281 0.1326 0.1317 -0.0049 0.0010  0.0030  61  MET   A CA  
1466 C  C   . MET   A 61  ? 0.1238 0.1258 0.1414 -0.0057 -0.0045 -0.0012 61  MET   A C   
1467 O  O   . MET   A 61  ? 0.1356 0.1264 0.1503 -0.0034 0.0059  -0.0013 61  MET   A O   
1468 C  CB  . MET   A 61  ? 0.1362 0.1341 0.1293 -0.0045 -0.0003 -0.0046 61  MET   A CB  
1469 C  CG  . MET   A 61  ? 0.1349 0.1433 0.1497 -0.0021 -0.0046 -0.0005 61  MET   A CG  
1470 S  SD  . MET   A 61  ? 0.1373 0.1434 0.1765 -0.0123 -0.0004 -0.0180 61  MET   A SD  
1471 C  CE  . MET   A 61  ? 0.1634 0.1539 0.1937 -0.0134 0.0199  -0.0162 61  MET   A CE  
1481 N  N   . GLN   A 62  ? 0.1234 0.1280 0.1443 -0.0039 -0.0032 -0.0016 62  GLN   A N   
1482 C  CA  . GLN   A 62  ? 0.1304 0.1256 0.1488 -0.0038 0.0013  0.0041  62  GLN   A CA  
1483 C  C   . GLN   A 62  ? 0.1293 0.1153 0.1527 -0.0041 0.0034  -0.0004 62  GLN   A C   
1484 O  O   . GLN   A 62  ? 0.1338 0.1353 0.1519 -0.0009 0.0049  0.0003  62  GLN   A O   
1485 C  CB  . GLN   A 62  ? 0.1268 0.1205 0.1580 -0.0020 -0.0006 0.0037  62  GLN   A CB  
1486 C  CG  . GLN   A 62  ? 0.1370 0.1201 0.1483 -0.0090 0.0013  0.0090  62  GLN   A CG  
1487 C  CD  . GLN   A 62  ? 0.1411 0.1251 0.1538 -0.0056 0.0041  0.0103  62  GLN   A CD  
1488 O  OE1 . GLN   A 62  ? 0.1409 0.1377 0.1572 -0.0039 0.0014  0.0076  62  GLN   A OE1 
1489 N  NE2 . GLN   A 62  ? 0.1547 0.1296 0.1615 0.0009  -0.0003 -0.0063 62  GLN   A NE2 
1498 N  N   . VAL   A 63  ? 0.1286 0.1272 0.1726 -0.0096 0.0061  -0.0183 63  VAL   A N   
1499 C  CA  . VAL   A 63  ? 0.1337 0.1397 0.1760 -0.0172 0.0042  -0.0113 63  VAL   A CA  
1500 C  C   . VAL   A 63  ? 0.1254 0.1422 0.1642 -0.0152 -0.0029 -0.0061 63  VAL   A C   
1501 O  O   . VAL   A 63  ? 0.1288 0.1391 0.1886 -0.0195 0.0011  -0.0047 63  VAL   A O   
1502 C  CB  . VAL   A 63  ? 0.1441 0.1584 0.2166 -0.0162 -0.0099 -0.0402 63  VAL   A CB  
1503 C  CG1 . VAL   A 63  ? 0.1551 0.1743 0.2537 -0.0193 -0.0109 -0.0625 63  VAL   A CG1 
1504 C  CG2 . VAL   A 63  ? 0.1517 0.1546 0.2343 -0.0089 0.0067  -0.0473 63  VAL   A CG2 
1514 N  N   . GLU   A 64  ? 0.1269 0.1437 0.1570 -0.0073 -0.0001 -0.0043 64  GLU   A N   
1515 C  CA  . GLU   A 64  ? 0.1234 0.1425 0.1605 -0.0070 -0.0046 0.0006  64  GLU   A CA  
1516 C  C   . GLU   A 64  ? 0.1255 0.1300 0.1593 -0.0074 0.0008  0.0004  64  GLU   A C   
1517 O  O   . GLU   A 64  ? 0.1323 0.1409 0.1653 -0.0018 0.0003  -0.0007 64  GLU   A O   
1518 C  CB  . GLU   A 64  ? 0.1301 0.1564 0.1718 -0.0081 0.0053  -0.0057 64  GLU   A CB  
1519 C  CG  . GLU   A 64  ? 0.1402 0.1608 0.1776 -0.0120 -0.0024 -0.0003 64  GLU   A CG  
1520 C  CD  . GLU   A 64  ? 0.1537 0.1657 0.1813 -0.0129 0.0071  -0.0044 64  GLU   A CD  
1521 O  OE1 . GLU   A 64  ? 0.1554 0.1748 0.2047 -0.0256 0.0152  -0.0031 64  GLU   A OE1 
1522 O  OE2 . GLU   A 64  ? 0.1712 0.1636 0.1828 -0.0244 -0.0051 0.0050  64  GLU   A OE2 
1529 N  N   . SER   A 65  ? 0.1218 0.1284 0.1598 -0.0015 -0.0007 0.0024  65  SER   A N   
1530 C  CA  . SER   A 65  ? 0.1287 0.1277 0.1513 -0.0057 -0.0057 -0.0070 65  SER   A CA  
1531 C  C   . SER   A 65  ? 0.1283 0.1346 0.1436 -0.0064 -0.0019 -0.0014 65  SER   A C   
1532 O  O   . SER   A 65  ? 0.1353 0.1376 0.1695 0.0010  0.0139  -0.0048 65  SER   A O   
1533 C  CB  . SER   A 65  ? 0.1276 0.1350 0.1502 -0.0100 0.0001  0.0055  65  SER   A CB  
1534 O  OG  . SER   A 65  ? 0.1262 0.1421 0.1588 -0.0093 -0.0031 0.0110  65  SER   A OG  
1540 N  N   . ASP   A 66  ? 0.1297 0.1305 0.1495 -0.0090 0.0137  0.0008  66  ASP   A N   
1541 C  CA  . ASP   A 66  ? 0.1390 0.1405 0.1669 0.0001  0.0114  0.0145  66  ASP   A CA  
1542 C  C   . ASP   A 66  ? 0.1387 0.1471 0.1673 -0.0048 0.0090  0.0150  66  ASP   A C   
1543 O  O   . ASP   A 66  ? 0.1453 0.1571 0.1821 -0.0012 0.0219  0.0230  66  ASP   A O   
1544 C  CB  . ASP   A 66  ? 0.1444 0.1570 0.2003 0.0039  0.0163  0.0337  66  ASP   A CB  
1545 C  CG  . ASP   A 66  ? 0.1674 0.1661 0.2364 0.0003  0.0070  0.0499  66  ASP   A CG  
1546 O  OD1 . ASP   A 66  ? 0.1686 0.1912 0.2131 -0.0077 -0.0030 0.0494  66  ASP   A OD1 
1547 O  OD2 . ASP   A 66  ? 0.1844 0.1781 0.3189 0.0208  -0.0162 0.0288  66  ASP   A OD2 
1552 N  N   . ASP   A 67  ? 0.1282 0.1450 0.1841 -0.0044 0.0082  0.0165  67  ASP   A N   
1553 C  CA  . ASP   A 67  ? 0.1265 0.1622 0.1983 -0.0048 0.0025  0.0209  67  ASP   A CA  
1554 C  C   . ASP   A 67  ? 0.1316 0.1598 0.1901 0.0007  0.0074  0.0231  67  ASP   A C   
1555 O  O   . ASP   A 67  ? 0.1319 0.1599 0.2102 0.0047  0.0244  0.0354  67  ASP   A O   
1556 C  CB  . ASP   A 67  ? 0.1418 0.1675 0.2278 -0.0092 -0.0111 0.0285  67  ASP   A CB  
1557 C  CG  . ASP   A 67  ? 0.1384 0.1820 0.2685 -0.0075 -0.0280 0.0423  67  ASP   A CG  
1558 O  OD1 . ASP   A 67  ? 0.1423 0.1992 0.3613 -0.0160 -0.0396 0.0532  67  ASP   A OD1 
1559 O  OD2 . ASP   A 67  ? 0.1443 0.1904 0.2418 0.0051  -0.0210 0.0273  67  ASP   A OD2 
1564 N  N   . TYR   A 68  ? 0.1340 0.1450 0.1907 0.0024  0.0144  0.0270  68  TYR   A N   
1565 C  CA  . TYR   A 68  ? 0.1452 0.1461 0.1766 0.0004  0.0225  0.0252  68  TYR   A CA  
1566 C  C   . TYR   A 68  ? 0.1361 0.1451 0.1785 -0.0032 0.0238  0.0207  68  TYR   A C   
1567 O  O   . TYR   A 68  ? 0.1426 0.1450 0.1931 0.0090  0.0306  0.0206  68  TYR   A O   
1568 C  CB  . TYR   A 68  ? 0.1482 0.1372 0.1889 0.0071  0.0395  0.0238  68  TYR   A CB  
1569 C  CG  . TYR   A 68  ? 0.1510 0.1551 0.2219 0.0058  0.0572  0.0287  68  TYR   A CG  
1570 C  CD1 . TYR   A 68  ? 0.1634 0.1668 0.2600 -0.0197 0.0460  -0.0118 68  TYR   A CD1 
1571 C  CD2 . TYR   A 68  ? 0.1720 0.1628 0.2662 0.0154  0.0619  0.0287  68  TYR   A CD2 
1572 C  CE1 . TYR   A 68  ? 0.1688 0.1772 0.3043 -0.0216 0.0609  -0.0237 68  TYR   A CE1 
1573 C  CE2 . TYR   A 68  ? 0.1728 0.1677 0.2898 0.0044  0.0720  0.0048  68  TYR   A CE2 
1574 C  CZ  . TYR   A 68  ? 0.1765 0.1769 0.3130 -0.0145 0.0563  -0.0247 68  TYR   A CZ  
1575 O  OH  . TYR   A 68  ? 0.2021 0.1773 0.3400 -0.0127 0.0236  -0.0487 68  TYR   A OH  
1585 N  N   . ILE   A 69  ? 0.1315 0.1361 0.1748 -0.0020 0.0187  0.0220  69  ILE   A N   
1586 C  CA  . ILE   A 69  ? 0.1368 0.1419 0.1709 -0.0005 0.0128  0.0115  69  ILE   A CA  
1587 C  C   . ILE   A 69  ? 0.1413 0.1460 0.1581 -0.0017 0.0186  0.0129  69  ILE   A C   
1588 O  O   . ILE   A 69  ? 0.1448 0.1518 0.1600 -0.0013 0.0240  0.0173  69  ILE   A O   
1589 C  CB  . ILE   A 69  ? 0.1469 0.1642 0.1805 -0.0001 0.0103  0.0019  69  ILE   A CB  
1590 C  CG1 . ILE   A 69  ? 0.1455 0.1677 0.1846 0.0021  0.0167  -0.0162 69  ILE   A CG1 
1591 C  CG2 . ILE   A 69  ? 0.1685 0.1863 0.1981 0.0088  0.0007  -0.0022 69  ILE   A CG2 
1592 C  CD1 . ILE   A 69  ? 0.1465 0.1761 0.2033 -0.0117 0.0173  -0.0157 69  ILE   A CD1 
1604 N  N   . ALA   A 70  ? 0.1464 0.1464 0.1691 -0.0102 0.0178  0.0144  70  ALA   A N   
1605 C  CA  . ALA   A 70  ? 0.1526 0.1564 0.1869 -0.0190 0.0267  0.0185  70  ALA   A CA  
1606 C  C   . ALA   A 70  ? 0.1520 0.1712 0.1784 -0.0161 0.0310  0.0202  70  ALA   A C   
1607 O  O   . ALA   A 70  ? 0.1693 0.2049 0.2064 0.0028  0.0473  0.0419  70  ALA   A O   
1608 C  CB  . ALA   A 70  ? 0.1486 0.1539 0.2195 -0.0204 0.0144  0.0142  70  ALA   A CB  
1614 N  N   . THR   A 71  ? 0.1448 0.1658 0.1799 -0.0067 0.0209  0.0238  71  THR   A N   
1615 C  CA  . THR   A 71  ? 0.1560 0.1832 0.2053 0.0052  0.0214  0.0213  71  THR   A CA  
1616 C  C   . THR   A 71  ? 0.1485 0.1781 0.2210 0.0098  0.0388  0.0188  71  THR   A C   
1617 O  O   . THR   A 71  ? 0.1527 0.1999 0.2720 0.0065  0.0484  -0.0052 71  THR   A O   
1618 C  CB  . THR   A 71  ? 0.1831 0.2026 0.2285 0.0120  -0.0188 0.0353  71  THR   A CB  
1619 O  OG1 . THR   A 71  ? 0.2068 0.2238 0.2359 0.0059  -0.0396 0.0332  71  THR   A OG1 
1620 C  CG2 . THR   A 71  ? 0.1938 0.2191 0.2618 0.0185  -0.0233 0.0472  71  THR   A CG2 
1628 N  N   . ASN   A 72  ? 0.1498 0.1539 0.2013 0.0095  0.0316  0.0263  72  ASN   A N   
1629 C  CA  . ASN   A 72  ? 0.1506 0.1623 0.2155 0.0140  0.0355  0.0223  72  ASN   A CA  
1630 C  C   . ASN   A 72  ? 0.1598 0.1623 0.2045 0.0063  0.0498  0.0128  72  ASN   A C   
1631 O  O   . ASN   A 72  ? 0.1759 0.1639 0.2347 0.0142  0.0451  -0.0015 72  ASN   A O   
1632 C  CB  . ASN   A 72  ? 0.1684 0.1708 0.2188 0.0149  0.0405  0.0264  72  ASN   A CB  
1633 C  CG  . ASN   A 72  ? 0.1889 0.1813 0.2225 0.0198  0.0335  0.0300  72  ASN   A CG  
1634 O  OD1 . ASN   A 72  ? 0.2092 0.2125 0.2422 0.0204  0.0445  0.0321  72  ASN   A OD1 
1635 N  ND2 . ASN   A 72  ? 0.2039 0.1813 0.2321 0.0479  0.0039  0.0161  72  ASN   A ND2 
1642 N  N   . GLY   A 73  ? 0.1589 0.1606 0.1836 0.0010  0.0419  0.0109  73  GLY   A N   
1643 C  CA  . GLY   A 73  ? 0.1664 0.1531 0.1730 -0.0081 0.0417  0.0085  73  GLY   A CA  
1644 C  C   . GLY   A 73  ? 0.1642 0.1461 0.1695 -0.0025 0.0459  0.0211  73  GLY   A C   
1645 O  O   . GLY   A 73  ? 0.1603 0.1545 0.1919 0.0083  0.0305  0.0298  73  GLY   A O   
1649 N  N   . PRO   A 74  ? 0.1728 0.1462 0.1701 -0.0124 0.0489  0.0175  74  PRO   A N   
1650 C  CA  . PRO   A 74  ? 0.1709 0.1455 0.1877 -0.0044 0.0455  0.0189  74  PRO   A CA  
1651 C  C   . PRO   A 74  ? 0.1650 0.1271 0.1832 -0.0074 0.0341  0.0098  74  PRO   A C   
1652 O  O   . PRO   A 74  ? 0.1713 0.1357 0.2070 0.0003  0.0366  -0.0042 74  PRO   A O   
1653 C  CB  . PRO   A 74  ? 0.1826 0.1724 0.2046 0.0010  0.0459  0.0302  74  PRO   A CB  
1654 C  CG  . PRO   A 74  ? 0.2061 0.2063 0.2512 -0.0186 0.0293  0.0184  74  PRO   A CG  
1655 C  CD  . PRO   A 74  ? 0.1856 0.1774 0.1977 -0.0272 0.0346  0.0069  74  PRO   A CD  
1663 N  N   . LEU   A 75  ? 0.1632 0.1221 0.1644 -0.0025 0.0285  0.0047  75  LEU   A N   
1664 C  CA  . LEU   A 75  ? 0.1651 0.1228 0.1489 -0.0012 0.0109  0.0108  75  LEU   A CA  
1665 C  C   . LEU   A 75  ? 0.1748 0.1391 0.1445 0.0076  0.0111  0.0088  75  LEU   A C   
1666 O  O   . LEU   A 75  ? 0.2054 0.1560 0.1485 0.0135  0.0035  0.0063  75  LEU   A O   
1667 C  CB  . LEU   A 75  ? 0.1629 0.1352 0.1412 -0.0091 0.0118  0.0209  75  LEU   A CB  
1668 C  CG  . LEU   A 75  ? 0.1800 0.1715 0.1526 -0.0384 0.0032  0.0111  75  LEU   A CG  
1669 C  CD1 . LEU   A 75  ? 0.1909 0.2187 0.1639 -0.0427 0.0077  -0.0057 75  LEU   A CD1 
1670 C  CD2 . LEU   A 75  ? 0.2111 0.2097 0.2124 -0.0145 0.0055  0.0162  75  LEU   A CD2 
1682 N  N   . LYS   A 76  ? 0.1737 0.1369 0.1574 -0.0046 0.0132  0.0008  76  LYS   A N   
1683 C  CA  . LYS   A 76  ? 0.1700 0.1630 0.1646 -0.0063 0.0169  -0.0133 76  LYS   A CA  
1684 C  C   . LYS   A 76  ? 0.1652 0.1453 0.1367 -0.0033 0.0125  0.0078  76  LYS   A C   
1685 O  O   . LYS   A 76  ? 0.1682 0.1368 0.1395 -0.0009 0.0143  0.0149  76  LYS   A O   
1686 C  CB  . LYS   A 76  ? 0.1703 0.1832 0.2132 0.0060  0.0174  -0.0387 76  LYS   A CB  
1687 C  CG  . LYS   A 76  ? 0.1809 0.1796 0.2632 0.0094  0.0117  -0.0305 76  LYS   A CG  
1688 C  CD  . LYS   A 76  ? 0.1901 0.1787 0.3095 0.0096  -0.0009 -0.0397 76  LYS   A CD  
1689 C  CE  . LYS   A 76  ? 0.2088 0.1991 0.3641 -0.0016 0.0075  -0.0491 76  LYS   A CE  
1690 N  NZ  . LYS   A 76  ? 0.2048 0.1891 0.3986 -0.0177 0.0069  -0.0588 76  LYS   A NZ  
1704 N  N   . VAL   A 77  ? 0.1767 0.1514 0.1341 -0.0004 0.0304  0.0123  77  VAL   A N   
1705 C  CA  . VAL   A 77  ? 0.1721 0.1517 0.1380 0.0015  0.0207  0.0130  77  VAL   A CA  
1706 C  C   . VAL   A 77  ? 0.1624 0.1466 0.1392 0.0032  0.0128  0.0033  77  VAL   A C   
1707 O  O   . VAL   A 77  ? 0.1720 0.1494 0.1372 0.0096  0.0348  -0.0064 77  VAL   A O   
1708 C  CB  . VAL   A 77  ? 0.1824 0.1655 0.1390 0.0044  0.0098  0.0161  77  VAL   A CB  
1709 C  CG1 . VAL   A 77  ? 0.1815 0.1839 0.1627 0.0138  -0.0028 0.0065  77  VAL   A CG1 
1710 C  CG2 . VAL   A 77  ? 0.2136 0.1781 0.1651 0.0006  0.0017  0.0148  77  VAL   A CG2 
1720 N  N   . GLY   A 78  ? 0.1599 0.1361 0.1448 0.0030  0.0225  0.0071  78  GLY   A N   
1721 C  CA  . GLY   A 78  ? 0.1609 0.1330 0.1458 -0.0026 0.0276  0.0109  78  GLY   A CA  
1722 C  C   . GLY   A 78  ? 0.1474 0.1349 0.1462 0.0038  0.0278  0.0149  78  GLY   A C   
1723 O  O   . GLY   A 78  ? 0.1482 0.1435 0.1580 0.0016  0.0224  0.0227  78  GLY   A O   
1727 N  N   . GLY   A 79  ? 0.1545 0.1309 0.1335 0.0021  0.0141  0.0119  79  GLY   A N   
1728 C  CA  . GLY   A 79  ? 0.1497 0.1357 0.1477 -0.0007 0.0181  0.0148  79  GLY   A CA  
1729 C  C   . GLY   A 79  ? 0.1370 0.1288 0.1365 -0.0034 0.0146  0.0073  79  GLY   A C   
1730 O  O   . GLY   A 79  ? 0.1386 0.1411 0.1590 0.0183  0.0158  0.0057  79  GLY   A O   
1734 N  N   . SER   A 80  ? 0.1326 0.1460 0.1568 -0.0011 0.0169  0.0007  80  SER   A N   
1735 C  CA  . SER   A 80  ? 0.1310 0.1356 0.1477 -0.0066 0.0060  0.0057  80  SER   A CA  
1736 C  C   . SER   A 80  ? 0.1319 0.1322 0.1504 -0.0062 0.0109  0.0130  80  SER   A C   
1737 O  O   . SER   A 80  ? 0.1339 0.1541 0.1925 0.0053  0.0184  -0.0007 80  SER   A O   
1738 C  CB  . SER   A 80  ? 0.1447 0.1363 0.1776 -0.0032 0.0120  -0.0024 80  SER   A CB  
1739 O  OG  . SER   A 80  ? 0.1687 0.1386 0.2269 0.0040  -0.0042 0.0251  80  SER   A OG  
1745 N  N   . CYS   A 81  ? 0.1257 0.1332 0.1519 -0.0021 0.0016  0.0136  81  CYS   A N   
1746 C  CA  . CYS   A 81  ? 0.1256 0.1407 0.1422 -0.0078 -0.0083 0.0199  81  CYS   A CA  
1747 C  C   . CYS   A 81  ? 0.1319 0.1431 0.1329 -0.0100 -0.0018 0.0301  81  CYS   A C   
1748 O  O   . CYS   A 81  ? 0.1278 0.1670 0.1594 -0.0012 0.0046  0.0338  81  CYS   A O   
1749 C  CB  . CYS   A 81  ? 0.1382 0.1505 0.1592 -0.0121 0.0001  0.0204  81  CYS   A CB  
1750 S  SG  . CYS   A 81  ? 0.1474 0.1402 0.1588 -0.0158 0.0017  0.0144  81  CYS   A SG  
1756 N  N   . VAL   A 82  ? 0.1344 0.1465 0.1391 -0.0022 -0.0117 0.0205  82  VAL   A N   
1757 C  CA  . VAL   A 82  ? 0.1412 0.1550 0.1420 -0.0025 -0.0102 0.0292  82  VAL   A CA  
1758 C  C   . VAL   A 82  ? 0.1369 0.1606 0.1575 -0.0051 -0.0139 0.0292  82  VAL   A C   
1759 O  O   . VAL   A 82  ? 0.1322 0.1603 0.1856 -0.0062 -0.0067 -0.0008 82  VAL   A O   
1760 C  CB  . VAL   A 82  ? 0.1701 0.1683 0.1561 -0.0021 -0.0036 0.0250  82  VAL   A CB  
1761 C  CG1 . VAL   A 82  ? 0.1860 0.1798 0.1876 0.0031  0.0006  0.0227  82  VAL   A CG1 
1762 C  CG2 . VAL   A 82  ? 0.1805 0.1726 0.1859 -0.0033 -0.0121 0.0267  82  VAL   A CG2 
1772 N  N   . LEU   A 83  ? 0.1341 0.1559 0.1466 -0.0088 -0.0120 0.0174  83  LEU   A N   
1773 C  CA  . LEU   A 83  ? 0.1416 0.1542 0.1375 -0.0138 -0.0123 0.0114  83  LEU   A CA  
1774 C  C   . LEU   A 83  ? 0.1461 0.1600 0.1362 -0.0142 -0.0216 0.0189  83  LEU   A C   
1775 O  O   . LEU   A 83  ? 0.1540 0.1593 0.1454 -0.0193 -0.0125 0.0186  83  LEU   A O   
1776 C  CB  . LEU   A 83  ? 0.1424 0.1547 0.1536 -0.0134 -0.0085 0.0168  83  LEU   A CB  
1777 C  CG  . LEU   A 83  ? 0.1593 0.1712 0.1550 -0.0144 0.0018  0.0035  83  LEU   A CG  
1778 C  CD1 . LEU   A 83  ? 0.1723 0.1726 0.1633 -0.0260 0.0070  0.0205  83  LEU   A CD1 
1779 C  CD2 . LEU   A 83  ? 0.1538 0.1854 0.1660 -0.0099 0.0121  0.0225  83  LEU   A CD2 
1791 N  N   . SER   A 84  ? 0.1570 0.1640 0.1325 -0.0192 -0.0145 0.0182  84  SER   A N   
1792 C  CA  . SER   A 84  ? 0.1648 0.1707 0.1200 -0.0141 -0.0128 0.0194  84  SER   A CA  
1793 C  C   . SER   A 84  ? 0.1678 0.1641 0.1246 -0.0212 -0.0003 0.0176  84  SER   A C   
1794 O  O   . SER   A 84  ? 0.1657 0.1792 0.1222 -0.0172 -0.0108 0.0128  84  SER   A O   
1795 C  CB  . SER   A 84  ? 0.1664 0.1909 0.1367 -0.0125 -0.0057 0.0066  84  SER   A CB  
1796 O  OG  . SER   A 84  ? 0.1688 0.2102 0.1534 -0.0131 -0.0198 -0.0076 84  SER   A OG  
1802 N  N   . GLY   A 85  ? 0.1799 0.1814 0.1244 -0.0230 0.0011  0.0099  85  GLY   A N   
1803 C  CA  . GLY   A 85  ? 0.1832 0.1894 0.1450 -0.0281 0.0112  0.0015  85  GLY   A CA  
1804 C  C   . GLY   A 85  ? 0.1769 0.1904 0.1291 -0.0195 -0.0116 0.0030  85  GLY   A C   
1805 O  O   . GLY   A 85  ? 0.1795 0.1994 0.1423 -0.0296 0.0043  -0.0143 85  GLY   A O   
1809 N  N   . HIS   A 86  ? 0.1764 0.1848 0.1218 -0.0200 -0.0113 0.0022  86  HIS   A N   
1810 C  CA  . HIS   A 86  ? 0.1958 0.1921 0.1210 -0.0231 -0.0024 0.0037  86  HIS   A CA  
1811 C  C   . HIS   A 86  ? 0.2144 0.2040 0.1119 -0.0254 -0.0121 0.0011  86  HIS   A C   
1812 O  O   . HIS   A 86  ? 0.2233 0.2276 0.1227 -0.0205 -0.0023 0.0038  86  HIS   A O   
1813 C  CB  . HIS   A 86  ? 0.1955 0.1838 0.1255 -0.0174 0.0024  0.0092  86  HIS   A CB  
1814 C  CG  . HIS   A 86  ? 0.1880 0.1840 0.1246 -0.0105 0.0003  0.0140  86  HIS   A CG  
1815 N  ND1 . HIS   A 86  ? 0.1961 0.1823 0.1619 -0.0227 0.0031  0.0067  86  HIS   A ND1 
1816 C  CD2 . HIS   A 86  ? 0.1918 0.1802 0.1224 0.0054  0.0108  0.0144  86  HIS   A CD2 
1817 C  CE1 . HIS   A 86  ? 0.1913 0.1829 0.1462 -0.0104 0.0190  0.0053  86  HIS   A CE1 
1818 N  NE2 . HIS   A 86  ? 0.1906 0.1785 0.1404 0.0063  0.0169  0.0207  86  HIS   A NE2 
1826 N  N   . ASN   A 87  ? 0.2270 0.2146 0.1326 -0.0201 0.0141  -0.0086 87  ASN   A N   
1827 C  CA  . ASN   A 87  ? 0.2458 0.2255 0.1366 -0.0185 0.0380  -0.0147 87  ASN   A CA  
1828 C  C   . ASN   A 87  ? 0.2474 0.2408 0.1694 -0.0276 0.0568  -0.0028 87  ASN   A C   
1829 O  O   . ASN   A 87  ? 0.2744 0.2586 0.2184 -0.0425 0.0849  -0.0184 87  ASN   A O   
1830 C  CB  . ASN   A 87  ? 0.2604 0.2304 0.1442 -0.0096 0.0416  -0.0123 87  ASN   A CB  
1831 C  CG  . ASN   A 87  ? 0.2736 0.2410 0.1504 0.0003  0.0504  -0.0079 87  ASN   A CG  
1832 O  OD1 . ASN   A 87  ? 0.2912 0.2406 0.1568 0.0168  0.0487  0.0077  87  ASN   A OD1 
1833 N  ND2 . ASN   A 87  ? 0.2772 0.2654 0.1605 -0.0007 0.0443  -0.0048 87  ASN   A ND2 
1840 N  N   . LEU   A 88  ? 0.2203 0.2291 0.1635 -0.0304 0.0299  0.0115  88  LEU   A N   
1841 C  CA  . LEU   A 88  ? 0.2021 0.2306 0.1767 -0.0377 0.0267  0.0240  88  LEU   A CA  
1842 C  C   . LEU   A 88  ? 0.1960 0.2340 0.1589 -0.0373 0.0307  0.0336  88  LEU   A C   
1843 O  O   . LEU   A 88  ? 0.2016 0.2387 0.2043 -0.0344 0.0330  0.0492  88  LEU   A O   
1844 C  CB  . LEU   A 88  ? 0.2050 0.2360 0.1928 -0.0426 -0.0106 0.0394  88  LEU   A CB  
1845 C  CG  . LEU   A 88  ? 0.2225 0.2486 0.2170 -0.0385 -0.0213 0.0370  88  LEU   A CG  
1846 C  CD1 . LEU   A 88  ? 0.2361 0.2560 0.2107 -0.0382 -0.0197 0.0222  88  LEU   A CD1 
1847 C  CD2 . LEU   A 88  ? 0.2330 0.2588 0.2614 -0.0312 -0.0196 0.0217  88  LEU   A CD2 
1859 N  N   . ALA   A 89  ? 0.1959 0.2239 0.1382 -0.0334 0.0200  0.0113  89  ALA   A N   
1860 C  CA  . ALA   A 89  ? 0.2026 0.2205 0.1314 -0.0260 0.0070  0.0214  89  ALA   A CA  
1861 C  C   . ALA   A 89  ? 0.2117 0.2203 0.1390 -0.0219 -0.0088 0.0170  89  ALA   A C   
1862 O  O   . ALA   A 89  ? 0.2119 0.2167 0.1711 -0.0325 -0.0164 -0.0096 89  ALA   A O   
1863 C  CB  . ALA   A 89  ? 0.1943 0.2175 0.1218 -0.0221 0.0055  0.0297  89  ALA   A CB  
1869 N  N   . LYS   A 90  ? 0.2219 0.2362 0.1441 -0.0352 -0.0258 0.0176  90  LYS   A N   
1870 C  CA  . LYS   A 90  ? 0.2326 0.2489 0.1387 -0.0272 -0.0386 0.0271  90  LYS   A CA  
1871 C  C   . LYS   A 90  ? 0.2075 0.2292 0.1363 -0.0295 -0.0396 0.0160  90  LYS   A C   
1872 O  O   . LYS   A 90  ? 0.2122 0.2479 0.1722 -0.0332 -0.0437 -0.0012 90  LYS   A O   
1873 C  CB  . LYS   A 90  ? 0.2616 0.2885 0.1780 -0.0223 -0.0485 0.0538  90  LYS   A CB  
1874 C  CG  . LYS   A 90  ? 0.3037 0.3229 0.2854 -0.0200 -0.0487 0.0578  90  LYS   A CG  
1875 C  CD  . LYS   A 90  ? 0.3513 0.3633 0.3947 -0.0241 -0.0295 0.0575  90  LYS   A CD  
1876 C  CE  . LYS   A 90  ? 0.3894 0.4001 0.4765 -0.0274 -0.0142 0.0494  90  LYS   A CE  
1877 N  NZ  . LYS   A 90  ? 0.4029 0.4119 0.5309 -0.0297 -0.0048 0.0422  90  LYS   A NZ  
1891 N  N   . HIS   A 91  ? 0.1921 0.2036 0.1154 -0.0246 -0.0422 0.0241  91  HIS   A N   
1892 C  CA  . HIS   A 91  ? 0.1836 0.1841 0.1273 -0.0190 -0.0353 0.0179  91  HIS   A CA  
1893 C  C   . HIS   A 91  ? 0.1633 0.1734 0.1094 -0.0165 -0.0217 0.0275  91  HIS   A C   
1894 O  O   . HIS   A 91  ? 0.1565 0.1876 0.1281 -0.0276 -0.0074 0.0243  91  HIS   A O   
1895 C  CB  . HIS   A 91  ? 0.2027 0.2097 0.1736 0.0033  -0.0498 0.0209  91  HIS   A CB  
1896 C  CG  . HIS   A 91  ? 0.2464 0.2614 0.2526 0.0163  -0.0780 0.0081  91  HIS   A CG  
1897 N  ND1 . HIS   A 91  ? 0.2562 0.2888 0.2971 0.0228  -0.0937 -0.0141 91  HIS   A ND1 
1898 C  CD2 . HIS   A 91  ? 0.2710 0.2807 0.2771 0.0242  -0.0873 0.0173  91  HIS   A CD2 
1899 C  CE1 . HIS   A 91  ? 0.2669 0.2978 0.3083 0.0268  -0.0929 -0.0000 91  HIS   A CE1 
1900 N  NE2 . HIS   A 91  ? 0.2807 0.2970 0.3017 0.0303  -0.0951 0.0097  91  HIS   A NE2 
1908 N  N   . CYS   A 92  ? 0.1575 0.1676 0.1117 -0.0215 -0.0101 0.0262  92  CYS   A N   
1909 C  CA  . CYS   A 92  ? 0.1381 0.1569 0.1179 -0.0161 -0.0016 0.0222  92  CYS   A CA  
1910 C  C   . CYS   A 92  ? 0.1351 0.1531 0.1135 -0.0208 -0.0014 0.0172  92  CYS   A C   
1911 O  O   . CYS   A 92  ? 0.1395 0.1599 0.1417 -0.0238 -0.0070 0.0140  92  CYS   A O   
1912 C  CB  . CYS   A 92  ? 0.1461 0.1602 0.1452 -0.0051 -0.0048 0.0115  92  CYS   A CB  
1913 S  SG  . CYS   A 92  ? 0.1445 0.1461 0.1352 -0.0148 -0.0071 0.0127  92  CYS   A SG  
1919 N  N   . LEU   A 93  ? 0.1336 0.1409 0.1326 -0.0151 0.0039  0.0176  93  LEU   A N   
1920 C  CA  . LEU   A 93  ? 0.1208 0.1347 0.1313 -0.0093 0.0022  0.0166  93  LEU   A CA  
1921 C  C   . LEU   A 93  ? 0.1301 0.1264 0.1154 -0.0003 0.0053  0.0121  93  LEU   A C   
1922 O  O   . LEU   A 93  ? 0.1251 0.1342 0.1182 -0.0041 -0.0016 0.0149  93  LEU   A O   
1923 C  CB  . LEU   A 93  ? 0.1345 0.1366 0.1392 -0.0048 -0.0034 0.0259  93  LEU   A CB  
1924 C  CG  . LEU   A 93  ? 0.1397 0.1369 0.1501 -0.0030 0.0014  0.0274  93  LEU   A CG  
1925 C  CD1 . LEU   A 93  ? 0.1438 0.1460 0.1746 0.0035  0.0142  0.0186  93  LEU   A CD1 
1926 C  CD2 . LEU   A 93  ? 0.1547 0.1379 0.1674 -0.0097 -0.0071 0.0130  93  LEU   A CD2 
1938 N  N   . HIS   A 94  ? 0.1190 0.1232 0.1234 -0.0000 0.0097  0.0177  94  HIS   A N   
1939 C  CA  . HIS   A 94  ? 0.1175 0.1293 0.1242 -0.0073 0.0006  0.0140  94  HIS   A CA  
1940 C  C   . HIS   A 94  ? 0.1224 0.1202 0.1385 -0.0084 0.0013  0.0078  94  HIS   A C   
1941 O  O   . HIS   A 94  ? 0.1225 0.1417 0.1689 0.0004  0.0046  -0.0068 94  HIS   A O   
1942 C  CB  . HIS   A 94  ? 0.1183 0.1284 0.1367 -0.0052 -0.0017 0.0094  94  HIS   A CB  
1943 C  CG  . HIS   A 94  ? 0.1259 0.1268 0.1251 -0.0066 -0.0027 0.0134  94  HIS   A CG  
1944 N  ND1 . HIS   A 94  ? 0.1236 0.1224 0.1279 -0.0037 -0.0049 0.0143  94  HIS   A ND1 
1945 C  CD2 . HIS   A 94  ? 0.1305 0.1415 0.1429 -0.0042 -0.0044 0.0051  94  HIS   A CD2 
1946 C  CE1 . HIS   A 94  ? 0.1289 0.1309 0.1275 -0.0105 -0.0129 0.0087  94  HIS   A CE1 
1947 N  NE2 . HIS   A 94  ? 0.1326 0.1316 0.1390 -0.0102 -0.0051 0.0027  94  HIS   A NE2 
1955 N  N   . VAL   A 95  ? 0.1186 0.1199 0.1088 -0.0042 0.0071  0.0026  95  VAL   A N   
1956 C  CA  . VAL   A 95  ? 0.1276 0.1278 0.1194 -0.0089 0.0140  0.0102  95  VAL   A CA  
1957 C  C   . VAL   A 95  ? 0.1266 0.1172 0.1026 -0.0167 -0.0012 0.0025  95  VAL   A C   
1958 O  O   . VAL   A 95  ? 0.1273 0.1370 0.1191 0.0040  0.0058  0.0057  95  VAL   A O   
1959 C  CB  . VAL   A 95  ? 0.1244 0.1274 0.1344 -0.0116 0.0024  0.0084  95  VAL   A CB  
1960 C  CG1 . VAL   A 95  ? 0.1367 0.1358 0.1413 -0.0166 0.0036  -0.0030 95  VAL   A CG1 
1961 C  CG2 . VAL   A 95  ? 0.1314 0.1212 0.1405 -0.0126 0.0017  0.0152  95  VAL   A CG2 
1971 N  N   . VAL   A 96  ? 0.1311 0.1202 0.1012 -0.0037 0.0090  0.0043  96  VAL   A N   
1972 C  CA  . VAL   A 96  ? 0.1384 0.1252 0.1175 -0.0059 0.0129  0.0186  96  VAL   A CA  
1973 C  C   . VAL   A 96  ? 0.1379 0.1360 0.1214 -0.0021 0.0111  0.0132  96  VAL   A C   
1974 O  O   . VAL   A 96  ? 0.1443 0.1403 0.1481 -0.0048 0.0173  -0.0022 96  VAL   A O   
1975 C  CB  . VAL   A 96  ? 0.1428 0.1320 0.1299 -0.0043 0.0224  0.0134  96  VAL   A CB  
1976 C  CG1 . VAL   A 96  ? 0.1497 0.1372 0.1168 -0.0068 0.0136  0.0101  96  VAL   A CG1 
1977 C  CG2 . VAL   A 96  ? 0.1414 0.1395 0.1401 -0.0138 0.0127  0.0096  96  VAL   A CG2 
1987 N  N   . GLY   A 97  ? 0.1374 0.1363 0.1209 -0.0072 0.0066  0.0070  97  GLY   A N   
1988 C  CA  . GLY   A 97  ? 0.1489 0.1482 0.1175 -0.0116 0.0050  0.0079  97  GLY   A CA  
1989 C  C   . GLY   A 97  ? 0.1538 0.1599 0.1087 -0.0131 0.0075  0.0044  97  GLY   A C   
1990 O  O   . GLY   A 97  ? 0.1629 0.1600 0.1323 -0.0123 0.0042  0.0166  97  GLY   A O   
1994 N  N   . PRO   A 98  ? 0.1546 0.1592 0.1040 -0.0039 0.0011  0.0165  98  PRO   A N   
1995 C  CA  . PRO   A 98  ? 0.1674 0.1859 0.1193 -0.0135 0.0014  0.0069  98  PRO   A CA  
1996 C  C   . PRO   A 98  ? 0.1761 0.1971 0.1068 -0.0217 0.0023  0.0294  98  PRO   A C   
1997 O  O   . PRO   A 98  ? 0.1677 0.1739 0.1410 -0.0126 -0.0015 0.0255  98  PRO   A O   
1998 C  CB  . PRO   A 98  ? 0.1769 0.2014 0.1167 -0.0038 -0.0047 -0.0045 98  PRO   A CB  
1999 C  CG  . PRO   A 98  ? 0.1751 0.1845 0.1313 -0.0020 -0.0037 -0.0107 98  PRO   A CG  
2000 C  CD  . PRO   A 98  ? 0.1636 0.1651 0.1137 0.0018  0.0003  0.0012  98  PRO   A CD  
2008 N  N   A ASN   A 99  ? 0.1734 0.2253 0.1190 -0.0220 0.0019  0.0456  99  ASN   A N   
2009 N  N   B ASN   A 99  ? 0.1968 0.2002 0.1317 -0.0173 -0.0068 0.0391  99  ASN   A N   
2010 C  CA  A ASN   A 99  ? 0.1921 0.2418 0.1126 -0.0279 -0.0052 0.0652  99  ASN   A CA  
2011 C  CA  B ASN   A 99  ? 0.2239 0.1986 0.1489 -0.0169 -0.0155 0.0477  99  ASN   A CA  
2012 C  C   A ASN   A 99  ? 0.2049 0.2693 0.1075 -0.0457 -0.0061 0.0707  99  ASN   A C   
2013 C  C   B ASN   A 99  ? 0.2399 0.1998 0.1645 -0.0144 -0.0205 0.0343  99  ASN   A C   
2014 O  O   A ASN   A 99  ? 0.2146 0.2844 0.1247 -0.0507 -0.0178 0.0681  99  ASN   A O   
2015 O  O   B ASN   A 99  ? 0.2438 0.1877 0.1601 -0.0103 -0.0292 0.0115  99  ASN   A O   
2016 C  CB  A ASN   A 99  ? 0.1921 0.2311 0.1295 -0.0183 -0.0150 0.0636  99  ASN   A CB  
2017 C  CB  B ASN   A 99  ? 0.2339 0.1976 0.1634 -0.0212 -0.0197 0.0639  99  ASN   A CB  
2018 C  CG  A ASN   A 99  ? 0.1920 0.2270 0.1424 -0.0144 -0.0222 0.0486  99  ASN   A CG  
2019 C  CG  B ASN   A 99  ? 0.2428 0.1969 0.1745 -0.0259 -0.0187 0.0793  99  ASN   A CG  
2020 O  OD1 A ASN   A 99  ? 0.2059 0.2381 0.1397 -0.0068 -0.0166 0.0357  99  ASN   A OD1 
2021 O  OD1 B ASN   A 99  ? 0.2519 0.2040 0.1657 -0.0298 -0.0172 0.0835  99  ASN   A OD1 
2022 N  ND2 A ASN   A 99  ? 0.1908 0.2175 0.1684 -0.0089 -0.0198 0.0610  99  ASN   A ND2 
2023 N  ND2 B ASN   A 99  ? 0.2462 0.1975 0.1983 -0.0199 -0.0298 0.0656  99  ASN   A ND2 
2036 N  N   A VAL   A 100 ? 0.2197 0.2864 0.1158 -0.0637 -0.0268 0.0649  100 VAL   A N   
2037 N  N   B VAL   A 100 ? 0.2508 0.2151 0.1880 -0.0187 -0.0208 0.0379  100 VAL   A N   
2038 C  CA  A VAL   A 100 ? 0.2410 0.3054 0.1433 -0.0671 -0.0348 0.0580  100 VAL   A CA  
2039 C  CA  B VAL   A 100 ? 0.2592 0.2324 0.2103 -0.0212 -0.0182 0.0387  100 VAL   A CA  
2040 C  C   A VAL   A 100 ? 0.2479 0.3121 0.1367 -0.0712 -0.0455 0.0787  100 VAL   A C   
2041 C  C   B VAL   A 100 ? 0.2697 0.2354 0.2101 -0.0204 -0.0207 0.0489  100 VAL   A C   
2042 O  O   A VAL   A 100 ? 0.2541 0.3142 0.1657 -0.0663 -0.0180 0.0797  100 VAL   A O   
2043 O  O   B VAL   A 100 ? 0.2685 0.2266 0.2082 -0.0231 -0.0173 0.0491  100 VAL   A O   
2044 C  CB  A VAL   A 100 ? 0.2587 0.3131 0.1809 -0.0756 -0.0328 0.0457  100 VAL   A CB  
2045 C  CB  B VAL   A 100 ? 0.2598 0.2471 0.2333 -0.0205 -0.0170 0.0261  100 VAL   A CB  
2046 C  CG1 A VAL   A 100 ? 0.2608 0.3190 0.2037 -0.0801 -0.0248 0.0438  100 VAL   A CG1 
2047 C  CG1 B VAL   A 100 ? 0.2593 0.2520 0.2445 -0.0196 -0.0158 0.0235  100 VAL   A CG1 
2048 C  CG2 A VAL   A 100 ? 0.2711 0.3148 0.2008 -0.0790 -0.0318 0.0300  100 VAL   A CG2 
2049 C  CG2 B VAL   A 100 ? 0.2624 0.2534 0.2482 -0.0244 -0.0152 0.0192  100 VAL   A CG2 
2068 N  N   A ASN   A 101 ? 0.2579 0.3229 0.1654 -0.0793 -0.0553 0.0986  101 ASN   A N   
2069 N  N   B ASN   A 101 ? 0.2784 0.2427 0.2164 -0.0156 -0.0249 0.0544  101 ASN   A N   
2070 C  CA  A ASN   A 101 ? 0.2858 0.3348 0.1870 -0.0813 -0.0536 0.1195  101 ASN   A CA  
2071 C  CA  B ASN   A 101 ? 0.2846 0.2458 0.2200 -0.0092 -0.0262 0.0557  101 ASN   A CA  
2072 C  C   A ASN   A 101 ? 0.3096 0.3610 0.2173 -0.0884 -0.0255 0.1372  101 ASN   A C   
2073 C  C   B ASN   A 101 ? 0.2989 0.2554 0.2243 -0.0081 -0.0142 0.0696  101 ASN   A C   
2074 O  O   A ASN   A 101 ? 0.3257 0.3658 0.2681 -0.0820 -0.0205 0.1272  101 ASN   A O   
2075 O  O   B ASN   A 101 ? 0.3037 0.2529 0.2105 -0.0077 -0.0086 0.0864  101 ASN   A O   
2076 C  CB  A ASN   A 101 ? 0.2897 0.3229 0.1863 -0.0760 -0.0731 0.1158  101 ASN   A CB  
2077 C  CB  B ASN   A 101 ? 0.2759 0.2388 0.2165 -0.0061 -0.0304 0.0457  101 ASN   A CB  
2078 C  CG  A ASN   A 101 ? 0.2926 0.3151 0.1994 -0.0751 -0.0767 0.0879  101 ASN   A CG  
2079 C  CG  B ASN   A 101 ? 0.2686 0.2348 0.2181 -0.0045 -0.0298 0.0353  101 ASN   A CG  
2080 O  OD1 A ASN   A 101 ? 0.2971 0.3240 0.2247 -0.0619 -0.0723 0.0550  101 ASN   A OD1 
2081 O  OD1 B ASN   A 101 ? 0.2700 0.2343 0.2151 -0.0055 -0.0229 0.0282  101 ASN   A OD1 
2082 N  ND2 A ASN   A 101 ? 0.2908 0.3012 0.2024 -0.0838 -0.0697 0.0925  101 ASN   A ND2 
2083 N  ND2 B ASN   A 101 ? 0.2627 0.2312 0.2258 -0.0022 -0.0290 0.0267  101 ASN   A ND2 
2096 N  N   A LYS   A 102 ? 0.3123 0.3890 0.2384 -0.1029 -0.0073 0.1332  102 LYS   A N   
2097 N  N   B LYS   A 102 ? 0.3095 0.2698 0.2513 -0.0131 -0.0012 0.0615  102 LYS   A N   
2098 C  CA  A LYS   A 102 ? 0.3224 0.4121 0.2422 -0.1083 -0.0079 0.1226  102 LYS   A CA  
2099 C  CA  B LYS   A 102 ? 0.3197 0.2816 0.2599 -0.0193 0.0086  0.0572  102 LYS   A CA  
2100 C  C   A LYS   A 102 ? 0.3301 0.4315 0.2229 -0.1003 -0.0029 0.1071  102 LYS   A C   
2101 C  C   B LYS   A 102 ? 0.3182 0.2780 0.2340 -0.0264 0.0115  0.0767  102 LYS   A C   
2102 O  O   A LYS   A 102 ? 0.3353 0.4443 0.2329 -0.0970 0.0062  0.0952  102 LYS   A O   
2103 O  O   B LYS   A 102 ? 0.3185 0.2695 0.2067 -0.0334 0.0159  0.0964  102 LYS   A O   
2104 C  CB  A LYS   A 102 ? 0.3327 0.4178 0.2764 -0.1140 -0.0198 0.1108  102 LYS   A CB  
2105 C  CB  B LYS   A 102 ? 0.3312 0.2970 0.3018 -0.0228 0.0100  0.0323  102 LYS   A CB  
2106 C  CG  A LYS   A 102 ? 0.3430 0.4247 0.3080 -0.1155 -0.0316 0.0915  102 LYS   A CG  
2107 C  CG  B LYS   A 102 ? 0.3407 0.3094 0.3406 -0.0258 0.0088  0.0118  102 LYS   A CG  
2108 C  CD  A LYS   A 102 ? 0.3572 0.4324 0.3392 -0.1146 -0.0427 0.0698  102 LYS   A CD  
2109 C  CD  B LYS   A 102 ? 0.3495 0.3201 0.3758 -0.0283 0.0068  -0.0034 102 LYS   A CD  
2110 C  CE  A LYS   A 102 ? 0.3699 0.4383 0.3686 -0.1112 -0.0532 0.0543  102 LYS   A CE  
2111 C  CE  B LYS   A 102 ? 0.3555 0.3293 0.4011 -0.0302 0.0041  -0.0144 102 LYS   A CE  
2112 N  NZ  A LYS   A 102 ? 0.3765 0.4410 0.3798 -0.1105 -0.0557 0.0444  102 LYS   A NZ  
2113 N  NZ  B LYS   A 102 ? 0.3591 0.3348 0.4149 -0.0304 0.0034  -0.0181 102 LYS   A NZ  
2140 N  N   A GLY   A 103 ? 0.3333 0.4403 0.2316 -0.0900 -0.0106 0.0864  103 GLY   A N   
2141 N  N   B GLY   A 103 ? 0.3150 0.2840 0.2359 -0.0259 0.0045  0.0721  103 GLY   A N   
2142 C  CA  A GLY   A 103 ? 0.3370 0.4438 0.2179 -0.0761 -0.0081 0.0695  103 GLY   A CA  
2143 C  CA  B GLY   A 103 ? 0.3102 0.2866 0.2275 -0.0272 0.0036  0.0721  103 GLY   A CA  
2144 C  C   A GLY   A 103 ? 0.3394 0.4487 0.2250 -0.0641 0.0024  0.0543  103 GLY   A C   
2145 C  C   B GLY   A 103 ? 0.3059 0.2866 0.2134 -0.0277 0.0000  0.0690  103 GLY   A C   
2146 O  O   A GLY   A 103 ? 0.3526 0.4569 0.2471 -0.0598 0.0053  0.0459  103 GLY   A O   
2147 O  O   B GLY   A 103 ? 0.3046 0.2873 0.2061 -0.0309 -0.0010 0.0764  103 GLY   A O   
2154 N  N   A GLU   A 104 ? 0.3245 0.4394 0.1889 -0.0608 0.0080  0.0468  104 GLU   A N   
2155 N  N   B GLU   A 104 ? 0.3039 0.2875 0.2102 -0.0208 -0.0070 0.0558  104 GLU   A N   
2156 C  CA  A GLU   A 104 ? 0.3027 0.4242 0.1641 -0.0650 0.0113  0.0360  104 GLU   A CA  
2157 C  CA  B GLU   A 104 ? 0.2993 0.2875 0.2105 -0.0178 -0.0125 0.0420  104 GLU   A CA  
2158 C  C   A GLU   A 104 ? 0.3051 0.4322 0.1609 -0.0632 0.0172  0.0154  104 GLU   A C   
2159 C  C   B GLU   A 104 ? 0.2982 0.2886 0.2202 -0.0140 -0.0105 0.0279  104 GLU   A C   
2160 O  O   A GLU   A 104 ? 0.2963 0.4340 0.1807 -0.0665 0.0072  0.0155  104 GLU   A O   
2161 O  O   B GLU   A 104 ? 0.2941 0.2821 0.2177 -0.0135 -0.0113 0.0335  104 GLU   A O   
2162 C  CB  A GLU   A 104 ? 0.2742 0.3989 0.1366 -0.0718 0.0210  0.0548  104 GLU   A CB  
2163 C  CB  B GLU   A 104 ? 0.2946 0.2880 0.2068 -0.0174 -0.0152 0.0403  104 GLU   A CB  
2164 C  CG  A GLU   A 104 ? 0.2558 0.3766 0.1417 -0.0700 0.0132  0.0682  104 GLU   A CG  
2165 C  CG  B GLU   A 104 ? 0.2931 0.2915 0.2114 -0.0142 -0.0206 0.0377  104 GLU   A CG  
2166 C  CD  A GLU   A 104 ? 0.2328 0.3548 0.1468 -0.0701 0.0111  0.0733  104 GLU   A CD  
2167 C  CD  B GLU   A 104 ? 0.2902 0.2947 0.2137 -0.0107 -0.0232 0.0350  104 GLU   A CD  
2168 O  OE1 A GLU   A 104 ? 0.2105 0.3375 0.1205 -0.0652 0.0089  0.0649  104 GLU   A OE1 
2169 O  OE1 B GLU   A 104 ? 0.2895 0.2968 0.2199 -0.0080 -0.0255 0.0373  104 GLU   A OE1 
2170 O  OE2 A GLU   A 104 ? 0.2422 0.3511 0.1703 -0.0724 0.0060  0.0859  104 GLU   A OE2 
2171 O  OE2 B GLU   A 104 ? 0.2899 0.2954 0.2128 -0.0099 -0.0266 0.0319  104 GLU   A OE2 
2184 N  N   A ASP   A 105 ? 0.3173 0.4377 0.1776 -0.0563 0.0336  -0.0089 105 ASP   A N   
2185 N  N   B ASP   A 105 ? 0.3035 0.2984 0.2373 -0.0132 -0.0055 0.0083  105 ASP   A N   
2186 C  CA  A ASP   A 105 ? 0.3225 0.4372 0.2182 -0.0485 0.0435  -0.0368 105 ASP   A CA  
2187 C  CA  B ASP   A 105 ? 0.3074 0.3083 0.2572 -0.0097 0.0007  -0.0133 105 ASP   A CA  
2188 C  C   A ASP   A 105 ? 0.2898 0.4167 0.1830 -0.0577 0.0321  -0.0561 105 ASP   A C   
2189 C  C   B ASP   A 105 ? 0.3027 0.3107 0.2507 -0.0151 0.0041  -0.0163 105 ASP   A C   
2190 O  O   A ASP   A 105 ? 0.2674 0.3967 0.1367 -0.0565 0.0313  -0.0810 105 ASP   A O   
2191 O  O   B ASP   A 105 ? 0.2977 0.3111 0.2364 -0.0145 0.0050  -0.0186 105 ASP   A O   
2192 C  CB  A ASP   A 105 ? 0.3558 0.4598 0.2907 -0.0358 0.0548  -0.0446 105 ASP   A CB  
2193 C  CB  B ASP   A 105 ? 0.3150 0.3157 0.2817 -0.0026 0.0005  -0.0312 105 ASP   A CB  
2194 C  CG  A ASP   A 105 ? 0.3846 0.4758 0.3520 -0.0233 0.0580  -0.0536 105 ASP   A CG  
2195 C  CG  B ASP   A 105 ? 0.3216 0.3209 0.2998 0.0048  -0.0036 -0.0468 105 ASP   A CG  
2196 O  OD1 A ASP   A 105 ? 0.3937 0.4827 0.3650 -0.0214 0.0556  -0.0659 105 ASP   A OD1 
2197 O  OD1 B ASP   A 105 ? 0.3240 0.3204 0.2936 0.0059  -0.0086 -0.0552 105 ASP   A OD1 
2198 O  OD2 A ASP   A 105 ? 0.3983 0.4817 0.3873 -0.0193 0.0631  -0.0467 105 ASP   A OD2 
2199 O  OD2 B ASP   A 105 ? 0.3254 0.3252 0.3168 0.0056  -0.0084 -0.0478 105 ASP   A OD2 
2208 N  N   A ILE   A 106 ? 0.2736 0.4009 0.2048 -0.0640 0.0072  -0.0570 106 ILE   A N   
2209 N  N   B ILE   A 106 ? 0.3017 0.3113 0.2578 -0.0205 0.0019  -0.0178 106 ILE   A N   
2210 C  CA  A ILE   A 106 ? 0.2466 0.3847 0.2216 -0.0773 -0.0198 -0.0712 106 ILE   A CA  
2211 C  CA  B ILE   A 106 ? 0.2986 0.3124 0.2673 -0.0284 0.0002  -0.0229 106 ILE   A CA  
2212 C  C   A ILE   A 106 ? 0.2265 0.3587 0.2238 -0.0921 -0.0135 -0.0869 106 ILE   A C   
2213 C  C   B ILE   A 106 ? 0.2934 0.3043 0.2682 -0.0348 0.0071  -0.0261 106 ILE   A C   
2214 O  O   A ILE   A 106 ? 0.2003 0.3478 0.2303 -0.0996 0.0032  -0.0817 106 ILE   A O   
2215 O  O   B ILE   A 106 ? 0.2906 0.3025 0.2659 -0.0335 0.0088  -0.0269 106 ILE   A O   
2216 C  CB  A ILE   A 106 ? 0.2475 0.3947 0.2695 -0.0672 -0.0409 -0.0466 106 ILE   A CB  
2217 C  CB  B ILE   A 106 ? 0.3019 0.3224 0.2888 -0.0285 -0.0066 -0.0173 106 ILE   A CB  
2218 C  CG1 A ILE   A 106 ? 0.2334 0.3962 0.2972 -0.0526 -0.0460 -0.0228 106 ILE   A CG1 
2219 C  CG1 B ILE   A 106 ? 0.3000 0.3260 0.3012 -0.0260 -0.0081 -0.0089 106 ILE   A CG1 
2220 C  CG2 A ILE   A 106 ? 0.2571 0.3990 0.2811 -0.0675 -0.0442 -0.0471 106 ILE   A CG2 
2221 C  CG2 B ILE   A 106 ? 0.3050 0.3259 0.2943 -0.0288 -0.0088 -0.0182 106 ILE   A CG2 
2222 C  CD1 A ILE   A 106 ? 0.2307 0.3944 0.3156 -0.0383 -0.0311 -0.0088 106 ILE   A CD1 
2223 C  CD1 B ILE   A 106 ? 0.3002 0.3266 0.3062 -0.0230 -0.0052 -0.0040 106 ILE   A CD1 
2246 N  N   A GLN   A 107 ? 0.2478 0.3434 0.2392 -0.0875 -0.0051 -0.1045 107 GLN   A N   
2247 N  N   B GLN   A 107 ? 0.2919 0.2961 0.2803 -0.0408 0.0145  -0.0276 107 GLN   A N   
2248 C  CA  A GLN   A 107 ? 0.2750 0.3286 0.3213 -0.0687 0.0224  -0.0928 107 GLN   A CA  
2249 C  CA  B GLN   A 107 ? 0.2892 0.2877 0.3054 -0.0447 0.0246  -0.0317 107 GLN   A CA  
2250 C  C   A GLN   A 107 ? 0.2498 0.2782 0.3106 -0.0554 0.0503  -0.0707 107 GLN   A C   
2251 C  C   B GLN   A 107 ? 0.2594 0.2603 0.2861 -0.0488 0.0419  -0.0422 107 GLN   A C   
2252 O  O   A GLN   A 107 ? 0.2528 0.2747 0.3712 -0.0425 0.0652  -0.0691 107 GLN   A O   
2253 O  O   B GLN   A 107 ? 0.2648 0.2617 0.3139 -0.0472 0.0435  -0.0395 107 GLN   A O   
2254 C  CB  A GLN   A 107 ? 0.3206 0.3595 0.4147 -0.0700 0.0121  -0.0932 107 GLN   A CB  
2255 C  CB  B GLN   A 107 ? 0.3132 0.3049 0.3490 -0.0467 0.0138  -0.0225 107 GLN   A CB  
2256 C  CG  A GLN   A 107 ? 0.3695 0.3915 0.5144 -0.0655 0.0037  -0.0836 107 GLN   A CG  
2257 C  CG  B GLN   A 107 ? 0.3346 0.3198 0.3957 -0.0476 0.0031  -0.0117 107 GLN   A CG  
2258 C  CD  A GLN   A 107 ? 0.4069 0.4153 0.6000 -0.0620 -0.0004 -0.0709 107 GLN   A CD  
2259 C  CD  B GLN   A 107 ? 0.3534 0.3338 0.4370 -0.0458 -0.0045 0.0006  107 GLN   A CD  
2260 O  OE1 A GLN   A 107 ? 0.4198 0.4237 0.6349 -0.0611 -0.0027 -0.0690 107 GLN   A OE1 
2261 O  OE1 B GLN   A 107 ? 0.3602 0.3394 0.4476 -0.0456 -0.0057 0.0057  107 GLN   A OE1 
2262 N  NE2 A GLN   A 107 ? 0.4188 0.4232 0.6279 -0.0621 -0.0019 -0.0684 107 GLN   A NE2 
2263 N  NE2 B GLN   A 107 ? 0.3588 0.3377 0.4494 -0.0455 -0.0090 0.0055  107 GLN   A NE2 
2280 N  N   . LEU   A 108 ? 0.2249 0.2323 0.2467 -0.0550 0.0535  -0.0600 108 LEU   A N   
2281 C  CA  . LEU   A 108 ? 0.1974 0.1901 0.2083 -0.0250 0.0451  -0.0224 108 LEU   A CA  
2282 C  C   . LEU   A 108 ? 0.1647 0.1502 0.2078 -0.0095 0.0331  0.0009  108 LEU   A C   
2283 O  O   . LEU   A 108 ? 0.1619 0.1546 0.2248 -0.0008 0.0389  0.0090  108 LEU   A O   
2284 C  CB  . LEU   A 108 ? 0.1970 0.2018 0.1822 -0.0268 0.0442  -0.0176 108 LEU   A CB  
2285 C  CG  . LEU   A 108 ? 0.2065 0.2296 0.2151 -0.0296 0.0503  -0.0192 108 LEU   A CG  
2286 C  CD1 . LEU   A 108 ? 0.2200 0.2395 0.2160 -0.0391 0.0565  -0.0162 108 LEU   A CD1 
2287 C  CD2 . LEU   A 108 ? 0.2074 0.2539 0.2638 -0.0237 0.0390  -0.0114 108 LEU   A CD2 
2300 N  N   . LEU   A 109 ? 0.1481 0.1529 0.2024 0.0040  0.0260  0.0165  109 LEU   A N   
2301 C  CA  . LEU   A 109 ? 0.1473 0.1489 0.1812 0.0036  0.0098  0.0174  109 LEU   A CA  
2302 C  C   . LEU   A 109 ? 0.1382 0.1398 0.1683 -0.0076 0.0173  0.0102  109 LEU   A C   
2303 O  O   . LEU   A 109 ? 0.1487 0.1322 0.1831 -0.0027 0.0028  0.0055  109 LEU   A O   
2304 C  CB  . LEU   A 109 ? 0.1577 0.1563 0.1933 0.0151  0.0078  0.0277  109 LEU   A CB  
2305 C  CG  . LEU   A 109 ? 0.1551 0.1651 0.1994 0.0096  0.0136  0.0345  109 LEU   A CG  
2306 C  CD1 . LEU   A 109 ? 0.1567 0.1564 0.2107 0.0018  0.0264  0.0132  109 LEU   A CD1 
2307 C  CD2 . LEU   A 109 ? 0.1497 0.1821 0.2230 0.0055  0.0105  0.0378  109 LEU   A CD2 
2319 N  N   . LYS   A 110 ? 0.1383 0.1397 0.1717 -0.0038 0.0043  0.0036  110 LYS   A N   
2320 C  CA  . LYS   A 110 ? 0.1421 0.1326 0.1792 -0.0080 0.0021  0.0096  110 LYS   A CA  
2321 C  C   . LYS   A 110 ? 0.1404 0.1246 0.1663 -0.0092 0.0081  -0.0009 110 LYS   A C   
2322 O  O   . LYS   A 110 ? 0.1357 0.1281 0.1839 -0.0092 0.0107  -0.0050 110 LYS   A O   
2323 C  CB  . LYS   A 110 ? 0.1480 0.1391 0.1949 -0.0005 -0.0105 -0.0014 110 LYS   A CB  
2324 C  CG  . LYS   A 110 ? 0.1566 0.1396 0.2051 -0.0065 -0.0095 -0.0072 110 LYS   A CG  
2325 C  CD  . LYS   A 110 ? 0.1605 0.1465 0.2101 -0.0135 -0.0080 -0.0122 110 LYS   A CD  
2326 C  CE  . LYS   A 110 ? 0.1667 0.1570 0.2304 -0.0095 0.0040  -0.0045 110 LYS   A CE  
2327 N  NZ  . LYS   A 110 ? 0.1639 0.1542 0.2400 -0.0166 0.0156  -0.0025 110 LYS   A NZ  
2341 N  N   . SER   A 111 ? 0.1446 0.1282 0.1637 -0.0041 0.0017  0.0010  111 SER   A N   
2342 C  CA  . SER   A 111 ? 0.1389 0.1357 0.1648 -0.0053 0.0076  -0.0003 111 SER   A CA  
2343 C  C   . SER   A 111 ? 0.1336 0.1313 0.1598 -0.0117 0.0122  0.0049  111 SER   A C   
2344 O  O   . SER   A 111 ? 0.1468 0.1253 0.1797 -0.0053 0.0082  0.0017  111 SER   A O   
2345 C  CB  . SER   A 111 ? 0.1533 0.1530 0.1894 -0.0032 0.0190  -0.0046 111 SER   A CB  
2346 O  OG  . SER   A 111 ? 0.2020 0.1783 0.1855 0.0004  0.0276  -0.0169 111 SER   A OG  
2352 N  N   . ALA   A 112 ? 0.1369 0.1281 0.1590 -0.0027 0.0188  0.0065  112 ALA   A N   
2353 C  CA  . ALA   A 112 ? 0.1418 0.1254 0.1604 -0.0032 0.0222  0.0023  112 ALA   A CA  
2354 C  C   . ALA   A 112 ? 0.1330 0.1167 0.1641 -0.0020 0.0139  0.0058  112 ALA   A C   
2355 O  O   . ALA   A 112 ? 0.1369 0.1251 0.1703 -0.0129 0.0118  0.0038  112 ALA   A O   
2356 C  CB  . ALA   A 112 ? 0.1566 0.1257 0.1640 -0.0031 0.0146  -0.0010 112 ALA   A CB  
2362 N  N   . TYR   A 113 ? 0.1236 0.1279 0.1738 -0.0080 0.0145  0.0141  113 TYR   A N   
2363 C  CA  . TYR   A 113 ? 0.1256 0.1221 0.1673 -0.0085 0.0187  0.0104  113 TYR   A CA  
2364 C  C   . TYR   A 113 ? 0.1238 0.1256 0.1573 -0.0110 0.0089  0.0045  113 TYR   A C   
2365 O  O   . TYR   A 113 ? 0.1301 0.1295 0.1732 -0.0097 0.0162  0.0020  113 TYR   A O   
2366 C  CB  . TYR   A 113 ? 0.1307 0.1372 0.1717 -0.0075 0.0054  0.0195  113 TYR   A CB  
2367 C  CG  . TYR   A 113 ? 0.1276 0.1342 0.1713 -0.0072 0.0194  0.0203  113 TYR   A CG  
2368 C  CD1 . TYR   A 113 ? 0.1305 0.1359 0.1709 -0.0042 0.0170  0.0218  113 TYR   A CD1 
2369 C  CD2 . TYR   A 113 ? 0.1346 0.1359 0.1607 -0.0115 0.0080  0.0180  113 TYR   A CD2 
2370 C  CE1 . TYR   A 113 ? 0.1374 0.1448 0.1599 -0.0093 0.0153  0.0269  113 TYR   A CE1 
2371 C  CE2 . TYR   A 113 ? 0.1349 0.1411 0.1676 -0.0094 0.0079  0.0210  113 TYR   A CE2 
2372 C  CZ  . TYR   A 113 ? 0.1331 0.1452 0.1556 -0.0009 0.0151  0.0269  113 TYR   A CZ  
2373 O  OH  . TYR   A 113 ? 0.1316 0.1532 0.1775 0.0095  0.0146  0.0296  113 TYR   A OH  
2383 N  N   . GLU   A 114 ? 0.1308 0.1221 0.1607 -0.0075 0.0202  0.0011  114 GLU   A N   
2384 C  CA  . GLU   A 114 ? 0.1294 0.1160 0.1789 0.0014  0.0104  0.0119  114 GLU   A CA  
2385 C  C   . GLU   A 114 ? 0.1229 0.1195 0.1802 0.0040  0.0172  0.0142  114 GLU   A C   
2386 O  O   . GLU   A 114 ? 0.1331 0.1215 0.1803 -0.0039 0.0052  0.0093  114 GLU   A O   
2387 C  CB  . GLU   A 114 ? 0.1307 0.1197 0.1832 -0.0077 0.0068  0.0075  114 GLU   A CB  
2388 C  CG  . GLU   A 114 ? 0.1414 0.1266 0.1791 0.0005  0.0119  0.0025  114 GLU   A CG  
2389 C  CD  . GLU   A 114 ? 0.1464 0.1275 0.1857 -0.0061 0.0055  0.0024  114 GLU   A CD  
2390 O  OE1 . GLU   A 114 ? 0.1426 0.1246 0.2012 -0.0072 0.0164  -0.0077 114 GLU   A OE1 
2391 O  OE2 . GLU   A 114 ? 0.1618 0.1373 0.2104 -0.0091 0.0113  -0.0095 114 GLU   A OE2 
2398 N  N   . ASN   A 115 ? 0.1284 0.1283 0.1603 -0.0095 0.0126  0.0080  115 ASN   A N   
2399 C  CA  . ASN   A 115 ? 0.1309 0.1300 0.1680 -0.0101 0.0107  0.0105  115 ASN   A CA  
2400 C  C   . ASN   A 115 ? 0.1339 0.1330 0.1510 -0.0115 0.0032  0.0103  115 ASN   A C   
2401 O  O   . ASN   A 115 ? 0.1355 0.1427 0.1546 -0.0128 0.0149  0.0161  115 ASN   A O   
2402 C  CB  . ASN   A 115 ? 0.1406 0.1340 0.1705 -0.0174 0.0136  0.0067  115 ASN   A CB  
2403 C  CG  . ASN   A 115 ? 0.1365 0.1589 0.1714 -0.0207 0.0245  0.0075  115 ASN   A CG  
2404 O  OD1 . ASN   A 115 ? 0.1407 0.2531 0.2000 -0.0198 0.0267  0.0275  115 ASN   A OD1 
2405 N  ND2 . ASN   A 115 ? 0.1384 0.1416 0.1768 -0.0142 0.0323  0.0088  115 ASN   A ND2 
2412 N  N   . PHE   A 116 ? 0.1258 0.1321 0.1583 -0.0055 0.0111  0.0168  116 PHE   A N   
2413 C  CA  . PHE   A 116 ? 0.1264 0.1461 0.1514 0.0020  0.0126  0.0137  116 PHE   A CA  
2414 C  C   . PHE   A 116 ? 0.1219 0.1480 0.1661 -0.0041 0.0173  0.0190  116 PHE   A C   
2415 O  O   . PHE   A 116 ? 0.1362 0.1495 0.1743 -0.0028 0.0147  0.0261  116 PHE   A O   
2416 C  CB  . PHE   A 116 ? 0.1287 0.1285 0.1647 -0.0077 0.0187  0.0166  116 PHE   A CB  
2417 C  CG  . PHE   A 116 ? 0.1323 0.1317 0.1513 -0.0103 0.0136  0.0087  116 PHE   A CG  
2418 C  CD1 . PHE   A 116 ? 0.1337 0.1283 0.1538 -0.0116 0.0098  0.0081  116 PHE   A CD1 
2419 C  CD2 . PHE   A 116 ? 0.1307 0.1425 0.1711 -0.0072 0.0247  0.0126  116 PHE   A CD2 
2420 C  CE1 . PHE   A 116 ? 0.1355 0.1288 0.1739 -0.0168 0.0077  0.0126  116 PHE   A CE1 
2421 C  CE2 . PHE   A 116 ? 0.1327 0.1400 0.1784 -0.0076 0.0180  0.0136  116 PHE   A CE2 
2422 C  CZ  . PHE   A 116 ? 0.1399 0.1239 0.1635 -0.0069 0.0080  0.0098  116 PHE   A CZ  
2432 N  N   . ASN   A 117 ? 0.1212 0.1406 0.1770 -0.0063 0.0177  0.0261  117 ASN   A N   
2433 C  CA  . ASN   A 117 ? 0.1325 0.1419 0.1857 -0.0044 0.0184  0.0272  117 ASN   A CA  
2434 C  C   . ASN   A 117 ? 0.1296 0.1463 0.1971 -0.0053 0.0160  0.0200  117 ASN   A C   
2435 O  O   . ASN   A 117 ? 0.1430 0.1460 0.2188 -0.0078 -0.0105 0.0384  117 ASN   A O   
2436 C  CB  . ASN   A 117 ? 0.1350 0.1492 0.1787 -0.0024 0.0118  0.0253  117 ASN   A CB  
2437 C  CG  . ASN   A 117 ? 0.1332 0.1422 0.1794 -0.0060 0.0078  0.0289  117 ASN   A CG  
2438 O  OD1 . ASN   A 117 ? 0.1372 0.1617 0.1949 -0.0156 0.0153  0.0226  117 ASN   A OD1 
2439 N  ND2 . ASN   A 117 ? 0.1279 0.1354 0.1862 0.0014  0.0032  0.0257  117 ASN   A ND2 
2446 N  N   . GLN   A 118 ? 0.1304 0.1417 0.1942 -0.0112 -0.0001 0.0299  118 GLN   A N   
2447 C  CA  . GLN   A 118 ? 0.1383 0.1540 0.2060 -0.0092 -0.0043 0.0241  118 GLN   A CA  
2448 C  C   . GLN   A 118 ? 0.1365 0.1605 0.1946 -0.0114 0.0003  0.0258  118 GLN   A C   
2449 O  O   . GLN   A 118 ? 0.1367 0.1944 0.2241 -0.0031 -0.0170 0.0169  118 GLN   A O   
2450 C  CB  . GLN   A 118 ? 0.1323 0.1569 0.2107 -0.0024 0.0054  0.0318  118 GLN   A CB  
2451 C  CG  . GLN   A 118 ? 0.1270 0.1570 0.2072 -0.0080 0.0049  0.0243  118 GLN   A CG  
2452 C  CD  . GLN   A 118 ? 0.1292 0.1637 0.2163 -0.0006 0.0024  0.0177  118 GLN   A CD  
2453 O  OE1 . GLN   A 118 ? 0.1357 0.1752 0.2297 0.0069  -0.0004 0.0119  118 GLN   A OE1 
2454 N  NE2 . GLN   A 118 ? 0.1401 0.1590 0.2181 0.0061  0.0013  0.0215  118 GLN   A NE2 
2463 N  N   . HIS   A 119 ? 0.1427 0.1540 0.1788 -0.0066 0.0036  0.0320  119 HIS   A N   
2464 C  CA  . HIS   A 119 ? 0.1481 0.1649 0.1759 -0.0096 -0.0017 0.0351  119 HIS   A CA  
2465 C  C   . HIS   A 119 ? 0.1634 0.1722 0.1635 -0.0125 0.0031  0.0244  119 HIS   A C   
2466 O  O   . HIS   A 119 ? 0.1687 0.1784 0.1734 -0.0318 0.0021  0.0310  119 HIS   A O   
2467 C  CB  . HIS   A 119 ? 0.1553 0.1657 0.1866 -0.0075 0.0157  0.0350  119 HIS   A CB  
2468 C  CG  . HIS   A 119 ? 0.1524 0.1634 0.2311 -0.0008 0.0104  0.0442  119 HIS   A CG  
2469 N  ND1 . HIS   A 119 ? 0.1652 0.1865 0.2931 -0.0129 0.0072  0.0264  119 HIS   A ND1 
2470 C  CD2 . HIS   A 119 ? 0.1671 0.1714 0.2544 0.0103  0.0258  0.0654  119 HIS   A CD2 
2471 C  CE1 . HIS   A 119 ? 0.1564 0.1882 0.3085 -0.0159 0.0220  0.0516  119 HIS   A CE1 
2472 N  NE2 . HIS   A 119 ? 0.1704 0.1814 0.3013 -0.0017 0.0357  0.0622  119 HIS   A NE2 
2480 N  N   . GLU   A 120 ? 0.1714 0.1950 0.1708 -0.0100 -0.0079 0.0548  120 GLU   A N   
2481 C  CA  . GLU   A 120 ? 0.1946 0.2305 0.2056 -0.0027 -0.0142 0.0998  120 GLU   A CA  
2482 C  C   . GLU   A 120 ? 0.1695 0.2144 0.1803 -0.0143 -0.0088 0.0924  120 GLU   A C   
2483 O  O   . GLU   A 120 ? 0.1719 0.2097 0.1912 -0.0163 -0.0015 0.0793  120 GLU   A O   
2484 C  CB  . GLU   A 120 ? 0.2704 0.3023 0.2693 0.0207  -0.0161 0.1544  120 GLU   A CB  
2485 C  CG  . GLU   A 120 ? 0.3747 0.3903 0.3912 0.0334  -0.0115 0.1582  120 GLU   A CG  
2486 C  CD  . GLU   A 120 ? 0.4610 0.4640 0.5221 0.0421  0.0021  0.1414  120 GLU   A CD  
2487 O  OE1 . GLU   A 120 ? 0.4848 0.4853 0.5501 0.0442  0.0063  0.1359  120 GLU   A OE1 
2488 O  OE2 . GLU   A 120 ? 0.5259 0.5259 0.5843 0.0441  0.0083  0.1337  120 GLU   A OE2 
2495 N  N   . VAL   A 121 ? 0.1680 0.2165 0.1566 -0.0124 0.0017  0.0726  121 VAL   A N   
2496 C  CA  . VAL   A 121 ? 0.1763 0.2200 0.1448 -0.0156 0.0130  0.0661  121 VAL   A CA  
2497 C  C   . VAL   A 121 ? 0.1662 0.1974 0.1300 -0.0225 0.0069  0.0470  121 VAL   A C   
2498 O  O   . VAL   A 121 ? 0.1670 0.1943 0.1537 -0.0295 -0.0082 0.0447  121 VAL   A O   
2499 C  CB  . VAL   A 121 ? 0.2151 0.2572 0.1884 -0.0007 0.0246  0.0751  121 VAL   A CB  
2500 C  CG1 . VAL   A 121 ? 0.2146 0.2681 0.1995 0.0114  0.0296  0.0789  121 VAL   A CG1 
2501 C  CG2 . VAL   A 121 ? 0.2398 0.2735 0.2357 -0.0117 0.0176  0.0616  121 VAL   A CG2 
2511 N  N   . LEU   A 122 ? 0.1543 0.1797 0.1412 -0.0216 0.0056  0.0464  122 LEU   A N   
2512 C  CA  . LEU   A 122 ? 0.1609 0.1643 0.1370 -0.0234 0.0184  0.0362  122 LEU   A CA  
2513 C  C   . LEU   A 122 ? 0.1527 0.1598 0.1382 -0.0279 0.0056  0.0365  122 LEU   A C   
2514 O  O   . LEU   A 122 ? 0.1509 0.1701 0.1800 -0.0330 0.0035  0.0400  122 LEU   A O   
2515 C  CB  . LEU   A 122 ? 0.1768 0.1621 0.1724 -0.0093 0.0073  0.0455  122 LEU   A CB  
2516 C  CG  . LEU   A 122 ? 0.1709 0.1689 0.1635 -0.0081 0.0157  0.0329  122 LEU   A CG  
2517 C  CD1 . LEU   A 122 ? 0.1896 0.1757 0.1842 -0.0219 0.0223  0.0305  122 LEU   A CD1 
2518 C  CD2 . LEU   A 122 ? 0.1600 0.1617 0.1634 -0.0009 0.0259  0.0279  122 LEU   A CD2 
2530 N  N   . LEU   A 123 ? 0.1476 0.1591 0.1355 -0.0250 0.0044  0.0267  123 LEU   A N   
2531 C  CA  . LEU   A 123 ? 0.1511 0.1544 0.1305 -0.0230 0.0087  0.0289  123 LEU   A CA  
2532 C  C   . LEU   A 123 ? 0.1448 0.1519 0.1170 -0.0200 0.0061  0.0283  123 LEU   A C   
2533 O  O   . LEU   A 123 ? 0.1411 0.1702 0.1391 -0.0269 0.0035  0.0324  123 LEU   A O   
2534 C  CB  . LEU   A 123 ? 0.1574 0.1643 0.1421 -0.0250 0.0171  0.0275  123 LEU   A CB  
2535 C  CG  . LEU   A 123 ? 0.1642 0.1819 0.1427 -0.0201 0.0160  0.0106  123 LEU   A CG  
2536 C  CD1 . LEU   A 123 ? 0.1669 0.1915 0.1529 -0.0143 0.0166  -0.0002 123 LEU   A CD1 
2537 C  CD2 . LEU   A 123 ? 0.1756 0.1826 0.1530 -0.0175 0.0148  0.0074  123 LEU   A CD2 
2549 N  N   A ALA   A 124 ? 0.1413 0.1426 0.1111 -0.0168 0.0031  0.0242  124 ALA   A N   
2550 N  N   B ALA   A 124 ? 0.1441 0.1439 0.1278 -0.0214 0.0078  0.0181  124 ALA   A N   
2551 C  CA  A ALA   A 124 ? 0.1371 0.1366 0.1128 -0.0105 -0.0052 0.0204  124 ALA   A CA  
2552 C  CA  B ALA   A 124 ? 0.1442 0.1418 0.1433 -0.0285 0.0039  0.0159  124 ALA   A CA  
2553 C  C   A ALA   A 124 ? 0.1272 0.1346 0.1097 -0.0085 0.0072  0.0273  124 ALA   A C   
2554 C  C   B ALA   A 124 ? 0.1432 0.1326 0.1445 -0.0246 0.0031  0.0217  124 ALA   A C   
2555 O  O   A ALA   A 124 ? 0.1276 0.1406 0.1445 -0.0094 0.0254  0.0302  124 ALA   A O   
2556 O  O   B ALA   A 124 ? 0.1448 0.1281 0.1653 -0.0171 0.0041  0.0256  124 ALA   A O   
2557 C  CB  A ALA   A 124 ? 0.1299 0.1268 0.1449 -0.0089 -0.0012 0.0203  124 ALA   A CB  
2558 C  CB  B ALA   A 124 ? 0.1473 0.1424 0.1539 -0.0333 0.0088  0.0117  124 ALA   A CB  
2569 N  N   A PRO   A 125 ? 0.1220 0.1415 0.1306 -0.0023 0.0102  0.0331  125 PRO   A N   
2570 N  N   B PRO   A 125 ? 0.1310 0.1230 0.1174 -0.0192 -0.0064 0.0260  125 PRO   A N   
2571 C  CA  A PRO   A 125 ? 0.1329 0.1532 0.1457 -0.0050 0.0081  0.0245  125 PRO   A CA  
2572 C  CA  B PRO   A 125 ? 0.1344 0.1321 0.1126 -0.0159 -0.0049 0.0263  125 PRO   A CA  
2573 C  C   A PRO   A 125 ? 0.1301 0.1456 0.1368 -0.0083 0.0093  0.0225  125 PRO   A C   
2574 C  C   B PRO   A 125 ? 0.1407 0.1414 0.1271 -0.0168 -0.0021 0.0231  125 PRO   A C   
2575 O  O   A PRO   A 125 ? 0.1331 0.1401 0.1494 0.0001  -0.0021 0.0195  125 PRO   A O   
2576 O  O   B PRO   A 125 ? 0.1425 0.1412 0.1459 -0.0172 -0.0020 0.0185  125 PRO   A O   
2577 C  CB  A PRO   A 125 ? 0.1359 0.1572 0.1576 -0.0127 0.0059  0.0233  125 PRO   A CB  
2578 C  CB  B PRO   A 125 ? 0.1251 0.1243 0.0997 -0.0174 -0.0126 0.0339  125 PRO   A CB  
2579 C  CG  A PRO   A 125 ? 0.1380 0.1498 0.1622 -0.0106 0.0065  0.0334  125 PRO   A CG  
2580 C  CG  B PRO   A 125 ? 0.1191 0.1137 0.1006 -0.0143 -0.0034 0.0261  125 PRO   A CG  
2581 C  CD  A PRO   A 125 ? 0.1255 0.1465 0.1491 -0.0063 0.0150  0.0253  125 PRO   A CD  
2582 C  CD  B PRO   A 125 ? 0.1176 0.1050 0.0995 -0.0228 -0.0014 0.0199  125 PRO   A CD  
2597 N  N   A LEU   A 126 ? 0.1282 0.1460 0.1349 -0.0051 0.0031  0.0245  126 LEU   A N   
2598 N  N   B LEU   A 126 ? 0.1472 0.1490 0.1348 -0.0106 -0.0040 0.0193  126 LEU   A N   
2599 C  CA  A LEU   A 126 ? 0.1307 0.1454 0.1475 -0.0016 0.0052  0.0274  126 LEU   A CA  
2600 C  CA  B LEU   A 126 ? 0.1447 0.1436 0.1421 -0.0056 0.0009  0.0176  126 LEU   A CA  
2601 C  C   A LEU   A 126 ? 0.1351 0.1382 0.1428 0.0101  -0.0047 0.0252  126 LEU   A C   
2602 C  C   B LEU   A 126 ? 0.1379 0.1370 0.1441 -0.0014 0.0056  0.0100  126 LEU   A C   
2603 O  O   A LEU   A 126 ? 0.1462 0.1417 0.1650 0.0193  0.0157  0.0299  126 LEU   A O   
2604 O  O   B LEU   A 126 ? 0.1370 0.1382 0.1533 -0.0066 0.0022  0.0189  126 LEU   A O   
2605 C  CB  A LEU   A 126 ? 0.1344 0.1395 0.1571 0.0016  0.0035  0.0230  126 LEU   A CB  
2606 C  CB  B LEU   A 126 ? 0.1503 0.1508 0.1639 -0.0068 0.0051  0.0038  126 LEU   A CB  
2607 C  CG  A LEU   A 126 ? 0.1300 0.1423 0.1843 0.0037  0.0184  0.0087  126 LEU   A CG  
2608 C  CG  B LEU   A 126 ? 0.1520 0.1527 0.1734 -0.0022 0.0143  -0.0093 126 LEU   A CG  
2609 C  CD1 A LEU   A 126 ? 0.1355 0.1557 0.2294 -0.0008 0.0140  0.0090  126 LEU   A CD1 
2610 C  CD1 B LEU   A 126 ? 0.1503 0.1472 0.1832 -0.0041 0.0175  -0.0204 126 LEU   A CD1 
2611 C  CD2 A LEU   A 126 ? 0.1398 0.1427 0.1854 -0.0093 0.0256  0.0132  126 LEU   A CD2 
2612 C  CD2 B LEU   A 126 ? 0.1517 0.1572 0.1768 0.0025  0.0071  -0.0109 126 LEU   A CD2 
2635 N  N   A LEU   A 127 ? 0.1381 0.1344 0.1418 0.0047  0.0048  0.0186  127 LEU   A N   
2636 N  N   B LEU   A 127 ? 0.1343 0.1296 0.1332 0.0045  0.0105  0.0096  127 LEU   A N   
2637 C  CA  A LEU   A 127 ? 0.1349 0.1365 0.1318 -0.0039 0.0032  0.0175  127 LEU   A CA  
2638 C  CA  B LEU   A 127 ? 0.1312 0.1396 0.1269 0.0059  0.0076  0.0159  127 LEU   A CA  
2639 C  C   A LEU   A 127 ? 0.1288 0.1329 0.1317 -0.0052 0.0012  0.0153  127 LEU   A C   
2640 C  C   B LEU   A 127 ? 0.1313 0.1441 0.1363 -0.0007 0.0117  0.0116  127 LEU   A C   
2641 O  O   A LEU   A 127 ? 0.1358 0.1303 0.1389 -0.0148 -0.0057 0.0119  127 LEU   A O   
2642 O  O   B LEU   A 127 ? 0.1360 0.1439 0.1353 -0.0081 0.0246  0.0187  127 LEU   A O   
2643 C  CB  A LEU   A 127 ? 0.1378 0.1440 0.1416 0.0019  0.0105  0.0100  127 LEU   A CB  
2644 C  CB  B LEU   A 127 ? 0.1310 0.1473 0.1320 0.0069  0.0000  0.0139  127 LEU   A CB  
2645 C  CG  A LEU   A 127 ? 0.1447 0.1504 0.1435 0.0083  0.0032  0.0127  127 LEU   A CG  
2646 C  CG  B LEU   A 127 ? 0.1342 0.1536 0.1352 0.0075  -0.0071 0.0199  127 LEU   A CG  
2647 C  CD1 A LEU   A 127 ? 0.1495 0.1442 0.1593 0.0078  0.0037  0.0107  127 LEU   A CD1 
2648 C  CD1 B LEU   A 127 ? 0.1305 0.1571 0.1484 0.0118  0.0023  0.0178  127 LEU   A CD1 
2649 C  CD2 A LEU   A 127 ? 0.1609 0.1514 0.1597 0.0109  -0.0098 0.0097  127 LEU   A CD2 
2650 C  CD2 B LEU   A 127 ? 0.1453 0.1621 0.1360 0.0046  -0.0240 0.0081  127 LEU   A CD2 
2673 N  N   A SER   A 128 ? 0.1349 0.1335 0.1285 -0.0079 0.0023  0.0160  128 SER   A N   
2674 N  N   B SER   A 128 ? 0.1322 0.1440 0.1416 -0.0055 0.0031  0.0149  128 SER   A N   
2675 C  CA  A SER   A 128 ? 0.1469 0.1394 0.1168 -0.0022 0.0048  0.0196  128 SER   A CA  
2676 C  CA  B SER   A 128 ? 0.1318 0.1393 0.1291 -0.0096 -0.0087 0.0177  128 SER   A CA  
2677 C  C   A SER   A 128 ? 0.1549 0.1503 0.1177 0.0075  0.0037  0.0227  128 SER   A C   
2678 C  C   B SER   A 128 ? 0.1268 0.1325 0.1219 -0.0184 -0.0235 0.0185  128 SER   A C   
2679 O  O   A SER   A 128 ? 0.1693 0.1657 0.1434 0.0102  0.0086  0.0176  128 SER   A O   
2680 O  O   B SER   A 128 ? 0.1222 0.1226 0.1338 -0.0244 -0.0369 0.0230  128 SER   A O   
2681 C  CB  A SER   A 128 ? 0.1484 0.1471 0.1328 -0.0063 0.0005  0.0153  128 SER   A CB  
2682 C  CB  B SER   A 128 ? 0.1335 0.1449 0.1253 -0.0098 -0.0122 0.0240  128 SER   A CB  
2683 O  OG  A SER   A 128 ? 0.1522 0.1590 0.1428 -0.0038 0.0067  0.0103  128 SER   A OG  
2684 O  OG  B SER   A 128 ? 0.1343 0.1502 0.1295 -0.0152 -0.0015 0.0337  128 SER   A OG  
2695 N  N   A ALA   A 129 ? 0.1559 0.1515 0.1461 0.0093  -0.0001 0.0320  129 ALA   A N   
2696 N  N   B ALA   A 129 ? 0.1275 0.1365 0.1319 -0.0199 -0.0218 0.0220  129 ALA   A N   
2697 C  CA  A ALA   A 129 ? 0.1530 0.1535 0.1708 0.0129  0.0090  0.0352  129 ALA   A CA  
2698 C  CA  B ALA   A 129 ? 0.1288 0.1418 0.1448 -0.0211 -0.0206 0.0235  129 ALA   A CA  
2699 C  C   A ALA   A 129 ? 0.1570 0.1527 0.1569 0.0147  0.0076  0.0188  129 ALA   A C   
2700 C  C   B ALA   A 129 ? 0.1318 0.1475 0.1533 -0.0246 -0.0262 0.0105  129 ALA   A C   
2701 O  O   A ALA   A 129 ? 0.1612 0.1532 0.1519 0.0091  0.0084  0.0233  129 ALA   A O   
2702 O  O   B ALA   A 129 ? 0.1273 0.1506 0.1582 -0.0289 -0.0240 0.0151  129 ALA   A O   
2703 C  CB  A ALA   A 129 ? 0.1599 0.1727 0.2025 0.0117  0.0190  0.0421  129 ALA   A CB  
2704 C  CB  B ALA   A 129 ? 0.1270 0.1492 0.1416 -0.0157 -0.0132 0.0285  129 ALA   A CB  
2715 N  N   A GLY   A 130 ? 0.1538 0.1497 0.1725 0.0108  0.0058  0.0145  130 GLY   A N   
2716 N  N   B GLY   A 130 ? 0.1386 0.1481 0.1679 -0.0248 -0.0269 0.0074  130 GLY   A N   
2717 C  CA  A GLY   A 130 ? 0.1673 0.1527 0.1742 0.0104  0.0074  0.0072  130 GLY   A CA  
2718 C  CA  B GLY   A 130 ? 0.1519 0.1496 0.1752 -0.0183 -0.0222 0.0065  130 GLY   A CA  
2719 C  C   A GLY   A 130 ? 0.1659 0.1465 0.1491 0.0109  -0.0044 0.0039  130 GLY   A C   
2720 C  C   B GLY   A 130 ? 0.1580 0.1519 0.1758 -0.0075 -0.0258 0.0074  130 GLY   A C   
2721 O  O   A GLY   A 130 ? 0.1741 0.1418 0.1481 0.0010  -0.0057 0.0099  130 GLY   A O   
2722 O  O   B GLY   A 130 ? 0.1660 0.1539 0.1847 -0.0027 -0.0277 0.0077  130 GLY   A O   
2729 N  N   A ILE   A 131 ? 0.1721 0.1413 0.1627 0.0052  -0.0092 0.0132  131 ILE   A N   
2730 N  N   B ILE   A 131 ? 0.1589 0.1485 0.1699 -0.0089 -0.0298 0.0126  131 ILE   A N   
2731 C  CA  A ILE   A 131 ? 0.1836 0.1404 0.1437 -0.0046 -0.0207 0.0098  131 ILE   A CA  
2732 C  CA  B ILE   A 131 ? 0.1621 0.1461 0.1656 -0.0057 -0.0360 0.0108  131 ILE   A CA  
2733 C  C   A ILE   A 131 ? 0.1799 0.1423 0.1401 -0.0082 -0.0077 0.0273  131 ILE   A C   
2734 C  C   B ILE   A 131 ? 0.1652 0.1486 0.1563 -0.0045 -0.0294 0.0084  131 ILE   A C   
2735 O  O   A ILE   A 131 ? 0.1869 0.1494 0.1647 -0.0078 -0.0072 0.0303  131 ILE   A O   
2736 O  O   B ILE   A 131 ? 0.1728 0.1521 0.1633 0.0003  -0.0266 0.0085  131 ILE   A O   
2737 C  CB  A ILE   A 131 ? 0.1935 0.1573 0.1638 -0.0090 -0.0290 -0.0015 131 ILE   A CB  
2738 C  CB  B ILE   A 131 ? 0.1587 0.1489 0.1678 -0.0013 -0.0425 0.0121  131 ILE   A CB  
2739 C  CG1 A ILE   A 131 ? 0.1991 0.1856 0.1715 -0.0144 -0.0354 -0.0040 131 ILE   A CG1 
2740 C  CG1 B ILE   A 131 ? 0.1591 0.1583 0.1676 0.0022  -0.0448 0.0144  131 ILE   A CG1 
2741 C  CG2 A ILE   A 131 ? 0.2032 0.1513 0.1882 -0.0038 -0.0241 -0.0110 131 ILE   A CG2 
2742 C  CG2 B ILE   A 131 ? 0.1520 0.1442 0.1694 -0.0044 -0.0437 0.0004  131 ILE   A CG2 
2743 C  CD1 A ILE   A 131 ? 0.2011 0.1939 0.2048 -0.0134 -0.0430 -0.0066 131 ILE   A CD1 
2744 C  CD1 B ILE   A 131 ? 0.1625 0.1626 0.1661 0.0012  -0.0483 0.0118  131 ILE   A CD1 
2767 N  N   A PHE   A 132 ? 0.1701 0.1455 0.1412 -0.0070 -0.0023 0.0262  132 PHE   A N   
2768 N  N   B PHE   A 132 ? 0.1578 0.1507 0.1500 -0.0016 -0.0239 0.0033  132 PHE   A N   
2769 C  CA  A PHE   A 132 ? 0.1667 0.1507 0.1262 -0.0120 0.0037  0.0197  132 PHE   A CA  
2770 C  CA  B PHE   A 132 ? 0.1621 0.1556 0.1549 -0.0041 -0.0142 0.0042  132 PHE   A CA  
2771 C  C   A PHE   A 132 ? 0.1639 0.1650 0.1237 -0.0111 0.0006  0.0147  132 PHE   A C   
2772 C  C   B PHE   A 132 ? 0.1699 0.1685 0.1657 -0.0065 -0.0183 0.0085  132 PHE   A C   
2773 O  O   A PHE   A 132 ? 0.1680 0.1755 0.1418 -0.0201 0.0008  0.0120  132 PHE   A O   
2774 O  O   B PHE   A 132 ? 0.1781 0.1797 0.1746 -0.0123 -0.0113 0.0180  132 PHE   A O   
2775 C  CB  A PHE   A 132 ? 0.1628 0.1469 0.1197 -0.0088 -0.0055 0.0201  132 PHE   A CB  
2776 C  CB  B PHE   A 132 ? 0.1545 0.1488 0.1425 -0.0050 -0.0089 0.0047  132 PHE   A CB  
2777 C  CG  A PHE   A 132 ? 0.1657 0.1478 0.1226 -0.0020 -0.0084 0.0157  132 PHE   A CG  
2778 C  CG  B PHE   A 132 ? 0.1548 0.1448 0.1341 -0.0023 -0.0100 -0.0048 132 PHE   A CG  
2779 C  CD1 A PHE   A 132 ? 0.1717 0.1568 0.1485 0.0024  -0.0140 0.0031  132 PHE   A CD1 
2780 C  CD1 B PHE   A 132 ? 0.1577 0.1482 0.1409 0.0035  -0.0059 -0.0115 132 PHE   A CD1 
2781 C  CD2 A PHE   A 132 ? 0.1675 0.1519 0.1357 -0.0051 0.0018  0.0087  132 PHE   A CD2 
2782 C  CD2 B PHE   A 132 ? 0.1539 0.1456 0.1298 -0.0000 -0.0138 -0.0120 132 PHE   A CD2 
2783 C  CE1 A PHE   A 132 ? 0.1804 0.1606 0.1617 -0.0020 -0.0237 -0.0009 132 PHE   A CE1 
2784 C  CE1 B PHE   A 132 ? 0.1588 0.1494 0.1369 0.0080  -0.0171 -0.0104 132 PHE   A CE1 
2785 C  CE2 A PHE   A 132 ? 0.1722 0.1542 0.1490 -0.0037 -0.0103 0.0117  132 PHE   A CE2 
2786 C  CE2 B PHE   A 132 ? 0.1546 0.1513 0.1321 0.0086  -0.0196 -0.0097 132 PHE   A CE2 
2787 C  CZ  A PHE   A 132 ? 0.1762 0.1572 0.1582 -0.0095 -0.0224 0.0066  132 PHE   A CZ  
2788 C  CZ  B PHE   A 132 ? 0.1568 0.1501 0.1354 0.0061  -0.0224 -0.0086 132 PHE   A CZ  
2807 N  N   A GLY   A 133 ? 0.1640 0.1649 0.1237 -0.0029 -0.0145 0.0246  133 GLY   A N   
2808 N  N   B GLY   A 133 ? 0.1712 0.1664 0.1618 -0.0087 -0.0221 0.0044  133 GLY   A N   
2809 C  CA  A GLY   A 133 ? 0.1708 0.1806 0.1410 -0.0052 -0.0238 0.0125  133 GLY   A CA  
2810 C  CA  B GLY   A 133 ? 0.1733 0.1699 0.1621 -0.0109 -0.0223 -0.0018 133 GLY   A CA  
2811 C  C   A GLY   A 133 ? 0.1821 0.1917 0.1432 -0.0109 -0.0439 0.0050  133 GLY   A C   
2812 C  C   B GLY   A 133 ? 0.1746 0.1741 0.1576 -0.0108 -0.0257 -0.0101 133 GLY   A C   
2813 O  O   A GLY   A 133 ? 0.1994 0.2040 0.1579 -0.0132 -0.0364 -0.0153 133 GLY   A O   
2814 O  O   B GLY   A 133 ? 0.1781 0.1804 0.1531 -0.0070 -0.0222 -0.0281 133 GLY   A O   
2821 N  N   A ALA   A 134 ? 0.1852 0.1808 0.1357 -0.0140 -0.0290 0.0072  134 ALA   A N   
2822 N  N   B ALA   A 134 ? 0.1766 0.1668 0.1586 -0.0146 -0.0181 -0.0066 134 ALA   A N   
2823 C  CA  A ALA   A 134 ? 0.1812 0.1785 0.1574 -0.0097 -0.0188 -0.0031 134 ALA   A CA  
2824 C  CA  B ALA   A 134 ? 0.1735 0.1615 0.1702 -0.0108 -0.0161 -0.0100 134 ALA   A CA  
2825 C  C   A ALA   A 134 ? 0.1838 0.1784 0.1459 -0.0113 -0.0105 0.0071  134 ALA   A C   
2826 C  C   B ALA   A 134 ? 0.1732 0.1594 0.1675 -0.0061 -0.0149 -0.0187 134 ALA   A C   
2827 O  O   A ALA   A 134 ? 0.2043 0.1882 0.1551 -0.0145 -0.0028 -0.0005 134 ALA   A O   
2828 O  O   B ALA   A 134 ? 0.1781 0.1623 0.1718 -0.0036 -0.0097 -0.0282 134 ALA   A O   
2829 C  CB  A ALA   A 134 ? 0.1918 0.1730 0.1903 -0.0077 -0.0233 -0.0137 134 ALA   A CB  
2830 C  CB  B ALA   A 134 ? 0.1750 0.1575 0.1767 -0.0122 -0.0144 -0.0056 134 ALA   A CB  
2841 N  N   A ASP   A 135 ? 0.1846 0.1735 0.1581 -0.0069 -0.0057 0.0098  135 ASP   A N   
2842 N  N   B ASP   A 135 ? 0.1750 0.1641 0.1667 -0.0107 -0.0168 -0.0082 135 ASP   A N   
2843 C  CA  A ASP   A 135 ? 0.1842 0.1832 0.1879 -0.0137 -0.0210 0.0073  135 ASP   A CA  
2844 C  CA  B ASP   A 135 ? 0.1741 0.1654 0.1658 -0.0150 -0.0226 -0.0047 135 ASP   A CA  
2845 C  C   A ASP   A 135 ? 0.1688 0.1706 0.1863 -0.0114 -0.0126 0.0107  135 ASP   A C   
2846 C  C   B ASP   A 135 ? 0.1612 0.1542 0.1625 -0.0127 -0.0201 -0.0053 135 ASP   A C   
2847 O  O   A ASP   A 135 ? 0.1663 0.1651 0.2018 -0.0048 -0.0080 0.0214  135 ASP   A O   
2848 O  O   B ASP   A 135 ? 0.1638 0.1524 0.1691 -0.0109 -0.0185 -0.0037 135 ASP   A O   
2849 C  CB  A ASP   A 135 ? 0.2046 0.2161 0.2352 -0.0327 -0.0446 -0.0077 135 ASP   A CB  
2850 C  CB  B ASP   A 135 ? 0.1835 0.1776 0.1726 -0.0152 -0.0347 -0.0005 135 ASP   A CB  
2851 C  CG  A ASP   A 135 ? 0.2263 0.2428 0.2794 -0.0537 -0.0548 -0.0095 135 ASP   A CG  
2852 C  CG  B ASP   A 135 ? 0.1928 0.1908 0.1943 -0.0140 -0.0410 0.0031  135 ASP   A CG  
2853 O  OD1 A ASP   A 135 ? 0.2273 0.2503 0.2838 -0.0577 -0.0593 0.0105  135 ASP   A OD1 
2854 O  OD1 B ASP   A 135 ? 0.1949 0.1881 0.1897 -0.0048 -0.0386 0.0109  135 ASP   A OD1 
2855 O  OD2 A ASP   A 135 ? 0.2541 0.2647 0.3283 -0.0599 -0.0397 -0.0132 135 ASP   A OD2 
2856 O  OD2 B ASP   A 135 ? 0.1990 0.2004 0.2194 -0.0201 -0.0428 -0.0063 135 ASP   A OD2 
2865 N  N   A PRO   A 136 ? 0.1654 0.1724 0.1883 -0.0041 -0.0093 0.0194  136 PRO   A N   
2866 N  N   B PRO   A 136 ? 0.1539 0.1465 0.1529 -0.0079 -0.0178 -0.0112 136 PRO   A N   
2867 C  CA  A PRO   A 136 ? 0.1595 0.1740 0.1936 -0.0114 -0.0046 0.0048  136 PRO   A CA  
2868 C  CA  B PRO   A 136 ? 0.1538 0.1567 0.1521 -0.0132 -0.0080 -0.0179 136 PRO   A CA  
2869 C  C   A PRO   A 136 ? 0.1419 0.1680 0.1963 -0.0044 -0.0017 0.0113  136 PRO   A C   
2870 C  C   B PRO   A 136 ? 0.1460 0.1628 0.1367 -0.0144 -0.0032 -0.0195 136 PRO   A C   
2871 O  O   A PRO   A 136 ? 0.1384 0.1698 0.1961 -0.0081 -0.0013 0.0139  136 PRO   A O   
2872 O  O   B PRO   A 136 ? 0.1433 0.1622 0.1015 -0.0097 0.0101  -0.0249 136 PRO   A O   
2873 C  CB  A PRO   A 136 ? 0.1755 0.1768 0.2042 -0.0101 -0.0069 0.0044  136 PRO   A CB  
2874 C  CB  B PRO   A 136 ? 0.1636 0.1557 0.1680 -0.0091 -0.0090 -0.0219 136 PRO   A CB  
2875 C  CG  A PRO   A 136 ? 0.1855 0.1796 0.2188 0.0007  -0.0070 0.0145  136 PRO   A CG  
2876 C  CG  B PRO   A 136 ? 0.1660 0.1501 0.1652 -0.0027 -0.0090 -0.0265 136 PRO   A CG  
2877 C  CD  A PRO   A 136 ? 0.1770 0.1742 0.2066 0.0050  -0.0065 0.0238  136 PRO   A CD  
2878 C  CD  B PRO   A 136 ? 0.1562 0.1419 0.1571 -0.0019 -0.0075 -0.0101 136 PRO   A CD  
2893 N  N   A ILE   A 137 ? 0.1430 0.1696 0.1968 -0.0017 -0.0150 0.0198  137 ILE   A N   
2894 N  N   B ILE   A 137 ? 0.1467 0.1649 0.1593 -0.0167 -0.0079 -0.0189 137 ILE   A N   
2895 C  CA  A ILE   A 137 ? 0.1478 0.1720 0.2110 -0.0106 -0.0190 0.0237  137 ILE   A CA  
2896 C  CA  B ILE   A 137 ? 0.1485 0.1704 0.1631 -0.0130 -0.0082 -0.0181 137 ILE   A CA  
2897 C  C   A ILE   A 137 ? 0.1480 0.1664 0.2016 -0.0135 -0.0195 0.0212  137 ILE   A C   
2898 C  C   B ILE   A 137 ? 0.1447 0.1734 0.1552 -0.0157 -0.0003 -0.0085 137 ILE   A C   
2899 O  O   A ILE   A 137 ? 0.1571 0.1636 0.2032 -0.0127 -0.0137 0.0147  137 ILE   A O   
2900 O  O   B ILE   A 137 ? 0.1430 0.1758 0.1498 -0.0192 0.0043  -0.0059 137 ILE   A O   
2901 C  CB  A ILE   A 137 ? 0.1565 0.1882 0.2450 -0.0162 -0.0380 0.0169  137 ILE   A CB  
2902 C  CB  B ILE   A 137 ? 0.1561 0.1686 0.1820 -0.0121 -0.0239 -0.0242 137 ILE   A CB  
2903 C  CG1 A ILE   A 137 ? 0.1668 0.2103 0.2935 -0.0161 -0.0390 0.0217  137 ILE   A CG1 
2904 C  CG1 B ILE   A 137 ? 0.1694 0.1717 0.2138 -0.0161 -0.0365 -0.0302 137 ILE   A CG1 
2905 C  CG2 A ILE   A 137 ? 0.1629 0.1849 0.2534 -0.0246 -0.0303 -0.0014 137 ILE   A CG2 
2906 C  CG2 B ILE   A 137 ? 0.1566 0.1739 0.1833 -0.0035 -0.0269 -0.0263 137 ILE   A CG2 
2907 C  CD1 A ILE   A 137 ? 0.1766 0.2227 0.3123 -0.0113 -0.0444 0.0284  137 ILE   A CD1 
2908 C  CD1 B ILE   A 137 ? 0.1809 0.1746 0.2285 -0.0217 -0.0450 -0.0280 137 ILE   A CD1 
2931 N  N   A HIS   A 138 ? 0.1471 0.1817 0.2044 -0.0096 -0.0068 0.0211  138 HIS   A N   
2932 N  N   B HIS   A 138 ? 0.1445 0.1789 0.1649 -0.0134 0.0150  -0.0020 138 HIS   A N   
2933 C  CA  A HIS   A 138 ? 0.1517 0.1847 0.1883 -0.0140 0.0002  0.0150  138 HIS   A CA  
2934 C  CA  B HIS   A 138 ? 0.1487 0.1789 0.1678 -0.0089 0.0170  0.0030  138 HIS   A CA  
2935 C  C   A HIS   A 138 ? 0.1447 0.1841 0.1809 -0.0105 -0.0055 0.0222  138 HIS   A C   
2936 C  C   B HIS   A 138 ? 0.1444 0.1766 0.1693 -0.0057 0.0115  0.0166  138 HIS   A C   
2937 O  O   A HIS   A 138 ? 0.1460 0.1897 0.1824 -0.0175 -0.0018 0.0266  138 HIS   A O   
2938 O  O   B HIS   A 138 ? 0.1474 0.1804 0.1712 -0.0051 0.0120  0.0150  138 HIS   A O   
2939 C  CB  A HIS   A 138 ? 0.1692 0.2082 0.1919 -0.0089 -0.0043 0.0101  138 HIS   A CB  
2940 C  CB  B HIS   A 138 ? 0.1498 0.1843 0.1717 -0.0000 0.0189  -0.0123 138 HIS   A CB  
2941 C  CG  A HIS   A 138 ? 0.1856 0.2170 0.1973 -0.0147 -0.0050 0.0073  138 HIS   A CG  
2942 C  CG  B HIS   A 138 ? 0.1565 0.1834 0.1800 -0.0012 0.0122  -0.0237 138 HIS   A CG  
2943 N  ND1 A HIS   A 138 ? 0.2026 0.2264 0.2268 -0.0182 -0.0069 0.0040  138 HIS   A ND1 
2944 N  ND1 B HIS   A 138 ? 0.1676 0.1879 0.2029 -0.0018 0.0016  -0.0267 138 HIS   A ND1 
2945 C  CD2 A HIS   A 138 ? 0.1829 0.2217 0.1932 -0.0104 0.0040  0.0042  138 HIS   A CD2 
2946 C  CD2 B HIS   A 138 ? 0.1548 0.1767 0.1817 -0.0005 0.0114  -0.0229 138 HIS   A CD2 
2947 C  CE1 A HIS   A 138 ? 0.2064 0.2302 0.2251 -0.0076 -0.0038 0.0029  138 HIS   A CE1 
2948 C  CE1 B HIS   A 138 ? 0.1669 0.1839 0.2038 0.0000  0.0007  -0.0255 138 HIS   A CE1 
2949 N  NE2 A HIS   A 138 ? 0.1955 0.2302 0.2005 -0.0053 0.0084  -0.0036 138 HIS   A NE2 
2950 N  NE2 B HIS   A 138 ? 0.1614 0.1787 0.1934 -0.0003 0.0058  -0.0267 138 HIS   A NE2 
2965 N  N   . SER   A 139 ? 0.1391 0.1683 0.1809 -0.0068 -0.0009 0.0284  139 SER   A N   
2966 C  CA  . SER   A 139 ? 0.1400 0.1647 0.1840 -0.0098 0.0020  0.0353  139 SER   A CA  
2967 C  C   . SER   A 139 ? 0.1377 0.1557 0.1801 -0.0097 0.0085  0.0205  139 SER   A C   
2968 O  O   . SER   A 139 ? 0.1330 0.1516 0.1929 -0.0099 0.0059  0.0349  139 SER   A O   
2969 C  CB  . SER   A 139 ? 0.1377 0.1635 0.1778 -0.0174 -0.0074 0.0370  139 SER   A CB  
2970 O  OG  . SER   A 139 ? 0.1414 0.1663 0.1808 -0.0182 -0.0071 0.0384  139 SER   A OG  
2977 N  N   . LEU   A 140 ? 0.1327 0.1574 0.1821 -0.0119 0.0083  0.0341  140 LEU   A N   
2978 C  CA  . LEU   A 140 ? 0.1309 0.1598 0.1856 -0.0099 0.0058  0.0297  140 LEU   A CA  
2979 C  C   . LEU   A 140 ? 0.1209 0.1641 0.1874 -0.0154 0.0003  0.0344  140 LEU   A C   
2980 O  O   . LEU   A 140 ? 0.1340 0.1644 0.2019 -0.0132 -0.0028 0.0402  140 LEU   A O   
2981 C  CB  . LEU   A 140 ? 0.1333 0.1712 0.1905 -0.0177 0.0080  0.0278  140 LEU   A CB  
2982 C  CG  . LEU   A 140 ? 0.1294 0.1857 0.1863 -0.0198 0.0086  0.0369  140 LEU   A CG  
2983 C  CD1 . LEU   A 140 ? 0.1364 0.1907 0.1953 -0.0090 0.0054  0.0307  140 LEU   A CD1 
2984 C  CD2 . LEU   A 140 ? 0.1357 0.2055 0.2025 -0.0166 0.0217  0.0417  140 LEU   A CD2 
2996 N  N   . ARG   A 141 ? 0.1282 0.1653 0.1868 -0.0108 0.0009  0.0275  141 ARG   A N   
2997 C  CA  . ARG   A 141 ? 0.1423 0.1802 0.2040 -0.0245 -0.0033 0.0154  141 ARG   A CA  
2998 C  C   . ARG   A 141 ? 0.1410 0.1646 0.1883 -0.0129 -0.0078 0.0167  141 ARG   A C   
2999 O  O   . ARG   A 141 ? 0.1400 0.1619 0.2056 -0.0151 0.0043  0.0121  141 ARG   A O   
3000 C  CB  . ARG   A 141 ? 0.1555 0.2048 0.2319 -0.0316 -0.0068 -0.0116 141 ARG   A CB  
3001 C  CG  . ARG   A 141 ? 0.1897 0.2432 0.2630 -0.0317 0.0150  -0.0199 141 ARG   A CG  
3002 C  CD  . ARG   A 141 ? 0.2218 0.2699 0.3022 -0.0397 0.0144  -0.0280 141 ARG   A CD  
3003 N  NE  . ARG   A 141 ? 0.2133 0.2908 0.3205 -0.0429 -0.0028 -0.0249 141 ARG   A NE  
3004 C  CZ  . ARG   A 141 ? 0.2201 0.3185 0.3293 -0.0594 0.0083  -0.0138 141 ARG   A CZ  
3005 N  NH1 . ARG   A 141 ? 0.2083 0.3216 0.3134 -0.0750 0.0337  -0.0295 141 ARG   A NH1 
3006 N  NH2 . ARG   A 141 ? 0.2286 0.3328 0.3535 -0.0562 -0.0026 0.0050  141 ARG   A NH2 
3020 N  N   . VAL   A 142 ? 0.1361 0.1594 0.1784 -0.0122 -0.0006 0.0106  142 VAL   A N   
3021 C  CA  . VAL   A 142 ? 0.1443 0.1607 0.1791 -0.0063 0.0125  0.0111  142 VAL   A CA  
3022 C  C   . VAL   A 142 ? 0.1234 0.1516 0.1830 -0.0114 0.0097  0.0136  142 VAL   A C   
3023 O  O   . VAL   A 142 ? 0.1287 0.1491 0.2014 -0.0030 0.0108  0.0164  142 VAL   A O   
3024 C  CB  . VAL   A 142 ? 0.1495 0.1604 0.1738 -0.0066 0.0157  0.0192  142 VAL   A CB  
3025 C  CG1 . VAL   A 142 ? 0.1505 0.1540 0.1833 -0.0189 0.0208  0.0055  142 VAL   A CG1 
3026 C  CG2 . VAL   A 142 ? 0.1576 0.1772 0.2000 -0.0011 0.0171  0.0167  142 VAL   A CG2 
3036 N  N   . CYS   A 143 ? 0.1295 0.1485 0.1738 -0.0134 0.0097  0.0143  143 CYS   A N   
3037 C  CA  . CYS   A 143 ? 0.1343 0.1514 0.1824 -0.0094 0.0126  0.0209  143 CYS   A CA  
3038 C  C   . CYS   A 143 ? 0.1312 0.1423 0.1866 -0.0103 0.0096  0.0263  143 CYS   A C   
3039 O  O   . CYS   A 143 ? 0.1311 0.1408 0.1898 -0.0081 0.0020  0.0278  143 CYS   A O   
3040 C  CB  . CYS   A 143 ? 0.1422 0.1518 0.1885 -0.0094 0.0197  0.0233  143 CYS   A CB  
3041 S  SG  . CYS   A 143 ? 0.1584 0.1608 0.1736 0.0016  0.0150  0.0189  143 CYS   A SG  
3047 N  N   . VAL   A 144 ? 0.1329 0.1545 0.1950 -0.0134 0.0122  0.0312  144 VAL   A N   
3048 C  CA  . VAL   A 144 ? 0.1403 0.1656 0.2318 -0.0191 0.0191  0.0316  144 VAL   A CA  
3049 C  C   . VAL   A 144 ? 0.1385 0.1603 0.2308 -0.0183 -0.0081 0.0258  144 VAL   A C   
3050 O  O   . VAL   A 144 ? 0.1526 0.1591 0.2402 -0.0071 -0.0138 0.0362  144 VAL   A O   
3051 C  CB  . VAL   A 144 ? 0.1649 0.1792 0.2993 -0.0070 0.0357  0.0418  144 VAL   A CB  
3052 C  CG1 . VAL   A 144 ? 0.1821 0.2002 0.3377 -0.0147 0.0178  0.0375  144 VAL   A CG1 
3053 C  CG2 . VAL   A 144 ? 0.1552 0.1844 0.3142 -0.0077 0.0452  0.0539  144 VAL   A CG2 
3063 N  N   . ASP   A 145 ? 0.1422 0.1517 0.2371 -0.0150 0.0001  0.0172  145 ASP   A N   
3064 C  CA  . ASP   A 145 ? 0.1540 0.1557 0.2477 -0.0203 -0.0023 0.0069  145 ASP   A CA  
3065 C  C   . ASP   A 145 ? 0.1467 0.1510 0.2469 -0.0154 -0.0036 0.0009  145 ASP   A C   
3066 O  O   . ASP   A 145 ? 0.1668 0.1612 0.2902 -0.0151 0.0005  -0.0291 145 ASP   A O   
3067 C  CB  . ASP   A 145 ? 0.1594 0.1863 0.2707 -0.0252 -0.0208 0.0061  145 ASP   A CB  
3068 C  CG  . ASP   A 145 ? 0.1776 0.2202 0.3035 -0.0438 -0.0364 0.0204  145 ASP   A CG  
3069 O  OD1 . ASP   A 145 ? 0.1743 0.2374 0.3091 -0.0582 -0.0214 0.0183  145 ASP   A OD1 
3070 O  OD2 . ASP   A 145 ? 0.2012 0.2417 0.3142 -0.0517 -0.0591 0.0221  145 ASP   A OD2 
3075 N  N   . THR   A 146 ? 0.1356 0.1386 0.2110 -0.0179 0.0068  0.0109  146 THR   A N   
3076 C  CA  . THR   A 146 ? 0.1320 0.1402 0.1929 -0.0076 0.0053  0.0095  146 THR   A CA  
3077 C  C   . THR   A 146 ? 0.1298 0.1393 0.1954 0.0009  0.0108  0.0224  146 THR   A C   
3078 O  O   . THR   A 146 ? 0.1457 0.1496 0.2109 0.0079  -0.0003 0.0150  146 THR   A O   
3079 C  CB  . THR   A 146 ? 0.1353 0.1436 0.1914 -0.0049 0.0081  0.0168  146 THR   A CB  
3080 O  OG1 . THR   A 146 ? 0.1377 0.1584 0.1935 0.0003  0.0003  0.0087  146 THR   A OG1 
3081 C  CG2 . THR   A 146 ? 0.1384 0.1485 0.2067 -0.0094 0.0161  0.0174  146 THR   A CG2 
3089 N  N   . VAL   A 147 ? 0.1254 0.1372 0.1898 -0.0000 0.0112  0.0144  147 VAL   A N   
3090 C  CA  . VAL   A 147 ? 0.1283 0.1467 0.1945 -0.0110 0.0260  0.0207  147 VAL   A CA  
3091 C  C   . VAL   A 147 ? 0.1410 0.1399 0.2096 -0.0163 0.0200  0.0325  147 VAL   A C   
3092 O  O   . VAL   A 147 ? 0.1448 0.1432 0.2206 -0.0201 0.0165  0.0250  147 VAL   A O   
3093 C  CB  . VAL   A 147 ? 0.1429 0.1481 0.1880 -0.0139 0.0247  0.0223  147 VAL   A CB  
3094 C  CG1 . VAL   A 147 ? 0.1694 0.1524 0.1915 -0.0148 0.0180  0.0193  147 VAL   A CG1 
3095 C  CG2 . VAL   A 147 ? 0.1469 0.1470 0.1792 -0.0130 0.0107  0.0138  147 VAL   A CG2 
3105 N  N   . ARG   A 148 ? 0.1403 0.1452 0.2114 -0.0191 0.0205  0.0423  148 ARG   A N   
3106 C  CA  . ARG   A 148 ? 0.1427 0.1479 0.2104 -0.0200 0.0153  0.0490  148 ARG   A CA  
3107 C  C   . ARG   A 148 ? 0.1554 0.1473 0.2070 -0.0244 0.0112  0.0642  148 ARG   A C   
3108 O  O   . ARG   A 148 ? 0.1818 0.1654 0.2348 -0.0250 0.0154  0.0624  148 ARG   A O   
3109 C  CB  . ARG   A 148 ? 0.1504 0.1551 0.2318 -0.0105 0.0264  0.0461  148 ARG   A CB  
3110 C  CG  . ARG   A 148 ? 0.1657 0.1504 0.2660 -0.0121 0.0374  0.0416  148 ARG   A CG  
3111 C  CD  . ARG   A 148 ? 0.1798 0.1501 0.2847 -0.0064 0.0426  0.0567  148 ARG   A CD  
3112 N  NE  . ARG   A 148 ? 0.1721 0.1532 0.2829 0.0063  0.0461  0.0538  148 ARG   A NE  
3113 C  CZ  . ARG   A 148 ? 0.1660 0.1416 0.2587 0.0047  0.0440  0.0424  148 ARG   A CZ  
3114 N  NH1 . ARG   A 148 ? 0.1708 0.1488 0.2662 -0.0069 0.0374  0.0248  148 ARG   A NH1 
3115 N  NH2 . ARG   A 148 ? 0.1605 0.1656 0.2652 0.0124  0.0480  0.0499  148 ARG   A NH2 
3129 N  N   . THR   A 149 ? 0.1562 0.1642 0.1888 -0.0237 -0.0083 0.0539  149 THR   A N   
3130 C  CA  . THR   A 149 ? 0.1566 0.1717 0.1901 -0.0190 0.0036  0.0535  149 THR   A CA  
3131 C  C   . THR   A 149 ? 0.1490 0.1637 0.1759 -0.0233 0.0038  0.0590  149 THR   A C   
3132 O  O   . THR   A 149 ? 0.1535 0.1761 0.2076 -0.0284 0.0029  0.0491  149 THR   A O   
3133 C  CB  . THR   A 149 ? 0.1578 0.1819 0.2064 -0.0180 0.0091  0.0438  149 THR   A CB  
3134 O  OG1 . THR   A 149 ? 0.1597 0.1690 0.2137 -0.0314 0.0120  0.0389  149 THR   A OG1 
3135 C  CG2 . THR   A 149 ? 0.1597 0.1873 0.2175 -0.0132 -0.0034 0.0340  149 THR   A CG2 
3143 N  N   . ASN   A 150 ? 0.1542 0.1650 0.1850 -0.0144 -0.0004 0.0605  150 ASN   A N   
3144 C  CA  . ASN   A 150 ? 0.1720 0.1780 0.1775 -0.0180 0.0085  0.0516  150 ASN   A CA  
3145 C  C   . ASN   A 150 ? 0.1532 0.1662 0.1810 -0.0228 0.0023  0.0519  150 ASN   A C   
3146 O  O   . ASN   A 150 ? 0.1594 0.1778 0.2159 -0.0200 -0.0182 0.0478  150 ASN   A O   
3147 C  CB  . ASN   A 150 ? 0.2185 0.2028 0.2101 -0.0243 0.0312  0.0678  150 ASN   A CB  
3148 C  CG  . ASN   A 150 ? 0.2689 0.2343 0.2846 -0.0172 0.0130  0.0728  150 ASN   A CG  
3149 O  OD1 . ASN   A 150 ? 0.2882 0.2453 0.3056 -0.0213 0.0198  0.0880  150 ASN   A OD1 
3150 N  ND2 . ASN   A 150 ? 0.2986 0.2576 0.3238 -0.0107 -0.0037 0.0654  150 ASN   A ND2 
3157 N  N   . VAL   A 151 ? 0.1558 0.1568 0.1838 -0.0216 0.0027  0.0544  151 VAL   A N   
3158 C  CA  . VAL   A 151 ? 0.1602 0.1574 0.1818 -0.0154 0.0121  0.0493  151 VAL   A CA  
3159 C  C   . VAL   A 151 ? 0.1474 0.1490 0.1820 -0.0251 0.0097  0.0446  151 VAL   A C   
3160 O  O   . VAL   A 151 ? 0.1559 0.1599 0.2155 -0.0222 0.0086  0.0383  151 VAL   A O   
3161 C  CB  . VAL   A 151 ? 0.1863 0.1707 0.1922 -0.0027 0.0105  0.0431  151 VAL   A CB  
3162 C  CG1 . VAL   A 151 ? 0.1866 0.1912 0.2152 -0.0107 -0.0003 0.0437  151 VAL   A CG1 
3163 C  CG2 . VAL   A 151 ? 0.1957 0.1639 0.1913 0.0025  0.0284  0.0304  151 VAL   A CG2 
3173 N  N   . TYR   A 152 ? 0.1471 0.1543 0.1861 -0.0247 0.0058  0.0407  152 TYR   A N   
3174 C  CA  . TYR   A 152 ? 0.1490 0.1647 0.1622 -0.0249 0.0115  0.0432  152 TYR   A CA  
3175 C  C   . TYR   A 152 ? 0.1409 0.1574 0.1587 -0.0195 0.0174  0.0368  152 TYR   A C   
3176 O  O   . TYR   A 152 ? 0.1484 0.1528 0.1652 -0.0252 0.0204  0.0304  152 TYR   A O   
3177 C  CB  . TYR   A 152 ? 0.1707 0.1695 0.1714 -0.0239 0.0206  0.0449  152 TYR   A CB  
3178 C  CG  . TYR   A 152 ? 0.1761 0.1927 0.1643 -0.0240 0.0265  0.0464  152 TYR   A CG  
3179 C  CD1 . TYR   A 152 ? 0.1826 0.2115 0.1853 -0.0143 0.0286  0.0509  152 TYR   A CD1 
3180 C  CD2 . TYR   A 152 ? 0.1847 0.1997 0.1648 -0.0420 0.0210  0.0426  152 TYR   A CD2 
3181 C  CE1 . TYR   A 152 ? 0.2160 0.2274 0.1970 -0.0118 0.0076  0.0629  152 TYR   A CE1 
3182 C  CE2 . TYR   A 152 ? 0.2094 0.2168 0.1879 -0.0423 0.0228  0.0536  152 TYR   A CE2 
3183 C  CZ  . TYR   A 152 ? 0.2314 0.2254 0.1875 -0.0282 0.0098  0.0780  152 TYR   A CZ  
3184 O  OH  . TYR   A 152 ? 0.2586 0.2498 0.2195 -0.0229 0.0085  0.0842  152 TYR   A OH  
3194 N  N   A LEU   A 153 ? 0.1390 0.1512 0.1735 -0.0267 0.0148  0.0416  153 LEU   A N   
3195 N  N   B LEU   A 153 ? 0.1429 0.1617 0.1564 -0.0216 0.0127  0.0374  153 LEU   A N   
3196 C  CA  A LEU   A 153 ? 0.1319 0.1485 0.1775 -0.0132 0.0190  0.0363  153 LEU   A CA  
3197 C  CA  B LEU   A 153 ? 0.1409 0.1641 0.1451 -0.0147 0.0150  0.0328  153 LEU   A CA  
3198 C  C   A LEU   A 153 ? 0.1367 0.1427 0.1816 -0.0150 0.0280  0.0251  153 LEU   A C   
3199 C  C   B LEU   A 153 ? 0.1446 0.1683 0.1368 -0.0113 0.0179  0.0293  153 LEU   A C   
3200 O  O   A LEU   A 153 ? 0.1480 0.1495 0.2119 -0.0189 0.0422  0.0113  153 LEU   A O   
3201 O  O   B LEU   A 153 ? 0.1490 0.1749 0.1501 -0.0157 0.0310  0.0301  153 LEU   A O   
3202 C  CB  A LEU   A 153 ? 0.1250 0.1418 0.1809 -0.0100 0.0173  0.0360  153 LEU   A CB  
3203 C  CB  B LEU   A 153 ? 0.1377 0.1623 0.1457 -0.0130 0.0129  0.0392  153 LEU   A CB  
3204 C  CG  A LEU   A 153 ? 0.1294 0.1458 0.1839 -0.0101 0.0204  0.0249  153 LEU   A CG  
3205 C  CG  B LEU   A 153 ? 0.1430 0.1683 0.1528 -0.0106 0.0130  0.0329  153 LEU   A CG  
3206 C  CD1 A LEU   A 153 ? 0.1466 0.1401 0.1928 -0.0107 0.0038  0.0275  153 LEU   A CD1 
3207 C  CD1 B LEU   A 153 ? 0.1482 0.1704 0.1671 -0.0045 0.0108  0.0342  153 LEU   A CD1 
3208 C  CD2 A LEU   A 153 ? 0.1314 0.1504 0.1703 -0.0116 0.0176  0.0091  153 LEU   A CD2 
3209 C  CD2 B LEU   A 153 ? 0.1467 0.1722 0.1531 -0.0165 0.0082  0.0284  153 LEU   A CD2 
3232 N  N   A ALA   A 154 ? 0.1264 0.1412 0.1768 -0.0154 0.0244  0.0283  154 ALA   A N   
3233 N  N   B ALA   A 154 ? 0.1429 0.1654 0.1217 -0.0065 0.0051  0.0179  154 ALA   A N   
3234 C  CA  A ALA   A 154 ? 0.1399 0.1477 0.1611 -0.0129 0.0323  0.0179  154 ALA   A CA  
3235 C  CA  B ALA   A 154 ? 0.1483 0.1633 0.1252 -0.0060 -0.0023 0.0106  154 ALA   A CA  
3236 C  C   A ALA   A 154 ? 0.1385 0.1382 0.1561 -0.0082 0.0294  0.0189  154 ALA   A C   
3237 C  C   B ALA   A 154 ? 0.1487 0.1634 0.1078 -0.0071 -0.0128 0.0043  154 ALA   A C   
3238 O  O   A ALA   A 154 ? 0.1489 0.1571 0.1599 -0.0146 0.0261  0.0112  154 ALA   A O   
3239 O  O   B ALA   A 154 ? 0.1556 0.1666 0.0844 -0.0163 -0.0154 0.0050  154 ALA   A O   
3240 C  CB  A ALA   A 154 ? 0.1592 0.1576 0.1628 -0.0052 0.0209  0.0133  154 ALA   A CB  
3241 C  CB  B ALA   A 154 ? 0.1517 0.1609 0.1341 -0.0064 -0.0155 0.0081  154 ALA   A CB  
3252 N  N   A VAL   A 155 ? 0.1206 0.1129 0.1230 0.0064  0.0339  0.0308  155 VAL   A N   
3253 N  N   B VAL   A 155 ? 0.1496 0.1611 0.1151 0.0001  -0.0076 0.0081  155 VAL   A N   
3254 C  CA  A VAL   A 155 ? 0.1402 0.1286 0.1656 0.0073  0.0257  0.0384  155 VAL   A CA  
3255 C  CA  B VAL   A 155 ? 0.1681 0.1758 0.1447 0.0028  -0.0169 -0.0003 155 VAL   A CA  
3256 C  CA  T VAL   A 155 ? 0.1666 0.1600 0.1603 -0.0188 0.0295  0.0393  155 VAL   A CA  
3257 C  C   A VAL   A 155 ? 0.1500 0.1453 0.1902 0.0242  0.0266  0.0500  155 VAL   A C   
3258 C  C   B VAL   A 155 ? 0.1831 0.1946 0.1820 0.0156  -0.0212 -0.0022 155 VAL   A C   
3259 C  C   T VAL   A 155 ? 0.1709 0.1665 0.1481 -0.0058 0.0364  0.0500  155 VAL   A C   
3260 O  O   A VAL   A 155 ? 0.1488 0.1498 0.2101 0.0310  0.0392  0.0321  155 VAL   A O   
3261 O  O   B VAL   A 155 ? 0.1775 0.1956 0.1793 0.0196  -0.0244 -0.0130 155 VAL   A O   
3262 O  O   T VAL   A 155 ? 0.1667 0.1741 0.1384 -0.0051 0.0379  0.0462  155 VAL   A O   
3263 C  CB  A VAL   A 155 ? 0.1547 0.1364 0.1834 0.0083  0.0042  0.0358  155 VAL   A CB  
3264 C  CB  B VAL   A 155 ? 0.1738 0.1711 0.1505 0.0006  -0.0228 -0.0128 155 VAL   A CB  
3265 C  CB  T VAL   A 155 ? 0.1686 0.1613 0.1779 -0.0191 0.0132  0.0271  155 VAL   A CB  
3266 C  CG1 A VAL   A 155 ? 0.1685 0.1447 0.1808 0.0127  -0.0008 0.0328  155 VAL   A CG1 
3267 C  CG1 B VAL   A 155 ? 0.1781 0.1692 0.1578 0.0005  -0.0242 -0.0150 155 VAL   A CG1 
3268 C  CG1 T VAL   A 155 ? 0.1759 0.1646 0.1810 -0.0142 0.0079  0.0199  155 VAL   A CG1 
3269 C  CG2 A VAL   A 155 ? 0.1666 0.1442 0.2077 0.0072  -0.0158 0.0338  155 VAL   A CG2 
3270 C  CG2 B VAL   A 155 ? 0.1820 0.1710 0.1562 0.0003  -0.0268 -0.0117 155 VAL   A CG2 
3271 C  CG2 T VAL   A 155 ? 0.1717 0.1644 0.1928 -0.0196 0.0012  0.0256  155 VAL   A CG2 
3297 N  N   A PHE   A 156 ? 0.1633 0.1593 0.2246 0.0310  0.0310  0.0693  156 PHE   A N   
3298 N  N   B PHE   A 156 ? 0.2013 0.2106 0.2161 0.0242  -0.0149 0.0036  156 PHE   A N   
3299 N  N   T PHE   A 156 ? 0.1820 0.1665 0.1641 0.0022  0.0440  0.0596  156 PHE   A N   
3300 C  CA  A PHE   A 156 ? 0.1837 0.1693 0.2585 0.0372  0.0320  0.0712  156 PHE   A CA  
3301 C  CA  B PHE   A 156 ? 0.2260 0.2326 0.2546 0.0269  -0.0025 0.0042  156 PHE   A CA  
3302 C  CA  T PHE   A 156 ? 0.1982 0.1643 0.1721 0.0072  0.0459  0.0563  156 PHE   A CA  
3303 C  C   A PHE   A 156 ? 0.1761 0.1640 0.2557 0.0451  0.0536  0.0847  156 PHE   A C   
3304 C  C   B PHE   A 156 ? 0.2411 0.2507 0.2665 0.0241  -0.0015 0.0144  156 PHE   A C   
3305 C  C   T PHE   A 156 ? 0.1994 0.1714 0.1796 0.0132  0.0530  0.0572  156 PHE   A C   
3306 O  O   A PHE   A 156 ? 0.1862 0.1637 0.2693 0.0344  0.0588  0.0797  156 PHE   A O   
3307 O  O   B PHE   A 156 ? 0.2487 0.2525 0.2741 0.0223  -0.0018 0.0167  156 PHE   A O   
3308 O  O   T PHE   A 156 ? 0.2057 0.1713 0.1803 0.0163  0.0576  0.0422  156 PHE   A O   
3309 C  CB  A PHE   A 156 ? 0.2019 0.1801 0.2737 0.0323  0.0158  0.0645  156 PHE   A CB  
3310 C  CB  B PHE   A 156 ? 0.2402 0.2422 0.2719 0.0240  0.0084  -0.0053 156 PHE   A CB  
3311 C  CB  T PHE   A 156 ? 0.2021 0.1514 0.1601 0.0093  0.0441  0.0563  156 PHE   A CB  
3312 C  CG  A PHE   A 156 ? 0.2189 0.1864 0.2915 0.0333  0.0091  0.0555  156 PHE   A CG  
3313 C  CG  B PHE   A 156 ? 0.2542 0.2507 0.2891 0.0242  0.0130  -0.0149 156 PHE   A CG  
3314 C  CG  T PHE   A 156 ? 0.2054 0.1415 0.1521 0.0171  0.0429  0.0609  156 PHE   A CG  
3315 C  CD1 A PHE   A 156 ? 0.2243 0.1887 0.2999 0.0403  0.0205  0.0493  156 PHE   A CD1 
3316 C  CD1 B PHE   A 156 ? 0.2602 0.2546 0.2984 0.0267  0.0134  -0.0202 156 PHE   A CD1 
3317 C  CD1 T PHE   A 156 ? 0.2044 0.1419 0.1842 0.0162  0.0326  0.0466  156 PHE   A CD1 
3318 C  CD2 A PHE   A 156 ? 0.2313 0.1980 0.2997 0.0362  0.0050  0.0518  156 PHE   A CD2 
3319 C  CD2 B PHE   A 156 ? 0.2572 0.2526 0.2972 0.0243  0.0119  -0.0225 156 PHE   A CD2 
3320 C  CD2 T PHE   A 156 ? 0.2087 0.1404 0.1617 0.0214  0.0392  0.0677  156 PHE   A CD2 
3321 C  CE1 A PHE   A 156 ? 0.2344 0.1935 0.3066 0.0406  0.0269  0.0383  156 PHE   A CE1 
3322 C  CE1 B PHE   A 156 ? 0.2625 0.2567 0.3013 0.0274  0.0114  -0.0257 156 PHE   A CE1 
3323 C  CE1 T PHE   A 156 ? 0.2073 0.1404 0.1914 0.0198  0.0337  0.0382  156 PHE   A CE1 
3324 C  CE2 A PHE   A 156 ? 0.2414 0.2049 0.3066 0.0371  0.0103  0.0367  156 PHE   A CE2 
3325 C  CE2 B PHE   A 156 ? 0.2616 0.2545 0.3019 0.0233  0.0101  -0.0276 156 PHE   A CE2 
3326 C  CE2 T PHE   A 156 ? 0.2097 0.1394 0.1747 0.0198  0.0385  0.0581  156 PHE   A CE2 
3327 C  CZ  A PHE   A 156 ? 0.2410 0.2041 0.3082 0.0410  0.0252  0.0311  156 PHE   A CZ  
3328 C  CZ  B PHE   A 156 ? 0.2640 0.2569 0.3003 0.0262  0.0093  -0.0306 156 PHE   A CZ  
3329 C  CZ  T PHE   A 156 ? 0.2067 0.1310 0.1871 0.0131  0.0396  0.0470  156 PHE   A CZ  
3357 N  N   A ASP   A 157 ? 0.1676 0.1743 0.2485 0.0552  0.0548  0.0911  157 ASP   A N   
3358 N  N   B ASP   A 157 ? 0.2447 0.2617 0.2620 0.0231  -0.0030 0.0209  157 ASP   A N   
3359 N  N   T ASP   A 157 ? 0.1872 0.1827 0.1937 0.0142  0.0458  0.0658  157 ASP   A N   
3360 C  CA  A ASP   A 157 ? 0.1833 0.2017 0.2580 0.0596  0.0531  0.0882  157 ASP   A CA  
3361 C  CA  B ASP   A 157 ? 0.2502 0.2762 0.2694 0.0182  -0.0010 0.0307  157 ASP   A CA  
3362 C  CA  T ASP   A 157 ? 0.1830 0.1973 0.2074 0.0206  0.0391  0.0685  157 ASP   A CA  
3363 C  C   A ASP   A 157 ? 0.1713 0.2229 0.2671 0.0614  0.0481  0.0937  157 ASP   A C   
3364 C  C   B ASP   A 157 ? 0.2400 0.2779 0.2736 0.0250  -0.0053 0.0388  157 ASP   A C   
3365 C  C   T ASP   A 157 ? 0.1855 0.2155 0.2206 0.0283  0.0408  0.0796  157 ASP   A C   
3366 O  O   A ASP   A 157 ? 0.1625 0.2246 0.2669 0.0580  0.0496  0.0960  157 ASP   A O   
3367 O  O   B ASP   A 157 ? 0.2363 0.2785 0.2744 0.0265  -0.0098 0.0404  157 ASP   A O   
3368 O  O   T ASP   A 157 ? 0.1780 0.2160 0.2234 0.0273  0.0466  0.0822  157 ASP   A O   
3369 C  CB  A ASP   A 157 ? 0.2165 0.2071 0.2810 0.0660  0.0419  0.0791  157 ASP   A CB  
3370 C  CB  B ASP   A 157 ? 0.2651 0.2873 0.2769 0.0080  0.0047  0.0323  157 ASP   A CB  
3371 C  CB  T ASP   A 157 ? 0.1762 0.1918 0.2198 0.0224  0.0276  0.0617  157 ASP   A CB  
3372 C  CG  A ASP   A 157 ? 0.2377 0.2098 0.3021 0.0744  0.0343  0.0767  157 ASP   A CG  
3373 C  CG  B ASP   A 157 ? 0.2765 0.2947 0.2845 0.0005  0.0132  0.0375  157 ASP   A CG  
3374 C  CG  T ASP   A 157 ? 0.1538 0.1774 0.2244 0.0291  0.0134  0.0611  157 ASP   A CG  
3375 O  OD1 A ASP   A 157 ? 0.2598 0.2147 0.3225 0.0691  0.0228  0.0766  157 ASP   A OD1 
3376 O  OD1 B ASP   A 157 ? 0.2850 0.2971 0.2929 -0.0022 0.0229  0.0431  157 ASP   A OD1 
3377 O  OD1 T ASP   A 157 ? 0.1446 0.1586 0.2388 0.0284  0.0137  0.0446  157 ASP   A OD1 
3378 O  OD2 A ASP   A 157 ? 0.2305 0.2024 0.3043 0.0786  0.0436  0.0899  157 ASP   A OD2 
3379 O  OD2 B ASP   A 157 ? 0.2834 0.2978 0.2853 -0.0004 0.0109  0.0369  157 ASP   A OD2 
3380 O  OD2 T ASP   A 157 ? 0.1331 0.1777 0.2090 0.0363  0.0002  0.0809  157 ASP   A OD2 
3393 N  N   A LYS   A 158 ? 0.1795 0.2450 0.2840 0.0608  0.0507  0.0754  158 LYS   A N   
3394 N  N   B LYS   A 158 ? 0.2345 0.2776 0.2715 0.0295  -0.0054 0.0421  158 LYS   A N   
3395 N  N   T LYS   A 158 ? 0.2006 0.2350 0.2380 0.0333  0.0378  0.0677  158 LYS   A N   
3396 C  CA  A LYS   A 158 ? 0.1831 0.2682 0.2948 0.0632  0.0584  0.0583  158 LYS   A CA  
3397 C  CA  B LYS   A 158 ? 0.2336 0.2812 0.2678 0.0301  0.0064  0.0416  158 LYS   A CA  
3398 C  CA  T LYS   A 158 ? 0.2145 0.2567 0.2590 0.0369  0.0345  0.0542  158 LYS   A CA  
3399 C  C   A LYS   A 158 ? 0.1757 0.2732 0.2724 0.0618  0.0421  0.0547  158 LYS   A C   
3400 C  C   B LYS   A 158 ? 0.2119 0.2787 0.2336 0.0380  0.0022  0.0451  158 LYS   A C   
3401 C  C   T LYS   A 158 ? 0.2147 0.2599 0.2491 0.0376  0.0225  0.0444  158 LYS   A C   
3402 O  O   A LYS   A 158 ? 0.1753 0.2803 0.2762 0.0571  0.0505  0.0500  158 LYS   A O   
3403 O  O   B LYS   A 158 ? 0.2008 0.2819 0.2109 0.0348  0.0026  0.0503  158 LYS   A O   
3404 O  O   T LYS   A 158 ? 0.2150 0.2607 0.2514 0.0367  0.0225  0.0392  158 LYS   A O   
3405 C  CB  A LYS   A 158 ? 0.2094 0.2809 0.3337 0.0603  0.0781  0.0502  158 LYS   A CB  
3406 C  CB  B LYS   A 158 ? 0.2504 0.2892 0.2966 0.0237  0.0190  0.0356  158 LYS   A CB  
3407 C  CB  T LYS   A 158 ? 0.2367 0.2727 0.2996 0.0361  0.0435  0.0455  158 LYS   A CB  
3408 C  CG  A LYS   A 158 ? 0.2390 0.2938 0.3711 0.0563  0.0879  0.0515  158 LYS   A CG  
3409 C  CG  B LYS   A 158 ? 0.2645 0.2975 0.3275 0.0179  0.0321  0.0312  158 LYS   A CG  
3410 C  CG  T LYS   A 158 ? 0.2578 0.2870 0.3373 0.0358  0.0496  0.0438  158 LYS   A CG  
3411 C  CD  A LYS   A 158 ? 0.2591 0.3041 0.3989 0.0547  0.0961  0.0617  158 LYS   A CD  
3412 C  CD  B LYS   A 158 ? 0.2747 0.3036 0.3553 0.0139  0.0432  0.0318  158 LYS   A CD  
3413 C  CD  T LYS   A 158 ? 0.2736 0.2979 0.3719 0.0385  0.0509  0.0464  158 LYS   A CD  
3414 C  CE  A LYS   A 158 ? 0.2739 0.3086 0.4185 0.0500  0.1002  0.0745  158 LYS   A CE  
3415 C  CE  B LYS   A 158 ? 0.2802 0.3069 0.3772 0.0129  0.0529  0.0334  158 LYS   A CE  
3416 C  CE  T LYS   A 158 ? 0.2867 0.3046 0.3984 0.0392  0.0487  0.0506  158 LYS   A CE  
3417 N  NZ  A LYS   A 158 ? 0.2802 0.3112 0.4284 0.0452  0.1051  0.0827  158 LYS   A NZ  
3418 N  NZ  B LYS   A 158 ? 0.2814 0.3089 0.3906 0.0098  0.0576  0.0346  158 LYS   A NZ  
3419 N  NZ  T LYS   A 158 ? 0.2935 0.3086 0.4115 0.0394  0.0481  0.0530  158 LYS   A NZ  
3459 N  N   A ASN   A 159 ? 0.1710 0.2678 0.2654 0.0533  0.0151  0.0508  159 ASN   A N   
3460 N  N   B ASN   A 159 ? 0.2040 0.2751 0.2276 0.0471  -0.0037 0.0393  159 ASN   A N   
3461 N  N   T ASN   A 159 ? 0.2176 0.2610 0.2536 0.0332  0.0102  0.0357  159 ASN   A N   
3462 C  CA  A ASN   A 159 ? 0.1750 0.2648 0.2604 0.0374  -0.0068 0.0526  159 ASN   A CA  
3463 C  CA  B ASN   A 159 ? 0.1992 0.2722 0.2255 0.0482  -0.0044 0.0340  159 ASN   A CA  
3464 C  CA  T ASN   A 159 ? 0.2274 0.2644 0.2601 0.0257  0.0007  0.0322  159 ASN   A CA  
3465 C  C   A ASN   A 159 ? 0.1637 0.2624 0.2457 0.0263  -0.0003 0.0492  159 ASN   A C   
3466 C  C   B ASN   A 159 ? 0.1849 0.2703 0.2223 0.0467  -0.0017 0.0356  159 ASN   A C   
3467 C  C   T ASN   A 159 ? 0.2340 0.2679 0.2616 0.0220  0.0092  0.0253  159 ASN   A C   
3468 O  O   A ASN   A 159 ? 0.1483 0.2577 0.2466 0.0290  -0.0051 0.0273  159 ASN   A O   
3469 O  O   B ASN   A 159 ? 0.1730 0.2787 0.2325 0.0560  -0.0094 0.0360  159 ASN   A O   
3470 O  O   T ASN   A 159 ? 0.2304 0.2648 0.2659 0.0220  0.0121  0.0141  159 ASN   A O   
3471 C  CB  A ASN   A 159 ? 0.1887 0.2681 0.2789 0.0347  -0.0181 0.0558  159 ASN   A CB  
3472 C  CB  B ASN   A 159 ? 0.2049 0.2723 0.2409 0.0462  -0.0031 0.0239  159 ASN   A CB  
3473 C  CB  T ASN   A 159 ? 0.2318 0.2668 0.2721 0.0238  -0.0089 0.0356  159 ASN   A CB  
3474 C  CG  A ASN   A 159 ? 0.2036 0.2783 0.3117 0.0311  -0.0192 0.0530  159 ASN   A CG  
3475 C  CG  B ASN   A 159 ? 0.2110 0.2748 0.2596 0.0351  0.0065  0.0070  159 ASN   A CG  
3476 C  CG  T ASN   A 159 ? 0.2373 0.2726 0.2927 0.0217  -0.0129 0.0359  159 ASN   A CG  
3477 O  OD1 A ASN   A 159 ? 0.2114 0.2905 0.3336 0.0261  -0.0086 0.0494  159 ASN   A OD1 
3478 O  OD1 B ASN   A 159 ? 0.2160 0.2798 0.2619 0.0312  0.0085  -0.0045 159 ASN   A OD1 
3479 O  OD1 T ASN   A 159 ? 0.2401 0.2805 0.3084 0.0192  -0.0061 0.0337  159 ASN   A OD1 
3480 N  ND2 A ASN   A 159 ? 0.2106 0.2816 0.3208 0.0313  -0.0265 0.0491  159 ASN   A ND2 
3481 N  ND2 B ASN   A 159 ? 0.2113 0.2749 0.2681 0.0314  0.0089  0.0091  159 ASN   A ND2 
3482 N  ND2 T ASN   A 159 ? 0.2404 0.2748 0.2973 0.0223  -0.0199 0.0345  159 ASN   A ND2 
3501 N  N   A LEU   A 160 ? 0.1554 0.2547 0.2328 0.0226  0.0037  0.0694  160 LEU   A N   
3502 N  N   B LEU   A 160 ? 0.1798 0.2613 0.2107 0.0382  0.0026  0.0463  160 LEU   A N   
3503 N  N   T LEU   A 160 ? 0.2400 0.2688 0.2608 0.0222  0.0107  0.0309  160 LEU   A N   
3504 C  CA  A LEU   A 160 ? 0.1495 0.2459 0.2170 0.0153  0.0234  0.0888  160 LEU   A CA  
3505 C  CA  B LEU   A 160 ? 0.1791 0.2526 0.2050 0.0317  0.0116  0.0515  160 LEU   A CA  
3506 C  CA  T LEU   A 160 ? 0.2492 0.2681 0.2590 0.0193  0.0182  0.0389  160 LEU   A CA  
3507 C  C   A LEU   A 160 ? 0.1267 0.2479 0.2036 0.0126  0.0336  0.0868  160 LEU   A C   
3508 C  C   B LEU   A 160 ? 0.1664 0.2478 0.1939 0.0319  0.0138  0.0519  160 LEU   A C   
3509 O  O   A LEU   A 160 ? 0.1120 0.2516 0.2050 0.0096  0.0228  0.0954  160 LEU   A O   
3510 O  O   B LEU   A 160 ? 0.1561 0.2470 0.1921 0.0369  0.0087  0.0540  160 LEU   A O   
3511 C  CB  A LEU   A 160 ? 0.1502 0.2388 0.2101 0.0112  0.0229  0.1023  160 LEU   A CB  
3512 C  CB  B LEU   A 160 ? 0.1901 0.2529 0.2087 0.0245  0.0163  0.0471  160 LEU   A CB  
3513 C  CB  T LEU   A 160 ? 0.2543 0.2687 0.2569 0.0177  0.0214  0.0459  160 LEU   A CB  
3514 C  CG  A LEU   A 160 ? 0.1501 0.2373 0.2147 0.0035  0.0206  0.0908  160 LEU   A CG  
3515 C  CG  B LEU   A 160 ? 0.2035 0.2560 0.2259 0.0189  0.0202  0.0341  160 LEU   A CG  
3516 C  CG  T LEU   A 160 ? 0.2592 0.2696 0.2567 0.0165  0.0222  0.0452  160 LEU   A CG  
3517 C  CD1 A LEU   A 160 ? 0.1567 0.2435 0.2242 -0.0022 0.0225  0.0809  160 LEU   A CD1 
3518 C  CD1 B LEU   A 160 ? 0.2064 0.2553 0.2343 0.0196  0.0190  0.0301  160 LEU   A CD1 
3519 C  CD1 T LEU   A 160 ? 0.2572 0.2668 0.2486 0.0119  0.0286  0.0474  160 LEU   A CD1 
3520 C  CD2 A LEU   A 160 ? 0.1463 0.2358 0.2283 0.0013  0.0222  0.0734  160 LEU   A CD2 
3521 C  CD2 B LEU   A 160 ? 0.2090 0.2592 0.2279 0.0162  0.0276  0.0285  160 LEU   A CD2 
3522 C  CD2 T LEU   A 160 ? 0.2599 0.2680 0.2547 0.0194  0.0213  0.0526  160 LEU   A CD2 
3555 N  N   A TYR   A 161 ? 0.1403 0.2412 0.2228 0.0077  0.0279  0.0894  161 TYR   A N   
3556 N  N   B TYR   A 161 ? 0.1723 0.2418 0.1928 0.0285  0.0192  0.0495  161 TYR   A N   
3557 C  CA  A TYR   A 161 ? 0.1532 0.2404 0.2263 0.0003  0.0306  0.0824  161 TYR   A CA  
3558 C  CA  B TYR   A 161 ? 0.1804 0.2373 0.1956 0.0235  0.0242  0.0444  161 TYR   A CA  
3559 C  C   A TYR   A 161 ? 0.1517 0.2651 0.2326 -0.0066 0.0249  0.0800  161 TYR   A C   
3560 C  C   B TYR   A 161 ? 0.1829 0.2447 0.2127 0.0215  0.0210  0.0383  161 TYR   A C   
3561 O  O   A TYR   A 161 ? 0.1428 0.2661 0.2138 -0.0152 0.0147  0.0758  161 TYR   A O   
3562 O  O   B TYR   A 161 ? 0.1819 0.2457 0.2103 0.0167  0.0198  0.0315  161 TYR   A O   
3563 C  CB  A TYR   A 161 ? 0.1640 0.2236 0.2235 0.0006  0.0359  0.0758  161 TYR   A CB  
3564 C  CB  B TYR   A 161 ? 0.1864 0.2288 0.1832 0.0202  0.0309  0.0466  161 TYR   A CB  
3565 C  CG  A TYR   A 161 ? 0.1589 0.2049 0.2182 0.0016  0.0222  0.0544  161 TYR   A CG  
3566 C  CG  B TYR   A 161 ? 0.1875 0.2145 0.1768 0.0158  0.0360  0.0451  161 TYR   A CG  
3567 C  CD1 A TYR   A 161 ? 0.1547 0.1986 0.2256 0.0019  0.0162  0.0365  161 TYR   A CD1 
3568 C  CD1 B TYR   A 161 ? 0.1908 0.2098 0.1837 0.0154  0.0321  0.0412  161 TYR   A CD1 
3569 C  CD2 A TYR   A 161 ? 0.1590 0.1983 0.2212 0.0064  0.0131  0.0422  161 TYR   A CD2 
3570 C  CD2 B TYR   A 161 ? 0.1906 0.2065 0.1856 0.0139  0.0433  0.0490  161 TYR   A CD2 
3571 C  CE1 A TYR   A 161 ? 0.1536 0.1872 0.2207 0.0026  0.0115  0.0359  161 TYR   A CE1 
3572 C  CE1 B TYR   A 161 ? 0.1938 0.2070 0.1930 0.0166  0.0297  0.0380  161 TYR   A CE1 
3573 C  CE2 A TYR   A 161 ? 0.1558 0.1831 0.2177 0.0024  0.0060  0.0419  161 TYR   A CE2 
3574 C  CE2 B TYR   A 161 ? 0.1939 0.2047 0.1974 0.0116  0.0411  0.0439  161 TYR   A CE2 
3575 C  CZ  A TYR   A 161 ? 0.1622 0.1758 0.2136 -0.0057 0.0043  0.0453  161 TYR   A CZ  
3576 C  CZ  B TYR   A 161 ? 0.2007 0.2070 0.2051 0.0158  0.0330  0.0384  161 TYR   A CZ  
3577 O  OH  A TYR   A 161 ? 0.1786 0.1659 0.2221 -0.0109 -0.0013 0.0501  161 TYR   A OH  
3578 O  OH  B TYR   A 161 ? 0.2118 0.2111 0.2352 0.0159  0.0278  0.0335  161 TYR   A OH  
3597 N  N   A ASP   A 162 ? 0.1504 0.2897 0.2546 -0.0020 0.0356  0.0829  162 ASP   A N   
3598 N  N   B ASP   A 162 ? 0.1867 0.2522 0.2322 0.0219  0.0211  0.0386  162 ASP   A N   
3599 C  CA  A ASP   A 162 ? 0.1470 0.3183 0.2512 0.0004  0.0406  0.0764  162 ASP   A CA  
3600 C  CA  B ASP   A 162 ? 0.1926 0.2617 0.2438 0.0167  0.0167  0.0358  162 ASP   A CA  
3601 C  C   A ASP   A 162 ? 0.1431 0.3244 0.2299 -0.0067 0.0295  0.0867  162 ASP   A C   
3602 C  C   B ASP   A 162 ? 0.1921 0.2659 0.2414 0.0114  0.0118  0.0438  162 ASP   A C   
3603 O  O   A ASP   A 162 ? 0.1341 0.3296 0.2282 -0.0068 0.0271  0.0684  162 ASP   A O   
3604 O  O   B ASP   A 162 ? 0.1902 0.2665 0.2341 0.0033  0.0205  0.0428  162 ASP   A O   
3605 C  CB  A ASP   A 162 ? 0.1541 0.3416 0.2866 0.0071  0.0515  0.0555  162 ASP   A CB  
3606 C  CB  B ASP   A 162 ? 0.1993 0.2673 0.2615 0.0167  0.0154  0.0277  162 ASP   A CB  
3607 C  CG  A ASP   A 162 ? 0.1698 0.3626 0.3180 0.0118  0.0626  0.0411  162 ASP   A CG  
3608 C  CG  B ASP   A 162 ? 0.2072 0.2726 0.2823 0.0156  0.0135  0.0216  162 ASP   A CG  
3609 O  OD1 A ASP   A 162 ? 0.1862 0.3731 0.3308 0.0086  0.0628  0.0421  162 ASP   A OD1 
3610 O  OD1 B ASP   A 162 ? 0.2158 0.2761 0.2921 0.0129  0.0162  0.0193  162 ASP   A OD1 
3611 O  OD2 A ASP   A 162 ? 0.1843 0.3708 0.3396 0.0248  0.0631  0.0320  162 ASP   A OD2 
3612 O  OD2 B ASP   A 162 ? 0.2092 0.2735 0.2958 0.0162  0.0155  0.0199  162 ASP   A OD2 
3621 N  N   A LYS   A 163 ? 0.1533 0.3295 0.2282 -0.0064 0.0086  0.0886  163 LYS   A N   
3622 N  N   B LYS   A 163 ? 0.1937 0.2673 0.2478 0.0159  -0.0040 0.0512  163 LYS   A N   
3623 C  CA  A LYS   A 163 ? 0.1642 0.3355 0.2301 -0.0043 -0.0061 0.0827  163 LYS   A CA  
3624 C  CA  B LYS   A 163 ? 0.1964 0.2689 0.2532 0.0157  -0.0133 0.0539  163 LYS   A CA  
3625 C  C   A LYS   A 163 ? 0.1599 0.3212 0.2227 -0.0148 0.0047  0.0893  163 LYS   A C   
3626 C  C   B LYS   A 163 ? 0.1832 0.2591 0.2353 0.0103  -0.0063 0.0571  163 LYS   A C   
3627 O  O   A LYS   A 163 ? 0.1510 0.3248 0.2182 -0.0179 0.0054  0.0824  163 LYS   A O   
3628 O  O   B LYS   A 163 ? 0.1836 0.2648 0.2306 0.0068  -0.0017 0.0630  163 LYS   A O   
3629 C  CB  A LYS   A 163 ? 0.1965 0.3538 0.2684 0.0140  -0.0168 0.0647  163 LYS   A CB  
3630 C  CB  B LYS   A 163 ? 0.2151 0.2825 0.2857 0.0156  -0.0170 0.0457  163 LYS   A CB  
3631 C  CG  A LYS   A 163 ? 0.2302 0.3695 0.3274 0.0171  -0.0182 0.0447  163 LYS   A CG  
3632 C  CG  B LYS   A 163 ? 0.2345 0.2967 0.3181 0.0164  -0.0222 0.0353  163 LYS   A CG  
3633 C  CD  A LYS   A 163 ? 0.2599 0.3829 0.3899 0.0164  -0.0136 0.0312  163 LYS   A CD  
3634 C  CD  B LYS   A 163 ? 0.2446 0.3055 0.3445 0.0164  -0.0281 0.0259  163 LYS   A CD  
3635 C  CE  A LYS   A 163 ? 0.2817 0.3903 0.4304 0.0153  -0.0084 0.0261  163 LYS   A CE  
3636 C  CE  B LYS   A 163 ? 0.2535 0.3120 0.3671 0.0182  -0.0292 0.0181  163 LYS   A CE  
3637 N  NZ  A LYS   A 163 ? 0.2932 0.3960 0.4581 0.0123  -0.0050 0.0260  163 LYS   A NZ  
3638 N  NZ  B LYS   A 163 ? 0.2615 0.3163 0.3832 0.0194  -0.0289 0.0139  163 LYS   A NZ  
3665 N  N   A LEU   A 164 ? 0.1450 0.2991 0.2024 -0.0207 0.0036  0.0858  164 LEU   A N   
3666 N  N   B LEU   A 164 ? 0.1667 0.2417 0.2213 0.0037  0.0049  0.0518  164 LEU   A N   
3667 C  CA  A LEU   A 164 ? 0.1507 0.2843 0.1849 -0.0300 0.0153  0.0766  164 LEU   A CA  
3668 C  CA  B LEU   A 164 ? 0.1586 0.2251 0.1999 -0.0024 0.0182  0.0515  164 LEU   A CA  
3669 C  C   A LEU   A 164 ? 0.1535 0.2788 0.1849 -0.0283 0.0085  0.0688  164 LEU   A C   
3670 C  C   B LEU   A 164 ? 0.1601 0.2276 0.2006 -0.0012 0.0250  0.0492  164 LEU   A C   
3671 O  O   A LEU   A 164 ? 0.1554 0.2812 0.1973 -0.0271 0.0211  0.0509  164 LEU   A O   
3672 O  O   B LEU   A 164 ? 0.1538 0.2303 0.1957 -0.0021 0.0332  0.0471  164 LEU   A O   
3673 C  CB  A LEU   A 164 ? 0.1492 0.2771 0.1856 -0.0272 0.0246  0.0681  164 LEU   A CB  
3674 C  CB  B LEU   A 164 ? 0.1549 0.2118 0.1846 -0.0073 0.0226  0.0511  164 LEU   A CB  
3675 C  CG  A LEU   A 164 ? 0.1521 0.2749 0.1846 -0.0215 0.0188  0.0634  164 LEU   A CG  
3676 C  CG  B LEU   A 164 ? 0.1550 0.2049 0.1844 -0.0044 0.0185  0.0429  164 LEU   A CG  
3677 C  CD1 A LEU   A 164 ? 0.1408 0.2704 0.1833 -0.0134 0.0150  0.0674  164 LEU   A CD1 
3678 C  CD1 B LEU   A 164 ? 0.1522 0.2044 0.1856 -0.0015 0.0223  0.0328  164 LEU   A CD1 
3679 C  CD2 A LEU   A 164 ? 0.1646 0.2783 0.1835 -0.0235 0.0252  0.0546  164 LEU   A CD2 
3680 C  CD2 B LEU   A 164 ? 0.1529 0.2033 0.1770 -0.0052 0.0172  0.0362  164 LEU   A CD2 
3703 N  N   A VAL   A 165 ? 0.1463 0.2694 0.1769 -0.0300 0.0132  0.0801  165 VAL   A N   
3704 N  N   B VAL   A 165 ? 0.1614 0.2284 0.2045 0.0052  0.0194  0.0446  165 VAL   A N   
3705 C  CA  A VAL   A 165 ? 0.1502 0.2674 0.1752 -0.0241 0.0156  0.0861  165 VAL   A CA  
3706 C  CA  B VAL   A 165 ? 0.1632 0.2309 0.2080 0.0053  0.0158  0.0420  165 VAL   A CA  
3707 C  C   A VAL   A 165 ? 0.1472 0.2733 0.1821 -0.0244 0.0169  0.0916  165 VAL   A C   
3708 C  C   B VAL   A 165 ? 0.1633 0.2350 0.2045 0.0053  0.0142  0.0461  165 VAL   A C   
3709 O  O   A VAL   A 165 ? 0.1462 0.2729 0.1829 -0.0313 0.0205  0.0797  165 VAL   A O   
3710 O  O   B VAL   A 165 ? 0.1621 0.2331 0.1888 0.0052  0.0077  0.0518  165 VAL   A O   
3711 C  CB  A VAL   A 165 ? 0.1659 0.2622 0.1809 -0.0205 0.0163  0.0764  165 VAL   A CB  
3712 C  CB  B VAL   A 165 ? 0.1628 0.2270 0.2173 0.0115  0.0051  0.0335  165 VAL   A CB  
3713 C  CG1 A VAL   A 165 ? 0.1646 0.2630 0.1719 -0.0152 0.0236  0.0593  165 VAL   A CG1 
3714 C  CG1 B VAL   A 165 ? 0.1669 0.2274 0.2170 0.0106  -0.0011 0.0340  165 VAL   A CG1 
3715 C  CG2 A VAL   A 165 ? 0.1722 0.2607 0.1905 -0.0166 0.0063  0.0784  165 VAL   A CG2 
3716 C  CG2 B VAL   A 165 ? 0.1663 0.2274 0.2281 0.0112  0.0059  0.0293  165 VAL   A CG2 
3735 N  N   A SER   A 166 ? 0.1410 0.2827 0.1946 -0.0165 0.0078  0.0807  166 SER   A N   
3736 N  N   B SER   A 166 ? 0.1616 0.2382 0.2155 0.0030  0.0190  0.0457  166 SER   A N   
3737 C  CA  A SER   A 166 ? 0.1422 0.2959 0.2126 -0.0219 0.0153  0.0710  166 SER   A CA  
3738 C  CA  B SER   A 166 ? 0.1614 0.2405 0.2152 -0.0024 0.0218  0.0464  166 SER   A CA  
3739 C  C   A SER   A 166 ? 0.1535 0.3030 0.2151 -0.0171 0.0043  0.0622  166 SER   A C   
3740 C  C   B SER   A 166 ? 0.1619 0.2394 0.2095 -0.0122 0.0221  0.0536  166 SER   A C   
3741 O  O   A SER   A 166 ? 0.1692 0.3185 0.2383 -0.0245 0.0058  0.0445  166 SER   A O   
3742 O  O   B SER   A 166 ? 0.1611 0.2373 0.2083 -0.0233 0.0261  0.0637  166 SER   A O   
3743 C  CB  A SER   A 166 ? 0.1472 0.3029 0.2433 -0.0119 0.0075  0.0636  166 SER   A CB  
3744 C  CB  B SER   A 166 ? 0.1650 0.2447 0.2354 -0.0020 0.0163  0.0332  166 SER   A CB  
3745 O  OG  A SER   A 166 ? 0.1720 0.3133 0.2785 -0.0137 0.0165  0.0625  166 SER   A OG  
3746 O  OG  B SER   A 166 ? 0.1709 0.2480 0.2543 -0.0007 0.0163  0.0243  166 SER   A OG  
3757 N  N   A SER   A 167 ? 0.1536 0.2936 0.1822 0.0020  0.0002  0.0749  167 SER   A N   
3758 N  N   B SER   A 167 ? 0.1683 0.2387 0.2218 -0.0087 0.0279  0.0464  167 SER   A N   
3759 C  CA  A SER   A 167 ? 0.1794 0.2906 0.1965 0.0039  -0.0016 0.0580  167 SER   A CA  
3760 C  CA  B SER   A 167 ? 0.1753 0.2377 0.2209 -0.0036 0.0347  0.0435  167 SER   A CA  
3761 C  C   A SER   A 167 ? 0.1853 0.2868 0.2014 0.0107  0.0190  0.0652  167 SER   A C   
3762 C  C   B SER   A 167 ? 0.1710 0.2440 0.2184 0.0036  0.0355  0.0419  167 SER   A C   
3763 O  O   A SER   A 167 ? 0.2097 0.2928 0.2270 0.0181  -0.0037 0.0629  167 SER   A O   
3764 O  O   B SER   A 167 ? 0.1822 0.2495 0.2182 0.0073  0.0272  0.0447  167 SER   A O   
3765 C  CB  A SER   A 167 ? 0.1885 0.2880 0.2106 0.0026  0.0024  0.0506  167 SER   A CB  
3766 C  CB  B SER   A 167 ? 0.1865 0.2342 0.2341 -0.0037 0.0378  0.0325  167 SER   A CB  
3767 O  OG  A SER   A 167 ? 0.1842 0.2828 0.2197 0.0001  0.0192  0.0498  167 SER   A OG  
3768 O  OG  B SER   A 167 ? 0.1947 0.2342 0.2522 0.0013  0.0362  0.0197  167 SER   A OG  
3779 N  N   A PHE   A 168 ? 0.1746 0.2820 0.1964 0.0150  0.0322  0.0639  168 PHE   A N   
3780 N  N   B PHE   A 168 ? 0.1628 0.2445 0.2138 0.0067  0.0368  0.0399  168 PHE   A N   
3781 C  CA  A PHE   A 168 ? 0.1785 0.2833 0.2117 0.0140  0.0332  0.0616  168 PHE   A CA  
3782 C  CA  B PHE   A 168 ? 0.1619 0.2467 0.2054 0.0052  0.0402  0.0358  168 PHE   A CA  
3783 C  C   A PHE   A 168 ? 0.1884 0.2954 0.2519 0.0051  0.0582  0.0485  168 PHE   A C   
3784 C  C   B PHE   A 168 ? 0.1606 0.2530 0.2047 -0.0003 0.0460  0.0264  168 PHE   A C   
3785 O  O   A PHE   A 168 ? 0.1968 0.3012 0.3033 -0.0035 0.0703  0.0581  168 PHE   A O   
3786 O  O   B PHE   A 168 ? 0.1502 0.2516 0.1893 -0.0010 0.0534  0.0232  168 PHE   A O   
3787 C  CB  A PHE   A 168 ? 0.1758 0.2748 0.1912 0.0081  0.0160  0.0569  168 PHE   A CB  
3788 C  CB  B PHE   A 168 ? 0.1701 0.2445 0.2039 0.0031  0.0351  0.0381  168 PHE   A CB  
3789 C  CG  A PHE   A 168 ? 0.1714 0.2702 0.1716 0.0019  0.0012  0.0538  168 PHE   A CG  
3790 C  CG  B PHE   A 168 ? 0.1763 0.2401 0.2123 0.0003  0.0309  0.0450  168 PHE   A CG  
3791 C  CD1 A PHE   A 168 ? 0.1698 0.2755 0.1747 -0.0070 0.0017  0.0625  168 PHE   A CD1 
3792 C  CD1 B PHE   A 168 ? 0.1800 0.2399 0.2252 -0.0006 0.0314  0.0511  168 PHE   A CD1 
3793 C  CD2 A PHE   A 168 ? 0.1702 0.2665 0.1658 0.0024  0.0037  0.0419  168 PHE   A CD2 
3794 C  CD2 B PHE   A 168 ? 0.1793 0.2367 0.2093 0.0028  0.0223  0.0494  168 PHE   A CD2 
3795 C  CE1 A PHE   A 168 ? 0.1619 0.2746 0.1656 -0.0096 0.0032  0.0619  168 PHE   A CE1 
3796 C  CE1 B PHE   A 168 ? 0.1814 0.2405 0.2270 -0.0013 0.0264  0.0521  168 PHE   A CE1 
3797 C  CE2 A PHE   A 168 ? 0.1743 0.2617 0.1760 -0.0006 0.0122  0.0503  168 PHE   A CE2 
3798 C  CE2 B PHE   A 168 ? 0.1843 0.2370 0.2144 0.0047  0.0131  0.0510  168 PHE   A CE2 
3799 C  CZ  A PHE   A 168 ? 0.1662 0.2674 0.1713 -0.0050 0.0080  0.0548  168 PHE   A CZ  
3800 C  CZ  B PHE   A 168 ? 0.1863 0.2388 0.2219 0.0016  0.0179  0.0502  168 PHE   A CZ  
3819 N  N   A LEU   A 169 ? 0.2207 0.2991 0.2844 -0.0039 0.0522  0.0218  169 LEU   A N   
3820 N  N   B LEU   A 169 ? 0.1754 0.2636 0.2330 -0.0035 0.0360  0.0291  169 LEU   A N   
3821 C  CA  A LEU   A 169 ? 0.2530 0.3091 0.3352 0.0009  0.0358  0.0048  169 LEU   A CA  
3822 C  CA  B LEU   A 169 ? 0.1960 0.2758 0.2673 -0.0083 0.0272  0.0220  169 LEU   A CA  
3823 C  C   A LEU   A 169 ? 0.2422 0.3016 0.3510 -0.0009 0.0440  0.0260  169 LEU   A C   
3824 C  C   B LEU   A 169 ? 0.2127 0.2837 0.2976 -0.0031 0.0212  0.0177  169 LEU   A C   
3825 O  O   A LEU   A 169 ? 0.2500 0.3039 0.3630 0.0037  0.0370  0.0256  169 LEU   A O   
3826 O  O   B LEU   A 169 ? 0.2264 0.2873 0.3135 -0.0047 0.0200  0.0193  169 LEU   A O   
3827 C  CB  A LEU   A 169 ? 0.2839 0.3255 0.3477 0.0018  0.0250  -0.0234 169 LEU   A CB  
3828 C  CB  B LEU   A 169 ? 0.2007 0.2810 0.2694 -0.0150 0.0223  0.0199  169 LEU   A CB  
3829 C  CG  A LEU   A 169 ? 0.3129 0.3392 0.3601 0.0004  0.0153  -0.0517 169 LEU   A CG  
3830 C  CG  B LEU   A 169 ? 0.2026 0.2834 0.2733 -0.0192 0.0205  0.0220  169 LEU   A CG  
3831 C  CD1 A LEU   A 169 ? 0.3252 0.3417 0.3698 -0.0006 0.0083  -0.0573 169 LEU   A CD1 
3832 C  CD1 B LEU   A 169 ? 0.2021 0.2847 0.2864 -0.0236 0.0132  0.0239  169 LEU   A CD1 
3833 C  CD2 A LEU   A 169 ? 0.3215 0.3468 0.3579 -0.0024 0.0156  -0.0601 169 LEU   A CD2 
3834 C  CD2 B LEU   A 169 ? 0.2108 0.2853 0.2748 -0.0219 0.0268  0.0227  169 LEU   A CD2 
3835 O  OXT A LEU   A 169 ? 0.2244 0.3018 0.3473 -0.0052 0.0590  0.0333  169 LEU   A OXT 
3836 O  OXT B LEU   A 169 ? 0.2128 0.2878 0.3064 -0.0027 0.0185  0.0132  169 LEU   A OXT 
3859 N  N   A SER   B 1   ? 0.3856 0.3548 0.3554 -0.1112 -0.0662 0.0474  1   SER   B N   
3860 N  N   B SER   B 1   ? 0.3419 0.3314 0.3500 -0.0662 -0.0456 0.0206  1   SER   B N   
3861 C  CA  A SER   B 1   ? 0.3765 0.3574 0.3667 -0.1166 -0.0716 0.0444  1   SER   B CA  
3862 C  CA  B SER   B 1   ? 0.3365 0.3310 0.3479 -0.0678 -0.0461 0.0195  1   SER   B CA  
3863 C  C   A SER   B 1   ? 0.3473 0.3566 0.3487 -0.1188 -0.0793 0.0591  1   SER   B C   
3864 C  C   B SER   B 1   ? 0.3211 0.3297 0.3324 -0.0668 -0.0501 0.0296  1   SER   B C   
3865 O  O   A SER   B 1   ? 0.3562 0.3577 0.3244 -0.1120 -0.0708 0.0604  1   SER   B O   
3866 O  O   B SER   B 1   ? 0.3225 0.3292 0.3187 -0.0662 -0.0520 0.0285  1   SER   B O   
3867 C  CB  A SER   B 1   ? 0.3909 0.3575 0.3861 -0.1169 -0.0626 0.0317  1   SER   B CB  
3868 C  CB  B SER   B 1   ? 0.3434 0.3301 0.3559 -0.0688 -0.0403 0.0090  1   SER   B CB  
3869 O  OG  A SER   B 1   ? 0.4056 0.3675 0.4310 -0.1144 -0.0546 0.0269  1   SER   B OG  
3870 O  OG  B SER   B 1   ? 0.3500 0.3330 0.3749 -0.0702 -0.0366 0.0036  1   SER   B OG  
3885 N  N   A MET   B 2   ? 0.3172 0.3522 0.3400 -0.1202 -0.0852 0.0939  2   MET   B N   
3886 N  N   B MET   B 2   ? 0.3073 0.3276 0.3231 -0.0635 -0.0491 0.0490  2   MET   B N   
3887 C  CA  A MET   B 2   ? 0.2989 0.3532 0.3565 -0.0974 -0.0883 0.1125  2   MET   B CA  
3888 C  CA  B MET   B 2   ? 0.2953 0.3251 0.3201 -0.0526 -0.0463 0.0627  2   MET   B CA  
3889 C  C   A MET   B 2   ? 0.2613 0.3308 0.3239 -0.0798 -0.0961 0.1395  2   MET   B C   
3890 C  C   B MET   B 2   ? 0.2759 0.3100 0.2957 -0.0471 -0.0397 0.0668  2   MET   B C   
3891 O  O   A MET   B 2   ? 0.2562 0.3437 0.3186 -0.0666 -0.1091 0.1466  2   MET   B O   
3892 O  O   B MET   B 2   ? 0.2775 0.3160 0.2978 -0.0441 -0.0326 0.0659  2   MET   B O   
3893 C  CB  A MET   B 2   ? 0.3300 0.3864 0.4433 -0.0732 -0.0685 0.0848  2   MET   B CB  
3894 C  CB  B MET   B 2   ? 0.3063 0.3403 0.3526 -0.0416 -0.0469 0.0674  2   MET   B CB  
3895 C  CG  A MET   B 2   ? 0.3578 0.4137 0.5196 -0.0498 -0.0468 0.0674  2   MET   B CG  
3896 C  CG  B MET   B 2   ? 0.3153 0.3531 0.3757 -0.0314 -0.0462 0.0789  2   MET   B CG  
3897 S  SD  A MET   B 2   ? 0.3852 0.4410 0.5952 -0.0304 -0.0330 0.0538  2   MET   B SD  
3898 S  SD  B MET   B 2   ? 0.3251 0.3664 0.3960 -0.0217 -0.0495 0.0902  2   MET   B SD  
3899 C  CE  A MET   B 2   ? 0.3870 0.4469 0.5976 -0.0287 -0.0247 0.0531  2   MET   B CE  
3900 C  CE  B MET   B 2   ? 0.3245 0.3681 0.4037 -0.0218 -0.0454 0.0816  2   MET   B CE  
3919 N  N   A VAL   B 3   ? 0.2304 0.2874 0.2976 -0.0829 -0.0849 0.1573  3   VAL   B N   
3920 N  N   B VAL   B 3   ? 0.2543 0.2854 0.2683 -0.0473 -0.0396 0.0725  3   VAL   B N   
3921 C  CA  A VAL   B 3   ? 0.2220 0.2543 0.2931 -0.0707 -0.0768 0.1344  3   VAL   B CA  
3922 C  CA  B VAL   B 3   ? 0.2379 0.2636 0.2512 -0.0440 -0.0378 0.0678  3   VAL   B CA  
3923 C  C   A VAL   B 3   ? 0.2062 0.2391 0.2571 -0.0619 -0.0660 0.1125  3   VAL   B C   
3924 C  C   B VAL   B 3   ? 0.2176 0.2454 0.2273 -0.0462 -0.0413 0.0726  3   VAL   B C   
3925 O  O   A VAL   B 3   ? 0.2040 0.2392 0.2759 -0.0611 -0.0726 0.1119  3   VAL   B O   
3926 O  O   B VAL   B 3   ? 0.2172 0.2498 0.2201 -0.0386 -0.0424 0.0653  3   VAL   B O   
3927 C  CB  A VAL   B 3   ? 0.2374 0.2467 0.3434 -0.0718 -0.0692 0.1189  3   VAL   B CB  
3928 C  CB  B VAL   B 3   ? 0.2437 0.2599 0.2650 -0.0418 -0.0307 0.0593  3   VAL   B CB  
3929 C  CG1 A VAL   B 3   ? 0.2439 0.2423 0.3608 -0.0716 -0.0675 0.1121  3   VAL   B CG1 
3930 C  CG1 B VAL   B 3   ? 0.2461 0.2578 0.2714 -0.0415 -0.0275 0.0546  3   VAL   B CG1 
3931 C  CG2 A VAL   B 3   ? 0.2411 0.2529 0.3652 -0.0685 -0.0592 0.1241  3   VAL   B CG2 
3932 C  CG2 B VAL   B 3   ? 0.2452 0.2604 0.2715 -0.0400 -0.0283 0.0603  3   VAL   B CG2 
3951 N  N   . ASN   B 4   ? 0.2001 0.2209 0.2231 -0.0586 -0.0484 0.0838  4   ASN   B N   
3952 C  CA  . ASN   B 4   ? 0.2003 0.2176 0.1898 -0.0593 -0.0485 0.0494  4   ASN   B CA  
3953 C  C   . ASN   B 4   ? 0.2103 0.2344 0.1858 -0.0598 -0.0334 0.0332  4   ASN   B C   
3954 O  O   . ASN   B 4   ? 0.2105 0.2418 0.2088 -0.0571 -0.0253 0.0114  4   ASN   B O   
3955 C  CB  . ASN   B 4   ? 0.1971 0.2081 0.1779 -0.0503 -0.0608 0.0414  4   ASN   B CB  
3956 C  CG  . ASN   B 4   ? 0.1940 0.1936 0.1677 -0.0504 -0.0535 0.0338  4   ASN   B CG  
3957 O  OD1 . ASN   B 4   ? 0.1942 0.1819 0.1721 -0.0464 -0.0459 0.0297  4   ASN   B OD1 
3958 N  ND2 . ASN   B 4   ? 0.2129 0.1985 0.1862 -0.0294 -0.0344 0.0242  4   ASN   B ND2 
3966 N  N   . SER   B 5   ? 0.2225 0.2509 0.1847 -0.0613 -0.0166 0.0329  5   SER   B N   
3967 C  CA  . SER   B 5   ? 0.2473 0.2829 0.2278 -0.0505 0.0076  0.0339  5   SER   B CA  
3968 C  C   . SER   B 5   ? 0.2645 0.2871 0.2595 -0.0658 0.0285  0.0372  5   SER   B C   
3969 O  O   . SER   B 5   ? 0.2782 0.2853 0.3368 -0.0623 0.0575  0.0324  5   SER   B O   
3970 C  CB  . SER   B 5   ? 0.2599 0.3082 0.2634 -0.0357 0.0157  0.0403  5   SER   B CB  
3971 O  OG  . SER   B 5   ? 0.2819 0.3348 0.3172 -0.0246 0.0187  0.0438  5   SER   B OG  
3977 N  N   . PHE   B 6   ? 0.2826 0.3054 0.2312 -0.0696 0.0388  0.0424  6   PHE   B N   
3978 C  CA  . PHE   B 6   ? 0.2884 0.3104 0.1961 -0.0879 0.0372  0.0224  6   PHE   B CA  
3979 C  C   . PHE   B 6   ? 0.3400 0.3443 0.2359 -0.0936 0.0589  -0.0108 6   PHE   B C   
3980 O  O   . PHE   B 6   ? 0.3561 0.3758 0.2724 -0.0862 0.0387  -0.0322 6   PHE   B O   
3981 C  CB  . PHE   B 6   ? 0.2551 0.2894 0.1711 -0.0770 0.0137  0.0212  6   PHE   B CB  
3982 C  CG  . PHE   B 6   ? 0.2199 0.2590 0.1687 -0.0709 -0.0022 0.0175  6   PHE   B CG  
3983 C  CD1 . PHE   B 6   ? 0.2179 0.2304 0.1514 -0.0654 -0.0179 0.0119  6   PHE   B CD1 
3984 C  CD2 . PHE   B 6   ? 0.1930 0.2563 0.1787 -0.0584 -0.0016 0.0406  6   PHE   B CD2 
3985 C  CE1 . PHE   B 6   ? 0.2142 0.2065 0.1589 -0.0539 -0.0211 0.0055  6   PHE   B CE1 
3986 C  CE2 . PHE   B 6   ? 0.1998 0.2418 0.1986 -0.0478 0.0040  0.0360  6   PHE   B CE2 
3987 C  CZ  . PHE   B 6   ? 0.2079 0.2162 0.1844 -0.0476 -0.0022 0.0108  6   PHE   B CZ  
3997 N  N   . SER   B 7   ? 0.3741 0.3307 0.2444 -0.1154 0.0885  -0.0396 7   SER   B N   
3998 C  CA  . SER   B 7   ? 0.4054 0.3482 0.2947 -0.1138 0.1115  -0.0476 7   SER   B CA  
3999 C  C   . SER   B 7   ? 0.4033 0.3279 0.2804 -0.1173 0.1281  -0.0577 7   SER   B C   
4000 O  O   . SER   B 7   ? 0.4119 0.3301 0.3095 -0.1160 0.1266  -0.0575 7   SER   B O   
4001 C  CB  . SER   B 7   ? 0.4277 0.3723 0.3639 -0.1093 0.1223  -0.0456 7   SER   B CB  
4002 O  OG  . SER   B 7   ? 0.4417 0.3779 0.4216 -0.1087 0.1252  -0.0373 7   SER   B OG  
4008 N  N   . GLY   B 8   ? 0.4006 0.3147 0.2879 -0.1053 0.1318  -0.0648 8   GLY   B N   
4009 C  CA  . GLY   B 8   ? 0.3870 0.2979 0.2962 -0.0964 0.1313  -0.0685 8   GLY   B CA  
4010 C  C   . GLY   B 8   ? 0.3641 0.2672 0.2886 -0.0955 0.1337  -0.0626 8   GLY   B C   
4011 O  O   . GLY   B 8   ? 0.3725 0.2742 0.3282 -0.0885 0.1380  -0.0643 8   GLY   B O   
4015 N  N   . TYR   B 9   ? 0.3453 0.2429 0.2611 -0.0843 0.1101  -0.0724 9   TYR   B N   
4016 C  CA  . TYR   B 9   ? 0.3239 0.2157 0.2403 -0.0689 0.0821  -0.0543 9   TYR   B CA  
4017 C  C   . TYR   B 9   ? 0.3183 0.2113 0.2274 -0.0589 0.0495  -0.0421 9   TYR   B C   
4018 O  O   . TYR   B 9   ? 0.3330 0.2310 0.2691 -0.0593 0.0457  -0.0333 9   TYR   B O   
4019 C  CB  . TYR   B 9   ? 0.3161 0.1960 0.2517 -0.0607 0.0745  -0.0467 9   TYR   B CB  
4020 C  CG  . TYR   B 9   ? 0.3038 0.1805 0.2513 -0.0669 0.0646  -0.0497 9   TYR   B CG  
4021 C  CD1 . TYR   B 9   ? 0.3035 0.1849 0.2591 -0.0795 0.0645  -0.0463 9   TYR   B CD1 
4022 C  CD2 . TYR   B 9   ? 0.2866 0.1730 0.2409 -0.0644 0.0622  -0.0466 9   TYR   B CD2 
4023 C  CE1 . TYR   B 9   ? 0.2963 0.1928 0.2561 -0.0823 0.0718  -0.0583 9   TYR   B CE1 
4024 C  CE2 . TYR   B 9   ? 0.2872 0.1703 0.2533 -0.0611 0.0642  -0.0523 9   TYR   B CE2 
4025 C  CZ  . TYR   B 9   ? 0.2896 0.1909 0.2637 -0.0740 0.0646  -0.0647 9   TYR   B CZ  
4026 O  OH  . TYR   B 9   ? 0.2852 0.2024 0.2784 -0.0839 0.0670  -0.0821 9   TYR   B OH  
4036 N  N   . LEU   B 10  ? 0.2954 0.1913 0.1999 -0.0558 0.0239  -0.0413 10  LEU   B N   
4037 C  CA  . LEU   B 10  ? 0.2926 0.1930 0.1965 -0.0671 -0.0119 -0.0374 10  LEU   B CA  
4038 C  C   . LEU   B 10  ? 0.2734 0.1948 0.1995 -0.0676 -0.0299 -0.0344 10  LEU   B C   
4039 O  O   . LEU   B 10  ? 0.2582 0.1968 0.2088 -0.0513 -0.0181 -0.0279 10  LEU   B O   
4040 C  CB  . LEU   B 10  ? 0.3064 0.1921 0.2235 -0.0753 -0.0352 -0.0173 10  LEU   B CB  
4041 C  CG  . LEU   B 10  ? 0.3270 0.2026 0.2602 -0.0658 -0.0619 -0.0107 10  LEU   B CG  
4042 C  CD1 . LEU   B 10  ? 0.3421 0.2165 0.2902 -0.0614 -0.0574 -0.0099 10  LEU   B CD1 
4043 C  CD2 . LEU   B 10  ? 0.3369 0.2069 0.2937 -0.0619 -0.0591 0.0120  10  LEU   B CD2 
4055 N  N   . LYS   B 11  ? 0.2902 0.2241 0.2014 -0.0567 -0.0300 -0.0228 11  LYS   B N   
4056 C  CA  . LYS   B 11  ? 0.3013 0.2474 0.2405 -0.0474 -0.0443 -0.0320 11  LYS   B CA  
4057 C  C   . LYS   B 11  ? 0.2803 0.2285 0.2481 -0.0667 -0.0451 -0.0439 11  LYS   B C   
4058 O  O   . LYS   B 11  ? 0.2992 0.2487 0.2841 -0.0807 -0.0408 -0.0763 11  LYS   B O   
4059 C  CB  . LYS   B 11  ? 0.3346 0.2973 0.3086 -0.0172 -0.0476 -0.0274 11  LYS   B CB  
4060 C  CG  . LYS   B 11  ? 0.3647 0.3299 0.3742 0.0000  -0.0530 -0.0300 11  LYS   B CG  
4061 C  CD  . LYS   B 11  ? 0.3889 0.3534 0.4374 0.0094  -0.0545 -0.0333 11  LYS   B CD  
4062 C  CE  . LYS   B 11  ? 0.4054 0.3697 0.4846 0.0112  -0.0556 -0.0350 11  LYS   B CE  
4063 N  NZ  . LYS   B 11  ? 0.4150 0.3793 0.5108 0.0117  -0.0579 -0.0335 11  LYS   B NZ  
4077 N  N   . LEU   B 12  ? 0.2436 0.2041 0.2446 -0.0568 -0.0403 -0.0377 12  LEU   B N   
4078 C  CA  . LEU   B 12  ? 0.2309 0.1834 0.2597 -0.0510 -0.0348 -0.0352 12  LEU   B CA  
4079 C  C   . LEU   B 12  ? 0.2221 0.1832 0.2664 -0.0531 -0.0486 -0.0283 12  LEU   B C   
4080 O  O   . LEU   B 12  ? 0.2224 0.1854 0.2846 -0.0642 -0.0600 -0.0194 12  LEU   B O   
4081 C  CB  . LEU   B 12  ? 0.2305 0.1663 0.2614 -0.0334 -0.0172 -0.0359 12  LEU   B CB  
4082 C  CG  . LEU   B 12  ? 0.2281 0.1608 0.2583 -0.0369 -0.0051 -0.0257 12  LEU   B CG  
4083 C  CD1 . LEU   B 12  ? 0.2413 0.1638 0.2550 -0.0252 -0.0022 -0.0076 12  LEU   B CD1 
4084 C  CD2 . LEU   B 12  ? 0.2322 0.1669 0.2726 -0.0388 0.0008  -0.0349 12  LEU   B CD2 
4096 N  N   . THR   B 13  ? 0.2130 0.1835 0.2748 -0.0540 -0.0466 -0.0412 13  THR   B N   
4097 C  CA  . THR   B 13  ? 0.2113 0.1926 0.2652 -0.0591 -0.0555 -0.0263 13  THR   B CA  
4098 C  C   . THR   B 13  ? 0.2484 0.2115 0.2788 -0.0680 -0.0734 -0.0183 13  THR   B C   
4099 O  O   . THR   B 13  ? 0.2660 0.2123 0.2872 -0.0632 -0.0369 -0.0177 13  THR   B O   
4100 C  CB  . THR   B 13  ? 0.1959 0.1938 0.2689 -0.0535 -0.0493 -0.0159 13  THR   B CB  
4101 O  OG1 . THR   B 13  ? 0.1848 0.1925 0.2761 -0.0432 -0.0422 -0.0180 13  THR   B OG1 
4102 C  CG2 . THR   B 13  ? 0.2088 0.2012 0.2686 -0.0454 -0.0420 -0.0045 13  THR   B CG2 
4110 N  N   A ASP   B 14  ? 0.2645 0.2308 0.2904 -0.0733 -0.1054 -0.0078 14  ASP   B N   
4111 N  N   B ASP   B 14  ? 0.2581 0.2247 0.2911 -0.0653 -0.0785 -0.0115 14  ASP   B N   
4112 C  CA  A ASP   B 14  ? 0.2763 0.2487 0.3134 -0.0730 -0.1119 0.0122  14  ASP   B CA  
4113 C  CA  B ASP   B 14  ? 0.2655 0.2361 0.3044 -0.0619 -0.0761 -0.0035 14  ASP   B CA  
4114 C  C   A ASP   B 14  ? 0.2627 0.2286 0.2727 -0.0758 -0.0915 0.0118  14  ASP   B C   
4115 C  C   B ASP   B 14  ? 0.2501 0.2209 0.2703 -0.0622 -0.0769 -0.0030 14  ASP   B C   
4116 O  O   A ASP   B 14  ? 0.2904 0.2409 0.2790 -0.0772 -0.0866 0.0257  14  ASP   B O   
4117 O  O   B ASP   B 14  ? 0.2598 0.2242 0.2700 -0.0593 -0.0783 -0.0078 14  ASP   B O   
4118 C  CB  A ASP   B 14  ? 0.2992 0.2843 0.3924 -0.0698 -0.1289 0.0171  14  ASP   B CB  
4119 C  CB  B ASP   B 14  ? 0.2860 0.2596 0.3544 -0.0576 -0.0710 0.0001  14  ASP   B CB  
4120 C  CG  A ASP   B 14  ? 0.3290 0.3172 0.4709 -0.0641 -0.1239 0.0037  14  ASP   B CG  
4121 C  CG  B ASP   B 14  ? 0.3067 0.2795 0.3999 -0.0519 -0.0630 -0.0037 14  ASP   B CG  
4122 O  OD1 A ASP   B 14  ? 0.3484 0.3293 0.4914 -0.0662 -0.1202 -0.0131 14  ASP   B OD1 
4123 O  OD1 B ASP   B 14  ? 0.3160 0.2897 0.4134 -0.0504 -0.0572 -0.0079 14  ASP   B OD1 
4124 O  OD2 A ASP   B 14  ? 0.3330 0.3316 0.5072 -0.0625 -0.1168 0.0082  14  ASP   B OD2 
4125 O  OD2 B ASP   B 14  ? 0.3123 0.2842 0.4155 -0.0534 -0.0624 -0.0031 14  ASP   B OD2 
4134 N  N   . ASN   B 15  ? 0.2274 0.2027 0.2434 -0.0574 -0.0755 0.0059  15  ASN   B N   
4135 C  CA  . ASN   B 15  ? 0.1857 0.1716 0.2301 -0.0366 -0.0499 0.0011  15  ASN   B CA  
4136 C  C   . ASN   B 15  ? 0.1655 0.1569 0.2114 -0.0225 -0.0398 -0.0045 15  ASN   B C   
4137 O  O   . ASN   B 15  ? 0.1696 0.1555 0.2343 -0.0266 -0.0465 -0.0122 15  ASN   B O   
4138 C  CB  . ASN   B 15  ? 0.1783 0.1657 0.2463 -0.0185 -0.0501 0.0031  15  ASN   B CB  
4139 C  CG  . ASN   B 15  ? 0.1645 0.1598 0.2470 -0.0262 -0.0288 0.0035  15  ASN   B CG  
4140 O  OD1 . ASN   B 15  ? 0.1737 0.1896 0.2752 -0.0444 -0.0312 0.0136  15  ASN   B OD1 
4141 N  ND2 . ASN   B 15  ? 0.1702 0.1452 0.2278 -0.0216 -0.0038 -0.0092 15  ASN   B ND2 
4149 N  N   . VAL   B 16  ? 0.1696 0.1552 0.2165 -0.0305 -0.0460 -0.0053 16  VAL   B N   
4150 C  CA  . VAL   B 16  ? 0.1773 0.1544 0.1946 -0.0276 -0.0371 -0.0217 16  VAL   B CA  
4151 C  C   . VAL   B 16  ? 0.1742 0.1648 0.1967 -0.0403 -0.0350 -0.0136 16  VAL   B C   
4152 O  O   . VAL   B 16  ? 0.1733 0.1786 0.2321 -0.0315 -0.0334 -0.0271 16  VAL   B O   
4153 C  CB  . VAL   B 16  ? 0.1800 0.1553 0.2107 -0.0162 -0.0248 -0.0140 16  VAL   B CB  
4154 C  CG1 . VAL   B 16  ? 0.1925 0.1442 0.2107 -0.0023 -0.0170 -0.0057 16  VAL   B CG1 
4155 C  CG2 . VAL   B 16  ? 0.1781 0.1587 0.2334 -0.0104 -0.0166 -0.0138 16  VAL   B CG2 
4165 N  N   . TYR   B 17  ? 0.1824 0.1707 0.2011 -0.0358 -0.0299 -0.0241 17  TYR   B N   
4166 C  CA  . TYR   B 17  ? 0.1910 0.1792 0.1902 -0.0362 -0.0279 -0.0044 17  TYR   B CA  
4167 C  C   . TYR   B 17  ? 0.1830 0.1580 0.1949 -0.0375 -0.0165 -0.0131 17  TYR   B C   
4168 O  O   . TYR   B 17  ? 0.1817 0.1602 0.2060 -0.0346 -0.0287 -0.0318 17  TYR   B O   
4169 C  CB  . TYR   B 17  ? 0.2191 0.2237 0.2161 -0.0218 -0.0251 0.0306  17  TYR   B CB  
4170 C  CG  . TYR   B 17  ? 0.2422 0.2768 0.2559 -0.0157 -0.0441 0.0396  17  TYR   B CG  
4171 C  CD1 . TYR   B 17  ? 0.2560 0.2932 0.2804 -0.0133 -0.0575 0.0503  17  TYR   B CD1 
4172 C  CD2 . TYR   B 17  ? 0.2652 0.3083 0.2846 -0.0074 -0.0519 0.0382  17  TYR   B CD2 
4173 C  CE1 . TYR   B 17  ? 0.2741 0.3186 0.2979 -0.0040 -0.0718 0.0442  17  TYR   B CE1 
4174 C  CE2 . TYR   B 17  ? 0.2802 0.3288 0.3081 0.0034  -0.0707 0.0434  17  TYR   B CE2 
4175 C  CZ  . TYR   B 17  ? 0.2890 0.3370 0.3113 0.0066  -0.0820 0.0471  17  TYR   B CZ  
4176 O  OH  . TYR   B 17  ? 0.3073 0.3567 0.3312 0.0148  -0.0883 0.0474  17  TYR   B OH  
4186 N  N   . ILE   B 18  ? 0.1880 0.1593 0.1885 -0.0322 -0.0093 -0.0181 18  ILE   B N   
4187 C  CA  . ILE   B 18  ? 0.1929 0.1545 0.1860 -0.0371 -0.0107 -0.0201 18  ILE   B CA  
4188 C  C   . ILE   B 18  ? 0.2094 0.1593 0.1742 -0.0479 -0.0102 -0.0249 18  ILE   B C   
4189 O  O   . ILE   B 18  ? 0.2317 0.1709 0.1930 -0.0412 -0.0072 -0.0305 18  ILE   B O   
4190 C  CB  . ILE   B 18  ? 0.1957 0.1614 0.2020 -0.0386 -0.0121 -0.0174 18  ILE   B CB  
4191 C  CG1 . ILE   B 18  ? 0.1998 0.1683 0.1994 -0.0375 -0.0087 -0.0090 18  ILE   B CG1 
4192 C  CG2 . ILE   B 18  ? 0.2008 0.1611 0.2034 -0.0427 -0.0213 -0.0205 18  ILE   B CG2 
4193 C  CD1 . ILE   B 18  ? 0.2072 0.1936 0.2158 -0.0345 -0.0195 0.0169  18  ILE   B CD1 
4205 N  N   . LYS   B 19  ? 0.2076 0.1617 0.1912 -0.0306 0.0295  -0.0298 19  LYS   B N   
4206 C  CA  . LYS   B 19  ? 0.2129 0.1648 0.2061 -0.0287 0.0292  -0.0346 19  LYS   B CA  
4207 C  C   . LYS   B 19  ? 0.1955 0.1575 0.2264 -0.0255 0.0318  -0.0473 19  LYS   B C   
4208 O  O   . LYS   B 19  ? 0.1896 0.1660 0.2123 -0.0187 0.0215  -0.0427 19  LYS   B O   
4209 C  CB  . LYS   B 19  ? 0.2386 0.1868 0.2203 -0.0366 0.0416  -0.0241 19  LYS   B CB  
4210 C  CG  . LYS   B 19  ? 0.2643 0.2043 0.2513 -0.0418 0.0455  -0.0258 19  LYS   B CG  
4211 C  CD  . LYS   B 19  ? 0.2881 0.2318 0.2626 -0.0504 0.0460  -0.0264 19  LYS   B CD  
4212 C  CE  . LYS   B 19  ? 0.3130 0.2599 0.2811 -0.0531 0.0437  -0.0353 19  LYS   B CE  
4213 N  NZ  . LYS   B 19  ? 0.3308 0.2777 0.2881 -0.0603 0.0478  -0.0364 19  LYS   B NZ  
4227 N  N   . ASN   B 20  ? 0.1950 0.1746 0.2595 -0.0168 0.0328  -0.0614 20  ASN   B N   
4228 C  CA  . ASN   B 20  ? 0.1990 0.1861 0.2848 -0.0105 0.0406  -0.0766 20  ASN   B CA  
4229 C  C   . ASN   B 20  ? 0.1964 0.2027 0.2839 -0.0204 0.0500  -0.0863 20  ASN   B C   
4230 O  O   . ASN   B 20  ? 0.2180 0.2372 0.2996 -0.0367 0.0477  -0.0882 20  ASN   B O   
4231 C  CB  . ASN   B 20  ? 0.2245 0.1874 0.3133 0.0091  0.0283  -0.0748 20  ASN   B CB  
4232 C  CG  . ASN   B 20  ? 0.2495 0.1935 0.3477 0.0390  0.0247  -0.0792 20  ASN   B CG  
4233 O  OD1 . ASN   B 20  ? 0.2811 0.2246 0.3854 0.0528  0.0267  -0.0817 20  ASN   B OD1 
4234 N  ND2 . ASN   B 20  ? 0.2362 0.1940 0.3398 0.0404  0.0074  -0.0712 20  ASN   B ND2 
4241 N  N   . ALA   B 21  ? 0.1969 0.1885 0.2870 -0.0270 0.0534  -0.0670 21  ALA   B N   
4242 C  CA  . ALA   B 21  ? 0.2082 0.1947 0.3035 -0.0341 0.0379  -0.0480 21  ALA   B CA  
4243 C  C   . ALA   B 21  ? 0.2053 0.1728 0.2876 -0.0235 0.0414  -0.0364 21  ALA   B C   
4244 O  O   . ALA   B 21  ? 0.2046 0.1610 0.2886 -0.0303 0.0402  -0.0279 21  ALA   B O   
4245 C  CB  . ALA   B 21  ? 0.2223 0.2222 0.3163 -0.0427 0.0362  -0.0311 21  ALA   B CB  
4251 N  N   . ASP   B 22  ? 0.1946 0.1632 0.2745 -0.0226 0.0318  -0.0313 22  ASP   B N   
4252 C  CA  . ASP   B 22  ? 0.1890 0.1540 0.2608 -0.0096 0.0287  -0.0264 22  ASP   B CA  
4253 C  C   . ASP   B 22  ? 0.1844 0.1518 0.2306 -0.0149 0.0151  -0.0121 22  ASP   B C   
4254 O  O   . ASP   B 22  ? 0.1817 0.1528 0.2329 -0.0105 0.0100  -0.0077 22  ASP   B O   
4255 C  CB  . ASP   B 22  ? 0.1966 0.1677 0.3035 -0.0036 0.0214  -0.0086 22  ASP   B CB  
4256 C  CG  . ASP   B 22  ? 0.2027 0.1866 0.3498 0.0006  -0.0030 -0.0048 22  ASP   B CG  
4257 O  OD1 . ASP   B 22  ? 0.2119 0.1795 0.3596 0.0023  -0.0183 -0.0018 22  ASP   B OD1 
4258 O  OD2 . ASP   B 22  ? 0.2126 0.2092 0.3939 0.0064  -0.0174 -0.0164 22  ASP   B OD2 
4263 N  N   . ILE   B 23  ? 0.1796 0.1517 0.2016 -0.0059 0.0073  0.0143  23  ILE   B N   
4264 C  CA  . ILE   B 23  ? 0.1680 0.1522 0.1755 -0.0087 0.0009  0.0057  23  ILE   B CA  
4265 C  C   . ILE   B 23  ? 0.1626 0.1518 0.1762 -0.0044 -0.0096 0.0038  23  ILE   B C   
4266 O  O   . ILE   B 23  ? 0.1607 0.1482 0.1687 -0.0090 -0.0058 0.0063  23  ILE   B O   
4267 C  CB  . ILE   B 23  ? 0.1672 0.1635 0.1970 -0.0136 0.0027  0.0107  23  ILE   B CB  
4268 C  CG1 . ILE   B 23  ? 0.1672 0.1691 0.2081 -0.0079 0.0042  0.0303  23  ILE   B CG1 
4269 C  CG2 . ILE   B 23  ? 0.1711 0.1819 0.2042 -0.0146 0.0062  0.0106  23  ILE   B CG2 
4270 C  CD1 . ILE   B 23  ? 0.1760 0.1767 0.2224 -0.0070 0.0046  0.0207  23  ILE   B CD1 
4282 N  N   . VAL   B 24  ? 0.1680 0.1546 0.1886 -0.0076 -0.0088 0.0037  24  VAL   B N   
4283 C  CA  . VAL   B 24  ? 0.1637 0.1557 0.2064 -0.0024 -0.0213 -0.0032 24  VAL   B CA  
4284 C  C   . VAL   B 24  ? 0.1582 0.1597 0.2168 -0.0115 -0.0092 0.0069  24  VAL   B C   
4285 O  O   . VAL   B 24  ? 0.1581 0.1695 0.2261 -0.0218 -0.0078 0.0146  24  VAL   B O   
4286 C  CB  . VAL   B 24  ? 0.1780 0.1718 0.2129 -0.0006 -0.0228 -0.0058 24  VAL   B CB  
4287 C  CG1 . VAL   B 24  ? 0.1784 0.1773 0.2480 -0.0132 -0.0268 0.0036  24  VAL   B CG1 
4288 C  CG2 . VAL   B 24  ? 0.1874 0.1968 0.2113 0.0054  -0.0241 -0.0160 24  VAL   B CG2 
4298 N  N   . GLU   B 25  ? 0.1801 0.1679 0.2211 -0.0118 0.0031  0.0056  25  GLU   B N   
4299 C  CA  . GLU   B 25  ? 0.1965 0.1941 0.2361 -0.0045 0.0129  -0.0071 25  GLU   B CA  
4300 C  C   . GLU   B 25  ? 0.1916 0.1903 0.2049 -0.0167 0.0138  -0.0064 25  GLU   B C   
4301 O  O   . GLU   B 25  ? 0.1966 0.2037 0.2181 -0.0141 0.0253  -0.0001 25  GLU   B O   
4302 C  CB  . GLU   B 25  ? 0.2299 0.2442 0.3009 0.0219  0.0205  -0.0093 25  GLU   B CB  
4303 C  CG  . GLU   B 25  ? 0.2735 0.3093 0.4062 0.0323  0.0132  -0.0122 25  GLU   B CG  
4304 C  CD  . GLU   B 25  ? 0.3195 0.3681 0.4960 0.0292  0.0066  -0.0141 25  GLU   B CD  
4305 O  OE1 . GLU   B 25  ? 0.3384 0.3892 0.5267 0.0333  0.0110  -0.0112 25  GLU   B OE1 
4306 O  OE2 . GLU   B 25  ? 0.3356 0.3869 0.5253 0.0284  -0.0011 -0.0214 25  GLU   B OE2 
4313 N  N   . GLU   B 26  ? 0.1893 0.1822 0.1882 -0.0313 0.0057  -0.0055 26  GLU   B N   
4314 C  CA  . GLU   B 26  ? 0.1829 0.1887 0.1945 -0.0416 -0.0114 0.0007  26  GLU   B CA  
4315 C  C   . GLU   B 26  ? 0.1666 0.1836 0.1729 -0.0331 -0.0038 0.0190  26  GLU   B C   
4316 O  O   . GLU   B 26  ? 0.1940 0.2116 0.1788 -0.0239 -0.0005 0.0261  26  GLU   B O   
4317 C  CB  . GLU   B 26  ? 0.2192 0.2112 0.2152 -0.0478 -0.0038 0.0153  26  GLU   B CB  
4318 C  CG  . GLU   B 26  ? 0.2627 0.2496 0.2739 -0.0484 0.0094  -0.0065 26  GLU   B CG  
4319 C  CD  . GLU   B 26  ? 0.2893 0.2711 0.2853 -0.0713 0.0278  -0.0475 26  GLU   B CD  
4320 O  OE1 . GLU   B 26  ? 0.3085 0.2572 0.2884 -0.0857 0.0752  -0.0404 26  GLU   B OE1 
4321 O  OE2 . GLU   B 26  ? 0.2912 0.3111 0.3244 -0.0615 0.0240  -0.0379 26  GLU   B OE2 
4328 N  N   . ALA   B 27  ? 0.1490 0.1770 0.1727 -0.0231 -0.0012 0.0236  27  ALA   B N   
4329 C  CA  . ALA   B 27  ? 0.1588 0.1685 0.1899 -0.0180 0.0013  0.0330  27  ALA   B CA  
4330 C  C   . ALA   B 27  ? 0.1634 0.1744 0.2123 -0.0120 0.0139  0.0411  27  ALA   B C   
4331 O  O   . ALA   B 27  ? 0.1765 0.1815 0.2230 -0.0025 0.0110  0.0484  27  ALA   B O   
4332 C  CB  . ALA   B 27  ? 0.1739 0.1514 0.1956 -0.0183 0.0054  0.0317  27  ALA   B CB  
4338 N  N   . LYS   B 28  ? 0.1610 0.1862 0.2604 -0.0188 0.0214  0.0576  28  LYS   B N   
4339 C  CA  . LYS   B 28  ? 0.1774 0.2257 0.2912 -0.0054 0.0544  0.0810  28  LYS   B CA  
4340 C  C   . LYS   B 28  ? 0.1965 0.2455 0.2776 0.0003  0.0661  0.0747  28  LYS   B C   
4341 O  O   . LYS   B 28  ? 0.2194 0.2534 0.2948 -0.0046 0.0642  0.0727  28  LYS   B O   
4342 C  CB  . LYS   B 28  ? 0.2002 0.2659 0.3373 0.0085  0.0892  0.0968  28  LYS   B CB  
4343 C  CG  . LYS   B 28  ? 0.2390 0.3206 0.3799 0.0178  0.0976  0.1066  28  LYS   B CG  
4344 C  CD  . LYS   B 28  ? 0.2996 0.3887 0.4418 0.0218  0.1070  0.1080  28  LYS   B CD  
4345 C  CE  . LYS   B 28  ? 0.3453 0.4387 0.4922 0.0291  0.1059  0.1131  28  LYS   B CE  
4346 N  NZ  . LYS   B 28  ? 0.3778 0.4552 0.5145 0.0340  0.1042  0.1192  28  LYS   B NZ  
4360 N  N   . LYS   B 29  ? 0.2120 0.2724 0.2754 0.0181  0.0701  0.0638  29  LYS   B N   
4361 C  CA  . LYS   B 29  ? 0.2583 0.3084 0.2977 0.0174  0.0715  0.0622  29  LYS   B CA  
4362 C  C   . LYS   B 29  ? 0.2522 0.3135 0.2567 0.0186  0.0515  0.0767  29  LYS   B C   
4363 O  O   . LYS   B 29  ? 0.2736 0.3381 0.2669 0.0236  0.0479  0.0821  29  LYS   B O   
4364 C  CB  . LYS   B 29  ? 0.3154 0.3435 0.3772 0.0171  0.0692  0.0475  29  LYS   B CB  
4365 C  CG  . LYS   B 29  ? 0.3627 0.3726 0.4618 0.0146  0.0697  0.0403  29  LYS   B CG  
4366 C  CD  . LYS   B 29  ? 0.4036 0.3930 0.5288 0.0091  0.0758  0.0325  29  LYS   B CD  
4367 C  CE  . LYS   B 29  ? 0.4335 0.4061 0.5744 0.0040  0.0823  0.0279  29  LYS   B CE  
4368 N  NZ  . LYS   B 29  ? 0.4431 0.4130 0.6026 0.0023  0.0852  0.0242  29  LYS   B NZ  
4382 N  N   . VAL   B 30  ? 0.2194 0.2972 0.2430 0.0096  0.0400  0.0705  30  VAL   B N   
4383 C  CA  . VAL   B 30  ? 0.2055 0.2846 0.2742 -0.0037 0.0108  0.0728  30  VAL   B CA  
4384 C  C   . VAL   B 30  ? 0.1895 0.2800 0.2711 -0.0065 0.0131  0.0991  30  VAL   B C   
4385 O  O   . VAL   B 30  ? 0.2087 0.2944 0.2769 0.0006  0.0102  0.1161  30  VAL   B O   
4386 C  CB  . VAL   B 30  ? 0.2081 0.2740 0.3101 -0.0182 -0.0218 0.0628  30  VAL   B CB  
4387 C  CG1 . VAL   B 30  ? 0.2113 0.2784 0.3064 -0.0213 -0.0182 0.0571  30  VAL   B CG1 
4388 C  CG2 . VAL   B 30  ? 0.2247 0.2705 0.3295 -0.0266 -0.0325 0.0504  30  VAL   B CG2 
4398 N  N   . LYS   B 31  ? 0.1734 0.2485 0.3079 -0.0266 0.0105  0.1073  31  LYS   B N   
4399 C  CA  . LYS   B 31  ? 0.1624 0.2411 0.3412 -0.0415 0.0018  0.1120  31  LYS   B CA  
4400 C  C   . LYS   B 31  ? 0.1601 0.1994 0.2908 -0.0344 -0.0233 0.0960  31  LYS   B C   
4401 O  O   . LYS   B 31  ? 0.1705 0.2090 0.3149 -0.0271 -0.0142 0.1064  31  LYS   B O   
4402 C  CB  . LYS   B 31  ? 0.1759 0.2935 0.3993 -0.0394 0.0297  0.1243  31  LYS   B CB  
4403 C  CG  . LYS   B 31  ? 0.2139 0.3421 0.4403 -0.0357 0.0418  0.1171  31  LYS   B CG  
4404 C  CD  . LYS   B 31  ? 0.2582 0.3930 0.4743 -0.0276 0.0406  0.1024  31  LYS   B CD  
4405 C  CE  . LYS   B 31  ? 0.2895 0.4274 0.5099 -0.0244 0.0323  0.0877  31  LYS   B CE  
4406 N  NZ  . LYS   B 31  ? 0.3005 0.4418 0.5212 -0.0170 0.0225  0.0761  31  LYS   B NZ  
4420 N  N   . PRO   B 32  ? 0.1655 0.1640 0.2279 -0.0314 -0.0351 0.0581  32  PRO   B N   
4421 C  CA  . PRO   B 32  ? 0.1804 0.1592 0.1770 -0.0322 -0.0362 0.0288  32  PRO   B CA  
4422 C  C   . PRO   B 32  ? 0.1912 0.1535 0.1801 -0.0369 -0.0564 0.0339  32  PRO   B C   
4423 O  O   . PRO   B 32  ? 0.2023 0.1557 0.2155 -0.0384 -0.0743 0.0375  32  PRO   B O   
4424 C  CB  . PRO   B 32  ? 0.1946 0.1586 0.1703 -0.0416 -0.0278 0.0180  32  PRO   B CB  
4425 C  CG  . PRO   B 32  ? 0.2096 0.1484 0.1897 -0.0316 -0.0472 0.0243  32  PRO   B CG  
4426 C  CD  . PRO   B 32  ? 0.1952 0.1511 0.2093 -0.0305 -0.0520 0.0311  32  PRO   B CD  
4434 N  N   . THR   B 33  ? 0.1942 0.1452 0.1598 -0.0273 -0.0517 0.0260  33  THR   B N   
4435 C  CA  . THR   B 33  ? 0.1992 0.1497 0.1616 -0.0344 -0.0454 0.0269  33  THR   B CA  
4436 C  C   . THR   B 33  ? 0.2006 0.1366 0.1557 -0.0362 -0.0436 0.0202  33  THR   B C   
4437 O  O   . THR   B 33  ? 0.2261 0.1374 0.1731 -0.0463 -0.0524 0.0173  33  THR   B O   
4438 C  CB  . THR   B 33  ? 0.2084 0.1590 0.1693 -0.0156 -0.0514 0.0226  33  THR   B CB  
4439 O  OG1 . THR   B 33  ? 0.1941 0.1628 0.1769 -0.0202 -0.0472 0.0309  33  THR   B OG1 
4440 C  CG2 . THR   B 33  ? 0.2355 0.1697 0.1917 -0.0128 -0.0491 0.0268  33  THR   B CG2 
4448 N  N   . VAL   B 34  ? 0.1863 0.1394 0.1485 -0.0383 -0.0393 0.0103  34  VAL   B N   
4449 C  CA  . VAL   B 34  ? 0.1727 0.1400 0.1469 -0.0288 -0.0351 0.0048  34  VAL   B CA  
4450 C  C   . VAL   B 34  ? 0.1581 0.1301 0.1347 -0.0269 -0.0218 0.0055  34  VAL   B C   
4451 O  O   . VAL   B 34  ? 0.1753 0.1305 0.1353 -0.0249 -0.0346 0.0047  34  VAL   B O   
4452 C  CB  . VAL   B 34  ? 0.1740 0.1438 0.1783 -0.0072 -0.0335 0.0003  34  VAL   B CB  
4453 C  CG1 . VAL   B 34  ? 0.1771 0.1581 0.1807 -0.0098 -0.0144 -0.0029 34  VAL   B CG1 
4454 C  CG2 . VAL   B 34  ? 0.1794 0.1502 0.2123 -0.0103 -0.0261 0.0069  34  VAL   B CG2 
4464 N  N   . VAL   B 35  ? 0.1528 0.1286 0.1245 -0.0252 -0.0127 0.0092  35  VAL   B N   
4465 C  CA  . VAL   B 35  ? 0.1395 0.1271 0.1262 -0.0209 -0.0062 0.0111  35  VAL   B CA  
4466 C  C   . VAL   B 35  ? 0.1337 0.1261 0.1305 -0.0186 -0.0173 0.0078  35  VAL   B C   
4467 O  O   . VAL   B 35  ? 0.1407 0.1288 0.1342 -0.0228 -0.0031 -0.0046 35  VAL   B O   
4468 C  CB  . VAL   B 35  ? 0.1447 0.1454 0.1398 -0.0196 0.0017  0.0062  35  VAL   B CB  
4469 C  CG1 . VAL   B 35  ? 0.1367 0.1589 0.1706 -0.0176 -0.0004 0.0024  35  VAL   B CG1 
4470 C  CG2 . VAL   B 35  ? 0.1378 0.1459 0.1567 -0.0071 -0.0023 0.0005  35  VAL   B CG2 
4480 N  N   . VAL   B 36  ? 0.1312 0.1244 0.1281 -0.0175 -0.0125 0.0113  36  VAL   B N   
4481 C  CA  . VAL   B 36  ? 0.1358 0.1165 0.1204 -0.0111 -0.0092 0.0060  36  VAL   B CA  
4482 C  C   . VAL   B 36  ? 0.1343 0.1186 0.1188 -0.0130 -0.0055 0.0023  36  VAL   B C   
4483 O  O   . VAL   B 36  ? 0.1370 0.1328 0.1453 -0.0117 -0.0033 -0.0054 36  VAL   B O   
4484 C  CB  . VAL   B 36  ? 0.1385 0.1268 0.1270 -0.0174 -0.0058 0.0058  36  VAL   B CB  
4485 C  CG1 . VAL   B 36  ? 0.1357 0.1391 0.1479 -0.0217 -0.0094 0.0050  36  VAL   B CG1 
4486 C  CG2 . VAL   B 36  ? 0.1457 0.1338 0.1459 -0.0129 -0.0171 0.0057  36  VAL   B CG2 
4496 N  N   . ASN   B 37  ? 0.1304 0.1235 0.1316 -0.0021 -0.0017 0.0041  37  ASN   B N   
4497 C  CA  . ASN   B 37  ? 0.1354 0.1205 0.1405 -0.0011 -0.0163 0.0063  37  ASN   B CA  
4498 C  C   . ASN   B 37  ? 0.1333 0.1315 0.1320 0.0048  -0.0086 0.0063  37  ASN   B C   
4499 O  O   . ASN   B 37  ? 0.1434 0.1377 0.1357 -0.0001 0.0000  0.0082  37  ASN   B O   
4500 C  CB  . ASN   B 37  ? 0.1310 0.1318 0.1281 -0.0028 -0.0117 0.0054  37  ASN   B CB  
4501 C  CG  . ASN   B 37  ? 0.1399 0.1305 0.1405 -0.0061 -0.0108 -0.0022 37  ASN   B CG  
4502 O  OD1 . ASN   B 37  ? 0.1468 0.1331 0.1534 0.0022  -0.0129 0.0018  37  ASN   B OD1 
4503 N  ND2 . ASN   B 37  ? 0.1445 0.1274 0.1448 -0.0011 -0.0163 0.0058  37  ASN   B ND2 
4510 N  N   . ALA   B 38  ? 0.1433 0.1269 0.1318 0.0094  0.0035  0.0082  38  ALA   B N   
4511 C  CA  . ALA   B 38  ? 0.1522 0.1302 0.1373 0.0033  0.0032  0.0113  38  ALA   B CA  
4512 C  C   . ALA   B 38  ? 0.1475 0.1281 0.1369 -0.0006 0.0011  0.0093  38  ALA   B C   
4513 O  O   . ALA   B 38  ? 0.1577 0.1387 0.1501 0.0030  -0.0008 0.0085  38  ALA   B O   
4514 C  CB  . ALA   B 38  ? 0.1712 0.1454 0.1519 -0.0061 0.0095  0.0152  38  ALA   B CB  
4520 N  N   . ALA   B 39  ? 0.1466 0.1348 0.1314 0.0096  -0.0066 0.0012  39  ALA   B N   
4521 C  CA  . ALA   B 39  ? 0.1546 0.1378 0.1193 0.0049  -0.0112 0.0069  39  ALA   B CA  
4522 C  C   . ALA   B 39  ? 0.1586 0.1452 0.1185 0.0073  -0.0037 0.0035  39  ALA   B C   
4523 O  O   . ALA   B 39  ? 0.1630 0.1503 0.1473 -0.0022 -0.0051 0.0099  39  ALA   B O   
4524 C  CB  . ALA   B 39  ? 0.1538 0.1395 0.1495 -0.0034 -0.0001 -0.0017 39  ALA   B CB  
4530 N  N   . ASN   B 40  ? 0.1605 0.1656 0.1184 -0.0030 0.0001  -0.0076 40  ASN   B N   
4531 C  CA  . ASN   B 40  ? 0.1657 0.1723 0.1367 0.0003  -0.0089 -0.0078 40  ASN   B CA  
4532 C  C   . ASN   B 40  ? 0.1681 0.1736 0.1252 0.0049  -0.0106 0.0003  40  ASN   B C   
4533 O  O   . ASN   B 40  ? 0.1662 0.1640 0.1319 0.0084  -0.0089 0.0011  40  ASN   B O   
4534 C  CB  . ASN   B 40  ? 0.1808 0.1698 0.1645 0.0072  -0.0163 0.0136  40  ASN   B CB  
4535 C  CG  . ASN   B 40  ? 0.1880 0.1739 0.1861 0.0027  -0.0258 0.0182  40  ASN   B CG  
4536 O  OD1 . ASN   B 40  ? 0.1855 0.1679 0.2723 0.0003  -0.0339 0.0163  40  ASN   B OD1 
4537 N  ND2 . ASN   B 40  ? 0.1898 0.1723 0.1936 -0.0007 -0.0183 0.0174  40  ASN   B ND2 
4544 N  N   . VAL   B 41  ? 0.1791 0.1815 0.1272 0.0092  0.0055  -0.0089 41  VAL   B N   
4545 C  CA  . VAL   B 41  ? 0.1846 0.1940 0.1362 0.0088  0.0013  -0.0084 41  VAL   B CA  
4546 C  C   . VAL   B 41  ? 0.1831 0.1919 0.1283 0.0209  -0.0062 -0.0141 41  VAL   B C   
4547 O  O   . VAL   B 41  ? 0.1869 0.1883 0.1459 0.0137  -0.0158 -0.0133 41  VAL   B O   
4548 C  CB  . VAL   B 41  ? 0.2018 0.2088 0.1618 -0.0081 0.0223  -0.0193 41  VAL   B CB  
4549 C  CG1 . VAL   B 41  ? 0.1996 0.2091 0.1825 -0.0151 0.0301  -0.0223 41  VAL   B CG1 
4550 C  CG2 . VAL   B 41  ? 0.2105 0.2260 0.1732 -0.0154 0.0237  -0.0215 41  VAL   B CG2 
4560 N  N   . TYR   B 42  ? 0.1925 0.1870 0.1332 0.0184  -0.0164 0.0012  42  TYR   B N   
4561 C  CA  . TYR   B 42  ? 0.1978 0.1897 0.1383 0.0140  -0.0270 -0.0137 42  TYR   B CA  
4562 C  C   . TYR   B 42  ? 0.1828 0.1666 0.1454 0.0136  -0.0211 -0.0131 42  TYR   B C   
4563 O  O   . TYR   B 42  ? 0.1869 0.1819 0.1797 0.0061  -0.0253 -0.0186 42  TYR   B O   
4564 C  CB  . TYR   B 42  ? 0.2187 0.2207 0.1627 0.0111  -0.0317 0.0027  42  TYR   B CB  
4565 C  CG  . TYR   B 42  ? 0.2248 0.2447 0.1661 -0.0025 -0.0317 0.0136  42  TYR   B CG  
4566 C  CD1 . TYR   B 42  ? 0.2234 0.2440 0.1426 -0.0072 -0.0207 0.0053  42  TYR   B CD1 
4567 C  CD2 . TYR   B 42  ? 0.2418 0.2588 0.2034 -0.0000 -0.0077 0.0206  42  TYR   B CD2 
4568 C  CE1 . TYR   B 42  ? 0.2377 0.2601 0.1518 0.0001  -0.0064 0.0140  42  TYR   B CE1 
4569 C  CE2 . TYR   B 42  ? 0.2518 0.2699 0.1940 0.0030  0.0240  0.0427  42  TYR   B CE2 
4570 C  CZ  . TYR   B 42  ? 0.2596 0.2805 0.1834 0.0170  0.0226  0.0261  42  TYR   B CZ  
4571 O  OH  . TYR   B 42  ? 0.2918 0.3084 0.2299 0.0338  0.0346  0.0350  42  TYR   B OH  
4581 N  N   . LEU   B 43  ? 0.1696 0.1555 0.1340 0.0083  -0.0109 -0.0110 43  LEU   B N   
4582 C  CA  . LEU   B 43  ? 0.1705 0.1576 0.1258 0.0042  -0.0148 -0.0054 43  LEU   B CA  
4583 C  C   . LEU   B 43  ? 0.1741 0.1542 0.1365 0.0033  -0.0159 -0.0039 43  LEU   B C   
4584 O  O   . LEU   B 43  ? 0.1673 0.1617 0.1697 0.0047  -0.0233 0.0053  43  LEU   B O   
4585 C  CB  . LEU   B 43  ? 0.1670 0.1575 0.1510 -0.0018 -0.0213 -0.0087 43  LEU   B CB  
4586 C  CG  . LEU   B 43  ? 0.1695 0.1529 0.1544 0.0020  -0.0251 -0.0108 43  LEU   B CG  
4587 C  CD1 . LEU   B 43  ? 0.1775 0.1574 0.1903 -0.0016 -0.0354 -0.0114 43  LEU   B CD1 
4588 C  CD2 . LEU   B 43  ? 0.1638 0.1540 0.1668 -0.0037 -0.0172 -0.0090 43  LEU   B CD2 
4600 N  N   . LYS   B 44  ? 0.1714 0.1503 0.1468 0.0053  -0.0116 -0.0064 44  LYS   B N   
4601 C  CA  . LYS   B 44  ? 0.1830 0.1686 0.1467 0.0096  -0.0127 0.0043  44  LYS   B CA  
4602 C  C   . LYS   B 44  ? 0.1701 0.1665 0.1405 0.0076  -0.0167 0.0067  44  LYS   B C   
4603 O  O   . LYS   B 44  ? 0.1913 0.1656 0.1774 -0.0021 -0.0084 0.0049  44  LYS   B O   
4604 C  CB  . LYS   B 44  ? 0.2098 0.1838 0.1685 0.0181  -0.0288 -0.0008 44  LYS   B CB  
4605 C  CG  . LYS   B 44  ? 0.2492 0.2166 0.2023 0.0114  -0.0475 0.0042  44  LYS   B CG  
4606 C  CD  . LYS   B 44  ? 0.2862 0.2392 0.2648 -0.0058 -0.0550 0.0023  44  LYS   B CD  
4607 C  CE  . LYS   B 44  ? 0.3148 0.2642 0.3151 -0.0134 -0.0631 0.0186  44  LYS   B CE  
4608 N  NZ  . LYS   B 44  ? 0.3261 0.2733 0.3441 -0.0119 -0.0715 0.0372  44  LYS   B NZ  
4622 N  N   . HIS   B 45  ? 0.1663 0.1646 0.1283 0.0045  -0.0171 0.0116  45  HIS   B N   
4623 C  CA  . HIS   B 45  ? 0.1713 0.1623 0.1450 0.0060  -0.0070 -0.0006 45  HIS   B CA  
4624 C  C   . HIS   B 45  ? 0.1903 0.1817 0.1825 0.0173  -0.0187 -0.0033 45  HIS   B C   
4625 O  O   . HIS   B 45  ? 0.2047 0.2068 0.2333 0.0455  0.0074  -0.0041 45  HIS   B O   
4626 C  CB  . HIS   B 45  ? 0.1666 0.1661 0.1505 0.0005  -0.0062 -0.0114 45  HIS   B CB  
4627 C  CG  . HIS   B 45  ? 0.1664 0.1578 0.1522 -0.0060 -0.0098 -0.0054 45  HIS   B CG  
4628 N  ND1 . HIS   B 45  ? 0.1689 0.1509 0.1540 0.0011  -0.0173 -0.0095 45  HIS   B ND1 
4629 C  CD2 . HIS   B 45  ? 0.1753 0.1623 0.1580 -0.0119 -0.0173 -0.0020 45  HIS   B CD2 
4630 C  CE1 . HIS   B 45  ? 0.1786 0.1433 0.1393 -0.0058 -0.0248 -0.0038 45  HIS   B CE1 
4631 N  NE2 . HIS   B 45  ? 0.1811 0.1518 0.1514 -0.0001 -0.0207 -0.0031 45  HIS   B NE2 
4639 N  N   A GLY   B 46  ? 0.2019 0.1791 0.2151 0.0202  -0.0372 0.0111  46  GLY   B N   
4640 N  N   B GLY   B 46  ? 0.1995 0.1872 0.2021 0.0178  -0.0282 0.0077  46  GLY   B N   
4641 C  CA  A GLY   B 46  ? 0.2180 0.1893 0.2522 0.0187  -0.0466 0.0126  46  GLY   B CA  
4642 C  CA  B GLY   B 46  ? 0.2102 0.1968 0.2220 0.0155  -0.0357 0.0139  46  GLY   B CA  
4643 C  C   A GLY   B 46  ? 0.2200 0.2023 0.3002 0.0255  -0.0476 0.0024  46  GLY   B C   
4644 C  C   B GLY   B 46  ? 0.2161 0.2080 0.2474 0.0165  -0.0395 0.0152  46  GLY   B C   
4645 O  O   A GLY   B 46  ? 0.2288 0.2145 0.3923 0.0331  -0.0287 -0.0257 46  GLY   B O   
4646 O  O   B GLY   B 46  ? 0.2198 0.2173 0.2492 0.0208  -0.0434 0.0309  46  GLY   B O   
4653 N  N   . GLY   B 47  ? 0.2194 0.2117 0.2706 0.0048  -0.0262 -0.0044 47  GLY   B N   
4654 C  CA  . GLY   B 47  ? 0.2054 0.1854 0.2299 0.0011  -0.0204 0.0004  47  GLY   B CA  
4655 C  C   . GLY   B 47  ? 0.1809 0.1682 0.1883 0.0054  0.0047  0.0001  47  GLY   B C   
4656 O  O   . GLY   B 47  ? 0.1874 0.1544 0.1983 0.0057  -0.0076 0.0103  47  GLY   B O   
4661 N  N   . GLY   B 48  ? 0.1694 0.1609 0.1871 -0.0015 -0.0131 0.0157  48  GLY   B N   
4662 C  CA  . GLY   B 48  ? 0.1638 0.1585 0.1825 -0.0017 -0.0010 0.0113  48  GLY   B CA  
4663 C  C   . GLY   B 48  ? 0.1568 0.1473 0.1720 -0.0015 0.0087  0.0022  48  GLY   B C   
4664 O  O   . GLY   B 48  ? 0.1491 0.1524 0.1955 0.0049  -0.0080 0.0044  48  GLY   B O   
4668 N  N   . VAL   B 49  ? 0.1601 0.1547 0.1564 0.0100  0.0010  0.0105  49  VAL   B N   
4669 C  CA  . VAL   B 49  ? 0.1571 0.1616 0.1488 0.0138  -0.0166 -0.0068 49  VAL   B CA  
4670 C  C   . VAL   B 49  ? 0.1464 0.1495 0.1347 0.0109  -0.0062 0.0060  49  VAL   B C   
4671 O  O   . VAL   B 49  ? 0.1565 0.1550 0.1583 0.0072  -0.0008 0.0075  49  VAL   B O   
4672 C  CB  . VAL   B 49  ? 0.1646 0.1733 0.1879 0.0041  -0.0264 -0.0048 49  VAL   B CB  
4673 C  CG1 . VAL   B 49  ? 0.1631 0.1753 0.1877 0.0084  -0.0360 0.0000  49  VAL   B CG1 
4674 C  CG2 . VAL   B 49  ? 0.1794 0.1874 0.2158 -0.0069 -0.0381 -0.0073 49  VAL   B CG2 
4684 N  N   . ALA   B 50  ? 0.1383 0.1450 0.1549 0.0002  -0.0040 0.0096  50  ALA   B N   
4685 C  CA  . ALA   B 50  ? 0.1395 0.1421 0.1537 0.0043  -0.0034 0.0050  50  ALA   B CA  
4686 C  C   . ALA   B 50  ? 0.1466 0.1437 0.1501 0.0042  -0.0050 0.0041  50  ALA   B C   
4687 O  O   . ALA   B 50  ? 0.1527 0.1418 0.1443 0.0049  -0.0006 0.0012  50  ALA   B O   
4688 C  CB  . ALA   B 50  ? 0.1463 0.1425 0.1628 -0.0006 -0.0062 0.0097  50  ALA   B CB  
4694 N  N   . GLY   B 51  ? 0.1522 0.1508 0.1620 0.0114  -0.0111 0.0089  51  GLY   B N   
4695 C  CA  . GLY   B 51  ? 0.1519 0.1581 0.1729 0.0187  -0.0191 0.0123  51  GLY   B CA  
4696 C  C   . GLY   B 51  ? 0.1505 0.1517 0.1738 0.0198  -0.0133 0.0108  51  GLY   B C   
4697 O  O   . GLY   B 51  ? 0.1529 0.1621 0.1953 0.0110  -0.0120 0.0009  51  GLY   B O   
4701 N  N   . ALA   B 52  ? 0.1480 0.1526 0.1699 0.0192  -0.0033 0.0093  52  ALA   B N   
4702 C  CA  . ALA   B 52  ? 0.1538 0.1562 0.1733 0.0189  0.0018  -0.0026 52  ALA   B CA  
4703 C  C   . ALA   B 52  ? 0.1470 0.1517 0.1510 0.0082  0.0022  0.0041  52  ALA   B C   
4704 O  O   . ALA   B 52  ? 0.1541 0.1584 0.1728 0.0111  0.0039  0.0043  52  ALA   B O   
4705 C  CB  . ALA   B 52  ? 0.1764 0.1586 0.1823 0.0089  0.0017  -0.0068 52  ALA   B CB  
4711 N  N   . LEU   B 53  ? 0.1370 0.1489 0.1592 0.0195  0.0006  0.0022  53  LEU   B N   
4712 C  CA  . LEU   B 53  ? 0.1431 0.1570 0.1509 0.0132  -0.0058 0.0059  53  LEU   B CA  
4713 C  C   . LEU   B 53  ? 0.1500 0.1486 0.1433 0.0105  0.0028  0.0071  53  LEU   B C   
4714 O  O   . LEU   B 53  ? 0.1502 0.1572 0.1642 0.0007  0.0083  0.0155  53  LEU   B O   
4715 C  CB  . LEU   B 53  ? 0.1492 0.1645 0.1647 0.0113  -0.0040 0.0182  53  LEU   B CB  
4716 C  CG  . LEU   B 53  ? 0.1452 0.1691 0.1738 0.0063  -0.0020 0.0161  53  LEU   B CG  
4717 C  CD1 . LEU   B 53  ? 0.1508 0.1907 0.2104 0.0106  -0.0025 0.0120  53  LEU   B CD1 
4718 C  CD2 . LEU   B 53  ? 0.1582 0.2004 0.1976 -0.0042 -0.0104 -0.0105 53  LEU   B CD2 
4730 N  N   . ASN   B 54  ? 0.1474 0.1394 0.1434 0.0054  -0.0022 0.0022  54  ASN   B N   
4731 C  CA  . ASN   B 54  ? 0.1537 0.1523 0.1584 0.0050  -0.0057 -0.0022 54  ASN   B CA  
4732 C  C   . ASN   B 54  ? 0.1462 0.1583 0.1745 0.0019  -0.0013 0.0043  54  ASN   B C   
4733 O  O   . ASN   B 54  ? 0.1453 0.1649 0.1903 -0.0037 0.0084  0.0026  54  ASN   B O   
4734 C  CB  . ASN   B 54  ? 0.1578 0.1682 0.1653 0.0072  -0.0036 0.0041  54  ASN   B CB  
4735 C  CG  . ASN   B 54  ? 0.1545 0.1749 0.1592 0.0073  -0.0069 0.0018  54  ASN   B CG  
4736 O  OD1 . ASN   B 54  ? 0.1499 0.1752 0.1773 0.0060  -0.0133 -0.0110 54  ASN   B OD1 
4737 N  ND2 . ASN   B 54  ? 0.1724 0.1892 0.1992 0.0030  -0.0269 0.0184  54  ASN   B ND2 
4744 N  N   . LYS   B 55  ? 0.1444 0.1685 0.1849 0.0143  -0.0001 0.0006  55  LYS   B N   
4745 C  CA  . LYS   B 55  ? 0.1530 0.1771 0.2111 0.0181  -0.0077 0.0052  55  LYS   B CA  
4746 C  C   . LYS   B 55  ? 0.1537 0.1760 0.1963 0.0128  0.0074  -0.0072 55  LYS   B C   
4747 O  O   . LYS   B 55  ? 0.1465 0.1878 0.2219 0.0095  0.0125  -0.0019 55  LYS   B O   
4748 C  CB  . LYS   B 55  ? 0.1588 0.1881 0.2604 0.0270  0.0097  0.0136  55  LYS   B CB  
4749 C  CG  . LYS   B 55  ? 0.1955 0.2169 0.3414 0.0318  0.0215  0.0329  55  LYS   B CG  
4750 C  CD  . LYS   B 55  ? 0.2305 0.2372 0.4110 0.0398  0.0350  0.0490  55  LYS   B CD  
4751 C  CE  . LYS   B 55  ? 0.2593 0.2614 0.4800 0.0381  0.0510  0.0551  55  LYS   B CE  
4752 N  NZ  . LYS   B 55  ? 0.2733 0.2782 0.5144 0.0381  0.0361  0.0662  55  LYS   B NZ  
4766 N  N   . ALA   B 56  ? 0.1545 0.1829 0.1747 0.0071  -0.0057 -0.0146 56  ALA   B N   
4767 C  CA  . ALA   B 56  ? 0.1644 0.1978 0.1810 -0.0002 0.0016  -0.0117 56  ALA   B CA  
4768 C  C   . ALA   B 56  ? 0.1597 0.1884 0.1797 0.0010  0.0132  -0.0004 56  ALA   B C   
4769 O  O   . ALA   B 56  ? 0.1763 0.1963 0.2034 0.0061  0.0337  0.0036  56  ALA   B O   
4770 C  CB  . ALA   B 56  ? 0.1798 0.2191 0.1824 -0.0119 -0.0061 -0.0074 56  ALA   B CB  
4776 N  N   . THR   B 57  ? 0.1507 0.1803 0.1931 0.0027  0.0214  0.0016  57  THR   B N   
4777 C  CA  . THR   B 57  ? 0.1617 0.1773 0.1956 -0.0041 0.0216  0.0079  57  THR   B CA  
4778 C  C   . THR   B 57  ? 0.1642 0.1848 0.2166 -0.0060 0.0193  0.0084  57  THR   B C   
4779 O  O   . THR   B 57  ? 0.1758 0.1903 0.2123 -0.0194 0.0168  0.0035  57  THR   B O   
4780 C  CB  . THR   B 57  ? 0.1719 0.1613 0.1678 -0.0064 0.0172  0.0141  57  THR   B CB  
4781 O  OG1 . THR   B 57  ? 0.1678 0.1608 0.1854 -0.0024 0.0127  0.0072  57  THR   B OG1 
4782 C  CG2 . THR   B 57  ? 0.1690 0.1685 0.1727 -0.0101 0.0111  0.0064  57  THR   B CG2 
4790 N  N   . ASN   B 58  ? 0.1485 0.2055 0.2245 -0.0135 0.0001  -0.0071 58  ASN   B N   
4791 C  CA  . ASN   B 58  ? 0.1695 0.2498 0.2708 -0.0280 0.0301  -0.0009 58  ASN   B CA  
4792 C  C   . ASN   B 58  ? 0.1515 0.2242 0.2301 -0.0179 0.0030  -0.0043 58  ASN   B C   
4793 O  O   . ASN   B 58  ? 0.1524 0.2399 0.2415 -0.0188 0.0075  -0.0173 58  ASN   B O   
4794 C  CB  . ASN   B 58  ? 0.2665 0.3319 0.4034 -0.0423 0.0611  0.0143  58  ASN   B CB  
4795 C  CG  . ASN   B 58  ? 0.3789 0.4113 0.5593 -0.0462 0.0729  0.0394  58  ASN   B CG  
4796 O  OD1 . ASN   B 58  ? 0.4013 0.4337 0.6199 -0.0477 0.0749  0.0464  58  ASN   B OD1 
4797 N  ND2 . ASN   B 58  ? 0.4770 0.4770 0.6086 -0.0488 0.0790  0.0471  58  ASN   B ND2 
4804 N  N   . ASN   B 59  ? 0.1548 0.2103 0.2038 -0.0098 -0.0054 0.0052  59  ASN   B N   
4805 C  CA  . ASN   B 59  ? 0.1561 0.2071 0.2003 -0.0100 -0.0176 0.0152  59  ASN   B CA  
4806 C  C   . ASN   B 59  ? 0.1495 0.1938 0.1891 -0.0139 -0.0175 -0.0011 59  ASN   B C   
4807 O  O   . ASN   B 59  ? 0.1555 0.1933 0.1897 -0.0147 -0.0135 -0.0033 59  ASN   B O   
4808 C  CB  . ASN   B 59  ? 0.1671 0.2212 0.2188 -0.0105 -0.0253 0.0171  59  ASN   B CB  
4809 C  CG  . ASN   B 59  ? 0.1787 0.2419 0.2405 -0.0053 -0.0342 0.0132  59  ASN   B CG  
4810 O  OD1 . ASN   B 59  ? 0.1815 0.2454 0.2335 0.0005  -0.0265 0.0248  59  ASN   B OD1 
4811 N  ND2 . ASN   B 59  ? 0.1833 0.2550 0.2474 -0.0107 -0.0350 0.0106  59  ASN   B ND2 
4818 N  N   . ALA   B 60  ? 0.1529 0.1868 0.1943 -0.0127 -0.0023 -0.0048 60  ALA   B N   
4819 C  CA  . ALA   B 60  ? 0.1547 0.1768 0.1917 -0.0160 -0.0060 0.0052  60  ALA   B CA  
4820 C  C   . ALA   B 60  ? 0.1566 0.1668 0.1715 -0.0164 -0.0056 0.0034  60  ALA   B C   
4821 O  O   . ALA   B 60  ? 0.1622 0.1695 0.1923 -0.0216 0.0035  -0.0062 60  ALA   B O   
4822 C  CB  . ALA   B 60  ? 0.1685 0.1762 0.2201 -0.0159 0.0086  0.0038  60  ALA   B CB  
4828 N  N   . MET   B 61  ? 0.1510 0.1563 0.1742 -0.0135 -0.0008 0.0058  61  MET   B N   
4829 C  CA  . MET   B 61  ? 0.1480 0.1579 0.1701 -0.0113 -0.0113 0.0016  61  MET   B CA  
4830 C  C   . MET   B 61  ? 0.1597 0.1504 0.1666 -0.0126 -0.0126 0.0099  61  MET   B C   
4831 O  O   . MET   B 61  ? 0.1578 0.1488 0.1665 -0.0026 -0.0057 -0.0127 61  MET   B O   
4832 C  CB  . MET   B 61  ? 0.1451 0.1590 0.1674 -0.0049 -0.0091 0.0024  61  MET   B CB  
4833 C  CG  . MET   B 61  ? 0.1420 0.1519 0.1589 -0.0062 -0.0075 0.0058  61  MET   B CG  
4834 S  SD  . MET   B 61  ? 0.1456 0.1569 0.1815 -0.0034 -0.0058 -0.0067 61  MET   B SD  
4835 C  CE  . MET   B 61  ? 0.1546 0.1748 0.1973 0.0003  -0.0025 -0.0249 61  MET   B CE  
4845 N  N   . GLN   B 62  ? 0.1529 0.1565 0.1570 -0.0078 -0.0158 0.0097  62  GLN   B N   
4846 C  CA  . GLN   B 62  ? 0.1593 0.1636 0.1610 0.0005  -0.0181 0.0022  62  GLN   B CA  
4847 C  C   . GLN   B 62  ? 0.1558 0.1664 0.1629 -0.0042 -0.0272 -0.0086 62  GLN   B C   
4848 O  O   . GLN   B 62  ? 0.1669 0.1717 0.1731 -0.0048 -0.0288 -0.0099 62  GLN   B O   
4849 C  CB  . GLN   B 62  ? 0.1621 0.1713 0.1609 -0.0015 -0.0097 0.0089  62  GLN   B CB  
4850 C  CG  . GLN   B 62  ? 0.1682 0.1730 0.1638 -0.0035 -0.0214 0.0073  62  GLN   B CG  
4851 C  CD  . GLN   B 62  ? 0.1660 0.1654 0.1512 0.0047  -0.0239 0.0113  62  GLN   B CD  
4852 O  OE1 . GLN   B 62  ? 0.1626 0.1637 0.1804 0.0038  -0.0281 -0.0023 62  GLN   B OE1 
4853 N  NE2 . GLN   B 62  ? 0.1638 0.1740 0.1683 0.0017  -0.0203 -0.0052 62  GLN   B NE2 
4862 N  N   . VAL   B 63  ? 0.1544 0.1702 0.1866 -0.0098 -0.0226 -0.0103 63  VAL   B N   
4863 C  CA  . VAL   B 63  ? 0.1662 0.1721 0.2075 -0.0157 -0.0280 -0.0088 63  VAL   B CA  
4864 C  C   . VAL   B 63  ? 0.1683 0.1651 0.1804 -0.0194 -0.0290 -0.0153 63  VAL   B C   
4865 O  O   . VAL   B 63  ? 0.1842 0.1634 0.2061 -0.0127 -0.0483 -0.0108 63  VAL   B O   
4866 C  CB  . VAL   B 63  ? 0.1642 0.1877 0.2482 -0.0238 -0.0264 -0.0111 63  VAL   B CB  
4867 C  CG1 . VAL   B 63  ? 0.1654 0.1916 0.2681 -0.0302 -0.0215 -0.0112 63  VAL   B CG1 
4868 C  CG2 . VAL   B 63  ? 0.1595 0.2062 0.2640 -0.0156 -0.0287 0.0007  63  VAL   B CG2 
4878 N  N   . GLU   B 64  ? 0.1653 0.1595 0.1782 -0.0173 -0.0214 -0.0080 64  GLU   B N   
4879 C  CA  . GLU   B 64  ? 0.1655 0.1469 0.1707 -0.0140 -0.0308 -0.0008 64  GLU   B CA  
4880 C  C   . GLU   B 64  ? 0.1599 0.1479 0.1694 -0.0107 -0.0246 -0.0097 64  GLU   B C   
4881 O  O   . GLU   B 64  ? 0.1745 0.1597 0.1663 -0.0138 -0.0263 -0.0176 64  GLU   B O   
4882 C  CB  . GLU   B 64  ? 0.1664 0.1566 0.1774 -0.0213 -0.0231 0.0040  64  GLU   B CB  
4883 C  CG  . GLU   B 64  ? 0.1757 0.1600 0.1789 -0.0313 -0.0286 -0.0155 64  GLU   B CG  
4884 C  CD  . GLU   B 64  ? 0.1760 0.1754 0.1852 -0.0369 -0.0316 -0.0122 64  GLU   B CD  
4885 O  OE1 . GLU   B 64  ? 0.1799 0.1906 0.2032 -0.0363 -0.0217 -0.0296 64  GLU   B OE1 
4886 O  OE2 . GLU   B 64  ? 0.1884 0.1885 0.1923 -0.0369 -0.0440 -0.0099 64  GLU   B OE2 
4893 N  N   . SER   B 65  ? 0.1648 0.1455 0.1614 -0.0121 -0.0170 -0.0157 65  SER   B N   
4894 C  CA  . SER   B 65  ? 0.1614 0.1412 0.1651 -0.0028 -0.0195 -0.0137 65  SER   B CA  
4895 C  C   . SER   B 65  ? 0.1644 0.1499 0.1599 0.0050  -0.0227 -0.0186 65  SER   B C   
4896 O  O   . SER   B 65  ? 0.1638 0.1617 0.1671 0.0034  -0.0269 -0.0246 65  SER   B O   
4897 C  CB  . SER   B 65  ? 0.1635 0.1451 0.1600 -0.0128 -0.0157 -0.0089 65  SER   B CB  
4898 O  OG  . SER   B 65  ? 0.1670 0.1487 0.1703 -0.0097 -0.0193 -0.0183 65  SER   B OG  
4904 N  N   . ASP   B 66  ? 0.1732 0.1555 0.1619 -0.0006 -0.0267 -0.0160 66  ASP   B N   
4905 C  CA  . ASP   B 66  ? 0.1818 0.1637 0.1556 0.0038  -0.0324 -0.0145 66  ASP   B CA  
4906 C  C   . ASP   B 66  ? 0.1888 0.1700 0.1419 -0.0053 -0.0224 -0.0144 66  ASP   B C   
4907 O  O   . ASP   B 66  ? 0.1905 0.1737 0.1539 0.0023  -0.0276 -0.0215 66  ASP   B O   
4908 C  CB  . ASP   B 66  ? 0.1936 0.1757 0.1772 0.0064  -0.0418 -0.0166 66  ASP   B CB  
4909 C  CG  . ASP   B 66  ? 0.2231 0.1933 0.2076 0.0133  -0.0554 -0.0055 66  ASP   B CG  
4910 O  OD1 . ASP   B 66  ? 0.2427 0.1867 0.2111 0.0082  -0.0547 0.0039  66  ASP   B OD1 
4911 O  OD2 . ASP   B 66  ? 0.2470 0.2140 0.2670 0.0337  -0.0542 -0.0017 66  ASP   B OD2 
4916 N  N   . ASP   B 67  ? 0.1769 0.1638 0.1517 -0.0144 -0.0233 -0.0122 67  ASP   B N   
4917 C  CA  . ASP   B 67  ? 0.1927 0.1603 0.1658 -0.0096 -0.0244 -0.0084 67  ASP   B CA  
4918 C  C   . ASP   B 67  ? 0.1880 0.1570 0.1801 0.0015  -0.0218 -0.0180 67  ASP   B C   
4919 O  O   . ASP   B 67  ? 0.1910 0.1624 0.1912 0.0047  -0.0185 -0.0253 67  ASP   B O   
4920 C  CB  . ASP   B 67  ? 0.2180 0.1740 0.1863 -0.0198 -0.0370 -0.0004 67  ASP   B CB  
4921 C  CG  . ASP   B 67  ? 0.2546 0.1798 0.1944 -0.0177 -0.0673 -0.0111 67  ASP   B CG  
4922 O  OD1 . ASP   B 67  ? 0.2786 0.1881 0.2126 -0.0164 -0.0614 -0.0114 67  ASP   B OD1 
4923 O  OD2 . ASP   B 67  ? 0.2700 0.1833 0.2120 -0.0031 -0.0731 -0.0089 67  ASP   B OD2 
4928 N  N   . TYR   B 68  ? 0.1821 0.1583 0.1682 0.0010  -0.0359 -0.0281 68  TYR   B N   
4929 C  CA  . TYR   B 68  ? 0.1762 0.1780 0.1814 0.0101  -0.0406 -0.0297 68  TYR   B CA  
4930 C  C   . TYR   B 68  ? 0.1679 0.1761 0.1848 0.0077  -0.0339 -0.0404 68  TYR   B C   
4931 O  O   . TYR   B 68  ? 0.1790 0.1844 0.1915 0.0121  -0.0316 -0.0542 68  TYR   B O   
4932 C  CB  . TYR   B 68  ? 0.1803 0.1945 0.1896 0.0074  -0.0503 -0.0435 68  TYR   B CB  
4933 C  CG  . TYR   B 68  ? 0.1924 0.2109 0.1994 0.0132  -0.0408 -0.0622 68  TYR   B CG  
4934 C  CD1 . TYR   B 68  ? 0.1936 0.2172 0.2316 -0.0088 -0.0373 -0.0760 68  TYR   B CD1 
4935 C  CD2 . TYR   B 68  ? 0.1961 0.2317 0.2243 0.0229  -0.0514 -0.0580 68  TYR   B CD2 
4936 C  CE1 . TYR   B 68  ? 0.1969 0.2357 0.2552 -0.0021 -0.0284 -0.0738 68  TYR   B CE1 
4937 C  CE2 . TYR   B 68  ? 0.1975 0.2395 0.2367 0.0200  -0.0313 -0.0744 68  TYR   B CE2 
4938 C  CZ  . TYR   B 68  ? 0.1917 0.2406 0.2542 0.0080  -0.0310 -0.0739 68  TYR   B CZ  
4939 O  OH  . TYR   B 68  ? 0.1871 0.2603 0.2732 0.0059  -0.0291 -0.0528 68  TYR   B OH  
4949 N  N   . ILE   B 69  ? 0.1701 0.1676 0.1909 0.0079  -0.0300 -0.0401 69  ILE   B N   
4950 C  CA  . ILE   B 69  ? 0.1823 0.1744 0.1929 -0.0016 -0.0224 -0.0446 69  ILE   B CA  
4951 C  C   . ILE   B 69  ? 0.1825 0.1698 0.1800 0.0081  -0.0345 -0.0346 69  ILE   B C   
4952 O  O   . ILE   B 69  ? 0.1864 0.1798 0.1814 0.0080  -0.0198 -0.0400 69  ILE   B O   
4953 C  CB  . ILE   B 69  ? 0.1868 0.1793 0.2019 -0.0048 0.0057  -0.0355 69  ILE   B CB  
4954 C  CG1 . ILE   B 69  ? 0.1880 0.1832 0.2156 -0.0099 0.0135  -0.0339 69  ILE   B CG1 
4955 C  CG2 . ILE   B 69  ? 0.2024 0.1863 0.2210 -0.0044 0.0092  -0.0264 69  ILE   B CG2 
4956 C  CD1 . ILE   B 69  ? 0.1841 0.1908 0.2269 -0.0187 0.0106  -0.0356 69  ILE   B CD1 
4968 N  N   . ALA   B 70  ? 0.1816 0.1673 0.1849 0.0064  -0.0392 -0.0299 70  ALA   B N   
4969 C  CA  . ALA   B 70  ? 0.1801 0.1710 0.1701 0.0060  -0.0422 -0.0278 70  ALA   B CA  
4970 C  C   . ALA   B 70  ? 0.1827 0.1661 0.1873 0.0033  -0.0472 -0.0374 70  ALA   B C   
4971 O  O   . ALA   B 70  ? 0.1910 0.1704 0.1919 0.0053  -0.0449 -0.0413 70  ALA   B O   
4972 C  CB  . ALA   B 70  ? 0.1811 0.1894 0.1781 0.0011  -0.0444 -0.0288 70  ALA   B CB  
4978 N  N   . THR   B 71  ? 0.1968 0.1723 0.1943 0.0021  -0.0565 -0.0366 71  THR   B N   
4979 C  CA  . THR   B 71  ? 0.2098 0.1753 0.2074 0.0084  -0.0646 -0.0325 71  THR   B CA  
4980 C  C   . THR   B 71  ? 0.2009 0.1802 0.2289 0.0285  -0.0585 -0.0509 71  THR   B C   
4981 O  O   . THR   B 71  ? 0.2129 0.1867 0.2694 0.0337  -0.0548 -0.0620 71  THR   B O   
4982 C  CB  . THR   B 71  ? 0.2320 0.1877 0.2307 -0.0032 -0.0716 -0.0109 71  THR   B CB  
4983 O  OG1 . THR   B 71  ? 0.2474 0.2131 0.2722 -0.0214 -0.0629 0.0096  71  THR   B OG1 
4984 C  CG2 . THR   B 71  ? 0.2466 0.1868 0.2611 -0.0011 -0.0641 -0.0004 71  THR   B CG2 
4992 N  N   . ASN   B 72  ? 0.1861 0.1888 0.2161 0.0146  -0.0617 -0.0686 72  ASN   B N   
4993 C  CA  . ASN   B 72  ? 0.1871 0.1983 0.2297 0.0136  -0.0483 -0.0725 72  ASN   B CA  
4994 C  C   . ASN   B 72  ? 0.1882 0.2077 0.2401 -0.0028 -0.0232 -0.0686 72  ASN   B C   
4995 O  O   . ASN   B 72  ? 0.1923 0.2237 0.2682 0.0010  -0.0065 -0.0747 72  ASN   B O   
4996 C  CB  . ASN   B 72  ? 0.1994 0.2170 0.2402 0.0104  -0.0610 -0.0601 72  ASN   B CB  
4997 C  CG  . ASN   B 72  ? 0.2121 0.2317 0.2542 0.0259  -0.0620 -0.0386 72  ASN   B CG  
4998 O  OD1 . ASN   B 72  ? 0.2380 0.2484 0.2528 0.0158  -0.0396 -0.0425 72  ASN   B OD1 
4999 N  ND2 . ASN   B 72  ? 0.2243 0.2351 0.2905 0.0441  -0.0538 -0.0024 72  ASN   B ND2 
5006 N  N   . GLY   B 73  ? 0.1945 0.2014 0.2180 -0.0047 -0.0343 -0.0683 73  GLY   B N   
5007 C  CA  . GLY   B 73  ? 0.1857 0.2098 0.1929 -0.0047 -0.0260 -0.0545 73  GLY   B CA  
5008 C  C   . GLY   B 73  ? 0.1876 0.2067 0.1502 0.0030  -0.0283 -0.0426 73  GLY   B C   
5009 O  O   . GLY   B 73  ? 0.1812 0.1937 0.1684 0.0048  -0.0205 -0.0272 73  GLY   B O   
5013 N  N   . PRO   B 74  ? 0.1912 0.2213 0.1474 0.0015  -0.0333 -0.0420 74  PRO   B N   
5014 C  CA  . PRO   B 74  ? 0.1830 0.2215 0.1369 0.0098  -0.0303 -0.0250 74  PRO   B CA  
5015 C  C   . PRO   B 74  ? 0.1673 0.2016 0.1402 0.0092  -0.0125 -0.0165 74  PRO   B C   
5016 O  O   . PRO   B 74  ? 0.1711 0.1994 0.1816 0.0097  -0.0084 -0.0357 74  PRO   B O   
5017 C  CB  . PRO   B 74  ? 0.1979 0.2392 0.1532 0.0067  -0.0216 -0.0206 74  PRO   B CB  
5018 C  CG  . PRO   B 74  ? 0.2171 0.2489 0.1795 0.0064  -0.0170 -0.0209 74  PRO   B CG  
5019 C  CD  . PRO   B 74  ? 0.2108 0.2374 0.1630 0.0084  -0.0175 -0.0370 74  PRO   B CD  
5027 N  N   . LEU   B 75  ? 0.1620 0.1853 0.1376 0.0077  -0.0166 -0.0208 75  LEU   B N   
5028 C  CA  . LEU   B 75  ? 0.1612 0.1851 0.1373 0.0028  -0.0173 -0.0046 75  LEU   B CA  
5029 C  C   . LEU   B 75  ? 0.1676 0.2020 0.1348 -0.0007 -0.0083 -0.0039 75  LEU   B C   
5030 O  O   . LEU   B 75  ? 0.1817 0.2183 0.1478 -0.0054 -0.0068 -0.0000 75  LEU   B O   
5031 C  CB  . LEU   B 75  ? 0.1710 0.1939 0.1299 -0.0085 -0.0205 0.0074  75  LEU   B CB  
5032 C  CG  . LEU   B 75  ? 0.2041 0.2121 0.1503 -0.0362 -0.0106 0.0047  75  LEU   B CG  
5033 C  CD1 . LEU   B 75  ? 0.2387 0.2218 0.1524 -0.0429 0.0091  -0.0030 75  LEU   B CD1 
5034 C  CD2 . LEU   B 75  ? 0.2373 0.2338 0.2189 -0.0290 0.0064  0.0093  75  LEU   B CD2 
5046 N  N   . LYS   B 76  ? 0.1708 0.2205 0.1598 0.0003  -0.0018 0.0046  76  LYS   B N   
5047 C  CA  . LYS   B 76  ? 0.1847 0.2316 0.1905 -0.0081 0.0203  -0.0024 76  LYS   B CA  
5048 C  C   . LYS   B 76  ? 0.1782 0.2142 0.1597 -0.0046 0.0110  0.0122  76  LYS   B C   
5049 O  O   . LYS   B 76  ? 0.1745 0.1972 0.1654 -0.0047 0.0049  0.0152  76  LYS   B O   
5050 C  CB  . LYS   B 76  ? 0.1987 0.2439 0.2483 -0.0134 0.0405  -0.0344 76  LYS   B CB  
5051 C  CG  . LYS   B 76  ? 0.2099 0.2647 0.2975 0.0001  0.0298  -0.0403 76  LYS   B CG  
5052 C  CD  . LYS   B 76  ? 0.2129 0.2715 0.3359 0.0084  0.0179  -0.0570 76  LYS   B CD  
5053 C  CE  . LYS   B 76  ? 0.2234 0.2883 0.3895 0.0125  -0.0006 -0.0659 76  LYS   B CE  
5054 N  NZ  . LYS   B 76  ? 0.2249 0.2950 0.4063 0.0087  -0.0276 -0.0852 76  LYS   B NZ  
5068 N  N   . VAL   B 77  ? 0.1804 0.2251 0.1655 0.0064  0.0088  0.0214  77  VAL   B N   
5069 C  CA  . VAL   B 77  ? 0.1843 0.2154 0.1707 0.0141  0.0138  0.0487  77  VAL   B CA  
5070 C  C   . VAL   B 77  ? 0.1728 0.1945 0.1654 0.0167  0.0260  0.0350  77  VAL   B C   
5071 O  O   . VAL   B 77  ? 0.1761 0.1900 0.1682 0.0235  0.0270  0.0235  77  VAL   B O   
5072 C  CB  . VAL   B 77  ? 0.1938 0.2261 0.2091 0.0144  0.0255  0.0660  77  VAL   B CB  
5073 C  CG1 . VAL   B 77  ? 0.2032 0.2172 0.2464 0.0049  0.0237  0.0801  77  VAL   B CG1 
5074 C  CG2 . VAL   B 77  ? 0.2105 0.2426 0.2289 0.0108  0.0115  0.0725  77  VAL   B CG2 
5084 N  N   . GLY   B 78  ? 0.1715 0.1804 0.1594 0.0081  0.0212  0.0281  78  GLY   B N   
5085 C  CA  . GLY   B 78  ? 0.1690 0.1679 0.1583 0.0100  0.0258  0.0197  78  GLY   B CA  
5086 C  C   . GLY   B 78  ? 0.1595 0.1665 0.1534 0.0071  0.0156  0.0134  78  GLY   B C   
5087 O  O   . GLY   B 78  ? 0.1635 0.1653 0.1624 0.0137  0.0148  0.0186  78  GLY   B O   
5091 N  N   . GLY   B 79  ? 0.1499 0.1710 0.1532 0.0085  0.0073  0.0095  79  GLY   B N   
5092 C  CA  . GLY   B 79  ? 0.1553 0.1643 0.1475 0.0117  0.0090  0.0087  79  GLY   B CA  
5093 C  C   . GLY   B 79  ? 0.1418 0.1569 0.1492 0.0070  0.0086  0.0052  79  GLY   B C   
5094 O  O   . GLY   B 79  ? 0.1531 0.1552 0.1718 0.0094  0.0156  0.0186  79  GLY   B O   
5098 N  N   . SER   B 80  ? 0.1459 0.1495 0.1606 0.0038  0.0184  0.0017  80  SER   B N   
5099 C  CA  . SER   B 80  ? 0.1416 0.1477 0.1611 0.0024  0.0014  0.0033  80  SER   B CA  
5100 C  C   . SER   B 80  ? 0.1403 0.1462 0.1634 0.0083  -0.0032 -0.0006 80  SER   B C   
5101 O  O   . SER   B 80  ? 0.1559 0.1460 0.1901 0.0097  0.0064  -0.0048 80  SER   B O   
5102 C  CB  . SER   B 80  ? 0.1472 0.1551 0.1659 -0.0042 0.0004  0.0106  80  SER   B CB  
5103 O  OG  . SER   B 80  ? 0.1548 0.1661 0.1840 -0.0039 -0.0143 0.0147  80  SER   B OG  
5109 N  N   . CYS   B 81  ? 0.1440 0.1321 0.1635 -0.0004 -0.0098 0.0004  81  CYS   B N   
5110 C  CA  . CYS   B 81  ? 0.1504 0.1252 0.1586 0.0034  -0.0160 0.0051  81  CYS   B CA  
5111 C  C   . CYS   B 81  ? 0.1390 0.1318 0.1403 0.0017  -0.0148 0.0037  81  CYS   B C   
5112 O  O   . CYS   B 81  ? 0.1620 0.1340 0.1602 0.0108  -0.0048 -0.0094 81  CYS   B O   
5113 C  CB  . CYS   B 81  ? 0.1682 0.1432 0.1669 -0.0065 -0.0131 0.0017  81  CYS   B CB  
5114 S  SG  . CYS   B 81  ? 0.1690 0.1616 0.1610 -0.0047 -0.0264 -0.0137 81  CYS   B SG  
5120 N  N   . VAL   B 82  ? 0.1445 0.1343 0.1467 0.0009  -0.0083 -0.0022 82  VAL   B N   
5121 C  CA  . VAL   B 82  ? 0.1527 0.1338 0.1477 -0.0100 -0.0123 0.0051  82  VAL   B CA  
5122 C  C   . VAL   B 82  ? 0.1620 0.1312 0.1621 -0.0020 -0.0054 -0.0077 82  VAL   B C   
5123 O  O   . VAL   B 82  ? 0.1665 0.1325 0.1951 -0.0038 -0.0111 -0.0204 82  VAL   B O   
5124 C  CB  . VAL   B 82  ? 0.1631 0.1502 0.1639 -0.0039 -0.0144 0.0070  82  VAL   B CB  
5125 C  CG1 . VAL   B 82  ? 0.1814 0.1706 0.1677 0.0022  -0.0226 0.0185  82  VAL   B CG1 
5126 C  CG2 . VAL   B 82  ? 0.1754 0.1632 0.1767 -0.0053 -0.0267 0.0114  82  VAL   B CG2 
5136 N  N   . LEU   B 83  ? 0.1485 0.1287 0.1456 -0.0150 -0.0176 -0.0052 83  LEU   B N   
5137 C  CA  . LEU   B 83  ? 0.1508 0.1343 0.1379 -0.0125 -0.0189 -0.0050 83  LEU   B CA  
5138 C  C   . LEU   B 83  ? 0.1525 0.1341 0.1398 -0.0186 -0.0183 -0.0023 83  LEU   B C   
5139 O  O   . LEU   B 83  ? 0.1522 0.1397 0.1370 -0.0204 -0.0101 0.0051  83  LEU   B O   
5140 C  CB  . LEU   B 83  ? 0.1571 0.1485 0.1422 -0.0174 -0.0248 -0.0066 83  LEU   B CB  
5141 C  CG  . LEU   B 83  ? 0.1790 0.1676 0.1543 -0.0229 -0.0094 -0.0076 83  LEU   B CG  
5142 C  CD1 . LEU   B 83  ? 0.1922 0.1696 0.1530 -0.0156 -0.0209 0.0023  83  LEU   B CD1 
5143 C  CD2 . LEU   B 83  ? 0.1949 0.1725 0.1723 -0.0080 -0.0125 -0.0254 83  LEU   B CD2 
5155 N  N   . SER   B 84  ? 0.1590 0.1436 0.1655 -0.0208 -0.0181 -0.0014 84  SER   B N   
5156 C  CA  . SER   B 84  ? 0.1568 0.1668 0.1582 -0.0249 -0.0152 0.0174  84  SER   B CA  
5157 C  C   . SER   B 84  ? 0.1560 0.1812 0.1194 -0.0188 -0.0150 0.0219  84  SER   B C   
5158 O  O   . SER   B 84  ? 0.1555 0.1643 0.1238 -0.0160 -0.0101 0.0037  84  SER   B O   
5159 C  CB  . SER   B 84  ? 0.1740 0.1689 0.2082 -0.0252 0.0059  0.0143  84  SER   B CB  
5160 O  OG  . SER   B 84  ? 0.1766 0.1853 0.2538 -0.0377 0.0141  0.0236  84  SER   B OG  
5166 N  N   . GLY   B 85  ? 0.1567 0.2000 0.1396 -0.0245 -0.0162 0.0259  85  GLY   B N   
5167 C  CA  . GLY   B 85  ? 0.1492 0.2069 0.1566 -0.0347 -0.0000 -0.0010 85  GLY   B CA  
5168 C  C   . GLY   B 85  ? 0.1501 0.1894 0.1438 -0.0397 -0.0023 0.0085  85  GLY   B C   
5169 O  O   . GLY   B 85  ? 0.1598 0.1839 0.1521 -0.0492 0.0124  -0.0060 85  GLY   B O   
5173 N  N   . HIS   B 86  ? 0.1486 0.1710 0.1585 -0.0306 -0.0158 0.0148  86  HIS   B N   
5174 C  CA  . HIS   B 86  ? 0.1522 0.1702 0.1604 -0.0285 -0.0209 0.0173  86  HIS   B CA  
5175 C  C   . HIS   B 86  ? 0.1449 0.1825 0.1518 -0.0407 -0.0110 0.0372  86  HIS   B C   
5176 O  O   . HIS   B 86  ? 0.1670 0.1916 0.1601 -0.0338 -0.0004 0.0370  86  HIS   B O   
5177 C  CB  . HIS   B 86  ? 0.1612 0.1674 0.1672 -0.0216 -0.0224 0.0055  86  HIS   B CB  
5178 C  CG  . HIS   B 86  ? 0.1701 0.1794 0.1594 -0.0193 -0.0182 0.0124  86  HIS   B CG  
5179 N  ND1 . HIS   B 86  ? 0.1711 0.2018 0.1789 -0.0261 -0.0256 -0.0044 86  HIS   B ND1 
5180 C  CD2 . HIS   B 86  ? 0.1684 0.1820 0.1674 -0.0103 -0.0289 0.0158  86  HIS   B CD2 
5181 C  CE1 . HIS   B 86  ? 0.1840 0.2015 0.1636 -0.0220 -0.0132 -0.0195 86  HIS   B CE1 
5182 N  NE2 . HIS   B 86  ? 0.1762 0.1954 0.1574 -0.0014 -0.0212 -0.0005 86  HIS   B NE2 
5190 N  N   . ASN   B 87  ? 0.1573 0.1822 0.1606 -0.0332 -0.0035 0.0282  87  ASN   B N   
5191 C  CA  . ASN   B 87  ? 0.1634 0.2000 0.1616 -0.0333 0.0149  0.0188  87  ASN   B CA  
5192 C  C   . ASN   B 87  ? 0.1779 0.1881 0.1484 -0.0326 0.0300  0.0141  87  ASN   B C   
5193 O  O   . ASN   B 87  ? 0.2023 0.2002 0.1838 -0.0275 0.0462  0.0099  87  ASN   B O   
5194 C  CB  . ASN   B 87  ? 0.1622 0.2365 0.1994 -0.0329 0.0221  0.0162  87  ASN   B CB  
5195 C  CG  . ASN   B 87  ? 0.1674 0.2588 0.2125 0.0022  0.0259  0.0354  87  ASN   B CG  
5196 O  OD1 . ASN   B 87  ? 0.1620 0.2463 0.2014 0.0052  0.0429  0.0502  87  ASN   B OD1 
5197 N  ND2 . ASN   B 87  ? 0.2068 0.2699 0.2491 0.0099  0.0332  0.0336  87  ASN   B ND2 
5204 N  N   . LEU   B 88  ? 0.1657 0.1768 0.1397 -0.0334 0.0140  0.0064  88  LEU   B N   
5205 C  CA  . LEU   B 88  ? 0.1695 0.1751 0.1460 -0.0336 0.0095  -0.0026 88  LEU   B CA  
5206 C  C   . LEU   B 88  ? 0.1683 0.1651 0.1467 -0.0350 0.0014  0.0009  88  LEU   B C   
5207 O  O   . LEU   B 88  ? 0.1958 0.1711 0.1761 -0.0236 -0.0297 -0.0080 88  LEU   B O   
5208 C  CB  . LEU   B 88  ? 0.1838 0.1719 0.1655 -0.0440 -0.0045 0.0090  88  LEU   B CB  
5209 C  CG  . LEU   B 88  ? 0.2249 0.2010 0.1880 -0.0376 -0.0272 0.0353  88  LEU   B CG  
5210 C  CD1 . LEU   B 88  ? 0.2398 0.2301 0.2150 -0.0479 -0.0208 0.0473  88  LEU   B CD1 
5211 C  CD2 . LEU   B 88  ? 0.2612 0.2283 0.2470 0.0041  -0.0554 0.0179  88  LEU   B CD2 
5223 N  N   . ALA   B 89  ? 0.1623 0.1592 0.1344 -0.0348 0.0160  0.0020  89  ALA   B N   
5224 C  CA  . ALA   B 89  ? 0.1656 0.1536 0.1268 -0.0372 0.0031  0.0095  89  ALA   B CA  
5225 C  C   . ALA   B 89  ? 0.1732 0.1537 0.1296 -0.0391 0.0142  0.0025  89  ALA   B C   
5226 O  O   . ALA   B 89  ? 0.1587 0.1600 0.1676 -0.0415 0.0141  -0.0233 89  ALA   B O   
5227 C  CB  . ALA   B 89  ? 0.1546 0.1493 0.1468 -0.0397 0.0069  0.0085  89  ALA   B CB  
5233 N  N   . LYS   B 90  ? 0.2009 0.1458 0.1398 -0.0433 -0.0049 0.0083  90  LYS   B N   
5234 C  CA  . LYS   B 90  ? 0.2141 0.1422 0.1337 -0.0433 -0.0085 0.0076  90  LYS   B CA  
5235 C  C   . LYS   B 90  ? 0.1990 0.1394 0.1498 -0.0445 -0.0089 -0.0033 90  LYS   B C   
5236 O  O   . LYS   B 90  ? 0.2110 0.1568 0.1663 -0.0614 0.0013  -0.0023 90  LYS   B O   
5237 C  CB  . LYS   B 90  ? 0.2366 0.1468 0.1734 -0.0368 0.0020  0.0189  90  LYS   B CB  
5238 C  CG  . LYS   B 90  ? 0.2408 0.1684 0.1739 -0.0244 0.0257  0.0182  90  LYS   B CG  
5239 C  CD  . LYS   B 90  ? 0.2762 0.1986 0.2297 -0.0164 0.0486  -0.0026 90  LYS   B CD  
5240 C  CE  . LYS   B 90  ? 0.2930 0.2185 0.2820 -0.0257 0.0616  -0.0060 90  LYS   B CE  
5241 N  NZ  . LYS   B 90  ? 0.3003 0.2113 0.2825 -0.0438 0.0846  -0.0066 90  LYS   B NZ  
5255 N  N   . HIS   B 91  ? 0.1694 0.1279 0.1329 -0.0362 -0.0140 0.0080  91  HIS   B N   
5256 C  CA  . HIS   B 91  ? 0.1642 0.1365 0.1450 -0.0235 -0.0151 0.0021  91  HIS   B CA  
5257 C  C   . HIS   B 91  ? 0.1544 0.1361 0.1234 -0.0244 -0.0032 0.0053  91  HIS   B C   
5258 O  O   . HIS   B 91  ? 0.1720 0.1389 0.1235 -0.0257 -0.0199 0.0033  91  HIS   B O   
5259 C  CB  . HIS   B 91  ? 0.1794 0.1389 0.1866 -0.0046 -0.0101 0.0142  91  HIS   B CB  
5260 C  CG  . HIS   B 91  ? 0.2237 0.1575 0.2568 0.0057  0.0217  0.0236  91  HIS   B CG  
5261 N  ND1 . HIS   B 91  ? 0.2527 0.1708 0.3175 0.0078  0.0291  0.0167  91  HIS   B ND1 
5262 C  CD2 . HIS   B 91  ? 0.2334 0.1830 0.3065 0.0200  0.0122  0.0513  91  HIS   B CD2 
5263 C  CE1 . HIS   B 91  ? 0.2559 0.1795 0.3312 0.0314  0.0329  0.0197  91  HIS   B CE1 
5264 N  NE2 . HIS   B 91  ? 0.2486 0.1928 0.3376 0.0335  0.0295  0.0591  91  HIS   B NE2 
5272 N  N   . CYS   B 92  ? 0.1442 0.1371 0.1287 -0.0270 -0.0137 0.0042  92  CYS   B N   
5273 C  CA  . CYS   B 92  ? 0.1492 0.1287 0.1258 -0.0227 -0.0030 0.0025  92  CYS   B CA  
5274 C  C   . CYS   B 92  ? 0.1464 0.1229 0.1153 -0.0156 -0.0001 -0.0029 92  CYS   B C   
5275 O  O   . CYS   B 92  ? 0.1506 0.1341 0.1380 -0.0175 -0.0056 -0.0017 92  CYS   B O   
5276 C  CB  . CYS   B 92  ? 0.1472 0.1377 0.1387 -0.0155 -0.0051 0.0031  92  CYS   B CB  
5277 S  SG  . CYS   B 92  ? 0.1461 0.1390 0.1426 -0.0112 -0.0121 0.0050  92  CYS   B SG  
5283 N  N   . LEU   B 93  ? 0.1382 0.1256 0.1178 -0.0170 -0.0074 -0.0030 93  LEU   B N   
5284 C  CA  . LEU   B 93  ? 0.1407 0.1305 0.1251 -0.0053 -0.0127 0.0025  93  LEU   B CA  
5285 C  C   . LEU   B 93  ? 0.1300 0.1265 0.1231 -0.0039 -0.0067 0.0055  93  LEU   B C   
5286 O  O   . LEU   B 93  ? 0.1364 0.1252 0.1391 -0.0055 -0.0074 0.0004  93  LEU   B O   
5287 C  CB  . LEU   B 93  ? 0.1446 0.1283 0.1474 -0.0042 -0.0104 -0.0011 93  LEU   B CB  
5288 C  CG  . LEU   B 93  ? 0.1376 0.1386 0.1659 -0.0057 -0.0054 0.0111  93  LEU   B CG  
5289 C  CD1 . LEU   B 93  ? 0.1342 0.1493 0.1673 0.0034  -0.0038 -0.0002 93  LEU   B CD1 
5290 C  CD2 . LEU   B 93  ? 0.1418 0.1483 0.1613 -0.0025 -0.0115 -0.0015 93  LEU   B CD2 
5302 N  N   . HIS   B 94  ? 0.1377 0.1173 0.1186 -0.0073 -0.0093 0.0097  94  HIS   B N   
5303 C  CA  . HIS   B 94  ? 0.1399 0.1238 0.1253 -0.0024 0.0016  0.0017  94  HIS   B CA  
5304 C  C   . HIS   B 94  ? 0.1350 0.1252 0.1478 -0.0105 -0.0017 0.0038  94  HIS   B C   
5305 O  O   . HIS   B 94  ? 0.1372 0.1361 0.1775 -0.0085 0.0163  -0.0098 94  HIS   B O   
5306 C  CB  . HIS   B 94  ? 0.1348 0.1347 0.1387 0.0021  -0.0061 0.0002  94  HIS   B CB  
5307 C  CG  . HIS   B 94  ? 0.1420 0.1266 0.1405 -0.0090 -0.0198 0.0026  94  HIS   B CG  
5308 N  ND1 . HIS   B 94  ? 0.1474 0.1313 0.1348 -0.0055 -0.0204 0.0043  94  HIS   B ND1 
5309 C  CD2 . HIS   B 94  ? 0.1463 0.1304 0.1419 -0.0028 -0.0121 0.0028  94  HIS   B CD2 
5310 C  CE1 . HIS   B 94  ? 0.1491 0.1312 0.1318 -0.0129 -0.0208 0.0052  94  HIS   B CE1 
5311 N  NE2 . HIS   B 94  ? 0.1413 0.1379 0.1428 -0.0168 -0.0096 0.0051  94  HIS   B NE2 
5319 N  N   . VAL   B 95  ? 0.1291 0.1270 0.1475 -0.0053 0.0030  0.0002  95  VAL   B N   
5320 C  CA  . VAL   B 95  ? 0.1352 0.1351 0.1358 -0.0046 0.0008  0.0099  95  VAL   B CA  
5321 C  C   . VAL   B 95  ? 0.1396 0.1363 0.1368 -0.0060 0.0057  0.0055  95  VAL   B C   
5322 O  O   . VAL   B 95  ? 0.1418 0.1320 0.1624 0.0045  0.0100  0.0160  95  VAL   B O   
5323 C  CB  . VAL   B 95  ? 0.1401 0.1327 0.1401 -0.0020 -0.0100 0.0047  95  VAL   B CB  
5324 C  CG1 . VAL   B 95  ? 0.1490 0.1472 0.1574 -0.0064 0.0029  0.0195  95  VAL   B CG1 
5325 C  CG2 . VAL   B 95  ? 0.1498 0.1346 0.1372 0.0074  -0.0086 -0.0016 95  VAL   B CG2 
5335 N  N   . VAL   B 96  ? 0.1491 0.1449 0.1397 0.0036  0.0079  0.0148  96  VAL   B N   
5336 C  CA  . VAL   B 96  ? 0.1575 0.1494 0.1306 0.0062  0.0073  0.0185  96  VAL   B CA  
5337 C  C   . VAL   B 96  ? 0.1586 0.1510 0.1508 0.0126  0.0109  0.0140  96  VAL   B C   
5338 O  O   . VAL   B 96  ? 0.1582 0.1583 0.1718 0.0103  0.0140  0.0048  96  VAL   B O   
5339 C  CB  . VAL   B 96  ? 0.1639 0.1684 0.1385 0.0090  0.0086  0.0155  96  VAL   B CB  
5340 C  CG1 . VAL   B 96  ? 0.1639 0.1873 0.1547 0.0237  0.0076  0.0055  96  VAL   B CG1 
5341 C  CG2 . VAL   B 96  ? 0.1745 0.1769 0.1522 0.0069  0.0131  0.0055  96  VAL   B CG2 
5351 N  N   . GLY   B 97  ? 0.1607 0.1511 0.1425 0.0065  0.0060  0.0181  97  GLY   B N   
5352 C  CA  . GLY   B 97  ? 0.1768 0.1569 0.1531 0.0027  0.0128  0.0207  97  GLY   B CA  
5353 C  C   . GLY   B 97  ? 0.1954 0.1633 0.1570 0.0057  0.0045  0.0185  97  GLY   B C   
5354 O  O   . GLY   B 97  ? 0.2053 0.1765 0.1557 0.0092  0.0010  0.0156  97  GLY   B O   
5358 N  N   . PRO   B 98  ? 0.2056 0.1675 0.1792 0.0072  0.0317  0.0328  98  PRO   B N   
5359 C  CA  . PRO   B 98  ? 0.2153 0.1799 0.1791 0.0125  0.0463  0.0237  98  PRO   B CA  
5360 C  C   . PRO   B 98  ? 0.2269 0.1823 0.1544 0.0279  0.0427  0.0401  98  PRO   B C   
5361 O  O   . PRO   B 98  ? 0.2208 0.1807 0.1817 0.0266  0.0418  0.0400  98  PRO   B O   
5362 C  CB  . PRO   B 98  ? 0.1974 0.1865 0.1952 0.0115  0.0537  0.0283  98  PRO   B CB  
5363 C  CG  . PRO   B 98  ? 0.1869 0.1839 0.1970 0.0073  0.0449  0.0400  98  PRO   B CG  
5364 C  CD  . PRO   B 98  ? 0.1860 0.1705 0.1912 0.0084  0.0374  0.0383  98  PRO   B CD  
5372 N  N   . ASN   B 99  ? 0.2411 0.1991 0.1568 0.0427  0.0379  0.0246  99  ASN   B N   
5373 C  CA  . ASN   B 99  ? 0.2566 0.2066 0.1648 0.0504  0.0296  0.0453  99  ASN   B CA  
5374 C  C   . ASN   B 99  ? 0.2822 0.2428 0.2039 0.0456  0.0477  0.0729  99  ASN   B C   
5375 O  O   . ASN   B 99  ? 0.2920 0.2490 0.2177 0.0479  0.0342  0.0737  99  ASN   B O   
5376 C  CB  . ASN   B 99  ? 0.2663 0.2091 0.1780 0.0491  0.0193  0.0342  99  ASN   B CB  
5377 C  CG  . ASN   B 99  ? 0.2695 0.2154 0.2013 0.0403  0.0016  0.0399  99  ASN   B CG  
5378 O  OD1 . ASN   B 99  ? 0.2749 0.2178 0.2242 0.0410  0.0070  0.0395  99  ASN   B OD1 
5379 N  ND2 . ASN   B 99  ? 0.2635 0.2137 0.2069 0.0410  -0.0247 0.0387  99  ASN   B ND2 
5386 N  N   A VAL   B 100 ? 0.2965 0.2555 0.2390 0.0339  0.0544  0.0908  100 VAL   B N   
5387 N  N   B VAL   B 100 ? 0.3032 0.2588 0.2425 0.0387  0.0416  0.0801  100 VAL   B N   
5388 C  CA  A VAL   B 100 ? 0.3237 0.2739 0.2983 0.0225  0.0550  0.1023  100 VAL   B CA  
5389 C  CA  B VAL   B 100 ? 0.3287 0.2755 0.2869 0.0310  0.0343  0.0855  100 VAL   B CA  
5390 C  C   A VAL   B 100 ? 0.3471 0.2800 0.2883 0.0291  0.0533  0.1200  100 VAL   B C   
5391 C  C   B VAL   B 100 ? 0.3485 0.2820 0.2887 0.0346  0.0336  0.1056  100 VAL   B C   
5392 O  O   A VAL   B 100 ? 0.3560 0.2894 0.2893 0.0254  0.0682  0.1170  100 VAL   B O   
5393 O  O   B VAL   B 100 ? 0.3531 0.2871 0.2886 0.0320  0.0370  0.1021  100 VAL   B O   
5394 C  CB  A VAL   B 100 ? 0.3318 0.2883 0.3734 -0.0007 0.0566  0.1096  100 VAL   B CB  
5395 C  CB  B VAL   B 100 ? 0.3351 0.2854 0.3305 0.0180  0.0294  0.0777  100 VAL   B CB  
5396 C  CG1 A VAL   B 100 ? 0.3366 0.2948 0.4019 -0.0041 0.0596  0.1074  100 VAL   B CG1 
5397 C  CG1 B VAL   B 100 ? 0.3382 0.2890 0.3465 0.0152  0.0291  0.0743  100 VAL   B CG1 
5398 C  CG2 A VAL   B 100 ? 0.3337 0.2917 0.3919 -0.0099 0.0623  0.1222  100 VAL   B CG2 
5399 C  CG2 B VAL   B 100 ? 0.3368 0.2884 0.3449 0.0134  0.0290  0.0772  100 VAL   B CG2 
5418 N  N   . ASN   B 101 ? 0.3627 0.2848 0.2923 0.0419  0.0308  0.1228  101 ASN   B N   
5419 C  CA  . ASN   B 101 ? 0.4014 0.3001 0.3115 0.0502  0.0078  0.1361  101 ASN   B CA  
5420 C  C   . ASN   B 101 ? 0.4406 0.3352 0.3187 0.0521  -0.0041 0.1489  101 ASN   B C   
5421 O  O   . ASN   B 101 ? 0.4462 0.3481 0.3512 0.0601  -0.0007 0.1205  101 ASN   B O   
5422 C  CB  . ASN   B 101 ? 0.4028 0.2879 0.3283 0.0466  0.0098  0.1179  101 ASN   B CB  
5423 C  CG  . ASN   B 101 ? 0.4027 0.2772 0.3387 0.0468  0.0108  0.1128  101 ASN   B CG  
5424 O  OD1 . ASN   B 101 ? 0.4084 0.2768 0.3654 0.0428  0.0255  0.1074  101 ASN   B OD1 
5425 N  ND2 . ASN   B 101 ? 0.3968 0.2705 0.3278 0.0494  0.0024  0.1051  101 ASN   B ND2 
5433 N  N   . LYS   B 102 ? 0.4720 0.3663 0.3375 0.0371  -0.0002 0.1478  102 LYS   B N   
5434 C  CA  . LYS   B 102 ? 0.5016 0.4071 0.3662 0.0191  0.0087  0.1211  102 LYS   B CA  
5435 C  C   . LYS   B 102 ? 0.4974 0.4087 0.3419 0.0188  0.0178  0.1243  102 LYS   B C   
5436 O  O   . LYS   B 102 ? 0.5080 0.4148 0.3555 0.0196  0.0021  0.1172  102 LYS   B O   
5437 C  CB  . LYS   B 102 ? 0.5313 0.4444 0.4361 0.0036  0.0191  0.0772  102 LYS   B CB  
5438 C  CG  . LYS   B 102 ? 0.5562 0.4756 0.5091 -0.0087 0.0302  0.0337  102 LYS   B CG  
5439 C  CD  . LYS   B 102 ? 0.5771 0.5007 0.5802 -0.0175 0.0415  -0.0008 102 LYS   B CD  
5440 C  CE  . LYS   B 102 ? 0.5917 0.5188 0.6371 -0.0247 0.0495  -0.0246 102 LYS   B CE  
5441 N  NZ  . LYS   B 102 ? 0.6001 0.5305 0.6700 -0.0281 0.0526  -0.0375 102 LYS   B NZ  
5455 N  N   . GLY   B 103 ? 0.4780 0.4002 0.3283 0.0158  0.0440  0.1257  103 GLY   B N   
5456 C  CA  . GLY   B 103 ? 0.4557 0.3926 0.3334 0.0159  0.0673  0.1035  103 GLY   B CA  
5457 C  C   . GLY   B 103 ? 0.4283 0.3779 0.3278 0.0112  0.0848  0.0799  103 GLY   B C   
5458 O  O   . GLY   B 103 ? 0.4348 0.3866 0.3258 0.0071  0.0928  0.0858  103 GLY   B O   
5462 N  N   A GLU   B 104 ? 0.4079 0.3610 0.3102 0.0119  0.1026  0.0638  104 GLU   B N   
5463 N  N   B GLU   B 104 ? 0.4120 0.3674 0.3294 0.0091  0.0714  0.0610  104 GLU   B N   
5464 C  CA  A GLU   B 104 ? 0.3870 0.3453 0.2882 0.0159  0.1136  0.0503  104 GLU   B CA  
5465 C  CA  B GLU   B 104 ? 0.3947 0.3564 0.3245 0.0074  0.0583  0.0415  104 GLU   B CA  
5466 C  C   A GLU   B 104 ? 0.3923 0.3515 0.3065 0.0022  0.1412  0.0542  104 GLU   B C   
5467 C  C   B GLU   B 104 ? 0.3896 0.3550 0.3359 0.0022  0.0629  0.0342  104 GLU   B C   
5468 O  O   A GLU   B 104 ? 0.3939 0.3534 0.3331 0.0005  0.1401  0.0511  104 GLU   B O   
5469 O  O   B GLU   B 104 ? 0.3901 0.3553 0.3441 0.0016  0.0626  0.0311  104 GLU   B O   
5470 C  CB  A GLU   B 104 ? 0.3678 0.3225 0.2741 0.0346  0.0794  0.0180  104 GLU   B CB  
5471 C  CB  B GLU   B 104 ? 0.3845 0.3459 0.3116 0.0105  0.0396  0.0250  104 GLU   B CB  
5472 C  CG  A GLU   B 104 ? 0.3529 0.3060 0.2570 0.0506  0.0353  -0.0146 104 GLU   B CG  
5473 C  CG  B GLU   B 104 ? 0.3763 0.3375 0.2999 0.0129  0.0195  0.0082  104 GLU   B CG  
5474 C  CD  A GLU   B 104 ? 0.3389 0.2898 0.2303 0.0634  -0.0001 -0.0279 104 GLU   B CD  
5475 C  CD  B GLU   B 104 ? 0.3700 0.3300 0.2885 0.0141  0.0040  -0.0023 104 GLU   B CD  
5476 O  OE1 A GLU   B 104 ? 0.3196 0.2740 0.1896 0.0729  0.0027  -0.0194 104 GLU   B OE1 
5477 O  OE1 B GLU   B 104 ? 0.3651 0.3249 0.2767 0.0130  0.0046  -0.0026 104 GLU   B OE1 
5478 O  OE2 A GLU   B 104 ? 0.3443 0.2947 0.2340 0.0623  -0.0311 -0.0399 104 GLU   B OE2 
5479 O  OE2 B GLU   B 104 ? 0.3703 0.3301 0.2897 0.0155  -0.0080 -0.0090 104 GLU   B OE2 
5492 N  N   A ASP   B 105 ? 0.3911 0.3554 0.3030 -0.0087 0.1660  0.0620  105 ASP   B N   
5493 N  N   B ASP   B 105 ? 0.3826 0.3530 0.3354 -0.0023 0.0677  0.0310  105 ASP   B N   
5494 C  CA  A ASP   B 105 ? 0.3938 0.3574 0.3225 -0.0175 0.1845  0.0495  105 ASP   B CA  
5495 C  CA  B ASP   B 105 ? 0.3768 0.3503 0.3427 -0.0065 0.0706  0.0229  105 ASP   B CA  
5496 C  C   A ASP   B 105 ? 0.3781 0.3281 0.2935 -0.0297 0.1839  0.0418  105 ASP   B C   
5497 C  C   B ASP   B 105 ? 0.3694 0.3411 0.3275 -0.0097 0.0681  0.0150  105 ASP   B C   
5498 O  O   A ASP   B 105 ? 0.3656 0.3211 0.2790 -0.0274 0.1773  0.0402  105 ASP   B O   
5499 O  O   B ASP   B 105 ? 0.3686 0.3389 0.3180 -0.0096 0.0689  0.0149  105 ASP   B O   
5500 C  CB  A ASP   B 105 ? 0.4095 0.3861 0.4000 -0.0071 0.1872  0.0282  105 ASP   B CB  
5501 C  CB  B ASP   B 105 ? 0.3766 0.3553 0.3672 -0.0055 0.0743  0.0200  105 ASP   B CB  
5502 C  CG  A ASP   B 105 ? 0.4207 0.4082 0.4719 -0.0001 0.1937  0.0111  105 ASP   B CG  
5503 C  CG  B ASP   B 105 ? 0.3754 0.3575 0.3910 -0.0061 0.0794  0.0192  105 ASP   B CG  
5504 O  OD1 A ASP   B 105 ? 0.4193 0.4135 0.4806 -0.0066 0.2074  0.0151  105 ASP   B OD1 
5505 O  OD1 B ASP   B 105 ? 0.3740 0.3589 0.3953 -0.0090 0.0816  0.0193  105 ASP   B OD1 
5506 O  OD2 A ASP   B 105 ? 0.4283 0.4191 0.5131 0.0089  0.1844  -0.0029 105 ASP   B OD2 
5507 O  OD2 B ASP   B 105 ? 0.3732 0.3573 0.3966 -0.0069 0.0845  0.0209  105 ASP   B OD2 
5516 N  N   A ILE   B 106 ? 0.3716 0.3040 0.3051 -0.0377 0.1674  0.0399  106 ILE   B N   
5517 N  N   B ILE   B 106 ? 0.3624 0.3335 0.3215 -0.0103 0.0617  0.0092  106 ILE   B N   
5518 C  CA  A ILE   B 106 ? 0.3528 0.2766 0.3153 -0.0537 0.1730  0.0319  106 ILE   B CA  
5519 C  CA  B ILE   B 106 ? 0.3531 0.3265 0.3223 -0.0116 0.0602  0.0029  106 ILE   B CA  
5520 C  C   A ILE   B 106 ? 0.3206 0.2708 0.3118 -0.0453 0.1685  0.0076  106 ILE   B C   
5521 C  C   B ILE   B 106 ? 0.3373 0.3228 0.3190 -0.0077 0.0582  -0.0047 106 ILE   B C   
5522 O  O   A ILE   B 106 ? 0.3050 0.2501 0.3093 -0.0510 0.1651  -0.0095 106 ILE   B O   
5523 O  O   B ILE   B 106 ? 0.3335 0.3182 0.3141 -0.0097 0.0524  -0.0103 106 ILE   B O   
5524 C  CB  A ILE   B 106 ? 0.3749 0.2680 0.3478 -0.0660 0.1596  0.0349  106 ILE   B CB  
5525 C  CB  B ILE   B 106 ? 0.3604 0.3264 0.3297 -0.0158 0.0591  0.0035  106 ILE   B CB  
5526 C  CG1 A ILE   B 106 ? 0.3857 0.2682 0.3604 -0.0557 0.1509  0.0249  106 ILE   B CG1 
5527 C  CG1 B ILE   B 106 ? 0.3633 0.3255 0.3341 -0.0140 0.0571  0.0028  106 ILE   B CG1 
5528 C  CG2 A ILE   B 106 ? 0.3810 0.2703 0.3701 -0.0790 0.1568  0.0416  106 ILE   B CG2 
5529 C  CG2 B ILE   B 106 ? 0.3633 0.3293 0.3364 -0.0187 0.0590  0.0039  106 ILE   B CG2 
5530 C  CD1 A ILE   B 106 ? 0.3906 0.2694 0.3568 -0.0485 0.1505  0.0255  106 ILE   B CD1 
5531 C  CD1 B ILE   B 106 ? 0.3646 0.3249 0.3353 -0.0122 0.0568  0.0039  106 ILE   B CD1 
5554 N  N   A GLN   B 107 ? 0.3117 0.2922 0.3272 -0.0341 0.1531  0.0092  107 GLN   B N   
5555 N  N   B GLN   B 107 ? 0.3266 0.3250 0.3283 -0.0039 0.0595  -0.0040 107 GLN   B N   
5556 C  CA  A GLN   B 107 ? 0.2980 0.3105 0.3432 -0.0258 0.1393  0.0130  107 GLN   B CA  
5557 C  CA  B GLN   B 107 ? 0.3147 0.3248 0.3395 -0.0002 0.0620  0.0009  107 GLN   B CA  
5558 C  C   A GLN   B 107 ? 0.2705 0.2878 0.3108 -0.0124 0.1049  0.0046  107 GLN   B C   
5559 C  C   B GLN   B 107 ? 0.2842 0.2995 0.3049 0.0044  0.0688  0.0007  107 GLN   B C   
5560 O  O   A GLN   B 107 ? 0.2624 0.2873 0.3461 -0.0084 0.0771  -0.0121 107 GLN   B O   
5561 O  O   B GLN   B 107 ? 0.2836 0.3024 0.3166 0.0052  0.0583  -0.0059 107 GLN   B O   
5562 C  CB  A GLN   B 107 ? 0.3311 0.3543 0.4182 -0.0233 0.1179  0.0170  107 GLN   B CB  
5563 C  CB  B GLN   B 107 ? 0.3356 0.3491 0.3926 -0.0001 0.0516  0.0034  107 GLN   B CB  
5564 C  CG  A GLN   B 107 ? 0.3655 0.3932 0.4941 -0.0160 0.0811  0.0196  107 GLN   B CG  
5565 C  CG  B GLN   B 107 ? 0.3545 0.3701 0.4437 0.0017  0.0376  0.0063  107 GLN   B CG  
5566 C  CD  A GLN   B 107 ? 0.3920 0.4230 0.5535 -0.0123 0.0540  0.0229  107 GLN   B CD  
5567 C  CD  B GLN   B 107 ? 0.3688 0.3860 0.4850 0.0022  0.0266  0.0087  107 GLN   B CD  
5568 O  OE1 A GLN   B 107 ? 0.4010 0.4352 0.5754 -0.0090 0.0500  0.0207  107 GLN   B OE1 
5569 O  OE1 B GLN   B 107 ? 0.3733 0.3922 0.4990 0.0031  0.0253  0.0085  107 GLN   B OE1 
5570 N  NE2 A GLN   B 107 ? 0.4034 0.4324 0.5736 -0.0095 0.0425  0.0282  107 GLN   B NE2 
5571 N  NE2 B GLN   B 107 ? 0.3751 0.3911 0.5002 0.0032  0.0225  0.0107  107 GLN   B NE2 
5588 N  N   . LEU   B 108 ? 0.2539 0.2708 0.2694 0.0122  0.0830  0.0053  108 LEU   B N   
5589 C  CA  . LEU   B 108 ? 0.2318 0.2420 0.2296 0.0266  0.0641  0.0230  108 LEU   B CA  
5590 C  C   . LEU   B 108 ? 0.1952 0.2017 0.2158 0.0286  0.0421  0.0363  108 LEU   B C   
5591 O  O   . LEU   B 108 ? 0.1965 0.1929 0.2116 0.0265  0.0308  0.0370  108 LEU   B O   
5592 C  CB  . LEU   B 108 ? 0.2461 0.2582 0.2211 0.0235  0.0680  0.0309  108 LEU   B CB  
5593 C  CG  . LEU   B 108 ? 0.2670 0.2837 0.2283 0.0214  0.0627  0.0052  108 LEU   B CG  
5594 C  CD1 . LEU   B 108 ? 0.2774 0.2975 0.2167 0.0091  0.0637  0.0111  108 LEU   B CD1 
5595 C  CD2 . LEU   B 108 ? 0.2832 0.2960 0.2467 0.0312  0.0543  -0.0145 108 LEU   B CD2 
5608 N  N   . LEU   B 109 ? 0.1816 0.1839 0.2117 0.0196  0.0392  0.0189  109 LEU   B N   
5609 C  CA  . LEU   B 109 ? 0.1677 0.1594 0.2248 0.0133  0.0325  0.0290  109 LEU   B CA  
5610 C  C   . LEU   B 109 ? 0.1533 0.1464 0.2170 0.0026  0.0336  0.0203  109 LEU   B C   
5611 O  O   . LEU   B 109 ? 0.1493 0.1413 0.2183 0.0061  0.0301  0.0282  109 LEU   B O   
5612 C  CB  . LEU   B 109 ? 0.1717 0.1483 0.2395 0.0098  0.0304  0.0364  109 LEU   B CB  
5613 C  CG  . LEU   B 109 ? 0.1710 0.1430 0.2345 0.0044  0.0213  0.0294  109 LEU   B CG  
5614 C  CD1 . LEU   B 109 ? 0.1635 0.1523 0.2243 0.0121  0.0271  0.0297  109 LEU   B CD1 
5615 C  CD2 . LEU   B 109 ? 0.1831 0.1460 0.2505 0.0049  0.0136  0.0222  109 LEU   B CD2 
5627 N  N   . LYS   B 110 ? 0.1519 0.1441 0.2115 -0.0089 0.0297  0.0219  110 LYS   B N   
5628 C  CA  . LYS   B 110 ? 0.1478 0.1400 0.2047 -0.0058 0.0276  0.0174  110 LYS   B CA  
5629 C  C   . LYS   B 110 ? 0.1516 0.1428 0.1983 -0.0066 0.0285  0.0128  110 LYS   B C   
5630 O  O   . LYS   B 110 ? 0.1412 0.1443 0.1977 -0.0060 0.0249  0.0061  110 LYS   B O   
5631 C  CB  . LYS   B 110 ? 0.1500 0.1363 0.2340 -0.0073 0.0308  0.0154  110 LYS   B CB  
5632 C  CG  . LYS   B 110 ? 0.1531 0.1442 0.2510 -0.0109 0.0153  0.0160  110 LYS   B CG  
5633 C  CD  . LYS   B 110 ? 0.1580 0.1419 0.2491 -0.0091 0.0239  0.0128  110 LYS   B CD  
5634 C  CE  . LYS   B 110 ? 0.1540 0.1552 0.2721 -0.0028 0.0188  0.0065  110 LYS   B CE  
5635 N  NZ  . LYS   B 110 ? 0.1526 0.1697 0.2748 0.0005  0.0072  0.0016  110 LYS   B NZ  
5649 N  N   . SER   B 111 ? 0.1542 0.1424 0.2110 -0.0079 0.0335  0.0192  111 SER   B N   
5650 C  CA  . SER   B 111 ? 0.1585 0.1436 0.1990 -0.0034 0.0342  0.0175  111 SER   B CA  
5651 C  C   . SER   B 111 ? 0.1580 0.1361 0.1957 -0.0007 0.0164  0.0104  111 SER   B C   
5652 O  O   . SER   B 111 ? 0.1459 0.1395 0.2051 -0.0016 0.0090  0.0135  111 SER   B O   
5653 C  CB  . SER   B 111 ? 0.1673 0.1641 0.2129 0.0014  0.0416  0.0265  111 SER   B CB  
5654 O  OG  . SER   B 111 ? 0.1855 0.2031 0.2274 0.0077  0.0496  0.0272  111 SER   B OG  
5660 N  N   . ALA   B 112 ? 0.1422 0.1352 0.2134 0.0035  0.0230  0.0211  112 ALA   B N   
5661 C  CA  . ALA   B 112 ? 0.1436 0.1451 0.1876 0.0000  0.0036  0.0108  112 ALA   B CA  
5662 C  C   . ALA   B 112 ? 0.1298 0.1427 0.1746 -0.0020 0.0102  0.0106  112 ALA   B C   
5663 O  O   . ALA   B 112 ? 0.1315 0.1467 0.1885 -0.0046 0.0156  0.0010  112 ALA   B O   
5664 C  CB  . ALA   B 112 ? 0.1417 0.1522 0.1993 0.0045  0.0117  0.0168  112 ALA   B CB  
5670 N  N   . TYR   B 113 ? 0.1299 0.1295 0.1973 -0.0012 0.0146  0.0120  113 TYR   B N   
5671 C  CA  . TYR   B 113 ? 0.1272 0.1330 0.1897 -0.0071 0.0151  0.0043  113 TYR   B CA  
5672 C  C   . TYR   B 113 ? 0.1256 0.1221 0.1820 -0.0087 0.0136  0.0076  113 TYR   B C   
5673 O  O   . TYR   B 113 ? 0.1283 0.1207 0.1809 -0.0061 0.0094  0.0007  113 TYR   B O   
5674 C  CB  . TYR   B 113 ? 0.1323 0.1267 0.1950 -0.0026 0.0181  0.0108  113 TYR   B CB  
5675 C  CG  . TYR   B 113 ? 0.1417 0.1311 0.2042 -0.0060 0.0155  0.0160  113 TYR   B CG  
5676 C  CD1 . TYR   B 113 ? 0.1444 0.1358 0.2212 -0.0045 0.0197  0.0138  113 TYR   B CD1 
5677 C  CD2 . TYR   B 113 ? 0.1458 0.1314 0.2082 -0.0065 0.0079  0.0175  113 TYR   B CD2 
5678 C  CE1 . TYR   B 113 ? 0.1419 0.1428 0.2130 -0.0085 0.0212  0.0095  113 TYR   B CE1 
5679 C  CE2 . TYR   B 113 ? 0.1525 0.1247 0.2146 0.0002  0.0139  0.0242  113 TYR   B CE2 
5680 C  CZ  . TYR   B 113 ? 0.1418 0.1284 0.2204 0.0026  0.0134  0.0162  113 TYR   B CZ  
5681 O  OH  . TYR   B 113 ? 0.1506 0.1237 0.2456 0.0087  0.0250  0.0084  113 TYR   B OH  
5691 N  N   . GLU   B 114 ? 0.1231 0.1252 0.1877 -0.0009 0.0153  0.0052  114 GLU   B N   
5692 C  CA  . GLU   B 114 ? 0.1287 0.1211 0.1868 0.0086  0.0066  0.0013  114 GLU   B CA  
5693 C  C   . GLU   B 114 ? 0.1310 0.1254 0.1684 0.0007  -0.0007 0.0035  114 GLU   B C   
5694 O  O   . GLU   B 114 ? 0.1220 0.1340 0.1819 0.0045  0.0005  0.0116  114 GLU   B O   
5695 C  CB  . GLU   B 114 ? 0.1351 0.1254 0.1925 0.0008  0.0158  0.0025  114 GLU   B CB  
5696 C  CG  . GLU   B 114 ? 0.1416 0.1258 0.1822 -0.0057 0.0119  0.0060  114 GLU   B CG  
5697 C  CD  . GLU   B 114 ? 0.1388 0.1284 0.1988 -0.0099 0.0126  0.0062  114 GLU   B CD  
5698 O  OE1 . GLU   B 114 ? 0.1275 0.1473 0.2028 -0.0100 0.0169  0.0060  114 GLU   B OE1 
5699 O  OE2 . GLU   B 114 ? 0.1391 0.1487 0.2139 -0.0196 0.0176  0.0020  114 GLU   B OE2 
5706 N  N   . ASN   B 115 ? 0.1405 0.1145 0.1692 -0.0054 -0.0056 0.0062  115 ASN   B N   
5707 C  CA  . ASN   B 115 ? 0.1349 0.1263 0.1594 -0.0075 -0.0014 0.0057  115 ASN   B CA  
5708 C  C   . ASN   B 115 ? 0.1269 0.1258 0.1601 -0.0141 0.0005  0.0004  115 ASN   B C   
5709 O  O   . ASN   B 115 ? 0.1369 0.1293 0.1764 -0.0100 0.0023  0.0042  115 ASN   B O   
5710 C  CB  . ASN   B 115 ? 0.1468 0.1340 0.1695 -0.0083 0.0040  0.0073  115 ASN   B CB  
5711 C  CG  . ASN   B 115 ? 0.1567 0.1484 0.1776 0.0013  0.0043  0.0013  115 ASN   B CG  
5712 O  OD1 . ASN   B 115 ? 0.1963 0.1583 0.1903 0.0014  0.0138  -0.0091 115 ASN   B OD1 
5713 N  ND2 . ASN   B 115 ? 0.1480 0.1579 0.1688 -0.0061 0.0110  0.0116  115 ASN   B ND2 
5720 N  N   . PHE   B 116 ? 0.1298 0.1264 0.1492 -0.0045 0.0042  -0.0038 116 PHE   B N   
5721 C  CA  . PHE   B 116 ? 0.1300 0.1294 0.1606 -0.0118 -0.0081 -0.0020 116 PHE   B CA  
5722 C  C   . PHE   B 116 ? 0.1316 0.1137 0.1621 -0.0111 -0.0025 0.0035  116 PHE   B C   
5723 O  O   . PHE   B 116 ? 0.1343 0.1274 0.1696 -0.0013 -0.0013 0.0038  116 PHE   B O   
5724 C  CB  . PHE   B 116 ? 0.1311 0.1181 0.1655 -0.0061 -0.0125 0.0021  116 PHE   B CB  
5725 C  CG  . PHE   B 116 ? 0.1235 0.1253 0.1648 -0.0040 0.0046  0.0034  116 PHE   B CG  
5726 C  CD1 . PHE   B 116 ? 0.1332 0.1309 0.1870 -0.0022 0.0030  0.0048  116 PHE   B CD1 
5727 C  CD2 . PHE   B 116 ? 0.1352 0.1330 0.1639 -0.0051 0.0031  -0.0000 116 PHE   B CD2 
5728 C  CE1 . PHE   B 116 ? 0.1319 0.1362 0.1787 0.0009  -0.0080 0.0015  116 PHE   B CE1 
5729 C  CE2 . PHE   B 116 ? 0.1341 0.1317 0.1592 -0.0043 0.0002  0.0106  116 PHE   B CE2 
5730 C  CZ  . PHE   B 116 ? 0.1242 0.1392 0.1783 -0.0010 -0.0068 0.0048  116 PHE   B CZ  
5740 N  N   . ASN   B 117 ? 0.1311 0.1218 0.1767 -0.0038 -0.0069 0.0038  117 ASN   B N   
5741 C  CA  . ASN   B 117 ? 0.1393 0.1239 0.1752 -0.0013 -0.0076 -0.0005 117 ASN   B CA  
5742 C  C   . ASN   B 117 ? 0.1402 0.1146 0.1892 -0.0009 -0.0081 0.0034  117 ASN   B C   
5743 O  O   . ASN   B 117 ? 0.1503 0.1224 0.2260 -0.0070 -0.0302 0.0110  117 ASN   B O   
5744 C  CB  . ASN   B 117 ? 0.1367 0.1264 0.1765 -0.0063 -0.0059 -0.0012 117 ASN   B CB  
5745 C  CG  . ASN   B 117 ? 0.1318 0.1254 0.1901 -0.0007 -0.0012 -0.0063 117 ASN   B CG  
5746 O  OD1 . ASN   B 117 ? 0.1551 0.1310 0.2020 -0.0141 0.0086  -0.0047 117 ASN   B OD1 
5747 N  ND2 . ASN   B 117 ? 0.1334 0.1314 0.1887 0.0002  -0.0029 -0.0059 117 ASN   B ND2 
5754 N  N   . GLN   B 118 ? 0.1424 0.1180 0.1780 -0.0111 -0.0106 -0.0008 118 GLN   B N   
5755 C  CA  . GLN   B 118 ? 0.1434 0.1236 0.1883 -0.0036 -0.0080 -0.0009 118 GLN   B CA  
5756 C  C   . GLN   B 118 ? 0.1453 0.1267 0.1984 -0.0030 -0.0057 -0.0069 118 GLN   B C   
5757 O  O   . GLN   B 118 ? 0.1646 0.1225 0.2363 -0.0086 0.0052  0.0008  118 GLN   B O   
5758 C  CB  . GLN   B 118 ? 0.1516 0.1281 0.2040 0.0027  -0.0067 0.0014  118 GLN   B CB  
5759 C  CG  . GLN   B 118 ? 0.1583 0.1326 0.2023 0.0022  -0.0017 -0.0114 118 GLN   B CG  
5760 C  CD  . GLN   B 118 ? 0.1644 0.1256 0.2001 -0.0010 -0.0066 -0.0185 118 GLN   B CD  
5761 O  OE1 . GLN   B 118 ? 0.1688 0.1265 0.2173 -0.0006 0.0065  -0.0006 118 GLN   B OE1 
5762 N  NE2 . GLN   B 118 ? 0.1701 0.1222 0.2033 -0.0027 -0.0089 -0.0004 118 GLN   B NE2 
5771 N  N   . HIS   B 119 ? 0.1536 0.1317 0.1491 -0.0050 -0.0049 0.0033  119 HIS   B N   
5772 C  CA  . HIS   B 119 ? 0.1619 0.1407 0.1539 -0.0027 -0.0135 0.0063  119 HIS   B CA  
5773 C  C   . HIS   B 119 ? 0.1619 0.1356 0.1571 -0.0055 -0.0203 0.0075  119 HIS   B C   
5774 O  O   . HIS   B 119 ? 0.1622 0.1388 0.1797 -0.0248 -0.0176 0.0109  119 HIS   B O   
5775 C  CB  . HIS   B 119 ? 0.1627 0.1441 0.1719 0.0004  -0.0209 -0.0018 119 HIS   B CB  
5776 C  CG  . HIS   B 119 ? 0.1646 0.1709 0.1854 0.0102  -0.0318 -0.0207 119 HIS   B CG  
5777 N  ND1 . HIS   B 119 ? 0.1753 0.1846 0.2206 0.0075  -0.0383 -0.0386 119 HIS   B ND1 
5778 C  CD2 . HIS   B 119 ? 0.1800 0.1886 0.1926 0.0370  -0.0413 -0.0208 119 HIS   B CD2 
5779 C  CE1 . HIS   B 119 ? 0.2011 0.1991 0.2280 0.0222  -0.0472 -0.0485 119 HIS   B CE1 
5780 N  NE2 . HIS   B 119 ? 0.1995 0.2100 0.2106 0.0312  -0.0516 -0.0426 119 HIS   B NE2 
5788 N  N   . GLU   B 120 ? 0.1811 0.1372 0.1603 -0.0102 -0.0332 0.0119  120 GLU   B N   
5789 C  CA  . GLU   B 120 ? 0.2055 0.1551 0.1656 -0.0023 -0.0398 0.0256  120 GLU   B CA  
5790 C  C   . GLU   B 120 ? 0.1814 0.1436 0.1619 -0.0125 -0.0329 0.0208  120 GLU   B C   
5791 O  O   . GLU   B 120 ? 0.1714 0.1583 0.1623 -0.0130 -0.0280 0.0110  120 GLU   B O   
5792 C  CB  . GLU   B 120 ? 0.2738 0.1964 0.2493 0.0222  -0.0697 0.0528  120 GLU   B CB  
5793 C  CG  . GLU   B 120 ? 0.3386 0.2669 0.3559 0.0327  -0.0956 0.0728  120 GLU   B CG  
5794 C  CD  . GLU   B 120 ? 0.3886 0.3372 0.4700 0.0369  -0.1036 0.0791  120 GLU   B CD  
5795 O  OE1 . GLU   B 120 ? 0.4086 0.3619 0.5091 0.0323  -0.1000 0.0882  120 GLU   B OE1 
5796 O  OE2 . GLU   B 120 ? 0.4119 0.3690 0.5285 0.0383  -0.1012 0.0669  120 GLU   B OE2 
5803 N  N   . VAL   B 121 ? 0.1738 0.1367 0.1651 -0.0243 -0.0150 0.0175  121 VAL   B N   
5804 C  CA  . VAL   B 121 ? 0.1663 0.1532 0.1524 -0.0197 -0.0166 0.0116  121 VAL   B CA  
5805 C  C   . VAL   B 121 ? 0.1545 0.1505 0.1478 -0.0222 -0.0115 0.0131  121 VAL   B C   
5806 O  O   . VAL   B 121 ? 0.1602 0.1447 0.1710 -0.0286 -0.0240 0.0052  121 VAL   B O   
5807 C  CB  . VAL   B 121 ? 0.1871 0.1890 0.1587 -0.0038 -0.0231 0.0163  121 VAL   B CB  
5808 C  CG1 . VAL   B 121 ? 0.1916 0.2045 0.1922 -0.0116 -0.0151 0.0203  121 VAL   B CG1 
5809 C  CG2 . VAL   B 121 ? 0.2163 0.2148 0.1641 0.0066  -0.0156 0.0053  121 VAL   B CG2 
5819 N  N   . LEU   B 122 ? 0.1491 0.1459 0.1401 -0.0123 -0.0185 0.0093  122 LEU   B N   
5820 C  CA  . LEU   B 122 ? 0.1424 0.1539 0.1223 -0.0186 -0.0161 0.0082  122 LEU   B CA  
5821 C  C   . LEU   B 122 ? 0.1414 0.1397 0.1361 -0.0223 -0.0121 0.0087  122 LEU   B C   
5822 O  O   . LEU   B 122 ? 0.1477 0.1377 0.1736 -0.0303 -0.0211 -0.0003 122 LEU   B O   
5823 C  CB  . LEU   B 122 ? 0.1678 0.1585 0.1613 -0.0037 -0.0259 0.0054  122 LEU   B CB  
5824 C  CG  . LEU   B 122 ? 0.1547 0.1638 0.1692 -0.0182 -0.0069 0.0067  122 LEU   B CG  
5825 C  CD1 . LEU   B 122 ? 0.1613 0.1833 0.1876 -0.0250 -0.0112 0.0071  122 LEU   B CD1 
5826 C  CD2 . LEU   B 122 ? 0.1624 0.1612 0.1425 -0.0084 -0.0098 -0.0080 122 LEU   B CD2 
5838 N  N   . LEU   B 123 ? 0.1463 0.1268 0.1334 -0.0219 -0.0137 0.0094  123 LEU   B N   
5839 C  CA  . LEU   B 123 ? 0.1527 0.1293 0.1392 -0.0217 -0.0163 0.0008  123 LEU   B CA  
5840 C  C   . LEU   B 123 ? 0.1444 0.1292 0.1405 -0.0264 -0.0161 0.0026  123 LEU   B C   
5841 O  O   . LEU   B 123 ? 0.1564 0.1327 0.1323 -0.0327 -0.0144 0.0047  123 LEU   B O   
5842 C  CB  . LEU   B 123 ? 0.1538 0.1340 0.1502 -0.0240 -0.0088 -0.0037 123 LEU   B CB  
5843 C  CG  . LEU   B 123 ? 0.1497 0.1406 0.1605 -0.0163 -0.0044 0.0074  123 LEU   B CG  
5844 C  CD1 . LEU   B 123 ? 0.1653 0.1439 0.1727 -0.0177 0.0035  -0.0119 123 LEU   B CD1 
5845 C  CD2 . LEU   B 123 ? 0.1624 0.1482 0.1813 -0.0139 -0.0024 0.0182  123 LEU   B CD2 
5857 N  N   . ALA   B 124 ? 0.1381 0.1270 0.1438 -0.0252 -0.0084 0.0040  124 ALA   B N   
5858 C  CA  . ALA   B 124 ? 0.1325 0.1311 0.1487 -0.0170 -0.0094 -0.0023 124 ALA   B CA  
5859 C  C   . ALA   B 124 ? 0.1305 0.1278 0.1501 -0.0161 -0.0073 -0.0000 124 ALA   B C   
5860 O  O   . ALA   B 124 ? 0.1448 0.1278 0.1589 -0.0140 -0.0147 -0.0062 124 ALA   B O   
5861 C  CB  . ALA   B 124 ? 0.1337 0.1340 0.1561 -0.0039 0.0017  0.0012  124 ALA   B CB  
5867 N  N   . PRO   B 125 ? 0.1411 0.1272 0.1470 -0.0161 -0.0110 0.0109  125 PRO   B N   
5868 C  CA  . PRO   B 125 ? 0.1538 0.1320 0.1583 -0.0187 -0.0146 0.0210  125 PRO   B CA  
5869 C  C   . PRO   B 125 ? 0.1455 0.1229 0.1668 -0.0196 -0.0128 0.0097  125 PRO   B C   
5870 O  O   . PRO   B 125 ? 0.1423 0.1271 0.1963 -0.0122 -0.0034 0.0151  125 PRO   B O   
5871 C  CB  . PRO   B 125 ? 0.1590 0.1580 0.1678 -0.0255 -0.0227 0.0359  125 PRO   B CB  
5872 C  CG  . PRO   B 125 ? 0.1609 0.1604 0.1586 -0.0311 -0.0192 0.0202  125 PRO   B CG  
5873 C  CD  . PRO   B 125 ? 0.1521 0.1432 0.1485 -0.0324 -0.0074 0.0134  125 PRO   B CD  
5881 N  N   . LEU   B 126 ? 0.1556 0.1243 0.1875 -0.0187 0.0074  0.0142  126 LEU   B N   
5882 C  CA  . LEU   B 126 ? 0.1589 0.1298 0.1978 -0.0157 0.0204  0.0183  126 LEU   B CA  
5883 C  C   . LEU   B 126 ? 0.1563 0.1351 0.1940 -0.0019 0.0121  0.0233  126 LEU   B C   
5884 O  O   . LEU   B 126 ? 0.1757 0.1646 0.2168 0.0149  -0.0099 -0.0036 126 LEU   B O   
5885 C  CB  . LEU   B 126 ? 0.1741 0.1358 0.2246 -0.0162 0.0273  0.0096  126 LEU   B CB  
5886 C  CG  . LEU   B 126 ? 0.1947 0.1398 0.2352 -0.0250 0.0263  -0.0057 126 LEU   B CG  
5887 C  CD1 . LEU   B 126 ? 0.2095 0.1513 0.2851 -0.0268 0.0204  -0.0152 126 LEU   B CD1 
5888 C  CD2 . LEU   B 126 ? 0.1957 0.1567 0.2395 -0.0287 0.0130  -0.0117 126 LEU   B CD2 
5900 N  N   . LEU   B 127 ? 0.1519 0.1299 0.2012 -0.0005 0.0186  0.0124  127 LEU   B N   
5901 C  CA  . LEU   B 127 ? 0.1536 0.1432 0.2050 -0.0051 0.0267  0.0236  127 LEU   B CA  
5902 C  C   . LEU   B 127 ? 0.1413 0.1361 0.2079 -0.0017 0.0203  0.0240  127 LEU   B C   
5903 O  O   . LEU   B 127 ? 0.1456 0.1389 0.2135 -0.0139 0.0112  0.0191  127 LEU   B O   
5904 C  CB  . LEU   B 127 ? 0.1661 0.1382 0.2100 0.0001  0.0253  0.0184  127 LEU   B CB  
5905 C  CG  . LEU   B 127 ? 0.1773 0.1349 0.2335 -0.0006 0.0265  0.0161  127 LEU   B CG  
5906 C  CD1 . LEU   B 127 ? 0.1826 0.1395 0.2327 0.0040  0.0162  0.0078  127 LEU   B CD1 
5907 C  CD2 . LEU   B 127 ? 0.1816 0.1456 0.2514 -0.0162 0.0217  0.0321  127 LEU   B CD2 
5919 N  N   . SER   B 128 ? 0.1462 0.1380 0.2146 0.0054  0.0023  0.0129  128 SER   B N   
5920 C  CA  . SER   B 128 ? 0.1635 0.1464 0.2087 0.0092  -0.0057 0.0199  128 SER   B CA  
5921 C  C   . SER   B 128 ? 0.1758 0.1461 0.2296 0.0106  -0.0210 0.0170  128 SER   B C   
5922 O  O   . SER   B 128 ? 0.1973 0.1474 0.2626 0.0078  -0.0175 0.0297  128 SER   B O   
5923 C  CB  . SER   B 128 ? 0.1719 0.1458 0.2058 0.0080  0.0000  0.0304  128 SER   B CB  
5924 O  OG  . SER   B 128 ? 0.1762 0.1650 0.2120 0.0133  0.0131  0.0342  128 SER   B OG  
5930 N  N   . ALA   B 129 ? 0.1910 0.1560 0.2516 0.0273  -0.0173 0.0008  129 ALA   B N   
5931 C  CA  . ALA   B 129 ? 0.2037 0.1631 0.2634 0.0342  -0.0142 -0.0075 129 ALA   B CA  
5932 C  C   . ALA   B 129 ? 0.1890 0.1619 0.2472 0.0212  0.0046  -0.0026 129 ALA   B C   
5933 O  O   . ALA   B 129 ? 0.1773 0.1611 0.2475 0.0213  -0.0058 0.0029  129 ALA   B O   
5934 C  CB  . ALA   B 129 ? 0.2298 0.1829 0.2945 0.0307  -0.0080 -0.0155 129 ALA   B CB  
5940 N  N   . GLY   B 130 ? 0.1901 0.1547 0.2491 0.0282  0.0033  -0.0102 130 GLY   B N   
5941 C  CA  . GLY   B 130 ? 0.1937 0.1657 0.2527 0.0231  0.0259  -0.0073 130 GLY   B CA  
5942 C  C   . GLY   B 130 ? 0.1962 0.1676 0.2545 0.0171  0.0161  0.0090  130 GLY   B C   
5943 O  O   . GLY   B 130 ? 0.2123 0.1790 0.2592 0.0190  0.0194  0.0202  130 GLY   B O   
5947 N  N   . ILE   B 131 ? 0.1868 0.1798 0.2636 0.0325  0.0130  0.0050  131 ILE   B N   
5948 C  CA  . ILE   B 131 ? 0.2128 0.1897 0.2646 0.0288  0.0027  0.0188  131 ILE   B CA  
5949 C  C   . ILE   B 131 ? 0.2221 0.1774 0.2342 0.0191  0.0010  0.0234  131 ILE   B C   
5950 O  O   . ILE   B 131 ? 0.2505 0.1900 0.2481 0.0183  -0.0181 0.0237  131 ILE   B O   
5951 C  CB  . ILE   B 131 ? 0.2168 0.2205 0.3085 0.0307  -0.0056 0.0283  131 ILE   B CB  
5952 C  CG1 . ILE   B 131 ? 0.2199 0.2380 0.3259 0.0073  -0.0016 0.0347  131 ILE   B CG1 
5953 C  CG2 . ILE   B 131 ? 0.2251 0.2368 0.3322 0.0358  0.0039  0.0247  131 ILE   B CG2 
5954 C  CD1 . ILE   B 131 ? 0.2305 0.2526 0.3403 -0.0097 -0.0082 0.0431  131 ILE   B CD1 
5966 N  N   . PHE   B 132 ? 0.2039 0.1641 0.2258 0.0149  0.0152  0.0235  132 PHE   B N   
5967 C  CA  . PHE   B 132 ? 0.2097 0.1671 0.2220 0.0064  0.0331  0.0177  132 PHE   B CA  
5968 C  C   . PHE   B 132 ? 0.2322 0.1835 0.2410 0.0101  0.0380  0.0190  132 PHE   B C   
5969 O  O   . PHE   B 132 ? 0.2528 0.2048 0.2584 0.0052  0.0525  0.0223  132 PHE   B O   
5970 C  CB  . PHE   B 132 ? 0.1905 0.1648 0.2042 0.0111  0.0327  0.0220  132 PHE   B CB  
5971 C  CG  . PHE   B 132 ? 0.1915 0.1729 0.2030 0.0128  0.0250  0.0203  132 PHE   B CG  
5972 C  CD1 . PHE   B 132 ? 0.1981 0.1701 0.2373 0.0089  0.0240  0.0267  132 PHE   B CD1 
5973 C  CD2 . PHE   B 132 ? 0.1928 0.1732 0.1800 0.0249  0.0230  0.0267  132 PHE   B CD2 
5974 C  CE1 . PHE   B 132 ? 0.2048 0.1722 0.2583 0.0088  0.0158  0.0291  132 PHE   B CE1 
5975 C  CE2 . PHE   B 132 ? 0.2040 0.1816 0.1994 0.0213  0.0164  0.0222  132 PHE   B CE2 
5976 C  CZ  . PHE   B 132 ? 0.2050 0.1769 0.2368 0.0091  -0.0013 0.0319  132 PHE   B CZ  
5986 N  N   . GLY   B 133 ? 0.2272 0.1775 0.2406 0.0078  0.0207  0.0442  133 GLY   B N   
5987 C  CA  . GLY   B 133 ? 0.2338 0.1913 0.2509 -0.0161 0.0302  0.0514  133 GLY   B CA  
5988 C  C   . GLY   B 133 ? 0.2400 0.1947 0.2540 -0.0274 0.0335  0.0546  133 GLY   B C   
5989 O  O   . GLY   B 133 ? 0.2579 0.2078 0.2920 -0.0362 0.0372  0.0656  133 GLY   B O   
5993 N  N   . ALA   B 134 ? 0.2237 0.1875 0.2405 -0.0304 0.0363  0.0349  134 ALA   B N   
5994 C  CA  . ALA   B 134 ? 0.2159 0.1895 0.2480 -0.0195 0.0429  0.0175  134 ALA   B CA  
5995 C  C   . ALA   B 134 ? 0.2187 0.1818 0.2526 -0.0086 0.0365  0.0306  134 ALA   B C   
5996 O  O   . ALA   B 134 ? 0.2262 0.1985 0.2661 0.0050  0.0276  0.0232  134 ALA   B O   
5997 C  CB  . ALA   B 134 ? 0.2143 0.1887 0.2685 -0.0125 0.0323  0.0073  134 ALA   B CB  
6003 N  N   . ASP   B 135 ? 0.2330 0.1696 0.2559 -0.0106 0.0230  0.0414  135 ASP   B N   
6004 C  CA  . ASP   B 135 ? 0.2488 0.1700 0.2728 -0.0098 0.0100  0.0370  135 ASP   B CA  
6005 C  C   . ASP   B 135 ? 0.2279 0.1630 0.2583 -0.0010 0.0033  0.0277  135 ASP   B C   
6006 O  O   . ASP   B 135 ? 0.2159 0.1554 0.2683 -0.0025 0.0090  0.0253  135 ASP   B O   
6007 C  CB  . ASP   B 135 ? 0.2753 0.1813 0.3040 -0.0314 0.0086  0.0447  135 ASP   B CB  
6008 C  CG  . ASP   B 135 ? 0.3029 0.1841 0.3432 -0.0512 0.0084  0.0411  135 ASP   B CG  
6009 O  OD1 . ASP   B 135 ? 0.3112 0.1675 0.3386 -0.0323 -0.0025 0.0349  135 ASP   B OD1 
6010 O  OD2 . ASP   B 135 ? 0.3291 0.2190 0.4008 -0.0687 0.0070  0.0183  135 ASP   B OD2 
6015 N  N   . PRO   B 136 ? 0.2237 0.1619 0.2684 0.0165  -0.0083 0.0209  136 PRO   B N   
6016 C  CA  . PRO   B 136 ? 0.2060 0.1509 0.2677 0.0113  -0.0068 0.0065  136 PRO   B CA  
6017 C  C   . PRO   B 136 ? 0.1893 0.1450 0.2686 0.0109  -0.0032 0.0126  136 PRO   B C   
6018 O  O   . PRO   B 136 ? 0.1709 0.1412 0.2642 0.0051  0.0064  0.0120  136 PRO   B O   
6019 C  CB  . PRO   B 136 ? 0.2098 0.1646 0.2837 0.0207  -0.0139 -0.0017 136 PRO   B CB  
6020 C  CG  . PRO   B 136 ? 0.2294 0.1749 0.3007 0.0257  -0.0063 0.0000  136 PRO   B CG  
6021 C  CD  . PRO   B 136 ? 0.2313 0.1756 0.2918 0.0363  -0.0026 0.0071  136 PRO   B CD  
6029 N  N   . ILE   B 137 ? 0.1983 0.1398 0.2812 0.0114  -0.0030 0.0048  137 ILE   B N   
6030 C  CA  . ILE   B 137 ? 0.2034 0.1321 0.2908 -0.0043 0.0008  0.0043  137 ILE   B CA  
6031 C  C   . ILE   B 137 ? 0.1931 0.1386 0.2821 -0.0115 0.0106  0.0125  137 ILE   B C   
6032 O  O   . ILE   B 137 ? 0.1837 0.1404 0.2752 -0.0117 0.0089  0.0053  137 ILE   B O   
6033 C  CB  . ILE   B 137 ? 0.2256 0.1382 0.3373 -0.0102 0.0003  0.0072  137 ILE   B CB  
6034 C  CG1 . ILE   B 137 ? 0.2474 0.1606 0.3868 -0.0005 0.0069  -0.0097 137 ILE   B CG1 
6035 C  CG2 . ILE   B 137 ? 0.2295 0.1431 0.3493 -0.0321 -0.0005 0.0172  137 ILE   B CG2 
6036 C  CD1 . ILE   B 137 ? 0.2685 0.1858 0.4290 0.0096  0.0075  -0.0058 137 ILE   B CD1 
6048 N  N   . HIS   B 138 ? 0.1980 0.1360 0.2834 -0.0091 0.0169  0.0207  138 HIS   B N   
6049 C  CA  . HIS   B 138 ? 0.2059 0.1444 0.2828 -0.0075 0.0282  0.0172  138 HIS   B CA  
6050 C  C   . HIS   B 138 ? 0.1891 0.1436 0.2673 -0.0102 0.0280  0.0221  138 HIS   B C   
6051 O  O   . HIS   B 138 ? 0.1796 0.1456 0.2818 -0.0019 0.0342  0.0335  138 HIS   B O   
6052 C  CB  . HIS   B 138 ? 0.2338 0.1593 0.2946 -0.0081 0.0411  0.0080  138 HIS   B CB  
6053 C  CG  . HIS   B 138 ? 0.2507 0.1724 0.2958 -0.0146 0.0529  0.0289  138 HIS   B CG  
6054 N  ND1 . HIS   B 138 ? 0.2553 0.1913 0.3218 -0.0080 0.0641  0.0153  138 HIS   B ND1 
6055 C  CD2 . HIS   B 138 ? 0.2643 0.1834 0.2886 -0.0128 0.0634  0.0238  138 HIS   B CD2 
6056 C  CE1 . HIS   B 138 ? 0.2600 0.1905 0.3116 -0.0113 0.0697  0.0178  138 HIS   B CE1 
6057 N  NE2 . HIS   B 138 ? 0.2662 0.1737 0.2958 -0.0053 0.0694  0.0152  138 HIS   B NE2 
6065 N  N   . SER   B 139 ? 0.1869 0.1354 0.2689 -0.0022 0.0251  0.0164  139 SER   B N   
6066 C  CA  . SER   B 139 ? 0.1795 0.1243 0.2458 -0.0062 0.0280  0.0072  139 SER   B CA  
6067 C  C   . SER   B 139 ? 0.1565 0.1268 0.2486 0.0048  0.0252  0.0105  139 SER   B C   
6068 O  O   . SER   B 139 ? 0.1601 0.1272 0.2434 0.0048  0.0089  0.0128  139 SER   B O   
6069 C  CB  . SER   B 139 ? 0.1890 0.1326 0.2499 0.0032  0.0134  0.0087  139 SER   B CB  
6070 O  OG  . SER   B 139 ? 0.1843 0.1297 0.2541 -0.0026 0.0002  0.0233  139 SER   B OG  
6076 N  N   . LEU   B 140 ? 0.1549 0.1196 0.2429 -0.0056 0.0219  0.0026  140 LEU   B N   
6077 C  CA  . LEU   B 140 ? 0.1561 0.1231 0.2470 -0.0031 0.0130  0.0045  140 LEU   B CA  
6078 C  C   . LEU   B 140 ? 0.1429 0.1256 0.2537 -0.0040 0.0029  -0.0025 140 LEU   B C   
6079 O  O   . LEU   B 140 ? 0.1481 0.1286 0.2466 -0.0034 -0.0008 0.0075  140 LEU   B O   
6080 C  CB  . LEU   B 140 ? 0.1513 0.1215 0.2536 -0.0110 0.0169  -0.0052 140 LEU   B CB  
6081 C  CG  . LEU   B 140 ? 0.1517 0.1298 0.2501 -0.0126 0.0108  0.0054  140 LEU   B CG  
6082 C  CD1 . LEU   B 140 ? 0.1569 0.1423 0.2649 -0.0086 0.0163  0.0086  140 LEU   B CD1 
6083 C  CD2 . LEU   B 140 ? 0.1743 0.1434 0.2625 -0.0058 0.0050  -0.0136 140 LEU   B CD2 
6095 N  N   . ARG   B 141 ? 0.1384 0.1238 0.2642 -0.0112 0.0063  -0.0030 141 ARG   B N   
6096 C  CA  . ARG   B 141 ? 0.1427 0.1249 0.2965 -0.0184 0.0223  -0.0043 141 ARG   B CA  
6097 C  C   . ARG   B 141 ? 0.1404 0.1253 0.2765 -0.0118 0.0125  -0.0008 141 ARG   B C   
6098 O  O   . ARG   B 141 ? 0.1483 0.1282 0.2802 -0.0167 0.0026  -0.0113 141 ARG   B O   
6099 C  CB  . ARG   B 141 ? 0.1592 0.1392 0.3275 -0.0170 0.0318  -0.0028 141 ARG   B CB  
6100 C  CG  . ARG   B 141 ? 0.1958 0.1620 0.3483 -0.0209 0.0377  -0.0004 141 ARG   B CG  
6101 C  CD  . ARG   B 141 ? 0.2415 0.1831 0.3467 -0.0128 0.0268  -0.0117 141 ARG   B CD  
6102 N  NE  . ARG   B 141 ? 0.2668 0.1855 0.3393 -0.0314 0.0315  -0.0172 141 ARG   B NE  
6103 C  CZ  . ARG   B 141 ? 0.2756 0.1809 0.3148 -0.0326 0.0400  -0.0289 141 ARG   B CZ  
6104 N  NH1 . ARG   B 141 ? 0.2867 0.1746 0.3023 -0.0306 0.0353  -0.0258 141 ARG   B NH1 
6105 N  NH2 . ARG   B 141 ? 0.2809 0.1931 0.3255 -0.0187 0.0230  -0.0275 141 ARG   B NH2 
6119 N  N   . VAL   B 142 ? 0.1464 0.1260 0.2656 -0.0117 0.0171  -0.0047 142 VAL   B N   
6120 C  CA  . VAL   B 142 ? 0.1408 0.1282 0.2521 -0.0092 0.0234  -0.0084 142 VAL   B CA  
6121 C  C   . VAL   B 142 ? 0.1411 0.1275 0.2500 -0.0067 0.0131  -0.0041 142 VAL   B C   
6122 O  O   . VAL   B 142 ? 0.1517 0.1221 0.2670 -0.0001 0.0179  -0.0028 142 VAL   B O   
6123 C  CB  . VAL   B 142 ? 0.1519 0.1428 0.2621 0.0008  0.0250  0.0081  142 VAL   B CB  
6124 C  CG1 . VAL   B 142 ? 0.1511 0.1413 0.2621 0.0114  0.0292  0.0045  142 VAL   B CG1 
6125 C  CG2 . VAL   B 142 ? 0.1699 0.1487 0.2708 0.0000  0.0197  0.0124  142 VAL   B CG2 
6135 N  N   . CYS   B 143 ? 0.1366 0.1302 0.2375 -0.0060 0.0093  0.0067  143 CYS   B N   
6136 C  CA  . CYS   B 143 ? 0.1341 0.1318 0.2423 -0.0083 0.0026  0.0015  143 CYS   B CA  
6137 C  C   . CYS   B 143 ? 0.1331 0.1281 0.2388 -0.0099 0.0042  -0.0050 143 CYS   B C   
6138 O  O   . CYS   B 143 ? 0.1406 0.1331 0.2459 -0.0094 0.0006  -0.0081 143 CYS   B O   
6139 C  CB  . CYS   B 143 ? 0.1369 0.1428 0.2409 -0.0061 -0.0020 0.0021  143 CYS   B CB  
6140 S  SG  . CYS   B 143 ? 0.1455 0.1495 0.2284 -0.0037 0.0058  0.0054  143 CYS   B SG  
6146 N  N   . VAL   B 144 ? 0.1427 0.1289 0.2475 -0.0106 0.0050  -0.0126 144 VAL   B N   
6147 C  CA  . VAL   B 144 ? 0.1433 0.1361 0.2692 -0.0127 -0.0045 -0.0183 144 VAL   B CA  
6148 C  C   . VAL   B 144 ? 0.1435 0.1355 0.2783 -0.0089 -0.0035 -0.0006 144 VAL   B C   
6149 O  O   . VAL   B 144 ? 0.1527 0.1541 0.3016 -0.0026 -0.0077 0.0168  144 VAL   B O   
6150 C  CB  . VAL   B 144 ? 0.1669 0.1557 0.3386 -0.0143 -0.0144 -0.0357 144 VAL   B CB  
6151 C  CG1 . VAL   B 144 ? 0.1877 0.1970 0.3638 -0.0167 -0.0184 -0.0367 144 VAL   B CG1 
6152 C  CG2 . VAL   B 144 ? 0.1765 0.1516 0.3328 -0.0020 -0.0258 -0.0362 144 VAL   B CG2 
6162 N  N   . ASP   B 145 ? 0.1445 0.1282 0.2793 -0.0098 -0.0018 -0.0188 145 ASP   B N   
6163 C  CA  . ASP   B 145 ? 0.1436 0.1408 0.3076 -0.0084 0.0069  -0.0122 145 ASP   B CA  
6164 C  C   . ASP   B 145 ? 0.1422 0.1355 0.2894 -0.0058 0.0143  -0.0119 145 ASP   B C   
6165 O  O   . ASP   B 145 ? 0.1437 0.1549 0.3414 -0.0132 0.0099  -0.0249 145 ASP   B O   
6166 C  CB  . ASP   B 145 ? 0.1489 0.1448 0.3460 -0.0153 0.0205  -0.0083 145 ASP   B CB  
6167 C  CG  . ASP   B 145 ? 0.1698 0.1503 0.3890 -0.0232 0.0350  -0.0079 145 ASP   B CG  
6168 O  OD1 . ASP   B 145 ? 0.1753 0.1544 0.3946 -0.0254 0.0048  -0.0199 145 ASP   B OD1 
6169 O  OD2 . ASP   B 145 ? 0.2045 0.1569 0.4341 -0.0334 0.0578  -0.0082 145 ASP   B OD2 
6174 N  N   . THR   B 146 ? 0.1310 0.1290 0.2497 -0.0165 0.0016  -0.0004 146 THR   B N   
6175 C  CA  . THR   B 146 ? 0.1352 0.1366 0.2285 -0.0085 0.0041  -0.0003 146 THR   B CA  
6176 C  C   . THR   B 146 ? 0.1383 0.1292 0.2238 -0.0009 -0.0026 0.0039  146 THR   B C   
6177 O  O   . THR   B 146 ? 0.1461 0.1314 0.2262 -0.0019 -0.0007 -0.0000 146 THR   B O   
6178 C  CB  . THR   B 146 ? 0.1446 0.1341 0.2347 -0.0068 0.0206  0.0024  146 THR   B CB  
6179 O  OG1 . THR   B 146 ? 0.1482 0.1335 0.2390 -0.0105 0.0165  0.0108  146 THR   B OG1 
6180 C  CG2 . THR   B 146 ? 0.1513 0.1340 0.2398 -0.0039 0.0183  0.0020  146 THR   B CG2 
6188 N  N   . VAL   B 147 ? 0.1463 0.1324 0.2096 -0.0030 0.0113  0.0060  147 VAL   B N   
6189 C  CA  . VAL   B 147 ? 0.1435 0.1285 0.2055 -0.0064 -0.0022 0.0034  147 VAL   B CA  
6190 C  C   . VAL   B 147 ? 0.1410 0.1298 0.2143 -0.0175 -0.0083 -0.0027 147 VAL   B C   
6191 O  O   . VAL   B 147 ? 0.1481 0.1458 0.2226 -0.0263 -0.0282 -0.0135 147 VAL   B O   
6192 C  CB  . VAL   B 147 ? 0.1467 0.1396 0.1965 -0.0043 -0.0043 0.0064  147 VAL   B CB  
6193 C  CG1 . VAL   B 147 ? 0.1474 0.1541 0.1753 -0.0137 -0.0044 0.0020  147 VAL   B CG1 
6194 C  CG2 . VAL   B 147 ? 0.1508 0.1391 0.2083 -0.0072 0.0004  0.0073  147 VAL   B CG2 
6204 N  N   . ARG   B 148 ? 0.1399 0.1297 0.2130 -0.0090 -0.0143 -0.0007 148 ARG   B N   
6205 C  CA  . ARG   B 148 ? 0.1468 0.1395 0.2080 -0.0070 -0.0182 -0.0083 148 ARG   B CA  
6206 C  C   . ARG   B 148 ? 0.1510 0.1456 0.1919 -0.0095 -0.0252 -0.0082 148 ARG   B C   
6207 O  O   . ARG   B 148 ? 0.1668 0.1787 0.1944 -0.0301 -0.0357 0.0011  148 ARG   B O   
6208 C  CB  . ARG   B 148 ? 0.1548 0.1432 0.2061 -0.0069 -0.0325 -0.0158 148 ARG   B CB  
6209 C  CG  . ARG   B 148 ? 0.1560 0.1618 0.2230 -0.0108 -0.0236 -0.0320 148 ARG   B CG  
6210 C  CD  . ARG   B 148 ? 0.1596 0.1776 0.2342 0.0039  -0.0204 -0.0336 148 ARG   B CD  
6211 N  NE  . ARG   B 148 ? 0.1586 0.1753 0.2278 0.0206  -0.0260 -0.0304 148 ARG   B NE  
6212 C  CZ  . ARG   B 148 ? 0.1521 0.1678 0.2117 0.0108  -0.0182 -0.0211 148 ARG   B CZ  
6213 N  NH1 . ARG   B 148 ? 0.1469 0.1730 0.2208 -0.0023 0.0019  -0.0171 148 ARG   B NH1 
6214 N  NH2 . ARG   B 148 ? 0.1752 0.1537 0.2010 0.0104  -0.0181 -0.0112 148 ARG   B NH2 
6228 N  N   . THR   B 149 ? 0.1540 0.1401 0.1921 -0.0124 -0.0221 -0.0017 149 THR   B N   
6229 C  CA  . THR   B 149 ? 0.1582 0.1439 0.1886 -0.0140 -0.0239 0.0049  149 THR   B CA  
6230 C  C   . THR   B 149 ? 0.1554 0.1444 0.1857 -0.0135 -0.0305 0.0044  149 THR   B C   
6231 O  O   . THR   B 149 ? 0.1633 0.1415 0.2014 -0.0165 -0.0109 0.0007  149 THR   B O   
6232 C  CB  . THR   B 149 ? 0.1597 0.1410 0.1833 -0.0143 -0.0232 0.0021  149 THR   B CB  
6233 O  OG1 . THR   B 149 ? 0.1600 0.1509 0.1799 -0.0232 -0.0258 -0.0044 149 THR   B OG1 
6234 C  CG2 . THR   B 149 ? 0.1687 0.1482 0.2049 -0.0065 -0.0172 -0.0012 149 THR   B CG2 
6242 N  N   . ASN   B 150 ? 0.1599 0.1396 0.1843 -0.0151 -0.0323 0.0021  150 ASN   B N   
6243 C  CA  . ASN   B 150 ? 0.1708 0.1605 0.1786 -0.0186 -0.0253 -0.0028 150 ASN   B CA  
6244 C  C   . ASN   B 150 ? 0.1611 0.1524 0.1684 -0.0135 -0.0219 -0.0038 150 ASN   B C   
6245 O  O   . ASN   B 150 ? 0.1679 0.1468 0.1891 -0.0283 -0.0359 0.0010  150 ASN   B O   
6246 C  CB  . ASN   B 150 ? 0.1908 0.1931 0.1922 -0.0210 -0.0387 0.0090  150 ASN   B CB  
6247 C  CG  . ASN   B 150 ? 0.2157 0.2325 0.2262 -0.0239 -0.0399 0.0274  150 ASN   B CG  
6248 O  OD1 . ASN   B 150 ? 0.2233 0.2504 0.2423 -0.0315 -0.0547 0.0264  150 ASN   B OD1 
6249 N  ND2 . ASN   B 150 ? 0.2308 0.2505 0.2596 -0.0166 -0.0459 0.0665  150 ASN   B ND2 
6256 N  N   . VAL   B 151 ? 0.1525 0.1535 0.1748 -0.0183 -0.0235 -0.0002 151 VAL   B N   
6257 C  CA  . VAL   B 151 ? 0.1551 0.1500 0.1717 -0.0239 -0.0168 -0.0073 151 VAL   B CA  
6258 C  C   . VAL   B 151 ? 0.1530 0.1377 0.1749 -0.0315 -0.0225 -0.0073 151 VAL   B C   
6259 O  O   . VAL   B 151 ? 0.1610 0.1454 0.1983 -0.0253 -0.0189 -0.0065 151 VAL   B O   
6260 C  CB  . VAL   B 151 ? 0.1707 0.1660 0.1941 -0.0078 -0.0153 -0.0074 151 VAL   B CB  
6261 C  CG1 . VAL   B 151 ? 0.1822 0.1768 0.2181 -0.0154 -0.0073 -0.0142 151 VAL   B CG1 
6262 C  CG2 . VAL   B 151 ? 0.1833 0.1776 0.1805 0.0103  -0.0162 0.0121  151 VAL   B CG2 
6272 N  N   . TYR   B 152 ? 0.1472 0.1349 0.1693 -0.0234 -0.0131 -0.0099 152 TYR   B N   
6273 C  CA  . TYR   B 152 ? 0.1514 0.1462 0.1586 -0.0260 -0.0141 -0.0123 152 TYR   B CA  
6274 C  C   . TYR   B 152 ? 0.1483 0.1332 0.1490 -0.0221 -0.0151 -0.0119 152 TYR   B C   
6275 O  O   . TYR   B 152 ? 0.1576 0.1395 0.1591 -0.0242 -0.0064 -0.0056 152 TYR   B O   
6276 C  CB  . TYR   B 152 ? 0.1653 0.1620 0.1635 -0.0258 -0.0081 0.0044  152 TYR   B CB  
6277 C  CG  . TYR   B 152 ? 0.1812 0.1677 0.1648 -0.0389 -0.0161 -0.0015 152 TYR   B CG  
6278 C  CD1 . TYR   B 152 ? 0.1885 0.1803 0.1508 -0.0284 -0.0273 -0.0019 152 TYR   B CD1 
6279 C  CD2 . TYR   B 152 ? 0.2042 0.1850 0.1688 -0.0359 -0.0107 -0.0080 152 TYR   B CD2 
6280 C  CE1 . TYR   B 152 ? 0.2062 0.1956 0.1751 -0.0242 -0.0313 0.0129  152 TYR   B CE1 
6281 C  CE2 . TYR   B 152 ? 0.2166 0.2086 0.1708 -0.0327 -0.0181 -0.0190 152 TYR   B CE2 
6282 C  CZ  . TYR   B 152 ? 0.2191 0.2208 0.1572 -0.0294 -0.0400 0.0135  152 TYR   B CZ  
6283 O  OH  . TYR   B 152 ? 0.2420 0.2540 0.1976 -0.0231 -0.0393 0.0150  152 TYR   B OH  
6293 N  N   . LEU   B 153 ? 0.1491 0.1289 0.1668 -0.0263 -0.0167 -0.0030 153 LEU   B N   
6294 C  CA  . LEU   B 153 ? 0.1625 0.1233 0.1649 -0.0238 -0.0085 -0.0132 153 LEU   B CA  
6295 C  C   . LEU   B 153 ? 0.1623 0.1274 0.1715 -0.0218 -0.0070 -0.0188 153 LEU   B C   
6296 O  O   . LEU   B 153 ? 0.1682 0.1484 0.1809 -0.0140 -0.0092 -0.0325 153 LEU   B O   
6297 C  CB  . LEU   B 153 ? 0.1589 0.1215 0.1712 -0.0244 -0.0040 -0.0099 153 LEU   B CB  
6298 C  CG  . LEU   B 153 ? 0.1558 0.1397 0.1988 -0.0243 -0.0055 -0.0110 153 LEU   B CG  
6299 C  CD1 . LEU   B 153 ? 0.1678 0.1553 0.2001 -0.0271 -0.0001 0.0035  153 LEU   B CD1 
6300 C  CD2 . LEU   B 153 ? 0.1584 0.1522 0.1974 -0.0277 0.0146  -0.0020 153 LEU   B CD2 
6312 N  N   . ALA   B 154 ? 0.1572 0.1304 0.1818 -0.0088 -0.0131 -0.0153 154 ALA   B N   
6313 C  CA  . ALA   B 154 ? 0.1661 0.1431 0.2009 -0.0003 -0.0170 -0.0184 154 ALA   B CA  
6314 C  C   . ALA   B 154 ? 0.1778 0.1510 0.2002 0.0065  -0.0217 -0.0269 154 ALA   B C   
6315 O  O   . ALA   B 154 ? 0.2048 0.1469 0.2149 0.0091  -0.0095 -0.0078 154 ALA   B O   
6316 C  CB  . ALA   B 154 ? 0.1670 0.1533 0.2295 -0.0073 -0.0154 -0.0256 154 ALA   B CB  
6322 N  N   . VAL   B 155 ? 0.1447 0.1401 0.2137 0.0029  0.0025  -0.0133 155 VAL   B N   
6323 C  CA  . VAL   B 155 ? 0.1467 0.1383 0.2209 0.0013  -0.0101 -0.0052 155 VAL   B CA  
6324 C  C   . VAL   B 155 ? 0.1461 0.1325 0.2197 -0.0029 -0.0125 -0.0109 155 VAL   B C   
6325 O  O   . VAL   B 155 ? 0.1600 0.1501 0.2591 0.0012  -0.0066 -0.0357 155 VAL   B O   
6326 C  CB  . VAL   B 155 ? 0.1516 0.1539 0.2506 -0.0044 -0.0242 0.0075  155 VAL   B CB  
6327 C  CG1 . VAL   B 155 ? 0.1525 0.1540 0.2469 -0.0110 -0.0154 0.0017  155 VAL   B CG1 
6328 C  CG2 . VAL   B 155 ? 0.1488 0.1625 0.2823 -0.0078 -0.0185 0.0368  155 VAL   B CG2 
6338 N  N   . PHE   B 156 ? 0.1405 0.1451 0.2363 0.0056  -0.0131 -0.0136 156 PHE   B N   
6339 C  CA  . PHE   B 156 ? 0.1389 0.1509 0.2732 0.0097  -0.0068 -0.0141 156 PHE   B CA  
6340 C  C   . PHE   B 156 ? 0.1348 0.1596 0.3082 0.0140  -0.0107 -0.0306 156 PHE   B C   
6341 O  O   . PHE   B 156 ? 0.1622 0.1797 0.3368 0.0234  -0.0040 -0.0358 156 PHE   B O   
6342 C  CB  . PHE   B 156 ? 0.1536 0.1481 0.2755 -0.0000 -0.0148 -0.0057 156 PHE   B CB  
6343 C  CG  . PHE   B 156 ? 0.1501 0.1563 0.2890 -0.0010 -0.0151 0.0101  156 PHE   B CG  
6344 C  CD1 . PHE   B 156 ? 0.1535 0.1793 0.3251 0.0019  -0.0087 0.0445  156 PHE   B CD1 
6345 C  CD2 . PHE   B 156 ? 0.1534 0.1710 0.2822 0.0051  -0.0197 0.0091  156 PHE   B CD2 
6346 C  CE1 . PHE   B 156 ? 0.1578 0.1980 0.3392 -0.0039 -0.0092 0.0416  156 PHE   B CE1 
6347 C  CE2 . PHE   B 156 ? 0.1607 0.1936 0.3146 0.0116  -0.0182 0.0132  156 PHE   B CE2 
6348 C  CZ  . PHE   B 156 ? 0.1495 0.2007 0.3339 0.0131  -0.0232 0.0235  156 PHE   B CZ  
6358 N  N   . ASP   B 157 ? 0.1425 0.1553 0.3173 0.0136  -0.0234 -0.0184 157 ASP   B N   
6359 C  CA  . ASP   B 157 ? 0.1538 0.1572 0.3563 0.0109  -0.0202 -0.0280 157 ASP   B CA  
6360 C  C   . ASP   B 157 ? 0.1579 0.1577 0.3669 0.0115  -0.0248 -0.0434 157 ASP   B C   
6361 O  O   . ASP   B 157 ? 0.1477 0.1641 0.3487 0.0051  -0.0220 -0.0383 157 ASP   B O   
6362 C  CB  . ASP   B 157 ? 0.1811 0.1779 0.3749 0.0051  -0.0379 -0.0158 157 ASP   B CB  
6363 C  CG  . ASP   B 157 ? 0.2159 0.1901 0.4027 0.0005  -0.0232 -0.0120 157 ASP   B CG  
6364 O  OD1 . ASP   B 157 ? 0.2227 0.1794 0.4179 0.0167  -0.0232 -0.0120 157 ASP   B OD1 
6365 O  OD2 . ASP   B 157 ? 0.2465 0.2101 0.4315 -0.0028 -0.0049 -0.0053 157 ASP   B OD2 
6370 N  N   . LYS   B 158 ? 0.1612 0.1817 0.3833 0.0105  -0.0107 -0.0706 158 LYS   B N   
6371 C  CA  . LYS   B 158 ? 0.1799 0.1990 0.3865 0.0061  -0.0044 -0.0868 158 LYS   B CA  
6372 C  C   . LYS   B 158 ? 0.1767 0.1866 0.3882 0.0096  -0.0105 -0.0798 158 LYS   B C   
6373 O  O   . LYS   B 158 ? 0.1770 0.1848 0.3928 0.0018  -0.0086 -0.0839 158 LYS   B O   
6374 C  CB  . LYS   B 158 ? 0.2075 0.2387 0.3844 0.0110  0.0115  -0.1109 158 LYS   B CB  
6375 C  CG  . LYS   B 158 ? 0.2387 0.2826 0.3898 0.0101  0.0187  -0.1149 158 LYS   B CG  
6376 C  CD  . LYS   B 158 ? 0.2615 0.3315 0.4012 0.0072  0.0256  -0.1085 158 LYS   B CD  
6377 C  CE  . LYS   B 158 ? 0.2827 0.3624 0.4143 0.0093  0.0255  -0.1041 158 LYS   B CE  
6378 N  NZ  . LYS   B 158 ? 0.2825 0.3775 0.4141 0.0048  0.0239  -0.1009 158 LYS   B NZ  
6392 N  N   . ASN   B 159 ? 0.1772 0.1729 0.4028 0.0043  -0.0225 -0.0641 159 ASN   B N   
6393 C  CA  . ASN   B 159 ? 0.1877 0.1673 0.4171 0.0157  -0.0359 -0.0490 159 ASN   B CA  
6394 C  C   . ASN   B 159 ? 0.1711 0.1495 0.4064 0.0109  -0.0514 -0.0384 159 ASN   B C   
6395 O  O   . ASN   B 159 ? 0.1718 0.1533 0.4154 -0.0001 -0.0525 -0.0269 159 ASN   B O   
6396 C  CB  . ASN   B 159 ? 0.2110 0.1818 0.4430 0.0268  -0.0363 -0.0475 159 ASN   B CB  
6397 C  CG  . ASN   B 159 ? 0.2409 0.2065 0.4768 0.0308  -0.0427 -0.0619 159 ASN   B CG  
6398 O  OD1 . ASN   B 159 ? 0.2581 0.2070 0.4793 0.0367  -0.0455 -0.0751 159 ASN   B OD1 
6399 N  ND2 . ASN   B 159 ? 0.2387 0.2196 0.4973 0.0375  -0.0452 -0.0511 159 ASN   B ND2 
6406 N  N   . LEU   B 160 ? 0.1640 0.1506 0.3829 0.0078  -0.0446 -0.0311 160 LEU   B N   
6407 C  CA  . LEU   B 160 ? 0.1629 0.1562 0.3392 0.0114  -0.0407 -0.0197 160 LEU   B CA  
6408 C  C   . LEU   B 160 ? 0.1567 0.1447 0.3281 0.0009  -0.0236 -0.0300 160 LEU   B C   
6409 O  O   . LEU   B 160 ? 0.1440 0.1509 0.3154 -0.0033 -0.0251 -0.0242 160 LEU   B O   
6410 C  CB  . LEU   B 160 ? 0.1652 0.1605 0.3219 0.0088  -0.0414 -0.0109 160 LEU   B CB  
6411 C  CG  . LEU   B 160 ? 0.1621 0.1745 0.3043 0.0123  -0.0337 -0.0070 160 LEU   B CG  
6412 C  CD1 . LEU   B 160 ? 0.1779 0.1911 0.3020 -0.0003 -0.0163 -0.0102 160 LEU   B CD1 
6413 C  CD2 . LEU   B 160 ? 0.1617 0.1808 0.2990 0.0289  -0.0341 -0.0230 160 LEU   B CD2 
6425 N  N   . TYR   B 161 ? 0.1481 0.1551 0.3323 -0.0050 -0.0022 -0.0422 161 TYR   B N   
6426 C  CA  . TYR   B 161 ? 0.1550 0.1511 0.3206 -0.0129 0.0124  -0.0532 161 TYR   B CA  
6427 C  C   . TYR   B 161 ? 0.1657 0.1562 0.3133 -0.0064 0.0159  -0.0450 161 TYR   B C   
6428 O  O   . TYR   B 161 ? 0.1742 0.1511 0.3041 -0.0183 -0.0033 -0.0356 161 TYR   B O   
6429 C  CB  . TYR   B 161 ? 0.1668 0.1642 0.3199 -0.0224 0.0240  -0.0556 161 TYR   B CB  
6430 C  CG  . TYR   B 161 ? 0.1913 0.1712 0.3152 -0.0311 0.0322  -0.0592 161 TYR   B CG  
6431 C  CD1 . TYR   B 161 ? 0.1999 0.1677 0.3171 -0.0408 0.0397  -0.0558 161 TYR   B CD1 
6432 C  CD2 . TYR   B 161 ? 0.2156 0.1829 0.3016 -0.0262 0.0254  -0.0630 161 TYR   B CD2 
6433 C  CE1 . TYR   B 161 ? 0.2206 0.1876 0.3168 -0.0458 0.0404  -0.0594 161 TYR   B CE1 
6434 C  CE2 . TYR   B 161 ? 0.2348 0.1981 0.3108 -0.0306 0.0294  -0.0625 161 TYR   B CE2 
6435 C  CZ  . TYR   B 161 ? 0.2360 0.2003 0.3119 -0.0471 0.0268  -0.0574 161 TYR   B CZ  
6436 O  OH  . TYR   B 161 ? 0.2632 0.2238 0.3332 -0.0494 0.0215  -0.0549 161 TYR   B OH  
6446 N  N   . ASP   B 162 ? 0.1690 0.1540 0.3298 -0.0080 -0.0013 -0.0620 162 ASP   B N   
6447 C  CA  . ASP   B 162 ? 0.1794 0.1659 0.3396 -0.0012 -0.0032 -0.0582 162 ASP   B CA  
6448 C  C   . ASP   B 162 ? 0.1745 0.1525 0.3348 -0.0132 -0.0028 -0.0482 162 ASP   B C   
6449 O  O   . ASP   B 162 ? 0.1817 0.1597 0.3309 -0.0161 -0.0125 -0.0361 162 ASP   B O   
6450 C  CB  . ASP   B 162 ? 0.1990 0.1813 0.3587 0.0044  -0.0070 -0.0795 162 ASP   B CB  
6451 C  CG  . ASP   B 162 ? 0.2025 0.2105 0.3824 0.0087  -0.0073 -0.0913 162 ASP   B CG  
6452 O  OD1 . ASP   B 162 ? 0.2016 0.2265 0.3824 0.0001  0.0041  -0.0884 162 ASP   B OD1 
6453 O  OD2 . ASP   B 162 ? 0.2191 0.2282 0.4099 0.0252  0.0032  -0.0857 162 ASP   B OD2 
6458 N  N   . LYS   B 163 ? 0.1669 0.1400 0.3283 -0.0153 -0.0198 -0.0290 163 LYS   B N   
6459 C  CA  . LYS   B 163 ? 0.1838 0.1488 0.3302 -0.0210 -0.0163 -0.0092 163 LYS   B CA  
6460 C  C   . LYS   B 163 ? 0.1545 0.1397 0.3116 -0.0252 -0.0151 -0.0035 163 LYS   B C   
6461 O  O   . LYS   B 163 ? 0.1561 0.1466 0.3389 -0.0220 -0.0191 0.0015  163 LYS   B O   
6462 C  CB  . LYS   B 163 ? 0.2327 0.1862 0.3638 -0.0192 -0.0260 0.0083  163 LYS   B CB  
6463 C  CG  . LYS   B 163 ? 0.3138 0.2699 0.4239 -0.0219 -0.0119 0.0169  163 LYS   B CG  
6464 C  CD  . LYS   B 163 ? 0.3783 0.3481 0.4915 -0.0323 -0.0086 0.0142  163 LYS   B CD  
6465 C  CE  . LYS   B 163 ? 0.4280 0.4016 0.5359 -0.0391 -0.0028 0.0159  163 LYS   B CE  
6466 N  NZ  . LYS   B 163 ? 0.4604 0.4437 0.5669 -0.0423 0.0005  0.0128  163 LYS   B NZ  
6480 N  N   . LEU   B 164 ? 0.1386 0.1399 0.2870 -0.0169 -0.0123 -0.0077 164 LEU   B N   
6481 C  CA  . LEU   B 164 ? 0.1505 0.1391 0.2578 -0.0111 -0.0191 -0.0027 164 LEU   B CA  
6482 C  C   . LEU   B 164 ? 0.1554 0.1402 0.2612 -0.0148 -0.0253 -0.0034 164 LEU   B C   
6483 O  O   . LEU   B 164 ? 0.1583 0.1599 0.2821 -0.0133 -0.0289 -0.0040 164 LEU   B O   
6484 C  CB  . LEU   B 164 ? 0.1439 0.1415 0.2452 -0.0112 -0.0203 -0.0078 164 LEU   B CB  
6485 C  CG  . LEU   B 164 ? 0.1570 0.1543 0.2608 -0.0093 -0.0123 -0.0012 164 LEU   B CG  
6486 C  CD1 . LEU   B 164 ? 0.1569 0.1524 0.2732 -0.0114 -0.0245 -0.0135 164 LEU   B CD1 
6487 C  CD2 . LEU   B 164 ? 0.1747 0.1880 0.2860 -0.0080 -0.0022 -0.0135 164 LEU   B CD2 
6499 N  N   . VAL   B 165 ? 0.1823 0.1481 0.2812 -0.0215 -0.0341 -0.0128 165 VAL   B N   
6500 C  CA  . VAL   B 165 ? 0.2146 0.1650 0.2917 -0.0344 -0.0559 -0.0118 165 VAL   B CA  
6501 C  C   . VAL   B 165 ? 0.2395 0.1794 0.3215 -0.0411 -0.0848 -0.0086 165 VAL   B C   
6502 O  O   . VAL   B 165 ? 0.2588 0.1948 0.3353 -0.0481 -0.0887 -0.0060 165 VAL   B O   
6503 C  CB  . VAL   B 165 ? 0.2393 0.1803 0.2994 -0.0218 -0.0216 -0.0202 165 VAL   B CB  
6504 C  CG1 . VAL   B 165 ? 0.2575 0.1886 0.3280 -0.0255 -0.0106 -0.0236 165 VAL   B CG1 
6505 C  CG2 . VAL   B 165 ? 0.2316 0.1843 0.2853 -0.0152 -0.0175 -0.0167 165 VAL   B CG2 
6515 N  N   . SER   B 166 ? 0.2514 0.1671 0.3503 -0.0375 -0.0879 -0.0263 166 SER   B N   
6516 C  CA  . SER   B 166 ? 0.2485 0.1626 0.4009 -0.0374 -0.0740 -0.0416 166 SER   B CA  
6517 C  C   . SER   B 166 ? 0.2315 0.1730 0.4186 -0.0365 -0.0696 -0.0125 166 SER   B C   
6518 O  O   . SER   B 166 ? 0.2329 0.1927 0.4444 -0.0488 -0.0806 -0.0389 166 SER   B O   
6519 C  CB  . SER   B 166 ? 0.2471 0.1774 0.4310 -0.0223 -0.0667 -0.0477 166 SER   B CB  
6520 O  OG  . SER   B 166 ? 0.2388 0.1722 0.4493 -0.0145 -0.0654 -0.0304 166 SER   B OG  
6526 N  N   . SER   B 167 ? 0.2100 0.1640 0.3914 -0.0444 -0.0712 0.0301  167 SER   B N   
6527 C  CA  . SER   B 167 ? 0.2007 0.1801 0.3748 -0.0355 -0.0492 0.0287  167 SER   B CA  
6528 C  C   . SER   B 167 ? 0.1957 0.1893 0.3514 -0.0493 -0.0449 0.0494  167 SER   B C   
6529 O  O   . SER   B 167 ? 0.2004 0.2005 0.3473 -0.0539 -0.0411 0.0433  167 SER   B O   
6530 C  CB  . SER   B 167 ? 0.1920 0.1829 0.3725 -0.0326 -0.0254 0.0245  167 SER   B CB  
6531 O  OG  . SER   B 167 ? 0.1900 0.1899 0.3590 -0.0290 -0.0133 0.0291  167 SER   B OG  
6537 N  N   . PHE   B 168 ? 0.1934 0.1855 0.3458 -0.0459 -0.0292 0.0576  168 PHE   B N   
6538 C  CA  . PHE   B 168 ? 0.2005 0.1797 0.3190 -0.0476 -0.0285 0.0328  168 PHE   B CA  
6539 C  C   . PHE   B 168 ? 0.1789 0.1620 0.2736 -0.0283 -0.0045 0.0200  168 PHE   B C   
6540 O  O   . PHE   B 168 ? 0.2055 0.1588 0.2760 -0.0023 -0.0108 -0.0048 168 PHE   B O   
6541 C  CB  . PHE   B 168 ? 0.2155 0.1853 0.3276 -0.0561 -0.0444 0.0449  168 PHE   B CB  
6542 C  CG  . PHE   B 168 ? 0.2433 0.1719 0.3127 -0.0521 -0.0492 0.0268  168 PHE   B CG  
6543 C  CD1 . PHE   B 168 ? 0.2717 0.1772 0.3188 -0.0401 -0.0604 0.0249  168 PHE   B CD1 
6544 C  CD2 . PHE   B 168 ? 0.2315 0.1639 0.3082 -0.0466 -0.0519 0.0276  168 PHE   B CD2 
6545 C  CE1 . PHE   B 168 ? 0.2833 0.1823 0.3226 -0.0299 -0.0493 0.0313  168 PHE   B CE1 
6546 C  CE2 . PHE   B 168 ? 0.2590 0.1683 0.3177 -0.0338 -0.0501 0.0256  168 PHE   B CE2 
6547 C  CZ  . PHE   B 168 ? 0.2711 0.1672 0.3189 -0.0208 -0.0581 0.0312  168 PHE   B CZ  
6557 N  N   . LEU   B 169 ? 0.1901 0.1771 0.2695 -0.0070 -0.0051 0.0050  169 LEU   B N   
6558 C  CA  . LEU   B 169 ? 0.2149 0.2042 0.2980 -0.0114 -0.0077 -0.0223 169 LEU   B CA  
6559 C  C   . LEU   B 169 ? 0.2472 0.2290 0.3483 0.0058  -0.0110 -0.0490 169 LEU   B C   
6560 O  O   . LEU   B 169 ? 0.2666 0.2523 0.3995 0.0079  -0.0082 -0.0649 169 LEU   B O   
6561 C  CB  . LEU   B 169 ? 0.2327 0.2469 0.3069 -0.0167 -0.0085 0.0006  169 LEU   B CB  
6562 C  CG  . LEU   B 169 ? 0.2745 0.2823 0.3439 -0.0018 -0.0033 0.0023  169 LEU   B CG  
6563 C  CD1 . LEU   B 169 ? 0.2893 0.3009 0.3494 -0.0008 -0.0065 0.0167  169 LEU   B CD1 
6564 C  CD2 . LEU   B 169 ? 0.2708 0.2891 0.3435 0.0132  0.0158  -0.0135 169 LEU   B CD2 
6565 O  OXT . LEU   B 169 ? 0.2659 0.2443 0.3443 0.0331  0.0016  -0.0551 169 LEU   B OXT 
6577 C  C1  T TFA   C .   ? 0.1278 0.1594 0.1032 -0.0219 0.0171  0.0118  201 TFA   A C1  
6578 C  C2  T TFA   C .   ? 0.1529 0.1840 0.1501 -0.0311 0.0119  -0.0033 201 TFA   A C2  
6579 O  O   T TFA   C .   ? 0.1042 0.1397 0.0923 -0.0185 0.0200  0.0199  201 TFA   A O   
6580 F  F1  T TFA   C .   ? 0.1675 0.1936 0.1858 -0.0272 0.0058  -0.0040 201 TFA   A F1  
6581 F  F2  T TFA   C .   ? 0.1674 0.1853 0.1444 -0.0298 0.0241  0.0050  201 TFA   A F2  
6582 F  F3  T TFA   C .   ? 0.1620 0.2047 0.1770 -0.0420 0.0230  -0.0187 201 TFA   A F3  
6583 O  OXT T TFA   C .   ? 0.1351 0.1583 0.1241 0.0106  0.0168  0.0213  201 TFA   A OXT 
6584 N  N2  B A1BAI D .   ? 0.1980 0.2274 0.1993 -0.0082 -0.0056 0.0094  202 A1BAI A N2  
6585 C  C3  B A1BAI D .   ? 0.2334 0.2404 0.2413 -0.0213 0.0080  -0.0067 202 A1BAI A C3  
6586 C  C6  B A1BAI D .   ? 0.1784 0.2180 0.1775 -0.0028 -0.0106 0.0256  202 A1BAI A C6  
6587 C  C9  B A1BAI D .   ? 0.1679 0.2162 0.1744 -0.0062 -0.0074 0.0336  202 A1BAI A C9  
6588 C  C1  B A1BAI D .   ? 0.2414 0.2428 0.2436 -0.0243 0.0137  -0.0148 202 A1BAI A C1  
6589 C  C10 B A1BAI D .   ? 0.2426 0.2453 0.2553 -0.0230 0.0100  -0.0094 202 A1BAI A C10 
6590 C  C11 B A1BAI D .   ? 0.2437 0.2465 0.2591 -0.0240 0.0107  -0.0102 202 A1BAI A C11 
6591 C  C2  B A1BAI D .   ? 0.2375 0.2415 0.2433 -0.0243 0.0114  -0.0122 202 A1BAI A C2  
6592 C  C4  B A1BAI D .   ? 0.2002 0.2293 0.2009 -0.0102 -0.0021 0.0089  202 A1BAI A C4  
6593 C  C5  B A1BAI D .   ? 0.1918 0.2243 0.1880 -0.0073 -0.0070 0.0183  202 A1BAI A C5  
6594 C  C7  B A1BAI D .   ? 0.1846 0.2238 0.1847 -0.0053 -0.0032 0.0186  202 A1BAI A C7  
6595 C  C8  B A1BAI D .   ? 0.1774 0.2227 0.1799 -0.0057 0.0003  0.0243  202 A1BAI A C8  
6596 N  N1  B A1BAI D .   ? 0.2201 0.2350 0.2237 -0.0158 0.0029  0.0025  202 A1BAI A N1  
6597 N  N3  B A1BAI D .   ? 0.1852 0.2210 0.1783 -0.0058 -0.0110 0.0239  202 A1BAI A N3  
6598 N  N4  B A1BAI D .   ? 0.1675 0.2110 0.1662 -0.0017 -0.0130 0.0378  202 A1BAI A N4  
6599 O  O1  B A1BAI D .   ? 0.2493 0.2486 0.2636 -0.0254 0.0112  -0.0088 202 A1BAI A O1  
6616 O  O1  C A1BAJ E .   ? 0.2489 0.2405 0.2464 -0.0202 0.0091  0.0020  203 A1BAJ A O1  
6617 C  C1  C A1BAJ E .   ? 0.2468 0.2409 0.2549 -0.0116 0.0052  0.0069  203 A1BAJ A C1  
6618 C  C2  C A1BAJ E .   ? 0.2428 0.2388 0.2494 -0.0125 0.0037  0.0060  203 A1BAJ A C2  
6619 C  C3  C A1BAJ E .   ? 0.2366 0.2359 0.2391 -0.0141 0.0042  0.0067  203 A1BAJ A C3  
6620 C  C4  C A1BAJ E .   ? 0.2062 0.2239 0.1979 -0.0069 0.0036  0.0159  203 A1BAJ A C4  
6621 C  C5  C A1BAJ E .   ? 0.1989 0.2182 0.1853 -0.0068 0.0013  0.0232  203 A1BAJ A C5  
6622 C  C6  C A1BAJ E .   ? 0.1883 0.2125 0.1756 -0.0033 -0.0017 0.0285  203 A1BAJ A C6  
6623 C  C7  C A1BAJ E .   ? 0.1935 0.2187 0.1824 -0.0042 0.0030  0.0231  203 A1BAJ A C7  
6624 C  C8  C A1BAJ E .   ? 0.1883 0.2190 0.1807 -0.0055 0.0054  0.0258  203 A1BAJ A C8  
6625 C  C10 C A1BAJ E .   ? 0.2438 0.2389 0.2434 -0.0189 0.0066  0.0029  203 A1BAJ A C10 
6626 C  C11 C A1BAJ E .   ? 0.2466 0.2399 0.2444 -0.0190 0.0080  0.0018  203 A1BAJ A C11 
6627 C  C9  C A1BAJ E .   ? 0.1798 0.2126 0.1753 -0.0062 0.0007  0.0335  203 A1BAJ A C9  
6628 N  N1  C A1BAJ E .   ? 0.2232 0.2299 0.2210 -0.0098 0.0038  0.0127  203 A1BAJ A N1  
6629 N  N2  C A1BAJ E .   ? 0.2037 0.2213 0.1954 -0.0066 0.0023  0.0159  203 A1BAJ A N2  
6630 N  N3  C A1BAJ E .   ? 0.1941 0.2150 0.1763 -0.0058 -0.0010 0.0281  203 A1BAJ A N3  
6631 N  N4  C A1BAJ E .   ? 0.1793 0.2061 0.1662 -0.0025 -0.0017 0.0377  203 A1BAJ A N4  
6648 CL CL  B CL    F .   ? 0.2185 0.1584 0.4048 -0.0206 -0.0378 -0.0303 204 CL    A CL  
6649 O  O   . HOH   G .   ? 0.2908 0.2473 0.3804 -0.0315 -0.0229 0.0594  301 HOH   A O   
6650 O  O   . HOH   G .   ? 0.6289 0.5936 0.5028 -0.0946 0.0169  0.2568  302 HOH   A O   
6651 O  O   . HOH   G .   ? 0.3014 0.2724 0.4201 -0.0304 -0.1206 0.1070  303 HOH   A O   
6652 O  O   . HOH   G .   ? 0.3912 0.7953 0.4608 -0.1159 0.0152  0.0976  304 HOH   A O   
6653 O  O   B HOH   G .   ? 0.1916 0.2905 0.3185 -0.0616 0.0541  0.0327  305 HOH   A O   
6654 O  O   . HOH   G .   ? 0.2320 0.2479 0.2370 -0.0254 0.0374  0.0477  306 HOH   A O   
6655 O  O   . HOH   G .   ? 0.6052 0.4293 0.3552 0.1345  -0.1264 0.0722  307 HOH   A O   
6656 O  O   . HOH   G .   ? 0.7593 0.5855 0.3903 -0.1444 -0.0398 0.1925  308 HOH   A O   
6657 O  O   . HOH   G .   ? 0.4761 0.3350 0.4758 -0.0348 0.1369  -0.0312 309 HOH   A O   
6658 O  O   . HOH   G .   ? 0.2818 0.6886 0.6093 -0.0361 -0.0759 0.1759  310 HOH   A O   
6659 O  O   . HOH   G .   ? 0.5798 0.3505 0.5464 -0.0526 0.1729  0.0923  311 HOH   A O   
6660 O  O   . HOH   G .   ? 0.1818 0.1759 0.2068 0.0138  -0.0255 0.0209  312 HOH   A O   
6661 O  O   B HOH   G .   ? 0.3394 0.4249 0.3162 0.0693  0.0351  0.0141  313 HOH   A O   
6662 O  O   . HOH   G .   ? 0.3114 0.3297 0.1626 -0.0346 0.0465  0.0391  314 HOH   A O   
6663 O  O   . HOH   G .   ? 0.2254 0.2148 0.3526 -0.0547 0.0104  -0.0368 315 HOH   A O   
6664 O  O   . HOH   G .   ? 0.6008 0.6106 0.5033 -0.1282 -0.1351 -0.1017 316 HOH   A O   
6665 O  O   . HOH   G .   ? 0.3457 0.3200 0.2789 -0.1265 0.0156  0.0717  317 HOH   A O   
6666 O  O   . HOH   G .   ? 0.6725 0.5456 0.3470 -0.0303 -0.0310 0.1168  318 HOH   A O   
6667 O  O   . HOH   G .   ? 0.4711 0.4163 0.4089 -0.2074 -0.1172 0.1903  319 HOH   A O   
6668 O  O   . HOH   G .   ? 0.3667 0.3818 0.4102 -0.0534 0.1773  0.0470  320 HOH   A O   
6669 O  O   . HOH   G .   ? 0.2643 0.5848 0.3756 -0.0094 -0.0574 0.0643  321 HOH   A O   
6670 O  O   . HOH   G .   ? 0.1845 0.3051 0.2972 0.0279  -0.0121 -0.0311 322 HOH   A O   
6671 O  O   . HOH   G .   ? 0.3098 0.3431 0.3644 -0.1262 0.0984  -0.0200 323 HOH   A O   
6672 O  O   . HOH   G .   ? 0.5892 0.4665 0.6638 0.0850  -0.0725 -0.0082 324 HOH   A O   
6673 O  O   . HOH   G .   ? 0.3750 0.3304 0.2522 -0.0552 -0.0351 0.0085  325 HOH   A O   
6674 O  O   . HOH   G .   ? 0.1675 0.1844 0.2577 0.0086  -0.0349 -0.0588 326 HOH   A O   
6675 O  O   . HOH   G .   ? 0.7255 0.6789 0.5543 -0.0529 0.0843  0.0982  327 HOH   A O   
6676 O  O   . HOH   G .   ? 0.4563 0.4942 0.5927 0.1621  0.1415  -0.0797 328 HOH   A O   
6677 O  O   A HOH   G .   ? 0.1501 0.2038 0.1728 0.0281  0.0348  0.0311  329 HOH   A O   
6678 O  O   . HOH   G .   ? 0.1942 0.3388 0.4376 -0.0442 0.0417  -0.1137 330 HOH   A O   
6679 O  O   . HOH   G .   ? 0.2783 0.3979 0.3768 -0.0955 -0.0554 -0.0477 331 HOH   A O   
6680 O  O   . HOH   G .   ? 0.2164 0.1702 0.1549 -0.0089 0.0207  0.0132  332 HOH   A O   
6681 O  O   . HOH   G .   ? 0.4699 0.3909 0.5446 0.0756  0.1447  -0.1435 333 HOH   A O   
6682 O  O   . HOH   G .   ? 0.2103 0.4735 0.4237 -0.0131 -0.0500 0.1785  334 HOH   A O   
6683 O  O   . HOH   G .   ? 0.1544 0.1574 0.2337 -0.0168 0.0113  0.0109  335 HOH   A O   
6684 O  O   . HOH   G .   ? 0.5237 0.4532 0.5074 0.0529  0.2103  -0.0492 336 HOH   A O   
6685 O  O   A HOH   G .   ? 0.2072 0.1495 0.2197 -0.0104 -0.0403 0.0056  337 HOH   A O   
6686 O  O   . HOH   G .   ? 0.5806 0.3623 0.3292 -0.1344 -0.1111 -0.0178 338 HOH   A O   
6687 O  O   . HOH   G .   ? 0.2362 0.2263 0.3057 0.0240  0.0264  0.0397  339 HOH   A O   
6688 O  O   . HOH   G .   ? 0.3414 0.4304 0.2507 -0.0317 0.0518  0.0191  340 HOH   A O   
6689 O  O   . HOH   G .   ? 0.4788 0.5138 0.2252 -0.1434 0.0745  0.0801  341 HOH   A O   
6690 O  O   . HOH   G .   ? 0.2641 0.5129 0.6229 0.0684  0.0550  0.0477  342 HOH   A O   
6691 O  O   A HOH   G .   ? 0.2191 0.3061 0.3901 0.0207  0.1172  0.1459  343 HOH   A O   
6692 O  O   . HOH   G .   ? 0.5019 0.4951 0.3870 -0.0424 0.0885  0.2045  344 HOH   A O   
6693 O  O   . HOH   G .   ? 0.4752 0.4024 0.3810 -0.0226 -0.0352 -0.0879 345 HOH   A O   
6694 O  O   . HOH   G .   ? 0.1586 0.4076 0.2495 -0.0035 0.0233  0.0570  346 HOH   A O   
6695 O  O   . HOH   G .   ? 0.3851 0.2131 0.4951 0.0278  -0.1551 0.0379  347 HOH   A O   
6696 O  O   . HOH   G .   ? 0.2639 0.3639 0.3919 0.0898  -0.0878 0.0075  348 HOH   A O   
6697 O  O   . HOH   G .   ? 0.5213 0.2815 0.3116 -0.1173 0.0334  0.0420  349 HOH   A O   
6698 O  O   . HOH   G .   ? 0.3530 0.2977 0.3576 -0.1070 -0.0170 -0.0120 350 HOH   A O   
6699 O  O   . HOH   G .   ? 0.1901 0.2155 0.3594 0.0177  0.0829  -0.0041 351 HOH   A O   
6700 O  O   . HOH   G .   ? 0.1571 0.2276 0.2175 -0.0008 -0.0048 0.0549  352 HOH   A O   
6701 O  O   . HOH   G .   ? 0.2645 0.2271 0.2418 -0.0326 0.0147  -0.0082 353 HOH   A O   
6702 O  O   A HOH   G .   ? 0.2019 0.2494 0.2356 0.0322  0.0248  0.0171  354 HOH   A O   
6703 O  O   . HOH   G .   ? 0.2261 0.1697 0.2380 0.0225  -0.0303 -0.0007 355 HOH   A O   
6704 O  O   . HOH   G .   ? 0.3259 0.3575 0.2333 -0.0870 -0.0235 -0.0709 356 HOH   A O   
6705 O  O   . HOH   G .   ? 0.1398 0.1366 0.1330 -0.0045 0.0119  0.0094  357 HOH   A O   
6706 O  O   . HOH   G .   ? 0.5167 0.2286 0.5034 0.0869  0.0016  0.0087  358 HOH   A O   
6707 O  O   . HOH   G .   ? 0.2986 0.3192 0.5021 -0.0463 -0.1127 -0.0784 359 HOH   A O   
6708 O  O   . HOH   G .   ? 0.1738 0.1771 0.1924 -0.0006 -0.0266 0.0065  360 HOH   A O   
6709 O  O   A HOH   G .   ? 0.3248 0.1688 0.1862 0.0149  0.0203  0.0034  361 HOH   A O   
6710 O  O   . HOH   G .   ? 0.3710 0.4110 0.3656 0.1807  0.0620  0.0377  362 HOH   A O   
6711 O  O   . HOH   G .   ? 0.2650 0.4051 0.3484 -0.0376 0.0644  -0.0107 363 HOH   A O   
6712 O  O   . HOH   G .   ? 0.5712 0.4046 0.3198 -0.0019 0.0124  0.1308  364 HOH   A O   
6713 O  O   . HOH   G .   ? 0.1497 0.1568 0.1492 -0.0059 -0.0114 -0.0090 365 HOH   A O   
6714 O  O   . HOH   G .   ? 0.1934 0.2112 0.2302 -0.0335 -0.0010 0.0330  366 HOH   A O   
6715 O  O   B HOH   G .   ? 0.3115 0.4333 0.1821 -0.0400 -0.0184 0.0063  367 HOH   A O   
6716 O  O   . HOH   G .   ? 0.1500 0.1946 0.2567 0.0023  -0.0060 0.0076  368 HOH   A O   
6717 O  O   . HOH   G .   ? 0.3824 0.2186 0.2461 0.1070  0.0565  0.0186  369 HOH   A O   
6718 O  O   A HOH   G .   ? 0.5746 0.2936 0.4696 0.0009  -0.1151 0.0477  370 HOH   A O   
6719 O  O   . HOH   G .   ? 0.2018 0.2031 0.1635 0.0094  0.0045  0.0128  371 HOH   A O   
6720 O  O   . HOH   G .   ? 0.1610 0.1393 0.2347 -0.0097 0.0242  -0.0147 372 HOH   A O   
6721 O  O   A HOH   G .   ? 0.2818 0.1849 0.2561 0.0563  0.0725  0.0256  373 HOH   A O   
6722 O  O   . HOH   G .   ? 0.2628 0.4190 0.3071 0.0552  0.0822  0.1649  374 HOH   A O   
6723 O  O   . HOH   G .   ? 0.4793 0.2686 0.4501 -0.1655 0.1624  -0.0606 375 HOH   A O   
6724 O  O   . HOH   G .   ? 0.3621 0.7147 0.4517 -0.0570 -0.1474 0.0791  376 HOH   A O   
6725 O  O   . HOH   G .   ? 0.1857 0.2495 0.2902 -0.0251 0.0671  0.0498  377 HOH   A O   
6726 O  O   . HOH   G .   ? 0.4116 0.2378 0.4331 -0.1165 0.0840  0.0297  378 HOH   A O   
6727 O  O   . HOH   G .   ? 0.2090 0.2193 0.3216 0.0047  -0.0484 0.0258  379 HOH   A O   
6728 O  O   . HOH   G .   ? 0.2159 0.2734 0.3293 0.0430  0.0884  -0.0444 380 HOH   A O   
6729 O  O   . HOH   G .   ? 0.2087 0.2382 0.2319 -0.0348 -0.0399 0.0501  381 HOH   A O   
6730 O  O   . HOH   G .   ? 0.3419 0.2375 0.5048 -0.0750 -0.0379 0.0249  382 HOH   A O   
6731 O  O   . HOH   G .   ? 0.1890 0.2743 0.2775 0.0468  0.0379  0.0933  383 HOH   A O   
6732 O  O   . HOH   G .   ? 0.5875 0.6172 0.3999 0.2231  -0.0313 -0.0124 384 HOH   A O   
6733 O  O   . HOH   G .   ? 0.1693 0.1787 0.2264 -0.0178 0.0032  0.0379  385 HOH   A O   
6734 O  O   . HOH   G .   ? 0.1803 0.2139 0.1856 -0.0144 0.0020  0.0533  386 HOH   A O   
6735 O  O   . HOH   G .   ? 0.3186 0.3048 0.3277 -0.0221 -0.0460 0.0993  387 HOH   A O   
6736 O  O   B HOH   G .   ? 0.2485 0.2718 0.2249 -0.0211 -0.0792 -0.0559 388 HOH   A O   
6737 O  O   . HOH   G .   ? 0.3159 0.2836 0.2231 0.0369  0.0804  0.0145  389 HOH   A O   
6738 O  O   . HOH   G .   ? 0.3427 0.6796 0.3470 0.1487  0.0706  -0.0943 390 HOH   A O   
6739 O  O   T HOH   G .   ? 0.0934 0.1086 0.2373 -0.0170 0.0287  0.0427  391 HOH   A O   
6740 O  O   . HOH   G .   ? 0.2620 0.2118 0.1801 -0.0652 0.0073  0.0350  392 HOH   A O   
6741 O  O   . HOH   G .   ? 0.3620 0.3435 0.2152 0.0117  -0.0837 0.0306  393 HOH   A O   
6742 O  O   . HOH   G .   ? 0.1490 0.1796 0.1763 0.0145  -0.0290 -0.0371 394 HOH   A O   
6743 O  O   . HOH   G .   ? 0.3662 0.5396 0.5427 0.0606  -0.0396 0.1662  395 HOH   A O   
6744 O  O   . HOH   G .   ? 0.2540 0.4177 0.3250 -0.0529 -0.0050 0.0762  396 HOH   A O   
6745 O  O   . HOH   G .   ? 0.2715 0.2770 0.3373 0.0034  -0.0454 -0.0707 397 HOH   A O   
6746 O  O   . HOH   G .   ? 0.1971 0.2269 0.2686 -0.0260 -0.0249 0.0870  398 HOH   A O   
6747 O  O   . HOH   G .   ? 0.2001 0.1958 0.3812 0.0403  0.1028  0.1110  399 HOH   A O   
6748 O  O   . HOH   G .   ? 0.5482 0.5628 0.5971 -0.0767 0.0425  0.1400  400 HOH   A O   
6749 O  O   . HOH   G .   ? 0.2680 0.3811 0.3762 -0.0400 0.0960  -0.0649 401 HOH   A O   
6750 O  O   . HOH   G .   ? 0.2496 0.1858 0.2657 -0.0043 0.0024  0.0242  402 HOH   A O   
6751 O  O   . HOH   G .   ? 0.1395 0.1486 0.1878 0.0007  -0.0198 0.0064  403 HOH   A O   
6752 O  O   . HOH   G .   ? 0.2067 0.2569 0.3809 -0.0112 -0.0207 0.0182  404 HOH   A O   
6753 O  O   . HOH   G .   ? 0.3975 0.6302 0.3791 -0.0653 0.0329  0.1163  405 HOH   A O   
6754 O  O   . HOH   G .   ? 0.5758 0.3195 0.5143 0.0957  0.0032  0.0074  406 HOH   A O   
6755 O  O   . HOH   G .   ? 0.3366 0.3973 0.3955 -0.0885 0.1549  0.0139  407 HOH   A O   
6756 O  O   A HOH   G .   ? 0.1863 0.1822 0.2878 -0.0080 0.0332  -0.0104 408 HOH   A O   
6757 O  O   . HOH   G .   ? 0.3024 0.2742 0.2120 -0.0645 -0.0765 0.0202  409 HOH   A O   
6758 O  O   . HOH   G .   ? 0.3994 0.6531 0.5327 0.2154  0.1019  0.0632  410 HOH   A O   
6759 O  O   B HOH   G .   ? 0.4179 0.2626 0.3500 0.0474  0.0035  -0.0277 411 HOH   A O   
6760 O  O   . HOH   G .   ? 0.4595 0.4443 0.2097 -0.0084 0.0783  0.0794  412 HOH   A O   
6761 O  O   . HOH   G .   ? 0.3094 0.3728 0.7044 -0.0059 0.1137  -0.0491 413 HOH   A O   
6762 O  O   . HOH   G .   ? 0.2233 0.1778 0.3046 0.0027  -0.0249 0.0168  414 HOH   A O   
6763 O  O   . HOH   G .   ? 0.1722 0.1412 0.1614 -0.0208 0.0115  0.0003  415 HOH   A O   
6764 O  O   . HOH   G .   ? 0.2054 0.1878 0.2669 0.0207  -0.0494 0.0200  416 HOH   A O   
6765 O  O   . HOH   G .   ? 0.1584 0.1677 0.3031 -0.0022 0.0087  0.0216  417 HOH   A O   
6766 O  O   . HOH   G .   ? 0.2512 0.2002 0.2691 -0.0477 -0.0033 0.0544  418 HOH   A O   
6767 O  O   . HOH   G .   ? 0.6259 0.5779 0.5344 0.0722  0.0992  0.0130  419 HOH   A O   
6768 O  O   . HOH   G .   ? 0.4096 0.2381 0.5410 -0.0805 -0.2249 0.1022  420 HOH   A O   
6769 O  O   . HOH   G .   ? 0.6602 0.4003 0.5013 0.1997  -0.0653 0.1573  421 HOH   A O   
6770 O  O   . HOH   G .   ? 0.2831 0.6128 0.1835 -0.0289 0.0442  0.0255  422 HOH   A O   
6771 O  O   . HOH   G .   ? 0.2174 0.2852 0.2708 -0.0178 -0.0619 0.0556  423 HOH   A O   
6772 O  O   . HOH   G .   ? 0.4240 0.4595 0.3582 0.1592  -0.0888 -0.1435 424 HOH   A O   
6773 O  O   . HOH   G .   ? 0.4903 0.5047 0.3746 0.2720  0.0168  -0.0572 425 HOH   A O   
6774 O  O   . HOH   G .   ? 0.4896 0.5810 0.3306 -0.1026 -0.0100 0.1091  426 HOH   A O   
6775 O  O   B HOH   G .   ? 0.1474 0.1426 0.3094 -0.0272 0.0087  0.0264  427 HOH   A O   
6776 O  O   . HOH   G .   ? 0.1644 0.2011 0.2739 -0.0067 0.0063  0.0362  428 HOH   A O   
6777 O  O   A HOH   G .   ? 0.2123 0.1933 0.2302 0.0122  0.0022  0.0514  429 HOH   A O   
6778 O  O   . HOH   G .   ? 0.3293 0.1377 0.2176 0.0088  -0.0442 0.0116  430 HOH   A O   
6779 O  O   A HOH   G .   ? 0.2000 0.2144 0.3530 0.0125  -0.0573 -0.0615 431 HOH   A O   
6780 O  O   . HOH   G .   ? 0.2341 0.4298 0.2528 0.1575  -0.0107 0.0157  432 HOH   A O   
6781 O  O   A HOH   G .   ? 0.2636 0.2991 0.2727 -0.0359 0.1027  -0.0138 433 HOH   A O   
6782 O  O   . HOH   G .   ? 0.8756 0.9121 0.7337 -0.0061 -0.0044 -0.0333 434 HOH   A O   
6783 O  O   . HOH   G .   ? 0.6372 0.6563 0.3901 0.1225  0.2423  -0.0290 435 HOH   A O   
6784 O  O   . HOH   G .   ? 0.6020 0.6336 0.6611 -0.1514 -0.0934 -0.0987 436 HOH   A O   
6785 O  O   . HOH   G .   ? 0.3665 0.2812 0.1821 -0.0790 0.0186  0.0665  437 HOH   A O   
6786 O  O   . HOH   G .   ? 0.5021 0.4753 0.4168 -0.0325 -0.1533 0.0305  438 HOH   A O   
6787 O  O   . HOH   G .   ? 0.2682 0.1656 0.2790 0.0049  -0.0017 0.0048  439 HOH   A O   
6788 O  O   . HOH   G .   ? 0.2824 0.3399 0.4927 -0.0245 0.0893  -0.1582 440 HOH   A O   
6789 O  O   . HOH   G .   ? 0.1810 0.2393 0.5036 -0.0255 -0.0798 0.0588  441 HOH   A O   
6790 O  O   . HOH   G .   ? 0.6161 0.6958 0.5900 -0.1295 0.0780  0.0405  442 HOH   A O   
6791 O  O   . HOH   G .   ? 0.5764 0.7518 0.4124 0.1815  -0.0765 0.1783  443 HOH   A O   
6792 O  O   . HOH   G .   ? 0.1780 0.1714 0.1521 -0.0043 -0.0153 -0.0103 444 HOH   A O   
6793 O  O   . HOH   G .   ? 0.5168 0.4303 0.5658 0.0586  0.0334  -0.1105 445 HOH   A O   
6794 O  O   . HOH   G .   ? 0.6447 0.6797 0.6059 0.0631  -0.1103 0.0233  446 HOH   A O   
6795 O  O   A HOH   G .   ? 0.2190 0.1840 0.2021 -0.0152 -0.0178 0.0020  447 HOH   A O   
6796 O  O   . HOH   G .   ? 0.4046 0.3544 0.3175 0.2094  -0.0399 -0.0323 448 HOH   A O   
6797 O  O   . HOH   G .   ? 0.5872 0.6252 0.6300 -0.1471 -0.0342 -0.1269 449 HOH   A O   
6798 O  O   A HOH   G .   ? 0.6172 0.4207 0.3412 -0.0092 0.0456  0.1165  450 HOH   A O   
6799 O  O   . HOH   G .   ? 0.2403 0.2169 0.2645 0.0144  0.0267  0.0213  451 HOH   A O   
6800 O  O   . HOH   G .   ? 0.4715 0.4682 0.4775 -0.1051 -0.0874 -0.1220 452 HOH   A O   
6801 O  O   B HOH   G .   ? 0.3730 0.3465 0.3251 0.0868  -0.0182 0.0247  453 HOH   A O   
6802 O  O   . HOH   G .   ? 0.2280 0.2846 0.2523 -0.0056 -0.0134 -0.0450 454 HOH   A O   
6803 O  O   . HOH   G .   ? 0.7045 0.5531 0.7689 0.1082  -0.1288 0.1950  455 HOH   A O   
6804 O  O   B HOH   G .   ? 0.4826 0.2648 0.3526 -0.0325 0.0694  0.0254  456 HOH   A O   
6805 O  O   . HOH   G .   ? 0.4736 0.4622 0.3915 0.0725  -0.0088 0.0581  457 HOH   A O   
6806 O  O   . HOH   G .   ? 0.5291 0.3578 0.4079 0.0215  0.0103  0.0133  458 HOH   A O   
6807 O  O   C HOH   G .   ? 0.2395 0.2566 0.2789 -0.0153 -0.0445 0.0004  459 HOH   A O   
6808 O  O   . HOH   G .   ? 0.6257 0.6109 0.5202 -0.0839 0.1048  0.1085  460 HOH   A O   
6809 O  O   . HOH   G .   ? 0.4267 0.3650 0.4406 0.0267  0.0141  0.0385  461 HOH   A O   
6810 O  O   B HOH   G .   ? 0.3470 0.1850 0.3429 0.0591  0.1317  0.0078  462 HOH   A O   
6811 O  O   . HOH   G .   ? 0.2726 0.4105 0.4339 0.0886  -0.0572 0.0966  463 HOH   A O   
6812 O  O   B HOH   G .   ? 0.4277 0.2697 0.2378 0.0989  0.0351  -0.0025 464 HOH   A O   
6813 O  O   . HOH   G .   ? 0.3368 0.4723 0.5534 -0.1303 0.1088  -0.1232 465 HOH   A O   
6814 O  O   . HOH   G .   ? 0.6977 0.7511 0.4810 0.0920  -0.1104 -0.0395 466 HOH   A O   
6815 O  O   . HOH   G .   ? 0.2943 0.2750 0.3801 -0.0683 0.0323  -0.0940 467 HOH   A O   
6816 O  O   . HOH   G .   ? 0.3553 0.4805 0.4848 0.0574  -0.0621 0.0978  468 HOH   A O   
6817 O  O   . HOH   G .   ? 0.3227 0.4912 0.3929 -0.0733 -0.0079 -0.0058 469 HOH   A O   
6818 O  O   . HOH   G .   ? 0.7514 0.6578 0.6369 0.1074  0.1641  0.2187  470 HOH   A O   
6819 O  O   . HOH   G .   ? 0.2790 0.2701 0.3589 -0.0959 0.0605  -0.0482 471 HOH   A O   
6820 O  O   . HOH   G .   ? 0.2626 0.4591 0.5095 0.0746  0.0049  -0.1884 472 HOH   A O   
6821 O  O   . HOH   G .   ? 0.6165 0.3658 0.6801 0.0821  0.0368  0.2211  473 HOH   A O   
6822 O  O   . HOH   G .   ? 0.3932 0.6475 0.3944 -0.0742 -0.0558 0.2398  474 HOH   A O   
6823 O  O   A HOH   G .   ? 0.2934 0.2592 0.5285 0.0899  -0.1893 -0.0977 475 HOH   A O   
6824 O  O   . HOH   G .   ? 0.5576 0.4739 0.4695 0.0092  0.1174  0.0321  476 HOH   A O   
6825 O  O   . HOH   G .   ? 0.4089 0.5262 0.3866 0.0351  -0.0506 -0.0629 477 HOH   A O   
6826 O  O   . HOH   G .   ? 0.2833 0.1820 0.2560 0.0222  -0.0957 -0.0306 478 HOH   A O   
6827 O  O   . HOH   G .   ? 0.3291 0.2644 0.3828 0.0253  0.0879  -0.0027 479 HOH   A O   
6828 O  O   . HOH   G .   ? 0.5915 0.5630 0.4933 0.1443  -0.1022 -0.0983 480 HOH   A O   
6829 O  O   . HOH   G .   ? 0.4593 0.4190 0.3579 -0.0576 -0.0456 -0.0142 481 HOH   A O   
6830 O  O   B HOH   G .   ? 0.1835 0.1760 0.3098 0.0442  -0.0514 0.0831  482 HOH   A O   
6831 O  O   . HOH   G .   ? 0.4451 0.4599 0.5415 -0.2041 -0.0557 -0.0590 483 HOH   A O   
6832 O  O   . HOH   G .   ? 0.3944 0.4895 0.2639 0.0136  0.0036  -0.0303 484 HOH   A O   
6833 O  O   . HOH   G .   ? 0.5180 0.2979 0.3494 -0.0816 -0.1309 0.0596  485 HOH   A O   
6834 O  O   . HOH   G .   ? 0.6877 0.5878 0.6899 -0.1096 0.0493  -0.0936 486 HOH   A O   
6835 O  O   . HOH   G .   ? 0.5446 0.5221 0.5486 -0.1752 -0.1259 0.0336  487 HOH   A O   
6836 O  O   . HOH   G .   ? 0.2872 0.4623 0.3647 -0.0383 -0.0235 -0.0936 488 HOH   A O   
6837 O  O   . HOH   G .   ? 0.5994 0.4305 0.3923 0.0600  0.0139  -0.1212 489 HOH   A O   
6838 O  O   . HOH   G .   ? 0.2435 0.2239 0.2724 0.0145  -0.0068 0.0147  490 HOH   A O   
6839 O  O   . HOH   G .   ? 0.7630 0.3913 0.3223 -0.0359 -0.1163 0.0547  491 HOH   A O   
6840 O  O   . HOH   G .   ? 0.2608 0.5457 0.3684 0.1184  0.0934  0.2448  492 HOH   A O   
6841 O  O   . HOH   G .   ? 0.3200 0.3833 0.4727 0.0126  0.1191  0.1080  493 HOH   A O   
6842 O  O   . HOH   G .   ? 0.6016 0.5796 0.4570 -0.0661 0.1214  0.1043  494 HOH   A O   
6843 O  O   . HOH   G .   ? 0.4747 0.3889 0.2697 -0.0936 0.1588  -0.0516 495 HOH   A O   
6844 O  O   . HOH   G .   ? 0.5408 0.5969 0.6634 0.1078  0.1685  -0.1072 496 HOH   A O   
6845 O  O   . HOH   G .   ? 0.5898 0.3888 0.4233 -0.0369 0.1134  -0.0404 497 HOH   A O   
6846 O  O   . HOH   G .   ? 0.5596 0.5102 0.4853 -0.0990 -0.1023 -0.0784 498 HOH   A O   
6847 O  O   . HOH   G .   ? 0.2667 0.2529 0.7195 -0.0121 -0.1240 0.0261  499 HOH   A O   
6848 O  O   . HOH   G .   ? 0.5177 0.5467 0.5654 0.0762  -0.1123 0.0386  500 HOH   A O   
6849 O  O   . HOH   G .   ? 0.3952 0.3919 0.4718 -0.1283 0.0065  0.1044  501 HOH   A O   
6850 O  O   . HOH   G .   ? 0.4419 0.3367 0.4986 -0.0173 0.2338  0.0239  502 HOH   A O   
6851 O  O   . HOH   G .   ? 0.2982 0.2326 0.5328 0.0132  0.0367  0.1204  503 HOH   A O   
6852 O  O   . HOH   G .   ? 0.2655 0.3502 0.4435 -0.0072 0.0925  -0.0440 504 HOH   A O   
6853 O  O   . HOH   G .   ? 0.6144 0.2654 0.4667 -0.0906 0.0703  0.0601  505 HOH   A O   
6854 O  O   . HOH   G .   ? 0.6927 0.6726 0.4848 0.1907  -0.1419 0.0949  506 HOH   A O   
6855 O  O   . HOH   G .   ? 0.2597 0.4134 0.3414 0.0901  -0.0390 0.0605  507 HOH   A O   
6856 O  O   . HOH   G .   ? 0.3757 0.7856 0.5928 -0.1095 -0.0366 0.2313  508 HOH   A O   
6857 O  O   . HOH   G .   ? 0.4748 0.2507 0.4085 -0.1291 0.0219  0.0258  509 HOH   A O   
6858 O  O   . HOH   G .   ? 0.2881 0.3886 0.4307 0.0676  -0.0339 0.0046  510 HOH   A O   
6859 O  O   . HOH   G .   ? 0.5915 0.7003 0.5105 0.0760  -0.0865 0.0499  511 HOH   A O   
6860 O  O   . HOH   G .   ? 0.6703 0.4112 0.5745 -0.0014 0.0929  -0.0060 512 HOH   A O   
6861 O  O   B HOH   G .   ? 0.2369 0.3316 0.2900 0.0162  0.0902  0.0029  513 HOH   A O   
6862 O  O   . HOH   G .   ? 0.2868 0.2623 0.4866 0.0107  0.0320  0.0647  514 HOH   A O   
6863 O  O   . HOH   G .   ? 0.5054 0.6895 0.5128 0.3030  0.0284  0.1611  515 HOH   A O   
6864 O  O   T HOH   G .   ? 0.1241 0.1217 0.1955 -0.0105 -0.0216 0.0292  516 HOH   A O   
6865 O  O   . HOH   G .   ? 0.4563 0.5751 0.4624 -0.0454 -0.0208 -0.1370 517 HOH   A O   
6866 O  O   A HOH   G .   ? 0.3979 0.8780 0.4315 0.1555  0.0547  -0.0289 518 HOH   A O   
6867 O  O   . HOH   G .   ? 0.2490 0.6738 0.4022 0.0338  0.0289  -0.0289 519 HOH   A O   
6868 O  O   . HOH   G .   ? 0.5678 0.4651 0.4595 0.1500  -0.0279 0.1232  520 HOH   A O   
6869 O  O   . HOH   G .   ? 0.4881 0.6829 0.5236 -0.0750 -0.0229 0.0618  521 HOH   A O   
6870 O  O   . HOH   G .   ? 0.3225 0.4309 0.5660 -0.0218 -0.0824 0.2550  522 HOH   A O   
6871 O  O   . HOH   H .   ? 0.2364 0.2366 0.3294 0.0221  0.0831  0.0422  201 HOH   B O   
6872 O  O   . HOH   H .   ? 0.6342 0.5754 0.5858 0.1675  0.0639  0.0170  202 HOH   B O   
6873 O  O   . HOH   H .   ? 0.5267 0.4824 0.2803 0.0386  -0.0174 -0.1185 203 HOH   B O   
6874 O  O   . HOH   H .   ? 0.4623 0.3021 0.3856 -0.0606 0.0216  -0.1209 204 HOH   B O   
6875 O  O   . HOH   H .   ? 0.5073 0.5739 0.4048 0.2831  -0.1372 -0.0301 205 HOH   B O   
6876 O  O   . HOH   H .   ? 0.4051 0.4426 0.4677 -0.1051 0.0617  -0.1511 206 HOH   B O   
6877 O  O   . HOH   H .   ? 0.3354 0.7177 0.3815 0.0226  -0.0024 0.2489  207 HOH   B O   
6878 O  O   . HOH   H .   ? 0.3861 0.3692 0.6639 -0.0874 0.0576  -0.0590 208 HOH   B O   
6879 O  O   . HOH   H .   ? 0.7042 0.3518 0.4384 0.0261  0.1301  -0.0025 209 HOH   B O   
6880 O  O   . HOH   H .   ? 0.4286 0.5961 0.3777 0.2806  -0.0388 0.0196  210 HOH   B O   
6881 O  O   . HOH   H .   ? 0.3500 0.5119 0.4431 0.1998  0.0512  -0.0230 211 HOH   B O   
6882 O  O   . HOH   H .   ? 0.1666 0.1981 0.2810 -0.0220 -0.0029 0.0060  212 HOH   B O   
6883 O  O   . HOH   H .   ? 0.1901 0.2253 0.2903 -0.0044 0.0128  -0.0251 213 HOH   B O   
6884 O  O   . HOH   H .   ? 0.4680 0.3872 0.6291 0.0488  -0.0944 0.2486  214 HOH   B O   
6885 O  O   . HOH   H .   ? 0.2840 0.2987 0.6273 0.0406  -0.0987 0.0606  215 HOH   B O   
6886 O  O   . HOH   H .   ? 0.2998 0.5262 0.5294 -0.0071 0.1570  -0.1894 216 HOH   B O   
6887 O  O   . HOH   H .   ? 0.4508 0.3836 0.3775 -0.0063 -0.0897 0.0371  217 HOH   B O   
6888 O  O   . HOH   H .   ? 0.4512 0.5422 0.6306 0.0322  -0.1564 -0.1065 218 HOH   B O   
6889 O  O   . HOH   H .   ? 0.5945 0.3028 0.4276 -0.1826 0.0096  0.0323  219 HOH   B O   
6890 O  O   . HOH   H .   ? 0.4971 0.2257 0.3066 -0.0052 -0.0954 0.0148  220 HOH   B O   
6891 O  O   . HOH   H .   ? 0.4705 0.4368 0.4275 0.0025  0.1009  -0.1713 221 HOH   B O   
6892 O  O   . HOH   H .   ? 0.3385 0.3189 0.4937 0.0609  -0.0436 0.0050  222 HOH   B O   
6893 O  O   . HOH   H .   ? 0.3224 0.3287 0.5696 -0.0035 0.0437  -0.0189 223 HOH   B O   
6894 O  O   . HOH   H .   ? 0.4260 0.6277 0.3822 0.2333  0.0061  -0.0385 224 HOH   B O   
6895 O  O   . HOH   H .   ? 0.2527 0.1883 0.2879 -0.0315 0.1090  -0.0033 225 HOH   B O   
6896 O  O   . HOH   H .   ? 0.3105 0.2120 0.5655 0.0252  0.2036  0.0875  226 HOH   B O   
6897 O  O   . HOH   H .   ? 0.2324 0.2358 0.4133 -0.0364 -0.0101 -0.0706 227 HOH   B O   
6898 O  O   . HOH   H .   ? 0.4069 0.3827 0.5249 -0.1615 -0.0138 0.1079  228 HOH   B O   
6899 O  O   . HOH   H .   ? 0.1756 0.2092 0.3143 -0.0104 0.0121  -0.0061 229 HOH   B O   
6900 O  O   . HOH   H .   ? 0.6890 0.4680 0.4690 0.2041  -0.0425 -0.1223 230 HOH   B O   
6901 O  O   . HOH   H .   ? 0.2608 0.3761 0.3203 -0.0660 0.0296  -0.0282 231 HOH   B O   
6902 O  O   . HOH   H .   ? 0.3603 0.1932 0.2157 0.0227  -0.0755 -0.0163 232 HOH   B O   
6903 O  O   . HOH   H .   ? 0.3150 0.2361 0.4767 -0.0037 0.1583  0.0261  233 HOH   B O   
6904 O  O   . HOH   H .   ? 0.5083 0.3235 0.4004 -0.2305 -0.0058 0.0080  234 HOH   B O   
6905 O  O   . HOH   H .   ? 0.2636 0.2737 0.3263 0.0325  0.0107  -0.0909 235 HOH   B O   
6906 O  O   . HOH   H .   ? 0.3854 0.3403 0.2211 0.0447  0.0714  0.0578  236 HOH   B O   
6907 O  O   . HOH   H .   ? 0.5795 0.5820 0.3319 0.1503  -0.0095 0.0355  237 HOH   B O   
6908 O  O   . HOH   H .   ? 0.1518 0.1479 0.1628 -0.0108 -0.0059 -0.0053 238 HOH   B O   
6909 O  O   . HOH   H .   ? 0.2357 0.3671 0.3232 -0.0518 -0.0632 -0.0514 239 HOH   B O   
6910 O  O   . HOH   H .   ? 0.2160 0.2512 0.3178 -0.0552 -0.0025 -0.0268 240 HOH   B O   
6911 O  O   . HOH   H .   ? 0.3124 0.2515 0.3387 -0.0125 0.0011  -0.0726 241 HOH   B O   
6912 O  O   . HOH   H .   ? 0.4301 0.3395 0.3568 -0.0862 0.0794  -0.1042 242 HOH   B O   
6913 O  O   . HOH   H .   ? 0.2833 0.2314 0.3073 0.0867  0.0699  0.0134  243 HOH   B O   
6914 O  O   . HOH   H .   ? 0.1620 0.1543 0.2704 0.0006  0.0131  -0.0087 244 HOH   B O   
6915 O  O   . HOH   H .   ? 0.2152 0.1381 0.3395 0.0059  -0.0641 -0.0126 245 HOH   B O   
6916 O  O   . HOH   H .   ? 0.2352 0.3732 0.2555 -0.0422 -0.0313 0.0639  246 HOH   B O   
6917 O  O   . HOH   H .   ? 0.3377 0.4121 0.2185 0.0340  0.0770  0.0211  247 HOH   B O   
6918 O  O   . HOH   H .   ? 0.3323 0.1739 0.5938 -0.0222 -0.1161 -0.0429 248 HOH   B O   
6919 O  O   . HOH   H .   ? 0.1464 0.1403 0.1647 -0.0020 -0.0062 0.0092  249 HOH   B O   
6920 O  O   . HOH   H .   ? 0.3627 0.3226 0.4287 0.0631  -0.0981 -0.1598 250 HOH   B O   
6921 O  O   . HOH   H .   ? 0.5941 0.3392 0.2618 0.0041  0.0621  -0.0016 251 HOH   B O   
6922 O  O   . HOH   H .   ? 0.2278 0.2010 0.2125 -0.0373 -0.0397 0.0123  252 HOH   B O   
6923 O  O   . HOH   H .   ? 0.3775 0.2672 0.4157 0.0742  -0.0332 -0.0590 253 HOH   B O   
6924 O  O   . HOH   H .   ? 0.2641 0.4007 0.5659 0.1044  -0.0775 -0.1169 254 HOH   B O   
6925 O  O   . HOH   H .   ? 0.2204 0.1540 0.2064 -0.0295 -0.0356 0.0250  255 HOH   B O   
6926 O  O   . HOH   H .   ? 0.3383 0.4832 0.3391 -0.0508 -0.1192 0.1124  256 HOH   B O   
6927 O  O   . HOH   H .   ? 0.2568 0.3672 0.3736 0.0233  0.1038  0.0135  257 HOH   B O   
6928 O  O   . HOH   H .   ? 0.2463 0.2254 0.1966 0.0080  -0.0235 0.0073  258 HOH   B O   
6929 O  O   . HOH   H .   ? 0.2467 0.2327 0.2670 0.0867  -0.0786 -0.0718 259 HOH   B O   
6930 O  O   . HOH   H .   ? 0.2920 0.3716 0.3154 -0.0834 -0.0356 -0.0610 260 HOH   B O   
6931 O  O   . HOH   H .   ? 0.2383 0.3268 0.2311 -0.0596 0.0341  0.0423  261 HOH   B O   
6932 O  O   . HOH   H .   ? 0.1711 0.1735 0.2920 -0.0203 -0.0221 0.0077  262 HOH   B O   
6933 O  O   . HOH   H .   ? 0.2328 0.2203 0.2184 0.0050  -0.0098 -0.0018 263 HOH   B O   
6934 O  O   . HOH   H .   ? 0.2219 0.2178 0.3315 -0.0028 -0.0616 -0.0397 264 HOH   B O   
6935 O  O   . HOH   H .   ? 0.2773 0.4691 0.5821 0.0210  -0.0058 -0.1162 265 HOH   B O   
6936 O  O   . HOH   H .   ? 0.1491 0.1716 0.2083 -0.0075 0.0063  0.0163  266 HOH   B O   
6937 O  O   . HOH   H .   ? 0.2540 0.2041 0.3112 -0.0626 0.0244  -0.0180 267 HOH   B O   
6938 O  O   . HOH   H .   ? 0.1916 0.1887 0.1778 -0.0454 -0.0416 0.0063  268 HOH   B O   
6939 O  O   . HOH   H .   ? 0.2192 0.4218 0.4999 -0.0484 -0.0162 -0.1332 269 HOH   B O   
6940 O  O   . HOH   H .   ? 0.2075 0.1561 0.2297 -0.0284 -0.0199 0.0113  270 HOH   B O   
6941 O  O   . HOH   H .   ? 0.2536 0.4000 0.3373 -0.0765 0.0649  -0.1421 271 HOH   B O   
6942 O  O   . HOH   H .   ? 0.4738 0.4097 0.2866 0.0456  -0.0118 -0.1027 272 HOH   B O   
6943 O  O   . HOH   H .   ? 0.2605 0.2955 0.2507 -0.0481 -0.0763 0.0110  273 HOH   B O   
6944 O  O   . HOH   H .   ? 0.1825 0.1435 0.4089 -0.0063 -0.0326 -0.0099 274 HOH   B O   
6945 O  O   . HOH   H .   ? 0.2511 0.2624 0.2394 -0.0488 -0.0693 -0.0343 275 HOH   B O   
6946 O  O   . HOH   H .   ? 0.3069 0.3388 0.5477 -0.0075 -0.0012 -0.0542 276 HOH   B O   
6947 O  O   . HOH   H .   ? 0.4358 0.2813 0.4318 -0.0143 -0.1362 -0.0354 277 HOH   B O   
6948 O  O   . HOH   H .   ? 0.2883 0.2195 0.4989 0.0251  0.0424  0.0369  278 HOH   B O   
6949 O  O   . HOH   H .   ? 0.2709 0.4455 0.2365 0.1708  -0.0406 -0.0658 279 HOH   B O   
6950 O  O   . HOH   H .   ? 0.1738 0.1635 0.3423 -0.0123 0.0129  -0.0044 280 HOH   B O   
6951 O  O   . HOH   H .   ? 0.3551 0.3787 0.4916 0.1209  -0.0851 -0.1230 281 HOH   B O   
6952 O  O   . HOH   H .   ? 0.3861 0.7243 0.3515 0.1490  -0.0399 0.1360  282 HOH   B O   
6953 O  O   . HOH   H .   ? 0.1672 0.1592 0.1935 0.0036  0.0047  0.0044  283 HOH   B O   
6954 O  O   . HOH   H .   ? 0.5792 0.3551 0.3121 0.2468  0.1166  0.0693  284 HOH   B O   
6955 O  O   . HOH   H .   ? 0.2835 0.4873 0.4717 -0.0935 -0.1149 0.0633  285 HOH   B O   
6956 O  O   . HOH   H .   ? 0.1834 0.3392 0.4705 0.0314  -0.0065 -0.1446 286 HOH   B O   
6957 O  O   . HOH   H .   ? 0.2820 0.6100 0.7084 0.1200  -0.0434 -0.0702 287 HOH   B O   
6958 O  O   . HOH   H .   ? 0.4385 0.4615 0.4935 -0.0131 -0.1535 0.0291  288 HOH   B O   
6959 O  O   . HOH   H .   ? 0.2439 0.2668 0.2853 0.0162  -0.0696 0.0155  289 HOH   B O   
6960 O  O   . HOH   H .   ? 0.1810 0.2048 0.2881 0.0203  -0.0101 0.0026  290 HOH   B O   
6961 O  O   . HOH   H .   ? 0.3526 0.2761 0.2257 0.0241  -0.0787 -0.0061 291 HOH   B O   
6962 O  O   . HOH   H .   ? 0.1673 0.2090 0.1643 -0.0164 -0.0187 0.0084  292 HOH   B O   
6963 O  O   . HOH   H .   ? 0.4566 0.4592 0.2319 0.0701  -0.0291 -0.0178 293 HOH   B O   
6964 O  O   . HOH   H .   ? 0.2468 0.6914 0.2629 0.0844  -0.0361 -0.0455 294 HOH   B O   
6965 O  O   . HOH   H .   ? 0.3627 0.2278 0.4021 -0.0840 -0.2021 0.0752  295 HOH   B O   
6966 O  O   . HOH   H .   ? 0.3298 0.2771 0.2981 -0.0129 0.0016  -0.1336 296 HOH   B O   
6967 O  O   . HOH   H .   ? 0.4349 0.3599 0.4758 -0.0699 0.0187  0.1352  297 HOH   B O   
6968 O  O   . HOH   H .   ? 0.4317 0.5874 0.2409 -0.0533 -0.0835 0.1197  298 HOH   B O   
6969 O  O   . HOH   H .   ? 0.2766 0.3169 0.4961 -0.0482 -0.1520 0.1124  299 HOH   B O   
6970 O  O   . HOH   H .   ? 0.3531 0.2000 0.3488 0.0769  0.1181  0.0500  300 HOH   B O   
6971 O  O   . HOH   H .   ? 0.2984 0.2995 0.5079 -0.0194 -0.0879 0.1114  301 HOH   B O   
6972 O  O   . HOH   H .   ? 0.5021 0.3876 0.2539 0.1453  -0.0836 0.0430  302 HOH   B O   
6973 O  O   . HOH   H .   ? 0.2187 0.1680 0.2658 -0.0258 -0.0342 -0.0027 303 HOH   B O   
6974 O  O   . HOH   H .   ? 0.6183 0.6363 0.5352 0.2978  -0.0040 -0.0138 304 HOH   B O   
6975 O  O   . HOH   H .   ? 0.1813 0.1712 0.2528 0.0053  0.0018  0.0138  305 HOH   B O   
6976 O  O   . HOH   H .   ? 0.3223 0.3675 0.4238 -0.1400 0.1112  -0.0508 306 HOH   B O   
6977 O  O   . HOH   H .   ? 0.4369 0.4554 0.2149 -0.0131 0.0520  0.0576  307 HOH   B O   
6978 O  O   . HOH   H .   ? 0.2139 0.2806 0.5994 0.0463  -0.0373 -0.0983 308 HOH   B O   
6979 O  O   . HOH   H .   ? 0.5339 0.2887 0.2367 -0.1769 0.0769  -0.0252 309 HOH   B O   
6980 O  O   . HOH   H .   ? 0.2753 0.3009 0.3836 -0.0390 0.1159  -0.0983 310 HOH   B O   
6981 O  O   . HOH   H .   ? 0.2063 0.1681 0.3541 0.0356  -0.0934 -0.0041 311 HOH   B O   
6982 O  O   . HOH   H .   ? 0.1615 0.1899 0.3037 -0.0287 -0.0114 0.0084  312 HOH   B O   
6983 O  O   . HOH   H .   ? 0.3467 0.4125 0.7145 -0.0124 -0.0899 0.1734  313 HOH   B O   
6984 O  O   . HOH   H .   ? 0.1631 0.1557 0.3275 0.0079  0.0007  -0.0004 314 HOH   B O   
6985 O  O   . HOH   H .   ? 0.4373 0.3282 0.5024 0.1098  0.2001  0.1657  315 HOH   B O   
6986 O  O   . HOH   H .   ? 0.2532 0.1594 0.2461 -0.0155 -0.0085 0.0379  316 HOH   B O   
6987 O  O   . HOH   H .   ? 0.2357 0.3318 0.4688 -0.0315 -0.0296 -0.0039 317 HOH   B O   
6988 O  O   . HOH   H .   ? 0.2160 0.2048 0.2055 -0.0134 0.0265  0.0165  318 HOH   B O   
6989 O  O   . HOH   H .   ? 0.4544 0.4804 0.2754 0.0811  -0.0542 -0.0859 319 HOH   B O   
6990 O  O   . HOH   H .   ? 0.4563 0.4165 0.6005 0.0552  -0.0045 0.0799  320 HOH   B O   
6991 O  O   . HOH   H .   ? 0.2259 0.5355 0.4879 -0.0438 -0.0362 -0.0260 321 HOH   B O   
6992 O  O   . HOH   H .   ? 0.1653 0.1667 0.3036 -0.0158 -0.0064 -0.0080 322 HOH   B O   
6993 O  O   . HOH   H .   ? 0.4190 0.2506 0.2608 0.1618  0.1100  0.0468  323 HOH   B O   
6994 O  O   . HOH   H .   ? 0.1661 0.2906 0.2537 -0.0135 -0.0147 0.0677  324 HOH   B O   
6995 O  O   . HOH   H .   ? 0.3016 0.2149 0.2458 0.0151  -0.0153 0.0270  325 HOH   B O   
6996 O  O   . HOH   H .   ? 0.6711 0.4198 0.5417 0.1272  0.1368  0.0047  326 HOH   B O   
6997 O  O   . HOH   H .   ? 0.4413 0.2506 0.3202 0.0237  0.0518  0.0728  327 HOH   B O   
6998 O  O   . HOH   H .   ? 0.5828 0.5399 0.5352 -0.1066 -0.0380 0.1184  328 HOH   B O   
6999 O  O   . HOH   H .   ? 0.6209 0.4614 0.6265 0.0914  -0.0929 0.1721  329 HOH   B O   
7000 O  O   . HOH   H .   ? 0.1914 0.2060 0.2969 0.0384  0.0396  0.0234  330 HOH   B O   
7001 O  O   . HOH   H .   ? 0.8047 0.2128 0.3261 0.0176  -0.0761 0.0162  331 HOH   B O   
7002 O  O   . HOH   H .   ? 0.1871 0.2769 0.3145 0.0318  -0.0200 -0.0501 332 HOH   B O   
7003 O  O   . HOH   H .   ? 0.2940 0.2106 0.4764 -0.0019 0.0061  0.0438  333 HOH   B O   
7004 O  O   . HOH   H .   ? 0.5712 0.3525 0.3657 -0.0094 0.1029  0.1163  334 HOH   B O   
7005 O  O   . HOH   H .   ? 0.2156 0.2470 0.5560 -0.0504 0.0056  0.1397  335 HOH   B O   
7006 O  O   . HOH   H .   ? 0.4457 0.6871 0.4009 -0.0124 -0.0427 0.1870  336 HOH   B O   
7007 O  O   . HOH   H .   ? 0.5938 0.4200 0.6218 -0.0793 -0.0670 -0.1154 337 HOH   B O   
7008 O  O   . HOH   H .   ? 0.1829 0.1482 0.2472 0.0048  -0.0190 0.0072  338 HOH   B O   
7009 O  O   . HOH   H .   ? 0.5049 0.3399 0.4505 0.0232  0.0574  -0.1616 339 HOH   B O   
7010 O  O   . HOH   H .   ? 0.5186 0.3218 0.3093 0.0505  -0.1224 -0.0702 340 HOH   B O   
7011 O  O   . HOH   H .   ? 0.4673 0.5410 0.3763 -0.0172 -0.1129 0.0616  341 HOH   B O   
7012 O  O   . HOH   H .   ? 0.3978 0.6203 0.4081 -0.1186 -0.0918 -0.0637 342 HOH   B O   
7013 O  O   . HOH   H .   ? 0.1974 0.6029 0.6424 -0.0210 -0.0740 0.0130  343 HOH   B O   
7014 O  O   . HOH   H .   ? 0.6526 0.6077 0.2996 -0.0129 -0.0534 0.1072  344 HOH   B O   
7015 O  O   . HOH   H .   ? 0.2214 0.2123 0.3111 -0.0168 0.0626  -0.0100 345 HOH   B O   
7016 O  O   . HOH   H .   ? 0.4170 0.5391 0.5248 0.0264  -0.0960 0.0384  346 HOH   B O   
7017 O  O   . HOH   H .   ? 0.2551 0.6254 0.3383 0.1663  -0.0651 -0.1587 347 HOH   B O   
7018 O  O   . HOH   H .   ? 0.2940 0.2355 0.5187 -0.0335 -0.1091 -0.0521 348 HOH   B O   
7019 O  O   . HOH   H .   ? 0.2313 0.3994 0.5009 0.0117  0.0619  0.0157  349 HOH   B O   
7020 O  O   . HOH   H .   ? 0.4976 0.5087 0.4560 -0.1019 0.0204  0.1209  350 HOH   B O   
7021 O  O   . HOH   H .   ? 0.4591 0.5790 0.6452 0.0289  0.0518  0.0021  351 HOH   B O   
7022 O  O   . HOH   H .   ? 0.3016 0.1961 0.4255 0.0471  -0.1410 -0.0587 352 HOH   B O   
7023 O  O   . HOH   H .   ? 0.3522 0.2423 0.3732 -0.0565 0.0313  -0.1045 353 HOH   B O   
7024 O  O   . HOH   H .   ? 0.3473 0.4366 0.4842 -0.1270 0.0080  -0.0446 354 HOH   B O   
7025 O  O   . HOH   H .   ? 0.4501 0.3496 0.5142 -0.1438 0.0944  0.0699  355 HOH   B O   
7026 O  O   . HOH   H .   ? 0.5315 0.3753 0.4304 0.0489  0.1378  -0.0717 356 HOH   B O   
7027 O  O   . HOH   H .   ? 0.3883 0.2720 0.3809 -0.0964 0.0136  -0.0675 357 HOH   B O   
7028 O  O   . HOH   H .   ? 0.4926 0.4679 0.5562 -0.0241 -0.0487 -0.0025 358 HOH   B O   
7029 O  O   . HOH   H .   ? 0.4945 0.3487 0.5076 0.0177  -0.1694 -0.0457 359 HOH   B O   
7030 O  O   . HOH   H .   ? 0.4491 0.5220 0.5410 0.1626  -0.1228 0.1723  360 HOH   B O   
7031 O  O   . HOH   H .   ? 0.4856 0.4353 0.6363 0.0325  0.0832  0.1528  361 HOH   B O   
7032 O  O   . HOH   H .   ? 0.2321 0.3770 0.6722 -0.0953 -0.0465 -0.0710 362 HOH   B O   
7033 O  O   . HOH   H .   ? 0.4711 0.5730 0.3344 0.1744  0.0107  0.0326  363 HOH   B O   
7034 O  O   . HOH   H .   ? 0.4741 0.3319 0.5390 -0.1448 -0.0429 0.0185  364 HOH   B O   
7035 O  O   . HOH   H .   ? 0.5825 0.4766 0.4332 0.0993  0.0536  0.0707  365 HOH   B O   
7036 O  O   . HOH   H .   ? 0.5040 0.3603 0.5531 0.0794  -0.1761 0.0223  366 HOH   B O   
7037 O  O   . HOH   H .   ? 0.5193 0.5942 0.3632 0.1751  -0.1226 0.0678  367 HOH   B O   
7038 O  O   . HOH   H .   ? 0.5212 0.5788 0.4477 -0.0898 -0.0652 -0.1061 368 HOH   B O   
7039 O  O   . HOH   H .   ? 0.7294 0.7572 0.4799 0.2094  -0.1336 0.1265  369 HOH   B O   
7040 O  O   . HOH   H .   ? 0.5829 0.2446 0.3717 0.0097  0.0295  0.0751  370 HOH   B O   
7041 O  O   . HOH   H .   ? 0.4437 0.5516 0.5014 0.2596  0.1040  0.1078  371 HOH   B O   
7042 O  O   . HOH   H .   ? 0.6090 0.3925 0.3287 -0.0983 -0.1211 -0.0570 372 HOH   B O   
7043 O  O   . HOH   H .   ? 0.5005 0.3223 0.4006 0.1088  -0.1606 -0.0557 373 HOH   B O   
7044 O  O   . HOH   H .   ? 0.4594 0.5343 0.4712 -0.1249 -0.0569 0.0587  374 HOH   B O   
7045 O  O   . HOH   H .   ? 0.2291 0.4755 0.4463 0.0146  -0.0440 -0.0760 375 HOH   B O   
7046 O  O   . HOH   H .   ? 0.6949 0.3751 0.5038 -0.1108 -0.0658 0.0217  376 HOH   B O   
7047 O  O   . HOH   H .   ? 0.3048 0.4093 0.2468 0.0502  0.0237  0.0044  377 HOH   B O   
7048 O  O   . HOH   H .   ? 0.4351 0.6801 0.5968 0.1036  0.0428  0.2579  378 HOH   B O   
7049 O  O   . HOH   H .   ? 0.5989 0.7176 0.4214 -0.1354 0.0238  -0.1377 379 HOH   B O   
7050 O  O   . HOH   H .   ? 0.4101 0.5140 0.4459 0.0623  -0.0073 -0.0063 380 HOH   B O   
7051 O  O   . HOH   H .   ? 0.6001 0.6441 0.6545 -0.0197 0.2055  0.1264  381 HOH   B O   
7052 O  O   . HOH   H .   ? 0.3006 0.2556 0.3546 0.0099  0.0252  0.0476  382 HOH   B O   
7053 O  O   . HOH   H .   ? 0.4812 0.8024 0.5529 0.0912  0.2163  0.1168  383 HOH   B O   
7054 O  O   . HOH   H .   ? 0.6556 0.4561 0.4136 0.1305  0.0834  -0.0503 384 HOH   B O   
7055 O  O   . HOH   H .   ? 0.5629 0.4564 0.4232 -0.0120 -0.0800 -0.0203 385 HOH   B O   
7056 O  O   . HOH   H .   ? 0.5699 0.4558 0.5843 -0.0754 0.0585  -0.0503 386 HOH   B O   
7057 O  O   . HOH   H .   ? 0.6542 0.5713 0.4814 0.2200  0.0014  -0.0256 387 HOH   B O   
7058 O  O   . HOH   H .   ? 0.2533 0.4411 0.3838 -0.0782 -0.0971 -0.0309 388 HOH   B O   
7059 O  O   . HOH   H .   ? 0.4683 0.3607 0.3768 0.0098  0.0571  -0.0006 389 HOH   B O   
7060 O  O   . HOH   H .   ? 0.3820 0.2548 0.3279 0.0837  -0.0182 0.0157  390 HOH   B O   
7061 O  O   . HOH   H .   ? 0.4698 0.4265 0.4063 0.0189  0.0591  0.0557  391 HOH   B O   
7062 O  O   . HOH   H .   ? 0.2638 0.4216 0.6317 -0.1360 -0.0783 0.0113  392 HOH   B O   
7063 O  O   . HOH   H .   ? 0.4294 0.2316 0.5306 -0.0477 0.0699  0.0621  393 HOH   B O   
7064 O  O   . HOH   H .   ? 0.4188 0.5790 0.4016 0.0902  -0.0135 -0.0978 394 HOH   B O   
7065 O  O   . HOH   H .   ? 0.4239 0.4382 0.4509 0.0281  0.0748  0.0975  395 HOH   B O   
7066 O  O   . HOH   H .   ? 0.3175 0.3760 0.4032 0.0292  0.0080  -0.0584 396 HOH   B O   
7067 O  O   . HOH   H .   ? 0.2190 0.3008 0.6007 -0.0576 -0.1058 0.0477  397 HOH   B O   
7068 O  O   . HOH   H .   ? 0.5843 0.4397 0.3234 -0.2391 -0.0478 0.1306  398 HOH   B O   
7069 O  O   . HOH   H .   ? 0.5740 0.6942 0.7320 0.2041  -0.1004 0.1607  399 HOH   B O   
7070 O  O   . HOH   H .   ? 0.5469 0.6530 0.3624 0.1508  0.0058  -0.0391 400 HOH   B O   
# 
