data_7HDA
# 
_entry.id   7HDA 
# 
_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   7HDA         pdb_00007hda 10.2210/pdb7hda/pdb 
WWPDB D_1001407328 ?            ?                   
# 
_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                        7HDA 
_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)-2-phenyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' 254.287   1   ?                      ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                       35.453    1   ?                      ? ? ? 
5 water       nat water                                                                18.015    413 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                               TFA   
3 '(2S)-2-phenyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' A1A7Z 
4 'CHLORIDE ION'                                                       CL    
5 water                                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A7Z non-polymer         . '(2S)-2-phenyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' ? 'C14 H14 N4 O'   254.287 
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 A1A7Z 1   202 201  A1A7Z LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 86   HOH   HOH A . 
F 5 HOH   3   303 196  HOH   HOH A . 
F 5 HOH   4   304 229  HOH   HOH A . 
F 5 HOH   5   305 1289 HOH   HOH A . 
F 5 HOH   6   306 209  HOH   HOH A . 
F 5 HOH   7   307 625  HOH   HOH A . 
F 5 HOH   8   308 661  HOH   HOH A . 
F 5 HOH   9   309 493  HOH   HOH A . 
F 5 HOH   10  310 1301 HOH   HOH A . 
F 5 HOH   11  311 247  HOH   HOH A . 
F 5 HOH   12  312 105  HOH   HOH A . 
F 5 HOH   13  313 136  HOH   HOH A . 
F 5 HOH   14  314 109  HOH   HOH A . 
F 5 HOH   15  315 1295 HOH   HOH A . 
F 5 HOH   16  316 630  HOH   HOH A . 
F 5 HOH   17  317 192  HOH   HOH A . 
F 5 HOH   18  318 124  HOH   HOH A . 
F 5 HOH   19  319 1310 HOH   HOH A . 
F 5 HOH   20  320 76   HOH   HOH A . 
F 5 HOH   21  321 409  HOH   HOH A . 
F 5 HOH   22  322 281  HOH   HOH A . 
F 5 HOH   23  323 1094 HOH   HOH A . 
F 5 HOH   24  324 1283 HOH   HOH A . 
F 5 HOH   25  325 236  HOH   HOH A . 
F 5 HOH   26  326 1275 HOH   HOH A . 
F 5 HOH   27  327 15   HOH   HOH A . 
F 5 HOH   28  328 165  HOH   HOH A . 
F 5 HOH   29  329 39   HOH   HOH A . 
F 5 HOH   30  330 153  HOH   HOH A . 
F 5 HOH   31  331 1300 HOH   HOH A . 
F 5 HOH   32  332 662  HOH   HOH A . 
F 5 HOH   33  333 469  HOH   HOH A . 
F 5 HOH   34  334 155  HOH   HOH A . 
F 5 HOH   35  335 164  HOH   HOH A . 
F 5 HOH   36  336 57   HOH   HOH A . 
F 5 HOH   37  337 140  HOH   HOH A . 
F 5 HOH   38  338 1290 HOH   HOH A . 
F 5 HOH   39  339 393  HOH   HOH A . 
F 5 HOH   40  340 241  HOH   HOH A . 
F 5 HOH   41  341 18   HOH   HOH A . 
F 5 HOH   42  342 225  HOH   HOH A . 
F 5 HOH   43  343 320  HOH   HOH A . 
F 5 HOH   44  344 1    HOH   HOH A . 
F 5 HOH   45  345 21   HOH   HOH A . 
F 5 HOH   46  346 132  HOH   HOH A . 
F 5 HOH   47  347 1308 HOH   HOH A . 
F 5 HOH   48  348 17   HOH   HOH A . 
F 5 HOH   49  349 337  HOH   HOH A . 
F 5 HOH   50  350 93   HOH   HOH A . 
F 5 HOH   51  351 964  HOH   HOH A . 
F 5 HOH   52  352 151  HOH   HOH A . 
F 5 HOH   53  353 42   HOH   HOH A . 
F 5 HOH   54  354 92   HOH   HOH A . 
F 5 HOH   55  355 354  HOH   HOH A . 
F 5 HOH   56  356 8    HOH   HOH A . 
F 5 HOH   57  357 2    HOH   HOH A . 
F 5 HOH   58  358 169  HOH   HOH A . 
F 5 HOH   59  359 56   HOH   HOH A . 
F 5 HOH   60  360 66   HOH   HOH A . 
F 5 HOH   61  361 396  HOH   HOH A . 
F 5 HOH   62  362 36   HOH   HOH A . 
F 5 HOH   63  363 4    HOH   HOH A . 
F 5 HOH   64  364 81   HOH   HOH A . 
F 5 HOH   65  365 148  HOH   HOH A . 
F 5 HOH   66  366 19   HOH   HOH A . 
F 5 HOH   67  367 139  HOH   HOH A . 
F 5 HOH   68  368 102  HOH   HOH A . 
F 5 HOH   69  369 12   HOH   HOH A . 
F 5 HOH   70  370 405  HOH   HOH A . 
F 5 HOH   71  371 939  HOH   HOH A . 
F 5 HOH   72  372 138  HOH   HOH A . 
F 5 HOH   73  373 33   HOH   HOH A . 
F 5 HOH   74  374 5    HOH   HOH A . 
F 5 HOH   75  375 162  HOH   HOH A . 
F 5 HOH   76  376 159  HOH   HOH A . 
F 5 HOH   77  377 218  HOH   HOH A . 
F 5 HOH   78  378 296  HOH   HOH A . 
F 5 HOH   79  379 45   HOH   HOH A . 
F 5 HOH   80  380 24   HOH   HOH A . 
F 5 HOH   81  381 186  HOH   HOH A . 
F 5 HOH   82  382 96   HOH   HOH A . 
F 5 HOH   83  383 26   HOH   HOH A . 
F 5 HOH   84  384 62   HOH   HOH A . 
F 5 HOH   85  385 46   HOH   HOH A . 
F 5 HOH   86  386 134  HOH   HOH A . 
F 5 HOH   87  387 78   HOH   HOH A . 
F 5 HOH   88  388 140  HOH   HOH A . 
F 5 HOH   89  389 366  HOH   HOH A . 
F 5 HOH   90  390 27   HOH   HOH A . 
F 5 HOH   91  391 6    HOH   HOH A . 
F 5 HOH   92  392 35   HOH   HOH A . 
F 5 HOH   93  393 49   HOH   HOH A . 
F 5 HOH   94  394 74   HOH   HOH A . 
F 5 HOH   95  395 154  HOH   HOH A . 
F 5 HOH   96  396 116  HOH   HOH A . 
F 5 HOH   97  397 461  HOH   HOH A . 
F 5 HOH   98  398 34   HOH   HOH A . 
F 5 HOH   99  399 381  HOH   HOH A . 
F 5 HOH   100 400 333  HOH   HOH A . 
F 5 HOH   101 401 85   HOH   HOH A . 
F 5 HOH   102 402 1313 HOH   HOH A . 
F 5 HOH   103 403 83   HOH   HOH A . 
F 5 HOH   104 404 58   HOH   HOH A . 
F 5 HOH   105 405 115  HOH   HOH A . 
F 5 HOH   106 406 67   HOH   HOH A . 
F 5 HOH   107 407 121  HOH   HOH A . 
F 5 HOH   108 408 303  HOH   HOH A . 
F 5 HOH   109 409 3    HOH   HOH A . 
F 5 HOH   110 410 1315 HOH   HOH A . 
F 5 HOH   111 411 1068 HOH   HOH A . 
F 5 HOH   112 412 199  HOH   HOH A . 
F 5 HOH   113 413 25   HOH   HOH A . 
F 5 HOH   114 414 68   HOH   HOH A . 
F 5 HOH   115 415 123  HOH   HOH A . 
F 5 HOH   116 416 195  HOH   HOH A . 
F 5 HOH   117 417 125  HOH   HOH A . 
F 5 HOH   118 418 351  HOH   HOH A . 
F 5 HOH   119 419 1296 HOH   HOH A . 
F 5 HOH   120 420 7    HOH   HOH A . 
F 5 HOH   121 421 156  HOH   HOH A . 
F 5 HOH   122 422 278  HOH   HOH A . 
F 5 HOH   123 423 122  HOH   HOH A . 
F 5 HOH   124 424 53   HOH   HOH A . 
F 5 HOH   125 425 1279 HOH   HOH A . 
F 5 HOH   126 426 95   HOH   HOH A . 
F 5 HOH   127 427 70   HOH   HOH A . 
F 5 HOH   128 428 397  HOH   HOH A . 
F 5 HOH   129 429 51   HOH   HOH A . 
F 5 HOH   130 430 582  HOH   HOH A . 
F 5 HOH   131 431 1309 HOH   HOH A . 
F 5 HOH   132 432 1238 HOH   HOH A . 
F 5 HOH   133 433 1222 HOH   HOH A . 
F 5 HOH   134 434 80   HOH   HOH A . 
F 5 HOH   135 435 71   HOH   HOH A . 
F 5 HOH   136 436 16   HOH   HOH A . 
F 5 HOH   137 437 212  HOH   HOH A . 
F 5 HOH   138 438 94   HOH   HOH A . 
F 5 HOH   139 439 188  HOH   HOH A . 
F 5 HOH   140 440 1189 HOH   HOH A . 
F 5 HOH   141 441 73   HOH   HOH A . 
F 5 HOH   142 442 944  HOH   HOH A . 
F 5 HOH   143 443 1286 HOH   HOH A . 
F 5 HOH   144 444 104  HOH   HOH A . 
F 5 HOH   145 445 40   HOH   HOH A . 
F 5 HOH   146 446 97   HOH   HOH A . 
F 5 HOH   147 447 952  HOH   HOH A . 
F 5 HOH   148 448 79   HOH   HOH A . 
F 5 HOH   149 449 576  HOH   HOH A . 
F 5 HOH   150 450 1134 HOH   HOH A . 
F 5 HOH   151 451 330  HOH   HOH A . 
F 5 HOH   152 452 1119 HOH   HOH A . 
F 5 HOH   153 453 107  HOH   HOH A . 
F 5 HOH   154 454 509  HOH   HOH A . 
F 5 HOH   155 455 726  HOH   HOH A . 
F 5 HOH   156 456 163  HOH   HOH A . 
F 5 HOH   157 457 408  HOH   HOH A . 
F 5 HOH   158 458 319  HOH   HOH A . 
F 5 HOH   159 459 756  HOH   HOH A . 
F 5 HOH   160 460 280  HOH   HOH A . 
F 5 HOH   161 461 63   HOH   HOH A . 
F 5 HOH   162 462 126  HOH   HOH A . 
F 5 HOH   163 463 361  HOH   HOH A . 
F 5 HOH   164 464 801  HOH   HOH A . 
F 5 HOH   165 465 556  HOH   HOH A . 
F 5 HOH   166 466 1276 HOH   HOH A . 
F 5 HOH   167 467 250  HOH   HOH A . 
F 5 HOH   168 468 1307 HOH   HOH A . 
F 5 HOH   169 469 370  HOH   HOH A . 
F 5 HOH   170 470 342  HOH   HOH A . 
F 5 HOH   171 471 224  HOH   HOH A . 
F 5 HOH   172 472 135  HOH   HOH A . 
F 5 HOH   173 473 267  HOH   HOH A . 
F 5 HOH   174 474 1287 HOH   HOH A . 
F 5 HOH   175 475 1306 HOH   HOH A . 
F 5 HOH   176 476 695  HOH   HOH A . 
F 5 HOH   177 477 919  HOH   HOH A . 
F 5 HOH   178 478 674  HOH   HOH A . 
F 5 HOH   179 479 202  HOH   HOH A . 
F 5 HOH   180 480 521  HOH   HOH A . 
F 5 HOH   181 481 318  HOH   HOH A . 
F 5 HOH   182 482 805  HOH   HOH A . 
F 5 HOH   183 483 1314 HOH   HOH A . 
F 5 HOH   184 484 331  HOH   HOH A . 
F 5 HOH   185 485 309  HOH   HOH A . 
F 5 HOH   186 486 1299 HOH   HOH A . 
F 5 HOH   187 487 711  HOH   HOH A . 
F 5 HOH   188 488 3    HOH   HOH A . 
F 5 HOH   189 489 941  HOH   HOH A . 
F 5 HOH   190 490 315  HOH   HOH A . 
F 5 HOH   191 491 263  HOH   HOH A . 
F 5 HOH   192 492 152  HOH   HOH A . 
F 5 HOH   193 493 356  HOH   HOH A . 
F 5 HOH   194 494 326  HOH   HOH A . 
F 5 HOH   195 495 208  HOH   HOH A . 
F 5 HOH   196 496 1071 HOH   HOH A . 
F 5 HOH   197 497 180  HOH   HOH A . 
F 5 HOH   198 498 350  HOH   HOH A . 
F 5 HOH   199 499 363  HOH   HOH A . 
F 5 HOH   200 500 1284 HOH   HOH A . 
F 5 HOH   201 501 313  HOH   HOH A . 
F 5 HOH   202 502 371  HOH   HOH A . 
F 5 HOH   203 503 5    HOH   HOH A . 
F 5 HOH   204 504 376  HOH   HOH A . 
F 5 HOH   205 505 4    HOH   HOH A . 
F 5 HOH   206 506 185  HOH   HOH A . 
F 5 HOH   207 507 429  HOH   HOH A . 
F 5 HOH   208 508 70   HOH   HOH A . 
F 5 HOH   209 509 772  HOH   HOH A . 
F 5 HOH   210 510 1074 HOH   HOH A . 
F 5 HOH   211 511 1292 HOH   HOH A . 
F 5 HOH   212 512 346  HOH   HOH A . 
F 5 HOH   213 513 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 1249 HOH   HOH B . 
G 5 HOH   5   205 358  HOH   HOH B . 
G 5 HOH   6   206 758  HOH   HOH B . 
G 5 HOH   7   207 364  HOH   HOH B . 
G 5 HOH   8   208 452  HOH   HOH B . 
G 5 HOH   9   209 120  HOH   HOH B . 
G 5 HOH   10  210 50   HOH   HOH B . 
G 5 HOH   11  211 232  HOH   HOH B . 
G 5 HOH   12  212 654  HOH   HOH B . 
G 5 HOH   13  213 743  HOH   HOH B . 
G 5 HOH   14  214 398  HOH   HOH B . 
G 5 HOH   15  215 900  HOH   HOH B . 
G 5 HOH   16  216 444  HOH   HOH B . 
G 5 HOH   17  217 531  HOH   HOH B . 
G 5 HOH   18  218 264  HOH   HOH B . 
G 5 HOH   19  219 1140 HOH   HOH B . 
G 5 HOH   20  220 1278 HOH   HOH B . 
G 5 HOH   21  221 332  HOH   HOH B . 
G 5 HOH   22  222 353  HOH   HOH B . 
G 5 HOH   23  223 205  HOH   HOH B . 
G 5 HOH   24  224 282  HOH   HOH B . 
G 5 HOH   25  225 343  HOH   HOH B . 
G 5 HOH   26  226 75   HOH   HOH B . 
G 5 HOH   27  227 131  HOH   HOH B . 
G 5 HOH   28  228 82   HOH   HOH B . 
G 5 HOH   29  229 172  HOH   HOH B . 
G 5 HOH   30  230 54   HOH   HOH B . 
G 5 HOH   31  231 60   HOH   HOH B . 
G 5 HOH   32  232 276  HOH   HOH B . 
G 5 HOH   33  233 128  HOH   HOH B . 
G 5 HOH   34  234 69   HOH   HOH B . 
G 5 HOH   35  235 272  HOH   HOH B . 
G 5 HOH   36  236 1    HOH   HOH B . 
G 5 HOH   37  237 325  HOH   HOH B . 
G 5 HOH   38  238 300  HOH   HOH B . 
G 5 HOH   39  239 14   HOH   HOH B . 
G 5 HOH   40  240 231  HOH   HOH B . 
G 5 HOH   41  241 133  HOH   HOH B . 
G 5 HOH   42  242 127  HOH   HOH B . 
G 5 HOH   43  243 1312 HOH   HOH B . 
G 5 HOH   44  244 110  HOH   HOH B . 
G 5 HOH   45  245 30   HOH   HOH B . 
G 5 HOH   46  246 166  HOH   HOH B . 
G 5 HOH   47  247 252  HOH   HOH B . 
G 5 HOH   48  248 181  HOH   HOH B . 
G 5 HOH   49  249 72   HOH   HOH B . 
G 5 HOH   50  250 129  HOH   HOH B . 
G 5 HOH   51  251 9    HOH   HOH B . 
G 5 HOH   52  252 52   HOH   HOH B . 
G 5 HOH   53  253 144  HOH   HOH B . 
G 5 HOH   54  254 723  HOH   HOH B . 
G 5 HOH   55  255 391  HOH   HOH B . 
G 5 HOH   56  256 41   HOH   HOH B . 
G 5 HOH   57  257 31   HOH   HOH B . 
G 5 HOH   58  258 143  HOH   HOH B . 
G 5 HOH   59  259 10   HOH   HOH B . 
G 5 HOH   60  260 150  HOH   HOH B . 
G 5 HOH   61  261 271  HOH   HOH B . 
G 5 HOH   62  262 242  HOH   HOH B . 
G 5 HOH   63  263 302  HOH   HOH B . 
G 5 HOH   64  264 47   HOH   HOH B . 
G 5 HOH   65  265 347  HOH   HOH B . 
G 5 HOH   66  266 59   HOH   HOH B . 
G 5 HOH   67  267 114  HOH   HOH B . 
G 5 HOH   68  268 147  HOH   HOH B . 
G 5 HOH   69  269 221  HOH   HOH B . 
G 5 HOH   70  270 61   HOH   HOH B . 
G 5 HOH   71  271 11   HOH   HOH B . 
G 5 HOH   72  272 117  HOH   HOH B . 
G 5 HOH   73  273 243  HOH   HOH B . 
G 5 HOH   74  274 103  HOH   HOH B . 
G 5 HOH   75  275 287  HOH   HOH B . 
G 5 HOH   76  276 20   HOH   HOH B . 
G 5 HOH   77  277 416  HOH   HOH B . 
G 5 HOH   78  278 84   HOH   HOH B . 
G 5 HOH   79  279 77   HOH   HOH B . 
G 5 HOH   80  280 175  HOH   HOH B . 
G 5 HOH   81  281 43   HOH   HOH B . 
G 5 HOH   82  282 1277 HOH   HOH B . 
G 5 HOH   83  283 1305 HOH   HOH B . 
G 5 HOH   84  284 220  HOH   HOH B . 
G 5 HOH   85  285 216  HOH   HOH B . 
G 5 HOH   86  286 235  HOH   HOH B . 
G 5 HOH   87  287 22   HOH   HOH B . 
G 5 HOH   88  288 99   HOH   HOH B . 
G 5 HOH   89  289 88   HOH   HOH B . 
G 5 HOH   90  290 1066 HOH   HOH B . 
G 5 HOH   91  291 106  HOH   HOH B . 
G 5 HOH   92  292 387  HOH   HOH B . 
G 5 HOH   93  293 89   HOH   HOH B . 
G 5 HOH   94  294 137  HOH   HOH B . 
G 5 HOH   95  295 112  HOH   HOH B . 
G 5 HOH   96  296 311  HOH   HOH B . 
G 5 HOH   97  297 13   HOH   HOH B . 
G 5 HOH   98  298 1106 HOH   HOH B . 
G 5 HOH   99  299 160  HOH   HOH B . 
G 5 HOH   100 300 142  HOH   HOH B . 
G 5 HOH   101 301 118  HOH   HOH B . 
G 5 HOH   102 302 299  HOH   HOH B . 
G 5 HOH   103 303 32   HOH   HOH B . 
G 5 HOH   104 304 316  HOH   HOH B . 
G 5 HOH   105 305 170  HOH   HOH B . 
G 5 HOH   106 306 207  HOH   HOH B . 
G 5 HOH   107 307 215  HOH   HOH B . 
G 5 HOH   108 308 101  HOH   HOH B . 
G 5 HOH   109 309 297  HOH   HOH B . 
G 5 HOH   110 310 37   HOH   HOH B . 
G 5 HOH   111 311 704  HOH   HOH B . 
G 5 HOH   112 312 38   HOH   HOH B . 
G 5 HOH   113 313 635  HOH   HOH B . 
G 5 HOH   114 314 1274 HOH   HOH B . 
G 5 HOH   115 315 1285 HOH   HOH B . 
G 5 HOH   116 316 91   HOH   HOH B . 
G 5 HOH   117 317 177  HOH   HOH B . 
G 5 HOH   118 318 48   HOH   HOH B . 
G 5 HOH   119 319 23   HOH   HOH B . 
G 5 HOH   120 320 161  HOH   HOH B . 
G 5 HOH   121 321 44   HOH   HOH B . 
G 5 HOH   122 322 28   HOH   HOH B . 
G 5 HOH   123 323 1291 HOH   HOH B . 
G 5 HOH   124 324 341  HOH   HOH B . 
G 5 HOH   125 325 197  HOH   HOH B . 
G 5 HOH   126 326 29   HOH   HOH B . 
G 5 HOH   127 327 1294 HOH   HOH B . 
G 5 HOH   128 328 100  HOH   HOH B . 
G 5 HOH   129 329 55   HOH   HOH B . 
G 5 HOH   130 330 182  HOH   HOH B . 
G 5 HOH   131 331 141  HOH   HOH B . 
G 5 HOH   132 332 98   HOH   HOH B . 
G 5 HOH   133 333 334  HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 65   HOH   HOH B . 
G 5 HOH   136 336 445  HOH   HOH B . 
G 5 HOH   137 337 1126 HOH   HOH B . 
G 5 HOH   138 338 234  HOH   HOH B . 
G 5 HOH   139 339 1293 HOH   HOH B . 
G 5 HOH   140 340 960  HOH   HOH B . 
G 5 HOH   141 341 619  HOH   HOH B . 
G 5 HOH   142 342 362  HOH   HOH B . 
G 5 HOH   143 343 339  HOH   HOH B . 
G 5 HOH   144 344 178  HOH   HOH B . 
G 5 HOH   145 345 90   HOH   HOH B . 
G 5 HOH   146 346 87   HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 623  HOH   HOH B . 
G 5 HOH   149 349 191  HOH   HOH B . 
G 5 HOH   150 350 1304 HOH   HOH B . 
G 5 HOH   151 351 1046 HOH   HOH B . 
G 5 HOH   152 352 335  HOH   HOH B . 
G 5 HOH   153 353 1280 HOH   HOH B . 
G 5 HOH   154 354 304  HOH   HOH B . 
G 5 HOH   155 355 203  HOH   HOH B . 
G 5 HOH   156 356 290  HOH   HOH B . 
G 5 HOH   157 357 541  HOH   HOH B . 
G 5 HOH   158 358 1077 HOH   HOH B . 
G 5 HOH   159 359 389  HOH   HOH B . 
G 5 HOH   160 360 718  HOH   HOH B . 
G 5 HOH   161 361 283  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 479  HOH   HOH B . 
G 5 HOH   164 364 1316 HOH   HOH B . 
G 5 HOH   165 365 291  HOH   HOH B . 
G 5 HOH   166 366 373  HOH   HOH B . 
G 5 HOH   167 367 898  HOH   HOH B . 
G 5 HOH   168 368 615  HOH   HOH B . 
G 5 HOH   169 369 340  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 190  HOH   HOH B . 
G 5 HOH   172 372 431  HOH   HOH B . 
G 5 HOH   173 373 310  HOH   HOH B . 
G 5 HOH   174 374 1303 HOH   HOH B . 
G 5 HOH   175 375 149  HOH   HOH B . 
G 5 HOH   176 376 1173 HOH   HOH B . 
G 5 HOH   177 377 183  HOH   HOH B . 
G 5 HOH   178 378 1000 HOH   HOH B . 
G 5 HOH   179 379 418  HOH   HOH B . 
G 5 HOH   180 380 1163 HOH   HOH B . 
G 5 HOH   181 381 1311 HOH   HOH B . 
G 5 HOH   182 382 176  HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 981  HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 470  HOH   HOH B . 
G 5 HOH   187 387 265  HOH   HOH B . 
G 5 HOH   188 388 1298 HOH   HOH B . 
G 5 HOH   189 389 248  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 355  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 314  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 566  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 792  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDA 
_cell.length_a           88.867 
_cell.length_b           88.867 
_cell.length_c           39.511 
_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                         7HDA 
_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          7HDA 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.78 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.430 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156353 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.900 
_reflns.B_iso_Wilson_estimate        12.050 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.048 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1015217 
_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  ? 41866 7491 ? 1.520 ? ? ? 5.600 ? 0.900  ? ? ? ? ? ? 96.500 1.679 0.696 0.604 
1 2 5.590 44.430 ? 7156  1038 ? 0.029 ? ? ? 6.900 ? 59.700 ? ? ? ? ? ? 99.900 0.031 0.012 0.999 
# 
_refine.entry_id                                 7HDA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4300 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7000 
_refine.ls_number_reflns_obs                     156263 
_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                          0.1467 
_refine.ls_R_factor_R_work                       0.1459 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1614 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7539 
_refine.ls_number_reflns_R_work                  148724 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.6776 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                68.110 
_refine.B_iso_min                                8.770 
_refine.pdbx_overall_phase_error                 18.6000 
_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                        44.4300 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.number_atoms_solvent             413 
_refine_hist.number_atoms_total               2996 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           18.27 
_refine_hist.pdbx_B_iso_mean_solvent          30.09 
_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 95.0000  4715 . 0.3906 0.3948 . 199 0.0000 4914 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4945 . 0.3284 0.2973 . 279 0.0000 5224 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4919 . 0.2799 0.2960 . 272 0.0000 5191 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4894 . 0.2686 0.2884 . 272 0.0000 5166 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4922 . 0.2456 0.2643 . 247 0.0000 5169 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4977 . 0.2225 0.2491 . 236 0.0000 5213 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4892 . 0.2004 0.2172 . 267 0.0000 5159 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5015 . 0.1899 0.2097 . 221 0.0000 5236 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4907 . 0.1770 0.2006 . 242 0.0000 5149 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4997 . 0.1587 0.1767 . 250 0.0000 5247 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4944 . 0.1470 0.1723 . 254 0.0000 5198 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4887 . 0.1365 0.1649 . 266 0.0000 5153 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5011 . 0.1304 0.1547 . 225 0.0000 5236 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4929 . 0.1336 0.1493 . 248 0.0000 5177 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4946 . 0.1348 0.1590 . 251 0.0000 5197 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4981 . 0.1325 0.1553 . 268 0.0000 5249 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4937 . 0.1350 0.1573 . 242 0.0000 5179 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4924 . 0.1339 0.1680 . 264 0.0000 5188 . 'X-RAY DIFFRACTION' 
1.3900 1.4300  30 100.0000 4999 . 0.1306 0.1696 . 234 0.0000 5233 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4957 . 0.1262 0.1377 . 252 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4987 . 0.1194 0.1292 . 239 0.0000 5226 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4967 . 0.1190 0.1372 . 265 0.0000 5232 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4929 . 0.1191 0.1312 . 262 0.0000 5191 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5031 . 0.1279 0.1411 . 203 0.0000 5234 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4949 . 0.1312 0.1480 . 290 0.0000 5239 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4997 . 0.1337 0.1360 . 248 0.0000 5245 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4957 . 0.1370 0.1461 . 287 0.0000 5244 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5017 . 0.1378 0.1419 . 252 0.0000 5269 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5017 . 0.1496 0.1637 . 253 0.0000 5270 . 'X-RAY DIFFRACTION' 
3.1700 44.4300 30 100.0000 5175 . 0.1499 0.1746 . 251 0.0000 5426 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDA 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003715' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDA 
_struct_keywords.pdbx_keywords   'Viral Protein, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HDA A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDA 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 7HDA SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDA MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDA SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDA MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    217 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    325 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
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  ? ? 55.81 -133.25 
2 1 SER A 128 ? B 67.14 -4.59   
3 1 HIS B 86  ? ? 57.80 -127.56 
# 
_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 511 ? 5.91 . 
2 1 O ? A HOH 512 ? 6.01 . 
3 1 O ? A HOH 513 ? 7.65 . 
4 1 O ? B HOH 400 ? 6.51 . 
# 
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 
A1A7Z N2   N  Y N 1   
A1A7Z C3   C  Y N 2   
A1A7Z C6   C  Y N 3   
A1A7Z C9   C  Y N 4   
A1A7Z C12  C  Y N 5   
A1A7Z C14  C  Y N 6   
A1A7Z C1   C  N N 7   
A1A7Z C10  C  Y N 8   
A1A7Z C11  C  Y N 9   
A1A7Z C13  C  Y N 10  
A1A7Z C2   C  N S 11  
A1A7Z C4   C  Y N 12  
A1A7Z C5   C  Y N 13  
A1A7Z C7   C  Y N 14  
A1A7Z C8   C  Y N 15  
A1A7Z N1   N  N N 16  
A1A7Z N3   N  Y N 17  
A1A7Z N4   N  Y N 18  
A1A7Z O1   O  N N 19  
A1A7Z H12  H  N N 20  
A1A7Z H14  H  N N 21  
A1A7Z H4   H  N N 22  
A1A7Z H3   H  N N 23  
A1A7Z H10  H  N N 24  
A1A7Z H11  H  N N 25  
A1A7Z H13  H  N N 26  
A1A7Z H1   H  N N 27  
A1A7Z H6   H  N N 28  
A1A7Z H7   H  N N 29  
A1A7Z H8   H  N N 30  
A1A7Z H5   H  N N 31  
A1A7Z H9   H  N N 32  
A1A7Z H2   H  N N 33  
ALA   N    N  N N 34  
ALA   CA   C  N S 35  
ALA   C    C  N N 36  
ALA   O    O  N N 37  
ALA   CB   C  N N 38  
ALA   OXT  O  N N 39  
ALA   H    H  N N 40  
ALA   H2   H  N N 41  
ALA   HA   H  N N 42  
ALA   HB1  H  N N 43  
ALA   HB2  H  N N 44  
ALA   HB3  H  N N 45  
ALA   HXT  H  N N 46  
ARG   N    N  N N 47  
ARG   CA   C  N S 48  
ARG   C    C  N N 49  
ARG   O    O  N N 50  
ARG   CB   C  N N 51  
ARG   CG   C  N N 52  
ARG   CD   C  N N 53  
ARG   NE   N  N N 54  
ARG   CZ   C  N N 55  
ARG   NH1  N  N N 56  
ARG   NH2  N  N N 57  
ARG   OXT  O  N N 58  
ARG   H    H  N N 59  
ARG   H2   H  N N 60  
ARG   HA   H  N N 61  
ARG   HB2  H  N N 62  
ARG   HB3  H  N N 63  
ARG   HG2  H  N N 64  
ARG   HG3  H  N N 65  
ARG   HD2  H  N N 66  
ARG   HD3  H  N N 67  
ARG   HE   H  N N 68  
ARG   HH11 H  N N 69  
ARG   HH12 H  N N 70  
ARG   HH21 H  N N 71  
ARG   HH22 H  N N 72  
ARG   HXT  H  N N 73  
ASN   N    N  N N 74  
ASN   CA   C  N S 75  
ASN   C    C  N N 76  
ASN   O    O  N N 77  
ASN   CB   C  N N 78  
ASN   CG   C  N N 79  
ASN   OD1  O  N N 80  
ASN   ND2  N  N N 81  
ASN   OXT  O  N N 82  
ASN   H    H  N N 83  
ASN   H2   H  N N 84  
ASN   HA   H  N N 85  
ASN   HB2  H  N N 86  
ASN   HB3  H  N N 87  
ASN   HD21 H  N N 88  
ASN   HD22 H  N N 89  
ASN   HXT  H  N N 90  
ASP   N    N  N N 91  
ASP   CA   C  N S 92  
ASP   C    C  N N 93  
ASP   O    O  N N 94  
ASP   CB   C  N N 95  
ASP   CG   C  N N 96  
ASP   OD1  O  N N 97  
ASP   OD2  O  N N 98  
ASP   OXT  O  N N 99  
ASP   H    H  N N 100 
ASP   H2   H  N N 101 
ASP   HA   H  N N 102 
ASP   HB2  H  N N 103 
ASP   HB3  H  N N 104 
ASP   HD2  H  N N 105 
ASP   HXT  H  N N 106 
CL    CL   CL N N 107 
CYS   N    N  N N 108 
CYS   CA   C  N R 109 
CYS   C    C  N N 110 
CYS   O    O  N N 111 
CYS   CB   C  N N 112 
CYS   SG   S  N N 113 
CYS   OXT  O  N N 114 
CYS   H    H  N N 115 
CYS   H2   H  N N 116 
CYS   HA   H  N N 117 
CYS   HB2  H  N N 118 
CYS   HB3  H  N N 119 
CYS   HG   H  N N 120 
CYS   HXT  H  N N 121 
GLN   N    N  N N 122 
GLN   CA   C  N S 123 
GLN   C    C  N N 124 
GLN   O    O  N N 125 
GLN   CB   C  N N 126 
GLN   CG   C  N N 127 
GLN   CD   C  N N 128 
GLN   OE1  O  N N 129 
GLN   NE2  N  N N 130 
GLN   OXT  O  N N 131 
GLN   H    H  N N 132 
GLN   H2   H  N N 133 
GLN   HA   H  N N 134 
GLN   HB2  H  N N 135 
GLN   HB3  H  N N 136 
GLN   HG2  H  N N 137 
GLN   HG3  H  N N 138 
GLN   HE21 H  N N 139 
GLN   HE22 H  N N 140 
GLN   HXT  H  N N 141 
GLU   N    N  N N 142 
GLU   CA   C  N S 143 
GLU   C    C  N N 144 
GLU   O    O  N N 145 
GLU   CB   C  N N 146 
GLU   CG   C  N N 147 
GLU   CD   C  N N 148 
GLU   OE1  O  N N 149 
GLU   OE2  O  N N 150 
GLU   OXT  O  N N 151 
GLU   H    H  N N 152 
GLU   H2   H  N N 153 
GLU   HA   H  N N 154 
GLU   HB2  H  N N 155 
GLU   HB3  H  N N 156 
GLU   HG2  H  N N 157 
GLU   HG3  H  N N 158 
GLU   HE2  H  N N 159 
GLU   HXT  H  N N 160 
GLY   N    N  N N 161 
GLY   CA   C  N N 162 
GLY   C    C  N N 163 
GLY   O    O  N N 164 
GLY   OXT  O  N N 165 
GLY   H    H  N N 166 
GLY   H2   H  N N 167 
GLY   HA2  H  N N 168 
GLY   HA3  H  N N 169 
GLY   HXT  H  N N 170 
HIS   N    N  N N 171 
HIS   CA   C  N S 172 
HIS   C    C  N N 173 
HIS   O    O  N N 174 
HIS   CB   C  N N 175 
HIS   CG   C  Y N 176 
HIS   ND1  N  Y N 177 
HIS   CD2  C  Y N 178 
HIS   CE1  C  Y N 179 
HIS   NE2  N  Y N 180 
HIS   OXT  O  N N 181 
HIS   H    H  N N 182 
HIS   H2   H  N N 183 
HIS   HA   H  N N 184 
HIS   HB2  H  N N 185 
HIS   HB3  H  N N 186 
HIS   HD1  H  N N 187 
HIS   HD2  H  N N 188 
HIS   HE1  H  N N 189 
HIS   HE2  H  N N 190 
HIS   HXT  H  N N 191 
HOH   O    O  N N 192 
HOH   H1   H  N N 193 
HOH   H2   H  N N 194 
ILE   N    N  N N 195 
ILE   CA   C  N S 196 
ILE   C    C  N N 197 
ILE   O    O  N N 198 
ILE   CB   C  N S 199 
ILE   CG1  C  N N 200 
ILE   CG2  C  N N 201 
ILE   CD1  C  N N 202 
ILE   OXT  O  N N 203 
ILE   H    H  N N 204 
ILE   H2   H  N N 205 
ILE   HA   H  N N 206 
ILE   HB   H  N N 207 
ILE   HG12 H  N N 208 
ILE   HG13 H  N N 209 
ILE   HG21 H  N N 210 
ILE   HG22 H  N N 211 
ILE   HG23 H  N N 212 
ILE   HD11 H  N N 213 
ILE   HD12 H  N N 214 
ILE   HD13 H  N N 215 
ILE   HXT  H  N N 216 
LEU   N    N  N N 217 
LEU   CA   C  N S 218 
LEU   C    C  N N 219 
LEU   O    O  N N 220 
LEU   CB   C  N N 221 
LEU   CG   C  N N 222 
LEU   CD1  C  N N 223 
LEU   CD2  C  N N 224 
LEU   OXT  O  N N 225 
LEU   H    H  N N 226 
LEU   H2   H  N N 227 
LEU   HA   H  N N 228 
LEU   HB2  H  N N 229 
LEU   HB3  H  N N 230 
LEU   HG   H  N N 231 
LEU   HD11 H  N N 232 
LEU   HD12 H  N N 233 
LEU   HD13 H  N N 234 
LEU   HD21 H  N N 235 
LEU   HD22 H  N N 236 
LEU   HD23 H  N N 237 
LEU   HXT  H  N N 238 
LYS   N    N  N N 239 
LYS   CA   C  N S 240 
LYS   C    C  N N 241 
LYS   O    O  N N 242 
LYS   CB   C  N N 243 
LYS   CG   C  N N 244 
LYS   CD   C  N N 245 
LYS   CE   C  N N 246 
LYS   NZ   N  N N 247 
LYS   OXT  O  N N 248 
LYS   H    H  N N 249 
LYS   H2   H  N N 250 
LYS   HA   H  N N 251 
LYS   HB2  H  N N 252 
LYS   HB3  H  N N 253 
LYS   HG2  H  N N 254 
LYS   HG3  H  N N 255 
LYS   HD2  H  N N 256 
LYS   HD3  H  N N 257 
LYS   HE2  H  N N 258 
LYS   HE3  H  N N 259 
LYS   HZ1  H  N N 260 
LYS   HZ2  H  N N 261 
LYS   HZ3  H  N N 262 
LYS   HXT  H  N N 263 
MET   N    N  N N 264 
MET   CA   C  N S 265 
MET   C    C  N N 266 
MET   O    O  N N 267 
MET   CB   C  N N 268 
MET   CG   C  N N 269 
MET   SD   S  N N 270 
MET   CE   C  N N 271 
MET   OXT  O  N N 272 
MET   H    H  N N 273 
MET   H2   H  N N 274 
MET   HA   H  N N 275 
MET   HB2  H  N N 276 
MET   HB3  H  N N 277 
MET   HG2  H  N N 278 
MET   HG3  H  N N 279 
MET   HE1  H  N N 280 
MET   HE2  H  N N 281 
MET   HE3  H  N N 282 
MET   HXT  H  N N 283 
PHE   N    N  N N 284 
PHE   CA   C  N S 285 
PHE   C    C  N N 286 
PHE   O    O  N N 287 
PHE   CB   C  N N 288 
PHE   CG   C  Y N 289 
PHE   CD1  C  Y N 290 
PHE   CD2  C  Y N 291 
PHE   CE1  C  Y N 292 
PHE   CE2  C  Y N 293 
PHE   CZ   C  Y N 294 
PHE   OXT  O  N N 295 
PHE   H    H  N N 296 
PHE   H2   H  N N 297 
PHE   HA   H  N N 298 
PHE   HB2  H  N N 299 
PHE   HB3  H  N N 300 
PHE   HD1  H  N N 301 
PHE   HD2  H  N N 302 
PHE   HE1  H  N N 303 
PHE   HE2  H  N N 304 
PHE   HZ   H  N N 305 
PHE   HXT  H  N N 306 
PRO   N    N  N N 307 
PRO   CA   C  N S 308 
PRO   C    C  N N 309 
PRO   O    O  N N 310 
PRO   CB   C  N N 311 
PRO   CG   C  N N 312 
PRO   CD   C  N N 313 
PRO   OXT  O  N N 314 
PRO   H    H  N N 315 
PRO   HA   H  N N 316 
PRO   HB2  H  N N 317 
PRO   HB3  H  N N 318 
PRO   HG2  H  N N 319 
PRO   HG3  H  N N 320 
PRO   HD2  H  N N 321 
PRO   HD3  H  N N 322 
PRO   HXT  H  N N 323 
SER   N    N  N N 324 
SER   CA   C  N S 325 
SER   C    C  N N 326 
SER   O    O  N N 327 
SER   CB   C  N N 328 
SER   OG   O  N N 329 
SER   OXT  O  N N 330 
SER   H    H  N N 331 
SER   H2   H  N N 332 
SER   HA   H  N N 333 
SER   HB2  H  N N 334 
SER   HB3  H  N N 335 
SER   HG   H  N N 336 
SER   HXT  H  N N 337 
TFA   C1   C  N N 338 
TFA   C2   C  N N 339 
TFA   O    O  N N 340 
TFA   F1   F  N N 341 
TFA   F2   F  N N 342 
TFA   F3   F  N N 343 
TFA   OXT  O  N N 344 
TFA   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TYR   N    N  N N 363 
TYR   CA   C  N S 364 
TYR   C    C  N N 365 
TYR   O    O  N N 366 
TYR   CB   C  N N 367 
TYR   CG   C  Y N 368 
TYR   CD1  C  Y N 369 
TYR   CD2  C  Y N 370 
TYR   CE1  C  Y N 371 
TYR   CE2  C  Y N 372 
TYR   CZ   C  Y N 373 
TYR   OH   O  N N 374 
TYR   OXT  O  N N 375 
TYR   H    H  N N 376 
TYR   H2   H  N N 377 
TYR   HA   H  N N 378 
TYR   HB2  H  N N 379 
TYR   HB3  H  N N 380 
TYR   HD1  H  N N 381 
TYR   HD2  H  N N 382 
TYR   HE1  H  N N 383 
TYR   HE2  H  N N 384 
TYR   HH   H  N N 385 
TYR   HXT  H  N N 386 
VAL   N    N  N N 387 
VAL   CA   C  N S 388 
VAL   C    C  N N 389 
VAL   O    O  N N 390 
VAL   CB   C  N N 391 
VAL   CG1  C  N N 392 
VAL   CG2  C  N N 393 
VAL   OXT  O  N N 394 
VAL   H    H  N N 395 
VAL   H2   H  N N 396 
VAL   HA   H  N N 397 
VAL   HB   H  N N 398 
VAL   HG11 H  N N 399 
VAL   HG12 H  N N 400 
VAL   HG13 H  N N 401 
VAL   HG21 H  N N 402 
VAL   HG22 H  N N 403 
VAL   HG23 H  N N 404 
VAL   HXT  H  N N 405 
# 
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 
A1A7Z C12 C11  doub Y N 1   
A1A7Z C12 C13  sing Y N 2   
A1A7Z C11 C10  sing Y N 3   
A1A7Z C13 C14  doub Y N 4   
A1A7Z C1  O1   sing N N 5   
A1A7Z C1  C2   sing N N 6   
A1A7Z C10 C9   doub Y N 7   
A1A7Z C14 C9   sing Y N 8   
A1A7Z C9  C2   sing N N 9   
A1A7Z C2  N1   sing N N 10  
A1A7Z N1  C3   sing N N 11  
A1A7Z C3  C6   doub Y N 12  
A1A7Z C3  N2   sing Y N 13  
A1A7Z C7  C6   sing Y N 14  
A1A7Z C7  C8   doub Y N 15  
A1A7Z C6  C5   sing Y N 16  
A1A7Z N2  C4   doub Y N 17  
A1A7Z C8  N4   sing Y N 18  
A1A7Z C5  N4   sing Y N 19  
A1A7Z C5  N3   doub Y N 20  
A1A7Z C4  N3   sing Y N 21  
A1A7Z C12 H12  sing N N 22  
A1A7Z C14 H14  sing N N 23  
A1A7Z C1  H4   sing N N 24  
A1A7Z C1  H3   sing N N 25  
A1A7Z C10 H10  sing N N 26  
A1A7Z C11 H11  sing N N 27  
A1A7Z C13 H13  sing N N 28  
A1A7Z C2  H1   sing N N 29  
A1A7Z C4  H6   sing N N 30  
A1A7Z C7  H7   sing N N 31  
A1A7Z C8  H8   sing N N 32  
A1A7Z N1  H5   sing N N 33  
A1A7Z N4  H9   sing N N 34  
A1A7Z O1  H2   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
TFA   C1  C2   sing N N 325 
TFA   C1  O    doub N N 326 
TFA   C1  OXT  sing N N 327 
TFA   C2  F1   sing N N 328 
TFA   C2  F2   sing N N 329 
TFA   C2  F3   sing N N 330 
TFA   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TYR   N   CA   sing N N 348 
TYR   N   H    sing N N 349 
TYR   N   H2   sing N N 350 
TYR   CA  C    sing N N 351 
TYR   CA  CB   sing N N 352 
TYR   CA  HA   sing N N 353 
TYR   C   O    doub N N 354 
TYR   C   OXT  sing N N 355 
TYR   CB  CG   sing N N 356 
TYR   CB  HB2  sing N N 357 
TYR   CB  HB3  sing N N 358 
TYR   CG  CD1  doub Y N 359 
TYR   CG  CD2  sing Y N 360 
TYR   CD1 CE1  sing Y N 361 
TYR   CD1 HD1  sing N N 362 
TYR   CD2 CE2  doub Y N 363 
TYR   CD2 HD2  sing N N 364 
TYR   CE1 CZ   doub Y N 365 
TYR   CE1 HE1  sing N N 366 
TYR   CE2 CZ   sing Y N 367 
TYR   CE2 HE2  sing N N 368 
TYR   CZ  OH   sing N N 369 
TYR   OH  HH   sing N N 370 
TYR   OXT HXT  sing N N 371 
VAL   N   CA   sing N N 372 
VAL   N   H    sing N N 373 
VAL   N   H2   sing N N 374 
VAL   CA  C    sing N N 375 
VAL   CA  CB   sing N N 376 
VAL   CA  HA   sing N N 377 
VAL   C   O    doub N N 378 
VAL   C   OXT  sing N N 379 
VAL   CB  CG1  sing N N 380 
VAL   CB  CG2  sing N N 381 
VAL   CB  HB   sing N N 382 
VAL   CG1 HG11 sing N N 383 
VAL   CG1 HG12 sing N N 384 
VAL   CG1 HG13 sing N N 385 
VAL   CG2 HG21 sing N N 386 
VAL   CG2 HG22 sing N N 387 
VAL   CG2 HG23 sing N N 388 
VAL   OXT HXT  sing N N 389 
# 
_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                    7HDA 
_atom_sites.fract_transf_matrix[1][1]   0.011253 
_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]   0.011253 
_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]   0.025309 
_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   ? 19.652 -16.161 22.228  0.64 54.80 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.570 -16.149 22.325  0.36 54.06 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.667 -15.101 22.398  0.64 54.33 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.619 -15.056 22.486  0.36 53.69 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.301 -13.743 22.110  0.64 52.78 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.282 -13.727 22.144  0.36 52.39 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.411 -13.460 22.561  0.64 53.29 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.397 -13.448 22.586  0.36 52.83 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.040 -15.142 23.807  0.64 55.02 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.032 -15.031 23.911  0.36 54.29 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.007 -14.035 23.964  0.64 55.20 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.013 -13.908 24.047  0.36 54.46 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.409 -16.503 24.068  0.64 55.24 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.402 -16.373 24.253  0.36 54.48 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.953 -15.233 21.759  0.64 65.20 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.883 -15.188 21.871  0.36 64.43 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.734 -15.002 24.469  0.64 66.02 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.746 -14.865 24.545  0.36 65.15 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.508 -14.186 24.782  0.64 66.24 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.540 -14.013 24.887  0.36 65.35 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.462 -13.180 24.008  0.64 66.24 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.476 -13.056 24.034  0.36 65.35 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.406 -14.055 23.203  0.64 66.24 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.387 -13.958 23.307  0.36 65.35 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.958 -16.482 24.927  0.64 66.29 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.964 -16.305 25.116  0.36 65.38 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.770 -16.695 23.364  0.64 66.29 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.752 -16.600 23.569  0.36 65.38 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.105 -17.178 24.076  0.64 66.29 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.097 -17.049 24.287  0.36 65.38 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.591 -12.909 21.352  1.00 50.20 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.042 -11.562 21.020  1.00 44.91 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.908 -10.575 21.293  1.00 40.00 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.806 -10.959 21.698  1.00 40.15 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.590 -11.467 19.588  1.00 44.27 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.572 -11.856 18.540  1.00 43.46 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.445 -11.361 18.535  1.00 43.09 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 18.967 -12.752 17.640  1.00 43.24 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.826 -13.110 21.012  0.64 60.24 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.839 -13.120 20.990  0.36 60.24 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.770 -11.334 21.610  1.00 53.89 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.864 -10.550 19.416  1.00 53.12 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.352 -12.060 19.502  1.00 53.12 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.429 -13.006 17.020  1.00 51.88 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.764 -13.077 17.677  1.00 51.88 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.171 -9.292  21.046  0.64 37.21 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.198 -9.292  21.083  0.36 37.51 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.262 -8.220  21.432  0.64 34.35 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.284 -8.213  21.430  0.36 34.91 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.405 -7.700  20.280  0.64 30.87 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.403 -7.780  20.264  0.36 31.79 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.779 -6.644  20.419  0.64 31.22 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.649 -6.811  20.401  0.36 31.93 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.040 -7.065  22.066  0.64 34.98 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.061 -7.014  21.984  0.36 35.36 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.015 -6.559  21.172  0.64 35.42 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 18.945 -6.482  21.013  0.36 35.63 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 18.880 -9.018  20.644  0.64 44.66 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 18.932 -9.021  20.726  0.36 45.02 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.663 -8.563  22.114  0.64 41.22 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.697 -8.522  22.133  0.36 41.89 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.420 -6.352  22.291  0.64 41.97 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.432 -6.325  22.250  0.36 42.43 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.480 -7.383  22.871  0.64 41.97 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.577 -7.303  22.755  0.36 42.43 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.436 -5.928  21.536  0.64 42.50 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.363 -5.827  21.335  0.36 42.75 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.361 -8.402  19.150  0.64 26.76 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.478 -8.467  19.127  0.36 28.44 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.461 -8.010  18.072  0.64 22.55 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.555 -8.202  18.032  0.36 25.11 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.021 -8.348  18.445  0.64 21.74 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.182 -8.744  18.401  0.36 24.08 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.748 -9.407  19.011  0.64 22.57 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 14.023 -9.953  18.605  0.36 24.05 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.840 -8.731  16.782  0.64 19.95 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 16.044 -8.886  16.760  0.36 23.07 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.114 -8.227  16.155  0.64 18.47 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.353 -8.361  16.247  0.36 21.51 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.113 -7.074  15.392  0.64 17.89 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.424 -7.127  15.627  0.36 20.67 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.303 -8.916  16.320  0.64 18.79 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.509 -9.114  16.367  0.36 21.37 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.279 -6.608  14.809  0.64 18.02 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.628 -6.645  15.147  0.36 20.50 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.469 -8.459  15.739  0.64 18.89 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.715 -8.639  15.888  0.36 21.10 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.457 -7.302  14.984  0.64 18.37 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.774 -7.403  15.277  0.36 20.76 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.835 -9.101  18.987  0.64 32.11 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 17.050 -9.091  18.968  0.36 34.12 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.522 -7.059  17.931  0.64 27.06 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.488 -7.248  17.877  0.36 30.13 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 15.952 -9.677  16.975  0.64 23.94 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 16.153 -9.834  16.940  0.36 27.69 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.121 -8.614  16.140  0.64 23.94 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.380 -8.759  16.065  0.36 27.69 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.316 -6.604  15.272  0.64 21.47 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.654 -6.613  15.539  0.36 24.80 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.314 -9.696  16.832  0.64 22.54 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.474 -9.949  16.779  0.36 25.64 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.263 -5.830  14.299  0.64 21.62 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.666 -5.812  14.735  0.36 24.60 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.262 -8.926  15.861  0.64 22.67 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.486 -9.152  15.977  0.36 25.32 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.239 -6.990  14.592  0.64 22.04 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.585 -7.081  14.954  0.36 24.91 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.092 -7.446  18.118  0.64 20.20 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.186 -7.864  18.481  0.36 23.40 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.711 -7.553  18.582  0.64 20.03 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 11.835 -8.281  18.827  0.36 22.82 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.727 -7.354  17.434  0.64 18.32 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 10.839 -7.652  17.864  0.36 21.47 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 10.931 -6.500  16.567  0.64 17.87 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 11.086 -6.586  17.293  0.36 21.64 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.439 -6.516  19.681  0.64 21.88 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.468 -7.925  20.277  0.36 23.77 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.135 -6.662  20.215  0.64 23.40 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 11.056 -6.574  20.392  0.36 24.23 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.242 -6.762  17.621  0.64 24.24 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.268 -7.018  18.328  0.36 28.08 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.565 -8.433  18.957  0.64 24.04 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.768 -9.241  18.733  0.36 27.39 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.090 -6.634  20.394  0.64 26.26 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 10.752 -8.518  20.571  0.36 28.53 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.526 -5.626  19.304  0.64 26.26 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 12.247 -8.053  20.840  0.36 28.53 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.008 -6.090  20.817  0.64 28.08 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.831 -6.416  21.186  0.36 29.08 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.650  -8.142  17.441  0.64 17.44 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 9.711  -8.336  17.682  0.36 19.89 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.565  -7.956  16.496  0.64 16.58 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.676  -7.885  16.780  0.36 18.38 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.807  -8.475  15.097  0.64 15.55 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 8.816  -8.377  15.359  0.36 16.75 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.107  -8.056  14.168  0.64 16.35 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 7.983  -8.022  14.515  0.36 16.90 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.527  -8.786  17.998  0.64 20.93 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.530  -9.080  18.071  0.36 23.87 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.775  -8.394  16.846  0.64 19.90 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 7.816  -8.184  17.111  0.36 22.06 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.374  -7.008  16.428  0.64 19.90 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.673  -6.917  16.758  0.36 22.06 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.767  -9.380  14.911  0.64 14.71 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 9.832  -9.184  15.067  0.36 15.42 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.071 -9.920  13.593  0.64 13.68 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.029 -9.691  13.721  0.36 14.27 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.237  -11.163 13.309  0.64 12.68 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.138  -10.896 13.468  0.36 13.21 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 9.028  -12.007 14.186  0.64 13.48 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 8.810  -11.662 14.380  0.36 14.04 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.561 -10.269 13.471  0.64 14.13 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.485 -10.112 13.504  0.36 14.59 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.456 -9.056  13.312  0.64 14.58 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.432 -8.951  13.341  0.36 15.04 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.787 -8.273  14.406  0.64 15.30 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 12.765 -8.154  14.423  0.36 15.60 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 12.942 -8.685  12.066  0.64 14.37 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 12.985 -8.650  12.105  0.36 14.83 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.587 -7.151  14.268  0.64 16.02 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.623 -7.086  14.283  0.36 16.01 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.741 -7.567  11.915  0.64 14.82 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.843 -7.583  11.952  0.36 15.17 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.059 -6.802  13.018  0.64 15.71 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.159 -6.803  13.044  0.36 15.96 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 14.850 -5.688  12.864  0.64 16.86 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 15.015 -5.740  12.895  0.36 16.89 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.253 -9.708  15.540  0.64 17.65 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.417 -9.463  15.635  0.36 18.51 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.861  -9.259  12.920  0.64 16.42 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 9.809  -9.001  13.077  0.36 17.12 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.843 -10.756 14.263  0.64 16.96 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 11.779 -10.633 14.268  0.36 17.51 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.671 -10.826 12.685  0.64 16.96 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.536 -10.654 12.699  0.36 17.51 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.462 -8.507  15.249  0.64 18.36 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.399 -8.346  15.258  0.36 18.72 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.726 -9.195  11.319  0.64 17.25 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.771 -9.174  11.366  0.36 17.80 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.803 -6.637  15.013  0.64 19.23 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 13.835 -6.562  15.019  0.36 19.21 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.066 -7.329  11.075  0.64 17.78 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.209 -7.390  11.120  0.36 18.20 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 14.984 -5.323  13.610  0.64 20.23 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 15.121 -5.362  13.636  0.36 20.27 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.779  -11.272 12.066  0.64 12.72 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 8.744  -11.050 12.211  0.36 12.42 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.203  -12.510 11.560  0.64 12.63 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.076  -12.255 11.753  0.36 12.24 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.338  -13.439 11.136  0.64 12.24 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.143  -13.232 11.269  0.36 12.12 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.323 -12.999 10.537  0.64 12.23 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 9.992  -12.876 10.444  0.36 12.12 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.317  -12.193 10.356  0.64 13.30 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.109  -11.918 10.619  0.36 12.84 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.632  -13.361 9.652   0.64 14.98 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.288  -13.120 10.162  0.36 14.17 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.586  -13.975 10.558  0.64 16.27 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.399  -13.600 11.298  0.36 15.15 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 6.014  -12.902 8.339   0.64 16.03 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 5.454  -12.766 8.947   0.36 15.35 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.803  -10.641 11.478  0.64 15.27 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 8.860  -10.464 11.589  0.36 14.90 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.668  -12.941 12.248  0.64 15.16 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.580  -12.654 12.486  0.36 14.69 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.615  -11.593 10.645  0.64 15.96 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.486  -11.229 10.920  0.36 15.41 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.863  -11.750 9.690   0.64 15.96 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.612  -11.589 9.856   0.36 15.41 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.290  -14.047 9.448   0.64 17.98 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 6.890  -13.841 9.920   0.36 17.01 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.194  -14.747 10.118  0.64 19.52 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 4.790  -14.270 10.955  0.36 18.18 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 6.007  -14.250 11.388  0.64 19.52 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 5.948  -13.982 11.999  0.36 18.18 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.899  -13.315 10.741  0.64 19.52 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 4.897  -12.846 11.646  0.36 18.18 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.582  -13.659 7.913   0.64 19.23 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 4.948  -13.546 8.677   0.36 18.42 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.363  -12.210 8.526   0.64 19.23 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 4.851  -12.042 9.179   0.36 18.42 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.716  -12.556 7.768   0.64 19.23 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.045  -12.487 8.230   0.36 18.42 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.209  -14.724 11.463  0.64 12.16 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.116  -14.449 11.803  0.36 11.77 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.223 -15.726 11.152  0.64 12.22 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.073 -15.475 11.410  0.36 11.58 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.883  -16.354 9.806   0.64 12.41 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.693  -16.014 10.036  0.36 10.90 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.835  -16.990 9.668   0.64 14.10 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.566  -16.482 9.837   0.36 10.93 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.266 -16.776 12.266  0.64 12.09 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.087 -16.598 12.445  0.36 12.08 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.299 -17.882 12.106  0.64 12.36 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.057 -17.731 12.136  0.36 12.58 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.400 -18.699 13.400  0.64 13.00 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.114 -18.727 13.287  0.36 13.60 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.390 -19.852 13.304  0.64 12.80 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.101 -19.861 13.034  0.36 13.70 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.767 -19.383 12.995  0.64 13.38 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.512 -19.387 12.937  0.36 14.12 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.519  -15.053 11.864  0.64 14.60 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.546  -14.706 12.395  0.36 14.13 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.093 -15.304 11.086  0.64 14.66 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 10.961 -15.084 11.353  0.36 13.90 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.463 -16.320 13.101  0.64 14.51 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.337 -16.219 13.303  0.36 14.50 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.399  -17.197 12.324  0.64 14.51 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.197  -16.975 12.500  0.36 14.50 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 11.032 -18.475 11.387  0.64 14.84 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 10.763 -18.201 11.340  0.36 15.10 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.169 -17.494 11.922  0.64 14.84 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 11.947 -17.367 12.003  0.36 15.10 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.684 -18.118 14.122  0.64 15.60 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.387 -18.265 14.094  0.36 16.32 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.525 -19.074 13.605  0.64 15.60 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.234 -19.118 13.410  0.36 16.32 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.415 -20.324 14.154  0.64 15.36 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.049 -20.497 13.766  0.36 16.44 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 12.110 -20.456 12.599  0.64 15.36 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 11.874 -20.299 12.198  0.36 16.44 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.308 -20.082 12.880  0.64 16.06 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.053 -20.073 12.757  0.36 16.95 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.763 -18.896 12.252  0.64 16.06 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.588 -18.784 12.288  0.36 16.95 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.079 -18.888 13.665  0.64 16.06 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 13.764 -19.018 13.707  0.36 16.95 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.757 -16.177 8.809   0.64 11.71 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.622 -15.934 9.083   0.36 11.32 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.512 -16.770 7.496   0.64 11.87 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.403 -16.471 7.744   0.36 11.64 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.115 -18.161 7.362   0.64 12.01 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 10.977 -17.873 7.572   0.36 11.94 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.501 -19.045 6.754   0.64 12.36 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.317 -18.746 7.001   0.36 11.95 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.052 -15.879 6.371   0.64 12.07 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 10.984 -15.533 6.676   0.36 12.27 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.401 -14.508 6.189   0.64 12.86 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.330 -14.155 6.563   0.36 12.91 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.181 -13.701 5.170   0.64 13.55 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.816 -13.436 5.314   0.36 13.13 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.933  -14.651 5.773   0.64 13.11 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.815  -14.277 6.558   0.36 13.26 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.489 -15.716 8.862   0.64 14.06 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.387 -15.547 9.183   0.36 13.58 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.556  -16.858 7.376   0.64 14.25 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.447  -16.535 7.592   0.36 13.97 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 11.993 -15.736 6.530   0.64 14.48 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.923 -15.392 6.869   0.36 14.72 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 10.939 -16.366 5.535   0.64 14.48 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.894 -15.965 5.810   0.36 14.72 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.425 -14.036 7.033   0.64 15.43 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.585 -13.622 7.333   0.36 15.50 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.759 -12.835 5.063   0.64 16.27 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.395 -12.562 5.270   0.36 15.76 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.092 -13.588 5.489   0.64 16.27 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.779 -13.337 5.361   0.36 15.76 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.186 -14.175 4.324   0.64 16.27 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.573 -13.959 4.534   0.36 15.76 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.537  -13.771 5.701   0.64 15.73 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.433  -13.441 6.251   0.36 15.91 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.889  -15.103 4.915   0.64 15.73 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.560  -14.999 5.965   0.36 15.91 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.457  -15.173 6.442   0.64 15.73 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.512  -14.467 7.461   0.36 15.91 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.320 -18.356 7.891   0.64 12.04 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.204 -18.099 8.036   0.36 12.06 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.018 -19.631 7.830   0.64 12.24 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.864 -19.395 7.927   0.36 12.45 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.772 -19.820 9.137   0.64 12.73 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.648 -19.652 9.211   0.36 12.87 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.679 -19.006 10.060  0.64 12.87 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.526 -18.926 10.204  0.36 13.17 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 14.017 -19.678 6.666   0.64 13.00 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.807 -19.441 6.714   0.36 12.78 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.091 -18.774 6.941   0.64 13.17 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.838 -18.463 6.885   0.36 12.92 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.366 -19.316 5.345   0.64 14.14 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 13.067 -19.182 5.403   0.36 13.53 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.770 -17.746 8.296   0.64 14.45 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.683 -17.498 8.412   0.36 14.48 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.382 -20.356 7.725   0.64 14.69 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.195 -20.091 7.823   0.36 14.94 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.371 -20.580 6.583   0.64 15.60 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.211 -20.321 6.654   0.36 15.33 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.773 -19.205 7.183   0.64 15.80 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.360 -18.477 6.226   0.36 15.50 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 13.984 -19.484 4.615   0.64 16.96 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.681 -19.275 4.652   0.36 16.24 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.571 -19.856 5.210   0.64 16.96 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.347 -19.823 5.294   0.36 16.24 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.118 -18.382 5.342   0.64 16.96 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.700 -18.287 5.397   0.36 16.24 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.575 -20.882 9.190   0.64 13.17 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.487 -20.689 9.166   0.36 13.46 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.415 -21.106 10.356  0.64 14.36 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.321 -21.049 10.306  0.36 14.12 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.197 -19.853 10.741  0.64 13.80 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.258 -19.919 10.708  0.36 13.53 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.354 -19.554 11.930  0.64 14.29 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.610 -19.795 11.887  0.36 13.75 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.379 -22.256 10.085  0.64 16.90 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.140 -22.292 9.955   0.36 15.82 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.350 -22.452 11.217  0.64 20.81 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.038 -22.747 11.093  0.36 17.40 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.922 -22.893 12.302  0.64 22.64 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.505 -23.076 12.175  0.36 18.01 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.538 -22.128 11.026  0.64 22.87 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.271 -22.803 10.899  0.36 18.31 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.665 -21.475 8.568   0.64 15.81 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.589 -21.188 8.479   0.36 16.15 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.857 -21.363 11.109  0.64 17.24 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.752 -21.257 11.062  0.36 16.95 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.867 -23.080 9.940   0.64 20.28 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.532 -23.021 9.763   0.36 18.99 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.905 -22.063 9.296   0.64 20.28 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.681 -22.096 9.172   0.36 18.99 ?  14  ASP   A HB3  1 
ATOM   358  N  N    . ASN   A 1 15  ? 16.679 -19.093 9.750   1.00 13.30 ?  15  ASN   A N    1 
ATOM   359  C  CA   . ASN   A 1 15  ? 17.661 -18.047 10.012  1.00 13.81 ?  15  ASN   A CA   1 
ATOM   360  C  C    . ASN   A 1 15  ? 17.292 -16.657 9.505   1.00 13.79 ?  15  ASN   A C    1 
ATOM   361  O  O    . ASN   A 1 15  ? 18.064 -15.723 9.740   1.00 15.16 ?  15  ASN   A O    1 
ATOM   362  C  CB   . ASN   A 1 15  ? 19.037 -18.445 9.440   1.00 13.56 ?  15  ASN   A CB   1 
ATOM   363  C  CG   . ASN   A 1 15  ? 19.030 -18.543 7.929   1.00 14.02 ?  15  ASN   A CG   1 
ATOM   364  O  OD1  . ASN   A 1 15  ? 18.318 -19.366 7.346   1.00 14.61 ?  15  ASN   A OD1  1 
ATOM   365  N  ND2  . ASN   A 1 15  ? 19.817 -17.690 7.281   1.00 14.01 ?  15  ASN   A ND2  1 
ATOM   366  H  H    A ASN   A 1 15  ? 16.445 -19.162 8.930   0.64 15.96 ?  15  ASN   A H    1 
ATOM   367  H  H    B ASN   A 1 15  ? 16.400 -19.115 8.941   0.36 15.96 ?  15  ASN   A H    1 
ATOM   368  H  HA   . ASN   A 1 15  ? 17.775 -17.967 10.970  1.00 16.57 ?  15  ASN   A HA   1 
ATOM   369  H  HB2  . ASN   A 1 15  ? 19.694 -17.772 9.699   1.00 16.28 ?  15  ASN   A HB2  1 
ATOM   370  H  HB3  . ASN   A 1 15  ? 19.296 -19.308 9.800   1.00 16.28 ?  15  ASN   A HB3  1 
ATOM   371  H  HD21 . ASN   A 1 15  ? 19.846 -17.700 6.422   1.00 16.81 ?  15  ASN   A HD21 1 
ATOM   372  H  HD22 . ASN   A 1 15  ? 20.298 -17.120 7.717   1.00 16.81 ?  15  ASN   A HD22 1 
ATOM   373  N  N    A VAL   A 1 16  ? 16.158 -16.483 8.825   0.64 13.45 ?  16  VAL   A N    1 
ATOM   374  N  N    B VAL   A 1 16  ? 16.150 -16.490 8.839   0.36 13.39 ?  16  VAL   A N    1 
ATOM   375  C  CA   A VAL   A 1 16  ? 15.775 -15.194 8.255   0.64 12.96 ?  16  VAL   A CA   1 
ATOM   376  C  CA   B VAL   A 1 16  ? 15.752 -15.219 8.244   0.36 12.94 ?  16  VAL   A CA   1 
ATOM   377  C  C    A VAL   A 1 16  ? 14.491 -14.703 8.909   0.64 12.66 ?  16  VAL   A C    1 
ATOM   378  C  C    B VAL   A 1 16  ? 14.493 -14.715 8.942   0.36 12.57 ?  16  VAL   A C    1 
ATOM   379  O  O    A VAL   A 1 16  ? 13.484 -15.426 8.965   0.64 12.65 ?  16  VAL   A O    1 
ATOM   380  O  O    B VAL   A 1 16  ? 13.510 -15.455 9.088   0.36 12.62 ?  16  VAL   A O    1 
ATOM   381  C  CB   A VAL   A 1 16  ? 15.632 -15.248 6.725   0.64 13.50 ?  16  VAL   A CB   1 
ATOM   382  C  CB   B VAL   A 1 16  ? 15.532 -15.352 6.726   0.36 13.26 ?  16  VAL   A CB   1 
ATOM   383  C  CG1  A VAL   A 1 16  ? 15.239 -13.871 6.186   0.64 14.12 ?  16  VAL   A CG1  1 
ATOM   384  C  CG1  B VAL   A 1 16  ? 15.075 -14.026 6.131   0.36 13.51 ?  16  VAL   A CG1  1 
ATOM   385  C  CG2  A VAL   A 1 16  ? 16.922 -15.736 6.081   0.64 14.33 ?  16  VAL   A CG2  1 
ATOM   386  C  CG2  B VAL   A 1 16  ? 16.803 -15.847 6.038   0.36 13.76 ?  16  VAL   A CG2  1 
ATOM   387  H  H    A VAL   A 1 16  ? 15.587 -17.111 8.686   0.64 16.14 ?  16  VAL   A H    1 
ATOM   388  H  H    B VAL   A 1 16  ? 15.581 -17.121 8.715   0.36 16.06 ?  16  VAL   A H    1 
ATOM   389  H  HA   A VAL   A 1 16  ? 16.472 -14.551 8.459   0.64 15.55 ?  16  VAL   A HA   1 
ATOM   390  H  HA   B VAL   A 1 16  ? 16.460 -14.570 8.386   0.36 15.53 ?  16  VAL   A HA   1 
ATOM   391  H  HB   A VAL   A 1 16  ? 14.928 -15.872 6.499   0.64 16.20 ?  16  VAL   A HB   1 
ATOM   392  H  HB   B VAL   A 1 16  ? 14.837 -16.007 6.567   0.36 15.92 ?  16  VAL   A HB   1 
ATOM   393  H  HG11 A VAL   A 1 16  ? 15.345 -13.872 5.223   0.64 16.94 ?  16  VAL   A HG11 1 
ATOM   394  H  HG11 B VAL   A 1 16  ? 15.131 -14.081 5.164   0.36 16.21 ?  16  VAL   A HG11 1 
ATOM   395  H  HG12 A VAL   A 1 16  ? 14.314 -13.692 6.416   0.64 16.94 ?  16  VAL   A HG12 1 
ATOM   396  H  HG12 B VAL   A 1 16  ? 14.159 -13.858 6.400   0.36 16.21 ?  16  VAL   A HG12 1 
ATOM   397  H  HG13 A VAL   A 1 16  ? 15.817 -13.200 6.582   0.64 16.94 ?  16  VAL   A HG13 1 
ATOM   398  H  HG13 B VAL   A 1 16  ? 15.654 -13.319 6.455   0.36 16.21 ?  16  VAL   A HG13 1 
ATOM   399  H  HG21 A VAL   A 1 16  ? 16.860 -15.618 5.121   0.64 17.19 ?  16  VAL   A HG21 1 
ATOM   400  H  HG21 B VAL   A 1 16  ? 16.656 -15.868 5.079   0.36 16.52 ?  16  VAL   A HG21 1 
ATOM   401  H  HG22 A VAL   A 1 16  ? 17.666 -15.222 6.431   0.64 17.19 ?  16  VAL   A HG22 1 
ATOM   402  H  HG22 B VAL   A 1 16  ? 17.534 -15.243 6.246   0.36 16.52 ?  16  VAL   A HG22 1 
ATOM   403  H  HG23 A VAL   A 1 16  ? 17.044 -16.675 6.293   0.64 17.19 ?  16  VAL   A HG23 1 
ATOM   404  H  HG23 B VAL   A 1 16  ? 17.012 -16.739 6.359   0.36 16.52 ?  16  VAL   A HG23 1 
ATOM   405  N  N    . TYR   A 1 17  ? 14.529 -13.447 9.352   1.00 12.29 ?  17  TYR   A N    1 
ATOM   406  C  CA   . TYR   A 1 17  ? 13.439 -12.767 10.039  1.00 12.31 ?  17  TYR   A CA   1 
ATOM   407  C  C    . TYR   A 1 17  ? 13.177 -11.439 9.331   1.00 12.64 ?  17  TYR   A C    1 
ATOM   408  O  O    . TYR   A 1 17  ? 14.085 -10.878 8.716   1.00 12.97 ?  17  TYR   A O    1 
ATOM   409  C  CB   . TYR   A 1 17  ? 13.860 -12.495 11.486  1.00 12.80 ?  17  TYR   A CB   1 
ATOM   410  C  CG   . TYR   A 1 17  ? 14.059 -13.757 12.296  1.00 13.97 ?  17  TYR   A CG   1 
ATOM   411  C  CD1  . TYR   A 1 17  ? 15.233 -14.502 12.208  1.00 15.14 ?  17  TYR   A CD1  1 
ATOM   412  C  CD2  . TYR   A 1 17  ? 13.059 -14.221 13.136  1.00 14.36 ?  17  TYR   A CD2  1 
ATOM   413  C  CE1  . TYR   A 1 17  ? 15.399 -15.675 12.942  1.00 15.40 ?  17  TYR   A CE1  1 
ATOM   414  C  CE2  . TYR   A 1 17  ? 13.216 -15.389 13.875  1.00 15.24 ?  17  TYR   A CE2  1 
ATOM   415  C  CZ   . TYR   A 1 17  ? 14.390 -16.113 13.779  1.00 15.70 ?  17  TYR   A CZ   1 
ATOM   416  O  OH   . TYR   A 1 17  ? 14.538 -17.272 14.517  1.00 16.74 ?  17  TYR   A OH   1 
ATOM   417  H  H    A TYR   A 1 17  ? 15.223 -12.942 9.255   0.64 14.75 ?  17  TYR   A H    1 
ATOM   418  H  H    B TYR   A 1 17  ? 15.216 -12.936 9.233   0.36 14.75 ?  17  TYR   A H    1 
ATOM   419  H  HA   . TYR   A 1 17  ? 12.637 -13.315 10.022  1.00 14.77 ?  17  TYR   A HA   1 
ATOM   420  H  HB2  . TYR   A 1 17  ? 14.695 -12.007 11.479  1.00 15.36 ?  17  TYR   A HB2  1 
ATOM   421  H  HB3  . TYR   A 1 17  ? 13.172 -11.972 11.912  1.00 15.36 ?  17  TYR   A HB3  1 
ATOM   422  H  HD1  . TYR   A 1 17  ? 15.917 -14.217 11.643  1.00 18.17 ?  17  TYR   A HD1  1 
ATOM   423  H  HD2  . TYR   A 1 17  ? 12.264 -13.744 13.207  1.00 17.23 ?  17  TYR   A HD2  1 
ATOM   424  H  HE1  . TYR   A 1 17  ? 16.193 -16.161 12.878  1.00 18.48 ?  17  TYR   A HE1  1 
ATOM   425  H  HE2  . TYR   A 1 17  ? 12.532 -15.675 14.438  1.00 18.29 ?  17  TYR   A HE2  1 
ATOM   426  H  HH   . TYR   A 1 17  ? 13.807 -17.471 14.878  1.00 20.08 ?  17  TYR   A HH   1 
ATOM   427  N  N    A ILE   A 1 18  ? 11.933 -10.956 9.373   0.64 12.66 ?  18  ILE   A N    1 
ATOM   428  N  N    B ILE   A 1 18  ? 11.960 -10.898 9.480   0.36 12.36 ?  18  ILE   A N    1 
ATOM   429  C  CA   A ILE   A 1 18  ? 11.548 -9.789  8.582   0.64 12.73 ?  18  ILE   A CA   1 
ATOM   430  C  CA   B ILE   A 1 18  ? 11.572 -9.673  8.784   0.36 11.85 ?  18  ILE   A CA   1 
ATOM   431  C  C    A ILE   A 1 18  ? 10.562 -8.912  9.351   0.64 13.10 ?  18  ILE   A C    1 
ATOM   432  C  C    B ILE   A 1 18  ? 10.655 -8.813  9.650   0.36 11.62 ?  18  ILE   A C    1 
ATOM   433  O  O    A ILE   A 1 18  ? 9.706  -9.414  10.086  0.64 13.06 ?  18  ILE   A O    1 
ATOM   434  O  O    B ILE   A 1 18  ? 9.888  -9.319  10.476  0.36 11.81 ?  18  ILE   A O    1 
ATOM   435  C  CB   A ILE   A 1 18  ? 11.028 -10.218 7.193   0.64 12.41 ?  18  ILE   A CB   1 
ATOM   436  C  CB   B ILE   A 1 18  ? 10.910 -10.001 7.431   0.36 11.46 ?  18  ILE   A CB   1 
ATOM   437  C  CG1  A ILE   A 1 18  ? 10.981 -9.030  6.236   0.64 12.71 ?  18  ILE   A CG1  1 
ATOM   438  C  CG1  B ILE   A 1 18  ? 10.884 -8.783  6.508   0.36 12.43 ?  18  ILE   A CG1  1 
ATOM   439  C  CG2  A ILE   A 1 18  ? 9.682  -10.948 7.300   0.64 12.35 ?  18  ILE   A CG2  1 
ATOM   440  C  CG2  B ILE   A 1 18  ? 9.509  -10.555 7.642   0.36 11.91 ?  18  ILE   A CG2  1 
ATOM   441  C  CD1  A ILE   A 1 18  ? 10.777 -9.439  4.812   0.64 13.68 ?  18  ILE   A CD1  1 
ATOM   442  C  CD1  B ILE   A 1 18  ? 10.454 -9.137  5.101   0.36 13.41 ?  18  ILE   A CD1  1 
ATOM   443  H  H    A ILE   A 1 18  ? 11.298 -11.302 9.844   0.64 15.19 ?  18  ILE   A H    1 
ATOM   444  H  H    B ILE   A 1 18  ? 11.343 -11.232 9.979   0.36 14.83 ?  18  ILE   A H    1 
ATOM   445  H  HA   A ILE   A 1 18  ? 12.349 -9.264  8.432   0.64 15.28 ?  18  ILE   A HA   1 
ATOM   446  H  HA   B ILE   A 1 18  ? 12.377 -9.159  8.605   0.36 14.22 ?  18  ILE   A HA   1 
ATOM   447  H  HB   A ILE   A 1 18  ? 11.667 -10.853 6.828   0.64 14.89 ?  18  ILE   A HB   1 
ATOM   448  H  HB   B ILE   A 1 18  ? 11.443 -10.683 7.006   0.36 13.75 ?  18  ILE   A HB   1 
ATOM   449  H  HG12 A ILE   A 1 18  ? 10.252 -8.448  6.490   0.64 15.25 ?  18  ILE   A HG12 1 
ATOM   450  H  HG12 B ILE   A 1 18  ? 10.262 -8.127  6.856   0.36 14.91 ?  18  ILE   A HG12 1 
ATOM   451  H  HG13 A ILE   A 1 18  ? 11.825 -8.550  6.289   0.64 15.25 ?  18  ILE   A HG13 1 
ATOM   452  H  HG13 B ILE   A 1 18  ? 11.777 -8.399  6.459   0.36 14.91 ?  18  ILE   A HG13 1 
ATOM   453  H  HG21 A ILE   A 1 18  ? 9.457  -11.330 6.433   0.64 14.82 ?  18  ILE   A HG21 1 
ATOM   454  H  HG21 B ILE   A 1 18  ? 9.216  -10.980 6.820   0.36 14.29 ?  18  ILE   A HG21 1 
ATOM   455  H  HG22 A ILE   A 1 18  ? 9.756  -11.659 7.958   0.64 14.82 ?  18  ILE   A HG22 1 
ATOM   456  H  HG22 B ILE   A 1 18  ? 9.532  -11.206 8.360   0.36 14.29 ?  18  ILE   A HG22 1 
ATOM   457  H  HG23 A ILE   A 1 18  ? 8.997  -10.319 7.569   0.64 14.82 ?  18  ILE   A HG23 1 
ATOM   458  H  HG23 B ILE   A 1 18  ? 8.908  -9.830  7.872   0.36 14.29 ?  18  ILE   A HG23 1 
ATOM   459  H  HD11 A ILE   A 1 18  ? 10.830 -8.650  4.250   0.64 16.41 ?  18  ILE   A HD11 1 
ATOM   460  H  HD11 B ILE   A 1 18  ? 10.582 -8.372  4.523   0.36 16.09 ?  18  ILE   A HD11 1 
ATOM   461  H  HD12 A ILE   A 1 18  ? 11.466 -10.072 4.563   0.64 16.41 ?  18  ILE   A HD12 1 
ATOM   462  H  HD12 B ILE   A 1 18  ? 10.994 -9.880  4.785   0.36 16.09 ?  18  ILE   A HD12 1 
ATOM   463  H  HD13 A ILE   A 1 18  ? 9.901  -9.847  4.727   0.64 16.41 ?  18  ILE   A HD13 1 
ATOM   464  H  HD13 B ILE   A 1 18  ? 9.519  -9.392  5.112   0.36 16.09 ?  18  ILE   A HD13 1 
ATOM   465  N  N    A LYS   A 1 19  ? 10.684 -7.593  9.168   0.64 13.32 ?  19  LYS   A N    1 
ATOM   466  N  N    B LYS   A 1 19  ? 10.720 -7.496  9.424   0.36 11.86 ?  19  LYS   A N    1 
ATOM   467  C  CA   A LYS   A 1 19  ? 9.862  -6.620  9.881   0.64 13.97 ?  19  LYS   A CA   1 
ATOM   468  C  CA   B LYS   A 1 19  ? 9.935  -6.535  10.188  0.36 13.25 ?  19  LYS   A CA   1 
ATOM   469  C  C    A LYS   A 1 19  ? 9.691  -5.370  9.027   0.64 13.50 ?  19  LYS   A C    1 
ATOM   470  C  C    B LYS   A 1 19  ? 9.765  -5.273  9.356   0.36 13.22 ?  19  LYS   A C    1 
ATOM   471  O  O    A LYS   A 1 19  ? 10.569 -5.020  8.236   0.64 13.17 ?  19  LYS   A O    1 
ATOM   472  O  O    B LYS   A 1 19  ? 10.715 -4.826  8.710   0.36 12.75 ?  19  LYS   A O    1 
ATOM   473  C  CB   A LYS   A 1 19  ? 10.551 -6.225  11.195  0.64 14.94 ?  19  LYS   A CB   1 
ATOM   474  C  CB   B LYS   A 1 19  ? 10.659 -6.201  11.498  0.36 14.28 ?  19  LYS   A CB   1 
ATOM   475  C  CG   A LYS   A 1 19  ? 9.775  -5.300  12.129  0.64 16.74 ?  19  LYS   A CG   1 
ATOM   476  C  CG   B LYS   A 1 19  ? 9.975  -5.196  12.399  0.36 15.56 ?  19  LYS   A CG   1 
ATOM   477  C  CD   A LYS   A 1 19  ? 10.642 -4.990  13.349  0.64 18.57 ?  19  LYS   A CD   1 
ATOM   478  C  CD   B LYS   A 1 19  ? 10.815 -5.003  13.649  0.36 17.03 ?  19  LYS   A CD   1 
ATOM   479  C  CE   A LYS   A 1 19  ? 9.966  -4.085  14.366  0.64 19.74 ?  19  LYS   A CE   1 
ATOM   480  C  CE   B LYS   A 1 19  ? 10.244 -3.960  14.583  0.36 17.77 ?  19  LYS   A CE   1 
ATOM   481  N  NZ   A LYS   A 1 19  ? 10.880 -3.808  15.517  0.64 20.29 ?  19  LYS   A NZ   1 
ATOM   482  N  NZ   B LYS   A 1 19  ? 11.095 -3.835  15.799  0.36 18.14 ?  19  LYS   A NZ   1 
ATOM   483  H  H    A LYS   A 1 19  ? 11.256 -7.245  8.626   0.64 15.99 ?  19  LYS   A H    1 
ATOM   484  H  H    B LYS   A 1 19  ? 11.222 -7.122  8.821   0.36 14.23 ?  19  LYS   A H    1 
ATOM   485  H  HA   A LYS   A 1 19  ? 8.996  -7.009  10.072  0.64 16.76 ?  19  LYS   A HA   1 
ATOM   486  H  HA   B LYS   A 1 19  ? 9.063  -6.894  10.390  0.36 15.90 ?  19  LYS   A HA   1 
ATOM   487  H  HB2  A LYS   A 1 19  ? 10.740 -7.038  11.690  0.64 17.93 ?  19  LYS   A HB2  1 
ATOM   488  H  HB2  B LYS   A 1 19  ? 10.754 -7.021  12.008  0.36 17.13 ?  19  LYS   A HB2  1 
ATOM   489  H  HB3  A LYS   A 1 19  ? 11.384 -5.783  10.975  0.64 17.93 ?  19  LYS   A HB3  1 
ATOM   490  H  HB3  B LYS   A 1 19  ? 11.538 -5.848  11.288  0.36 17.13 ?  19  LYS   A HB3  1 
ATOM   491  H  HG2  A LYS   A 1 19  ? 9.569  -4.469  11.673  0.64 20.09 ?  19  LYS   A HG2  1 
ATOM   492  H  HG2  B LYS   A 1 19  ? 9.897  -4.344  11.942  0.36 18.67 ?  19  LYS   A HG2  1 
ATOM   493  H  HG3  A LYS   A 1 19  ? 8.962  -5.739  12.427  0.64 20.09 ?  19  LYS   A HG3  1 
ATOM   494  H  HG3  B LYS   A 1 19  ? 9.102  -5.530  12.657  0.36 18.67 ?  19  LYS   A HG3  1 
ATOM   495  H  HD2  A LYS   A 1 19  ? 10.865 -5.823  13.796  0.64 22.29 ?  19  LYS   A HD2  1 
ATOM   496  H  HD2  B LYS   A 1 19  ? 10.863 -5.846  14.129  0.36 20.44 ?  19  LYS   A HD2  1 
ATOM   497  H  HD3  A LYS   A 1 19  ? 11.455 -4.550  13.054  0.64 22.29 ?  19  LYS   A HD3  1 
ATOM   498  H  HD3  B LYS   A 1 19  ? 11.706 -4.720  13.388  0.36 20.44 ?  19  LYS   A HD3  1 
ATOM   499  H  HE2  A LYS   A 1 19  ? 9.741  -3.240  13.948  0.64 23.69 ?  19  LYS   A HE2  1 
ATOM   500  H  HE2  B LYS   A 1 19  ? 10.220 -3.102  14.132  0.36 21.32 ?  19  LYS   A HE2  1 
ATOM   501  H  HE3  A LYS   A 1 19  ? 9.170  -4.518  14.708  0.64 23.69 ?  19  LYS   A HE3  1 
ATOM   502  H  HE3  B LYS   A 1 19  ? 9.351  -4.226  14.855  0.36 21.32 ?  19  LYS   A HE3  1 
ATOM   503  H  HZ1  A LYS   A 1 19  ? 10.470 -3.297  16.118  0.64 24.35 ?  19  LYS   A HZ1  1 
ATOM   504  H  HZ1  B LYS   A 1 19  ? 10.758 -3.217  16.341  0.36 21.77 ?  19  LYS   A HZ1  1 
ATOM   505  H  HZ2  A LYS   A 1 19  ? 11.122 -4.574  15.905  0.64 24.35 ?  19  LYS   A HZ2  1 
ATOM   506  H  HZ2  B LYS   A 1 19  ? 11.124 -4.614  16.228  0.36 21.77 ?  19  LYS   A HZ2  1 
ATOM   507  H  HZ3  A LYS   A 1 19  ? 11.612 -3.388  15.232  0.64 24.35 ?  19  LYS   A HZ3  1 
ATOM   508  H  HZ3  B LYS   A 1 19  ? 11.921 -3.601  15.567  0.36 21.77 ?  19  LYS   A HZ3  1 
ATOM   509  N  N    A ASN   A 1 20  ? 8.553  -4.696  9.198   0.64 14.48 ?  20  ASN   A N    1 
ATOM   510  N  N    B ASN   A 1 20  ? 8.556  -4.709  9.361   0.36 14.43 ?  20  ASN   A N    1 
ATOM   511  C  CA   A ASN   A 1 20  ? 8.334  -3.369  8.614   0.64 15.76 ?  20  ASN   A CA   1 
ATOM   512  C  CA   B ASN   A 1 20  ? 8.346  -3.389  8.773   0.36 15.62 ?  20  ASN   A CA   1 
ATOM   513  C  C    A ASN   A 1 20  ? 8.924  -2.347  9.578   0.64 16.79 ?  20  ASN   A C    1 
ATOM   514  C  C    B ASN   A 1 20  ? 9.002  -2.361  9.681   0.36 16.08 ?  20  ASN   A C    1 
ATOM   515  O  O    A ASN   A 1 20  ? 8.344  -2.067  10.631  0.64 18.59 ?  20  ASN   A O    1 
ATOM   516  O  O    B ASN   A 1 20  ? 8.537  -2.119  10.799  0.36 16.94 ?  20  ASN   A O    1 
ATOM   517  C  CB   A ASN   A 1 20  ? 6.840  -3.141  8.391   0.64 16.03 ?  20  ASN   A CB   1 
ATOM   518  C  CB   B ASN   A 1 20  ? 6.859  -3.090  8.596   0.36 16.39 ?  20  ASN   A CB   1 
ATOM   519  C  CG   A ASN   A 1 20  ? 6.510  -1.738  7.877   0.64 16.69 ?  20  ASN   A CG   1 
ATOM   520  C  CG   B ASN   A 1 20  ? 6.583  -1.607  8.373   0.36 17.37 ?  20  ASN   A CG   1 
ATOM   521  O  OD1  A ASN   A 1 20  ? 5.483  -1.163  8.246   0.64 18.08 ?  20  ASN   A OD1  1 
ATOM   522  O  OD1  B ASN   A 1 20  ? 5.739  -1.020  9.047   0.36 18.81 ?  20  ASN   A OD1  1 
ATOM   523  N  ND2  A ASN   A 1 20  ? 7.366  -1.195  7.015   0.64 17.23 ?  20  ASN   A ND2  1 
ATOM   524  N  ND2  B ASN   A 1 20  ? 7.310  -0.994  7.437   0.36 17.09 ?  20  ASN   A ND2  1 
ATOM   525  H  H    A ASN   A 1 20  ? 7.885  -5.003  9.642   0.64 17.37 ?  20  ASN   A H    1 
ATOM   526  H  H    B ASN   A 1 20  ? 7.853  -5.065  9.693   0.36 17.32 ?  20  ASN   A H    1 
ATOM   527  H  HA   A ASN   A 1 20  ? 8.799  -3.317  7.767   0.64 18.91 ?  20  ASN   A HA   1 
ATOM   528  H  HA   B ASN   A 1 20  ? 8.766  -3.345  7.900   0.36 18.75 ?  20  ASN   A HA   1 
ATOM   529  H  HB2  A ASN   A 1 20  ? 6.523  -3.780  7.740   0.64 19.24 ?  20  ASN   A HB2  1 
ATOM   530  H  HB2  B ASN   A 1 20  ? 6.523  -3.576  7.822   0.36 19.67 ?  20  ASN   A HB2  1 
ATOM   531  H  HB3  A ASN   A 1 20  ? 6.382  -3.276  9.237   0.64 19.24 ?  20  ASN   A HB3  1 
ATOM   532  H  HB3  B ASN   A 1 20  ? 6.377  -3.364  9.391   0.36 19.67 ?  20  ASN   A HB3  1 
ATOM   533  H  HD21 A ASN   A 1 20  ? 7.218  -0.411  6.709   0.64 20.68 ?  20  ASN   A HD21 1 
ATOM   534  H  HD21 B ASN   A 1 20  ? 7.192  -0.156  7.272   0.36 20.51 ?  20  ASN   A HD21 1 
ATOM   535  H  HD22 A ASN   A 1 20  ? 8.067  -1.632  6.768   0.64 20.68 ?  20  ASN   A HD22 1 
ATOM   536  H  HD22 B ASN   A 1 20  ? 7.900  -1.436  6.991   0.36 20.51 ?  20  ASN   A HD22 1 
ATOM   537  N  N    A ALA   A 1 21  ? 10.088 -1.789  9.234   0.64 16.81 ?  21  ALA   A N    1 
ATOM   538  N  N    B ALA   A 1 21  ? 10.110 -1.793  9.224   0.36 15.94 ?  21  ALA   A N    1 
ATOM   539  C  CA   A ALA   A 1 21  ? 10.782 -0.919  10.175  0.64 16.74 ?  21  ALA   A CA   1 
ATOM   540  C  CA   B ALA   A 1 21  ? 10.782 -0.756  9.986   0.36 15.78 ?  21  ALA   A CA   1 
ATOM   541  C  C    A ALA   A 1 21  ? 11.752 -0.006  9.441   0.64 15.58 ?  21  ALA   A C    1 
ATOM   542  C  C    B ALA   A 1 21  ? 11.778 -0.052  9.084   0.36 15.23 ?  21  ALA   A C    1 
ATOM   543  O  O    A ALA   A 1 21  ? 12.230 -0.330  8.350   0.64 16.09 ?  21  ALA   A O    1 
ATOM   544  O  O    B ALA   A 1 21  ? 12.260 -0.623  8.101   0.36 15.57 ?  21  ALA   A O    1 
ATOM   545  C  CB   A ALA   A 1 21  ? 11.531 -1.732  11.236  0.64 17.67 ?  21  ALA   A CB   1 
ATOM   546  C  CB   B ALA   A 1 21  ? 11.516 -1.344  11.194  0.36 16.13 ?  21  ALA   A CB   1 
ATOM   547  H  H    A ALA   A 1 21  ? 10.482 -1.887  8.474   0.64 20.17 ?  21  ALA   A H    1 
ATOM   548  H  H    B ALA   A 1 21  ? 10.497 -2.007  8.490   0.36 19.13 ?  21  ALA   A H    1 
ATOM   549  H  HA   A ALA   A 1 21  ? 10.132 -0.360  10.626  0.64 20.08 ?  21  ALA   A HA   1 
ATOM   550  H  HA   B ALA   A 1 21  ? 10.128 -0.112  10.303  0.36 18.94 ?  21  ALA   A HA   1 
ATOM   551  H  HB1  A ALA   A 1 21  ? 11.956 -1.120  11.857  0.64 21.20 ?  21  ALA   A HB1  1 
ATOM   552  H  HB1  B ALA   A 1 21  ? 11.946 -0.622  11.677  0.36 19.36 ?  21  ALA   A HB1  1 
ATOM   553  H  HB2  A ALA   A 1 21  ? 10.891 -2.290  11.709  0.64 21.20 ?  21  ALA   A HB2  1 
ATOM   554  H  HB2  B ALA   A 1 21  ? 10.874 -1.792  11.766  0.36 19.36 ?  21  ALA   A HB2  1 
ATOM   555  H  HB3  A ALA   A 1 21  ? 12.195 -2.285  10.802  0.64 21.20 ?  21  ALA   A HB3  1 
ATOM   556  H  HB3  B ALA   A 1 21  ? 12.180 -1.976  10.879  0.36 19.36 ?  21  ALA   A HB3  1 
ATOM   557  N  N    A ASP   A 1 22  ? 12.029 1.139   10.068  0.64 14.41 ?  22  ASP   A N    1 
ATOM   558  N  N    B ASP   A 1 22  ? 12.057 1.201   9.423   0.36 14.97 ?  22  ASP   A N    1 
ATOM   559  C  CA   A ASP   A 1 22  ? 13.063 2.064   9.617   0.64 14.38 ?  22  ASP   A CA   1 
ATOM   560  C  CA   B ASP   A 1 22  ? 13.221 1.886   8.882   0.36 14.92 ?  22  ASP   A CA   1 
ATOM   561  C  C    A ASP   A 1 22  ? 14.398 1.593   10.183  0.64 13.34 ?  22  ASP   A C    1 
ATOM   562  C  C    B ASP   A 1 22  ? 14.469 1.329   9.558   0.36 13.97 ?  22  ASP   A C    1 
ATOM   563  O  O    A ASP   A 1 22  ? 14.587 1.579   11.404  0.64 13.83 ?  22  ASP   A O    1 
ATOM   564  O  O    B ASP   A 1 22  ? 14.562 1.309   10.788  0.36 14.20 ?  22  ASP   A O    1 
ATOM   565  C  CB   A ASP   A 1 22  ? 12.725 3.469   10.120  0.64 16.26 ?  22  ASP   A CB   1 
ATOM   566  C  CB   B ASP   A 1 22  ? 13.088 3.384   9.162   0.36 16.83 ?  22  ASP   A CB   1 
ATOM   567  C  CG   A ASP   A 1 22  ? 13.732 4.526   9.670   0.64 18.41 ?  22  ASP   A CG   1 
ATOM   568  C  CG   B ASP   A 1 22  ? 14.245 4.201   8.627   0.36 18.44 ?  22  ASP   A CG   1 
ATOM   569  O  OD1  A ASP   A 1 22  ? 14.866 4.182   9.290   0.64 18.68 ?  22  ASP   A OD1  1 
ATOM   570  O  OD1  B ASP   A 1 22  ? 15.182 3.625   8.041   0.36 18.89 ?  22  ASP   A OD1  1 
ATOM   571  O  OD2  A ASP   A 1 22  ? 13.384 5.724   9.708   0.64 20.28 -1 22  ASP   A OD2  1 
ATOM   572  O  OD2  B ASP   A 1 22  ? 14.213 5.438   8.805   0.36 19.62 -1 22  ASP   A OD2  1 
ATOM   573  H  H    A ASP   A 1 22  ? 11.612 1.414   10.771  0.64 17.30 ?  22  ASP   A H    1 
ATOM   574  H  H    B ASP   A 1 22  ? 11.573 1.680   9.955   0.36 17.96 ?  22  ASP   A H    1 
ATOM   575  H  HA   A ASP   A 1 22  ? 13.108 2.077   8.650   0.64 17.25 ?  22  ASP   A HA   1 
ATOM   576  H  HA   B ASP   A 1 22  ? 13.274 1.736   7.921   0.36 17.91 ?  22  ASP   A HA   1 
ATOM   577  H  HB2  A ASP   A 1 22  ? 11.847 3.723   9.782   0.64 19.51 ?  22  ASP   A HB2  1 
ATOM   578  H  HB2  B ASP   A 1 22  ? 12.278 3.714   8.752   0.36 20.20 ?  22  ASP   A HB2  1 
ATOM   579  H  HB3  A ASP   A 1 22  ? 12.703 3.461   11.093  0.64 19.51 ?  22  ASP   A HB3  1 
ATOM   580  H  HB3  B ASP   A 1 22  ? 13.071 3.524   10.115  0.36 20.20 ?  22  ASP   A HB3  1 
ATOM   581  N  N    A ILE   A 1 23  ? 15.316 1.196   9.296   0.64 13.18 ?  23  ILE   A N    1 
ATOM   582  N  N    B ILE   A 1 23  ? 15.424 0.855   8.752   0.36 13.81 ?  23  ILE   A N    1 
ATOM   583  C  CA   A ILE   A 1 23  ? 16.568 0.575   9.727   0.64 12.79 ?  23  ILE   A CA   1 
ATOM   584  C  CA   B ILE   A 1 23  ? 16.632 0.244   9.303   0.36 13.52 ?  23  ILE   A CA   1 
ATOM   585  C  C    A ILE   A 1 23  ? 17.380 1.515   10.609  0.64 13.07 ?  23  ILE   A C    1 
ATOM   586  C  C    B ILE   A 1 23  ? 17.377 1.223   10.197  0.36 14.14 ?  23  ILE   A C    1 
ATOM   587  O  O    A ILE   A 1 23  ? 18.095 1.064   11.513  0.64 13.80 ?  23  ILE   A O    1 
ATOM   588  O  O    B ILE   A 1 23  ? 18.051 0.815   11.150  0.36 14.28 ?  23  ILE   A O    1 
ATOM   589  C  CB   A ILE   A 1 23  ? 17.358 0.055   8.505   0.64 12.64 ?  23  ILE   A CB   1 
ATOM   590  C  CB   B ILE   A 1 23  ? 17.536 -0.324  8.187   0.36 12.89 ?  23  ILE   A CB   1 
ATOM   591  C  CG1  A ILE   A 1 23  ? 18.501 -0.863  8.945   0.64 12.98 ?  23  ILE   A CG1  1 
ATOM   592  C  CG1  B ILE   A 1 23  ? 18.607 -1.243  8.790   0.36 12.45 ?  23  ILE   A CG1  1 
ATOM   593  C  CG2  A ILE   A 1 23  ? 17.866 1.210   7.644   0.64 12.80 ?  23  ILE   A CG2  1 
ATOM   594  C  CG2  B ILE   A 1 23  ? 18.181 0.800   7.382   0.36 12.82 ?  23  ILE   A CG2  1 
ATOM   595  C  CD1  A ILE   A 1 23  ? 19.160 -1.598  7.798   0.64 13.34 ?  23  ILE   A CD1  1 
ATOM   596  C  CD1  B ILE   A 1 23  ? 19.533 -1.874  7.766   0.36 12.39 ?  23  ILE   A CD1  1 
ATOM   597  H  H    A ILE   A 1 23  ? 15.232 1.276   8.445   0.64 15.81 ?  23  ILE   A H    1 
ATOM   598  H  H    B ILE   A 1 23  ? 15.395 0.875   7.903   0.36 16.57 ?  23  ILE   A H    1 
ATOM   599  H  HA   A ILE   A 1 23  ? 16.348 -0.197  10.265  0.64 15.35 ?  23  ILE   A HA   1 
ATOM   600  H  HA   B ILE   A 1 23  ? 16.362 -0.505  9.857   0.36 16.22 ?  23  ILE   A HA   1 
ATOM   601  H  HB   A ILE   A 1 23  ? 16.750 -0.468  7.958   0.64 15.17 ?  23  ILE   A HB   1 
ATOM   602  H  HB   B ILE   A 1 23  ? 16.988 -0.853  7.589   0.36 15.47 ?  23  ILE   A HB   1 
ATOM   603  H  HG12 A ILE   A 1 23  ? 19.179 -0.331  9.385   0.64 15.58 ?  23  ILE   A HG12 1 
ATOM   604  H  HG12 B ILE   A 1 23  ? 19.155 -0.730  9.404   0.36 14.95 ?  23  ILE   A HG12 1 
ATOM   605  H  HG13 A ILE   A 1 23  ? 18.147 -1.525  9.558   0.64 15.58 ?  23  ILE   A HG13 1 
ATOM   606  H  HG13 B ILE   A 1 23  ? 18.167 -1.964  9.271   0.36 14.95 ?  23  ILE   A HG13 1 
ATOM   607  H  HG21 A ILE   A 1 23  ? 18.215 0.858   6.809   0.64 15.35 ?  23  ILE   A HG21 1 
ATOM   608  H  HG21 B ILE   A 1 23  ? 18.566 0.426   6.571   0.36 15.38 ?  23  ILE   A HG21 1 
ATOM   609  H  HG22 A ILE   A 1 23  ? 17.126 1.815   7.456   0.64 15.35 ?  23  ILE   A HG22 1 
ATOM   610  H  HG22 B ILE   A 1 23  ? 17.503 1.452   7.153   0.36 15.38 ?  23  ILE   A HG22 1 
ATOM   611  H  HG23 A ILE   A 1 23  ? 18.563 1.684   8.121   0.64 15.35 ?  23  ILE   A HG23 1 
ATOM   612  H  HG23 B ILE   A 1 23  ? 18.877 1.215   7.914   0.36 15.38 ?  23  ILE   A HG23 1 
ATOM   613  H  HD11 A ILE   A 1 23  ? 19.817 -2.213  8.156   0.64 16.00 ?  23  ILE   A HD11 1 
ATOM   614  H  HD11 B ILE   A 1 23  ? 20.096 -2.529  8.211   0.36 14.87 ?  23  ILE   A HD11 1 
ATOM   615  H  HD12 A ILE   A 1 23  ? 18.480 -2.088  7.307   0.64 16.00 ?  23  ILE   A HD12 1 
ATOM   616  H  HD12 B ILE   A 1 23  ? 18.998 -2.308  7.084   0.36 14.87 ?  23  ILE   A HD12 1 
ATOM   617  H  HD13 A ILE   A 1 23  ? 19.589 -0.954  7.215   0.64 16.00 ?  23  ILE   A HD13 1 
ATOM   618  H  HD13 B ILE   A 1 23  ? 20.082 -1.182  7.367   0.36 14.87 ?  23  ILE   A HD13 1 
ATOM   619  N  N    A VAL   A 1 24  ? 17.272 2.826   10.385  0.64 13.89 ?  24  VAL   A N    1 
ATOM   620  N  N    B VAL   A 1 24  ? 17.272 2.523   9.912   0.36 14.79 ?  24  VAL   A N    1 
ATOM   621  C  CA   A VAL   A 1 24  ? 17.964 3.780   11.249  0.64 14.81 ?  24  VAL   A CA   1 
ATOM   622  C  CA   B VAL   A 1 24  ? 17.903 3.520   10.770  0.36 15.76 ?  24  VAL   A CA   1 
ATOM   623  C  C    A VAL   A 1 24  ? 17.432 3.683   12.672  0.64 15.38 ?  24  VAL   A C    1 
ATOM   624  C  C    B VAL   A 1 24  ? 17.264 3.510   12.152  0.36 16.51 ?  24  VAL   A C    1 
ATOM   625  O  O    A VAL   A 1 24  ? 18.198 3.575   13.640  0.64 15.89 ?  24  VAL   A O    1 
ATOM   626  O  O    B VAL   A 1 24  ? 17.955 3.587   13.174  0.36 17.13 ?  24  VAL   A O    1 
ATOM   627  C  CB   A VAL   A 1 24  ? 17.828 5.208   10.690  0.64 15.55 ?  24  VAL   A CB   1 
ATOM   628  C  CB   B VAL   A 1 24  ? 17.841 4.908   10.107  0.36 16.20 ?  24  VAL   A CB   1 
ATOM   629  C  CG1  A VAL   A 1 24  ? 18.305 6.231   11.713  0.64 16.22 ?  24  VAL   A CG1  1 
ATOM   630  C  CG1  B VAL   A 1 24  ? 18.512 5.948   10.985  0.36 16.99 ?  24  VAL   A CG1  1 
ATOM   631  C  CG2  A VAL   A 1 24  ? 18.597 5.346   9.386   0.64 16.18 ?  24  VAL   A CG2  1 
ATOM   632  C  CG2  B VAL   A 1 24  ? 18.488 4.859   8.731   0.36 15.89 ?  24  VAL   A CG2  1 
ATOM   633  H  H    A VAL   A 1 24  ? 16.812 3.180   9.751   0.64 16.67 ?  24  VAL   A H    1 
ATOM   634  H  H    B VAL   A 1 24  ? 16.846 2.847   9.241   0.36 17.75 ?  24  VAL   A H    1 
ATOM   635  H  HA   A VAL   A 1 24  ? 18.909 3.559   11.266  0.64 17.78 ?  24  VAL   A HA   1 
ATOM   636  H  HA   B VAL   A 1 24  ? 18.837 3.291   10.880  0.36 18.91 ?  24  VAL   A HA   1 
ATOM   637  H  HB   A VAL   A 1 24  ? 16.894 5.385   10.500  0.64 18.66 ?  24  VAL   A HB   1 
ATOM   638  H  HB   B VAL   A 1 24  ? 16.913 5.166   9.992   0.36 19.44 ?  24  VAL   A HB   1 
ATOM   639  H  HG11 A VAL   A 1 24  ? 18.481 7.068   11.257  0.64 19.46 ?  24  VAL   A HG11 1 
ATOM   640  H  HG11 B VAL   A 1 24  ? 18.662 6.752   10.464  0.36 20.39 ?  24  VAL   A HG11 1 
ATOM   641  H  HG12 A VAL   A 1 24  ? 17.611 6.356   12.377  0.64 19.46 ?  24  VAL   A HG12 1 
ATOM   642  H  HG12 B VAL   A 1 24  ? 17.931 6.144   11.736  0.36 20.39 ?  24  VAL   A HG12 1 
ATOM   643  H  HG13 A VAL   A 1 24  ? 19.116 5.903   12.130  0.64 19.46 ?  24  VAL   A HG13 1 
ATOM   644  H  HG13 B VAL   A 1 24  ? 19.359 5.595   11.300  0.36 20.39 ?  24  VAL   A HG13 1 
ATOM   645  H  HG21 A VAL   A 1 24  ? 18.432 6.226   9.010   0.64 19.41 ?  24  VAL   A HG21 1 
ATOM   646  H  HG21 B VAL   A 1 24  ? 18.560 5.760   8.382   0.36 19.07 ?  24  VAL   A HG21 1 
ATOM   647  H  HG22 A VAL   A 1 24  ? 19.546 5.238   9.564   0.64 19.41 ?  24  VAL   A HG22 1 
ATOM   648  H  HG22 B VAL   A 1 24  ? 19.371 4.465   8.813   0.36 19.07 ?  24  VAL   A HG22 1 
ATOM   649  H  HG23 A VAL   A 1 24  ? 18.299 4.662   8.764   0.64 19.41 ?  24  VAL   A HG23 1 
ATOM   650  H  HG23 B VAL   A 1 24  ? 17.940 4.318   8.142   0.36 19.07 ?  24  VAL   A HG23 1 
ATOM   651  N  N    A GLU   A 1 25  ? 16.107 3.732   12.819  0.64 16.09 ?  25  GLU   A N    1 
ATOM   652  N  N    B GLU   A 1 25  ? 15.935 3.396   12.206  0.36 17.03 ?  25  GLU   A N    1 
ATOM   653  C  CA   A GLU   A 1 25  ? 15.508 3.668   14.147  0.64 17.45 ?  25  GLU   A CA   1 
ATOM   654  C  CA   B GLU   A 1 25  ? 15.253 3.337   13.495  0.36 18.25 ?  25  GLU   A CA   1 
ATOM   655  C  C    A GLU   A 1 25  ? 15.739 2.309   14.789  0.64 16.76 ?  25  GLU   A C    1 
ATOM   656  C  C    B GLU   A 1 25  ? 15.551 2.030   14.224  0.36 18.06 ?  25  GLU   A C    1 
ATOM   657  O  O    A GLU   A 1 25  ? 15.961 2.220   16.002  0.64 17.45 ?  25  GLU   A O    1 
ATOM   658  O  O    B GLU   A 1 25  ? 15.758 2.029   15.443  0.36 18.30 ?  25  GLU   A O    1 
ATOM   659  C  CB   A GLU   A 1 25  ? 14.019 4.004   14.061  0.64 19.61 ?  25  GLU   A CB   1 
ATOM   660  C  CB   B GLU   A 1 25  ? 13.749 3.534   13.298  0.36 20.02 ?  25  GLU   A CB   1 
ATOM   661  C  CG   A GLU   A 1 25  ? 13.759 5.454   13.677  0.64 22.45 ?  25  GLU   A CG   1 
ATOM   662  C  CG   B GLU   A 1 25  ? 13.387 4.919   12.785  0.36 22.12 ?  25  GLU   A CG   1 
ATOM   663  C  CD   A GLU   A 1 25  ? 14.556 6.440   14.517  0.64 24.96 ?  25  GLU   A CD   1 
ATOM   664  C  CD   B GLU   A 1 25  ? 13.892 6.026   13.690  0.36 24.04 ?  25  GLU   A CD   1 
ATOM   665  O  OE1  A GLU   A 1 25  ? 14.597 6.279   15.756  0.64 25.65 ?  25  GLU   A OE1  1 
ATOM   666  O  OE1  B GLU   A 1 25  ? 13.877 5.835   14.925  0.36 24.74 ?  25  GLU   A OE1  1 
ATOM   667  O  OE2  A GLU   A 1 25  ? 15.162 7.363   13.933  0.64 26.40 -1 25  GLU   A OE2  1 
ATOM   668  O  OE2  B GLU   A 1 25  ? 14.316 7.078   13.168  0.36 24.86 -1 25  GLU   A OE2  1 
ATOM   669  H  H    A GLU   A 1 25  ? 15.545 3.812   12.173  0.64 19.31 ?  25  GLU   A H    1 
ATOM   670  H  H    B GLU   A 1 25  ? 15.417 3.354   11.520  0.36 20.44 ?  25  GLU   A H    1 
ATOM   671  H  HA   A GLU   A 1 25  ? 15.936 4.324   14.717  0.64 20.94 ?  25  GLU   A HA   1 
ATOM   672  H  HA   B GLU   A 1 25  ? 15.578 4.061   14.049  0.36 21.90 ?  25  GLU   A HA   1 
ATOM   673  H  HB2  A GLU   A 1 25  ? 13.602 3.440   13.386  0.64 23.53 ?  25  GLU   A HB2  1 
ATOM   674  H  HB2  B GLU   A 1 25  ? 13.426 2.884   12.651  0.36 24.02 ?  25  GLU   A HB2  1 
ATOM   675  H  HB3  A GLU   A 1 25  ? 13.602 3.845   14.923  0.64 23.53 ?  25  GLU   A HB3  1 
ATOM   676  H  HB3  B GLU   A 1 25  ? 13.300 3.404   14.147  0.36 24.02 ?  25  GLU   A HB3  1 
ATOM   677  H  HG2  A GLU   A 1 25  ? 14.019 5.586   12.754  0.64 26.94 ?  25  GLU   A HG2  1 
ATOM   678  H  HG2  B GLU   A 1 25  ? 13.787 5.047   11.911  0.36 26.55 ?  25  GLU   A HG2  1 
ATOM   679  H  HG3  A GLU   A 1 25  ? 12.815 5.647   13.790  0.64 26.94 ?  25  GLU   A HG3  1 
ATOM   680  H  HG3  B GLU   A 1 25  ? 12.422 4.993   12.725  0.36 26.55 ?  25  GLU   A HG3  1 
ATOM   681  N  N    A GLU   A 1 26  ? 15.712 1.241   13.990  0.64 16.26 ?  26  GLU   A N    1 
ATOM   682  N  N    B GLU   A 1 26  ? 15.578 0.908   13.500  0.36 17.51 ?  26  GLU   A N    1 
ATOM   683  C  CA   A GLU   A 1 26  ? 15.991 -0.089  14.519  0.64 16.50 ?  26  GLU   A CA   1 
ATOM   684  C  CA   B GLU   A 1 26  ? 15.942 -0.362  14.122  0.36 17.53 ?  26  GLU   A CA   1 
ATOM   685  C  C    A GLU   A 1 26  ? 17.415 -0.178  15.055  0.64 16.15 ?  26  GLU   A C    1 
ATOM   686  C  C    B GLU   A 1 26  ? 17.342 -0.306  14.719  0.36 16.70 ?  26  GLU   A C    1 
ATOM   687  O  O    A GLU   A 1 26  ? 17.646 -0.673  16.163  0.64 16.48 ?  26  GLU   A O    1 
ATOM   688  O  O    B GLU   A 1 26  ? 17.588 -0.855  15.799  0.36 16.67 ?  26  GLU   A O    1 
ATOM   689  C  CB   A GLU   A 1 26  ? 15.772 -1.140  13.431  0.64 17.83 ?  26  GLU   A CB   1 
ATOM   690  C  CB   B GLU   A 1 26  ? 15.865 -1.497  13.100  0.36 18.55 ?  26  GLU   A CB   1 
ATOM   691  C  CG   A GLU   A 1 26  ? 14.333 -1.565  13.226  0.64 20.92 ?  26  GLU   A CG   1 
ATOM   692  C  CG   B GLU   A 1 26  ? 14.499 -2.139  12.964  0.36 18.94 ?  26  GLU   A CG   1 
ATOM   693  C  CD   A GLU   A 1 26  ? 13.765 -2.361  14.377  0.64 22.71 ?  26  GLU   A CD   1 
ATOM   694  C  CD   B GLU   A 1 26  ? 14.037 -2.804  14.253  0.36 18.50 ?  26  GLU   A CD   1 
ATOM   695  O  OE1  A GLU   A 1 26  ? 14.445 -3.283  14.875  0.64 22.96 ?  26  GLU   A OE1  1 
ATOM   696  O  OE1  B GLU   A 1 26  ? 14.374 -3.985  14.504  0.36 18.62 ?  26  GLU   A OE1  1 
ATOM   697  O  OE2  A GLU   A 1 26  ? 12.627 -2.050  14.778  0.64 23.81 -1 26  GLU   A OE2  1 
ATOM   698  O  OE2  B GLU   A 1 26  ? 13.347 -2.132  15.035  0.36 17.71 -1 26  GLU   A OE2  1 
ATOM   699  H  H    A GLU   A 1 26  ? 15.553 1.268   13.146  0.64 19.51 ?  26  GLU   A H    1 
ATOM   700  H  H    B GLU   A 1 26  ? 15.385 0.857   12.664  0.36 21.01 ?  26  GLU   A H    1 
ATOM   701  H  HA   A GLU   A 1 26  ? 15.382 -0.274  15.246  0.64 19.80 ?  26  GLU   A HA   1 
ATOM   702  H  HA   B GLU   A 1 26  ? 15.319 -0.550  14.841  0.36 21.04 ?  26  GLU   A HA   1 
ATOM   703  H  HB2  A GLU   A 1 26  ? 16.087 -0.779  12.583  0.64 21.40 ?  26  GLU   A HB2  1 
ATOM   704  H  HB2  B GLU   A 1 26  ? 16.117 -1.150  12.232  0.36 22.26 ?  26  GLU   A HB2  1 
ATOM   705  H  HB3  A GLU   A 1 26  ? 16.288 -1.929  13.654  0.64 21.40 ?  26  GLU   A HB3  1 
ATOM   706  H  HB3  B GLU   A 1 26  ? 16.488 -2.194  13.366  0.36 22.26 ?  26  GLU   A HB3  1 
ATOM   707  H  HG2  A GLU   A 1 26  ? 13.779 -0.782  13.151  0.64 25.10 ?  26  GLU   A HG2  1 
ATOM   708  H  HG2  B GLU   A 1 26  ? 13.858 -1.455  12.697  0.36 22.72 ?  26  GLU   A HG2  1 
ATOM   709  H  HG3  A GLU   A 1 26  ? 14.274 -2.103  12.421  0.64 25.10 ?  26  GLU   A HG3  1 
ATOM   710  H  HG3  B GLU   A 1 26  ? 14.538 -2.833  12.293  0.36 22.72 ?  26  GLU   A HG3  1 
ATOM   711  N  N    A ALA   A 1 27  ? 18.391 0.290   14.272  0.64 15.33 ?  27  ALA   A N    1 
ATOM   712  N  N    B ALA   A 1 27  ? 18.281 0.338   14.022  0.36 15.70 ?  27  ALA   A N    1 
ATOM   713  C  CA   A ALA   A 1 27  ? 19.781 0.215   14.710  0.64 15.77 ?  27  ALA   A CA   1 
ATOM   714  C  CA   B ALA   A 1 27  ? 19.655 0.383   14.512  0.36 15.67 ?  27  ALA   A CA   1 
ATOM   715  C  C    A ALA   A 1 27  ? 19.999 1.018   15.986  0.64 17.05 ?  27  ALA   A C    1 
ATOM   716  C  C    B ALA   A 1 27  ? 19.763 1.212   15.787  0.36 16.62 ?  27  ALA   A C    1 
ATOM   717  O  O    A ALA   A 1 27  ? 20.687 0.561   16.906  0.64 17.43 ?  27  ALA   A O    1 
ATOM   718  O  O    B ALA   A 1 27  ? 20.436 0.807   16.742  0.36 16.68 ?  27  ALA   A O    1 
ATOM   719  C  CB   A ALA   A 1 27  ? 20.715 0.701   13.598  0.64 15.46 ?  27  ALA   A CB   1 
ATOM   720  C  CB   B ALA   A 1 27  ? 20.578 0.937   13.426  0.36 15.04 ?  27  ALA   A CB   1 
ATOM   721  H  H    A ALA   A 1 27  ? 18.278 0.647   13.499  0.64 18.40 ?  27  ALA   A H    1 
ATOM   722  H  H    B ALA   A 1 27  ? 18.148 0.746   13.277  0.36 18.85 ?  27  ALA   A H    1 
ATOM   723  H  HA   A ALA   A 1 27  ? 20.003 -0.710  14.900  0.64 18.92 ?  27  ALA   A HA   1 
ATOM   724  H  HA   B ALA   A 1 27  ? 19.943 -0.518  14.717  0.36 18.80 ?  27  ALA   A HA   1 
ATOM   725  H  HB1  A ALA   A 1 27  ? 21.636 0.641   13.908  0.64 18.56 ?  27  ALA   A HB1  1 
ATOM   726  H  HB1  B ALA   A 1 27  ? 21.486 0.957   13.766  0.36 18.05 ?  27  ALA   A HB1  1 
ATOM   727  H  HB2  A ALA   A 1 27  ? 20.597 0.136   12.817  0.64 18.56 ?  27  ALA   A HB2  1 
ATOM   728  H  HB2  B ALA   A 1 27  ? 20.529 0.360   12.647  0.36 18.05 ?  27  ALA   A HB2  1 
ATOM   729  H  HB3  A ALA   A 1 27  ? 20.501 1.619   13.379  0.64 18.56 ?  27  ALA   A HB3  1 
ATOM   730  H  HB3  B ALA   A 1 27  ? 20.291 1.833   13.193  0.36 18.05 ?  27  ALA   A HB3  1 
ATOM   731  N  N    A LYS   A 1 28  ? 19.417 2.217   16.065  0.64 18.92 ?  28  LYS   A N    1 
ATOM   732  N  N    B LYS   A 1 28  ? 19.098 2.369   15.828  0.36 18.16 ?  28  LYS   A N    1 
ATOM   733  C  CA   A LYS   A 1 28  ? 19.570 3.026   17.270  0.64 21.27 ?  28  LYS   A CA   1 
ATOM   734  C  CA   B LYS   A 1 28  ? 19.222 3.254   16.983  0.36 19.98 ?  28  LYS   A CA   1 
ATOM   735  C  C    A LYS   A 1 28  ? 19.013 2.306   18.492  0.64 22.67 ?  28  LYS   A C    1 
ATOM   736  C  C    B LYS   A 1 28  ? 18.706 2.603   18.259  0.36 21.46 ?  28  LYS   A C    1 
ATOM   737  O  O    A LYS   A 1 28  ? 19.570 2.414   19.591  0.64 23.86 ?  28  LYS   A O    1 
ATOM   738  O  O    B LYS   A 1 28  ? 19.167 2.941   19.355  0.36 21.75 ?  28  LYS   A O    1 
ATOM   739  C  CB   A LYS   A 1 28  ? 18.916 4.399   17.083  0.64 22.93 ?  28  LYS   A CB   1 
ATOM   740  C  CB   B LYS   A 1 28  ? 18.472 4.560   16.725  0.36 20.90 ?  28  LYS   A CB   1 
ATOM   741  C  CG   A LYS   A 1 28  ? 19.715 5.340   16.188  0.64 24.25 ?  28  LYS   A CG   1 
ATOM   742  C  CG   B LYS   A 1 28  ? 19.068 5.404   15.616  0.36 21.92 ?  28  LYS   A CG   1 
ATOM   743  C  CD   A LYS   A 1 28  ? 19.216 6.777   16.267  0.64 26.14 ?  28  LYS   A CD   1 
ATOM   744  C  CD   B LYS   A 1 28  ? 18.315 6.713   15.457  0.36 23.05 ?  28  LYS   A CD   1 
ATOM   745  C  CE   A LYS   A 1 28  ? 17.925 6.965   15.496  0.64 27.64 ?  28  LYS   A CE   1 
ATOM   746  C  CE   B LYS   A 1 28  ? 18.915 7.573   14.358  0.36 23.99 ?  28  LYS   A CE   1 
ATOM   747  N  NZ   A LYS   A 1 28  ? 17.515 8.396   15.458  0.64 28.46 ?  28  LYS   A NZ   1 
ATOM   748  N  NZ   B LYS   A 1 28  ? 18.252 8.904   14.263  0.36 24.45 ?  28  LYS   A NZ   1 
ATOM   749  H  H    A LYS   A 1 28  ? 18.943 2.576   15.448  0.64 22.70 ?  28  LYS   A H    1 
ATOM   750  H  H    B LYS   A 1 28  ? 18.579 2.659   15.209  0.36 21.79 ?  28  LYS   A H    1 
ATOM   751  H  HA   A LYS   A 1 28  ? 20.511 3.172   17.437  0.64 25.53 ?  28  LYS   A HA   1 
ATOM   752  H  HA   B LYS   A 1 28  ? 20.156 3.469   17.117  0.36 23.98 ?  28  LYS   A HA   1 
ATOM   753  H  HB2  A LYS   A 1 28  ? 18.044 4.283   16.679  0.64 27.52 ?  28  LYS   A HB2  1 
ATOM   754  H  HB2  B LYS   A 1 28  ? 17.557 4.351   16.481  0.36 25.08 ?  28  LYS   A HB2  1 
ATOM   755  H  HB3  A LYS   A 1 28  ? 18.824 4.829   17.948  0.64 27.52 ?  28  LYS   A HB3  1 
ATOM   756  H  HB3  B LYS   A 1 28  ? 18.481 5.090   17.538  0.36 25.08 ?  28  LYS   A HB3  1 
ATOM   757  H  HG2  A LYS   A 1 28  ? 20.644 5.331   16.463  0.64 29.10 ?  28  LYS   A HG2  1 
ATOM   758  H  HG2  B LYS   A 1 28  ? 19.991 5.607   15.830  0.36 26.30 ?  28  LYS   A HG2  1 
ATOM   759  H  HG3  A LYS   A 1 28  ? 19.636 5.047   15.267  0.64 29.10 ?  28  LYS   A HG3  1 
ATOM   760  H  HG3  B LYS   A 1 28  ? 19.019 4.918   14.778  0.36 26.30 ?  28  LYS   A HG3  1 
ATOM   761  H  HD2  A LYS   A 1 28  ? 19.052 7.011   17.194  0.64 31.36 ?  28  LYS   A HD2  1 
ATOM   762  H  HD2  B LYS   A 1 28  ? 17.391 6.525   15.228  0.36 27.66 ?  28  LYS   A HD2  1 
ATOM   763  H  HD3  A LYS   A 1 28  ? 19.884 7.370   15.886  0.64 31.36 ?  28  LYS   A HD3  1 
ATOM   764  H  HD3  B LYS   A 1 28  ? 18.360 7.209   16.290  0.36 27.66 ?  28  LYS   A HD3  1 
ATOM   765  H  HE2  A LYS   A 1 28  ? 18.050 6.661   14.583  0.64 33.17 ?  28  LYS   A HE2  1 
ATOM   766  H  HE2  B LYS   A 1 28  ? 19.856 7.715   14.545  0.36 28.79 ?  28  LYS   A HE2  1 
ATOM   767  H  HE3  A LYS   A 1 28  ? 17.219 6.458   15.925  0.64 33.17 ?  28  LYS   A HE3  1 
ATOM   768  H  HE3  B LYS   A 1 28  ? 18.810 7.119   13.507  0.36 28.79 ?  28  LYS   A HE3  1 
ATOM   769  H  HZ1  A LYS   A 1 28  ? 16.757 8.483   15.001  0.64 34.15 ?  28  LYS   A HZ1  1 
ATOM   770  H  HZ1  B LYS   A 1 28  ? 18.624 9.383   13.612  0.36 29.34 ?  28  LYS   A HZ1  1 
ATOM   771  H  HZ2  A LYS   A 1 28  ? 17.392 8.698   16.286  0.64 34.15 ?  28  LYS   A HZ2  1 
ATOM   772  H  HZ2  B LYS   A 1 28  ? 17.386 8.801   14.087  0.36 29.34 ?  28  LYS   A HZ2  1 
ATOM   773  H  HZ3  A LYS   A 1 28  ? 18.148 8.883   15.064  0.64 34.15 ?  28  LYS   A HZ3  1 
ATOM   774  H  HZ3  B LYS   A 1 28  ? 18.341 9.343   15.032  0.36 29.34 ?  28  LYS   A HZ3  1 
ATOM   775  N  N    A LYS   A 1 29  ? 17.929 1.546   18.317  0.64 23.55 ?  29  LYS   A N    1 
ATOM   776  N  N    B LYS   A 1 29  ? 17.748 1.685   18.143  0.36 22.80 ?  29  LYS   A N    1 
ATOM   777  C  CA   A LYS   A 1 29  ? 17.321 0.832   19.436  0.64 25.46 ?  29  LYS   A CA   1 
ATOM   778  C  CA   B LYS   A 1 29  ? 17.161 1.033   19.308  0.36 24.69 ?  29  LYS   A CA   1 
ATOM   779  C  C    A LYS   A 1 29  ? 18.131 -0.404  19.817  0.64 25.02 ?  29  LYS   A C    1 
ATOM   780  C  C    B LYS   A 1 29  ? 17.935 -0.215  19.717  0.36 24.59 ?  29  LYS   A C    1 
ATOM   781  O  O    A LYS   A 1 29  ? 18.436 -0.619  20.996  0.64 26.01 ?  29  LYS   A O    1 
ATOM   782  O  O    B LYS   A 1 29  ? 18.205 -0.420  20.905  0.36 25.23 ?  29  LYS   A O    1 
ATOM   783  C  CB   A LYS   A 1 29  ? 15.889 0.428   19.073  0.64 28.18 ?  29  LYS   A CB   1 
ATOM   784  C  CB   B LYS   A 1 29  ? 15.705 0.664   19.009  0.36 26.77 ?  29  LYS   A CB   1 
ATOM   785  C  CG   A LYS   A 1 29  ? 15.126 -0.265  20.192  0.64 30.93 ?  29  LYS   A CG   1 
ATOM   786  C  CG   B LYS   A 1 29  ? 14.959 0.018   20.169  0.36 28.76 ?  29  LYS   A CG   1 
ATOM   787  C  CD   A LYS   A 1 29  ? 14.780 0.705   21.309  0.64 33.37 ?  29  LYS   A CD   1 
ATOM   788  C  CD   B LYS   A 1 29  ? 14.636 1.027   21.257  0.36 30.47 ?  29  LYS   A CD   1 
ATOM   789  C  CE   A LYS   A 1 29  ? 13.907 0.046   22.365  0.64 35.04 ?  29  LYS   A CE   1 
ATOM   790  C  CE   B LYS   A 1 29  ? 13.741 0.421   22.327  0.36 31.70 ?  29  LYS   A CE   1 
ATOM   791  N  NZ   A LYS   A 1 29  ? 13.494 1.011   23.420  0.64 36.01 ?  29  LYS   A NZ   1 
ATOM   792  N  NZ   B LYS   A 1 29  ? 13.409 1.406   23.392  0.36 32.42 ?  29  LYS   A NZ   1 
ATOM   793  H  H    A LYS   A 1 29  ? 17.530 1.425   17.564  0.64 28.26 ?  29  LYS   A H    1 
ATOM   794  H  H    B LYS   A 1 29  ? 17.415 1.424   17.395  0.36 27.36 ?  29  LYS   A H    1 
ATOM   795  H  HA   A LYS   A 1 29  ? 17.280 1.419   20.207  0.64 30.55 ?  29  LYS   A HA   1 
ATOM   796  H  HA   B LYS   A 1 29  ? 17.170 1.648   20.055  0.36 29.63 ?  29  LYS   A HA   1 
ATOM   797  H  HB2  A LYS   A 1 29  ? 15.391 1.224   18.831  0.64 33.81 ?  29  LYS   A HB2  1 
ATOM   798  H  HB2  B LYS   A 1 29  ? 15.228 1.471   18.768  0.36 32.12 ?  29  LYS   A HB2  1 
ATOM   799  H  HB3  A LYS   A 1 29  ? 15.918 -0.181  18.319  0.64 33.81 ?  29  LYS   A HB3  1 
ATOM   800  H  HB3  B LYS   A 1 29  ? 15.691 0.040   18.268  0.36 32.12 ?  29  LYS   A HB3  1 
ATOM   801  H  HG2  A LYS   A 1 29  ? 14.298 -0.626  19.837  0.64 37.11 ?  29  LYS   A HG2  1 
ATOM   802  H  HG2  B LYS   A 1 29  ? 14.125 -0.350  19.840  0.36 34.51 ?  29  LYS   A HG2  1 
ATOM   803  H  HG3  A LYS   A 1 29  ? 15.667 -0.979  20.565  0.64 37.11 ?  29  LYS   A HG3  1 
ATOM   804  H  HG3  B LYS   A 1 29  ? 15.503 -0.686  20.558  0.36 34.51 ?  29  LYS   A HG3  1 
ATOM   805  H  HD2  A LYS   A 1 29  ? 15.597 1.009   21.735  0.64 40.04 ?  29  LYS   A HD2  1 
ATOM   806  H  HD2  B LYS   A 1 29  ? 15.459 1.320   21.678  0.36 36.56 ?  29  LYS   A HD2  1 
ATOM   807  H  HD3  A LYS   A 1 29  ? 14.294 1.459   20.938  0.64 40.04 ?  29  LYS   A HD3  1 
ATOM   808  H  HD3  B LYS   A 1 29  ? 14.172 1.783   20.864  0.36 36.56 ?  29  LYS   A HD3  1 
ATOM   809  H  HE2  A LYS   A 1 29  ? 13.107 -0.306  21.943  0.64 42.05 ?  29  LYS   A HE2  1 
ATOM   810  H  HE2  B LYS   A 1 29  ? 12.912 0.123   21.919  0.36 38.04 ?  29  LYS   A HE2  1 
ATOM   811  H  HE3  A LYS   A 1 29  ? 14.405 -0.672  22.787  0.64 42.05 ?  29  LYS   A HE3  1 
ATOM   812  H  HE3  B LYS   A 1 29  ? 14.199 -0.329  22.738  0.36 38.04 ?  29  LYS   A HE3  1 
ATOM   813  H  HZ1  A LYS   A 1 29  ? 12.984 0.601   24.024  0.64 43.21 ?  29  LYS   A HZ1  1 
ATOM   814  H  HZ1  B LYS   A 1 29  ? 12.886 1.027   24.004  0.36 38.90 ?  29  LYS   A HZ1  1 
ATOM   815  H  HZ2  A LYS   A 1 29  ? 14.212 1.345   23.825  0.64 43.21 ?  29  LYS   A HZ2  1 
ATOM   816  H  HZ2  B LYS   A 1 29  ? 14.155 1.691   23.785  0.36 38.90 ?  29  LYS   A HZ2  1 
ATOM   817  H  HZ3  A LYS   A 1 29  ? 13.030 1.678   23.057  0.64 43.21 ?  29  LYS   A HZ3  1 
ATOM   818  H  HZ3  B LYS   A 1 29  ? 12.983 2.103   23.039  0.36 38.90 ?  29  LYS   A HZ3  1 
ATOM   819  N  N    A VAL   A 1 30  ? 18.470 -1.234  18.831  0.64 23.69 ?  30  VAL   A N    1 
ATOM   820  N  N    B VAL   A 1 30  ? 18.288 -1.060  18.748  0.36 24.01 ?  30  VAL   A N    1 
ATOM   821  C  CA   A VAL   A 1 30  ? 19.119 -2.511  19.109  0.64 22.88 ?  30  VAL   A CA   1 
ATOM   822  C  CA   B VAL   A 1 30  ? 18.924 -2.334  19.067  0.36 23.58 ?  30  VAL   A CA   1 
ATOM   823  C  C    A VAL   A 1 30  ? 20.618 -2.345  19.336  0.64 21.60 ?  30  VAL   A C    1 
ATOM   824  C  C    B VAL   A 1 30  ? 20.418 -2.166  19.322  0.36 23.10 ?  30  VAL   A C    1 
ATOM   825  O  O    A VAL   A 1 30  ? 21.210 -3.068  20.145  0.64 21.82 ?  30  VAL   A O    1 
ATOM   826  O  O    B VAL   A 1 30  ? 20.990 -2.871  20.161  0.36 23.00 ?  30  VAL   A O    1 
ATOM   827  C  CB   A VAL   A 1 30  ? 18.830 -3.497  17.961  0.64 23.45 ?  30  VAL   A CB   1 
ATOM   828  C  CB   B VAL   A 1 30  ? 18.655 -3.352  17.945  0.36 23.70 ?  30  VAL   A CB   1 
ATOM   829  C  CG1  A VAL   A 1 30  ? 19.602 -4.797  18.154  0.64 24.12 ?  30  VAL   A CG1  1 
ATOM   830  C  CG1  B VAL   A 1 30  ? 19.371 -4.666  18.228  0.36 23.96 ?  30  VAL   A CG1  1 
ATOM   831  C  CG2  A VAL   A 1 30  ? 17.336 -3.771  17.856  0.64 24.12 ?  30  VAL   A CG2  1 
ATOM   832  C  CG2  B VAL   A 1 30  ? 17.160 -3.578  17.780  0.36 23.90 ?  30  VAL   A CG2  1 
ATOM   833  H  H    A VAL   A 1 30  ? 18.326 -1.085  17.997  0.64 28.42 ?  30  VAL   A H    1 
ATOM   834  H  H    B VAL   A 1 30  ? 18.167 -0.923  17.907  0.36 28.82 ?  30  VAL   A H    1 
ATOM   835  H  HA   A VAL   A 1 30  ? 18.732 -2.885  19.914  0.64 27.46 ?  30  VAL   A HA   1 
ATOM   836  H  HA   B VAL   A 1 30  ? 18.522 -2.683  19.875  0.36 28.30 ?  30  VAL   A HA   1 
ATOM   837  H  HB   A VAL   A 1 30  ? 19.121 -3.104  17.123  0.64 28.14 ?  30  VAL   A HB   1 
ATOM   838  H  HB   B VAL   A 1 30  ? 18.999 -3.003  17.108  0.36 28.44 ?  30  VAL   A HB   1 
ATOM   839  H  HG11 A VAL   A 1 30  ? 19.239 -5.470  17.556  0.64 28.94 ?  30  VAL   A HG11 1 
ATOM   840  H  HG11 B VAL   A 1 30  ? 19.006 -5.355  17.650  0.36 28.76 ?  30  VAL   A HG11 1 
ATOM   841  H  HG12 A VAL   A 1 30  ? 20.537 -4.647  17.951  0.64 28.94 ?  30  VAL   A HG12 1 
ATOM   842  H  HG12 B VAL   A 1 30  ? 20.318 -4.556  18.051  0.36 28.76 ?  30  VAL   A HG12 1 
ATOM   843  H  HG13 A VAL   A 1 30  ? 19.503 -5.089  19.074  0.64 28.94 ?  30  VAL   A HG13 1 
ATOM   844  H  HG13 B VAL   A 1 30  ? 19.231 -4.906  19.156  0.36 28.76 ?  30  VAL   A HG13 1 
ATOM   845  H  HG21 A VAL   A 1 30  ? 17.183 -4.424  17.155  0.64 28.94 ?  30  VAL   A HG21 1 
ATOM   846  H  HG21 B VAL   A 1 30  ? 17.016 -4.264  17.109  0.36 28.67 ?  30  VAL   A HG21 1 
ATOM   847  H  HG22 A VAL   A 1 30  ? 17.019 -4.116  18.705  0.64 28.94 ?  30  VAL   A HG22 1 
ATOM   848  H  HG22 B VAL   A 1 30  ? 16.790 -3.864  18.630  0.36 28.67 ?  30  VAL   A HG22 1 
ATOM   849  H  HG23 A VAL   A 1 30  ? 16.879 -2.943  17.643  0.64 28.94 ?  30  VAL   A HG23 1 
ATOM   850  H  HG23 B VAL   A 1 30  ? 16.746 -2.749  17.499  0.36 28.67 ?  30  VAL   A HG23 1 
ATOM   851  N  N    A LYS   A 1 31  ? 21.253 -1.406  18.643  0.64 20.62 ?  31  LYS   A N    1 
ATOM   852  N  N    B LYS   A 1 31  ? 21.065 -1.238  18.627  0.36 22.97 ?  31  LYS   A N    1 
ATOM   853  C  CA   A LYS   A 1 31  ? 22.706 -1.297  18.604  0.64 21.16 ?  31  LYS   A CA   1 
ATOM   854  C  CA   B LYS   A 1 31  ? 22.519 -1.143  18.592  0.36 23.31 ?  31  LYS   A CA   1 
ATOM   855  C  C    A LYS   A 1 31  ? 23.320 -2.654  18.247  0.64 18.86 ?  31  LYS   A C    1 
ATOM   856  C  C    B LYS   A 1 31  ? 23.121 -2.517  18.286  0.36 21.24 ?  31  LYS   A C    1 
ATOM   857  O  O    A LYS   A 1 31  ? 24.107 -3.211  19.019  0.64 19.80 ?  31  LYS   A O    1 
ATOM   858  O  O    B LYS   A 1 31  ? 23.863 -3.072  19.102  0.36 21.76 ?  31  LYS   A O    1 
ATOM   859  C  CB   A LYS   A 1 31  ? 23.276 -0.764  19.912  0.64 25.45 ?  31  LYS   A CB   1 
ATOM   860  C  CB   B LYS   A 1 31  ? 23.087 -0.575  19.885  0.36 26.12 ?  31  LYS   A CB   1 
ATOM   861  C  CG   A LYS   A 1 31  ? 22.592 0.499   20.416  0.64 29.99 ?  31  LYS   A CG   1 
ATOM   862  C  CG   B LYS   A 1 31  ? 22.450 0.726   20.326  0.36 29.07 ?  31  LYS   A CG   1 
ATOM   863  C  CD   A LYS   A 1 31  ? 23.602 1.577   20.785  0.64 33.47 ?  31  LYS   A CD   1 
ATOM   864  C  CD   B LYS   A 1 31  ? 23.482 1.659   20.932  0.36 31.41 ?  31  LYS   A CD   1 
ATOM   865  C  CE   A LYS   A 1 31  ? 22.986 2.635   21.689  0.64 35.90 ?  31  LYS   A CE   1 
ATOM   866  C  CE   B LYS   A 1 31  ? 22.829 2.732   21.783  0.36 33.07 ?  31  LYS   A CE   1 
ATOM   867  N  NZ   A LYS   A 1 31  ? 21.784 3.279   21.091  0.64 37.19 ?  31  LYS   A NZ   1 
ATOM   868  N  NZ   B LYS   A 1 31  ? 21.689 3.389   21.088  0.36 33.94 ?  31  LYS   A NZ   1 
ATOM   869  H  H    A LYS   A 1 31  ? 20.850 -0.810  18.177  0.64 24.74 ?  31  LYS   A H    1 
ATOM   870  H  H    B LYS   A 1 31  ? 20.672 -0.641  18.157  0.36 27.56 ?  31  LYS   A H    1 
ATOM   871  H  HA   A LYS   A 1 31  ? 22.942 -0.672  17.907  0.64 25.39 ?  31  LYS   A HA   1 
ATOM   872  H  HA   B LYS   A 1 31  ? 22.765 -0.540  17.878  0.36 27.97 ?  31  LYS   A HA   1 
ATOM   873  H  HB2  A LYS   A 1 31  ? 23.185 -1.444  20.593  0.64 30.54 ?  31  LYS   A HB2  1 
ATOM   874  H  HB2  B LYS   A 1 31  ? 22.952 -1.222  20.591  0.36 31.35 ?  31  LYS   A HB2  1 
ATOM   875  H  HB3  A LYS   A 1 31  ? 24.215 -0.557  19.776  0.64 30.54 ?  31  LYS   A HB3  1 
ATOM   876  H  HB3  B LYS   A 1 31  ? 24.038 -0.413  19.765  0.36 31.35 ?  31  LYS   A HB3  1 
ATOM   877  H  HG2  A LYS   A 1 31  ? 22.014 0.851   19.721  0.64 35.99 ?  31  LYS   A HG2  1 
ATOM   878  H  HG2  B LYS   A 1 31  ? 22.052 1.166   19.558  0.36 34.89 ?  31  LYS   A HG2  1 
ATOM   879  H  HG3  A LYS   A 1 31  ? 22.073 0.286   21.208  0.64 35.99 ?  31  LYS   A HG3  1 
ATOM   880  H  HG3  B LYS   A 1 31  ? 21.773 0.542   20.997  0.36 34.89 ?  31  LYS   A HG3  1 
ATOM   881  H  HD2  A LYS   A 1 31  ? 24.347 1.172   21.256  0.64 40.16 ?  31  LYS   A HD2  1 
ATOM   882  H  HD2  B LYS   A 1 31  ? 24.085 1.147   21.495  0.36 37.69 ?  31  LYS   A HD2  1 
ATOM   883  H  HD3  A LYS   A 1 31  ? 23.915 2.013   19.976  0.64 40.16 ?  31  LYS   A HD3  1 
ATOM   884  H  HD3  B LYS   A 1 31  ? 23.977 2.094   20.219  0.36 37.69 ?  31  LYS   A HD3  1 
ATOM   885  H  HE2  A LYS   A 1 31  ? 22.719 2.220   22.524  0.64 43.07 ?  31  LYS   A HE2  1 
ATOM   886  H  HE2  B LYS   A 1 31  ? 22.496 2.327   22.598  0.36 39.68 ?  31  LYS   A HE2  1 
ATOM   887  H  HE3  A LYS   A 1 31  ? 23.644 3.328   21.858  0.64 43.07 ?  31  LYS   A HE3  1 
ATOM   888  H  HE3  B LYS   A 1 31  ? 23.486 3.413   21.994  0.36 39.68 ?  31  LYS   A HE3  1 
ATOM   889  H  HZ1  A LYS   A 1 31  ? 21.462 3.896   21.646  0.64 44.63 ?  31  LYS   A HZ1  1 
ATOM   890  H  HZ1  B LYS   A 1 31  ? 21.375 4.057   21.584  0.36 40.73 ?  31  LYS   A HZ1  1 
ATOM   891  H  HZ2  A LYS   A 1 31  ? 21.998 3.667   20.319  0.64 44.63 ?  31  LYS   A HZ2  1 
ATOM   892  H  HZ2  B LYS   A 1 31  ? 21.956 3.711   20.303  0.36 40.73 ?  31  LYS   A HZ2  1 
ATOM   893  H  HZ3  A LYS   A 1 31  ? 21.153 2.668   20.942  0.64 44.63 ?  31  LYS   A HZ3  1 
ATOM   894  H  HZ3  B LYS   A 1 31  ? 21.035 2.800   20.951  0.36 40.73 ?  31  LYS   A HZ3  1 
ATOM   895  N  N    A PRO   A 1 32  ? 22.978 -3.204  17.086  0.64 17.16 ?  32  PRO   A N    1 
ATOM   896  N  N    B PRO   A 1 32  ? 22.817 -3.088  17.125  0.36 18.97 ?  32  PRO   A N    1 
ATOM   897  C  CA   A PRO   A 1 32  ? 23.449 -4.544  16.737  0.64 17.08 ?  32  PRO   A CA   1 
ATOM   898  C  CA   B PRO   A 1 32  ? 23.295 -4.437  16.818  0.36 17.91 ?  32  PRO   A CA   1 
ATOM   899  C  C    A PRO   A 1 32  ? 24.949 -4.566  16.521  0.64 16.96 ?  32  PRO   A C    1 
ATOM   900  C  C    B PRO   A 1 32  ? 24.801 -4.446  16.622  0.36 16.95 ?  32  PRO   A C    1 
ATOM   901  O  O    A PRO   A 1 32  ? 25.593 -3.540  16.283  0.64 16.82 ?  32  PRO   A O    1 
ATOM   902  O  O    B PRO   A 1 32  ? 25.455 -3.409  16.498  0.36 16.85 ?  32  PRO   A O    1 
ATOM   903  C  CB   A PRO   A 1 32  ? 22.719 -4.832  15.423  0.64 17.10 ?  32  PRO   A CB   1 
ATOM   904  C  CB   B PRO   A 1 32  ? 22.571 -4.768  15.513  0.36 17.94 ?  32  PRO   A CB   1 
ATOM   905  C  CG   A PRO   A 1 32  ? 22.560 -3.480  14.807  0.64 16.28 ?  32  PRO   A CG   1 
ATOM   906  C  CG   B PRO   A 1 32  ? 22.421 -3.446  14.848  0.36 17.93 ?  32  PRO   A CG   1 
ATOM   907  C  CD   A PRO   A 1 32  ? 22.259 -2.573  15.967  0.64 16.32 ?  32  PRO   A CD   1 
ATOM   908  C  CD   B PRO   A 1 32  ? 22.140 -2.476  15.968  0.36 18.18 ?  32  PRO   A CD   1 
ATOM   909  H  HA   A PRO   A 1 32  ? 23.194 -5.191  17.414  0.64 20.50 ?  32  PRO   A HA   1 
ATOM   910  H  HA   B PRO   A 1 32  ? 23.042 -5.065  17.512  0.36 21.50 ?  32  PRO   A HA   1 
ATOM   911  H  HB2  A PRO   A 1 32  ? 23.263 -5.412  14.863  0.64 20.51 ?  32  PRO   A HB2  1 
ATOM   912  H  HB2  B PRO   A 1 32  ? 23.113 -5.369  14.976  0.36 21.53 ?  32  PRO   A HB2  1 
ATOM   913  H  HB3  A PRO   A 1 32  ? 21.857 -5.240  15.605  0.64 20.51 ?  32  PRO   A HB3  1 
ATOM   914  H  HB3  B PRO   A 1 32  ? 21.705 -5.162  15.704  0.36 21.53 ?  32  PRO   A HB3  1 
ATOM   915  H  HG2  A PRO   A 1 32  ? 23.385 -3.226  14.366  0.64 19.53 ?  32  PRO   A HG2  1 
ATOM   916  H  HG2  B PRO   A 1 32  ? 23.246 -3.217  14.391  0.36 21.51 ?  32  PRO   A HG2  1 
ATOM   917  H  HG3  A PRO   A 1 32  ? 21.822 -3.498  14.177  0.64 19.53 ?  32  PRO   A HG3  1 
ATOM   918  H  HG3  B PRO   A 1 32  ? 21.680 -3.478  14.223  0.36 21.51 ?  32  PRO   A HG3  1 
ATOM   919  H  HD2  A PRO   A 1 32  ? 22.609 -1.686  15.788  0.64 19.59 ?  32  PRO   A HD2  1 
ATOM   920  H  HD2  B PRO   A 1 32  ? 22.525 -1.610  15.762  0.36 21.82 ?  32  PRO   A HD2  1 
ATOM   921  H  HD3  A PRO   A 1 32  ? 21.309 -2.557  16.140  0.64 19.59 ?  32  PRO   A HD3  1 
ATOM   922  H  HD3  B PRO   A 1 32  ? 21.187 -2.416  16.125  0.36 21.82 ?  32  PRO   A HD3  1 
ATOM   923  N  N    A THR   A 1 33  ? 25.502 -5.776  16.582  0.64 16.94 ?  33  THR   A N    1 
ATOM   924  N  N    B THR   A 1 33  ? 25.352 -5.659  16.590  0.36 16.38 ?  33  THR   A N    1 
ATOM   925  C  CA   A THR   A 1 33  ? 26.911 -5.951  16.265  0.64 17.13 ?  33  THR   A CA   1 
ATOM   926  C  CA   B THR   A 1 33  ? 26.773 -5.809  16.301  0.36 15.90 ?  33  THR   A CA   1 
ATOM   927  C  C    A THR   A 1 33  ? 27.206 -5.499  14.841  0.64 15.49 ?  33  THR   A C    1 
ATOM   928  C  C    B THR   A 1 33  ? 27.092 -5.340  14.886  0.36 14.86 ?  33  THR   A C    1 
ATOM   929  O  O    A THR   A 1 33  ? 28.260 -4.905  14.577  0.64 15.29 ?  33  THR   A O    1 
ATOM   930  O  O    B THR   A 1 33  ? 28.061 -4.603  14.665  0.36 14.94 ?  33  THR   A O    1 
ATOM   931  C  CB   A THR   A 1 33  ? 27.308 -7.414  16.462  0.64 19.10 ?  33  THR   A CB   1 
ATOM   932  C  CB   B THR   A 1 33  ? 27.188 -7.266  16.496  0.36 16.89 ?  33  THR   A CB   1 
ATOM   933  O  OG1  A THR   A 1 33  ? 27.034 -7.809  17.812  0.64 21.08 ?  33  THR   A OG1  1 
ATOM   934  O  OG1  B THR   A 1 33  ? 26.850 -7.684  17.824  0.36 18.11 ?  33  THR   A OG1  1 
ATOM   935  C  CG2  A THR   A 1 33  ? 28.787 -7.616  16.178  0.64 19.62 ?  33  THR   A CG2  1 
ATOM   936  C  CG2  B THR   A 1 33  ? 28.687 -7.430  16.279  0.36 17.21 ?  33  THR   A CG2  1 
ATOM   937  H  H    A THR   A 1 33  ? 25.087 -6.502  16.788  0.64 20.33 ?  33  THR   A H    1 
ATOM   938  H  H    B THR   A 1 33  ? 24.932 -6.398  16.740  0.36 19.65 ?  33  THR   A H    1 
ATOM   939  H  HA   A THR   A 1 33  ? 27.445 -5.411  16.868  0.64 20.55 ?  33  THR   A HA   1 
ATOM   940  H  HA   B THR   A 1 33  ? 27.281 -5.268  16.925  0.36 19.08 ?  33  THR   A HA   1 
ATOM   941  H  HB   A THR   A 1 33  ? 26.798 -7.975  15.856  0.64 22.92 ?  33  THR   A HB   1 
ATOM   942  H  HB   B THR   A 1 33  ? 26.724 -7.828  15.855  0.36 20.26 ?  33  THR   A HB   1 
ATOM   943  H  HG1  A THR   A 1 33  ? 27.468 -7.328  18.349  0.64 25.30 ?  33  THR   A HG1  1 
ATOM   944  H  HG1  B THR   A 1 33  ? 27.261 -7.213  18.388  0.36 21.74 ?  33  THR   A HG1  1 
ATOM   945  H  HG21 A THR   A 1 33  ? 29.064 -8.494  16.488  0.64 23.54 ?  33  THR   A HG21 1 
ATOM   946  H  HG21 B THR   A 1 33  ? 28.968 -8.315  16.562  0.36 20.65 ?  33  THR   A HG21 1 
ATOM   947  H  HG22 A THR   A 1 33  ? 28.955 -7.550  15.227  0.64 23.54 ?  33  THR   A HG22 1 
ATOM   948  H  HG22 B THR   A 1 33  ? 28.902 -7.318  15.340  0.36 20.65 ?  33  THR   A HG22 1 
ATOM   949  H  HG23 A THR   A 1 33  ? 29.306 -6.942  16.643  0.64 23.54 ?  33  THR   A HG23 1 
ATOM   950  H  HG23 B THR   A 1 33  ? 29.170 -6.768  16.796  0.36 20.65 ?  33  THR   A HG23 1 
ATOM   951  N  N    . VAL   A 1 34  ? 26.282 -5.755  13.914  1.00 14.01 ?  34  VAL   A N    1 
ATOM   952  C  CA   . VAL   A 1 34  ? 26.478 -5.421  12.506  1.00 12.76 ?  34  VAL   A CA   1 
ATOM   953  C  C    . VAL   A 1 34  ? 25.181 -4.859  11.936  1.00 12.20 ?  34  VAL   A C    1 
ATOM   954  O  O    . VAL   A 1 34  ? 24.140 -5.530  11.974  1.00 12.98 ?  34  VAL   A O    1 
ATOM   955  C  CB   . VAL   A 1 34  ? 26.920 -6.633  11.667  1.00 13.44 ?  34  VAL   A CB   1 
ATOM   956  C  CG1  . VAL   A 1 34  ? 27.089 -6.225  10.208  1.00 13.48 ?  34  VAL   A CG1  1 
ATOM   957  C  CG2  . VAL   A 1 34  ? 28.204 -7.258  12.217  1.00 14.69 ?  34  VAL   A CG2  1 
ATOM   958  H  H    A VAL   A 1 34  ? 25.522 -6.119  14.082  0.64 16.81 ?  34  VAL   A H    1 
ATOM   959  H  H    B VAL   A 1 34  ? 25.592 -6.248  14.050  0.36 16.81 ?  34  VAL   A H    1 
ATOM   960  H  HA   . VAL   A 1 34  ? 27.162 -4.732  12.428  1.00 15.31 ?  34  VAL   A HA   1 
ATOM   961  H  HB   . VAL   A 1 34  ? 26.221 -7.303  11.710  1.00 16.13 ?  34  VAL   A HB   1 
ATOM   962  H  HG11 . VAL   A 1 34  ? 27.591 -6.915  9.749   1.00 16.17 ?  34  VAL   A HG11 1 
ATOM   963  H  HG12 . VAL   A 1 34  ? 26.214 -6.128  9.801   1.00 16.17 ?  34  VAL   A HG12 1 
ATOM   964  H  HG13 . VAL   A 1 34  ? 27.570 -5.384  10.169  1.00 16.17 ?  34  VAL   A HG13 1 
ATOM   965  H  HG21 . VAL   A 1 34  ? 28.472 -7.986  11.632  1.00 17.63 ?  34  VAL   A HG21 1 
ATOM   966  H  HG22 . VAL   A 1 34  ? 28.899 -6.584  12.245  1.00 17.63 ?  34  VAL   A HG22 1 
ATOM   967  H  HG23 . VAL   A 1 34  ? 28.035 -7.599  13.109  1.00 17.63 ?  34  VAL   A HG23 1 
ATOM   968  N  N    . VAL   A 1 35  ? 25.249 -3.650  11.382  1.00 11.56 ?  35  VAL   A N    1 
ATOM   969  C  CA   . VAL   A 1 35  ? 24.222 -3.140  10.482  1.00 11.02 ?  35  VAL   A CA   1 
ATOM   970  C  C    . VAL   A 1 35  ? 24.784 -3.147  9.066   1.00 10.55 ?  35  VAL   A C    1 
ATOM   971  O  O    . VAL   A 1 35  ? 25.935 -2.749  8.843   1.00 11.18 ?  35  VAL   A O    1 
ATOM   972  C  CB   . VAL   A 1 35  ? 23.689 -1.744  10.884  1.00 11.58 ?  35  VAL   A CB   1 
ATOM   973  C  CG1  . VAL   A 1 35  ? 24.763 -0.660  10.781  1.00 12.36 ?  35  VAL   A CG1  1 
ATOM   974  C  CG2  . VAL   A 1 35  ? 22.462 -1.381  10.032  1.00 12.31 ?  35  VAL   A CG2  1 
ATOM   975  H  H    . VAL   A 1 35  ? 25.892 -3.094  11.508  1.00 13.87 ?  35  VAL   A H    1 
ATOM   976  H  HA   . VAL   A 1 35  ? 23.465 -3.748  10.497  1.00 13.22 ?  35  VAL   A HA   1 
ATOM   977  H  HB   . VAL   A 1 35  ? 23.392 -1.778  11.804  1.00 13.90 ?  35  VAL   A HB   1 
ATOM   978  H  HG11 . VAL   A 1 35  ? 24.407 0.172   11.136  1.00 14.83 ?  35  VAL   A HG11 1 
ATOM   979  H  HG12 . VAL   A 1 35  ? 25.534 -0.935  11.297  1.00 14.83 ?  35  VAL   A HG12 1 
ATOM   980  H  HG13 . VAL   A 1 35  ? 25.009 -0.541  9.851   1.00 14.83 ?  35  VAL   A HG13 1 
ATOM   981  H  HG21 . VAL   A 1 35  ? 22.100 -0.536  10.335  1.00 14.77 ?  35  VAL   A HG21 1 
ATOM   982  H  HG22 . VAL   A 1 35  ? 22.733 -1.307  9.099   1.00 14.77 ?  35  VAL   A HG22 1 
ATOM   983  H  HG23 . VAL   A 1 35  ? 21.794 -2.080  10.122  1.00 14.77 ?  35  VAL   A HG23 1 
ATOM   984  N  N    . VAL   A 1 36  ? 23.969 -3.597  8.108   1.00 9.84  ?  36  VAL   A N    1 
ATOM   985  C  CA   . VAL   A 1 36  ? 24.352 -3.619  6.703   1.00 9.55  ?  36  VAL   A CA   1 
ATOM   986  C  C    . VAL   A 1 36  ? 23.896 -2.328  6.033   1.00 10.04 ?  36  VAL   A C    1 
ATOM   987  O  O    . VAL   A 1 36  ? 22.733 -1.927  6.159   1.00 10.64 ?  36  VAL   A O    1 
ATOM   988  C  CB   . VAL   A 1 36  ? 23.747 -4.832  5.984   1.00 9.90  ?  36  VAL   A CB   1 
ATOM   989  C  CG1  . VAL   A 1 36  ? 24.003 -4.752  4.498   1.00 10.41 ?  36  VAL   A CG1  1 
ATOM   990  C  CG2  . VAL   A 1 36  ? 24.303 -6.129  6.558   1.00 11.09 ?  36  VAL   A CG2  1 
ATOM   991  H  H    . VAL   A 1 36  ? 23.175 -3.905  8.249   1.00 11.81 ?  36  VAL   A H    1 
ATOM   992  H  HA   . VAL   A 1 36  ? 25.322 -3.680  6.632   1.00 11.46 ?  36  VAL   A HA   1 
ATOM   993  H  HB   . VAL   A 1 36  ? 22.785 -4.830  6.120   1.00 11.88 ?  36  VAL   A HB   1 
ATOM   994  H  HG11 . VAL   A 1 36  ? 23.880 -5.630  4.109   1.00 12.50 ?  36  VAL   A HG11 1 
ATOM   995  H  HG12 . VAL   A 1 36  ? 23.376 -4.125  4.099   1.00 12.50 ?  36  VAL   A HG12 1 
ATOM   996  H  HG13 . VAL   A 1 36  ? 24.913 -4.450  4.351   1.00 12.50 ?  36  VAL   A HG13 1 
ATOM   997  H  HG21 . VAL   A 1 36  ? 23.907 -6.883  6.085   1.00 13.31 ?  36  VAL   A HG21 1 
ATOM   998  H  HG22 . VAL   A 1 36  ? 25.266 -6.142  6.444   1.00 13.31 ?  36  VAL   A HG22 1 
ATOM   999  H  HG23 . VAL   A 1 36  ? 24.081 -6.183  7.501   1.00 13.31 ?  36  VAL   A HG23 1 
ATOM   1000 N  N    . ASN   A 1 37  ? 24.815 -1.692  5.307   1.00 9.54  ?  37  ASN   A N    1 
ATOM   1001 C  CA   . ASN   A 1 37  ? 24.496 -0.571  4.434   1.00 9.24  ?  37  ASN   A CA   1 
ATOM   1002 C  C    . ASN   A 1 37  ? 24.363 -1.048  2.997   1.00 9.12  ?  37  ASN   A C    1 
ATOM   1003 O  O    . ASN   A 1 37  ? 25.151 -1.881  2.527   1.00 9.72  ?  37  ASN   A O    1 
ATOM   1004 C  CB   . ASN   A 1 37  ? 25.575 0.502   4.513   1.00 9.44  ?  37  ASN   A CB   1 
ATOM   1005 C  CG   . ASN   A 1 37  ? 25.256 1.705   3.664   1.00 9.67  ?  37  ASN   A CG   1 
ATOM   1006 O  OD1  . ASN   A 1 37  ? 24.082 2.045   3.470   1.00 10.30 ?  37  ASN   A OD1  1 
ATOM   1007 N  ND2  . ASN   A 1 37  ? 26.300 2.353   3.146   1.00 9.95  ?  37  ASN   A ND2  1 
ATOM   1008 H  H    . ASN   A 1 37  ? 25.654 -1.890  5.316   1.00 11.44 ?  37  ASN   A H    1 
ATOM   1009 H  HA   . ASN   A 1 37  ? 23.657 -0.174  4.711   1.00 11.09 ?  37  ASN   A HA   1 
ATOM   1010 H  HB2  . ASN   A 1 37  ? 25.664 0.797   5.435   1.00 11.32 ?  37  ASN   A HB2  1 
ATOM   1011 H  HB3  . ASN   A 1 37  ? 26.420 0.125   4.208   1.00 11.32 ?  37  ASN   A HB3  1 
ATOM   1012 H  HD21 . ASN   A 1 37  ? 26.171 3.047   2.652   1.00 11.94 ?  37  ASN   A HD21 1 
ATOM   1013 H  HD22 . ASN   A 1 37  ? 27.097 2.090   3.303   1.00 11.94 ?  37  ASN   A HD22 1 
ATOM   1014 N  N    . ALA   A 1 38  ? 23.351 -0.512  2.308   1.00 9.58  ?  38  ALA   A N    1 
ATOM   1015 C  CA   . ALA   A 1 38  ? 23.170 -0.682  0.866   1.00 9.90  ?  38  ALA   A CA   1 
ATOM   1016 C  C    . ALA   A 1 38  ? 24.066 0.331   0.151   1.00 10.00 ?  38  ALA   A C    1 
ATOM   1017 O  O    . ALA   A 1 38  ? 23.637 1.410   -0.276  1.00 10.12 ?  38  ALA   A O    1 
ATOM   1018 C  CB   . ALA   A 1 38  ? 21.706 -0.500  0.492   1.00 11.62 ?  38  ALA   A CB   1 
ATOM   1019 H  H    . ALA   A 1 38  ? 22.750 -0.013  2.669   1.00 11.49 ?  38  ALA   A H    1 
ATOM   1020 H  HA   . ALA   A 1 38  ? 23.447 -1.573  0.610   1.00 11.88 ?  38  ALA   A HA   1 
ATOM   1021 H  HB1  . ALA   A 1 38  ? 21.585 -0.740  -0.441  1.00 13.95 ?  38  ALA   A HB1  1 
ATOM   1022 H  HB2  . ALA   A 1 38  ? 21.161 -1.079  1.053   1.00 13.95 ?  38  ALA   A HB2  1 
ATOM   1023 H  HB3  . ALA   A 1 38  ? 21.454 0.424   0.631   1.00 13.95 ?  38  ALA   A HB3  1 
ATOM   1024 N  N    A ALA   A 1 39  ? 25.334 -0.049  0.003   0.64 9.81  ?  39  ALA   A N    1 
ATOM   1025 N  N    B ALA   A 1 39  ? 25.344 -0.016  0.043   0.36 9.98  ?  39  ALA   A N    1 
ATOM   1026 C  CA   A ALA   A 1 39  ? 26.393 0.827   -0.467  0.64 9.88  ?  39  ALA   A CA   1 
ATOM   1027 C  CA   B ALA   A 1 39  ? 26.345 0.909   -0.461  0.36 10.37 ?  39  ALA   A CA   1 
ATOM   1028 C  C    A ALA   A 1 39  ? 26.523 0.793   -1.990  0.64 10.04 ?  39  ALA   A C    1 
ATOM   1029 C  C    B ALA   A 1 39  ? 26.503 0.789   -1.973  0.36 9.64  ?  39  ALA   A C    1 
ATOM   1030 O  O    A ALA   A 1 39  ? 25.989 -0.084  -2.675  0.64 10.09 ?  39  ALA   A O    1 
ATOM   1031 O  O    B ALA   A 1 39  ? 26.149 -0.222  -2.586  0.36 9.57  ?  39  ALA   A O    1 
ATOM   1032 C  CB   A ALA   A 1 39  ? 27.715 0.411   0.185   0.64 9.86  ?  39  ALA   A CB   1 
ATOM   1033 C  CB   B ALA   A 1 39  ? 27.691 0.643   0.212   0.36 11.31 ?  39  ALA   A CB   1 
ATOM   1034 H  H    A ALA   A 1 39  ? 25.605 -0.849  0.178   0.64 11.78 ?  39  ALA   A H    1 
ATOM   1035 H  H    B ALA   A 1 39  ? 25.654 -0.790  0.262   0.36 11.98 ?  39  ALA   A H    1 
ATOM   1036 H  HA   A ALA   A 1 39  ? 26.189 1.738   -0.196  0.64 11.86 ?  39  ALA   A HA   1 
ATOM   1037 H  HA   B ALA   A 1 39  ? 26.069 1.816   -0.248  0.36 12.44 ?  39  ALA   A HA   1 
ATOM   1038 H  HB1  A ALA   A 1 39  ? 28.415 1.005   -0.127  0.64 11.83 ?  39  ALA   A HB1  1 
ATOM   1039 H  HB1  B ALA   A 1 39  ? 28.342 1.270   -0.136  0.36 13.58 ?  39  ALA   A HB1  1 
ATOM   1040 H  HB2  A ALA   A 1 39  ? 27.626 0.487   1.152   0.64 11.83 ?  39  ALA   A HB2  1 
ATOM   1041 H  HB2  B ALA   A 1 39  ? 27.592 0.763   1.170   0.36 13.58 ?  39  ALA   A HB2  1 
ATOM   1042 H  HB3  A ALA   A 1 39  ? 27.913 -0.501  -0.059  0.64 11.83 ?  39  ALA   A HB3  1 
ATOM   1043 H  HB3  B ALA   A 1 39  ? 27.964 -0.265  0.017   0.36 13.58 ?  39  ALA   A HB3  1 
ATOM   1044 N  N    A ASN   A 1 40  ? 27.256 1.775   -2.518  0.64 10.46 ?  40  ASN   A N    1 
ATOM   1045 N  N    B ASN   A 1 40  ? 27.054 1.845   -2.571  0.36 9.22  ?  40  ASN   A N    1 
ATOM   1046 C  CA   A ASN   A 1 40  ? 27.808 1.720   -3.867  0.64 10.30 ?  40  ASN   A CA   1 
ATOM   1047 C  CA   B ASN   A 1 40  ? 27.556 1.797   -3.936  0.36 9.67  ?  40  ASN   A CA   1 
ATOM   1048 C  C    A ASN   A 1 40  ? 29.333 1.625   -3.788  0.64 9.46  ?  40  ASN   A C    1 
ATOM   1049 C  C    B ASN   A 1 40  ? 29.078 1.648   -3.915  0.36 9.40  ?  40  ASN   A C    1 
ATOM   1050 O  O    A ASN   A 1 40  ? 29.926 1.745   -2.712  0.64 9.68  ?  40  ASN   A O    1 
ATOM   1051 O  O    B ASN   A 1 40  ? 29.714 1.696   -2.860  0.36 9.65  ?  40  ASN   A O    1 
ATOM   1052 C  CB   A ASN   A 1 40  ? 27.317 2.885   -4.746  0.64 11.25 ?  40  ASN   A CB   1 
ATOM   1053 C  CB   B ASN   A 1 40  ? 27.126 3.036   -4.730  0.36 10.53 ?  40  ASN   A CB   1 
ATOM   1054 C  CG   A ASN   A 1 40  ? 27.654 4.249   -4.179  0.64 12.08 ?  40  ASN   A CG   1 
ATOM   1055 C  CG   B ASN   A 1 40  ? 27.586 4.331   -4.095  0.36 11.64 ?  40  ASN   A CG   1 
ATOM   1056 O  OD1  A ASN   A 1 40  ? 28.798 4.514   -3.805  0.64 12.79 ?  40  ASN   A OD1  1 
ATOM   1057 O  OD1  B ASN   A 1 40  ? 28.787 4.576   -3.955  0.36 12.00 ?  40  ASN   A OD1  1 
ATOM   1058 N  ND2  A ASN   A 1 40  ? 26.649 5.132   -4.117  0.64 12.40 ?  40  ASN   A ND2  1 
ATOM   1059 N  ND2  B ASN   A 1 40  ? 26.630 5.180   -3.722  0.36 12.38 ?  40  ASN   A ND2  1 
ATOM   1060 H  H    A ASN   A 1 40  ? 27.453 2.495   -2.098  0.64 12.55 ?  40  ASN   A H    1 
ATOM   1061 H  H    B ASN   A 1 40  ? 27.156 2.611   -2.193  0.36 11.07 ?  40  ASN   A H    1 
ATOM   1062 H  HA   A ASN   A 1 40  ? 27.500 0.904   -4.286  0.64 12.36 ?  40  ASN   A HA   1 
ATOM   1063 H  HA   B ASN   A 1 40  ? 27.185 1.017   -4.381  0.36 11.60 ?  40  ASN   A HA   1 
ATOM   1064 H  HB2  A ASN   A 1 40  ? 27.730 2.810   -5.624  0.64 13.49 ?  40  ASN   A HB2  1 
ATOM   1065 H  HB2  B ASN   A 1 40  ? 27.504 2.987   -5.621  0.36 12.64 ?  40  ASN   A HB2  1 
ATOM   1066 H  HB3  A ASN   A 1 40  ? 26.353 2.828   -4.833  0.64 13.49 ?  40  ASN   A HB3  1 
ATOM   1067 H  HB3  B ASN   A 1 40  ? 26.158 3.050   -4.784  0.36 12.64 ?  40  ASN   A HB3  1 
ATOM   1068 H  HD21 A ASN   A 1 40  ? 26.788 5.927   -3.811  0.64 14.88 ?  40  ASN   A HD21 1 
ATOM   1069 H  HD21 B ASN   A 1 40  ? 26.840 5.930   -3.357  0.36 14.85 ?  40  ASN   A HD21 1 
ATOM   1070 H  HD22 A ASN   A 1 40  ? 25.862 4.908   -4.381  0.64 14.88 ?  40  ASN   A HD22 1 
ATOM   1071 H  HD22 B ASN   A 1 40  ? 25.803 4.977   -3.843  0.36 14.85 ?  40  ASN   A HD22 1 
ATOM   1072 N  N    A VAL   A 1 41  ? 29.964 1.350   -4.935  0.64 9.70  ?  41  VAL   A N    1 
ATOM   1073 N  N    B VAL   A 1 41  ? 29.660 1.442   -5.100  0.36 9.63  ?  41  VAL   A N    1 
ATOM   1074 C  CA   A VAL   A 1 41  ? 31.394 1.043   -4.946  0.64 10.37 ?  41  VAL   A CA   1 
ATOM   1075 C  CA   B VAL   A 1 41  ? 31.082 1.115   -5.173  0.36 10.24 ?  41  VAL   A CA   1 
ATOM   1076 C  C    A VAL   A 1 41  ? 32.242 2.207   -4.471  0.64 10.33 ?  41  VAL   A C    1 
ATOM   1077 C  C    B VAL   A 1 41  ? 31.976 2.244   -4.677  0.36 10.42 ?  41  VAL   A C    1 
ATOM   1078 O  O    A VAL   A 1 41  ? 33.375 1.998   -4.022  0.64 10.42 ?  41  VAL   A O    1 
ATOM   1079 O  O    B VAL   A 1 41  ? 33.134 1.994   -4.322  0.36 10.67 ?  41  VAL   A O    1 
ATOM   1080 C  CB   A VAL   A 1 41  ? 31.890 0.542   -6.326  0.64 10.29 ?  41  VAL   A CB   1 
ATOM   1081 C  CB   B VAL   A 1 41  ? 31.499 0.675   -6.595  0.36 10.82 ?  41  VAL   A CB   1 
ATOM   1082 C  CG1  A VAL   A 1 41  ? 31.182 -0.744  -6.728  0.64 11.55 ?  41  VAL   A CG1  1 
ATOM   1083 C  CG1  B VAL   A 1 41  ? 30.819 -0.637  -6.970  0.36 11.60 ?  41  VAL   A CG1  1 
ATOM   1084 C  CG2  A VAL   A 1 41  ? 31.759 1.606   -7.410  0.64 10.32 ?  41  VAL   A CG2  1 
ATOM   1085 C  CG2  B VAL   A 1 41  ? 31.194 1.764   -7.617  0.36 11.23 ?  41  VAL   A CG2  1 
ATOM   1086 H  H    A VAL   A 1 41  ? 29.593 1.334   -5.705  0.64 11.64 ?  41  VAL   A H    1 
ATOM   1087 H  H    B VAL   A 1 41  ? 29.257 1.480   -5.860  0.36 11.55 ?  41  VAL   A H    1 
ATOM   1088 H  HA   A VAL   A 1 41  ? 31.553 0.323   -4.321  0.64 12.44 ?  41  VAL   A HA   1 
ATOM   1089 H  HA   B VAL   A 1 41  ? 31.237 0.352   -4.594  0.36 12.28 ?  41  VAL   A HA   1 
ATOM   1090 H  HB   A VAL   A 1 41  ? 32.834 0.332   -6.253  0.64 12.34 ?  41  VAL   A HB   1 
ATOM   1091 H  HB   B VAL   A 1 41  ? 32.456 0.520   -6.605  0.36 12.99 ?  41  VAL   A HB   1 
ATOM   1092 H  HG11 A VAL   A 1 41  ? 31.519 -1.044  -7.587  0.64 13.86 ?  41  VAL   A HG11 1 
ATOM   1093 H  HG11 B VAL   A 1 41  ? 31.068 -0.877  -7.875  0.36 13.92 ?  41  VAL   A HG11 1 
ATOM   1094 H  HG12 A VAL   A 1 41  ? 31.347 -1.423  -6.054  0.64 13.86 ?  41  VAL   A HG12 1 
ATOM   1095 H  HG12 B VAL   A 1 41  ? 31.111 -1.331  -6.354  0.36 13.92 ?  41  VAL   A HG12 1 
ATOM   1096 H  HG13 A VAL   A 1 41  ? 30.226 -0.573  -6.793  0.64 13.86 ?  41  VAL   A HG13 1 
ATOM   1097 H  HG13 B VAL   A 1 41  ? 29.859 -0.529  -6.908  0.36 13.92 ?  41  VAL   A HG13 1 
ATOM   1098 H  HG21 A VAL   A 1 41  ? 31.986 1.210   -8.271  0.64 12.38 ?  41  VAL   A HG21 1 
ATOM   1099 H  HG21 B VAL   A 1 41  ? 31.511 1.474   -8.487  0.36 13.48 ?  41  VAL   A HG21 1 
ATOM   1100 H  HG22 A VAL   A 1 41  ? 30.851 1.933   -7.426  0.64 12.38 ?  41  VAL   A HG22 1 
ATOM   1101 H  HG22 B VAL   A 1 41  ? 30.236 1.910   -7.648  0.36 13.48 ?  41  VAL   A HG22 1 
ATOM   1102 H  HG23 A VAL   A 1 41  ? 32.374 2.332   -7.215  0.64 12.38 ?  41  VAL   A HG23 1 
ATOM   1103 H  HG23 B VAL   A 1 41  ? 31.648 2.578   -7.354  0.36 13.48 ?  41  VAL   A HG23 1 
ATOM   1104 N  N    A TYR   A 1 42  ? 31.734 3.435   -4.586  0.64 10.56 ?  42  TYR   A N    1 
ATOM   1105 N  N    B TYR   A 1 42  ? 31.487 3.488   -4.666  0.36 10.44 ?  42  TYR   A N    1 
ATOM   1106 C  CA   A TYR   A 1 42  ? 32.442 4.635   -4.168  0.64 10.73 ?  42  TYR   A CA   1 
ATOM   1107 C  CA   B TYR   A 1 42  ? 32.289 4.635   -4.250  0.36 10.70 ?  42  TYR   A CA   1 
ATOM   1108 C  C    A TYR   A 1 42  ? 32.160 5.001   -2.721  0.64 10.55 ?  42  TYR   A C    1 
ATOM   1109 C  C    B TYR   A 1 42  ? 32.066 5.032   -2.795  0.36 10.36 ?  42  TYR   A C    1 
ATOM   1110 O  O    A TYR   A 1 42  ? 32.741 5.972   -2.212  0.64 11.20 ?  42  TYR   A O    1 
ATOM   1111 O  O    B TYR   A 1 42  ? 32.609 6.054   -2.352  0.36 10.58 ?  42  TYR   A O    1 
ATOM   1112 C  CB   A TYR   A 1 42  ? 32.065 5.809   -5.092  0.64 11.66 ?  42  TYR   A CB   1 
ATOM   1113 C  CB   B TYR   A 1 42  ? 31.999 5.841   -5.146  0.36 11.47 ?  42  TYR   A CB   1 
ATOM   1114 C  CG   A TYR   A 1 42  ? 32.281 5.488   -6.559  0.64 12.27 ?  42  TYR   A CG   1 
ATOM   1115 C  CG   B TYR   A 1 42  ? 32.121 5.546   -6.622  0.36 11.91 ?  42  TYR   A CG   1 
ATOM   1116 C  CD1  A TYR   A 1 42  ? 33.556 5.297   -7.063  0.64 13.21 ?  42  TYR   A CD1  1 
ATOM   1117 C  CD1  B TYR   A 1 42  ? 33.359 5.324   -7.206  0.36 12.09 ?  42  TYR   A CD1  1 
ATOM   1118 C  CD2  A TYR   A 1 42  ? 31.207 5.346   -7.433  0.64 13.19 ?  42  TYR   A CD2  1 
ATOM   1119 C  CD2  B TYR   A 1 42  ? 30.996 5.488   -7.429  0.36 12.71 ?  42  TYR   A CD2  1 
ATOM   1120 C  CE1  A TYR   A 1 42  ? 33.763 4.979   -8.393  0.64 13.40 ?  42  TYR   A CE1  1 
ATOM   1121 C  CE1  B TYR   A 1 42  ? 33.472 5.045   -8.556  0.36 12.26 ?  42  TYR   A CE1  1 
ATOM   1122 C  CE2  A TYR   A 1 42  ? 31.406 5.035   -8.770  0.64 13.88 ?  42  TYR   A CE2  1 
ATOM   1123 C  CE2  B TYR   A 1 42  ? 31.098 5.218   -8.778  0.36 13.15 ?  42  TYR   A CE2  1 
ATOM   1124 C  CZ   A TYR   A 1 42  ? 32.689 4.854   -9.243  0.64 13.65 ?  42  TYR   A CZ   1 
ATOM   1125 C  CZ   B TYR   A 1 42  ? 32.338 4.996   -9.338  0.36 12.88 ?  42  TYR   A CZ   1 
ATOM   1126 O  OH   A TYR   A 1 42  ? 32.901 4.538   -10.566 0.64 14.49 ?  42  TYR   A OH   1 
ATOM   1127 O  OH   B TYR   A 1 42  ? 32.447 4.725   -10.682 0.36 13.72 ?  42  TYR   A OH   1 
ATOM   1128 H  H    A TYR   A 1 42  ? 30.956 3.594   -4.908  0.64 12.67 ?  42  TYR   A H    1 
ATOM   1129 H  H    B TYR   A 1 42  ? 30.683 3.689   -4.915  0.36 12.53 ?  42  TYR   A H    1 
ATOM   1130 H  HA   A TYR   A 1 42  ? 33.395 4.492   -4.255  0.64 12.88 ?  42  TYR   A HA   1 
ATOM   1131 H  HA   B TYR   A 1 42  ? 33.223 4.406   -4.357  0.36 12.84 ?  42  TYR   A HA   1 
ATOM   1132 H  HB2  A TYR   A 1 42  ? 31.125 6.026   -4.967  0.64 13.99 ?  42  TYR   A HB2  1 
ATOM   1133 H  HB2  B TYR   A 1 42  ? 31.093 6.147   -4.974  0.36 13.76 ?  42  TYR   A HB2  1 
ATOM   1134 H  HB3  A TYR   A 1 42  ? 32.613 6.580   -4.872  0.64 13.99 ?  42  TYR   A HB3  1 
ATOM   1135 H  HB3  B TYR   A 1 42  ? 32.629 6.547   -4.927  0.36 13.76 ?  42  TYR   A HB3  1 
ATOM   1136 H  HD1  A TYR   A 1 42  ? 34.288 5.377   -6.495  0.64 15.86 ?  42  TYR   A HD1  1 
ATOM   1137 H  HD1  B TYR   A 1 42  ? 34.126 5.353   -6.677  0.36 14.51 ?  42  TYR   A HD1  1 
ATOM   1138 H  HD2  A TYR   A 1 42  ? 30.339 5.469   -7.118  0.64 15.82 ?  42  TYR   A HD2  1 
ATOM   1139 H  HD2  B TYR   A 1 42  ? 30.157 5.636   -7.053  0.36 15.25 ?  42  TYR   A HD2  1 
ATOM   1140 H  HE1  A TYR   A 1 42  ? 34.628 4.860   -8.714  0.64 16.08 ?  42  TYR   A HE1  1 
ATOM   1141 H  HE1  B TYR   A 1 42  ? 34.310 4.897   -8.932  0.36 14.71 ?  42  TYR   A HE1  1 
ATOM   1142 H  HE2  A TYR   A 1 42  ? 30.677 4.950   -9.347  0.64 16.66 ?  42  TYR   A HE2  1 
ATOM   1143 H  HE2  B TYR   A 1 42  ? 30.334 5.182   -9.305  0.36 15.78 ?  42  TYR   A HE2  1 
ATOM   1144 H  HH   A TYR   A 1 42  ? 33.722 4.428   -10.707 0.64 17.39 ?  42  TYR   A HH   1 
ATOM   1145 H  HH   B TYR   A 1 42  ? 31.688 4.726   -11.037 0.36 16.47 ?  42  TYR   A HH   1 
ATOM   1146 N  N    . LEU   A 1 43  ? 31.271 4.257   -2.055  1.00 10.16 ?  43  LEU   A N    1 
ATOM   1147 C  CA   . LEU   A 1 43  ? 30.830 4.598   -0.703  1.00 10.01 ?  43  LEU   A CA   1 
ATOM   1148 C  C    . LEU   A 1 43  ? 30.345 6.045   -0.613  1.00 10.14 ?  43  LEU   A C    1 
ATOM   1149 O  O    . LEU   A 1 43  ? 30.615 6.755   0.360   1.00 11.38 ?  43  LEU   A O    1 
ATOM   1150 C  CB   . LEU   A 1 43  ? 31.875 4.287   0.365   1.00 10.32 ?  43  LEU   A CB   1 
ATOM   1151 C  CG   . LEU   A 1 43  ? 32.371 2.837   0.461   1.00 10.87 ?  43  LEU   A CG   1 
ATOM   1152 C  CD1  . LEU   A 1 43  ? 33.402 2.723   1.569   1.00 11.71 ?  43  LEU   A CD1  1 
ATOM   1153 C  CD2  . LEU   A 1 43  ? 31.221 1.861   0.683   1.00 11.37 ?  43  LEU   A CD2  1 
ATOM   1154 H  H    A LEU   A 1 43  ? 30.912 3.535   -2.362  0.64 12.20 ?  43  LEU   A H    1 
ATOM   1155 H  H    B LEU   A 1 43  ? 30.958 3.499   -2.323  0.36 12.20 ?  43  LEU   A H    1 
ATOM   1156 H  HA   . LEU   A 1 43  ? 30.063 4.039   -0.499  1.00 12.01 ?  43  LEU   A HA   1 
ATOM   1157 H  HB2  . LEU   A 1 43  ? 32.649 4.849   0.202   1.00 12.38 ?  43  LEU   A HB2  1 
ATOM   1158 H  HB3  . LEU   A 1 43  ? 31.493 4.515   1.230   1.00 12.38 ?  43  LEU   A HB3  1 
ATOM   1159 H  HG   . LEU   A 1 43  ? 32.810 2.600   -0.370  1.00 13.04 ?  43  LEU   A HG   1 
ATOM   1160 H  HD11 . LEU   A 1 43  ? 33.710 1.804   1.621   1.00 14.05 ?  43  LEU   A HD11 1 
ATOM   1161 H  HD12 . LEU   A 1 43  ? 34.147 3.311   1.372   1.00 14.05 ?  43  LEU   A HD12 1 
ATOM   1162 H  HD13 . LEU   A 1 43  ? 32.991 2.980   2.411   1.00 14.05 ?  43  LEU   A HD13 1 
ATOM   1163 H  HD21 . LEU   A 1 43  ? 31.588 0.976   0.837   1.00 13.64 ?  43  LEU   A HD21 1 
ATOM   1164 H  HD22 . LEU   A 1 43  ? 30.712 2.148   1.455   1.00 13.64 ?  43  LEU   A HD22 1 
ATOM   1165 H  HD23 . LEU   A 1 43  ? 30.661 1.856   -0.106  1.00 13.64 ?  43  LEU   A HD23 1 
ATOM   1166 N  N    A LYS   A 1 44  ? 29.627 6.487   -1.646  0.64 10.21 ?  44  LYS   A N    1 
ATOM   1167 N  N    B LYS   A 1 44  ? 29.619 6.481   -1.644  0.36 10.61 ?  44  LYS   A N    1 
ATOM   1168 C  CA   A LYS   A 1 44  ? 28.985 7.801   -1.650  0.64 10.35 ?  44  LYS   A CA   1 
ATOM   1169 C  CA   B LYS   A 1 44  ? 28.976 7.795   -1.660  0.36 11.21 ?  44  LYS   A CA   1 
ATOM   1170 C  C    A LYS   A 1 44  ? 27.559 7.609   -1.151  0.64 10.00 ?  44  LYS   A C    1 
ATOM   1171 C  C    B LYS   A 1 44  ? 27.553 7.611   -1.153  0.36 10.45 ?  44  LYS   A C    1 
ATOM   1172 O  O    A LYS   A 1 44  ? 26.696 7.088   -1.865  0.64 11.27 ?  44  LYS   A O    1 
ATOM   1173 O  O    B LYS   A 1 44  ? 26.680 7.112   -1.870  0.36 11.11 ?  44  LYS   A O    1 
ATOM   1174 C  CB   A LYS   A 1 44  ? 29.030 8.422   -3.039  0.64 12.90 ?  44  LYS   A CB   1 
ATOM   1175 C  CB   B LYS   A 1 44  ? 29.001 8.390   -3.063  0.36 13.58 ?  44  LYS   A CB   1 
ATOM   1176 C  CG   A LYS   A 1 44  ? 30.414 8.878   -3.467  0.64 16.27 ?  44  LYS   A CG   1 
ATOM   1177 C  CG   B LYS   A 1 44  ? 30.357 8.921   -3.495  0.36 16.37 ?  44  LYS   A CG   1 
ATOM   1178 C  CD   A LYS   A 1 44  ? 31.084 9.775   -2.429  0.64 20.99 ?  44  LYS   A CD   1 
ATOM   1179 C  CD   B LYS   A 1 44  ? 30.938 9.886   -2.470  0.36 19.54 ?  44  LYS   A CD   1 
ATOM   1180 C  CE   A LYS   A 1 44  ? 32.420 10.292  -2.928  0.64 23.84 ?  44  LYS   A CE   1 
ATOM   1181 C  CE   B LYS   A 1 44  ? 32.201 10.540  -2.991  0.36 21.62 ?  44  LYS   A CE   1 
ATOM   1182 N  NZ   A LYS   A 1 44  ? 33.234 10.868  -1.827  0.64 25.23 ?  44  LYS   A NZ   1 
ATOM   1183 N  NZ   B LYS   A 1 44  ? 33.041 11.088  -1.894  0.36 23.03 ?  44  LYS   A NZ   1 
ATOM   1184 H  H    A LYS   A 1 44  ? 29.491 6.031   -2.364  0.64 12.25 ?  44  LYS   A H    1 
ATOM   1185 H  H    B LYS   A 1 44  ? 29.479 6.021   -2.359  0.36 12.73 ?  44  LYS   A H    1 
ATOM   1186 H  HA   A LYS   A 1 44  ? 29.433 8.379   -1.017  0.64 12.42 ?  44  LYS   A HA   1 
ATOM   1187 H  HA   B LYS   A 1 44  ? 29.432 8.387   -1.044  0.36 13.46 ?  44  LYS   A HA   1 
ATOM   1188 H  HB2  A LYS   A 1 44  ? 28.720 7.769   -3.684  0.64 15.48 ?  44  LYS   A HB2  1 
ATOM   1189 H  HB2  B LYS   A 1 44  ? 28.737 7.705   -3.697  0.36 16.29 ?  44  LYS   A HB2  1 
ATOM   1190 H  HB3  A LYS   A 1 44  ? 28.447 9.198   -3.050  0.64 15.48 ?  44  LYS   A HB3  1 
ATOM   1191 H  HB3  B LYS   A 1 44  ? 28.372 9.128   -3.099  0.36 16.29 ?  44  LYS   A HB3  1 
ATOM   1192 H  HG2  A LYS   A 1 44  ? 30.977 8.101   -3.602  0.64 19.52 ?  44  LYS   A HG2  1 
ATOM   1193 H  HG2  B LYS   A 1 44  ? 30.973 8.179   -3.599  0.36 19.64 ?  44  LYS   A HG2  1 
ATOM   1194 H  HG3  A LYS   A 1 44  ? 30.340 9.383   -4.294  0.64 19.52 ?  44  LYS   A HG3  1 
ATOM   1195 H  HG3  B LYS   A 1 44  ? 30.262 9.397   -4.337  0.36 19.64 ?  44  LYS   A HG3  1 
ATOM   1196 H  HD2  A LYS   A 1 44  ? 30.505 10.530  -2.236  0.64 25.19 ?  44  LYS   A HD2  1 
ATOM   1197 H  HD2  B LYS   A 1 44  ? 30.283 10.573  -2.269  0.36 23.45 ?  44  LYS   A HD2  1 
ATOM   1198 H  HD3  A LYS   A 1 44  ? 31.249 9.263   -1.620  0.64 25.19 ?  44  LYS   A HD3  1 
ATOM   1199 H  HD3  B LYS   A 1 44  ? 31.169 9.395   -1.663  0.36 23.45 ?  44  LYS   A HD3  1 
ATOM   1200 H  HE2  A LYS   A 1 44  ? 32.918 9.558   -3.320  0.64 28.61 ?  44  LYS   A HE2  1 
ATOM   1201 H  HE2  B LYS   A 1 44  ? 32.723 9.878   -3.471  0.36 25.95 ?  44  LYS   A HE2  1 
ATOM   1202 H  HE3  A LYS   A 1 44  ? 32.264 10.984  -3.588  0.64 28.61 ?  44  LYS   A HE3  1 
ATOM   1203 H  HE3  B LYS   A 1 44  ? 31.958 11.268  -3.581  0.36 25.95 ?  44  LYS   A HE3  1 
ATOM   1204 H  HZ1  A LYS   A 1 44  ? 34.009 11.166  -2.147  0.64 30.27 ?  44  LYS   A HZ1  1 
ATOM   1205 H  HZ1  B LYS   A 1 44  ? 33.773 11.463  -2.233  0.36 27.64 ?  44  LYS   A HZ1  1 
ATOM   1206 H  HZ2  A LYS   A 1 44  ? 32.797 11.550  -1.452  0.64 30.27 ?  44  LYS   A HZ2  1 
ATOM   1207 H  HZ2  B LYS   A 1 44  ? 32.585 11.701  -1.439  0.36 27.64 ?  44  LYS   A HZ2  1 
ATOM   1208 H  HZ3  A LYS   A 1 44  ? 33.392 10.252  -1.208  0.64 30.27 ?  44  LYS   A HZ3  1 
ATOM   1209 H  HZ3  B LYS   A 1 44  ? 33.282 10.434  -1.339  0.36 27.64 ?  44  LYS   A HZ3  1 
ATOM   1210 N  N    . HIS   A 1 45  ? 27.321 7.999   0.098   1.00 9.95  ?  45  HIS   A N    1 
ATOM   1211 C  CA   . HIS   A 1 45  ? 26.075 7.673   0.789   1.00 9.96  ?  45  HIS   A CA   1 
ATOM   1212 C  C    . HIS   A 1 45  ? 25.062 8.806   0.617   1.00 10.76 ?  45  HIS   A C    1 
ATOM   1213 O  O    . HIS   A 1 45  ? 24.781 9.582   1.532   1.00 12.75 ?  45  HIS   A O    1 
ATOM   1214 C  CB   . HIS   A 1 45  ? 26.362 7.418   2.258   1.00 10.09 ?  45  HIS   A CB   1 
ATOM   1215 C  CG   . HIS   A 1 45  ? 27.475 6.449   2.495   1.00 9.51  ?  45  HIS   A CG   1 
ATOM   1216 N  ND1  . HIS   A 1 45  ? 27.472 5.162   1.997   1.00 10.12 ?  45  HIS   A ND1  1 
ATOM   1217 C  CD2  . HIS   A 1 45  ? 28.640 6.602   3.171   1.00 9.85  ?  45  HIS   A CD2  1 
ATOM   1218 C  CE1  . HIS   A 1 45  ? 28.591 4.566   2.370   1.00 10.17 ?  45  HIS   A CE1  1 
ATOM   1219 N  NE2  . HIS   A 1 45  ? 29.316 5.414   3.082   1.00 10.11 ?  45  HIS   A NE2  1 
ATOM   1220 H  H    A HIS   A 1 45  ? 27.871 8.460   0.571   0.64 11.94 ?  45  HIS   A H    1 
ATOM   1221 H  H    B HIS   A 1 45  ? 27.879 8.443   0.578   0.36 11.94 ?  45  HIS   A H    1 
ATOM   1222 H  HA   . HIS   A 1 45  ? 25.695 6.865   0.407   1.00 11.96 ?  45  HIS   A HA   1 
ATOM   1223 H  HB2  . HIS   A 1 45  ? 26.594 8.259   2.681   1.00 12.10 ?  45  HIS   A HB2  1 
ATOM   1224 H  HB3  . HIS   A 1 45  ? 25.557 7.058   2.674   1.00 12.10 ?  45  HIS   A HB3  1 
ATOM   1225 H  HD2  . HIS   A 1 45  ? 28.931 7.374   3.611   1.00 11.83 ?  45  HIS   A HD2  1 
ATOM   1226 H  HE1  . HIS   A 1 45  ? 28.828 3.689   2.180   1.00 12.20 ?  45  HIS   A HE1  1 
ATOM   1227 H  HE2  . HIS   A 1 45  ? 30.087 5.251   3.432   1.00 12.13 ?  45  HIS   A HE2  1 
ATOM   1228 N  N    A GLY   A 1 46  ? 24.442 8.838   -0.557  0.64 11.71 ?  46  GLY   A N    1 
ATOM   1229 N  N    B GLY   A 1 46  ? 24.540 8.921   -0.600  0.36 11.29 ?  46  GLY   A N    1 
ATOM   1230 C  CA   A GLY   A 1 46  ? 23.577 9.951   -0.899  0.64 12.09 ?  46  GLY   A CA   1 
ATOM   1231 C  CA   B GLY   A 1 46  ? 23.778 10.107  -0.955  0.36 11.49 ?  46  GLY   A CA   1 
ATOM   1232 C  C    A GLY   A 1 46  ? 22.103 9.764   -0.598  0.64 12.10 ?  46  GLY   A C    1 
ATOM   1233 C  C    B GLY   A 1 46  ? 22.297 10.036  -0.644  0.36 11.42 ?  46  GLY   A C    1 
ATOM   1234 O  O    A GLY   A 1 46  ? 21.433 10.713  -0.170  0.64 13.02 ?  46  GLY   A O    1 
ATOM   1235 O  O    B GLY   A 1 46  ? 21.655 11.062  -0.394  0.36 11.63 ?  46  GLY   A O    1 
ATOM   1236 H  H    A GLY   A 1 46  ? 24.499 8.231   -1.163  0.64 14.05 ?  46  GLY   A H    1 
ATOM   1237 H  H    B GLY   A 1 46  ? 24.604 8.333   -1.224  0.36 13.55 ?  46  GLY   A H    1 
ATOM   1238 H  HA2  A GLY   A 1 46  ? 23.867 10.736  -0.411  0.64 14.50 ?  46  GLY   A HA2  1 
ATOM   1239 H  HA2  B GLY   A 1 46  ? 24.154 10.873  -0.487  0.36 13.79 ?  46  GLY   A HA2  1 
ATOM   1240 H  HA3  A GLY   A 1 46  ? 23.669 10.138  -1.845  0.64 14.50 ?  46  GLY   A HA3  1 
ATOM   1241 H  HA3  B GLY   A 1 46  ? 23.866 10.266  -1.905  0.36 13.79 ?  46  GLY   A HA3  1 
ATOM   1242 N  N    A GLY   A 1 47  ? 21.577 8.562   -0.823  0.64 12.10 ?  47  GLY   A N    1 
ATOM   1243 N  N    B GLY   A 1 47  ? 21.737 8.836   -0.689  0.36 11.10 ?  47  GLY   A N    1 
ATOM   1244 C  CA   A GLY   A 1 47  ? 20.145 8.353   -0.804  0.64 11.97 ?  47  GLY   A CA   1 
ATOM   1245 C  CA   B GLY   A 1 47  ? 20.317 8.647   -0.464  0.36 11.60 ?  47  GLY   A CA   1 
ATOM   1246 C  C    A GLY   A 1 47  ? 19.805 6.947   -0.365  0.64 11.66 ?  47  GLY   A C    1 
ATOM   1247 C  C    B GLY   A 1 47  ? 20.033 7.180   -0.228  0.36 11.72 ?  47  GLY   A C    1 
ATOM   1248 O  O    A GLY   A 1 47  ? 20.685 6.128   -0.092  0.64 11.40 ?  47  GLY   A O    1 
ATOM   1249 O  O    B GLY   A 1 47  ? 20.944 6.349   -0.163  0.36 12.28 ?  47  GLY   A O    1 
ATOM   1250 H  H    A GLY   A 1 47  ? 22.038 7.845   -0.970  0.64 14.52 ?  47  GLY   A H    1 
ATOM   1251 H  H    B GLY   A 1 47  ? 22.162 8.116   -0.850  0.36 13.33 ?  47  GLY   A H    1 
ATOM   1252 H  HA2  A GLY   A 1 47  ? 19.728 8.976   -0.194  0.64 14.36 ?  47  GLY   A HA2  1 
ATOM   1253 H  HA2  B GLY   A 1 47  ? 20.031 9.166   0.307   0.36 13.92 ?  47  GLY   A HA2  1 
ATOM   1254 H  HA3  A GLY   A 1 47  ? 19.783 8.490   -1.693  0.64 14.36 ?  47  GLY   A HA3  1 
ATOM   1255 H  HA3  B GLY   A 1 47  ? 19.823 8.945   -1.243  0.36 13.92 ?  47  GLY   A HA3  1 
ATOM   1256 N  N    A GLY   A 1 48  ? 18.507 6.663   -0.318  0.64 11.78 ?  48  GLY   A N    1 
ATOM   1257 N  N    B GLY   A 1 48  ? 18.747 6.861   -0.114  0.36 11.97 ?  48  GLY   A N    1 
ATOM   1258 C  CA   A GLY   A 1 48  ? 18.068 5.367   0.138   0.64 11.55 ?  48  GLY   A CA   1 
ATOM   1259 C  CA   B GLY   A 1 48  ? 18.375 5.492   0.183   0.36 12.02 ?  48  GLY   A CA   1 
ATOM   1260 C  C    A GLY   A 1 48  ? 18.569 5.088   1.539   0.64 10.91 ?  48  GLY   A C    1 
ATOM   1261 C  C    B GLY   A 1 48  ? 18.829 5.085   1.576   0.36 11.73 ?  48  GLY   A C    1 
ATOM   1262 O  O    A GLY   A 1 48  ? 18.721 5.989   2.373   0.64 11.66 ?  48  GLY   A O    1 
ATOM   1263 O  O    B GLY   A 1 48  ? 18.967 5.911   2.485   0.36 12.48 ?  48  GLY   A O    1 
ATOM   1264 H  H    A GLY   A 1 48  ? 17.872 7.203   -0.532  0.64 14.14 ?  48  GLY   A H    1 
ATOM   1265 H  H    B GLY   A 1 48  ? 18.094 7.409   -0.204  0.36 14.36 ?  48  GLY   A H    1 
ATOM   1266 H  HA2  A GLY   A 1 48  ? 17.098 5.324   0.140   0.64 13.86 ?  48  GLY   A HA2  1 
ATOM   1267 H  HA2  B GLY   A 1 48  ? 17.413 5.396   0.116   0.36 14.43 ?  48  GLY   A HA2  1 
ATOM   1268 H  HA3  A GLY   A 1 48  ? 18.409 4.676   -0.451  0.64 13.86 ?  48  GLY   A HA3  1 
ATOM   1269 H  HA3  B GLY   A 1 48  ? 18.792 4.894   -0.460  0.36 14.43 ?  48  GLY   A HA3  1 
ATOM   1270 N  N    A VAL   A 1 49  ? 18.825 3.806   1.803   0.64 10.40 ?  49  VAL   A N    1 
ATOM   1271 N  N    B VAL   A 1 49  ? 19.072 3.781   1.740   0.36 11.47 ?  49  VAL   A N    1 
ATOM   1272 C  CA   A VAL   A 1 49  ? 19.325 3.394   3.110   0.64 10.59 ?  49  VAL   A CA   1 
ATOM   1273 C  CA   B VAL   A 1 49  ? 19.607 3.269   3.002   0.36 10.99 ?  49  VAL   A CA   1 
ATOM   1274 C  C    A VAL   A 1 49  ? 20.644 4.088   3.432   0.64 9.98  ?  49  VAL   A C    1 
ATOM   1275 C  C    B VAL   A 1 49  ? 20.866 4.033   3.389   0.36 9.71  ?  49  VAL   A C    1 
ATOM   1276 O  O    A VAL   A 1 49  ? 20.866 4.524   4.566   0.64 10.92 ?  49  VAL   A O    1 
ATOM   1277 O  O    B VAL   A 1 49  ? 21.037 4.443   4.542   0.36 9.59  ?  49  VAL   A O    1 
ATOM   1278 C  CB   A VAL   A 1 49  ? 19.464 1.860   3.153   0.64 11.10 ?  49  VAL   A CB   1 
ATOM   1279 C  CB   B VAL   A 1 49  ? 19.896 1.760   2.891   0.36 10.80 ?  49  VAL   A CB   1 
ATOM   1280 C  CG1  A VAL   A 1 49  ? 20.264 1.426   4.373   0.64 11.84 ?  49  VAL   A CG1  1 
ATOM   1281 C  CG1  B VAL   A 1 49  ? 20.702 1.291   4.098   0.36 10.36 ?  49  VAL   A CG1  1 
ATOM   1282 C  CG2  A VAL   A 1 49  ? 18.090 1.198   3.146   0.64 12.52 ?  49  VAL   A CG2  1 
ATOM   1283 C  CG2  B VAL   A 1 49  ? 18.616 0.959   2.750   0.36 11.61 ?  49  VAL   A CG2  1 
ATOM   1284 H  H    A VAL   A 1 49  ? 18.717 3.157   1.246   0.64 12.48 ?  49  VAL   A H    1 
ATOM   1285 H  H    B VAL   A 1 49  ? 18.948 3.180   1.139   0.36 13.77 ?  49  VAL   A H    1 
ATOM   1286 H  HA   A VAL   A 1 49  ? 18.682 3.648   3.788   0.64 12.70 ?  49  VAL   A HA   1 
ATOM   1287 H  HA   B VAL   A 1 49  ? 18.949 3.399   3.704   0.36 13.18 ?  49  VAL   A HA   1 
ATOM   1288 H  HB   A VAL   A 1 49  ? 19.946 1.563   2.363   0.64 13.32 ?  49  VAL   A HB   1 
ATOM   1289 H  HB   B VAL   A 1 49  ? 20.433 1.607   2.099   0.36 12.95 ?  49  VAL   A HB   1 
ATOM   1290 H  HG11 A VAL   A 1 49  ? 20.099 0.487   4.533   0.64 14.21 ?  49  VAL   A HG11 1 
ATOM   1291 H  HG11 B VAL   A 1 49  ? 20.610 0.331   4.184   0.36 12.43 ?  49  VAL   A HG11 1 
ATOM   1292 H  HG12 A VAL   A 1 49  ? 21.205 1.576   4.204   0.64 14.21 ?  49  VAL   A HG12 1 
ATOM   1293 H  HG12 B VAL   A 1 49  ? 21.636 1.521   3.969   0.36 12.43 ?  49  VAL   A HG12 1 
ATOM   1294 H  HG13 A VAL   A 1 49  ? 19.972 1.949   5.136   0.64 14.21 ?  49  VAL   A HG13 1 
ATOM   1295 H  HG13 B VAL   A 1 49  ? 20.360 1.727   4.895   0.36 12.43 ?  49  VAL   A HG13 1 
ATOM   1296 H  HG21 A VAL   A 1 49  ? 18.206 0.237   3.167   0.64 15.02 ?  49  VAL   A HG21 1 
ATOM   1297 H  HG21 B VAL   A 1 49  ? 18.845 0.044   2.522   0.36 13.93 ?  49  VAL   A HG21 1 
ATOM   1298 H  HG22 A VAL   A 1 49  ? 17.600 1.493   3.927   0.64 15.02 ?  49  VAL   A HG22 1 
ATOM   1299 H  HG22 B VAL   A 1 49  ? 18.140 0.981   3.593   0.36 13.93 ?  49  VAL   A HG22 1 
ATOM   1300 H  HG23 A VAL   A 1 49  ? 17.623 1.461   2.339   0.64 15.02 ?  49  VAL   A HG23 1 
ATOM   1301 H  HG23 B VAL   A 1 49  ? 18.076 1.350   2.048   0.36 13.93 ?  49  VAL   A HG23 1 
ATOM   1302 N  N    A ALA   A 1 50  ? 21.557 4.151   2.458   0.64 9.51  ?  50  ALA   A N    1 
ATOM   1303 N  N    B ALA   A 1 50  ? 21.780 4.204   2.432   0.36 9.03  ?  50  ALA   A N    1 
ATOM   1304 C  CA   A ALA   A 1 50  ? 22.878 4.724   2.707   0.64 9.49  ?  50  ALA   A CA   1 
ATOM   1305 C  CA   B ALA   A 1 50  ? 23.083 4.781   2.746   0.36 8.86  ?  50  ALA   A CA   1 
ATOM   1306 C  C    A ALA   A 1 50  ? 22.778 6.184   3.126   0.64 9.53  ?  50  ALA   A C    1 
ATOM   1307 C  C    B ALA   A 1 50  ? 22.954 6.237   3.171   0.36 9.01  ?  50  ALA   A C    1 
ATOM   1308 O  O    A ALA   A 1 50  ? 23.425 6.609   4.089   0.64 10.25 ?  50  ALA   A O    1 
ATOM   1309 O  O    B ALA   A 1 50  ? 23.550 6.657   4.171   0.36 9.39  ?  50  ALA   A O    1 
ATOM   1310 C  CB   A ALA   A 1 50  ? 23.749 4.596   1.460   0.64 9.43  ?  50  ALA   A CB   1 
ATOM   1311 C  CB   B ALA   A 1 50  ? 24.015 4.651   1.543   0.36 8.77  ?  50  ALA   A CB   1 
ATOM   1312 H  H    A ALA   A 1 50  ? 21.436 3.871   1.654   0.64 11.41 ?  50  ALA   A H    1 
ATOM   1313 H  H    B ALA   A 1 50  ? 21.664 4.002   1.603   0.36 10.83 ?  50  ALA   A H    1 
ATOM   1314 H  HA   A ALA   A 1 50  ? 23.307 4.238   3.428   0.64 11.39 ?  50  ALA   A HA   1 
ATOM   1315 H  HA   B ALA   A 1 50  ? 23.472 4.293   3.484   0.36 10.63 ?  50  ALA   A HA   1 
ATOM   1316 H  HB1  A ALA   A 1 50  ? 24.621 4.981   1.644   0.64 11.32 ?  50  ALA   A HB1  1 
ATOM   1317 H  HB1  B ALA   A 1 50  ? 24.874 5.038   1.768   0.36 10.52 ?  50  ALA   A HB1  1 
ATOM   1318 H  HB2  A ALA   A 1 50  ? 23.842 3.658   1.234   0.64 11.32 ?  50  ALA   A HB2  1 
ATOM   1319 H  HB2  B ALA   A 1 50  ? 24.121 3.711   1.326   0.36 10.52 ?  50  ALA   A HB2  1 
ATOM   1320 H  HB3  A ALA   A 1 50  ? 23.324 5.074   0.730   0.64 11.32 ?  50  ALA   A HB3  1 
ATOM   1321 H  HB3  B ALA   A 1 50  ? 23.626 5.122   0.788   0.36 10.52 ?  50  ALA   A HB3  1 
ATOM   1322 N  N    A GLY   A 1 51  ? 21.978 6.973   2.405   0.64 9.84  ?  51  GLY   A N    1 
ATOM   1323 N  N    B GLY   A 1 51  ? 22.182 7.025   2.421   0.36 9.43  ?  51  GLY   A N    1 
ATOM   1324 C  CA   A GLY   A 1 51  ? 21.802 8.361   2.799   0.64 10.41 ?  51  GLY   A CA   1 
ATOM   1325 C  CA   B GLY   A 1 51  ? 22.021 8.424   2.776   0.36 9.17  ?  51  GLY   A CA   1 
ATOM   1326 C  C    A GLY   A 1 51  ? 21.237 8.480   4.200   0.64 10.31 ?  51  GLY   A C    1 
ATOM   1327 C  C    B GLY   A 1 51  ? 21.345 8.600   4.121   0.36 9.19  ?  51  GLY   A C    1 
ATOM   1328 O  O    A GLY   A 1 51  ? 21.658 9.339   4.980   0.64 11.08 ?  51  GLY   A O    1 
ATOM   1329 O  O    B GLY   A 1 51  ? 21.674 9.520   4.875   0.36 9.71  ?  51  GLY   A O    1 
ATOM   1330 H  H    A GLY   A 1 51  ? 21.548 6.734   1.696   0.64 11.80 ?  51  GLY   A H    1 
ATOM   1331 H  H    B GLY   A 1 51  ? 21.752 6.777   1.717   0.36 11.31 ?  51  GLY   A H    1 
ATOM   1332 H  HA2  A GLY   A 1 51  ? 22.658 8.820   2.762   0.64 12.49 ?  51  GLY   A HA2  1 
ATOM   1333 H  HA2  B GLY   A 1 51  ? 22.890 8.850   2.813   0.36 11.00 ?  51  GLY   A HA2  1 
ATOM   1334 H  HA3  A GLY   A 1 51  ? 21.194 8.798   2.178   0.64 12.49 ?  51  GLY   A HA3  1 
ATOM   1335 H  HA3  B GLY   A 1 51  ? 21.487 8.871   2.099   0.36 11.00 ?  51  GLY   A HA3  1 
ATOM   1336 N  N    A ALA   A 1 52  ? 20.279 7.613   4.539   0.64 10.49 ?  52  ALA   A N    1 
ATOM   1337 N  N    B ALA   A 1 52  ? 20.385 7.727   4.437   0.36 9.57  ?  52  ALA   A N    1 
ATOM   1338 C  CA   A ALA   A 1 52  ? 19.657 7.660   5.857   0.64 10.83 ?  52  ALA   A CA   1 
ATOM   1339 C  CA   B ALA   A 1 52  ? 19.697 7.815   5.721   0.36 9.87  ?  52  ALA   A CA   1 
ATOM   1340 C  C    A ALA   A 1 52  ? 20.633 7.258   6.961   0.64 10.41 ?  52  ALA   A C    1 
ATOM   1341 C  C    B ALA   A 1 52  ? 20.614 7.404   6.872   0.36 9.62  ?  52  ALA   A C    1 
ATOM   1342 O  O    A ALA   A 1 52  ? 20.709 7.914   8.005   0.64 11.41 ?  52  ALA   A O    1 
ATOM   1343 O  O    B ALA   A 1 52  ? 20.684 8.089   7.897   0.36 10.30 ?  52  ALA   A O    1 
ATOM   1344 C  CB   A ALA   A 1 52  ? 18.417 6.767   5.867   0.64 12.96 ?  52  ALA   A CB   1 
ATOM   1345 C  CB   B ALA   A 1 52  ? 18.422 6.969   5.688   0.36 10.77 ?  52  ALA   A CB   1 
ATOM   1346 H  H    A ALA   A 1 52  ? 19.987 6.987   4.021   0.64 12.59 ?  52  ALA   A H    1 
ATOM   1347 H  H    B ALA   A 1 52  ? 20.124 7.079   3.932   0.36 11.49 ?  52  ALA   A H    1 
ATOM   1348 H  HA   A ALA   A 1 52  ? 19.374 8.567   6.026   0.64 13.00 ?  52  ALA   A HA   1 
ATOM   1349 H  HA   B ALA   A 1 52  ? 19.430 8.735   5.865   0.36 11.84 ?  52  ALA   A HA   1 
ATOM   1350 H  HB1  A ALA   A 1 52  ? 18.011 6.811   6.745   0.64 15.55 ?  52  ALA   A HB1  1 
ATOM   1351 H  HB1  B ALA   A 1 52  ? 17.967 7.048   6.543   0.36 12.92 ?  52  ALA   A HB1  1 
ATOM   1352 H  HB2  A ALA   A 1 52  ? 17.793 7.089   5.196   0.64 15.55 ?  52  ALA   A HB2  1 
ATOM   1353 H  HB2  B ALA   A 1 52  ? 17.843 7.291   4.978   0.36 12.92 ?  52  ALA   A HB2  1 
ATOM   1354 H  HB3  A ALA   A 1 52  ? 18.680 5.857   5.665   0.64 15.55 ?  52  ALA   A HB3  1 
ATOM   1355 H  HB3  B ALA   A 1 52  ? 18.658 6.042   5.525   0.36 12.92 ?  52  ALA   A HB3  1 
ATOM   1356 N  N    A LEU   A 1 53  ? 21.382 6.169   6.763   0.64 10.15 ?  53  LEU   A N    1 
ATOM   1357 N  N    B LEU   A 1 53  ? 21.336 6.289   6.719   0.36 9.46  ?  53  LEU   A N    1 
ATOM   1358 C  CA   A LEU   A 1 53  ? 22.346 5.762   7.782   0.64 10.39 ?  53  LEU   A CA   1 
ATOM   1359 C  CA   B LEU   A 1 53  ? 22.296 5.885   7.745   0.36 9.88  ?  53  LEU   A CA   1 
ATOM   1360 C  C    A LEU   A 1 53  ? 23.405 6.835   7.974   0.64 10.00 ?  53  LEU   A C    1 
ATOM   1361 C  C    B LEU   A 1 53  ? 23.336 6.977   7.962   0.36 9.48  ?  53  LEU   A C    1 
ATOM   1362 O  O    A LEU   A 1 53  ? 23.774 7.162   9.106   0.64 10.61 ?  53  LEU   A O    1 
ATOM   1363 O  O    B LEU   A 1 53  ? 23.580 7.405   9.096   0.36 9.60  ?  53  LEU   A O    1 
ATOM   1364 C  CB   A LEU   A 1 53  ? 23.000 4.429   7.409   0.64 10.84 ?  53  LEU   A CB   1 
ATOM   1365 C  CB   B LEU   A 1 53  ? 22.984 4.569   7.358   0.36 10.46 ?  53  LEU   A CB   1 
ATOM   1366 C  CG   A LEU   A 1 53  ? 22.079 3.207   7.434   0.64 11.54 ?  53  LEU   A CG   1 
ATOM   1367 C  CG   B LEU   A 1 53  ? 22.249 3.222   7.447   0.36 10.74 ?  53  LEU   A CG   1 
ATOM   1368 C  CD1  A LEU   A 1 53  ? 22.781 2.014   6.816   0.64 11.59 ?  53  LEU   A CD1  1 
ATOM   1369 C  CD1  B LEU   A 1 53  ? 23.139 2.100   6.905   0.36 10.66 ?  53  LEU   A CD1  1 
ATOM   1370 C  CD2  A LEU   A 1 53  ? 21.642 2.889   8.853   0.64 13.29 ?  53  LEU   A CD2  1 
ATOM   1371 C  CD2  B LEU   A 1 53  ? 21.813 2.904   8.869   0.36 11.80 ?  53  LEU   A CD2  1 
ATOM   1372 H  H    A LEU   A 1 53  ? 21.346 5.656   6.068   0.64 12.18 ?  53  LEU   A H    1 
ATOM   1373 H  H    B LEU   A 1 53  ? 21.285 5.761   6.043   0.36 11.35 ?  53  LEU   A H    1 
ATOM   1374 H  HA   A LEU   A 1 53  ? 21.883 5.640   8.623   0.64 12.47 ?  53  LEU   A HA   1 
ATOM   1375 H  HA   B LEU   A 1 53  ? 21.824 5.747   8.581   0.36 11.85 ?  53  LEU   A HA   1 
ATOM   1376 H  HB2  A LEU   A 1 53  ? 23.361 4.504   6.509   0.64 13.01 ?  53  LEU   A HB2  1 
ATOM   1377 H  HB2  B LEU   A 1 53  ? 23.268 4.656   6.436   0.36 12.55 ?  53  LEU   A HB2  1 
ATOM   1378 H  HB3  A LEU   A 1 53  ? 23.725 4.257   8.031   0.64 13.01 ?  53  LEU   A HB3  1 
ATOM   1379 H  HB3  B LEU   A 1 53  ? 23.768 4.482   7.918   0.36 12.55 ?  53  LEU   A HB3  1 
ATOM   1380 H  HG   A LEU   A 1 53  ? 21.285 3.399   6.904   0.64 13.85 ?  53  LEU   A HG   1 
ATOM   1381 H  HG   B LEU   A 1 53  ? 21.457 3.257   6.891   0.36 12.89 ?  53  LEU   A HG   1 
ATOM   1382 H  HD11 A LEU   A 1 53  ? 22.183 1.254   6.840   0.64 13.91 ?  53  LEU   A HD11 1 
ATOM   1383 H  HD11 B LEU   A 1 53  ? 22.663 1.257   6.968   0.36 12.79 ?  53  LEU   A HD11 1 
ATOM   1384 H  HD12 A LEU   A 1 53  ? 23.013 2.228   5.898   0.64 13.91 ?  53  LEU   A HD12 1 
ATOM   1385 H  HD12 B LEU   A 1 53  ? 23.357 2.286   5.977   0.36 12.79 ?  53  LEU   A HD12 1 
ATOM   1386 H  HD13 A LEU   A 1 53  ? 23.583 1.828   7.326   0.64 13.91 ?  53  LEU   A HD13 1 
ATOM   1387 H  HD13 B LEU   A 1 53  ? 23.954 2.058   7.432   0.36 12.79 ?  53  LEU   A HD13 1 
ATOM   1388 H  HD21 A LEU   A 1 53  ? 21.139 2.062   8.849   0.64 15.95 ?  53  LEU   A HD21 1 
ATOM   1389 H  HD21 B LEU   A 1 53  ? 21.188 2.160   8.848   0.36 14.16 ?  53  LEU   A HD21 1 
ATOM   1390 H  HD22 A LEU   A 1 53  ? 22.430 2.797   9.409   0.64 15.95 ?  53  LEU   A HD22 1 
ATOM   1391 H  HD22 B LEU   A 1 53  ? 22.590 2.668   9.395   0.36 14.16 ?  53  LEU   A HD22 1 
ATOM   1392 H  HD23 A LEU   A 1 53  ? 21.087 3.613   9.183   0.64 15.95 ?  53  LEU   A HD23 1 
ATOM   1393 H  HD23 B LEU   A 1 53  ? 21.379 3.684   9.250   0.36 14.16 ?  53  LEU   A HD23 1 
ATOM   1394 N  N    A ASN   A 1 54  ? 23.887 7.410   6.879   0.64 9.87  ?  54  ASN   A N    1 
ATOM   1395 N  N    B ASN   A 1 54  ? 23.948 7.455   6.877   0.36 9.58  ?  54  ASN   A N    1 
ATOM   1396 C  CA   A ASN   A 1 54  ? 24.935 8.409   7.008   0.64 9.73  ?  54  ASN   A CA   1 
ATOM   1397 C  CA   B ASN   A 1 54  ? 24.988 8.468   7.014   0.36 9.58  ?  54  ASN   A CA   1 
ATOM   1398 C  C    A ASN   A 1 54  ? 24.426 9.656   7.732   0.64 10.14 ?  54  ASN   A C    1 
ATOM   1399 C  C    B ASN   A 1 54  ? 24.456 9.719   7.703   0.36 10.12 ?  54  ASN   A C    1 
ATOM   1400 O  O    A ASN   A 1 54  ? 25.109 10.191  8.615   0.64 10.51 ?  54  ASN   A O    1 
ATOM   1401 O  O    B ASN   A 1 54  ? 25.153 10.325  8.527   0.36 10.58 ?  54  ASN   A O    1 
ATOM   1402 C  CB   A ASN   A 1 54  ? 25.498 8.762   5.641   0.64 9.82  ?  54  ASN   A CB   1 
ATOM   1403 C  CB   B ASN   A 1 54  ? 25.578 8.825   5.654   0.36 9.58  ?  54  ASN   A CB   1 
ATOM   1404 C  CG   A ASN   A 1 54  ? 26.562 9.824   5.738   0.64 10.13 ?  54  ASN   A CG   1 
ATOM   1405 C  CG   B ASN   A 1 54  ? 26.527 10.000  5.743   0.36 9.51  ?  54  ASN   A CG   1 
ATOM   1406 O  OD1  A ASN   A 1 54  ? 27.549 9.662   6.465   0.64 10.05 ?  54  ASN   A OD1  1 
ATOM   1407 O  OD1  B ASN   A 1 54  ? 27.576 9.913   6.387   0.36 9.35  ?  54  ASN   A OD1  1 
ATOM   1408 N  ND2  A ASN   A 1 54  ? 26.364 10.928  5.039   0.64 10.63 ?  54  ASN   A ND2  1 
ATOM   1409 N  ND2  B ASN   A 1 54  ? 26.156 11.115  5.126   0.36 10.05 ?  54  ASN   A ND2  1 
ATOM   1410 H  H    A ASN   A 1 54  ? 23.629 7.243   6.075   0.64 11.84 ?  54  ASN   A H    1 
ATOM   1411 H  H    B ASN   A 1 54  ? 23.779 7.214   6.071   0.36 11.49 ?  54  ASN   A H    1 
ATOM   1412 H  HA   A ASN   A 1 54  ? 25.652 8.035   7.538   0.64 11.67 ?  54  ASN   A HA   1 
ATOM   1413 H  HA   B ASN   A 1 54  ? 25.698 8.112   7.566   0.36 11.50 ?  54  ASN   A HA   1 
ATOM   1414 H  HB2  A ASN   A 1 54  ? 25.894 7.963   5.248   0.64 11.78 ?  54  ASN   A HB2  1 
ATOM   1415 H  HB2  B ASN   A 1 54  ? 26.072 8.060   5.316   0.36 11.50 ?  54  ASN   A HB2  1 
ATOM   1416 H  HB3  A ASN   A 1 54  ? 24.784 9.091   5.075   0.64 11.78 ?  54  ASN   A HB3  1 
ATOM   1417 H  HB3  B ASN   A 1 54  ? 24.860 9.056   5.046   0.36 11.50 ?  54  ASN   A HB3  1 
ATOM   1418 H  HD21 A ASN   A 1 54  ? 26.944 11.559  5.070   0.64 12.76 ?  54  ASN   A HD21 1 
ATOM   1419 H  HD21 B ASN   A 1 54  ? 26.661 11.811  5.156   0.36 12.05 ?  54  ASN   A HD21 1 
ATOM   1420 H  HD22 A ASN   A 1 54  ? 25.662 11.006  4.550   0.64 12.76 ?  54  ASN   A HD22 1 
ATOM   1421 H  HD22 B ASN   A 1 54  ? 25.416 11.139  4.688   0.36 12.05 ?  54  ASN   A HD22 1 
ATOM   1422 N  N    . LYS   A 1 55  ? 23.227 10.129  7.375   1.00 10.34 ?  55  LYS   A N    1 
ATOM   1423 C  CA   . LYS   A 1 55  ? 22.642 11.288  8.043   1.00 10.98 ?  55  LYS   A CA   1 
ATOM   1424 C  C    . LYS   A 1 55  ? 22.549 11.057  9.546   1.00 11.00 ?  55  LYS   A C    1 
ATOM   1425 O  O    . LYS   A 1 55  ? 22.829 11.960  10.345  1.00 11.87 ?  55  LYS   A O    1 
ATOM   1426 C  CB   . LYS   A 1 55  ? 21.270 11.581  7.429   1.00 11.66 ?  55  LYS   A CB   1 
ATOM   1427 C  CG   . LYS   A 1 55  ? 20.514 12.741  8.056   1.00 13.49 ?  55  LYS   A CG   1 
ATOM   1428 C  CD   . LYS   A 1 55  ? 19.190 12.964  7.327   1.00 15.18 ?  55  LYS   A CD   1 
ATOM   1429 C  CE   . LYS   A 1 55  ? 18.323 14.023  7.993   1.00 17.61 ?  55  LYS   A CE   1 
ATOM   1430 N  NZ   . LYS   A 1 55  ? 16.992 14.128  7.329   1.00 18.47 ?  55  LYS   A NZ   1 
ATOM   1431 H  H    A LYS   A 1 55  ? 22.729 9.791   6.755   0.64 12.40 ?  55  LYS   A H    1 
ATOM   1432 H  H    B LYS   A 1 55  ? 22.717 9.757   6.785   0.36 12.40 ?  55  LYS   A H    1 
ATOM   1433 H  HA   . LYS   A 1 55  ? 23.208 12.060  7.890   1.00 13.18 ?  55  LYS   A HA   1 
ATOM   1434 H  HB2  . LYS   A 1 55  ? 21.389 11.793  6.489   1.00 13.99 ?  55  LYS   A HB2  1 
ATOM   1435 H  HB3  . LYS   A 1 55  ? 20.715 10.793  7.517   1.00 13.99 ?  55  LYS   A HB3  1 
ATOM   1436 H  HG2  . LYS   A 1 55  ? 20.316 12.537  8.985   1.00 16.19 ?  55  LYS   A HG2  1 
ATOM   1437 H  HG3  . LYS   A 1 55  ? 21.040 13.550  7.990   1.00 16.19 ?  55  LYS   A HG3  1 
ATOM   1438 H  HD2  . LYS   A 1 55  ? 19.376 13.251  6.418   1.00 18.21 ?  55  LYS   A HD2  1 
ATOM   1439 H  HD3  . LYS   A 1 55  ? 18.693 12.129  7.313   1.00 18.21 ?  55  LYS   A HD3  1 
ATOM   1440 H  HE2  . LYS   A 1 55  ? 18.183 13.782  8.921   1.00 21.13 ?  55  LYS   A HE2  1 
ATOM   1441 H  HE3  . LYS   A 1 55  ? 18.766 14.882  7.930   1.00 21.13 ?  55  LYS   A HE3  1 
ATOM   1442 H  HZ1  . LYS   A 1 55  ? 16.395 14.469  7.895   1.00 22.17 ?  55  LYS   A HZ1  1 
ATOM   1443 H  HZ2  . LYS   A 1 55  ? 17.045 14.661  6.616   1.00 22.17 ?  55  LYS   A HZ2  1 
ATOM   1444 H  HZ3  . LYS   A 1 55  ? 16.711 13.324  7.068   1.00 22.17 ?  55  LYS   A HZ3  1 
ATOM   1445 N  N    . ALA   A 1 56  ? 22.164 9.844   9.952   1.00 11.59 ?  56  ALA   A N    1 
ATOM   1446 C  CA   . ALA   A 1 56  ? 22.033 9.529   11.369  1.00 12.54 ?  56  ALA   A CA   1 
ATOM   1447 C  C    . ALA   A 1 56  ? 23.374 9.555   12.097  1.00 12.13 ?  56  ALA   A C    1 
ATOM   1448 O  O    . ALA   A 1 56  ? 23.395 9.751   13.314  1.00 13.31 ?  56  ALA   A O    1 
ATOM   1449 C  CB   . ALA   A 1 56  ? 21.323 8.185   11.559  1.00 13.25 ?  56  ALA   A CB   1 
ATOM   1450 H  H    . ALA   A 1 56  ? 21.984 9.190   9.423   1.00 13.91 ?  56  ALA   A H    1 
ATOM   1451 H  HA   . ALA   A 1 56  ? 21.476 10.203  11.778  1.00 15.05 ?  56  ALA   A HA   1 
ATOM   1452 H  HB1  . ALA   A 1 56  ? 21.241 8.002   12.510  1.00 15.90 ?  56  ALA   A HB1  1 
ATOM   1453 H  HB2  . ALA   A 1 56  ? 20.439 8.237   11.159  1.00 15.90 ?  56  ALA   A HB2  1 
ATOM   1454 H  HB3  . ALA   A 1 56  ? 21.838 7.486   11.131  1.00 15.90 ?  56  ALA   A HB3  1 
ATOM   1455 N  N    . THR   A 1 57  ? 24.487 9.358   11.387  1.00 11.18 ?  57  THR   A N    1 
ATOM   1456 C  CA   . THR   A 1 57  ? 25.827 9.489   11.965  1.00 11.08 ?  57  THR   A CA   1 
ATOM   1457 C  C    . THR   A 1 57  ? 26.382 10.910  11.882  1.00 11.65 ?  57  THR   A C    1 
ATOM   1458 O  O    . THR   A 1 57  ? 27.571 11.115  12.169  1.00 12.22 ?  57  THR   A O    1 
ATOM   1459 C  CB   . THR   A 1 57  ? 26.838 8.536   11.299  1.00 11.18 ?  57  THR   A CB   1 
ATOM   1460 O  OG1  . THR   A 1 57  ? 27.232 9.033   10.003  1.00 10.98 ?  57  THR   A OG1  1 
ATOM   1461 C  CG2  . THR   A 1 57  ? 26.301 7.117   11.193  1.00 11.17 ?  57  THR   A CG2  1 
ATOM   1462 H  H    . THR   A 1 57  ? 24.491 9.115   10.560  1.00 13.42 ?  57  THR   A H    1 
ATOM   1463 H  HA   . THR   A 1 57  ? 25.780 9.236   12.905  1.00 13.30 ?  57  THR   A HA   1 
ATOM   1464 H  HB   . THR   A 1 57  ? 27.629 8.489   11.863  1.00 13.42 ?  57  THR   A HB   1 
ATOM   1465 H  HG1  . THR   A 1 57  ? 26.552 9.106   9.516   1.00 13.17 ?  57  THR   A HG1  1 
ATOM   1466 H  HG21 . THR   A 1 57  ? 26.976 6.524   10.821  1.00 13.41 ?  57  THR   A HG21 1 
ATOM   1467 H  HG22 . THR   A 1 57  ? 26.045 6.781   12.070  1.00 13.41 ?  57  THR   A HG22 1 
ATOM   1468 H  HG23 . THR   A 1 57  ? 25.520 7.093   10.616  1.00 13.41 ?  57  THR   A HG23 1 
ATOM   1469 N  N    . ASN   A 1 58  ? 25.569 11.885  11.476  1.00 12.06 ?  58  ASN   A N    1 
ATOM   1470 C  CA   . ASN   A 1 58  ? 26.039 13.264  11.371  1.00 13.10 ?  58  ASN   A CA   1 
ATOM   1471 C  C    . ASN   A 1 58  ? 27.198 13.381  10.373  1.00 11.94 ?  58  ASN   A C    1 
ATOM   1472 O  O    . ASN   A 1 58  ? 28.098 14.216  10.531  1.00 12.47 ?  58  ASN   A O    1 
ATOM   1473 C  CB   . ASN   A 1 58  ? 26.397 13.811  12.766  1.00 15.87 ?  58  ASN   A CB   1 
ATOM   1474 C  CG   . ASN   A 1 58  ? 26.806 15.267  12.757  1.00 19.99 ?  58  ASN   A CG   1 
ATOM   1475 O  OD1  . ASN   A 1 58  ? 26.180 16.090  12.101  1.00 21.67 ?  58  ASN   A OD1  1 
ATOM   1476 N  ND2  . ASN   A 1 58  ? 27.861 15.595  13.504  1.00 21.50 ?  58  ASN   A ND2  1 
ATOM   1477 H  H    . ASN   A 1 58  ? 24.745 11.764  11.247  1.00 14.47 ?  58  ASN   A H    1 
ATOM   1478 H  HA   . ASN   A 1 58  ? 25.310 13.795  11.030  1.00 15.72 ?  58  ASN   A HA   1 
ATOM   1479 H  HB2  . ASN   A 1 58  ? 25.616 13.718  13.346  1.00 19.04 ?  58  ASN   A HB2  1 
ATOM   1480 H  HB3  . ASN   A 1 58  ? 27.133 13.303  13.132  1.00 19.04 ?  58  ASN   A HB3  1 
ATOM   1481 H  HD21 . ASN   A 1 58  ? 28.123 16.416  13.536  1.00 25.81 ?  58  ASN   A HD21 1 
ATOM   1482 H  HD22 . ASN   A 1 58  ? 28.270 14.993  13.951  1.00 25.81 ?  58  ASN   A HD22 1 
ATOM   1483 N  N    . ASN   A 1 59  ? 27.179 12.556  9.322   1.00 10.97 ?  59  ASN   A N    1 
ATOM   1484 C  CA   . ASN   A 1 59  ? 28.159 12.527  8.227   1.00 10.92 ?  59  ASN   A CA   1 
ATOM   1485 C  C    . ASN   A 1 59  ? 29.473 11.847  8.622   1.00 10.63 ?  59  ASN   A C    1 
ATOM   1486 O  O    . ASN   A 1 59  ? 30.392 11.796  7.795   1.00 10.68 ?  59  ASN   A O    1 
ATOM   1487 C  CB   . ASN   A 1 59  ? 28.441 13.912  7.615   1.00 10.89 ?  59  ASN   A CB   1 
ATOM   1488 C  CG   . ASN   A 1 59  ? 28.808 13.843  6.146   1.00 11.22 ?  59  ASN   A CG   1 
ATOM   1489 O  OD1  . ASN   A 1 59  ? 28.104 13.228  5.345   1.00 11.66 ?  59  ASN   A OD1  1 
ATOM   1490 N  ND2  . ASN   A 1 59  ? 29.904 14.507  5.775   1.00 11.84 ?  59  ASN   A ND2  1 
ATOM   1491 H  H    . ASN   A 1 59  ? 26.564 11.964  9.209   1.00 13.16 ?  59  ASN   A H    1 
ATOM   1492 H  HA   . ASN   A 1 59  ? 27.778 11.993  7.518   1.00 13.11 ?  59  ASN   A HA   1 
ATOM   1493 H  HB2  . ASN   A 1 59  ? 27.648 14.463  7.694   1.00 13.07 ?  59  ASN   A HB2  1 
ATOM   1494 H  HB3  . ASN   A 1 59  ? 29.181 14.325  8.085   1.00 13.07 ?  59  ASN   A HB3  1 
ATOM   1495 H  HD21 . ASN   A 1 59  ? 30.158 14.504  4.951   1.00 14.21 ?  59  ASN   A HD21 1 
ATOM   1496 H  HD22 . ASN   A 1 59  ? 30.376 14.933  6.360   1.00 14.21 ?  59  ASN   A HD22 1 
ATOM   1497 N  N    . ALA   A 1 60  ? 29.595 11.305  9.834   1.00 10.74 ?  60  ALA   A N    1 
ATOM   1498 C  CA   . ALA   A 1 60  ? 30.830 10.619  10.194  1.00 11.06 ?  60  ALA   A CA   1 
ATOM   1499 C  C    . ALA   A 1 60  ? 31.053 9.384   9.330   1.00 10.68 ?  60  ALA   A C    1 
ATOM   1500 O  O    . ALA   A 1 60  ? 32.197 9.055   8.996   1.00 11.08 ?  60  ALA   A O    1 
ATOM   1501 C  CB   . ALA   A 1 60  ? 30.815 10.248  11.674  1.00 11.58 ?  60  ALA   A CB   1 
ATOM   1502 H  H    . ALA   A 1 60  ? 28.994 11.317  10.447  1.00 12.89 ?  60  ALA   A H    1 
ATOM   1503 H  HA   . ALA   A 1 60  ? 31.578 11.222  10.047  1.00 13.27 ?  60  ALA   A HA   1 
ATOM   1504 H  HB1  . ALA   A 1 60  ? 31.644 9.796   11.896  1.00 13.90 ?  60  ALA   A HB1  1 
ATOM   1505 H  HB2  . ALA   A 1 60  ? 30.732 11.061  12.201  1.00 13.90 ?  60  ALA   A HB2  1 
ATOM   1506 H  HB3  . ALA   A 1 60  ? 30.061 9.665   11.846  1.00 13.90 ?  60  ALA   A HB3  1 
ATOM   1507 N  N    . MET   A 1 61  ? 29.979 8.694   8.945   1.00 10.25 ?  61  MET   A N    1 
ATOM   1508 C  CA   . MET   A 1 61  ? 30.120 7.552   8.046   1.00 10.19 ?  61  MET   A CA   1 
ATOM   1509 C  C    . MET   A 1 61  ? 30.752 7.968   6.719   1.00 10.10 ?  61  MET   A C    1 
ATOM   1510 O  O    . MET   A 1 61  ? 31.654 7.286   6.212   1.00 10.58 ?  61  MET   A O    1 
ATOM   1511 C  CB   . MET   A 1 61  ? 28.761 6.882   7.844   1.00 10.27 ?  61  MET   A CB   1 
ATOM   1512 C  CG   . MET   A 1 61  ? 28.766 5.716   6.875   1.00 10.88 ?  61  MET   A CG   1 
ATOM   1513 S  SD   . MET   A 1 61  ? 27.143 4.974   6.646   1.00 11.74 ?  61  MET   A SD   1 
ATOM   1514 C  CE   . MET   A 1 61  ? 26.997 4.084   8.197   1.00 13.42 ?  61  MET   A CE   1 
ATOM   1515 H  H    . MET   A 1 61  ? 29.171 8.864   9.179   1.00 12.30 ?  61  MET   A H    1 
ATOM   1516 H  HA   . MET   A 1 61  ? 30.702 6.900   8.468   1.00 12.23 ?  61  MET   A HA   1 
ATOM   1517 H  HB2  . MET   A 1 61  ? 28.451 6.548   8.700   1.00 12.32 ?  61  MET   A HB2  1 
ATOM   1518 H  HB3  . MET   A 1 61  ? 28.137 7.538   7.504   1.00 12.32 ?  61  MET   A HB3  1 
ATOM   1519 H  HG2  . MET   A 1 61  ? 29.062 6.012   6.005   1.00 13.05 ?  61  MET   A HG2  1 
ATOM   1520 H  HG3  . MET   A 1 61  ? 29.354 5.019   7.210   1.00 13.05 ?  61  MET   A HG3  1 
ATOM   1521 H  HE1  . MET   A 1 61  ? 26.151 3.606   8.211   1.00 16.10 ?  61  MET   A HE1  1 
ATOM   1522 H  HE2  . MET   A 1 61  ? 27.731 3.455   8.270   1.00 16.10 ?  61  MET   A HE2  1 
ATOM   1523 H  HE3  . MET   A 1 61  ? 27.028 4.715   8.935   1.00 16.10 ?  61  MET   A HE3  1 
ATOM   1524 N  N    . GLN   A 1 62  ? 30.318 9.104   6.159   1.00 9.87  ?  62  GLN   A N    1 
ATOM   1525 C  CA   . GLN   A 1 62  ? 30.884 9.572   4.897   1.00 10.15 ?  62  GLN   A CA   1 
ATOM   1526 C  C    . GLN   A 1 62  ? 32.356 9.950   5.046   1.00 10.14 ?  62  GLN   A C    1 
ATOM   1527 O  O    . GLN   A 1 62  ? 33.169 9.633   4.174   1.00 10.41 ?  62  GLN   A O    1 
ATOM   1528 C  CB   . GLN   A 1 62  ? 30.081 10.753  4.357   1.00 10.23 ?  62  GLN   A CB   1 
ATOM   1529 C  CG   . GLN   A 1 62  ? 30.466 11.116  2.932   1.00 10.44 ?  62  GLN   A CG   1 
ATOM   1530 C  CD   . GLN   A 1 62  ? 30.139 9.991   1.979   1.00 10.31 ?  62  GLN   A CD   1 
ATOM   1531 O  OE1  . GLN   A 1 62  ? 28.956 9.684   1.768   1.00 11.11 ?  62  GLN   A OE1  1 
ATOM   1532 N  NE2  . GLN   A 1 62  ? 31.159 9.319   1.453   1.00 10.96 ?  62  GLN   A NE2  1 
ATOM   1533 H  H    . GLN   A 1 62  ? 29.704 9.606   6.488   1.00 11.84 ?  62  GLN   A H    1 
ATOM   1534 H  HA   . GLN   A 1 62  ? 30.834 8.848   4.252   1.00 12.18 ?  62  GLN   A HA   1 
ATOM   1535 H  HB2  . GLN   A 1 62  ? 29.139 10.523  4.368   1.00 12.27 ?  62  GLN   A HB2  1 
ATOM   1536 H  HB3  . GLN   A 1 62  ? 30.243 11.526  4.919   1.00 12.27 ?  62  GLN   A HB3  1 
ATOM   1537 H  HG2  . GLN   A 1 62  ? 29.961 11.897  2.659   1.00 12.53 ?  62  GLN   A HG2  1 
ATOM   1538 H  HG3  . GLN   A 1 62  ? 31.415 11.292  2.889   1.00 12.53 ?  62  GLN   A HG3  1 
ATOM   1539 H  HE21 . GLN   A 1 62  ? 31.968 9.552   1.640   1.00 13.15 ?  62  GLN   A HE21 1 
ATOM   1540 H  HE22 . GLN   A 1 62  ? 31.016 8.665   0.914   1.00 13.15 ?  62  GLN   A HE22 1 
ATOM   1541 N  N    . VAL   A 1 63  ? 32.715 10.628  6.139   1.00 10.72 ?  63  VAL   A N    1 
ATOM   1542 C  CA   . VAL   A 1 63  ? 34.111 11.015  6.358   1.00 11.56 ?  63  VAL   A CA   1 
ATOM   1543 C  C    . VAL   A 1 63  ? 35.005 9.779   6.424   1.00 10.74 ?  63  VAL   A C    1 
ATOM   1544 O  O    . VAL   A 1 63  ? 36.057 9.707   5.773   1.00 11.41 ?  63  VAL   A O    1 
ATOM   1545 C  CB   . VAL   A 1 63  ? 34.222 11.887  7.622   1.00 13.23 ?  63  VAL   A CB   1 
ATOM   1546 C  CG1  . VAL   A 1 63  ? 35.674 12.125  7.988   1.00 14.75 ?  63  VAL   A CG1  1 
ATOM   1547 C  CG2  . VAL   A 1 63  ? 33.497 13.224  7.411   1.00 13.79 ?  63  VAL   A CG2  1 
ATOM   1548 H  H    . VAL   A 1 63  ? 32.170 10.879  6.763   1.00 12.87 ?  63  VAL   A H    1 
ATOM   1549 H  HA   . VAL   A 1 63  ? 34.401 11.550  5.606   1.00 13.87 ?  63  VAL   A HA   1 
ATOM   1550 H  HB   . VAL   A 1 63  ? 33.799 11.429  8.365   1.00 15.88 ?  63  VAL   A HB   1 
ATOM   1551 H  HG11 . VAL   A 1 63  ? 35.722 12.859  8.620   1.00 17.69 ?  63  VAL   A HG11 1 
ATOM   1552 H  HG12 . VAL   A 1 63  ? 36.037 11.320  8.387   1.00 17.69 ?  63  VAL   A HG12 1 
ATOM   1553 H  HG13 . VAL   A 1 63  ? 36.167 12.350  7.183   1.00 17.69 ?  63  VAL   A HG13 1 
ATOM   1554 H  HG21 . VAL   A 1 63  ? 33.590 13.765  8.213   1.00 16.54 ?  63  VAL   A HG21 1 
ATOM   1555 H  HG22 . VAL   A 1 63  ? 33.895 13.685  6.656   1.00 16.54 ?  63  VAL   A HG22 1 
ATOM   1556 H  HG23 . VAL   A 1 63  ? 32.559 13.051  7.237   1.00 16.54 ?  63  VAL   A HG23 1 
ATOM   1557 N  N    . GLU   A 1 64  ? 34.586 8.774   7.197   1.00 10.86 ?  64  GLU   A N    1 
ATOM   1558 C  CA   . GLU   A 1 64  ? 35.344 7.532   7.288   1.00 10.96 ?  64  GLU   A CA   1 
ATOM   1559 C  C    . GLU   A 1 64  ? 35.426 6.843   5.931   1.00 10.72 ?  64  GLU   A C    1 
ATOM   1560 O  O    . GLU   A 1 64  ? 36.475 6.300   5.554   1.00 11.18 ?  64  GLU   A O    1 
ATOM   1561 C  CB   . GLU   A 1 64  ? 34.654 6.625   8.306   1.00 11.51 ?  64  GLU   A CB   1 
ATOM   1562 C  CG   . GLU   A 1 64  ? 35.293 5.269   8.451   1.00 12.44 ?  64  GLU   A CG   1 
ATOM   1563 C  CD   . GLU   A 1 64  ? 34.409 4.282   9.185   1.00 12.97 ?  64  GLU   A CD   1 
ATOM   1564 O  OE1  . GLU   A 1 64  ? 33.170 4.377   9.054   1.00 13.38 ?  64  GLU   A OE1  1 
ATOM   1565 O  OE2  . GLU   A 1 64  ? 34.955 3.391   9.875   1.00 13.23 -1 64  GLU   A OE2  1 
ATOM   1566 H  H    . GLU   A 1 64  ? 33.865 8.787   7.667   1.00 13.03 ?  64  GLU   A H    1 
ATOM   1567 H  HA   . GLU   A 1 64  ? 36.243 7.728   7.603   1.00 13.16 ?  64  GLU   A HA   1 
ATOM   1568 H  HB2  . GLU   A 1 64  ? 34.681 7.061   9.179   1.00 13.81 ?  64  GLU   A HB2  1 
ATOM   1569 H  HB3  . GLU   A 1 64  ? 33.734 6.502   8.034   1.00 13.81 ?  64  GLU   A HB3  1 
ATOM   1570 H  HG2  . GLU   A 1 64  ? 35.483 4.901   7.571   1.00 14.92 ?  64  GLU   A HG2  1 
ATOM   1571 H  HG3  . GLU   A 1 64  ? 36.119 5.362   8.950   1.00 14.92 ?  64  GLU   A HG3  1 
ATOM   1572 N  N    . SER   A 1 65  ? 34.314 6.843   5.194   1.00 10.27 ?  65  SER   A N    1 
ATOM   1573 C  CA   . SER   A 1 65  ? 34.264 6.180   3.897   1.00 10.17 ?  65  SER   A CA   1 
ATOM   1574 C  C    . SER   A 1 65  ? 35.189 6.846   2.887   1.00 10.39 ?  65  SER   A C    1 
ATOM   1575 O  O    . SER   A 1 65  ? 35.829 6.164   2.081   1.00 11.40 ?  65  SER   A O    1 
ATOM   1576 C  CB   . SER   A 1 65  ? 32.833 6.180   3.364   1.00 10.35 ?  65  SER   A CB   1 
ATOM   1577 O  OG   . SER   A 1 65  ? 31.974 5.378   4.165   1.00 10.85 ?  65  SER   A OG   1 
ATOM   1578 H  H    . SER   A 1 65  ? 33.581 7.230   5.423   1.00 12.32 ?  65  SER   A H    1 
ATOM   1579 H  HA   . SER   A 1 65  ? 34.550 5.261   4.002   1.00 12.21 ?  65  SER   A HA   1 
ATOM   1580 H  HB2  . SER   A 1 65  ? 32.494 7.084   3.359   1.00 12.42 ?  65  SER   A HB2  1 
ATOM   1581 H  HB3  . SER   A 1 65  ? 32.836 5.821   2.462   1.00 12.42 ?  65  SER   A HB3  1 
ATOM   1582 H  HG   . SER   A 1 65  ? 31.964 5.669   4.958   1.00 13.02 ?  65  SER   A HG   1 
ATOM   1583 N  N    . ASP   A 1 66  ? 35.266 8.176   2.904   1.00 10.56 ?  66  ASP   A N    1 
ATOM   1584 C  CA   . ASP   A 1 66  ? 36.129 8.871   1.955   1.00 11.39 ?  66  ASP   A CA   1 
ATOM   1585 C  C    . ASP   A 1 66  ? 37.591 8.521   2.199   1.00 11.50 ?  66  ASP   A C    1 
ATOM   1586 O  O    . ASP   A 1 66  ? 38.363 8.344   1.250   1.00 12.35 ?  66  ASP   A O    1 
ATOM   1587 C  CB   . ASP   A 1 66  ? 35.911 10.380  2.056   1.00 12.68 ?  66  ASP   A CB   1 
ATOM   1588 C  CG   . ASP   A 1 66  ? 34.583 10.839  1.443   1.00 14.68 ?  66  ASP   A CG   1 
ATOM   1589 O  OD1  . ASP   A 1 66  ? 33.872 10.037  0.796   1.00 14.93 ?  66  ASP   A OD1  1 
ATOM   1590 O  OD2  . ASP   A 1 66  ? 34.280 12.044  1.582   1.00 17.30 -1 66  ASP   A OD2  1 
ATOM   1591 H  H    . ASP   A 1 66  ? 34.828 8.690   3.441   1.00 12.67 ?  66  ASP   A H    1 
ATOM   1592 H  HA   . ASP   A 1 66  ? 35.897 8.594   1.056   1.00 13.66 ?  66  ASP   A HA   1 
ATOM   1593 H  HB2  . ASP   A 1 66  ? 35.910 10.641  2.989   1.00 15.22 ?  66  ASP   A HB2  1 
ATOM   1594 H  HB3  . ASP   A 1 66  ? 36.630 10.835  1.586   1.00 15.22 ?  66  ASP   A HB3  1 
ATOM   1595 N  N    . ASP   A 1 67  ? 37.984 8.396   3.465   1.00 11.58 ?  67  ASP   A N    1 
ATOM   1596 C  CA   . ASP   A 1 67  ? 39.338 7.947   3.769   1.00 12.20 ?  67  ASP   A CA   1 
ATOM   1597 C  C    . ASP   A 1 67  ? 39.563 6.511   3.301   1.00 12.14 ?  67  ASP   A C    1 
ATOM   1598 O  O    . ASP   A 1 67  ? 40.629 6.182   2.762   1.00 12.86 ?  67  ASP   A O    1 
ATOM   1599 C  CB   . ASP   A 1 67  ? 39.610 8.086   5.266   1.00 13.66 ?  67  ASP   A CB   1 
ATOM   1600 C  CG   . ASP   A 1 67  ? 40.906 7.423   5.688   1.00 14.87 ?  67  ASP   A CG   1 
ATOM   1601 O  OD1  . ASP   A 1 67  ? 41.981 8.058   5.566   1.00 17.70 ?  67  ASP   A OD1  1 
ATOM   1602 O  OD2  . ASP   A 1 67  ? 40.851 6.259   6.143   1.00 14.76 -1 67  ASP   A OD2  1 
ATOM   1603 H  H    . ASP   A 1 67  ? 37.498 8.564   4.149   1.00 13.90 ?  67  ASP   A H    1 
ATOM   1604 H  HA   . ASP   A 1 67  ? 39.972 8.513   3.296   1.00 14.64 ?  67  ASP   A HA   1 
ATOM   1605 H  HB2  . ASP   A 1 67  ? 39.669 9.024   5.487   1.00 16.40 ?  67  ASP   A HB2  1 
ATOM   1606 H  HB3  . ASP   A 1 67  ? 38.886 7.667   5.755   1.00 16.40 ?  67  ASP   A HB3  1 
ATOM   1607 N  N    . TYR   A 1 68  ? 38.568 5.636   3.497   1.00 11.93 ?  68  TYR   A N    1 
ATOM   1608 C  CA   . TYR   A 1 68  ? 38.684 4.254   3.028   1.00 12.05 ?  68  TYR   A CA   1 
ATOM   1609 C  C    . TYR   A 1 68  ? 38.927 4.197   1.519   1.00 11.78 ?  68  TYR   A C    1 
ATOM   1610 O  O    . TYR   A 1 68  ? 39.809 3.466   1.048   1.00 12.35 ?  68  TYR   A O    1 
ATOM   1611 C  CB   . TYR   A 1 68  ? 37.441 3.429   3.412   1.00 12.49 ?  68  TYR   A CB   1 
ATOM   1612 C  CG   . TYR   A 1 68  ? 37.467 2.039   2.784   1.00 14.10 ?  68  TYR   A CG   1 
ATOM   1613 C  CD1  . TYR   A 1 68  ? 37.007 1.839   1.486   1.00 15.44 ?  68  TYR   A CD1  1 
ATOM   1614 C  CD2  . TYR   A 1 68  ? 37.999 0.953   3.458   1.00 15.83 ?  68  TYR   A CD2  1 
ATOM   1615 C  CE1  . TYR   A 1 68  ? 37.076 0.618   0.874   1.00 16.93 ?  68  TYR   A CE1  1 
ATOM   1616 C  CE2  . TYR   A 1 68  ? 38.063 -0.309  2.846   1.00 16.49 ?  68  TYR   A CE2  1 
ATOM   1617 C  CZ   . TYR   A 1 68  ? 37.606 -0.453  1.554   1.00 17.08 ?  68  TYR   A CZ   1 
ATOM   1618 O  OH   . TYR   A 1 68  ? 37.679 -1.672  0.928   1.00 18.61 ?  68  TYR   A OH   1 
ATOM   1619 H  H    . TYR   A 1 68  ? 37.823 5.817   3.894   1.00 14.32 ?  68  TYR   A H    1 
ATOM   1620 H  HA   . TYR   A 1 68  ? 39.447 3.846   3.464   1.00 14.45 ?  68  TYR   A HA   1 
ATOM   1621 H  HB2  . TYR   A 1 68  ? 37.412 3.326   4.377   1.00 14.99 ?  68  TYR   A HB2  1 
ATOM   1622 H  HB3  . TYR   A 1 68  ? 36.644 3.889   3.102   1.00 14.99 ?  68  TYR   A HB3  1 
ATOM   1623 H  HD1  . TYR   A 1 68  ? 36.662 2.568   1.015   1.00 18.53 ?  68  TYR   A HD1  1 
ATOM   1624 H  HD2  . TYR   A 1 68  ? 38.330 1.061   4.318   1.00 19.00 ?  68  TYR   A HD2  1 
ATOM   1625 H  HE1  . TYR   A 1 68  ? 36.756 0.513   0.007   1.00 20.32 ?  68  TYR   A HE1  1 
ATOM   1626 H  HE2  . TYR   A 1 68  ? 38.425 -1.039  3.291   1.00 19.78 ?  68  TYR   A HE2  1 
ATOM   1627 H  HH   . TYR   A 1 68  ? 38.009 -2.241  1.448   1.00 22.33 ?  68  TYR   A HH   1 
ATOM   1628 N  N    . ILE   A 1 69  ? 38.144 4.956   0.742   1.00 11.04 ?  69  ILE   A N    1 
ATOM   1629 C  CA   . ILE   A 1 69  ? 38.285 4.943   -0.714  1.00 11.31 ?  69  ILE   A CA   1 
ATOM   1630 C  C    . ILE   A 1 69  ? 39.620 5.555   -1.142  1.00 11.42 ?  69  ILE   A C    1 
ATOM   1631 O  O    . ILE   A 1 69  ? 40.270 5.070   -2.077  1.00 11.81 ?  69  ILE   A O    1 
ATOM   1632 C  CB   . ILE   A 1 69  ? 37.084 5.645   -1.386  1.00 12.45 ?  69  ILE   A CB   1 
ATOM   1633 C  CG1  . ILE   A 1 69  ? 35.771 4.904   -1.118  1.00 12.80 ?  69  ILE   A CG1  1 
ATOM   1634 C  CG2  . ILE   A 1 69  ? 37.334 5.832   -2.891  1.00 14.13 ?  69  ILE   A CG2  1 
ATOM   1635 C  CD1  . ILE   A 1 69  ? 35.623 3.618   -1.891  1.00 13.50 ?  69  ILE   A CD1  1 
ATOM   1636 H  H    . ILE   A 1 69  ? 37.538 5.489   1.037   1.00 13.25 ?  69  ILE   A H    1 
ATOM   1637 H  HA   . ILE   A 1 69  ? 38.285 4.020   -1.009  1.00 13.57 ?  69  ILE   A HA   1 
ATOM   1638 H  HB   . ILE   A 1 69  ? 37.007 6.524   -0.995  1.00 14.94 ?  69  ILE   A HB   1 
ATOM   1639 H  HG12 . ILE   A 1 69  ? 35.723 4.690   -0.171  1.00 15.36 ?  69  ILE   A HG12 1 
ATOM   1640 H  HG13 . ILE   A 1 69  ? 35.032 5.486   -1.357  1.00 15.36 ?  69  ILE   A HG13 1 
ATOM   1641 H  HG21 . ILE   A 1 69  ? 36.489 6.031   -3.328  1.00 16.95 ?  69  ILE   A HG21 1 
ATOM   1642 H  HG22 . ILE   A 1 69  ? 37.948 6.577   -3.020  1.00 16.95 ?  69  ILE   A HG22 1 
ATOM   1643 H  HG23 . ILE   A 1 69  ? 37.713 5.023   -3.259  1.00 16.95 ?  69  ILE   A HG23 1 
ATOM   1644 H  HD11 . ILE   A 1 69  ? 34.832 3.156   -1.576  1.00 16.21 ?  69  ILE   A HD11 1 
ATOM   1645 H  HD12 . ILE   A 1 69  ? 35.527 3.829   -2.834  1.00 16.21 ?  69  ILE   A HD12 1 
ATOM   1646 H  HD13 . ILE   A 1 69  ? 36.407 3.071   -1.749  1.00 16.21 ?  69  ILE   A HD13 1 
ATOM   1647 N  N    . ALA   A 1 70  ? 40.039 6.638   -0.489  1.00 11.92 ?  70  ALA   A N    1 
ATOM   1648 C  CA   . ALA   A 1 70  ? 41.321 7.242   -0.846  1.00 12.78 ?  70  ALA   A CA   1 
ATOM   1649 C  C    . ALA   A 1 70  ? 42.472 6.257   -0.662  1.00 13.08 ?  70  ALA   A C    1 
ATOM   1650 O  O    . ALA   A 1 70  ? 43.454 6.302   -1.408  1.00 15.44 ?  70  ALA   A O    1 
ATOM   1651 C  CB   . ALA   A 1 70  ? 41.556 8.507   -0.022  1.00 13.41 ?  70  ALA   A CB   1 
ATOM   1652 H  H    . ALA   A 1 70  ? 39.609 7.034   0.138   1.00 14.31 ?  70  ALA   A H    1 
ATOM   1653 H  HA   . ALA   A 1 70  ? 41.294 7.503   -1.782  1.00 15.34 ?  70  ALA   A HA   1 
ATOM   1654 H  HB1  . ALA   A 1 70  ? 42.415 8.890   -0.274  1.00 16.09 ?  70  ALA   A HB1  1 
ATOM   1655 H  HB2  . ALA   A 1 70  ? 40.848 9.143   -0.201  1.00 16.09 ?  70  ALA   A HB2  1 
ATOM   1656 H  HB3  . ALA   A 1 70  ? 41.566 8.273   0.919   1.00 16.09 ?  70  ALA   A HB3  1 
ATOM   1657 N  N    . THR   A 1 71  ? 42.362 5.358   0.311   1.00 12.51 ?  71  THR   A N    1 
ATOM   1658 C  CA   . THR   A 1 71  ? 43.415 4.379   0.567   1.00 14.38 ?  71  THR   A CA   1 
ATOM   1659 C  C    . THR   A 1 71  ? 43.297 3.150   -0.327  1.00 14.36 ?  71  THR   A C    1 
ATOM   1660 O  O    . THR   A 1 71  ? 44.313 2.631   -0.812  1.00 16.23 ?  71  THR   A O    1 
ATOM   1661 C  CB   . THR   A 1 71  ? 43.335 3.926   2.021   1.00 16.53 ?  71  THR   A CB   1 
ATOM   1662 O  OG1  . THR   A 1 71  ? 43.577 5.047   2.874   1.00 17.73 ?  71  THR   A OG1  1 
ATOM   1663 C  CG2  . THR   A 1 71  ? 44.345 2.817   2.309   1.00 17.99 ?  71  THR   A CG2  1 
ATOM   1664 H  H    . THR   A 1 71  ? 41.684 5.289   0.834   1.00 15.01 ?  71  THR   A H    1 
ATOM   1665 H  HA   . THR   A 1 71  ? 44.279 4.785   0.412   1.00 17.26 ?  71  THR   A HA   1 
ATOM   1666 H  HB   . THR   A 1 71  ? 42.445 3.566   2.188   1.00 19.84 ?  71  THR   A HB   1 
ATOM   1667 H  HG1  . THR   A 1 71  ? 42.983 5.628   2.741   1.00 21.28 ?  71  THR   A HG1  1 
ATOM   1668 H  HG21 . THR   A 1 71  ? 44.480 2.735   3.266   1.00 21.59 ?  71  THR   A HG21 1 
ATOM   1669 H  HG22 . THR   A 1 71  ? 44.029 1.966   1.964   1.00 21.59 ?  71  THR   A HG22 1 
ATOM   1670 H  HG23 . THR   A 1 71  ? 45.198 3.027   1.891   1.00 21.59 ?  71  THR   A HG23 1 
ATOM   1671 N  N    . ASN   A 1 72  ? 42.072 2.646   -0.519  1.00 13.34 ?  72  ASN   A N    1 
ATOM   1672 C  CA   . ASN   A 1 72  ? 41.854 1.319   -1.081  1.00 13.80 ?  72  ASN   A CA   1 
ATOM   1673 C  C    . ASN   A 1 72  ? 41.236 1.306   -2.467  1.00 13.86 ?  72  ASN   A C    1 
ATOM   1674 O  O    . ASN   A 1 72  ? 41.238 0.249   -3.113  1.00 15.09 ?  72  ASN   A O    1 
ATOM   1675 C  CB   . ASN   A 1 72  ? 40.960 0.503   -0.142  1.00 14.40 ?  72  ASN   A CB   1 
ATOM   1676 C  CG   . ASN   A 1 72  ? 41.572 0.342   1.222   1.00 15.59 ?  72  ASN   A CG   1 
ATOM   1677 O  OD1  . ASN   A 1 72  ? 41.129 0.948   2.194   1.00 17.31 ?  72  ASN   A OD1  1 
ATOM   1678 N  ND2  . ASN   A 1 72  ? 42.615 -0.454  1.297   1.00 15.75 ?  72  ASN   A ND2  1 
ATOM   1679 H  H    . ASN   A 1 72  ? 41.341 3.060   -0.326  1.00 16.01 ?  72  ASN   A H    1 
ATOM   1680 H  HA   . ASN   A 1 72  ? 42.707 0.867   -1.144  1.00 16.56 ?  72  ASN   A HA   1 
ATOM   1681 H  HB2  . ASN   A 1 72  ? 40.107 0.951   -0.045  1.00 17.28 ?  72  ASN   A HB2  1 
ATOM   1682 H  HB3  . ASN   A 1 72  ? 40.830 -0.383  -0.522  1.00 17.28 ?  72  ASN   A HB3  1 
ATOM   1683 H  HD21 . ASN   A 1 72  ? 43.008 -0.577  2.052   1.00 18.90 ?  72  ASN   A HD21 1 
ATOM   1684 H  HD22 . ASN   A 1 72  ? 42.906 -0.853  0.592   1.00 18.90 ?  72  ASN   A HD22 1 
ATOM   1685 N  N    . GLY   A 1 73  ? 40.688 2.424   -2.932  1.00 13.22 ?  73  GLY   A N    1 
ATOM   1686 C  CA   . GLY   A 1 73  ? 39.952 2.440   -4.171  1.00 13.03 ?  73  GLY   A CA   1 
ATOM   1687 C  C    . GLY   A 1 73  ? 38.558 1.857   -4.007  1.00 12.40 ?  73  GLY   A C    1 
ATOM   1688 O  O    . GLY   A 1 73  ? 38.167 1.403   -2.926  1.00 12.96 ?  73  GLY   A O    1 
ATOM   1689 H  H    . GLY   A 1 73  ? 40.741 3.199   -2.547  1.00 15.86 ?  73  GLY   A H    1 
ATOM   1690 H  HA2  . GLY   A 1 73  ? 39.871 3.358   -4.485  1.00 15.63 ?  73  GLY   A HA2  1 
ATOM   1691 H  HA3  . GLY   A 1 73  ? 40.433 1.929   -4.840  1.00 15.63 ?  73  GLY   A HA3  1 
ATOM   1692 N  N    . PRO   A 1 74  ? 37.783 1.868   -5.089  1.00 12.90 ?  74  PRO   A N    1 
ATOM   1693 C  CA   . PRO   A 1 74  ? 36.384 1.437   -5.011  1.00 12.77 ?  74  PRO   A CA   1 
ATOM   1694 C  C    . PRO   A 1 74  ? 36.235 -0.045  -4.694  1.00 12.10 ?  74  PRO   A C    1 
ATOM   1695 O  O    . PRO   A 1 74  ? 37.106 -0.877  -4.968  1.00 13.32 ?  74  PRO   A O    1 
ATOM   1696 C  CB   . PRO   A 1 74  ? 35.840 1.737   -6.414  1.00 14.80 ?  74  PRO   A CB   1 
ATOM   1697 C  CG   . PRO   A 1 74  ? 36.784 2.713   -7.011  1.00 17.54 ?  74  PRO   A CG   1 
ATOM   1698 C  CD   . PRO   A 1 74  ? 38.123 2.394   -6.421  1.00 15.05 ?  74  PRO   A CD   1 
ATOM   1699 H  HA   . PRO   A 1 74  ? 35.904 1.966   -4.353  1.00 15.33 ?  74  PRO   A HA   1 
ATOM   1700 H  HB2  . PRO   A 1 74  ? 35.817 0.918   -6.931  1.00 17.76 ?  74  PRO   A HB2  1 
ATOM   1701 H  HB3  . PRO   A 1 74  ? 34.953 2.121   -6.338  1.00 17.76 ?  74  PRO   A HB3  1 
ATOM   1702 H  HG2  . PRO   A 1 74  ? 36.806 2.603   -7.973  1.00 21.05 ?  74  PRO   A HG2  1 
ATOM   1703 H  HG3  . PRO   A 1 74  ? 36.519 3.615   -6.775  1.00 21.05 ?  74  PRO   A HG3  1 
ATOM   1704 H  HD2  . PRO   A 1 74  ? 38.581 1.717   -6.948  1.00 18.06 ?  74  PRO   A HD2  1 
ATOM   1705 H  HD3  . PRO   A 1 74  ? 38.662 3.203   -6.349  1.00 18.06 ?  74  PRO   A HD3  1 
ATOM   1706 N  N    . LEU   A 1 75  ? 35.079 -0.363  -4.113  1.00 11.60 ?  75  LEU   A N    1 
ATOM   1707 C  CA   . LEU   A 1 75  ? 34.676 -1.751  -3.965  1.00 10.95 ?  75  LEU   A CA   1 
ATOM   1708 C  C    . LEU   A 1 75  ? 34.291 -2.326  -5.326  1.00 11.63 ?  75  LEU   A C    1 
ATOM   1709 O  O    . LEU   A 1 75  ? 34.180 -1.610  -6.326  1.00 12.83 ?  75  LEU   A O    1 
ATOM   1710 C  CB   . LEU   A 1 75  ? 33.489 -1.869  -3.011  1.00 11.28 ?  75  LEU   A CB   1 
ATOM   1711 C  CG   . LEU   A 1 75  ? 33.698 -1.464  -1.555  1.00 12.94 ?  75  LEU   A CG   1 
ATOM   1712 C  CD1  . LEU   A 1 75  ? 32.417 -1.683  -0.758  1.00 14.94 ?  75  LEU   A CD1  1 
ATOM   1713 C  CD2  . LEU   A 1 75  ? 34.850 -2.172  -0.901  1.00 16.20 ?  75  LEU   A CD2  1 
ATOM   1714 H  H    . LEU   A 1 75  ? 34.515 0.211   -3.801  1.00 13.92 ?  75  LEU   A H    1 
ATOM   1715 H  HA   . LEU   A 1 75  ? 35.414 -2.262  -3.613  1.00 13.14 ?  75  LEU   A HA   1 
ATOM   1716 H  HB2  . LEU   A 1 75  ? 32.770 -1.324  -3.357  1.00 13.54 ?  75  LEU   A HB2  1 
ATOM   1717 H  HB3  . LEU   A 1 75  ? 33.210 -2.799  -3.007  1.00 13.54 ?  75  LEU   A HB3  1 
ATOM   1718 H  HG   . LEU   A 1 75  ? 33.895 -0.513  -1.528  1.00 15.53 ?  75  LEU   A HG   1 
ATOM   1719 H  HD11 . LEU   A 1 75  ? 32.567 -1.416  0.163   1.00 17.92 ?  75  LEU   A HD11 1 
ATOM   1720 H  HD12 . LEU   A 1 75  ? 31.709 -1.145  -1.147  1.00 17.92 ?  75  LEU   A HD12 1 
ATOM   1721 H  HD13 . LEU   A 1 75  ? 32.179 -2.621  -0.796  1.00 17.92 ?  75  LEU   A HD13 1 
ATOM   1722 H  HD21 . LEU   A 1 75  ? 34.895 -1.911  0.032   1.00 19.44 ?  75  LEU   A HD21 1 
ATOM   1723 H  HD22 . LEU   A 1 75  ? 34.715 -3.128  -0.972  1.00 19.44 ?  75  LEU   A HD22 1 
ATOM   1724 H  HD23 . LEU   A 1 75  ? 35.674 -1.920  -1.352  1.00 19.44 ?  75  LEU   A HD23 1 
ATOM   1725 N  N    . LYS   A 1 76  ? 34.095 -3.644  -5.346  1.00 12.08 ?  76  LYS   A N    1 
ATOM   1726 C  CA   . LYS   A 1 76  ? 33.504 -4.363  -6.470  1.00 12.66 ?  76  LYS   A CA   1 
ATOM   1727 C  C    . LYS   A 1 76  ? 31.992 -4.447  -6.274  1.00 11.10 ?  76  LYS   A C    1 
ATOM   1728 O  O    . LYS   A 1 76  ? 31.514 -4.577  -5.149  1.00 11.30 ?  76  LYS   A O    1 
ATOM   1729 C  CB   . LYS   A 1 76  ? 34.047 -5.802  -6.525  1.00 14.33 ?  76  LYS   A CB   1 
ATOM   1730 C  CG   . LYS   A 1 76  ? 35.553 -5.918  -6.730  1.00 15.72 ?  76  LYS   A CG   1 
ATOM   1731 C  CD   . LYS   A 1 76  ? 36.066 -7.327  -6.532  1.00 16.94 ?  76  LYS   A CD   1 
ATOM   1732 C  CE   . LYS   A 1 76  ? 37.559 -7.391  -6.756  1.00 19.41 ?  76  LYS   A CE   1 
ATOM   1733 N  NZ   . LYS   A 1 76  ? 38.085 -8.750  -6.539  1.00 20.16 ?  76  LYS   A NZ   1 
ATOM   1734 H  H    . LYS   A 1 76  ? 34.310 -4.162  -4.691  1.00 14.50 ?  76  LYS   A H    1 
ATOM   1735 H  HA   . LYS   A 1 76  ? 33.703 -3.909  -7.305  1.00 15.20 ?  76  LYS   A HA   1 
ATOM   1736 H  HB2  . LYS   A 1 76  ? 33.830 -6.243  -5.688  1.00 17.19 ?  76  LYS   A HB2  1 
ATOM   1737 H  HB3  . LYS   A 1 76  ? 33.614 -6.263  -7.259  1.00 17.19 ?  76  LYS   A HB3  1 
ATOM   1738 H  HG2  . LYS   A 1 76  ? 35.771 -5.641  -7.635  1.00 18.87 ?  76  LYS   A HG2  1 
ATOM   1739 H  HG3  . LYS   A 1 76  ? 36.005 -5.341  -6.092  1.00 18.87 ?  76  LYS   A HG3  1 
ATOM   1740 H  HD2  . LYS   A 1 76  ? 35.879 -7.618  -5.625  1.00 20.32 ?  76  LYS   A HD2  1 
ATOM   1741 H  HD3  . LYS   A 1 76  ? 35.637 -7.922  -7.170  1.00 20.32 ?  76  LYS   A HD3  1 
ATOM   1742 H  HE2  . LYS   A 1 76  ? 37.758 -7.129  -7.668  1.00 23.29 ?  76  LYS   A HE2  1 
ATOM   1743 H  HE3  . LYS   A 1 76  ? 38.001 -6.792  -6.131  1.00 23.29 ?  76  LYS   A HE3  1 
ATOM   1744 H  HZ1  . LYS   A 1 76  ? 38.965 -8.769  -6.675  1.00 24.19 ?  76  LYS   A HZ1  1 
ATOM   1745 H  HZ2  . LYS   A 1 76  ? 37.919 -9.019  -5.705  1.00 24.19 ?  76  LYS   A HZ2  1 
ATOM   1746 H  HZ3  . LYS   A 1 76  ? 37.698 -9.325  -7.104  1.00 24.19 ?  76  LYS   A HZ3  1 
ATOM   1747 N  N    . VAL   A 1 77  ? 31.237 -4.410  -7.379  1.00 11.59 ?  77  VAL   A N    1 
ATOM   1748 C  CA   . VAL   A 1 77  ? 29.829 -4.802  -7.292  1.00 11.65 ?  77  VAL   A CA   1 
ATOM   1749 C  C    . VAL   A 1 77  ? 29.765 -6.256  -6.849  1.00 11.55 ?  77  VAL   A C    1 
ATOM   1750 O  O    . VAL   A 1 77  ? 30.419 -7.129  -7.433  1.00 11.99 ?  77  VAL   A O    1 
ATOM   1751 C  CB   . VAL   A 1 77  ? 29.101 -4.583  -8.627  1.00 12.69 ?  77  VAL   A CB   1 
ATOM   1752 C  CG1  . VAL   A 1 77  ? 27.637 -5.002  -8.515  1.00 13.98 ?  77  VAL   A CG1  1 
ATOM   1753 C  CG2  . VAL   A 1 77  ? 29.208 -3.133  -9.056  1.00 14.36 ?  77  VAL   A CG2  1 
ATOM   1754 H  H    . VAL   A 1 77  ? 31.513 -4.170  -8.157  1.00 13.90 ?  77  VAL   A H    1 
ATOM   1755 H  HA   . VAL   A 1 77  ? 29.395 -4.259  -6.617  1.00 13.98 ?  77  VAL   A HA   1 
ATOM   1756 H  HB   . VAL   A 1 77  ? 29.524 -5.127  -9.310  1.00 15.23 ?  77  VAL   A HB   1 
ATOM   1757 H  HG11 . VAL   A 1 77  ? 27.165 -4.703  -9.305  1.00 16.78 ?  77  VAL   A HG11 1 
ATOM   1758 H  HG12 . VAL   A 1 77  ? 27.591 -5.968  -8.445  1.00 16.78 ?  77  VAL   A HG12 1 
ATOM   1759 H  HG13 . VAL   A 1 77  ? 27.254 -4.593  -7.724  1.00 16.78 ?  77  VAL   A HG13 1 
ATOM   1760 H  HG21 . VAL   A 1 77  ? 28.684 -3.007  -9.863  1.00 17.23 ?  77  VAL   A HG21 1 
ATOM   1761 H  HG22 . VAL   A 1 77  ? 28.863 -2.570  -8.346  1.00 17.23 ?  77  VAL   A HG22 1 
ATOM   1762 H  HG23 . VAL   A 1 77  ? 30.137 -2.919  -9.228  1.00 17.23 ?  77  VAL   A HG23 1 
ATOM   1763 N  N    . GLY   A 1 78  ? 28.989 -6.523  -5.798  1.00 10.91 ?  78  GLY   A N    1 
ATOM   1764 C  CA   . GLY   A 1 78  ? 28.964 -7.816  -5.146  1.00 11.30 ?  78  GLY   A CA   1 
ATOM   1765 C  C    . GLY   A 1 78  ? 29.875 -7.910  -3.942  1.00 10.85 ?  78  GLY   A C    1 
ATOM   1766 O  O    . GLY   A 1 78  ? 29.813 -8.909  -3.213  1.00 11.59 ?  78  GLY   A O    1 
ATOM   1767 H  H    . GLY   A 1 78  ? 28.454 -5.944  -5.444  1.00 13.09 ?  78  GLY   A H    1 
ATOM   1768 H  HA2  . GLY   A 1 78  ? 28.059 -8.006  -4.862  1.00 13.56 ?  78  GLY   A HA2  1 
ATOM   1769 H  HA3  . GLY   A 1 78  ? 29.231 -8.494  -5.788  1.00 13.56 ?  78  GLY   A HA3  1 
ATOM   1770 N  N    . GLY   A 1 79  ? 30.730 -6.904  -3.722  1.00 10.82 ?  79  GLY   A N    1 
ATOM   1771 C  CA   . GLY   A 1 79  ? 31.689 -6.925  -2.642  1.00 11.04 ?  79  GLY   A CA   1 
ATOM   1772 C  C    . GLY   A 1 79  ? 31.239 -6.122  -1.430  1.00 10.60 ?  79  GLY   A C    1 
ATOM   1773 O  O    . GLY   A 1 79  ? 30.123 -5.610  -1.360  1.00 10.99 ?  79  GLY   A O    1 
ATOM   1774 H  H    . GLY   A 1 79  ? 30.765 -6.186  -4.198  1.00 12.98 ?  79  GLY   A H    1 
ATOM   1775 H  HA2  . GLY   A 1 79  ? 31.837 -7.849  -2.369  1.00 13.25 ?  79  GLY   A HA2  1 
ATOM   1776 H  HA3  . GLY   A 1 79  ? 32.531 -6.565  -2.955  1.00 13.25 ?  79  GLY   A HA3  1 
ATOM   1777 N  N    . SER   A 1 80  ? 32.141 -6.032  -0.453  1.00 11.32 ?  80  SER   A N    1 
ATOM   1778 C  CA   . SER   A 1 80  ? 31.819 -5.401  0.817   1.00 10.71 ?  80  SER   A CA   1 
ATOM   1779 C  C    . SER   A 1 80  ? 33.090 -4.953  1.523   1.00 10.73 ?  80  SER   A C    1 
ATOM   1780 O  O    . SER   A 1 80  ? 34.199 -5.395  1.199   1.00 12.37 ?  80  SER   A O    1 
ATOM   1781 C  CB   . SER   A 1 80  ? 31.052 -6.360  1.734   1.00 11.94 ?  80  SER   A CB   1 
ATOM   1782 O  OG   . SER   A 1 80  ? 31.888 -7.408  2.210   1.00 13.78 ?  80  SER   A OG   1 
ATOM   1783 H  H    . SER   A 1 80  ? 32.952 -6.323  -0.505  1.00 13.58 ?  80  SER   A H    1 
ATOM   1784 H  HA   . SER   A 1 80  ? 31.267 -4.619  0.637   1.00 12.85 ?  80  SER   A HA   1 
ATOM   1785 H  HB2  . SER   A 1 80  ? 30.710 -5.854  2.486   1.00 14.33 ?  80  SER   A HB2  1 
ATOM   1786 H  HB3  . SER   A 1 80  ? 30.314 -6.739  1.229   1.00 14.33 ?  80  SER   A HB3  1 
ATOM   1787 H  HG   . SER   A 1 80  ? 32.186 -7.844  1.556   1.00 16.54 ?  80  SER   A HG   1 
ATOM   1788 N  N    . CYS   A 1 81  ? 32.902 -4.097  2.525   1.00 10.43 ?  81  CYS   A N    1 
ATOM   1789 C  CA   . CYS   A 1 81  ? 33.952 -3.810  3.494   1.00 10.70 ?  81  CYS   A CA   1 
ATOM   1790 C  C    . CYS   A 1 81  ? 33.302 -3.579  4.851   1.00 10.64 ?  81  CYS   A C    1 
ATOM   1791 O  O    . CYS   A 1 81  ? 32.137 -3.176  4.934   1.00 11.56 ?  81  CYS   A O    1 
ATOM   1792 C  CB   . CYS   A 1 81  ? 34.822 -2.615  3.077   1.00 11.52 ?  81  CYS   A CB   1 
ATOM   1793 S  SG   . CYS   A 1 81  ? 33.933 -1.046  3.083   1.00 11.65 ?  81  CYS   A SG   1 
ATOM   1794 H  H    . CYS   A 1 81  ? 32.165 -3.674  2.674   1.00 12.52 ?  81  CYS   A H    1 
ATOM   1795 H  HA   . CYS   A 1 81  ? 34.530 -4.584  3.568   1.00 12.84 ?  81  CYS   A HA   1 
ATOM   1796 H  HB2  . CYS   A 1 81  ? 35.571 -2.544  3.694   1.00 13.82 ?  81  CYS   A HB2  1 
ATOM   1797 H  HB3  . CYS   A 1 81  ? 35.158 -2.771  2.177   1.00 13.82 ?  81  CYS   A HB3  1 
ATOM   1798 H  HG   . CYS   A 1 81  ? 34.684 -0.170  2.749   1.00 13.98 ?  81  CYS   A HG   1 
ATOM   1799 N  N    . VAL   A 1 82  ? 34.070 -3.835  5.910   1.00 11.07 ?  82  VAL   A N    1 
ATOM   1800 C  CA   . VAL   A 1 82  ? 33.639 -3.591  7.282   1.00 11.73 ?  82  VAL   A CA   1 
ATOM   1801 C  C    . VAL   A 1 82  ? 34.239 -2.277  7.753   1.00 11.67 ?  82  VAL   A C    1 
ATOM   1802 O  O    . VAL   A 1 82  ? 35.465 -2.109  7.741   1.00 12.31 ?  82  VAL   A O    1 
ATOM   1803 C  CB   . VAL   A 1 82  ? 34.066 -4.729  8.219   1.00 13.02 ?  82  VAL   A CB   1 
ATOM   1804 C  CG1  . VAL   A 1 82  ? 33.602 -4.435  9.636   1.00 14.47 ?  82  VAL   A CG1  1 
ATOM   1805 C  CG2  . VAL   A 1 82  ? 33.518 -6.057  7.731   1.00 14.00 ?  82  VAL   A CG2  1 
ATOM   1806 H  H    . VAL   A 1 82  ? 34.868 -4.167  5.857   1.00 13.29 ?  82  VAL   A H    1 
ATOM   1807 H  HA   . VAL   A 1 82  ? 32.673 -3.511  7.304   1.00 14.07 ?  82  VAL   A HA   1 
ATOM   1808 H  HB   . VAL   A 1 82  ? 35.031 -4.779  8.229   1.00 15.63 ?  82  VAL   A HB   1 
ATOM   1809 H  HG11 . VAL   A 1 82  ? 33.686 -5.242  10.166  1.00 17.36 ?  82  VAL   A HG11 1 
ATOM   1810 H  HG12 . VAL   A 1 82  ? 34.151 -3.731  10.016  1.00 17.36 ?  82  VAL   A HG12 1 
ATOM   1811 H  HG13 . VAL   A 1 82  ? 32.672 -4.152  9.614   1.00 17.36 ?  82  VAL   A HG13 1 
ATOM   1812 H  HG21 . VAL   A 1 82  ? 33.753 -6.747  8.371   1.00 16.80 ?  82  VAL   A HG21 1 
ATOM   1813 H  HG22 . VAL   A 1 82  ? 32.553 -5.994  7.651   1.00 16.80 ?  82  VAL   A HG22 1 
ATOM   1814 H  HG23 . VAL   A 1 82  ? 33.909 -6.261  6.867   1.00 16.80 ?  82  VAL   A HG23 1 
ATOM   1815 N  N    . LEU   A 1 83  ? 33.383 -1.347  8.165   1.00 10.83 ?  83  LEU   A N    1 
ATOM   1816 C  CA   . LEU   A 1 83  ? 33.800 -0.080  8.744   1.00 11.00 ?  83  LEU   A CA   1 
ATOM   1817 C  C    . LEU   A 1 83  ? 33.079 0.102   10.076  1.00 11.15 ?  83  LEU   A C    1 
ATOM   1818 O  O    . LEU   A 1 83  ? 32.364 -0.791  10.546  1.00 11.82 ?  83  LEU   A O    1 
ATOM   1819 C  CB   . LEU   A 1 83  ? 33.550 1.079   7.765   1.00 11.66 ?  83  LEU   A CB   1 
ATOM   1820 C  CG   . LEU   A 1 83  ? 34.457 1.063   6.529   1.00 12.30 ?  83  LEU   A CG   1 
ATOM   1821 C  CD1  . LEU   A 1 83  ? 34.040 2.110   5.516   1.00 13.29 ?  83  LEU   A CD1  1 
ATOM   1822 C  CD2  . LEU   A 1 83  ? 35.935 1.269   6.912   1.00 12.97 ?  83  LEU   A CD2  1 
ATOM   1823 H  H    . LEU   A 1 83  ? 32.526 -1.429  8.114   1.00 12.99 ?  83  LEU   A H    1 
ATOM   1824 H  HA   . LEU   A 1 83  ? 34.750 -0.109  8.922   1.00 13.20 ?  83  LEU   A HA   1 
ATOM   1825 H  HB2  . LEU   A 1 83  ? 32.632 1.040   7.450   1.00 13.99 ?  83  LEU   A HB2  1 
ATOM   1826 H  HB3  . LEU   A 1 83  ? 33.697 1.923   8.224   1.00 13.99 ?  83  LEU   A HB3  1 
ATOM   1827 H  HG   . LEU   A 1 83  ? 34.386 0.199   6.101   1.00 14.76 ?  83  LEU   A HG   1 
ATOM   1828 H  HD11 . LEU   A 1 83  ? 34.636 2.061   4.747   1.00 15.95 ?  83  LEU   A HD11 1 
ATOM   1829 H  HD12 . LEU   A 1 83  ? 33.130 1.933   5.237   1.00 15.95 ?  83  LEU   A HD12 1 
ATOM   1830 H  HD13 . LEU   A 1 83  ? 34.101 2.988   5.921   1.00 15.95 ?  83  LEU   A HD13 1 
ATOM   1831 H  HD21 . LEU   A 1 83  ? 36.458 1.418   6.104   1.00 15.56 ?  83  LEU   A HD21 1 
ATOM   1832 H  HD22 . LEU   A 1 83  ? 36.011 2.041   7.496   1.00 15.56 ?  83  LEU   A HD22 1 
ATOM   1833 H  HD23 . LEU   A 1 83  ? 36.261 0.477   7.369   1.00 15.56 ?  83  LEU   A HD23 1 
ATOM   1834 N  N    . SER   A 1 84  ? 33.293 1.253   10.708  1.00 11.88 ?  84  SER   A N    1 
ATOM   1835 C  CA   . SER   A 1 84  ? 32.646 1.518   11.984  1.00 12.02 ?  84  SER   A CA   1 
ATOM   1836 C  C    . SER   A 1 84  ? 31.128 1.595   11.831  1.00 11.83 ?  84  SER   A C    1 
ATOM   1837 O  O    . SER   A 1 84  ? 30.605 2.047   10.814  1.00 11.85 ?  84  SER   A O    1 
ATOM   1838 C  CB   . SER   A 1 84  ? 33.136 2.845   12.546  1.00 12.93 ?  84  SER   A CB   1 
ATOM   1839 O  OG   . SER   A 1 84  ? 32.513 3.116   13.781  1.00 13.87 ?  84  SER   A OG   1 
ATOM   1840 H  H    . SER   A 1 84  ? 33.798 1.890   10.416  1.00 14.26 ?  84  SER   A H    1 
ATOM   1841 H  HA   . SER   A 1 84  ? 32.867 0.812   12.608  1.00 14.43 ?  84  SER   A HA   1 
ATOM   1842 H  HB2  . SER   A 1 84  ? 34.096 2.802   12.667  1.00 15.52 ?  84  SER   A HB2  1 
ATOM   1843 H  HB3  . SER   A 1 84  ? 32.912 3.553   11.918  1.00 15.52 ?  84  SER   A HB3  1 
ATOM   1844 H  HG   . SER   A 1 84  ? 32.790 3.845   14.091  1.00 16.65 ?  84  SER   A HG   1 
ATOM   1845 N  N    . GLY   A 1 85  ? 30.419 1.186   12.880  1.00 12.58 ?  85  GLY   A N    1 
ATOM   1846 C  CA   . GLY   A 1 85  ? 28.994 1.420   12.966  1.00 13.32 ?  85  GLY   A CA   1 
ATOM   1847 C  C    . GLY   A 1 85  ? 28.625 2.739   13.610  1.00 13.02 ?  85  GLY   A C    1 
ATOM   1848 O  O    . GLY   A 1 85  ? 27.435 3.057   13.714  1.00 13.66 ?  85  GLY   A O    1 
ATOM   1849 H  H    . GLY   A 1 85  ? 30.746 0.769   13.556  1.00 15.10 ?  85  GLY   A H    1 
ATOM   1850 H  HA2  . GLY   A 1 85  ? 28.612 1.402   12.073  1.00 15.98 ?  85  GLY   A HA2  1 
ATOM   1851 H  HA3  . GLY   A 1 85  ? 28.583 0.710   13.481  1.00 15.98 ?  85  GLY   A HA3  1 
ATOM   1852 N  N    . HIS   A 1 86  ? 29.611 3.517   14.053  1.00 12.44 ?  86  HIS   A N    1 
ATOM   1853 C  CA   . HIS   A 1 86  ? 29.378 4.857   14.610  1.00 12.99 ?  86  HIS   A CA   1 
ATOM   1854 C  C    . HIS   A 1 86  ? 28.388 4.745   15.762  1.00 13.80 ?  86  HIS   A C    1 
ATOM   1855 O  O    . HIS   A 1 86  ? 28.568 3.874   16.629  1.00 15.16 ?  86  HIS   A O    1 
ATOM   1856 C  CB   . HIS   A 1 86  ? 29.006 5.826   13.497  1.00 12.95 ?  86  HIS   A CB   1 
ATOM   1857 C  CG   . HIS   A 1 86  ? 30.070 5.930   12.465  1.00 12.89 ?  86  HIS   A CG   1 
ATOM   1858 N  ND1  . HIS   A 1 86  ? 31.152 6.775   12.596  1.00 14.09 ?  86  HIS   A ND1  1 
ATOM   1859 C  CD2  . HIS   A 1 86  ? 30.261 5.242   11.317  1.00 12.76 ?  86  HIS   A CD2  1 
ATOM   1860 C  CE1  . HIS   A 1 86  ? 31.954 6.611   11.560  1.00 13.68 ?  86  HIS   A CE1  1 
ATOM   1861 N  NE2  . HIS   A 1 86  ? 31.443 5.682   10.775  1.00 12.93 ?  86  HIS   A NE2  1 
ATOM   1862 H  H    . HIS   A 1 86  ? 30.435 3.289   14.050  1.00 14.93 ?  86  HIS   A H    1 
ATOM   1863 H  HA   . HIS   A 1 86  ? 30.211 5.174   14.984  1.00 15.59 ?  86  HIS   A HA   1 
ATOM   1864 H  HB2  . HIS   A 1 86  ? 28.190 5.528   13.063  1.00 15.54 ?  86  HIS   A HB2  1 
ATOM   1865 H  HB3  . HIS   A 1 86  ? 28.870 6.715   13.874  1.00 15.54 ?  86  HIS   A HB3  1 
ATOM   1866 H  HD2  . HIS   A 1 86  ? 29.702 4.579   10.968  1.00 15.32 ?  86  HIS   A HD2  1 
ATOM   1867 H  HE1  . HIS   A 1 86  ? 32.743 7.072   11.396  1.00 16.42 ?  86  HIS   A HE1  1 
ATOM   1868 H  HE2  . HIS   A 1 86  ? 31.781 5.405   10.026  1.00 15.51 ?  86  HIS   A HE2  1 
ATOM   1869 N  N    . ASN   A 1 87  ? 27.372 5.596   15.823  1.00 14.93 ?  87  ASN   A N    1 
ATOM   1870 C  CA   . ASN   A 1 87  ? 26.386 5.588   16.889  1.00 15.93 ?  87  ASN   A CA   1 
ATOM   1871 C  C    . ASN   A 1 87  ? 25.262 4.593   16.650  1.00 17.25 ?  87  ASN   A C    1 
ATOM   1872 O  O    . ASN   A 1 87  ? 24.332 4.538   17.458  1.00 19.55 ?  87  ASN   A O    1 
ATOM   1873 C  CB   . ASN   A 1 87  ? 25.786 6.990   17.045  1.00 16.96 ?  87  ASN   A CB   1 
ATOM   1874 C  CG   . ASN   A 1 87  ? 25.288 7.565   15.727  1.00 17.77 ?  87  ASN   A CG   1 
ATOM   1875 O  OD1  . ASN   A 1 87  ? 25.941 7.440   14.694  1.00 18.39 ?  87  ASN   A OD1  1 
ATOM   1876 N  ND2  . ASN   A 1 87  ? 24.129 8.200   15.761  1.00 18.90 ?  87  ASN   A ND2  1 
ATOM   1877 H  H    . ASN   A 1 87  ? 27.227 6.205   15.238  1.00 17.92 ?  87  ASN   A H    1 
ATOM   1878 H  HA   . ASN   A 1 87  ? 26.817 5.349   17.728  1.00 19.12 ?  87  ASN   A HA   1 
ATOM   1879 H  HB2  . ASN   A 1 87  ? 25.033 6.943   17.660  1.00 20.35 ?  87  ASN   A HB2  1 
ATOM   1880 H  HB3  . ASN   A 1 87  ? 26.464 7.583   17.396  1.00 20.35 ?  87  ASN   A HB3  1 
ATOM   1881 H  HD21 . ASN   A 1 87  ? 23.808 8.539   15.040  1.00 22.68 ?  87  ASN   A HD21 1 
ATOM   1882 H  HD22 . ASN   A 1 87  ? 23.702 8.276   16.502  1.00 22.68 ?  87  ASN   A HD22 1 
ATOM   1883 N  N    . LEU   A 1 88  ? 25.326 3.804   15.581  1.00 15.66 ?  88  LEU   A N    1 
ATOM   1884 C  CA   . LEU   A 1 88  ? 24.217 2.943   15.184  1.00 15.74 ?  88  LEU   A CA   1 
ATOM   1885 C  C    . LEU   A 1 88  ? 24.425 1.465   15.484  1.00 15.52 ?  88  LEU   A C    1 
ATOM   1886 O  O    . LEU   A 1 88  ? 23.440 0.738   15.650  1.00 16.50 ?  88  LEU   A O    1 
ATOM   1887 C  CB   . LEU   A 1 88  ? 23.964 3.094   13.681  1.00 16.45 ?  88  LEU   A CB   1 
ATOM   1888 C  CG   . LEU   A 1 88  ? 23.673 4.512   13.187  1.00 18.24 ?  88  LEU   A CG   1 
ATOM   1889 C  CD1  . LEU   A 1 88  ? 23.541 4.516   11.676  1.00 18.67 ?  88  LEU   A CD1  1 
ATOM   1890 C  CD2  . LEU   A 1 88  ? 22.412 5.070   13.838  1.00 19.81 ?  88  LEU   A CD2  1 
ATOM   1891 H  H    . LEU   A 1 88  ? 26.013 3.749   15.064  1.00 18.79 ?  88  LEU   A H    1 
ATOM   1892 H  HA   . LEU   A 1 88  ? 23.419 3.233   15.650  1.00 18.89 ?  88  LEU   A HA   1 
ATOM   1893 H  HB2  . LEU   A 1 88  ? 24.744 2.781   13.205  1.00 19.74 ?  88  LEU   A HB2  1 
ATOM   1894 H  HB3  . LEU   A 1 88  ? 23.198 2.547   13.448  1.00 19.74 ?  88  LEU   A HB3  1 
ATOM   1895 H  HG   . LEU   A 1 88  ? 24.411 5.093   13.423  1.00 21.89 ?  88  LEU   A HG   1 
ATOM   1896 H  HD11 . LEU   A 1 88  ? 23.366 5.421   11.373  1.00 22.40 ?  88  LEU   A HD11 1 
ATOM   1897 H  HD12 . LEU   A 1 88  ? 24.368 4.192   11.287  1.00 22.40 ?  88  LEU   A HD12 1 
ATOM   1898 H  HD13 . LEU   A 1 88  ? 22.806 3.935   11.420  1.00 22.40 ?  88  LEU   A HD13 1 
ATOM   1899 H  HD21 . LEU   A 1 88  ? 22.198 5.925   13.432  1.00 23.77 ?  88  LEU   A HD21 1 
ATOM   1900 H  HD22 . LEU   A 1 88  ? 21.683 4.446   13.697  1.00 23.77 ?  88  LEU   A HD22 1 
ATOM   1901 H  HD23 . LEU   A 1 88  ? 22.572 5.184   14.787  1.00 23.77 ?  88  LEU   A HD23 1 
ATOM   1902 N  N    . ALA   A 1 89  ? 25.673 1.013   15.544  1.00 14.64 ?  89  ALA   A N    1 
ATOM   1903 C  CA   . ALA   A 1 89  ? 26.018 -0.398  15.632  1.00 14.16 ?  89  ALA   A CA   1 
ATOM   1904 C  C    . ALA   A 1 89  ? 27.501 -0.463  15.961  1.00 14.55 ?  89  ALA   A C    1 
ATOM   1905 O  O    . ALA   A 1 89  ? 28.218 0.534   15.850  1.00 15.49 ?  89  ALA   A O    1 
ATOM   1906 C  CB   . ALA   A 1 89  ? 25.750 -1.102  14.303  1.00 13.61 ?  89  ALA   A CB   1 
ATOM   1907 H  H    . ALA   A 1 89  ? 26.360 1.530   15.525  1.00 17.56 ?  89  ALA   A H    1 
ATOM   1908 H  HA   . ALA   A 1 89  ? 25.504 -0.824  16.338  1.00 16.99 ?  89  ALA   A HA   1 
ATOM   1909 H  HB1  . ALA   A 1 89  ? 25.997 -2.036  14.387  1.00 16.33 ?  89  ALA   A HB1  1 
ATOM   1910 H  HB2  . ALA   A 1 89  ? 24.806 -1.028  14.086  1.00 16.33 ?  89  ALA   A HB2  1 
ATOM   1911 H  HB3  . ALA   A 1 89  ? 26.282 -0.680  13.610  1.00 16.33 ?  89  ALA   A HB3  1 
ATOM   1912 N  N    . LYS   A 1 90  ? 27.971 -1.646  16.350  1.00 15.35 ?  90  LYS   A N    1 
ATOM   1913 C  CA   . LYS   A 1 90  ? 29.413 -1.805  16.506  1.00 16.56 ?  90  LYS   A CA   1 
ATOM   1914 C  C    . LYS   A 1 90  ? 30.121 -1.616  15.166  1.00 14.98 ?  90  LYS   A C    1 
ATOM   1915 O  O    . LYS   A 1 90  ? 31.058 -0.808  15.045  1.00 16.28 ?  90  LYS   A O    1 
ATOM   1916 C  CB   . LYS   A 1 90  ? 29.742 -3.168  17.117  1.00 19.38 ?  90  LYS   A CB   1 
ATOM   1917 C  CG   . LYS   A 1 90  ? 31.220 -3.326  17.461  1.00 23.79 ?  90  LYS   A CG   1 
ATOM   1918 C  CD   . LYS   A 1 90  ? 31.463 -4.550  18.331  1.00 28.32 ?  90  LYS   A CD   1 
ATOM   1919 C  CE   . LYS   A 1 90  ? 32.868 -4.557  18.917  1.00 32.21 ?  90  LYS   A CE   1 
ATOM   1920 N  NZ   . LYS   A 1 90  ? 33.909 -4.915  17.915  1.00 34.15 ?  90  LYS   A NZ   1 
ATOM   1921 H  H    . LYS   A 1 90  ? 27.493 -2.337  16.531  1.00 18.42 ?  90  LYS   A H    1 
ATOM   1922 H  HA   . LYS   A 1 90  ? 29.738 -1.122  17.113  1.00 19.87 ?  90  LYS   A HA   1 
ATOM   1923 H  HB2  . LYS   A 1 90  ? 29.229 -3.281  17.935  1.00 23.25 ?  90  LYS   A HB2  1 
ATOM   1924 H  HB3  . LYS   A 1 90  ? 29.505 -3.865  16.484  1.00 23.25 ?  90  LYS   A HB3  1 
ATOM   1925 H  HG2  . LYS   A 1 90  ? 31.730 -3.428  16.642  1.00 28.55 ?  90  LYS   A HG2  1 
ATOM   1926 H  HG3  . LYS   A 1 90  ? 31.520 -2.542  17.948  1.00 28.55 ?  90  LYS   A HG3  1 
ATOM   1927 H  HD2  . LYS   A 1 90  ? 30.828 -4.553  19.066  1.00 33.98 ?  90  LYS   A HD2  1 
ATOM   1928 H  HD3  . LYS   A 1 90  ? 31.354 -5.352  17.795  1.00 33.98 ?  90  LYS   A HD3  1 
ATOM   1929 H  HE2  . LYS   A 1 90  ? 33.073 -3.671  19.256  1.00 38.65 ?  90  LYS   A HE2  1 
ATOM   1930 H  HE3  . LYS   A 1 90  ? 32.909 -5.205  19.637  1.00 38.65 ?  90  LYS   A HE3  1 
ATOM   1931 H  HZ1  . LYS   A 1 90  ? 34.714 -4.910  18.297  1.00 40.98 ?  90  LYS   A HZ1  1 
ATOM   1932 H  HZ2  . LYS   A 1 90  ? 33.750 -5.729  17.589  1.00 40.98 ?  90  LYS   A HZ2  1 
ATOM   1933 H  HZ3  . LYS   A 1 90  ? 33.903 -4.329  17.246  1.00 40.98 ?  90  LYS   A HZ3  1 
ATOM   1934 N  N    . HIS   A 1 91  ? 29.652 -2.327  14.142  1.00 13.12 ?  91  HIS   A N    1 
ATOM   1935 C  CA   . HIS   A 1 91  ? 30.237 -2.315  12.816  1.00 12.57 ?  91  HIS   A CA   1 
ATOM   1936 C  C    . HIS   A 1 91  ? 29.159 -2.041  11.783  1.00 11.38 ?  91  HIS   A C    1 
ATOM   1937 O  O    . HIS   A 1 91  ? 27.994 -2.400  11.973  1.00 12.13 ?  91  HIS   A O    1 
ATOM   1938 C  CB   . HIS   A 1 91  ? 30.828 -3.687  12.463  1.00 15.17 ?  91  HIS   A CB   1 
ATOM   1939 C  CG   . HIS   A 1 91  ? 31.810 -4.205  13.463  1.00 19.18 ?  91  HIS   A CG   1 
ATOM   1940 N  ND1  . HIS   A 1 91  ? 33.098 -3.723  13.559  1.00 21.25 ?  91  HIS   A ND1  1 
ATOM   1941 C  CD2  . HIS   A 1 91  ? 31.701 -5.175  14.401  1.00 21.01 ?  91  HIS   A CD2  1 
ATOM   1942 C  CE1  . HIS   A 1 91  ? 33.739 -4.370  14.517  1.00 22.35 ?  91  HIS   A CE1  1 
ATOM   1943 N  NE2  . HIS   A 1 91  ? 32.913 -5.258  15.043  1.00 22.42 ?  91  HIS   A NE2  1 
ATOM   1944 H  H    . HIS   A 1 91  ? 28.964 -2.852  14.203  1.00 15.75 ?  91  HIS   A H    1 
ATOM   1945 H  HA   . HIS   A 1 91  ? 30.929 -1.642  12.757  1.00 15.09 ?  91  HIS   A HA   1 
ATOM   1946 H  HB2  . HIS   A 1 91  ? 30.105 -4.334  12.402  1.00 18.21 ?  91  HIS   A HB2  1 
ATOM   1947 H  HB3  . HIS   A 1 91  ? 31.281 -3.622  11.609  1.00 18.21 ?  91  HIS   A HB3  1 
ATOM   1948 H  HD1  . HIS   A 1 91  ? 33.434 -3.097  13.070  1.00 25.50 ?  91  HIS   A HD1  1 
ATOM   1949 H  HD2  . HIS   A 1 91  ? 30.952 -5.690  14.581  1.00 25.21 ?  91  HIS   A HD2  1 
ATOM   1950 H  HE1  . HIS   A 1 91  ? 34.624 -4.221  14.775  1.00 26.82 ?  91  HIS   A HE1  1 
ATOM   1951 N  N    . CYS   A 1 92  ? 29.563 -1.441  10.670  1.00 11.23 ?  92  CYS   A N    1 
ATOM   1952 C  CA   . CYS   A 1 92  ? 28.732 -1.372  9.476   1.00 10.85 ?  92  CYS   A CA   1 
ATOM   1953 C  C    . CYS   A 1 92  ? 29.389 -2.190  8.373   1.00 10.53 ?  92  CYS   A C    1 
ATOM   1954 O  O    . CYS   A 1 92  ? 30.553 -1.944  8.019   1.00 11.35 ?  92  CYS   A O    1 
ATOM   1955 C  CB   . CYS   A 1 92  ? 28.519 0.072   9.015   1.00 10.84 ?  92  CYS   A CB   1 
ATOM   1956 S  SG   . CYS   A 1 92  ? 27.526 0.184   7.500   1.00 11.00 ?  92  CYS   A SG   1 
ATOM   1957 H  H    . CYS   A 1 92  ? 30.330 -1.054  10.585  1.00 13.48 ?  92  CYS   A H    1 
ATOM   1958 H  HA   . CYS   A 1 92  ? 27.867 -1.758  9.670   1.00 13.02 ?  92  CYS   A HA   1 
ATOM   1959 H  HB2  . CYS   A 1 92  ? 28.053 0.564   9.710   1.00 13.00 ?  92  CYS   A HB2  1 
ATOM   1960 H  HB3  . CYS   A 1 92  ? 29.378 0.482   8.836   1.00 13.00 ?  92  CYS   A HB3  1 
ATOM   1961 H  HG   . CYS   A 1 92  ? 27.394 1.337   7.211   1.00 13.20 ?  92  CYS   A HG   1 
ATOM   1962 N  N    . LEU   A 1 93  ? 28.653 -3.176  7.863   1.00 10.44 ?  93  LEU   A N    1 
ATOM   1963 C  CA   . LEU   A 1 93  ? 29.059 -3.932  6.686   1.00 10.13 ?  93  LEU   A CA   1 
ATOM   1964 C  C    . LEU   A 1 93  ? 28.467 -3.238  5.462   1.00 9.86  ?  93  LEU   A C    1 
ATOM   1965 O  O    . LEU   A 1 93  ? 27.253 -3.296  5.230   1.00 9.94  ?  93  LEU   A O    1 
ATOM   1966 C  CB   . LEU   A 1 93  ? 28.580 -5.381  6.795   1.00 10.80 ?  93  LEU   A CB   1 
ATOM   1967 C  CG   . LEU   A 1 93  ? 28.972 -6.286  5.626   1.00 11.26 ?  93  LEU   A CG   1 
ATOM   1968 C  CD1  . LEU   A 1 93  ? 30.474 -6.557  5.604   1.00 11.89 ?  93  LEU   A CD1  1 
ATOM   1969 C  CD2  . LEU   A 1 93  ? 28.184 -7.599  5.667   1.00 11.91 ?  93  LEU   A CD2  1 
ATOM   1970 H  H    . LEU   A 1 93  ? 27.899 -3.424  8.196   1.00 12.53 ?  93  LEU   A H    1 
ATOM   1971 H  HA   . LEU   A 1 93  ? 30.022 -3.925  6.614   1.00 12.15 ?  93  LEU   A HA   1 
ATOM   1972 H  HB2  . LEU   A 1 93  ? 28.955 -5.767  7.605   1.00 12.95 ?  93  LEU   A HB2  1 
ATOM   1973 H  HB3  . LEU   A 1 93  ? 27.614 -5.385  6.853   1.00 12.95 ?  93  LEU   A HB3  1 
ATOM   1974 H  HG   . LEU   A 1 93  ? 28.755 -5.840  4.800   1.00 13.51 ?  93  LEU   A HG   1 
ATOM   1975 H  HD11 . LEU   A 1 93  ? 30.677 -7.163  4.874   1.00 14.26 ?  93  LEU   A HD11 1 
ATOM   1976 H  HD12 . LEU   A 1 93  ? 30.948 -5.721  5.484   1.00 14.26 ?  93  LEU   A HD12 1 
ATOM   1977 H  HD13 . LEU   A 1 93  ? 30.736 -6.965  6.449   1.00 14.26 ?  93  LEU   A HD13 1 
ATOM   1978 H  HD21 . LEU   A 1 93  ? 28.453 -8.155  4.918   1.00 14.30 ?  93  LEU   A HD21 1 
ATOM   1979 H  HD22 . LEU   A 1 93  ? 28.366 -8.057  6.501   1.00 14.30 ?  93  LEU   A HD22 1 
ATOM   1980 H  HD23 . LEU   A 1 93  ? 27.236 -7.396  5.602   1.00 14.30 ?  93  LEU   A HD23 1 
ATOM   1981 N  N    . HIS   A 1 94  ? 29.322 -2.550  4.701   1.00 9.46  ?  94  HIS   A N    1 
ATOM   1982 C  CA   . HIS   A 1 94  ? 28.906 -1.882  3.469   1.00 9.64  ?  94  HIS   A CA   1 
ATOM   1983 C  C    . HIS   A 1 94  ? 28.917 -2.921  2.361   1.00 9.58  ?  94  HIS   A C    1 
ATOM   1984 O  O    . HIS   A 1 94  ? 29.984 -3.437  2.021   1.00 11.22 ?  94  HIS   A O    1 
ATOM   1985 C  CB   . HIS   A 1 94  ? 29.867 -0.738  3.142   1.00 9.73  ?  94  HIS   A CB   1 
ATOM   1986 C  CG   . HIS   A 1 94  ? 29.857 0.355   4.157   1.00 9.57  ?  94  HIS   A CG   1 
ATOM   1987 N  ND1  . HIS   A 1 94  ? 28.982 1.421   4.099   1.00 9.50  ?  94  HIS   A ND1  1 
ATOM   1988 C  CD2  . HIS   A 1 94  ? 30.586 0.518   5.285   1.00 10.22 ?  94  HIS   A CD2  1 
ATOM   1989 C  CE1  . HIS   A 1 94  ? 29.198 2.205   5.140   1.00 9.62  ?  94  HIS   A CE1  1 
ATOM   1990 N  NE2  . HIS   A 1 94  ? 30.159 1.677   5.877   1.00 10.23 ?  94  HIS   A NE2  1 
ATOM   1991 H  H    . HIS   A 1 94  ? 30.156 -2.450  4.881   1.00 11.35 ?  94  HIS   A H    1 
ATOM   1992 H  HA   . HIS   A 1 94  ? 28.003 -1.530  3.566   1.00 11.57 ?  94  HIS   A HA   1 
ATOM   1993 H  HB2  . HIS   A 1 94  ? 30.762 -1.088  3.093   1.00 11.67 ?  94  HIS   A HB2  1 
ATOM   1994 H  HB3  . HIS   A 1 94  ? 29.608 -0.351  2.289   1.00 11.67 ?  94  HIS   A HB3  1 
ATOM   1995 H  HD2  . HIS   A 1 94  ? 31.254 -0.038  5.596   1.00 12.26 ?  94  HIS   A HD2  1 
ATOM   1996 H  HE1  . HIS   A 1 94  ? 28.731 2.993   5.327   1.00 11.54 ?  94  HIS   A HE1  1 
ATOM   1997 H  HE2  . HIS   A 1 94  ? 30.467 2.021   6.602   1.00 12.27 ?  94  HIS   A HE2  1 
ATOM   1998 N  N    . VAL   A 1 95  ? 27.746 -3.242  1.809   1.00 9.00  ?  95  VAL   A N    1 
ATOM   1999 C  CA   . VAL   A 1 95  ? 27.601 -4.273  0.787   1.00 9.40  ?  95  VAL   A CA   1 
ATOM   2000 C  C    . VAL   A 1 95  ? 27.055 -3.635  -0.480  1.00 9.03  ?  95  VAL   A C    1 
ATOM   2001 O  O    . VAL   A 1 95  ? 26.051 -2.914  -0.429  1.00 9.60  ?  95  VAL   A O    1 
ATOM   2002 C  CB   . VAL   A 1 95  ? 26.680 -5.421  1.242   1.00 10.03 ?  95  VAL   A CB   1 
ATOM   2003 C  CG1  . VAL   A 1 95  ? 26.568 -6.459  0.136   1.00 10.71 ?  95  VAL   A CG1  1 
ATOM   2004 C  CG2  . VAL   A 1 95  ? 27.180 -6.043  2.533   1.00 10.35 ?  95  VAL   A CG2  1 
ATOM   2005 H  H    . VAL   A 1 95  ? 27.002 -2.866  2.022   1.00 10.80 ?  95  VAL   A H    1 
ATOM   2006 H  HA   . VAL   A 1 95  ? 28.468 -4.646  0.583   1.00 11.28 ?  95  VAL   A HA   1 
ATOM   2007 H  HB   . VAL   A 1 95  ? 25.792 -5.068  1.403   1.00 12.04 ?  95  VAL   A HB   1 
ATOM   2008 H  HG11 . VAL   A 1 95  ? 26.187 -7.274  0.504   1.00 12.85 ?  95  VAL   A HG11 1 
ATOM   2009 H  HG12 . VAL   A 1 95  ? 25.992 -6.120  -0.568  1.00 12.85 ?  95  VAL   A HG12 1 
ATOM   2010 H  HG13 . VAL   A 1 95  ? 27.452 -6.644  -0.219  1.00 12.85 ?  95  VAL   A HG13 1 
ATOM   2011 H  HG21 . VAL   A 1 95  ? 26.613 -6.802  2.756   1.00 12.42 ?  95  VAL   A HG21 1 
ATOM   2012 H  HG22 . VAL   A 1 95  ? 28.093 -6.339  2.410   1.00 12.42 ?  95  VAL   A HG22 1 
ATOM   2013 H  HG23 . VAL   A 1 95  ? 27.134 -5.381  3.239   1.00 12.42 ?  95  VAL   A HG23 1 
ATOM   2014 N  N    . VAL   A 1 96  ? 27.694 -3.923  -1.612  1.00 9.19  ?  96  VAL   A N    1 
ATOM   2015 C  CA   . VAL   A 1 96  ? 27.291 -3.380  -2.901  1.00 10.02 ?  96  VAL   A CA   1 
ATOM   2016 C  C    . VAL   A 1 96  ? 26.486 -4.435  -3.657  1.00 10.25 ?  96  VAL   A C    1 
ATOM   2017 O  O    . VAL   A 1 96  ? 27.044 -5.381  -4.223  1.00 11.02 ?  96  VAL   A O    1 
ATOM   2018 C  CB   . VAL   A 1 96  ? 28.489 -2.901  -3.720  1.00 10.42 ?  96  VAL   A CB   1 
ATOM   2019 C  CG1  . VAL   A 1 96  ? 27.986 -2.263  -4.996  1.00 10.65 ?  96  VAL   A CG1  1 
ATOM   2020 C  CG2  . VAL   A 1 96  ? 29.352 -1.929  -2.918  1.00 11.01 ?  96  VAL   A CG2  1 
ATOM   2021 H  H    . VAL   A 1 96  ? 28.389 -4.436  -1.653  1.00 11.03 ?  96  VAL   A H    1 
ATOM   2022 H  HA   . VAL   A 1 96  ? 26.716 -2.615  -2.748  1.00 12.03 ?  96  VAL   A HA   1 
ATOM   2023 H  HB   . VAL   A 1 96  ? 29.039 -3.661  -3.954  1.00 12.50 ?  96  VAL   A HB   1 
ATOM   2024 H  HG11 . VAL   A 1 96  ? 28.721 -1.787  -5.415  1.00 12.78 ?  96  VAL   A HG11 1 
ATOM   2025 H  HG12 . VAL   A 1 96  ? 27.657 -2.952  -5.587  1.00 12.78 ?  96  VAL   A HG12 1 
ATOM   2026 H  HG13 . VAL   A 1 96  ? 27.276 -1.638  -4.777  1.00 12.78 ?  96  VAL   A HG13 1 
ATOM   2027 H  HG21 . VAL   A 1 96  ? 30.055 -1.584  -3.486  1.00 13.21 ?  96  VAL   A HG21 1 
ATOM   2028 H  HG22 . VAL   A 1 96  ? 28.793 -1.197  -2.601  1.00 13.21 ?  96  VAL   A HG22 1 
ATOM   2029 H  HG23 . VAL   A 1 96  ? 29.736 -2.396  -2.158  1.00 13.21 ?  96  VAL   A HG23 1 
ATOM   2030 N  N    . GLY   A 1 97  ? 25.166 -4.269  -3.695  1.00 10.28 ?  97  GLY   A N    1 
ATOM   2031 C  CA   . GLY   A 1 97  ? 24.353 -5.028  -4.607  1.00 10.79 ?  97  GLY   A CA   1 
ATOM   2032 C  C    . GLY   A 1 97  ? 24.352 -4.373  -5.975  1.00 10.81 ?  97  GLY   A C    1 
ATOM   2033 O  O    . GLY   A 1 97  ? 24.639 -3.179  -6.117  1.00 11.53 ?  97  GLY   A O    1 
ATOM   2034 H  H    . GLY   A 1 97  ? 24.727 -3.719  -3.189  1.00 12.34 ?  97  GLY   A H    1 
ATOM   2035 H  HA2  . GLY   A 1 97  ? 24.711 -5.926  -4.676  1.00 12.94 ?  97  GLY   A HA2  1 
ATOM   2036 H  HA3  . GLY   A 1 97  ? 23.445 -5.076  -4.270  1.00 12.94 ?  97  GLY   A HA3  1 
ATOM   2037 N  N    . PRO   A 1 98  ? 24.036 -5.140  -7.012  1.00 10.96 ?  98  PRO   A N    1 
ATOM   2038 C  CA   . PRO   A 1 98  ? 23.925 -4.547  -8.345  1.00 12.07 ?  98  PRO   A CA   1 
ATOM   2039 C  C    . PRO   A 1 98  ? 22.806 -3.514  -8.408  1.00 12.17 ?  98  PRO   A C    1 
ATOM   2040 O  O    . PRO   A 1 98  ? 21.726 -3.686  -7.835  1.00 12.45 ?  98  PRO   A O    1 
ATOM   2041 C  CB   . PRO   A 1 98  ? 23.626 -5.755  -9.241  1.00 13.03 ?  98  PRO   A CB   1 
ATOM   2042 C  CG   . PRO   A 1 98  ? 22.991 -6.755  -8.327  1.00 12.80 ?  98  PRO   A CG   1 
ATOM   2043 C  CD   . PRO   A 1 98  ? 23.726 -6.579  -7.019  1.00 11.40 ?  98  PRO   A CD   1 
ATOM   2044 H  HA   . PRO   A 1 98  ? 24.765 -4.142  -8.602  1.00 14.48 ?  98  PRO   A HA   1 
ATOM   2045 H  HB2  . PRO   A 1 98  ? 23.014 -5.491  -9.943  1.00 15.63 ?  98  PRO   A HB2  1 
ATOM   2046 H  HB3  . PRO   A 1 98  ? 24.453 -6.099  -9.607  1.00 15.63 ?  98  PRO   A HB3  1 
ATOM   2047 H  HG2  . PRO   A 1 98  ? 22.047 -6.550  -8.221  1.00 15.36 ?  98  PRO   A HG2  1 
ATOM   2048 H  HG3  . PRO   A 1 98  ? 23.116 -7.647  -8.678  1.00 15.36 ?  98  PRO   A HG3  1 
ATOM   2049 H  HD2  . PRO   A 1 98  ? 23.149 -6.814  -6.269  1.00 13.68 ?  98  PRO   A HD2  1 
ATOM   2050 H  HD3  . PRO   A 1 98  ? 24.543 -7.104  -7.011  1.00 13.68 ?  98  PRO   A HD3  1 
ATOM   2051 N  N    A ASN   A 1 99  ? 23.079 -2.396  -9.087  0.64 13.21 ?  99  ASN   A N    1 
ATOM   2052 N  N    B ASN   A 1 99  ? 23.080 -2.454  -9.149  0.36 13.13 ?  99  ASN   A N    1 
ATOM   2053 C  CA   A ASN   A 1 99  ? 22.103 -1.313  -9.264  0.64 14.01 ?  99  ASN   A CA   1 
ATOM   2054 C  CA   B ASN   A 1 99  ? 22.092 -1.451  -9.502  0.36 14.12 ?  99  ASN   A CA   1 
ATOM   2055 C  C    A ASN   A 1 99  ? 21.537 -1.423  -10.677 0.64 15.02 ?  99  ASN   A C    1 
ATOM   2056 C  C    B ASN   A 1 99  ? 21.536 -1.820  -10.873 0.36 14.81 ?  99  ASN   A C    1 
ATOM   2057 O  O    A ASN   A 1 99  ? 22.198 -1.066  -11.657 0.64 16.02 ?  99  ASN   A O    1 
ATOM   2058 O  O    B ASN   A 1 99  ? 22.264 -1.809  -11.872 0.36 14.74 ?  99  ASN   A O    1 
ATOM   2059 C  CB   A ASN   A 1 99  ? 22.735 0.058   -9.017  0.64 13.71 ?  99  ASN   A CB   1 
ATOM   2060 C  CB   B ASN   A 1 99  ? 22.758 -0.082  -9.539  0.36 15.11 ?  99  ASN   A CB   1 
ATOM   2061 C  CG   A ASN   A 1 99  ? 21.703 1.200   -8.989  0.64 13.50 ?  99  ASN   A CG   1 
ATOM   2062 C  CG   B ASN   A 1 99  ? 21.769 1.040   -9.728  0.36 15.93 ?  99  ASN   A CG   1 
ATOM   2063 O  OD1  A ASN   A 1 99  ? 20.685 1.151   -9.682  0.64 14.11 ?  99  ASN   A OD1  1 
ATOM   2064 O  OD1  B ASN   A 1 99  ? 20.811 0.918   -10.489 0.36 15.87 ?  99  ASN   A OD1  1 
ATOM   2065 N  ND2  A ASN   A 1 99  ? 21.984 2.243   -8.201  0.64 13.73 ?  99  ASN   A ND2  1 
ATOM   2066 N  ND2  B ASN   A 1 99  ? 21.991 2.144   -9.028  0.36 16.55 ?  99  ASN   A ND2  1 
ATOM   2067 H  H    A ASN   A 1 99  ? 23.838 -2.231  -9.453  0.64 15.85 ?  99  ASN   A H    1 
ATOM   2068 H  H    B ASN   A 1 99  ? 23.865 -2.285  -9.459  0.36 15.76 ?  99  ASN   A H    1 
ATOM   2069 H  HA   A ASN   A 1 99  ? 21.376 -1.430  -8.628  0.64 16.82 ?  99  ASN   A HA   1 
ATOM   2070 H  HA   B ASN   A 1 99  ? 21.370 -1.451  -8.847  0.36 16.95 ?  99  ASN   A HA   1 
ATOM   2071 H  HB2  A ASN   A 1 99  ? 23.192 0.051   -8.166  0.64 16.45 ?  99  ASN   A HB2  1 
ATOM   2072 H  HB2  B ASN   A 1 99  ? 23.234 0.058   -8.705  0.36 18.13 ?  99  ASN   A HB2  1 
ATOM   2073 H  HB3  A ASN   A 1 99  ? 23.367 0.243   -9.733  0.64 16.45 ?  99  ASN   A HB3  1 
ATOM   2074 H  HB3  B ASN   A 1 99  ? 23.375 -0.069  -10.284 0.36 18.13 ?  99  ASN   A HB3  1 
ATOM   2075 H  HD21 A ASN   A 1 99  ? 21.441 2.914   -8.154  0.64 16.47 ?  99  ASN   A HD21 1 
ATOM   2076 H  HD21 B ASN   A 1 99  ? 21.454 2.809   -9.095  0.36 19.85 ?  99  ASN   A HD21 1 
ATOM   2077 H  HD22 A ASN   A 1 99  ? 22.705 2.246   -7.735  0.64 16.47 ?  99  ASN   A HD22 1 
ATOM   2078 H  HD22 B ASN   A 1 99  ? 22.673 2.189   -8.505  0.36 19.85 ?  99  ASN   A HD22 1 
ATOM   2079 N  N    A VAL   A 1 100 ? 20.297 -1.915  -10.770 0.64 15.95 ?  100 VAL   A N    1 
ATOM   2080 N  N    B VAL   A 1 100 ? 20.244 -2.151  -10.911 0.36 16.59 ?  100 VAL   A N    1 
ATOM   2081 C  CA   A VAL   A 1 100 ? 19.656 -2.115  -12.067 0.64 17.36 ?  100 VAL   A CA   1 
ATOM   2082 C  CA   B VAL   A 1 100 ? 19.599 -2.532  -12.163 0.36 18.80 ?  100 VAL   A CA   1 
ATOM   2083 C  C    A VAL   A 1 100 ? 19.519 -0.799  -12.822 0.64 17.51 ?  100 VAL   A C    1 
ATOM   2084 C  C    B VAL   A 1 100 ? 19.650 -1.393  -13.162 0.36 19.71 ?  100 VAL   A C    1 
ATOM   2085 O  O    A VAL   A 1 100 ? 19.602 -0.772  -14.056 0.64 18.45 ?  100 VAL   A O    1 
ATOM   2086 O  O    B VAL   A 1 100 ? 19.752 -1.619  -14.375 0.36 19.83 ?  100 VAL   A O    1 
ATOM   2087 C  CB   A VAL   A 1 100 ? 18.310 -2.849  -11.888 0.64 18.78 ?  100 VAL   A CB   1 
ATOM   2088 C  CB   B VAL   A 1 100 ? 18.145 -2.957  -11.891 0.36 20.01 ?  100 VAL   A CB   1 
ATOM   2089 C  CG1  A VAL   A 1 100 ? 17.561 -2.963  -13.213 0.64 19.30 ?  100 VAL   A CG1  1 
ATOM   2090 C  CG1  B VAL   A 1 100 ? 17.520 -3.551  -13.144 0.36 20.40 ?  100 VAL   A CG1  1 
ATOM   2091 C  CG2  A VAL   A 1 100 ? 18.550 -4.234  -11.297 0.64 18.64 ?  100 VAL   A CG2  1 
ATOM   2092 C  CG2  B VAL   A 1 100 ? 18.098 -3.933  -10.741 0.36 20.53 ?  100 VAL   A CG2  1 
ATOM   2093 H  H    A VAL   A 1 100 ? 19.804 -2.143  -10.098 0.64 19.14 ?  100 VAL   A H    1 
ATOM   2094 H  H    B VAL   A 1 100 ? 19.726 -2.157  -10.227 0.36 19.91 ?  100 VAL   A H    1 
ATOM   2095 H  HA   A VAL   A 1 100 ? 20.220 -2.690  -12.601 0.64 20.83 ?  100 VAL   A HA   1 
ATOM   2096 H  HA   B VAL   A 1 100 ? 20.069 -3.287  -12.547 0.36 22.56 ?  100 VAL   A HA   1 
ATOM   2097 H  HB   A VAL   A 1 100 ? 17.749 -2.354  -11.272 0.64 22.54 ?  100 VAL   A HB   1 
ATOM   2098 H  HB   B VAL   A 1 100 ? 17.631 -2.169  -11.646 0.36 24.02 ?  100 VAL   A HB   1 
ATOM   2099 H  HG11 A VAL   A 1 100 ? 16.827 -3.593  -13.110 0.64 23.16 ?  100 VAL   A HG11 1 
ATOM   2100 H  HG11 B VAL   A 1 100 ? 16.630 -3.867  -12.929 0.36 24.48 ?  100 VAL   A HG11 1 
ATOM   2101 H  HG12 A VAL   A 1 100 ? 17.213 -2.094  -13.461 0.64 23.16 ?  100 VAL   A HG12 1 
ATOM   2102 H  HG12 B VAL   A 1 100 ? 17.470 -2.867  -13.831 0.36 24.48 ?  100 VAL   A HG12 1 
ATOM   2103 H  HG13 A VAL   A 1 100 ? 18.171 -3.285  -13.896 0.64 23.16 ?  100 VAL   A HG13 1 
ATOM   2104 H  HG13 B VAL   A 1 100 ? 18.071 -4.287  -13.450 0.36 24.48 ?  100 VAL   A HG13 1 
ATOM   2105 H  HG21 A VAL   A 1 100 ? 17.703 -4.705  -11.232 0.64 22.37 ?  100 VAL   A HG21 1 
ATOM   2106 H  HG21 B VAL   A 1 100 ? 17.261 -4.414  -10.775 0.36 24.64 ?  100 VAL   A HG21 1 
ATOM   2107 H  HG22 A VAL   A 1 100 ? 19.155 -4.725  -11.876 0.64 22.37 ?  100 VAL   A HG22 1 
ATOM   2108 H  HG22 B VAL   A 1 100 ? 18.843 -4.548  -10.825 0.36 24.64 ?  100 VAL   A HG22 1 
ATOM   2109 H  HG23 A VAL   A 1 100 ? 18.943 -4.138  -10.415 0.64 22.37 ?  100 VAL   A HG23 1 
ATOM   2110 H  HG23 B VAL   A 1 100 ? 18.167 -3.441  -9.908  0.36 24.64 ?  100 VAL   A HG23 1 
ATOM   2111 N  N    A ASN   A 1 101 ? 19.320 0.309   -12.113 0.64 18.08 ?  101 ASN   A N    1 
ATOM   2112 N  N    B ASN   A 1 101 ? 19.552 -0.155  -12.677 0.36 20.52 ?  101 ASN   A N    1 
ATOM   2113 C  CA   A ASN   A 1 101 ? 19.249 1.595   -12.795 0.64 18.77 ?  101 ASN   A CA   1 
ATOM   2114 C  CA   B ASN   A 1 101 ? 19.523 1.004   -13.557 0.36 21.24 ?  101 ASN   A CA   1 
ATOM   2115 C  C    A ASN   A 1 101 ? 20.598 2.044   -13.355 0.64 21.05 ?  101 ASN   A C    1 
ATOM   2116 C  C    B ASN   A 1 101 ? 20.880 1.286   -14.184 0.36 22.50 ?  101 ASN   A C    1 
ATOM   2117 O  O    A ASN   A 1 101 ? 20.656 3.099   -14.000 0.64 22.63 ?  101 ASN   A O    1 
ATOM   2118 O  O    B ASN   A 1 101 ? 20.942 1.986   -15.200 0.36 22.52 ?  101 ASN   A O    1 
ATOM   2119 C  CB   A ASN   A 1 101 ? 18.625 2.635   -11.864 0.64 18.02 ?  101 ASN   A CB   1 
ATOM   2120 C  CB   B ASN   A 1 101 ? 19.020 2.220   -12.777 0.36 20.91 ?  101 ASN   A CB   1 
ATOM   2121 C  CG   A ASN   A 1 101 ? 17.238 2.211   -11.380 0.64 17.66 ?  101 ASN   A CG   1 
ATOM   2122 C  CG   B ASN   A 1 101 ? 17.792 1.905   -11.941 0.36 21.18 ?  101 ASN   A CG   1 
ATOM   2123 O  OD1  A ASN   A 1 101 ? 16.423 1.709   -12.158 0.64 18.11 ?  101 ASN   A OD1  1 
ATOM   2124 O  OD1  B ASN   A 1 101 ? 16.881 1.206   -12.388 0.36 21.65 ?  101 ASN   A OD1  1 
ATOM   2125 N  ND2  A ASN   A 1 101 ? 16.976 2.390   -10.092 0.64 17.64 ?  101 ASN   A ND2  1 
ATOM   2126 N  ND2  B ASN   A 1 101 ? 17.772 2.404   -10.711 0.36 21.37 ?  101 ASN   A ND2  1 
ATOM   2127 H  H    A ASN   A 1 101 ? 19.218 0.342   -11.262 0.64 21.70 ?  101 ASN   A H    1 
ATOM   2128 H  H    B ASN   A 1 101 ? 19.496 0.039   -11.840 0.36 24.62 ?  101 ASN   A H    1 
ATOM   2129 H  HA   A ASN   A 1 101 ? 18.652 1.499   -13.551 0.64 22.53 ?  101 ASN   A HA   1 
ATOM   2130 H  HA   B ASN   A 1 101 ? 18.903 0.841   -14.278 0.36 25.48 ?  101 ASN   A HA   1 
ATOM   2131 H  HB2  A ASN   A 1 101 ? 19.194 2.754   -11.089 0.64 21.63 ?  101 ASN   A HB2  1 
ATOM   2132 H  HB2  B ASN   A 1 101 ? 19.717 2.516   -12.173 0.36 25.10 ?  101 ASN   A HB2  1 
ATOM   2133 H  HB3  A ASN   A 1 101 ? 18.537 3.477   -12.345 0.64 21.63 ?  101 ASN   A HB3  1 
ATOM   2134 H  HB3  B ASN   A 1 101 ? 18.790 2.934   -13.398 0.36 25.10 ?  101 ASN   A HB3  1 
ATOM   2135 H  HD21 A ASN   A 1 101 ? 16.207 2.165   -9.778  0.64 21.16 ?  101 ASN   A HD21 1 
ATOM   2136 H  HD21 B ASN   A 1 101 ? 17.099 2.253   -10.198 0.36 25.64 ?  101 ASN   A HD21 1 
ATOM   2137 H  HD22 A ASN   A 1 101 ? 17.567 2.738   -9.576  0.64 21.16 ?  101 ASN   A HD22 1 
ATOM   2138 H  HD22 B ASN   A 1 101 ? 18.426 2.887   -10.431 0.36 25.64 ?  101 ASN   A HD22 1 
ATOM   2139 N  N    A LYS   A 1 102 ? 21.665 1.262   -13.149 0.64 22.87 ?  102 LYS   A N    1 
ATOM   2140 N  N    B LYS   A 1 102 ? 21.960 0.761   -13.608 0.36 23.77 ?  102 LYS   A N    1 
ATOM   2141 C  CA   A LYS   A 1 102 ? 22.950 1.464   -13.809 0.64 24.32 ?  102 LYS   A CA   1 
ATOM   2142 C  CA   B LYS   A 1 102 ? 23.293 0.868   -14.186 0.36 24.58 ?  102 LYS   A CA   1 
ATOM   2143 C  C    A LYS   A 1 102 ? 23.269 0.379   -14.829 0.64 25.09 ?  102 LYS   A C    1 
ATOM   2144 C  C    B LYS   A 1 102 ? 23.619 -0.298  -15.113 0.36 23.83 ?  102 LYS   A C    1 
ATOM   2145 O  O    A LYS   A 1 102 ? 24.326 0.443   -15.462 0.64 25.58 ?  102 LYS   A O    1 
ATOM   2146 O  O    B LYS   A 1 102 ? 24.761 -0.411  -15.570 0.36 23.50 ?  102 LYS   A O    1 
ATOM   2147 C  CB   A LYS   A 1 102 ? 24.086 1.519   -12.780 0.64 25.48 ?  102 LYS   A CB   1 
ATOM   2148 C  CB   B LYS   A 1 102 ? 24.351 0.935   -13.077 0.36 26.13 ?  102 LYS   A CB   1 
ATOM   2149 C  CG   A LYS   A 1 102 ? 23.975 2.635   -11.763 0.64 26.40 ?  102 LYS   A CG   1 
ATOM   2150 C  CG   B LYS   A 1 102 ? 24.314 2.192   -12.220 0.36 27.60 ?  102 LYS   A CG   1 
ATOM   2151 C  CD   A LYS   A 1 102 ? 25.156 2.601   -10.802 0.64 27.56 ?  102 LYS   A CD   1 
ATOM   2152 C  CD   B LYS   A 1 102 ? 25.278 2.074   -11.043 0.36 29.09 ?  102 LYS   A CD   1 
ATOM   2153 C  CE   A LYS   A 1 102 ? 25.069 3.704   -9.762  0.64 28.37 ?  102 LYS   A CE   1 
ATOM   2154 C  CE   B LYS   A 1 102 ? 25.334 3.353   -10.222 0.36 30.26 ?  102 LYS   A CE   1 
ATOM   2155 N  NZ   A LYS   A 1 102 ? 26.182 3.617   -8.772  0.64 28.74 ?  102 LYS   A NZ   1 
ATOM   2156 N  NZ   B LYS   A 1 102 ? 26.644 4.049   -10.373 0.36 30.91 ?  102 LYS   A NZ   1 
ATOM   2157 H  H    A LYS   A 1 102 ? 21.666 0.582   -12.620 0.64 27.44 ?  102 LYS   A H    1 
ATOM   2158 H  H    B LYS   A 1 102 ? 21.943 0.327   -12.865 0.36 28.52 ?  102 LYS   A H    1 
ATOM   2159 H  HA   A LYS   A 1 102 ? 22.938 2.303   -14.284 0.64 29.18 ?  102 LYS   A HA   1 
ATOM   2160 H  HA   B LYS   A 1 102 ? 23.347 1.694   -14.695 0.36 29.50 ?  102 LYS   A HA   1 
ATOM   2161 H  HB2  A LYS   A 1 102 ? 24.105 0.680   -12.293 0.64 30.57 ?  102 LYS   A HB2  1 
ATOM   2162 H  HB2  B LYS   A 1 102 ? 24.224 0.180   -12.484 0.36 31.36 ?  102 LYS   A HB2  1 
ATOM   2163 H  HB3  A LYS   A 1 102 ? 24.927 1.637   -13.252 0.64 30.57 ?  102 LYS   A HB3  1 
ATOM   2164 H  HB3  B LYS   A 1 102 ? 25.232 0.884   -13.485 0.36 31.36 ?  102 LYS   A HB3  1 
ATOM   2165 H  HG2  A LYS   A 1 102 ? 23.974 3.489   -12.223 0.64 31.68 ?  102 LYS   A HG2  1 
ATOM   2166 H  HG2  B LYS   A 1 102 ? 24.579 2.956   -12.756 0.36 33.12 ?  102 LYS   A HG2  1 
ATOM   2167 H  HG3  A LYS   A 1 102 ? 23.158 2.524   -11.252 0.64 31.68 ?  102 LYS   A HG3  1 
ATOM   2168 H  HG3  B LYS   A 1 102 ? 23.418 2.317   -11.871 0.36 33.12 ?  102 LYS   A HG3  1 
ATOM   2169 H  HD2  A LYS   A 1 102 ? 25.167 1.748   -10.341 0.64 33.07 ?  102 LYS   A HD2  1 
ATOM   2170 H  HD2  B LYS   A 1 102 ? 24.990 1.355   -10.460 0.36 34.90 ?  102 LYS   A HD2  1 
ATOM   2171 H  HD3  A LYS   A 1 102 ? 25.978 2.720   -11.305 0.64 33.07 ?  102 LYS   A HD3  1 
ATOM   2172 H  HD3  B LYS   A 1 102 ? 26.170 1.892   -11.378 0.36 34.90 ?  102 LYS   A HD3  1 
ATOM   2173 H  HE2  A LYS   A 1 102 ? 25.123 4.565   -10.207 0.64 34.04 ?  102 LYS   A HE2  1 
ATOM   2174 H  HE2  B LYS   A 1 102 ? 24.635 3.955   -10.521 0.36 36.31 ?  102 LYS   A HE2  1 
ATOM   2175 H  HE3  A LYS   A 1 102 ? 24.228 3.626   -9.285  0.64 34.04 ?  102 LYS   A HE3  1 
ATOM   2176 H  HE3  B LYS   A 1 102 ? 25.211 3.137   -9.284  0.36 36.31 ?  102 LYS   A HE3  1 
ATOM   2177 H  HZ1  A LYS   A 1 102 ? 26.108 4.271   -8.175  0.64 34.49 ?  102 LYS   A HZ1  1 
ATOM   2178 H  HZ1  B LYS   A 1 102 ? 26.652 4.793   -9.885  0.36 37.09 ?  102 LYS   A HZ1  1 
ATOM   2179 H  HZ2  A LYS   A 1 102 ? 26.150 2.834   -8.350  0.64 34.49 ?  102 LYS   A HZ2  1 
ATOM   2180 H  HZ2  B LYS   A 1 102 ? 27.305 3.517   -10.100 0.36 37.09 ?  102 LYS   A HZ2  1 
ATOM   2181 H  HZ3  A LYS   A 1 102 ? 26.965 3.689   -9.189  0.64 34.49 ?  102 LYS   A HZ3  1 
ATOM   2182 H  HZ3  B LYS   A 1 102 ? 26.779 4.262   -11.227 0.36 37.09 ?  102 LYS   A HZ3  1 
ATOM   2183 N  N    A GLY   A 1 103 ? 22.399 -0.617  -14.997 0.64 26.08 ?  103 GLY   A N    1 
ATOM   2184 N  N    B GLY   A 1 103 ? 22.655 -1.175  -15.385 0.36 23.68 ?  103 GLY   A N    1 
ATOM   2185 C  CA   A GLY   A 1 103 ? 22.647 -1.696  -15.934 0.64 26.52 ?  103 GLY   A CA   1 
ATOM   2186 C  CA   B GLY   A 1 103 ? 22.915 -2.328  -16.224 0.36 23.28 ?  103 GLY   A CA   1 
ATOM   2187 C  C    A GLY   A 1 103 ? 23.499 -2.826  -15.404 0.64 26.90 ?  103 GLY   A C    1 
ATOM   2188 C  C    B GLY   A 1 103 ? 23.714 -3.429  -15.567 0.36 22.39 ?  103 GLY   A C    1 
ATOM   2189 O  O    A GLY   A 1 103 ? 24.086 -3.564  -16.200 0.64 28.01 ?  103 GLY   A O    1 
ATOM   2190 O  O    B GLY   A 1 103 ? 24.195 -4.330  -16.262 0.36 22.70 ?  103 GLY   A O    1 
ATOM   2191 H  H    A GLY   A 1 103 ? 21.658 -0.692  -14.577 0.64 31.29 ?  103 GLY   A H    1 
ATOM   2192 H  H    B GLY   A 1 103 ? 21.848 -1.121  -15.091 0.36 28.41 ?  103 GLY   A H    1 
ATOM   2193 H  HA2  A GLY   A 1 103 ? 21.795 -2.064  -16.231 0.64 31.82 ?  103 GLY   A HA2  1 
ATOM   2194 H  HA2  B GLY   A 1 103 ? 22.072 -2.711  -16.503 0.36 27.93 ?  103 GLY   A HA2  1 
ATOM   2195 H  HA3  A GLY   A 1 103 ? 23.104 -1.346  -16.713 0.64 31.82 ?  103 GLY   A HA3  1 
ATOM   2196 H  HA3  B GLY   A 1 103 ? 23.389 -2.028  -17.018 0.36 27.93 ?  103 GLY   A HA3  1 
ATOM   2197 N  N    A GLU   A 1 104 ? 23.590 -2.990  -14.087 0.64 25.44 ?  104 GLU   A N    1 
ATOM   2198 N  N    B GLU   A 1 104 ? 23.855 -3.399  -14.246 0.36 20.89 ?  104 GLU   A N    1 
ATOM   2199 C  CA   A GLU   A 1 104 ? 24.460 -3.995  -13.493 0.64 24.03 ?  104 GLU   A CA   1 
ATOM   2200 C  CA   B GLU   A 1 104 ? 24.734 -4.331  -13.555 0.36 19.59 ?  104 GLU   A CA   1 
ATOM   2201 C  C    A GLU   A 1 104 ? 23.766 -5.353  -13.401 0.64 24.22 ?  104 GLU   A C    1 
ATOM   2202 C  C    B GLU   A 1 104 ? 24.064 -5.694  -13.393 0.36 19.55 ?  104 GLU   A C    1 
ATOM   2203 O  O    A GLU   A 1 104 ? 22.539 -5.447  -13.305 0.64 24.32 ?  104 GLU   A O    1 
ATOM   2204 O  O    B GLU   A 1 104 ? 22.862 -5.791  -13.124 0.36 19.33 ?  104 GLU   A O    1 
ATOM   2205 C  CB   A GLU   A 1 104 ? 24.962 -3.517  -12.126 0.64 22.20 ?  104 GLU   A CB   1 
ATOM   2206 C  CB   B GLU   A 1 104 ? 25.152 -3.741  -12.205 0.36 18.79 ?  104 GLU   A CB   1 
ATOM   2207 C  CG   A GLU   A 1 104 ? 25.947 -2.348  -12.273 0.64 21.58 ?  104 GLU   A CG   1 
ATOM   2208 C  CG   B GLU   A 1 104 ? 25.813 -2.366  -12.361 0.36 18.88 ?  104 GLU   A CG   1 
ATOM   2209 C  CD   A GLU   A 1 104 ? 26.239 -1.564  -10.999 0.64 20.73 ?  104 GLU   A CD   1 
ATOM   2210 C  CD   B GLU   A 1 104 ? 26.259 -1.727  -11.055 0.36 18.63 ?  104 GLU   A CD   1 
ATOM   2211 O  OE1  A GLU   A 1 104 ? 25.640 -1.842  -9.941  0.64 19.26 ?  104 GLU   A OE1  1 
ATOM   2212 O  OE1  B GLU   A 1 104 ? 25.737 -2.089  -9.983  0.36 17.95 ?  104 GLU   A OE1  1 
ATOM   2213 O  OE2  A GLU   A 1 104 ? 27.081 -0.637  -11.080 0.64 21.62 -1 104 GLU   A OE2  1 
ATOM   2214 O  OE2  B GLU   A 1 104 ? 27.140 -0.840  -11.113 0.36 19.38 -1 104 GLU   A OE2  1 
ATOM   2215 H  H    A GLU   A 1 104 ? 23.161 -2.516  -13.512 0.64 30.52 ?  104 GLU   A H    1 
ATOM   2216 H  H    B GLU   A 1 104 ? 23.447 -2.842  -13.730 0.36 25.07 ?  104 GLU   A H    1 
ATOM   2217 H  HA   A GLU   A 1 104 ? 25.232 -4.104  -14.067 0.64 28.84 ?  104 GLU   A HA   1 
ATOM   2218 H  HA   B GLU   A 1 104 ? 25.541 -4.448  -14.084 0.36 23.51 ?  104 GLU   A HA   1 
ATOM   2219 H  HB2  A GLU   A 1 104 ? 24.206 -3.220  -11.597 0.64 26.64 ?  104 GLU   A HB2  1 
ATOM   2220 H  HB2  B GLU   A 1 104 ? 24.370 -3.637  -11.644 0.36 22.55 ?  104 GLU   A HB2  1 
ATOM   2221 H  HB3  A GLU   A 1 104 ? 25.418 -4.250  -11.683 0.64 26.64 ?  104 GLU   A HB3  1 
ATOM   2222 H  HB3  B GLU   A 1 104 ? 25.794 -4.334  -11.784 0.36 22.55 ?  104 GLU   A HB3  1 
ATOM   2223 H  HG2  A GLU   A 1 104 ? 26.787 -2.697  -12.603 0.64 25.89 ?  104 GLU   A HG2  1 
ATOM   2224 H  HG2  B GLU   A 1 104 ? 26.597 -2.457  -12.923 0.36 22.66 ?  104 GLU   A HG2  1 
ATOM   2225 H  HG3  A GLU   A 1 104 ? 25.579 -1.718  -12.910 0.64 25.89 ?  104 GLU   A HG3  1 
ATOM   2226 H  HG3  B GLU   A 1 104 ? 25.180 -1.762  -12.781 0.36 22.66 ?  104 GLU   A HG3  1 
ATOM   2227 N  N    A ASP   A 1 105 ? 24.580 -6.410  -13.434 0.64 24.64 ?  105 ASP   A N    1 
ATOM   2228 N  N    B ASP   A 1 105 ? 24.862 -6.746  -13.571 0.36 20.69 ?  105 ASP   A N    1 
ATOM   2229 C  CA   A ASP   A 1 105 ? 24.087 -7.775  -13.592 0.64 25.76 ?  105 ASP   A CA   1 
ATOM   2230 C  CA   B ASP   A 1 105 ? 24.370 -8.120  -13.610 0.36 21.95 ?  105 ASP   A CA   1 
ATOM   2231 C  C    A ASP   A 1 105 ? 23.411 -8.257  -12.311 0.64 23.60 ?  105 ASP   A C    1 
ATOM   2232 C  C    B ASP   A 1 105 ? 23.605 -8.466  -12.339 0.36 21.74 ?  105 ASP   A C    1 
ATOM   2233 O  O    A ASP   A 1 105 ? 24.053 -8.358  -11.262 0.64 21.67 ?  105 ASP   A O    1 
ATOM   2234 O  O    B ASP   A 1 105 ? 24.172 -8.464  -11.242 0.36 20.86 ?  105 ASP   A O    1 
ATOM   2235 C  CB   A ASP   A 1 105 ? 25.258 -8.689  -13.946 0.64 28.98 ?  105 ASP   A CB   1 
ATOM   2236 C  CB   B ASP   A 1 105 ? 25.574 -9.049  -13.767 0.36 23.41 ?  105 ASP   A CB   1 
ATOM   2237 C  CG   A ASP   A 1 105 ? 24.823 -10.109 -14.226 0.64 31.74 ?  105 ASP   A CG   1 
ATOM   2238 C  CG   B ASP   A 1 105 ? 25.190 -10.510 -13.905 0.36 24.45 ?  105 ASP   A CG   1 
ATOM   2239 O  OD1  A ASP   A 1 105 ? 23.602 -10.342 -14.339 0.64 32.30 ?  105 ASP   A OD1  1 
ATOM   2240 O  OD1  B ASP   A 1 105 ? 23.982 -10.817 -13.981 0.36 24.43 ?  105 ASP   A OD1  1 
ATOM   2241 O  OD2  A ASP   A 1 105 ? 25.704 -10.989 -14.338 0.64 33.31 -1 105 ASP   A OD2  1 
ATOM   2242 O  OD2  B ASP   A 1 105 ? 26.113 -11.356 -13.934 0.36 25.29 -1 105 ASP   A OD2  1 
ATOM   2243 H  H    A ASP   A 1 105 ? 25.437 -6.361  -13.369 0.64 29.57 ?  105 ASP   A H    1 
ATOM   2244 H  H    B ASP   A 1 105 ? 25.709 -6.679  -13.683 0.36 24.82 ?  105 ASP   A H    1 
ATOM   2245 H  HA   A ASP   A 1 105 ? 23.442 -7.815  -14.315 0.64 30.91 ?  105 ASP   A HA   1 
ATOM   2246 H  HA   B ASP   A 1 105 ? 23.774 -8.231  -14.368 0.36 26.34 ?  105 ASP   A HA   1 
ATOM   2247 H  HB2  A ASP   A 1 105 ? 25.693 -8.357  -14.749 0.64 34.77 ?  105 ASP   A HB2  1 
ATOM   2248 H  HB2  B ASP   A 1 105 ? 26.070 -8.780  -14.555 0.36 28.09 ?  105 ASP   A HB2  1 
ATOM   2249 H  HB3  A ASP   A 1 105 ? 25.893 -8.696  -13.209 0.64 34.77 ?  105 ASP   A HB3  1 
ATOM   2250 H  HB3  B ASP   A 1 105 ? 26.130 -8.972  -12.979 0.36 28.09 ?  105 ASP   A HB3  1 
ATOM   2251 N  N    A ILE   A 1 106 ? 22.122 -8.592  -12.406 0.64 23.20 ?  106 ILE   A N    1 
ATOM   2252 N  N    B ILE   A 1 106 ? 22.318 -8.788  -12.490 0.36 22.37 ?  106 ILE   A N    1 
ATOM   2253 C  CA   A ILE   A 1 106 ? 21.365 -9.013  -11.233 0.64 22.38 ?  106 ILE   A CA   1 
ATOM   2254 C  CA   B ILE   A 1 106 ? 21.504 -9.140  -11.332 0.36 23.01 ?  106 ILE   A CA   1 
ATOM   2255 C  C    A ILE   A 1 106 ? 21.916 -10.296 -10.629 0.64 21.58 ?  106 ILE   A C    1 
ATOM   2256 C  C    B ILE   A 1 106 ? 21.992 -10.421 -10.674 0.36 22.91 ?  106 ILE   A C    1 
ATOM   2257 O  O    A ILE   A 1 106 ? 21.713 -10.549 -9.438  0.64 20.80 ?  106 ILE   A O    1 
ATOM   2258 O  O    B ILE   A 1 106 ? 21.750 -10.632 -9.481  0.36 22.60 ?  106 ILE   A O    1 
ATOM   2259 C  CB   A ILE   A 1 106 ? 19.860 -9.119  -11.572 0.64 23.52 ?  106 ILE   A CB   1 
ATOM   2260 C  CB   B ILE   A 1 106 ? 20.007 -9.216  -11.706 0.36 24.14 ?  106 ILE   A CB   1 
ATOM   2261 C  CG1  A ILE   A 1 106 ? 19.018 -9.228  -10.298 0.64 23.88 ?  106 ILE   A CG1  1 
ATOM   2262 C  CG1  B ILE   A 1 106 ? 19.134 -9.184  -10.449 0.36 24.73 ?  106 ILE   A CG1  1 
ATOM   2263 C  CG2  A ILE   A 1 106 ? 19.592 -10.315 -12.470 0.64 24.00 ?  106 ILE   A CG2  1 
ATOM   2264 C  CG2  B ILE   A 1 106 ? 19.717 -10.479 -12.489 0.36 24.40 ?  106 ILE   A CG2  1 
ATOM   2265 C  CD1  A ILE   A 1 106 ? 19.119 -8.023  -9.391  0.64 24.12 ?  106 ILE   A CD1  1 
ATOM   2266 C  CD1  B ILE   A 1 106 ? 19.276 -7.919  -9.633  0.36 25.12 ?  106 ILE   A CD1  1 
ATOM   2267 H  H    A ILE   A 1 106 ? 21.671 -8.578  -13.134 0.64 27.84 ?  106 ILE   A H    1 
ATOM   2268 H  H    B ILE   A 1 106 ? 21.901 -8.803  -13.242 0.36 26.84 ?  106 ILE   A H    1 
ATOM   2269 H  HA   A ILE   A 1 106 ? 21.465 -8.333  -10.558 0.64 26.86 ?  106 ILE   A HA   1 
ATOM   2270 H  HA   B ILE   A 1 106 ? 21.605 -8.436  -10.678 0.36 27.62 ?  106 ILE   A HA   1 
ATOM   2271 H  HB   A ILE   A 1 106 ? 19.598 -8.315  -12.046 0.64 28.23 ?  106 ILE   A HB   1 
ATOM   2272 H  HB   B ILE   A 1 106 ? 19.785 -8.448  -12.258 0.36 28.97 ?  106 ILE   A HB   1 
ATOM   2273 H  HG12 A ILE   A 1 106 ? 18.086 -9.328  -10.549 0.64 28.66 ?  106 ILE   A HG12 1 
ATOM   2274 H  HG12 B ILE   A 1 106 ? 18.204 -9.260  -10.712 0.36 29.68 ?  106 ILE   A HG12 1 
ATOM   2275 H  HG13 A ILE   A 1 106 ? 19.307 -10.003 -9.794  0.64 28.66 ?  106 ILE   A HG13 1 
ATOM   2276 H  HG13 B ILE   A 1 106 ? 19.376 -9.931  -9.880  0.36 29.68 ?  106 ILE   A HG13 1 
ATOM   2277 H  HG21 A ILE   A 1 106 ? 18.692 -10.246 -12.821 0.64 28.80 ?  106 ILE   A HG21 1 
ATOM   2278 H  HG21 B ILE   A 1 106 ? 18.854 -10.387 -12.921 0.36 29.28 ?  106 ILE   A HG21 1 
ATOM   2279 H  HG22 A ILE   A 1 106 ? 20.234 -10.310 -13.196 0.64 28.80 ?  106 ILE   A HG22 1 
ATOM   2280 H  HG22 B ILE   A 1 106 ? 20.411 -10.601 -13.152 0.36 29.28 ?  106 ILE   A HG22 1 
ATOM   2281 H  HG23 A ILE   A 1 106 ? 19.685 -11.127 -11.949 0.64 28.80 ?  106 ILE   A HG23 1 
ATOM   2282 H  HG23 B ILE   A 1 106 ? 19.704 -11.231 -11.877 0.36 29.28 ?  106 ILE   A HG23 1 
ATOM   2283 H  HD11 A ILE   A 1 106 ? 18.393 -8.048  -8.751  0.64 28.94 ?  106 ILE   A HD11 1 
ATOM   2284 H  HD11 B ILE   A 1 106 ? 18.514 -7.841  -9.041  0.36 30.14 ?  106 ILE   A HD11 1 
ATOM   2285 H  HD12 A ILE   A 1 106 ? 19.971 -8.046  -8.926  0.64 28.94 ?  106 ILE   A HD12 1 
ATOM   2286 H  HD12 B ILE   A 1 106 ? 20.094 -7.967  -9.114  0.36 30.14 ?  106 ILE   A HD12 1 
ATOM   2287 H  HD13 A ILE   A 1 106 ? 19.058 -7.217  -9.929  0.64 28.94 ?  106 ILE   A HD13 1 
ATOM   2288 H  HD13 B ILE   A 1 106 ? 19.307 -7.159  -10.235 0.36 30.14 ?  106 ILE   A HD13 1 
ATOM   2289 N  N    A GLN   A 1 107 ? 22.627 -11.109 -11.421 0.64 22.35 ?  107 GLN   A N    1 
ATOM   2290 N  N    B GLN   A 1 107 ? 22.683 -11.286 -11.423 0.36 23.12 ?  107 GLN   A N    1 
ATOM   2291 C  CA   A GLN   A 1 107 ? 23.234 -12.329 -10.893 0.64 24.57 ?  107 GLN   A CA   1 
ATOM   2292 C  CA   B GLN   A 1 107 ? 23.299 -12.459 -10.816 0.36 23.98 ?  107 GLN   A CA   1 
ATOM   2293 C  C    A GLN   A 1 107 ? 24.198 -12.028 -9.751  0.64 22.13 ?  107 GLN   A C    1 
ATOM   2294 C  C    B GLN   A 1 107 ? 24.304 -12.077 -9.740  0.36 21.68 ?  107 GLN   A C    1 
ATOM   2295 O  O    A GLN   A 1 107 ? 24.392 -12.866 -8.863  0.64 23.30 ?  107 GLN   A O    1 
ATOM   2296 O  O    B GLN   A 1 107 ? 24.641 -12.914 -8.896  0.36 22.60 ?  107 GLN   A O    1 
ATOM   2297 C  CB   A GLN   A 1 107 ? 23.943 -13.087 -12.022 0.64 28.82 ?  107 GLN   A CB   1 
ATOM   2298 C  CB   B GLN   A 1 107 ? 23.974 -13.318 -11.889 0.36 26.94 ?  107 GLN   A CB   1 
ATOM   2299 C  CG   A GLN   A 1 107 ? 23.072 -13.316 -13.255 0.64 33.15 ?  107 GLN   A CG   1 
ATOM   2300 C  CG   B GLN   A 1 107 ? 23.017 -13.839 -12.949 0.36 29.84 ?  107 GLN   A CG   1 
ATOM   2301 C  CD   A GLN   A 1 107 ? 21.792 -14.065 -12.936 0.64 36.86 ?  107 GLN   A CD   1 
ATOM   2302 C  CD   B GLN   A 1 107 ? 21.954 -14.754 -12.375 0.36 32.29 ?  107 GLN   A CD   1 
ATOM   2303 O  OE1  A GLN   A 1 107 ? 21.817 -15.120 -12.302 0.64 38.40 ?  107 GLN   A OE1  1 
ATOM   2304 O  OE1  B GLN   A 1 107 ? 22.249 -15.637 -11.567 0.36 33.14 ?  107 GLN   A OE1  1 
ATOM   2305 N  NE2  A GLN   A 1 107 ? 20.662 -13.518 -13.369 0.64 38.05 ?  107 GLN   A NE2  1 
ATOM   2306 N  NE2  B GLN   A 1 107 ? 20.707 -14.543 -12.783 0.36 33.14 ?  107 GLN   A NE2  1 
ATOM   2307 H  H    A GLN   A 1 107 ? 22.773 -10.976 -12.256 0.64 26.82 ?  107 GLN   A H    1 
ATOM   2308 H  H    B GLN   A 1 107 ? 22.808 -11.218 -12.270 0.36 27.75 ?  107 GLN   A H    1 
ATOM   2309 H  HA   A GLN   A 1 107 ? 22.546 -12.907 -10.542 0.64 29.48 ?  107 GLN   A HA   1 
ATOM   2310 H  HA   B GLN   A 1 107 ? 22.611 -12.995 -10.398 0.36 28.78 ?  107 GLN   A HA   1 
ATOM   2311 H  HB2  A GLN   A 1 107 ? 24.723 -12.583 -12.306 0.64 34.58 ?  107 GLN   A HB2  1 
ATOM   2312 H  HB2  B GLN   A 1 107 ? 24.653 -12.791 -12.337 0.36 32.33 ?  107 GLN   A HB2  1 
ATOM   2313 H  HB3  A GLN   A 1 107 ? 24.219 -13.960 -11.697 0.64 34.58 ?  107 GLN   A HB3  1 
ATOM   2314 H  HB3  B GLN   A 1 107 ? 24.385 -14.088 -11.462 0.36 32.33 ?  107 GLN   A HB3  1 
ATOM   2315 H  HG2  A GLN   A 1 107 ? 22.828 -12.460 -13.641 0.64 39.78 ?  107 GLN   A HG2  1 
ATOM   2316 H  HG2  B GLN   A 1 107 ? 22.572 -13.086 -13.370 0.36 35.81 ?  107 GLN   A HG2  1 
ATOM   2317 H  HG3  A GLN   A 1 107 ? 23.572 -13.837 -13.904 0.64 39.78 ?  107 GLN   A HG3  1 
ATOM   2318 H  HG3  B GLN   A 1 107 ? 23.519 -14.339 -13.612 0.36 35.81 ?  107 GLN   A HG3  1 
ATOM   2319 H  HE21 A GLN   A 1 107 ? 20.682 -12.779 -13.808 0.64 45.66 ?  107 GLN   A HE21 1 
ATOM   2320 H  HE21 B GLN   A 1 107 ? 20.539 -13.915 -13.346 0.36 39.77 ?  107 GLN   A HE21 1 
ATOM   2321 H  HE22 A GLN   A 1 107 ? 19.910 -13.905 -13.212 0.64 45.66 ?  107 GLN   A HE22 1 
ATOM   2322 H  HE22 B GLN   A 1 107 ? 20.068 -15.035 -12.484 0.36 39.77 ?  107 GLN   A HE22 1 
ATOM   2323 N  N    . LEU   A 1 108 ? 24.785 -10.830 -9.739  1.00 18.79 ?  108 LEU   A N    1 
ATOM   2324 C  CA   . LEU   A 1 108 ? 25.698 -10.411 -8.686  1.00 15.64 ?  108 LEU   A CA   1 
ATOM   2325 C  C    . LEU   A 1 108 ? 24.997 -10.241 -7.348  1.00 13.73 ?  108 LEU   A C    1 
ATOM   2326 O  O    . LEU   A 1 108 ? 25.678 -10.084 -6.332  1.00 14.06 ?  108 LEU   A O    1 
ATOM   2327 C  CB   . LEU   A 1 108 ? 26.423 -9.117  -9.083  1.00 15.72 ?  108 LEU   A CB   1 
ATOM   2328 C  CG   . LEU   A 1 108 ? 27.426 -9.315  -10.222 1.00 17.25 ?  108 LEU   A CG   1 
ATOM   2329 C  CD1  . LEU   A 1 108 ? 27.887 -7.979  -10.792 1.00 17.95 ?  108 LEU   A CD1  1 
ATOM   2330 C  CD2  . LEU   A 1 108 ? 28.627 -10.130 -9.759  1.00 18.86 ?  108 LEU   A CD2  1 
ATOM   2331 H  H    A LEU   A 1 108 ? 24.659 -10.231 -10.337 0.64 22.55 ?  108 LEU   A H    1 
ATOM   2332 H  H    B LEU   A 1 108 ? 24.612 -10.232 -10.327 0.36 22.55 ?  108 LEU   A H    1 
ATOM   2333 H  HA   . LEU   A 1 108 ? 26.371 -11.095 -8.566  1.00 18.77 ?  108 LEU   A HA   1 
ATOM   2334 H  HB2  . LEU   A 1 108 ? 25.767 -8.463  -9.375  1.00 18.86 ?  108 LEU   A HB2  1 
ATOM   2335 H  HB3  . LEU   A 1 108 ? 26.908 -8.777  -8.315  1.00 18.86 ?  108 LEU   A HB3  1 
ATOM   2336 H  HG   . LEU   A 1 108 ? 26.995 -9.810  -10.937 1.00 20.70 ?  108 LEU   A HG   1 
ATOM   2337 H  HD11 . LEU   A 1 108 ? 28.508 -8.144  -11.523 1.00 21.54 ?  108 LEU   A HD11 1 
ATOM   2338 H  HD12 . LEU   A 1 108 ? 27.117 -7.491  -11.118 1.00 21.54 ?  108 LEU   A HD12 1 
ATOM   2339 H  HD13 . LEU   A 1 108 ? 28.331 -7.473  -10.094 1.00 21.54 ?  108 LEU   A HD13 1 
ATOM   2340 H  HD21 . LEU   A 1 108 ? 29.312 -10.099 -10.443 1.00 22.63 ?  108 LEU   A HD21 1 
ATOM   2341 H  HD22 . LEU   A 1 108 ? 28.965 -9.746  -8.934  1.00 22.63 ?  108 LEU   A HD22 1 
ATOM   2342 H  HD23 . LEU   A 1 108 ? 28.349 -11.046 -9.608  1.00 22.63 ?  108 LEU   A HD23 1 
ATOM   2343 N  N    . LEU   A 1 109 ? 23.661 -10.294 -7.311  1.00 12.93 ?  109 LEU   A N    1 
ATOM   2344 C  CA   . LEU   A 1 109 ? 22.964 -10.167 -6.038  1.00 12.33 ?  109 LEU   A CA   1 
ATOM   2345 C  C    . LEU   A 1 109 ? 23.308 -11.321 -5.099  1.00 11.80 ?  109 LEU   A C    1 
ATOM   2346 O  O    . LEU   A 1 109 ? 23.443 -11.125 -3.886  1.00 12.13 ?  109 LEU   A O    1 
ATOM   2347 C  CB   . LEU   A 1 109 ? 21.459 -10.085 -6.285  1.00 13.25 ?  109 LEU   A CB   1 
ATOM   2348 C  CG   . LEU   A 1 109 ? 20.564 -9.792  -5.081  1.00 13.35 ?  109 LEU   A CG   1 
ATOM   2349 C  CD1  . LEU   A 1 109 ? 21.018 -8.533  -4.364  1.00 13.48 ?  109 LEU   A CD1  1 
ATOM   2350 C  CD2  . LEU   A 1 109 ? 19.112 -9.659  -5.519  1.00 14.40 ?  109 LEU   A CD2  1 
ATOM   2351 H  H    . LEU   A 1 109 ? 23.147 -10.397 -7.992  1.00 15.52 ?  109 LEU   A H    1 
ATOM   2352 H  HA   . LEU   A 1 109 ? 23.243 -9.342  -5.609  1.00 14.80 ?  109 LEU   A HA   1 
ATOM   2353 H  HB2  . LEU   A 1 109 ? 21.299 -9.380  -6.933  1.00 15.89 ?  109 LEU   A HB2  1 
ATOM   2354 H  HB3  . LEU   A 1 109 ? 21.166 -10.930 -6.652  1.00 15.89 ?  109 LEU   A HB3  1 
ATOM   2355 H  HG   . LEU   A 1 109 ? 20.620 -10.526 -4.454  1.00 16.02 ?  109 LEU   A HG   1 
ATOM   2356 H  HD11 . LEU   A 1 109 ? 20.334 -8.259  -3.733  1.00 16.18 ?  109 LEU   A HD11 1 
ATOM   2357 H  HD12 . LEU   A 1 109 ? 21.848 -8.711  -3.899  1.00 16.18 ?  109 LEU   A HD12 1 
ATOM   2358 H  HD13 . LEU   A 1 109 ? 21.154 -7.825  -5.021  1.00 16.18 ?  109 LEU   A HD13 1 
ATOM   2359 H  HD21 . LEU   A 1 109 ? 18.575 -9.371  -4.762  1.00 17.29 ?  109 LEU   A HD21 1 
ATOM   2360 H  HD22 . LEU   A 1 109 ? 19.051 -9.006  -6.233  1.00 17.29 ?  109 LEU   A HD22 1 
ATOM   2361 H  HD23 . LEU   A 1 109 ? 18.796 -10.522 -5.835  1.00 17.29 ?  109 LEU   A HD23 1 
ATOM   2362 N  N    . LYS   A 1 110 ? 23.453 -12.535 -5.633  1.00 11.51 ?  110 LYS   A N    1 
ATOM   2363 C  CA   . LYS   A 1 110 ? 23.824 -13.657 -4.775  1.00 11.92 ?  110 LYS   A CA   1 
ATOM   2364 C  C    . LYS   A 1 110 ? 25.205 -13.434 -4.165  1.00 11.38 ?  110 LYS   A C    1 
ATOM   2365 O  O    . LYS   A 1 110 ? 25.402 -13.633 -2.964  1.00 11.51 ?  110 LYS   A O    1 
ATOM   2366 C  CB   . LYS   A 1 110 ? 23.757 -14.981 -5.543  1.00 12.85 ?  110 LYS   A CB   1 
ATOM   2367 C  CG   . LYS   A 1 110 ? 23.948 -16.196 -4.638  1.00 13.09 ?  110 LYS   A CG   1 
ATOM   2368 C  CD   . LYS   A 1 110 ? 23.726 -17.519 -5.352  1.00 13.26 ?  110 LYS   A CD   1 
ATOM   2369 C  CE   . LYS   A 1 110 ? 23.835 -18.698 -4.394  1.00 14.43 ?  110 LYS   A CE   1 
ATOM   2370 N  NZ   . LYS   A 1 110 ? 22.653 -18.814 -3.497  1.00 14.67 ?  110 LYS   A NZ   1 
ATOM   2371 H  H    . LYS   A 1 110 ? 23.349 -12.731 -6.461  1.00 13.81 ?  110 LYS   A H    1 
ATOM   2372 H  HA   . LYS   A 1 110 ? 23.185 -13.710 -4.041  1.00 14.30 ?  110 LYS   A HA   1 
ATOM   2373 H  HB2  . LYS   A 1 110 ? 22.886 -15.057 -5.965  1.00 15.41 ?  110 LYS   A HB2  1 
ATOM   2374 H  HB3  . LYS   A 1 110 ? 24.455 -14.993 -6.211  1.00 15.41 ?  110 LYS   A HB3  1 
ATOM   2375 H  HG2  . LYS   A 1 110 ? 24.852 -16.189 -4.289  1.00 15.70 ?  110 LYS   A HG2  1 
ATOM   2376 H  HG3  . LYS   A 1 110 ? 23.312 -16.143 -3.904  1.00 15.70 ?  110 LYS   A HG3  1 
ATOM   2377 H  HD2  . LYS   A 1 110 ? 22.842 -17.530 -5.742  1.00 15.91 ?  110 LYS   A HD2  1 
ATOM   2378 H  HD3  . LYS   A 1 110 ? 24.402 -17.625 -6.040  1.00 15.91 ?  110 LYS   A HD3  1 
ATOM   2379 H  HE2  . LYS   A 1 110 ? 23.911 -19.519 -4.906  1.00 17.32 ?  110 LYS   A HE2  1 
ATOM   2380 H  HE3  . LYS   A 1 110 ? 24.627 -18.584 -3.837  1.00 17.32 ?  110 LYS   A HE3  1 
ATOM   2381 H  HZ1  . LYS   A 1 110 ? 22.749 -19.509 -2.954  1.00 17.61 ?  110 LYS   A HZ1  1 
ATOM   2382 H  HZ2  . LYS   A 1 110 ? 22.568 -18.072 -3.011  1.00 17.61 ?  110 LYS   A HZ2  1 
ATOM   2383 H  HZ3  . LYS   A 1 110 ? 21.916 -18.924 -3.985  1.00 17.61 ?  110 LYS   A HZ3  1 
ATOM   2384 N  N    . SER   A 1 111 ? 26.169 -13.001 -4.982  1.00 11.40 ?  111 SER   A N    1 
ATOM   2385 C  CA   . SER   A 1 111 ? 27.500 -12.686 -4.467  1.00 11.35 ?  111 SER   A CA   1 
ATOM   2386 C  C    . SER   A 1 111 ? 27.432 -11.636 -3.361  1.00 11.12 ?  111 SER   A C    1 
ATOM   2387 O  O    . SER   A 1 111 ? 28.131 -11.741 -2.346  1.00 11.77 ?  111 SER   A O    1 
ATOM   2388 C  CB   . SER   A 1 111 ? 28.388 -12.196 -5.610  1.00 12.81 ?  111 SER   A CB   1 
ATOM   2389 O  OG   . SER   A 1 111 ? 28.475 -13.181 -6.629  1.00 14.71 ?  111 SER   A OG   1 
ATOM   2390 H  H    . SER   A 1 111 ? 26.073 -12.888 -5.828  1.00 13.68 ?  111 SER   A H    1 
ATOM   2391 H  HA   . SER   A 1 111 ? 27.898 -13.491 -4.101  1.00 13.62 ?  111 SER   A HA   1 
ATOM   2392 H  HB2  . SER   A 1 111 ? 27.998 -11.393 -5.991  1.00 15.37 ?  111 SER   A HB2  1 
ATOM   2393 H  HB3  . SER   A 1 111 ? 29.272 -12.007 -5.267  1.00 15.37 ?  111 SER   A HB3  1 
ATOM   2394 H  HG   . SER   A 1 111 ? 28.978 -12.902 -7.252  1.00 17.66 ?  111 SER   A HG   1 
ATOM   2395 N  N    . ALA   A 1 112 ? 26.587 -10.616 -3.541  1.00 11.30 ?  112 ALA   A N    1 
ATOM   2396 C  CA   . ALA   A 1 112 ? 26.442 -9.578  -2.523  1.00 11.16 ?  112 ALA   A CA   1 
ATOM   2397 C  C    . ALA   A 1 112 ? 25.960 -10.177 -1.203  1.00 11.33 ?  112 ALA   A C    1 
ATOM   2398 O  O    . ALA   A 1 112 ? 26.505 -9.880  -0.134  1.00 11.40 ?  112 ALA   A O    1 
ATOM   2399 C  CB   . ALA   A 1 112 ? 25.483 -8.490  -3.016  1.00 11.62 ?  112 ALA   A CB   1 
ATOM   2400 H  H    . ALA   A 1 112 ? 26.092 -10.504 -4.234  1.00 13.55 ?  112 ALA   A H    1 
ATOM   2401 H  HA   . ALA   A 1 112 ? 27.308 -9.163  -2.368  1.00 13.39 ?  112 ALA   A HA   1 
ATOM   2402 H  HB1  . ALA   A 1 112 ? 25.417 -7.794  -2.338  1.00 13.94 ?  112 ALA   A HB1  1 
ATOM   2403 H  HB2  . ALA   A 1 112 ? 25.824 -8.113  -3.840  1.00 13.94 ?  112 ALA   A HB2  1 
ATOM   2404 H  HB3  . ALA   A 1 112 ? 24.609 -8.883  -3.167  1.00 13.94 ?  112 ALA   A HB3  1 
ATOM   2405 N  N    . TYR   A 1 113 ? 24.924 -11.020 -1.256  1.00 11.07 ?  113 TYR   A N    1 
ATOM   2406 C  CA   . TYR   A 1 113 ? 24.413 -11.622 -0.028  1.00 10.84 ?  113 TYR   A CA   1 
ATOM   2407 C  C    . TYR   A 1 113 ? 25.418 -12.576 0.619   1.00 10.66 ?  113 TYR   A C    1 
ATOM   2408 O  O    . TYR   A 1 113 ? 25.376 -12.766 1.838   1.00 11.56 ?  113 TYR   A O    1 
ATOM   2409 C  CB   . TYR   A 1 113 ? 23.092 -12.350 -0.292  1.00 11.33 ?  113 TYR   A CB   1 
ATOM   2410 C  CG   . TYR   A 1 113 ? 21.872 -11.455 -0.209  1.00 10.96 ?  113 TYR   A CG   1 
ATOM   2411 C  CD1  . TYR   A 1 113 ? 21.508 -10.859 0.994   1.00 11.20 ?  113 TYR   A CD1  1 
ATOM   2412 C  CD2  . TYR   A 1 113 ? 21.065 -11.231 -1.322  1.00 11.10 ?  113 TYR   A CD2  1 
ATOM   2413 C  CE1  . TYR   A 1 113 ? 20.382 -10.058 1.086   1.00 11.45 ?  113 TYR   A CE1  1 
ATOM   2414 C  CE2  . TYR   A 1 113 ? 19.914 -10.432 -1.232  1.00 11.28 ?  113 TYR   A CE2  1 
ATOM   2415 C  CZ   . TYR   A 1 113 ? 19.587 -9.859  -0.023  1.00 11.27 ?  113 TYR   A CZ   1 
ATOM   2416 O  OH   . TYR   A 1 113 ? 18.464 -9.067  0.094   1.00 11.69 ?  113 TYR   A OH   1 
ATOM   2417 H  H    . TYR   A 1 113 ? 24.514 -11.247 -1.976  1.00 13.28 ?  113 TYR   A H    1 
ATOM   2418 H  HA   . TYR   A 1 113 ? 24.240 -10.913 0.609   1.00 13.01 ?  113 TYR   A HA   1 
ATOM   2419 H  HB2  . TYR   A 1 113 ? 23.114 -12.726 -1.184  1.00 13.59 ?  113 TYR   A HB2  1 
ATOM   2420 H  HB3  . TYR   A 1 113 ? 22.987 -13.052 0.364   1.00 13.59 ?  113 TYR   A HB3  1 
ATOM   2421 H  HD1  . TYR   A 1 113 ? 22.035 -11.000 1.748   1.00 13.43 ?  113 TYR   A HD1  1 
ATOM   2422 H  HD2  . TYR   A 1 113 ? 21.280 -11.632 -2.130  1.00 13.33 ?  113 TYR   A HD2  1 
ATOM   2423 H  HE1  . TYR   A 1 113 ? 20.153 -9.670  1.899   1.00 13.74 ?  113 TYR   A HE1  1 
ATOM   2424 H  HE2  . TYR   A 1 113 ? 19.377 -10.288 -1.978  1.00 13.53 ?  113 TYR   A HE2  1 
ATOM   2425 H  HH   . TYR   A 1 113 ? 18.073 -9.024  -0.653  1.00 14.02 ?  113 TYR   A HH   1 
ATOM   2426 N  N    . GLU   A 1 114 ? 26.318 -13.193 -0.160  1.00 10.96 ?  114 GLU   A N    1 
ATOM   2427 C  CA   . GLU   A 1 114 ? 27.311 -14.089 0.443   1.00 11.23 ?  114 GLU   A CA   1 
ATOM   2428 C  C    . GLU   A 1 114 ? 28.152 -13.377 1.498   1.00 11.18 ?  114 GLU   A C    1 
ATOM   2429 O  O    . GLU   A 1 114 ? 28.626 -14.010 2.450   1.00 11.58 ?  114 GLU   A O    1 
ATOM   2430 C  CB   . GLU   A 1 114 ? 28.185 -14.732 -0.641  1.00 11.17 ?  114 GLU   A CB   1 
ATOM   2431 C  CG   . GLU   A 1 114 ? 27.421 -15.788 -1.420  1.00 11.71 ?  114 GLU   A CG   1 
ATOM   2432 C  CD   . GLU   A 1 114 ? 28.130 -16.320 -2.658  1.00 12.33 ?  114 GLU   A CD   1 
ATOM   2433 O  OE1  . GLU   A 1 114 ? 29.085 -15.685 -3.155  1.00 12.51 ?  114 GLU   A OE1  1 
ATOM   2434 O  OE2  . GLU   A 1 114 ? 27.693 -17.385 -3.149  1.00 13.44 -1 114 GLU   A OE2  1 
ATOM   2435 H  H    . GLU   A 1 114 ? 26.374 -13.105 -1.021  1.00 13.15 ?  114 GLU   A H    1 
ATOM   2436 H  HA   . GLU   A 1 114 ? 26.835 -14.801 0.886   1.00 13.48 ?  114 GLU   A HA   1 
ATOM   2437 H  HB2  . GLU   A 1 114 ? 28.477 -14.053 -1.268  1.00 13.41 ?  114 GLU   A HB2  1 
ATOM   2438 H  HB3  . GLU   A 1 114 ? 28.944 -15.161 -0.226  1.00 13.41 ?  114 GLU   A HB3  1 
ATOM   2439 H  HG2  . GLU   A 1 114 ? 27.257 -16.543 -0.837  1.00 14.05 ?  114 GLU   A HG2  1 
ATOM   2440 H  HG3  . GLU   A 1 114 ? 26.574 -15.408 -1.707  1.00 14.05 ?  114 GLU   A HG3  1 
ATOM   2441 N  N    . ASN   A 1 115 ? 28.336 -12.060 1.365   1.00 10.98 ?  115 ASN   A N    1 
ATOM   2442 C  CA   . ASN   A 1 115 ? 29.099 -11.328 2.371   1.00 11.28 ?  115 ASN   A CA   1 
ATOM   2443 C  C    . ASN   A 1 115 ? 28.480 -11.460 3.757   1.00 10.84 ?  115 ASN   A C    1 
ATOM   2444 O  O    . ASN   A 1 115 ? 29.191 -11.393 4.766   1.00 11.49 ?  115 ASN   A O    1 
ATOM   2445 C  CB   . ASN   A 1 115 ? 29.202 -9.853  1.989   1.00 11.30 ?  115 ASN   A CB   1 
ATOM   2446 C  CG   . ASN   A 1 115 ? 30.009 -9.636  0.735   1.00 11.69 ?  115 ASN   A CG   1 
ATOM   2447 O  OD1  . ASN   A 1 115 ? 31.230 -9.749  0.756   1.00 15.09 ?  115 ASN   A OD1  1 
ATOM   2448 N  ND2  . ASN   A 1 115 ? 29.345 -9.332  -0.363  1.00 11.81 ?  115 ASN   A ND2  1 
ATOM   2449 H  H    . ASN   A 1 115 ? 28.028 -11.574 0.724   1.00 13.17 ?  115 ASN   A H    1 
ATOM   2450 H  HA   . ASN   A 1 115 ? 29.993 -11.691 2.414   1.00 13.53 ?  115 ASN   A HA   1 
ATOM   2451 H  HB2  . ASN   A 1 115 ? 28.306 -9.502  1.848   1.00 13.57 ?  115 ASN   A HB2  1 
ATOM   2452 H  HB3  . ASN   A 1 115 ? 29.632 -9.371  2.716   1.00 13.57 ?  115 ASN   A HB3  1 
ATOM   2453 H  HD21 . ASN   A 1 115 ? 29.770 -9.203  -1.098  1.00 14.17 ?  115 ASN   A HD21 1 
ATOM   2454 H  HD22 . ASN   A 1 115 ? 28.487 -9.277  -0.346  1.00 14.17 ?  115 ASN   A HD22 1 
ATOM   2455 N  N    . PHE   A 1 116 ? 27.155 -11.632 3.833   1.00 10.90 ?  116 PHE   A N    1 
ATOM   2456 C  CA   . PHE   A 1 116 ? 26.498 -11.728 5.133   1.00 10.99 ?  116 PHE   A CA   1 
ATOM   2457 C  C    . PHE   A 1 116 ? 26.971 -12.961 5.907   1.00 11.31 ?  116 PHE   A C    1 
ATOM   2458 O  O    . PHE   A 1 116 ? 26.904 -12.978 7.137   1.00 12.03 ?  116 PHE   A O    1 
ATOM   2459 C  CB   . PHE   A 1 116 ? 24.970 -11.857 4.988   1.00 11.23 ?  116 PHE   A CB   1 
ATOM   2460 C  CG   . PHE   A 1 116 ? 24.215 -10.606 4.531   1.00 10.60 ?  116 PHE   A CG   1 
ATOM   2461 C  CD1  . PHE   A 1 116 ? 24.796 -9.577  3.802   1.00 10.69 ?  116 PHE   A CD1  1 
ATOM   2462 C  CD2  . PHE   A 1 116 ? 22.859 -10.505 4.837   1.00 11.30 ?  116 PHE   A CD2  1 
ATOM   2463 C  CE1  . PHE   A 1 116 ? 24.028 -8.493  3.386   1.00 11.05 ?  116 PHE   A CE1  1 
ATOM   2464 C  CE2  . PHE   A 1 116 ? 22.098 -9.424  4.435   1.00 11.59 ?  116 PHE   A CE2  1 
ATOM   2465 C  CZ   . PHE   A 1 116 ? 22.677 -8.417  3.712   1.00 10.97 ?  116 PHE   A CZ   1 
ATOM   2466 H  H    . PHE   A 1 116 ? 26.618 -11.686 3.158   1.00 13.08 ?  116 PHE   A H    1 
ATOM   2467 H  HA   . PHE   A 1 116 ? 26.690 -10.938 5.661   1.00 13.19 ?  116 PHE   A HA   1 
ATOM   2468 H  HB2  . PHE   A 1 116 ? 24.787 -12.560 4.343   1.00 13.47 ?  116 PHE   A HB2  1 
ATOM   2469 H  HB3  . PHE   A 1 116 ? 24.605 -12.119 5.851   1.00 13.47 ?  116 PHE   A HB3  1 
ATOM   2470 H  HD1  . PHE   A 1 116 ? 25.693 -9.631  3.573   1.00 12.83 ?  116 PHE   A HD1  1 
ATOM   2471 H  HD2  . PHE   A 1 116 ? 22.453 -11.196 5.323   1.00 13.56 ?  116 PHE   A HD2  1 
ATOM   2472 H  HE1  . PHE   A 1 116 ? 24.424 -7.806  2.904   1.00 13.26 ?  116 PHE   A HE1  1 
ATOM   2473 H  HE2  . PHE   A 1 116 ? 21.194 -9.386  4.659   1.00 13.91 ?  116 PHE   A HE2  1 
ATOM   2474 H  HZ   . PHE   A 1 116 ? 22.171 -7.683  3.448   1.00 13.16 ?  116 PHE   A HZ   1 
ATOM   2475 N  N    . ASN   A 1 117 ? 27.417 -14.014 5.208   1.00 11.49 ?  117 ASN   A N    1 
ATOM   2476 C  CA   . ASN   A 1 117 ? 27.786 -15.258 5.879   1.00 11.85 ?  117 ASN   A CA   1 
ATOM   2477 C  C    . ASN   A 1 117 ? 29.046 -15.136 6.720   1.00 12.49 ?  117 ASN   A C    1 
ATOM   2478 O  O    . ASN   A 1 117 ? 29.338 -16.052 7.497   1.00 12.95 ?  117 ASN   A O    1 
ATOM   2479 C  CB   . ASN   A 1 117 ? 27.908 -16.389 4.862   1.00 11.95 ?  117 ASN   A CB   1 
ATOM   2480 C  CG   . ASN   A 1 117 ? 26.556 -16.776 4.314   1.00 11.94 ?  117 ASN   A CG   1 
ATOM   2481 O  OD1  . ASN   A 1 117 ? 25.573 -16.789 5.053   1.00 12.86 ?  117 ASN   A OD1  1 
ATOM   2482 N  ND2  . ASN   A 1 117 ? 26.480 -17.034 3.024   1.00 11.69 ?  117 ASN   A ND2  1 
ATOM   2483 H  H    . ASN   A 1 117 ? 27.494 -14.034 4.348   1.00 13.79 ?  117 ASN   A H    1 
ATOM   2484 H  HA   . ASN   A 1 117 ? 27.062 -15.493 6.480   1.00 14.22 ?  117 ASN   A HA   1 
ATOM   2485 H  HB2  . ASN   A 1 117 ? 28.466 -16.098 4.123   1.00 14.34 ?  117 ASN   A HB2  1 
ATOM   2486 H  HB3  . ASN   A 1 117 ? 28.293 -17.164 5.294   1.00 14.34 ?  117 ASN   A HB3  1 
ATOM   2487 H  HD21 . ASN   A 1 117 ? 25.727 -17.245 2.677   1.00 14.03 ?  117 ASN   A HD21 1 
ATOM   2488 H  HD22 . ASN   A 1 117 ? 27.190 -17.000 2.540   1.00 14.03 ?  117 ASN   A HD22 1 
ATOM   2489 N  N    . GLN   A 1 118 ? 29.773 -14.023 6.610   1.00 12.40 ?  118 GLN   A N    1 
ATOM   2490 C  CA   . GLN   A 1 118 ? 30.947 -13.782 7.438   1.00 12.92 ?  118 GLN   A CA   1 
ATOM   2491 C  C    . GLN   A 1 118 ? 30.599 -13.202 8.805   1.00 13.18 ?  118 GLN   A C    1 
ATOM   2492 O  O    . GLN   A 1 118 ? 31.510 -12.912 9.590   1.00 14.29 ?  118 GLN   A O    1 
ATOM   2493 C  CB   . GLN   A 1 118 ? 31.946 -12.880 6.702   1.00 12.88 ?  118 GLN   A CB   1 
ATOM   2494 C  CG   . GLN   A 1 118 ? 32.419 -13.464 5.382   1.00 12.84 ?  118 GLN   A CG   1 
ATOM   2495 C  CD   . GLN   A 1 118 ? 33.258 -14.721 5.559   1.00 13.62 ?  118 GLN   A CD   1 
ATOM   2496 O  OE1  . GLN   A 1 118 ? 34.119 -14.790 6.446   1.00 14.30 ?  118 GLN   A OE1  1 
ATOM   2497 N  NE2  . GLN   A 1 118 ? 33.013 -15.724 4.710   1.00 13.62 ?  118 GLN   A NE2  1 
ATOM   2498 H  H    . GLN   A 1 118 ? 29.594 -13.380 6.061   1.00 14.88 ?  118 GLN   A H    1 
ATOM   2499 H  HA   . GLN   A 1 118 ? 31.380 -14.636 7.591   1.00 15.51 ?  118 GLN   A HA   1 
ATOM   2500 H  HB2  . GLN   A 1 118 ? 31.524 -12.027 6.521   1.00 15.46 ?  118 GLN   A HB2  1 
ATOM   2501 H  HB3  . GLN   A 1 118 ? 32.723 -12.753 7.268   1.00 15.46 ?  118 GLN   A HB3  1 
ATOM   2502 H  HG2  . GLN   A 1 118 ? 31.646 -13.685 4.836   1.00 15.41 ?  118 GLN   A HG2  1 
ATOM   2503 H  HG3  . GLN   A 1 118 ? 32.966 -12.805 4.925   1.00 15.41 ?  118 GLN   A HG3  1 
ATOM   2504 H  HE21 . GLN   A 1 118 ? 32.397 -15.637 4.103   1.00 16.34 ?  118 GLN   A HE21 1 
ATOM   2505 H  HE22 . GLN   A 1 118 ? 33.449 -16.459 4.764   1.00 16.34 ?  118 GLN   A HE22 1 
ATOM   2506 N  N    . HIS   A 1 119 ? 29.311 -13.049 9.113   1.00 12.63 ?  119 HIS   A N    1 
ATOM   2507 C  CA   . HIS   A 1 119 ? 28.860 -12.442 10.360  1.00 12.67 ?  119 HIS   A CA   1 
ATOM   2508 C  C    . HIS   A 1 119 ? 27.716 -13.258 10.936  1.00 13.49 ?  119 HIS   A C    1 
ATOM   2509 O  O    . HIS   A 1 119 ? 26.773 -13.600 10.218  1.00 13.93 ?  119 HIS   A O    1 
ATOM   2510 C  CB   . HIS   A 1 119 ? 28.406 -11.012 10.083  1.00 13.32 ?  119 HIS   A CB   1 
ATOM   2511 C  CG   . HIS   A 1 119 ? 29.487 -10.200 9.472   1.00 14.41 ?  119 HIS   A CG   1 
ATOM   2512 N  ND1  . HIS   A 1 119 ? 30.450 -9.575  10.230  1.00 16.60 ?  119 HIS   A ND1  1 
ATOM   2513 C  CD2  . HIS   A 1 119 ? 29.829 -10.005 8.179   1.00 15.27 ?  119 HIS   A CD2  1 
ATOM   2514 C  CE1  . HIS   A 1 119 ? 31.319 -8.992  9.425   1.00 16.62 ?  119 HIS   A CE1  1 
ATOM   2515 N  NE2  . HIS   A 1 119 ? 30.973 -9.246  8.176   1.00 16.63 ?  119 HIS   A NE2  1 
ATOM   2516 H  H    . HIS   A 1 119 ? 28.659 -13.303 8.604   1.00 15.15 ?  119 HIS   A H    1 
ATOM   2517 H  HA   . HIS   A 1 119 ? 29.588 -12.431 11.000  1.00 15.20 ?  119 HIS   A HA   1 
ATOM   2518 H  HB2  . HIS   A 1 119 ? 27.652 -11.035 9.472   1.00 15.99 ?  119 HIS   A HB2  1 
ATOM   2519 H  HB3  . HIS   A 1 119 ? 28.147 -10.600 10.921  1.00 15.99 ?  119 HIS   A HB3  1 
ATOM   2520 H  HD2  . HIS   A 1 119 ? 29.375 -10.326 7.430   1.00 18.33 ?  119 HIS   A HD2  1 
ATOM   2521 H  HE1  . HIS   A 1 119 ? 32.053 -8.486  9.689   1.00 19.95 ?  119 HIS   A HE1  1 
ATOM   2522 H  HE2  . HIS   A 1 119 ? 31.378 -8.956  7.473   1.00 19.95 ?  119 HIS   A HE2  1 
ATOM   2523 N  N    . GLU   A 1 120 ? 27.789 -13.552 12.237  1.00 14.42 ?  120 GLU   A N    1 
ATOM   2524 C  CA   . GLU   A 1 120 ? 26.832 -14.479 12.842  1.00 16.81 ?  120 GLU   A CA   1 
ATOM   2525 C  C    . GLU   A 1 120 ? 25.415 -13.914 12.895  1.00 14.71 ?  120 GLU   A C    1 
ATOM   2526 O  O    . GLU   A 1 120 ? 24.441 -14.675 12.773  1.00 15.14 ?  120 GLU   A O    1 
ATOM   2527 C  CB   . GLU   A 1 120 ? 27.302 -14.869 14.245  1.00 22.31 ?  120 GLU   A CB   1 
ATOM   2528 C  CG   . GLU   A 1 120 ? 28.503 -15.801 14.265  1.00 30.25 ?  120 GLU   A CG   1 
ATOM   2529 C  CD   . GLU   A 1 120 ? 28.665 -16.514 15.592  1.00 37.32 ?  120 GLU   A CD   1 
ATOM   2530 O  OE1  . GLU   A 1 120 ? 28.261 -15.943 16.628  1.00 39.64 ?  120 GLU   A OE1  1 
ATOM   2531 O  OE2  . GLU   A 1 120 ? 29.192 -17.647 15.600  1.00 42.66 -1 120 GLU   A OE2  1 
ATOM   2532 H  H    . GLU   A 1 120 ? 28.380 -13.236 12.782  1.00 17.30 ?  120 GLU   A H    1 
ATOM   2533 H  HA   . GLU   A 1 120 ? 26.812 -15.290 12.313  1.00 20.17 ?  120 GLU   A HA   1 
ATOM   2534 H  HB2  . GLU   A 1 120 ? 27.550 -14.069 14.735  1.00 26.77 ?  120 GLU   A HB2  1 
ATOM   2535 H  HB3  . GLU   A 1 120 ? 26.577 -15.323 14.707  1.00 26.77 ?  120 GLU   A HB3  1 
ATOM   2536 H  HG2  . GLU   A 1 120 ? 28.401 -16.468 13.568  1.00 36.30 ?  120 GLU   A HG2  1 
ATOM   2537 H  HG3  . GLU   A 1 120 ? 29.310 -15.286 14.120  1.00 36.30 ?  120 GLU   A HG3  1 
ATOM   2538 N  N    A VAL   A 1 121 ? 25.280 -12.603 13.099  0.64 13.99 ?  121 VAL   A N    1 
ATOM   2539 N  N    B VAL   A 1 121 ? 25.277 -12.605 13.110  0.36 14.33 ?  121 VAL   A N    1 
ATOM   2540 C  CA   A VAL   A 1 121 ? 23.984 -11.938 13.216  0.64 14.15 ?  121 VAL   A CA   1 
ATOM   2541 C  CA   B VAL   A 1 121 ? 23.978 -11.944 13.211  0.36 14.34 ?  121 VAL   A CA   1 
ATOM   2542 C  C    A VAL   A 1 121 ? 24.093 -10.565 12.565  0.64 12.97 ?  121 VAL   A C    1 
ATOM   2543 C  C    B VAL   A 1 121 ? 24.091 -10.567 12.568  0.36 13.20 ?  121 VAL   A C    1 
ATOM   2544 O  O    A VAL   A 1 121 ? 25.061 -9.836  12.806  0.64 13.34 ?  121 VAL   A O    1 
ATOM   2545 O  O    B VAL   A 1 121 ? 25.063 -9.843  12.805  0.36 13.42 ?  121 VAL   A O    1 
ATOM   2546 C  CB   A VAL   A 1 121 ? 23.552 -11.774 14.693  0.64 16.81 ?  121 VAL   A CB   1 
ATOM   2547 C  CB   B VAL   A 1 121 ? 23.511 -11.804 14.680  0.36 16.27 ?  121 VAL   A CB   1 
ATOM   2548 C  CG1  A VAL   A 1 121 ? 22.173 -11.131 14.780  0.64 17.27 ?  121 VAL   A CG1  1 
ATOM   2549 C  CG1  B VAL   A 1 121 ? 22.129 -11.168 14.743  0.36 16.62 ?  121 VAL   A CG1  1 
ATOM   2550 C  CG2  A VAL   A 1 121 ? 23.560 -13.099 15.435  0.64 18.62 ?  121 VAL   A CG2  1 
ATOM   2551 C  CG2  B VAL   A 1 121 ? 23.503 -13.144 15.400  0.36 17.58 ?  121 VAL   A CG2  1 
ATOM   2552 H  H    A VAL   A 1 121 ? 25.947 -12.066 13.184  0.64 16.79 ?  121 VAL   A H    1 
ATOM   2553 H  H    B VAL   A 1 121 ? 25.942 -12.066 13.205  0.36 17.19 ?  121 VAL   A H    1 
ATOM   2554 H  HA   A VAL   A 1 121 ? 23.311 -12.460 12.754  0.64 16.99 ?  121 VAL   A HA   1 
ATOM   2555 H  HA   B VAL   A 1 121 ? 23.316 -12.461 12.730  0.36 17.20 ?  121 VAL   A HA   1 
ATOM   2556 H  HB   A VAL   A 1 121 ? 24.178 -11.185 15.140  0.64 20.17 ?  121 VAL   A HB   1 
ATOM   2557 H  HB   B VAL   A 1 121 ? 24.125 -11.221 15.151  0.36 19.52 ?  121 VAL   A HB   1 
ATOM   2558 H  HG11 A VAL   A 1 121 ? 21.856 -11.181 15.697  0.64 20.72 ?  121 VAL   A HG11 1 
ATOM   2559 H  HG11 B VAL   A 1 121 ? 21.791 -11.237 15.651  0.36 19.94 ?  121 VAL   A HG11 1 
ATOM   2560 H  HG12 A VAL   A 1 121 ? 22.234 -10.203 14.505  0.64 20.72 ?  121 VAL   A HG12 1 
ATOM   2561 H  HG12 B VAL   A 1 121 ? 22.196 -10.235 14.487  0.36 19.94 ?  121 VAL   A HG12 1 
ATOM   2562 H  HG13 A VAL   A 1 121 ? 21.562 -11.610 14.197  0.64 20.72 ?  121 VAL   A HG13 1 
ATOM   2563 H  HG13 B VAL   A 1 121 ? 21.536 -11.638 14.136  0.36 19.94 ?  121 VAL   A HG13 1 
ATOM   2564 H  HG21 A VAL   A 1 121 ? 23.217 -12.960 16.337  0.64 22.34 ?  121 VAL   A HG21 1 
ATOM   2565 H  HG21 B VAL   A 1 121 ? 23.143 -13.020 16.297  0.36 21.10 ?  121 VAL   A HG21 1 
ATOM   2566 H  HG22 A VAL   A 1 121 ? 22.990 -13.730 14.966  0.64 22.34 ?  121 VAL   A HG22 1 
ATOM   2567 H  HG22 B VAL   A 1 121 ? 22.945 -13.767 14.909  0.36 21.10 ?  121 VAL   A HG22 1 
ATOM   2568 H  HG23 A VAL   A 1 121 ? 24.465 -13.436 15.477  0.64 22.34 ?  121 VAL   A HG23 1 
ATOM   2569 H  HG23 B VAL   A 1 121 ? 24.409 -13.481 15.456  0.36 21.10 ?  121 VAL   A HG23 1 
ATOM   2570 N  N    . LEU   A 1 122 ? 23.090 -10.195 11.768  1.00 12.32 ?  122 LEU   A N    1 
ATOM   2571 C  CA   . LEU   A 1 122 ? 23.091 -8.900  11.090  1.00 11.95 ?  122 LEU   A CA   1 
ATOM   2572 C  C    . LEU   A 1 122 ? 21.693 -8.304  11.054  1.00 11.86 ?  122 LEU   A C    1 
ATOM   2573 O  O    . LEU   A 1 122 ? 20.703 -9.023  10.913  1.00 12.82 ?  122 LEU   A O    1 
ATOM   2574 C  CB   . LEU   A 1 122 ? 23.532 -8.996  9.624   1.00 13.33 ?  122 LEU   A CB   1 
ATOM   2575 C  CG   . LEU   A 1 122 ? 24.748 -9.841  9.275   1.00 13.33 ?  122 LEU   A CG   1 
ATOM   2576 C  CD1  . LEU   A 1 122 ? 24.349 -11.287 9.060   1.00 13.97 ?  122 LEU   A CD1  1 
ATOM   2577 C  CD2  . LEU   A 1 122 ? 25.438 -9.281  8.039   1.00 12.93 ?  122 LEU   A CD2  1 
ATOM   2578 H  H    A LEU   A 1 122 ? 22.393 -10.675 11.606  0.64 14.79 ?  122 LEU   A H    1 
ATOM   2579 H  H    B LEU   A 1 122 ? 22.396 -10.678 11.600  0.36 14.79 ?  122 LEU   A H    1 
ATOM   2580 H  HA   . LEU   A 1 122 ? 23.678 -8.282  11.554  1.00 14.34 ?  122 LEU   A HA   1 
ATOM   2581 H  HB2  . LEU   A 1 122 ? 22.798 -9.358  9.114   1.00 16.00 ?  122 LEU   A HB2  1 
ATOM   2582 H  HB3  . LEU   A 1 122 ? 23.730 -8.101  9.313   1.00 16.00 ?  122 LEU   A HB3  1 
ATOM   2583 H  HG   . LEU   A 1 122 ? 25.392 -9.816  10.004  1.00 16.00 ?  122 LEU   A HG   1 
ATOM   2584 H  HD11 . LEU   A 1 122 ? 25.127 -11.803 8.791   1.00 16.77 ?  122 LEU   A HD11 1 
ATOM   2585 H  HD12 . LEU   A 1 122 ? 23.990 -11.644 9.888   1.00 16.77 ?  122 LEU   A HD12 1 
ATOM   2586 H  HD13 . LEU   A 1 122 ? 23.673 -11.329 8.364   1.00 16.77 ?  122 LEU   A HD13 1 
ATOM   2587 H  HD21 . LEU   A 1 122 ? 26.193 -9.855  7.802   1.00 15.52 ?  122 LEU   A HD21 1 
ATOM   2588 H  HD22 . LEU   A 1 122 ? 24.806 -9.260  7.304   1.00 15.52 ?  122 LEU   A HD22 1 
ATOM   2589 H  HD23 . LEU   A 1 122 ? 25.759 -8.387  8.229   1.00 15.52 ?  122 LEU   A HD23 1 
ATOM   2590 N  N    . LEU   A 1 123 ? 21.630 -6.973  11.151  1.00 11.40 ?  123 LEU   A N    1 
ATOM   2591 C  CA   . LEU   A 1 123 ? 20.461 -6.178  10.780  1.00 11.44 ?  123 LEU   A CA   1 
ATOM   2592 C  C    . LEU   A 1 123 ? 20.706 -5.648  9.375   1.00 10.97 ?  123 LEU   A C    1 
ATOM   2593 O  O    . LEU   A 1 123 ? 21.754 -5.047  9.129   1.00 11.40 ?  123 LEU   A O    1 
ATOM   2594 C  CB   . LEU   A 1 123 ? 20.321 -4.997  11.744  1.00 12.02 ?  123 LEU   A CB   1 
ATOM   2595 C  CG   . LEU   A 1 123 ? 19.273 -3.933  11.399  1.00 12.51 ?  123 LEU   A CG   1 
ATOM   2596 C  CD1  . LEU   A 1 123 ? 17.877 -4.530  11.375  1.00 13.37 ?  123 LEU   A CD1  1 
ATOM   2597 C  CD2  . LEU   A 1 123 ? 19.351 -2.767  12.386  1.00 13.15 ?  123 LEU   A CD2  1 
ATOM   2598 H  H    . LEU   A 1 123 ? 22.284 -6.491  11.436  1.00 13.68 ?  123 LEU   A H    1 
ATOM   2599 H  HA   . LEU   A 1 123 ? 19.656 -6.718  10.797  1.00 13.73 ?  123 LEU   A HA   1 
ATOM   2600 H  HB2  . LEU   A 1 123 ? 20.085 -5.346  12.621  1.00 14.42 ?  123 LEU   A HB2  1 
ATOM   2601 H  HB3  . LEU   A 1 123 ? 21.174 -4.545  11.802  1.00 14.42 ?  123 LEU   A HB3  1 
ATOM   2602 H  HG   . LEU   A 1 123 ? 19.458 -3.577  10.513  1.00 15.02 ?  123 LEU   A HG   1 
ATOM   2603 H  HD11 . LEU   A 1 123 ? 17.233 -3.831  11.190  1.00 16.05 ?  123 LEU   A HD11 1 
ATOM   2604 H  HD12 . LEU   A 1 123 ? 17.835 -5.210  10.682  1.00 16.05 ?  123 LEU   A HD12 1 
ATOM   2605 H  HD13 . LEU   A 1 123 ? 17.692 -4.932  12.240  1.00 16.05 ?  123 LEU   A HD13 1 
ATOM   2606 H  HD21 . LEU   A 1 123 ? 18.681 -2.108  12.153  1.00 15.79 ?  123 LEU   A HD21 1 
ATOM   2607 H  HD22 . LEU   A 1 123 ? 19.179 -3.109  13.282  1.00 15.79 ?  123 LEU   A HD22 1 
ATOM   2608 H  HD23 . LEU   A 1 123 ? 20.235 -2.379  12.347  1.00 15.79 ?  123 LEU   A HD23 1 
ATOM   2609 N  N    . ALA   A 1 124 ? 19.756 -5.844  8.460   1.00 10.58 ?  124 ALA   A N    1 
ATOM   2610 C  CA   . ALA   A 1 124 ? 20.037 -5.562  7.062   1.00 10.65 ?  124 ALA   A CA   1 
ATOM   2611 C  C    . ALA   A 1 124 ? 18.807 -5.108  6.292   1.00 10.50 ?  124 ALA   A C    1 
ATOM   2612 O  O    . ALA   A 1 124 ? 17.671 -5.456  6.653   1.00 11.11 ?  124 ALA   A O    1 
ATOM   2613 C  CB   . ALA   A 1 124 ? 20.616 -6.798  6.362   1.00 11.04 ?  124 ALA   A CB   1 
ATOM   2614 H  H    . ALA   A 1 124 ? 18.957 -6.132  8.624   1.00 12.70 ?  124 ALA   A H    1 
ATOM   2615 H  HA   . ALA   A 1 124 ? 20.711 -4.868  7.035   1.00 12.78 ?  124 ALA   A HA   1 
ATOM   2616 H  HB1  . ALA   A 1 124 ? 20.805 -6.583  5.434   1.00 13.25 ?  124 ALA   A HB1  1 
ATOM   2617 H  HB2  . ALA   A 1 124 ? 21.446 -7.060  6.808   1.00 13.25 ?  124 ALA   A HB2  1 
ATOM   2618 H  HB3  . ALA   A 1 124 ? 19.979 -7.525  6.412   1.00 13.25 ?  124 ALA   A HB3  1 
ATOM   2619 N  N    A PRO   A 1 125 ? 19.005 -4.370  5.204   0.64 9.89  ?  125 PRO   A N    1 
ATOM   2620 N  N    B PRO   A 1 125 ? 19.000 -4.333  5.225   0.36 10.46 ?  125 PRO   A N    1 
ATOM   2621 C  CA   A PRO   A 1 125 ? 17.957 -4.140  4.213   0.64 9.89  ?  125 PRO   A CA   1 
ATOM   2622 C  CA   B PRO   A 1 125 ? 17.895 -4.007  4.324   0.36 10.57 ?  125 PRO   A CA   1 
ATOM   2623 C  C    A PRO   A 1 125 ? 18.011 -5.219  3.138   0.64 9.81  ?  125 PRO   A C    1 
ATOM   2624 C  C    B PRO   A 1 125 ? 17.859 -5.003  3.179   0.36 10.77 ?  125 PRO   A C    1 
ATOM   2625 O  O    A PRO   A 1 125 ? 18.984 -5.969  3.021   0.64 10.15 ?  125 PRO   A O    1 
ATOM   2626 O  O    B PRO   A 1 125 ? 18.753 -5.850  3.074   0.36 11.64 ?  125 PRO   A O    1 
ATOM   2627 C  CB   A PRO   A 1 125 ? 18.398 -2.804  3.606   0.64 10.17 ?  125 PRO   A CB   1 
ATOM   2628 C  CB   B PRO   A 1 125 ? 18.291 -2.621  3.814   0.36 10.75 ?  125 PRO   A CB   1 
ATOM   2629 C  CG   A PRO   A 1 125 ? 19.922 -2.951  3.553   0.64 10.21 ?  125 PRO   A CG   1 
ATOM   2630 C  CG   B PRO   A 1 125 ? 19.804 -2.742  3.685   0.36 11.17 ?  125 PRO   A CG   1 
ATOM   2631 C  CD   A PRO   A 1 125 ? 20.274 -3.719  4.822   0.64 10.35 ?  125 PRO   A CD   1 
ATOM   2632 C  CD   B PRO   A 1 125 ? 20.255 -3.684  4.797   0.36 11.00 ?  125 PRO   A CD   1 
ATOM   2633 H  HA   A PRO   A 1 125 ? 17.076 -4.084  4.612   0.64 11.86 ?  125 PRO   A HA   1 
ATOM   2634 H  HA   B PRO   A 1 125 ? 17.044 -3.974  4.798   0.36 12.68 ?  125 PRO   A HA   1 
ATOM   2635 H  HB2  A PRO   A 1 125 ? 18.019 -2.703  2.718   0.64 12.20 ?  125 PRO   A HB2  1 
ATOM   2636 H  HB2  B PRO   A 1 125 ? 17.875 -2.454  2.952   0.36 12.90 ?  125 PRO   A HB2  1 
ATOM   2637 H  HB3  A PRO   A 1 125 ? 18.133 -2.076  4.187   0.64 12.20 ?  125 PRO   A HB3  1 
ATOM   2638 H  HB3  B PRO   A 1 125 ? 18.044 -1.940  4.460   0.36 12.90 ?  125 PRO   A HB3  1 
ATOM   2639 H  HG2  A PRO   A 1 125 ? 20.177 -3.453  2.760   0.64 12.25 ?  125 PRO   A HG2  1 
ATOM   2640 H  HG2  B PRO   A 1 125 ? 20.025 -3.113  2.817   0.36 13.41 ?  125 PRO   A HG2  1 
ATOM   2641 H  HG3  A PRO   A 1 125 ? 20.335 -2.071  3.548   0.64 12.25 ?  125 PRO   A HG3  1 
ATOM   2642 H  HG3  B PRO   A 1 125 ? 20.208 -1.869  3.795   0.36 13.41 ?  125 PRO   A HG3  1 
ATOM   2643 H  HD2  A PRO   A 1 125 ? 20.962 -4.375  4.640   0.64 12.42 ?  125 PRO   A HD2  1 
ATOM   2644 H  HD2  B PRO   A 1 125 ? 20.882 -4.341  4.450   0.36 13.20 ?  125 PRO   A HD2  1 
ATOM   2645 H  HD3  A PRO   A 1 125 ? 20.551 -3.100  5.520   0.64 12.42 ?  125 PRO   A HD3  1 
ATOM   2646 H  HD3  B PRO   A 1 125 ? 20.645 -3.177  5.529   0.36 13.20 ?  125 PRO   A HD3  1 
ATOM   2647 N  N    A LEU   A 1 126 ? 16.957 -5.261  2.329   0.64 10.13 ?  126 LEU   A N    1 
ATOM   2648 N  N    B LEU   A 1 126 ? 16.861 -4.907  2.306   0.36 11.15 ?  126 LEU   A N    1 
ATOM   2649 C  CA   A LEU   A 1 126 ? 16.971 -6.085  1.129   0.64 10.66 ?  126 LEU   A CA   1 
ATOM   2650 C  CA   B LEU   A 1 126 ? 16.816 -5.746  1.112   0.36 11.30 ?  126 LEU   A CA   1 
ATOM   2651 C  C    A LEU   A 1 126 ? 17.900 -5.469  0.088   0.64 10.51 ?  126 LEU   A C    1 
ATOM   2652 C  C    B LEU   A 1 126 ? 17.789 -5.195  0.077   0.36 10.65 ?  126 LEU   A C    1 
ATOM   2653 O  O    A LEU   A 1 126 ? 17.690 -4.338  -0.361  0.64 11.75 ?  126 LEU   A O    1 
ATOM   2654 O  O    B LEU   A 1 126 ? 17.541 -4.143  -0.521  0.36 11.03 ?  126 LEU   A O    1 
ATOM   2655 C  CB   A LEU   A 1 126 ? 15.557 -6.222  0.579   0.64 10.83 ?  126 LEU   A CB   1 
ATOM   2656 C  CB   B LEU   A 1 126 ? 15.405 -5.769  0.538   0.36 12.64 ?  126 LEU   A CB   1 
ATOM   2657 C  CG   A LEU   A 1 126 ? 14.639 -7.149  1.376   0.64 11.16 ?  126 LEU   A CG   1 
ATOM   2658 C  CG   B LEU   A 1 126 ? 14.353 -6.571  1.298   0.36 13.68 ?  126 LEU   A CG   1 
ATOM   2659 C  CD1  A LEU   A 1 126 ? 13.207 -6.991  0.906   0.64 12.67 ?  126 LEU   A CD1  1 
ATOM   2660 C  CD1  B LEU   A 1 126 ? 12.991 -6.386  0.650   0.36 14.01 ?  126 LEU   A CD1  1 
ATOM   2661 C  CD2  A LEU   A 1 126 ? 15.098 -8.600  1.239   0.64 11.23 ?  126 LEU   A CD2  1 
ATOM   2662 C  CD2  B LEU   A 1 126 ? 14.731 -8.040  1.343   0.36 14.04 ?  126 LEU   A CD2  1 
ATOM   2663 H  H    A LEU   A 1 126 ? 16.233 -4.818  2.445   0.64 12.15 ?  126 LEU   A H    1 
ATOM   2664 H  H    B LEU   A 1 126 ? 16.194 -4.365  2.391   0.36 13.38 ?  126 LEU   A H    1 
ATOM   2665 H  HA   A LEU   A 1 126 ? 17.305 -6.967  1.344   0.64 12.79 ?  126 LEU   A HA   1 
ATOM   2666 H  HA   B LEU   A 1 126 ? 17.082 -6.650  1.346   0.36 13.56 ?  126 LEU   A HA   1 
ATOM   2667 H  HB2  A LEU   A 1 126 ? 15.144 -5.344  0.568   0.64 13.00 ?  126 LEU   A HB2  1 
ATOM   2668 H  HB2  B LEU   A 1 126 ? 15.089 -4.854  0.488   0.36 15.17 ?  126 LEU   A HB2  1 
ATOM   2669 H  HB3  A LEU   A 1 126 ? 15.605 -6.569  -0.324  0.64 13.00 ?  126 LEU   A HB3  1 
ATOM   2670 H  HB3  B LEU   A 1 126 ? 15.458 -6.140  -0.355  0.36 15.17 ?  126 LEU   A HB3  1 
ATOM   2671 H  HG   A LEU   A 1 126 ? 14.675 -6.905  2.316   0.64 13.39 ?  126 LEU   A HG   1 
ATOM   2672 H  HG   B LEU   A 1 126 ? 14.299 -6.242  2.209   0.36 16.42 ?  126 LEU   A HG   1 
ATOM   2673 H  HD11 A LEU   A 1 126 ? 12.638 -7.585  1.417   0.64 15.20 ?  126 LEU   A HD11 1 
ATOM   2674 H  HD11 B LEU   A 1 126 ? 12.347 -6.944  1.112   0.36 16.82 ?  126 LEU   A HD11 1 
ATOM   2675 H  HD12 A LEU   A 1 126 ? 12.930 -6.069  1.040   0.64 15.20 ?  126 LEU   A HD12 1 
ATOM   2676 H  HD12 B LEU   A 1 126 ? 12.731 -5.454  0.717   0.36 16.82 ?  126 LEU   A HD12 1 
ATOM   2677 H  HD13 A LEU   A 1 126 ? 13.160 -7.214  -0.037  0.64 15.20 ?  126 LEU   A HD13 1 
ATOM   2678 H  HD13 B LEU   A 1 126 ? 13.047 -6.648  -0.282  0.36 16.82 ?  126 LEU   A HD13 1 
ATOM   2679 H  HD21 A LEU   A 1 126 ? 14.428 -9.182  1.625   0.64 13.47 ?  126 LEU   A HD21 1 
ATOM   2680 H  HD21 B LEU   A 1 126 ? 13.981 -8.546  1.690   0.36 16.85 ?  126 LEU   A HD21 1 
ATOM   2681 H  HD22 A LEU   A 1 126 ? 15.216 -8.804  0.298   0.64 13.47 ?  126 LEU   A HD22 1 
ATOM   2682 H  HD22 B LEU   A 1 126 ? 14.945 -8.336  0.444   0.36 16.85 ?  126 LEU   A HD22 1 
ATOM   2683 H  HD23 A LEU   A 1 126 ? 15.942 -8.710  1.708   0.64 13.47 ?  126 LEU   A HD23 1 
ATOM   2684 H  HD23 B LEU   A 1 126 ? 15.502 -8.149  1.920   0.36 16.85 ?  126 LEU   A HD23 1 
ATOM   2685 N  N    A LEU   A 1 127 ? 18.930 -6.217  -0.298  0.64 10.66 ?  127 LEU   A N    1 
ATOM   2686 N  N    B LEU   A 1 127 ? 18.889 -5.906  -0.157  0.36 10.06 ?  127 LEU   A N    1 
ATOM   2687 C  CA   A LEU   A 1 127 ? 19.927 -5.707  -1.229  0.64 10.35 ?  127 LEU   A CA   1 
ATOM   2688 C  CA   B LEU   A 1 127 ? 19.881 -5.423  -1.108  0.36 9.99  ?  127 LEU   A CA   1 
ATOM   2689 C  C    A LEU   A 1 127 ? 19.323 -5.507  -2.613  0.64 9.94  ?  127 LEU   A C    1 
ATOM   2690 C  C    B LEU   A 1 127 ? 19.295 -5.341  -2.513  0.36 10.25 ?  127 LEU   A C    1 
ATOM   2691 O  O    A LEU   A 1 127 ? 18.516 -6.310  -3.089  0.64 10.01 ?  127 LEU   A O    1 
ATOM   2692 O  O    B LEU   A 1 127 ? 18.437 -6.134  -2.909  0.36 10.68 ?  127 LEU   A O    1 
ATOM   2693 C  CB   A LEU   A 1 127 ? 21.105 -6.678  -1.320  0.64 11.09 ?  127 LEU   A CB   1 
ATOM   2694 C  CB   B LEU   A 1 127 ? 21.108 -6.334  -1.122  0.36 10.31 ?  127 LEU   A CB   1 
ATOM   2695 C  CG   A LEU   A 1 127 ? 21.902 -6.923  -0.041  0.64 11.51 ?  127 LEU   A CG   1 
ATOM   2696 C  CG   B LEU   A 1 127 ? 21.898 -6.416  0.186   0.36 10.58 ?  127 LEU   A CG   1 
ATOM   2697 C  CD1  A LEU   A 1 127 ? 22.991 -7.926  -0.319  0.64 11.36 ?  127 LEU   A CD1  1 
ATOM   2698 C  CD1  B LEU   A 1 127 ? 23.089 -7.345  0.026   0.36 10.90 ?  127 LEU   A CD1  1 
ATOM   2699 C  CD2  A LEU   A 1 127 ? 22.506 -5.638  0.477   0.64 12.35 ?  127 LEU   A CD2  1 
ATOM   2700 C  CD2  B LEU   A 1 127 ? 22.346 -5.038  0.668   0.36 11.48 ?  127 LEU   A CD2  1 
ATOM   2701 H  H    A LEU   A 1 127 ? 19.074 -7.022  -0.027  0.64 12.79 ?  127 LEU   A H    1 
ATOM   2702 H  H    B LEU   A 1 127 ? 19.087 -6.655  0.225   0.36 12.07 ?  127 LEU   A H    1 
ATOM   2703 H  HA   A LEU   A 1 127 ? 20.261 -4.855  -0.908  0.64 12.42 ?  127 LEU   A HA   1 
ATOM   2704 H  HA   B LEU   A 1 127 ? 20.163 -4.535  -0.843  0.36 11.99 ?  127 LEU   A HA   1 
ATOM   2705 H  HB2  A LEU   A 1 127 ? 20.765 -7.538  -1.614  0.64 13.30 ?  127 LEU   A HB2  1 
ATOM   2706 H  HB2  B LEU   A 1 127 ? 20.814 -7.232  -1.347  0.36 12.37 ?  127 LEU   A HB2  1 
ATOM   2707 H  HB3  A LEU   A 1 127 ? 21.728 -6.338  -1.979  0.64 13.30 ?  127 LEU   A HB3  1 
ATOM   2708 H  HB3  B LEU   A 1 127 ? 21.710 -6.012  -1.813  0.36 12.37 ?  127 LEU   A HB3  1 
ATOM   2709 H  HG   A LEU   A 1 127 ? 21.315 -7.293  0.643   0.64 13.82 ?  127 LEU   A HG   1 
ATOM   2710 H  HG   B LEU   A 1 127 ? 21.322 -6.792  0.867   0.36 12.69 ?  127 LEU   A HG   1 
ATOM   2711 H  HD11 A LEU   A 1 127 ? 23.464 -8.119  0.506   0.64 13.63 ?  127 LEU   A HD11 1 
ATOM   2712 H  HD11 B LEU   A 1 127 ? 23.600 -7.341  0.850   0.36 13.08 ?  127 LEU   A HD11 1 
ATOM   2713 H  HD12 A LEU   A 1 127 ? 22.592 -8.743  -0.667  0.64 13.63 ?  127 LEU   A HD12 1 
ATOM   2714 H  HD12 B LEU   A 1 127 ? 22.767 -8.240  -0.160  0.36 13.08 ?  127 LEU   A HD12 1 
ATOM   2715 H  HD13 A LEU   A 1 127 ? 23.601 -7.555  -0.973  0.64 13.63 ?  127 LEU   A HD13 1 
ATOM   2716 H  HD13 B LEU   A 1 127 ? 23.639 -7.029  -0.707  0.36 13.08 ?  127 LEU   A HD13 1 
ATOM   2717 H  HD21 A LEU   A 1 127 ? 23.100 -5.843  1.215   0.64 14.82 ?  127 LEU   A HD21 1 
ATOM   2718 H  HD21 B LEU   A 1 127 ? 22.953 -5.149  1.417   0.36 13.77 ?  127 LEU   A HD21 1 
ATOM   2719 H  HD22 A LEU   A 1 127 ? 23.007 -5.219  -0.243  0.64 14.82 ?  127 LEU   A HD22 1 
ATOM   2720 H  HD22 B LEU   A 1 127 ? 22.795 -4.578  -0.057  0.36 13.77 ?  127 LEU   A HD22 1 
ATOM   2721 H  HD23 A LEU   A 1 127 ? 21.796 -5.052  0.771   0.64 14.82 ?  127 LEU   A HD23 1 
ATOM   2722 H  HD23 B LEU   A 1 127 ? 21.566 -4.531  0.948   0.36 13.77 ?  127 LEU   A HD23 1 
ATOM   2723 N  N    A SER   A 1 128 ? 19.738 -4.429  -3.263  0.64 10.24 ?  128 SER   A N    1 
ATOM   2724 N  N    B SER   A 1 128 ? 19.778 -4.358  -3.267  0.36 10.43 ?  128 SER   A N    1 
ATOM   2725 C  CA   A SER   A 1 128 ? 19.322 -4.033  -4.603  0.64 10.66 ?  128 SER   A CA   1 
ATOM   2726 C  CA   B SER   A 1 128 ? 19.427 -4.065  -4.652  0.36 10.04 ?  128 SER   A CA   1 
ATOM   2727 C  C    A SER   A 1 128 ? 17.861 -3.601  -4.685  0.64 10.93 ?  128 SER   A C    1 
ATOM   2728 C  C    B SER   A 1 128 ? 17.992 -3.587  -4.840  0.36 9.55  ?  128 SER   A C    1 
ATOM   2729 O  O    A SER   A 1 128 ? 17.374 -3.322  -5.785  0.64 12.36 ?  128 SER   A O    1 
ATOM   2730 O  O    B SER   A 1 128 ? 17.631 -3.215  -5.961  0.36 9.54  ?  128 SER   A O    1 
ATOM   2731 C  CB   A SER   A 1 128 ? 19.670 -5.080  -5.672  0.64 11.10 ?  128 SER   A CB   1 
ATOM   2732 C  CB   B SER   A 1 128 ? 19.741 -5.217  -5.617  0.36 10.26 ?  128 SER   A CB   1 
ATOM   2733 O  OG   A SER   A 1 128 ? 21.079 -5.275  -5.728  0.64 11.56 ?  128 SER   A OG   1 
ATOM   2734 O  OG   B SER   A 1 128 ? 21.144 -5.430  -5.693  0.36 10.54 ?  128 SER   A OG   1 
ATOM   2735 H  H    A SER   A 1 128 ? 20.313 -3.879  -2.925  0.64 12.29 ?  128 SER   A H    1 
ATOM   2736 H  H    B SER   A 1 128 ? 20.370 -3.808  -2.967  0.36 12.51 ?  128 SER   A H    1 
ATOM   2737 H  HA   A SER   A 1 128 ? 19.848 -3.256  -4.825  0.64 12.79 ?  128 SER   A HA   1 
ATOM   2738 H  HA   B SER   A 1 128 ? 19.981 -3.324  -4.926  0.36 12.05 ?  128 SER   A HA   1 
ATOM   2739 H  HB2  A SER   A 1 128 ? 19.237 -5.920  -5.457  0.64 13.32 ?  128 SER   A HB2  1 
ATOM   2740 H  HB2  B SER   A 1 128 ? 19.308 -6.022  -5.298  0.36 12.32 ?  128 SER   A HB2  1 
ATOM   2741 H  HB3  A SER   A 1 128 ? 19.361 -4.759  -6.538  0.64 13.32 ?  128 SER   A HB3  1 
ATOM   2742 H  HB3  B SER   A 1 128 ? 19.405 -4.983  -6.499  0.36 12.32 ?  128 SER   A HB3  1 
ATOM   2743 H  HG   A SER   A 1 128 ? 21.461 -4.549  -5.908  0.64 13.87 ?  128 SER   A HG   1 
ATOM   2744 H  HG   B SER   A 1 128 ? 21.519 -4.724  -5.957  0.36 12.65 ?  128 SER   A HG   1 
ATOM   2745 N  N    A ALA   A 1 129 ? 17.155 -3.520  -3.556  0.64 11.95 ?  129 ALA   A N    1 
ATOM   2746 N  N    B ALA   A 1 129 ? 17.174 -3.565  -3.790  0.36 10.18 ?  129 ALA   A N    1 
ATOM   2747 C  CA   A ALA   A 1 129 ? 15.781 -3.037  -3.544  0.64 11.93 ?  129 ALA   A CA   1 
ATOM   2748 C  CA   B ALA   A 1 129 ? 15.808 -3.075  -3.878  0.36 10.27 ?  129 ALA   A CA   1 
ATOM   2749 C  C    A ALA   A 1 129 ? 15.764 -1.507  -3.526  0.64 11.79 ?  129 ALA   A C    1 
ATOM   2750 C  C    B ALA   A 1 129 ? 15.803 -1.555  -3.698  0.36 10.80 ?  129 ALA   A C    1 
ATOM   2751 O  O    A ALA   A 1 129 ? 16.807 -0.845  -3.570  0.64 11.94 ?  129 ALA   A O    1 
ATOM   2752 O  O    B ALA   A 1 129 ? 16.849 -0.900  -3.743  0.36 10.63 ?  129 ALA   A O    1 
ATOM   2753 C  CB   A ALA   A 1 129 ? 15.013 -3.625  -2.359  0.64 13.19 ?  129 ALA   A CB   1 
ATOM   2754 C  CB   B ALA   A 1 129 ? 14.917 -3.820  -2.881  0.36 10.02 ?  129 ALA   A CB   1 
ATOM   2755 H  H    A ALA   A 1 129 ? 17.448 -3.746  -2.779  0.64 14.34 ?  129 ALA   A H    1 
ATOM   2756 H  H    B ALA   A 1 129 ? 17.391 -3.834  -3.000  0.36 12.21 ?  129 ALA   A H    1 
ATOM   2757 H  HA   A ALA   A 1 129 ? 15.340 -3.335  -4.355  0.64 14.32 ?  129 ALA   A HA   1 
ATOM   2758 H  HA   B ALA   A 1 129 ? 15.468 -3.259  -4.763  0.36 12.32 ?  129 ALA   A HA   1 
ATOM   2759 H  HB1  A ALA   A 1 129 ? 14.100 -3.295  -2.378  0.64 15.83 ?  129 ALA   A HB1  1 
ATOM   2760 H  HB1  B ALA   A 1 129 ? 14.014 -3.470  -2.940  0.36 12.03 ?  129 ALA   A HB1  1 
ATOM   2761 H  HB2  A ALA   A 1 129 ? 15.015 -4.592  -2.428  0.64 15.83 ?  129 ALA   A HB2  1 
ATOM   2762 H  HB2  B ALA   A 1 129 ? 14.921 -4.765  -3.099  0.36 12.03 ?  129 ALA   A HB2  1 
ATOM   2763 H  HB3  A ALA   A 1 129 ? 15.446 -3.351  -1.535  0.64 15.83 ?  129 ALA   A HB3  1 
ATOM   2764 H  HB3  B ALA   A 1 129 ? 15.264 -3.688  -1.983  0.36 12.03 ?  129 ALA   A HB3  1 
ATOM   2765 N  N    A GLY   A 1 130 ? 14.562 -0.938  -3.481  0.64 12.42 ?  130 GLY   A N    1 
ATOM   2766 N  N    B GLY   A 1 130 ? 14.619 -0.974  -3.511  0.36 11.41 ?  130 GLY   A N    1 
ATOM   2767 C  CA   A GLY   A 1 130 ? 14.440 0.510   -3.470  0.64 12.66 ?  130 GLY   A CA   1 
ATOM   2768 C  CA   B GLY   A 1 130 ? 14.537 0.466   -3.340  0.36 11.69 ?  130 GLY   A CA   1 
ATOM   2769 C  C    A GLY   A 1 130 ? 15.089 1.120   -4.696  0.64 12.29 ?  130 GLY   A C    1 
ATOM   2770 C  C    B GLY   A 1 130 ? 15.086 1.186   -4.554  0.36 11.62 ?  130 GLY   A C    1 
ATOM   2771 O  O    A GLY   A 1 130 ? 14.886 0.659   -5.825  0.64 12.73 ?  130 GLY   A O    1 
ATOM   2772 O  O    B GLY   A 1 130 ? 14.821 0.808   -5.700  0.36 11.88 ?  130 GLY   A O    1 
ATOM   2773 H  H    A GLY   A 1 130 ? 13.812 -1.368  -3.459  0.64 14.90 ?  130 GLY   A H    1 
ATOM   2774 H  H    B GLY   A 1 130 ? 13.863 -1.387  -3.491  0.36 13.69 ?  130 GLY   A H    1 
ATOM   2775 H  HA2  A GLY   A 1 130 ? 13.499 0.756   -3.456  0.64 15.19 ?  130 GLY   A HA2  1 
ATOM   2776 H  HA2  B GLY   A 1 130 ? 13.608 0.723   -3.202  0.36 14.03 ?  130 GLY   A HA2  1 
ATOM   2777 H  HA3  A GLY   A 1 130 ? 14.868 0.864   -2.681  0.64 15.19 ?  130 GLY   A HA3  1 
ATOM   2778 H  HA3  B GLY   A 1 130 ? 15.049 0.733   -2.564  0.36 14.03 ?  130 GLY   A HA3  1 
ATOM   2779 N  N    A ILE   A 1 131 ? 15.890 2.170   -4.476  0.64 12.41 ?  131 ILE   A N    1 
ATOM   2780 N  N    B ILE   A 1 131 ? 15.876 2.236   -4.306  0.36 11.90 ?  131 ILE   A N    1 
ATOM   2781 C  CA   A ILE   A 1 131 ? 16.457 2.936   -5.584  0.64 12.50 ?  131 ILE   A CA   1 
ATOM   2782 C  CA   B ILE   A 1 131 ? 16.440 3.038   -5.388  0.36 12.34 ?  131 ILE   A CA   1 
ATOM   2783 C  C    A ILE   A 1 131 ? 17.525 2.179   -6.368  0.64 12.27 ?  131 ILE   A C    1 
ATOM   2784 C  C    B ILE   A 1 131 ? 17.408 2.259   -6.269  0.36 12.48 ?  131 ILE   A C    1 
ATOM   2785 O  O    A ILE   A 1 131 ? 17.978 2.685   -7.403  0.64 12.97 ?  131 ILE   A O    1 
ATOM   2786 O  O    B ILE   A 1 131 ? 17.781 2.748   -7.341  0.36 12.98 ?  131 ILE   A O    1 
ATOM   2787 C  CB   A ILE   A 1 131 ? 16.946 4.335   -5.146  0.64 13.54 ?  131 ILE   A CB   1 
ATOM   2788 C  CB   B ILE   A 1 131 ? 17.115 4.330   -4.862  0.36 13.02 ?  131 ILE   A CB   1 
ATOM   2789 C  CG1  A ILE   A 1 131 ? 18.175 4.238   -4.236  0.64 15.04 ?  131 ILE   A CG1  1 
ATOM   2790 C  CG1  B ILE   A 1 131 ? 18.386 4.012   -4.064  0.36 14.01 ?  131 ILE   A CG1  1 
ATOM   2791 C  CG2  A ILE   A 1 131 ? 15.810 5.115   -4.474  0.64 13.52 ?  131 ILE   A CG2  1 
ATOM   2792 C  CG2  B ILE   A 1 131 ? 16.145 5.134   -4.018  0.36 13.37 ?  131 ILE   A CG2  1 
ATOM   2793 C  CD1  A ILE   A 1 131 ? 18.758 5.594   -3.847  0.64 15.92 ?  131 ILE   A CD1  1 
ATOM   2794 C  CD1  B ILE   A 1 131 ? 19.100 5.256   -3.533  0.36 14.57 ?  131 ILE   A CD1  1 
ATOM   2795 H  H    A ILE   A 1 131 ? 16.100 2.462   -3.696  0.64 14.89 ?  131 ILE   A H    1 
ATOM   2796 H  H    B ILE   A 1 131 ? 16.081 2.503   -3.516  0.36 14.27 ?  131 ILE   A H    1 
ATOM   2797 H  HA   A ILE   A 1 131 ? 15.736 3.092   -6.208  0.64 15.00 ?  131 ILE   A HA   1 
ATOM   2798 H  HA   B ILE   A 1 131 ? 15.711 3.319   -5.962  0.36 14.80 ?  131 ILE   A HA   1 
ATOM   2799 H  HB   A ILE   A 1 131 ? 17.203 4.816   -5.944  0.64 16.25 ?  131 ILE   A HB   1 
ATOM   2800 H  HB   B ILE   A 1 131 ? 17.362 4.868   -5.630  0.36 15.62 ?  131 ILE   A HB   1 
ATOM   2801 H  HG12 A ILE   A 1 131 ? 17.929 3.776   -3.420  0.64 18.05 ?  131 ILE   A HG12 1 
ATOM   2802 H  HG12 B ILE   A 1 131 ? 18.150 3.459   -3.306  0.36 16.81 ?  131 ILE   A HG12 1 
ATOM   2803 H  HG13 A ILE   A 1 131 ? 18.872 3.741   -4.696  0.64 18.05 ?  131 ILE   A HG13 1 
ATOM   2804 H  HG13 B ILE   A 1 131 ? 19.013 3.543   -4.636  0.36 16.81 ?  131 ILE   A HG13 1 
ATOM   2805 H  HG21 A ILE   A 1 131 ? 16.097 6.029   -4.328  0.64 16.23 ?  131 ILE   A HG21 1 
ATOM   2806 H  HG21 B ILE   A 1 131 ? 16.508 6.022   -3.880  0.36 16.05 ?  131 ILE   A HG21 1 
ATOM   2807 H  HG22 A ILE   A 1 131 ? 15.033 5.101   -5.054  0.64 16.23 ?  131 ILE   A HG22 1 
ATOM   2808 H  HG22 B ILE   A 1 131 ? 15.297 5.192   -4.484  0.36 16.05 ?  131 ILE   A HG22 1 
ATOM   2809 H  HG23 A ILE   A 1 131 ? 15.596 4.695   -3.625  0.64 16.23 ?  131 ILE   A HG23 1 
ATOM   2810 H  HG23 B ILE   A 1 131 ? 16.025 4.686   -3.167  0.36 16.05 ?  131 ILE   A HG23 1 
ATOM   2811 H  HD11 A ILE   A 1 131 ? 19.599 5.455   -3.382  0.64 19.11 ?  131 ILE   A HD11 1 
ATOM   2812 H  HD11 B ILE   A 1 131 ? 19.963 4.998   -3.173  0.36 17.48 ?  131 ILE   A HD11 1 
ATOM   2813 H  HD12 A ILE   A 1 131 ? 18.909 6.115   -4.651  0.64 19.11 ?  131 ILE   A HD12 1 
ATOM   2814 H  HD12 B ILE   A 1 131 ? 19.224 5.888   -4.262  0.36 17.48 ?  131 ILE   A HD12 1 
ATOM   2815 H  HD13 A ILE   A 1 131 ? 18.132 6.053   -3.267  0.64 19.11 ?  131 ILE   A HD13 1 
ATOM   2816 H  HD13 B ILE   A 1 131 ? 18.560 5.663   -2.836  0.36 17.48 ?  131 ILE   A HD13 1 
ATOM   2817 N  N    A PHE   A 1 132 ? 17.936 0.981   -5.922  0.64 11.81 ?  132 PHE   A N    1 
ATOM   2818 N  N    B PHE   A 1 132 ? 17.824 1.059   -5.853  0.36 12.54 ?  132 PHE   A N    1 
ATOM   2819 C  CA   A PHE   A 1 132 ? 18.782 0.127   -6.754  0.64 11.98 ?  132 PHE   A CA   1 
ATOM   2820 C  CA   B PHE   A 1 132 ? 18.769 0.283   -6.648  0.36 12.57 ?  132 PHE   A CA   1 
ATOM   2821 C  C    A PHE   A 1 132 ? 17.989 -0.636  -7.819  0.64 12.25 ?  132 PHE   A C    1 
ATOM   2822 C  C    B PHE   A 1 132 ? 18.116 -0.456  -7.818  0.36 13.03 ?  132 PHE   A C    1 
ATOM   2823 O  O    A PHE   A 1 132 ? 18.597 -1.300  -8.664  0.64 12.47 ?  132 PHE   A O    1 
ATOM   2824 O  O    B PHE   A 1 132 ? 18.839 -0.961  -8.683  0.36 13.73 ?  132 PHE   A O    1 
ATOM   2825 C  CB   A PHE   A 1 132 ? 19.609 -0.854  -5.905  0.64 11.33 ?  132 PHE   A CB   1 
ATOM   2826 C  CB   B PHE   A 1 132 ? 19.556 -0.695  -5.766  0.36 11.92 ?  132 PHE   A CB   1 
ATOM   2827 C  CG   A PHE   A 1 132 ? 20.833 -0.242  -5.241  0.64 11.20 ?  132 PHE   A CG   1 
ATOM   2828 C  CG   B PHE   A 1 132 ? 20.787 -0.098  -5.119  0.36 11.45 ?  132 PHE   A CG   1 
ATOM   2829 C  CD1  A PHE   A 1 132 ? 20.714 0.805   -4.342  0.64 12.10 ?  132 PHE   A CD1  1 
ATOM   2830 C  CD1  B PHE   A 1 132 ? 20.676 0.875   -4.138  0.36 11.88 ?  132 PHE   A CD1  1 
ATOM   2831 C  CD2  A PHE   A 1 132 ? 22.095 -0.776  -5.469  0.64 11.96 ?  132 PHE   A CD2  1 
ATOM   2832 C  CD2  B PHE   A 1 132 ? 22.054 -0.542  -5.469  0.36 11.64 ?  132 PHE   A CD2  1 
ATOM   2833 C  CE1  A PHE   A 1 132 ? 21.840 1.339   -3.719  0.64 12.70 ?  132 PHE   A CE1  1 
ATOM   2834 C  CE1  B PHE   A 1 132 ? 21.807 1.410   -3.537  0.36 12.25 ?  132 PHE   A CE1  1 
ATOM   2835 C  CE2  A PHE   A 1 132 ? 23.219 -0.252  -4.846  0.64 12.36 ?  132 PHE   A CE2  1 
ATOM   2836 C  CE2  B PHE   A 1 132 ? 23.188 -0.013  -4.869  0.36 12.05 ?  132 PHE   A CE2  1 
ATOM   2837 C  CZ   A PHE   A 1 132 ? 23.087 0.807   -3.969  0.64 12.42 ?  132 PHE   A CZ   1 
ATOM   2838 C  CZ   B PHE   A 1 132 ? 23.060 0.963   -3.901  0.36 12.28 ?  132 PHE   A CZ   1 
ATOM   2839 H  H    A PHE   A 1 132 ? 17.744 0.644   -5.149  0.64 14.17 ?  132 PHE   A H    1 
ATOM   2840 H  H    B PHE   A 1 132 ? 17.569 0.680   -5.122  0.36 15.04 ?  132 PHE   A H    1 
ATOM   2841 H  HA   A PHE   A 1 132 ? 19.414 0.695   -7.215  0.64 14.37 ?  132 PHE   A HA   1 
ATOM   2842 H  HA   B PHE   A 1 132 ? 19.410 0.904   -7.023  0.36 15.09 ?  132 PHE   A HA   1 
ATOM   2843 H  HB2  A PHE   A 1 132 ? 19.044 -1.209  -5.200  0.64 13.60 ?  132 PHE   A HB2  1 
ATOM   2844 H  HB2  B PHE   A 1 132 ? 18.978 -1.010  -5.056  0.36 14.30 ?  132 PHE   A HB2  1 
ATOM   2845 H  HB3  A PHE   A 1 132 ? 19.916 -1.582  -6.472  0.64 13.60 ?  132 PHE   A HB3  1 
ATOM   2846 H  HB3  B PHE   A 1 132 ? 19.844 -1.439  -6.314  0.36 14.30 ?  132 PHE   A HB3  1 
ATOM   2847 H  HD1  A PHE   A 1 132 ? 19.879 1.169   -4.162  0.64 14.51 ?  132 PHE   A HD1  1 
ATOM   2848 H  HD1  B PHE   A 1 132 ? 19.835 1.183   -3.888  0.36 14.26 ?  132 PHE   A HD1  1 
ATOM   2849 H  HD2  A PHE   A 1 132 ? 22.190 -1.493  -6.059  0.64 14.35 ?  132 PHE   A HD2  1 
ATOM   2850 H  HD2  B PHE   A 1 132 ? 22.148 -1.201  -6.121  0.36 13.97 ?  132 PHE   A HD2  1 
ATOM   2851 H  HE1  A PHE   A 1 132 ? 21.753 2.052   -3.125  0.64 15.23 ?  132 PHE   A HE1  1 
ATOM   2852 H  HE1  B PHE   A 1 132 ? 21.722 2.068   -2.885  0.36 14.70 ?  132 PHE   A HE1  1 
ATOM   2853 H  HE2  A PHE   A 1 132 ? 24.059 -0.612  -5.022  0.64 14.83 ?  132 PHE   A HE2  1 
ATOM   2854 H  HE2  B PHE   A 1 132 ? 24.032 -0.317  -5.119  0.36 14.47 ?  132 PHE   A HE2  1 
ATOM   2855 H  HZ   A PHE   A 1 132 ? 23.840 1.167   -3.553  0.64 14.90 ?  132 PHE   A HZ   1 
ATOM   2856 H  HZ   B PHE   A 1 132 ? 23.820 1.321   -3.499  0.36 14.73 ?  132 PHE   A HZ   1 
ATOM   2857 N  N    A GLY   A 1 133 ? 16.656 -0.577  -7.789  0.64 12.57 ?  133 GLY   A N    1 
ATOM   2858 N  N    B GLY   A 1 133 ? 16.785 -0.545  -7.874  0.36 13.01 ?  133 GLY   A N    1 
ATOM   2859 C  CA   A GLY   A 1 133 ? 15.839 -0.935  -8.938  0.64 13.38 ?  133 GLY   A CA   1 
ATOM   2860 C  CA   B GLY   A 1 133 ? 16.084 -0.935  -9.084  0.36 13.16 ?  133 GLY   A CA   1 
ATOM   2861 C  C    A GLY   A 1 133 ? 15.584 -2.407  -9.194  0.64 13.48 ?  133 GLY   A C    1 
ATOM   2862 C  C    B GLY   A 1 133 ? 15.474 -2.325  -9.089  0.36 13.05 ?  133 GLY   A C    1 
ATOM   2863 O  O    A GLY   A 1 133 ? 15.016 -2.732  -10.243 0.64 14.22 ?  133 GLY   A O    1 
ATOM   2864 O  O    B GLY   A 1 133 ? 14.587 -2.583  -9.914  0.36 13.11 ?  133 GLY   A O    1 
ATOM   2865 H  H    A GLY   A 1 133 ? 16.200 -0.325  -7.106  0.64 15.08 ?  133 GLY   A H    1 
ATOM   2866 H  H    B GLY   A 1 133 ? 16.261 -0.378  -7.209  0.36 15.62 ?  133 GLY   A H    1 
ATOM   2867 H  HA2  A GLY   A 1 133 ? 14.971 -0.511  -8.839  0.64 16.06 ?  133 GLY   A HA2  1 
ATOM   2868 H  HA2  B GLY   A 1 133 ? 15.366 -0.310  -9.252  0.36 15.80 ?  133 GLY   A HA2  1 
ATOM   2869 H  HA3  A GLY   A 1 133 ? 16.252 -0.573  -9.736  0.64 16.06 ?  133 GLY   A HA3  1 
ATOM   2870 H  HA3  B GLY   A 1 133 ? 16.699 -0.881  -9.832  0.36 15.80 ?  133 GLY   A HA3  1 
ATOM   2871 N  N    A ALA   A 1 134 ? 15.975 -3.309  -8.296  0.64 13.15 ?  134 ALA   A N    1 
ATOM   2872 N  N    B ALA   A 1 134 ? 15.911 -3.227  -8.216  0.36 13.09 ?  134 ALA   A N    1 
ATOM   2873 C  CA   A ALA   A 1 134 ? 15.659 -4.718  -8.481  0.64 13.42 ?  134 ALA   A CA   1 
ATOM   2874 C  CA   B ALA   A 1 134 ? 15.472 -4.612  -8.304  0.36 13.13 ?  134 ALA   A CA   1 
ATOM   2875 C  C    A ALA   A 1 134 ? 14.282 -5.037  -7.893  0.64 13.37 ?  134 ALA   A C    1 
ATOM   2876 C  C    B ALA   A 1 134 ? 14.167 -4.836  -7.549  0.36 12.82 ?  134 ALA   A C    1 
ATOM   2877 O  O    A ALA   A 1 134 ? 13.676 -4.236  -7.178  0.64 14.25 ?  134 ALA   A O    1 
ATOM   2878 O  O    B ALA   A 1 134 ? 13.797 -4.080  -6.647  0.36 12.86 ?  134 ALA   A O    1 
ATOM   2879 C  CB   A ALA   A 1 134 ? 16.741 -5.603  -7.858  0.64 14.27 ?  134 ALA   A CB   1 
ATOM   2880 C  CB   B ALA   A 1 134 ? 16.536 -5.558  -7.756  0.36 13.56 ?  134 ALA   A CB   1 
ATOM   2881 H  H    A ALA   A 1 134 ? 16.427 -3.127  -7.582  0.64 15.77 ?  134 ALA   A H    1 
ATOM   2882 H  H    B ALA   A 1 134 ? 16.451 -3.059  -7.569  0.36 15.71 ?  134 ALA   A H    1 
ATOM   2883 H  HA   A ALA   A 1 134 ? 15.632 -4.909  -9.432  0.64 16.10 ?  134 ALA   A HA   1 
ATOM   2884 H  HA   B ALA   A 1 134 ? 15.318 -4.828  -9.236  0.36 15.76 ?  134 ALA   A HA   1 
ATOM   2885 H  HB1  A ALA   A 1 134 ? 16.516 -6.531  -8.017  0.64 17.13 ?  134 ALA   A HB1  1 
ATOM   2886 H  HB1  B ALA   A 1 134 ? 16.214 -6.468  -7.847  0.36 16.27 ?  134 ALA   A HB1  1 
ATOM   2887 H  HB2  A ALA   A 1 134 ? 17.596 -5.394  -8.272  0.64 17.13 ?  134 ALA   A HB2  1 
ATOM   2888 H  HB2  B ALA   A 1 134 ? 17.347 -5.436  -8.267  0.36 16.27 ?  134 ALA   A HB2  1 
ATOM   2889 H  HB3  A ALA   A 1 134 ? 16.785 -5.427  -6.907  0.64 17.13 ?  134 ALA   A HB3  1 
ATOM   2890 H  HB3  B ALA   A 1 134 ? 16.689 -5.349  -6.824  0.36 16.27 ?  134 ALA   A HB3  1 
ATOM   2891 N  N    A ASP   A 1 135 ? 13.781 -6.227  -8.224  0.64 13.45 ?  135 ASP   A N    1 
ATOM   2892 N  N    B ASP   A 1 135 ? 13.478 -5.907  -7.933  0.36 13.23 ?  135 ASP   A N    1 
ATOM   2893 C  CA   A ASP   A 1 135 ? 12.514 -6.706  -7.679  0.64 14.07 ?  135 ASP   A CA   1 
ATOM   2894 C  CA   B ASP   A 1 135 ? 12.233 -6.307  -7.293  0.36 13.62 ?  135 ASP   A CA   1 
ATOM   2895 C  C    A ASP   A 1 135 ? 12.731 -7.147  -6.238  0.64 13.68 ?  135 ASP   A C    1 
ATOM   2896 C  C    B ASP   A 1 135 ? 12.532 -6.799  -5.881  0.36 13.02 ?  135 ASP   A C    1 
ATOM   2897 O  O    A ASP   A 1 135 ? 13.528 -8.059  -5.996  0.64 13.60 ?  135 ASP   A O    1 
ATOM   2898 O  O    B ASP   A 1 135 ? 13.283 -7.771  -5.721  0.36 12.66 ?  135 ASP   A O    1 
ATOM   2899 C  CB   A ASP   A 1 135 ? 12.026 -7.890  -8.507  0.64 16.45 ?  135 ASP   A CB   1 
ATOM   2900 C  CB   B ASP   A 1 135 ? 11.602 -7.425  -8.120  0.36 14.77 ?  135 ASP   A CB   1 
ATOM   2901 C  CG   A ASP   A 1 135 ? 10.730 -8.513  -7.981  0.64 18.21 ?  135 ASP   A CG   1 
ATOM   2902 C  CG   B ASP   A 1 135 ? 10.209 -7.799  -7.643  0.36 16.34 ?  135 ASP   A CG   1 
ATOM   2903 O  OD1  A ASP   A 1 135 ? 10.183 -8.067  -6.954  0.64 18.10 ?  135 ASP   A OD1  1 
ATOM   2904 O  OD1  B ASP   A 1 135 ? 9.854  -7.459  -6.493  0.36 16.61 ?  135 ASP   A OD1  1 
ATOM   2905 O  OD2  A ASP   A 1 135 ? 10.254 -9.471  -8.623  0.64 20.57 -1 135 ASP   A OD2  1 
ATOM   2906 O  OD2  B ASP   A 1 135 ? 9.475  -8.444  -8.420  0.36 17.66 -1 135 ASP   A OD2  1 
ATOM   2907 H  H    A ASP   A 1 135 ? 14.159 -6.776  -8.765  0.64 16.15 ?  135 ASP   A H    1 
ATOM   2908 H  H    B ASP   A 1 135 ? 13.711 -6.423  -8.576  0.36 15.88 ?  135 ASP   A H    1 
ATOM   2909 H  HA   A ASP   A 1 135 ? 11.856 -5.997  -7.719  0.64 16.88 ?  135 ASP   A HA   1 
ATOM   2910 H  HA   B ASP   A 1 135 ? 11.613 -5.556  -7.270  0.36 16.35 ?  135 ASP   A HA   1 
ATOM   2911 H  HB2  A ASP   A 1 135 ? 11.860 -7.592  -9.410  0.64 19.74 ?  135 ASP   A HB2  1 
ATOM   2912 H  HB2  B ASP   A 1 135 ? 11.549 -7.137  -9.049  0.36 17.72 ?  135 ASP   A HB2  1 
ATOM   2913 H  HB3  A ASP   A 1 135 ? 12.708 -8.578  -8.500  0.64 19.74 ?  135 ASP   A HB3  1 
ATOM   2914 H  HB3  B ASP   A 1 135 ? 12.155 -8.216  -8.053  0.36 17.72 ?  135 ASP   A HB3  1 
ATOM   2915 N  N    A PRO   A 1 136 ? 12.060 -6.536  -5.260  0.64 13.24 ?  136 PRO   A N    1 
ATOM   2916 N  N    B PRO   A 1 136 ? 11.989 -6.166  -4.838  0.36 12.68 ?  136 PRO   A N    1 
ATOM   2917 C  CA   A PRO   A 1 136 ? 12.286 -6.937  -3.860  0.64 13.72 ?  136 PRO   A CA   1 
ATOM   2918 C  CA   B PRO   A 1 136 ? 12.273 -6.631  -3.471  0.36 12.76 ?  136 PRO   A CA   1 
ATOM   2919 C  C    A PRO   A 1 136 ? 11.873 -8.366  -3.547  0.64 13.01 ?  136 PRO   A C    1 
ATOM   2920 C  C    B PRO   A 1 136 ? 11.843 -8.065  -3.210  0.36 12.04 ?  136 PRO   A C    1 
ATOM   2921 O  O    A PRO   A 1 136 ? 12.492 -8.995  -2.682  0.64 12.93 ?  136 PRO   A O    1 
ATOM   2922 O  O    B PRO   A 1 136 ? 12.409 -8.720  -2.326  0.36 10.96 ?  136 PRO   A O    1 
ATOM   2923 C  CB   A PRO   A 1 136 ? 11.471 -5.909  -3.064  0.64 14.39 ?  136 PRO   A CB   1 
ATOM   2924 C  CB   B PRO   A 1 136 ? 11.508 -5.627  -2.595  0.36 13.22 ?  136 PRO   A CB   1 
ATOM   2925 C  CG   A PRO   A 1 136 ? 10.426 -5.426  -4.027  0.64 14.81 ?  136 PRO   A CG   1 
ATOM   2926 C  CG   B PRO   A 1 136 ? 10.445 -5.074  -3.494  0.36 13.52 ?  136 PRO   A CG   1 
ATOM   2927 C  CD   A PRO   A 1 136 ? 11.077 -5.443  -5.375  0.64 14.16 ?  136 PRO   A CD   1 
ATOM   2928 C  CD   B PRO   A 1 136 ? 11.087 -5.003  -4.845  0.36 12.84 ?  136 PRO   A CD   1 
ATOM   2929 H  HA   A PRO   A 1 136 ? 13.224 -6.833  -3.630  0.64 16.46 ?  136 PRO   A HA   1 
ATOM   2930 H  HA   B PRO   A 1 136 ? 13.221 -6.547  -3.283  0.36 15.31 ?  136 PRO   A HA   1 
ATOM   2931 H  HB2  A PRO   A 1 136 ? 11.060 -6.336  -2.294  0.64 17.27 ?  136 PRO   A HB2  1 
ATOM   2932 H  HB2  B PRO   A 1 136 ? 11.113 -6.083  -1.838  0.36 15.87 ?  136 PRO   A HB2  1 
ATOM   2933 H  HB3  A PRO   A 1 136 ? 12.048 -5.180  -2.782  0.64 17.27 ?  136 PRO   A HB3  1 
ATOM   2934 H  HB3  B PRO   A 1 136 ? 12.106 -4.920  -2.302  0.36 15.87 ?  136 PRO   A HB3  1 
ATOM   2935 H  HG2  A PRO   A 1 136 ? 9.666  -6.025  -4.007  0.64 17.78 ?  136 PRO   A HG2  1 
ATOM   2936 H  HG2  B PRO   A 1 136 ? 9.683  -5.676  -3.511  0.36 16.23 ?  136 PRO   A HG2  1 
ATOM   2937 H  HG3  A PRO   A 1 136 ? 10.161 -4.524  -3.791  0.64 17.78 ?  136 PRO   A HG3  1 
ATOM   2938 H  HG3  B PRO   A 1 136 ? 10.181 -4.192  -3.195  0.36 16.23 ?  136 PRO   A HG3  1 
ATOM   2939 H  HD2  A PRO   A 1 136 ? 10.421 -5.653  -6.061  0.64 16.99 ?  136 PRO   A HD2  1 
ATOM   2940 H  HD2  B PRO   A 1 136 ? 10.417 -5.096  -5.543  0.36 15.41 ?  136 PRO   A HD2  1 
ATOM   2941 H  HD3  A PRO   A 1 136 ? 11.522 -4.601  -5.552  0.64 16.99 ?  136 PRO   A HD3  1 
ATOM   2942 H  HD3  B PRO   A 1 136 ? 11.593 -4.179  -4.945  0.36 15.41 ?  136 PRO   A HD3  1 
ATOM   2943 N  N    A ILE   A 1 137 ? 10.832 -8.892  -4.196  0.64 13.18 ?  137 ILE   A N    1 
ATOM   2944 N  N    B ILE   A 1 137 ? 10.843 -8.567  -3.939  0.36 12.60 ?  137 ILE   A N    1 
ATOM   2945 C  CA   A ILE   A 1 137 ? 10.474 -10.294 -3.994  0.64 13.73 ?  137 ILE   A CA   1 
ATOM   2946 C  CA   B ILE   A 1 137 ? 10.434 -9.960  -3.780  0.36 13.03 ?  137 ILE   A CA   1 
ATOM   2947 C  C    A ILE   A 1 137 ? 11.648 -11.183 -4.376  0.64 13.20 ?  137 ILE   A C    1 
ATOM   2948 C  C    B ILE   A 1 137 ? 11.565 -10.895 -4.194  0.36 12.99 ?  137 ILE   A C    1 
ATOM   2949 O  O    A ILE   A 1 137 ? 11.970 -12.157 -3.683  0.64 13.43 ?  137 ILE   A O    1 
ATOM   2950 O  O    B ILE   A 1 137 ? 11.850 -11.890 -3.517  0.36 13.02 ?  137 ILE   A O    1 
ATOM   2951 C  CB   A ILE   A 1 137 ? 9.194  -10.646 -4.779  0.64 14.70 ?  137 ILE   A CB   1 
ATOM   2952 C  CB   B ILE   A 1 137 ? 9.141  -10.231 -4.574  0.36 13.57 ?  137 ILE   A CB   1 
ATOM   2953 C  CG1  A ILE   A 1 137 ? 7.993  -9.856  -4.245  0.64 16.20 ?  137 ILE   A CG1  1 
ATOM   2954 C  CG1  B ILE   A 1 137 ? 8.027  -9.265  -4.143  0.36 14.66 ?  137 ILE   A CG1  1 
ATOM   2955 C  CG2  A ILE   A 1 137 ? 8.929  -12.149 -4.712  0.64 14.88 ?  137 ILE   A CG2  1 
ATOM   2956 C  CG2  B ILE   A 1 137 ? 8.707  -11.686 -4.406  0.36 13.46 ?  137 ILE   A CG2  1 
ATOM   2957 C  CD1  A ILE   A 1 137 ? 6.718  -10.036 -5.052  0.64 17.41 ?  137 ILE   A CD1  1 
ATOM   2958 C  CD1  B ILE   A 1 137 ? 6.793  -9.308  -5.026  0.36 15.43 ?  137 ILE   A CD1  1 
ATOM   2959 H  H    A ILE   A 1 137 ? 10.332 -8.470  -4.750  0.64 15.81 ?  137 ILE   A H    1 
ATOM   2960 H  H    B ILE   A 1 137 ? 10.388 -8.119  -4.518  0.36 15.12 ?  137 ILE   A H    1 
ATOM   2961 H  HA   A ILE   A 1 137 ? 10.292 -10.444 -3.056  0.64 16.47 ?  137 ILE   A HA   1 
ATOM   2962 H  HA   B ILE   A 1 137 ? 10.241 -10.120 -2.843  0.36 15.64 ?  137 ILE   A HA   1 
ATOM   2963 H  HB   A ILE   A 1 137 ? 9.325  -10.408 -5.707  0.64 17.64 ?  137 ILE   A HB   1 
ATOM   2964 H  HB   B ILE   A 1 137 ? 9.323  -10.076 -5.512  0.36 16.28 ?  137 ILE   A HB   1 
ATOM   2965 H  HG12 A ILE   A 1 137 ? 7.812  -10.139 -3.335  0.64 19.44 ?  137 ILE   A HG12 1 
ATOM   2966 H  HG12 B ILE   A 1 137 ? 7.751  -9.487  -3.241  0.36 17.59 ?  137 ILE   A HG12 1 
ATOM   2967 H  HG13 A ILE   A 1 137 ? 8.217  -8.911  -4.254  0.64 19.44 ?  137 ILE   A HG13 1 
ATOM   2968 H  HG13 B ILE   A 1 137 ? 8.366  -8.355  -4.166  0.36 17.59 ?  137 ILE   A HG13 1 
ATOM   2969 H  HG21 A ILE   A 1 137 ? 8.013  -12.340 -4.979  0.64 17.86 ?  137 ILE   A HG21 1 
ATOM   2970 H  HG21 B ILE   A 1 137 ? 7.842  -11.811 -4.825  0.36 16.15 ?  137 ILE   A HG21 1 
ATOM   2971 H  HG22 A ILE   A 1 137 ? 9.538  -12.604 -5.310  0.64 17.86 ?  137 ILE   A HG22 1 
ATOM   2972 H  HG22 B ILE   A 1 137 ? 9.362  -12.262 -4.830  0.36 16.15 ?  137 ILE   A HG22 1 
ATOM   2973 H  HG23 A ILE   A 1 137 ? 9.067  -12.451 -3.802  0.64 17.86 ?  137 ILE   A HG23 1 
ATOM   2974 H  HG23 B ILE   A 1 137 ? 8.648  -11.891 -3.460  0.36 16.15 ?  137 ILE   A HG23 1 
ATOM   2975 H  HD11 A ILE   A 1 137 ? 5.989  -10.235 -4.445  0.64 20.89 ?  137 ILE   A HD11 1 
ATOM   2976 H  HD11 B ILE   A 1 137 ? 6.212  -8.566  -4.793  0.36 18.52 ?  137 ILE   A HD11 1 
ATOM   2977 H  HD12 A ILE   A 1 137 ? 6.543  -9.215  -5.530  0.64 20.89 ?  137 ILE   A HD12 1 
ATOM   2978 H  HD12 B ILE   A 1 137 ? 7.067  -9.233  -5.955  0.36 18.52 ?  137 ILE   A HD12 1 
ATOM   2979 H  HD13 A ILE   A 1 137 ? 6.832  -10.761 -5.684  0.64 20.89 ?  137 ILE   A HD13 1 
ATOM   2980 H  HD13 B ILE   A 1 137 ? 6.331  -10.148 -4.885  0.36 18.52 ?  137 ILE   A HD13 1 
ATOM   2981 N  N    A HIS   A 1 138 ? 12.309 -10.854 -5.485  0.64 13.49 ?  138 HIS   A N    1 
ATOM   2982 N  N    B HIS   A 1 138 ? 12.228 -10.586 -5.312  0.36 13.24 ?  138 HIS   A N    1 
ATOM   2983 C  CA   A HIS   A 1 138 ? 13.520 -11.568 -5.865  0.64 13.50 ?  138 HIS   A CA   1 
ATOM   2984 C  CA   B HIS   A 1 138 ? 13.338 -11.412 -5.780  0.36 12.98 ?  138 HIS   A CA   1 
ATOM   2985 C  C    A HIS   A 1 138 ? 14.638 -11.372 -4.842  0.64 13.20 ?  138 HIS   A C    1 
ATOM   2986 C  C    B HIS   A 1 138 ? 14.517 -11.347 -4.816  0.36 12.91 ?  138 HIS   A C    1 
ATOM   2987 O  O    A HIS   A 1 138 ? 15.331 -12.336 -4.488  0.64 13.70 ?  138 HIS   A O    1 
ATOM   2988 O  O    B HIS   A 1 138 ? 15.131 -12.372 -4.497  0.36 13.31 ?  138 HIS   A O    1 
ATOM   2989 C  CB   A HIS   A 1 138 ? 13.960 -11.148 -7.266  0.64 14.68 ?  138 HIS   A CB   1 
ATOM   2990 C  CB   B HIS   A 1 138 ? 13.749 -10.953 -7.180  0.36 13.15 ?  138 HIS   A CB   1 
ATOM   2991 C  CG   A HIS   A 1 138 ? 15.207 -11.834 -7.724  0.64 15.93 ?  138 HIS   A CG   1 
ATOM   2992 C  CG   B HIS   A 1 138 ? 15.034 -11.548 -7.662  0.36 13.63 ?  138 HIS   A CG   1 
ATOM   2993 N  ND1  A HIS   A 1 138 ? 15.274 -13.195 -7.935  0.64 17.19 ?  138 HIS   A ND1  1 
ATOM   2994 N  ND1  B HIS   A 1 138 ? 15.175 -12.889 -7.947  0.36 14.50 ?  138 HIS   A ND1  1 
ATOM   2995 C  CD2  A HIS   A 1 138 ? 16.444 -11.351 -7.982  0.64 16.47 ?  138 HIS   A CD2  1 
ATOM   2996 C  CD2  B HIS   A 1 138 ? 16.238 -10.981 -7.915  0.36 13.83 ?  138 HIS   A CD2  1 
ATOM   2997 C  CE1  A HIS   A 1 138 ? 16.496 -13.517 -8.320  0.64 17.61 ?  138 HIS   A CE1  1 
ATOM   2998 C  CE1  B HIS   A 1 138 ? 16.412 -13.123 -8.350  0.36 14.42 ?  138 HIS   A CE1  1 
ATOM   2999 N  NE2  A HIS   A 1 138 ? 17.226 -12.417 -8.355  0.64 17.13 ?  138 HIS   A NE2  1 
ATOM   3000 N  NE2  B HIS   A 1 138 ? 17.077 -11.981 -8.341  0.36 14.15 ?  138 HIS   A NE2  1 
ATOM   3001 H  H    A HIS   A 1 138 ? 12.068 -10.235 -6.033  0.64 16.19 ?  138 HIS   A H    1 
ATOM   3002 H  H    B HIS   A 1 138 ? 12.058 -9.903  -5.810  0.36 15.89 ?  138 HIS   A H    1 
ATOM   3003 H  HA   A HIS   A 1 138 ? 13.317 -12.513 -5.901  0.64 16.20 ?  138 HIS   A HA   1 
ATOM   3004 H  HA   B HIS   A 1 138 ? 13.046 -12.331 -5.836  0.36 15.58 ?  138 HIS   A HA   1 
ATOM   3005 H  HB2  A HIS   A 1 138 ? 13.249 -11.365 -7.897  0.64 17.62 ?  138 HIS   A HB2  1 
ATOM   3006 H  HB2  B HIS   A 1 138 ? 13.050 -11.205 -7.807  0.36 15.78 ?  138 HIS   A HB2  1 
ATOM   3007 H  HB3  A HIS   A 1 138 ? 14.121 -10.192 -7.274  0.64 17.62 ?  138 HIS   A HB3  1 
ATOM   3008 H  HB3  B HIS   A 1 138 ? 13.851 -9.988  -7.177  0.36 15.78 ?  138 HIS   A HB3  1 
ATOM   3009 H  HD1  A HIS   A 1 138 ? 14.617 -13.746 -7.839  0.64 20.63 ?  138 HIS   A HD1  1 
ATOM   3010 H  HD1  B HIS   A 1 138 ? 14.555 -13.481 -7.869  0.36 17.40 ?  138 HIS   A HD1  1 
ATOM   3011 H  HD2  A HIS   A 1 138 ? 16.706 -10.461 -7.922  0.64 19.77 ?  138 HIS   A HD2  1 
ATOM   3012 H  HD2  B HIS   A 1 138 ? 16.454 -10.082 -7.820  0.36 16.59 ?  138 HIS   A HD2  1 
ATOM   3013 H  HE1  A HIS   A 1 138 ? 16.791 -14.371 -8.525  0.64 21.13 ?  138 HIS   A HE1  1 
ATOM   3014 H  HE1  B HIS   A 1 138 ? 16.752 -13.952 -8.600  0.36 17.31 ?  138 HIS   A HE1  1 
ATOM   3015 N  N    . SER   A 1 139 ? 14.835 -10.144 -4.345  1.00 12.80 ?  139 SER   A N    1 
ATOM   3016 C  CA   . SER   A 1 139 ? 15.903 -9.956  -3.372  1.00 12.60 ?  139 SER   A CA   1 
ATOM   3017 C  C    . SER   A 1 139 ? 15.680 -10.802 -2.125  1.00 12.28 ?  139 SER   A C    1 
ATOM   3018 O  O    . SER   A 1 139 ? 16.628 -11.390 -1.592  1.00 12.43 ?  139 SER   A O    1 
ATOM   3019 C  CB   . SER   A 1 139 ? 16.029 -8.476  -3.010  1.00 12.28 ?  139 SER   A CB   1 
ATOM   3020 O  OG   . SER   A 1 139 ? 17.106 -8.302  -2.107  1.00 12.58 ?  139 SER   A OG   1 
ATOM   3021 H  H    A SER   A 1 139 ? 14.388 -9.437  -4.544  0.64 15.36 ?  139 SER   A H    1 
ATOM   3022 H  H    B SER   A 1 139 ? 14.436 -9.415  -4.568  0.36 15.36 ?  139 SER   A H    1 
ATOM   3023 H  HA   . SER   A 1 139 ? 16.746 -10.228 -3.769  1.00 15.12 ?  139 SER   A HA   1 
ATOM   3024 H  HB2  . SER   A 1 139 ? 16.203 -7.956  -3.811  1.00 14.74 ?  139 SER   A HB2  1 
ATOM   3025 H  HB3  . SER   A 1 139 ? 15.205 -8.174  -2.590  1.00 14.74 ?  139 SER   A HB3  1 
ATOM   3026 H  HG   . SER   A 1 139 ? 17.179 -7.485  -1.892  1.00 15.10 ?  139 SER   A HG   1 
ATOM   3027 N  N    . LEU   A 1 140 ? 14.439 -10.870 -1.640  1.00 11.85 ?  140 LEU   A N    1 
ATOM   3028 C  CA   . LEU   A 1 140 ? 14.160 -11.689 -0.463  1.00 11.84 ?  140 LEU   A CA   1 
ATOM   3029 C  C    . LEU   A 1 140 ? 14.430 -13.164 -0.741  1.00 12.15 ?  140 LEU   A C    1 
ATOM   3030 O  O    . LEU   A 1 140 ? 14.980 -13.878 0.110   1.00 12.86 ?  140 LEU   A O    1 
ATOM   3031 C  CB   . LEU   A 1 140 ? 12.716 -11.473 -0.015  1.00 12.44 ?  140 LEU   A CB   1 
ATOM   3032 C  CG   . LEU   A 1 140 ? 12.246 -12.331 1.160   1.00 13.08 ?  140 LEU   A CG   1 
ATOM   3033 C  CD1  . LEU   A 1 140 ? 13.128 -12.149 2.391   1.00 13.48 ?  140 LEU   A CD1  1 
ATOM   3034 C  CD2  . LEU   A 1 140 ? 10.787 -12.020 1.495   1.00 13.88 ?  140 LEU   A CD2  1 
ATOM   3035 H  H    . LEU   A 1 140 ? 13.758 -10.455 -1.963  1.00 14.22 ?  140 LEU   A H    1 
ATOM   3036 H  HA   . LEU   A 1 140 ? 14.739 -11.409 0.263   1.00 14.21 ?  140 LEU   A HA   1 
ATOM   3037 H  HB2  . LEU   A 1 140 ? 12.608 -10.551 0.247   1.00 14.93 ?  140 LEU   A HB2  1 
ATOM   3038 H  HB3  . LEU   A 1 140 ? 12.132 -11.674 -0.762  1.00 14.93 ?  140 LEU   A HB3  1 
ATOM   3039 H  HG   . LEU   A 1 140 ? 12.285 -13.269 0.907   1.00 15.70 ?  140 LEU   A HG   1 
ATOM   3040 H  HD11 . LEU   A 1 140 ? 12.747 -12.650 3.132   1.00 16.18 ?  140 LEU   A HD11 1 
ATOM   3041 H  HD12 . LEU   A 1 140 ? 14.016 -12.487 2.191   1.00 16.18 ?  140 LEU   A HD12 1 
ATOM   3042 H  HD13 . LEU   A 1 140 ? 13.170 -11.210 2.613   1.00 16.18 ?  140 LEU   A HD13 1 
ATOM   3043 H  HD21 . LEU   A 1 140 ? 10.491 -12.608 2.215   1.00 16.65 ?  140 LEU   A HD21 1 
ATOM   3044 H  HD22 . LEU   A 1 140 ? 10.713 -11.097 1.775   1.00 16.65 ?  140 LEU   A HD22 1 
ATOM   3045 H  HD23 . LEU   A 1 140 ? 10.239 -12.175 0.707   1.00 16.65 ?  140 LEU   A HD23 1 
ATOM   3046 N  N    . ARG   A 1 141 ? 14.049 -13.639 -1.929  1.00 12.65 ?  141 ARG   A N    1 
ATOM   3047 C  CA   . ARG   A 1 141 ? 14.291 -15.031 -2.291  1.00 13.87 ?  141 ARG   A CA   1 
ATOM   3048 C  C    . ARG   A 1 141 ? 15.786 -15.338 -2.307  1.00 13.23 ?  141 ARG   A C    1 
ATOM   3049 O  O    . ARG   A 1 141 ? 16.236 -16.357 -1.765  1.00 13.52 ?  141 ARG   A O    1 
ATOM   3050 C  CB   . ARG   A 1 141 ? 13.674 -15.294 -3.665  1.00 15.37 ?  141 ARG   A CB   1 
ATOM   3051 C  CG   . ARG   A 1 141 ? 13.656 -16.746 -4.098  1.00 18.09 ?  141 ARG   A CG   1 
ATOM   3052 C  CD   . ARG   A 1 141 ? 12.620 -17.509 -3.325  1.00 20.66 ?  141 ARG   A CD   1 
ATOM   3053 N  NE   . ARG   A 1 141 ? 13.228 -18.315 -2.281  1.00 21.69 ?  141 ARG   A NE   1 
ATOM   3054 C  CZ   . ARG   A 1 141 ? 12.550 -18.888 -1.295  1.00 22.58 ?  141 ARG   A CZ   1 
ATOM   3055 N  NH1  . ARG   A 1 141 ? 11.263 -18.646 -1.108  1.00 21.63 ?  141 ARG   A NH1  1 
ATOM   3056 N  NH2  . ARG   A 1 141 ? 13.181 -19.721 -0.473  1.00 24.05 ?  141 ARG   A NH2  1 
ATOM   3057 H  H    . ARG   A 1 141 ? 13.651 -13.176 -2.534  1.00 15.18 ?  141 ARG   A H    1 
ATOM   3058 H  HA   . ARG   A 1 141 ? 13.868 -15.612 -1.643  1.00 16.64 ?  141 ARG   A HA   1 
ATOM   3059 H  HB2  . ARG   A 1 141 ? 12.757 -14.976 -3.657  1.00 18.44 ?  141 ARG   A HB2  1 
ATOM   3060 H  HB3  . ARG   A 1 141 ? 14.179 -14.799 -4.327  1.00 18.44 ?  141 ARG   A HB3  1 
ATOM   3061 H  HG2  . ARG   A 1 141 ? 13.439 -16.799 -5.044  1.00 21.71 ?  141 ARG   A HG2  1 
ATOM   3062 H  HG3  . ARG   A 1 141 ? 14.526 -17.148 -3.932  1.00 21.71 ?  141 ARG   A HG3  1 
ATOM   3063 H  HD2  . ARG   A 1 141 ? 12.009 -16.885 -2.901  1.00 24.80 ?  141 ARG   A HD2  1 
ATOM   3064 H  HD3  . ARG   A 1 141 ? 12.133 -18.093 -3.929  1.00 24.80 ?  141 ARG   A HD3  1 
ATOM   3065 H  HE   . ARG   A 1 141 ? 14.059 -18.518 -2.364  1.00 26.03 ?  141 ARG   A HE   1 
ATOM   3066 H  HH11 . ARG   A 1 141 ? 10.837 -18.121 -1.639  1.00 25.95 ?  141 ARG   A HH11 1 
ATOM   3067 H  HH12 . ARG   A 1 141 ? 10.842 -19.027 -0.458  1.00 25.95 ?  141 ARG   A HH12 1 
ATOM   3068 H  HH21 . ARG   A 1 141 ? 14.017 -19.884 -0.583  1.00 28.86 ?  141 ARG   A HH21 1 
ATOM   3069 H  HH22 . ARG   A 1 141 ? 12.754 -20.089 0.179   1.00 28.86 ?  141 ARG   A HH22 1 
ATOM   3070 N  N    . VAL   A 1 142 ? 16.578 -14.467 -2.938  1.00 12.48 ?  142 VAL   A N    1 
ATOM   3071 C  CA   . VAL   A 1 142 ? 18.023 -14.674 -2.967  1.00 12.55 ?  142 VAL   A CA   1 
ATOM   3072 C  C    . VAL   A 1 142 ? 18.590 -14.661 -1.554  1.00 11.78 ?  142 VAL   A C    1 
ATOM   3073 O  O    . VAL   A 1 142 ? 19.454 -15.475 -1.210  1.00 12.25 ?  142 VAL   A O    1 
ATOM   3074 C  CB   . VAL   A 1 142 ? 18.717 -13.651 -3.886  1.00 12.76 ?  142 VAL   A CB   1 
ATOM   3075 C  CG1  . VAL   A 1 142 ? 20.229 -13.855 -3.856  1.00 12.94 ?  142 VAL   A CG1  1 
ATOM   3076 C  CG2  . VAL   A 1 142 ? 18.223 -13.781 -5.311  1.00 14.44 ?  142 VAL   A CG2  1 
ATOM   3077 H  H    . VAL   A 1 142 ? 16.308 -13.754 -3.352  1.00 14.98 ?  142 VAL   A H    1 
ATOM   3078 H  HA   . VAL   A 1 142 ? 18.197 -15.545 -3.341  1.00 15.06 ?  142 VAL   A HA   1 
ATOM   3079 H  HB   . VAL   A 1 142 ? 18.532 -12.746 -3.579  1.00 15.31 ?  142 VAL   A HB   1 
ATOM   3080 H  HG11 . VAL   A 1 142 ? 20.634 -13.350 -4.583  1.00 15.53 ?  142 VAL   A HG11 1 
ATOM   3081 H  HG12 . VAL   A 1 142 ? 20.581 -13.540 -3.007  1.00 15.53 ?  142 VAL   A HG12 1 
ATOM   3082 H  HG13 . VAL   A 1 142 ? 20.423 -14.798 -3.967  1.00 15.53 ?  142 VAL   A HG13 1 
ATOM   3083 H  HG21 . VAL   A 1 142 ? 18.691 -13.137 -5.868  1.00 17.32 ?  142 VAL   A HG21 1 
ATOM   3084 H  HG22 . VAL   A 1 142 ? 18.406 -14.681 -5.621  1.00 17.32 ?  142 VAL   A HG22 1 
ATOM   3085 H  HG23 . VAL   A 1 142 ? 17.273 -13.607 -5.328  1.00 17.32 ?  142 VAL   A HG23 1 
ATOM   3086 N  N    . CYS   A 1 143 ? 18.119 -13.740 -0.713  1.00 11.79 ?  143 CYS   A N    1 
ATOM   3087 C  CA   . CYS   A 1 143 ? 18.584 -13.695 0.669   1.00 11.92 ?  143 CYS   A CA   1 
ATOM   3088 C  C    . CYS   A 1 143 ? 18.354 -15.034 1.364   1.00 12.08 ?  143 CYS   A C    1 
ATOM   3089 O  O    . CYS   A 1 143 ? 19.273 -15.614 1.948   1.00 12.20 ?  143 CYS   A O    1 
ATOM   3090 C  CB   . CYS   A 1 143 ? 17.858 -12.575 1.412   1.00 12.47 ?  143 CYS   A CB   1 
ATOM   3091 S  SG   . CYS   A 1 143 ? 18.344 -12.398 3.143   1.00 12.60 ?  143 CYS   A SG   1 
ATOM   3092 H  H    . CYS   A 1 143 ? 17.531 -13.146 -0.912  1.00 14.15 ?  143 CYS   A H    1 
ATOM   3093 H  HA   . CYS   A 1 143 ? 19.534 -13.512 0.681   1.00 14.31 ?  143 CYS   A HA   1 
ATOM   3094 H  HB2  . CYS   A 1 143 ? 18.037 -11.736 0.963   1.00 14.97 ?  143 CYS   A HB2  1 
ATOM   3095 H  HB3  . CYS   A 1 143 ? 16.906 -12.757 1.392   1.00 14.97 ?  143 CYS   A HB3  1 
ATOM   3096 H  HG   . CYS   A 1 143 ? 17.797 -11.431 3.595   1.00 15.12 ?  143 CYS   A HG   1 
ATOM   3097 N  N    . VAL   A 1 144 ? 17.121 -15.539 1.308   1.00 12.69 ?  144 VAL   A N    1 
ATOM   3098 C  CA   . VAL   A 1 144 ? 16.779 -16.775 2.003   1.00 13.72 ?  144 VAL   A CA   1 
ATOM   3099 C  C    . VAL   A 1 144 ? 17.599 -17.946 1.477   1.00 13.71 ?  144 VAL   A C    1 
ATOM   3100 O  O    . VAL   A 1 144 ? 17.964 -18.857 2.233   1.00 14.39 ?  144 VAL   A O    1 
ATOM   3101 C  CB   . VAL   A 1 144 ? 15.262 -17.021 1.875   1.00 16.80 ?  144 VAL   A CB   1 
ATOM   3102 C  CG1  . VAL   A 1 144 ? 14.904 -18.456 2.222   1.00 19.00 ?  144 VAL   A CG1  1 
ATOM   3103 C  CG2  . VAL   A 1 144 ? 14.506 -16.014 2.741   1.00 16.66 ?  144 VAL   A CG2  1 
ATOM   3104 H  H    . VAL   A 1 144 ? 16.463 -15.184 0.871   1.00 15.23 ?  144 VAL   A H    1 
ATOM   3105 H  HA   . VAL   A 1 144 ? 16.977 -16.668 2.941   1.00 16.47 ?  144 VAL   A HA   1 
ATOM   3106 H  HB   . VAL   A 1 144 ? 14.996 -16.865 0.951   1.00 20.16 ?  144 VAL   A HB   1 
ATOM   3107 H  HG11 . VAL   A 1 144 ? 13.953 -18.505 2.411   1.00 22.80 ?  144 VAL   A HG11 1 
ATOM   3108 H  HG12 . VAL   A 1 144 ? 15.120 -19.027 1.469   1.00 22.80 ?  144 VAL   A HG12 1 
ATOM   3109 H  HG13 . VAL   A 1 144 ? 15.410 -18.723 3.003   1.00 22.80 ?  144 VAL   A HG13 1 
ATOM   3110 H  HG21 . VAL   A 1 144 ? 13.550 -16.185 2.671   1.00 19.99 ?  144 VAL   A HG21 1 
ATOM   3111 H  HG22 . VAL   A 1 144 ? 14.789 -16.109 3.662   1.00 19.99 ?  144 VAL   A HG22 1 
ATOM   3112 H  HG23 . VAL   A 1 144 ? 14.697 -15.113 2.428   1.00 19.99 ?  144 VAL   A HG23 1 
ATOM   3113 N  N    . ASP   A 1 145 ? 17.863 -17.966 0.174   1.00 13.86 ?  145 ASP   A N    1 
ATOM   3114 C  CA   . ASP   A 1 145 ? 18.580 -19.068 -0.456  1.00 14.56 ?  145 ASP   A CA   1 
ATOM   3115 C  C    . ASP   A 1 145 ? 20.100 -18.916 -0.406  1.00 14.37 ?  145 ASP   A C    1 
ATOM   3116 O  O    . ASP   A 1 145 ? 20.807 -19.813 -0.882  1.00 16.16 ?  145 ASP   A O    1 
ATOM   3117 C  CB   . ASP   A 1 145 ? 18.138 -19.212 -1.915  1.00 16.26 ?  145 ASP   A CB   1 
ATOM   3118 C  CG   . ASP   A 1 145 ? 16.686 -19.650 -2.052  1.00 18.47 ?  145 ASP   A CG   1 
ATOM   3119 O  OD1  . ASP   A 1 145 ? 16.113 -20.196 -1.084  1.00 18.80 ?  145 ASP   A OD1  1 
ATOM   3120 O  OD2  . ASP   A 1 145 ? 16.118 -19.440 -3.140  1.00 20.00 -1 145 ASP   A OD2  1 
ATOM   3121 H  H    . ASP   A 1 145 ? 17.620 -17.350 -0.380  1.00 16.64 ?  145 ASP   A H    1 
ATOM   3122 H  HA   . ASP   A 1 145 ? 18.347 -19.890 0.002   1.00 17.48 ?  145 ASP   A HA   1 
ATOM   3123 H  HB2  . ASP   A 1 145 ? 18.246 -18.358 -2.362  1.00 19.51 ?  145 ASP   A HB2  1 
ATOM   3124 H  HB3  . ASP   A 1 145 ? 18.689 -19.884 -2.345  1.00 19.51 ?  145 ASP   A HB3  1 
ATOM   3125 N  N    . THR   A 1 146 ? 20.621 -17.822 0.141   1.00 12.78 ?  146 THR   A N    1 
ATOM   3126 C  CA   . THR   A 1 146 ? 22.061 -17.567 0.163   1.00 12.54 ?  146 THR   A CA   1 
ATOM   3127 C  C    . THR   A 1 146 ? 22.616 -17.382 1.563   1.00 12.25 ?  146 THR   A C    1 
ATOM   3128 O  O    . THR   A 1 146 ? 23.693 -17.912 1.875   1.00 13.40 ?  146 THR   A O    1 
ATOM   3129 C  CB   . THR   A 1 146 ? 22.389 -16.317 -0.674  1.00 12.56 ?  146 THR   A CB   1 
ATOM   3130 O  OG1  . THR   A 1 146 ? 21.867 -16.481 -1.996  1.00 13.08 ?  146 THR   A OG1  1 
ATOM   3131 C  CG2  . THR   A 1 146 ? 23.888 -16.092 -0.754  1.00 13.13 ?  146 THR   A CG2  1 
ATOM   3132 H  H    . THR   A 1 146 ? 20.155 -17.196 0.507   1.00 15.34 ?  146 THR   A H    1 
ATOM   3133 H  HA   . THR   A 1 146 ? 22.523 -18.316 -0.237  1.00 15.05 ?  146 THR   A HA   1 
ATOM   3134 H  HB   . THR   A 1 146 ? 21.989 -15.536 -0.258  1.00 15.07 ?  146 THR   A HB   1 
ATOM   3135 H  HG1  . THR   A 1 146 ? 21.031 -16.553 -1.963  1.00 15.69 ?  146 THR   A HG1  1 
ATOM   3136 H  HG21 . THR   A 1 146 ? 24.084 -15.433 -1.437  1.00 15.76 ?  146 THR   A HG21 1 
ATOM   3137 H  HG22 . THR   A 1 146 ? 24.223 -15.772 0.098   1.00 15.76 ?  146 THR   A HG22 1 
ATOM   3138 H  HG23 . THR   A 1 146 ? 24.333 -16.923 -0.979  1.00 15.76 ?  146 THR   A HG23 1 
ATOM   3139 N  N    . VAL   A 1 147 ? 21.931 -16.610 2.401   1.00 12.27 ?  147 VAL   A N    1 
ATOM   3140 C  CA   . VAL   A 1 147 ? 22.417 -16.310 3.739   1.00 12.23 ?  147 VAL   A CA   1 
ATOM   3141 C  C    . VAL   A 1 147 ? 22.101 -17.479 4.660   1.00 12.51 ?  147 VAL   A C    1 
ATOM   3142 O  O    . VAL   A 1 147 ? 20.960 -17.956 4.713   1.00 13.20 ?  147 VAL   A O    1 
ATOM   3143 C  CB   . VAL   A 1 147 ? 21.798 -15.001 4.253   1.00 12.14 ?  147 VAL   A CB   1 
ATOM   3144 C  CG1  . VAL   A 1 147 ? 22.338 -14.680 5.629   1.00 13.31 ?  147 VAL   A CG1  1 
ATOM   3145 C  CG2  . VAL   A 1 147 ? 22.060 -13.867 3.275   1.00 12.45 ?  147 VAL   A CG2  1 
ATOM   3146 H  H    . VAL   A 1 147 ? 21.170 -16.250 2.219   1.00 14.72 ?  147 VAL   A H    1 
ATOM   3147 H  HA   . VAL   A 1 147 ? 23.380 -16.201 3.707   1.00 14.68 ?  147 VAL   A HA   1 
ATOM   3148 H  HB   . VAL   A 1 147 ? 20.841 -15.119 4.330   1.00 14.56 ?  147 VAL   A HB   1 
ATOM   3149 H  HG11 . VAL   A 1 147 ? 22.083 -13.778 5.862   1.00 15.98 ?  147 VAL   A HG11 1 
ATOM   3150 H  HG12 . VAL   A 1 147 ? 21.965 -15.308 6.270   1.00 15.98 ?  147 VAL   A HG12 1 
ATOM   3151 H  HG13 . VAL   A 1 147 ? 23.306 -14.760 5.614   1.00 15.98 ?  147 VAL   A HG13 1 
ATOM   3152 H  HG21 . VAL   A 1 147 ? 21.745 -13.039 3.669   1.00 14.94 ?  147 VAL   A HG21 1 
ATOM   3153 H  HG22 . VAL   A 1 147 ? 23.010 -13.814 3.102   1.00 14.94 ?  147 VAL   A HG22 1 
ATOM   3154 H  HG23 . VAL   A 1 147 ? 21.580 -14.046 2.452   1.00 14.94 ?  147 VAL   A HG23 1 
ATOM   3155 N  N    . ARG   A 1 148 ? 23.120 -17.945 5.380   1.00 12.71 ?  148 ARG   A N    1 
ATOM   3156 C  CA   . ARG   A 1 148 ? 22.992 -19.020 6.348   1.00 13.16 ?  148 ARG   A CA   1 
ATOM   3157 C  C    . ARG   A 1 148 ? 23.110 -18.543 7.783   1.00 13.36 ?  148 ARG   A C    1 
ATOM   3158 O  O    . ARG   A 1 148 ? 22.700 -19.267 8.697   1.00 14.91 ?  148 ARG   A O    1 
ATOM   3159 C  CB   . ARG   A 1 148 ? 24.042 -20.109 6.078   1.00 13.69 ?  148 ARG   A CB   1 
ATOM   3160 C  CG   . ARG   A 1 148 ? 23.881 -20.757 4.714   1.00 14.69 ?  148 ARG   A CG   1 
ATOM   3161 C  CD   . ARG   A 1 148 ? 24.965 -21.793 4.428   1.00 15.79 ?  148 ARG   A CD   1 
ATOM   3162 N  NE   . ARG   A 1 148 ? 26.307 -21.218 4.451   1.00 15.90 ?  148 ARG   A NE   1 
ATOM   3163 C  CZ   . ARG   A 1 148 ? 26.820 -20.479 3.475   1.00 15.05 ?  148 ARG   A CZ   1 
ATOM   3164 N  NH1  . ARG   A 1 148 ? 26.150 -20.246 2.359   1.00 15.36 ?  148 ARG   A NH1  1 
ATOM   3165 N  NH2  . ARG   A 1 148 ? 28.039 -19.956 3.622   1.00 15.31 ?  148 ARG   A NH2  1 
ATOM   3166 H  H    . ARG   A 1 148 ? 23.924 -17.637 5.312   1.00 15.25 ?  148 ARG   A H    1 
ATOM   3167 H  HA   . ARG   A 1 148 ? 22.123 -19.423 6.245   1.00 15.79 ?  148 ARG   A HA   1 
ATOM   3168 H  HB2  . ARG   A 1 148 ? 24.928 -19.727 6.122   1.00 16.43 ?  148 ARG   A HB2  1 
ATOM   3169 H  HB3  . ARG   A 1 148 ? 23.948 -20.812 6.744   1.00 16.43 ?  148 ARG   A HB3  1 
ATOM   3170 H  HG2  . ARG   A 1 148 ? 23.017 -21.192 4.674   1.00 17.63 ?  148 ARG   A HG2  1 
ATOM   3171 H  HG3  . ARG   A 1 148 ? 23.934 -20.060 4.036   1.00 17.63 ?  148 ARG   A HG3  1 
ATOM   3172 H  HD2  . ARG   A 1 148 ? 24.923 -22.484 5.104   1.00 18.95 ?  148 ARG   A HD2  1 
ATOM   3173 H  HD3  . ARG   A 1 148 ? 24.811 -22.171 3.549   1.00 18.95 ?  148 ARG   A HD3  1 
ATOM   3174 H  HE   . ARG   A 1 148 ? 26.793 -21.359 5.141   1.00 19.08 ?  148 ARG   A HE   1 
ATOM   3175 H  HH11 . ARG   A 1 148 ? 25.360 -20.563 2.251   1.00 18.44 ?  148 ARG   A HH11 1 
ATOM   3176 H  HH12 . ARG   A 1 148 ? 26.503 -19.756 1.741   1.00 18.44 ?  148 ARG   A HH12 1 
ATOM   3177 H  HH21 . ARG   A 1 148 ? 28.481 -20.095 4.342   1.00 18.38 ?  148 ARG   A HH21 1 
ATOM   3178 H  HH22 . ARG   A 1 148 ? 28.378 -19.473 2.993   1.00 18.38 ?  148 ARG   A HH22 1 
ATOM   3179 N  N    . THR   A 1 149 ? 23.653 -17.347 7.996   1.00 13.21 ?  149 THR   A N    1 
ATOM   3180 C  CA   . THR   A 1 149 ? 23.722 -16.744 9.313   1.00 13.42 ?  149 THR   A CA   1 
ATOM   3181 C  C    . THR   A 1 149 ? 22.394 -16.050 9.619   1.00 13.08 ?  149 THR   A C    1 
ATOM   3182 O  O    . THR   A 1 149 ? 21.466 -16.036 8.803   1.00 13.78 ?  149 THR   A O    1 
ATOM   3183 C  CB   . THR   A 1 149 ? 24.922 -15.807 9.374   1.00 13.99 ?  149 THR   A CB   1 
ATOM   3184 O  OG1  . THR   A 1 149 ? 24.808 -14.876 8.295   1.00 13.80 ?  149 THR   A OG1  1 
ATOM   3185 C  CG2  . THR   A 1 149 ? 26.233 -16.604 9.264   1.00 14.80 ?  149 THR   A CG2  1 
ATOM   3186 H  H    . THR   A 1 149 ? 23.997 -16.855 7.375   1.00 15.85 ?  149 THR   A H    1 
ATOM   3187 H  HA   . THR   A 1 149 ? 23.846 -17.444 9.970   1.00 16.11 ?  149 THR   A HA   1 
ATOM   3188 H  HB   . THR   A 1 149 ? 24.910 -15.330 10.216  1.00 16.79 ?  149 THR   A HB   1 
ATOM   3189 H  HG1  . THR   A 1 149 ? 25.461 -14.347 8.300   1.00 16.56 ?  149 THR   A HG1  1 
ATOM   3190 H  HG21 . THR   A 1 149 ? 26.992 -16.007 9.321   1.00 17.76 ?  149 THR   A HG21 1 
ATOM   3191 H  HG22 . THR   A 1 149 ? 26.290 -17.255 9.985   1.00 17.76 ?  149 THR   A HG22 1 
ATOM   3192 H  HG23 . THR   A 1 149 ? 26.268 -17.079 8.416   1.00 17.76 ?  149 THR   A HG23 1 
ATOM   3193 N  N    . ASN   A 1 150 ? 22.270 -15.509 10.824  1.00 13.47 ?  150 ASN   A N    1 
ATOM   3194 C  CA   . ASN   A 1 150 ? 20.986 -14.991 11.298  1.00 13.89 ?  150 ASN   A CA   1 
ATOM   3195 C  C    . ASN   A 1 150 ? 20.812 -13.552 10.830  1.00 12.79 ?  150 ASN   A C    1 
ATOM   3196 O  O    . ASN   A 1 150 ? 21.566 -12.659 11.237  1.00 14.33 ?  150 ASN   A O    1 
ATOM   3197 C  CB   . ASN   A 1 150 ? 20.913 -15.104 12.816  1.00 16.56 ?  150 ASN   A CB   1 
ATOM   3198 C  CG   . ASN   A 1 150 ? 20.822 -16.537 13.276  1.00 20.70 ?  150 ASN   A CG   1 
ATOM   3199 O  OD1  . ASN   A 1 150 ? 20.205 -17.367 12.608  1.00 21.96 ?  150 ASN   A OD1  1 
ATOM   3200 N  ND2  . ASN   A 1 150 ? 21.447 -16.846 14.409  1.00 22.97 ?  150 ASN   A ND2  1 
ATOM   3201 H  H    . ASN   A 1 150 ? 22.912 -15.432 11.391  1.00 16.16 ?  150 ASN   A H    1 
ATOM   3202 H  HA   . ASN   A 1 150 ? 20.267 -15.530 10.925  1.00 16.67 ?  150 ASN   A HA   1 
ATOM   3203 H  HB2  . ASN   A 1 150 ? 21.709 -14.715 13.205  1.00 19.88 ?  150 ASN   A HB2  1 
ATOM   3204 H  HB3  . ASN   A 1 150 ? 20.122 -14.644 13.135  1.00 19.88 ?  150 ASN   A HB3  1 
ATOM   3205 H  HD21 . ASN   A 1 150 ? 21.431 -17.655 14.714  1.00 27.57 ?  150 ASN   A HD21 1 
ATOM   3206 H  HD22 . ASN   A 1 150 ? 21.869 -16.238 14.849  1.00 27.57 ?  150 ASN   A HD22 1 
ATOM   3207 N  N    . VAL   A 1 151 ? 19.824 -13.323 9.972   1.00 12.36 ?  151 VAL   A N    1 
ATOM   3208 C  CA   . VAL   A 1 151 ? 19.614 -12.018 9.362   1.00 12.58 ?  151 VAL   A CA   1 
ATOM   3209 C  C    . VAL   A 1 151 ? 18.226 -11.501 9.718   1.00 12.59 ?  151 VAL   A C    1 
ATOM   3210 O  O    . VAL   A 1 151 ? 17.220 -12.213 9.570   1.00 13.73 ?  151 VAL   A O    1 
ATOM   3211 C  CB   . VAL   A 1 151 ? 19.901 -12.026 7.845   1.00 14.12 ?  151 VAL   A CB   1 
ATOM   3212 C  CG1  . VAL   A 1 151 ? 19.080 -13.071 7.111   1.00 15.15 ?  151 VAL   A CG1  1 
ATOM   3213 C  CG2  . VAL   A 1 151 ? 19.705 -10.627 7.248   1.00 14.47 ?  151 VAL   A CG2  1 
ATOM   3214 H  H    . VAL   A 1 151 ? 19.254 -13.922 9.725   1.00 14.83 ?  151 VAL   A H    1 
ATOM   3215 H  HA   . VAL   A 1 151 ? 20.256 -11.406 9.753   1.00 15.09 ?  151 VAL   A HA   1 
ATOM   3216 H  HB   . VAL   A 1 151 ? 20.837 -12.261 7.712   1.00 16.94 ?  151 VAL   A HB   1 
ATOM   3217 H  HG11 . VAL   A 1 151 ? 19.270 -13.025 6.160   1.00 18.18 ?  151 VAL   A HG11 1 
ATOM   3218 H  HG12 . VAL   A 1 151 ? 19.315 -13.956 7.446   1.00 18.18 ?  151 VAL   A HG12 1 
ATOM   3219 H  HG13 . VAL   A 1 151 ? 18.137 -12.905 7.266   1.00 18.18 ?  151 VAL   A HG13 1 
ATOM   3220 H  HG21 . VAL   A 1 151 ? 20.019 -10.630 6.327   1.00 17.36 ?  151 VAL   A HG21 1 
ATOM   3221 H  HG22 . VAL   A 1 151 ? 18.763 -10.402 7.272   1.00 17.36 ?  151 VAL   A HG22 1 
ATOM   3222 H  HG23 . VAL   A 1 151 ? 20.216 -9.988  7.766   1.00 17.36 ?  151 VAL   A HG23 1 
ATOM   3223 N  N    . TYR   A 1 152 ? 18.201 -10.256 10.196  1.00 12.51 ?  152 TYR   A N    1 
ATOM   3224 C  CA   . TYR   A 1 152 ? 17.003 -9.525  10.573  1.00 12.59 ?  152 TYR   A CA   1 
ATOM   3225 C  C    . TYR   A 1 152 ? 16.814 -8.427  9.538   1.00 11.57 ?  152 TYR   A C    1 
ATOM   3226 O  O    . TYR   A 1 152 ? 17.592 -7.467  9.492   1.00 11.99 ?  152 TYR   A O    1 
ATOM   3227 C  CB   . TYR   A 1 152 ? 17.172 -8.975  11.986  1.00 13.32 ?  152 TYR   A CB   1 
ATOM   3228 C  CG   . TYR   A 1 152 ? 17.127 -10.092 12.991  1.00 13.87 ?  152 TYR   A CG   1 
ATOM   3229 C  CD1  . TYR   A 1 152 ? 18.260 -10.841 13.281  1.00 15.30 ?  152 TYR   A CD1  1 
ATOM   3230 C  CD2  . TYR   A 1 152 ? 15.939 -10.440 13.611  1.00 14.28 ?  152 TYR   A CD2  1 
ATOM   3231 C  CE1  . TYR   A 1 152 ? 18.212 -11.895 14.176  1.00 16.65 ?  152 TYR   A CE1  1 
ATOM   3232 C  CE2  . TYR   A 1 152 ? 15.879 -11.495 14.510  1.00 15.68 ?  152 TYR   A CE2  1 
ATOM   3233 C  CZ   . TYR   A 1 152 ? 17.020 -12.219 14.791  1.00 16.53 ?  152 TYR   A CZ   1 
ATOM   3234 O  OH   . TYR   A 1 152 ? 16.970 -13.274 15.680  1.00 19.17 ?  152 TYR   A OH   1 
ATOM   3235 H  H    . TYR   A 1 152 ? 18.923 -9.785  10.299  1.00 15.02 ?  152 TYR   A H    1 
ATOM   3236 H  HA   . TYR   A 1 152 ? 16.242 -10.120 10.550  1.00 15.11 ?  152 TYR   A HA   1 
ATOM   3237 H  HB2  . TYR   A 1 152 ? 18.035 -8.534  12.055  1.00 15.99 ?  152 TYR   A HB2  1 
ATOM   3238 H  HB3  . TYR   A 1 152 ? 16.457 -8.356  12.175  1.00 15.99 ?  152 TYR   A HB3  1 
ATOM   3239 H  HD1  . TYR   A 1 152 ? 19.064 -10.629 12.862  1.00 18.36 ?  152 TYR   A HD1  1 
ATOM   3240 H  HD2  . TYR   A 1 152 ? 15.164 -9.955  13.416  1.00 17.14 ?  152 TYR   A HD2  1 
ATOM   3241 H  HE1  . TYR   A 1 152 ? 18.979 -12.378 14.364  1.00 19.99 ?  152 TYR   A HE1  1 
ATOM   3242 H  HE2  . TYR   A 1 152 ? 15.073 -11.704 14.921  1.00 18.81 ?  152 TYR   A HE2  1 
ATOM   3243 H  HH   . TYR   A 1 152 ? 16.190 -13.345 15.985  1.00 23.00 ?  152 TYR   A HH   1 
ATOM   3244 N  N    A LEU   A 1 153 ? 15.811 -8.606  8.678   0.64 11.81 ?  153 LEU   A N    1 
ATOM   3245 N  N    B LEU   A 1 153 ? 15.767 -8.546  8.728   0.36 11.53 ?  153 LEU   A N    1 
ATOM   3246 C  CA   A LEU   A 1 153 ? 15.555 -7.729  7.543   0.64 11.86 ?  153 LEU   A CA   1 
ATOM   3247 C  CA   B LEU   A 1 153 ? 15.522 -7.633  7.620   0.36 11.37 ?  153 LEU   A CA   1 
ATOM   3248 C  C    A LEU   A 1 153 ? 14.569 -6.636  7.932   0.64 12.29 ?  153 LEU   A C    1 
ATOM   3249 C  C    B LEU   A 1 153 ? 14.513 -6.568  8.028   0.36 11.65 ?  153 LEU   A C    1 
ATOM   3250 O  O    A LEU   A 1 153 ? 13.449 -6.927  8.367   0.64 13.68 ?  153 LEU   A O    1 
ATOM   3251 O  O    B LEU   A 1 153 ? 13.439 -6.889  8.550   0.36 12.49 ?  153 LEU   A O    1 
ATOM   3252 C  CB   A LEU   A 1 153 ? 14.982 -8.527  6.373   0.64 12.07 ?  153 LEU   A CB   1 
ATOM   3253 C  CB   B LEU   A 1 153 ? 14.995 -8.398  6.405   0.36 11.68 ?  153 LEU   A CB   1 
ATOM   3254 C  CG   A LEU   A 1 153 ? 15.934 -9.512  5.696   0.64 11.86 ?  153 LEU   A CG   1 
ATOM   3255 C  CG   B LEU   A 1 153 ? 15.933 -9.445  5.803   0.36 12.05 ?  153 LEU   A CG   1 
ATOM   3256 C  CD1  A LEU   A 1 153 ? 15.153 -10.440 4.775   0.64 12.14 ?  153 LEU   A CD1  1 
ATOM   3257 C  CD1  B LEU   A 1 153 ? 15.202 -10.243 4.729   0.36 12.76 ?  153 LEU   A CD1  1 
ATOM   3258 C  CD2  A LEU   A 1 153 ? 17.000 -8.752  4.925   0.64 11.91 ?  153 LEU   A CD2  1 
ATOM   3259 C  CD2  B LEU   A 1 153 ? 17.182 -8.784  5.236   0.36 11.98 ?  153 LEU   A CD2  1 
ATOM   3260 H  H    A LEU   A 1 153 ? 15.251 -9.262  8.736   0.64 14.17 ?  153 LEU   A H    1 
ATOM   3261 H  H    B LEU   A 1 153 ? 15.164 -9.158  8.811   0.36 13.84 ?  153 LEU   A H    1 
ATOM   3262 H  HA   A LEU   A 1 153 ? 16.382 -7.319  7.264   0.64 14.23 ?  153 LEU   A HA   1 
ATOM   3263 H  HA   B LEU   A 1 153 ? 16.349 -7.199  7.375   0.36 13.65 ?  153 LEU   A HA   1 
ATOM   3264 H  HB2  A LEU   A 1 153 ? 14.215 -9.035  6.695   0.64 14.48 ?  153 LEU   A HB2  1 
ATOM   3265 H  HB2  B LEU   A 1 153 ? 14.181 -8.859  6.668   0.36 14.01 ?  153 LEU   A HB2  1 
ATOM   3266 H  HB3  A LEU   A 1 153 ? 14.683 -7.899  5.695   0.64 14.48 ?  153 LEU   A HB3  1 
ATOM   3267 H  HB3  B LEU   A 1 153 ? 14.791 -7.758  5.708   0.36 14.01 ?  153 LEU   A HB3  1 
ATOM   3268 H  HG   A LEU   A 1 153 ? 16.371 -10.052 6.379   0.64 14.23 ?  153 LEU   A HG   1 
ATOM   3269 H  HG   B LEU   A 1 153 ? 16.210 -10.061 6.501   0.36 14.46 ?  153 LEU   A HG   1 
ATOM   3270 H  HD11 A LEU   A 1 153 ? 15.753 -11.115 4.427   0.64 14.57 ?  153 LEU   A HD11 1 
ATOM   3271 H  HD11 B LEU   A 1 153 ? 15.768 -10.972 4.434   0.36 15.31 ?  153 LEU   A HD11 1 
ATOM   3272 H  HD12 A LEU   A 1 153 ? 14.438 -10.856 5.277   0.64 14.57 ?  153 LEU   A HD12 1 
ATOM   3273 H  HD12 B LEU   A 1 153 ? 14.379 -10.595 5.104   0.36 15.31 ?  153 LEU   A HD12 1 
ATOM   3274 H  HD13 A LEU   A 1 153 ? 14.785 -9.915  4.046   0.64 14.57 ?  153 LEU   A HD13 1 
ATOM   3275 H  HD13 B LEU   A 1 153 ? 14.999 -9.656  3.983   0.36 15.31 ?  153 LEU   A HD13 1 
ATOM   3276 H  HD21 A LEU   A 1 153 ? 17.563 -9.389  4.467   0.64 14.29 ?  153 LEU   A HD21 1 
ATOM   3277 H  HD21 B LEU   A 1 153 ? 17.718 -9.456  4.790   0.36 14.38 ?  153 LEU   A HD21 1 
ATOM   3278 H  HD22 A LEU   A 1 153 ? 16.561 -8.170  4.287   0.64 14.29 ?  153 LEU   A HD22 1 
ATOM   3279 H  HD22 B LEU   A 1 153 ? 16.914 -8.098  4.606   0.36 14.38 ?  153 LEU   A HD22 1 
ATOM   3280 H  HD23 A LEU   A 1 153 ? 17.524 -8.229  5.549   0.64 14.29 ?  153 LEU   A HD23 1 
ATOM   3281 H  HD23 B LEU   A 1 153 ? 17.686 -8.387  5.964   0.36 14.38 ?  153 LEU   A HD23 1 
ATOM   3282 N  N    A ALA   A 1 154 ? 14.978 -5.389  7.736   0.64 12.38 ?  154 ALA   A N    1 
ATOM   3283 N  N    B ALA   A 1 154 ? 14.863 -5.303  7.789   0.36 11.41 ?  154 ALA   A N    1 
ATOM   3284 C  CA   A ALA   A 1 154 ? 14.144 -4.222  7.980   0.64 12.79 ?  154 ALA   A CA   1 
ATOM   3285 C  CA   B ALA   A 1 154 ? 13.968 -4.168  7.992   0.36 11.93 ?  154 ALA   A CA   1 
ATOM   3286 C  C    A ALA   A 1 154 ? 13.637 -3.713  6.641   0.64 12.38 ?  154 ALA   A C    1 
ATOM   3287 C  C    B ALA   A 1 154 ? 13.523 -3.661  6.624   0.36 11.86 ?  154 ALA   A C    1 
ATOM   3288 O  O    A ALA   A 1 154 ? 14.433 -3.417  5.743   0.64 12.97 ?  154 ALA   A O    1 
ATOM   3289 O  O    B ALA   A 1 154 ? 14.338 -3.144  5.853   0.36 12.15 ?  154 ALA   A O    1 
ATOM   3290 C  CB   A ALA   A 1 154 ? 14.950 -3.127  8.676   0.64 13.38 ?  154 ALA   A CB   1 
ATOM   3291 C  CB   B ALA   A 1 154 ? 14.674 -3.060  8.770   0.36 12.42 ?  154 ALA   A CB   1 
ATOM   3292 H  H    A ALA   A 1 154 ? 15.759 -5.191  7.435   0.64 14.86 ?  154 ALA   A H    1 
ATOM   3293 H  H    B ALA   A 1 154 ? 15.649 -5.068  7.512   0.36 13.70 ?  154 ALA   A H    1 
ATOM   3294 H  HA   A ALA   A 1 154 ? 13.384 -4.465  8.534   0.64 15.35 ?  154 ALA   A HA   1 
ATOM   3295 H  HA   B ALA   A 1 154 ? 13.189 -4.456  8.495   0.36 14.31 ?  154 ALA   A HA   1 
ATOM   3296 H  HB1  A ALA   A 1 154 ? 14.375 -2.362  8.825   0.64 16.05 ?  154 ALA   A HB1  1 
ATOM   3297 H  HB1  B ALA   A 1 154 ? 14.057 -2.322  8.892   0.36 14.90 ?  154 ALA   A HB1  1 
ATOM   3298 H  HB2  A ALA   A 1 154 ? 15.278 -3.470  9.520   0.64 16.05 ?  154 ALA   A HB2  1 
ATOM   3299 H  HB2  B ALA   A 1 154 ? 14.953 -3.405  9.633   0.36 14.90 ?  154 ALA   A HB2  1 
ATOM   3300 H  HB3  A ALA   A 1 154 ? 15.694 -2.877  8.105   0.64 16.05 ?  154 ALA   A HB3  1 
ATOM   3301 H  HB3  B ALA   A 1 154 ? 15.448 -2.765  8.265   0.36 14.90 ?  154 ALA   A HB3  1 
ATOM   3302 N  N    A VAL   A 1 155 ? 12.315 -3.615  6.516   0.34 10.58 ?  155 VAL   A N    1 
ATOM   3303 N  N    B VAL   A 1 155 ? 12.232 -3.807  6.332   0.36 10.77 ?  155 VAL   A N    1 
ATOM   3304 C  CA   A VAL   A 1 155 ? 11.648 -3.145  5.308   0.34 11.89 ?  155 VAL   A CA   1 
ATOM   3305 C  CA   B VAL   A 1 155 ? 11.643 -3.404  5.058   0.36 11.99 ?  155 VAL   A CA   1 
ATOM   3306 C  CA   T VAL   A 1 155 ? 11.634 -3.258  5.317   0.30 14.20 ?  155 VAL   A CA   1 
ATOM   3307 C  C    A VAL   A 1 155 ? 10.931 -1.854  5.672   0.34 12.61 ?  155 VAL   A C    1 
ATOM   3308 C  C    B VAL   A 1 155 ? 10.946 -2.064  5.250   0.36 12.55 ?  155 VAL   A C    1 
ATOM   3309 C  C    T VAL   A 1 155 ? 11.041 -1.886  5.645   0.30 13.80 ?  155 VAL   A C    1 
ATOM   3310 O  O    A VAL   A 1 155 ? 9.980  -1.867  6.463   0.34 13.51 ?  155 VAL   A O    1 
ATOM   3311 O  O    B VAL   A 1 155 ? 10.059 -1.931  6.101   0.36 13.21 ?  155 VAL   A O    1 
ATOM   3312 O  O    T VAL   A 1 155 ? 10.200 -1.757  6.536   0.30 14.11 ?  155 VAL   A O    1 
ATOM   3313 C  CB   A VAL   A 1 155 ? 10.664 -4.187  4.762   0.34 12.60 ?  155 VAL   A CB   1 
ATOM   3314 C  CB   B VAL   A 1 155 ? 10.670 -4.470  4.533   0.36 12.28 ?  155 VAL   A CB   1 
ATOM   3315 C  CB   T VAL   A 1 155 ? 10.580 -4.244  4.768   0.30 14.52 ?  155 VAL   A CB   1 
ATOM   3316 C  CG1  A VAL   A 1 155 ? 9.939  -3.645  3.541   0.34 12.85 ?  155 VAL   A CG1  1 
ATOM   3317 C  CG1  B VAL   A 1 155 ? 10.018 -4.012  3.228   0.36 12.30 ?  155 VAL   A CG1  1 
ATOM   3318 C  CG1  T VAL   A 1 155 ? 9.879  -3.657  3.555   0.30 14.69 ?  155 VAL   A CG1  1 
ATOM   3319 C  CG2  A VAL   A 1 155 ? 11.398 -5.482  4.437   0.34 13.36 ?  155 VAL   A CG2  1 
ATOM   3320 C  CG2  B VAL   A 1 155 ? 11.404 -5.788  4.345   0.36 13.10 ?  155 VAL   A CG2  1 
ATOM   3321 C  CG2  T VAL   A 1 155 ? 11.232 -5.582  4.418   0.30 14.87 ?  155 VAL   A CG2  1 
ATOM   3322 H  H    A VAL   A 1 155 ? 11.762 -3.821  7.145   0.34 12.70 ?  155 VAL   A H    1 
ATOM   3323 H  H    B VAL   A 1 155 ? 11.662 -4.167  6.870   0.36 12.93 ?  155 VAL   A H    1 
ATOM   3324 H  HA   A VAL   A 1 155 ? 12.309 -2.950  4.626   0.34 14.27 ?  155 VAL   A HA   1 
ATOM   3325 H  HA   B VAL   A 1 155 ? 12.345 -3.289  4.401   0.36 14.38 ?  155 VAL   A HA   1 
ATOM   3326 H  HB   A VAL   A 1 155 ? 10.003 -4.382  5.445   0.34 15.13 ?  155 VAL   A HB   1 
ATOM   3327 H  HB   B VAL   A 1 155 ? 9.966  -4.614  5.188   0.36 14.74 ?  155 VAL   A HB   1 
ATOM   3328 H  HB   T VAL   A 1 155 ? 9.914  -4.408  5.453   0.30 17.42 ?  155 VAL   A HB   1 
ATOM   3329 H  HG11 A VAL   A 1 155 ? 9.471  -4.374  3.107   0.34 15.42 ?  155 VAL   A HG11 1 
ATOM   3330 H  HG11 B VAL   A 1 155 ? 9.420  -4.705  2.912   0.36 14.76 ?  155 VAL   A HG11 1 
ATOM   3331 H  HG11 T VAL   A 1 155 ? 9.359  -4.353  3.124   0.30 17.63 ?  155 VAL   A HG11 1 
ATOM   3332 H  HG12 A VAL   A 1 155 ? 9.305  -2.967  3.825   0.34 15.42 ?  155 VAL   A HG12 1 
ATOM   3333 H  HG12 B VAL   A 1 155 ? 9.512  -3.200  3.388   0.36 14.76 ?  155 VAL   A HG12 1 
ATOM   3334 H  HG12 T VAL   A 1 155 ? 9.294  -2.940  3.844   0.30 17.63 ?  155 VAL   A HG12 1 
ATOM   3335 H  HG13 A VAL   A 1 155 ? 10.589 -3.260  2.934   0.34 15.42 ?  155 VAL   A HG13 1 
ATOM   3336 H  HG13 B VAL   A 1 155 ? 10.711 -3.847  2.571   0.36 14.76 ?  155 VAL   A HG13 1 
ATOM   3337 H  HG13 T VAL   A 1 155 ? 10.546 -3.315  2.940   0.30 17.63 ?  155 VAL   A HG13 1 
ATOM   3338 H  HG21 A VAL   A 1 155 ? 10.770 -6.111  4.050   0.34 16.03 ?  155 VAL   A HG21 1 
ATOM   3339 H  HG21 B VAL   A 1 155 ? 10.869 -6.369  3.787   0.36 15.72 ?  155 VAL   A HG21 1 
ATOM   3340 H  HG21 T VAL   A 1 155 ? 10.553 -6.187  4.080   0.30 17.84 ?  155 VAL   A HG21 1 
ATOM   3341 H  HG22 A VAL   A 1 155 ? 12.108 -5.291  3.804   0.34 16.03 ?  155 VAL   A HG22 1 
ATOM   3342 H  HG22 B VAL   A 1 155 ? 12.258 -5.612  3.918   0.36 15.72 ?  155 VAL   A HG22 1 
ATOM   3343 H  HG22 T VAL   A 1 155 ? 11.910 -5.435  3.739   0.30 17.84 ?  155 VAL   A HG22 1 
ATOM   3344 H  HG23 A VAL   A 1 155 ? 11.774 -5.848  5.253   0.34 16.03 ?  155 VAL   A HG23 1 
ATOM   3345 H  HG23 B VAL   A 1 155 ? 11.548 -6.197  5.214   0.36 15.72 ?  155 VAL   A HG23 1 
ATOM   3346 H  HG23 T VAL   A 1 155 ? 11.640 -5.955  5.215   0.30 17.84 ?  155 VAL   A HG23 1 
ATOM   3347 N  N    A PHE   A 1 156 ? 11.386 -0.738  5.098   0.34 13.11 ?  156 PHE   A N    1 
ATOM   3348 N  N    B PHE   A 1 156 ? 11.321 -1.087  4.421   0.36 13.53 ?  156 PHE   A N    1 
ATOM   3349 N  N    T PHE   A 1 156 ? 11.503 -0.864  4.919   0.30 13.40 ?  156 PHE   A N    1 
ATOM   3350 C  CA   A PHE   A 1 156 ? 10.822 0.562   5.452   0.34 14.23 ?  156 PHE   A CA   1 
ATOM   3351 C  CA   B PHE   A 1 156 ? 10.930 0.303   4.645   0.36 14.77 ?  156 PHE   A CA   1 
ATOM   3352 C  CA   T PHE   A 1 156 ? 11.072 0.507   5.185   0.30 13.63 ?  156 PHE   A CA   1 
ATOM   3353 C  C    A PHE   A 1 156 ? 9.359  0.671   5.035   0.34 14.86 ?  156 PHE   A C    1 
ATOM   3354 C  C    B PHE   A 1 156 ? 9.433  0.514   4.445   0.36 16.14 ?  156 PHE   A C    1 
ATOM   3355 C  C    T PHE   A 1 156 ? 9.612  0.725   4.809   0.30 13.91 ?  156 PHE   A C    1 
ATOM   3356 O  O    A PHE   A 1 156 ? 8.511  1.120   5.817   0.34 15.46 ?  156 PHE   A O    1 
ATOM   3357 O  O    B PHE   A 1 156 ? 8.779  1.172   5.264   0.36 17.21 ?  156 PHE   A O    1 
ATOM   3358 O  O    T PHE   A 1 156 ? 8.862  1.370   5.552   0.30 14.23 ?  156 PHE   A O    1 
ATOM   3359 C  CB   A PHE   A 1 156 ? 11.651 1.678   4.813   0.34 15.04 ?  156 PHE   A CB   1 
ATOM   3360 C  CB   B PHE   A 1 156 ? 11.746 1.204   3.713   0.36 14.70 ?  156 PHE   A CB   1 
ATOM   3361 C  CB   T PHE   A 1 156 ? 11.958 1.478   4.403   0.30 13.14 ?  156 PHE   A CB   1 
ATOM   3362 C  CG   A PHE   A 1 156 ? 11.144 3.058   5.121   0.34 15.75 ?  156 PHE   A CG   1 
ATOM   3363 C  CG   B PHE   A 1 156 ? 11.461 2.676   3.856   0.36 15.14 ?  156 PHE   A CG   1 
ATOM   3364 C  CG   T PHE   A 1 156 ? 11.601 2.928   4.599   0.30 13.08 ?  156 PHE   A CG   1 
ATOM   3365 C  CD1  A PHE   A 1 156 ? 11.098 3.507   6.429   0.34 16.36 ?  156 PHE   A CD1  1 
ATOM   3366 C  CD1  B PHE   A 1 156 ? 12.061 3.420   4.857   0.36 15.83 ?  156 PHE   A CD1  1 
ATOM   3367 C  CD1  T PHE   A 1 156 ? 11.938 3.584   5.772   0.30 13.61 ?  156 PHE   A CD1  1 
ATOM   3368 C  CD2  A PHE   A 1 156 ? 10.726 3.908   4.108   0.34 16.33 ?  156 PHE   A CD2  1 
ATOM   3369 C  CD2  B PHE   A 1 156 ? 10.629 3.326   2.952   0.36 14.87 ?  156 PHE   A CD2  1 
ATOM   3370 C  CD2  T PHE   A 1 156 ? 10.948 3.642   3.603   0.30 13.33 ?  156 PHE   A CD2  1 
ATOM   3371 C  CE1  A PHE   A 1 156 ? 10.635 4.773   6.724   0.34 16.99 ?  156 PHE   A CE1  1 
ATOM   3372 C  CE1  B PHE   A 1 156 ? 11.814 4.777   4.976   0.36 16.04 ?  156 PHE   A CE1  1 
ATOM   3373 C  CE1  T PHE   A 1 156 ? 11.620 4.918   5.960   0.30 14.00 ?  156 PHE   A CE1  1 
ATOM   3374 C  CE2  A PHE   A 1 156 ? 10.257 5.176   4.398   0.34 16.78 ?  156 PHE   A CE2  1 
ATOM   3375 C  CE2  B PHE   A 1 156 ? 10.377 4.683   3.067   0.36 15.26 ?  156 PHE   A CE2  1 
ATOM   3376 C  CE2  T PHE   A 1 156 ? 10.624 4.978   3.785   0.30 13.71 ?  156 PHE   A CE2  1 
ATOM   3377 C  CZ   A PHE   A 1 156 ? 10.218 5.611   5.707   0.34 17.34 ?  156 PHE   A CZ   1 
ATOM   3378 C  CZ   B PHE   A 1 156 ? 10.973 5.409   4.077   0.36 15.69 ?  156 PHE   A CZ   1 
ATOM   3379 C  CZ   T PHE   A 1 156 ? 10.964 5.617   4.966   0.30 13.62 ?  156 PHE   A CZ   1 
ATOM   3380 H  H    A PHE   A 1 156 ? 12.017 -0.706  4.507   0.34 15.73 ?  156 PHE   A H    1 
ATOM   3381 H  H    B PHE   A 1 156 ? 11.800 -1.206  3.721   0.36 16.24 ?  156 PHE   A H    1 
ATOM   3382 H  H    T PHE   A 1 156 ? 12.071 -0.937  4.276   0.30 16.08 ?  156 PHE   A H    1 
ATOM   3383 H  HA   A PHE   A 1 156 ? 10.869 0.679   6.411   0.34 17.08 ?  156 PHE   A HA   1 
ATOM   3384 H  HA   B PHE   A 1 156 ? 11.138 0.544   5.558   0.36 17.73 ?  156 PHE   A HA   1 
ATOM   3385 H  HA   T PHE   A 1 156 ? 11.176 0.697   6.131   0.30 16.35 ?  156 PHE   A HA   1 
ATOM   3386 H  HB2  A PHE   A 1 156 ? 12.566 1.620   5.139   0.34 18.05 ?  156 PHE   A HB2  1 
ATOM   3387 H  HB2  B PHE   A 1 156 ? 12.686 1.069   3.903   0.36 17.63 ?  156 PHE   A HB2  1 
ATOM   3388 H  HB2  T PHE   A 1 156 ? 12.877 1.361   4.687   0.30 15.77 ?  156 PHE   A HB2  1 
ATOM   3389 H  HB3  A PHE   A 1 156 ? 11.643 1.569   3.849   0.34 18.05 ?  156 PHE   A HB3  1 
ATOM   3390 H  HB3  B PHE   A 1 156 ? 11.557 0.955   2.796   0.36 17.63 ?  156 PHE   A HB3  1 
ATOM   3391 H  HB3  T PHE   A 1 156 ? 11.878 1.280   3.457   0.30 15.77 ?  156 PHE   A HB3  1 
ATOM   3392 H  HD1  A PHE   A 1 156 ? 11.380 2.948   7.116   0.34 19.63 ?  156 PHE   A HD1  1 
ATOM   3393 H  HD1  B PHE   A 1 156 ? 12.626 3.001   5.464   0.36 18.99 ?  156 PHE   A HD1  1 
ATOM   3394 H  HD1  T PHE   A 1 156 ? 12.376 3.121   6.448   0.30 16.34 ?  156 PHE   A HD1  1 
ATOM   3395 H  HD2  A PHE   A 1 156 ? 10.754 3.616   3.225   0.34 19.60 ?  156 PHE   A HD2  1 
ATOM   3396 H  HD2  B PHE   A 1 156 ? 10.222 2.840   2.269   0.36 17.85 ?  156 PHE   A HD2  1 
ATOM   3397 H  HD2  T PHE   A 1 156 ? 10.714 3.218   2.810   0.30 16.00 ?  156 PHE   A HD2  1 
ATOM   3398 H  HE1  A PHE   A 1 156 ? 10.608 5.063   7.608   0.34 20.39 ?  156 PHE   A HE1  1 
ATOM   3399 H  HE1  B PHE   A 1 156 ? 12.213 5.266   5.656   0.36 19.25 ?  156 PHE   A HE1  1 
ATOM   3400 H  HE1  T PHE   A 1 156 ? 11.845 5.346   6.755   0.30 16.80 ?  156 PHE   A HE1  1 
ATOM   3401 H  HE2  A PHE   A 1 156 ? 9.979  5.737   3.710   0.34 20.14 ?  156 PHE   A HE2  1 
ATOM   3402 H  HE2  B PHE   A 1 156 ? 9.810  5.103   2.460   0.36 18.32 ?  156 PHE   A HE2  1 
ATOM   3403 H  HE2  T PHE   A 1 156 ? 10.180 5.447   3.113   0.30 16.45 ?  156 PHE   A HE2  1 
ATOM   3404 H  HZ   A PHE   A 1 156 ? 9.905  6.464   5.906   0.34 20.80 ?  156 PHE   A HZ   1 
ATOM   3405 H  HZ   B PHE   A 1 156 ? 10.802 6.319   4.154   0.36 18.83 ?  156 PHE   A HZ   1 
ATOM   3406 H  HZ   T PHE   A 1 156 ? 10.746 6.515   5.091   0.30 16.34 ?  156 PHE   A HZ   1 
ATOM   3407 N  N    A ASP   A 1 157 ? 9.046  0.276   3.804   0.34 14.85 ?  157 ASP   A N    1 
ATOM   3408 N  N    B ASP   A 1 157 ? 8.868  -0.019  3.365   0.36 17.14 ?  157 ASP   A N    1 
ATOM   3409 N  N    T ASP   A 1 157 ? 9.198  0.215   3.653   0.30 13.91 ?  157 ASP   A N    1 
ATOM   3410 C  CA   A ASP   A 1 157 ? 7.720  0.496   3.238   0.34 15.61 ?  157 ASP   A CA   1 
ATOM   3411 C  CA   B ASP   A 1 157 ? 7.498  0.307   2.985   0.36 17.75 ?  157 ASP   A CA   1 
ATOM   3412 C  CA   T ASP   A 1 157 ? 7.894  0.520   3.077   0.30 14.28 ?  157 ASP   A CA   1 
ATOM   3413 C  C    A ASP   A 1 157 ? 6.739  -0.522  3.813   0.34 16.14 ?  157 ASP   A C    1 
ATOM   3414 C  C    B ASP   A 1 157 ? 6.535  -0.822  3.340   0.36 16.67 ?  157 ASP   A C    1 
ATOM   3415 C  C    T ASP   A 1 157 ? 6.853  -0.454  3.622   0.30 15.22 ?  157 ASP   A C    1 
ATOM   3416 O  O    A ASP   A 1 157 ? 6.920  -1.733  3.637   0.34 16.03 ?  157 ASP   A O    1 
ATOM   3417 O  O    B ASP   A 1 157 ? 6.793  -1.993  3.039   0.36 16.09 ?  157 ASP   A O    1 
ATOM   3418 O  O    T ASP   A 1 157 ? 6.969  -1.669  3.422   0.30 15.46 ?  157 ASP   A O    1 
ATOM   3419 C  CB   A ASP   A 1 157 ? 7.791  0.365   1.718   0.34 16.09 ?  157 ASP   A CB   1 
ATOM   3420 C  CB   B ASP   A 1 157 ? 7.397  0.681   1.506   0.36 19.65 ?  157 ASP   A CB   1 
ATOM   3421 C  CB   T ASP   A 1 157 ? 7.995  0.412   1.556   0.30 14.15 ?  157 ASP   A CB   1 
ATOM   3422 C  CG   A ASP   A 1 157 ? 6.534  0.894   1.024   0.34 16.91 ?  157 ASP   A CG   1 
ATOM   3423 C  CG   B ASP   A 1 157 ? 6.671  1.991   1.291   0.36 21.50 ?  157 ASP   A CG   1 
ATOM   3424 C  CG   T ASP   A 1 157 ? 6.791  0.988   0.847   0.30 13.78 ?  157 ASP   A CG   1 
ATOM   3425 O  OD1  A ASP   A 1 157 ? 6.249  2.107   1.130   0.34 18.29 ?  157 ASP   A OD1  1 
ATOM   3426 O  OD1  B ASP   A 1 157 ? 7.313  3.062   1.394   0.36 22.66 ?  157 ASP   A OD1  1 
ATOM   3427 O  OD1  T ASP   A 1 157 ? 5.695  0.405   0.988   0.30 14.07 ?  157 ASP   A OD1  1 
ATOM   3428 O  OD2  A ASP   A 1 157 ? 5.825  0.092   0.375   0.34 16.20 -1 157 ASP   A OD2  1 
ATOM   3429 O  OD2  B ASP   A 1 157 ? 5.452  1.946   1.029   0.36 21.61 -1 157 ASP   A OD2  1 
ATOM   3430 O  OD2  T ASP   A 1 157 ? 6.937  2.021   0.157   0.30 13.31 -1 157 ASP   A OD2  1 
ATOM   3431 H  H    A ASP   A 1 157 ? 9.590  -0.127  3.273   0.34 17.82 ?  157 ASP   A H    1 
ATOM   3432 H  H    B ASP   A 1 157 ? 9.257  -0.579  2.837   0.36 20.56 ?  157 ASP   A H    1 
ATOM   3433 H  H    T ASP   A 1 157 ? 9.671  -0.314  3.167   0.30 16.69 ?  157 ASP   A H    1 
ATOM   3434 H  HA   A ASP   A 1 157 ? 7.413  1.395   3.452   0.34 18.73 ?  157 ASP   A HA   1 
ATOM   3435 H  HA   B ASP   A 1 157 ? 7.216  1.074   3.493   0.36 21.30 ?  157 ASP   A HA   1 
ATOM   3436 H  HA   T ASP   A 1 157 ? 7.634  1.427   3.309   0.30 17.14 ?  157 ASP   A HA   1 
ATOM   3437 H  HB2  A ASP   A 1 157 ? 8.579  0.840   1.396   0.34 19.31 ?  157 ASP   A HB2  1 
ATOM   3438 H  HB2  B ASP   A 1 157 ? 8.285  0.784   1.143   0.36 23.58 ?  157 ASP   A HB2  1 
ATOM   3439 H  HB2  T ASP   A 1 157 ? 8.786  0.887   1.257   0.30 16.97 ?  157 ASP   A HB2  1 
ATOM   3440 H  HB3  A ASP   A 1 157 ? 7.882  -0.575  1.496   0.34 19.31 ?  157 ASP   A HB3  1 
ATOM   3441 H  HB3  B ASP   A 1 157 ? 6.909  -0.005  1.031   0.36 23.58 ?  157 ASP   A HB3  1 
ATOM   3442 H  HB3  T ASP   A 1 157 ? 8.068  -0.525  1.313   0.30 16.97 ?  157 ASP   A HB3  1 
ATOM   3443 N  N    A LYS   A 1 158 ? 5.697  -0.040  4.497   0.34 17.22 ?  158 LYS   A N    1 
ATOM   3444 N  N    B LYS   A 1 158 ? 5.414  -0.447  3.965   0.36 16.78 ?  158 LYS   A N    1 
ATOM   3445 N  N    T LYS   A 1 158 ? 5.833  0.078   4.305   0.30 16.27 ?  158 LYS   A N    1 
ATOM   3446 C  CA   A LYS   A 1 158 ? 4.715  -0.960  5.067   0.34 18.07 ?  158 LYS   A CA   1 
ATOM   3447 C  CA   B LYS   A 1 158 ? 4.472  -1.417  4.520   0.36 17.26 ?  158 LYS   A CA   1 
ATOM   3448 C  CA   T LYS   A 1 158 ? 4.841  -0.796  4.929   0.30 17.47 ?  158 LYS   A CA   1 
ATOM   3449 C  C    A LYS   A 1 158 ? 3.974  -1.715  3.976   0.34 17.36 ?  158 LYS   A C    1 
ATOM   3450 C  C    B LYS   A 1 158 ? 3.785  -2.221  3.419   0.36 16.14 ?  158 LYS   A C    1 
ATOM   3451 C  C    T LYS   A 1 158 ? 4.071  -1.595  3.887   0.30 17.01 ?  158 LYS   A C    1 
ATOM   3452 O  O    A LYS   A 1 158 ? 3.770  -2.930  4.081   0.34 17.40 ?  158 LYS   A O    1 
ATOM   3453 O  O    B LYS   A 1 158 ? 3.655  -3.447  3.521   0.36 15.54 ?  158 LYS   A O    1 
ATOM   3454 O  O    T LYS   A 1 158 ? 3.836  -2.795  4.067   0.30 16.97 ?  158 LYS   A O    1 
ATOM   3455 C  CB   A LYS   A 1 158 ? 3.726  -0.217  5.966   0.34 19.83 ?  158 LYS   A CB   1 
ATOM   3456 C  CB   B LYS   A 1 158 ? 3.452  -0.665  5.384   0.36 19.21 ?  158 LYS   A CB   1 
ATOM   3457 C  CB   T LYS   A 1 158 ? 3.878  0.005   5.809   0.30 19.45 ?  158 LYS   A CB   1 
ATOM   3458 C  CG   A LYS   A 1 158 ? 2.503  -1.049  6.393   0.34 21.62 ?  158 LYS   A CG   1 
ATOM   3459 C  CG   B LYS   A 1 158 ? 2.276  -1.484  5.893   0.36 20.89 ?  158 LYS   A CG   1 
ATOM   3460 C  CG   T LYS   A 1 158 ? 2.650  -0.788  6.275   0.30 21.33 ?  158 LYS   A CG   1 
ATOM   3461 C  CD   A LYS   A 1 158 ? 2.870  -2.345  7.130   0.34 23.07 ?  158 LYS   A CD   1 
ATOM   3462 C  CD   B LYS   A 1 158 ? 2.706  -2.571  6.868   0.36 22.10 ?  158 LYS   A CD   1 
ATOM   3463 C  CD   T LYS   A 1 158 ? 3.029  -2.016  7.104   0.30 23.18 ?  158 LYS   A CD   1 
ATOM   3464 C  CE   A LYS   A 1 158 ? 1.627  -3.024  7.709   0.34 23.92 ?  158 LYS   A CE   1 
ATOM   3465 C  CE   B LYS   A 1 158 ? 1.498  -3.125  7.610   0.36 22.73 ?  158 LYS   A CE   1 
ATOM   3466 C  CE   T LYS   A 1 158 ? 1.794  -2.828  7.495   0.30 24.44 ?  158 LYS   A CE   1 
ATOM   3467 N  NZ   A LYS   A 1 158 ? 1.899  -4.382  8.267   0.34 24.24 ?  158 LYS   A NZ   1 
ATOM   3468 N  NZ   B LYS   A 1 158 ? 1.781  -4.412  8.303   0.36 22.76 ?  158 LYS   A NZ   1 
ATOM   3469 N  NZ   T LYS   A 1 158 ? 2.129  -4.053  8.280   0.30 25.07 ?  158 LYS   A NZ   1 
ATOM   3470 H  H    A LYS   A 1 158 ? 5.541  0.794   4.637   0.34 20.66 ?  158 LYS   A H    1 
ATOM   3471 H  H    B LYS   A 1 158 ? 5.175  0.371   4.078   0.36 20.14 ?  158 LYS   A H    1 
ATOM   3472 H  H    T LYS   A 1 158 ? 5.696  0.920   4.416   0.30 19.52 ?  158 LYS   A H    1 
ATOM   3473 H  HA   A LYS   A 1 158 ? 5.179  -1.613  5.609   0.34 21.69 ?  158 LYS   A HA   1 
ATOM   3474 H  HA   B LYS   A 1 158 ? 4.946  -2.034  5.096   0.36 20.71 ?  158 LYS   A HA   1 
ATOM   3475 H  HA   T LYS   A 1 158 ? 5.301  -1.427  5.501   0.30 20.97 ?  158 LYS   A HA   1 
ATOM   3476 H  HB2  A LYS   A 1 158 ? 4.185  0.068   6.770   0.34 23.79 ?  158 LYS   A HB2  1 
ATOM   3477 H  HB2  B LYS   A 1 158 ? 3.912  -0.310  6.166   0.36 23.05 ?  158 LYS   A HB2  1 
ATOM   3478 H  HB2  T LYS   A 1 158 ? 4.353  0.300   6.604   0.30 23.34 ?  158 LYS   A HB2  1 
ATOM   3479 H  HB3  A LYS   A 1 158 ? 3.397  0.558   5.487   0.34 23.79 ?  158 LYS   A HB3  1 
ATOM   3480 H  HB3  B LYS   A 1 158 ? 3.089  0.071   4.867   0.36 23.05 ?  158 LYS   A HB3  1 
ATOM   3481 H  HB3  T LYS   A 1 158 ? 3.561  0.773   5.313   0.30 23.34 ?  158 LYS   A HB3  1 
ATOM   3482 H  HG2  A LYS   A 1 158 ? 1.961  -0.516  6.993   0.34 25.94 ?  158 LYS   A HG2  1 
ATOM   3483 H  HG2  B LYS   A 1 158 ? 1.661  -0.893  6.358   0.36 25.07 ?  158 LYS   A HG2  1 
ATOM   3484 H  HG2  T LYS   A 1 158 ? 2.100  -0.217  6.831   0.30 25.60 ?  158 LYS   A HG2  1 
ATOM   3485 H  HG3  A LYS   A 1 158 ? 1.982  -1.287  5.609   0.34 25.94 ?  158 LYS   A HG3  1 
ATOM   3486 H  HG3  B LYS   A 1 158 ? 1.824  -1.904  5.146   0.36 25.07 ?  158 LYS   A HG3  1 
ATOM   3487 H  HG3  T LYS   A 1 158 ? 2.136  -1.087  5.506   0.30 25.60 ?  158 LYS   A HG3  1 
ATOM   3488 H  HD2  A LYS   A 1 158 ? 3.295  -2.962  6.514   0.34 27.69 ?  158 LYS   A HD2  1 
ATOM   3489 H  HD2  B LYS   A 1 158 ? 3.128  -3.293  6.378   0.36 26.52 ?  158 LYS   A HD2  1 
ATOM   3490 H  HD2  T LYS   A 1 158 ? 3.615  -2.591  6.588   0.30 27.82 ?  158 LYS   A HD2  1 
ATOM   3491 H  HD3  A LYS   A 1 158 ? 3.465  -2.140  7.866   0.34 27.69 ?  158 LYS   A HD3  1 
ATOM   3492 H  HD3  B LYS   A 1 158 ? 3.323  -2.194  7.517   0.36 26.52 ?  158 LYS   A HD3  1 
ATOM   3493 H  HD3  T LYS   A 1 158 ? 3.472  -1.730  7.919   0.30 27.82 ?  158 LYS   A HD3  1 
ATOM   3494 H  HE2  A LYS   A 1 158 ? 1.270  -2.474  8.425   0.34 28.71 ?  158 LYS   A HE2  1 
ATOM   3495 H  HE2  B LYS   A 1 158 ? 1.219  -2.479  8.278   0.36 27.28 ?  158 LYS   A HE2  1 
ATOM   3496 H  HE2  T LYS   A 1 158 ? 1.207  -2.277  8.037   0.30 29.33 ?  158 LYS   A HE2  1 
ATOM   3497 H  HE3  A LYS   A 1 158 ? 0.966  -3.119  7.008   0.34 28.71 ?  158 LYS   A HE3  1 
ATOM   3498 H  HE3  B LYS   A 1 158 ? 0.783  -3.272  6.974   0.36 27.28 ?  158 LYS   A HE3  1 
ATOM   3499 H  HE3  T LYS   A 1 158 ? 1.331  -3.109  6.689   0.30 29.33 ?  158 LYS   A HE3  1 
ATOM   3500 H  HZ1  A LYS   A 1 158 ? 1.148  -4.735  8.593   0.34 29.09 ?  158 LYS   A HZ1  1 
ATOM   3501 H  HZ1  B LYS   A 1 158 ? 1.049  -4.698  8.722   0.36 27.31 ?  158 LYS   A HZ1  1 
ATOM   3502 H  HZ1  T LYS   A 1 158 ? 1.384  -4.497  8.487   0.30 30.08 ?  158 LYS   A HZ1  1 
ATOM   3503 H  HZ2  A LYS   A 1 158 ? 2.215  -4.916  7.628   0.34 29.09 ?  158 LYS   A HZ2  1 
ATOM   3504 H  HZ2  B LYS   A 1 158 ? 2.034  -5.027  7.711   0.36 27.31 ?  158 LYS   A HZ2  1 
ATOM   3505 H  HZ2  T LYS   A 1 158 ? 2.658  -4.587  7.803   0.30 30.08 ?  158 LYS   A HZ2  1 
ATOM   3506 H  HZ3  A LYS   A 1 158 ? 2.500  -4.330  8.922   0.34 29.09 ?  158 LYS   A HZ3  1 
ATOM   3507 H  HZ3  B LYS   A 1 158 ? 2.431  -4.300  8.900   0.36 27.31 ?  158 LYS   A HZ3  1 
ATOM   3508 H  HZ3  T LYS   A 1 158 ? 2.548  -3.829  9.033   0.30 30.08 ?  158 LYS   A HZ3  1 
ATOM   3509 N  N    A ASN   A 1 159 ? 3.549  -1.015  2.924   0.34 17.19 ?  159 ASN   A N    1 
ATOM   3510 N  N    B ASN   A 1 159 ? 3.340  -1.542  2.363   0.36 16.56 ?  159 ASN   A N    1 
ATOM   3511 N  N    T ASN   A 1 159 ? 3.653  -0.952  2.802   0.30 17.13 ?  159 ASN   A N    1 
ATOM   3512 C  CA   A ASN   A 1 159 ? 2.872  -1.701  1.831   0.34 16.90 ?  159 ASN   A CA   1 
ATOM   3513 C  CA   B ASN   A 1 159 ? 2.728  -2.214  1.223   0.36 17.05 ?  159 ASN   A CA   1 
ATOM   3514 C  CA   T ASN   A 1 159 ? 2.907  -1.655  1.767   0.30 17.37 ?  159 ASN   A CA   1 
ATOM   3515 C  C    A ASN   A 1 159 ? 3.770  -2.766  1.216   0.34 16.02 ?  159 ASN   A C    1 
ATOM   3516 C  C    B ASN   A 1 159 ? 3.610  -3.360  0.730   0.36 15.91 ?  159 ASN   A C    1 
ATOM   3517 C  C    T ASN   A 1 159 ? 3.744  -2.766  1.145   0.30 17.20 ?  159 ASN   A C    1 
ATOM   3518 O  O    A ASN   A 1 159 ? 3.323  -3.886  0.953   0.34 15.65 ?  159 ASN   A O    1 
ATOM   3519 O  O    B ASN   A 1 159 ? 3.154  -4.501  0.579   0.36 16.04 ?  159 ASN   A O    1 
ATOM   3520 O  O    T ASN   A 1 159 ? 3.219  -3.817  0.795   0.30 17.31 ?  159 ASN   A O    1 
ATOM   3521 C  CB   A ASN   A 1 159 ? 2.392  -0.693  0.783   0.34 18.18 ?  159 ASN   A CB   1 
ATOM   3522 C  CB   B ASN   A 1 159 ? 2.511  -1.161  0.132   0.36 18.85 ?  159 ASN   A CB   1 
ATOM   3523 C  CB   T ASN   A 1 159 ? 2.404  -0.689  0.692   0.30 18.35 ?  159 ASN   A CB   1 
ATOM   3524 C  CG   A ASN   A 1 159 ? 1.140  0.044   1.218   0.34 19.77 ?  159 ASN   A CG   1 
ATOM   3525 C  CG   B ASN   A 1 159 ? 1.608  -1.636  -0.975  0.36 20.65 ?  159 ASN   A CG   1 
ATOM   3526 C  CG   T ASN   A 1 159 ? 1.174  0.082   1.132   0.30 19.54 ?  159 ASN   A CG   1 
ATOM   3527 O  OD1  A ASN   A 1 159 ? 0.292  -0.515  1.911   0.34 20.77 ?  159 ASN   A OD1  1 
ATOM   3528 O  OD1  B ASN   A 1 159 ? 0.413  -1.340  -0.987  0.36 21.30 ?  159 ASN   A OD1  1 
ATOM   3529 O  OD1  T ASN   A 1 159 ? 0.360  -0.422  1.904   0.30 20.36 ?  159 ASN   A OD1  1 
ATOM   3530 N  ND2  A ASN   A 1 159 ? 1.016  1.302   0.809   0.34 20.33 ?  159 ASN   A ND2  1 
ATOM   3531 N  ND2  B ASN   A 1 159 ? 2.175  -2.357  -1.929  0.36 21.27 ?  159 ASN   A ND2  1 
ATOM   3532 N  ND2  T ASN   A 1 159 ? 1.031  1.304   0.640   0.30 19.91 ?  159 ASN   A ND2  1 
ATOM   3533 H  H    A ASN   A 1 159 ? 3.635  -0.168  2.824   0.34 20.63 ?  159 ASN   A H    1 
ATOM   3534 H  H    B ASN   A 1 159 ? 3.394  -0.692  2.283   0.36 19.88 ?  159 ASN   A H    1 
ATOM   3535 H  H    T ASN   A 1 159 ? 3.779  -0.118  2.647   0.30 20.56 ?  159 ASN   A H    1 
ATOM   3536 H  HA   A ASN   A 1 159 ? 2.088  -2.151  2.183   0.34 20.28 ?  159 ASN   A HA   1 
ATOM   3537 H  HA   B ASN   A 1 159 ? 1.861  -2.571  1.478   0.36 20.46 ?  159 ASN   A HA   1 
ATOM   3538 H  HA   T ASN   A 1 159 ? 2.134  -2.075  2.172   0.30 20.84 ?  159 ASN   A HA   1 
ATOM   3539 H  HB2  A ASN   A 1 159 ? 3.085  -0.036  0.632   0.34 21.82 ?  159 ASN   A HB2  1 
ATOM   3540 H  HB2  B ASN   A 1 159 ? 2.108  -0.369  0.533   0.36 22.62 ?  159 ASN   A HB2  1 
ATOM   3541 H  HB2  T ASN   A 1 159 ? 3.100  -0.050  0.489   0.30 22.02 ?  159 ASN   A HB2  1 
ATOM   3542 H  HB3  A ASN   A 1 159 ? 2.190  -1.165  -0.042  0.34 21.82 ?  159 ASN   A HB3  1 
ATOM   3543 H  HB3  B ASN   A 1 159 ? 3.368  -0.927  -0.256  0.36 22.62 ?  159 ASN   A HB3  1 
ATOM   3544 H  HB3  T ASN   A 1 159 ? 2.175  -1.198  -0.105  0.30 22.02 ?  159 ASN   A HB3  1 
ATOM   3545 H  HD21 A ASN   A 1 159 ? 0.322  1.758   1.028   0.34 24.40 ?  159 ASN   A HD21 1 
ATOM   3546 H  HD21 B ASN   A 1 159 ? 1.702  -2.644  -2.584  0.36 25.53 ?  159 ASN   A HD21 1 
ATOM   3547 H  HD21 T ASN   A 1 159 ? 0.347  1.776   0.859   0.30 23.89 ?  159 ASN   A HD21 1 
ATOM   3548 H  HD22 A ASN   A 1 159 ? 1.631  1.657   0.327   0.34 24.40 ?  159 ASN   A HD22 1 
ATOM   3549 H  HD22 B ASN   A 1 159 ? 3.014  -2.537  -1.886  0.36 25.53 ?  159 ASN   A HD22 1 
ATOM   3550 H  HD22 T ASN   A 1 159 ? 1.623  1.621   0.106   0.30 23.89 ?  159 ASN   A HD22 1 
ATOM   3551 N  N    A LEU   A 1 160 ? 5.049  -2.453  1.009   0.34 15.08 ?  160 LEU   A N    1 
ATOM   3552 N  N    B LEU   A 1 160 ? 4.895  -3.077  0.505   0.36 15.15 ?  160 LEU   A N    1 
ATOM   3553 N  N    T LEU   A 1 160 ? 5.045  -2.543  1.016   0.30 16.62 ?  160 LEU   A N    1 
ATOM   3554 C  CA   A LEU   A 1 160 ? 5.946  -3.465  0.463   0.34 14.31 ?  160 LEU   A CA   1 
ATOM   3555 C  CA   B LEU   A 1 160 ? 5.813  -4.118  0.054   0.36 15.06 ?  160 LEU   A CA   1 
ATOM   3556 C  CA   T LEU   A 1 160 ? 5.922  -3.581  0.491   0.30 16.04 ?  160 LEU   A CA   1 
ATOM   3557 C  C    A LEU   A 1 160 ? 6.118  -4.631  1.428   0.34 13.37 ?  160 LEU   A C    1 
ATOM   3558 C  C    B LEU   A 1 160 ? 6.061  -5.151  1.150   0.36 14.22 ?  160 LEU   A C    1 
ATOM   3559 O  O    A LEU   A 1 160 ? 6.149  -5.791  1.005   0.34 13.10 ?  160 LEU   A O    1 
ATOM   3560 O  O    B LEU   A 1 160 ? 6.083  -6.354  0.874   0.36 14.67 ?  160 LEU   A O    1 
ATOM   3561 C  CB   A LEU   A 1 160 ? 7.301  -2.861  0.104   0.34 14.36 ?  160 LEU   A CB   1 
ATOM   3562 C  CB   B LEU   A 1 160 ? 7.124  -3.489  -0.417  0.36 16.37 ?  160 LEU   A CB   1 
ATOM   3563 C  CB   T LEU   A 1 160 ? 7.277  -3.006  0.089   0.30 15.44 ?  160 LEU   A CB   1 
ATOM   3564 C  CG   A LEU   A 1 160 ? 8.323  -3.919  -0.320  0.34 15.09 ?  160 LEU   A CG   1 
ATOM   3565 C  CG   B LEU   A 1 160 ? 7.010  -2.662  -1.699  0.36 18.65 ?  160 LEU   A CG   1 
ATOM   3566 C  CG   T LEU   A 1 160 ? 8.288  -4.068  -0.344  0.30 15.43 ?  160 LEU   A CG   1 
ATOM   3567 C  CD1  A LEU   A 1 160 ? 7.851  -4.702  -1.534  0.34 15.51 ?  160 LEU   A CD1  1 
ATOM   3568 C  CD1  B LEU   A 1 160 ? 8.212  -1.755  -1.892  0.36 19.26 ?  160 LEU   A CD1  1 
ATOM   3569 C  CD1  T LEU   A 1 160 ? 7.806  -4.822  -1.568  0.30 15.73 ?  160 LEU   A CD1  1 
ATOM   3570 C  CD2  A LEU   A 1 160 ? 9.661  -3.281  -0.591  0.34 15.35 ?  160 LEU   A CD2  1 
ATOM   3571 C  CD2  B LEU   A 1 160 ? 6.819  -3.571  -2.907  0.36 19.41 ?  160 LEU   A CD2  1 
ATOM   3572 C  CD2  T LEU   A 1 160 ? 9.630  -3.425  -0.615  0.30 15.45 ?  160 LEU   A CD2  1 
ATOM   3573 H  H    A LEU   A 1 160 ? 5.409  -1.689  1.177   0.34 18.10 ?  160 LEU   A H    1 
ATOM   3574 H  H    B LEU   A 1 160 ? 5.251  -2.305  0.614   0.36 18.18 ?  160 LEU   A H    1 
ATOM   3575 H  H    T LEU   A 1 160 ? 5.442  -1.806  1.222   0.30 19.94 ?  160 LEU   A H    1 
ATOM   3576 H  HA   A LEU   A 1 160 ? 5.559  -3.811  -0.351  0.34 17.17 ?  160 LEU   A HA   1 
ATOM   3577 H  HA   B LEU   A 1 160 ? 5.413  -4.576  -0.703  0.36 18.08 ?  160 LEU   A HA   1 
ATOM   3578 H  HB2  A LEU   A 1 160 ? 7.197  -2.211  -0.619  0.34 17.24 ?  160 LEU   A HB2  1 
ATOM   3579 H  HB2  B LEU   A 1 160 ? 7.454  -2.904  0.282   0.36 19.65 ?  160 LEU   A HB2  1 
ATOM   3580 H  HB2  T LEU   A 1 160 ? 7.157  -2.383  -0.649  0.30 18.52 ?  160 LEU   A HB2  1 
ATOM   3581 H  HB3  A LEU   A 1 160 ? 7.660  -2.428  0.890   0.34 17.24 ?  160 LEU   A HB3  1 
ATOM   3582 H  HB3  B LEU   A 1 160 ? 7.765  -4.199  -0.579  0.36 19.65 ?  160 LEU   A HB3  1 
ATOM   3583 H  HB3  T LEU   A 1 160 ? 7.655  -2.540  0.852   0.30 18.52 ?  160 LEU   A HB3  1 
ATOM   3584 H  HG   A LEU   A 1 160 ? 8.451  -4.544  0.408   0.34 18.11 ?  160 LEU   A HG   1 
ATOM   3585 H  HG   B LEU   A 1 160 ? 6.231  -2.098  -1.623  0.36 22.37 ?  160 LEU   A HG   1 
ATOM   3586 H  HG   T LEU   A 1 160 ? 8.402  -4.705  0.377   0.30 18.51 ?  160 LEU   A HG   1 
ATOM   3587 H  HD11 A LEU   A 1 160 ? 8.579  -5.258  -1.848  0.34 18.61 ?  160 LEU   A HD11 1 
ATOM   3588 H  HD11 B LEU   A 1 160 ? 8.084  -1.232  -2.700  0.36 23.11 ?  160 LEU   A HD11 1 
ATOM   3589 H  HD11 T LEU   A 1 160 ? 8.506  -5.425  -1.861  0.30 18.87 ?  160 LEU   A HD11 1 
ATOM   3590 H  HD12 A LEU   A 1 160 ? 7.096  -5.256  -1.280  0.34 18.61 ?  160 LEU   A HD12 1 
ATOM   3591 H  HD12 B LEU   A 1 160 ? 8.284  -1.164  -1.125  0.36 23.11 ?  160 LEU   A HD12 1 
ATOM   3592 H  HD12 T LEU   A 1 160 ? 7.011  -5.325  -1.335  0.30 18.87 ?  160 LEU   A HD12 1 
ATOM   3593 H  HD13 A LEU   A 1 160 ? 7.586  -4.078  -2.229  0.34 18.61 ?  160 LEU   A HD13 1 
ATOM   3594 H  HD13 B LEU   A 1 160 ? 9.009  -2.298  -1.970  0.36 23.11 ?  160 LEU   A HD13 1 
ATOM   3595 H  HD13 T LEU   A 1 160 ? 7.602  -4.185  -2.270  0.30 18.87 ?  160 LEU   A HD13 1 
ATOM   3596 H  HD21 A LEU   A 1 160 ? 10.291 -3.974  -0.846  0.34 18.41 ?  160 LEU   A HD21 1 
ATOM   3597 H  HD21 B LEU   A 1 160 ? 6.821  -3.030  -3.712  0.36 23.30 ?  160 LEU   A HD21 1 
ATOM   3598 H  HD21 T LEU   A 1 160 ? 10.260 -4.111  -0.886  0.30 18.53 ?  160 LEU   A HD21 1 
ATOM   3599 H  HD22 A LEU   A 1 160 ? 9.567  -2.638  -1.309  0.34 18.41 ?  160 LEU   A HD22 1 
ATOM   3600 H  HD22 B LEU   A 1 160 ? 7.546  -4.213  -2.938  0.36 23.30 ?  160 LEU   A HD22 1 
ATOM   3601 H  HD22 T LEU   A 1 160 ? 9.530  -2.769  -1.323  0.30 18.53 ?  160 LEU   A HD22 1 
ATOM   3602 H  HD23 A LEU   A 1 160 ? 9.970  -2.837  0.215   0.34 18.41 ?  160 LEU   A HD23 1 
ATOM   3603 H  HD23 B LEU   A 1 160 ? 5.972  -4.036  -2.823  0.36 23.30 ?  160 LEU   A HD23 1 
ATOM   3604 H  HD23 T LEU   A 1 160 ? 9.943  -2.991  0.195   0.30 18.53 ?  160 LEU   A HD23 1 
ATOM   3605 N  N    A TYR   A 1 161 ? 6.249  -4.344  2.725   0.64 14.95 ?  161 TYR   A N    1 
ATOM   3606 N  N    B TYR   A 1 161 ? 6.240  -4.704  2.398   0.36 14.48 ?  161 TYR   A N    1 
ATOM   3607 C  CA   A TYR   A 1 161 ? 6.385  -5.418  3.704   0.64 15.14 ?  161 TYR   A CA   1 
ATOM   3608 C  CA   B TYR   A 1 161 ? 6.398  -5.631  3.519   0.36 14.78 ?  161 TYR   A CA   1 
ATOM   3609 C  C    A TYR   A 1 161 ? 5.233  -6.413  3.603   0.64 16.52 ?  161 TYR   A C    1 
ATOM   3610 C  C    B TYR   A 1 161 ? 5.238  -6.614  3.582   0.36 15.48 ?  161 TYR   A C    1 
ATOM   3611 O  O    A TYR   A 1 161 ? 5.443  -7.631  3.618   0.64 16.55 ?  161 TYR   A O    1 
ATOM   3612 O  O    B TYR   A 1 161 ? 5.437  -7.834  3.617   0.36 15.36 ?  161 TYR   A O    1 
ATOM   3613 C  CB   A TYR   A 1 161 ? 6.470  -4.845  5.116   0.64 15.26 ?  161 TYR   A CB   1 
ATOM   3614 C  CB   B TYR   A 1 161 ? 6.512  -4.863  4.843   0.36 15.08 ?  161 TYR   A CB   1 
ATOM   3615 C  CG   A TYR   A 1 161 ? 6.376  -5.914  6.167   0.64 14.77 ?  161 TYR   A CG   1 
ATOM   3616 C  CG   B TYR   A 1 161 ? 6.405  -5.752  6.075   0.36 15.21 ?  161 TYR   A CG   1 
ATOM   3617 C  CD1  A TYR   A 1 161 ? 7.492  -6.642  6.539   0.64 14.61 ?  161 TYR   A CD1  1 
ATOM   3618 C  CD1  B TYR   A 1 161 ? 7.508  -6.452  6.549   0.36 15.43 ?  161 TYR   A CD1  1 
ATOM   3619 C  CD2  A TYR   A 1 161 ? 5.166  -6.203  6.782   0.64 14.50 ?  161 TYR   A CD2  1 
ATOM   3620 C  CD2  B TYR   A 1 161 ? 5.201  -5.894  6.761   0.36 15.25 ?  161 TYR   A CD2  1 
ATOM   3621 C  CE1  A TYR   A 1 161 ? 7.407  -7.626  7.490   0.64 14.20 ?  161 TYR   A CE1  1 
ATOM   3622 C  CE1  B TYR   A 1 161 ? 7.416  -7.273  7.666   0.36 15.64 ?  161 TYR   A CE1  1 
ATOM   3623 C  CE2  A TYR   A 1 161 ? 5.073  -7.185  7.733   0.64 13.90 ?  161 TYR   A CE2  1 
ATOM   3624 C  CE2  B TYR   A 1 161 ? 5.100  -6.715  7.880   0.36 15.52 ?  161 TYR   A CE2  1 
ATOM   3625 C  CZ   A TYR   A 1 161 ? 6.197  -7.893  8.084   0.64 13.63 ?  161 TYR   A CZ   1 
ATOM   3626 C  CZ   B TYR   A 1 161 ? 6.212  -7.399  8.327   0.36 16.08 ?  161 TYR   A CZ   1 
ATOM   3627 O  OH   A TYR   A 1 161 ? 6.129  -8.869  9.039   0.64 13.55 ?  161 TYR   A OH   1 
ATOM   3628 O  OH   B TYR   A 1 161 ? 6.123  -8.215  9.435   0.36 17.39 ?  161 TYR   A OH   1 
ATOM   3629 H  H    A TYR   A 1 161 ? 6.255  -3.546  3.059   0.64 17.94 ?  161 TYR   A H    1 
ATOM   3630 H  H    B TYR   A 1 161 ? 6.264  -3.879  2.615   0.36 17.38 ?  161 TYR   A H    1 
ATOM   3631 H  HA   A TYR   A 1 161 ? 7.205  -5.894  3.530   0.64 18.17 ?  161 TYR   A HA   1 
ATOM   3632 H  HA   B TYR   A 1 161 ? 7.212  -6.142  3.400   0.36 17.73 ?  161 TYR   A HA   1 
ATOM   3633 H  HB2  A TYR   A 1 161 ? 7.321  -4.389  5.223   0.64 18.31 ?  161 TYR   A HB2  1 
ATOM   3634 H  HB2  B TYR   A 1 161 ? 7.373  -4.415  4.872   0.36 18.09 ?  161 TYR   A HB2  1 
ATOM   3635 H  HB3  A TYR   A 1 161 ? 5.740  -4.220  5.255   0.64 18.31 ?  161 TYR   A HB3  1 
ATOM   3636 H  HB3  B TYR   A 1 161 ? 5.800  -4.204  4.887   0.36 18.09 ?  161 TYR   A HB3  1 
ATOM   3637 H  HD1  A TYR   A 1 161 ? 8.312  -6.465  6.134   0.64 17.53 ?  161 TYR   A HD1  1 
ATOM   3638 H  HD1  B TYR   A 1 161 ? 8.322  -6.371  6.109   0.36 18.52 ?  161 TYR   A HD1  1 
ATOM   3639 H  HD2  A TYR   A 1 161 ? 4.401  -5.730  6.544   0.64 17.40 ?  161 TYR   A HD2  1 
ATOM   3640 H  HD2  B TYR   A 1 161 ? 4.446  -5.436  6.467   0.36 18.30 ?  161 TYR   A HD2  1 
ATOM   3641 H  HE1  A TYR   A 1 161 ? 8.166  -8.114  7.730   0.64 17.04 ?  161 TYR   A HE1  1 
ATOM   3642 H  HE1  B TYR   A 1 161 ? 8.166  -7.735  7.972   0.36 18.77 ?  161 TYR   A HE1  1 
ATOM   3643 H  HE2  A TYR   A 1 161 ? 4.253  -7.375  8.137   0.64 16.69 ?  161 TYR   A HE2  1 
ATOM   3644 H  HE2  B TYR   A 1 161 ? 4.286  -6.799  8.331   0.36 18.63 ?  161 TYR   A HE2  1 
ATOM   3645 H  HH   A TYR   A 1 161 ? 5.334  -8.946  9.321   0.64 16.26 ?  161 TYR   A HH   1 
ATOM   3646 H  HH   B TYR   A 1 161 ? 6.864  -8.572  9.602   0.36 20.87 ?  161 TYR   A HH   1 
ATOM   3647 N  N    A ASP   A 1 162 ? 3.998  -5.912  3.519   0.64 17.56 ?  162 ASP   A N    1 
ATOM   3648 N  N    B ASP   A 1 162 ? 4.008  -6.095  3.607   0.36 16.45 ?  162 ASP   A N    1 
ATOM   3649 C  CA   A ASP   A 1 162 ? 2.852  -6.817  3.447   0.64 18.39 ?  162 ASP   A CA   1 
ATOM   3650 C  CA   B ASP   A 1 162 ? 2.842  -6.973  3.640   0.36 17.02 ?  162 ASP   A CA   1 
ATOM   3651 C  C    A ASP   A 1 162 ? 2.902  -7.661  2.181   0.64 17.89 ?  162 ASP   A C    1 
ATOM   3652 C  C    B ASP   A 1 162 ? 2.823  -7.898  2.431   0.36 17.24 ?  162 ASP   A C    1 
ATOM   3653 O  O    A ASP   A 1 162 ? 2.543  -8.844  2.197   0.64 18.42 ?  162 ASP   A O    1 
ATOM   3654 O  O    B ASP   A 1 162 ? 2.460  -9.075  2.546   0.36 17.21 ?  162 ASP   A O    1 
ATOM   3655 C  CB   A ASP   A 1 162 ? 1.538  -6.036  3.506   0.64 20.21 ?  162 ASP   A CB   1 
ATOM   3656 C  CB   B ASP   A 1 162 ? 1.557  -6.147  3.716   0.36 17.63 ?  162 ASP   A CB   1 
ATOM   3657 C  CG   A ASP   A 1 162 ? 1.258  -5.438  4.870   0.64 21.97 ?  162 ASP   A CG   1 
ATOM   3658 C  CG   B ASP   A 1 162 ? 1.301  -5.585  5.099   0.36 18.56 ?  162 ASP   A CG   1 
ATOM   3659 O  OD1  A ASP   A 1 162 ? 1.791  -5.946  5.876   0.64 22.80 ?  162 ASP   A OD1  1 
ATOM   3660 O  OD1  B ASP   A 1 162 ? 2.101  -5.862  6.018   0.36 19.33 ?  162 ASP   A OD1  1 
ATOM   3661 O  OD2  A ASP   A 1 162 ? 0.474  -4.462  4.928   0.64 23.13 -1 162 ASP   A OD2  1 
ATOM   3662 O  OD2  B ASP   A 1 162 ? 0.281  -4.880  5.266   0.36 18.81 -1 162 ASP   A OD2  1 
ATOM   3663 H  H    A ASP   A 1 162 ? 3.797  -5.075  3.506   0.64 21.07 ?  162 ASP   A H    1 
ATOM   3664 H  H    B ASP   A 1 162 ? 3.825  -5.255  3.604   0.36 19.74 ?  162 ASP   A H    1 
ATOM   3665 H  HA   A ASP   A 1 162 ? 2.876  -7.422  4.205   0.64 22.07 ?  162 ASP   A HA   1 
ATOM   3666 H  HA   B ASP   A 1 162 ? 2.886  -7.526  4.433   0.36 20.42 ?  162 ASP   A HA   1 
ATOM   3667 H  HB2  A ASP   A 1 162 ? 1.577  -5.299  2.890   0.64 24.25 ?  162 ASP   A HB2  1 
ATOM   3668 H  HB2  B ASP   A 1 162 ? 1.612  -5.411  3.086   0.36 21.16 ?  162 ASP   A HB2  1 
ATOM   3669 H  HB3  A ASP   A 1 162 ? 0.806  -6.634  3.276   0.64 24.25 ?  162 ASP   A HB3  1 
ATOM   3670 H  HB3  B ASP   A 1 162 ? 0.800  -6.711  3.505   0.36 21.16 ?  162 ASP   A HB3  1 
ATOM   3671 N  N    A LYS   A 1 163 ? 3.337  -7.069  1.067   0.64 18.58 ?  163 LYS   A N    1 
ATOM   3672 N  N    B LYS   A 1 163 ? 3.216  -7.387  1.262   0.36 17.94 ?  163 LYS   A N    1 
ATOM   3673 C  CA   A LYS   A 1 163 ? 3.420  -7.831  -0.174  0.64 19.02 ?  163 LYS   A CA   1 
ATOM   3674 C  CA   B LYS   A 1 163 ? 3.320  -8.244  0.087   0.36 18.58 ?  163 LYS   A CA   1 
ATOM   3675 C  C    A LYS   A 1 163 ? 4.467  -8.939  -0.088  0.64 18.27 ?  163 LYS   A C    1 
ATOM   3676 C  C    B LYS   A 1 163 ? 4.477  -9.226  0.227   0.36 17.86 ?  163 LYS   A C    1 
ATOM   3677 O  O    A LYS   A 1 163 ? 4.272  -10.024 -0.644  0.64 17.72 ?  163 LYS   A O    1 
ATOM   3678 O  O    B LYS   A 1 163 ? 4.347  -10.403 -0.129  0.36 17.99 ?  163 LYS   A O    1 
ATOM   3679 C  CB   A LYS   A 1 163 ? 3.711  -6.903  -1.353  0.64 21.51 ?  163 LYS   A CB   1 
ATOM   3680 C  CB   B LYS   A 1 163 ? 3.481  -7.392  -1.171  0.36 20.53 ?  163 LYS   A CB   1 
ATOM   3681 C  CG   A LYS   A 1 163 ? 3.787  -7.637  -2.682  0.64 24.23 ?  163 LYS   A CG   1 
ATOM   3682 C  CG   B LYS   A 1 163 ? 2.328  -7.510  -2.158  0.36 22.85 ?  163 LYS   A CG   1 
ATOM   3683 C  CD   A LYS   A 1 163 ? 4.207  -6.718  -3.813  0.64 26.92 ?  163 LYS   A CD   1 
ATOM   3684 C  CD   B LYS   A 1 163 ? 2.593  -6.698  -3.416  0.36 24.66 ?  163 LYS   A CD   1 
ATOM   3685 C  CE   A LYS   A 1 163 ? 4.192  -7.449  -5.146  0.64 29.09 ?  163 LYS   A CE   1 
ATOM   3686 C  CE   B LYS   A 1 163 ? 3.818  -7.208  -4.163  0.36 25.82 ?  163 LYS   A CE   1 
ATOM   3687 N  NZ   A LYS   A 1 163 ? 4.835  -6.653  -6.227  0.64 30.28 ?  163 LYS   A NZ   1 
ATOM   3688 N  NZ   B LYS   A 1 163 ? 4.137  -6.366  -5.345  0.36 26.42 ?  163 LYS   A NZ   1 
ATOM   3689 H  H    A LYS   A 1 163 ? 3.576  -6.241  1.010   0.64 22.29 ?  163 LYS   A H    1 
ATOM   3690 H  H    B LYS   A 1 163 ? 3.431  -6.564  1.127   0.36 21.53 ?  163 LYS   A H    1 
ATOM   3691 H  HA   A LYS   A 1 163 ? 2.559  -8.245  -0.333  0.64 22.82 ?  163 LYS   A HA   1 
ATOM   3692 H  HA   B LYS   A 1 163 ? 2.503  -8.756  -0.007  0.36 22.30 ?  163 LYS   A HA   1 
ATOM   3693 H  HB2  A LYS   A 1 163 ? 3.000  -6.240  -1.418  0.64 25.81 ?  163 LYS   A HB2  1 
ATOM   3694 H  HB2  B LYS   A 1 163 ? 3.553  -6.457  -0.922  0.36 24.63 ?  163 LYS   A HB2  1 
ATOM   3695 H  HB3  A LYS   A 1 163 ? 4.559  -6.458  -1.205  0.64 25.81 ?  163 LYS   A HB3  1 
ATOM   3696 H  HB3  B LYS   A 1 163 ? 4.292  -7.674  -1.616  0.36 24.63 ?  163 LYS   A HB3  1 
ATOM   3697 H  HG2  A LYS   A 1 163 ? 4.442  -8.351  -2.621  0.64 29.07 ?  163 LYS   A HG2  1 
ATOM   3698 H  HG2  B LYS   A 1 163 ? 2.217  -8.440  -2.413  0.36 27.42 ?  163 LYS   A HG2  1 
ATOM   3699 H  HG3  A LYS   A 1 163 ? 2.914  -8.003  -2.894  0.64 29.07 ?  163 LYS   A HG3  1 
ATOM   3700 H  HG3  B LYS   A 1 163 ? 1.515  -7.176  -1.745  0.36 27.42 ?  163 LYS   A HG3  1 
ATOM   3701 H  HD2  A LYS   A 1 163 ? 3.589  -5.974  -3.866  0.64 32.30 ?  163 LYS   A HD2  1 
ATOM   3702 H  HD2  B LYS   A 1 163 ? 1.826  -6.766  -4.009  0.36 29.59 ?  163 LYS   A HD2  1 
ATOM   3703 H  HD3  A LYS   A 1 163 ? 5.108  -6.400  -3.649  0.64 32.30 ?  163 LYS   A HD3  1 
ATOM   3704 H  HD3  B LYS   A 1 163 ? 2.747  -5.772  -3.173  0.36 29.59 ?  163 LYS   A HD3  1 
ATOM   3705 H  HE2  A LYS   A 1 163 ? 4.669  -8.288  -5.055  0.64 34.91 ?  163 LYS   A HE2  1 
ATOM   3706 H  HE2  B LYS   A 1 163 ? 4.593  -7.187  -3.579  0.36 30.99 ?  163 LYS   A HE2  1 
ATOM   3707 H  HE3  A LYS   A 1 163 ? 3.273  -7.619  -5.404  0.64 34.91 ?  163 LYS   A HE3  1 
ATOM   3708 H  HE3  B LYS   A 1 163 ? 3.652  -8.116  -4.463  0.36 30.99 ?  163 LYS   A HE3  1 
ATOM   3709 H  HZ1  A LYS   A 1 163 ? 4.811  -7.105  -6.993  0.64 36.34 ?  163 LYS   A HZ1  1 
ATOM   3710 H  HZ1  B LYS   A 1 163 ? 4.857  -6.687  -5.758  0.36 31.70 ?  163 LYS   A HZ1  1 
ATOM   3711 H  HZ2  A LYS   A 1 163 ? 4.402  -5.882  -6.333  0.64 36.34 ?  163 LYS   A HZ2  1 
ATOM   3712 H  HZ2  B LYS   A 1 163 ? 3.453  -6.367  -5.911  0.36 31.70 ?  163 LYS   A HZ2  1 
ATOM   3713 H  HZ3  A LYS   A 1 163 ? 5.682  -6.483  -6.017  0.64 36.34 ?  163 LYS   A HZ3  1 
ATOM   3714 H  HZ3  B LYS   A 1 163 ? 4.300  -5.530  -5.086  0.36 31.70 ?  163 LYS   A HZ3  1 
ATOM   3715 N  N    A LEU   A 1 164 ? 5.591  -8.684  0.588   0.64 17.11 ?  164 LEU   A N    1 
ATOM   3716 N  N    B LEU   A 1 164 ? 5.615  -8.757  0.744   0.36 16.93 ?  164 LEU   A N    1 
ATOM   3717 C  CA   A LEU   A 1 164 ? 6.644  -9.697  0.665   0.64 16.23 ?  164 LEU   A CA   1 
ATOM   3718 C  CA   B LEU   A 1 164 ? 6.741  -9.650  1.005   0.36 15.62 ?  164 LEU   A CA   1 
ATOM   3719 C  C    A LEU   A 1 164 ? 6.210  -10.891 1.505   0.64 16.18 ?  164 LEU   A C    1 
ATOM   3720 C  C    B LEU   A 1 164 ? 6.320  -10.791 1.919   0.36 15.40 ?  164 LEU   A C    1 
ATOM   3721 O  O    A LEU   A 1 164 ? 6.498  -12.041 1.156   0.64 16.18 ?  164 LEU   A O    1 
ATOM   3722 O  O    B LEU   A 1 164 ? 6.649  -11.957 1.673   0.36 15.14 ?  164 LEU   A O    1 
ATOM   3723 C  CB   A LEU   A 1 164 ? 7.916  -9.087  1.244   0.64 15.83 ?  164 LEU   A CB   1 
ATOM   3724 C  CB   B LEU   A 1 164 ? 7.887  -8.862  1.640   0.36 14.80 ?  164 LEU   A CB   1 
ATOM   3725 C  CG   A LEU   A 1 164 ? 8.612  -8.065  0.347   0.64 15.78 ?  164 LEU   A CG   1 
ATOM   3726 C  CG   B LEU   A 1 164 ? 8.728  -7.971  0.725   0.36 14.66 ?  164 LEU   A CG   1 
ATOM   3727 C  CD1  A LEU   A 1 164 ? 9.581  -7.212  1.149   0.64 15.22 ?  164 LEU   A CD1  1 
ATOM   3728 C  CD1  B LEU   A 1 164 ? 9.601  -7.065  1.563   0.36 14.74 ?  164 LEU   A CD1  1 
ATOM   3729 C  CD2  A LEU   A 1 164 ? 9.341  -8.768  -0.781  0.64 16.21 ?  164 LEU   A CD2  1 
ATOM   3730 C  CD2  B LEU   A 1 164 ? 9.586  -8.799  -0.217  0.36 14.17 ?  164 LEU   A CD2  1 
ATOM   3731 H  H    A LEU   A 1 164 ? 5.764  -7.948  1.008   0.64 20.53 ?  164 LEU   A H    1 
ATOM   3732 H  H    B LEU   A 1 164 ? 5.753  -7.936  0.961   0.36 20.31 ?  164 LEU   A H    1 
ATOM   3733 H  HA   A LEU   A 1 164 ? 6.838  -10.013 -0.227  0.64 19.48 ?  164 LEU   A HA   1 
ATOM   3734 H  HA   B LEU   A 1 164 ? 7.056  -10.023 0.168   0.36 18.75 ?  164 LEU   A HA   1 
ATOM   3735 H  HB2  A LEU   A 1 164 ? 7.697  -8.644  2.077   0.64 18.99 ?  164 LEU   A HB2  1 
ATOM   3736 H  HB2  B LEU   A 1 164 ? 7.513  -8.287  2.326   0.36 17.76 ?  164 LEU   A HB2  1 
ATOM   3737 H  HB3  A LEU   A 1 164 ? 8.549  -9.804  1.414   0.64 18.99 ?  164 LEU   A HB3  1 
ATOM   3738 H  HB3  B LEU   A 1 164 ? 8.496  -9.493  2.052   0.36 17.76 ?  164 LEU   A HB3  1 
ATOM   3739 H  HG   A LEU   A 1 164 ? 7.946  -7.477  -0.042  0.64 18.93 ?  164 LEU   A HG   1 
ATOM   3740 H  HG   B LEU   A 1 164 ? 8.146  -7.412  0.189   0.36 17.59 ?  164 LEU   A HG   1 
ATOM   3741 H  HD11 A LEU   A 1 164 ? 10.011 -6.578  0.556   0.64 18.26 ?  164 LEU   A HD11 1 
ATOM   3742 H  HD11 B LEU   A 1 164 ? 9.927  -6.335  1.014   0.36 17.68 ?  164 LEU   A HD11 1 
ATOM   3743 H  HD12 A LEU   A 1 164 ? 9.088  -6.738  1.839   0.64 18.26 ?  164 LEU   A HD12 1 
ATOM   3744 H  HD12 B LEU   A 1 164 ? 9.071  -6.717  2.297   0.36 17.68 ?  164 LEU   A HD12 1 
ATOM   3745 H  HD13 A LEU   A 1 164 ? 10.246 -7.789  1.557   0.64 18.26 ?  164 LEU   A HD13 1 
ATOM   3746 H  HD13 B LEU   A 1 164 ? 10.344 -7.580  1.912   0.36 17.68 ?  164 LEU   A HD13 1 
ATOM   3747 H  HD21 A LEU   A 1 164 ? 9.803  -8.106  -1.318  0.64 19.45 ?  164 LEU   A HD21 1 
ATOM   3748 H  HD21 B LEU   A 1 164 ? 10.136 -8.204  -0.751  0.36 17.01 ?  164 LEU   A HD21 1 
ATOM   3749 H  HD22 A LEU   A 1 164 ? 9.980  -9.392  -0.402  0.64 19.45 ?  164 LEU   A HD22 1 
ATOM   3750 H  HD22 B LEU   A 1 164 ? 10.149 -9.389  0.306   0.36 17.01 ?  164 LEU   A HD22 1 
ATOM   3751 H  HD23 A LEU   A 1 164 ? 8.695  -9.245  -1.324  0.64 19.45 ?  164 LEU   A HD23 1 
ATOM   3752 H  HD23 B LEU   A 1 164 ? 9.005  -9.319  -0.793  0.36 17.01 ?  164 LEU   A HD23 1 
ATOM   3753 N  N    A VAL   A 1 165 ? 5.533  -10.634 2.622   0.64 15.60 ?  165 VAL   A N    1 
ATOM   3754 N  N    B VAL   A 1 165 ? 5.599  -10.466 2.992   0.36 15.19 ?  165 VAL   A N    1 
ATOM   3755 C  CA   A VAL   A 1 165 ? 5.070  -11.716 3.486   0.64 15.21 ?  165 VAL   A CA   1 
ATOM   3756 C  CA   B VAL   A 1 165 ? 5.091  -11.502 3.884   0.36 15.38 ?  165 VAL   A CA   1 
ATOM   3757 C  C    A VAL   A 1 165 ? 4.040  -12.567 2.757   0.64 15.12 ?  165 VAL   A C    1 
ATOM   3758 C  C    B VAL   A 1 165 ? 4.065  -12.369 3.169   0.36 15.04 ?  165 VAL   A C    1 
ATOM   3759 O  O    A VAL   A 1 165 ? 4.155  -13.797 2.687   0.64 15.03 ?  165 VAL   A O    1 
ATOM   3760 O  O    B VAL   A 1 165 ? 4.131  -13.604 3.218   0.36 14.45 ?  165 VAL   A O    1 
ATOM   3761 C  CB   A VAL   A 1 165 ? 4.507  -11.132 4.796   0.64 15.51 ?  165 VAL   A CB   1 
ATOM   3762 C  CB   B VAL   A 1 165 ? 4.512  -10.873 5.163   0.36 15.84 ?  165 VAL   A CB   1 
ATOM   3763 C  CG1  A VAL   A 1 165 ? 3.799  -12.208 5.618   0.64 15.81 ?  165 VAL   A CG1  1 
ATOM   3764 C  CG1  B VAL   A 1 165 ? 3.669  -11.892 5.920   0.36 16.04 ?  165 VAL   A CG1  1 
ATOM   3765 C  CG2  A VAL   A 1 165 ? 5.614  -10.453 5.600   0.64 15.79 ?  165 VAL   A CG2  1 
ATOM   3766 C  CG2  B VAL   A 1 165 ? 5.633  -10.336 6.037   0.36 16.18 ?  165 VAL   A CG2  1 
ATOM   3767 H  H    A VAL   A 1 165 ? 5.316  -9.852  2.898   0.64 18.72 ?  165 VAL   A H    1 
ATOM   3768 H  H    B VAL   A 1 165 ? 5.406  -9.659  3.227   0.36 18.23 ?  165 VAL   A H    1 
ATOM   3769 H  HA   A VAL   A 1 165 ? 5.819  -12.288 3.715   0.64 18.25 ?  165 VAL   A HA   1 
ATOM   3770 H  HA   B VAL   A 1 165 ? 5.826  -12.073 4.142   0.36 18.46 ?  165 VAL   A HA   1 
ATOM   3771 H  HB   A VAL   A 1 165 ? 3.852  -10.454 4.579   0.64 18.61 ?  165 VAL   A HB   1 
ATOM   3772 H  HB   B VAL   A 1 165 ? 3.938  -10.129 4.921   0.36 19.01 ?  165 VAL   A HB   1 
ATOM   3773 H  HG11 A VAL   A 1 165 ? 3.687  -11.888 6.528   0.64 18.97 ?  165 VAL   A HG11 1 
ATOM   3774 H  HG11 B VAL   A 1 165 ? 3.554  -11.587 6.832   0.36 19.25 ?  165 VAL   A HG11 1 
ATOM   3775 H  HG12 A VAL   A 1 165 ? 2.928  -12.384 5.226   0.64 18.97 ?  165 VAL   A HG12 1 
ATOM   3776 H  HG12 B VAL   A 1 165 ? 2.803  -11.973 5.487   0.36 19.25 ?  165 VAL   A HG12 1 
ATOM   3777 H  HG13 A VAL   A 1 165 ? 4.335  -13.014 5.616   0.64 18.97 ?  165 VAL   A HG13 1 
ATOM   3778 H  HG13 B VAL   A 1 165 ? 4.126  -12.747 5.912   0.36 19.25 ?  165 VAL   A HG13 1 
ATOM   3779 H  HG21 A VAL   A 1 165 ? 5.241  -10.104 6.427   0.64 18.95 ?  165 VAL   A HG21 1 
ATOM   3780 H  HG21 B VAL   A 1 165 ? 5.249  -9.940  6.834   0.36 19.42 ?  165 VAL   A HG21 1 
ATOM   3781 H  HG22 A VAL   A 1 165 ? 6.307  -11.102 5.802   0.64 18.95 ?  165 VAL   A HG22 1 
ATOM   3782 H  HG22 B VAL   A 1 165 ? 6.221  -11.068 6.279   0.36 19.42 ?  165 VAL   A HG22 1 
ATOM   3783 H  HG23 A VAL   A 1 165 ? 5.986  -9.725  5.076   0.64 18.95 ?  165 VAL   A HG23 1 
ATOM   3784 H  HG23 B VAL   A 1 165 ? 6.126  -9.665  5.538   0.36 19.42 ?  165 VAL   A HG23 1 
ATOM   3785 N  N    A SER   A 1 166 ? 3.016  -11.917 2.200   0.64 16.03 ?  166 SER   A N    1 
ATOM   3786 N  N    B SER   A 1 166 ? 3.096  -11.739 2.499   0.36 15.65 ?  166 SER   A N    1 
ATOM   3787 C  CA   A SER   A 1 166 ? 1.902  -12.637 1.591   0.64 16.80 ?  166 SER   A CA   1 
ATOM   3788 C  CA   B SER   A 1 166 ? 1.955  -12.500 1.998   0.36 16.24 ?  166 SER   A CA   1 
ATOM   3789 C  C    A SER   A 1 166 ? 2.346  -13.433 0.376   0.64 17.48 ?  166 SER   A C    1 
ATOM   3790 C  C    B SER   A 1 166 ? 2.359  -13.507 0.925   0.36 16.59 ?  166 SER   A C    1 
ATOM   3791 O  O    A SER   A 1 166 ? 1.691  -14.417 0.010   0.64 18.50 ?  166 SER   A O    1 
ATOM   3792 O  O    B SER   A 1 166 ? 1.755  -14.581 0.830   0.36 16.95 ?  166 SER   A O    1 
ATOM   3793 C  CB   A SER   A 1 166 ? 0.802  -11.652 1.180   0.64 17.42 ?  166 SER   A CB   1 
ATOM   3794 C  CB   B SER   A 1 166 ? 0.845  -11.557 1.513   0.36 16.85 ?  166 SER   A CB   1 
ATOM   3795 O  OG   A SER   A 1 166 ? 0.178  -11.042 2.303   0.64 18.22 ?  166 SER   A OG   1 
ATOM   3796 O  OG   B SER   A 1 166 ? 1.186  -10.905 0.304   0.36 17.56 ?  166 SER   A OG   1 
ATOM   3797 H  H    A SER   A 1 166 ? 2.940  -11.070 2.169   0.64 19.23 ?  166 SER   A H    1 
ATOM   3798 H  H    B SER   A 1 166 ? 3.066  -10.890 2.335   0.36 18.78 ?  166 SER   A H    1 
ATOM   3799 H  HA   A SER   A 1 166 ? 1.518  -13.258 2.234   0.64 20.16 ?  166 SER   A HA   1 
ATOM   3800 H  HA   B SER   A 1 166 ? 1.581  -13.006 2.731   0.36 19.49 ?  166 SER   A HA   1 
ATOM   3801 H  HB2  A SER   A 1 166 ? 1.192  -10.970 0.610   0.64 20.90 ?  166 SER   A HB2  1 
ATOM   3802 H  HB2  B SER   A 1 166 ? 0.035  -12.070 1.356   0.36 20.22 ?  166 SER   A HB2  1 
ATOM   3803 H  HB3  A SER   A 1 166 ? 0.113  -12.130 0.692   0.64 20.90 ?  166 SER   A HB3  1 
ATOM   3804 H  HB3  B SER   A 1 166 ? 0.671  -10.889 2.204   0.36 20.22 ?  166 SER   A HB3  1 
ATOM   3805 H  HG   A SER   A 1 166 ? -0.392 -10.481 2.048   0.64 21.86 ?  166 SER   A HG   1 
ATOM   3806 H  HG   B SER   A 1 166 ? 0.573  -10.375 0.076   0.36 21.07 ?  166 SER   A HG   1 
ATOM   3807 N  N    A SER   A 1 167 ? 3.431  -13.015 -0.274  0.64 16.84 ?  167 SER   A N    1 
ATOM   3808 N  N    B SER   A 1 167 ? 3.393  -13.213 0.139   0.36 17.26 ?  167 SER   A N    1 
ATOM   3809 C  CA   A SER   A 1 167 ? 3.950  -13.707 -1.443  0.64 17.48 ?  167 SER   A CA   1 
ATOM   3810 C  CA   B SER   A 1 167 ? 3.715  -14.030 -1.025  0.36 18.09 ?  167 SER   A CA   1 
ATOM   3811 C  C    A SER   A 1 167 ? 5.110  -14.635 -1.110  0.64 17.72 ?  167 SER   A C    1 
ATOM   3812 C  C    B SER   A 1 167 ? 4.892  -14.975 -0.801  0.36 18.56 ?  167 SER   A C    1 
ATOM   3813 O  O    A SER   A 1 167 ? 5.632  -15.298 -2.013  0.64 18.72 ?  167 SER   A O    1 
ATOM   3814 O  O    B SER   A 1 167 ? 5.387  -15.565 -1.767  0.36 19.06 ?  167 SER   A O    1 
ATOM   3815 C  CB   A SER   A 1 167 ? 4.388  -12.693 -2.512  0.64 17.65 ?  167 SER   A CB   1 
ATOM   3816 C  CB   B SER   A 1 167 ? 3.967  -13.144 -2.250  0.36 19.13 ?  167 SER   A CB   1 
ATOM   3817 O  OG   A SER   A 1 167 ? 5.435  -11.860 -2.028  0.64 18.25 ?  167 SER   A OG   1 
ATOM   3818 O  OG   B SER   A 1 167 ? 5.106  -12.322 -2.063  0.36 20.17 ?  167 SER   A OG   1 
ATOM   3819 H  H    A SER   A 1 167 ? 3.875  -12.313 -0.057  0.64 20.21 ?  167 SER   A H    1 
ATOM   3820 H  H    B SER   A 1 167 ? 3.928  -12.552 0.271   0.36 20.71 ?  167 SER   A H    1 
ATOM   3821 H  HA   A SER   A 1 167 ? 3.240  -14.241 -1.826  0.64 20.97 ?  167 SER   A HA   1 
ATOM   3822 H  HA   B SER   A 1 167 ? 2.946  -14.579 -1.230  0.36 21.70 ?  167 SER   A HA   1 
ATOM   3823 H  HB2  A SER   A 1 167 ? 4.709  -13.177 -3.290  0.64 21.18 ?  167 SER   A HB2  1 
ATOM   3824 H  HB2  B SER   A 1 167 ? 4.112  -13.713 -3.022  0.36 22.96 ?  167 SER   A HB2  1 
ATOM   3825 H  HB3  A SER   A 1 167 ? 3.620  -12.148 -2.763  0.64 21.18 ?  167 SER   A HB3  1 
ATOM   3826 H  HB3  B SER   A 1 167 ? 3.185  -12.584 -2.399  0.36 22.96 ?  167 SER   A HB3  1 
ATOM   3827 H  HG   A SER   A 1 167 ? 5.148  -11.413 -1.369  0.64 21.90 ?  167 SER   A HG   1 
ATOM   3828 H  HG   B SER   A 1 167 ? 4.983  -11.810 -1.407  0.36 24.21 ?  167 SER   A HG   1 
ATOM   3829 N  N    A PHE   A 1 168 ? 5.536  -14.691 0.150   0.64 17.25 ?  168 PHE   A N    1 
ATOM   3830 N  N    B PHE   A 1 168 ? 5.333  -15.162 0.442   0.36 18.58 ?  168 PHE   A N    1 
ATOM   3831 C  CA   A PHE   A 1 168 ? 6.697  -15.503 0.496   0.64 17.56 ?  168 PHE   A CA   1 
ATOM   3832 C  CA   B PHE   A 1 168 ? 6.525  -15.967 0.698   0.36 19.28 ?  168 PHE   A CA   1 
ATOM   3833 C  C    A PHE   A 1 168 ? 6.373  -16.986 0.391   0.64 18.39 ?  168 PHE   A C    1 
ATOM   3834 C  C    B PHE   A 1 168 ? 6.205  -17.441 0.491   0.36 22.14 ?  168 PHE   A C    1 
ATOM   3835 O  O    A PHE   A 1 168 ? 5.341  -17.449 0.893   0.64 20.64 ?  168 PHE   A O    1 
ATOM   3836 O  O    B PHE   A 1 168 ? 5.496  -18.054 1.296   0.36 21.83 ?  168 PHE   A O    1 
ATOM   3837 C  CB   A PHE   A 1 168 ? 7.183  -15.202 1.911   0.64 17.13 ?  168 PHE   A CB   1 
ATOM   3838 C  CB   B PHE   A 1 168 ? 7.053  -15.722 2.107   0.36 17.64 ?  168 PHE   A CB   1 
ATOM   3839 C  CG   A PHE   A 1 168 ? 8.453  -15.924 2.255   0.64 16.77 ?  168 PHE   A CG   1 
ATOM   3840 C  CG   B PHE   A 1 168 ? 8.345  -16.434 2.393   0.36 16.18 ?  168 PHE   A CG   1 
ATOM   3841 C  CD1  A PHE   A 1 168 ? 9.649  -15.519 1.695   0.64 16.88 ?  168 PHE   A CD1  1 
ATOM   3842 C  CD1  B PHE   A 1 168 ? 9.511  -16.066 1.741   0.36 15.84 ?  168 PHE   A CD1  1 
ATOM   3843 C  CD2  A PHE   A 1 168 ? 8.456  -17.024 3.099   0.64 16.60 ?  168 PHE   A CD2  1 
ATOM   3844 C  CD2  B PHE   A 1 168 ? 8.394  -17.475 3.305   0.36 15.72 ?  168 PHE   A CD2  1 
ATOM   3845 C  CE1  A PHE   A 1 168 ? 10.825 -16.182 1.983   0.64 16.57 ?  168 PHE   A CE1  1 
ATOM   3846 C  CE1  B PHE   A 1 168 ? 10.700 -16.721 1.995   0.36 15.49 ?  168 PHE   A CE1  1 
ATOM   3847 C  CE2  A PHE   A 1 168 ? 9.636  -17.687 3.393   0.64 16.85 ?  168 PHE   A CE2  1 
ATOM   3848 C  CE2  B PHE   A 1 168 ? 9.582  -18.132 3.565   0.36 15.69 ?  168 PHE   A CE2  1 
ATOM   3849 C  CZ   A PHE   A 1 168 ? 10.818 -17.265 2.834   0.64 16.66 ?  168 PHE   A CZ   1 
ATOM   3850 C  CZ   B PHE   A 1 168 ? 10.735 -17.754 2.908   0.36 15.76 ?  168 PHE   A CZ   1 
ATOM   3851 H  H    A PHE   A 1 168 ? 5.196  -14.250 0.806   0.64 20.70 ?  168 PHE   A H    1 
ATOM   3852 H  H    B PHE   A 1 168 ? 4.962  -14.840 1.148   0.36 22.30 ?  168 PHE   A H    1 
ATOM   3853 H  HA   A PHE   A 1 168 ? 7.424  -15.296 -0.120  0.64 21.08 ?  168 PHE   A HA   1 
ATOM   3854 H  HA   B PHE   A 1 168 ? 7.214  -15.723 0.066   0.36 23.14 ?  168 PHE   A HA   1 
ATOM   3855 H  HB2  A PHE   A 1 168 ? 7.346  -14.249 1.997   0.64 20.55 ?  168 PHE   A HB2  1 
ATOM   3856 H  HB2  B PHE   A 1 168 ? 7.204  -14.773 2.220   0.36 21.17 ?  168 PHE   A HB2  1 
ATOM   3857 H  HB3  A PHE   A 1 168 ? 6.502  -15.480 2.542   0.64 20.55 ?  168 PHE   A HB3  1 
ATOM   3858 H  HB3  B PHE   A 1 168 ? 6.394  -16.033 2.747   0.36 21.17 ?  168 PHE   A HB3  1 
ATOM   3859 H  HD1  A PHE   A 1 168 ? 9.667  -14.786 1.120   0.64 20.26 ?  168 PHE   A HD1  1 
ATOM   3860 H  HD1  B PHE   A 1 168 ? 9.493  -15.372 1.123   0.36 19.01 ?  168 PHE   A HD1  1 
ATOM   3861 H  HD2  A PHE   A 1 168 ? 7.660  -17.311 3.481   0.64 19.92 ?  168 PHE   A HD2  1 
ATOM   3862 H  HD2  B PHE   A 1 168 ? 7.618  -17.735 3.748   0.36 18.86 ?  168 PHE   A HD2  1 
ATOM   3863 H  HE1  A PHE   A 1 168 ? 11.631 -15.894 1.606   0.64 19.88 ?  168 PHE   A HE1  1 
ATOM   3864 H  HE1  B PHE   A 1 168 ? 11.477 -16.465 1.552   0.36 18.58 ?  168 PHE   A HE1  1 
ATOM   3865 H  HE2  A PHE   A 1 168 ? 9.628  -18.419 3.966   0.64 20.22 ?  168 PHE   A HE2  1 
ATOM   3866 H  HE2  B PHE   A 1 168 ? 9.602  -18.831 4.180   0.36 18.83 ?  168 PHE   A HE2  1 
ATOM   3867 H  HZ   A PHE   A 1 168 ? 11.614 -17.711 3.030   0.64 19.99 ?  168 PHE   A HZ   1 
ATOM   3868 H  HZ   B PHE   A 1 168 ? 11.536 -18.197 3.082   0.36 18.91 ?  168 PHE   A HZ   1 
ATOM   3869 N  N    A LEU   A 1 169 ? 7.283  -17.737 -0.227  0.64 19.33 ?  169 LEU   A N    1 
ATOM   3870 N  N    B LEU   A 1 169 ? 6.749  -18.015 -0.576  0.36 25.82 ?  169 LEU   A N    1 
ATOM   3871 C  CA   A LEU   A 1 169 ? 7.091  -19.167 -0.390  0.64 22.19 ?  169 LEU   A CA   1 
ATOM   3872 C  CA   B LEU   A 1 169 ? 6.475  -19.397 -0.929  0.36 28.89 ?  169 LEU   A CA   1 
ATOM   3873 C  C    A LEU   A 1 169 ? 7.915  -19.926 0.630   0.64 22.68 ?  169 LEU   A C    1 
ATOM   3874 C  C    B LEU   A 1 169 ? 7.173  -20.347 0.039   0.36 30.62 ?  169 LEU   A C    1 
ATOM   3875 O  O    A LEU   A 1 169 ? 7.357  -20.424 1.611   0.64 23.29 ?  169 LEU   A O    1 
ATOM   3876 O  O    B LEU   A 1 169 ? 6.526  -21.032 0.832   0.36 31.20 ?  169 LEU   A O    1 
ATOM   3877 C  CB   A LEU   A 1 169 ? 7.423  -19.604 -1.823  0.64 24.01 ?  169 LEU   A CB   1 
ATOM   3878 C  CB   B LEU   A 1 169 ? 6.954  -19.672 -2.360  0.36 29.90 ?  169 LEU   A CB   1 
ATOM   3879 C  CG   A LEU   A 1 169 ? 7.147  -21.074 -2.162  0.64 25.60 ?  169 LEU   A CG   1 
ATOM   3880 C  CG   B LEU   A 1 169 ? 6.178  -20.670 -3.228  0.36 30.66 ?  169 LEU   A CG   1 
ATOM   3881 C  CD1  A LEU   A 1 169 ? 5.740  -21.474 -1.746  0.64 26.20 ?  169 LEU   A CD1  1 
ATOM   3882 C  CD1  B LEU   A 1 169 ? 5.052  -21.349 -2.461  0.36 31.01 ?  169 LEU   A CD1  1 
ATOM   3883 C  CD2  A LEU   A 1 169 ? 7.352  -21.340 -3.649  0.64 26.04 ?  169 LEU   A CD2  1 
ATOM   3884 C  CD2  B LEU   A 1 169 ? 5.639  -19.972 -4.470  0.36 30.83 ?  169 LEU   A CD2  1 
ATOM   3885 O  OXT  A LEU   A 1 169 ? 9.134  -20.043 0.505   0.64 21.94 -1 169 LEU   A OXT  1 
ATOM   3886 O  OXT  B LEU   A 1 169 ? 8.402  -20.447 0.053   0.36 31.38 -1 169 LEU   A OXT  1 
ATOM   3887 H  H    A LEU   A 1 169 ? 8.023  -17.437 -0.559  0.64 23.20 ?  169 LEU   A H    1 
ATOM   3888 H  H    B LEU   A 1 169 ? 7.282  -17.620 -1.119  0.36 30.98 ?  169 LEU   A H    1 
ATOM   3889 H  HA   A LEU   A 1 169 ? 6.174  -19.386 -0.207  0.64 26.63 ?  169 LEU   A HA   1 
ATOM   3890 H  HA   B LEU   A 1 169 ? 5.519  -19.537 -0.864  0.36 34.67 ?  169 LEU   A HA   1 
ATOM   3891 H  HB2  A LEU   A 1 169 ? 6.892  -19.067 -2.434  0.64 28.82 ?  169 LEU   A HB2  1 
ATOM   3892 H  HB2  B LEU   A 1 169 ? 6.957  -18.829 -2.838  0.36 35.88 ?  169 LEU   A HB2  1 
ATOM   3893 H  HB3  A LEU   A 1 169 ? 8.363  -19.445 -1.990  0.64 28.82 ?  169 LEU   A HB3  1 
ATOM   3894 H  HB3  B LEU   A 1 169 ? 7.866  -20.004 -2.306  0.36 35.88 ?  169 LEU   A HB3  1 
ATOM   3895 H  HG   A LEU   A 1 169 ? 7.771  -21.634 -1.675  0.64 30.72 ?  169 LEU   A HG   1 
ATOM   3896 H  HG   B LEU   A 1 169 ? 6.789  -21.362 -3.526  0.36 36.79 ?  169 LEU   A HG   1 
ATOM   3897 H  HD11 A LEU   A 1 169 ? 5.524  -22.333 -2.141  0.64 31.44 ?  169 LEU   A HD11 1 
ATOM   3898 H  HD11 B LEU   A 1 169 ? 4.662  -22.033 -3.018  0.36 37.21 ?  169 LEU   A HD11 1 
ATOM   3899 H  HD12 A LEU   A 1 169 ? 5.702  -21.537 -0.779  0.64 31.44 ?  169 LEU   A HD12 1 
ATOM   3900 H  HD12 B LEU   A 1 169 ? 5.413  -21.743 -1.651  0.36 37.21 ?  169 LEU   A HD12 1 
ATOM   3901 H  HD13 A LEU   A 1 169 ? 5.115  -20.801 -2.060  0.64 31.44 ?  169 LEU   A HD13 1 
ATOM   3902 H  HD13 B LEU   A 1 169 ? 4.381  -20.686 -2.234  0.36 37.21 ?  169 LEU   A HD13 1 
ATOM   3903 H  HD21 A LEU   A 1 169 ? 7.177  -22.278 -3.831  0.64 31.25 ?  169 LEU   A HD21 1 
ATOM   3904 H  HD21 B LEU   A 1 169 ? 5.113  -20.605 -4.984  0.36 36.99 ?  169 LEU   A HD21 1 
ATOM   3905 H  HD22 A LEU   A 1 169 ? 6.737  -20.787 -4.157  0.64 31.25 ?  169 LEU   A HD22 1 
ATOM   3906 H  HD22 B LEU   A 1 169 ? 5.084  -19.225 -4.197  0.36 36.99 ?  169 LEU   A HD22 1 
ATOM   3907 H  HD23 A LEU   A 1 169 ? 8.266  -21.122 -3.886  0.64 31.25 ?  169 LEU   A HD23 1 
ATOM   3908 H  HD23 B LEU   A 1 169 ? 6.385  -19.653 -5.003  0.36 36.99 ?  169 LEU   A HD23 1 
ATOM   3909 N  N    A SER   B 1 1   ? 50.854 -9.261  -23.733 0.64 27.82 ?  1   SER   B N    1 
ATOM   3910 N  N    B SER   B 1 1   ? 50.788 -9.260  -23.727 0.36 25.87 ?  1   SER   B N    1 
ATOM   3911 C  CA   A SER   B 1 1   ? 51.341 -10.314 -22.819 0.64 27.83 ?  1   SER   B CA   1 
ATOM   3912 C  CA   B SER   B 1 1   ? 51.290 -10.271 -22.774 0.36 25.71 ?  1   SER   B CA   1 
ATOM   3913 C  C    A SER   B 1 1   ? 50.259 -11.352 -22.559 0.64 26.77 ?  1   SER   B C    1 
ATOM   3914 C  C    B SER   B 1 1   ? 50.242 -11.344 -22.541 0.36 24.78 ?  1   SER   B C    1 
ATOM   3915 O  O    A SER   B 1 1   ? 49.073 -11.139 -22.839 0.64 26.44 ?  1   SER   B O    1 
ATOM   3916 O  O    B SER   B 1 1   ? 49.056 -11.161 -22.835 0.36 24.67 ?  1   SER   B O    1 
ATOM   3917 C  CB   A SER   B 1 1   ? 51.806 -9.712  -21.496 0.64 28.67 ?  1   SER   B CB   1 
ATOM   3918 C  CB   B SER   B 1 1   ? 51.665 -9.624  -21.445 0.36 26.29 ?  1   SER   B CB   1 
ATOM   3919 O  OG   A SER   B 1 1   ? 50.702 -9.386  -20.674 0.64 30.32 ?  1   SER   B OG   1 
ATOM   3920 O  OG   B SER   B 1 1   ? 50.526 -9.478  -20.617 0.36 27.32 ?  1   SER   B OG   1 
ATOM   3921 H  H1   A SER   B 1 1   ? 50.768 -9.603  -24.548 0.64 33.39 ?  1   SER   B H1   1 
ATOM   3922 H  H1   B SER   B 1 1   ? 50.690 -9.639  -24.524 0.36 31.04 ?  1   SER   B H1   1 
ATOM   3923 H  H2   A SER   B 1 1   ? 50.071 -8.966  -23.444 0.64 33.39 ?  1   SER   B H2   1 
ATOM   3924 H  H2   B SER   B 1 1   ? 50.009 -8.953  -23.439 0.36 31.04 ?  1   SER   B H2   1 
ATOM   3925 H  H3   A SER   B 1 1   ? 51.444 -8.597  -23.745 0.64 33.39 ?  1   SER   B H3   1 
ATOM   3926 H  H3   B SER   B 1 1   ? 51.377 -8.599  -23.778 0.36 31.04 ?  1   SER   B H3   1 
ATOM   3927 H  HA   A SER   B 1 1   ? 52.093 -10.752 -23.238 0.64 33.39 ?  1   SER   B HA   1 
ATOM   3928 H  HA   B SER   B 1 1   ? 52.077 -10.684 -23.151 0.36 30.86 ?  1   SER   B HA   1 
ATOM   3929 H  HB2  A SER   B 1 1   ? 52.363 -10.362 -21.042 0.64 34.41 ?  1   SER   B HB2  1 
ATOM   3930 H  HB2  B SER   B 1 1   ? 52.318 -10.187 -21.003 0.36 31.55 ?  1   SER   B HB2  1 
ATOM   3931 H  HB3  A SER   B 1 1   ? 52.313 -8.906  -21.675 0.64 34.41 ?  1   SER   B HB3  1 
ATOM   3932 H  HB3  B SER   B 1 1   ? 52.041 -8.747  -21.615 0.36 31.55 ?  1   SER   B HB3  1 
ATOM   3933 H  HG   A SER   B 1 1   ? 50.964 -8.933  -20.016 0.64 36.38 ?  1   SER   B HG   1 
ATOM   3934 H  HG   B SER   B 1 1   ? 50.707 -8.967  -19.976 0.36 32.78 ?  1   SER   B HG   1 
ATOM   3935 N  N    A MET   B 1 2   ? 50.689 -12.476 -22.003 0.64 26.23 ?  2   MET   B N    1 
ATOM   3936 N  N    B MET   B 1 2   ? 50.693 -12.465 -21.997 0.36 23.99 ?  2   MET   B N    1 
ATOM   3937 C  CA   A MET   B 1 2   ? 49.859 -13.662 -21.842 0.64 26.25 ?  2   MET   B CA   1 
ATOM   3938 C  CA   B MET   B 1 2   ? 49.869 -13.651 -21.816 0.36 23.56 ?  2   MET   B CA   1 
ATOM   3939 C  C    A MET   B 1 2   ? 49.605 -13.873 -20.355 0.64 23.82 ?  2   MET   B C    1 
ATOM   3940 C  C    B MET   B 1 2   ? 49.613 -13.824 -20.330 0.36 22.44 ?  2   MET   B C    1 
ATOM   3941 O  O    A MET   B 1 2   ? 50.532 -14.185 -19.600 0.64 24.04 ?  2   MET   B O    1 
ATOM   3942 O  O    B MET   B 1 2   ? 50.547 -14.056 -19.555 0.36 22.51 ?  2   MET   B O    1 
ATOM   3943 C  CB   A MET   B 1 2   ? 50.581 -14.859 -22.449 0.64 30.00 ?  2   MET   B CB   1 
ATOM   3944 C  CB   B MET   B 1 2   ? 50.603 -14.854 -22.381 0.36 25.20 ?  2   MET   B CB   1 
ATOM   3945 C  CG   A MET   B 1 2   ? 49.736 -16.111 -22.595 0.64 33.48 ?  2   MET   B CG   1 
ATOM   3946 C  CG   B MET   B 1 2   ? 49.712 -16.016 -22.801 0.36 26.49 ?  2   MET   B CG   1 
ATOM   3947 S  SD   A MET   B 1 2   ? 50.595 -17.363 -23.567 0.64 36.71 ?  2   MET   B SD   1 
ATOM   3948 S  SD   B MET   B 1 2   ? 50.585 -17.102 -23.935 0.36 27.69 ?  2   MET   B SD   1 
ATOM   3949 C  CE   A MET   B 1 2   ? 51.123 -16.360 -24.953 0.64 37.09 ?  2   MET   B CE   1 
ATOM   3950 C  CE   B MET   B 1 2   ? 51.583 -15.905 -24.794 0.36 27.85 ?  2   MET   B CE   1 
ATOM   3951 H  H    A MET   B 1 2   ? 51.489 -12.582 -21.704 0.64 31.48 ?  2   MET   B H    1 
ATOM   3952 H  H    B MET   B 1 2   ? 51.502 -12.574 -21.719 0.36 28.79 ?  2   MET   B H    1 
ATOM   3953 H  HA   A MET   B 1 2   ? 49.020 -13.545 -22.311 0.64 31.50 ?  2   MET   B HA   1 
ATOM   3954 H  HA   B MET   B 1 2   ? 49.036 -13.561 -22.303 0.36 28.28 ?  2   MET   B HA   1 
ATOM   3955 H  HB2  A MET   B 1 2   ? 50.891 -14.585 -23.323 0.64 36.01 ?  2   MET   B HB2  1 
ATOM   3956 H  HB2  B MET   B 1 2   ? 51.076 -14.483 -23.131 0.36 30.24 ?  2   MET   B HB2  1 
ATOM   3957 H  HB3  A MET   B 1 2   ? 51.340 -15.093 -21.895 0.64 36.01 ?  2   MET   B HB3  1 
ATOM   3958 H  HB3  B MET   B 1 2   ? 51.234 -15.208 -21.743 0.36 30.24 ?  2   MET   B HB3  1 
ATOM   3959 H  HG2  A MET   B 1 2   ? 49.554 -16.479 -21.714 0.64 40.18 ?  2   MET   B HG2  1 
ATOM   3960 H  HG2  B MET   B 1 2   ? 49.454 -16.531 -22.012 0.36 31.79 ?  2   MET   B HG2  1 
ATOM   3961 H  HG3  A MET   B 1 2   ? 48.907 -15.893 -23.048 0.64 40.18 ?  2   MET   B HG3  1 
ATOM   3962 H  HG3  B MET   B 1 2   ? 48.924 -15.691 -23.257 0.36 31.79 ?  2   MET   B HG3  1 
ATOM   3963 H  HE1  A MET   B 1 2   ? 51.288 -16.933 -25.707 0.64 44.51 ?  2   MET   B HE1  1 
ATOM   3964 H  HE1  B MET   B 1 2   ? 51.899 -16.328 -25.572 0.36 33.43 ?  2   MET   B HE1  1 
ATOM   3965 H  HE2  A MET   B 1 2   ? 50.418 -15.722 -25.163 0.64 44.51 ?  2   MET   B HE2  1 
ATOM   3966 H  HE2  B MET   B 1 2   ? 51.027 -15.139 -25.032 0.36 33.43 ?  2   MET   B HE2  1 
ATOM   3967 H  HE3  A MET   B 1 2   ? 51.935 -15.879 -24.712 0.64 44.51 ?  2   MET   B HE3  1 
ATOM   3968 H  HE3  B MET   B 1 2   ? 52.336 -15.625 -24.234 0.36 33.43 ?  2   MET   B HE3  1 
ATOM   3969 N  N    . VAL   B 1 3   ? 48.353 -13.694 -19.937 1.00 21.32 ?  3   VAL   B N    1 
ATOM   3970 C  CA   . VAL   B 1 3   ? 47.939 -13.931 -18.563 1.00 19.86 ?  3   VAL   B CA   1 
ATOM   3971 C  C    . VAL   B 1 3   ? 46.707 -14.825 -18.592 1.00 18.06 ?  3   VAL   B C    1 
ATOM   3972 O  O    . VAL   B 1 3   ? 45.975 -14.890 -19.582 1.00 18.76 ?  3   VAL   B O    1 
ATOM   3973 C  CB   . VAL   B 1 3   ? 47.660 -12.619 -17.795 1.00 21.38 ?  3   VAL   B CB   1 
ATOM   3974 C  CG1  . VAL   B 1 3   ? 48.941 -11.778 -17.666 1.00 21.74 ?  3   VAL   B CG1  1 
ATOM   3975 C  CG2  . VAL   B 1 3   ? 46.553 -11.828 -18.477 1.00 22.19 ?  3   VAL   B CG2  1 
ATOM   3976 H  H    A VAL   B 1 3   ? 47.714 -13.439 -20.455 0.64 25.59 ?  3   VAL   B H    1 
ATOM   3977 H  H    B VAL   B 1 3   ? 47.713 -13.455 -20.461 0.36 25.59 ?  3   VAL   B H    1 
ATOM   3978 H  HA   . VAL   B 1 3   ? 48.643 -14.405 -18.096 1.00 23.83 ?  3   VAL   B HA   1 
ATOM   3979 H  HB   . VAL   B 1 3   ? 47.361 -12.840 -16.901 1.00 25.66 ?  3   VAL   B HB   1 
ATOM   3980 H  HG11 . VAL   B 1 3   ? 48.734 -10.967 -17.176 1.00 26.09 ?  3   VAL   B HG11 1 
ATOM   3981 H  HG12 . VAL   B 1 3   ? 49.607 -12.295 -17.186 1.00 26.09 ?  3   VAL   B HG12 1 
ATOM   3982 H  HG13 . VAL   B 1 3   ? 49.264 -11.558 -18.552 1.00 26.09 ?  3   VAL   B HG13 1 
ATOM   3983 H  HG21 . VAL   B 1 3   ? 46.482 -10.959 -18.055 1.00 26.63 ?  3   VAL   B HG21 1 
ATOM   3984 H  HG22 . VAL   B 1 3   ? 46.770 -11.724 -19.416 1.00 26.63 ?  3   VAL   B HG22 1 
ATOM   3985 H  HG23 . VAL   B 1 3   ? 45.716 -12.311 -18.383 1.00 26.63 ?  3   VAL   B HG23 1 
ATOM   3986 N  N    . ASN   B 1 4   ? 46.492 -15.533 -17.488 1.00 16.12 ?  4   ASN   B N    1 
ATOM   3987 C  CA   . ASN   B 1 4   ? 45.350 -16.437 -17.370 1.00 15.38 ?  4   ASN   B CA   1 
ATOM   3988 C  C    . ASN   B 1 4   ? 45.286 -17.401 -18.552 1.00 15.96 ?  4   ASN   B C    1 
ATOM   3989 O  O    . ASN   B 1 4   ? 44.224 -17.653 -19.115 1.00 16.43 ?  4   ASN   B O    1 
ATOM   3990 C  CB   . ASN   B 1 4   ? 44.040 -15.660 -17.216 1.00 15.02 ?  4   ASN   B CB   1 
ATOM   3991 C  CG   . ASN   B 1 4   ? 44.000 -14.848 -15.936 1.00 14.39 ?  4   ASN   B CG   1 
ATOM   3992 O  OD1  . ASN   B 1 4   ? 44.280 -15.364 -14.852 1.00 14.22 ?  4   ASN   B OD1  1 
ATOM   3993 N  ND2  . ASN   B 1 4   ? 43.662 -13.567 -16.055 1.00 15.17 ?  4   ASN   B ND2  1 
ATOM   3994 H  H    . ASN   B 1 4   ? 46.997 -15.517 -16.792 1.00 19.34 ?  4   ASN   B H    1 
ATOM   3995 H  HA   . ASN   B 1 4   ? 45.467 -16.970 -16.569 1.00 18.46 ?  4   ASN   B HA   1 
ATOM   3996 H  HB2  . ASN   B 1 4   ? 43.944 -15.049 -17.964 1.00 18.02 ?  4   ASN   B HB2  1 
ATOM   3997 H  HB3  . ASN   B 1 4   ? 43.300 -16.285 -17.199 1.00 18.02 ?  4   ASN   B HB3  1 
ATOM   3998 H  HD21 . ASN   B 1 4   ? 43.632 -13.061 -15.356 1.00 18.21 ?  4   ASN   B HD21 1 
ATOM   3999 H  HD22 . ASN   B 1 4   ? 43.480 -13.234 -16.828 1.00 18.21 ?  4   ASN   B HD22 1 
ATOM   4000 N  N    . SER   B 1 5   ? 46.441 -17.944 -18.932 1.00 16.66 ?  5   SER   B N    1 
ATOM   4001 C  CA   . SER   B 1 5   ? 46.531 -18.866 -20.065 1.00 19.06 ?  5   SER   B CA   1 
ATOM   4002 C  C    . SER   B 1 5   ? 46.515 -20.296 -19.535 1.00 20.73 ?  5   SER   B C    1 
ATOM   4003 O  O    . SER   B 1 5   ? 47.530 -20.983 -19.466 1.00 23.18 ?  5   SER   B O    1 
ATOM   4004 C  CB   . SER   B 1 5   ? 47.789 -18.580 -20.887 1.00 20.74 ?  5   SER   B CB   1 
ATOM   4005 O  OG   . SER   B 1 5   ? 48.959 -18.722 -20.099 1.00 23.89 ?  5   SER   B OG   1 
ATOM   4006 H  H    . SER   B 1 5   ? 47.195 -17.803 -18.544 1.00 19.99 ?  5   SER   B H    1 
ATOM   4007 H  HA   . SER   B 1 5   ? 45.764 -18.745 -20.645 1.00 22.88 ?  5   SER   B HA   1 
ATOM   4008 H  HB2  . SER   B 1 5   ? 47.831 -19.203 -21.634 1.00 24.88 ?  5   SER   B HB2  1 
ATOM   4009 H  HB3  . SER   B 1 5   ? 47.741 -17.671 -21.225 1.00 24.88 ?  5   SER   B HB3  1 
ATOM   4010 H  HG   . SER   B 1 5   ? 49.021 -19.511 -19.820 1.00 28.67 ?  5   SER   B HG   1 
ATOM   4011 N  N    . PHE   B 1 6   ? 45.321 -20.723 -19.131 1.00 21.50 ?  6   PHE   B N    1 
ATOM   4012 C  CA   . PHE   B 1 6   ? 45.128 -22.063 -18.596 1.00 21.18 ?  6   PHE   B CA   1 
ATOM   4013 C  C    . PHE   B 1 6   ? 45.043 -23.051 -19.749 1.00 24.83 ?  6   PHE   B C    1 
ATOM   4014 O  O    . PHE   B 1 6   ? 44.346 -22.801 -20.736 1.00 26.68 ?  6   PHE   B O    1 
ATOM   4015 C  CB   . PHE   B 1 6   ? 43.844 -22.114 -17.769 1.00 19.45 ?  6   PHE   B CB   1 
ATOM   4016 C  CG   . PHE   B 1 6   ? 43.875 -21.251 -16.539 1.00 17.49 ?  6   PHE   B CG   1 
ATOM   4017 C  CD1  . PHE   B 1 6   ? 44.384 -21.740 -15.351 1.00 16.44 ?  6   PHE   B CD1  1 
ATOM   4018 C  CD2  . PHE   B 1 6   ? 43.398 -19.947 -16.573 1.00 16.63 ?  6   PHE   B CD2  1 
ATOM   4019 C  CE1  . PHE   B 1 6   ? 44.405 -20.950 -14.211 1.00 15.76 ?  6   PHE   B CE1  1 
ATOM   4020 C  CE2  . PHE   B 1 6   ? 43.428 -19.148 -15.445 1.00 17.06 ?  6   PHE   B CE2  1 
ATOM   4021 C  CZ   . PHE   B 1 6   ? 43.934 -19.642 -14.265 1.00 16.28 ?  6   PHE   B CZ   1 
ATOM   4022 H  H    . PHE   B 1 6   ? 44.599 -20.257 -19.166 1.00 25.80 ?  6   PHE   B H    1 
ATOM   4023 H  HA   . PHE   B 1 6   ? 45.876 -22.307 -18.032 1.00 25.42 ?  6   PHE   B HA   1 
ATOM   4024 H  HB2  . PHE   B 1 6   ? 43.103 -21.817 -18.321 1.00 23.33 ?  6   PHE   B HB2  1 
ATOM   4025 H  HB3  . PHE   B 1 6   ? 43.691 -23.029 -17.483 1.00 23.33 ?  6   PHE   B HB3  1 
ATOM   4026 H  HD1  . PHE   B 1 6   ? 44.711 -22.609 -15.313 1.00 19.73 ?  6   PHE   B HD1  1 
ATOM   4027 H  HD2  . PHE   B 1 6   ? 43.051 -19.610 -17.365 1.00 19.96 ?  6   PHE   B HD2  1 
ATOM   4028 H  HE1  . PHE   B 1 6   ? 44.761 -21.281 -13.417 1.00 18.92 ?  6   PHE   B HE1  1 
ATOM   4029 H  HE2  . PHE   B 1 6   ? 43.096 -18.280 -15.483 1.00 20.47 ?  6   PHE   B HE2  1 
ATOM   4030 H  HZ   . PHE   B 1 6   ? 43.950 -19.110 -13.502 1.00 19.53 ?  6   PHE   B HZ   1 
ATOM   4031 N  N    . SER   B 1 7   ? 45.770 -24.162 -19.633 1.00 25.86 ?  7   SER   B N    1 
ATOM   4032 C  CA   . SER   B 1 7   ? 45.833 -25.157 -20.693 1.00 29.18 ?  7   SER   B CA   1 
ATOM   4033 C  C    . SER   B 1 7   ? 45.776 -26.557 -20.099 1.00 28.02 ?  7   SER   B C    1 
ATOM   4034 O  O    . SER   B 1 7   ? 46.370 -26.825 -19.052 1.00 28.93 ?  7   SER   B O    1 
ATOM   4035 C  CB   . SER   B 1 7   ? 47.120 -24.997 -21.517 1.00 32.66 ?  7   SER   B CB   1 
ATOM   4036 O  OG   . SER   B 1 7   ? 47.094 -25.821 -22.670 1.00 34.76 ?  7   SER   B OG   1 
ATOM   4037 H  H    . SER   B 1 7   ? 46.249 -24.356 -18.943 1.00 31.03 ?  7   SER   B H    1 
ATOM   4038 H  HA   . SER   B 1 7   ? 45.078 -25.048 -21.286 1.00 35.02 ?  7   SER   B HA   1 
ATOM   4039 H  HB2  . SER   B 1 7   ? 47.204 -24.071 -21.797 1.00 39.19 ?  7   SER   B HB2  1 
ATOM   4040 H  HB3  . SER   B 1 7   ? 47.882 -25.245 -20.969 1.00 39.19 ?  7   SER   B HB3  1 
ATOM   4041 H  HG   . SER   B 1 7   ? 47.804 -25.723 -23.109 1.00 41.71 ?  7   SER   B HG   1 
ATOM   4042 N  N    . GLY   B 1 8   ? 45.057 -27.447 -20.781 1.00 27.44 ?  8   GLY   B N    1 
ATOM   4043 C  CA   . GLY   B 1 8   ? 45.024 -28.840 -20.393 1.00 26.73 ?  8   GLY   B CA   1 
ATOM   4044 C  C    . GLY   B 1 8   ? 44.078 -29.173 -19.270 1.00 25.12 ?  8   GLY   B C    1 
ATOM   4045 O  O    . GLY   B 1 8   ? 44.216 -30.241 -18.659 1.00 26.52 ?  8   GLY   B O    1 
ATOM   4046 H  H    . GLY   B 1 8   ? 44.585 -27.258 -21.471 1.00 32.92 ?  8   GLY   B H    1 
ATOM   4047 H  HA2  . GLY   B 1 8   ? 44.761 -29.370 -21.157 1.00 32.08 ?  8   GLY   B HA2  1 
ATOM   4048 H  HA3  . GLY   B 1 8   ? 45.912 -29.113 -20.122 1.00 32.08 ?  8   GLY   B HA3  1 
ATOM   4049 N  N    . TYR   B 1 9   ? 43.098 -28.318 -18.991 1.00 23.22 ?  9   TYR   B N    1 
ATOM   4050 C  CA   . TYR   B 1 9   ? 42.150 -28.589 -17.923 1.00 21.19 ?  9   TYR   B CA   1 
ATOM   4051 C  C    . TYR   B 1 9   ? 40.966 -29.388 -18.435 1.00 20.47 ?  9   TYR   B C    1 
ATOM   4052 O  O    . TYR   B 1 9   ? 40.546 -29.259 -19.589 1.00 22.28 ?  9   TYR   B O    1 
ATOM   4053 C  CB   . TYR   B 1 9   ? 41.641 -27.302 -17.281 1.00 20.30 ?  9   TYR   B CB   1 
ATOM   4054 C  CG   . TYR   B 1 9   ? 42.666 -26.671 -16.371 1.00 19.60 ?  9   TYR   B CG   1 
ATOM   4055 C  CD1  . TYR   B 1 9   ? 43.761 -25.998 -16.892 1.00 19.88 ?  9   TYR   B CD1  1 
ATOM   4056 C  CD2  . TYR   B 1 9   ? 42.552 -26.766 -14.993 1.00 19.00 ?  9   TYR   B CD2  1 
ATOM   4057 C  CE1  . TYR   B 1 9   ? 44.712 -25.431 -16.069 1.00 19.76 ?  9   TYR   B CE1  1 
ATOM   4058 C  CE2  . TYR   B 1 9   ? 43.501 -26.198 -14.157 1.00 19.05 ?  9   TYR   B CE2  1 
ATOM   4059 C  CZ   . TYR   B 1 9   ? 44.580 -25.527 -14.703 1.00 19.48 ?  9   TYR   B CZ   1 
ATOM   4060 O  OH   . TYR   B 1 9   ? 45.532 -24.970 -13.887 1.00 20.27 ?  9   TYR   B OH   1 
ATOM   4061 H  H    . TYR   B 1 9   ? 42.943 -27.586 -19.419 1.00 27.86 ?  9   TYR   B H    1 
ATOM   4062 H  HA   . TYR   B 1 9   ? 42.581 -29.111 -17.234 1.00 25.43 ?  9   TYR   B HA   1 
ATOM   4063 H  HB2  . TYR   B 1 9   ? 41.412 -26.658 -17.972 1.00 24.36 ?  9   TYR   B HB2  1 
ATOM   4064 H  HB3  . TYR   B 1 9   ? 40.861 -27.511 -16.748 1.00 24.36 ?  9   TYR   B HB3  1 
ATOM   4065 H  HD1  . TYR   B 1 9   ? 43.853 -25.932 -17.816 1.00 23.85 ?  9   TYR   B HD1  1 
ATOM   4066 H  HD2  . TYR   B 1 9   ? 41.820 -27.219 -14.624 1.00 22.80 ?  9   TYR   B HD2  1 
ATOM   4067 H  HE1  . TYR   B 1 9   ? 45.432 -24.987 -16.437 1.00 23.71 ?  9   TYR   B HE1  1 
ATOM   4068 H  HE2  . TYR   B 1 9   ? 43.399 -26.273 -13.235 1.00 22.86 ?  9   TYR   B HE2  1 
ATOM   4069 H  HH   . TYR   B 1 9   ? 46.114 -24.603 -14.355 1.00 24.32 ?  9   TYR   B HH   1 
ATOM   4070 N  N    . LEU   B 1 10  ? 40.440 -30.229 -17.554 1.00 18.72 ?  10  LEU   B N    1 
ATOM   4071 C  CA   . LEU   B 1 10  ? 39.234 -30.991 -17.816 1.00 18.73 ?  10  LEU   B CA   1 
ATOM   4072 C  C    . LEU   B 1 10  ? 38.050 -30.220 -17.250 1.00 18.16 ?  10  LEU   B C    1 
ATOM   4073 O  O    . LEU   B 1 10  ? 38.074 -29.799 -16.090 1.00 17.88 ?  10  LEU   B O    1 
ATOM   4074 C  CB   . LEU   B 1 10  ? 39.347 -32.356 -17.138 1.00 19.68 ?  10  LEU   B CB   1 
ATOM   4075 C  CG   . LEU   B 1 10  ? 38.206 -33.322 -17.441 1.00 21.23 ?  10  LEU   B CG   1 
ATOM   4076 C  CD1  . LEU   B 1 10  ? 38.295 -33.807 -18.882 1.00 22.56 ?  10  LEU   B CD1  1 
ATOM   4077 C  CD2  . LEU   B 1 10  ? 38.203 -34.495 -16.471 1.00 22.28 ?  10  LEU   B CD2  1 
ATOM   4078 H  H    . LEU   B 1 10  ? 40.765 -30.375 -16.768 1.00 22.46 ?  10  LEU   B H    1 
ATOM   4079 H  HA   . LEU   B 1 10  ? 39.108 -31.119 -18.768 1.00 22.48 ?  10  LEU   B HA   1 
ATOM   4080 H  HB2  . LEU   B 1 10  ? 40.172 -32.779 -17.426 1.00 23.62 ?  10  LEU   B HB2  1 
ATOM   4081 H  HB3  . LEU   B 1 10  ? 39.370 -32.227 -16.174 1.00 23.62 ?  10  LEU   B HB3  1 
ATOM   4082 H  HG   . LEU   B 1 10  ? 37.363 -32.857 -17.338 1.00 25.47 ?  10  LEU   B HG   1 
ATOM   4083 H  HD11 . LEU   B 1 10  ? 37.616 -34.480 -19.030 1.00 27.08 ?  10  LEU   B HD11 1 
ATOM   4084 H  HD12 . LEU   B 1 10  ? 38.150 -33.051 -19.474 1.00 27.08 ?  10  LEU   B HD12 1 
ATOM   4085 H  HD13 . LEU   B 1 10  ? 39.176 -34.182 -19.032 1.00 27.08 ?  10  LEU   B HD13 1 
ATOM   4086 H  HD21 . LEU   B 1 10  ? 37.466 -35.085 -16.696 1.00 26.74 ?  10  LEU   B HD21 1 
ATOM   4087 H  HD22 . LEU   B 1 10  ? 39.043 -34.968 -16.547 1.00 26.74 ?  10  LEU   B HD22 1 
ATOM   4088 H  HD23 . LEU   B 1 10  ? 38.090 -34.154 -15.570 1.00 26.74 ?  10  LEU   B HD23 1 
ATOM   4089 N  N    . LYS   B 1 11  ? 37.021 -30.039 -18.071 1.00 19.43 ?  11  LYS   B N    1 
ATOM   4090 C  CA   . LYS   B 1 11  ? 35.828 -29.317 -17.655 1.00 21.38 ?  11  LYS   B CA   1 
ATOM   4091 C  C    . LYS   B 1 11  ? 34.949 -30.238 -16.814 1.00 20.30 ?  11  LYS   B C    1 
ATOM   4092 O  O    . LYS   B 1 11  ? 34.572 -31.327 -17.265 1.00 22.22 ?  11  LYS   B O    1 
ATOM   4093 C  CB   . LYS   B 1 11  ? 35.079 -28.844 -18.901 1.00 25.64 ?  11  LYS   B CB   1 
ATOM   4094 C  CG   . LYS   B 1 11  ? 33.919 -27.899 -18.648 1.00 29.32 ?  11  LYS   B CG   1 
ATOM   4095 C  CD   . LYS   B 1 11  ? 33.190 -27.596 -19.952 1.00 32.33 ?  11  LYS   B CD   1 
ATOM   4096 C  CE   . LYS   B 1 11  ? 32.147 -26.507 -19.779 1.00 34.60 ?  11  LYS   B CE   1 
ATOM   4097 N  NZ   . LYS   B 1 11  ? 32.770 -25.169 -19.592 1.00 35.83 ?  11  LYS   B NZ   1 
ATOM   4098 H  H    . LYS   B 1 11  ? 36.986 -30.327 -18.882 1.00 23.32 ?  11  LYS   B H    1 
ATOM   4099 H  HA   . LYS   B 1 11  ? 36.077 -28.543 -17.126 1.00 25.65 ?  11  LYS   B HA   1 
ATOM   4100 H  HB2  . LYS   B 1 11  ? 35.706 -28.380 -19.479 1.00 30.77 ?  11  LYS   B HB2  1 
ATOM   4101 H  HB3  . LYS   B 1 11  ? 34.726 -29.619 -19.362 1.00 30.77 ?  11  LYS   B HB3  1 
ATOM   4102 H  HG2  . LYS   B 1 11  ? 33.292 -28.313 -18.035 1.00 35.18 ?  11  LYS   B HG2  1 
ATOM   4103 H  HG3  . LYS   B 1 11  ? 34.253 -27.065 -18.283 1.00 35.18 ?  11  LYS   B HG3  1 
ATOM   4104 H  HD2  . LYS   B 1 11  ? 33.834 -27.297 -20.615 1.00 38.79 ?  11  LYS   B HD2  1 
ATOM   4105 H  HD3  . LYS   B 1 11  ? 32.743 -28.400 -20.261 1.00 38.79 ?  11  LYS   B HD3  1 
ATOM   4106 H  HE2  . LYS   B 1 11  ? 31.586 -26.473 -20.570 1.00 41.52 ?  11  LYS   B HE2  1 
ATOM   4107 H  HE3  . LYS   B 1 11  ? 31.609 -26.707 -18.997 1.00 41.52 ?  11  LYS   B HE3  1 
ATOM   4108 H  HZ1  . LYS   B 1 11  ? 32.138 -24.548 -19.510 1.00 43.00 ?  11  LYS   B HZ1  1 
ATOM   4109 H  HZ2  . LYS   B 1 11  ? 33.275 -25.168 -18.860 1.00 43.00 ?  11  LYS   B HZ2  1 
ATOM   4110 H  HZ3  . LYS   B 1 11  ? 33.280 -24.971 -20.295 1.00 43.00 ?  11  LYS   B HZ3  1 
ATOM   4111 N  N    . LEU   B 1 12  ? 34.624 -29.808 -15.594 1.00 18.73 ?  12  LEU   B N    1 
ATOM   4112 C  CA   . LEU   B 1 12  ? 33.668 -30.515 -14.749 1.00 17.89 ?  12  LEU   B CA   1 
ATOM   4113 C  C    . LEU   B 1 12  ? 32.275 -29.911 -14.840 1.00 17.80 ?  12  LEU   B C    1 
ATOM   4114 O  O    . LEU   B 1 12  ? 31.291 -30.631 -15.020 1.00 18.12 ?  12  LEU   B O    1 
ATOM   4115 C  CB   . LEU   B 1 12  ? 34.129 -30.536 -13.285 1.00 17.24 ?  12  LEU   B CB   1 
ATOM   4116 C  CG   . LEU   B 1 12  ? 35.471 -31.215 -13.009 1.00 17.24 ?  12  LEU   B CG   1 
ATOM   4117 C  CD1  . LEU   B 1 12  ? 35.835 -31.161 -11.531 1.00 17.58 ?  12  LEU   B CD1  1 
ATOM   4118 C  CD2  . LEU   B 1 12  ? 35.470 -32.649 -13.511 1.00 18.04 ?  12  LEU   B CD2  1 
ATOM   4119 H  H    . LEU   B 1 12  ? 34.936 -29.089 -15.231 1.00 22.48 ?  12  LEU   B H    1 
ATOM   4120 H  HA   . LEU   B 1 12  ? 33.597 -31.431 -15.055 1.00 21.46 ?  12  LEU   B HA   1 
ATOM   4121 H  HB2  . LEU   B 1 12  ? 34.192 -29.622 -12.974 1.00 20.69 ?  12  LEU   B HB2  1 
ATOM   4122 H  HB3  . LEU   B 1 12  ? 33.454 -31.006 -12.763 1.00 20.69 ?  12  LEU   B HB3  1 
ATOM   4123 H  HG   . LEU   B 1 12  ? 36.158 -30.735 -13.493 1.00 20.69 ?  12  LEU   B HG   1 
ATOM   4124 H  HD11 . LEU   B 1 12  ? 36.696 -31.597 -11.403 1.00 21.10 ?  12  LEU   B HD11 1 
ATOM   4125 H  HD12 . LEU   B 1 12  ? 35.892 -30.235 -11.249 1.00 21.10 ?  12  LEU   B HD12 1 
ATOM   4126 H  HD13 . LEU   B 1 12  ? 35.155 -31.623 -11.017 1.00 21.10 ?  12  LEU   B HD13 1 
ATOM   4127 H  HD21 . LEU   B 1 12  ? 36.273 -33.092 -13.201 1.00 21.64 ?  12  LEU   B HD21 1 
ATOM   4128 H  HD22 . LEU   B 1 12  ? 34.685 -33.103 -13.165 1.00 21.64 ?  12  LEU   B HD22 1 
ATOM   4129 H  HD23 . LEU   B 1 12  ? 35.446 -32.643 -14.481 1.00 21.64 ?  12  LEU   B HD23 1 
ATOM   4130 N  N    . THR   B 1 13  ? 32.184 -28.592 -14.716 1.00 17.64 ?  13  THR   B N    1 
ATOM   4131 C  CA   . THR   B 1 13  ? 30.960 -27.840 -14.919 1.00 17.73 ?  13  THR   B CA   1 
ATOM   4132 C  C    . THR   B 1 13  ? 31.293 -26.652 -15.815 1.00 19.94 ?  13  THR   B C    1 
ATOM   4133 O  O    . THR   B 1 13  ? 32.437 -26.470 -16.247 1.00 20.87 ?  13  THR   B O    1 
ATOM   4134 C  CB   . THR   B 1 13  ? 30.361 -27.358 -13.590 1.00 17.25 ?  13  THR   B CB   1 
ATOM   4135 O  OG1  . THR   B 1 13  ? 31.198 -26.328 -13.049 1.00 16.87 ?  13  THR   B OG1  1 
ATOM   4136 C  CG2  . THR   B 1 13  ? 30.252 -28.509 -12.589 1.00 17.52 ?  13  THR   B CG2  1 
ATOM   4137 H  H    . THR   B 1 13  ? 32.848 -28.089 -14.499 1.00 21.17 ?  13  THR   B H    1 
ATOM   4138 H  HA   . THR   B 1 13  ? 30.301 -28.400 -15.361 1.00 21.27 ?  13  THR   B HA   1 
ATOM   4139 H  HB   . THR   B 1 13  ? 29.468 -27.000 -13.745 1.00 20.70 ?  13  THR   B HB   1 
ATOM   4140 H  HG1  . THR   B 1 13  ? 30.879 -25.564 -13.237 1.00 20.24 ?  13  THR   B HG1  1 
ATOM   4141 H  HG21 . THR   B 1 13  ? 29.764 -28.221 -11.800 1.00 21.02 ?  13  THR   B HG21 1 
ATOM   4142 H  HG22 . THR   B 1 13  ? 29.784 -29.256 -12.992 1.00 21.02 ?  13  THR   B HG22 1 
ATOM   4143 H  HG23 . THR   B 1 13  ? 31.138 -28.800 -12.320 1.00 21.02 ?  13  THR   B HG23 1 
ATOM   4144 N  N    A ASP   B 1 14  ? 30.284 -25.826 -16.085 0.64 20.63 ?  14  ASP   B N    1 
ATOM   4145 N  N    B ASP   B 1 14  ? 30.287 -25.815 -16.079 0.36 20.55 ?  14  ASP   B N    1 
ATOM   4146 C  CA   A ASP   B 1 14  ? 30.505 -24.672 -16.947 0.64 22.35 ?  14  ASP   B CA   1 
ATOM   4147 C  CA   B ASP   B 1 14  ? 30.494 -24.662 -16.949 0.36 21.58 ?  14  ASP   B CA   1 
ATOM   4148 C  C    A ASP   B 1 14  ? 31.611 -23.769 -16.413 0.64 20.72 ?  14  ASP   B C    1 
ATOM   4149 C  C    B ASP   B 1 14  ? 31.500 -23.667 -16.387 0.36 19.94 ?  14  ASP   B C    1 
ATOM   4150 O  O    A ASP   B 1 14  ? 32.293 -23.098 -17.199 0.64 21.98 ?  14  ASP   B O    1 
ATOM   4151 O  O    B ASP   B 1 14  ? 31.967 -22.796 -17.130 0.36 20.31 ?  14  ASP   B O    1 
ATOM   4152 C  CB   A ASP   B 1 14  ? 29.205 -23.888 -17.120 0.64 25.85 ?  14  ASP   B CB   1 
ATOM   4153 C  CB   B ASP   B 1 14  ? 29.172 -23.936 -17.198 0.36 24.22 ?  14  ASP   B CB   1 
ATOM   4154 C  CG   A ASP   B 1 14  ? 28.228 -24.568 -18.057 0.64 29.40 ?  14  ASP   B CG   1 
ATOM   4155 C  CG   B ASP   B 1 14  ? 28.295 -24.655 -18.205 0.36 26.64 ?  14  ASP   B CG   1 
ATOM   4156 O  OD1  A ASP   B 1 14  ? 28.598 -25.580 -18.696 0.64 30.44 ?  14  ASP   B OD1  1 
ATOM   4157 O  OD1  B ASP   B 1 14  ? 28.847 -25.275 -19.140 0.36 27.38 ?  14  ASP   B OD1  1 
ATOM   4158 O  OD2  A ASP   B 1 14  ? 27.078 -24.093 -18.147 0.64 30.99 -1 14  ASP   B OD2  1 
ATOM   4159 O  OD2  B ASP   B 1 14  ? 27.055 -24.608 -18.062 0.36 27.53 -1 14  ASP   B OD2  1 
ATOM   4160 H  H    A ASP   B 1 14  ? 29.484 -25.903 -15.780 0.64 24.76 ?  14  ASP   B H    1 
ATOM   4161 H  H    B ASP   B 1 14  ? 29.489 -25.891 -15.771 0.36 24.67 ?  14  ASP   B H    1 
ATOM   4162 H  HA   A ASP   B 1 14  ? 30.786 -24.981 -17.818 0.64 26.82 ?  14  ASP   B HA   1 
ATOM   4163 H  HA   B ASP   B 1 14  ? 30.825 -24.976 -17.805 0.36 25.89 ?  14  ASP   B HA   1 
ATOM   4164 H  HB2  A ASP   B 1 14  ? 28.762 -23.809 -16.263 0.64 31.02 ?  14  ASP   B HB2  1 
ATOM   4165 H  HB2  B ASP   B 1 14  ? 28.687 -23.873 -16.360 0.36 29.07 ?  14  ASP   B HB2  1 
ATOM   4166 H  HB3  A ASP   B 1 14  ? 29.409 -23.008 -17.474 0.64 31.02 ?  14  ASP   B HB3  1 
ATOM   4167 H  HB3  B ASP   B 1 14  ? 29.367 -23.042 -17.532 0.36 29.07 ?  14  ASP   B HB3  1 
ATOM   4168 N  N    . ASN   B 1 15  ? 31.818 -23.745 -15.092 1.00 18.21 ?  15  ASN   B N    1 
ATOM   4169 C  CA   . ASN   B 1 15  ? 32.784 -22.828 -14.487 1.00 15.95 ?  15  ASN   B CA   1 
ATOM   4170 C  C    . ASN   B 1 15  ? 33.876 -23.482 -13.650 1.00 14.53 ?  15  ASN   B C    1 
ATOM   4171 O  O    . ASN   B 1 15  ? 34.729 -22.757 -13.129 1.00 14.59 ?  15  ASN   B O    1 
ATOM   4172 C  CB   . ASN   B 1 15  ? 32.071 -21.769 -13.631 1.00 15.50 ?  15  ASN   B CB   1 
ATOM   4173 C  CG   . ASN   B 1 15  ? 31.441 -22.358 -12.386 1.00 15.29 ?  15  ASN   B CG   1 
ATOM   4174 O  OD1  . ASN   B 1 15  ? 30.490 -23.141 -12.474 1.00 16.93 ?  15  ASN   B OD1  1 
ATOM   4175 N  ND2  . ASN   B 1 15  ? 31.967 -22.009 -11.225 1.00 14.27 ?  15  ASN   B ND2  1 
ATOM   4176 H  H    A ASN   B 1 15  ? 31.410 -24.253 -14.526 0.64 21.85 ?  15  ASN   B H    1 
ATOM   4177 H  H    B ASN   B 1 15  ? 31.461 -24.300 -14.536 0.36 21.85 ?  15  ASN   B H    1 
ATOM   4178 H  HA   . ASN   B 1 15  ? 33.234 -22.352 -15.194 1.00 19.14 ?  15  ASN   B HA   1 
ATOM   4179 H  HB2  . ASN   B 1 15  ? 32.720 -21.094 -13.356 1.00 18.60 ?  15  ASN   B HB2  1 
ATOM   4180 H  HB3  . ASN   B 1 15  ? 31.370 -21.348 -14.155 1.00 18.60 ?  15  ASN   B HB3  1 
ATOM   4181 H  HD21 . ASN   B 1 15  ? 31.639 -22.313 -10.490 1.00 17.13 ?  15  ASN   B HD21 1 
ATOM   4182 H  HD22 . ASN   B 1 15  ? 32.639 -21.462 -11.195 1.00 17.13 ?  15  ASN   B HD22 1 
ATOM   4183 N  N    . VAL   B 1 16  ? 33.881 -24.803 -13.490 1.00 14.02 ?  16  VAL   B N    1 
ATOM   4184 C  CA   . VAL   B 1 16  ? 34.885 -25.492 -12.686 1.00 13.88 ?  16  VAL   B CA   1 
ATOM   4185 C  C    . VAL   B 1 16  ? 35.674 -26.432 -13.583 1.00 14.12 ?  16  VAL   B C    1 
ATOM   4186 O  O    . VAL   B 1 16  ? 35.094 -27.307 -14.242 1.00 15.03 ?  16  VAL   B O    1 
ATOM   4187 C  CB   . VAL   B 1 16  ? 34.263 -26.256 -11.506 1.00 14.27 ?  16  VAL   B CB   1 
ATOM   4188 C  CG1  . VAL   B 1 16  ? 35.353 -26.986 -10.715 1.00 14.00 ?  16  VAL   B CG1  1 
ATOM   4189 C  CG2  . VAL   B 1 16  ? 33.458 -25.311 -10.615 1.00 14.77 ?  16  VAL   B CG2  1 
ATOM   4190 H  H    . VAL   B 1 16  ? 33.292 -25.333 -13.839 1.00 16.83 ?  16  VAL   B H    1 
ATOM   4191 H  HA   . VAL   B 1 16  ? 35.498 -24.835 -12.321 1.00 16.66 ?  16  VAL   B HA   1 
ATOM   4192 H  HB   . VAL   B 1 16  ? 33.656 -26.928 -11.853 1.00 17.12 ?  16  VAL   B HB   1 
ATOM   4193 H  HG11 . VAL   B 1 16  ? 34.982 -27.288 -9.870  1.00 16.80 ?  16  VAL   B HG11 1 
ATOM   4194 H  HG12 . VAL   B 1 16  ? 35.669 -27.745 -11.226 1.00 16.80 ?  16  VAL   B HG12 1 
ATOM   4195 H  HG13 . VAL   B 1 16  ? 36.087 -26.370 -10.546 1.00 16.80 ?  16  VAL   B HG13 1 
ATOM   4196 H  HG21 . VAL   B 1 16  ? 33.127 -25.805 -9.847  1.00 17.73 ?  16  VAL   B HG21 1 
ATOM   4197 H  HG22 . VAL   B 1 16  ? 34.028 -24.587 -10.323 1.00 17.73 ?  16  VAL   B HG22 1 
ATOM   4198 H  HG23 . VAL   B 1 16  ? 32.709 -24.959 -11.125 1.00 17.73 ?  16  VAL   B HG23 1 
ATOM   4199 N  N    . TYR   B 1 17  ? 36.997 -26.265 -13.563 1.00 14.34 ?  17  TYR   B N    1 
ATOM   4200 C  CA   . TYR   B 1 17  ? 37.945 -27.009 -14.377 1.00 14.83 ?  17  TYR   B CA   1 
ATOM   4201 C  C    . TYR   B 1 17  ? 38.999 -27.618 -13.462 1.00 13.83 ?  17  TYR   B C    1 
ATOM   4202 O  O    . TYR   B 1 17  ? 39.280 -27.088 -12.383 1.00 14.35 ?  17  TYR   B O    1 
ATOM   4203 C  CB   . TYR   B 1 17  ? 38.647 -26.077 -15.375 1.00 17.75 ?  17  TYR   B CB   1 
ATOM   4204 C  CG   . TYR   B 1 17  ? 37.717 -25.311 -16.286 1.00 21.45 ?  17  TYR   B CG   1 
ATOM   4205 C  CD1  . TYR   B 1 17  ? 37.139 -24.115 -15.879 1.00 22.99 ?  17  TYR   B CD1  1 
ATOM   4206 C  CD2  . TYR   B 1 17  ? 37.424 -25.780 -17.559 1.00 23.58 ?  17  TYR   B CD2  1 
ATOM   4207 C  CE1  . TYR   B 1 17  ? 36.287 -23.409 -16.714 1.00 24.64 ?  17  TYR   B CE1  1 
ATOM   4208 C  CE2  . TYR   B 1 17  ? 36.577 -25.084 -18.401 1.00 25.27 ?  17  TYR   B CE2  1 
ATOM   4209 C  CZ   . TYR   B 1 17  ? 36.012 -23.900 -17.973 1.00 25.97 ?  17  TYR   B CZ   1 
ATOM   4210 O  OH   . TYR   B 1 17  ? 35.171 -23.203 -18.808 1.00 27.50 ?  17  TYR   B OH   1 
ATOM   4211 H  H    . TYR   B 1 17  ? 37.390 -25.686 -13.058 1.00 17.21 ?  17  TYR   B H    1 
ATOM   4212 H  HA   . TYR   B 1 17  ? 37.484 -27.715 -14.866 1.00 17.80 ?  17  TYR   B HA   1 
ATOM   4213 H  HB2  . TYR   B 1 17  ? 39.178 -25.434 -14.883 1.00 21.30 ?  17  TYR   B HB2  1 
ATOM   4214 H  HB3  . TYR   B 1 17  ? 39.219 -26.611 -15.942 1.00 21.30 ?  17  TYR   B HB3  1 
ATOM   4215 H  HD1  . TYR   B 1 17  ? 37.323 -23.782 -15.031 1.00 27.59 ?  17  TYR   B HD1  1 
ATOM   4216 H  HD2  . TYR   B 1 17  ? 37.800 -26.577 -17.851 1.00 28.29 ?  17  TYR   B HD2  1 
ATOM   4217 H  HE1  . TYR   B 1 17  ? 35.904 -22.609 -16.430 1.00 29.56 ?  17  TYR   B HE1  1 
ATOM   4218 H  HE2  . TYR   B 1 17  ? 36.386 -25.412 -19.252 1.00 30.32 ?  17  TYR   B HE2  1 
ATOM   4219 H  HH   . TYR   B 1 17  ? 35.084 -23.607 -19.539 1.00 33.00 ?  17  TYR   B HH   1 
ATOM   4220 N  N    . ILE   B 1 18  ? 39.602 -28.729 -13.892 1.00 14.07 ?  18  ILE   B N    1 
ATOM   4221 C  CA   . ILE   B 1 18  ? 40.533 -29.452 -13.031 1.00 14.06 ?  18  ILE   B CA   1 
ATOM   4222 C  C    . ILE   B 1 18  ? 41.696 -30.000 -13.851 1.00 14.66 ?  18  ILE   B C    1 
ATOM   4223 O  O    . ILE   B 1 18  ? 41.539 -30.384 -15.014 1.00 15.97 ?  18  ILE   B O    1 
ATOM   4224 C  CB   . ILE   B 1 18  ? 39.789 -30.556 -12.228 1.00 14.38 ?  18  ILE   B CB   1 
ATOM   4225 C  CG1  . ILE   B 1 18  ? 40.654 -31.090 -11.083 1.00 14.48 ?  18  ILE   B CG1  1 
ATOM   4226 C  CG2  . ILE   B 1 18  ? 39.297 -31.687 -13.147 1.00 14.93 ?  18  ILE   B CG2  1 
ATOM   4227 C  CD1  . ILE   B 1 18  ? 39.867 -31.928 -10.078 1.00 15.94 ?  18  ILE   B CD1  1 
ATOM   4228 H  H    . ILE   B 1 18  ? 39.488 -29.081 -14.667 1.00 16.88 ?  18  ILE   B H    1 
ATOM   4229 H  HA   . ILE   B 1 18  ? 40.892 -28.834 -12.380 1.00 16.88 ?  18  ILE   B HA   1 
ATOM   4230 H  HB   . ILE   B 1 18  ? 39.001 -30.157 -11.825 1.00 17.26 ?  18  ILE   B HB   1 
ATOM   4231 H  HG12 . ILE   B 1 18  ? 41.357 -31.644 -11.448 1.00 17.38 ?  18  ILE   B HG12 1 
ATOM   4232 H  HG13 . ILE   B 1 18  ? 41.035 -30.338 -10.603 1.00 17.38 ?  18  ILE   B HG13 1 
ATOM   4233 H  HG21 . ILE   B 1 18  ? 38.711 -32.277 -12.642 1.00 17.92 ?  18  ILE   B HG21 1 
ATOM   4234 H  HG22 . ILE   B 1 18  ? 38.807 -31.296 -13.888 1.00 17.92 ?  18  ILE   B HG22 1 
ATOM   4235 H  HG23 . ILE   B 1 18  ? 40.059 -32.183 -13.478 1.00 17.92 ?  18  ILE   B HG23 1 
ATOM   4236 H  HD11 . ILE   B 1 18  ? 40.457 -32.192 -9.352  1.00 19.12 ?  18  ILE   B HD11 1 
ATOM   4237 H  HD12 . ILE   B 1 18  ? 39.130 -31.404 -9.729  1.00 19.12 ?  18  ILE   B HD12 1 
ATOM   4238 H  HD13 . ILE   B 1 18  ? 39.525 -32.722 -10.524 1.00 19.12 ?  18  ILE   B HD13 1 
ATOM   4239 N  N    . LYS   B 1 19  ? 42.872 -30.046 -13.221 1.00 15.11 ?  19  LYS   B N    1 
ATOM   4240 C  CA   . LYS   B 1 19  ? 44.086 -30.511 -13.876 1.00 16.09 ?  19  LYS   B CA   1 
ATOM   4241 C  C    . LYS   B 1 19  ? 44.992 -31.188 -12.857 1.00 15.36 ?  19  LYS   B C    1 
ATOM   4242 O  O    . LYS   B 1 19  ? 45.071 -30.761 -11.704 1.00 14.99 ?  19  LYS   B O    1 
ATOM   4243 C  CB   . LYS   B 1 19  ? 44.846 -29.339 -14.510 1.00 17.33 ?  19  LYS   B CB   1 
ATOM   4244 C  CG   . LYS   B 1 19  ? 46.028 -29.739 -15.375 1.00 19.32 ?  19  LYS   B CG   1 
ATOM   4245 C  CD   . LYS   B 1 19  ? 46.761 -28.506 -15.897 1.00 20.92 ?  19  LYS   B CD   1 
ATOM   4246 C  CE   . LYS   B 1 19  ? 47.903 -28.883 -16.820 1.00 22.94 ?  19  LYS   B CE   1 
ATOM   4247 N  NZ   . LYS   B 1 19  ? 48.666 -27.690 -17.276 1.00 24.19 ?  19  LYS   B NZ   1 
ATOM   4248 H  H    . LYS   B 1 19  ? 42.980 -29.808 -12.399 1.00 18.13 ?  19  LYS   B H    1 
ATOM   4249 H  HA   . LYS   B 1 19  ? 43.851 -31.147 -14.569 1.00 19.31 ?  19  LYS   B HA   1 
ATOM   4250 H  HB2  . LYS   B 1 19  ? 44.229 -28.842 -15.068 1.00 20.80 ?  19  LYS   B HB2  1 
ATOM   4251 H  HB3  . LYS   B 1 19  ? 45.174 -28.765 -13.797 1.00 20.80 ?  19  LYS   B HB3  1 
ATOM   4252 H  HG2  . LYS   B 1 19  ? 46.643 -30.269 -14.847 1.00 23.19 ?  19  LYS   B HG2  1 
ATOM   4253 H  HG3  . LYS   B 1 19  ? 45.703 -30.253 -16.133 1.00 23.19 ?  19  LYS   B HG3  1 
ATOM   4254 H  HD2  . LYS   B 1 19  ? 46.136 -27.950 -16.391 1.00 25.10 ?  19  LYS   B HD2  1 
ATOM   4255 H  HD3  . LYS   B 1 19  ? 47.124 -28.012 -15.144 1.00 25.10 ?  19  LYS   B HD3  1 
ATOM   4256 H  HE2  . LYS   B 1 19  ? 48.511 -29.473 -16.347 1.00 27.53 ?  19  LYS   B HE2  1 
ATOM   4257 H  HE3  . LYS   B 1 19  ? 47.543 -29.333 -17.602 1.00 27.53 ?  19  LYS   B HE3  1 
ATOM   4258 H  HZ1  . LYS   B 1 19  ? 49.300 -27.936 -17.851 1.00 29.03 ?  19  LYS   B HZ1  1 
ATOM   4259 H  HZ2  . LYS   B 1 19  ? 48.119 -27.114 -17.678 1.00 29.03 ?  19  LYS   B HZ2  1 
ATOM   4260 H  HZ3  . LYS   B 1 19  ? 49.047 -27.289 -16.579 1.00 29.03 ?  19  LYS   B HZ3  1 
ATOM   4261 N  N    . ASN   B 1 20  ? 45.680 -32.240 -13.295 1.00 16.96 ?  20  ASN   B N    1 
ATOM   4262 C  CA   . ASN   B 1 20  ? 46.710 -32.876 -12.478 1.00 17.98 ?  20  ASN   B CA   1 
ATOM   4263 C  C    . ASN   B 1 20  ? 47.982 -32.058 -12.671 1.00 18.23 ?  20  ASN   B C    1 
ATOM   4264 O  O    . ASN   B 1 20  ? 48.627 -32.135 -13.720 1.00 20.08 ?  20  ASN   B O    1 
ATOM   4265 C  CB   . ASN   B 1 20  ? 46.875 -34.331 -12.912 1.00 19.63 ?  20  ASN   B CB   1 
ATOM   4266 C  CG   . ASN   B 1 20  ? 48.027 -35.051 -12.218 1.00 21.14 ?  20  ASN   B CG   1 
ATOM   4267 O  OD1  . ASN   B 1 20  ? 48.682 -35.909 -12.823 1.00 23.46 ?  20  ASN   B OD1  1 
ATOM   4268 N  ND2  . ASN   B 1 20  ? 48.263 -34.736 -10.952 1.00 20.81 ?  20  ASN   B ND2  1 
ATOM   4269 H  H    . ASN   B 1 20  ? 45.571 -32.599 -14.067 1.00 20.35 ?  20  ASN   B H    1 
ATOM   4270 H  HA   . ASN   B 1 20  ? 46.442 -32.850 -11.545 1.00 21.57 ?  20  ASN   B HA   1 
ATOM   4271 H  HB2  . ASN   B 1 20  ? 46.054 -34.812 -12.707 1.00 23.55 ?  20  ASN   B HB2  1 
ATOM   4272 H  HB3  . ASN   B 1 20  ? 47.039 -34.354 -13.865 1.00 23.55 ?  20  ASN   B HB3  1 
ATOM   4273 H  HD21 . ASN   B 1 20  ? 48.902 -35.118 -10.525 1.00 24.97 ?  20  ASN   B HD21 1 
ATOM   4274 H  HD22 . ASN   B 1 20  ? 47.782 -34.137 -10.553 1.00 24.97 ?  20  ASN   B HD22 1 
ATOM   4275 N  N    . ALA   B 1 21  ? 48.333 -31.245 -11.672 1.00 17.60 ?  21  ALA   B N    1 
ATOM   4276 C  CA   . ALA   B 1 21  ? 49.448 -30.323 -11.826 1.00 18.25 ?  21  ALA   B CA   1 
ATOM   4277 C  C    . ALA   B 1 21  ? 49.917 -29.835 -10.464 1.00 17.00 ?  21  ALA   B C    1 
ATOM   4278 O  O    . ALA   B 1 21  ? 49.181 -29.869 -9.475  1.00 17.09 ?  21  ALA   B O    1 
ATOM   4279 C  CB   . ALA   B 1 21  ? 49.061 -29.135 -12.709 1.00 19.53 ?  21  ALA   B CB   1 
ATOM   4280 H  H    . ALA   B 1 21  ? 47.941 -31.210 -10.901 1.00 21.12 ?  21  ALA   B H    1 
ATOM   4281 H  HA   . ALA   B 1 21  ? 50.185 -30.791 -12.246 1.00 21.90 ?  21  ALA   B HA   1 
ATOM   4282 H  HB1  . ALA   B 1 21  ? 49.850 -28.599 -12.863 1.00 23.43 ?  21  ALA   B HB1  1 
ATOM   4283 H  HB2  . ALA   B 1 21  ? 48.718 -29.475 -13.550 1.00 23.43 ?  21  ALA   B HB2  1 
ATOM   4284 H  HB3  . ALA   B 1 21  ? 48.379 -28.616 -12.258 1.00 23.43 ?  21  ALA   B HB3  1 
ATOM   4285 N  N    . ASP   B 1 22  ? 51.171 -29.384 -10.444 1.00 16.42 ?  22  ASP   B N    1 
ATOM   4286 C  CA   . ASP   B 1 22  ? 51.781 -28.692 -9.313  1.00 15.59 ?  22  ASP   B CA   1 
ATOM   4287 C  C    . ASP   B 1 22  ? 51.375 -27.220 -9.392  1.00 14.58 ?  22  ASP   B C    1 
ATOM   4288 O  O    . ASP   B 1 22  ? 51.678 -26.547 -10.381 1.00 14.80 ?  22  ASP   B O    1 
ATOM   4289 C  CB   . ASP   B 1 22  ? 53.300 -28.873 -9.462  1.00 17.22 ?  22  ASP   B CB   1 
ATOM   4290 C  CG   . ASP   B 1 22  ? 54.128 -28.109 -8.434  1.00 19.21 ?  22  ASP   B CG   1 
ATOM   4291 O  OD1  . ASP   B 1 22  ? 53.763 -26.996 -8.032  1.00 18.90 ?  22  ASP   B OD1  1 
ATOM   4292 O  OD2  . ASP   B 1 22  ? 55.204 -28.618 -8.055  1.00 21.82 -1 22  ASP   B OD2  1 
ATOM   4293 H  H    . ASP   B 1 22  ? 51.713 -29.469 -11.110 1.00 19.71 ?  22  ASP   B H    1 
ATOM   4294 H  HA   . ASP   B 1 22  ? 51.486 -29.078 -8.470  1.00 18.71 ?  22  ASP   B HA   1 
ATOM   4295 H  HB2  . ASP   B 1 22  ? 53.520 -29.809 -9.372  1.00 20.66 ?  22  ASP   B HB2  1 
ATOM   4296 H  HB3  . ASP   B 1 22  ? 53.568 -28.551 -10.336 1.00 20.66 ?  22  ASP   B HB3  1 
ATOM   4297 N  N    . ILE   B 1 23  ? 50.671 -26.725 -8.367  1.00 13.82 ?  23  ILE   B N    1 
ATOM   4298 C  CA   . ILE   B 1 23  ? 50.076 -25.386 -8.437  1.00 12.73 ?  23  ILE   B CA   1 
ATOM   4299 C  C    . ILE   B 1 23  ? 51.131 -24.297 -8.582  1.00 12.42 ?  23  ILE   B C    1 
ATOM   4300 O  O    . ILE   B 1 23  ? 50.863 -23.249 -9.182  1.00 12.14 ?  23  ILE   B O    1 
ATOM   4301 C  CB   . ILE   B 1 23  ? 49.144 -25.136 -7.237  1.00 13.29 ?  23  ILE   B CB   1 
ATOM   4302 C  CG1  . ILE   B 1 23  ? 48.316 -23.868 -7.448  1.00 13.78 ?  23  ILE   B CG1  1 
ATOM   4303 C  CG2  . ILE   B 1 23  ? 49.916 -25.096 -5.938  1.00 14.02 ?  23  ILE   B CG2  1 
ATOM   4304 C  CD1  . ILE   B 1 23  ? 47.194 -23.697 -6.433  1.00 14.36 ?  23  ILE   B CD1  1 
ATOM   4305 H  H    . ILE   B 1 23  ? 50.524 -27.144 -7.630  1.00 16.59 ?  23  ILE   B H    1 
ATOM   4306 H  HA   . ILE   B 1 23  ? 49.529 -25.349 -9.233  1.00 15.28 ?  23  ILE   B HA   1 
ATOM   4307 H  HB   . ILE   B 1 23  ? 48.526 -25.882 -7.189  1.00 15.95 ?  23  ILE   B HB   1 
ATOM   4308 H  HG12 . ILE   B 1 23  ? 48.904 -23.095 -7.375  1.00 16.53 ?  23  ILE   B HG12 1 
ATOM   4309 H  HG13 . ILE   B 1 23  ? 47.920 -23.892 -8.334  1.00 16.53 ?  23  ILE   B HG13 1 
ATOM   4310 H  HG21 . ILE   B 1 23  ? 49.292 -25.089 -5.198  1.00 16.83 ?  23  ILE   B HG21 1 
ATOM   4311 H  HG22 . ILE   B 1 23  ? 50.484 -25.882 -5.884  1.00 16.83 ?  23  ILE   B HG22 1 
ATOM   4312 H  HG23 . ILE   B 1 23  ? 50.463 -24.294 -5.919  1.00 16.83 ?  23  ILE   B HG23 1 
ATOM   4313 H  HD11 . ILE   B 1 23  ? 46.672 -22.917 -6.671  1.00 17.23 ?  23  ILE   B HD11 1 
ATOM   4314 H  HD12 . ILE   B 1 23  ? 46.636 -24.491 -6.454  1.00 17.23 ?  23  ILE   B HD12 1 
ATOM   4315 H  HD13 . ILE   B 1 23  ? 47.581 -23.586 -5.553  1.00 17.23 ?  23  ILE   B HD13 1 
ATOM   4316 N  N    . VAL   B 1 24  ? 52.329 -24.502 -8.024  1.00 12.71 ?  24  VAL   B N    1 
ATOM   4317 C  CA   . VAL   B 1 24  ? 53.404 -23.520 -8.189  1.00 13.34 ?  24  VAL   B CA   1 
ATOM   4318 C  C    . VAL   B 1 24  ? 53.860 -23.475 -9.641  1.00 13.75 ?  24  VAL   B C    1 
ATOM   4319 O  O    . VAL   B 1 24  ? 54.007 -22.401 -10.237 1.00 14.15 ?  24  VAL   B O    1 
ATOM   4320 C  CB   . VAL   B 1 24  ? 54.579 -23.837 -7.241  1.00 14.03 ?  24  VAL   B CB   1 
ATOM   4321 C  CG1  . VAL   B 1 24  ? 55.793 -22.967 -7.573  1.00 15.11 ?  24  VAL   B CG1  1 
ATOM   4322 C  CG2  . VAL   B 1 24  ? 54.168 -23.634 -5.803  1.00 15.26 ?  24  VAL   B CG2  1 
ATOM   4323 H  H    . VAL   B 1 24  ? 52.543 -25.188 -7.552  1.00 15.25 ?  24  VAL   B H    1 
ATOM   4324 H  HA   . VAL   B 1 24  ? 53.068 -22.643 -7.955  1.00 16.00 ?  24  VAL   B HA   1 
ATOM   4325 H  HB   . VAL   B 1 24  ? 54.837 -24.767 -7.349  1.00 16.84 ?  24  VAL   B HB   1 
ATOM   4326 H  HG11 . VAL   B 1 24  ? 56.394 -22.966 -6.811  1.00 18.13 ?  24  VAL   B HG11 1 
ATOM   4327 H  HG12 . VAL   B 1 24  ? 56.242 -23.334 -8.348  1.00 18.13 ?  24  VAL   B HG12 1 
ATOM   4328 H  HG13 . VAL   B 1 24  ? 55.490 -22.064 -7.754  1.00 18.13 ?  24  VAL   B HG13 1 
ATOM   4329 H  HG21 . VAL   B 1 24  ? 54.897 -23.899 -5.222  1.00 18.31 ?  24  VAL   B HG21 1 
ATOM   4330 H  HG22 . VAL   B 1 24  ? 53.959 -22.695 -5.665  1.00 18.31 ?  24  VAL   B HG22 1 
ATOM   4331 H  HG23 . VAL   B 1 24  ? 53.384 -24.176 -5.618  1.00 18.31 ?  24  VAL   B HG23 1 
ATOM   4332 N  N    . GLU   B 1 25  ? 54.124 -24.648 -10.225 1.00 14.80 ?  25  GLU   B N    1 
ATOM   4333 C  CA   . GLU   B 1 25  ? 54.518 -24.687 -11.628 1.00 16.20 ?  25  GLU   B CA   1 
ATOM   4334 C  C    . GLU   B 1 25  ? 53.408 -24.151 -12.519 1.00 14.99 ?  25  GLU   B C    1 
ATOM   4335 O  O    . GLU   B 1 25  ? 53.675 -23.432 -13.492 1.00 15.69 ?  25  GLU   B O    1 
ATOM   4336 C  CB   . GLU   B 1 25  ? 54.913 -26.108 -12.023 1.00 20.13 ?  25  GLU   B CB   1 
ATOM   4337 C  CG   . GLU   B 1 25  ? 56.213 -26.557 -11.373 1.00 25.49 ?  25  GLU   B CG   1 
ATOM   4338 C  CD   . GLU   B 1 25  ? 57.333 -25.530 -11.498 1.00 30.29 ?  25  GLU   B CD   1 
ATOM   4339 O  OE1  . GLU   B 1 25  ? 57.722 -25.205 -12.640 1.00 32.28 ?  25  GLU   B OE1  1 
ATOM   4340 O  OE2  . GLU   B 1 25  ? 57.816 -25.030 -10.454 1.00 31.88 -1 25  GLU   B OE2  1 
ATOM   4341 H  H    . GLU   B 1 25  ? 54.085 -25.414 -9.834  1.00 17.76 ?  25  GLU   B H    1 
ATOM   4342 H  HA   . GLU   B 1 25  ? 55.277 -24.101 -11.752 1.00 19.44 ?  25  GLU   B HA   1 
ATOM   4343 H  HB2  . GLU   B 1 25  ? 54.210 -26.719 -11.742 1.00 24.16 ?  25  GLU   B HB2  1 
ATOM   4344 H  HB3  . GLU   B 1 25  ? 55.021 -26.149 -12.985 1.00 24.16 ?  25  GLU   B HB3  1 
ATOM   4345 H  HG2  . GLU   B 1 25  ? 56.060 -26.705 -10.432 1.00 30.59 ?  25  GLU   B HG2  1 
ATOM   4346 H  HG3  . GLU   B 1 25  ? 56.511 -27.371 -11.803 1.00 30.59 ?  25  GLU   B HG3  1 
ATOM   4347 N  N    . GLU   B 1 26  ? 52.155 -24.468 -12.183 1.00 14.01 ?  26  GLU   B N    1 
ATOM   4348 C  CA   . GLU   B 1 26  ? 51.028 -23.944 -12.945 1.00 14.81 ?  26  GLU   B CA   1 
ATOM   4349 C  C    . GLU   B 1 26  ? 50.977 -22.426 -12.874 1.00 13.71 ?  26  GLU   B C    1 
ATOM   4350 O  O    . GLU   B 1 26  ? 50.786 -21.756 -13.893 1.00 15.00 ?  26  GLU   B O    1 
ATOM   4351 C  CB   . GLU   B 1 26  ? 49.713 -24.527 -12.425 1.00 16.65 ?  26  GLU   B CB   1 
ATOM   4352 C  CG   . GLU   B 1 26  ? 49.268 -25.803 -13.110 1.00 20.24 ?  26  GLU   B CG   1 
ATOM   4353 C  CD   . GLU   B 1 26  ? 49.024 -25.646 -14.610 1.00 21.97 ?  26  GLU   B CD   1 
ATOM   4354 O  OE1  . GLU   B 1 26  ? 48.058 -24.972 -15.032 1.00 22.54 ?  26  GLU   B OE1  1 
ATOM   4355 O  OE2  . GLU   B 1 26  ? 49.801 -26.233 -15.372 1.00 24.13 -1 26  GLU   B OE2  1 
ATOM   4356 H  H    . GLU   B 1 26  ? 51.932 -24.982 -11.525 1.00 16.81 ?  26  GLU   B H    1 
ATOM   4357 H  HA   . GLU   B 1 26  ? 51.130 -24.198 -13.872 1.00 17.77 ?  26  GLU   B HA   1 
ATOM   4358 H  HB2  . GLU   B 1 26  ? 49.810 -24.721 -11.477 1.00 19.98 ?  26  GLU   B HB2  1 
ATOM   4359 H  HB3  . GLU   B 1 26  ? 49.011 -23.865 -12.546 1.00 19.98 ?  26  GLU   B HB3  1 
ATOM   4360 H  HG2  . GLU   B 1 26  ? 49.967 -26.457 -13.007 1.00 24.29 ?  26  GLU   B HG2  1 
ATOM   4361 H  HG3  . GLU   B 1 26  ? 48.448 -26.108 -12.695 1.00 24.29 ?  26  GLU   B HG3  1 
ATOM   4362 N  N    . ALA   B 1 27  ? 51.127 -21.865 -11.673 1.00 12.74 ?  27  ALA   B N    1 
ATOM   4363 C  CA   . ALA   B 1 27  ? 51.079 -20.414 -11.537 1.00 13.27 ?  27  ALA   B CA   1 
ATOM   4364 C  C    . ALA   B 1 27  ? 52.155 -19.750 -12.392 1.00 14.41 ?  27  ALA   B C    1 
ATOM   4365 O  O    . ALA   B 1 27  ? 51.900 -18.741 -13.066 1.00 15.29 ?  27  ALA   B O    1 
ATOM   4366 C  CB   . ALA   B 1 27  ? 51.215 -20.022 -10.065 1.00 13.53 ?  27  ALA   B CB   1 
ATOM   4367 H  H    . ALA   B 1 27  ? 51.242 -22.296 -10.932 1.00 15.29 ?  27  ALA   B H    1 
ATOM   4368 H  HA   . ALA   B 1 27  ? 50.219 -20.097 -11.843 1.00 15.93 ?  27  ALA   B HA   1 
ATOM   4369 H  HB1  . ALA   B 1 27  ? 51.173 -19.053 -9.990  1.00 16.24 ?  27  ALA   B HB1  1 
ATOM   4370 H  HB2  . ALA   B 1 27  ? 50.479 -20.416 -9.562  1.00 16.24 ?  27  ALA   B HB2  1 
ATOM   4371 H  HB3  . ALA   B 1 27  ? 52.058 -20.344 -9.721  1.00 16.24 ?  27  ALA   B HB3  1 
ATOM   4372 N  N    . LYS   B 1 28  ? 53.367 -20.308 -12.389 1.00 15.99 ?  28  LYS   B N    1 
ATOM   4373 C  CA   . LYS   B 1 28  ? 54.442 -19.698 -13.162 1.00 18.11 ?  28  LYS   B CA   1 
ATOM   4374 C  C    . LYS   B 1 28  ? 54.179 -19.781 -14.660 1.00 18.82 ?  28  LYS   B C    1 
ATOM   4375 O  O    . LYS   B 1 28  ? 54.591 -18.886 -15.409 1.00 19.77 ?  28  LYS   B O    1 
ATOM   4376 C  CB   . LYS   B 1 28  ? 55.795 -20.304 -12.776 1.00 20.98 ?  28  LYS   B CB   1 
ATOM   4377 C  CG   . LYS   B 1 28  ? 56.195 -19.948 -11.350 1.00 24.02 ?  28  LYS   B CG   1 
ATOM   4378 C  CD   . LYS   B 1 28  ? 57.625 -20.339 -11.002 1.00 28.50 ?  28  LYS   B CD   1 
ATOM   4379 C  CE   . LYS   B 1 28  ? 57.752 -21.815 -10.716 1.00 31.82 ?  28  LYS   B CE   1 
ATOM   4380 N  NZ   . LYS   B 1 28  ? 59.095 -22.138 -10.157 1.00 33.64 ?  28  LYS   B NZ   1 
ATOM   4381 H  H    . LYS   B 1 28  ? 53.587 -21.018 -11.954 1.00 19.19 ?  28  LYS   B H    1 
ATOM   4382 H  HA   . LYS   B 1 28  ? 54.480 -18.758 -12.940 1.00 21.74 ?  28  LYS   B HA   1 
ATOM   4383 H  HB2  . LYS   B 1 28  ? 55.746 -21.268 -12.845 1.00 25.18 ?  28  LYS   B HB2  1 
ATOM   4384 H  HB3  . LYS   B 1 28  ? 56.479 -19.960 -13.375 1.00 25.18 ?  28  LYS   B HB3  1 
ATOM   4385 H  HG2  . LYS   B 1 28  ? 56.109 -18.988 -11.236 1.00 28.82 ?  28  LYS   B HG2  1 
ATOM   4386 H  HG3  . LYS   B 1 28  ? 55.600 -20.407 -10.740 1.00 28.82 ?  28  LYS   B HG3  1 
ATOM   4387 H  HD2  . LYS   B 1 28  ? 58.204 -20.121 -11.749 1.00 34.20 ?  28  LYS   B HD2  1 
ATOM   4388 H  HD3  . LYS   B 1 28  ? 57.901 -19.849 -10.211 1.00 34.20 ?  28  LYS   B HD3  1 
ATOM   4389 H  HE2  . LYS   B 1 28  ? 57.080 -22.076 -10.067 1.00 38.18 ?  28  LYS   B HE2  1 
ATOM   4390 H  HE3  . LYS   B 1 28  ? 57.635 -22.314 -11.540 1.00 38.18 ?  28  LYS   B HE3  1 
ATOM   4391 H  HZ1  . LYS   B 1 28  ? 59.155 -23.010 -9.993  1.00 40.37 ?  28  LYS   B HZ1  1 
ATOM   4392 H  HZ2  . LYS   B 1 28  ? 59.729 -21.907 -10.738 1.00 40.37 ?  28  LYS   B HZ2  1 
ATOM   4393 H  HZ3  . LYS   B 1 28  ? 59.223 -21.691 -9.398  1.00 40.37 ?  28  LYS   B HZ3  1 
ATOM   4394 N  N    . LYS   B 1 29  ? 53.471 -20.818 -15.109 1.00 19.89 ?  29  LYS   B N    1 
ATOM   4395 C  CA   . LYS   B 1 29  ? 53.190 -20.979 -16.531 1.00 22.67 ?  29  LYS   B CA   1 
ATOM   4396 C  C    . LYS   B 1 29  ? 51.944 -20.220 -16.978 1.00 21.42 ?  29  LYS   B C    1 
ATOM   4397 O  O    . LYS   B 1 29  ? 51.949 -19.606 -18.051 1.00 22.86 ?  29  LYS   B O    1 
ATOM   4398 C  CB   . LYS   B 1 29  ? 53.053 -22.465 -16.873 1.00 27.53 ?  29  LYS   B CB   1 
ATOM   4399 C  CG   . LYS   B 1 29  ? 53.002 -22.755 -18.362 1.00 31.89 ?  29  LYS   B CG   1 
ATOM   4400 C  CD   . LYS   B 1 29  ? 53.219 -24.237 -18.644 1.00 35.43 ?  29  LYS   B CD   1 
ATOM   4401 C  CE   . LYS   B 1 29  ? 52.034 -25.081 -18.203 1.00 37.90 ?  29  LYS   B CE   1 
ATOM   4402 N  NZ   . LYS   B 1 29  ? 52.261 -26.533 -18.465 1.00 38.88 ?  29  LYS   B NZ   1 
ATOM   4403 H  H    . LYS   B 1 29  ? 53.141 -21.442 -14.607 1.00 23.87 ?  29  LYS   B H    1 
ATOM   4404 H  HA   . LYS   B 1 29  ? 53.938 -20.631 -17.029 1.00 27.20 ?  29  LYS   B HA   1 
ATOM   4405 H  HB2  . LYS   B 1 29  ? 53.820 -22.937 -16.510 1.00 33.03 ?  29  LYS   B HB2  1 
ATOM   4406 H  HB3  . LYS   B 1 29  ? 52.239 -22.807 -16.480 1.00 33.03 ?  29  LYS   B HB3  1 
ATOM   4407 H  HG2  . LYS   B 1 29  ? 52.132 -22.501 -18.707 1.00 38.27 ?  29  LYS   B HG2  1 
ATOM   4408 H  HG3  . LYS   B 1 29  ? 53.701 -22.252 -18.811 1.00 38.27 ?  29  LYS   B HG3  1 
ATOM   4409 H  HD2  . LYS   B 1 29  ? 53.345 -24.365 -19.596 1.00 42.52 ?  29  LYS   B HD2  1 
ATOM   4410 H  HD3  . LYS   B 1 29  ? 54.004 -24.542 -18.160 1.00 42.52 ?  29  LYS   B HD3  1 
ATOM   4411 H  HE2  . LYS   B 1 29  ? 51.892 -24.965 -17.250 1.00 45.48 ?  29  LYS   B HE2  1 
ATOM   4412 H  HE3  . LYS   B 1 29  ? 51.244 -24.805 -18.695 1.00 45.48 ?  29  LYS   B HE3  1 
ATOM   4413 H  HZ1  . LYS   B 1 29  ? 51.554 -27.005 -18.200 1.00 46.66 ?  29  LYS   B HZ1  1 
ATOM   4414 H  HZ2  . LYS   B 1 29  ? 52.389 -26.669 -19.335 1.00 46.66 ?  29  LYS   B HZ2  1 
ATOM   4415 H  HZ3  . LYS   B 1 29  ? 52.979 -26.814 -18.020 1.00 46.66 ?  29  LYS   B HZ3  1 
ATOM   4416 N  N    . VAL   B 1 30  ? 50.881 -20.256 -16.172 1.00 19.31 ?  30  VAL   B N    1 
ATOM   4417 C  CA   . VAL   B 1 30  ? 49.592 -19.666 -16.542 1.00 19.43 ?  30  VAL   B CA   1 
ATOM   4418 C  C    . VAL   B 1 30  ? 49.594 -18.153 -16.388 1.00 18.46 ?  30  VAL   B C    1 
ATOM   4419 O  O    . VAL   B 1 30  ? 48.872 -17.445 -17.105 1.00 19.26 ?  30  VAL   B O    1 
ATOM   4420 C  CB   . VAL   B 1 30  ? 48.497 -20.288 -15.654 1.00 20.70 ?  30  VAL   B CB   1 
ATOM   4421 C  CG1  . VAL   B 1 30  ? 47.209 -19.475 -15.703 1.00 21.48 ?  30  VAL   B CG1  1 
ATOM   4422 C  CG2  . VAL   B 1 30  ? 48.250 -21.740 -16.044 1.00 21.59 ?  30  VAL   B CG2  1 
ATOM   4423 H  H    . VAL   B 1 30  ? 50.871 -20.643 -15.395 1.00 23.18 ?  30  VAL   B H    1 
ATOM   4424 H  HA   . VAL   B 1 30  ? 49.393 -19.892 -17.463 1.00 23.32 ?  30  VAL   B HA   1 
ATOM   4425 H  HB   . VAL   B 1 30  ? 48.806 -20.291 -14.734 1.00 24.84 ?  30  VAL   B HB   1 
ATOM   4426 H  HG11 . VAL   B 1 30  ? 46.474 -20.058 -15.462 1.00 25.78 ?  30  VAL   B HG11 1 
ATOM   4427 H  HG12 . VAL   B 1 30  ? 47.271 -18.746 -15.069 1.00 25.78 ?  30  VAL   B HG12 1 
ATOM   4428 H  HG13 . VAL   B 1 30  ? 47.078 -19.142 -16.599 1.00 25.78 ?  30  VAL   B HG13 1 
ATOM   4429 H  HG21 . VAL   B 1 30  ? 47.566 -22.114 -15.461 1.00 25.91 ?  30  VAL   B HG21 1 
ATOM   4430 H  HG22 . VAL   B 1 30  ? 47.946 -21.773 -16.966 1.00 25.91 ?  30  VAL   B HG22 1 
ATOM   4431 H  HG23 . VAL   B 1 30  ? 49.073 -22.241 -15.948 1.00 25.91 ?  30  VAL   B HG23 1 
ATOM   4432 N  N    A LYS   B 1 31  ? 50.373 -17.637 -15.447 0.64 18.01 ?  31  LYS   B N    1 
ATOM   4433 N  N    B LYS   B 1 31  ? 50.371 -17.645 -15.443 0.36 18.25 ?  31  LYS   B N    1 
ATOM   4434 C  CA   A LYS   B 1 31  ? 50.408 -16.224 -15.099 0.64 18.08 ?  31  LYS   B CA   1 
ATOM   4435 C  CA   B LYS   B 1 31  ? 50.406 -16.235 -15.093 0.36 18.34 ?  31  LYS   B CA   1 
ATOM   4436 C  C    A LYS   B 1 31  ? 49.021 -15.727 -14.694 0.64 16.15 ?  31  LYS   B C    1 
ATOM   4437 C  C    B LYS   B 1 31  ? 49.004 -15.762 -14.722 0.36 16.24 ?  31  LYS   B C    1 
ATOM   4438 O  O    A LYS   B 1 31  ? 48.496 -14.779 -15.293 0.64 17.02 ?  31  LYS   B O    1 
ATOM   4439 O  O    B LYS   B 1 31  ? 48.443 -14.882 -15.387 0.36 16.46 ?  31  LYS   B O    1 
ATOM   4440 C  CB   A LYS   B 1 31  ? 51.030 -15.410 -16.238 0.64 20.78 ?  31  LYS   B CB   1 
ATOM   4441 C  CB   B LYS   B 1 31  ? 51.027 -15.426 -16.233 0.36 20.73 ?  31  LYS   B CB   1 
ATOM   4442 C  CG   A LYS   B 1 31  ? 52.480 -15.800 -16.531 0.64 23.44 ?  31  LYS   B CG   1 
ATOM   4443 C  CG   B LYS   B 1 31  ? 52.433 -15.901 -16.588 0.36 22.90 ?  31  LYS   B CG   1 
ATOM   4444 C  CD   A LYS   B 1 31  ? 53.059 -14.989 -17.677 0.64 26.27 ?  31  LYS   B CD   1 
ATOM   4445 C  CD   B LYS   B 1 31  ? 53.012 -15.138 -17.762 0.36 24.88 ?  31  LYS   B CD   1 
ATOM   4446 C  CE   A LYS   B 1 31  ? 54.537 -15.265 -17.859 0.64 28.50 ?  31  LYS   B CE   1 
ATOM   4447 C  CE   B LYS   B 1 31  ? 54.495 -15.414 -17.916 0.36 26.47 ?  31  LYS   B CE   1 
ATOM   4448 N  NZ   A LYS   B 1 31  ? 55.295 -14.923 -16.627 0.64 29.79 ?  31  LYS   B NZ   1 
ATOM   4449 N  NZ   B LYS   B 1 31  ? 55.233 -15.058 -16.674 0.36 27.41 ?  31  LYS   B NZ   1 
ATOM   4450 H  H    A LYS   B 1 31  ? 50.910 -18.117 -14.980 0.64 21.61 ?  31  LYS   B H    1 
ATOM   4451 H  H    B LYS   B 1 31  ? 50.905 -18.124 -14.974 0.36 21.90 ?  31  LYS   B H    1 
ATOM   4452 H  HA   A LYS   B 1 31  ? 50.973 -16.130 -14.331 0.64 21.69 ?  31  LYS   B HA   1 
ATOM   4453 H  HA   B LYS   B 1 31  ? 50.969 -16.134 -14.320 0.36 22.01 ?  31  LYS   B HA   1 
ATOM   4454 H  HB2  A LYS   B 1 31  ? 50.518 -15.547 -17.049 0.64 24.93 ?  31  LYS   B HB2  1 
ATOM   4455 H  HB2  B LYS   B 1 31  ? 50.477 -15.507 -17.025 0.36 24.88 ?  31  LYS   B HB2  1 
ATOM   4456 H  HB3  A LYS   B 1 31  ? 51.019 -14.475 -15.990 0.64 24.93 ?  31  LYS   B HB3  1 
ATOM   4457 H  HB3  B LYS   B 1 31  ? 51.088 -14.498 -15.961 0.36 24.88 ?  31  LYS   B HB3  1 
ATOM   4458 H  HG2  A LYS   B 1 31  ? 53.015 -15.640 -15.737 0.64 28.13 ?  31  LYS   B HG2  1 
ATOM   4459 H  HG2  B LYS   B 1 31  ? 53.010 -15.773 -15.819 0.36 27.48 ?  31  LYS   B HG2  1 
ATOM   4460 H  HG3  A LYS   B 1 31  ? 52.516 -16.740 -16.773 0.64 28.13 ?  31  LYS   B HG3  1 
ATOM   4461 H  HG3  B LYS   B 1 31  ? 52.404 -16.841 -16.827 0.36 27.48 ?  31  LYS   B HG3  1 
ATOM   4462 H  HD2  A LYS   B 1 31  ? 52.601 -15.227 -18.497 0.64 31.52 ?  31  LYS   B HD2  1 
ATOM   4463 H  HD2  B LYS   B 1 31  ? 52.564 -15.415 -18.575 0.36 29.86 ?  31  LYS   B HD2  1 
ATOM   4464 H  HD3  A LYS   B 1 31  ? 52.947 -14.046 -17.487 0.64 31.52 ?  31  LYS   B HD3  1 
ATOM   4465 H  HD3  B LYS   B 1 31  ? 52.893 -14.188 -17.615 0.36 29.86 ?  31  LYS   B HD3  1 
ATOM   4466 H  HE2  A LYS   B 1 31  ? 54.670 -16.208 -18.049 0.64 34.20 ?  31  LYS   B HE2  1 
ATOM   4467 H  HE2  B LYS   B 1 31  ? 54.632 -16.359 -18.093 0.36 31.76 ?  31  LYS   B HE2  1 
ATOM   4468 H  HE3  A LYS   B 1 31  ? 54.878 -14.724 -18.589 0.64 34.20 ?  31  LYS   B HE3  1 
ATOM   4469 H  HE3  B LYS   B 1 31  ? 54.848 -14.880 -18.646 0.36 31.76 ?  31  LYS   B HE3  1 
ATOM   4470 H  HZ1  A LYS   B 1 31  ? 56.169 -14.972 -16.782 0.64 35.75 ?  31  LYS   B HZ1  1 
ATOM   4471 H  HZ1  B LYS   B 1 31  ? 56.108 -15.045 -16.833 0.36 32.89 ?  31  LYS   B HZ1  1 
ATOM   4472 H  HZ2  A LYS   B 1 31  ? 55.093 -14.096 -16.367 0.64 35.75 ?  31  LYS   B HZ2  1 
ATOM   4473 H  HZ2  B LYS   B 1 31  ? 54.978 -14.253 -16.391 0.36 32.89 ?  31  LYS   B HZ2  1 
ATOM   4474 H  HZ3  A LYS   B 1 31  ? 55.085 -15.490 -15.973 0.64 35.75 ?  31  LYS   B HZ3  1 
ATOM   4475 H  HZ3  B LYS   B 1 31  ? 55.063 -15.655 -16.036 0.36 32.89 ?  31  LYS   B HZ3  1 
ATOM   4476 N  N    . PRO   B 1 32  ? 48.412 -16.321 -13.665 1.00 14.57 ?  32  PRO   B N    1 
ATOM   4477 C  CA   . PRO   B 1 32  ? 47.037 -15.957 -13.303 1.00 13.74 ?  32  PRO   B CA   1 
ATOM   4478 C  C    . PRO   B 1 32  ? 46.959 -14.612 -12.599 1.00 13.61 ?  32  PRO   B C    1 
ATOM   4479 O  O    . PRO   B 1 32  ? 47.881 -14.193 -11.893 1.00 14.71 ?  32  PRO   B O    1 
ATOM   4480 C  CB   . PRO   B 1 32  ? 46.643 -17.072 -12.327 1.00 13.92 ?  32  PRO   B CB   1 
ATOM   4481 C  CG   . PRO   B 1 32  ? 47.939 -17.419 -11.652 1.00 13.94 ?  32  PRO   B CG   1 
ATOM   4482 C  CD   . PRO   B 1 32  ? 48.993 -17.293 -12.715 1.00 14.28 ?  32  PRO   B CD   1 
ATOM   4483 H  HA   . PRO   B 1 32  ? 46.460 -15.973 -14.083 1.00 16.49 ?  32  PRO   B HA   1 
ATOM   4484 H  HB2  . PRO   B 1 32  ? 45.993 -16.740 -11.687 1.00 16.70 ?  32  PRO   B HB2  1 
ATOM   4485 H  HB3  . PRO   B 1 32  ? 46.290 -17.835 -12.815 1.00 16.70 ?  32  PRO   B HB3  1 
ATOM   4486 H  HG2  . PRO   B 1 32  ? 48.109 -16.795 -10.925 1.00 16.73 ?  32  PRO   B HG2  1 
ATOM   4487 H  HG3  . PRO   B 1 32  ? 47.906 -18.329 -11.316 1.00 16.73 ?  32  PRO   B HG3  1 
ATOM   4488 H  HD2  . PRO   B 1 32  ? 49.809 -16.942 -12.329 1.00 17.13 ?  32  PRO   B HD2  1 
ATOM   4489 H  HD3  . PRO   B 1 32  ? 49.129 -18.141 -13.147 1.00 17.13 ?  32  PRO   B HD3  1 
ATOM   4490 N  N    . THR   B 1 33  ? 45.808 -13.953 -12.768 1.00 13.28 ?  33  THR   B N    1 
ATOM   4491 C  CA   . THR   B 1 33  ? 45.519 -12.775 -11.956 1.00 13.40 ?  33  THR   B CA   1 
ATOM   4492 C  C    . THR   B 1 33  ? 45.478 -13.133 -10.474 1.00 12.95 ?  33  THR   B C    1 
ATOM   4493 O  O    . THR   B 1 33  ? 45.948 -12.354 -9.629  1.00 13.81 ?  33  THR   B O    1 
ATOM   4494 C  CB   . THR   B 1 33  ? 44.197 -12.143 -12.403 1.00 14.30 ?  33  THR   B CB   1 
ATOM   4495 O  OG1  . THR   B 1 33  ? 44.244 -11.878 -13.809 1.00 14.09 ?  33  THR   B OG1  1 
ATOM   4496 C  CG2  . THR   B 1 33  ? 43.937 -10.847 -11.642 1.00 15.51 ?  33  THR   B CG2  1 
ATOM   4497 H  H    . THR   B 1 33  ? 45.192 -14.165 -13.337 1.00 15.94 ?  33  THR   B H    1 
ATOM   4498 H  HA   . THR   B 1 33  ? 46.217 -12.122 -12.090 1.00 16.08 ?  33  THR   B HA   1 
ATOM   4499 H  HB   . THR   B 1 33  ? 43.466 -12.761 -12.218 1.00 17.16 ?  33  THR   B HB   1 
ATOM   4500 H  HG1  . THR   B 1 33  ? 43.519 -11.521 -14.059 1.00 16.90 ?  33  THR   B HG1  1 
ATOM   4501 H  HG21 . THR   B 1 33  ? 43.184 -10.380 -12.030 1.00 18.61 ?  33  THR   B HG21 1 
ATOM   4502 H  HG22 . THR   B 1 33  ? 43.744 -11.040 -10.710 1.00 18.61 ?  33  THR   B HG22 1 
ATOM   4503 H  HG23 . THR   B 1 33  ? 44.721 -10.277 -11.689 1.00 18.61 ?  33  THR   B HG23 1 
ATOM   4504 N  N    . VAL   B 1 34  ? 44.919 -14.300 -10.136 1.00 12.19 ?  34  VAL   B N    1 
ATOM   4505 C  CA   . VAL   B 1 34  ? 44.722 -14.696 -8.745  1.00 11.60 ?  34  VAL   B CA   1 
ATOM   4506 C  C    . VAL   B 1 34  ? 45.140 -16.148 -8.574  1.00 10.45 ?  34  VAL   B C    1 
ATOM   4507 O  O    . VAL   B 1 34  ? 44.612 -17.034 -9.254  1.00 11.39 ?  34  VAL   B O    1 
ATOM   4508 C  CB   . VAL   B 1 34  ? 43.252 -14.542 -8.300  1.00 12.76 ?  34  VAL   B CB   1 
ATOM   4509 C  CG1  . VAL   B 1 34  ? 43.088 -14.999 -6.857  1.00 12.91 ?  34  VAL   B CG1  1 
ATOM   4510 C  CG2  . VAL   B 1 34  ? 42.759 -13.117 -8.484  1.00 13.58 ?  34  VAL   B CG2  1 
ATOM   4511 H  H    . VAL   B 1 34  ? 44.645 -14.890 -10.705 1.00 14.63 ?  34  VAL   B H    1 
ATOM   4512 H  HA   . VAL   B 1 34  ? 45.279 -14.142 -8.172  1.00 13.92 ?  34  VAL   B HA   1 
ATOM   4513 H  HB   . VAL   B 1 34  ? 42.704 -15.117 -8.854  1.00 15.31 ?  34  VAL   B HB   1 
ATOM   4514 H  HG11 . VAL   B 1 34  ? 42.240 -14.673 -6.517  1.00 15.49 ?  34  VAL   B HG11 1 
ATOM   4515 H  HG12 . VAL   B 1 34  ? 43.102 -15.970 -6.824  1.00 15.49 ?  34  VAL   B HG12 1 
ATOM   4516 H  HG13 . VAL   B 1 34  ? 43.815 -14.640 -6.324  1.00 15.49 ?  34  VAL   B HG13 1 
ATOM   4517 H  HG21 . VAL   B 1 34  ? 41.841 -13.059 -8.174  1.00 16.30 ?  34  VAL   B HG21 1 
ATOM   4518 H  HG22 . VAL   B 1 34  ? 43.321 -12.518 -7.972  1.00 16.30 ?  34  VAL   B HG22 1 
ATOM   4519 H  HG23 . VAL   B 1 34  ? 42.803 -12.887 -9.427  1.00 16.30 ?  34  VAL   B HG23 1 
ATOM   4520 N  N    . VAL   B 1 35  ? 46.044 -16.399 -7.631  1.00 10.01 ?  35  VAL   B N    1 
ATOM   4521 C  CA   . VAL   B 1 35  ? 46.278 -17.742 -7.111  1.00 10.00 ?  35  VAL   B CA   1 
ATOM   4522 C  C    . VAL   B 1 35  ? 45.742 -17.795 -5.690  1.00 9.75  ?  35  VAL   B C    1 
ATOM   4523 O  O    . VAL   B 1 35  ? 45.956 -16.868 -4.903  1.00 10.29 ?  35  VAL   B O    1 
ATOM   4524 C  CB   . VAL   B 1 35  ? 47.762 -18.171 -7.193  1.00 11.13 ?  35  VAL   B CB   1 
ATOM   4525 C  CG1  . VAL   B 1 35  ? 48.666 -17.317 -6.292  1.00 11.77 ?  35  VAL   B CG1  1 
ATOM   4526 C  CG2  . VAL   B 1 35  ? 47.904 -19.656 -6.856  1.00 11.58 ?  35  VAL   B CG2  1 
ATOM   4527 H  H    . VAL   B 1 35  ? 46.544 -15.794 -7.267  1.00 12.02 ?  35  VAL   B H    1 
ATOM   4528 H  HA   . VAL   B 1 35  ? 45.759 -18.368 -7.637  1.00 12.00 ?  35  VAL   B HA   1 
ATOM   4529 H  HB   . VAL   B 1 35  ? 48.059 -18.052 -8.110  1.00 13.36 ?  35  VAL   B HB   1 
ATOM   4530 H  HG11 . VAL   B 1 35  ? 49.586 -17.555 -6.469  1.00 14.12 ?  35  VAL   B HG11 1 
ATOM   4531 H  HG12 . VAL   B 1 35  ? 48.511 -16.385 -6.493  1.00 14.12 ?  35  VAL   B HG12 1 
ATOM   4532 H  HG13 . VAL   B 1 35  ? 48.443 -17.503 -5.367  1.00 14.12 ?  35  VAL   B HG13 1 
ATOM   4533 H  HG21 . VAL   B 1 35  ? 48.824 -19.925 -6.972  1.00 13.89 ?  35  VAL   B HG21 1 
ATOM   4534 H  HG22 . VAL   B 1 35  ? 47.628 -19.803 -5.934  1.00 13.89 ?  35  VAL   B HG22 1 
ATOM   4535 H  HG23 . VAL   B 1 35  ? 47.330 -20.177 -7.450  1.00 13.89 ?  35  VAL   B HG23 1 
ATOM   4536 N  N    . VAL   B 1 36  ? 45.020 -18.870 -5.373  1.00 9.91  ?  36  VAL   B N    1 
ATOM   4537 C  CA   . VAL   B 1 36  ? 44.474 -19.070 -4.040  1.00 9.66  ?  36  VAL   B CA   1 
ATOM   4538 C  C    . VAL   B 1 36  ? 45.478 -19.833 -3.182  1.00 9.45  ?  36  VAL   B C    1 
ATOM   4539 O  O    . VAL   B 1 36  ? 46.018 -20.871 -3.599  1.00 10.42 ?  36  VAL   B O    1 
ATOM   4540 C  CB   . VAL   B 1 36  ? 43.132 -19.823 -4.115  1.00 10.22 ?  36  VAL   B CB   1 
ATOM   4541 C  CG1  . VAL   B 1 36  ? 42.633 -20.189 -2.722  1.00 10.62 ?  36  VAL   B CG1  1 
ATOM   4542 C  CG2  . VAL   B 1 36  ? 42.103 -18.991 -4.848  1.00 10.66 ?  36  VAL   B CG2  1 
ATOM   4543 H  H    . VAL   B 1 36  ? 44.835 -19.507 -5.921  1.00 11.89 ?  36  VAL   B H    1 
ATOM   4544 H  HA   . VAL   B 1 36  ? 44.307 -18.207 -3.627  1.00 11.59 ?  36  VAL   B HA   1 
ATOM   4545 H  HB   . VAL   B 1 36  ? 43.258 -20.647 -4.612  1.00 12.27 ?  36  VAL   B HB   1 
ATOM   4546 H  HG11 . VAL   B 1 36  ? 41.691 -20.415 -2.773  1.00 12.74 ?  36  VAL   B HG11 1 
ATOM   4547 H  HG12 . VAL   B 1 36  ? 43.138 -20.942 -2.387  1.00 12.74 ?  36  VAL   B HG12 1 
ATOM   4548 H  HG13 . VAL   B 1 36  ? 42.751 -19.420 -2.135  1.00 12.74 ?  36  VAL   B HG13 1 
ATOM   4549 H  HG21 . VAL   B 1 36  ? 41.261 -19.472 -4.869  1.00 12.79 ?  36  VAL   B HG21 1 
ATOM   4550 H  HG22 . VAL   B 1 36  ? 41.989 -18.147 -4.380  1.00 12.79 ?  36  VAL   B HG22 1 
ATOM   4551 H  HG23 . VAL   B 1 36  ? 42.413 -18.826 -5.752  1.00 12.79 ?  36  VAL   B HG23 1 
ATOM   4552 N  N    . ASN   B 1 37  ? 45.696 -19.337 -1.964  1.00 9.92  ?  37  ASN   B N    1 
ATOM   4553 C  CA   . ASN   B 1 37  ? 46.447 -20.059 -0.949  1.00 10.28 ?  37  ASN   B CA   1 
ATOM   4554 C  C    . ASN   B 1 37  ? 45.500 -20.728 0.040   1.00 10.22 ?  37  ASN   B C    1 
ATOM   4555 O  O    . ASN   B 1 37  ? 44.488 -20.149 0.450   1.00 10.37 ?  37  ASN   B O    1 
ATOM   4556 C  CB   . ASN   B 1 37  ? 47.385 -19.115 -0.199  1.00 10.30 ?  37  ASN   B CB   1 
ATOM   4557 C  CG   . ASN   B 1 37  ? 48.231 -19.832 0.818   1.00 10.48 ?  37  ASN   B CG   1 
ATOM   4558 O  OD1  . ASN   B 1 37  ? 48.569 -21.011 0.650   1.00 11.19 ?  37  ASN   B OD1  1 
ATOM   4559 N  ND2  . ASN   B 1 37  ? 48.575 -19.127 1.884   1.00 10.54 ?  37  ASN   B ND2  1 
ATOM   4560 H  H    . ASN   B 1 37  ? 45.405 -18.567 -1.698  1.00 11.90 ?  37  ASN   B H    1 
ATOM   4561 H  HA   . ASN   B 1 37  ? 46.975 -20.750 -1.372  1.00 12.33 ?  37  ASN   B HA   1 
ATOM   4562 H  HB2  . ASN   B 1 37  ? 47.981 -18.697 -0.838  1.00 12.36 ?  37  ASN   B HB2  1 
ATOM   4563 H  HB3  . ASN   B 1 37  ? 46.861 -18.444 0.262   1.00 12.36 ?  37  ASN   B HB3  1 
ATOM   4564 H  HD21 . ASN   B 1 37  ? 49.068 -19.481 2.494   1.00 12.64 ?  37  ASN   B HD21 1 
ATOM   4565 H  HD22 . ASN   B 1 37  ? 48.328 -18.311 1.964   1.00 12.64 ?  37  ASN   B HD22 1 
ATOM   4566 N  N    . ALA   B 1 38  ? 45.844 -21.963 0.412   1.00 10.39 ?  38  ALA   B N    1 
ATOM   4567 C  CA   . ALA   B 1 38  ? 45.191 -22.709 1.490   1.00 10.68 ?  38  ALA   B CA   1 
ATOM   4568 C  C    . ALA   B 1 38  ? 45.774 -22.220 2.816   1.00 10.63 ?  38  ALA   B C    1 
ATOM   4569 O  O    . ALA   B 1 38  ? 46.678 -22.824 3.404   1.00 11.70 ?  38  ALA   B O    1 
ATOM   4570 C  CB   . ALA   B 1 38  ? 45.418 -24.205 1.301   1.00 12.10 ?  38  ALA   B CB   1 
ATOM   4571 H  H    . ALA   B 1 38  ? 46.488 -22.404 0.049   1.00 12.47 ?  38  ALA   B H    1 
ATOM   4572 H  HA   . ALA   B 1 38  ? 44.238 -22.534 1.485   1.00 12.81 ?  38  ALA   B HA   1 
ATOM   4573 H  HB1  . ALA   B 1 38  ? 44.975 -24.686 2.025   1.00 14.52 ?  38  ALA   B HB1  1 
ATOM   4574 H  HB2  . ALA   B 1 38  ? 45.040 -24.477 0.452   1.00 14.52 ?  38  ALA   B HB2  1 
ATOM   4575 H  HB3  . ALA   B 1 38  ? 46.368 -24.389 1.320   1.00 14.52 ?  38  ALA   B HB3  1 
ATOM   4576 N  N    . ALA   B 1 39  ? 45.257 -21.079 3.273   1.00 10.48 ?  39  ALA   B N    1 
ATOM   4577 C  CA   . ALA   B 1 39  ? 45.805 -20.341 4.400   1.00 11.01 ?  39  ALA   B CA   1 
ATOM   4578 C  C    . ALA   B 1 39  ? 45.193 -20.786 5.728   1.00 10.77 ?  39  ALA   B C    1 
ATOM   4579 O  O    . ALA   B 1 39  ? 44.163 -21.460 5.781   1.00 11.81 ?  39  ALA   B O    1 
ATOM   4580 C  CB   . ALA   B 1 39  ? 45.552 -18.843 4.199   1.00 11.40 ?  39  ALA   B CB   1 
ATOM   4581 H  H    . ALA   B 1 39  ? 44.566 -20.704 2.927   1.00 12.57 ?  39  ALA   B H    1 
ATOM   4582 H  HA   . ALA   B 1 39  ? 46.760 -20.483 4.445   1.00 13.21 ?  39  ALA   B HA   1 
ATOM   4583 H  HB1  . ALA   B 1 39  ? 45.916 -18.355 4.954   1.00 13.68 ?  39  ALA   B HB1  1 
ATOM   4584 H  HB2  . ALA   B 1 39  ? 45.984 -18.556 3.379   1.00 13.68 ?  39  ALA   B HB2  1 
ATOM   4585 H  HB3  . ALA   B 1 39  ? 44.594 -18.687 4.137   1.00 13.68 ?  39  ALA   B HB3  1 
ATOM   4586 N  N    . ASN   B 1 40  ? 45.837 -20.367 6.814   1.00 11.18 ?  40  ASN   B N    1 
ATOM   4587 C  CA   . ASN   B 1 40  ? 45.270 -20.405 8.153   1.00 12.23 ?  40  ASN   B CA   1 
ATOM   4588 C  C    . ASN   B 1 40  ? 45.088 -18.977 8.673   1.00 12.01 ?  40  ASN   B C    1 
ATOM   4589 O  O    . ASN   B 1 40  ? 45.496 -17.998 8.039   1.00 11.73 ?  40  ASN   B O    1 
ATOM   4590 C  CB   . ASN   B 1 40  ? 46.117 -21.275 9.097   1.00 13.33 ?  40  ASN   B CB   1 
ATOM   4591 C  CG   . ASN   B 1 40  ? 47.574 -20.871 9.124   1.00 14.20 ?  40  ASN   B CG   1 
ATOM   4592 O  OD1  . ASN   B 1 40  ? 47.901 -19.689 9.192   1.00 16.09 ?  40  ASN   B OD1  1 
ATOM   4593 N  ND2  . ASN   B 1 40  ? 48.459 -21.850 9.073   1.00 14.31 ?  40  ASN   B ND2  1 
ATOM   4594 H  H    . ASN   B 1 40  ? 46.636 -20.053 6.795   1.00 13.42 ?  40  ASN   B H    1 
ATOM   4595 H  HA   . ASN   B 1 40  ? 44.387 -20.800 8.104   1.00 14.68 ?  40  ASN   B HA   1 
ATOM   4596 H  HB2  . ASN   B 1 40  ? 45.763 -21.196 9.997   1.00 15.99 ?  40  ASN   B HB2  1 
ATOM   4597 H  HB3  . ASN   B 1 40  ? 46.063 -22.196 8.800   1.00 15.99 ?  40  ASN   B HB3  1 
ATOM   4598 H  HD21 . ASN   B 1 40  ? 49.298 -21.673 9.087   1.00 17.18 ?  40  ASN   B HD21 1 
ATOM   4599 H  HD22 . ASN   B 1 40  ? 48.192 -22.668 9.022   1.00 17.18 ?  40  ASN   B HD22 1 
ATOM   4600 N  N    . VAL   B 1 41  ? 44.441 -18.852 9.833   1.00 12.50 ?  41  VAL   B N    1 
ATOM   4601 C  CA   . VAL   B 1 41  ? 43.985 -17.531 10.275  1.00 12.85 ?  41  VAL   B CA   1 
ATOM   4602 C  C    . VAL   B 1 41  ? 45.136 -16.577 10.576  1.00 12.80 ?  41  VAL   B C    1 
ATOM   4603 O  O    . VAL   B 1 41  ? 44.953 -15.354 10.497  1.00 13.12 ?  41  VAL   B O    1 
ATOM   4604 C  CB   . VAL   B 1 41  ? 43.003 -17.604 11.461  1.00 14.42 ?  41  VAL   B CB   1 
ATOM   4605 C  CG1  . VAL   B 1 41  ? 41.694 -18.272 11.049  1.00 14.78 ?  41  VAL   B CG1  1 
ATOM   4606 C  CG2  . VAL   B 1 41  ? 43.642 -18.290 12.665  1.00 15.63 ?  41  VAL   B CG2  1 
ATOM   4607 H  H    . VAL   B 1 41  ? 44.256 -19.497 10.363  1.00 15.00 ?  41  VAL   B H    1 
ATOM   4608 H  HA   . VAL   B 1 41  ? 43.491 -17.134 9.545   1.00 15.42 ?  41  VAL   B HA   1 
ATOM   4609 H  HB   . VAL   B 1 41  ? 42.784 -16.700 11.733  1.00 17.31 ?  41  VAL   B HB   1 
ATOM   4610 H  HG11 . VAL   B 1 41  ? 41.083 -18.267 11.805  1.00 17.73 ?  41  VAL   B HG11 1 
ATOM   4611 H  HG12 . VAL   B 1 41  ? 41.306 -17.776 10.311  1.00 17.73 ?  41  VAL   B HG12 1 
ATOM   4612 H  HG13 . VAL   B 1 41  ? 41.875 -19.184 10.778  1.00 17.73 ?  41  VAL   B HG13 1 
ATOM   4613 H  HG21 . VAL   B 1 41  ? 42.997 -18.325 13.389  1.00 18.76 ?  41  VAL   B HG21 1 
ATOM   4614 H  HG22 . VAL   B 1 41  ? 43.906 -19.189 12.415  1.00 18.76 ?  41  VAL   B HG22 1 
ATOM   4615 H  HG23 . VAL   B 1 41  ? 44.420 -17.781 12.941  1.00 18.76 ?  41  VAL   B HG23 1 
ATOM   4616 N  N    . TYR   B 1 42  ? 46.305 -17.093 10.957  1.00 12.93 ?  42  TYR   B N    1 
ATOM   4617 C  CA   . TYR   B 1 42  ? 47.462 -16.249 11.225  1.00 13.30 ?  42  TYR   B CA   1 
ATOM   4618 C  C    . TYR   B 1 42  ? 48.425 -16.177 10.043  1.00 12.77 ?  42  TYR   B C    1 
ATOM   4619 O  O    . TYR   B 1 42  ? 49.514 -15.609 10.177  1.00 13.84 ?  42  TYR   B O    1 
ATOM   4620 C  CB   . TYR   B 1 42  ? 48.155 -16.653 12.534  1.00 15.23 ?  42  TYR   B CB   1 
ATOM   4621 C  CG   . TYR   B 1 42  ? 47.552 -15.962 13.757  1.00 15.76 ?  42  TYR   B CG   1 
ATOM   4622 C  CD1  . TYR   B 1 42  ? 47.762 -14.604 13.979  1.00 15.26 ?  42  TYR   B CD1  1 
ATOM   4623 C  CD2  . TYR   B 1 42  ? 46.769 -16.654 14.671  1.00 17.25 ?  42  TYR   B CD2  1 
ATOM   4624 C  CE1  . TYR   B 1 42  ? 47.218 -13.959 15.074  1.00 16.06 ?  42  TYR   B CE1  1 
ATOM   4625 C  CE2  . TYR   B 1 42  ? 46.225 -16.015 15.778  1.00 17.40 ?  42  TYR   B CE2  1 
ATOM   4626 C  CZ   . TYR   B 1 42  ? 46.451 -14.662 15.971  1.00 17.90 ?  42  TYR   B CZ   1 
ATOM   4627 O  OH   . TYR   B 1 42  ? 45.920 -14.004 17.065  1.00 20.87 ?  42  TYR   B OH   1 
ATOM   4628 H  H    . TYR   B 1 42  ? 46.454 -17.941 11.052  1.00 15.52 ?  42  TYR   B H    1 
ATOM   4629 H  HA   . TYR   B 1 42  ? 47.134 -15.352 11.357  1.00 15.96 ?  42  TYR   B HA   1 
ATOM   4630 H  HB2  . TYR   B 1 42  ? 48.069 -17.611 12.656  1.00 18.28 ?  42  TYR   B HB2  1 
ATOM   4631 H  HB3  . TYR   B 1 42  ? 49.092 -16.407 12.481  1.00 18.28 ?  42  TYR   B HB3  1 
ATOM   4632 H  HD1  . TYR   B 1 42  ? 48.282 -14.121 13.371  1.00 18.31 ?  42  TYR   B HD1  1 
ATOM   4633 H  HD2  . TYR   B 1 42  ? 46.612 -17.564 14.541  1.00 20.70 ?  42  TYR   B HD2  1 
ATOM   4634 H  HE1  . TYR   B 1 42  ? 47.376 -13.052 15.201  1.00 19.28 ?  42  TYR   B HE1  1 
ATOM   4635 H  HE2  . TYR   B 1 42  ? 45.702 -16.495 16.378  1.00 20.88 ?  42  TYR   B HE2  1 
ATOM   4636 H  HH   . TYR   B 1 42  ? 46.143 -13.199 17.042  1.00 25.05 ?  42  TYR   B HH   1 
ATOM   4637 N  N    . LEU   B 1 43  ? 48.023 -16.684 8.879   1.00 11.72 ?  43  LEU   B N    1 
ATOM   4638 C  CA   . LEU   B 1 43  ? 48.836 -16.622 7.666   1.00 11.66 ?  43  LEU   B CA   1 
ATOM   4639 C  C    . LEU   B 1 43  ? 50.248 -17.133 7.926   1.00 11.77 ?  43  LEU   B C    1 
ATOM   4640 O  O    . LEU   B 1 43  ? 51.234 -16.538 7.483   1.00 12.46 ?  43  LEU   B O    1 
ATOM   4641 C  CB   . LEU   B 1 43  ? 48.861 -15.219 7.055   1.00 11.58 ?  43  LEU   B CB   1 
ATOM   4642 C  CG   . LEU   B 1 43  ? 47.501 -14.607 6.698   1.00 12.12 ?  43  LEU   B CG   1 
ATOM   4643 C  CD1  . LEU   B 1 43  ? 47.714 -13.205 6.127   1.00 13.25 ?  43  LEU   B CD1  1 
ATOM   4644 C  CD2  . LEU   B 1 43  ? 46.731 -15.491 5.730   1.00 12.30 ?  43  LEU   B CD2  1 
ATOM   4645 H  H    . LEU   B 1 43  ? 47.274 -17.086 8.761   1.00 14.06 ?  43  LEU   B H    1 
ATOM   4646 H  HA   . LEU   B 1 43  ? 48.441 -17.215 7.005   1.00 13.99 ?  43  LEU   B HA   1 
ATOM   4647 H  HB2  . LEU   B 1 43  ? 49.294 -14.624 7.683   1.00 13.89 ?  43  LEU   B HB2  1 
ATOM   4648 H  HB3  . LEU   B 1 43  ? 49.380 -15.258 6.235   1.00 13.89 ?  43  LEU   B HB3  1 
ATOM   4649 H  HG   . LEU   B 1 43  ? 46.976 -14.518 7.510   1.00 14.54 ?  43  LEU   B HG   1 
ATOM   4650 H  HD11 . LEU   B 1 43  ? 46.851 -12.819 5.907   1.00 15.90 ?  43  LEU   B HD11 1 
ATOM   4651 H  HD12 . LEU   B 1 43  ? 48.160 -12.655 6.792   1.00 15.90 ?  43  LEU   B HD12 1 
ATOM   4652 H  HD13 . LEU   B 1 43  ? 48.262 -13.268 5.330   1.00 15.90 ?  43  LEU   B HD13 1 
ATOM   4653 H  HD21 . LEU   B 1 43  ? 45.928 -15.023 5.447   1.00 14.76 ?  43  LEU   B HD21 1 
ATOM   4654 H  HD22 . LEU   B 1 43  ? 47.291 -15.680 4.962   1.00 14.76 ?  43  LEU   B HD22 1 
ATOM   4655 H  HD23 . LEU   B 1 43  ? 46.491 -16.316 6.178   1.00 14.76 ?  43  LEU   B HD23 1 
ATOM   4656 N  N    . LYS   B 1 44  ? 50.343 -18.251 8.647   1.00 11.76 ?  44  LYS   B N    1 
ATOM   4657 C  CA   . LYS   B 1 44  ? 51.609 -18.932 8.888   1.00 12.67 ?  44  LYS   B CA   1 
ATOM   4658 C  C    . LYS   B 1 44  ? 51.725 -20.050 7.861   1.00 12.25 ?  44  LYS   B C    1 
ATOM   4659 O  O    . LYS   B 1 44  ? 51.032 -21.068 7.954   1.00 13.48 ?  44  LYS   B O    1 
ATOM   4660 C  CB   . LYS   B 1 44  ? 51.671 -19.454 10.322  1.00 14.44 ?  44  LYS   B CB   1 
ATOM   4661 C  CG   . LYS   B 1 44  ? 51.868 -18.345 11.348  1.00 17.24 ?  44  LYS   B CG   1 
ATOM   4662 C  CD   . LYS   B 1 44  ? 53.076 -17.487 10.948  1.00 20.29 ?  44  LYS   B CD   1 
ATOM   4663 C  CE   . LYS   B 1 44  ? 53.525 -16.542 12.027  1.00 23.22 ?  44  LYS   B CE   1 
ATOM   4664 N  NZ   . LYS   B 1 44  ? 54.742 -15.783 11.648  1.00 24.71 ?  44  LYS   B NZ   1 
ATOM   4665 H  H    . LYS   B 1 44  ? 49.669 -18.636 9.014   1.00 14.11 ?  44  LYS   B H    1 
ATOM   4666 H  HA   . LYS   B 1 44  ? 52.343 -18.321 8.722   1.00 15.21 ?  44  LYS   B HA   1 
ATOM   4667 H  HB2  . LYS   B 1 44  ? 50.833 -19.903 10.531  1.00 17.33 ?  44  LYS   B HB2  1 
ATOM   4668 H  HB3  . LYS   B 1 44  ? 52.408 -20.073 10.406  1.00 17.33 ?  44  LYS   B HB3  1 
ATOM   4669 H  HG2  . LYS   B 1 44  ? 51.080 -17.784 11.380  1.00 20.68 ?  44  LYS   B HG2  1 
ATOM   4670 H  HG3  . LYS   B 1 44  ? 52.043 -18.739 12.221  1.00 20.68 ?  44  LYS   B HG3  1 
ATOM   4671 H  HD2  . LYS   B 1 44  ? 53.814 -18.079 10.714  1.00 24.35 ?  44  LYS   B HD2  1 
ATOM   4672 H  HD3  . LYS   B 1 44  ? 52.831 -16.947 10.180  1.00 24.35 ?  44  LYS   B HD3  1 
ATOM   4673 H  HE2  . LYS   B 1 44  ? 52.819 -15.899 12.171  1.00 27.86 ?  44  LYS   B HE2  1 
ATOM   4674 H  HE3  . LYS   B 1 44  ? 53.710 -17.044 12.836  1.00 27.86 ?  44  LYS   B HE3  1 
ATOM   4675 H  HZ1  . LYS   B 1 44  ? 54.971 -15.230 12.306  1.00 29.65 ?  44  LYS   B HZ1  1 
ATOM   4676 H  HZ2  . LYS   B 1 44  ? 55.416 -16.340 11.488  1.00 29.65 ?  44  LYS   B HZ2  1 
ATOM   4677 H  HZ3  . LYS   B 1 44  ? 54.585 -15.303 10.912  1.00 29.65 ?  44  LYS   B HZ3  1 
ATOM   4678 N  N    . HIS   B 1 45  ? 52.585 -19.839 6.866   1.00 11.91 ?  45  HIS   B N    1 
ATOM   4679 C  CA   . HIS   B 1 45  ? 52.612 -20.670 5.663   1.00 11.94 ?  45  HIS   B CA   1 
ATOM   4680 C  C    . HIS   B 1 45  ? 53.629 -21.797 5.828   1.00 14.03 ?  45  HIS   B C    1 
ATOM   4681 O  O    . HIS   B 1 45  ? 54.689 -21.821 5.211   1.00 16.63 ?  45  HIS   B O    1 
ATOM   4682 C  CB   . HIS   B 1 45  ? 52.932 -19.818 4.448   1.00 11.93 ?  45  HIS   B CB   1 
ATOM   4683 C  CG   . HIS   B 1 45  ? 52.064 -18.614 4.330   1.00 11.82 ?  45  HIS   B CG   1 
ATOM   4684 N  ND1  . HIS   B 1 45  ? 50.687 -18.691 4.294   1.00 11.96 ?  45  HIS   B ND1  1 
ATOM   4685 C  CD2  . HIS   B 1 45  ? 52.383 -17.302 4.252   1.00 12.36 ?  45  HIS   B CD2  1 
ATOM   4686 C  CE1  . HIS   B 1 45  ? 50.201 -17.465 4.190   1.00 11.66 ?  45  HIS   B CE1  1 
ATOM   4687 N  NE2  . HIS   B 1 45  ? 51.206 -16.606 4.159   1.00 12.04 ?  45  HIS   B NE2  1 
ATOM   4688 H  H    . HIS   B 1 45  ? 53.159 -19.200 6.859   1.00 14.30 ?  45  HIS   B H    1 
ATOM   4689 H  HA   . HIS   B 1 45  ? 51.731 -21.066 5.530   1.00 14.33 ?  45  HIS   B HA   1 
ATOM   4690 H  HB2  . HIS   B 1 45  ? 53.851 -19.522 4.506   1.00 14.32 ?  45  HIS   B HB2  1 
ATOM   4691 H  HB3  . HIS   B 1 45  ? 52.809 -20.358 3.647   1.00 14.32 ?  45  HIS   B HB3  1 
ATOM   4692 H  HD2  . HIS   B 1 45  ? 53.239 -16.941 4.258   1.00 14.83 ?  45  HIS   B HD2  1 
ATOM   4693 H  HE1  . HIS   B 1 45  ? 49.299 -17.242 4.135   1.00 13.99 ?  45  HIS   B HE1  1 
ATOM   4694 H  HE2  . HIS   B 1 45  ? 51.132 -15.750 4.100   1.00 14.45 ?  45  HIS   B HE2  1 
ATOM   4695 N  N    A GLY   B 1 46  ? 53.257 -22.766 6.660   0.64 14.94 ?  46  GLY   B N    1 
ATOM   4696 N  N    B GLY   B 1 46  ? 53.270 -22.747 6.681   0.36 14.87 ?  46  GLY   B N    1 
ATOM   4697 C  CA   A GLY   B 1 46  ? 54.181 -23.814 7.054   0.64 16.65 ?  46  GLY   B CA   1 
ATOM   4698 C  CA   B GLY   B 1 46  ? 54.188 -23.813 7.022   0.36 16.04 ?  46  GLY   B CA   1 
ATOM   4699 C  C    A GLY   B 1 46  ? 54.240 -25.050 6.177   0.64 18.08 ?  46  GLY   B C    1 
ATOM   4700 C  C    B GLY   B 1 46  ? 54.222 -24.951 6.021   0.36 17.16 ?  46  GLY   B C    1 
ATOM   4701 O  O    A GLY   B 1 46  ? 55.331 -25.507 5.821   0.64 20.72 ?  46  GLY   B O    1 
ATOM   4702 O  O    B GLY   B 1 46  ? 55.253 -25.211 5.394   0.36 17.99 ?  46  GLY   B O    1 
ATOM   4703 H  H    A GLY   B 1 46  ? 52.476 -22.823 7.024   0.64 17.93 ?  46  GLY   B H    1 
ATOM   4704 H  H    B GLY   B 1 46  ? 52.502 -22.789 7.077   0.36 17.84 ?  46  GLY   B H    1 
ATOM   4705 H  HA2  A GLY   B 1 46  ? 55.072 -23.437 7.095   0.64 19.98 ?  46  GLY   B HA2  1 
ATOM   4706 H  HA2  B GLY   B 1 46  ? 55.081 -23.444 7.090   0.36 19.25 ?  46  GLY   B HA2  1 
ATOM   4707 H  HA3  A GLY   B 1 46  ? 53.944 -24.114 7.944   0.64 19.98 ?  46  GLY   B HA3  1 
ATOM   4708 H  HA3  B GLY   B 1 46  ? 53.943 -24.168 7.892   0.36 19.25 ?  46  GLY   B HA3  1 
ATOM   4709 N  N    . GLY   B 1 47  ? 53.087 -25.625 5.842   1.00 17.70 ?  47  GLY   B N    1 
ATOM   4710 C  CA   . GLY   B 1 47  ? 53.039 -26.891 5.139   1.00 15.69 ?  47  GLY   B CA   1 
ATOM   4711 C  C    . GLY   B 1 47  ? 52.115 -26.871 3.937   1.00 13.71 ?  47  GLY   B C    1 
ATOM   4712 O  O    . GLY   B 1 47  ? 51.459 -25.870 3.646   1.00 13.64 ?  47  GLY   B O    1 
ATOM   4713 H  H    A GLY   B 1 47  ? 52.310 -25.308 6.037   0.64 21.24 ?  47  GLY   B H    1 
ATOM   4714 H  H    B GLY   B 1 47  ? 52.316 -25.356 6.120   0.36 21.24 ?  47  GLY   B H    1 
ATOM   4715 H  HA2  . GLY   B 1 47  ? 53.926 -27.132 4.834   1.00 18.83 ?  47  GLY   B HA2  1 
ATOM   4716 H  HA3  . GLY   B 1 47  ? 52.731 -27.582 5.748   1.00 18.83 ?  47  GLY   B HA3  1 
ATOM   4717 N  N    . GLY   B 1 48  ? 52.069 -28.010 3.250   1.00 13.18 ?  48  GLY   B N    1 
ATOM   4718 C  CA   . GLY   B 1 48  ? 51.148 -28.163 2.141   1.00 12.84 ?  48  GLY   B CA   1 
ATOM   4719 C  C    . GLY   B 1 48  ? 51.283 -27.053 1.125   1.00 12.11 ?  48  GLY   B C    1 
ATOM   4720 O  O    . GLY   B 1 48  ? 52.387 -26.591 0.809   1.00 12.84 ?  48  GLY   B O    1 
ATOM   4721 H  H    . GLY   B 1 48  ? 52.560 -28.695 3.402   1.00 15.82 ?  48  GLY   B H    1 
ATOM   4722 H  HA2  . GLY   B 1 48  ? 51.311 -29.013 1.695   1.00 15.41 ?  48  GLY   B HA2  1 
ATOM   4723 H  HA3  . GLY   B 1 48  ? 50.234 -28.167 2.471   1.00 15.41 ?  48  GLY   B HA3  1 
ATOM   4724 N  N    . VAL   B 1 49  ? 50.137 -26.628 0.592   1.00 12.00 ?  49  VAL   B N    1 
ATOM   4725 C  CA   . VAL   B 1 49  ? 50.119 -25.607 -0.452  1.00 12.01 ?  49  VAL   B CA   1 
ATOM   4726 C  C    . VAL   B 1 49  ? 50.778 -24.319 0.032   1.00 11.23 ?  49  VAL   B C    1 
ATOM   4727 O  O    . VAL   B 1 49  ? 51.565 -23.698 -0.691  1.00 12.02 ?  49  VAL   B O    1 
ATOM   4728 C  CB   . VAL   B 1 49  ? 48.676 -25.353 -0.928  1.00 13.14 ?  49  VAL   B CB   1 
ATOM   4729 C  CG1  . VAL   B 1 49  ? 48.605 -24.118 -1.815  1.00 13.09 ?  49  VAL   B CG1  1 
ATOM   4730 C  CG2  . VAL   B 1 49  ? 48.130 -26.573 -1.668  1.00 15.07 ?  49  VAL   B CG2  1 
ATOM   4731 H  H    . VAL   B 1 49  ? 49.349 -26.913 0.817   1.00 14.40 ?  49  VAL   B H    1 
ATOM   4732 H  HA   . VAL   B 1 49  ? 50.621 -25.930 -1.212  1.00 14.41 ?  49  VAL   B HA   1 
ATOM   4733 H  HB   . VAL   B 1 49  ? 48.107 -25.198 -0.159  1.00 15.77 ?  49  VAL   B HB   1 
ATOM   4734 H  HG11 . VAL   B 1 49  ? 47.773 -24.133 -2.316  1.00 15.70 ?  49  VAL   B HG11 1 
ATOM   4735 H  HG12 . VAL   B 1 49  ? 48.636 -23.323 -1.258  1.00 15.70 ?  49  VAL   B HG12 1 
ATOM   4736 H  HG13 . VAL   B 1 49  ? 49.356 -24.124 -2.428  1.00 15.70 ?  49  VAL   B HG13 1 
ATOM   4737 H  HG21 . VAL   B 1 49  ? 47.222 -26.391 -1.959  1.00 18.08 ?  49  VAL   B HG21 1 
ATOM   4738 H  HG22 . VAL   B 1 49  ? 48.692 -26.751 -2.441  1.00 18.08 ?  49  VAL   B HG22 1 
ATOM   4739 H  HG23 . VAL   B 1 49  ? 48.140 -27.336 -1.071  1.00 18.08 ?  49  VAL   B HG23 1 
ATOM   4740 N  N    . ALA   B 1 50  ? 50.435 -23.870 1.241   1.00 11.20 ?  50  ALA   B N    1 
ATOM   4741 C  CA   . ALA   B 1 50  ? 50.957 -22.590 1.712   1.00 11.00 ?  50  ALA   B CA   1 
ATOM   4742 C  C    . ALA   B 1 50  ? 52.477 -22.621 1.825   1.00 11.41 ?  50  ALA   B C    1 
ATOM   4743 O  O    . ALA   B 1 50  ? 53.158 -21.655 1.458   1.00 11.23 ?  50  ALA   B O    1 
ATOM   4744 C  CB   . ALA   B 1 50  ? 50.325 -22.221 3.051   1.00 11.24 ?  50  ALA   B CB   1 
ATOM   4745 H  H    . ALA   B 1 50  ? 49.915 -24.275 1.793   1.00 13.44 ?  50  ALA   B H    1 
ATOM   4746 H  HA   . ALA   B 1 50  ? 50.726 -21.902 1.073   1.00 13.20 ?  50  ALA   B HA   1 
ATOM   4747 H  HB1  . ALA   B 1 50  ? 50.682 -21.367 3.344   1.00 13.49 ?  50  ALA   B HB1  1 
ATOM   4748 H  HB2  . ALA   B 1 50  ? 49.362 -22.151 2.936   1.00 13.49 ?  50  ALA   B HB2  1 
ATOM   4749 H  HB3  . ALA   B 1 50  ? 50.531 -22.908 3.701   1.00 13.49 ?  50  ALA   B HB3  1 
ATOM   4750 N  N    . GLY   B 1 51  ? 53.026 -23.713 2.345   1.00 11.92 ?  51  GLY   B N    1 
ATOM   4751 C  CA   . GLY   B 1 51  ? 54.470 -23.817 2.421   1.00 12.33 ?  51  GLY   B CA   1 
ATOM   4752 C  C    . GLY   B 1 51  ? 55.120 -23.777 1.055   1.00 12.30 ?  51  GLY   B C    1 
ATOM   4753 O  O    . GLY   B 1 51  ? 56.162 -23.143 0.872   1.00 13.22 ?  51  GLY   B O    1 
ATOM   4754 H  H    . GLY   B 1 51  ? 52.594 -24.393 2.651   1.00 14.30 ?  51  GLY   B H    1 
ATOM   4755 H  HA2  . GLY   B 1 51  ? 54.820 -23.081 2.950   1.00 14.80 ?  51  GLY   B HA2  1 
ATOM   4756 H  HA3  . GLY   B 1 51  ? 54.714 -24.650 2.854   1.00 14.80 ?  51  GLY   B HA3  1 
ATOM   4757 N  N    . ALA   B 1 52  ? 54.512 -24.441 0.073   1.00 12.10 ?  52  ALA   B N    1 
ATOM   4758 C  CA   . ALA   B 1 52  ? 55.075 -24.448 -1.272  1.00 12.50 ?  52  ALA   B CA   1 
ATOM   4759 C  C    . ALA   B 1 52  ? 54.994 -23.068 -1.921  1.00 11.72 ?  52  ALA   B C    1 
ATOM   4760 O  O    . ALA   B 1 52  ? 55.963 -22.615 -2.552  1.00 12.68 ?  52  ALA   B O    1 
ATOM   4761 C  CB   . ALA   B 1 52  ? 54.371 -25.491 -2.132  1.00 13.25 ?  52  ALA   B CB   1 
ATOM   4762 H  H    . ALA   B 1 52  ? 53.775 -24.881 0.159   1.00 14.51 ?  52  ALA   B H    1 
ATOM   4763 H  HA   . ALA   B 1 52  ? 56.007 -24.690 -1.212  1.00 15.00 ?  52  ALA   B HA   1 
ATOM   4764 H  HB1  . ALA   B 1 52  ? 54.766 -25.481 -3.020  1.00 15.91 ?  52  ALA   B HB1  1 
ATOM   4765 H  HB2  . ALA   B 1 52  ? 54.497 -26.366 -1.728  1.00 15.91 ?  52  ALA   B HB2  1 
ATOM   4766 H  HB3  . ALA   B 1 52  ? 53.430 -25.281 -2.184  1.00 15.91 ?  52  ALA   B HB3  1 
ATOM   4767 N  N    . LEU   B 1 53  ? 53.846 -22.390 -1.807  1.00 11.27 ?  53  LEU   B N    1 
ATOM   4768 C  CA   . LEU   B 1 53  ? 53.735 -21.050 -2.380  1.00 11.40 ?  53  LEU   B CA   1 
ATOM   4769 C  C    . LEU   B 1 53  ? 54.745 -20.109 -1.737  1.00 11.40 ?  53  LEU   B C    1 
ATOM   4770 O  O    . LEU   B 1 53  ? 55.448 -19.360 -2.427  1.00 12.00 ?  53  LEU   B O    1 
ATOM   4771 C  CB   . LEU   B 1 53  ? 52.316 -20.503 -2.211  1.00 12.00 ?  53  LEU   B CB   1 
ATOM   4772 C  CG   . LEU   B 1 53  ? 51.172 -21.225 -2.928  1.00 12.18 ?  53  LEU   B CG   1 
ATOM   4773 C  CD1  . LEU   B 1 53  ? 49.837 -20.601 -2.569  1.00 13.58 ?  53  LEU   B CD1  1 
ATOM   4774 C  CD2  . LEU   B 1 53  ? 51.366 -21.245 -4.441  1.00 14.27 ?  53  LEU   B CD2  1 
ATOM   4775 H  H    . LEU   B 1 53  ? 53.137 -22.673 -1.410  1.00 13.52 ?  53  LEU   B H    1 
ATOM   4776 H  HA   . LEU   B 1 53  ? 53.932 -21.099 -3.332  1.00 13.68 ?  53  LEU   B HA   1 
ATOM   4777 H  HB2  . LEU   B 1 53  ? 52.108 -20.512 -1.266  1.00 14.39 ?  53  LEU   B HB2  1 
ATOM   4778 H  HB3  . LEU   B 1 53  ? 52.314 -19.587 -2.529  1.00 14.39 ?  53  LEU   B HB3  1 
ATOM   4779 H  HG   . LEU   B 1 53  ? 51.148 -22.143 -2.625  1.00 14.62 ?  53  LEU   B HG   1 
ATOM   4780 H  HD11 . LEU   B 1 53  ? 49.128 -21.080 -3.030  1.00 16.29 ?  53  LEU   B HD11 1 
ATOM   4781 H  HD12 . LEU   B 1 53  ? 49.703 -20.671 -1.607  1.00 16.29 ?  53  LEU   B HD12 1 
ATOM   4782 H  HD13 . LEU   B 1 53  ? 49.835 -19.671 -2.835  1.00 16.29 ?  53  LEU   B HD13 1 
ATOM   4783 H  HD21 . LEU   B 1 53  ? 50.644 -21.755 -4.843  1.00 17.13 ?  53  LEU   B HD21 1 
ATOM   4784 H  HD22 . LEU   B 1 53  ? 51.349 -20.335 -4.773  1.00 17.13 ?  53  LEU   B HD22 1 
ATOM   4785 H  HD23 . LEU   B 1 53  ? 52.216 -21.660 -4.644  1.00 17.13 ?  53  LEU   B HD23 1 
ATOM   4786 N  N    . ASN   B 1 54  ? 54.839 -20.138 -0.410  1.00 11.03 ?  54  ASN   B N    1 
ATOM   4787 C  CA   . ASN   B 1 54  ? 55.750 -19.222 0.261   1.00 11.85 ?  54  ASN   B CA   1 
ATOM   4788 C  C    . ASN   B 1 54  ? 57.196 -19.500 -0.129  1.00 12.16 ?  54  ASN   B C    1 
ATOM   4789 O  O    . ASN   B 1 54  ? 57.974 -18.564 -0.356  1.00 12.60 ?  54  ASN   B O    1 
ATOM   4790 C  CB   . ASN   B 1 54  ? 55.589 -19.297 1.773   1.00 12.65 ?  54  ASN   B CB   1 
ATOM   4791 C  CG   . ASN   B 1 54  ? 56.570 -18.386 2.485   1.00 12.65 ?  54  ASN   B CG   1 
ATOM   4792 O  OD1  . ASN   B 1 54  ? 56.591 -17.174 2.249   1.00 13.02 ?  54  ASN   B OD1  1 
ATOM   4793 N  ND2  . ASN   B 1 54  ? 57.411 -18.963 3.334   1.00 14.14 ?  54  ASN   B ND2  1 
ATOM   4794 H  H    . ASN   B 1 54  ? 54.398 -20.664 0.107   1.00 13.24 ?  54  ASN   B H    1 
ATOM   4795 H  HA   . ASN   B 1 54  ? 55.537 -18.318 -0.016  1.00 14.22 ?  54  ASN   B HA   1 
ATOM   4796 H  HB2  . ASN   B 1 54  ? 54.688 -19.021 2.012   1.00 15.18 ?  54  ASN   B HB2  1 
ATOM   4797 H  HB3  . ASN   B 1 54  ? 55.748 -20.207 2.069   1.00 15.18 ?  54  ASN   B HB3  1 
ATOM   4798 H  HD21 . ASN   B 1 54  ? 57.992 -18.489 3.757   1.00 16.97 ?  54  ASN   B HD21 1 
ATOM   4799 H  HD22 . ASN   B 1 54  ? 57.377 -19.814 3.467   1.00 16.97 ?  54  ASN   B HD22 1 
ATOM   4800 N  N    . LYS   B 1 55  ? 57.582 -20.778 -0.189  1.00 12.60 ?  55  LYS   B N    1 
ATOM   4801 C  CA   . LYS   B 1 55  ? 58.937 -21.124 -0.606  1.00 13.45 ?  55  LYS   B CA   1 
ATOM   4802 C  C    . LYS   B 1 55  ? 59.237 -20.584 -1.998  1.00 13.47 ?  55  LYS   B C    1 
ATOM   4803 O  O    . LYS   B 1 55  ? 60.337 -20.078 -2.250  1.00 14.25 ?  55  LYS   B O    1 
ATOM   4804 C  CB   . LYS   B 1 55  ? 59.128 -22.643 -0.555  1.00 15.34 ?  55  LYS   B CB   1 
ATOM   4805 C  CG   . LYS   B 1 55  ? 60.492 -23.121 -1.020  1.00 19.47 ?  55  LYS   B CG   1 
ATOM   4806 C  CD   . LYS   B 1 55  ? 60.656 -24.621 -0.828  1.00 22.96 ?  55  LYS   B CD   1 
ATOM   4807 C  CE   . LYS   B 1 55  ? 60.720 -24.997 0.649   1.00 26.04 ?  55  LYS   B CE   1 
ATOM   4808 N  NZ   . LYS   B 1 55  ? 61.133 -26.408 0.848   1.00 27.81 ?  55  LYS   B NZ   1 
ATOM   4809 H  H    . LYS   B 1 55  ? 57.079 -21.451 -0.000  1.00 15.12 ?  55  LYS   B H    1 
ATOM   4810 H  HA   . LYS   B 1 55  ? 59.565 -20.722 0.011   1.00 16.14 ?  55  LYS   B HA   1 
ATOM   4811 H  HB2  . LYS   B 1 55  ? 59.006 -22.934 0.364   1.00 18.41 ?  55  LYS   B HB2  1 
ATOM   4812 H  HB3  . LYS   B 1 55  ? 58.459 -23.061 -1.119  1.00 18.41 ?  55  LYS   B HB3  1 
ATOM   4813 H  HG2  . LYS   B 1 55  ? 60.593 -22.924 -1.964  1.00 23.37 ?  55  LYS   B HG2  1 
ATOM   4814 H  HG3  . LYS   B 1 55  ? 61.179 -22.669 -0.507  1.00 23.37 ?  55  LYS   B HG3  1 
ATOM   4815 H  HD2  . LYS   B 1 55  ? 59.899 -25.082 -1.224  1.00 27.55 ?  55  LYS   B HD2  1 
ATOM   4816 H  HD3  . LYS   B 1 55  ? 61.482 -24.911 -1.248  1.00 27.55 ?  55  LYS   B HD3  1 
ATOM   4817 H  HE2  . LYS   B 1 55  ? 61.364 -24.419 1.093   1.00 31.25 ?  55  LYS   B HE2  1 
ATOM   4818 H  HE3  . LYS   B 1 55  ? 59.840 -24.875 1.044   1.00 31.25 ?  55  LYS   B HE3  1 
ATOM   4819 H  HZ1  . LYS   B 1 55  ? 61.137 -26.600 1.717   1.00 33.37 ?  55  LYS   B HZ1  1 
ATOM   4820 H  HZ2  . LYS   B 1 55  ? 60.562 -26.949 0.434   1.00 33.37 ?  55  LYS   B HZ2  1 
ATOM   4821 H  HZ3  . LYS   B 1 55  ? 61.947 -26.533 0.518   1.00 33.37 ?  55  LYS   B HZ3  1 
ATOM   4822 N  N    . ALA   B 1 56  ? 58.268 -20.672 -2.915  1.00 13.00 ?  56  ALA   B N    1 
ATOM   4823 C  CA   . ALA   B 1 56  ? 58.492 -20.175 -4.266  1.00 13.82 ?  56  ALA   B CA   1 
ATOM   4824 C  C    . ALA   B 1 56  ? 58.766 -18.679 -4.271  1.00 13.66 ?  56  ALA   B C    1 
ATOM   4825 O  O    . ALA   B 1 56  ? 59.490 -18.185 -5.146  1.00 14.77 ?  56  ALA   B O    1 
ATOM   4826 C  CB   . ALA   B 1 56  ? 57.294 -20.505 -5.156  1.00 14.61 ?  56  ALA   B CB   1 
ATOM   4827 H  H    . ALA   B 1 56  ? 57.480 -20.996 -2.779  1.00 15.60 ?  56  ALA   B H    1 
ATOM   4828 H  HA   . ALA   B 1 56  ? 59.266 -20.614 -4.639  1.00 16.59 ?  56  ALA   B HA   1 
ATOM   4829 H  HB1  . ALA   B 1 56  ? 57.463 -20.169 -6.053  1.00 17.53 ?  56  ALA   B HB1  1 
ATOM   4830 H  HB2  . ALA   B 1 56  ? 57.179 -21.468 -5.183  1.00 17.53 ?  56  ALA   B HB2  1 
ATOM   4831 H  HB3  . ALA   B 1 56  ? 56.500 -20.086 -4.793  1.00 17.53 ?  56  ALA   B HB3  1 
ATOM   4832 N  N    . THR   B 1 57  ? 58.203 -17.940 -3.312  1.00 13.30 ?  57  THR   B N    1 
ATOM   4833 C  CA   . THR   B 1 57  ? 58.440 -16.504 -3.196  1.00 13.30 ?  57  THR   B CA   1 
ATOM   4834 C  C    . THR   B 1 57  ? 59.686 -16.177 -2.381  1.00 13.91 ?  57  THR   B C    1 
ATOM   4835 O  O    . THR   B 1 57  ? 59.925 -15.002 -2.079  1.00 14.42 ?  57  THR   B O    1 
ATOM   4836 C  CB   . THR   B 1 57  ? 57.238 -15.771 -2.568  1.00 12.85 ?  57  THR   B CB   1 
ATOM   4837 O  OG1  . THR   B 1 57  ? 57.216 -15.981 -1.149  1.00 13.14 ?  57  THR   B OG1  1 
ATOM   4838 C  CG2  . THR   B 1 57  ? 55.919 -16.200 -3.205  1.00 13.02 ?  57  THR   B CG2  1 
ATOM   4839 H  H    . THR   B 1 57  ? 57.665 -18.249 -2.716  1.00 15.96 ?  57  THR   B H    1 
ATOM   4840 H  HA   . THR   B 1 57  ? 58.566 -16.139 -4.087  1.00 15.96 ?  57  THR   B HA   1 
ATOM   4841 H  HB   . THR   B 1 57  ? 57.338 -14.820 -2.737  1.00 15.42 ?  57  THR   B HB   1 
ATOM   4842 H  HG1  . THR   B 1 57  ? 57.146 -16.805 -0.987  1.00 15.77 ?  57  THR   B HG1  1 
ATOM   4843 H  HG21 . THR   B 1 57  ? 55.194 -15.656 -2.869  1.00 15.62 ?  57  THR   B HG21 1 
ATOM   4844 H  HG22 . THR   B 1 57  ? 55.968 -16.104 -4.170  1.00 15.62 ?  57  THR   B HG22 1 
ATOM   4845 H  HG23 . THR   B 1 57  ? 55.738 -17.131 -2.995  1.00 15.62 ?  57  THR   B HG23 1 
ATOM   4846 N  N    . ASN   B 1 58  ? 60.480 -17.180 -2.018  1.00 14.82 ?  58  ASN   B N    1 
ATOM   4847 C  CA   . ASN   B 1 58  ? 61.677 -16.965 -1.209  1.00 17.63 ?  58  ASN   B CA   1 
ATOM   4848 C  C    . ASN   B 1 58  ? 61.343 -16.251 0.101   1.00 15.55 ?  58  ASN   B C    1 
ATOM   4849 O  O    . ASN   B 1 58  ? 62.086 -15.381 0.569   1.00 16.24 ?  58  ASN   B O    1 
ATOM   4850 C  CB   . ASN   B 1 58  ? 62.769 -16.223 -1.987  1.00 24.84 ?  58  ASN   B CB   1 
ATOM   4851 C  CG   . ASN   B 1 58  ? 64.140 -16.381 -1.355  1.00 33.08 ?  58  ASN   B CG   1 
ATOM   4852 O  OD1  . ASN   B 1 58  ? 64.431 -17.397 -0.726  1.00 36.03 ?  58  ASN   B OD1  1 
ATOM   4853 N  ND2  . ASN   B 1 58  ? 64.987 -15.371 -1.518  1.00 38.99 ?  58  ASN   B ND2  1 
ATOM   4854 H  H    . ASN   B 1 58  ? 60.348 -18.004 -2.231  1.00 17.79 ?  58  ASN   B H    1 
ATOM   4855 H  HA   . ASN   B 1 58  ? 62.038 -17.838 -0.985  1.00 21.16 ?  58  ASN   B HA   1 
ATOM   4856 H  HB2  . ASN   B 1 58  ? 62.814 -16.575 -2.892  1.00 29.81 ?  58  ASN   B HB2  1 
ATOM   4857 H  HB3  . ASN   B 1 58  ? 62.559 -15.278 -2.009  1.00 29.81 ?  58  ASN   B HB3  1 
ATOM   4858 H  HD21 . ASN   B 1 58  ? 65.777 -15.413 -1.179  1.00 46.79 ?  58  ASN   B HD21 1 
ATOM   4859 H  HD22 . ASN   B 1 58  ? 64.747 -14.675 -1.962  1.00 46.79 ?  58  ASN   B HD22 1 
ATOM   4860 N  N    . ASN   B 1 59  ? 60.216 -16.629 0.702   1.00 14.58 ?  59  ASN   B N    1 
ATOM   4861 C  CA   . ASN   B 1 59  ? 59.741 -16.152 2.000   1.00 14.29 ?  59  ASN   B CA   1 
ATOM   4862 C  C    . ASN   B 1 59  ? 59.144 -14.747 1.942   1.00 13.86 ?  59  ASN   B C    1 
ATOM   4863 O  O    . ASN   B 1 59  ? 58.713 -14.239 2.985   1.00 14.12 ?  59  ASN   B O    1 
ATOM   4864 C  CB   . ASN   B 1 59  ? 60.812 -16.210 3.104   1.00 15.34 ?  59  ASN   B CB   1 
ATOM   4865 C  CG   . ASN   B 1 59  ? 60.221 -16.377 4.484   1.00 16.42 ?  59  ASN   B CG   1 
ATOM   4866 O  OD1  . ASN   B 1 59  ? 59.397 -17.263 4.717   1.00 16.99 ?  59  ASN   B OD1  1 
ATOM   4867 N  ND2  . ASN   B 1 59  ? 60.640 -15.527 5.413   1.00 17.29 ?  59  ASN   B ND2  1 
ATOM   4868 H  H    . ASN   B 1 59  ? 59.676 -17.211 0.358   1.00 17.49 ?  59  ASN   B H    1 
ATOM   4869 H  HA   . ASN   B 1 59  ? 59.032 -16.746 2.283   1.00 17.15 ?  59  ASN   B HA   1 
ATOM   4870 H  HB2  . ASN   B 1 59  ? 61.401 -16.965 2.943   1.00 18.41 ?  59  ASN   B HB2  1 
ATOM   4871 H  HB3  . ASN   B 1 59  ? 61.320 -15.386 3.102   1.00 18.41 ?  59  ASN   B HB3  1 
ATOM   4872 H  HD21 . ASN   B 1 59  ? 60.332 -15.580 6.216   1.00 20.75 ?  59  ASN   B HD21 1 
ATOM   4873 H  HD22 . ASN   B 1 59  ? 61.212 -14.919 5.212   1.00 20.75 ?  59  ASN   B HD22 1 
ATOM   4874 N  N    . ALA   B 1 60  ? 59.078 -14.109 0.769   1.00 13.61 ?  60  ALA   B N    1 
ATOM   4875 C  CA   . ALA   B 1 60  ? 58.485 -12.777 0.687   1.00 13.60 ?  60  ALA   B CA   1 
ATOM   4876 C  C    . ALA   B 1 60  ? 57.016 -12.803 1.086   1.00 12.59 ?  60  ALA   B C    1 
ATOM   4877 O  O    . ALA   B 1 60  ? 56.512 -11.853 1.698   1.00 13.31 ?  60  ALA   B O    1 
ATOM   4878 C  CB   . ALA   B 1 60  ? 58.642 -12.211 -0.725  1.00 14.42 ?  60  ALA   B CB   1 
ATOM   4879 H  H    . ALA   B 1 60  ? 59.369 -14.425 0.022   1.00 16.33 ?  60  ALA   B H    1 
ATOM   4880 H  HA   . ALA   B 1 60  ? 58.948 -12.191 1.299   1.00 16.32 ?  60  ALA   B HA   1 
ATOM   4881 H  HB1  . ALA   B 1 60  ? 58.243 -11.330 -0.757  1.00 17.31 ?  60  ALA   B HB1  1 
ATOM   4882 H  HB2  . ALA   B 1 60  ? 59.589 -12.155 -0.939  1.00 17.31 ?  60  ALA   B HB2  1 
ATOM   4883 H  HB3  . ALA   B 1 60  ? 58.199 -12.802 -1.355  1.00 17.31 ?  60  ALA   B HB3  1 
ATOM   4884 N  N    . MET   B 1 61  ? 56.311 -13.881 0.743   1.00 12.08 ?  61  MET   B N    1 
ATOM   4885 C  CA   . MET   B 1 61  ? 54.913 -13.998 1.134   1.00 11.82 ?  61  MET   B CA   1 
ATOM   4886 C  C    . MET   B 1 61  ? 54.770 -14.002 2.657   1.00 12.09 ?  61  MET   B C    1 
ATOM   4887 O  O    . MET   B 1 61  ? 53.867 -13.355 3.208   1.00 11.75 ?  61  MET   B O    1 
ATOM   4888 C  CB   . MET   B 1 61  ? 54.337 -15.267 0.505   1.00 11.82 ?  61  MET   B CB   1 
ATOM   4889 C  CG   . MET   B 1 61  ? 52.899 -15.563 0.928   1.00 11.53 ?  61  MET   B CG   1 
ATOM   4890 S  SD   . MET   B 1 61  ? 52.243 -17.065 0.165   1.00 12.09 ?  61  MET   B SD   1 
ATOM   4891 C  CE   . MET   B 1 61  ? 51.982 -16.482 -1.508  1.00 13.10 ?  61  MET   B CE   1 
ATOM   4892 H  H    . MET   B 1 61  ? 56.617 -14.556 0.292   1.00 14.50 ?  61  MET   B H    1 
ATOM   4893 H  HA   . MET   B 1 61  ? 54.423 -13.247 0.768   1.00 14.19 ?  61  MET   B HA   1 
ATOM   4894 H  HB2  . MET   B 1 61  ? 54.342 -15.174 -0.465  1.00 14.18 ?  61  MET   B HB2  1 
ATOM   4895 H  HB3  . MET   B 1 61  ? 54.884 -16.026 0.760   1.00 14.18 ?  61  MET   B HB3  1 
ATOM   4896 H  HG2  . MET   B 1 61  ? 52.869 -15.690 1.892   1.00 13.84 ?  61  MET   B HG2  1 
ATOM   4897 H  HG3  . MET   B 1 61  ? 52.332 -14.819 0.676   1.00 13.84 ?  61  MET   B HG3  1 
ATOM   4898 H  HE1  . MET   B 1 61  ? 51.590 -17.195 -2.033  1.00 15.72 ?  61  MET   B HE1  1 
ATOM   4899 H  HE2  . MET   B 1 61  ? 51.377 -15.718 -1.489  1.00 15.72 ?  61  MET   B HE2  1 
ATOM   4900 H  HE3  . MET   B 1 61  ? 52.832 -16.215 -1.887  1.00 15.72 ?  61  MET   B HE3  1 
ATOM   4901 N  N    . GLN   B 1 62  ? 55.656 -14.712 3.361   1.00 12.07 ?  62  GLN   B N    1 
ATOM   4902 C  CA   . GLN   B 1 62  ? 55.546 -14.771 4.817   1.00 12.14 ?  62  GLN   B CA   1 
ATOM   4903 C  C    . GLN   B 1 62  ? 55.828 -13.417 5.454   1.00 12.29 ?  62  GLN   B C    1 
ATOM   4904 O  O    . GLN   B 1 62  ? 55.136 -13.019 6.399   1.00 12.93 ?  62  GLN   B O    1 
ATOM   4905 C  CB   . GLN   B 1 62  ? 56.489 -15.833 5.390   1.00 12.45 ?  62  GLN   B CB   1 
ATOM   4906 C  CG   . GLN   B 1 62  ? 56.262 -16.094 6.872   1.00 12.90 ?  62  GLN   B CG   1 
ATOM   4907 C  CD   . GLN   B 1 62  ? 54.888 -16.689 7.120   1.00 12.26 ?  62  GLN   B CD   1 
ATOM   4908 O  OE1  . GLN   B 1 62  ? 54.633 -17.838 6.761   1.00 12.93 ?  62  GLN   B OE1  1 
ATOM   4909 N  NE2  . GLN   B 1 62  ? 53.975 -15.896 7.681   1.00 12.90 ?  62  GLN   B NE2  1 
ATOM   4910 H  H    . GLN   B 1 62  ? 56.312 -15.158 3.023   1.00 14.48 ?  62  GLN   B H    1 
ATOM   4911 H  HA   . GLN   B 1 62  ? 54.638 -15.024 5.044   1.00 14.57 ?  62  GLN   B HA   1 
ATOM   4912 H  HB2  . GLN   B 1 62  ? 56.350 -16.670 4.919   1.00 14.94 ?  62  GLN   B HB2  1 
ATOM   4913 H  HB3  . GLN   B 1 62  ? 57.405 -15.537 5.275   1.00 14.94 ?  62  GLN   B HB3  1 
ATOM   4914 H  HG2  . GLN   B 1 62  ? 56.931 -16.721 7.189   1.00 15.48 ?  62  GLN   B HG2  1 
ATOM   4915 H  HG3  . GLN   B 1 62  ? 56.330 -15.257 7.359   1.00 15.48 ?  62  GLN   B HG3  1 
ATOM   4916 H  HE21 . GLN   B 1 62  ? 54.183 -15.092 7.905   1.00 15.48 ?  62  GLN   B HE21 1 
ATOM   4917 H  HE22 . GLN   B 1 62  ? 53.183 -16.193 7.828   1.00 15.48 ?  62  GLN   B HE22 1 
ATOM   4918 N  N    . VAL   B 1 63  ? 56.847 -12.704 4.967   1.00 12.67 ?  63  VAL   B N    1 
ATOM   4919 C  CA   . VAL   B 1 63  ? 57.152 -11.384 5.517   1.00 13.82 ?  63  VAL   B CA   1 
ATOM   4920 C  C    . VAL   B 1 63  ? 55.960 -10.448 5.334   1.00 13.16 ?  63  VAL   B C    1 
ATOM   4921 O  O    . VAL   B 1 63  ? 55.546 -9.742  6.264   1.00 13.72 ?  63  VAL   B O    1 
ATOM   4922 C  CB   . VAL   B 1 63  ? 58.444 -10.826 4.893   1.00 14.89 ?  63  VAL   B CB   1 
ATOM   4923 C  CG1  . VAL   B 1 63  ? 58.673 -9.389  5.338   1.00 15.63 ?  63  VAL   B CG1  1 
ATOM   4924 C  CG2  . VAL   B 1 63  ? 59.624 -11.704 5.279   1.00 15.64 ?  63  VAL   B CG2  1 
ATOM   4925 H  H    . VAL   B 1 63  ? 57.360 -12.955 4.319   1.00 15.20 ?  63  VAL   B H    1 
ATOM   4926 H  HA   . VAL   B 1 63  ? 57.305 -11.481 6.465   1.00 16.58 ?  63  VAL   B HA   1 
ATOM   4927 H  HB   . VAL   B 1 63  ? 58.369 -10.838 3.925   1.00 17.86 ?  63  VAL   B HB   1 
ATOM   4928 H  HG11 . VAL   B 1 63  ? 59.591 -9.143  5.149   1.00 18.76 ?  63  VAL   B HG11 1 
ATOM   4929 H  HG12 . VAL   B 1 63  ? 58.068 -8.808  4.854   1.00 18.76 ?  63  VAL   B HG12 1 
ATOM   4930 H  HG13 . VAL   B 1 63  ? 58.506 -9.327  6.292   1.00 18.76 ?  63  VAL   B HG13 1 
ATOM   4931 H  HG21 . VAL   B 1 63  ? 60.437 -11.328 4.902   1.00 18.77 ?  63  VAL   B HG21 1 
ATOM   4932 H  HG22 . VAL   B 1 63  ? 59.695 -11.730 6.248   1.00 18.77 ?  63  VAL   B HG22 1 
ATOM   4933 H  HG23 . VAL   B 1 63  ? 59.484 -12.599 4.935   1.00 18.77 ?  63  VAL   B HG23 1 
ATOM   4934 N  N    . GLU   B 1 64  ? 55.386 -10.438 4.129   1.00 12.67 ?  64  GLU   B N    1 
ATOM   4935 C  CA   . GLU   B 1 64  ? 54.219 -9.603  3.854   1.00 12.52 ?  64  GLU   B CA   1 
ATOM   4936 C  C    . GLU   B 1 64  ? 53.037 -10.006 4.730   1.00 12.15 ?  64  GLU   B C    1 
ATOM   4937 O  O    . GLU   B 1 64  ? 52.291 -9.145  5.227   1.00 12.50 ?  64  GLU   B O    1 
ATOM   4938 C  CB   . GLU   B 1 64  ? 53.858 -9.748  2.374   1.00 12.88 ?  64  GLU   B CB   1 
ATOM   4939 C  CG   . GLU   B 1 64  ? 52.590 -9.025  1.940   1.00 12.81 ?  64  GLU   B CG   1 
ATOM   4940 C  CD   . GLU   B 1 64  ? 52.067 -9.520  0.598   1.00 13.61 ?  64  GLU   B CD   1 
ATOM   4941 O  OE1  . GLU   B 1 64  ? 52.246 -10.729 0.286   1.00 14.37 ?  64  GLU   B OE1  1 
ATOM   4942 O  OE2  . GLU   B 1 64  ? 51.445 -8.706  -0.130  1.00 14.35 -1 64  GLU   B OE2  1 
ATOM   4943 H  H    . GLU   B 1 64  ? 55.652 -10.905 3.452   1.00 15.20 ?  64  GLU   B H    1 
ATOM   4944 H  HA   . GLU   B 1 64  ? 54.435 -8.674  4.032   1.00 15.03 ?  64  GLU   B HA   1 
ATOM   4945 H  HB2  . GLU   B 1 64  ? 54.587 -9.382  1.842   1.00 15.46 ?  64  GLU   B HB2  1 
ATOM   4946 H  HB3  . GLU   B 1 64  ? 53.746 -10.683 2.173   1.00 15.46 ?  64  GLU   B HB3  1 
ATOM   4947 H  HG2  . GLU   B 1 64  ? 51.888 -9.170  2.599   1.00 15.37 ?  64  GLU   B HG2  1 
ATOM   4948 H  HG3  . GLU   B 1 64  ? 52.773 -8.076  1.862   1.00 15.37 ?  64  GLU   B HG3  1 
ATOM   4949 N  N    . SER   B 1 65  ? 52.851 -11.314 4.922   1.00 11.72 ?  65  SER   B N    1 
ATOM   4950 C  CA   . SER   B 1 65  ? 51.737 -11.816 5.717   1.00 11.70 ?  65  SER   B CA   1 
ATOM   4951 C  C    . SER   B 1 65  ? 51.871 -11.416 7.180   1.00 11.85 ?  65  SER   B C    1 
ATOM   4952 O  O    . SER   B 1 65  ? 50.874 -11.049 7.816   1.00 12.18 ?  65  SER   B O    1 
ATOM   4953 C  CB   . SER   B 1 65  ? 51.652 -13.334 5.589   1.00 11.85 ?  65  SER   B CB   1 
ATOM   4954 O  OG   . SER   B 1 65  ? 51.310 -13.738 4.273   1.00 12.20 ?  65  SER   B OG   1 
ATOM   4955 H  H    . SER   B 1 65  ? 53.360 -11.933 4.603   1.00 14.07 ?  65  SER   B H    1 
ATOM   4956 H  HA   . SER   B 1 65  ? 50.911 -11.437 5.383   1.00 14.05 ?  65  SER   B HA   1 
ATOM   4957 H  HB2  . SER   B 1 65  ? 52.508 -13.719 5.813   1.00 14.22 ?  65  SER   B HB2  1 
ATOM   4958 H  HB3  . SER   B 1 65  ? 50.971 -13.660 6.202   1.00 14.22 ?  65  SER   B HB3  1 
ATOM   4959 H  HG   . SER   B 1 65  ? 51.878 -13.446 3.723   1.00 14.64 ?  65  SER   B HG   1 
ATOM   4960 N  N    . ASP   B 1 66  ? 53.080 -11.517 7.747   1.00 12.44 ?  66  ASP   B N    1 
ATOM   4961 C  CA   . ASP   B 1 66  ? 53.265 -11.122 9.142   1.00 12.65 ?  66  ASP   B CA   1 
ATOM   4962 C  C    . ASP   B 1 66  ? 52.955 -9.641  9.336   1.00 12.74 ?  66  ASP   B C    1 
ATOM   4963 O  O    . ASP   B 1 66  ? 52.389 -9.245  10.361  1.00 13.28 ?  66  ASP   B O    1 
ATOM   4964 C  CB   . ASP   B 1 66  ? 54.690 -11.437 9.606   1.00 13.96 ?  66  ASP   B CB   1 
ATOM   4965 C  CG   . ASP   B 1 66  ? 54.954 -12.931 9.758   1.00 15.89 ?  66  ASP   B CG   1 
ATOM   4966 O  OD1  . ASP   B 1 66  ? 54.001 -13.741 9.683   1.00 16.71 ?  66  ASP   B OD1  1 
ATOM   4967 O  OD2  . ASP   B 1 66  ? 56.134 -13.300 9.965   1.00 18.39 -1 66  ASP   B OD2  1 
ATOM   4968 H  H    . ASP   B 1 66  ? 53.787 -11.815 7.361   1.00 14.93 ?  66  ASP   B H    1 
ATOM   4969 H  HA   . ASP   B 1 66  ? 52.652 -11.621 9.702   1.00 15.18 ?  66  ASP   B HA   1 
ATOM   4970 H  HB2  . ASP   B 1 66  ? 55.317 -11.087 8.957   1.00 16.75 ?  66  ASP   B HB2  1 
ATOM   4971 H  HB3  . ASP   B 1 66  ? 54.839 -11.014 10.471  1.00 16.75 ?  66  ASP   B HB3  1 
ATOM   4972 N  N    . ASP   B 1 67  ? 53.330 -8.801  8.368   1.00 12.29 ?  67  ASP   B N    1 
ATOM   4973 C  CA   . ASP   B 1 67  ? 52.987 -7.386  8.452   1.00 12.87 ?  67  ASP   B CA   1 
ATOM   4974 C  C    . ASP   B 1 67  ? 51.476 -7.179  8.373   1.00 13.02 ?  67  ASP   B C    1 
ATOM   4975 O  O    . ASP   B 1 67  ? 50.915 -6.372  9.123   1.00 13.71 ?  67  ASP   B O    1 
ATOM   4976 C  CB   . ASP   B 1 67  ? 53.706 -6.617  7.348   1.00 14.28 ?  67  ASP   B CB   1 
ATOM   4977 C  CG   . ASP   B 1 67  ? 53.278 -5.174  7.291   1.00 16.06 ?  67  ASP   B CG   1 
ATOM   4978 O  OD1  . ASP   B 1 67  ? 53.771 -4.355  8.100   1.00 17.31 ?  67  ASP   B OD1  1 
ATOM   4979 O  OD2  . ASP   B 1 67  ? 52.414 -4.879  6.451   1.00 17.05 -1 67  ASP   B OD2  1 
ATOM   4980 H  H    . ASP   B 1 67  ? 53.780 -9.023  7.668   1.00 14.75 ?  67  ASP   B H    1 
ATOM   4981 H  HA   . ASP   B 1 67  ? 53.292 -7.038  9.304   1.00 15.44 ?  67  ASP   B HA   1 
ATOM   4982 H  HB2  . ASP   B 1 67  ? 54.664 -6.646  7.511   1.00 17.14 ?  67  ASP   B HB2  1 
ATOM   4983 H  HB3  . ASP   B 1 67  ? 53.508 -7.031  6.490   1.00 17.14 ?  67  ASP   B HB3  1 
ATOM   4984 N  N    . TYR   B 1 68  ? 50.798 -7.913  7.485   1.00 12.68 ?  68  TYR   B N    1 
ATOM   4985 C  CA   . TYR   B 1 68  ? 49.340 -7.835  7.412   1.00 13.45 ?  68  TYR   B CA   1 
ATOM   4986 C  C    . TYR   B 1 68  ? 48.706 -8.177  8.756   1.00 13.37 ?  68  TYR   B C    1 
ATOM   4987 O  O    . TYR   B 1 68  ? 47.773 -7.498  9.203   1.00 14.11 ?  68  TYR   B O    1 
ATOM   4988 C  CB   . TYR   B 1 68  ? 48.807 -8.760  6.310   1.00 14.25 ?  68  TYR   B CB   1 
ATOM   4989 C  CG   . TYR   B 1 68  ? 47.301 -8.907  6.367   1.00 15.55 ?  68  TYR   B CG   1 
ATOM   4990 C  CD1  . TYR   B 1 68  ? 46.714 -9.862  7.188   1.00 16.22 ?  68  TYR   B CD1  1 
ATOM   4991 C  CD2  . TYR   B 1 68  ? 46.468 -8.072  5.637   1.00 16.67 ?  68  TYR   B CD2  1 
ATOM   4992 C  CE1  . TYR   B 1 68  ? 45.349 -9.987  7.277   1.00 17.48 ?  68  TYR   B CE1  1 
ATOM   4993 C  CE2  . TYR   B 1 68  ? 45.084 -8.197  5.717   1.00 17.39 ?  68  TYR   B CE2  1 
ATOM   4994 C  CZ   . TYR   B 1 68  ? 44.545 -9.157  6.539   1.00 17.63 ?  68  TYR   B CZ   1 
ATOM   4995 O  OH   . TYR   B 1 68  ? 43.179 -9.279  6.636   1.00 18.72 ?  68  TYR   B OH   1 
ATOM   4996 H  H    . TYR   B 1 68  ? 51.156 -8.467  6.926   1.00 15.22 ?  68  TYR   B H    1 
ATOM   4997 H  HA   . TYR   B 1 68  ? 49.092 -6.929  7.189   1.00 16.14 ?  68  TYR   B HA   1 
ATOM   4998 H  HB2  . TYR   B 1 68  ? 49.036 -8.390  5.446   1.00 17.10 ?  68  TYR   B HB2  1 
ATOM   4999 H  HB3  . TYR   B 1 68  ? 49.197 -9.642  6.414   1.00 17.10 ?  68  TYR   B HB3  1 
ATOM   5000 H  HD1  . TYR   B 1 68  ? 47.255 -10.433 7.690   1.00 19.46 ?  68  TYR   B HD1  1 
ATOM   5001 H  HD2  . TYR   B 1 68  ? 46.840 -7.419  5.094   1.00 20.00 ?  68  TYR   B HD2  1 
ATOM   5002 H  HE1  . TYR   B 1 68  ? 44.968 -10.644 7.822   1.00 20.97 ?  68  TYR   B HE1  1 
ATOM   5003 H  HE2  . TYR   B 1 68  ? 44.527 -7.634  5.228   1.00 20.87 ?  68  TYR   B HE2  1 
ATOM   5004 H  HH   . TYR   B 1 68  ? 42.788 -8.726  6.129   1.00 22.47 ?  68  TYR   B HH   1 
ATOM   5005 N  N    . ILE   B 1 69  ? 49.188 -9.243  9.404   1.00 13.02 ?  69  ILE   B N    1 
ATOM   5006 C  CA   . ILE   B 1 69  ? 48.627 -9.669  10.684  1.00 13.54 ?  69  ILE   B CA   1 
ATOM   5007 C  C    . ILE   B 1 69  ? 48.881 -8.623  11.764  1.00 13.39 ?  69  ILE   B C    1 
ATOM   5008 O  O    . ILE   B 1 69  ? 48.012 -8.348  12.599  1.00 13.79 ?  69  ILE   B O    1 
ATOM   5009 C  CB   . ILE   B 1 69  ? 49.200 -11.045 11.075  1.00 14.13 ?  69  ILE   B CB   1 
ATOM   5010 C  CG1  . ILE   B 1 69  ? 48.664 -12.147 10.152  1.00 14.53 ?  69  ILE   B CG1  1 
ATOM   5011 C  CG2  . ILE   B 1 69  ? 48.921 -11.357 12.543  1.00 15.19 ?  69  ILE   B CG2  1 
ATOM   5012 C  CD1  . ILE   B 1 69  ? 47.189 -12.469 10.325  1.00 14.85 ?  69  ILE   B CD1  1 
ATOM   5013 H  H    . ILE   B 1 69  ? 49.837 -9.733  9.127   1.00 15.63 ?  69  ILE   B H    1 
ATOM   5014 H  HA   . ILE   B 1 69  ? 47.667 -9.766  10.588  1.00 16.24 ?  69  ILE   B HA   1 
ATOM   5015 H  HB   . ILE   B 1 69  ? 50.163 -11.006 10.964  1.00 16.95 ?  69  ILE   B HB   1 
ATOM   5016 H  HG12 . ILE   B 1 69  ? 48.802 -11.868 9.232   1.00 17.43 ?  69  ILE   B HG12 1 
ATOM   5017 H  HG13 . ILE   B 1 69  ? 49.169 -12.960 10.321  1.00 17.43 ?  69  ILE   B HG13 1 
ATOM   5018 H  HG21 . ILE   B 1 69  ? 49.055 -12.306 12.692  1.00 18.23 ?  69  ILE   B HG21 1 
ATOM   5019 H  HG22 . ILE   B 1 69  ? 49.533 -10.849 13.100  1.00 18.23 ?  69  ILE   B HG22 1 
ATOM   5020 H  HG23 . ILE   B 1 69  ? 48.005 -11.117 12.749  1.00 18.23 ?  69  ILE   B HG23 1 
ATOM   5021 H  HD11 . ILE   B 1 69  ? 46.954 -13.176 9.703   1.00 17.82 ?  69  ILE   B HD11 1 
ATOM   5022 H  HD12 . ILE   B 1 69  ? 47.035 -12.765 11.234  1.00 17.82 ?  69  ILE   B HD12 1 
ATOM   5023 H  HD13 . ILE   B 1 69  ? 46.668 -11.677 10.137  1.00 17.82 ?  69  ILE   B HD13 1 
ATOM   5024 N  N    . ALA   B 1 70  ? 50.075 -8.034  11.785  1.00 13.11 ?  70  ALA   B N    1 
ATOM   5025 C  CA   . ALA   B 1 70  ? 50.356 -6.998  12.773  1.00 12.99 ?  70  ALA   B CA   1 
ATOM   5026 C  C    . ALA   B 1 70  ? 49.359 -5.854  12.660  1.00 13.58 ?  70  ALA   B C    1 
ATOM   5027 O  O    . ALA   B 1 70  ? 48.910 -5.308  13.673  1.00 14.02 ?  70  ALA   B O    1 
ATOM   5028 C  CB   . ALA   B 1 70  ? 51.784 -6.483  12.597  1.00 13.64 ?  70  ALA   B CB   1 
ATOM   5029 H  H    . ALA   B 1 70  ? 50.718 -8.215  11.253  1.00 15.73 ?  70  ALA   B H    1 
ATOM   5030 H  HA   . ALA   B 1 70  ? 50.282 -7.376  13.663  1.00 15.59 ?  70  ALA   B HA   1 
ATOM   5031 H  HB1  . ALA   B 1 70  ? 51.970 -5.822  13.281  1.00 16.37 ?  70  ALA   B HB1  1 
ATOM   5032 H  HB2  . ALA   B 1 70  ? 52.402 -7.228  12.681  1.00 16.37 ?  70  ALA   B HB2  1 
ATOM   5033 H  HB3  . ALA   B 1 70  ? 51.871 -6.083  11.716  1.00 16.37 ?  70  ALA   B HB3  1 
ATOM   5034 N  N    . THR   B 1 71  ? 48.987 -5.491  11.435  1.00 13.95 ?  71  THR   B N    1 
ATOM   5035 C  CA   . THR   B 1 71  ? 48.095 -4.355  11.230  1.00 14.86 ?  71  THR   B CA   1 
ATOM   5036 C  C    . THR   B 1 71  ? 46.628 -4.725  11.431  1.00 15.63 ?  71  THR   B C    1 
ATOM   5037 O  O    . THR   B 1 71  ? 45.844 -3.911  11.938  1.00 17.12 ?  71  THR   B O    1 
ATOM   5038 C  CB   . THR   B 1 71  ? 48.312 -3.780  9.827   1.00 16.85 ?  71  THR   B CB   1 
ATOM   5039 O  OG1  . THR   B 1 71  ? 49.639 -3.251  9.728   1.00 19.23 ?  71  THR   B OG1  1 
ATOM   5040 C  CG2  . THR   B 1 71  ? 47.297 -2.684  9.513   1.00 17.81 ?  71  THR   B CG2  1 
ATOM   5041 H  H    . THR   B 1 71  ? 49.234 -5.884  10.712  1.00 16.74 ?  71  THR   B H    1 
ATOM   5042 H  HA   . THR   B 1 71  ? 48.316 -3.661  11.868  1.00 17.84 ?  71  THR   B HA   1 
ATOM   5043 H  HB   . THR   B 1 71  ? 48.214 -4.481  9.167   1.00 20.22 ?  71  THR   B HB   1 
ATOM   5044 H  HG1  . THR   B 1 71  ? 49.763 -2.908  8.966   1.00 23.07 ?  71  THR   B HG1  1 
ATOM   5045 H  HG21 . THR   B 1 71  ? 47.601 -2.156  8.756   1.00 21.37 ?  71  THR   B HG21 1 
ATOM   5046 H  HG22 . THR   B 1 71  ? 46.438 -3.076  9.295   1.00 21.37 ?  71  THR   B HG22 1 
ATOM   5047 H  HG23 . THR   B 1 71  ? 47.193 -2.097  10.279  1.00 21.37 ?  71  THR   B HG23 1 
ATOM   5048 N  N    . ASN   B 1 72  ? 46.235 -5.940  11.042  1.00 15.03 ?  72  ASN   B N    1 
ATOM   5049 C  CA   . ASN   B 1 72  ? 44.830 -6.294  10.910  1.00 15.51 ?  72  ASN   B CA   1 
ATOM   5050 C  C    . ASN   B 1 72  ? 44.356 -7.384  11.860  1.00 16.21 ?  72  ASN   B C    1 
ATOM   5051 O  O    . ASN   B 1 72  ? 43.141 -7.535  12.032  1.00 17.56 ?  72  ASN   B O    1 
ATOM   5052 C  CB   . ASN   B 1 72  ? 44.533 -6.727  9.465   1.00 16.53 ?  72  ASN   B CB   1 
ATOM   5053 C  CG   . ASN   B 1 72  ? 44.803 -5.625  8.467   1.00 17.33 ?  72  ASN   B CG   1 
ATOM   5054 O  OD1  . ASN   B 1 72  ? 45.816 -5.636  7.760   1.00 18.59 ?  72  ASN   B OD1  1 
ATOM   5055 N  ND2  . ASN   B 1 72  ? 43.919 -4.644  8.430   1.00 18.91 ?  72  ASN   B ND2  1 
ATOM   5056 H  H    . ASN   B 1 72  ? 46.776 -6.587  10.853  1.00 18.04 ?  72  ASN   B H    1 
ATOM   5057 H  HA   . ASN   B 1 72  ? 44.300 -5.503  11.085  1.00 18.61 ?  72  ASN   B HA   1 
ATOM   5058 H  HB2  . ASN   B 1 72  ? 45.103 -7.481  9.234   1.00 19.83 ?  72  ASN   B HB2  1 
ATOM   5059 H  HB3  . ASN   B 1 72  ? 43.603 -6.976  9.389   1.00 19.83 ?  72  ASN   B HB3  1 
ATOM   5060 H  HD21 . ASN   B 1 72  ? 44.023 -3.989  7.881   1.00 22.69 ?  72  ASN   B HD21 1 
ATOM   5061 H  HD22 . ASN   B 1 72  ? 43.226 -4.669  8.940   1.00 22.69 ?  72  ASN   B HD22 1 
ATOM   5062 N  N    . GLY   B 1 73  ? 45.258 -8.141  12.476  1.00 15.79 ?  73  GLY   B N    1 
ATOM   5063 C  CA   . GLY   B 1 73  ? 44.861 -9.276  13.273  1.00 15.21 ?  73  GLY   B CA   1 
ATOM   5064 C  C    . GLY   B 1 73  ? 44.499 -10.465 12.408  1.00 14.28 ?  73  GLY   B C    1 
ATOM   5065 O  O    . GLY   B 1 73  ? 44.486 -10.386 11.177  1.00 14.01 ?  73  GLY   B O    1 
ATOM   5066 H  H    . GLY   B 1 73  ? 46.109 -8.013  12.445  1.00 18.94 ?  73  GLY   B H    1 
ATOM   5067 H  HA2  . GLY   B 1 73  ? 45.585 -9.528  13.865  1.00 18.25 ?  73  GLY   B HA2  1 
ATOM   5068 H  HA3  . GLY   B 1 73  ? 44.087 -9.039  13.813  1.00 18.25 ?  73  GLY   B HA3  1 
ATOM   5069 N  N    . PRO   B 1 74  ? 44.194 -11.591 13.050  1.00 14.13 ?  74  PRO   B N    1 
ATOM   5070 C  CA   . PRO   B 1 74  ? 43.936 -12.825 12.306  1.00 13.52 ?  74  PRO   B CA   1 
ATOM   5071 C  C    . PRO   B 1 74  ? 42.642 -12.767 11.508  1.00 13.12 ?  74  PRO   B C    1 
ATOM   5072 O  O    . PRO   B 1 74  ? 41.699 -12.036 11.834  1.00 14.26 ?  74  PRO   B O    1 
ATOM   5073 C  CB   . PRO   B 1 74  ? 43.846 -13.883 13.412  1.00 14.47 ?  74  PRO   B CB   1 
ATOM   5074 C  CG   . PRO   B 1 74  ? 43.415 -13.124 14.624  1.00 15.97 ?  74  PRO   B CG   1 
ATOM   5075 C  CD   . PRO   B 1 74  ? 44.103 -11.794 14.505  1.00 15.53 ?  74  PRO   B CD   1 
ATOM   5076 H  HA   . PRO   B 1 74  ? 44.683 -13.027 11.713  1.00 16.22 ?  74  PRO   B HA   1 
ATOM   5077 H  HB2  . PRO   B 1 74  ? 43.186 -14.551 13.167  1.00 17.36 ?  74  PRO   B HB2  1 
ATOM   5078 H  HB3  . PRO   B 1 74  ? 44.715 -14.289 13.548  1.00 17.36 ?  74  PRO   B HB3  1 
ATOM   5079 H  HG2  . PRO   B 1 74  ? 42.450 -13.016 14.614  1.00 19.17 ?  74  PRO   B HG2  1 
ATOM   5080 H  HG3  . PRO   B 1 74  ? 43.703 -13.592 15.420  1.00 19.17 ?  74  PRO   B HG3  1 
ATOM   5081 H  HD2  . PRO   B 1 74  ? 43.563 -11.097 14.917  1.00 18.63 ?  74  PRO   B HD2  1 
ATOM   5082 H  HD3  . PRO   B 1 74  ? 44.989 -11.832 14.895  1.00 18.63 ?  74  PRO   B HD3  1 
ATOM   5083 N  N    . LEU   B 1 75  ? 42.608 -13.577 10.455  1.00 12.36 ?  75  LEU   B N    1 
ATOM   5084 C  CA   . LEU   B 1 75  ? 41.394 -13.789 9.688   1.00 12.53 ?  75  LEU   B CA   1 
ATOM   5085 C  C    . LEU   B 1 75  ? 40.412 -14.643 10.489  1.00 13.10 ?  75  LEU   B C    1 
ATOM   5086 O  O    . LEU   B 1 75  ? 40.752 -15.217 11.527  1.00 14.23 ?  75  LEU   B O    1 
ATOM   5087 C  CB   . LEU   B 1 75  ? 41.715 -14.513 8.379   1.00 12.66 ?  75  LEU   B CB   1 
ATOM   5088 C  CG   . LEU   B 1 75  ? 42.560 -13.764 7.347   1.00 14.22 ?  75  LEU   B CG   1 
ATOM   5089 C  CD1  . LEU   B 1 75  ? 42.750 -14.589 6.076   1.00 15.91 ?  75  LEU   B CD1  1 
ATOM   5090 C  CD2  . LEU   B 1 75  ? 41.965 -12.420 7.014   1.00 17.62 ?  75  LEU   B CD2  1 
ATOM   5091 H  H    . LEU   B 1 75  ? 43.285 -14.026 10.162  1.00 14.83 ?  75  LEU   B H    1 
ATOM   5092 H  HA   . LEU   B 1 75  ? 40.977 -12.939 9.483   1.00 15.04 ?  75  LEU   B HA   1 
ATOM   5093 H  HB2  . LEU   B 1 75  ? 42.192 -15.332 8.594   1.00 15.19 ?  75  LEU   B HB2  1 
ATOM   5094 H  HB3  . LEU   B 1 75  ? 40.877 -14.743 7.945   1.00 15.19 ?  75  LEU   B HB3  1 
ATOM   5095 H  HG   . LEU   B 1 75  ? 43.441 -13.610 7.723   1.00 17.06 ?  75  LEU   B HG   1 
ATOM   5096 H  HD11 . LEU   B 1 75  ? 43.296 -14.086 5.448   1.00 19.09 ?  75  LEU   B HD11 1 
ATOM   5097 H  HD12 . LEU   B 1 75  ? 43.194 -15.423 6.300   1.00 19.09 ?  75  LEU   B HD12 1 
ATOM   5098 H  HD13 . LEU   B 1 75  ? 41.883 -14.772 5.683   1.00 19.09 ?  75  LEU   B HD13 1 
ATOM   5099 H  HD21 . LEU   B 1 75  ? 42.452 -12.033 6.271   1.00 21.15 ?  75  LEU   B HD21 1 
ATOM   5100 H  HD22 . LEU   B 1 75  ? 41.034 -12.540 6.777   1.00 21.15 ?  75  LEU   B HD22 1 
ATOM   5101 H  HD23 . LEU   B 1 75  ? 42.037 -11.844 7.793   1.00 21.15 ?  75  LEU   B HD23 1 
ATOM   5102 N  N    . LYS   B 1 76  ? 39.181 -14.733 9.981   1.00 14.20 ?  76  LYS   B N    1 
ATOM   5103 C  CA   . LYS   B 1 76  ? 38.195 -15.694 10.462  1.00 15.61 ?  76  LYS   B CA   1 
ATOM   5104 C  C    . LYS   B 1 76  ? 38.294 -16.969 9.628   1.00 14.36 ?  76  LYS   B C    1 
ATOM   5105 O  O    . LYS   B 1 76  ? 38.571 -16.917 8.430   1.00 14.01 ?  76  LYS   B O    1 
ATOM   5106 C  CB   . LYS   B 1 76  ? 36.770 -15.140 10.295  1.00 17.50 ?  76  LYS   B CB   1 
ATOM   5107 C  CG   . LYS   B 1 76  ? 36.490 -13.751 10.904  1.00 19.40 ?  76  LYS   B CG   1 
ATOM   5108 C  CD   . LYS   B 1 76  ? 35.082 -13.234 10.549  1.00 20.71 ?  76  LYS   B CD   1 
ATOM   5109 C  CE   . LYS   B 1 76  ? 34.822 -11.845 11.123  1.00 22.50 ?  76  LYS   B CE   1 
ATOM   5110 N  NZ   . LYS   B 1 76  ? 33.521 -11.263 10.690  1.00 23.18 ?  76  LYS   B NZ   1 
ATOM   5111 H  H    . LYS   B 1 76  ? 38.892 -14.243 9.337   1.00 17.04 ?  76  LYS   B H    1 
ATOM   5112 H  HA   . LYS   B 1 76  ? 38.356 -15.911 11.394  1.00 18.73 ?  76  LYS   B HA   1 
ATOM   5113 H  HB2  . LYS   B 1 76  ? 36.579 -15.082 9.346   1.00 21.00 ?  76  LYS   B HB2  1 
ATOM   5114 H  HB3  . LYS   B 1 76  ? 36.154 -15.765 10.709  1.00 21.00 ?  76  LYS   B HB3  1 
ATOM   5115 H  HG2  . LYS   B 1 76  ? 36.561 -13.811 11.870  1.00 23.28 ?  76  LYS   B HG2  1 
ATOM   5116 H  HG3  . LYS   B 1 76  ? 37.145 -13.120 10.561  1.00 23.28 ?  76  LYS   B HG3  1 
ATOM   5117 H  HD2  . LYS   B 1 76  ? 34.998 -13.187 9.583   1.00 24.85 ?  76  LYS   B HD2  1 
ATOM   5118 H  HD3  . LYS   B 1 76  ? 34.422 -13.844 10.912  1.00 24.85 ?  76  LYS   B HD3  1 
ATOM   5119 H  HE2  . LYS   B 1 76  ? 34.819 -11.903 12.090  1.00 27.01 ?  76  LYS   B HE2  1 
ATOM   5120 H  HE3  . LYS   B 1 76  ? 35.530 -11.249 10.830  1.00 27.01 ?  76  LYS   B HE3  1 
ATOM   5121 H  HZ1  . LYS   B 1 76  ? 33.413 -10.454 11.050  1.00 27.82 ?  76  LYS   B HZ1  1 
ATOM   5122 H  HZ2  . LYS   B 1 76  ? 33.496 -11.188 9.803   1.00 27.82 ?  76  LYS   B HZ2  1 
ATOM   5123 H  HZ3  . LYS   B 1 76  ? 32.848 -11.784 10.954  1.00 27.82 ?  76  LYS   B HZ3  1 
ATOM   5124 N  N    . VAL   B 1 77  ? 38.052 -18.124 10.260  1.00 15.02 ?  77  VAL   B N    1 
ATOM   5125 C  CA   . VAL   B 1 77  ? 37.842 -19.339 9.478   1.00 14.71 ?  77  VAL   B CA   1 
ATOM   5126 C  C    . VAL   B 1 77  ? 36.652 -19.108 8.560   1.00 13.80 ?  77  VAL   B C    1 
ATOM   5127 O  O    . VAL   B 1 77  ? 35.584 -18.672 9.006   1.00 13.93 ?  77  VAL   B O    1 
ATOM   5128 C  CB   . VAL   B 1 77  ? 37.635 -20.558 10.391  1.00 16.46 ?  77  VAL   B CB   1 
ATOM   5129 C  CG1  . VAL   B 1 77  ? 37.349 -21.795 9.549   1.00 17.07 ?  77  VAL   B CG1  1 
ATOM   5130 C  CG2  . VAL   B 1 77  ? 38.858 -20.780 11.276  1.00 17.86 ?  77  VAL   B CG2  1 
ATOM   5131 H  H    . VAL   B 1 77  ? 38.008 -18.226 11.107  1.00 18.02 ?  77  VAL   B H    1 
ATOM   5132 H  HA   . VAL   B 1 77  ? 38.617 -19.503 8.921   1.00 17.65 ?  77  VAL   B HA   1 
ATOM   5133 H  HB   . VAL   B 1 77  ? 36.866 -20.399 10.961  1.00 19.75 ?  77  VAL   B HB   1 
ATOM   5134 H  HG11 . VAL   B 1 77  ? 37.395 -22.578 10.120  1.00 20.48 ?  77  VAL   B HG11 1 
ATOM   5135 H  HG12 . VAL   B 1 77  ? 36.460 -21.723 9.163   1.00 20.48 ?  77  VAL   B HG12 1 
ATOM   5136 H  HG13 . VAL   B 1 77  ? 38.012 -21.859 8.846   1.00 20.48 ?  77  VAL   B HG13 1 
ATOM   5137 H  HG21 . VAL   B 1 77  ? 38.719 -21.578 11.806  1.00 21.43 ?  77  VAL   B HG21 1 
ATOM   5138 H  HG22 . VAL   B 1 77  ? 39.638 -20.887 10.711  1.00 21.43 ?  77  VAL   B HG22 1 
ATOM   5139 H  HG23 . VAL   B 1 77  ? 38.970 -20.010 11.854  1.00 21.43 ?  77  VAL   B HG23 1 
ATOM   5140 N  N    . GLY   B 1 78  ? 36.834 -19.383 7.269   1.00 13.28 ?  78  GLY   B N    1 
ATOM   5141 C  CA   . GLY   B 1 78  ? 35.855 -19.066 6.257   1.00 12.89 ?  78  GLY   B CA   1 
ATOM   5142 C  C    . GLY   B 1 78  ? 36.091 -17.750 5.553   1.00 12.33 ?  78  GLY   B C    1 
ATOM   5143 O  O    . GLY   B 1 78  ? 35.400 -17.468 4.569   1.00 12.79 ?  78  GLY   B O    1 
ATOM   5144 H  H    . GLY   B 1 78  ? 37.533 -19.773 6.953   1.00 15.93 ?  78  GLY   B H    1 
ATOM   5145 H  HA2  . GLY   B 1 78  ? 35.848 -19.763 5.588   1.00 15.47 ?  78  GLY   B HA2  1 
ATOM   5146 H  HA3  . GLY   B 1 78  ? 34.975 -19.030 6.667   1.00 15.47 ?  78  GLY   B HA3  1 
ATOM   5147 N  N    . GLY   B 1 79  ? 37.037 -16.938 6.034   1.00 12.66 ?  79  GLY   B N    1 
ATOM   5148 C  CA   . GLY   B 1 79  ? 37.335 -15.647 5.449   1.00 12.14 ?  79  GLY   B CA   1 
ATOM   5149 C  C    . GLY   B 1 79  ? 38.582 -15.672 4.573   1.00 11.64 ?  79  GLY   B C    1 
ATOM   5150 O  O    . GLY   B 1 79  ? 39.200 -16.708 4.335   1.00 12.13 ?  79  GLY   B O    1 
ATOM   5151 H  H    . GLY   B 1 79  ? 37.530 -17.124 6.710   1.00 15.19 ?  79  GLY   B H    1 
ATOM   5152 H  HA2  . GLY   B 1 79  ? 36.587 -15.353 4.905   1.00 14.57 ?  79  GLY   B HA2  1 
ATOM   5153 H  HA3  . GLY   B 1 79  ? 37.476 -14.997 6.154   1.00 14.57 ?  79  GLY   B HA3  1 
ATOM   5154 N  N    . SER   B 1 80  ? 38.950 -14.481 4.095   1.00 11.77 ?  80  SER   B N    1 
ATOM   5155 C  CA   . SER   B 1 80  ? 40.057 -14.354 3.154   1.00 11.36 ?  80  SER   B CA   1 
ATOM   5156 C  C    . SER   B 1 80  ? 40.638 -12.948 3.205   1.00 11.18 ?  80  SER   B C    1 
ATOM   5157 O  O    . SER   B 1 80  ? 40.020 -12.009 3.714   1.00 12.25 ?  80  SER   B O    1 
ATOM   5158 C  CB   . SER   B 1 80  ? 39.609 -14.648 1.719   1.00 12.03 ?  80  SER   B CB   1 
ATOM   5159 O  OG   . SER   B 1 80  ? 38.772 -13.617 1.217   1.00 12.70 ?  80  SER   B OG   1 
ATOM   5160 H  H    . SER   B 1 80  ? 38.579 -13.735 4.302   1.00 14.12 ?  80  SER   B H    1 
ATOM   5161 H  HA   . SER   B 1 80  ? 40.749 -14.987 3.400   1.00 13.64 ?  80  SER   B HA   1 
ATOM   5162 H  HB2  . SER   B 1 80  ? 40.391 -14.715 1.150   1.00 14.43 ?  80  SER   B HB2  1 
ATOM   5163 H  HB3  . SER   B 1 80  ? 39.118 -15.485 1.706   1.00 14.43 ?  80  SER   B HB3  1 
ATOM   5164 H  HG   . SER   B 1 80  ? 38.083 -13.544 1.705   1.00 15.24 ?  80  SER   B HG   1 
ATOM   5165 N  N    . CYS   B 1 81  ? 41.828 -12.809 2.622   1.00 10.76 ?  81  CYS   B N    1 
ATOM   5166 C  CA   . CYS   B 1 81  ? 42.374 -11.496 2.306   1.00 11.05 ?  81  CYS   B CA   1 
ATOM   5167 C  C    . CYS   B 1 81  ? 43.148 -11.580 0.999   1.00 10.51 ?  81  CYS   B C    1 
ATOM   5168 O  O    . CYS   B 1 81  ? 43.659 -12.641 0.624   1.00 11.55 ?  81  CYS   B O    1 
ATOM   5169 C  CB   . CYS   B 1 81  ? 43.268 -10.938 3.424   1.00 12.35 ?  81  CYS   B CB   1 
ATOM   5170 S  SG   . CYS   B 1 81  ? 44.789 -11.876 3.687   1.00 12.29 ?  81  CYS   B SG   1 
ATOM   5171 H  H    . CYS   B 1 81  ? 42.341 -13.467 2.394   1.00 12.91 ?  81  CYS   B H    1 
ATOM   5172 H  HA   . CYS   B 1 81  ? 41.641 -10.876 2.178   1.00 13.26 ?  81  CYS   B HA   1 
ATOM   5173 H  HB2  . CYS   B 1 81  ? 43.522 -10.027 3.199   1.00 14.82 ?  81  CYS   B HB2  1 
ATOM   5174 H  HB3  . CYS   B 1 81  ? 42.767 -10.936 4.258   1.00 14.82 ?  81  CYS   B HB3  1 
ATOM   5175 H  HG   . CYS   B 1 81  ? 45.409 -11.365 4.586   1.00 14.75 ?  81  CYS   B HG   1 
ATOM   5176 N  N    . VAL   B 1 82  ? 43.259 -10.434 0.328   1.00 10.66 ?  82  VAL   B N    1 
ATOM   5177 C  CA   . VAL   B 1 82  ? 44.023 -10.311 -0.911  1.00 11.05 ?  82  VAL   B CA   1 
ATOM   5178 C  C    . VAL   B 1 82  ? 45.367 -9.671  -0.597  1.00 11.42 ?  82  VAL   B C    1 
ATOM   5179 O  O    . VAL   B 1 82  ? 45.423 -8.557  -0.064  1.00 12.26 ?  82  VAL   B O    1 
ATOM   5180 C  CB   . VAL   B 1 82  ? 43.275 -9.476  -1.959  1.00 12.34 ?  82  VAL   B CB   1 
ATOM   5181 C  CG1  . VAL   B 1 82  ? 44.113 -9.341  -3.229  1.00 13.68 ?  82  VAL   B CG1  1 
ATOM   5182 C  CG2  . VAL   B 1 82  ? 41.910 -10.074 -2.257  1.00 13.54 ?  82  VAL   B CG2  1 
ATOM   5183 H  H    . VAL   B 1 82  ? 42.882 -9.692  0.570   1.00 12.79 ?  82  VAL   B H    1 
ATOM   5184 H  HA   . VAL   B 1 82  ? 44.181 -11.192 -1.278  1.00 13.26 ?  82  VAL   B HA   1 
ATOM   5185 H  HB   . VAL   B 1 82  ? 43.135 -8.585  -1.608  1.00 14.81 ?  82  VAL   B HB   1 
ATOM   5186 H  HG11 . VAL   B 1 82  ? 43.548 -9.015  -3.946  1.00 16.42 ?  82  VAL   B HG11 1 
ATOM   5187 H  HG12 . VAL   B 1 82  ? 44.835 -8.712  -3.068  1.00 16.42 ?  82  VAL   B HG12 1 
ATOM   5188 H  HG13 . VAL   B 1 82  ? 44.476 -10.209 -3.463  1.00 16.42 ?  82  VAL   B HG13 1 
ATOM   5189 H  HG21 . VAL   B 1 82  ? 41.482 -9.556  -2.957  1.00 16.25 ?  82  VAL   B HG21 1 
ATOM   5190 H  HG22 . VAL   B 1 82  ? 42.023 -10.993 -2.548  1.00 16.25 ?  82  VAL   B HG22 1 
ATOM   5191 H  HG23 . VAL   B 1 82  ? 41.372 -10.048 -1.450  1.00 16.25 ?  82  VAL   B HG23 1 
ATOM   5192 N  N    . LEU   B 1 83  ? 46.444 -10.361 -0.957  1.00 10.87 ?  83  LEU   B N    1 
ATOM   5193 C  CA   . LEU   B 1 83  ? 47.803 -9.846  -0.840  1.00 10.83 ?  83  LEU   B CA   1 
ATOM   5194 C  C    . LEU   B 1 83  ? 48.500 -9.989  -2.193  1.00 10.65 ?  83  LEU   B C    1 
ATOM   5195 O  O    . LEU   B 1 83  ? 47.899 -10.411 -3.184  1.00 10.70 ?  83  LEU   B O    1 
ATOM   5196 C  CB   . LEU   B 1 83  ? 48.557 -10.518 0.317   1.00 11.51 ?  83  LEU   B CB   1 
ATOM   5197 C  CG   . LEU   B 1 83  ? 48.047 -10.158 1.718   1.00 12.48 ?  83  LEU   B CG   1 
ATOM   5198 C  CD1  . LEU   B 1 83  ? 48.664 -11.037 2.794   1.00 13.03 ?  83  LEU   B CD1  1 
ATOM   5199 C  CD2  . LEU   B 1 83  ? 48.251 -8.672  2.049   1.00 13.35 ?  83  LEU   B CD2  1 
ATOM   5200 H  H    . LEU   B 1 83  ? 46.405 -11.159 -1.285  1.00 13.04 ?  83  LEU   B H    1 
ATOM   5201 H  HA   . LEU   B 1 83  ? 47.748 -8.903  -0.646  1.00 12.99 ?  83  LEU   B HA   1 
ATOM   5202 H  HB2  . LEU   B 1 83  ? 48.487 -11.478 0.219   1.00 13.81 ?  83  LEU   B HB2  1 
ATOM   5203 H  HB3  . LEU   B 1 83  ? 49.488 -10.251 0.266   1.00 13.81 ?  83  LEU   B HB3  1 
ATOM   5204 H  HG   . LEU   B 1 83  ? 47.094 -10.317 1.736   1.00 14.97 ?  83  LEU   B HG   1 
ATOM   5205 H  HD11 . LEU   B 1 83  ? 48.307 -10.778 3.660   1.00 15.64 ?  83  LEU   B HD11 1 
ATOM   5206 H  HD12 . LEU   B 1 83  ? 48.431 -11.965 2.612   1.00 15.64 ?  83  LEU   B HD12 1 
ATOM   5207 H  HD13 . LEU   B 1 83  ? 49.625 -10.931 2.786   1.00 15.64 ?  83  LEU   B HD13 1 
ATOM   5208 H  HD21 . LEU   B 1 83  ? 48.022 -8.523  2.981   1.00 16.02 ?  83  LEU   B HD21 1 
ATOM   5209 H  HD22 . LEU   B 1 83  ? 49.177 -8.435  1.894   1.00 16.02 ?  83  LEU   B HD22 1 
ATOM   5210 H  HD23 . LEU   B 1 83  ? 47.672 -8.139  1.480   1.00 16.02 ?  83  LEU   B HD23 1 
ATOM   5211 N  N    . SER   B 1 84  ? 49.775 -9.614  -2.252  1.00 11.79 ?  84  SER   B N    1 
ATOM   5212 C  CA   . SER   B 1 84  ? 50.515 -9.745  -3.497  1.00 12.02 ?  84  SER   B CA   1 
ATOM   5213 C  C    . SER   B 1 84  ? 50.677 -11.209 -3.895  1.00 11.30 ?  84  SER   B C    1 
ATOM   5214 O  O    . SER   B 1 84  ? 50.785 -12.102 -3.054  1.00 11.24 ?  84  SER   B O    1 
ATOM   5215 C  CB   . SER   B 1 84  ? 51.905 -9.129  -3.354  1.00 13.73 ?  84  SER   B CB   1 
ATOM   5216 O  OG   . SER   B 1 84  ? 52.653 -9.345  -4.536  1.00 15.34 ?  84  SER   B OG   1 
ATOM   5217 H  H    . SER   B 1 84  ? 50.217 -9.275  -1.599  1.00 14.14 ?  84  SER   B H    1 
ATOM   5218 H  HA   . SER   B 1 84  ? 50.046 -9.283  -4.209  1.00 14.43 ?  84  SER   B HA   1 
ATOM   5219 H  HB2  . SER   B 1 84  ? 51.818 -8.173  -3.197  1.00 16.47 ?  84  SER   B HB2  1 
ATOM   5220 H  HB3  . SER   B 1 84  ? 52.366 -9.545  -2.608  1.00 16.47 ?  84  SER   B HB3  1 
ATOM   5221 H  HG   . SER   B 1 84  ? 53.421 -8.997  -4.460  1.00 18.41 ?  84  SER   B HG   1 
ATOM   5222 N  N    . GLY   B 1 85  ? 50.741 -11.442 -5.199  1.00 12.27 ?  85  GLY   B N    1 
ATOM   5223 C  CA   . GLY   B 1 85  ? 51.090 -12.740 -5.724  1.00 12.91 ?  85  GLY   B CA   1 
ATOM   5224 C  C    . GLY   B 1 85  ? 52.560 -12.925 -6.037  1.00 12.17 ?  85  GLY   B C    1 
ATOM   5225 O  O    . GLY   B 1 85  ? 52.940 -14.002 -6.499  1.00 12.93 ?  85  GLY   B O    1 
ATOM   5226 H  H    . GLY   B 1 85  ? 50.597 -10.855 -5.804  1.00 14.73 ?  85  GLY   B H    1 
ATOM   5227 H  HA2  . GLY   B 1 85  ? 50.837 -13.424 -5.081  1.00 15.50 ?  85  GLY   B HA2  1 
ATOM   5228 H  HA3  . GLY   B 1 85  ? 50.597 -12.898 -6.538  1.00 15.50 ?  85  GLY   B HA3  1 
ATOM   5229 N  N    . HIS   B 1 86  ? 53.411 -11.921 -5.823  1.00 12.14 ?  86  HIS   B N    1 
ATOM   5230 C  CA   . HIS   B 1 86  ? 54.876 -12.081 -5.904  1.00 12.01 ?  86  HIS   B CA   1 
ATOM   5231 C  C    . HIS   B 1 86  ? 55.250 -12.596 -7.292  1.00 12.42 ?  86  HIS   B C    1 
ATOM   5232 O  O    . HIS   B 1 86  ? 54.859 -11.982 -8.297  1.00 13.16 ?  86  HIS   B O    1 
ATOM   5233 C  CB   . HIS   B 1 86  ? 55.364 -12.925 -4.722  1.00 12.71 ?  86  HIS   B CB   1 
ATOM   5234 C  CG   . HIS   B 1 86  ? 55.049 -12.316 -3.397  1.00 12.77 ?  86  HIS   B CG   1 
ATOM   5235 N  ND1  . HIS   B 1 86  ? 55.873 -11.399 -2.780  1.00 14.22 ?  86  HIS   B ND1  1 
ATOM   5236 C  CD2  . HIS   B 1 86  ? 53.973 -12.461 -2.590  1.00 12.83 ?  86  HIS   B CD2  1 
ATOM   5237 C  CE1  . HIS   B 1 86  ? 55.312 -11.005 -1.650  1.00 14.24 ?  86  HIS   B CE1  1 
ATOM   5238 N  NE2  . HIS   B 1 86  ? 54.158 -11.633 -1.512  1.00 13.37 ?  86  HIS   B NE2  1 
ATOM   5239 H  H    . HIS   B 1 86  ? 53.168 -11.123 -5.625  1.00 14.57 ?  86  HIS   B H    1 
ATOM   5240 H  HA   . HIS   B 1 86  ? 55.282 -11.208 -5.808  1.00 14.42 ?  86  HIS   B HA   1 
ATOM   5241 H  HB2  . HIS   B 1 86  ? 54.943 -13.798 -4.760  1.00 15.25 ?  86  HIS   B HB2  1 
ATOM   5242 H  HB3  . HIS   B 1 86  ? 56.329 -13.023 -4.780  1.00 15.25 ?  86  HIS   B HB3  1 
ATOM   5243 H  HD2  . HIS   B 1 86  ? 53.232 -13.008 -2.748  1.00 15.40 ?  86  HIS   B HD2  1 
ATOM   5244 H  HE1  . HIS   B 1 86  ? 55.674 -10.404 -1.045  1.00 17.09 ?  86  HIS   B HE1  1 
ATOM   5245 H  HE2  . HIS   B 1 86  ? 53.614 -11.553 -0.847  1.00 16.04 ?  86  HIS   B HE2  1 
ATOM   5246 N  N    . ASN   B 1 87  ? 56.015 -13.680 -7.399  1.00 12.86 ?  87  ASN   B N    1 
ATOM   5247 C  CA   . ASN   B 1 87  ? 56.410 -14.254 -8.676  1.00 13.52 ?  87  ASN   B CA   1 
ATOM   5248 C  C    . ASN   B 1 87  ? 55.423 -15.300 -9.178  1.00 13.35 ?  87  ASN   B C    1 
ATOM   5249 O  O    . ASN   B 1 87  ? 55.733 -16.007 -10.143 1.00 15.13 ?  87  ASN   B O    1 
ATOM   5250 C  CB   . ASN   B 1 87  ? 57.805 -14.880 -8.557  1.00 15.41 ?  87  ASN   B CB   1 
ATOM   5251 C  CG   . ASN   B 1 87  ? 57.859 -15.998 -7.518  1.00 16.08 ?  87  ASN   B CG   1 
ATOM   5252 O  OD1  . ASN   B 1 87  ? 57.232 -15.911 -6.459  1.00 15.25 ?  87  ASN   B OD1  1 
ATOM   5253 N  ND2  . ASN   B 1 87  ? 58.597 -17.067 -7.829  1.00 18.32 ?  87  ASN   B ND2  1 
ATOM   5254 H  H    . ASN   B 1 87  ? 56.322 -14.116 -6.725  1.00 15.44 ?  87  ASN   B H    1 
ATOM   5255 H  HA   . ASN   B 1 87  ? 56.453 -13.548 -9.338  1.00 16.22 ?  87  ASN   B HA   1 
ATOM   5256 H  HB2  . ASN   B 1 87  ? 58.055 -15.254 -9.419  1.00 18.50 ?  87  ASN   B HB2  1 
ATOM   5257 H  HB3  . ASN   B 1 87  ? 58.436 -14.193 -8.298  1.00 18.50 ?  87  ASN   B HB3  1 
ATOM   5258 H  HD21 . ASN   B 1 87  ? 58.658 -17.719 -7.275  1.00 21.98 ?  87  ASN   B HD21 1 
ATOM   5259 H  HD22 . ASN   B 1 87  ? 59.013 -17.098 -8.582  1.00 21.98 ?  87  ASN   B HD22 1 
ATOM   5260 N  N    . LEU   B 1 88  ? 54.241 -15.402 -8.558  1.00 12.30 ?  88  LEU   B N    1 
ATOM   5261 C  CA   . LEU   B 1 88  ? 53.257 -16.428 -8.881  1.00 12.62 ?  88  LEU   B CA   1 
ATOM   5262 C  C    . LEU   B 1 88  ? 52.029 -15.909 -9.605  1.00 12.24 ?  88  LEU   B C    1 
ATOM   5263 O  O    . LEU   B 1 88  ? 51.439 -16.656 -10.396 1.00 14.22 ?  88  LEU   B O    1 
ATOM   5264 C  CB   . LEU   B 1 88  ? 52.792 -17.116 -7.597  1.00 13.49 ?  88  LEU   B CB   1 
ATOM   5265 C  CG   . LEU   B 1 88  ? 53.908 -17.786 -6.811  1.00 15.98 ?  88  LEU   B CG   1 
ATOM   5266 C  CD1  . LEU   B 1 88  ? 53.403 -18.177 -5.435  1.00 17.48 ?  88  LEU   B CD1  1 
ATOM   5267 C  CD2  . LEU   B 1 88  ? 54.417 -18.994 -7.572  1.00 19.14 ?  88  LEU   B CD2  1 
ATOM   5268 H  H    . LEU   B 1 88  ? 53.980 -14.863 -7.930  1.00 14.76 ?  88  LEU   B H    1 
ATOM   5269 H  HA   . LEU   B 1 88  ? 53.670 -17.088 -9.445  1.00 15.14 ?  88  LEU   B HA   1 
ATOM   5270 H  HB2  . LEU   B 1 88  ? 52.372 -16.460 -7.018  1.00 16.19 ?  88  LEU   B HB2  1 
ATOM   5271 H  HB3  . LEU   B 1 88  ? 52.142 -17.802 -7.832  1.00 16.19 ?  88  LEU   B HB3  1 
ATOM   5272 H  HG   . LEU   B 1 88  ? 54.640 -17.161 -6.701  1.00 19.17 ?  88  LEU   B HG   1 
ATOM   5273 H  HD11 . LEU   B 1 88  ? 54.073 -18.724 -4.998  1.00 20.98 ?  88  LEU   B HD11 1 
ATOM   5274 H  HD12 . LEU   B 1 88  ? 53.240 -17.373 -4.918  1.00 20.98 ?  88  LEU   B HD12 1 
ATOM   5275 H  HD13 . LEU   B 1 88  ? 52.579 -18.679 -5.536  1.00 20.98 ?  88  LEU   B HD13 1 
ATOM   5276 H  HD21 . LEU   B 1 88  ? 55.048 -19.471 -7.013  1.00 22.97 ?  88  LEU   B HD21 1 
ATOM   5277 H  HD22 . LEU   B 1 88  ? 53.667 -19.566 -7.793  1.00 22.97 ?  88  LEU   B HD22 1 
ATOM   5278 H  HD23 . LEU   B 1 88  ? 54.855 -18.692 -8.384  1.00 22.97 ?  88  LEU   B HD23 1 
ATOM   5279 N  N    . ALA   B 1 89  ? 51.623 -14.673 -9.340  1.00 11.64 ?  89  ALA   B N    1 
ATOM   5280 C  CA   . ALA   B 1 89  ? 50.335 -14.176 -9.797  1.00 11.01 ?  89  ALA   B CA   1 
ATOM   5281 C  C    . ALA   B 1 89  ? 50.305 -12.688 -9.510  1.00 11.64 ?  89  ALA   B C    1 
ATOM   5282 O  O    . ALA   B 1 89  ? 51.136 -12.176 -8.762  1.00 12.09 ?  89  ALA   B O    1 
ATOM   5283 C  CB   . ALA   B 1 89  ? 49.189 -14.853 -9.054  1.00 11.46 ?  89  ALA   B CB   1 
ATOM   5284 H  H    . ALA   B 1 89  ? 52.070 -14.091 -8.889  1.00 13.96 ?  89  ALA   B H    1 
ATOM   5285 H  HA   . ALA   B 1 89  ? 50.228 -14.316 -10.755 1.00 13.21 ?  89  ALA   B HA   1 
ATOM   5286 H  HB1  . ALA   B 1 89  ? 48.344 -14.518 -9.400  1.00 13.75 ?  89  ALA   B HB1  1 
ATOM   5287 H  HB2  . ALA   B 1 89  ? 49.247 -15.810 -9.202  1.00 13.75 ?  89  ALA   B HB2  1 
ATOM   5288 H  HB3  . ALA   B 1 89  ? 49.265 -14.655 -8.113  1.00 13.75 ?  89  ALA   B HB3  1 
ATOM   5289 N  N    . LYS   B 1 90  ? 49.325 -11.995 -10.082 1.00 12.55 ?  90  LYS   B N    1 
ATOM   5290 C  CA   . LYS   B 1 90  ? 49.137 -10.608 -9.676  1.00 12.50 ?  90  LYS   B CA   1 
ATOM   5291 C  C    . LYS   B 1 90  ? 48.819 -10.530 -8.186  1.00 12.25 ?  90  LYS   B C    1 
ATOM   5292 O  O    . LYS   B 1 90  ? 49.462 -9.780  -7.437  1.00 13.34 ?  90  LYS   B O    1 
ATOM   5293 C  CB   . LYS   B 1 90  ? 48.062 -9.942  -10.533 1.00 14.19 ?  90  LYS   B CB   1 
ATOM   5294 C  CG   . LYS   B 1 90  ? 47.757 -8.500  -10.145 1.00 14.52 ?  90  LYS   B CG   1 
ATOM   5295 C  CD   . LYS   B 1 90  ? 48.966 -7.599  -10.216 1.00 17.25 ?  90  LYS   B CD   1 
ATOM   5296 C  CE   . LYS   B 1 90  ? 48.523 -6.179  -9.949  1.00 19.13 ?  90  LYS   B CE   1 
ATOM   5297 N  NZ   . LYS   B 1 90  ? 49.680 -5.258  -9.840  1.00 18.62 ?  90  LYS   B NZ   1 
ATOM   5298 H  H    . LYS   B 1 90  ? 48.777 -12.293 -10.676 1.00 15.05 ?  90  LYS   B H    1 
ATOM   5299 H  HA   . LYS   B 1 90  ? 49.963 -10.132 -9.821  1.00 15.00 ?  90  LYS   B HA   1 
ATOM   5300 H  HB2  . LYS   B 1 90  ? 48.358 -9.939  -11.459 1.00 17.03 ?  90  LYS   B HB2  1 
ATOM   5301 H  HB3  . LYS   B 1 90  ? 47.238 -10.450 -10.460 1.00 17.03 ?  90  LYS   B HB3  1 
ATOM   5302 H  HG2  . LYS   B 1 90  ? 47.083 -8.147  -10.751 1.00 17.42 ?  90  LYS   B HG2  1 
ATOM   5303 H  HG3  . LYS   B 1 90  ? 47.415 -8.481  -9.235  1.00 17.42 ?  90  LYS   B HG3  1 
ATOM   5304 H  HD2  . LYS   B 1 90  ? 49.609 -7.858  -9.537  1.00 20.69 ?  90  LYS   B HD2  1 
ATOM   5305 H  HD3  . LYS   B 1 90  ? 49.359 -7.646  -11.100 1.00 20.69 ?  90  LYS   B HD3  1 
ATOM   5306 H  HE2  . LYS   B 1 90  ? 47.962 -5.870  -10.681 1.00 22.96 ?  90  LYS   B HE2  1 
ATOM   5307 H  HE3  . LYS   B 1 90  ? 48.030 -6.141  -9.114  1.00 22.96 ?  90  LYS   B HE3  1 
ATOM   5308 H  HZ1  . LYS   B 1 90  ? 49.399 -4.427  -9.685  1.00 22.34 ?  90  LYS   B HZ1  1 
ATOM   5309 H  HZ2  . LYS   B 1 90  ? 50.210 -5.513  -9.172  1.00 22.34 ?  90  LYS   B HZ2  1 
ATOM   5310 H  HZ3  . LYS   B 1 90  ? 50.148 -5.267  -10.599 1.00 22.34 ?  90  LYS   B HZ3  1 
ATOM   5311 N  N    . HIS   B 1 91  ? 47.856 -11.341 -7.737  1.00 11.01 ?  91  HIS   B N    1 
ATOM   5312 C  CA   . HIS   B 1 91  ? 47.386 -11.364 -6.364  1.00 11.07 ?  91  HIS   B CA   1 
ATOM   5313 C  C    . HIS   B 1 91  ? 47.381 -12.791 -5.844  1.00 10.52 ?  91  HIS   B C    1 
ATOM   5314 O  O    . HIS   B 1 91  ? 47.151 -13.745 -6.597  1.00 11.00 ?  91  HIS   B O    1 
ATOM   5315 C  CB   . HIS   B 1 91  ? 45.933 -10.884 -6.251  1.00 12.43 ?  91  HIS   B CB   1 
ATOM   5316 C  CG   . HIS   B 1 91  ? 45.725 -9.474  -6.683  1.00 15.76 ?  91  HIS   B CG   1 
ATOM   5317 N  ND1  . HIS   B 1 91  ? 46.338 -8.404  -6.067  1.00 18.30 ?  91  HIS   B ND1  1 
ATOM   5318 C  CD2  . HIS   B 1 91  ? 44.947 -8.954  -7.657  1.00 18.27 ?  91  HIS   B CD2  1 
ATOM   5319 C  CE1  . HIS   B 1 91  ? 45.960 -7.282  -6.656  1.00 19.66 ?  91  HIS   B CE1  1 
ATOM   5320 N  NE2  . HIS   B 1 91  ? 45.110 -7.589  -7.621  1.00 19.81 ?  91  HIS   B NE2  1 
ATOM   5321 H  H    . HIS   B 1 91  ? 47.442 -11.910 -8.233  1.00 13.21 ?  91  HIS   B H    1 
ATOM   5322 H  HA   . HIS   B 1 91  ? 47.956 -10.807 -5.797  1.00 13.28 ?  91  HIS   B HA   1 
ATOM   5323 H  HB2  . HIS   B 1 91  ? 45.374 -11.446 -6.806  1.00 14.92 ?  91  HIS   B HB2  1 
ATOM   5324 H  HB3  . HIS   B 1 91  ? 45.649 -10.953 -5.323  1.00 14.92 ?  91  HIS   B HB3  1 
ATOM   5325 H  HD1  . HIS   B 1 91  ? 46.889 -8.458  -5.405  1.00 21.96 ?  91  HIS   B HD1  1 
ATOM   5326 H  HD2  . HIS   B 1 91  ? 44.408 -9.423  -8.246  1.00 21.93 ?  91  HIS   B HD2  1 
ATOM   5327 H  HE1  . HIS   B 1 91  ? 46.242 -6.425  -6.422  1.00 23.59 ?  91  HIS   B HE1  1 
ATOM   5328 N  N    . CYS   B 1 92  ? 47.575 -12.928 -4.539  1.00 10.27 ?  92  CYS   B N    1 
ATOM   5329 C  CA   . CYS   B 1 92  ? 47.270 -14.163 -3.830  1.00 9.94  ?  92  CYS   B CA   1 
ATOM   5330 C  C    . CYS   B 1 92  ? 46.048 -13.920 -2.951  1.00 9.70  ?  92  CYS   B C    1 
ATOM   5331 O  O    . CYS   B 1 92  ? 46.048 -13.014 -2.108  1.00 10.56 ?  92  CYS   B O    1 
ATOM   5332 C  CB   . CYS   B 1 92  ? 48.442 -14.622 -2.970  1.00 10.30 ?  92  CYS   B CB   1 
ATOM   5333 S  SG   . CYS   B 1 92  ? 48.087 -16.155 -2.069  1.00 10.89 ?  92  CYS   B SG   1 
ATOM   5334 H  H    . CYS   B 1 92  ? 47.905 -12.311 -4.029  1.00 12.32 ?  92  CYS   B H    1 
ATOM   5335 H  HA   . CYS   B 1 92  ? 47.069 -14.862 -4.474  1.00 11.92 ?  92  CYS   B HA   1 
ATOM   5336 H  HB2  . CYS   B 1 92  ? 49.210 -14.780 -3.537  1.00 12.36 ?  92  CYS   B HB2  1 
ATOM   5337 H  HB3  . CYS   B 1 92  ? 48.641 -13.932 -2.320  1.00 12.36 ?  92  CYS   B HB3  1 
ATOM   5338 H  HG   . CYS   B 1 92  ? 49.056 -16.466 -1.438  1.00 13.07 ?  92  CYS   B HG   1 
ATOM   5339 N  N    . LEU   B 1 93  ? 45.009 -14.729 -3.156  1.00 9.77  ?  93  LEU   B N    1 
ATOM   5340 C  CA   . LEU   B 1 93  ? 43.830 -14.736 -2.296  1.00 9.94  ?  93  LEU   B CA   1 
ATOM   5341 C  C    . LEU   B 1 93  ? 44.045 -15.799 -1.224  1.00 9.26  ?  93  LEU   B C    1 
ATOM   5342 O  O    . LEU   B 1 93  ? 44.009 -17.000 -1.513  1.00 10.07 ?  93  LEU   B O    1 
ATOM   5343 C  CB   . LEU   B 1 93  ? 42.568 -15.029 -3.105  1.00 10.56 ?  93  LEU   B CB   1 
ATOM   5344 C  CG   . LEU   B 1 93  ? 41.267 -15.042 -2.298  1.00 11.27 ?  93  LEU   B CG   1 
ATOM   5345 C  CD1  . LEU   B 1 93  ? 40.915 -13.645 -1.817  1.00 11.18 ?  93  LEU   B CD1  1 
ATOM   5346 C  CD2  . LEU   B 1 93  ? 40.131 -15.638 -3.111  1.00 11.54 ?  93  LEU   B CD2  1 
ATOM   5347 H  H    . LEU   B 1 93  ? 44.967 -15.308 -3.801  1.00 11.72 ?  93  LEU   B H    1 
ATOM   5348 H  HA   . LEU   B 1 93  ? 43.740 -13.873 -1.867  1.00 11.93 ?  93  LEU   B HA   1 
ATOM   5349 H  HB2  . LEU   B 1 93  ? 42.481 -14.340 -3.788  1.00 12.67 ?  93  LEU   B HB2  1 
ATOM   5350 H  HB3  . LEU   B 1 93  ? 42.663 -15.891 -3.524  1.00 12.67 ?  93  LEU   B HB3  1 
ATOM   5351 H  HG   . LEU   B 1 93  ? 41.392 -15.594 -1.517  1.00 13.52 ?  93  LEU   B HG   1 
ATOM   5352 H  HD11 . LEU   B 1 93  ? 40.063 -13.674 -1.362  1.00 13.42 ?  93  LEU   B HD11 1 
ATOM   5353 H  HD12 . LEU   B 1 93  ? 41.607 -13.334 -1.214  1.00 13.42 ?  93  LEU   B HD12 1 
ATOM   5354 H  HD13 . LEU   B 1 93  ? 40.860 -13.051 -2.587  1.00 13.42 ?  93  LEU   B HD13 1 
ATOM   5355 H  HD21 . LEU   B 1 93  ? 39.323 -15.632 -2.573  1.00 13.85 ?  93  LEU   B HD21 1 
ATOM   5356 H  HD22 . LEU   B 1 93  ? 39.999 -15.111 -3.913  1.00 13.85 ?  93  LEU   B HD22 1 
ATOM   5357 H  HD23 . LEU   B 1 93  ? 40.360 -16.552 -3.350  1.00 13.85 ?  93  LEU   B HD23 1 
ATOM   5358 N  N    . HIS   B 1 94  ? 44.329 -15.361 -0.005  1.00 9.55  ?  94  HIS   B N    1 
ATOM   5359 C  CA   . HIS   B 1 94  ? 44.547 -16.267 1.114   1.00 9.62  ?  94  HIS   B CA   1 
ATOM   5360 C  C    . HIS   B 1 94  ? 43.185 -16.622 1.695   1.00 10.07 ?  94  HIS   B C    1 
ATOM   5361 O  O    . HIS   B 1 94  ? 42.516 -15.746 2.246   1.00 11.42 ?  94  HIS   B O    1 
ATOM   5362 C  CB   . HIS   B 1 94  ? 45.420 -15.589 2.170   1.00 10.38 ?  94  HIS   B CB   1 
ATOM   5363 C  CG   . HIS   B 1 94  ? 46.809 -15.292 1.705   1.00 9.99  ?  94  HIS   B CG   1 
ATOM   5364 N  ND1  . HIS   B 1 94  ? 47.832 -16.213 1.790   1.00 10.34 ?  94  HIS   B ND1  1 
ATOM   5365 C  CD2  . HIS   B 1 94  ? 47.321 -14.188 1.113   1.00 10.33 ?  94  HIS   B CD2  1 
ATOM   5366 C  CE1  . HIS   B 1 94  ? 48.924 -15.665 1.281   1.00 10.32 ?  94  HIS   B CE1  1 
ATOM   5367 N  NE2  . HIS   B 1 94  ? 48.642 -14.439 0.866   1.00 10.63 ?  94  HIS   B NE2  1 
ATOM   5368 H  H    . HIS   B 1 94  ? 44.412 -14.526 0.195   1.00 11.46 ?  94  HIS   B H    1 
ATOM   5369 H  HA   . HIS   B 1 94  ? 44.981 -17.075 0.805   1.00 11.54 ?  94  HIS   B HA   1 
ATOM   5370 H  HB2  . HIS   B 1 94  ? 45.006 -14.751 2.420   1.00 12.46 ?  94  HIS   B HB2  1 
ATOM   5371 H  HB3  . HIS   B 1 94  ? 45.481 -16.176 2.936   1.00 12.46 ?  94  HIS   B HB3  1 
ATOM   5372 H  HD2  . HIS   B 1 94  ? 46.868 -13.406 0.915   1.00 12.39 ?  94  HIS   B HD2  1 
ATOM   5373 H  HE1  . HIS   B 1 94  ? 49.752 -16.088 1.221   1.00 12.38 ?  94  HIS   B HE1  1 
ATOM   5374 H  HE2  . HIS   B 1 94  ? 49.201 -13.903 0.498   1.00 12.75 ?  94  HIS   B HE2  1 
ATOM   5375 N  N    . VAL   B 1 95  ? 42.753 -17.876 1.549   1.00 10.01 ?  95  VAL   B N    1 
ATOM   5376 C  CA   . VAL   B 1 95  ? 41.423 -18.312 1.979   1.00 10.09 ?  95  VAL   B CA   1 
ATOM   5377 C  C    . VAL   B 1 95  ? 41.588 -19.348 3.079   1.00 10.23 ?  95  VAL   B C    1 
ATOM   5378 O  O    . VAL   B 1 95  ? 42.359 -20.301 2.923   1.00 10.95 ?  95  VAL   B O    1 
ATOM   5379 C  CB   . VAL   B 1 95  ? 40.606 -18.918 0.819   1.00 10.50 ?  95  VAL   B CB   1 
ATOM   5380 C  CG1  . VAL   B 1 95  ? 39.214 -19.366 1.299   1.00 11.87 ?  95  VAL   B CG1  1 
ATOM   5381 C  CG2  . VAL   B 1 95  ? 40.485 -17.936 -0.322  1.00 10.42 ?  95  VAL   B CG2  1 
ATOM   5382 H  H    . VAL   B 1 95  ? 43.220 -18.506 1.194   1.00 12.01 ?  95  VAL   B H    1 
ATOM   5383 H  HA   . VAL   B 1 95  ? 40.931 -17.557 2.339   1.00 12.10 ?  95  VAL   B HA   1 
ATOM   5384 H  HB   . VAL   B 1 95  ? 41.065 -19.698 0.486   1.00 12.60 ?  95  VAL   B HB   1 
ATOM   5385 H  HG11 . VAL   B 1 95  ? 38.660 -19.573 0.525   1.00 14.24 ?  95  VAL   B HG11 1 
ATOM   5386 H  HG12 . VAL   B 1 95  ? 39.304 -20.156 1.854   1.00 14.24 ?  95  VAL   B HG12 1 
ATOM   5387 H  HG13 . VAL   B 1 95  ? 38.802 -18.649 1.809   1.00 14.24 ?  95  VAL   B HG13 1 
ATOM   5388 H  HG21 . VAL   B 1 95  ? 39.915 -18.323 -1.007  1.00 12.51 ?  95  VAL   B HG21 1 
ATOM   5389 H  HG22 . VAL   B 1 95  ? 40.093 -17.114 0.009   1.00 12.51 ?  95  VAL   B HG22 1 
ATOM   5390 H  HG23 . VAL   B 1 95  ? 41.367 -17.766 -0.681  1.00 12.51 ?  95  VAL   B HG23 1 
ATOM   5391 N  N    . VAL   B 1 96  ? 40.861 -19.175 4.176   1.00 10.72 ?  96  VAL   B N    1 
ATOM   5392 C  CA   . VAL   B 1 96  ? 40.938 -20.089 5.315   1.00 11.21 ?  96  VAL   B CA   1 
ATOM   5393 C  C    . VAL   B 1 96  ? 39.749 -21.049 5.268   1.00 11.80 ?  96  VAL   B C    1 
ATOM   5394 O  O    . VAL   B 1 96  ? 38.632 -20.695 5.656   1.00 12.63 ?  96  VAL   B O    1 
ATOM   5395 C  CB   . VAL   B 1 96  ? 40.988 -19.337 6.649   1.00 11.70 ?  96  VAL   B CB   1 
ATOM   5396 C  CG1  . VAL   B 1 96  ? 41.159 -20.328 7.797   1.00 12.54 ?  96  VAL   B CG1  1 
ATOM   5397 C  CG2  . VAL   B 1 96  ? 42.102 -18.298 6.656   1.00 12.39 ?  96  VAL   B CG2  1 
ATOM   5398 H  H    . VAL   B 1 96  ? 40.303 -18.531 4.290   1.00 12.86 ?  96  VAL   B H    1 
ATOM   5399 H  HA   . VAL   B 1 96  ? 41.748 -20.619 5.243   1.00 13.45 ?  96  VAL   B HA   1 
ATOM   5400 H  HB   . VAL   B 1 96  ? 40.144 -18.878 6.781   1.00 14.04 ?  96  VAL   B HB   1 
ATOM   5401 H  HG11 . VAL   B 1 96  ? 41.346 -19.837 8.614   1.00 15.05 ?  96  VAL   B HG11 1 
ATOM   5402 H  HG12 . VAL   B 1 96  ? 40.343 -20.843 7.904   1.00 15.05 ?  96  VAL   B HG12 1 
ATOM   5403 H  HG13 . VAL   B 1 96  ? 41.901 -20.922 7.597   1.00 15.05 ?  96  VAL   B HG13 1 
ATOM   5404 H  HG21 . VAL   B 1 96  ? 42.147 -17.886 7.537   1.00 14.87 ?  96  VAL   B HG21 1 
ATOM   5405 H  HG22 . VAL   B 1 96  ? 42.944 -18.728 6.452   1.00 14.87 ?  96  VAL   B HG22 1 
ATOM   5406 H  HG23 . VAL   B 1 96  ? 41.906 -17.617 5.990   1.00 14.87 ?  96  VAL   B HG23 1 
ATOM   5407 N  N    . GLY   B 1 97  ? 39.983 -22.282 4.828   1.00 11.84 ?  97  GLY   B N    1 
ATOM   5408 C  CA   . GLY   B 1 97  ? 39.007 -23.334 4.987   1.00 12.64 ?  97  GLY   B CA   1 
ATOM   5409 C  C    . GLY   B 1 97  ? 39.136 -23.949 6.365   1.00 13.73 ?  97  GLY   B C    1 
ATOM   5410 O  O    . GLY   B 1 97  ? 40.179 -23.823 7.023   1.00 14.21 ?  97  GLY   B O    1 
ATOM   5411 H  H    . GLY   B 1 97  ? 40.708 -22.525 4.424   1.00 14.20 ?  97  GLY   B H    1 
ATOM   5412 H  HA2  . GLY   B 1 97  ? 38.114 -22.967 4.874   1.00 15.17 ?  97  GLY   B HA2  1 
ATOM   5413 H  HA3  . GLY   B 1 97  ? 39.147 -24.019 4.311   1.00 15.17 ?  97  GLY   B HA3  1 
ATOM   5414 N  N    . PRO   B 1 98  ? 38.090 -24.633 6.829   1.00 14.53 ?  98  PRO   B N    1 
ATOM   5415 C  CA   . PRO   B 1 98  ? 38.186 -25.325 8.117   1.00 15.29 ?  98  PRO   B CA   1 
ATOM   5416 C  C    . PRO   B 1 98  ? 39.211 -26.449 8.074   1.00 15.01 ?  98  PRO   B C    1 
ATOM   5417 O  O    . PRO   B 1 98  ? 39.315 -27.185 7.095   1.00 15.53 ?  98  PRO   B O    1 
ATOM   5418 C  CB   . PRO   B 1 98  ? 36.767 -25.864 8.333   1.00 15.46 ?  98  PRO   B CB   1 
ATOM   5419 C  CG   . PRO   B 1 98  ? 36.200 -26.003 6.969   1.00 15.22 ?  98  PRO   B CG   1 
ATOM   5420 C  CD   . PRO   B 1 98  ? 36.765 -24.825 6.206   1.00 14.60 ?  98  PRO   B CD   1 
ATOM   5421 H  HA   . PRO   B 1 98  ? 38.414 -24.700 8.818   1.00 18.34 ?  98  PRO   B HA   1 
ATOM   5422 H  HB2  . PRO   B 1 98  ? 36.812 -26.728 8.775   1.00 18.55 ?  98  PRO   B HB2  1 
ATOM   5423 H  HB3  . PRO   B 1 98  ? 36.254 -25.233 8.857   1.00 18.55 ?  98  PRO   B HB3  1 
ATOM   5424 H  HG2  . PRO   B 1 98  ? 36.491 -26.841 6.574   1.00 18.26 ?  98  PRO   B HG2  1 
ATOM   5425 H  HG3  . PRO   B 1 98  ? 35.233 -25.958 7.009   1.00 18.26 ?  98  PRO   B HG3  1 
ATOM   5426 H  HD2  . PRO   B 1 98  ? 36.850 -25.044 5.260   1.00 17.52 ?  98  PRO   B HD2  1 
ATOM   5427 H  HD3  . PRO   B 1 98  ? 36.211 -24.038 6.336   1.00 17.52 ?  98  PRO   B HD3  1 
ATOM   5428 N  N    . ASN   B 1 99  ? 39.968 -26.573 9.155   1.00 16.47 ?  99  ASN   B N    1 
ATOM   5429 C  CA   . ASN   B 1 99  ? 40.946 -27.645 9.319   1.00 17.62 ?  99  ASN   B CA   1 
ATOM   5430 C  C    . ASN   B 1 99  ? 40.319 -28.725 10.199  1.00 20.53 ?  99  ASN   B C    1 
ATOM   5431 O  O    . ASN   B 1 99  ? 40.245 -28.578 11.421  1.00 21.42 ?  99  ASN   B O    1 
ATOM   5432 C  CB   . ASN   B 1 99  ? 42.220 -27.086 9.939   1.00 17.84 ?  99  ASN   B CB   1 
ATOM   5433 C  CG   . ASN   B 1 99  ? 43.350 -28.089 9.953   1.00 18.63 ?  99  ASN   B CG   1 
ATOM   5434 O  OD1  . ASN   B 1 99  ? 43.129 -29.278 10.141  1.00 19.30 ?  99  ASN   B OD1  1 
ATOM   5435 N  ND2  . ASN   B 1 99  ? 44.568 -27.613 9.754   1.00 18.73 ?  99  ASN   B ND2  1 
ATOM   5436 H  H    . ASN   B 1 99  ? 39.932 -26.035 9.820   1.00 19.77 ?  99  ASN   B H    1 
ATOM   5437 H  HA   . ASN   B 1 99  ? 41.157 -28.036 8.457   1.00 21.14 ?  99  ASN   B HA   1 
ATOM   5438 H  HB2  . ASN   B 1 99  ? 42.502 -26.316 9.431   1.00 21.41 ?  99  ASN   B HB2  1 
ATOM   5439 H  HB3  . ASN   B 1 99  ? 42.030 -26.832 10.858  1.00 21.41 ?  99  ASN   B HB3  1 
ATOM   5440 H  HD21 . ASN   B 1 99  ? 45.242 -28.143 9.749   1.00 22.47 ?  99  ASN   B HD21 1 
ATOM   5441 H  HD22 . ASN   B 1 99  ? 44.677 -26.770 9.627   1.00 22.47 ?  99  ASN   B HD22 1 
ATOM   5442 N  N    A VAL   B 1 100 ? 39.847 -29.807 9.571   0.64 22.29 ?  100 VAL   B N    1 
ATOM   5443 N  N    B VAL   B 1 100 ? 39.864 -29.810 9.565   0.36 22.38 ?  100 VAL   B N    1 
ATOM   5444 C  CA   A VAL   B 1 100 ? 39.234 -30.898 10.328  0.64 25.00 ?  100 VAL   B CA   1 
ATOM   5445 C  CA   B VAL   B 1 100 ? 39.241 -30.912 10.296  0.36 24.70 ?  100 VAL   B CA   1 
ATOM   5446 C  C    A VAL   B 1 100 ? 40.246 -31.561 11.254  0.64 25.64 ?  100 VAL   B C    1 
ATOM   5447 C  C    B VAL   B 1 100 ? 40.240 -31.581 11.230  0.36 25.46 ?  100 VAL   B C    1 
ATOM   5448 O  O    A VAL   B 1 100 ? 39.881 -32.067 12.322  0.64 26.24 ?  100 VAL   B O    1 
ATOM   5449 O  O    B VAL   B 1 100 ? 39.860 -32.107 12.284  0.36 25.76 ?  100 VAL   B O    1 
ATOM   5450 C  CB   A VAL   B 1 100 ? 38.572 -31.911 9.371   0.64 27.25 ?  100 VAL   B CB   1 
ATOM   5451 C  CB   B VAL   B 1 100 ? 38.613 -31.912 9.305   0.36 26.33 ?  100 VAL   B CB   1 
ATOM   5452 C  CG1  A VAL   B 1 100 ? 38.087 -33.135 10.135  0.64 28.25 ?  100 VAL   B CG1  1 
ATOM   5453 C  CG1  B VAL   B 1 100 ? 38.112 -33.152 10.030  0.36 27.00 ?  100 VAL   B CG1  1 
ATOM   5454 C  CG2  A VAL   B 1 100 ? 37.415 -31.258 8.633   0.64 27.81 ?  100 VAL   B CG2  1 
ATOM   5455 C  CG2  B VAL   B 1 100 ? 37.480 -31.249 8.536   0.36 26.77 ?  100 VAL   B CG2  1 
ATOM   5456 H  H    A VAL   B 1 100 ? 39.855 -29.921 8.717   0.64 26.74 ?  100 VAL   B H    1 
ATOM   5457 H  H    B VAL   B 1 100 ? 39.898 -29.927 8.714   0.36 26.86 ?  100 VAL   B H    1 
ATOM   5458 H  HA   A VAL   B 1 100 ? 38.527 -30.526 10.880  0.64 30.00 ?  100 VAL   B HA   1 
ATOM   5459 H  HA   B VAL   B 1 100 ? 38.522 -30.554 10.840  0.36 29.64 ?  100 VAL   B HA   1 
ATOM   5460 H  HB   A VAL   B 1 100 ? 39.224 -32.206 8.718   0.64 32.70 ?  100 VAL   B HB   1 
ATOM   5461 H  HB   B VAL   B 1 100 ? 39.286 -32.192 8.666   0.36 31.59 ?  100 VAL   B HB   1 
ATOM   5462 H  HG11 A VAL   B 1 100 ? 37.490 -33.646 9.563   0.64 33.90 ?  100 VAL   B HG11 1 
ATOM   5463 H  HG11 B VAL   B 1 100 ? 37.535 -33.655 9.431   0.36 32.40 ?  100 VAL   B HG11 1 
ATOM   5464 H  HG12 A VAL   B 1 100 ? 38.849 -33.682 10.383  0.64 33.90 ?  100 VAL   B HG12 1 
ATOM   5465 H  HG12 B VAL   B 1 100 ? 38.870 -33.698 10.290  0.36 32.40 ?  100 VAL   B HG12 1 
ATOM   5466 H  HG13 A VAL   B 1 100 ? 37.611 -32.846 10.929  0.64 33.90 ?  100 VAL   B HG13 1 
ATOM   5467 H  HG13 B VAL   B 1 100 ? 37.612 -32.879 10.814  0.36 32.40 ?  100 VAL   B HG13 1 
ATOM   5468 H  HG21 A VAL   B 1 100 ? 37.016 -31.908 8.033   0.64 33.37 ?  100 VAL   B HG21 1 
ATOM   5469 H  HG21 B VAL   B 1 100 ? 37.090 -31.896 7.928   0.36 32.13 ?  100 VAL   B HG21 1 
ATOM   5470 H  HG22 A VAL   B 1 100 ? 36.756 -30.959 9.280   0.64 33.37 ?  100 VAL   B HG22 1 
ATOM   5471 H  HG22 B VAL   B 1 100 ? 36.810 -30.940 9.166   0.36 32.13 ?  100 VAL   B HG22 1 
ATOM   5472 H  HG23 A VAL   B 1 100 ? 37.750 -30.503 8.128   0.64 33.37 ?  100 VAL   B HG23 1 
ATOM   5473 H  HG23 B VAL   B 1 100 ? 37.836 -30.498 8.036   0.36 32.13 ?  100 VAL   B HG23 1 
ATOM   5474 N  N    . ASN   B 1 101 ? 41.523 -31.590 10.862  1.00 25.98 ?  101 ASN   B N    1 
ATOM   5475 C  CA   . ASN   B 1 101 ? 42.555 -32.127 11.747  1.00 28.13 ?  101 ASN   B CA   1 
ATOM   5476 C  C    . ASN   B 1 101 ? 42.738 -31.285 13.003  1.00 31.40 ?  101 ASN   B C    1 
ATOM   5477 O  O    . ASN   B 1 101 ? 43.362 -31.756 13.962  1.00 32.15 ?  101 ASN   B O    1 
ATOM   5478 C  CB   . ASN   B 1 101 ? 43.885 -32.273 11.003  1.00 27.44 ?  101 ASN   B CB   1 
ATOM   5479 C  CG   . ASN   B 1 101 ? 43.879 -33.432 10.023  1.00 26.74 ?  101 ASN   B CG   1 
ATOM   5480 O  OD1  . ASN   B 1 101 ? 43.221 -34.440 10.250  1.00 27.47 ?  101 ASN   B OD1  1 
ATOM   5481 N  ND2  . ASN   B 1 101 ? 44.607 -33.287 8.925   1.00 26.02 ?  101 ASN   B ND2  1 
ATOM   5482 H  H    A ASN   B 1 101 ? 41.808 -31.324 10.095  0.64 31.17 ?  101 ASN   B H    1 
ATOM   5483 H  H    B ASN   B 1 101 ? 41.815 -31.302 10.106  0.36 31.17 ?  101 ASN   B H    1 
ATOM   5484 H  HA   . ASN   B 1 101 ? 42.282 -33.012 12.030  1.00 33.76 ?  101 ASN   B HA   1 
ATOM   5485 H  HB2  . ASN   B 1 101 ? 44.066 -31.464 10.504  1.00 32.93 ?  101 ASN   B HB2  1 
ATOM   5486 H  HB3  . ASN   B 1 101 ? 44.593 -32.429 11.651  1.00 32.93 ?  101 ASN   B HB3  1 
ATOM   5487 H  HD21 . ASN   B 1 101 ? 44.633 -33.917 8.341   1.00 31.22 ?  101 ASN   B HD21 1 
ATOM   5488 H  HD22 . ASN   B 1 101 ? 45.047 -32.560 8.795   1.00 31.22 ?  101 ASN   B HD22 1 
ATOM   5489 N  N    A LYS   B 1 102 ? 42.221 -30.055 13.015  0.64 33.15 ?  102 LYS   B N    1 
ATOM   5490 N  N    B LYS   B 1 102 ? 42.219 -30.057 13.019  0.36 33.15 ?  102 LYS   B N    1 
ATOM   5491 C  CA   A LYS   B 1 102 ? 42.195 -29.210 14.202  0.64 35.12 ?  102 LYS   B CA   1 
ATOM   5492 C  CA   B LYS   B 1 102 ? 42.197 -29.219 14.210  0.36 34.96 ?  102 LYS   B CA   1 
ATOM   5493 C  C    A LYS   B 1 102 ? 40.821 -29.177 14.861  0.64 34.40 ?  102 LYS   B C    1 
ATOM   5494 C  C    B LYS   B 1 102 ? 40.824 -29.184 14.869  0.36 34.43 ?  102 LYS   B C    1 
ATOM   5495 O  O    A LYS   B 1 102 ? 40.607 -28.384 15.783  0.64 34.71 ?  102 LYS   B O    1 
ATOM   5496 O  O    B LYS   B 1 102 ? 40.615 -28.403 15.802  0.36 34.74 ?  102 LYS   B O    1 
ATOM   5497 C  CB   A LYS   B 1 102 ? 42.612 -27.781 13.851  0.64 37.82 ?  102 LYS   B CB   1 
ATOM   5498 C  CB   B LYS   B 1 102 ? 42.637 -27.794 13.868  0.36 37.18 ?  102 LYS   B CB   1 
ATOM   5499 C  CG   A LYS   B 1 102 ? 44.075 -27.592 13.495  0.64 40.41 ?  102 LYS   B CG   1 
ATOM   5500 C  CG   B LYS   B 1 102 ? 44.102 -27.649 13.495  0.36 39.23 ?  102 LYS   B CG   1 
ATOM   5501 C  CD   A LYS   B 1 102 ? 44.328 -26.140 13.112  0.64 42.59 ?  102 LYS   B CD   1 
ATOM   5502 C  CD   B LYS   B 1 102 ? 44.391 -26.232 13.024  0.36 40.92 ?  102 LYS   B CD   1 
ATOM   5503 C  CE   A LYS   B 1 102 ? 45.791 -25.865 12.819  0.64 44.19 ?  102 LYS   B CE   1 
ATOM   5504 C  CE   B LYS   B 1 102 ? 45.877 -25.984 12.835  0.36 42.19 ?  102 LYS   B CE   1 
ATOM   5505 N  NZ   A LYS   B 1 102 ? 46.004 -24.445 12.416  0.64 45.12 ?  102 LYS   B NZ   1 
ATOM   5506 N  NZ   B LYS   B 1 102 ? 46.136 -24.593 12.366  0.36 42.93 ?  102 LYS   B NZ   1 
ATOM   5507 H  H    A LYS   B 1 102 ? 41.872 -29.679 12.326  0.64 39.78 ?  102 LYS   B H    1 
ATOM   5508 H  H    B LYS   B 1 102 ? 41.865 -29.681 12.331  0.36 39.78 ?  102 LYS   B H    1 
ATOM   5509 H  HA   A LYS   B 1 102 ? 42.831 -29.554 14.848  0.64 42.14 ?  102 LYS   B HA   1 
ATOM   5510 H  HA   B LYS   B 1 102 ? 42.828 -29.575 14.853  0.36 41.95 ?  102 LYS   B HA   1 
ATOM   5511 H  HB2  A LYS   B 1 102 ? 42.088 -27.485 13.092  0.64 45.38 ?  102 LYS   B HB2  1 
ATOM   5512 H  HB2  B LYS   B 1 102 ? 42.112 -27.478 13.118  0.36 44.61 ?  102 LYS   B HB2  1 
ATOM   5513 H  HB3  A LYS   B 1 102 ? 42.426 -27.210 14.614  0.64 45.38 ?  102 LYS   B HB3  1 
ATOM   5514 H  HB3  B LYS   B 1 102 ? 42.476 -27.227 14.640  0.36 44.61 ?  102 LYS   B HB3  1 
ATOM   5515 H  HG2  A LYS   B 1 102 ? 44.629 -27.811 14.261  0.64 48.49 ?  102 LYS   B HG2  1 
ATOM   5516 H  HG2  B LYS   B 1 102 ? 44.655 -27.834 14.271  0.36 47.08 ?  102 LYS   B HG2  1 
ATOM   5517 H  HG3  A LYS   B 1 102 ? 44.302 -28.155 12.738  0.64 48.49 ?  102 LYS   B HG3  1 
ATOM   5518 H  HG3  B LYS   B 1 102 ? 44.315 -28.262 12.774  0.36 47.08 ?  102 LYS   B HG3  1 
ATOM   5519 H  HD2  A LYS   B 1 102 ? 43.815 -25.928 12.316  0.64 51.11 ?  102 LYS   B HD2  1 
ATOM   5520 H  HD2  B LYS   B 1 102 ? 43.949 -26.084 12.173  0.36 49.11 ?  102 LYS   B HD2  1 
ATOM   5521 H  HD3  A LYS   B 1 102 ? 44.054 -25.567 13.846  0.64 51.11 ?  102 LYS   B HD3  1 
ATOM   5522 H  HD3  B LYS   B 1 102 ? 44.062 -25.604 13.685  0.36 49.11 ?  102 LYS   B HD3  1 
ATOM   5523 H  HE2  A LYS   B 1 102 ? 46.316 -26.037 13.617  0.64 53.03 ?  102 LYS   B HE2  1 
ATOM   5524 H  HE2  B LYS   B 1 102 ? 46.335 -26.110 13.681  0.36 50.63 ?  102 LYS   B HE2  1 
ATOM   5525 H  HE3  A LYS   B 1 102 ? 46.086 -26.436 12.093  0.64 53.03 ?  102 LYS   B HE3  1 
ATOM   5526 H  HE3  B LYS   B 1 102 ? 46.224 -26.599 12.170  0.36 50.63 ?  102 LYS   B HE3  1 
ATOM   5527 H  HZ1  A LYS   B 1 102 ? 46.866 -24.302 12.249  0.64 54.14 ?  102 LYS   B HZ1  1 
ATOM   5528 H  HZ1  B LYS   B 1 102 ? 47.010 -24.465 12.261  0.36 51.52 ?  102 LYS   B HZ1  1 
ATOM   5529 H  HZ2  A LYS   B 1 102 ? 45.533 -24.263 11.683  0.64 54.14 ?  102 LYS   B HZ2  1 
ATOM   5530 H  HZ2  B LYS   B 1 102 ? 45.727 -24.454 11.588  0.36 51.52 ?  102 LYS   B HZ2  1 
ATOM   5531 H  HZ3  A LYS   B 1 102 ? 45.743 -23.900 13.070  0.64 54.14 ?  102 LYS   B HZ3  1 
ATOM   5532 H  HZ3  B LYS   B 1 102 ? 45.828 -24.009 12.963  0.36 51.52 ?  102 LYS   B HZ3  1 
ATOM   5533 N  N    . GLY   B 1 103 ? 39.883 -30.000 14.399  1.00 33.66 ?  103 GLY   B N    1 
ATOM   5534 C  CA   . GLY   B 1 103 ? 38.556 -30.045 14.980  1.00 33.00 ?  103 GLY   B CA   1 
ATOM   5535 C  C    . GLY   B 1 103 ? 37.607 -28.964 14.515  1.00 31.78 ?  103 GLY   B C    1 
ATOM   5536 O  O    . GLY   B 1 103 ? 36.516 -28.837 15.083  1.00 32.05 ?  103 GLY   B O    1 
ATOM   5537 H  H    A GLY   B 1 103 ? 39.994 -30.543 13.743  0.64 40.39 ?  103 GLY   B H    1 
ATOM   5538 H  H    B GLY   B 1 103 ? 39.992 -30.538 13.739  0.36 40.39 ?  103 GLY   B H    1 
ATOM   5539 H  HA2  . GLY   B 1 103 ? 38.153 -30.903 14.774  1.00 39.60 ?  103 GLY   B HA2  1 
ATOM   5540 H  HA3  . GLY   B 1 103 ? 38.632 -29.976 15.944  1.00 39.60 ?  103 GLY   B HA3  1 
ATOM   5541 N  N    A GLU   B 1 104 ? 37.988 -28.176 13.513  0.64 30.60 ?  104 GLU   B N    1 
ATOM   5542 N  N    B GLU   B 1 104 ? 37.971 -28.193 13.496  0.36 31.03 ?  104 GLU   B N    1 
ATOM   5543 C  CA   A GLU   B 1 104 ? 37.151 -27.080 13.053  0.64 29.29 ?  104 GLU   B CA   1 
ATOM   5544 C  CA   B GLU   B 1 104 ? 37.114 -27.117 13.024  0.36 30.09 ?  104 GLU   B CA   1 
ATOM   5545 C  C    A GLU   B 1 104 ? 35.966 -27.607 12.243  0.64 29.54 ?  104 GLU   B C    1 
ATOM   5546 C  C    B GLU   B 1 104 ? 35.955 -27.667 12.198  0.36 30.10 ?  104 GLU   B C    1 
ATOM   5547 O  O    A GLU   B 1 104 ? 36.004 -28.697 11.665  0.64 30.06 ?  104 GLU   B O    1 
ATOM   5548 O  O    B GLU   B 1 104 ? 36.035 -28.753 11.614  0.36 30.33 ?  104 GLU   B O    1 
ATOM   5549 C  CB   A GLU   B 1 104 ? 37.986 -26.085 12.242  0.64 28.13 ?  104 GLU   B CB   1 
ATOM   5550 C  CB   B GLU   B 1 104 ? 37.933 -26.105 12.223  0.36 29.30 ?  104 GLU   B CB   1 
ATOM   5551 C  CG   A GLU   B 1 104 ? 39.095 -25.446 13.071  0.64 26.96 ?  104 GLU   B CG   1 
ATOM   5552 C  CG   B GLU   B 1 104 ? 39.023 -25.453 13.065  0.36 28.53 ?  104 GLU   B CG   1 
ATOM   5553 C  CD   A GLU   B 1 104 ? 40.024 -24.556 12.272  0.64 25.73 ?  104 GLU   B CD   1 
ATOM   5554 C  CD   B GLU   B 1 104 ? 39.975 -24.596 12.256  0.36 27.81 ?  104 GLU   B CD   1 
ATOM   5555 O  OE1  A GLU   B 1 104 ? 40.016 -24.620 11.025  0.64 24.03 ?  104 GLU   B OE1  1 
ATOM   5556 O  OE1  B GLU   B 1 104 ? 39.913 -24.632 11.010  0.36 27.07 ?  104 GLU   B OE1  1 
ATOM   5557 O  OE2  A GLU   B 1 104 ? 40.775 -23.786 12.907  0.64 25.92 -1 104 GLU   B OE2  1 
ATOM   5558 O  OE2  B GLU   B 1 104 ? 40.791 -23.884 12.877  0.36 27.77 -1 104 GLU   B OE2  1 
ATOM   5559 H  H    A GLU   B 1 104 ? 38.732 -28.251 13.090  0.64 36.73 ?  104 GLU   B H    1 
ATOM   5560 H  H    B GLU   B 1 104 ? 38.711 -28.270 13.064  0.36 37.24 ?  104 GLU   B H    1 
ATOM   5561 H  HA   A GLU   B 1 104 ? 36.801 -26.608 13.825  0.64 35.15 ?  104 GLU   B HA   1 
ATOM   5562 H  HA   B GLU   B 1 104 ? 36.740 -26.658 13.789  0.36 36.11 ?  104 GLU   B HA   1 
ATOM   5563 H  HB2  A GLU   B 1 104 ? 38.398 -26.548 11.496  0.64 33.76 ?  104 GLU   B HB2  1 
ATOM   5564 H  HB2  B GLU   B 1 104 ? 38.356 -26.555 11.476  0.36 35.16 ?  104 GLU   B HB2  1 
ATOM   5565 H  HB3  A GLU   B 1 104 ? 37.408 -25.376 11.916  0.64 33.76 ?  104 GLU   B HB3  1 
ATOM   5566 H  HB3  B GLU   B 1 104 ? 37.343 -25.405 11.899  0.36 35.16 ?  104 GLU   B HB3  1 
ATOM   5567 H  HG2  A GLU   B 1 104 ? 38.695 -24.903 13.769  0.64 32.35 ?  104 GLU   B HG2  1 
ATOM   5568 H  HG2  B GLU   B 1 104 ? 38.606 -24.888 13.735  0.36 34.24 ?  104 GLU   B HG2  1 
ATOM   5569 H  HG3  A GLU   B 1 104 ? 39.637 -26.143 13.469  0.64 32.35 ?  104 GLU   B HG3  1 
ATOM   5570 H  HG3  B GLU   B 1 104 ? 39.543 -26.148 13.500  0.36 34.24 ?  104 GLU   B HG3  1 
ATOM   5571 N  N    A ASP   B 1 105 ? 34.900 -26.809 12.213  0.64 29.33 ?  105 ASP   B N    1 
ATOM   5572 N  N    B ASP   B 1 105 ? 34.865 -26.902 12.160  0.36 29.84 ?  105 ASP   B N    1 
ATOM   5573 C  CA   A ASP   B 1 105 ? 33.623 -27.259 11.669  0.64 29.82 ?  105 ASP   B CA   1 
ATOM   5574 C  CA   B ASP   B 1 105 ? 33.603 -27.373 11.599  0.36 29.84 ?  105 ASP   B CA   1 
ATOM   5575 C  C    A ASP   B 1 105 ? 33.678 -27.311 10.146  0.64 27.86 ?  105 ASP   B C    1 
ATOM   5576 C  C    B ASP   B 1 105 ? 33.678 -27.387 10.076  0.36 28.70 ?  105 ASP   B C    1 
ATOM   5577 O  O    A ASP   B 1 105 ? 33.835 -26.279 9.487   0.64 26.89 ?  105 ASP   B O    1 
ATOM   5578 O  O    B ASP   B 1 105 ? 33.876 -26.342 9.446   0.36 28.27 ?  105 ASP   B O    1 
ATOM   5579 C  CB   A ASP   B 1 105 ? 32.510 -26.316 12.123  0.64 32.66 ?  105 ASP   B CB   1 
ATOM   5580 C  CB   B ASP   B 1 105 ? 32.458 -26.477 12.071  0.36 31.01 ?  105 ASP   B CB   1 
ATOM   5581 C  CG   A ASP   B 1 105 ? 31.136 -26.779 11.680  0.64 35.07 ?  105 ASP   B CG   1 
ATOM   5582 C  CG   B ASP   B 1 105 ? 31.092 -27.050 11.733  0.36 32.00 ?  105 ASP   B CG   1 
ATOM   5583 O  OD1  A ASP   B 1 105 ? 31.030 -27.893 11.125  0.64 35.40 ?  105 ASP   B OD1  1 
ATOM   5584 O  OD1  B ASP   B 1 105 ? 31.034 -28.067 11.010  0.36 32.20 ?  105 ASP   B OD1  1 
ATOM   5585 O  OD2  A ASP   B 1 105 ? 30.160 -26.025 11.882  0.64 36.46 -1 105 ASP   B OD2  1 
ATOM   5586 O  OD2  B ASP   B 1 105 ? 30.076 -26.491 12.199  0.36 32.35 -1 105 ASP   B OD2  1 
ATOM   5587 H  H    A ASP   B 1 105 ? 34.892 -26.000 12.505  0.64 35.20 ?  105 ASP   B H    1 
ATOM   5588 H  H    B ASP   B 1 105 ? 34.832 -26.096 12.455  0.36 35.80 ?  105 ASP   B H    1 
ATOM   5589 H  HA   A ASP   B 1 105 ? 33.427 -28.149 12.002  0.64 35.79 ?  105 ASP   B HA   1 
ATOM   5590 H  HA   B ASP   B 1 105 ? 33.424 -28.276 11.905  0.36 35.81 ?  105 ASP   B HA   1 
ATOM   5591 H  HB2  A ASP   B 1 105 ? 32.524 -26.250 13.093  0.64 39.19 ?  105 ASP   B HB2  1 
ATOM   5592 H  HB2  B ASP   B 1 105 ? 32.510 -26.375 13.035  0.36 37.21 ?  105 ASP   B HB2  1 
ATOM   5593 H  HB3  A ASP   B 1 105 ? 32.654 -25.442 11.730  0.64 39.19 ?  105 ASP   B HB3  1 
ATOM   5594 H  HB3  B ASP   B 1 105 ? 32.538 -25.607 11.644  0.36 37.21 ?  105 ASP   B HB3  1 
ATOM   5595 N  N    A ILE   B 1 106 ? 33.506 -28.514 9.591   0.64 27.37 ?  106 ILE   B N    1 
ATOM   5596 N  N    B ILE   B 1 106 ? 33.500 -28.573 9.488   0.36 28.09 ?  106 ILE   B N    1 
ATOM   5597 C  CA   A ILE   B 1 106 ? 33.504 -28.698 8.145   0.64 26.29 ?  106 ILE   B CA   1 
ATOM   5598 C  CA   B ILE   B 1 106 ? 33.512 -28.721 8.038   0.36 27.43 ?  106 ILE   B CA   1 
ATOM   5599 C  C    A ILE   B 1 106 ? 32.410 -27.878 7.469   0.64 24.80 ?  106 ILE   B C    1 
ATOM   5600 C  C    B ILE   B 1 106 ? 32.412 -27.900 7.376   0.36 26.53 ?  106 ILE   B C    1 
ATOM   5601 O  O    A ILE   B 1 106 ? 32.507 -27.584 6.272   0.64 24.14 ?  106 ILE   B O    1 
ATOM   5602 O  O    B ILE   B 1 106 ? 32.498 -27.598 6.181   0.36 26.15 ?  106 ILE   B O    1 
ATOM   5603 C  CB   A ILE   B 1 106 ? 33.391 -30.206 7.819   0.64 27.01 ?  106 ILE   B CB   1 
ATOM   5604 C  CB   B ILE   B 1 106 ? 33.421 -30.222 7.673   0.36 27.76 ?  106 ILE   B CB   1 
ATOM   5605 C  CG1  A ILE   B 1 106 ? 33.646 -30.469 6.335   0.64 27.58 ?  106 ILE   B CG1  1 
ATOM   5606 C  CG1  B ILE   B 1 106 ? 33.701 -30.444 6.185   0.36 28.04 ?  106 ILE   B CG1  1 
ATOM   5607 C  CG2  A ILE   B 1 106 ? 32.026 -30.746 8.232   0.64 27.69 ?  106 ILE   B CG2  1 
ATOM   5608 C  CG2  B ILE   B 1 106 ? 32.055 -30.784 8.045   0.36 28.11 ?  106 ILE   B CG2  1 
ATOM   5609 C  CD1  A ILE   B 1 106 ? 35.015 -30.035 5.873   0.64 27.69 ?  106 ILE   B CD1  1 
ATOM   5610 C  CD1  B ILE   B 1 106 ? 35.062 -29.962 5.746   0.36 28.18 ?  106 ILE   B CD1  1 
ATOM   5611 H  H    A ILE   B 1 106 ? 33.387 -29.238 10.037  0.64 32.84 ?  106 ILE   B H    1 
ATOM   5612 H  H    B ILE   B 1 106 ? 33.376 -29.308 9.913   0.36 33.71 ?  106 ILE   B H    1 
ATOM   5613 H  HA   A ILE   B 1 106 ? 34.352 -28.385 7.803   0.64 31.55 ?  106 ILE   B HA   1 
ATOM   5614 H  HA   B ILE   B 1 106 ? 34.356 -28.387 7.706   0.36 32.91 ?  106 ILE   B HA   1 
ATOM   5615 H  HB   A ILE   B 1 106 ? 34.063 -30.677 8.331   0.64 32.41 ?  106 ILE   B HB   1 
ATOM   5616 H  HB   B ILE   B 1 106 ? 34.092 -30.700 8.183   0.36 33.31 ?  106 ILE   B HB   1 
ATOM   5617 H  HG12 A ILE   B 1 106 ? 33.570 -31.423 6.169   0.64 33.10 ?  106 ILE   B HG12 1 
ATOM   5618 H  HG12 B ILE   B 1 106 ? 33.653 -31.396 5.997   0.36 33.65 ?  106 ILE   B HG12 1 
ATOM   5619 H  HG13 A ILE   B 1 106 ? 32.989 -29.991 5.809   0.64 33.10 ?  106 ILE   B HG13 1 
ATOM   5620 H  HG13 B ILE   B 1 106 ? 33.035 -29.974 5.663   0.36 33.65 ?  106 ILE   B HG13 1 
ATOM   5621 H  HG21 A ILE   B 1 106 ? 32.031 -31.713 8.147   0.64 33.23 ?  106 ILE   B HG21 1 
ATOM   5622 H  HG21 B ILE   B 1 106 ? 32.078 -31.750 7.963   0.36 33.74 ?  106 ILE   B HG21 1 
ATOM   5623 H  HG22 A ILE   B 1 106 ? 31.853 -30.499 9.155   0.64 33.23 ?  106 ILE   B HG22 1 
ATOM   5624 H  HG22 B ILE   B 1 106 ? 31.851 -30.536 8.961   0.36 33.74 ?  106 ILE   B HG22 1 
ATOM   5625 H  HG23 A ILE   B 1 106 ? 31.344 -30.368 7.656   0.64 33.23 ?  106 ILE   B HG23 1 
ATOM   5626 H  HG23 B ILE   B 1 106 ? 31.386 -30.417 7.447   0.36 33.74 ?  106 ILE   B HG23 1 
ATOM   5627 H  HD11 A ILE   B 1 106 ? 35.204 -30.447 5.016   0.64 33.23 ?  106 ILE   B HD11 1 
ATOM   5628 H  HD11 B ILE   B 1 106 ? 35.274 -30.358 4.888   0.36 33.81 ?  106 ILE   B HD11 1 
ATOM   5629 H  HD12 A ILE   B 1 106 ? 35.028 -29.068 5.783   0.64 33.23 ?  106 ILE   B HD12 1 
ATOM   5630 H  HD12 B ILE   B 1 106 ? 35.043 -28.995 5.668   0.36 33.81 ?  106 ILE   B HD12 1 
ATOM   5631 H  HD13 A ILE   B 1 106 ? 35.675 -30.317 6.527   0.64 33.23 ?  106 ILE   B HD13 1 
ATOM   5632 H  HD13 B ILE   B 1 106 ? 35.720 -30.230 6.406   0.36 33.81 ?  106 ILE   B HD13 1 
ATOM   5633 N  N    A GLN   B 1 107 ? 31.372 -27.483 8.212   0.64 25.30 ?  107 GLN   B N    1 
ATOM   5634 N  N    B GLN   B 1 107 ? 31.374 -27.526 8.128   0.36 26.48 ?  107 GLN   B N    1 
ATOM   5635 C  CA   A GLN   B 1 107 ? 30.289 -26.707 7.617   0.64 25.85 ?  107 GLN   B CA   1 
ATOM   5636 C  CA   B GLN   B 1 107 ? 30.292 -26.723 7.567   0.36 26.48 ?  107 GLN   B CA   1 
ATOM   5637 C  C    A GLN   B 1 107 ? 30.771 -25.361 7.098   0.64 23.69 ?  107 GLN   B C    1 
ATOM   5638 C  C    B GLN   B 1 107 ? 30.768 -25.353 7.094   0.36 24.11 ?  107 GLN   B C    1 
ATOM   5639 O  O    A GLN   B 1 107 ? 30.132 -24.786 6.213   0.64 24.27 ?  107 GLN   B O    1 
ATOM   5640 O  O    B GLN   B 1 107 ? 30.110 -24.745 6.243   0.36 24.48 ?  107 GLN   B O    1 
ATOM   5641 C  CB   A GLN   B 1 107 ? 29.167 -26.504 8.641   0.64 29.49 ?  107 GLN   B CB   1 
ATOM   5642 C  CB   B GLN   B 1 107 ? 29.169 -26.574 8.598   0.36 29.14 ?  107 GLN   B CB   1 
ATOM   5643 C  CG   A GLN   B 1 107 ? 27.847 -26.001 8.057   0.64 33.02 ?  107 GLN   B CG   1 
ATOM   5644 C  CG   B GLN   B 1 107 ? 27.840 -26.090 8.027   0.36 31.66 ?  107 GLN   B CG   1 
ATOM   5645 C  CD   A GLN   B 1 107 ? 27.781 -24.488 7.955   0.64 35.76 ?  107 GLN   B CD   1 
ATOM   5646 C  CD   B GLN   B 1 107 ? 27.713 -24.577 8.020   0.36 33.62 ?  107 GLN   B CD   1 
ATOM   5647 O  OE1  A GLN   B 1 107 ? 28.616 -23.777 8.515   0.64 36.82 ?  107 GLN   B OE1  1 
ATOM   5648 O  OE1  B GLN   B 1 107 ? 28.530 -23.869 8.610   0.36 34.28 ?  107 GLN   B OE1  1 
ATOM   5649 N  NE2  A GLN   B 1 107 ? 26.779 -23.987 7.237   0.64 36.65 ?  107 GLN   B NE2  1 
ATOM   5650 N  NE2  B GLN   B 1 107 ? 26.680 -24.074 7.352   0.36 34.33 ?  107 GLN   B NE2  1 
ATOM   5651 H  H    A GLN   B 1 107 ? 31.284 -27.626 9.052   0.64 30.36 ?  107 GLN   B H    1 
ATOM   5652 H  H    B GLN   B 1 107 ? 31.272 -27.730 8.956   0.36 31.78 ?  107 GLN   B H    1 
ATOM   5653 H  HA   A GLN   B 1 107 ? 29.922 -27.203 6.870   0.64 31.02 ?  107 GLN   B HA   1 
ATOM   5654 H  HA   B GLN   B 1 107 ? 29.924 -27.192 6.801   0.36 31.77 ?  107 GLN   B HA   1 
ATOM   5655 H  HB2  A GLN   B 1 107 ? 28.990 -27.352 9.068   0.64 35.39 ?  107 GLN   B HB2  1 
ATOM   5656 H  HB2  B GLN   B 1 107 ? 29.010 -27.436 9.009   0.36 34.97 ?  107 GLN   B HB2  1 
ATOM   5657 H  HB3  A GLN   B 1 107 ? 29.462 -25.859 9.302   0.64 35.39 ?  107 GLN   B HB3  1 
ATOM   5658 H  HB3  B GLN   B 1 107 ? 29.450 -25.939 9.276   0.36 34.97 ?  107 GLN   B HB3  1 
ATOM   5659 H  HG2  A GLN   B 1 107 ? 27.734 -26.363 7.165   0.64 39.62 ?  107 GLN   B HG2  1 
ATOM   5660 H  HG2  B GLN   B 1 107 ? 27.755 -26.400 7.112   0.36 37.99 ?  107 GLN   B HG2  1 
ATOM   5661 H  HG3  A GLN   B 1 107 ? 27.117 -26.297 8.628   0.64 39.62 ?  107 GLN   B HG3  1 
ATOM   5662 H  HG3  B GLN   B 1 107 ? 27.115 -26.450 8.566   0.36 37.99 ?  107 GLN   B HG3  1 
ATOM   5663 H  HE21 A GLN   B 1 107 ? 26.214 -24.515 6.858   0.64 43.98 ?  107 GLN   B HE21 1 
ATOM   5664 H  HE21 B GLN   B 1 107 ? 26.129 -24.599 6.950   0.36 41.19 ?  107 GLN   B HE21 1 
ATOM   5665 H  HE22 A GLN   B 1 107 ? 26.694 -23.135 7.150   0.64 43.98 ?  107 GLN   B HE22 1 
ATOM   5666 H  HE22 B GLN   B 1 107 ? 26.561 -23.223 7.320   0.36 41.19 ?  107 GLN   B HE22 1 
ATOM   5667 N  N    . LEU   B 1 108 ? 31.894 -24.856 7.616   1.00 21.61 ?  108 LEU   B N    1 
ATOM   5668 C  CA   . LEU   B 1 108 ? 32.438 -23.560 7.205   1.00 18.88 ?  108 LEU   B CA   1 
ATOM   5669 C  C    . LEU   B 1 108 ? 33.089 -23.582 5.829   1.00 16.34 ?  108 LEU   B C    1 
ATOM   5670 O  O    . LEU   B 1 108 ? 33.515 -22.521 5.340   1.00 15.50 ?  108 LEU   B O    1 
ATOM   5671 C  CB   . LEU   B 1 108 ? 33.435 -23.066 8.251   1.00 19.11 ?  108 LEU   B CB   1 
ATOM   5672 C  CG   . LEU   B 1 108 ? 32.807 -22.547 9.545   1.00 20.59 ?  108 LEU   B CG   1 
ATOM   5673 C  CD1  . LEU   B 1 108 ? 33.826 -22.538 10.666  1.00 20.96 ?  108 LEU   B CD1  1 
ATOM   5674 C  CD2  . LEU   B 1 108 ? 32.249 -21.147 9.331   1.00 21.47 ?  108 LEU   B CD2  1 
ATOM   5675 H  H    A LEU   B 1 108 ? 32.348 -25.247 8.228   0.64 25.94 ?  108 LEU   B H    1 
ATOM   5676 H  H    B LEU   B 1 108 ? 32.354 -25.253 8.220   0.36 25.94 ?  108 LEU   B H    1 
ATOM   5677 H  HA   . LEU   B 1 108 ? 31.712 -22.925 7.170   1.00 22.65 ?  108 LEU   B HA   1 
ATOM   5678 H  HB2  . LEU   B 1 108 ? 34.023 -23.797 8.490   1.00 22.94 ?  108 LEU   B HB2  1 
ATOM   5679 H  HB3  . LEU   B 1 108 ? 33.948 -22.342 7.868   1.00 22.94 ?  108 LEU   B HB3  1 
ATOM   5680 H  HG   . LEU   B 1 108 ? 32.072 -23.128 9.806   1.00 24.70 ?  108 LEU   B HG   1 
ATOM   5681 H  HD11 . LEU   B 1 108 ? 33.398 -22.229 11.481  1.00 25.16 ?  108 LEU   B HD11 1 
ATOM   5682 H  HD12 . LEU   B 1 108 ? 34.166 -23.437 10.792  1.00 25.16 ?  108 LEU   B HD12 1 
ATOM   5683 H  HD13 . LEU   B 1 108 ? 34.551 -21.939 10.427  1.00 25.16 ?  108 LEU   B HD13 1 
ATOM   5684 H  HD21 . LEU   B 1 108 ? 31.875 -20.823 10.166  1.00 25.76 ?  108 LEU   B HD21 1 
ATOM   5685 H  HD22 . LEU   B 1 108 ? 32.968 -20.563 9.043   1.00 25.76 ?  108 LEU   B HD22 1 
ATOM   5686 H  HD23 . LEU   B 1 108 ? 31.558 -21.181 8.651   1.00 25.76 ?  108 LEU   B HD23 1 
ATOM   5687 N  N    . LEU   B 1 109 ? 33.155 -24.751 5.195   1.00 15.09 ?  109 LEU   B N    1 
ATOM   5688 C  CA   . LEU   B 1 109 ? 33.785 -24.864 3.887   1.00 14.31 ?  109 LEU   B CA   1 
ATOM   5689 C  C    . LEU   B 1 109 ? 33.018 -24.083 2.824   1.00 13.86 ?  109 LEU   B C    1 
ATOM   5690 O  O    . LEU   B 1 109 ? 33.632 -23.490 1.927   1.00 13.20 ?  109 LEU   B O    1 
ATOM   5691 C  CB   . LEU   B 1 109 ? 33.900 -26.344 3.512   1.00 14.47 ?  109 LEU   B CB   1 
ATOM   5692 C  CG   . LEU   B 1 109 ? 34.685 -26.694 2.250   1.00 14.17 ?  109 LEU   B CG   1 
ATOM   5693 C  CD1  . LEU   B 1 109 ? 36.060 -26.038 2.255   1.00 13.91 ?  109 LEU   B CD1  1 
ATOM   5694 C  CD2  . LEU   B 1 109 ? 34.830 -28.204 2.118   1.00 15.09 ?  109 LEU   B CD2  1 
ATOM   5695 H  H    . LEU   B 1 109 ? 32.855 -25.493 5.500   1.00 18.11 ?  109 LEU   B H    1 
ATOM   5696 H  HA   . LEU   B 1 109 ? 34.683 -24.499 3.932   1.00 17.17 ?  109 LEU   B HA   1 
ATOM   5697 H  HB2  . LEU   B 1 109 ? 34.333 -26.810 4.245   1.00 17.36 ?  109 LEU   B HB2  1 
ATOM   5698 H  HB3  . LEU   B 1 109 ? 33.007 -26.700 3.393   1.00 17.36 ?  109 LEU   B HB3  1 
ATOM   5699 H  HG   . LEU   B 1 109 ? 34.200 -26.382 1.468   1.00 17.00 ?  109 LEU   B HG   1 
ATOM   5700 H  HD11 . LEU   B 1 109 ? 36.591 -26.409 1.531   1.00 16.69 ?  109 LEU   B HD11 1 
ATOM   5701 H  HD12 . LEU   B 1 109 ? 35.951 -25.087 2.134   1.00 16.69 ?  109 LEU   B HD12 1 
ATOM   5702 H  HD13 . LEU   B 1 109 ? 36.489 -26.224 3.105   1.00 16.69 ?  109 LEU   B HD13 1 
ATOM   5703 H  HD21 . LEU   B 1 109 ? 35.396 -28.408 1.353   1.00 18.11 ?  109 LEU   B HD21 1 
ATOM   5704 H  HD22 . LEU   B 1 109 ? 35.233 -28.558 2.926   1.00 18.11 ?  109 LEU   B HD22 1 
ATOM   5705 H  HD23 . LEU   B 1 109 ? 33.952 -28.602 1.987   1.00 18.11 ?  109 LEU   B HD23 1 
ATOM   5706 N  N    . LYS   B 1 110 ? 31.684 -24.045 2.908   1.00 13.40 ?  110 LYS   B N    1 
ATOM   5707 C  CA   . LYS   B 1 110 ? 30.929 -23.286 1.914   1.00 13.41 ?  110 LYS   B CA   1 
ATOM   5708 C  C    . LYS   B 1 110 ? 31.265 -21.797 1.997   1.00 12.85 ?  110 LYS   B C    1 
ATOM   5709 O  O    . LYS   B 1 110 ? 31.523 -21.150 0.977   1.00 12.63 ?  110 LYS   B O    1 
ATOM   5710 C  CB   . LYS   B 1 110 ? 29.425 -23.538 2.069   1.00 13.74 ?  110 LYS   B CB   1 
ATOM   5711 C  CG   . LYS   B 1 110 ? 28.614 -22.917 0.945   1.00 14.01 ?  110 LYS   B CG   1 
ATOM   5712 C  CD   . LYS   B 1 110 ? 27.156 -23.363 0.963   1.00 14.33 ?  110 LYS   B CD   1 
ATOM   5713 C  CE   . LYS   B 1 110 ? 26.387 -22.826 -0.246  1.00 15.25 ?  110 LYS   B CE   1 
ATOM   5714 N  NZ   . LYS   B 1 110 ? 26.694 -23.535 -1.519  1.00 15.47 ?  110 LYS   B NZ   1 
ATOM   5715 H  H    . LYS   B 1 110 ? 31.214 -24.444 3.500   1.00 16.08 ?  110 LYS   B H    1 
ATOM   5716 H  HA   . LYS   B 1 110 ? 31.186 -23.593 1.027   1.00 16.09 ?  110 LYS   B HA   1 
ATOM   5717 H  HB2  . LYS   B 1 110 ? 29.264 -24.498 2.062   1.00 16.48 ?  110 LYS   B HB2  1 
ATOM   5718 H  HB3  . LYS   B 1 110 ? 29.126 -23.160 2.908   1.00 16.48 ?  110 LYS   B HB3  1 
ATOM   5719 H  HG2  . LYS   B 1 110 ? 28.627 -21.951 1.041   1.00 16.81 ?  110 LYS   B HG2  1 
ATOM   5720 H  HG3  . LYS   B 1 110 ? 28.994 -23.173 0.094   1.00 16.81 ?  110 LYS   B HG3  1 
ATOM   5721 H  HD2  . LYS   B 1 110 ? 27.118 -24.336 0.940   1.00 17.19 ?  110 LYS   B HD2  1 
ATOM   5722 H  HD3  . LYS   B 1 110 ? 26.726 -23.035 1.770   1.00 17.19 ?  110 LYS   B HD3  1 
ATOM   5723 H  HE2  . LYS   B 1 110 ? 25.437 -22.913 -0.080  1.00 18.30 ?  110 LYS   B HE2  1 
ATOM   5724 H  HE3  . LYS   B 1 110 ? 26.616 -21.890 -0.366  1.00 18.30 ?  110 LYS   B HE3  1 
ATOM   5725 H  HZ1  . LYS   B 1 110 ? 26.226 -23.180 -2.185  1.00 18.57 ?  110 LYS   B HZ1  1 
ATOM   5726 H  HZ2  . LYS   B 1 110 ? 27.563 -23.463 -1.705  1.00 18.57 ?  110 LYS   B HZ2  1 
ATOM   5727 H  HZ3  . LYS   B 1 110 ? 26.487 -24.397 -1.443  1.00 18.57 ?  110 LYS   B HZ3  1 
ATOM   5728 N  N    . SER   B 1 111 ? 31.282 -21.243 3.214   1.00 13.59 ?  111 SER   B N    1 
ATOM   5729 C  CA   . SER   B 1 111 ? 31.677 -19.845 3.391   1.00 13.21 ?  111 SER   B CA   1 
ATOM   5730 C  C    . SER   B 1 111 ? 33.057 -19.586 2.801   1.00 12.63 ?  111 SER   B C    1 
ATOM   5731 O  O    . SER   B 1 111 ? 33.281 -18.556 2.148   1.00 12.77 ?  111 SER   B O    1 
ATOM   5732 C  CB   . SER   B 1 111 ? 31.674 -19.487 4.876   1.00 14.44 ?  111 SER   B CB   1 
ATOM   5733 O  OG   . SER   B 1 111 ? 30.367 -19.494 5.413   1.00 16.07 ?  111 SER   B OG   1 
ATOM   5734 H  H    . SER   B 1 111 ? 31.079 -21.659 3.939   1.00 16.31 ?  111 SER   B H    1 
ATOM   5735 H  HA   . SER   B 1 111 ? 31.041 -19.278 2.938   1.00 15.85 ?  111 SER   B HA   1 
ATOM   5736 H  HB2  . SER   B 1 111 ? 32.202 -20.141 5.361   1.00 17.32 ?  111 SER   B HB2  1 
ATOM   5737 H  HB3  . SER   B 1 111 ? 32.052 -18.606 4.987   1.00 17.32 ?  111 SER   B HB3  1 
ATOM   5738 H  HG   . SER   B 1 111 ? 30.386 -19.285 6.234   1.00 19.29 ?  111 SER   B HG   1 
ATOM   5739 N  N    . ALA   B 1 112 ? 33.995 -20.506 3.027   1.00 12.59 ?  112 ALA   B N    1 
ATOM   5740 C  CA   . ALA   B 1 112 ? 35.339 -20.343 2.481   1.00 12.47 ?  112 ALA   B CA   1 
ATOM   5741 C  C    . ALA   B 1 112 ? 35.308 -20.247 0.957   1.00 11.70 ?  112 ALA   B C    1 
ATOM   5742 O  O    . ALA   B 1 112 ? 35.935 -19.359 0.363   1.00 11.97 ?  112 ALA   B O    1 
ATOM   5743 C  CB   . ALA   B 1 112 ? 36.235 -21.491 2.958   1.00 12.67 ?  112 ALA   B CB   1 
ATOM   5744 H  H    . ALA   B 1 112 ? 33.881 -21.225 3.495   1.00 15.11 ?  112 ALA   B H    1 
ATOM   5745 H  HA   . ALA   B 1 112 ? 35.710 -19.517 2.824   1.00 14.96 ?  112 ALA   B HA   1 
ATOM   5746 H  HB1  . ALA   B 1 112 ? 37.126 -21.362 2.592   1.00 15.20 ?  112 ALA   B HB1  1 
ATOM   5747 H  HB2  . ALA   B 1 112 ? 36.275 -21.478 3.929   1.00 15.20 ?  112 ALA   B HB2  1 
ATOM   5748 H  HB3  . ALA   B 1 112 ? 35.867 -22.330 2.652   1.00 15.20 ?  112 ALA   B HB3  1 
ATOM   5749 N  N    . TYR   B 1 113 ? 34.581 -21.157 0.300   1.00 11.76 ?  113 TYR   B N    1 
ATOM   5750 C  CA   . TYR   B 1 113 ? 34.504 -21.107 -1.155  1.00 11.53 ?  113 TYR   B CA   1 
ATOM   5751 C  C    . TYR   B 1 113 ? 33.795 -19.856 -1.670  1.00 11.19 ?  113 TYR   B C    1 
ATOM   5752 O  O    . TYR   B 1 113 ? 34.060 -19.429 -2.797  1.00 11.45 ?  113 TYR   B O    1 
ATOM   5753 C  CB   . TYR   B 1 113 ? 33.832 -22.367 -1.704  1.00 11.52 ?  113 TYR   B CB   1 
ATOM   5754 C  CG   . TYR   B 1 113 ? 34.794 -23.518 -1.955  1.00 11.99 ?  113 TYR   B CG   1 
ATOM   5755 C  CD1  . TYR   B 1 113 ? 35.800 -23.414 -2.910  1.00 12.79 ?  113 TYR   B CD1  1 
ATOM   5756 C  CD2  . TYR   B 1 113 ? 34.688 -24.711 -1.253  1.00 12.08 ?  113 TYR   B CD2  1 
ATOM   5757 C  CE1  . TYR   B 1 113 ? 36.684 -24.455 -3.150  1.00 12.57 ?  113 TYR   B CE1  1 
ATOM   5758 C  CE2  . TYR   B 1 113 ? 35.563 -25.765 -1.487  1.00 12.47 ?  113 TYR   B CE2  1 
ATOM   5759 C  CZ   . TYR   B 1 113 ? 36.552 -25.636 -2.441  1.00 12.63 ?  113 TYR   B CZ   1 
ATOM   5760 O  OH   . TYR   B 1 113 ? 37.436 -26.660 -2.703  1.00 13.48 ?  113 TYR   B OH   1 
ATOM   5761 H  H    . TYR   B 1 113 ? 34.124 -21.793 0.672   1.00 14.11 ?  113 TYR   B H    1 
ATOM   5762 H  HA   . TYR   B 1 113 ? 35.406 -21.089 -1.493  1.00 13.84 ?  113 TYR   B HA   1 
ATOM   5763 H  HB2  . TYR   B 1 113 ? 33.167 -22.679 -1.067  1.00 13.82 ?  113 TYR   B HB2  1 
ATOM   5764 H  HB3  . TYR   B 1 113 ? 33.402 -22.153 -2.546  1.00 13.82 ?  113 TYR   B HB3  1 
ATOM   5765 H  HD1  . TYR   B 1 113 ? 35.890 -22.621 -3.393  1.00 15.35 ?  113 TYR   B HD1  1 
ATOM   5766 H  HD2  . TYR   B 1 113 ? 34.014 -24.802 -0.620  1.00 14.50 ?  113 TYR   B HD2  1 
ATOM   5767 H  HE1  . TYR   B 1 113 ? 37.350 -24.363 -3.797  1.00 15.08 ?  113 TYR   B HE1  1 
ATOM   5768 H  HE2  . TYR   B 1 113 ? 35.469 -26.560 -1.014  1.00 14.97 ?  113 TYR   B HE2  1 
ATOM   5769 H  HH   . TYR   B 1 113 ? 37.253 -27.321 -2.222  1.00 16.17 ?  113 TYR   B HH   1 
ATOM   5770 N  N    . GLU   B 1 114 ? 32.868 -19.283 -0.891  1.00 11.52 ?  114 GLU   B N    1 
ATOM   5771 C  CA   . GLU   B 1 114 ? 32.184 -18.067 -1.335  1.00 11.49 ?  114 GLU   B CA   1 
ATOM   5772 C  C    . GLU   B 1 114 ? 33.170 -16.947 -1.644  1.00 11.26 ?  114 GLU   B C    1 
ATOM   5773 O  O    . GLU   B 1 114 ? 32.890 -16.091 -2.490  1.00 11.66 ?  114 GLU   B O    1 
ATOM   5774 C  CB   . GLU   B 1 114 ? 31.133 -17.642 -0.306  1.00 11.99 ?  114 GLU   B CB   1 
ATOM   5775 C  CG   . GLU   B 1 114 ? 29.905 -18.557 -0.384  1.00 11.96 ?  114 GLU   B CG   1 
ATOM   5776 C  CD   . GLU   B 1 114 ? 28.886 -18.378 0.725   1.00 12.34 ?  114 GLU   B CD   1 
ATOM   5777 O  OE1  . GLU   B 1 114 ? 29.170 -17.748 1.762   1.00 12.75 ?  114 GLU   B OE1  1 
ATOM   5778 O  OE2  . GLU   B 1 114 ? 27.763 -18.919 0.566   1.00 13.39 -1 114 GLU   B OE2  1 
ATOM   5779 H  H    . GLU   B 1 114 ? 32.610 -19.586 -0.123  1.00 13.82 ?  114 GLU   B H    1 
ATOM   5780 H  HA   . GLU   B 1 114 ? 31.716 -18.264 -2.155  1.00 13.78 ?  114 GLU   B HA   1 
ATOM   5781 H  HB2  . GLU   B 1 114 ? 31.509 -17.709 0.590   1.00 14.38 ?  114 GLU   B HB2  1 
ATOM   5782 H  HB3  . GLU   B 1 114 ? 30.852 -16.734 -0.485  1.00 14.38 ?  114 GLU   B HB3  1 
ATOM   5783 H  HG2  . GLU   B 1 114 ? 29.461 -18.392 -1.224  1.00 14.35 ?  114 GLU   B HG2  1 
ATOM   5784 H  HG3  . GLU   B 1 114 ? 30.213 -19.478 -0.350  1.00 14.35 ?  114 GLU   B HG3  1 
ATOM   5785 N  N    . ASN   B 1 115 ? 34.338 -16.941 -0.994  1.00 11.12 ?  115 ASN   B N    1 
ATOM   5786 C  CA   . ASN   B 1 115 ? 35.331 -15.911 -1.295  1.00 10.89 ?  115 ASN   B CA   1 
ATOM   5787 C  C    . ASN   B 1 115 ? 35.742 -15.936 -2.761  1.00 10.59 ?  115 ASN   B C    1 
ATOM   5788 O  O    . ASN   B 1 115 ? 36.134 -14.898 -3.317  1.00 11.36 ?  115 ASN   B O    1 
ATOM   5789 C  CB   . ASN   B 1 115 ? 36.567 -16.091 -0.411  1.00 11.67 ?  115 ASN   B CB   1 
ATOM   5790 C  CG   . ASN   B 1 115 ? 36.301 -15.812 1.049   1.00 11.99 ?  115 ASN   B CG   1 
ATOM   5791 O  OD1  . ASN   B 1 115 ? 36.297 -14.659 1.485   1.00 13.94 ?  115 ASN   B OD1  1 
ATOM   5792 N  ND2  . ASN   B 1 115 ? 36.131 -16.876 1.830   1.00 12.18 ?  115 ASN   B ND2  1 
ATOM   5793 H  H    . ASN   B 1 115 ? 34.578 -17.506 -0.382  1.00 13.34 ?  115 ASN   B H    1 
ATOM   5794 H  HA   . ASN   B 1 115 ? 34.957 -15.042 -1.105  1.00 13.07 ?  115 ASN   B HA   1 
ATOM   5795 H  HB2  . ASN   B 1 115 ? 36.889 -17.004 -0.490  1.00 14.00 ?  115 ASN   B HB2  1 
ATOM   5796 H  HB3  . ASN   B 1 115 ? 37.260 -15.475 -0.704  1.00 14.00 ?  115 ASN   B HB3  1 
ATOM   5797 H  HD21 . ASN   B 1 115 ? 35.986 -16.773 2.671   1.00 14.61 ?  115 ASN   B HD21 1 
ATOM   5798 H  HD22 . ASN   B 1 115 ? 36.157 -17.670 1.495   1.00 14.61 ?  115 ASN   B HD22 1 
ATOM   5799 N  N    . PHE   B 1 116 ? 35.708 -17.116 -3.397  1.00 10.58 ?  116 PHE   B N    1 
ATOM   5800 C  CA   . PHE   B 1 116 ? 36.146 -17.204 -4.786  1.00 11.21 ?  116 PHE   B CA   1 
ATOM   5801 C  C    . PHE   B 1 116 ? 35.243 -16.380 -5.703  1.00 10.85 ?  116 PHE   B C    1 
ATOM   5802 O  O    . PHE   B 1 116 ? 35.674 -15.955 -6.780  1.00 11.45 ?  116 PHE   B O    1 
ATOM   5803 C  CB   . PHE   B 1 116 ? 36.116 -18.650 -5.307  1.00 10.65 ?  116 PHE   B CB   1 
ATOM   5804 C  CG   . PHE   B 1 116 ? 37.185 -19.611 -4.755  1.00 10.49 ?  116 PHE   B CG   1 
ATOM   5805 C  CD1  . PHE   B 1 116 ? 37.830 -19.429 -3.546  1.00 11.54 ?  116 PHE   B CD1  1 
ATOM   5806 C  CD2  . PHE   B 1 116 ? 37.484 -20.750 -5.488  1.00 10.76 ?  116 PHE   B CD2  1 
ATOM   5807 C  CE1  . PHE   B 1 116 ? 38.765 -20.366 -3.090  1.00 11.71 ?  116 PHE   B CE1  1 
ATOM   5808 C  CE2  . PHE   B 1 116 ? 38.414 -21.688 -5.045  1.00 11.02 ?  116 PHE   B CE2  1 
ATOM   5809 C  CZ   . PHE   B 1 116 ? 39.047 -21.505 -3.845  1.00 11.25 ?  116 PHE   B CZ   1 
ATOM   5810 H  H    . PHE   B 1 116 ? 35.437 -17.860 -3.055  1.00 12.69 ?  116 PHE   B H    1 
ATOM   5811 H  HA   . PHE   B 1 116 ? 37.054 -16.873 -4.862  1.00 13.46 ?  116 PHE   B HA   1 
ATOM   5812 H  HB2  . PHE   B 1 116 ? 35.243 -19.031 -5.089  1.00 12.78 ?  116 PHE   B HB2  1 
ATOM   5813 H  HB3  . PHE   B 1 116 ? 36.213 -18.628 -6.272  1.00 12.78 ?  116 PHE   B HB3  1 
ATOM   5814 H  HD1  . PHE   B 1 116 ? 37.630 -18.680 -3.030  1.00 13.85 ?  116 PHE   B HD1  1 
ATOM   5815 H  HD2  . PHE   B 1 116 ? 37.046 -20.894 -6.300  1.00 12.91 ?  116 PHE   B HD2  1 
ATOM   5816 H  HE1  . PHE   B 1 116 ? 39.195 -20.233 -2.277  1.00 14.06 ?  116 PHE   B HE1  1 
ATOM   5817 H  HE2  . PHE   B 1 116 ? 38.597 -22.437 -5.561  1.00 13.22 ?  116 PHE   B HE2  1 
ATOM   5818 H  HZ   . PHE   B 1 116 ? 39.679 -22.118 -3.551  1.00 13.50 ?  116 PHE   B HZ   1 
ATOM   5819 N  N    . ASN   B 1 117 ? 33.976 -16.184 -5.318  1.00 11.00 ?  117 ASN   B N    1 
ATOM   5820 C  CA   . ASN   B 1 117 ? 33.030 -15.483 -6.183  1.00 11.48 ?  117 ASN   B CA   1 
ATOM   5821 C  C    . ASN   B 1 117 ? 33.350 -14.003 -6.341  1.00 11.90 ?  117 ASN   B C    1 
ATOM   5822 O  O    . ASN   B 1 117 ? 32.755 -13.348 -7.201  1.00 13.17 ?  117 ASN   B O    1 
ATOM   5823 C  CB   . ASN   B 1 117 ? 31.608 -15.700 -5.684  1.00 11.58 ?  117 ASN   B CB   1 
ATOM   5824 C  CG   . ASN   B 1 117 ? 31.149 -17.112 -5.936  1.00 12.11 ?  117 ASN   B CG   1 
ATOM   5825 O  OD1  . ASN   B 1 117 ? 31.497 -17.702 -6.958  1.00 12.82 ?  117 ASN   B OD1  1 
ATOM   5826 N  ND2  . ASN   B 1 117 ? 30.413 -17.685 -4.996  1.00 12.06 ?  117 ASN   B ND2  1 
ATOM   5827 H  H    . ASN   B 1 117 ? 33.650 -16.449 -4.565  1.00 13.20 ?  117 ASN   B H    1 
ATOM   5828 H  HA   . ASN   B 1 117 ? 33.086 -15.886 -7.061  1.00 13.77 ?  117 ASN   B HA   1 
ATOM   5829 H  HB2  . ASN   B 1 117 ? 31.575 -15.535 -4.725  1.00 13.90 ?  117 ASN   B HB2  1 
ATOM   5830 H  HB3  . ASN   B 1 117 ? 31.013 -15.089 -6.146  1.00 13.90 ?  117 ASN   B HB3  1 
ATOM   5831 H  HD21 . ASN   B 1 117 ? 30.127 -18.491 -5.104  1.00 14.47 ?  117 ASN   B HD21 1 
ATOM   5832 H  HD22 . ASN   B 1 117 ? 30.195 -17.246 -4.289  1.00 14.47 ?  117 ASN   B HD22 1 
ATOM   5833 N  N    . GLN   B 1 118 ? 34.288 -13.474 -5.564  1.00 11.36 ?  118 GLN   B N    1 
ATOM   5834 C  CA   . GLN   B 1 118 ? 34.711 -12.086 -5.706  1.00 12.18 ?  118 GLN   B CA   1 
ATOM   5835 C  C    . GLN   B 1 118 ? 35.779 -11.894 -6.778  1.00 12.37 ?  118 GLN   B C    1 
ATOM   5836 O  O    . GLN   B 1 118 ? 36.251 -10.769 -6.960  1.00 13.64 ?  118 GLN   B O    1 
ATOM   5837 C  CB   . GLN   B 1 118 ? 35.189 -11.551 -4.352  1.00 12.33 ?  118 GLN   B CB   1 
ATOM   5838 C  CG   . GLN   B 1 118 ? 34.105 -11.589 -3.285  1.00 12.60 ?  118 GLN   B CG   1 
ATOM   5839 C  CD   . GLN   B 1 118 ? 32.936 -10.674 -3.608  1.00 12.92 ?  118 GLN   B CD   1 
ATOM   5840 O  OE1  . GLN   B 1 118 ? 33.124 -9.534  -4.050  1.00 13.54 ?  118 GLN   B OE1  1 
ATOM   5841 N  NE2  . GLN   B 1 118 ? 31.723 -11.169 -3.401  1.00 13.31 ?  118 GLN   B NE2  1 
ATOM   5842 H  H    . GLN   B 1 118 ? 34.714 -13.899 -4.946  1.00 13.64 ?  118 GLN   B H    1 
ATOM   5843 H  HA   . GLN   B 1 118 ? 33.946 -11.559 -5.981  1.00 14.61 ?  118 GLN   B HA   1 
ATOM   5844 H  HB2  . GLN   B 1 118 ? 35.935 -12.082 -4.046  1.00 14.80 ?  118 GLN   B HB2  1 
ATOM   5845 H  HB3  . GLN   B 1 118 ? 35.465 -10.622 -4.460  1.00 14.80 ?  118 GLN   B HB3  1 
ATOM   5846 H  HG2  . GLN   B 1 118 ? 33.769 -12.498 -3.213  1.00 15.12 ?  118 GLN   B HG2  1 
ATOM   5847 H  HG3  . GLN   B 1 118 ? 34.485 -11.308 -2.440  1.00 15.12 ?  118 GLN   B HG3  1 
ATOM   5848 H  HE21 . GLN   B 1 118 ? 31.635 -11.966 -3.088  1.00 15.97 ?  118 GLN   B HE21 1 
ATOM   5849 H  HE22 . GLN   B 1 118 ? 31.034 -10.691 -3.569  1.00 15.97 ?  118 GLN   B HE22 1 
ATOM   5850 N  N    . HIS   B 1 119 ? 36.134 -12.952 -7.509  1.00 11.57 ?  119 HIS   B N    1 
ATOM   5851 C  CA   . HIS   B 1 119 ? 37.176 -12.913 -8.527  1.00 11.79 ?  119 HIS   B CA   1 
ATOM   5852 C  C    . HIS   B 1 119 ? 36.697 -13.647 -9.766  1.00 11.86 ?  119 HIS   B C    1 
ATOM   5853 O  O    . HIS   B 1 119 ? 36.192 -14.763 -9.664  1.00 12.77 ?  119 HIS   B O    1 
ATOM   5854 C  CB   . HIS   B 1 119 ? 38.460 -13.539 -7.978  1.00 12.43 ?  119 HIS   B CB   1 
ATOM   5855 C  CG   . HIS   B 1 119 ? 38.941 -12.837 -6.754  1.00 13.52 ?  119 HIS   B CG   1 
ATOM   5856 N  ND1  . HIS   B 1 119 ? 39.748 -11.720 -6.807  1.00 14.62 ?  119 HIS   B ND1  1 
ATOM   5857 C  CD2  . HIS   B 1 119 ? 38.638 -13.026 -5.449  1.00 14.73 ?  119 HIS   B CD2  1 
ATOM   5858 C  CE1  . HIS   B 1 119 ? 39.960 -11.285 -5.579  1.00 15.62 ?  119 HIS   B CE1  1 
ATOM   5859 N  NE2  . HIS   B 1 119 ? 39.287 -12.048 -4.738  1.00 15.98 ?  119 HIS   B NE2  1 
ATOM   5860 H  H    . HIS   B 1 119 ? 35.761 -13.730 -7.444  1.00 13.88 ?  119 HIS   B H    1 
ATOM   5861 H  HA   . HIS   B 1 119 ? 37.358 -11.989 -8.770  1.00 14.15 ?  119 HIS   B HA   1 
ATOM   5862 H  HB2  . HIS   B 1 119 ? 38.292 -14.465 -7.755  1.00 14.92 ?  119 HIS   B HB2  1 
ATOM   5863 H  HB3  . HIS   B 1 119 ? 39.156 -13.479 -8.655  1.00 14.92 ?  119 HIS   B HB3  1 
ATOM   5864 H  HD2  . HIS   B 1 119 ? 38.094 -13.696 -5.099  1.00 17.67 ?  119 HIS   B HD2  1 
ATOM   5865 H  HE1  . HIS   B 1 119 ? 40.496 -10.563 -5.344  1.00 18.75 ?  119 HIS   B HE1  1 
ATOM   5866 H  HE2  . HIS   B 1 119 ? 39.287 -11.969 -3.880  1.00 19.17 ?  119 HIS   B HE2  1 
ATOM   5867 N  N    . GLU   B 1 120 ? 36.848 -13.027 -10.936 1.00 12.37 ?  120 GLU   B N    1 
ATOM   5868 C  CA   . GLU   B 1 120 ? 36.269 -13.616 -12.139 1.00 13.82 ?  120 GLU   B CA   1 
ATOM   5869 C  C    . GLU   B 1 120 ? 36.948 -14.919 -12.544 1.00 12.88 ?  120 GLU   B C    1 
ATOM   5870 O  O    . GLU   B 1 120 ? 36.286 -15.792 -13.119 1.00 13.22 ?  120 GLU   B O    1 
ATOM   5871 C  CB   . GLU   B 1 120 ? 36.275 -12.609 -13.287 1.00 18.45 ?  120 GLU   B CB   1 
ATOM   5872 C  CG   . GLU   B 1 120 ? 35.302 -11.458 -13.079 1.00 24.76 ?  120 GLU   B CG   1 
ATOM   5873 C  CD   . GLU   B 1 120 ? 35.178 -10.560 -14.295 1.00 30.74 ?  120 GLU   B CD   1 
ATOM   5874 O  OE1  . GLU   B 1 120 ? 36.177 -10.404 -15.029 1.00 33.34 ?  120 GLU   B OE1  1 
ATOM   5875 O  OE2  . GLU   B 1 120 ? 34.078 -10.011 -14.514 1.00 33.85 -1 120 GLU   B OE2  1 
ATOM   5876 H  H    . GLU   B 1 120 ? 37.262 -12.279 -11.059 1.00 14.84 ?  120 GLU   B H    1 
ATOM   5877 H  HA   . GLU   B 1 120 ? 35.346 -13.827 -11.954 1.00 16.59 ?  120 GLU   B HA   1 
ATOM   5878 H  HB2  . GLU   B 1 120 ? 37.161 -12.230 -13.380 1.00 22.14 ?  120 GLU   B HB2  1 
ATOM   5879 H  HB3  . GLU   B 1 120 ? 36.021 -13.061 -14.109 1.00 22.14 ?  120 GLU   B HB3  1 
ATOM   5880 H  HG2  . GLU   B 1 120 ? 34.420 -11.818 -12.888 1.00 29.71 ?  120 GLU   B HG2  1 
ATOM   5881 H  HG3  . GLU   B 1 120 ? 35.605 -10.916 -12.335 1.00 29.71 ?  120 GLU   B HG3  1 
ATOM   5882 N  N    . VAL   B 1 121 ? 38.249 -15.061 -12.284 1.00 12.45 ?  121 VAL   B N    1 
ATOM   5883 C  CA   . VAL   B 1 121 ? 38.993 -16.271 -12.628 1.00 12.12 ?  121 VAL   B CA   1 
ATOM   5884 C  C    . VAL   B 1 121 ? 40.102 -16.469 -11.606 1.00 11.69 ?  121 VAL   B C    1 
ATOM   5885 O  O    . VAL   B 1 121 ? 40.778 -15.509 -11.215 1.00 12.08 ?  121 VAL   B O    1 
ATOM   5886 C  CB   . VAL   B 1 121 ? 39.507 -16.235 -14.087 1.00 14.02 ?  121 VAL   B CB   1 
ATOM   5887 C  CG1  . VAL   B 1 121 ? 40.369 -15.000 -14.348 1.00 15.19 ?  121 VAL   B CG1  1 
ATOM   5888 C  CG2  . VAL   B 1 121 ? 40.257 -17.522 -14.434 1.00 15.66 ?  121 VAL   B CG2  1 
ATOM   5889 H  H    . VAL   B 1 121 ? 38.738 -14.454 -11.918 1.00 14.94 ?  121 VAL   B H    1 
ATOM   5890 H  HA   . VAL   B 1 121 ? 38.384 -17.025 -12.558 1.00 14.54 ?  121 VAL   B HA   1 
ATOM   5891 H  HB   . VAL   B 1 121 ? 38.739 -16.185 -14.682 1.00 16.82 ?  121 VAL   B HB   1 
ATOM   5892 H  HG11 . VAL   B 1 121 ? 40.685 -15.022 -15.265 1.00 18.23 ?  121 VAL   B HG11 1 
ATOM   5893 H  HG12 . VAL   B 1 121 ? 39.833 -14.205 -14.202 1.00 18.23 ?  121 VAL   B HG12 1 
ATOM   5894 H  HG13 . VAL   B 1 121 ? 41.123 -15.008 -13.738 1.00 18.23 ?  121 VAL   B HG13 1 
ATOM   5895 H  HG21 . VAL   B 1 121 ? 40.461 -17.523 -15.384 1.00 18.79 ?  121 VAL   B HG21 1 
ATOM   5896 H  HG22 . VAL   B 1 121 ? 41.080 -17.559 -13.922 1.00 18.79 ?  121 VAL   B HG22 1 
ATOM   5897 H  HG23 . VAL   B 1 121 ? 39.698 -18.286 -14.219 1.00 18.79 ?  121 VAL   B HG23 1 
ATOM   5898 N  N    . LEU   B 1 122 ? 40.278 -17.724 -11.169 1.00 11.21 ?  122 LEU   B N    1 
ATOM   5899 C  CA   . LEU   B 1 122 ? 41.261 -18.078 -10.147 1.00 11.09 ?  122 LEU   B CA   1 
ATOM   5900 C  C    . LEU   B 1 122 ? 41.913 -19.414 -10.469 1.00 11.09 ?  122 LEU   B C    1 
ATOM   5901 O  O    . LEU   B 1 122 ? 41.252 -20.333 -10.970 1.00 11.99 ?  122 LEU   B O    1 
ATOM   5902 C  CB   . LEU   B 1 122 ? 40.613 -18.300 -8.767  1.00 12.64 ?  122 LEU   B CB   1 
ATOM   5903 C  CG   . LEU   B 1 122 ? 39.573 -17.284 -8.286  1.00 12.90 ?  122 LEU   B CG   1 
ATOM   5904 C  CD1  . LEU   B 1 122 ? 38.174 -17.654 -8.758  1.00 13.92 ?  122 LEU   B CD1  1 
ATOM   5905 C  CD2  . LEU   B 1 122 ? 39.619 -17.159 -6.775  1.00 12.39 ?  122 LEU   B CD2  1 
ATOM   5906 H  H    . LEU   B 1 122 ? 39.829 -18.403 -11.452 1.00 13.45 ?  122 LEU   B H    1 
ATOM   5907 H  HA   . LEU   B 1 122 ? 41.940 -17.386 -10.073 1.00 13.30 ?  122 LEU   B HA   1 
ATOM   5908 H  HB2  . LEU   B 1 122 ? 40.173 -19.163 -8.778  1.00 15.17 ?  122 LEU   B HB2  1 
ATOM   5909 H  HB3  . LEU   B 1 122 ? 41.318 -18.311 -8.101  1.00 15.17 ?  122 LEU   B HB3  1 
ATOM   5910 H  HG   . LEU   B 1 122 ? 39.790 -16.415 -8.658  1.00 15.48 ?  122 LEU   B HG   1 
ATOM   5911 H  HD11 . LEU   B 1 122 ? 37.542 -17.010 -8.399  1.00 16.71 ?  122 LEU   B HD11 1 
ATOM   5912 H  HD12 . LEU   B 1 122 ? 38.153 -17.629 -9.728  1.00 16.71 ?  122 LEU   B HD12 1 
ATOM   5913 H  HD13 . LEU   B 1 122 ? 37.959 -18.542 -8.443  1.00 16.71 ?  122 LEU   B HD13 1 
ATOM   5914 H  HD21 . LEU   B 1 122 ? 38.934 -16.535 -6.486  1.00 14.87 ?  122 LEU   B HD21 1 
ATOM   5915 H  HD22 . LEU   B 1 122 ? 39.463 -18.029 -6.379  1.00 14.87 ?  122 LEU   B HD22 1 
ATOM   5916 H  HD23 . LEU   B 1 122 ? 40.496 -16.829 -6.512  1.00 14.87 ?  122 LEU   B HD23 1 
ATOM   5917 N  N    . LEU   B 1 123 ? 43.200 -19.525 -10.115 1.00 10.66 ?  123 LEU   B N    1 
ATOM   5918 C  CA   . LEU   B 1 123 ? 43.911 -20.794 -9.991  1.00 10.89 ?  123 LEU   B CA   1 
ATOM   5919 C  C    . LEU   B 1 123 ? 43.886 -21.181 -8.517  1.00 10.58 ?  123 LEU   B C    1 
ATOM   5920 O  O    . LEU   B 1 123 ? 44.235 -20.353 -7.666  1.00 10.84 ?  123 LEU   B O    1 
ATOM   5921 C  CB   . LEU   B 1 123 ? 45.360 -20.614 -10.448 1.00 11.25 ?  123 LEU   B CB   1 
ATOM   5922 C  CG   . LEU   B 1 123 ? 46.309 -21.794 -10.207 1.00 11.47 ?  123 LEU   B CG   1 
ATOM   5923 C  CD1  . LEU   B 1 123 ? 45.892 -23.043 -10.985 1.00 12.44 ?  123 LEU   B CD1  1 
ATOM   5924 C  CD2  . LEU   B 1 123 ? 47.723 -21.386 -10.578 1.00 12.19 ?  123 LEU   B CD2  1 
ATOM   5925 H  H    . LEU   B 1 123 ? 43.698 -18.845 -9.921  1.00 12.79 ?  123 LEU   B H    1 
ATOM   5926 H  HA   . LEU   B 1 123 ? 43.474 -21.484 -10.519 1.00 13.07 ?  123 LEU   B HA   1 
ATOM   5927 H  HB2  . LEU   B 1 123 ? 45.351 -20.444 -11.401 1.00 13.50 ?  123 LEU   B HB2  1 
ATOM   5928 H  HB3  . LEU   B 1 123 ? 45.727 -19.851 -9.984  1.00 13.50 ?  123 LEU   B HB3  1 
ATOM   5929 H  HG   . LEU   B 1 123 ? 46.306 -22.019 -9.262  1.00 13.77 ?  123 LEU   B HG   1 
ATOM   5930 H  HD11 . LEU   B 1 123 ? 46.530 -23.749 -10.808 1.00 14.93 ?  123 LEU   B HD11 1 
ATOM   5931 H  HD12 . LEU   B 1 123 ? 45.007 -23.312 -10.696 1.00 14.93 ?  123 LEU   B HD12 1 
ATOM   5932 H  HD13 . LEU   B 1 123 ? 45.883 -22.831 -11.931 1.00 14.93 ?  123 LEU   B HD13 1 
ATOM   5933 H  HD21 . LEU   B 1 123 ? 48.315 -22.136 -10.426 1.00 14.62 ?  123 LEU   B HD21 1 
ATOM   5934 H  HD22 . LEU   B 1 123 ? 47.737 -21.134 -11.515 1.00 14.62 ?  123 LEU   B HD22 1 
ATOM   5935 H  HD23 . LEU   B 1 123 ? 47.985 -20.633 -10.028 1.00 14.62 ?  123 LEU   B HD23 1 
ATOM   5936 N  N    . ALA   B 1 124 ? 43.462 -22.413 -8.207  1.00 10.57 ?  124 ALA   B N    1 
ATOM   5937 C  CA   . ALA   B 1 124 ? 43.191 -22.735 -6.811  1.00 10.63 ?  124 ALA   B CA   1 
ATOM   5938 C  C    . ALA   B 1 124 ? 43.458 -24.195 -6.474  1.00 10.50 ?  124 ALA   B C    1 
ATOM   5939 O  O    . ALA   B 1 124 ? 43.330 -25.072 -7.338  1.00 11.04 ?  124 ALA   B O    1 
ATOM   5940 C  CB   . ALA   B 1 124 ? 41.736 -22.415 -6.446  1.00 11.14 ?  124 ALA   B CB   1 
ATOM   5941 H  H    . ALA   B 1 124 ? 43.321 -23.061 -8.766  1.00 12.69 ?  124 ALA   B H    1 
ATOM   5942 H  HA   . ALA   B 1 124 ? 43.763 -22.183 -6.261  1.00 12.76 ?  124 ALA   B HA   1 
ATOM   5943 H  HB1  . ALA   B 1 124 ? 41.583 -22.635 -5.513  1.00 13.37 ?  124 ALA   B HB1  1 
ATOM   5944 H  HB2  . ALA   B 1 124 ? 41.574 -21.468 -6.592  1.00 13.37 ?  124 ALA   B HB2  1 
ATOM   5945 H  HB3  . ALA   B 1 124 ? 41.142 -22.939 -7.009  1.00 13.37 ?  124 ALA   B HB3  1 
ATOM   5946 N  N    . PRO   B 1 125 ? 43.763 -24.482 -5.212  1.00 10.71 ?  125 PRO   B N    1 
ATOM   5947 C  CA   . PRO   B 1 125 ? 43.704 -25.846 -4.686  1.00 11.19 ?  125 PRO   B CA   1 
ATOM   5948 C  C    . PRO   B 1 125 ? 42.303 -26.119 -4.137  1.00 11.61 ?  125 PRO   B C    1 
ATOM   5949 O  O    . PRO   B 1 125 ? 41.506 -25.199 -3.929  1.00 11.96 ?  125 PRO   B O    1 
ATOM   5950 C  CB   . PRO   B 1 125 ? 44.691 -25.767 -3.516  1.00 12.22 ?  125 PRO   B CB   1 
ATOM   5951 C  CG   . PRO   B 1 125 ? 44.438 -24.382 -2.951  1.00 12.47 ?  125 PRO   B CG   1 
ATOM   5952 C  CD   . PRO   B 1 125 ? 44.093 -23.510 -4.153  1.00 11.41 ?  125 PRO   B CD   1 
ATOM   5953 H  HA   . PRO   B 1 125 ? 43.978 -26.516 -5.334  1.00 13.42 ?  125 PRO   B HA   1 
ATOM   5954 H  HB2  . PRO   B 1 125 ? 44.486 -26.452 -2.856  1.00 14.66 ?  125 PRO   B HB2  1 
ATOM   5955 H  HB3  . PRO   B 1 125 ? 45.602 -25.853 -3.835  1.00 14.66 ?  125 PRO   B HB3  1 
ATOM   5956 H  HG2  . PRO   B 1 125 ? 43.694 -24.406 -2.327  1.00 14.96 ?  125 PRO   B HG2  1 
ATOM   5957 H  HG3  . PRO   B 1 125 ? 45.239 -24.051 -2.510  1.00 14.96 ?  125 PRO   B HG3  1 
ATOM   5958 H  HD2  . PRO   B 1 125 ? 43.326 -22.950 -3.962  1.00 13.69 ?  125 PRO   B HD2  1 
ATOM   5959 H  HD3  . PRO   B 1 125 ? 44.864 -22.974 -4.414  1.00 13.69 ?  125 PRO   B HD3  1 
ATOM   5960 N  N    . LEU   B 1 126 ? 42.036 -27.395 -3.845  1.00 12.09 ?  126 LEU   B N    1 
ATOM   5961 C  CA   . LEU   B 1 126 ? 40.813 -27.758 -3.135  1.00 12.77 ?  126 LEU   B CA   1 
ATOM   5962 C  C    . LEU   B 1 126 ? 40.926 -27.357 -1.674  1.00 13.13 ?  126 LEU   B C    1 
ATOM   5963 O  O    . LEU   B 1 126 ? 41.820 -27.820 -0.960  1.00 14.82 ?  126 LEU   B O    1 
ATOM   5964 C  CB   . LEU   B 1 126 ? 40.559 -29.258 -3.239  1.00 13.98 ?  126 LEU   B CB   1 
ATOM   5965 C  CG   . LEU   B 1 126 ? 40.038 -29.752 -4.591  1.00 15.12 ?  126 LEU   B CG   1 
ATOM   5966 C  CD1  . LEU   B 1 126 ? 40.080 -31.262 -4.659  1.00 17.24 ?  126 LEU   B CD1  1 
ATOM   5967 C  CD2  . LEU   B 1 126 ? 38.627 -29.264 -4.858  1.00 15.37 ?  126 LEU   B CD2  1 
ATOM   5968 H  H    . LEU   B 1 126 ? 42.548 -28.062 -4.030  1.00 14.51 ?  126 LEU   B H    1 
ATOM   5969 H  HA   . LEU   B 1 126 ? 40.063 -27.287 -3.522  1.00 15.32 ?  126 LEU   B HA   1 
ATOM   5970 H  HB2  . LEU   B 1 126 ? 41.390 -29.722 -3.058  1.00 16.78 ?  126 LEU   B HB2  1 
ATOM   5971 H  HB3  . LEU   B 1 126 ? 39.899 -29.502 -2.570  1.00 16.78 ?  126 LEU   B HB3  1 
ATOM   5972 H  HG   . LEU   B 1 126 ? 40.616 -29.403 -5.292  1.00 18.14 ?  126 LEU   B HG   1 
ATOM   5973 H  HD11 . LEU   B 1 126 ? 39.749 -31.547 -5.526  1.00 20.69 ?  126 LEU   B HD11 1 
ATOM   5974 H  HD12 . LEU   B 1 126 ? 40.991 -31.563 -4.536  1.00 20.69 ?  126 LEU   B HD12 1 
ATOM   5975 H  HD13 . LEU   B 1 126 ? 39.513 -31.623 -3.957  1.00 20.69 ?  126 LEU   B HD13 1 
ATOM   5976 H  HD21 . LEU   B 1 126 ? 38.302 -29.674 -5.675  1.00 18.45 ?  126 LEU   B HD21 1 
ATOM   5977 H  HD22 . LEU   B 1 126 ? 38.061 -29.511 -4.113  1.00 18.45 ?  126 LEU   B HD22 1 
ATOM   5978 H  HD23 . LEU   B 1 126 ? 38.639 -28.296 -4.959  1.00 18.45 ?  126 LEU   B HD23 1 
ATOM   5979 N  N    . LEU   B 1 127 ? 40.001 -26.520 -1.218  1.00 12.75 ?  127 LEU   B N    1 
ATOM   5980 C  CA   . LEU   B 1 127 ? 40.059 -26.030 0.148   1.00 13.04 ?  127 LEU   B CA   1 
ATOM   5981 C  C    . LEU   B 1 127 ? 39.786 -27.153 1.142   1.00 12.74 ?  127 LEU   B C    1 
ATOM   5982 O  O    . LEU   B 1 127 ? 38.961 -28.044 0.915   1.00 13.09 ?  127 LEU   B O    1 
ATOM   5983 C  CB   . LEU   B 1 127 ? 39.042 -24.907 0.359   1.00 13.55 ?  127 LEU   B CB   1 
ATOM   5984 C  CG   . LEU   B 1 127 ? 39.216 -23.648 -0.489  1.00 13.91 ?  127 LEU   B CG   1 
ATOM   5985 C  CD1  . LEU   B 1 127 ? 38.095 -22.675 -0.169  1.00 14.18 ?  127 LEU   B CD1  1 
ATOM   5986 C  CD2  . LEU   B 1 127 ? 40.576 -22.993 -0.262  1.00 14.50 ?  127 LEU   B CD2  1 
ATOM   5987 H  H    . LEU   B 1 127 ? 39.338 -26.213 -1.679  1.00 15.30 ?  127 LEU   B H    1 
ATOM   5988 H  HA   . LEU   B 1 127 ? 40.947 -25.672 0.321   1.00 15.65 ?  127 LEU   B HA   1 
ATOM   5989 H  HB2  . LEU   B 1 127 ? 38.160 -25.261 0.170   1.00 16.27 ?  127 LEU   B HB2  1 
ATOM   5990 H  HB3  . LEU   B 1 127 ? 39.084 -24.633 1.289   1.00 16.27 ?  127 LEU   B HB3  1 
ATOM   5991 H  HG   . LEU   B 1 127 ? 39.139 -23.879 -1.424  1.00 16.69 ?  127 LEU   B HG   1 
ATOM   5992 H  HD11 . LEU   B 1 127 ? 38.208 -21.869 -0.705  1.00 17.02 ?  127 LEU   B HD11 1 
ATOM   5993 H  HD12 . LEU   B 1 127 ? 37.241 -23.086 -0.375  1.00 17.02 ?  127 LEU   B HD12 1 
ATOM   5994 H  HD13 . LEU   B 1 127 ? 38.130 -22.444 0.775   1.00 17.02 ?  127 LEU   B HD13 1 
ATOM   5995 H  HD21 . LEU   B 1 127 ? 40.605 -22.151 -0.743  1.00 17.40 ?  127 LEU   B HD21 1 
ATOM   5996 H  HD22 . LEU   B 1 127 ? 40.695 -22.835 0.688   1.00 17.40 ?  127 LEU   B HD22 1 
ATOM   5997 H  HD23 . LEU   B 1 127 ? 41.265 -23.588 -0.589  1.00 17.40 ?  127 LEU   B HD23 1 
ATOM   5998 N  N    . SER   B 1 128 ? 40.471 -27.070 2.273   1.00 12.81 ?  128 SER   B N    1 
ATOM   5999 C  CA   . SER   B 1 128 ? 40.349 -27.980 3.399   1.00 13.40 ?  128 SER   B CA   1 
ATOM   6000 C  C    . SER   B 1 128 ? 40.840 -29.391 3.086   1.00 14.66 ?  128 SER   B C    1 
ATOM   6001 O  O    . SER   B 1 128 ? 40.734 -30.266 3.941   1.00 15.88 ?  128 SER   B O    1 
ATOM   6002 C  CB   . SER   B 1 128 ? 38.943 -27.982 4.017   1.00 13.66 ?  128 SER   B CB   1 
ATOM   6003 O  OG   . SER   B 1 128 ? 38.640 -26.705 4.572   1.00 14.42 ?  128 SER   B OG   1 
ATOM   6004 H  H    . SER   B 1 128 ? 41.048 -26.447 2.420   1.00 15.38 ?  128 SER   B H    1 
ATOM   6005 H  HA   . SER   B 1 128 ? 40.932 -27.645 4.087   1.00 16.07 ?  128 SER   B HA   1 
ATOM   6006 H  HB2  . SER   B 1 128 ? 38.287 -28.203 3.332   1.00 16.39 ?  128 SER   B HB2  1 
ATOM   6007 H  HB3  . SER   B 1 128 ? 38.909 -28.656 4.725   1.00 16.39 ?  128 SER   B HB3  1 
ATOM   6008 H  HG   . SER   B 1 128 ? 39.208 -26.515 5.161   1.00 17.30 ?  128 SER   B HG   1 
ATOM   6009 N  N    . ALA   B 1 129 ? 41.420 -29.621 1.906   1.00 15.68 ?  129 ALA   B N    1 
ATOM   6010 C  CA   . ALA   B 1 129 ? 41.964 -30.922 1.548   1.00 16.67 ?  129 ALA   B CA   1 
ATOM   6011 C  C    . ALA   B 1 129 ? 43.358 -31.097 2.135   1.00 15.67 ?  129 ALA   B C    1 
ATOM   6012 O  O    . ALA   B 1 129 ? 43.918 -30.194 2.767   1.00 15.47 ?  129 ALA   B O    1 
ATOM   6013 C  CB   . ALA   B 1 129 ? 42.026 -31.071 0.030   1.00 18.34 ?  129 ALA   B CB   1 
ATOM   6014 H  H    . ALA   B 1 129 ? 41.511 -29.028 1.287   1.00 18.82 ?  129 ALA   B H    1 
ATOM   6015 H  HA   . ALA   B 1 129 ? 41.393 -31.617 1.900   1.00 20.01 ?  129 ALA   B HA   1 
ATOM   6016 H  HB1  . ALA   B 1 129 ? 42.380 -31.950 -0.188  1.00 22.01 ?  129 ALA   B HB1  1 
ATOM   6017 H  HB2  . ALA   B 1 129 ? 41.134 -30.975 -0.333  1.00 22.01 ?  129 ALA   B HB2  1 
ATOM   6018 H  HB3  . ALA   B 1 129 ? 42.609 -30.384 -0.334  1.00 22.01 ?  129 ALA   B HB3  1 
ATOM   6019 N  N    . GLY   B 1 130 ? 43.927 -32.280 1.899   1.00 15.58 ?  130 GLY   B N    1 
ATOM   6020 C  CA   . GLY   B 1 130 ? 45.318 -32.517 2.247   1.00 16.24 ?  130 GLY   B CA   1 
ATOM   6021 C  C    . GLY   B 1 130 ? 45.533 -32.420 3.738   1.00 16.36 ?  130 GLY   B C    1 
ATOM   6022 O  O    . GLY   B 1 130 ? 44.832 -33.059 4.536   1.00 17.01 ?  130 GLY   B O    1 
ATOM   6023 H  H    . GLY   B 1 130 ? 43.532 -32.953 1.534   1.00 18.70 ?  130 GLY   B H    1 
ATOM   6024 H  HA2  . GLY   B 1 130 ? 45.584 -33.403 1.954   1.00 19.49 ?  130 GLY   B HA2  1 
ATOM   6025 H  HA3  . GLY   B 1 130 ? 45.882 -31.863 1.808   1.00 19.49 ?  130 GLY   B HA3  1 
ATOM   6026 N  N    . ILE   B 1 131 ? 46.510 -31.593 4.127   1.00 16.69 ?  131 ILE   B N    1 
ATOM   6027 C  CA   . ILE   B 1 131 ? 46.866 -31.462 5.532   1.00 17.40 ?  131 ILE   B CA   1 
ATOM   6028 C  C    . ILE   B 1 131 ? 45.749 -30.859 6.366   1.00 16.55 ?  131 ILE   B C    1 
ATOM   6029 O  O    . ILE   B 1 131 ? 45.823 -30.923 7.597   1.00 18.08 ?  131 ILE   B O    1 
ATOM   6030 C  CB   . ILE   B 1 131 ? 48.191 -30.691 5.735   1.00 19.02 ?  131 ILE   B CB   1 
ATOM   6031 C  CG1  . ILE   B 1 131 ? 48.027 -29.207 5.380   1.00 20.14 ?  131 ILE   B CG1  1 
ATOM   6032 C  CG2  . ILE   B 1 131 ? 49.314 -31.329 4.916   1.00 19.93 ?  131 ILE   B CG2  1 
ATOM   6033 C  CD1  . ILE   B 1 131 ? 49.245 -28.354 5.695   1.00 21.45 ?  131 ILE   B CD1  1 
ATOM   6034 H  H    . ILE   B 1 131 ? 46.974 -31.095 3.599   1.00 20.03 ?  131 ILE   B H    1 
ATOM   6035 H  HA   . ILE   B 1 131 ? 47.008 -32.349 5.881   1.00 20.88 ?  131 ILE   B HA   1 
ATOM   6036 H  HB   . ILE   B 1 131 ? 48.429 -30.750 6.673   1.00 22.83 ?  131 ILE   B HB   1 
ATOM   6037 H  HG12 . ILE   B 1 131 ? 47.849 -29.134 4.431   1.00 24.17 ?  131 ILE   B HG12 1 
ATOM   6038 H  HG13 . ILE   B 1 131 ? 47.280 -28.839 5.882   1.00 24.17 ?  131 ILE   B HG13 1 
ATOM   6039 H  HG21 . ILE   B 1 131 ? 50.153 -30.923 5.170   1.00 23.91 ?  131 ILE   B HG21 1 
ATOM   6040 H  HG22 . ILE   B 1 131 ? 49.328 -32.278 5.096   1.00 23.91 ?  131 ILE   B HG22 1 
ATOM   6041 H  HG23 . ILE   B 1 131 ? 49.137 -31.170 3.974   1.00 23.91 ?  131 ILE   B HG23 1 
ATOM   6042 H  HD11 . ILE   B 1 131 ? 49.025 -27.423 5.533   1.00 25.75 ?  131 ILE   B HD11 1 
ATOM   6043 H  HD12 . ILE   B 1 131 ? 49.484 -28.479 6.627   1.00 25.75 ?  131 ILE   B HD12 1 
ATOM   6044 H  HD13 . ILE   B 1 131 ? 49.977 -28.627 5.124   1.00 25.75 ?  131 ILE   B HD13 1 
ATOM   6045 N  N    . PHE   B 1 132 ? 44.717 -30.280 5.736   1.00 15.38 ?  132 PHE   B N    1 
ATOM   6046 C  CA   . PHE   B 1 132 ? 43.559 -29.773 6.465   1.00 15.74 ?  132 PHE   B CA   1 
ATOM   6047 C  C    . PHE   B 1 132 ? 42.532 -30.859 6.794   1.00 17.24 ?  132 PHE   B C    1 
ATOM   6048 O  O    . PHE   B 1 132 ? 41.620 -30.601 7.588   1.00 18.80 ?  132 PHE   B O    1 
ATOM   6049 C  CB   . PHE   B 1 132 ? 42.878 -28.638 5.685   1.00 14.83 ?  132 PHE   B CB   1 
ATOM   6050 C  CG   . PHE   B 1 132 ? 43.576 -27.295 5.793   1.00 14.79 ?  132 PHE   B CG   1 
ATOM   6051 C  CD1  . PHE   B 1 132 ? 44.864 -27.116 5.315   1.00 15.35 ?  132 PHE   B CD1  1 
ATOM   6052 C  CD2  . PHE   B 1 132 ? 42.908 -26.194 6.317   1.00 14.50 ?  132 PHE   B CD2  1 
ATOM   6053 C  CE1  . PHE   B 1 132 ? 45.487 -25.874 5.401   1.00 16.12 ?  132 PHE   B CE1  1 
ATOM   6054 C  CE2  . PHE   B 1 132 ? 43.519 -24.951 6.397   1.00 14.99 ?  132 PHE   B CE2  1 
ATOM   6055 C  CZ   . PHE   B 1 132 ? 44.809 -24.795 5.943   1.00 15.99 ?  132 PHE   B CZ   1 
ATOM   6056 H  H    . PHE   B 1 132 ? 44.662 -30.173 4.882   1.00 18.45 ?  132 PHE   B H    1 
ATOM   6057 H  HA   . PHE   B 1 132 ? 43.863 -29.402 7.305   1.00 18.89 ?  132 PHE   B HA   1 
ATOM   6058 H  HB2  . PHE   B 1 132 ? 42.857 -28.879 4.748   1.00 17.80 ?  132 PHE   B HB2  1 
ATOM   6059 H  HB3  . PHE   B 1 132 ? 41.972 -28.528 6.017   1.00 17.80 ?  132 PHE   B HB3  1 
ATOM   6060 H  HD1  . PHE   B 1 132 ? 45.326 -27.843 4.957   1.00 18.42 ?  132 PHE   B HD1  1 
ATOM   6061 H  HD2  . PHE   B 1 132 ? 42.039 -26.294 6.631   1.00 17.40 ?  132 PHE   B HD2  1 
ATOM   6062 H  HE1  . PHE   B 1 132 ? 46.359 -25.773 5.093   1.00 19.34 ?  132 PHE   B HE1  1 
ATOM   6063 H  HE2  . PHE   B 1 132 ? 43.066 -24.227 6.767   1.00 17.98 ?  132 PHE   B HE2  1 
ATOM   6064 H  HZ   . PHE   B 1 132 ? 45.226 -23.964 6.002   1.00 19.18 ?  132 PHE   B HZ   1 
ATOM   6065 N  N    . GLY   B 1 133 ? 42.632 -32.057 6.201   1.00 16.82 ?  133 GLY   B N    1 
ATOM   6066 C  CA   . GLY   B 1 133 ? 41.913 -33.218 6.698   1.00 17.72 ?  133 GLY   B CA   1 
ATOM   6067 C  C    . GLY   B 1 133 ? 40.515 -33.477 6.164   1.00 18.13 ?  133 GLY   B C    1 
ATOM   6068 O  O    . GLY   B 1 133 ? 39.929 -34.501 6.526   1.00 20.13 ?  133 GLY   B O    1 
ATOM   6069 H  H    . GLY   B 1 133 ? 43.123 -32.216 5.509   1.00 20.19 ?  133 GLY   B H    1 
ATOM   6070 H  HA2  . GLY   B 1 133 ? 42.446 -34.004 6.511   1.00 21.27 ?  133 GLY   B HA2  1 
ATOM   6071 H  HA3  . GLY   B 1 133 ? 41.842 -33.134 7.661   1.00 21.27 ?  133 GLY   B HA3  1 
ATOM   6072 N  N    . ALA   B 1 134 ? 39.950 -32.605 5.334   1.00 17.16 ?  134 ALA   B N    1 
ATOM   6073 C  CA   . ALA   B 1 134 ? 38.628 -32.897 4.798   1.00 17.13 ?  134 ALA   B CA   1 
ATOM   6074 C  C    . ALA   B 1 134 ? 38.721 -33.892 3.645   1.00 17.33 ?  134 ALA   B C    1 
ATOM   6075 O  O    . ALA   B 1 134 ? 39.777 -34.083 3.035   1.00 18.46 ?  134 ALA   B O    1 
ATOM   6076 C  CB   . ALA   B 1 134 ? 37.946 -31.616 4.320   1.00 17.34 ?  134 ALA   B CB   1 
ATOM   6077 H  H    . ALA   B 1 134 ? 40.294 -31.852 5.085   1.00 20.59 ?  134 ALA   B H    1 
ATOM   6078 H  HA   . ALA   B 1 134 ? 38.081 -33.284 5.499   1.00 20.56 ?  134 ALA   B HA   1 
ATOM   6079 H  HB1  . ALA   B 1 134 ? 37.062 -31.838 3.986   1.00 20.81 ?  134 ALA   B HB1  1 
ATOM   6080 H  HB2  . ALA   B 1 134 ? 37.874 -30.997 5.063   1.00 20.81 ?  134 ALA   B HB2  1 
ATOM   6081 H  HB3  . ALA   B 1 134 ? 38.478 -31.221 3.610   1.00 20.81 ?  134 ALA   B HB3  1 
ATOM   6082 N  N    . ASP   B 1 135 ? 37.590 -34.524 3.354   1.00 17.87 ?  135 ASP   B N    1 
ATOM   6083 C  CA   . ASP   B 1 135 ? 37.489 -35.414 2.206   1.00 18.37 ?  135 ASP   B CA   1 
ATOM   6084 C  C    . ASP   B 1 135 ? 37.589 -34.576 0.938   1.00 17.15 ?  135 ASP   B C    1 
ATOM   6085 O  O    . ASP   B 1 135 ? 36.738 -33.700 0.717   1.00 17.14 ?  135 ASP   B O    1 
ATOM   6086 C  CB   . ASP   B 1 135 ? 36.148 -36.141 2.258   1.00 20.27 ?  135 ASP   B CB   1 
ATOM   6087 C  CG   . ASP   B 1 135 ? 35.972 -37.140 1.134   1.00 22.20 ?  135 ASP   B CG   1 
ATOM   6088 O  OD1  . ASP   B 1 135 ? 36.833 -37.197 0.231   1.00 22.10 ?  135 ASP   B OD1  1 
ATOM   6089 O  OD2  . ASP   B 1 135 ? 34.975 -37.895 1.171   1.00 25.09 -1 135 ASP   B OD2  1 
ATOM   6090 H  H    . ASP   B 1 135 ? 36.865 -34.456 3.809   1.00 21.45 ?  135 ASP   B H    1 
ATOM   6091 H  HA   . ASP   B 1 135 ? 38.206 -36.072 2.237   1.00 22.05 ?  135 ASP   B HA   1 
ATOM   6092 H  HB2  . ASP   B 1 135 ? 36.082 -36.621 3.097   1.00 24.32 ?  135 ASP   B HB2  1 
ATOM   6093 H  HB3  . ASP   B 1 135 ? 35.437 -35.489 2.187   1.00 24.32 ?  135 ASP   B HB3  1 
ATOM   6094 N  N    . PRO   B 1 136 ? 38.597 -34.789 0.089   1.00 17.17 ?  136 PRO   B N    1 
ATOM   6095 C  CA   . PRO   B 1 136 ? 38.695 -33.972 -1.130  1.00 16.25 ?  136 PRO   B CA   1 
ATOM   6096 C  C    . PRO   B 1 136 ? 37.499 -34.120 -2.049  1.00 15.72 ?  136 PRO   B C    1 
ATOM   6097 O  O    . PRO   B 1 136 ? 37.176 -33.170 -2.770  1.00 15.20 ?  136 PRO   B O    1 
ATOM   6098 C  CB   . PRO   B 1 136 ? 40.003 -34.452 -1.777  1.00 17.14 ?  136 PRO   B CB   1 
ATOM   6099 C  CG   . PRO   B 1 136 ? 40.211 -35.838 -1.228  1.00 18.49 ?  136 PRO   B CG   1 
ATOM   6100 C  CD   . PRO   B 1 136 ? 39.675 -35.790 0.174   1.00 18.35 ?  136 PRO   B CD   1 
ATOM   6101 H  HA   . PRO   B 1 136 ? 38.786 -33.040 -0.895  1.00 19.50 ?  136 PRO   B HA   1 
ATOM   6102 H  HB2  . PRO   B 1 136 ? 39.906 -34.475 -2.744  1.00 20.56 ?  136 PRO   B HB2  1 
ATOM   6103 H  HB3  . PRO   B 1 136 ? 40.730 -33.865 -1.520  1.00 20.56 ?  136 PRO   B HB3  1 
ATOM   6104 H  HG2  . PRO   B 1 136 ? 39.715 -36.483 -1.760  1.00 22.19 ?  136 PRO   B HG2  1 
ATOM   6105 H  HG3  . PRO   B 1 136 ? 41.157 -36.055 -1.225  1.00 22.19 ?  136 PRO   B HG3  1 
ATOM   6106 H  HD2  . PRO   B 1 136 ? 39.320 -36.656 0.431   1.00 22.02 ?  136 PRO   B HD2  1 
ATOM   6107 H  HD3  . PRO   B 1 136 ? 40.363 -35.491 0.792   1.00 22.02 ?  136 PRO   B HD3  1 
ATOM   6108 N  N    . ILE   B 1 137 ? 36.839 -35.285 -2.050  1.00 16.19 ?  137 ILE   B N    1 
ATOM   6109 C  CA   . ILE   B 1 137 ? 35.619 -35.454 -2.836  1.00 16.68 ?  137 ILE   B CA   1 
ATOM   6110 C  C    . ILE   B 1 137 ? 34.549 -34.482 -2.359  1.00 16.20 ?  137 ILE   B C    1 
ATOM   6111 O  O    . ILE   B 1 137 ? 33.837 -33.867 -3.164  1.00 15.46 ?  137 ILE   B O    1 
ATOM   6112 C  CB   . ILE   B 1 137 ? 35.142 -36.920 -2.771  1.00 18.46 ?  137 ILE   B CB   1 
ATOM   6113 C  CG1  . ILE   B 1 137 ? 36.142 -37.833 -3.486  1.00 20.75 ?  137 ILE   B CG1  1 
ATOM   6114 C  CG2  . ILE   B 1 137 ? 33.734 -37.057 -3.366  1.00 18.88 ?  137 ILE   B CG2  1 
ATOM   6115 C  CD1  . ILE   B 1 137 ? 35.822 -39.310 -3.374  1.00 23.05 ?  137 ILE   B CD1  1 
ATOM   6116 H  H    . ILE   B 1 137 ? 37.075 -35.990 -1.612  1.00 19.43 ?  137 ILE   B H    1 
ATOM   6117 H  HA   . ILE   B 1 137 ? 35.812 -35.253 -3.766  1.00 20.01 ?  137 ILE   B HA   1 
ATOM   6118 H  HB   . ILE   B 1 137 ? 35.098 -37.187 -1.844  1.00 22.15 ?  137 ILE   B HB   1 
ATOM   6119 H  HG12 . ILE   B 1 137 ? 36.158 -37.610 -4.429  1.00 24.90 ?  137 ILE   B HG12 1 
ATOM   6120 H  HG13 . ILE   B 1 137 ? 37.019 -37.697 -3.099  1.00 24.90 ?  137 ILE   B HG13 1 
ATOM   6121 H  HG21 . ILE   B 1 137 ? 33.476 -37.995 -3.390  1.00 22.65 ?  137 ILE   B HG21 1 
ATOM   6122 H  HG22 . ILE   B 1 137 ? 33.099 -36.576 -2.813  1.00 22.65 ?  137 ILE   B HG22 1 
ATOM   6123 H  HG23 . ILE   B 1 137 ? 33.729 -36.697 -4.266  1.00 22.65 ?  137 ILE   B HG23 1 
ATOM   6124 H  HD11 . ILE   B 1 137 ? 36.453 -39.798 -3.921  1.00 27.67 ?  137 ILE   B HD11 1 
ATOM   6125 H  HD12 . ILE   B 1 137 ? 35.899 -39.586 -2.447  1.00 27.67 ?  137 ILE   B HD12 1 
ATOM   6126 H  HD13 . ILE   B 1 137 ? 34.923 -39.480 -3.697  1.00 27.67 ?  137 ILE   B HD13 1 
ATOM   6127 N  N    . HIS   B 1 138 ? 34.421 -34.324 -1.043  1.00 16.20 ?  138 HIS   B N    1 
ATOM   6128 C  CA   . HIS   B 1 138 ? 33.468 -33.359 -0.508  1.00 16.65 ?  138 HIS   B CA   1 
ATOM   6129 C  C    . HIS   B 1 138 ? 33.882 -31.929 -0.835  1.00 15.60 ?  138 HIS   B C    1 
ATOM   6130 O  O    . HIS   B 1 138 ? 33.034 -31.082 -1.141  1.00 16.07 ?  138 HIS   B O    1 
ATOM   6131 C  CB   . HIS   B 1 138 ? 33.354 -33.531 1.000   1.00 17.82 ?  138 HIS   B CB   1 
ATOM   6132 C  CG   . HIS   B 1 138 ? 32.422 -32.553 1.635   1.00 18.96 ?  138 HIS   B CG   1 
ATOM   6133 N  ND1  . HIS   B 1 138 ? 31.087 -32.478 1.301   1.00 20.36 ?  138 HIS   B ND1  1 
ATOM   6134 C  CD2  . HIS   B 1 138 ? 32.637 -31.582 2.553   1.00 19.61 ?  138 HIS   B CD2  1 
ATOM   6135 C  CE1  . HIS   B 1 138 ? 30.515 -31.516 2.002   1.00 20.65 ?  138 HIS   B CE1  1 
ATOM   6136 N  NE2  . HIS   B 1 138 ? 31.432 -30.960 2.773   1.00 19.96 ?  138 HIS   B NE2  1 
ATOM   6137 H  H    . HIS   B 1 138 ? 34.871 -34.759 -0.453  1.00 19.44 ?  138 HIS   B H    1 
ATOM   6138 H  HA   . HIS   B 1 138 ? 32.597 -33.525 -0.901  1.00 19.98 ?  138 HIS   B HA   1 
ATOM   6139 H  HB2  . HIS   B 1 138 ? 33.020 -34.423 1.190   1.00 21.39 ?  138 HIS   B HB2  1 
ATOM   6140 H  HB3  . HIS   B 1 138 ? 34.228 -33.413 1.398   1.00 21.39 ?  138 HIS   B HB3  1 
ATOM   6141 H  HD1  . HIS   B 1 138 ? 30.687 -32.984 0.729   1.00 24.43 ?  138 HIS   B HD1  1 
ATOM   6142 H  HD2  . HIS   B 1 138 ? 33.439 -31.383 2.974   1.00 23.53 ?  138 HIS   B HD2  1 
ATOM   6143 H  HE1  . HIS   B 1 138 ? 29.613 -31.279 1.962   1.00 24.78 ?  138 HIS   B HE1  1 
ATOM   6144 N  N    . SER   B 1 139 ? 35.178 -31.632 -0.762  1.00 15.09 ?  139 SER   B N    1 
ATOM   6145 C  CA   . SER   B 1 139 ? 35.622 -30.283 -1.085  1.00 14.44 ?  139 SER   B CA   1 
ATOM   6146 C  C    . SER   B 1 139 ? 35.286 -29.935 -2.526  1.00 13.72 ?  139 SER   B C    1 
ATOM   6147 O  O    . SER   B 1 139 ? 34.830 -28.821 -2.809  1.00 14.07 ?  139 SER   B O    1 
ATOM   6148 C  CB   . SER   B 1 139 ? 37.117 -30.144 -0.813  1.00 14.82 ?  139 SER   B CB   1 
ATOM   6149 O  OG   . SER   B 1 139 ? 37.537 -28.816 -1.062  1.00 14.99 ?  139 SER   B OG   1 
ATOM   6150 H  H    . SER   B 1 139 ? 35.798 -32.177 -0.535  1.00 18.11 ?  139 SER   B H    1 
ATOM   6151 H  HA   . SER   B 1 139 ? 35.153 -29.655 -0.519  1.00 17.33 ?  139 SER   B HA   1 
ATOM   6152 H  HB2  . SER   B 1 139 ? 37.290 -30.372 0.117   1.00 17.78 ?  139 SER   B HB2  1 
ATOM   6153 H  HB3  . SER   B 1 139 ? 37.608 -30.741 -1.397  1.00 17.78 ?  139 SER   B HB3  1 
ATOM   6154 H  HG   . SER   B 1 139 ? 38.362 -28.738 -0.891  1.00 17.98 ?  139 SER   B HG   1 
ATOM   6155 N  N    . LEU   B 1 140 ? 35.473 -30.883 -3.447  1.00 13.41 ?  140 LEU   B N    1 
ATOM   6156 C  CA   . LEU   B 1 140 ? 35.108 -30.637 -4.836  1.00 13.37 ?  140 LEU   B CA   1 
ATOM   6157 C  C    . LEU   B 1 140 ? 33.605 -30.409 -4.972  1.00 13.82 ?  140 LEU   B C    1 
ATOM   6158 O  O    . LEU   B 1 140 ? 33.171 -29.529 -5.720  1.00 13.77 ?  140 LEU   B O    1 
ATOM   6159 C  CB   . LEU   B 1 140 ? 35.580 -31.800 -5.710  1.00 13.55 ?  140 LEU   B CB   1 
ATOM   6160 C  CG   . LEU   B 1 140 ? 35.208 -31.694 -7.181  1.00 14.07 ?  140 LEU   B CG   1 
ATOM   6161 C  CD1  . LEU   B 1 140 ? 35.781 -30.421 -7.770  1.00 14.63 ?  140 LEU   B CD1  1 
ATOM   6162 C  CD2  . LEU   B 1 140 ? 35.686 -32.929 -7.923  1.00 14.99 ?  140 LEU   B CD2  1 
ATOM   6163 H  H    . LEU   B 1 140 ? 35.803 -31.663 -3.296  1.00 16.09 ?  140 LEU   B H    1 
ATOM   6164 H  HA   . LEU   B 1 140 ? 35.567 -29.838 -5.141  1.00 16.05 ?  140 LEU   B HA   1 
ATOM   6165 H  HB2  . LEU   B 1 140 ? 36.550 -31.859 -5.660  1.00 16.26 ?  140 LEU   B HB2  1 
ATOM   6166 H  HB3  . LEU   B 1 140 ? 35.190 -32.623 -5.374  1.00 16.26 ?  140 LEU   B HB3  1 
ATOM   6167 H  HG   . LEU   B 1 140 ? 34.243 -31.644 -7.260  1.00 16.88 ?  140 LEU   B HG   1 
ATOM   6168 H  HD11 . LEU   B 1 140 ? 35.683 -30.448 -8.732  1.00 17.56 ?  140 LEU   B HD11 1 
ATOM   6169 H  HD12 . LEU   B 1 140 ? 35.296 -29.657 -7.411  1.00 17.56 ?  140 LEU   B HD12 1 
ATOM   6170 H  HD13 . LEU   B 1 140 ? 36.719 -30.356 -7.531  1.00 17.56 ?  140 LEU   B HD13 1 
ATOM   6171 H  HD21 . LEU   B 1 140 ? 35.437 -32.842 -8.857  1.00 17.99 ?  140 LEU   B HD21 1 
ATOM   6172 H  HD22 . LEU   B 1 140 ? 36.643 -32.997 -7.834  1.00 17.99 ?  140 LEU   B HD22 1 
ATOM   6173 H  HD23 . LEU   B 1 140 ? 35.253 -33.705 -7.535  1.00 17.99 ?  140 LEU   B HD23 1 
ATOM   6174 N  N    . ARG   B 1 141 ? 32.801 -31.198 -4.254  1.00 13.60 ?  141 ARG   B N    1 
ATOM   6175 C  CA   . ARG   B 1 141 ? 31.352 -31.020 -4.232  1.00 15.06 ?  141 ARG   B CA   1 
ATOM   6176 C  C    . ARG   B 1 141 ? 30.976 -29.606 -3.812  1.00 14.49 ?  141 ARG   B C    1 
ATOM   6177 O  O    . ARG   B 1 141 ? 30.173 -28.935 -4.477  1.00 14.50 ?  141 ARG   B O    1 
ATOM   6178 C  CB   . ARG   B 1 141 ? 30.765 -32.041 -3.249  1.00 16.39 ?  141 ARG   B CB   1 
ATOM   6179 C  CG   . ARG   B 1 141 ? 29.293 -31.939 -2.944  1.00 18.08 ?  141 ARG   B CG   1 
ATOM   6180 C  CD   . ARG   B 1 141 ? 28.522 -32.600 -4.014  1.00 19.76 ?  141 ARG   B CD   1 
ATOM   6181 N  NE   . ARG   B 1 141 ? 28.240 -31.687 -5.110  1.00 20.00 ?  141 ARG   B NE   1 
ATOM   6182 C  CZ   . ARG   B 1 141 ? 28.219 -32.033 -6.389  1.00 19.47 ?  141 ARG   B CZ   1 
ATOM   6183 N  NH1  . ARG   B 1 141 ? 28.649 -33.218 -6.794  1.00 19.08 ?  141 ARG   B NH1  1 
ATOM   6184 N  NH2  . ARG   B 1 141 ? 27.750 -31.170 -7.284  1.00 19.98 ?  141 ARG   B NH2  1 
ATOM   6185 H  H    . ARG   B 1 141 ? 33.082 -31.844 -3.765  1.00 16.31 ?  141 ARG   B H    1 
ATOM   6186 H  HA   . ARG   B 1 141 ? 30.988 -31.182 -5.111  1.00 18.07 ?  141 ARG   B HA   1 
ATOM   6187 H  HB2  . ARG   B 1 141 ? 30.936 -32.928 -3.604  1.00 19.67 ?  141 ARG   B HB2  1 
ATOM   6188 H  HB3  . ARG   B 1 141 ? 31.234 -31.948 -2.406  1.00 19.67 ?  141 ARG   B HB3  1 
ATOM   6189 H  HG2  . ARG   B 1 141 ? 29.112 -32.380 -2.103  1.00 21.70 ?  141 ARG   B HG2  1 
ATOM   6190 H  HG3  . ARG   B 1 141 ? 29.027 -31.003 -2.897  1.00 21.70 ?  141 ARG   B HG3  1 
ATOM   6191 H  HD2  . ARG   B 1 141 ? 29.029 -33.356 -4.355  1.00 23.71 ?  141 ARG   B HD2  1 
ATOM   6192 H  HD3  . ARG   B 1 141 ? 27.685 -32.911 -3.646  1.00 23.71 ?  141 ARG   B HD3  1 
ATOM   6193 H  HE   . ARG   B 1 141 ? 28.039 -30.875 -4.909  1.00 24.00 ?  141 ARG   B HE   1 
ATOM   6194 H  HH11 . ARG   B 1 141 ? 28.946 -33.794 -6.227  1.00 22.90 ?  141 ARG   B HH11 1 
ATOM   6195 H  HH12 . ARG   B 1 141 ? 28.637 -33.414 -7.629  1.00 22.90 ?  141 ARG   B HH12 1 
ATOM   6196 H  HH21 . ARG   B 1 141 ? 27.473 -30.393 -7.032  1.00 23.98 ?  141 ARG   B HH21 1 
ATOM   6197 H  HH22 . ARG   B 1 141 ? 27.751 -31.371 -8.120  1.00 23.98 ?  141 ARG   B HH22 1 
ATOM   6198 N  N    . VAL   B 1 142 ? 31.520 -29.154 -2.682  1.00 14.28 ?  142 VAL   B N    1 
ATOM   6199 C  CA   . VAL   B 1 142 ? 31.188 -27.819 -2.197  1.00 14.18 ?  142 VAL   B CA   1 
ATOM   6200 C  C    . VAL   B 1 142 ? 31.662 -26.762 -3.186  1.00 13.81 ?  142 VAL   B C    1 
ATOM   6201 O  O    . VAL   B 1 142 ? 30.960 -25.778 -3.444  1.00 14.23 ?  142 VAL   B O    1 
ATOM   6202 C  CB   . VAL   B 1 142 ? 31.735 -27.595 -0.773  1.00 14.60 ?  142 VAL   B CB   1 
ATOM   6203 C  CG1  . VAL   B 1 142 ? 31.434 -26.171 -0.303  1.00 14.42 ?  142 VAL   B CG1  1 
ATOM   6204 C  CG2  . VAL   B 1 142 ? 31.132 -28.613 0.184   1.00 15.24 ?  142 VAL   B CG2  1 
ATOM   6205 H  H    . VAL   B 1 142 ? 32.078 -29.587 -2.187  1.00 17.13 ?  142 VAL   B H    1 
ATOM   6206 H  HA   . VAL   B 1 142 ? 30.229 -27.746 -2.142  1.00 17.02 ?  142 VAL   B HA   1 
ATOM   6207 H  HB   . VAL   B 1 142 ? 32.700 -27.717 -0.774  1.00 17.52 ?  142 VAL   B HB   1 
ATOM   6208 H  HG11 . VAL   B 1 142 ? 31.628 -26.103 0.644   1.00 17.31 ?  142 VAL   B HG11 1 
ATOM   6209 H  HG12 . VAL   B 1 142 ? 31.999 -25.549 -0.796  1.00 17.31 ?  142 VAL   B HG12 1 
ATOM   6210 H  HG13 . VAL   B 1 142 ? 30.503 -25.974 -0.469  1.00 17.31 ?  142 VAL   B HG13 1 
ATOM   6211 H  HG21 . VAL   B 1 142 ? 31.446 -28.429 1.082   1.00 18.28 ?  142 VAL   B HG21 1 
ATOM   6212 H  HG22 . VAL   B 1 142 ? 30.165 -28.542 0.148   1.00 18.28 ?  142 VAL   B HG22 1 
ATOM   6213 H  HG23 . VAL   B 1 142 ? 31.407 -29.504 -0.087  1.00 18.28 ?  142 VAL   B HG23 1 
ATOM   6214 N  N    . CYS   B 1 143 ? 32.842 -26.957 -3.774  1.00 13.24 ?  143 CYS   B N    1 
ATOM   6215 C  CA   . CYS   B 1 143 ? 33.335 -26.022 -4.782  1.00 13.15 ?  143 CYS   B CA   1 
ATOM   6216 C  C    . CYS   B 1 143 ? 32.335 -25.882 -5.924  1.00 13.05 ?  143 CYS   B C    1 
ATOM   6217 O  O    . CYS   B 1 143 ? 31.935 -24.771 -6.291  1.00 13.10 ?  143 CYS   B O    1 
ATOM   6218 C  CB   . CYS   B 1 143 ? 34.684 -26.514 -5.313  1.00 13.71 ?  143 CYS   B CB   1 
ATOM   6219 S  SG   . CYS   B 1 143 ? 35.448 -25.416 -6.526  1.00 13.65 ?  143 CYS   B SG   1 
ATOM   6220 H  H    . CYS   B 1 143 ? 33.374 -27.609 -3.609  1.00 15.89 ?  143 CYS   B H    1 
ATOM   6221 H  HA   . CYS   B 1 143 ? 33.469 -25.146 -4.384  1.00 15.78 ?  143 CYS   B HA   1 
ATOM   6222 H  HB2  . CYS   B 1 143 ? 35.305 -26.606 -4.571  1.00 16.45 ?  143 CYS   B HB2  1 
ATOM   6223 H  HB3  . CYS   B 1 143 ? 34.560 -27.376 -5.736  1.00 16.45 ?  143 CYS   B HB3  1 
ATOM   6224 H  HG   . CYS   B 1 143 ? 36.521 -25.858 -6.849  1.00 16.38 ?  143 CYS   B HG   1 
ATOM   6225 N  N    . VAL   B 1 144 ? 31.934 -27.007 -6.514  1.00 13.70 ?  144 VAL   B N    1 
ATOM   6226 C  CA   . VAL   B 1 144 ? 31.022 -26.953 -7.651  1.00 14.58 ?  144 VAL   B CA   1 
ATOM   6227 C  C    . VAL   B 1 144 ? 29.684 -26.335 -7.274  1.00 14.47 ?  144 VAL   B C    1 
ATOM   6228 O  O    . VAL   B 1 144 ? 29.070 -25.628 -8.084  1.00 15.77 ?  144 VAL   B O    1 
ATOM   6229 C  CB   . VAL   B 1 144 ? 30.856 -28.373 -8.208  1.00 17.37 ?  144 VAL   B CB   1 
ATOM   6230 C  CG1  . VAL   B 1 144 ? 29.568 -28.507 -9.015  1.00 19.82 ?  144 VAL   B CG1  1 
ATOM   6231 C  CG2  . VAL   B 1 144 ? 32.090 -28.773 -9.019  1.00 17.27 ?  144 VAL   B CG2  1 
ATOM   6232 H  H    . VAL   B 1 144 ? 32.180 -27.798 -6.286  1.00 16.44 ?  144 VAL   B H    1 
ATOM   6233 H  HA   . VAL   B 1 144 ? 31.410 -26.406 -8.350  1.00 17.49 ?  144 VAL   B HA   1 
ATOM   6234 H  HB   . VAL   B 1 144 ? 30.793 -28.991 -7.461  1.00 20.85 ?  144 VAL   B HB   1 
ATOM   6235 H  HG11 . VAL   B 1 144 ? 29.630 -29.306 -9.567  1.00 23.78 ?  144 VAL   B HG11 1 
ATOM   6236 H  HG12 . VAL   B 1 144 ? 28.819 -28.594 -8.405  1.00 23.78 ?  144 VAL   B HG12 1 
ATOM   6237 H  HG13 . VAL   B 1 144 ? 29.461 -27.729 -9.576  1.00 23.78 ?  144 VAL   B HG13 1 
ATOM   6238 H  HG21 . VAL   B 1 144 ? 31.968 -29.674 -9.357  1.00 20.72 ?  144 VAL   B HG21 1 
ATOM   6239 H  HG22 . VAL   B 1 144 ? 32.190 -28.154 -9.762  1.00 20.72 ?  144 VAL   B HG22 1 
ATOM   6240 H  HG23 . VAL   B 1 144 ? 32.869 -28.733 -8.447  1.00 20.72 ?  144 VAL   B HG23 1 
ATOM   6241 N  N    . ASP   B 1 145 ? 29.216 -26.573 -6.054  1.00 14.73 ?  145 ASP   B N    1 
ATOM   6242 C  CA   . ASP   B 1 145 ? 27.907 -26.100 -5.628  1.00 15.60 ?  145 ASP   B CA   1 
ATOM   6243 C  C    . ASP   B 1 145 ? 27.935 -24.677 -5.087  1.00 14.94 ?  145 ASP   B C    1 
ATOM   6244 O  O    . ASP   B 1 145 ? 26.875 -24.133 -4.755  1.00 16.85 ?  145 ASP   B O    1 
ATOM   6245 C  CB   . ASP   B 1 145 ? 27.320 -27.021 -4.548  1.00 17.08 ?  145 ASP   B CB   1 
ATOM   6246 C  CG   . ASP   B 1 145 ? 26.957 -28.397 -5.059  1.00 18.74 ?  145 ASP   B CG   1 
ATOM   6247 O  OD1  . ASP   B 1 145 ? 26.848 -28.594 -6.286  1.00 18.77 ?  145 ASP   B OD1  1 
ATOM   6248 O  OD2  . ASP   B 1 145 ? 26.769 -29.285 -4.205  1.00 20.82 -1 145 ASP   B OD2  1 
ATOM   6249 H  H    . ASP   B 1 145 ? 29.652 -26.996 -5.442  1.00 17.68 ?  145 ASP   B H    1 
ATOM   6250 H  HA   . ASP   B 1 145 ? 27.312 -26.100 -6.390  1.00 18.72 ?  145 ASP   B HA   1 
ATOM   6251 H  HB2  . ASP   B 1 145 ? 27.969 -27.135 -3.847  1.00 20.50 ?  145 ASP   B HB2  1 
ATOM   6252 H  HB3  . ASP   B 1 145 ? 26.512 -26.609 -4.198  1.00 20.50 ?  145 ASP   B HB3  1 
ATOM   6253 N  N    . THR   B 1 146 ? 29.115 -24.059 -4.987  1.00 13.51 ?  146 THR   B N    1 
ATOM   6254 C  CA   . THR   B 1 146 ? 29.252 -22.736 -4.385  1.00 13.23 ?  146 THR   B CA   1 
ATOM   6255 C  C    . THR   B 1 146 ? 29.884 -21.710 -5.309  1.00 13.24 ?  146 THR   B C    1 
ATOM   6256 O  O    . THR   B 1 146 ? 29.433 -20.549 -5.359  1.00 13.39 ?  146 THR   B O    1 
ATOM   6257 C  CB   . THR   B 1 146 ? 30.083 -22.837 -3.097  1.00 13.33 ?  146 THR   B CB   1 
ATOM   6258 O  OG1  . THR   B 1 146 ? 29.507 -23.827 -2.238  1.00 14.02 ?  146 THR   B OG1  1 
ATOM   6259 C  CG2  . THR   B 1 146 ? 30.150 -21.496 -2.382  1.00 14.07 ?  146 THR   B CG2  1 
ATOM   6260 H  H    . THR   B 1 146 ? 29.865 -24.385 -5.267  1.00 16.22 ?  146 THR   B H    1 
ATOM   6261 H  HA   . THR   B 1 146 ? 28.377 -22.406 -4.144  1.00 15.87 ?  146 THR   B HA   1 
ATOM   6262 H  HB   . THR   B 1 146 ? 30.991 -23.094 -3.322  1.00 15.99 ?  146 THR   B HB   1 
ATOM   6263 H  HG1  . THR   B 1 146 ? 29.546 -24.587 -2.608  1.00 16.83 ?  146 THR   B HG1  1 
ATOM   6264 H  HG21 . THR   B 1 146 ? 30.503 -21.610 -1.487  1.00 16.88 ?  146 THR   B HG21 1 
ATOM   6265 H  HG22 . THR   B 1 146 ? 30.732 -20.885 -2.870  1.00 16.88 ?  146 THR   B HG22 1 
ATOM   6266 H  HG23 . THR   B 1 146 ? 29.265 -21.104 -2.325  1.00 16.88 ?  146 THR   B HG23 1 
ATOM   6267 N  N    . VAL   B 1 147 ? 30.945 -22.086 -6.009  1.00 12.70 ?  147 VAL   B N    1 
ATOM   6268 C  CA   . VAL   B 1 147 ? 31.672 -21.147 -6.849  1.00 12.57 ?  147 VAL   B CA   1 
ATOM   6269 C  C    . VAL   B 1 147 ? 30.934 -21.012 -8.168  1.00 12.77 ?  147 VAL   B C    1 
ATOM   6270 O  O    . VAL   B 1 147 ? 30.558 -22.015 -8.791  1.00 13.83 ?  147 VAL   B O    1 
ATOM   6271 C  CB   . VAL   B 1 147 ? 33.122 -21.610 -7.054  1.00 12.79 ?  147 VAL   B CB   1 
ATOM   6272 C  CG1  . VAL   B 1 147 ? 33.885 -20.578 -7.864  1.00 12.56 ?  147 VAL   B CG1  1 
ATOM   6273 C  CG2  . VAL   B 1 147 ? 33.801 -21.819 -5.712  1.00 12.64 ?  147 VAL   B CG2  1 
ATOM   6274 H  H    . VAL   B 1 147 ? 31.269 -22.888 -6.024  1.00 15.24 ?  147 VAL   B H    1 
ATOM   6275 H  HA   . VAL   B 1 147 ? 31.692 -20.279 -6.419  1.00 15.08 ?  147 VAL   B HA   1 
ATOM   6276 H  HB   . VAL   B 1 147 ? 33.134 -22.451 -7.543  1.00 15.34 ?  147 VAL   B HB   1 
ATOM   6277 H  HG11 . VAL   B 1 147 ? 34.827 -20.803 -7.860  1.00 15.07 ?  147 VAL   B HG11 1 
ATOM   6278 H  HG12 . VAL   B 1 147 ? 33.549 -20.573 -8.774  1.00 15.07 ?  147 VAL   B HG12 1 
ATOM   6279 H  HG13 . VAL   B 1 147 ? 33.753 -19.703 -7.460  1.00 15.07 ?  147 VAL   B HG13 1 
ATOM   6280 H  HG21 . VAL   B 1 147 ? 34.741 -22.013 -5.858  1.00 15.16 ?  147 VAL   B HG21 1 
ATOM   6281 H  HG22 . VAL   B 1 147 ? 33.710 -21.010 -5.185  1.00 15.16 ?  147 VAL   B HG22 1 
ATOM   6282 H  HG23 . VAL   B 1 147 ? 33.378 -22.562 -5.255  1.00 15.16 ?  147 VAL   B HG23 1 
ATOM   6283 N  N    . ARG   B 1 148 ? 30.730 -19.763 -8.592  1.00 12.61 ?  148 ARG   B N    1 
ATOM   6284 C  CA   . ARG   B 1 148 ? 30.107 -19.452 -9.866  1.00 12.73 ?  148 ARG   B CA   1 
ATOM   6285 C  C    . ARG   B 1 148 ? 31.061 -18.778 -10.840 1.00 12.92 ?  148 ARG   B C    1 
ATOM   6286 O  O    . ARG   B 1 148 ? 30.768 -18.746 -12.038 1.00 14.28 ?  148 ARG   B O    1 
ATOM   6287 C  CB   . ARG   B 1 148 ? 28.864 -18.571 -9.654  1.00 13.06 ?  148 ARG   B CB   1 
ATOM   6288 C  CG   . ARG   B 1 148 ? 27.784 -19.279 -8.838  1.00 13.89 ?  148 ARG   B CG   1 
ATOM   6289 C  CD   . ARG   B 1 148 ? 26.576 -18.389 -8.525  1.00 14.90 ?  148 ARG   B CD   1 
ATOM   6290 N  NE   . ARG   B 1 148 ? 26.961 -17.186 -7.798  1.00 15.22 ?  148 ARG   B NE   1 
ATOM   6291 C  CZ   . ARG   B 1 148 ? 27.266 -17.147 -6.507  1.00 14.15 ?  148 ARG   B CZ   1 
ATOM   6292 N  NH1  . ARG   B 1 148 ? 27.199 -18.231 -5.746  1.00 14.27 ?  148 ARG   B NH1  1 
ATOM   6293 N  NH2  . ARG   B 1 148 ? 27.657 -15.994 -5.968  1.00 13.92 ?  148 ARG   B NH2  1 
ATOM   6294 H  H    . ARG   B 1 148 ? 30.954 -19.060 -8.143  1.00 15.13 ?  148 ARG   B H    1 
ATOM   6295 H  HA   . ARG   B 1 148 ? 29.809 -20.278 -10.275 1.00 15.28 ?  148 ARG   B HA   1 
ATOM   6296 H  HB2  . ARG   B 1 148 ? 29.120 -17.766 -9.179  1.00 15.67 ?  148 ARG   B HB2  1 
ATOM   6297 H  HB3  . ARG   B 1 148 ? 28.485 -18.341 -10.519 1.00 15.67 ?  148 ARG   B HB3  1 
ATOM   6298 H  HG2  . ARG   B 1 148 ? 27.464 -20.049 -9.340  1.00 16.67 ?  148 ARG   B HG2  1 
ATOM   6299 H  HG3  . ARG   B 1 148 ? 28.165 -19.572 -7.996  1.00 16.67 ?  148 ARG   B HG3  1 
ATOM   6300 H  HD2  . ARG   B 1 148 ? 26.156 -18.121 -9.356  1.00 17.88 ?  148 ARG   B HD2  1 
ATOM   6301 H  HD3  . ARG   B 1 148 ? 25.947 -18.889 -7.979  1.00 17.88 ?  148 ARG   B HD3  1 
ATOM   6302 H  HE   . ARG   B 1 148 ? 27.002 -16.454 -8.239  1.00 18.26 ?  148 ARG   B HE   1 
ATOM   6303 H  HH11 . ARG   B 1 148 ? 26.946 -18.984 -6.080  1.00 17.12 ?  148 ARG   B HH11 1 
ATOM   6304 H  HH12 . ARG   B 1 148 ? 27.398 -18.184 -4.909  1.00 17.12 ?  148 ARG   B HH12 1 
ATOM   6305 H  HH21 . ARG   B 1 148 ? 27.709 -15.290 -6.455  1.00 16.70 ?  148 ARG   B HH21 1 
ATOM   6306 H  HH22 . ARG   B 1 148 ? 27.858 -15.958 -5.133  1.00 16.70 ?  148 ARG   B HH22 1 
ATOM   6307 N  N    . THR   B 1 149 ? 32.170 -18.223 -10.355 1.00 12.55 ?  149 THR   B N    1 
ATOM   6308 C  CA   . THR   B 1 149 ? 33.210 -17.664 -11.205 1.00 12.64 ?  149 THR   B CA   1 
ATOM   6309 C  C    . THR   B 1 149 ? 34.092 -18.805 -11.717 1.00 12.60 ?  149 THR   B C    1 
ATOM   6310 O  O    . THR   B 1 149 ? 33.897 -19.973 -11.374 1.00 12.99 ?  149 THR   B O    1 
ATOM   6311 C  CB   . THR   B 1 149 ? 33.987 -16.608 -10.428 1.00 13.01 ?  149 THR   B CB   1 
ATOM   6312 O  OG1  . THR   B 1 149 ? 34.444 -17.195 -9.210  1.00 13.07 ?  149 THR   B OG1  1 
ATOM   6313 C  CG2  . THR   B 1 149 ? 33.101 -15.393 -10.135 1.00 13.61 ?  149 THR   B CG2  1 
ATOM   6314 H  H    . THR   B 1 149 ? 32.336 -18.153 -9.515  1.00 15.06 ?  149 THR   B H    1 
ATOM   6315 H  HA   . THR   B 1 149 ? 32.803 -17.230 -11.968 1.00 15.17 ?  149 THR   B HA   1 
ATOM   6316 H  HB   . THR   B 1 149 ? 34.753 -16.320 -10.944 1.00 15.61 ?  149 THR   B HB   1 
ATOM   6317 H  HG1  . THR   B 1 149 ? 34.866 -16.623 -8.748  1.00 15.68 ?  149 THR   B HG1  1 
ATOM   6318 H  HG21 . THR   B 1 149 ? 33.609 -14.722 -9.648  1.00 16.33 ?  149 THR   B HG21 1 
ATOM   6319 H  HG22 . THR   B 1 149 ? 32.789 -15.005 -10.968 1.00 16.33 ?  149 THR   B HG22 1 
ATOM   6320 H  HG23 . THR   B 1 149 ? 32.337 -15.656 -9.602  1.00 16.33 ?  149 THR   B HG23 1 
ATOM   6321 N  N    . ASN   B 1 150 ? 35.059 -18.485 -12.570 1.00 12.54 ?  150 ASN   B N    1 
ATOM   6322 C  CA   . ASN   B 1 150 ? 35.827 -19.514 -13.264 1.00 12.86 ?  150 ASN   B CA   1 
ATOM   6323 C  C    . ASN   B 1 150 ? 36.989 -19.963 -12.387 1.00 12.86 ?  150 ASN   B C    1 
ATOM   6324 O  O    . ASN   B 1 150 ? 37.922 -19.191 -12.132 1.00 13.12 ?  150 ASN   B O    1 
ATOM   6325 C  CB   . ASN   B 1 150 ? 36.303 -18.988 -14.610 1.00 14.78 ?  150 ASN   B CB   1 
ATOM   6326 C  CG   . ASN   B 1 150 ? 35.160 -18.767 -15.557 1.00 17.68 ?  150 ASN   B CG   1 
ATOM   6327 O  OD1  . ASN   B 1 150 ? 34.264 -19.595 -15.645 1.00 18.49 ?  150 ASN   B OD1  1 
ATOM   6328 N  ND2  . ASN   B 1 150 ? 35.152 -17.636 -16.238 1.00 19.29 ?  150 ASN   B ND2  1 
ATOM   6329 H  H    . ASN   B 1 150 ? 35.298 -17.679 -12.760 1.00 15.05 ?  150 ASN   B H    1 
ATOM   6330 H  HA   . ASN   B 1 150 ? 35.252 -20.282 -13.424 1.00 15.43 ?  150 ASN   B HA   1 
ATOM   6331 H  HB2  . ASN   B 1 150 ? 36.751 -18.139 -14.480 1.00 17.73 ?  150 ASN   B HB2  1 
ATOM   6332 H  HB3  . ASN   B 1 150 ? 36.904 -19.631 -15.011 1.00 17.73 ?  150 ASN   B HB3  1 
ATOM   6333 H  HD21 . ASN   B 1 150 ? 34.511 -17.465 -16.789 1.00 23.15 ?  150 ASN   B HD21 1 
ATOM   6334 H  HD22 . ASN   B 1 150 ? 35.793 -17.073 -16.142 1.00 23.15 ?  150 ASN   B HD22 1 
ATOM   6335 N  N    . VAL   B 1 151 ? 36.941 -21.209 -11.927 1.00 12.53 ?  151 VAL   B N    1 
ATOM   6336 C  CA   . VAL   B 1 151 ? 37.959 -21.739 -11.033 1.00 12.55 ?  151 VAL   B CA   1 
ATOM   6337 C  C    . VAL   B 1 151 ? 38.663 -22.913 -11.706 1.00 12.25 ?  151 VAL   B C    1 
ATOM   6338 O  O    . VAL   B 1 151 ? 38.019 -23.846 -12.211 1.00 13.43 ?  151 VAL   B O    1 
ATOM   6339 C  CB   . VAL   B 1 151 ? 37.401 -22.078 -9.635  1.00 13.41 ?  151 VAL   B CB   1 
ATOM   6340 C  CG1  . VAL   B 1 151 ? 36.233 -23.065 -9.710  1.00 14.69 ?  151 VAL   B CG1  1 
ATOM   6341 C  CG2  . VAL   B 1 151 ? 38.514 -22.583 -8.725  1.00 13.80 ?  151 VAL   B CG2  1 
ATOM   6342 H  H    . VAL   B 1 151 ? 36.318 -21.772 -12.127 1.00 15.04 ?  151 VAL   B H    1 
ATOM   6343 H  HA   . VAL   B 1 151 ? 38.624 -21.045 -10.901 1.00 15.06 ?  151 VAL   B HA   1 
ATOM   6344 H  HB   . VAL   B 1 151 ? 37.055 -21.261 -9.240  1.00 16.09 ?  151 VAL   B HB   1 
ATOM   6345 H  HG11 . VAL   B 1 151 ? 35.918 -23.255 -8.811  1.00 17.63 ?  151 VAL   B HG11 1 
ATOM   6346 H  HG12 . VAL   B 1 151 ? 35.513 -22.673 -10.232 1.00 17.63 ?  151 VAL   B HG12 1 
ATOM   6347 H  HG13 . VAL   B 1 151 ? 36.535 -23.886 -10.132 1.00 17.63 ?  151 VAL   B HG13 1 
ATOM   6348 H  HG21 . VAL   B 1 151 ? 38.169 -22.653 -7.820  1.00 16.56 ?  151 VAL   B HG21 1 
ATOM   6349 H  HG22 . VAL   B 1 151 ? 38.807 -23.452 -9.035  1.00 16.56 ?  151 VAL   B HG22 1 
ATOM   6350 H  HG23 . VAL   B 1 151 ? 39.250 -21.952 -8.748  1.00 16.56 ?  151 VAL   B HG23 1 
ATOM   6351 N  N    . TYR   B 1 152 ? 39.995 -22.827 -11.727 1.00 11.76 ?  152 TYR   B N    1 
ATOM   6352 C  CA   . TYR   B 1 152 ? 40.900 -23.811 -12.303 1.00 12.14 ?  152 TYR   B CA   1 
ATOM   6353 C  C    . TYR   B 1 152 ? 41.624 -24.482 -11.139 1.00 11.54 ?  152 TYR   B C    1 
ATOM   6354 O  O    . TYR   B 1 152 ? 42.473 -23.861 -10.488 1.00 11.94 ?  152 TYR   B O    1 
ATOM   6355 C  CB   . TYR   B 1 152 ? 41.872 -23.108 -13.256 1.00 12.76 ?  152 TYR   B CB   1 
ATOM   6356 C  CG   . TYR   B 1 152 ? 41.190 -22.646 -14.525 1.00 13.49 ?  152 TYR   B CG   1 
ATOM   6357 C  CD1  . TYR   B 1 152 ? 40.532 -21.418 -14.591 1.00 13.81 ?  152 TYR   B CD1  1 
ATOM   6358 C  CD2  . TYR   B 1 152 ? 41.181 -23.452 -15.650 1.00 14.43 ?  152 TYR   B CD2  1 
ATOM   6359 C  CE1  . TYR   B 1 152 ? 39.887 -21.018 -15.745 1.00 15.22 ?  152 TYR   B CE1  1 
ATOM   6360 C  CE2  . TYR   B 1 152 ? 40.542 -23.063 -16.807 1.00 15.31 ?  152 TYR   B CE2  1 
ATOM   6361 C  CZ   . TYR   B 1 152 ? 39.900 -21.841 -16.852 1.00 15.41 ?  152 TYR   B CZ   1 
ATOM   6362 O  OH   . TYR   B 1 152 ? 39.267 -21.464 -18.012 1.00 18.13 ?  152 TYR   B OH   1 
ATOM   6363 H  H    . TYR   B 1 152 ? 40.424 -22.157 -11.382 1.00 14.11 ?  152 TYR   B H    1 
ATOM   6364 H  HA   . TYR   B 1 152 ? 40.391 -24.478 -12.793 1.00 14.57 ?  152 TYR   B HA   1 
ATOM   6365 H  HB2  . TYR   B 1 152 ? 42.245 -22.334 -12.807 1.00 15.31 ?  152 TYR   B HB2  1 
ATOM   6366 H  HB3  . TYR   B 1 152 ? 42.580 -23.726 -13.496 1.00 15.31 ?  152 TYR   B HB3  1 
ATOM   6367 H  HD1  . TYR   B 1 152 ? 40.518 -20.863 -13.842 1.00 16.57 ?  152 TYR   B HD1  1 
ATOM   6368 H  HD2  . TYR   B 1 152 ? 41.609 -24.279 -15.622 1.00 17.31 ?  152 TYR   B HD2  1 
ATOM   6369 H  HE1  . TYR   B 1 152 ? 39.456 -20.194 -15.781 1.00 18.26 ?  152 TYR   B HE1  1 
ATOM   6370 H  HE2  . TYR   B 1 152 ? 40.553 -23.616 -17.555 1.00 18.37 ?  152 TYR   B HE2  1 
ATOM   6371 H  HH   . TYR   B 1 152 ? 38.918 -20.704 -17.910 1.00 21.76 ?  152 TYR   B HH   1 
ATOM   6372 N  N    . LEU   B 1 153 ? 41.261 -25.738 -10.866 1.00 11.68 ?  153 LEU   B N    1 
ATOM   6373 C  CA   . LEU   B 1 153 ? 41.768 -26.485 -9.725  1.00 11.71 ?  153 LEU   B CA   1 
ATOM   6374 C  C    . LEU   B 1 153 ? 42.998 -27.286 -10.125 1.00 11.92 ?  153 LEU   B C    1 
ATOM   6375 O  O    . LEU   B 1 153 ? 42.977 -28.012 -11.124 1.00 12.83 ?  153 LEU   B O    1 
ATOM   6376 C  CB   . LEU   B 1 153 ? 40.691 -27.446 -9.208  1.00 11.66 ?  153 LEU   B CB   1 
ATOM   6377 C  CG   . LEU   B 1 153 ? 39.434 -26.786 -8.639  1.00 12.59 ?  153 LEU   B CG   1 
ATOM   6378 C  CD1  . LEU   B 1 153 ? 38.324 -27.821 -8.486  1.00 13.43 ?  153 LEU   B CD1  1 
ATOM   6379 C  CD2  . LEU   B 1 153 ? 39.733 -26.128 -7.302  1.00 13.18 ?  153 LEU   B CD2  1 
ATOM   6380 H  H    . LEU   B 1 153 ? 40.694 -26.191 -11.343 1.00 14.02 ?  153 LEU   B H    1 
ATOM   6381 H  HA   . LEU   B 1 153 ? 41.998 -25.870 -9.016  1.00 14.05 ?  153 LEU   B HA   1 
ATOM   6382 H  HB2  . LEU   B 1 153 ? 40.411 -28.020 -9.936  1.00 13.99 ?  153 LEU   B HB2  1 
ATOM   6383 H  HB3  . LEU   B 1 153 ? 41.077 -27.988 -8.499  1.00 13.99 ?  153 LEU   B HB3  1 
ATOM   6384 H  HG   . LEU   B 1 153 ? 39.125 -26.096 -9.251  1.00 15.10 ?  153 LEU   B HG   1 
ATOM   6385 H  HD11 . LEU   B 1 153 ? 37.519 -27.374 -8.176  1.00 16.12 ?  153 LEU   B HD11 1 
ATOM   6386 H  HD12 . LEU   B 1 153 ? 38.164 -28.234 -9.345  1.00 16.12 ?  153 LEU   B HD12 1 
ATOM   6387 H  HD13 . LEU   B 1 153 ? 38.605 -28.484 -7.840  1.00 16.12 ?  153 LEU   B HD13 1 
ATOM   6388 H  HD21 . LEU   B 1 153 ? 38.920 -25.751 -6.937  1.00 15.82 ?  153 LEU   B HD21 1 
ATOM   6389 H  HD22 . LEU   B 1 153 ? 40.093 -26.794 -6.694  1.00 15.82 ?  153 LEU   B HD22 1 
ATOM   6390 H  HD23 . LEU   B 1 153 ? 40.392 -25.421 -7.436  1.00 15.82 ?  153 LEU   B HD23 1 
ATOM   6391 N  N    . ALA   B 1 154 ? 44.051 -27.176 -9.323  1.00 11.93 ?  154 ALA   B N    1 
ATOM   6392 C  CA   . ALA   B 1 154 ? 45.277 -27.943 -9.502  1.00 12.81 ?  154 ALA   B CA   1 
ATOM   6393 C  C    . ALA   B 1 154 ? 45.343 -29.017 -8.422  1.00 13.47 ?  154 ALA   B C    1 
ATOM   6394 O  O    . ALA   B 1 154 ? 45.274 -28.711 -7.224  1.00 14.80 ?  154 ALA   B O    1 
ATOM   6395 C  CB   . ALA   B 1 154 ? 46.503 -27.033 -9.444  1.00 13.99 ?  154 ALA   B CB   1 
ATOM   6396 H  H    . ALA   B 1 154 ? 44.074 -26.639 -8.646  1.00 14.31 ?  154 ALA   B H    1 
ATOM   6397 H  HA   . ALA   B 1 154 ? 45.260 -28.375 -10.366 1.00 15.37 ?  154 ALA   B HA   1 
ATOM   6398 H  HB1  . ALA   B 1 154 ? 47.301 -27.568 -9.565  1.00 16.78 ?  154 ALA   B HB1  1 
ATOM   6399 H  HB2  . ALA   B 1 154 ? 46.440 -26.369 -10.152 1.00 16.78 ?  154 ALA   B HB2  1 
ATOM   6400 H  HB3  . ALA   B 1 154 ? 46.531 -26.588 -8.581  1.00 16.78 ?  154 ALA   B HB3  1 
ATOM   6401 N  N    . VAL   B 1 155 ? 45.465 -30.269 -8.850  1.00 12.88 ?  155 VAL   B N    1 
ATOM   6402 C  CA   . VAL   B 1 155 ? 45.572 -31.415 -7.956  1.00 13.30 ?  155 VAL   B CA   1 
ATOM   6403 C  C    . VAL   B 1 155 ? 46.912 -32.083 -8.237  1.00 13.28 ?  155 VAL   B C    1 
ATOM   6404 O  O    . VAL   B 1 155 ? 47.142 -32.582 -9.346  1.00 14.90 ?  155 VAL   B O    1 
ATOM   6405 C  CB   . VAL   B 1 155 ? 44.413 -32.407 -8.154  1.00 14.38 ?  155 VAL   B CB   1 
ATOM   6406 C  CG1  . VAL   B 1 155 ? 44.591 -33.610 -7.243  1.00 14.68 ?  155 VAL   B CG1  1 
ATOM   6407 C  CG2  . VAL   B 1 155 ? 43.068 -31.716 -7.905  1.00 15.40 ?  155 VAL   B CG2  1 
ATOM   6408 H  H    . VAL   B 1 155 ? 45.494 -30.486 -9.682  1.00 15.45 ?  155 VAL   B H    1 
ATOM   6409 H  HA   . VAL   B 1 155 ? 45.563 -31.112 -7.032  1.00 15.96 ?  155 VAL   B HA   1 
ATOM   6410 H  HB   . VAL   B 1 155 ? 44.421 -32.719 -9.073  1.00 17.26 ?  155 VAL   B HB   1 
ATOM   6411 H  HG11 . VAL   B 1 155 ? 43.764 -34.118 -7.222  1.00 17.62 ?  155 VAL   B HG11 1 
ATOM   6412 H  HG12 . VAL   B 1 155 ? 45.309 -34.169 -7.585  1.00 17.62 ?  155 VAL   B HG12 1 
ATOM   6413 H  HG13 . VAL   B 1 155 ? 44.810 -33.303 -6.348  1.00 17.62 ?  155 VAL   B HG13 1 
ATOM   6414 H  HG21 . VAL   B 1 155 ? 42.358 -32.375 -7.991  1.00 18.48 ?  155 VAL   B HG21 1 
ATOM   6415 H  HG22 . VAL   B 1 155 ? 43.067 -31.347 -7.008  1.00 18.48 ?  155 VAL   B HG22 1 
ATOM   6416 H  HG23 . VAL   B 1 155 ? 42.947 -31.012 -8.557  1.00 18.48 ?  155 VAL   B HG23 1 
ATOM   6417 N  N    . PHE   B 1 156 ? 47.778 -32.122 -7.226  1.00 13.74 ?  156 PHE   B N    1 
ATOM   6418 C  CA   . PHE   B 1 156 ? 49.153 -32.581 -7.434  1.00 14.68 ?  156 PHE   B CA   1 
ATOM   6419 C  C    . PHE   B 1 156 ? 49.243 -34.081 -7.717  1.00 15.96 ?  156 PHE   B C    1 
ATOM   6420 O  O    . PHE   B 1 156 ? 49.962 -34.510 -8.630  1.00 17.77 ?  156 PHE   B O    1 
ATOM   6421 C  CB   . PHE   B 1 156 ? 49.990 -32.215 -6.212  1.00 14.88 ?  156 PHE   B CB   1 
ATOM   6422 C  CG   . PHE   B 1 156 ? 51.411 -32.680 -6.276  1.00 15.57 ?  156 PHE   B CG   1 
ATOM   6423 C  CD1  . PHE   B 1 156 ? 52.289 -32.152 -7.206  1.00 17.10 ?  156 PHE   B CD1  1 
ATOM   6424 C  CD2  . PHE   B 1 156 ? 51.880 -33.624 -5.382  1.00 15.69 ?  156 PHE   B CD2  1 
ATOM   6425 C  CE1  . PHE   B 1 156 ? 53.608 -32.566 -7.255  1.00 17.94 ?  156 PHE   B CE1  1 
ATOM   6426 C  CE2  . PHE   B 1 156 ? 53.199 -34.040 -5.426  1.00 17.11 ?  156 PHE   B CE2  1 
ATOM   6427 C  CZ   . PHE   B 1 156 ? 54.055 -33.513 -6.366  1.00 17.88 ?  156 PHE   B CZ   1 
ATOM   6428 H  H    . PHE   B 1 156 ? 47.597 -31.896 -6.416  1.00 16.49 ?  156 PHE   B H    1 
ATOM   6429 H  HA   . PHE   B 1 156 ? 49.522 -32.116 -8.197  1.00 17.62 ?  156 PHE   B HA   1 
ATOM   6430 H  HB2  . PHE   B 1 156 ? 50.002 -31.247 -6.127  1.00 17.86 ?  156 PHE   B HB2  1 
ATOM   6431 H  HB3  . PHE   B 1 156 ? 49.586 -32.607 -5.425  1.00 17.86 ?  156 PHE   B HB3  1 
ATOM   6432 H  HD1  . PHE   B 1 156 ? 51.989 -31.508 -7.811  1.00 20.52 ?  156 PHE   B HD1  1 
ATOM   6433 H  HD2  . PHE   B 1 156 ? 51.298 -33.985 -4.750  1.00 18.82 ?  156 PHE   B HD2  1 
ATOM   6434 H  HE1  . PHE   B 1 156 ? 54.191 -32.207 -7.888  1.00 21.53 ?  156 PHE   B HE1  1 
ATOM   6435 H  HE2  . PHE   B 1 156 ? 53.501 -34.686 -4.827  1.00 20.54 ?  156 PHE   B HE2  1 
ATOM   6436 H  HZ   . PHE   B 1 156 ? 54.941 -33.797 -6.396  1.00 21.45 ?  156 PHE   B HZ   1 
ATOM   6437 N  N    . ASP   B 1 157 ? 48.577 -34.899 -6.913  1.00 16.44 ?  157 ASP   B N    1 
ATOM   6438 C  CA   . ASP   B 1 157 ? 48.728 -36.346 -7.003  1.00 17.81 ?  157 ASP   B CA   1 
ATOM   6439 C  C    . ASP   B 1 157 ? 47.811 -36.897 -8.090  1.00 17.88 ?  157 ASP   B C    1 
ATOM   6440 O  O    . ASP   B 1 157 ? 46.585 -36.780 -7.986  1.00 17.22 ?  157 ASP   B O    1 
ATOM   6441 C  CB   . ASP   B 1 157 ? 48.368 -36.955 -5.654  1.00 19.46 ?  157 ASP   B CB   1 
ATOM   6442 C  CG   . ASP   B 1 157 ? 48.508 -38.467 -5.634  1.00 21.58 ?  157 ASP   B CG   1 
ATOM   6443 O  OD1  . ASP   B 1 157 ? 48.839 -39.070 -6.683  1.00 21.85 ?  157 ASP   B OD1  1 
ATOM   6444 O  OD2  . ASP   B 1 157 ? 48.295 -39.055 -4.556  1.00 23.71 -1 157 ASP   B OD2  1 
ATOM   6445 H  H    . ASP   B 1 157 ? 48.034 -34.640 -6.304  1.00 19.73 ?  157 ASP   B H    1 
ATOM   6446 H  HA   . ASP   B 1 157 ? 49.649 -36.574 -7.218  1.00 21.37 ?  157 ASP   B HA   1 
ATOM   6447 H  HB2  . ASP   B 1 157 ? 48.943 -36.571 -4.974  1.00 23.35 ?  157 ASP   B HB2  1 
ATOM   6448 H  HB3  . ASP   B 1 157 ? 47.440 -36.739 -5.456  1.00 23.35 ?  157 ASP   B HB3  1 
ATOM   6449 N  N    . LYS   B 1 158 ? 48.404 -37.519 -9.117  1.00 18.77 ?  158 LYS   B N    1 
ATOM   6450 C  CA   . LYS   B 1 158 ? 47.627 -38.135 -10.195 1.00 19.97 ?  158 LYS   B CA   1 
ATOM   6451 C  C    . LYS   B 1 158 ? 46.566 -39.099 -9.661  1.00 19.96 ?  158 LYS   B C    1 
ATOM   6452 O  O    . LYS   B 1 158 ? 45.462 -39.188 -10.212 1.00 20.32 ?  158 LYS   B O    1 
ATOM   6453 C  CB   . LYS   B 1 158 ? 48.573 -38.860 -11.162 1.00 21.89 ?  158 LYS   B CB   1 
ATOM   6454 C  CG   . LYS   B 1 158 ? 47.892 -39.762 -12.186 1.00 24.37 ?  158 LYS   B CG   1 
ATOM   6455 C  CD   . LYS   B 1 158 ? 47.040 -38.981 -13.170 1.00 27.06 ?  158 LYS   B CD   1 
ATOM   6456 C  CE   . LYS   B 1 158 ? 46.429 -39.906 -14.211 1.00 28.75 ?  158 LYS   B CE   1 
ATOM   6457 N  NZ   . LYS   B 1 158 ? 45.348 -39.243 -14.995 1.00 28.91 ?  158 LYS   B NZ   1 
ATOM   6458 H  H    . LYS   B 1 158 ? 49.260 -37.597 -9.212  1.00 22.52 ?  158 LYS   B H    1 
ATOM   6459 H  HA   . LYS   B 1 158 ? 47.178 -37.436 -10.697 1.00 23.96 ?  158 LYS   B HA   1 
ATOM   6460 H  HB2  . LYS   B 1 158 ? 49.083 -38.196 -11.659 1.00 26.27 ?  158 LYS   B HB2  1 
ATOM   6461 H  HB3  . LYS   B 1 158 ? 49.182 -39.412 -10.647 1.00 26.27 ?  158 LYS   B HB3  1 
ATOM   6462 H  HG2  . LYS   B 1 158 ? 48.575 -40.228 -12.692 1.00 29.25 ?  158 LYS   B HG2  1 
ATOM   6463 H  HG3  . LYS   B 1 158 ? 47.326 -40.409 -11.735 1.00 29.25 ?  158 LYS   B HG3  1 
ATOM   6464 H  HD2  . LYS   B 1 158 ? 46.322 -38.536 -12.694 1.00 32.47 ?  158 LYS   B HD2  1 
ATOM   6465 H  HD3  . LYS   B 1 158 ? 47.595 -38.329 -13.628 1.00 32.47 ?  158 LYS   B HD3  1 
ATOM   6466 H  HE2  . LYS   B 1 158 ? 47.119 -40.188 -14.831 1.00 34.50 ?  158 LYS   B HE2  1 
ATOM   6467 H  HE3  . LYS   B 1 158 ? 46.047 -40.679 -13.765 1.00 34.50 ?  158 LYS   B HE3  1 
ATOM   6468 H  HZ1  . LYS   B 1 158 ? 45.012 -39.810 -15.592 1.00 34.69 ?  158 LYS   B HZ1  1 
ATOM   6469 H  HZ2  . LYS   B 1 158 ? 44.696 -38.977 -14.450 1.00 34.69 ?  158 LYS   B HZ2  1 
ATOM   6470 H  HZ3  . LYS   B 1 158 ? 45.675 -38.533 -15.422 1.00 34.69 ?  158 LYS   B HZ3  1 
ATOM   6471 N  N    . ASN   B 1 159 ? 46.888 -39.854 -8.609  1.00 20.30 ?  159 ASN   B N    1 
ATOM   6472 C  CA   . ASN   B 1 159 ? 45.932 -40.837 -8.104  1.00 20.75 ?  159 ASN   B CA   1 
ATOM   6473 C  C    . ASN   B 1 159 ? 44.734 -40.163 -7.430  1.00 19.43 ?  159 ASN   B C    1 
ATOM   6474 O  O    . ASN   B 1 159 ? 43.600 -40.653 -7.530  1.00 19.62 ?  159 ASN   B O    1 
ATOM   6475 C  CB   . ASN   B 1 159 ? 46.641 -41.813 -7.167  1.00 22.61 ?  159 ASN   B CB   1 
ATOM   6476 C  CG   . ASN   B 1 159 ? 47.658 -42.669 -7.889  1.00 24.48 ?  159 ASN   B CG   1 
ATOM   6477 O  OD1  . ASN   B 1 159 ? 47.403 -43.163 -8.996  1.00 25.39 ?  159 ASN   B OD1  1 
ATOM   6478 N  ND2  . ASN   B 1 159 ? 48.820 -42.854 -7.270  1.00 25.00 ?  159 ASN   B ND2  1 
ATOM   6479 H  H    . ASN   B 1 159 ? 47.634 -39.806 -8.185  1.00 24.36 ?  159 ASN   B H    1 
ATOM   6480 H  HA   . ASN   B 1 159 ? 45.600 -41.344 -8.860  1.00 24.90 ?  159 ASN   B HA   1 
ATOM   6481 H  HB2  . ASN   B 1 159 ? 47.102 -41.314 -6.478  1.00 27.13 ?  159 ASN   B HB2  1 
ATOM   6482 H  HB3  . ASN   B 1 159 ? 45.982 -42.402 -6.777  1.00 27.13 ?  159 ASN   B HB3  1 
ATOM   6483 H  HD21 . ASN   B 1 159 ? 49.436 -43.334 -7.637  1.00 30.01 ?  159 ASN   B HD21 1 
ATOM   6484 H  HD22 . ASN   B 1 159 ? 48.958 -42.508 -6.494  1.00 30.01 ?  159 ASN   B HD22 1 
ATOM   6485 N  N    . LEU   B 1 160 ? 44.953 -39.034 -6.747  1.00 18.68 ?  160 LEU   B N    1 
ATOM   6486 C  CA   . LEU   B 1 160 ? 43.823 -38.295 -6.201  1.00 17.78 ?  160 LEU   B CA   1 
ATOM   6487 C  C    . LEU   B 1 160 ? 43.035 -37.626 -7.315  1.00 16.71 ?  160 LEU   B C    1 
ATOM   6488 O  O    . LEU   B 1 160 ? 41.799 -37.618 -7.291  1.00 16.32 ?  160 LEU   B O    1 
ATOM   6489 C  CB   . LEU   B 1 160 ? 44.293 -37.265 -5.177  1.00 17.13 ?  160 LEU   B CB   1 
ATOM   6490 C  CG   . LEU   B 1 160 ? 43.168 -36.363 -4.656  1.00 16.70 ?  160 LEU   B CG   1 
ATOM   6491 C  CD1  . LEU   B 1 160 ? 42.053 -37.206 -4.047  1.00 17.70 ?  160 LEU   B CD1  1 
ATOM   6492 C  CD2  . LEU   B 1 160 ? 43.706 -35.365 -3.647  1.00 16.95 ?  160 LEU   B CD2  1 
ATOM   6493 H  H    . LEU   B 1 160 ? 45.728 -38.690 -6.594  1.00 22.42 ?  160 LEU   B H    1 
ATOM   6494 H  HA   . LEU   B 1 160 ? 43.235 -38.923 -5.757  1.00 21.33 ?  160 LEU   B HA   1 
ATOM   6495 H  HB2  . LEU   B 1 160 ? 44.682 -37.737 -4.420  1.00 20.55 ?  160 LEU   B HB2  1 
ATOM   6496 H  HB3  . LEU   B 1 160 ? 44.969 -36.701 -5.589  1.00 20.55 ?  160 LEU   B HB3  1 
ATOM   6497 H  HG   . LEU   B 1 160 ? 42.797 -35.867 -5.399  1.00 20.04 ?  160 LEU   B HG   1 
ATOM   6498 H  HD11 . LEU   B 1 160 ? 41.441 -36.621 -3.583  1.00 21.24 ?  160 LEU   B HD11 1 
ATOM   6499 H  HD12 . LEU   B 1 160 ? 41.589 -37.683 -4.754  1.00 21.24 ?  160 LEU   B HD12 1 
ATOM   6500 H  HD13 . LEU   B 1 160 ? 42.443 -37.843 -3.423  1.00 21.24 ?  160 LEU   B HD13 1 
ATOM   6501 H  HD21 . LEU   B 1 160 ? 42.979 -34.797 -3.357  1.00 20.33 ?  160 LEU   B HD21 1 
ATOM   6502 H  HD22 . LEU   B 1 160 ? 44.075 -35.849 -2.892  1.00 20.33 ?  160 LEU   B HD22 1 
ATOM   6503 H  HD23 . LEU   B 1 160 ? 44.399 -34.834 -4.070  1.00 20.33 ?  160 LEU   B HD23 1 
ATOM   6504 N  N    . TYR   B 1 161 ? 43.735 -37.054 -8.298  1.00 16.88 ?  161 TYR   B N    1 
ATOM   6505 C  CA   . TYR   B 1 161 ? 43.061 -36.494 -9.466  1.00 16.93 ?  161 TYR   B CA   1 
ATOM   6506 C  C    . TYR   B 1 161 ? 42.111 -37.519 -10.078 1.00 16.81 ?  161 TYR   B C    1 
ATOM   6507 O  O    . TYR   B 1 161 ? 40.936 -37.229 -10.327 1.00 16.86 ?  161 TYR   B O    1 
ATOM   6508 C  CB   . TYR   B 1 161 ? 44.101 -36.021 -10.491 1.00 17.61 ?  161 TYR   B CB   1 
ATOM   6509 C  CG   . TYR   B 1 161 ? 43.516 -35.550 -11.807 1.00 18.03 ?  161 TYR   B CG   1 
ATOM   6510 C  CD1  . TYR   B 1 161 ? 43.125 -34.228 -11.978 1.00 18.35 ?  161 TYR   B CD1  1 
ATOM   6511 C  CD2  . TYR   B 1 161 ? 43.345 -36.428 -12.876 1.00 18.83 ?  161 TYR   B CD2  1 
ATOM   6512 C  CE1  . TYR   B 1 161 ? 42.587 -33.793 -13.165 1.00 19.53 ?  161 TYR   B CE1  1 
ATOM   6513 C  CE2  . TYR   B 1 161 ? 42.804 -35.999 -14.069 1.00 19.85 ?  161 TYR   B CE2  1 
ATOM   6514 C  CZ   . TYR   B 1 161 ? 42.428 -34.680 -14.208 1.00 20.11 ?  161 TYR   B CZ   1 
ATOM   6515 O  OH   . TYR   B 1 161 ? 41.885 -34.237 -15.390 1.00 22.10 ?  161 TYR   B OH   1 
ATOM   6516 H  H    . TYR   B 1 161 ? 44.590 -36.991 -8.321  1.00 20.25 ?  161 TYR   B H    1 
ATOM   6517 H  HA   . TYR   B 1 161 ? 42.537 -35.727 -9.195  1.00 20.32 ?  161 TYR   B HA   1 
ATOM   6518 H  HB2  . TYR   B 1 161 ? 44.598 -35.280 -10.112 1.00 21.14 ?  161 TYR   B HB2  1 
ATOM   6519 H  HB3  . TYR   B 1 161 ? 44.705 -36.754 -10.688 1.00 21.14 ?  161 TYR   B HB3  1 
ATOM   6520 H  HD1  . TYR   B 1 161 ? 43.228 -33.621 -11.279 1.00 22.03 ?  161 TYR   B HD1  1 
ATOM   6521 H  HD2  . TYR   B 1 161 ? 43.594 -37.318 -12.789 1.00 22.59 ?  161 TYR   B HD2  1 
ATOM   6522 H  HE1  . TYR   B 1 161 ? 42.331 -32.899 -13.260 1.00 23.43 ?  161 TYR   B HE1  1 
ATOM   6523 H  HE2  . TYR   B 1 161 ? 42.693 -36.592 -14.778 1.00 23.82 ?  161 TYR   B HE2  1 
ATOM   6524 H  HH   . TYR   B 1 161 ? 41.839 -34.869 -15.943 1.00 26.52 ?  161 TYR   B HH   1 
ATOM   6525 N  N    . ASP   B 1 162 ? 42.604 -38.741 -10.301 1.00 17.49 ?  162 ASP   B N    1 
ATOM   6526 C  CA   . ASP   B 1 162 ? 41.777 -39.775 -10.915 1.00 17.90 ?  162 ASP   B CA   1 
ATOM   6527 C  C    . ASP   B 1 162 ? 40.571 -40.113 -10.046 1.00 17.39 ?  162 ASP   B C    1 
ATOM   6528 O  O    . ASP   B 1 162 ? 39.464 -40.321 -10.561 1.00 17.59 ?  162 ASP   B O    1 
ATOM   6529 C  CB   . ASP   B 1 162 ? 42.606 -41.038 -11.166 1.00 19.51 ?  162 ASP   B CB   1 
ATOM   6530 C  CG   . ASP   B 1 162 ? 43.611 -40.877 -12.294 1.00 20.93 ?  162 ASP   B CG   1 
ATOM   6531 O  OD1  . ASP   B 1 162 ? 43.486 -39.937 -13.101 1.00 21.38 ?  162 ASP   B OD1  1 
ATOM   6532 O  OD2  . ASP   B 1 162 ? 44.524 -41.723 -12.389 1.00 22.50 -1 162 ASP   B OD2  1 
ATOM   6533 H  H    . ASP   B 1 162 ? 43.404 -38.989 -10.115 1.00 20.98 ?  162 ASP   B H    1 
ATOM   6534 H  HA   . ASP   B 1 162 ? 41.450 -39.460 -11.770 1.00 21.48 ?  162 ASP   B HA   1 
ATOM   6535 H  HB2  . ASP   B 1 162 ? 43.104 -41.258 -10.364 1.00 23.41 ?  162 ASP   B HB2  1 
ATOM   6536 H  HB3  . ASP   B 1 162 ? 42.010 -41.769 -11.397 1.00 23.41 ?  162 ASP   B HB3  1 
ATOM   6537 N  N    A LYS   B 1 163 ? 40.767 -40.194 -8.728  0.64 16.30 ?  163 LYS   B N    1 
ATOM   6538 N  N    B LYS   B 1 163 ? 40.763 -40.181 -8.727  0.36 17.17 ?  163 LYS   B N    1 
ATOM   6539 C  CA   A LYS   B 1 163 ? 39.640 -40.458 -7.839  0.64 16.92 ?  163 LYS   B CA   1 
ATOM   6540 C  CA   B LYS   B 1 163 ? 39.640 -40.455 -7.836  0.36 17.75 ?  163 LYS   B CA   1 
ATOM   6541 C  C    A LYS   B 1 163 ? 38.602 -39.342 -7.909  0.64 15.72 ?  163 LYS   B C    1 
ATOM   6542 C  C    B LYS   B 1 163 ? 38.602 -39.339 -7.894  0.36 16.18 ?  163 LYS   B C    1 
ATOM   6543 O  O    A LYS   B 1 163 ? 37.392 -39.608 -7.905  0.64 16.32 ?  163 LYS   B O    1 
ATOM   6544 O  O    B LYS   B 1 163 ? 37.392 -39.603 -7.871  0.36 16.43 ?  163 LYS   B O    1 
ATOM   6545 C  CB   A LYS   B 1 163 ? 40.125 -40.638 -6.402  0.64 19.29 ?  163 LYS   B CB   1 
ATOM   6546 C  CB   B LYS   B 1 163 ? 40.137 -40.639 -6.404  0.36 20.20 ?  163 LYS   B CB   1 
ATOM   6547 C  CG   A LYS   B 1 163 ? 39.045 -41.180 -5.483  0.64 23.53 ?  163 LYS   B CG   1 
ATOM   6548 C  CG   B LYS   B 1 163 ? 39.064 -41.138 -5.455  0.36 23.21 ?  163 LYS   B CG   1 
ATOM   6549 C  CD   A LYS   B 1 163 ? 39.457 -41.175 -4.022  0.64 27.27 ?  163 LYS   B CD   1 
ATOM   6550 C  CD   B LYS   B 1 163 ? 39.568 -41.262 -4.030  0.36 26.07 ?  163 LYS   B CD   1 
ATOM   6551 C  CE   A LYS   B 1 163 ? 38.390 -41.851 -3.171  0.64 29.70 ?  163 LYS   B CE   1 
ATOM   6552 C  CE   B LYS   B 1 163 ? 38.513 -41.917 -3.151  0.36 28.27 ?  163 LYS   B CE   1 
ATOM   6553 N  NZ   A LYS   B 1 163 ? 38.497 -41.498 -1.730  0.64 30.61 ?  163 LYS   B NZ   1 
ATOM   6554 N  NZ   B LYS   B 1 163 ? 38.736 -41.664 -1.702  0.36 29.15 ?  163 LYS   B NZ   1 
ATOM   6555 H  H    A LYS   B 1 163 ? 41.529 -40.102 -8.336  0.64 19.56 ?  163 LYS   B H    1 
ATOM   6556 H  H    B LYS   B 1 163 ? 41.522 -40.081 -8.334  0.36 20.60 ?  163 LYS   B H    1 
ATOM   6557 H  HA   A LYS   B 1 163 ? 39.212 -41.280 -8.116  0.64 20.31 ?  163 LYS   B HA   1 
ATOM   6558 H  HA   B LYS   B 1 163 ? 39.210 -41.277 -8.114  0.36 21.30 ?  163 LYS   B HA   1 
ATOM   6559 H  HB2  A LYS   B 1 163 ? 40.867 -41.264 -6.395  0.64 23.15 ?  163 LYS   B HB2  1 
ATOM   6560 H  HB2  B LYS   B 1 163 ? 40.859 -41.286 -6.403  0.36 24.24 ?  163 LYS   B HB2  1 
ATOM   6561 H  HB3  A LYS   B 1 163 ? 40.411 -39.780 -6.053  0.64 23.15 ?  163 LYS   B HB3  1 
ATOM   6562 H  HB3  B LYS   B 1 163 ? 40.457 -39.787 -6.070  0.36 24.24 ?  163 LYS   B HB3  1 
ATOM   6563 H  HG2  A LYS   B 1 163 ? 38.248 -40.636 -5.570  0.64 28.24 ?  163 LYS   B HG2  1 
ATOM   6564 H  HG2  B LYS   B 1 163 ? 38.321 -40.515 -5.456  0.36 27.85 ?  163 LYS   B HG2  1 
ATOM   6565 H  HG3  A LYS   B 1 163 ? 38.848 -42.098 -5.734  0.64 28.24 ?  163 LYS   B HG3  1 
ATOM   6566 H  HG3  B LYS   B 1 163 ? 38.765 -42.014 -5.746  0.36 27.85 ?  163 LYS   B HG3  1 
ATOM   6567 H  HD2  A LYS   B 1 163 ? 40.289 -41.664 -3.917  0.64 32.72 ?  163 LYS   B HD2  1 
ATOM   6568 H  HD2  B LYS   B 1 163 ? 40.367 -41.814 -4.016  0.36 31.28 ?  163 LYS   B HD2  1 
ATOM   6569 H  HD3  A LYS   B 1 163 ? 39.561 -40.260 -3.718  0.64 32.72 ?  163 LYS   B HD3  1 
ATOM   6570 H  HD3  B LYS   B 1 163 ? 39.760 -40.379 -3.676  0.36 31.28 ?  163 LYS   B HD3  1 
ATOM   6571 H  HE2  A LYS   B 1 163 ? 37.512 -41.586 -3.487  0.64 35.64 ?  163 LYS   B HE2  1 
ATOM   6572 H  HE2  B LYS   B 1 163 ? 37.640 -41.568 -3.390  0.36 33.93 ?  163 LYS   B HE2  1 
ATOM   6573 H  HE3  A LYS   B 1 163 ? 38.489 -42.812 -3.251  0.64 35.64 ?  163 LYS   B HE3  1 
ATOM   6574 H  HE3  B LYS   B 1 163 ? 38.536 -42.876 -3.296  0.36 33.93 ?  163 LYS   B HE3  1 
ATOM   6575 H  HZ1  A LYS   B 1 163 ? 37.858 -41.910 -1.269  0.64 36.73 ?  163 LYS   B HZ1  1 
ATOM   6576 H  HZ1  B LYS   B 1 163 ? 38.099 -42.062 -1.224  0.36 34.98 ?  163 LYS   B HZ1  1 
ATOM   6577 H  HZ2  A LYS   B 1 163 ? 39.290 -41.750 -1.415  0.64 36.73 ?  163 LYS   B HZ2  1 
ATOM   6578 H  HZ2  B LYS   B 1 163 ? 39.527 -41.986 -1.456  0.36 34.98 ?  163 LYS   B HZ2  1 
ATOM   6579 H  HZ3  A LYS   B 1 163 ? 38.409 -40.619 -1.625  0.64 36.73 ?  163 LYS   B HZ3  1 
ATOM   6580 H  HZ3  B LYS   B 1 163 ? 38.715 -40.789 -1.541  0.36 34.98 ?  163 LYS   B HZ3  1 
ATOM   6581 N  N    . LEU   B 1 164 ? 39.057 -38.086 -7.958  1.00 14.78 ?  164 LEU   B N    1 
ATOM   6582 C  CA   . LEU   B 1 164 ? 38.138 -36.950 -8.015  1.00 14.54 ?  164 LEU   B CA   1 
ATOM   6583 C  C    . LEU   B 1 164 ? 37.355 -36.934 -9.324  1.00 15.14 ?  164 LEU   B C    1 
ATOM   6584 O  O    . LEU   B 1 164 ? 36.129 -36.741 -9.328  1.00 16.31 ?  164 LEU   B O    1 
ATOM   6585 C  CB   . LEU   B 1 164 ? 38.936 -35.655 -7.847  1.00 14.32 ?  164 LEU   B CB   1 
ATOM   6586 C  CG   . LEU   B 1 164 ? 39.470 -35.366 -6.445  1.00 14.95 ?  164 LEU   B CG   1 
ATOM   6587 C  CD1  . LEU   B 1 164 ? 40.552 -34.300 -6.518  1.00 15.00 ?  164 LEU   B CD1  1 
ATOM   6588 C  CD2  . LEU   B 1 164 ? 38.358 -34.918 -5.518  1.00 16.70 ?  164 LEU   B CD2  1 
ATOM   6589 H  H    A LEU   B 1 164 ? 39.894 -37.865 -7.955  0.64 17.74 ?  164 LEU   B H    1 
ATOM   6590 H  H    B LEU   B 1 164 ? 39.894 -37.867 -7.969  0.36 17.74 ?  164 LEU   B H    1 
ATOM   6591 H  HA   . LEU   B 1 164 ? 37.511 -37.013 -7.287  1.00 17.45 ?  164 LEU   B HA   1 
ATOM   6592 H  HB2  . LEU   B 1 164 ? 39.702 -35.685 -8.445  1.00 17.18 ?  164 LEU   B HB2  1 
ATOM   6593 H  HB3  . LEU   B 1 164 ? 38.368 -34.912 -8.093  1.00 17.18 ?  164 LEU   B HB3  1 
ATOM   6594 H  HG   . LEU   B 1 164 ? 39.875 -36.167 -6.080  1.00 17.94 ?  164 LEU   B HG   1 
ATOM   6595 H  HD11 . LEU   B 1 164 ? 40.880 -34.111 -5.622  1.00 18.00 ?  164 LEU   B HD11 1 
ATOM   6596 H  HD12 . LEU   B 1 164 ? 41.286 -34.620 -7.071  1.00 18.00 ?  164 LEU   B HD12 1 
ATOM   6597 H  HD13 . LEU   B 1 164 ? 40.181 -33.490 -6.906  1.00 18.00 ?  164 LEU   B HD13 1 
ATOM   6598 H  HD21 . LEU   B 1 164 ? 38.733 -34.700 -4.651  1.00 20.04 ?  164 LEU   B HD21 1 
ATOM   6599 H  HD22 . LEU   B 1 164 ? 37.926 -34.136 -5.897  1.00 20.04 ?  164 LEU   B HD22 1 
ATOM   6600 H  HD23 . LEU   B 1 164 ? 37.717 -35.640 -5.430  1.00 20.04 ?  164 LEU   B HD23 1 
ATOM   6601 N  N    . VAL   B 1 165 ? 38.050 -37.114 -10.450 1.00 16.62 ?  165 VAL   B N    1 
ATOM   6602 C  CA   . VAL   B 1 165 ? 37.394 -37.059 -11.753 1.00 18.07 ?  165 VAL   B CA   1 
ATOM   6603 C  C    . VAL   B 1 165 ? 36.465 -38.254 -11.930 1.00 19.55 ?  165 VAL   B C    1 
ATOM   6604 O  O    . VAL   B 1 165 ? 35.305 -38.108 -12.339 1.00 20.72 ?  165 VAL   B O    1 
ATOM   6605 C  CB   . VAL   B 1 165 ? 38.441 -36.986 -12.881 1.00 18.94 ?  165 VAL   B CB   1 
ATOM   6606 C  CG1  . VAL   B 1 165 ? 37.774 -37.109 -14.231 1.00 20.08 ?  165 VAL   B CG1  1 
ATOM   6607 C  CG2  . VAL   B 1 165 ? 39.230 -35.692 -12.794 1.00 18.65 ?  165 VAL   B CG2  1 
ATOM   6608 H  H    . VAL   B 1 165 ? 38.900 -37.267 -10.488 1.00 19.94 ?  165 VAL   B H    1 
ATOM   6609 H  HA   . VAL   B 1 165 ? 36.857 -36.258 -11.802 1.00 21.68 ?  165 VAL   B HA   1 
ATOM   6610 H  HB   . VAL   B 1 165 ? 39.068 -37.721 -12.785 1.00 22.73 ?  165 VAL   B HB   1 
ATOM   6611 H  HG11 . VAL   B 1 165 ? 38.391 -36.813 -14.916 1.00 24.10 ?  165 VAL   B HG11 1 
ATOM   6612 H  HG12 . VAL   B 1 165 ? 37.543 -38.041 -14.381 1.00 24.10 ?  165 VAL   B HG12 1 
ATOM   6613 H  HG13 . VAL   B 1 165 ? 36.976 -36.564 -14.240 1.00 24.10 ?  165 VAL   B HG13 1 
ATOM   6614 H  HG21 . VAL   B 1 165 ? 39.865 -35.655 -13.530 1.00 22.38 ?  165 VAL   B HG21 1 
ATOM   6615 H  HG22 . VAL   B 1 165 ? 38.618 -34.940 -12.855 1.00 22.38 ?  165 VAL   B HG22 1 
ATOM   6616 H  HG23 . VAL   B 1 165 ? 39.706 -35.662 -11.950 1.00 22.38 ?  165 VAL   B HG23 1 
ATOM   6617 N  N    . SER   B 1 166 ? 36.964 -39.458 -11.621 1.00 20.41 ?  166 SER   B N    1 
ATOM   6618 C  CA   . SER   B 1 166 ? 36.206 -40.668 -11.908 1.00 21.68 ?  166 SER   B CA   1 
ATOM   6619 C  C    . SER   B 1 166 ? 34.945 -40.751 -11.062 1.00 22.30 ?  166 SER   B C    1 
ATOM   6620 O  O    . SER   B 1 166 ? 33.976 -41.382 -11.480 1.00 23.66 ?  166 SER   B O    1 
ATOM   6621 C  CB   . SER   B 1 166 ? 37.071 -41.923 -11.727 1.00 22.62 ?  166 SER   B CB   1 
ATOM   6622 O  OG   . SER   B 1 166 ? 37.443 -42.119 -10.373 1.00 22.81 ?  166 SER   B OG   1 
ATOM   6623 H  H    . SER   B 1 166 ? 37.737 -39.596 -11.258 1.00 24.49 ?  166 SER   B H    1 
ATOM   6624 H  HA   . SER   B 1 166 ? 35.935 -40.647 -12.839 1.00 26.01 ?  166 SER   B HA   1 
ATOM   6625 H  HB2  . SER   B 1 166 ? 36.570 -42.698 -12.026 1.00 27.14 ?  166 SER   B HB2  1 
ATOM   6626 H  HB3  . SER   B 1 166 ? 37.877 -41.832 -12.264 1.00 27.14 ?  166 SER   B HB3  1 
ATOM   6627 H  HG   . SER   B 1 166 ? 37.894 -41.465 -10.103 1.00 27.38 ?  166 SER   B HG   1 
ATOM   6628 N  N    . SER   B 1 167 ? 34.927 -40.132 -9.886  1.00 20.80 ?  167 SER   B N    1 
ATOM   6629 C  CA   . SER   B 1 167 ? 33.773 -40.189 -8.996  1.00 20.27 ?  167 SER   B CA   1 
ATOM   6630 C  C    . SER   B 1 167 ? 32.862 -38.964 -9.091  1.00 19.66 ?  167 SER   B C    1 
ATOM   6631 O  O    . SER   B 1 167 ? 31.783 -38.966 -8.488  1.00 19.74 ?  167 SER   B O    1 
ATOM   6632 C  CB   . SER   B 1 167 ? 34.228 -40.376 -7.543  1.00 20.04 ?  167 SER   B CB   1 
ATOM   6633 O  OG   . SER   B 1 167 ? 34.898 -39.214 -7.072  1.00 19.84 ?  167 SER   B OG   1 
ATOM   6634 H  H    . SER   B 1 167 ? 35.579 -39.674 -9.581  1.00 24.96 ?  167 SER   B H    1 
ATOM   6635 H  HA   . SER   B 1 167 ? 33.241 -40.965 -9.234  1.00 24.32 ?  167 SER   B HA   1 
ATOM   6636 H  HB2  . SER   B 1 167 ? 33.450 -40.546 -6.990  1.00 24.05 ?  167 SER   B HB2  1 
ATOM   6637 H  HB3  . SER   B 1 167 ? 34.834 -41.138 -7.500  1.00 24.05 ?  167 SER   B HB3  1 
ATOM   6638 H  HG   . SER   B 1 167 ? 35.576 -39.068 -7.544  1.00 23.81 ?  167 SER   B HG   1 
ATOM   6639 N  N    . PHE   B 1 168 ? 33.247 -37.929 -9.840  1.00 19.14 ?  168 PHE   B N    1 
ATOM   6640 C  CA   . PHE   B 1 168 ? 32.411 -36.729 -9.913  1.00 18.17 ?  168 PHE   B CA   1 
ATOM   6641 C  C    . PHE   B 1 168 ? 31.106 -36.995 -10.659 1.00 16.15 ?  168 PHE   B C    1 
ATOM   6642 O  O    . PHE   B 1 168 ? 30.056 -36.413 -10.322 1.00 16.84 ?  168 PHE   B O    1 
ATOM   6643 C  CB   . PHE   B 1 168 ? 33.176 -35.588 -10.582 1.00 18.90 ?  168 PHE   B CB   1 
ATOM   6644 C  CG   . PHE   B 1 168 ? 32.365 -34.340 -10.729 1.00 18.81 ?  168 PHE   B CG   1 
ATOM   6645 C  CD1  . PHE   B 1 168 ? 32.014 -33.601 -9.610  1.00 19.90 ?  168 PHE   B CD1  1 
ATOM   6646 C  CD2  . PHE   B 1 168 ? 31.927 -33.917 -11.969 1.00 18.39 ?  168 PHE   B CD2  1 
ATOM   6647 C  CE1  . PHE   B 1 168 ? 31.246 -32.457 -9.724  1.00 20.30 ?  168 PHE   B CE1  1 
ATOM   6648 C  CE2  . PHE   B 1 168 ? 31.167 -32.761 -12.097 1.00 19.41 ?  168 PHE   B CE2  1 
ATOM   6649 C  CZ   . PHE   B 1 168 ? 30.823 -32.030 -10.970 1.00 19.77 ?  168 PHE   B CZ   1 
ATOM   6650 H  H    . PHE   B 1 168 ? 33.966 -37.896 -10.306 1.00 22.97 ?  168 PHE   B H    1 
ATOM   6651 H  HA   . PHE   B 1 168 ? 32.181 -36.451 -9.017  1.00 21.80 ?  168 PHE   B HA   1 
ATOM   6652 H  HB2  . PHE   B 1 168 ? 33.953 -35.375 -10.044 1.00 22.69 ?  168 PHE   B HB2  1 
ATOM   6653 H  HB3  . PHE   B 1 168 ? 33.451 -35.867 -11.469 1.00 22.69 ?  168 PHE   B HB3  1 
ATOM   6654 H  HD1  . PHE   B 1 168 ? 32.293 -33.888 -8.771  1.00 23.88 ?  168 PHE   B HD1  1 
ATOM   6655 H  HD2  . PHE   B 1 168 ? 32.154 -34.400 -12.728 1.00 22.07 ?  168 PHE   B HD2  1 
ATOM   6656 H  HE1  . PHE   B 1 168 ? 31.020 -31.973 -8.964  1.00 24.36 ?  168 PHE   B HE1  1 
ATOM   6657 H  HE2  . PHE   B 1 168 ? 30.879 -32.482 -12.939 1.00 23.29 ?  168 PHE   B HE2  1 
ATOM   6658 H  HZ   . PHE   B 1 168 ? 30.307 -31.260 -11.053 1.00 23.72 ?  168 PHE   B HZ   1 
ATOM   6659 N  N    . LEU   B 1 169 ? 31.153 -37.859 -11.670 1.00 16.50 ?  169 LEU   B N    1 
ATOM   6660 C  CA   . LEU   B 1 169 ? 29.979 -38.189 -12.470 1.00 18.54 ?  169 LEU   B CA   1 
ATOM   6661 C  C    . LEU   B 1 169 ? 29.971 -39.636 -12.945 1.00 21.63 ?  169 LEU   B C    1 
ATOM   6662 O  O    . LEU   B 1 169 ? 29.065 -40.058 -13.665 1.00 23.87 ?  169 LEU   B O    1 
ATOM   6663 C  CB   . LEU   B 1 169 ? 29.895 -37.270 -13.688 1.00 20.35 ?  169 LEU   B CB   1 
ATOM   6664 C  CG   . LEU   B 1 169 ? 28.644 -36.401 -13.791 1.00 23.22 ?  169 LEU   B CG   1 
ATOM   6665 C  CD1  . LEU   B 1 169 ? 28.596 -35.763 -15.159 1.00 24.21 ?  169 LEU   B CD1  1 
ATOM   6666 C  CD2  . LEU   B 1 169 ? 27.377 -37.199 -13.525 1.00 23.09 ?  169 LEU   B CD2  1 
ATOM   6667 O  OXT  . LEU   B 1 169 ? 30.874 -40.405 -12.631 1.00 22.89 -1 169 LEU   B OXT  1 
ATOM   6668 H  H    . LEU   B 1 169 ? 31.869 -38.265 -11.927 1.00 19.80 ?  169 LEU   B H    1 
ATOM   6669 H  HA   . LEU   B 1 169 ? 29.194 -38.047 -11.927 1.00 22.25 ?  169 LEU   B HA   1 
ATOM   6670 H  HB2  . LEU   B 1 169 ? 30.657 -36.671 -13.678 1.00 24.42 ?  169 LEU   B HB2  1 
ATOM   6671 H  HB3  . LEU   B 1 169 ? 29.925 -37.815 -14.491 1.00 24.42 ?  169 LEU   B HB3  1 
ATOM   6672 H  HG   . LEU   B 1 169 ? 28.694 -35.689 -13.132 1.00 27.86 ?  169 LEU   B HG   1 
ATOM   6673 H  HD11 . LEU   B 1 169 ? 27.818 -35.187 -15.210 1.00 29.06 ?  169 LEU   B HD11 1 
ATOM   6674 H  HD12 . LEU   B 1 169 ? 29.404 -35.244 -15.289 1.00 29.06 ?  169 LEU   B HD12 1 
ATOM   6675 H  HD13 . LEU   B 1 169 ? 28.537 -36.462 -15.827 1.00 29.06 ?  169 LEU   B HD13 1 
ATOM   6676 H  HD21 . LEU   B 1 169 ? 26.629 -36.761 -13.954 1.00 27.70 ?  169 LEU   B HD21 1 
ATOM   6677 H  HD22 . LEU   B 1 169 ? 27.490 -38.094 -13.888 1.00 27.70 ?  169 LEU   B HD22 1 
ATOM   6678 H  HD23 . LEU   B 1 169 ? 27.232 -37.248 -12.568 1.00 27.70 ?  169 LEU   B HD23 1 
HETATM 6679 C  C1   T TFA   C 2 .   ? 12.140 -1.280  1.454   0.30 10.45 ?  201 TFA   A C1   1 
HETATM 6680 C  C2   T TFA   C 2 .   ? 12.762 -1.713  0.100   0.30 12.89 ?  201 TFA   A C2   1 
HETATM 6681 O  O    T TFA   C 2 .   ? 12.860 -1.551  2.422   0.30 9.06  ?  201 TFA   A O    1 
HETATM 6682 F  F1   T TFA   C 2 .   ? 12.817 -3.054  0.031   0.30 14.13 ?  201 TFA   A F1   1 
HETATM 6683 F  F2   T TFA   C 2 .   ? 12.063 -1.302  -0.972  0.30 12.53 ?  201 TFA   A F2   1 
HETATM 6684 F  F3   T TFA   C 2 .   ? 14.002 -1.245  -0.073  0.30 14.39 ?  201 TFA   A F3   1 
HETATM 6685 O  OXT  T TFA   C 2 .   ? 11.044 -0.718  1.384   0.30 10.71 ?  201 TFA   A OXT  1 
HETATM 6686 N  N2   B A1A7Z D 3 .   ? 15.057 -0.301  3.773   0.36 17.56 ?  202 A1A7Z A N2   1 
HETATM 6687 C  C3   B A1A7Z D 3 .   ? 15.377 0.777   2.977   0.36 17.21 ?  202 A1A7Z A C3   1 
HETATM 6688 C  C6   B A1A7Z D 3 .   ? 15.579 2.058   3.625   0.36 16.43 ?  202 A1A7Z A C6   1 
HETATM 6689 C  C9   B A1A7Z D 3 .   ? 13.566 -0.380  0.214   0.36 19.61 ?  202 A1A7Z A C9   1 
HETATM 6690 C  C12  B A1A7Z D 3 .   ? 10.983 0.087   -0.891  0.36 20.69 ?  202 A1A7Z A C12  1 
HETATM 6691 C  C14  B A1A7Z D 3 .   ? 12.623 -1.433  0.090   0.36 20.23 ?  202 A1A7Z A C14  1 
HETATM 6692 C  C1   B A1A7Z D 3 .   ? 16.025 -0.984  -0.343  0.36 18.15 ?  202 A1A7Z A C1   1 
HETATM 6693 C  C10  B A1A7Z D 3 .   ? 13.174 0.902   -0.225  0.36 19.98 ?  202 A1A7Z A C10  1 
HETATM 6694 C  C11  B A1A7Z D 3 .   ? 11.899 1.149   -0.773  0.36 20.41 ?  202 A1A7Z A C11  1 
HETATM 6695 C  C13  B A1A7Z D 3 .   ? 11.341 -1.202  -0.457  0.36 20.74 ?  202 A1A7Z A C13  1 
HETATM 6696 C  C2   B A1A7Z D 3 .   ? 15.003 -0.629  0.829   0.36 18.30 ?  202 A1A7Z A C2   1 
HETATM 6697 C  C4   B A1A7Z D 3 .   ? 14.933 -0.149  5.139   0.36 17.53 ?  202 A1A7Z A C4   1 
HETATM 6698 C  C5   B A1A7Z D 3 .   ? 15.414 2.029   5.036   0.36 16.18 ?  202 A1A7Z A C5   1 
HETATM 6699 C  C7   B A1A7Z D 3 .   ? 15.913 3.436   3.333   0.36 15.88 ?  202 A1A7Z A C7   1 
HETATM 6700 C  C8   B A1A7Z D 3 .   ? 15.936 4.161   4.512   0.36 15.35 ?  202 A1A7Z A C8   1 
HETATM 6701 N  N1   B A1A7Z D 3 .   ? 15.488 0.548   1.596   0.36 17.55 ?  202 A1A7Z A N1   1 
HETATM 6702 N  N3   B A1A7Z D 3 .   ? 15.088 0.970   5.851   0.36 17.05 ?  202 A1A7Z A N3   1 
HETATM 6703 N  N4   B A1A7Z D 3 .   ? 15.633 3.294   5.580   0.36 15.04 ?  202 A1A7Z A N4   1 
HETATM 6704 O  O1   B A1A7Z D 3 .   ? 17.158 -1.631  0.189   0.36 17.48 ?  202 A1A7Z A O1   1 
HETATM 6705 H  H12  B A1A7Z D 3 .   ? 9.966  0.258   -1.322  0.36 24.83 ?  202 A1A7Z A H12  1 
HETATM 6706 H  H14  B A1A7Z D 3 .   ? 12.874 -2.472  0.426   0.36 24.27 ?  202 A1A7Z A H14  1 
HETATM 6707 H  H4   B A1A7Z D 3 .   ? 15.497 -1.629  -1.081  0.36 21.78 ?  202 A1A7Z A H4   1 
HETATM 6708 H  H3   B A1A7Z D 3 .   ? 16.303 -0.044  -0.857  0.36 21.78 ?  202 A1A7Z A H3   1 
HETATM 6709 H  H10  B A1A7Z D 3 .   ? 13.873 1.764   -0.146  0.36 23.97 ?  202 A1A7Z A H10  1 
HETATM 6710 H  H11  B A1A7Z D 3 .   ? 11.638 2.193   -1.111  0.36 24.49 ?  202 A1A7Z A H11  1 
HETATM 6711 H  H13  B A1A7Z D 3 .   ? 10.618 -2.052  -0.545  0.36 24.89 ?  202 A1A7Z A H13  1 
HETATM 6712 H  H1   B A1A7Z D 3 .   ? 14.988 -1.510  1.508   0.36 21.96 ?  202 A1A7Z A H1   1 
HETATM 6713 H  H6   B A1A7Z D 3 .   ? 14.662 -1.045  5.752   0.36 21.04 ?  202 A1A7Z A H6   1 
HETATM 6714 H  H7   B A1A7Z D 3 .   ? 16.121 3.930   2.397   0.36 19.06 ?  202 A1A7Z A H7   1 
HETATM 6715 H  H8   B A1A7Z D 3 .   ? 16.119 5.180   4.837   0.36 18.42 ?  202 A1A7Z A H8   1 
HETATM 6716 H  H5   B A1A7Z D 3 .   ? 15.943 1.262   1.012   0.36 21.06 ?  202 A1A7Z A H5   1 
HETATM 6717 H  H9   B A1A7Z D 3 .   ? 15.577 3.552   6.518   0.36 18.05 ?  202 A1A7Z A H9   1 
HETATM 6718 H  H2   B A1A7Z D 3 .   ? 17.746 -1.980  -0.497  0.36 20.98 ?  202 A1A7Z A H2   1 
HETATM 6719 CL CL   B CL    E 4 .   ? 16.124 2.741   -1.150  0.36 17.05 ?  203 CL    A CL   1 
HETATM 6720 O  O    . HOH   F 5 .   ? 14.770 -4.562  20.517  1.00 45.70 ?  301 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 5 .   ? 6.837  -7.991  11.762  1.00 18.56 ?  302 HOH   A O    1 
HETATM 6722 O  O    A HOH   F 5 .   ? 4.720  3.934   0.556   0.64 20.08 ?  303 HOH   A O    1 
HETATM 6723 O  O    . HOH   F 5 .   ? 12.011 0.325   14.682  1.00 33.05 ?  304 HOH   A O    1 
HETATM 6724 O  O    . HOH   F 5 .   ? 18.633 -2.338  -16.456 1.00 44.89 ?  305 HOH   A O    1 
HETATM 6725 O  O    . HOH   F 5 .   ? 15.054 -12.200 18.623  1.00 39.75 ?  306 HOH   A O    1 
HETATM 6726 O  O    . HOH   F 5 .   ? 34.346 -1.841  12.520  1.00 35.09 ?  307 HOH   A O    1 
HETATM 6727 O  O    . HOH   F 5 .   ? 9.155  -10.146 19.304  1.00 39.38 ?  308 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 5 .   ? 7.626  -6.283  -6.628  1.00 40.00 ?  309 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 5 .   ? 11.763 -10.856 -10.131 1.00 45.16 ?  310 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 0.631  -4.363  0.128   1.00 32.39 ?  311 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 7.923  -12.596 -0.921  1.00 20.87 ?  312 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 14.647 -13.894 16.652  1.00 25.96 ?  313 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 5 .   ? 28.982 0.493   -9.725  1.00 21.50 ?  314 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 28.152 -6.300  19.611  1.00 42.74 ?  315 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? 18.632 -19.393 13.474  1.00 34.95 ?  316 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 14.161 -4.531  -11.924 1.00 33.03 ?  317 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 30.237 -13.335 -8.548  1.00 25.25 ?  318 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 28.628 -10.657 -14.037 1.00 41.67 ?  319 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 42.466 10.584  5.095   1.00 19.62 ?  320 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? -0.407 -2.928  2.998   1.00 34.73 ?  321 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 31.013 6.227   -12.291 1.00 27.50 ?  322 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? -1.334 -4.377  7.283   1.00 52.22 ?  323 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 15.089 4.086   17.644  1.00 43.22 ?  324 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 36.165 -5.103  -0.535  1.00 29.84 ?  325 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 14.485 -24.681 11.576  1.00 40.34 ?  326 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 26.507 -19.338 -1.772  1.00 14.27 ?  327 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 44.367 7.170   6.377   1.00 25.66 ?  328 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 13.263 -1.461  -6.682  1.00 16.09 ?  329 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 17.068 -17.975 15.019  1.00 25.68 ?  330 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 22.306 5.401   18.974  1.00 42.58 ?  331 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 7.934  -21.518 3.986   1.00 45.54 ?  332 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 38.320 10.185  7.130   1.00 41.15 ?  333 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 13.549 -15.215 -7.548  1.00 24.58 ?  334 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 37.557 2.797   10.190  1.00 26.59 ?  335 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 9.868  -21.410 5.643   1.00 18.72 ?  336 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 31.027 -18.122 7.807   1.00 19.53 ?  337 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? -0.593 -8.470  2.131   1.00 41.88 ?  338 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 5 .   ? 3.558  -9.391  9.640   1.00 27.49 ?  339 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 27.380 13.797  2.814   1.00 29.36 ?  340 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 22.735 12.517  1.600   1.00 14.67 ?  341 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 34.045 -1.049  -8.960  1.00 27.36 ?  342 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 20.677 -19.769 -5.067  1.00 27.24 ?  343 HOH   A O    1 
HETATM 6763 O  O    B HOH   F 5 .   ? 14.804 -2.953  3.198   0.36 22.92 ?  344 HOH   A O    1 
HETATM 6764 O  O    A HOH   F 5 .   ? 14.655 -3.640  3.057   0.64 12.86 ?  345 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 10.961 1.711   12.488  1.00 24.40 ?  346 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 27.464 -6.130  -14.001 1.00 37.08 ?  347 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 21.295 -2.327  -2.313  1.00 15.38 ?  348 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 18.898 -21.979 6.930   1.00 32.22 ?  349 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 26.913 11.456  1.613   1.00 16.64 ?  350 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 28.413 -0.130  -13.398 1.00 33.96 ?  351 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 19.921 -12.548 -8.886  1.00 25.11 ?  352 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 38.593 5.002   7.001   1.00 14.95 ?  353 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 39.819 -1.028  -5.152  1.00 21.12 ?  354 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 42.633 4.317   5.454   1.00 30.14 ?  355 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 27.968 0.835   -7.150  1.00 13.64 ?  356 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 24.055 -2.092  -2.103  1.00 10.33 ?  357 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 14.379 -21.230 -4.269  1.00 29.30 ?  358 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 18.607 9.510   8.989   1.00 20.61 ?  359 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 35.787 -12.649 6.846   1.00 15.55 ?  360 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 22.150 -19.279 11.387  1.00 35.27 ?  361 HOH   A O    1 
HETATM 6781 O  O    A HOH   F 5 .   ? 17.520 -1.704  0.403   0.64 16.26 ?  362 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 18.941 -0.719  -1.695  1.00 13.48 ?  363 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 31.842 -9.361  -6.686  1.00 22.56 ?  364 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 13.898 -4.919  17.384  1.00 25.97 ?  365 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 31.105 -13.943 -2.472  1.00 14.05 ?  366 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 17.155 -17.779 -5.076  1.00 25.88 ?  367 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 31.690 8.212   14.886  1.00 23.27 ?  368 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 23.502 11.414  4.056   1.00 12.03 ?  369 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 8.858  -12.026 17.113  1.00 44.32 ?  370 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 37.257 -2.808  9.721   1.00 41.61 ?  371 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 21.893 -21.898 8.440   1.00 29.00 ?  372 HOH   A O    1 
HETATM 6792 O  O    A HOH   F 5 .   ? 14.293 0.591   6.755   0.64 14.85 ?  373 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 30.821 3.104   8.267   1.00 11.70 ?  374 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 37.360 11.995  4.924   1.00 28.17 ?  375 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 44.050 8.482   -3.023  1.00 27.18 ?  376 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 43.431 7.816   2.707   1.00 30.08 ?  377 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 15.514 11.851  7.929   1.00 38.98 ?  378 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 33.656 -7.147  4.349   1.00 16.34 ?  379 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 6.402  -5.420  10.983  1.00 18.72 ?  380 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 16.532 -22.062 0.947   1.00 28.69 ?  381 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 15.176 -8.073  -9.784  1.00 22.02 ?  382 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 25.736 -0.780  -7.360  1.00 14.93 ?  383 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 33.531 -16.954 8.113   1.00 19.38 ?  384 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 27.450 -10.604 14.055  1.00 17.64 ?  385 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 31.828 -7.305  -9.852  1.00 21.45 ?  386 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 20.103 4.520   -7.541  1.00 19.31 ?  387 HOH   A O    1 
HETATM 6807 O  O    T HOH   F 5 .   ? 15.430 -0.409  2.344   0.30 11.61 ?  388 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 21.191 10.301  14.976  1.00 34.66 ?  389 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 24.441 3.616   -1.830  1.00 14.89 ?  390 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 21.397 3.118   -0.333  1.00 13.14 ?  391 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 24.141 -7.713  14.414  1.00 16.73 ?  392 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 16.996 -19.279 4.858   1.00 15.31 ?  393 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 15.156 -21.526 14.211  1.00 18.28 ?  394 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 24.670 -17.499 12.734  1.00 23.98 ?  395 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 37.571 -2.039  5.844   1.00 26.98 ?  396 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 22.604 -11.830 21.802  1.00 48.04 ?  397 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 14.067 -23.049 7.428   1.00 18.01 ?  398 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 5.379  2.808   4.938   1.00 29.68 ?  399 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 21.784 -13.822 -8.225  1.00 40.75 ?  400 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 24.594 1.998   -7.036  1.00 19.05 ?  401 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 15.847 2.112   24.708  1.00 43.92 ?  402 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 30.650 1.909   16.700  1.00 20.76 ?  403 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 32.783 -9.259  5.954   1.00 19.25 ?  404 HOH   A O    1 
HETATM 6824 O  O    A HOH   F 5 .   ? 11.090 -0.365  1.886   0.70 24.33 ?  405 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 20.561 -20.018 2.747   1.00 18.61 ?  406 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 30.029 -10.054 13.037  1.00 22.47 ?  407 HOH   A O    1 
HETATM 6827 O  O    A HOH   F 5 .   ? 15.819 -0.930  5.229   0.64 16.43 ?  408 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 26.970 4.187   -0.685  1.00 12.24 ?  409 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 27.232 2.336   18.691  1.00 30.73 ?  410 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 40.940 -8.311  -6.792  1.00 35.82 ?  411 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 23.977 -15.727 -9.240  1.00 38.13 ?  412 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 23.949 -20.276 -1.349  1.00 16.71 ?  413 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 38.155 -1.335  -1.918  1.00 18.73 ?  414 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 30.289 -12.872 13.556  1.00 20.01 ?  415 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 14.556 -0.535  -12.192 1.00 23.60 ?  416 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 32.694 -4.229  -9.893  1.00 27.95 ?  417 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 6.691  -3.236  12.775  1.00 29.40 ?  418 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 19.424 -11.077 23.998  1.00 68.11 ?  419 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 15.982 6.842   2.958   1.00 18.75 ?  420 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 32.513 -10.631 3.237   1.00 30.68 ?  421 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 16.225 16.665  8.582   1.00 34.64 ?  422 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 24.076 3.943   -4.867  1.00 21.49 ?  423 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 35.136 -5.230  -3.093  1.00 17.67 ?  424 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 44.991 -0.636  3.038   1.00 39.84 ?  425 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 36.752 -4.952  5.381   1.00 23.55 ?  426 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 11.617 -10.727 16.851  1.00 24.28 ?  427 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 41.645 1.539   5.047   1.00 36.56 ?  428 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 10.375 -13.731 -1.725  1.00 16.44 ?  429 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 16.202 -14.203 20.136  1.00 51.93 ?  430 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 10.421 -22.202 -1.258  1.00 49.63 ?  431 HOH   A O    1 
HETATM 6851 O  O    A HOH   F 5 .   ? 18.480 4.835   -15.072 0.64 34.42 ?  432 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 22.623 8.220   18.345  1.00 46.53 ?  433 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 23.366 -20.931 1.321   1.00 18.57 ?  434 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 23.461 -8.007  17.067  1.00 21.54 ?  435 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 18.921 1.986   -0.730  1.00 12.87 ?  436 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 27.156 -3.175  19.368  1.00 37.37 ?  437 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 34.430 -8.086  -0.578  1.00 26.46 ?  438 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 23.221 7.586   -3.236  1.00 30.61 ?  439 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 20.609 -17.701 24.782  1.00 53.30 ?  440 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 37.760 -8.830  -3.469  1.00 22.99 ?  441 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 18.383 -15.967 16.281  1.00 37.65 ?  442 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 21.295 -9.227  21.333  1.00 49.29 ?  443 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 31.360 -12.773 0.015   1.00 20.24 ?  444 HOH   A O    1 
HETATM 6864 O  O    A HOH   F 5 .   ? 16.287 2.956   -1.486  0.64 15.78 ?  445 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 30.617 14.811  2.737   1.00 19.19 ?  446 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 9.418  -16.262 -2.024  1.00 43.71 ?  447 HOH   A O    1 
HETATM 6867 O  O    A HOH   F 5 .   ? 14.049 -0.324  3.418   0.34 20.37 ?  448 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 21.465 -14.699 17.922  1.00 52.33 ?  449 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 29.794 -1.943  -12.746 1.00 44.58 ?  450 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 29.781 -16.083 10.781  1.00 34.74 ?  451 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 27.832 7.073   -6.541  1.00 38.74 ?  452 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 25.457 8.242   -4.864  1.00 32.19 ?  453 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 32.469 -15.935 10.859  1.00 30.34 ?  454 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 24.838 5.647   20.715  1.00 54.94 ?  455 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 19.899 -17.356 -5.093  1.00 23.40 ?  456 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 23.157 -22.334 -3.346  1.00 36.35 ?  457 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 18.766 10.905  11.260  1.00 33.26 ?  458 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 24.651 14.702  7.801   1.00 35.84 ?  459 HOH   A O    1 
HETATM 6879 O  O    . HOH   F 5 .   ? 21.923 5.179   -5.920  1.00 32.43 ?  460 HOH   A O    1 
HETATM 6880 O  O    . HOH   F 5 .   ? 23.506 13.766  5.456   1.00 17.70 ?  461 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 15.739 -21.541 3.661   1.00 23.93 ?  462 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 26.957 11.697  -1.415  1.00 32.39 ?  463 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 27.466 -11.390 16.555  1.00 37.52 ?  464 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 39.638 -6.994  -3.511  1.00 45.33 ?  465 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 11.975 -13.411 16.341  1.00 50.34 ?  466 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 25.853 10.819  -3.787  1.00 26.41 ?  467 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 12.287 1.622   17.295  1.00 40.48 ?  468 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 18.086 -16.234 -8.880  1.00 40.27 ?  469 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 10.993 -15.102 -6.130  1.00 34.71 ?  470 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 15.743 -17.133 -7.040  1.00 29.86 ?  471 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 23.153 11.840  -4.099  1.00 19.04 ?  472 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 13.957 -10.323 -10.924 1.00 32.36 ?  473 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 28.800 9.070   17.541  1.00 37.47 ?  474 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 35.232 7.490   12.227  1.00 43.36 ?  475 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 17.436 -18.733 19.820  1.00 49.88 ?  476 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 30.815 0.712   19.142  1.00 38.97 ?  477 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 41.065 -3.966  -0.400  1.00 36.40 ?  478 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 16.803 -20.500 16.137  1.00 28.86 ?  479 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 28.630 -4.665  -12.311 1.00 34.59 ?  480 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 44.582 10.436  -1.621  1.00 31.21 ?  481 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 18.362 -23.175 1.907   1.00 43.55 ?  482 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 28.696 -7.976  -15.285 1.00 47.90 ?  483 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 39.224 2.426   7.433   1.00 31.11 ?  484 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 41.805 9.427   -3.971  1.00 29.73 ?  485 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 23.254 -12.843 19.305  1.00 44.25 ?  486 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 16.065 -6.830  -11.929 1.00 43.10 ?  487 HOH   A O    1 
HETATM 6907 O  O    B HOH   F 5 .   ? 8.769  2.263   -2.707  0.36 20.32 ?  488 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 13.906 -25.250 8.876   1.00 32.09 ?  489 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 31.535 -0.592  -10.563 1.00 30.36 ?  490 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 40.637 -0.264  -7.795  1.00 33.05 ?  491 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 20.065 -22.333 4.205   1.00 27.78 ?  492 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 30.822 5.815   -14.747 1.00 34.91 ?  493 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 20.532 -16.065 -7.411  1.00 29.49 ?  494 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 16.195 -23.405 5.725   1.00 26.70 ?  495 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 30.777 -5.882  -11.916 1.00 46.48 ?  496 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 37.398 -6.634  7.637   1.00 26.55 ?  497 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 23.143 -23.771 1.574   1.00 31.21 ?  498 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 39.528 -0.011  6.605   1.00 29.78 ?  499 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 8.100  -3.096  -5.871  1.00 50.09 ?  500 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 38.048 13.939  6.740   1.00 47.62 ?  501 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 29.038 14.476  0.807   1.00 46.55 ?  502 HOH   A O    1 
HETATM 6922 O  O    B HOH   F 5 .   ? 9.922  -1.520  -4.706  0.36 29.22 ?  503 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 14.762 8.375   4.896   1.00 39.33 ?  504 HOH   A O    1 
HETATM 6924 O  O    B HOH   F 5 .   ? 9.878  1.259   -4.990  0.36 21.51 ?  505 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 22.047 -24.017 4.490   1.00 26.51 ?  506 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 36.481 -6.568  10.162  1.00 45.54 ?  507 HOH   A O    1 
HETATM 6927 O  O    T HOH   F 5 .   ? 11.950 -2.140  -3.699  0.30 11.70 ?  508 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 17.338 -6.612  -14.237 1.00 38.88 ?  509 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 24.123 9.035   -7.244  1.00 37.16 ?  510 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 15.837 -12.212 27.393  1.00 44.60 ?  511 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 16.344 -21.140 18.750  1.00 37.72 ?  512 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 14.738 -22.749 19.850  1.00 34.90 ?  513 HOH   A O    1 
HETATM 6933 O  O    . HOH   G 5 .   ? 29.845 -22.431 5.511   1.00 19.42 ?  201 HOH   B O    1 
HETATM 6934 O  O    . HOH   G 5 .   ? 41.759 -36.045 -17.146 1.00 32.87 ?  202 HOH   B O    1 
HETATM 6935 O  O    . HOH   G 5 .   ? 27.726 -29.204 -1.833  1.00 35.80 ?  203 HOH   B O    1 
HETATM 6936 O  O    . HOH   G 5 .   ? 38.033 -39.502 -0.174  1.00 37.98 ?  204 HOH   B O    1 
HETATM 6937 O  O    . HOH   G 5 .   ? 48.132 -6.883  15.557  1.00 31.37 ?  205 HOH   B O    1 
HETATM 6938 O  O    . HOH   G 5 .   ? 41.359 -7.871  5.468   1.00 40.17 ?  206 HOH   B O    1 
HETATM 6939 O  O    . HOH   G 5 .   ? 59.201 -18.698 6.874   1.00 36.51 ?  207 HOH   B O    1 
HETATM 6940 O  O    . HOH   G 5 .   ? 57.753 -24.532 5.057   1.00 36.60 ?  208 HOH   B O    1 
HETATM 6941 O  O    . HOH   G 5 .   ? 54.558 -9.414  -8.690  1.00 19.11 ?  209 HOH   B O    1 
HETATM 6942 O  O    . HOH   G 5 .   ? 30.243 -41.051 -8.025  1.00 17.00 ?  210 HOH   B O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 29.944 -26.319 4.076   1.00 27.21 ?  211 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 47.456 -7.404  -3.895  1.00 38.41 ?  212 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 56.392 -19.736 7.291   1.00 31.18 ?  213 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 27.914 -41.948 -15.108 1.00 36.92 ?  214 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 49.510 -22.717 -19.745 1.00 46.50 ?  215 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 44.455 -7.248  2.028   1.00 35.03 ?  216 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 53.000 -13.467 -20.375 1.00 35.22 ?  217 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 58.271 -12.941 8.434   1.00 32.10 ?  218 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 57.177 -26.885 -7.675  1.00 41.22 ?  219 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 37.119 -19.905 -18.100 1.00 35.83 ?  220 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 56.729 -30.786 -7.759  1.00 29.43 ?  221 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 50.276 -3.341  7.136   1.00 35.20 ?  222 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 30.938 -28.766 4.346   1.00 28.35 ?  223 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 36.020 -43.382 -8.483  1.00 32.64 ?  224 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 55.472 -16.581 -14.356 1.00 33.67 ?  225 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 34.564 -36.420 -7.171  1.00 18.80 ?  226 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 50.816 -6.099  0.165   1.00 27.10 ?  227 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 41.543 -39.235 -14.840 1.00 22.38 ?  228 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 34.916 -24.632 13.830  1.00 32.71 ?  229 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 57.457 -16.288 -12.219 1.00 18.58 ?  230 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 51.724 -6.471  4.357   1.00 19.21 ?  231 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 29.858 -34.223 -0.400  1.00 36.19 ?  232 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 40.659 -16.075 14.117  1.00 23.61 ?  233 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 32.813 -43.845 -11.282 1.00 20.74 ?  234 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 39.355 -10.906 6.123   1.00 25.01 ?  235 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 50.780 -12.995 -0.468  1.00 11.79 ?  236 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 46.442 -1.568  13.218  1.00 27.69 ?  237 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 25.449 -25.961 -1.287  1.00 31.75 ?  238 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 42.591 -25.386 2.680   1.00 15.30 ?  239 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 51.607 -13.844 11.014  1.00 26.85 ?  240 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 44.546 -27.760 -0.669  1.00 21.97 ?  241 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 41.388 -9.617  13.103  1.00 21.94 ?  242 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 48.598 -36.571 -15.492 1.00 43.13 ?  243 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 35.154 -7.993  -3.014  1.00 17.51 ?  244 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 39.535 -11.117 0.341   1.00 16.20 ?  245 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 44.945 -43.634 -10.447 1.00 28.17 ?  246 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 48.052 -24.580 -17.762 1.00 30.86 ?  247 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 28.424 -19.727 -13.121 1.00 24.74 ?  248 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 41.896 -23.521 9.324   1.00 18.10 ?  249 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 43.079 -43.297 -8.148  1.00 28.70 ?  250 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 42.671 -22.880 3.873   1.00 11.64 ?  251 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 57.676 -24.408 -3.789  1.00 20.90 ?  252 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 34.287 -18.417 11.442  1.00 25.18 ?  253 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 45.144 -34.996 6.810   1.00 44.72 ?  254 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 50.984 -40.017 -8.179  1.00 35.21 ?  255 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 38.508 -11.065 -2.250  1.00 18.73 ?  256 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 40.373 -12.768 -11.515 1.00 15.34 ?  257 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 43.251 -32.442 -17.043 1.00 23.78 ?  258 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 30.874 -15.730 2.681   1.00 14.00 ?  259 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 58.244 -10.671 -4.075  1.00 20.35 ?  260 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 31.799 -17.924 -14.506 1.00 31.56 ?  261 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 56.180 -23.626 -14.736 1.00 27.43 ?  262 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 49.764 -0.491  10.220  1.00 29.90 ?  263 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 29.762 -25.261 -10.780 1.00 16.96 ?  264 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 38.943 -11.912 12.359  1.00 34.35 ?  265 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 48.052 -22.773 5.854   1.00 17.94 ?  266 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 46.661 -31.299 -4.778  1.00 21.59 ?  267 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 42.407 -34.741 3.814   1.00 26.77 ?  268 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 30.556 -42.296 -10.562 1.00 29.55 ?  269 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 57.541 -9.238  1.439   1.00 19.28 ?  270 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 43.415 -15.819 -12.179 1.00 14.16 ?  271 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 42.382 -9.924  9.347   1.00 20.44 ?  272 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 28.508 -30.983 -14.656 1.00 30.74 ?  273 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 27.158 -31.873 -9.960  1.00 19.65 ?  274 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 46.902 -29.585 9.848   1.00 32.02 ?  275 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 49.368 -28.739 -6.861  1.00 15.32 ?  276 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 42.932 -20.343 -20.711 1.00 38.75 ?  277 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 56.982 -8.644  8.450   1.00 18.57 ?  278 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 28.277 -34.405 -9.398  1.00 17.99 ?  279 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 34.500 -12.790 2.641   1.00 24.66 ?  280 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 27.992 -22.907 -7.964  1.00 17.99 ?  281 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 35.011 -33.376 -19.185 1.00 31.02 ?  282 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 41.216 -5.511  11.483  1.00 46.54 ?  283 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 50.064 -24.634 5.815   1.00 33.35 ?  284 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 59.834 -15.290 8.151   1.00 33.08 ?  285 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 27.597 -26.699 -15.605 1.00 32.22 ?  286 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 48.445 -25.068 3.146   1.00 13.47 ?  287 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 45.343 -33.448 -15.883 1.00 24.04 ?  288 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 52.578 -10.374 13.009  1.00 21.49 ?  289 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 36.847 -12.775 -1.493  1.00 26.35 ?  290 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 33.554 -15.325 -13.942 1.00 21.16 ?  291 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 42.395 -9.921  -14.870 1.00 38.37 ?  292 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 47.115 -34.006 -4.576  1.00 17.89 ?  293 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 51.265 -37.629 -9.577  1.00 27.40 ?  294 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 44.667 -27.492 2.026   1.00 15.79 ?  295 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 37.482 -18.088 13.105  1.00 32.24 ?  296 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 48.732 -20.034 5.969   1.00 13.69 ?  297 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 57.138 -12.076 12.405  1.00 39.04 ?  298 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 42.713 -12.308 -18.505 1.00 29.81 ?  299 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 44.077 -29.376 -4.650  1.00 23.17 ?  300 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 52.543 -29.299 -13.016 1.00 25.28 ?  301 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 45.951 -40.451 -3.518  1.00 29.45 ?  302 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 40.306 -10.869 -9.544  1.00 16.96 ?  303 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 52.654 -35.681 -8.638  1.00 28.88 ?  304 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 62.768 -13.598 4.760   1.00 27.05 ?  305 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 48.652 -12.049 -14.198 1.00 26.33 ?  306 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 53.123 -16.071 -12.741 1.00 26.93 ?  307 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 53.540 -30.215 4.542   1.00 19.05 ?  308 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 35.104 -33.558 4.612   1.00 29.05 ?  309 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 37.892 -10.271 -10.789 1.00 17.32 ?  310 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 62.901 -20.242 -0.796  1.00 36.12 ?  311 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 25.964 -21.501 -3.531  1.00 16.61 ?  312 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 37.328 -35.691 7.266   1.00 32.79 ?  313 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 51.405 -33.039 -10.756 1.00 39.70 ?  314 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 51.786 -5.981  -7.879  1.00 46.52 ?  315 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 41.793 -8.054  1.348   1.00 23.74 ?  316 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 37.140 -30.626 -20.988 1.00 31.89 ?  317 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 32.839 -34.631 -5.864  1.00 17.10 ?  318 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 43.236 -21.433 10.703  1.00 16.09 ?  319 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 60.022 -17.157 -10.444 1.00 33.62 ?  320 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 38.366 -12.720 7.941   1.00 18.37 ?  321 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 26.367 -21.074 -6.209  1.00 16.79 ?  322 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 48.104 -32.706 -16.618 1.00 43.92 ?  323 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 43.525 -15.421 18.191  1.00 28.65 ?  324 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 53.690 -12.572 -22.234 1.00 33.19 ?  325 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 36.765 -12.405 4.308   1.00 17.31 ?  326 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 44.165 -1.742  7.620   1.00 46.92 ?  327 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 44.659 -24.594 9.614   1.00 20.29 ?  328 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 43.160 -34.629 0.141   1.00 20.79 ?  329 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 38.450 -9.373  -13.303 1.00 26.34 ?  330 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 57.607 -22.008 3.373   1.00 30.19 ?  331 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 47.215 -24.504 8.192   1.00 25.47 ?  332 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 27.918 -14.814 -9.479  1.00 35.62 ?  333 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 33.627 -31.211 11.073  1.00 33.36 ?  334 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 47.511 -27.458 2.041   1.00 14.79 ?  335 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 45.719 -36.344 -16.065 1.00 35.04 ?  336 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 41.258 -24.450 15.919  1.00 45.79 ?  337 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 42.861 -43.550 -14.318 1.00 42.64 ?  338 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 37.087 -15.138 -16.519 1.00 39.87 ?  339 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 38.518 -12.193 -16.230 1.00 43.34 ?  340 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 46.857 -19.921 12.331  1.00 30.23 ?  341 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 28.909 -42.966 -12.351 1.00 39.60 ?  342 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 39.504 -23.602 -20.389 1.00 35.47 ?  343 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 37.116 -45.243 -9.729  1.00 35.47 ?  344 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 33.033 -14.687 1.070   1.00 19.96 ?  345 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 34.569 -10.338 7.671   1.00 23.33 ?  346 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 39.843 -44.343 -11.163 1.00 39.53 ?  347 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 33.745 -9.550  -8.878  1.00 32.18 ?  348 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 40.447 -43.544 -9.079  1.00 26.93 ?  349 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 38.557 -22.353 15.034  1.00 39.19 ?  350 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 62.593 -20.165 -4.801  1.00 42.70 ?  351 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 27.780 -26.613 -0.527  1.00 29.93 ?  352 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 44.169 -37.391 -17.666 1.00 35.26 ?  353 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 55.714 -8.274  10.842  1.00 24.09 ?  354 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 23.229 -23.658 6.834   1.00 32.47 ?  355 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 56.630 -7.301  3.111   1.00 26.13 ?  356 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 36.101 -8.567  -9.718  1.00 34.59 ?  357 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 34.147 -7.756  11.446  1.00 39.05 ?  358 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 61.587 -19.926 1.738   1.00 36.12 ?  359 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 56.962 -21.646 -16.405 1.00 39.94 ?  360 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 40.277 -8.804  9.901   1.00 34.70 ?  361 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 27.167 -25.972 -11.391 1.00 33.08 ?  362 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 43.229 -12.680 -21.185 1.00 41.62 ?  363 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 54.249 -5.730  2.981   1.00 35.26 ?  364 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 40.262 -11.349 -13.972 1.00 32.40 ?  365 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 58.909 -10.476 9.259   1.00 39.69 ?  366 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 32.584 -23.646 14.093  1.00 38.99 ?  367 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 48.360 -26.478 8.848   1.00 40.48 ?  368 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 36.174 -8.659  8.981   1.00 33.73 ?  369 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 39.870 -7.052  7.865   1.00 39.65 ?  370 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 56.148 -7.817  -0.628  1.00 33.76 ?  371 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 63.093 -12.449 6.946   1.00 36.45 ?  372 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 52.088 -12.934 13.370  1.00 30.56 ?  373 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 41.853 -10.002 -17.453 1.00 50.84 ?  374 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 38.081 -10.616 10.064  1.00 28.95 ?  375 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 41.891 -6.766  -4.908  1.00 46.38 ?  376 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 36.541 -22.858 13.305  1.00 28.22 ?  377 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 42.673 -17.093 -23.168 1.00 44.58 ?  378 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 40.127 -7.662  3.212   1.00 34.02 ?  379 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 44.077 -5.562  -3.495  1.00 41.39 ?  380 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 39.675 -14.036 15.688  1.00 49.94 ?  381 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 52.900 -29.912 7.215   1.00 23.26 ?  382 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 60.557 -22.271 2.903   1.00 46.49 ?  383 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 25.819 -18.890 -11.865 1.00 40.74 ?  384 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 46.852 -5.325  2.848   1.00 37.91 ?  385 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 35.469 -33.718 7.369   1.00 39.56 ?  386 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 35.303 -20.354 13.299  1.00 32.68 ?  387 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 41.004 -9.731  15.830  1.00 46.63 ?  388 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 23.945 -20.913 -7.639  1.00 28.61 ?  389 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 40.733 -6.608  -0.879  1.00 24.73 ?  390 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 44.129 -31.765 -3.739  1.00 35.33 ?  391 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 26.663 -28.023 -13.463 1.00 34.59 ?  392 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 27.948 -27.097 2.236   1.00 29.22 ?  393 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 50.652 -30.841 8.715   1.00 28.75 ?  394 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 24.665 -20.669 -10.502 1.00 39.47 ?  395 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 34.416 -33.486 9.654   1.00 35.64 ?  396 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 26.858 -30.716 -12.599 1.00 28.62 ?  397 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 45.771 -20.164 15.204  1.00 49.71 ?  398 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 57.758 -6.577  -2.377  1.00 33.90 ?  399 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 40.927 -11.826 -22.316 1.00 39.07 ?  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   ? 0.6678 0.6723 0.7420 -0.0047 -0.0227 0.0726  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6655 0.6692 0.7195 -0.0081 -0.0211 0.0578  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6648 0.6690 0.7306 -0.0060 -0.0226 0.0722  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6624 0.6663 0.7114 -0.0091 -0.0214 0.0587  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6465 0.6532 0.7057 -0.0133 -0.0263 0.0734  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6453 0.6518 0.6935 -0.0150 -0.0252 0.0656  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6492 0.6553 0.7204 -0.0120 -0.0279 0.0765  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6481 0.6539 0.7051 -0.0139 -0.0263 0.0670  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6762 0.6786 0.7357 -0.0011 -0.0179 0.0703  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6730 0.6750 0.7147 -0.0052 -0.0174 0.0531  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6796 0.6814 0.7363 0.0003  -0.0161 0.0703  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6762 0.6777 0.7155 -0.0040 -0.0158 0.0516  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6801 0.6818 0.7369 0.0012  -0.0159 0.0703  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6766 0.6779 0.7156 -0.0035 -0.0157 0.0516  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6215 0.6322 0.6536 -0.0226 -0.0271 0.0708  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5683 0.5876 0.5504 -0.0407 -0.0292 0.0698  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5001 0.5372 0.4824 -0.0584 -0.0134 0.0379  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5032 0.5401 0.4823 -0.0578 -0.0172 0.0414  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5799 0.5906 0.5116 -0.0426 -0.0447 0.0993  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5886 0.5905 0.4723 -0.0453 -0.0589 0.1253  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5938 0.5890 0.4544 -0.0458 -0.0638 0.1364  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5900 0.5908 0.4620 -0.0461 -0.0625 0.1368  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.4597 0.5087 0.4455 -0.0730 0.0016  0.0195  5   SER   A N   
47   N  N   B SER   A 5   ? 0.4672 0.5087 0.4494 -0.0631 -0.0095 0.0205  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4184 0.4787 0.4080 -0.0867 0.0178  0.0026  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4331 0.4789 0.4143 -0.0661 -0.0051 0.0036  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.3741 0.4395 0.3591 -0.0955 0.0354  -0.0027 5   SER   A C   
51   C  C   B SER   A 5   ? 0.3957 0.4431 0.3692 -0.0655 0.0011  -0.0055 5   SER   A C   
52   O  O   A SER   A 5   ? 0.3794 0.4473 0.3594 -0.0897 0.0413  -0.0138 5   SER   A O   
53   O  O   B SER   A 5   ? 0.3972 0.4462 0.3697 -0.0642 -0.0002 -0.0116 5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4239 0.4864 0.4187 -0.0896 0.0184  -0.0063 5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4373 0.4841 0.4221 -0.0679 -0.0058 -0.0029 5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4283 0.4908 0.4265 -0.0897 0.0210  -0.0109 5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4400 0.4871 0.4266 -0.0681 -0.0056 -0.0068 5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3219 0.3909 0.3038 -0.1091 0.0468  0.0085  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3553 0.4035 0.3216 -0.0645 0.0094  -0.0061 6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2734 0.3414 0.2419 -0.1160 0.0497  0.0269  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3166 0.3636 0.2738 -0.0613 0.0153  -0.0040 6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2603 0.3329 0.2329 -0.1233 0.0626  0.0280  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3022 0.3504 0.2623 -0.0586 0.0246  -0.0093 6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2647 0.3373 0.2557 -0.1221 0.0732  0.0342  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3028 0.3518 0.2592 -0.0621 0.0270  -0.0083 6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2479 0.3047 0.2053 -0.1087 0.0325  0.0408  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.2953 0.3374 0.2440 -0.0596 0.0112  0.0009  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2275 0.2792 0.1951 -0.0962 0.0190  0.0492  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.2750 0.3155 0.2268 -0.0581 0.0098  0.0059  6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2193 0.2679 0.1925 -0.0884 0.0118  0.0493  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.2660 0.3058 0.2135 -0.0556 0.0070  0.0100  6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2311 0.2734 0.2093 -0.0829 0.0098  0.0501  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.2702 0.3078 0.2339 -0.0536 0.0128  0.0065  6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2209 0.2671 0.1967 -0.0804 0.0125  0.0525  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2611 0.3011 0.2167 -0.0554 0.0102  0.0102  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2304 0.2708 0.2165 -0.0773 0.0042  0.0444  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.2655 0.3027 0.2337 -0.0532 0.0146  0.0056  6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2273 0.2685 0.2021 -0.0777 0.0043  0.0455  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2614 0.3003 0.2270 -0.0544 0.0120  0.0063  6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2459 0.3178 0.2037 -0.1293 0.0611  0.0277  7   SER   A N   
109  N  N   B SER   A 7   ? 0.2881 0.3370 0.2641 -0.0517 0.0287  -0.0145 7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2412 0.3123 0.2076 -0.1164 0.0540  0.0050  7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.2757 0.3219 0.2695 -0.0436 0.0345  -0.0184 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2293 0.2819 0.1849 -0.1058 0.0561  0.0055  7   SER   A C   
113  C  C   B SER   A 7   ? 0.2606 0.2997 0.2554 -0.0380 0.0431  -0.0151 7   SER   A C   
114  O  O   A SER   A 7   ? 0.2409 0.2734 0.1646 -0.1059 0.0587  0.0110  7   SER   A O   
115  O  O   B SER   A 7   ? 0.2638 0.3006 0.2579 -0.0368 0.0426  -0.0206 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2564 0.3430 0.2320 -0.0992 0.0630  -0.0017 7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.2818 0.3292 0.2924 -0.0382 0.0313  -0.0267 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2682 0.3624 0.2585 -0.0909 0.0574  -0.0137 7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.2822 0.3346 0.3040 -0.0367 0.0312  -0.0289 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2081 0.2609 0.1937 -0.0918 0.0461  -0.0027 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2420 0.2750 0.2389 -0.0344 0.0485  -0.0087 8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.1943 0.2370 0.1986 -0.0678 0.0380  -0.0039 8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2248 0.2495 0.2242 -0.0261 0.0467  0.0016  8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1722 0.2177 0.2008 -0.0479 0.0367  -0.0025 8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2040 0.2273 0.2054 -0.0197 0.0441  0.0118  8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1749 0.2204 0.2259 -0.0277 0.0491  -0.0223 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2061 0.2281 0.2081 -0.0149 0.0493  0.0074  8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1554 0.2006 0.2029 -0.0387 0.0374  0.0166  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.1822 0.2055 0.1982 -0.0136 0.0330  0.0282  9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1430 0.1888 0.1880 -0.0374 0.0300  0.0187  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1672 0.1902 0.1847 -0.0109 0.0255  0.0297  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1428 0.1612 0.1776 -0.0243 0.0348  0.0320  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1559 0.1675 0.1783 0.0024  0.0229  0.0320  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1557 0.1612 0.1955 -0.0156 0.0392  0.0237  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1585 0.1758 0.1990 0.0136  0.0168  0.0297  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1361 0.2072 0.1936 -0.0348 0.0303  0.0089  9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1681 0.2000 0.1864 -0.0145 0.0243  0.0221  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1362 0.2200 0.1978 -0.0265 0.0370  0.0061  9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1718 0.2085 0.1912 -0.0165 0.0279  0.0157  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1428 0.2300 0.2084 -0.0402 0.0472  0.0025  9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1769 0.2154 0.2006 -0.0265 0.0332  0.0116  9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1357 0.2130 0.1974 -0.0190 0.0270  0.0174  9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1716 0.2040 0.1880 -0.0130 0.0248  0.0185  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1500 0.2336 0.2252 -0.0441 0.0464  -0.0008 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1812 0.2174 0.2096 -0.0290 0.0341  0.0064  9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1390 0.2195 0.2044 -0.0266 0.0282  0.0110  9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1749 0.2080 0.1934 -0.0174 0.0267  0.0134  9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1394 0.2286 0.2289 -0.0471 0.0492  -0.0008 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1789 0.2152 0.2123 -0.0288 0.0387  0.0070  9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1470 0.2379 0.2556 -0.0646 0.0475  -0.0082 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1881 0.2226 0.2311 -0.0354 0.0433  0.0039  9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1436 0.1522 0.1876 -0.0276 0.0184  0.0379  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1516 0.1531 0.1672 -0.0009 0.0167  0.0297  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1302 0.1505 0.1992 -0.0280 0.0146  0.0466  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1456 0.1509 0.1687 -0.0044 0.0112  0.0322  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1243 0.1438 0.1970 -0.0188 0.0165  0.0474  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1441 0.1477 0.1687 -0.0132 0.0081  0.0403  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1202 0.1433 0.2012 -0.0116 0.0194  0.0484  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1391 0.1398 0.1816 -0.0136 0.0154  0.0524  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1335 0.1541 0.2176 -0.0189 0.0064  0.0546  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1514 0.1579 0.1787 -0.0027 0.0040  0.0335  10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1483 0.1674 0.2534 -0.0031 -0.0190 0.0582  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1621 0.1712 0.2051 0.0037  -0.0041 0.0304  10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1687 0.1763 0.2731 -0.0174 -0.0103 0.0424  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.1713 0.1797 0.2246 -0.0055 0.0042  0.0231  10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1548 0.1871 0.2670 0.0101  -0.0076 0.0530  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.1735 0.1830 0.2267 0.0115  -0.0206 0.0299  10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1289 0.1446 0.1887 -0.0247 0.0289  0.0421  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1463 0.1483 0.1528 -0.0218 -0.0005 0.0318  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1345 0.1355 0.1942 -0.0267 0.0232  0.0365  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1466 0.1443 0.1491 -0.0308 0.0015  0.0326  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1307 0.1333 0.2074 -0.0226 0.0202  0.0263  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1379 0.1292 0.1472 -0.0288 0.0060  0.0214  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1409 0.1506 0.2442 -0.0418 0.0241  0.0144  11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1351 0.1205 0.1599 -0.0259 0.0121  0.0060  11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1432 0.1359 0.1803 -0.0226 0.0110  0.0273  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1561 0.1448 0.1582 -0.0322 -0.0031 0.0368  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1546 0.1355 0.1797 -0.0246 0.0054  0.0321  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1636 0.1486 0.1659 -0.0343 0.0023  0.0519  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1641 0.1409 0.1887 -0.0279 -0.0052 0.0312  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.1717 0.1609 0.1843 -0.0300 0.0077  0.0600  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1718 0.1389 0.1757 -0.0185 -0.0098 0.0323  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.1732 0.1637 0.1837 -0.0232 0.0053  0.0677  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1738 0.1419 0.1928 -0.0076 -0.0117 0.0345  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1704 0.1671 0.1991 -0.0171 0.0014  0.0636  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1232 0.1250 0.1968 -0.0273 0.0180  0.0330  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1323 0.1401 0.1576 -0.0159 0.0003  0.0137  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1301 0.1381 0.1828 -0.0196 0.0093  0.0370  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1310 0.1527 0.1587 -0.0090 0.0082  0.0141  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1385 0.1302 0.1874 -0.0250 0.0096  0.0370  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1332 0.1572 0.1633 -0.0060 0.0235  0.0164  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1437 0.1314 0.1944 -0.0213 0.0053  0.0160  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1365 0.1576 0.1599 0.0017  0.0172  0.0112  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1359 0.1391 0.1836 -0.0152 0.0070  0.0366  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1330 0.1593 0.1737 -0.0024 0.0038  0.0123  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1433 0.1467 0.1986 -0.0094 0.0198  0.0383  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1371 0.1642 0.1894 0.0044  0.0109  0.0094  12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1506 0.1569 0.2075 0.0056  0.0396  0.0526  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1375 0.1707 0.1908 0.0160  0.0257  0.0113  12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1387 0.1537 0.2057 -0.0093 0.0205  0.0365  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1384 0.1679 0.1974 0.0045  0.0105  -0.0022 12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1360 0.1305 0.1909 -0.0223 0.0058  0.0366  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1307 0.1573 0.1704 -0.0077 0.0247  0.0186  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1366 0.1314 0.1972 -0.0197 0.0075  0.0283  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1335 0.1598 0.1797 -0.0079 0.0243  0.0246  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1376 0.1365 0.2096 -0.0215 0.0060  0.0356  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1382 0.1683 0.1826 -0.0131 0.0230  0.0328  13  THR   A C   
312  O  O   A THR   A 13  ? 0.1340 0.1362 0.2188 -0.0159 0.0027  0.0386  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1441 0.1716 0.1846 -0.0159 0.0188  0.0447  13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1394 0.1444 0.2102 -0.0150 0.0052  0.0305  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1333 0.1611 0.1911 -0.0004 0.0281  0.0371  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1350 0.1419 0.2234 -0.0170 -0.0076 0.0436  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1203 0.1607 0.2097 -0.0008 0.0373  0.0499  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1460 0.1687 0.2224 -0.0152 0.0096  0.0152  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1410 0.1746 0.1986 0.0037  0.0281  0.0286  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1418 0.1357 0.2231 -0.0296 0.0040  0.0550  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1405 0.1694 0.2016 -0.0166 0.0148  0.0388  14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1431 0.1495 0.2532 -0.0261 -0.0114 0.0664  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1441 0.1728 0.2197 -0.0127 -0.0014 0.0503  14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1416 0.1514 0.2314 -0.0275 -0.0139 0.0666  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1402 0.1600 0.2138 -0.0105 -0.0062 0.0574  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1558 0.1510 0.2360 -0.0394 -0.0221 0.0682  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1456 0.1616 0.2151 -0.0018 -0.0073 0.0544  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1564 0.1698 0.3161 -0.0298 -0.0156 0.0833  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1526 0.1928 0.2557 -0.0168 -0.0096 0.0568  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1803 0.2131 0.3972 -0.0336 -0.0110 0.0771  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1540 0.2150 0.2923 -0.0271 -0.0080 0.0611  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.1920 0.2421 0.4260 -0.0166 -0.0297 0.0733  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1550 0.2241 0.3052 -0.0344 -0.0038 0.0633  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.2049 0.2306 0.4334 -0.0467 -0.0094 0.0599  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1584 0.2248 0.3126 -0.0282 -0.0127 0.0581  14  ASP   A OD2 
358  N  N   . ASN   A 15  ? 0.1346 0.1448 0.2260 -0.0234 -0.0040 0.0667  15  ASN   A N   
359  C  CA  . ASN   A 15  ? 0.1403 0.1446 0.2397 -0.0175 -0.0115 0.0571  15  ASN   A CA  
360  C  C   . ASN   A 15  ? 0.1380 0.1441 0.2418 -0.0229 -0.0033 0.0553  15  ASN   A C   
361  O  O   . ASN   A 15  ? 0.1432 0.1454 0.2874 -0.0253 -0.0202 0.0458  15  ASN   A O   
362  C  CB  . ASN   A 15  ? 0.1373 0.1475 0.2306 -0.0087 -0.0077 0.0531  15  ASN   A CB  
363  C  CG  . ASN   A 15  ? 0.1423 0.1485 0.2420 -0.0092 -0.0002 0.0331  15  ASN   A CG  
364  O  OD1 . ASN   A 15  ? 0.1543 0.1522 0.2485 -0.0230 -0.0048 0.0339  15  ASN   A OD1 
365  N  ND2 . ASN   A 15  ? 0.1495 0.1556 0.2273 -0.0193 0.0059  0.0345  15  ASN   A ND2 
373  N  N   A VAL   A 16  ? 0.1392 0.1435 0.2281 -0.0233 -0.0032 0.0551  16  VAL   A N   
374  N  N   B VAL   A 16  ? 0.1386 0.1485 0.2216 -0.0229 -0.0003 0.0499  16  VAL   A N   
375  C  CA  A VAL   A 16  ? 0.1328 0.1414 0.2181 -0.0207 -0.0004 0.0570  16  VAL   A CA  
376  C  CA  B VAL   A 16  ? 0.1358 0.1497 0.2064 -0.0218 0.0053  0.0458  16  VAL   A CA  
377  C  C   A VAL   A 16  ? 0.1260 0.1456 0.2092 -0.0228 0.0021  0.0471  16  VAL   A C   
378  C  C   B VAL   A 16  ? 0.1279 0.1490 0.2008 -0.0219 0.0067  0.0442  16  VAL   A C   
379  O  O   A VAL   A 16  ? 0.1249 0.1403 0.2153 -0.0184 0.0093  0.0467  16  VAL   A O   
380  O  O   B VAL   A 16  ? 0.1268 0.1488 0.2037 -0.0186 0.0136  0.0409  16  VAL   A O   
381  C  CB  A VAL   A 16  ? 0.1398 0.1540 0.2193 -0.0028 0.0210  0.0595  16  VAL   A CB  
382  C  CB  B VAL   A 16  ? 0.1441 0.1591 0.2008 -0.0146 0.0214  0.0418  16  VAL   A CB  
383  C  CG1 A VAL   A 16  ? 0.1513 0.1639 0.2212 0.0018  0.0218  0.0651  16  VAL   A CG1 
384  C  CG1 B VAL   A 16  ? 0.1492 0.1653 0.1988 -0.0137 0.0233  0.0420  16  VAL   A CG1 
385  C  CG2 A VAL   A 16  ? 0.1464 0.1684 0.2296 0.0031  0.0359  0.0535  16  VAL   A CG2 
386  C  CG2 B VAL   A 16  ? 0.1493 0.1669 0.2068 -0.0137 0.0305  0.0318  16  VAL   A CG2 
405  N  N   . TYR   A 17  ? 0.1203 0.1466 0.2001 -0.0218 0.0054  0.0519  17  TYR   A N   
406  C  CA  . TYR   A 17  ? 0.1287 0.1476 0.1915 -0.0275 0.0008  0.0530  17  TYR   A CA  
407  C  C   . TYR   A 17  ? 0.1377 0.1435 0.1989 -0.0214 0.0084  0.0450  17  TYR   A C   
408  O  O   . TYR   A 17  ? 0.1284 0.1462 0.2183 -0.0199 0.0186  0.0602  17  TYR   A O   
409  C  CB  . TYR   A 17  ? 0.1505 0.1478 0.1879 -0.0352 -0.0123 0.0519  17  TYR   A CB  
410  C  CG  . TYR   A 17  ? 0.1752 0.1582 0.1975 -0.0390 -0.0282 0.0409  17  TYR   A CG  
411  C  CD1 . TYR   A 17  ? 0.1909 0.1696 0.2148 -0.0226 -0.0332 0.0421  17  TYR   A CD1 
412  C  CD2 . TYR   A 17  ? 0.1915 0.1633 0.1907 -0.0498 -0.0181 0.0451  17  TYR   A CD2 
413  C  CE1 . TYR   A 17  ? 0.2003 0.1666 0.2182 -0.0280 -0.0373 0.0402  17  TYR   A CE1 
414  C  CE2 . TYR   A 17  ? 0.2077 0.1651 0.2064 -0.0528 -0.0296 0.0333  17  TYR   A CE2 
415  C  CZ  . TYR   A 17  ? 0.2164 0.1630 0.2170 -0.0434 -0.0380 0.0452  17  TYR   A CZ  
416  O  OH  . TYR   A 17  ? 0.2458 0.1612 0.2289 -0.0367 -0.0432 0.0460  17  TYR   A OH  
427  N  N   A ILE   A 18  ? 0.1373 0.1416 0.2022 -0.0167 0.0113  0.0606  18  ILE   A N   
428  N  N   B ILE   A 18  ? 0.1389 0.1504 0.1802 -0.0219 0.0167  0.0396  18  ILE   A N   
429  C  CA  A ILE   A 18  ? 0.1355 0.1426 0.2056 -0.0157 0.0187  0.0523  18  ILE   A CA  
430  C  CA  B ILE   A 18  ? 0.1374 0.1563 0.1566 -0.0176 0.0223  0.0253  18  ILE   A CA  
431  C  C   A ILE   A 18  ? 0.1357 0.1468 0.2152 -0.0279 0.0199  0.0523  18  ILE   A C   
432  C  C   B ILE   A 18  ? 0.1388 0.1664 0.1363 -0.0185 0.0129  0.0284  18  ILE   A C   
433  O  O   A ILE   A 18  ? 0.1288 0.1579 0.2097 -0.0329 0.0110  0.0512  18  ILE   A O   
434  O  O   B ILE   A 18  ? 0.1338 0.1738 0.1412 -0.0297 0.0063  0.0216  18  ILE   A O   
435  C  CB  A ILE   A 18  ? 0.1402 0.1391 0.1922 -0.0024 0.0197  0.0525  18  ILE   A CB  
436  C  CB  B ILE   A 18  ? 0.1375 0.1509 0.1472 -0.0126 0.0395  0.0215  18  ILE   A CB  
437  C  CG1 A ILE   A 18  ? 0.1528 0.1457 0.1844 0.0165  0.0085  0.0434  18  ILE   A CG1 
438  C  CG1 B ILE   A 18  ? 0.1510 0.1626 0.1586 -0.0155 0.0434  0.0274  18  ILE   A CG1 
439  C  CG2 A ILE   A 18  ? 0.1365 0.1365 0.1962 0.0080  0.0150  0.0386  18  ILE   A CG2 
440  C  CG2 B ILE   A 18  ? 0.1428 0.1558 0.1538 -0.0082 0.0346  0.0193  18  ILE   A CG2 
441  C  CD1 A ILE   A 18  ? 0.1715 0.1525 0.1957 0.0338  0.0143  0.0489  18  ILE   A CD1 
442  C  CD1 B ILE   A 18  ? 0.1640 0.1752 0.1703 -0.0089 0.0481  0.0192  18  ILE   A CD1 
465  N  N   A LYS   A 19  ? 0.1390 0.1510 0.2162 -0.0173 0.0374  0.0494  19  LYS   A N   
466  N  N   B LYS   A 19  ? 0.1447 0.1711 0.1346 -0.0039 0.0258  0.0195  19  LYS   A N   
467  C  CA  A LYS   A 19  ? 0.1510 0.1658 0.2139 -0.0164 0.0376  0.0555  19  LYS   A CA  
468  C  CA  B LYS   A 19  ? 0.1625 0.1835 0.1574 0.0026  0.0311  0.0126  19  LYS   A CA  
469  C  C   A LYS   A 19  ? 0.1371 0.1533 0.2226 -0.0128 0.0377  0.0580  19  LYS   A C   
470  C  C   B LYS   A 19  ? 0.1612 0.1765 0.1648 0.0101  0.0252  0.0134  19  LYS   A C   
471  O  O   A LYS   A 19  ? 0.1300 0.1482 0.2223 -0.0119 0.0368  0.0535  19  LYS   A O   
472  O  O   B LYS   A 19  ? 0.1589 0.1686 0.1570 0.0105  0.0127  0.0175  19  LYS   A O   
473  C  CB  A LYS   A 19  ? 0.1742 0.1896 0.2039 -0.0160 0.0407  0.0567  19  LYS   A CB  
474  C  CB  B LYS   A 19  ? 0.1755 0.1973 0.1695 0.0003  0.0399  0.0028  19  LYS   A CB  
475  C  CG  A LYS   A 19  ? 0.2055 0.2132 0.2173 -0.0139 0.0334  0.0401  19  LYS   A CG  
476  C  CG  B LYS   A 19  ? 0.1992 0.2094 0.1826 -0.0007 0.0370  0.0023  19  LYS   A CG  
477  C  CD  A LYS   A 19  ? 0.2345 0.2359 0.2352 -0.0182 0.0296  0.0294  19  LYS   A CD  
478  C  CD  B LYS   A 19  ? 0.2207 0.2237 0.2026 -0.0046 0.0322  0.0083  19  LYS   A CD  
479  C  CE  A LYS   A 19  ? 0.2573 0.2487 0.2442 -0.0281 0.0279  0.0228  19  LYS   A CE  
480  C  CE  B LYS   A 19  ? 0.2347 0.2306 0.2099 -0.0143 0.0235  0.0147  19  LYS   A CE  
481  N  NZ  A LYS   A 19  ? 0.2702 0.2594 0.2413 -0.0378 0.0357  0.0099  19  LYS   A NZ  
482  N  NZ  B LYS   A 19  ? 0.2429 0.2350 0.2116 -0.0252 0.0292  0.0091  19  LYS   A NZ  
509  N  N   A ASN   A 20  ? 0.1433 0.1573 0.2493 -0.0167 0.0429  0.0633  20  ASN   A N   
510  N  N   B ASN   A 20  ? 0.1701 0.1832 0.1951 0.0102  0.0285  0.0122  20  ASN   A N   
511  C  CA  A ASN   A 20  ? 0.1604 0.1738 0.2646 0.0059  0.0529  0.0483  20  ASN   A CA  
512  C  CA  B ASN   A 20  ? 0.1845 0.1922 0.2169 0.0185  0.0347  0.0053  20  ASN   A CA  
513  C  C   A ASN   A 20  ? 0.1808 0.1817 0.2756 -0.0033 0.0696  0.0276  20  ASN   A C   
514  C  C   B ASN   A 20  ? 0.1928 0.1937 0.2244 0.0087  0.0520  0.0040  20  ASN   A C   
515  O  O   A ASN   A 20  ? 0.2078 0.2015 0.2970 -0.0303 0.0717  0.0069  20  ASN   A O   
516  O  O   B ASN   A 20  ? 0.2067 0.2048 0.2322 -0.0068 0.0457  -0.0044 20  ASN   A O   
517  C  CB  A ASN   A 20  ? 0.1629 0.1866 0.2598 0.0193  0.0649  0.0620  20  ASN   A CB  
518  C  CB  B ASN   A 20  ? 0.1956 0.2000 0.2271 0.0300  0.0288  0.0075  20  ASN   A CB  
519  C  CG  A ASN   A 20  ? 0.1714 0.1985 0.2643 0.0375  0.0765  0.0631  20  ASN   A CG  
520  C  CG  B ASN   A 20  ? 0.2099 0.2067 0.2436 0.0404  0.0257  0.0025  20  ASN   A CG  
521  O  OD1 A ASN   A 20  ? 0.2031 0.2055 0.2785 0.0558  0.0805  0.0492  20  ASN   A OD1 
522  O  OD1 B ASN   A 20  ? 0.2309 0.2207 0.2630 0.0402  0.0177  0.0047  20  ASN   A OD1 
523  N  ND2 A ASN   A 20  ? 0.1772 0.1999 0.2776 0.0345  0.0654  0.0854  20  ASN   A ND2 
524  N  ND2 B ASN   A 20  ? 0.2101 0.1975 0.2417 0.0484  0.0200  0.0047  20  ASN   A ND2 
537  N  N   A ALA   A 21  ? 0.1850 0.1812 0.2725 0.0022  0.0562  0.0221  21  ALA   A N   
538  N  N   B ALA   A 21  ? 0.1917 0.1902 0.2238 0.0063  0.0589  0.0110  21  ALA   A N   
539  C  CA  A ALA   A 21  ? 0.1918 0.1771 0.2670 -0.0044 0.0435  0.0339  21  ALA   A CA  
540  C  CA  B ALA   A 21  ? 0.1920 0.1840 0.2237 -0.0034 0.0651  0.0291  21  ALA   A CA  
541  C  C   A ALA   A 21  ? 0.1759 0.1754 0.2409 -0.0020 0.0467  0.0324  21  ALA   A C   
542  C  C   B ALA   A 21  ? 0.1796 0.1755 0.2236 -0.0032 0.0753  0.0370  21  ALA   A C   
543  O  O   A ALA   A 21  ? 0.1787 0.1811 0.2517 0.0040  0.0424  0.0215  21  ALA   A O   
544  O  O   B ALA   A 21  ? 0.1735 0.1682 0.2499 0.0068  0.0716  0.0327  21  ALA   A O   
545  C  CB  A ALA   A 21  ? 0.2101 0.1794 0.2818 -0.0160 0.0332  0.0361  21  ALA   A CB  
546  C  CB  B ALA   A 21  ? 0.2012 0.1848 0.2270 -0.0146 0.0619  0.0305  21  ALA   A CB  
557  N  N   A ASP   A 22  ? 0.1659 0.1671 0.2147 -0.0091 0.0512  0.0462  22  ASP   A N   
558  N  N   B ASP   A 22  ? 0.1810 0.1738 0.2140 -0.0079 0.0799  0.0407  22  ASP   A N   
559  C  CA  A ASP   A 22  ? 0.1677 0.1703 0.2083 -0.0051 0.0409  0.0445  22  ASP   A CA  
560  C  CA  B ASP   A 22  ? 0.1873 0.1701 0.2096 -0.0080 0.0744  0.0424  22  ASP   A CA  
561  C  C   A ASP   A 22  ? 0.1575 0.1796 0.1697 -0.0059 0.0348  0.0287  22  ASP   A C   
562  C  C   B ASP   A 22  ? 0.1711 0.1712 0.1885 -0.0194 0.0759  0.0268  22  ASP   A C   
563  O  O   A ASP   A 22  ? 0.1593 0.1939 0.1725 -0.0121 0.0384  0.0146  22  ASP   A O   
564  O  O   B ASP   A 22  ? 0.1639 0.1781 0.1977 -0.0277 0.0646  0.0090  22  ASP   A O   
565  C  CB  A ASP   A 22  ? 0.1875 0.1693 0.2608 -0.0137 0.0377  0.0380  22  ASP   A CB  
566  C  CB  B ASP   A 22  ? 0.2118 0.1744 0.2533 0.0004  0.0608  0.0418  22  ASP   A CB  
567  C  CG  A ASP   A 22  ? 0.2051 0.1758 0.3188 -0.0160 0.0090  0.0386  22  ASP   A CG  
568  C  CG  B ASP   A 22  ? 0.2288 0.1818 0.2901 0.0044  0.0524  0.0380  22  ASP   A CG  
569  O  OD1 A ASP   A 22  ? 0.1995 0.1756 0.3347 -0.0273 -0.0070 0.0461  22  ASP   A OD1 
570  O  OD1 B ASP   A 22  ? 0.2321 0.1850 0.3008 -0.0019 0.0520  0.0328  22  ASP   A OD1 
571  O  OD2 A ASP   A 22  ? 0.2254 0.1867 0.3586 -0.0120 0.0063  0.0282  22  ASP   A OD2 
572  O  OD2 B ASP   A 22  ? 0.2401 0.1906 0.3146 0.0087  0.0530  0.0316  22  ASP   A OD2 
581  N  N   A ILE   A 23  ? 0.1580 0.1781 0.1645 0.0007  0.0349  0.0133  23  ILE   A N   
582  N  N   B ILE   A 23  ? 0.1715 0.1697 0.1835 -0.0161 0.0699  0.0124  23  ILE   A N   
583  C  CA  A ILE   A 23  ? 0.1541 0.1673 0.1647 -0.0048 0.0253  0.0121  23  ILE   A CA  
584  C  CA  B ILE   A 23  ? 0.1681 0.1723 0.1733 -0.0220 0.0521  0.0057  23  ILE   A CA  
585  C  C   A ILE   A 23  ? 0.1547 0.1766 0.1653 -0.0082 0.0402  0.0112  23  ILE   A C   
586  C  C   B ILE   A 23  ? 0.1771 0.1845 0.1758 -0.0365 0.0483  -0.0064 23  ILE   A C   
587  O  O   A ILE   A 23  ? 0.1626 0.1841 0.1777 -0.0058 0.0304  0.0027  23  ILE   A O   
588  O  O   B ILE   A 23  ? 0.1772 0.1861 0.1793 -0.0378 0.0420  -0.0147 23  ILE   A O   
589  C  CB  A ILE   A 23  ? 0.1594 0.1615 0.1592 0.0004  0.0222  0.0109  23  ILE   A CB  
590  C  CB  B ILE   A 23  ? 0.1646 0.1657 0.1596 -0.0132 0.0354  0.0073  23  ILE   A CB  
591  C  CG1 A ILE   A 23  ? 0.1650 0.1623 0.1659 0.0089  0.0207  0.0077  23  ILE   A CG1 
592  C  CG1 B ILE   A 23  ? 0.1657 0.1645 0.1430 -0.0140 0.0199  0.0029  23  ILE   A CG1 
593  C  CG2 A ILE   A 23  ? 0.1625 0.1654 0.1583 0.0068  0.0229  0.0138  23  ILE   A CG2 
594  C  CG2 B ILE   A 23  ? 0.1661 0.1620 0.1588 -0.0048 0.0311  0.0005  23  ILE   A CG2 
595  C  CD1 A ILE   A 23  ? 0.1660 0.1621 0.1786 0.0122  0.0065  0.0019  23  ILE   A CD1 
596  C  CD1 B ILE   A 23  ? 0.1614 0.1668 0.1426 -0.0143 0.0026  0.0010  23  ILE   A CD1 
619  N  N   A VAL   A 24  ? 0.1607 0.1842 0.1829 -0.0160 0.0418  0.0046  24  VAL   A N   
620  N  N   B VAL   A 24  ? 0.1889 0.1924 0.1806 -0.0492 0.0382  -0.0118 24  VAL   A N   
621  C  CA  A VAL   A 24  ? 0.1814 0.1941 0.1873 -0.0237 0.0406  0.0014  24  VAL   A CA  
622  C  CA  B VAL   A 24  ? 0.2070 0.2005 0.1913 -0.0500 0.0312  -0.0122 24  VAL   A CA  
623  C  C   A VAL   A 24  ? 0.1836 0.2135 0.1875 -0.0351 0.0342  -0.0026 24  VAL   A C   
624  C  C   B VAL   A 24  ? 0.2137 0.2112 0.2025 -0.0493 0.0333  -0.0156 24  VAL   A C   
625  O  O   A VAL   A 24  ? 0.1898 0.2182 0.1956 -0.0309 0.0364  -0.0012 24  VAL   A O   
626  O  O   B VAL   A 24  ? 0.2221 0.2137 0.2149 -0.0432 0.0363  -0.0091 24  VAL   A O   
627  C  CB  A VAL   A 24  ? 0.1914 0.1952 0.2042 -0.0181 0.0463  -0.0007 24  VAL   A CB  
628  C  CB  B VAL   A 24  ? 0.2137 0.2041 0.1978 -0.0501 0.0279  -0.0099 24  VAL   A CB  
629  C  CG1 A VAL   A 24  ? 0.2004 0.2030 0.2127 -0.0169 0.0514  -0.0149 24  VAL   A CG1 
630  C  CG1 B VAL   A 24  ? 0.2230 0.2117 0.2109 -0.0441 0.0280  -0.0091 24  VAL   A CG1 
631  C  CG2 A VAL   A 24  ? 0.2043 0.2012 0.2091 -0.0175 0.0588  0.0107  24  VAL   A CG2 
632  C  CG2 B VAL   A 24  ? 0.2124 0.1996 0.1919 -0.0593 0.0258  -0.0113 24  VAL   A CG2 
651  N  N   A GLU   A 25  ? 0.1863 0.2347 0.1903 -0.0423 0.0463  -0.0116 25  GLU   A N   
652  N  N   B GLU   A 25  ? 0.2136 0.2271 0.2065 -0.0495 0.0428  -0.0198 25  GLU   A N   
653  C  CA  A GLU   A 25  ? 0.2005 0.2612 0.2014 -0.0346 0.0520  -0.0212 25  GLU   A CA  
654  C  CA  B GLU   A 25  ? 0.2229 0.2461 0.2245 -0.0465 0.0438  -0.0185 25  GLU   A CA  
655  C  C   A GLU   A 25  ? 0.1914 0.2718 0.1737 -0.0427 0.0621  -0.0150 25  GLU   A C   
656  C  C   B GLU   A 25  ? 0.2217 0.2488 0.2158 -0.0422 0.0547  -0.0178 25  GLU   A C   
657  O  O   A GLU   A 25  ? 0.1962 0.2845 0.1825 -0.0458 0.0526  -0.0114 25  GLU   A O   
658  O  O   B GLU   A 25  ? 0.2251 0.2548 0.2154 -0.0379 0.0569  -0.0246 25  GLU   A O   
659  C  CB  A GLU   A 25  ? 0.2220 0.2839 0.2391 -0.0226 0.0494  -0.0269 25  GLU   A CB  
660  C  CB  B GLU   A 25  ? 0.2346 0.2613 0.2646 -0.0471 0.0399  -0.0175 25  GLU   A CB  
661  C  CG  A GLU   A 25  ? 0.2507 0.3061 0.2960 -0.0214 0.0304  -0.0326 25  GLU   A CG  
662  C  CG  B GLU   A 25  ? 0.2504 0.2767 0.3134 -0.0478 0.0253  -0.0188 25  GLU   A CG  
663  C  CD  A GLU   A 25  ? 0.2716 0.3257 0.3509 -0.0231 0.0160  -0.0315 25  GLU   A CD  
664  C  CD  B GLU   A 25  ? 0.2622 0.2903 0.3609 -0.0456 0.0117  -0.0195 25  GLU   A CD  
665  O  OE1 A GLU   A 25  ? 0.2817 0.3324 0.3605 -0.0188 0.0059  -0.0383 25  GLU   A OE1 
666  O  OE1 B GLU   A 25  ? 0.2663 0.2937 0.3800 -0.0470 0.0029  -0.0220 25  GLU   A OE1 
667  O  OE2 A GLU   A 25  ? 0.2787 0.3346 0.3898 -0.0246 0.0110  -0.0352 25  GLU   A OE2 
668  O  OE2 B GLU   A 25  ? 0.2664 0.2982 0.3801 -0.0407 0.0077  -0.0166 25  GLU   A OE2 
681  N  N   A GLU   A 26  ? 0.1820 0.2671 0.1687 -0.0568 0.0626  -0.0181 26  GLU   A N   
682  N  N   B GLU   A 26  ? 0.2155 0.2406 0.2091 -0.0454 0.0694  -0.0130 26  GLU   A N   
683  C  CA  A GLU   A 26  ? 0.1968 0.2698 0.1602 -0.0658 0.0597  -0.0096 26  GLU   A CA  
684  C  CA  B GLU   A 26  ? 0.2187 0.2331 0.2143 -0.0459 0.0728  -0.0027 26  GLU   A CA  
685  C  C   A GLU   A 26  ? 0.2014 0.2605 0.1517 -0.0696 0.0490  0.0025  26  GLU   A C   
686  C  C   B GLU   A 26  ? 0.2105 0.2272 0.1968 -0.0405 0.0709  0.0067  26  GLU   A C   
687  O  O   A GLU   A 26  ? 0.2094 0.2661 0.1506 -0.0823 0.0440  0.0103  26  GLU   A O   
688  O  O   B GLU   A 26  ? 0.2164 0.2286 0.1884 -0.0494 0.0726  0.0100  26  GLU   A O   
689  C  CB  A GLU   A 26  ? 0.2147 0.2825 0.1803 -0.0637 0.0538  -0.0174 26  GLU   A CB  
690  C  CB  B GLU   A 26  ? 0.2321 0.2252 0.2474 -0.0546 0.0680  -0.0098 26  GLU   A CB  
691  C  CG  A GLU   A 26  ? 0.2387 0.3053 0.2507 -0.0614 0.0392  -0.0219 26  GLU   A CG  
692  C  CG  B GLU   A 26  ? 0.2396 0.2146 0.2652 -0.0660 0.0782  -0.0244 26  GLU   A CG  
693  C  CD  A GLU   A 26  ? 0.2482 0.3262 0.2884 -0.0594 0.0461  -0.0195 26  GLU   A CD  
694  C  CD  B GLU   A 26  ? 0.2352 0.1995 0.2683 -0.0916 0.1006  -0.0309 26  GLU   A CD  
695  O  OE1 A GLU   A 26  ? 0.2542 0.3369 0.2811 -0.0575 0.0499  -0.0249 26  GLU   A OE1 
696  O  OE1 B GLU   A 26  ? 0.2345 0.1914 0.2814 -0.0998 0.1088  -0.0552 26  GLU   A OE1 
697  O  OE2 A GLU   A 26  ? 0.2530 0.3327 0.3189 -0.0613 0.0362  -0.0206 26  GLU   A OE2 
698  O  OE2 B GLU   A 26  ? 0.2319 0.2028 0.2383 -0.0813 0.1181  -0.0226 26  GLU   A OE2 
711  N  N   A ALA   A 27  ? 0.1885 0.2403 0.1537 -0.0730 0.0486  0.0065  27  ALA   A N   
712  N  N   B ALA   A 27  ? 0.1929 0.2206 0.1831 -0.0298 0.0678  0.0186  27  ALA   A N   
713  C  CA  A ALA   A 27  ? 0.1964 0.2416 0.1612 -0.0707 0.0370  0.0004  27  ALA   A CA  
714  C  CA  B ALA   A 27  ? 0.1923 0.2284 0.1747 -0.0173 0.0559  0.0200  27  ALA   A CA  
715  C  C   A ALA   A 27  ? 0.2221 0.2528 0.1729 -0.0787 0.0322  -0.0185 27  ALA   A C   
716  C  C   B ALA   A 27  ? 0.2057 0.2443 0.1814 -0.0085 0.0509  0.0107  27  ALA   A C   
717  O  O   A ALA   A 27  ? 0.2296 0.2485 0.1841 -0.0832 0.0175  -0.0103 27  ALA   A O   
718  O  O   B ALA   A 27  ? 0.2044 0.2423 0.1870 -0.0063 0.0489  0.0148  27  ALA   A O   
719  C  CB  A ALA   A 27  ? 0.1822 0.2326 0.1727 -0.0722 0.0295  -0.0015 27  ALA   A CB  
720  C  CB  B ALA   A 27  ? 0.1825 0.2215 0.1674 -0.0205 0.0545  0.0230  27  ALA   A CB  
731  N  N   A LYS   A 28  ? 0.2553 0.2785 0.1848 -0.0705 0.0324  -0.0477 28  LYS   A N   
732  N  N   B LYS   A 28  ? 0.2308 0.2635 0.1957 0.0004  0.0422  -0.0056 28  LYS   A N   
733  C  CA  A LYS   A 28  ? 0.2910 0.3075 0.2097 -0.0608 0.0443  -0.0558 28  LYS   A CA  
734  C  CA  B LYS   A 28  ? 0.2581 0.2854 0.2158 0.0096  0.0332  -0.0162 28  LYS   A CA  
735  C  C   A LYS   A 28  ? 0.3112 0.3341 0.2161 -0.0648 0.0685  -0.0413 28  LYS   A C   
736  C  C   B LYS   A 28  ? 0.2840 0.3068 0.2245 0.0059  0.0293  -0.0084 28  LYS   A C   
737  O  O   A LYS   A 28  ? 0.3166 0.3389 0.2511 -0.0592 0.0512  -0.0392 28  LYS   A O   
738  O  O   B LYS   A 28  ? 0.2905 0.3093 0.2267 0.0070  0.0177  -0.0039 28  LYS   A O   
739  C  CB  A LYS   A 28  ? 0.3056 0.3165 0.2492 -0.0424 0.0380  -0.0617 28  LYS   A CB  
740  C  CB  B LYS   A 28  ? 0.2638 0.2891 0.2413 0.0191  0.0309  -0.0260 28  LYS   A CB  
741  C  CG  A LYS   A 28  ? 0.3177 0.3237 0.2798 -0.0301 0.0404  -0.0649 28  LYS   A CG  
742  C  CG  B LYS   A 28  ? 0.2685 0.2939 0.2704 0.0207  0.0317  -0.0294 28  LYS   A CG  
743  C  CD  A LYS   A 28  ? 0.3267 0.3365 0.3299 -0.0222 0.0408  -0.0649 28  LYS   A CD  
744  C  CD  B LYS   A 28  ? 0.2755 0.3019 0.2985 0.0202  0.0313  -0.0327 28  LYS   A CD  
745  C  CE  A LYS   A 28  ? 0.3336 0.3453 0.3714 -0.0173 0.0417  -0.0675 28  LYS   A CE  
746  C  CE  B LYS   A 28  ? 0.2831 0.3085 0.3199 0.0184  0.0306  -0.0338 28  LYS   A CE  
747  N  NZ  A LYS   A 28  ? 0.3396 0.3488 0.3929 -0.0135 0.0445  -0.0671 28  LYS   A NZ  
748  N  NZ  B LYS   A 28  ? 0.2879 0.3117 0.3294 0.0176  0.0287  -0.0338 28  LYS   A NZ  
775  N  N   A LYS   A 29  ? 0.3238 0.3569 0.2142 -0.0778 0.1040  -0.0193 29  LYS   A N   
776  N  N   B LYS   A 29  ? 0.3014 0.3250 0.2400 -0.0012 0.0430  0.0002  29  LYS   A N   
777  C  CA  A LYS   A 29  ? 0.3463 0.3837 0.2373 -0.0832 0.1181  -0.0056 29  LYS   A CA  
778  C  CA  B LYS   A 29  ? 0.3230 0.3455 0.2696 -0.0077 0.0485  0.0066  29  LYS   A CA  
779  C  C   A LYS   A 29  ? 0.3536 0.3799 0.2171 -0.0936 0.1057  0.0071  29  LYS   A C   
780  C  C   B LYS   A 29  ? 0.3310 0.3462 0.2572 -0.0186 0.0418  0.0152  29  LYS   A C   
781  O  O   A LYS   A 29  ? 0.3656 0.3922 0.2305 -0.0850 0.1042  0.0038  29  LYS   A O   
782  O  O   B LYS   A 29  ? 0.3378 0.3542 0.2665 -0.0181 0.0427  0.0139  29  LYS   A O   
783  C  CB  A LYS   A 29  ? 0.3620 0.4141 0.2945 -0.0733 0.1299  -0.0020 29  LYS   A CB  
784  C  CB  B LYS   A 29  ? 0.3361 0.3638 0.3172 -0.0015 0.0560  0.0073  29  LYS   A CB  
785  C  CG  A LYS   A 29  ? 0.3799 0.4389 0.3563 -0.0630 0.1317  -0.0021 29  LYS   A CG  
786  C  CG  B LYS   A 29  ? 0.3500 0.3787 0.3640 0.0043  0.0601  0.0057  29  LYS   A CG  
787  C  CD  A LYS   A 29  ? 0.3941 0.4575 0.4161 -0.0555 0.1277  -0.0038 29  LYS   A CD  
788  C  CD  B LYS   A 29  ? 0.3604 0.3902 0.4070 0.0086  0.0613  0.0057  29  LYS   A CD  
789  C  CE  A LYS   A 29  ? 0.4036 0.4693 0.4584 -0.0507 0.1255  -0.0038 29  LYS   A CE  
790  C  CE  B LYS   A 29  ? 0.3675 0.3987 0.4383 0.0114  0.0625  0.0042  29  LYS   A CE  
791  N  NZ  A LYS   A 29  ? 0.4077 0.4759 0.4845 -0.0470 0.1225  -0.0044 29  LYS   A NZ  
792  N  NZ  B LYS   A 29  ? 0.3710 0.4030 0.4576 0.0130  0.0610  0.0044  29  LYS   A NZ  
819  N  N   A VAL   A 30  ? 0.3419 0.3606 0.1976 -0.1132 0.0991  0.0160  30  VAL   A N   
820  N  N   B VAL   A 30  ? 0.3300 0.3382 0.2442 -0.0295 0.0373  0.0187  30  VAL   A N   
821  C  CA  A VAL   A 30  ? 0.3393 0.3436 0.1865 -0.1297 0.0702  0.0302  30  VAL   A CA  
822  C  CA  B VAL   A 30  ? 0.3289 0.3297 0.2373 -0.0391 0.0215  0.0259  30  VAL   A CA  
823  C  C   A VAL   A 30  ? 0.3363 0.3247 0.1598 -0.1278 0.0510  0.0380  30  VAL   A C   
824  C  C   B VAL   A 30  ? 0.3289 0.3250 0.2239 -0.0412 0.0088  0.0229  30  VAL   A C   
825  O  O   A VAL   A 30  ? 0.3432 0.3272 0.1587 -0.1297 0.0446  0.0400  30  VAL   A O   
826  O  O   B VAL   A 30  ? 0.3303 0.3256 0.2180 -0.0420 0.0037  0.0243  30  VAL   A O   
827  C  CB  A VAL   A 30  ? 0.3364 0.3380 0.2167 -0.1396 0.0535  0.0307  30  VAL   A CB  
828  C  CB  B VAL   A 30  ? 0.3274 0.3238 0.2494 -0.0454 0.0169  0.0308  30  VAL   A CB  
829  C  CG1 A VAL   A 30  ? 0.3425 0.3384 0.2355 -0.1382 0.0406  0.0287  30  VAL   A CG1 
830  C  CG1 B VAL   A 30  ? 0.3294 0.3227 0.2584 -0.0463 0.0136  0.0312  30  VAL   A CG1 
831  C  CG2 A VAL   A 30  ? 0.3347 0.3380 0.2436 -0.1469 0.0528  0.0291  30  VAL   A CG2 
832  C  CG2 B VAL   A 30  ? 0.3267 0.3221 0.2592 -0.0477 0.0173  0.0346  30  VAL   A CG2 
851  N  N   A LYS   A 31  ? 0.3302 0.3084 0.1448 -0.1314 0.0253  0.0335  31  LYS   A N   
852  N  N   B LYS   A 31  ? 0.3274 0.3193 0.2260 -0.0421 -0.0023 0.0180  31  LYS   A N   
853  C  CA  A LYS   A 31  ? 0.3385 0.3065 0.1588 -0.1124 -0.0048 0.0326  31  LYS   A CA  
854  C  CA  B LYS   A 31  ? 0.3265 0.3176 0.2415 -0.0382 -0.0132 0.0168  31  LYS   A CA  
855  C  C   A LYS   A 31  ? 0.3123 0.2823 0.1218 -0.0910 -0.0110 0.0606  31  LYS   A C   
856  C  C   B LYS   A 31  ? 0.3031 0.3006 0.2033 -0.0312 -0.0123 0.0325  31  LYS   A C   
857  O  O   A LYS   A 31  ? 0.3244 0.2987 0.1291 -0.0866 -0.0251 0.0696  31  LYS   A O   
858  O  O   B LYS   A 31  ? 0.3083 0.3075 0.2107 -0.0263 -0.0188 0.0377  31  LYS   A O   
859  C  CB  A LYS   A 31  ? 0.3712 0.3325 0.2633 -0.0993 -0.0259 0.0059  31  LYS   A CB  
860  C  CB  B LYS   A 31  ? 0.3482 0.3348 0.3095 -0.0381 -0.0228 0.0020  31  LYS   A CB  
861  C  CG  A LYS   A 31  ? 0.4058 0.3557 0.3780 -0.0832 -0.0446 -0.0077 31  LYS   A CG  
862  C  CG  B LYS   A 31  ? 0.3697 0.3517 0.3832 -0.0354 -0.0331 -0.0075 31  LYS   A CG  
863  C  CD  A LYS   A 31  ? 0.4333 0.3722 0.4662 -0.0699 -0.0614 -0.0213 31  LYS   A CD  
864  C  CD  B LYS   A 31  ? 0.3860 0.3646 0.4427 -0.0320 -0.0432 -0.0171 31  LYS   A CD  
865  C  CE  A LYS   A 31  ? 0.4521 0.3879 0.5239 -0.0602 -0.0729 -0.0299 31  LYS   A CE  
866  C  CE  B LYS   A 31  ? 0.3976 0.3744 0.4844 -0.0297 -0.0497 -0.0225 31  LYS   A CE  
867  N  NZ  A LYS   A 31  ? 0.4618 0.3984 0.5529 -0.0553 -0.0787 -0.0343 31  LYS   A NZ  
868  N  NZ  B LYS   A 31  ? 0.4046 0.3791 0.5060 -0.0284 -0.0528 -0.0257 31  LYS   A NZ  
895  N  N   A PRO   A 32  ? 0.2858 0.2533 0.1130 -0.0956 -0.0137 0.0466  32  PRO   A N   
896  N  N   B PRO   A 32  ? 0.2729 0.2753 0.1727 -0.0304 -0.0034 0.0317  32  PRO   A N   
897  C  CA  A PRO   A 32  ? 0.2742 0.2377 0.1373 -0.0863 -0.0210 0.0542  32  PRO   A CA  
898  C  CA  B PRO   A 32  ? 0.2567 0.2599 0.1640 -0.0273 -0.0029 0.0420  32  PRO   A CA  
899  C  C   A PRO   A 32  ? 0.2677 0.2277 0.1490 -0.0712 -0.0274 0.0577  32  PRO   A C   
900  C  C   B PRO   A 32  ? 0.2441 0.2451 0.1547 -0.0230 -0.0118 0.0535  32  PRO   A C   
901  O  O   A PRO   A 32  ? 0.2653 0.2197 0.1543 -0.0738 -0.0314 0.0545  32  PRO   A O   
902  O  O   B PRO   A 32  ? 0.2396 0.2412 0.1595 -0.0201 -0.0182 0.0525  32  PRO   A O   
903  C  CB  A PRO   A 32  ? 0.2650 0.2408 0.1438 -0.0916 -0.0223 0.0424  32  PRO   A CB  
904  C  CB  B PRO   A 32  ? 0.2524 0.2621 0.1672 -0.0267 0.0023  0.0327  32  PRO   A CB  
905  C  CG  A PRO   A 32  ? 0.2645 0.2421 0.1119 -0.0872 -0.0376 0.0265  32  PRO   A CG  
906  C  CG  B PRO   A 32  ? 0.2548 0.2648 0.1615 -0.0243 -0.0025 0.0228  32  PRO   A CG  
907  C  CD  A PRO   A 32  ? 0.2696 0.2460 0.1047 -0.0900 -0.0276 0.0334  32  PRO   A CD  
908  C  CD  B PRO   A 32  ? 0.2610 0.2699 0.1599 -0.0271 -0.0014 0.0242  32  PRO   A CD  
923  N  N   A THR   A 33  ? 0.2680 0.2270 0.1487 -0.0590 -0.0296 0.0602  33  THR   A N   
924  N  N   B THR   A 33  ? 0.2395 0.2357 0.1472 -0.0244 -0.0152 0.0601  33  THR   A N   
925  C  CA  A THR   A 33  ? 0.2622 0.2312 0.1573 -0.0447 -0.0448 0.0591  33  THR   A CA  
926  C  CA  B THR   A 33  ? 0.2339 0.2268 0.1435 -0.0234 -0.0259 0.0646  33  THR   A CA  
927  C  C   A THR   A 33  ? 0.2261 0.2121 0.1502 -0.0426 -0.0408 0.0499  33  THR   A C   
928  C  C   B THR   A 33  ? 0.2144 0.2080 0.1422 -0.0331 -0.0250 0.0539  33  THR   A C   
929  O  O   A THR   A 33  ? 0.2166 0.2090 0.1555 -0.0411 -0.0490 0.0506  33  THR   A O   
930  O  O   B THR   A 33  ? 0.2108 0.2020 0.1547 -0.0355 -0.0225 0.0511  33  THR   A O   
931  C  CB  A THR   A 33  ? 0.2890 0.2555 0.1812 -0.0368 -0.0514 0.0696  33  THR   A CB  
932  C  CB  B THR   A 33  ? 0.2487 0.2388 0.1541 -0.0165 -0.0276 0.0788  33  THR   A CB  
933  O  OG1 A THR   A 33  ? 0.3090 0.2726 0.2193 -0.0290 -0.0469 0.0754  33  THR   A OG1 
934  O  OG1 B THR   A 33  ? 0.2601 0.2522 0.1759 -0.0109 -0.0283 0.0836  33  THR   A OG1 
935  C  CG2 A THR   A 33  ? 0.2951 0.2613 0.1890 -0.0291 -0.0590 0.0681  33  THR   A CG2 
936  C  CG2 B THR   A 33  ? 0.2518 0.2410 0.1612 -0.0122 -0.0288 0.0798  33  THR   A CG2 
951  N  N   . VAL   A 34  ? 0.2008 0.1974 0.1341 -0.0399 -0.0293 0.0541  34  VAL   A N   
952  C  CA  . VAL   A 34  ? 0.1760 0.1755 0.1333 -0.0366 -0.0223 0.0459  34  VAL   A CA  
953  C  C   . VAL   A 34  ? 0.1652 0.1692 0.1291 -0.0341 -0.0106 0.0332  34  VAL   A C   
954  O  O   . VAL   A 34  ? 0.1703 0.1717 0.1513 -0.0394 -0.0095 0.0423  34  VAL   A O   
955  C  CB  . VAL   A 34  ? 0.1761 0.1781 0.1565 -0.0374 -0.0135 0.0318  34  VAL   A CB  
956  C  CG1 . VAL   A 34  ? 0.1805 0.1765 0.1551 -0.0344 0.0020  0.0169  34  VAL   A CG1 
957  C  CG2 . VAL   A 34  ? 0.1878 0.1926 0.1778 -0.0313 -0.0221 0.0381  34  VAL   A CG2 
968  N  N   . VAL   A 35  ? 0.1435 0.1590 0.1368 -0.0355 -0.0134 0.0317  35  VAL   A N   
969  C  CA  . VAL   A 35  ? 0.1370 0.1539 0.1277 -0.0277 -0.0009 0.0205  35  VAL   A CA  
970  C  C   . VAL   A 35  ? 0.1359 0.1412 0.1237 -0.0218 0.0084  0.0204  35  VAL   A C   
971  O  O   . VAL   A 35  ? 0.1314 0.1525 0.1408 -0.0251 0.0117  0.0214  35  VAL   A O   
972  C  CB  . VAL   A 35  ? 0.1420 0.1561 0.1420 -0.0169 0.0102  0.0075  35  VAL   A CB  
973  C  CG1 . VAL   A 35  ? 0.1567 0.1647 0.1481 -0.0180 0.0021  0.0004  35  VAL   A CG1 
974  C  CG2 . VAL   A 35  ? 0.1390 0.1594 0.1692 -0.0059 0.0161  0.0079  35  VAL   A CG2 
984  N  N   . VAL   A 36  ? 0.1206 0.1361 0.1172 -0.0229 0.0051  0.0246  36  VAL   A N   
985  C  CA  . VAL   A 36  ? 0.1162 0.1218 0.1250 -0.0131 -0.0010 0.0202  36  VAL   A CA  
986  C  C   . VAL   A 36  ? 0.1167 0.1291 0.1355 -0.0118 0.0036  0.0174  36  VAL   A C   
987  O  O   . VAL   A 36  ? 0.1234 0.1252 0.1557 -0.0080 0.0142  0.0181  36  VAL   A O   
988  C  CB  . VAL   A 36  ? 0.1189 0.1182 0.1390 -0.0124 0.0047  0.0216  36  VAL   A CB  
989  C  CG1 . VAL   A 36  ? 0.1278 0.1185 0.1493 -0.0230 0.0119  0.0033  36  VAL   A CG1 
990  C  CG2 . VAL   A 36  ? 0.1348 0.1217 0.1649 -0.0119 -0.0045 0.0223  36  VAL   A CG2 
1000 N  N   . ASN   A 37  ? 0.1157 0.1172 0.1294 -0.0112 0.0052  0.0201  37  ASN   A N   
1001 C  CA  . ASN   A 37  ? 0.1143 0.1107 0.1260 -0.0048 -0.0010 0.0184  37  ASN   A CA  
1002 C  C   . ASN   A 37  ? 0.1086 0.1123 0.1256 -0.0066 0.0111  0.0259  37  ASN   A C   
1003 O  O   . ASN   A 37  ? 0.1227 0.1247 0.1218 0.0006  0.0101  0.0113  37  ASN   A O   
1004 C  CB  . ASN   A 37  ? 0.1178 0.1160 0.1247 -0.0061 -0.0007 0.0225  37  ASN   A CB  
1005 C  CG  . ASN   A 37  ? 0.1168 0.1147 0.1358 -0.0036 0.0008  0.0136  37  ASN   A CG  
1006 O  OD1 . ASN   A 37  ? 0.1147 0.1185 0.1582 0.0003  0.0004  0.0140  37  ASN   A OD1 
1007 N  ND2 . ASN   A 37  ? 0.1244 0.1154 0.1383 -0.0041 0.0006  0.0244  37  ASN   A ND2 
1014 N  N   . ALA   A 38  ? 0.1120 0.1205 0.1314 -0.0048 0.0143  0.0144  38  ALA   A N   
1015 C  CA  . ALA   A 38  ? 0.1229 0.1241 0.1290 -0.0070 0.0023  0.0066  38  ALA   A CA  
1016 C  C   . ALA   A 38  ? 0.1209 0.1259 0.1332 -0.0010 -0.0070 0.0087  38  ALA   A C   
1017 O  O   . ALA   A 38  ? 0.1239 0.1191 0.1415 0.0014  -0.0083 0.0094  38  ALA   A O   
1018 C  CB  . ALA   A 38  ? 0.1301 0.1589 0.1525 -0.0134 -0.0114 0.0056  38  ALA   A CB  
1024 N  N   A ALA   A 39  ? 0.1123 0.1169 0.1436 0.0028  0.0039  0.0136  39  ALA   A N   
1025 N  N   B ALA   A 39  ? 0.1222 0.1222 0.1348 -0.0006 -0.0016 0.0138  39  ALA   A N   
1026 C  CA  A ALA   A 39  ? 0.1206 0.1155 0.1393 0.0037  0.0065  0.0020  39  ALA   A CA  
1027 C  CA  B ALA   A 39  ? 0.1319 0.1271 0.1349 -0.0032 0.0025  0.0157  39  ALA   A CA  
1028 C  C   A ALA   A 39  ? 0.1203 0.1157 0.1456 0.0079  0.0017  -0.0003 39  ALA   A C   
1029 C  C   B ALA   A 39  ? 0.1238 0.1144 0.1282 -0.0089 0.0051  0.0189  39  ALA   A C   
1030 O  O   A ALA   A 39  ? 0.1276 0.1218 0.1339 0.0089  -0.0028 0.0053  39  ALA   A O   
1031 O  O   B ALA   A 39  ? 0.1217 0.1130 0.1291 -0.0182 0.0032  0.0245  39  ALA   A O   
1032 C  CB  A ALA   A 39  ? 0.1129 0.1216 0.1401 -0.0045 -0.0061 0.0001  39  ALA   A CB  
1033 C  CB  B ALA   A 39  ? 0.1397 0.1416 0.1486 -0.0002 -0.0034 0.0103  39  ALA   A CB  
1044 N  N   A ASN   A 40  ? 0.1239 0.1244 0.1491 -0.0020 0.0193  -0.0007 40  ASN   A N   
1045 N  N   B ASN   A 40  ? 0.1253 0.1103 0.1149 -0.0102 0.0193  0.0194  40  ASN   A N   
1046 C  CA  A ASN   A 40  ? 0.1220 0.1218 0.1477 0.0023  0.0076  -0.0029 40  ASN   A CA  
1047 C  CA  B ASN   A 40  ? 0.1293 0.1090 0.1291 -0.0015 0.0112  0.0165  40  ASN   A CA  
1048 C  C   A ASN   A 40  ? 0.1177 0.1135 0.1282 -0.0035 0.0155  0.0081  40  ASN   A C   
1049 C  C   B ASN   A 40  ? 0.1266 0.1038 0.1269 -0.0074 0.0160  0.0231  40  ASN   A C   
1050 O  O   A ASN   A 40  ? 0.1155 0.1255 0.1266 -0.0034 0.0062  0.0152  40  ASN   A O   
1051 O  O   B ASN   A 40  ? 0.1222 0.1077 0.1367 -0.0175 0.0172  0.0226  40  ASN   A O   
1052 C  CB  A ASN   A 40  ? 0.1377 0.1333 0.1562 0.0028  -0.0046 0.0010  40  ASN   A CB  
1053 C  CB  B ASN   A 40  ? 0.1405 0.1147 0.1449 0.0012  0.0119  0.0207  40  ASN   A CB  
1054 C  CG  A ASN   A 40  ? 0.1499 0.1357 0.1732 0.0051  -0.0112 0.0033  40  ASN   A CG  
1055 C  CG  B ASN   A 40  ? 0.1472 0.1250 0.1700 0.0021  0.0163  0.0204  40  ASN   A CG  
1056 O  OD1 A ASN   A 40  ? 0.1570 0.1302 0.1988 0.0071  -0.0198 -0.0006 40  ASN   A OD1 
1057 O  OD1 B ASN   A 40  ? 0.1518 0.1266 0.1776 -0.0033 0.0253  0.0247  40  ASN   A OD1 
1058 N  ND2 A ASN   A 40  ? 0.1587 0.1457 0.1666 0.0057  -0.0123 -0.0154 40  ASN   A ND2 
1059 N  ND2 B ASN   A 40  ? 0.1522 0.1388 0.1792 0.0061  0.0162  0.0057  40  ASN   A ND2 
1072 N  N   A VAL   A 41  ? 0.1191 0.1153 0.1341 0.0026  0.0181  0.0166  41  VAL   A N   
1073 N  N   B VAL   A 41  ? 0.1321 0.1126 0.1211 -0.0034 0.0127  0.0290  41  VAL   A N   
1074 C  CA  A VAL   A 41  ? 0.1236 0.1206 0.1497 0.0051  0.0130  0.0126  41  VAL   A CA  
1075 C  CA  B VAL   A 41  ? 0.1353 0.1183 0.1354 0.0013  0.0204  0.0238  41  VAL   A CA  
1076 C  C   A VAL   A 41  ? 0.1255 0.1163 0.1506 0.0094  0.0141  0.0146  41  VAL   A C   
1077 C  C   B VAL   A 41  ? 0.1396 0.1206 0.1356 -0.0101 0.0239  0.0198  41  VAL   A C   
1078 O  O   A VAL   A 41  ? 0.1280 0.1097 0.1584 0.0072  0.0020  0.0050  41  VAL   A O   
1079 O  O   B VAL   A 41  ? 0.1452 0.1210 0.1391 -0.0152 0.0116  0.0108  41  VAL   A O   
1080 C  CB  A VAL   A 41  ? 0.1227 0.1250 0.1432 0.0032  0.0156  0.0111  41  VAL   A CB  
1081 C  CB  B VAL   A 41  ? 0.1390 0.1296 0.1427 0.0098  0.0303  0.0232  41  VAL   A CB  
1082 C  CG1 A VAL   A 41  ? 0.1417 0.1337 0.1634 0.0036  0.0063  0.0061  41  VAL   A CG1 
1083 C  CG1 B VAL   A 41  ? 0.1536 0.1359 0.1513 0.0140  0.0406  0.0148  41  VAL   A CG1 
1084 C  CG2 A VAL   A 41  ? 0.1264 0.1313 0.1342 -0.0041 0.0259  0.0003  41  VAL   A CG2 
1085 C  CG2 B VAL   A 41  ? 0.1379 0.1391 0.1498 0.0066  0.0206  0.0235  41  VAL   A CG2 
1104 N  N   A TYR   A 42  ? 0.1248 0.1133 0.1631 -0.0016 0.0234  0.0256  42  TYR   A N   
1105 N  N   B TYR   A 42  ? 0.1358 0.1165 0.1446 -0.0076 0.0288  0.0231  42  TYR   A N   
1106 C  CA  A TYR   A 42  ? 0.1318 0.1092 0.1667 -0.0039 0.0237  0.0285  42  TYR   A CA  
1107 C  CA  B TYR   A 42  ? 0.1393 0.1165 0.1506 -0.0076 0.0298  0.0234  42  TYR   A CA  
1108 C  C   A TYR   A 42  ? 0.1211 0.1103 0.1696 -0.0020 0.0176  0.0240  42  TYR   A C   
1109 C  C   B TYR   A 42  ? 0.1344 0.1118 0.1475 -0.0088 0.0244  0.0267  42  TYR   A C   
1110 O  O   A TYR   A 42  ? 0.1177 0.1183 0.1894 -0.0029 0.0107  0.0026  42  TYR   A O   
1111 O  O   B TYR   A 42  ? 0.1349 0.1124 0.1546 -0.0177 0.0303  0.0309  42  TYR   A O   
1112 C  CB  A TYR   A 42  ? 0.1566 0.1219 0.1645 -0.0044 0.0290  0.0342  42  TYR   A CB  
1113 C  CB  B TYR   A 42  ? 0.1537 0.1260 0.1559 -0.0058 0.0220  0.0269  42  TYR   A CB  
1114 C  CG  A TYR   A 42  ? 0.1689 0.1355 0.1618 -0.0010 0.0244  0.0380  42  TYR   A CG  
1115 C  CG  B TYR   A 42  ? 0.1624 0.1356 0.1545 -0.0012 0.0099  0.0289  42  TYR   A CG  
1116 C  CD1 A TYR   A 42  ? 0.1775 0.1502 0.1743 -0.0074 0.0307  0.0240  42  TYR   A CD1 
1117 C  CD1 B TYR   A 42  ? 0.1638 0.1398 0.1558 -0.0024 0.0078  0.0301  42  TYR   A CD1 
1118 C  CD2 A TYR   A 42  ? 0.1763 0.1547 0.1700 0.0009  0.0157  0.0340  42  TYR   A CD2 
1119 C  CD2 B TYR   A 42  ? 0.1705 0.1505 0.1619 0.0049  0.0089  0.0198  42  TYR   A CD2 
1120 C  CE1 A TYR   A 42  ? 0.1819 0.1555 0.1719 -0.0088 0.0314  0.0190  42  TYR   A CE1 
1121 C  CE1 B TYR   A 42  ? 0.1656 0.1436 0.1567 -0.0026 0.0084  0.0259  42  TYR   A CE1 
1122 C  CE2 A TYR   A 42  ? 0.1794 0.1635 0.1845 -0.0065 0.0128  0.0284  42  TYR   A CE2 
1123 C  CE2 B TYR   A 42  ? 0.1752 0.1591 0.1654 0.0028  0.0130  0.0180  42  TYR   A CE2 
1124 C  CZ  A TYR   A 42  ? 0.1859 0.1645 0.1683 -0.0125 0.0291  0.0255  42  TYR   A CZ  
1125 C  CZ  B TYR   A 42  ? 0.1725 0.1573 0.1595 -0.0035 0.0197  0.0161  42  TYR   A CZ  
1126 O  OH  A TYR   A 42  ? 0.1903 0.1796 0.1807 -0.0129 0.0209  0.0212  42  TYR   A OH  
1127 O  OH  B TYR   A 42  ? 0.1740 0.1722 0.1753 -0.0104 0.0213  0.0100  42  TYR   A OH  
1146 N  N   . LEU   A 43  ? 0.1269 0.1120 0.1472 -0.0039 0.0179  0.0124  43  LEU   A N   
1147 C  CA  . LEU   A 43  ? 0.1227 0.1149 0.1426 -0.0084 0.0106  0.0071  43  LEU   A CA  
1148 C  C   . LEU   A 43  ? 0.1209 0.1156 0.1488 -0.0044 0.0066  0.0058  43  LEU   A C   
1149 O  O   . LEU   A 43  ? 0.1332 0.1220 0.1771 -0.0021 -0.0050 0.0011  43  LEU   A O   
1150 C  CB  . LEU   A 43  ? 0.1241 0.1150 0.1530 -0.0110 0.0036  0.0063  43  LEU   A CB  
1151 C  CG  . LEU   A 43  ? 0.1310 0.1133 0.1687 -0.0044 0.0053  0.0113  43  LEU   A CG  
1152 C  CD1 . LEU   A 43  ? 0.1373 0.1197 0.1879 -0.0058 -0.0041 0.0146  43  LEU   A CD1 
1153 C  CD2 . LEU   A 43  ? 0.1434 0.1171 0.1714 -0.0047 0.0077  0.0216  43  LEU   A CD2 
1166 N  N   A LYS   A 44  ? 0.1311 0.1141 0.1429 -0.0054 0.0077  0.0147  44  LYS   A N   
1167 N  N   B LYS   A 44  ? 0.1319 0.1211 0.1501 -0.0031 0.0034  0.0083  44  LYS   A N   
1168 C  CA  A LYS   A 44  ? 0.1419 0.1161 0.1353 -0.0047 0.0177  0.0217  44  LYS   A CA  
1169 C  CA  B LYS   A 44  ? 0.1428 0.1286 0.1547 -0.0022 0.0049  0.0098  44  LYS   A CA  
1170 C  C   A LYS   A 44  ? 0.1284 0.1229 0.1288 0.0055  0.0007  0.0107  44  LYS   A C   
1171 C  C   B LYS   A 44  ? 0.1303 0.1271 0.1396 0.0031  -0.0016 0.0079  44  LYS   A C   
1172 O  O   A LYS   A 44  ? 0.1346 0.1413 0.1524 0.0006  -0.0010 0.0013  44  LYS   A O   
1173 O  O   B LYS   A 44  ? 0.1352 0.1392 0.1476 -0.0005 -0.0018 0.0017  44  LYS   A O   
1174 C  CB  A LYS   A 44  ? 0.1773 0.1351 0.1777 -0.0023 0.0316  0.0278  44  LYS   A CB  
1175 C  CB  B LYS   A 44  ? 0.1709 0.1482 0.1968 -0.0017 0.0085  0.0092  44  LYS   A CB  
1176 C  CG  A LYS   A 44  ? 0.2064 0.1654 0.2464 -0.0110 0.0549  0.0393  44  LYS   A CG  
1177 C  CG  B LYS   A 44  ? 0.1944 0.1739 0.2535 -0.0054 0.0186  0.0162  44  LYS   A CG  
1178 C  CD  A LYS   A 44  ? 0.2430 0.2141 0.3403 -0.0134 0.0407  0.0273  44  LYS   A CD  
1179 C  CD  B LYS   A 44  ? 0.2193 0.2065 0.3167 -0.0112 0.0114  0.0164  44  LYS   A CD  
1180 C  CE  A LYS   A 44  ? 0.2625 0.2445 0.3988 -0.0146 0.0349  0.0188  44  LYS   A CE  
1181 C  CE  B LYS   A 44  ? 0.2332 0.2314 0.3570 -0.0158 0.0046  0.0165  44  LYS   A CE  
1182 N  NZ  A LYS   A 44  ? 0.2690 0.2633 0.4261 -0.0171 0.0389  0.0169  44  LYS   A NZ  
1183 N  NZ  B LYS   A 44  ? 0.2428 0.2505 0.3818 -0.0216 0.0063  0.0191  44  LYS   A NZ  
1210 N  N   . HIS   A 45  ? 0.1174 0.1185 0.1422 0.0031  0.0025  0.0160  45  HIS   A N   
1211 C  CA  . HIS   A 45  ? 0.1178 0.1173 0.1435 0.0014  -0.0067 0.0146  45  HIS   A CA  
1212 C  C   . HIS   A 45  ? 0.1251 0.1316 0.1523 0.0053  -0.0084 0.0115  45  HIS   A C   
1213 O  O   . HIS   A 45  ? 0.1466 0.1533 0.1845 0.0284  -0.0128 -0.0051 45  HIS   A O   
1214 C  CB  . HIS   A 45  ? 0.1220 0.1186 0.1426 0.0009  -0.0023 0.0065  45  HIS   A CB  
1215 C  CG  . HIS   A 45  ? 0.1127 0.1177 0.1308 -0.0049 0.0068  0.0084  45  HIS   A CG  
1216 N  ND1 . HIS   A 45  ? 0.1072 0.1251 0.1522 -0.0052 -0.0012 0.0190  45  HIS   A ND1 
1217 C  CD2 . HIS   A 45  ? 0.1187 0.1205 0.1352 -0.0067 -0.0071 0.0170  45  HIS   A CD2 
1218 C  CE1 . HIS   A 45  ? 0.1125 0.1306 0.1432 -0.0083 -0.0054 0.0207  45  HIS   A CE1 
1219 N  NE2 . HIS   A 45  ? 0.1184 0.1272 0.1384 -0.0018 -0.0000 0.0241  45  HIS   A NE2 
1228 N  N   A GLY   A 46  ? 0.1398 0.1340 0.1712 0.0083  -0.0158 0.0108  46  GLY   A N   
1229 N  N   B GLY   A 46  ? 0.1285 0.1377 0.1627 0.0147  -0.0168 0.0202  46  GLY   A N   
1230 C  CA  A GLY   A 46  ? 0.1419 0.1376 0.1797 0.0091  -0.0121 0.0169  46  GLY   A CA  
1231 C  CA  B GLY   A 46  ? 0.1311 0.1353 0.1701 0.0171  -0.0253 0.0333  46  GLY   A CA  
1232 C  C   A GLY   A 46  ? 0.1424 0.1332 0.1840 0.0141  -0.0146 0.0242  46  GLY   A C   
1233 C  C   B GLY   A 46  ? 0.1355 0.1257 0.1728 0.0142  -0.0345 0.0372  46  GLY   A C   
1234 O  O   A GLY   A 46  ? 0.1447 0.1403 0.2097 0.0028  -0.0212 0.0122  46  GLY   A O   
1235 O  O   B GLY   A 46  ? 0.1371 0.1116 0.1934 0.0130  -0.0309 0.0583  46  GLY   A O   
1242 N  N   A GLY   A 47  ? 0.1464 0.1380 0.1755 0.0163  -0.0157 0.0087  47  GLY   A N   
1243 N  N   B GLY   A 47  ? 0.1333 0.1284 0.1603 0.0124  -0.0518 0.0167  47  GLY   A N   
1244 C  CA  A GLY   A 47  ? 0.1426 0.1438 0.1684 0.0181  -0.0321 -0.0042 47  GLY   A CA  
1245 C  CA  B GLY   A 47  ? 0.1396 0.1321 0.1690 0.0093  -0.0598 -0.0007 47  GLY   A CA  
1246 C  C   A GLY   A 47  ? 0.1338 0.1323 0.1769 0.0139  -0.0401 -0.0057 47  GLY   A C   
1247 C  C   B GLY   A 47  ? 0.1389 0.1356 0.1706 0.0069  -0.0577 -0.0087 47  GLY   A C   
1248 O  O   A GLY   A 47  ? 0.1261 0.1275 0.1796 0.0179  -0.0396 0.0157  47  GLY   A O   
1249 O  O   B GLY   A 47  ? 0.1396 0.1363 0.1906 0.0080  -0.0513 0.0065  47  GLY   A O   
1256 N  N   A GLY   A 48  ? 0.1270 0.1332 0.1875 0.0140  -0.0548 -0.0072 48  GLY   A N   
1257 N  N   B GLY   A 48  ? 0.1376 0.1440 0.1731 0.0055  -0.0576 -0.0208 48  GLY   A N   
1258 C  CA  A GLY   A 48  ? 0.1239 0.1208 0.1943 0.0083  -0.0446 -0.0111 48  GLY   A CA  
1259 C  CA  B GLY   A 48  ? 0.1298 0.1468 0.1801 -0.0010 -0.0393 -0.0202 48  GLY   A CA  
1260 C  C   A GLY   A 48  ? 0.1206 0.1185 0.1752 0.0014  -0.0150 -0.0106 48  GLY   A C   
1261 C  C   B GLY   A 48  ? 0.1250 0.1476 0.1730 0.0066  -0.0109 -0.0070 48  GLY   A C   
1262 O  O   A GLY   A 48  ? 0.1375 0.1176 0.1880 0.0096  -0.0240 -0.0117 48  GLY   A O   
1263 O  O   B GLY   A 48  ? 0.1335 0.1541 0.1865 0.0069  -0.0107 -0.0029 48  GLY   A O   
1270 N  N   A VAL   A 49  ? 0.1090 0.1155 0.1706 -0.0077 -0.0113 -0.0062 49  VAL   A N   
1271 N  N   B VAL   A 49  ? 0.1260 0.1419 0.1679 0.0028  -0.0052 -0.0017 49  VAL   A N   
1272 C  CA  A VAL   A 49  ? 0.1236 0.1165 0.1621 -0.0086 0.0142  -0.0036 49  VAL   A CA  
1273 C  CA  B VAL   A 49  ? 0.1227 0.1388 0.1559 0.0008  0.0017  0.0052  49  VAL   A CA  
1274 C  C   A VAL   A 49  ? 0.1237 0.1052 0.1503 -0.0058 0.0044  0.0046  49  VAL   A C   
1275 C  C   B VAL   A 49  ? 0.1189 0.1248 0.1251 0.0058  -0.0001 0.0030  49  VAL   A C   
1276 O  O   A VAL   A 49  ? 0.1319 0.1145 0.1685 -0.0127 0.0127  0.0034  49  VAL   A O   
1277 O  O   B VAL   A 49  ? 0.1221 0.1255 0.1166 0.0158  0.0099  -0.0010 49  VAL   A O   
1278 C  CB  A VAL   A 49  ? 0.1347 0.1201 0.1669 -0.0099 0.0192  -0.0086 49  VAL   A CB  
1279 C  CB  B VAL   A 49  ? 0.1197 0.1341 0.1564 -0.0017 0.0109  0.0107  49  VAL   A CB  
1280 C  CG1 A VAL   A 49  ? 0.1424 0.1131 0.1945 -0.0014 0.0226  -0.0066 49  VAL   A CG1 
1281 C  CG1 B VAL   A 49  ? 0.1106 0.1279 0.1551 0.0105  0.0139  0.0134  49  VAL   A CG1 
1282 C  CG2 A VAL   A 49  ? 0.1407 0.1321 0.2028 -0.0247 0.0259  -0.0176 49  VAL   A CG2 
1283 C  CG2 B VAL   A 49  ? 0.1301 0.1413 0.1698 0.0065  0.0226  0.0138  49  VAL   A CG2 
1302 N  N   A ALA   A 50  ? 0.1167 0.1059 0.1388 -0.0048 -0.0139 0.0066  50  ALA   A N   
1303 N  N   B ALA   A 50  ? 0.1157 0.1172 0.1101 0.0086  -0.0080 0.0020  50  ALA   A N   
1304 C  CA  A ALA   A 50  ? 0.1109 0.1110 0.1388 -0.0111 -0.0099 0.0103  50  ALA   A CA  
1305 C  CA  B ALA   A 50  ? 0.1098 0.1145 0.1122 0.0009  -0.0093 0.0051  50  ALA   A CA  
1306 C  C   A ALA   A 50  ? 0.1082 0.1156 0.1384 -0.0138 -0.0049 0.0116  50  ALA   A C   
1307 C  C   B ALA   A 50  ? 0.1098 0.1156 0.1167 -0.0050 0.0061  -0.0049 50  ALA   A C   
1308 O  O   A ALA   A 50  ? 0.1170 0.1190 0.1533 0.0017  -0.0146 0.0052  50  ALA   A O   
1309 O  O   B ALA   A 50  ? 0.1122 0.1186 0.1259 -0.0006 0.0125  -0.0110 50  ALA   A O   
1310 C  CB  A ALA   A 50  ? 0.1036 0.1122 0.1425 -0.0131 -0.0032 -0.0059 50  ALA   A CB  
1311 C  CB  B ALA   A 50  ? 0.1113 0.1079 0.1140 0.0070  -0.0098 0.0028  50  ALA   A CB  
1322 N  N   A GLY   A 51  ? 0.1105 0.1116 0.1516 -0.0004 -0.0064 0.0154  51  GLY   A N   
1323 N  N   B GLY   A 51  ? 0.1167 0.1145 0.1269 0.0038  -0.0070 -0.0137 51  GLY   A N   
1324 C  CA  A GLY   A 51  ? 0.1240 0.1053 0.1663 -0.0010 -0.0130 0.0130  51  GLY   A CA  
1325 C  CA  B GLY   A 51  ? 0.1118 0.1099 0.1266 0.0054  -0.0168 -0.0078 51  GLY   A CA  
1326 C  C   A GLY   A 51  ? 0.1180 0.1129 0.1608 0.0012  -0.0013 -0.0033 51  GLY   A C   
1327 C  C   B GLY   A 51  ? 0.1111 0.1122 0.1257 0.0096  -0.0057 -0.0027 51  GLY   A C   
1328 O  O   A GLY   A 51  ? 0.1214 0.1252 0.1745 -0.0007 -0.0098 -0.0108 51  GLY   A O   
1329 O  O   B GLY   A 51  ? 0.1124 0.1187 0.1379 0.0053  -0.0070 -0.0030 51  GLY   A O   
1336 N  N   A ALA   A 52  ? 0.1156 0.1281 0.1550 -0.0050 0.0018  -0.0095 52  ALA   A N   
1337 N  N   B ALA   A 52  ? 0.1161 0.1189 0.1287 0.0079  -0.0003 -0.0077 52  ALA   A N   
1338 C  CA  A ALA   A 52  ? 0.1158 0.1337 0.1621 -0.0113 0.0062  -0.0074 52  ALA   A CA  
1339 C  CA  B ALA   A 52  ? 0.1100 0.1234 0.1415 0.0029  -0.0002 -0.0081 52  ALA   A CA  
1340 C  C   A ALA   A 52  ? 0.1160 0.1290 0.1504 -0.0163 0.0115  -0.0056 52  ALA   A C   
1341 C  C   B ALA   A 52  ? 0.1109 0.1215 0.1330 0.0027  -0.0018 -0.0127 52  ALA   A C   
1342 O  O   A ALA   A 52  ? 0.1273 0.1359 0.1706 -0.0097 0.0085  -0.0133 52  ALA   A O   
1343 O  O   B ALA   A 52  ? 0.1168 0.1301 0.1445 0.0045  -0.0070 -0.0180 52  ALA   A O   
1344 C  CB  A ALA   A 52  ? 0.1342 0.1638 0.1944 -0.0152 -0.0006 -0.0034 52  ALA   A CB  
1345 C  CB  B ALA   A 52  ? 0.1185 0.1363 0.1543 -0.0054 0.0023  0.0065  52  ALA   A CB  
1356 N  N   A LEU   A 53  ? 0.1136 0.1290 0.1431 -0.0111 0.0076  0.0004  53  LEU   A N   
1357 N  N   B LEU   A 53  ? 0.1112 0.1191 0.1291 0.0031  -0.0019 -0.0125 53  LEU   A N   
1358 C  CA  A LEU   A 53  ? 0.1283 0.1326 0.1337 -0.0123 0.0113  0.0058  53  LEU   A CA  
1359 C  CA  B LEU   A 53  ? 0.1215 0.1268 0.1269 0.0009  0.0052  -0.0065 53  LEU   A CA  
1360 C  C   A LEU   A 53  ? 0.1248 0.1331 0.1221 -0.0082 0.0018  0.0068  53  LEU   A C   
1361 C  C   B LEU   A 53  ? 0.1190 0.1319 0.1092 0.0115  0.0061  0.0021  53  LEU   A C   
1362 O  O   A LEU   A 53  ? 0.1309 0.1346 0.1377 -0.0146 -0.0046 0.0030  53  LEU   A O   
1363 O  O   B LEU   A 53  ? 0.1263 0.1339 0.1046 0.0155  0.0014  0.0044  53  LEU   A O   
1364 C  CB  A LEU   A 53  ? 0.1425 0.1321 0.1374 -0.0139 0.0071  0.0086  53  LEU   A CB  
1365 C  CB  B LEU   A 53  ? 0.1296 0.1317 0.1362 -0.0092 0.0008  -0.0045 53  LEU   A CB  
1366 C  CG  A LEU   A 53  ? 0.1603 0.1326 0.1457 -0.0200 -0.0008 0.0180  53  LEU   A CG  
1367 C  CG  B LEU   A 53  ? 0.1349 0.1339 0.1392 -0.0183 -0.0023 -0.0019 53  LEU   A CG  
1368 C  CD1 A LEU   A 53  ? 0.1616 0.1368 0.1421 -0.0104 -0.0050 0.0165  53  LEU   A CD1 
1369 C  CD1 B LEU   A 53  ? 0.1319 0.1349 0.1380 -0.0226 -0.0050 -0.0055 53  LEU   A CD1 
1370 C  CD2 A LEU   A 53  ? 0.1867 0.1487 0.1698 -0.0336 0.0060  0.0204  53  LEU   A CD2 
1371 C  CD2 B LEU   A 53  ? 0.1497 0.1418 0.1569 -0.0302 0.0038  -0.0021 53  LEU   A CD2 
1394 N  N   A ASN   A 54  ? 0.1149 0.1287 0.1315 -0.0159 -0.0071 0.0074  54  ASN   A N   
1395 N  N   B ASN   A 54  ? 0.1135 0.1341 0.1163 0.0130  0.0011  0.0025  54  ASN   A N   
1396 C  CA  A ASN   A 54  ? 0.1077 0.1195 0.1423 -0.0138 -0.0094 0.0051  54  ASN   A CA  
1397 C  CA  B ASN   A 54  ? 0.1067 0.1321 0.1254 0.0151  0.0020  0.0024  54  ASN   A CA  
1398 C  C   A ASN   A 54  ? 0.1180 0.1242 0.1433 -0.0164 -0.0028 -0.0029 54  ASN   A C   
1399 C  C   B ASN   A 54  ? 0.1171 0.1301 0.1374 0.0016  -0.0007 -0.0039 54  ASN   A C   
1400 O  O   A ASN   A 54  ? 0.1227 0.1362 0.1404 -0.0153 -0.0017 -0.0105 54  ASN   A O   
1401 O  O   B ASN   A 54  ? 0.1232 0.1309 0.1481 -0.0018 -0.0014 -0.0093 54  ASN   A O   
1402 C  CB  A ASN   A 54  ? 0.1107 0.1147 0.1477 -0.0235 -0.0165 0.0057  54  ASN   A CB  
1403 C  CB  B ASN   A 54  ? 0.1091 0.1335 0.1214 0.0252  0.0011  0.0036  54  ASN   A CB  
1404 C  CG  A ASN   A 54  ? 0.1157 0.1147 0.1544 -0.0115 -0.0104 0.0069  54  ASN   A CG  
1405 C  CG  B ASN   A 54  ? 0.1068 0.1331 0.1215 0.0332  0.0057  -0.0038 54  ASN   A CG  
1406 O  OD1 A ASN   A 54  ? 0.1150 0.1105 0.1564 -0.0189 -0.0148 0.0177  54  ASN   A OD1 
1407 O  OD1 B ASN   A 54  ? 0.1051 0.1312 0.1190 0.0267  -0.0014 -0.0166 54  ASN   A OD1 
1408 N  ND2 A ASN   A 54  ? 0.1152 0.1243 0.1644 -0.0153 -0.0186 0.0157  54  ASN   A ND2 
1409 N  ND2 B ASN   A 54  ? 0.1098 0.1373 0.1346 0.0322  0.0023  0.0057  54  ASN   A ND2 
1422 N  N   . LYS   A 55  ? 0.1198 0.1302 0.1428 -0.0066 -0.0030 -0.0070 55  LYS   A N   
1423 C  CA  . LYS   A 55  ? 0.1261 0.1400 0.1511 0.0025  -0.0109 -0.0172 55  LYS   A CA  
1424 C  C   . LYS   A 55  ? 0.1242 0.1423 0.1514 -0.0022 -0.0036 -0.0211 55  LYS   A C   
1425 O  O   . LYS   A 55  ? 0.1354 0.1524 0.1631 0.0020  -0.0036 -0.0283 55  LYS   A O   
1426 C  CB  . LYS   A 55  ? 0.1323 0.1478 0.1629 0.0090  -0.0058 -0.0195 55  LYS   A CB  
1427 C  CG  . LYS   A 55  ? 0.1488 0.1748 0.1891 0.0231  -0.0176 -0.0264 55  LYS   A CG  
1428 C  CD  . LYS   A 55  ? 0.1602 0.2130 0.2035 0.0366  -0.0084 -0.0274 55  LYS   A CD  
1429 C  CE  . LYS   A 55  ? 0.1830 0.2497 0.2364 0.0515  -0.0181 -0.0295 55  LYS   A CE  
1430 N  NZ  . LYS   A 55  ? 0.1899 0.2590 0.2531 0.0610  -0.0183 -0.0343 55  LYS   A NZ  
1445 N  N   . ALA   A 56  ? 0.1354 0.1497 0.1554 -0.0094 0.0009  -0.0190 56  ALA   A N   
1446 C  CA  . ALA   A 56  ? 0.1499 0.1689 0.1578 -0.0136 0.0075  -0.0226 56  ALA   A CA  
1447 C  C   . ALA   A 56  ? 0.1460 0.1789 0.1359 -0.0097 0.0124  -0.0238 56  ALA   A C   
1448 O  O   . ALA   A 56  ? 0.1490 0.2097 0.1468 -0.0023 0.0134  -0.0144 56  ALA   A O   
1449 C  CB  . ALA   A 56  ? 0.1564 0.1849 0.1623 -0.0204 0.0112  -0.0075 56  ALA   A CB  
1455 N  N   . THR   A 57  ? 0.1300 0.1574 0.1374 -0.0036 0.0081  -0.0191 57  THR   A N   
1456 C  CA  . THR   A 57  ? 0.1371 0.1543 0.1295 -0.0083 0.0007  -0.0141 57  THR   A CA  
1457 C  C   . THR   A 57  ? 0.1388 0.1680 0.1358 -0.0029 -0.0050 -0.0155 57  THR   A C   
1458 O  O   . THR   A 57  ? 0.1354 0.1713 0.1577 -0.0078 -0.0151 -0.0237 57  THR   A O   
1459 C  CB  . THR   A 57  ? 0.1346 0.1562 0.1341 -0.0119 -0.0011 -0.0046 57  THR   A CB  
1460 O  OG1 . THR   A 57  ? 0.1206 0.1504 0.1461 -0.0101 0.0049  -0.0107 57  THR   A OG1 
1461 C  CG2 . THR   A 57  ? 0.1443 0.1595 0.1207 -0.0059 0.0014  0.0096  57  THR   A CG2 
1469 N  N   . ASN   A 58  ? 0.1386 0.1633 0.1563 -0.0090 0.0065  -0.0280 58  ASN   A N   
1470 C  CA  . ASN   A 58  ? 0.1595 0.1587 0.1795 -0.0209 0.0191  -0.0365 58  ASN   A CA  
1471 C  C   . ASN   A 58  ? 0.1371 0.1401 0.1763 -0.0024 -0.0020 -0.0226 58  ASN   A C   
1472 O  O   . ASN   A 58  ? 0.1373 0.1557 0.1809 -0.0165 -0.0022 -0.0312 58  ASN   A O   
1473 C  CB  . ASN   A 58  ? 0.2041 0.1766 0.2222 -0.0288 0.0410  -0.0588 58  ASN   A CB  
1474 C  CG  . ASN   A 58  ? 0.2539 0.2032 0.3026 -0.0243 0.0464  -0.0407 58  ASN   A CG  
1475 O  OD1 . ASN   A 58  ? 0.2856 0.1946 0.3433 0.0138  0.0763  -0.0339 58  ASN   A OD1 
1476 N  ND2 . ASN   A 58  ? 0.2676 0.2187 0.3308 -0.0281 0.0392  -0.0381 58  ASN   A ND2 
1483 N  N   . ASN   A 59  ? 0.1201 0.1326 0.1640 -0.0080 -0.0149 -0.0143 59  ASN   A N   
1484 C  CA  . ASN   A 59  ? 0.1233 0.1248 0.1670 -0.0012 -0.0086 -0.0079 59  ASN   A CA  
1485 C  C   . ASN   A 59  ? 0.1224 0.1273 0.1542 -0.0010 -0.0106 -0.0102 59  ASN   A C   
1486 O  O   . ASN   A 59  ? 0.1244 0.1301 0.1512 -0.0039 -0.0039 0.0012  59  ASN   A O   
1487 C  CB  . ASN   A 59  ? 0.1279 0.1232 0.1627 -0.0031 -0.0180 -0.0139 59  ASN   A CB  
1488 C  CG  . ASN   A 59  ? 0.1341 0.1268 0.1655 -0.0024 -0.0186 0.0017  59  ASN   A CG  
1489 O  OD1 . ASN   A 59  ? 0.1481 0.1370 0.1581 -0.0147 -0.0228 0.0025  59  ASN   A OD1 
1490 N  ND2 . ASN   A 59  ? 0.1430 0.1318 0.1750 -0.0133 -0.0132 0.0014  59  ASN   A ND2 
1497 N  N   . ALA   A 60  ? 0.1206 0.1333 0.1542 -0.0027 -0.0087 -0.0015 60  ALA   A N   
1498 C  CA  . ALA   A 60  ? 0.1201 0.1393 0.1609 -0.0052 -0.0142 0.0043  60  ALA   A CA  
1499 C  C   . ALA   A 60  ? 0.1197 0.1308 0.1555 -0.0075 -0.0111 -0.0021 60  ALA   A C   
1500 O  O   . ALA   A 60  ? 0.1132 0.1289 0.1788 -0.0041 -0.0108 -0.0067 60  ALA   A O   
1501 C  CB  . ALA   A 60  ? 0.1327 0.1493 0.1580 -0.0060 -0.0093 -0.0089 60  ALA   A CB  
1507 N  N   . MET   A 61  ? 0.1154 0.1278 0.1464 -0.0074 -0.0020 -0.0057 61  MET   A N   
1508 C  CA  . MET   A 61  ? 0.1133 0.1223 0.1515 -0.0101 -0.0030 -0.0002 61  MET   A CA  
1509 C  C   . MET   A 61  ? 0.1150 0.1211 0.1476 -0.0112 -0.0056 -0.0005 61  MET   A C   
1510 O  O   . MET   A 61  ? 0.1151 0.1243 0.1624 -0.0083 0.0008  0.0032  61  MET   A O   
1511 C  CB  . MET   A 61  ? 0.1265 0.1245 0.1391 -0.0077 0.0060  -0.0019 61  MET   A CB  
1512 C  CG  . MET   A 61  ? 0.1225 0.1320 0.1588 -0.0041 -0.0046 0.0026  61  MET   A CG  
1513 S  SD  . MET   A 61  ? 0.1259 0.1299 0.1901 -0.0114 -0.0006 -0.0160 61  MET   A SD  
1514 C  CE  . MET   A 61  ? 0.1451 0.1370 0.2277 -0.0127 0.0114  -0.0041 61  MET   A CE  
1524 N  N   . GLN   A 62  ? 0.1187 0.1153 0.1409 -0.0090 -0.0031 -0.0013 62  GLN   A N   
1525 C  CA  . GLN   A 62  ? 0.1181 0.1126 0.1549 -0.0046 -0.0029 0.0057  62  GLN   A CA  
1526 C  C   . GLN   A 62  ? 0.1168 0.1058 0.1625 -0.0008 0.0027  0.0020  62  GLN   A C   
1527 O  O   . GLN   A 62  ? 0.1204 0.1189 0.1563 -0.0017 0.0041  -0.0019 62  GLN   A O   
1528 C  CB  . GLN   A 62  ? 0.1158 0.1137 0.1591 -0.0008 0.0003  0.0070  62  GLN   A CB  
1529 C  CG  . GLN   A 62  ? 0.1261 0.1150 0.1557 -0.0053 -0.0005 0.0116  62  GLN   A CG  
1530 C  CD  . GLN   A 62  ? 0.1308 0.1149 0.1462 -0.0006 0.0087  0.0119  62  GLN   A CD  
1531 O  OE1 . GLN   A 62  ? 0.1330 0.1275 0.1615 0.0004  0.0012  0.0030  62  GLN   A OE1 
1532 N  NE2 . GLN   A 62  ? 0.1342 0.1209 0.1612 -0.0004 -0.0007 0.0010  62  GLN   A NE2 
1541 N  N   . VAL   A 63  ? 0.1124 0.1162 0.1787 -0.0116 0.0112  -0.0147 63  VAL   A N   
1542 C  CA  . VAL   A 63  ? 0.1166 0.1269 0.1957 -0.0106 -0.0028 -0.0132 63  VAL   A CA  
1543 C  C   . VAL   A 63  ? 0.1017 0.1291 0.1773 -0.0138 -0.0077 -0.0121 63  VAL   A C   
1544 O  O   . VAL   A 63  ? 0.1093 0.1272 0.1972 -0.0180 -0.0028 -0.0092 63  VAL   A O   
1545 C  CB  . VAL   A 63  ? 0.1324 0.1422 0.2281 -0.0120 -0.0047 -0.0330 63  VAL   A CB  
1546 C  CG1 . VAL   A 63  ? 0.1434 0.1638 0.2531 -0.0097 -0.0174 -0.0496 63  VAL   A CG1 
1547 C  CG2 . VAL   A 63  ? 0.1434 0.1421 0.2384 -0.0085 0.0039  -0.0291 63  VAL   A CG2 
1557 N  N   . GLU   A 64  ? 0.1143 0.1375 0.1608 -0.0075 -0.0017 -0.0118 64  GLU   A N   
1558 C  CA  . GLU   A 64  ? 0.1155 0.1274 0.1737 -0.0012 -0.0064 0.0055  64  GLU   A CA  
1559 C  C   . GLU   A 64  ? 0.1121 0.1254 0.1697 -0.0063 -0.0016 0.0085  64  GLU   A C   
1560 O  O   . GLU   A 64  ? 0.1178 0.1302 0.1769 -0.0052 -0.0003 0.0005  64  GLU   A O   
1561 C  CB  . GLU   A 64  ? 0.1249 0.1352 0.1772 -0.0077 0.0019  -0.0044 64  GLU   A CB  
1562 C  CG  . GLU   A 64  ? 0.1334 0.1442 0.1949 -0.0128 -0.0003 0.0044  64  GLU   A CG  
1563 C  CD  . GLU   A 64  ? 0.1406 0.1557 0.1966 -0.0155 0.0065  0.0040  64  GLU   A CD  
1564 O  OE1 . GLU   A 64  ? 0.1382 0.1662 0.2038 -0.0199 0.0154  0.0033  64  GLU   A OE1 
1565 O  OE2 . GLU   A 64  ? 0.1564 0.1558 0.1906 -0.0236 -0.0080 0.0051  64  GLU   A OE2 
1572 N  N   . SER   A 65  ? 0.1064 0.1253 0.1584 0.0040  -0.0025 0.0004  65  SER   A N   
1573 C  CA  . SER   A 65  ? 0.1150 0.1176 0.1538 0.0003  -0.0106 -0.0000 65  SER   A CA  
1574 C  C   . SER   A 65  ? 0.1145 0.1283 0.1520 -0.0087 -0.0030 0.0004  65  SER   A C   
1575 O  O   . SER   A 65  ? 0.1216 0.1311 0.1804 -0.0022 0.0121  -0.0061 65  SER   A O   
1576 C  CB  . SER   A 65  ? 0.1178 0.1141 0.1613 -0.0095 0.0060  0.0030  65  SER   A CB  
1577 O  OG  . SER   A 65  ? 0.1154 0.1318 0.1652 -0.0102 -0.0056 0.0149  65  SER   A OG  
1583 N  N   . ASP   A 66  ? 0.1175 0.1235 0.1602 -0.0082 0.0086  0.0106  66  ASP   A N   
1584 C  CA  . ASP   A 66  ? 0.1286 0.1339 0.1701 -0.0060 0.0075  0.0169  66  ASP   A CA  
1585 C  C   . ASP   A 66  ? 0.1241 0.1294 0.1836 -0.0026 0.0177  0.0191  66  ASP   A C   
1586 O  O   . ASP   A 66  ? 0.1272 0.1398 0.2025 -0.0046 0.0244  0.0271  66  ASP   A O   
1587 C  CB  . ASP   A 66  ? 0.1304 0.1415 0.2099 -0.0010 0.0115  0.0307  66  ASP   A CB  
1588 C  CG  . ASP   A 66  ? 0.1612 0.1574 0.2394 -0.0052 -0.0021 0.0467  66  ASP   A CG  
1589 O  OD1 . ASP   A 66  ? 0.1602 0.1863 0.2206 -0.0111 -0.0036 0.0516  66  ASP   A OD1 
1590 O  OD2 . ASP   A 66  ? 0.1785 0.1689 0.3098 0.0126  -0.0165 0.0271  66  ASP   A OD2 
1595 N  N   . ASP   A 67  ? 0.1151 0.1316 0.1933 -0.0022 0.0077  0.0223  67  ASP   A N   
1596 C  CA  . ASP   A 67  ? 0.1192 0.1462 0.1981 -0.0073 0.0083  0.0235  67  ASP   A CA  
1597 C  C   . ASP   A 67  ? 0.1204 0.1481 0.1929 -0.0035 0.0083  0.0219  67  ASP   A C   
1598 O  O   . ASP   A 67  ? 0.1192 0.1554 0.2139 0.0043  0.0195  0.0291  67  ASP   A O   
1599 C  CB  . ASP   A 67  ? 0.1288 0.1531 0.2373 -0.0095 -0.0095 0.0358  67  ASP   A CB  
1600 C  CG  . ASP   A 67  ? 0.1252 0.1673 0.2724 -0.0123 -0.0258 0.0479  67  ASP   A CG  
1601 O  OD1 . ASP   A 67  ? 0.1293 0.1909 0.3523 -0.0153 -0.0409 0.0532  67  ASP   A OD1 
1602 O  OD2 . ASP   A 67  ? 0.1256 0.1746 0.2605 -0.0043 -0.0157 0.0365  67  ASP   A OD2 
1607 N  N   . TYR   A 68  ? 0.1212 0.1362 0.1960 0.0007  0.0135  0.0341  68  TYR   A N   
1608 C  CA  . TYR   A 68  ? 0.1317 0.1344 0.1916 -0.0013 0.0200  0.0312  68  TYR   A CA  
1609 C  C   . TYR   A 68  ? 0.1248 0.1348 0.1880 0.0007  0.0270  0.0199  68  TYR   A C   
1610 O  O   . TYR   A 68  ? 0.1332 0.1357 0.2004 0.0058  0.0254  0.0200  68  TYR   A O   
1611 C  CB  . TYR   A 68  ? 0.1333 0.1321 0.2094 0.0102  0.0392  0.0300  68  TYR   A CB  
1612 C  CG  . TYR   A 68  ? 0.1440 0.1476 0.2443 0.0021  0.0536  0.0368  68  TYR   A CG  
1613 C  CD1 . TYR   A 68  ? 0.1545 0.1532 0.2791 -0.0211 0.0429  -0.0005 68  TYR   A CD1 
1614 C  CD2 . TYR   A 68  ? 0.1685 0.1541 0.2790 0.0091  0.0533  0.0377  68  TYR   A CD2 
1615 C  CE1 . TYR   A 68  ? 0.1634 0.1651 0.3150 -0.0251 0.0540  -0.0121 68  TYR   A CE1 
1616 C  CE2 . TYR   A 68  ? 0.1651 0.1578 0.3035 -0.0007 0.0691  0.0150  68  TYR   A CE2 
1617 C  CZ  . TYR   A 68  ? 0.1663 0.1612 0.3216 -0.0255 0.0567  -0.0149 68  TYR   A CZ  
1618 O  OH  . TYR   A 68  ? 0.1960 0.1658 0.3453 -0.0209 0.0368  -0.0462 68  TYR   A OH  
1628 N  N   . ILE   A 69  ? 0.1181 0.1249 0.1764 0.0013  0.0138  0.0204  69  ILE   A N   
1629 C  CA  . ILE   A 69  ? 0.1273 0.1301 0.1722 0.0013  0.0130  0.0157  69  ILE   A CA  
1630 C  C   . ILE   A 69  ? 0.1327 0.1332 0.1681 0.0066  0.0227  0.0201  69  ILE   A C   
1631 O  O   . ILE   A 69  ? 0.1386 0.1378 0.1724 -0.0013 0.0229  0.0196  69  ILE   A O   
1632 C  CB  . ILE   A 69  ? 0.1364 0.1569 0.1798 0.0032  0.0115  -0.0025 69  ILE   A CB  
1633 C  CG1 . ILE   A 69  ? 0.1336 0.1661 0.1867 0.0021  0.0145  -0.0160 69  ILE   A CG1 
1634 C  CG2 . ILE   A 69  ? 0.1559 0.1783 0.2025 0.0110  0.0004  -0.0106 69  ILE   A CG2 
1635 C  CD1 . ILE   A 69  ? 0.1358 0.1755 0.2018 -0.0100 0.0191  -0.0281 69  ILE   A CD1 
1647 N  N   . ALA   A 70  ? 0.1334 0.1340 0.1857 -0.0062 0.0223  0.0201  70  ALA   A N   
1648 C  CA  . ALA   A 70  ? 0.1411 0.1443 0.2003 -0.0138 0.0329  0.0260  70  ALA   A CA  
1649 C  C   . ALA   A 70  ? 0.1307 0.1578 0.2087 -0.0170 0.0305  0.0232  70  ALA   A C   
1650 O  O   . ALA   A 70  ? 0.1547 0.1960 0.2361 0.0069  0.0511  0.0456  70  ALA   A O   
1651 C  CB  . ALA   A 70  ? 0.1496 0.1430 0.2170 -0.0198 0.0248  0.0248  70  ALA   A CB  
1657 N  N   . THR   A 71  ? 0.1248 0.1558 0.1947 -0.0056 0.0214  0.0264  71  THR   A N   
1658 C  CA  . THR   A 71  ? 0.1418 0.1771 0.2275 0.0051  0.0137  0.0281  71  THR   A CA  
1659 C  C   . THR   A 71  ? 0.1300 0.1705 0.2451 0.0134  0.0250  0.0248  71  THR   A C   
1660 O  O   . THR   A 71  ? 0.1344 0.1949 0.2874 0.0123  0.0372  -0.0060 71  THR   A O   
1661 C  CB  . THR   A 71  ? 0.1692 0.1983 0.2607 0.0168  -0.0188 0.0392  71  THR   A CB  
1662 O  OG1 . THR   A 71  ? 0.1931 0.2158 0.2649 0.0083  -0.0367 0.0266  71  THR   A OG1 
1663 C  CG2 . THR   A 71  ? 0.1765 0.2161 0.2911 0.0254  -0.0264 0.0482  71  THR   A CG2 
1671 N  N   . ASN   A 72  ? 0.1343 0.1525 0.2200 0.0101  0.0280  0.0333  72  ASN   A N   
1672 C  CA  . ASN   A 72  ? 0.1405 0.1512 0.2329 0.0154  0.0398  0.0290  72  ASN   A CA  
1673 C  C   . ASN   A 72  ? 0.1525 0.1495 0.2246 0.0076  0.0506  0.0168  72  ASN   A C   
1674 O  O   . ASN   A 72  ? 0.1688 0.1517 0.2529 0.0125  0.0443  0.0023  72  ASN   A O   
1675 C  CB  . ASN   A 72  ? 0.1605 0.1563 0.2303 0.0167  0.0407  0.0230  72  ASN   A CB  
1676 C  CG  . ASN   A 72  ? 0.1856 0.1716 0.2352 0.0237  0.0372  0.0246  72  ASN   A CG  
1677 O  OD1 . ASN   A 72  ? 0.1998 0.2063 0.2518 0.0232  0.0436  0.0304  72  ASN   A OD1 
1678 N  ND2 . ASN   A 72  ? 0.2020 0.1695 0.2268 0.0521  0.0224  0.0197  72  ASN   A ND2 
1685 N  N   . GLY   A 73  ? 0.1542 0.1481 0.1998 0.0037  0.0498  0.0114  73  GLY   A N   
1686 C  CA  . GLY   A 73  ? 0.1602 0.1475 0.1873 -0.0045 0.0482  0.0108  73  GLY   A CA  
1687 C  C   . GLY   A 73  ? 0.1576 0.1350 0.1784 -0.0070 0.0524  0.0250  73  GLY   A C   
1688 O  O   . GLY   A 73  ? 0.1593 0.1377 0.1954 0.0097  0.0381  0.0285  73  GLY   A O   
1692 N  N   . PRO   A 74  ? 0.1664 0.1418 0.1818 -0.0154 0.0470  0.0135  74  PRO   A N   
1693 C  CA  . PRO   A 74  ? 0.1628 0.1353 0.1873 -0.0014 0.0433  0.0121  74  PRO   A CA  
1694 C  C   . PRO   A 74  ? 0.1524 0.1244 0.1831 -0.0002 0.0334  0.0061  74  PRO   A C   
1695 O  O   . PRO   A 74  ? 0.1597 0.1295 0.2169 0.0001  0.0416  -0.0076 74  PRO   A O   
1696 C  CB  . PRO   A 74  ? 0.1815 0.1616 0.2192 -0.0002 0.0532  0.0185  74  PRO   A CB  
1697 C  CG  . PRO   A 74  ? 0.2063 0.2004 0.2599 -0.0194 0.0351  0.0037  74  PRO   A CG  
1698 C  CD  . PRO   A 74  ? 0.1823 0.1764 0.2130 -0.0295 0.0334  -0.0032 74  PRO   A CD  
1706 N  N   . LEU   A 75  ? 0.1498 0.1204 0.1704 -0.0018 0.0206  0.0002  75  LEU   A N   
1707 C  CA  . LEU   A 75  ? 0.1535 0.1133 0.1493 -0.0005 0.0097  0.0089  75  LEU   A CA  
1708 C  C   . LEU   A 75  ? 0.1640 0.1270 0.1509 0.0026  0.0148  0.0127  75  LEU   A C   
1709 O  O   . LEU   A 75  ? 0.1923 0.1427 0.1525 0.0125  0.0098  0.0055  75  LEU   A O   
1710 C  CB  . LEU   A 75  ? 0.1598 0.1239 0.1450 -0.0067 0.0139  0.0234  75  LEU   A CB  
1711 C  CG  . LEU   A 75  ? 0.1780 0.1589 0.1549 -0.0383 0.0085  0.0202  75  LEU   A CG  
1712 C  CD1 . LEU   A 75  ? 0.1874 0.2106 0.1695 -0.0363 0.0042  0.0052  75  LEU   A CD1 
1713 C  CD2 . LEU   A 75  ? 0.2135 0.1958 0.2062 -0.0109 0.0055  0.0248  75  LEU   A CD2 
1725 N  N   . LYS   A 76  ? 0.1649 0.1305 0.1637 -0.0066 0.0124  -0.0026 76  LYS   A N   
1726 C  CA  . LYS   A 76  ? 0.1615 0.1491 0.1705 -0.0081 0.0143  -0.0109 76  LYS   A CA  
1727 C  C   . LYS   A 76  ? 0.1523 0.1301 0.1393 -0.0012 0.0118  0.0026  76  LYS   A C   
1728 O  O   . LYS   A 76  ? 0.1563 0.1268 0.1463 -0.0012 0.0149  0.0148  76  LYS   A O   
1729 C  CB  . LYS   A 76  ? 0.1635 0.1718 0.2091 0.0062  0.0126  -0.0351 76  LYS   A CB  
1730 C  CG  . LYS   A 76  ? 0.1702 0.1666 0.2606 0.0122  0.0117  -0.0309 76  LYS   A CG  
1731 C  CD  . LYS   A 76  ? 0.1736 0.1661 0.3038 0.0154  0.0025  -0.0345 76  LYS   A CD  
1732 C  CE  . LYS   A 76  ? 0.1905 0.1890 0.3579 0.0071  0.0058  -0.0442 76  LYS   A CE  
1733 N  NZ  . LYS   A 76  ? 0.1877 0.1789 0.3993 -0.0156 -0.0013 -0.0519 76  LYS   A NZ  
1747 N  N   . VAL   A 77  ? 0.1635 0.1350 0.1418 0.0010  0.0258  0.0171  77  VAL   A N   
1748 C  CA  . VAL   A 77  ? 0.1587 0.1382 0.1457 0.0068  0.0192  0.0112  77  VAL   A CA  
1749 C  C   . VAL   A 77  ? 0.1534 0.1382 0.1472 0.0046  0.0150  0.0015  77  VAL   A C   
1750 O  O   . VAL   A 77  ? 0.1596 0.1410 0.1551 0.0113  0.0306  -0.0081 77  VAL   A O   
1751 C  CB  . VAL   A 77  ? 0.1722 0.1537 0.1564 0.0012  0.0119  0.0176  77  VAL   A CB  
1752 C  CG1 . VAL   A 77  ? 0.1703 0.1747 0.1863 0.0080  0.0021  -0.0018 77  VAL   A CG1 
1753 C  CG2 . VAL   A 77  ? 0.1980 0.1698 0.1777 0.0021  -0.0052 0.0229  77  VAL   A CG2 
1763 N  N   . GLY   A 78  ? 0.1492 0.1314 0.1338 0.0004  0.0176  0.0046  78  GLY   A N   
1764 C  CA  . GLY   A 78  ? 0.1499 0.1284 0.1511 -0.0043 0.0252  0.0085  78  GLY   A CA  
1765 C  C   . GLY   A 78  ? 0.1372 0.1190 0.1562 0.0020  0.0261  0.0171  78  GLY   A C   
1766 O  O   . GLY   A 78  ? 0.1314 0.1272 0.1817 -0.0038 0.0172  0.0244  78  GLY   A O   
1770 N  N   . GLY   A 79  ? 0.1423 0.1158 0.1530 -0.0016 0.0162  0.0156  79  GLY   A N   
1771 C  CA  . GLY   A 79  ? 0.1420 0.1196 0.1579 0.0021  0.0100  0.0165  79  GLY   A CA  
1772 C  C   . GLY   A 79  ? 0.1267 0.1189 0.1570 -0.0009 0.0085  0.0105  79  GLY   A C   
1773 O  O   . GLY   A 79  ? 0.1300 0.1287 0.1586 0.0161  0.0114  0.0027  79  GLY   A O   
1777 N  N   . SER   A 80  ? 0.1218 0.1285 0.1796 0.0004  0.0083  0.0014  80  SER   A N   
1778 C  CA  . SER   A 80  ? 0.1197 0.1207 0.1666 -0.0001 0.0031  0.0040  80  SER   A CA  
1779 C  C   . SER   A 80  ? 0.1186 0.1272 0.1617 -0.0031 0.0083  0.0158  80  SER   A C   
1780 O  O   . SER   A 80  ? 0.1189 0.1513 0.1996 0.0060  0.0094  -0.0007 80  SER   A O   
1781 C  CB  . SER   A 80  ? 0.1381 0.1252 0.1903 -0.0064 0.0066  0.0106  80  SER   A CB  
1782 O  OG  . SER   A 80  ? 0.1644 0.1279 0.2314 0.0034  -0.0076 0.0286  80  SER   A OG  
1788 N  N   . CYS   A 81  ? 0.1153 0.1231 0.1579 -0.0005 -0.0048 0.0152  81  CYS   A N   
1789 C  CA  . CYS   A 81  ? 0.1174 0.1318 0.1573 -0.0056 -0.0060 0.0221  81  CYS   A CA  
1790 C  C   . CYS   A 81  ? 0.1131 0.1262 0.1650 -0.0069 -0.0054 0.0311  81  CYS   A C   
1791 O  O   . CYS   A 81  ? 0.1130 0.1568 0.1694 -0.0013 -0.0026 0.0417  81  CYS   A O   
1792 C  CB  . CYS   A 81  ? 0.1265 0.1343 0.1769 -0.0166 -0.0001 0.0214  81  CYS   A CB  
1793 S  SG  . CYS   A 81  ? 0.1377 0.1289 0.1760 -0.0134 -0.0011 0.0162  81  CYS   A SG  
1799 N  N   . VAL   A 82  ? 0.1136 0.1333 0.1739 -0.0006 -0.0134 0.0209  82  VAL   A N   
1800 C  CA  . VAL   A 82  ? 0.1345 0.1417 0.1693 -0.0010 -0.0059 0.0332  82  VAL   A CA  
1801 C  C   . VAL   A 82  ? 0.1271 0.1435 0.1729 -0.0021 -0.0071 0.0309  82  VAL   A C   
1802 O  O   . VAL   A 82  ? 0.1236 0.1545 0.1897 -0.0020 -0.0097 0.0044  82  VAL   A O   
1803 C  CB  . VAL   A 82  ? 0.1615 0.1539 0.1794 0.0006  -0.0030 0.0360  82  VAL   A CB  
1804 C  CG1 . VAL   A 82  ? 0.1773 0.1693 0.2029 0.0034  -0.0025 0.0264  82  VAL   A CG1 
1805 C  CG2 . VAL   A 82  ? 0.1694 0.1572 0.2053 0.0018  -0.0010 0.0341  82  VAL   A CG2 
1815 N  N   . LEU   A 83  ? 0.1183 0.1444 0.1487 -0.0148 -0.0139 0.0155  83  LEU   A N   
1816 C  CA  . LEU   A 83  ? 0.1215 0.1463 0.1500 -0.0138 -0.0118 0.0113  83  LEU   A CA  
1817 C  C   . LEU   A 83  ? 0.1302 0.1481 0.1454 -0.0128 -0.0174 0.0238  83  LEU   A C   
1818 O  O   . LEU   A 83  ? 0.1438 0.1468 0.1585 -0.0159 -0.0085 0.0287  83  LEU   A O   
1819 C  CB  . LEU   A 83  ? 0.1329 0.1480 0.1622 -0.0124 -0.0157 0.0153  83  LEU   A CB  
1820 C  CG  . LEU   A 83  ? 0.1447 0.1587 0.1641 -0.0120 -0.0012 0.0072  83  LEU   A CG  
1821 C  CD1 . LEU   A 83  ? 0.1587 0.1659 0.1802 -0.0247 -0.0031 0.0167  83  LEU   A CD1 
1822 C  CD2 . LEU   A 83  ? 0.1410 0.1711 0.1806 -0.0103 0.0154  0.0090  83  LEU   A CD2 
1834 N  N   . SER   A 84  ? 0.1411 0.1544 0.1561 -0.0192 -0.0173 0.0280  84  SER   A N   
1835 C  CA  . SER   A 84  ? 0.1599 0.1581 0.1389 -0.0166 -0.0121 0.0202  84  SER   A CA  
1836 C  C   . SER   A 84  ? 0.1639 0.1562 0.1292 -0.0234 0.0032  0.0170  84  SER   A C   
1837 O  O   . SER   A 84  ? 0.1581 0.1651 0.1271 -0.0154 -0.0081 0.0120  84  SER   A O   
1838 C  CB  . SER   A 84  ? 0.1630 0.1812 0.1471 -0.0103 -0.0121 0.0053  84  SER   A CB  
1839 O  OG  . SER   A 84  ? 0.1634 0.2038 0.1598 -0.0157 -0.0183 -0.0028 84  SER   A OG  
1845 N  N   . GLY   A 85  ? 0.1710 0.1676 0.1394 -0.0259 0.0041  0.0077  85  GLY   A N   
1846 C  CA  . GLY   A 85  ? 0.1712 0.1738 0.1610 -0.0256 0.0117  0.0003  85  GLY   A CA  
1847 C  C   . GLY   A 85  ? 0.1716 0.1796 0.1434 -0.0184 0.0003  0.0056  85  GLY   A C   
1848 O  O   . GLY   A 85  ? 0.1729 0.1889 0.1572 -0.0285 0.0091  -0.0104 85  GLY   A O   
1852 N  N   . HIS   A 86  ? 0.1722 0.1705 0.1301 -0.0218 -0.0088 0.0043  86  HIS   A N   
1853 C  CA  . HIS   A 86  ? 0.1883 0.1811 0.1244 -0.0275 -0.0029 0.0108  86  HIS   A CA  
1854 C  C   . HIS   A 86  ? 0.2094 0.1963 0.1187 -0.0326 -0.0058 0.0065  86  HIS   A C   
1855 O  O   . HIS   A 86  ? 0.2201 0.2197 0.1364 -0.0318 0.0027  0.0002  86  HIS   A O   
1856 C  CB  . HIS   A 86  ? 0.1903 0.1713 0.1306 -0.0187 0.0073  0.0131  86  HIS   A CB  
1857 C  CG  . HIS   A 86  ? 0.1811 0.1663 0.1425 -0.0158 0.0001  0.0161  86  HIS   A CG  
1858 N  ND1 . HIS   A 86  ? 0.1907 0.1690 0.1756 -0.0266 -0.0020 0.0127  86  HIS   A ND1 
1859 C  CD2 . HIS   A 86  ? 0.1802 0.1580 0.1468 -0.0015 0.0072  0.0147  86  HIS   A CD2 
1860 C  CE1 . HIS   A 86  ? 0.1803 0.1675 0.1721 -0.0213 0.0132  0.0124  86  HIS   A CE1 
1861 N  NE2 . HIS   A 86  ? 0.1768 0.1624 0.1519 -0.0012 0.0104  0.0220  86  HIS   A NE2 
1869 N  N   . ASN   A 87  ? 0.2216 0.2072 0.1386 -0.0226 0.0176  -0.0072 87  ASN   A N   
1870 C  CA  . ASN   A 87  ? 0.2418 0.2188 0.1446 -0.0176 0.0383  -0.0160 87  ASN   A CA  
1871 C  C   . ASN   A 87  ? 0.2413 0.2360 0.1780 -0.0231 0.0547  0.0010  87  ASN   A C   
1872 O  O   . ASN   A 87  ? 0.2645 0.2549 0.2235 -0.0373 0.0857  -0.0072 87  ASN   A O   
1873 C  CB  . ASN   A 87  ? 0.2618 0.2263 0.1563 -0.0022 0.0371  -0.0184 87  ASN   A CB  
1874 C  CG  . ASN   A 87  ? 0.2774 0.2366 0.1613 0.0059  0.0504  -0.0096 87  ASN   A CG  
1875 O  OD1 . ASN   A 87  ? 0.2954 0.2365 0.1670 0.0228  0.0482  0.0039  87  ASN   A OD1 
1876 N  ND2 . ASN   A 87  ? 0.2824 0.2598 0.1760 0.0061  0.0511  -0.0048 87  ASN   A ND2 
1883 N  N   . LEU   A 88  ? 0.2102 0.2208 0.1639 -0.0255 0.0354  0.0075  88  LEU   A N   
1884 C  CA  . LEU   A 88  ? 0.1939 0.2207 0.1835 -0.0339 0.0330  0.0230  88  LEU   A CA  
1885 C  C   . LEU   A 88  ? 0.1911 0.2227 0.1758 -0.0336 0.0321  0.0286  88  LEU   A C   
1886 O  O   . LEU   A 88  ? 0.1925 0.2259 0.2086 -0.0284 0.0375  0.0474  88  LEU   A O   
1887 C  CB  . LEU   A 88  ? 0.1936 0.2284 0.2031 -0.0400 0.0029  0.0330  88  LEU   A CB  
1888 C  CG  . LEU   A 88  ? 0.2136 0.2425 0.2369 -0.0426 -0.0126 0.0313  88  LEU   A CG  
1889 C  CD1 . LEU   A 88  ? 0.2266 0.2517 0.2310 -0.0448 -0.0142 0.0179  88  LEU   A CD1 
1890 C  CD2 . LEU   A 88  ? 0.2260 0.2534 0.2731 -0.0388 -0.0138 0.0240  88  LEU   A CD2 
1902 N  N   . ALA   A 89  ? 0.1906 0.2147 0.1508 -0.0339 0.0175  0.0119  89  ALA   A N   
1903 C  CA  . ALA   A 89  ? 0.1913 0.2129 0.1336 -0.0261 0.0036  0.0223  89  ALA   A CA  
1904 C  C   . ALA   A 89  ? 0.1996 0.2135 0.1400 -0.0228 -0.0070 0.0331  89  ALA   A C   
1905 O  O   . ALA   A 89  ? 0.1956 0.2065 0.1866 -0.0359 -0.0076 0.0041  89  ALA   A O   
1906 C  CB  . ALA   A 89  ? 0.1843 0.2125 0.1202 -0.0230 -0.0019 0.0285  89  ALA   A CB  
1912 N  N   . LYS   A 90  ? 0.2070 0.2274 0.1489 -0.0333 -0.0161 0.0340  90  LYS   A N   
1913 C  CA  . LYS   A 90  ? 0.2189 0.2454 0.1649 -0.0263 -0.0351 0.0300  90  LYS   A CA  
1914 C  C   . LYS   A 90  ? 0.1925 0.2272 0.1494 -0.0310 -0.0368 0.0193  90  LYS   A C   
1915 O  O   . LYS   A 90  ? 0.1986 0.2443 0.1758 -0.0301 -0.0369 0.0083  90  LYS   A O   
1916 C  CB  . LYS   A 90  ? 0.2512 0.2841 0.2010 -0.0193 -0.0403 0.0489  90  LYS   A CB  
1917 C  CG  . LYS   A 90  ? 0.2907 0.3178 0.2955 -0.0180 -0.0376 0.0506  90  LYS   A CG  
1918 C  CD  . LYS   A 90  ? 0.3327 0.3514 0.3920 -0.0188 -0.0271 0.0557  90  LYS   A CD  
1919 C  CE  . LYS   A 90  ? 0.3675 0.3845 0.4718 -0.0199 -0.0147 0.0545  90  LYS   A CE  
1920 N  NZ  . LYS   A 90  ? 0.3759 0.3998 0.5219 -0.0222 -0.0057 0.0481  90  LYS   A NZ  
1934 N  N   . HIS   A 91  ? 0.1808 0.1973 0.1205 -0.0295 -0.0379 0.0292  91  HIS   A N   
1935 C  CA  . HIS   A 91  ? 0.1667 0.1777 0.1333 -0.0140 -0.0284 0.0246  91  HIS   A CA  
1936 C  C   . HIS   A 91  ? 0.1466 0.1609 0.1248 -0.0157 -0.0128 0.0339  91  HIS   A C   
1937 O  O   . HIS   A 91  ? 0.1478 0.1751 0.1380 -0.0233 -0.0015 0.0302  91  HIS   A O   
1938 C  CB  . HIS   A 91  ? 0.1855 0.2112 0.1799 0.0067  -0.0435 0.0287  91  HIS   A CB  
1939 C  CG  . HIS   A 91  ? 0.2299 0.2616 0.2374 0.0173  -0.0736 0.0173  91  HIS   A CG  
1940 N  ND1 . HIS   A 91  ? 0.2443 0.2884 0.2746 0.0217  -0.0878 -0.0045 91  HIS   A ND1 
1941 C  CD2 . HIS   A 91  ? 0.2563 0.2865 0.2555 0.0201  -0.0853 0.0237  91  HIS   A CD2 
1942 C  CE1 . HIS   A 91  ? 0.2564 0.3015 0.2912 0.0237  -0.0842 0.0060  91  HIS   A CE1 
1943 N  NE2 . HIS   A 91  ? 0.2665 0.3014 0.2840 0.0258  -0.0886 0.0139  91  HIS   A NE2 
1951 N  N   . CYS   A 92  ? 0.1305 0.1562 0.1400 -0.0235 -0.0108 0.0293  92  CYS   A N   
1952 C  CA  . CYS   A 92  ? 0.1297 0.1472 0.1355 -0.0142 0.0021  0.0181  92  CYS   A CA  
1953 C  C   . CYS   A 92  ? 0.1271 0.1365 0.1365 -0.0109 0.0002  0.0169  92  CYS   A C   
1954 O  O   . CYS   A 92  ? 0.1272 0.1454 0.1586 -0.0126 -0.0045 0.0155  92  CYS   A O   
1955 C  CB  . CYS   A 92  ? 0.1318 0.1444 0.1355 -0.0102 -0.0087 0.0163  92  CYS   A CB  
1956 S  SG  . CYS   A 92  ? 0.1294 0.1323 0.1563 -0.0128 -0.0058 0.0178  92  CYS   A SG  
1962 N  N   . LEU   A 93  ? 0.1277 0.1280 0.1410 -0.0091 0.0065  0.0130  93  LEU   A N   
1963 C  CA  . LEU   A 93  ? 0.1129 0.1258 0.1460 -0.0037 -0.0014 0.0210  93  LEU   A CA  
1964 C  C   . LEU   A 93  ? 0.1182 0.1161 0.1403 0.0007  0.0009  0.0150  93  LEU   A C   
1965 O  O   . LEU   A 93  ? 0.1078 0.1245 0.1454 -0.0043 -0.0033 0.0124  93  LEU   A O   
1966 C  CB  . LEU   A 93  ? 0.1231 0.1283 0.1587 -0.0098 -0.0056 0.0275  93  LEU   A CB  
1967 C  CG  . LEU   A 93  ? 0.1292 0.1270 0.1716 -0.0032 -0.0012 0.0246  93  LEU   A CG  
1968 C  CD1 . LEU   A 93  ? 0.1370 0.1357 0.1790 0.0010  0.0009  0.0145  93  LEU   A CD1 
1969 C  CD2 . LEU   A 93  ? 0.1419 0.1254 0.1853 -0.0119 -0.0033 0.0207  93  LEU   A CD2 
1981 N  N   . HIS   A 94  ? 0.1110 0.1094 0.1391 -0.0035 0.0090  0.0202  94  HIS   A N   
1982 C  CA  . HIS   A 94  ? 0.1065 0.1110 0.1490 -0.0066 0.0020  0.0166  94  HIS   A CA  
1983 C  C   . HIS   A 94  ? 0.1074 0.1078 0.1487 -0.0051 -0.0011 0.0109  94  HIS   A C   
1984 O  O   . HIS   A 94  ? 0.1100 0.1325 0.1839 -0.0050 0.0012  -0.0094 94  HIS   A O   
1985 C  CB  . HIS   A 94  ? 0.1083 0.1096 0.1517 -0.0030 -0.0056 0.0112  94  HIS   A CB  
1986 C  CG  . HIS   A 94  ? 0.1116 0.1144 0.1375 -0.0080 -0.0028 0.0165  94  HIS   A CG  
1987 N  ND1 . HIS   A 94  ? 0.1113 0.1128 0.1369 -0.0088 -0.0027 0.0166  94  HIS   A ND1 
1988 C  CD2 . HIS   A 94  ? 0.1197 0.1226 0.1459 -0.0065 -0.0022 0.0077  94  HIS   A CD2 
1989 C  CE1 . HIS   A 94  ? 0.1148 0.1168 0.1340 -0.0134 -0.0118 0.0142  94  HIS   A CE1 
1990 N  NE2 . HIS   A 94  ? 0.1229 0.1209 0.1448 -0.0128 -0.0060 0.0089  94  HIS   A NE2 
1998 N  N   . VAL   A 95  ? 0.1055 0.1131 0.1232 -0.0039 0.0045  0.0091  95  VAL   A N   
1999 C  CA  . VAL   A 95  ? 0.1160 0.1116 0.1294 -0.0036 0.0110  0.0086  95  VAL   A CA  
2000 C  C   . VAL   A 95  ? 0.1149 0.1120 0.1161 -0.0143 0.0057  0.0053  95  VAL   A C   
2001 O  O   . VAL   A 95  ? 0.1134 0.1232 0.1284 0.0048  0.0021  0.0090  95  VAL   A O   
2002 C  CB  . VAL   A 95  ? 0.1151 0.1100 0.1562 -0.0102 0.0039  0.0115  95  VAL   A CB  
2003 C  CG1 . VAL   A 95  ? 0.1284 0.1153 0.1631 -0.0172 0.0021  0.0028  95  VAL   A CG1 
2004 C  CG2 . VAL   A 95  ? 0.1199 0.1209 0.1523 -0.0092 0.0083  0.0291  95  VAL   A CG2 
2014 N  N   . VAL   A 96  ? 0.1164 0.1132 0.1197 -0.0035 0.0025  0.0085  96  VAL   A N   
2015 C  CA  . VAL   A 96  ? 0.1322 0.1198 0.1289 0.0019  0.0060  0.0219  96  VAL   A CA  
2016 C  C   . VAL   A 96  ? 0.1327 0.1249 0.1317 -0.0013 0.0130  0.0145  96  VAL   A C   
2017 O  O   . VAL   A 96  ? 0.1391 0.1289 0.1508 -0.0056 0.0197  -0.0060 96  VAL   A O   
2018 C  CB  . VAL   A 96  ? 0.1291 0.1230 0.1437 0.0008  0.0179  0.0201  96  VAL   A CB  
2019 C  CG1 . VAL   A 96  ? 0.1414 0.1316 0.1315 -0.0026 0.0156  0.0040  96  VAL   A CG1 
2020 C  CG2 . VAL   A 96  ? 0.1258 0.1241 0.1683 -0.0148 0.0158  0.0136  96  VAL   A CG2 
2030 N  N   . GLY   A 97  ? 0.1322 0.1225 0.1359 -0.0061 0.0041  0.0099  97  GLY   A N   
2031 C  CA  . GLY   A 97  ? 0.1417 0.1340 0.1341 -0.0058 -0.0037 0.0126  97  GLY   A CA  
2032 C  C   . GLY   A 97  ? 0.1363 0.1474 0.1271 -0.0061 0.0049  0.0086  97  GLY   A C   
2033 O  O   . GLY   A 97  ? 0.1472 0.1462 0.1448 -0.0086 -0.0012 0.0151  97  GLY   A O   
2037 N  N   . PRO   A 98  ? 0.1387 0.1513 0.1264 -0.0031 -0.0039 0.0193  98  PRO   A N   
2038 C  CA  . PRO   A 98  ? 0.1485 0.1753 0.1346 -0.0091 0.0033  0.0115  98  PRO   A CA  
2039 C  C   . PRO   A 98  ? 0.1564 0.1877 0.1183 -0.0164 -0.0074 0.0290  98  PRO   A C   
2040 O  O   . PRO   A 98  ? 0.1504 0.1677 0.1550 -0.0120 -0.0049 0.0268  98  PRO   A O   
2041 C  CB  . PRO   A 98  ? 0.1701 0.1867 0.1381 -0.0008 -0.0043 -0.0063 98  PRO   A CB  
2042 C  CG  . PRO   A 98  ? 0.1687 0.1767 0.1409 -0.0024 -0.0076 -0.0106 98  PRO   A CG  
2043 C  CD  . PRO   A 98  ? 0.1483 0.1549 0.1299 -0.0019 -0.0042 0.0084  98  PRO   A CD  
2051 N  N   A ASN   A 99  ? 0.1597 0.2173 0.1249 -0.0204 -0.0027 0.0432  99  ASN   A N   
2052 N  N   B ASN   A 99  ? 0.1787 0.1933 0.1269 -0.0139 -0.0172 0.0508  99  ASN   A N   
2053 C  CA  A ASN   A 99  ? 0.1754 0.2331 0.1238 -0.0272 -0.0025 0.0568  99  ASN   A CA  
2054 C  CA  B ASN   A 99  ? 0.2063 0.1932 0.1371 -0.0129 -0.0254 0.0684  99  ASN   A CA  
2055 C  C   A ASN   A 99  ? 0.1919 0.2560 0.1229 -0.0396 -0.0047 0.0581  99  ASN   A C   
2056 C  C   B ASN   A 99  ? 0.2263 0.1940 0.1425 -0.0100 -0.0292 0.0633  99  ASN   A C   
2057 O  O   A ASN   A 99  ? 0.2032 0.2672 0.1383 -0.0360 -0.0072 0.0555  99  ASN   A O   
2058 O  O   B ASN   A 99  ? 0.2286 0.1753 0.1561 -0.0042 -0.0353 0.0414  99  ASN   A O   
2059 C  CB  A ASN   A 99  ? 0.1758 0.2278 0.1172 -0.0274 -0.0135 0.0630  99  ASN   A CB  
2060 C  CB  B ASN   A 99  ? 0.2157 0.1961 0.1623 -0.0163 -0.0357 0.0785  99  ASN   A CB  
2061 C  CG  A ASN   A 99  ? 0.1795 0.2232 0.1104 -0.0265 -0.0239 0.0465  99  ASN   A CG  
2062 C  CG  B ASN   A 99  ? 0.2253 0.1998 0.1801 -0.0215 -0.0420 0.0910  99  ASN   A CG  
2063 O  OD1 A ASN   A 99  ? 0.1872 0.2349 0.1141 -0.0173 -0.0168 0.0257  99  ASN   A OD1 
2064 O  OD1 B ASN   A 99  ? 0.2316 0.2104 0.1610 -0.0248 -0.0446 0.0964  99  ASN   A OD1 
2065 N  ND2 A ASN   A 99  ? 0.1889 0.2176 0.1151 -0.0191 -0.0318 0.0653  99  ASN   A ND2 
2066 N  ND2 B ASN   A 99  ? 0.2304 0.1981 0.2002 -0.0139 -0.0491 0.0851  99  ASN   A ND2 
2079 N  N   A VAL   A 100 ? 0.2051 0.2695 0.1315 -0.0523 -0.0300 0.0418  100 VAL   A N   
2080 N  N   B VAL   A 100 ? 0.2451 0.2215 0.1637 -0.0080 -0.0304 0.0597  100 VAL   A N   
2081 C  CA  A VAL   A 100 ? 0.2273 0.2810 0.1513 -0.0611 -0.0327 0.0312  100 VAL   A CA  
2082 C  CA  B VAL   A 100 ? 0.2638 0.2481 0.2024 -0.0060 -0.0241 0.0445  100 VAL   A CA  
2083 C  C   A VAL   A 100 ? 0.2381 0.2863 0.1409 -0.0648 -0.0286 0.0477  100 VAL   A C   
2084 C  C   B VAL   A 100 ? 0.2750 0.2638 0.2100 0.0057  -0.0255 0.0449  100 VAL   A C   
2085 O  O   A VAL   A 100 ? 0.2494 0.2889 0.1625 -0.0567 -0.0120 0.0506  100 VAL   A O   
2086 O  O   B VAL   A 100 ? 0.2753 0.2620 0.2161 0.0109  -0.0234 0.0373  100 VAL   A O   
2087 C  CB  A VAL   A 100 ? 0.2460 0.2869 0.1807 -0.0644 -0.0365 0.0189  100 VAL   A CB  
2088 C  CB  B VAL   A 100 ? 0.2718 0.2537 0.2349 -0.0081 -0.0196 0.0303  100 VAL   A CB  
2089 C  CG1 A VAL   A 100 ? 0.2487 0.2892 0.1954 -0.0666 -0.0306 0.0245  100 VAL   A CG1 
2090 C  CG1 B VAL   A 100 ? 0.2725 0.2554 0.2470 -0.0115 -0.0152 0.0294  100 VAL   A CG1 
2091 C  CG2 A VAL   A 100 ? 0.2544 0.2891 0.1648 -0.0668 -0.0320 0.0053  100 VAL   A CG2 
2092 C  CG2 B VAL   A 100 ? 0.2763 0.2551 0.2488 -0.0111 -0.0135 0.0213  100 VAL   A CG2 
2111 N  N   A ASN   A 101 ? 0.2422 0.2983 0.1466 -0.0666 -0.0240 0.0697  101 ASN   A N   
2112 N  N   B ASN   A 101 ? 0.2876 0.2745 0.2174 0.0109  -0.0292 0.0505  101 ASN   A N   
2113 C  CA  A ASN   A 101 ? 0.2568 0.3042 0.1524 -0.0715 -0.0185 0.0903  101 ASN   A CA  
2114 C  CA  B ASN   A 101 ? 0.3011 0.2797 0.2260 0.0162  -0.0253 0.0576  101 ASN   A CA  
2115 C  C   A ASN   A 101 ? 0.2841 0.3339 0.1818 -0.0717 0.0028  0.1088  101 ASN   A C   
2116 C  C   B ASN   A 101 ? 0.3166 0.2935 0.2449 0.0158  -0.0117 0.0718  101 ASN   A C   
2117 O  O   A ASN   A 101 ? 0.2986 0.3361 0.2251 -0.0698 -0.0026 0.0982  101 ASN   A O   
2118 O  O   B ASN   A 101 ? 0.3218 0.2932 0.2407 0.0164  -0.0166 0.0809  101 ASN   A O   
2119 C  CB  A ASN   A 101 ? 0.2510 0.2859 0.1478 -0.0693 -0.0372 0.0794  101 ASN   A CB  
2120 C  CB  B ASN   A 101 ? 0.2990 0.2728 0.2228 0.0189  -0.0282 0.0464  101 ASN   A CB  
2121 C  CG  A ASN   A 101 ? 0.2471 0.2735 0.1505 -0.0676 -0.0472 0.0459  101 ASN   A CG  
2122 C  CG  B ASN   A 101 ? 0.3001 0.2717 0.2330 0.0172  -0.0299 0.0354  101 ASN   A CG  
2123 O  OD1 A ASN   A 101 ? 0.2387 0.2751 0.1742 -0.0461 -0.0455 0.0088  101 ASN   A OD1 
2124 O  OD1 B ASN   A 101 ? 0.3069 0.2730 0.2427 0.0118  -0.0244 0.0346  101 ASN   A OD1 
2125 N  ND2 A ASN   A 101 ? 0.2529 0.2630 0.1543 -0.0815 -0.0397 0.0565  101 ASN   A ND2 
2126 N  ND2 B ASN   A 101 ? 0.2982 0.2718 0.2419 0.0211  -0.0274 0.0242  101 ASN   A ND2 
2139 N  N   A LYS   A 102 ? 0.2933 0.3643 0.2114 -0.0753 0.0170  0.1158  102 LYS   A N   
2140 N  N   B LYS   A 102 ? 0.3262 0.3058 0.2710 0.0128  0.0058  0.0760  102 LYS   A N   
2141 C  CA  A LYS   A 102 ? 0.3055 0.3889 0.2296 -0.0765 0.0131  0.1131  102 LYS   A CA  
2142 C  CA  B LYS   A 102 ? 0.3360 0.3176 0.2804 0.0049  0.0181  0.0762  102 LYS   A CA  
2143 C  C   A LYS   A 102 ? 0.3134 0.4118 0.2281 -0.0640 0.0108  0.1031  102 LYS   A C   
2144 C  C   B LYS   A 102 ? 0.3337 0.3153 0.2565 0.0081  0.0099  0.0911  102 LYS   A C   
2145 O  O   A LYS   A 102 ? 0.3128 0.4225 0.2367 -0.0604 0.0140  0.0968  102 LYS   A O   
2146 O  O   B LYS   A 102 ? 0.3363 0.3118 0.2449 0.0107  0.0092  0.1097  102 LYS   A O   
2147 C  CB  A LYS   A 102 ? 0.3139 0.3909 0.2633 -0.0847 0.0044  0.1023  102 LYS   A CB  
2148 C  CB  B LYS   A 102 ? 0.3473 0.3308 0.3149 -0.0032 0.0292  0.0611  102 LYS   A CB  
2149 C  CG  A LYS   A 102 ? 0.3221 0.3909 0.2902 -0.0904 -0.0058 0.0857  102 LYS   A CG  
2150 C  CG  B LYS   A 102 ? 0.3566 0.3415 0.3505 -0.0101 0.0379  0.0473  102 LYS   A CG  
2151 C  CD  A LYS   A 102 ? 0.3336 0.3920 0.3216 -0.0950 -0.0167 0.0647  102 LYS   A CD  
2152 C  CD  B LYS   A 102 ? 0.3656 0.3523 0.3872 -0.0158 0.0455  0.0342  102 LYS   A CD  
2153 C  CE  A LYS   A 102 ? 0.3445 0.3927 0.3407 -0.0970 -0.0230 0.0553  102 LYS   A CE  
2154 C  CE  B LYS   A 102 ? 0.3730 0.3602 0.4165 -0.0197 0.0475  0.0274  102 LYS   A CE  
2155 N  NZ  A LYS   A 102 ? 0.3489 0.3905 0.3525 -0.1035 -0.0212 0.0469  102 LYS   A NZ  
2156 N  NZ  B LYS   A 102 ? 0.3769 0.3647 0.4326 -0.0224 0.0477  0.0229  102 LYS   A NZ  
2183 N  N   A GLY   A 103 ? 0.3187 0.4244 0.2476 -0.0513 0.0011  0.0781  103 GLY   A N   
2184 N  N   B GLY   A 103 ? 0.3273 0.3200 0.2523 0.0117  -0.0036 0.0778  103 GLY   A N   
2185 C  CA  A GLY   A 103 ? 0.3246 0.4320 0.2510 -0.0388 0.0002  0.0583  103 GLY   A CA  
2186 C  CA  B GLY   A 103 ? 0.3211 0.3182 0.2451 0.0145  -0.0131 0.0769  103 GLY   A CA  
2187 C  C   A GLY   A 103 ? 0.3265 0.4389 0.2565 -0.0316 0.0079  0.0465  103 GLY   A C   
2188 C  C   B GLY   A 103 ? 0.3110 0.3128 0.2270 0.0150  -0.0157 0.0701  103 GLY   A C   
2189 O  O   A GLY   A 103 ? 0.3382 0.4459 0.2800 -0.0258 0.0095  0.0368  103 GLY   A O   
2190 O  O   B GLY   A 103 ? 0.3197 0.3157 0.2272 0.0153  -0.0195 0.0751  103 GLY   A O   
2197 N  N   A GLU   A 104 ? 0.3119 0.4332 0.2213 -0.0359 0.0187  0.0408  104 GLU   A N   
2198 N  N   B GLU   A 104 ? 0.2906 0.3014 0.2016 0.0138  -0.0218 0.0658  104 GLU   A N   
2199 C  CA  A GLU   A 104 ? 0.2939 0.4229 0.1963 -0.0478 0.0308  0.0348  104 GLU   A CA  
2200 C  CA  B GLU   A 104 ? 0.2725 0.2908 0.1810 0.0086  -0.0255 0.0543  104 GLU   A CA  
2201 C  C   A GLU   A 104 ? 0.2972 0.4309 0.1923 -0.0481 0.0285  0.0094  104 GLU   A C   
2202 C  C   B GLU   A 104 ? 0.2712 0.2882 0.1836 0.0160  -0.0188 0.0378  104 GLU   A C   
2203 O  O   A GLU   A 104 ? 0.2901 0.4329 0.2010 -0.0490 0.0134  0.0047  104 GLU   A O   
2204 O  O   B GLU   A 104 ? 0.2682 0.2782 0.1880 0.0193  -0.0192 0.0436  104 GLU   A O   
2205 C  CB  A GLU   A 104 ? 0.2655 0.4027 0.1754 -0.0612 0.0452  0.0584  104 GLU   A CB  
2206 C  CB  B GLU   A 104 ? 0.2573 0.2859 0.1709 -0.0037 -0.0310 0.0562  104 GLU   A CB  
2207 C  CG  A GLU   A 104 ? 0.2480 0.3861 0.1857 -0.0670 0.0455  0.0740  104 GLU   A CG  
2208 C  CG  B GLU   A 104 ? 0.2477 0.2873 0.1824 -0.0102 -0.0415 0.0542  104 GLU   A CG  
2209 C  CD  A GLU   A 104 ? 0.2317 0.3707 0.1853 -0.0687 0.0444  0.0809  104 GLU   A CD  
2210 C  CD  B GLU   A 104 ? 0.2352 0.2857 0.1869 -0.0117 -0.0540 0.0516  104 GLU   A CD  
2211 O  OE1 A GLU   A 104 ? 0.2168 0.3593 0.1555 -0.0656 0.0355  0.0792  104 GLU   A OE1 
2212 O  OE1 B GLU   A 104 ? 0.2257 0.2809 0.1755 -0.0076 -0.0656 0.0526  104 GLU   A OE1 
2213 O  OE2 A GLU   A 104 ? 0.2441 0.3669 0.2105 -0.0706 0.0448  0.0931  104 GLU   A OE2 
2214 O  OE2 B GLU   A 104 ? 0.2410 0.2877 0.2078 -0.0158 -0.0479 0.0477  104 GLU   A OE2 
2227 N  N   A ASP   A 105 ? 0.3063 0.4349 0.1952 -0.0446 0.0414  -0.0182 105 ASP   A N   
2228 N  N   B ASP   A 105 ? 0.2804 0.2992 0.2064 0.0174  -0.0098 0.0140  105 ASP   A N   
2229 C  CA  A ASP   A 105 ? 0.3125 0.4369 0.2294 -0.0385 0.0421  -0.0429 105 ASP   A CA  
2230 C  CA  B ASP   A 105 ? 0.2876 0.3092 0.2371 0.0208  0.0024  -0.0163 105 ASP   A CA  
2231 C  C   A ASP   A 105 ? 0.2852 0.4190 0.1923 -0.0524 0.0304  -0.0614 105 ASP   A C   
2232 C  C   B ASP   A 105 ? 0.2869 0.3105 0.2287 0.0072  0.0048  -0.0242 105 ASP   A C   
2233 O  O   A ASP   A 105 ? 0.2712 0.4110 0.1413 -0.0566 0.0315  -0.0867 105 ASP   A O   
2234 O  O   B ASP   A 105 ? 0.2826 0.3077 0.2023 0.0073  0.0094  -0.0307 105 ASP   A O   
2235 C  CB  A ASP   A 105 ? 0.3421 0.4562 0.3028 -0.0221 0.0495  -0.0503 105 ASP   A CB  
2236 C  CB  B ASP   A 105 ? 0.2953 0.3172 0.2769 0.0346  0.0123  -0.0393 105 ASP   A CB  
2237 C  CG  A ASP   A 105 ? 0.3693 0.4703 0.3665 -0.0095 0.0501  -0.0567 105 ASP   A CG  
2238 C  CG  B ASP   A 105 ? 0.3003 0.3200 0.3086 0.0475  0.0178  -0.0603 105 ASP   A CG  
2239 O  OD1 A ASP   A 105 ? 0.3757 0.4759 0.3757 -0.0078 0.0484  -0.0658 105 ASP   A OD1 
2240 O  OD1 B ASP   A 105 ? 0.3039 0.3181 0.3061 0.0467  0.0167  -0.0714 105 ASP   A OD1 
2241 O  OD2 A ASP   A 105 ? 0.3861 0.4757 0.4039 -0.0043 0.0530  -0.0501 105 ASP   A OD2 
2242 O  OD2 B ASP   A 105 ? 0.3010 0.3234 0.3366 0.0535  0.0199  -0.0589 105 ASP   A OD2 
2251 N  N   A ILE   A 106 ? 0.2687 0.4037 0.2091 -0.0607 0.0050  -0.0604 106 ILE   A N   
2252 N  N   B ILE   A 106 ? 0.2891 0.3136 0.2471 -0.0050 -0.0022 -0.0266 106 ILE   A N   
2253 C  CA  A ILE   A 106 ? 0.2406 0.3860 0.2238 -0.0753 -0.0198 -0.0759 106 ILE   A CA  
2254 C  CA  B ILE   A 106 ? 0.2892 0.3183 0.2670 -0.0221 -0.0069 -0.0347 106 ILE   A CA  
2255 C  C   A ILE   A 106 ? 0.2276 0.3615 0.2310 -0.0907 -0.0171 -0.0953 106 ILE   A C   
2256 C  C   B ILE   A 106 ? 0.2878 0.3132 0.2694 -0.0348 0.0001  -0.0382 106 ILE   A C   
2257 O  O   A ILE   A 106 ? 0.2046 0.3501 0.2356 -0.0969 -0.0041 -0.0967 106 ILE   A O   
2258 O  O   B ILE   A 106 ? 0.2823 0.3115 0.2650 -0.0361 0.0020  -0.0403 106 ILE   A O   
2259 C  CB  A ILE   A 106 ? 0.2360 0.3961 0.2617 -0.0630 -0.0412 -0.0496 106 ILE   A CB  
2260 C  CB  B ILE   A 106 ? 0.2936 0.3301 0.2936 -0.0239 -0.0180 -0.0281 106 ILE   A CB  
2261 C  CG1 A ILE   A 106 ? 0.2231 0.3988 0.2854 -0.0483 -0.0426 -0.0250 106 ILE   A CG1 
2262 C  CG1 B ILE   A 106 ? 0.2928 0.3365 0.3104 -0.0209 -0.0215 -0.0204 106 ILE   A CG1 
2263 C  CG2 A ILE   A 106 ? 0.2430 0.3983 0.2706 -0.0635 -0.0467 -0.0493 106 ILE   A CG2 
2264 C  CG2 B ILE   A 106 ? 0.2974 0.3323 0.2972 -0.0257 -0.0211 -0.0295 106 ILE   A CG2 
2265 C  CD1 A ILE   A 106 ? 0.2191 0.3973 0.3001 -0.0372 -0.0341 -0.0133 106 ILE   A CD1 
2266 C  CD1 B ILE   A 106 ? 0.2941 0.3380 0.3222 -0.0179 -0.0199 -0.0181 106 ILE   A CD1 
2289 N  N   A GLN   A 107 ? 0.2525 0.3462 0.2506 -0.0863 0.0009  -0.1108 107 GLN   A N   
2290 N  N   B GLN   A 107 ? 0.2924 0.3058 0.2804 -0.0419 0.0120  -0.0426 107 GLN   A N   
2291 C  CA  A GLN   A 107 ? 0.2768 0.3307 0.3260 -0.0702 0.0280  -0.0998 107 GLN   A CA  
2292 C  CA  B GLN   A 107 ? 0.2950 0.2988 0.3175 -0.0463 0.0236  -0.0438 107 GLN   A CA  
2293 C  C   A GLN   A 107 ? 0.2482 0.2802 0.3125 -0.0613 0.0530  -0.0751 107 GLN   A C   
2294 C  C   B GLN   A 107 ? 0.2614 0.2670 0.2955 -0.0503 0.0441  -0.0509 107 GLN   A C   
2295 O  O   A GLN   A 107 ? 0.2485 0.2725 0.3641 -0.0555 0.0689  -0.0719 107 GLN   A O   
2296 O  O   B GLN   A 107 ? 0.2686 0.2668 0.3233 -0.0489 0.0462  -0.0475 107 GLN   A O   
2297 C  CB  A GLN   A 107 ? 0.3168 0.3593 0.4187 -0.0727 0.0161  -0.1001 107 GLN   A CB  
2298 C  CB  B GLN   A 107 ? 0.3256 0.3213 0.3766 -0.0501 0.0085  -0.0315 107 GLN   A CB  
2299 C  CG  A GLN   A 107 ? 0.3540 0.3878 0.5177 -0.0719 0.0071  -0.0917 107 GLN   A CG  
2300 C  CG  B GLN   A 107 ? 0.3525 0.3424 0.4388 -0.0521 -0.0053 -0.0170 107 GLN   A CG  
2301 C  CD  A GLN   A 107 ? 0.3871 0.4111 0.6021 -0.0695 0.0016  -0.0789 107 GLN   A CD  
2302 C  CD  B GLN   A 107 ? 0.3749 0.3611 0.4910 -0.0509 -0.0152 -0.0034 107 GLN   A CD  
2303 O  OE1 A GLN   A 107 ? 0.4039 0.4182 0.6370 -0.0659 -0.0010 -0.0749 107 GLN   A OE1 
2304 O  OE1 B GLN   A 107 ? 0.3819 0.3681 0.5091 -0.0494 -0.0177 0.0026  107 GLN   A OE1 
2305 N  NE2 A GLN   A 107 ? 0.3946 0.4210 0.6301 -0.0724 -0.0012 -0.0774 107 GLN   A NE2 
2306 N  NE2 B GLN   A 107 ? 0.3822 0.3667 0.5102 -0.0511 -0.0224 0.0012  107 GLN   A NE2 
2323 N  N   . LEU   A 108 ? 0.2205 0.2358 0.2576 -0.0564 0.0543  -0.0645 108 LEU   A N   
2324 C  CA  . LEU   A 108 ? 0.1888 0.1864 0.2191 -0.0233 0.0440  -0.0291 108 LEU   A CA  
2325 C  C   . LEU   A 108 ? 0.1640 0.1464 0.2113 -0.0093 0.0383  0.0006  108 LEU   A C   
2326 O  O   . LEU   A 108 ? 0.1571 0.1440 0.2329 -0.0004 0.0467  0.0017  108 LEU   A O   
2327 C  CB  . LEU   A 108 ? 0.1877 0.1945 0.2150 -0.0266 0.0480  -0.0197 108 LEU   A CB  
2328 C  CG  . LEU   A 108 ? 0.2003 0.2154 0.2397 -0.0250 0.0589  -0.0258 108 LEU   A CG  
2329 C  CD1 . LEU   A 108 ? 0.2196 0.2210 0.2414 -0.0326 0.0656  -0.0207 108 LEU   A CD1 
2330 C  CD2 . LEU   A 108 ? 0.2037 0.2357 0.2773 -0.0169 0.0619  -0.0193 108 LEU   A CD2 
2343 N  N   . LEU   A 109 ? 0.1469 0.1388 0.2056 0.0047  0.0244  0.0103  109 LEU   A N   
2344 C  CA  . LEU   A 109 ? 0.1410 0.1351 0.1924 0.0046  0.0124  0.0142  109 LEU   A CA  
2345 C  C   . LEU   A 109 ? 0.1312 0.1298 0.1871 -0.0034 0.0158  0.0041  109 LEU   A C   
2346 O  O   . LEU   A 109 ? 0.1426 0.1149 0.2033 -0.0007 0.0062  0.0085  109 LEU   A O   
2347 C  CB  . LEU   A 109 ? 0.1462 0.1427 0.2143 0.0100  0.0019  0.0343  109 LEU   A CB  
2348 C  CG  . LEU   A 109 ? 0.1404 0.1501 0.2168 0.0061  0.0069  0.0345  109 LEU   A CG  
2349 C  CD1 . LEU   A 109 ? 0.1458 0.1382 0.2281 0.0028  0.0141  0.0187  109 LEU   A CD1 
2350 C  CD2 . LEU   A 109 ? 0.1391 0.1714 0.2368 0.0013  0.0006  0.0290  109 LEU   A CD2 
2362 N  N   . LYS   A 110 ? 0.1338 0.1298 0.1737 -0.0028 0.0060  0.0026  110 LYS   A N   
2363 C  CA  . LYS   A 110 ? 0.1339 0.1242 0.1948 -0.0086 -0.0023 0.0110  110 LYS   A CA  
2364 C  C   . LYS   A 110 ? 0.1363 0.1162 0.1800 -0.0042 0.0050  0.0038  110 LYS   A C   
2365 O  O   . LYS   A 110 ? 0.1289 0.1147 0.1940 -0.0058 0.0086  -0.0064 110 LYS   A O   
2366 C  CB  . LYS   A 110 ? 0.1386 0.1273 0.2221 -0.0110 -0.0053 -0.0012 110 LYS   A CB  
2367 C  CG  . LYS   A 110 ? 0.1462 0.1262 0.2247 -0.0045 -0.0144 -0.0014 110 LYS   A CG  
2368 C  CD  . LYS   A 110 ? 0.1458 0.1302 0.2277 -0.0114 -0.0088 -0.0095 110 LYS   A CD  
2369 C  CE  . LYS   A 110 ? 0.1564 0.1431 0.2488 -0.0081 0.0061  -0.0176 110 LYS   A CE  
2370 N  NZ  . LYS   A 110 ? 0.1554 0.1472 0.2549 -0.0193 0.0158  -0.0070 110 LYS   A NZ  
2384 N  N   . SER   A 111 ? 0.1326 0.1233 0.1772 0.0019  0.0038  0.0091  111 SER   A N   
2385 C  CA  . SER   A 111 ? 0.1221 0.1272 0.1820 0.0004  0.0099  0.0029  111 SER   A CA  
2386 C  C   . SER   A 111 ? 0.1196 0.1186 0.1845 -0.0085 0.0112  0.0114  111 SER   A C   
2387 O  O   . SER   A 111 ? 0.1332 0.1129 0.2010 -0.0068 0.0154  0.0117  111 SER   A O   
2388 C  CB  . SER   A 111 ? 0.1430 0.1496 0.1940 -0.0030 0.0130  -0.0064 111 SER   A CB  
2389 O  OG  . SER   A 111 ? 0.1905 0.1685 0.2001 0.0048  0.0247  -0.0180 111 SER   A OG  
2395 N  N   . ALA   A 112 ? 0.1259 0.1129 0.1904 -0.0043 0.0141  0.0131  112 ALA   A N   
2396 C  CA  . ALA   A 112 ? 0.1282 0.1141 0.1818 -0.0074 0.0231  -0.0006 112 ALA   A CA  
2397 C  C   . ALA   A 112 ? 0.1246 0.1114 0.1944 -0.0043 0.0124  0.0030  112 ALA   A C   
2398 O  O   . ALA   A 112 ? 0.1232 0.1069 0.2030 -0.0137 0.0140  0.0118  112 ALA   A O   
2399 C  CB  . ALA   A 112 ? 0.1401 0.1190 0.1824 -0.0038 0.0190  -0.0028 112 ALA   A CB  
2405 N  N   . TYR   A 113 ? 0.1172 0.1144 0.1890 -0.0061 0.0100  0.0134  113 TYR   A N   
2406 C  CA  . TYR   A 113 ? 0.1134 0.1151 0.1835 -0.0039 0.0208  0.0135  113 TYR   A CA  
2407 C  C   . TYR   A 113 ? 0.1126 0.1102 0.1824 -0.0125 0.0122  0.0082  113 TYR   A C   
2408 O  O   . TYR   A 113 ? 0.1211 0.1161 0.2022 -0.0061 0.0172  0.0079  113 TYR   A O   
2409 C  CB  . TYR   A 113 ? 0.1154 0.1211 0.1938 -0.0046 0.0031  0.0142  113 TYR   A CB  
2410 C  CG  . TYR   A 113 ? 0.1152 0.1209 0.1805 -0.0108 0.0137  0.0198  113 TYR   A CG  
2411 C  CD1 . TYR   A 113 ? 0.1191 0.1274 0.1788 0.0021  0.0101  0.0183  113 TYR   A CD1 
2412 C  CD2 . TYR   A 113 ? 0.1207 0.1234 0.1779 -0.0106 0.0088  0.0176  113 TYR   A CD2 
2413 C  CE1 . TYR   A 113 ? 0.1222 0.1367 0.1761 -0.0050 0.0048  0.0224  113 TYR   A CE1 
2414 C  CE2 . TYR   A 113 ? 0.1249 0.1310 0.1726 -0.0084 0.0061  0.0227  113 TYR   A CE2 
2415 C  CZ  . TYR   A 113 ? 0.1214 0.1339 0.1730 0.0028  0.0166  0.0223  113 TYR   A CZ  
2416 O  OH  . TYR   A 113 ? 0.1221 0.1426 0.1792 0.0071  0.0138  0.0283  113 TYR   A OH  
2426 N  N   . GLU   A 114 ? 0.1154 0.1131 0.1878 -0.0077 0.0143  0.0180  114 GLU   A N   
2427 C  CA  . GLU   A 114 ? 0.1196 0.1092 0.1978 -0.0005 0.0111  0.0158  114 GLU   A CA  
2428 C  C   . GLU   A 114 ? 0.1156 0.1156 0.1934 -0.0022 0.0124  0.0129  114 GLU   A C   
2429 O  O   . GLU   A 114 ? 0.1225 0.1217 0.1958 0.0017  0.0083  0.0145  114 GLU   A O   
2430 C  CB  . GLU   A 114 ? 0.1166 0.1113 0.1967 -0.0068 0.0058  0.0138  114 GLU   A CB  
2431 C  CG  . GLU   A 114 ? 0.1272 0.1133 0.2045 0.0041  0.0086  0.0063  114 GLU   A CG  
2432 C  CD  . GLU   A 114 ? 0.1340 0.1135 0.2208 -0.0031 0.0050  0.0024  114 GLU   A CD  
2433 O  OE1 . GLU   A 114 ? 0.1337 0.1166 0.2251 -0.0089 0.0149  -0.0048 114 GLU   A OE1 
2434 O  OE2 . GLU   A 114 ? 0.1544 0.1212 0.2351 -0.0103 0.0069  -0.0163 114 GLU   A OE2 
2441 N  N   . ASN   A 115 ? 0.1200 0.1143 0.1827 -0.0104 0.0107  0.0087  115 ASN   A N   
2442 C  CA  . ASN   A 115 ? 0.1209 0.1226 0.1849 -0.0107 0.0155  0.0066  115 ASN   A CA  
2443 C  C   . ASN   A 115 ? 0.1189 0.1141 0.1788 -0.0098 0.0066  0.0138  115 ASN   A C   
2444 O  O   . ASN   A 115 ? 0.1222 0.1239 0.1903 -0.0079 0.0092  0.0200  115 ASN   A O   
2445 C  CB  . ASN   A 115 ? 0.1244 0.1277 0.1775 -0.0149 0.0131  0.0049  115 ASN   A CB  
2446 C  CG  . ASN   A 115 ? 0.1226 0.1393 0.1820 -0.0216 0.0246  0.0028  115 ASN   A CG  
2447 O  OD1 . ASN   A 115 ? 0.1336 0.2401 0.1996 -0.0182 0.0302  0.0229  115 ASN   A OD1 
2448 N  ND2 . ASN   A 115 ? 0.1301 0.1216 0.1969 -0.0130 0.0297  0.0102  115 ASN   A ND2 
2455 N  N   . PHE   A 116 ? 0.1115 0.1185 0.1843 -0.0021 0.0147  0.0222  116 PHE   A N   
2456 C  CA  . PHE   A 116 ? 0.1157 0.1264 0.1756 0.0013  0.0182  0.0190  116 PHE   A CA  
2457 C  C   . PHE   A 116 ? 0.1196 0.1239 0.1864 -0.0079 0.0135  0.0212  116 PHE   A C   
2458 O  O   . PHE   A 116 ? 0.1248 0.1352 0.1972 -0.0017 0.0087  0.0320  116 PHE   A O   
2459 C  CB  . PHE   A 116 ? 0.1175 0.1188 0.1902 -0.0047 0.0149  0.0209  116 PHE   A CB  
2460 C  CG  . PHE   A 116 ? 0.1183 0.1133 0.1710 -0.0069 0.0111  0.0160  116 PHE   A CG  
2461 C  CD1 . PHE   A 116 ? 0.1256 0.1153 0.1653 -0.0044 0.0146  0.0136  116 PHE   A CD1 
2462 C  CD2 . PHE   A 116 ? 0.1253 0.1280 0.1762 -0.0048 0.0195  0.0205  116 PHE   A CD2 
2463 C  CE1 . PHE   A 116 ? 0.1269 0.1129 0.1800 -0.0152 0.0064  0.0124  116 PHE   A CE1 
2464 C  CE2 . PHE   A 116 ? 0.1239 0.1191 0.1976 -0.0044 0.0103  0.0100  116 PHE   A CE2 
2465 C  CZ  . PHE   A 116 ? 0.1261 0.1029 0.1876 -0.0013 0.0031  0.0080  116 PHE   A CZ  
2475 N  N   . ASN   A 117 ? 0.1225 0.1196 0.1944 -0.0087 0.0126  0.0257  117 ASN   A N   
2476 C  CA  . ASN   A 117 ? 0.1217 0.1196 0.2088 -0.0046 0.0131  0.0266  117 ASN   A CA  
2477 C  C   . ASN   A 117 ? 0.1261 0.1280 0.2206 0.0007  0.0167  0.0277  117 ASN   A C   
2478 O  O   . ASN   A 117 ? 0.1283 0.1357 0.2280 -0.0063 -0.0048 0.0394  117 ASN   A O   
2479 C  CB  . ASN   A 117 ? 0.1237 0.1274 0.2030 -0.0006 0.0114  0.0312  117 ASN   A CB  
2480 C  CG  . ASN   A 117 ? 0.1189 0.1265 0.2084 0.0029  0.0123  0.0256  117 ASN   A CG  
2481 O  OD1 . ASN   A 117 ? 0.1195 0.1456 0.2237 -0.0071 0.0141  0.0189  117 ASN   A OD1 
2482 N  ND2 . ASN   A 117 ? 0.1165 0.1233 0.2046 -0.0008 0.0048  0.0251  117 ASN   A ND2 
2489 N  N   . GLN   A 118 ? 0.1261 0.1287 0.2163 -0.0040 0.0016  0.0356  118 GLN   A N   
2490 C  CA  . GLN   A 118 ? 0.1292 0.1416 0.2202 -0.0016 -0.0060 0.0266  118 GLN   A CA  
2491 C  C   . GLN   A 118 ? 0.1336 0.1533 0.2138 -0.0038 -0.0072 0.0339  118 GLN   A C   
2492 O  O   . GLN   A 118 ? 0.1313 0.1837 0.2280 0.0017  -0.0148 0.0145  118 GLN   A O   
2493 C  CB  . GLN   A 118 ? 0.1248 0.1392 0.2254 -0.0032 0.0045  0.0353  118 GLN   A CB  
2494 C  CG  . GLN   A 118 ? 0.1190 0.1433 0.2255 -0.0035 0.0072  0.0377  118 GLN   A CG  
2495 C  CD  . GLN   A 118 ? 0.1209 0.1487 0.2478 0.0022  0.0072  0.0299  118 GLN   A CD  
2496 O  OE1 . GLN   A 118 ? 0.1263 0.1586 0.2584 0.0105  0.0018  0.0241  118 GLN   A OE1 
2497 N  NE2 . GLN   A 118 ? 0.1334 0.1446 0.2394 0.0014  0.0045  0.0312  118 GLN   A NE2 
2506 N  N   . HIS   A 119 ? 0.1337 0.1440 0.2022 -0.0041 -0.0040 0.0361  119 HIS   A N   
2507 C  CA  . HIS   A 119 ? 0.1404 0.1506 0.1903 -0.0084 -0.0084 0.0437  119 HIS   A CA  
2508 C  C   . HIS   A 119 ? 0.1517 0.1615 0.1994 -0.0073 0.0048  0.0441  119 HIS   A C   
2509 O  O   . HIS   A 119 ? 0.1527 0.1706 0.2061 -0.0244 -0.0027 0.0523  119 HIS   A O   
2510 C  CB  . HIS   A 119 ? 0.1505 0.1513 0.2045 -0.0081 0.0146  0.0437  119 HIS   A CB  
2511 C  CG  . HIS   A 119 ? 0.1457 0.1580 0.2437 -0.0053 0.0139  0.0490  119 HIS   A CG  
2512 N  ND1 . HIS   A 119 ? 0.1591 0.1763 0.2952 -0.0136 0.0142  0.0336  119 HIS   A ND1 
2513 C  CD2 . HIS   A 119 ? 0.1542 0.1658 0.2603 0.0100  0.0292  0.0632  119 HIS   A CD2 
2514 C  CE1 . HIS   A 119 ? 0.1602 0.1732 0.2981 -0.0117 0.0278  0.0609  119 HIS   A CE1 
2515 N  NE2 . HIS   A 119 ? 0.1667 0.1734 0.2916 -0.0008 0.0407  0.0735  119 HIS   A NE2 
2523 N  N   . GLU   A 120 ? 0.1595 0.1861 0.2020 -0.0048 -0.0068 0.0728  120 GLU   A N   
2524 C  CA  . GLU   A 120 ? 0.1873 0.2220 0.2294 -0.0002 -0.0157 0.1092  120 GLU   A CA  
2525 C  C   . GLU   A 120 ? 0.1642 0.2025 0.1922 -0.0152 -0.0061 0.1030  120 GLU   A C   
2526 O  O   . GLU   A 120 ? 0.1637 0.1997 0.2119 -0.0204 -0.0105 0.0948  120 GLU   A O   
2527 C  CB  . GLU   A 120 ? 0.2600 0.2949 0.2927 0.0191  -0.0206 0.1524  120 GLU   A CB  
2528 C  CG  . GLU   A 120 ? 0.3592 0.3805 0.4097 0.0317  -0.0116 0.1532  120 GLU   A CG  
2529 C  CD  . GLU   A 120 ? 0.4402 0.4482 0.5298 0.0404  0.0001  0.1353  120 GLU   A CD  
2530 O  OE1 . GLU   A 120 ? 0.4694 0.4722 0.5647 0.0413  0.0036  0.1304  120 GLU   A OE1 
2531 O  OE2 . GLU   A 120 ? 0.5165 0.5165 0.5878 0.0421  0.0043  0.1261  120 GLU   A OE2 
2538 N  N   A VAL   A 121 ? 0.1533 0.2074 0.1710 -0.0151 0.0101  0.0819  121 VAL   A N   
2539 N  N   B VAL   A 121 ? 0.1604 0.2048 0.1792 -0.0140 0.0015  0.0828  121 VAL   A N   
2540 C  CA  A VAL   A 121 ? 0.1591 0.2115 0.1672 -0.0178 0.0159  0.0764  121 VAL   A CA  
2541 C  CA  B VAL   A 121 ? 0.1637 0.2058 0.1753 -0.0146 0.0059  0.0725  121 VAL   A CA  
2542 C  C   A VAL   A 121 ? 0.1491 0.1898 0.1541 -0.0260 0.0080  0.0595  121 VAL   A C   
2543 C  C   B VAL   A 121 ? 0.1518 0.1867 0.1629 -0.0219 0.0045  0.0602  121 VAL   A C   
2544 O  O   A VAL   A 121 ? 0.1534 0.1892 0.1643 -0.0325 -0.0095 0.0487  121 VAL   A O   
2545 O  O   B VAL   A 121 ? 0.1549 0.1877 0.1671 -0.0253 -0.0066 0.0580  121 VAL   A O   
2546 C  CB  A VAL   A 121 ? 0.1963 0.2412 0.2012 -0.0084 0.0213  0.0812  121 VAL   A CB  
2547 C  CB  B VAL   A 121 ? 0.1896 0.2286 0.1998 -0.0064 0.0080  0.0717  121 VAL   A CB  
2548 C  CG1 A VAL   A 121 ? 0.2012 0.2543 0.2006 -0.0038 0.0268  0.0825  121 VAL   A CG1 
2549 C  CG1 B VAL   A 121 ? 0.1932 0.2381 0.2002 -0.0038 0.0114  0.0721  121 VAL   A CG1 
2550 C  CG2 A VAL   A 121 ? 0.2166 0.2515 0.2392 -0.0139 0.0197  0.0709  121 VAL   A CG2 
2551 C  CG2 B VAL   A 121 ? 0.2052 0.2377 0.2251 -0.0071 0.0075  0.0634  121 VAL   A CG2 
2570 N  N   . LEU   A 122 ? 0.1399 0.1675 0.1607 -0.0226 0.0043  0.0530  122 LEU   A N   
2571 C  CA  . LEU   A 122 ? 0.1451 0.1515 0.1575 -0.0205 0.0206  0.0442  122 LEU   A CA  
2572 C  C   . LEU   A 122 ? 0.1427 0.1472 0.1606 -0.0301 0.0033  0.0393  122 LEU   A C   
2573 O  O   . LEU   A 122 ? 0.1421 0.1564 0.1886 -0.0299 0.0032  0.0431  122 LEU   A O   
2574 C  CB  . LEU   A 122 ? 0.1624 0.1539 0.1903 -0.0088 0.0101  0.0440  122 LEU   A CB  
2575 C  CG  . LEU   A 122 ? 0.1616 0.1573 0.1876 -0.0094 0.0185  0.0323  122 LEU   A CG  
2576 C  CD1 . LEU   A 122 ? 0.1809 0.1624 0.1876 -0.0123 0.0266  0.0335  122 LEU   A CD1 
2577 C  CD2 . LEU   A 122 ? 0.1540 0.1526 0.1848 -0.0111 0.0281  0.0362  122 LEU   A CD2 
2590 N  N   . LEU   A 123 ? 0.1316 0.1467 0.1549 -0.0276 0.0046  0.0326  123 LEU   A N   
2591 C  CA  . LEU   A 123 ? 0.1304 0.1466 0.1577 -0.0258 0.0062  0.0307  123 LEU   A CA  
2592 C  C   . LEU   A 123 ? 0.1305 0.1384 0.1481 -0.0207 0.0080  0.0381  123 LEU   A C   
2593 O  O   . LEU   A 123 ? 0.1288 0.1513 0.1531 -0.0258 0.0013  0.0383  123 LEU   A O   
2594 C  CB  . LEU   A 123 ? 0.1439 0.1578 0.1548 -0.0280 0.0190  0.0328  123 LEU   A CB  
2595 C  CG  . LEU   A 123 ? 0.1451 0.1688 0.1615 -0.0181 0.0130  0.0216  123 LEU   A CG  
2596 C  CD1 . LEU   A 123 ? 0.1488 0.1760 0.1834 -0.0111 0.0116  0.0128  123 LEU   A CD1 
2597 C  CD2 . LEU   A 123 ? 0.1602 0.1798 0.1598 -0.0146 0.0032  0.0178  123 LEU   A CD2 
2609 N  N   . ALA   A 124 ? 0.1286 0.1332 0.1402 -0.0151 0.0093  0.0253  124 ALA   A N   
2610 C  CA  . ALA   A 124 ? 0.1246 0.1290 0.1509 -0.0169 0.0068  0.0295  124 ALA   A CA  
2611 C  C   . ALA   A 124 ? 0.1188 0.1324 0.1476 -0.0134 0.0148  0.0275  124 ALA   A C   
2612 O  O   . ALA   A 124 ? 0.1208 0.1385 0.1628 -0.0139 0.0164  0.0385  124 ALA   A O   
2613 C  CB  . ALA   A 124 ? 0.1231 0.1282 0.1682 -0.0096 0.0047  0.0266  124 ALA   A CB  
2619 N  N   A PRO   A 125 ? 0.1087 0.1231 0.1439 -0.0105 0.0061  0.0397  125 PRO   A N   
2620 N  N   B PRO   A 125 ? 0.1277 0.1353 0.1344 -0.0135 0.0085  0.0292  125 PRO   A N   
2621 C  CA  A PRO   A 125 ? 0.1111 0.1191 0.1455 -0.0031 0.0052  0.0269  125 PRO   A CA  
2622 C  CA  B PRO   A 125 ? 0.1364 0.1352 0.1300 -0.0095 0.0065  0.0217  125 PRO   A CA  
2623 C  C   A PRO   A 125 ? 0.1021 0.1209 0.1498 -0.0044 0.0057  0.0276  125 PRO   A C   
2624 C  C   B PRO   A 125 ? 0.1360 0.1356 0.1376 -0.0015 0.0090  0.0191  125 PRO   A C   
2625 O  O   A PRO   A 125 ? 0.1062 0.1231 0.1562 0.0007  0.0053  0.0223  125 PRO   A O   
2626 O  O   B PRO   A 125 ? 0.1412 0.1373 0.1638 0.0015  0.0092  0.0215  125 PRO   A O   
2627 C  CB  A PRO   A 125 ? 0.1249 0.1163 0.1451 -0.0045 0.0064  0.0181  125 PRO   A CB  
2628 C  CB  B PRO   A 125 ? 0.1404 0.1349 0.1331 -0.0101 0.0121  0.0166  125 PRO   A CB  
2629 C  CG  A PRO   A 125 ? 0.1205 0.1139 0.1533 -0.0080 0.0156  0.0309  125 PRO   A CG  
2630 C  CG  B PRO   A 125 ? 0.1431 0.1391 0.1423 -0.0148 0.0103  0.0188  125 PRO   A CG  
2631 C  CD  A PRO   A 125 ? 0.1125 0.1260 0.1548 -0.0131 0.0102  0.0364  125 PRO   A CD  
2632 C  CD  B PRO   A 125 ? 0.1350 0.1423 0.1406 -0.0164 0.0107  0.0236  125 PRO   A CD  
2647 N  N   A LEU   A 126 ? 0.1018 0.1236 0.1595 -0.0010 0.0052  0.0269  126 LEU   A N   
2648 N  N   B LEU   A 126 ? 0.1411 0.1352 0.1471 -0.0018 0.0087  0.0124  126 LEU   A N   
2649 C  CA  A LEU   A 126 ? 0.1135 0.1250 0.1665 -0.0014 0.0045  0.0233  126 LEU   A CA  
2650 C  CA  B LEU   A 126 ? 0.1444 0.1301 0.1550 -0.0038 0.0127  0.0072  126 LEU   A CA  
2651 C  C   A LEU   A 126 ? 0.1172 0.1182 0.1641 -0.0000 0.0014  0.0211  126 LEU   A C   
2652 C  C   B LEU   A 126 ? 0.1342 0.1227 0.1475 0.0036  0.0155  0.0035  126 LEU   A C   
2653 O  O   A LEU   A 126 ? 0.1283 0.1241 0.1940 0.0104  0.0213  0.0279  126 LEU   A O   
2654 O  O   B LEU   A 126 ? 0.1441 0.1224 0.1527 0.0001  0.0131  0.0195  126 LEU   A O   
2655 C  CB  A LEU   A 126 ? 0.1186 0.1200 0.1730 -0.0053 0.0072  0.0187  126 LEU   A CB  
2656 C  CB  B LEU   A 126 ? 0.1561 0.1412 0.1829 -0.0148 0.0103  0.0013  126 LEU   A CB  
2657 C  CG  A LEU   A 126 ? 0.1165 0.1235 0.1840 -0.0007 0.0147  0.0124  126 LEU   A CG  
2658 C  CG  B LEU   A 126 ? 0.1614 0.1508 0.2076 -0.0185 0.0109  -0.0009 126 LEU   A CG  
2659 C  CD1 A LEU   A 126 ? 0.1236 0.1366 0.2212 -0.0082 0.0137  0.0228  126 LEU   A CD1 
2660 C  CD1 B LEU   A 126 ? 0.1655 0.1505 0.2163 -0.0191 0.0090  -0.0082 126 LEU   A CD1 
2661 C  CD2 A LEU   A 126 ? 0.1259 0.1249 0.1758 -0.0059 0.0177  0.0181  126 LEU   A CD2 
2662 C  CD2 B LEU   A 126 ? 0.1581 0.1556 0.2198 -0.0169 0.0057  0.0046  126 LEU   A CD2 
2685 N  N   A LEU   A 127 ? 0.1259 0.1232 0.1559 -0.0000 0.0081  0.0132  127 LEU   A N   
2686 N  N   B LEU   A 127 ? 0.1244 0.1218 0.1361 0.0080  0.0204  0.0035  127 LEU   A N   
2687 C  CA  A LEU   A 127 ? 0.1295 0.1252 0.1386 -0.0044 -0.0004 0.0054  127 LEU   A CA  
2688 C  CA  B LEU   A 127 ? 0.1218 0.1290 0.1289 0.0058  0.0097  0.0128  127 LEU   A CA  
2689 C  C   A LEU   A 127 ? 0.1224 0.1154 0.1398 -0.0024 -0.0041 0.0046  127 LEU   A C   
2690 C  C   B LEU   A 127 ? 0.1230 0.1311 0.1355 0.0073  0.0105  0.0001  127 LEU   A C   
2691 O  O   A LEU   A 127 ? 0.1253 0.1117 0.1435 -0.0157 -0.0053 0.0157  127 LEU   A O   
2692 O  O   B LEU   A 127 ? 0.1284 0.1393 0.1381 0.0001  0.0172  -0.0021 127 LEU   A O   
2693 C  CB  A LEU   A 127 ? 0.1364 0.1313 0.1534 0.0101  0.0036  0.0096  127 LEU   A CB  
2694 C  CB  B LEU   A 127 ? 0.1235 0.1386 0.1296 0.0051  -0.0028 0.0083  127 LEU   A CB  
2695 C  CG  A LEU   A 127 ? 0.1414 0.1344 0.1617 0.0089  -0.0020 0.0104  127 LEU   A CG  
2696 C  CG  B LEU   A 127 ? 0.1218 0.1502 0.1300 0.0134  -0.0167 0.0153  127 LEU   A CG  
2697 C  CD1 A LEU   A 127 ? 0.1390 0.1241 0.1686 -0.0007 0.0028  0.0010  127 LEU   A CD1 
2698 C  CD1 B LEU   A 127 ? 0.1192 0.1509 0.1440 0.0209  0.0009  0.0245  127 LEU   A CD1 
2699 C  CD2 A LEU   A 127 ? 0.1476 0.1333 0.1883 0.0200  -0.0092 0.0157  127 LEU   A CD2 
2700 C  CD2 B LEU   A 127 ? 0.1291 0.1637 0.1434 0.0177  -0.0308 -0.0052 127 LEU   A CD2 
2723 N  N   A SER   A 128 ? 0.1211 0.1198 0.1484 -0.0086 -0.0058 0.0118  128 SER   A N   
2724 N  N   B SER   A 128 ? 0.1211 0.1311 0.1441 -0.0015 0.0017  0.0072  128 SER   A N   
2725 C  CA  A SER   A 128 ? 0.1379 0.1252 0.1420 -0.0027 -0.0048 0.0183  128 SER   A CA  
2726 C  CA  B SER   A 128 ? 0.1231 0.1241 0.1344 -0.0069 -0.0070 0.0117  128 SER   A CA  
2727 C  C   A SER   A 128 ? 0.1438 0.1305 0.1410 0.0025  0.0031  0.0206  128 SER   A C   
2728 C  C   B SER   A 128 ? 0.1166 0.1173 0.1288 -0.0053 -0.0197 0.0168  128 SER   A C   
2729 O  O   A SER   A 128 ? 0.1640 0.1474 0.1584 0.0012  0.0174  0.0192  128 SER   A O   
2730 O  O   B SER   A 128 ? 0.1102 0.1174 0.1348 -0.0036 -0.0257 0.0106  128 SER   A O   
2731 C  CB  A SER   A 128 ? 0.1390 0.1385 0.1442 0.0001  -0.0033 0.0184  128 SER   A CB  
2732 C  CB  B SER   A 128 ? 0.1246 0.1313 0.1341 -0.0090 -0.0021 0.0119  128 SER   A CB  
2733 O  OG  A SER   A 128 ? 0.1414 0.1441 0.1538 -0.0002 0.0033  0.0092  128 SER   A OG  
2734 O  OG  B SER   A 128 ? 0.1254 0.1395 0.1357 -0.0141 0.0077  0.0182  128 SER   A OG  
2745 N  N   A ALA   A 129 ? 0.1426 0.1431 0.1682 0.0032  0.0005  0.0261  129 ALA   A N   
2746 N  N   B ALA   A 129 ? 0.1207 0.1237 0.1423 -0.0026 -0.0155 0.0247  129 ALA   A N   
2747 C  CA  A ALA   A 129 ? 0.1352 0.1450 0.1733 0.0014  0.0031  0.0288  129 ALA   A CA  
2748 C  CA  B ALA   A 129 ? 0.1203 0.1261 0.1437 -0.0039 -0.0162 0.0313  129 ALA   A CA  
2749 C  C   A ALA   A 129 ? 0.1409 0.1413 0.1659 -0.0020 -0.0065 0.0104  129 ALA   A C   
2750 C  C   B ALA   A 129 ? 0.1262 0.1348 0.1494 -0.0039 -0.0254 0.0223  129 ALA   A C   
2751 O  O   A ALA   A 129 ? 0.1470 0.1443 0.1624 -0.0052 0.0017  0.0166  129 ALA   A O   
2752 O  O   B ALA   A 129 ? 0.1281 0.1381 0.1376 -0.0030 -0.0248 0.0243  129 ALA   A O   
2753 C  CB  A ALA   A 129 ? 0.1407 0.1640 0.1965 0.0015  -0.0011 0.0291  129 ALA   A CB  
2754 C  CB  B ALA   A 129 ? 0.1184 0.1291 0.1334 -0.0082 -0.0217 0.0312  129 ALA   A CB  
2765 N  N   A GLY   A 130 ? 0.1479 0.1376 0.1864 0.0019  -0.0073 0.0088  130 GLY   A N   
2766 N  N   B GLY   A 130 ? 0.1318 0.1369 0.1647 -0.0010 -0.0199 0.0197  130 GLY   A N   
2767 C  CA  A GLY   A 130 ? 0.1675 0.1366 0.1768 0.0051  -0.0086 0.0077  130 GLY   A CA  
2768 C  CA  B GLY   A 130 ? 0.1454 0.1396 0.1594 0.0033  -0.0104 0.0121  130 GLY   A CA  
2769 C  C   A GLY   A 130 ? 0.1708 0.1301 0.1662 0.0010  -0.0194 0.0066  130 GLY   A C   
2770 C  C   B GLY   A 130 ? 0.1481 0.1397 0.1537 0.0041  -0.0081 0.0059  130 GLY   A C   
2771 O  O   A GLY   A 130 ? 0.1741 0.1267 0.1831 0.0028  -0.0313 0.0035  130 GLY   A O   
2772 O  O   B GLY   A 130 ? 0.1532 0.1406 0.1578 0.0044  -0.0033 0.0037  130 GLY   A O   
2779 N  N   A ILE   A 131 ? 0.1862 0.1256 0.1596 -0.0095 -0.0193 0.0175  131 ILE   A N   
2780 N  N   B ILE   A 131 ? 0.1590 0.1384 0.1546 0.0026  -0.0218 0.0114  131 ILE   A N   
2781 C  CA  A ILE   A 131 ? 0.2009 0.1315 0.1424 -0.0178 -0.0293 0.0136  131 ILE   A CA  
2782 C  CA  B ILE   A 131 ? 0.1742 0.1428 0.1517 -0.0011 -0.0354 0.0122  131 ILE   A CA  
2783 C  C   A ILE   A 131 ? 0.1809 0.1360 0.1492 -0.0163 -0.0141 0.0272  131 ILE   A C   
2784 C  C   B ILE   A 131 ? 0.1697 0.1460 0.1585 0.0022  -0.0229 0.0190  131 ILE   A C   
2785 O  O   A ILE   A 131 ? 0.1851 0.1424 0.1654 -0.0113 -0.0169 0.0219  131 ILE   A O   
2786 O  O   B ILE   A 131 ? 0.1686 0.1473 0.1774 0.0073  -0.0267 0.0249  131 ILE   A O   
2787 C  CB  A ILE   A 131 ? 0.2259 0.1420 0.1467 -0.0239 -0.0395 0.0064  131 ILE   A CB  
2788 C  CB  B ILE   A 131 ? 0.1898 0.1553 0.1494 -0.0095 -0.0623 0.0092  131 ILE   A CB  
2789 C  CG1 A ILE   A 131 ? 0.2286 0.1745 0.1685 -0.0344 -0.0392 0.0144  131 ILE   A CG1 
2790 C  CG1 B ILE   A 131 ? 0.1957 0.1741 0.1624 -0.0160 -0.0664 0.0115  131 ILE   A CG1 
2791 C  CG2 A ILE   A 131 ? 0.2364 0.1282 0.1493 -0.0175 -0.0324 -0.0134 131 ILE   A CG2 
2792 C  CG2 B ILE   A 131 ? 0.1965 0.1543 0.1573 -0.0057 -0.0708 0.0039  131 ILE   A CG2 
2793 C  CD1 A ILE   A 131 ? 0.2292 0.1835 0.1922 -0.0348 -0.0476 0.0095  131 ILE   A CD1 
2794 C  CD1 B ILE   A 131 ? 0.1998 0.1796 0.1741 -0.0174 -0.0711 0.0103  131 ILE   A CD1 
2817 N  N   A PHE   A 132 ? 0.1624 0.1340 0.1523 -0.0119 -0.0084 0.0264  132 PHE   A N   
2818 N  N   B PHE   A 132 ? 0.1683 0.1489 0.1592 0.0011  -0.0140 0.0134  132 PHE   A N   
2819 C  CA  A PHE   A 132 ? 0.1636 0.1396 0.1518 -0.0156 -0.0086 0.0144  132 PHE   A CA  
2820 C  CA  B PHE   A 132 ? 0.1725 0.1534 0.1518 -0.0022 -0.0097 0.0024  132 PHE   A CA  
2821 C  C   A PHE   A 132 ? 0.1643 0.1497 0.1516 -0.0186 -0.0113 0.0172  132 PHE   A C   
2822 C  C   B PHE   A 132 ? 0.1767 0.1631 0.1552 -0.0055 -0.0145 0.0077  132 PHE   A C   
2823 O  O   A PHE   A 132 ? 0.1661 0.1553 0.1526 -0.0285 -0.0116 0.0147  132 PHE   A O   
2824 O  O   B PHE   A 132 ? 0.1854 0.1710 0.1654 -0.0148 -0.0132 -0.0008 132 PHE   A O   
2825 C  CB  A PHE   A 132 ? 0.1586 0.1337 0.1383 -0.0151 -0.0164 0.0237  132 PHE   A CB  
2826 C  CB  B PHE   A 132 ? 0.1703 0.1457 0.1369 -0.0005 -0.0071 -0.0068 132 PHE   A CB  
2827 C  CG  A PHE   A 132 ? 0.1549 0.1313 0.1392 -0.0062 -0.0219 0.0212  132 PHE   A CG  
2828 C  CG  B PHE   A 132 ? 0.1652 0.1402 0.1296 0.0054  -0.0038 -0.0136 132 PHE   A CG  
2829 C  CD1 A PHE   A 132 ? 0.1532 0.1472 0.1592 -0.0010 -0.0198 0.0053  132 PHE   A CD1 
2830 C  CD1 B PHE   A 132 ? 0.1642 0.1485 0.1388 0.0092  0.0002  -0.0227 132 PHE   A CD1 
2831 C  CD2 A PHE   A 132 ? 0.1597 0.1379 0.1567 -0.0015 -0.0255 0.0174  132 PHE   A CD2 
2832 C  CD2 B PHE   A 132 ? 0.1674 0.1382 0.1368 0.0109  0.0013  -0.0255 132 PHE   A CD2 
2833 C  CE1 A PHE   A 132 ? 0.1576 0.1518 0.1729 -0.0059 -0.0224 -0.0001 132 PHE   A CE1 
2834 C  CE1 B PHE   A 132 ? 0.1666 0.1509 0.1481 0.0093  -0.0034 -0.0235 132 PHE   A CE1 
2835 C  CE2 A PHE   A 132 ? 0.1579 0.1427 0.1689 -0.0017 -0.0280 0.0176  132 PHE   A CE2 
2836 C  CE2 B PHE   A 132 ? 0.1663 0.1437 0.1480 0.0167  0.0003  -0.0275 132 PHE   A CE2 
2837 C  CZ  A PHE   A 132 ? 0.1553 0.1447 0.1717 -0.0143 -0.0298 0.0120  132 PHE   A CZ  
2838 C  CZ  B PHE   A 132 ? 0.1662 0.1465 0.1539 0.0095  -0.0028 -0.0207 132 PHE   A CZ  
2857 N  N   A GLY   A 133 ? 0.1665 0.1558 0.1553 -0.0181 -0.0328 0.0255  133 GLY   A N   
2858 N  N   B GLY   A 133 ? 0.1754 0.1632 0.1559 -0.0055 -0.0259 0.0163  133 GLY   A N   
2859 C  CA  A GLY   A 133 ? 0.1748 0.1683 0.1655 -0.0270 -0.0398 0.0147  133 GLY   A CA  
2860 C  CA  B GLY   A 133 ? 0.1765 0.1671 0.1565 -0.0074 -0.0226 0.0097  133 GLY   A CA  
2861 C  C   A GLY   A 133 ? 0.1764 0.1765 0.1594 -0.0230 -0.0447 0.0049  133 GLY   A C   
2862 C  C   B GLY   A 133 ? 0.1738 0.1713 0.1507 -0.0001 -0.0211 -0.0047 133 GLY   A C   
2863 O  O   A GLY   A 133 ? 0.1835 0.1927 0.1642 -0.0222 -0.0292 -0.0159 133 GLY   A O   
2864 O  O   B GLY   A 133 ? 0.1719 0.1807 0.1457 0.0089  -0.0154 -0.0247 133 GLY   A O   
2871 N  N   A ALA   A 134 ? 0.1763 0.1658 0.1573 -0.0216 -0.0362 0.0048  134 ALA   A N   
2872 N  N   B ALA   A 134 ? 0.1763 0.1640 0.1571 -0.0039 -0.0167 -0.0054 134 ALA   A N   
2873 C  CA  A ALA   A 134 ? 0.1706 0.1661 0.1731 -0.0195 -0.0307 0.0038  134 ALA   A CA  
2874 C  CA  B ALA   A 134 ? 0.1737 0.1576 0.1676 -0.0024 -0.0124 -0.0092 134 ALA   A CA  
2875 C  C   A ALA   A 134 ? 0.1697 0.1679 0.1705 -0.0142 -0.0264 0.0080  134 ALA   A C   
2876 C  C   B ALA   A 134 ? 0.1701 0.1506 0.1666 0.0009  -0.0125 -0.0119 134 ALA   A C   
2877 O  O   A ALA   A 134 ? 0.1906 0.1738 0.1772 -0.0184 -0.0196 0.0072  134 ALA   A O   
2878 O  O   B ALA   A 134 ? 0.1738 0.1522 0.1627 0.0016  -0.0044 -0.0156 134 ALA   A O   
2879 C  CB  A ALA   A 134 ? 0.1777 0.1647 0.1998 -0.0170 -0.0296 -0.0049 134 ALA   A CB  
2880 C  CB  B ALA   A 134 ? 0.1772 0.1566 0.1814 -0.0028 -0.0121 -0.0118 134 ALA   A CB  
2891 N  N   A ASP   A 135 ? 0.1674 0.1632 0.1807 -0.0060 -0.0234 0.0009  135 ASP   A N   
2892 N  N   B ASP   A 135 ? 0.1721 0.1495 0.1811 -0.0048 -0.0143 -0.0021 135 ASP   A N   
2893 C  CA  A ASP   A 135 ? 0.1659 0.1713 0.1973 -0.0132 -0.0309 0.0022  135 ASP   A CA  
2894 C  CA  B ASP   A 135 ? 0.1723 0.1484 0.1970 -0.0075 -0.0222 -0.0046 135 ASP   A CA  
2895 C  C   A ASP   A 135 ? 0.1572 0.1585 0.2040 -0.0090 -0.0167 0.0159  135 ASP   A C   
2896 C  C   B ASP   A 135 ? 0.1618 0.1386 0.1945 -0.0015 -0.0197 -0.0025 135 ASP   A C   
2897 O  O   A ASP   A 135 ? 0.1482 0.1503 0.2184 -0.0073 -0.0157 0.0231  135 ASP   A O   
2898 O  O   B ASP   A 135 ? 0.1562 0.1343 0.1906 -0.0002 -0.0183 0.0047  135 ASP   A O   
2899 C  CB  A ASP   A 135 ? 0.1885 0.2015 0.2351 -0.0311 -0.0457 -0.0111 135 ASP   A CB  
2900 C  CB  B ASP   A 135 ? 0.1860 0.1630 0.2122 -0.0103 -0.0376 -0.0104 135 ASP   A CB  
2901 C  CG  A ASP   A 135 ? 0.2039 0.2237 0.2645 -0.0501 -0.0552 -0.0152 135 ASP   A CG  
2902 C  CG  B ASP   A 135 ? 0.1976 0.1841 0.2392 -0.0119 -0.0428 -0.0080 135 ASP   A CG  
2903 O  OD1 A ASP   A 135 ? 0.1965 0.2308 0.2604 -0.0609 -0.0575 0.0052  135 ASP   A OD1 
2904 O  OD1 B ASP   A 135 ? 0.2000 0.1860 0.2451 -0.0072 -0.0434 -0.0059 135 ASP   A OD1 
2905 O  OD2 A ASP   A 135 ? 0.2284 0.2434 0.3097 -0.0510 -0.0378 -0.0159 135 ASP   A OD2 
2906 O  OD2 B ASP   A 135 ? 0.2071 0.1971 0.2670 -0.0192 -0.0418 -0.0078 135 ASP   A OD2 
2915 N  N   A PRO   A 136 ? 0.1503 0.1505 0.2023 -0.0018 -0.0072 0.0251  136 PRO   A N   
2916 N  N   B PRO   A 136 ? 0.1570 0.1309 0.1939 0.0056  -0.0104 -0.0114 136 PRO   A N   
2917 C  CA  A PRO   A 136 ? 0.1483 0.1554 0.2177 -0.0059 -0.0021 0.0134  136 PRO   A CA  
2918 C  CA  B PRO   A 136 ? 0.1514 0.1432 0.1901 -0.0007 -0.0029 -0.0264 136 PRO   A CA  
2919 C  C   A PRO   A 136 ? 0.1301 0.1446 0.2198 0.0036  -0.0039 0.0074  136 PRO   A C   
2920 C  C   B PRO   A 136 ? 0.1360 0.1489 0.1725 0.0043  -0.0040 -0.0186 136 PRO   A C   
2921 O  O   A PRO   A 136 ? 0.1264 0.1481 0.2167 -0.0083 -0.0030 0.0048  136 PRO   A O   
2922 O  O   B PRO   A 136 ? 0.1252 0.1416 0.1496 0.0129  0.0128  -0.0139 136 PRO   A O   
2923 C  CB  A PRO   A 136 ? 0.1653 0.1567 0.2248 -0.0036 0.0019  0.0100  136 PRO   A CB  
2924 C  CB  B PRO   A 136 ? 0.1622 0.1405 0.1998 0.0009  -0.0003 -0.0344 136 PRO   A CB  
2925 C  CG  A PRO   A 136 ? 0.1746 0.1592 0.2290 0.0066  -0.0016 0.0081  136 PRO   A CG  
2926 C  CG  B PRO   A 136 ? 0.1678 0.1392 0.2068 0.0060  -0.0011 -0.0283 136 PRO   A CG  
2927 C  CD  A PRO   A 136 ? 0.1658 0.1563 0.2158 0.0070  -0.0092 0.0197  136 PRO   A CD  
2928 C  CD  B PRO   A 136 ? 0.1630 0.1276 0.1972 0.0098  0.0013  -0.0141 136 PRO   A CD  
2943 N  N   A ILE   A 137 ? 0.1275 0.1417 0.2315 0.0006  -0.0151 0.0176  137 ILE   A N   
2944 N  N   B ILE   A 137 ? 0.1368 0.1540 0.1878 0.0001  -0.0094 -0.0111 137 ILE   A N   
2945 C  CA  A ILE   A 137 ? 0.1347 0.1495 0.2373 -0.0104 -0.0198 0.0273  137 ILE   A CA  
2946 C  CA  B ILE   A 137 ? 0.1383 0.1596 0.1972 0.0023  -0.0053 -0.0085 137 ILE   A CA  
2947 C  C   A ILE   A 137 ? 0.1360 0.1508 0.2149 -0.0167 -0.0209 0.0258  137 ILE   A C   
2948 C  C   B ILE   A 137 ? 0.1366 0.1688 0.1880 -0.0050 0.0057  -0.0045 137 ILE   A C   
2949 O  O   A ILE   A 137 ? 0.1478 0.1461 0.2164 -0.0180 -0.0194 0.0231  137 ILE   A O   
2950 O  O   B ILE   A 137 ? 0.1332 0.1711 0.1905 0.0004  0.0096  -0.0012 137 ILE   A O   
2951 C  CB  A ILE   A 137 ? 0.1430 0.1519 0.2636 -0.0115 -0.0318 0.0243  137 ILE   A CB  
2952 C  CB  B ILE   A 137 ? 0.1429 0.1541 0.2186 0.0053  -0.0149 -0.0039 137 ILE   A CB  
2953 C  CG1 A ILE   A 137 ? 0.1512 0.1691 0.2951 -0.0126 -0.0349 0.0289  137 ILE   A CG1 
2954 C  CG1 B ILE   A 137 ? 0.1490 0.1594 0.2484 0.0119  -0.0317 0.0015  137 ILE   A CG1 
2955 C  CG2 A ILE   A 137 ? 0.1529 0.1537 0.2590 -0.0132 -0.0382 0.0059  137 ILE   A CG2 
2956 C  CG2 B ILE   A 137 ? 0.1481 0.1450 0.2182 0.0046  -0.0101 -0.0076 137 ILE   A CG2 
2957 C  CD1 A ILE   A 137 ? 0.1689 0.1811 0.3115 -0.0056 -0.0339 0.0251  137 ILE   A CD1 
2958 C  CD1 B ILE   A 137 ? 0.1579 0.1599 0.2685 0.0117  -0.0323 0.0050  137 ILE   A CD1 
2981 N  N   A HIS   A 138 ? 0.1307 0.1680 0.2138 -0.0108 -0.0142 0.0178  138 HIS   A N   
2982 N  N   B HIS   A 138 ? 0.1371 0.1777 0.1884 -0.0069 0.0169  -0.0061 138 HIS   A N   
2983 C  CA  A HIS   A 138 ? 0.1320 0.1802 0.2008 -0.0117 -0.0059 0.0215  138 HIS   A CA  
2984 C  CA  B HIS   A 138 ? 0.1374 0.1745 0.1813 -0.0070 0.0195  0.0035  138 HIS   A CA  
2985 C  C   A HIS   A 138 ? 0.1256 0.1740 0.2020 -0.0065 -0.0146 0.0208  138 HIS   A C   
2986 C  C   B HIS   A 138 ? 0.1324 0.1690 0.1892 -0.0023 0.0104  0.0190  138 HIS   A C   
2987 O  O   A HIS   A 138 ? 0.1376 0.1796 0.2033 -0.0095 -0.0161 0.0163  138 HIS   A O   
2988 O  O   B HIS   A 138 ? 0.1413 0.1720 0.1926 -0.0034 0.0126  0.0230  138 HIS   A O   
2989 C  CB  A HIS   A 138 ? 0.1544 0.2020 0.2015 -0.0081 -0.0165 0.0213  138 HIS   A CB  
2990 C  CB  B HIS   A 138 ? 0.1434 0.1801 0.1763 -0.0009 0.0183  -0.0116 138 HIS   A CB  
2991 C  CG  A HIS   A 138 ? 0.1758 0.2151 0.2145 -0.0141 -0.0171 0.0121  138 HIS   A CG  
2992 C  CG  B HIS   A 138 ? 0.1531 0.1802 0.1846 0.0006  0.0127  -0.0298 138 HIS   A CG  
2993 N  ND1 A HIS   A 138 ? 0.1895 0.2255 0.2383 -0.0186 -0.0151 -0.0022 138 HIS   A ND1 
2994 N  ND1 B HIS   A 138 ? 0.1628 0.1827 0.2054 0.0022  0.0046  -0.0377 138 HIS   A ND1 
2995 C  CD2 A HIS   A 138 ? 0.1824 0.2230 0.2205 -0.0103 -0.0156 0.0203  138 HIS   A CD2 
2996 C  CD2 B HIS   A 138 ? 0.1571 0.1768 0.1916 0.0054  0.0138  -0.0342 138 HIS   A CD2 
2997 C  CE1 A HIS   A 138 ? 0.1951 0.2303 0.2437 -0.0112 -0.0206 0.0056  138 HIS   A CE1 
2998 C  CE1 B HIS   A 138 ? 0.1642 0.1759 0.2078 0.0090  -0.0045 -0.0395 138 HIS   A CE1 
2999 N  NE2 A HIS   A 138 ? 0.1907 0.2306 0.2297 -0.0075 -0.0150 0.0151  138 HIS   A NE2 
3000 N  NE2 B HIS   A 138 ? 0.1633 0.1757 0.1986 0.0083  0.0016  -0.0388 138 HIS   A NE2 
3015 N  N   . SER   A 139 ? 0.1251 0.1613 0.1998 -0.0048 -0.0050 0.0276  139 SER   A N   
3016 C  CA  . SER   A 139 ? 0.1219 0.1580 0.1990 -0.0096 0.0040  0.0348  139 SER   A CA  
3017 C  C   . SER   A 139 ? 0.1160 0.1514 0.1993 -0.0073 0.0120  0.0199  139 SER   A C   
3018 O  O   . SER   A 139 ? 0.1112 0.1484 0.2125 -0.0125 0.0072  0.0240  139 SER   A O   
3019 C  CB  . SER   A 139 ? 0.1205 0.1572 0.1889 -0.0178 -0.0037 0.0369  139 SER   A CB  
3020 O  OG  . SER   A 139 ? 0.1341 0.1573 0.1866 -0.0220 -0.0141 0.0397  139 SER   A OG  
3027 N  N   . LEU   A 140 ? 0.1180 0.1513 0.1810 -0.0079 0.0036  0.0350  140 LEU   A N   
3028 C  CA  . LEU   A 140 ? 0.1178 0.1446 0.1876 -0.0129 0.0042  0.0285  140 LEU   A CA  
3029 C  C   . LEU   A 140 ? 0.1173 0.1527 0.1918 -0.0196 0.0029  0.0332  140 LEU   A C   
3030 O  O   . LEU   A 140 ? 0.1272 0.1524 0.2088 -0.0087 0.0013  0.0359  140 LEU   A O   
3031 C  CB  . LEU   A 140 ? 0.1237 0.1494 0.1996 -0.0157 0.0062  0.0309  140 LEU   A CB  
3032 C  CG  . LEU   A 140 ? 0.1236 0.1672 0.2061 -0.0192 0.0069  0.0443  140 LEU   A CG  
3033 C  CD1 . LEU   A 140 ? 0.1283 0.1672 0.2168 -0.0122 -0.0003 0.0384  140 LEU   A CD1 
3034 C  CD2 . LEU   A 140 ? 0.1287 0.1858 0.2128 -0.0111 0.0179  0.0479  140 LEU   A CD2 
3046 N  N   . ARG   A 141 ? 0.1215 0.1539 0.2052 -0.0133 -0.0010 0.0267  141 ARG   A N   
3047 C  CA  . ARG   A 141 ? 0.1356 0.1651 0.2262 -0.0223 -0.0099 0.0130  141 ARG   A CA  
3048 C  C   . ARG   A 141 ? 0.1428 0.1496 0.2104 -0.0148 -0.0078 0.0044  141 ARG   A C   
3049 O  O   . ARG   A 141 ? 0.1360 0.1484 0.2293 -0.0154 0.0020  0.0066  141 ARG   A O   
3050 C  CB  . ARG   A 141 ? 0.1478 0.1963 0.2398 -0.0274 -0.0163 0.0024  141 ARG   A CB  
3051 C  CG  . ARG   A 141 ? 0.1860 0.2356 0.2657 -0.0303 -0.0019 -0.0071 141 ARG   A CG  
3052 C  CD  . ARG   A 141 ? 0.2252 0.2617 0.2982 -0.0374 -0.0009 -0.0239 141 ARG   A CD  
3053 N  NE  . ARG   A 141 ? 0.2251 0.2871 0.3119 -0.0344 -0.0097 -0.0244 141 ARG   A NE  
3054 C  CZ  . ARG   A 141 ? 0.2278 0.3133 0.3169 -0.0489 -0.0003 -0.0202 141 ARG   A CZ  
3055 N  NH1 . ARG   A 141 ? 0.2087 0.3099 0.3032 -0.0644 0.0220  -0.0341 141 ARG   A NH1 
3056 N  NH2 . ARG   A 141 ? 0.2387 0.3370 0.3382 -0.0437 -0.0164 -0.0098 141 ARG   A NH2 
3070 N  N   . VAL   A 142 ? 0.1324 0.1473 0.1946 -0.0081 0.0009  0.0071  142 VAL   A N   
3071 C  CA  . VAL   A 142 ? 0.1334 0.1446 0.1988 -0.0028 0.0151  0.0063  142 VAL   A CA  
3072 C  C   . VAL   A 142 ? 0.1130 0.1345 0.2002 -0.0135 0.0061  0.0093  142 VAL   A C   
3073 O  O   . VAL   A 142 ? 0.1169 0.1384 0.2100 0.0007  0.0080  0.0131  142 VAL   A O   
3074 C  CB  . VAL   A 142 ? 0.1410 0.1524 0.1915 -0.0067 0.0173  0.0155  142 VAL   A CB  
3075 C  CG1 . VAL   A 142 ? 0.1373 0.1509 0.2036 -0.0145 0.0155  0.0105  142 VAL   A CG1 
3076 C  CG2 . VAL   A 142 ? 0.1542 0.1765 0.2178 -0.0008 0.0149  0.0153  142 VAL   A CG2 
3086 N  N   . CYS   A 143 ? 0.1213 0.1340 0.1927 -0.0138 0.0035  0.0168  143 CYS   A N   
3087 C  CA  . CYS   A 143 ? 0.1185 0.1364 0.1981 -0.0134 0.0056  0.0165  143 CYS   A CA  
3088 C  C   . CYS   A 143 ? 0.1182 0.1369 0.2040 -0.0158 0.0054  0.0286  143 CYS   A C   
3089 O  O   . CYS   A 143 ? 0.1145 0.1451 0.2042 -0.0119 0.0024  0.0303  143 CYS   A O   
3090 C  CB  . CYS   A 143 ? 0.1285 0.1450 0.2005 -0.0139 0.0055  0.0328  143 CYS   A CB  
3091 S  SG  . CYS   A 143 ? 0.1447 0.1491 0.1850 0.0003  0.0115  0.0210  143 CYS   A SG  
3097 N  N   . VAL   A 144 ? 0.1197 0.1419 0.2207 -0.0078 0.0060  0.0361  144 VAL   A N   
3098 C  CA  . VAL   A 144 ? 0.1253 0.1536 0.2424 -0.0145 0.0154  0.0357  144 VAL   A CA  
3099 C  C   . VAL   A 144 ? 0.1281 0.1459 0.2469 -0.0185 -0.0099 0.0268  144 VAL   A C   
3100 O  O   . VAL   A 144 ? 0.1455 0.1500 0.2511 -0.0073 -0.0083 0.0324  144 VAL   A O   
3101 C  CB  . VAL   A 144 ? 0.1482 0.1827 0.3074 -0.0060 0.0349  0.0416  144 VAL   A CB  
3102 C  CG1 . VAL   A 144 ? 0.1717 0.2011 0.3491 -0.0193 0.0194  0.0436  144 VAL   A CG1 
3103 C  CG2 . VAL   A 144 ? 0.1261 0.1878 0.3190 -0.0052 0.0420  0.0552  144 VAL   A CG2 
3113 N  N   . ASP   A 145 ? 0.1340 0.1378 0.2550 -0.0173 -0.0019 0.0197  145 ASP   A N   
3114 C  CA  . ASP   A 145 ? 0.1470 0.1459 0.2605 -0.0182 0.0003  0.0113  145 ASP   A CA  
3115 C  C   . ASP   A 145 ? 0.1459 0.1389 0.2614 -0.0124 -0.0036 0.0054  145 ASP   A C   
3116 O  O   . ASP   A 145 ? 0.1597 0.1496 0.3046 -0.0147 -0.0094 -0.0266 145 ASP   A O   
3117 C  CB  . ASP   A 145 ? 0.1577 0.1774 0.2827 -0.0263 -0.0130 0.0074  145 ASP   A CB  
3118 C  CG  . ASP   A 145 ? 0.1734 0.2169 0.3116 -0.0402 -0.0232 0.0166  145 ASP   A CG  
3119 O  OD1 . ASP   A 145 ? 0.1672 0.2282 0.3189 -0.0510 -0.0139 0.0169  145 ASP   A OD1 
3120 O  OD2 . ASP   A 145 ? 0.1899 0.2455 0.3243 -0.0542 -0.0423 0.0170  145 ASP   A OD2 
3125 N  N   . THR   A 146 ? 0.1279 0.1337 0.2241 -0.0149 0.0072  0.0061  146 THR   A N   
3126 C  CA  . THR   A 146 ? 0.1249 0.1317 0.2198 -0.0085 0.0064  0.0086  146 THR   A CA  
3127 C  C   . THR   A 146 ? 0.1148 0.1268 0.2238 -0.0022 0.0107  0.0190  146 THR   A C   
3128 O  O   . THR   A 146 ? 0.1288 0.1407 0.2395 0.0023  -0.0006 0.0216  146 THR   A O   
3129 C  CB  . THR   A 146 ? 0.1196 0.1322 0.2253 -0.0059 0.0058  0.0088  146 THR   A CB  
3130 O  OG1 . THR   A 146 ? 0.1239 0.1464 0.2265 -0.0013 -0.0004 0.0076  146 THR   A OG1 
3131 C  CG2 . THR   A 146 ? 0.1225 0.1339 0.2425 -0.0057 0.0091  0.0101  146 THR   A CG2 
3139 N  N   . VAL   A 147 ? 0.1176 0.1307 0.2179 -0.0017 0.0112  0.0201  147 VAL   A N   
3140 C  CA  . VAL   A 147 ? 0.1164 0.1344 0.2139 -0.0077 0.0188  0.0263  147 VAL   A CA  
3141 C  C   . VAL   A 147 ? 0.1191 0.1341 0.2220 -0.0128 0.0150  0.0304  147 VAL   A C   
3142 O  O   . VAL   A 147 ? 0.1255 0.1384 0.2378 -0.0173 0.0054  0.0307  147 VAL   A O   
3143 C  CB  . VAL   A 147 ? 0.1254 0.1354 0.2003 -0.0091 0.0204  0.0287  147 VAL   A CB  
3144 C  CG1 . VAL   A 147 ? 0.1599 0.1403 0.2056 -0.0097 0.0139  0.0351  147 VAL   A CG1 
3145 C  CG2 . VAL   A 147 ? 0.1377 0.1304 0.2049 -0.0136 0.0068  0.0196  147 VAL   A CG2 
3155 N  N   . ARG   A 148 ? 0.1155 0.1378 0.2296 -0.0172 0.0184  0.0498  148 ARG   A N   
3156 C  CA  . ARG   A 148 ? 0.1297 0.1400 0.2303 -0.0186 0.0058  0.0514  148 ARG   A CA  
3157 C  C   . ARG   A 148 ? 0.1446 0.1366 0.2263 -0.0170 0.0062  0.0677  148 ARG   A C   
3158 O  O   . ARG   A 148 ? 0.1702 0.1489 0.2475 -0.0225 0.0145  0.0527  148 ARG   A O   
3159 C  CB  . ARG   A 148 ? 0.1364 0.1382 0.2456 -0.0093 0.0196  0.0530  148 ARG   A CB  
3160 C  CG  . ARG   A 148 ? 0.1522 0.1355 0.2706 -0.0066 0.0339  0.0454  148 ARG   A CG  
3161 C  CD  . ARG   A 148 ? 0.1715 0.1356 0.2929 -0.0049 0.0415  0.0567  148 ARG   A CD  
3162 N  NE  . ARG   A 148 ? 0.1700 0.1435 0.2907 0.0159  0.0468  0.0591  148 ARG   A NE  
3163 C  CZ  . ARG   A 148 ? 0.1620 0.1340 0.2759 0.0040  0.0408  0.0499  148 ARG   A CZ  
3164 N  NH1 . ARG   A 148 ? 0.1664 0.1304 0.2870 -0.0148 0.0431  0.0267  148 ARG   A NH1 
3165 N  NH2 . ARG   A 148 ? 0.1555 0.1582 0.2682 0.0159  0.0467  0.0513  148 ARG   A NH2 
3179 N  N   . THR   A 149 ? 0.1393 0.1481 0.2145 -0.0140 -0.0014 0.0595  149 THR   A N   
3180 C  CA  . THR   A 149 ? 0.1395 0.1542 0.2162 -0.0167 0.0001  0.0548  149 THR   A CA  
3181 C  C   . THR   A 149 ? 0.1352 0.1540 0.2077 -0.0156 0.0050  0.0612  149 THR   A C   
3182 O  O   . THR   A 149 ? 0.1374 0.1626 0.2235 -0.0227 0.0026  0.0638  149 THR   A O   
3183 C  CB  . THR   A 149 ? 0.1432 0.1664 0.2220 -0.0166 0.0030  0.0496  149 THR   A CB  
3184 O  OG1 . THR   A 149 ? 0.1428 0.1543 0.2273 -0.0280 0.0080  0.0415  149 THR   A OG1 
3185 C  CG2 . THR   A 149 ? 0.1437 0.1839 0.2346 -0.0101 -0.0125 0.0369  149 THR   A CG2 
3193 N  N   . ASN   A 150 ? 0.1413 0.1610 0.2093 -0.0110 0.0021  0.0672  150 ASN   A N   
3194 C  CA  . ASN   A 150 ? 0.1531 0.1637 0.2111 -0.0079 0.0008  0.0562  150 ASN   A CA  
3195 C  C   . ASN   A 150 ? 0.1335 0.1498 0.2028 -0.0128 0.0014  0.0534  150 ASN   A C   
3196 O  O   . ASN   A 150 ? 0.1482 0.1644 0.2317 -0.0168 -0.0141 0.0489  150 ASN   A O   
3197 C  CB  . ASN   A 150 ? 0.2011 0.1902 0.2380 -0.0182 0.0271  0.0769  150 ASN   A CB  
3198 C  CG  . ASN   A 150 ? 0.2560 0.2251 0.3052 -0.0191 0.0058  0.0816  150 ASN   A CG  
3199 O  OD1 . ASN   A 150 ? 0.2844 0.2317 0.3182 -0.0266 0.0106  0.0977  150 ASN   A OD1 
3200 N  ND2 . ASN   A 150 ? 0.2830 0.2507 0.3392 -0.0094 -0.0059 0.0721  150 ASN   A ND2 
3207 N  N   . VAL   A 151 ? 0.1351 0.1452 0.1893 -0.0183 0.0037  0.0474  151 VAL   A N   
3208 C  CA  . VAL   A 151 ? 0.1413 0.1494 0.1871 -0.0216 0.0074  0.0476  151 VAL   A CA  
3209 C  C   . VAL   A 151 ? 0.1375 0.1422 0.1985 -0.0332 0.0107  0.0498  151 VAL   A C   
3210 O  O   . VAL   A 151 ? 0.1516 0.1506 0.2196 -0.0221 0.0060  0.0395  151 VAL   A O   
3211 C  CB  . VAL   A 151 ? 0.1690 0.1673 0.2001 -0.0070 0.0069  0.0464  151 VAL   A CB  
3212 C  CG1 . VAL   A 151 ? 0.1617 0.1908 0.2231 -0.0046 0.0020  0.0354  151 VAL   A CG1 
3213 C  CG2 . VAL   A 151 ? 0.1807 0.1636 0.2053 -0.0025 0.0257  0.0451  151 VAL   A CG2 
3223 N  N   . TYR   A 152 ? 0.1305 0.1454 0.1995 -0.0307 0.0049  0.0451  152 TYR   A N   
3224 C  CA  . TYR   A 152 ? 0.1409 0.1548 0.1828 -0.0261 0.0074  0.0479  152 TYR   A CA  
3225 C  C   . TYR   A 152 ? 0.1338 0.1405 0.1654 -0.0171 0.0151  0.0487  152 TYR   A C   
3226 O  O   . TYR   A 152 ? 0.1454 0.1366 0.1734 -0.0240 0.0187  0.0378  152 TYR   A O   
3227 C  CB  . TYR   A 152 ? 0.1521 0.1630 0.1911 -0.0246 0.0201  0.0541  152 TYR   A CB  
3228 C  CG  . TYR   A 152 ? 0.1571 0.1869 0.1828 -0.0244 0.0275  0.0604  152 TYR   A CG  
3229 C  CD1 . TYR   A 152 ? 0.1670 0.2091 0.2054 -0.0151 0.0331  0.0609  152 TYR   A CD1 
3230 C  CD2 . TYR   A 152 ? 0.1635 0.1945 0.1846 -0.0364 0.0131  0.0561  152 TYR   A CD2 
3231 C  CE1 . TYR   A 152 ? 0.2025 0.2235 0.2067 -0.0057 0.0155  0.0725  152 TYR   A CE1 
3232 C  CE2 . TYR   A 152 ? 0.1893 0.2110 0.1953 -0.0413 0.0186  0.0570  152 TYR   A CE2 
3233 C  CZ  . TYR   A 152 ? 0.2184 0.2154 0.1943 -0.0246 0.0137  0.0854  152 TYR   A CZ  
3234 O  OH  . TYR   A 152 ? 0.2560 0.2336 0.2387 -0.0217 0.0154  0.1018  152 TYR   A OH  
3244 N  N   A LEU   A 153 ? 0.1298 0.1404 0.1786 -0.0210 0.0121  0.0450  153 LEU   A N   
3245 N  N   B LEU   A 153 ? 0.1293 0.1487 0.1602 -0.0184 0.0152  0.0453  153 LEU   A N   
3246 C  CA  A LEU   A 153 ? 0.1231 0.1354 0.1922 -0.0131 0.0141  0.0470  153 LEU   A CA  
3247 C  CA  B LEU   A 153 ? 0.1218 0.1531 0.1573 -0.0137 0.0215  0.0472  153 LEU   A CA  
3248 C  C   A LEU   A 153 ? 0.1303 0.1370 0.1996 -0.0068 0.0254  0.0473  153 LEU   A C   
3249 C  C   B LEU   A 153 ? 0.1234 0.1547 0.1645 -0.0070 0.0313  0.0413  153 LEU   A C   
3250 O  O   A LEU   A 153 ? 0.1398 0.1490 0.2311 -0.0118 0.0436  0.0510  153 LEU   A O   
3251 O  O   B LEU   A 153 ? 0.1288 0.1652 0.1807 -0.0081 0.0366  0.0365  153 LEU   A O   
3252 C  CB  A LEU   A 153 ? 0.1209 0.1327 0.2049 -0.0136 0.0085  0.0337  153 LEU   A CB  
3253 C  CB  B LEU   A 153 ? 0.1211 0.1605 0.1621 -0.0142 0.0146  0.0492  153 LEU   A CB  
3254 C  CG  A LEU   A 153 ? 0.1222 0.1290 0.1994 -0.0119 0.0106  0.0263  153 LEU   A CG  
3255 C  CG  B LEU   A 153 ? 0.1257 0.1671 0.1649 -0.0087 0.0078  0.0461  153 LEU   A CG  
3256 C  CD1 A LEU   A 153 ? 0.1347 0.1271 0.1995 -0.0193 0.0036  0.0272  153 LEU   A CD1 
3257 C  CD1 B LEU   A 153 ? 0.1389 0.1697 0.1763 -0.0052 0.0066  0.0465  153 LEU   A CD1 
3258 C  CD2 A LEU   A 153 ? 0.1286 0.1286 0.1951 -0.0113 0.0124  0.0043  153 LEU   A CD2 
3259 C  CD2 B LEU   A 153 ? 0.1256 0.1709 0.1588 -0.0106 0.0014  0.0379  153 LEU   A CD2 
3282 N  N   A ALA   A 154 ? 0.1316 0.1323 0.2066 -0.0036 0.0197  0.0444  154 ALA   A N   
3283 N  N   B ALA   A 154 ? 0.1182 0.1485 0.1670 -0.0098 0.0406  0.0419  154 ALA   A N   
3284 C  CA  A ALA   A 154 ? 0.1353 0.1367 0.2141 0.0031  0.0242  0.0434  154 ALA   A CA  
3285 C  CA  B ALA   A 154 ? 0.1246 0.1438 0.1848 -0.0043 0.0349  0.0417  154 ALA   A CA  
3286 C  C   A ALA   A 154 ? 0.1263 0.1362 0.2078 0.0100  0.0225  0.0445  154 ALA   A C   
3287 C  C   B ALA   A 154 ? 0.1304 0.1370 0.1831 -0.0050 0.0349  0.0447  154 ALA   A C   
3288 O  O   A ALA   A 154 ? 0.1339 0.1450 0.2141 0.0119  0.0248  0.0378  154 ALA   A O   
3289 O  O   B ALA   A 154 ? 0.1392 0.1393 0.1832 -0.0109 0.0317  0.0462  154 ALA   A O   
3290 C  CB  A ALA   A 154 ? 0.1459 0.1368 0.2255 0.0106  0.0248  0.0277  154 ALA   A CB  
3291 C  CB  B ALA   A 154 ? 0.1241 0.1475 0.2002 0.0026  0.0386  0.0324  154 ALA   A CB  
3302 N  N   A VAL   A 155 ? 0.1127 0.1165 0.1729 0.0133  0.0135  0.0533  155 VAL   A N   
3303 N  N   B VAL   A 155 ? 0.1214 0.1211 0.1668 -0.0023 0.0362  0.0422  155 VAL   A N   
3304 C  CA  A VAL   A 155 ? 0.1332 0.1320 0.1865 0.0124  0.0092  0.0524  155 VAL   A CA  
3305 C  CA  B VAL   A 155 ? 0.1402 0.1320 0.1832 -0.0074 0.0391  0.0435  155 VAL   A CA  
3306 C  CA  T VAL   A 155 ? 0.1800 0.1741 0.1853 0.0081  0.0175  0.0350  155 VAL   A CA  
3307 C  C   A VAL   A 155 ? 0.1394 0.1426 0.1971 0.0234  0.0091  0.0519  155 VAL   A C   
3308 C  C   B VAL   A 155 ? 0.1522 0.1419 0.1827 -0.0039 0.0431  0.0510  155 VAL   A C   
3309 C  C   T VAL   A 155 ? 0.1761 0.1725 0.1756 0.0193  0.0183  0.0310  155 VAL   A C   
3310 O  O   A VAL   A 155 ? 0.1406 0.1526 0.2200 0.0333  0.0182  0.0413  155 VAL   A O   
3311 O  O   B VAL   A 155 ? 0.1570 0.1450 0.1998 0.0025  0.0498  0.0562  155 VAL   A O   
3312 O  O   T VAL   A 155 ? 0.1769 0.1807 0.1784 0.0253  0.0148  0.0268  155 VAL   A O   
3313 C  CB  A VAL   A 155 ? 0.1451 0.1394 0.1944 0.0131  0.0000  0.0450  155 VAL   A CB  
3314 C  CB  B VAL   A 155 ? 0.1461 0.1342 0.1865 -0.0006 0.0235  0.0304  155 VAL   A CB  
3315 C  CB  T VAL   A 155 ? 0.1822 0.1772 0.1922 0.0084  0.0086  0.0350  155 VAL   A CB  
3316 C  CG1 A VAL   A 155 ? 0.1537 0.1418 0.1927 0.0166  -0.0051 0.0472  155 VAL   A CG1 
3317 C  CG1 B VAL   A 155 ? 0.1523 0.1368 0.1781 0.0112  0.0247  0.0211  155 VAL   A CG1 
3318 C  CG1 T VAL   A 155 ? 0.1868 0.1790 0.1925 0.0110  0.0036  0.0375  155 VAL   A CG1 
3319 C  CG2 A VAL   A 155 ? 0.1569 0.1466 0.2041 0.0185  -0.0077 0.0382  155 VAL   A CG2 
3320 C  CG2 B VAL   A 155 ? 0.1585 0.1367 0.2027 0.0063  0.0111  0.0338  155 VAL   A CG2 
3321 C  CG2 T VAL   A 155 ? 0.1861 0.1813 0.1976 0.0115  0.0044  0.0344  155 VAL   A CG2 
3347 N  N   A PHE   A 156 ? 0.1534 0.1454 0.1993 0.0176  0.0040  0.0614  156 PHE   A N   
3348 N  N   B PHE   A 156 ? 0.1702 0.1494 0.1946 -0.0065 0.0408  0.0531  156 PHE   A N   
3349 N  N   T PHE   A 156 ? 0.1775 0.1629 0.1689 0.0200  0.0206  0.0328  156 PHE   A N   
3350 C  CA  A PHE   A 156 ? 0.1709 0.1508 0.2190 0.0230  0.0118  0.0675  156 PHE   A CA  
3351 C  CA  B PHE   A 156 ? 0.1922 0.1615 0.2076 -0.0063 0.0245  0.0671  156 PHE   A CA  
3352 C  CA  T PHE   A 156 ? 0.1865 0.1580 0.1734 0.0224  0.0267  0.0315  156 PHE   A CA  
3353 C  C   A PHE   A 156 ? 0.1690 0.1627 0.2329 0.0312  0.0246  0.0680  156 PHE   A C   
3354 C  C   B PHE   A 156 ? 0.2009 0.1776 0.2346 -0.0019 0.0308  0.0772  156 PHE   A C   
3355 C  C   T PHE   A 156 ? 0.1778 0.1600 0.1909 0.0279  0.0445  0.0418  156 PHE   A C   
3356 O  O   A PHE   A 156 ? 0.1764 0.1693 0.2419 0.0240  0.0358  0.0614  156 PHE   A O   
3357 O  O   B PHE   A 156 ? 0.2115 0.1865 0.2559 0.0000  0.0406  0.0771  156 PHE   A O   
3358 O  O   T PHE   A 156 ? 0.1829 0.1557 0.2019 0.0309  0.0520  0.0277  156 PHE   A O   
3359 C  CB  A PHE   A 156 ? 0.1855 0.1555 0.2304 0.0184  0.0078  0.0691  156 PHE   A CB  
3360 C  CB  B PHE   A 156 ? 0.1961 0.1570 0.2053 -0.0114 0.0132  0.0658  156 PHE   A CB  
3361 C  CB  T PHE   A 156 ? 0.1940 0.1519 0.1535 0.0196  0.0175  0.0215  156 PHE   A CB  
3362 C  CG  A PHE   A 156 ? 0.2012 0.1604 0.2370 0.0190  0.0075  0.0673  156 PHE   A CG  
3363 C  CG  B PHE   A 156 ? 0.2050 0.1575 0.2129 -0.0114 0.0044  0.0717  156 PHE   A CG  
3364 C  CG  T PHE   A 156 ? 0.2018 0.1531 0.1420 0.0189  0.0093  0.0168  156 PHE   A CG  
3365 C  CD1 A PHE   A 156 ? 0.2078 0.1717 0.2420 0.0219  0.0167  0.0605  156 PHE   A CD1 
3366 C  CD1 B PHE   A 156 ? 0.2109 0.1674 0.2232 -0.0074 0.0118  0.0680  156 PHE   A CD1 
3367 C  CD1 T PHE   A 156 ? 0.2078 0.1613 0.1481 0.0197  0.0052  0.0125  156 PHE   A CD1 
3368 C  CD2 A PHE   A 156 ? 0.2106 0.1694 0.2405 0.0235  0.0049  0.0679  156 PHE   A CD2 
3369 C  CD2 B PHE   A 156 ? 0.2070 0.1514 0.2067 -0.0127 -0.0043 0.0734  156 PHE   A CD2 
3370 C  CD2 T PHE   A 156 ? 0.2045 0.1542 0.1479 0.0238  0.0076  0.0098  156 PHE   A CD2 
3371 C  CE1 A PHE   A 156 ? 0.2167 0.1760 0.2528 0.0223  0.0250  0.0571  156 PHE   A CE1 
3372 C  CE1 B PHE   A 156 ? 0.2118 0.1697 0.2281 -0.0087 0.0181  0.0661  156 PHE   A CE1 
3373 C  CE1 T PHE   A 156 ? 0.2112 0.1641 0.1567 0.0224  0.0062  0.0080  156 PHE   A CE1 
3374 C  CE2 A PHE   A 156 ? 0.2180 0.1761 0.2436 0.0255  0.0119  0.0603  156 PHE   A CE2 
3375 C  CE2 B PHE   A 156 ? 0.2103 0.1521 0.2176 -0.0148 -0.0039 0.0634  156 PHE   A CE2 
3376 C  CE2 T PHE   A 156 ? 0.2092 0.1567 0.1549 0.0224  0.0046  0.0055  156 PHE   A CE2 
3377 C  CZ  A PHE   A 156 ? 0.2221 0.1808 0.2559 0.0259  0.0213  0.0542  156 PHE   A CZ  
3378 C  CZ  B PHE   A 156 ? 0.2097 0.1583 0.2281 -0.0121 0.0109  0.0679  156 PHE   A CZ  
3379 C  CZ  T PHE   A 156 ? 0.2087 0.1544 0.1544 0.0201  0.0057  0.0096  156 PHE   A CZ  
3407 N  N   A ASP   A 157 ? 0.1611 0.1701 0.2331 0.0386  0.0160  0.0699  157 ASP   A N   
3408 N  N   B ASP   A 157 ? 0.1979 0.1937 0.2595 -0.0035 0.0180  0.0758  157 ASP   A N   
3409 N  N   T ASP   A 157 ? 0.1598 0.1679 0.2006 0.0275  0.0354  0.0588  157 ASP   A N   
3410 C  CA  A ASP   A 157 ? 0.1657 0.1898 0.2375 0.0457  0.0154  0.0770  157 ASP   A CA  
3411 C  CA  B ASP   A 157 ? 0.1948 0.2128 0.2669 0.0001  0.0018  0.0699  157 ASP   A CA  
3412 C  CA  T ASP   A 157 ? 0.1549 0.1819 0.2059 0.0329  0.0293  0.0719  157 ASP   A CA  
3413 C  C   A ASP   A 157 ? 0.1621 0.2067 0.2443 0.0424  0.0169  0.0755  157 ASP   A C   
3414 C  C   B ASP   A 157 ? 0.1759 0.2070 0.2503 0.0027  0.0052  0.0706  157 ASP   A C   
3415 C  C   T ASP   A 157 ? 0.1608 0.2001 0.2172 0.0296  0.0316  0.0723  157 ASP   A C   
3416 O  O   A ASP   A 157 ? 0.1628 0.2088 0.2376 0.0410  0.0140  0.0805  157 ASP   A O   
3417 O  O   B ASP   A 157 ? 0.1720 0.2038 0.2354 0.0073  0.0075  0.0699  157 ASP   A O   
3418 O  O   T ASP   A 157 ? 0.1604 0.2055 0.2216 0.0324  0.0305  0.0669  157 ASP   A O   
3419 C  CB  A ASP   A 157 ? 0.1714 0.1954 0.2447 0.0581  0.0152  0.0731  157 ASP   A CB  
3420 C  CB  B ASP   A 157 ? 0.2061 0.2415 0.2989 0.0040  -0.0128 0.0573  157 ASP   A CB  
3421 C  CB  T ASP   A 157 ? 0.1494 0.1797 0.2083 0.0415  0.0218  0.0743  157 ASP   A CB  
3422 C  CG  A ASP   A 157 ? 0.1827 0.2020 0.2578 0.0632  0.0084  0.0735  157 ASP   A CG  
3423 C  CG  B ASP   A 157 ? 0.2187 0.2661 0.3320 0.0082  -0.0269 0.0468  157 ASP   A CG  
3424 C  CG  T ASP   A 157 ? 0.1407 0.1754 0.2076 0.0422  0.0141  0.0778  157 ASP   A CG  
3425 O  OD1 A ASP   A 157 ? 0.1928 0.2172 0.2849 0.0614  -0.0146 0.0587  157 ASP   A OD1 
3426 O  OD1 B ASP   A 157 ? 0.2306 0.2839 0.3465 0.0085  -0.0307 0.0473  157 ASP   A OD1 
3427 O  OD1 T ASP   A 157 ? 0.1347 0.1714 0.2286 0.0442  0.0252  0.0601  157 ASP   A OD1 
3428 O  OD2 A ASP   A 157 ? 0.1798 0.1914 0.2442 0.0635  0.0249  0.0932  157 ASP   A OD2 
3429 O  OD2 B ASP   A 157 ? 0.2126 0.2672 0.3412 0.0141  -0.0311 0.0422  157 ASP   A OD2 
3430 O  OD2 T ASP   A 157 ? 0.1352 0.1789 0.1916 0.0386  0.0007  0.0888  157 ASP   A OD2 
3443 N  N   A LYS   A 158 ? 0.1724 0.2224 0.2594 0.0422  0.0270  0.0571  158 LYS   A N   
3444 N  N   B LYS   A 158 ? 0.1708 0.2103 0.2565 0.0008  0.0087  0.0593  158 LYS   A N   
3445 N  N   T LYS   A 158 ? 0.1764 0.2138 0.2279 0.0245  0.0384  0.0608  158 LYS   A N   
3446 C  CA  A LYS   A 158 ? 0.1767 0.2375 0.2725 0.0447  0.0333  0.0437  158 LYS   A CA  
3447 C  CA  B LYS   A 158 ? 0.1760 0.2200 0.2598 0.0014  0.0199  0.0525  158 LYS   A CA  
3448 C  CA  T LYS   A 158 ? 0.1888 0.2279 0.2472 0.0244  0.0347  0.0485  158 LYS   A CA  
3449 C  C   A LYS   A 158 ? 0.1630 0.2373 0.2593 0.0512  0.0201  0.0407  158 LYS   A C   
3450 C  C   B LYS   A 158 ? 0.1583 0.2177 0.2372 0.0036  0.0046  0.0483  158 LYS   A C   
3451 C  C   T LYS   A 158 ? 0.1819 0.2238 0.2405 0.0275  0.0202  0.0377  158 LYS   A C   
3452 O  O   A LYS   A 158 ? 0.1590 0.2411 0.2609 0.0454  0.0279  0.0335  158 LYS   A O   
3453 O  O   B LYS   A 158 ? 0.1473 0.2126 0.2308 -0.0084 0.0043  0.0456  158 LYS   A O   
3454 O  O   T LYS   A 158 ? 0.1784 0.2238 0.2427 0.0237  0.0223  0.0286  158 LYS   A O   
3455 C  CB  A LYS   A 158 ? 0.1960 0.2495 0.3079 0.0390  0.0537  0.0369  158 LYS   A CB  
3456 C  CB  B LYS   A 158 ? 0.1973 0.2388 0.2939 0.0051  0.0369  0.0551  158 LYS   A CB  
3457 C  CB  T LYS   A 158 ? 0.2095 0.2423 0.2872 0.0195  0.0466  0.0448  158 LYS   A CB  
3458 C  CG  A LYS   A 158 ? 0.2171 0.2622 0.3420 0.0374  0.0622  0.0381  158 LYS   A CG  
3459 C  CG  B LYS   A 158 ? 0.2153 0.2527 0.3259 0.0069  0.0484  0.0644  158 LYS   A CG  
3460 C  CG  T LYS   A 158 ? 0.2305 0.2563 0.3238 0.0178  0.0539  0.0475  158 LYS   A CG  
3461 C  CD  A LYS   A 158 ? 0.2342 0.2734 0.3690 0.0369  0.0723  0.0454  158 LYS   A CD  
3462 C  CD  B LYS   A 158 ? 0.2258 0.2651 0.3490 0.0056  0.0670  0.0765  158 LYS   A CD  
3463 C  CD  T LYS   A 158 ? 0.2512 0.2687 0.3609 0.0204  0.0561  0.0511  158 LYS   A CD  
3464 C  CE  A LYS   A 158 ? 0.2454 0.2784 0.3852 0.0354  0.0813  0.0574  158 LYS   A CE  
3465 C  CE  B LYS   A 158 ? 0.2300 0.2719 0.3619 0.0055  0.0816  0.0940  158 LYS   A CE  
3466 C  CE  T LYS   A 158 ? 0.2651 0.2747 0.3889 0.0223  0.0574  0.0566  158 LYS   A CE  
3467 N  NZ  A LYS   A 158 ? 0.2501 0.2795 0.3914 0.0334  0.0896  0.0649  158 LYS   A NZ  
3468 N  NZ  B LYS   A 158 ? 0.2275 0.2733 0.3641 0.0016  0.0957  0.1070  158 LYS   A NZ  
3469 N  NZ  T LYS   A 158 ? 0.2723 0.2769 0.4033 0.0252  0.0578  0.0588  158 LYS   A NZ  
3509 N  N   A ASN   A 159 ? 0.1602 0.2347 0.2584 0.0492  0.0035  0.0416  159 ASN   A N   
3510 N  N   B ASN   A 159 ? 0.1638 0.2277 0.2378 0.0180  -0.0014 0.0440  159 ASN   A N   
3511 N  N   T ASN   A 159 ? 0.1831 0.2221 0.2458 0.0252  0.0093  0.0333  159 ASN   A N   
3512 C  CA  A ASN   A 159 ? 0.1584 0.2336 0.2502 0.0420  -0.0131 0.0442  159 ASN   A CA  
3513 C  CA  B ASN   A 159 ? 0.1677 0.2371 0.2431 0.0256  -0.0065 0.0506  159 ASN   A CA  
3514 C  CA  T ASN   A 159 ? 0.1898 0.2224 0.2476 0.0220  -0.0026 0.0332  159 ASN   A CA  
3515 C  C   A ASN   A 159 ? 0.1459 0.2272 0.2354 0.0321  -0.0119 0.0415  159 ASN   A C   
3516 C  C   B ASN   A 159 ? 0.1491 0.2282 0.2272 0.0134  -0.0057 0.0478  159 ASN   A C   
3517 C  C   T ASN   A 159 ? 0.1911 0.2168 0.2455 0.0162  0.0013  0.0264  159 ASN   A C   
3518 O  O   A ASN   A 159 ? 0.1346 0.2209 0.2392 0.0268  -0.0210 0.0261  159 ASN   A O   
3519 O  O   B ASN   A 159 ? 0.1450 0.2362 0.2284 0.0142  -0.0076 0.0485  159 ASN   A O   
3520 O  O   T ASN   A 159 ? 0.1919 0.2104 0.2553 0.0119  0.0006  0.0130  159 ASN   A O   
3521 C  CB  A ASN   A 159 ? 0.1749 0.2433 0.2726 0.0377  -0.0137 0.0528  159 ASN   A CB  
3522 C  CB  B ASN   A 159 ? 0.1902 0.2526 0.2735 0.0334  -0.0075 0.0563  159 ASN   A CB  
3523 C  CB  T ASN   A 159 ? 0.1995 0.2322 0.2654 0.0215  -0.0066 0.0447  159 ASN   A CB  
3524 C  CG  A ASN   A 159 ? 0.1920 0.2559 0.3033 0.0332  -0.0078 0.0574  159 ASN   A CG  
3525 C  CG  B ASN   A 159 ? 0.2076 0.2672 0.3099 0.0260  0.0004  0.0483  159 ASN   A CG  
3526 C  CG  T ASN   A 159 ? 0.2091 0.2437 0.2895 0.0207  -0.0032 0.0521  159 ASN   A CG  
3527 O  OD1 A ASN   A 159 ? 0.1998 0.2671 0.3221 0.0321  0.0049  0.0611  159 ASN   A OD1 
3528 O  OD1 B ASN   A 159 ? 0.2107 0.2761 0.3225 0.0248  -0.0091 0.0432  159 ASN   A OD1 
3529 O  OD1 T ASN   A 159 ? 0.2119 0.2546 0.3070 0.0217  0.0096  0.0546  159 ASN   A OD1 
3530 N  ND2 A ASN   A 159 ? 0.1981 0.2598 0.3147 0.0289  -0.0096 0.0512  159 ASN   A ND2 
3531 N  ND2 B ASN   A 159 ? 0.2157 0.2715 0.3212 0.0248  0.0045  0.0534  159 ASN   A ND2 
3532 N  ND2 T ASN   A 159 ? 0.2132 0.2474 0.2959 0.0180  -0.0073 0.0498  159 ASN   A ND2 
3551 N  N   A LEU   A 160 ? 0.1395 0.2206 0.2130 0.0289  -0.0082 0.0552  160 LEU   A N   
3552 N  N   B LEU   A 160 ? 0.1431 0.2156 0.2170 0.0016  -0.0091 0.0547  160 LEU   A N   
3553 N  N   T LEU   A 160 ? 0.1872 0.2119 0.2323 0.0148  0.0017  0.0340  160 LEU   A N   
3554 C  CA  A LEU   A 160 ? 0.1338 0.2156 0.1942 0.0159  0.0114  0.0731  160 LEU   A CA  
3555 C  CA  B LEU   A 160 ? 0.1484 0.2126 0.2114 -0.0007 0.0011  0.0589  160 LEU   A CA  
3556 C  CA  T LEU   A 160 ? 0.1850 0.2061 0.2185 0.0052  0.0117  0.0492  160 LEU   A CA  
3557 C  C   A LEU   A 160 ? 0.1139 0.2120 0.1820 0.0062  0.0257  0.0851  160 LEU   A C   
3558 C  C   B LEU   A 160 ? 0.1323 0.2108 0.1973 0.0085  0.0120  0.0692  160 LEU   A C   
3559 O  O   A LEU   A 160 ? 0.1059 0.2087 0.1829 0.0025  0.0127  0.0922  160 LEU   A O   
3560 O  O   B LEU   A 160 ? 0.1391 0.2088 0.2094 0.0099  0.0129  0.0702  160 LEU   A O   
3561 C  CB  A LEU   A 160 ? 0.1400 0.2174 0.1884 0.0146  0.0141  0.0775  160 LEU   A CB  
3562 C  CB  B LEU   A 160 ? 0.1735 0.2205 0.2281 -0.0027 0.0054  0.0436  160 LEU   A CB  
3563 C  CB  T LEU   A 160 ? 0.1797 0.2048 0.2020 -0.0052 0.0221  0.0604  160 LEU   A CB  
3564 C  CG  A LEU   A 160 ? 0.1454 0.2240 0.2041 0.0102  0.0175  0.0668  160 LEU   A CG  
3565 C  CG  B LEU   A 160 ? 0.2029 0.2413 0.2643 -0.0018 0.0085  0.0202  160 LEU   A CG  
3566 C  CG  T LEU   A 160 ? 0.1762 0.2082 0.2018 -0.0157 0.0290  0.0609  160 LEU   A CG  
3567 C  CD1 A LEU   A 160 ? 0.1519 0.2278 0.2096 0.0047  0.0288  0.0590  160 LEU   A CD1 
3568 C  CD1 B LEU   A 160 ? 0.2112 0.2470 0.2734 -0.0001 0.0106  0.0165  160 LEU   A CD1 
3569 C  CD1 T LEU   A 160 ? 0.1807 0.2133 0.2035 -0.0184 0.0379  0.0565  160 LEU   A CD1 
3570 C  CD2 A LEU   A 160 ? 0.1471 0.2257 0.2102 0.0113  0.0216  0.0594  160 LEU   A CD2 
3571 C  CD2 B LEU   A 160 ? 0.2121 0.2479 0.2776 -0.0050 0.0098  0.0145  160 LEU   A CD2 
3572 C  CD2 T LEU   A 160 ? 0.1756 0.2080 0.2033 -0.0179 0.0323  0.0571  160 LEU   A CD2 
3605 N  N   A TYR   A 161 ? 0.1290 0.2170 0.2220 0.0034  0.0279  0.0778  161 TYR   A N   
3606 N  N   B TYR   A 161 ? 0.1348 0.2156 0.1998 0.0145  0.0230  0.0721  161 TYR   A N   
3607 C  CA  A TYR   A 161 ? 0.1291 0.2255 0.2206 0.0002  0.0251  0.0754  161 TYR   A CA  
3608 C  CA  B TYR   A 161 ? 0.1424 0.2198 0.1993 0.0146  0.0227  0.0830  161 TYR   A CA  
3609 C  C   A TYR   A 161 ? 0.1301 0.2545 0.2433 -0.0020 0.0169  0.0751  161 TYR   A C   
3610 C  C   B TYR   A 161 ? 0.1415 0.2298 0.2168 0.0151  0.0164  0.0804  161 TYR   A C   
3611 O  O   A TYR   A 161 ? 0.1288 0.2536 0.2462 -0.0103 0.0152  0.0754  161 TYR   A O   
3612 O  O   B TYR   A 161 ? 0.1408 0.2291 0.2138 0.0078  0.0190  0.0851  161 TYR   A O   
3613 C  CB  A TYR   A 161 ? 0.1383 0.2138 0.2275 -0.0051 0.0274  0.0721  161 TYR   A CB  
3614 C  CB  B TYR   A 161 ? 0.1550 0.2185 0.1994 0.0129  0.0289  0.0835  161 TYR   A CB  
3615 C  CG  A TYR   A 161 ? 0.1363 0.1974 0.2275 -0.0032 0.0112  0.0582  161 TYR   A CG  
3616 C  CG  B TYR   A 161 ? 0.1604 0.2117 0.2058 0.0122  0.0313  0.0757  161 TYR   A CG  
3617 C  CD1 A TYR   A 161 ? 0.1308 0.1873 0.2370 -0.0060 0.0005  0.0477  161 TYR   A CD1 
3618 C  CD1 B TYR   A 161 ? 0.1625 0.2069 0.2168 0.0111  0.0264  0.0685  161 TYR   A CD1 
3619 C  CD2 A TYR   A 161 ? 0.1350 0.1891 0.2270 0.0085  0.0072  0.0542  161 TYR   A CD2 
3620 C  CD2 B TYR   A 161 ? 0.1629 0.2042 0.2124 0.0105  0.0378  0.0774  161 TYR   A CD2 
3621 C  CE1 A TYR   A 161 ? 0.1327 0.1728 0.2339 0.0029  -0.0017 0.0443  161 TYR   A CE1 
3622 C  CE1 B TYR   A 161 ? 0.1648 0.2063 0.2232 0.0119  0.0281  0.0609  161 TYR   A CE1 
3623 C  CE2 A TYR   A 161 ? 0.1346 0.1710 0.2226 0.0022  0.0025  0.0582  161 TYR   A CE2 
3624 C  CE2 B TYR   A 161 ? 0.1658 0.2043 0.2197 0.0029  0.0405  0.0723  161 TYR   A CE2 
3625 C  CZ  A TYR   A 161 ? 0.1410 0.1624 0.2144 -0.0002 -0.0006 0.0514  161 TYR   A CZ  
3626 C  CZ  B TYR   A 161 ? 0.1741 0.2078 0.2290 0.0031  0.0330  0.0630  161 TYR   A CZ  
3627 O  OH  A TYR   A 161 ? 0.1556 0.1455 0.2137 -0.0068 0.0017  0.0559  161 TYR   A OH  
3628 O  OH  B TYR   A 161 ? 0.1868 0.2136 0.2603 0.0008  0.0236  0.0536  161 TYR   A OH  
3647 N  N   A ASP   A 162 ? 0.1292 0.2840 0.2539 0.0031  0.0287  0.0846  162 ASP   A N   
3648 N  N   B ASP   A 162 ? 0.1443 0.2412 0.2395 0.0154  0.0180  0.0724  162 ASP   A N   
3649 C  CA  A ASP   A 162 ? 0.1280 0.3168 0.2539 0.0036  0.0360  0.0791  162 ASP   A CA  
3650 C  CA  B ASP   A 162 ? 0.1476 0.2558 0.2432 0.0050  0.0261  0.0691  162 ASP   A CA  
3651 C  C   A ASP   A 162 ? 0.1197 0.3280 0.2321 0.0007  0.0304  0.0839  162 ASP   A C   
3652 C  C   B ASP   A 162 ? 0.1485 0.2687 0.2378 -0.0063 0.0295  0.0725  162 ASP   A C   
3653 O  O   A ASP   A 162 ? 0.1250 0.3326 0.2421 -0.0012 0.0305  0.0705  162 ASP   A O   
3654 O  O   B ASP   A 162 ? 0.1510 0.2690 0.2337 -0.0141 0.0386  0.0699  162 ASP   A O   
3655 C  CB  A ASP   A 162 ? 0.1390 0.3384 0.2904 0.0093  0.0446  0.0624  162 ASP   A CB  
3656 C  CB  B ASP   A 162 ? 0.1512 0.2581 0.2605 0.0100  0.0305  0.0622  162 ASP   A CB  
3657 C  CG  A ASP   A 162 ? 0.1508 0.3604 0.3238 0.0133  0.0505  0.0514  162 ASP   A CG  
3658 C  CG  B ASP   A 162 ? 0.1549 0.2665 0.2838 0.0126  0.0323  0.0573  162 ASP   A CG  
3659 O  OD1 A ASP   A 162 ? 0.1580 0.3678 0.3403 0.0034  0.0442  0.0472  162 ASP   A OD1 
3660 O  OD1 B ASP   A 162 ? 0.1640 0.2748 0.2956 0.0063  0.0275  0.0468  162 ASP   A OD1 
3661 O  OD2 A ASP   A 162 ? 0.1682 0.3706 0.3399 0.0213  0.0553  0.0461  162 ASP   A OD2 
3662 O  OD2 B ASP   A 162 ? 0.1546 0.2621 0.2981 0.0136  0.0444  0.0605  162 ASP   A OD2 
3671 N  N   A LYS   A 163 ? 0.1292 0.3397 0.2369 -0.0050 0.0150  0.0870  163 LYS   A N   
3672 N  N   B LYS   A 163 ? 0.1537 0.2797 0.2484 -0.0138 0.0140  0.0745  163 LYS   A N   
3673 C  CA  A LYS   A 163 ? 0.1410 0.3472 0.2345 -0.0081 0.0060  0.0859  163 LYS   A CA  
3674 C  CA  B LYS   A 163 ? 0.1648 0.2916 0.2496 -0.0152 0.0066  0.0750  163 LYS   A CA  
3675 C  C   A LYS   A 163 ? 0.1412 0.3367 0.2163 -0.0158 0.0094  0.0881  163 LYS   A C   
3676 C  C   B LYS   A 163 ? 0.1562 0.2896 0.2330 -0.0130 0.0070  0.0710  163 LYS   A C   
3677 O  O   A LYS   A 163 ? 0.1344 0.3379 0.2009 -0.0182 0.0013  0.0939  163 LYS   A O   
3678 O  O   B LYS   A 163 ? 0.1581 0.2991 0.2264 -0.0125 0.0051  0.0771  163 LYS   A O   
3679 C  CB  A LYS   A 163 ? 0.1767 0.3673 0.2733 0.0132  -0.0091 0.0765  163 LYS   A CB  
3680 C  CB  B LYS   A 163 ? 0.1899 0.3066 0.2834 -0.0158 0.0017  0.0688  163 LYS   A CB  
3681 C  CG  A LYS   A 163 ? 0.2089 0.3855 0.3261 0.0180  -0.0081 0.0654  163 LYS   A CG  
3682 C  CG  B LYS   A 163 ? 0.2183 0.3244 0.3254 -0.0166 0.0035  0.0567  163 LYS   A CG  
3683 C  CD  A LYS   A 163 ? 0.2384 0.4001 0.3842 0.0220  -0.0065 0.0587  163 LYS   A CD  
3684 C  CD  B LYS   A 163 ? 0.2372 0.3357 0.3639 -0.0167 0.0063  0.0484  163 LYS   A CD  
3685 C  CE  A LYS   A 163 ? 0.2649 0.4081 0.4322 0.0236  0.0022  0.0564  163 LYS   A CE  
3686 C  CE  B LYS   A 163 ? 0.2483 0.3423 0.3906 -0.0161 0.0099  0.0440  163 LYS   A CE  
3687 N  NZ  A LYS   A 163 ? 0.2768 0.4138 0.4601 0.0227  0.0042  0.0526  163 LYS   A NZ  
3688 N  NZ  B LYS   A 163 ? 0.2546 0.3449 0.4042 -0.0146 0.0142  0.0424  163 LYS   A NZ  
3715 N  N   A LEU   A 164 ? 0.1309 0.3137 0.2056 -0.0238 0.0034  0.0806  164 LEU   A N   
3716 N  N   B LEU   A 164 ? 0.1442 0.2737 0.2253 -0.0134 0.0081  0.0575  164 LEU   A N   
3717 C  CA  A LEU   A 164 ? 0.1341 0.2931 0.1896 -0.0330 0.0104  0.0720  164 LEU   A CA  
3718 C  CA  B LEU   A 164 ? 0.1391 0.2588 0.1957 -0.0146 0.0174  0.0492  164 LEU   A CA  
3719 C  C   A LEU   A 164 ? 0.1490 0.2893 0.1765 -0.0318 0.0072  0.0584  164 LEU   A C   
3720 C  C   B LEU   A 164 ? 0.1448 0.2578 0.1827 -0.0221 0.0256  0.0436  164 LEU   A C   
3721 O  O   A LEU   A 164 ? 0.1587 0.2917 0.1643 -0.0305 0.0224  0.0452  164 LEU   A O   
3722 O  O   B LEU   A 164 ? 0.1458 0.2594 0.1700 -0.0319 0.0342  0.0410  164 LEU   A O   
3723 C  CB  A LEU   A 164 ? 0.1324 0.2808 0.1882 -0.0292 0.0140  0.0743  164 LEU   A CB  
3724 C  CB  B LEU   A 164 ? 0.1350 0.2462 0.1812 -0.0042 0.0166  0.0440  164 LEU   A CB  
3725 C  CG  A LEU   A 164 ? 0.1425 0.2730 0.1841 -0.0260 0.0079  0.0719  164 LEU   A CG  
3726 C  CG  B LEU   A 164 ? 0.1406 0.2368 0.1793 0.0020  0.0093  0.0433  164 LEU   A CG  
3727 C  CD1 A LEU   A 164 ? 0.1348 0.2683 0.1751 -0.0234 0.0102  0.0759  164 LEU   A CD1 
3728 C  CD1 B LEU   A 164 ? 0.1398 0.2384 0.1817 0.0049  0.0109  0.0345  164 LEU   A CD1 
3729 C  CD2 A LEU   A 164 ? 0.1590 0.2729 0.1840 -0.0264 0.0081  0.0669  164 LEU   A CD2 
3730 C  CD2 B LEU   A 164 ? 0.1421 0.2292 0.1672 -0.0010 0.0135  0.0479  164 LEU   A CD2 
3753 N  N   A VAL   A 165 ? 0.1406 0.2787 0.1734 -0.0362 0.0091  0.0628  165 VAL   A N   
3754 N  N   B VAL   A 165 ? 0.1401 0.2535 0.1836 -0.0253 0.0255  0.0380  165 VAL   A N   
3755 C  CA  A VAL   A 165 ? 0.1490 0.2726 0.1561 -0.0356 0.0156  0.0647  165 VAL   A CA  
3756 C  CA  B VAL   A 165 ? 0.1483 0.2532 0.1831 -0.0244 0.0298  0.0351  165 VAL   A CA  
3757 C  C   A VAL   A 165 ? 0.1415 0.2839 0.1490 -0.0270 0.0233  0.0661  165 VAL   A C   
3758 C  C   B VAL   A 165 ? 0.1389 0.2560 0.1767 -0.0202 0.0316  0.0296  165 VAL   A C   
3759 O  O   A VAL   A 165 ? 0.1395 0.2830 0.1486 -0.0282 0.0273  0.0544  165 VAL   A O   
3760 O  O   B VAL   A 165 ? 0.1372 0.2543 0.1574 -0.0224 0.0330  0.0247  165 VAL   A O   
3761 C  CB  A VAL   A 165 ? 0.1601 0.2597 0.1695 -0.0364 0.0182  0.0546  165 VAL   A CB  
3762 C  CB  B VAL   A 165 ? 0.1612 0.2520 0.1885 -0.0252 0.0326  0.0289  165 VAL   A CB  
3763 C  CG1 A VAL   A 165 ? 0.1656 0.2591 0.1759 -0.0343 0.0244  0.0400  165 VAL   A CG1 
3764 C  CG1 B VAL   A 165 ? 0.1654 0.2543 0.1899 -0.0263 0.0368  0.0214  165 VAL   A CG1 
3765 C  CG2 A VAL   A 165 ? 0.1717 0.2592 0.1692 -0.0331 0.0182  0.0626  165 VAL   A CG2 
3766 C  CG2 B VAL   A 165 ? 0.1704 0.2525 0.1920 -0.0244 0.0313  0.0280  165 VAL   A CG2 
3785 N  N   A SER   A 166 ? 0.1378 0.2992 0.1719 -0.0168 0.0160  0.0589  166 SER   A N   
3786 N  N   B SER   A 166 ? 0.1314 0.2654 0.1979 -0.0137 0.0324  0.0317  166 SER   A N   
3787 C  CA  A SER   A 166 ? 0.1406 0.3148 0.1828 -0.0163 0.0162  0.0522  166 SER   A CA  
3788 C  CA  B SER   A 166 ? 0.1380 0.2758 0.2032 -0.0147 0.0279  0.0318  166 SER   A CA  
3789 C  C   A SER   A 166 ? 0.1457 0.3311 0.1873 -0.0141 0.0092  0.0477  166 SER   A C   
3790 C  C   B SER   A 166 ? 0.1545 0.2858 0.1899 -0.0238 0.0248  0.0369  166 SER   A C   
3791 O  O   A SER   A 166 ? 0.1651 0.3442 0.1936 -0.0249 0.0101  0.0322  166 SER   A O   
3792 O  O   B SER   A 166 ? 0.1630 0.2935 0.1875 -0.0335 0.0324  0.0379  166 SER   A O   
3793 C  CB  A SER   A 166 ? 0.1462 0.3158 0.1997 -0.0128 0.0185  0.0540  166 SER   A CB  
3794 C  CB  B SER   A 166 ? 0.1349 0.2758 0.2294 -0.0061 0.0214  0.0246  166 SER   A CB  
3795 O  OG  A SER   A 166 ? 0.1567 0.3171 0.2184 -0.0100 0.0192  0.0617  166 SER   A OG  
3796 O  OG  B SER   A 166 ? 0.1352 0.2757 0.2564 0.0007  0.0114  0.0286  166 SER   A OG  
3807 N  N   A SER   A 167 ? 0.1420 0.3286 0.1693 0.0056  0.0102  0.0623  167 SER   A N   
3808 N  N   B SER   A 167 ? 0.1691 0.2857 0.2008 -0.0181 0.0216  0.0413  167 SER   A N   
3809 C  CA  A SER   A 167 ? 0.1556 0.3265 0.1819 0.0109  0.0051  0.0536  167 SER   A CA  
3810 C  CA  B SER   A 167 ? 0.1857 0.2869 0.2146 -0.0168 0.0256  0.0403  167 SER   A CA  
3811 C  C   A SER   A 167 ? 0.1577 0.3216 0.1940 0.0191  0.0242  0.0506  167 SER   A C   
3812 C  C   B SER   A 167 ? 0.1947 0.2905 0.2199 -0.0117 0.0263  0.0346  167 SER   A C   
3813 O  O   A SER   A 167 ? 0.1757 0.3282 0.2074 0.0207  0.0114  0.0514  167 SER   A O   
3814 O  O   B SER   A 167 ? 0.2024 0.2940 0.2278 -0.0166 0.0217  0.0329  167 SER   A O   
3815 C  CB  A SER   A 167 ? 0.1527 0.3277 0.1903 0.0048  0.0065  0.0550  167 SER   A CB  
3816 C  CB  B SER   A 167 ? 0.1978 0.2873 0.2418 -0.0159 0.0231  0.0351  167 SER   A CB  
3817 O  OG  A SER   A 167 ? 0.1538 0.3315 0.2082 -0.0021 0.0276  0.0553  167 SER   A OG  
3818 O  OG  B SER   A 167 ? 0.2097 0.2889 0.2679 -0.0165 0.0159  0.0324  167 SER   A OG  
3829 N  N   A PHE   A 168 ? 0.1439 0.3102 0.2012 0.0256  0.0311  0.0492  168 PHE   A N   
3830 N  N   B PHE   A 168 ? 0.2001 0.2890 0.2169 -0.0008 0.0210  0.0378  168 PHE   A N   
3831 C  CA  A PHE   A 168 ? 0.1411 0.3001 0.2261 0.0235  0.0311  0.0508  168 PHE   A CA  
3832 C  CA  B PHE   A 168 ? 0.2163 0.2866 0.2296 0.0023  0.0159  0.0395  168 PHE   A CA  
3833 C  C   A PHE   A 168 ? 0.1458 0.3091 0.2440 0.0114  0.0615  0.0348  168 PHE   A C   
3834 C  C   B PHE   A 168 ? 0.2530 0.3094 0.2787 0.0094  0.0227  0.0458  168 PHE   A C   
3835 O  O   A PHE   A 168 ? 0.1701 0.3141 0.3002 0.0050  0.0671  0.0478  168 PHE   A O   
3836 O  O   B PHE   A 168 ? 0.2493 0.3089 0.2712 0.0085  0.0282  0.0596  168 PHE   A O   
3837 C  CB  A PHE   A 168 ? 0.1451 0.2839 0.2219 0.0188  0.0170  0.0630  168 PHE   A CB  
3838 C  CB  B PHE   A 168 ? 0.2069 0.2630 0.2005 -0.0065 0.0040  0.0343  168 PHE   A CB  
3839 C  CG  A PHE   A 168 ? 0.1424 0.2737 0.2210 0.0117  0.0144  0.0722  168 PHE   A CG  
3840 C  CG  B PHE   A 168 ? 0.1980 0.2393 0.1777 -0.0155 -0.0072 0.0314  168 PHE   A CG  
3841 C  CD1 A PHE   A 168 ? 0.1462 0.2712 0.2241 0.0024  0.0111  0.0789  168 PHE   A CD1 
3842 C  CD1 B PHE   A 168 ? 0.1935 0.2309 0.1774 -0.0188 -0.0138 0.0302  168 PHE   A CD1 
3843 C  CD2 A PHE   A 168 ? 0.1378 0.2723 0.2205 0.0090  0.0351  0.0734  168 PHE   A CD2 
3844 C  CD2 B PHE   A 168 ? 0.1975 0.2294 0.1703 -0.0172 -0.0138 0.0291  168 PHE   A CD2 
3845 C  CE1 A PHE   A 168 ? 0.1375 0.2668 0.2252 0.0020  0.0184  0.0834  168 PHE   A CE1 
3846 C  CE1 B PHE   A 168 ? 0.1860 0.2281 0.1743 -0.0231 -0.0189 0.0284  168 PHE   A CE1 
3847 C  CE2 A PHE   A 168 ? 0.1446 0.2637 0.2320 0.0064  0.0287  0.0809  168 PHE   A CE2 
3848 C  CE2 B PHE   A 168 ? 0.1973 0.2275 0.1714 -0.0183 -0.0194 0.0309  168 PHE   A CE2 
3849 C  CZ  A PHE   A 168 ? 0.1406 0.2631 0.2293 0.0045  0.0229  0.0833  168 PHE   A CZ  
3850 C  CZ  B PHE   A 168 ? 0.1936 0.2282 0.1770 -0.0196 -0.0201 0.0324  168 PHE   A CZ  
3869 N  N   A LEU   A 169 ? 0.1596 0.3155 0.2596 -0.0076 0.0539  0.0041  169 LEU   A N   
3870 N  N   B LEU   A 169 ? 0.2981 0.3336 0.3494 0.0139  0.0182  0.0394  169 LEU   A N   
3871 C  CA  A LEU   A 169 ? 0.2023 0.3258 0.3151 -0.0035 0.0230  -0.0103 169 LEU   A CA  
3872 C  CA  B LEU   A 169 ? 0.3347 0.3555 0.4075 0.0222  0.0054  0.0347  169 LEU   A CA  
3873 C  C   A LEU   A 169 ? 0.2022 0.3193 0.3400 -0.0071 0.0245  0.0008  169 LEU   A C   
3874 C  C   B LEU   A 169 ? 0.3502 0.3653 0.4478 0.0263  0.0045  0.0379  169 LEU   A C   
3875 O  O   A LEU   A 169 ? 0.2085 0.3210 0.3555 -0.0054 0.0189  -0.0013 169 LEU   A O   
3876 O  O   B LEU   A 169 ? 0.3557 0.3671 0.4626 0.0298  0.0044  0.0425  169 LEU   A O   
3877 C  CB  A LEU   A 169 ? 0.2389 0.3370 0.3366 -0.0025 0.0007  -0.0333 169 LEU   A CB  
3878 C  CB  B LEU   A 169 ? 0.3530 0.3651 0.4180 0.0250  -0.0038 0.0255  169 LEU   A CB  
3879 C  CG  A LEU   A 169 ? 0.2716 0.3461 0.3548 -0.0040 -0.0200 -0.0554 169 LEU   A CG  
3880 C  CG  B LEU   A 169 ? 0.3672 0.3722 0.4253 0.0271  -0.0102 0.0163  169 LEU   A CG  
3881 C  CD1 A LEU   A 169 ? 0.2836 0.3465 0.3654 -0.0027 -0.0330 -0.0602 169 LEU   A CD1 
3882 C  CD1 B LEU   A 169 ? 0.3722 0.3749 0.4310 0.0283  -0.0142 0.0136  169 LEU   A CD1 
3883 C  CD2 A LEU   A 169 ? 0.2807 0.3510 0.3578 -0.0077 -0.0204 -0.0622 169 LEU   A CD2 
3884 C  CD2 B LEU   A 169 ? 0.3717 0.3744 0.4252 0.0272  -0.0107 0.0133  169 LEU   A CD2 
3885 O  OXT A LEU   A 169 ? 0.1838 0.3168 0.3329 -0.0129 0.0290  0.0107  169 LEU   A OXT 
3886 O  OXT B LEU   A 169 ? 0.3574 0.3713 0.4638 0.0242  0.0053  0.0350  169 LEU   A OXT 
3909 N  N   A SER   B 1   ? 0.3756 0.3301 0.3515 -0.1027 -0.0631 0.0332  1   SER   B N   
3910 N  N   B SER   B 1   ? 0.3305 0.3126 0.3398 -0.0822 -0.0485 0.0275  1   SER   B N   
3911 C  CA  A SER   B 1   ? 0.3689 0.3341 0.3543 -0.1054 -0.0693 0.0324  1   SER   B CA  
3912 C  CA  B SER   B 1   ? 0.3245 0.3148 0.3376 -0.0845 -0.0522 0.0284  1   SER   B CA  
3913 C  C   A SER   B 1   ? 0.3460 0.3383 0.3328 -0.1045 -0.0772 0.0480  1   SER   B C   
3914 C  C   B SER   B 1   ? 0.3065 0.3158 0.3191 -0.0860 -0.0637 0.0465  1   SER   B C   
3915 O  O   A SER   B 1   ? 0.3527 0.3393 0.3126 -0.0981 -0.0693 0.0499  1   SER   B O   
3916 O  O   B SER   B 1   ? 0.3108 0.3171 0.3096 -0.0829 -0.0598 0.0444  1   SER   B O   
3917 C  CB  A SER   B 1   ? 0.3797 0.3304 0.3794 -0.1074 -0.0621 0.0161  1   SER   B CB  
3918 C  CB  B SER   B 1   ? 0.3322 0.3131 0.3538 -0.0842 -0.0422 0.0113  1   SER   B CB  
3919 O  OG  A SER   B 1   ? 0.3914 0.3396 0.4209 -0.1059 -0.0525 0.0097  1   SER   B OG  
3920 O  OG  B SER   B 1   ? 0.3404 0.3190 0.3785 -0.0828 -0.0356 0.0020  1   SER   B OG  
3935 N  N   A MET   B 2   ? 0.3206 0.3377 0.3384 -0.1070 -0.0796 0.0772  2   MET   B N   
3936 N  N   B MET   B 2   ? 0.2868 0.3130 0.3117 -0.0885 -0.0718 0.0784  2   MET   B N   
3937 C  CA  A MET   B 2   ? 0.3000 0.3387 0.3588 -0.0916 -0.0805 0.0994  2   MET   B CA  
3938 C  CA  B MET   B 2   ? 0.2700 0.3133 0.3120 -0.0793 -0.0798 0.1069  2   MET   B CA  
3939 C  C   A MET   B 2   ? 0.2616 0.3158 0.3277 -0.0743 -0.0957 0.1308  2   MET   B C   
3940 C  C   B MET   B 2   ? 0.2486 0.2998 0.3040 -0.0730 -0.0905 0.1310  2   MET   B C   
3941 O  O   A MET   B 2   ? 0.2584 0.3238 0.3312 -0.0559 -0.1147 0.1331  2   MET   B O   
3942 O  O   B MET   B 2   ? 0.2467 0.3032 0.3053 -0.0634 -0.1020 0.1291  2   MET   B O   
3943 C  CB  A MET   B 2   ? 0.3304 0.3704 0.4392 -0.0726 -0.0600 0.0761  2   MET   B CB  
3944 C  CB  B MET   B 2   ? 0.2838 0.3351 0.3386 -0.0622 -0.0719 0.1024  2   MET   B CB  
3945 C  CG  A MET   B 2   ? 0.3584 0.3962 0.5176 -0.0529 -0.0411 0.0626  2   MET   B CG  
3946 C  CG  B MET   B 2   ? 0.2967 0.3535 0.3564 -0.0447 -0.0667 0.1076  2   MET   B CG  
3947 S  SD  A MET   B 2   ? 0.3826 0.4220 0.5900 -0.0373 -0.0253 0.0496  2   MET   B SD  
3948 S  SD  B MET   B 2   ? 0.3086 0.3712 0.3725 -0.0283 -0.0649 0.1129  2   MET   B SD  
3949 C  CE  A MET   B 2   ? 0.3834 0.4294 0.5965 -0.0379 -0.0157 0.0485  2   MET   B CE  
3950 C  CE  B MET   B 2   ? 0.3087 0.3719 0.3778 -0.0285 -0.0585 0.1058  2   MET   B CE  
3969 N  N   . VAL   B 3   ? 0.2314 0.2814 0.2974 -0.0767 -0.0860 0.1471  3   VAL   B N   
3970 C  CA  . VAL   B 3   ? 0.2145 0.2478 0.2922 -0.0705 -0.0698 0.1253  3   VAL   B CA  
3971 C  C   . VAL   B 3   ? 0.1912 0.2402 0.2548 -0.0672 -0.0663 0.1045  3   VAL   B C   
3972 O  O   . VAL   B 3   ? 0.1913 0.2577 0.2639 -0.0697 -0.0647 0.1162  3   VAL   B O   
3973 C  CB  . VAL   B 3   ? 0.2279 0.2348 0.3497 -0.0692 -0.0603 0.1059  3   VAL   B CB  
3974 C  CG1 . VAL   B 3   ? 0.2315 0.2224 0.3721 -0.0670 -0.0622 0.1019  3   VAL   B CG1 
3975 C  CG2 . VAL   B 3   ? 0.2323 0.2417 0.3693 -0.0653 -0.0503 0.1093  3   VAL   B CG2 
3986 N  N   . ASN   B 4   ? 0.1833 0.2061 0.2231 -0.0663 -0.0547 0.0770  4   ASN   B N   
3987 C  CA  . ASN   B 4   ? 0.1884 0.2041 0.1919 -0.0587 -0.0527 0.0444  4   ASN   B CA  
3988 C  C   . ASN   B 4   ? 0.1917 0.2211 0.1937 -0.0581 -0.0454 0.0373  4   ASN   B C   
3989 O  O   . ASN   B 4   ? 0.1892 0.2275 0.2075 -0.0544 -0.0344 0.0205  4   ASN   B O   
3990 C  CB  . ASN   B 4   ? 0.1900 0.1984 0.1824 -0.0495 -0.0625 0.0303  4   ASN   B CB  
3991 C  CG  . ASN   B 4   ? 0.1874 0.1830 0.1766 -0.0476 -0.0586 0.0254  4   ASN   B CG  
3992 O  OD1 . ASN   B 4   ? 0.1904 0.1691 0.1809 -0.0456 -0.0581 0.0270  4   ASN   B OD1 
3993 N  ND2 . ASN   B 4   ? 0.1999 0.1919 0.1848 -0.0286 -0.0408 0.0225  4   ASN   B ND2 
4000 N  N   . SER   B 5   ? 0.2014 0.2357 0.1958 -0.0665 -0.0333 0.0295  5   SER   B N   
4001 C  CA  . SER   B 5   ? 0.2307 0.2760 0.2177 -0.0550 -0.0105 0.0322  5   SER   B CA  
4002 C  C   . SER   B 5   ? 0.2527 0.2866 0.2483 -0.0750 0.0147  0.0344  5   SER   B C   
4003 O  O   . SER   B 5   ? 0.2711 0.2836 0.3259 -0.0696 0.0510  0.0301  5   SER   B O   
4004 C  CB  . SER   B 5   ? 0.2423 0.3022 0.2434 -0.0429 0.0014  0.0451  5   SER   B CB  
4005 O  OG  . SER   B 5   ? 0.2695 0.3365 0.3018 -0.0310 0.0000  0.0508  5   SER   B OG  
4011 N  N   . PHE   B 6   ? 0.2775 0.3100 0.2293 -0.0835 0.0316  0.0478  6   PHE   B N   
4012 C  CA  . PHE   B 6   ? 0.2887 0.3179 0.1981 -0.1028 0.0383  0.0286  6   PHE   B CA  
4013 C  C   . PHE   B 6   ? 0.3412 0.3551 0.2470 -0.1076 0.0625  -0.0035 6   PHE   B C   
4014 O  O   . PHE   B 6   ? 0.3550 0.3836 0.2750 -0.0952 0.0487  -0.0213 6   PHE   B O   
4015 C  CB  . PHE   B 6   ? 0.2561 0.2940 0.1887 -0.0925 0.0139  0.0243  6   PHE   B CB  
4016 C  CG  . PHE   B 6   ? 0.2216 0.2557 0.1873 -0.0814 -0.0032 0.0230  6   PHE   B CG  
4017 C  CD1 . PHE   B 6   ? 0.2197 0.2281 0.1769 -0.0772 -0.0239 0.0177  6   PHE   B CD1 
4018 C  CD2 . PHE   B 6   ? 0.1959 0.2493 0.1866 -0.0650 0.0014  0.0448  6   PHE   B CD2 
4019 C  CE1 . PHE   B 6   ? 0.2118 0.2054 0.1818 -0.0672 -0.0285 0.0124  6   PHE   B CE1 
4020 C  CE2 . PHE   B 6   ? 0.1953 0.2345 0.2185 -0.0524 0.0057  0.0423  6   PHE   B CE2 
4021 C  CZ  . PHE   B 6   ? 0.1991 0.2134 0.2061 -0.0556 -0.0090 0.0221  6   PHE   B CZ  
4031 N  N   . SER   B 7   ? 0.3766 0.3438 0.2621 -0.1320 0.0961  -0.0271 7   SER   B N   
4032 C  CA  . SER   B 7   ? 0.4164 0.3677 0.3247 -0.1320 0.1211  -0.0349 7   SER   B CA  
4033 C  C   . SER   B 7   ? 0.4192 0.3421 0.3035 -0.1377 0.1373  -0.0559 7   SER   B C   
4034 O  O   . SER   B 7   ? 0.4318 0.3424 0.3248 -0.1429 0.1411  -0.0552 7   SER   B O   
4035 C  CB  . SER   B 7   ? 0.4435 0.3993 0.3980 -0.1271 0.1436  -0.0263 7   SER   B CB  
4036 O  OG  . SER   B 7   ? 0.4608 0.4036 0.4564 -0.1230 0.1458  -0.0152 7   SER   B OG  
4042 N  N   . GLY   B 8   ? 0.4164 0.3267 0.2993 -0.1236 0.1406  -0.0699 8   GLY   B N   
4043 C  CA  . GLY   B 8   ? 0.4031 0.3087 0.3040 -0.1132 0.1360  -0.0790 8   GLY   B CA  
4044 C  C   . GLY   B 8   ? 0.3811 0.2774 0.2958 -0.1114 0.1377  -0.0689 8   GLY   B C   
4045 O  O   . GLY   B 8   ? 0.3930 0.2841 0.3306 -0.1008 0.1413  -0.0794 8   GLY   B O   
4049 N  N   . TYR   B 9   ? 0.3605 0.2527 0.2691 -0.0992 0.1123  -0.0735 9   TYR   B N   
4050 C  CA  . TYR   B 9   ? 0.3381 0.2219 0.2452 -0.0854 0.0852  -0.0583 9   TYR   B CA  
4051 C  C   . TYR   B 9   ? 0.3286 0.2162 0.2330 -0.0768 0.0559  -0.0463 9   TYR   B C   
4052 O  O   . TYR   B 9   ? 0.3384 0.2310 0.2773 -0.0751 0.0500  -0.0371 9   TYR   B O   
4053 C  CB  . TYR   B 9   ? 0.3276 0.1934 0.2503 -0.0818 0.0792  -0.0479 9   TYR   B CB  
4054 C  CG  . TYR   B 9   ? 0.3172 0.1754 0.2522 -0.0838 0.0667  -0.0530 9   TYR   B CG  
4055 C  CD1 . TYR   B 9   ? 0.3170 0.1789 0.2594 -0.0920 0.0700  -0.0545 9   TYR   B CD1 
4056 C  CD2 . TYR   B 9   ? 0.3046 0.1723 0.2452 -0.0745 0.0617  -0.0563 9   TYR   B CD2 
4057 C  CE1 . TYR   B 9   ? 0.3129 0.1867 0.2510 -0.0871 0.0766  -0.0720 9   TYR   B CE1 
4058 C  CE2 . TYR   B 9   ? 0.3023 0.1684 0.2531 -0.0730 0.0693  -0.0550 9   TYR   B CE2 
4059 C  CZ  . TYR   B 9   ? 0.3034 0.1854 0.2513 -0.0804 0.0697  -0.0803 9   TYR   B CZ  
4060 O  OH  . TYR   B 9   ? 0.2955 0.1997 0.2750 -0.0891 0.0662  -0.0849 9   TYR   B OH  
4070 N  N   . LEU   B 10  ? 0.3128 0.1907 0.2078 -0.0752 0.0343  -0.0442 10  LEU   B N   
4071 C  CA  . LEU   B 10  ? 0.3075 0.1868 0.2175 -0.0876 -0.0049 -0.0390 10  LEU   B CA  
4072 C  C   . LEU   B 10  ? 0.2855 0.1865 0.2178 -0.0841 -0.0276 -0.0380 10  LEU   B C   
4073 O  O   . LEU   B 10  ? 0.2657 0.1913 0.2225 -0.0685 -0.0200 -0.0255 10  LEU   B O   
4074 C  CB  . LEU   B 10  ? 0.3249 0.1876 0.2353 -0.0897 -0.0294 -0.0201 10  LEU   B CB  
4075 C  CG  . LEU   B 10  ? 0.3428 0.1992 0.2646 -0.0804 -0.0597 -0.0086 10  LEU   B CG  
4076 C  CD1 . LEU   B 10  ? 0.3550 0.2100 0.2923 -0.0787 -0.0562 -0.0051 10  LEU   B CD1 
4077 C  CD2 . LEU   B 10  ? 0.3511 0.2040 0.2915 -0.0808 -0.0521 0.0123  10  LEU   B CD2 
4089 N  N   . LYS   B 11  ? 0.3013 0.2141 0.2230 -0.0723 -0.0318 -0.0201 11  LYS   B N   
4090 C  CA  . LYS   B 11  ? 0.3145 0.2385 0.2592 -0.0597 -0.0476 -0.0203 11  LYS   B CA  
4091 C  C   . LYS   B 11  ? 0.2922 0.2175 0.2615 -0.0772 -0.0540 -0.0350 11  LYS   B C   
4092 O  O   . LYS   B 11  ? 0.3086 0.2372 0.2987 -0.0893 -0.0534 -0.0668 11  LYS   B O   
4093 C  CB  . LYS   B 11  ? 0.3513 0.2906 0.3324 -0.0328 -0.0489 -0.0165 11  LYS   B CB  
4094 C  CG  . LYS   B 11  ? 0.3811 0.3256 0.4072 -0.0166 -0.0590 -0.0206 11  LYS   B CG  
4095 C  CD  . LYS   B 11  ? 0.4040 0.3514 0.4729 -0.0066 -0.0615 -0.0258 11  LYS   B CD  
4096 C  CE  . LYS   B 11  ? 0.4215 0.3697 0.5234 -0.0015 -0.0608 -0.0289 11  LYS   B CE  
4097 N  NZ  . LYS   B 11  ? 0.4321 0.3792 0.5502 0.0022  -0.0611 -0.0272 11  LYS   B NZ  
4111 N  N   . LEU   B 12  ? 0.2566 0.1944 0.2608 -0.0653 -0.0508 -0.0320 12  LEU   B N   
4112 C  CA  . LEU   B 12  ? 0.2375 0.1744 0.2677 -0.0582 -0.0435 -0.0266 12  LEU   B CA  
4113 C  C   . LEU   B 12  ? 0.2278 0.1736 0.2748 -0.0596 -0.0556 -0.0182 12  LEU   B C   
4114 O  O   . LEU   B 12  ? 0.2274 0.1743 0.2868 -0.0735 -0.0717 -0.0091 12  LEU   B O   
4115 C  CB  . LEU   B 12  ? 0.2350 0.1540 0.2662 -0.0506 -0.0320 -0.0234 12  LEU   B CB  
4116 C  CG  . LEU   B 12  ? 0.2338 0.1503 0.2711 -0.0507 -0.0244 -0.0210 12  LEU   B CG  
4117 C  CD1 . LEU   B 12  ? 0.2472 0.1523 0.2684 -0.0331 -0.0196 0.0029  12  LEU   B CD1 
4118 C  CD2 . LEU   B 12  ? 0.2419 0.1598 0.2837 -0.0495 -0.0175 -0.0296 12  LEU   B CD2 
4130 N  N   . THR   B 13  ? 0.2161 0.1749 0.2794 -0.0601 -0.0589 -0.0315 13  THR   B N   
4131 C  CA  . THR   B 13  ? 0.2165 0.1868 0.2703 -0.0630 -0.0668 -0.0136 13  THR   B CA  
4132 C  C   . THR   B 13  ? 0.2622 0.2070 0.2885 -0.0727 -0.0837 -0.0088 13  THR   B C   
4133 O  O   . THR   B 13  ? 0.2811 0.2036 0.3083 -0.0740 -0.0521 -0.0086 13  THR   B O   
4134 C  CB  . THR   B 13  ? 0.1950 0.1850 0.2754 -0.0542 -0.0585 -0.0113 13  THR   B CB  
4135 O  OG1 . THR   B 13  ? 0.1823 0.1776 0.2809 -0.0385 -0.0440 -0.0220 13  THR   B OG1 
4136 C  CG2 . THR   B 13  ? 0.1997 0.1897 0.2762 -0.0506 -0.0459 0.0024  13  THR   B CG2 
4144 N  N   A ASP   B 14  ? 0.2735 0.2177 0.2926 -0.0836 -0.1168 -0.0055 14  ASP   B N   
4145 N  N   B ASP   B 14  ? 0.2716 0.2162 0.2932 -0.0759 -0.0924 -0.0026 14  ASP   B N   
4146 C  CA  A ASP   B 14  ? 0.2862 0.2335 0.3296 -0.0844 -0.1120 0.0160  14  ASP   B CA  
4147 C  CA  B ASP   B 14  ? 0.2786 0.2277 0.3135 -0.0746 -0.0876 0.0117  14  ASP   B CA  
4148 C  C   A ASP   B 14  ? 0.2727 0.2173 0.2974 -0.0856 -0.0943 0.0202  14  ASP   B C   
4149 C  C   B ASP   B 14  ? 0.2628 0.2090 0.2856 -0.0751 -0.0874 0.0130  14  ASP   B C   
4150 O  O   A ASP   B 14  ? 0.2969 0.2354 0.3031 -0.0854 -0.0903 0.0288  14  ASP   B O   
4151 O  O   B ASP   B 14  ? 0.2750 0.2117 0.2848 -0.0723 -0.0885 0.0118  14  ASP   B O   
4152 C  CB  A ASP   B 14  ? 0.3097 0.2688 0.4037 -0.0798 -0.1190 0.0167  14  ASP   B CB  
4153 C  CB  B ASP   B 14  ? 0.2984 0.2571 0.3649 -0.0696 -0.0807 0.0147  14  ASP   B CB  
4154 C  CG  A ASP   B 14  ? 0.3356 0.3028 0.4788 -0.0723 -0.1169 0.0044  14  ASP   B CG  
4155 C  CG  B ASP   B 14  ? 0.3172 0.2810 0.4140 -0.0619 -0.0716 0.0101  14  ASP   B CG  
4156 O  OD1 A ASP   B 14  ? 0.3474 0.3115 0.4975 -0.0769 -0.1193 -0.0103 14  ASP   B OD1 
4157 O  OD1 B ASP   B 14  ? 0.3234 0.2906 0.4264 -0.0598 -0.0653 0.0064  14  ASP   B OD1 
4158 O  OD2 A ASP   B 14  ? 0.3425 0.3197 0.5154 -0.0665 -0.1114 0.0086  14  ASP   B OD2 
4159 O  OD2 B ASP   B 14  ? 0.3226 0.2877 0.4357 -0.0631 -0.0712 0.0109  14  ASP   B OD2 
4168 N  N   . ASN   B 15  ? 0.2349 0.1892 0.2676 -0.0694 -0.0910 0.0152  15  ASN   B N   
4169 C  CA  . ASN   B 15  ? 0.1899 0.1622 0.2539 -0.0425 -0.0676 0.0058  15  ASN   B CA  
4170 C  C   . ASN   B 15  ? 0.1734 0.1431 0.2355 -0.0273 -0.0549 -0.0024 15  ASN   B C   
4171 O  O   . ASN   B 15  ? 0.1720 0.1391 0.2431 -0.0284 -0.0565 -0.0121 15  ASN   B O   
4172 C  CB  . ASN   B 15  ? 0.1792 0.1571 0.2527 -0.0184 -0.0650 0.0115  15  ASN   B CB  
4173 C  CG  . ASN   B 15  ? 0.1628 0.1528 0.2654 -0.0291 -0.0345 0.0125  15  ASN   B CG  
4174 O  OD1 . ASN   B 15  ? 0.1711 0.1840 0.2883 -0.0491 -0.0351 0.0213  15  ASN   B OD1 
4175 N  ND2 . ASN   B 15  ? 0.1561 0.1328 0.2534 -0.0186 -0.0079 -0.0040 15  ASN   B ND2 
4183 N  N   . VAL   B 16  ? 0.1745 0.1368 0.2216 -0.0375 -0.0543 -0.0042 16  VAL   B N   
4184 C  CA  . VAL   B 16  ? 0.1754 0.1414 0.2107 -0.0290 -0.0479 -0.0161 16  VAL   B CA  
4185 C  C   . VAL   B 16  ? 0.1741 0.1560 0.2065 -0.0395 -0.0436 -0.0124 16  VAL   B C   
4186 O  O   . VAL   B 16  ? 0.1749 0.1667 0.2296 -0.0363 -0.0359 -0.0244 16  VAL   B O   
4187 C  CB  . VAL   B 16  ? 0.1772 0.1423 0.2226 -0.0165 -0.0301 -0.0208 16  VAL   B CB  
4188 C  CG1 . VAL   B 16  ? 0.1848 0.1361 0.2112 -0.0081 -0.0246 -0.0130 16  VAL   B CG1 
4189 C  CG2 . VAL   B 16  ? 0.1750 0.1466 0.2397 -0.0127 -0.0244 -0.0209 16  VAL   B CG2 
4199 N  N   . TYR   B 17  ? 0.1791 0.1629 0.2030 -0.0343 -0.0397 -0.0112 17  TYR   B N   
4200 C  CA  . TYR   B 17  ? 0.1889 0.1777 0.1969 -0.0457 -0.0331 0.0090  17  TYR   B CA  
4201 C  C   . TYR   B 17  ? 0.1782 0.1468 0.2005 -0.0524 -0.0171 -0.0149 17  TYR   B C   
4202 O  O   . TYR   B 17  ? 0.1765 0.1522 0.2164 -0.0398 -0.0299 -0.0331 17  TYR   B O   
4203 C  CB  . TYR   B 17  ? 0.2268 0.2268 0.2211 -0.0307 -0.0429 0.0426  17  TYR   B CB  
4204 C  CG  . TYR   B 17  ? 0.2558 0.2865 0.2727 -0.0234 -0.0588 0.0516  17  TYR   B CG  
4205 C  CD1 . TYR   B 17  ? 0.2713 0.3056 0.2968 -0.0207 -0.0693 0.0620  17  TYR   B CD1 
4206 C  CD2 . TYR   B 17  ? 0.2778 0.3168 0.3014 -0.0134 -0.0645 0.0519  17  TYR   B CD2 
4207 C  CE1 . TYR   B 17  ? 0.2882 0.3297 0.3182 -0.0129 -0.0804 0.0600  17  TYR   B CE1 
4208 C  CE2 . TYR   B 17  ? 0.2943 0.3375 0.3282 -0.0013 -0.0782 0.0610  17  TYR   B CE2 
4209 C  CZ  . TYR   B 17  ? 0.3037 0.3466 0.3363 -0.0009 -0.0880 0.0618  17  TYR   B CZ  
4210 O  OH  . TYR   B 17  ? 0.3187 0.3657 0.3603 0.0074  -0.0960 0.0575  17  TYR   B OH  
4220 N  N   . ILE   B 18  ? 0.1945 0.1525 0.1874 -0.0459 -0.0092 -0.0205 18  ILE   B N   
4221 C  CA  . ILE   B 18  ? 0.1962 0.1463 0.1919 -0.0464 -0.0104 -0.0230 18  ILE   B CA  
4222 C  C   . ILE   B 18  ? 0.2124 0.1494 0.1953 -0.0557 -0.0079 -0.0325 18  ILE   B C   
4223 O  O   . ILE   B 18  ? 0.2329 0.1632 0.2107 -0.0465 -0.0009 -0.0423 18  ILE   B O   
4224 C  CB  . ILE   B 18  ? 0.1988 0.1474 0.2002 -0.0457 -0.0110 -0.0234 18  ILE   B CB  
4225 C  CG1 . ILE   B 18  ? 0.1963 0.1533 0.2006 -0.0420 -0.0032 -0.0165 18  ILE   B CG1 
4226 C  CG2 . ILE   B 18  ? 0.2047 0.1551 0.2077 -0.0473 -0.0151 -0.0131 18  ILE   B CG2 
4227 C  CD1 . ILE   B 18  ? 0.2047 0.1799 0.2209 -0.0380 -0.0236 0.0079  18  ILE   B CD1 
4239 N  N   . LYS   B 19  ? 0.2103 0.1496 0.2142 -0.0345 0.0328  -0.0338 19  LYS   B N   
4240 C  CA  . LYS   B 19  ? 0.2156 0.1580 0.2379 -0.0407 0.0299  -0.0463 19  LYS   B CA  
4241 C  C   . LYS   B 19  ? 0.1994 0.1495 0.2349 -0.0354 0.0380  -0.0579 19  LYS   B C   
4242 O  O   . LYS   B 19  ? 0.1883 0.1572 0.2242 -0.0240 0.0224  -0.0545 19  LYS   B O   
4243 C  CB  . LYS   B 19  ? 0.2425 0.1747 0.2413 -0.0411 0.0362  -0.0446 19  LYS   B CB  
4244 C  CG  . LYS   B 19  ? 0.2662 0.1993 0.2687 -0.0489 0.0391  -0.0421 19  LYS   B CG  
4245 C  CD  . LYS   B 19  ? 0.2911 0.2294 0.2743 -0.0536 0.0551  -0.0375 19  LYS   B CD  
4246 C  CE  . LYS   B 19  ? 0.3211 0.2589 0.2917 -0.0501 0.0529  -0.0339 19  LYS   B CE  
4247 N  NZ  . LYS   B 19  ? 0.3441 0.2771 0.2981 -0.0543 0.0598  -0.0260 19  LYS   B NZ  
4261 N  N   . ASN   B 20  ? 0.1990 0.1664 0.2791 -0.0288 0.0467  -0.0646 20  ASN   B N   
4262 C  CA  . ASN   B 20  ? 0.1963 0.1824 0.3043 -0.0186 0.0500  -0.0854 20  ASN   B CA  
4263 C  C   . ASN   B 20  ? 0.1942 0.1995 0.2990 -0.0283 0.0535  -0.0913 20  ASN   B C   
4264 O  O   . ASN   B 20  ? 0.2114 0.2411 0.3106 -0.0422 0.0532  -0.0888 20  ASN   B O   
4265 C  CB  . ASN   B 20  ? 0.2206 0.1873 0.3378 0.0030  0.0395  -0.0879 20  ASN   B CB  
4266 C  CG  . ASN   B 20  ? 0.2494 0.1937 0.3602 0.0350  0.0363  -0.1005 20  ASN   B CG  
4267 O  OD1 . ASN   B 20  ? 0.2836 0.2206 0.3870 0.0514  0.0337  -0.0973 20  ASN   B OD1 
4268 N  ND2 . ASN   B 20  ? 0.2390 0.2001 0.3514 0.0358  0.0232  -0.0938 20  ASN   B ND2 
4275 N  N   . ALA   B 21  ? 0.1965 0.1777 0.2946 -0.0322 0.0576  -0.0727 21  ALA   B N   
4276 C  CA  . ALA   B 21  ? 0.2062 0.1863 0.3009 -0.0363 0.0420  -0.0579 21  ALA   B CA  
4277 C  C   . ALA   B 21  ? 0.2051 0.1607 0.2802 -0.0268 0.0438  -0.0388 21  ALA   B C   
4278 O  O   . ALA   B 21  ? 0.2090 0.1551 0.2851 -0.0338 0.0389  -0.0287 21  ALA   B O   
4279 C  CB  . ALA   B 21  ? 0.2224 0.2118 0.3077 -0.0499 0.0395  -0.0441 21  ALA   B CB  
4285 N  N   . ASP   B 22  ? 0.1958 0.1520 0.2761 -0.0257 0.0397  -0.0316 22  ASP   B N   
4286 C  CA  . ASP   B 22  ? 0.1872 0.1419 0.2634 -0.0139 0.0350  -0.0248 22  ASP   B CA  
4287 C  C   . ASP   B 22  ? 0.1786 0.1405 0.2350 -0.0210 0.0229  -0.0123 22  ASP   B C   
4288 O  O   . ASP   B 22  ? 0.1783 0.1491 0.2348 -0.0157 0.0167  -0.0095 22  ASP   B O   
4289 C  CB  . ASP   B 22  ? 0.1942 0.1551 0.3049 -0.0075 0.0384  -0.0144 22  ASP   B CB  
4290 C  CG  . ASP   B 22  ? 0.1965 0.1769 0.3563 0.0005  0.0110  -0.0127 22  ASP   B CG  
4291 O  OD1 . ASP   B 22  ? 0.2004 0.1686 0.3493 -0.0016 -0.0086 -0.0111 22  ASP   B OD1 
4292 O  OD2 . ASP   B 22  ? 0.2122 0.2015 0.4155 0.0123  -0.0111 -0.0219 22  ASP   B OD2 
4297 N  N   . ILE   B 23  ? 0.1809 0.1364 0.2079 -0.0144 0.0058  0.0158  23  ILE   B N   
4298 C  CA  . ILE   B 23  ? 0.1685 0.1315 0.1839 -0.0139 -0.0044 0.0079  23  ILE   B CA  
4299 C  C   . ILE   B 23  ? 0.1586 0.1328 0.1806 -0.0055 -0.0093 -0.0001 23  ILE   B C   
4300 O  O   . ILE   B 23  ? 0.1504 0.1339 0.1770 -0.0089 -0.0033 0.0097  23  ILE   B O   
4301 C  CB  . ILE   B 23  ? 0.1616 0.1430 0.2004 -0.0187 -0.0022 0.0125  23  ILE   B CB  
4302 C  CG1 . ILE   B 23  ? 0.1542 0.1507 0.2186 -0.0126 0.0008  0.0225  23  ILE   B CG1 
4303 C  CG2 . ILE   B 23  ? 0.1666 0.1623 0.2039 -0.0151 0.0009  0.0111  23  ILE   B CG2 
4304 C  CD1 . ILE   B 23  ? 0.1604 0.1621 0.2229 -0.0063 -0.0017 0.0184  23  ILE   B CD1 
4316 N  N   . VAL   B 24  ? 0.1626 0.1317 0.1887 -0.0083 -0.0125 0.0034  24  VAL   B N   
4317 C  CA  . VAL   B 24  ? 0.1503 0.1426 0.2138 -0.0095 -0.0173 -0.0015 24  VAL   B CA  
4318 C  C   . VAL   B 24  ? 0.1502 0.1468 0.2254 -0.0220 -0.0078 0.0005  24  VAL   B C   
4319 O  O   . VAL   B 24  ? 0.1481 0.1541 0.2353 -0.0205 -0.0024 0.0091  24  VAL   B O   
4320 C  CB  . VAL   B 24  ? 0.1629 0.1622 0.2080 0.0008  -0.0239 0.0007  24  VAL   B CB  
4321 C  CG1 . VAL   B 24  ? 0.1636 0.1689 0.2415 -0.0070 -0.0311 0.0002  24  VAL   B CG1 
4322 C  CG2 . VAL   B 24  ? 0.1731 0.1927 0.2140 0.0002  -0.0210 -0.0112 24  VAL   B CG2 
4332 N  N   . GLU   B 25  ? 0.1741 0.1607 0.2276 -0.0166 0.0063  0.0058  25  GLU   B N   
4333 C  CA  . GLU   B 25  ? 0.1822 0.1838 0.2494 -0.0080 0.0213  -0.0002 25  GLU   B CA  
4334 C  C   . GLU   B 25  ? 0.1786 0.1741 0.2167 -0.0208 0.0215  0.0015  25  GLU   B C   
4335 O  O   . GLU   B 25  ? 0.1795 0.1885 0.2281 -0.0161 0.0251  -0.0025 25  GLU   B O   
4336 C  CB  . GLU   B 25  ? 0.2198 0.2262 0.3189 0.0161  0.0346  -0.0069 25  GLU   B CB  
4337 C  CG  . GLU   B 25  ? 0.2692 0.2790 0.4203 0.0232  0.0245  -0.0094 25  GLU   B CG  
4338 C  CD  . GLU   B 25  ? 0.3119 0.3370 0.5018 0.0213  0.0199  -0.0071 25  GLU   B CD  
4339 O  OE1 . GLU   B 25  ? 0.3299 0.3641 0.5326 0.0280  0.0273  -0.0038 25  GLU   B OE1 
4340 O  OE2 . GLU   B 25  ? 0.3223 0.3553 0.5338 0.0214  0.0142  -0.0133 25  GLU   B OE2 
4347 N  N   . GLU   B 26  ? 0.1807 0.1637 0.1880 -0.0290 0.0140  -0.0017 26  GLU   B N   
4348 C  CA  . GLU   B 26  ? 0.1821 0.1817 0.1989 -0.0371 -0.0056 0.0027  26  GLU   B CA  
4349 C  C   . GLU   B 26  ? 0.1617 0.1814 0.1780 -0.0294 0.0071  0.0151  26  GLU   B C   
4350 O  O   . GLU   B 26  ? 0.1795 0.2039 0.1866 -0.0282 0.0029  0.0221  26  GLU   B O   
4351 C  CB  . GLU   B 26  ? 0.2137 0.2032 0.2157 -0.0491 0.0057  0.0203  26  GLU   B CB  
4352 C  CG  . GLU   B 26  ? 0.2574 0.2455 0.2661 -0.0566 0.0154  -0.0066 26  GLU   B CG  
4353 C  CD  . GLU   B 26  ? 0.2867 0.2701 0.2778 -0.0772 0.0320  -0.0413 26  GLU   B CD  
4354 O  OE1 . GLU   B 26  ? 0.3081 0.2592 0.2890 -0.0910 0.0753  -0.0401 26  GLU   B OE1 
4355 O  OE2 . GLU   B 26  ? 0.2935 0.3077 0.3158 -0.0687 0.0298  -0.0337 26  GLU   B OE2 
4362 N  N   . ALA   B 27  ? 0.1468 0.1646 0.1728 -0.0293 0.0096  0.0177  27  ALA   B N   
4363 C  CA  . ALA   B 27  ? 0.1486 0.1634 0.1923 -0.0224 -0.0003 0.0344  27  ALA   B CA  
4364 C  C   . ALA   B 27  ? 0.1516 0.1733 0.2225 -0.0155 0.0075  0.0423  27  ALA   B C   
4365 O  O   . ALA   B 27  ? 0.1647 0.1822 0.2343 -0.0052 0.0110  0.0526  27  ALA   B O   
4366 C  CB  . ALA   B 27  ? 0.1643 0.1448 0.2049 -0.0186 0.0059  0.0307  27  ALA   B CB  
4372 N  N   . LYS   B 28  ? 0.1459 0.1953 0.2664 -0.0230 0.0191  0.0596  28  LYS   B N   
4373 C  CA  . LYS   B 28  ? 0.1648 0.2366 0.2868 -0.0138 0.0648  0.0824  28  LYS   B CA  
4374 C  C   . LYS   B 28  ? 0.1935 0.2480 0.2737 -0.0084 0.0721  0.0725  28  LYS   B C   
4375 O  O   . LYS   B 28  ? 0.2158 0.2499 0.2855 -0.0106 0.0675  0.0676  28  LYS   B O   
4376 C  CB  . LYS   B 28  ? 0.1816 0.2737 0.3419 0.0016  0.0925  0.0997  28  LYS   B CB  
4377 C  CG  . LYS   B 28  ? 0.2106 0.3144 0.3875 0.0068  0.0964  0.1187  28  LYS   B CG  
4378 C  CD  . LYS   B 28  ? 0.2630 0.3699 0.4500 0.0117  0.1020  0.1211  28  LYS   B CD  
4379 C  CE  . LYS   B 28  ? 0.3005 0.4123 0.4961 0.0219  0.1000  0.1271  28  LYS   B CE  
4380 N  NZ  . LYS   B 28  ? 0.3414 0.4156 0.5214 0.0315  0.0997  0.1353  28  LYS   B NZ  
4394 N  N   . LYS   B 29  ? 0.2094 0.2711 0.2752 0.0084  0.0681  0.0592  29  LYS   B N   
4395 C  CA  . LYS   B 29  ? 0.2531 0.3073 0.3010 0.0114  0.0669  0.0574  29  LYS   B CA  
4396 C  C   . LYS   B 29  ? 0.2454 0.3067 0.2618 0.0125  0.0470  0.0730  29  LYS   B C   
4397 O  O   . LYS   B 29  ? 0.2669 0.3284 0.2735 0.0211  0.0441  0.0796  29  LYS   B O   
4398 C  CB  . LYS   B 29  ? 0.3142 0.3461 0.3857 0.0087  0.0672  0.0451  29  LYS   B CB  
4399 C  CG  . LYS   B 29  ? 0.3625 0.3784 0.4707 0.0056  0.0698  0.0416  29  LYS   B CG  
4400 C  CD  . LYS   B 29  ? 0.4041 0.4012 0.5408 0.0007  0.0791  0.0332  29  LYS   B CD  
4401 C  CE  . LYS   B 29  ? 0.4350 0.4155 0.5894 -0.0037 0.0886  0.0291  29  LYS   B CE  
4402 N  NZ  . LYS   B 29  ? 0.4414 0.4228 0.6131 -0.0048 0.0927  0.0260  29  LYS   B NZ  
4416 N  N   . VAL   B 30  ? 0.2107 0.2835 0.2396 -0.0013 0.0313  0.0709  30  VAL   B N   
4417 C  CA  . VAL   B 30  ? 0.2015 0.2725 0.2644 -0.0127 -0.0012 0.0728  30  VAL   B CA  
4418 C  C   . VAL   B 30  ? 0.1849 0.2599 0.2566 -0.0164 -0.0045 0.0879  30  VAL   B C   
4419 O  O   . VAL   B 30  ? 0.1987 0.2725 0.2605 -0.0097 0.0022  0.1027  30  VAL   B O   
4420 C  CB  . VAL   B 30  ? 0.2075 0.2711 0.3079 -0.0234 -0.0289 0.0682  30  VAL   B CB  
4421 C  CG1 . VAL   B 30  ? 0.2161 0.2834 0.3167 -0.0236 -0.0276 0.0592  30  VAL   B CG1 
4422 C  CG2 . VAL   B 30  ? 0.2219 0.2674 0.3312 -0.0313 -0.0344 0.0569  30  VAL   B CG2 
4432 N  N   A LYS   B 31  ? 0.1721 0.2335 0.2787 -0.0339 0.0002  0.1009  31  LYS   B N   
4433 N  N   B LYS   B 31  ? 0.1872 0.2420 0.2644 -0.0246 -0.0117 0.0818  31  LYS   B N   
4434 C  CA  A LYS   B 31  ? 0.1543 0.2275 0.3051 -0.0472 -0.0030 0.1014  31  LYS   B CA  
4435 C  CA  B LYS   B 31  ? 0.1874 0.2330 0.2764 -0.0301 -0.0214 0.0713  31  LYS   B CA  
4436 C  C   A LYS   B 31  ? 0.1525 0.1898 0.2712 -0.0394 -0.0272 0.0917  31  LYS   B C   
4437 C  C   B LYS   B 31  ? 0.1751 0.1949 0.2471 -0.0332 -0.0415 0.0647  31  LYS   B C   
4438 O  O   A LYS   B 31  ? 0.1555 0.1955 0.2957 -0.0338 -0.0172 0.1044  31  LYS   B O   
4439 O  O   B LYS   B 31  ? 0.1774 0.1987 0.2492 -0.0333 -0.0483 0.0633  31  LYS   B O   
4440 C  CB  A LYS   B 31  ? 0.1667 0.2676 0.3551 -0.0453 0.0255  0.1104  31  LYS   B CB  
4441 C  CB  B LYS   B 31  ? 0.2084 0.2641 0.3152 -0.0244 -0.0086 0.0660  31  LYS   B CB  
4442 C  CG  A LYS   B 31  ? 0.1898 0.3036 0.3971 -0.0445 0.0381  0.1048  31  LYS   B CG  
4443 C  CG  B LYS   B 31  ? 0.2298 0.2896 0.3508 -0.0233 -0.0014 0.0535  31  LYS   B CG  
4444 C  CD  A LYS   B 31  ? 0.2153 0.3446 0.4382 -0.0361 0.0329  0.0903  31  LYS   B CD  
4445 C  CD  B LYS   B 31  ? 0.2473 0.3128 0.3852 -0.0225 -0.0006 0.0419  31  LYS   B CD  
4446 C  CE  A LYS   B 31  ? 0.2373 0.3735 0.4722 -0.0282 0.0230  0.0758  31  LYS   B CE  
4447 C  CE  B LYS   B 31  ? 0.2615 0.3301 0.4139 -0.0209 -0.0017 0.0331  31  LYS   B CE  
4448 N  NZ  A LYS   B 31  ? 0.2577 0.3852 0.4889 -0.0188 0.0128  0.0612  31  LYS   B NZ  
4449 N  NZ  B LYS   B 31  ? 0.2727 0.3412 0.4274 -0.0175 -0.0065 0.0240  31  LYS   B NZ  
4476 N  N   . PRO   B 32  ? 0.1683 0.1586 0.2268 -0.0365 -0.0465 0.0591  32  PRO   B N   
4477 C  CA  . PRO   B 32  ? 0.1799 0.1515 0.1906 -0.0397 -0.0501 0.0350  32  PRO   B CA  
4478 C  C   . PRO   B 32  ? 0.1895 0.1413 0.1862 -0.0433 -0.0637 0.0402  32  PRO   B C   
4479 O  O   . PRO   B 32  ? 0.1984 0.1442 0.2163 -0.0474 -0.0732 0.0356  32  PRO   B O   
4480 C  CB  . PRO   B 32  ? 0.1999 0.1438 0.1851 -0.0471 -0.0317 0.0207  32  PRO   B CB  
4481 C  CG  . PRO   B 32  ? 0.2109 0.1332 0.1856 -0.0349 -0.0474 0.0250  32  PRO   B CG  
4482 C  CD  . PRO   B 32  ? 0.1941 0.1413 0.2070 -0.0285 -0.0603 0.0275  32  PRO   B CD  
4490 N  N   . THR   B 33  ? 0.1943 0.1306 0.1798 -0.0396 -0.0577 0.0236  33  THR   B N   
4491 C  CA  . THR   B 33  ? 0.2009 0.1369 0.1713 -0.0437 -0.0489 0.0258  33  THR   B CA  
4492 C  C   . THR   B 33  ? 0.2028 0.1241 0.1650 -0.0367 -0.0466 0.0193  33  THR   B C   
4493 O  O   . THR   B 33  ? 0.2192 0.1241 0.1815 -0.0465 -0.0491 0.0154  33  THR   B O   
4494 C  CB  . THR   B 33  ? 0.2087 0.1502 0.1845 -0.0242 -0.0558 0.0260  33  THR   B CB  
4495 O  OG1 . THR   B 33  ? 0.1965 0.1551 0.1837 -0.0262 -0.0512 0.0307  33  THR   B OG1 
4496 C  CG2 . THR   B 33  ? 0.2299 0.1617 0.1977 -0.0209 -0.0551 0.0235  33  THR   B CG2 
4504 N  N   . VAL   B 34  ? 0.1840 0.1235 0.1555 -0.0421 -0.0489 0.0202  34  VAL   B N   
4505 C  CA  . VAL   B 34  ? 0.1647 0.1222 0.1539 -0.0292 -0.0424 0.0110  34  VAL   B CA  
4506 C  C   . VAL   B 34  ? 0.1473 0.1180 0.1316 -0.0302 -0.0252 0.0080  34  VAL   B C   
4507 O  O   . VAL   B 34  ? 0.1643 0.1236 0.1448 -0.0296 -0.0380 0.0053  34  VAL   B O   
4508 C  CB  . VAL   B 34  ? 0.1711 0.1298 0.1838 -0.0111 -0.0397 0.0040  34  VAL   B CB  
4509 C  CG1 . VAL   B 34  ? 0.1696 0.1456 0.1752 -0.0090 -0.0166 0.0016  34  VAL   B CG1 
4510 C  CG2 . VAL   B 34  ? 0.1738 0.1337 0.2085 -0.0113 -0.0364 0.0045  34  VAL   B CG2 
4520 N  N   . VAL   B 35  ? 0.1352 0.1190 0.1263 -0.0278 -0.0120 0.0079  35  VAL   B N   
4521 C  CA  . VAL   B 35  ? 0.1323 0.1175 0.1303 -0.0238 -0.0143 0.0115  35  VAL   B CA  
4522 C  C   . VAL   B 35  ? 0.1245 0.1098 0.1360 -0.0223 -0.0160 0.0087  35  VAL   B C   
4523 O  O   . VAL   B 35  ? 0.1348 0.1162 0.1400 -0.0251 -0.0098 -0.0040 35  VAL   B O   
4524 C  CB  . VAL   B 35  ? 0.1365 0.1337 0.1526 -0.0206 0.0004  0.0046  35  VAL   B CB  
4525 C  CG1 . VAL   B 35  ? 0.1332 0.1403 0.1735 -0.0229 -0.0041 -0.0064 35  VAL   B CG1 
4526 C  CG2 . VAL   B 35  ? 0.1340 0.1330 0.1728 -0.0126 0.0006  0.0071  35  VAL   B CG2 
4536 N  N   . VAL   B 36  ? 0.1258 0.1108 0.1399 -0.0213 -0.0169 0.0109  36  VAL   B N   
4537 C  CA  . VAL   B 36  ? 0.1178 0.1103 0.1390 -0.0178 -0.0104 0.0124  36  VAL   B CA  
4538 C  C   . VAL   B 36  ? 0.1172 0.1113 0.1306 -0.0150 -0.0023 0.0036  36  VAL   B C   
4539 O  O   . VAL   B 36  ? 0.1288 0.1206 0.1464 -0.0102 0.0002  -0.0029 36  VAL   B O   
4540 C  CB  . VAL   B 36  ? 0.1218 0.1173 0.1492 -0.0161 -0.0086 0.0110  36  VAL   B CB  
4541 C  CG1 . VAL   B 36  ? 0.1210 0.1294 0.1531 -0.0221 -0.0058 0.0063  36  VAL   B CG1 
4542 C  CG2 . VAL   B 36  ? 0.1264 0.1246 0.1539 -0.0149 -0.0123 0.0084  36  VAL   B CG2 
4552 N  N   . ASN   B 37  ? 0.1208 0.1156 0.1405 -0.0015 -0.0031 0.0066  37  ASN   B N   
4553 C  CA  . ASN   B 37  ? 0.1256 0.1151 0.1498 0.0009  -0.0155 0.0080  37  ASN   B CA  
4554 C  C   . ASN   B 37  ? 0.1216 0.1194 0.1471 -0.0037 -0.0156 0.0065  37  ASN   B C   
4555 O  O   . ASN   B 37  ? 0.1277 0.1263 0.1400 -0.0012 -0.0036 0.0036  37  ASN   B O   
4556 C  CB  . ASN   B 37  ? 0.1263 0.1208 0.1441 -0.0044 -0.0126 0.0090  37  ASN   B CB  
4557 C  CG  . ASN   B 37  ? 0.1279 0.1197 0.1506 -0.0094 -0.0145 0.0030  37  ASN   B CG  
4558 O  OD1 . ASN   B 37  ? 0.1371 0.1277 0.1604 0.0015  -0.0148 0.0032  37  ASN   B OD1 
4559 N  ND2 . ASN   B 37  ? 0.1346 0.1162 0.1494 -0.0026 -0.0186 0.0088  37  ASN   B ND2 
4566 N  N   . ALA   B 38  ? 0.1303 0.1184 0.1462 0.0014  -0.0017 0.0091  38  ALA   B N   
4567 C  CA  . ALA   B 38  ? 0.1373 0.1223 0.1460 -0.0005 -0.0012 0.0136  38  ALA   B CA  
4568 C  C   . ALA   B 38  ? 0.1317 0.1208 0.1516 -0.0045 0.0008  0.0139  38  ALA   B C   
4569 O  O   . ALA   B 38  ? 0.1489 0.1321 0.1634 0.0026  -0.0011 0.0132  38  ALA   B O   
4570 C  CB  . ALA   B 38  ? 0.1621 0.1261 0.1716 -0.0113 0.0008  0.0016  38  ALA   B CB  
4576 N  N   . ALA   B 39  ? 0.1359 0.1196 0.1426 0.0062  -0.0042 0.0089  39  ALA   B N   
4577 C  CA  . ALA   B 39  ? 0.1431 0.1269 0.1484 0.0028  -0.0106 0.0096  39  ALA   B CA  
4578 C  C   . ALA   B 39  ? 0.1499 0.1303 0.1291 0.0029  -0.0052 0.0035  39  ALA   B C   
4579 O  O   . ALA   B 39  ? 0.1576 0.1414 0.1499 -0.0008 -0.0078 0.0122  39  ALA   B O   
4580 C  CB  . ALA   B 39  ? 0.1414 0.1297 0.1621 -0.0088 -0.0032 0.0069  39  ALA   B CB  
4586 N  N   . ASN   B 40  ? 0.1448 0.1525 0.1275 -0.0057 0.0051  -0.0043 40  ASN   B N   
4587 C  CA  . ASN   B 40  ? 0.1541 0.1565 0.1540 -0.0012 -0.0014 -0.0016 40  ASN   B CA  
4588 C  C   . ASN   B 40  ? 0.1619 0.1530 0.1413 0.0064  -0.0096 0.0065  40  ASN   B C   
4589 O  O   . ASN   B 40  ? 0.1569 0.1475 0.1415 0.0118  -0.0111 0.0044  40  ASN   B O   
4590 C  CB  . ASN   B 40  ? 0.1717 0.1554 0.1792 0.0114  -0.0104 0.0145  40  ASN   B CB  
4591 C  CG  . ASN   B 40  ? 0.1754 0.1617 0.2024 0.0061  -0.0209 0.0236  40  ASN   B CG  
4592 O  OD1 . ASN   B 40  ? 0.1755 0.1588 0.2772 0.0062  -0.0320 0.0209  40  ASN   B OD1 
4593 N  ND2 . ASN   B 40  ? 0.1774 0.1598 0.2067 0.0006  -0.0195 0.0231  40  ASN   B ND2 
4600 N  N   . VAL   B 41  ? 0.1726 0.1573 0.1449 0.0120  0.0030  -0.0007 41  VAL   B N   
4601 C  CA  . VAL   B 41  ? 0.1803 0.1679 0.1401 0.0048  0.0036  -0.0031 41  VAL   B CA  
4602 C  C   . VAL   B 41  ? 0.1814 0.1700 0.1351 0.0123  -0.0050 -0.0153 41  VAL   B C   
4603 O  O   . VAL   B 41  ? 0.1775 0.1681 0.1529 0.0105  -0.0095 -0.0153 41  VAL   B O   
4604 C  CB  . VAL   B 41  ? 0.1980 0.1829 0.1671 -0.0079 0.0203  -0.0172 41  VAL   B CB  
4605 C  CG1 . VAL   B 41  ? 0.1968 0.1904 0.1742 -0.0131 0.0269  -0.0227 41  VAL   B CG1 
4606 C  CG2 . VAL   B 41  ? 0.2117 0.2017 0.1805 -0.0149 0.0265  -0.0115 41  VAL   B CG2 
4616 N  N   . TYR   B 42  ? 0.1856 0.1723 0.1334 0.0123  -0.0156 0.0038  42  TYR   B N   
4617 C  CA  . TYR   B 42  ? 0.1908 0.1756 0.1391 0.0153  -0.0236 -0.0038 42  TYR   B CA  
4618 C  C   . TYR   B 42  ? 0.1709 0.1565 0.1577 0.0151  -0.0204 -0.0043 42  TYR   B C   
4619 O  O   . TYR   B 42  ? 0.1692 0.1628 0.1938 0.0120  -0.0268 -0.0095 42  TYR   B O   
4620 C  CB  . TYR   B 42  ? 0.2132 0.2080 0.1576 0.0158  -0.0326 0.0083  42  TYR   B CB  
4621 C  CG  . TYR   B 42  ? 0.2197 0.2220 0.1570 0.0042  -0.0284 0.0245  42  TYR   B CG  
4622 C  CD1 . TYR   B 42  ? 0.2117 0.2198 0.1483 -0.0033 -0.0167 0.0097  42  TYR   B CD1 
4623 C  CD2 . TYR   B 42  ? 0.2328 0.2320 0.1905 0.0103  -0.0168 0.0290  42  TYR   B CD2 
4624 C  CE1 . TYR   B 42  ? 0.2236 0.2347 0.1521 0.0041  -0.0164 0.0164  42  TYR   B CE1 
4625 C  CE2 . TYR   B 42  ? 0.2380 0.2451 0.1781 0.0129  0.0065  0.0422  42  TYR   B CE2 
4626 C  CZ  . TYR   B 42  ? 0.2464 0.2598 0.1740 0.0214  0.0129  0.0229  42  TYR   B CZ  
4627 O  OH  . TYR   B 42  ? 0.2765 0.2929 0.2236 0.0375  0.0199  0.0302  42  TYR   B OH  
4637 N  N   . LEU   B 43  ? 0.1600 0.1460 0.1393 0.0046  -0.0174 -0.0107 43  LEU   B N   
4638 C  CA  . LEU   B 43  ? 0.1617 0.1468 0.1344 -0.0018 -0.0172 -0.0048 43  LEU   B CA  
4639 C  C   . LEU   B 43  ? 0.1631 0.1542 0.1299 -0.0013 -0.0156 0.0076  43  LEU   B C   
4640 O  O   . LEU   B 43  ? 0.1557 0.1530 0.1645 0.0045  -0.0231 0.0074  43  LEU   B O   
4641 C  CB  . LEU   B 43  ? 0.1564 0.1383 0.1452 -0.0051 -0.0192 -0.0054 43  LEU   B CB  
4642 C  CG  . LEU   B 43  ? 0.1618 0.1357 0.1629 0.0012  -0.0242 -0.0058 43  LEU   B CG  
4643 C  CD1 . LEU   B 43  ? 0.1669 0.1433 0.1932 -0.0008 -0.0380 -0.0095 43  LEU   B CD1 
4644 C  CD2 . LEU   B 43  ? 0.1594 0.1349 0.1729 -0.0068 -0.0238 -0.0028 43  LEU   B CD2 
4656 N  N   . LYS   B 44  ? 0.1564 0.1509 0.1394 0.0085  -0.0102 -0.0015 44  LYS   B N   
4657 C  CA  . LYS   B 44  ? 0.1705 0.1557 0.1553 0.0056  -0.0093 0.0074  44  LYS   B CA  
4658 C  C   . LYS   B 44  ? 0.1576 0.1480 0.1598 0.0145  -0.0147 0.0023  44  LYS   B C   
4659 O  O   . LYS   B 44  ? 0.1836 0.1460 0.1825 0.0016  -0.0047 0.0056  44  LYS   B O   
4660 C  CB  . LYS   B 44  ? 0.2003 0.1734 0.1752 0.0174  -0.0272 0.0013  44  LYS   B CB  
4661 C  CG  . LYS   B 44  ? 0.2392 0.2021 0.2136 0.0123  -0.0526 0.0128  44  LYS   B CG  
4662 C  CD  . LYS   B 44  ? 0.2746 0.2254 0.2708 -0.0056 -0.0653 0.0116  44  LYS   B CD  
4663 C  CE  . LYS   B 44  ? 0.3073 0.2581 0.3168 -0.0129 -0.0674 0.0244  44  LYS   B CE  
4664 N  NZ  . LYS   B 44  ? 0.3239 0.2709 0.3440 -0.0147 -0.0764 0.0338  44  LYS   B NZ  
4678 N  N   . HIS   B 45  ? 0.1539 0.1536 0.1451 0.0090  -0.0133 0.0084  45  HIS   B N   
4679 C  CA  . HIS   B 45  ? 0.1526 0.1451 0.1562 0.0113  -0.0111 0.0018  45  HIS   B CA  
4680 C  C   . HIS   B 45  ? 0.1777 0.1675 0.1880 0.0161  -0.0160 -0.0022 45  HIS   B C   
4681 O  O   . HIS   B 45  ? 0.1926 0.2003 0.2391 0.0428  0.0092  0.0028  45  HIS   B O   
4682 C  CB  . HIS   B 45  ? 0.1472 0.1485 0.1577 0.0037  -0.0075 -0.0014 45  HIS   B CB  
4683 C  CG  . HIS   B 45  ? 0.1491 0.1478 0.1523 -0.0080 -0.0127 0.0010  45  HIS   B CG  
4684 N  ND1 . HIS   B 45  ? 0.1555 0.1375 0.1613 0.0012  -0.0207 -0.0066 45  HIS   B ND1 
4685 C  CD2 . HIS   B 45  ? 0.1612 0.1483 0.1599 -0.0155 -0.0148 -0.0038 45  HIS   B CD2 
4686 C  CE1 . HIS   B 45  ? 0.1670 0.1297 0.1463 -0.0042 -0.0264 -0.0076 45  HIS   B CE1 
4687 N  NE2 . HIS   B 45  ? 0.1724 0.1384 0.1467 -0.0073 -0.0209 -0.0079 45  HIS   B NE2 
4695 N  N   A GLY   B 46  ? 0.1897 0.1583 0.2197 0.0194  -0.0375 0.0047  46  GLY   B N   
4696 N  N   B GLY   B 46  ? 0.1887 0.1703 0.2059 0.0193  -0.0308 0.0067  46  GLY   B N   
4697 C  CA  A GLY   B 46  ? 0.2023 0.1696 0.2609 0.0149  -0.0502 0.0018  46  GLY   B CA  
4698 C  CA  B GLY   B 46  ? 0.1988 0.1812 0.2294 0.0175  -0.0407 0.0101  46  GLY   B CA  
4699 C  C   A GLY   B 46  ? 0.2003 0.1861 0.3006 0.0236  -0.0436 0.0006  46  GLY   B C   
4700 C  C   B GLY   B 46  ? 0.2001 0.1946 0.2575 0.0219  -0.0381 0.0141  46  GLY   B C   
4701 O  O   A GLY   B 46  ? 0.2082 0.1972 0.3820 0.0303  -0.0169 -0.0209 46  GLY   B O   
4702 O  O   B GLY   B 46  ? 0.2052 0.2032 0.2750 0.0298  -0.0296 0.0239  46  GLY   B O   
4709 N  N   . GLY   B 47  ? 0.1988 0.1997 0.2740 0.0087  -0.0313 0.0045  47  GLY   B N   
4710 C  CA  . GLY   B 47  ? 0.1879 0.1709 0.2373 0.0038  -0.0226 0.0033  47  GLY   B CA  
4711 C  C   . GLY   B 47  ? 0.1692 0.1536 0.1982 -0.0005 -0.0079 0.0037  47  GLY   B C   
4712 O  O   . GLY   B 47  ? 0.1784 0.1412 0.1988 0.0039  -0.0170 0.0123  47  GLY   B O   
4717 N  N   . GLY   B 48  ? 0.1482 0.1461 0.2067 -0.0008 -0.0182 0.0164  48  GLY   B N   
4718 C  CA  . GLY   B 48  ? 0.1483 0.1330 0.2068 -0.0091 -0.0056 0.0118  48  GLY   B CA  
4719 C  C   . GLY   B 48  ? 0.1396 0.1352 0.1853 -0.0001 0.0086  0.0060  48  GLY   B C   
4720 O  O   . GLY   B 48  ? 0.1398 0.1392 0.2090 0.0011  -0.0033 0.0024  48  GLY   B O   
4724 N  N   . VAL   B 49  ? 0.1411 0.1434 0.1716 0.0121  -0.0035 0.0097  49  VAL   B N   
4725 C  CA  . VAL   B 49  ? 0.1466 0.1462 0.1635 0.0150  -0.0134 -0.0063 49  VAL   B CA  
4726 C  C   . VAL   B 49  ? 0.1426 0.1363 0.1477 0.0178  -0.0039 0.0036  49  VAL   B C   
4727 O  O   . VAL   B 49  ? 0.1512 0.1399 0.1655 0.0055  -0.0033 0.0012  49  VAL   B O   
4728 C  CB  . VAL   B 49  ? 0.1489 0.1570 0.1934 0.0068  -0.0253 -0.0013 49  VAL   B CB  
4729 C  CG1 . VAL   B 49  ? 0.1458 0.1680 0.1835 0.0064  -0.0337 0.0006  49  VAL   B CG1 
4730 C  CG2 . VAL   B 49  ? 0.1686 0.1735 0.2305 -0.0087 -0.0359 0.0024  49  VAL   B CG2 
4740 N  N   . ALA   B 50  ? 0.1345 0.1374 0.1536 0.0033  -0.0049 0.0041  50  ALA   B N   
4741 C  CA  . ALA   B 50  ? 0.1337 0.1274 0.1567 0.0055  -0.0057 0.0039  50  ALA   B CA  
4742 C  C   . ALA   B 50  ? 0.1430 0.1335 0.1570 0.0054  -0.0092 0.0028  50  ALA   B C   
4743 O  O   . ALA   B 50  ? 0.1438 0.1309 0.1518 0.0030  -0.0034 0.0024  50  ALA   B O   
4744 C  CB  . ALA   B 50  ? 0.1414 0.1259 0.1597 0.0015  -0.0027 0.0079  50  ALA   B CB  
4750 N  N   . GLY   B 51  ? 0.1393 0.1409 0.1726 0.0101  -0.0179 0.0125  51  GLY   B N   
4751 C  CA  . GLY   B 51  ? 0.1340 0.1451 0.1893 0.0197  -0.0209 0.0093  51  GLY   B CA  
4752 C  C   . GLY   B 51  ? 0.1384 0.1424 0.1865 0.0196  -0.0071 0.0042  51  GLY   B C   
4753 O  O   . GLY   B 51  ? 0.1409 0.1565 0.2047 0.0066  -0.0129 -0.0014 51  GLY   B O   
4757 N  N   . ALA   B 52  ? 0.1399 0.1399 0.1798 0.0148  -0.0023 0.0099  52  ALA   B N   
4758 C  CA  . ALA   B 52  ? 0.1391 0.1496 0.1863 0.0168  -0.0002 -0.0033 52  ALA   B CA  
4759 C  C   . ALA   B 52  ? 0.1294 0.1489 0.1670 0.0081  -0.0020 -0.0003 52  ALA   B C   
4760 O  O   . ALA   B 52  ? 0.1350 0.1611 0.1856 0.0097  0.0087  0.0042  52  ALA   B O   
4761 C  CB  . ALA   B 52  ? 0.1569 0.1534 0.1934 0.0098  -0.0018 -0.0033 52  ALA   B CB  
4767 N  N   . LEU   B 53  ? 0.1275 0.1402 0.1604 0.0137  0.0046  0.0046  53  LEU   B N   
4768 C  CA  . LEU   B 53  ? 0.1290 0.1467 0.1572 0.0103  -0.0070 0.0044  53  LEU   B CA  
4769 C  C   . LEU   B 53  ? 0.1397 0.1389 0.1546 0.0109  0.0062  0.0073  53  LEU   B C   
4770 O  O   . LEU   B 53  ? 0.1463 0.1504 0.1592 -0.0020 0.0002  0.0120  53  LEU   B O   
4771 C  CB  . LEU   B 53  ? 0.1332 0.1593 0.1632 0.0032  -0.0022 0.0149  53  LEU   B CB  
4772 C  CG  . LEU   B 53  ? 0.1300 0.1657 0.1671 -0.0010 -0.0040 0.0225  53  LEU   B CG  
4773 C  CD1 . LEU   B 53  ? 0.1317 0.1868 0.1973 0.0100  -0.0042 0.0006  53  LEU   B CD1 
4774 C  CD2 . LEU   B 53  ? 0.1460 0.1951 0.2013 -0.0092 -0.0084 -0.0108 53  LEU   B CD2 
4786 N  N   . ASN   B 54  ? 0.1364 0.1326 0.1501 0.0081  -0.0058 0.0027  54  ASN   B N   
4787 C  CA  . ASN   B 54  ? 0.1462 0.1421 0.1619 0.0085  -0.0038 0.0007  54  ASN   B CA  
4788 C  C   . ASN   B 54  ? 0.1404 0.1413 0.1802 0.0038  -0.0035 0.0031  54  ASN   B C   
4789 O  O   . ASN   B 54  ? 0.1353 0.1483 0.1951 -0.0009 0.0027  -0.0033 54  ASN   B O   
4790 C  CB  . ASN   B 54  ? 0.1483 0.1581 0.1743 0.0100  0.0029  0.0030  54  ASN   B CB  
4791 C  CG  . ASN   B 54  ? 0.1417 0.1614 0.1775 0.0088  -0.0062 0.0017  54  ASN   B CG  
4792 O  OD1 . ASN   B 54  ? 0.1369 0.1644 0.1935 0.0043  -0.0141 -0.0102 54  ASN   B OD1 
4793 N  ND2 . ASN   B 54  ? 0.1588 0.1808 0.1977 0.0019  -0.0322 0.0105  54  ASN   B ND2 
4800 N  N   . LYS   B 55  ? 0.1378 0.1558 0.1852 0.0070  -0.0009 0.0017  55  LYS   B N   
4801 C  CA  . LYS   B 55  ? 0.1357 0.1691 0.2062 0.0126  -0.0057 0.0043  55  LYS   B CA  
4802 C  C   . LYS   B 55  ? 0.1336 0.1671 0.2112 0.0109  0.0080  -0.0051 55  LYS   B C   
4803 O  O   . LYS   B 55  ? 0.1289 0.1871 0.2254 0.0126  0.0110  -0.0122 55  LYS   B O   
4804 C  CB  . LYS   B 55  ? 0.1470 0.1883 0.2476 0.0253  0.0028  0.0099  55  LYS   B CB  
4805 C  CG  . LYS   B 55  ? 0.1920 0.2171 0.3308 0.0342  0.0166  0.0210  55  LYS   B CG  
4806 C  CD  . LYS   B 55  ? 0.2315 0.2404 0.4004 0.0427  0.0396  0.0308  55  LYS   B CD  
4807 C  CE  . LYS   B 55  ? 0.2600 0.2628 0.4665 0.0464  0.0617  0.0319  55  LYS   B CE  
4808 N  NZ  . LYS   B 55  ? 0.2699 0.2821 0.5047 0.0440  0.0499  0.0482  55  LYS   B NZ  
4822 N  N   . ALA   B 56  ? 0.1345 0.1653 0.1942 0.0028  0.0053  -0.0094 56  ALA   B N   
4823 C  CA  . ALA   B 56  ? 0.1484 0.1871 0.1897 0.0011  0.0034  -0.0162 56  ALA   B CA  
4824 C  C   . ALA   B 56  ? 0.1498 0.1830 0.1860 0.0012  0.0103  -0.0064 56  ALA   B C   
4825 O  O   . ALA   B 56  ? 0.1609 0.1911 0.2092 0.0062  0.0263  -0.0031 56  ALA   B O   
4826 C  CB  . ALA   B 56  ? 0.1598 0.2058 0.1895 -0.0091 0.0033  -0.0164 56  ALA   B CB  
4832 N  N   . THR   B 57  ? 0.1403 0.1714 0.1938 -0.0004 0.0146  0.0015  57  THR   B N   
4833 C  CA  . THR   B 57  ? 0.1467 0.1682 0.1905 -0.0038 0.0164  0.0060  57  THR   B CA  
4834 C  C   . THR   B 57  ? 0.1414 0.1802 0.2068 -0.0036 0.0201  -0.0004 57  THR   B C   
4835 O  O   . THR   B 57  ? 0.1486 0.1773 0.2221 -0.0243 0.0101  0.0031  57  THR   B O   
4836 C  CB  . THR   B 57  ? 0.1573 0.1560 0.1748 -0.0023 0.0164  0.0156  57  THR   B CB  
4837 O  OG1 . THR   B 57  ? 0.1558 0.1490 0.1946 -0.0029 0.0154  0.0079  57  THR   B OG1 
4838 C  CG2 . THR   B 57  ? 0.1590 0.1602 0.1753 -0.0045 0.0125  0.0109  57  THR   B CG2 
4846 N  N   . ASN   B 58  ? 0.1279 0.2013 0.2340 -0.0053 0.0081  -0.0128 58  ASN   B N   
4847 C  CA  . ASN   B 58  ? 0.1518 0.2450 0.2732 -0.0223 0.0256  -0.0018 58  ASN   B CA  
4848 C  C   . ASN   B 58  ? 0.1377 0.2225 0.2305 -0.0162 -0.0040 0.0059  58  ASN   B C   
4849 O  O   . ASN   B 58  ? 0.1519 0.2284 0.2368 -0.0179 -0.0065 -0.0108 58  ASN   B O   
4850 C  CB  . ASN   B 58  ? 0.2392 0.3168 0.3879 -0.0329 0.0677  0.0078  58  ASN   B CB  
4851 C  CG  . ASN   B 58  ? 0.3459 0.3866 0.5244 -0.0368 0.0907  0.0307  58  ASN   B CG  
4852 O  OD1 . ASN   B 58  ? 0.3713 0.4161 0.5815 -0.0358 0.0906  0.0353  58  ASN   B OD1 
4853 N  ND2 . ASN   B 58  ? 0.4558 0.4558 0.5700 -0.0404 0.1007  0.0392  58  ASN   B ND2 
4860 N  N   . ASN   B 59  ? 0.1380 0.2055 0.2104 -0.0101 -0.0079 0.0102  59  ASN   B N   
4861 C  CA  . ASN   B 59  ? 0.1470 0.2025 0.1935 -0.0077 -0.0110 0.0167  59  ASN   B CA  
4862 C  C   . ASN   B 59  ? 0.1409 0.1929 0.1927 -0.0132 -0.0078 -0.0020 59  ASN   B C   
4863 O  O   . ASN   B 59  ? 0.1454 0.1948 0.1963 -0.0141 -0.0077 -0.0047 59  ASN   B O   
4864 C  CB  . ASN   B 59  ? 0.1553 0.2208 0.2068 -0.0053 -0.0277 0.0155  59  ASN   B CB  
4865 C  CG  . ASN   B 59  ? 0.1658 0.2350 0.2231 -0.0025 -0.0408 0.0107  59  ASN   B CG  
4866 O  OD1 . ASN   B 59  ? 0.1685 0.2379 0.2393 0.0014  -0.0208 0.0268  59  ASN   B OD1 
4867 N  ND2 . ASN   B 59  ? 0.1725 0.2470 0.2373 -0.0110 -0.0472 0.0007  59  ASN   B ND2 
4874 N  N   . ALA   B 60  ? 0.1450 0.1814 0.1908 -0.0128 0.0023  0.0001  60  ALA   B N   
4875 C  CA  . ALA   B 60  ? 0.1508 0.1667 0.1993 -0.0182 -0.0019 0.0051  60  ALA   B CA  
4876 C  C   . ALA   B 60  ? 0.1508 0.1554 0.1721 -0.0129 -0.0041 0.0023  60  ALA   B C   
4877 O  O   . ALA   B 60  ? 0.1548 0.1575 0.1936 -0.0184 0.0041  -0.0068 60  ALA   B O   
4878 C  CB  . ALA   B 60  ? 0.1667 0.1597 0.2217 -0.0178 0.0097  0.0010  60  ALA   B CB  
4884 N  N   . MET   B 61  ? 0.1427 0.1478 0.1685 -0.0068 -0.0018 0.0030  61  MET   B N   
4885 C  CA  . MET   B 61  ? 0.1346 0.1469 0.1678 -0.0050 -0.0107 0.0052  61  MET   B CA  
4886 C  C   . MET   B 61  ? 0.1404 0.1449 0.1739 -0.0127 -0.0074 0.0096  61  MET   B C   
4887 O  O   . MET   B 61  ? 0.1421 0.1400 0.1645 -0.0051 -0.0077 -0.0122 61  MET   B O   
4888 C  CB  . MET   B 61  ? 0.1299 0.1489 0.1703 -0.0021 -0.0137 0.0038  61  MET   B CB  
4889 C  CG  . MET   B 61  ? 0.1330 0.1486 0.1565 -0.0047 -0.0091 0.0113  61  MET   B CG  
4890 S  SD  . MET   B 61  ? 0.1339 0.1447 0.1809 -0.0021 -0.0070 -0.0089 61  MET   B SD  
4891 C  CE  . MET   B 61  ? 0.1430 0.1616 0.1932 0.0048  -0.0011 -0.0215 61  MET   B CE  
4901 N  N   . GLN   B 62  ? 0.1388 0.1507 0.1690 -0.0085 -0.0174 0.0026  62  GLN   B N   
4902 C  CA  . GLN   B 62  ? 0.1381 0.1519 0.1712 -0.0049 -0.0155 0.0004  62  GLN   B CA  
4903 C  C   . GLN   B 62  ? 0.1408 0.1539 0.1722 -0.0033 -0.0243 -0.0002 62  GLN   B C   
4904 O  O   . GLN   B 62  ? 0.1575 0.1550 0.1788 -0.0043 -0.0281 -0.0026 62  GLN   B O   
4905 C  CB  . GLN   B 62  ? 0.1403 0.1595 0.1734 -0.0031 -0.0119 0.0065  62  GLN   B CB  
4906 C  CG  . GLN   B 62  ? 0.1491 0.1619 0.1793 0.0004  -0.0202 -0.0053 62  GLN   B CG  
4907 C  CD  . GLN   B 62  ? 0.1502 0.1582 0.1575 0.0034  -0.0269 0.0035  62  GLN   B CD  
4908 O  OE1 . GLN   B 62  ? 0.1539 0.1533 0.1842 -0.0017 -0.0323 -0.0010 62  GLN   B OE1 
4909 N  NE2 . GLN   B 62  ? 0.1475 0.1647 0.1779 0.0033  -0.0187 -0.0101 62  GLN   B NE2 
4918 N  N   . VAL   B 63  ? 0.1430 0.1590 0.1793 -0.0093 -0.0222 -0.0082 63  VAL   B N   
4919 C  CA  . VAL   B 63  ? 0.1570 0.1622 0.2058 -0.0140 -0.0265 -0.0037 63  VAL   B CA  
4920 C  C   . VAL   B 63  ? 0.1582 0.1525 0.1894 -0.0228 -0.0331 -0.0201 63  VAL   B C   
4921 O  O   . VAL   B 63  ? 0.1686 0.1519 0.2008 -0.0189 -0.0423 -0.0152 63  VAL   B O   
4922 C  CB  . VAL   B 63  ? 0.1551 0.1778 0.2327 -0.0177 -0.0311 -0.0087 63  VAL   B CB  
4923 C  CG1 . VAL   B 63  ? 0.1663 0.1817 0.2460 -0.0246 -0.0236 -0.0143 63  VAL   B CG1 
4924 C  CG2 . VAL   B 63  ? 0.1483 0.2005 0.2454 -0.0134 -0.0327 -0.0092 63  VAL   B CG2 
4934 N  N   . GLU   B 64  ? 0.1575 0.1436 0.1803 -0.0143 -0.0245 -0.0092 64  GLU   B N   
4935 C  CA  . GLU   B 64  ? 0.1570 0.1384 0.1805 -0.0171 -0.0280 -0.0024 64  GLU   B CA  
4936 C  C   . GLU   B 64  ? 0.1472 0.1393 0.1753 -0.0076 -0.0267 -0.0080 64  GLU   B C   
4937 O  O   . GLU   B 64  ? 0.1575 0.1493 0.1682 -0.0096 -0.0256 -0.0135 64  GLU   B O   
4938 C  CB  . GLU   B 64  ? 0.1532 0.1481 0.1883 -0.0242 -0.0258 -0.0028 64  GLU   B CB  
4939 C  CG  . GLU   B 64  ? 0.1630 0.1488 0.1748 -0.0311 -0.0313 -0.0112 64  GLU   B CG  
4940 C  CD  . GLU   B 64  ? 0.1736 0.1605 0.1832 -0.0382 -0.0285 -0.0017 64  GLU   B CD  
4941 O  OE1 . GLU   B 64  ? 0.1739 0.1783 0.1937 -0.0417 -0.0240 -0.0225 64  GLU   B OE1 
4942 O  OE2 . GLU   B 64  ? 0.1854 0.1708 0.1890 -0.0358 -0.0402 -0.0083 64  GLU   B OE2 
4949 N  N   . SER   B 65  ? 0.1498 0.1346 0.1611 -0.0087 -0.0140 -0.0110 65  SER   B N   
4950 C  CA  . SER   B 65  ? 0.1523 0.1309 0.1615 0.0023  -0.0121 -0.0083 65  SER   B CA  
4951 C  C   . SER   B 65  ? 0.1560 0.1339 0.1604 0.0033  -0.0202 -0.0173 65  SER   B C   
4952 O  O   . SER   B 65  ? 0.1588 0.1452 0.1588 -0.0023 -0.0273 -0.0222 65  SER   B O   
4953 C  CB  . SER   B 65  ? 0.1551 0.1349 0.1603 -0.0106 -0.0119 -0.0095 65  SER   B CB  
4954 O  OG  . SER   B 65  ? 0.1519 0.1416 0.1701 -0.0109 -0.0174 -0.0224 65  SER   B OG  
4960 N  N   . ASP   B 66  ? 0.1633 0.1447 0.1648 -0.0036 -0.0274 -0.0178 66  ASP   B N   
4961 C  CA  . ASP   B 66  ? 0.1691 0.1500 0.1617 0.0016  -0.0311 -0.0087 66  ASP   B CA  
4962 C  C   . ASP   B 66  ? 0.1719 0.1503 0.1620 -0.0063 -0.0275 -0.0153 66  ASP   B C   
4963 O  O   . ASP   B 66  ? 0.1731 0.1608 0.1705 0.0019  -0.0253 -0.0195 66  ASP   B O   
4964 C  CB  . ASP   B 66  ? 0.1817 0.1595 0.1892 0.0092  -0.0379 -0.0116 66  ASP   B CB  
4965 C  CG  . ASP   B 66  ? 0.2126 0.1751 0.2161 0.0173  -0.0505 0.0000  66  ASP   B CG  
4966 O  OD1 . ASP   B 66  ? 0.2393 0.1728 0.2227 0.0063  -0.0550 0.0119  66  ASP   B OD1 
4967 O  OD2 . ASP   B 66  ? 0.2325 0.2020 0.2644 0.0350  -0.0441 0.0001  66  ASP   B OD2 
4972 N  N   . ASP   B 67  ? 0.1645 0.1482 0.1542 -0.0123 -0.0244 -0.0226 67  ASP   B N   
4973 C  CA  . ASP   B 67  ? 0.1825 0.1405 0.1659 -0.0070 -0.0220 -0.0107 67  ASP   B CA  
4974 C  C   . ASP   B 67  ? 0.1728 0.1428 0.1793 0.0041  -0.0287 -0.0145 67  ASP   B C   
4975 O  O   . ASP   B 67  ? 0.1778 0.1527 0.1904 0.0028  -0.0154 -0.0220 67  ASP   B O   
4976 C  CB  . ASP   B 67  ? 0.2042 0.1502 0.1883 -0.0172 -0.0375 -0.0092 67  ASP   B CB  
4977 C  CG  . ASP   B 67  ? 0.2387 0.1597 0.2119 -0.0147 -0.0642 -0.0106 67  ASP   B CG  
4978 O  OD1 . ASP   B 67  ? 0.2672 0.1666 0.2238 -0.0153 -0.0636 -0.0113 67  ASP   B OD1 
4979 O  OD2 . ASP   B 67  ? 0.2481 0.1722 0.2276 0.0022  -0.0702 -0.0091 67  ASP   B OD2 
4984 N  N   . TYR   B 68  ? 0.1716 0.1443 0.1660 0.0046  -0.0426 -0.0192 68  TYR   B N   
4985 C  CA  . TYR   B 68  ? 0.1667 0.1574 0.1869 0.0071  -0.0441 -0.0242 68  TYR   B CA  
4986 C  C   . TYR   B 68  ? 0.1600 0.1588 0.1892 0.0003  -0.0348 -0.0353 68  TYR   B C   
4987 O  O   . TYR   B 68  ? 0.1645 0.1707 0.2009 0.0055  -0.0276 -0.0500 68  TYR   B O   
4988 C  CB  . TYR   B 68  ? 0.1710 0.1781 0.1924 0.0089  -0.0520 -0.0400 68  TYR   B CB  
4989 C  CG  . TYR   B 68  ? 0.1840 0.1976 0.2093 0.0130  -0.0412 -0.0599 68  TYR   B CG  
4990 C  CD1 . TYR   B 68  ? 0.1844 0.1998 0.2320 -0.0078 -0.0371 -0.0695 68  TYR   B CD1 
4991 C  CD2 . TYR   B 68  ? 0.1915 0.2230 0.2188 0.0203  -0.0525 -0.0577 68  TYR   B CD2 
4992 C  CE1 . TYR   B 68  ? 0.1912 0.2244 0.2485 -0.0078 -0.0361 -0.0619 68  TYR   B CE1 
4993 C  CE2 . TYR   B 68  ? 0.1930 0.2315 0.2363 0.0202  -0.0414 -0.0658 68  TYR   B CE2 
4994 C  CZ  . TYR   B 68  ? 0.1862 0.2339 0.2498 0.0073  -0.0408 -0.0645 68  TYR   B CZ  
4995 O  OH  . TYR   B 68  ? 0.1795 0.2482 0.2838 0.0073  -0.0345 -0.0438 68  TYR   B OH  
5005 N  N   . ILE   B 69  ? 0.1603 0.1506 0.1839 -0.0004 -0.0326 -0.0318 69  ILE   B N   
5006 C  CA  . ILE   B 69  ? 0.1717 0.1569 0.1858 -0.0048 -0.0256 -0.0300 69  ILE   B CA  
5007 C  C   . ILE   B 69  ? 0.1676 0.1576 0.1836 0.0082  -0.0384 -0.0240 69  ILE   B C   
5008 O  O   . ILE   B 69  ? 0.1739 0.1628 0.1873 0.0071  -0.0210 -0.0309 69  ILE   B O   
5009 C  CB  . ILE   B 69  ? 0.1804 0.1561 0.2003 -0.0042 -0.0066 -0.0259 69  ILE   B CB  
5010 C  CG1 . ILE   B 69  ? 0.1770 0.1609 0.2142 -0.0027 0.0078  -0.0272 69  ILE   B CG1 
5011 C  CG2 . ILE   B 69  ? 0.1921 0.1688 0.2163 -0.0034 -0.0027 -0.0157 69  ILE   B CG2 
5012 C  CD1 . ILE   B 69  ? 0.1747 0.1720 0.2177 -0.0158 0.0127  -0.0235 69  ILE   B CD1 
5024 N  N   . ALA   B 70  ? 0.1619 0.1556 0.1807 0.0098  -0.0411 -0.0259 70  ALA   B N   
5025 C  CA  . ALA   B 70  ? 0.1706 0.1613 0.1617 0.0024  -0.0450 -0.0240 70  ALA   B CA  
5026 C  C   . ALA   B 70  ? 0.1763 0.1561 0.1836 0.0019  -0.0419 -0.0352 70  ALA   B C   
5027 O  O   . ALA   B 70  ? 0.1897 0.1606 0.1822 0.0075  -0.0413 -0.0307 70  ALA   B O   
5028 C  CB  . ALA   B 70  ? 0.1785 0.1756 0.1643 -0.0058 -0.0447 -0.0206 70  ALA   B CB  
5034 N  N   . THR   B 71  ? 0.1796 0.1595 0.1910 0.0044  -0.0544 -0.0352 71  THR   B N   
5035 C  CA  . THR   B 71  ? 0.1951 0.1629 0.2068 0.0077  -0.0623 -0.0388 71  THR   B CA  
5036 C  C   . THR   B 71  ? 0.1907 0.1716 0.2314 0.0273  -0.0583 -0.0539 71  THR   B C   
5037 O  O   . THR   B 71  ? 0.2043 0.1791 0.2669 0.0303  -0.0535 -0.0677 71  THR   B O   
5038 C  CB  . THR   B 71  ? 0.2249 0.1841 0.2312 0.0010  -0.0782 -0.0167 71  THR   B CB  
5039 O  OG1 . THR   B 71  ? 0.2409 0.2117 0.2780 -0.0180 -0.0734 0.0050  71  THR   B OG1 
5040 C  CG2 . THR   B 71  ? 0.2420 0.1816 0.2532 0.0066  -0.0716 -0.0042 71  THR   B CG2 
5048 N  N   . ASN   B 72  ? 0.1784 0.1729 0.2198 0.0155  -0.0574 -0.0679 72  ASN   B N   
5049 C  CA  . ASN   B 72  ? 0.1770 0.1823 0.2299 0.0178  -0.0493 -0.0765 72  ASN   B CA  
5050 C  C   . ASN   B 72  ? 0.1783 0.1946 0.2430 0.0073  -0.0275 -0.0676 72  ASN   B C   
5051 O  O   . ASN   B 72  ? 0.1807 0.2103 0.2761 0.0118  -0.0131 -0.0736 72  ASN   B O   
5052 C  CB  . ASN   B 72  ? 0.1780 0.1999 0.2501 0.0155  -0.0589 -0.0653 72  ASN   B CB  
5053 C  CG  . ASN   B 72  ? 0.1955 0.2159 0.2472 0.0275  -0.0600 -0.0406 72  ASN   B CG  
5054 O  OD1 . ASN   B 72  ? 0.2188 0.2331 0.2545 0.0155  -0.0461 -0.0427 72  ASN   B OD1 
5055 N  ND2 . ASN   B 72  ? 0.2087 0.2256 0.2843 0.0378  -0.0503 -0.0029 72  ASN   B ND2 
5062 N  N   . GLY   B 73  ? 0.1807 0.1910 0.2282 -0.0030 -0.0296 -0.0659 73  GLY   B N   
5063 C  CA  . GLY   B 73  ? 0.1773 0.1982 0.2025 -0.0014 -0.0214 -0.0472 73  GLY   B CA  
5064 C  C   . GLY   B 73  ? 0.1742 0.1991 0.1691 0.0046  -0.0208 -0.0400 73  GLY   B C   
5065 O  O   . GLY   B 73  ? 0.1673 0.1878 0.1771 0.0057  -0.0148 -0.0274 73  GLY   B O   
5069 N  N   . PRO   B 74  ? 0.1734 0.2054 0.1582 0.0021  -0.0274 -0.0356 74  PRO   B N   
5070 C  CA  . PRO   B 74  ? 0.1670 0.2047 0.1420 0.0058  -0.0183 -0.0199 74  PRO   B CA  
5071 C  C   . PRO   B 74  ? 0.1545 0.1855 0.1583 0.0048  -0.0188 -0.0137 74  PRO   B C   
5072 O  O   . PRO   B 74  ? 0.1588 0.1914 0.1918 0.0075  -0.0148 -0.0258 74  PRO   B O   
5073 C  CB  . PRO   B 74  ? 0.1795 0.2238 0.1464 0.0037  -0.0112 -0.0170 74  PRO   B CB  
5074 C  CG  . PRO   B 74  ? 0.1977 0.2363 0.1729 0.0034  -0.0157 -0.0096 74  PRO   B CG  
5075 C  CD  . PRO   B 74  ? 0.1953 0.2213 0.1733 0.0103  -0.0121 -0.0214 74  PRO   B CD  
5083 N  N   . LEU   B 75  ? 0.1491 0.1760 0.1446 0.0069  -0.0219 -0.0147 75  LEU   B N   
5084 C  CA  . LEU   B 75  ? 0.1575 0.1732 0.1454 0.0035  -0.0148 -0.0038 75  LEU   B CA  
5085 C  C   . LEU   B 75  ? 0.1666 0.1892 0.1420 0.0080  -0.0048 -0.0040 75  LEU   B C   
5086 O  O   . LEU   B 75  ? 0.1802 0.2054 0.1552 0.0027  -0.0018 0.0001  75  LEU   B O   
5087 C  CB  . LEU   B 75  ? 0.1650 0.1807 0.1352 -0.0093 -0.0205 0.0101  75  LEU   B CB  
5088 C  CG  . LEU   B 75  ? 0.1976 0.1983 0.1443 -0.0324 -0.0088 0.0074  75  LEU   B CG  
5089 C  CD1 . LEU   B 75  ? 0.2245 0.2183 0.1616 -0.0398 0.0105  0.0006  75  LEU   B CD1 
5090 C  CD2 . LEU   B 75  ? 0.2359 0.2185 0.2153 -0.0284 0.0065  0.0108  75  LEU   B CD2 
5102 N  N   . LYS   B 76  ? 0.1654 0.2077 0.1665 0.0033  0.0044  0.0083  76  LYS   B N   
5103 C  CA  . LYS   B 76  ? 0.1728 0.2188 0.2014 -0.0097 0.0228  0.0094  76  LYS   B CA  
5104 C  C   . LYS   B 76  ? 0.1601 0.2033 0.1824 -0.0048 0.0161  0.0261  76  LYS   B C   
5105 O  O   . LYS   B 76  ? 0.1652 0.1826 0.1845 -0.0062 0.0131  0.0226  76  LYS   B O   
5106 C  CB  . LYS   B 76  ? 0.1885 0.2253 0.2511 -0.0187 0.0390  -0.0224 76  LYS   B CB  
5107 C  CG  . LYS   B 76  ? 0.1993 0.2440 0.2938 -0.0055 0.0256  -0.0300 76  LYS   B CG  
5108 C  CD  . LYS   B 76  ? 0.2013 0.2529 0.3326 0.0079  0.0142  -0.0483 76  LYS   B CD  
5109 C  CE  . LYS   B 76  ? 0.2061 0.2710 0.3780 0.0095  0.0045  -0.0545 76  LYS   B CE  
5110 N  NZ  . LYS   B 76  ? 0.2035 0.2790 0.3984 0.0051  -0.0170 -0.0687 76  LYS   B NZ  
5124 N  N   . VAL   B 77  ? 0.1708 0.2151 0.1847 0.0066  0.0156  0.0292  77  VAL   B N   
5125 C  CA  . VAL   B 77  ? 0.1714 0.2065 0.1809 0.0101  0.0205  0.0598  77  VAL   B CA  
5126 C  C   . VAL   B 77  ? 0.1602 0.1833 0.1810 0.0133  0.0254  0.0469  77  VAL   B C   
5127 O  O   . VAL   B 77  ? 0.1616 0.1808 0.1870 0.0209  0.0278  0.0318  77  VAL   B O   
5128 C  CB  . VAL   B 77  ? 0.1850 0.2187 0.2218 0.0088  0.0274  0.0730  77  VAL   B CB  
5129 C  CG1 . VAL   B 77  ? 0.1906 0.2085 0.2495 0.0078  0.0310  0.0859  77  VAL   B CG1 
5130 C  CG2 . VAL   B 77  ? 0.2003 0.2362 0.2421 0.0034  0.0139  0.0729  77  VAL   B CG2 
5140 N  N   . GLY   B 78  ? 0.1609 0.1638 0.1796 0.0084  0.0193  0.0308  78  GLY   B N   
5141 C  CA  . GLY   B 78  ? 0.1550 0.1584 0.1765 0.0111  0.0277  0.0192  78  GLY   B CA  
5142 C  C   . GLY   B 78  ? 0.1469 0.1502 0.1716 0.0141  0.0217  0.0229  78  GLY   B C   
5143 O  O   . GLY   B 78  ? 0.1456 0.1556 0.1847 0.0164  0.0197  0.0285  78  GLY   B O   
5147 N  N   . GLY   B 79  ? 0.1454 0.1611 0.1746 0.0088  0.0197  0.0177  79  GLY   B N   
5148 C  CA  . GLY   B 79  ? 0.1440 0.1455 0.1719 0.0094  0.0140  0.0133  79  GLY   B CA  
5149 C  C   . GLY   B 79  ? 0.1333 0.1375 0.1716 0.0103  0.0145  0.0095  79  GLY   B C   
5150 O  O   . GLY   B 79  ? 0.1423 0.1371 0.1814 0.0112  0.0203  0.0173  79  GLY   B O   
5154 N  N   . SER   B 80  ? 0.1362 0.1347 0.1762 0.0100  0.0198  0.0125  80  SER   B N   
5155 C  CA  . SER   B 80  ? 0.1287 0.1337 0.1694 0.0018  0.0012  0.0124  80  SER   B CA  
5156 C  C   . SER   B 80  ? 0.1338 0.1327 0.1581 0.0107  -0.0021 0.0065  80  SER   B C   
5157 O  O   . SER   B 80  ? 0.1429 0.1348 0.1878 0.0071  0.0078  -0.0000 80  SER   B O   
5158 C  CB  . SER   B 80  ? 0.1351 0.1440 0.1779 -0.0060 -0.0023 0.0122  80  SER   B CB  
5159 O  OG  . SER   B 80  ? 0.1419 0.1528 0.1876 -0.0002 -0.0133 0.0082  80  SER   B OG  
5165 N  N   . CYS   B 81  ? 0.1291 0.1195 0.1601 0.0009  -0.0051 0.0032  81  CYS   B N   
5166 C  CA  . CYS   B 81  ? 0.1339 0.1190 0.1670 0.0022  -0.0141 0.0013  81  CYS   B CA  
5167 C  C   . CYS   B 81  ? 0.1324 0.1185 0.1483 -0.0006 -0.0110 0.0037  81  CYS   B C   
5168 O  O   . CYS   B 81  ? 0.1528 0.1222 0.1639 0.0042  -0.0015 -0.0017 81  CYS   B O   
5169 C  CB  . CYS   B 81  ? 0.1544 0.1308 0.1842 0.0007  -0.0111 0.0025  81  CYS   B CB  
5170 S  SG  . CYS   B 81  ? 0.1543 0.1498 0.1629 -0.0043 -0.0271 -0.0082 81  CYS   B SG  
5176 N  N   . VAL   B 82  ? 0.1365 0.1170 0.1514 -0.0072 -0.0160 0.0010  82  VAL   B N   
5177 C  CA  . VAL   B 82  ? 0.1399 0.1252 0.1548 -0.0055 -0.0119 0.0042  82  VAL   B CA  
5178 C  C   . VAL   B 82  ? 0.1492 0.1185 0.1662 -0.0086 -0.0030 -0.0026 82  VAL   B C   
5179 O  O   . VAL   B 82  ? 0.1635 0.1211 0.1810 -0.0089 -0.0103 -0.0141 82  VAL   B O   
5180 C  CB  . VAL   B 82  ? 0.1483 0.1431 0.1776 -0.0036 -0.0175 0.0111  82  VAL   B CB  
5181 C  CG1 . VAL   B 82  ? 0.1699 0.1639 0.1861 -0.0026 -0.0113 0.0134  82  VAL   B CG1 
5182 C  CG2 . VAL   B 82  ? 0.1593 0.1578 0.1974 -0.0098 -0.0288 0.0156  82  VAL   B CG2 
5192 N  N   . LEU   B 83  ? 0.1363 0.1201 0.1566 -0.0180 -0.0170 -0.0039 83  LEU   B N   
5193 C  CA  . LEU   B 83  ? 0.1374 0.1229 0.1511 -0.0173 -0.0124 -0.0006 83  LEU   B CA  
5194 C  C   . LEU   B 83  ? 0.1395 0.1211 0.1439 -0.0225 -0.0132 -0.0020 83  LEU   B C   
5195 O  O   . LEU   B 83  ? 0.1436 0.1313 0.1315 -0.0268 -0.0147 0.0066  83  LEU   B O   
5196 C  CB  . LEU   B 83  ? 0.1444 0.1335 0.1594 -0.0138 -0.0243 -0.0101 83  LEU   B CB  
5197 C  CG  . LEU   B 83  ? 0.1585 0.1514 0.1641 -0.0146 -0.0153 -0.0071 83  LEU   B CG  
5198 C  CD1 . LEU   B 83  ? 0.1700 0.1585 0.1666 -0.0026 -0.0244 -0.0085 83  LEU   B CD1 
5199 C  CD2 . LEU   B 83  ? 0.1824 0.1578 0.1672 -0.0103 -0.0213 -0.0159 83  LEU   B CD2 
5211 N  N   . SER   B 84  ? 0.1511 0.1266 0.1702 -0.0256 -0.0195 -0.0004 84  SER   B N   
5212 C  CA  . SER   B 84  ? 0.1434 0.1514 0.1620 -0.0280 -0.0113 0.0167  84  SER   B CA  
5213 C  C   . SER   B 84  ? 0.1398 0.1636 0.1259 -0.0217 -0.0146 0.0203  84  SER   B C   
5214 O  O   . SER   B 84  ? 0.1470 0.1529 0.1271 -0.0200 -0.0137 0.0076  84  SER   B O   
5215 C  CB  . SER   B 84  ? 0.1599 0.1570 0.2047 -0.0325 0.0045  0.0217  84  SER   B CB  
5216 O  OG  . SER   B 84  ? 0.1646 0.1775 0.2409 -0.0414 0.0035  0.0268  84  SER   B OG  
5222 N  N   . GLY   B 85  ? 0.1489 0.1818 0.1356 -0.0279 -0.0181 0.0334  85  GLY   B N   
5223 C  CA  . GLY   B 85  ? 0.1465 0.1883 0.1558 -0.0375 -0.0011 0.0023  85  GLY   B CA  
5224 C  C   . GLY   B 85  ? 0.1479 0.1724 0.1424 -0.0421 -0.0046 0.0067  85  GLY   B C   
5225 O  O   . GLY   B 85  ? 0.1555 0.1690 0.1669 -0.0528 0.0098  -0.0114 85  GLY   B O   
5229 N  N   . HIS   B 86  ? 0.1456 0.1588 0.1569 -0.0303 -0.0175 0.0099  86  HIS   B N   
5230 C  CA  . HIS   B 86  ? 0.1458 0.1608 0.1498 -0.0272 -0.0235 0.0159  86  HIS   B CA  
5231 C  C   . HIS   B 86  ? 0.1450 0.1718 0.1549 -0.0388 -0.0088 0.0315  86  HIS   B C   
5232 O  O   . HIS   B 86  ? 0.1586 0.1789 0.1623 -0.0304 0.0059  0.0255  86  HIS   B O   
5233 C  CB  . HIS   B 86  ? 0.1565 0.1639 0.1625 -0.0210 -0.0295 0.0022  86  HIS   B CB  
5234 C  CG  . HIS   B 86  ? 0.1625 0.1679 0.1549 -0.0153 -0.0292 0.0083  86  HIS   B CG  
5235 N  ND1 . HIS   B 86  ? 0.1713 0.1899 0.1791 -0.0214 -0.0368 -0.0069 86  HIS   B ND1 
5236 C  CD2 . HIS   B 86  ? 0.1583 0.1658 0.1633 -0.0099 -0.0244 0.0130  86  HIS   B CD2 
5237 C  CE1 . HIS   B 86  ? 0.1765 0.1860 0.1786 -0.0168 -0.0149 -0.0202 86  HIS   B CE1 
5238 N  NE2 . HIS   B 86  ? 0.1638 0.1756 0.1685 -0.0051 -0.0165 0.0016  86  HIS   B NE2 
5246 N  N   . ASN   B 87  ? 0.1503 0.1763 0.1622 -0.0342 -0.0064 0.0229  87  ASN   B N   
5247 C  CA  . ASN   B 87  ? 0.1576 0.1920 0.1640 -0.0350 0.0198  0.0198  87  ASN   B CA  
5248 C  C   . ASN   B 87  ? 0.1726 0.1785 0.1561 -0.0304 0.0348  0.0166  87  ASN   B C   
5249 O  O   . ASN   B 87  ? 0.1926 0.1909 0.1915 -0.0243 0.0499  0.0145  87  ASN   B O   
5250 C  CB  . ASN   B 87  ? 0.1601 0.2290 0.1965 -0.0270 0.0187  0.0165  87  ASN   B CB  
5251 C  CG  . ASN   B 87  ? 0.1635 0.2488 0.1986 0.0044  0.0219  0.0359  87  ASN   B CG  
5252 O  OD1 . ASN   B 87  ? 0.1605 0.2337 0.1852 0.0070  0.0377  0.0488  87  ASN   B OD1 
5253 N  ND2 . ASN   B 87  ? 0.1971 0.2621 0.2367 0.0085  0.0318  0.0322  87  ASN   B ND2 
5260 N  N   . LEU   B 88  ? 0.1607 0.1638 0.1429 -0.0324 0.0177  0.0136  88  LEU   B N   
5261 C  CA  . LEU   B 88  ? 0.1677 0.1578 0.1539 -0.0372 0.0069  0.0009  88  LEU   B CA  
5262 C  C   . LEU   B 88  ? 0.1689 0.1494 0.1466 -0.0374 -0.0055 0.0045  88  LEU   B C   
5263 O  O   . LEU   B 88  ? 0.1991 0.1517 0.1896 -0.0202 -0.0338 -0.0047 88  LEU   B O   
5264 C  CB  . LEU   B 88  ? 0.1825 0.1665 0.1638 -0.0472 -0.0036 0.0144  88  LEU   B CB  
5265 C  CG  . LEU   B 88  ? 0.2201 0.1939 0.1930 -0.0467 -0.0221 0.0337  88  LEU   B CG  
5266 C  CD1 . LEU   B 88  ? 0.2306 0.2248 0.2089 -0.0558 -0.0266 0.0469  88  LEU   B CD1 
5267 C  CD2 . LEU   B 88  ? 0.2563 0.2214 0.2496 -0.0066 -0.0467 0.0117  88  LEU   B CD2 
5279 N  N   . ALA   B 89  ? 0.1578 0.1494 0.1349 -0.0395 0.0075  0.0047  89  ALA   B N   
5280 C  CA  . ALA   B 89  ? 0.1523 0.1429 0.1229 -0.0421 0.0027  0.0122  89  ALA   B CA  
5281 C  C   . ALA   B 89  ? 0.1634 0.1472 0.1316 -0.0456 0.0089  0.0063  89  ALA   B C   
5282 O  O   . ALA   B 89  ? 0.1427 0.1532 0.1634 -0.0393 0.0135  -0.0209 89  ALA   B O   
5283 C  CB  . ALA   B 89  ? 0.1455 0.1439 0.1461 -0.0357 0.0121  0.0136  89  ALA   B CB  
5289 N  N   . LYS   B 90  ? 0.1960 0.1388 0.1419 -0.0517 -0.0066 0.0142  90  LYS   B N   
5290 C  CA  . LYS   B 90  ? 0.2044 0.1320 0.1386 -0.0490 -0.0117 0.0065  90  LYS   B CA  
5291 C  C   . LYS   B 90  ? 0.1910 0.1220 0.1524 -0.0451 -0.0090 0.0002  90  LYS   B C   
5292 O  O   . LYS   B 90  ? 0.1997 0.1416 0.1657 -0.0579 0.0014  -0.0004 90  LYS   B O   
5293 C  CB  . LYS   B 90  ? 0.2239 0.1410 0.1743 -0.0347 0.0005  0.0229  90  LYS   B CB  
5294 C  CG  . LYS   B 90  ? 0.2249 0.1565 0.1702 -0.0181 0.0196  0.0203  90  LYS   B CG  
5295 C  CD  . LYS   B 90  ? 0.2621 0.1785 0.2146 -0.0074 0.0427  0.0094  90  LYS   B CD  
5296 C  CE  . LYS   B 90  ? 0.2732 0.1935 0.2601 -0.0126 0.0499  -0.0018 90  LYS   B CE  
5297 N  NZ  . LYS   B 90  ? 0.2733 0.1800 0.2541 -0.0277 0.0566  -0.0123 90  LYS   B NZ  
5311 N  N   . HIS   B 91  ? 0.1683 0.1208 0.1291 -0.0356 -0.0230 0.0132  91  HIS   B N   
5312 C  CA  . HIS   B 91  ? 0.1527 0.1223 0.1455 -0.0303 -0.0208 0.0092  91  HIS   B CA  
5313 C  C   . HIS   B 91  ? 0.1431 0.1260 0.1307 -0.0272 -0.0066 0.0052  91  HIS   B C   
5314 O  O   . HIS   B 91  ? 0.1555 0.1273 0.1353 -0.0295 -0.0243 0.0083  91  HIS   B O   
5315 C  CB  . HIS   B 91  ? 0.1703 0.1244 0.1776 -0.0155 -0.0163 0.0122  91  HIS   B CB  
5316 C  CG  . HIS   B 91  ? 0.2113 0.1417 0.2456 -0.0023 0.0163  0.0259  91  HIS   B CG  
5317 N  ND1 . HIS   B 91  ? 0.2400 0.1487 0.3065 -0.0038 0.0287  0.0117  91  HIS   B ND1 
5318 C  CD2 . HIS   B 91  ? 0.2252 0.1757 0.2934 0.0120  0.0012  0.0573  91  HIS   B CD2 
5319 C  CE1 . HIS   B 91  ? 0.2462 0.1702 0.3305 0.0158  0.0302  0.0200  91  HIS   B CE1 
5320 N  NE2 . HIS   B 91  ? 0.2418 0.1851 0.3258 0.0253  0.0179  0.0621  91  HIS   B NE2 
5328 N  N   . CYS   B 92  ? 0.1362 0.1217 0.1323 -0.0260 -0.0156 0.0024  92  CYS   B N   
5329 C  CA  . CYS   B 92  ? 0.1343 0.1161 0.1271 -0.0216 -0.0056 0.0007  92  CYS   B CA  
5330 C  C   . CYS   B 92  ? 0.1314 0.1073 0.1299 -0.0149 -0.0028 0.0025  92  CYS   B C   
5331 O  O   . CYS   B 92  ? 0.1362 0.1210 0.1440 -0.0194 -0.0041 0.0010  92  CYS   B O   
5332 C  CB  . CYS   B 92  ? 0.1330 0.1272 0.1310 -0.0143 -0.0098 0.0007  92  CYS   B CB  
5333 S  SG  . CYS   B 92  ? 0.1347 0.1262 0.1528 -0.0104 -0.0131 0.0068  92  CYS   B SG  
5339 N  N   . LEU   B 93  ? 0.1250 0.1156 0.1305 -0.0146 -0.0090 -0.0019 93  LEU   B N   
5340 C  CA  . LEU   B 93  ? 0.1247 0.1165 0.1366 -0.0056 -0.0085 0.0039  93  LEU   B CA  
5341 C  C   . LEU   B 93  ? 0.1207 0.1147 0.1163 -0.0047 -0.0027 0.0083  93  LEU   B C   
5342 O  O   . LEU   B 93  ? 0.1275 0.1123 0.1430 -0.0077 -0.0085 0.0038  93  LEU   B O   
5343 C  CB  . LEU   B 93  ? 0.1241 0.1169 0.1601 0.0023  -0.0087 0.0051  93  LEU   B CB  
5344 C  CG  . LEU   B 93  ? 0.1226 0.1311 0.1744 -0.0039 -0.0081 0.0093  93  LEU   B CG  
5345 C  CD1 . LEU   B 93  ? 0.1263 0.1327 0.1657 0.0043  -0.0043 0.0013  93  LEU   B CD1 
5346 C  CD2 . LEU   B 93  ? 0.1224 0.1337 0.1825 -0.0049 -0.0152 0.0013  93  LEU   B CD2 
5358 N  N   . HIS   B 94  ? 0.1283 0.1111 0.1234 -0.0088 -0.0096 0.0043  94  HIS   B N   
5359 C  CA  . HIS   B 94  ? 0.1317 0.1137 0.1200 -0.0020 -0.0049 0.0116  94  HIS   B CA  
5360 C  C   . HIS   B 94  ? 0.1208 0.1172 0.1447 -0.0015 -0.0044 0.0091  94  HIS   B C   
5361 O  O   . HIS   B 94  ? 0.1234 0.1246 0.1860 -0.0057 0.0127  0.0004  94  HIS   B O   
5362 C  CB  . HIS   B 94  ? 0.1336 0.1191 0.1416 0.0003  -0.0083 0.0043  94  HIS   B CB  
5363 C  CG  . HIS   B 94  ? 0.1254 0.1183 0.1359 -0.0099 -0.0206 0.0044  94  HIS   B CG  
5364 N  ND1 . HIS   B 94  ? 0.1341 0.1254 0.1333 -0.0079 -0.0258 0.0047  94  HIS   B ND1 
5365 C  CD2 . HIS   B 94  ? 0.1351 0.1191 0.1382 0.0016  -0.0166 0.0077  94  HIS   B CD2 
5366 C  CE1 . HIS   B 94  ? 0.1406 0.1233 0.1281 -0.0110 -0.0219 0.0086  94  HIS   B CE1 
5367 N  NE2 . HIS   B 94  ? 0.1352 0.1240 0.1445 -0.0145 -0.0152 0.0033  94  HIS   B NE2 
5375 N  N   . VAL   B 95  ? 0.1173 0.1152 0.1477 -0.0023 -0.0020 0.0077  95  VAL   B N   
5376 C  CA  . VAL   B 95  ? 0.1217 0.1274 0.1341 0.0023  0.0057  0.0200  95  VAL   B CA  
5377 C  C   . VAL   B 95  ? 0.1233 0.1237 0.1417 -0.0039 0.0129  0.0078  95  VAL   B C   
5378 O  O   . VAL   B 95  ? 0.1303 0.1235 0.1624 0.0063  0.0047  0.0145  95  VAL   B O   
5379 C  CB  . VAL   B 95  ? 0.1297 0.1236 0.1458 0.0006  -0.0048 0.0078  95  VAL   B CB  
5380 C  CG1 . VAL   B 95  ? 0.1337 0.1431 0.1741 -0.0103 -0.0032 0.0179  95  VAL   B CG1 
5381 C  CG2 . VAL   B 95  ? 0.1326 0.1208 0.1427 0.0028  -0.0068 0.0130  95  VAL   B CG2 
5391 N  N   . VAL   B 96  ? 0.1365 0.1251 0.1456 0.0057  0.0102  0.0192  96  VAL   B N   
5392 C  CA  . VAL   B 96  ? 0.1445 0.1329 0.1484 0.0079  0.0087  0.0187  96  VAL   B CA  
5393 C  C   . VAL   B 96  ? 0.1465 0.1356 0.1661 0.0045  0.0102  0.0195  96  VAL   B C   
5394 O  O   . VAL   B 96  ? 0.1509 0.1456 0.1832 0.0021  0.0147  0.0080  96  VAL   B O   
5395 C  CB  . VAL   B 96  ? 0.1525 0.1535 0.1385 0.0118  0.0051  0.0174  96  VAL   B CB  
5396 C  CG1 . VAL   B 96  ? 0.1537 0.1725 0.1504 0.0165  0.0046  0.0049  96  VAL   B CG1 
5397 C  CG2 . VAL   B 96  ? 0.1632 0.1563 0.1513 0.0110  0.0139  0.0077  96  VAL   B CG2 
5407 N  N   . GLY   B 97  ? 0.1555 0.1387 0.1555 -0.0002 0.0064  0.0240  97  GLY   B N   
5408 C  CA  . GLY   B 97  ? 0.1686 0.1445 0.1673 -0.0008 0.0125  0.0211  97  GLY   B CA  
5409 C  C   . GLY   B 97  ? 0.1897 0.1523 0.1798 0.0090  0.0089  0.0196  97  GLY   B C   
5410 O  O   . GLY   B 97  ? 0.2061 0.1598 0.1739 0.0066  0.0073  0.0137  97  GLY   B O   
5414 N  N   . PRO   B 98  ? 0.2044 0.1592 0.1886 0.0099  0.0373  0.0335  98  PRO   B N   
5415 C  CA  . PRO   B 98  ? 0.2174 0.1792 0.1842 0.0223  0.0452  0.0262  98  PRO   B CA  
5416 C  C   . PRO   B 98  ? 0.2303 0.1790 0.1612 0.0405  0.0501  0.0467  98  PRO   B C   
5417 O  O   . PRO   B 98  ? 0.2224 0.1765 0.1910 0.0282  0.0543  0.0530  98  PRO   B O   
5418 C  CB  . PRO   B 98  ? 0.2078 0.1855 0.1939 0.0140  0.0537  0.0276  98  PRO   B CB  
5419 C  CG  . PRO   B 98  ? 0.2041 0.1764 0.1978 0.0097  0.0451  0.0441  98  PRO   B CG  
5420 C  CD  . PRO   B 98  ? 0.1900 0.1633 0.2014 0.0107  0.0447  0.0404  98  PRO   B CD  
5428 N  N   . ASN   B 99  ? 0.2460 0.1976 0.1824 0.0548  0.0472  0.0308  99  ASN   B N   
5429 C  CA  . ASN   B 99  ? 0.2703 0.2135 0.1856 0.0592  0.0439  0.0585  99  ASN   B CA  
5430 C  C   . ASN   B 99  ? 0.3024 0.2486 0.2289 0.0576  0.0583  0.0948  99  ASN   B C   
5431 O  O   . ASN   B 99  ? 0.3157 0.2566 0.2415 0.0585  0.0443  0.1019  99  ASN   B O   
5432 C  CB  . ASN   B 99  ? 0.2811 0.2108 0.1861 0.0597  0.0302  0.0474  99  ASN   B CB  
5433 C  CG  . ASN   B 99  ? 0.2858 0.2146 0.2074 0.0548  0.0209  0.0382  99  ASN   B CG  
5434 O  OD1 . ASN   B 99  ? 0.2878 0.2160 0.2294 0.0526  0.0231  0.0508  99  ASN   B OD1 
5435 N  ND2 . ASN   B 99  ? 0.2839 0.2112 0.2164 0.0593  0.0004  0.0275  99  ASN   B ND2 
5442 N  N   A VAL   B 100 ? 0.3194 0.2628 0.2647 0.0459  0.0666  0.1220  100 VAL   B N   
5443 N  N   B VAL   B 100 ? 0.3221 0.2632 0.2651 0.0472  0.0548  0.1102  100 VAL   B N   
5444 C  CA  A VAL   B 100 ? 0.3469 0.2847 0.3184 0.0305  0.0644  0.1316  100 VAL   B CA  
5445 C  CA  B VAL   B 100 ? 0.3476 0.2821 0.3088 0.0342  0.0470  0.1153  100 VAL   B CA  
5446 C  C   A VAL   B 100 ? 0.3688 0.2924 0.3131 0.0351  0.0576  0.1422  100 VAL   B C   
5447 C  C   B VAL   B 100 ? 0.3682 0.2904 0.3087 0.0367  0.0447  0.1317  100 VAL   B C   
5448 O  O   A VAL   B 100 ? 0.3760 0.3044 0.3166 0.0333  0.0673  0.1310  100 VAL   B O   
5449 O  O   B VAL   B 100 ? 0.3727 0.2972 0.3089 0.0336  0.0475  0.1238  100 VAL   B O   
5450 C  CB  A VAL   B 100 ? 0.3549 0.2980 0.3826 0.0062  0.0638  0.1385  100 VAL   B CB  
5451 C  CB  B VAL   B 100 ? 0.3537 0.2925 0.3541 0.0165  0.0409  0.1112  100 VAL   B CB  
5452 C  CG1 A VAL   B 100 ? 0.3596 0.3059 0.4079 0.0000  0.0617  0.1352  100 VAL   B CG1 
5453 C  CG1 B VAL   B 100 ? 0.3569 0.2981 0.3707 0.0116  0.0391  0.1086  100 VAL   B CG1 
5454 C  CG2 A VAL   B 100 ? 0.3552 0.3002 0.4012 -0.0023 0.0651  0.1447  100 VAL   B CG2 
5455 C  CG2 B VAL   B 100 ? 0.3545 0.2948 0.3681 0.0105  0.0389  0.1115  100 VAL   B CG2 
5474 N  N   . ASN   B 101 ? 0.3831 0.2949 0.3091 0.0449  0.0389  0.1465  101 ASN   B N   
5475 C  CA  . ASN   B 101 ? 0.4216 0.3170 0.3301 0.0487  0.0207  0.1491  101 ASN   B CA  
5476 C  C   . ASN   B 101 ? 0.4708 0.3722 0.3500 0.0369  0.0062  0.1373  101 ASN   B C   
5477 O  O   . ASN   B 101 ? 0.4746 0.3808 0.3663 0.0428  0.0063  0.1187  101 ASN   B O   
5478 C  CB  . ASN   B 101 ? 0.4130 0.2944 0.3350 0.0523  0.0263  0.1301  101 ASN   B CB  
5479 C  CG  . ASN   B 101 ? 0.4040 0.2752 0.3368 0.0547  0.0279  0.1239  101 ASN   B CG  
5480 O  OD1 . ASN   B 101 ? 0.4069 0.2730 0.3639 0.0496  0.0422  0.1123  101 ASN   B OD1 
5481 N  ND2 . ASN   B 101 ? 0.3950 0.2651 0.3283 0.0565  0.0276  0.1112  101 ASN   B ND2 
5489 N  N   A LYS   B 102 ? 0.4951 0.3982 0.3662 0.0251  0.0070  0.1270  102 LYS   B N   
5490 N  N   B LYS   B 102 ? 0.4914 0.3979 0.3702 0.0273  0.0060  0.1242  102 LYS   B N   
5491 C  CA  A LYS   B 102 ? 0.5168 0.4256 0.3919 0.0124  0.0112  0.1065  102 LYS   B CA  
5492 C  CA  B LYS   B 102 ? 0.5091 0.4229 0.3962 0.0175  0.0089  0.1053  102 LYS   B CA  
5493 C  C   A LYS   B 102 ? 0.5144 0.4254 0.3671 0.0158  0.0132  0.1149  102 LYS   B C   
5494 C  C   B LYS   B 102 ? 0.5095 0.4242 0.3743 0.0177  0.0135  0.1131  102 LYS   B C   
5495 O  O   A LYS   B 102 ? 0.5225 0.4300 0.3665 0.0160  0.0021  0.1165  102 LYS   B O   
5496 O  O   B LYS   B 102 ? 0.5157 0.4287 0.3758 0.0169  0.0063  0.1158  102 LYS   B O   
5497 C  CB  A LYS   B 102 ? 0.5386 0.4508 0.4475 -0.0017 0.0221  0.0690  102 LYS   B CB  
5498 C  CB  B LYS   B 102 ? 0.5242 0.4442 0.4441 0.0089  0.0130  0.0732  102 LYS   B CB  
5499 C  CG  A LYS   B 102 ? 0.5565 0.4718 0.5070 -0.0127 0.0327  0.0316  102 LYS   B CG  
5500 C  CG  B LYS   B 102 ? 0.5361 0.4615 0.4930 0.0021  0.0176  0.0417  102 LYS   B CG  
5501 C  CD  A LYS   B 102 ? 0.5703 0.4882 0.5596 -0.0209 0.0429  0.0015  102 LYS   B CD  
5502 C  CD  B LYS   B 102 ? 0.5451 0.4748 0.5349 -0.0029 0.0227  0.0157  102 LYS   B CD  
5503 C  CE  A LYS   B 102 ? 0.5788 0.4993 0.6010 -0.0278 0.0515  -0.0195 102 LYS   B CE  
5504 C  CE  B LYS   B 102 ? 0.5510 0.4842 0.5679 -0.0069 0.0270  -0.0024 102 LYS   B CE  
5505 N  NZ  A LYS   B 102 ? 0.5833 0.5061 0.6248 -0.0312 0.0562  -0.0315 102 LYS   B NZ  
5506 N  NZ  B LYS   B 102 ? 0.5545 0.4900 0.5867 -0.0088 0.0293  -0.0122 102 LYS   B NZ  
5533 N  N   . GLY   B 103 ? 0.5016 0.4190 0.3584 0.0189  0.0278  0.1125  103 GLY   B N   
5534 C  CA  . GLY   B 103 ? 0.4812 0.4087 0.3640 0.0254  0.0547  0.0930  103 GLY   B CA  
5535 C  C   . GLY   B 103 ? 0.4569 0.3941 0.3565 0.0287  0.0788  0.0733  103 GLY   B C   
5536 O  O   . GLY   B 103 ? 0.4631 0.4007 0.3538 0.0245  0.0838  0.0742  103 GLY   B O   
5541 N  N   A GLU   B 104 ? 0.4394 0.3801 0.3434 0.0368  0.0985  0.0614  104 GLU   B N   
5542 N  N   B GLU   B 104 ? 0.4411 0.3843 0.3538 0.0267  0.0751  0.0581  104 GLU   B N   
5543 C  CA  A GLU   B 104 ? 0.4203 0.3646 0.3282 0.0469  0.1094  0.0479  104 GLU   B CA  
5544 C  CA  B GLU   B 104 ? 0.4239 0.3729 0.3466 0.0252  0.0675  0.0406  104 GLU   B CA  
5545 C  C   A GLU   B 104 ? 0.4199 0.3662 0.3363 0.0271  0.1467  0.0537  104 GLU   B C   
5546 C  C   B GLU   B 104 ? 0.4176 0.3707 0.3553 0.0161  0.0835  0.0371  104 GLU   B C   
5547 O  O   A GLU   B 104 ? 0.4193 0.3676 0.3553 0.0239  0.1478  0.0545  104 GLU   B O   
5548 O  O   B GLU   B 104 ? 0.4168 0.3705 0.3652 0.0151  0.0842  0.0361  104 GLU   B O   
5549 C  CB  A GLU   B 104 ? 0.4055 0.3468 0.3168 0.0756  0.0750  0.0190  104 GLU   B CB  
5550 C  CB  B GLU   B 104 ? 0.4151 0.3632 0.3350 0.0315  0.0421  0.0222  104 GLU   B CB  
5551 C  CG  A GLU   B 104 ? 0.3916 0.3318 0.3008 0.0998  0.0337  -0.0119 104 GLU   B CG  
5552 C  CG  B GLU   B 104 ? 0.4073 0.3549 0.3219 0.0358  0.0146  0.0024  104 GLU   B CG  
5553 C  CD  A GLU   B 104 ? 0.3783 0.3177 0.2816 0.1186  0.0001  -0.0281 104 GLU   B CD  
5554 C  CD  B GLU   B 104 ? 0.4004 0.3466 0.3095 0.0373  -0.0063 -0.0111 104 GLU   B CD  
5555 O  OE1 A GLU   B 104 ? 0.3636 0.3023 0.2473 0.1294  0.0027  -0.0286 104 GLU   B OE1 
5556 O  OE1 B GLU   B 104 ? 0.3938 0.3396 0.2952 0.0361  -0.0070 -0.0131 104 GLU   B OE1 
5557 O  OE2 A GLU   B 104 ? 0.3804 0.3224 0.2819 0.1194  -0.0271 -0.0396 104 GLU   B OE2 
5558 O  OE2 B GLU   B 104 ? 0.4009 0.3469 0.3074 0.0380  -0.0217 -0.0202 104 GLU   B OE2 
5571 N  N   A ASP   B 105 ? 0.4164 0.3674 0.3306 0.0112  0.1774  0.0580  105 ASP   B N   
5572 N  N   B ASP   B 105 ? 0.4110 0.3693 0.3534 0.0076  0.0970  0.0351  105 ASP   B N   
5573 C  CA  A ASP   B 105 ? 0.4161 0.3697 0.3474 -0.0021 0.1963  0.0450  105 ASP   B CA  
5574 C  CA  B ASP   B 105 ? 0.4061 0.3675 0.3601 -0.0001 0.1069  0.0265  105 ASP   B CA  
5575 C  C   A ASP   B 105 ? 0.3974 0.3440 0.3171 -0.0175 0.1972  0.0444  105 ASP   B C   
5576 C  C   B ASP   B 105 ? 0.3958 0.3561 0.3385 -0.0069 0.1087  0.0226  105 ASP   B C   
5577 O  O   A ASP   B 105 ? 0.3816 0.3376 0.3025 -0.0137 0.1927  0.0474  105 ASP   B O   
5578 O  O   B ASP   B 105 ? 0.3929 0.3532 0.3280 -0.0052 0.1136  0.0255  105 ASP   B O   
5579 C  CB  A ASP   B 105 ? 0.4326 0.3916 0.4166 0.0049  0.2047  0.0244  105 ASP   B CB  
5580 C  CB  B ASP   B 105 ? 0.4089 0.3748 0.3945 0.0018  0.1143  0.0195  105 ASP   B CB  
5581 C  CG  A ASP   B 105 ? 0.4428 0.4067 0.4831 0.0099  0.2129  0.0090  105 ASP   B CG  
5582 C  CG  B ASP   B 105 ? 0.4101 0.3786 0.4272 0.0023  0.1214  0.0155  105 ASP   B CG  
5583 O  OD1 A ASP   B 105 ? 0.4414 0.4106 0.4929 0.0048  0.2259  0.0140  105 ASP   B OD1 
5584 O  OD1 B ASP   B 105 ? 0.4086 0.3794 0.4354 -0.0007 0.1247  0.0165  105 ASP   B OD1 
5585 O  OD2 A ASP   B 105 ? 0.4492 0.4137 0.5224 0.0178  0.2042  -0.0045 105 ASP   B OD2 
5586 O  OD2 B ASP   B 105 ? 0.4094 0.3806 0.4392 0.0032  0.1253  0.0153  105 ASP   B OD2 
5595 N  N   A ILE   B 106 ? 0.3891 0.3224 0.3283 -0.0290 0.1805  0.0396  106 ILE   B N   
5596 N  N   B ILE   B 106 ? 0.3873 0.3456 0.3345 -0.0115 0.0986  0.0165  106 ILE   B N   
5597 C  CA  A ILE   B 106 ? 0.3716 0.2958 0.3316 -0.0488 0.1836  0.0394  106 ILE   B CA  
5598 C  CA  B ILE   B 106 ? 0.3744 0.3341 0.3335 -0.0170 0.0954  0.0106  106 ILE   B CA  
5599 C  C   A ILE   B 106 ? 0.3373 0.2873 0.3176 -0.0449 0.1844  0.0235  106 ILE   B C   
5600 C  C   B ILE   B 106 ? 0.3534 0.3275 0.3271 -0.0146 0.0947  0.0023  106 ILE   B C   
5601 O  O   A ILE   B 106 ? 0.3278 0.2662 0.3233 -0.0527 0.1770  0.0167  106 ILE   B O   
5602 O  O   B ILE   B 106 ? 0.3497 0.3203 0.3236 -0.0185 0.0905  -0.0010 106 ILE   B O   
5603 C  CB  A ILE   B 106 ? 0.3909 0.2862 0.3492 -0.0602 0.1729  0.0479  106 ILE   B CB  
5604 C  CB  B ILE   B 106 ? 0.3824 0.3326 0.3398 -0.0225 0.0912  0.0112  106 ILE   B CB  
5605 C  CG1 A ILE   B 106 ? 0.3993 0.2867 0.3621 -0.0560 0.1601  0.0360  106 ILE   B CG1 
5606 C  CG1 B ILE   B 106 ? 0.3867 0.3330 0.3456 -0.0218 0.0851  0.0083  106 ILE   B CG1 
5607 C  CG2 A ILE   B 106 ? 0.3967 0.2877 0.3677 -0.0667 0.1734  0.0552  106 ILE   B CG2 
5608 C  CG2 B ILE   B 106 ? 0.3849 0.3348 0.3486 -0.0246 0.0924  0.0116  106 ILE   B CG2 
5609 C  CD1 A ILE   B 106 ? 0.4043 0.2896 0.3583 -0.0525 0.1565  0.0333  106 ILE   B CD1 
5610 C  CD1 B ILE   B 106 ? 0.3897 0.3345 0.3463 -0.0207 0.0825  0.0074  106 ILE   B CD1 
5633 N  N   A GLN   B 107 ? 0.3238 0.3038 0.3337 -0.0376 0.1732  0.0225  107 GLN   B N   
5634 N  N   B GLN   B 107 ? 0.3386 0.3295 0.3382 -0.0108 0.0920  0.0013  107 GLN   B N   
5635 C  CA  A GLN   B 107 ? 0.3092 0.3182 0.3548 -0.0325 0.1443  0.0226  107 GLN   B CA  
5636 C  CA  B GLN   B 107 ? 0.3237 0.3299 0.3523 -0.0087 0.0847  0.0051  107 GLN   B CA  
5637 C  C   A GLN   B 107 ? 0.2788 0.2968 0.3245 -0.0191 0.1172  0.0131  107 GLN   B C   
5638 C  C   B GLN   B 107 ? 0.2904 0.3054 0.3204 -0.0039 0.0882  0.0040  107 GLN   B C   
5639 O  O   A GLN   B 107 ? 0.2702 0.2972 0.3547 -0.0138 0.0906  -0.0018 107 GLN   B O   
5640 O  O   B GLN   B 107 ? 0.2880 0.3081 0.3338 -0.0009 0.0746  -0.0036 107 GLN   B O   
5641 C  CB  A GLN   B 107 ? 0.3390 0.3557 0.4259 -0.0311 0.1181  0.0239  107 GLN   B CB  
5642 C  CB  B GLN   B 107 ? 0.3456 0.3551 0.4064 -0.0090 0.0689  0.0068  107 GLN   B CB  
5643 C  CG  A GLN   B 107 ? 0.3700 0.3879 0.4966 -0.0254 0.0820  0.0234  107 GLN   B CG  
5644 C  CG  B GLN   B 107 ? 0.3664 0.3767 0.4598 -0.0073 0.0498  0.0083  107 GLN   B CG  
5645 C  CD  A GLN   B 107 ? 0.3940 0.4128 0.5517 -0.0226 0.0552  0.0254  107 GLN   B CD  
5646 C  CD  B GLN   B 107 ? 0.3822 0.3923 0.5028 -0.0068 0.0346  0.0104  107 GLN   B CD  
5647 O  OE1 A GLN   B 107 ? 0.4025 0.4235 0.5731 -0.0190 0.0488  0.0236  107 GLN   B OE1 
5648 O  OE1 B GLN   B 107 ? 0.3868 0.3979 0.5179 -0.0057 0.0319  0.0107  107 GLN   B OE1 
5649 N  NE2 A GLN   B 107 ? 0.4034 0.4195 0.5698 -0.0209 0.0454  0.0298  107 GLN   B NE2 
5650 N  NE2 B GLN   B 107 ? 0.3891 0.3970 0.5182 -0.0059 0.0293  0.0124  107 GLN   B NE2 
5667 N  N   . LEU   B 108 ? 0.2586 0.2770 0.2857 0.0048  0.0990  0.0060  108 LEU   B N   
5668 C  CA  . LEU   B 108 ? 0.2280 0.2445 0.2448 0.0212  0.0745  0.0178  108 LEU   B CA  
5669 C  C   . LEU   B 108 ? 0.1867 0.2002 0.2340 0.0166  0.0471  0.0267  108 LEU   B C   
5670 O  O   . LEU   B 108 ? 0.1789 0.1818 0.2282 0.0172  0.0372  0.0240  108 LEU   B O   
5671 C  CB  . LEU   B 108 ? 0.2401 0.2614 0.2247 0.0199  0.0737  0.0360  108 LEU   B CB  
5672 C  CG  . LEU   B 108 ? 0.2571 0.2926 0.2325 0.0222  0.0637  0.0143  108 LEU   B CG  
5673 C  CD1 . LEU   B 108 ? 0.2688 0.3063 0.2214 0.0153  0.0605  0.0149  108 LEU   B CD1 
5674 C  CD2 . LEU   B 108 ? 0.2706 0.3039 0.2412 0.0300  0.0533  -0.0008 108 LEU   B CD2 
5687 N  N   . LEU   B 109 ? 0.1692 0.1763 0.2279 0.0080  0.0391  0.0265  109 LEU   B N   
5688 C  CA  . LEU   B 109 ? 0.1550 0.1444 0.2443 0.0041  0.0408  0.0325  109 LEU   B CA  
5689 C  C   . LEU   B 109 ? 0.1456 0.1298 0.2512 0.0007  0.0345  0.0225  109 LEU   B C   
5690 O  O   . LEU   B 109 ? 0.1435 0.1265 0.2317 0.0003  0.0321  0.0289  109 LEU   B O   
5691 C  CB  . LEU   B 109 ? 0.1628 0.1320 0.2550 0.0017  0.0310  0.0399  109 LEU   B CB  
5692 C  CG  . LEU   B 109 ? 0.1534 0.1342 0.2509 0.0005  0.0238  0.0289  109 LEU   B CG  
5693 C  CD1 . LEU   B 109 ? 0.1521 0.1471 0.2291 0.0116  0.0274  0.0337  109 LEU   B CD1 
5694 C  CD2 . LEU   B 109 ? 0.1619 0.1390 0.2725 0.0039  0.0189  0.0231  109 LEU   B CD2 
5706 N  N   . LYS   B 110 ? 0.1398 0.1272 0.2421 -0.0066 0.0328  0.0216  110 LYS   B N   
5707 C  CA  . LYS   B 110 ? 0.1379 0.1308 0.2407 -0.0042 0.0279  0.0159  110 LYS   B CA  
5708 C  C   . LYS   B 110 ? 0.1329 0.1281 0.2273 -0.0035 0.0315  0.0181  110 LYS   B C   
5709 O  O   . LYS   B 110 ? 0.1260 0.1325 0.2215 -0.0034 0.0270  0.0145  110 LYS   B O   
5710 C  CB  . LYS   B 110 ? 0.1403 0.1282 0.2533 0.0030  0.0330  0.0160  110 LYS   B CB  
5711 C  CG  . LYS   B 110 ? 0.1368 0.1269 0.2686 -0.0001 0.0151  0.0188  110 LYS   B CG  
5712 C  CD  . LYS   B 110 ? 0.1382 0.1311 0.2750 -0.0070 0.0250  0.0223  110 LYS   B CD  
5713 C  CE  . LYS   B 110 ? 0.1396 0.1443 0.2955 0.0007  0.0264  0.0091  110 LYS   B CE  
5714 N  NZ  . LYS   B 110 ? 0.1402 0.1635 0.2842 0.0048  0.0134  0.0055  110 LYS   B NZ  
5728 N  N   . SER   B 111 ? 0.1452 0.1338 0.2372 -0.0059 0.0311  0.0187  111 SER   B N   
5729 C  CA  . SER   B 111 ? 0.1443 0.1340 0.2235 -0.0015 0.0258  0.0173  111 SER   B CA  
5730 C  C   . SER   B 111 ? 0.1362 0.1258 0.2177 -0.0004 0.0149  0.0069  111 SER   B C   
5731 O  O   . SER   B 111 ? 0.1314 0.1280 0.2256 0.0000  0.0139  0.0099  111 SER   B O   
5732 C  CB  . SER   B 111 ? 0.1560 0.1539 0.2386 -0.0018 0.0416  0.0290  111 SER   B CB  
5733 O  OG  . SER   B 111 ? 0.1711 0.1829 0.2568 0.0070  0.0491  0.0330  111 SER   B OG  
5739 N  N   . ALA   B 112 ? 0.1290 0.1326 0.2169 0.0056  0.0287  0.0222  112 ALA   B N   
5740 C  CA  . ALA   B 112 ? 0.1314 0.1377 0.2047 0.0028  0.0069  0.0051  112 ALA   B CA  
5741 C  C   . ALA   B 112 ? 0.1286 0.1256 0.1902 0.0007  0.0060  0.0049  112 ALA   B C   
5742 O  O   . ALA   B 112 ? 0.1288 0.1273 0.1987 -0.0054 0.0099  0.0023  112 ALA   B O   
5743 C  CB  . ALA   B 112 ? 0.1263 0.1373 0.2177 0.0104  0.0086  0.0119  112 ALA   B CB  
5749 N  N   . TYR   B 113 ? 0.1222 0.1174 0.2072 -0.0013 0.0130  0.0065  113 TYR   B N   
5750 C  CA  . TYR   B 113 ? 0.1198 0.1152 0.2032 -0.0011 0.0162  0.0017  113 TYR   B CA  
5751 C  C   . TYR   B 113 ? 0.1148 0.1090 0.2013 -0.0082 0.0112  0.0077  113 TYR   B C   
5752 O  O   . TYR   B 113 ? 0.1221 0.1194 0.1937 -0.0065 0.0028  0.0026  113 TYR   B O   
5753 C  CB  . TYR   B 113 ? 0.1240 0.1100 0.2038 -0.0027 0.0203  0.0085  113 TYR   B CB  
5754 C  CG  . TYR   B 113 ? 0.1296 0.1146 0.2113 -0.0082 0.0134  0.0142  113 TYR   B CG  
5755 C  CD1 . TYR   B 113 ? 0.1327 0.1230 0.2303 -0.0076 0.0142  0.0196  113 TYR   B CD1 
5756 C  CD2 . TYR   B 113 ? 0.1322 0.1182 0.2086 -0.0066 0.0083  0.0127  113 TYR   B CD2 
5757 C  CE1 . TYR   B 113 ? 0.1282 0.1259 0.2233 -0.0051 0.0203  0.0115  113 TYR   B CE1 
5758 C  CE2 . TYR   B 113 ? 0.1346 0.1104 0.2289 0.0007  0.0115  0.0094  113 TYR   B CE2 
5759 C  CZ  . TYR   B 113 ? 0.1256 0.1191 0.2354 0.0006  0.0073  0.0130  113 TYR   B CZ  
5760 O  OH  . TYR   B 113 ? 0.1382 0.1121 0.2618 0.0110  0.0186  0.0125  113 TYR   B OH  
5770 N  N   . GLU   B 114 ? 0.1168 0.1086 0.2123 -0.0084 0.0132  0.0030  114 GLU   B N   
5771 C  CA  . GLU   B 114 ? 0.1162 0.1062 0.2140 0.0026  0.0031  0.0034  114 GLU   B CA  
5772 C  C   . GLU   B 114 ? 0.1166 0.1091 0.2020 0.0012  0.0007  0.0012  114 GLU   B C   
5773 O  O   . GLU   B 114 ? 0.1187 0.1138 0.2106 0.0021  0.0005  0.0103  114 GLU   B O   
5774 C  CB  . GLU   B 114 ? 0.1206 0.1171 0.2177 -0.0069 0.0192  0.0047  114 GLU   B CB  
5775 C  CG  . GLU   B 114 ? 0.1242 0.1109 0.2192 -0.0043 0.0101  0.0096  114 GLU   B CG  
5776 C  CD  . GLU   B 114 ? 0.1229 0.1197 0.2265 -0.0051 0.0129  0.0072  114 GLU   B CD  
5777 O  OE1 . GLU   B 114 ? 0.1171 0.1322 0.2350 -0.0105 0.0197  0.0090  114 GLU   B OE1 
5778 O  OE2 . GLU   B 114 ? 0.1233 0.1448 0.2407 -0.0190 0.0132  0.0084  114 GLU   B OE2 
5785 N  N   . ASN   B 115 ? 0.1250 0.1079 0.1895 -0.0015 -0.0049 0.0057  115 ASN   B N   
5786 C  CA  . ASN   B 115 ? 0.1254 0.1124 0.1760 -0.0111 -0.0009 0.0157  115 ASN   B CA  
5787 C  C   . ASN   B 115 ? 0.1128 0.1072 0.1824 -0.0171 -0.0063 0.0047  115 ASN   B C   
5788 O  O   . ASN   B 115 ? 0.1297 0.1129 0.1889 -0.0140 -0.0048 0.0032  115 ASN   B O   
5789 C  CB  . ASN   B 115 ? 0.1308 0.1261 0.1863 -0.0143 0.0006  0.0053  115 ASN   B CB  
5790 C  CG  . ASN   B 115 ? 0.1356 0.1303 0.1899 -0.0036 -0.0013 0.0026  115 ASN   B CG  
5791 O  OD1 . ASN   B 115 ? 0.1787 0.1425 0.2083 -0.0037 0.0117  -0.0104 115 ASN   B OD1 
5792 N  ND2 . ASN   B 115 ? 0.1358 0.1405 0.1865 -0.0107 0.0082  0.0038  115 ASN   B ND2 
5799 N  N   . PHE   B 116 ? 0.1168 0.1107 0.1744 -0.0085 0.0009  0.0111  116 PHE   B N   
5800 C  CA  . PHE   B 116 ? 0.1226 0.1151 0.1884 -0.0130 -0.0005 0.0114  116 PHE   B CA  
5801 C  C   . PHE   B 116 ? 0.1198 0.1052 0.1873 -0.0175 -0.0085 0.0084  116 PHE   B C   
5802 O  O   . PHE   B 116 ? 0.1256 0.1198 0.1894 -0.0077 -0.0100 0.0102  116 PHE   B O   
5803 C  CB  . PHE   B 116 ? 0.1194 0.1089 0.1763 -0.0080 -0.0082 0.0085  116 PHE   B CB  
5804 C  CG  . PHE   B 116 ? 0.1157 0.1090 0.1739 -0.0110 0.0015  0.0063  116 PHE   B CG  
5805 C  CD1 . PHE   B 116 ? 0.1255 0.1166 0.1965 -0.0064 -0.0017 0.0025  116 PHE   B CD1 
5806 C  CD2 . PHE   B 116 ? 0.1185 0.1212 0.1691 -0.0052 0.0054  -0.0013 116 PHE   B CD2 
5807 C  CE1 . PHE   B 116 ? 0.1227 0.1223 0.2001 -0.0087 -0.0156 0.0061  116 PHE   B CE1 
5808 C  CE2 . PHE   B 116 ? 0.1215 0.1213 0.1757 -0.0086 -0.0047 0.0018  116 PHE   B CE2 
5809 C  CZ  . PHE   B 116 ? 0.1174 0.1214 0.1887 -0.0063 -0.0113 0.0050  116 PHE   B CZ  
5819 N  N   . ASN   B 117 ? 0.1156 0.1106 0.1919 -0.0071 -0.0097 0.0073  117 ASN   B N   
5820 C  CA  . ASN   B 117 ? 0.1280 0.1137 0.1944 -0.0026 -0.0055 -0.0006 117 ASN   B CA  
5821 C  C   . ASN   B 117 ? 0.1332 0.1160 0.2030 -0.0004 -0.0107 0.0029  117 ASN   B C   
5822 O  O   . ASN   B 117 ? 0.1364 0.1207 0.2431 -0.0075 -0.0327 0.0142  117 ASN   B O   
5823 C  CB  . ASN   B 117 ? 0.1299 0.1156 0.1947 -0.0026 -0.0046 -0.0042 117 ASN   B CB  
5824 C  CG  . ASN   B 117 ? 0.1292 0.1185 0.2125 0.0014  -0.0068 -0.0032 117 ASN   B CG  
5825 O  OD1 . ASN   B 117 ? 0.1454 0.1132 0.2286 -0.0104 0.0011  -0.0076 117 ASN   B OD1 
5826 N  ND2 . ASN   B 117 ? 0.1287 0.1246 0.2048 -0.0036 -0.0031 0.0013  117 ASN   B ND2 
5833 N  N   . GLN   B 118 ? 0.1338 0.1122 0.1858 -0.0113 -0.0191 -0.0031 118 GLN   B N   
5834 C  CA  . GLN   B 118 ? 0.1380 0.1183 0.2063 -0.0036 -0.0153 0.0023  118 GLN   B CA  
5835 C  C   . GLN   B 118 ? 0.1418 0.1114 0.2168 0.0021  -0.0105 0.0013  118 GLN   B C   
5836 O  O   . GLN   B 118 ? 0.1631 0.1073 0.2479 -0.0056 -0.0001 0.0094  118 GLN   B O   
5837 C  CB  . GLN   B 118 ? 0.1355 0.1204 0.2126 -0.0051 -0.0216 0.0041  118 GLN   B CB  
5838 C  CG  . GLN   B 118 ? 0.1419 0.1251 0.2118 0.0013  -0.0138 -0.0076 118 GLN   B CG  
5839 C  CD  . GLN   B 118 ? 0.1479 0.1163 0.2268 0.0006  -0.0123 -0.0104 118 GLN   B CD  
5840 O  OE1 . GLN   B 118 ? 0.1554 0.1128 0.2462 0.0028  0.0023  0.0044  118 GLN   B OE1 
5841 N  NE2 . GLN   B 118 ? 0.1629 0.1194 0.2234 0.0015  -0.0111 0.0035  118 GLN   B NE2 
5850 N  N   . HIS   B 119 ? 0.1415 0.1151 0.1828 -0.0042 -0.0154 0.0081  119 HIS   B N   
5851 C  CA  . HIS   B 119 ? 0.1460 0.1283 0.1736 -0.0040 -0.0121 0.0022  119 HIS   B CA  
5852 C  C   . HIS   B 119 ? 0.1557 0.1250 0.1698 -0.0070 -0.0301 0.0061  119 HIS   B C   
5853 O  O   . HIS   B 119 ? 0.1650 0.1236 0.1967 -0.0259 -0.0211 0.0062  119 HIS   B O   
5854 C  CB  . HIS   B 119 ? 0.1508 0.1376 0.1839 -0.0036 -0.0191 0.0027  119 HIS   B CB  
5855 C  CG  . HIS   B 119 ? 0.1550 0.1627 0.1961 0.0066  -0.0331 -0.0177 119 HIS   B CG  
5856 N  ND1 . HIS   B 119 ? 0.1651 0.1751 0.2154 0.0032  -0.0427 -0.0299 119 HIS   B ND1 
5857 C  CD2 . HIS   B 119 ? 0.1718 0.1819 0.2058 0.0376  -0.0456 -0.0199 119 HIS   B CD2 
5858 C  CE1 . HIS   B 119 ? 0.1820 0.1891 0.2225 0.0167  -0.0433 -0.0472 119 HIS   B CE1 
5859 N  NE2 . HIS   B 119 ? 0.1842 0.2002 0.2227 0.0353  -0.0476 -0.0389 119 HIS   B NE2 
5867 N  N   . GLU   B 120 ? 0.1740 0.1325 0.1634 -0.0132 -0.0361 0.0139  120 GLU   B N   
5868 C  CA  . GLU   B 120 ? 0.2005 0.1452 0.1796 -0.0071 -0.0468 0.0284  120 GLU   B CA  
5869 C  C   . GLU   B 120 ? 0.1786 0.1306 0.1802 -0.0124 -0.0383 0.0247  120 GLU   B C   
5870 O  O   . GLU   B 120 ? 0.1711 0.1472 0.1841 -0.0127 -0.0421 0.0118  120 GLU   B O   
5871 C  CB  . GLU   B 120 ? 0.2669 0.1786 0.2554 0.0215  -0.0764 0.0514  120 GLU   B CB  
5872 C  CG  . GLU   B 120 ? 0.3278 0.2584 0.3545 0.0338  -0.0977 0.0695  120 GLU   B CG  
5873 C  CD  . GLU   B 120 ? 0.3760 0.3276 0.4645 0.0382  -0.1011 0.0725  120 GLU   B CD  
5874 O  OE1 . GLU   B 120 ? 0.4026 0.3576 0.5066 0.0334  -0.0948 0.0793  120 GLU   B OE1 
5875 O  OE2 . GLU   B 120 ? 0.3936 0.3727 0.5198 0.0369  -0.0976 0.0658  120 GLU   B OE2 
5882 N  N   . VAL   B 121 ? 0.1625 0.1274 0.1830 -0.0254 -0.0293 0.0267  121 VAL   B N   
5883 C  CA  . VAL   B 121 ? 0.1576 0.1404 0.1624 -0.0232 -0.0273 0.0237  121 VAL   B CA  
5884 C  C   . VAL   B 121 ? 0.1510 0.1323 0.1609 -0.0253 -0.0217 0.0190  121 VAL   B C   
5885 O  O   . VAL   B 121 ? 0.1587 0.1290 0.1712 -0.0329 -0.0287 0.0097  121 VAL   B O   
5886 C  CB  . VAL   B 121 ? 0.1805 0.1820 0.1702 -0.0054 -0.0341 0.0255  121 VAL   B CB  
5887 C  CG1 . VAL   B 121 ? 0.1785 0.1918 0.2068 -0.0118 -0.0126 0.0151  121 VAL   B CG1 
5888 C  CG2 . VAL   B 121 ? 0.2107 0.2080 0.1762 0.0025  -0.0330 0.0099  121 VAL   B CG2 
5898 N  N   . LEU   B 122 ? 0.1394 0.1294 0.1570 -0.0214 -0.0248 0.0088  122 LEU   B N   
5899 C  CA  . LEU   B 122 ? 0.1337 0.1368 0.1506 -0.0231 -0.0282 0.0133  122 LEU   B CA  
5900 C  C   . LEU   B 122 ? 0.1405 0.1248 0.1560 -0.0226 -0.0265 0.0107  122 LEU   B C   
5901 O  O   . LEU   B 122 ? 0.1499 0.1213 0.1844 -0.0286 -0.0315 -0.0010 122 LEU   B O   
5902 C  CB  . LEU   B 122 ? 0.1577 0.1474 0.1753 -0.0080 -0.0263 0.0147  122 LEU   B CB  
5903 C  CG  . LEU   B 122 ? 0.1469 0.1541 0.1891 -0.0158 -0.0100 0.0116  122 LEU   B CG  
5904 C  CD1 . LEU   B 122 ? 0.1469 0.1787 0.2033 -0.0303 -0.0234 0.0097  122 LEU   B CD1 
5905 C  CD2 . LEU   B 122 ? 0.1504 0.1501 0.1704 -0.0044 -0.0116 0.0006  122 LEU   B CD2 
5917 N  N   . LEU   B 123 ? 0.1422 0.1136 0.1492 -0.0265 -0.0175 0.0114  123 LEU   B N   
5918 C  CA  . LEU   B 123 ? 0.1448 0.1130 0.1560 -0.0261 -0.0228 0.0037  123 LEU   B CA  
5919 C  C   . LEU   B 123 ? 0.1368 0.1112 0.1538 -0.0277 -0.0248 0.0064  123 LEU   B C   
5920 O  O   . LEU   B 123 ? 0.1421 0.1145 0.1550 -0.0306 -0.0154 -0.0000 123 LEU   B O   
5921 C  CB  . LEU   B 123 ? 0.1471 0.1200 0.1602 -0.0240 -0.0211 -0.0005 123 LEU   B CB  
5922 C  CG  . LEU   B 123 ? 0.1429 0.1274 0.1655 -0.0169 -0.0131 0.0066  123 LEU   B CG  
5923 C  CD1 . LEU   B 123 ? 0.1576 0.1297 0.1855 -0.0194 -0.0059 -0.0078 123 LEU   B CD1 
5924 C  CD2 . LEU   B 123 ? 0.1473 0.1385 0.1773 -0.0197 -0.0016 0.0155  123 LEU   B CD2 
5936 N  N   . ALA   B 124 ? 0.1346 0.1108 0.1564 -0.0223 -0.0083 0.0007  124 ALA   B N   
5937 C  CA  . ALA   B 124 ? 0.1247 0.1152 0.1640 -0.0207 -0.0136 -0.0021 124 ALA   B CA  
5938 C  C   . ALA   B 124 ? 0.1214 0.1128 0.1645 -0.0189 -0.0134 0.0022  124 ALA   B C   
5939 O  O   . ALA   B 124 ? 0.1333 0.1169 0.1694 -0.0153 -0.0096 0.0019  124 ALA   B O   
5940 C  CB  . ALA   B 124 ? 0.1287 0.1220 0.1726 -0.0077 -0.0011 0.0066  124 ALA   B CB  
5946 N  N   . PRO   B 125 ? 0.1302 0.1141 0.1625 -0.0126 -0.0187 0.0133  125 PRO   B N   
5947 C  CA  . PRO   B 125 ? 0.1378 0.1177 0.1696 -0.0138 -0.0108 0.0254  125 PRO   B CA  
5948 C  C   . PRO   B 125 ? 0.1329 0.1176 0.1905 -0.0140 -0.0068 0.0059  125 PRO   B C   
5949 O  O   . PRO   B 125 ? 0.1375 0.1179 0.1988 -0.0104 0.0008  0.0181  125 PRO   B O   
5950 C  CB  . PRO   B 125 ? 0.1401 0.1395 0.1845 -0.0196 -0.0145 0.0389  125 PRO   B CB  
5951 C  CG  . PRO   B 125 ? 0.1470 0.1455 0.1812 -0.0341 -0.0189 0.0209  125 PRO   B CG  
5952 C  CD  . PRO   B 125 ? 0.1396 0.1247 0.1692 -0.0360 -0.0125 0.0110  125 PRO   B CD  
5960 N  N   . LEU   B 126 ? 0.1390 0.1100 0.2103 -0.0162 0.0121  0.0193  126 LEU   B N   
5961 C  CA  . LEU   B 126 ? 0.1434 0.1245 0.2174 -0.0118 0.0185  0.0164  126 LEU   B CA  
5962 C  C   . LEU   B 126 ? 0.1337 0.1351 0.2300 -0.0028 0.0215  0.0203  126 LEU   B C   
5963 O  O   . LEU   B 126 ? 0.1569 0.1600 0.2462 0.0158  -0.0050 -0.0100 126 LEU   B O   
5964 C  CB  . LEU   B 126 ? 0.1595 0.1258 0.2459 -0.0210 0.0276  0.0116  126 LEU   B CB  
5965 C  CG  . LEU   B 126 ? 0.1765 0.1350 0.2630 -0.0319 0.0167  -0.0098 126 LEU   B CG  
5966 C  CD1 . LEU   B 126 ? 0.1935 0.1456 0.3159 -0.0294 0.0113  -0.0179 126 LEU   B CD1 
5967 C  CD2 . LEU   B 126 ? 0.1810 0.1444 0.2587 -0.0356 0.0148  -0.0140 126 LEU   B CD2 
5979 N  N   . LEU   B 127 ? 0.1352 0.1205 0.2288 0.0034  0.0325  0.0114  127 LEU   B N   
5980 C  CA  . LEU   B 127 ? 0.1384 0.1304 0.2268 -0.0044 0.0318  0.0203  127 LEU   B CA  
5981 C  C   . LEU   B 127 ? 0.1315 0.1203 0.2324 -0.0019 0.0176  0.0250  127 LEU   B C   
5982 O  O   . LEU   B 127 ? 0.1333 0.1263 0.2379 -0.0116 0.0132  0.0224  127 LEU   B O   
5983 C  CB  . LEU   B 127 ? 0.1489 0.1279 0.2382 -0.0038 0.0264  0.0223  127 LEU   B CB  
5984 C  CG  . LEU   B 127 ? 0.1616 0.1287 0.2381 0.0045  0.0222  0.0184  127 LEU   B CG  
5985 C  CD1 . LEU   B 127 ? 0.1661 0.1277 0.2452 0.0053  0.0143  0.0139  127 LEU   B CD1 
5986 C  CD2 . LEU   B 127 ? 0.1649 0.1380 0.2480 -0.0195 0.0211  0.0310  127 LEU   B CD2 
5998 N  N   . SER   B 128 ? 0.1361 0.1184 0.2324 0.0005  0.0087  0.0196  128 SER   B N   
5999 C  CA  . SER   B 128 ? 0.1519 0.1293 0.2277 0.0039  -0.0050 0.0289  128 SER   B CA  
6000 C  C   . SER   B 128 ? 0.1630 0.1352 0.2589 0.0011  -0.0246 0.0266  128 SER   B C   
6001 O  O   . SER   B 128 ? 0.1775 0.1425 0.2833 -0.0001 -0.0247 0.0401  128 SER   B O   
6002 C  CB  . SER   B 128 ? 0.1670 0.1312 0.2207 0.0098  0.0057  0.0362  128 SER   B CB  
6003 O  OG  . SER   B 128 ? 0.1746 0.1483 0.2249 0.0063  0.0110  0.0337  128 SER   B OG  
6009 N  N   . ALA   B 129 ? 0.1777 0.1406 0.2776 0.0208  -0.0163 0.0066  129 ALA   B N   
6010 C  CA  . ALA   B 129 ? 0.1906 0.1488 0.2940 0.0278  -0.0104 0.0003  129 ALA   B CA  
6011 C  C   . ALA   B 129 ? 0.1783 0.1371 0.2799 0.0176  0.0038  0.0037  129 ALA   B C   
6012 O  O   . ALA   B 129 ? 0.1653 0.1413 0.2814 0.0152  0.0001  0.0053  129 ALA   B O   
6013 C  CB  . ALA   B 129 ? 0.2089 0.1732 0.3149 0.0267  0.0063  -0.0027 129 ALA   B CB  
6019 N  N   . GLY   B 130 ? 0.1808 0.1345 0.2767 0.0225  0.0057  -0.0028 130 GLY   B N   
6020 C  CA  . GLY   B 130 ? 0.1837 0.1524 0.2811 0.0173  0.0238  -0.0047 130 GLY   B CA  
6021 C  C   . GLY   B 130 ? 0.1901 0.1573 0.2741 0.0082  0.0171  0.0063  130 GLY   B C   
6022 O  O   . GLY   B 130 ? 0.2023 0.1682 0.2758 0.0111  0.0158  0.0216  130 GLY   B O   
6026 N  N   . ILE   B 131 ? 0.1847 0.1694 0.2800 0.0257  0.0079  0.0066  131 ILE   B N   
6027 C  CA  . ILE   B 131 ? 0.2011 0.1817 0.2784 0.0267  0.0021  0.0239  131 ILE   B CA  
6028 C  C   . ILE   B 131 ? 0.2099 0.1764 0.2424 0.0181  0.0022  0.0291  131 ILE   B C   
6029 O  O   . ILE   B 131 ? 0.2414 0.1903 0.2551 0.0214  -0.0068 0.0310  131 ILE   B O   
6030 C  CB  . ILE   B 131 ? 0.1978 0.2064 0.3186 0.0259  -0.0136 0.0364  131 ILE   B CB  
6031 C  CG1 . ILE   B 131 ? 0.2040 0.2252 0.3361 -0.0026 -0.0113 0.0387  131 ILE   B CG1 
6032 C  CG2 . ILE   B 131 ? 0.1953 0.2219 0.3400 0.0396  -0.0143 0.0297  131 ILE   B CG2 
6033 C  CD1 . ILE   B 131 ? 0.2161 0.2432 0.3558 -0.0182 -0.0164 0.0452  131 ILE   B CD1 
6045 N  N   . PHE   B 132 ? 0.1944 0.1596 0.2302 0.0100  0.0177  0.0258  132 PHE   B N   
6046 C  CA  . PHE   B 132 ? 0.2101 0.1594 0.2286 0.0068  0.0426  0.0174  132 PHE   B CA  
6047 C  C   . PHE   B 132 ? 0.2268 0.1731 0.2550 0.0116  0.0592  0.0157  132 PHE   B C   
6048 O  O   . PHE   B 132 ? 0.2412 0.1933 0.2799 0.0019  0.0719  0.0202  132 PHE   B O   
6049 C  CB  . PHE   B 132 ? 0.1926 0.1589 0.2120 0.0098  0.0460  0.0216  132 PHE   B CB  
6050 C  CG  . PHE   B 132 ? 0.1888 0.1620 0.2112 0.0171  0.0397  0.0241  132 PHE   B CG  
6051 C  CD1 . PHE   B 132 ? 0.1954 0.1583 0.2296 0.0161  0.0335  0.0270  132 PHE   B CD1 
6052 C  CD2 . PHE   B 132 ? 0.1908 0.1667 0.1934 0.0283  0.0347  0.0302  132 PHE   B CD2 
6053 C  CE1 . PHE   B 132 ? 0.2041 0.1641 0.2442 0.0084  0.0183  0.0285  132 PHE   B CE1 
6054 C  CE2 . PHE   B 132 ? 0.1984 0.1703 0.2007 0.0252  0.0172  0.0289  132 PHE   B CE2 
6055 C  CZ  . PHE   B 132 ? 0.2031 0.1714 0.2329 0.0105  0.0010  0.0343  132 PHE   B CZ  
6065 N  N   . GLY   B 133 ? 0.2248 0.1645 0.2500 0.0035  0.0420  0.0415  133 GLY   B N   
6066 C  CA  . GLY   B 133 ? 0.2311 0.1763 0.2660 -0.0155 0.0336  0.0489  133 GLY   B CA  
6067 C  C   . GLY   B 133 ? 0.2366 0.1856 0.2667 -0.0308 0.0389  0.0546  133 GLY   B C   
6068 O  O   . GLY   B 133 ? 0.2591 0.1998 0.3059 -0.0440 0.0415  0.0625  133 GLY   B O   
6072 N  N   . ALA   B 134 ? 0.2158 0.1820 0.2540 -0.0306 0.0329  0.0357  134 ALA   B N   
6073 C  CA  . ALA   B 134 ? 0.2136 0.1804 0.2570 -0.0207 0.0412  0.0263  134 ALA   B CA  
6074 C  C   . ALA   B 134 ? 0.2194 0.1706 0.2684 -0.0153 0.0366  0.0398  134 ALA   B C   
6075 O  O   . ALA   B 134 ? 0.2220 0.1864 0.2929 0.0010  0.0302  0.0344  134 ALA   B O   
6076 C  CB  . ALA   B 134 ? 0.2143 0.1824 0.2622 -0.0131 0.0404  0.0193  134 ALA   B CB  
6082 N  N   . ASP   B 135 ? 0.2352 0.1654 0.2786 -0.0172 0.0221  0.0450  135 ASP   B N   
6083 C  CA  . ASP   B 135 ? 0.2474 0.1530 0.2977 -0.0175 0.0065  0.0466  135 ASP   B CA  
6084 C  C   . ASP   B 135 ? 0.2236 0.1456 0.2824 -0.0054 0.0027  0.0390  135 ASP   B C   
6085 O  O   . ASP   B 135 ? 0.2156 0.1457 0.2901 -0.0087 0.0080  0.0351  135 ASP   B O   
6086 C  CB  . ASP   B 135 ? 0.2814 0.1625 0.3263 -0.0351 0.0033  0.0531  135 ASP   B CB  
6087 C  CG  . ASP   B 135 ? 0.3098 0.1651 0.3685 -0.0552 0.0046  0.0443  135 ASP   B CG  
6088 O  OD1 . ASP   B 135 ? 0.3173 0.1509 0.3716 -0.0330 -0.0090 0.0376  135 ASP   B OD1 
6089 O  OD2 . ASP   B 135 ? 0.3319 0.1991 0.4222 -0.0696 0.0109  0.0256  135 ASP   B OD2 
6094 N  N   . PRO   B 136 ? 0.2133 0.1496 0.2892 0.0141  -0.0141 0.0264  136 PRO   B N   
6095 C  CA  . PRO   B 136 ? 0.1920 0.1375 0.2881 0.0126  -0.0087 0.0163  136 PRO   B CA  
6096 C  C   . PRO   B 136 ? 0.1758 0.1230 0.2984 0.0151  -0.0066 0.0138  136 PRO   B C   
6097 O  O   . PRO   B 136 ? 0.1589 0.1249 0.2936 0.0090  -0.0002 0.0121  136 PRO   B O   
6098 C  CB  . PRO   B 136 ? 0.1972 0.1638 0.2900 0.0239  -0.0137 0.0034  136 PRO   B CB  
6099 C  CG  . PRO   B 136 ? 0.2177 0.1743 0.3107 0.0326  -0.0061 0.0032  136 PRO   B CG  
6100 C  CD  . PRO   B 136 ? 0.2183 0.1724 0.3067 0.0401  -0.0026 0.0083  136 PRO   B CD  
6108 N  N   . ILE   B 137 ? 0.1879 0.1201 0.3072 0.0214  -0.0087 0.0081  137 ILE   B N   
6109 C  CA  . ILE   B 137 ? 0.1947 0.1223 0.3166 0.0040  -0.0045 0.0031  137 ILE   B CA  
6110 C  C   . ILE   B 137 ? 0.1856 0.1274 0.3024 -0.0088 0.0018  0.0161  137 ILE   B C   
6111 O  O   . ILE   B 137 ? 0.1737 0.1258 0.2881 -0.0125 0.0075  0.0126  137 ILE   B O   
6112 C  CB  . ILE   B 137 ? 0.2216 0.1230 0.3568 -0.0084 0.0011  -0.0019 137 ILE   B CB  
6113 C  CG1 . ILE   B 137 ? 0.2433 0.1423 0.4029 0.0009  0.0146  -0.0122 137 ILE   B CG1 
6114 C  CG2 . ILE   B 137 ? 0.2246 0.1284 0.3642 -0.0320 -0.0102 0.0023  137 ILE   B CG2 
6115 C  CD1 . ILE   B 137 ? 0.2645 0.1741 0.4373 0.0162  0.0087  -0.0027 137 ILE   B CD1 
6127 N  N   . HIS   B 138 ? 0.1901 0.1273 0.2980 -0.0093 0.0188  0.0179  138 HIS   B N   
6128 C  CA  . HIS   B 138 ? 0.2001 0.1369 0.2958 -0.0096 0.0374  0.0248  138 HIS   B CA  
6129 C  C   . HIS   B 138 ? 0.1758 0.1356 0.2813 -0.0048 0.0315  0.0271  138 HIS   B C   
6130 O  O   . HIS   B 138 ? 0.1655 0.1407 0.3043 0.0015  0.0343  0.0374  138 HIS   B O   
6131 C  CB  . HIS   B 138 ? 0.2238 0.1494 0.3040 -0.0127 0.0562  0.0219  138 HIS   B CB  
6132 C  CG  . HIS   B 138 ? 0.2435 0.1652 0.3116 -0.0158 0.0769  0.0388  138 HIS   B CG  
6133 N  ND1 . HIS   B 138 ? 0.2531 0.1841 0.3363 -0.0100 0.0879  0.0315  138 HIS   B ND1 
6134 C  CD2 . HIS   B 138 ? 0.2562 0.1812 0.3076 -0.0142 0.0795  0.0324  138 HIS   B CD2 
6135 C  CE1 . HIS   B 138 ? 0.2553 0.1909 0.3385 -0.0106 0.0836  0.0317  138 HIS   B CE1 
6136 N  NE2 . HIS   B 138 ? 0.2582 0.1837 0.3166 -0.0068 0.0858  0.0262  138 HIS   B NE2 
6144 N  N   . SER   B 139 ? 0.1745 0.1188 0.2801 -0.0010 0.0259  0.0196  139 SER   B N   
6145 C  CA  . SER   B 139 ? 0.1718 0.1121 0.2648 -0.0009 0.0295  0.0083  139 SER   B CA  
6146 C  C   . SER   B 139 ? 0.1473 0.1092 0.2646 -0.0052 0.0130  0.0118  139 SER   B C   
6147 O  O   . SER   B 139 ? 0.1465 0.1145 0.2735 -0.0027 0.0045  0.0175  139 SER   B O   
6148 C  CB  . SER   B 139 ? 0.1788 0.1158 0.2684 -0.0054 0.0064  0.0055  139 SER   B CB  
6149 O  OG  . SER   B 139 ? 0.1753 0.1199 0.2741 -0.0036 -0.0020 0.0169  139 SER   B OG  
6155 N  N   . LEU   B 140 ? 0.1510 0.1066 0.2519 -0.0089 0.0185  0.0020  140 LEU   B N   
6156 C  CA  . LEU   B 140 ? 0.1495 0.1072 0.2513 -0.0054 0.0169  0.0024  140 LEU   B CA  
6157 C  C   . LEU   B 140 ? 0.1481 0.1082 0.2688 -0.0070 0.0035  0.0021  140 LEU   B C   
6158 O  O   . LEU   B 140 ? 0.1438 0.1179 0.2616 -0.0044 -0.0011 0.0072  140 LEU   B O   
6159 C  CB  . LEU   B 140 ? 0.1461 0.1103 0.2586 -0.0139 0.0153  -0.0088 140 LEU   B CB  
6160 C  CG  . LEU   B 140 ? 0.1570 0.1144 0.2632 -0.0157 0.0024  0.0013  140 LEU   B CG  
6161 C  CD1 . LEU   B 140 ? 0.1647 0.1225 0.2688 -0.0163 0.0128  0.0043  140 LEU   B CD1 
6162 C  CD2 . LEU   B 140 ? 0.1713 0.1290 0.2692 -0.0203 -0.0046 -0.0030 140 LEU   B CD2 
6174 N  N   . ARG   B 141 ? 0.1328 0.1097 0.2740 -0.0067 0.0124  0.0027  141 ARG   B N   
6175 C  CA  . ARG   B 141 ? 0.1424 0.1129 0.3168 -0.0174 0.0271  0.0007  141 ARG   B CA  
6176 C  C   . ARG   B 141 ? 0.1333 0.1150 0.3024 -0.0165 0.0134  0.0061  141 ARG   B C   
6177 O  O   . ARG   B 141 ? 0.1364 0.1216 0.2928 -0.0143 0.0014  -0.0047 141 ARG   B O   
6178 C  CB  . ARG   B 141 ? 0.1579 0.1267 0.3381 -0.0202 0.0379  -0.0023 141 ARG   B CB  
6179 C  CG  . ARG   B 141 ? 0.1862 0.1558 0.3450 -0.0208 0.0357  -0.0040 141 ARG   B CG  
6180 C  CD  . ARG   B 141 ? 0.2299 0.1812 0.3397 -0.0194 0.0191  -0.0096 141 ARG   B CD  
6181 N  NE  . ARG   B 141 ? 0.2568 0.1761 0.3269 -0.0338 0.0244  -0.0201 141 ARG   B NE  
6182 C  CZ  . ARG   B 141 ? 0.2712 0.1641 0.3044 -0.0305 0.0329  -0.0267 141 ARG   B CZ  
6183 N  NH1 . ARG   B 141 ? 0.2807 0.1505 0.2939 -0.0313 0.0293  -0.0360 141 ARG   B NH1 
6184 N  NH2 . ARG   B 141 ? 0.2742 0.1730 0.3121 -0.0214 0.0242  -0.0161 141 ARG   B NH2 
6198 N  N   . VAL   B 142 ? 0.1380 0.1079 0.2965 -0.0145 0.0216  0.0025  142 VAL   B N   
6199 C  CA  . VAL   B 142 ? 0.1345 0.1158 0.2887 -0.0064 0.0233  -0.0044 142 VAL   B CA  
6200 C  C   . VAL   B 142 ? 0.1312 0.1124 0.2812 0.0003  0.0157  -0.0019 142 VAL   B C   
6201 O  O   . VAL   B 142 ? 0.1369 0.1157 0.2879 -0.0011 0.0125  -0.0001 142 VAL   B O   
6202 C  CB  . VAL   B 142 ? 0.1450 0.1262 0.2836 0.0010  0.0254  0.0154  142 VAL   B CB  
6203 C  CG1 . VAL   B 142 ? 0.1445 0.1268 0.2766 0.0063  0.0245  0.0072  142 VAL   B CG1 
6204 C  CG2 . VAL   B 142 ? 0.1681 0.1267 0.2841 0.0004  0.0230  0.0170  142 VAL   B CG2 
6214 N  N   . CYS   B 143 ? 0.1244 0.1135 0.2651 0.0011  0.0071  0.0077  143 CYS   B N   
6215 C  CA  . CYS   B 143 ? 0.1205 0.1115 0.2676 -0.0070 0.0015  0.0048  143 CYS   B CA  
6216 C  C   . CYS   B 143 ? 0.1187 0.1120 0.2650 -0.0077 0.0088  0.0009  143 CYS   B C   
6217 O  O   . CYS   B 143 ? 0.1240 0.1217 0.2519 -0.0070 -0.0005 -0.0011 143 CYS   B O   
6218 C  CB  . CYS   B 143 ? 0.1328 0.1260 0.2621 -0.0068 0.0023  0.0055  143 CYS   B CB  
6219 S  SG  . CYS   B 143 ? 0.1332 0.1379 0.2475 -0.0055 0.0020  0.0069  143 CYS   B SG  
6225 N  N   . VAL   B 144 ? 0.1250 0.1113 0.2844 -0.0100 -0.0032 -0.0172 144 VAL   B N   
6226 C  CA  . VAL   B 144 ? 0.1310 0.1257 0.2971 -0.0183 -0.0149 -0.0211 144 VAL   B CA  
6227 C  C   . VAL   B 144 ? 0.1294 0.1279 0.2924 -0.0141 -0.0168 0.0032  144 VAL   B C   
6228 O  O   . VAL   B 144 ? 0.1415 0.1483 0.3094 -0.0069 -0.0144 0.0218  144 VAL   B O   
6229 C  CB  . VAL   B 144 ? 0.1606 0.1442 0.3552 -0.0193 -0.0246 -0.0355 144 VAL   B CB  
6230 C  CG1 . VAL   B 144 ? 0.1846 0.1913 0.3769 -0.0146 -0.0291 -0.0228 144 VAL   B CG1 
6231 C  CG2 . VAL   B 144 ? 0.1751 0.1380 0.3431 -0.0016 -0.0414 -0.0437 144 VAL   B CG2 
6241 N  N   . ASP   B 145 ? 0.1305 0.1215 0.3078 -0.0144 -0.0029 -0.0109 145 ASP   B N   
6242 C  CA  . ASP   B 145 ? 0.1329 0.1234 0.3363 -0.0091 0.0090  -0.0056 145 ASP   B CA  
6243 C  C   . ASP   B 145 ? 0.1272 0.1249 0.3155 -0.0075 0.0061  -0.0076 145 ASP   B C   
6244 O  O   . ASP   B 145 ? 0.1297 0.1426 0.3681 -0.0125 0.0094  -0.0237 145 ASP   B O   
6245 C  CB  . ASP   B 145 ? 0.1404 0.1339 0.3747 -0.0172 0.0214  0.0006  145 ASP   B CB  
6246 C  CG  . ASP   B 145 ? 0.1584 0.1375 0.4162 -0.0215 0.0285  -0.0069 145 ASP   B CG  
6247 O  OD1 . ASP   B 145 ? 0.1632 0.1411 0.4088 -0.0234 -0.0099 -0.0187 145 ASP   B OD1 
6248 O  OD2 . ASP   B 145 ? 0.1905 0.1434 0.4574 -0.0316 0.0511  -0.0032 145 ASP   B OD2 
6253 N  N   . THR   B 146 ? 0.1238 0.1168 0.2728 -0.0103 -0.0003 0.0010  146 THR   B N   
6254 C  CA  . THR   B 146 ? 0.1279 0.1152 0.2596 -0.0078 0.0128  -0.0022 146 THR   B CA  
6255 C  C   . THR   B 146 ? 0.1347 0.1157 0.2527 -0.0099 0.0051  0.0029  146 THR   B C   
6256 O  O   . THR   B 146 ? 0.1398 0.1134 0.2556 -0.0097 -0.0041 0.0012  146 THR   B O   
6257 C  CB  . THR   B 146 ? 0.1348 0.1105 0.2611 -0.0061 0.0158  0.0005  146 THR   B CB  
6258 O  OG1 . THR   B 146 ? 0.1423 0.1121 0.2783 -0.0074 0.0209  0.0064  146 THR   B OG1 
6259 C  CG2 . THR   B 146 ? 0.1445 0.1222 0.2678 -0.0035 0.0146  -0.0030 146 THR   B CG2 
6267 N  N   . VAL   B 147 ? 0.1310 0.1146 0.2370 -0.0080 0.0121  0.0027  147 VAL   B N   
6268 C  CA  . VAL   B 147 ? 0.1318 0.1125 0.2333 -0.0084 -0.0085 -0.0019 147 VAL   B CA  
6269 C  C   . VAL   B 147 ? 0.1263 0.1149 0.2439 -0.0184 -0.0165 -0.0005 147 VAL   B C   
6270 O  O   . VAL   B 147 ? 0.1407 0.1259 0.2589 -0.0216 -0.0353 -0.0079 147 VAL   B O   
6271 C  CB  . VAL   B 147 ? 0.1396 0.1269 0.2193 -0.0067 -0.0109 0.0030  147 VAL   B CB  
6272 C  CG1 . VAL   B 147 ? 0.1404 0.1410 0.1957 -0.0069 -0.0092 0.0062  147 VAL   B CG1 
6273 C  CG2 . VAL   B 147 ? 0.1374 0.1252 0.2176 -0.0081 -0.0019 0.0080  147 VAL   B CG2 
6283 N  N   . ARG   B 148 ? 0.1318 0.1143 0.2329 -0.0134 -0.0201 -0.0030 148 ARG   B N   
6284 C  CA  . ARG   B 148 ? 0.1331 0.1290 0.2218 -0.0092 -0.0284 -0.0093 148 ARG   B CA  
6285 C  C   . ARG   B 148 ? 0.1402 0.1414 0.2093 -0.0130 -0.0290 -0.0032 148 ARG   B C   
6286 O  O   . ARG   B 148 ? 0.1587 0.1685 0.2153 -0.0287 -0.0418 0.0032  148 ARG   B O   
6287 C  CB  . ARG   B 148 ? 0.1421 0.1369 0.2172 0.0006  -0.0362 -0.0202 148 ARG   B CB  
6288 C  CG  . ARG   B 148 ? 0.1400 0.1554 0.2325 -0.0081 -0.0341 -0.0358 148 ARG   B CG  
6289 C  CD  . ARG   B 148 ? 0.1436 0.1742 0.2482 0.0053  -0.0388 -0.0397 148 ARG   B CD  
6290 N  NE  . ARG   B 148 ? 0.1473 0.1738 0.2571 0.0193  -0.0391 -0.0413 148 ARG   B NE  
6291 C  CZ  . ARG   B 148 ? 0.1404 0.1587 0.2385 0.0118  -0.0280 -0.0330 148 ARG   B CZ  
6292 N  NH1 . ARG   B 148 ? 0.1400 0.1640 0.2381 -0.0095 -0.0022 -0.0239 148 ARG   B NH1 
6293 N  NH2 . ARG   B 148 ? 0.1601 0.1444 0.2244 0.0150  -0.0145 -0.0184 148 ARG   B NH2 
6307 N  N   . THR   B 149 ? 0.1435 0.1297 0.2038 -0.0129 -0.0275 -0.0002 149 THR   B N   
6308 C  CA  . THR   B 149 ? 0.1512 0.1328 0.1962 -0.0140 -0.0262 0.0060  149 THR   B CA  
6309 C  C   . THR   B 149 ? 0.1497 0.1332 0.1959 -0.0171 -0.0282 0.0052  149 THR   B C   
6310 O  O   . THR   B 149 ? 0.1548 0.1285 0.2103 -0.0222 -0.0147 0.0042  149 THR   B O   
6311 C  CB  . THR   B 149 ? 0.1549 0.1270 0.2125 -0.0150 -0.0369 0.0047  149 THR   B CB  
6312 O  OG1 . THR   B 149 ? 0.1552 0.1367 0.2046 -0.0241 -0.0376 0.0068  149 THR   B OG1 
6313 C  CG2 . THR   B 149 ? 0.1630 0.1352 0.2190 -0.0073 -0.0335 -0.0003 149 THR   B CG2 
6321 N  N   . ASN   B 150 ? 0.1572 0.1347 0.1845 -0.0180 -0.0382 0.0031  150 ASN   B N   
6322 C  CA  . ASN   B 150 ? 0.1677 0.1438 0.1771 -0.0248 -0.0328 -0.0026 150 ASN   B CA  
6323 C  C   . ASN   B 150 ? 0.1534 0.1395 0.1958 -0.0227 -0.0272 -0.0020 150 ASN   B C   
6324 O  O   . ASN   B 150 ? 0.1616 0.1347 0.2021 -0.0274 -0.0420 -0.0017 150 ASN   B O   
6325 C  CB  . ASN   B 150 ? 0.1898 0.1760 0.1955 -0.0291 -0.0500 0.0105  150 ASN   B CB  
6326 C  CG  . ASN   B 150 ? 0.2178 0.2154 0.2388 -0.0208 -0.0541 0.0256  150 ASN   B CG  
6327 O  OD1 . ASN   B 150 ? 0.2264 0.2312 0.2449 -0.0265 -0.0670 0.0184  150 ASN   B OD1 
6328 N  ND2 . ASN   B 150 ? 0.2312 0.2334 0.2685 -0.0124 -0.0558 0.0650  150 ASN   B ND2 
6335 N  N   . VAL   B 151 ? 0.1460 0.1366 0.1935 -0.0254 -0.0360 -0.0031 151 VAL   B N   
6336 C  CA  . VAL   B 151 ? 0.1487 0.1419 0.1862 -0.0274 -0.0212 -0.0084 151 VAL   B CA  
6337 C  C   . VAL   B 151 ? 0.1501 0.1329 0.1823 -0.0315 -0.0282 -0.0015 151 VAL   B C   
6338 O  O   . VAL   B 151 ? 0.1614 0.1367 0.2121 -0.0276 -0.0267 -0.0057 151 VAL   B O   
6339 C  CB  . VAL   B 151 ? 0.1672 0.1487 0.1937 -0.0153 -0.0181 -0.0109 151 VAL   B CB  
6340 C  CG1 . VAL   B 151 ? 0.1774 0.1539 0.2270 -0.0221 -0.0093 -0.0128 151 VAL   B CG1 
6341 C  CG2 . VAL   B 151 ? 0.1790 0.1653 0.1801 0.0062  -0.0230 0.0046  151 VAL   B CG2 
6351 N  N   . TYR   B 152 ? 0.1432 0.1242 0.1796 -0.0241 -0.0250 -0.0045 152 TYR   B N   
6352 C  CA  . TYR   B 152 ? 0.1513 0.1422 0.1678 -0.0309 -0.0132 -0.0082 152 TYR   B CA  
6353 C  C   . TYR   B 152 ? 0.1533 0.1236 0.1616 -0.0216 -0.0179 -0.0117 152 TYR   B C   
6354 O  O   . TYR   B 152 ? 0.1587 0.1266 0.1685 -0.0291 -0.0133 -0.0038 152 TYR   B O   
6355 C  CB  . TYR   B 152 ? 0.1632 0.1594 0.1623 -0.0292 -0.0192 0.0025  152 TYR   B CB  
6356 C  CG  . TYR   B 152 ? 0.1811 0.1663 0.1652 -0.0422 -0.0233 0.0002  152 TYR   B CG  
6357 C  CD1 . TYR   B 152 ? 0.1930 0.1744 0.1574 -0.0364 -0.0273 0.0074  152 TYR   B CD1 
6358 C  CD2 . TYR   B 152 ? 0.1985 0.1815 0.1681 -0.0419 -0.0196 -0.0075 152 TYR   B CD2 
6359 C  CE1 . TYR   B 152 ? 0.2064 0.1922 0.1796 -0.0300 -0.0289 0.0193  152 TYR   B CE1 
6360 C  CE2 . TYR   B 152 ? 0.2088 0.2033 0.1695 -0.0434 -0.0178 -0.0135 152 TYR   B CE2 
6361 C  CZ  . TYR   B 152 ? 0.2081 0.2146 0.1627 -0.0394 -0.0457 0.0105  152 TYR   B CZ  
6362 O  OH  . TYR   B 152 ? 0.2334 0.2476 0.2079 -0.0283 -0.0427 0.0169  152 TYR   B OH  
6372 N  N   . LEU   B 153 ? 0.1519 0.1193 0.1727 -0.0297 -0.0175 -0.0070 153 LEU   B N   
6373 C  CA  . LEU   B 153 ? 0.1549 0.1200 0.1700 -0.0243 -0.0114 -0.0097 153 LEU   B CA  
6374 C  C   . LEU   B 153 ? 0.1522 0.1159 0.1848 -0.0256 -0.0111 -0.0229 153 LEU   B C   
6375 O  O   . LEU   B 153 ? 0.1606 0.1383 0.1886 -0.0164 -0.0118 -0.0370 153 LEU   B O   
6376 C  CB  . LEU   B 153 ? 0.1520 0.1125 0.1786 -0.0306 -0.0164 -0.0062 153 LEU   B CB  
6377 C  CG  . LEU   B 153 ? 0.1478 0.1281 0.2023 -0.0279 -0.0050 -0.0031 153 LEU   B CG  
6378 C  CD1 . LEU   B 153 ? 0.1570 0.1396 0.2137 -0.0264 0.0017  0.0116  153 LEU   B CD1 
6379 C  CD2 . LEU   B 153 ? 0.1485 0.1376 0.2148 -0.0309 0.0077  0.0059  153 LEU   B CD2 
6391 N  N   . ALA   B 154 ? 0.1408 0.1238 0.1886 -0.0138 -0.0167 -0.0173 154 ALA   B N   
6392 C  CA  . ALA   B 154 ? 0.1515 0.1320 0.2032 -0.0062 -0.0120 -0.0252 154 ALA   B CA  
6393 C  C   . ALA   B 154 ? 0.1645 0.1370 0.2102 -0.0015 -0.0185 -0.0274 154 ALA   B C   
6394 O  O   . ALA   B 154 ? 0.1966 0.1338 0.2321 0.0013  -0.0065 -0.0084 154 ALA   B O   
6395 C  CB  . ALA   B 154 ? 0.1474 0.1470 0.2371 -0.0041 -0.0084 -0.0312 154 ALA   B CB  
6401 N  N   . VAL   B 155 ? 0.1352 0.1257 0.2283 -0.0116 0.0031  -0.0166 155 VAL   B N   
6402 C  CA  . VAL   B 155 ? 0.1336 0.1242 0.2476 -0.0087 -0.0127 -0.0142 155 VAL   B CA  
6403 C  C   . VAL   B 155 ? 0.1328 0.1268 0.2451 -0.0068 -0.0133 -0.0233 155 VAL   B C   
6404 O  O   . VAL   B 155 ? 0.1537 0.1422 0.2703 0.0026  -0.0144 -0.0386 155 VAL   B O   
6405 C  CB  . VAL   B 155 ? 0.1405 0.1396 0.2664 -0.0111 -0.0248 0.0013  155 VAL   B CB  
6406 C  CG1 . VAL   B 155 ? 0.1499 0.1377 0.2703 -0.0178 -0.0198 0.0041  155 VAL   B CG1 
6407 C  CG2 . VAL   B 155 ? 0.1342 0.1556 0.2954 -0.0063 -0.0157 0.0371  155 VAL   B CG2 
6417 N  N   . PHE   B 156 ? 0.1231 0.1366 0.2622 0.0025  -0.0056 -0.0219 156 PHE   B N   
6418 C  CA  . PHE   B 156 ? 0.1292 0.1432 0.2855 0.0048  -0.0030 -0.0177 156 PHE   B CA  
6419 C  C   . PHE   B 156 ? 0.1281 0.1559 0.3224 0.0074  -0.0070 -0.0365 156 PHE   B C   
6420 O  O   . PHE   B 156 ? 0.1534 0.1741 0.3475 0.0186  -0.0032 -0.0449 156 PHE   B O   
6421 C  CB  . PHE   B 156 ? 0.1390 0.1441 0.2822 0.0033  -0.0111 -0.0069 156 PHE   B CB  
6422 C  CG  . PHE   B 156 ? 0.1399 0.1578 0.2937 0.0018  -0.0111 0.0085  156 PHE   B CG  
6423 C  CD1 . PHE   B 156 ? 0.1390 0.1831 0.3278 0.0037  -0.0031 0.0369  156 PHE   B CD1 
6424 C  CD2 . PHE   B 156 ? 0.1455 0.1680 0.2825 0.0105  -0.0238 0.0100  156 PHE   B CD2 
6425 C  CE1 . PHE   B 156 ? 0.1453 0.1986 0.3379 0.0049  -0.0031 0.0367  156 PHE   B CE1 
6426 C  CE2 . PHE   B 156 ? 0.1509 0.1899 0.3095 0.0118  -0.0157 0.0125  156 PHE   B CE2 
6427 C  CZ  . PHE   B 156 ? 0.1449 0.2004 0.3340 0.0179  -0.0123 0.0244  156 PHE   B CZ  
6437 N  N   . ASP   B 157 ? 0.1366 0.1466 0.3416 0.0141  -0.0306 -0.0152 157 ASP   B N   
6438 C  CA  . ASP   B 157 ? 0.1449 0.1537 0.3781 0.0072  -0.0259 -0.0263 157 ASP   B CA  
6439 C  C   . ASP   B 157 ? 0.1434 0.1498 0.3864 0.0081  -0.0226 -0.0435 157 ASP   B C   
6440 O  O   . ASP   B 157 ? 0.1330 0.1459 0.3753 0.0051  -0.0180 -0.0392 157 ASP   B O   
6441 C  CB  . ASP   B 157 ? 0.1704 0.1713 0.3975 0.0020  -0.0454 -0.0131 157 ASP   B CB  
6442 C  CG  . ASP   B 157 ? 0.2111 0.1827 0.4260 -0.0044 -0.0314 -0.0116 157 ASP   B CG  
6443 O  OD1 . ASP   B 157 ? 0.2175 0.1716 0.4409 0.0054  -0.0292 -0.0034 157 ASP   B OD1 
6444 O  OD2 . ASP   B 157 ? 0.2479 0.2019 0.4512 -0.0032 -0.0100 -0.0131 157 ASP   B OD2 
6449 N  N   . LYS   B 158 ? 0.1463 0.1748 0.3920 0.0085  -0.0128 -0.0675 158 LYS   B N   
6450 C  CA  . LYS   B 158 ? 0.1639 0.1941 0.4007 0.0053  0.0033  -0.0914 158 LYS   B CA  
6451 C  C   . LYS   B 158 ? 0.1674 0.1787 0.4123 0.0104  -0.0001 -0.0906 158 LYS   B C   
6452 O  O   . LYS   B 158 ? 0.1725 0.1786 0.4208 -0.0045 -0.0005 -0.0979 158 LYS   B O   
6453 C  CB  . LYS   B 158 ? 0.1889 0.2364 0.4066 0.0041  0.0248  -0.1139 158 LYS   B CB  
6454 C  CG  . LYS   B 158 ? 0.2362 0.2754 0.4144 0.0073  0.0280  -0.1252 158 LYS   B CG  
6455 C  CD  . LYS   B 158 ? 0.2751 0.3239 0.4289 0.0033  0.0351  -0.1171 158 LYS   B CD  
6456 C  CE  . LYS   B 158 ? 0.2981 0.3544 0.4400 0.0064  0.0378  -0.1134 158 LYS   B CE  
6457 N  NZ  . LYS   B 158 ? 0.2960 0.3645 0.4380 0.0056  0.0393  -0.1148 158 LYS   B NZ  
6471 N  N   . ASN   B 159 ? 0.1712 0.1719 0.4281 -0.0005 -0.0154 -0.0731 159 ASN   B N   
6472 C  CA  . ASN   B 159 ? 0.1781 0.1659 0.4443 0.0148  -0.0311 -0.0548 159 ASN   B CA  
6473 C  C   . ASN   B 159 ? 0.1601 0.1453 0.4328 0.0059  -0.0502 -0.0440 159 ASN   B C   
6474 O  O   . ASN   B 159 ? 0.1630 0.1348 0.4475 -0.0054 -0.0541 -0.0269 159 ASN   B O   
6475 C  CB  . ASN   B 159 ? 0.2020 0.1828 0.4742 0.0296  -0.0435 -0.0484 159 ASN   B CB  
6476 C  CG  . ASN   B 159 ? 0.2331 0.1999 0.4971 0.0381  -0.0565 -0.0616 159 ASN   B CG  
6477 O  OD1 . ASN   B 159 ? 0.2546 0.2045 0.5056 0.0474  -0.0566 -0.0724 159 ASN   B OD1 
6478 N  ND2 . ASN   B 159 ? 0.2302 0.2060 0.5139 0.0379  -0.0600 -0.0590 159 ASN   B ND2 
6485 N  N   . LEU   B 160 ? 0.1516 0.1445 0.4138 0.0050  -0.0543 -0.0356 160 LEU   B N   
6486 C  CA  . LEU   B 160 ? 0.1538 0.1498 0.3719 0.0104  -0.0424 -0.0207 160 LEU   B CA  
6487 C  C   . LEU   B 160 ? 0.1436 0.1359 0.3555 0.0018  -0.0306 -0.0356 160 LEU   B C   
6488 O  O   . LEU   B 160 ? 0.1297 0.1399 0.3505 -0.0022 -0.0325 -0.0252 160 LEU   B O   
6489 C  CB  . LEU   B 160 ? 0.1518 0.1540 0.3450 0.0118  -0.0428 -0.0115 160 LEU   B CB  
6490 C  CG  . LEU   B 160 ? 0.1474 0.1692 0.3179 0.0059  -0.0356 -0.0095 160 LEU   B CG  
6491 C  CD1 . LEU   B 160 ? 0.1709 0.1849 0.3168 -0.0047 -0.0242 -0.0122 160 LEU   B CD1 
6492 C  CD2 . LEU   B 160 ? 0.1532 0.1763 0.3144 0.0144  -0.0239 -0.0195 160 LEU   B CD2 
6504 N  N   . TYR   B 161 ? 0.1453 0.1410 0.3549 -0.0108 -0.0047 -0.0481 161 TYR   B N   
6505 C  CA  . TYR   B 161 ? 0.1544 0.1415 0.3475 -0.0199 0.0125  -0.0542 161 TYR   B CA  
6506 C  C   . TYR   B 161 ? 0.1601 0.1404 0.3382 -0.0157 0.0206  -0.0528 161 TYR   B C   
6507 O  O   . TYR   B 161 ? 0.1680 0.1411 0.3313 -0.0223 0.0105  -0.0366 161 TYR   B O   
6508 C  CB  . TYR   B 161 ? 0.1732 0.1556 0.3404 -0.0246 0.0305  -0.0635 161 TYR   B CB  
6509 C  CG  . TYR   B 161 ? 0.1939 0.1589 0.3323 -0.0358 0.0370  -0.0708 161 TYR   B CG  
6510 C  CD1 . TYR   B 161 ? 0.2030 0.1595 0.3348 -0.0471 0.0451  -0.0624 161 TYR   B CD1 
6511 C  CD2 . TYR   B 161 ? 0.2223 0.1658 0.3271 -0.0295 0.0309  -0.0698 161 TYR   B CD2 
6512 C  CE1 . TYR   B 161 ? 0.2282 0.1799 0.3337 -0.0517 0.0420  -0.0649 161 TYR   B CE1 
6513 C  CE2 . TYR   B 161 ? 0.2430 0.1881 0.3230 -0.0379 0.0390  -0.0610 161 TYR   B CE2 
6514 C  CZ  . TYR   B 161 ? 0.2446 0.1926 0.3267 -0.0555 0.0327  -0.0563 161 TYR   B CZ  
6515 O  OH  . TYR   B 161 ? 0.2729 0.2152 0.3517 -0.0555 0.0357  -0.0499 161 TYR   B OH  
6525 N  N   . ASP   B 162 ? 0.1660 0.1425 0.3560 -0.0114 0.0047  -0.0641 162 ASP   B N   
6526 C  CA  . ASP   B 162 ? 0.1719 0.1464 0.3619 -0.0068 -0.0048 -0.0612 162 ASP   B CA  
6527 C  C   . ASP   B 162 ? 0.1690 0.1414 0.3505 -0.0080 -0.0078 -0.0407 162 ASP   B C   
6528 O  O   . ASP   B 162 ? 0.1736 0.1455 0.3493 -0.0171 -0.0271 -0.0335 162 ASP   B O   
6529 C  CB  . ASP   B 162 ? 0.1927 0.1662 0.3824 -0.0036 -0.0167 -0.0766 162 ASP   B CB  
6530 C  CG  . ASP   B 162 ? 0.2014 0.1934 0.4005 0.0050  -0.0050 -0.0934 162 ASP   B CG  
6531 O  OD1 . ASP   B 162 ? 0.2031 0.2126 0.3968 -0.0062 0.0079  -0.0860 162 ASP   B OD1 
6532 O  OD2 . ASP   B 162 ? 0.2108 0.2167 0.4273 0.0201  0.0040  -0.0856 162 ASP   B OD2 
6537 N  N   A LYS   B 163 ? 0.1649 0.1193 0.3351 -0.0044 -0.0184 -0.0263 163 LYS   B N   
6538 N  N   B LYS   B 163 ? 0.1719 0.1418 0.3385 -0.0075 -0.0161 -0.0250 163 LYS   B N   
6539 C  CA  A LYS   B 163 ? 0.1744 0.1323 0.3362 -0.0162 -0.0168 -0.0082 163 LYS   B CA  
6540 C  CA  B LYS   B 163 ? 0.1803 0.1587 0.3355 -0.0126 -0.0164 -0.0093 163 LYS   B CA  
6541 C  C   A LYS   B 163 ? 0.1474 0.1298 0.3200 -0.0170 -0.0168 -0.0028 163 LYS   B C   
6542 C  C   B LYS   B 163 ? 0.1544 0.1423 0.3181 -0.0144 -0.0178 -0.0033 163 LYS   B C   
6543 O  O   A LYS   B 163 ? 0.1413 0.1419 0.3368 -0.0169 -0.0151 -0.0038 163 LYS   B O   
6544 O  O   B LYS   B 163 ? 0.1510 0.1479 0.3254 -0.0150 -0.0186 -0.0029 163 LYS   B O   
6545 C  CB  A LYS   B 163 ? 0.2121 0.1583 0.3626 -0.0172 -0.0190 0.0035  163 LYS   B CB  
6546 C  CB  B LYS   B 163 ? 0.2135 0.1954 0.3585 -0.0116 -0.0186 -0.0018 163 LYS   B CB  
6547 C  CG  A LYS   B 163 ? 0.2731 0.2205 0.4005 -0.0172 -0.0054 0.0035  163 LYS   B CG  
6548 C  CG  B LYS   B 163 ? 0.2545 0.2392 0.3881 -0.0105 -0.0117 -0.0003 163 LYS   B CG  
6549 C  CD  A LYS   B 163 ? 0.3255 0.2688 0.4417 -0.0242 -0.0001 -0.0078 163 LYS   B CD  
6550 C  CD  B LYS   B 163 ? 0.2907 0.2772 0.4226 -0.0135 -0.0085 -0.0037 163 LYS   B CD  
6551 C  CE  A LYS   B 163 ? 0.3557 0.3032 0.4695 -0.0274 0.0062  -0.0096 163 LYS   B CE  
6552 C  CE  B LYS   B 163 ? 0.3177 0.3079 0.4487 -0.0154 -0.0043 -0.0034 163 LYS   B CE  
6553 N  NZ  A LYS   B 163 ? 0.3700 0.3060 0.4871 -0.0286 0.0085  -0.0121 163 LYS   B NZ  
6554 N  NZ  B LYS   B 163 ? 0.3278 0.3146 0.4653 -0.0161 -0.0025 -0.0040 163 LYS   B NZ  
6581 N  N   . LEU   B 164 ? 0.1370 0.1251 0.2996 -0.0139 -0.0214 -0.0013 164 LEU   B N   
6582 C  CA  . LEU   B 164 ? 0.1375 0.1283 0.2867 -0.0100 -0.0273 0.0031  164 LEU   B CA  
6583 C  C   . LEU   B 164 ? 0.1471 0.1285 0.2997 -0.0141 -0.0340 0.0057  164 LEU   B C   
6584 O  O   . LEU   B 164 ? 0.1499 0.1466 0.3230 -0.0176 -0.0369 0.0043  164 LEU   B O   
6585 C  CB  . LEU   B 164 ? 0.1369 0.1259 0.2813 -0.0199 -0.0202 -0.0002 164 LEU   B CB  
6586 C  CG  . LEU   B 164 ? 0.1450 0.1385 0.2846 -0.0180 -0.0097 0.0040  164 LEU   B CG  
6587 C  CD1 . LEU   B 164 ? 0.1517 0.1397 0.2787 -0.0204 -0.0148 -0.0003 164 LEU   B CD1 
6588 C  CD2 . LEU   B 164 ? 0.1612 0.1745 0.2987 -0.0120 0.0049  -0.0039 164 LEU   B CD2 
6601 N  N   . VAL   B 165 ? 0.1789 0.1384 0.3140 -0.0259 -0.0441 -0.0029 165 VAL   B N   
6602 C  CA  . VAL   B 165 ? 0.2172 0.1531 0.3161 -0.0333 -0.0559 -0.0093 165 VAL   B CA  
6603 C  C   . VAL   B 165 ? 0.2428 0.1585 0.3416 -0.0437 -0.0870 -0.0083 165 VAL   B C   
6604 O  O   . VAL   B 165 ? 0.2646 0.1733 0.3493 -0.0482 -0.0940 -0.0050 165 VAL   B O   
6605 C  CB  . VAL   B 165 ? 0.2399 0.1700 0.3099 -0.0189 -0.0230 -0.0223 165 VAL   B CB  
6606 C  CG1 . VAL   B 165 ? 0.2560 0.1780 0.3291 -0.0221 -0.0082 -0.0150 165 VAL   B CG1 
6607 C  CG2 . VAL   B 165 ? 0.2360 0.1704 0.3021 -0.0122 -0.0121 -0.0202 165 VAL   B CG2 
6617 N  N   . SER   B 166 ? 0.2495 0.1442 0.3818 -0.0402 -0.0937 -0.0189 166 SER   B N   
6618 C  CA  . SER   B 166 ? 0.2468 0.1453 0.4316 -0.0396 -0.0768 -0.0282 166 SER   B CA  
6619 C  C   . SER   B 166 ? 0.2354 0.1596 0.4522 -0.0379 -0.0705 -0.0025 166 SER   B C   
6620 O  O   . SER   B 166 ? 0.2407 0.1824 0.4758 -0.0523 -0.0963 -0.0267 166 SER   B O   
6621 C  CB  . SER   B 166 ? 0.2454 0.1551 0.4589 -0.0332 -0.0694 -0.0365 166 SER   B CB  
6622 O  OG  . SER   B 166 ? 0.2352 0.1553 0.4764 -0.0231 -0.0756 -0.0226 166 SER   B OG  
6628 N  N   . SER   B 167 ? 0.2107 0.1501 0.4294 -0.0383 -0.0678 0.0311  167 SER   B N   
6629 C  CA  . SER   B 167 ? 0.2006 0.1621 0.4074 -0.0301 -0.0482 0.0322  167 SER   B CA  
6630 C  C   . SER   B 167 ? 0.1914 0.1700 0.3854 -0.0473 -0.0457 0.0460  167 SER   B C   
6631 O  O   . SER   B 167 ? 0.1902 0.1816 0.3782 -0.0555 -0.0556 0.0443  167 SER   B O   
6632 C  CB  . SER   B 167 ? 0.1868 0.1643 0.4105 -0.0245 -0.0285 0.0282  167 SER   B CB  
6633 O  OG  . SER   B 167 ? 0.1785 0.1754 0.4000 -0.0156 -0.0146 0.0284  167 SER   B OG  
6639 N  N   . PHE   B 168 ? 0.1952 0.1677 0.3645 -0.0430 -0.0305 0.0592  168 PHE   B N   
6640 C  CA  . PHE   B 168 ? 0.1935 0.1683 0.3286 -0.0495 -0.0354 0.0385  168 PHE   B CA  
6641 C  C   . PHE   B 168 ? 0.1632 0.1598 0.2906 -0.0330 -0.0224 0.0171  168 PHE   B C   
6642 O  O   . PHE   B 168 ? 0.1920 0.1513 0.2964 -0.0072 -0.0180 -0.0011 168 PHE   B O   
6643 C  CB  . PHE   B 168 ? 0.2140 0.1716 0.3326 -0.0601 -0.0558 0.0507  168 PHE   B CB  
6644 C  CG  . PHE   B 168 ? 0.2400 0.1588 0.3158 -0.0620 -0.0623 0.0272  168 PHE   B CG  
6645 C  CD1 . PHE   B 168 ? 0.2664 0.1667 0.3229 -0.0578 -0.0574 0.0201  168 PHE   B CD1 
6646 C  CD2 . PHE   B 168 ? 0.2334 0.1537 0.3115 -0.0517 -0.0591 0.0339  168 PHE   B CD2 
6647 C  CE1 . PHE   B 168 ? 0.2794 0.1758 0.3162 -0.0452 -0.0356 0.0297  168 PHE   B CE1 
6648 C  CE2 . PHE   B 168 ? 0.2591 0.1626 0.3157 -0.0396 -0.0583 0.0267  168 PHE   B CE2 
6649 C  CZ  . PHE   B 168 ? 0.2693 0.1651 0.3167 -0.0319 -0.0529 0.0322  168 PHE   B CZ  
6659 N  N   . LEU   B 169 ? 0.1719 0.1705 0.2845 -0.0118 -0.0096 0.0002  169 LEU   B N   
6660 C  CA  . LEU   B 169 ? 0.1983 0.1968 0.3094 -0.0110 0.0003  -0.0337 169 LEU   B CA  
6661 C  C   . LEU   B 169 ? 0.2344 0.2192 0.3681 0.0014  -0.0030 -0.0645 169 LEU   B C   
6662 O  O   . LEU   B 169 ? 0.2571 0.2380 0.4117 -0.0025 0.0014  -0.0832 169 LEU   B O   
6663 C  CB  . LEU   B 169 ? 0.2219 0.2417 0.3095 -0.0155 0.0051  -0.0072 169 LEU   B CB  
6664 C  CG  . LEU   B 169 ? 0.2646 0.2804 0.3372 -0.0043 0.0082  0.0000  169 LEU   B CG  
6665 C  CD1 . LEU   B 169 ? 0.2809 0.3002 0.3389 -0.0051 0.0083  0.0156  169 LEU   B CD1 
6666 C  CD2 . LEU   B 169 ? 0.2606 0.2866 0.3299 0.0101  0.0269  -0.0133 169 LEU   B CD2 
6667 O  OXT . LEU   B 169 ? 0.2535 0.2374 0.3789 0.0289  0.0071  -0.0620 169 LEU   B OXT 
6679 C  C1  T TFA   C .   ? 0.1193 0.1413 0.1366 -0.0050 0.0247  0.0202  201 TFA   A C1  
6680 C  C2  T TFA   C .   ? 0.1480 0.1738 0.1681 -0.0091 0.0156  -0.0039 201 TFA   A C2  
6681 O  O   T TFA   C .   ? 0.0986 0.1162 0.1293 -0.0041 0.0277  0.0323  201 TFA   A O   
6682 F  F1  T TFA   C .   ? 0.1599 0.1836 0.1931 -0.0033 0.0084  -0.0133 201 TFA   A F1  
6683 F  F2  T TFA   C .   ? 0.1439 0.1804 0.1517 -0.0253 0.0206  0.0068  201 TFA   A F2  
6684 F  F3  T TFA   C .   ? 0.1653 0.1884 0.1931 -0.0132 0.0320  -0.0118 201 TFA   A F3  
6685 O  OXT T TFA   C .   ? 0.1158 0.1386 0.1524 0.0128  0.0223  0.0184  201 TFA   A OXT 
6686 N  N2  B A1A7Z D .   ? 0.1770 0.2333 0.2570 -0.0441 -0.0273 -0.0041 202 A1A7Z A N2  
6687 C  C3  B A1A7Z D .   ? 0.1707 0.2359 0.2472 -0.0330 -0.0276 0.0050  202 A1A7Z A C3  
6688 C  C6  B A1A7Z D .   ? 0.1639 0.2255 0.2349 -0.0361 -0.0216 0.0188  202 A1A7Z A C6  
6689 C  C9  B A1A7Z D .   ? 0.1875 0.2706 0.2870 -0.0130 -0.0415 0.0082  202 A1A7Z A C9  
6690 C  C12 B A1A7Z D .   ? 0.2033 0.2891 0.2937 -0.0121 -0.0510 0.0152  202 A1A7Z A C12 
6691 C  C14 B A1A7Z D .   ? 0.1943 0.2795 0.2947 -0.0106 -0.0526 0.0069  202 A1A7Z A C14 
6692 C  C1  B A1A7Z D .   ? 0.1689 0.2553 0.2654 -0.0150 -0.0271 -0.0089 202 A1A7Z A C1  
6693 C  C10 B A1A7Z D .   ? 0.1948 0.2790 0.2853 -0.0102 -0.0467 0.0168  202 A1A7Z A C10 
6694 C  C11 B A1A7Z D .   ? 0.2008 0.2868 0.2878 -0.0117 -0.0481 0.0227  202 A1A7Z A C11 
6695 C  C13 B A1A7Z D .   ? 0.2015 0.2871 0.2994 -0.0108 -0.0547 0.0108  202 A1A7Z A C13 
6696 C  C2  B A1A7Z D .   ? 0.1721 0.2547 0.2686 -0.0180 -0.0316 -0.0035 202 A1A7Z A C2  
6697 C  C4  B A1A7Z D .   ? 0.1823 0.2313 0.2524 -0.0415 -0.0266 0.0047  202 A1A7Z A C4  
6698 C  C5  B A1A7Z D .   ? 0.1641 0.2170 0.2336 -0.0359 -0.0238 0.0203  202 A1A7Z A C5  
6699 C  C7  B A1A7Z D .   ? 0.1524 0.2208 0.2302 -0.0338 -0.0200 0.0243  202 A1A7Z A C7  
6700 C  C8  B A1A7Z D .   ? 0.1417 0.2127 0.2288 -0.0352 -0.0219 0.0316  202 A1A7Z A C8  
6701 N  N1  B A1A7Z D .   ? 0.1683 0.2437 0.2548 -0.0246 -0.0290 -0.0092 202 A1A7Z A N1  
6702 N  N3  B A1A7Z D .   ? 0.1776 0.2242 0.2460 -0.0413 -0.0281 0.0124  202 A1A7Z A N3  
6703 N  N4  B A1A7Z D .   ? 0.1448 0.2042 0.2224 -0.0315 -0.0242 0.0351  202 A1A7Z A N4  
6704 O  O1  B A1A7Z D .   ? 0.1582 0.2542 0.2518 -0.0090 -0.0244 -0.0099 202 A1A7Z A O1  
6719 CL CL  B CL    E .   ? 0.1748 0.1450 0.3279 -0.0144 0.0004  0.0081  203 CL    A CL  
6720 O  O   . HOH   F .   ? 0.4077 0.8259 0.5026 -0.1149 0.0618  0.1085  301 HOH   A O   
6721 O  O   . HOH   F .   ? 0.2163 0.2349 0.2538 -0.0334 0.0431  0.0567  302 HOH   A O   
6722 O  O   A HOH   F .   ? 0.2167 0.2196 0.3266 -0.0052 -0.0128 0.0311  303 HOH   A O   
6723 O  O   . HOH   F .   ? 0.4372 0.3472 0.4713 -0.0192 0.1474  -0.0321 304 HOH   A O   
6724 O  O   . HOH   F .   ? 0.7242 0.5583 0.4231 -0.1498 -0.0377 0.1924  305 HOH   A O   
6725 O  O   . HOH   F .   ? 0.5937 0.3760 0.5405 -0.0953 0.1647  0.1137  306 HOH   A O   
6726 O  O   . HOH   F .   ? 0.5894 0.4151 0.3287 0.1501  -0.1312 0.0597  307 HOH   A O   
6727 O  O   . HOH   F .   ? 0.5346 0.4784 0.4834 -0.0602 0.1592  0.2068  308 HOH   A O   
6728 O  O   . HOH   F .   ? 0.2949 0.6542 0.5705 -0.0738 -0.0941 0.2139  309 HOH   A O   
6729 O  O   . HOH   F .   ? 0.5593 0.6496 0.5069 -0.1286 -0.1127 -0.1050 310 HOH   A O   
6730 O  O   . HOH   F .   ? 0.2647 0.5722 0.3939 0.0364  -0.0674 0.0667  311 HOH   A O   
6731 O  O   . HOH   F .   ? 0.1503 0.4021 0.2405 0.0051  0.0257  0.0762  312 HOH   A O   
6732 O  O   . HOH   F .   ? 0.3649 0.3312 0.2901 -0.1454 0.0037  0.0724  313 HOH   A O   
6733 O  O   . HOH   F .   ? 0.2922 0.3632 0.1616 -0.0527 0.0383  0.0457  314 HOH   A O   
6734 O  O   . HOH   F .   ? 0.7063 0.5502 0.3674 -0.0628 -0.0473 0.1200  315 HOH   A O   
6735 O  O   . HOH   F .   ? 0.4792 0.4329 0.4159 -0.1980 -0.1210 0.2095  316 HOH   A O   
6736 O  O   . HOH   F .   ? 0.5572 0.3479 0.3499 -0.1258 -0.0888 0.0199  317 HOH   A O   
6737 O  O   . HOH   F .   ? 0.1892 0.4390 0.3311 0.0925  0.0086  0.0517  318 HOH   A O   
6738 O  O   . HOH   F .   ? 0.6024 0.5701 0.4106 0.2070  -0.0511 -0.0479 319 HOH   A O   
6739 O  O   . HOH   F .   ? 0.2120 0.1745 0.3591 -0.0447 0.0007  -0.0256 320 HOH   A O   
6740 O  O   . HOH   F .   ? 0.2397 0.5248 0.5550 0.0964  0.0417  0.0753  321 HOH   A O   
6741 O  O   . HOH   F .   ? 0.4874 0.2635 0.2938 -0.1335 0.0456  0.0242  322 HOH   A O   
6742 O  O   . HOH   F .   ? 0.7773 0.6520 0.5549 -0.0814 0.0758  0.0798  323 HOH   A O   
6743 O  O   . HOH   F .   ? 0.5052 0.4807 0.6562 0.1611  0.1509  -0.0906 324 HOH   A O   
6744 O  O   . HOH   F .   ? 0.4003 0.3693 0.3640 -0.0845 0.1810  0.0194  325 HOH   A O   
6745 O  O   . HOH   F .   ? 0.5430 0.3934 0.5964 0.0957  0.1470  -0.1567 326 HOH   A O   
6746 O  O   . HOH   F .   ? 0.1494 0.1428 0.2501 -0.0221 0.0099  0.0120  327 HOH   A O   
6747 O  O   . HOH   F .   ? 0.2243 0.3731 0.3775 0.0840  -0.0613 -0.0130 328 HOH   A O   
6748 O  O   . HOH   F .   ? 0.2062 0.1606 0.2445 -0.0084 -0.0514 -0.0099 329 HOH   A O   
6749 O  O   . HOH   F .   ? 0.3053 0.2516 0.4190 -0.0333 -0.1328 0.1104  330 HOH   A O   
6750 O  O   . HOH   F .   ? 0.5734 0.5507 0.4937 0.0467  0.2620  -0.0643 331 HOH   A O   
6751 O  O   . HOH   F .   ? 0.7740 0.3260 0.6302 -0.0395 -0.1315 0.1305  332 HOH   A O   
6752 O  O   . HOH   F .   ? 0.5788 0.5500 0.4347 0.0680  -0.0375 -0.1031 333 HOH   A O   
6753 O  O   . HOH   F .   ? 0.3016 0.2608 0.3717 -0.0673 -0.0089 -0.0187 334 HOH   A O   
6754 O  O   . HOH   F .   ? 0.2098 0.4034 0.3970 -0.0274 -0.0603 0.1625  335 HOH   A O   
6755 O  O   . HOH   F .   ? 0.2525 0.2011 0.2577 -0.0342 0.0067  -0.0164 336 HOH   A O   
6756 O  O   . HOH   F .   ? 0.2185 0.2206 0.3031 0.0203  0.0351  0.0462  337 HOH   A O   
6757 O  O   . HOH   F .   ? 0.5352 0.4147 0.6415 0.0818  -0.0801 -0.0424 338 HOH   A O   
6758 O  O   . HOH   F .   ? 0.2353 0.3171 0.4921 0.0001  0.1007  0.1824  339 HOH   A O   
6759 O  O   . HOH   F .   ? 0.4653 0.1941 0.4564 0.0483  -0.1316 0.0509  340 HOH   A O   
6760 O  O   . HOH   F .   ? 0.1708 0.1710 0.2157 0.0144  -0.0295 0.0223  341 HOH   A O   
6761 O  O   . HOH   F .   ? 0.3469 0.4500 0.2426 -0.0391 0.0564  0.0217  342 HOH   A O   
6762 O  O   . HOH   F .   ? 0.2854 0.3437 0.4059 -0.0841 -0.0735 -0.0366 343 HOH   A O   
6763 O  O   B HOH   F .   ? 0.3369 0.2793 0.2545 0.0608  0.0179  0.0273  344 HOH   A O   
6764 O  O   A HOH   F .   ? 0.1187 0.1821 0.1879 0.0331  0.0371  0.0386  345 HOH   A O   
6765 O  O   . HOH   F .   ? 0.2561 0.3219 0.3491 -0.0438 0.0912  -0.0474 346 HOH   A O   
6766 O  O   . HOH   F .   ? 0.3769 0.6144 0.4174 -0.0821 -0.0096 0.1513  347 HOH   A O   
6767 O  O   . HOH   F .   ? 0.1501 0.1676 0.2665 0.0112  -0.0331 -0.0536 348 HOH   A O   
6768 O  O   . HOH   F .   ? 0.4802 0.1993 0.5448 0.0565  0.0097  0.0084  349 HOH   A O   
6769 O  O   . HOH   F .   ? 0.2132 0.1711 0.2480 0.0269  -0.0351 -0.0034 350 HOH   A O   
6770 O  O   . HOH   F .   ? 0.5108 0.4984 0.2812 -0.1276 0.1298  0.0598  351 HOH   A O   
6771 O  O   . HOH   F .   ? 0.1903 0.3486 0.4153 -0.0258 0.0405  -0.0969 352 HOH   A O   
6772 O  O   . HOH   F .   ? 0.1448 0.2046 0.2187 -0.0004 -0.0096 0.0434  353 HOH   A O   
6773 O  O   . HOH   F .   ? 0.1895 0.2030 0.4101 0.0242  0.0886  -0.0079 354 HOH   A O   
6774 O  O   . HOH   F .   ? 0.3436 0.4031 0.3985 0.1759  0.0869  0.0427  355 HOH   A O   
6775 O  O   . HOH   F .   ? 0.2000 0.1573 0.1608 -0.0078 0.0158  0.0201  356 HOH   A O   
6776 O  O   . HOH   F .   ? 0.1247 0.1236 0.1442 -0.0003 0.0118  0.0050  357 HOH   A O   
6777 O  O   . HOH   F .   ? 0.3066 0.3249 0.4817 -0.0683 -0.1183 -0.0678 358 HOH   A O   
6778 O  O   . HOH   F .   ? 0.1853 0.2359 0.3620 0.0273  0.0808  -0.0393 359 HOH   A O   
6779 O  O   . HOH   F .   ? 0.1369 0.1903 0.2636 0.0021  -0.0103 0.0254  360 HOH   A O   
6780 O  O   . HOH   F .   ? 0.6118 0.3767 0.3516 0.0176  0.0206  0.1488  361 HOH   A O   
6781 O  O   A HOH   F .   ? 0.2754 0.1593 0.1832 0.0034  -0.0155 0.0001  362 HOH   A O   
6782 O  O   . HOH   F .   ? 0.1598 0.1517 0.2007 0.0015  -0.0353 0.0065  363 HOH   A O   
6783 O  O   . HOH   F .   ? 0.3783 0.2071 0.2719 0.1033  0.0450  0.0207  364 HOH   A O   
6784 O  O   . HOH   F .   ? 0.3102 0.3410 0.3354 -0.1436 0.0823  -0.0281 365 HOH   A O   
6785 O  O   . HOH   F .   ? 0.1502 0.1330 0.2505 -0.0158 0.0176  -0.0112 366 HOH   A O   
6786 O  O   . HOH   F .   ? 0.2580 0.3887 0.3367 -0.0457 0.0590  0.0282  367 HOH   A O   
6787 O  O   . HOH   F .   ? 0.2848 0.3581 0.2411 -0.0986 -0.0031 -0.0631 368 HOH   A O   
6788 O  O   . HOH   F .   ? 0.1281 0.1383 0.1906 -0.0040 -0.0155 0.0090  369 HOH   A O   
6789 O  O   . HOH   F .   ? 0.6996 0.5096 0.4748 -0.1153 -0.0112 0.1943  370 HOH   A O   
6790 O  O   . HOH   F .   ? 0.3586 0.7122 0.5103 -0.0545 -0.1591 0.0644  371 HOH   A O   
6791 O  O   . HOH   F .   ? 0.3946 0.2390 0.4682 -0.1164 0.0791  0.0445  372 HOH   A O   
6792 O  O   A HOH   F .   ? 0.1508 0.2066 0.2067 0.0029  0.0244  0.0224  373 HOH   A O   
6793 O  O   . HOH   F .   ? 0.1389 0.1520 0.1538 -0.0082 -0.0168 -0.0022 374 HOH   A O   
6794 O  O   . HOH   F .   ? 0.4270 0.2311 0.4121 -0.1333 0.1530  -0.0398 375 HOH   A O   
6795 O  O   . HOH   F .   ? 0.2659 0.4546 0.3122 0.0610  0.0793  0.1911  376 HOH   A O   
6796 O  O   . HOH   F .   ? 0.3610 0.4175 0.3646 -0.0111 -0.0523 0.1024  377 HOH   A O   
6797 O  O   . HOH   F .   ? 0.3451 0.5311 0.6050 0.0757  0.0027  0.1691  378 HOH   A O   
6798 O  O   . HOH   F .   ? 0.1712 0.1876 0.2622 -0.0287 0.0076  0.0374  379 HOH   A O   
6799 O  O   . HOH   F .   ? 0.1677 0.2397 0.3040 -0.0064 0.0576  0.0669  380 HOH   A O   
6800 O  O   . HOH   F .   ? 0.3284 0.2537 0.5078 -0.0840 -0.0074 -0.0008 381 HOH   A O   
6801 O  O   . HOH   F .   ? 0.2404 0.2616 0.3346 -0.0024 -0.0237 -0.0628 382 HOH   A O   
6802 O  O   . HOH   F .   ? 0.1677 0.2106 0.1890 -0.0176 0.0044  0.0614  383 HOH   A O   
6803 O  O   . HOH   F .   ? 0.1775 0.2880 0.2706 0.0405  0.0437  0.1040  384 HOH   A O   
6804 O  O   . HOH   F .   ? 0.1948 0.2296 0.2457 -0.0418 -0.0536 0.0559  385 HOH   A O   
6805 O  O   . HOH   F .   ? 0.2986 0.2899 0.2266 0.0270  0.0584  0.0055  386 HOH   A O   
6806 O  O   . HOH   F .   ? 0.2162 0.2277 0.2900 0.0111  -0.0075 0.0826  387 HOH   A O   
6807 O  O   T HOH   F .   ? 0.0985 0.0983 0.2442 -0.0184 0.0086  0.0572  388 HOH   A O   
6808 O  O   . HOH   F .   ? 0.2922 0.7042 0.3207 0.1339  0.0513  -0.0763 389 HOH   A O   
6809 O  O   . HOH   F .   ? 0.1951 0.1937 0.1770 -0.0029 0.0161  0.0139  390 HOH   A O   
6810 O  O   . HOH   F .   ? 0.1538 0.1615 0.1841 0.0162  -0.0324 -0.0271 391 HOH   A O   
6811 O  O   . HOH   F .   ? 0.2573 0.1936 0.1849 -0.0592 0.0073  0.0360  392 HOH   A O   
6812 O  O   . HOH   F .   ? 0.1682 0.1639 0.2495 -0.0242 0.0074  0.0423  393 HOH   A O   
6813 O  O   . HOH   F .   ? 0.1840 0.2153 0.2954 -0.0174 -0.0348 0.0813  394 HOH   A O   
6814 O  O   . HOH   F .   ? 0.3217 0.2550 0.3346 -0.0159 -0.0439 0.0988  395 HOH   A O   
6815 O  O   . HOH   F .   ? 0.2462 0.3981 0.3807 -0.0341 0.1060  -0.0712 396 HOH   A O   
6816 O  O   . HOH   F .   ? 0.5702 0.5532 0.7017 -0.1065 -0.0249 0.1613  397 HOH   A O   
6817 O  O   . HOH   F .   ? 0.2339 0.1729 0.2776 -0.0123 0.0184  0.0291  398 HOH   A O   
6818 O  O   . HOH   F .   ? 0.3766 0.3860 0.3651 0.1184  0.0550  -0.0340 399 HOH   A O   
6819 O  O   . HOH   F .   ? 0.3629 0.6284 0.5571 0.1702  0.0824  0.0042  400 HOH   A O   
6820 O  O   . HOH   F .   ? 0.1941 0.2080 0.3219 -0.0021 -0.0462 0.0357  401 HOH   A O   
6821 O  O   . HOH   F .   ? 0.6342 0.5540 0.4808 0.0603  0.1343  0.0193  402 HOH   A O   
6822 O  O   . HOH   F .   ? 0.2948 0.2540 0.2399 -0.0708 -0.0862 0.0356  403 HOH   A O   
6823 O  O   . HOH   F .   ? 0.1788 0.1847 0.3679 0.0316  0.0857  0.1025  404 HOH   A O   
6824 O  O   A HOH   F .   ? 0.3817 0.2618 0.2811 0.0593  0.1019  0.0471  405 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2186 0.1699 0.3184 0.0046  -0.0263 0.0190  406 HOH   A O   
6826 O  O   . HOH   F .   ? 0.1862 0.2442 0.4234 -0.0072 -0.0284 0.0176  407 HOH   A O   
6827 O  O   A HOH   F .   ? 0.1582 0.1803 0.2856 -0.0138 0.0254  -0.0025 408 HOH   A O   
6828 O  O   . HOH   F .   ? 0.1714 0.1325 0.1611 -0.0259 0.0130  -0.0032 409 HOH   A O   
6829 O  O   . HOH   F .   ? 0.4974 0.4573 0.2130 -0.0618 0.0843  0.0827  410 HOH   A O   
6830 O  O   . HOH   F .   ? 0.2712 0.3519 0.7377 -0.0274 0.1008  -0.0471 411 HOH   A O   
6831 O  O   . HOH   F .   ? 0.6069 0.2998 0.5423 0.1426  -0.0589 -0.0057 412 HOH   A O   
6832 O  O   . HOH   F .   ? 0.1510 0.1651 0.3190 -0.0029 -0.0049 0.0313  413 HOH   A O   
6833 O  O   . HOH   F .   ? 0.2359 0.2142 0.2616 -0.0531 0.0004  0.0664  414 HOH   A O   
6834 O  O   . HOH   F .   ? 0.1993 0.3003 0.2608 -0.0299 -0.0483 0.0630  415 HOH   A O   
6835 O  O   . HOH   F .   ? 0.3220 0.3487 0.2260 -0.0499 -0.0821 0.0431  416 HOH   A O   
6836 O  O   . HOH   F .   ? 0.2771 0.6079 0.1769 -0.0544 0.0476  0.0210  417 HOH   A O   
6837 O  O   . HOH   F .   ? 0.2987 0.3911 0.4271 -0.0589 0.1346  -0.0055 418 HOH   A O   
6838 O  O   . HOH   F .   ? 0.9242 0.9412 0.7226 -0.0036 -0.0195 -0.0725 419 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2072 0.1723 0.3329 0.0261  -0.0701 0.0148  420 HOH   A O   
6840 O  O   . HOH   F .   ? 0.4133 0.2216 0.5309 -0.0849 -0.2194 0.1100  421 HOH   A O   
6841 O  O   . HOH   F .   ? 0.4469 0.4801 0.3893 0.1830  -0.0921 -0.1736 422 HOH   A O   
6842 O  O   . HOH   F .   ? 0.2109 0.2330 0.3728 0.0062  -0.0339 -0.0508 423 HOH   A O   
6843 O  O   . HOH   F .   ? 0.3337 0.1202 0.2175 0.0094  -0.0598 0.0043  424 HOH   A O   
6844 O  O   . HOH   F .   ? 0.6700 0.3932 0.4504 0.1866  -0.0858 0.1397  425 HOH   A O   
6845 O  O   . HOH   F .   ? 0.2284 0.3872 0.2794 0.1463  0.0006  0.0323  426 HOH   A O   
6846 O  O   . HOH   F .   ? 0.3350 0.3448 0.2428 -0.0362 -0.0465 0.0200  427 HOH   A O   
6847 O  O   . HOH   F .   ? 0.4318 0.6259 0.3313 -0.0916 -0.0009 0.1510  428 HOH   A O   
6848 O  O   . HOH   F .   ? 0.1535 0.1935 0.2776 -0.0122 -0.0011 0.0381  429 HOH   A O   
6849 O  O   . HOH   F .   ? 0.6087 0.7083 0.6561 -0.1110 -0.1158 -0.0509 430 HOH   A O   
6850 O  O   . HOH   F .   ? 0.6502 0.7087 0.5267 -0.0589 0.0854  0.0049  431 HOH   A O   
6851 O  O   A HOH   F .   ? 0.4658 0.5287 0.3134 0.0549  -0.0802 0.1349  432 HOH   A O   
6852 O  O   . HOH   F .   ? 0.6650 0.6737 0.4291 0.1049  0.2792  -0.0634 433 HOH   A O   
6853 O  O   . HOH   F .   ? 0.2559 0.1583 0.2914 0.0051  0.0137  0.0093  434 HOH   A O   
6854 O  O   . HOH   F .   ? 0.3436 0.2750 0.2000 -0.0789 0.0116  0.0712  435 HOH   A O   
6855 O  O   . HOH   F .   ? 0.1775 0.1418 0.1698 -0.0034 -0.0219 -0.0034 436 HOH   A O   
6856 O  O   . HOH   F .   ? 0.5622 0.4712 0.3866 -0.0111 -0.1481 0.0182  437 HOH   A O   
6857 O  O   . HOH   F .   ? 0.3565 0.3117 0.3371 0.1793  -0.0754 -0.0639 438 HOH   A O   
6858 O  O   . HOH   F .   ? 0.3054 0.3397 0.5178 -0.0116 0.1079  -0.1422 439 HOH   A O   
6859 O  O   . HOH   F .   ? 0.7079 0.6427 0.6747 0.0561  -0.1335 -0.0427 440 HOH   A O   
6860 O  O   . HOH   F .   ? 0.1826 0.2061 0.4849 -0.0200 -0.0775 0.0505  441 HOH   A O   
6861 O  O   . HOH   F .   ? 0.5087 0.4329 0.4890 -0.1140 -0.1166 -0.1366 442 HOH   A O   
6862 O  O   . HOH   F .   ? 0.5635 0.6281 0.6813 -0.1374 0.0005  -0.1253 443 HOH   A O   
6863 O  O   . HOH   F .   ? 0.2153 0.2727 0.2811 0.0113  -0.0186 -0.0574 444 HOH   A O   
6864 O  O   A HOH   F .   ? 0.2115 0.1866 0.2014 -0.0101 -0.0056 -0.0113 445 HOH   A O   
6865 O  O   . HOH   F .   ? 0.2425 0.1979 0.2886 0.0072  0.0326  0.0287  446 HOH   A O   
6866 O  O   . HOH   F .   ? 0.6411 0.4575 0.5622 0.1023  0.0747  -0.1197 447 HOH   A O   
6867 O  O   A HOH   F .   ? 0.3279 0.1859 0.2603 -0.1012 0.0118  0.0639  448 HOH   A O   
6868 O  O   . HOH   F .   ? 0.6527 0.5647 0.7708 0.1109  -0.1317 0.1809  449 HOH   A O   
6869 O  O   . HOH   F .   ? 0.6192 0.5696 0.5051 -0.0722 0.0883  0.1240  450 HOH   A O   
6870 O  O   . HOH   F .   ? 0.4908 0.3905 0.4388 -0.0174 0.0938  0.0140  451 HOH   A O   
6871 O  O   . HOH   F .   ? 0.4471 0.5680 0.4570 0.0574  -0.0355 0.1235  452 HOH   A O   
6872 O  O   . HOH   F .   ? 0.3570 0.4281 0.4381 0.1782  -0.0296 0.1258  453 HOH   A O   
6873 O  O   . HOH   F .   ? 0.4158 0.3172 0.4198 0.0259  0.0010  0.0211  454 HOH   A O   
6874 O  O   . HOH   F .   ? 0.7357 0.8511 0.5008 -0.0001 -0.1232 -0.0648 455 HOH   A O   
6875 O  O   . HOH   F .   ? 0.2672 0.2649 0.3569 -0.0485 0.0230  -0.0779 456 HOH   A O   
6876 O  O   . HOH   F .   ? 0.3453 0.4956 0.5403 -0.1600 0.0877  -0.1492 457 HOH   A O   
6877 O  O   . HOH   F .   ? 0.2497 0.4315 0.5826 0.0659  0.0207  -0.1718 458 HOH   A O   
6878 O  O   . HOH   F .   ? 0.3797 0.5055 0.4766 0.0598  -0.0077 0.1133  459 HOH   A O   
6879 O  O   . HOH   F .   ? 0.2931 0.2721 0.6671 0.0535  -0.1719 -0.0596 460 HOH   A O   
6880 O  O   . HOH   F .   ? 0.2446 0.1732 0.2548 0.0090  -0.0870 -0.0178 461 HOH   A O   
6881 O  O   . HOH   F .   ? 0.2851 0.2619 0.3624 -0.0935 0.0550  -0.0429 462 HOH   A O   
6882 O  O   . HOH   F .   ? 0.3443 0.4579 0.4287 -0.0895 -0.0171 0.0006  463 HOH   A O   
6883 O  O   . HOH   F .   ? 0.3733 0.6730 0.3794 -0.0789 -0.0768 0.2321  464 HOH   A O   
6884 O  O   . HOH   F .   ? 0.6856 0.3540 0.6829 0.0091  -0.0557 0.2569  465 HOH   A O   
6885 O  O   . HOH   F .   ? 0.6742 0.5652 0.6732 0.1244  0.1742  0.1898  466 HOH   A O   
6886 O  O   . HOH   F .   ? 0.3228 0.2759 0.4048 0.0191  0.0922  -0.0052 467 HOH   A O   
6887 O  O   . HOH   F .   ? 0.5807 0.4571 0.5004 0.0228  0.1406  0.0190  468 HOH   A O   
6888 O  O   . HOH   F .   ? 0.5242 0.5548 0.4510 0.1010  -0.0359 -0.0741 469 HOH   A O   
6889 O  O   . HOH   F .   ? 0.4177 0.5125 0.3886 0.0447  -0.0597 -0.0859 470 HOH   A O   
6890 O  O   . HOH   F .   ? 0.4246 0.4319 0.2779 -0.0055 -0.0079 -0.0200 471 HOH   A O   
6891 O  O   . HOH   F .   ? 0.2446 0.2120 0.2669 0.0134  -0.0017 -0.0032 472 HOH   A O   
6892 O  O   . HOH   F .   ? 0.4077 0.5065 0.3153 -0.0520 -0.0431 -0.0281 473 HOH   A O   
6893 O  O   . HOH   F .   ? 0.4695 0.4194 0.5348 -0.1866 -0.0700 -0.0630 474 HOH   A O   
6894 O  O   . HOH   F .   ? 0.4966 0.5362 0.6148 -0.1859 -0.1344 -0.0047 475 HOH   A O   
6895 O  O   . HOH   F .   ? 0.6158 0.5618 0.7177 -0.1202 0.0451  -0.0691 476 HOH   A O   
6896 O  O   . HOH   F .   ? 0.7688 0.3775 0.3343 -0.0454 -0.1353 0.0365  477 HOH   A O   
6897 O  O   . HOH   F .   ? 0.5497 0.3862 0.4470 0.0144  -0.0286 -0.1030 478 HOH   A O   
6898 O  O   . HOH   F .   ? 0.4643 0.2823 0.3501 -0.0669 -0.1313 0.0634  479 HOH   A O   
6899 O  O   . HOH   F .   ? 0.5679 0.3873 0.3590 -0.0285 0.1192  -0.0148 480 HOH   A O   
6900 O  O   . HOH   F .   ? 0.3188 0.3933 0.4735 -0.0159 0.1438  0.0687  481 HOH   A O   
6901 O  O   . HOH   F .   ? 0.5595 0.5081 0.5871 0.0923  -0.1004 0.0803  482 HOH   A O   
6902 O  O   . HOH   F .   ? 0.5841 0.5560 0.6799 0.0814  0.2259  -0.1044 483 HOH   A O   
6903 O  O   . HOH   F .   ? 0.2558 0.2415 0.6847 -0.0130 -0.1285 0.0292  484 HOH   A O   
6904 O  O   . HOH   F .   ? 0.2616 0.5091 0.3590 0.0947  0.0964  0.2324  485 HOH   A O   
6905 O  O   . HOH   F .   ? 0.6376 0.6315 0.4121 -0.0861 0.1025  0.1242  486 HOH   A O   
6906 O  O   . HOH   F .   ? 0.6252 0.4994 0.5132 -0.1044 -0.1096 -0.0833 487 HOH   A O   
6907 O  O   B HOH   F .   ? 0.2510 0.3299 0.1911 0.0307  -0.0130 0.0210  488 HOH   A O   
6908 O  O   . HOH   F .   ? 0.4138 0.3404 0.4651 -0.0994 0.0100  0.0798  489 HOH   A O   
6909 O  O   . HOH   F .   ? 0.4857 0.3970 0.2710 -0.1151 0.1513  -0.0638 490 HOH   A O   
6910 O  O   . HOH   F .   ? 0.4754 0.3069 0.4734 -0.0188 0.2321  0.0364  491 HOH   A O   
6911 O  O   . HOH   F .   ? 0.2845 0.2229 0.5483 0.0212  0.0438  0.0971  492 HOH   A O   
6912 O  O   . HOH   F .   ? 0.6632 0.2524 0.4109 -0.0609 0.0761  0.0538  493 HOH   A O   
6913 O  O   . HOH   F .   ? 0.2704 0.4776 0.3725 -0.0430 -0.0210 -0.0982 494 HOH   A O   
6914 O  O   . HOH   F .   ? 0.2538 0.2816 0.4790 0.0035  0.1001  -0.0125 495 HOH   A O   
6915 O  O   . HOH   F .   ? 0.3641 0.8024 0.5994 -0.1100 -0.0338 0.2134  496 HOH   A O   
6916 O  O   . HOH   F .   ? 0.2723 0.4040 0.3323 0.0980  -0.0495 0.0733  497 HOH   A O   
6917 O  O   . HOH   F .   ? 0.4818 0.2764 0.4276 -0.1508 -0.0177 0.0344  498 HOH   A O   
6918 O  O   . HOH   F .   ? 0.2848 0.3952 0.4513 0.0541  -0.0630 -0.0303 499 HOH   A O   
6919 O  O   . HOH   F .   ? 0.7176 0.6810 0.5047 0.1760  -0.1440 0.0774  500 HOH   A O   
6920 O  O   . HOH   F .   ? 0.7184 0.4808 0.6099 0.0850  -0.0176 0.0337  501 HOH   A O   
6921 O  O   . HOH   F .   ? 0.5380 0.7076 0.5230 0.1149  -0.0741 0.0416  502 HOH   A O   
6922 O  O   B HOH   F .   ? 0.5131 0.2429 0.3543 0.0068  -0.1894 0.0775  503 HOH   A O   
6923 O  O   . HOH   F .   ? 0.3163 0.7943 0.3838 0.1186  0.0734  -0.0088 504 HOH   A O   
6924 O  O   B HOH   F .   ? 0.2903 0.2273 0.2996 0.0455  -0.0774 0.0091  505 HOH   A O   
6925 O  O   . HOH   F .   ? 0.2953 0.2465 0.4654 0.0018  0.0465  0.0694  506 HOH   A O   
6926 O  O   . HOH   F .   ? 0.5588 0.6520 0.5194 0.3351  0.0094  0.1266  507 HOH   A O   
6927 O  O   T HOH   F .   ? 0.0846 0.1154 0.2445 -0.0226 -0.0278 0.0648  508 HOH   A O   
6928 O  O   . HOH   F .   ? 0.5310 0.5569 0.3892 -0.0612 -0.0526 -0.1106 509 HOH   A O   
6929 O  O   . HOH   F .   ? 0.2536 0.7025 0.4558 0.0019  0.0476  -0.1031 510 HOH   A O   
6930 O  O   . HOH   F .   ? 0.4404 0.7133 0.5407 -0.0744 -0.0408 0.1059  511 HOH   A O   
6931 O  O   . HOH   F .   ? 0.5205 0.4725 0.4402 0.1454  -0.0351 0.1524  512 HOH   A O   
6932 O  O   . HOH   F .   ? 0.2718 0.4739 0.5805 -0.0391 -0.1005 0.2870  513 HOH   A O   
6933 O  O   . HOH   G .   ? 0.2178 0.2112 0.3087 0.0098  0.0666  0.0250  201 HOH   B O   
6934 O  O   . HOH   G .   ? 0.5124 0.3311 0.4054 -0.0363 0.0253  -0.1470 202 HOH   B O   
6935 O  O   . HOH   G .   ? 0.3794 0.3790 0.6020 -0.0996 0.0413  -0.0421 203 HOH   B O   
6936 O  O   . HOH   G .   ? 0.7124 0.2960 0.4347 0.1264  0.0968  0.0224  204 HOH   B O   
6937 O  O   . HOH   G .   ? 0.4421 0.4674 0.2824 -0.0056 -0.0420 -0.1462 205 HOH   B O   
6938 O  O   . HOH   G .   ? 0.4861 0.5912 0.4492 0.2961  -0.1250 -0.0497 206 HOH   B O   
6939 O  O   . HOH   G .   ? 0.2906 0.7195 0.3769 0.0657  0.0270  0.2479  207 HOH   B O   
6940 O  O   . HOH   G .   ? 0.3451 0.5094 0.5361 0.2289  0.0585  -0.0515 208 HOH   B O   
6941 O  O   . HOH   G .   ? 0.1933 0.2164 0.3166 -0.0058 0.0221  -0.0268 209 HOH   B O   
6942 O  O   . HOH   G .   ? 0.1697 0.1843 0.2920 -0.0114 -0.0064 0.0049  210 HOH   B O   
6943 O  O   . HOH   G .   ? 0.2809 0.1868 0.5660 0.0102  0.1822  0.0637  211 HOH   B O   
6944 O  O   . HOH   G .   ? 0.4557 0.4007 0.6030 0.0444  -0.0810 0.2599  212 HOH   B O   
6945 O  O   . HOH   G .   ? 0.2599 0.2641 0.6604 0.0490  -0.1074 0.0640  213 HOH   B O   
6946 O  O   . HOH   G .   ? 0.3229 0.5339 0.5458 -0.0059 0.1918  -0.1716 214 HOH   B O   
6947 O  O   . HOH   G .   ? 0.6255 0.5348 0.6066 0.1441  0.0265  0.0062  215 HOH   B O   
6948 O  O   . HOH   G .   ? 0.4710 0.4662 0.3937 0.0505  0.1148  -0.1526 216 HOH   B O   
6949 O  O   . HOH   G .   ? 0.3885 0.3936 0.5560 -0.0908 0.0066  -0.1500 217 HOH   B O   
6950 O  O   . HOH   G .   ? 0.5002 0.3578 0.3617 0.0025  -0.1287 0.0489  218 HOH   B O   
6951 O  O   . HOH   G .   ? 0.4322 0.4661 0.6680 0.0514  -0.1562 -0.1052 219 HOH   B O   
6952 O  O   . HOH   G .   ? 0.4027 0.5875 0.3712 0.1118  0.0252  -0.0228 220 HOH   B O   
6953 O  O   . HOH   G .   ? 0.2914 0.3410 0.4858 0.0321  -0.0476 0.0185  221 HOH   B O   
6954 O  O   . HOH   G .   ? 0.4066 0.5571 0.3736 0.2441  -0.0476 -0.0050 222 HOH   B O   
6955 O  O   . HOH   G .   ? 0.3184 0.2349 0.5239 -0.0066 0.1877  0.0321  223 HOH   B O   
6956 O  O   . HOH   G .   ? 0.3143 0.3319 0.5941 -0.0236 0.0919  -0.0280 224 HOH   B O   
6957 O  O   . HOH   G .   ? 0.5624 0.2915 0.4255 -0.1668 -0.0198 0.0396  225 HOH   B O   
6958 O  O   . HOH   G .   ? 0.1699 0.2013 0.3431 -0.0142 0.0177  0.0040  226 HOH   B O   
6959 O  O   . HOH   G .   ? 0.4906 0.2083 0.3307 -0.0154 -0.0994 0.0114  227 HOH   B O   
6960 O  O   . HOH   G .   ? 0.2165 0.2221 0.4116 -0.0397 0.0008  -0.0530 228 HOH   B O   
6961 O  O   . HOH   G .   ? 0.5811 0.3838 0.2781 -0.0626 0.0412  0.0223  229 HOH   B O   
6962 O  O   . HOH   G .   ? 0.2405 0.1795 0.2860 -0.0322 0.1002  -0.0043 230 HOH   B O   
6963 O  O   . HOH   G .   ? 0.3608 0.1627 0.2062 0.0077  -0.0738 -0.0050 231 HOH   B O   
6964 O  O   . HOH   G .   ? 0.3797 0.4377 0.5577 -0.1686 -0.0238 0.1203  232 HOH   B O   
6965 O  O   . HOH   G .   ? 0.3634 0.2998 0.2339 0.0430  0.0653  0.0509  233 HOH   B O   
6966 O  O   . HOH   G .   ? 0.2118 0.2325 0.3439 -0.0504 0.0040  -0.0330 234 HOH   B O   
6967 O  O   . HOH   G .   ? 0.2618 0.3738 0.3149 -0.0772 0.0276  -0.0147 235 HOH   B O   
6968 O  O   . HOH   G .   ? 0.1404 0.1378 0.1699 -0.0138 -0.0033 0.0004  236 HOH   B O   
6969 O  O   . HOH   G .   ? 0.3491 0.2604 0.4427 0.0443  -0.1035 -0.1384 237 HOH   B O   
6970 O  O   . HOH   G .   ? 0.5156 0.3042 0.3865 -0.2213 -0.0228 0.0185  238 HOH   B O   
6971 O  O   . HOH   G .   ? 0.1574 0.1410 0.2830 -0.0046 0.0007  -0.0044 239 HOH   B O   
6972 O  O   . HOH   G .   ? 0.2804 0.4245 0.3151 -0.0963 -0.0342 -0.0583 240 HOH   B O   
6973 O  O   . HOH   G .   ? 0.2024 0.3829 0.2497 -0.0443 -0.0239 0.0442  241 HOH   B O   
6974 O  O   . HOH   G .   ? 0.2752 0.2461 0.3124 0.0478  0.0212  -0.0785 242 HOH   B O   
6975 O  O   . HOH   G .   ? 0.6904 0.4773 0.4711 0.1943  -0.0253 -0.1030 243 HOH   B O   
6976 O  O   . HOH   G .   ? 0.2017 0.1227 0.3408 0.0073  -0.0555 -0.0097 244 HOH   B O   
6977 O  O   . HOH   G .   ? 0.2101 0.1876 0.2177 -0.0317 -0.0409 0.0230  245 HOH   B O   
6978 O  O   . HOH   G .   ? 0.3760 0.2667 0.4275 0.0832  -0.0342 -0.0611 246 HOH   B O   
6979 O  O   . HOH   G .   ? 0.4488 0.3722 0.3515 -0.1091 0.0722  -0.1285 247 HOH   B O   
6980 O  O   . HOH   G .   ? 0.2258 0.3819 0.3322 -0.0327 -0.0680 -0.0472 248 HOH   B O   
6981 O  O   . HOH   G .   ? 0.2721 0.2099 0.2058 0.0122  -0.0148 -0.0025 249 HOH   B O   
6982 O  O   . HOH   G .   ? 0.3093 0.1655 0.6157 -0.0104 -0.1200 -0.0048 250 HOH   B O   
6983 O  O   . HOH   G .   ? 0.1438 0.1218 0.1766 -0.0028 -0.0130 0.0095  251 HOH   B O   
6984 O  O   . HOH   G .   ? 0.2699 0.2168 0.3075 0.0734  0.0686  -0.0017 252 HOH   B O   
6985 O  O   . HOH   G .   ? 0.3132 0.4092 0.2343 0.0065  0.0667  0.0325  253 HOH   B O   
6986 O  O   . HOH   G .   ? 0.7159 0.6317 0.3516 0.0436  0.0101  0.0722  254 HOH   B O   
6987 O  O   . HOH   G .   ? 0.2442 0.4987 0.5951 0.1532  -0.0530 -0.0904 255 HOH   B O   
6988 O  O   . HOH   G .   ? 0.2302 0.1938 0.2876 0.0719  -0.0815 -0.0619 256 HOH   B O   
6989 O  O   . HOH   G .   ? 0.2092 0.1471 0.2265 -0.0347 -0.0428 0.0297  257 HOH   B O   
6990 O  O   . HOH   G .   ? 0.3223 0.2600 0.3214 -0.0389 0.0303  -0.0544 258 HOH   B O   
6991 O  O   . HOH   G .   ? 0.1319 0.1711 0.2292 -0.0078 0.0091  0.0114  259 HOH   B O   
6992 O  O   . HOH   G .   ? 0.2326 0.3106 0.2300 -0.0565 0.0347  0.0502  260 HOH   B O   
6993 O  O   . HOH   G .   ? 0.3306 0.5366 0.3322 -0.0427 -0.1165 0.1115  261 HOH   B O   
6994 O  O   . HOH   G .   ? 0.2534 0.3948 0.3941 0.0388  0.1393  0.0392  262 HOH   B O   
6995 O  O   . HOH   G .   ? 0.4244 0.2347 0.4770 -0.0220 -0.1108 -0.0203 263 HOH   B O   
6996 O  O   . HOH   G .   ? 0.1582 0.1605 0.3259 -0.0229 -0.0181 0.0157  264 HOH   B O   
6997 O  O   . HOH   G .   ? 0.2408 0.4384 0.6259 -0.0009 0.0567  -0.1116 265 HOH   B O   
6998 O  O   . HOH   G .   ? 0.2317 0.2134 0.2363 0.0037  -0.0068 -0.0095 266 HOH   B O   
6999 O  O   . HOH   G .   ? 0.2327 0.3511 0.2364 0.1118  -0.0317 -0.0396 267 HOH   B O   
7000 O  O   . HOH   G .   ? 0.2769 0.2090 0.5313 0.0159  0.0670  0.0471  268 HOH   B O   
7001 O  O   . HOH   G .   ? 0.4222 0.4005 0.3003 0.0450  -0.0149 -0.0915 269 HOH   B O   
7002 O  O   . HOH   G .   ? 0.2569 0.1893 0.2864 -0.0573 0.0156  -0.0151 270 HOH   B O   
7003 O  O   . HOH   G .   ? 0.1885 0.1831 0.1663 -0.0478 -0.0491 0.0168  271 HOH   B O   
7004 O  O   . HOH   G .   ? 0.2331 0.2881 0.2556 -0.0398 -0.0770 0.0193  272 HOH   B O   
7005 O  O   . HOH   G .   ? 0.2109 0.4557 0.5012 -0.0433 -0.0278 -0.1335 273 HOH   B O   
7006 O  O   . HOH   G .   ? 0.2109 0.1935 0.3422 -0.0047 -0.0550 -0.0208 274 HOH   B O   
7007 O  O   . HOH   G .   ? 0.3980 0.3790 0.4396 0.1440  -0.1023 -0.1433 275 HOH   B O   
7008 O  O   . HOH   G .   ? 0.1955 0.1421 0.2447 -0.0230 -0.0059 0.0139  276 HOH   B O   
7009 O  O   . HOH   G .   ? 0.5413 0.6767 0.2541 0.0409  -0.0361 0.1185  277 HOH   B O   
7010 O  O   . HOH   G .   ? 0.2226 0.2434 0.2395 -0.0346 -0.0598 -0.0393 278 HOH   B O   
7011 O  O   . HOH   G .   ? 0.1750 0.1379 0.3707 -0.0138 -0.0293 -0.0020 279 HOH   B O   
7012 O  O   . HOH   G .   ? 0.2296 0.3496 0.3577 -0.0551 0.0590  -0.1301 280 HOH   B O   
7013 O  O   . HOH   G .   ? 0.1613 0.1538 0.3686 -0.0172 0.0030  -0.0051 281 HOH   B O   
7014 O  O   . HOH   G .   ? 0.2829 0.3395 0.5564 -0.0031 -0.0107 -0.0374 282 HOH   B O   
7015 O  O   . HOH   G .   ? 0.2746 0.7515 0.7421 0.1590  -0.0783 -0.0769 283 HOH   B O   
7016 O  O   . HOH   G .   ? 0.5578 0.3808 0.3287 0.2528  0.1327  0.1077  284 HOH   B O   
7017 O  O   . HOH   G .   ? 0.2587 0.7550 0.2433 0.0894  -0.0413 -0.0546 285 HOH   B O   
7018 O  O   . HOH   G .   ? 0.2946 0.4659 0.4637 -0.0985 -0.1086 0.0608  286 HOH   B O   
7019 O  O   . HOH   G .   ? 0.1615 0.1493 0.2009 0.0030  0.0069  0.0009  287 HOH   B O   
7020 O  O   . HOH   G .   ? 0.3225 0.2801 0.3110 -0.0295 0.0086  -0.1308 288 HOH   B O   
7021 O  O   . HOH   G .   ? 0.3296 0.2596 0.2273 -0.0098 -0.0795 0.0089  289 HOH   B O   
7022 O  O   . HOH   G .   ? 0.3813 0.2167 0.4032 -0.1036 -0.1995 0.0903  290 HOH   B O   
7023 O  O   . HOH   G .   ? 0.2590 0.2624 0.2826 0.0149  -0.0836 0.0166  291 HOH   B O   
7024 O  O   . HOH   G .   ? 0.3489 0.7009 0.4081 0.1412  -0.0256 0.1291  292 HOH   B O   
7025 O  O   . HOH   G .   ? 0.1652 0.2125 0.3020 0.0173  -0.0026 0.0187  293 HOH   B O   
7026 O  O   . HOH   G .   ? 0.1680 0.3733 0.4997 0.0436  -0.0079 -0.1393 294 HOH   B O   
7027 O  O   . HOH   G .   ? 0.1914 0.1507 0.2578 0.0085  0.0029  0.0217  295 HOH   B O   
7028 O  O   . HOH   G .   ? 0.4793 0.4813 0.2643 0.0106  0.1044  0.0985  296 HOH   B O   
7029 O  O   . HOH   G .   ? 0.1604 0.1959 0.1640 -0.0102 -0.0149 0.0112  297 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4686 0.4944 0.5205 0.0372  -0.1669 0.0270  298 HOH   B O   
7031 O  O   . HOH   G .   ? 0.5210 0.3678 0.2438 0.1593  -0.0980 0.0302  299 HOH   B O   
7032 O  O   . HOH   G .   ? 0.3307 0.1929 0.3567 0.0725  0.1163  0.0445  300 HOH   B O   
7033 O  O   . HOH   G .   ? 0.2808 0.3007 0.3791 -0.0489 0.1167  -0.1056 301 HOH   B O   
7034 O  O   . HOH   G .   ? 0.3071 0.3028 0.5089 -0.0419 -0.0995 0.1228  302 HOH   B O   
7035 O  O   . HOH   G .   ? 0.2182 0.1581 0.2680 -0.0334 -0.0227 -0.0060 303 HOH   B O   
7036 O  O   . HOH   G .   ? 0.2062 0.2877 0.6036 0.0499  -0.0428 -0.0931 304 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2153 0.3280 0.4846 -0.0212 -0.0360 -0.0146 305 HOH   B O   
7038 O  O   . HOH   G .   ? 0.2148 0.2271 0.5586 -0.0457 -0.0038 0.1340  306 HOH   B O   
7039 O  O   . HOH   G .   ? 0.4932 0.2935 0.2366 -0.1886 0.0703  -0.0292 307 HOH   B O   
7040 O  O   . HOH   G .   ? 0.2061 0.1483 0.3694 0.0336  -0.0977 0.0031  308 HOH   B O   
7041 O  O   . HOH   G .   ? 0.3485 0.3382 0.4171 -0.1416 0.1375  -0.0309 309 HOH   B O   
7042 O  O   . HOH   G .   ? 0.2510 0.1408 0.2664 -0.0171 -0.0250 0.0378  310 HOH   B O   
7043 O  O   . HOH   G .   ? 0.4623 0.3819 0.5282 0.0538  0.0032  0.0762  311 HOH   B O   
7044 O  O   . HOH   G .   ? 0.1484 0.1463 0.3366 0.0024  -0.0078 -0.0056 312 HOH   B O   
7045 O  O   . HOH   G .   ? 0.4574 0.3526 0.4361 -0.0970 0.0041  0.1258  313 HOH   B O   
7046 O  O   . HOH   G .   ? 0.4275 0.3903 0.6905 -0.0320 -0.1126 0.2013  314 HOH   B O   
7047 O  O   . HOH   G .   ? 0.6147 0.6548 0.4980 0.3239  -0.0218 -0.0344 315 HOH   B O   
7048 O  O   . HOH   G .   ? 0.4038 0.2339 0.2643 0.1553  0.1085  0.0355  316 HOH   B O   
7049 O  O   . HOH   G .   ? 0.5002 0.4274 0.2841 0.0021  -0.0518 -0.0669 317 HOH   B O   
7050 O  O   . HOH   G .   ? 0.1539 0.1767 0.3191 -0.0217 -0.0159 0.0130  318 HOH   B O   
7051 O  O   . HOH   G .   ? 0.2165 0.1907 0.2042 -0.0139 0.0178  0.0250  319 HOH   B O   
7052 O  O   . HOH   G .   ? 0.4337 0.3184 0.5255 0.1002  0.2047  0.1796  320 HOH   B O   
7053 O  O   . HOH   G .   ? 0.1629 0.2759 0.2592 -0.0078 -0.0148 0.0739  321 HOH   B O   
7054 O  O   . HOH   G .   ? 0.1519 0.1619 0.3240 -0.0136 -0.0186 -0.0145 322 HOH   B O   
7055 O  O   . HOH   G .   ? 0.7049 0.4390 0.5248 0.1501  0.1328  -0.0121 323 HOH   B O   
7056 O  O   . HOH   G .   ? 0.4081 0.4433 0.2370 0.1007  -0.0564 -0.0052 324 HOH   B O   
7057 O  O   . HOH   G .   ? 0.2042 0.5444 0.5125 -0.0318 -0.0141 0.0507  325 HOH   B O   
7058 O  O   . HOH   G .   ? 0.1762 0.1825 0.2989 0.0167  0.0417  0.0106  326 HOH   B O   
7059 O  O   . HOH   G .   ? 0.6390 0.4922 0.6516 0.1729  -0.0729 0.1873  327 HOH   B O   
7060 O  O   . HOH   G .   ? 0.3154 0.2112 0.2444 0.0323  -0.0178 0.0216  328 HOH   B O   
7061 O  O   . HOH   G .   ? 0.1685 0.2843 0.3371 0.0263  -0.0163 -0.0649 329 HOH   B O   
7062 O  O   . HOH   G .   ? 0.4395 0.2603 0.3011 0.0338  0.0318  0.0842  330 HOH   B O   
7063 O  O   . HOH   G .   ? 0.2886 0.3222 0.5362 -0.0756 -0.1638 0.1815  331 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2713 0.1880 0.5083 -0.0093 -0.0028 0.0596  332 HOH   B O   
7065 O  O   . HOH   G .   ? 0.8118 0.2142 0.3275 0.0332  -0.0799 0.0003  333 HOH   B O   
7066 O  O   . HOH   G .   ? 0.5506 0.3554 0.3614 0.0331  0.1036  0.1537  334 HOH   B O   
7067 O  O   . HOH   G .   ? 0.1690 0.1390 0.2539 0.0080  -0.0222 0.0068  335 HOH   B O   
7068 O  O   . HOH   G .   ? 0.5296 0.3672 0.4346 0.0313  0.0662  -0.1401 336 HOH   B O   
7069 O  O   . HOH   G .   ? 0.5791 0.5666 0.5942 -0.1101 -0.0586 0.1726  337 HOH   B O   
7070 O  O   . HOH   G .   ? 0.5809 0.4143 0.6247 -0.0658 -0.0819 -0.1259 338 HOH   B O   
7071 O  O   . HOH   G .   ? 0.4208 0.6710 0.4230 -0.0235 -0.0548 0.2052  339 HOH   B O   
7072 O  O   . HOH   G .   ? 0.7358 0.5896 0.3212 0.0187  -0.0795 0.1094  340 HOH   B O   
7073 O  O   . HOH   G .   ? 0.4809 0.3482 0.3196 0.0618  -0.1157 -0.0886 341 HOH   B O   
7074 O  O   . HOH   G .   ? 0.2466 0.6095 0.6484 0.0065  -0.1267 -0.0790 342 HOH   B O   
7075 O  O   . HOH   G .   ? 0.4733 0.5112 0.3633 -0.0024 -0.0957 0.0114  343 HOH   B O   
7076 O  O   . HOH   G .   ? 0.3707 0.5794 0.3978 -0.1239 -0.0819 -0.0169 344 HOH   B O   
7077 O  O   . HOH   G .   ? 0.2095 0.2022 0.3465 -0.0033 0.0709  -0.0139 345 HOH   B O   
7078 O  O   . HOH   G .   ? 0.2924 0.1800 0.4139 0.0351  -0.1239 -0.0542 346 HOH   B O   
7079 O  O   . HOH   G .   ? 0.4244 0.5118 0.5659 0.0200  -0.0890 0.0714  347 HOH   B O   
7080 O  O   . HOH   G .   ? 0.2507 0.6258 0.3461 0.1657  -0.0660 -0.1365 348 HOH   B O   
7081 O  O   . HOH   G .   ? 0.2791 0.2298 0.5144 -0.0266 -0.0994 -0.0609 349 HOH   B O   
7082 O  O   . HOH   G .   ? 0.4641 0.5336 0.4911 -0.1120 -0.0110 0.1121  350 HOH   B O   
7083 O  O   . HOH   G .   ? 0.4149 0.5562 0.6514 -0.0139 0.0238  -0.0498 351 HOH   B O   
7084 O  O   . HOH   G .   ? 0.2196 0.4229 0.4947 0.0157  0.0579  0.0272  352 HOH   B O   
7085 O  O   . HOH   G .   ? 0.3391 0.4893 0.5114 -0.1752 -0.0065 -0.0733 353 HOH   B O   
7086 O  O   . HOH   G .   ? 0.3593 0.2127 0.3433 -0.0692 0.0423  -0.0743 354 HOH   B O   
7087 O  O   . HOH   G .   ? 0.4419 0.3175 0.4742 -0.1131 0.0948  0.0428  355 HOH   B O   
7088 O  O   . HOH   G .   ? 0.3631 0.2668 0.3630 -0.0951 0.0038  -0.0568 356 HOH   B O   
7089 O  O   . HOH   G .   ? 0.5144 0.3887 0.4112 0.0426  0.1187  -0.0779 357 HOH   B O   
7090 O  O   . HOH   G .   ? 0.4741 0.4948 0.5150 0.1675  -0.1298 0.1416  358 HOH   B O   
7091 O  O   . HOH   G .   ? 0.5206 0.3464 0.5055 -0.0065 -0.1522 -0.0418 359 HOH   B O   
7092 O  O   . HOH   G .   ? 0.4764 0.3942 0.6467 0.0482  0.1023  0.1321  360 HOH   B O   
7093 O  O   . HOH   G .   ? 0.4116 0.5899 0.3168 0.2021  0.0072  0.0322  361 HOH   B O   
7094 O  O   . HOH   G .   ? 0.2201 0.3706 0.6662 -0.0750 -0.0629 -0.0807 362 HOH   B O   
7095 O  O   . HOH   G .   ? 0.5116 0.4999 0.5698 -0.0017 0.0144  0.0061  363 HOH   B O   
7096 O  O   . HOH   G .   ? 0.5150 0.3184 0.5063 -0.1458 -0.0111 0.0174  364 HOH   B O   
7097 O  O   . HOH   G .   ? 0.6366 0.2135 0.3809 -0.0159 0.0181  0.0602  365 HOH   B O   
7098 O  O   . HOH   G .   ? 0.5597 0.6038 0.3448 0.2248  -0.1287 0.0557  366 HOH   B O   
7099 O  O   . HOH   G .   ? 0.6195 0.4479 0.4140 0.1085  0.0734  0.0764  367 HOH   B O   
7100 O  O   . HOH   G .   ? 0.5083 0.5793 0.4505 -0.0925 -0.0485 -0.1121 368 HOH   B O   
7101 O  O   . HOH   G .   ? 0.4094 0.3681 0.5043 0.1186  -0.1438 -0.0123 369 HOH   B O   
7102 O  O   . HOH   G .   ? 0.4164 0.5754 0.5148 0.2567  0.1208  0.1728  370 HOH   B O   
7103 O  O   . HOH   G .   ? 0.6392 0.3379 0.3055 -0.1172 -0.1090 -0.0442 371 HOH   B O   
7104 O  O   . HOH   G .   ? 0.4166 0.5001 0.4684 -0.0368 -0.0494 0.0084  372 HOH   B O   
7105 O  O   . HOH   G .   ? 0.4110 0.3290 0.4210 0.1006  -0.1204 -0.0681 373 HOH   B O   
7106 O  O   . HOH   G .   ? 0.7450 0.7053 0.4815 0.2729  -0.1432 0.0313  374 HOH   B O   
7107 O  O   . HOH   G .   ? 0.2422 0.4493 0.4085 0.0293  -0.0454 -0.0765 375 HOH   B O   
7108 O  O   . HOH   G .   ? 0.4754 0.6929 0.5940 0.1493  0.0503  0.2772  376 HOH   B O   
7109 O  O   . HOH   G .   ? 0.2933 0.5375 0.2414 0.0175  0.0190  0.0231  377 HOH   B O   
7110 O  O   . HOH   G .   ? 0.5380 0.7302 0.4255 -0.1396 0.0232  -0.1444 378 HOH   B O   
7111 O  O   . HOH   G .   ? 0.3682 0.4346 0.4897 0.1245  0.0118  0.0092  379 HOH   B O   
7112 O  O   . HOH   G .   ? 0.6924 0.3804 0.4999 -0.0708 -0.1048 0.0350  380 HOH   B O   
7113 O  O   . HOH   G .   ? 0.5687 0.6901 0.6387 -0.0302 0.1663  0.1727  381 HOH   B O   
7114 O  O   . HOH   G .   ? 0.3101 0.2425 0.3311 0.0111  0.0333  0.0362  382 HOH   B O   
7115 O  O   . HOH   G .   ? 0.4582 0.7866 0.5216 0.0200  0.1932  0.0130  383 HOH   B O   
7116 O  O   . HOH   G .   ? 0.5748 0.5099 0.4632 0.0234  -0.0575 -0.0468 384 HOH   B O   
7117 O  O   . HOH   G .   ? 0.6882 0.3556 0.3967 0.0479  0.1340  -0.0490 385 HOH   B O   
7118 O  O   . HOH   G .   ? 0.6052 0.4010 0.4967 -0.0637 0.0683  -0.0111 386 HOH   B O   
7119 O  O   . HOH   G .   ? 0.4827 0.3853 0.3736 0.0076  0.0515  -0.0264 387 HOH   B O   
7120 O  O   . HOH   G .   ? 0.7265 0.5922 0.4530 0.2737  0.0043  -0.0439 388 HOH   B O   
7121 O  O   . HOH   G .   ? 0.2441 0.4350 0.4080 -0.0848 -0.0900 -0.0390 389 HOH   B O   
7122 O  O   . HOH   G .   ? 0.3601 0.2216 0.3580 0.0547  -0.0465 0.0231  390 HOH   B O   
7123 O  O   . HOH   G .   ? 0.4642 0.4373 0.4408 0.0368  0.0622  0.0571  391 HOH   B O   
7124 O  O   . HOH   G .   ? 0.2549 0.3948 0.6643 -0.1262 -0.0797 -0.0061 392 HOH   B O   
7125 O  O   . HOH   G .   ? 0.3750 0.2176 0.5177 -0.0277 0.0549  0.0437  393 HOH   B O   
7126 O  O   . HOH   G .   ? 0.3246 0.3641 0.4036 0.0330  0.0173  -0.0701 394 HOH   B O   
7127 O  O   . HOH   G .   ? 0.4524 0.6225 0.4248 0.1643  0.0440  -0.0903 395 HOH   B O   
7128 O  O   . HOH   G .   ? 0.4140 0.4583 0.4818 0.0036  0.1080  0.1249  396 HOH   B O   
7129 O  O   . HOH   G .   ? 0.2118 0.2768 0.5987 -0.0615 -0.0979 0.0258  397 HOH   B O   
7130 O  O   . HOH   G .   ? 0.5614 0.6716 0.6556 0.1060  -0.1328 0.1944  398 HOH   B O   
7131 O  O   . HOH   G .   ? 0.5453 0.4216 0.3211 -0.2442 -0.0697 0.1201  399 HOH   B O   
7132 O  O   . HOH   G .   ? 0.5491 0.5714 0.3638 0.1835  -0.0169 -0.0472 400 HOH   B O   
# 
