data_7HED
# 
_entry.id   7HED 
# 
_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   7HED         pdb_00007hed 10.2210/pdb7hed/pdb 
WWPDB D_1001407367 ?            ?                   
# 
_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                        7HED 
_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 '{1-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl}methanol' 218.255   2   ?                      ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                   35.453    1   ?                      ? ? ? 
5 water       nat water                                                            18.015    417 ?                      ? ? ? 
# 
_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 '{1-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl}methanol' A1A9T 
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 
A1A9T non-polymer         . '{1-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl}methanol' ? 'C11 H14 N4 O'   218.255 
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 A1A9T 1   202 201  A1A9T LA1 A . 
E 3 A1A9T 1   203 301  A1A9T LA2 A . 
F 4 CL    1   204 1    CL    CL  A . 
G 5 HOH   1   301 292  HOH   HOH A . 
G 5 HOH   2   302 1301 HOH   HOH A . 
G 5 HOH   3   303 136  HOH   HOH A . 
G 5 HOH   4   304 1289 HOH   HOH A . 
G 5 HOH   5   305 153  HOH   HOH A . 
G 5 HOH   6   306 85   HOH   HOH A . 
G 5 HOH   7   307 196  HOH   HOH A . 
G 5 HOH   8   308 662  HOH   HOH A . 
G 5 HOH   9   309 625  HOH   HOH A . 
G 5 HOH   10  310 247  HOH   HOH A . 
G 5 HOH   11  311 155  HOH   HOH A . 
G 5 HOH   12  312 105  HOH   HOH A . 
G 5 HOH   13  313 409  HOH   HOH A . 
G 5 HOH   14  314 405  HOH   HOH A . 
G 5 HOH   15  315 1290 HOH   HOH A . 
G 5 HOH   16  316 5    HOH   HOH A . 
G 5 HOH   17  317 109  HOH   HOH A . 
G 5 HOH   18  318 209  HOH   HOH A . 
G 5 HOH   19  319 229  HOH   HOH A . 
G 5 HOH   20  320 1283 HOH   HOH A . 
G 5 HOH   21  321 964  HOH   HOH A . 
G 5 HOH   22  322 151  HOH   HOH A . 
G 5 HOH   23  323 124  HOH   HOH A . 
G 5 HOH   24  324 21   HOH   HOH A . 
G 5 HOH   25  325 76   HOH   HOH A . 
G 5 HOH   26  326 86   HOH   HOH A . 
G 5 HOH   27  327 1295 HOH   HOH A . 
G 5 HOH   28  328 630  HOH   HOH A . 
G 5 HOH   29  329 192  HOH   HOH A . 
G 5 HOH   30  330 57   HOH   HOH A . 
G 5 HOH   31  331 225  HOH   HOH A . 
G 5 HOH   32  332 493  HOH   HOH A . 
G 5 HOH   33  333 15   HOH   HOH A . 
G 5 HOH   34  334 393  HOH   HOH A . 
G 5 HOH   35  335 469  HOH   HOH A . 
G 5 HOH   36  336 241  HOH   HOH A . 
G 5 HOH   37  337 164  HOH   HOH A . 
G 5 HOH   38  338 396  HOH   HOH A . 
G 5 HOH   39  339 140  HOH   HOH A . 
G 5 HOH   40  340 165  HOH   HOH A . 
G 5 HOH   41  341 320  HOH   HOH A . 
G 5 HOH   42  342 661  HOH   HOH A . 
G 5 HOH   43  343 33   HOH   HOH A . 
G 5 HOH   44  344 281  HOH   HOH A . 
G 5 HOH   45  345 337  HOH   HOH A . 
G 5 HOH   46  346 8    HOH   HOH A . 
G 5 HOH   47  347 17   HOH   HOH A . 
G 5 HOH   48  348 96   HOH   HOH A . 
G 5 HOH   49  349 42   HOH   HOH A . 
G 5 HOH   50  350 148  HOH   HOH A . 
G 5 HOH   51  351 92   HOH   HOH A . 
G 5 HOH   52  352 36   HOH   HOH A . 
G 5 HOH   53  353 354  HOH   HOH A . 
G 5 HOH   54  354 1300 HOH   HOH A . 
G 5 HOH   55  355 3    HOH   HOH A . 
G 5 HOH   56  356 236  HOH   HOH A . 
G 5 HOH   57  357 93   HOH   HOH A . 
G 5 HOH   58  358 66   HOH   HOH A . 
G 5 HOH   59  359 1310 HOH   HOH A . 
G 5 HOH   60  360 169  HOH   HOH A . 
G 5 HOH   61  361 102  HOH   HOH A . 
G 5 HOH   62  362 218  HOH   HOH A . 
G 5 HOH   63  363 139  HOH   HOH A . 
G 5 HOH   64  364 39   HOH   HOH A . 
G 5 HOH   65  365 2    HOH   HOH A . 
G 5 HOH   66  366 81   HOH   HOH A . 
G 5 HOH   67  367 5    HOH   HOH A . 
G 5 HOH   68  368 26   HOH   HOH A . 
G 5 HOH   69  369 366  HOH   HOH A . 
G 5 HOH   70  370 1275 HOH   HOH A . 
G 5 HOH   71  371 45   HOH   HOH A . 
G 5 HOH   72  372 49   HOH   HOH A . 
G 5 HOH   73  373 19   HOH   HOH A . 
G 5 HOH   74  374 162  HOH   HOH A . 
G 5 HOH   75  375 159  HOH   HOH A . 
G 5 HOH   76  376 46   HOH   HOH A . 
G 5 HOH   77  377 18   HOH   HOH A . 
G 5 HOH   78  378 35   HOH   HOH A . 
G 5 HOH   79  379 4    HOH   HOH A . 
G 5 HOH   80  380 939  HOH   HOH A . 
G 5 HOH   81  381 154  HOH   HOH A . 
G 5 HOH   82  382 56   HOH   HOH A . 
G 5 HOH   83  383 24   HOH   HOH A . 
G 5 HOH   84  384 138  HOH   HOH A . 
G 5 HOH   85  385 140  HOH   HOH A . 
G 5 HOH   86  386 27   HOH   HOH A . 
G 5 HOH   87  387 186  HOH   HOH A . 
G 5 HOH   88  388 2    HOH   HOH A . 
G 5 HOH   89  389 62   HOH   HOH A . 
G 5 HOH   90  390 116  HOH   HOH A . 
G 5 HOH   91  391 78   HOH   HOH A . 
G 5 HOH   92  392 461  HOH   HOH A . 
G 5 HOH   93  393 58   HOH   HOH A . 
G 5 HOH   94  394 134  HOH   HOH A . 
G 5 HOH   95  395 1309 HOH   HOH A . 
G 5 HOH   96  396 34   HOH   HOH A . 
G 5 HOH   97  397 6    HOH   HOH A . 
G 5 HOH   98  398 1308 HOH   HOH A . 
G 5 HOH   99  399 351  HOH   HOH A . 
G 5 HOH   100 400 115  HOH   HOH A . 
G 5 HOH   101 401 296  HOH   HOH A . 
G 5 HOH   102 402 7    HOH   HOH A . 
G 5 HOH   103 403 333  HOH   HOH A . 
G 5 HOH   104 404 303  HOH   HOH A . 
G 5 HOH   105 405 199  HOH   HOH A . 
G 5 HOH   106 406 1315 HOH   HOH A . 
G 5 HOH   107 407 74   HOH   HOH A . 
G 5 HOH   108 408 12   HOH   HOH A . 
G 5 HOH   109 409 8    HOH   HOH A . 
G 5 HOH   110 410 1313 HOH   HOH A . 
G 5 HOH   111 411 67   HOH   HOH A . 
G 5 HOH   112 412 83   HOH   HOH A . 
G 5 HOH   113 413 122  HOH   HOH A . 
G 5 HOH   114 414 195  HOH   HOH A . 
G 5 HOH   115 415 3    HOH   HOH A . 
G 5 HOH   116 416 278  HOH   HOH A . 
G 5 HOH   117 417 121  HOH   HOH A . 
G 5 HOH   118 418 1068 HOH   HOH A . 
G 5 HOH   119 419 68   HOH   HOH A . 
G 5 HOH   120 420 125  HOH   HOH A . 
G 5 HOH   121 421 25   HOH   HOH A . 
G 5 HOH   122 422 123  HOH   HOH A . 
G 5 HOH   123 423 7    HOH   HOH A . 
G 5 HOH   124 424 397  HOH   HOH A . 
G 5 HOH   125 425 51   HOH   HOH A . 
G 5 HOH   126 426 53   HOH   HOH A . 
G 5 HOH   127 427 95   HOH   HOH A . 
G 5 HOH   128 428 156  HOH   HOH A . 
G 5 HOH   129 429 381  HOH   HOH A . 
G 5 HOH   130 430 582  HOH   HOH A . 
G 5 HOH   131 431 132  HOH   HOH A . 
G 5 HOH   132 432 1279 HOH   HOH A . 
G 5 HOH   133 433 1296 HOH   HOH A . 
G 5 HOH   134 434 1094 HOH   HOH A . 
G 5 HOH   135 435 70   HOH   HOH A . 
G 5 HOH   136 436 944  HOH   HOH A . 
G 5 HOH   137 437 1222 HOH   HOH A . 
G 5 HOH   138 438 212  HOH   HOH A . 
G 5 HOH   139 439 80   HOH   HOH A . 
G 5 HOH   140 440 952  HOH   HOH A . 
G 5 HOH   141 441 73   HOH   HOH A . 
G 5 HOH   142 442 1238 HOH   HOH A . 
G 5 HOH   143 443 71   HOH   HOH A . 
G 5 HOH   144 444 16   HOH   HOH A . 
G 5 HOH   145 445 94   HOH   HOH A . 
G 5 HOH   146 446 79   HOH   HOH A . 
G 5 HOH   147 447 1286 HOH   HOH A . 
G 5 HOH   148 448 40   HOH   HOH A . 
G 5 HOH   149 449 97   HOH   HOH A . 
G 5 HOH   150 450 1134 HOH   HOH A . 
G 5 HOH   151 451 104  HOH   HOH A . 
G 5 HOH   152 452 188  HOH   HOH A . 
G 5 HOH   153 453 1189 HOH   HOH A . 
G 5 HOH   154 454 576  HOH   HOH A . 
G 5 HOH   155 455 6    HOH   HOH A . 
G 5 HOH   156 456 1119 HOH   HOH A . 
G 5 HOH   157 457 330  HOH   HOH A . 
G 5 HOH   158 458 509  HOH   HOH A . 
G 5 HOH   159 459 107  HOH   HOH A . 
G 5 HOH   160 460 726  HOH   HOH A . 
G 5 HOH   161 461 4    HOH   HOH A . 
G 5 HOH   162 462 163  HOH   HOH A . 
G 5 HOH   163 463 408  HOH   HOH A . 
G 5 HOH   164 464 756  HOH   HOH A . 
G 5 HOH   165 465 370  HOH   HOH A . 
G 5 HOH   166 466 1284 HOH   HOH A . 
G 5 HOH   167 467 280  HOH   HOH A . 
G 5 HOH   168 468 556  HOH   HOH A . 
G 5 HOH   169 469 126  HOH   HOH A . 
G 5 HOH   170 470 319  HOH   HOH A . 
G 5 HOH   171 471 1307 HOH   HOH A . 
G 5 HOH   172 472 801  HOH   HOH A . 
G 5 HOH   173 473 342  HOH   HOH A . 
G 5 HOH   174 474 361  HOH   HOH A . 
G 5 HOH   175 475 224  HOH   HOH A . 
G 5 HOH   176 476 1276 HOH   HOH A . 
G 5 HOH   177 477 63   HOH   HOH A . 
G 5 HOH   178 478 250  HOH   HOH A . 
G 5 HOH   179 479 202  HOH   HOH A . 
G 5 HOH   180 480 521  HOH   HOH A . 
G 5 HOH   181 481 1306 HOH   HOH A . 
G 5 HOH   182 482 267  HOH   HOH A . 
G 5 HOH   183 483 1287 HOH   HOH A . 
G 5 HOH   184 484 711  HOH   HOH A . 
G 5 HOH   185 485 674  HOH   HOH A . 
G 5 HOH   186 486 695  HOH   HOH A . 
G 5 HOH   187 487 318  HOH   HOH A . 
G 5 HOH   188 488 919  HOH   HOH A . 
G 5 HOH   189 489 1314 HOH   HOH A . 
G 5 HOH   190 490 135  HOH   HOH A . 
G 5 HOH   191 491 309  HOH   HOH A . 
G 5 HOH   192 492 331  HOH   HOH A . 
G 5 HOH   193 493 805  HOH   HOH A . 
G 5 HOH   194 494 315  HOH   HOH A . 
G 5 HOH   195 495 1299 HOH   HOH A . 
G 5 HOH   196 496 326  HOH   HOH A . 
G 5 HOH   197 497 941  HOH   HOH A . 
G 5 HOH   198 498 263  HOH   HOH A . 
G 5 HOH   199 499 208  HOH   HOH A . 
G 5 HOH   200 500 152  HOH   HOH A . 
G 5 HOH   201 501 356  HOH   HOH A . 
G 5 HOH   202 502 1071 HOH   HOH A . 
G 5 HOH   203 503 180  HOH   HOH A . 
G 5 HOH   204 504 363  HOH   HOH A . 
G 5 HOH   205 505 9    HOH   HOH A . 
G 5 HOH   206 506 371  HOH   HOH A . 
G 5 HOH   207 507 313  HOH   HOH A . 
G 5 HOH   208 508 429  HOH   HOH A . 
G 5 HOH   209 509 185  HOH   HOH A . 
G 5 HOH   210 510 70   HOH   HOH A . 
G 5 HOH   211 511 772  HOH   HOH A . 
G 5 HOH   212 512 376  HOH   HOH A . 
G 5 HOH   213 513 1074 HOH   HOH A . 
G 5 HOH   214 514 346  HOH   HOH A . 
G 5 HOH   215 515 1292 HOH   HOH A . 
G 5 HOH   216 516 1078 HOH   HOH A . 
H 5 HOH   1   201 64   HOH   HOH B . 
H 5 HOH   2   202 240  HOH   HOH B . 
H 5 HOH   3   203 549  HOH   HOH B . 
H 5 HOH   4   204 232  HOH   HOH B . 
H 5 HOH   5   205 900  HOH   HOH B . 
H 5 HOH   6   206 531  HOH   HOH B . 
H 5 HOH   7   207 364  HOH   HOH B . 
H 5 HOH   8   208 758  HOH   HOH B . 
H 5 HOH   9   209 50   HOH   HOH B . 
H 5 HOH   10  210 264  HOH   HOH B . 
H 5 HOH   11  211 743  HOH   HOH B . 
H 5 HOH   12  212 120  HOH   HOH B . 
H 5 HOH   13  213 205  HOH   HOH B . 
H 5 HOH   14  214 398  HOH   HOH B . 
H 5 HOH   15  215 332  HOH   HOH B . 
H 5 HOH   16  216 353  HOH   HOH B . 
H 5 HOH   17  217 1278 HOH   HOH B . 
H 5 HOH   18  218 654  HOH   HOH B . 
H 5 HOH   19  219 1249 HOH   HOH B . 
H 5 HOH   20  220 358  HOH   HOH B . 
H 5 HOH   21  221 82   HOH   HOH B . 
H 5 HOH   22  222 172  HOH   HOH B . 
H 5 HOH   23  223 444  HOH   HOH B . 
H 5 HOH   24  224 1140 HOH   HOH B . 
H 5 HOH   25  225 75   HOH   HOH B . 
H 5 HOH   26  226 452  HOH   HOH B . 
H 5 HOH   27  227 1312 HOH   HOH B . 
H 5 HOH   28  228 343  HOH   HOH B . 
H 5 HOH   29  229 131  HOH   HOH B . 
H 5 HOH   30  230 54   HOH   HOH B . 
H 5 HOH   31  231 60   HOH   HOH B . 
H 5 HOH   32  232 69   HOH   HOH B . 
H 5 HOH   33  233 128  HOH   HOH B . 
H 5 HOH   34  234 41   HOH   HOH B . 
H 5 HOH   35  235 110  HOH   HOH B . 
H 5 HOH   36  236 127  HOH   HOH B . 
H 5 HOH   37  237 276  HOH   HOH B . 
H 5 HOH   38  238 252  HOH   HOH B . 
H 5 HOH   39  239 166  HOH   HOH B . 
H 5 HOH   40  240 272  HOH   HOH B . 
H 5 HOH   41  241 300  HOH   HOH B . 
H 5 HOH   42  242 325  HOH   HOH B . 
H 5 HOH   43  243 52   HOH   HOH B . 
H 5 HOH   44  244 14   HOH   HOH B . 
H 5 HOH   45  245 129  HOH   HOH B . 
H 5 HOH   46  246 133  HOH   HOH B . 
H 5 HOH   47  247 1    HOH   HOH B . 
H 5 HOH   48  248 9    HOH   HOH B . 
H 5 HOH   49  249 181  HOH   HOH B . 
H 5 HOH   50  250 231  HOH   HOH B . 
H 5 HOH   51  251 391  HOH   HOH B . 
H 5 HOH   52  252 723  HOH   HOH B . 
H 5 HOH   53  253 30   HOH   HOH B . 
H 5 HOH   54  254 271  HOH   HOH B . 
H 5 HOH   55  255 150  HOH   HOH B . 
H 5 HOH   56  256 31   HOH   HOH B . 
H 5 HOH   57  257 47   HOH   HOH B . 
H 5 HOH   58  258 143  HOH   HOH B . 
H 5 HOH   59  259 144  HOH   HOH B . 
H 5 HOH   60  260 243  HOH   HOH B . 
H 5 HOH   61  261 103  HOH   HOH B . 
H 5 HOH   62  262 282  HOH   HOH B . 
H 5 HOH   63  263 10   HOH   HOH B . 
H 5 HOH   64  264 242  HOH   HOH B . 
H 5 HOH   65  265 59   HOH   HOH B . 
H 5 HOH   66  266 72   HOH   HOH B . 
H 5 HOH   67  267 61   HOH   HOH B . 
H 5 HOH   68  268 1277 HOH   HOH B . 
H 5 HOH   69  269 114  HOH   HOH B . 
H 5 HOH   70  270 117  HOH   HOH B . 
H 5 HOH   71  271 20   HOH   HOH B . 
H 5 HOH   72  272 302  HOH   HOH B . 
H 5 HOH   73  273 347  HOH   HOH B . 
H 5 HOH   74  274 84   HOH   HOH B . 
H 5 HOH   75  275 11   HOH   HOH B . 
H 5 HOH   76  276 147  HOH   HOH B . 
H 5 HOH   77  277 287  HOH   HOH B . 
H 5 HOH   78  278 175  HOH   HOH B . 
H 5 HOH   79  279 221  HOH   HOH B . 
H 5 HOH   80  280 77   HOH   HOH B . 
H 5 HOH   81  281 43   HOH   HOH B . 
H 5 HOH   82  282 416  HOH   HOH B . 
H 5 HOH   83  283 22   HOH   HOH B . 
H 5 HOH   84  284 99   HOH   HOH B . 
H 5 HOH   85  285 216  HOH   HOH B . 
H 5 HOH   86  286 1305 HOH   HOH B . 
H 5 HOH   87  287 235  HOH   HOH B . 
H 5 HOH   88  288 220  HOH   HOH B . 
H 5 HOH   89  289 13   HOH   HOH B . 
H 5 HOH   90  290 1066 HOH   HOH B . 
H 5 HOH   91  291 106  HOH   HOH B . 
H 5 HOH   92  292 89   HOH   HOH B . 
H 5 HOH   93  293 160  HOH   HOH B . 
H 5 HOH   94  294 311  HOH   HOH B . 
H 5 HOH   95  295 299  HOH   HOH B . 
H 5 HOH   96  296 88   HOH   HOH B . 
H 5 HOH   97  297 387  HOH   HOH B . 
H 5 HOH   98  298 137  HOH   HOH B . 
H 5 HOH   99  299 316  HOH   HOH B . 
H 5 HOH   100 300 215  HOH   HOH B . 
H 5 HOH   101 301 112  HOH   HOH B . 
H 5 HOH   102 302 1106 HOH   HOH B . 
H 5 HOH   103 303 101  HOH   HOH B . 
H 5 HOH   104 304 297  HOH   HOH B . 
H 5 HOH   105 305 32   HOH   HOH B . 
H 5 HOH   106 306 207  HOH   HOH B . 
H 5 HOH   107 307 170  HOH   HOH B . 
H 5 HOH   108 308 142  HOH   HOH B . 
H 5 HOH   109 309 197  HOH   HOH B . 
H 5 HOH   110 310 118  HOH   HOH B . 
H 5 HOH   111 311 38   HOH   HOH B . 
H 5 HOH   112 312 37   HOH   HOH B . 
H 5 HOH   113 313 177  HOH   HOH B . 
H 5 HOH   114 314 635  HOH   HOH B . 
H 5 HOH   115 315 23   HOH   HOH B . 
H 5 HOH   116 316 48   HOH   HOH B . 
H 5 HOH   117 317 91   HOH   HOH B . 
H 5 HOH   118 318 44   HOH   HOH B . 
H 5 HOH   119 319 28   HOH   HOH B . 
H 5 HOH   120 320 1285 HOH   HOH B . 
H 5 HOH   121 321 704  HOH   HOH B . 
H 5 HOH   122 322 1274 HOH   HOH B . 
H 5 HOH   123 323 1291 HOH   HOH B . 
H 5 HOH   124 324 161  HOH   HOH B . 
H 5 HOH   125 325 29   HOH   HOH B . 
H 5 HOH   126 326 100  HOH   HOH B . 
H 5 HOH   127 327 1294 HOH   HOH B . 
H 5 HOH   128 328 55   HOH   HOH B . 
H 5 HOH   129 329 182  HOH   HOH B . 
H 5 HOH   130 330 98   HOH   HOH B . 
H 5 HOH   131 331 334  HOH   HOH B . 
H 5 HOH   132 332 341  HOH   HOH B . 
H 5 HOH   133 333 141  HOH   HOH B . 
H 5 HOH   134 334 717  HOH   HOH B . 
H 5 HOH   135 335 65   HOH   HOH B . 
H 5 HOH   136 336 1126 HOH   HOH B . 
H 5 HOH   137 337 445  HOH   HOH B . 
H 5 HOH   138 338 1293 HOH   HOH B . 
H 5 HOH   139 339 234  HOH   HOH B . 
H 5 HOH   140 340 619  HOH   HOH B . 
H 5 HOH   141 341 178  HOH   HOH B . 
H 5 HOH   142 342 960  HOH   HOH B . 
H 5 HOH   143 343 362  HOH   HOH B . 
H 5 HOH   144 344 339  HOH   HOH B . 
H 5 HOH   145 345 90   HOH   HOH B . 
H 5 HOH   146 346 463  HOH   HOH B . 
H 5 HOH   147 347 87   HOH   HOH B . 
H 5 HOH   148 348 1304 HOH   HOH B . 
H 5 HOH   149 349 191  HOH   HOH B . 
H 5 HOH   150 350 623  HOH   HOH B . 
H 5 HOH   151 351 335  HOH   HOH B . 
H 5 HOH   152 352 1046 HOH   HOH B . 
H 5 HOH   153 353 304  HOH   HOH B . 
H 5 HOH   154 354 1280 HOH   HOH B . 
H 5 HOH   155 355 203  HOH   HOH B . 
H 5 HOH   156 356 541  HOH   HOH B . 
H 5 HOH   157 357 290  HOH   HOH B . 
H 5 HOH   158 358 1077 HOH   HOH B . 
H 5 HOH   159 359 389  HOH   HOH B . 
H 5 HOH   160 360 718  HOH   HOH B . 
H 5 HOH   161 361 283  HOH   HOH B . 
H 5 HOH   162 362 1072 HOH   HOH B . 
H 5 HOH   163 363 479  HOH   HOH B . 
H 5 HOH   164 364 291  HOH   HOH B . 
H 5 HOH   165 365 1316 HOH   HOH B . 
H 5 HOH   166 366 898  HOH   HOH B . 
H 5 HOH   167 367 615  HOH   HOH B . 
H 5 HOH   168 368 373  HOH   HOH B . 
H 5 HOH   169 369 340  HOH   HOH B . 
H 5 HOH   170 370 1303 HOH   HOH B . 
H 5 HOH   171 371 667  HOH   HOH B . 
H 5 HOH   172 372 310  HOH   HOH B . 
H 5 HOH   173 373 190  HOH   HOH B . 
H 5 HOH   174 374 149  HOH   HOH B . 
H 5 HOH   175 375 1173 HOH   HOH B . 
H 5 HOH   176 376 431  HOH   HOH B . 
H 5 HOH   177 377 183  HOH   HOH B . 
H 5 HOH   178 378 1000 HOH   HOH B . 
H 5 HOH   179 379 1163 HOH   HOH B . 
H 5 HOH   180 380 418  HOH   HOH B . 
H 5 HOH   181 381 424  HOH   HOH B . 
H 5 HOH   182 382 176  HOH   HOH B . 
H 5 HOH   183 383 1311 HOH   HOH B . 
H 5 HOH   184 384 491  HOH   HOH B . 
H 5 HOH   185 385 981  HOH   HOH B . 
H 5 HOH   186 386 1298 HOH   HOH B . 
H 5 HOH   187 387 248  HOH   HOH B . 
H 5 HOH   188 388 470  HOH   HOH B . 
H 5 HOH   189 389 265  HOH   HOH B . 
H 5 HOH   190 390 350  HOH   HOH B . 
H 5 HOH   191 391 184  HOH   HOH B . 
H 5 HOH   192 392 410  HOH   HOH B . 
H 5 HOH   193 393 360  HOH   HOH B . 
H 5 HOH   194 394 355  HOH   HOH B . 
H 5 HOH   195 395 274  HOH   HOH B . 
H 5 HOH   196 396 314  HOH   HOH B . 
H 5 HOH   197 397 566  HOH   HOH B . 
H 5 HOH   198 398 157  HOH   HOH B . 
H 5 HOH   199 399 321  HOH   HOH B . 
H 5 HOH   200 400 792  HOH   HOH B . 
H 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HED 
_cell.length_a           88.741 
_cell.length_b           88.741 
_cell.length_c           39.435 
_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                         7HED 
_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          7HED 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.51 
_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                     7HED 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.370 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   155841 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.036 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        19.400 
_reflns.B_iso_Wilson_estimate        12.490 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.039 
_reflns.pdbx_Rpim_I_all              0.015 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1016081 
_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  ? 41131 7490 ? 0.985 ? ? ? 5.500 ? 1.400  ? ? ? ? ? ? 97.800 1.090 0.455 0.813 
1 2 5.590 44.370 ? 7032  1037 ? 0.027 ? ? ? 6.800 ? 68.300 ? ? ? ? ? ? 99.800 0.030 0.011 0.999 
# 
_refine.entry_id                                 7HED 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3700 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7500 
_refine.ls_number_reflns_obs                     155745 
_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                          0.1471 
_refine.ls_R_factor_R_work                       0.1465 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1589 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7513 
_refine.ls_number_reflns_R_work                  148232 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.0084 
_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                            0.0900 
_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                                67.630 
_refine.B_iso_min                                9.910 
_refine.pdbx_overall_phase_error                 18.5800 
_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                        44.3700 
_refine_hist.pdbx_number_atoms_ligand         68 
_refine_hist.number_atoms_solvent             417 
_refine_hist.number_atoms_total               3027 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.61 
_refine_hist.pdbx_B_iso_mean_solvent          31.13 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0200 1.0300  30 97.0000  4791 . 0.3315 0.3378 . 192 0.0000 4983 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4904 . 0.2802 0.2854 . 286 0.0000 5190 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4870 . 0.2414 0.2233 . 280 0.0000 5150 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4907 . 0.2250 0.2438 . 282 0.0000 5189 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4925 . 0.2183 0.2263 . 227 0.0000 5152 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4937 . 0.2055 0.2373 . 235 0.0000 5172 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4902 . 0.1885 0.2042 . 267 0.0000 5169 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4964 . 0.1749 0.1892 . 221 0.0000 5185 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4878 . 0.1669 0.1819 . 240 0.0000 5118 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4931 . 0.1547 0.1863 . 255 0.0000 5186 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4946 . 0.1453 0.1750 . 247 0.0000 5193 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4894 . 0.1364 0.1669 . 270 0.0000 5164 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5036 . 0.1313 0.1525 . 215 0.0000 5251 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4879 . 0.1307 0.1536 . 246 0.0000 5125 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4904 . 0.1331 0.1522 . 250 0.0000 5154 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4932 . 0.1345 0.1475 . 270 0.0000 5202 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4957 . 0.1381 0.1590 . 247 0.0000 5204 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4919 . 0.1370 0.1455 . 260 0.0000 5179 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4959 . 0.1363 0.1715 . 239 0.0000 5198 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4966 . 0.1308 0.1410 . 243 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4945 . 0.1227 0.1299 . 244 0.0000 5189 . 'X-RAY DIFFRACTION' 
1.5200 1.5800  30 100.0000 4926 . 0.1242 0.1394 . 256 0.0000 5182 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 4943 . 0.1248 0.1343 . 268 0.0000 5211 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5005 . 0.1341 0.1419 . 200 0.0000 5205 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4947 . 0.1387 0.1415 . 290 0.0000 5237 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4949 . 0.1380 0.1368 . 243 0.0000 5192 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4943 . 0.1398 0.1492 . 287 0.0000 5230 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 4992 . 0.1405 0.1474 . 252 0.0000 5244 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5017 . 0.1527 0.1612 . 249 0.0000 5266 . 'X-RAY DIFFRACTION' 
3.1700 44.3700 30 100.0000 5164 . 0.1494 0.1717 . 252 0.0000 5416 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HED 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003670' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HED 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H 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 7HED A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HED 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 7HED SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HED MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HED SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HED MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? 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 LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HED 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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  ? ? 55.20   -132.89 
2 1 SER A 128 ? B 68.51   -2.76   
3 1 ASP A 162 ? B -80.85  39.57   
4 1 LYS A 163 ? B -150.94 -39.19  
5 1 HIS B 86  ? ? 57.95   -128.23 
# 
_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 514 ? 5.86 . 
2 1 O ? A HOH 515 ? 5.87 . 
3 1 O ? A HOH 516 ? 7.49 . 
4 1 O ? B HOH 401 ? 6.55 . 
# 
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 
A1A9T N2   N  Y N 1   
A1A9T C3   C  Y N 2   
A1A9T C6   C  Y N 3   
A1A9T C9   C  N N 4   
A1A9T C1   C  N N 5   
A1A9T C10  C  N N 6   
A1A9T C11  C  N N 7   
A1A9T C2   C  N N 8   
A1A9T C4   C  Y N 9   
A1A9T C5   C  Y N 10  
A1A9T C7   C  Y N 11  
A1A9T C8   C  Y N 12  
A1A9T N1   N  N N 13  
A1A9T N3   N  Y N 14  
A1A9T N4   N  Y N 15  
A1A9T O1   O  N N 16  
A1A9T H10  H  N N 17  
A1A9T H9   H  N N 18  
A1A9T H2   H  N N 19  
A1A9T H3   H  N N 20  
A1A9T H12  H  N N 21  
A1A9T H11  H  N N 22  
A1A9T H13  H  N N 23  
A1A9T H14  H  N N 24  
A1A9T H5   H  N N 25  
A1A9T H6   H  N N 26  
A1A9T H7   H  N N 27  
A1A9T H4   H  N N 28  
A1A9T H8   H  N N 29  
A1A9T H1   H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CL    CL   CL N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
GLN   N    N  N N 119 
GLN   CA   C  N S 120 
GLN   C    C  N N 121 
GLN   O    O  N N 122 
GLN   CB   C  N N 123 
GLN   CG   C  N N 124 
GLN   CD   C  N N 125 
GLN   OE1  O  N N 126 
GLN   NE2  N  N N 127 
GLN   OXT  O  N N 128 
GLN   H    H  N N 129 
GLN   H2   H  N N 130 
GLN   HA   H  N N 131 
GLN   HB2  H  N N 132 
GLN   HB3  H  N N 133 
GLN   HG2  H  N N 134 
GLN   HG3  H  N N 135 
GLN   HE21 H  N N 136 
GLN   HE22 H  N N 137 
GLN   HXT  H  N N 138 
GLU   N    N  N N 139 
GLU   CA   C  N S 140 
GLU   C    C  N N 141 
GLU   O    O  N N 142 
GLU   CB   C  N N 143 
GLU   CG   C  N N 144 
GLU   CD   C  N N 145 
GLU   OE1  O  N N 146 
GLU   OE2  O  N N 147 
GLU   OXT  O  N N 148 
GLU   H    H  N N 149 
GLU   H2   H  N N 150 
GLU   HA   H  N N 151 
GLU   HB2  H  N N 152 
GLU   HB3  H  N N 153 
GLU   HG2  H  N N 154 
GLU   HG3  H  N N 155 
GLU   HE2  H  N N 156 
GLU   HXT  H  N N 157 
GLY   N    N  N N 158 
GLY   CA   C  N N 159 
GLY   C    C  N N 160 
GLY   O    O  N N 161 
GLY   OXT  O  N N 162 
GLY   H    H  N N 163 
GLY   H2   H  N N 164 
GLY   HA2  H  N N 165 
GLY   HA3  H  N N 166 
GLY   HXT  H  N N 167 
HIS   N    N  N N 168 
HIS   CA   C  N S 169 
HIS   C    C  N N 170 
HIS   O    O  N N 171 
HIS   CB   C  N N 172 
HIS   CG   C  Y N 173 
HIS   ND1  N  Y N 174 
HIS   CD2  C  Y N 175 
HIS   CE1  C  Y N 176 
HIS   NE2  N  Y N 177 
HIS   OXT  O  N N 178 
HIS   H    H  N N 179 
HIS   H2   H  N N 180 
HIS   HA   H  N N 181 
HIS   HB2  H  N N 182 
HIS   HB3  H  N N 183 
HIS   HD1  H  N N 184 
HIS   HD2  H  N N 185 
HIS   HE1  H  N N 186 
HIS   HE2  H  N N 187 
HIS   HXT  H  N N 188 
HOH   O    O  N N 189 
HOH   H1   H  N N 190 
HOH   H2   H  N N 191 
ILE   N    N  N N 192 
ILE   CA   C  N S 193 
ILE   C    C  N N 194 
ILE   O    O  N N 195 
ILE   CB   C  N S 196 
ILE   CG1  C  N N 197 
ILE   CG2  C  N N 198 
ILE   CD1  C  N N 199 
ILE   OXT  O  N N 200 
ILE   H    H  N N 201 
ILE   H2   H  N N 202 
ILE   HA   H  N N 203 
ILE   HB   H  N N 204 
ILE   HG12 H  N N 205 
ILE   HG13 H  N N 206 
ILE   HG21 H  N N 207 
ILE   HG22 H  N N 208 
ILE   HG23 H  N N 209 
ILE   HD11 H  N N 210 
ILE   HD12 H  N N 211 
ILE   HD13 H  N N 212 
ILE   HXT  H  N N 213 
LEU   N    N  N N 214 
LEU   CA   C  N S 215 
LEU   C    C  N N 216 
LEU   O    O  N N 217 
LEU   CB   C  N N 218 
LEU   CG   C  N N 219 
LEU   CD1  C  N N 220 
LEU   CD2  C  N N 221 
LEU   OXT  O  N N 222 
LEU   H    H  N N 223 
LEU   H2   H  N N 224 
LEU   HA   H  N N 225 
LEU   HB2  H  N N 226 
LEU   HB3  H  N N 227 
LEU   HG   H  N N 228 
LEU   HD11 H  N N 229 
LEU   HD12 H  N N 230 
LEU   HD13 H  N N 231 
LEU   HD21 H  N N 232 
LEU   HD22 H  N N 233 
LEU   HD23 H  N N 234 
LEU   HXT  H  N N 235 
LYS   N    N  N N 236 
LYS   CA   C  N S 237 
LYS   C    C  N N 238 
LYS   O    O  N N 239 
LYS   CB   C  N N 240 
LYS   CG   C  N N 241 
LYS   CD   C  N N 242 
LYS   CE   C  N N 243 
LYS   NZ   N  N N 244 
LYS   OXT  O  N N 245 
LYS   H    H  N N 246 
LYS   H2   H  N N 247 
LYS   HA   H  N N 248 
LYS   HB2  H  N N 249 
LYS   HB3  H  N N 250 
LYS   HG2  H  N N 251 
LYS   HG3  H  N N 252 
LYS   HD2  H  N N 253 
LYS   HD3  H  N N 254 
LYS   HE2  H  N N 255 
LYS   HE3  H  N N 256 
LYS   HZ1  H  N N 257 
LYS   HZ2  H  N N 258 
LYS   HZ3  H  N N 259 
LYS   HXT  H  N N 260 
MET   N    N  N N 261 
MET   CA   C  N S 262 
MET   C    C  N N 263 
MET   O    O  N N 264 
MET   CB   C  N N 265 
MET   CG   C  N N 266 
MET   SD   S  N N 267 
MET   CE   C  N N 268 
MET   OXT  O  N N 269 
MET   H    H  N N 270 
MET   H2   H  N N 271 
MET   HA   H  N N 272 
MET   HB2  H  N N 273 
MET   HB3  H  N N 274 
MET   HG2  H  N N 275 
MET   HG3  H  N N 276 
MET   HE1  H  N N 277 
MET   HE2  H  N N 278 
MET   HE3  H  N N 279 
MET   HXT  H  N N 280 
PHE   N    N  N N 281 
PHE   CA   C  N S 282 
PHE   C    C  N N 283 
PHE   O    O  N N 284 
PHE   CB   C  N N 285 
PHE   CG   C  Y N 286 
PHE   CD1  C  Y N 287 
PHE   CD2  C  Y N 288 
PHE   CE1  C  Y N 289 
PHE   CE2  C  Y N 290 
PHE   CZ   C  Y N 291 
PHE   OXT  O  N N 292 
PHE   H    H  N N 293 
PHE   H2   H  N N 294 
PHE   HA   H  N N 295 
PHE   HB2  H  N N 296 
PHE   HB3  H  N N 297 
PHE   HD1  H  N N 298 
PHE   HD2  H  N N 299 
PHE   HE1  H  N N 300 
PHE   HE2  H  N N 301 
PHE   HZ   H  N N 302 
PHE   HXT  H  N N 303 
PRO   N    N  N N 304 
PRO   CA   C  N S 305 
PRO   C    C  N N 306 
PRO   O    O  N N 307 
PRO   CB   C  N N 308 
PRO   CG   C  N N 309 
PRO   CD   C  N N 310 
PRO   OXT  O  N N 311 
PRO   H    H  N N 312 
PRO   HA   H  N N 313 
PRO   HB2  H  N N 314 
PRO   HB3  H  N N 315 
PRO   HG2  H  N N 316 
PRO   HG3  H  N N 317 
PRO   HD2  H  N N 318 
PRO   HD3  H  N N 319 
PRO   HXT  H  N N 320 
SER   N    N  N N 321 
SER   CA   C  N S 322 
SER   C    C  N N 323 
SER   O    O  N N 324 
SER   CB   C  N N 325 
SER   OG   O  N N 326 
SER   OXT  O  N N 327 
SER   H    H  N N 328 
SER   H2   H  N N 329 
SER   HA   H  N N 330 
SER   HB2  H  N N 331 
SER   HB3  H  N N 332 
SER   HG   H  N N 333 
SER   HXT  H  N N 334 
TFA   C1   C  N N 335 
TFA   C2   C  N N 336 
TFA   O    O  N N 337 
TFA   F1   F  N N 338 
TFA   F2   F  N N 339 
TFA   F3   F  N N 340 
TFA   OXT  O  N N 341 
TFA   HXT  H  N N 342 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TYR   N    N  N N 360 
TYR   CA   C  N S 361 
TYR   C    C  N N 362 
TYR   O    O  N N 363 
TYR   CB   C  N N 364 
TYR   CG   C  Y N 365 
TYR   CD1  C  Y N 366 
TYR   CD2  C  Y N 367 
TYR   CE1  C  Y N 368 
TYR   CE2  C  Y N 369 
TYR   CZ   C  Y N 370 
TYR   OH   O  N N 371 
TYR   OXT  O  N N 372 
TYR   H    H  N N 373 
TYR   H2   H  N N 374 
TYR   HA   H  N N 375 
TYR   HB2  H  N N 376 
TYR   HB3  H  N N 377 
TYR   HD1  H  N N 378 
TYR   HD2  H  N N 379 
TYR   HE1  H  N N 380 
TYR   HE2  H  N N 381 
TYR   HH   H  N N 382 
TYR   HXT  H  N N 383 
VAL   N    N  N N 384 
VAL   CA   C  N S 385 
VAL   C    C  N N 386 
VAL   O    O  N N 387 
VAL   CB   C  N N 388 
VAL   CG1  C  N N 389 
VAL   CG2  C  N N 390 
VAL   OXT  O  N N 391 
VAL   H    H  N N 392 
VAL   H2   H  N N 393 
VAL   HA   H  N N 394 
VAL   HB   H  N N 395 
VAL   HG11 H  N N 396 
VAL   HG12 H  N N 397 
VAL   HG13 H  N N 398 
VAL   HG21 H  N N 399 
VAL   HG22 H  N N 400 
VAL   HG23 H  N N 401 
VAL   HXT  H  N N 402 
# 
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 
A1A9T C10 C11  sing N N 1   
A1A9T C10 C9   sing N N 2   
A1A9T C11 C2   sing N N 3   
A1A9T C9  C2   sing N N 4   
A1A9T C2  C1   sing N N 5   
A1A9T C2  N1   sing N N 6   
A1A9T C1  O1   sing N N 7   
A1A9T N1  C3   sing N N 8   
A1A9T C3  C6   doub Y N 9   
A1A9T C3  N2   sing Y N 10  
A1A9T C7  C6   sing Y N 11  
A1A9T C7  C8   doub Y N 12  
A1A9T C6  C5   sing Y N 13  
A1A9T N2  C4   doub Y N 14  
A1A9T C8  N4   sing Y N 15  
A1A9T C5  N4   sing Y N 16  
A1A9T C5  N3   doub Y N 17  
A1A9T C4  N3   sing Y N 18  
A1A9T C9  H10  sing N N 19  
A1A9T C9  H9   sing N N 20  
A1A9T C1  H2   sing N N 21  
A1A9T C1  H3   sing N N 22  
A1A9T C10 H12  sing N N 23  
A1A9T C10 H11  sing N N 24  
A1A9T C11 H13  sing N N 25  
A1A9T C11 H14  sing N N 26  
A1A9T C4  H5   sing N N 27  
A1A9T C7  H6   sing N N 28  
A1A9T C8  H7   sing N N 29  
A1A9T N1  H4   sing N N 30  
A1A9T N4  H8   sing N N 31  
A1A9T O1  H1   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
TFA   C1  C2   sing N N 322 
TFA   C1  O    doub N N 323 
TFA   C1  OXT  sing N N 324 
TFA   C2  F1   sing N N 325 
TFA   C2  F2   sing N N 326 
TFA   C2  F3   sing N N 327 
TFA   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HED 
_atom_sites.fract_transf_matrix[1][1]   0.011269 
_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]   0.011269 
_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]   0.025358 
_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    . VAL   A 1 3   ? 19.588 -16.173 22.292  1.00 55.47 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.628 -15.089 22.460  1.00 54.85 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.279 -13.750 22.129  1.00 52.51 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.389 -13.465 22.580  1.00 53.31 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.026 -15.088 23.881  1.00 56.02 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 17.020 -13.955 24.036  1.00 56.37 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.371 -16.430 24.181  1.00 56.36 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.898 -15.220 21.840  1.00 65.81 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.734 -14.950 24.529  1.00 67.21 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.525 -14.084 24.861  1.00 67.63 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.495 -13.110 24.067  1.00 67.63 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.412 -13.968 23.281  1.00 67.63 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.936 -16.384 25.047  1.00 67.62 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.716 -16.622 23.491  1.00 67.62 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.053 -17.119 24.191  1.00 67.62 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.590 -12.935 21.331  1.00 48.73 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.034 -11.582 21.011  1.00 44.51 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.899 -10.600 21.294  1.00 40.30 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.801 -10.987 21.706  1.00 40.17 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.579 -11.477 19.579  1.00 44.13 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.564 -11.872 18.533  1.00 43.58 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.449 -11.351 18.503  1.00 43.37 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 18.947 -12.800 17.662  1.00 43.42 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.845 -13.152 20.958  1.00 58.46 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.763 -11.359 21.602  1.00 53.39 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.846 -10.559 19.410  1.00 52.94 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.346 -12.064 19.491  1.00 52.94 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.409 -13.059 17.044  1.00 52.08 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.736 -13.143 17.716  1.00 52.08 ?  4   ASN   A HD22 1 
ATOM   30   N  N    A SER   A 1 5   ? 18.177 -9.313  21.086  0.64 38.01 ?  5   SER   A N    1 
ATOM   31   N  N    B SER   A 1 5   ? 18.165 -9.317  21.041  0.36 38.27 ?  5   SER   A N    1 
ATOM   32   C  CA   A SER   A 1 5   ? 17.256 -8.246  21.457  0.64 35.66 ?  5   SER   A CA   1 
ATOM   33   C  CA   B SER   A 1 5   ? 17.282 -8.233  21.452  0.36 36.14 ?  5   SER   A CA   1 
ATOM   34   C  C    A SER   A 1 5   ? 16.396 -7.762  20.294  0.64 32.34 ?  5   SER   A C    1 
ATOM   35   C  C    B SER   A 1 5   ? 16.407 -7.697  20.322  0.36 33.10 ?  5   SER   A C    1 
ATOM   36   O  O    A SER   A 1 5   ? 15.723 -6.735  20.423  0.64 32.56 ?  5   SER   A O    1 
ATOM   37   O  O    B SER   A 1 5   ? 15.720 -6.688  20.516  0.36 33.30 ?  5   SER   A O    1 
ATOM   38   C  CB   A SER   A 1 5   ? 18.021 -7.072  22.075  0.64 36.64 ?  5   SER   A CB   1 
ATOM   39   C  CB   B SER   A 1 5   ? 18.095 -7.093  22.070  0.36 36.97 ?  5   SER   A CB   1 
ATOM   40   O  OG   A SER   A 1 5   ? 18.984 -6.556  21.173  0.64 37.21 ?  5   SER   A OG   1 
ATOM   41   O  OG   B SER   A 1 5   ? 18.980 -6.524  21.121  0.36 37.43 ?  5   SER   A OG   1 
ATOM   42   H  H    A SER   A 1 5   ? 18.904 -9.032  20.722  0.64 45.60 ?  5   SER   A H    1 
ATOM   43   H  H    B SER   A 1 5   ? 18.866 -9.051  20.620  0.36 45.91 ?  5   SER   A H    1 
ATOM   44   H  HA   A SER   A 1 5   ? 16.659 -8.584  22.141  0.64 42.78 ?  5   SER   A HA   1 
ATOM   45   H  HA   B SER   A 1 5   ? 16.691 -8.568  22.141  0.36 43.35 ?  5   SER   A HA   1 
ATOM   46   H  HB2  A SER   A 1 5   ? 17.391 -6.368  22.301  0.64 43.95 ?  5   SER   A HB2  1 
ATOM   47   H  HB2  B SER   A 1 5   ? 17.484 -6.407  22.387  0.36 44.35 ?  5   SER   A HB2  1 
ATOM   48   H  HB3  A SER   A 1 5   ? 18.473 -7.377  22.880  0.64 43.95 ?  5   SER   A HB3  1 
ATOM   49   H  HB3  B SER   A 1 5   ? 18.613 -7.441  22.813  0.36 44.35 ?  5   SER   A HB3  1 
ATOM   50   H  HG   A SER   A 1 5   ? 19.394 -5.913  21.528  0.64 44.64 ?  5   SER   A HG   1 
ATOM   51   H  HG   B SER   A 1 5   ? 19.414 -5.896  21.474  0.36 44.90 ?  5   SER   A HG   1 
ATOM   52   N  N    A PHE   A 1 6   ? 16.400 -8.470  19.168  0.64 28.59 ?  6   PHE   A N    1 
ATOM   53   N  N    B PHE   A 1 6   ? 16.412 -8.333  19.154  0.36 29.72 ?  6   PHE   A N    1 
ATOM   54   C  CA   A PHE   A 1 6   ? 15.503 -8.122  18.074  0.64 25.04 ?  6   PHE   A CA   1 
ATOM   55   C  CA   B PHE   A 1 6   ? 15.500 -7.931  18.091  0.36 26.37 ?  6   PHE   A CA   1 
ATOM   56   C  C    A PHE   A 1 6   ? 14.070 -8.494  18.441  0.64 24.38 ?  6   PHE   A C    1 
ATOM   57   C  C    B PHE   A 1 6   ? 14.071 -8.277  18.495  0.36 25.51 ?  6   PHE   A C    1 
ATOM   58   O  O    A PHE   A 1 6   ? 13.818 -9.557  19.012  0.64 25.33 ?  6   PHE   A O    1 
ATOM   59   O  O    B PHE   A 1 6   ? 13.772 -9.432  18.813  0.36 25.56 ?  6   PHE   A O    1 
ATOM   60   C  CB   A PHE   A 1 6   ? 15.930 -8.842  16.796  0.64 22.91 ?  6   PHE   A CB   1 
ATOM   61   C  CB   B PHE   A 1 6   ? 15.856 -8.649  16.791  0.36 24.32 ?  6   PHE   A CB   1 
ATOM   62   C  CG   A PHE   A 1 6   ? 17.210 -8.309  16.202  0.64 21.36 ?  6   PHE   A CG   1 
ATOM   63   C  CG   B PHE   A 1 6   ? 17.153 -8.196  16.174  0.36 22.70 ?  6   PHE   A CG   1 
ATOM   64   C  CD1  A PHE   A 1 6   ? 17.210 -7.137  15.464  0.64 20.69 ?  6   PHE   A CD1  1 
ATOM   65   C  CD1  B PHE   A 1 6   ? 17.223 -7.002  15.474  0.36 21.98 ?  6   PHE   A CD1  1 
ATOM   66   C  CD2  A PHE   A 1 6   ? 18.406 -8.982  16.384  0.64 21.70 ?  6   PHE   A CD2  1 
ATOM   67   C  CD2  B PHE   A 1 6   ? 18.294 -8.974  16.277  0.36 22.39 ?  6   PHE   A CD2  1 
ATOM   68   C  CE1  A PHE   A 1 6   ? 18.380 -6.645  14.917  0.64 20.66 ?  6   PHE   A CE1  1 
ATOM   69   C  CE1  B PHE   A 1 6   ? 18.411 -6.587  14.899  0.36 21.75 ?  6   PHE   A CE1  1 
ATOM   70   C  CE2  A PHE   A 1 6   ? 19.577 -8.496  15.838  0.64 21.68 ?  6   PHE   A CE2  1 
ATOM   71   C  CE2  B PHE   A 1 6   ? 19.483 -8.566  15.703  0.36 22.12 ?  6   PHE   A CE2  1 
ATOM   72   C  CZ   A PHE   A 1 6   ? 19.564 -7.324  15.104  0.64 21.08 ?  6   PHE   A CZ   1 
ATOM   73   C  CZ   B PHE   A 1 6   ? 19.541 -7.370  15.013  0.36 21.80 ?  6   PHE   A CZ   1 
ATOM   74   H  H    A PHE   A 1 6   ? 16.903 -9.151  19.018  0.64 34.29 ?  6   PHE   A H    1 
ATOM   75   H  H    B PHE   A 1 6   ? 16.923 -8.994  18.955  0.36 35.64 ?  6   PHE   A H    1 
ATOM   76   H  HA   A PHE   A 1 6   ? 15.536 -7.173  17.922  0.64 30.03 ?  6   PHE   A HA   1 
ATOM   77   H  HA   B PHE   A 1 6   ? 15.562 -6.975  17.947  0.36 31.63 ?  6   PHE   A HA   1 
ATOM   78   H  HB2  A PHE   A 1 6   ? 16.060 -9.786  16.997  0.64 27.47 ?  6   PHE   A HB2  1 
ATOM   79   H  HB2  B PHE   A 1 6   ? 15.929 -9.599  16.973  0.36 29.17 ?  6   PHE   A HB2  1 
ATOM   80   H  HB3  A PHE   A 1 6   ? 15.228 -8.745  16.135  0.64 27.47 ?  6   PHE   A HB3  1 
ATOM   81   H  HB3  B PHE   A 1 6   ? 15.150 -8.492  16.146  0.36 29.17 ?  6   PHE   A HB3  1 
ATOM   82   H  HD1  A PHE   A 1 6   ? 16.411 -6.680  15.337  0.64 24.81 ?  6   PHE   A HD1  1 
ATOM   83   H  HD1  B PHE   A 1 6   ? 16.464 -6.471  15.395  0.36 26.36 ?  6   PHE   A HD1  1 
ATOM   84   H  HD2  A PHE   A 1 6   ? 18.419 -9.773  16.880  0.64 26.03 ?  6   PHE   A HD2  1 
ATOM   85   H  HD2  B PHE   A 1 6   ? 18.261 -9.780  16.741  0.36 26.85 ?  6   PHE   A HD2  1 
ATOM   86   H  HE1  A PHE   A 1 6   ? 18.366 -5.857  14.424  0.64 24.78 ?  6   PHE   A HE1  1 
ATOM   87   H  HE1  B PHE   A 1 6   ? 18.447 -5.782  14.434  0.36 26.08 ?  6   PHE   A HE1  1 
ATOM   88   H  HE2  A PHE   A 1 6   ? 20.376 -8.954  15.968  0.64 26.00 ?  6   PHE   A HE2  1 
ATOM   89   H  HE2  B PHE   A 1 6   ? 20.245 -9.095  15.782  0.36 26.53 ?  6   PHE   A HE2  1 
ATOM   90   H  HZ   A PHE   A 1 6   ? 20.351 -6.994  14.738  0.64 25.27 ?  6   PHE   A HZ   1 
ATOM   91   H  HZ   B PHE   A 1 6   ? 20.340 -7.093  14.626  0.36 26.15 ?  6   PHE   A HZ   1 
ATOM   92   N  N    A SER   A 1 7   ? 13.126 -7.608  18.115  0.64 22.65 ?  7   SER   A N    1 
ATOM   93   N  N    B SER   A 1 7   ? 13.186 -7.282  18.480  0.36 24.73 ?  7   SER   A N    1 
ATOM   94   C  CA   A SER   A 1 7   ? 11.754 -7.716  18.598  0.64 22.01 ?  7   SER   A CA   1 
ATOM   95   C  CA   B SER   A 1 7   ? 11.832 -7.437  18.993  0.36 24.47 ?  7   SER   A CA   1 
ATOM   96   C  C    A SER   A 1 7   ? 10.759 -7.467  17.472  0.64 19.70 ?  7   SER   A C    1 
ATOM   97   C  C    B SER   A 1 7   ? 10.817 -7.069  17.919  0.36 22.84 ?  7   SER   A C    1 
ATOM   98   O  O    A SER   A 1 7   ? 10.954 -6.573  16.643  0.64 19.64 ?  7   SER   A O    1 
ATOM   99   O  O    B SER   A 1 7   ? 11.033 -6.135  17.140  0.36 23.01 ?  7   SER   A O    1 
ATOM   100  C  CB   A SER   A 1 7   ? 11.504 -6.694  19.716  0.64 23.63 ?  7   SER   A CB   1 
ATOM   101  C  CB   B SER   A 1 7   ? 11.624 -6.557  20.233  0.36 25.55 ?  7   SER   A CB   1 
ATOM   102  O  OG   A SER   A 1 7   ? 10.156 -6.715  20.150  0.64 24.84 ?  7   SER   A OG   1 
ATOM   103  O  OG   B SER   A 1 7   ? 10.683 -7.137  21.119  0.36 26.34 ?  7   SER   A OG   1 
ATOM   104  H  H    A SER   A 1 7   ? 13.262 -6.934  17.608  0.64 27.17 ?  7   SER   A H    1 
ATOM   105  H  H    B SER   A 1 7   ? 13.347 -6.494  18.169  0.36 29.66 ?  7   SER   A H    1 
ATOM   106  H  HA   A SER   A 1 7   ? 11.599 -8.604  18.956  0.64 26.39 ?  7   SER   A HA   1 
ATOM   107  H  HA   B SER   A 1 7   ? 11.682 -8.359  19.248  0.36 29.35 ?  7   SER   A HA   1 
ATOM   108  H  HB2  A SER   A 1 7   ? 12.082 -6.903  20.468  0.64 28.34 ?  7   SER   A HB2  1 
ATOM   109  H  HB2  B SER   A 1 7   ? 12.476 -6.453  20.690  0.36 30.64 ?  7   SER   A HB2  1 
ATOM   110  H  HB3  A SER   A 1 7   ? 11.711 -5.806  19.382  0.64 28.34 ?  7   SER   A HB3  1 
ATOM   111  H  HB3  B SER   A 1 7   ? 11.291 -5.691  19.956  0.36 30.64 ?  7   SER   A HB3  1 
ATOM   112  H  HG   A SER   A 1 7   ? 10.044 -6.150  20.764  0.64 29.79 ?  7   SER   A HG   1 
ATOM   113  H  HG   B SER   A 1 7   ? 10.595 -6.654  21.801  0.36 31.59 ?  7   SER   A HG   1 
ATOM   114  N  N    A GLY   A 1 8   ? 9.677  -8.248  17.463  0.64 18.08 ?  8   GLY   A N    1 
ATOM   115  N  N    B GLY   A 1 8   ? 9.711  -7.813  17.879  0.36 21.14 ?  8   GLY   A N    1 
ATOM   116  C  CA   A GLY   A 1 8   ? 8.590  -8.021  16.531  0.64 16.95 ?  8   GLY   A CA   1 
ATOM   117  C  CA   B GLY   A 1 8   ? 8.637  -7.536  16.947  0.36 19.56 ?  8   GLY   A CA   1 
ATOM   118  C  C    A GLY   A 1 8   ? 8.813  -8.522  15.123  0.64 15.63 ?  8   GLY   A C    1 
ATOM   119  C  C    B GLY   A 1 8   ? 8.808  -8.116  15.562  0.36 17.70 ?  8   GLY   A C    1 
ATOM   120  O  O    A GLY   A 1 8   ? 8.085  -8.111  14.212  0.64 16.13 ?  8   GLY   A O    1 
ATOM   121  O  O    B GLY   A 1 8   ? 8.022  -7.777  14.670  0.36 17.93 ?  8   GLY   A O    1 
ATOM   122  H  H    A GLY   A 1 8   ? 9.552  -8.911  17.997  0.64 21.68 ?  8   GLY   A H    1 
ATOM   123  H  H    B GLY   A 1 8   ? 9.561  -8.489  18.390  0.36 25.35 ?  8   GLY   A H    1 
ATOM   124  H  HA2  A GLY   A 1 8   ? 7.789  -8.447  16.882  0.64 20.32 ?  8   GLY   A HA2  1 
ATOM   125  H  HA2  B GLY   A 1 8   ? 7.809  -7.890  17.305  0.36 23.46 ?  8   GLY   A HA2  1 
ATOM   126  H  HA3  A GLY   A 1 8   ? 8.419  -7.070  16.477  0.64 20.32 ?  8   GLY   A HA3  1 
ATOM   127  H  HA3  B GLY   A 1 8   ? 8.537  -6.574  16.860  0.36 23.46 ?  8   GLY   A HA3  1 
ATOM   128  N  N    A TYR   A 1 9   ? 9.790  -9.404  14.911  0.64 14.52 ?  9   TYR   A N    1 
ATOM   129  N  N    B TYR   A 1 9   ? 9.797  -8.980  15.350  0.36 16.08 ?  9   TYR   A N    1 
ATOM   130  C  CA   A TYR   A 1 9   ? 10.075 -9.929  13.584  0.64 13.49 ?  9   TYR   A CA   1 
ATOM   131  C  CA   B TYR   A 1 9   ? 10.059 -9.535  14.028  0.36 14.76 ?  9   TYR   A CA   1 
ATOM   132  C  C    A TYR   A 1 9   ? 9.220  -11.152 13.285  0.64 12.66 ?  9   TYR   A C    1 
ATOM   133  C  C    B TYR   A 1 9   ? 9.215  -10.778 13.776  0.36 14.01 ?  9   TYR   A C    1 
ATOM   134  O  O    A TYR   A 1 9   ? 8.960  -11.981 14.161  0.64 13.78 ?  9   TYR   A O    1 
ATOM   135  O  O    B TYR   A 1 9   ? 8.941  -11.560 14.690  0.36 15.04 ?  9   TYR   A O    1 
ATOM   136  C  CB   A TYR   A 1 9   ? 11.550 -10.320 13.454  0.64 13.73 ?  9   TYR   A CB   1 
ATOM   137  C  CB   B TYR   A 1 9   ? 11.543 -9.881  13.869  0.36 14.95 ?  9   TYR   A CB   1 
ATOM   138  C  CG   A TYR   A 1 9   ? 12.473 -9.138  13.300  0.64 14.11 ?  9   TYR   A CG   1 
ATOM   139  C  CG   B TYR   A 1 9   ? 12.422 -8.678  13.612  0.36 14.71 ?  9   TYR   A CG   1 
ATOM   140  C  CD1  A TYR   A 1 9   ? 12.824 -8.367  14.398  0.64 14.50 ?  9   TYR   A CD1  1 
ATOM   141  C  CD1  B TYR   A 1 9   ? 12.671 -7.757  14.616  0.36 14.80 ?  9   TYR   A CD1  1 
ATOM   142  C  CD2  A TYR   A 1 9   ? 12.976 -8.787  12.056  0.64 14.72 ?  9   TYR   A CD2  1 
ATOM   143  C  CD2  B TYR   A 1 9   ? 12.995 -8.461  12.364  0.36 14.43 ?  9   TYR   A CD2  1 
ATOM   144  C  CE1  A TYR   A 1 9   ? 13.652 -7.275  14.263  0.64 15.41 ?  9   TYR   A CE1  1 
ATOM   145  C  CE1  B TYR   A 1 9   ? 13.461 -6.655  14.391  0.36 14.86 ?  9   TYR   A CE1  1 
ATOM   146  C  CE2  A TYR   A 1 9   ? 13.801 -7.701  11.908  0.64 15.41 ?  9   TYR   A CE2  1 
ATOM   147  C  CE2  B TYR   A 1 9   ? 13.790 -7.355  12.128  0.36 14.34 ?  9   TYR   A CE2  1 
ATOM   148  C  CZ   A TYR   A 1 9   ? 14.134 -6.947  13.012  0.64 15.92 ?  9   TYR   A CZ   1 
ATOM   149  C  CZ   B TYR   A 1 9   ? 14.017 -6.459  13.148  0.36 14.68 ?  9   TYR   A CZ   1 
ATOM   150  O  OH   A TYR   A 1 9   ? 14.958 -5.866  12.853  0.64 17.26 ?  9   TYR   A OH   1 
ATOM   151  O  OH   B TYR   A 1 9   ? 14.799 -5.353  12.928  0.36 14.87 ?  9   TYR   A OH   1 
ATOM   152  H  H    A TYR   A 1 9   ? 10.295 -9.724  15.529  0.64 17.41 ?  9   TYR   A H    1 
ATOM   153  H  H    B TYR   A 1 9   ? 10.332 -9.260  15.961  0.36 19.29 ?  9   TYR   A H    1 
ATOM   154  H  HA   A TYR   A 1 9   ? 9.877  -9.256  12.920  0.64 16.18 ?  9   TYR   A HA   1 
ATOM   155  H  HA   B TYR   A 1 9   ? 9.831  -8.873  13.357  0.36 17.70 ?  9   TYR   A HA   1 
ATOM   156  H  HB2  A TYR   A 1 9   ? 11.819 -10.815 14.244  0.64 16.46 ?  9   TYR   A HB2  1 
ATOM   157  H  HB2  B TYR   A 1 9   ? 11.857 -10.313 14.677  0.36 17.93 ?  9   TYR   A HB2  1 
ATOM   158  H  HB3  A TYR   A 1 9   ? 11.643 -10.876 12.668  0.64 16.46 ?  9   TYR   A HB3  1 
ATOM   159  H  HB3  B TYR   A 1 9   ? 11.640 -10.484 13.116  0.36 17.93 ?  9   TYR   A HB3  1 
ATOM   160  H  HD1  A TYR   A 1 9   ? 12.487 -8.591  15.240  0.64 17.39 ?  9   TYR   A HD1  1 
ATOM   161  H  HD1  B TYR   A 1 9   ? 12.295 -7.884  15.457  0.36 17.75 ?  9   TYR   A HD1  1 
ATOM   162  H  HD2  A TYR   A 1 9   ? 12.744 -9.296  11.312  0.64 17.65 ?  9   TYR   A HD2  1 
ATOM   163  H  HD2  B TYR   A 1 9   ? 12.838 -9.068  11.676  0.36 17.30 ?  9   TYR   A HD2  1 
ATOM   164  H  HE1  A TYR   A 1 9   ? 13.885 -6.770  15.008  0.64 18.47 ?  9   TYR   A HE1  1 
ATOM   165  H  HE1  B TYR   A 1 9   ? 13.623 -6.043  15.073  0.36 17.81 ?  9   TYR   A HE1  1 
ATOM   166  H  HE2  A TYR   A 1 9   ? 14.138 -7.483  11.070  0.64 18.47 ?  9   TYR   A HE2  1 
ATOM   167  H  HE2  B TYR   A 1 9   ? 14.172 -7.220  11.288  0.36 17.19 ?  9   TYR   A HE2  1 
ATOM   168  H  HH   A TYR   A 1 9   ? 15.108 -5.502  13.593  0.64 20.70 ?  9   TYR   A HH   1 
ATOM   169  H  HH   B TYR   A 1 9   ? 14.901 -4.919  13.640  0.36 17.83 ?  9   TYR   A HH   1 
ATOM   170  N  N    A LEU   A 1 10  ? 8.809  -11.270 12.028  0.64 12.54 ?  10  LEU   A N    1 
ATOM   171  N  N    B LEU   A 1 10  ? 8.789  -10.932 12.525  0.36 13.43 ?  10  LEU   A N    1 
ATOM   172  C  CA   A LEU   A 1 10  ? 8.213  -12.498 11.527  0.64 12.25 ?  10  LEU   A CA   1 
ATOM   173  C  CA   B LEU   A 1 10  ? 8.146  -12.146 12.045  0.36 13.26 ?  10  LEU   A CA   1 
ATOM   174  C  C    A LEU   A 1 10  ? 9.332  -13.439 11.095  0.64 12.06 ?  10  LEU   A C    1 
ATOM   175  C  C    B LEU   A 1 10  ? 9.230  -13.108 11.576  0.36 12.59 ?  10  LEU   A C    1 
ATOM   176  O  O    A LEU   A 1 10  ? 10.282 -13.020 10.421  0.64 12.31 ?  10  LEU   A O    1 
ATOM   177  O  O    B LEU   A 1 10  ? 10.145 -12.713 10.847  0.36 12.24 ?  10  LEU   A O    1 
ATOM   178  C  CB   A LEU   A 1 10  ? 7.333  -12.178 10.324  0.64 13.32 ?  10  LEU   A CB   1 
ATOM   179  C  CB   B LEU   A 1 10  ? 7.216  -11.799 10.882  0.36 13.95 ?  10  LEU   A CB   1 
ATOM   180  C  CG   A LEU   A 1 10  ? 6.628  -13.361 9.661   0.64 15.56 ?  10  LEU   A CG   1 
ATOM   181  C  CG   B LEU   A 1 10  ? 6.487  -12.936 10.170  0.36 15.04 ?  10  LEU   A CG   1 
ATOM   182  C  CD1  A LEU   A 1 10  ? 5.597  -13.953 10.600  0.64 16.88 ?  10  LEU   A CD1  1 
ATOM   183  C  CD1  B LEU   A 1 10  ? 5.490  -13.599 11.103  0.36 15.97 ?  10  LEU   A CD1  1 
ATOM   184  C  CD2  A LEU   A 1 10  ? 5.994  -12.939 8.347   0.64 16.66 ?  10  LEU   A CD2  1 
ATOM   185  C  CD2  B LEU   A 1 10  ? 5.798  -12.376 8.938   0.36 16.10 ?  10  LEU   A CD2  1 
ATOM   186  H  H    A LEU   A 1 10  ? 8.872  -10.652 11.434  0.64 15.03 ?  10  LEU   A H    1 
ATOM   187  H  H    B LEU   A 1 10  ? 8.860  -10.318 11.925  0.36 16.10 ?  10  LEU   A H    1 
ATOM   188  H  HA   A LEU   A 1 10  ? 7.681  -12.926 12.221  0.64 14.68 ?  10  LEU   A HA   1 
ATOM   189  H  HA   B LEU   A 1 10  ? 7.629  -12.559 12.756  0.36 15.90 ?  10  LEU   A HA   1 
ATOM   190  H  HB2  A LEU   A 1 10  ? 6.646  -11.562 10.607  0.64 15.97 ?  10  LEU   A HB2  1 
ATOM   191  H  HB2  B LEU   A 1 10  ? 6.529  -11.194 11.213  0.36 16.72 ?  10  LEU   A HB2  1 
ATOM   192  H  HB3  A LEU   A 1 10  ? 7.888  -11.765 9.648   0.64 15.97 ?  10  LEU   A HB3  1 
ATOM   193  H  HB3  B LEU   A 1 10  ? 7.738  -11.337 10.208  0.36 16.72 ?  10  LEU   A HB3  1 
ATOM   194  H  HG   A LEU   A 1 10  ? 7.280  -14.057 9.463   0.64 18.65 ?  10  LEU   A HG   1 
ATOM   195  H  HG   B LEU   A 1 10  ? 7.129  -13.602 9.882   0.36 18.03 ?  10  LEU   A HG   1 
ATOM   196  H  HD11 A LEU   A 1 10  ? 5.192  -14.731 10.183  0.64 20.24 ?  10  LEU   A HD11 1 
ATOM   197  H  HD11 B LEU   A 1 10  ? 5.090  -14.359 10.650  0.36 19.15 ?  10  LEU   A HD11 1 
ATOM   198  H  HD12 A LEU   A 1 10  ? 6.029  -14.212 11.429  0.64 20.24 ?  10  LEU   A HD12 1 
ATOM   199  H  HD12 B LEU   A 1 10  ? 5.953  -13.897 11.901  0.36 19.15 ?  10  LEU   A HD12 1 
ATOM   200  H  HD13 A LEU   A 1 10  ? 4.916  -13.285 10.781  0.64 20.24 ?  10  LEU   A HD13 1 
ATOM   201  H  HD13 B LEU   A 1 10  ? 4.803  -12.957 11.340  0.36 19.15 ?  10  LEU   A HD13 1 
ATOM   202  H  HD21 A LEU   A 1 10  ? 5.552  -13.706 7.948   0.64 19.97 ?  10  LEU   A HD21 1 
ATOM   203  H  HD21 B LEU   A 1 10  ? 5.323  -13.092 8.490   0.36 19.30 ?  10  LEU   A HD21 1 
ATOM   204  H  HD22 A LEU   A 1 10  ? 5.347  -12.239 8.524   0.64 19.97 ?  10  LEU   A HD22 1 
ATOM   205  H  HD22 B LEU   A 1 10  ? 5.174  -11.685 9.214   0.36 19.30 ?  10  LEU   A HD22 1 
ATOM   206  H  HD23 A LEU   A 1 10  ? 6.687  -12.610 7.755   0.64 19.97 ?  10  LEU   A HD23 1 
ATOM   207  H  HD23 B LEU   A 1 10  ? 6.468  -11.999 8.347   0.36 19.30 ?  10  LEU   A HD23 1 
ATOM   208  N  N    A LYS   A 1 11  ? 9.221  -14.708 11.480  0.64 12.39 ?  11  LYS   A N    1 
ATOM   209  N  N    B LYS   A 1 11  ? 9.136  -14.363 12.002  0.36 12.77 ?  11  LYS   A N    1 
ATOM   210  C  CA   A LYS   A 1 11  ? 10.218 -15.715 11.147  0.64 12.65 ?  11  LYS   A CA   1 
ATOM   211  C  CA   B LYS   A 1 11  ? 10.104 -15.375 11.602  0.36 12.70 ?  11  LYS   A CA   1 
ATOM   212  C  C    A LYS   A 1 11  ? 9.872  -16.314 9.792   0.64 12.53 ?  11  LYS   A C    1 
ATOM   213  C  C    B LYS   A 1 11  ? 9.727  -15.911 10.225  0.36 11.93 ?  11  LYS   A C    1 
ATOM   214  O  O    A LYS   A 1 11  ? 8.811  -16.922 9.637   0.64 14.25 ?  11  LYS   A O    1 
ATOM   215  O  O    B LYS   A 1 11  ? 8.601  -16.381 10.024  0.36 12.24 ?  11  LYS   A O    1 
ATOM   216  C  CB   A LYS   A 1 11  ? 10.240 -16.791 12.231  0.64 13.01 ?  11  LYS   A CB   1 
ATOM   217  C  CB   B LYS   A 1 11  ? 10.135 -16.501 12.634  0.36 13.01 ?  11  LYS   A CB   1 
ATOM   218  C  CG   A LYS   A 1 11  ? 11.250 -17.905 12.029  0.64 13.48 ?  11  LYS   A CG   1 
ATOM   219  C  CG   B LYS   A 1 11  ? 11.185 -17.581 12.372  0.36 13.33 ?  11  LYS   A CG   1 
ATOM   220  C  CD   A LYS   A 1 11  ? 11.335 -18.739 13.303  0.64 14.58 ?  11  LYS   A CD   1 
ATOM   221  C  CD   B LYS   A 1 11  ? 11.291 -18.553 13.550  0.36 13.99 ?  11  LYS   A CD   1 
ATOM   222  C  CE   A LYS   A 1 11  ? 12.315 -19.892 13.194  0.64 15.00 ?  11  LYS   A CE   1 
ATOM   223  C  CE   B LYS   A 1 11  ? 12.316 -19.664 13.307  0.36 14.26 ?  11  LYS   A CE   1 
ATOM   224  N  NZ   A LYS   A 1 11  ? 13.693 -19.422 12.895  0.64 14.62 ?  11  LYS   A NZ   1 
ATOM   225  N  NZ   B LYS   A 1 11  ? 13.720 -19.162 13.272  0.36 14.02 ?  11  LYS   A NZ   1 
ATOM   226  H  H    A LYS   A 1 11  ? 8.559  -15.018 11.942  0.64 14.85 ?  11  LYS   A H    1 
ATOM   227  H  H    B LYS   A 1 11  ? 8.518  -14.648 12.524  0.36 15.31 ?  11  LYS   A H    1 
ATOM   228  H  HA   A LYS   A 1 11  ? 11.094 -15.306 11.096  0.64 15.16 ?  11  LYS   A HA   1 
ATOM   229  H  HA   B LYS   A 1 11  ? 10.985 -14.972 11.544  0.36 15.23 ?  11  LYS   A HA   1 
ATOM   230  H  HB2  A LYS   A 1 11  ? 10.450 -16.370 13.081  0.64 15.60 ?  11  LYS   A HB2  1 
ATOM   231  H  HB2  B LYS   A 1 11  ? 10.321 -16.112 13.502  0.36 15.59 ?  11  LYS   A HB2  1 
ATOM   232  H  HB3  A LYS   A 1 11  ? 9.367  -17.204 12.281  0.64 15.60 ?  11  LYS   A HB3  1 
ATOM   233  H  HB3  B LYS   A 1 11  ? 9.266  -16.928 12.645  0.36 15.59 ?  11  LYS   A HB3  1 
ATOM   234  H  HG2  A LYS   A 1 11  ? 10.966 -18.482 11.300  0.64 16.16 ?  11  LYS   A HG2  1 
ATOM   235  H  HG2  B LYS   A 1 11  ? 10.933 -18.085 11.583  0.36 15.97 ?  11  LYS   A HG2  1 
ATOM   236  H  HG3  A LYS   A 1 11  ? 12.127 -17.531 11.845  0.64 16.16 ?  11  LYS   A HG3  1 
ATOM   237  H  HG3  B LYS   A 1 11  ? 12.050 -17.163 12.242  0.36 15.97 ?  11  LYS   A HG3  1 
ATOM   238  H  HD2  A LYS   A 1 11  ? 11.622 -18.170 14.034  0.64 17.48 ?  11  LYS   A HD2  1 
ATOM   239  H  HD2  B LYS   A 1 11  ? 11.563 -18.065 14.343  0.36 16.78 ?  11  LYS   A HD2  1 
ATOM   240  H  HD3  A LYS   A 1 11  ? 10.458 -19.109 13.496  0.64 17.48 ?  11  LYS   A HD3  1 
ATOM   241  H  HD3  B LYS   A 1 11  ? 10.428 -18.971 13.697  0.36 16.78 ?  11  LYS   A HD3  1 
ATOM   242  H  HE2  A LYS   A 1 11  ? 12.336 -20.375 14.035  0.64 17.99 ?  11  LYS   A HE2  1 
ATOM   243  H  HE2  B LYS   A 1 11  ? 12.254 -20.320 14.020  0.36 17.10 ?  11  LYS   A HE2  1 
ATOM   244  H  HE3  A LYS   A 1 11  ? 12.034 -20.481 12.477  0.64 17.99 ?  11  LYS   A HE3  1 
ATOM   245  H  HE3  B LYS   A 1 11  ? 12.132 -20.088 12.453  0.36 17.10 ?  11  LYS   A HE3  1 
ATOM   246  H  HZ1  A LYS   A 1 11  ? 14.248 -20.117 12.849  0.64 17.52 ?  11  LYS   A HZ1  1 
ATOM   247  H  HZ1  B LYS   A 1 11  ? 14.283 -19.836 13.118  0.36 16.81 ?  11  LYS   A HZ1  1 
ATOM   248  H  HZ2  A LYS   A 1 11  ? 13.705 -18.991 12.117  0.64 17.52 ?  11  LYS   A HZ2  1 
ATOM   249  H  HZ2  B LYS   A 1 11  ? 13.812 -18.559 12.624  0.36 16.81 ?  11  LYS   A HZ2  1 
ATOM   250  H  HZ3  A LYS   A 1 11  ? 13.972 -18.871 13.536  0.64 17.52 ?  11  LYS   A HZ3  1 
ATOM   251  H  HZ3  B LYS   A 1 11  ? 13.929 -18.785 14.050  0.36 16.81 ?  11  LYS   A HZ3  1 
ATOM   252  N  N    A LEU   A 1 12  ? 10.767 -16.162 8.816   0.64 11.80 ?  12  LEU   A N    1 
ATOM   253  N  N    B LEU   A 1 12  ? 10.652 -15.819 9.271   0.36 12.09 ?  12  LEU   A N    1 
ATOM   254  C  CA   A LEU   A 1 12  ? 10.516 -16.740 7.500   0.64 12.01 ?  12  LEU   A CA   1 
ATOM   255  C  CA   B LEU   A 1 12  ? 10.419 -16.329 7.923   0.36 12.42 ?  12  LEU   A CA   1 
ATOM   256  C  C    A LEU   A 1 12  ? 11.102 -18.141 7.358   0.64 12.21 ?  12  LEU   A C    1 
ATOM   257  C  C    B LEU   A 1 12  ? 10.976 -17.733 7.729   0.36 12.33 ?  12  LEU   A C    1 
ATOM   258  O  O    A LEU   A 1 12  ? 10.473 -19.013 6.750   0.64 12.54 ?  12  LEU   A O    1 
ATOM   259  O  O    B LEU   A 1 12  ? 10.299 -18.600 7.168   0.36 12.39 ?  12  LEU   A O    1 
ATOM   260  C  CB   A LEU   A 1 12  ? 11.075 -15.842 6.394   0.64 12.11 ?  12  LEU   A CB   1 
ATOM   261  C  CB   B LEU   A 1 12  ? 11.016 -15.379 6.876   0.36 13.30 ?  12  LEU   A CB   1 
ATOM   262  C  CG   A LEU   A 1 12  ? 10.426 -14.469 6.214   0.64 13.11 ?  12  LEU   A CG   1 
ATOM   263  C  CG   B LEU   A 1 12  ? 10.345 -14.011 6.747   0.36 13.80 ?  12  LEU   A CG   1 
ATOM   264  C  CD1  A LEU   A 1 12  ? 11.173 -13.698 5.148   0.64 13.84 ?  12  LEU   A CD1  1 
ATOM   265  C  CD1  B LEU   A 1 12  ? 10.941 -13.219 5.588   0.36 14.20 ?  12  LEU   A CD1  1 
ATOM   266  C  CD2  A LEU   A 1 12  ? 8.953  -14.607 5.853   0.64 14.11 ?  12  LEU   A CD2  1 
ATOM   267  C  CD2  B LEU   A 1 12  ? 8.842  -14.166 6.578   0.36 14.17 ?  12  LEU   A CD2  1 
ATOM   268  H  H    A LEU   A 1 12  ? 11.522 -15.744 8.892   0.64 14.15 ?  12  LEU   A H    1 
ATOM   269  H  H    B LEU   A 1 12  ? 11.427 -15.453 9.378   0.36 14.49 ?  12  LEU   A H    1 
ATOM   270  H  HA   A LEU   A 1 12  ? 9.562  -16.817 7.375   0.64 14.39 ?  12  LEU   A HA   1 
ATOM   271  H  HA   B LEU   A 1 12  ? 9.463  -16.373 7.773   0.36 14.89 ?  12  LEU   A HA   1 
ATOM   272  H  HB2  A LEU   A 1 12  ? 12.015 -15.695 6.575   0.64 14.51 ?  12  LEU   A HB2  1 
ATOM   273  H  HB2  B LEU   A 1 12  ? 11.946 -15.220 7.097   0.36 15.94 ?  12  LEU   A HB2  1 
ATOM   274  H  HB3  A LEU   A 1 12  ? 10.983 -16.318 5.553   0.64 14.51 ?  12  LEU   A HB3  1 
ATOM   275  H  HB3  B LEU   A 1 12  ? 10.959 -15.805 6.007   0.36 15.94 ?  12  LEU   A HB3  1 
ATOM   276  H  HG   A LEU   A 1 12  ? 10.487 -13.979 7.046   0.64 15.71 ?  12  LEU   A HG   1 
ATOM   277  H  HG   B LEU   A 1 12  ? 10.502 -13.504 7.560   0.36 16.55 ?  12  LEU   A HG   1 
ATOM   278  H  HD11 A LEU   A 1 12  ? 10.757 -12.830 5.036   0.64 16.59 ?  12  LEU   A HD11 1 
ATOM   279  H  HD11 B LEU   A 1 12  ? 10.501 -12.354 5.536   0.36 17.02 ?  12  LEU   A HD11 1 
ATOM   280  H  HD12 A LEU   A 1 12  ? 12.097 -13.589 5.426   0.64 16.59 ?  12  LEU   A HD12 1 
ATOM   281  H  HD12 B LEU   A 1 12  ? 11.890 -13.098 5.743   0.36 17.02 ?  12  LEU   A HD12 1 
ATOM   282  H  HD13 A LEU   A 1 12  ? 11.138 -14.192 4.313   0.64 16.59 ?  12  LEU   A HD13 1 
ATOM   283  H  HD13 B LEU   A 1 12  ? 10.799 -13.711 4.765   0.36 17.02 ?  12  LEU   A HD13 1 
ATOM   284  H  HD21 A LEU   A 1 12  ? 8.592  -13.731 5.651   0.64 16.91 ?  12  LEU   A HD21 1 
ATOM   285  H  HD21 B LEU   A 1 12  ? 8.472  -13.331 6.255   0.36 16.98 ?  12  LEU   A HD21 1 
ATOM   286  H  HD22 A LEU   A 1 12  ? 8.869  -15.184 5.076   0.64 16.91 ?  12  LEU   A HD22 1 
ATOM   287  H  HD22 B LEU   A 1 12  ? 8.670  -14.876 5.942   0.36 16.98 ?  12  LEU   A HD22 1 
ATOM   288  H  HD23 A LEU   A 1 12  ? 8.474  -14.997 6.603   0.64 16.91 ?  12  LEU   A HD23 1 
ATOM   289  H  HD23 B LEU   A 1 12  ? 8.451  -14.390 7.438   0.36 16.98 ?  12  LEU   A HD23 1 
ATOM   290  N  N    A THR   A 1 13  ? 12.307 -18.355 7.881   0.64 12.48 ?  13  THR   A N    1 
ATOM   291  N  N    B THR   A 1 13  ? 12.210 -17.968 8.167   0.36 12.34 ?  13  THR   A N    1 
ATOM   292  C  CA   A THR   A 1 13  ? 13.009 -19.633 7.809   0.64 13.25 ?  13  THR   A CA   1 
ATOM   293  C  CA   B THR   A 1 13  ? 12.845 -19.269 8.033   0.36 12.65 ?  13  THR   A CA   1 
ATOM   294  C  C    A THR   A 1 13  ? 13.765 -19.825 9.117   0.64 13.88 ?  13  THR   A C    1 
ATOM   295  C  C    B THR   A 1 13  ? 13.625 -19.561 9.306   0.36 13.53 ?  13  THR   A C    1 
ATOM   296  O  O    A THR   A 1 13  ? 13.654 -19.022 10.047  0.64 13.91 ?  13  THR   A O    1 
ATOM   297  O  O    B THR   A 1 13  ? 13.534 -18.844 10.308  0.36 13.87 ?  13  THR   A O    1 
ATOM   298  C  CB   A THR   A 1 13  ? 13.996 -19.688 6.632   0.64 14.22 ?  13  THR   A CB   1 
ATOM   299  C  CB   B THR   A 1 13  ? 13.790 -19.320 6.824   0.36 12.95 ?  13  THR   A CB   1 
ATOM   300  O  OG1  A THR   A 1 13  ? 15.070 -18.774 6.871   0.64 14.79 ?  13  THR   A OG1  1 
ATOM   301  O  OG1  B THR   A 1 13  ? 14.864 -18.397 7.032   0.36 13.03 ?  13  THR   A OG1  1 
ATOM   302  C  CG2  A THR   A 1 13  ? 13.323 -19.348 5.315   0.64 15.11 ?  13  THR   A CG2  1 
ATOM   303  C  CG2  B THR   A 1 13  ? 13.067 -18.982 5.524   0.36 13.14 ?  13  THR   A CG2  1 
ATOM   304  H  H    A THR   A 1 13  ? 12.759 -17.757 8.294   0.64 14.96 ?  13  THR   A H    1 
ATOM   305  H  H    B THR   A 1 13  ? 12.708 -17.369 8.539   0.36 14.79 ?  13  THR   A H    1 
ATOM   306  H  HA   A THR   A 1 13  ? 12.369 -20.361 7.705   0.64 15.88 ?  13  THR   A HA   1 
ATOM   307  H  HA   B THR   A 1 13  ? 12.162 -19.947 7.921   0.36 15.16 ?  13  THR   A HA   1 
ATOM   308  H  HB   A THR   A 1 13  ? 14.360 -20.588 6.557   0.64 17.04 ?  13  THR   A HB   1 
ATOM   309  H  HB   B THR   A 1 13  ? 14.154 -20.213 6.738   0.36 15.53 ?  13  THR   A HB   1 
ATOM   310  H  HG1  A THR   A 1 13  ? 15.612 -18.792 6.225   0.64 17.74 ?  13  THR   A HG1  1 
ATOM   311  H  HG1  B THR   A 1 13  ? 15.388 -18.411 6.372   0.36 15.62 ?  13  THR   A HG1  1 
ATOM   312  H  HG21 A THR   A 1 13  ? 13.925 -19.537 4.577   0.64 18.11 ?  13  THR   A HG21 1 
ATOM   313  H  HG21 B THR   A 1 13  ? 13.678 -19.073 4.773   0.36 15.75 ?  13  THR   A HG21 1 
ATOM   314  H  HG22 A THR   A 1 13  ? 12.520 -19.882 5.207   0.64 18.11 ?  13  THR   A HG22 1 
ATOM   315  H  HG22 B THR   A 1 13  ? 12.321 -19.591 5.393   0.36 15.75 ?  13  THR   A HG22 1 
ATOM   316  H  HG23 A THR   A 1 13  ? 13.084 -18.410 5.298   0.64 18.11 ?  13  THR   A HG23 1 
ATOM   317  H  HG23 B THR   A 1 13  ? 12.734 -18.075 5.552   0.36 15.75 ?  13  THR   A HG23 1 
ATOM   318  N  N    A ASP   A 1 14  ? 14.580 -20.879 9.176   0.64 14.66 ?  14  ASP   A N    1 
ATOM   319  N  N    B ASP   A 1 14  ? 14.418 -20.628 9.235   0.36 14.37 ?  14  ASP   A N    1 
ATOM   320  C  CA   A ASP   A 1 14  ? 15.395 -21.108 10.362  0.64 16.00 ?  14  ASP   A CA   1 
ATOM   321  C  CA   B ASP   A 1 14  ? 15.296 -21.005 10.333  0.36 15.33 ?  14  ASP   A CA   1 
ATOM   322  C  C    A ASP   A 1 14  ? 16.176 -19.861 10.761  0.64 15.56 ?  14  ASP   A C    1 
ATOM   323  C  C    B ASP   A 1 14  ? 16.250 -19.880 10.711  0.36 14.49 ?  14  ASP   A C    1 
ATOM   324  O  O    A ASP   A 1 14  ? 16.292 -19.545 11.952  0.64 15.79 ?  14  ASP   A O    1 
ATOM   325  O  O    B ASP   A 1 14  ? 16.691 -19.810 11.864  0.36 14.37 ?  14  ASP   A O    1 
ATOM   326  C  CB   A ASP   A 1 14  ? 16.365 -22.259 10.111  0.64 18.06 ?  14  ASP   A CB   1 
ATOM   327  C  CB   B ASP   A 1 14  ? 16.082 -22.254 9.932   0.36 17.21 ?  14  ASP   A CB   1 
ATOM   328  C  CG   A ASP   A 1 14  ? 17.293 -22.481 11.276  0.64 21.48 ?  14  ASP   A CG   1 
ATOM   329  C  CG   B ASP   A 1 14  ? 17.036 -22.720 11.016  0.36 18.77 ?  14  ASP   A CG   1 
ATOM   330  O  OD1  A ASP   A 1 14  ? 16.824 -22.942 12.338  0.64 23.49 ?  14  ASP   A OD1  1 
ATOM   331  O  OD1  B ASP   A 1 14  ? 16.557 -23.024 12.131  0.36 19.61 ?  14  ASP   A OD1  1 
ATOM   332  O  OD2  A ASP   A 1 14  ? 18.490 -22.165 11.131  0.64 23.39 -1 14  ASP   A OD2  1 
ATOM   333  O  OD2  B ASP   A 1 14  ? 18.254 -22.803 10.749  0.36 19.79 -1 14  ASP   A OD2  1 
ATOM   334  H  H    A ASP   A 1 14  ? 14.687 -21.471 8.552   0.64 17.58 ?  14  ASP   A H    1 
ATOM   335  H  H    B ASP   A 1 14  ? 14.456 -21.144 8.557   0.36 17.22 ?  14  ASP   A H    1 
ATOM   336  H  HA   A ASP   A 1 14  ? 14.823 -21.362 11.104  0.64 19.19 ?  14  ASP   A HA   1 
ATOM   337  H  HA   B ASP   A 1 14  ? 14.759 -21.217 11.110  0.36 18.38 ?  14  ASP   A HA   1 
ATOM   338  H  HB2  A ASP   A 1 14  ? 15.857 -23.079 9.950   0.64 21.65 ?  14  ASP   A HB2  1 
ATOM   339  H  HB2  B ASP   A 1 14  ? 15.453 -22.978 9.761   0.36 20.63 ?  14  ASP   A HB2  1 
ATOM   340  H  HB3  A ASP   A 1 14  ? 16.912 -22.061 9.336   0.64 21.65 ?  14  ASP   A HB3  1 
ATOM   341  H  HB3  B ASP   A 1 14  ? 16.587 -22.063 9.125   0.36 20.63 ?  14  ASP   A HB3  1 
ATOM   342  N  N    A ASN   A 1 15  ? 16.719 -19.136 9.782   0.64 14.96 ?  15  ASN   A N    1 
ATOM   343  N  N    B ASN   A 1 15  ? 16.575 -18.983 9.771   0.36 13.85 ?  15  ASN   A N    1 
ATOM   344  C  CA   A ASN   A 1 15  ? 17.685 -18.081 10.058  0.64 15.62 ?  15  ASN   A CA   1 
ATOM   345  C  CA   B ASN   A 1 15  ? 17.584 -17.962 10.026  0.36 14.14 ?  15  ASN   A CA   1 
ATOM   346  C  C    A ASN   A 1 15  ? 17.317 -16.709 9.508   0.64 15.69 ?  15  ASN   A C    1 
ATOM   347  C  C    B ASN   A 1 15  ? 17.210 -16.548 9.595   0.36 14.28 ?  15  ASN   A C    1 
ATOM   348  O  O    A ASN   A 1 15  ? 18.094 -15.772 9.716   0.64 16.80 ?  15  ASN   A O    1 
ATOM   349  O  O    B ASN   A 1 15  ? 17.979 -15.624 9.879   0.36 15.38 ?  15  ASN   A O    1 
ATOM   350  C  CB   A ASN   A 1 15  ? 19.066 -18.470 9.505   0.64 15.50 ?  15  ASN   A CB   1 
ATOM   351  C  CB   B ASN   A 1 15  ? 18.946 -18.353 9.412   0.36 13.98 ?  15  ASN   A CB   1 
ATOM   352  C  CG   A ASN   A 1 15  ? 19.066 -18.591 7.995   0.64 15.90 ?  15  ASN   A CG   1 
ATOM   353  C  CG   B ASN   A 1 15  ? 18.917 -18.441 7.893   0.36 14.19 ?  15  ASN   A CG   1 
ATOM   354  O  OD1  A ASN   A 1 15  ? 18.309 -19.378 7.425   0.64 17.09 ?  15  ASN   A OD1  1 
ATOM   355  O  OD1  B ASN   A 1 15  ? 18.249 -19.306 7.321   0.36 15.09 ?  15  ASN   A OD1  1 
ATOM   356  N  ND2  A ASN   A 1 15  ? 19.897 -17.792 7.335   0.64 15.69 ?  15  ASN   A ND2  1 
ATOM   357  N  ND2  B ASN   A 1 15  ? 19.672 -17.560 7.232   0.36 13.69 ?  15  ASN   A ND2  1 
ATOM   358  H  H    A ASN   A 1 15  ? 16.554 -19.249 8.951   0.64 17.93 ?  15  ASN   A H    1 
ATOM   359  H  H    B ASN   A 1 15  ? 16.214 -18.940 8.991   0.36 16.60 ?  15  ASN   A H    1 
ATOM   360  H  HA   A ASN   A 1 15  ? 17.783 -17.992 11.019  0.64 18.73 ?  15  ASN   A HA   1 
ATOM   361  H  HA   B ASN   A 1 15  ? 17.725 -17.923 10.980  0.36 16.95 ?  15  ASN   A HA   1 
ATOM   362  H  HB2  A ASN   A 1 15  ? 19.715 -17.783 9.755   0.64 18.58 ?  15  ASN   A HB2  1 
ATOM   363  H  HB2  B ASN   A 1 15  ? 19.608 -17.683 9.659   0.36 16.76 ?  15  ASN   A HB2  1 
ATOM   364  H  HB3  A ASN   A 1 15  ? 19.340 -19.324 9.880   0.64 18.58 ?  15  ASN   A HB3  1 
ATOM   365  H  HB3  B ASN   A 1 15  ? 19.212 -19.218 9.756   0.36 16.76 ?  15  ASN   A HB3  1 
ATOM   366  H  HD21 A ASN   A 1 15  ? 19.924 -17.825 6.477   0.64 18.81 ?  15  ASN   A HD21 1 
ATOM   367  H  HD21 B ASN   A 1 15  ? 19.702 -17.572 6.370   0.36 16.41 ?  15  ASN   A HD21 1 
ATOM   368  H  HD22 A ASN   A 1 15  ? 20.414 -17.252 7.762   0.64 18.81 ?  15  ASN   A HD22 1 
ATOM   369  H  HD22 B ASN   A 1 15  ? 20.130 -16.971 7.664   0.36 16.41 ?  15  ASN   A HD22 1 
ATOM   370  N  N    A VAL   A 1 16  ? 16.197 -16.551 8.800   0.64 15.36 ?  16  VAL   A N    1 
ATOM   371  N  N    B VAL   A 1 16  ? 16.059 -16.339 8.959   0.36 13.69 ?  16  VAL   A N    1 
ATOM   372  C  CA   A VAL   A 1 16  ? 15.810 -15.270 8.210   0.64 14.63 ?  16  VAL   A CA   1 
ATOM   373  C  CA   B VAL   A 1 16  ? 15.681 -15.047 8.396   0.36 13.41 ?  16  VAL   A CA   1 
ATOM   374  C  C    A VAL   A 1 16  ? 14.521 -14.768 8.851   0.64 13.77 ?  16  VAL   A C    1 
ATOM   375  C  C    B VAL   A 1 16  ? 14.436 -14.538 9.116   0.36 13.21 ?  16  VAL   A C    1 
ATOM   376  O  O    A VAL   A 1 16  ? 13.512 -15.485 8.898   0.64 13.33 ?  16  VAL   A O    1 
ATOM   377  O  O    B VAL   A 1 16  ? 13.464 -15.283 9.300   0.36 13.14 ?  16  VAL   A O    1 
ATOM   378  C  CB   A VAL   A 1 16  ? 15.663 -15.345 6.680   0.64 15.03 ?  16  VAL   A CB   1 
ATOM   379  C  CB   B VAL   A 1 16  ? 15.457 -15.148 6.875   0.36 13.67 ?  16  VAL   A CB   1 
ATOM   380  C  CG1  A VAL   A 1 16  ? 15.225 -13.992 6.132   0.64 15.90 ?  16  VAL   A CG1  1 
ATOM   381  C  CG1  B VAL   A 1 16  ? 15.082 -13.791 6.278   0.36 14.12 ?  16  VAL   A CG1  1 
ATOM   382  C  CG2  A VAL   A 1 16  ? 16.966 -15.778 6.034   0.64 15.47 ?  16  VAL   A CG2  1 
ATOM   383  C  CG2  B VAL   A 1 16  ? 16.697 -15.722 6.186   0.36 14.15 ?  16  VAL   A CG2  1 
ATOM   384  H  H    A VAL   A 1 16  ? 15.648 -17.196 8.641   0.64 18.42 ?  16  VAL   A H    1 
ATOM   385  H  H    B VAL   A 1 16  ? 15.462 -16.945 8.842   0.36 16.41 ?  16  VAL   A H    1 
ATOM   386  H  HA   A VAL   A 1 16  ? 16.510 -14.627 8.400   0.64 17.54 ?  16  VAL   A HA   1 
ATOM   387  H  HA   B VAL   A 1 16  ? 16.391 -14.407 8.552   0.36 16.07 ?  16  VAL   A HA   1 
ATOM   388  H  HB   A VAL   A 1 16  ? 14.985 -16.002 6.456   0.64 18.02 ?  16  VAL   A HB   1 
ATOM   389  H  HB   B VAL   A 1 16  ? 14.723 -15.756 6.710   0.36 16.39 ?  16  VAL   A HB   1 
ATOM   390  H  HG11 A VAL   A 1 16  ? 15.354 -13.986 5.173   0.64 19.06 ?  16  VAL   A HG11 1 
ATOM   391  H  HG11 B VAL   A 1 16  ? 15.089 -13.864 5.309   0.36 16.93 ?  16  VAL   A HG11 1 
ATOM   392  H  HG12 A VAL   A 1 16  ? 14.287 -13.856 6.341   0.64 19.06 ?  16  VAL   A HG12 1 
ATOM   393  H  HG12 B VAL   A 1 16  ? 14.195 -13.545 6.582   0.36 16.93 ?  16  VAL   A HG12 1 
ATOM   394  H  HG13 A VAL   A 1 16  ? 15.763 -13.299 6.545   0.64 19.06 ?  16  VAL   A HG13 1 
ATOM   395  H  HG13 B VAL   A 1 16  ? 15.729 -13.129 6.562   0.36 16.93 ?  16  VAL   A HG13 1 
ATOM   396  H  HG21 A VAL   A 1 16  ? 16.873 -15.723 5.071   0.64 18.55 ?  16  VAL   A HG21 1 
ATOM   397  H  HG21 B VAL   A 1 16  ? 16.564 -15.702 5.225   0.36 16.97 ?  16  VAL   A HG21 1 
ATOM   398  H  HG22 A VAL   A 1 16  ? 17.675 -15.187 6.332   0.64 18.55 ?  16  VAL   A HG22 1 
ATOM   399  H  HG22 B VAL   A 1 16  ? 17.471 -15.185 6.422   0.36 16.97 ?  16  VAL   A HG22 1 
ATOM   400  H  HG23 A VAL   A 1 16  ? 17.163 -16.688 6.299   0.64 18.55 ?  16  VAL   A HG23 1 
ATOM   401  H  HG23 B VAL   A 1 16  ? 16.831 -16.637 6.481   0.36 16.97 ?  16  VAL   A HG23 1 
ATOM   402  N  N    A TYR   A 1 17  ? 14.555 -13.510 9.284   0.64 13.47 ?  17  TYR   A N    1 
ATOM   403  N  N    B TYR   A 1 17  ? 14.471 -13.261 9.506   0.36 13.11 ?  17  TYR   A N    1 
ATOM   404  C  CA   A TYR   A 1 17  ? 13.452 -12.817 9.934   0.64 12.93 ?  17  TYR   A CA   1 
ATOM   405  C  CA   B TYR   A 1 17  ? 13.428 -12.611 10.288  0.36 12.32 ?  17  TYR   A CA   1 
ATOM   406  C  C    A TYR   A 1 17  ? 13.188 -11.505 9.202   0.64 12.52 ?  17  TYR   A C    1 
ATOM   407  C  C    B TYR   A 1 17  ? 13.168 -11.243 9.673   0.36 11.64 ?  17  TYR   A C    1 
ATOM   408  O  O    A TYR   A 1 17  ? 14.088 -10.948 8.570   0.64 12.13 ?  17  TYR   A O    1 
ATOM   409  O  O    B TYR   A 1 17  ? 14.086 -10.634 9.123   0.36 11.49 ?  17  TYR   A O    1 
ATOM   410  C  CB   A TYR   A 1 17  ? 13.829 -12.512 11.386  0.64 13.67 ?  17  TYR   A CB   1 
ATOM   411  C  CB   B TYR   A 1 17  ? 13.901 -12.445 11.739  0.36 13.06 ?  17  TYR   A CB   1 
ATOM   412  C  CG   A TYR   A 1 17  ? 13.988 -13.748 12.240  0.64 15.03 ?  17  TYR   A CG   1 
ATOM   413  C  CG   B TYR   A 1 17  ? 14.182 -13.755 12.459  0.36 13.88 ?  17  TYR   A CG   1 
ATOM   414  C  CD1  A TYR   A 1 17  ? 15.161 -14.498 12.218  0.64 15.92 ?  17  TYR   A CD1  1 
ATOM   415  C  CD1  B TYR   A 1 17  ? 15.380 -14.448 12.273  0.36 14.47 ?  17  TYR   A CD1  1 
ATOM   416  C  CD2  A TYR   A 1 17  ? 12.956 -14.180 13.061  0.64 15.15 ?  17  TYR   A CD2  1 
ATOM   417  C  CD2  B TYR   A 1 17  ? 13.249 -14.295 13.332  0.36 14.06 ?  17  TYR   A CD2  1 
ATOM   418  C  CE1  A TYR   A 1 17  ? 15.298 -15.646 12.992  0.64 15.95 ?  17  TYR   A CE1  1 
ATOM   419  C  CE1  B TYR   A 1 17  ? 15.626 -15.649 12.935  0.36 15.00 ?  17  TYR   A CE1  1 
ATOM   420  C  CE2  A TYR   A 1 17  ? 13.084 -15.326 13.841  0.64 15.62 ?  17  TYR   A CE2  1 
ATOM   421  C  CE2  B TYR   A 1 17  ? 13.487 -15.488 13.996  0.36 14.34 ?  17  TYR   A CE2  1 
ATOM   422  C  CZ   A TYR   A 1 17  ? 14.259 -16.053 13.806  0.64 15.81 ?  17  TYR   A CZ   1 
ATOM   423  C  CZ   B TYR   A 1 17  ? 14.673 -16.161 13.796  0.36 14.71 ?  17  TYR   A CZ   1 
ATOM   424  O  OH   A TYR   A 1 17  ? 14.388 -17.191 14.579  0.64 16.20 ?  17  TYR   A OH   1 
ATOM   425  O  OH   B TYR   A 1 17  ? 14.900 -17.345 14.464  0.36 15.01 ?  17  TYR   A OH   1 
ATOM   426  H  H    A TYR   A 1 17  ? 15.254 -13.026 9.205   0.64 16.15 ?  17  TYR   A H    1 
ATOM   427  H  H    B TYR   A 1 17  ? 15.118 -12.721 9.311   0.36 15.72 ?  17  TYR   A H    1 
ATOM   428  H  HA   A TYR   A 1 17  ? 12.656 -13.383 9.917   0.64 15.50 ?  17  TYR   A HA   1 
ATOM   429  H  HA   B TYR   A 1 17  ? 12.608 -13.126 10.264  0.36 14.77 ?  17  TYR   A HA   1 
ATOM   430  H  HB2  A TYR   A 1 17  ? 14.671 -12.037 11.397  0.64 16.38 ?  17  TYR   A HB2  1 
ATOM   431  H  HB2  B TYR   A 1 17  ? 14.721 -11.927 11.737  0.36 15.65 ?  17  TYR   A HB2  1 
ATOM   432  H  HB3  A TYR   A 1 17  ? 13.134 -11.973 11.776  0.64 16.38 ?  17  TYR   A HB3  1 
ATOM   433  H  HB3  B TYR   A 1 17  ? 13.217 -11.975 12.237  0.36 15.65 ?  17  TYR   A HB3  1 
ATOM   434  H  HD1  A TYR   A 1 17  ? 15.867 -14.230 11.671  0.64 19.09 ?  17  TYR   A HD1  1 
ATOM   435  H  HD1  B TYR   A 1 17  ? 16.023 -14.111 11.690  0.36 17.35 ?  17  TYR   A HD1  1 
ATOM   436  H  HD2  A TYR   A 1 17  ? 12.161 -13.700 13.090  0.64 18.16 ?  17  TYR   A HD2  1 
ATOM   437  H  HD2  B TYR   A 1 17  ? 12.446 -13.849 13.469  0.36 16.86 ?  17  TYR   A HD2  1 
ATOM   438  H  HE1  A TYR   A 1 17  ? 16.094 -16.134 12.967  0.64 19.12 ?  17  TYR   A HE1  1 
ATOM   439  H  HE1  B TYR   A 1 17  ? 16.430 -16.106 12.805  0.36 17.99 ?  17  TYR   A HE1  1 
ATOM   440  H  HE2  A TYR   A 1 17  ? 12.382 -15.601 14.386  0.64 18.73 ?  17  TYR   A HE2  1 
ATOM   441  H  HE2  B TYR   A 1 17  ? 12.849 -15.833 14.578  0.36 17.19 ?  17  TYR   A HE2  1 
ATOM   442  H  HH   A TYR   A 1 17  ? 13.633 -17.432 14.855  0.64 19.42 ?  17  TYR   A HH   1 
ATOM   443  H  HH   B TYR   A 1 17  ? 15.631 -17.683 14.223  0.36 18.00 ?  17  TYR   A HH   1 
ATOM   444  N  N    A ILE   A 1 18  ? 11.959 -10.985 9.305   0.64 12.38 ?  18  ILE   A N    1 
ATOM   445  N  N    B ILE   A 1 18  ? 11.928 -10.745 9.761   0.36 11.54 ?  18  ILE   A N    1 
ATOM   446  C  CA   A ILE   A 1 18  ? 11.575 -9.798  8.541   0.64 12.25 ?  18  ILE   A CA   1 
ATOM   447  C  CA   B ILE   A 1 18  ? 11.550 -9.537  9.026   0.36 11.12 ?  18  ILE   A CA   1 
ATOM   448  C  C    A ILE   A 1 18  ? 10.597 -8.941  9.338   0.64 12.67 ?  18  ILE   A C    1 
ATOM   449  C  C    B ILE   A 1 18  ? 10.628 -8.652  9.859   0.36 11.28 ?  18  ILE   A C    1 
ATOM   450  O  O    A ILE   A 1 18  ? 9.775  -9.452  10.099  0.64 13.17 ?  18  ILE   A O    1 
ATOM   451  O  O    B ILE   A 1 18  ? 9.773  -9.145  10.604  0.36 11.84 ?  18  ILE   A O    1 
ATOM   452  C  CB   A ILE   A 1 18  ? 11.022 -10.209 7.157   0.64 12.33 ?  18  ILE   A CB   1 
ATOM   453  C  CB   B ILE   A 1 18  ? 10.936 -9.886  7.653   0.36 10.63 ?  18  ILE   A CB   1 
ATOM   454  C  CG1  A ILE   A 1 18  ? 10.940 -9.008  6.223   0.64 12.46 ?  18  ILE   A CG1  1 
ATOM   455  C  CG1  B ILE   A 1 18  ? 10.909 -8.659  6.740   0.36 11.68 ?  18  ILE   A CG1  1 
ATOM   456  C  CG2  A ILE   A 1 18  ? 9.684  -10.927 7.311   0.64 12.27 ?  18  ILE   A CG2  1 
ATOM   457  C  CG2  B ILE   A 1 18  ? 9.543  -10.481 7.814   0.36 11.14 ?  18  ILE   A CG2  1 
ATOM   458  C  CD1  A ILE   A 1 18  ? 10.741 -9.400  4.781   0.64 14.03 ?  18  ILE   A CD1  1 
ATOM   459  C  CD1  B ILE   A 1 18  ? 10.558 -8.986  5.308   0.36 12.51 ?  18  ILE   A CD1  1 
ATOM   460  H  H    A ILE   A 1 18  ? 11.349 -11.307 9.818   0.64 14.84 ?  18  ILE   A H    1 
ATOM   461  H  H    B ILE   A 1 18  ? 11.294 -11.080 10.239  0.36 13.84 ?  18  ILE   A H    1 
ATOM   462  H  HA   A ILE   A 1 18  ? 12.373 -9.275  8.388   0.64 14.69 ?  18  ILE   A HA   1 
ATOM   463  H  HA   B ILE   A 1 18  ? 12.355 -9.023  8.855   0.36 13.32 ?  18  ILE   A HA   1 
ATOM   464  H  HB   A ILE   A 1 18  ? 11.646 -10.845 6.766   0.64 14.78 ?  18  ILE   A HB   1 
ATOM   465  H  HB   B ILE   A 1 18  ? 11.503 -10.549 7.238   0.36 12.74 ?  18  ILE   A HB   1 
ATOM   466  H  HG12 A ILE   A 1 18  ? 10.197 -8.451  6.492   0.64 14.94 ?  18  ILE   A HG12 1 
ATOM   467  H  HG12 B ILE   A 1 18  ? 10.250 -8.029  7.071   0.36 14.00 ?  18  ILE   A HG12 1 
ATOM   468  H  HG13 A ILE   A 1 18  ? 11.771 -8.508  6.285   0.64 14.94 ?  18  ILE   A HG13 1 
ATOM   469  H  HG13 B ILE   A 1 18  ? 11.789 -8.243  6.740   0.36 14.00 ?  18  ILE   A HG13 1 
ATOM   470  H  HG21 A ILE   A 1 18  ? 9.433  -11.318 6.456   0.64 14.71 ?  18  ILE   A HG21 1 
ATOM   471  H  HG21 B ILE   A 1 18  ? 9.266  -10.867 6.967   0.36 13.35 ?  18  ILE   A HG21 1 
ATOM   472  H  HG22 A ILE   A 1 18  ? 9.772  -11.631 7.976   0.64 14.71 ?  18  ILE   A HG22 1 
ATOM   473  H  HG22 B ILE   A 1 18  ? 9.572  -11.169 8.496   0.36 13.35 ?  18  ILE   A HG22 1 
ATOM   474  H  HG23 A ILE   A 1 18  ? 9.010  -10.291 7.592   0.64 14.71 ?  18  ILE   A HG23 1 
ATOM   475  H  HG23 B ILE   A 1 18  ? 8.923  -9.781  8.075   0.36 13.35 ?  18  ILE   A HG23 1 
ATOM   476  H  HD11 A ILE   A 1 18  ? 10.731 -8.595  4.235   0.64 16.82 ?  18  ILE   A HD11 1 
ATOM   477  H  HD11 B ILE   A 1 18  ? 10.626 -8.182  4.770   0.36 14.99 ?  18  ILE   A HD11 1 
ATOM   478  H  HD12 A ILE   A 1 18  ? 11.466 -9.978  4.503   0.64 16.82 ?  18  ILE   A HD12 1 
ATOM   479  H  HD12 B ILE   A 1 18  ? 11.174 -9.658  4.976   0.36 14.99 ?  18  ILE   A HD12 1 
ATOM   480  H  HD13 A ILE   A 1 18  ? 9.893  -9.864  4.694   0.64 16.82 ?  18  ILE   A HD13 1 
ATOM   481  H  HD13 B ILE   A 1 18  ? 9.650  -9.328  5.275   0.36 14.99 ?  18  ILE   A HD13 1 
ATOM   482  N  N    A LYS   A 1 19  ? 10.680 -7.621  9.140   0.64 12.47 ?  19  LYS   A N    1 
ATOM   483  N  N    B LYS   A 1 19  ? 10.809 -7.333  9.722   0.36 11.48 ?  19  LYS   A N    1 
ATOM   484  C  CA   A LYS   A 1 19  ? 9.865  -6.664  9.882   0.64 13.32 ?  19  LYS   A CA   1 
ATOM   485  C  CA   B LYS   A 1 19  ? 10.021 -6.347  10.449  0.36 12.69 ?  19  LYS   A CA   1 
ATOM   486  C  C    A LYS   A 1 19  ? 9.685  -5.396  9.054   0.64 13.53 ?  19  LYS   A C    1 
ATOM   487  C  C    B LYS   A 1 19  ? 9.805  -5.132  9.561   0.36 13.04 ?  19  LYS   A C    1 
ATOM   488  O  O    A LYS   A 1 19  ? 10.576 -5.010  8.293   0.64 13.56 ?  19  LYS   A O    1 
ATOM   489  O  O    B LYS   A 1 19  ? 10.699 -4.745  8.806   0.36 12.93 ?  19  LYS   A O    1 
ATOM   490  C  CB   A LYS   A 1 19  ? 10.561 -6.316  11.207  0.64 14.70 ?  19  LYS   A CB   1 
ATOM   491  C  CB   B LYS   A 1 19  ? 10.745 -5.918  11.735  0.36 13.30 ?  19  LYS   A CB   1 
ATOM   492  C  CG   A LYS   A 1 19  ? 9.814  -5.363  12.136  0.64 16.09 ?  19  LYS   A CG   1 
ATOM   493  C  CG   B LYS   A 1 19  ? 9.966  -4.981  12.641  0.36 14.70 ?  19  LYS   A CG   1 
ATOM   494  C  CD   A LYS   A 1 19  ? 10.686 -5.065  13.355  0.64 17.43 ?  19  LYS   A CD   1 
ATOM   495  C  CD   B LYS   A 1 19  ? 10.810 -4.577  13.843  0.36 15.83 ?  19  LYS   A CD   1 
ATOM   496  C  CE   A LYS   A 1 19  ? 10.014 -4.157  14.369  0.64 18.47 ?  19  LYS   A CE   1 
ATOM   497  C  CE   B LYS   A 1 19  ? 10.037 -3.696  14.806  0.36 16.94 ?  19  LYS   A CE   1 
ATOM   498  N  NZ   A LYS   A 1 19  ? 10.916 -3.904  15.536  0.64 19.03 ?  19  LYS   A NZ   1 
ATOM   499  N  NZ   B LYS   A 1 19  ? 10.840 -3.375  16.014  0.36 17.63 ?  19  LYS   A NZ   1 
ATOM   500  H  H    A LYS   A 1 19  ? 11.212 -7.262  8.572   0.64 14.95 ?  19  LYS   A H    1 
ATOM   501  H  H    B LYS   A 1 19  ? 11.411 -6.969  9.206   0.36 13.76 ?  19  LYS   A H    1 
ATOM   502  H  HA   A LYS   A 1 19  ? 8.994  -7.059  10.072  0.64 15.96 ?  19  LYS   A HA   1 
ATOM   503  H  HA   B LYS   A 1 19  ? 9.163  -6.720  10.689  0.36 15.22 ?  19  LYS   A HA   1 
ATOM   504  H  HB2  A LYS   A 1 19  ? 10.704 -7.143  11.701  0.64 17.62 ?  19  LYS   A HB2  1 
ATOM   505  H  HB2  B LYS   A 1 19  ? 10.944 -6.709  12.259  0.36 15.95 ?  19  LYS   A HB2  1 
ATOM   506  H  HB3  A LYS   A 1 19  ? 11.414 -5.914  11.001  0.64 17.62 ?  19  LYS   A HB3  1 
ATOM   507  H  HB3  B LYS   A 1 19  ? 11.572 -5.469  11.499  0.36 15.95 ?  19  LYS   A HB3  1 
ATOM   508  H  HG2  A LYS   A 1 19  ? 9.630  -4.530  11.673  0.64 19.29 ?  19  LYS   A HG2  1 
ATOM   509  H  HG2  B LYS   A 1 19  ? 9.729  -4.177  12.155  0.36 17.62 ?  19  LYS   A HG2  1 
ATOM   510  H  HG3  A LYS   A 1 19  ? 8.987  -5.775  12.438  0.64 19.29 ?  19  LYS   A HG3  1 
ATOM   511  H  HG3  B LYS   A 1 19  ? 9.170  -5.429  12.967  0.36 17.62 ?  19  LYS   A HG3  1 
ATOM   512  H  HD2  A LYS   A 1 19  ? 10.902 -5.899  13.801  0.64 20.90 ?  19  LYS   A HD2  1 
ATOM   513  H  HD2  B LYS   A 1 19  ? 11.084 -5.375  14.321  0.36 18.98 ?  19  LYS   A HD2  1 
ATOM   514  H  HD3  A LYS   A 1 19  ? 11.501 -4.629  13.059  0.64 20.90 ?  19  LYS   A HD3  1 
ATOM   515  H  HD3  B LYS   A 1 19  ? 11.589 -4.086  13.536  0.36 18.98 ?  19  LYS   A HD3  1 
ATOM   516  H  HE2  A LYS   A 1 19  ? 9.809  -3.302  13.955  0.64 22.14 ?  19  LYS   A HE2  1 
ATOM   517  H  HE2  B LYS   A 1 19  ? 9.807  -2.866  14.364  0.36 20.32 ?  19  LYS   A HE2  1 
ATOM   518  H  HE3  A LYS   A 1 19  ? 9.203  -4.576  14.695  0.64 22.14 ?  19  LYS   A HE3  1 
ATOM   519  H  HE3  B LYS   A 1 19  ? 9.236  -4.163  15.089  0.36 20.32 ?  19  LYS   A HE3  1 
ATOM   520  H  HZ1  A LYS   A 1 19  ? 10.507 -3.385  16.132  0.64 22.82 ?  19  LYS   A HZ1  1 
ATOM   521  H  HZ1  B LYS   A 1 19  ? 10.367 -2.859  16.564  0.36 21.14 ?  19  LYS   A HZ1  1 
ATOM   522  H  HZ2  A LYS   A 1 19  ? 11.131 -4.676  15.925  0.64 22.82 ?  19  LYS   A HZ2  1 
ATOM   523  H  HZ2  B LYS   A 1 19  ? 11.063 -4.124  16.440  0.36 21.14 ?  19  LYS   A HZ2  1 
ATOM   524  H  HZ3  A LYS   A 1 19  ? 11.660 -3.502  15.264  0.64 22.82 ?  19  LYS   A HZ3  1 
ATOM   525  H  HZ3  B LYS   A 1 19  ? 11.582 -2.944  15.780  0.36 21.14 ?  19  LYS   A HZ3  1 
ATOM   526  N  N    A ASN   A 1 20  ? 8.525  -4.747  9.205   0.64 14.57 ?  20  ASN   A N    1 
ATOM   527  N  N    B ASN   A 1 20  ? 8.617  -4.535  9.646   0.36 14.30 ?  20  ASN   A N    1 
ATOM   528  C  CA   A ASN   A 1 20  ? 8.330  -3.403  8.662   0.64 16.30 ?  20  ASN   A CA   1 
ATOM   529  C  CA   B ASN   A 1 20  ? 8.305  -3.306  8.914   0.36 15.44 ?  20  ASN   A CA   1 
ATOM   530  C  C    A ASN   A 1 20  ? 8.953  -2.411  9.637   0.64 17.11 ?  20  ASN   A C    1 
ATOM   531  C  C    B ASN   A 1 20  ? 8.852  -2.136  9.722   0.36 16.22 ?  20  ASN   A C    1 
ATOM   532  O  O    A ASN   A 1 20  ? 8.447  -2.212  10.747  0.64 17.52 ?  20  ASN   A O    1 
ATOM   533  O  O    B ASN   A 1 20  ? 8.187  -1.604  10.614  0.36 16.76 ?  20  ASN   A O    1 
ATOM   534  C  CB   A ASN   A 1 20  ? 6.842  -3.125  8.439   0.64 17.13 ?  20  ASN   A CB   1 
ATOM   535  C  CB   B ASN   A 1 20  ? 6.795  -3.189  8.708   0.36 15.90 ?  20  ASN   A CB   1 
ATOM   536  C  CG   A ASN   A 1 20  ? 6.536  -1.653  8.136   0.64 18.14 ?  20  ASN   A CG   1 
ATOM   537  C  CG   B ASN   A 1 20  ? 6.389  -1.995  7.832   0.36 16.23 ?  20  ASN   A CG   1 
ATOM   538  O  OD1  A ASN   A 1 20  ? 5.562  -1.101  8.650   0.64 20.21 ?  20  ASN   A OD1  1 
ATOM   539  O  OD1  B ASN   A 1 20  ? 5.231  -1.548  7.866   0.36 16.14 ?  20  ASN   A OD1  1 
ATOM   540  N  ND2  A ASN   A 1 20  ? 7.354  -1.024  7.295   0.64 17.83 ?  20  ASN   A ND2  1 
ATOM   541  N  ND2  B ASN   A 1 20  ? 7.330  -1.484  7.041   0.36 17.11 ?  20  ASN   A ND2  1 
ATOM   542  H  H    A ASN   A 1 20  ? 7.841  -5.073  9.617   0.64 17.47 ?  20  ASN   A H    1 
ATOM   543  H  H    B ASN   A 1 20  ? 7.971  -4.835  10.120  0.36 17.14 ?  20  ASN   A H    1 
ATOM   544  H  HA   A ASN   A 1 20  ? 8.786  -3.338  7.813   0.64 19.54 ?  20  ASN   A HA   1 
ATOM   545  H  HA   B ASN   A 1 20  ? 8.753  -3.330  8.055   0.36 18.51 ?  20  ASN   A HA   1 
ATOM   546  H  HB2  A ASN   A 1 20  ? 6.532  -3.650  7.685   0.64 20.54 ?  20  ASN   A HB2  1 
ATOM   547  H  HB2  B ASN   A 1 20  ? 6.477  -4.000  8.284   0.36 19.06 ?  20  ASN   A HB2  1 
ATOM   548  H  HB3  A ASN   A 1 20  ? 6.350  -3.376  9.236   0.64 20.54 ?  20  ASN   A HB3  1 
ATOM   549  H  HB3  B ASN   A 1 20  ? 6.372  -3.080  9.574   0.36 19.06 ?  20  ASN   A HB3  1 
ATOM   550  H  HD21 A ASN   A 1 20  ? 7.219  -0.200  7.098   0.64 21.38 ?  20  ASN   A HD21 1 
ATOM   551  H  HD21 B ASN   A 1 20  ? 7.140  -0.821  6.536   0.36 20.52 ?  20  ASN   A HD21 1 
ATOM   552  H  HD22 A ASN   A 1 20  ? 8.027  -1.443  6.956   0.64 21.38 ?  20  ASN   A HD22 1 
ATOM   553  H  HD22 B ASN   A 1 20  ? 8.128  -1.810  7.032   0.36 20.52 ?  20  ASN   A HD22 1 
ATOM   554  N  N    A ALA   A 1 21  ? 10.070 -1.805  9.246   0.64 17.28 ?  21  ALA   A N    1 
ATOM   555  N  N    B ALA   A 1 21  ? 10.084 -1.731  9.410   0.36 16.51 ?  21  ALA   A N    1 
ATOM   556  C  CA   A ALA   A 1 21  ? 10.770 -0.926  10.168  0.64 17.02 ?  21  ALA   A CA   1 
ATOM   557  C  CA   B ALA   A 1 21  ? 10.734 -0.664  10.158  0.36 16.56 ?  21  ALA   A CA   1 
ATOM   558  C  C    A ALA   A 1 21  ? 11.719 -0.022  9.403   0.64 16.82 ?  21  ALA   A C    1 
ATOM   559  C  C    B ALA   A 1 21  ? 11.865 -0.073  9.331   0.36 15.89 ?  21  ALA   A C    1 
ATOM   560  O  O    A ALA   A 1 21  ? 12.171 -0.359  8.307   0.64 16.88 ?  21  ALA   A O    1 
ATOM   561  O  O    B ALA   A 1 21  ? 12.407 -0.718  8.432   0.36 15.81 ?  21  ALA   A O    1 
ATOM   562  C  CB   A ALA   A 1 21  ? 11.548 -1.726  11.216  0.64 17.11 ?  21  ALA   A CB   1 
ATOM   563  C  CB   B ALA   A 1 21  ? 11.264 -1.162  11.509  0.36 17.13 ?  21  ALA   A CB   1 
ATOM   564  H  H    A ALA   A 1 21  ? 10.431 -1.889  8.471   0.64 20.72 ?  21  ALA   A H    1 
ATOM   565  H  H    B ALA   A 1 21  ? 10.562 -2.056  8.770   0.36 19.80 ?  21  ALA   A H    1 
ATOM   566  H  HA   A ALA   A 1 21  ? 10.121 -0.371  10.629  0.64 20.41 ?  21  ALA   A HA   1 
ATOM   567  H  HA   B ALA   A 1 21  ? 10.090 0.038   10.330  0.36 19.86 ?  21  ALA   A HA   1 
ATOM   568  H  HB1  A ALA   A 1 21  ? 11.978 -1.108  11.824  0.64 20.51 ?  21  ALA   A HB1  1 
ATOM   569  H  HB1  B ALA   A 1 21  ? 11.687 -0.421  11.976  0.36 20.54 ?  21  ALA   A HB1  1 
ATOM   570  H  HB2  A ALA   A 1 21  ? 10.926 -2.292  11.704  0.64 20.51 ?  21  ALA   A HB2  1 
ATOM   571  H  HB2  B ALA   A 1 21  ? 10.523 -1.501  12.036  0.36 20.54 ?  21  ALA   A HB2  1 
ATOM   572  H  HB3  A ALA   A 1 21  ? 12.210 -2.273  10.768  0.64 20.51 ?  21  ALA   A HB3  1 
ATOM   573  H  HB3  B ALA   A 1 21  ? 11.912 -1.867  11.358  0.36 20.54 ?  21  ALA   A HB3  1 
ATOM   574  N  N    A ASP   A 1 22  ? 11.993 1.139   10.001  0.64 16.77 ?  22  ASP   A N    1 
ATOM   575  N  N    B ASP   A 1 22  ? 12.188 1.181   9.642   0.36 15.58 ?  22  ASP   A N    1 
ATOM   576  C  CA   A ASP   A 1 22  ? 13.035 2.049   9.538   0.64 16.82 ?  22  ASP   A CA   1 
ATOM   577  C  CA   B ASP   A 1 22  ? 13.391 1.824   9.127   0.36 15.62 ?  22  ASP   A CA   1 
ATOM   578  C  C    A ASP   A 1 22  ? 14.361 1.558   10.110  0.64 15.54 ?  22  ASP   A C    1 
ATOM   579  C  C    B ASP   A 1 22  ? 14.610 1.181   9.781   0.36 14.48 ?  22  ASP   A C    1 
ATOM   580  O  O    A ASP   A 1 22  ? 14.557 1.561   11.330  0.64 16.01 ?  22  ASP   A O    1 
ATOM   581  O  O    B ASP   A 1 22  ? 14.683 1.077   11.010  0.36 14.70 ?  22  ASP   A O    1 
ATOM   582  C  CB   A ASP   A 1 22  ? 12.710 3.462   10.017  0.64 18.88 ?  22  ASP   A CB   1 
ATOM   583  C  CB   B ASP   A 1 22  ? 13.333 3.316   9.476   0.36 16.97 ?  22  ASP   A CB   1 
ATOM   584  C  CG   A ASP   A 1 22  ? 13.731 4.492   9.558   0.64 20.99 ?  22  ASP   A CG   1 
ATOM   585  C  CG   B ASP   A 1 22  ? 14.414 4.142   8.798   0.36 17.80 ?  22  ASP   A CG   1 
ATOM   586  O  OD1  A ASP   A 1 22  ? 14.851 4.119   9.160   0.64 21.27 ?  22  ASP   A OD1  1 
ATOM   587  O  OD1  B ASP   A 1 22  ? 15.412 3.569   8.320   0.36 17.42 ?  22  ASP   A OD1  1 
ATOM   588  O  OD2  A ASP   A 1 22  ? 13.410 5.697   9.605   0.64 22.63 -1 22  ASP   A OD2  1 
ATOM   589  O  OD2  B ASP   A 1 22  ? 14.267 5.384   8.761   0.36 18.63 -1 22  ASP   A OD2  1 
ATOM   590  H  H    A ASP   A 1 22  ? 11.562 1.433   10.688  0.64 20.10 ?  22  ASP   A H    1 
ATOM   591  H  H    B ASP   A 1 22  ? 11.712 1.689   10.146  0.36 18.68 ?  22  ASP   A H    1 
ATOM   592  H  HA   A ASP   A 1 22  ? 13.079 2.045   8.569   0.64 20.17 ?  22  ASP   A HA   1 
ATOM   593  H  HA   B ASP   A 1 22  ? 13.444 1.715   8.162   0.36 18.73 ?  22  ASP   A HA   1 
ATOM   594  H  HB2  A ASP   A 1 22  ? 11.841 3.729   9.666   0.64 22.64 ?  22  ASP   A HB2  1 
ATOM   595  H  HB2  B ASP   A 1 22  ? 12.479 3.670   9.195   0.36 20.35 ?  22  ASP   A HB2  1 
ATOM   596  H  HB3  A ASP   A 1 22  ? 12.680 3.470   10.990  0.64 22.64 ?  22  ASP   A HB3  1 
ATOM   597  H  HB3  B ASP   A 1 22  ? 13.439 3.414   10.433  0.36 20.35 ?  22  ASP   A HB3  1 
ATOM   598  N  N    A ILE   A 1 23  ? 15.268 1.123   9.230   0.64 15.08 ?  23  ILE   A N    1 
ATOM   599  N  N    B ILE   A 1 23  ? 15.566 0.734   8.958   0.36 13.67 ?  23  ILE   A N    1 
ATOM   600  C  CA   A ILE   A 1 23  ? 16.525 0.522   9.673   0.64 14.62 ?  23  ILE   A CA   1 
ATOM   601  C  CA   B ILE   A 1 23  ? 16.771 0.094   9.483   0.36 13.10 ?  23  ILE   A CA   1 
ATOM   602  C  C    A ILE   A 1 23  ? 17.319 1.476   10.556  0.64 14.56 ?  23  ILE   A C    1 
ATOM   603  C  C    B ILE   A 1 23  ? 17.517 1.041   10.410  0.36 13.71 ?  23  ILE   A C    1 
ATOM   604  O  O    A ILE   A 1 23  ? 18.032 1.038   11.466  0.64 14.99 ?  23  ILE   A O    1 
ATOM   605  O  O    B ILE   A 1 23  ? 18.170 0.607   11.366  0.36 13.84 ?  23  ILE   A O    1 
ATOM   606  C  CB   A ILE   A 1 23  ? 17.337 0.018   8.460   0.64 14.33 ?  23  ILE   A CB   1 
ATOM   607  C  CB   B ILE   A 1 23  ? 17.671 -0.426  8.338   0.36 12.52 ?  23  ILE   A CB   1 
ATOM   608  C  CG1  A ILE   A 1 23  ? 18.498 -0.868  8.926   0.64 14.43 ?  23  ILE   A CG1  1 
ATOM   609  C  CG1  B ILE   A 1 23  ? 18.761 -1.351  8.895   0.36 12.53 ?  23  ILE   A CG1  1 
ATOM   610  C  CG2  A ILE   A 1 23  ? 17.803 1.187   7.591   0.64 14.60 ?  23  ILE   A CG2  1 
ATOM   611  C  CG2  B ILE   A 1 23  ? 18.304 0.728   7.564   0.36 12.36 ?  23  ILE   A CG2  1 
ATOM   612  C  CD1  A ILE   A 1 23  ? 19.179 -1.619  7.803   0.64 14.86 ?  23  ILE   A CD1  1 
ATOM   613  C  CD1  B ILE   A 1 23  ? 19.626 -2.008  7.829   0.36 12.64 ?  23  ILE   A CD1  1 
ATOM   614  H  H    A ILE   A 1 23  ? 15.167 1.161   8.383   0.64 18.08 ?  23  ILE   A H    1 
ATOM   615  H  H    B ILE   A 1 23  ? 15.545 0.791   8.111   0.36 16.39 ?  23  ILE   A H    1 
ATOM   616  H  HA   A ILE   A 1 23  ? 16.311 -0.252  10.216  0.64 17.53 ?  23  ILE   A HA   1 
ATOM   617  H  HA   B ILE   A 1 23  ? 16.501 -0.676  10.004  0.36 15.71 ?  23  ILE   A HA   1 
ATOM   618  H  HB   A ILE   A 1 23  ? 16.746 -0.530  7.923   0.64 17.18 ?  23  ILE   A HB   1 
ATOM   619  H  HB   B ILE   A 1 23  ? 17.126 -0.942  7.725   0.36 15.01 ?  23  ILE   A HB   1 
ATOM   620  H  HG12 A ILE   A 1 23  ? 19.165 -0.310  9.356   0.64 17.30 ?  23  ILE   A HG12 1 
ATOM   621  H  HG12 B ILE   A 1 23  ? 19.348 -0.837  9.471   0.36 15.03 ?  23  ILE   A HG12 1 
ATOM   622  H  HG13 A ILE   A 1 23  ? 18.159 -1.522  9.557   0.64 17.30 ?  23  ILE   A HG13 1 
ATOM   623  H  HG13 B ILE   A 1 23  ? 18.340 -2.060  9.407   0.36 15.03 ?  23  ILE   A HG13 1 
ATOM   624  H  HG21 A ILE   A 1 23  ? 18.192 0.838   6.774   0.64 17.51 ?  23  ILE   A HG21 1 
ATOM   625  H  HG21 B ILE   A 1 23  ? 18.689 0.381   6.740   0.36 14.82 ?  23  ILE   A HG21 1 
ATOM   626  H  HG22 A ILE   A 1 23  ? 17.035 1.746   7.375   0.64 17.51 ?  23  ILE   A HG22 1 
ATOM   627  H  HG22 B ILE   A 1 23  ? 17.619 1.379   7.358   0.36 14.82 ?  23  ILE   A HG22 1 
ATOM   628  H  HG23 A ILE   A 1 23  ? 18.459 1.707   8.077   0.64 17.51 ?  23  ILE   A HG23 1 
ATOM   629  H  HG23 B ILE   A 1 23  ? 18.998 1.132   8.106   0.36 14.82 ?  23  ILE   A HG23 1 
ATOM   630  H  HD11 A ILE   A 1 23  ? 19.868 -2.188  8.179   0.64 17.81 ?  23  ILE   A HD11 1 
ATOM   631  H  HD11 B ILE   A 1 23  ? 20.223 -2.648  8.254   0.36 15.15 ?  23  ILE   A HD11 1 
ATOM   632  H  HD12 A ILE   A 1 23  ? 18.519 -2.159  7.341   0.64 17.81 ?  23  ILE   A HD12 1 
ATOM   633  H  HD12 B ILE   A 1 23  ? 19.053 -2.466  7.194   0.36 15.15 ?  23  ILE   A HD12 1 
ATOM   634  H  HD13 A ILE   A 1 23  ? 19.573 -0.980  7.190   0.64 17.81 ?  23  ILE   A HD13 1 
ATOM   635  H  HD13 B ILE   A 1 23  ? 20.145 -1.326  7.375   0.36 15.15 ?  23  ILE   A HD13 1 
ATOM   636  N  N    A VAL   A 1 24  ? 17.199 2.785   10.323  0.64 15.15 ?  24  VAL   A N    1 
ATOM   637  N  N    B VAL   A 1 24  ? 17.428 2.345   10.148  0.36 14.85 ?  24  VAL   A N    1 
ATOM   638  C  CA   A VAL   A 1 24  ? 17.878 3.754   11.180  0.64 16.40 ?  24  VAL   A CA   1 
ATOM   639  C  CA   B VAL   A 1 24  ? 18.059 3.334   11.015  0.36 16.20 ?  24  VAL   A CA   1 
ATOM   640  C  C    A VAL   A 1 24  ? 17.347 3.666   12.605  0.64 17.03 ?  24  VAL   A C    1 
ATOM   641  C  C    B VAL   A 1 24  ? 17.446 3.288   12.408  0.36 17.01 ?  24  VAL   A C    1 
ATOM   642  O  O    A VAL   A 1 24  ? 18.113 3.577   13.573  0.64 17.75 ?  24  VAL   A O    1 
ATOM   643  O  O    B VAL   A 1 24  ? 18.157 3.356   13.419  0.36 17.71 ?  24  VAL   A O    1 
ATOM   644  C  CB   A VAL   A 1 24  ? 17.727 5.173   10.607  0.64 17.04 ?  24  VAL   A CB   1 
ATOM   645  C  CB   B VAL   A 1 24  ? 17.947 4.729   10.373  0.36 16.98 ?  24  VAL   A CB   1 
ATOM   646  C  CG1  A VAL   A 1 24  ? 18.203 6.213   11.617  0.64 17.52 ?  24  VAL   A CG1  1 
ATOM   647  C  CG1  B VAL   A 1 24  ? 18.559 5.779   11.272  0.36 17.80 ?  24  VAL   A CG1  1 
ATOM   648  C  CG2  A VAL   A 1 24  ? 18.489 5.300   9.299   0.64 17.52 ?  24  VAL   A CG2  1 
ATOM   649  C  CG2  B VAL   A 1 24  ? 18.615 4.726   9.005   0.36 17.01 ?  24  VAL   A CG2  1 
ATOM   650  H  H    A VAL   A 1 24  ? 16.732 3.132   9.687   0.64 18.17 ?  24  VAL   A H    1 
ATOM   651  H  H    B VAL   A 1 24  ? 17.008 2.678   9.481   0.36 17.80 ?  24  VAL   A H    1 
ATOM   652  H  HA   A VAL   A 1 24  ? 18.823 3.545   11.201  0.64 19.67 ?  24  VAL   A HA   1 
ATOM   653  H  HA   B VAL   A 1 24  ? 18.999 3.122   11.101  0.36 19.42 ?  24  VAL   A HA   1 
ATOM   654  H  HB   A VAL   A 1 24  ? 16.791 5.345   10.418  0.64 20.43 ?  24  VAL   A HB   1 
ATOM   655  H  HB   B VAL   A 1 24  ? 17.010 4.948   10.248  0.36 20.35 ?  24  VAL   A HB   1 
ATOM   656  H  HG11 A VAL   A 1 24  ? 18.367 7.049   11.153  0.64 21.00 ?  24  VAL   A HG11 1 
ATOM   657  H  HG11 B VAL   A 1 24  ? 18.735 6.578   10.751  0.36 21.35 ?  24  VAL   A HG11 1 
ATOM   658  H  HG12 A VAL   A 1 24  ? 17.517 6.338   12.289  0.64 21.00 ?  24  VAL   A HG12 1 
ATOM   659  H  HG12 B VAL   A 1 24  ? 17.931 5.980   11.982  0.36 21.35 ?  24  VAL   A HG12 1 
ATOM   660  H  HG13 A VAL   A 1 24  ? 19.022 5.897   12.028  0.64 21.00 ?  24  VAL   A HG13 1 
ATOM   661  H  HG13 B VAL   A 1 24  ? 19.387 5.436   11.643  0.36 21.35 ?  24  VAL   A HG13 1 
ATOM   662  H  HG21 A VAL   A 1 24  ? 18.278 6.154   8.888   0.64 21.01 ?  24  VAL   A HG21 1 
ATOM   663  H  HG21 B VAL   A 1 24  ? 18.613 5.628   8.650   0.36 20.40 ?  24  VAL   A HG21 1 
ATOM   664  H  HG22 A VAL   A 1 24  ? 19.442 5.251   9.481   0.64 21.01 ?  24  VAL   A HG22 1 
ATOM   665  H  HG22 B VAL   A 1 24  ? 19.528 4.410   9.102   0.36 20.40 ?  24  VAL   A HG22 1 
ATOM   666  H  HG23 A VAL   A 1 24  ? 18.229 4.577   8.705   0.64 21.01 ?  24  VAL   A HG23 1 
ATOM   667  H  HG23 B VAL   A 1 24  ? 18.124 4.136   8.412   0.36 20.40 ?  24  VAL   A HG23 1 
ATOM   668  N  N    A GLU   A 1 25  ? 16.022 3.708   12.753  0.64 17.61 ?  25  GLU   A N    1 
ATOM   669  N  N    B GLU   A 1 25  ? 16.119 3.152   12.486  0.36 17.47 ?  25  GLU   A N    1 
ATOM   670  C  CA   A GLU   A 1 25  ? 15.430 3.652   14.084  0.64 18.71 ?  25  GLU   A CA   1 
ATOM   671  C  CA   B GLU   A 1 25  ? 15.458 3.076   13.786  0.36 18.52 ?  25  GLU   A CA   1 
ATOM   672  C  C    A GLU   A 1 25  ? 15.668 2.296   14.735  0.64 17.32 ?  25  GLU   A C    1 
ATOM   673  C  C    B GLU   A 1 25  ? 15.746 1.746   14.477  0.36 18.07 ?  25  GLU   A C    1 
ATOM   674  O  O    A GLU   A 1 25  ? 15.885 2.215   15.950  0.64 18.01 ?  25  GLU   A O    1 
ATOM   675  O  O    B GLU   A 1 25  ? 15.979 1.711   15.691  0.36 18.22 ?  25  GLU   A O    1 
ATOM   676  C  CB   A GLU   A 1 25  ? 13.939 3.988   14.008  0.64 21.14 ?  25  GLU   A CB   1 
ATOM   677  C  CB   B GLU   A 1 25  ? 13.954 3.317   13.630  0.36 19.86 ?  25  GLU   A CB   1 
ATOM   678  C  CG   A GLU   A 1 25  ? 13.668 5.451   13.675  0.64 24.17 ?  25  GLU   A CG   1 
ATOM   679  C  CG   B GLU   A 1 25  ? 13.615 4.717   13.138  0.36 21.77 ?  25  GLU   A CG   1 
ATOM   680  C  CD   A GLU   A 1 25  ? 14.475 6.412   14.534  0.64 26.73 ?  25  GLU   A CD   1 
ATOM   681  C  CD   B GLU   A 1 25  ? 14.089 5.797   14.090  0.36 23.44 ?  25  GLU   A CD   1 
ATOM   682  O  OE1  A GLU   A 1 25  ? 14.527 6.216   15.767  0.64 27.52 ?  25  GLU   A OE1  1 
ATOM   683  O  OE1  B GLU   A 1 25  ? 14.106 5.544   15.314  0.36 24.24 ?  25  GLU   A OE1  1 
ATOM   684  O  OE2  A GLU   A 1 25  ? 15.079 7.348   13.969  0.64 27.88 -1 25  GLU   A OE2  1 
ATOM   685  O  OE2  B GLU   A 1 25  ? 14.450 6.894   13.614  0.36 24.16 -1 25  GLU   A OE2  1 
ATOM   686  H  H    A GLU   A 1 25  ? 15.455 3.778   12.106  0.64 21.11 ?  25  GLU   A H    1 
ATOM   687  H  H    B GLU   A 1 25  ? 15.589 3.100   11.810  0.36 20.95 ?  25  GLU   A H    1 
ATOM   688  H  HA   A GLU   A 1 25  ? 15.861 4.315   14.643  0.64 22.44 ?  25  GLU   A HA   1 
ATOM   689  H  HA   B GLU   A 1 25  ? 15.809 3.776   14.352  0.36 22.21 ?  25  GLU   A HA   1 
ATOM   690  H  HB2  A GLU   A 1 25  ? 13.522 3.449   13.312  0.64 25.36 ?  25  GLU   A HB2  1 
ATOM   691  H  HB2  B GLU   A 1 25  ? 13.595 2.685   12.989  0.36 23.82 ?  25  GLU   A HB2  1 
ATOM   692  H  HB3  A GLU   A 1 25  ? 13.521 3.798   14.862  0.64 25.36 ?  25  GLU   A HB3  1 
ATOM   693  H  HB3  B GLU   A 1 25  ? 13.524 3.194   14.491  0.36 23.82 ?  25  GLU   A HB3  1 
ATOM   694  H  HG2  A GLU   A 1 25  ? 13.914 5.616   12.754  0.64 28.99 ?  25  GLU   A HG2  1 
ATOM   695  H  HG2  B GLU   A 1 25  ? 14.043 4.866   12.281  0.36 26.11 ?  25  GLU   A HG2  1 
ATOM   696  H  HG3  A GLU   A 1 25  ? 12.725 5.638   13.811  0.64 28.99 ?  25  GLU   A HG3  1 
ATOM   697  H  HG3  B GLU   A 1 25  ? 12.653 4.800   13.048  0.36 26.11 ?  25  GLU   A HG3  1 
ATOM   698  N  N    A GLU   A 1 26  ? 15.648 1.224   13.942  0.64 16.97 ?  26  GLU   A N    1 
ATOM   699  N  N    B GLU   A 1 26  ? 15.744 0.643   13.724  0.36 17.89 ?  26  GLU   A N    1 
ATOM   700  C  CA   A GLU   A 1 26  ? 15.937 -0.100  14.482  0.64 17.01 ?  26  GLU   A CA   1 
ATOM   701  C  CA   B GLU   A 1 26  ? 16.134 -0.638  14.306  0.36 18.10 ?  26  GLU   A CA   1 
ATOM   702  C  C    A GLU   A 1 26  ? 17.362 -0.170  15.019  0.64 16.43 ?  26  GLU   A C    1 
ATOM   703  C  C    B GLU   A 1 26  ? 17.559 -0.584  14.840  0.36 17.69 ?  26  GLU   A C    1 
ATOM   704  O  O    A GLU   A 1 26  ? 17.598 -0.670  16.124  0.64 16.58 ?  26  GLU   A O    1 
ATOM   705  O  O    B GLU   A 1 26  ? 17.867 -1.189  15.874  0.36 17.47 ?  26  GLU   A O    1 
ATOM   706  C  CB   A GLU   A 1 26  ? 15.735 -1.160  13.400  0.64 18.29 ?  26  GLU   A CB   1 
ATOM   707  C  CB   B GLU   A 1 26  ? 15.988 -1.759  13.275  0.36 18.92 ?  26  GLU   A CB   1 
ATOM   708  C  CG   A GLU   A 1 26  ? 14.326 -1.694  13.282  0.64 21.23 ?  26  GLU   A CG   1 
ATOM   709  C  CG   B GLU   A 1 26  ? 14.550 -2.110  12.946  0.36 19.38 ?  26  GLU   A CG   1 
ATOM   710  C  CD   A GLU   A 1 26  ? 13.918 -2.540  14.476  0.64 23.22 ?  26  GLU   A CD   1 
ATOM   711  C  CD   B GLU   A 1 26  ? 13.776 -2.604  14.152  0.36 19.69 ?  26  GLU   A CD   1 
ATOM   712  O  OE1  A GLU   A 1 26  ? 14.414 -3.683  14.616  0.64 24.17 ?  26  GLU   A OE1  1 
ATOM   713  O  OE1  B GLU   A 1 26  ? 14.228 -3.575  14.799  0.36 20.53 ?  26  GLU   A OE1  1 
ATOM   714  O  OE2  A GLU   A 1 26  ? 13.104 -2.051  15.278  0.64 24.29 -1 26  GLU   A OE2  1 
ATOM   715  O  OE2  B GLU   A 1 26  ? 12.719 -2.011  14.454  0.36 18.77 -1 26  GLU   A OE2  1 
ATOM   716  H  H    A GLU   A 1 26  ? 15.468 1.244   13.101  0.64 20.34 ?  26  GLU   A H    1 
ATOM   717  H  H    B GLU   A 1 26  ? 15.519 0.609   12.895  0.36 21.45 ?  26  GLU   A H    1 
ATOM   718  H  HA   A GLU   A 1 26  ? 15.326 -0.281  15.211  0.64 20.40 ?  26  GLU   A HA   1 
ATOM   719  H  HA   B GLU   A 1 26  ? 15.551 -0.839  15.052  0.36 21.70 ?  26  GLU   A HA   1 
ATOM   720  H  HB2  A GLU   A 1 26  ? 15.974 -0.775  12.542  0.64 21.93 ?  26  GLU   A HB2  1 
ATOM   721  H  HB2  B GLU   A 1 26  ? 16.419 -1.486  12.449  0.36 22.68 ?  26  GLU   A HB2  1 
ATOM   722  H  HB3  A GLU   A 1 26  ? 16.317 -1.907  13.597  0.64 21.93 ?  26  GLU   A HB3  1 
ATOM   723  H  HB3  B GLU   A 1 26  ? 16.417 -2.560  13.617  0.36 22.68 ?  26  GLU   A HB3  1 
ATOM   724  H  HG2  A GLU   A 1 26  ? 13.711 -0.946  13.209  0.64 25.46 ?  26  GLU   A HG2  1 
ATOM   725  H  HG2  B GLU   A 1 26  ? 14.098 -1.320  12.615  0.36 23.24 ?  26  GLU   A HG2  1 
ATOM   726  H  HG3  A GLU   A 1 26  ? 14.263 -2.249  12.488  0.64 25.46 ?  26  GLU   A HG3  1 
ATOM   727  H  HG3  B GLU   A 1 26  ? 14.537 -2.809  12.275  0.36 23.24 ?  26  GLU   A HG3  1 
ATOM   728  N  N    A ALA   A 1 27  ? 18.330 0.322   14.239  0.64 15.85 ?  27  ALA   A N    1 
ATOM   729  N  N    B ALA   A 1 27  ? 18.445 0.139   14.154  0.36 17.46 ?  27  ALA   A N    1 
ATOM   730  C  CA   A ALA   A 1 27  ? 19.724 0.246   14.665  0.64 16.85 ?  27  ALA   A CA   1 
ATOM   731  C  CA   B ALA   A 1 27  ? 19.812 0.265   14.645  0.36 17.84 ?  27  ALA   A CA   1 
ATOM   732  C  C    A ALA   A 1 27  ? 19.948 1.023   15.956  0.64 18.18 ?  27  ALA   A C    1 
ATOM   733  C  C    B ALA   A 1 27  ? 19.868 1.130   15.899  0.36 18.86 ?  27  ALA   A C    1 
ATOM   734  O  O    A ALA   A 1 27  ? 20.632 0.545   16.868  0.64 18.56 ?  27  ALA   A O    1 
ATOM   735  O  O    B ALA   A 1 27  ? 20.535 0.773   16.877  0.36 18.83 ?  27  ALA   A O    1 
ATOM   736  C  CB   A ALA   A 1 27  ? 20.646 0.758   13.556  0.64 16.46 ?  27  ALA   A CB   1 
ATOM   737  C  CB   B ALA   A 1 27  ? 20.717 0.825   13.547  0.36 17.47 ?  27  ALA   A CB   1 
ATOM   738  H  H    A ALA   A 1 27  ? 18.205 0.697   13.473  0.64 19.01 ?  27  ALA   A H    1 
ATOM   739  H  H    B ALA   A 1 27  ? 18.282 0.554   13.418  0.36 20.93 ?  27  ALA   A H    1 
ATOM   740  H  HA   A ALA   A 1 27  ? 19.945 -0.681  14.831  0.64 20.21 ?  27  ALA   A HA   1 
ATOM   741  H  HA   B ALA   A 1 27  ? 20.143 -0.617  14.875  0.36 21.39 ?  27  ALA   A HA   1 
ATOM   742  H  HB1  A ALA   A 1 27  ? 21.566 0.697   13.860  0.64 19.74 ?  27  ALA   A HB1  1 
ATOM   743  H  HB1  B ALA   A 1 27  ? 21.623 0.892   13.889  0.36 20.95 ?  27  ALA   A HB1  1 
ATOM   744  H  HB2  A ALA   A 1 27  ? 20.523 0.209   12.765  0.64 19.74 ?  27  ALA   A HB2  1 
ATOM   745  H  HB2  B ALA   A 1 27  ? 20.699 0.225   12.782  0.36 20.95 ?  27  ALA   A HB2  1 
ATOM   746  H  HB3  A ALA   A 1 27  ? 20.424 1.680   13.358  0.64 19.74 ?  27  ALA   A HB3  1 
ATOM   747  H  HB3  B ALA   A 1 27  ? 20.396 1.701   13.286  0.36 20.95 ?  27  ALA   A HB3  1 
ATOM   748  N  N    A LYS   A 1 28  ? 19.370 2.221   16.059  0.64 20.20 ?  28  LYS   A N    1 
ATOM   749  N  N    B LYS   A 1 28  ? 19.157 2.261   15.900  0.36 20.36 ?  28  LYS   A N    1 
ATOM   750  C  CA   A LYS   A 1 28  ? 19.532 3.012   17.274  0.64 22.72 ?  28  LYS   A CA   1 
ATOM   751  C  CA   B LYS   A 1 28  ? 19.205 3.163   17.048  0.36 21.99 ?  28  LYS   A CA   1 
ATOM   752  C  C    A LYS   A 1 28  ? 18.966 2.283   18.487  0.64 23.81 ?  28  LYS   A C    1 
ATOM   753  C  C    B LYS   A 1 28  ? 18.682 2.507   18.320  0.36 23.27 ?  28  LYS   A C    1 
ATOM   754  O  O    A LYS   A 1 28  ? 19.544 2.340   19.579  0.64 24.76 ?  28  LYS   A O    1 
ATOM   755  O  O    B LYS   A 1 28  ? 19.057 2.915   19.425  0.36 23.60 ?  28  LYS   A O    1 
ATOM   756  C  CB   A LYS   A 1 28  ? 18.891 4.391   17.099  0.64 24.70 ?  28  LYS   A CB   1 
ATOM   757  C  CB   B LYS   A 1 28  ? 18.411 4.436   16.759  0.36 22.79 ?  28  LYS   A CB   1 
ATOM   758  C  CG   A LYS   A 1 28  ? 19.695 5.317   16.197  0.64 26.61 ?  28  LYS   A CG   1 
ATOM   759  C  CG   B LYS   A 1 28  ? 19.112 5.406   15.826  0.36 23.91 ?  28  LYS   A CG   1 
ATOM   760  C  CD   A LYS   A 1 28  ? 19.224 6.760   16.278  0.64 28.70 ?  28  LYS   A CD   1 
ATOM   761  C  CD   B LYS   A 1 28  ? 18.467 6.784   15.868  0.36 25.38 ?  28  LYS   A CD   1 
ATOM   762  C  CE   A LYS   A 1 28  ? 17.941 6.969   15.499  0.64 30.22 ?  28  LYS   A CE   1 
ATOM   763  C  CE   B LYS   A 1 28  ? 17.733 7.101   14.578  0.36 26.61 ?  28  LYS   A CE   1 
ATOM   764  N  NZ   A LYS   A 1 28  ? 17.585 8.413   15.419  0.64 31.28 ?  28  LYS   A NZ   1 
ATOM   765  N  NZ   B LYS   A 1 28  ? 17.268 8.517   14.542  0.36 27.14 ?  28  LYS   A NZ   1 
ATOM   766  H  H    A LYS   A 1 28  ? 18.895 2.591   15.450  0.64 24.22 ?  28  LYS   A H    1 
ATOM   767  H  H    B LYS   A 1 28  ? 18.653 2.525   15.254  0.36 24.41 ?  28  LYS   A H    1 
ATOM   768  H  HA   A LYS   A 1 28  ? 20.477 3.147   17.439  0.64 27.25 ?  28  LYS   A HA   1 
ATOM   769  H  HA   B LYS   A 1 28  ? 20.126 3.419   17.200  0.36 26.37 ?  28  LYS   A HA   1 
ATOM   770  H  HB2  A LYS   A 1 28  ? 18.014 4.286   16.702  0.64 29.62 ?  28  LYS   A HB2  1 
ATOM   771  H  HB2  B LYS   A 1 28  ? 17.566 4.192   16.350  0.36 27.33 ?  28  LYS   A HB2  1 
ATOM   772  H  HB3  A LYS   A 1 28  ? 18.816 4.819   17.965  0.64 29.62 ?  28  LYS   A HB3  1 
ATOM   773  H  HB3  B LYS   A 1 28  ? 18.250 4.894   17.598  0.36 27.33 ?  28  LYS   A HB3  1 
ATOM   774  H  HG2  A LYS   A 1 28  ? 20.627 5.292   16.463  0.64 31.92 ?  28  LYS   A HG2  1 
ATOM   775  H  HG2  B LYS   A 1 28  ? 20.039 5.496   16.095  0.36 28.67 ?  28  LYS   A HG2  1 
ATOM   776  H  HG3  A LYS   A 1 28  ? 19.604 5.024   15.277  0.64 31.92 ?  28  LYS   A HG3  1 
ATOM   777  H  HG3  B LYS   A 1 28  ? 19.058 5.073   14.916  0.36 28.67 ?  28  LYS   A HG3  1 
ATOM   778  H  HD2  A LYS   A 1 28  ? 19.056 6.992   17.205  0.64 34.42 ?  28  LYS   A HD2  1 
ATOM   779  H  HD2  B LYS   A 1 28  ? 17.828 6.818   16.597  0.36 30.44 ?  28  LYS   A HD2  1 
ATOM   780  H  HD3  A LYS   A 1 28  ? 19.904 7.342   15.904  0.64 34.42 ?  28  LYS   A HD3  1 
ATOM   781  H  HD3  B LYS   A 1 28  ? 19.157 7.453   15.997  0.36 30.44 ?  28  LYS   A HD3  1 
ATOM   782  H  HE2  A LYS   A 1 28  ? 18.057 6.633   14.596  0.64 36.25 ?  28  LYS   A HE2  1 
ATOM   783  H  HE2  B LYS   A 1 28  ? 18.337 6.966   13.833  0.36 31.92 ?  28  LYS   A HE2  1 
ATOM   784  H  HE3  A LYS   A 1 28  ? 17.217 6.501   15.942  0.64 36.25 ?  28  LYS   A HE3  1 
ATOM   785  H  HE3  B LYS   A 1 28  ? 16.958 6.521   14.496  0.36 31.92 ?  28  LYS   A HE3  1 
ATOM   786  H  HZ1  A LYS   A 1 28  ? 16.831 8.515   14.958  0.64 37.52 ?  28  LYS   A HZ1  1 
ATOM   787  H  HZ1  B LYS   A 1 28  ? 16.842 8.679   13.778  0.36 32.55 ?  28  LYS   A HZ1  1 
ATOM   788  H  HZ2  A LYS   A 1 28  ? 17.472 8.744   16.237  0.64 37.52 ?  28  LYS   A HZ2  1 
ATOM   789  H  HZ2  B LYS   A 1 28  ? 16.716 8.674   15.221  0.36 32.55 ?  28  LYS   A HZ2  1 
ATOM   790  H  HZ3  A LYS   A 1 28  ? 18.237 8.864   15.013  0.64 37.52 ?  28  LYS   A HZ3  1 
ATOM   791  H  HZ3  B LYS   A 1 28  ? 17.967 9.067   14.605  0.36 32.55 ?  28  LYS   A HZ3  1 
ATOM   792  N  N    A LYS   A 1 29  ? 17.849 1.574   18.311  0.64 24.51 ?  29  LYS   A N    1 
ATOM   793  N  N    B LYS   A 1 29  ? 17.813 1.506   18.191  0.36 24.63 ?  29  LYS   A N    1 
ATOM   794  C  CA   A LYS   A 1 29  ? 17.247 0.851   19.428  0.64 26.33 ?  29  LYS   A CA   1 
ATOM   795  C  CA   B LYS   A 1 29  ? 17.215 0.852   19.350  0.36 26.45 ?  29  LYS   A CA   1 
ATOM   796  C  C    A LYS   A 1 29  ? 18.073 -0.374  19.802  0.64 26.00 ?  29  LYS   A C    1 
ATOM   797  C  C    B LYS   A 1 29  ? 17.990 -0.388  19.779  0.36 25.95 ?  29  LYS   A C    1 
ATOM   798  O  O    A LYS   A 1 29  ? 18.416 -0.569  20.975  0.64 26.82 ?  29  LYS   A O    1 
ATOM   799  O  O    B LYS   A 1 29  ? 18.211 -0.597  20.977  0.36 26.34 ?  29  LYS   A O    1 
ATOM   800  C  CB   A LYS   A 1 29  ? 15.816 0.441   19.073  0.64 28.95 ?  29  LYS   A CB   1 
ATOM   801  C  CB   B LYS   A 1 29  ? 15.770 0.461   19.027  0.36 28.72 ?  29  LYS   A CB   1 
ATOM   802  C  CG   A LYS   A 1 29  ? 15.069 -0.255  20.204  0.64 31.67 ?  29  LYS   A CG   1 
ATOM   803  C  CG   B LYS   A 1 29  ? 15.000 -0.145  20.190  0.36 30.86 ?  29  LYS   A CG   1 
ATOM   804  C  CD   A LYS   A 1 29  ? 14.758 0.708   21.339  0.64 34.17 ?  29  LYS   A CD   1 
ATOM   805  C  CD   B LYS   A 1 29  ? 14.674 0.899   21.246  0.36 32.72 ?  29  LYS   A CD   1 
ATOM   806  C  CE   A LYS   A 1 29  ? 13.884 0.053   22.397  0.64 35.96 ?  29  LYS   A CE   1 
ATOM   807  C  CE   B LYS   A 1 29  ? 13.793 0.320   22.342  0.36 34.06 ?  29  LYS   A CE   1 
ATOM   808  N  NZ   A LYS   A 1 29  ? 13.464 1.021   23.447  0.64 37.02 ?  29  LYS   A NZ   1 
ATOM   809  N  NZ   B LYS   A 1 29  ? 13.430 1.344   23.359  0.36 34.84 ?  29  LYS   A NZ   1 
ATOM   810  H  H    A LYS   A 1 29  ? 17.425 1.499   17.570  0.64 29.39 ?  29  LYS   A H    1 
ATOM   811  H  H    B LYS   A 1 29  ? 17.547 1.188   17.439  0.36 29.54 ?  29  LYS   A H    1 
ATOM   812  H  HA   A LYS   A 1 29  ? 17.208 1.433   20.202  0.64 31.58 ?  29  LYS   A HA   1 
ATOM   813  H  HA   B LYS   A 1 29  ? 17.201 1.471   20.095  0.36 31.72 ?  29  LYS   A HA   1 
ATOM   814  H  HB2  A LYS   A 1 29  ? 15.312 1.236   18.836  0.64 34.72 ?  29  LYS   A HB2  1 
ATOM   815  H  HB2  B LYS   A 1 29  ? 15.293 1.256   18.743  0.36 34.45 ?  29  LYS   A HB2  1 
ATOM   816  H  HB3  A LYS   A 1 29  ? 15.842 -0.168  18.319  0.64 34.72 ?  29  LYS   A HB3  1 
ATOM   817  H  HB3  B LYS   A 1 29  ? 15.778 -0.190  18.309  0.36 34.45 ?  29  LYS   A HB3  1 
ATOM   818  H  HG2  A LYS   A 1 29  ? 14.230 -0.604  19.866  0.64 37.99 ?  29  LYS   A HG2  1 
ATOM   819  H  HG2  B LYS   A 1 29  ? 14.165 -0.513  19.860  0.36 37.01 ?  29  LYS   A HG2  1 
ATOM   820  H  HG3  A LYS   A 1 29  ? 15.611 -0.978  20.559  0.64 37.99 ?  29  LYS   A HG3  1 
ATOM   821  H  HG3  B LYS   A 1 29  ? 15.529 -0.844  20.606  0.36 37.01 ?  29  LYS   A HG3  1 
ATOM   822  H  HD2  A LYS   A 1 29  ? 15.586 0.989   21.760  0.64 40.99 ?  29  LYS   A HD2  1 
ATOM   823  H  HD2  B LYS   A 1 29  ? 15.497 1.214   21.651  0.36 39.25 ?  29  LYS   A HD2  1 
ATOM   824  H  HD3  A LYS   A 1 29  ? 14.283 1.477   20.985  0.64 40.99 ?  29  LYS   A HD3  1 
ATOM   825  H  HD3  B LYS   A 1 29  ? 14.199 1.636   20.831  0.36 39.25 ?  29  LYS   A HD3  1 
ATOM   826  H  HE2  A LYS   A 1 29  ? 13.086 -0.303  21.975  0.64 43.13 ?  29  LYS   A HE2  1 
ATOM   827  H  HE2  B LYS   A 1 29  ? 12.974 -0.020  21.947  0.36 40.85 ?  29  LYS   A HE2  1 
ATOM   828  H  HE3  A LYS   A 1 29  ? 14.382 -0.662  22.824  0.64 43.13 ?  29  LYS   A HE3  1 
ATOM   829  H  HE3  B LYS   A 1 29  ? 14.270 -0.397  22.789  0.36 40.85 ?  29  LYS   A HE3  1 
ATOM   830  H  HZ1  A LYS   A 1 29  ? 12.955 0.612   24.052  0.64 44.41 ?  29  LYS   A HZ1  1 
ATOM   831  H  HZ1  B LYS   A 1 29  ? 12.916 0.980   23.987  0.36 41.79 ?  29  LYS   A HZ1  1 
ATOM   832  H  HZ2  A LYS   A 1 29  ? 14.180 1.359   23.853  0.64 44.41 ?  29  LYS   A HZ2  1 
ATOM   833  H  HZ2  B LYS   A 1 29  ? 14.166 1.668   23.740  0.36 41.79 ?  29  LYS   A HZ2  1 
ATOM   834  H  HZ3  A LYS   A 1 29  ? 13.000 1.685   23.080  0.64 44.41 ?  29  LYS   A HZ3  1 
ATOM   835  H  HZ3  B LYS   A 1 29  ? 12.986 2.012   22.973  0.36 41.79 ?  29  LYS   A HZ3  1 
ATOM   836  N  N    . VAL   A 1 30  ? 18.393 -1.219  18.822  1.00 25.15 ?  30  VAL   A N    1 
ATOM   837  C  CA   . VAL   A 1 30  ? 19.051 -2.482  19.135  1.00 24.12 ?  30  VAL   A CA   1 
ATOM   838  C  C    . VAL   A 1 30  ? 20.555 -2.324  19.343  1.00 22.97 ?  30  VAL   A C    1 
ATOM   839  O  O    . VAL   A 1 30  ? 21.152 -3.056  20.140  1.00 23.52 ?  30  VAL   A O    1 
ATOM   840  C  CB   . VAL   A 1 30  ? 18.754 -3.494  18.012  1.00 24.65 ?  30  VAL   A CB   1 
ATOM   841  C  CG1  . VAL   A 1 30  ? 19.508 -4.799  18.239  1.00 25.25 ?  30  VAL   A CG1  1 
ATOM   842  C  CG2  . VAL   A 1 30  ? 17.257 -3.750  17.906  1.00 25.14 ?  30  VAL   A CG2  1 
ATOM   843  H  H    A VAL   A 1 30  ? 18.237 -1.091  17.985  0.64 30.17 ?  30  VAL   A H    1 
ATOM   844  H  H    B VAL   A 1 30  ? 18.278 -1.081  17.980  0.36 30.17 ?  30  VAL   A H    1 
ATOM   845  H  HA   . VAL   A 1 30  ? 18.666 -2.837  19.952  1.00 28.92 ?  30  VAL   A HA   1 
ATOM   846  H  HB   . VAL   A 1 30  ? 19.052 -3.126  17.167  1.00 29.57 ?  30  VAL   A HB   1 
ATOM   847  H  HG11 . VAL   A 1 30  ? 19.133 -5.485  17.661  1.00 30.28 ?  30  VAL   A HG11 1 
ATOM   848  H  HG12 . VAL   A 1 30  ? 20.444 -4.668  18.028  1.00 30.28 ?  30  VAL   A HG12 1 
ATOM   849  H  HG13 . VAL   A 1 30  ? 19.408 -5.064  19.167  1.00 30.28 ?  30  VAL   A HG13 1 
ATOM   850  H  HG21 . VAL   A 1 30  ? 17.100 -4.434  17.235  1.00 30.15 ?  30  VAL   A HG21 1 
ATOM   851  H  HG22 . VAL   A 1 30  ? 16.927 -4.052  18.767  1.00 30.15 ?  30  VAL   A HG22 1 
ATOM   852  H  HG23 . VAL   A 1 30  ? 16.813 -2.928  17.650  1.00 30.15 ?  30  VAL   A HG23 1 
ATOM   853  N  N    A LYS   A 1 31  ? 21.187 -1.383  18.650  0.64 22.34 ?  31  LYS   A N    1 
ATOM   854  N  N    B LYS   A 1 31  ? 21.181 -1.377  18.653  0.36 23.08 ?  31  LYS   A N    1 
ATOM   855  C  CA   A LYS   A 1 31  ? 22.640 -1.271  18.608  0.64 23.21 ?  31  LYS   A CA   1 
ATOM   856  C  CA   B LYS   A 1 31  ? 22.633 -1.265  18.597  0.36 23.89 ?  31  LYS   A CA   1 
ATOM   857  C  C    A LYS   A 1 31  ? 23.267 -2.627  18.271  0.64 21.47 ?  31  LYS   A C    1 
ATOM   858  C  C    B LYS   A 1 31  ? 23.258 -2.625  18.272  0.36 21.98 ?  31  LYS   A C    1 
ATOM   859  O  O    A LYS   A 1 31  ? 24.045 -3.173  19.058  0.64 22.19 ?  31  LYS   A O    1 
ATOM   860  O  O    B LYS   A 1 31  ? 24.025 -3.171  19.070  0.36 22.51 ?  31  LYS   A O    1 
ATOM   861  C  CB   A LYS   A 1 31  ? 23.207 -0.717  19.908  0.64 27.11 ?  31  LYS   A CB   1 
ATOM   862  C  CB   B LYS   A 1 31  ? 23.209 -0.690  19.884  0.36 27.11 ?  31  LYS   A CB   1 
ATOM   863  C  CG   A LYS   A 1 31  ? 22.522 0.549   20.397  0.64 31.32 ?  31  LYS   A CG   1 
ATOM   864  C  CG   B LYS   A 1 31  ? 22.508 0.569   20.366  0.36 30.35 ?  31  LYS   A CG   1 
ATOM   865  C  CD   A LYS   A 1 31  ? 23.536 1.612   20.792  0.64 34.61 ?  31  LYS   A CD   1 
ATOM   866  C  CD   B LYS   A 1 31  ? 23.505 1.637   20.786  0.36 32.91 ?  31  LYS   A CD   1 
ATOM   867  C  CE   A LYS   A 1 31  ? 22.928 2.641   21.733  0.64 36.82 ?  31  LYS   A CE   1 
ATOM   868  C  CE   B LYS   A 1 31  ? 22.859 2.676   21.690  0.36 34.63 ?  31  LYS   A CE   1 
ATOM   869  N  NZ   A LYS   A 1 31  ? 21.703 3.274   21.174  0.64 37.97 ?  31  LYS   A NZ   1 
ATOM   870  N  NZ   B LYS   A 1 31  ? 21.627 3.271   21.107  0.36 35.55 ?  31  LYS   A NZ   1 
ATOM   871  H  H    A LYS   A 1 31  ? 20.784 -0.785  18.184  0.64 26.79 ?  31  LYS   A H    1 
ATOM   872  H  H    B LYS   A 1 31  ? 20.772 -0.774  18.198  0.36 27.68 ?  31  LYS   A H    1 
ATOM   873  H  HA   A LYS   A 1 31  ? 22.873 -0.653  17.904  0.64 27.83 ?  31  LYS   A HA   1 
ATOM   874  H  HA   B LYS   A 1 31  ? 22.860 -0.658  17.883  0.36 28.65 ?  31  LYS   A HA   1 
ATOM   875  H  HB2  A LYS   A 1 31  ? 23.117 -1.390  20.596  0.64 32.51 ?  31  LYS   A HB2  1 
ATOM   876  H  HB2  B LYS   A 1 31  ? 23.136 -1.355  20.580  0.36 32.52 ?  31  LYS   A HB2  1 
ATOM   877  H  HB3  A LYS   A 1 31  ? 24.146 -0.510  19.771  0.64 32.51 ?  31  LYS   A HB3  1 
ATOM   878  H  HB3  B LYS   A 1 31  ? 24.144 -0.473  19.735  0.36 32.52 ?  31  LYS   A HB3  1 
ATOM   879  H  HG2  A LYS   A 1 31  ? 21.965 0.909   19.688  0.64 37.57 ?  31  LYS   A HG2  1 
ATOM   880  H  HG2  B LYS   A 1 31  ? 21.964 0.929   19.648  0.36 36.40 ?  31  LYS   A HG2  1 
ATOM   881  H  HG3  A LYS   A 1 31  ? 21.981 0.341   21.175  0.64 37.57 ?  31  LYS   A HG3  1 
ATOM   882  H  HG3  B LYS   A 1 31  ? 21.953 0.354   21.132  0.36 36.40 ?  31  LYS   A HG3  1 
ATOM   883  H  HD2  A LYS   A 1 31  ? 24.283 1.191   21.245  0.64 41.52 ?  31  LYS   A HD2  1 
ATOM   884  H  HD2  B LYS   A 1 31  ? 24.235 1.220   21.272  0.36 39.47 ?  31  LYS   A HD2  1 
ATOM   885  H  HD3  A LYS   A 1 31  ? 23.843 2.073   19.995  0.64 41.52 ?  31  LYS   A HD3  1 
ATOM   886  H  HD3  B LYS   A 1 31  ? 23.843 2.088   19.996  0.36 39.47 ?  31  LYS   A HD3  1 
ATOM   887  H  HE2  A LYS   A 1 31  ? 22.688 2.204   22.565  0.64 44.16 ?  31  LYS   A HE2  1 
ATOM   888  H  HE2  B LYS   A 1 31  ? 22.610 2.252   22.522  0.36 41.54 ?  31  LYS   A HE2  1 
ATOM   889  H  HE3  A LYS   A 1 31  ? 23.579 3.340   21.900  0.64 44.16 ?  31  LYS   A HE3  1 
ATOM   890  H  HE3  B LYS   A 1 31  ? 23.494 3.391   21.857  0.36 41.54 ?  31  LYS   A HE3  1 
ATOM   891  H  HZ1  A LYS   A 1 31  ? 21.389 3.883   21.742  0.64 45.55 ?  31  LYS   A HZ1  1 
ATOM   892  H  HZ1  B LYS   A 1 31  ? 21.299 3.889   21.659  0.36 42.65 ?  31  LYS   A HZ1  1 
ATOM   893  H  HZ2  A LYS   A 1 31  ? 21.891 3.671   20.400  0.64 45.55 ?  31  LYS   A HZ2  1 
ATOM   894  H  HZ2  B LYS   A 1 31  ? 21.812 3.650   20.325  0.36 42.65 ?  31  LYS   A HZ2  1 
ATOM   895  H  HZ3  A LYS   A 1 31  ? 21.076 2.657   21.037  0.64 45.55 ?  31  LYS   A HZ3  1 
ATOM   896  H  HZ3  B LYS   A 1 31  ? 21.012 2.639   20.986  0.36 42.65 ?  31  LYS   A HZ3  1 
ATOM   897  N  N    . PRO   A 1 32  ? 22.947 -3.189  17.109  1.00 19.90 ?  32  PRO   A N    1 
ATOM   898  C  CA   . PRO   A 1 32  ? 23.426 -4.531  16.785  1.00 19.38 ?  32  PRO   A CA   1 
ATOM   899  C  C    . PRO   A 1 32  ? 24.926 -4.548  16.570  1.00 19.21 ?  32  PRO   A C    1 
ATOM   900  O  O    . PRO   A 1 32  ? 25.569 -3.519  16.346  1.00 19.13 ?  32  PRO   A O    1 
ATOM   901  C  CB   . PRO   A 1 32  ? 22.694 -4.846  15.478  1.00 19.30 ?  32  PRO   A CB   1 
ATOM   902  C  CG   . PRO   A 1 32  ? 22.524 -3.502  14.836  1.00 18.53 ?  32  PRO   A CG   1 
ATOM   903  C  CD   . PRO   A 1 32  ? 22.230 -2.575  15.980  1.00 18.75 ?  32  PRO   A CD   1 
ATOM   904  H  HA   . PRO   A 1 32  ? 23.177 -5.168  17.472  1.00 23.23 ?  32  PRO   A HA   1 
ATOM   905  H  HB2  . PRO   A 1 32  ? 23.237 -5.431  14.925  1.00 23.14 ?  32  PRO   A HB2  1 
ATOM   906  H  HB3  . PRO   A 1 32  ? 21.833 -5.253  15.669  1.00 23.14 ?  32  PRO   A HB3  1 
ATOM   907  H  HG2  . PRO   A 1 32  ? 23.343 -3.254  14.384  1.00 22.21 ?  32  PRO   A HG2  1 
ATOM   908  H  HG3  . PRO   A 1 32  ? 21.779 -3.534  14.214  1.00 22.21 ?  32  PRO   A HG3  1 
ATOM   909  H  HD2  . PRO   A 1 32  ? 22.586 -1.694  15.782  1.00 22.49 ?  32  PRO   A HD2  1 
ATOM   910  H  HD3  . PRO   A 1 32  ? 21.280 -2.549  16.151  1.00 22.49 ?  32  PRO   A HD3  1 
ATOM   911  N  N    . THR   A 1 33  ? 25.480 -5.758  16.610  1.00 19.14 ?  33  THR   A N    1 
ATOM   912  C  CA   . THR   A 1 33  ? 26.889 -5.923  16.290  1.00 19.11 ?  33  THR   A CA   1 
ATOM   913  C  C    . THR   A 1 33  ? 27.184 -5.461  14.869  1.00 17.48 ?  33  THR   A C    1 
ATOM   914  O  O    . THR   A 1 33  ? 28.210 -4.812  14.623  1.00 17.44 ?  33  THR   A O    1 
ATOM   915  C  CB   . THR   A 1 33  ? 27.296 -7.382  16.480  1.00 20.60 ?  33  THR   A CB   1 
ATOM   916  O  OG1  . THR   A 1 33  ? 27.013 -7.780  17.825  1.00 22.37 ?  33  THR   A OG1  1 
ATOM   917  C  CG2  . THR   A 1 33  ? 28.777 -7.566  16.202  1.00 21.24 ?  33  THR   A CG2  1 
ATOM   918  H  H    . THR   A 1 33  ? 25.065 -6.485  16.805  1.00 22.96 ?  33  THR   A H    1 
ATOM   919  H  HA   . THR   A 1 33  ? 27.417 -5.381  16.896  1.00 22.92 ?  33  THR   A HA   1 
ATOM   920  H  HB   . THR   A 1 33  ? 26.795 -7.943  15.864  1.00 24.71 ?  33  THR   A HB   1 
ATOM   921  H  HG1  . THR   A 1 33  ? 27.448 -7.302  18.364  1.00 26.83 ?  33  THR   A HG1  1 
ATOM   922  H  HG21 . THR   A 1 33  ? 29.060 -8.446  16.495  1.00 25.47 ?  33  THR   A HG21 1 
ATOM   923  H  HG22 . THR   A 1 33  ? 28.952 -7.480  15.252  1.00 25.47 ?  33  THR   A HG22 1 
ATOM   924  H  HG23 . THR   A 1 33  ? 29.287 -6.895  16.681  1.00 25.47 ?  33  THR   A HG23 1 
ATOM   925  N  N    . VAL   A 1 34  ? 26.300 -5.785  13.922  1.00 15.71 ?  34  VAL   A N    1 
ATOM   926  C  CA   . VAL   A 1 34  ? 26.490 -5.452  12.514  1.00 14.49 ?  34  VAL   A CA   1 
ATOM   927  C  C    . VAL   A 1 34  ? 25.190 -4.891  11.950  1.00 13.69 ?  34  VAL   A C    1 
ATOM   928  O  O    . VAL   A 1 34  ? 24.148 -5.558  11.998  1.00 14.53 ?  34  VAL   A O    1 
ATOM   929  C  CB   . VAL   A 1 34  ? 26.935 -6.668  11.682  1.00 15.22 ?  34  VAL   A CB   1 
ATOM   930  C  CG1  . VAL   A 1 34  ? 27.125 -6.273  10.224  1.00 15.60 ?  34  VAL   A CG1  1 
ATOM   931  C  CG2  . VAL   A 1 34  ? 28.212 -7.284  12.247  1.00 16.17 ?  34  VAL   A CG2  1 
ATOM   932  H  H    . VAL   A 1 34  ? 25.567 -6.215  14.078  1.00 18.84 ?  34  VAL   A H    1 
ATOM   933  H  HA   . VAL   A 1 34  ? 27.173 -4.766  12.439  1.00 17.37 ?  34  VAL   A HA   1 
ATOM   934  H  HB   . VAL   A 1 34  ? 26.239 -7.341  11.718  1.00 18.25 ?  34  VAL   A HB   1 
ATOM   935  H  HG11 . VAL   A 1 34  ? 27.604 -6.982  9.767   1.00 18.70 ?  34  VAL   A HG11 1 
ATOM   936  H  HG12 . VAL   A 1 34  ? 26.258 -6.140  9.814   1.00 18.70 ?  34  VAL   A HG12 1 
ATOM   937  H  HG13 . VAL   A 1 34  ? 27.642 -5.451  10.186  1.00 18.70 ?  34  VAL   A HG13 1 
ATOM   938  H  HG21 . VAL   A 1 34  ? 28.495 -8.013  11.669  1.00 19.39 ?  34  VAL   A HG21 1 
ATOM   939  H  HG22 . VAL   A 1 34  ? 28.905 -6.607  12.285  1.00 19.39 ?  34  VAL   A HG22 1 
ATOM   940  H  HG23 . VAL   A 1 34  ? 28.033 -7.625  13.139  1.00 19.39 ?  34  VAL   A HG23 1 
ATOM   941  N  N    . VAL   A 1 35  ? 25.256 -3.683  11.391  1.00 13.20 ?  35  VAL   A N    1 
ATOM   942  C  CA   . VAL   A 1 35  ? 24.220 -3.165  10.504  1.00 12.72 ?  35  VAL   A CA   1 
ATOM   943  C  C    . VAL   A 1 35  ? 24.769 -3.167  9.084   1.00 11.87 ?  35  VAL   A C    1 
ATOM   944  O  O    . VAL   A 1 35  ? 25.918 -2.772  8.853   1.00 12.39 ?  35  VAL   A O    1 
ATOM   945  C  CB   . VAL   A 1 35  ? 23.695 -1.771  10.915  1.00 12.96 ?  35  VAL   A CB   1 
ATOM   946  C  CG1  . VAL   A 1 35  ? 24.768 -0.686  10.780  1.00 13.44 ?  35  VAL   A CG1  1 
ATOM   947  C  CG2  . VAL   A 1 35  ? 22.466 -1.413  10.088  1.00 13.42 ?  35  VAL   A CG2  1 
ATOM   948  H  H    . VAL   A 1 35  ? 25.903 -3.130  11.508  1.00 15.82 ?  35  VAL   A H    1 
ATOM   949  H  HA   . VAL   A 1 35  ? 23.461 -3.774  10.525  1.00 15.25 ?  35  VAL   A HA   1 
ATOM   950  H  HB   . VAL   A 1 35  ? 23.416 -1.799  11.840  1.00 15.54 ?  35  VAL   A HB   1 
ATOM   951  H  HG11 . VAL   A 1 35  ? 24.429 0.142   11.155  1.00 16.11 ?  35  VAL   A HG11 1 
ATOM   952  H  HG12 . VAL   A 1 35  ? 25.559 -0.971  11.259  1.00 16.11 ?  35  VAL   A HG12 1 
ATOM   953  H  HG13 . VAL   A 1 35  ? 24.976 -0.560  9.840   1.00 16.11 ?  35  VAL   A HG13 1 
ATOM   954  H  HG21 . VAL   A 1 35  ? 22.106 -0.571  10.402  1.00 16.09 ?  35  VAL   A HG21 1 
ATOM   955  H  HG22 . VAL   A 1 35  ? 22.725 -1.333  9.154   1.00 16.09 ?  35  VAL   A HG22 1 
ATOM   956  H  HG23 . VAL   A 1 35  ? 21.803 -2.115  10.186  1.00 16.09 ?  35  VAL   A HG23 1 
ATOM   957  N  N    . VAL   A 1 36  ? 23.956 -3.633  8.136   1.00 11.41 ?  36  VAL   A N    1 
ATOM   958  C  CA   . VAL   A 1 36  ? 24.338 -3.648  6.731   1.00 11.13 ?  36  VAL   A CA   1 
ATOM   959  C  C    . VAL   A 1 36  ? 23.881 -2.356  6.072   1.00 11.18 ?  36  VAL   A C    1 
ATOM   960  O  O    . VAL   A 1 36  ? 22.716 -1.960  6.202   1.00 11.78 ?  36  VAL   A O    1 
ATOM   961  C  CB   . VAL   A 1 36  ? 23.735 -4.863  6.013   1.00 11.23 ?  36  VAL   A CB   1 
ATOM   962  C  CG1  . VAL   A 1 36  ? 23.999 -4.789  4.527   1.00 11.75 ?  36  VAL   A CG1  1 
ATOM   963  C  CG2  . VAL   A 1 36  ? 24.290 -6.151  6.595   1.00 12.27 ?  36  VAL   A CG2  1 
ATOM   964  H  H    . VAL   A 1 36  ? 23.163 -3.941  8.285   1.00 13.67 ?  36  VAL   A H    1 
ATOM   965  H  HA   . VAL   A 1 36  ? 25.305 -3.705  6.664   1.00 13.34 ?  36  VAL   A HA   1 
ATOM   966  H  HB   . VAL   A 1 36  ? 22.774 -4.860  6.146   1.00 13.46 ?  36  VAL   A HB   1 
ATOM   967  H  HG11 . VAL   A 1 36  ? 23.855 -5.667  4.136   1.00 14.08 ?  36  VAL   A HG11 1 
ATOM   968  H  HG12 . VAL   A 1 36  ? 23.392 -4.148  4.122   1.00 14.08 ?  36  VAL   A HG12 1 
ATOM   969  H  HG13 . VAL   A 1 36  ? 24.918 -4.513  4.381   1.00 14.08 ?  36  VAL   A HG13 1 
ATOM   970  H  HG21 . VAL   A 1 36  ? 23.903 -6.907  6.120   1.00 14.71 ?  36  VAL   A HG21 1 
ATOM   971  H  HG22 . VAL   A 1 36  ? 25.254 -6.157  6.490   1.00 14.71 ?  36  VAL   A HG22 1 
ATOM   972  H  HG23 . VAL   A 1 36  ? 24.060 -6.204  7.536   1.00 14.71 ?  36  VAL   A HG23 1 
ATOM   973  N  N    . ASN   A 1 37  ? 24.799 -1.719  5.344   1.00 10.66 ?  37  ASN   A N    1 
ATOM   974  C  CA   . ASN   A 1 37  ? 24.468 -0.603  4.476   1.00 10.33 ?  37  ASN   A CA   1 
ATOM   975  C  C    . ASN   A 1 37  ? 24.333 -1.075  3.038   1.00 10.35 ?  37  ASN   A C    1 
ATOM   976  O  O    . ASN   A 1 37  ? 25.120 -1.902  2.564   1.00 10.99 ?  37  ASN   A O    1 
ATOM   977  C  CB   . ASN   A 1 37  ? 25.544 0.480   4.551   1.00 10.69 ?  37  ASN   A CB   1 
ATOM   978  C  CG   . ASN   A 1 37  ? 25.214 1.672   3.692   1.00 10.77 ?  37  ASN   A CG   1 
ATOM   979  O  OD1  . ASN   A 1 37  ? 24.040 2.006   3.505   1.00 11.29 ?  37  ASN   A OD1  1 
ATOM   980  N  ND2  . ASN   A 1 37  ? 26.244 2.322   3.163   1.00 11.19 ?  37  ASN   A ND2  1 
ATOM   981  H  H    . ASN   A 1 37  ? 25.637 -1.918  5.346   1.00 12.77 ?  37  ASN   A H    1 
ATOM   982  H  HA   . ASN   A 1 37  ? 23.628 -0.215  4.754   1.00 12.38 ?  37  ASN   A HA   1 
ATOM   983  H  HB2  . ASN   A 1 37  ? 25.625 0.784   5.471   1.00 12.81 ?  37  ASN   A HB2  1 
ATOM   984  H  HB3  . ASN   A 1 37  ? 26.392 0.111   4.250   1.00 12.81 ?  37  ASN   A HB3  1 
ATOM   985  H  HD21 . ASN   A 1 37  ? 26.103 3.008   2.659   1.00 13.41 ?  37  ASN   A HD21 1 
ATOM   986  H  HD22 . ASN   A 1 37  ? 27.041 2.063   3.311   1.00 13.41 ?  37  ASN   A HD22 1 
ATOM   987  N  N    A ALA   A 1 38  ? 23.313 -0.545  2.363   0.64 10.67 ?  38  ALA   A N    1 
ATOM   988  N  N    B ALA   A 1 38  ? 23.325 -0.552  2.340   0.36 10.59 ?  38  ALA   A N    1 
ATOM   989  C  CA   A ALA   A 1 38  ? 23.113 -0.682  0.923   0.64 10.76 ?  38  ALA   A CA   1 
ATOM   990  C  CA   B ALA   A 1 38  ? 23.162 -0.802  0.906   0.36 10.80 ?  38  ALA   A CA   1 
ATOM   991  C  C    A ALA   A 1 38  ? 24.028 0.320   0.222   0.64 10.91 ?  38  ALA   A C    1 
ATOM   992  C  C    B ALA   A 1 38  ? 23.999 0.224   0.141   0.36 10.76 ?  38  ALA   A C    1 
ATOM   993  O  O    A ALA   A 1 38  ? 23.628 1.425   -0.158  0.64 10.69 ?  38  ALA   A O    1 
ATOM   994  O  O    B ALA   A 1 38  ? 23.511 1.237   -0.371  0.36 10.80 ?  38  ALA   A O    1 
ATOM   995  C  CB   A ALA   A 1 38  ? 21.651 -0.421  0.581   0.64 11.45 ?  38  ALA   A CB   1 
ATOM   996  C  CB   B ALA   A 1 38  ? 21.691 -0.765  0.516   0.36 11.25 ?  38  ALA   A CB   1 
ATOM   997  H  H    A ALA   A 1 38  ? 22.705 -0.068  2.740   0.64 12.78 ?  38  ALA   A H    1 
ATOM   998  H  H    B ALA   A 1 38  ? 22.718 -0.046  2.680   0.36 12.69 ?  38  ALA   A H    1 
ATOM   999  H  HA   A ALA   A 1 38  ? 23.349 -1.577  0.639   0.64 12.90 ?  38  ALA   A HA   1 
ATOM   1000 H  HA   B ALA   A 1 38  ? 23.507 -1.687  0.701   0.36 12.94 ?  38  ALA   A HA   1 
ATOM   1001 H  HB1  A ALA   A 1 38  ? 21.528 -0.516  -0.376  0.64 13.73 ?  38  ALA   A HB1  1 
ATOM   1002 H  HB1  B ALA   A 1 38  ? 21.621 -0.904  -0.441  0.36 13.49 ?  38  ALA   A HB1  1 
ATOM   1003 H  HB2  A ALA   A 1 38  ? 21.097 -1.061  1.053   0.64 13.73 ?  38  ALA   A HB2  1 
ATOM   1004 H  HB2  B ALA   A 1 38  ? 21.219 -1.467  0.990   0.36 13.49 ?  38  ALA   A HB2  1 
ATOM   1005 H  HB3  A ALA   A 1 38  ? 21.418 0.482   0.855   0.64 13.73 ?  38  ALA   A HB3  1 
ATOM   1006 H  HB3  B ALA   A 1 38  ? 21.327 0.100   0.752   0.36 13.49 ?  38  ALA   A HB3  1 
ATOM   1007 N  N    . ALA   A 1 39  ? 25.290 -0.068  0.063   1.00 10.99 ?  39  ALA   A N    1 
ATOM   1008 C  CA   . ALA   A 1 39  ? 26.313 0.833   -0.439  1.00 11.04 ?  39  ALA   A CA   1 
ATOM   1009 C  C    . ALA   A 1 39  ? 26.442 0.769   -1.956  1.00 10.64 ?  39  ALA   A C    1 
ATOM   1010 O  O    . ALA   A 1 39  ? 25.964 -0.158  -2.614  1.00 11.33 ?  39  ALA   A O    1 
ATOM   1011 C  CB   . ALA   A 1 39  ? 27.653 0.463   0.206   1.00 11.74 ?  39  ALA   A CB   1 
ATOM   1012 H  H    A ALA   A 1 39  ? 25.581 -0.858  0.251   0.64 13.17 ?  39  ALA   A H    1 
ATOM   1013 H  H    B ALA   A 1 39  ? 25.613 -0.829  0.309   0.36 13.17 ?  39  ALA   A H    1 
ATOM   1014 H  HA   . ALA   A 1 39  ? 26.088 1.745   -0.181  1.00 13.23 ?  39  ALA   A HA   1 
ATOM   1015 H  HB1  . ALA   A 1 39  ? 28.334 1.071   -0.122  1.00 14.08 ?  39  ALA   A HB1  1 
ATOM   1016 H  HB2  . ALA   A 1 39  ? 27.572 0.555   1.173   1.00 14.08 ?  39  ALA   A HB2  1 
ATOM   1017 H  HB3  . ALA   A 1 39  ? 27.872 -0.446  -0.024  1.00 14.08 ?  39  ALA   A HB3  1 
ATOM   1018 N  N    A ASN   A 1 40  ? 27.158 1.760   -2.495  0.64 11.12 ?  40  ASN   A N    1 
ATOM   1019 N  N    B ASN   A 1 40  ? 27.058 1.800   -2.523  0.36 10.86 ?  40  ASN   A N    1 
ATOM   1020 C  CA   A ASN   A 1 40  ? 27.726 1.718   -3.836  0.64 11.05 ?  40  ASN   A CA   1 
ATOM   1021 C  CA   B ASN   A 1 40  ? 27.507 1.749   -3.906  0.36 10.95 ?  40  ASN   A CA   1 
ATOM   1022 C  C    A ASN   A 1 40  ? 29.250 1.611   -3.743  0.64 10.27 ?  40  ASN   A C    1 
ATOM   1023 C  C    B ASN   A 1 40  ? 29.026 1.627   -3.923  0.36 10.37 ?  40  ASN   A C    1 
ATOM   1024 O  O    A ASN   A 1 40  ? 29.834 1.724   -2.662  0.64 10.57 ?  40  ASN   A O    1 
ATOM   1025 O  O    B ASN   A 1 40  ? 29.684 1.702   -2.885  0.36 10.50 ?  40  ASN   A O    1 
ATOM   1026 C  CB   A ASN   A 1 40  ? 27.249 2.898   -4.704  0.64 11.96 ?  40  ASN   A CB   1 
ATOM   1027 C  CB   B ASN   A 1 40  ? 27.023 2.964   -4.710  0.36 11.64 ?  40  ASN   A CB   1 
ATOM   1028 C  CG   A ASN   A 1 40  ? 27.626 4.255   -4.142  0.64 12.55 ?  40  ASN   A CG   1 
ATOM   1029 C  CG   B ASN   A 1 40  ? 27.405 4.279   -4.072  0.36 12.19 ?  40  ASN   A CG   1 
ATOM   1030 O  OD1  A ASN   A 1 40  ? 28.789 4.500   -3.806  0.64 13.17 ?  40  ASN   A OD1  1 
ATOM   1031 O  OD1  B ASN   A 1 40  ? 28.587 4.596   -3.930  0.36 13.18 ?  40  ASN   A OD1  1 
ATOM   1032 N  ND2  A ASN   A 1 40  ? 26.638 5.157   -4.055  0.64 12.97 ?  40  ASN   A ND2  1 
ATOM   1033 N  ND2  B ASN   A 1 40  ? 26.400 5.065   -3.701  0.36 12.37 ?  40  ASN   A ND2  1 
ATOM   1034 H  H    A ASN   A 1 40  ? 27.345 2.485   -2.077  0.64 13.33 ?  40  ASN   A H    1 
ATOM   1035 H  H    B ASN   A 1 40  ? 27.229 2.542   -2.124  0.36 13.01 ?  40  ASN   A H    1 
ATOM   1036 H  HA   A ASN   A 1 40  ? 27.423 0.910   -4.268  0.64 13.25 ?  40  ASN   A HA   1 
ATOM   1037 H  HA   B ASN   A 1 40  ? 27.134 0.951   -4.325  0.36 13.12 ?  40  ASN   A HA   1 
ATOM   1038 H  HB2  A ASN   A 1 40  ? 27.642 2.819   -5.589  0.64 14.34 ?  40  ASN   A HB2  1 
ATOM   1039 H  HB2  B ASN   A 1 40  ? 27.417 2.929   -5.594  0.36 13.95 ?  40  ASN   A HB2  1 
ATOM   1040 H  HB3  A ASN   A 1 40  ? 26.281 2.862   -4.772  0.64 14.34 ?  40  ASN   A HB3  1 
ATOM   1041 H  HB3  B ASN   A 1 40  ? 26.055 2.925   -4.780  0.36 13.95 ?  40  ASN   A HB3  1 
ATOM   1042 H  HD21 A ASN   A 1 40  ? 26.798 5.948   -3.747  0.64 15.55 ?  40  ASN   A HD21 1 
ATOM   1043 H  HD21 B ASN   A 1 40  ? 26.564 5.824   -3.335  0.36 14.82 ?  40  ASN   A HD21 1 
ATOM   1044 H  HD22 A ASN   A 1 40  ? 25.839 4.948   -4.294  0.64 15.55 ?  40  ASN   A HD22 1 
ATOM   1045 H  HD22 B ASN   A 1 40  ? 25.587 4.812   -3.824  0.36 14.82 ?  40  ASN   A HD22 1 
ATOM   1046 N  N    A VAL   A 1 41  ? 29.885 1.346   -4.891  0.64 10.70 ?  41  VAL   A N    1 
ATOM   1047 N  N    B VAL   A 1 41  ? 29.589 1.430   -5.118  0.36 10.65 ?  41  VAL   A N    1 
ATOM   1048 C  CA   A VAL   A 1 41  ? 31.315 1.033   -4.905  0.64 10.85 ?  41  VAL   A CA   1 
ATOM   1049 C  CA   B VAL   A 1 41  ? 31.011 1.105   -5.205  0.36 10.98 ?  41  VAL   A CA   1 
ATOM   1050 C  C    A VAL   A 1 41  ? 32.157 2.194   -4.412  0.64 10.85 ?  41  VAL   A C    1 
ATOM   1051 C  C    B VAL   A 1 41  ? 31.909 2.232   -4.714  0.36 10.78 ?  41  VAL   A C    1 
ATOM   1052 O  O    A VAL   A 1 41  ? 33.275 1.988   -3.922  0.64 10.76 ?  41  VAL   A O    1 
ATOM   1053 O  O    B VAL   A 1 41  ? 33.088 1.991   -4.423  0.36 10.15 ?  41  VAL   A O    1 
ATOM   1054 C  CB   A VAL   A 1 41  ? 31.805 0.533   -6.286  0.64 10.93 ?  41  VAL   A CB   1 
ATOM   1055 C  CB   B VAL   A 1 41  ? 31.425 0.690   -6.632  0.36 11.77 ?  41  VAL   A CB   1 
ATOM   1056 C  CG1  A VAL   A 1 41  ? 31.103 -0.758  -6.678  0.64 12.06 ?  41  VAL   A CG1  1 
ATOM   1057 C  CG1  B VAL   A 1 41  ? 30.815 -0.651  -6.996  0.36 12.63 ?  41  VAL   A CG1  1 
ATOM   1058 C  CG2  A VAL   A 1 41  ? 31.659 1.603   -7.378  0.64 10.95 ?  41  VAL   A CG2  1 
ATOM   1059 C  CG2  B VAL   A 1 41  ? 31.045 1.767   -7.641  0.36 12.34 ?  41  VAL   A CG2  1 
ATOM   1060 H  H    A VAL   A 1 41  ? 29.519 1.332   -5.662  0.64 12.83 ?  41  VAL   A H    1 
ATOM   1061 H  H    B VAL   A 1 41  ? 29.174 1.478   -5.871  0.36 12.76 ?  41  VAL   A H    1 
ATOM   1062 H  HA   A VAL   A 1 41  ? 31.479 0.315   -4.281  0.64 13.00 ?  41  VAL   A HA   1 
ATOM   1063 H  HA   B VAL   A 1 41  ? 31.165 0.334   -4.634  0.36 13.16 ?  41  VAL   A HA   1 
ATOM   1064 H  HB   A VAL   A 1 41  ? 32.754 0.329   -6.221  0.64 13.10 ?  41  VAL   A HB   1 
ATOM   1065 H  HB   B VAL   A 1 41  ? 32.390 0.594   -6.652  0.36 14.11 ?  41  VAL   A HB   1 
ATOM   1066 H  HG11 A VAL   A 1 41  ? 31.444 -1.064  -7.535  0.64 14.45 ?  41  VAL   A HG11 1 
ATOM   1067 H  HG11 B VAL   A 1 41  ? 31.082 -0.883  -7.897  0.36 15.14 ?  41  VAL   A HG11 1 
ATOM   1068 H  HG12 A VAL   A 1 41  ? 31.268 -1.429  -5.998  0.64 14.45 ?  41  VAL   A HG12 1 
ATOM   1069 H  HG12 B VAL   A 1 41  ? 31.136 -1.324  -6.372  0.36 15.14 ?  41  VAL   A HG12 1 
ATOM   1070 H  HG13 A VAL   A 1 41  ? 30.148 -0.589  -6.748  0.64 14.45 ?  41  VAL   A HG13 1 
ATOM   1071 H  HG13 B VAL   A 1 41  ? 29.849 -0.586  -6.941  0.36 15.14 ?  41  VAL   A HG13 1 
ATOM   1072 H  HG21 A VAL   A 1 41  ? 31.890 1.208   -8.239  0.64 13.13 ?  41  VAL   A HG21 1 
ATOM   1073 H  HG21 B VAL   A 1 41  ? 31.415 1.529   -8.504  0.36 14.79 ?  41  VAL   A HG21 1 
ATOM   1074 H  HG22 A VAL   A 1 41  ? 30.747 1.916   -7.393  0.64 13.13 ?  41  VAL   A HG22 1 
ATOM   1075 H  HG22 B VAL   A 1 41  ? 30.078 1.821   -7.700  0.36 14.79 ?  41  VAL   A HG22 1 
ATOM   1076 H  HG23 A VAL   A 1 41  ? 32.265 2.336   -7.185  0.64 13.13 ?  41  VAL   A HG23 1 
ATOM   1077 H  HG23 B VAL   A 1 41  ? 31.406 2.618   -7.349  0.36 14.79 ?  41  VAL   A HG23 1 
ATOM   1078 N  N    A TYR   A 1 42  ? 31.664 3.424   -4.559  0.64 11.42 ?  42  TYR   A N    1 
ATOM   1079 N  N    B TYR   A 1 42  ? 31.404 3.468   -4.658  0.36 11.44 ?  42  TYR   A N    1 
ATOM   1080 C  CA   A TYR   A 1 42  ? 32.374 4.624   -4.140  0.64 11.81 ?  42  TYR   A CA   1 
ATOM   1081 C  CA   B TYR   A 1 42  ? 32.202 4.617   -4.237  0.36 11.73 ?  42  TYR   A CA   1 
ATOM   1082 C  C    A TYR   A 1 42  ? 32.084 4.989   -2.697  0.64 11.51 ?  42  TYR   A C    1 
ATOM   1083 C  C    B TYR   A 1 42  ? 31.988 5.011   -2.782  0.36 11.45 ?  42  TYR   A C    1 
ATOM   1084 O  O    A TYR   A 1 42  ? 32.652 5.966   -2.186  0.64 12.04 ?  42  TYR   A O    1 
ATOM   1085 O  O    B TYR   A 1 42  ? 32.539 6.026   -2.342  0.36 11.81 ?  42  TYR   A O    1 
ATOM   1086 C  CB   A TYR   A 1 42  ? 32.009 5.804   -5.064  0.64 12.47 ?  42  TYR   A CB   1 
ATOM   1087 C  CB   B TYR   A 1 42  ? 31.903 5.828   -5.128  0.36 12.37 ?  42  TYR   A CB   1 
ATOM   1088 C  CG   A TYR   A 1 42  ? 32.208 5.482   -6.531  0.64 12.96 ?  42  TYR   A CG   1 
ATOM   1089 C  CG   B TYR   A 1 42  ? 32.055 5.540   -6.598  0.36 13.07 ?  42  TYR   A CG   1 
ATOM   1090 C  CD1  A TYR   A 1 42  ? 33.478 5.293   -7.047  0.64 13.62 ?  42  TYR   A CD1  1 
ATOM   1091 C  CD1  B TYR   A 1 42  ? 33.306 5.327   -7.156  0.36 13.43 ?  42  TYR   A CD1  1 
ATOM   1092 C  CD2  A TYR   A 1 42  ? 31.127 5.334   -7.391  0.64 14.14 ?  42  TYR   A CD2  1 
ATOM   1093 C  CD2  B TYR   A 1 42  ? 30.948 5.479   -7.428  0.36 14.21 ?  42  TYR   A CD2  1 
ATOM   1094 C  CE1  A TYR   A 1 42  ? 33.672 4.974   -8.378  0.64 14.10 ?  42  TYR   A CE1  1 
ATOM   1095 C  CE1  B TYR   A 1 42  ? 33.448 5.054   -8.503  0.36 13.99 ?  42  TYR   A CE1  1 
ATOM   1096 C  CE2  A TYR   A 1 42  ? 31.314 5.025   -8.730  0.64 15.01 ?  42  TYR   A CE2  1 
ATOM   1097 C  CE2  B TYR   A 1 42  ? 31.079 5.217   -8.772  0.36 14.90 ?  42  TYR   A CE2  1 
ATOM   1098 C  CZ   A TYR   A 1 42  ? 32.591 4.846   -9.216  0.64 14.79 ?  42  TYR   A CZ   1 
ATOM   1099 C  CZ   B TYR   A 1 42  ? 32.328 5.002   -9.307  0.36 14.69 ?  42  TYR   A CZ   1 
ATOM   1100 O  OH   A TYR   A 1 42  ? 32.791 4.529   -10.539 0.64 15.96 ?  42  TYR   A OH   1 
ATOM   1101 O  OH   B TYR   A 1 42  ? 32.453 4.739   -10.650 0.36 15.56 ?  42  TYR   A OH   1 
ATOM   1102 H  H    A TYR   A 1 42  ? 30.897 3.591   -4.900  0.64 13.69 ?  42  TYR   A H    1 
ATOM   1103 H  H    B TYR   A 1 42  ? 30.596 3.670   -4.896  0.36 13.71 ?  42  TYR   A H    1 
ATOM   1104 H  HA   A TYR   A 1 42  ? 33.332 4.481   -4.223  0.64 14.16 ?  42  TYR   A HA   1 
ATOM   1105 H  HA   B TYR   A 1 42  ? 33.136 4.395   -4.353  0.36 14.06 ?  42  TYR   A HA   1 
ATOM   1106 H  HB2  A TYR   A 1 42  ? 31.074 6.033   -4.929  0.64 14.95 ?  42  TYR   A HB2  1 
ATOM   1107 H  HB2  B TYR   A 1 42  ? 30.988 6.115   -4.972  0.36 14.83 ?  42  TYR   A HB2  1 
ATOM   1108 H  HB3  A TYR   A 1 42  ? 32.569 6.568   -4.846  0.64 14.95 ?  42  TYR   A HB3  1 
ATOM   1109 H  HB3  B TYR   A 1 42  ? 32.516 6.543   -4.896  0.36 14.83 ?  42  TYR   A HB3  1 
ATOM   1110 H  HD1  A TYR   A 1 42  ? 34.217 5.378   -6.487  0.64 16.33 ?  42  TYR   A HD1  1 
ATOM   1111 H  HD1  B TYR   A 1 42  ? 34.062 5.359   -6.612  0.36 16.10 ?  42  TYR   A HD1  1 
ATOM   1112 H  HD2  A TYR   A 1 42  ? 30.262 5.458   -7.065  0.64 16.96 ?  42  TYR   A HD2  1 
ATOM   1113 H  HD2  B TYR   A 1 42  ? 30.101 5.623   -7.069  0.36 17.04 ?  42  TYR   A HD2  1 
ATOM   1114 H  HE1  A TYR   A 1 42  ? 34.533 4.859   -8.711  0.64 16.90 ?  42  TYR   A HE1  1 
ATOM   1115 H  HE1  B TYR   A 1 42  ? 34.294 4.913   -8.864  0.36 16.77 ?  42  TYR   A HE1  1 
ATOM   1116 H  HE2  A TYR   A 1 42  ? 30.577 4.938   -9.297  0.64 18.00 ?  42  TYR   A HE2  1 
ATOM   1117 H  HE2  B TYR   A 1 42  ? 30.326 5.180   -9.315  0.36 17.87 ?  42  TYR   A HE2  1 
ATOM   1118 H  HH   A TYR   A 1 42  ? 33.612 4.433   -10.690 0.64 19.14 ?  42  TYR   A HH   1 
ATOM   1119 H  HH   B TYR   A 1 42  ? 31.698 4.740   -11.013 0.36 18.66 ?  42  TYR   A HH   1 
ATOM   1120 N  N    . LEU   A 1 43  ? 31.199 4.237   -2.037  1.00 11.21 ?  43  LEU   A N    1 
ATOM   1121 C  CA   . LEU   A 1 43  ? 30.764 4.581   -0.686  1.00 10.99 ?  43  LEU   A CA   1 
ATOM   1122 C  C    . LEU   A 1 43  ? 30.278 6.028   -0.596  1.00 11.10 ?  43  LEU   A C    1 
ATOM   1123 O  O    . LEU   A 1 43  ? 30.535 6.733   0.380   1.00 12.19 ?  43  LEU   A O    1 
ATOM   1124 C  CB   . LEU   A 1 43  ? 31.811 4.273   0.379   1.00 11.43 ?  43  LEU   A CB   1 
ATOM   1125 C  CG   . LEU   A 1 43  ? 32.305 2.823   0.464   1.00 11.93 ?  43  LEU   A CG   1 
ATOM   1126 C  CD1  . LEU   A 1 43  ? 33.351 2.712   1.557   1.00 12.68 ?  43  LEU   A CD1  1 
ATOM   1127 C  CD2  . LEU   A 1 43  ? 31.163 1.843   0.705   1.00 12.24 ?  43  LEU   A CD2  1 
ATOM   1128 H  H    A LEU   A 1 43  ? 30.839 3.516   -2.348  0.64 13.43 ?  43  LEU   A H    1 
ATOM   1129 H  H    B LEU   A 1 43  ? 30.889 3.476   -2.303  0.36 13.43 ?  43  LEU   A H    1 
ATOM   1130 H  HA   . LEU   A 1 43  ? 29.996 4.021   -0.478  1.00 13.17 ?  43  LEU   A HA   1 
ATOM   1131 H  HB2  . LEU   A 1 43  ? 32.582 4.837   0.217   1.00 13.71 ?  43  LEU   A HB2  1 
ATOM   1132 H  HB3  . LEU   A 1 43  ? 31.428 4.497   1.247   1.00 13.71 ?  43  LEU   A HB3  1 
ATOM   1133 H  HG   . LEU   A 1 43  ? 32.728 2.588   -0.376  1.00 14.30 ?  43  LEU   A HG   1 
ATOM   1134 H  HD11 . LEU   A 1 43  ? 33.661 1.792   1.604   1.00 15.20 ?  43  LEU   A HD11 1 
ATOM   1135 H  HD12 . LEU   A 1 43  ? 34.092 3.300   1.348   1.00 15.20 ?  43  LEU   A HD12 1 
ATOM   1136 H  HD13 . LEU   A 1 43  ? 32.952 2.968   2.404   1.00 15.20 ?  43  LEU   A HD13 1 
ATOM   1137 H  HD21 . LEU   A 1 43  ? 31.537 0.960   0.847   1.00 14.68 ?  43  LEU   A HD21 1 
ATOM   1138 H  HD22 . LEU   A 1 43  ? 30.669 2.127   1.487   1.00 14.68 ?  43  LEU   A HD22 1 
ATOM   1139 H  HD23 . LEU   A 1 43  ? 30.586 1.840   -0.073  1.00 14.68 ?  43  LEU   A HD23 1 
ATOM   1140 N  N    A LYS   A 1 44  ? 29.551 6.468   -1.622  0.64 11.25 ?  44  LYS   A N    1 
ATOM   1141 N  N    B LYS   A 1 44  ? 29.562 6.466   -1.633  0.36 11.60 ?  44  LYS   A N    1 
ATOM   1142 C  CA   A LYS   A 1 44  ? 28.911 7.783   -1.609  0.64 11.50 ?  44  LYS   A CA   1 
ATOM   1143 C  CA   B LYS   A 1 44  ? 28.891 7.762   -1.639  0.36 12.26 ?  44  LYS   A CA   1 
ATOM   1144 C  C    A LYS   A 1 44  ? 27.480 7.596   -1.127  0.64 11.19 ?  44  LYS   A C    1 
ATOM   1145 C  C    B LYS   A 1 44  ? 27.478 7.549   -1.113  0.36 11.52 ?  44  LYS   A C    1 
ATOM   1146 O  O    A LYS   A 1 44  ? 26.613 7.116   -1.863  0.64 12.38 ?  44  LYS   A O    1 
ATOM   1147 O  O    B LYS   A 1 44  ? 26.622 6.992   -1.810  0.36 11.98 ?  44  LYS   A O    1 
ATOM   1148 C  CB   A LYS   A 1 44  ? 28.974 8.432   -2.983  0.64 13.62 ?  44  LYS   A CB   1 
ATOM   1149 C  CB   B LYS   A 1 44  ? 28.870 8.346   -3.049  0.36 14.52 ?  44  LYS   A CB   1 
ATOM   1150 C  CG   A LYS   A 1 44  ? 30.371 8.858   -3.399  0.64 16.77 ?  44  LYS   A CG   1 
ATOM   1151 C  CG   B LYS   A 1 44  ? 30.211 8.862   -3.540  0.36 17.21 ?  44  LYS   A CG   1 
ATOM   1152 C  CD   A LYS   A 1 44  ? 31.042 9.758   -2.367  0.64 21.41 ?  44  LYS   A CD   1 
ATOM   1153 C  CD   B LYS   A 1 44  ? 30.843 9.824   -2.544  0.36 20.31 ?  44  LYS   A CD   1 
ATOM   1154 C  CE   A LYS   A 1 44  ? 32.379 10.266  -2.868  0.64 24.12 ?  44  LYS   A CE   1 
ATOM   1155 C  CE   B LYS   A 1 44  ? 32.014 10.561  -3.165  0.36 22.18 ?  44  LYS   A CE   1 
ATOM   1156 N  NZ   A LYS   A 1 44  ? 33.182 10.876  -1.777  0.64 25.48 ?  44  LYS   A NZ   1 
ATOM   1157 N  NZ   B LYS   A 1 44  ? 32.897 11.181  -2.141  0.36 23.66 ?  44  LYS   A NZ   1 
ATOM   1158 H  H    A LYS   A 1 44  ? 29.418 6.020   -2.346  0.64 13.48 ?  44  LYS   A H    1 
ATOM   1159 H  H    B LYS   A 1 44  ? 29.446 6.015   -2.358  0.36 13.90 ?  44  LYS   A H    1 
ATOM   1160 H  HA   A LYS   A 1 44  ? 29.359 8.347   -0.965  0.64 13.79 ?  44  LYS   A HA   1 
ATOM   1161 H  HA   B LYS   A 1 44  ? 29.348 8.375   -1.042  0.36 14.70 ?  44  LYS   A HA   1 
ATOM   1162 H  HB2  A LYS   A 1 44  ? 28.646 7.805   -3.644  0.64 16.33 ?  44  LYS   A HB2  1 
ATOM   1163 H  HB2  B LYS   A 1 44  ? 28.580 7.659   -3.669  0.36 17.41 ?  44  LYS   A HB2  1 
ATOM   1164 H  HB3  A LYS   A 1 44  ? 28.415 9.226   -2.975  0.64 16.33 ?  44  LYS   A HB3  1 
ATOM   1165 H  HB3  B LYS   A 1 44  ? 28.249 9.091   -3.073  0.36 17.41 ?  44  LYS   A HB3  1 
ATOM   1166 H  HG2  A LYS   A 1 44  ? 30.925 8.068   -3.512  0.64 20.10 ?  44  LYS   A HG2  1 
ATOM   1167 H  HG2  B LYS   A 1 44  ? 30.817 8.114   -3.667  0.36 20.64 ?  44  LYS   A HG2  1 
ATOM   1168 H  HG3  A LYS   A 1 44  ? 30.321 9.349   -4.235  0.64 20.10 ?  44  LYS   A HG3  1 
ATOM   1169 H  HG3  B LYS   A 1 44  ? 30.088 9.337   -4.379  0.36 20.64 ?  44  LYS   A HG3  1 
ATOM   1170 H  HD2  A LYS   A 1 44  ? 30.466 10.516  -2.183  0.64 25.68 ?  44  LYS   A HD2  1 
ATOM   1171 H  HD2  B LYS   A 1 44  ? 30.179 10.471  -2.259  0.36 24.36 ?  44  LYS   A HD2  1 
ATOM   1172 H  HD3  A LYS   A 1 44  ? 31.201 9.251   -1.554  0.64 25.68 ?  44  LYS   A HD3  1 
ATOM   1173 H  HD3  B LYS   A 1 44  ? 31.171 9.320   -1.779  0.36 24.36 ?  44  LYS   A HD3  1 
ATOM   1174 H  HE2  A LYS   A 1 44  ? 32.883 9.524   -3.237  0.64 28.93 ?  44  LYS   A HE2  1 
ATOM   1175 H  HE2  B LYS   A 1 44  ? 32.544 9.932   -3.681  0.36 26.60 ?  44  LYS   A HE2  1 
ATOM   1176 H  HE3  A LYS   A 1 44  ? 32.227 10.939  -3.549  0.64 28.93 ?  44  LYS   A HE3  1 
ATOM   1177 H  HE3  B LYS   A 1 44  ? 31.675 11.263  -3.739  0.36 26.60 ?  44  LYS   A HE3  1 
ATOM   1178 H  HZ1  A LYS   A 1 44  ? 33.957 11.168  -2.098  0.64 30.56 ?  44  LYS   A HZ1  1 
ATOM   1179 H  HZ1  B LYS   A 1 44  ? 33.572 11.603  -2.539  0.36 28.37 ?  44  LYS   A HZ1  1 
ATOM   1180 H  HZ2  A LYS   A 1 44  ? 32.737 11.565  -1.424  0.64 30.56 ?  44  LYS   A HZ2  1 
ATOM   1181 H  HZ2  B LYS   A 1 44  ? 32.436 11.765  -1.655  0.36 28.37 ?  44  LYS   A HZ2  1 
ATOM   1182 H  HZ3  A LYS   A 1 44  ? 33.335 10.277  -1.140  0.64 30.56 ?  44  LYS   A HZ3  1 
ATOM   1183 H  HZ3  B LYS   A 1 44  ? 33.227 10.553  -1.602  0.36 28.37 ?  44  LYS   A HZ3  1 
ATOM   1184 N  N    . HIS   A 1 45  ? 27.237 7.971   0.127   1.00 10.94 ?  45  HIS   A N    1 
ATOM   1185 C  CA   . HIS   A 1 45  ? 26.002 7.629   0.825   1.00 10.88 ?  45  HIS   A CA   1 
ATOM   1186 C  C    . HIS   A 1 45  ? 24.977 8.746   0.657   1.00 11.60 ?  45  HIS   A C    1 
ATOM   1187 O  O    . HIS   A 1 45  ? 24.695 9.516   1.575   1.00 13.57 ?  45  HIS   A O    1 
ATOM   1188 C  CB   . HIS   A 1 45  ? 26.294 7.378   2.291   1.00 10.77 ?  45  HIS   A CB   1 
ATOM   1189 C  CG   . HIS   A 1 45  ? 27.407 6.414   2.523   1.00 10.61 ?  45  HIS   A CG   1 
ATOM   1190 N  ND1  . HIS   A 1 45  ? 27.401 5.125   2.030   1.00 11.11 ?  45  HIS   A ND1  1 
ATOM   1191 C  CD2  . HIS   A 1 45  ? 28.575 6.572   3.190   1.00 10.85 ?  45  HIS   A CD2  1 
ATOM   1192 C  CE1  . HIS   A 1 45  ? 28.525 4.534   2.398   1.00 11.05 ?  45  HIS   A CE1  1 
ATOM   1193 N  NE2  . HIS   A 1 45  ? 29.254 5.388   3.098   1.00 11.12 ?  45  HIS   A NE2  1 
ATOM   1194 H  H    A HIS   A 1 45  ? 27.784 8.438   0.600   0.64 13.12 ?  45  HIS   A H    1 
ATOM   1195 H  H    B HIS   A 1 45  ? 27.780 8.452   0.590   0.36 13.12 ?  45  HIS   A H    1 
ATOM   1196 H  HA   . HIS   A 1 45  ? 25.630 6.817   0.443   1.00 13.04 ?  45  HIS   A HA   1 
ATOM   1197 H  HB2  . HIS   A 1 45  ? 26.526 8.220   2.712   1.00 12.90 ?  45  HIS   A HB2  1 
ATOM   1198 H  HB3  . HIS   A 1 45  ? 25.491 7.016   2.710   1.00 12.90 ?  45  HIS   A HB3  1 
ATOM   1199 H  HD2  . HIS   A 1 45  ? 28.867 7.349   3.623   1.00 13.00 ?  45  HIS   A HD2  1 
ATOM   1200 H  HE1  . HIS   A 1 45  ? 28.761 3.656   2.213   1.00 13.24 ?  45  HIS   A HE1  1 
ATOM   1201 H  HE2  . HIS   A 1 45  ? 30.027 5.227   3.447   1.00 13.32 ?  45  HIS   A HE2  1 
ATOM   1202 N  N    . GLY   A 1 46  ? 24.394 8.814   -0.533  1.00 12.87 ?  46  GLY   A N    1 
ATOM   1203 C  CA   . GLY   A 1 46  ? 23.568 9.957   -0.872  1.00 13.51 ?  46  GLY   A CA   1 
ATOM   1204 C  C    . GLY   A 1 46  ? 22.087 9.823   -0.574  1.00 13.45 ?  46  GLY   A C    1 
ATOM   1205 O  O    . GLY   A 1 46  ? 21.435 10.815  -0.231  1.00 14.86 ?  46  GLY   A O    1 
ATOM   1206 H  H    . GLY   A 1 46  ? 24.460 8.225   -1.152  1.00 15.43 ?  46  GLY   A H    1 
ATOM   1207 H  HA2  . GLY   A 1 46  ? 23.889 10.736  -0.387  1.00 16.20 ?  46  GLY   A HA2  1 
ATOM   1208 H  HA3  . GLY   A 1 46  ? 23.658 10.143  -1.818  1.00 16.20 ?  46  GLY   A HA3  1 
ATOM   1209 N  N    A GLY   A 1 47  ? 21.549 8.626   -0.757  0.64 13.39 ?  47  GLY   A N    1 
ATOM   1210 N  N    B GLY   A 1 47  ? 21.535 8.610   -0.657  0.36 12.96 ?  47  GLY   A N    1 
ATOM   1211 C  CA   A GLY   A 1 47  ? 20.115 8.424   -0.728  0.64 13.61 ?  47  GLY   A CA   1 
ATOM   1212 C  CA   B GLY   A 1 47  ? 20.102 8.420   -0.490  0.36 12.64 ?  47  GLY   A CA   1 
ATOM   1213 C  C    A GLY   A 1 47  ? 19.818 6.980   -0.395  0.64 12.89 ?  47  GLY   A C    1 
ATOM   1214 C  C    B GLY   A 1 47  ? 19.742 7.009   -0.066  0.36 11.44 ?  47  GLY   A C    1 
ATOM   1215 O  O    A GLY   A 1 47  ? 20.723 6.164   -0.206  0.64 12.94 ?  47  GLY   A O    1 
ATOM   1216 O  O    B GLY   A 1 47  ? 20.610 6.153   0.119   0.36 11.18 ?  47  GLY   A O    1 
ATOM   1217 H  H    A GLY   A 1 47  ? 22.000 7.907   -0.881  0.64 16.05 ?  47  GLY   A H    1 
ATOM   1218 H  H    B GLY   A 1 47  ? 21.968 7.883   -0.795  0.36 15.53 ?  47  GLY   A H    1 
ATOM   1219 H  HA2  A GLY   A 1 47  ? 19.708 9.006   -0.064  0.64 16.32 ?  47  GLY   A HA2  1 
ATOM   1220 H  HA2  B GLY   A 1 47  ? 19.764 9.026   0.185   0.36 15.15 ?  47  GLY   A HA2  1 
ATOM   1221 H  HA3  A GLY   A 1 47  ? 19.739 8.632   -1.599  0.64 16.32 ?  47  GLY   A HA3  1 
ATOM   1222 H  HA3  B GLY   A 1 47  ? 19.652 8.613   -1.328  0.36 15.15 ?  47  GLY   A HA3  1 
ATOM   1223 N  N    A GLY   A 1 48  ? 18.532 6.659   -0.350  0.64 12.73 ?  48  GLY   A N    1 
ATOM   1224 N  N    B GLY   A 1 48  ? 18.434 6.775   0.089   0.36 11.75 ?  48  GLY   A N    1 
ATOM   1225 C  CA   A GLY   A 1 48  ? 18.151 5.332   0.070   0.64 12.79 ?  48  GLY   A CA   1 
ATOM   1226 C  CA   B GLY   A 1 48  ? 17.948 5.457   0.478   0.36 11.17 ?  48  GLY   A CA   1 
ATOM   1227 C  C    A GLY   A 1 48  ? 18.611 5.062   1.490   0.64 12.36 ?  48  GLY   A C    1 
ATOM   1228 C  C    B GLY   A 1 48  ? 18.522 5.023   1.811   0.36 11.35 ?  48  GLY   A C    1 
ATOM   1229 O  O    A GLY   A 1 48  ? 18.776 5.977   2.308   0.64 12.39 ?  48  GLY   A O    1 
ATOM   1230 O  O    B GLY   A 1 48  ? 18.692 5.825   2.738   0.36 11.62 ?  48  GLY   A O    1 
ATOM   1231 H  H    A GLY   A 1 48  ? 17.881 7.180   -0.549  0.64 15.26 ?  48  GLY   A H    1 
ATOM   1232 H  H    B GLY   A 1 48  ? 17.800 7.356   -0.019  0.36 14.09 ?  48  GLY   A H    1 
ATOM   1233 H  HA2  A GLY   A 1 48  ? 17.192 5.234   0.028   0.64 15.33 ?  48  GLY   A HA2  1 
ATOM   1234 H  HA2  B GLY   A 1 48  ? 16.974 5.459   0.543   0.36 13.39 ?  48  GLY   A HA2  1 
ATOM   1235 H  HA3  A GLY   A 1 48  ? 18.563 4.674   -0.512  0.64 15.33 ?  48  GLY   A HA3  1 
ATOM   1236 H  HA3  B GLY   A 1 48  ? 18.202 4.797   -0.188  0.36 13.39 ?  48  GLY   A HA3  1 
ATOM   1237 N  N    A VAL   A 1 49  ? 18.831 3.778   1.784   0.64 12.26 ?  49  VAL   A N    1 
ATOM   1238 N  N    B VAL   A 1 49  ? 18.818 3.726   1.909   0.36 11.11 ?  49  VAL   A N    1 
ATOM   1239 C  CA   A VAL   A 1 49  ? 19.317 3.378   3.103   0.64 12.13 ?  49  VAL   A CA   1 
ATOM   1240 C  CA   B VAL   A 1 49  ? 19.413 3.174   3.122   0.36 10.99 ?  49  VAL   A CA   1 
ATOM   1241 C  C    A VAL   A 1 49  ? 20.628 4.085   3.434   0.64 10.96 ?  49  VAL   A C    1 
ATOM   1242 C  C    B VAL   A 1 49  ? 20.696 3.915   3.471   0.36 10.44 ?  49  VAL   A C    1 
ATOM   1243 O  O    A VAL   A 1 49  ? 20.822 4.560   4.556   0.64 11.54 ?  49  VAL   A O    1 
ATOM   1244 O  O    B VAL   A 1 49  ? 20.931 4.268   4.631   0.36 9.94  ?  49  VAL   A O    1 
ATOM   1245 C  CB   A VAL   A 1 49  ? 19.464 1.845   3.171   0.64 12.92 ?  49  VAL   A CB   1 
ATOM   1246 C  CB   B VAL   A 1 49  ? 19.667 1.666   2.946   0.36 10.82 ?  49  VAL   A CB   1 
ATOM   1247 C  CG1  A VAL   A 1 49  ? 20.265 1.418   4.399   0.64 12.94 ?  49  VAL   A CG1  1 
ATOM   1248 C  CG1  B VAL   A 1 49  ? 20.531 1.134   4.077   0.36 10.21 ?  49  VAL   A CG1  1 
ATOM   1249 C  CG2  A VAL   A 1 49  ? 18.093 1.183   3.180   0.64 14.56 ?  49  VAL   A CG2  1 
ATOM   1250 C  CG2  B VAL   A 1 49  ? 18.352 0.900   2.864   0.36 11.27 ?  49  VAL   A CG2  1 
ATOM   1251 H  H    A VAL   A 1 49  ? 18.705 3.119   1.243   0.64 14.70 ?  49  VAL   A H    1 
ATOM   1252 H  H    B VAL   A 1 49  ? 18.686 3.146   1.291   0.36 13.31 ?  49  VAL   A H    1 
ATOM   1253 H  HA   A VAL   A 1 49  ? 18.666 3.633   3.773   0.64 14.54 ?  49  VAL   A HA   1 
ATOM   1254 H  HA   B VAL   A 1 49  ? 18.799 3.285   3.862   0.36 13.18 ?  49  VAL   A HA   1 
ATOM   1255 H  HB   A VAL   A 1 49  ? 19.943 1.532   2.386   0.64 15.48 ?  49  VAL   A HB   1 
ATOM   1256 H  HB   B VAL   A 1 49  ? 20.147 1.521   2.116   0.36 12.96 ?  49  VAL   A HB   1 
ATOM   1257 H  HG11 A VAL   A 1 49  ? 20.109 0.475   4.567   0.64 15.51 ?  49  VAL   A HG11 1 
ATOM   1258 H  HG11 B VAL   A 1 49  ? 20.440 0.169   4.115   0.36 12.24 ?  49  VAL   A HG11 1 
ATOM   1259 H  HG12 A VAL   A 1 49  ? 21.209 1.571   4.234   0.64 15.51 ?  49  VAL   A HG12 1 
ATOM   1260 H  HG12 B VAL   A 1 49  ? 21.459 1.369   3.906   0.36 12.24 ?  49  VAL   A HG12 1 
ATOM   1261 H  HG13 A VAL   A 1 49  ? 19.971 1.940   5.163   0.64 15.51 ?  49  VAL   A HG13 1 
ATOM   1262 H  HG13 B VAL   A 1 49  ? 20.237 1.527   4.912   0.36 12.24 ?  49  VAL   A HG13 1 
ATOM   1263 H  HG21 A VAL   A 1 49  ? 18.207 0.221   3.214   0.64 17.46 ?  49  VAL   A HG21 1 
ATOM   1264 H  HG21 B VAL   A 1 49  ? 18.539 -0.043  2.750   0.36 13.50 ?  49  VAL   A HG21 1 
ATOM   1265 H  HG22 A VAL   A 1 49  ? 17.604 1.489   3.959   0.64 17.46 ?  49  VAL   A HG22 1 
ATOM   1266 H  HG22 B VAL   A 1 49  ? 17.853 1.044   3.685   0.36 13.50 ?  49  VAL   A HG22 1 
ATOM   1267 H  HG23 A VAL   A 1 49  ? 17.623 1.434   2.371   0.64 17.46 ?  49  VAL   A HG23 1 
ATOM   1268 H  HG23 B VAL   A 1 49  ? 17.843 1.233   2.108   0.36 13.50 ?  49  VAL   A HG23 1 
ATOM   1269 N  N    . ALA   A 1 50  ? 21.560 4.125   2.477   1.00 10.56 ?  50  ALA   A N    1 
ATOM   1270 C  CA   . ALA   A 1 50  ? 22.877 4.697   2.746   1.00 10.46 ?  50  ALA   A CA   1 
ATOM   1271 C  C    . ALA   A 1 50  ? 22.775 6.155   3.170   1.00 10.64 ?  50  ALA   A C    1 
ATOM   1272 O  O    . ALA   A 1 50  ? 23.404 6.577   4.148   1.00 10.96 ?  50  ALA   A O    1 
ATOM   1273 C  CB   . ALA   A 1 50  ? 23.761 4.567   1.508   1.00 10.33 ?  50  ALA   A CB   1 
ATOM   1274 H  H    A ALA   A 1 50  ? 21.456 3.833   1.676   0.64 12.66 ?  50  ALA   A H    1 
ATOM   1275 H  H    B ALA   A 1 50  ? 21.410 3.946   1.651   0.36 12.66 ?  50  ALA   A H    1 
ATOM   1276 H  HA   . ALA   A 1 50  ? 23.299 4.209   3.472   1.00 12.53 ?  50  ALA   A HA   1 
ATOM   1277 H  HB1  . ALA   A 1 50  ? 24.631 4.955   1.699   1.00 12.38 ?  50  ALA   A HB1  1 
ATOM   1278 H  HB2  . ALA   A 1 50  ? 23.856 3.633   1.281   1.00 12.38 ?  50  ALA   A HB2  1 
ATOM   1279 H  HB3  . ALA   A 1 50  ? 23.343 5.048   0.773   1.00 12.38 ?  50  ALA   A HB3  1 
ATOM   1280 N  N    . GLY   A 1 51  ? 21.981 6.942   2.443   1.00 10.89 ?  51  GLY   A N    1 
ATOM   1281 C  CA   . GLY   A 1 51  ? 21.811 8.332   2.823   1.00 11.39 ?  51  GLY   A CA   1 
ATOM   1282 C  C    . GLY   A 1 51  ? 21.216 8.470   4.208   1.00 11.24 ?  51  GLY   A C    1 
ATOM   1283 O  O    . GLY   A 1 51  ? 21.598 9.359   4.975   1.00 11.82 ?  51  GLY   A O    1 
ATOM   1284 H  H    . GLY   A 1 51  ? 21.554 6.697   1.736   1.00 13.05 ?  51  GLY   A H    1 
ATOM   1285 H  HA2  . GLY   A 1 51  ? 22.666 8.784   2.802   1.00 13.65 ?  51  GLY   A HA2  1 
ATOM   1286 H  HA3  . GLY   A 1 51  ? 21.217 8.768   2.186   1.00 13.65 ?  51  GLY   A HA3  1 
ATOM   1287 N  N    . ALA   A 1 52  ? 20.250 7.605   4.537   1.00 11.47 ?  52  ALA   A N    1 
ATOM   1288 C  CA   . ALA   A 1 52  ? 19.603 7.663   5.842   1.00 11.92 ?  52  ALA   A CA   1 
ATOM   1289 C  C    . ALA   A 1 52  ? 20.559 7.256   6.964   1.00 11.42 ?  52  ALA   A C    1 
ATOM   1290 O  O    . ALA   A 1 52  ? 20.628 7.920   8.004   1.00 12.44 ?  52  ALA   A O    1 
ATOM   1291 C  CB   . ALA   A 1 52  ? 18.341 6.796   5.841   1.00 13.41 ?  52  ALA   A CB   1 
ATOM   1292 H  H    . ALA   A 1 52  ? 19.974 6.965   4.027   1.00 13.75 ?  52  ALA   A H    1 
ATOM   1293 H  HA   . ALA   A 1 52  ? 19.330 8.574   6.005   1.00 14.29 ?  52  ALA   A HA   1 
ATOM   1294 H  HB1  . ALA   A 1 52  ? 17.912 6.861   6.712   1.00 16.08 ?  52  ALA   A HB1  1 
ATOM   1295 H  HB2  . ALA   A 1 52  ? 17.733 7.122   5.155   1.00 16.08 ?  52  ALA   A HB2  1 
ATOM   1296 H  HB3  . ALA   A 1 52  ? 18.580 5.876   5.659   1.00 16.08 ?  52  ALA   A HB3  1 
ATOM   1297 N  N    A LEU   A 1 53  ? 21.290 6.154   6.787   0.64 11.23 ?  53  LEU   A N    1 
ATOM   1298 N  N    B LEU   A 1 53  ? 21.307 6.164   6.768   0.36 11.02 ?  53  LEU   A N    1 
ATOM   1299 C  CA   A LEU   A 1 53  ? 22.266 5.766   7.802   0.64 11.68 ?  53  LEU   A CA   1 
ATOM   1300 C  CA   B LEU   A 1 53  ? 22.273 5.736   7.779   0.36 11.06 ?  53  LEU   A CA   1 
ATOM   1301 C  C    A LEU   A 1 53  ? 23.294 6.869   7.996   0.64 10.99 ?  53  LEU   A C    1 
ATOM   1302 C  C    B LEU   A 1 53  ? 23.351 6.790   7.985   0.36 10.72 ?  53  LEU   A C    1 
ATOM   1303 O  O    A LEU   A 1 53  ? 23.576 7.284   9.126   0.64 11.91 ?  53  LEU   A O    1 
ATOM   1304 O  O    B LEU   A 1 53  ? 23.752 7.066   9.121   0.36 11.16 ?  53  LEU   A O    1 
ATOM   1305 C  CB   A LEU   A 1 53  ? 22.951 4.447   7.421   0.64 12.28 ?  53  LEU   A CB   1 
ATOM   1306 C  CB   B LEU   A 1 53  ? 22.918 4.406   7.372   0.36 11.03 ?  53  LEU   A CB   1 
ATOM   1307 C  CG   A LEU   A 1 53  ? 22.087 3.180   7.444   0.64 13.20 ?  53  LEU   A CG   1 
ATOM   1308 C  CG   B LEU   A 1 53  ? 22.106 3.119   7.556   0.36 10.91 ?  53  LEU   A CG   1 
ATOM   1309 C  CD1  A LEU   A 1 53  ? 22.887 1.990   6.938   0.64 13.73 ?  53  LEU   A CD1  1 
ATOM   1310 C  CD1  B LEU   A 1 53  ? 22.749 1.976   6.791   0.36 11.48 ?  53  LEU   A CD1  1 
ATOM   1311 C  CD2  A LEU   A 1 53  ? 21.538 2.908   8.839   0.64 13.73 ?  53  LEU   A CD2  1 
ATOM   1312 C  CD2  B LEU   A 1 53  ? 21.975 2.756   9.024   0.36 10.68 ?  53  LEU   A CD2  1 
ATOM   1313 H  H    A LEU   A 1 53  ? 21.239 5.627   6.108   0.64 13.46 ?  53  LEU   A H    1 
ATOM   1314 H  H    B LEU   A 1 53  ? 21.273 5.662   6.071   0.36 13.21 ?  53  LEU   A H    1 
ATOM   1315 H  HA   A LEU   A 1 53  ? 21.809 5.630   8.644   0.64 14.00 ?  53  LEU   A HA   1 
ATOM   1316 H  HA   B LEU   A 1 53  ? 21.815 5.600   8.622   0.36 13.25 ?  53  LEU   A HA   1 
ATOM   1317 H  HB2  A LEU   A 1 53  ? 23.301 4.535   6.517   0.64 14.72 ?  53  LEU   A HB2  1 
ATOM   1318 H  HB2  B LEU   A 1 53  ? 23.147 4.463   6.429   0.36 13.22 ?  53  LEU   A HB2  1 
ATOM   1319 H  HB3  A LEU   A 1 53  ? 23.689 4.298   8.032   0.64 14.72 ?  53  LEU   A HB3  1 
ATOM   1320 H  HB3  B LEU   A 1 53  ? 23.732 4.299   7.887   0.36 13.22 ?  53  LEU   A HB3  1 
ATOM   1321 H  HG   A LEU   A 1 53  ? 21.332 3.304   6.846   0.64 15.82 ?  53  LEU   A HG   1 
ATOM   1322 H  HG   B LEU   A 1 53  ? 21.216 3.254   7.193   0.36 13.08 ?  53  LEU   A HG   1 
ATOM   1323 H  HD11 A LEU   A 1 53  ? 22.321 1.200   6.959   0.64 16.45 ?  53  LEU   A HD11 1 
ATOM   1324 H  HD11 B LEU   A 1 53  ? 22.222 1.173   6.927   0.36 13.75 ?  53  LEU   A HD11 1 
ATOM   1325 H  HD12 A LEU   A 1 53  ? 23.172 2.167   6.028   0.64 16.45 ?  53  LEU   A HD12 1 
ATOM   1326 H  HD12 B LEU   A 1 53  ? 22.773 2.201   5.848   0.36 13.75 ?  53  LEU   A HD12 1 
ATOM   1327 H  HD13 A LEU   A 1 53  ? 23.656 1.862   7.510   0.64 16.45 ?  53  LEU   A HD13 1 
ATOM   1328 H  HD13 B LEU   A 1 53  ? 23.649 1.843   7.124   0.36 13.75 ?  53  LEU   A HD13 1 
ATOM   1329 H  HD21 A LEU   A 1 53  ? 21.096 2.046   8.845   0.64 16.46 ?  53  LEU   A HD21 1 
ATOM   1330 H  HD21 B LEU   A 1 53  ? 21.412 1.970   9.103   0.36 12.80 ?  53  LEU   A HD21 1 
ATOM   1331 H  HD22 A LEU   A 1 53  ? 22.274 2.909   9.472   0.64 16.46 ?  53  LEU   A HD22 1 
ATOM   1332 H  HD22 B LEU   A 1 53  ? 22.856 2.572   9.382   0.36 12.80 ?  53  LEU   A HD22 1 
ATOM   1333 H  HD23 A LEU   A 1 53  ? 20.905 3.606   9.071   0.64 16.46 ?  53  LEU   A HD23 1 
ATOM   1334 H  HD23 B LEU   A 1 53  ? 21.572 3.501   9.497   0.36 12.80 ?  53  LEU   A HD23 1 
ATOM   1335 N  N    . ASN   A 1 54  ? 23.844 7.379   6.897   1.00 10.62 ?  54  ASN   A N    1 
ATOM   1336 C  CA   . ASN   A 1 54  ? 24.890 8.376   7.026   1.00 10.79 ?  54  ASN   A CA   1 
ATOM   1337 C  C    . ASN   A 1 54  ? 24.378 9.624   7.741   1.00 11.44 ?  54  ASN   A C    1 
ATOM   1338 O  O    . ASN   A 1 54  ? 25.070 10.182  8.604   1.00 12.00 ?  54  ASN   A O    1 
ATOM   1339 C  CB   . ASN   A 1 54  ? 25.453 8.733   5.664   1.00 11.04 ?  54  ASN   A CB   1 
ATOM   1340 C  CG   . ASN   A 1 54  ? 26.467 9.837   5.770   1.00 11.16 ?  54  ASN   A CG   1 
ATOM   1341 O  OD1  . ASN   A 1 54  ? 27.478 9.691   6.470   1.00 11.29 ?  54  ASN   A OD1  1 
ATOM   1342 N  ND2  . ASN   A 1 54  ? 26.211 10.955  5.109   1.00 11.93 ?  54  ASN   A ND2  1 
ATOM   1343 H  H    A ASN   A 1 54  ? 23.625 7.171   6.091   0.64 12.72 ?  54  ASN   A H    1 
ATOM   1344 H  H    B ASN   A 1 54  ? 23.585 7.220   6.092   0.36 12.72 ?  54  ASN   A H    1 
ATOM   1345 H  HA   . ASN   A 1 54  ? 25.606 8.008   7.556   1.00 12.93 ?  54  ASN   A HA   1 
ATOM   1346 H  HB2  . ASN   A 1 54  ? 25.887 7.948   5.284   1.00 13.23 ?  54  ASN   A HB2  1 
ATOM   1347 H  HB3  . ASN   A 1 54  ? 24.735 9.029   5.082   1.00 13.23 ?  54  ASN   A HB3  1 
ATOM   1348 H  HD21 . ASN   A 1 54  ? 26.766 11.610  5.143   1.00 14.29 ?  54  ASN   A HD21 1 
ATOM   1349 H  HD22 . ASN   A 1 54  ? 25.494 11.023  4.639   1.00 14.29 ?  54  ASN   A HD22 1 
ATOM   1350 N  N    . LYS   A 1 55  ? 23.166 10.073  7.400   1.00 11.74 ?  55  LYS   A N    1 
ATOM   1351 C  CA   . LYS   A 1 55  ? 22.583 11.228  8.069   1.00 12.41 ?  55  LYS   A CA   1 
ATOM   1352 C  C    . LYS   A 1 55  ? 22.493 10.998  9.571   1.00 12.37 ?  55  LYS   A C    1 
ATOM   1353 O  O    . LYS   A 1 55  ? 22.773 11.904  10.367  1.00 13.05 ?  55  LYS   A O    1 
ATOM   1354 C  CB   . LYS   A 1 55  ? 21.210 11.516  7.463   1.00 13.21 ?  55  LYS   A CB   1 
ATOM   1355 C  CG   . LYS   A 1 55  ? 20.469 12.681  8.079   1.00 14.93 ?  55  LYS   A CG   1 
ATOM   1356 C  CD   . LYS   A 1 55  ? 19.137 12.907  7.364   1.00 16.38 ?  55  LYS   A CD   1 
ATOM   1357 C  CE   . LYS   A 1 55  ? 18.315 14.007  8.014   1.00 18.10 ?  55  LYS   A CE   1 
ATOM   1358 N  NZ   . LYS   A 1 55  ? 16.973 14.146  7.375   1.00 18.75 ?  55  LYS   A NZ   1 
ATOM   1359 H  H    . LYS   A 1 55  ? 22.660 9.722   6.795   1.00 14.07 ?  55  LYS   A H    1 
ATOM   1360 H  HA   . LYS   A 1 55  ? 23.143 12.002  7.917   1.00 14.87 ?  55  LYS   A HA   1 
ATOM   1361 H  HB2  . LYS   A 1 55  ? 21.318 11.713  6.520   1.00 15.83 ?  55  LYS   A HB2  1 
ATOM   1362 H  HB3  . LYS   A 1 55  ? 20.648 10.731  7.567   1.00 15.83 ?  55  LYS   A HB3  1 
ATOM   1363 H  HG2  . LYS   A 1 55  ? 20.278 12.492  9.012   1.00 17.90 ?  55  LYS   A HG2  1 
ATOM   1364 H  HG3  . LYS   A 1 55  ? 20.997 13.486  7.995   1.00 17.90 ?  55  LYS   A HG3  1 
ATOM   1365 H  HD2  . LYS   A 1 55  ? 19.312 13.158  6.442   1.00 19.64 ?  55  LYS   A HD2  1 
ATOM   1366 H  HD3  . LYS   A 1 55  ? 18.620 12.084  7.390   1.00 19.64 ?  55  LYS   A HD3  1 
ATOM   1367 H  HE2  . LYS   A 1 55  ? 18.187 13.796  8.950   1.00 21.70 ?  55  LYS   A HE2  1 
ATOM   1368 H  HE3  . LYS   A 1 55  ? 18.786 14.850  7.920   1.00 21.70 ?  55  LYS   A HE3  1 
ATOM   1369 H  HZ1  . LYS   A 1 55  ? 16.432 14.618  7.903   1.00 22.48 ?  55  LYS   A HZ1  1 
ATOM   1370 H  HZ2  . LYS   A 1 55  ? 17.047 14.567  6.593   1.00 22.48 ?  55  LYS   A HZ2  1 
ATOM   1371 H  HZ3  . LYS   A 1 55  ? 16.612 13.344  7.238   1.00 22.48 ?  55  LYS   A HZ3  1 
ATOM   1372 N  N    . ALA   A 1 56  ? 22.108 9.786   9.978   1.00 12.91 ?  56  ALA   A N    1 
ATOM   1373 C  CA   . ALA   A 1 56  ? 21.983 9.469   11.395  1.00 13.59 ?  56  ALA   A CA   1 
ATOM   1374 C  C    . ALA   A 1 56  ? 23.322 9.498   12.121  1.00 13.26 ?  56  ALA   A C    1 
ATOM   1375 O  O    . ALA   A 1 56  ? 23.341 9.684   13.341  1.00 14.70 ?  56  ALA   A O    1 
ATOM   1376 C  CB   . ALA   A 1 56  ? 21.288 8.116   11.579  1.00 14.23 ?  56  ALA   A CB   1 
ATOM   1377 H  H    . ALA   A 1 56  ? 21.909 9.137   9.451   1.00 15.47 ?  56  ALA   A H    1 
ATOM   1378 H  HA   . ALA   A 1 56  ? 21.425 10.133  11.814  1.00 16.29 ?  56  ALA   A HA   1 
ATOM   1379 H  HB1  . ALA   A 1 56  ? 21.216 7.920   12.529  1.00 17.06 ?  56  ALA   A HB1  1 
ATOM   1380 H  HB2  . ALA   A 1 56  ? 20.400 8.163   11.188  1.00 17.06 ?  56  ALA   A HB2  1 
ATOM   1381 H  HB3  . ALA   A 1 56  ? 21.805 7.424   11.139  1.00 17.06 ?  56  ALA   A HB3  1 
ATOM   1382 N  N    . THR   A 1 57  ? 24.434 9.308   11.408  1.00 12.55 ?  57  THR   A N    1 
ATOM   1383 C  CA   . THR   A 1 57  ? 25.775 9.438   11.983  1.00 12.41 ?  57  THR   A CA   1 
ATOM   1384 C  C    . THR   A 1 57  ? 26.330 10.857  11.900  1.00 12.78 ?  57  THR   A C    1 
ATOM   1385 O  O    . THR   A 1 57  ? 27.517 11.065  12.182  1.00 13.28 ?  57  THR   A O    1 
ATOM   1386 C  CB   . THR   A 1 57  ? 26.790 8.491   11.311  1.00 12.27 ?  57  THR   A CB   1 
ATOM   1387 O  OG1  . THR   A 1 57  ? 27.173 8.988   10.016  1.00 12.10 ?  57  THR   A OG1  1 
ATOM   1388 C  CG2  . THR   A 1 57  ? 26.267 7.069   11.208  1.00 12.30 ?  57  THR   A CG2  1 
ATOM   1389 H  H    . THR   A 1 57  ? 24.441 9.076   10.580  1.00 15.05 ?  57  THR   A H    1 
ATOM   1390 H  HA   . THR   A 1 57  ? 25.733 9.182   12.925  1.00 14.87 ?  57  THR   A HA   1 
ATOM   1391 H  HB   . THR   A 1 57  ? 27.587 8.454   11.868  1.00 14.71 ?  57  THR   A HB   1 
ATOM   1392 H  HG1  . THR   A 1 57  ? 26.494 9.057   9.526   1.00 14.51 ?  57  THR   A HG1  1 
ATOM   1393 H  HG21 . THR   A 1 57  ? 26.913 6.504   10.751  1.00 14.75 ?  57  THR   A HG21 1 
ATOM   1394 H  HG22 . THR   A 1 57  ? 26.106 6.704   12.093  1.00 14.75 ?  57  THR   A HG22 1 
ATOM   1395 H  HG23 . THR   A 1 57  ? 25.435 7.051   10.710  1.00 14.75 ?  57  THR   A HG23 1 
ATOM   1396 N  N    . ASN   A 1 58  ? 25.517 11.831  11.496  1.00 13.19 ?  58  ASN   A N    1 
ATOM   1397 C  CA   . ASN   A 1 58  ? 25.983 13.210  11.395  1.00 13.88 ?  58  ASN   A CA   1 
ATOM   1398 C  C    . ASN   A 1 58  ? 27.129 13.334  10.384  1.00 12.75 ?  58  ASN   A C    1 
ATOM   1399 O  O    . ASN   A 1 58  ? 28.022 14.171  10.537  1.00 13.45 ?  58  ASN   A O    1 
ATOM   1400 C  CB   . ASN   A 1 58  ? 26.365 13.748  12.788  1.00 16.57 ?  58  ASN   A CB   1 
ATOM   1401 C  CG   . ASN   A 1 58  ? 26.777 15.210  12.781  1.00 20.09 ?  58  ASN   A CG   1 
ATOM   1402 O  OD1  . ASN   A 1 58  ? 26.147 16.036  12.130  1.00 21.77 ?  58  ASN   A OD1  1 
ATOM   1403 N  ND2  . ASN   A 1 58  ? 27.836 15.538  13.528  1.00 21.31 ?  58  ASN   A ND2  1 
ATOM   1404 H  H    . ASN   A 1 58  ? 24.693 11.712  11.271  1.00 15.82 ?  58  ASN   A H    1 
ATOM   1405 H  HA   . ASN   A 1 58  ? 25.249 13.748  11.069  1.00 16.64 ?  58  ASN   A HA   1 
ATOM   1406 H  HB2  . ASN   A 1 58  ? 25.596 13.659  13.383  1.00 19.87 ?  58  ASN   A HB2  1 
ATOM   1407 H  HB3  . ASN   A 1 58  ? 27.107 13.240  13.140  1.00 19.87 ?  58  ASN   A HB3  1 
ATOM   1408 H  HD21 . ASN   A 1 58  ? 28.101 16.359  13.561  1.00 25.55 ?  58  ASN   A HD21 1 
ATOM   1409 H  HD22 . ASN   A 1 58  ? 28.245 14.935  13.975  1.00 25.55 ?  58  ASN   A HD22 1 
ATOM   1410 N  N    . ASN   A 1 59  ? 27.111 12.510  9.333   1.00 11.95 ?  59  ASN   A N    1 
ATOM   1411 C  CA   . ASN   A 1 59  ? 28.087 12.491  8.237   1.00 11.65 ?  59  ASN   A CA   1 
ATOM   1412 C  C    . ASN   A 1 59  ? 29.404 11.809  8.628   1.00 11.22 ?  59  ASN   A C    1 
ATOM   1413 O  O    . ASN   A 1 59  ? 30.326 11.768  7.806   1.00 11.67 ?  59  ASN   A O    1 
ATOM   1414 C  CB   . ASN   A 1 59  ? 28.377 13.877  7.632   1.00 12.02 ?  59  ASN   A CB   1 
ATOM   1415 C  CG   . ASN   A 1 59  ? 28.730 13.806  6.161   1.00 12.29 ?  59  ASN   A CG   1 
ATOM   1416 O  OD1  . ASN   A 1 59  ? 28.021 13.175  5.367   1.00 12.48 ?  59  ASN   A OD1  1 
ATOM   1417 N  ND2  . ASN   A 1 59  ? 29.826 14.465  5.780   1.00 12.76 ?  59  ASN   A ND2  1 
ATOM   1418 H  H    . ASN   A 1 59  ? 26.505 11.908  9.230   1.00 14.32 ?  59  ASN   A H    1 
ATOM   1419 H  HA   . ASN   A 1 59  ? 27.708 11.960  7.526   1.00 13.96 ?  59  ASN   A HA   1 
ATOM   1420 H  HB2  . ASN   A 1 59  ? 27.592 14.439  7.721   1.00 14.41 ?  59  ASN   A HB2  1 
ATOM   1421 H  HB3  . ASN   A 1 59  ? 29.128 14.282  8.096   1.00 14.41 ?  59  ASN   A HB3  1 
ATOM   1422 H  HD21 . ASN   A 1 59  ? 30.075 14.462  4.954   1.00 15.30 ?  59  ASN   A HD21 1 
ATOM   1423 H  HD22 . ASN   A 1 59  ? 30.302 14.895  6.361   1.00 15.30 ?  59  ASN   A HD22 1 
ATOM   1424 N  N    . ALA   A 1 60  ? 29.526 11.263  9.837   1.00 11.52 ?  60  ALA   A N    1 
ATOM   1425 C  CA   . ALA   A 1 60  ? 30.764 10.583  10.199  1.00 11.76 ?  60  ALA   A CA   1 
ATOM   1426 C  C    . ALA   A 1 60  ? 30.993 9.345   9.340   1.00 11.86 ?  60  ALA   A C    1 
ATOM   1427 O  O    . ALA   A 1 60  ? 32.139 9.022   9.008   1.00 12.29 ?  60  ALA   A O    1 
ATOM   1428 C  CB   . ALA   A 1 60  ? 30.760 10.229  11.681  1.00 12.57 ?  60  ALA   A CB   1 
ATOM   1429 H  H    . ALA   A 1 60  ? 28.922 11.267  10.444  1.00 13.81 ?  60  ALA   A H    1 
ATOM   1430 H  HA   . ALA   A 1 60  ? 31.507 11.188  10.039  1.00 14.09 ?  60  ALA   A HA   1 
ATOM   1431 H  HB1  . ALA   A 1 60  ? 31.590 9.782   11.899  1.00 15.07 ?  60  ALA   A HB1  1 
ATOM   1432 H  HB2  . ALA   A 1 60  ? 30.679 11.049  12.196  1.00 15.07 ?  60  ALA   A HB2  1 
ATOM   1433 H  HB3  . ALA   A 1 60  ? 30.008 9.648   11.862  1.00 15.07 ?  60  ALA   A HB3  1 
ATOM   1434 N  N    . MET   A 1 61  ? 29.920 8.649   8.958   1.00 11.35 ?  61  MET   A N    1 
ATOM   1435 C  CA   . MET   A 1 61  ? 30.058 7.510   8.055   1.00 10.95 ?  61  MET   A CA   1 
ATOM   1436 C  C    . MET   A 1 61  ? 30.689 7.933   6.731   1.00 11.09 ?  61  MET   A C    1 
ATOM   1437 O  O    . MET   A 1 61  ? 31.585 7.251   6.215   1.00 11.37 ?  61  MET   A O    1 
ATOM   1438 C  CB   . MET   A 1 61  ? 28.695 6.856   7.830   1.00 11.22 ?  61  MET   A CB   1 
ATOM   1439 C  CG   . MET   A 1 61  ? 28.708 5.684   6.860   1.00 11.88 ?  61  MET   A CG   1 
ATOM   1440 S  SD   . MET   A 1 61  ? 27.088 4.935   6.660   1.00 12.62 ?  61  MET   A SD   1 
ATOM   1441 C  CE   . MET   A 1 61  ? 26.959 4.048   8.221   1.00 14.49 ?  61  MET   A CE   1 
ATOM   1442 H  H    . MET   A 1 61  ? 29.111 8.814   9.198   1.00 13.61 ?  61  MET   A H    1 
ATOM   1443 H  HA   . MET   A 1 61  ? 30.631 6.850   8.472   1.00 13.13 ?  61  MET   A HA   1 
ATOM   1444 H  HB2  . MET   A 1 61  ? 28.363 6.531   8.678   1.00 13.45 ?  61  MET   A HB2  1 
ATOM   1445 H  HB3  . MET   A 1 61  ? 28.085 7.521   7.472   1.00 13.45 ?  61  MET   A HB3  1 
ATOM   1446 H  HG2  . MET   A 1 61  ? 28.995 5.986   5.984   1.00 14.24 ?  61  MET   A HG2  1 
ATOM   1447 H  HG3  . MET   A 1 61  ? 29.312 4.999   7.190   1.00 14.24 ?  61  MET   A HG3  1 
ATOM   1448 H  HE1  . MET   A 1 61  ? 26.121 3.562   8.240   1.00 17.38 ?  61  MET   A HE1  1 
ATOM   1449 H  HE2  . MET   A 1 61  ? 27.703 3.432   8.296   1.00 17.38 ?  61  MET   A HE2  1 
ATOM   1450 H  HE3  . MET   A 1 61  ? 26.986 4.688   8.953   1.00 17.38 ?  61  MET   A HE3  1 
ATOM   1451 N  N    . GLN   A 1 62  ? 30.246 9.062   6.171   1.00 11.02 ?  62  GLN   A N    1 
ATOM   1452 C  CA   . GLN   A 1 62  ? 30.811 9.531   4.910   1.00 11.35 ?  62  GLN   A CA   1 
ATOM   1453 C  C    . GLN   A 1 62  ? 32.280 9.909   5.057   1.00 11.06 ?  62  GLN   A C    1 
ATOM   1454 O  O    . GLN   A 1 62  ? 33.091 9.596   4.180   1.00 11.51 ?  62  GLN   A O    1 
ATOM   1455 C  CB   . GLN   A 1 62  ? 30.008 10.717  4.379   1.00 11.29 ?  62  GLN   A CB   1 
ATOM   1456 C  CG   . GLN   A 1 62  ? 30.390 11.082  2.953   1.00 11.21 ?  62  GLN   A CG   1 
ATOM   1457 C  CD   . GLN   A 1 62  ? 30.067 9.957   1.999   1.00 11.43 ?  62  GLN   A CD   1 
ATOM   1458 O  OE1  . GLN   A 1 62  ? 28.890 9.653   1.783   1.00 11.96 ?  62  GLN   A OE1  1 
ATOM   1459 N  NE2  . GLN   A 1 62  ? 31.092 9.287   1.473   1.00 12.17 ?  62  GLN   A NE2  1 
ATOM   1460 H  H    . GLN   A 1 62  ? 29.625 9.555   6.496   1.00 13.21 ?  62  GLN   A H    1 
ATOM   1461 H  HA   . GLN   A 1 62  ? 30.757 8.814   4.260   1.00 13.60 ?  62  GLN   A HA   1 
ATOM   1462 H  HB2  . GLN   A 1 62  ? 29.066 10.498  4.395   1.00 13.53 ?  62  GLN   A HB2  1 
ATOM   1463 H  HB3  . GLN   A 1 62  ? 30.180 11.493  4.941   1.00 13.53 ?  62  GLN   A HB3  1 
ATOM   1464 H  HG2  . GLN   A 1 62  ? 29.885 11.861  2.676   1.00 13.44 ?  62  GLN   A HG2  1 
ATOM   1465 H  HG3  . GLN   A 1 62  ? 31.340 11.258  2.904   1.00 13.44 ?  62  GLN   A HG3  1 
ATOM   1466 H  HE21 . GLN   A 1 62  ? 31.898 9.522   1.660   1.00 14.59 ?  62  GLN   A HE21 1 
ATOM   1467 H  HE22 . GLN   A 1 62  ? 30.948 8.635   0.932   1.00 14.59 ?  62  GLN   A HE22 1 
ATOM   1468 N  N    . VAL   A 1 63  ? 32.640 10.584  6.152   1.00 11.63 ?  63  VAL   A N    1 
ATOM   1469 C  CA   . VAL   A 1 63  ? 34.030 10.983  6.365   1.00 12.53 ?  63  VAL   A CA   1 
ATOM   1470 C  C    . VAL   A 1 63  ? 34.929 9.751   6.431   1.00 11.97 ?  63  VAL   A C    1 
ATOM   1471 O  O    . VAL   A 1 63  ? 35.978 9.681   5.775   1.00 12.49 ?  63  VAL   A O    1 
ATOM   1472 C  CB   . VAL   A 1 63  ? 34.143 11.857  7.628   1.00 13.86 ?  63  VAL   A CB   1 
ATOM   1473 C  CG1  . VAL   A 1 63  ? 35.591 12.091  7.993   1.00 15.46 ?  63  VAL   A CG1  1 
ATOM   1474 C  CG2  . VAL   A 1 63  ? 33.428 13.192  7.416   1.00 14.27 ?  63  VAL   A CG2  1 
ATOM   1475 H  H    . VAL   A 1 63  ? 32.098 10.827  6.779   1.00 13.94 ?  63  VAL   A H    1 
ATOM   1476 H  HA   . VAL   A 1 63  ? 34.316 11.521  5.613   1.00 15.03 ?  63  VAL   A HA   1 
ATOM   1477 H  HB   . VAL   A 1 63  ? 33.715 11.402  8.373   1.00 16.62 ?  63  VAL   A HB   1 
ATOM   1478 H  HG11 . VAL   A 1 63  ? 35.642 12.829  8.618   1.00 18.54 ?  63  VAL   A HG11 1 
ATOM   1479 H  HG12 . VAL   A 1 63  ? 35.948 11.287  8.401   1.00 18.54 ?  63  VAL   A HG12 1 
ATOM   1480 H  HG13 . VAL   A 1 63  ? 36.085 12.304  7.186   1.00 18.54 ?  63  VAL   A HG13 1 
ATOM   1481 H  HG21 . VAL   A 1 63  ? 33.516 13.730  8.222   1.00 17.11 ?  63  VAL   A HG21 1 
ATOM   1482 H  HG22 . VAL   A 1 63  ? 33.838 13.653  6.668   1.00 17.11 ?  63  VAL   A HG22 1 
ATOM   1483 H  HG23 . VAL   A 1 63  ? 32.492 13.026  7.232   1.00 17.11 ?  63  VAL   A HG23 1 
ATOM   1484 N  N    . GLU   A 1 64  ? 34.510 8.746   7.205   1.00 11.94 ?  64  GLU   A N    1 
ATOM   1485 C  CA   . GLU   A 1 64  ? 35.270 7.508   7.304   1.00 11.89 ?  64  GLU   A CA   1 
ATOM   1486 C  C    . GLU   A 1 64  ? 35.364 6.818   5.949   1.00 11.47 ?  64  GLU   A C    1 
ATOM   1487 O  O    . GLU   A 1 64  ? 36.416 6.273   5.576   1.00 12.06 ?  64  GLU   A O    1 
ATOM   1488 C  CB   . GLU   A 1 64  ? 34.589 6.601   8.329   1.00 12.54 ?  64  GLU   A CB   1 
ATOM   1489 C  CG   . GLU   A 1 64  ? 35.237 5.245   8.467   1.00 13.30 ?  64  GLU   A CG   1 
ATOM   1490 C  CD   . GLU   A 1 64  ? 34.359 4.250   9.192   1.00 14.10 ?  64  GLU   A CD   1 
ATOM   1491 O  OE1  . GLU   A 1 64  ? 33.121 4.346   9.054   1.00 14.82 ?  64  GLU   A OE1  1 
ATOM   1492 O  OE2  . GLU   A 1 64  ? 34.910 3.363   9.886   1.00 14.28 -1 64  GLU   A OE2  1 
ATOM   1493 H  H    . GLU   A 1 64  ? 33.784 8.757   7.671   1.00 14.31 ?  64  GLU   A H    1 
ATOM   1494 H  HA   . GLU   A 1 64  ? 36.168 7.711   7.619   1.00 14.25 ?  64  GLU   A HA   1 
ATOM   1495 H  HB2  . GLU   A 1 64  ? 34.619 7.037   9.201   1.00 15.03 ?  64  GLU   A HB2  1 
ATOM   1496 H  HB3  . GLU   A 1 64  ? 33.665 6.476   8.063   1.00 15.03 ?  64  GLU   A HB3  1 
ATOM   1497 H  HG2  . GLU   A 1 64  ? 35.423 4.880   7.585   1.00 15.95 ?  64  GLU   A HG2  1 
ATOM   1498 H  HG3  . GLU   A 1 64  ? 36.061 5.339   8.964   1.00 15.95 ?  64  GLU   A HG3  1 
ATOM   1499 N  N    . SER   A 1 65  ? 34.250 6.811   5.212   1.00 11.09 ?  65  SER   A N    1 
ATOM   1500 C  CA   . SER   A 1 65  ? 34.196 6.151   3.912   1.00 11.17 ?  65  SER   A CA   1 
ATOM   1501 C  C    . SER   A 1 65  ? 35.118 6.819   2.900   1.00 11.28 ?  65  SER   A C    1 
ATOM   1502 O  O    . SER   A 1 65  ? 35.758 6.140   2.089   1.00 12.25 ?  65  SER   A O    1 
ATOM   1503 C  CB   . SER   A 1 65  ? 32.764 6.159   3.382   1.00 11.37 ?  65  SER   A CB   1 
ATOM   1504 O  OG   . SER   A 1 65  ? 31.909 5.352   4.181   1.00 11.80 ?  65  SER   A OG   1 
ATOM   1505 H  H    . SER   A 1 65  ? 33.513 7.187   5.446   1.00 13.30 ?  65  SER   A H    1 
ATOM   1506 H  HA   . SER   A 1 65  ? 34.481 5.230   4.013   1.00 13.39 ?  65  SER   A HA   1 
ATOM   1507 H  HB2  . SER   A 1 65  ? 32.430 7.065   3.387   1.00 13.63 ?  65  SER   A HB2  1 
ATOM   1508 H  HB3  . SER   A 1 65  ? 32.766 5.808   2.478   1.00 13.63 ?  65  SER   A HB3  1 
ATOM   1509 H  HG   . SER   A 1 65  ? 31.906 5.640   4.975   1.00 14.15 ?  65  SER   A HG   1 
ATOM   1510 N  N    . ASP   A 1 66  ? 35.197 8.152   2.921   1.00 11.67 ?  66  ASP   A N    1 
ATOM   1511 C  CA   . ASP   A 1 66  ? 36.057 8.847   1.969   1.00 12.64 ?  66  ASP   A CA   1 
ATOM   1512 C  C    . ASP   A 1 66  ? 37.521 8.495   2.208   1.00 12.25 ?  66  ASP   A C    1 
ATOM   1513 O  O    . ASP   A 1 66  ? 38.293 8.326   1.257   1.00 13.36 ?  66  ASP   A O    1 
ATOM   1514 C  CB   . ASP   A 1 66  ? 35.834 10.355  2.066   1.00 13.83 ?  66  ASP   A CB   1 
ATOM   1515 C  CG   . ASP   A 1 66  ? 34.500 10.812  1.456   1.00 15.64 ?  66  ASP   A CG   1 
ATOM   1516 O  OD1  . ASP   A 1 66  ? 33.790 10.015  0.804   1.00 15.95 ?  66  ASP   A OD1  1 
ATOM   1517 O  OD2  . ASP   A 1 66  ? 34.194 12.010  1.609   1.00 18.47 -1 66  ASP   A OD2  1 
ATOM   1518 H  H    . ASP   A 1 66  ? 34.761 8.667   3.464   1.00 13.99 ?  66  ASP   A H    1 
ATOM   1519 H  HA   . ASP   A 1 66  ? 35.818 8.567   1.074   1.00 15.15 ?  66  ASP   A HA   1 
ATOM   1520 H  HB2  . ASP   A 1 66  ? 35.829 10.616  2.998   1.00 16.58 ?  66  ASP   A HB2  1 
ATOM   1521 H  HB3  . ASP   A 1 66  ? 36.551 10.808  1.596   1.00 16.58 ?  66  ASP   A HB3  1 
ATOM   1522 N  N    . ASP   A 1 67  ? 37.918 8.364   3.473   1.00 12.36 ?  67  ASP   A N    1 
ATOM   1523 C  CA   . ASP   A 1 67  ? 39.271 7.915   3.777   1.00 13.33 ?  67  ASP   A CA   1 
ATOM   1524 C  C    . ASP   A 1 67  ? 39.491 6.479   3.316   1.00 13.62 ?  67  ASP   A C    1 
ATOM   1525 O  O    . ASP   A 1 67  ? 40.552 6.153   2.772   1.00 14.27 ?  67  ASP   A O    1 
ATOM   1526 C  CB   . ASP   A 1 67  ? 39.533 8.054   5.275   1.00 14.41 ?  67  ASP   A CB   1 
ATOM   1527 C  CG   . ASP   A 1 67  ? 40.826 7.398   5.704   1.00 15.80 ?  67  ASP   A CG   1 
ATOM   1528 O  OD1  . ASP   A 1 67  ? 41.898 8.033   5.573   1.00 18.39 ?  67  ASP   A OD1  1 
ATOM   1529 O  OD2  . ASP   A 1 67  ? 40.774 6.237   6.171   1.00 15.87 -1 67  ASP   A OD2  1 
ATOM   1530 H  H    . ASP   A 1 67  ? 37.436 8.533   4.161   1.00 14.81 ?  67  ASP   A H    1 
ATOM   1531 H  HA   . ASP   A 1 67  ? 39.907 8.478   3.307   1.00 15.98 ?  67  ASP   A HA   1 
ATOM   1532 H  HB2  . ASP   A 1 67  ? 39.588 8.991   5.497   1.00 17.28 ?  67  ASP   A HB2  1 
ATOM   1533 H  HB3  . ASP   A 1 67  ? 38.809 7.630   5.761   1.00 17.28 ?  67  ASP   A HB3  1 
ATOM   1534 N  N    . TYR   A 1 68  ? 38.496 5.605   3.510   1.00 12.94 ?  68  TYR   A N    1 
ATOM   1535 C  CA   . TYR   A 1 68  ? 38.616 4.228   3.037   1.00 13.05 ?  68  TYR   A CA   1 
ATOM   1536 C  C    . TYR   A 1 68  ? 38.860 4.179   1.530   1.00 12.91 ?  68  TYR   A C    1 
ATOM   1537 O  O    . TYR   A 1 68  ? 39.738 3.446   1.058   1.00 13.17 ?  68  TYR   A O    1 
ATOM   1538 C  CB   . TYR   A 1 68  ? 37.366 3.406   3.411   1.00 13.47 ?  68  TYR   A CB   1 
ATOM   1539 C  CG   . TYR   A 1 68  ? 37.394 2.019   2.783   1.00 14.78 ?  68  TYR   A CG   1 
ATOM   1540 C  CD1  . TYR   A 1 68  ? 36.933 1.824   1.488   1.00 15.75 ?  68  TYR   A CD1  1 
ATOM   1541 C  CD2  . TYR   A 1 68  ? 37.929 0.931   3.456   1.00 16.18 ?  68  TYR   A CD2  1 
ATOM   1542 C  CE1  . TYR   A 1 68  ? 37.003 0.612   0.873   1.00 17.01 ?  68  TYR   A CE1  1 
ATOM   1543 C  CE2  . TYR   A 1 68  ? 37.992 -0.326  2.843   1.00 16.96 ?  68  TYR   A CE2  1 
ATOM   1544 C  CZ   . TYR   A 1 68  ? 37.532 -0.462  1.551   1.00 17.30 ?  68  TYR   A CZ   1 
ATOM   1545 O  OH   . TYR   A 1 68  ? 37.610 -1.679  0.925   1.00 18.26 ?  68  TYR   A OH   1 
ATOM   1546 H  H    . TYR   A 1 68  ? 37.751 5.783   3.906   1.00 15.51 ?  68  TYR   A H    1 
ATOM   1547 H  HA   . TYR   A 1 68  ? 39.377 3.815   3.470   1.00 15.65 ?  68  TYR   A HA   1 
ATOM   1548 H  HB2  . TYR   A 1 68  ? 37.330 3.301   4.374   1.00 16.14 ?  68  TYR   A HB2  1 
ATOM   1549 H  HB3  . TYR   A 1 68  ? 36.573 3.866   3.093   1.00 16.14 ?  68  TYR   A HB3  1 
ATOM   1550 H  HD1  . TYR   A 1 68  ? 36.590 2.553   1.020   1.00 18.89 ?  68  TYR   A HD1  1 
ATOM   1551 H  HD2  . TYR   A 1 68  ? 38.260 1.041   4.317   1.00 19.40 ?  68  TYR   A HD2  1 
ATOM   1552 H  HE1  . TYR   A 1 68  ? 36.682 0.509   0.008   1.00 20.40 ?  68  TYR   A HE1  1 
ATOM   1553 H  HE2  . TYR   A 1 68  ? 38.357 -1.052  3.289   1.00 20.34 ?  68  TYR   A HE2  1 
ATOM   1554 H  HH   . TYR   A 1 68  ? 37.941 -2.248  1.451   1.00 21.90 ?  68  TYR   A HH   1 
ATOM   1555 N  N    . ILE   A 1 69  ? 38.076 4.936   0.754   1.00 12.37 ?  69  ILE   A N    1 
ATOM   1556 C  CA   . ILE   A 1 69  ? 38.216 4.925   -0.700  1.00 12.52 ?  69  ILE   A CA   1 
ATOM   1557 C  C    . ILE   A 1 69  ? 39.554 5.525   -1.125  1.00 12.64 ?  69  ILE   A C    1 
ATOM   1558 O  O    . ILE   A 1 69  ? 40.199 5.039   -2.063  1.00 13.20 ?  69  ILE   A O    1 
ATOM   1559 C  CB   . ILE   A 1 69  ? 37.023 5.639   -1.366  1.00 13.29 ?  69  ILE   A CB   1 
ATOM   1560 C  CG1  . ILE   A 1 69  ? 35.708 4.909   -1.082  1.00 13.95 ?  69  ILE   A CG1  1 
ATOM   1561 C  CG2  . ILE   A 1 69  ? 37.256 5.813   -2.873  1.00 14.68 ?  69  ILE   A CG2  1 
ATOM   1562 C  CD1  . ILE   A 1 69  ? 35.542 3.620   -1.861  1.00 14.38 ?  69  ILE   A CD1  1 
ATOM   1563 H  H    . ILE   A 1 69  ? 37.474 5.473   1.047   1.00 14.83 ?  69  ILE   A H    1 
ATOM   1564 H  HA   . ILE   A 1 69  ? 38.209 4.005   -0.999  1.00 15.01 ?  69  ILE   A HA   1 
ATOM   1565 H  HB   . ILE   A 1 69  ? 36.953 6.521   -0.979  1.00 15.93 ?  69  ILE   A HB   1 
ATOM   1566 H  HG12 . ILE   A 1 69  ? 35.673 4.687   -0.135  1.00 16.73 ?  69  ILE   A HG12 1 
ATOM   1567 H  HG13 . ILE   A 1 69  ? 34.970 5.492   -1.308  1.00 16.73 ?  69  ILE   A HG13 1 
ATOM   1568 H  HG21 . ILE   A 1 69  ? 36.408 6.025   -3.301  1.00 17.60 ?  69  ILE   A HG21 1 
ATOM   1569 H  HG22 . ILE   A 1 69  ? 37.881 6.542   -3.017  1.00 17.60 ?  69  ILE   A HG22 1 
ATOM   1570 H  HG23 . ILE   A 1 69  ? 37.612 4.991   -3.241  1.00 17.60 ?  69  ILE   A HG23 1 
ATOM   1571 H  HD11 . ILE   A 1 69  ? 34.760 3.152   -1.530  1.00 17.24 ?  69  ILE   A HD11 1 
ATOM   1572 H  HD12 . ILE   A 1 69  ? 35.424 3.833   -2.801  1.00 17.24 ?  69  ILE   A HD12 1 
ATOM   1573 H  HD13 . ILE   A 1 69  ? 36.331 3.070   -1.742  1.00 17.24 ?  69  ILE   A HD13 1 
ATOM   1574 N  N    . ALA   A 1 70  ? 39.976 6.605   -0.470  1.00 13.32 ?  70  ALA   A N    1 
ATOM   1575 C  CA   . ALA   A 1 70  ? 41.253 7.215   -0.822  1.00 14.30 ?  70  ALA   A CA   1 
ATOM   1576 C  C    . ALA   A 1 70  ? 42.402 6.234   -0.645  1.00 14.64 ?  70  ALA   A C    1 
ATOM   1577 O  O    . ALA   A 1 70  ? 43.374 6.274   -1.402  1.00 16.45 ?  70  ALA   A O    1 
ATOM   1578 C  CB   . ALA   A 1 70  ? 41.485 8.472   0.021   1.00 14.65 ?  70  ALA   A CB   1 
ATOM   1579 H  H    . ALA   A 1 70  ? 39.548 6.996   0.160   1.00 15.97 ?  70  ALA   A H    1 
ATOM   1580 H  HA   . ALA   A 1 70  ? 41.227 7.490   -1.755  1.00 17.14 ?  70  ALA   A HA   1 
ATOM   1581 H  HB1  . ALA   A 1 70  ? 42.342 8.863   -0.226  1.00 17.57 ?  70  ALA   A HB1  1 
ATOM   1582 H  HB2  . ALA   A 1 70  ? 40.774 9.108   -0.147  1.00 17.57 ?  70  ALA   A HB2  1 
ATOM   1583 H  HB3  . ALA   A 1 70  ? 41.497 8.226   0.959   1.00 17.57 ?  70  ALA   A HB3  1 
ATOM   1584 N  N    . THR   A 1 71  ? 42.291 5.329   0.324   1.00 14.14 ?  71  THR   A N    1 
ATOM   1585 C  CA   . THR   A 1 71  ? 43.341 4.352   0.586   1.00 15.80 ?  71  THR   A CA   1 
ATOM   1586 C  C    . THR   A 1 71  ? 43.224 3.122   -0.305  1.00 15.70 ?  71  THR   A C    1 
ATOM   1587 O  O    . THR   A 1 71  ? 44.239 2.600   -0.782  1.00 17.90 ?  71  THR   A O    1 
ATOM   1588 C  CB   . THR   A 1 71  ? 43.258 3.907   2.042   1.00 18.03 ?  71  THR   A CB   1 
ATOM   1589 O  OG1  . THR   A 1 71  ? 43.502 5.030   2.893   1.00 19.61 ?  71  THR   A OG1  1 
ATOM   1590 C  CG2  . THR   A 1 71  ? 44.261 2.798   2.339   1.00 19.53 ?  71  THR   A CG2  1 
ATOM   1591 H  H    . THR   A 1 71  ? 41.610 5.256   0.839   1.00 16.95 ?  71  THR   A H    1 
ATOM   1592 H  HA   . THR   A 1 71  ? 44.207 4.753   0.430   1.00 18.95 ?  71  THR   A HA   1 
ATOM   1593 H  HB   . THR   A 1 71  ? 42.366 3.557   2.213   1.00 21.62 ?  71  THR   A HB   1 
ATOM   1594 H  HG1  . THR   A 1 71  ? 42.925 5.622   2.746   1.00 23.52 ?  71  THR   A HG1  1 
ATOM   1595 H  HG21 . THR   A 1 71  ? 44.389 2.721   3.297   1.00 23.42 ?  71  THR   A HG21 1 
ATOM   1596 H  HG22 . THR   A 1 71  ? 43.941 1.948   1.996   1.00 23.42 ?  71  THR   A HG22 1 
ATOM   1597 H  HG23 . THR   A 1 71  ? 45.115 3.004   1.924   1.00 23.42 ?  71  THR   A HG23 1 
ATOM   1598 N  N    . ASN   A 1 72  ? 42.001 2.624   -0.512  1.00 14.41 ?  72  ASN   A N    1 
ATOM   1599 C  CA   . ASN   A 1 72  ? 41.780 1.296   -1.066  1.00 14.69 ?  72  ASN   A CA   1 
ATOM   1600 C  C    . ASN   A 1 72  ? 41.162 1.280   -2.452  1.00 14.78 ?  72  ASN   A C    1 
ATOM   1601 O  O    . ASN   A 1 72  ? 41.164 0.222   -3.093  1.00 15.87 ?  72  ASN   A O    1 
ATOM   1602 C  CB   . ASN   A 1 72  ? 40.885 0.482   -0.125  1.00 15.60 ?  72  ASN   A CB   1 
ATOM   1603 C  CG   . ASN   A 1 72  ? 41.494 0.331   1.244   1.00 16.58 ?  72  ASN   A CG   1 
ATOM   1604 O  OD1  . ASN   A 1 72  ? 41.043 0.930   2.215   1.00 18.44 ?  72  ASN   A OD1  1 
ATOM   1605 N  ND2  . ASN   A 1 72  ? 42.548 -0.447  1.322   1.00 17.09 ?  72  ASN   A ND2  1 
ATOM   1606 H  H    . ASN   A 1 72  ? 41.270 3.050   -0.335  1.00 17.27 ?  72  ASN   A H    1 
ATOM   1607 H  HA   . ASN   A 1 72  ? 42.632 0.845   -1.131  1.00 17.61 ?  72  ASN   A HA   1 
ATOM   1608 H  HB2  . ASN   A 1 72  ? 40.031 0.927   -0.036  1.00 18.70 ?  72  ASN   A HB2  1 
ATOM   1609 H  HB3  . ASN   A 1 72  ? 40.762 -0.405  -0.502  1.00 18.70 ?  72  ASN   A HB3  1 
ATOM   1610 H  HD21 . ASN   A 1 72  ? 42.939 -0.560  2.080   1.00 20.49 ?  72  ASN   A HD21 1 
ATOM   1611 H  HD22 . ASN   A 1 72  ? 42.849 -0.842  0.620   1.00 20.49 ?  72  ASN   A HD22 1 
ATOM   1612 N  N    . GLY   A 1 73  ? 40.615 2.395   -2.920  1.00 14.23 ?  73  GLY   A N    1 
ATOM   1613 C  CA   . GLY   A 1 73  ? 39.879 2.402   -4.158  1.00 13.90 ?  73  GLY   A CA   1 
ATOM   1614 C  C    . GLY   A 1 73  ? 38.485 1.836   -3.985  1.00 13.48 ?  73  GLY   A C    1 
ATOM   1615 O  O    . GLY   A 1 73  ? 38.090 1.393   -2.900  1.00 14.26 ?  73  GLY   A O    1 
ATOM   1616 H  H    . GLY   A 1 73  ? 40.660 3.168   -2.538  1.00 17.06 ?  73  GLY   A H    1 
ATOM   1617 H  HA2  . GLY   A 1 73  ? 39.810 3.315   -4.488  1.00 16.66 ?  73  GLY   A HA2  1 
ATOM   1618 H  HA3  . GLY   A 1 73  ? 40.353 1.874   -4.822  1.00 16.66 ?  73  GLY   A HA3  1 
ATOM   1619 N  N    . PRO   A 1 74  ? 37.710 1.857   -5.067  1.00 13.89 ?  74  PRO   A N    1 
ATOM   1620 C  CA   . PRO   A 1 74  ? 36.311 1.430   -4.989  1.00 13.91 ?  74  PRO   A CA   1 
ATOM   1621 C  C    . PRO   A 1 74  ? 36.162 -0.051  -4.671  1.00 13.41 ?  74  PRO   A C    1 
ATOM   1622 O  O    . PRO   A 1 74  ? 37.033 -0.880  -4.950  1.00 14.25 ?  74  PRO   A O    1 
ATOM   1623 C  CB   . PRO   A 1 74  ? 35.770 1.731   -6.393  1.00 15.75 ?  74  PRO   A CB   1 
ATOM   1624 C  CG   . PRO   A 1 74  ? 36.725 2.698   -6.994  1.00 18.46 ?  74  PRO   A CG   1 
ATOM   1625 C  CD   . PRO   A 1 74  ? 38.056 2.361   -6.406  1.00 15.92 ?  74  PRO   A CD   1 
ATOM   1626 H  HA   . PRO   A 1 74  ? 35.828 1.957   -4.332  1.00 16.67 ?  74  PRO   A HA   1 
ATOM   1627 H  HB2  . PRO   A 1 74  ? 35.738 0.910   -6.909  1.00 18.88 ?  74  PRO   A HB2  1 
ATOM   1628 H  HB3  . PRO   A 1 74  ? 34.884 2.123   -6.322  1.00 18.88 ?  74  PRO   A HB3  1 
ATOM   1629 H  HG2  . PRO   A 1 74  ? 36.741 2.585   -7.956  1.00 22.14 ?  74  PRO   A HG2  1 
ATOM   1630 H  HG3  . PRO   A 1 74  ? 36.468 3.600   -6.757  1.00 22.14 ?  74  PRO   A HG3  1 
ATOM   1631 H  HD2  . PRO   A 1 74  ? 38.498 1.670   -6.929  1.00 19.08 ?  74  PRO   A HD2  1 
ATOM   1632 H  HD3  . PRO   A 1 74  ? 38.607 3.160   -6.346  1.00 19.08 ?  74  PRO   A HD3  1 
ATOM   1633 N  N    . LEU   A 1 75  ? 35.016 -0.374  -4.085  1.00 12.73 ?  75  LEU   A N    1 
ATOM   1634 C  CA   . LEU   A 1 75  ? 34.613 -1.761  -3.943  1.00 12.19 ?  75  LEU   A CA   1 
ATOM   1635 C  C    . LEU   A 1 75  ? 34.230 -2.335  -5.305  1.00 13.07 ?  75  LEU   A C    1 
ATOM   1636 O  O    . LEU   A 1 75  ? 34.098 -1.618  -6.302  1.00 14.48 ?  75  LEU   A O    1 
ATOM   1637 C  CB   . LEU   A 1 75  ? 33.424 -1.881  -2.993  1.00 12.54 ?  75  LEU   A CB   1 
ATOM   1638 C  CG   . LEU   A 1 75  ? 33.630 -1.474  -1.537  1.00 13.82 ?  75  LEU   A CG   1 
ATOM   1639 C  CD1  . LEU   A 1 75  ? 32.338 -1.667  -0.753  1.00 16.04 ?  75  LEU   A CD1  1 
ATOM   1640 C  CD2  . LEU   A 1 75  ? 34.763 -2.203  -0.872  1.00 16.93 ?  75  LEU   A CD2  1 
ATOM   1641 H  H    . LEU   A 1 75  ? 34.461 0.193   -3.757  1.00 15.26 ?  75  LEU   A H    1 
ATOM   1642 H  HA   . LEU   A 1 75  ? 35.348 -2.279  -3.587  1.00 14.61 ?  75  LEU   A HA   1 
ATOM   1643 H  HB2  . LEU   A 1 75  ? 32.705 -1.333  -3.341  1.00 15.03 ?  75  LEU   A HB2  1 
ATOM   1644 H  HB3  . LEU   A 1 75  ? 33.140 -2.810  -2.989  1.00 15.03 ?  75  LEU   A HB3  1 
ATOM   1645 H  HG   . LEU   A 1 75  ? 33.847 -0.529  -1.515  1.00 16.57 ?  75  LEU   A HG   1 
ATOM   1646 H  HD11 . LEU   A 1 75  ? 32.488 -1.400  0.168   1.00 19.23 ?  75  LEU   A HD11 1 
ATOM   1647 H  HD12 . LEU   A 1 75  ? 31.647 -1.113  -1.149  1.00 19.23 ?  75  LEU   A HD12 1 
ATOM   1648 H  HD13 . LEU   A 1 75  ? 32.082 -2.599  -0.792  1.00 19.23 ?  75  LEU   A HD13 1 
ATOM   1649 H  HD21 . LEU   A 1 75  ? 34.811 -1.932  0.060   1.00 20.30 ?  75  LEU   A HD21 1 
ATOM   1650 H  HD22 . LEU   A 1 75  ? 34.609 -3.157  -0.932  1.00 20.30 ?  75  LEU   A HD22 1 
ATOM   1651 H  HD23 . LEU   A 1 75  ? 35.597 -1.974  -1.320  1.00 20.30 ?  75  LEU   A HD23 1 
ATOM   1652 N  N    . LYS   A 1 76  ? 34.054 -3.655  -5.329  1.00 13.36 ?  76  LYS   A N    1 
ATOM   1653 C  CA   . LYS   A 1 76  ? 33.451 -4.372  -6.448  1.00 13.81 ?  76  LYS   A CA   1 
ATOM   1654 C  C    . LYS   A 1 76  ? 31.939 -4.451  -6.249  1.00 12.45 ?  76  LYS   A C    1 
ATOM   1655 O  O    . LYS   A 1 76  ? 31.462 -4.569  -5.124  1.00 12.65 ?  76  LYS   A O    1 
ATOM   1656 C  CB   . LYS   A 1 76  ? 33.991 -5.811  -6.506  1.00 15.17 ?  76  LYS   A CB   1 
ATOM   1657 C  CG   . LYS   A 1 76  ? 35.498 -5.919  -6.718  1.00 16.75 ?  76  LYS   A CG   1 
ATOM   1658 C  CD   . LYS   A 1 76  ? 36.028 -7.318  -6.472  1.00 18.24 ?  76  LYS   A CD   1 
ATOM   1659 C  CE   . LYS   A 1 76  ? 37.531 -7.373  -6.646  1.00 20.56 ?  76  LYS   A CE   1 
ATOM   1660 N  NZ   . LYS   A 1 76  ? 38.058 -8.738  -6.470  1.00 21.24 ?  76  LYS   A NZ   1 
ATOM   1661 H  H    . LYS   A 1 76  ? 34.291 -4.178  -4.686  1.00 16.02 ?  76  LYS   A H    1 
ATOM   1662 H  HA   . LYS   A 1 76  ? 33.645 -3.919  -7.284  1.00 16.55 ?  76  LYS   A HA   1 
ATOM   1663 H  HB2  . LYS   A 1 76  ? 33.778 -6.253  -5.670  1.00 18.19 ?  76  LYS   A HB2  1 
ATOM   1664 H  HB3  . LYS   A 1 76  ? 33.556 -6.272  -7.240  1.00 18.19 ?  76  LYS   A HB3  1 
ATOM   1665 H  HG2  . LYS   A 1 76  ? 35.708 -5.675  -7.634  1.00 20.09 ?  76  LYS   A HG2  1 
ATOM   1666 H  HG3  . LYS   A 1 76  ? 35.949 -5.317  -6.105  1.00 20.09 ?  76  LYS   A HG3  1 
ATOM   1667 H  HD2  . LYS   A 1 76  ? 35.814 -7.589  -5.565  1.00 21.87 ?  76  LYS   A HD2  1 
ATOM   1668 H  HD3  . LYS   A 1 76  ? 35.624 -7.931  -7.108  1.00 21.87 ?  76  LYS   A HD3  1 
ATOM   1669 H  HE2  . LYS   A 1 76  ? 37.761 -7.075  -7.538  1.00 24.65 ?  76  LYS   A HE2  1 
ATOM   1670 H  HE3  . LYS   A 1 76  ? 37.950 -6.804  -5.982  1.00 24.65 ?  76  LYS   A HE3  1 
ATOM   1671 H  HZ1  . LYS   A 1 76  ? 38.942 -8.750  -6.577  1.00 25.48 ?  76  LYS   A HZ1  1 
ATOM   1672 H  HZ2  . LYS   A 1 76  ? 37.864 -9.045  -5.654  1.00 25.48 ?  76  LYS   A HZ2  1 
ATOM   1673 H  HZ3  . LYS   A 1 76  ? 37.692 -9.292  -7.071  1.00 25.48 ?  76  LYS   A HZ3  1 
ATOM   1674 N  N    . VAL   A 1 77  ? 31.185 -4.417  -7.352  1.00 12.88 ?  77  VAL   A N    1 
ATOM   1675 C  CA   . VAL   A 1 77  ? 29.779 -4.801  -7.263  1.00 12.87 ?  77  VAL   A CA   1 
ATOM   1676 C  C    . VAL   A 1 77  ? 29.716 -6.256  -6.821  1.00 12.55 ?  77  VAL   A C    1 
ATOM   1677 O  O    . VAL   A 1 77  ? 30.372 -7.128  -7.406  1.00 13.13 ?  77  VAL   A O    1 
ATOM   1678 C  CB   . VAL   A 1 77  ? 29.055 -4.586  -8.600  1.00 13.71 ?  77  VAL   A CB   1 
ATOM   1679 C  CG1  . VAL   A 1 77  ? 27.601 -5.043  -8.488  1.00 14.51 ?  77  VAL   A CG1  1 
ATOM   1680 C  CG2  . VAL   A 1 77  ? 29.125 -3.134  -9.016  1.00 15.25 ?  77  VAL   A CG2  1 
ATOM   1681 H  H    . VAL   A 1 77  ? 31.461 -4.176  -8.130  1.00 15.44 ?  77  VAL   A H    1 
ATOM   1682 H  HA   . VAL   A 1 77  ? 29.342 -4.257  -6.588  1.00 15.43 ?  77  VAL   A HA   1 
ATOM   1683 H  HB   . VAL   A 1 77  ? 29.490 -5.116  -9.286  1.00 16.44 ?  77  VAL   A HB   1 
ATOM   1684 H  HG11 . VAL   A 1 77  ? 27.114 -4.729  -9.264  1.00 17.40 ?  77  VAL   A HG11 1 
ATOM   1685 H  HG12 . VAL   A 1 77  ? 27.575 -6.012  -8.450  1.00 17.40 ?  77  VAL   A HG12 1 
ATOM   1686 H  HG13 . VAL   A 1 77  ? 27.216 -4.668  -7.680  1.00 17.40 ?  77  VAL   A HG13 1 
ATOM   1687 H  HG21 . VAL   A 1 77  ? 28.619 -3.016  -9.834  1.00 18.29 ?  77  VAL   A HG21 1 
ATOM   1688 H  HG22 . VAL   A 1 77  ? 28.743 -2.587  -8.309  1.00 18.29 ?  77  VAL   A HG22 1 
ATOM   1689 H  HG23 . VAL   A 1 77  ? 30.051 -2.889  -9.159  1.00 18.29 ?  77  VAL   A HG23 1 
ATOM   1690 N  N    . GLY   A 1 78  ? 28.934 -6.527  -5.776  1.00 12.37 ?  78  GLY   A N    1 
ATOM   1691 C  CA   . GLY   A 1 78  ? 28.912 -7.820  -5.126  1.00 12.62 ?  78  GLY   A CA   1 
ATOM   1692 C  C    . GLY   A 1 78  ? 29.826 -7.915  -3.927  1.00 12.09 ?  78  GLY   A C    1 
ATOM   1693 O  O    . GLY   A 1 78  ? 29.776 -8.922  -3.204  1.00 12.86 ?  78  GLY   A O    1 
ATOM   1694 H  H    . GLY   A 1 78  ? 28.385 -5.955  -5.430  1.00 14.83 ?  78  GLY   A H    1 
ATOM   1695 H  HA2  . GLY   A 1 78  ? 28.007 -8.012  -4.840  1.00 15.13 ?  78  GLY   A HA2  1 
ATOM   1696 H  HA3  . GLY   A 1 78  ? 29.175 -8.497  -5.770  1.00 15.13 ?  78  GLY   A HA3  1 
ATOM   1697 N  N    . GLY   A 1 79  ? 30.677 -6.905  -3.705  1.00 12.04 ?  79  GLY   A N    1 
ATOM   1698 C  CA   . GLY   A 1 79  ? 31.645 -6.921  -2.634  1.00 12.44 ?  79  GLY   A CA   1 
ATOM   1699 C  C    . GLY   A 1 79  ? 31.197 -6.129  -1.414  1.00 11.66 ?  79  GLY   A C    1 
ATOM   1700 O  O    . GLY   A 1 79  ? 30.082 -5.620  -1.337  1.00 12.41 ?  79  GLY   A O    1 
ATOM   1701 H  H    . GLY   A 1 79  ? 30.708 -6.187  -4.183  1.00 14.43 ?  79  GLY   A H    1 
ATOM   1702 H  HA2  . GLY   A 1 79  ? 31.803 -7.848  -2.367  1.00 14.91 ?  79  GLY   A HA2  1 
ATOM   1703 H  HA3  . GLY   A 1 79  ? 32.482 -6.555  -2.951  1.00 14.91 ?  79  GLY   A HA3  1 
ATOM   1704 N  N    . SER   A 1 80  ? 32.102 -6.037  -0.443  1.00 12.48 ?  80  SER   A N    1 
ATOM   1705 C  CA   . SER   A 1 80  ? 31.780 -5.404  0.827   1.00 12.13 ?  80  SER   A CA   1 
ATOM   1706 C  C    . SER   A 1 80  ? 33.053 -4.956  1.526   1.00 11.78 ?  80  SER   A C    1 
ATOM   1707 O  O    . SER   A 1 80  ? 34.162 -5.388  1.196   1.00 13.29 ?  80  SER   A O    1 
ATOM   1708 C  CB   . SER   A 1 80  ? 31.018 -6.365  1.745   1.00 13.33 ?  80  SER   A CB   1 
ATOM   1709 O  OG   . SER   A 1 80  ? 31.853 -7.408  2.225   1.00 14.60 ?  80  SER   A OG   1 
ATOM   1710 H  H    . SER   A 1 80  ? 32.911 -6.323  -0.502  1.00 14.96 ?  80  SER   A H    1 
ATOM   1711 H  HA   . SER   A 1 80  ? 31.226 -4.624  0.645   1.00 14.54 ?  80  SER   A HA   1 
ATOM   1712 H  HB2  . SER   A 1 80  ? 30.670 -5.861  2.495   1.00 15.98 ?  80  SER   A HB2  1 
ATOM   1713 H  HB3  . SER   A 1 80  ? 30.283 -6.755  1.241   1.00 15.98 ?  80  SER   A HB3  1 
ATOM   1714 H  HG   . SER   A 1 80  ? 32.161 -7.841  1.575   1.00 17.50 ?  80  SER   A HG   1 
ATOM   1715 N  N    . CYS   A 1 81  ? 32.868 -4.104  2.532   1.00 11.61 ?  81  CYS   A N    1 
ATOM   1716 C  CA   . CYS   A 1 81  ? 33.916 -3.818  3.498   1.00 12.09 ?  81  CYS   A CA   1 
ATOM   1717 C  C    . CYS   A 1 81  ? 33.270 -3.583  4.856   1.00 11.61 ?  81  CYS   A C    1 
ATOM   1718 O  O    . CYS   A 1 81  ? 32.103 -3.184  4.946   1.00 12.82 ?  81  CYS   A O    1 
ATOM   1719 C  CB   . CYS   A 1 81  ? 34.787 -2.623  3.085   1.00 12.79 ?  81  CYS   A CB   1 
ATOM   1720 S  SG   . CYS   A 1 81  ? 33.888 -1.052  3.096   1.00 12.41 ?  81  CYS   A SG   1 
ATOM   1721 H  H    . CYS   A 1 81  ? 32.127 -3.685  2.685   1.00 13.91 ?  81  CYS   A H    1 
ATOM   1722 H  HA   . CYS   A 1 81  ? 34.492 -4.592  3.572   1.00 14.50 ?  81  CYS   A HA   1 
ATOM   1723 H  HB2  . CYS   A 1 81  ? 35.533 -2.552  3.703   1.00 15.34 ?  81  CYS   A HB2  1 
ATOM   1724 H  HB3  . CYS   A 1 81  ? 35.120 -2.775  2.185   1.00 15.34 ?  81  CYS   A HB3  1 
ATOM   1725 H  HG   . CYS   A 1 81  ? 34.642 -0.174  2.767   1.00 14.87 ?  81  CYS   A HG   1 
ATOM   1726 N  N    . VAL   A 1 82  ? 34.040 -3.841  5.910   1.00 12.05 ?  82  VAL   A N    1 
ATOM   1727 C  CA   . VAL   A 1 82  ? 33.617 -3.596  7.281   1.00 12.64 ?  82  VAL   A CA   1 
ATOM   1728 C  C    . VAL   A 1 82  ? 34.215 -2.279  7.748   1.00 12.99 ?  82  VAL   A C    1 
ATOM   1729 O  O    . VAL   A 1 82  ? 35.439 -2.107  7.733   1.00 13.32 ?  82  VAL   A O    1 
ATOM   1730 C  CB   . VAL   A 1 82  ? 34.039 -4.737  8.215   1.00 14.43 ?  82  VAL   A CB   1 
ATOM   1731 C  CG1  . VAL   A 1 82  ? 33.592 -4.445  9.641   1.00 15.85 ?  82  VAL   A CG1  1 
ATOM   1732 C  CG2  . VAL   A 1 82  ? 33.470 -6.059  7.737   1.00 15.26 ?  82  VAL   A CG2  1 
ATOM   1733 H  H    . VAL   A 1 82  ? 34.836 -4.179  5.849   1.00 14.44 ?  82  VAL   A H    1 
ATOM   1734 H  HA   . VAL   A 1 82  ? 32.652 -3.516  7.304   1.00 15.16 ?  82  VAL   A HA   1 
ATOM   1735 H  HB   . VAL   A 1 82  ? 35.005 -4.803  8.214   1.00 17.29 ?  82  VAL   A HB   1 
ATOM   1736 H  HG11 . VAL   A 1 82  ? 33.687 -5.251  10.171  1.00 19.01 ?  82  VAL   A HG11 1 
ATOM   1737 H  HG12 . VAL   A 1 82  ? 34.143 -3.739  10.014  1.00 19.01 ?  82  VAL   A HG12 1 
ATOM   1738 H  HG13 . VAL   A 1 82  ? 32.660 -4.167  9.631   1.00 19.01 ?  82  VAL   A HG13 1 
ATOM   1739 H  HG21 . VAL   A 1 82  ? 33.704 -6.752  8.372   1.00 18.30 ?  82  VAL   A HG21 1 
ATOM   1740 H  HG22 . VAL   A 1 82  ? 32.503 -5.983  7.673   1.00 18.30 ?  82  VAL   A HG22 1 
ATOM   1741 H  HG23 . VAL   A 1 82  ? 33.842 -6.268  6.866   1.00 18.30 ?  82  VAL   A HG23 1 
ATOM   1742 N  N    . LEU   A 1 83  ? 33.357 -1.355  8.167   1.00 12.28 ?  83  LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 83  ? 33.779 -0.094  8.751   1.00 11.96 ?  83  LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 83  ? 33.057 0.082   10.082  1.00 12.21 ?  83  LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 83  ? 32.335 -0.808  10.546  1.00 13.10 ?  83  LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 83  ? 33.528 1.067   7.777   1.00 12.57 ?  83  LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 83  ? 34.422 1.060   6.532   1.00 13.14 ?  83  LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 83  ? 33.990 2.109   5.523   1.00 13.92 ?  83  LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 83  ? 35.894 1.271   6.906   1.00 13.88 ?  83  LEU   A CD2  1 
ATOM   1750 H  H    . LEU   A 1 83  ? 32.504 -1.438  8.115   1.00 14.71 ?  83  LEU   A H    1 
ATOM   1751 H  HA   . LEU   A 1 83  ? 34.728 -0.121  8.929   1.00 14.33 ?  83  LEU   A HA   1 
ATOM   1752 H  HB2  . LEU   A 1 83  ? 32.609 1.031   7.465   1.00 15.07 ?  83  LEU   A HB2  1 
ATOM   1753 H  HB3  . LEU   A 1 83  ? 33.680 1.909   8.234   1.00 15.07 ?  83  LEU   A HB3  1 
ATOM   1754 H  HG   . LEU   A 1 83  ? 34.355 0.194   6.102   1.00 15.75 ?  83  LEU   A HG   1 
ATOM   1755 H  HD11 . LEU   A 1 83  ? 34.578 2.066   4.749   1.00 16.68 ?  83  LEU   A HD11 1 
ATOM   1756 H  HD12 . LEU   A 1 83  ? 33.078 1.925   5.252   1.00 16.68 ?  83  LEU   A HD12 1 
ATOM   1757 H  HD13 . LEU   A 1 83  ? 34.047 2.985   5.932   1.00 16.68 ?  83  LEU   A HD13 1 
ATOM   1758 H  HD21 . LEU   A 1 83  ? 36.414 1.419   6.095   1.00 16.64 ?  83  LEU   A HD21 1 
ATOM   1759 H  HD22 . LEU   A 1 83  ? 35.969 2.048   7.485   1.00 16.64 ?  83  LEU   A HD22 1 
ATOM   1760 H  HD23 . LEU   A 1 83  ? 36.226 0.485   7.366   1.00 16.64 ?  83  LEU   A HD23 1 
ATOM   1761 N  N    . SER   A 1 84  ? 33.263 1.236   10.706  1.00 12.98 ?  84  SER   A N    1 
ATOM   1762 C  CA   . SER   A 1 84  ? 32.625 1.498   11.983  1.00 12.92 ?  84  SER   A CA   1 
ATOM   1763 C  C    . SER   A 1 84  ? 31.108 1.583   11.841  1.00 12.96 ?  84  SER   A C    1 
ATOM   1764 O  O    . SER   A 1 84  ? 30.579 2.036   10.825  1.00 13.12 ?  84  SER   A O    1 
ATOM   1765 C  CB   . SER   A 1 84  ? 33.113 2.826   12.547  1.00 13.83 ?  84  SER   A CB   1 
ATOM   1766 O  OG   . SER   A 1 84  ? 32.498 3.090   13.790  1.00 15.17 ?  84  SER   A OG   1 
ATOM   1767 H  H    . SER   A 1 84  ? 33.754 1.883   10.405  1.00 15.56 ?  84  SER   A H    1 
ATOM   1768 H  HA   . SER   A 1 84  ? 32.847 0.792   12.604  1.00 15.49 ?  84  SER   A HA   1 
ATOM   1769 H  HB2  . SER   A 1 84  ? 34.074 2.788   12.663  1.00 16.58 ?  84  SER   A HB2  1 
ATOM   1770 H  HB3  . SER   A 1 84  ? 32.881 3.538   11.927  1.00 16.58 ?  84  SER   A HB3  1 
ATOM   1771 H  HG   . SER   A 1 84  ? 32.777 3.819   14.102  1.00 18.18 ?  84  SER   A HG   1 
ATOM   1772 N  N    . GLY   A 1 85  ? 30.404 1.166   12.892  1.00 13.97 ?  85  GLY   A N    1 
ATOM   1773 C  CA   . GLY   A 1 85  ? 28.980 1.392   12.993  1.00 14.47 ?  85  GLY   A CA   1 
ATOM   1774 C  C    . GLY   A 1 85  ? 28.606 2.711   13.626  1.00 14.18 ?  85  GLY   A C    1 
ATOM   1775 O  O    . GLY   A 1 85  ? 27.414 3.023   13.733  1.00 14.97 ?  85  GLY   A O    1 
ATOM   1776 H  H    . GLY   A 1 85  ? 30.744 0.741   13.563  1.00 16.75 ?  85  GLY   A H    1 
ATOM   1777 H  HA2  . GLY   A 1 85  ? 28.595 1.359   12.105  1.00 17.35 ?  85  GLY   A HA2  1 
ATOM   1778 H  HA3  . GLY   A 1 85  ? 28.586 0.680   13.518  1.00 17.35 ?  85  GLY   A HA3  1 
ATOM   1779 N  N    . HIS   A 1 86  ? 29.591 3.496   14.056  1.00 13.89 ?  86  HIS   A N    1 
ATOM   1780 C  CA   . HIS   A 1 86  ? 29.368 4.831   14.622  1.00 14.15 ?  86  HIS   A CA   1 
ATOM   1781 C  C    . HIS   A 1 86  ? 28.388 4.709   15.782  1.00 15.11 ?  86  HIS   A C    1 
ATOM   1782 O  O    . HIS   A 1 86  ? 28.580 3.835   16.643  1.00 16.54 ?  86  HIS   A O    1 
ATOM   1783 C  CB   . HIS   A 1 86  ? 28.992 5.809   13.518  1.00 14.18 ?  86  HIS   A CB   1 
ATOM   1784 C  CG   . HIS   A 1 86  ? 30.047 5.904   12.475  1.00 13.99 ?  86  HIS   A CG   1 
ATOM   1785 N  ND1  . HIS   A 1 86  ? 31.129 6.748   12.593  1.00 15.24 ?  86  HIS   A ND1  1 
ATOM   1786 C  CD2  . HIS   A 1 86  ? 30.229 5.207   11.331  1.00 13.65 ?  86  HIS   A CD2  1 
ATOM   1787 C  CE1  . HIS   A 1 86  ? 31.918 6.585   11.547  1.00 14.79 ?  86  HIS   A CE1  1 
ATOM   1788 N  NE2  . HIS   A 1 86  ? 31.405 5.644   10.777  1.00 14.13 ?  86  HIS   A NE2  1 
ATOM   1789 H  H    . HIS   A 1 86  ? 30.418 3.276   14.036  1.00 16.65 ?  86  HIS   A H    1 
ATOM   1790 H  HA   . HIS   A 1 86  ? 30.204 5.144   14.993  1.00 16.97 ?  86  HIS   A HA   1 
ATOM   1791 H  HB2  . HIS   A 1 86  ? 28.166 5.524   13.093  1.00 17.00 ?  86  HIS   A HB2  1 
ATOM   1792 H  HB3  . HIS   A 1 86  ? 28.870 6.700   13.899  1.00 17.00 ?  86  HIS   A HB3  1 
ATOM   1793 H  HD2  . HIS   A 1 86  ? 29.668 4.539   10.991  1.00 16.36 ?  86  HIS   A HD2  1 
ATOM   1794 H  HE1  . HIS   A 1 86  ? 32.702 7.050   11.374  1.00 17.74 ?  86  HIS   A HE1  1 
ATOM   1795 H  HE2  . HIS   A 1 86  ? 31.735 5.366   10.026  1.00 16.94 ?  86  HIS   A HE2  1 
ATOM   1796 N  N    . ASN   A 1 87  ? 27.370 5.555   15.855  1.00 16.40 ?  87  ASN   A N    1 
ATOM   1797 C  CA   . ASN   A 1 87  ? 26.393 5.545   16.928  1.00 17.20 ?  87  ASN   A CA   1 
ATOM   1798 C  C    . ASN   A 1 87  ? 25.269 4.549   16.696  1.00 18.45 ?  87  ASN   A C    1 
ATOM   1799 O  O    . ASN   A 1 87  ? 24.351 4.484   17.516  1.00 20.59 ?  87  ASN   A O    1 
ATOM   1800 C  CB   . ASN   A 1 87  ? 25.796 6.951   17.083  1.00 17.98 ?  87  ASN   A CB   1 
ATOM   1801 C  CG   . ASN   A 1 87  ? 25.304 7.532   15.761  1.00 18.94 ?  87  ASN   A CG   1 
ATOM   1802 O  OD1  . ASN   A 1 87  ? 25.957 7.408   14.727  1.00 19.25 ?  87  ASN   A OD1  1 
ATOM   1803 N  ND2  . ASN   A 1 87  ? 24.151 8.173   15.795  1.00 19.94 ?  87  ASN   A ND2  1 
ATOM   1804 H  H    . ASN   A 1 87  ? 27.213 6.159   15.269  1.00 19.67 ?  87  ASN   A H    1 
ATOM   1805 H  HA   . ASN   A 1 87  ? 26.827 5.306   17.765  1.00 20.62 ?  87  ASN   A HA   1 
ATOM   1806 H  HB2  . ASN   A 1 87  ? 25.039 6.906   17.697  1.00 21.56 ?  87  ASN   A HB2  1 
ATOM   1807 H  HB3  . ASN   A 1 87  ? 26.475 7.540   17.443  1.00 21.56 ?  87  ASN   A HB3  1 
ATOM   1808 H  HD21 . ASN   A 1 87  ? 23.836 8.514   15.074  1.00 23.92 ?  87  ASN   A HD21 1 
ATOM   1809 H  HD22 . ASN   A 1 87  ? 23.723 8.250   16.536  1.00 23.92 ?  87  ASN   A HD22 1 
ATOM   1810 N  N    . LEU   A 1 88  ? 25.317 3.774   15.617  1.00 17.30 ?  88  LEU   A N    1 
ATOM   1811 C  CA   . LEU   A 1 88  ? 24.205 2.916   15.223  1.00 17.01 ?  88  LEU   A CA   1 
ATOM   1812 C  C    . LEU   A 1 88  ? 24.423 1.438   15.506  1.00 16.59 ?  88  LEU   A C    1 
ATOM   1813 O  O    . LEU   A 1 88  ? 23.445 0.706   15.677  1.00 17.69 ?  88  LEU   A O    1 
ATOM   1814 C  CB   . LEU   A 1 88  ? 23.945 3.080   13.724  1.00 17.32 ?  88  LEU   A CB   1 
ATOM   1815 C  CG   . LEU   A 1 88  ? 23.658 4.507   13.250  1.00 18.79 ?  88  LEU   A CG   1 
ATOM   1816 C  CD1  . LEU   A 1 88  ? 23.511 4.535   11.742  1.00 19.37 ?  88  LEU   A CD1  1 
ATOM   1817 C  CD2  . LEU   A 1 88  ? 22.408 5.062   13.920  1.00 20.37 ?  88  LEU   A CD2  1 
ATOM   1818 H  H    . LEU   A 1 88  ? 25.998 3.722   15.097  1.00 20.74 ?  88  LEU   A H    1 
ATOM   1819 H  HA   . LEU   A 1 88  ? 23.406 3.200   15.695  1.00 20.40 ?  88  LEU   A HA   1 
ATOM   1820 H  HB2  . LEU   A 1 88  ? 24.724 2.770   13.242  1.00 20.77 ?  88  LEU   A HB2  1 
ATOM   1821 H  HB3  . LEU   A 1 88  ? 23.177 2.541   13.486  1.00 20.77 ?  88  LEU   A HB3  1 
ATOM   1822 H  HG   . LEU   A 1 88  ? 24.405 5.080   13.488  1.00 22.54 ?  88  LEU   A HG   1 
ATOM   1823 H  HD11 . LEU   A 1 88  ? 23.343 5.449   11.457  1.00 23.23 ?  88  LEU   A HD11 1 
ATOM   1824 H  HD12 . LEU   A 1 88  ? 24.331 4.210   11.338  1.00 23.23 ?  88  LEU   A HD12 1 
ATOM   1825 H  HD13 . LEU   A 1 88  ? 22.767 3.968   11.487  1.00 23.23 ?  88  LEU   A HD13 1 
ATOM   1826 H  HD21 . LEU   A 1 88  ? 22.191 5.919   13.520  1.00 24.43 ?  88  LEU   A HD21 1 
ATOM   1827 H  HD22 . LEU   A 1 88  ? 21.679 4.438   13.786  1.00 24.43 ?  88  LEU   A HD22 1 
ATOM   1828 H  HD23 . LEU   A 1 88  ? 22.582 5.173   14.867  1.00 24.43 ?  88  LEU   A HD23 1 
ATOM   1829 N  N    . ALA   A 1 89  ? 25.672 0.991   15.541  1.00 15.77 ?  89  ALA   A N    1 
ATOM   1830 C  CA   . ALA   A 1 89  ? 26.017 -0.420  15.643  1.00 15.68 ?  89  ALA   A CA   1 
ATOM   1831 C  C    . ALA   A 1 89  ? 27.501 -0.484  15.967  1.00 16.25 ?  89  ALA   A C    1 
ATOM   1832 O  O    . ALA   A 1 89  ? 28.217 0.510   15.852  1.00 16.57 ?  89  ALA   A O    1 
ATOM   1833 C  CB   . ALA   A 1 89  ? 25.736 -1.138  14.323  1.00 15.23 ?  89  ALA   A CB   1 
ATOM   1834 H  H    . ALA   A 1 89  ? 26.359 1.508   15.498  1.00 18.91 ?  89  ALA   A H    1 
ATOM   1835 H  HA   . ALA   A 1 89  ? 25.507 -0.837  16.356  1.00 18.80 ?  89  ALA   A HA   1 
ATOM   1836 H  HB1  . ALA   A 1 89  ? 25.986 -2.071  14.414  1.00 18.26 ?  89  ALA   A HB1  1 
ATOM   1837 H  HB2  . ALA   A 1 89  ? 24.788 -1.070  14.119  1.00 18.26 ?  89  ALA   A HB2  1 
ATOM   1838 H  HB3  . ALA   A 1 89  ? 26.256 -0.723  13.620  1.00 18.26 ?  89  ALA   A HB3  1 
ATOM   1839 N  N    . LYS   A 1 90  ? 27.971 -1.661  16.366  1.00 17.08 ?  90  LYS   A N    1 
ATOM   1840 C  CA   . LYS   A 1 90  ? 29.413 -1.821  16.517  1.00 17.73 ?  90  LYS   A CA   1 
ATOM   1841 C  C    . LYS   A 1 90  ? 30.116 -1.636  15.175  1.00 16.42 ?  90  LYS   A C    1 
ATOM   1842 O  O    . LYS   A 1 90  ? 31.051 -0.828  15.049  1.00 17.41 ?  90  LYS   A O    1 
ATOM   1843 C  CB   . LYS   A 1 90  ? 29.739 -3.183  17.128  1.00 20.69 ?  90  LYS   A CB   1 
ATOM   1844 C  CG   . LYS   A 1 90  ? 31.221 -3.354  17.440  1.00 25.82 ?  90  LYS   A CG   1 
ATOM   1845 C  CD   . LYS   A 1 90  ? 31.468 -4.552  18.343  1.00 31.21 ?  90  LYS   A CD   1 
ATOM   1846 C  CE   . LYS   A 1 90  ? 32.882 -4.549  18.910  1.00 35.39 ?  90  LYS   A CE   1 
ATOM   1847 N  NZ   . LYS   A 1 90  ? 33.908 -4.955  17.910  1.00 37.56 ?  90  LYS   A NZ   1 
ATOM   1848 H  H    . LYS   A 1 90  ? 27.492 -2.348  16.554  1.00 20.48 ?  90  LYS   A H    1 
ATOM   1849 H  HA   . LYS   A 1 90  ? 29.740 -1.137  17.118  1.00 21.26 ?  90  LYS   A HA   1 
ATOM   1850 H  HB2  . LYS   A 1 90  ? 29.242 -3.282  17.959  1.00 24.81 ?  90  LYS   A HB2  1 
ATOM   1851 H  HB3  . LYS   A 1 90  ? 29.478 -3.880  16.506  1.00 24.81 ?  90  LYS   A HB3  1 
ATOM   1852 H  HG2  . LYS   A 1 90  ? 31.707 -3.489  16.612  1.00 30.97 ?  90  LYS   A HG2  1 
ATOM   1853 H  HG3  . LYS   A 1 90  ? 31.544 -2.559  17.892  1.00 30.97 ?  90  LYS   A HG3  1 
ATOM   1854 H  HD2  . LYS   A 1 90  ? 30.843 -4.527  19.086  1.00 37.44 ?  90  LYS   A HD2  1 
ATOM   1855 H  HD3  . LYS   A 1 90  ? 31.347 -5.368  17.832  1.00 37.44 ?  90  LYS   A HD3  1 
ATOM   1856 H  HE2  . LYS   A 1 90  ? 33.100 -3.654  19.214  1.00 42.46 ?  90  LYS   A HE2  1 
ATOM   1857 H  HE3  . LYS   A 1 90  ? 32.926 -5.171  19.653  1.00 42.46 ?  90  LYS   A HE3  1 
ATOM   1858 H  HZ1  . LYS   A 1 90  ? 33.736 -5.777  17.615  1.00 45.05 ?  90  LYS   A HZ1  1 
ATOM   1859 H  HZ2  . LYS   A 1 90  ? 33.903 -4.392  17.222  1.00 45.05 ?  90  LYS   A HZ2  1 
ATOM   1860 H  HZ3  . LYS   A 1 90  ? 34.717 -4.948  18.284  1.00 45.05 ?  90  LYS   A HZ3  1 
ATOM   1861 N  N    . HIS   A 1 91  ? 29.649 -2.354  14.154  1.00 14.61 ?  91  HIS   A N    1 
ATOM   1862 C  CA   . HIS   A 1 91  ? 30.231 -2.342  12.825  1.00 13.92 ?  91  HIS   A CA   1 
ATOM   1863 C  C    . HIS   A 1 91  ? 29.151 -2.061  11.796  1.00 12.99 ?  91  HIS   A C    1 
ATOM   1864 O  O    . HIS   A 1 91  ? 27.984 -2.413  11.988  1.00 13.62 ?  91  HIS   A O    1 
ATOM   1865 C  CB   . HIS   A 1 91  ? 30.823 -3.710  12.470  1.00 16.24 ?  91  HIS   A CB   1 
ATOM   1866 C  CG   . HIS   A 1 91  ? 31.827 -4.215  13.455  1.00 20.37 ?  91  HIS   A CG   1 
ATOM   1867 N  ND1  . HIS   A 1 91  ? 33.109 -3.716  13.532  1.00 22.32 ?  91  HIS   A ND1  1 
ATOM   1868 C  CD2  . HIS   A 1 91  ? 31.744 -5.186  14.395  1.00 22.13 ?  91  HIS   A CD2  1 
ATOM   1869 C  CE1  . HIS   A 1 91  ? 33.772 -4.353  14.481  1.00 23.23 ?  91  HIS   A CE1  1 
ATOM   1870 N  NE2  . HIS   A 1 91  ? 32.966 -5.252  15.020  1.00 23.23 ?  91  HIS   A NE2  1 
ATOM   1871 H  H    . HIS   A 1 91  ? 28.959 -2.885  14.217  1.00 17.52 ?  91  HIS   A H    1 
ATOM   1872 H  HA   . HIS   A 1 91  ? 30.920 -1.670  12.766  1.00 16.68 ?  91  HIS   A HA   1 
ATOM   1873 H  HB2  . HIS   A 1 91  ? 30.106 -4.364  12.424  1.00 19.48 ?  91  HIS   A HB2  1 
ATOM   1874 H  HB3  . HIS   A 1 91  ? 31.262 -3.647  11.607  1.00 19.48 ?  91  HIS   A HB3  1 
ATOM   1875 H  HD1  . HIS   A 1 91  ? 33.429 -3.088  13.036  1.00 26.77 ?  91  HIS   A HD1  1 
ATOM   1876 H  HD2  . HIS   A 1 91  ? 31.005 -5.709  14.588  1.00 26.54 ?  91  HIS   A HD2  1 
ATOM   1877 H  HE1  . HIS   A 1 91  ? 34.659 -4.192  14.725  1.00 27.86 ?  91  HIS   A HE1  1 
ATOM   1878 N  N    . CYS   A 1 92  ? 29.559 -1.464  10.682  1.00 12.51 ?  92  CYS   A N    1 
ATOM   1879 C  CA   . CYS   A 1 92  ? 28.731 -1.389  9.487   1.00 12.29 ?  92  CYS   A CA   1 
ATOM   1880 C  C    . CYS   A 1 92  ? 29.378 -2.210  8.382   1.00 11.87 ?  92  CYS   A C    1 
ATOM   1881 O  O    . CYS   A 1 92  ? 30.536 -1.961  8.010   1.00 12.37 ?  92  CYS   A O    1 
ATOM   1882 C  CB   . CYS   A 1 92  ? 28.521 0.050   9.022   1.00 12.47 ?  92  CYS   A CB   1 
ATOM   1883 S  SG   . CYS   A 1 92  ? 27.499 0.161   7.513   1.00 11.71 ?  92  CYS   A SG   1 
ATOM   1884 H  H    . CYS   A 1 92  ? 30.331 -1.088  10.596  1.00 14.99 ?  92  CYS   A H    1 
ATOM   1885 H  HA   . CYS   A 1 92  ? 27.864 -1.771  9.681   1.00 14.73 ?  92  CYS   A HA   1 
ATOM   1886 H  HB2  . CYS   A 1 92  ? 28.074 0.551   9.726   1.00 14.95 ?  92  CYS   A HB2  1 
ATOM   1887 H  HB3  . CYS   A 1 92  ? 29.382 0.452   8.828   1.00 14.95 ?  92  CYS   A HB3  1 
ATOM   1888 H  HG   . CYS   A 1 92  ? 27.361 1.315   7.223   1.00 14.04 ?  92  CYS   A HG   1 
ATOM   1889 N  N    . LEU   A 1 93  ? 28.637 -3.192  7.879   1.00 11.49 ?  93  LEU   A N    1 
ATOM   1890 C  CA   . LEU   A 1 93  ? 29.040 -3.952  6.702   1.00 11.16 ?  93  LEU   A CA   1 
ATOM   1891 C  C    . LEU   A 1 93  ? 28.448 -3.264  5.477   1.00 10.97 ?  93  LEU   A C    1 
ATOM   1892 O  O    . LEU   A 1 93  ? 27.234 -3.320  5.251   1.00 11.10 ?  93  LEU   A O    1 
ATOM   1893 C  CB   . LEU   A 1 93  ? 28.565 -5.399  6.810   1.00 11.70 ?  93  LEU   A CB   1 
ATOM   1894 C  CG   . LEU   A 1 93  ? 28.951 -6.296  5.634   1.00 12.07 ?  93  LEU   A CG   1 
ATOM   1895 C  CD1  . LEU   A 1 93  ? 30.449 -6.566  5.620   1.00 13.04 ?  93  LEU   A CD1  1 
ATOM   1896 C  CD2  . LEU   A 1 93  ? 28.174 -7.614  5.676   1.00 13.13 ?  93  LEU   A CD2  1 
ATOM   1897 H  H    . LEU   A 1 93  ? 27.882 -3.440  8.215   1.00 13.77 ?  93  LEU   A H    1 
ATOM   1898 H  HA   . LEU   A 1 93  ? 30.003 -3.938  6.627   1.00 13.38 ?  93  LEU   A HA   1 
ATOM   1899 H  HB2  . LEU   A 1 93  ? 28.953 -5.786  7.613   1.00 14.02 ?  93  LEU   A HB2  1 
ATOM   1900 H  HB3  . LEU   A 1 93  ? 27.601 -5.405  6.879   1.00 14.02 ?  93  LEU   A HB3  1 
ATOM   1901 H  HG   . LEU   A 1 93  ? 28.729 -5.849  4.807   1.00 14.47 ?  93  LEU   A HG   1 
ATOM   1902 H  HD11 . LEU   A 1 93  ? 30.657 -7.173  4.892   1.00 15.63 ?  93  LEU   A HD11 1 
ATOM   1903 H  HD12 . LEU   A 1 93  ? 30.924 -5.731  5.502   1.00 15.63 ?  93  LEU   A HD12 1 
ATOM   1904 H  HD13 . LEU   A 1 93  ? 30.707 -6.975  6.467   1.00 15.63 ?  93  LEU   A HD13 1 
ATOM   1905 H  HD21 . LEU   A 1 93  ? 28.439 -8.163  4.919   1.00 15.74 ?  93  LEU   A HD21 1 
ATOM   1906 H  HD22 . LEU   A 1 93  ? 28.372 -8.077  6.504   1.00 15.74 ?  93  LEU   A HD22 1 
ATOM   1907 H  HD23 . LEU   A 1 93  ? 27.223 -7.421  5.623   1.00 15.74 ?  93  LEU   A HD23 1 
ATOM   1908 N  N    . HIS   A 1 94  ? 29.298 -2.574  4.717   1.00 10.62 ?  94  HIS   A N    1 
ATOM   1909 C  CA   . HIS   A 1 94  ? 28.872 -1.902  3.493   1.00 10.80 ?  94  HIS   A CA   1 
ATOM   1910 C  C    . HIS   A 1 94  ? 28.884 -2.935  2.381   1.00 10.71 ?  94  HIS   A C    1 
ATOM   1911 O  O    . HIS   A 1 94  ? 29.948 -3.447  2.034   1.00 12.34 ?  94  HIS   A O    1 
ATOM   1912 C  CB   . HIS   A 1 94  ? 29.824 -0.753  3.159   1.00 10.73 ?  94  HIS   A CB   1 
ATOM   1913 C  CG   . HIS   A 1 94  ? 29.814 0.340   4.173   1.00 10.56 ?  94  HIS   A CG   1 
ATOM   1914 N  ND1  . HIS   A 1 94  ? 28.936 1.404   4.119   1.00 10.67 ?  94  HIS   A ND1  1 
ATOM   1915 C  CD2  . HIS   A 1 94  ? 30.556 0.513   5.288   1.00 11.27 ?  94  HIS   A CD2  1 
ATOM   1916 C  CE1  . HIS   A 1 94  ? 29.150 2.185   5.162   1.00 10.94 ?  94  HIS   A CE1  1 
ATOM   1917 N  NE2  . HIS   A 1 94  ? 30.131 1.671   5.883   1.00 11.10 ?  94  HIS   A NE2  1 
ATOM   1918 H  H    . HIS   A 1 94  ? 30.134 -2.478  4.887   1.00 12.72 ?  94  HIS   A H    1 
ATOM   1919 H  HA   . HIS   A 1 94  ? 27.967 -1.553  3.595   1.00 12.95 ?  94  HIS   A HA   1 
ATOM   1920 H  HB2  . HIS   A 1 94  ? 30.720 -1.095  3.103   1.00 12.85 ?  94  HIS   A HB2  1 
ATOM   1921 H  HB3  . HIS   A 1 94  ? 29.556 -0.365  2.308   1.00 12.85 ?  94  HIS   A HB3  1 
ATOM   1922 H  HD2  . HIS   A 1 94  ? 31.232 -0.038  5.591   1.00 13.51 ?  94  HIS   A HD2  1 
ATOM   1923 H  HE1  . HIS   A 1 94  ? 28.684 2.975   5.350   1.00 13.11 ?  94  HIS   A HE1  1 
ATOM   1924 H  HE2  . HIS   A 1 94  ? 30.445 2.018   6.604   1.00 13.31 ?  94  HIS   A HE2  1 
ATOM   1925 N  N    . VAL   A 1 95  ? 27.714 -3.259  1.832   1.00 10.20 ?  95  VAL   A N    1 
ATOM   1926 C  CA   . VAL   A 1 95  ? 27.571 -4.294  0.813   1.00 10.46 ?  95  VAL   A CA   1 
ATOM   1927 C  C    . VAL   A 1 95  ? 27.025 -3.653  -0.449  1.00 10.17 ?  95  VAL   A C    1 
ATOM   1928 O  O    . VAL   A 1 95  ? 26.021 -2.931  -0.394  1.00 11.02 ?  95  VAL   A O    1 
ATOM   1929 C  CB   . VAL   A 1 95  ? 26.642 -5.434  1.267   1.00 11.14 ?  95  VAL   A CB   1 
ATOM   1930 C  CG1  . VAL   A 1 95  ? 26.534 -6.480  0.163   1.00 12.11 ?  95  VAL   A CG1  1 
ATOM   1931 C  CG2  . VAL   A 1 95  ? 27.143 -6.051  2.552   1.00 11.50 ?  95  VAL   A CG2  1 
ATOM   1932 H  H    . VAL   A 1 95  ? 26.963 -2.896  2.052   1.00 12.22 ?  95  VAL   A H    1 
ATOM   1933 H  HA   . VAL   A 1 95  ? 28.438 -4.670  0.610   1.00 12.53 ?  95  VAL   A HA   1 
ATOM   1934 H  HB   . VAL   A 1 95  ? 25.755 -5.078  1.425   1.00 13.35 ?  95  VAL   A HB   1 
ATOM   1935 H  HG11 . VAL   A 1 95  ? 26.133 -7.289  0.529   1.00 14.52 ?  95  VAL   A HG11 1 
ATOM   1936 H  HG12 . VAL   A 1 95  ? 25.977 -6.140  -0.556  1.00 14.52 ?  95  VAL   A HG12 1 
ATOM   1937 H  HG13 . VAL   A 1 95  ? 27.421 -6.685  -0.175  1.00 14.52 ?  95  VAL   A HG13 1 
ATOM   1938 H  HG21 . VAL   A 1 95  ? 26.578 -6.810  2.771   1.00 13.78 ?  95  VAL   A HG21 1 
ATOM   1939 H  HG22 . VAL   A 1 95  ? 28.056 -6.339  2.426   1.00 13.78 ?  95  VAL   A HG22 1 
ATOM   1940 H  HG23 . VAL   A 1 95  ? 27.091 -5.386  3.253   1.00 13.78 ?  95  VAL   A HG23 1 
ATOM   1941 N  N    . VAL   A 1 96  ? 27.655 -3.941  -1.586  1.00 10.27 ?  96  VAL   A N    1 
ATOM   1942 C  CA   . VAL   A 1 96  ? 27.241 -3.392  -2.869  1.00 10.92 ?  96  VAL   A CA   1 
ATOM   1943 C  C    . VAL   A 1 96  ? 26.439 -4.445  -3.625  1.00 11.38 ?  96  VAL   A C    1 
ATOM   1944 O  O    . VAL   A 1 96  ? 27.000 -5.391  -4.187  1.00 12.34 ?  96  VAL   A O    1 
ATOM   1945 C  CB   . VAL   A 1 96  ? 28.435 -2.915  -3.696  1.00 11.50 ?  96  VAL   A CB   1 
ATOM   1946 C  CG1  . VAL   A 1 96  ? 27.935 -2.280  -4.976  1.00 11.30 ?  96  VAL   A CG1  1 
ATOM   1947 C  CG2  . VAL   A 1 96  ? 29.297 -1.943  -2.900  1.00 11.74 ?  96  VAL   A CG2  1 
ATOM   1948 H  H    . VAL   A 1 96  ? 28.341 -4.466  -1.637  1.00 12.31 ?  96  VAL   A H    1 
ATOM   1949 H  HA   . VAL   A 1 96  ? 26.667 -2.629  -2.711  1.00 13.08 ?  96  VAL   A HA   1 
ATOM   1950 H  HB   . VAL   A 1 96  ? 28.986 -3.673  -3.931  1.00 13.78 ?  96  VAL   A HB   1 
ATOM   1951 H  HG11 . VAL   A 1 96  ? 28.668 -1.801  -5.393  1.00 13.54 ?  96  VAL   A HG11 1 
ATOM   1952 H  HG12 . VAL   A 1 96  ? 27.613 -2.974  -5.567  1.00 13.54 ?  96  VAL   A HG12 1 
ATOM   1953 H  HG13 . VAL   A 1 96  ? 27.218 -1.662  -4.761  1.00 13.54 ?  96  VAL   A HG13 1 
ATOM   1954 H  HG21 . VAL   A 1 96  ? 30.000 -1.597  -3.471  1.00 14.07 ?  96  VAL   A HG21 1 
ATOM   1955 H  HG22 . VAL   A 1 96  ? 28.741 -1.209  -2.584  1.00 14.07 ?  96  VAL   A HG22 1 
ATOM   1956 H  HG23 . VAL   A 1 96  ? 29.685 -2.407  -2.141  1.00 14.07 ?  96  VAL   A HG23 1 
ATOM   1957 N  N    A GLY   A 1 97  ? 25.120 -4.291  -3.644  0.64 11.19 ?  97  GLY   A N    1 
ATOM   1958 N  N    B GLY   A 1 97  ? 25.122 -4.278  -3.658  0.36 11.39 ?  97  GLY   A N    1 
ATOM   1959 C  CA   A GLY   A 1 97  ? 24.300 -5.039  -4.560  0.64 12.02 ?  97  GLY   A CA   1 
ATOM   1960 C  CA   B GLY   A 1 97  ? 24.297 -5.041  -4.559  0.36 11.88 ?  97  GLY   A CA   1 
ATOM   1961 C  C    A GLY   A 1 97  ? 24.329 -4.392  -5.929  0.64 12.25 ?  97  GLY   A C    1 
ATOM   1962 C  C    B GLY   A 1 97  ? 24.249 -4.374  -5.919  0.36 12.09 ?  97  GLY   A C    1 
ATOM   1963 O  O    A GLY   A 1 97  ? 24.671 -3.213  -6.070  0.64 12.88 ?  97  GLY   A O    1 
ATOM   1964 O  O    B GLY   A 1 97  ? 24.448 -3.161  -6.042  0.36 12.26 ?  97  GLY   A O    1 
ATOM   1965 H  H    A GLY   A 1 97  ? 24.683 -3.754  -3.128  0.64 13.41 ?  97  GLY   A H    1 
ATOM   1966 H  H    B GLY   A 1 97  ? 24.687 -3.724  -3.159  0.36 13.65 ?  97  GLY   A H    1 
ATOM   1967 H  HA2  A GLY   A 1 97  ? 24.637 -5.943  -4.628  0.64 14.41 ?  97  GLY   A HA2  1 
ATOM   1968 H  HA2  B GLY   A 1 97  ? 24.663 -5.934  -4.648  0.36 14.24 ?  97  GLY   A HA2  1 
ATOM   1969 H  HA3  A GLY   A 1 97  ? 23.385 -5.066  -4.235  0.64 14.41 ?  97  GLY   A HA3  1 
ATOM   1970 H  HA3  B GLY   A 1 97  ? 23.396 -5.101  -4.208  0.36 14.24 ?  97  GLY   A HA3  1 
ATOM   1971 N  N    . PRO   A 1 98  ? 23.978 -5.146  -6.968  1.00 12.32 ?  98  PRO   A N    1 
ATOM   1972 C  CA   . PRO   A 1 98  ? 23.888 -4.552  -8.305  1.00 13.84 ?  98  PRO   A CA   1 
ATOM   1973 C  C    . PRO   A 1 98  ? 22.774 -3.514  -8.384  1.00 14.14 ?  98  PRO   A C    1 
ATOM   1974 O  O    . PRO   A 1 98  ? 21.690 -3.684  -7.817  1.00 13.84 ?  98  PRO   A O    1 
ATOM   1975 C  CB   . PRO   A 1 98  ? 23.599 -5.759  -9.207  1.00 14.30 ?  98  PRO   A CB   1 
ATOM   1976 C  CG   . PRO   A 1 98  ? 22.951 -6.766  -8.295  1.00 14.10 ?  98  PRO   A CG   1 
ATOM   1977 C  CD   . PRO   A 1 98  ? 23.673 -6.588  -6.977  1.00 12.80 ?  98  PRO   A CD   1 
ATOM   1978 H  HA   . PRO   A 1 98  ? 24.737 -4.152  -8.558  1.00 16.59 ?  98  PRO   A HA   1 
ATOM   1979 H  HB2  . PRO   A 1 98  ? 22.990 -5.498  -9.914  1.00 17.15 ?  98  PRO   A HB2  1 
ATOM   1980 H  HB3  . PRO   A 1 98  ? 24.427 -6.106  -9.569  1.00 17.15 ?  98  PRO   A HB3  1 
ATOM   1981 H  HG2  . PRO   A 1 98  ? 22.008 -6.568  -8.199  1.00 16.90 ?  98  PRO   A HG2  1 
ATOM   1982 H  HG3  . PRO   A 1 98  ? 23.087 -7.661  -8.641  1.00 16.90 ?  98  PRO   A HG3  1 
ATOM   1983 H  HD2  . PRO   A 1 98  ? 23.090 -6.819  -6.233  1.00 15.35 ?  98  PRO   A HD2  1 
ATOM   1984 H  HD3  . PRO   A 1 98  ? 24.494 -7.108  -6.957  1.00 15.35 ?  98  PRO   A HD3  1 
ATOM   1985 N  N    A ASN   A 1 99  ? 23.048 -2.394  -9.069  0.64 14.99 ?  99  ASN   A N    1 
ATOM   1986 N  N    B ASN   A 1 99  ? 23.075 -2.451  -9.115  0.36 15.02 ?  99  ASN   A N    1 
ATOM   1987 C  CA   A ASN   A 1 99  ? 22.069 -1.306  -9.231  0.64 15.55 ?  99  ASN   A CA   1 
ATOM   1988 C  CA   B ASN   A 1 99  ? 22.102 -1.448  -9.506  0.36 15.64 ?  99  ASN   A CA   1 
ATOM   1989 C  C    A ASN   A 1 99  ? 21.490 -1.385  -10.642 0.64 16.44 ?  99  ASN   A C    1 
ATOM   1990 C  C    B ASN   A 1 99  ? 21.567 -1.847  -10.877 0.36 15.94 ?  99  ASN   A C    1 
ATOM   1991 O  O    A ASN   A 1 99  ? 22.136 -0.985  -11.616 0.64 16.92 ?  99  ASN   A O    1 
ATOM   1992 O  O    B ASN   A 1 99  ? 22.296 -1.809  -11.876 0.36 15.32 ?  99  ASN   A O    1 
ATOM   1993 C  CB   A ASN   A 1 99  ? 22.680 0.068   -8.948  0.64 15.00 ?  99  ASN   A CB   1 
ATOM   1994 C  CB   B ASN   A 1 99  ? 22.782 -0.085  -9.548  0.36 16.51 ?  99  ASN   A CB   1 
ATOM   1995 C  CG   A ASN   A 1 99  ? 21.636 1.205   -8.950  0.64 14.79 ?  99  ASN   A CG   1 
ATOM   1996 C  CG   B ASN   A 1 99  ? 21.807 1.041   -9.764  0.36 17.29 ?  99  ASN   A CG   1 
ATOM   1997 O  OD1  A ASN   A 1 99  ? 20.649 1.156   -9.685  0.64 15.59 ?  99  ASN   A OD1  1 
ATOM   1998 O  OD1  B ASN   A 1 99  ? 20.862 0.914   -10.538 0.36 17.64 ?  99  ASN   A OD1  1 
ATOM   1999 N  ND2  A ASN   A 1 99  ? 21.873 2.237   -8.135  0.64 15.08 ?  99  ASN   A ND2  1 
ATOM   2000 N  ND2  B ASN   A 1 99  ? 22.024 2.152   -9.068  0.36 17.93 ?  99  ASN   A ND2  1 
ATOM   2001 H  H    A ASN   A 1 99  ? 23.807 -2.233  -9.445  0.64 17.97 ?  99  ASN   A H    1 
ATOM   2002 H  H    B ASN   A 1 99  ? 23.872 -2.281  -9.398  0.36 18.00 ?  99  ASN   A H    1 
ATOM   2003 H  HA   A ASN   A 1 99  ? 21.343 -1.443  -8.603  0.64 18.64 ?  99  ASN   A HA   1 
ATOM   2004 H  HA   B ASN   A 1 99  ? 21.372 -1.428  -8.863  0.36 18.75 ?  99  ASN   A HA   1 
ATOM   2005 H  HB2  A ASN   A 1 99  ? 23.104 0.057   -8.079  0.64 17.98 ?  99  ASN   A HB2  1 
ATOM   2006 H  HB2  B ASN   A 1 99  ? 23.241 0.068   -8.706  0.36 19.79 ?  99  ASN   A HB2  1 
ATOM   2007 H  HB3  A ASN   A 1 99  ? 23.339 0.268   -9.635  0.64 17.98 ?  99  ASN   A HB3  1 
ATOM   2008 H  HB3  B ASN   A 1 99  ? 23.421 -0.077  -10.278 0.36 19.79 ?  99  ASN   A HB3  1 
ATOM   2009 H  HD21 A ASN   A 1 99  ? 21.325 2.903   -8.102  0.64 18.08 ?  99  ASN   A HD21 1 
ATOM   2010 H  HD21 B ASN   A 1 99  ? 21.496 2.824   -9.156  0.36 21.50 ?  99  ASN   A HD21 1 
ATOM   2011 H  HD22 A ASN   A 1 99  ? 22.574 2.239   -7.636  0.64 18.08 ?  99  ASN   A HD22 1 
ATOM   2012 H  HD22 B ASN   A 1 99  ? 22.695 2.199   -8.530  0.36 21.50 ?  99  ASN   A HD22 1 
ATOM   2013 N  N    A VAL   A 1 100 ? 20.256 -1.895  -10.736 0.64 17.06 ?  100 VAL   A N    1 
ATOM   2014 N  N    B VAL   A 1 100 ? 20.297 -2.251  -10.916 0.36 17.03 ?  100 VAL   A N    1 
ATOM   2015 C  CA   A VAL   A 1 100 ? 19.608 -2.106  -12.030 0.64 18.67 ?  100 VAL   A CA   1 
ATOM   2016 C  CA   B VAL   A 1 100 ? 19.686 -2.703  -12.161 0.36 18.24 ?  100 VAL   A CA   1 
ATOM   2017 C  C    A VAL   A 1 100 ? 19.470 -0.797  -12.792 0.64 18.28 ?  100 VAL   A C    1 
ATOM   2018 C  C    B VAL   A 1 100 ? 19.613 -1.574  -13.174 0.36 17.91 ?  100 VAL   A C    1 
ATOM   2019 O  O    A VAL   A 1 100 ? 19.542 -0.777  -14.026 0.64 18.80 ?  100 VAL   A O    1 
ATOM   2020 O  O    B VAL   A 1 100 ? 19.664 -1.812  -14.388 0.36 17.64 ?  100 VAL   A O    1 
ATOM   2021 C  CB   A VAL   A 1 100 ? 18.253 -2.825  -11.840 0.64 20.49 ?  100 VAL   A CB   1 
ATOM   2022 C  CB   B VAL   A 1 100 ? 18.296 -3.293  -11.861 0.36 19.71 ?  100 VAL   A CB   1 
ATOM   2023 C  CG1  A VAL   A 1 100 ? 17.500 -2.942  -13.161 0.64 20.96 ?  100 VAL   A CG1  1 
ATOM   2024 C  CG1  B VAL   A 1 100 ? 17.524 -3.535  -13.147 0.36 20.19 ?  100 VAL   A CG1  1 
ATOM   2025 C  CG2  A VAL   A 1 100 ? 18.470 -4.208  -11.238 0.64 21.15 ?  100 VAL   A CG2  1 
ATOM   2026 C  CG2  B VAL   A 1 100 ? 18.444 -4.573  -11.067 0.36 20.17 ?  100 VAL   A CG2  1 
ATOM   2027 H  H    A VAL   A 1 100 ? 19.771 -2.134  -10.061 0.64 20.46 ?  100 VAL   A H    1 
ATOM   2028 H  H    B VAL   A 1 100 ? 19.774 -2.278  -10.234 0.36 20.42 ?  100 VAL   A H    1 
ATOM   2029 H  HA   A VAL   A 1 100 ? 20.162 -2.695  -12.562 0.64 22.39 ?  100 VAL   A HA   1 
ATOM   2030 H  HA   B VAL   A 1 100 ? 20.234 -3.404  -12.541 0.36 21.87 ?  100 VAL   A HA   1 
ATOM   2031 H  HB   A VAL   A 1 100 ? 17.698 -2.321  -11.227 0.64 24.58 ?  100 VAL   A HB   1 
ATOM   2032 H  HB   B VAL   A 1 100 ? 17.796 -2.655  -11.326 0.36 23.64 ?  100 VAL   A HB   1 
ATOM   2033 H  HG11 A VAL   A 1 100 ? 16.768 -3.575  -13.056 0.64 25.14 ?  100 VAL   A HG11 1 
ATOM   2034 H  HG11 B VAL   A 1 100 ? 16.772 -4.114  -12.951 0.36 24.21 ?  100 VAL   A HG11 1 
ATOM   2035 H  HG12 A VAL   A 1 100 ? 17.149 -2.074  -13.406 0.64 25.14 ?  100 VAL   A HG12 1 
ATOM   2036 H  HG12 B VAL   A 1 100 ? 17.204 -2.686  -13.493 0.36 24.21 ?  100 VAL   A HG12 1 
ATOM   2037 H  HG13 A VAL   A 1 100 ? 18.109 -3.263  -13.845 0.64 25.14 ?  100 VAL   A HG13 1 
ATOM   2038 H  HG13 B VAL   A 1 100 ? 18.110 -3.958  -13.792 0.36 24.21 ?  100 VAL   A HG13 1 
ATOM   2039 H  HG21 A VAL   A 1 100 ? 17.614 -4.663  -11.158 0.64 25.36 ?  100 VAL   A HG21 1 
ATOM   2040 H  HG21 B VAL   A 1 100 ? 17.567 -4.954  -10.926 0.36 24.18 ?  100 VAL   A HG21 1 
ATOM   2041 H  HG22 A VAL   A 1 100 ? 19.058 -4.719  -11.819 0.64 25.36 ?  100 VAL   A HG22 1 
ATOM   2042 H  HG22 B VAL   A 1 100 ? 19.001 -5.188  -11.569 0.36 24.18 ?  100 VAL   A HG22 1 
ATOM   2043 H  HG23 A VAL   A 1 100 ? 18.874 -4.113  -10.362 0.64 25.36 ?  100 VAL   A HG23 1 
ATOM   2044 H  HG23 B VAL   A 1 100 ? 18.862 -4.366  -10.216 0.36 24.18 ?  100 VAL   A HG23 1 
ATOM   2045 N  N    A ASN   A 1 101 ? 19.267 0.311   -12.086 0.64 19.16 ?  101 ASN   A N    1 
ATOM   2046 N  N    B ASN   A 1 101 ? 19.479 -0.333  -12.702 0.36 18.15 ?  101 ASN   A N    1 
ATOM   2047 C  CA   A ASN   A 1 101 ? 19.194 1.597   -12.764 0.64 20.17 ?  101 ASN   A CA   1 
ATOM   2048 C  CA   B ASN   A 1 101 ? 19.388 0.808   -13.604 0.36 19.01 ?  101 ASN   A CA   1 
ATOM   2049 C  C    A ASN   A 1 101 ? 20.549 2.055   -13.310 0.64 22.39 ?  101 ASN   A C    1 
ATOM   2050 C  C    B ASN   A 1 101 ? 20.688 1.056   -14.357 0.36 20.19 ?  101 ASN   A C    1 
ATOM   2051 O  O    A ASN   A 1 101 ? 20.613 3.127   -13.925 0.64 24.17 ?  101 ASN   A O    1 
ATOM   2052 O  O    B ASN   A 1 101 ? 20.658 1.672   -15.427 0.36 20.38 ?  101 ASN   A O    1 
ATOM   2053 C  CB   A ASN   A 1 101 ? 18.558 2.634   -11.835 0.64 19.62 ?  101 ASN   A CB   1 
ATOM   2054 C  CB   B ASN   A 1 101 ? 18.979 2.057   -12.819 0.36 18.78 ?  101 ASN   A CB   1 
ATOM   2055 C  CG   A ASN   A 1 101 ? 17.163 2.215   -11.366 0.64 19.14 ?  101 ASN   A CG   1 
ATOM   2056 C  CG   B ASN   A 1 101 ? 17.773 1.811   -11.928 0.36 19.18 ?  101 ASN   A CG   1 
ATOM   2057 O  OD1  A ASN   A 1 101 ? 16.349 1.734   -12.155 0.64 19.44 ?  101 ASN   A OD1  1 
ATOM   2058 O  OD1  B ASN   A 1 101 ? 16.780 1.216   -12.352 0.36 19.89 ?  101 ASN   A OD1  1 
ATOM   2059 N  ND2  A ASN   A 1 101 ? 16.893 2.377   -10.078 0.64 19.21 ?  101 ASN   A ND2  1 
ATOM   2060 N  ND2  B ASN   A 1 101 ? 17.861 2.251   -10.680 0.36 19.24 ?  101 ASN   A ND2  1 
ATOM   2061 H  H    A ASN   A 1 101 ? 19.163 0.342   -11.235 0.64 22.98 ?  101 ASN   A H    1 
ATOM   2062 H  H    B ASN   A 1 101 ? 19.430 -0.121  -11.867 0.36 21.77 ?  101 ASN   A H    1 
ATOM   2063 H  HA   A ASN   A 1 101 ? 18.604 1.499   -13.526 0.64 24.19 ?  101 ASN   A HA   1 
ATOM   2064 H  HA   B ASN   A 1 101 ? 18.699 0.638   -14.260 0.36 22.80 ?  101 ASN   A HA   1 
ATOM   2065 H  HB2  A ASN   A 1 101 ? 19.119 2.750   -11.056 0.64 23.53 ?  101 ASN   A HB2  1 
ATOM   2066 H  HB2  B ASN   A 1 101 ? 19.716 2.342   -12.256 0.36 22.52 ?  101 ASN   A HB2  1 
ATOM   2067 H  HB3  A ASN   A 1 101 ? 18.479 3.478   -12.316 0.64 23.53 ?  101 ASN   A HB3  1 
ATOM   2068 H  HB3  B ASN   A 1 101 ? 18.751 2.769   -13.445 0.36 22.52 ?  101 ASN   A HB3  1 
ATOM   2069 H  HD21 A ASN   A 1 101 ? 16.121 2.156   -9.772  0.64 23.03 ?  101 ASN   A HD21 1 
ATOM   2070 H  HD21 B ASN   A 1 101 ? 17.205 2.136   -10.139 0.36 23.07 ?  101 ASN   A HD21 1 
ATOM   2071 H  HD22 A ASN   A 1 101 ? 17.486 2.711   -9.554  0.64 23.03 ?  101 ASN   A HD22 1 
ATOM   2072 H  HD22 B ASN   A 1 101 ? 18.571 2.659   -10.417 0.36 23.07 ?  101 ASN   A HD22 1 
ATOM   2073 N  N    A LYS   A 1 102 ? 21.610 1.259   -13.118 0.64 24.25 ?  102 LYS   A N    1 
ATOM   2074 N  N    B LYS   A 1 102 ? 21.819 0.598   -13.826 0.36 21.36 ?  102 LYS   A N    1 
ATOM   2075 C  CA   A LYS   A 1 102 ? 22.905 1.461   -13.759 0.64 25.86 ?  102 LYS   A CA   1 
ATOM   2076 C  CA   B LYS   A 1 102 ? 23.107 0.705   -14.497 0.36 22.22 ?  102 LYS   A CA   1 
ATOM   2077 C  C    A LYS   A 1 102 ? 23.238 0.382   -14.781 0.64 26.84 ?  102 LYS   A C    1 
ATOM   2078 C  C    B LYS   A 1 102 ? 23.435 -0.532  -15.326 0.36 21.74 ?  102 LYS   A C    1 
ATOM   2079 O  O    A LYS   A 1 102 ? 24.325 0.425   -15.367 0.64 27.17 ?  102 LYS   A O    1 
ATOM   2080 O  O    B LYS   A 1 102 ? 24.572 -0.670  -15.789 0.36 21.60 ?  102 LYS   A O    1 
ATOM   2081 C  CB   A LYS   A 1 102 ? 24.025 1.498   -12.711 0.64 27.28 ?  102 LYS   A CB   1 
ATOM   2082 C  CB   B LYS   A 1 102 ? 24.224 0.937   -13.476 0.36 23.84 ?  102 LYS   A CB   1 
ATOM   2083 C  CG   A LYS   A 1 102 ? 23.931 2.633   -11.716 0.64 28.50 ?  102 LYS   A CG   1 
ATOM   2084 C  CG   B LYS   A 1 102 ? 24.029 2.149   -12.583 0.36 25.42 ?  102 LYS   A CG   1 
ATOM   2085 C  CD   A LYS   A 1 102 ? 25.100 2.584   -10.742 0.64 30.01 ?  102 LYS   A CD   1 
ATOM   2086 C  CD   B LYS   A 1 102 ? 25.101 2.205   -11.505 0.36 27.17 ?  102 LYS   A CD   1 
ATOM   2087 C  CE   A LYS   A 1 102 ? 25.051 3.730   -9.746  0.64 31.23 ?  102 LYS   A CE   1 
ATOM   2088 C  CE   B LYS   A 1 102 ? 24.793 3.272   -10.468 0.36 28.47 ?  102 LYS   A CE   1 
ATOM   2089 N  NZ   A LYS   A 1 102 ? 26.143 3.625   -8.735  0.64 31.86 ?  102 LYS   A NZ   1 
ATOM   2090 N  NZ   B LYS   A 1 102 ? 25.255 2.864   -9.111  0.36 29.38 ?  102 LYS   A NZ   1 
ATOM   2091 H  H    A LYS   A 1 102 ? 21.601 0.564   -12.606 0.64 29.08 ?  102 LYS   A H    1 
ATOM   2092 H  H    B LYS   A 1 102 ? 21.864 0.219   -13.059 0.36 25.61 ?  102 LYS   A H    1 
ATOM   2093 H  HA   A LYS   A 1 102 ? 22.904 2.303   -14.227 0.64 31.01 ?  102 LYS   A HA   1 
ATOM   2094 H  HA   B LYS   A 1 102 ? 23.093 1.475   -15.083 0.36 26.64 ?  102 LYS   A HA   1 
ATOM   2095 H  HB2  A LYS   A 1 102 ? 24.007 0.666   -12.211 0.64 32.72 ?  102 LYS   A HB2  1 
ATOM   2096 H  HB2  B LYS   A 1 102 ? 24.280 0.163   -12.900 0.36 28.59 ?  102 LYS   A HB2  1 
ATOM   2097 H  HB3  A LYS   A 1 102 ? 24.876 1.579   -13.172 0.64 32.72 ?  102 LYS   A HB3  1 
ATOM   2098 H  HB3  B LYS   A 1 102 ? 25.064 1.052   -13.953 0.36 28.59 ?  102 LYS   A HB3  1 
ATOM   2099 H  HG2  A LYS   A 1 102 ? 23.959 3.479   -12.191 0.64 34.18 ?  102 LYS   A HG2  1 
ATOM   2100 H  HG2  B LYS   A 1 102 ? 24.088 2.958   -13.115 0.36 30.49 ?  102 LYS   A HG2  1 
ATOM   2101 H  HG3  A LYS   A 1 102 ? 23.105 2.553   -11.214 0.64 34.18 ?  102 LYS   A HG3  1 
ATOM   2102 H  HG3  B LYS   A 1 102 ? 23.163 2.093   -12.149 0.36 30.49 ?  102 LYS   A HG3  1 
ATOM   2103 H  HD2  A LYS   A 1 102 ? 25.068 1.749   -10.249 0.64 35.99 ?  102 LYS   A HD2  1 
ATOM   2104 H  HD2  B LYS   A 1 102 ? 25.149 1.347   -11.055 0.36 32.59 ?  102 LYS   A HD2  1 
ATOM   2105 H  HD3  A LYS   A 1 102 ? 25.932 2.646   -11.239 0.64 35.99 ?  102 LYS   A HD3  1 
ATOM   2106 H  HD3  B LYS   A 1 102 ? 25.956 2.417   -11.915 0.36 32.59 ?  102 LYS   A HD3  1 
ATOM   2107 H  HE2  A LYS   A 1 102 ? 25.155 4.570   -10.222 0.64 37.46 ?  102 LYS   A HE2  1 
ATOM   2108 H  HE2  B LYS   A 1 102 ? 25.250 4.093   -10.710 0.36 34.15 ?  102 LYS   A HE2  1 
ATOM   2109 H  HE3  A LYS   A 1 102 ? 24.200 3.712   -9.281  0.64 37.46 ?  102 LYS   A HE3  1 
ATOM   2110 H  HE3  B LYS   A 1 102 ? 23.835 3.420   -10.434 0.36 34.15 ?  102 LYS   A HE3  1 
ATOM   2111 H  HZ1  A LYS   A 1 102 ? 26.095 4.304   -8.164  0.64 38.22 ?  102 LYS   A HZ1  1 
ATOM   2112 H  HZ1  B LYS   A 1 102 ? 25.065 3.501   -8.520  0.36 35.24 ?  102 LYS   A HZ1  1 
ATOM   2113 H  HZ2  A LYS   A 1 102 ? 26.066 2.861   -8.285  0.64 38.22 ?  102 LYS   A HZ2  1 
ATOM   2114 H  HZ2  B LYS   A 1 102 ? 24.848 2.110   -8.865  0.36 35.24 ?  102 LYS   A HZ2  1 
ATOM   2115 H  HZ3  A LYS   A 1 102 ? 26.935 3.642   -9.141  0.64 38.22 ?  102 LYS   A HZ3  1 
ATOM   2116 H  HZ3  B LYS   A 1 102 ? 26.135 2.728   -9.117  0.36 35.24 ?  102 LYS   A HZ3  1 
ATOM   2117 N  N    A GLY   A 1 103 ? 22.349 -0.585  -15.004 0.64 27.96 ?  103 GLY   A N    1 
ATOM   2118 N  N    B GLY   A 1 103 ? 22.480 -1.443  -15.505 0.36 21.45 ?  103 GLY   A N    1 
ATOM   2119 C  CA   A GLY   A 1 103 ? 22.622 -1.666  -15.930 0.64 28.72 ?  103 GLY   A CA   1 
ATOM   2120 C  CA   B GLY   A 1 103 ? 22.737 -2.644  -16.273 0.36 21.25 ?  103 GLY   A CA   1 
ATOM   2121 C  C    A GLY   A 1 103 ? 23.505 -2.761  -15.381 0.64 29.14 ?  103 GLY   A C    1 
ATOM   2122 C  C    B GLY   A 1 103 ? 23.572 -3.685  -15.566 0.36 20.51 ?  103 GLY   A C    1 
ATOM   2123 O  O    A GLY   A 1 103 ? 24.162 -3.457  -16.161 0.64 29.86 ?  103 GLY   A O    1 
ATOM   2124 O  O    B GLY   A 1 103 ? 24.027 -4.634  -16.211 0.36 20.71 ?  103 GLY   A O    1 
ATOM   2125 H  H    A GLY   A 1 103 ? 21.582 -0.643  -14.627 0.64 33.54 ?  103 GLY   A H    1 
ATOM   2126 H  H    B GLY   A 1 103 ? 21.681 -1.385  -15.187 0.36 25.72 ?  103 GLY   A H    1 
ATOM   2127 H  HA2  A GLY   A 1 103 ? 21.779 -2.056  -16.233 0.64 34.45 ?  103 GLY   A HA2  1 
ATOM   2128 H  HA2  B GLY   A 1 103 ? 21.894 -3.051  -16.517 0.36 25.48 ?  103 GLY   A HA2  1 
ATOM   2129 H  HA3  A GLY   A 1 103 ? 23.079 -1.314  -16.706 0.64 34.45 ?  103 GLY   A HA3  1 
ATOM   2130 H  HA3  B GLY   A 1 103 ? 23.199 -2.396  -17.091 0.36 25.48 ?  103 GLY   A HA3  1 
ATOM   2131 N  N    A GLU   A 1 104 ? 23.555 -2.931  -14.063 0.64 28.17 ?  104 GLU   A N    1 
ATOM   2132 N  N    B GLU   A 1 104 ? 23.783 -3.540  -14.261 0.36 19.48 ?  104 GLU   A N    1 
ATOM   2133 C  CA   A GLU   A 1 104 ? 24.422 -3.923  -13.446 0.64 27.20 ?  104 GLU   A CA   1 
ATOM   2134 C  CA   B GLU   A 1 104 ? 24.658 -4.453  -13.540 0.36 18.34 ?  104 GLU   A CA   1 
ATOM   2135 C  C    A GLU   A 1 104 ? 23.734 -5.284  -13.358 0.64 27.51 ?  104 GLU   A C    1 
ATOM   2136 C  C    B GLU   A 1 104 ? 23.982 -5.812  -13.364 0.36 18.46 ?  104 GLU   A C    1 
ATOM   2137 O  O    A GLU   A 1 104 ? 22.509 -5.383  -13.240 0.64 27.39 ?  104 GLU   A O    1 
ATOM   2138 O  O    B GLU   A 1 104 ? 22.780 -5.902  -13.098 0.36 18.41 ?  104 GLU   A O    1 
ATOM   2139 C  CB   A GLU   A 1 104 ? 24.891 -3.434  -12.071 0.64 25.86 ?  104 GLU   A CB   1 
ATOM   2140 C  CB   B GLU   A 1 104 ? 25.054 -3.835  -12.195 0.36 17.96 ?  104 GLU   A CB   1 
ATOM   2141 C  CG   A GLU   A 1 104 ? 25.909 -2.288  -12.199 0.64 24.86 ?  104 GLU   A CG   1 
ATOM   2142 C  CG   B GLU   A 1 104 ? 25.563 -2.395  -12.338 0.36 18.34 ?  104 GLU   A CG   1 
ATOM   2143 C  CD   A GLU   A 1 104 ? 26.141 -1.473  -10.930 0.64 23.91 ?  104 GLU   A CD   1 
ATOM   2144 C  CD   B GLU   A 1 104 ? 26.208 -1.823  -11.082 0.36 17.94 ?  104 GLU   A CD   1 
ATOM   2145 O  OE1  A GLU   A 1 104 ? 25.528 -1.770  -9.887  0.64 22.54 ?  104 GLU   A OE1  1 
ATOM   2146 O  OE1  B GLU   A 1 104 ? 25.781 -2.162  -9.959  0.36 17.32 ?  104 GLU   A OE1  1 
ATOM   2147 O  OE2  A GLU   A 1 104 ? 26.941 -0.509  -10.994 0.64 24.37 -1 104 GLU   A OE2  1 
ATOM   2148 O  OE2  B GLU   A 1 104 ? 27.148 -1.008  -11.230 0.36 18.35 -1 104 GLU   A OE2  1 
ATOM   2149 H  H    A GLU   A 1 104 ? 23.100 -2.468  -13.499 0.64 33.78 ?  104 GLU   A H    1 
ATOM   2150 H  H    B GLU   A 1 104 ? 23.431 -2.920  -13.777 0.36 23.36 ?  104 GLU   A H    1 
ATOM   2151 H  HA   A GLU   A 1 104 ? 25.203 -4.035  -14.004 0.64 32.63 ?  104 GLU   A HA   1 
ATOM   2152 H  HA   B GLU   A 1 104 ? 25.470 -4.581  -14.057 0.36 21.99 ?  104 GLU   A HA   1 
ATOM   2153 H  HB2  A GLU   A 1 104 ? 24.123 -3.115  -11.573 0.64 31.01 ?  104 GLU   A HB2  1 
ATOM   2154 H  HB2  B GLU   A 1 104 ? 24.281 -3.820  -11.613 0.36 21.53 ?  104 GLU   A HB2  1 
ATOM   2155 H  HB3  A GLU   A 1 104 ? 25.312 -4.173  -11.602 0.64 31.01 ?  104 GLU   A HB3  1 
ATOM   2156 H  HB3  B GLU   A 1 104 ? 25.764 -4.361  -11.801 0.36 21.53 ?  104 GLU   A HB3  1 
ATOM   2157 H  HG2  A GLU   A 1 104 ? 26.753 -2.666  -12.480 0.64 29.81 ?  104 GLU   A HG2  1 
ATOM   2158 H  HG2  B GLU   A 1 104 ? 26.227 -2.360  -13.044 0.36 22.00 ?  104 GLU   A HG2  1 
ATOM   2159 H  HG3  A GLU   A 1 104 ? 25.582 -1.669  -12.866 0.64 29.81 ?  104 GLU   A HG3  1 
ATOM   2160 H  HG3  B GLU   A 1 104 ? 24.811 -1.827  -12.568 0.36 22.00 ?  104 GLU   A HG3  1 
ATOM   2161 N  N    A ASP   A 1 105 ? 24.549 -6.338  -13.430 0.64 28.21 ?  105 ASP   A N    1 
ATOM   2162 N  N    B ASP   A 1 105 ? 24.774 -6.869  -13.537 0.36 19.42 ?  105 ASP   A N    1 
ATOM   2163 C  CA   A ASP   A 1 105 ? 24.054 -7.703  -13.569 0.64 29.04 ?  105 ASP   A CA   1 
ATOM   2164 C  CA   B ASP   A 1 105 ? 24.276 -8.241  -13.573 0.36 20.48 ?  105 ASP   A CA   1 
ATOM   2165 C  C    A ASP   A 1 105 ? 23.378 -8.156  -12.278 0.64 27.19 ?  105 ASP   A C    1 
ATOM   2166 C  C    B ASP   A 1 105 ? 23.537 -8.596  -12.289 0.36 19.87 ?  105 ASP   A C    1 
ATOM   2167 O  O    A ASP   A 1 105 ? 23.997 -8.151  -11.209 0.64 26.03 ?  105 ASP   A O    1 
ATOM   2168 O  O    B ASP   A 1 105 ? 24.124 -8.605  -11.204 0.36 18.15 ?  105 ASP   A O    1 
ATOM   2169 C  CB   A ASP   A 1 105 ? 25.224 -8.625  -13.911 0.64 31.63 ?  105 ASP   A CB   1 
ATOM   2170 C  CB   B ASP   A 1 105 ? 25.473 -9.174  -13.766 0.36 22.33 ?  105 ASP   A CB   1 
ATOM   2171 C  CG   A ASP   A 1 105 ? 24.783 -10.041 -14.201 0.64 33.83 ?  105 ASP   A CG   1 
ATOM   2172 C  CG   B ASP   A 1 105 ? 25.086 -10.640 -13.811 0.36 23.92 ?  105 ASP   A CG   1 
ATOM   2173 O  OD1  A ASP   A 1 105 ? 23.560 -10.271 -14.298 0.64 34.41 ?  105 ASP   A OD1  1 
ATOM   2174 O  OD1  B ASP   A 1 105 ? 23.880 -10.947 -13.902 0.36 24.22 ?  105 ASP   A OD1  1 
ATOM   2175 O  OD2  A ASP   A 1 105 ? 25.660 -10.921 -14.340 0.64 34.93 -1 105 ASP   A OD2  1 
ATOM   2176 O  OD2  B ASP   A 1 105 ? 26.005 -11.489 -13.750 0.36 24.78 -1 105 ASP   A OD2  1 
ATOM   2177 H  H    A ASP   A 1 105 ? 25.407 -6.291  -13.399 0.64 33.83 ?  105 ASP   A H    1 
ATOM   2178 H  H    B ASP   A 1 105 ? 25.619 -6.809  -13.652 0.36 23.29 ?  105 ASP   A H    1 
ATOM   2179 H  HA   A ASP   A 1 105 ? 23.409 -7.757  -14.291 0.64 34.83 ?  105 ASP   A HA   1 
ATOM   2180 H  HA   B ASP   A 1 105 ? 23.666 -8.347  -14.319 0.36 24.56 ?  105 ASP   A HA   1 
ATOM   2181 H  HB2  A ASP   A 1 105 ? 25.674 -8.296  -14.708 0.64 37.94 ?  105 ASP   A HB2  1 
ATOM   2182 H  HB2  B ASP   A 1 105 ? 25.917 -8.940  -14.596 0.36 26.78 ?  105 ASP   A HB2  1 
ATOM   2183 H  HB3  A ASP   A 1 105 ? 25.851 -8.642  -13.167 0.64 37.94 ?  105 ASP   A HB3  1 
ATOM   2184 H  HB3  B ASP   A 1 105 ? 26.079 -9.062  -13.020 0.36 26.78 ?  105 ASP   A HB3  1 
ATOM   2185 N  N    A ILE   A 1 106 ? 22.109 -8.564  -12.380 0.64 26.46 ?  106 ILE   A N    1 
ATOM   2186 N  N    B ILE   A 1 106 ? 22.249 -8.924  -12.420 0.36 20.93 ?  106 ILE   A N    1 
ATOM   2187 C  CA   A ILE   A 1 106 ? 21.356 -8.981  -11.203 0.64 25.41 ?  106 ILE   A CA   1 
ATOM   2188 C  CA   B ILE   A 1 106 ? 21.456 -9.264  -11.246 0.36 22.04 ?  106 ILE   A CA   1 
ATOM   2189 C  C    A ILE   A 1 106 ? 21.892 -10.276 -10.607 0.64 24.29 ?  106 ILE   A C    1 
ATOM   2190 C  C    B ILE   A 1 106 ? 21.970 -10.534 -10.593 0.36 22.58 ?  106 ILE   A C    1 
ATOM   2191 O  O    A ILE   A 1 106 ? 21.666 -10.541 -9.421  0.64 23.37 ?  106 ILE   A O    1 
ATOM   2192 O  O    B ILE   A 1 106 ? 21.759 -10.741 -9.393  0.36 22.54 ?  106 ILE   A O    1 
ATOM   2193 C  CB   A ILE   A 1 106 ? 19.849 -9.067  -11.528 0.64 26.68 ?  106 ILE   A CB   1 
ATOM   2194 C  CB   B ILE   A 1 106 ? 19.957 -9.363  -11.602 0.36 23.25 ?  106 ILE   A CB   1 
ATOM   2195 C  CG1  A ILE   A 1 106 ? 19.013 -9.153  -10.247 0.64 27.26 ?  106 ILE   A CG1  1 
ATOM   2196 C  CG1  B ILE   A 1 106 ? 19.095 -9.347  -10.336 0.36 23.98 ?  106 ILE   A CG1  1 
ATOM   2197 C  CG2  A ILE   A 1 106 ? 19.554 -10.262 -12.419 0.64 27.32 ?  106 ILE   A CG2  1 
ATOM   2198 C  CG2  B ILE   A 1 106 ? 19.678 -10.627 -12.380 0.36 23.64 ?  106 ILE   A CG2  1 
ATOM   2199 C  CD1  A ILE   A 1 106 ? 19.118 -7.929  -9.361  0.64 27.64 ?  106 ILE   A CD1  1 
ATOM   2200 C  CD1  B ILE   A 1 106 ? 19.200 -8.075  -9.532  0.36 24.37 ?  106 ILE   A CD1  1 
ATOM   2201 H  H    A ILE   A 1 106 ? 21.669 -8.599  -13.115 0.64 31.74 ?  106 ILE   A H    1 
ATOM   2202 H  H    B ILE   A 1 106 ? 21.829 -8.971  -13.167 0.36 25.11 ?  106 ILE   A H    1 
ATOM   2203 H  HA   A ILE   A 1 106 ? 21.468 -8.304  -10.527 0.64 30.48 ?  106 ILE   A HA   1 
ATOM   2204 H  HA   B ILE   A 1 106 ? 21.561 -8.553  -10.603 0.36 26.43 ?  106 ILE   A HA   1 
ATOM   2205 H  HB   A ILE   A 1 106 ? 19.596 -8.263  -12.004 0.64 32.00 ?  106 ILE   A HB   1 
ATOM   2206 H  HB   B ILE   A 1 106 ? 19.719 -8.598  -12.150 0.36 27.89 ?  106 ILE   A HB   1 
ATOM   2207 H  HG12 A ILE   A 1 106 ? 18.079 -9.258  -10.492 0.64 32.70 ?  106 ILE   A HG12 1 
ATOM   2208 H  HG12 B ILE   A 1 106 ? 18.166 -9.453  -10.591 0.36 28.76 ?  106 ILE   A HG12 1 
ATOM   2209 H  HG13 A ILE   A 1 106 ? 19.303 -9.919  -9.730  0.64 32.70 ?  106 ILE   A HG13 1 
ATOM   2210 H  HG13 B ILE   A 1 106 ? 19.365 -10.079 -9.763  0.36 28.76 ?  106 ILE   A HG13 1 
ATOM   2211 H  HG21 A ILE   A 1 106 ? 18.651 -10.180 -12.763 0.64 32.76 ?  106 ILE   A HG21 1 
ATOM   2212 H  HG21 B ILE   A 1 106 ? 18.807 -10.549 -12.795 0.36 28.35 ?  106 ILE   A HG21 1 
ATOM   2213 H  HG22 A ILE   A 1 106 ? 20.189 -10.269 -13.152 0.64 32.76 ?  106 ILE   A HG22 1 
ATOM   2214 H  HG22 B ILE   A 1 106 ? 20.363 -10.732 -13.056 0.36 28.35 ?  106 ILE   A HG22 1 
ATOM   2215 H  HG23 A ILE   A 1 106 ? 19.638 -11.074 -11.898 0.64 32.76 ?  106 ILE   A HG23 1 
ATOM   2216 H  HG23 B ILE   A 1 106 ? 19.692 -11.380 -11.770 0.36 28.35 ?  106 ILE   A HG23 1 
ATOM   2217 H  HD11 A ILE   A 1 106 ? 18.401 -7.950  -8.710  0.64 33.15 ?  106 ILE   A HD11 1 
ATOM   2218 H  HD11 B ILE   A 1 106 ? 18.459 -8.036  -8.909  0.36 29.23 ?  106 ILE   A HD11 1 
ATOM   2219 H  HD12 A ILE   A 1 106 ? 19.976 -7.938  -8.908  0.64 33.15 ?  106 ILE   A HD12 1 
ATOM   2220 H  HD12 B ILE   A 1 106 ? 20.040 -8.078  -9.045  0.36 29.23 ?  106 ILE   A HD12 1 
ATOM   2221 H  HD13 A ILE   A 1 106 ? 19.042 -7.134  -9.912  0.64 33.15 ?  106 ILE   A HD13 1 
ATOM   2222 H  HD13 B ILE   A 1 106 ? 19.168 -7.317  -10.135 0.36 29.23 ?  106 ILE   A HD13 1 
ATOM   2223 N  N    A GLN   A 1 107 ? 22.622 -11.080 -11.390 0.64 24.79 ?  107 GLN   A N    1 
ATOM   2224 N  N    B GLN   A 1 107 ? 22.657 -11.391 -11.355 0.36 23.25 ?  107 GLN   A N    1 
ATOM   2225 C  CA   A GLN   A 1 107 ? 23.197 -12.317 -10.866 0.64 26.19 ?  107 GLN   A CA   1 
ATOM   2226 C  CA   B GLN   A 1 107 ? 23.318 -12.540 -10.755 0.36 24.62 ?  107 GLN   A CA   1 
ATOM   2227 C  C    A GLN   A 1 107 ? 24.160 -12.038 -9.718  0.64 23.63 ?  107 GLN   A C    1 
ATOM   2228 C  C    B GLN   A 1 107 ? 24.334 -12.118 -9.702  0.36 22.74 ?  107 GLN   A C    1 
ATOM   2229 O  O    A GLN   A 1 107 ? 24.331 -12.877 -8.827  0.64 24.58 ?  107 GLN   A O    1 
ATOM   2230 O  O    B GLN   A 1 107 ? 24.722 -12.942 -8.866  0.36 23.44 ?  107 GLN   A O    1 
ATOM   2231 C  CB   A GLN   A 1 107 ? 23.900 -13.081 -11.993 0.64 29.96 ?  107 GLN   A CB   1 
ATOM   2232 C  CB   B GLN   A 1 107 ? 23.995 -13.390 -11.836 0.36 27.65 ?  107 GLN   A CB   1 
ATOM   2233 C  CG   A GLN   A 1 107 ? 23.028 -13.290 -13.227 0.64 33.90 ?  107 GLN   A CG   1 
ATOM   2234 C  CG   B GLN   A 1 107 ? 23.054 -13.863 -12.938 0.36 30.54 ?  107 GLN   A CG   1 
ATOM   2235 C  CD   A GLN   A 1 107 ? 21.751 -14.048 -12.917 0.64 37.05 ?  107 GLN   A CD   1 
ATOM   2236 C  CD   B GLN   A 1 107 ? 21.975 -14.800 -12.433 0.36 33.07 ?  107 GLN   A CD   1 
ATOM   2237 O  OE1  A GLN   A 1 107 ? 21.780 -15.100 -12.278 0.64 38.30 ?  107 GLN   A OE1  1 
ATOM   2238 O  OE1  B GLN   A 1 107 ? 22.165 -15.512 -11.446 0.36 33.97 ?  107 GLN   A OE1  1 
ATOM   2239 N  NE2  A GLN   A 1 107 ? 20.620 -13.513 -13.361 0.64 38.05 ?  107 GLN   A NE2  1 
ATOM   2240 N  NE2  B GLN   A 1 107 ? 20.832 -14.805 -13.113 0.36 33.86 ?  107 GLN   A NE2  1 
ATOM   2241 H  H    A GLN   A 1 107 ? 22.810 -10.925 -12.214 0.64 29.73 ?  107 GLN   A H    1 
ATOM   2242 H  H    B GLN   A 1 107 ? 22.754 -11.324 -12.207 0.36 27.88 ?  107 GLN   A H    1 
ATOM   2243 H  HA   A GLN   A 1 107 ? 22.493 -12.880 -10.524 0.64 31.42 ?  107 GLN   A HA   1 
ATOM   2244 H  HA   B GLN   A 1 107 ? 22.652 -13.094 -10.324 0.36 29.52 ?  107 GLN   A HA   1 
ATOM   2245 H  HB2  A GLN   A 1 107 ? 24.689 -12.588 -12.272 0.64 35.94 ?  107 GLN   A HB2  1 
ATOM   2246 H  HB2  B GLN   A 1 107 ? 24.696 -12.868 -12.254 0.36 33.17 ?  107 GLN   A HB2  1 
ATOM   2247 H  HB3  A GLN   A 1 107 ? 24.162 -13.959 -11.670 0.64 35.94 ?  107 GLN   A HB3  1 
ATOM   2248 H  HB3  B GLN   A 1 107 ? 24.378 -14.179 -11.420 0.36 33.17 ?  107 GLN   A HB3  1 
ATOM   2249 H  HG2  A GLN   A 1 107 ? 22.782 -12.427 -13.596 0.64 40.67 ?  107 GLN   A HG2  1 
ATOM   2250 H  HG2  B GLN   A 1 107 ? 22.617 -13.095 -13.337 0.36 36.63 ?  107 GLN   A HG2  1 
ATOM   2251 H  HG3  A GLN   A 1 107 ? 23.527 -13.798 -13.886 0.64 40.67 ?  107 GLN   A HG3  1 
ATOM   2252 H  HG3  B GLN   A 1 107 ? 23.567 -14.337 -13.610 0.36 36.63 ?  107 GLN   A HG3  1 
ATOM   2253 H  HE21 A GLN   A 1 107 ? 20.636 -12.776 -13.803 0.64 45.65 ?  107 GLN   A HE21 1 
ATOM   2254 H  HE21 B GLN   A 1 107 ? 20.738 -14.291 -13.797 0.36 40.61 ?  107 GLN   A HE21 1 
ATOM   2255 H  HE22 A GLN   A 1 107 ? 19.871 -13.907 -13.208 0.64 45.65 ?  107 GLN   A HE22 1 
ATOM   2256 H  HE22 B GLN   A 1 107 ? 20.187 -15.319 -12.871 0.36 40.61 ?  107 GLN   A HE22 1 
ATOM   2257 N  N    . LEU   A 1 108 ? 24.771 -10.854 -9.710  1.00 20.39 ?  108 LEU   A N    1 
ATOM   2258 C  CA   . LEU   A 1 108 ? 25.671 -10.417 -8.653  1.00 17.23 ?  108 LEU   A CA   1 
ATOM   2259 C  C    . LEU   A 1 108 ? 24.957 -10.236 -7.323  1.00 15.14 ?  108 LEU   A C    1 
ATOM   2260 O  O    . LEU   A 1 108 ? 25.630 -10.065 -6.304  1.00 15.52 ?  108 LEU   A O    1 
ATOM   2261 C  CB   . LEU   A 1 108 ? 26.390 -9.124  -9.060  1.00 17.14 ?  108 LEU   A CB   1 
ATOM   2262 C  CG   . LEU   A 1 108 ? 27.411 -9.336  -10.178 1.00 18.73 ?  108 LEU   A CG   1 
ATOM   2263 C  CD1  . LEU   A 1 108 ? 27.877 -8.007  -10.750 1.00 19.67 ?  108 LEU   A CD1  1 
ATOM   2264 C  CD2  . LEU   A 1 108 ? 28.608 -10.144 -9.682  1.00 20.34 ?  108 LEU   A CD2  1 
ATOM   2265 H  H    A LEU   A 1 108 ? 24.672 -10.271 -10.330 0.64 24.45 ?  108 LEU   A H    1 
ATOM   2266 H  H    B LEU   A 1 108 ? 24.580 -10.266 -10.302 0.36 24.45 ?  108 LEU   A H    1 
ATOM   2267 H  HA   . LEU   A 1 108 ? 26.348 -11.098 -8.523  1.00 20.66 ?  108 LEU   A HA   1 
ATOM   2268 H  HB2  . LEU   A 1 108 ? 25.735 -8.483  -9.376  1.00 20.55 ?  108 LEU   A HB2  1 
ATOM   2269 H  HB3  . LEU   A 1 108 ? 26.860 -8.769  -8.292  1.00 20.55 ?  108 LEU   A HB3  1 
ATOM   2270 H  HG   . LEU   A 1 108 ? 26.997 -9.841  -10.896 1.00 22.46 ?  108 LEU   A HG   1 
ATOM   2271 H  HD11 . LEU   A 1 108 ? 28.492 -8.175  -11.484 1.00 23.59 ?  108 LEU   A HD11 1 
ATOM   2272 H  HD12 . LEU   A 1 108 ? 27.107 -7.515  -11.071 1.00 23.59 ?  108 LEU   A HD12 1 
ATOM   2273 H  HD13 . LEU   A 1 108 ? 28.327 -7.503  -10.054 1.00 23.59 ?  108 LEU   A HD13 1 
ATOM   2274 H  HD21 . LEU   A 1 108 ? 29.312 -10.104 -10.345 1.00 24.39 ?  108 LEU   A HD21 1 
ATOM   2275 H  HD22 . LEU   A 1 108 ? 28.917 -9.761  -8.845  1.00 24.39 ?  108 LEU   A HD22 1 
ATOM   2276 H  HD23 . LEU   A 1 108 ? 28.333 -11.063 -9.543  1.00 24.39 ?  108 LEU   A HD23 1 
ATOM   2277 N  N    . LEU   A 1 109 ? 23.624 -10.298 -7.291  1.00 14.29 ?  109 LEU   A N    1 
ATOM   2278 C  CA   . LEU   A 1 109 ? 22.928 -10.170 -6.017  1.00 13.49 ?  109 LEU   A CA   1 
ATOM   2279 C  C    . LEU   A 1 109 ? 23.272 -11.320 -5.076  1.00 12.80 ?  109 LEU   A C    1 
ATOM   2280 O  O    . LEU   A 1 109 ? 23.414 -11.118 -3.866  1.00 13.62 ?  109 LEU   A O    1 
ATOM   2281 C  CB   . LEU   A 1 109 ? 21.422 -10.090 -6.260  1.00 14.32 ?  109 LEU   A CB   1 
ATOM   2282 C  CG   . LEU   A 1 109 ? 20.535 -9.787  -5.055  1.00 14.55 ?  109 LEU   A CG   1 
ATOM   2283 C  CD1  . LEU   A 1 109 ? 20.993 -8.514  -4.372  1.00 15.02 ?  109 LEU   A CD1  1 
ATOM   2284 C  CD2  . LEU   A 1 109 ? 19.085 -9.657  -5.490  1.00 15.57 ?  109 LEU   A CD2  1 
ATOM   2285 H  H    . LEU   A 1 109 ? 23.110 -10.409 -7.975  1.00 17.14 ?  109 LEU   A H    1 
ATOM   2286 H  HA   . LEU   A 1 109 ? 23.208 -9.342  -5.594  1.00 16.17 ?  109 LEU   A HA   1 
ATOM   2287 H  HB2  . LEU   A 1 109 ? 21.257 -9.393  -6.913  1.00 17.17 ?  109 LEU   A HB2  1 
ATOM   2288 H  HB3  . LEU   A 1 109 ? 21.127 -10.940 -6.616  1.00 17.17 ?  109 LEU   A HB3  1 
ATOM   2289 H  HG   . LEU   A 1 109 ? 20.593 -10.508 -4.412  1.00 17.44 ?  109 LEU   A HG   1 
ATOM   2290 H  HD11 . LEU   A 1 109 ? 20.312 -8.215  -3.750  1.00 18.00 ?  109 LEU   A HD11 1 
ATOM   2291 H  HD12 . LEU   A 1 109 ? 21.822 -8.683  -3.900  1.00 18.00 ?  109 LEU   A HD12 1 
ATOM   2292 H  HD13 . LEU   A 1 109 ? 21.137 -7.824  -5.049  1.00 18.00 ?  109 LEU   A HD13 1 
ATOM   2293 H  HD21 . LEU   A 1 109 ? 18.547 -9.354  -4.738  1.00 18.67 ?  109 LEU   A HD21 1 
ATOM   2294 H  HD22 . LEU   A 1 109 ? 19.022 -9.016  -6.215  1.00 18.67 ?  109 LEU   A HD22 1 
ATOM   2295 H  HD23 . LEU   A 1 109 ? 18.764 -10.525 -5.790  1.00 18.67 ?  109 LEU   A HD23 1 
ATOM   2296 N  N    . LYS   A 1 110 ? 23.416 -12.535 -5.606  1.00 12.68 ?  110 LYS   A N    1 
ATOM   2297 C  CA   . LYS   A 1 110 ? 23.793 -13.650 -4.744  1.00 12.79 ?  110 LYS   A CA   1 
ATOM   2298 C  C    . LYS   A 1 110 ? 25.171 -13.422 -4.138  1.00 12.40 ?  110 LYS   A C    1 
ATOM   2299 O  O    . LYS   A 1 110 ? 25.370 -13.626 -2.937  1.00 12.88 ?  110 LYS   A O    1 
ATOM   2300 C  CB   . LYS   A 1 110 ? 23.720 -14.976 -5.502  1.00 13.99 ?  110 LYS   A CB   1 
ATOM   2301 C  CG   . LYS   A 1 110 ? 23.921 -16.186 -4.594  1.00 14.10 ?  110 LYS   A CG   1 
ATOM   2302 C  CD   . LYS   A 1 110 ? 23.691 -17.502 -5.308  1.00 14.61 ?  110 LYS   A CD   1 
ATOM   2303 C  CE   . LYS   A 1 110 ? 23.796 -18.682 -4.354  1.00 15.55 ?  110 LYS   A CE   1 
ATOM   2304 N  NZ   . LYS   A 1 110 ? 22.604 -18.811 -3.478  1.00 16.16 ?  110 LYS   A NZ   1 
ATOM   2305 H  H    . LYS   A 1 110 ? 23.299 -12.735 -6.432  1.00 15.20 ?  110 LYS   A H    1 
ATOM   2306 H  HA   . LYS   A 1 110 ? 23.154 -13.699 -4.009  1.00 15.34 ?  110 LYS   A HA   1 
ATOM   2307 H  HB2  . LYS   A 1 110 ? 22.843 -15.059 -5.913  1.00 16.77 ?  110 LYS   A HB2  1 
ATOM   2308 H  HB3  . LYS   A 1 110 ? 24.408 -14.992 -6.178  1.00 16.77 ?  110 LYS   A HB3  1 
ATOM   2309 H  HG2  . LYS   A 1 110 ? 24.831 -16.180 -4.256  1.00 16.90 ?  110 LYS   A HG2  1 
ATOM   2310 H  HG3  . LYS   A 1 110 ? 23.296 -16.135 -3.852  1.00 16.90 ?  110 LYS   A HG3  1 
ATOM   2311 H  HD2  . LYS   A 1 110 ? 22.809 -17.508 -5.696  1.00 17.51 ?  110 LYS   A HD2  1 
ATOM   2312 H  HD3  . LYS   A 1 110 ? 24.368 -17.612 -5.995  1.00 17.51 ?  110 LYS   A HD3  1 
ATOM   2313 H  HE2  . LYS   A 1 110 ? 23.885 -19.501 -4.865  1.00 18.64 ?  110 LYS   A HE2  1 
ATOM   2314 H  HE3  . LYS   A 1 110 ? 24.576 -18.564 -3.782  1.00 18.64 ?  110 LYS   A HE3  1 
ATOM   2315 H  HZ1  . LYS   A 1 110 ? 22.693 -19.504 -2.935  1.00 19.38 ?  110 LYS   A HZ1  1 
ATOM   2316 H  HZ2  . LYS   A 1 110 ? 22.504 -18.068 -2.992  1.00 19.38 ?  110 LYS   A HZ2  1 
ATOM   2317 H  HZ3  . LYS   A 1 110 ? 21.874 -18.921 -3.979  1.00 19.38 ?  110 LYS   A HZ3  1 
ATOM   2318 N  N    . SER   A 1 111 ? 26.132 -12.987 -4.958  1.00 12.67 ?  111 SER   A N    1 
ATOM   2319 C  CA   . SER   A 1 111 ? 27.462 -12.682 -4.442  1.00 12.93 ?  111 SER   A CA   1 
ATOM   2320 C  C    . SER   A 1 111 ? 27.395 -11.634 -3.337  1.00 12.51 ?  111 SER   A C    1 
ATOM   2321 O  O    . SER   A 1 111 ? 28.096 -11.732 -2.324  1.00 13.11 ?  111 SER   A O    1 
ATOM   2322 C  CB   . SER   A 1 111 ? 28.356 -12.191 -5.584  1.00 14.15 ?  111 SER   A CB   1 
ATOM   2323 O  OG   . SER   A 1 111 ? 28.465 -13.174 -6.601  1.00 15.89 ?  111 SER   A OG   1 
ATOM   2324 H  H    . SER   A 1 111 ? 26.031 -12.863 -5.801  1.00 15.19 ?  111 SER   A H    1 
ATOM   2325 H  HA   . SER   A 1 111 ? 27.854 -13.490 -4.076  1.00 15.50 ?  111 SER   A HA   1 
ATOM   2326 H  HB2  . SER   A 1 111 ? 27.963 -11.393 -5.971  1.00 16.97 ?  111 SER   A HB2  1 
ATOM   2327 H  HB3  . SER   A 1 111 ? 29.235 -11.992 -5.232  1.00 16.97 ?  111 SER   A HB3  1 
ATOM   2328 H  HG   . SER   A 1 111 ? 28.974 -12.892 -7.217  1.00 19.05 ?  111 SER   A HG   1 
ATOM   2329 N  N    . ALA   A 1 112 ? 26.545 -10.620 -3.514  1.00 12.76 ?  112 ALA   A N    1 
ATOM   2330 C  CA   . ALA   A 1 112 ? 26.404 -9.578  -2.501  1.00 12.57 ?  112 ALA   A CA   1 
ATOM   2331 C  C    . ALA   A 1 112 ? 25.921 -10.169 -1.180  1.00 12.41 ?  112 ALA   A C    1 
ATOM   2332 O  O    . ALA   A 1 112 ? 26.474 -9.883  -0.110  1.00 12.87 ?  112 ALA   A O    1 
ATOM   2333 C  CB   . ALA   A 1 112 ? 25.448 -8.490  -3.000  1.00 12.79 ?  112 ALA   A CB   1 
ATOM   2334 H  H    . ALA   A 1 112 ? 26.043 -10.513 -4.205  1.00 15.29 ?  112 ALA   A H    1 
ATOM   2335 H  HA   . ALA   A 1 112 ? 27.271 -9.163  -2.348  1.00 15.07 ?  112 ALA   A HA   1 
ATOM   2336 H  HB1  . ALA   A 1 112 ? 25.380 -7.790  -2.325  1.00 15.33 ?  112 ALA   A HB1  1 
ATOM   2337 H  HB2  . ALA   A 1 112 ? 25.798 -8.109  -3.824  1.00 15.33 ?  112 ALA   A HB2  1 
ATOM   2338 H  HB3  . ALA   A 1 112 ? 24.576 -8.878  -3.160  1.00 15.33 ?  112 ALA   A HB3  1 
ATOM   2339 N  N    . TYR   A 1 113 ? 24.888 -11.014 -1.234  1.00 12.63 ?  113 TYR   A N    1 
ATOM   2340 C  CA   . TYR   A 1 113 ? 24.381 -11.616 -0.005  1.00 12.32 ?  113 TYR   A CA   1 
ATOM   2341 C  C    . TYR   A 1 113 ? 25.382 -12.569 0.643   1.00 12.32 ?  113 TYR   A C    1 
ATOM   2342 O  O    . TYR   A 1 113 ? 25.334 -12.760 1.862   1.00 12.70 ?  113 TYR   A O    1 
ATOM   2343 C  CB   . TYR   A 1 113 ? 23.063 -12.345 -0.269  1.00 12.57 ?  113 TYR   A CB   1 
ATOM   2344 C  CG   . TYR   A 1 113 ? 21.843 -11.450 -0.189  1.00 12.29 ?  113 TYR   A CG   1 
ATOM   2345 C  CD1  . TYR   A 1 113 ? 21.474 -10.848 1.009   1.00 12.48 ?  113 TYR   A CD1  1 
ATOM   2346 C  CD2  . TYR   A 1 113 ? 21.048 -11.233 -1.303  1.00 12.55 ?  113 TYR   A CD2  1 
ATOM   2347 C  CE1  . TYR   A 1 113 ? 20.345 -10.052 1.090   1.00 12.67 ?  113 TYR   A CE1  1 
ATOM   2348 C  CE2  . TYR   A 1 113 ? 19.899 -10.430 -1.227  1.00 12.79 ?  113 TYR   A CE2  1 
ATOM   2349 C  CZ   . TYR   A 1 113 ? 19.564 -9.849  -0.026  1.00 12.42 ?  113 TYR   A CZ   1 
ATOM   2350 O  OH   . TYR   A 1 113 ? 18.437 -9.056  0.083   1.00 13.15 ?  113 TYR   A OH   1 
ATOM   2351 H  H    . TYR   A 1 113 ? 24.477 -11.242 -1.954  1.00 15.14 ?  113 TYR   A H    1 
ATOM   2352 H  HA   . TYR   A 1 113 ? 24.203 -10.911 0.631   1.00 14.77 ?  113 TYR   A HA   1 
ATOM   2353 H  HB2  . TYR   A 1 113 ? 23.088 -12.727 -1.159  1.00 15.07 ?  113 TYR   A HB2  1 
ATOM   2354 H  HB3  . TYR   A 1 113 ? 22.959 -13.048 0.390   1.00 15.07 ?  113 TYR   A HB3  1 
ATOM   2355 H  HD1  . TYR   A 1 113 ? 21.994 -10.989 1.769   1.00 14.95 ?  113 TYR   A HD1  1 
ATOM   2356 H  HD2  . TYR   A 1 113 ? 21.269 -11.636 -2.109  1.00 15.04 ?  113 TYR   A HD2  1 
ATOM   2357 H  HE1  . TYR   A 1 113 ? 20.115 -9.659  1.899   1.00 15.19 ?  113 TYR   A HE1  1 
ATOM   2358 H  HE2  . TYR   A 1 113 ? 19.368 -10.290 -1.978  1.00 15.33 ?  113 TYR   A HE2  1 
ATOM   2359 H  HH   . TYR   A 1 113 ? 18.056 -9.015  -0.673  1.00 15.77 ?  113 TYR   A HH   1 
ATOM   2360 N  N    . GLU   A 1 114 ? 26.283 -13.184 -0.139  1.00 12.29 ?  114 GLU   A N    1 
ATOM   2361 C  CA   . GLU   A 1 114 ? 27.275 -14.081 0.459   1.00 12.49 ?  114 GLU   A CA   1 
ATOM   2362 C  C    . GLU   A 1 114 ? 28.123 -13.372 1.509   1.00 12.41 ?  114 GLU   A C    1 
ATOM   2363 O  O    . GLU   A 1 114 ? 28.595 -14.006 2.461   1.00 12.68 ?  114 GLU   A O    1 
ATOM   2364 C  CB   . GLU   A 1 114 ? 28.145 -14.727 -0.627  1.00 12.70 ?  114 GLU   A CB   1 
ATOM   2365 C  CG   . GLU   A 1 114 ? 27.377 -15.773 -1.416  1.00 13.30 ?  114 GLU   A CG   1 
ATOM   2366 C  CD   . GLU   A 1 114 ? 28.094 -16.311 -2.649  1.00 13.61 ?  114 GLU   A CD   1 
ATOM   2367 O  OE1  . GLU   A 1 114 ? 29.051 -15.682 -3.148  1.00 13.84 ?  114 GLU   A OE1  1 
ATOM   2368 O  OE2  . GLU   A 1 114 ? 27.658 -17.372 -3.142  1.00 14.85 -1 114 GLU   A OE2  1 
ATOM   2369 H  H    . GLU   A 1 114 ? 26.341 -13.091 -0.997  1.00 14.74 ?  114 GLU   A H    1 
ATOM   2370 H  HA   . GLU   A 1 114 ? 26.797 -14.792 0.907   1.00 14.97 ?  114 GLU   A HA   1 
ATOM   2371 H  HB2  . GLU   A 1 114 ? 28.443 -14.045 -1.247  1.00 15.23 ?  114 GLU   A HB2  1 
ATOM   2372 H  HB3  . GLU   A 1 114 ? 28.900 -15.161 -0.210  1.00 15.23 ?  114 GLU   A HB3  1 
ATOM   2373 H  HG2  . GLU   A 1 114 ? 27.196 -16.526 -0.834  1.00 15.95 ?  114 GLU   A HG2  1 
ATOM   2374 H  HG3  . GLU   A 1 114 ? 26.538 -15.384 -1.713  1.00 15.95 ?  114 GLU   A HG3  1 
ATOM   2375 N  N    . ASN   A 1 115 ? 28.304 -12.056 1.379   1.00 12.23 ?  115 ASN   A N    1 
ATOM   2376 C  CA   . ASN   A 1 115 ? 29.073 -11.328 2.383   1.00 12.71 ?  115 ASN   A CA   1 
ATOM   2377 C  C    . ASN   A 1 115 ? 28.456 -11.462 3.769   1.00 12.57 ?  115 ASN   A C    1 
ATOM   2378 O  O    . ASN   A 1 115 ? 29.172 -11.396 4.775   1.00 13.06 ?  115 ASN   A O    1 
ATOM   2379 C  CB   . ASN   A 1 115 ? 29.175 -9.854  2.004   1.00 13.07 ?  115 ASN   A CB   1 
ATOM   2380 C  CG   . ASN   A 1 115 ? 29.972 -9.633  0.739   1.00 13.44 ?  115 ASN   A CG   1 
ATOM   2381 O  OD1  . ASN   A 1 115 ? 31.189 -9.727  0.756   1.00 16.57 ?  115 ASN   A OD1  1 
ATOM   2382 N  ND2  . ASN   A 1 115 ? 29.296 -9.327  -0.357  1.00 12.86 ?  115 ASN   A ND2  1 
ATOM   2383 H  H    . ASN   A 1 115 ? 27.992 -11.568 0.737   1.00 14.66 ?  115 ASN   A H    1 
ATOM   2384 H  HA   . ASN   A 1 115 ? 29.967 -11.696 2.418   1.00 15.23 ?  115 ASN   A HA   1 
ATOM   2385 H  HB2  . ASN   A 1 115 ? 28.282 -9.498  1.874   1.00 15.67 ?  115 ASN   A HB2  1 
ATOM   2386 H  HB3  . ASN   A 1 115 ? 29.616 -9.376  2.728   1.00 15.67 ?  115 ASN   A HB3  1 
ATOM   2387 H  HD21 . ASN   A 1 115 ? 29.708 -9.192  -1.099  1.00 15.42 ?  115 ASN   A HD21 1 
ATOM   2388 H  HD22 . ASN   A 1 115 ? 28.435 -9.287  -0.333  1.00 15.42 ?  115 ASN   A HD22 1 
ATOM   2389 N  N    . PHE   A 1 116 ? 27.128 -11.633 3.847   1.00 12.69 ?  116 PHE   A N    1 
ATOM   2390 C  CA   . PHE   A 1 116 ? 26.477 -11.729 5.152   1.00 12.61 ?  116 PHE   A CA   1 
ATOM   2391 C  C    . PHE   A 1 116 ? 26.953 -12.958 5.925   1.00 12.58 ?  116 PHE   A C    1 
ATOM   2392 O  O    . PHE   A 1 116 ? 26.885 -12.975 7.157   1.00 13.32 ?  116 PHE   A O    1 
ATOM   2393 C  CB   . PHE   A 1 116 ? 24.949 -11.858 5.015   1.00 12.83 ?  116 PHE   A CB   1 
ATOM   2394 C  CG   . PHE   A 1 116 ? 24.193 -10.609 4.550   1.00 12.31 ?  116 PHE   A CG   1 
ATOM   2395 C  CD1  . PHE   A 1 116 ? 24.771 -9.584  3.816   1.00 12.32 ?  116 PHE   A CD1  1 
ATOM   2396 C  CD2  . PHE   A 1 116 ? 22.837 -10.509 4.854   1.00 12.94 ?  116 PHE   A CD2  1 
ATOM   2397 C  CE1  . PHE   A 1 116 ? 24.006 -8.511  3.392   1.00 12.61 ?  116 PHE   A CE1  1 
ATOM   2398 C  CE2  . PHE   A 1 116 ? 22.078 -9.441  4.442   1.00 12.86 ?  116 PHE   A CE2  1 
ATOM   2399 C  CZ   . PHE   A 1 116 ? 22.657 -8.438  3.712   1.00 12.20 ?  116 PHE   A CZ   1 
ATOM   2400 H  H    . PHE   A 1 116 ? 26.592 -11.684 3.174   1.00 15.22 ?  116 PHE   A H    1 
ATOM   2401 H  HA   . PHE   A 1 116 ? 26.669 -10.937 5.676   1.00 15.11 ?  116 PHE   A HA   1 
ATOM   2402 H  HB2  . PHE   A 1 116 ? 24.761 -12.567 4.377   1.00 15.38 ?  116 PHE   A HB2  1 
ATOM   2403 H  HB3  . PHE   A 1 116 ? 24.589 -12.112 5.883   1.00 15.38 ?  116 PHE   A HB3  1 
ATOM   2404 H  HD1  . PHE   A 1 116 ? 25.668 -9.646  3.593   1.00 14.77 ?  116 PHE   A HD1  1 
ATOM   2405 H  HD2  . PHE   A 1 116 ? 22.426 -11.199 5.341   1.00 15.52 ?  116 PHE   A HD2  1 
ATOM   2406 H  HE1  . PHE   A 1 116 ? 24.406 -7.832  2.907   1.00 15.11 ?  116 PHE   A HE1  1 
ATOM   2407 H  HE2  . PHE   A 1 116 ? 21.171 -9.402  4.663   1.00 15.41 ?  116 PHE   A HE2  1 
ATOM   2408 H  HZ   . PHE   A 1 116 ? 22.150 -7.707  3.442   1.00 14.62 ?  116 PHE   A HZ   1 
ATOM   2409 N  N    . ASN   A 1 117 ? 27.397 -14.007 5.222   1.00 13.02 ?  117 ASN   A N    1 
ATOM   2410 C  CA   . ASN   A 1 117 ? 27.766 -15.252 5.888   1.00 13.13 ?  117 ASN   A CA   1 
ATOM   2411 C  C    . ASN   A 1 117 ? 29.025 -15.132 6.725   1.00 13.91 ?  117 ASN   A C    1 
ATOM   2412 O  O    . ASN   A 1 117 ? 29.328 -16.055 7.487   1.00 14.94 ?  117 ASN   A O    1 
ATOM   2413 C  CB   . ASN   A 1 117 ? 27.887 -16.373 4.865   1.00 13.27 ?  117 ASN   A CB   1 
ATOM   2414 C  CG   . ASN   A 1 117 ? 26.536 -16.762 4.323   1.00 13.38 ?  117 ASN   A CG   1 
ATOM   2415 O  OD1  . ASN   A 1 117 ? 25.554 -16.782 5.069   1.00 14.19 ?  117 ASN   A OD1  1 
ATOM   2416 N  ND2  . ASN   A 1 117 ? 26.455 -17.018 3.032   1.00 13.12 ?  117 ASN   A ND2  1 
ATOM   2417 H  H    . ASN   A 1 117 ? 27.477 -14.020 4.363   1.00 15.61 ?  117 ASN   A H    1 
ATOM   2418 H  HA   . ASN   A 1 117 ? 27.040 -15.488 6.489   1.00 15.74 ?  117 ASN   A HA   1 
ATOM   2419 H  HB2  . ASN   A 1 117 ? 28.437 -16.072 4.124   1.00 15.91 ?  117 ASN   A HB2  1 
ATOM   2420 H  HB3  . ASN   A 1 117 ? 28.280 -17.146 5.288   1.00 15.91 ?  117 ASN   A HB3  1 
ATOM   2421 H  HD21 . ASN   A 1 117 ? 25.705 -17.241 2.688   1.00 15.73 ?  117 ASN   A HD21 1 
ATOM   2422 H  HD22 . ASN   A 1 117 ? 27.165 -16.982 2.546   1.00 15.73 ?  117 ASN   A HD22 1 
ATOM   2423 N  N    . GLN   A 1 118 ? 29.754 -14.020 6.612   1.00 13.46 ?  118 GLN   A N    1 
ATOM   2424 C  CA   . GLN   A 1 118 ? 30.930 -13.788 7.438   1.00 14.10 ?  118 GLN   A CA   1 
ATOM   2425 C  C    . GLN   A 1 118 ? 30.585 -13.216 8.808   1.00 14.16 ?  118 GLN   A C    1 
ATOM   2426 O  O    . GLN   A 1 118 ? 31.502 -12.923 9.586   1.00 15.57 ?  118 GLN   A O    1 
ATOM   2427 C  CB   . GLN   A 1 118 ? 31.929 -12.886 6.704   1.00 14.62 ?  118 GLN   A CB   1 
ATOM   2428 C  CG   . GLN   A 1 118 ? 32.394 -13.464 5.377   1.00 14.46 ?  118 GLN   A CG   1 
ATOM   2429 C  CD   . GLN   A 1 118 ? 33.230 -14.722 5.551   1.00 14.65 ?  118 GLN   A CD   1 
ATOM   2430 O  OE1  . GLN   A 1 118 ? 34.100 -14.779 6.426   1.00 15.48 ?  118 GLN   A OE1  1 
ATOM   2431 N  NE2  . GLN   A 1 118 ? 32.985 -15.726 4.707   1.00 14.51 ?  118 GLN   A NE2  1 
ATOM   2432 H  H    . GLN   A 1 118 ? 29.575 -13.373 6.062   1.00 16.14 ?  118 GLN   A H    1 
ATOM   2433 H  HA   . GLN   A 1 118 ? 31.358 -14.645 7.581   1.00 16.91 ?  118 GLN   A HA   1 
ATOM   2434 H  HB2  . GLN   A 1 118 ? 31.510 -12.031 6.531   1.00 17.52 ?  118 GLN   A HB2  1 
ATOM   2435 H  HB3  . GLN   A 1 118 ? 32.708 -12.768 7.268   1.00 17.52 ?  118 GLN   A HB3  1 
ATOM   2436 H  HG2  . GLN   A 1 118 ? 31.618 -13.688 4.834   1.00 17.34 ?  118 GLN   A HG2  1 
ATOM   2437 H  HG3  . GLN   A 1 118 ? 32.936 -12.804 4.916   1.00 17.34 ?  118 GLN   A HG3  1 
ATOM   2438 H  HE21 . GLN   A 1 118 ? 32.364 -15.645 4.106   1.00 17.40 ?  118 GLN   A HE21 1 
ATOM   2439 H  HE22 . GLN   A 1 118 ? 33.427 -16.457 4.761   1.00 17.40 ?  118 GLN   A HE22 1 
ATOM   2440 N  N    . HIS   A 1 119 ? 29.296 -13.059 9.118   1.00 13.85 ?  119 HIS   A N    1 
ATOM   2441 C  CA   . HIS   A 1 119 ? 28.847 -12.454 10.365  1.00 14.36 ?  119 HIS   A CA   1 
ATOM   2442 C  C    . HIS   A 1 119 ? 27.704 -13.272 10.939  1.00 14.76 ?  119 HIS   A C    1 
ATOM   2443 O  O    . HIS   A 1 119 ? 26.760 -13.610 10.221  1.00 15.12 ?  119 HIS   A O    1 
ATOM   2444 C  CB   . HIS   A 1 119 ? 28.399 -11.019 10.099  1.00 14.87 ?  119 HIS   A CB   1 
ATOM   2445 C  CG   . HIS   A 1 119 ? 29.479 -10.214 9.471   1.00 15.99 ?  119 HIS   A CG   1 
ATOM   2446 N  ND1  . HIS   A 1 119 ? 30.459 -9.599  10.213  1.00 18.34 ?  119 HIS   A ND1  1 
ATOM   2447 C  CD2  . HIS   A 1 119 ? 29.801 -10.021 8.172   1.00 16.91 ?  119 HIS   A CD2  1 
ATOM   2448 C  CE1  . HIS   A 1 119 ? 31.317 -9.016  9.395   1.00 18.27 ?  119 HIS   A CE1  1 
ATOM   2449 N  NE2  . HIS   A 1 119 ? 30.947 -9.265  8.152   1.00 18.11 ?  119 HIS   A NE2  1 
ATOM   2450 H  H    . HIS   A 1 119 ? 28.644 -13.320 8.612   1.00 16.61 ?  119 HIS   A H    1 
ATOM   2451 H  HA   . HIS   A 1 119 ? 29.576 -12.448 11.002  1.00 17.21 ?  119 HIS   A HA   1 
ATOM   2452 H  HB2  . HIS   A 1 119 ? 27.635 -11.035 9.501   1.00 17.83 ?  119 HIS   A HB2  1 
ATOM   2453 H  HB3  . HIS   A 1 119 ? 28.159 -10.607 10.942  1.00 17.83 ?  119 HIS   A HB3  1 
ATOM   2454 H  HD2  . HIS   A 1 119 ? 29.334 -10.339 7.429   1.00 20.28 ?  119 HIS   A HD2  1 
ATOM   2455 H  HE1  . HIS   A 1 119 ? 32.055 -8.514  9.651   1.00 21.91 ?  119 HIS   A HE1  1 
ATOM   2456 H  HE2  . HIS   A 1 119 ? 31.345 -8.978  7.444   1.00 21.71 ?  119 HIS   A HE2  1 
ATOM   2457 N  N    . GLU   A 1 120 ? 27.784 -13.573 12.237  1.00 15.93 ?  120 GLU   A N    1 
ATOM   2458 C  CA   . GLU   A 1 120 ? 26.831 -14.501 12.839  1.00 18.24 ?  120 GLU   A CA   1 
ATOM   2459 C  C    . GLU   A 1 120 ? 25.416 -13.937 12.896  1.00 16.53 ?  120 GLU   A C    1 
ATOM   2460 O  O    . GLU   A 1 120 ? 24.443 -14.699 12.778  1.00 16.60 ?  120 GLU   A O    1 
ATOM   2461 C  CB   . GLU   A 1 120 ? 27.301 -14.894 14.243  1.00 23.56 ?  120 GLU   A CB   1 
ATOM   2462 C  CG   . GLU   A 1 120 ? 28.506 -15.820 14.259  1.00 30.69 ?  120 GLU   A CG   1 
ATOM   2463 C  CD   . GLU   A 1 120 ? 28.630 -16.593 15.556  1.00 37.25 ?  120 GLU   A CD   1 
ATOM   2464 O  OE1  . GLU   A 1 120 ? 28.204 -16.067 16.606  1.00 39.39 ?  120 GLU   A OE1  1 
ATOM   2465 O  OE2  . GLU   A 1 120 ? 29.151 -17.728 15.524  1.00 40.40 -1 120 GLU   A OE2  1 
ATOM   2466 H  H    . GLU   A 1 120 ? 28.383 -13.265 12.781  1.00 19.10 ?  120 GLU   A H    1 
ATOM   2467 H  HA   . GLU   A 1 120 ? 26.811 -15.311 12.310  1.00 21.87 ?  120 GLU   A HA   1 
ATOM   2468 H  HB2  . GLU   A 1 120 ? 27.542 -14.096 14.737  1.00 28.25 ?  120 GLU   A HB2  1 
ATOM   2469 H  HB3  . GLU   A 1 120 ? 26.577 -15.355 14.702  1.00 28.25 ?  120 GLU   A HB3  1 
ATOM   2470 H  HG2  . GLU   A 1 120 ? 28.433 -16.453 13.529  1.00 36.81 ?  120 GLU   A HG2  1 
ATOM   2471 H  HG3  . GLU   A 1 120 ? 29.314 -15.294 14.168  1.00 36.81 ?  120 GLU   A HG3  1 
ATOM   2472 N  N    . VAL   A 1 121 ? 25.282 -12.629 13.111  1.00 15.58 ?  121 VAL   A N    1 
ATOM   2473 C  CA   . VAL   A 1 121 ? 23.987 -11.965 13.224  1.00 15.55 ?  121 VAL   A CA   1 
ATOM   2474 C  C    . VAL   A 1 121 ? 24.101 -10.588 12.580  1.00 14.42 ?  121 VAL   A C    1 
ATOM   2475 O  O    . VAL   A 1 121 ? 25.071 -9.862  12.820  1.00 15.26 ?  121 VAL   A O    1 
ATOM   2476 C  CB   . VAL   A 1 121 ? 23.549 -11.811 14.698  1.00 18.47 ?  121 VAL   A CB   1 
ATOM   2477 C  CG1  . VAL   A 1 121 ? 22.151 -11.213 14.783  1.00 18.95 ?  121 VAL   A CG1  1 
ATOM   2478 C  CG2  . VAL   A 1 121 ? 23.597 -13.136 15.442  1.00 20.43 ?  121 VAL   A CG2  1 
ATOM   2479 H  H    . VAL   A 1 121 ? 25.949 -12.090 13.200  1.00 18.68 ?  121 VAL   A H    1 
ATOM   2480 H  HA   . VAL   A 1 121 ? 23.316 -12.484 12.753  1.00 18.64 ?  121 VAL   A HA   1 
ATOM   2481 H  HB   . VAL   A 1 121 ? 24.157 -11.203 15.144  1.00 22.15 ?  121 VAL   A HB   1 
ATOM   2482 H  HG11 . VAL   A 1 121 ? 21.843 -11.255 15.704  1.00 22.72 ?  121 VAL   A HG11 1 
ATOM   2483 H  HG12 . VAL   A 1 121 ? 22.179 -10.291 14.487  1.00 22.72 ?  121 VAL   A HG12 1 
ATOM   2484 H  HG13 . VAL   A 1 121 ? 21.551 -11.726 14.216  1.00 22.72 ?  121 VAL   A HG13 1 
ATOM   2485 H  HG21 . VAL   A 1 121 ? 23.242 -13.009 16.341  1.00 24.50 ?  121 VAL   A HG21 1 
ATOM   2486 H  HG22 . VAL   A 1 121 ? 23.054 -13.788 14.969  1.00 24.50 ?  121 VAL   A HG22 1 
ATOM   2487 H  HG23 . VAL   A 1 121 ? 24.514 -13.442 15.493  1.00 24.50 ?  121 VAL   A HG23 1 
ATOM   2488 N  N    . LEU   A 1 122 ? 23.090 -10.206 11.793  1.00 13.56 ?  122 LEU   A N    1 
ATOM   2489 C  CA   . LEU   A 1 122 ? 23.089 -8.908  11.127  1.00 13.51 ?  122 LEU   A CA   1 
ATOM   2490 C  C    . LEU   A 1 122 ? 21.693 -8.310  11.084  1.00 13.40 ?  122 LEU   A C    1 
ATOM   2491 O  O    . LEU   A 1 122 ? 20.698 -9.027  10.950  1.00 14.45 ?  122 LEU   A O    1 
ATOM   2492 C  CB   . LEU   A 1 122 ? 23.535 -8.998  9.665   1.00 14.75 ?  122 LEU   A CB   1 
ATOM   2493 C  CG   . LEU   A 1 122 ? 24.733 -9.865  9.304   1.00 14.85 ?  122 LEU   A CG   1 
ATOM   2494 C  CD1  . LEU   A 1 122 ? 24.308 -11.301 9.069   1.00 15.58 ?  122 LEU   A CD1  1 
ATOM   2495 C  CD2  . LEU   A 1 122 ? 25.428 -9.302  8.074   1.00 14.28 ?  122 LEU   A CD2  1 
ATOM   2496 H  H    . LEU   A 1 122 ? 22.384 -10.682 11.632  1.00 16.25 ?  122 LEU   A H    1 
ATOM   2497 H  HA   . LEU   A 1 122 ? 23.680 -8.299  11.597  1.00 16.19 ?  122 LEU   A HA   1 
ATOM   2498 H  HB2  . LEU   A 1 122 ? 22.795 -9.335  9.146   1.00 17.68 ?  122 LEU   A HB2  1 
ATOM   2499 H  HB3  . LEU   A 1 122 ? 23.753 -8.103  9.365   1.00 17.68 ?  122 LEU   A HB3  1 
ATOM   2500 H  HG   . LEU   A 1 122 ? 25.379 -9.861  10.032  1.00 17.80 ?  122 LEU   A HG   1 
ATOM   2501 H  HD11 . LEU   A 1 122 ? 25.077 -11.827 8.794   1.00 18.67 ?  122 LEU   A HD11 1 
ATOM   2502 H  HD12 . LEU   A 1 122 ? 23.942 -11.662 9.892   1.00 18.67 ?  122 LEU   A HD12 1 
ATOM   2503 H  HD13 . LEU   A 1 122 ? 23.632 -11.321 8.371   1.00 18.67 ?  122 LEU   A HD13 1 
ATOM   2504 H  HD21 . LEU   A 1 122 ? 26.173 -9.885  7.824   1.00 17.12 ?  122 LEU   A HD21 1 
ATOM   2505 H  HD22 . LEU   A 1 122 ? 24.797 -9.253  7.342   1.00 17.12 ?  122 LEU   A HD22 1 
ATOM   2506 H  HD23 . LEU   A 1 122 ? 25.772 -8.415  8.276   1.00 17.12 ?  122 LEU   A HD23 1 
ATOM   2507 N  N    A LEU   A 1 123 ? 21.637 -6.983  11.165  0.64 13.04 ?  123 LEU   A N    1 
ATOM   2508 N  N    B LEU   A 1 123 ? 21.641 -6.985  11.225  0.36 12.87 ?  123 LEU   A N    1 
ATOM   2509 C  CA   A LEU   A 1 123 ? 20.473 -6.197  10.774  0.64 12.61 ?  123 LEU   A CA   1 
ATOM   2510 C  CA   B LEU   A 1 123 ? 20.470 -6.176  10.900  0.36 12.46 ?  123 LEU   A CA   1 
ATOM   2511 C  C    A LEU   A 1 123 ? 20.720 -5.674  9.369   0.64 12.03 ?  123 LEU   A C    1 
ATOM   2512 C  C    B LEU   A 1 123 ? 20.709 -5.635  9.495   0.36 11.84 ?  123 LEU   A C    1 
ATOM   2513 O  O    A LEU   A 1 123 ? 21.816 -5.185  9.081   0.64 11.47 ?  123 LEU   A O    1 
ATOM   2514 O  O    B LEU   A 1 123 ? 21.640 -4.851  9.284   0.36 11.81 ?  123 LEU   A O    1 
ATOM   2515 C  CB   A LEU   A 1 123 ? 20.313 -5.007  11.720  0.64 13.32 ?  123 LEU   A CB   1 
ATOM   2516 C  CB   B LEU   A 1 123 ? 20.332 -5.035  11.907  0.36 13.02 ?  123 LEU   A CB   1 
ATOM   2517 C  CG   A LEU   A 1 123 ? 19.246 -3.968  11.372  0.64 14.14 ?  123 LEU   A CG   1 
ATOM   2518 C  CG   B LEU   A 1 123 ? 19.355 -3.911  11.544  0.36 13.24 ?  123 LEU   A CG   1 
ATOM   2519 C  CD1  A LEU   A 1 123 ? 17.868 -4.608  11.375  0.64 14.54 ?  123 LEU   A CD1  1 
ATOM   2520 C  CD1  B LEU   A 1 123 ? 17.908 -4.399  11.534  0.36 13.53 ?  123 LEU   A CD1  1 
ATOM   2521 C  CD2  A LEU   A 1 123 ? 19.303 -2.801  12.351  0.64 14.57 ?  123 LEU   A CD2  1 
ATOM   2522 C  CD2  B LEU   A 1 123 ? 19.521 -2.729  12.486  0.36 13.46 ?  123 LEU   A CD2  1 
ATOM   2523 H  H    A LEU   A 1 123 ? 22.297 -6.497  11.446  0.64 15.63 ?  123 LEU   A H    1 
ATOM   2524 H  H    B LEU   A 1 123 ? 22.301 -6.509  11.514  0.36 15.42 ?  123 LEU   A H    1 
ATOM   2525 H  HA   A LEU   A 1 123 ? 19.675 -6.744  10.784  0.64 15.12 ?  123 LEU   A HA   1 
ATOM   2526 H  HA   B LEU   A 1 123 ? 19.668 -6.717  10.910  0.36 14.93 ?  123 LEU   A HA   1 
ATOM   2527 H  HB2  A LEU   A 1 123 ? 20.089 -5.354  12.596  0.64 15.96 ?  123 LEU   A HB2  1 
ATOM   2528 H  HB2  B LEU   A 1 123 ? 20.035 -5.409  12.754  0.36 15.60 ?  123 LEU   A HB2  1 
ATOM   2529 H  HB3  A LEU   A 1 123 ? 21.156 -4.541  11.761  0.64 15.96 ?  123 LEU   A HB3  1 
ATOM   2530 H  HB3  B LEU   A 1 123 ? 21.203 -4.625  12.029  0.36 15.60 ?  123 LEU   A HB3  1 
ATOM   2531 H  HG   A LEU   A 1 123 ? 19.408 -3.613  10.483  0.64 16.96 ?  123 LEU   A HG   1 
ATOM   2532 H  HG   B LEU   A 1 123 ? 19.557 -3.594  10.652  0.36 15.87 ?  123 LEU   A HG   1 
ATOM   2533 H  HD11 A LEU   A 1 123 ? 17.199 -3.926  11.205  0.64 17.43 ?  123 LEU   A HD11 1 
ATOM   2534 H  HD11 B LEU   A 1 123 ? 17.323 -3.655  11.315  0.36 16.22 ?  123 LEU   A HD11 1 
ATOM   2535 H  HD12 A LEU   A 1 123 ? 17.835 -5.284  10.681  0.64 17.43 ?  123 LEU   A HD12 1 
ATOM   2536 H  HD12 B LEU   A 1 123 ? 17.813 -5.099  10.867  0.36 16.22 ?  123 LEU   A HD12 1 
ATOM   2537 H  HD13 A LEU   A 1 123 ? 17.713 -5.015  12.242  0.64 17.43 ?  123 LEU   A HD13 1 
ATOM   2538 H  HD13 B LEU   A 1 123 ? 17.683 -4.747  12.411  0.36 16.22 ?  123 LEU   A HD13 1 
ATOM   2539 H  HD21 A LEU   A 1 123 ? 18.621 -2.152  12.118  0.64 17.47 ?  123 LEU   A HD21 1 
ATOM   2540 H  HD21 B LEU   A 1 123 ? 18.890 -2.036  12.236  0.36 16.14 ?  123 LEU   A HD21 1 
ATOM   2541 H  HD22 A LEU   A 1 123 ? 19.145 -3.135  13.250  0.64 17.47 ?  123 LEU   A HD22 1 
ATOM   2542 H  HD22 B LEU   A 1 123 ? 19.347 -3.023  13.394  0.36 16.14 ?  123 LEU   A HD22 1 
ATOM   2543 H  HD23 A LEU   A 1 123 ? 20.181 -2.391  12.303  0.64 17.47 ?  123 LEU   A HD23 1 
ATOM   2544 H  HD23 B LEU   A 1 123 ? 20.427 -2.395  12.413  0.36 16.14 ?  123 LEU   A HD23 1 
ATOM   2545 N  N    A ALA   A 1 124 ? 19.714 -5.754  8.492   0.64 11.36 ?  124 ALA   A N    1 
ATOM   2546 N  N    B ALA   A 1 124 ? 19.891 -6.058  8.532   0.36 11.45 ?  124 ALA   A N    1 
ATOM   2547 C  CA   A ALA   A 1 124 ? 20.000 -5.506  7.084   0.64 10.88 ?  124 ALA   A CA   1 
ATOM   2548 C  CA   B ALA   A 1 124 ? 20.179 -5.789  7.131   0.36 12.00 ?  124 ALA   A CA   1 
ATOM   2549 C  C    A ALA   A 1 124 ? 18.756 -5.071  6.319   0.64 11.04 ?  124 ALA   A C    1 
ATOM   2550 C  C    B ALA   A 1 124 ? 18.963 -5.262  6.383   0.36 11.87 ?  124 ALA   A C    1 
ATOM   2551 O  O    A ALA   A 1 124 ? 17.629 -5.425  6.699   0.64 12.04 ?  124 ALA   A O    1 
ATOM   2552 O  O    B ALA   A 1 124 ? 17.821 -5.558  6.749   0.36 12.32 ?  124 ALA   A O    1 
ATOM   2553 C  CB   A ALA   A 1 124 ? 20.593 -6.756  6.427   0.64 11.36 ?  124 ALA   A CB   1 
ATOM   2554 C  CB   B ALA   A 1 124 ? 20.671 -7.060  6.420   0.36 12.82 ?  124 ALA   A CB   1 
ATOM   2555 H  H    A ALA   A 1 124 ? 18.892 -5.924  8.686   0.64 13.61 ?  124 ALA   A H    1 
ATOM   2556 H  H    B ALA   A 1 124 ? 19.174 -6.511  8.669   0.36 13.72 ?  124 ALA   A H    1 
ATOM   2557 H  HA   A ALA   A 1 124 ? 20.660 -4.799  7.033   0.64 13.04 ?  124 ALA   A HA   1 
ATOM   2558 H  HA   B ALA   A 1 124 ? 20.887 -5.132  7.086   0.36 14.38 ?  124 ALA   A HA   1 
ATOM   2559 H  HB1  A ALA   A 1 124 ? 20.776 -6.562  5.496   0.64 13.62 ?  124 ALA   A HB1  1 
ATOM   2560 H  HB1  B ALA   A 1 124 ? 20.857 -6.851  5.489   0.36 15.36 ?  124 ALA   A HB1  1 
ATOM   2561 H  HB2  A ALA   A 1 124 ? 21.418 -6.987  6.886   0.64 13.62 ?  124 ALA   A HB2  1 
ATOM   2562 H  HB2  B ALA   A 1 124 ? 21.481 -7.380  6.851   0.36 15.36 ?  124 ALA   A HB2  1 
ATOM   2563 H  HB3  A ALA   A 1 124 ? 19.958 -7.481  6.502   0.64 13.62 ?  124 ALA   A HB3  1 
ATOM   2564 H  HB3  B ALA   A 1 124 ? 19.981 -7.742  6.471   0.36 15.36 ?  124 ALA   A HB3  1 
ATOM   2565 N  N    A PRO   A 1 125 ? 18.936 -4.338  5.223   0.64 11.25 ?  125 PRO   A N    1 
ATOM   2566 N  N    B PRO   A 1 125 ? 19.185 -4.503  5.311   0.36 10.87 ?  125 PRO   A N    1 
ATOM   2567 C  CA   A PRO   A 1 125 ? 17.879 -4.136  4.234   0.64 11.83 ?  125 PRO   A CA   1 
ATOM   2568 C  CA   B PRO   A 1 125 ? 18.091 -4.095  4.433   0.36 11.31 ?  125 PRO   A CA   1 
ATOM   2569 C  C    A PRO   A 1 125 ? 17.963 -5.203  3.145   0.64 11.37 ?  125 PRO   A C    1 
ATOM   2570 C  C    B PRO   A 1 125 ? 17.975 -5.105  3.295   0.36 12.11 ?  125 PRO   A C    1 
ATOM   2571 O  O    A PRO   A 1 125 ? 18.942 -5.945  3.034   0.64 11.60 ?  125 PRO   A O    1 
ATOM   2572 O  O    B PRO   A 1 125 ? 18.796 -6.014  3.154   0.36 12.16 ?  125 PRO   A O    1 
ATOM   2573 C  CB   A PRO   A 1 125 ? 18.266 -2.774  3.644   0.64 12.14 ?  125 PRO   A CB   1 
ATOM   2574 C  CB   B PRO   A 1 125 ? 18.604 -2.755  3.896   0.36 10.54 ?  125 PRO   A CB   1 
ATOM   2575 C  CG   A PRO   A 1 125 ? 19.765 -2.853  3.605   0.64 12.36 ?  125 PRO   A CG   1 
ATOM   2576 C  CG   B PRO   A 1 125 ? 20.075 -3.037  3.683   0.36 10.07 ?  125 PRO   A CG   1 
ATOM   2577 C  CD   A PRO   A 1 125 ? 20.164 -3.605  4.859   0.64 11.77 ?  125 PRO   A CD   1 
ATOM   2578 C  CD   B PRO   A 1 125 ? 20.478 -4.000  4.801   0.36 9.91  ?  125 PRO   A CD   1 
ATOM   2579 H  HA   A PRO   A 1 125 ? 16.995 -4.116  4.642   0.64 14.18 ?  125 PRO   A HA   1 
ATOM   2580 H  HA   B PRO   A 1 125 ? 17.262 -3.983  4.926   0.36 13.55 ?  125 PRO   A HA   1 
ATOM   2581 H  HB2  A PRO   A 1 125 ? 17.890 -2.683  2.757   0.64 14.55 ?  125 PRO   A HB2  1 
ATOM   2582 H  HB2  B PRO   A 1 125 ? 18.155 -2.538  3.064   0.36 12.63 ?  125 PRO   A HB2  1 
ATOM   2583 H  HB3  A PRO   A 1 125 ? 17.962 -2.066  4.233   0.64 14.55 ?  125 PRO   A HB3  1 
ATOM   2584 H  HB3  B PRO   A 1 125 ? 18.470 -2.053  4.559   0.36 12.63 ?  125 PRO   A HB3  1 
ATOM   2585 H  HG2  A PRO   A 1 125 ? 20.046 -3.341  2.816   0.64 14.81 ?  125 PRO   A HG2  1 
ATOM   2586 H  HG2  B PRO   A 1 125 ? 20.202 -3.446  2.811   0.36 12.07 ?  125 PRO   A HG2  1 
ATOM   2587 H  HG3  A PRO   A 1 125 ? 20.137 -1.959  3.610   0.64 14.81 ?  125 PRO   A HG3  1 
ATOM   2588 H  HG3  B PRO   A 1 125 ? 20.577 -2.207  3.742   0.36 12.07 ?  125 PRO   A HG3  1 
ATOM   2589 H  HD2  A PRO   A 1 125 ? 20.888 -4.221  4.678   0.64 14.11 ?  125 PRO   A HD2  1 
ATOM   2590 H  HD2  B PRO   A 1 125 ? 21.017 -4.724  4.434   0.36 11.87 ?  125 PRO   A HD2  1 
ATOM   2591 H  HD3  A PRO   A 1 125 ? 20.399 -2.980  5.570   0.64 14.11 ?  125 PRO   A HD3  1 
ATOM   2592 H  HD3  B PRO   A 1 125 ? 20.962 -3.520  5.491   0.36 11.87 ?  125 PRO   A HD3  1 
ATOM   2593 N  N    A LEU   A 1 126 ? 16.917 -5.247  2.321   0.64 11.00 ?  126 LEU   A N    1 
ATOM   2594 N  N    B LEU   A 1 126 ? 16.946 -4.922  2.470   0.36 12.95 ?  126 LEU   A N    1 
ATOM   2595 C  CA   A LEU   A 1 126 ? 16.934 -6.057  1.111   0.64 11.48 ?  126 LEU   A CA   1 
ATOM   2596 C  CA   B LEU   A 1 126 ? 16.780 -5.754  1.280   0.36 13.59 ?  126 LEU   A CA   1 
ATOM   2597 C  C    A LEU   A 1 126 ? 17.870 -5.434  0.080   0.64 11.72 ?  126 LEU   A C    1 
ATOM   2598 C  C    B LEU   A 1 126 ? 17.699 -5.220  0.185   0.36 12.51 ?  126 LEU   A C    1 
ATOM   2599 O  O    A LEU   A 1 126 ? 17.667 -4.296  -0.357  0.64 12.71 ?  126 LEU   A O    1 
ATOM   2600 O  O    B LEU   A 1 126 ? 17.403 -4.202  -0.446  0.36 12.97 ?  126 LEU   A O    1 
ATOM   2601 C  CB   A LEU   A 1 126 ? 15.525 -6.179  0.547   0.64 11.81 ?  126 LEU   A CB   1 
ATOM   2602 C  CB   B LEU   A 1 126 ? 15.325 -5.716  0.831   0.36 15.72 ?  126 LEU   A CB   1 
ATOM   2603 C  CG   A LEU   A 1 126 ? 14.595 -7.088  1.350   0.64 12.50 ?  126 LEU   A CG   1 
ATOM   2604 C  CG   B LEU   A 1 126 ? 14.766 -6.848  -0.029  0.36 17.20 ?  126 LEU   A CG   1 
ATOM   2605 C  CD1  A LEU   A 1 126 ? 13.160 -6.946  0.868   0.64 13.58 ?  126 LEU   A CD1  1 
ATOM   2606 C  CD1  B LEU   A 1 126 ? 14.941 -8.197  0.642   0.36 17.61 ?  126 LEU   A CD1  1 
ATOM   2607 C  CD2  A LEU   A 1 126 ? 15.055 -8.539  1.256   0.64 12.56 ?  126 LEU   A CD2  1 
ATOM   2608 C  CD2  B LEU   A 1 126 ? 13.296 -6.583  -0.306  0.36 17.33 ?  126 LEU   A CD2  1 
ATOM   2609 H  H    A LEU   A 1 126 ? 16.190 -4.804  2.431   0.64 13.18 ?  126 LEU   A H    1 
ATOM   2610 H  H    B LEU   A 1 126 ? 16.311 -4.336  2.578   0.36 15.53 ?  126 LEU   A H    1 
ATOM   2611 H  HA   A LEU   A 1 126 ? 17.259 -6.948  1.321   0.64 13.77 ?  126 LEU   A HA   1 
ATOM   2612 H  HA   B LEU   A 1 126 ? 17.033 -6.669  1.492   0.36 16.29 ?  126 LEU   A HA   1 
ATOM   2613 H  HB2  A LEU   A 1 126 ? 15.118 -5.298  0.526   0.64 14.16 ?  126 LEU   A HB2  1 
ATOM   2614 H  HB2  B LEU   A 1 126 ? 14.777 -5.676  1.626   0.36 18.85 ?  126 LEU   A HB2  1 
ATOM   2615 H  HB3  A LEU   A 1 126 ? 15.573 -6.536  -0.354  0.64 14.16 ?  126 LEU   A HB3  1 
ATOM   2616 H  HB3  B LEU   A 1 126 ? 15.205 -4.897  0.325   0.36 18.85 ?  126 LEU   A HB3  1 
ATOM   2617 H  HG   A LEU   A 1 126 ? 14.619 -6.827  2.281   0.64 14.98 ?  126 LEU   A HG   1 
ATOM   2618 H  HG   B LEU   A 1 126 ? 15.235 -6.861  -0.878  0.36 20.62 ?  126 LEU   A HG   1 
ATOM   2619 H  HD11 A LEU   A 1 126 ? 12.589 -7.535  1.390   0.64 16.28 ?  126 LEU   A HD11 1 
ATOM   2620 H  HD11 B LEU   A 1 126 ? 14.445 -8.863  0.142   0.36 21.11 ?  126 LEU   A HD11 1 
ATOM   2621 H  HD12 A LEU   A 1 126 ? 12.876 -6.027  0.979   0.64 16.28 ?  126 LEU   A HD12 1 
ATOM   2622 H  HD12 B LEU   A 1 126 ? 15.883 -8.425  0.652   0.36 21.11 ?  126 LEU   A HD12 1 
ATOM   2623 H  HD13 A LEU   A 1 126 ? 13.114 -7.196  -0.071  0.64 16.28 ?  126 LEU   A HD13 1 
ATOM   2624 H  HD13 B LEU   A 1 126 ? 14.601 -8.143  1.549   0.36 21.11 ?  126 LEU   A HD13 1 
ATOM   2625 H  HD21 A LEU   A 1 126 ? 14.362 -9.116  1.616   0.64 15.05 ?  126 LEU   A HD21 1 
ATOM   2626 H  HD21 B LEU   A 1 126 ? 12.944 -7.302  -0.853  0.36 20.78 ?  126 LEU   A HD21 1 
ATOM   2627 H  HD22 A LEU   A 1 126 ? 15.215 -8.760  0.324   0.64 15.05 ?  126 LEU   A HD22 1 
ATOM   2628 H  HD22 B LEU   A 1 126 ? 12.820 -6.546  0.539   0.36 20.78 ?  126 LEU   A HD22 1 
ATOM   2629 H  HD23 A LEU   A 1 126 ? 15.871 -8.645  1.766   0.64 15.05 ?  126 LEU   A HD23 1 
ATOM   2630 H  HD23 B LEU   A 1 126 ? 13.208 -5.737  -0.772  0.36 20.78 ?  126 LEU   A HD23 1 
ATOM   2631 N  N    A LEU   A 1 127 ? 18.895 -6.187  -0.309  0.64 11.14 ?  127 LEU   A N    1 
ATOM   2632 N  N    B LEU   A 1 127 ? 18.815 -5.910  -0.059  0.36 11.97 ?  127 LEU   A N    1 
ATOM   2633 C  CA   A LEU   A 1 127 ? 19.894 -5.681  -1.239  0.64 11.28 ?  127 LEU   A CA   1 
ATOM   2634 C  CA   B LEU   A 1 127 ? 19.798 -5.406  -1.011  0.36 11.77 ?  127 LEU   A CA   1 
ATOM   2635 C  C    A LEU   A 1 127 ? 19.295 -5.497  -2.623  0.64 10.86 ?  127 LEU   A C    1 
ATOM   2636 C  C    B LEU   A 1 127 ? 19.209 -5.316  -2.411  0.36 11.67 ?  127 LEU   A C    1 
ATOM   2637 O  O    A LEU   A 1 127 ? 18.467 -6.292  -3.078  0.64 10.92 ?  127 LEU   A O    1 
ATOM   2638 O  O    B LEU   A 1 127 ? 18.387 -6.142  -2.819  0.36 12.11 ?  127 LEU   A O    1 
ATOM   2639 C  CB   A LEU   A 1 127 ? 21.065 -6.658  -1.325  0.64 12.04 ?  127 LEU   A CB   1 
ATOM   2640 C  CB   B LEU   A 1 127 ? 21.040 -6.300  -1.042  0.36 12.08 ?  127 LEU   A CB   1 
ATOM   2641 C  CG   A LEU   A 1 127 ? 21.842 -6.901  -0.032  0.64 12.26 ?  127 LEU   A CG   1 
ATOM   2642 C  CG   B LEU   A 1 127 ? 21.888 -6.324  0.231   0.36 12.04 ?  127 LEU   A CG   1 
ATOM   2643 C  CD1  A LEU   A 1 127 ? 22.944 -7.901  -0.296  0.64 12.78 ?  127 LEU   A CD1  1 
ATOM   2644 C  CD1  B LEU   A 1 127 ? 23.040 -7.301  0.086   0.36 12.30 ?  127 LEU   A CD1  1 
ATOM   2645 C  CD2  A LEU   A 1 127 ? 22.418 -5.611  0.507   0.64 12.95 ?  127 LEU   A CD2  1 
ATOM   2646 C  CD2  B LEU   A 1 127 ? 22.406 -4.930  0.577   0.36 12.51 ?  127 LEU   A CD2  1 
ATOM   2647 H  H    A LEU   A 1 127 ? 19.038 -6.996  -0.038  0.64 13.35 ?  127 LEU   A H    1 
ATOM   2648 H  H    B LEU   A 1 127 ? 19.027 -6.660  0.312   0.36 14.35 ?  127 LEU   A H    1 
ATOM   2649 H  HA   A LEU   A 1 127 ? 20.229 -4.829  -0.918  0.64 13.52 ?  127 LEU   A HA   1 
ATOM   2650 H  HA   B LEU   A 1 127 ? 20.072 -4.516  -0.744  0.36 14.11 ?  127 LEU   A HA   1 
ATOM   2651 H  HB2  A LEU   A 1 127 ? 20.724 -7.517  -1.620  0.64 14.43 ?  127 LEU   A HB2  1 
ATOM   2652 H  HB2  B LEU   A 1 127 ? 20.755 -7.210  -1.222  0.36 14.48 ?  127 LEU   A HB2  1 
ATOM   2653 H  HB3  A LEU   A 1 127 ? 21.696 -6.320  -1.976  0.64 14.43 ?  127 LEU   A HB3  1 
ATOM   2654 H  HB3  B LEU   A 1 127 ? 21.611 -5.996  -1.769  0.36 14.48 ?  127 LEU   A HB3  1 
ATOM   2655 H  HG   A LEU   A 1 127 ? 21.244 -7.279  0.638   0.64 14.69 ?  127 LEU   A HG   1 
ATOM   2656 H  HG   B LEU   A 1 127 ? 21.333 -6.625  0.965   0.36 14.43 ?  127 LEU   A HG   1 
ATOM   2657 H  HD11 A LEU   A 1 127 ? 23.410 -8.085  0.536   0.64 15.32 ?  127 LEU   A HD11 1 
ATOM   2658 H  HD11 B LEU   A 1 127 ? 23.581 -7.266  0.889   0.36 14.74 ?  127 LEU   A HD11 1 
ATOM   2659 H  HD12 A LEU   A 1 127 ? 22.553 -8.722  -0.641  0.64 15.32 ?  127 LEU   A HD12 1 
ATOM   2660 H  HD12 B LEU   A 1 127 ? 22.680 -8.194  -0.035  0.36 14.74 ?  127 LEU   A HD12 1 
ATOM   2661 H  HD13 A LEU   A 1 127 ? 23.557 -7.529  -0.946  0.64 15.32 ?  127 LEU   A HD13 1 
ATOM   2662 H  HD13 B LEU   A 1 127 ? 23.571 -7.049  -0.685  0.36 14.74 ?  127 LEU   A HD13 1 
ATOM   2663 H  HD21 A LEU   A 1 127 ? 23.018 -5.819  1.240   0.64 15.52 ?  127 LEU   A HD21 1 
ATOM   2664 H  HD21 B LEU   A 1 127 ? 23.052 -5.004  1.297   0.36 15.00 ?  127 LEU   A HD21 1 
ATOM   2665 H  HD22 A LEU   A 1 127 ? 22.907 -5.170  -0.205  0.64 15.52 ?  127 LEU   A HD22 1 
ATOM   2666 H  HD22 B LEU   A 1 127 ? 22.828 -4.544  -0.207  0.36 15.00 ?  127 LEU   A HD22 1 
ATOM   2667 H  HD23 A LEU   A 1 127 ? 21.695 -5.048  0.815   0.64 15.52 ?  127 LEU   A HD23 1 
ATOM   2668 H  HD23 B LEU   A 1 127 ? 21.661 -4.375  0.858   0.36 15.00 ?  127 LEU   A HD23 1 
ATOM   2669 N  N    A SER   A 1 128 ? 19.730 -4.439  -3.294  0.64 11.07 ?  128 SER   A N    1 
ATOM   2670 N  N    B SER   A 1 128 ? 19.641 -4.290  -3.140  0.36 11.19 ?  128 SER   A N    1 
ATOM   2671 C  CA   A SER   A 1 128 ? 19.319 -4.069  -4.639  0.64 11.59 ?  128 SER   A CA   1 
ATOM   2672 C  CA   B SER   A 1 128 ? 19.296 -3.985  -4.524  0.36 11.27 ?  128 SER   A CA   1 
ATOM   2673 C  C    A SER   A 1 128 ? 17.861 -3.618  -4.724  0.64 12.09 ?  128 SER   A C    1 
ATOM   2674 C  C    B SER   A 1 128 ? 17.848 -3.556  -4.727  0.36 11.19 ?  128 SER   A C    1 
ATOM   2675 O  O    A SER   A 1 128 ? 17.393 -3.326  -5.824  0.64 13.34 ?  128 SER   A O    1 
ATOM   2676 O  O    B SER   A 1 128 ? 17.484 -3.211  -5.855  0.36 11.62 ?  128 SER   A O    1 
ATOM   2677 C  CB   A SER   A 1 128 ? 19.640 -5.142  -5.692  0.64 12.19 ?  128 SER   A CB   1 
ATOM   2678 C  CB   B SER   A 1 128 ? 19.675 -5.095  -5.514  0.36 11.14 ?  128 SER   A CB   1 
ATOM   2679 O  OG   A SER   A 1 128 ? 21.039 -5.387  -5.743  0.64 12.87 ?  128 SER   A OG   1 
ATOM   2680 O  OG   B SER   A 1 128 ? 21.085 -5.193  -5.625  0.36 11.40 ?  128 SER   A OG   1 
ATOM   2681 H  H    A SER   A 1 128 ? 20.323 -3.897  -2.971  0.64 13.26 ?  128 SER   A H    1 
ATOM   2682 H  H    B SER   A 1 128 ? 20.190 -3.711  -2.821  0.36 13.41 ?  128 SER   A H    1 
ATOM   2683 H  HA   A SER   A 1 128 ? 19.847 -3.300  -4.881  0.64 13.89 ?  128 SER   A HA   1 
ATOM   2684 H  HA   B SER   A 1 128 ? 19.821 -3.215  -4.775  0.36 13.51 ?  128 SER   A HA   1 
ATOM   2685 H  HB2  A SER   A 1 128 ? 19.179 -5.962  -5.466  0.64 14.62 ?  128 SER   A HB2  1 
ATOM   2686 H  HB2  B SER   A 1 128 ? 19.314 -5.935  -5.201  0.36 13.35 ?  128 SER   A HB2  1 
ATOM   2687 H  HB3  A SER   A 1 128 ? 19.348 -4.823  -6.563  0.64 14.62 ?  128 SER   A HB3  1 
ATOM   2688 H  HB3  B SER   A 1 128 ? 19.301 -4.875  -6.387  0.36 13.35 ?  128 SER   A HB3  1 
ATOM   2689 H  HG   A SER   A 1 128 ? 21.449 -4.673  -5.922  0.64 15.42 ?  128 SER   A HG   1 
ATOM   2690 H  HG   B SER   A 1 128 ? 21.398 -4.457  -5.886  0.36 13.66 ?  128 SER   A HG   1 
ATOM   2691 N  N    A ALA   A 1 129 ? 17.140 -3.540  -3.602  0.64 12.77 ?  129 ALA   A N    1 
ATOM   2692 N  N    B ALA   A 1 129 ? 17.022 -3.546  -3.683  0.36 11.75 ?  129 ALA   A N    1 
ATOM   2693 C  CA   A ALA   A 1 129 ? 15.766 -3.052  -3.581  0.64 12.81 ?  129 ALA   A CA   1 
ATOM   2694 C  CA   B ALA   A 1 129 ? 15.652 -3.069  -3.805  0.36 12.16 ?  129 ALA   A CA   1 
ATOM   2695 C  C    A ALA   A 1 129 ? 15.769 -1.525  -3.510  0.64 12.31 ?  129 ALA   A C    1 
ATOM   2696 C  C    B ALA   A 1 129 ? 15.626 -1.543  -3.745  0.36 12.31 ?  129 ALA   A C    1 
ATOM   2697 O  O    A ALA   A 1 129 ? 16.819 -0.877  -3.569  0.64 12.75 ?  129 ALA   A O    1 
ATOM   2698 O  O    B ALA   A 1 129 ? 16.662 -0.872  -3.712  0.36 12.73 ?  129 ALA   A O    1 
ATOM   2699 C  CB   A ALA   A 1 129 ? 14.998 -3.685  -2.422  0.64 13.75 ?  129 ALA   A CB   1 
ATOM   2700 C  CB   B ALA   A 1 129 ? 14.765 -3.728  -2.750  0.36 12.76 ?  129 ALA   A CB   1 
ATOM   2701 H  H    A ALA   A 1 129 ? 17.435 -3.766  -2.824  0.64 15.31 ?  129 ALA   A H    1 
ATOM   2702 H  H    B ALA   A 1 129 ? 17.231 -3.819  -2.888  0.36 14.08 ?  129 ALA   A H    1 
ATOM   2703 H  HA   A ALA   A 1 129 ? 15.332 -3.316  -4.405  0.64 15.36 ?  129 ALA   A HA   1 
ATOM   2704 H  HA   B ALA   A 1 129 ? 15.316 -3.313  -4.674  0.36 14.58 ?  129 ALA   A HA   1 
ATOM   2705 H  HB1  A ALA   A 1 129 ? 14.085 -3.352  -2.431  0.64 16.48 ?  129 ALA   A HB1  1 
ATOM   2706 H  HB1  B ALA   A 1 129 ? 13.905 -3.280  -2.737  0.36 15.30 ?  129 ALA   A HB1  1 
ATOM   2707 H  HB2  A ALA   A 1 129 ? 15.000 -4.647  -2.531  0.64 16.48 ?  129 ALA   A HB2  1 
ATOM   2708 H  HB2  B ALA   A 1 129 ? 14.649 -4.660  -2.977  0.36 15.30 ?  129 ALA   A HB2  1 
ATOM   2709 H  HB3  A ALA   A 1 129 ? 15.429 -3.443  -1.587  0.64 16.48 ?  129 ALA   A HB3  1 
ATOM   2710 H  HB3  B ALA   A 1 129 ? 15.187 -3.651  -1.878  0.36 15.30 ?  129 ALA   A HB3  1 
ATOM   2711 N  N    A GLY   A 1 130 ? 14.584 -0.933  -3.383  0.64 12.41 ?  130 GLY   A N    1 
ATOM   2712 N  N    B GLY   A 1 130 ? 14.420 -0.984  -3.733  0.36 12.22 ?  130 GLY   A N    1 
ATOM   2713 C  CA   A GLY   A 1 130 ? 14.507 0.517   -3.332  0.64 12.75 ?  130 GLY   A CA   1 
ATOM   2714 C  CA   B GLY   A 1 130 ? 14.269 0.457   -3.650  0.36 12.61 ?  130 GLY   A CA   1 
ATOM   2715 C  C    A GLY   A 1 130 ? 15.063 1.134   -4.601  0.64 13.20 ?  130 GLY   A C    1 
ATOM   2716 C  C    B GLY   A 1 130 ? 15.015 1.157   -4.766  0.36 13.19 ?  130 GLY   A C    1 
ATOM   2717 O  O    A GLY   A 1 130 ? 14.743 0.703   -5.714  0.64 12.81 ?  130 GLY   A O    1 
ATOM   2718 O  O    B GLY   A 1 130 ? 14.983 0.737   -5.928  0.36 13.59 ?  130 GLY   A O    1 
ATOM   2719 H  H    A GLY   A 1 130 ? 13.828 -1.339  -3.327  0.64 14.88 ?  130 GLY   A H    1 
ATOM   2720 H  H    B GLY   A 1 130 ? 13.685 -1.426  -3.772  0.36 14.65 ?  130 GLY   A H    1 
ATOM   2721 H  HA2  A GLY   A 1 130 ? 13.581 0.794   -3.226  0.64 15.29 ?  130 GLY   A HA2  1 
ATOM   2722 H  HA2  B GLY   A 1 130 ? 13.325 0.681   -3.705  0.36 15.11 ?  130 GLY   A HA2  1 
ATOM   2723 H  HA3  A GLY   A 1 130 ? 15.019 0.847   -2.582  0.64 15.29 ?  130 GLY   A HA3  1 
ATOM   2724 H  HA3  B GLY   A 1 130 ? 14.612 0.778   -2.802  0.36 15.11 ?  130 GLY   A HA3  1 
ATOM   2725 N  N    A ILE   A 1 131 ? 15.905 2.162   -4.437  0.64 13.75 ?  131 ILE   A N    1 
ATOM   2726 N  N    B ILE   A 1 131 ? 15.717 2.237   -4.406  0.36 13.64 ?  131 ILE   A N    1 
ATOM   2727 C  CA   A ILE   A 1 131 ? 16.423 2.930   -5.569  0.64 13.71 ?  131 ILE   A CA   1 
ATOM   2728 C  CA   B ILE   A 1 131 ? 16.386 3.073   -5.400  0.36 13.76 ?  131 ILE   A CA   1 
ATOM   2729 C  C    A ILE   A 1 131 ? 17.482 2.174   -6.371  0.64 13.33 ?  131 ILE   A C    1 
ATOM   2730 C  C    B ILE   A 1 131 ? 17.362 2.292   -6.271  0.36 13.38 ?  131 ILE   A C    1 
ATOM   2731 O  O    A ILE   A 1 131 ? 17.934 2.670   -7.409  0.64 14.19 ?  131 ILE   A O    1 
ATOM   2732 O  O    B ILE   A 1 131 ? 17.768 2.786   -7.329  0.36 13.54 ?  131 ILE   A O    1 
ATOM   2733 C  CB   A ILE   A 1 131 ? 16.928 4.327   -5.149  0.64 14.68 ?  131 ILE   A CB   1 
ATOM   2734 C  CB   B ILE   A 1 131 ? 17.067 4.314   -4.771  0.36 14.80 ?  131 ILE   A CB   1 
ATOM   2735 C  CG1  A ILE   A 1 131 ? 18.167 4.223   -4.251  0.64 15.99 ?  131 ILE   A CG1  1 
ATOM   2736 C  CG1  B ILE   A 1 131 ? 18.290 3.926   -3.933  0.36 15.77 ?  131 ILE   A CG1  1 
ATOM   2737 C  CG2  A ILE   A 1 131 ? 15.811 5.122   -4.467  0.64 14.99 ?  131 ILE   A CG2  1 
ATOM   2738 C  CG2  B ILE   A 1 131 ? 16.076 5.115   -3.938  0.36 15.14 ?  131 ILE   A CG2  1 
ATOM   2739 C  CD1  A ILE   A 1 131 ? 18.767 5.572   -3.862  0.64 16.80 ?  131 ILE   A CD1  1 
ATOM   2740 C  CD1  B ILE   A 1 131 ? 19.067 5.135   -3.419  0.36 16.26 ?  131 ILE   A CD1  1 
ATOM   2741 H  H    A ILE   A 1 131 ? 16.167 2.455   -3.670  0.64 16.49 ?  131 ILE   A H    1 
ATOM   2742 H  H    B ILE   A 1 131 ? 15.799 2.506   -3.596  0.36 16.35 ?  131 ILE   A H    1 
ATOM   2743 H  HA   A ILE   A 1 131 ? 15.691 3.076   -6.182  0.64 16.44 ?  131 ILE   A HA   1 
ATOM   2744 H  HA   B ILE   A 1 131 ? 15.709 3.412   -5.994  0.36 16.49 ?  131 ILE   A HA   1 
ATOM   2745 H  HB   A ILE   A 1 131 ? 17.182 4.803   -5.955  0.64 17.60 ?  131 ILE   A HB   1 
ATOM   2746 H  HB   B ILE   A 1 131 ? 17.366 4.884   -5.494  0.36 17.74 ?  131 ILE   A HB   1 
ATOM   2747 H  HG12 A ILE   A 1 131 ? 17.923 3.757   -3.437  0.64 19.17 ?  131 ILE   A HG12 1 
ATOM   2748 H  HG12 B ILE   A 1 131 ? 17.998 3.411   -3.168  0.36 18.90 ?  131 ILE   A HG12 1 
ATOM   2749 H  HG13 A ILE   A 1 131 ? 18.855 3.721   -4.721  0.64 19.17 ?  131 ILE   A HG13 1 
ATOM   2750 H  HG13 B ILE   A 1 131 ? 18.896 3.401   -4.477  0.36 18.90 ?  131 ILE   A HG13 1 
ATOM   2751 H  HG21 A ILE   A 1 131 ? 16.099 6.040   -4.353  0.64 17.97 ?  131 ILE   A HG21 1 
ATOM   2752 H  HG21 B ILE   A 1 131 ? 16.469 5.974   -3.718  0.36 18.15 ?  131 ILE   A HG21 1 
ATOM   2753 H  HG22 A ILE   A 1 131 ? 15.017 5.091   -5.024  0.64 17.97 ?  131 ILE   A HG22 1 
ATOM   2754 H  HG22 B ILE   A 1 131 ? 15.266 5.247   -4.456  0.36 18.15 ?  131 ILE   A HG22 1 
ATOM   2755 H  HG23 A ILE   A 1 131 ? 15.622 4.722   -3.603  0.64 17.97 ?  131 ILE   A HG23 1 
ATOM   2756 H  HG23 B ILE   A 1 131 ? 15.873 4.624   -3.128  0.36 18.15 ?  131 ILE   A HG23 1 
ATOM   2757 H  HD11 A ILE   A 1 131 ? 19.604 5.421   -3.396  0.64 20.14 ?  131 ILE   A HD11 1 
ATOM   2758 H  HD11 B ILE   A 1 131 ? 19.894 4.832   -3.016  0.36 19.49 ?  131 ILE   A HD11 1 
ATOM   2759 H  HD12 A ILE   A 1 131 ? 18.926 6.090   -4.667  0.64 20.14 ?  131 ILE   A HD12 1 
ATOM   2760 H  HD12 B ILE   A 1 131 ? 19.261 5.728   -4.165  0.36 19.49 ?  131 ILE   A HD12 1 
ATOM   2761 H  HD13 A ILE   A 1 131 ? 18.144 6.039   -3.285  0.64 20.14 ?  131 ILE   A HD13 1 
ATOM   2762 H  HD13 B ILE   A 1 131 ? 18.529 5.603   -2.760  0.36 19.49 ?  131 ILE   A HD13 1 
ATOM   2763 N  N    A PHE   A 1 132 ? 17.888 0.977   -5.916  0.64 12.91 ?  132 PHE   A N    1 
ATOM   2764 N  N    B PHE   A 1 132 ? 17.755 1.083   -5.861  0.36 13.53 ?  132 PHE   A N    1 
ATOM   2765 C  CA   A PHE   A 1 132 ? 18.751 0.132   -6.740  0.64 13.07 ?  132 PHE   A CA   1 
ATOM   2766 C  CA   B PHE   A 1 132 ? 18.684 0.302   -6.670  0.36 13.69 ?  132 PHE   A CA   1 
ATOM   2767 C  C    A PHE   A 1 132 ? 17.971 -0.630  -7.812  0.64 13.51 ?  132 PHE   A C    1 
ATOM   2768 C  C    B PHE   A 1 132 ? 18.008 -0.409  -7.843  0.36 14.23 ?  132 PHE   A C    1 
ATOM   2769 O  O    A PHE   A 1 132 ? 18.590 -1.294  -8.649  0.64 13.89 ?  132 PHE   A O    1 
ATOM   2770 O  O    B PHE   A 1 132 ? 18.704 -0.854  -8.761  0.36 14.38 ?  132 PHE   A O    1 
ATOM   2771 C  CB   A PHE   A 1 132 ? 19.565 -0.852  -5.885  0.64 12.76 ?  132 PHE   A CB   1 
ATOM   2772 C  CB   B PHE   A 1 132 ? 19.464 -0.688  -5.800  0.36 13.23 ?  132 PHE   A CB   1 
ATOM   2773 C  CG   A PHE   A 1 132 ? 20.789 -0.250  -5.220  0.64 12.59 ?  132 PHE   A CG   1 
ATOM   2774 C  CG   B PHE   A 1 132 ? 20.693 -0.101  -5.143  0.36 13.09 ?  132 PHE   A CG   1 
ATOM   2775 C  CD1  A PHE   A 1 132 ? 20.672 0.794   -4.319  0.64 13.35 ?  132 PHE   A CD1  1 
ATOM   2776 C  CD1  B PHE   A 1 132 ? 20.582 0.882   -4.173  0.36 13.64 ?  132 PHE   A CD1  1 
ATOM   2777 C  CD2  A PHE   A 1 132 ? 22.049 -0.778  -5.460  0.64 13.17 ?  132 PHE   A CD2  1 
ATOM   2778 C  CD2  B PHE   A 1 132 ? 21.957 -0.560  -5.479  0.36 13.10 ?  132 PHE   A CD2  1 
ATOM   2779 C  CE1  A PHE   A 1 132 ? 21.795 1.323   -3.695  0.64 13.79 ?  132 PHE   A CE1  1 
ATOM   2780 C  CE1  B PHE   A 1 132 ? 21.710 1.408   -3.563  0.36 13.95 ?  132 PHE   A CE1  1 
ATOM   2781 C  CE2  A PHE   A 1 132 ? 23.171 -0.257  -4.837  0.64 13.50 ?  132 PHE   A CE2  1 
ATOM   2782 C  CE2  B PHE   A 1 132 ? 23.088 -0.040  -4.871  0.36 13.54 ?  132 PHE   A CE2  1 
ATOM   2783 C  CZ   A PHE   A 1 132 ? 23.042 0.797   -3.953  0.64 13.44 ?  132 PHE   A CZ   1 
ATOM   2784 C  CZ   B PHE   A 1 132 ? 22.962 0.947   -3.912  0.36 13.69 ?  132 PHE   A CZ   1 
ATOM   2785 H  H    A PHE   A 1 132 ? 17.692 0.636   -5.150  0.64 15.48 ?  132 PHE   A H    1 
ATOM   2786 H  H    B PHE   A 1 132 ? 17.503 0.710   -5.125  0.36 16.21 ?  132 PHE   A H    1 
ATOM   2787 H  HA   A PHE   A 1 132 ? 19.391 0.702   -7.194  0.64 15.67 ?  132 PHE   A HA   1 
ATOM   2788 H  HA   B PHE   A 1 132 ? 19.329 0.919   -7.044  0.36 16.41 ?  132 PHE   A HA   1 
ATOM   2789 H  HB2  A PHE   A 1 132 ? 18.995 -1.201  -5.183  0.64 15.30 ?  132 PHE   A HB2  1 
ATOM   2790 H  HB2  B PHE   A 1 132 ? 18.883 -1.012  -5.096  0.36 15.86 ?  132 PHE   A HB2  1 
ATOM   2791 H  HB3  A PHE   A 1 132 ? 19.869 -1.585  -6.451  0.64 15.30 ?  132 PHE   A HB3  1 
ATOM   2792 H  HB3  B PHE   A 1 132 ? 19.752 -1.425  -6.358  0.36 15.86 ?  132 PHE   A HB3  1 
ATOM   2793 H  HD1  A PHE   A 1 132 ? 19.837 1.152   -4.135  0.64 16.01 ?  132 PHE   A HD1  1 
ATOM   2794 H  HD1  B PHE   A 1 132 ? 19.742 1.199   -3.933  0.36 16.36 ?  132 PHE   A HD1  1 
ATOM   2795 H  HD2  A PHE   A 1 132 ? 22.149 -1.490  -6.055  0.64 15.79 ?  132 PHE   A HD2  1 
ATOM   2796 H  HD2  B PHE   A 1 132 ? 22.049 -1.224  -6.125  0.36 15.70 ?  132 PHE   A HD2  1 
ATOM   2797 H  HE1  A PHE   A 1 132 ? 21.710 2.033   -3.097  0.64 16.53 ?  132 PHE   A HE1  1 
ATOM   2798 H  HE1  B PHE   A 1 132 ? 21.625 2.072   -2.917  0.36 16.72 ?  132 PHE   A HE1  1 
ATOM   2799 H  HE2  A PHE   A 1 132 ? 24.014 -0.613  -5.020  0.64 16.18 ?  132 PHE   A HE2  1 
ATOM   2800 H  HE2  B PHE   A 1 132 ? 23.932 -0.354  -5.111  0.36 16.23 ?  132 PHE   A HE2  1 
ATOM   2801 H  HZ   A PHE   A 1 132 ? 23.798 1.154   -3.538  0.64 16.11 ?  132 PHE   A HZ   1 
ATOM   2802 H  HZ   B PHE   A 1 132 ? 23.722 1.298   -3.505  0.36 16.41 ?  132 PHE   A HZ   1 
ATOM   2803 N  N    A GLY   A 1 133 ? 16.639 -0.565  -7.799  0.64 13.90 ?  133 GLY   A N    1 
ATOM   2804 N  N    B GLY   A 1 133 ? 16.679 -0.534  -7.842  0.36 14.61 ?  133 GLY   A N    1 
ATOM   2805 C  CA   A GLY   A 1 133 ? 15.830 -0.925  -8.947  0.64 14.66 ?  133 GLY   A CA   1 
ATOM   2806 C  CA   B GLY   A 1 133 ? 15.947 -0.886  -9.042  0.36 15.24 ?  133 GLY   A CA   1 
ATOM   2807 C  C    A GLY   A 1 133 ? 15.497 -2.389  -9.139  0.64 15.00 ?  133 GLY   A C    1 
ATOM   2808 C  C    B GLY   A 1 133 ? 15.563 -2.343  -9.209  0.36 15.67 ?  133 GLY   A C    1 
ATOM   2809 O  O    A GLY   A 1 133 ? 14.881 -2.719  -10.158 0.64 16.48 ?  133 GLY   A O    1 
ATOM   2810 O  O    B GLY   A 1 133 ? 14.779 -2.645  -10.116 0.36 16.34 ?  133 GLY   A O    1 
ATOM   2811 H  H    A GLY   A 1 133 ? 16.179 -0.314  -7.118  0.64 16.67 ?  133 GLY   A H    1 
ATOM   2812 H  H    B GLY   A 1 133 ? 16.178 -0.413  -7.151  0.36 17.52 ?  133 GLY   A H    1 
ATOM   2813 H  HA2  A GLY   A 1 133 ? 14.990 -0.443  -8.895  0.64 17.57 ?  133 GLY   A HA2  1 
ATOM   2814 H  HA2  B GLY   A 1 133 ? 15.124 -0.382  -9.062  0.36 18.28 ?  133 GLY   A HA2  1 
ATOM   2815 H  HA3  A GLY   A 1 133 ? 16.285 -0.639  -9.752  0.64 17.57 ?  133 GLY   A HA3  1 
ATOM   2816 H  HA3  B GLY   A 1 133 ? 16.476 -0.626  -9.814  0.36 18.28 ?  133 GLY   A HA3  1 
ATOM   2817 N  N    A ALA   A 1 134 ? 15.872 -3.278  -8.220  0.64 14.00 ?  134 ALA   A N    1 
ATOM   2818 N  N    B ALA   A 1 134 ? 16.070 -3.251  -8.378  0.36 15.48 ?  134 ALA   A N    1 
ATOM   2819 C  CA   A ALA   A 1 134 ? 15.505 -4.677  -8.372  0.64 14.07 ?  134 ALA   A CA   1 
ATOM   2820 C  CA   B ALA   A 1 134 ? 15.776 -4.662  -8.574  0.36 15.79 ?  134 ALA   A CA   1 
ATOM   2821 C  C    A ALA   A 1 134 ? 14.159 -4.963  -7.708  0.64 14.22 ?  134 ALA   A C    1 
ATOM   2822 C  C    B ALA   A 1 134 ? 14.423 -5.027  -7.970  0.36 15.89 ?  134 ALA   A C    1 
ATOM   2823 O  O    A ALA   A 1 134 ? 13.634 -4.170  -6.923  0.64 15.50 ?  134 ALA   A O    1 
ATOM   2824 O  O    B ALA   A 1 134 ? 13.856 -4.295  -7.155  0.36 16.55 ?  134 ALA   A O    1 
ATOM   2825 C  CB   A ALA   A 1 134 ? 16.583 -5.596  -7.802  0.64 14.78 ?  134 ALA   A CB   1 
ATOM   2826 C  CB   B ALA   A 1 134 ? 16.867 -5.534  -7.954  0.36 16.32 ?  134 ALA   A CB   1 
ATOM   2827 H  H    A ALA   A 1 134 ? 16.336 -3.094  -7.513  0.64 16.79 ?  134 ALA   A H    1 
ATOM   2828 H  H    B ALA   A 1 134 ? 16.574 -3.076  -7.703  0.36 18.56 ?  134 ALA   A H    1 
ATOM   2829 H  HA   A ALA   A 1 134 ? 15.416 -4.871  -9.316  0.64 16.87 ?  134 ALA   A HA   1 
ATOM   2830 H  HA   B ALA   A 1 134 ? 15.742 -4.849  -9.524  0.36 18.93 ?  134 ALA   A HA   1 
ATOM   2831 H  HB1  A ALA   A 1 134 ? 16.316 -6.516  -7.949  0.64 17.72 ?  134 ALA   A HB1  1 
ATOM   2832 H  HB1  B ALA   A 1 134 ? 16.649 -6.466  -8.109  0.36 19.56 ?  134 ALA   A HB1  1 
ATOM   2833 H  HB2  A ALA   A 1 134 ? 17.418 -5.415  -8.261  0.64 17.72 ?  134 ALA   A HB2  1 
ATOM   2834 H  HB2  B ALA   A 1 134 ? 17.715 -5.318  -8.371  0.36 19.56 ?  134 ALA   A HB2  1 
ATOM   2835 H  HB3  A ALA   A 1 134 ? 16.677 -5.422  -6.855  0.64 17.72 ?  134 ALA   A HB3  1 
ATOM   2836 H  HB3  B ALA   A 1 134 ? 16.910 -5.356  -7.002  0.36 19.56 ?  134 ALA   A HB3  1 
ATOM   2837 N  N    A ASP   A 1 135 ? 13.600 -6.121  -8.048  0.64 14.43 ?  135 ASP   A N    1 
ATOM   2838 N  N    B ASP   A 1 135 ? 13.912 -6.183  -8.380  0.36 15.96 ?  135 ASP   A N    1 
ATOM   2839 C  CA   A ASP   A 1 135 ? 12.347 -6.587  -7.461  0.64 15.52 ?  135 ASP   A CA   1 
ATOM   2840 C  CA   B ASP   A 1 135 ? 12.641 -6.682  -7.867  0.36 16.43 ?  135 ASP   A CA   1 
ATOM   2841 C  C    A ASP   A 1 135 ? 12.606 -7.038  -6.028  0.64 14.84 ?  135 ASP   A C    1 
ATOM   2842 C  C    B ASP   A 1 135 ? 12.817 -7.102  -6.414  0.36 15.85 ?  135 ASP   A C    1 
ATOM   2843 O  O    A ASP   A 1 135 ? 13.398 -7.966  -5.817  0.64 14.86 ?  135 ASP   A O    1 
ATOM   2844 O  O    B ASP   A 1 135 ? 13.580 -8.037  -6.138  0.36 15.73 ?  135 ASP   A O    1 
ATOM   2845 C  CB   A ASP   A 1 135 ? 11.835 -7.763  -8.292  0.64 18.00 ?  135 ASP   A CB   1 
ATOM   2846 C  CB   B ASP   A 1 135 ? 12.186 -7.875  -8.700  0.36 18.15 ?  135 ASP   A CB   1 
ATOM   2847 C  CG   A ASP   A 1 135 ? 10.523 -8.343  -7.772  0.64 20.31 ?  135 ASP   A CG   1 
ATOM   2848 C  CG   B ASP   A 1 135 ? 10.968 -8.576  -8.116  0.36 19.82 ?  135 ASP   A CG   1 
ATOM   2849 O  OD1  A ASP   A 1 135 ? 10.038 -7.907  -6.704  0.64 20.72 ?  135 ASP   A OD1  1 
ATOM   2850 O  OD1  B ASP   A 1 135 ? 10.186 -7.930  -7.388  0.36 20.58 ?  135 ASP   A OD1  1 
ATOM   2851 O  OD2  A ASP   A 1 135 ? 9.965  -9.228  -8.458  0.64 22.42 -1 135 ASP   A OD2  1 
ATOM   2852 O  OD2  B ASP   A 1 135 ? 10.804 -9.787  -8.379  0.36 20.78 -1 135 ASP   A OD2  1 
ATOM   2853 H  H    A ASP   A 1 135 ? 13.926 -6.661  -8.629  0.64 17.30 ?  135 ASP   A H    1 
ATOM   2854 H  H    B ASP   A 1 135 ? 14.284 -6.700  -8.954  0.36 19.13 ?  135 ASP   A H    1 
ATOM   2855 H  HA   A ASP   A 1 135 ? 11.680 -5.875  -7.486  0.64 18.61 ?  135 ASP   A HA   1 
ATOM   2856 H  HA   B ASP   A 1 135 ? 11.972 -5.984  -7.933  0.36 19.70 ?  135 ASP   A HA   1 
ATOM   2857 H  HB2  A ASP   A 1 135 ? 11.677 -7.465  -9.200  0.64 21.59 ?  135 ASP   A HB2  1 
ATOM   2858 H  HB2  B ASP   A 1 135 ? 11.974 -7.565  -9.595  0.36 21.76 ?  135 ASP   A HB2  1 
ATOM   2859 H  HB3  A ASP   A 1 135 ? 12.507 -8.463  -8.285  0.64 21.59 ?  135 ASP   A HB3  1 
ATOM   2860 H  HB3  B ASP   A 1 135 ? 12.895 -8.528  -8.728  0.36 21.76 ?  135 ASP   A HB3  1 
ATOM   2861 N  N    A PRO   A 1 136 ? 11.989 -6.415  -5.022  0.64 14.72 ?  136 PRO   A N    1 
ATOM   2862 N  N    B PRO   A 1 136 ? 12.147 -6.451  -5.462  0.36 15.63 ?  136 PRO   A N    1 
ATOM   2863 C  CA   A PRO   A 1 136 ? 12.246 -6.837  -3.634  0.64 14.55 ?  136 PRO   A CA   1 
ATOM   2864 C  CA   B PRO   A 1 136 ? 12.333 -6.828  -4.052  0.36 15.49 ?  136 PRO   A CA   1 
ATOM   2865 C  C    A PRO   A 1 136 ? 11.841 -8.272  -3.327  0.64 13.43 ?  136 PRO   A C    1 
ATOM   2866 C  C    B PRO   A 1 136 ? 11.878 -8.241  -3.738  0.36 15.28 ?  136 PRO   A C    1 
ATOM   2867 O  O    A PRO   A 1 136 ? 12.452 -8.894  -2.449  0.64 13.03 ?  136 PRO   A O    1 
ATOM   2868 O  O    B PRO   A 1 136 ? 12.451 -8.881  -2.849  0.36 15.29 ?  136 PRO   A O    1 
ATOM   2869 C  CB   A PRO   A 1 136 ? 11.454 -5.815  -2.803  0.64 15.56 ?  136 PRO   A CB   1 
ATOM   2870 C  CB   B PRO   A 1 136 ? 11.524 -5.765  -3.295  0.36 15.53 ?  136 PRO   A CB   1 
ATOM   2871 C  CG   A PRO   A 1 136 ? 10.427 -5.262  -3.747  0.64 16.45 ?  136 PRO   A CG   1 
ATOM   2872 C  CG   B PRO   A 1 136 ? 10.510 -5.285  -4.289  0.36 15.81 ?  136 PRO   A CG   1 
ATOM   2873 C  CD   A PRO   A 1 136 ? 11.081 -5.256  -5.090  0.64 15.65 ?  136 PRO   A CD   1 
ATOM   2874 C  CD   B PRO   A 1 136 ? 11.179 -5.354  -5.624  0.36 15.91 ?  136 PRO   A CD   1 
ATOM   2875 H  HA   A PRO   A 1 136 ? 13.190 -6.729  -3.432  0.64 17.44 ?  136 PRO   A HA   1 
ATOM   2876 H  HA   B PRO   A 1 136 ? 13.266 -6.749  -3.799  0.36 18.57 ?  136 PRO   A HA   1 
ATOM   2877 H  HB2  A PRO   A 1 136 ? 11.027 -6.261  -2.057  0.64 18.66 ?  136 PRO   A HB2  1 
ATOM   2878 H  HB2  B PRO   A 1 136 ? 11.092 -6.165  -2.525  0.36 18.62 ?  136 PRO   A HB2  1 
ATOM   2879 H  HB3  A PRO   A 1 136 ? 12.047 -5.113  -2.492  0.64 18.66 ?  136 PRO   A HB3  1 
ATOM   2880 H  HB3  B PRO   A 1 136 ? 12.108 -5.038  -3.023  0.36 18.62 ?  136 PRO   A HB3  1 
ATOM   2881 H  HG2  A PRO   A 1 136 ? 9.647  -5.835  -3.754  0.64 19.73 ?  136 PRO   A HG2  1 
ATOM   2882 H  HG2  B PRO   A 1 136 ? 9.735  -5.866  -4.267  0.36 18.96 ?  136 PRO   A HG2  1 
ATOM   2883 H  HG3  A PRO   A 1 136 ? 10.190 -4.360  -3.481  0.64 19.73 ?  136 PRO   A HG3  1 
ATOM   2884 H  HG3  B PRO   A 1 136 ? 10.259 -4.371  -4.084  0.36 18.96 ?  136 PRO   A HG3  1 
ATOM   2885 H  HD2  A PRO   A 1 136 ? 10.414 -5.384  -5.788  0.64 18.77 ?  136 PRO   A HD2  1 
ATOM   2886 H  HD2  B PRO   A 1 136 ? 10.533 -5.574  -6.315  0.36 19.08 ?  136 PRO   A HD2  1 
ATOM   2887 H  HD3  A PRO   A 1 136 ? 11.579 -4.432  -5.227  0.64 18.77 ?  136 PRO   A HD3  1 
ATOM   2888 H  HD3  B PRO   A 1 136 ? 11.644 -4.526  -5.820  0.36 19.08 ?  136 PRO   A HD3  1 
ATOM   2889 N  N    A ILE   A 1 137 ? 10.808 -8.804  -3.990  0.64 13.48 ?  137 ILE   A N    1 
ATOM   2890 N  N    B ILE   A 1 137 ? 10.861 -8.746  -4.439  0.36 15.31 ?  137 ILE   A N    1 
ATOM   2891 C  CA   A ILE   A 1 137 ? 10.448 -10.208 -3.791  0.64 13.76 ?  137 ILE   A CA   1 
ATOM   2892 C  CA   B ILE   A 1 137 ? 10.442 -10.132 -4.250  0.36 15.96 ?  137 ILE   A CA   1 
ATOM   2893 C  C    A ILE   A 1 137 ? 11.608 -11.104 -4.204  0.64 13.84 ?  137 ILE   A C    1 
ATOM   2894 C  C    B ILE   A 1 137 ? 11.606 -11.069 -4.535  0.36 16.11 ?  137 ILE   A C    1 
ATOM   2895 O  O    A ILE   A 1 137 ? 11.956 -12.067 -3.507  0.64 14.20 ?  137 ILE   A O    1 
ATOM   2896 O  O    B ILE   A 1 137 ? 11.833 -12.047 -3.812  0.36 16.34 ?  137 ILE   A O    1 
ATOM   2897 C  CB   A ILE   A 1 137 ? 9.157  -10.551 -4.563  0.64 14.74 ?  137 ILE   A CB   1 
ATOM   2898 C  CB   B ILE   A 1 137 ? 9.228  -10.440 -5.146  0.36 16.59 ?  137 ILE   A CB   1 
ATOM   2899 C  CG1  A ILE   A 1 137 ? 7.970  -9.703  -4.078  0.64 15.82 ?  137 ILE   A CG1  1 
ATOM   2900 C  CG1  B ILE   A 1 137 ? 8.119  -9.407  -4.916  0.36 17.18 ?  137 ILE   A CG1  1 
ATOM   2901 C  CG2  A ILE   A 1 137 ? 8.843  -12.041 -4.441  0.64 15.50 ?  137 ILE   A CG2  1 
ATOM   2902 C  CG2  B ILE   A 1 137 ? 8.720  -11.852 -4.886  0.36 16.65 ?  137 ILE   A CG2  1 
ATOM   2903 C  CD1  A ILE   A 1 137 ? 6.699  -9.897  -4.900  0.64 17.07 ?  137 ILE   A CD1  1 
ATOM   2904 C  CD1  B ILE   A 1 137 ? 7.032  -9.438  -5.960  0.36 17.57 ?  137 ILE   A CD1  1 
ATOM   2905 H  H    A ILE   A 1 137 ? 10.310 -8.376  -4.548  0.64 16.15 ?  137 ILE   A H    1 
ATOM   2906 H  H    B ILE   A 1 137 ? 10.411 -8.309  -5.025  0.36 18.36 ?  137 ILE   A H    1 
ATOM   2907 H  HA   A ILE   A 1 137 ? 10.279 -10.355 -2.850  0.64 16.50 ?  137 ILE   A HA   1 
ATOM   2908 H  HA   B ILE   A 1 137 ? 10.170 -10.264 -3.328  0.36 19.14 ?  137 ILE   A HA   1 
ATOM   2909 H  HB   A ILE   A 1 137 ? 9.300  -10.348 -5.499  0.64 17.67 ?  137 ILE   A HB   1 
ATOM   2910 H  HB   B ILE   A 1 137 ? 9.510  -10.387 -6.071  0.36 19.90 ?  137 ILE   A HB   1 
ATOM   2911 H  HG12 A ILE   A 1 137 ? 7.772  -9.933  -3.158  0.64 18.96 ?  137 ILE   A HG12 1 
ATOM   2912 H  HG12 B ILE   A 1 137 ? 7.712  -9.580  -4.055  0.36 20.60 ?  137 ILE   A HG12 1 
ATOM   2913 H  HG13 A ILE   A 1 137 ? 8.215  -8.761  -4.133  0.64 18.96 ?  137 ILE   A HG13 1 
ATOM   2914 H  HG13 B ILE   A 1 137 ? 8.496  -8.512  -4.922  0.36 20.60 ?  137 ILE   A HG13 1 
ATOM   2915 H  HG21 A ILE   A 1 137 ? 7.945  -12.216 -4.768  0.64 18.59 ?  137 ILE   A HG21 1 
ATOM   2916 H  HG21 B ILE   A 1 137 ? 7.902  -11.990 -5.386  0.36 19.96 ?  137 ILE   A HG21 1 
ATOM   2917 H  HG22 A ILE   A 1 137 ? 9.482  -12.540 -4.969  0.64 18.59 ?  137 ILE   A HG22 1 
ATOM   2918 H  HG22 B ILE   A 1 137 ? 9.393  -12.489 -5.173  0.36 19.96 ?  137 ILE   A HG22 1 
ATOM   2919 H  HG23 A ILE   A 1 137 ? 8.906  -12.298 -3.510  0.64 18.59 ?  137 ILE   A HG23 1 
ATOM   2920 H  HG23 B ILE   A 1 137 ? 8.550  -11.956 -3.937  0.36 19.96 ?  137 ILE   A HG23 1 
ATOM   2921 H  HD11 A ILE   A 1 137 ? 5.987  -10.193 -4.313  0.64 20.46 ?  137 ILE   A HD11 1 
ATOM   2922 H  HD11 B ILE   A 1 137 ? 6.517  -8.617  -5.903  0.36 21.07 ?  137 ILE   A HD11 1 
ATOM   2923 H  HD12 A ILE   A 1 137 ? 6.468  -9.054  -5.312  0.64 20.46 ?  137 ILE   A HD12 1 
ATOM   2924 H  HD12 B ILE   A 1 137 ? 7.440  -9.508  -6.838  0.36 21.07 ?  137 ILE   A HD12 1 
ATOM   2925 H  HD13 A ILE   A 1 137 ? 6.862  -10.562 -5.588  0.64 20.46 ?  137 ILE   A HD13 1 
ATOM   2926 H  HD13 B ILE   A 1 137 ? 6.461  -10.202 -5.799  0.36 21.07 ?  137 ILE   A HD13 1 
ATOM   2927 N  N    A HIS   A 1 138 ? 12.228 -10.789 -5.342  0.64 14.36 ?  138 HIS   A N    1 
ATOM   2928 N  N    B HIS   A 1 138 ? 12.361 -10.782 -5.595  0.36 16.27 ?  138 HIS   A N    1 
ATOM   2929 C  CA   A HIS   A 1 138 ? 13.398 -11.532 -5.795  0.64 14.66 ?  138 HIS   A CA   1 
ATOM   2930 C  CA   B HIS   A 1 138 ? 13.537 -11.587 -5.904  0.36 15.98 ?  138 HIS   A CA   1 
ATOM   2931 C  C    A HIS   A 1 138 ? 14.550 -11.403 -4.804  0.64 14.51 ?  138 HIS   A C    1 
ATOM   2932 C  C    B HIS   A 1 138 ? 14.635 -11.404 -4.860  0.36 15.04 ?  138 HIS   A C    1 
ATOM   2933 O  O    A HIS   A 1 138 ? 15.200 -12.396 -4.454  0.64 14.88 ?  138 HIS   A O    1 
ATOM   2934 O  O    B HIS   A 1 138 ? 15.326 -12.368 -4.511  0.36 15.01 ?  138 HIS   A O    1 
ATOM   2935 C  CB   A HIS   A 1 138 ? 13.806 -11.048 -7.186  0.64 14.84 ?  138 HIS   A CB   1 
ATOM   2936 C  CB   B HIS   A 1 138 ? 14.043 -11.256 -7.306  0.36 16.83 ?  138 HIS   A CB   1 
ATOM   2937 C  CG   A HIS   A 1 138 ? 15.087 -11.651 -7.671  0.64 15.54 ?  138 HIS   A CG   1 
ATOM   2938 C  CG   B HIS   A 1 138 ? 15.243 -12.052 -7.717  0.36 17.67 ?  138 HIS   A CG   1 
ATOM   2939 N  ND1  A HIS   A 1 138 ? 15.221 -12.996 -7.939  0.64 16.74 ?  138 HIS   A ND1  1 
ATOM   2940 N  ND1  B HIS   A 1 138 ? 15.191 -13.407 -7.962  0.36 18.26 ?  138 HIS   A ND1  1 
ATOM   2941 C  CD2  A HIS   A 1 138 ? 16.300 -11.097 -7.908  0.64 15.40 ?  138 HIS   A CD2  1 
ATOM   2942 C  CD2  B HIS   A 1 138 ? 16.528 -11.682 -7.921  0.36 18.10 ?  138 HIS   A CD2  1 
ATOM   2943 C  CE1  A HIS   A 1 138 ? 16.456 -13.243 -8.337  0.64 16.81 ?  138 HIS   A CE1  1 
ATOM   2944 C  CE1  B HIS   A 1 138 ? 16.392 -13.837 -8.303  0.36 18.51 ?  138 HIS   A CE1  1 
ATOM   2945 N  NE2  A HIS   A 1 138 ? 17.134 -12.109 -8.325  0.64 16.16 ?  138 HIS   A NE2  1 
ATOM   2946 N  NE2  B HIS   A 1 138 ? 17.222 -12.810 -8.286  0.36 18.22 ?  138 HIS   A NE2  1 
ATOM   2947 H  H    A HIS   A 1 138 ? 11.988 -10.146 -5.871  0.64 17.21 ?  138 HIS   A H    1 
ATOM   2948 H  H    B HIS   A 1 138 ? 12.203 -10.143 -6.151  0.36 19.51 ?  138 HIS   A H    1 
ATOM   2949 H  HA   A HIS   A 1 138 ? 13.164 -12.466 -5.865  0.64 17.57 ?  138 HIS   A HA   1 
ATOM   2950 H  HA   B HIS   A 1 138 ? 13.278 -12.519 -5.900  0.36 19.16 ?  138 HIS   A HA   1 
ATOM   2951 H  HB2  A HIS   A 1 138 ? 13.104 -11.282 -7.821  0.64 17.79 ?  138 HIS   A HB2  1 
ATOM   2952 H  HB2  B HIS   A 1 138 ? 13.335 -11.437 -7.946  0.36 20.18 ?  138 HIS   A HB2  1 
ATOM   2953 H  HB3  A HIS   A 1 138 ? 13.916 -10.083 -7.169  0.64 17.79 ?  138 HIS   A HB3  1 
ATOM   2954 H  HB3  B HIS   A 1 138 ? 14.286 -10.319 -7.341  0.36 20.18 ?  138 HIS   A HB3  1 
ATOM   2955 H  HD1  A HIS   A 1 138 ? 14.589 -13.581 -7.868  0.64 20.07 ?  138 HIS   A HD1  1 
ATOM   2956 H  HD1  B HIS   A 1 138 ? 14.485 -13.898 -7.906  0.36 21.90 ?  138 HIS   A HD1  1 
ATOM   2957 H  HD2  A HIS   A 1 138 ? 16.518 -10.199 -7.813  0.64 18.47 ?  138 HIS   A HD2  1 
ATOM   2958 H  HD2  B HIS   A 1 138 ? 16.876 -10.827 -7.832  0.36 21.71 ?  138 HIS   A HD2  1 
ATOM   2959 H  HE1  A HIS   A 1 138 ? 16.787 -14.075 -8.578  0.64 20.15 ?  138 HIS   A HE1  1 
ATOM   2960 H  HE1  B HIS   A 1 138 ? 16.613 -14.716 -8.518  0.36 22.19 ?  138 HIS   A HE1  1 
ATOM   2961 N  N    . SER   A 1 139 ? 14.824 -10.182 -4.350  1.00 14.08 ?  139 SER   A N    1 
ATOM   2962 C  CA   . SER   A 1 139 ? 15.887 -9.977  -3.372  1.00 13.82 ?  139 SER   A CA   1 
ATOM   2963 C  C    . SER   A 1 139 ? 15.661 -10.814 -2.117  1.00 13.59 ?  139 SER   A C    1 
ATOM   2964 O  O    . SER   A 1 139 ? 16.609 -11.400 -1.576  1.00 13.65 ?  139 SER   A O    1 
ATOM   2965 C  CB   . SER   A 1 139 ? 16.011 -8.498  -3.021  1.00 13.64 ?  139 SER   A CB   1 
ATOM   2966 O  OG   . SER   A 1 139 ? 17.080 -8.316  -2.110  1.00 13.94 ?  139 SER   A OG   1 
ATOM   2967 H  H    A SER   A 1 139 ? 14.416 -9.463  -4.589  0.64 16.88 ?  139 SER   A H    1 
ATOM   2968 H  H    B SER   A 1 139 ? 14.373 -9.479  -4.554  0.36 16.88 ?  139 SER   A H    1 
ATOM   2969 H  HA   . SER   A 1 139 ? 16.731 -10.253 -3.762  1.00 16.57 ?  139 SER   A HA   1 
ATOM   2970 H  HB2  . SER   A 1 139 ? 16.189 -7.985  -3.826  1.00 16.36 ?  139 SER   A HB2  1 
ATOM   2971 H  HB3  . SER   A 1 139 ? 15.183 -8.194  -2.612  1.00 16.36 ?  139 SER   A HB3  1 
ATOM   2972 H  HG   . SER   A 1 139 ? 17.157 -7.497  -1.906  1.00 16.72 ?  139 SER   A HG   1 
ATOM   2973 N  N    . LEU   A 1 140 ? 14.417 -10.880 -1.637  1.00 13.37 ?  140 LEU   A N    1 
ATOM   2974 C  CA   . LEU   A 1 140 ? 14.142 -11.690 -0.454  1.00 13.47 ?  140 LEU   A CA   1 
ATOM   2975 C  C    . LEU   A 1 140 ? 14.410 -13.166 -0.725  1.00 13.72 ?  140 LEU   A C    1 
ATOM   2976 O  O    . LEU   A 1 140 ? 14.960 -13.876 0.129   1.00 14.57 ?  140 LEU   A O    1 
ATOM   2977 C  CB   . LEU   A 1 140 ? 12.702 -11.467 0.003   1.00 14.10 ?  140 LEU   A CB   1 
ATOM   2978 C  CG   . LEU   A 1 140 ? 12.238 -12.302 1.196   1.00 14.66 ?  140 LEU   A CG   1 
ATOM   2979 C  CD1  . LEU   A 1 140 ? 13.138 -12.103 2.404   1.00 15.22 ?  140 LEU   A CD1  1 
ATOM   2980 C  CD2  . LEU   A 1 140 ? 10.781 -11.976 1.540   1.00 15.40 ?  140 LEU   A CD2  1 
ATOM   2981 H  H    . LEU   A 1 140 ? 13.738 -10.470 -1.967  1.00 16.03 ?  140 LEU   A H    1 
ATOM   2982 H  HA   . LEU   A 1 140 ? 14.728 -11.411 0.263   1.00 16.15 ?  140 LEU   A HA   1 
ATOM   2983 H  HB2  . LEU   A 1 140 ? 12.597 -10.540 0.250   1.00 16.90 ?  140 LEU   A HB2  1 
ATOM   2984 H  HB3  . LEU   A 1 140 ? 12.110 -11.676 -0.738  1.00 16.90 ?  140 LEU   A HB3  1 
ATOM   2985 H  HG   . LEU   A 1 140 ? 12.268 -13.245 0.953   1.00 17.57 ?  140 LEU   A HG   1 
ATOM   2986 H  HD11 . LEU   A 1 140 ? 12.755 -12.573 3.162   1.00 18.24 ?  140 LEU   A HD11 1 
ATOM   2987 H  HD12 . LEU   A 1 140 ? 14.015 -12.468 2.200   1.00 18.24 ?  140 LEU   A HD12 1 
ATOM   2988 H  HD13 . LEU   A 1 140 ? 13.203 -11.159 2.592   1.00 18.24 ?  140 LEU   A HD13 1 
ATOM   2989 H  HD21 . LEU   A 1 140 ? 10.486 -12.556 2.266   1.00 18.47 ?  140 LEU   A HD21 1 
ATOM   2990 H  HD22 . LEU   A 1 140 ? 10.720 -11.050 1.816   1.00 18.47 ?  140 LEU   A HD22 1 
ATOM   2991 H  HD23 . LEU   A 1 140 ? 10.224 -12.128 0.759   1.00 18.47 ?  140 LEU   A HD23 1 
ATOM   2992 N  N    . ARG   A 1 141 ? 14.029 -13.646 -1.912  1.00 14.18 ?  141 ARG   A N    1 
ATOM   2993 C  CA   . ARG   A 1 141 ? 14.270 -15.039 -2.266  1.00 15.24 ?  141 ARG   A CA   1 
ATOM   2994 C  C    . ARG   A 1 141 ? 15.766 -15.344 -2.276  1.00 14.62 ?  141 ARG   A C    1 
ATOM   2995 O  O    . ARG   A 1 141 ? 16.212 -16.356 -1.721  1.00 14.86 ?  141 ARG   A O    1 
ATOM   2996 C  CB   . ARG   A 1 141 ? 13.642 -15.316 -3.634  1.00 16.83 ?  141 ARG   A CB   1 
ATOM   2997 C  CG   . ARG   A 1 141 ? 13.644 -16.767 -4.064  1.00 19.62 ?  141 ARG   A CG   1 
ATOM   2998 C  CD   . ARG   A 1 141 ? 12.611 -17.537 -3.300  1.00 22.30 ?  141 ARG   A CD   1 
ATOM   2999 N  NE   . ARG   A 1 141 ? 13.216 -18.342 -2.252  1.00 23.67 ?  141 ARG   A NE   1 
ATOM   3000 C  CZ   . ARG   A 1 141 ? 12.536 -18.881 -1.247  1.00 24.44 ?  141 ARG   A CZ   1 
ATOM   3001 N  NH1  . ARG   A 1 141 ? 11.257 -18.602 -1.049  1.00 23.55 ?  141 ARG   A NH1  1 
ATOM   3002 N  NH2  . ARG   A 1 141 ? 13.156 -19.714 -0.416  1.00 25.59 ?  141 ARG   A NH2  1 
ATOM   3003 H  H    . ARG   A 1 141 ? 13.638 -13.183 -2.527  1.00 17.00 ?  141 ARG   A H    1 
ATOM   3004 H  HA   . ARG   A 1 141 ? 13.848 -15.614 -1.615  1.00 18.27 ?  141 ARG   A HA   1 
ATOM   3005 H  HB2  . ARG   A 1 141 ? 12.720 -15.012 -3.621  1.00 20.17 ?  141 ARG   A HB2  1 
ATOM   3006 H  HB3  . ARG   A 1 141 ? 14.133 -14.814 -4.305  1.00 20.17 ?  141 ARG   A HB3  1 
ATOM   3007 H  HG2  . ARG   A 1 141 ? 13.439 -16.826 -5.012  1.00 23.53 ?  141 ARG   A HG2  1 
ATOM   3008 H  HG3  . ARG   A 1 141 ? 14.517 -17.159 -3.887  1.00 23.53 ?  141 ARG   A HG3  1 
ATOM   3009 H  HD2  . ARG   A 1 141 ? 11.997 -16.919 -2.872  1.00 26.74 ?  141 ARG   A HD2  1 
ATOM   3010 H  HD3  . ARG   A 1 141 ? 12.123 -18.116 -3.912  1.00 26.74 ?  141 ARG   A HD3  1 
ATOM   3011 H  HE   . ARG   A 1 141 ? 14.026 -18.607 -2.369  1.00 28.39 ?  141 ARG   A HE   1 
ATOM   3012 H  HH11 . ARG   A 1 141 ? 10.839 -18.077 -1.585  1.00 28.25 ?  141 ARG   A HH11 1 
ATOM   3013 H  HH12 . ARG   A 1 141 ? 10.839 -18.953 -0.382  1.00 28.25 ?  141 ARG   A HH12 1 
ATOM   3014 H  HH21 . ARG   A 1 141 ? 13.986 -19.905 -0.538  1.00 30.70 ?  141 ARG   A HH21 1 
ATOM   3015 H  HH22 . ARG   A 1 141 ? 12.731 -20.055 0.251   1.00 30.70 ?  141 ARG   A HH22 1 
ATOM   3016 N  N    . VAL   A 1 142 ? 16.561 -14.473 -2.902  1.00 13.88 ?  142 VAL   A N    1 
ATOM   3017 C  CA   . VAL   A 1 142 ? 18.005 -14.687 -2.929  1.00 14.02 ?  142 VAL   A CA   1 
ATOM   3018 C  C    . VAL   A 1 142 ? 18.572 -14.663 -1.516  1.00 13.48 ?  142 VAL   A C    1 
ATOM   3019 O  O    . VAL   A 1 142 ? 19.433 -15.476 -1.167  1.00 13.87 ?  142 VAL   A O    1 
ATOM   3020 C  CB   . VAL   A 1 142 ? 18.702 -13.670 -3.851  1.00 14.24 ?  142 VAL   A CB   1 
ATOM   3021 C  CG1  . VAL   A 1 142 ? 20.213 -13.881 -3.817  1.00 14.41 ?  142 VAL   A CG1  1 
ATOM   3022 C  CG2  . VAL   A 1 142 ? 18.195 -13.806 -5.275  1.00 15.37 ?  142 VAL   A CG2  1 
ATOM   3023 H  H    . VAL   A 1 142 ? 16.297 -13.757 -3.313  1.00 16.64 ?  142 VAL   A H    1 
ATOM   3024 H  HA   . VAL   A 1 142 ? 18.178 -15.563 -3.296  1.00 16.81 ?  142 VAL   A HA   1 
ATOM   3025 H  HB   . VAL   A 1 142 ? 18.522 -12.766 -3.546  1.00 17.08 ?  142 VAL   A HB   1 
ATOM   3026 H  HG11 . VAL   A 1 142 ? 20.620 -13.395 -4.553  1.00 17.28 ?  142 VAL   A HG11 1 
ATOM   3027 H  HG12 . VAL   A 1 142 ? 20.565 -13.554 -2.974  1.00 17.28 ?  142 VAL   A HG12 1 
ATOM   3028 H  HG13 . VAL   A 1 142 ? 20.401 -14.830 -3.909  1.00 17.28 ?  142 VAL   A HG13 1 
ATOM   3029 H  HG21 . VAL   A 1 142 ? 18.660 -13.162 -5.836  1.00 18.43 ?  142 VAL   A HG21 1 
ATOM   3030 H  HG22 . VAL   A 1 142 ? 18.379 -14.705 -5.585  1.00 18.43 ?  142 VAL   A HG22 1 
ATOM   3031 H  HG23 . VAL   A 1 142 ? 17.247 -13.632 -5.286  1.00 18.43 ?  142 VAL   A HG23 1 
ATOM   3032 N  N    . CYS   A 1 143 ? 18.102 -13.737 -0.683  1.00 13.32 ?  143 CYS   A N    1 
ATOM   3033 C  CA   . CYS   A 1 143 ? 18.564 -13.685 0.698   1.00 13.49 ?  143 CYS   A CA   1 
ATOM   3034 C  C    . CYS   A 1 143 ? 18.331 -15.019 1.395   1.00 13.85 ?  143 CYS   A C    1 
ATOM   3035 O  O    . CYS   A 1 143 ? 19.251 -15.607 1.974   1.00 13.63 ?  143 CYS   A O    1 
ATOM   3036 C  CB   . CYS   A 1 143 ? 17.839 -12.563 1.433   1.00 13.86 ?  143 CYS   A CB   1 
ATOM   3037 S  SG   . CYS   A 1 143 ? 18.314 -12.386 3.151   1.00 14.13 ?  143 CYS   A SG   1 
ATOM   3038 H  H    . CYS   A 1 143 ? 17.523 -13.137 -0.891  1.00 15.96 ?  143 CYS   A H    1 
ATOM   3039 H  HA   . CYS   A 1 143 ? 19.514 -13.503 0.713   1.00 16.17 ?  143 CYS   A HA   1 
ATOM   3040 H  HB2  . CYS   A 1 143 ? 18.027 -11.722 0.986   1.00 16.62 ?  143 CYS   A HB2  1 
ATOM   3041 H  HB3  . CYS   A 1 143 ? 16.888 -12.735 1.409   1.00 16.62 ?  143 CYS   A HB3  1 
ATOM   3042 H  HG   . CYS   A 1 143 ? 17.762 -11.427 3.607   1.00 16.94 ?  143 CYS   A HG   1 
ATOM   3043 N  N    . VAL   A 1 144 ? 17.098 -15.519 1.339   1.00 14.62 ?  144 VAL   A N    1 
ATOM   3044 C  CA   . VAL   A 1 144 ? 16.756 -16.755 2.035   1.00 15.80 ?  144 VAL   A CA   1 
ATOM   3045 C  C    . VAL   A 1 144 ? 17.571 -17.926 1.507   1.00 15.52 ?  144 VAL   A C    1 
ATOM   3046 O  O    . VAL   A 1 144 ? 17.936 -18.833 2.265   1.00 16.19 ?  144 VAL   A O    1 
ATOM   3047 C  CB   . VAL   A 1 144 ? 15.239 -16.993 1.914   1.00 18.33 ?  144 VAL   A CB   1 
ATOM   3048 C  CG1  . VAL   A 1 144 ? 14.873 -18.426 2.246   1.00 20.13 ?  144 VAL   A CG1  1 
ATOM   3049 C  CG2  . VAL   A 1 144 ? 14.491 -15.990 2.794   1.00 18.50 ?  144 VAL   A CG2  1 
ATOM   3050 H  H    . VAL   A 1 144 ? 16.438 -15.157 0.911   1.00 17.53 ?  144 VAL   A H    1 
ATOM   3051 H  HA   . VAL   A 1 144 ? 16.956 -16.652 2.973   1.00 18.94 ?  144 VAL   A HA   1 
ATOM   3052 H  HB   . VAL   A 1 144 ? 14.964 -16.826 0.994   1.00 21.98 ?  144 VAL   A HB   1 
ATOM   3053 H  HG11 . VAL   A 1 144 ? 13.919 -18.473 2.436   1.00 24.14 ?  144 VAL   A HG11 1 
ATOM   3054 H  HG12 . VAL   A 1 144 ? 15.081 -18.991 1.486   1.00 24.14 ?  144 VAL   A HG12 1 
ATOM   3055 H  HG13 . VAL   A 1 144 ? 15.376 -18.706 3.023   1.00 24.14 ?  144 VAL   A HG13 1 
ATOM   3056 H  HG21 . VAL   A 1 144 ? 13.533 -16.149 2.724   1.00 22.18 ?  144 VAL   A HG21 1 
ATOM   3057 H  HG22 . VAL   A 1 144 ? 14.774 -16.099 3.714   1.00 22.18 ?  144 VAL   A HG22 1 
ATOM   3058 H  HG23 . VAL   A 1 144 ? 14.691 -15.086 2.493   1.00 22.18 ?  144 VAL   A HG23 1 
ATOM   3059 N  N    . ASP   A 1 145 ? 17.841 -17.947 0.203   1.00 15.59 ?  145 ASP   A N    1 
ATOM   3060 C  CA   . ASP   A 1 145 ? 18.549 -19.057 -0.425  1.00 16.20 ?  145 ASP   A CA   1 
ATOM   3061 C  C    . ASP   A 1 145 ? 20.067 -18.916 -0.372  1.00 16.11 ?  145 ASP   A C    1 
ATOM   3062 O  O    . ASP   A 1 145 ? 20.772 -19.821 -0.833  1.00 17.82 ?  145 ASP   A O    1 
ATOM   3063 C  CB   . ASP   A 1 145 ? 18.110 -19.202 -1.884  1.00 17.78 ?  145 ASP   A CB   1 
ATOM   3064 C  CG   . ASP   A 1 145 ? 16.666 -19.651 -2.023  1.00 19.90 ?  145 ASP   A CG   1 
ATOM   3065 O  OD1  . ASP   A 1 145 ? 16.096 -20.187 -1.049  1.00 20.41 ?  145 ASP   A OD1  1 
ATOM   3066 O  OD2  . ASP   A 1 145 ? 16.101 -19.452 -3.116  1.00 21.61 -1 145 ASP   A OD2  1 
ATOM   3067 H  H    . ASP   A 1 145 ? 17.599 -17.329 -0.352  1.00 18.69 ?  145 ASP   A H    1 
ATOM   3068 H  HA   . ASP   A 1 145 ? 18.308 -19.876 0.033   1.00 19.42 ?  145 ASP   A HA   1 
ATOM   3069 H  HB2  . ASP   A 1 145 ? 18.209 -18.346 -2.333  1.00 21.33 ?  145 ASP   A HB2  1 
ATOM   3070 H  HB3  . ASP   A 1 145 ? 18.667 -19.868 -2.317  1.00 21.33 ?  145 ASP   A HB3  1 
ATOM   3071 N  N    . THR   A 1 146 ? 20.590 -17.814 0.164   1.00 14.33 ?  146 THR   A N    1 
ATOM   3072 C  CA   . THR   A 1 146 ? 22.030 -17.564 0.183   1.00 13.99 ?  146 THR   A CA   1 
ATOM   3073 C  C    . THR   A 1 146 ? 22.582 -17.387 1.585   1.00 13.70 ?  146 THR   A C    1 
ATOM   3074 O  O    . THR   A 1 146 ? 23.665 -17.913 1.894   1.00 14.81 ?  146 THR   A O    1 
ATOM   3075 C  CB   . THR   A 1 146 ? 22.358 -16.315 -0.655  1.00 13.90 ?  146 THR   A CB   1 
ATOM   3076 O  OG1  . THR   A 1 146 ? 21.836 -16.479 -1.974  1.00 14.59 ?  146 THR   A OG1  1 
ATOM   3077 C  CG2  . THR   A 1 146 ? 23.860 -16.086 -0.735  1.00 14.47 ?  146 THR   A CG2  1 
ATOM   3078 H  H    . THR   A 1 146 ? 20.125 -17.181 0.522   1.00 17.18 ?  146 THR   A H    1 
ATOM   3079 H  HA   . THR   A 1 146 ? 22.487 -18.311 -0.220  1.00 16.78 ?  146 THR   A HA   1 
ATOM   3080 H  HB   . THR   A 1 146 ? 21.958 -15.530 -0.245  1.00 16.67 ?  146 THR   A HB   1 
ATOM   3081 H  HG1  . THR   A 1 146 ? 21.000 -16.553 -1.944  1.00 17.49 ?  146 THR   A HG1  1 
ATOM   3082 H  HG21 . THR   A 1 146 ? 24.059 -15.425 -1.414  1.00 17.35 ?  146 THR   A HG21 1 
ATOM   3083 H  HG22 . THR   A 1 146 ? 24.196 -15.773 0.119   1.00 17.35 ?  146 THR   A HG22 1 
ATOM   3084 H  HG23 . THR   A 1 146 ? 24.305 -16.918 -0.965  1.00 17.35 ?  146 THR   A HG23 1 
ATOM   3085 N  N    . VAL   A 1 147 ? 21.906 -16.606 2.421   1.00 13.93 ?  147 VAL   A N    1 
ATOM   3086 C  CA   . VAL   A 1 147 ? 22.403 -16.305 3.755   1.00 13.94 ?  147 VAL   A CA   1 
ATOM   3087 C  C    . VAL   A 1 147 ? 22.088 -17.472 4.679   1.00 14.29 ?  147 VAL   A C    1 
ATOM   3088 O  O    . VAL   A 1 147 ? 20.945 -17.945 4.742   1.00 14.95 ?  147 VAL   A O    1 
ATOM   3089 C  CB   . VAL   A 1 147 ? 21.787 -14.999 4.276   1.00 14.10 ?  147 VAL   A CB   1 
ATOM   3090 C  CG1  . VAL   A 1 147 ? 22.315 -14.696 5.655   1.00 15.17 ?  147 VAL   A CG1  1 
ATOM   3091 C  CG2  . VAL   A 1 147 ? 22.050 -13.855 3.310   1.00 14.22 ?  147 VAL   A CG2  1 
ATOM   3092 H  H    . VAL   A 1 147 ? 21.150 -16.234 2.238   1.00 16.70 ?  147 VAL   A H    1 
ATOM   3093 H  HA   . VAL   A 1 147 ? 23.366 -16.194 3.718   1.00 16.71 ?  147 VAL   A HA   1 
ATOM   3094 H  HB   . VAL   A 1 147 ? 20.829 -15.114 4.347   1.00 16.91 ?  147 VAL   A HB   1 
ATOM   3095 H  HG11 . VAL   A 1 147 ? 22.082 -13.787 5.888   1.00 18.19 ?  147 VAL   A HG11 1 
ATOM   3096 H  HG12 . VAL   A 1 147 ? 21.909 -15.313 6.290   1.00 18.19 ?  147 VAL   A HG12 1 
ATOM   3097 H  HG13 . VAL   A 1 147 ? 23.277 -14.807 5.657   1.00 18.19 ?  147 VAL   A HG13 1 
ATOM   3098 H  HG21 . VAL   A 1 147 ? 21.726 -13.032 3.707   1.00 17.05 ?  147 VAL   A HG21 1 
ATOM   3099 H  HG22 . VAL   A 1 147 ? 23.000 -13.796 3.144   1.00 17.05 ?  147 VAL   A HG22 1 
ATOM   3100 H  HG23 . VAL   A 1 147 ? 21.576 -14.033 2.483   1.00 17.05 ?  147 VAL   A HG23 1 
ATOM   3101 N  N    . ARG   A 1 148 ? 23.112 -17.936 5.396   1.00 14.65 ?  148 ARG   A N    1 
ATOM   3102 C  CA   . ARG   A 1 148 ? 22.982 -19.015 6.363   1.00 15.00 ?  148 ARG   A CA   1 
ATOM   3103 C  C    . ARG   A 1 148 ? 23.103 -18.546 7.801   1.00 15.00 ?  148 ARG   A C    1 
ATOM   3104 O  O    . ARG   A 1 148 ? 22.689 -19.273 8.713   1.00 16.60 ?  148 ARG   A O    1 
ATOM   3105 C  CB   . ARG   A 1 148 ? 24.028 -20.106 6.086   1.00 15.31 ?  148 ARG   A CB   1 
ATOM   3106 C  CG   . ARG   A 1 148 ? 23.872 -20.739 4.716   1.00 16.56 ?  148 ARG   A CG   1 
ATOM   3107 C  CD   . ARG   A 1 148 ? 24.954 -21.777 4.435   1.00 17.47 ?  148 ARG   A CD   1 
ATOM   3108 N  NE   . ARG   A 1 148 ? 26.295 -21.200 4.472   1.00 17.42 ?  148 ARG   A NE   1 
ATOM   3109 C  CZ   . ARG   A 1 148 ? 26.812 -20.461 3.501   1.00 16.72 ?  148 ARG   A CZ   1 
ATOM   3110 N  NH1  . ARG   A 1 148 ? 26.152 -20.239 2.377   1.00 17.10 ?  148 ARG   A NH1  1 
ATOM   3111 N  NH2  . ARG   A 1 148 ? 28.027 -19.938 3.657   1.00 16.98 ?  148 ARG   A NH2  1 
ATOM   3112 H  H    . ARG   A 1 148 ? 23.917 -17.632 5.326   1.00 17.56 ?  148 ARG   A H    1 
ATOM   3113 H  HA   . ARG   A 1 148 ? 22.110 -19.414 6.263   1.00 17.98 ?  148 ARG   A HA   1 
ATOM   3114 H  HB2  . ARG   A 1 148 ? 24.914 -19.722 6.137   1.00 18.35 ?  148 ARG   A HB2  1 
ATOM   3115 H  HB3  . ARG   A 1 148 ? 23.929 -20.811 6.747   1.00 18.35 ?  148 ARG   A HB3  1 
ATOM   3116 H  HG2  . ARG   A 1 148 ? 23.003 -21.170 4.665   1.00 19.85 ?  148 ARG   A HG2  1 
ATOM   3117 H  HG3  . ARG   A 1 148 ? 23.932 -20.040 4.041   1.00 19.85 ?  148 ARG   A HG3  1 
ATOM   3118 H  HD2  . ARG   A 1 148 ? 24.899 -22.470 5.109   1.00 20.95 ?  148 ARG   A HD2  1 
ATOM   3119 H  HD3  . ARG   A 1 148 ? 24.803 -22.153 3.554   1.00 20.95 ?  148 ARG   A HD3  1 
ATOM   3120 H  HE   . ARG   A 1 148 ? 26.768 -21.343 5.170   1.00 20.89 ?  148 ARG   A HE   1 
ATOM   3121 H  HH11 . ARG   A 1 148 ? 25.364 -20.562 2.264   1.00 20.50 ?  148 ARG   A HH11 1 
ATOM   3122 H  HH12 . ARG   A 1 148 ? 26.507 -19.753 1.761   1.00 20.50 ?  148 ARG   A HH12 1 
ATOM   3123 H  HH21 . ARG   A 1 148 ? 28.461 -20.074 4.385   1.00 20.36 ?  148 ARG   A HH21 1 
ATOM   3124 H  HH22 . ARG   A 1 148 ? 28.371 -19.457 3.033   1.00 20.36 ?  148 ARG   A HH22 1 
ATOM   3125 N  N    . THR   A 1 149 ? 23.647 -17.350 8.015   1.00 15.35 ?  149 THR   A N    1 
ATOM   3126 C  CA   . THR   A 1 149 ? 23.723 -16.747 9.332   1.00 15.53 ?  149 THR   A CA   1 
ATOM   3127 C  C    . THR   A 1 149 ? 22.397 -16.051 9.636   1.00 14.96 ?  149 THR   A C    1 
ATOM   3128 O  O    . THR   A 1 149 ? 21.468 -16.041 8.819   1.00 15.45 ?  149 THR   A O    1 
ATOM   3129 C  CB   . THR   A 1 149 ? 24.921 -15.807 9.386   1.00 15.72 ?  149 THR   A CB   1 
ATOM   3130 O  OG1  . THR   A 1 149 ? 24.795 -14.878 8.311   1.00 15.64 ?  149 THR   A OG1  1 
ATOM   3131 C  CG2  . THR   A 1 149 ? 26.228 -16.600 9.252   1.00 16.08 ?  149 THR   A CG2  1 
ATOM   3132 H  H    . THR   A 1 149 ? 23.989 -16.853 7.395   1.00 18.40 ?  149 THR   A H    1 
ATOM   3133 H  HA   . THR   A 1 149 ? 23.850 -17.448 9.991   1.00 18.62 ?  149 THR   A HA   1 
ATOM   3134 H  HB   . THR   A 1 149 ? 24.920 -15.337 10.234  1.00 18.84 ?  149 THR   A HB   1 
ATOM   3135 H  HG1  . THR   A 1 149 ? 25.443 -14.346 8.315   1.00 18.75 ?  149 THR   A HG1  1 
ATOM   3136 H  HG21 . THR   A 1 149 ? 26.987 -16.001 9.312   1.00 19.28 ?  149 THR   A HG21 1 
ATOM   3137 H  HG22 . THR   A 1 149 ? 26.295 -17.263 9.959   1.00 19.28 ?  149 THR   A HG22 1 
ATOM   3138 H  HG23 . THR   A 1 149 ? 26.257 -17.058 8.394   1.00 19.28 ?  149 THR   A HG23 1 
ATOM   3139 N  N    . ASN   A 1 150 ? 22.273 -15.510 10.842  1.00 15.24 ?  150 ASN   A N    1 
ATOM   3140 C  CA   . ASN   A 1 150 ? 20.988 -15.000 11.323  1.00 15.57 ?  150 ASN   A CA   1 
ATOM   3141 C  C    . ASN   A 1 150 ? 20.810 -13.562 10.855  1.00 14.56 ?  150 ASN   A C    1 
ATOM   3142 O  O    . ASN   A 1 150 ? 21.560 -12.668 11.268  1.00 15.81 ?  150 ASN   A O    1 
ATOM   3143 C  CB   . ASN   A 1 150 ? 20.927 -15.098 12.842  1.00 18.40 ?  150 ASN   A CB   1 
ATOM   3144 C  CG   . ASN   A 1 150 ? 20.810 -16.523 13.319  1.00 22.15 ?  150 ASN   A CG   1 
ATOM   3145 O  OD1  . ASN   A 1 150 ? 20.223 -17.361 12.637  1.00 23.38 ?  150 ASN   A OD1  1 
ATOM   3146 N  ND2  . ASN   A 1 150 ? 21.376 -16.814 14.488  1.00 24.54 ?  150 ASN   A ND2  1 
ATOM   3147 H  H    . ASN   A 1 150 ? 22.913 -15.436 11.409  1.00 18.27 ?  150 ASN   A H    1 
ATOM   3148 H  HA   . ASN   A 1 150 ? 20.266 -15.541 10.955  1.00 18.67 ?  150 ASN   A HA   1 
ATOM   3149 H  HB2  . ASN   A 1 150 ? 21.735 -14.723 13.220  1.00 22.07 ?  150 ASN   A HB2  1 
ATOM   3150 H  HB3  . ASN   A 1 150 ? 20.150 -14.615 13.164  1.00 22.07 ?  150 ASN   A HB3  1 
ATOM   3151 H  HD21 . ASN   A 1 150 ? 21.339 -17.616 14.806  1.00 29.43 ?  150 ASN   A HD21 1 
ATOM   3152 H  HD22 . ASN   A 1 150 ? 21.780 -16.199 14.936  1.00 29.43 ?  150 ASN   A HD22 1 
ATOM   3153 N  N    . VAL   A 1 151 ? 19.821 -13.333 9.995   1.00 14.12 ?  151 VAL   A N    1 
ATOM   3154 C  CA   . VAL   A 1 151 ? 19.611 -12.029 9.389   1.00 14.34 ?  151 VAL   A CA   1 
ATOM   3155 C  C    . VAL   A 1 151 ? 18.230 -11.502 9.756   1.00 14.08 ?  151 VAL   A C    1 
ATOM   3156 O  O    . VAL   A 1 151 ? 17.215 -12.208 9.624   1.00 15.38 ?  151 VAL   A O    1 
ATOM   3157 C  CB   . VAL   A 1 151 ? 19.896 -12.025 7.872   1.00 15.62 ?  151 VAL   A CB   1 
ATOM   3158 C  CG1  . VAL   A 1 151 ? 19.074 -13.057 7.136   1.00 16.53 ?  151 VAL   A CG1  1 
ATOM   3159 C  CG2  . VAL   A 1 151 ? 19.693 -10.618 7.287   1.00 15.73 ?  151 VAL   A CG2  1 
ATOM   3160 H  H    . VAL   A 1 151 ? 19.252 -13.931 9.745   1.00 16.92 ?  151 VAL   A H    1 
ATOM   3161 H  HA   . VAL   A 1 151 ? 20.260 -11.419 9.782   1.00 17.19 ?  151 VAL   A HA   1 
ATOM   3162 H  HB   . VAL   A 1 151 ? 20.830 -12.253 7.735   1.00 18.72 ?  151 VAL   A HB   1 
ATOM   3163 H  HG11 . VAL   A 1 151 ? 19.265 -13.004 6.185   1.00 19.82 ?  151 VAL   A HG11 1 
ATOM   3164 H  HG12 . VAL   A 1 151 ? 19.309 -13.945 7.465   1.00 19.82 ?  151 VAL   A HG12 1 
ATOM   3165 H  HG13 . VAL   A 1 151 ? 18.132 -12.891 7.293   1.00 19.82 ?  151 VAL   A HG13 1 
ATOM   3166 H  HG21 . VAL   A 1 151 ? 20.007 -10.611 6.368   1.00 18.86 ?  151 VAL   A HG21 1 
ATOM   3167 H  HG22 . VAL   A 1 151 ? 18.749 -10.396 7.314   1.00 18.86 ?  151 VAL   A HG22 1 
ATOM   3168 H  HG23 . VAL   A 1 151 ? 20.200 -9.981  7.813   1.00 18.86 ?  151 VAL   A HG23 1 
ATOM   3169 N  N    A TYR   A 1 152 ? 18.205 -10.255 10.204  0.64 14.21 ?  152 TYR   A N    1 
ATOM   3170 N  N    B TYR   A 1 152 ? 18.220 -10.252 10.238  0.36 13.79 ?  152 TYR   A N    1 
ATOM   3171 C  CA   A TYR   A 1 152 ? 16.990 -9.537  10.547  0.64 13.79 ?  152 TYR   A CA   1 
ATOM   3172 C  CA   B TYR   A 1 152 ? 17.042 -9.531  10.698  0.36 13.17 ?  152 TYR   A CA   1 
ATOM   3173 C  C    A TYR   A 1 152 ? 16.802 -8.454  9.493   0.64 12.91 ?  152 TYR   A C    1 
ATOM   3174 C  C    B TYR   A 1 152 ? 16.823 -8.373  9.742   0.36 12.34 ?  152 TYR   A C    1 
ATOM   3175 O  O    A TYR   A 1 152 ? 17.586 -7.498  9.425   0.64 12.96 ?  152 TYR   A O    1 
ATOM   3176 O  O    B TYR   A 1 152 ? 17.561 -7.382  9.779   0.36 12.74 ?  152 TYR   A O    1 
ATOM   3177 C  CB   A TYR   A 1 152 ? 17.123 -8.989  11.964  0.64 14.56 ?  152 TYR   A CB   1 
ATOM   3178 C  CB   B TYR   A 1 152 ? 17.261 -9.022  12.119  0.36 13.90 ?  152 TYR   A CB   1 
ATOM   3179 C  CG   A TYR   A 1 152 ? 17.131 -10.118 12.968  0.64 15.46 ?  152 TYR   A CG   1 
ATOM   3180 C  CG   B TYR   A 1 152 ? 17.120 -10.118 13.135  0.36 14.79 ?  152 TYR   A CG   1 
ATOM   3181 C  CD1  A TYR   A 1 152 ? 18.302 -10.798 13.286  0.64 16.71 ?  152 TYR   A CD1  1 
ATOM   3182 C  CD1  B TYR   A 1 152 ? 18.182 -10.959 13.430  0.36 15.51 ?  152 TYR   A CD1  1 
ATOM   3183 C  CD2  A TYR   A 1 152 ? 15.954 -10.548 13.559  0.64 15.79 ?  152 TYR   A CD2  1 
ATOM   3184 C  CD2  B TYR   A 1 152 ? 15.911 -10.335 13.777  0.36 15.00 ?  152 TYR   A CD2  1 
ATOM   3185 C  CE1  A TYR   A 1 152 ? 18.303 -11.859 14.182  0.64 17.61 ?  152 TYR   A CE1  1 
ATOM   3186 C  CE1  B TYR   A 1 152 ? 18.048 -11.983 14.349  0.36 16.57 ?  152 TYR   A CE1  1 
ATOM   3187 C  CE2  A TYR   A 1 152 ? 15.941 -11.612 14.456  0.64 17.08 ?  152 TYR   A CE2  1 
ATOM   3188 C  CE2  B TYR   A 1 152 ? 15.766 -11.355 14.698  0.36 16.31 ?  152 TYR   A CE2  1 
ATOM   3189 C  CZ   A TYR   A 1 152 ? 17.120 -12.261 14.764  0.64 17.80 ?  152 TYR   A CZ   1 
ATOM   3190 C  CZ   B TYR   A 1 152 ? 16.837 -12.176 14.982  0.36 17.01 ?  152 TYR   A CZ   1 
ATOM   3191 O  OH   A TYR   A 1 152 ? 17.117 -13.318 15.654  0.64 19.28 ?  152 TYR   A OH   1 
ATOM   3192 O  OH   B TYR   A 1 152 ? 16.698 -13.193 15.898  0.36 18.60 ?  152 TYR   A OH   1 
ATOM   3193 H  H    A TYR   A 1 152 ? 18.921 -9.776  10.309  0.64 17.04 ?  152 TYR   A H    1 
ATOM   3194 H  H    B TYR   A 1 152 ? 18.939 -9.768  10.295  0.36 16.53 ?  152 TYR   A H    1 
ATOM   3195 H  HA   A TYR   A 1 152 ? 16.238 -10.149 10.513  0.64 16.54 ?  152 TYR   A HA   1 
ATOM   3196 H  HA   B TYR   A 1 152 ? 16.268 -10.106 10.678  0.36 15.79 ?  152 TYR   A HA   1 
ATOM   3197 H  HB2  A TYR   A 1 152 ? 17.959 -8.509  12.044  0.64 17.46 ?  152 TYR   A HB2  1 
ATOM   3198 H  HB2  B TYR   A 1 152 ? 18.158 -8.657  12.193  0.36 16.66 ?  152 TYR   A HB2  1 
ATOM   3199 H  HB3  A TYR   A 1 152 ? 16.375 -8.412  12.158  0.64 17.46 ?  152 TYR   A HB3  1 
ATOM   3200 H  HB3  B TYR   A 1 152 ? 16.605 -8.337  12.320  0.36 16.66 ?  152 TYR   A HB3  1 
ATOM   3201 H  HD1  A TYR   A 1 152 ? 19.101 -10.539 12.896  0.64 20.04 ?  152 TYR   A HD1  1 
ATOM   3202 H  HD1  B TYR   A 1 152 ? 18.999 -10.828 12.999  0.36 18.60 ?  152 TYR   A HD1  1 
ATOM   3203 H  HD2  A TYR   A 1 152 ? 15.153 -10.122 13.352  0.64 18.94 ?  152 TYR   A HD2  1 
ATOM   3204 H  HD2  B TYR   A 1 152 ? 15.184 -9.783  13.584  0.36 17.98 ?  152 TYR   A HD2  1 
ATOM   3205 H  HE1  A TYR   A 1 152 ? 19.094 -12.300 14.396  0.64 21.12 ?  152 TYR   A HE1  1 
ATOM   3206 H  HE1  B TYR   A 1 152 ? 18.775 -12.531 14.538  0.36 19.87 ?  152 TYR   A HE1  1 
ATOM   3207 H  HE2  A TYR   A 1 152 ? 15.139 -11.882 14.853  0.64 20.48 ?  152 TYR   A HE2  1 
ATOM   3208 H  HE2  B TYR   A 1 152 ? 14.952 -11.485 15.124  0.36 19.56 ?  152 TYR   A HE2  1 
ATOM   3209 H  HH   A TYR   A 1 152 ? 16.333 -13.454 15.943  0.64 23.12 ?  152 TYR   A HH   1 
ATOM   3210 H  HH   B TYR   A 1 152 ? 15.989 -13.089 16.328  0.36 22.30 ?  152 TYR   A HH   1 
ATOM   3211 N  N    A LEU   A 1 153 ? 15.795 -8.639  8.642   0.64 12.89 ?  153 LEU   A N    1 
ATOM   3212 N  N    B LEU   A 1 153 ? 15.816 -8.502  8.889   0.36 12.08 ?  153 LEU   A N    1 
ATOM   3213 C  CA   A LEU   A 1 153 ? 15.542 -7.768  7.503   0.64 12.42 ?  153 LEU   A CA   1 
ATOM   3214 C  CA   B LEU   A 1 153 ? 15.562 -7.537  7.835   0.36 11.51 ?  153 LEU   A CA   1 
ATOM   3215 C  C    A LEU   A 1 153 ? 14.537 -6.682  7.863   0.64 12.28 ?  153 LEU   A C    1 
ATOM   3216 C  C    B LEU   A 1 153 ? 14.587 -6.476  8.322   0.36 11.50 ?  153 LEU   A C    1 
ATOM   3217 O  O    A LEU   A 1 153 ? 13.418 -6.980  8.293   0.64 12.97 ?  153 LEU   A O    1 
ATOM   3218 O  O    B LEU   A 1 153 ? 13.500 -6.797  8.818   0.36 11.57 ?  153 LEU   A O    1 
ATOM   3219 C  CB   A LEU   A 1 153 ? 14.989 -8.587  6.337   0.64 12.11 ?  153 LEU   A CB   1 
ATOM   3220 C  CB   B LEU   A 1 153 ? 14.990 -8.239  6.604   0.36 11.51 ?  153 LEU   A CB   1 
ATOM   3221 C  CG   A LEU   A 1 153 ? 15.955 -9.558  5.658   0.64 12.51 ?  153 LEU   A CG   1 
ATOM   3222 C  CG   B LEU   A 1 153 ? 15.890 -9.302  5.973   0.36 11.87 ?  153 LEU   A CG   1 
ATOM   3223 C  CD1  A LEU   A 1 153 ? 15.196 -10.480 4.719   0.64 12.70 ?  153 LEU   A CD1  1 
ATOM   3224 C  CD1  B LEU   A 1 153 ? 15.116 -10.062 4.907   0.36 12.20 ?  153 LEU   A CD1  1 
ATOM   3225 C  CD2  A LEU   A 1 153 ? 17.006 -8.777  4.897   0.64 12.35 ?  153 LEU   A CD2  1 
ATOM   3226 C  CD2  B LEU   A 1 153 ? 17.157 -8.677  5.391   0.36 12.33 ?  153 LEU   A CD2  1 
ATOM   3227 H  H    A LEU   A 1 153 ? 15.223 -9.290  8.713   0.64 15.46 ?  153 LEU   A H    1 
ATOM   3228 H  H    B LEU   A 1 153 ? 15.249 -9.147  8.908   0.36 14.48 ?  153 LEU   A H    1 
ATOM   3229 H  HA   A LEU   A 1 153 ? 16.370 -7.357  7.226   0.64 14.88 ?  153 LEU   A HA   1 
ATOM   3230 H  HA   B LEU   A 1 153 ? 16.390 -7.103  7.591   0.36 13.80 ?  153 LEU   A HA   1 
ATOM   3231 H  HB2  A LEU   A 1 153 ? 14.238 -9.116  6.662   0.64 14.52 ?  153 LEU   A HB2  1 
ATOM   3232 H  HB2  B LEU   A 1 153 ? 14.162 -8.674  6.858   0.36 13.79 ?  153 LEU   A HB2  1 
ATOM   3233 H  HB3  A LEU   A 1 153 ? 14.677 -7.977  5.656   0.64 14.52 ?  153 LEU   A HB3  1 
ATOM   3234 H  HB3  B LEU   A 1 153 ? 14.810 -7.570  5.925   0.36 13.79 ?  153 LEU   A HB3  1 
ATOM   3235 H  HG   A LEU   A 1 153 ? 16.401 -10.103 6.331   0.64 14.99 ?  153 LEU   A HG   1 
ATOM   3236 H  HG   B LEU   A 1 153 ? 16.158 -9.934  6.657   0.36 14.22 ?  153 LEU   A HG   1 
ATOM   3237 H  HD11 A LEU   A 1 153 ? 15.766 -11.230 4.485   0.64 15.22 ?  153 LEU   A HD11 1 
ATOM   3238 H  HD11 B LEU   A 1 153 ? 15.695 -10.733 4.514   0.36 14.62 ?  153 LEU   A HD11 1 
ATOM   3239 H  HD12 A LEU   A 1 153 ? 14.399 -10.797 5.164   0.64 15.22 ?  153 LEU   A HD12 1 
ATOM   3240 H  HD12 B LEU   A 1 153 ? 14.348 -10.486 5.318   0.36 14.62 ?  153 LEU   A HD12 1 
ATOM   3241 H  HD13 A LEU   A 1 153 ? 14.959 -9.983  3.921   0.64 15.22 ?  153 LEU   A HD13 1 
ATOM   3242 H  HD13 B LEU   A 1 153 ? 14.823 -9.437  4.224   0.36 14.62 ?  153 LEU   A HD13 1 
ATOM   3243 H  HD21 A LEU   A 1 153 ? 17.582 -9.394  4.431   0.64 14.80 ?  153 LEU   A HD21 1 
ATOM   3244 H  HD21 B LEU   A 1 153 ? 17.671 -9.365  4.940   0.36 14.78 ?  153 LEU   A HD21 1 
ATOM   3245 H  HD22 A LEU   A 1 153 ? 16.555 -8.194  4.265   0.64 14.80 ?  153 LEU   A HD22 1 
ATOM   3246 H  HD22 B LEU   A 1 153 ? 16.908 -7.983  4.761   0.36 14.78 ?  153 LEU   A HD22 1 
ATOM   3247 H  HD23 A LEU   A 1 153 ? 17.518 -8.249  5.527   0.64 14.80 ?  153 LEU   A HD23 1 
ATOM   3248 H  HD23 B LEU   A 1 153 ? 17.683 -8.294  6.113   0.36 14.78 ?  153 LEU   A HD23 1 
ATOM   3249 N  N    A ALA   A 1 154 ? 14.924 -5.428  7.651   0.64 12.02 ?  154 ALA   A N    1 
ATOM   3250 N  N    B ALA   A 1 154 ? 14.986 -5.217  8.184   0.36 11.49 ?  154 ALA   A N    1 
ATOM   3251 C  CA   A ALA   A 1 154 ? 14.058 -4.280  7.882   0.64 12.52 ?  154 ALA   A CA   1 
ATOM   3252 C  CA   B ALA   A 1 154 ? 14.114 -4.075  8.414   0.36 11.93 ?  154 ALA   A CA   1 
ATOM   3253 C  C    A ALA   A 1 154 ? 13.563 -3.764  6.537   0.64 12.13 ?  154 ALA   A C    1 
ATOM   3254 C  C    B ALA   A 1 154 ? 13.704 -3.536  7.050   0.36 12.24 ?  154 ALA   A C    1 
ATOM   3255 O  O    A ALA   A 1 154 ? 14.367 -3.378  5.680   0.64 13.04 ?  154 ALA   A O    1 
ATOM   3256 O  O    B ALA   A 1 154 ? 14.563 -3.145  6.254   0.36 12.23 ?  154 ALA   A O    1 
ATOM   3257 C  CB   A ALA   A 1 154 ? 14.815 -3.180  8.622   0.64 13.10 ?  154 ALA   A CB   1 
ATOM   3258 C  CB   B ALA   A 1 154 ? 14.844 -3.002  9.222   0.36 11.97 ?  154 ALA   A CB   1 
ATOM   3259 H  H    A ALA   A 1 154 ? 15.703 -5.221  7.366   0.64 14.40 ?  154 ALA   A H    1 
ATOM   3260 H  H    B ALA   A 1 154 ? 15.785 -4.986  7.949   0.36 13.78 ?  154 ALA   A H    1 
ATOM   3261 H  HA   A ALA   A 1 154 ? 13.291 -4.553  8.420   0.64 15.01 ?  154 ALA   A HA   1 
ATOM   3262 H  HA   B ALA   A 1 154 ? 13.319 -4.347  8.898   0.36 14.30 ?  154 ALA   A HA   1 
ATOM   3263 H  HB1  A ALA   A 1 154 ? 14.217 -2.432  8.763   0.64 15.70 ?  154 ALA   A HB1  1 
ATOM   3264 H  HB1  B ALA   A 1 154 ? 14.247 -2.253  9.373   0.36 14.34 ?  154 ALA   A HB1  1 
ATOM   3265 H  HB2  A ALA   A 1 154 ? 15.122 -3.527  9.475   0.64 15.70 ?  154 ALA   A HB2  1 
ATOM   3266 H  HB2  B ALA   A 1 154 ? 15.120 -3.381  10.072  0.36 14.34 ?  154 ALA   A HB2  1 
ATOM   3267 H  HB3  A ALA   A 1 154 ? 15.572 -2.909  8.083   0.64 15.70 ?  154 ALA   A HB3  1 
ATOM   3268 H  HB3  B ALA   A 1 154 ? 15.625 -2.708  8.725   0.36 14.34 ?  154 ALA   A HB3  1 
ATOM   3269 N  N    A VAL   A 1 155 ? 12.245 -3.769  6.356   0.34 10.38 ?  155 VAL   A N    1 
ATOM   3270 N  N    B VAL   A 1 155 ? 12.404 -3.545  6.769   0.36 12.72 ?  155 VAL   A N    1 
ATOM   3271 C  CA   A VAL   A 1 155 ? 11.584 -3.268  5.157   0.34 12.36 ?  155 VAL   A CA   1 
ATOM   3272 C  CA   B VAL   A 1 155 ? 11.863 -3.087  5.493   0.36 14.85 ?  155 VAL   A CA   1 
ATOM   3273 C  CA   T VAL   A 1 155 ? 11.623 -3.316  5.234   0.30 14.31 ?  155 VAL   A CA   1 
ATOM   3274 C  C    A VAL   A 1 155 ? 10.893 -1.963  5.528   0.34 13.72 ?  155 VAL   A C    1 
ATOM   3275 C  C    B VAL   A 1 155 ? 11.014 -1.853  5.772   0.36 16.31 ?  155 VAL   A C    1 
ATOM   3276 C  C    T VAL   A 1 155 ? 11.012 -1.950  5.558   0.30 14.19 ?  155 VAL   A C    1 
ATOM   3277 O  O    A VAL   A 1 155 ? 9.987  -1.955  6.370   0.34 14.40 ?  155 VAL   A O    1 
ATOM   3278 O  O    B VAL   A 1 155 ? 9.906  -1.960  6.311   0.36 16.93 ?  155 VAL   A O    1 
ATOM   3279 O  O    T VAL   A 1 155 ? 10.214 -1.816  6.484   0.30 14.04 ?  155 VAL   A O    1 
ATOM   3280 C  CB   A VAL   A 1 155 ? 10.577 -4.294  4.614   0.34 12.91 ?  155 VAL   A CB   1 
ATOM   3281 C  CB   B VAL   A 1 155 ? 11.043 -4.182  4.798   0.36 15.03 ?  155 VAL   A CB   1 
ATOM   3282 C  CB   T VAL   A 1 155 ? 10.586 -4.331  4.706   0.30 14.21 ?  155 VAL   A CB   1 
ATOM   3283 C  CG1  A VAL   A 1 155 ? 9.913  -3.779  3.345   0.34 13.40 ?  155 VAL   A CG1  1 
ATOM   3284 C  CG1  B VAL   A 1 155 ? 10.405 -3.639  3.532   0.36 15.16 ?  155 VAL   A CG1  1 
ATOM   3285 C  CG1  T VAL   A 1 155 ? 9.889  -3.788  3.469   0.30 14.21 ?  155 VAL   A CG1  1 
ATOM   3286 C  CG2  A VAL   A 1 155 ? 11.271 -5.626  4.364   0.34 13.58 ?  155 VAL   A CG2  1 
ATOM   3287 C  CG2  B VAL   A 1 155 ? 11.924 -5.385  4.485   0.36 14.96 ?  155 VAL   A CG2  1 
ATOM   3288 C  CG2  T VAL   A 1 155 ? 11.264 -5.664  4.397   0.30 14.69 ?  155 VAL   A CG2  1 
ATOM   3289 H  H    A VAL   A 1 155 ? 11.691 -4.094  6.935   0.34 12.44 ?  155 VAL   A H    1 
ATOM   3290 H  H    B VAL   A 1 155 ? 11.800 -3.812  7.318   0.36 15.25 ?  155 VAL   A H    1 
ATOM   3291 H  HA   A VAL   A 1 155 ? 12.244 -3.089  4.474   0.34 14.82 ?  155 VAL   A HA   1 
ATOM   3292 H  HA   B VAL   A 1 155 ? 12.591 -2.829  4.905   0.36 17.80 ?  155 VAL   A HA   1 
ATOM   3293 H  HB   A VAL   A 1 155 ? 9.881  -4.435  5.278   0.34 15.47 ?  155 VAL   A HB   1 
ATOM   3294 H  HB   B VAL   A 1 155 ? 10.336 -4.472  5.394   0.36 18.02 ?  155 VAL   A HB   1 
ATOM   3295 H  HB   T VAL   A 1 155 ? 9.910  -4.489  5.387   0.30 17.04 ?  155 VAL   A HB   1 
ATOM   3296 H  HG11 A VAL   A 1 155 ? 9.333  -4.469  2.991   0.34 16.06 ?  155 VAL   A HG11 1 
ATOM   3297 H  HG11 B VAL   A 1 155 ? 10.096 -4.384  2.994   0.36 18.17 ?  155 VAL   A HG11 1 
ATOM   3298 H  HG11 T VAL   A 1 155 ? 9.358  -4.493  3.069   0.30 17.03 ?  155 VAL   A HG11 1 
ATOM   3299 H  HG12 A VAL   A 1 155 ? 9.392  -2.987  3.555   0.34 16.06 ?  155 VAL   A HG12 1 
ATOM   3300 H  HG12 B VAL   A 1 155 ? 9.655  -3.072  3.772   0.36 18.17 ?  155 VAL   A HG12 1 
ATOM   3301 H  HG12 T VAL   A 1 155 ? 9.318  -3.047  3.724   0.30 17.03 ?  155 VAL   A HG12 1 
ATOM   3302 H  HG13 A VAL   A 1 155 ? 10.601 -3.560  2.697   0.34 16.06 ?  155 VAL   A HG13 1 
ATOM   3303 H  HG13 B VAL   A 1 155 ? 11.065 -3.128  3.040   0.36 18.17 ?  155 VAL   A HG13 1 
ATOM   3304 H  HG13 T VAL   A 1 155 ? 10.562 -3.485  2.838   0.30 17.03 ?  155 VAL   A HG13 1 
ATOM   3305 H  HG21 A VAL   A 1 155 ? 10.648 -6.227  3.927   0.34 16.28 ?  155 VAL   A HG21 1 
ATOM   3306 H  HG21 B VAL   A 1 155 ? 11.392 -6.055  4.029   0.36 17.94 ?  155 VAL   A HG21 1 
ATOM   3307 H  HG21 T VAL   A 1 155 ? 10.601 -6.289  4.063   0.30 17.61 ?  155 VAL   A HG21 1 
ATOM   3308 H  HG22 A VAL   A 1 155 ? 12.042 -5.476  3.797   0.34 16.28 ?  155 VAL   A HG22 1 
ATOM   3309 H  HG22 B VAL   A 1 155 ? 12.658 -5.101  3.917   0.36 17.94 ?  155 VAL   A HG22 1 
ATOM   3310 H  HG22 T VAL   A 1 155 ? 11.949 -5.520  3.724   0.30 17.61 ?  155 VAL   A HG22 1 
ATOM   3311 H  HG23 A VAL   A 1 155 ? 11.551 -6.000  5.214   0.34 16.28 ?  155 VAL   A HG23 1 
ATOM   3312 H  HG23 B VAL   A 1 155 ? 12.272 -5.747  5.316   0.36 17.94 ?  155 VAL   A HG23 1 
ATOM   3313 H  HG23 T VAL   A 1 155 ? 11.667 -6.011  5.208   0.30 17.61 ?  155 VAL   A HG23 1 
ATOM   3314 N  N    A PHE   A 1 156 ? 11.310 -0.862  4.898   0.34 14.57 ?  156 PHE   A N    1 
ATOM   3315 N  N    B PHE   A 1 156 ? 11.525 -0.679  5.390   0.36 16.92 ?  156 PHE   A N    1 
ATOM   3316 N  N    T PHE   A 1 156 ? 11.404 -0.935  4.785   0.30 14.32 ?  156 PHE   A N    1 
ATOM   3317 C  CA   A PHE   A 1 156 ? 10.811 0.453   5.302   0.34 16.23 ?  156 PHE   A CA   1 
ATOM   3318 C  CA   B PHE   A 1 156 ? 10.868 0.575   5.755   0.36 18.46 ?  156 PHE   A CA   1 
ATOM   3319 C  CA   T PHE   A 1 156 ? 10.994 0.437   5.082   0.30 14.93 ?  156 PHE   A CA   1 
ATOM   3320 C  C    A PHE   A 1 156 ? 9.344  0.635   4.933   0.34 16.82 ?  156 PHE   A C    1 
ATOM   3321 C  C    B PHE   A 1 156 ? 9.470  0.677   5.150   0.36 18.82 ?  156 PHE   A C    1 
ATOM   3322 C  C    T PHE   A 1 156 ? 9.532  0.675   4.726   0.30 15.60 ?  156 PHE   A C    1 
ATOM   3323 O  O    A PHE   A 1 156 ? 8.571  1.214   5.706   0.34 17.12 ?  156 PHE   A O    1 
ATOM   3324 O  O    B PHE   A 1 156 ? 8.502  0.996   5.850   0.36 19.16 ?  156 PHE   A O    1 
ATOM   3325 O  O    T PHE   A 1 156 ? 8.811  1.359   5.461   0.30 15.92 ?  156 PHE   A O    1 
ATOM   3326 C  CB   A PHE   A 1 156 ? 11.665 1.556   4.671   0.34 17.24 ?  156 PHE   A CB   1 
ATOM   3327 C  CB   B PHE   A 1 156 ? 11.739 1.763   5.331   0.36 19.73 ?  156 PHE   A CB   1 
ATOM   3328 C  CB   T PHE   A 1 156 ? 11.887 1.411   4.311   0.30 14.48 ?  156 PHE   A CB   1 
ATOM   3329 C  CG   A PHE   A 1 156 ? 11.223 2.954   5.034   0.34 18.60 ?  156 PHE   A CG   1 
ATOM   3330 C  CG   B PHE   A 1 156 ? 11.045 3.091   5.447   0.36 21.11 ?  156 PHE   A CG   1 
ATOM   3331 C  CG   T PHE   A 1 156 ? 11.545 2.867   4.525   0.30 14.44 ?  156 PHE   A CG   1 
ATOM   3332 C  CD1  A PHE   A 1 156 ? 11.168 3.352   6.361   0.34 19.12 ?  156 PHE   A CD1  1 
ATOM   3333 C  CD1  B PHE   A 1 156 ? 10.967 3.741   6.667   0.36 21.68 ?  156 PHE   A CD1  1 
ATOM   3334 C  CD1  T PHE   A 1 156 ? 11.928 3.517   5.691   0.30 15.31 ?  156 PHE   A CD1  1 
ATOM   3335 C  CD2  A PHE   A 1 156 ? 10.880 3.873   4.051   0.34 19.53 ?  156 PHE   A CD2  1 
ATOM   3336 C  CD2  B PHE   A 1 156 ? 10.469 3.688   4.336   0.36 21.89 ?  156 PHE   A CD2  1 
ATOM   3337 C  CD2  T PHE   A 1 156 ? 10.871 3.588   3.551   0.30 14.63 ?  156 PHE   A CD2  1 
ATOM   3338 C  CE1  A PHE   A 1 156 ? 10.766 4.633   6.703   0.34 19.46 ?  156 PHE   A CE1  1 
ATOM   3339 C  CE1  B PHE   A 1 156 ? 10.327 4.960   6.777   0.36 22.02 ?  156 PHE   A CE1  1 
ATOM   3340 C  CE1  T PHE   A 1 156 ? 11.628 4.852   5.891   0.30 15.99 ?  156 PHE   A CE1  1 
ATOM   3341 C  CE2  A PHE   A 1 156 ? 10.478 5.157   4.387   0.34 20.08 ?  156 PHE   A CE2  1 
ATOM   3342 C  CE2  B PHE   A 1 156 ? 9.828  4.908   4.440   0.36 22.07 ?  156 PHE   A CE2  1 
ATOM   3343 C  CE2  T PHE   A 1 156 ? 10.568 4.924   3.745   0.30 15.40 ?  156 PHE   A CE2  1 
ATOM   3344 C  CZ   A PHE   A 1 156 ? 10.425 5.537   5.714   0.34 19.80 ?  156 PHE   A CZ   1 
ATOM   3345 C  CZ   B PHE   A 1 156 ? 9.757  5.545   5.661   0.36 22.29 ?  156 PHE   A CZ   1 
ATOM   3346 C  CZ   T PHE   A 1 156 ? 10.949 5.558   4.918   0.30 15.93 ?  156 PHE   A CZ   1 
ATOM   3347 H  H    A PHE   A 1 156 ? 11.860 -0.857  4.239   0.34 17.47 ?  156 PHE   A H    1 
ATOM   3348 H  H    B PHE   A 1 156 ? 12.246 -0.581  4.928   0.36 20.29 ?  156 PHE   A H    1 
ATOM   3349 H  H    T PHE   A 1 156 ? 11.900 -1.022  4.092   0.30 17.17 ?  156 PHE   A H    1 
ATOM   3350 H  HA   A PHE   A 1 156 ? 10.890 0.533   6.264   0.34 19.46 ?  156 PHE   A HA   1 
ATOM   3351 H  HA   B PHE   A 1 156 ? 10.779 0.613   6.718   0.36 22.14 ?  156 PHE   A HA   1 
ATOM   3352 H  HA   T PHE   A 1 156 ? 11.110 0.600   6.031   0.30 17.89 ?  156 PHE   A HA   1 
ATOM   3353 H  HB2  A PHE   A 1 156 ? 12.585 1.450   4.967   0.34 20.67 ?  156 PHE   A HB2  1 
ATOM   3354 H  HB2  B PHE   A 1 156 ? 12.531 1.794   5.898   0.36 23.66 ?  156 PHE   A HB2  1 
ATOM   3355 H  HB2  T PHE   A 1 156 ? 12.805 1.274   4.592   0.30 17.36 ?  156 PHE   A HB2  1 
ATOM   3356 H  HB3  A PHE   A 1 156 ? 11.623 1.473   3.706   0.34 20.67 ?  156 PHE   A HB3  1 
ATOM   3357 H  HB3  B PHE   A 1 156 ? 12.007 1.649   4.406   0.36 23.66 ?  156 PHE   A HB3  1 
ATOM   3358 H  HB3  T PHE   A 1 156 ? 11.802 1.222   3.364   0.30 17.36 ?  156 PHE   A HB3  1 
ATOM   3359 H  HD1  A PHE   A 1 156 ? 11.398 2.749   7.032   0.34 22.93 ?  156 PHE   A HD1  1 
ATOM   3360 H  HD1  B PHE   A 1 156 ? 11.352 3.353   7.420   0.36 26.00 ?  156 PHE   A HD1  1 
ATOM   3361 H  HD1  T PHE   A 1 156 ? 12.383 3.039   6.353   0.30 18.36 ?  156 PHE   A HD1  1 
ATOM   3362 H  HD2  A PHE   A 1 156 ? 10.916 3.622   3.157   0.34 23.42 ?  156 PHE   A HD2  1 
ATOM   3363 H  HD2  B PHE   A 1 156 ? 10.517 3.262   3.511   0.36 26.25 ?  156 PHE   A HD2  1 
ATOM   3364 H  HD2  T PHE   A 1 156 ? 10.612 3.161   2.768   0.30 17.54 ?  156 PHE   A HD2  1 
ATOM   3365 H  HE1  A PHE   A 1 156 ? 10.731 4.887   7.598   0.34 23.33 ?  156 PHE   A HE1  1 
ATOM   3366 H  HE1  B PHE   A 1 156 ? 10.281 5.389   7.601   0.36 26.40 ?  156 PHE   A HE1  1 
ATOM   3367 H  HE1  T PHE   A 1 156 ? 11.884 5.269   6.683   0.30 19.17 ?  156 PHE   A HE1  1 
ATOM   3368 H  HE2  A PHE   A 1 156 ? 10.249 5.763   3.721   0.34 24.08 ?  156 PHE   A HE2  1 
ATOM   3369 H  HE2  B PHE   A 1 156 ? 9.445  5.297   3.687   0.36 26.47 ?  156 PHE   A HE2  1 
ATOM   3370 H  HE2  T PHE   A 1 156 ? 10.110 5.395   3.093   0.30 18.47 ?  156 PHE   A HE2  1 
ATOM   3371 H  HZ   A PHE   A 1 156 ? 10.155 6.398   5.944   0.34 23.74 ?  156 PHE   A HZ   1 
ATOM   3372 H  HZ   B PHE   A 1 156 ? 9.326  6.365   5.734   0.36 26.73 ?  156 PHE   A HZ   1 
ATOM   3373 H  HZ   T PHE   A 1 156 ? 10.745 6.453   5.054   0.30 19.10 ?  156 PHE   A HZ   1 
ATOM   3374 N  N    A ASP   A 1 157 ? 8.944  0.151   3.763   0.34 17.85 ?  157 ASP   A N    1 
ATOM   3375 N  N    B ASP   A 1 157 ? 9.346  0.414   3.850   0.36 18.71 ?  157 ASP   A N    1 
ATOM   3376 N  N    T ASP   A 1 157 ? 9.083  0.123   3.607   0.30 16.39 ?  157 ASP   A N    1 
ATOM   3377 C  CA   A ASP   A 1 157 ? 7.616  0.408   3.223   0.34 19.06 ?  157 ASP   A CA   1 
ATOM   3378 C  CA   B ASP   A 1 157 ? 8.088  0.636   3.146   0.36 19.13 ?  157 ASP   A CA   1 
ATOM   3379 C  CA   T ASP   A 1 157 ? 7.776  0.436   3.049   0.30 17.24 ?  157 ASP   A CA   1 
ATOM   3380 C  C    A ASP   A 1 157 ? 6.644  -0.648  3.738   0.34 19.66 ?  157 ASP   A C    1 
ATOM   3381 C  C    B ASP   A 1 157 ? 7.031  -0.357  3.615   0.36 19.39 ?  157 ASP   A C    1 
ATOM   3382 C  C    T ASP   A 1 157 ? 6.748  -0.563  3.567   0.30 17.60 ?  157 ASP   A C    1 
ATOM   3383 O  O    A ASP   A 1 157 ? 6.806  -1.840  3.453   0.34 19.33 ?  157 ASP   A O    1 
ATOM   3384 O  O    B ASP   A 1 157 ? 7.272  -1.567  3.648   0.36 19.65 ?  157 ASP   A O    1 
ATOM   3385 O  O    T ASP   A 1 157 ? 6.846  -1.763  3.285   0.30 17.15 ?  157 ASP   A O    1 
ATOM   3386 C  CB   A ASP   A 1 157 ? 7.675  0.385   1.698   0.34 19.64 ?  157 ASP   A CB   1 
ATOM   3387 C  CB   B ASP   A 1 157 ? 8.307  0.470   1.644   0.36 19.22 ?  157 ASP   A CB   1 
ATOM   3388 C  CB   T ASP   A 1 157 ? 7.869  0.381   1.527   0.30 17.69 ?  157 ASP   A CB   1 
ATOM   3389 C  CG   A ASP   A 1 157 ? 6.384  0.854   1.055   0.34 20.49 ?  157 ASP   A CG   1 
ATOM   3390 C  CG   B ASP   A 1 157 ? 7.171  1.059   0.822   0.36 19.14 ?  157 ASP   A CG   1 
ATOM   3391 C  CG   T ASP   A 1 157 ? 6.654  0.949   0.849   0.30 18.01 ?  157 ASP   A CG   1 
ATOM   3392 O  OD1  A ASP   A 1 157 ? 6.018  2.034   1.231   0.34 21.08 ?  157 ASP   A OD1  1 
ATOM   3393 O  OD1  B ASP   A 1 157 ? 7.200  2.277   0.537   0.36 19.43 ?  157 ASP   A OD1  1 
ATOM   3394 O  OD1  T ASP   A 1 157 ? 5.564  0.375   1.043   0.30 17.97 ?  157 ASP   A OD1  1 
ATOM   3395 O  OD2  A ASP   A 1 157 ? 5.728  0.035   0.376   0.34 20.31 -1 157 ASP   A OD2  1 
ATOM   3396 O  OD2  B ASP   A 1 157 ? 6.236  0.301   0.477   0.36 19.60 -1 157 ASP   A OD2  1 
ATOM   3397 O  OD2  T ASP   A 1 157 ? 6.782  1.964   0.133   0.30 18.03 -1 157 ASP   A OD2  1 
ATOM   3398 H  H    A ASP   A 1 157 ? 9.434  -0.350  3.261   0.34 21.40 ?  157 ASP   A H    1 
ATOM   3399 H  H    B ASP   A 1 157 ? 9.978  0.107   3.357   0.36 22.43 ?  157 ASP   A H    1 
ATOM   3400 H  H    T ASP   A 1 157 ? 9.521  -0.455  3.150   0.30 19.65 ?  157 ASP   A H    1 
ATOM   3401 H  HA   A ASP   A 1 157 ? 7.311  1.281   3.513   0.34 22.85 ?  157 ASP   A HA   1 
ATOM   3402 H  HA   B ASP   A 1 157 ? 7.771  1.539   3.316   0.36 22.94 ?  157 ASP   A HA   1 
ATOM   3403 H  HA   T ASP   A 1 157 ? 7.505  1.325   3.322   0.30 20.68 ?  157 ASP   A HA   1 
ATOM   3404 H  HB2  A ASP   A 1 157 ? 8.428  0.935   1.412   0.34 23.55 ?  157 ASP   A HB2  1 
ATOM   3405 H  HB2  B ASP   A 1 157 ? 9.149  0.893   1.400   0.36 23.04 ?  157 ASP   A HB2  1 
ATOM   3406 H  HB2  T ASP   A 1 157 ? 8.650  0.881   1.249   0.30 21.21 ?  157 ASP   A HB2  1 
ATOM   3407 H  HB3  A ASP   A 1 157 ? 7.814  -0.523  1.401   0.34 23.55 ?  157 ASP   A HB3  1 
ATOM   3408 H  HB3  B ASP   A 1 157 ? 8.352  -0.479  1.437   0.36 23.04 ?  157 ASP   A HB3  1 
ATOM   3409 H  HB3  T ASP   A 1 157 ? 7.954  -0.544  1.251   0.30 21.21 ?  157 ASP   A HB3  1 
ATOM   3410 N  N    A LYS   A 1 158 ? 5.633  -0.206  4.493   0.34 20.77 ?  158 LYS   A N    1 
ATOM   3411 N  N    B LYS   A 1 158 ? 5.843  0.151   3.954   0.36 19.69 ?  158 LYS   A N    1 
ATOM   3412 N  N    T LYS   A 1 158 ? 5.760  -0.063  4.319   0.30 18.68 ?  158 LYS   A N    1 
ATOM   3413 C  CA   A LYS   A 1 158 ? 4.665  -1.140  5.063   0.34 21.48 ?  158 LYS   A CA   1 
ATOM   3414 C  CA   B LYS   A 1 158 ? 4.808  -0.721  4.500   0.36 20.34 ?  158 LYS   A CA   1 
ATOM   3415 C  CA   T LYS   A 1 158 ? 4.775  -0.946  4.940   0.30 19.98 ?  158 LYS   A CA   1 
ATOM   3416 C  C    A LYS   A 1 158 ? 3.918  -1.890  3.969   0.34 21.12 ?  158 LYS   A C    1 
ATOM   3417 C  C    B LYS   A 1 158 ? 4.139  -1.558  3.417   0.36 20.42 ?  158 LYS   A C    1 
ATOM   3418 C  C    T LYS   A 1 158 ? 4.007  -1.740  3.893   0.30 20.02 ?  158 LYS   A C    1 
ATOM   3419 O  O    A LYS   A 1 158 ? 3.739  -3.111  4.053   0.34 21.24 ?  158 LYS   A O    1 
ATOM   3420 O  O    B LYS   A 1 158 ? 3.874  -2.747  3.626   0.36 20.51 ?  158 LYS   A O    1 
ATOM   3421 O  O    T LYS   A 1 158 ? 3.790  -2.946  4.054   0.30 20.21 ?  158 LYS   A O    1 
ATOM   3422 C  CB   A LYS   A 1 158 ? 3.693  -0.393  5.979   0.34 22.33 ?  158 LYS   A CB   1 
ATOM   3423 C  CB   B LYS   A 1 158 ? 3.763  0.102   5.248   0.36 21.38 ?  158 LYS   A CB   1 
ATOM   3424 C  CB   T LYS   A 1 158 ? 3.818  -0.136  5.821   0.30 21.43 ?  158 LYS   A CB   1 
ATOM   3425 C  CG   A LYS   A 1 158 ? 2.458  -1.189  6.404   0.34 23.17 ?  158 LYS   A CG   1 
ATOM   3426 C  CG   B LYS   A 1 158 ? 2.488  -0.660  5.548   0.36 22.35 ?  158 LYS   A CG   1 
ATOM   3427 C  CG   T LYS   A 1 158 ? 2.578  -0.900  6.291   0.30 22.70 ?  158 LYS   A CG   1 
ATOM   3428 C  CD   A LYS   A 1 158 ? 2.810  -2.430  7.217   0.34 23.70 ?  158 LYS   A CD   1 
ATOM   3429 C  CD   B LYS   A 1 158 ? 1.528  0.198   6.338   0.36 23.31 ?  158 LYS   A CD   1 
ATOM   3430 C  CD   T LYS   A 1 158 ? 2.936  -2.114  7.140   0.30 23.85 ?  158 LYS   A CD   1 
ATOM   3431 C  CE   A LYS   A 1 158 ? 1.550  -3.117  7.738   0.34 23.91 ?  158 LYS   A CE   1 
ATOM   3432 C  CE   B LYS   A 1 158 ? 0.101  -0.280  6.179   0.36 24.10 ?  158 LYS   A CE   1 
ATOM   3433 C  CE   T LYS   A 1 158 ? 1.686  -2.884  7.556   0.30 24.59 ?  158 LYS   A CE   1 
ATOM   3434 N  NZ   A LYS   A 1 158 ? 1.827  -4.457  8.329   0.34 24.11 ?  158 LYS   A NZ   1 
ATOM   3435 N  NZ   B LYS   A 1 158 ? -0.853 0.635   6.859   0.36 24.49 ?  158 LYS   A NZ   1 
ATOM   3436 N  NZ   T LYS   A 1 158 ? 2.007  -4.115  8.333   0.30 25.03 ?  158 LYS   A NZ   1 
ATOM   3437 H  H    A LYS   A 1 158 ? 5.488  0.617   4.683   0.34 24.91 ?  158 LYS   A H    1 
ATOM   3438 H  H    B LYS   A 1 158 ? 5.615  0.978   3.871   0.36 23.61 ?  158 LYS   A H    1 
ATOM   3439 H  H    T LYS   A 1 158 ? 5.636  0.771   4.481   0.30 22.40 ?  158 LYS   A H    1 
ATOM   3440 H  HA   A LYS   A 1 158 ? 5.135  -1.794  5.601   0.34 25.76 ?  158 LYS   A HA   1 
ATOM   3441 H  HA   B LYS   A 1 158 ? 5.218  -1.328  5.134   0.36 24.39 ?  158 LYS   A HA   1 
ATOM   3442 H  HA   T LYS   A 1 158 ? 5.231  -1.578  5.517   0.30 23.97 ?  158 LYS   A HA   1 
ATOM   3443 H  HB2  A LYS   A 1 158 ? 4.165  -0.137  6.788   0.34 26.79 ?  158 LYS   A HB2  1 
ATOM   3444 H  HB2  B LYS   A 1 158 ? 4.141  0.389   6.093   0.36 25.64 ?  158 LYS   A HB2  1 
ATOM   3445 H  HB2  T LYS   A 1 158 ? 4.294  0.156   6.617   0.30 25.69 ?  158 LYS   A HB2  1 
ATOM   3446 H  HB3  A LYS   A 1 158 ? 3.383  0.404   5.520   0.34 26.79 ?  158 LYS   A HB3  1 
ATOM   3447 H  HB3  B LYS   A 1 158 ? 3.528  0.872   4.711   0.36 25.64 ?  158 LYS   A HB3  1 
ATOM   3448 H  HB3  T LYS   A 1 158 ? 3.511  0.638   5.325   0.30 25.69 ?  158 LYS   A HB3  1 
ATOM   3449 H  HG2  A LYS   A 1 158 ? 1.899  -0.623  6.957   0.34 27.78 ?  158 LYS   A HG2  1 
ATOM   3450 H  HG2  B LYS   A 1 158 ? 2.049  -0.909  4.719   0.36 26.81 ?  158 LYS   A HG2  1 
ATOM   3451 H  HG2  T LYS   A 1 158 ? 2.033  -0.310  6.834   0.30 27.23 ?  158 LYS   A HG2  1 
ATOM   3452 H  HG3  A LYS   A 1 158 ? 1.961  -1.469  5.618   0.34 27.78 ?  158 LYS   A HG3  1 
ATOM   3453 H  HG3  B LYS   A 1 158 ? 2.701  -1.453  6.069   0.36 26.81 ?  158 LYS   A HG3  1 
ATOM   3454 H  HG3  T LYS   A 1 158 ? 2.065  -1.203  5.524   0.30 27.23 ?  158 LYS   A HG3  1 
ATOM   3455 H  HD2  A LYS   A 1 158 ? 3.290  -3.057  6.656   0.34 28.42 ?  158 LYS   A HD2  1 
ATOM   3456 H  HD2  B LYS   A 1 158 ? 1.765  0.155   7.277   0.36 27.96 ?  158 LYS   A HD2  1 
ATOM   3457 H  HD2  T LYS   A 1 158 ? 3.504  -2.712  6.631   0.30 28.60 ?  158 LYS   A HD2  1 
ATOM   3458 H  HD3  A LYS   A 1 158 ? 3.354  -2.171  7.977   0.34 28.42 ?  158 LYS   A HD3  1 
ATOM   3459 H  HD3  B LYS   A 1 158 ? 1.585  1.112   6.017   0.36 27.96 ?  158 LYS   A HD3  1 
ATOM   3460 H  HD3  T LYS   A 1 158 ? 3.392  -1.820  7.945   0.30 28.60 ?  158 LYS   A HD3  1 
ATOM   3461 H  HE2  A LYS   A 1 158 ? 1.148  -2.562  8.426   0.34 28.68 ?  158 LYS   A HE2  1 
ATOM   3462 H  HE2  B LYS   A 1 158 ? -0.123 -0.309  5.234   0.36 28.91 ?  158 LYS   A HE2  1 
ATOM   3463 H  HE2  T LYS   A 1 158 ? 1.128  -2.315  8.109   0.30 29.49 ?  158 LYS   A HE2  1 
ATOM   3464 H  HE3  A LYS   A 1 158 ? 0.929  -3.235  7.004   0.34 28.68 ?  158 LYS   A HE3  1 
ATOM   3465 H  HE3  B LYS   A 1 158 ? 0.014  -1.163  6.571   0.36 28.91 ?  158 LYS   A HE3  1 
ATOM   3466 H  HE3  T LYS   A 1 158 ? 1.200  -3.151  6.760   0.30 29.49 ?  158 LYS   A HE3  1 
ATOM   3467 H  HZ1  A LYS   A 1 158 ? 1.071  -4.824  8.621   0.34 28.92 ?  158 LYS   A HZ1  1 
ATOM   3468 H  HZ1  B LYS   A 1 158 ? -1.685 0.338   6.755   0.36 29.38 ?  158 LYS   A HZ1  1 
ATOM   3469 H  HZ1  T LYS   A 1 158 ? 1.257  -4.539  8.557   0.30 30.02 ?  158 LYS   A HZ1  1 
ATOM   3470 H  HZ2  A LYS   A 1 158 ? 2.190  -4.990  7.715   0.34 28.92 ?  158 LYS   A HZ2  1 
ATOM   3471 H  HZ2  B LYS   A 1 158 ? -0.667 0.676   7.728   0.36 29.38 ?  158 LYS   A HZ2  1 
ATOM   3472 H  HZ2  T LYS   A 1 158 ? 2.511  -4.662  7.843   0.30 30.02 ?  158 LYS   A HZ2  1 
ATOM   3473 H  HZ3  A LYS   A 1 158 ? 2.393  -4.377  9.012   0.34 28.92 ?  158 LYS   A HZ3  1 
ATOM   3474 H  HZ3  B LYS   A 1 158 ? -0.792 1.452   6.512   0.36 29.38 ?  158 LYS   A HZ3  1 
ATOM   3475 H  HZ3  T LYS   A 1 158 ? 2.450  -3.900  9.074   0.30 30.02 ?  158 LYS   A HZ3  1 
ATOM   3476 N  N    A ASN   A 1 159 ? 3.475  -1.179  2.931   0.34 20.87 ?  159 ASN   A N    1 
ATOM   3477 N  N    B ASN   A 1 159 ? 3.836  -0.958  2.265   0.36 20.80 ?  159 ASN   A N    1 
ATOM   3478 N  N    T ASN   A 1 159 ? 3.580  -1.085  2.820   0.30 20.21 ?  159 ASN   A N    1 
ATOM   3479 C  CA   A ASN   A 1 159 ? 2.803  -1.853  1.828   0.34 20.39 ?  159 ASN   A CA   1 
ATOM   3480 C  CA   B ASN   A 1 159 ? 3.199  -1.718  1.195   0.36 21.76 ?  159 ASN   A CA   1 
ATOM   3481 C  CA   T ASN   A 1 159 ? 2.841  -1.772  1.770   0.30 20.53 ?  159 ASN   A CA   1 
ATOM   3482 C  C    A ASN   A 1 159 ? 3.715  -2.902  1.201   0.34 18.95 ?  159 ASN   A C    1 
ATOM   3483 C  C    B ASN   A 1 159 ? 4.107  -2.834  0.701   0.36 21.12 ?  159 ASN   A C    1 
ATOM   3484 C  C    T ASN   A 1 159 ? 3.690  -2.865  1.124   0.30 20.36 ?  159 ASN   A C    1 
ATOM   3485 O  O    A ASN   A 1 159 ? 3.286  -4.029  0.928   0.34 18.24 ?  159 ASN   A O    1 
ATOM   3486 O  O    B ASN   A 1 159 ? 3.637  -3.934  0.389   0.36 20.91 ?  159 ASN   A O    1 
ATOM   3487 O  O    T ASN   A 1 159 ? 3.173  -3.911  0.742   0.30 20.35 ?  159 ASN   A O    1 
ATOM   3488 C  CB   A ASN   A 1 159 ? 2.315  -0.826  0.802   0.34 21.44 ?  159 ASN   A CB   1 
ATOM   3489 C  CB   B ASN   A 1 159 ? 2.801  -0.789  0.048   0.36 23.41 ?  159 ASN   A CB   1 
ATOM   3490 C  CB   T ASN   A 1 159 ? 2.334  -0.777  0.722   0.30 21.18 ?  159 ASN   A CB   1 
ATOM   3491 C  CG   A ASN   A 1 159 ? 1.118  -0.029  1.300   0.34 22.71 ?  159 ASN   A CG   1 
ATOM   3492 C  CG   B ASN   A 1 159 ? 1.620  0.094   0.399   0.36 25.15 ?  159 ASN   A CG   1 
ATOM   3493 C  CG   T ASN   A 1 159 ? 1.144  0.031   1.214   0.30 22.03 ?  159 ASN   A CG   1 
ATOM   3494 O  OD1  A ASN   A 1 159 ? 0.296  -0.543  2.055   0.34 23.53 ?  159 ASN   A OD1  1 
ATOM   3495 O  OD1  B ASN   A 1 159 ? 1.722  1.322   0.398   0.36 25.90 ?  159 ASN   A OD1  1 
ATOM   3496 O  OD1  T ASN   A 1 159 ? 0.362  -0.442  2.035   0.30 22.60 ?  159 ASN   A OD1  1 
ATOM   3497 N  ND2  A ASN   A 1 159 ? 1.014  1.227   0.877   0.34 23.18 ?  159 ASN   A ND2  1 
ATOM   3498 N  ND2  B ASN   A 1 159 ? 0.485  -0.531  0.700   0.36 25.97 ?  159 ASN   A ND2  1 
ATOM   3499 N  ND2  T ASN   A 1 159 ? 1.001  1.251   0.713   0.30 22.36 ?  159 ASN   A ND2  1 
ATOM   3500 H  H    A ASN   A 1 159 ? 3.554  -0.329  2.844   0.34 25.03 ?  159 ASN   A H    1 
ATOM   3501 H  H    B ASN   A 1 159 ? 3.992  -0.135  2.080   0.36 24.95 ?  159 ASN   A H    1 
ATOM   3502 H  H    T ASN   A 1 159 ? 3.698  -0.247  2.685   0.30 24.24 ?  159 ASN   A H    1 
ATOM   3503 H  HA   A ASN   A 1 159 ? 2.019  -2.311  2.173   0.34 24.45 ?  159 ASN   A HA   1 
ATOM   3504 H  HA   B ASN   A 1 159 ? 2.395  -2.130  1.538   0.36 26.10 ?  159 ASN   A HA   1 
ATOM   3505 H  HA   T ASN   A 1 159 ? 2.067  -2.204  2.164   0.30 24.62 ?  159 ASN   A HA   1 
ATOM   3506 H  HB2  A ASN   A 1 159 ? 3.023  -0.196  0.613   0.34 25.72 ?  159 ASN   A HB2  1 
ATOM   3507 H  HB2  B ASN   A 1 159 ? 3.549  -0.214  -0.171  0.36 28.08 ?  159 ASN   A HB2  1 
ATOM   3508 H  HB2  T ASN   A 1 159 ? 3.042  -0.157  0.503   0.30 25.40 ?  159 ASN   A HB2  1 
ATOM   3509 H  HB3  A ASN   A 1 159 ? 2.047  -1.285  -0.010  0.34 25.72 ?  159 ASN   A HB3  1 
ATOM   3510 H  HB3  B ASN   A 1 159 ? 2.554  -1.324  -0.723  0.36 28.08 ?  159 ASN   A HB3  1 
ATOM   3511 H  HB3  T ASN   A 1 159 ? 2.060  -1.267  -0.071  0.30 25.40 ?  159 ASN   A HB3  1 
ATOM   3512 H  HD21 A ASN   A 1 159 ? 0.351  1.714   1.131   0.34 27.80 ?  159 ASN   A HD21 1 
ATOM   3513 H  HD21 B ASN   A 1 159 ? -0.213 -0.077  0.908   0.36 31.14 ?  159 ASN   A HD21 1 
ATOM   3514 H  HD21 T ASN   A 1 159 ? 0.339  1.741   0.960   0.30 26.81 ?  159 ASN   A HD21 1 
ATOM   3515 H  HD22 A ASN   A 1 159 ? 1.610  1.553   0.354   0.34 27.80 ?  159 ASN   A HD22 1 
ATOM   3516 H  HD22 B ASN   A 1 159 ? 0.450  -1.392  0.687   0.36 31.14 ?  159 ASN   A HD22 1 
ATOM   3517 H  HD22 T ASN   A 1 159 ? 1.570  1.548   0.145   0.30 26.81 ?  159 ASN   A HD22 1 
ATOM   3518 N  N    A LEU   A 1 160 ? 4.992  -2.573  1.013   0.34 18.09 ?  160 LEU   A N    1 
ATOM   3519 N  N    B LEU   A 1 160 ? 5.414  -2.573  0.628   0.36 20.23 ?  160 LEU   A N    1 
ATOM   3520 N  N    T LEU   A 1 160 ? 4.993  -2.633  1.019   0.30 20.07 ?  160 LEU   A N    1 
ATOM   3521 C  CA   A LEU   A 1 160 ? 5.913  -3.569  0.480   0.34 17.23 ?  160 LEU   A CA   1 
ATOM   3522 C  CA   B LEU   A 1 160 ? 6.357  -3.612  0.225   0.36 19.87 ?  160 LEU   A CA   1 
ATOM   3523 C  CA   T LEU   A 1 160 ? 5.886  -3.641  0.460   0.30 19.65 ?  160 LEU   A CA   1 
ATOM   3524 C  C    A LEU   A 1 160 ? 6.116  -4.708  1.470   0.34 16.13 ?  160 LEU   A C    1 
ATOM   3525 C  C    B LEU   A 1 160 ? 6.335  -4.777  1.207   0.36 19.22 ?  160 LEU   A C    1 
ATOM   3526 O  O    A LEU   A 1 160 ? 6.139  -5.881  1.079   0.34 16.09 ?  160 LEU   A O    1 
ATOM   3527 O  O    B LEU   A 1 160 ? 6.211  -5.942  0.808   0.36 19.08 ?  160 LEU   A O    1 
ATOM   3528 C  CB   A LEU   A 1 160 ? 7.247  -2.923  0.122   0.34 17.46 ?  160 LEU   A CB   1 
ATOM   3529 C  CB   B LEU   A 1 160 ? 7.764  -3.018  0.124   0.36 20.37 ?  160 LEU   A CB   1 
ATOM   3530 C  CB   T LEU   A 1 160 ? 7.238  -3.028  0.106   0.30 19.28 ?  160 LEU   A CB   1 
ATOM   3531 C  CG   A LEU   A 1 160 ? 8.314  -3.920  -0.324  0.34 18.11 ?  160 LEU   A CG   1 
ATOM   3532 C  CG   B LEU   A 1 160 ? 8.910  -4.005  -0.112  0.36 20.98 ?  160 LEU   A CG   1 
ATOM   3533 C  CG   T LEU   A 1 160 ? 8.295  -4.027  -0.359  0.30 19.24 ?  160 LEU   A CG   1 
ATOM   3534 C  CD1  A LEU   A 1 160 ? 7.819  -4.718  -1.514  0.34 18.62 ?  160 LEU   A CD1  1 
ATOM   3535 C  CD1  B LEU   A 1 160 ? 8.605  -4.890  -1.303  0.36 20.87 ?  160 LEU   A CD1  1 
ATOM   3536 C  CD1  T LEU   A 1 160 ? 7.828  -4.766  -1.597  0.30 19.51 ?  160 LEU   A CD1  1 
ATOM   3537 C  CD2  A LEU   A 1 160 ? 9.602  -3.199  -0.651  0.34 17.97 ?  160 LEU   A CD2  1 
ATOM   3538 C  CD2  B LEU   A 1 160 ? 10.232 -3.270  -0.316  0.36 21.26 ?  160 LEU   A CD2  1 
ATOM   3539 C  CD2  T LEU   A 1 160 ? 9.603  -3.312  -0.625  0.30 18.93 ?  160 LEU   A CD2  1 
ATOM   3540 H  H    A LEU   A 1 160 ? 5.337  -1.806  1.198   0.34 21.69 ?  160 LEU   A H    1 
ATOM   3541 H  H    B LEU   A 1 160 ? 5.775  -1.813  0.808   0.36 24.26 ?  160 LEU   A H    1 
ATOM   3542 H  H    T LEU   A 1 160 ? 5.383  -1.906  1.266   0.30 24.06 ?  160 LEU   A H    1 
ATOM   3543 H  HA   A LEU   A 1 160 ? 5.526  -3.936  -0.327  0.34 20.66 ?  160 LEU   A HA   1 
ATOM   3544 H  HA   B LEU   A 1 160 ? 6.106  -3.943  -0.652  0.36 23.83 ?  160 LEU   A HA   1 
ATOM   3545 H  HB2  A LEU   A 1 160 ? 7.109  -2.276  -0.594  0.34 20.93 ?  160 LEU   A HB2  1 
ATOM   3546 H  HB2  B LEU   A 1 160 ? 7.778  -2.381  -0.608  0.36 24.42 ?  160 LEU   A HB2  1 
ATOM   3547 H  HB2  T LEU   A 1 160 ? 7.110  -2.376  -0.604  0.30 23.12 ?  160 LEU   A HB2  1 
ATOM   3548 H  HB3  A LEU   A 1 160 ? 7.585  -2.478  0.910   0.34 20.93 ?  160 LEU   A HB3  1 
ATOM   3549 H  HB3  B LEU   A 1 160 ? 7.955  -2.559  0.955   0.36 24.42 ?  160 LEU   A HB3  1 
ATOM   3550 H  HB3  T LEU   A 1 160 ? 7.585  -2.589  0.896   0.30 23.12 ?  160 LEU   A HB3  1 
ATOM   3551 H  HG   A LEU   A 1 160 ? 8.495  -4.536  0.402   0.34 21.71 ?  160 LEU   A HG   1 
ATOM   3552 H  HG   B LEU   A 1 160 ? 9.008  -4.572  0.669   0.36 25.16 ?  160 LEU   A HG   1 
ATOM   3553 H  HG   T LEU   A 1 160 ? 8.445  -4.677  0.345   0.30 23.08 ?  160 LEU   A HG   1 
ATOM   3554 H  HD11 A LEU   A 1 160 ? 8.541  -5.270  -1.838  0.34 22.32 ?  160 LEU   A HD11 1 
ATOM   3555 H  HD11 B LEU   A 1 160 ? 9.357  -5.481  -1.452  0.36 25.02 ?  160 LEU   A HD11 1 
ATOM   3556 H  HD11 T LEU   A 1 160 ? 8.552  -5.321  -1.923  0.30 23.40 ?  160 LEU   A HD11 1 
ATOM   3557 H  HD12 A LEU   A 1 160 ? 7.075  -5.278  -1.237  0.34 22.32 ?  160 LEU   A HD12 1 
ATOM   3558 H  HD12 B LEU   A 1 160 ? 7.811  -5.412  -1.115  0.36 25.02 ?  160 LEU   A HD12 1 
ATOM   3559 H  HD12 T LEU   A 1 160 ? 7.064  -5.318  -1.366  0.30 23.40 ?  160 LEU   A HD12 1 
ATOM   3560 H  HD13 A LEU   A 1 160 ? 7.529  -4.103  -2.208  0.34 22.32 ?  160 LEU   A HD13 1 
ATOM   3561 H  HD13 B LEU   A 1 160 ? 8.462  -4.331  -2.082  0.36 25.02 ?  160 LEU   A HD13 1 
ATOM   3562 H  HD13 T LEU   A 1 160 ? 7.576  -4.118  -2.274  0.30 23.40 ?  160 LEU   A HD13 1 
ATOM   3563 H  HD21 A LEU   A 1 160 ? 10.264 -3.852  -0.928  0.34 21.54 ?  160 LEU   A HD21 1 
ATOM   3564 H  HD21 B LEU   A 1 160 ? 10.943 -3.921  -0.429  0.36 25.49 ?  160 LEU   A HD21 1 
ATOM   3565 H  HD21 T LEU   A 1 160 ? 10.263 -3.960  -0.916  0.30 22.70 ?  160 LEU   A HD21 1 
ATOM   3566 H  HD22 A LEU   A 1 160 ? 9.438  -2.568  -1.369  0.34 21.54 ?  160 LEU   A HD22 1 
ATOM   3567 H  HD22 B LEU   A 1 160 ? 10.165 -2.713  -1.108  0.36 25.49 ?  160 LEU   A HD22 1 
ATOM   3568 H  HD22 T LEU   A 1 160 ? 9.463  -2.647  -1.318  0.30 22.70 ?  160 LEU   A HD22 1 
ATOM   3569 H  HD23 A LEU   A 1 160 ? 9.912  -2.728  0.139   0.34 21.54 ?  160 LEU   A HD23 1 
ATOM   3570 H  HD23 B LEU   A 1 160 ? 10.410 -2.718  0.462   0.36 25.49 ?  160 LEU   A HD23 1 
ATOM   3571 H  HD23 T LEU   A 1 160 ? 9.900  -2.880  0.192   0.30 22.70 ?  160 LEU   A HD23 1 
ATOM   3572 N  N    A TYR   A 1 161 ? 6.271  -4.384  2.754   0.64 16.92 ?  161 TYR   A N    1 
ATOM   3573 N  N    B TYR   A 1 161 ? 6.469  -4.479  2.500   0.36 18.78 ?  161 TYR   A N    1 
ATOM   3574 C  CA   A TYR   A 1 161 ? 6.415  -5.426  3.762   0.64 16.58 ?  161 TYR   A CA   1 
ATOM   3575 C  CA   B TYR   A 1 161 ? 6.422  -5.522  3.521   0.36 18.72 ?  161 TYR   A CA   1 
ATOM   3576 C  C    A TYR   A 1 161 ? 5.262  -6.418  3.690   0.64 17.29 ?  161 TYR   A C    1 
ATOM   3577 C  C    B TYR   A 1 161 ? 5.155  -6.358  3.386   0.36 20.01 ?  161 TYR   A C    1 
ATOM   3578 O  O    A TYR   A 1 161 ? 5.472  -7.636  3.634   0.64 16.83 ?  161 TYR   A O    1 
ATOM   3579 O  O    B TYR   A 1 161 ? 5.186  -7.583  3.553   0.36 19.95 ?  161 TYR   A O    1 
ATOM   3580 C  CB   A TYR   A 1 161 ? 6.501  -4.811  5.158   0.64 16.74 ?  161 TYR   A CB   1 
ATOM   3581 C  CB   B TYR   A 1 161 ? 6.508  -4.876  4.908   0.36 17.82 ?  161 TYR   A CB   1 
ATOM   3582 C  CG   A TYR   A 1 161 ? 6.402  -5.863  6.223   0.64 16.15 ?  161 TYR   A CG   1 
ATOM   3583 C  CG   B TYR   A 1 161 ? 6.404  -5.832  6.081   0.36 17.13 ?  161 TYR   A CG   1 
ATOM   3584 C  CD1  A TYR   A 1 161 ? 7.477  -6.690  6.497   0.64 16.03 ?  161 TYR   A CD1  1 
ATOM   3585 C  CD1  B TYR   A 1 161 ? 5.165  -6.229  6.571   0.36 17.25 ?  161 TYR   A CD1  1 
ATOM   3586 C  CD2  A TYR   A 1 161 ? 5.221  -6.056  6.936   0.64 15.92 ?  161 TYR   A CD2  1 
ATOM   3587 C  CD2  B TYR   A 1 161 ? 7.544  -6.317  6.716   0.36 16.66 ?  161 TYR   A CD2  1 
ATOM   3588 C  CE1  A TYR   A 1 161 ? 7.393  -7.669  7.451   0.64 15.35 ?  161 TYR   A CE1  1 
ATOM   3589 C  CE1  B TYR   A 1 161 ? 5.063  -7.095  7.643   0.36 17.16 ?  161 TYR   A CE1  1 
ATOM   3590 C  CE2  A TYR   A 1 161 ? 5.127  -7.039  7.897   0.64 16.04 ?  161 TYR   A CE2  1 
ATOM   3591 C  CE2  B TYR   A 1 161 ? 7.451  -7.186  7.791   0.36 16.68 ?  161 TYR   A CE2  1 
ATOM   3592 C  CZ   A TYR   A 1 161 ? 6.218  -7.844  8.148   0.64 15.54 ?  161 TYR   A CZ   1 
ATOM   3593 C  CZ   B TYR   A 1 161 ? 6.207  -7.568  8.251   0.36 17.18 ?  161 TYR   A CZ   1 
ATOM   3594 O  OH   A TYR   A 1 161 ? 6.157  -8.832  9.101   0.64 15.67 ?  161 TYR   A OH   1 
ATOM   3595 O  OH   B TYR   A 1 161 ? 6.115  -8.430  9.320   0.36 18.00 ?  161 TYR   A OH   1 
ATOM   3596 H  H    A TYR   A 1 161 ? 6.287  -3.580  3.062   0.64 20.28 ?  161 TYR   A H    1 
ATOM   3597 H  H    B TYR   A 1 161 ? 6.584  -3.685  2.806   0.36 22.52 ?  161 TYR   A H    1 
ATOM   3598 H  HA   A TYR   A 1 161 ? 7.231  -5.913  3.601   0.64 19.88 ?  161 TYR   A HA   1 
ATOM   3599 H  HA   B TYR   A 1 161 ? 7.190  -6.104  3.410   0.36 22.45 ?  161 TYR   A HA   1 
ATOM   3600 H  HB2  A TYR   A 1 161 ? 7.355  -4.359  5.257   0.64 20.07 ?  161 TYR   A HB2  1 
ATOM   3601 H  HB2  B TYR   A 1 161 ? 7.361  -4.418  4.983   0.36 21.36 ?  161 TYR   A HB2  1 
ATOM   3602 H  HB3  A TYR   A 1 161 ? 5.773  -4.182  5.284   0.64 20.07 ?  161 TYR   A HB3  1 
ATOM   3603 H  HB3  B TYR   A 1 161 ? 5.788  -4.233  4.994   0.36 21.36 ?  161 TYR   A HB3  1 
ATOM   3604 H  HD1  A TYR   A 1 161 ? 8.271  -6.586  6.025   0.64 19.22 ?  161 TYR   A HD1  1 
ATOM   3605 H  HD1  B TYR   A 1 161 ? 4.390  -5.916  6.166   0.36 20.68 ?  161 TYR   A HD1  1 
ATOM   3606 H  HD2  A TYR   A 1 161 ? 4.484  -5.517  6.768   0.64 19.08 ?  161 TYR   A HD2  1 
ATOM   3607 H  HD2  B TYR   A 1 161 ? 8.385  -6.060  6.409   0.36 19.98 ?  161 TYR   A HD2  1 
ATOM   3608 H  HE1  A TYR   A 1 161 ? 8.124  -8.225  7.621   0.64 18.41 ?  161 TYR   A HE1  1 
ATOM   3609 H  HE1  B TYR   A 1 161 ? 4.226  -7.354  7.959   0.36 20.57 ?  161 TYR   A HE1  1 
ATOM   3610 H  HE2  A TYR   A 1 161 ? 4.334  -7.164  8.373   0.64 19.23 ?  161 TYR   A HE2  1 
ATOM   3611 H  HE2  B TYR   A 1 161 ? 8.223  -7.503  8.207   0.36 20.00 ?  161 TYR   A HE2  1 
ATOM   3612 H  HH   A TYR   A 1 161 ? 5.389  -8.850  9.456   0.64 18.79 ?  161 TYR   A HH   1 
ATOM   3613 H  HH   B TYR   A 1 161 ? 5.306  -8.583  9.502   0.36 21.59 ?  161 TYR   A HH   1 
ATOM   3614 N  N    A ASP   A 1 162 ? 4.026  -5.907  3.700   0.64 17.57 ?  162 ASP   A N    1 
ATOM   3615 N  N    B ASP   A 1 162 ? 4.031  -5.709  3.075   0.36 21.13 ?  162 ASP   A N    1 
ATOM   3616 C  CA   A ASP   A 1 162 ? 2.864  -6.788  3.600   0.64 18.13 ?  162 ASP   A CA   1 
ATOM   3617 C  CA   B ASP   A 1 162 ? 2.735  -6.367  2.888   0.36 22.54 ?  162 ASP   A CA   1 
ATOM   3618 C  C    A ASP   A 1 162 ? 2.902  -7.589  2.313   0.64 17.30 ?  162 ASP   A C    1 
ATOM   3619 C  C    B ASP   A 1 162 ? 2.571  -7.002  1.505   0.36 23.09 ?  162 ASP   A C    1 
ATOM   3620 O  O    A ASP   A 1 162 ? 2.556  -8.780  2.299   0.64 17.61 ?  162 ASP   A O    1 
ATOM   3621 O  O    B ASP   A 1 162 ? 1.492  -6.933  0.911   0.36 24.07 ?  162 ASP   A O    1 
ATOM   3622 C  CB   A ASP   A 1 162 ? 1.565  -5.983  3.660   0.64 19.59 ?  162 ASP   A CB   1 
ATOM   3623 C  CB   B ASP   A 1 162 ? 1.617  -5.357  3.144   0.36 23.10 ?  162 ASP   A CB   1 
ATOM   3624 C  CG   A ASP   A 1 162 ? 1.260  -5.465  5.038   0.64 21.38 ?  162 ASP   A CG   1 
ATOM   3625 C  CG   B ASP   A 1 162 ? 1.557  -4.879  4.584   0.36 23.56 ?  162 ASP   A CG   1 
ATOM   3626 O  OD1  A ASP   A 1 162 ? 1.918  -5.890  6.004   0.64 22.21 ?  162 ASP   A OD1  1 
ATOM   3627 O  OD1  B ASP   A 1 162 ? 2.260  -5.449  5.443   0.36 24.08 ?  162 ASP   A OD1  1 
ATOM   3628 O  OD2  A ASP   A 1 162 ? 0.342  -4.629  5.153   0.64 22.58 -1 162 ASP   A OD2  1 
ATOM   3629 O  OD2  B ASP   A 1 162 ? 0.784  -3.932  4.854   0.36 23.31 -1 162 ASP   A OD2  1 
ATOM   3630 H  H    A ASP   A 1 162 ? 3.831  -5.067  3.774   0.64 21.07 ?  162 ASP   A H    1 
ATOM   3631 H  H    B ASP   A 1 162 ? 3.999  -4.859  2.976   0.36 25.34 ?  162 ASP   A H    1 
ATOM   3632 H  HA   A ASP   A 1 162 ? 2.867  -7.413  4.342   0.64 21.74 ?  162 ASP   A HA   1 
ATOM   3633 H  HA   B ASP   A 1 162 ? 2.653  -7.074  3.540   0.36 27.03 ?  162 ASP   A HA   1 
ATOM   3634 H  HB2  A ASP   A 1 162 ? 1.636  -5.215  3.081   0.64 23.49 ?  162 ASP   A HB2  1 
ATOM   3635 H  HB2  B ASP   A 1 162 ? 1.742  -4.593  2.559   0.36 27.70 ?  162 ASP   A HB2  1 
ATOM   3636 H  HB3  A ASP   A 1 162 ? 0.828  -6.551  3.379   0.64 23.49 ?  162 ASP   A HB3  1 
ATOM   3637 H  HB3  B ASP   A 1 162 ? 0.768  -5.778  2.971   0.36 27.70 ?  162 ASP   A HB3  1 
ATOM   3638 N  N    A LYS   A 1 163 ? 3.294  -6.950  1.209   0.64 17.96 ?  163 LYS   A N    1 
ATOM   3639 N  N    B LYS   A 1 163 ? 3.623  -7.621  0.973   0.36 22.16 ?  163 LYS   A N    1 
ATOM   3640 C  CA   A LYS   A 1 163 ? 3.397  -7.699  -0.033  0.64 18.74 ?  163 LYS   A CA   1 
ATOM   3641 C  CA   B LYS   A 1 163 ? 3.567  -8.330  -0.301  0.36 21.01 ?  163 LYS   A CA   1 
ATOM   3642 C  C    A LYS   A 1 163 ? 4.482  -8.763  0.066   0.64 17.59 ?  163 LYS   A C    1 
ATOM   3643 C  C    B LYS   A 1 163 ? 4.599  -9.449  -0.248  0.36 18.39 ?  163 LYS   A C    1 
ATOM   3644 O  O    A LYS   A 1 163 ? 4.319  -9.871  -0.450  0.64 17.30 ?  163 LYS   A O    1 
ATOM   3645 O  O    B LYS   A 1 163 ? 4.366  -10.567 -0.723  0.36 18.57 ?  163 LYS   A O    1 
ATOM   3646 C  CB   A LYS   A 1 163 ? 3.642  -6.774  -1.226  0.64 21.28 ?  163 LYS   A CB   1 
ATOM   3647 C  CB   B LYS   A 1 163 ? 3.871  -7.371  -1.461  0.36 22.82 ?  163 LYS   A CB   1 
ATOM   3648 C  CG   A LYS   A 1 163 ? 3.684  -7.537  -2.544  0.64 24.06 ?  163 LYS   A CG   1 
ATOM   3649 C  CG   B LYS   A 1 163 ? 3.698  -7.982  -2.852  0.36 24.74 ?  163 LYS   A CG   1 
ATOM   3650 C  CD   A LYS   A 1 163 ? 4.097  -6.662  -3.706  0.64 26.30 ?  163 LYS   A CD   1 
ATOM   3651 C  CD   B LYS   A 1 163 ? 4.708  -7.435  -3.862  0.36 26.33 ?  163 LYS   A CD   1 
ATOM   3652 C  CE   A LYS   A 1 163 ? 4.048  -7.436  -5.015  0.64 28.04 ?  163 LYS   A CE   1 
ATOM   3653 C  CE   B LYS   A 1 163 ? 4.294  -6.090  -4.445  0.36 27.55 ?  163 LYS   A CE   1 
ATOM   3654 N  NZ   A LYS   A 1 163 ? 4.679  -6.686  -6.135  0.64 29.05 ?  163 LYS   A NZ   1 
ATOM   3655 N  NZ   B LYS   A 1 163 ? 5.278  -5.606  -5.460  0.36 28.39 ?  163 LYS   A NZ   1 
ATOM   3656 H  H    A LYS   A 1 163 ? 3.484  -6.100  1.155   0.64 21.54 ?  163 LYS   A H    1 
ATOM   3657 H  H    B LYS   A 1 163 ? 4.398  -7.646  1.344   0.36 26.58 ?  163 LYS   A H    1 
ATOM   3658 H  HA   A LYS   A 1 163 ? 2.550  -8.146  -0.185  0.64 22.47 ?  163 LYS   A HA   1 
ATOM   3659 H  HA   B LYS   A 1 163 ? 2.686  -8.714  -0.435  0.36 25.19 ?  163 LYS   A HA   1 
ATOM   3660 H  HB2  A LYS   A 1 163 ? 2.918  -6.121  -1.283  0.64 25.52 ?  163 LYS   A HB2  1 
ATOM   3661 H  HB2  B LYS   A 1 163 ? 3.273  -6.608  -1.402  0.36 27.37 ?  163 LYS   A HB2  1 
ATOM   3662 H  HB3  A LYS   A 1 163 ? 4.486  -6.318  -1.113  0.64 25.52 ?  163 LYS   A HB3  1 
ATOM   3663 H  HB3  B LYS   A 1 163 ? 4.790  -7.069  -1.383  0.36 27.37 ?  163 LYS   A HB3  1 
ATOM   3664 H  HG2  A LYS   A 1 163 ? 4.324  -8.262  -2.478  0.64 28.86 ?  163 LYS   A HG2  1 
ATOM   3665 H  HG2  B LYS   A 1 163 ? 3.817  -8.941  -2.799  0.36 29.67 ?  163 LYS   A HG2  1 
ATOM   3666 H  HG3  A LYS   A 1 163 ? 2.800  -7.894  -2.734  0.64 28.86 ?  163 LYS   A HG3  1 
ATOM   3667 H  HG3  B LYS   A 1 163 ? 2.807  -7.775  -3.180  0.36 29.67 ?  163 LYS   A HG3  1 
ATOM   3668 H  HD2  A LYS   A 1 163 ? 3.490  -5.910  -3.773  0.64 31.54 ?  163 LYS   A HD2  1 
ATOM   3669 H  HD2  B LYS   A 1 163 ? 5.569  -7.320  -3.428  0.36 31.58 ?  163 LYS   A HD2  1 
ATOM   3670 H  HD3  A LYS   A 1 163 ? 5.005  -6.354  -3.566  0.64 31.54 ?  163 LYS   A HD3  1 
ATOM   3671 H  HD3  B LYS   A 1 163 ? 4.789  -8.062  -4.596  0.36 31.58 ?  163 LYS   A HD3  1 
ATOM   3672 H  HE2  A LYS   A 1 163 ? 4.516  -8.278  -4.906  0.64 33.64 ?  163 LYS   A HE2  1 
ATOM   3673 H  HE2  B LYS   A 1 163 ? 3.431  -6.180  -4.881  0.36 33.05 ?  163 LYS   A HE2  1 
ATOM   3674 H  HE3  A LYS   A 1 163 ? 3.123  -7.601  -5.250  0.64 33.64 ?  163 LYS   A HE3  1 
ATOM   3675 H  HE3  B LYS   A 1 163 ? 4.244  -5.431  -3.735  0.36 33.05 ?  163 LYS   A HE3  1 
ATOM   3676 H  HZ1  A LYS   A 1 163 ? 4.635  -7.163  -6.884  0.64 34.85 ?  163 LYS   A HZ1  1 
ATOM   3677 H  HZ1  B LYS   A 1 163 ? 5.018  -4.821  -5.789  0.36 34.05 ?  163 LYS   A HZ1  1 
ATOM   3678 H  HZ2  A LYS   A 1 163 ? 4.254  -5.913  -6.259  0.64 34.85 ?  163 LYS   A HZ2  1 
ATOM   3679 H  HZ2  B LYS   A 1 163 ? 6.080  -5.511  -5.085  0.36 34.05 ?  163 LYS   A HZ2  1 
ATOM   3680 H  HZ3  A LYS   A 1 163 ? 5.533  -6.519  -5.948  0.64 34.85 ?  163 LYS   A HZ3  1 
ATOM   3681 H  HZ3  B LYS   A 1 163 ? 5.340  -6.192  -6.128  0.36 34.05 ?  163 LYS   A HZ3  1 
ATOM   3682 N  N    A LEU   A 1 164 ? 5.596  -8.448  0.729   0.64 15.91 ?  164 LEU   A N    1 
ATOM   3683 N  N    B LEU   A 1 164 ? 5.750  -9.136  0.353   0.36 16.14 ?  164 LEU   A N    1 
ATOM   3684 C  CA   A LEU   A 1 164 ? 6.666  -9.432  0.873   0.64 15.29 ?  164 LEU   A CA   1 
ATOM   3685 C  CA   B LEU   A 1 164 ? 6.800  -10.129 0.535   0.36 14.94 ?  164 LEU   A CA   1 
ATOM   3686 C  C    A LEU   A 1 164 ? 6.223  -10.600 1.742   0.64 15.60 ?  164 LEU   A C    1 
ATOM   3687 C  C    B LEU   A 1 164 ? 6.333  -11.256 1.444   0.36 14.70 ?  164 LEU   A C    1 
ATOM   3688 O  O    A LEU   A 1 164 ? 6.514  -11.760 1.426   0.64 15.79 ?  164 LEU   A O    1 
ATOM   3689 O  O    B LEU   A 1 164 ? 6.634  -12.430 1.198   0.36 14.73 ?  164 LEU   A O    1 
ATOM   3690 C  CB   A LEU   A 1 164 ? 7.894  -8.771  1.483   0.64 14.65 ?  164 LEU   A CB   1 
ATOM   3691 C  CB   B LEU   A 1 164 ? 8.038  -9.462  1.132   0.36 14.74 ?  164 LEU   A CB   1 
ATOM   3692 C  CG   A LEU   A 1 164 ? 8.698  -7.853  0.566   0.64 14.80 ?  164 LEU   A CG   1 
ATOM   3693 C  CG   B LEU   A 1 164 ? 8.803  -8.468  0.260   0.36 15.04 ?  164 LEU   A CG   1 
ATOM   3694 C  CD1  A LEU   A 1 164 ? 9.635  -7.014  1.402   0.64 14.31 ?  164 LEU   A CD1  1 
ATOM   3695 C  CD1  B LEU   A 1 164 ? 9.774  -7.672  1.115   0.36 15.41 ?  164 LEU   A CD1  1 
ATOM   3696 C  CD2  A LEU   A 1 164 ? 9.484  -8.658  -0.462  0.64 15.15 ?  164 LEU   A CD2  1 
ATOM   3697 C  CD2  B LEU   A 1 164 ? 9.546  -9.191  -0.847  0.36 15.38 ?  164 LEU   A CD2  1 
ATOM   3698 H  H    A LEU   A 1 164 ? 5.756  -7.678  1.095   0.64 19.07 ?  164 LEU   A H    1 
ATOM   3699 H  H    B LEU   A 1 164 ? 5.940  -8.359  0.667   0.36 19.35 ?  164 LEU   A H    1 
ATOM   3700 H  HA   A LEU   A 1 164 ? 6.903  -9.768  -0.006  0.64 18.33 ?  164 LEU   A HA   1 
ATOM   3701 H  HA   B LEU   A 1 164 ? 7.031  -10.504 -0.323  0.36 17.92 ?  164 LEU   A HA   1 
ATOM   3702 H  HB2  A LEU   A 1 164 ? 7.609  -8.234  2.238   0.64 17.57 ?  164 LEU   A HB2  1 
ATOM   3703 H  HB2  B LEU   A 1 164 ? 7.765  -8.988  1.931   0.36 17.68 ?  164 LEU   A HB2  1 
ATOM   3704 H  HB3  A LEU   A 1 164 ? 8.493  -9.466  1.785   0.64 17.57 ?  164 LEU   A HB3  1 
ATOM   3705 H  HB3  B LEU   A 1 164 ? 8.661  -10.163 1.375   0.36 17.68 ?  164 LEU   A HB3  1 
ATOM   3706 H  HG   A LEU   A 1 164 ? 8.097  -7.257  0.089   0.64 17.74 ?  164 LEU   A HG   1 
ATOM   3707 H  HG   B LEU   A 1 164 ? 8.178  -7.847  -0.146  0.36 18.03 ?  164 LEU   A HG   1 
ATOM   3708 H  HD11 A LEU   A 1 164 ? 10.130 -6.418  0.822   0.64 17.15 ?  164 LEU   A HD11 1 
ATOM   3709 H  HD11 B LEU   A 1 164 ? 10.261 -7.055  0.549   0.36 18.48 ?  164 LEU   A HD11 1 
ATOM   3710 H  HD12 A LEU   A 1 164 ? 9.110  -6.503  2.037   0.64 17.15 ?  164 LEU   A HD12 1 
ATOM   3711 H  HD12 B LEU   A 1 164 ? 9.277  -7.185  1.789   0.36 18.48 ?  164 LEU   A HD12 1 
ATOM   3712 H  HD13 A LEU   A 1 164 ? 10.244 -7.603  1.874   0.64 17.15 ?  164 LEU   A HD13 1 
ATOM   3713 H  HD13 B LEU   A 1 164 ? 10.393 -8.288  1.542   0.36 18.48 ?  164 LEU   A HD13 1 
ATOM   3714 H  HD21 A LEU   A 1 164 ? 10.018 -8.053  -1.004  0.64 18.16 ?  164 LEU   A HD21 1 
ATOM   3715 H  HD21 B LEU   A 1 164 ? 10.039 -8.542  -1.371  0.36 18.44 ?  164 LEU   A HD21 1 
ATOM   3716 H  HD22 A LEU   A 1 164 ? 10.065 -9.283  0.001   0.64 18.16 ?  164 LEU   A HD22 1 
ATOM   3717 H  HD22 B LEU   A 1 164 ? 10.158 -9.830  -0.449  0.36 18.44 ?  164 LEU   A HD22 1 
ATOM   3718 H  HD23 A LEU   A 1 164 ? 8.864  -9.145  -1.029  0.64 18.16 ?  164 LEU   A HD23 1 
ATOM   3719 H  HD23 B LEU   A 1 164 ? 8.904  -9.652  -1.408  0.36 18.44 ?  164 LEU   A HD23 1 
ATOM   3720 N  N    A VAL   A 1 165 ? 5.540  -10.310 2.850   0.64 15.25 ?  165 VAL   A N    1 
ATOM   3721 N  N    B VAL   A 1 165 ? 5.603  -10.916 2.505   0.36 14.43 ?  165 VAL   A N    1 
ATOM   3722 C  CA   A VAL   A 1 165 ? 5.053  -11.378 3.720   0.64 15.74 ?  165 VAL   A CA   1 
ATOM   3723 C  CA   B VAL   A 1 165 ? 5.114  -11.930 3.431   0.36 14.24 ?  165 VAL   A CA   1 
ATOM   3724 C  C    A VAL   A 1 165 ? 4.018  -12.223 2.992   0.64 15.65 ?  165 VAL   A C    1 
ATOM   3725 C  C    B VAL   A 1 165 ? 4.109  -12.837 2.734   0.36 14.52 ?  165 VAL   A C    1 
ATOM   3726 O  O    A VAL   A 1 165 ? 4.092  -13.457 2.982   0.64 15.53 ?  165 VAL   A O    1 
ATOM   3727 O  O    B VAL   A 1 165 ? 4.255  -14.063 2.721   0.36 14.23 ?  165 VAL   A O    1 
ATOM   3728 C  CB   A VAL   A 1 165 ? 4.501  -10.797 5.034   0.64 16.76 ?  165 VAL   A CB   1 
ATOM   3729 C  CB   B VAL   A 1 165 ? 4.508  -11.256 4.676   0.36 14.79 ?  165 VAL   A CB   1 
ATOM   3730 C  CG1  A VAL   A 1 165 ? 3.679  -11.843 5.779   0.64 17.23 ?  165 VAL   A CG1  1 
ATOM   3731 C  CG1  B VAL   A 1 165 ? 3.899  -12.292 5.621   0.36 15.08 ?  165 VAL   A CG1  1 
ATOM   3732 C  CG2  A VAL   A 1 165 ? 5.643  -10.293 5.898   0.64 17.08 ?  165 VAL   A CG2  1 
ATOM   3733 C  CG2  B VAL   A 1 165 ? 5.557  -10.413 5.386   0.36 15.38 ?  165 VAL   A CG2  1 
ATOM   3734 H  H    A VAL   A 1 165 ? 5.346  -9.511  3.113   0.64 18.29 ?  165 VAL   A H    1 
ATOM   3735 H  H    B VAL   A 1 165 ? 5.361  -10.116 2.703   0.36 17.30 ?  165 VAL   A H    1 
ATOM   3736 H  HA   A VAL   A 1 165 ? 5.797  -11.951 3.943   0.64 18.87 ?  165 VAL   A HA   1 
ATOM   3737 H  HA   B VAL   A 1 165 ? 5.858  -12.478 3.727   0.36 17.07 ?  165 VAL   A HA   1 
ATOM   3738 H  HB   A VAL   A 1 165 ? 3.921  -10.042 4.833   0.64 20.09 ?  165 VAL   A HB   1 
ATOM   3739 H  HB   B VAL   A 1 165 ? 3.796  -10.660 4.396   0.36 17.73 ?  165 VAL   A HB   1 
ATOM   3740 H  HG11 A VAL   A 1 165 ? 3.581  -11.567 6.703   0.64 20.66 ?  165 VAL   A HG11 1 
ATOM   3741 H  HG11 B VAL   A 1 165 ? 3.728  -11.873 6.480   0.36 18.09 ?  165 VAL   A HG11 1 
ATOM   3742 H  HG12 A VAL   A 1 165 ? 2.805  -11.917 5.364   0.64 20.66 ?  165 VAL   A HG12 1 
ATOM   3743 H  HG12 B VAL   A 1 165 ? 3.066  -12.614 5.242   0.36 18.09 ?  165 VAL   A HG12 1 
ATOM   3744 H  HG13 A VAL   A 1 165 ? 4.142  -12.695 5.737   0.64 20.66 ?  165 VAL   A HG13 1 
ATOM   3745 H  HG13 B VAL   A 1 165 ? 4.523  -13.024 5.729   0.36 18.09 ?  165 VAL   A HG13 1 
ATOM   3746 H  HG21 A VAL   A 1 165 ? 5.292  -10.034 6.762   0.64 20.48 ?  165 VAL   A HG21 1 
ATOM   3747 H  HG21 B VAL   A 1 165 ? 5.172  -10.040 6.195   0.36 18.44 ?  165 VAL   A HG21 1 
ATOM   3748 H  HG22 A VAL   A 1 165 ? 6.294  -11.004 6.002   0.64 20.48 ?  165 VAL   A HG22 1 
ATOM   3749 H  HG22 B VAL   A 1 165 ? 6.316  -10.973 5.606   0.36 18.44 ?  165 VAL   A HG22 1 
ATOM   3750 H  HG23 A VAL   A 1 165 ? 6.055  -9.529  5.462   0.64 20.48 ?  165 VAL   A HG23 1 
ATOM   3751 H  HG23 B VAL   A 1 165 ? 5.837  -9.695  4.794   0.36 18.44 ?  165 VAL   A HG23 1 
ATOM   3752 N  N    A SER   A 1 166 ? 3.037  -11.572 2.366   0.64 15.75 ?  166 SER   A N    1 
ATOM   3753 N  N    B SER   A 1 166 ? 3.092  -12.240 2.111   0.36 14.82 ?  166 SER   A N    1 
ATOM   3754 C  CA   A SER   A 1 166 ? 1.933  -12.312 1.764   0.64 16.42 ?  166 SER   A CA   1 
ATOM   3755 C  CA   B SER   A 1 166 ? 1.982  -13.031 1.597   0.36 15.76 ?  166 SER   A CA   1 
ATOM   3756 C  C    A SER   A 1 166 ? 2.357  -13.134 0.557   0.64 16.56 ?  166 SER   A C    1 
ATOM   3757 C  C    B SER   A 1 166 ? 2.422  -13.979 0.493   0.36 15.89 ?  166 SER   A C    1 
ATOM   3758 O  O    A SER   A 1 166 ? 1.665  -14.099 0.215   0.64 18.22 ?  166 SER   A O    1 
ATOM   3759 O  O    B SER   A 1 166 ? 1.873  -15.079 0.371   0.36 16.05 ?  166 SER   A O    1 
ATOM   3760 C  CB   A SER   A 1 166 ? 0.805  -11.366 1.347   0.64 17.59 ?  166 SER   A CB   1 
ATOM   3761 C  CB   B SER   A 1 166 ? 0.839  -12.121 1.132   0.36 16.92 ?  166 SER   A CB   1 
ATOM   3762 O  OG   A SER   A 1 166 ? 0.141  -10.819 2.473   0.64 19.56 ?  166 SER   A OG   1 
ATOM   3763 O  OG   B SER   A 1 166 ? 1.296  -11.019 0.371   0.36 17.98 ?  166 SER   A OG   1 
ATOM   3764 H  H    A SER   A 1 166 ? 2.979  -10.719 2.289   0.64 18.88 ?  166 SER   A H    1 
ATOM   3765 H  H    B SER   A 1 166 ? 3.032  -11.401 1.972   0.36 17.76 ?  166 SER   A H    1 
ATOM   3766 H  HA   A SER   A 1 166 ? 1.569  -12.924 2.424   0.64 19.68 ?  166 SER   A HA   1 
ATOM   3767 H  HA   B SER   A 1 166 ? 1.636  -13.579 2.317   0.36 18.89 ?  166 SER   A HA   1 
ATOM   3768 H  HB2  A SER   A 1 166 ? 1.175  -10.646 0.819   0.64 21.10 ?  166 SER   A HB2  1 
ATOM   3769 H  HB2  B SER   A 1 166 ? 0.241  -12.633 0.570   0.36 20.29 ?  166 SER   A HB2  1 
ATOM   3770 H  HB3  A SER   A 1 166 ? 0.156  -11.864 0.819   0.64 21.10 ?  166 SER   A HB3  1 
ATOM   3771 H  HB3  B SER   A 1 166 ? 0.363  -11.802 1.915   0.36 20.29 ?  166 SER   A HB3  1 
ATOM   3772 H  HG   A SER   A 1 166 ? -0.472 -10.302 2.224   0.64 23.45 ?  166 SER   A HG   1 
ATOM   3773 H  HG   B SER   A 1 166 ? 0.656  -10.521 0.162   0.36 21.56 ?  166 SER   A HG   1 
ATOM   3774 N  N    A SER   A 1 167 ? 3.463  -12.786 -0.101  0.64 15.93 ?  167 SER   A N    1 
ATOM   3775 N  N    B SER   A 1 167 ? 3.412  -13.591 -0.306  0.36 16.18 ?  167 SER   A N    1 
ATOM   3776 C  CA   A SER   A 1 167 ? 3.902  -13.509 -1.287  0.64 16.76 ?  167 SER   A CA   1 
ATOM   3777 C  CA   B SER   A 1 167 ? 3.876  -14.438 -1.394  0.36 16.98 ?  167 SER   A CA   1 
ATOM   3778 C  C    A SER   A 1 167 ? 5.043  -14.475 -1.008  0.64 17.28 ?  167 SER   A C    1 
ATOM   3779 C  C    B SER   A 1 167 ? 5.034  -15.345 -0.992  0.36 17.42 ?  167 SER   A C    1 
ATOM   3780 O  O    A SER   A 1 167 ? 5.526  -15.125 -1.941  0.64 17.70 ?  167 SER   A O    1 
ATOM   3781 O  O    B SER   A 1 167 ? 5.631  -15.982 -1.867  0.36 17.60 ?  167 SER   A O    1 
ATOM   3782 C  CB   A SER   A 1 167 ? 4.326  -12.530 -2.390  0.64 16.92 ?  167 SER   A CB   1 
ATOM   3783 C  CB   B SER   A 1 167 ? 4.276  -13.583 -2.601  0.36 17.50 ?  167 SER   A CB   1 
ATOM   3784 O  OG   A SER   A 1 167 ? 5.413  -11.724 -1.964  0.64 17.37 ?  167 SER   A OG   1 
ATOM   3785 O  OG   B SER   A 1 167 ? 5.362  -12.727 -2.291  0.36 17.67 ?  167 SER   A OG   1 
ATOM   3786 H  H    A SER   A 1 167 ? 3.972  -12.129 0.123   0.64 19.10 ?  167 SER   A H    1 
ATOM   3787 H  H    B SER   A 1 167 ? 3.826  -12.835 -0.240  0.36 19.40 ?  167 SER   A H    1 
ATOM   3788 H  HA   A SER   A 1 167 ? 3.159  -14.027 -1.627  0.64 20.09 ?  167 SER   A HA   1 
ATOM   3789 H  HA   B SER   A 1 167 ? 3.143  -15.006 -1.671  0.36 20.36 ?  167 SER   A HA   1 
ATOM   3790 H  HB2  A SER   A 1 167 ? 4.594  -13.039 -3.172  0.64 20.29 ?  167 SER   A HB2  1 
ATOM   3791 H  HB2  B SER   A 1 167 ? 4.535  -14.174 -3.328  0.36 20.99 ?  167 SER   A HB2  1 
ATOM   3792 H  HB3  A SER   A 1 167 ? 3.564  -11.964 -2.613  0.64 20.29 ?  167 SER   A HB3  1 
ATOM   3793 H  HB3  B SER   A 1 167 ? 3.514  -13.046 -2.871  0.36 20.99 ?  167 SER   A HB3  1 
ATOM   3794 H  HG   A SER   A 1 167 ? 5.173  -11.274 -1.291  0.64 20.83 ?  167 SER   A HG   1 
ATOM   3795 H  HG   B SER   A 1 167 ? 5.146  -12.212 -1.664  0.36 21.18 ?  167 SER   A HG   1 
ATOM   3796 N  N    A PHE   A 1 168 ? 5.489  -14.592 0.239   0.64 17.52 ?  168 PHE   A N    1 
ATOM   3797 N  N    B PHE   A 1 168 ? 5.350  -15.444 0.299   0.36 18.27 ?  168 PHE   A N    1 
ATOM   3798 C  CA   A PHE   A 1 168 ? 6.660  -15.411 0.517   0.64 18.09 ?  168 PHE   A CA   1 
ATOM   3799 C  CA   B PHE   A 1 168 ? 6.584  -16.109 0.703   0.36 19.58 ?  168 PHE   A CA   1 
ATOM   3800 C  C    A PHE   A 1 168 ? 6.322  -16.889 0.403   0.64 19.64 ?  168 PHE   A C    1 
ATOM   3801 C  C    B PHE   A 1 168 ? 6.478  -17.619 0.547   0.36 22.10 ?  168 PHE   A C    1 
ATOM   3802 O  O    A PHE   A 1 168 ? 5.328  -17.357 0.967   0.64 21.07 ?  168 PHE   A O    1 
ATOM   3803 O  O    B PHE   A 1 168 ? 5.528  -18.249 1.021   0.36 22.33 ?  168 PHE   A O    1 
ATOM   3804 C  CB   A PHE   A 1 168 ? 7.207  -15.139 1.912   0.64 17.42 ?  168 PHE   A CB   1 
ATOM   3805 C  CB   B PHE   A 1 168 ? 6.955  -15.752 2.142   0.36 19.11 ?  168 PHE   A CB   1 
ATOM   3806 C  CG   A PHE   A 1 168 ? 8.448  -15.926 2.210   0.64 16.68 ?  168 PHE   A CG   1 
ATOM   3807 C  CG   B PHE   A 1 168 ? 8.310  -16.262 2.561   0.36 19.12 ?  168 PHE   A CG   1 
ATOM   3808 C  CD1  A PHE   A 1 168 ? 9.632  -15.624 1.562   0.64 16.81 ?  168 PHE   A CD1  1 
ATOM   3809 C  CD1  B PHE   A 1 168 ? 9.467  -15.688 2.057   0.36 19.16 ?  168 PHE   A CD1  1 
ATOM   3810 C  CD2  A PHE   A 1 168 ? 8.433  -16.992 3.093   0.64 16.58 ?  168 PHE   A CD2  1 
ATOM   3811 C  CD2  B PHE   A 1 168 ? 8.429  -17.311 3.459   0.36 19.28 ?  168 PHE   A CD2  1 
ATOM   3812 C  CE1  A PHE   A 1 168 ? 10.781 -16.352 1.806   0.64 16.39 ?  168 PHE   A CE1  1 
ATOM   3813 C  CE1  B PHE   A 1 168 ? 10.715 -16.152 2.439   0.36 19.31 ?  168 PHE   A CE1  1 
ATOM   3814 C  CE2  A PHE   A 1 168 ? 9.585  -17.721 3.343   0.64 16.79 ?  168 PHE   A CE2  1 
ATOM   3815 C  CE2  B PHE   A 1 168 ? 9.674  -17.777 3.845   0.36 19.48 ?  168 PHE   A CE2  1 
ATOM   3816 C  CZ   A PHE   A 1 168 ? 10.757 -17.397 2.697   0.64 16.51 ?  168 PHE   A CZ   1 
ATOM   3817 C  CZ   B PHE   A 1 168 ? 10.817 -17.197 3.334   0.36 19.48 ?  168 PHE   A CZ   1 
ATOM   3818 H  H    A PHE   A 1 168 ? 5.138  -14.216 0.927   0.64 21.01 ?  168 PHE   A H    1 
ATOM   3819 H  H    B PHE   A 1 168 ? 4.878  -15.139 0.950   0.36 21.91 ?  168 PHE   A H    1 
ATOM   3820 H  HA   A PHE   A 1 168 ? 7.356  -15.202 -0.130  0.64 21.69 ?  168 PHE   A HA   1 
ATOM   3821 H  HA   B PHE   A 1 168 ? 7.301  -15.809 0.129   0.36 23.48 ?  168 PHE   A HA   1 
ATOM   3822 H  HB2  A PHE   A 1 168 ? 7.422  -14.196 1.990   0.64 20.89 ?  168 PHE   A HB2  1 
ATOM   3823 H  HB2  B PHE   A 1 168 ? 6.965  -14.787 2.230   0.36 22.92 ?  168 PHE   A HB2  1 
ATOM   3824 H  HB3  A PHE   A 1 168 ? 6.534  -15.382 2.566   0.64 20.89 ?  168 PHE   A HB3  1 
ATOM   3825 H  HB3  B PHE   A 1 168 ? 6.299  -16.134 2.743   0.36 22.92 ?  168 PHE   A HB3  1 
ATOM   3826 H  HD1  A PHE   A 1 168 ? 9.660  -14.917 0.956   0.64 20.15 ?  168 PHE   A HD1  1 
ATOM   3827 H  HD1  B PHE   A 1 168 ? 9.408  -14.985 1.453   0.36 22.98 ?  168 PHE   A HD1  1 
ATOM   3828 H  HD2  A PHE   A 1 168 ? 7.644  -17.213 3.533   0.64 19.88 ?  168 PHE   A HD2  1 
ATOM   3829 H  HD2  B PHE   A 1 168 ? 7.664  -17.708 3.808   0.36 23.12 ?  168 PHE   A HD2  1 
ATOM   3830 H  HE1  A PHE   A 1 168 ? 11.576 -16.136 1.370   0.64 19.65 ?  168 PHE   A HE1  1 
ATOM   3831 H  HE1  B PHE   A 1 168 ? 11.486 -15.760 2.094   0.36 23.16 ?  168 PHE   A HE1  1 
ATOM   3832 H  HE2  A PHE   A 1 168 ? 9.563  -18.431 3.945   0.64 20.13 ?  168 PHE   A HE2  1 
ATOM   3833 H  HE2  B PHE   A 1 168 ? 9.740  -18.482 4.449   0.36 23.36 ?  168 PHE   A HE2  1 
ATOM   3834 H  HZ   A PHE   A 1 168 ? 11.531 -17.889 2.863   0.64 19.79 ?  168 PHE   A HZ   1 
ATOM   3835 H  HZ   B PHE   A 1 168 ? 11.656 -17.509 3.593   0.36 23.36 ?  168 PHE   A HZ   1 
ATOM   3836 N  N    A LEU   A 1 169 ? 7.173  -17.634 -0.301  0.64 21.92 ?  169 LEU   A N    1 
ATOM   3837 N  N    B LEU   A 1 169 ? 7.479  -18.195 -0.109  0.36 24.82 ?  169 LEU   A N    1 
ATOM   3838 C  CA   A LEU   A 1 169 ? 6.961  -19.067 -0.438  0.64 25.52 ?  169 LEU   A CA   1 
ATOM   3839 C  CA   B LEU   A 1 169 ? 7.572  -19.629 -0.316  0.36 28.42 ?  169 LEU   A CA   1 
ATOM   3840 C  C    A LEU   A 1 169 ? 7.816  -19.824 0.569   0.64 26.24 ?  169 LEU   A C    1 
ATOM   3841 C  C    B LEU   A 1 169 ? 8.223  -20.278 0.899   0.36 29.80 ?  169 LEU   A C    1 
ATOM   3842 O  O    A LEU   A 1 169 ? 7.283  -20.358 1.543   0.64 26.76 ?  169 LEU   A O    1 
ATOM   3843 O  O    B LEU   A 1 169 ? 7.590  -20.437 1.943   0.36 30.22 ?  169 LEU   A O    1 
ATOM   3844 C  CB   A LEU   A 1 169 ? 7.243  -19.534 -1.871  0.64 27.58 ?  169 LEU   A CB   1 
ATOM   3845 C  CB   B LEU   A 1 169 ? 8.403  -19.904 -1.579  0.36 30.12 ?  169 LEU   A CB   1 
ATOM   3846 C  CG   A LEU   A 1 169 ? 6.968  -21.015 -2.161  0.64 29.39 ?  169 LEU   A CG   1 
ATOM   3847 C  CG   B LEU   A 1 169 ? 7.742  -20.536 -2.809  0.36 31.39 ?  169 LEU   A CG   1 
ATOM   3848 C  CD1  A LEU   A 1 169 ? 5.561  -21.409 -1.734  0.64 30.09 ?  169 LEU   A CD1  1 
ATOM   3849 C  CD1  B LEU   A 1 169 ? 6.230  -20.431 -2.748  0.36 31.89 ?  169 LEU   A CD1  1 
ATOM   3850 C  CD2  A LEU   A 1 169 ? 7.180  -21.326 -3.637  0.64 29.96 ?  169 LEU   A CD2  1 
ATOM   3851 C  CD2  B LEU   A 1 169 ? 8.271  -19.879 -4.079  0.36 31.80 ?  169 LEU   A CD2  1 
ATOM   3852 O  OXT  A LEU   A 1 169 ? 9.041  -19.903 0.448   0.64 25.80 -1 169 LEU   A OXT  1 
ATOM   3853 O  OXT  B LEU   A 1 169 ? 9.395  -20.653 0.873   0.36 30.02 -1 169 LEU   A OXT  1 
ATOM   3854 H  H    A LEU   A 1 169 ? 7.874  -17.332 -0.706  0.64 26.29 ?  169 LEU   A H    1 
ATOM   3855 H  H    B LEU   A 1 169 ? 8.134  -17.759 -0.453  0.36 29.77 ?  169 LEU   A H    1 
ATOM   3856 H  HA   A LEU   A 1 169 ? 6.038  -19.266 -0.238  0.64 30.61 ?  169 LEU   A HA   1 
ATOM   3857 H  HA   B LEU   A 1 169 ? 6.681  -20.002 -0.405  0.36 34.09 ?  169 LEU   A HA   1 
ATOM   3858 H  HB2  A LEU   A 1 169 ? 6.684  -19.017 -2.475  0.64 33.08 ?  169 LEU   A HB2  1 
ATOM   3859 H  HB2  B LEU   A 1 169 ? 8.771  -19.058 -1.879  0.36 36.13 ?  169 LEU   A HB2  1 
ATOM   3860 H  HB3  A LEU   A 1 169 ? 8.174  -19.370 -2.074  0.64 33.08 ?  169 LEU   A HB3  1 
ATOM   3861 H  HB3  B LEU   A 1 169 ? 9.135  -20.484 -1.335  0.36 36.13 ?  169 LEU   A HB3  1 
ATOM   3862 H  HG   A LEU   A 1 169 ? 7.593  -21.556 -1.654  0.64 35.25 ?  169 LEU   A HG   1 
ATOM   3863 H  HG   B LEU   A 1 169 ? 7.979  -21.477 -2.846  0.36 37.66 ?  169 LEU   A HG   1 
ATOM   3864 H  HD11 A LEU   A 1 169 ? 5.359  -22.291 -2.084  0.64 36.10 ?  169 LEU   A HD11 1 
ATOM   3865 H  HD11 B LEU   A 1 169 ? 5.870  -20.633 -3.618  0.36 38.25 ?  169 LEU   A HD11 1 
ATOM   3866 H  HD12 A LEU   A 1 169 ? 5.515  -21.421 -0.765  0.64 36.10 ?  169 LEU   A HD12 1 
ATOM   3867 H  HD12 B LEU   A 1 169 ? 5.899  -21.069 -2.094  0.36 38.25 ?  169 LEU   A HD12 1 
ATOM   3868 H  HD13 A LEU   A 1 169 ? 4.930  -20.762 -2.089  0.64 36.10 ?  169 LEU   A HD13 1 
ATOM   3869 H  HD13 B LEU   A 1 169 ? 5.988  -19.527 -2.488  0.36 38.25 ?  169 LEU   A HD13 1 
ATOM   3870 H  HD21 A LEU   A 1 169 ? 7.005  -22.269 -3.790  0.64 35.93 ?  169 LEU   A HD21 1 
ATOM   3871 H  HD21 B LEU   A 1 169 ? 7.878  -20.318 -4.850  0.36 38.14 ?  169 LEU   A HD21 1 
ATOM   3872 H  HD22 A LEU   A 1 169 ? 6.568  -20.788 -4.164  0.64 35.93 ?  169 LEU   A HD22 1 
ATOM   3873 H  HD22 B LEU   A 1 169 ? 8.027  -18.939 -4.074  0.36 38.14 ?  169 LEU   A HD22 1 
ATOM   3874 H  HD23 A LEU   A 1 169 ? 8.096  -21.117 -3.876  0.64 35.93 ?  169 LEU   A HD23 1 
ATOM   3875 H  HD23 B LEU   A 1 169 ? 9.237  -19.969 -4.106  0.36 38.14 ?  169 LEU   A HD23 1 
ATOM   3876 N  N    A SER   B 1 1   ? 50.779 -9.267  -23.703 0.64 28.80 ?  1   SER   B N    1 
ATOM   3877 N  N    B SER   B 1 1   ? 50.738 -9.325  -23.681 0.36 27.05 ?  1   SER   B N    1 
ATOM   3878 C  CA   A SER   B 1 1   ? 51.293 -10.311 -22.791 0.64 28.69 ?  1   SER   B CA   1 
ATOM   3879 C  CA   B SER   B 1 1   ? 51.257 -10.314 -22.712 0.36 26.93 ?  1   SER   B CA   1 
ATOM   3880 C  C    A SER   B 1 1   ? 50.231 -11.372 -22.525 0.64 27.71 ?  1   SER   B C    1 
ATOM   3881 C  C    B SER   B 1 1   ? 50.228 -11.406 -22.469 0.36 26.40 ?  1   SER   B C    1 
ATOM   3882 O  O    A SER   B 1 1   ? 49.034 -11.165 -22.763 0.64 27.66 ?  1   SER   B O    1 
ATOM   3883 O  O    B SER   B 1 1   ? 49.026 -11.213 -22.676 0.36 26.44 ?  1   SER   B O    1 
ATOM   3884 C  CB   A SER   B 1 1   ? 51.750 -9.695  -21.472 0.64 29.35 ?  1   SER   B CB   1 
ATOM   3885 C  CB   B SER   B 1 1   ? 51.610 -9.640  -21.390 0.36 27.20 ?  1   SER   B CB   1 
ATOM   3886 O  OG   A SER   B 1 1   ? 50.643 -9.430  -20.631 0.64 30.77 ?  1   SER   B OG   1 
ATOM   3887 O  OG   B SER   B 1 1   ? 50.467 -9.525  -20.564 0.36 27.96 ?  1   SER   B OG   1 
ATOM   3888 H  H1   A SER   B 1 1   ? 50.675 -9.616  -24.513 0.64 34.54 ?  1   SER   B H1   1 
ATOM   3889 H  H1   B SER   B 1 1   ? 50.649 -9.716  -24.474 0.36 32.45 ?  1   SER   B H1   1 
ATOM   3890 H  H2   A SER   B 1 1   ? 50.001 -8.975  -23.397 0.64 34.54 ?  1   SER   B H2   1 
ATOM   3891 H  H2   B SER   B 1 1   ? 49.952 -9.028  -23.400 0.36 32.45 ?  1   SER   B H2   1 
ATOM   3892 H  H3   A SER   B 1 1   ? 51.363 -8.599  -23.735 0.64 34.54 ?  1   SER   B H3   1 
ATOM   3893 H  H3   B SER   B 1 1   ? 51.315 -8.653  -23.740 0.36 32.45 ?  1   SER   B H3   1 
ATOM   3894 H  HA   A SER   B 1 1   ? 52.057 -10.729 -23.215 0.64 34.41 ?  1   SER   B HA   1 
ATOM   3895 H  HA   B SER   B 1 1   ? 52.055 -10.714 -23.081 0.36 32.30 ?  1   SER   B HA   1 
ATOM   3896 H  HB2  A SER   B 1 1   ? 52.340 -10.320 -21.028 0.64 35.20 ?  1   SER   B HB2  1 
ATOM   3897 H  HB2  B SER   B 1 1   ? 52.278 -10.178 -20.940 0.36 32.62 ?  1   SER   B HB2  1 
ATOM   3898 H  HB3  A SER   B 1 1   ? 52.219 -8.865  -21.654 0.64 35.20 ?  1   SER   B HB3  1 
ATOM   3899 H  HB3  B SER   B 1 1   ? 51.960 -8.754  -21.570 0.36 32.62 ?  1   SER   B HB3  1 
ATOM   3900 H  HG   A SER   B 1 1   ? 50.899 -9.004  -19.954 0.64 36.91 ?  1   SER   B HG   1 
ATOM   3901 H  HG   B SER   B 1 1   ? 50.648 -9.048  -19.897 0.36 33.54 ?  1   SER   B HG   1 
ATOM   3902 N  N    A MET   B 1 2   ? 50.688 -12.507 -22.014 0.64 26.98 ?  2   MET   B N    1 
ATOM   3903 N  N    B MET   B 1 2   ? 50.714 -12.555 -22.019 0.36 25.84 ?  2   MET   B N    1 
ATOM   3904 C  CA   A MET   B 1 2   ? 49.871 -13.703 -21.859 0.64 27.16 ?  2   MET   B CA   1 
ATOM   3905 C  CA   B MET   B 1 2   ? 49.890 -13.740 -21.834 0.36 25.69 ?  2   MET   B CA   1 
ATOM   3906 C  C    A MET   B 1 2   ? 49.611 -13.920 -20.374 0.64 25.02 ?  2   MET   B C    1 
ATOM   3907 C  C    B MET   B 1 2   ? 49.618 -13.901 -20.348 0.36 24.19 ?  2   MET   B C    1 
ATOM   3908 O  O    A MET   B 1 2   ? 50.533 -14.237 -19.617 0.64 25.31 ?  2   MET   B O    1 
ATOM   3909 O  O    B MET   B 1 2   ? 50.539 -14.153 -19.565 0.36 24.32 ?  2   MET   B O    1 
ATOM   3910 C  CB   A MET   B 1 2   ? 50.603 -14.890 -22.470 0.64 30.52 ?  2   MET   B CB   1 
ATOM   3911 C  CB   B MET   B 1 2   ? 50.627 -14.950 -22.382 0.36 27.60 ?  2   MET   B CB   1 
ATOM   3912 C  CG   A MET   B 1 2   ? 49.765 -16.147 -22.620 0.64 33.73 ?  2   MET   B CG   1 
ATOM   3913 C  CG   B MET   B 1 2   ? 49.735 -16.122 -22.770 0.36 29.20 ?  2   MET   B CG   1 
ATOM   3914 S  SD   A MET   B 1 2   ? 50.605 -17.360 -23.655 0.64 36.80 ?  2   MET   B SD   1 
ATOM   3915 S  SD   B MET   B 1 2   ? 50.586 -17.189 -23.935 0.36 30.58 ?  2   MET   B SD   1 
ATOM   3916 C  CE   A MET   B 1 2   ? 51.109 -16.303 -25.007 0.64 37.05 ?  2   MET   B CE   1 
ATOM   3917 C  CE   B MET   B 1 2   ? 51.431 -15.955 -24.903 0.36 30.97 ?  2   MET   B CE   1 
ATOM   3918 H  H    A MET   B 1 2   ? 51.499 -12.614 -21.742 0.64 32.36 ?  2   MET   B H    1 
ATOM   3919 H  H    B MET   B 1 2   ? 51.541 -12.682 -21.806 0.36 30.99 ?  2   MET   B H    1 
ATOM   3920 H  HA   A MET   B 1 2   ? 49.033 -13.590 -22.331 0.64 32.58 ?  2   MET   B HA   1 
ATOM   3921 H  HA   B MET   B 1 2   ? 49.060 -13.652 -22.327 0.36 30.81 ?  2   MET   B HA   1 
ATOM   3922 H  HB2  A MET   B 1 2   ? 50.911 -14.604 -23.341 0.64 36.60 ?  2   MET   B HB2  1 
ATOM   3923 H  HB2  B MET   B 1 2   ? 51.130 -14.607 -23.130 0.36 33.10 ?  2   MET   B HB2  1 
ATOM   3924 H  HB3  A MET   B 1 2   ? 51.363 -15.122 -21.920 0.64 36.60 ?  2   MET   B HB3  1 
ATOM   3925 H  HB3  B MET   B 1 2   ? 51.239 -15.293 -21.730 0.36 33.10 ?  2   MET   B HB3  1 
ATOM   3926 H  HG2  A MET   B 1 2   ? 49.614 -16.539 -21.741 0.64 40.45 ?  2   MET   B HG2  1 
ATOM   3927 H  HG2  B MET   B 1 2   ? 49.521 -16.645 -21.972 0.36 35.02 ?  2   MET   B HG2  1 
ATOM   3928 H  HG3  A MET   B 1 2   ? 48.919 -15.928 -23.040 0.64 40.45 ?  2   MET   B HG3  1 
ATOM   3929 H  HG3  B MET   B 1 2   ? 48.921 -15.806 -23.190 0.36 35.02 ?  2   MET   B HG3  1 
ATOM   3930 H  HE1  A MET   B 1 2   ? 51.246 -16.847 -25.785 0.64 44.45 ?  2   MET   B HE1  1 
ATOM   3931 H  HE1  B MET   B 1 2   ? 51.582 -16.345 -25.745 0.36 37.14 ?  2   MET   B HE1  1 
ATOM   3932 H  HE2  A MET   B 1 2   ? 50.404 -15.652 -25.172 0.64 44.45 ?  2   MET   B HE2  1 
ATOM   3933 H  HE2  B MET   B 1 2   ? 50.859 -15.171 -25.012 0.36 37.14 ?  2   MET   B HE2  1 
ATOM   3934 H  HE3  A MET   B 1 2   ? 51.933 -15.840 -24.769 0.64 44.45 ?  2   MET   B HE3  1 
ATOM   3935 H  HE3  B MET   B 1 2   ? 52.278 -15.704 -24.473 0.36 37.14 ?  2   MET   B HE3  1 
ATOM   3936 N  N    . VAL   B 1 3   ? 48.359 -13.734 -19.962 1.00 22.59 ?  3   VAL   B N    1 
ATOM   3937 C  CA   . VAL   B 1 3   ? 47.935 -13.954 -18.588 1.00 21.12 ?  3   VAL   B CA   1 
ATOM   3938 C  C    . VAL   B 1 3   ? 46.694 -14.834 -18.609 1.00 19.06 ?  3   VAL   B C    1 
ATOM   3939 O  O    . VAL   B 1 3   ? 45.961 -14.903 -19.599 1.00 19.72 ?  3   VAL   B O    1 
ATOM   3940 C  CB   . VAL   B 1 3   ? 47.653 -12.637 -17.836 1.00 22.30 ?  3   VAL   B CB   1 
ATOM   3941 C  CG1  . VAL   B 1 3   ? 48.928 -11.791 -17.715 1.00 22.70 ?  3   VAL   B CG1  1 
ATOM   3942 C  CG2  . VAL   B 1 3   ? 46.545 -11.861 -18.525 1.00 22.88 ?  3   VAL   B CG2  1 
ATOM   3943 H  H    A VAL   B 1 3   ? 47.723 -13.483 -20.484 0.64 27.09 ?  3   VAL   B H    1 
ATOM   3944 H  H    B VAL   B 1 3   ? 47.728 -13.483 -20.490 0.36 27.09 ?  3   VAL   B H    1 
ATOM   3945 H  HA   . VAL   B 1 3   ? 48.634 -14.431 -18.114 1.00 25.32 ?  3   VAL   B HA   1 
ATOM   3946 H  HB   . VAL   B 1 3   ? 47.354 -12.856 -16.939 1.00 26.74 ?  3   VAL   B HB   1 
ATOM   3947 H  HG11 . VAL   B 1 3   ? 48.717 -10.979 -17.231 1.00 27.23 ?  3   VAL   B HG11 1 
ATOM   3948 H  HG12 . VAL   B 1 3   ? 49.598 -12.301 -17.232 1.00 27.23 ?  3   VAL   B HG12 1 
ATOM   3949 H  HG13 . VAL   B 1 3   ? 49.248 -11.579 -18.603 1.00 27.23 ?  3   VAL   B HG13 1 
ATOM   3950 H  HG21 . VAL   B 1 3   ? 46.478 -10.987 -18.119 1.00 27.44 ?  3   VAL   B HG21 1 
ATOM   3951 H  HG22 . VAL   B 1 3   ? 46.757 -11.777 -19.467 1.00 27.44 ?  3   VAL   B HG22 1 
ATOM   3952 H  HG23 . VAL   B 1 3   ? 45.708 -12.342 -18.417 1.00 27.44 ?  3   VAL   B HG23 1 
ATOM   3953 N  N    . ASN   B 1 4   ? 46.465 -15.515 -17.491 1.00 17.05 ?  4   ASN   B N    1 
ATOM   3954 C  CA   . ASN   B 1 4   ? 45.322 -16.419 -17.365 1.00 16.32 ?  4   ASN   B CA   1 
ATOM   3955 C  C    . ASN   B 1 4   ? 45.258 -17.386 -18.544 1.00 16.63 ?  4   ASN   B C    1 
ATOM   3956 O  O    . ASN   B 1 4   ? 44.201 -17.621 -19.122 1.00 17.21 ?  4   ASN   B O    1 
ATOM   3957 C  CB   . ASN   B 1 4   ? 44.009 -15.644 -17.214 1.00 15.64 ?  4   ASN   B CB   1 
ATOM   3958 C  CG   . ASN   B 1 4   ? 43.958 -14.834 -15.929 1.00 15.05 ?  4   ASN   B CG   1 
ATOM   3959 O  OD1  . ASN   B 1 4   ? 44.235 -15.348 -14.845 1.00 15.02 ?  4   ASN   B OD1  1 
ATOM   3960 N  ND2  . ASN   B 1 4   ? 43.624 -13.553 -16.051 1.00 16.30 ?  4   ASN   B ND2  1 
ATOM   3961 H  H    . ASN   B 1 4   ? 46.963 -15.482 -16.792 1.00 20.44 ?  4   ASN   B H    1 
ATOM   3962 H  HA   . ASN   B 1 4   ? 45.443 -16.953 -16.563 1.00 19.57 ?  4   ASN   B HA   1 
ATOM   3963 H  HB2  . ASN   B 1 4   ? 43.918 -15.032 -17.962 1.00 18.75 ?  4   ASN   B HB2  1 
ATOM   3964 H  HB3  . ASN   B 1 4   ? 43.271 -16.272 -17.207 1.00 18.75 ?  4   ASN   B HB3  1 
ATOM   3965 H  HD21 . ASN   B 1 4   ? 43.586 -13.050 -15.352 1.00 19.54 ?  4   ASN   B HD21 1 
ATOM   3966 H  HD22 . ASN   B 1 4   ? 43.446 -13.221 -16.825 1.00 19.54 ?  4   ASN   B HD22 1 
ATOM   3967 N  N    . SER   B 1 5   ? 46.412 -17.943 -18.913 1.00 17.53 ?  5   SER   B N    1 
ATOM   3968 C  CA   . SER   B 1 5   ? 46.507 -18.859 -20.050 1.00 19.93 ?  5   SER   B CA   1 
ATOM   3969 C  C    . SER   B 1 5   ? 46.490 -20.275 -19.491 1.00 21.56 ?  5   SER   B C    1 
ATOM   3970 O  O    . SER   B 1 5   ? 47.514 -20.942 -19.374 1.00 23.37 ?  5   SER   B O    1 
ATOM   3971 C  CB   . SER   B 1 5   ? 47.768 -18.577 -20.864 1.00 21.53 ?  5   SER   B CB   1 
ATOM   3972 O  OG   . SER   B 1 5   ? 48.934 -18.744 -20.078 1.00 24.27 ?  5   SER   B OG   1 
ATOM   3973 H  H    . SER   B 1 5   ? 47.163 -17.811 -18.517 1.00 21.02 ?  5   SER   B H    1 
ATOM   3974 H  HA   . SER   B 1 5   ? 45.737 -18.746 -20.626 1.00 23.90 ?  5   SER   B HA   1 
ATOM   3975 H  HB2  . SER   B 1 5   ? 47.798 -19.189 -21.618 1.00 25.82 ?  5   SER   B HB2  1 
ATOM   3976 H  HB3  . SER   B 1 5   ? 47.727 -17.663 -21.185 1.00 25.82 ?  5   SER   B HB3  1 
ATOM   3977 H  HG   . SER   B 1 5   ? 48.990 -19.540 -19.818 1.00 29.11 ?  5   SER   B HG   1 
ATOM   3978 N  N    . PHE   B 1 6   ? 45.294 -20.713 -19.109 1.00 22.59 ?  6   PHE   B N    1 
ATOM   3979 C  CA   . PHE   B 1 6   ? 45.095 -22.053 -18.579 1.00 22.66 ?  6   PHE   B CA   1 
ATOM   3980 C  C    . PHE   B 1 6   ? 45.008 -23.031 -19.742 1.00 26.58 ?  6   PHE   B C    1 
ATOM   3981 O  O    . PHE   B 1 6   ? 44.312 -22.770 -20.727 1.00 28.43 ?  6   PHE   B O    1 
ATOM   3982 C  CB   . PHE   B 1 6   ? 43.806 -22.097 -17.758 1.00 20.70 ?  6   PHE   B CB   1 
ATOM   3983 C  CG   . PHE   B 1 6   ? 43.835 -21.226 -16.532 1.00 18.71 ?  6   PHE   B CG   1 
ATOM   3984 C  CD1  . PHE   B 1 6   ? 44.347 -21.705 -15.340 1.00 17.71 ?  6   PHE   B CD1  1 
ATOM   3985 C  CD2  . PHE   B 1 6   ? 43.349 -19.927 -16.575 1.00 17.93 ?  6   PHE   B CD2  1 
ATOM   3986 C  CE1  . PHE   B 1 6   ? 44.364 -20.907 -14.206 1.00 16.88 ?  6   PHE   B CE1  1 
ATOM   3987 C  CE2  . PHE   B 1 6   ? 43.371 -19.122 -15.452 1.00 18.16 ?  6   PHE   B CE2  1 
ATOM   3988 C  CZ   . PHE   B 1 6   ? 43.885 -19.604 -14.268 1.00 17.44 ?  6   PHE   B CZ   1 
ATOM   3989 H  H    . PHE   B 1 6   ? 44.571 -20.249 -19.152 1.00 27.10 ?  6   PHE   B H    1 
ATOM   3990 H  HA   . PHE   B 1 6   ? 45.837 -22.306 -18.013 1.00 27.18 ?  6   PHE   B HA   1 
ATOM   3991 H  HB2  . PHE   B 1 6   ? 43.067 -21.800 -18.314 1.00 24.82 ?  6   PHE   B HB2  1 
ATOM   3992 H  HB3  . PHE   B 1 6   ? 43.647 -23.010 -17.467 1.00 24.82 ?  6   PHE   B HB3  1 
ATOM   3993 H  HD1  . PHE   B 1 6   ? 44.680 -22.572 -15.297 1.00 21.24 ?  6   PHE   B HD1  1 
ATOM   3994 H  HD2  . PHE   B 1 6   ? 42.996 -19.597 -17.367 1.00 21.50 ?  6   PHE   B HD2  1 
ATOM   3995 H  HE1  . PHE   B 1 6   ? 44.722 -21.233 -13.410 1.00 20.24 ?  6   PHE   B HE1  1 
ATOM   3996 H  HE2  . PHE   B 1 6   ? 43.034 -18.255 -15.492 1.00 21.78 ?  6   PHE   B HE2  1 
ATOM   3997 H  HZ   . PHE   B 1 6   ? 43.897 -19.069 -13.508 1.00 20.92 ?  6   PHE   B HZ   1 
ATOM   3998 N  N    A SER   B 1 7   ? 45.723 -24.149 -19.629 0.64 27.39 ?  7   SER   B N    1 
ATOM   3999 N  N    B SER   B 1 7   ? 45.726 -24.148 -19.634 0.36 27.78 ?  7   SER   B N    1 
ATOM   4000 C  CA   A SER   B 1 7   ? 45.796 -25.137 -20.696 0.64 29.21 ?  7   SER   B CA   1 
ATOM   4001 C  CA   B SER   B 1 7   ? 45.778 -25.132 -20.705 0.36 29.36 ?  7   SER   B CA   1 
ATOM   4002 C  C    A SER   B 1 7   ? 45.740 -26.539 -20.106 0.64 28.61 ?  7   SER   B C    1 
ATOM   4003 C  C    B SER   B 1 7   ? 45.751 -26.536 -20.120 0.36 28.95 ?  7   SER   B C    1 
ATOM   4004 O  O    A SER   B 1 7   ? 46.342 -26.810 -19.063 0.64 28.88 ?  7   SER   B O    1 
ATOM   4005 O  O    B SER   B 1 7   ? 46.386 -26.806 -19.097 0.36 29.26 ?  7   SER   B O    1 
ATOM   4006 C  CB   A SER   B 1 7   ? 47.090 -24.966 -21.506 0.64 31.28 ?  7   SER   B CB   1 
ATOM   4007 C  CB   B SER   B 1 7   ? 47.042 -24.947 -21.557 0.36 30.96 ?  7   SER   B CB   1 
ATOM   4008 O  OG   A SER   B 1 7   ? 47.143 -25.881 -22.587 0.64 32.86 ?  7   SER   B OG   1 
ATOM   4009 O  OG   B SER   B 1 7   ? 46.960 -25.693 -22.759 0.36 32.07 ?  7   SER   B OG   1 
ATOM   4010 H  H    A SER   B 1 7   ? 46.190 -24.355 -18.935 0.64 32.86 ?  7   SER   B H    1 
ATOM   4011 H  H    B SER   B 1 7   ? 46.201 -24.354 -18.946 0.36 33.33 ?  7   SER   B H    1 
ATOM   4012 H  HA   A SER   B 1 7   ? 45.044 -25.026 -21.295 0.64 35.04 ?  7   SER   B HA   1 
ATOM   4013 H  HA   B SER   B 1 7   ? 45.007 -25.026 -21.280 0.36 35.22 ?  7   SER   B HA   1 
ATOM   4014 H  HB2  A SER   B 1 7   ? 47.124 -24.061 -21.860 0.64 37.52 ?  7   SER   B HB2  1 
ATOM   4015 H  HB2  B SER   B 1 7   ? 47.141 -24.006 -21.777 0.36 37.14 ?  7   SER   B HB2  1 
ATOM   4016 H  HB3  A SER   B 1 7   ? 47.851 -25.120 -20.924 0.64 37.52 ?  7   SER   B HB3  1 
ATOM   4017 H  HB3  B SER   B 1 7   ? 47.812 -25.250 -21.051 0.36 37.14 ?  7   SER   B HB3  1 
ATOM   4018 H  HG   A SER   B 1 7   ? 47.856 -25.775 -23.019 0.64 39.41 ?  7   SER   B HG   1 
ATOM   4019 H  HG   B SER   B 1 7   ? 47.657 -25.581 -23.216 0.36 38.47 ?  7   SER   B HG   1 
ATOM   4020 N  N    . GLY   B 1 8   ? 45.012 -27.426 -20.780 1.00 28.40 ?  8   GLY   B N    1 
ATOM   4021 C  CA   . GLY   B 1 8   ? 44.959 -28.813 -20.372 1.00 27.32 ?  8   GLY   B CA   1 
ATOM   4022 C  C    . GLY   B 1 8   ? 44.008 -29.125 -19.246 1.00 25.74 ?  8   GLY   B C    1 
ATOM   4023 O  O    . GLY   B 1 8   ? 44.137 -30.188 -18.625 1.00 26.99 ?  8   GLY   B O    1 
ATOM   4024 H  H    A GLY   B 1 8   ? 44.544 -27.240 -21.475 0.64 34.06 ?  8   GLY   B H    1 
ATOM   4025 H  H    B GLY   B 1 8   ? 44.538 -27.241 -21.471 0.36 34.06 ?  8   GLY   B H    1 
ATOM   4026 H  HA2  . GLY   B 1 8   ? 44.694 -29.350 -21.130 1.00 32.77 ?  8   GLY   B HA2  1 
ATOM   4027 H  HA3  . GLY   B 1 8   ? 45.843 -29.092 -20.094 1.00 32.77 ?  8   GLY   B HA3  1 
ATOM   4028 N  N    . TYR   B 1 9   ? 43.031 -28.263 -18.978 1.00 24.10 ?  9   TYR   B N    1 
ATOM   4029 C  CA   . TYR   B 1 9   ? 42.082 -28.526 -17.909 1.00 22.14 ?  9   TYR   B CA   1 
ATOM   4030 C  C    . TYR   B 1 9   ? 40.890 -29.316 -18.415 1.00 21.73 ?  9   TYR   B C    1 
ATOM   4031 O  O    . TYR   B 1 9   ? 40.461 -29.177 -19.564 1.00 23.40 ?  9   TYR   B O    1 
ATOM   4032 C  CB   . TYR   B 1 9   ? 41.585 -27.236 -17.265 1.00 21.68 ?  9   TYR   B CB   1 
ATOM   4033 C  CG   . TYR   B 1 9   ? 42.612 -26.622 -16.350 1.00 21.04 ?  9   TYR   B CG   1 
ATOM   4034 C  CD1  . TYR   B 1 9   ? 43.721 -25.967 -16.867 1.00 21.36 ?  9   TYR   B CD1  1 
ATOM   4035 C  CD2  . TYR   B 1 9   ? 42.487 -26.709 -14.972 1.00 20.34 ?  9   TYR   B CD2  1 
ATOM   4036 C  CE1  . TYR   B 1 9   ? 44.675 -25.409 -16.038 1.00 21.40 ?  9   TYR   B CE1  1 
ATOM   4037 C  CE2  . TYR   B 1 9   ? 43.440 -26.157 -14.132 1.00 20.30 ?  9   TYR   B CE2  1 
ATOM   4038 C  CZ   . TYR   B 1 9   ? 44.534 -25.503 -14.672 1.00 21.07 ?  9   TYR   B CZ   1 
ATOM   4039 O  OH   . TYR   B 1 9   ? 45.491 -24.951 -13.852 1.00 21.51 ?  9   TYR   B OH   1 
ATOM   4040 H  H    . TYR   B 1 9   ? 42.875 -27.538 -19.414 1.00 28.90 ?  9   TYR   B H    1 
ATOM   4041 H  HA   . TYR   B 1 9   ? 42.508 -29.054 -17.222 1.00 26.55 ?  9   TYR   B HA   1 
ATOM   4042 H  HB2  . TYR   B 1 9   ? 41.360 -26.591 -17.956 1.00 26.00 ?  9   TYR   B HB2  1 
ATOM   4043 H  HB3  . TYR   B 1 9   ? 40.799 -27.444 -16.737 1.00 26.00 ?  9   TYR   B HB3  1 
ATOM   4044 H  HD1  . TYR   B 1 9   ? 43.818 -25.906 -17.791 1.00 25.62 ?  9   TYR   B HD1  1 
ATOM   4045 H  HD2  . TYR   B 1 9   ? 41.746 -27.150 -14.608 1.00 24.40 ?  9   TYR   B HD2  1 
ATOM   4046 H  HE1  . TYR   B 1 9   ? 45.406 -24.983 -16.403 1.00 25.66 ?  9   TYR   B HE1  1 
ATOM   4047 H  HE2  . TYR   B 1 9   ? 43.333 -26.227 -13.211 1.00 24.35 ?  9   TYR   B HE2  1 
ATOM   4048 H  HH   . TYR   B 1 9   ? 46.083 -24.603 -14.320 1.00 25.80 ?  9   TYR   B HH   1 
ATOM   4049 N  N    . LEU   B 1 10  ? 40.367 -30.160 -17.532 1.00 20.28 ?  10  LEU   B N    1 
ATOM   4050 C  CA   . LEU   B 1 10  ? 39.161 -30.923 -17.789 1.00 20.21 ?  10  LEU   B CA   1 
ATOM   4051 C  C    . LEU   B 1 10  ? 37.978 -30.147 -17.231 1.00 19.81 ?  10  LEU   B C    1 
ATOM   4052 O  O    . LEU   B 1 10  ? 37.995 -29.735 -16.069 1.00 19.28 ?  10  LEU   B O    1 
ATOM   4053 C  CB   . LEU   B 1 10  ? 39.264 -32.282 -17.096 1.00 20.99 ?  10  LEU   B CB   1 
ATOM   4054 C  CG   . LEU   B 1 10  ? 38.136 -33.260 -17.411 1.00 22.50 ?  10  LEU   B CG   1 
ATOM   4055 C  CD1  . LEU   B 1 10  ? 38.267 -33.766 -18.841 1.00 23.46 ?  10  LEU   B CD1  1 
ATOM   4056 C  CD2  . LEU   B 1 10  ? 38.125 -34.414 -16.422 1.00 23.45 ?  10  LEU   B CD2  1 
ATOM   4057 H  H    . LEU   B 1 10  ? 40.690 -30.304 -16.744 1.00 24.31 ?  10  LEU   B H    1 
ATOM   4058 H  HA   . LEU   B 1 10  ? 39.032 -31.058 -18.736 1.00 24.23 ?  10  LEU   B HA   1 
ATOM   4059 H  HB2  . LEU   B 1 10  ? 40.095 -32.704 -17.366 1.00 25.17 ?  10  LEU   B HB2  1 
ATOM   4060 H  HB3  . LEU   B 1 10  ? 39.269 -32.147 -16.133 1.00 25.17 ?  10  LEU   B HB3  1 
ATOM   4061 H  HG   . LEU   B 1 10  ? 37.285 -32.798 -17.335 1.00 26.98 ?  10  LEU   B HG   1 
ATOM   4062 H  HD11 . LEU   B 1 10  ? 37.590 -34.440 -18.999 1.00 28.13 ?  10  LEU   B HD11 1 
ATOM   4063 H  HD12 . LEU   B 1 10  ? 38.143 -33.021 -19.450 1.00 28.13 ?  10  LEU   B HD12 1 
ATOM   4064 H  HD13 . LEU   B 1 10  ? 39.150 -34.147 -18.958 1.00 28.13 ?  10  LEU   B HD13 1 
ATOM   4065 H  HD21 . LEU   B 1 10  ? 37.401 -35.015 -16.651 1.00 28.12 ?  10  LEU   B HD21 1 
ATOM   4066 H  HD22 . LEU   B 1 10  ? 38.973 -34.876 -16.473 1.00 28.12 ?  10  LEU   B HD22 1 
ATOM   4067 H  HD23 . LEU   B 1 10  ? 37.992 -34.057 -15.529 1.00 28.12 ?  10  LEU   B HD23 1 
ATOM   4068 N  N    . LYS   B 1 11  ? 36.954 -29.963 -18.057 1.00 20.74 ?  11  LYS   B N    1 
ATOM   4069 C  CA   . LYS   B 1 11  ? 35.749 -29.261 -17.644 1.00 22.94 ?  11  LYS   B CA   1 
ATOM   4070 C  C    . LYS   B 1 11  ? 34.898 -30.194 -16.788 1.00 21.76 ?  11  LYS   B C    1 
ATOM   4071 O  O    . LYS   B 1 11  ? 34.551 -31.299 -17.222 1.00 23.27 ?  11  LYS   B O    1 
ATOM   4072 C  CB   . LYS   B 1 11  ? 34.988 -28.821 -18.895 1.00 26.96 ?  11  LYS   B CB   1 
ATOM   4073 C  CG   . LYS   B 1 11  ? 33.870 -27.826 -18.662 1.00 30.45 ?  11  LYS   B CG   1 
ATOM   4074 C  CD   . LYS   B 1 11  ? 33.145 -27.528 -19.969 1.00 33.33 ?  11  LYS   B CD   1 
ATOM   4075 C  CE   . LYS   B 1 11  ? 32.146 -26.394 -19.814 1.00 35.34 ?  11  LYS   B CE   1 
ATOM   4076 N  NZ   . LYS   B 1 11  ? 32.817 -25.085 -19.580 1.00 36.47 ?  11  LYS   B NZ   1 
ATOM   4077 H  H    . LYS   B 1 11  ? 36.922 -30.247 -18.870 1.00 24.87 ?  11  LYS   B H    1 
ATOM   4078 H  HA   . LYS   B 1 11  ? 35.979 -28.475 -17.125 1.00 27.51 ?  11  LYS   B HA   1 
ATOM   4079 H  HB2  . LYS   B 1 11  ? 35.617 -28.406 -19.508 1.00 32.34 ?  11  LYS   B HB2  1 
ATOM   4080 H  HB3  . LYS   B 1 11  ? 34.597 -29.602 -19.314 1.00 32.34 ?  11  LYS   B HB3  1 
ATOM   4081 H  HG2  . LYS   B 1 11  ? 33.231 -28.200 -18.037 1.00 36.53 ?  11  LYS   B HG2  1 
ATOM   4082 H  HG3  . LYS   B 1 11  ? 34.239 -26.998 -18.320 1.00 36.53 ?  11  LYS   B HG3  1 
ATOM   4083 H  HD2  . LYS   B 1 11  ? 33.795 -27.271 -20.643 1.00 39.98 ?  11  LYS   B HD2  1 
ATOM   4084 H  HD3  . LYS   B 1 11  ? 32.664 -28.321 -20.256 1.00 39.98 ?  11  LYS   B HD3  1 
ATOM   4085 H  HE2  . LYS   B 1 11  ? 31.616 -26.323 -20.623 1.00 42.40 ?  11  LYS   B HE2  1 
ATOM   4086 H  HE3  . LYS   B 1 11  ? 31.573 -26.584 -19.055 1.00 42.40 ?  11  LYS   B HE3  1 
ATOM   4087 H  HZ1  . LYS   B 1 11  ? 32.208 -24.440 -19.508 1.00 43.74 ?  11  LYS   B HZ1  1 
ATOM   4088 H  HZ2  . LYS   B 1 11  ? 33.295 -25.117 -18.831 1.00 43.74 ?  11  LYS   B HZ2  1 
ATOM   4089 H  HZ3  . LYS   B 1 11  ? 33.358 -24.896 -20.262 1.00 43.74 ?  11  LYS   B HZ3  1 
ATOM   4090 N  N    . LEU   B 1 12  ? 34.565 -29.757 -15.573 1.00 20.15 ?  12  LEU   B N    1 
ATOM   4091 C  CA   . LEU   B 1 12  ? 33.609 -30.463 -14.726 1.00 19.49 ?  12  LEU   B CA   1 
ATOM   4092 C  C    . LEU   B 1 12  ? 32.220 -29.851 -14.812 1.00 19.35 ?  12  LEU   B C    1 
ATOM   4093 O  O    . LEU   B 1 12  ? 31.231 -30.564 -14.981 1.00 19.56 ?  12  LEU   B O    1 
ATOM   4094 C  CB   . LEU   B 1 12  ? 34.075 -30.479 -13.264 1.00 18.71 ?  12  LEU   B CB   1 
ATOM   4095 C  CG   . LEU   B 1 12  ? 35.421 -31.154 -12.997 1.00 18.41 ?  12  LEU   B CG   1 
ATOM   4096 C  CD1  . LEU   B 1 12  ? 35.781 -31.100 -11.523 1.00 18.67 ?  12  LEU   B CD1  1 
ATOM   4097 C  CD2  . LEU   B 1 12  ? 35.424 -32.591 -13.503 1.00 18.72 ?  12  LEU   B CD2  1 
ATOM   4098 H  H    . LEU   B 1 12  ? 34.874 -29.041 -15.214 1.00 24.16 ?  12  LEU   B H    1 
ATOM   4099 H  HA   . LEU   B 1 12  ? 33.532 -31.380 -15.029 1.00 23.37 ?  12  LEU   B HA   1 
ATOM   4100 H  HB2  . LEU   B 1 12  ? 34.138 -29.563 -12.956 1.00 22.43 ?  12  LEU   B HB2  1 
ATOM   4101 H  HB3  . LEU   B 1 12  ? 33.403 -30.948 -12.737 1.00 22.43 ?  12  LEU   B HB3  1 
ATOM   4102 H  HG   . LEU   B 1 12  ? 36.102 -30.670 -13.484 1.00 22.07 ?  12  LEU   B HG   1 
ATOM   4103 H  HD11 . LEU   B 1 12  ? 36.643 -31.532 -11.394 1.00 22.39 ?  12  LEU   B HD11 1 
ATOM   4104 H  HD12 . LEU   B 1 12  ? 35.836 -30.172 -11.242 1.00 22.39 ?  12  LEU   B HD12 1 
ATOM   4105 H  HD13 . LEU   B 1 12  ? 35.102 -31.562 -11.009 1.00 22.39 ?  12  LEU   B HD13 1 
ATOM   4106 H  HD21 . LEU   B 1 12  ? 36.234 -33.027 -13.201 1.00 22.45 ?  12  LEU   B HD21 1 
ATOM   4107 H  HD22 . LEU   B 1 12  ? 34.646 -33.052 -13.152 1.00 22.45 ?  12  LEU   B HD22 1 
ATOM   4108 H  HD23 . LEU   B 1 12  ? 35.393 -32.584 -14.473 1.00 22.45 ?  12  LEU   B HD23 1 
ATOM   4109 N  N    . THR   B 1 13  ? 32.131 -28.535 -14.694 1.00 19.29 ?  13  THR   B N    1 
ATOM   4110 C  CA   . THR   B 1 13  ? 30.910 -27.781 -14.903 1.00 19.22 ?  13  THR   B CA   1 
ATOM   4111 C  C    . THR   B 1 13  ? 31.255 -26.595 -15.795 1.00 21.27 ?  13  THR   B C    1 
ATOM   4112 O  O    . THR   B 1 13  ? 32.406 -26.417 -16.216 1.00 22.07 ?  13  THR   B O    1 
ATOM   4113 C  CB   . THR   B 1 13  ? 30.315 -27.293 -13.577 1.00 18.86 ?  13  THR   B CB   1 
ATOM   4114 O  OG1  . THR   B 1 13  ? 31.162 -26.272 -13.036 1.00 18.52 ?  13  THR   B OG1  1 
ATOM   4115 C  CG2  . THR   B 1 13  ? 30.188 -28.438 -12.579 1.00 19.48 ?  13  THR   B CG2  1 
ATOM   4116 H  H    . THR   B 1 13  ? 32.796 -28.034 -14.479 1.00 23.13 ?  13  THR   B H    1 
ATOM   4117 H  HA   . THR   B 1 13  ? 30.248 -28.337 -15.347 1.00 23.05 ?  13  THR   B HA   1 
ATOM   4118 H  HB   . THR   B 1 13  ? 29.421 -26.927 -13.732 1.00 22.62 ?  13  THR   B HB   1 
ATOM   4119 H  HG1  . THR   B 1 13  ? 30.847 -25.509 -13.225 1.00 22.21 ?  13  THR   B HG1  1 
ATOM   4120 H  HG21 . THR   B 1 13  ? 29.687 -28.149 -11.798 1.00 23.36 ?  13  THR   B HG21 1 
ATOM   4121 H  HG22 . THR   B 1 13  ? 29.725 -29.186 -12.988 1.00 23.36 ?  13  THR   B HG22 1 
ATOM   4122 H  HG23 . THR   B 1 13  ? 31.069 -28.728 -12.297 1.00 23.36 ?  13  THR   B HG23 1 
ATOM   4123 N  N    A ASP   B 1 14  ? 30.249 -25.765 -16.073 0.64 22.33 ?  14  ASP   B N    1 
ATOM   4124 N  N    B ASP   B 1 14  ? 30.251 -25.759 -16.073 0.36 22.08 ?  14  ASP   B N    1 
ATOM   4125 C  CA   A ASP   B 1 14  ? 30.477 -24.613 -16.937 0.64 23.48 ?  14  ASP   B CA   1 
ATOM   4126 C  CA   B ASP   B 1 14  ? 30.471 -24.608 -16.942 0.36 22.93 ?  14  ASP   B CA   1 
ATOM   4127 C  C    A ASP   B 1 14  ? 31.574 -23.706 -16.396 0.64 21.74 ?  14  ASP   B C    1 
ATOM   4128 C  C    B ASP   B 1 14  ? 31.493 -23.631 -16.380 0.36 21.29 ?  14  ASP   B C    1 
ATOM   4129 O  O    A ASP   B 1 14  ? 32.248 -23.023 -17.178 0.64 22.73 ?  14  ASP   B O    1 
ATOM   4130 O  O    B ASP   B 1 14  ? 32.008 -22.799 -17.135 0.36 21.70 ?  14  ASP   B O    1 
ATOM   4131 C  CB   A ASP   B 1 14  ? 29.180 -23.827 -17.129 0.64 26.65 ?  14  ASP   B CB   1 
ATOM   4132 C  CB   B ASP   B 1 14  ? 29.161 -23.862 -17.193 0.36 25.55 ?  14  ASP   B CB   1 
ATOM   4133 C  CG   A ASP   B 1 14  ? 28.211 -24.516 -18.066 0.64 29.89 ?  14  ASP   B CG   1 
ATOM   4134 C  CG   B ASP   B 1 14  ? 28.272 -24.568 -18.197 0.36 28.02 ?  14  ASP   B CG   1 
ATOM   4135 O  OD1  A ASP   B 1 14  ? 28.604 -25.491 -18.744 0.64 30.92 ?  14  ASP   B OD1  1 
ATOM   4136 O  OD1  B ASP   B 1 14  ? 28.811 -25.257 -19.089 0.36 28.82 ?  14  ASP   B OD1  1 
ATOM   4137 O  OD2  A ASP   B 1 14  ? 27.043 -24.079 -18.118 0.64 31.17 -1 14  ASP   B OD2  1 
ATOM   4138 O  OD2  B ASP   B 1 14  ? 27.034 -24.435 -18.097 0.36 28.93 -1 14  ASP   B OD2  1 
ATOM   4139 H  H    A ASP   B 1 14  ? 29.446 -25.834 -15.772 0.64 26.78 ?  14  ASP   B H    1 
ATOM   4140 H  H    B ASP   B 1 14  ? 29.447 -25.832 -15.775 0.36 26.48 ?  14  ASP   B H    1 
ATOM   4141 H  HA   A ASP   B 1 14  ? 30.768 -24.922 -17.804 0.64 28.16 ?  14  ASP   B HA   1 
ATOM   4142 H  HA   B ASP   B 1 14  ? 30.802 -24.922 -17.796 0.36 27.50 ?  14  ASP   B HA   1 
ATOM   4143 H  HB2  A ASP   B 1 14  ? 28.735 -23.726 -16.275 0.64 31.97 ?  14  ASP   B HB2  1 
ATOM   4144 H  HB2  B ASP   B 1 14  ? 28.677 -23.785 -16.356 0.36 30.64 ?  14  ASP   B HB2  1 
ATOM   4145 H  HB3  A ASP   B 1 14  ? 29.385 -22.955 -17.504 0.64 31.97 ?  14  ASP   B HB3  1 
ATOM   4146 H  HB3  B ASP   B 1 14  ? 29.366 -22.974 -17.536 0.36 30.64 ?  14  ASP   B HB3  1 
ATOM   4147 N  N    . ASN   B 1 15  ? 31.780 -23.689 -15.076 1.00 19.69 ?  15  ASN   B N    1 
ATOM   4148 C  CA   . ASN   B 1 15  ? 32.740 -22.773 -14.467 1.00 17.33 ?  15  ASN   B CA   1 
ATOM   4149 C  C    . ASN   B 1 15  ? 33.831 -23.432 -13.633 1.00 15.89 ?  15  ASN   B C    1 
ATOM   4150 O  O    . ASN   B 1 15  ? 34.691 -22.712 -13.116 1.00 15.75 ?  15  ASN   B O    1 
ATOM   4151 C  CB   . ASN   B 1 15  ? 32.023 -21.720 -13.607 1.00 17.24 ?  15  ASN   B CB   1 
ATOM   4152 C  CG   . ASN   B 1 15  ? 31.407 -22.317 -12.360 1.00 17.10 ?  15  ASN   B CG   1 
ATOM   4153 O  OD1  . ASN   B 1 15  ? 30.462 -23.112 -12.439 1.00 18.65 ?  15  ASN   B OD1  1 
ATOM   4154 N  ND2  . ASN   B 1 15  ? 31.940 -21.959 -11.204 1.00 16.21 ?  15  ASN   B ND2  1 
ATOM   4155 H  H    A ASN   B 1 15  ? 31.371 -24.197 -14.513 0.64 23.61 ?  15  ASN   B H    1 
ATOM   4156 H  H    B ASN   B 1 15  ? 31.407 -24.230 -14.519 0.36 23.61 ?  15  ASN   B H    1 
ATOM   4157 H  HA   . ASN   B 1 15  ? 33.188 -22.287 -15.166 1.00 20.78 ?  15  ASN   B HA   1 
ATOM   4158 H  HB2  . ASN   B 1 15  ? 32.660 -21.036 -13.332 1.00 20.67 ?  15  ASN   B HB2  1 
ATOM   4159 H  HB3  . ASN   B 1 15  ? 31.308 -21.306 -14.125 1.00 20.67 ?  15  ASN   B HB3  1 
ATOM   4160 H  HD21 . ASN   B 1 15  ? 31.625 -22.265 -10.463 1.00 19.43 ?  15  ASN   B HD21 1 
ATOM   4161 H  HD22 . ASN   B 1 15  ? 32.611 -21.411 -11.183 1.00 19.43 ?  15  ASN   B HD22 1 
ATOM   4162 N  N    . VAL   B 1 16  ? 33.833 -24.751 -13.476 1.00 15.62 ?  16  VAL   B N    1 
ATOM   4163 C  CA   . VAL   B 1 16  ? 34.837 -25.436 -12.668 1.00 15.45 ?  16  VAL   B CA   1 
ATOM   4164 C  C    . VAL   B 1 16  ? 35.630 -26.372 -13.565 1.00 15.67 ?  16  VAL   B C    1 
ATOM   4165 O  O    . VAL   B 1 16  ? 35.055 -27.258 -14.218 1.00 16.51 ?  16  VAL   B O    1 
ATOM   4166 C  CB   . VAL   B 1 16  ? 34.214 -26.201 -11.491 1.00 15.61 ?  16  VAL   B CB   1 
ATOM   4167 C  CG1  . VAL   B 1 16  ? 35.298 -26.938 -10.705 1.00 15.49 ?  16  VAL   B CG1  1 
ATOM   4168 C  CG2  . VAL   B 1 16  ? 33.421 -25.252 -10.594 1.00 16.21 ?  16  VAL   B CG2  1 
ATOM   4169 H  H    . VAL   B 1 16  ? 33.244 -25.279 -13.824 1.00 18.72 ?  16  VAL   B H    1 
ATOM   4170 H  HA   . VAL   B 1 16  ? 35.446 -24.778 -12.302 1.00 18.52 ?  16  VAL   B HA   1 
ATOM   4171 H  HB   . VAL   B 1 16  ? 33.596 -26.866 -11.837 1.00 18.72 ?  16  VAL   B HB   1 
ATOM   4172 H  HG11 . VAL   B 1 16  ? 34.925 -27.238 -9.860  1.00 18.57 ?  16  VAL   B HG11 1 
ATOM   4173 H  HG12 . VAL   B 1 16  ? 35.601 -27.701 -11.220 1.00 18.57 ?  16  VAL   B HG12 1 
ATOM   4174 H  HG13 . VAL   B 1 16  ? 36.035 -26.330 -10.541 1.00 18.57 ?  16  VAL   B HG13 1 
ATOM   4175 H  HG21 . VAL   B 1 16  ? 33.089 -25.745 -9.825  1.00 19.43 ?  16  VAL   B HG21 1 
ATOM   4176 H  HG22 . VAL   B 1 16  ? 33.999 -24.534 -10.303 1.00 19.43 ?  16  VAL   B HG22 1 
ATOM   4177 H  HG23 . VAL   B 1 16  ? 32.673 -24.892 -11.099 1.00 19.43 ?  16  VAL   B HG23 1 
ATOM   4178 N  N    . TYR   B 1 17  ? 36.950 -26.198 -13.551 1.00 16.12 ?  17  TYR   B N    1 
ATOM   4179 C  CA   . TYR   B 1 17  ? 37.894 -26.952 -14.361 1.00 16.19 ?  17  TYR   B CA   1 
ATOM   4180 C  C    . TYR   B 1 17  ? 38.949 -27.563 -13.447 1.00 15.26 ?  17  TYR   B C    1 
ATOM   4181 O  O    . TYR   B 1 17  ? 39.231 -27.037 -12.368 1.00 15.46 ?  17  TYR   B O    1 
ATOM   4182 C  CB   . TYR   B 1 17  ? 38.598 -26.035 -15.372 1.00 18.96 ?  17  TYR   B CB   1 
ATOM   4183 C  CG   . TYR   B 1 17  ? 37.669 -25.273 -16.286 1.00 22.35 ?  17  TYR   B CG   1 
ATOM   4184 C  CD1  . TYR   B 1 17  ? 37.100 -24.072 -15.888 1.00 23.96 ?  17  TYR   B CD1  1 
ATOM   4185 C  CD2  . TYR   B 1 17  ? 37.368 -25.753 -17.554 1.00 24.35 ?  17  TYR   B CD2  1 
ATOM   4186 C  CE1  . TYR   B 1 17  ? 36.250 -23.370 -16.724 1.00 25.50 ?  17  TYR   B CE1  1 
ATOM   4187 C  CE2  . TYR   B 1 17  ? 36.521 -25.059 -18.398 1.00 25.76 ?  17  TYR   B CE2  1 
ATOM   4188 C  CZ   . TYR   B 1 17  ? 35.963 -23.869 -17.976 1.00 26.49 ?  17  TYR   B CZ   1 
ATOM   4189 O  OH   . TYR   B 1 17  ? 35.121 -23.172 -18.810 1.00 27.72 ?  17  TYR   B OH   1 
ATOM   4190 H  H    . TYR   B 1 17  ? 37.338 -25.611 -13.052 1.00 19.32 ?  17  TYR   B H    1 
ATOM   4191 H  HA   . TYR   B 1 17  ? 37.425 -27.658 -14.841 1.00 19.41 ?  17  TYR   B HA   1 
ATOM   4192 H  HB2  . TYR   B 1 17  ? 39.136 -25.390 -14.890 1.00 22.73 ?  17  TYR   B HB2  1 
ATOM   4193 H  HB3  . TYR   B 1 17  ? 39.161 -26.581 -15.934 1.00 22.73 ?  17  TYR   B HB3  1 
ATOM   4194 H  HD1  . TYR   B 1 17  ? 37.289 -23.733 -15.045 1.00 28.73 ?  17  TYR   B HD1  1 
ATOM   4195 H  HD2  . TYR   B 1 17  ? 37.737 -26.555 -17.842 1.00 29.21 ?  17  TYR   B HD2  1 
ATOM   4196 H  HE1  . TYR   B 1 17  ? 35.873 -22.566 -16.444 1.00 30.59 ?  17  TYR   B HE1  1 
ATOM   4197 H  HE2  . TYR   B 1 17  ? 36.321 -25.393 -19.246 1.00 30.90 ?  17  TYR   B HE2  1 
ATOM   4198 H  HH   . TYR   B 1 17  ? 35.028 -23.581 -19.538 1.00 33.24 ?  17  TYR   B HH   1 
ATOM   4199 N  N    . ILE   B 1 18  ? 39.547 -28.672 -13.880 1.00 15.52 ?  18  ILE   B N    1 
ATOM   4200 C  CA   . ILE   B 1 18  ? 40.477 -29.393 -13.020 1.00 15.35 ?  18  ILE   B CA   1 
ATOM   4201 C  C    . ILE   B 1 18  ? 41.635 -29.946 -13.843 1.00 15.68 ?  18  ILE   B C    1 
ATOM   4202 O  O    . ILE   B 1 18  ? 41.471 -30.340 -15.003 1.00 16.98 ?  18  ILE   B O    1 
ATOM   4203 C  CB   . ILE   B 1 18  ? 39.733 -30.495 -12.217 1.00 15.70 ?  18  ILE   B CB   1 
ATOM   4204 C  CG1  . ILE   B 1 18  ? 40.605 -31.045 -11.087 1.00 16.03 ?  18  ILE   B CG1  1 
ATOM   4205 C  CG2  . ILE   B 1 18  ? 39.232 -31.611 -13.141 1.00 15.99 ?  18  ILE   B CG2  1 
ATOM   4206 C  CD1  . ILE   B 1 18  ? 39.819 -31.866 -10.070 1.00 17.66 ?  18  ILE   B CD1  1 
ATOM   4207 H  H    . ILE   B 1 18  ? 39.424 -29.027 -14.651 1.00 18.61 ?  18  ILE   B H    1 
ATOM   4208 H  HA   . ILE   B 1 18  ? 40.837 -28.774 -12.367 1.00 18.40 ?  18  ILE   B HA   1 
ATOM   4209 H  HB   . ILE   B 1 18  ? 38.948 -30.095 -11.803 1.00 18.82 ?  18  ILE   B HB   1 
ATOM   4210 H  HG12 . ILE   B 1 18  ? 41.289 -31.613 -11.465 1.00 19.22 ?  18  ILE   B HG12 1 
ATOM   4211 H  HG13 . ILE   B 1 18  ? 41.010 -30.300 -10.616 1.00 19.22 ?  18  ILE   B HG13 1 
ATOM   4212 H  HG21 . ILE   B 1 18  ? 38.639 -32.199 -12.640 1.00 19.17 ?  18  ILE   B HG21 1 
ATOM   4213 H  HG22 . ILE   B 1 18  ? 38.745 -31.211 -13.879 1.00 19.17 ?  18  ILE   B HG22 1 
ATOM   4214 H  HG23 . ILE   B 1 18  ? 39.989 -32.112 -13.473 1.00 19.17 ?  18  ILE   B HG23 1 
ATOM   4215 H  HD11 . ILE   B 1 18  ? 40.418 -32.146 -9.359  1.00 21.18 ?  18  ILE   B HD11 1 
ATOM   4216 H  HD12 . ILE   B 1 18  ? 39.105 -31.320 -9.704  1.00 21.18 ?  18  ILE   B HD12 1 
ATOM   4217 H  HD13 . ILE   B 1 18  ? 39.445 -32.645 -10.513 1.00 21.18 ?  18  ILE   B HD13 1 
ATOM   4218 N  N    . LYS   B 1 19  ? 42.810 -29.998 -13.216 1.00 16.06 ?  19  LYS   B N    1 
ATOM   4219 C  CA   . LYS   B 1 19  ? 44.024 -30.462 -13.871 1.00 16.99 ?  19  LYS   B CA   1 
ATOM   4220 C  C    . LYS   B 1 19  ? 44.931 -31.142 -12.854 1.00 16.98 ?  19  LYS   B C    1 
ATOM   4221 O  O    . LYS   B 1 19  ? 45.017 -30.715 -11.701 1.00 16.32 ?  19  LYS   B O    1 
ATOM   4222 C  CB   . LYS   B 1 19  ? 44.785 -29.286 -14.499 1.00 18.37 ?  19  LYS   B CB   1 
ATOM   4223 C  CG   . LYS   B 1 19  ? 45.953 -29.691 -15.378 1.00 20.54 ?  19  LYS   B CG   1 
ATOM   4224 C  CD   . LYS   B 1 19  ? 46.693 -28.463 -15.900 1.00 22.22 ?  19  LYS   B CD   1 
ATOM   4225 C  CE   . LYS   B 1 19  ? 47.846 -28.843 -16.813 1.00 24.11 ?  19  LYS   B CE   1 
ATOM   4226 N  NZ   . LYS   B 1 19  ? 48.602 -27.651 -17.286 1.00 25.16 ?  19  LYS   B NZ   1 
ATOM   4227 H  H    . LYS   B 1 19  ? 42.916 -29.762 -12.393 1.00 19.25 ?  19  LYS   B H    1 
ATOM   4228 H  HA   . LYS   B 1 19  ? 43.787 -31.095 -14.567 1.00 20.37 ?  19  LYS   B HA   1 
ATOM   4229 H  HB2  . LYS   B 1 19  ? 44.164 -28.779 -15.045 1.00 22.03 ?  19  LYS   B HB2  1 
ATOM   4230 H  HB3  . LYS   B 1 19  ? 45.123 -28.724 -13.782 1.00 22.03 ?  19  LYS   B HB3  1 
ATOM   4231 H  HG2  . LYS   B 1 19  ? 46.567 -30.230 -14.860 1.00 24.63 ?  19  LYS   B HG2  1 
ATOM   4232 H  HG3  . LYS   B 1 19  ? 45.614 -30.196 -16.136 1.00 24.63 ?  19  LYS   B HG3  1 
ATOM   4233 H  HD2  . LYS   B 1 19  ? 46.074 -27.908 -16.402 1.00 26.65 ?  19  LYS   B HD2  1 
ATOM   4234 H  HD3  . LYS   B 1 19  ? 47.050 -27.966 -15.146 1.00 26.65 ?  19  LYS   B HD3  1 
ATOM   4235 H  HE2  . LYS   B 1 19  ? 48.456 -29.421 -16.328 1.00 28.92 ?  19  LYS   B HE2  1 
ATOM   4236 H  HE3  . LYS   B 1 19  ? 47.493 -29.310 -17.589 1.00 28.92 ?  19  LYS   B HE3  1 
ATOM   4237 H  HZ1  . LYS   B 1 19  ? 49.253 -27.904 -17.838 1.00 30.17 ?  19  LYS   B HZ1  1 
ATOM   4238 H  HZ2  . LYS   B 1 19  ? 48.056 -27.096 -17.719 1.00 30.17 ?  19  LYS   B HZ2  1 
ATOM   4239 H  HZ3  . LYS   B 1 19  ? 48.960 -27.223 -16.594 1.00 30.17 ?  19  LYS   B HZ3  1 
ATOM   4240 N  N    . ASN   B 1 20  ? 45.612 -32.196 -13.292 1.00 17.97 ?  20  ASN   B N    1 
ATOM   4241 C  CA   . ASN   B 1 20  ? 46.651 -32.828 -12.482 1.00 19.24 ?  20  ASN   B CA   1 
ATOM   4242 C  C    . ASN   B 1 20  ? 47.924 -32.006 -12.668 1.00 19.64 ?  20  ASN   B C    1 
ATOM   4243 O  O    . ASN   B 1 20  ? 48.576 -32.082 -13.713 1.00 21.38 ?  20  ASN   B O    1 
ATOM   4244 C  CB   . ASN   B 1 20  ? 46.824 -34.281 -12.920 1.00 20.77 ?  20  ASN   B CB   1 
ATOM   4245 C  CG   . ASN   B 1 20  ? 47.979 -34.992 -12.226 1.00 22.41 ?  20  ASN   B CG   1 
ATOM   4246 O  OD1  . ASN   B 1 20  ? 48.643 -35.842 -12.831 1.00 24.59 ?  20  ASN   B OD1  1 
ATOM   4247 N  ND2  . ASN   B 1 20  ? 48.209 -34.677 -10.958 1.00 22.02 ?  20  ASN   B ND2  1 
ATOM   4248 H  H    . ASN   B 1 20  ? 45.491 -32.564 -14.062 1.00 21.55 ?  20  ASN   B H    1 
ATOM   4249 H  HA   . ASN   B 1 20  ? 46.381 -32.810 -11.549 1.00 23.07 ?  20  ASN   B HA   1 
ATOM   4250 H  HB2  . ASN   B 1 20  ? 46.005 -34.769 -12.719 1.00 24.91 ?  20  ASN   B HB2  1 
ATOM   4251 H  HB3  . ASN   B 1 20  ? 46.989 -34.301 -13.874 1.00 24.91 ?  20  ASN   B HB3  1 
ATOM   4252 H  HD21 . ASN   B 1 20  ? 48.852 -35.053 -10.531 1.00 26.40 ?  20  ASN   B HD21 1 
ATOM   4253 H  HD22 . ASN   B 1 20  ? 47.725 -34.081 -10.560 1.00 26.40 ?  20  ASN   B HD22 1 
ATOM   4254 N  N    . ALA   B 1 21  ? 48.276 -31.198 -11.664 1.00 19.22 ?  21  ALA   B N    1 
ATOM   4255 C  CA   . ALA   B 1 21  ? 49.396 -30.279 -11.807 1.00 19.60 ?  21  ALA   B CA   1 
ATOM   4256 C  C    . ALA   B 1 21  ? 49.859 -29.790 -10.443 1.00 18.38 ?  21  ALA   B C    1 
ATOM   4257 O  O    . ALA   B 1 21  ? 49.115 -29.817 -9.457  1.00 18.22 ?  21  ALA   B O    1 
ATOM   4258 C  CB   . ALA   B 1 21  ? 49.015 -29.094 -12.692 1.00 20.86 ?  21  ALA   B CB   1 
ATOM   4259 H  H    . ALA   B 1 21  ? 47.875 -31.169 -10.898 1.00 23.05 ?  21  ALA   B H    1 
ATOM   4260 H  HA   . ALA   B 1 21  ? 50.128 -30.754 -12.227 1.00 23.50 ?  21  ALA   B HA   1 
ATOM   4261 H  HB1  . ALA   B 1 21  ? 49.809 -28.561 -12.839 1.00 25.01 ?  21  ALA   B HB1  1 
ATOM   4262 H  HB2  . ALA   B 1 21  ? 48.677 -29.431 -13.535 1.00 25.01 ?  21  ALA   B HB2  1 
ATOM   4263 H  HB3  . ALA   B 1 21  ? 48.333 -28.573 -12.243 1.00 25.01 ?  21  ALA   B HB3  1 
ATOM   4264 N  N    . ASP   B 1 22  ? 51.119 -29.347 -10.423 1.00 17.43 ?  22  ASP   B N    1 
ATOM   4265 C  CA   . ASP   B 1 22  ? 51.738 -28.654 -9.298  1.00 16.45 ?  22  ASP   B CA   1 
ATOM   4266 C  C    . ASP   B 1 22  ? 51.335 -27.182 -9.376  1.00 15.27 ?  22  ASP   B C    1 
ATOM   4267 O  O    . ASP   B 1 22  ? 51.641 -26.509 -10.364 1.00 15.58 ?  22  ASP   B O    1 
ATOM   4268 C  CB   . ASP   B 1 22  ? 53.255 -28.828 -9.460  1.00 17.76 ?  22  ASP   B CB   1 
ATOM   4269 C  CG   . ASP   B 1 22  ? 54.085 -28.077 -8.428  1.00 19.58 ?  22  ASP   B CG   1 
ATOM   4270 O  OD1  . ASP   B 1 22  ? 53.727 -26.958 -8.021  1.00 19.68 ?  22  ASP   B OD1  1 
ATOM   4271 O  OD2  . ASP   B 1 22  ? 55.153 -28.608 -8.053  1.00 21.90 -1 22  ASP   B OD2  1 
ATOM   4272 H  H    . ASP   B 1 22  ? 51.658 -29.442 -11.091 1.00 20.90 ?  22  ASP   B H    1 
ATOM   4273 H  HA   . ASP   B 1 22  ? 51.448 -29.039 -8.454  1.00 19.73 ?  22  ASP   B HA   1 
ATOM   4274 H  HB2  . ASP   B 1 22  ? 53.476 -29.766 -9.385  1.00 21.29 ?  22  ASP   B HB2  1 
ATOM   4275 H  HB3  . ASP   B 1 22  ? 53.516 -28.492 -10.331 1.00 21.29 ?  22  ASP   B HB3  1 
ATOM   4276 N  N    . ILE   B 1 23  ? 50.621 -26.690 -8.355  1.00 14.71 ?  23  ILE   B N    1 
ATOM   4277 C  CA   . ILE   B 1 23  ? 50.033 -25.349 -8.422  1.00 13.92 ?  23  ILE   B CA   1 
ATOM   4278 C  C    . ILE   B 1 23  ? 51.092 -24.262 -8.557  1.00 13.49 ?  23  ILE   B C    1 
ATOM   4279 O  O    . ILE   B 1 23  ? 50.831 -23.220 -9.164  1.00 12.96 ?  23  ILE   B O    1 
ATOM   4280 C  CB   . ILE   B 1 23  ? 49.091 -25.104 -7.227  1.00 14.19 ?  23  ILE   B CB   1 
ATOM   4281 C  CG1  . ILE   B 1 23  ? 48.278 -23.824 -7.424  1.00 14.82 ?  23  ILE   B CG1  1 
ATOM   4282 C  CG2  . ILE   B 1 23  ? 49.854 -25.075 -5.922  1.00 14.88 ?  23  ILE   B CG2  1 
ATOM   4283 C  CD1  . ILE   B 1 23  ? 47.121 -23.692 -6.450  1.00 15.54 ?  23  ILE   B CD1  1 
ATOM   4284 H  H    . ILE   B 1 23  ? 50.470 -27.111 -7.620  1.00 17.63 ?  23  ILE   B H    1 
ATOM   4285 H  HA   . ILE   B 1 23  ? 49.489 -25.309 -9.221  1.00 16.68 ?  23  ILE   B HA   1 
ATOM   4286 H  HB   . ILE   B 1 23  ? 48.464 -25.845 -7.191  1.00 17.02 ?  23  ILE   B HB   1 
ATOM   4287 H  HG12 . ILE   B 1 23  ? 48.866 -23.058 -7.295  1.00 17.77 ?  23  ILE   B HG12 1 
ATOM   4288 H  HG13 . ILE   B 1 23  ? 47.920 -23.810 -8.326  1.00 17.77 ?  23  ILE   B HG13 1 
ATOM   4289 H  HG21 . ILE   B 1 23  ? 49.221 -25.065 -5.189  1.00 17.85 ?  23  ILE   B HG21 1 
ATOM   4290 H  HG22 . ILE   B 1 23  ? 50.412 -25.867 -5.867  1.00 17.85 ?  23  ILE   B HG22 1 
ATOM   4291 H  HG23 . ILE   B 1 23  ? 50.405 -24.279 -5.898  1.00 17.85 ?  23  ILE   B HG23 1 
ATOM   4292 H  HD11 . ILE   B 1 23  ? 46.609 -22.903 -6.676  1.00 18.63 ?  23  ILE   B HD11 1 
ATOM   4293 H  HD12 . ILE   B 1 23  ? 46.562 -24.484 -6.526  1.00 18.63 ?  23  ILE   B HD12 1 
ATOM   4294 H  HD13 . ILE   B 1 23  ? 47.472 -23.620 -5.551  1.00 18.63 ?  23  ILE   B HD13 1 
ATOM   4295 N  N    . VAL   B 1 24  ? 52.287 -24.467 -7.998  1.00 13.69 ?  24  VAL   B N    1 
ATOM   4296 C  CA   . VAL   B 1 24  ? 53.360 -23.484 -8.167  1.00 14.38 ?  24  VAL   B CA   1 
ATOM   4297 C  C    . VAL   B 1 24  ? 53.816 -23.440 -9.620  1.00 14.37 ?  24  VAL   B C    1 
ATOM   4298 O  O    . VAL   B 1 24  ? 53.958 -22.364 -10.216 1.00 15.05 ?  24  VAL   B O    1 
ATOM   4299 C  CB   . VAL   B 1 24  ? 54.538 -23.794 -7.222  1.00 15.17 ?  24  VAL   B CB   1 
ATOM   4300 C  CG1  . VAL   B 1 24  ? 55.741 -22.906 -7.551  1.00 15.89 ?  24  VAL   B CG1  1 
ATOM   4301 C  CG2  . VAL   B 1 24  ? 54.126 -23.613 -5.779  1.00 16.04 ?  24  VAL   B CG2  1 
ATOM   4302 H  H    . VAL   B 1 24  ? 52.498 -25.149 -7.522  1.00 16.41 ?  24  VAL   B H    1 
ATOM   4303 H  HA   . VAL   B 1 24  ? 53.025 -22.606 -7.937  1.00 17.24 ?  24  VAL   B HA   1 
ATOM   4304 H  HB   . VAL   B 1 24  ? 54.810 -24.717 -7.338  1.00 18.19 ?  24  VAL   B HB   1 
ATOM   4305 H  HG11 . VAL   B 1 24  ? 56.331 -22.879 -6.783  1.00 19.05 ?  24  VAL   B HG11 1 
ATOM   4306 H  HG12 . VAL   B 1 24  ? 56.205 -23.277 -8.314  1.00 19.05 ?  24  VAL   B HG12 1 
ATOM   4307 H  HG13 . VAL   B 1 24  ? 55.422 -22.011 -7.753  1.00 19.05 ?  24  VAL   B HG13 1 
ATOM   4308 H  HG21 . VAL   B 1 24  ? 54.856 -23.881 -5.201  1.00 19.23 ?  24  VAL   B HG21 1 
ATOM   4309 H  HG22 . VAL   B 1 24  ? 53.913 -22.677 -5.627  1.00 19.23 ?  24  VAL   B HG22 1 
ATOM   4310 H  HG23 . VAL   B 1 24  ? 53.344 -24.161 -5.601  1.00 19.23 ?  24  VAL   B HG23 1 
ATOM   4311 N  N    . GLU   B 1 25  ? 54.075 -24.612 -10.206 1.00 15.55 ?  25  GLU   B N    1 
ATOM   4312 C  CA   . GLU   B 1 25  ? 54.468 -24.653 -11.610 1.00 17.26 ?  25  GLU   B CA   1 
ATOM   4313 C  C    . GLU   B 1 25  ? 53.358 -24.119 -12.502 1.00 15.84 ?  25  GLU   B C    1 
ATOM   4314 O  O    . GLU   B 1 25  ? 53.625 -23.404 -13.477 1.00 16.68 ?  25  GLU   B O    1 
ATOM   4315 C  CB   . GLU   B 1 25  ? 54.875 -26.070 -12.007 1.00 22.13 ?  25  GLU   B CB   1 
ATOM   4316 C  CG   . GLU   B 1 25  ? 56.186 -26.506 -11.367 1.00 28.35 ?  25  GLU   B CG   1 
ATOM   4317 C  CD   . GLU   B 1 25  ? 57.281 -25.451 -11.452 1.00 34.11 ?  25  GLU   B CD   1 
ATOM   4318 O  OE1  . GLU   B 1 25  ? 57.666 -25.072 -12.579 1.00 36.14 ?  25  GLU   B OE1  1 
ATOM   4319 O  OE2  . GLU   B 1 25  ? 57.747 -24.986 -10.386 1.00 36.00 -1 25  GLU   B OE2  1 
ATOM   4320 H  H    . GLU   B 1 25  ? 54.033 -25.381 -9.816  1.00 18.64 ?  25  GLU   B H    1 
ATOM   4321 H  HA   . GLU   B 1 25  ? 55.223 -24.060 -11.732 1.00 20.69 ?  25  GLU   B HA   1 
ATOM   4322 H  HB2  . GLU   B 1 25  ? 54.181 -26.689 -11.724 1.00 26.54 ?  25  GLU   B HB2  1 
ATOM   4323 H  HB3  . GLU   B 1 25  ? 54.978 -26.108 -12.971 1.00 26.54 ?  25  GLU   B HB3  1 
ATOM   4324 H  HG2  . GLU   B 1 25  ? 56.035 -26.681 -10.431 1.00 34.00 ?  25  GLU   B HG2  1 
ATOM   4325 H  HG3  . GLU   B 1 25  ? 56.503 -27.301 -11.819 1.00 34.00 ?  25  GLU   B HG3  1 
ATOM   4326 N  N    . GLU   B 1 26  ? 52.105 -24.436 -12.167 1.00 14.89 ?  26  GLU   B N    1 
ATOM   4327 C  CA   . GLU   B 1 26  ? 50.980 -23.913 -12.931 1.00 15.47 ?  26  GLU   B CA   1 
ATOM   4328 C  C    . GLU   B 1 26  ? 50.933 -22.396 -12.858 1.00 14.70 ?  26  GLU   B C    1 
ATOM   4329 O  O    . GLU   B 1 26  ? 50.740 -21.723 -13.875 1.00 15.87 ?  26  GLU   B O    1 
ATOM   4330 C  CB   . GLU   B 1 26  ? 49.666 -24.491 -12.405 1.00 17.14 ?  26  GLU   B CB   1 
ATOM   4331 C  CG   . GLU   B 1 26  ? 49.191 -25.749 -13.107 1.00 20.93 ?  26  GLU   B CG   1 
ATOM   4332 C  CD   . GLU   B 1 26  ? 48.940 -25.567 -14.606 1.00 22.41 ?  26  GLU   B CD   1 
ATOM   4333 O  OE1  . GLU   B 1 26  ? 47.958 -24.909 -15.016 1.00 23.34 ?  26  GLU   B OE1  1 
ATOM   4334 O  OE2  . GLU   B 1 26  ? 49.731 -26.122 -15.378 1.00 24.82 -1 26  GLU   B OE2  1 
ATOM   4335 H  H    . GLU   B 1 26  ? 51.882 -24.950 -11.508 1.00 17.85 ?  26  GLU   B H    1 
ATOM   4336 H  HA   . GLU   B 1 26  ? 51.080 -24.170 -13.857 1.00 18.54 ?  26  GLU   B HA   1 
ATOM   4337 H  HB2  . GLU   B 1 26  ? 49.776 -24.707 -11.462 1.00 20.55 ?  26  GLU   B HB2  1 
ATOM   4338 H  HB3  . GLU   B 1 26  ? 48.972 -23.819 -12.500 1.00 20.55 ?  26  GLU   B HB3  1 
ATOM   4339 H  HG2  . GLU   B 1 26  ? 49.872 -26.422 -13.010 1.00 25.10 ?  26  GLU   B HG2  1 
ATOM   4340 H  HG3  . GLU   B 1 26  ? 48.363 -26.040 -12.694 1.00 25.10 ?  26  GLU   B HG3  1 
ATOM   4341 N  N    . ALA   B 1 27  ? 51.082 -21.840 -11.654 1.00 13.81 ?  27  ALA   B N    1 
ATOM   4342 C  CA   . ALA   B 1 27  ? 51.042 -20.390 -11.511 1.00 13.99 ?  27  ALA   B CA   1 
ATOM   4343 C  C    . ALA   B 1 27  ? 52.114 -19.727 -12.368 1.00 15.06 ?  27  ALA   B C    1 
ATOM   4344 O  O    . ALA   B 1 27  ? 51.854 -18.726 -13.048 1.00 15.88 ?  27  ALA   B O    1 
ATOM   4345 C  CB   . ALA   B 1 27  ? 51.191 -20.002 -10.039 1.00 14.23 ?  27  ALA   B CB   1 
ATOM   4346 H  H    . ALA   B 1 27  ? 51.198 -22.275 -10.918 1.00 16.55 ?  27  ALA   B H    1 
ATOM   4347 H  HA   . ALA   B 1 27  ? 50.182 -20.069 -11.810 1.00 16.77 ?  27  ALA   B HA   1 
ATOM   4348 H  HB1  . ALA   B 1 27  ? 51.156 -19.038 -9.960  1.00 17.05 ?  27  ALA   B HB1  1 
ATOM   4349 H  HB2  . ALA   B 1 27  ? 50.462 -20.401 -9.532  1.00 17.05 ?  27  ALA   B HB2  1 
ATOM   4350 H  HB3  . ALA   B 1 27  ? 52.039 -20.334 -9.706  1.00 17.05 ?  27  ALA   B HB3  1 
ATOM   4351 N  N    . LYS   B 1 28  ? 53.327 -20.279 -12.361 1.00 16.32 ?  28  LYS   B N    1 
ATOM   4352 C  CA   . LYS   B 1 28  ? 54.398 -19.659 -13.129 1.00 18.43 ?  28  LYS   B CA   1 
ATOM   4353 C  C    . LYS   B 1 28  ? 54.144 -19.746 -14.628 1.00 19.29 ?  28  LYS   B C    1 
ATOM   4354 O  O    . LYS   B 1 28  ? 54.548 -18.845 -15.377 1.00 20.41 ?  28  LYS   B O    1 
ATOM   4355 C  CB   . LYS   B 1 28  ? 55.755 -20.252 -12.735 1.00 21.34 ?  28  LYS   B CB   1 
ATOM   4356 C  CG   . LYS   B 1 28  ? 56.149 -19.903 -11.302 1.00 24.86 ?  28  LYS   B CG   1 
ATOM   4357 C  CD   . LYS   B 1 28  ? 57.575 -20.303 -10.952 1.00 29.36 ?  28  LYS   B CD   1 
ATOM   4358 C  CE   . LYS   B 1 28  ? 57.678 -21.775 -10.626 1.00 33.06 ?  28  LYS   B CE   1 
ATOM   4359 N  NZ   . LYS   B 1 28  ? 59.029 -22.125 -10.105 1.00 35.32 ?  28  LYS   B NZ   1 
ATOM   4360 H  H    . LYS   B 1 28  ? 53.553 -20.991 -11.930 1.00 19.57 ?  28  LYS   B H    1 
ATOM   4361 H  HA   . LYS   B 1 28  ? 54.427 -18.719 -12.911 1.00 22.10 ?  28  LYS   B HA   1 
ATOM   4362 H  HB2  . LYS   B 1 28  ? 55.717 -21.217 -12.808 1.00 25.59 ?  28  LYS   B HB2  1 
ATOM   4363 H  HB3  . LYS   B 1 28  ? 56.440 -19.901 -13.328 1.00 25.59 ?  28  LYS   B HB3  1 
ATOM   4364 H  HG2  . LYS   B 1 28  ? 56.068 -18.943 -11.183 1.00 29.82 ?  28  LYS   B HG2  1 
ATOM   4365 H  HG3  . LYS   B 1 28  ? 55.550 -20.362 -10.695 1.00 29.82 ?  28  LYS   B HG3  1 
ATOM   4366 H  HD2  . LYS   B 1 28  ? 58.152 -20.116 -11.709 1.00 35.22 ?  28  LYS   B HD2  1 
ATOM   4367 H  HD3  . LYS   B 1 28  ? 57.863 -19.795 -10.177 1.00 35.22 ?  28  LYS   B HD3  1 
ATOM   4368 H  HE2  . LYS   B 1 28  ? 57.022 -21.996 -9.945  1.00 39.65 ?  28  LYS   B HE2  1 
ATOM   4369 H  HE3  . LYS   B 1 28  ? 57.515 -22.293 -11.429 1.00 39.65 ?  28  LYS   B HE3  1 
ATOM   4370 H  HZ1  . LYS   B 1 28  ? 59.068 -22.993 -9.919  1.00 42.37 ?  28  LYS   B HZ1  1 
ATOM   4371 H  HZ2  . LYS   B 1 28  ? 59.648 -21.931 -10.714 1.00 42.37 ?  28  LYS   B HZ2  1 
ATOM   4372 H  HZ3  . LYS   B 1 28  ? 59.199 -21.662 -9.364  1.00 42.37 ?  28  LYS   B HZ3  1 
ATOM   4373 N  N    . LYS   B 1 29  ? 53.444 -20.790 -15.077 1.00 20.54 ?  29  LYS   B N    1 
ATOM   4374 C  CA   . LYS   B 1 29  ? 53.163 -20.954 -16.498 1.00 23.43 ?  29  LYS   B CA   1 
ATOM   4375 C  C    . LYS   B 1 29  ? 51.914 -20.200 -16.943 1.00 22.09 ?  29  LYS   B C    1 
ATOM   4376 O  O    . LYS   B 1 29  ? 51.911 -19.594 -18.020 1.00 23.47 ?  29  LYS   B O    1 
ATOM   4377 C  CB   . LYS   B 1 29  ? 53.029 -22.440 -16.840 1.00 28.53 ?  29  LYS   B CB   1 
ATOM   4378 C  CG   . LYS   B 1 29  ? 52.846 -22.720 -18.322 1.00 33.43 ?  29  LYS   B CG   1 
ATOM   4379 C  CD   . LYS   B 1 29  ? 53.067 -24.193 -18.644 1.00 37.35 ?  29  LYS   B CD   1 
ATOM   4380 C  CE   . LYS   B 1 29  ? 51.948 -25.067 -18.100 1.00 40.13 ?  29  LYS   B CE   1 
ATOM   4381 N  NZ   . LYS   B 1 29  ? 52.196 -26.513 -18.374 1.00 41.55 ?  29  LYS   B NZ   1 
ATOM   4382 H  H    . LYS   B 1 29  ? 53.116 -21.419 -14.574 1.00 24.63 ?  29  LYS   B H    1 
ATOM   4383 H  HA   . LYS   B 1 29  ? 53.912 -20.606 -16.998 1.00 28.10 ?  29  LYS   B HA   1 
ATOM   4384 H  HB2  . LYS   B 1 29  ? 53.835 -22.899 -16.553 1.00 34.22 ?  29  LYS   B HB2  1 
ATOM   4385 H  HB3  . LYS   B 1 29  ? 52.262 -22.802 -16.375 1.00 34.22 ?  29  LYS   B HB3  1 
ATOM   4386 H  HG2  . LYS   B 1 29  ? 51.942 -22.482 -18.581 1.00 40.09 ?  29  LYS   B HG2  1 
ATOM   4387 H  HG3  . LYS   B 1 29  ? 53.488 -22.197 -18.828 1.00 40.09 ?  29  LYS   B HG3  1 
ATOM   4388 H  HD2  . LYS   B 1 29  ? 53.100 -24.308 -19.606 1.00 44.80 ?  29  LYS   B HD2  1 
ATOM   4389 H  HD3  . LYS   B 1 29  ? 53.901 -24.487 -18.243 1.00 44.80 ?  29  LYS   B HD3  1 
ATOM   4390 H  HE2  . LYS   B 1 29  ? 51.884 -24.948 -17.140 1.00 48.14 ?  29  LYS   B HE2  1 
ATOM   4391 H  HE3  . LYS   B 1 29  ? 51.112 -24.817 -18.525 1.00 48.14 ?  29  LYS   B HE3  1 
ATOM   4392 H  HZ1  . LYS   B 1 29  ? 51.529 -27.004 -18.048 1.00 49.84 ?  29  LYS   B HZ1  1 
ATOM   4393 H  HZ2  . LYS   B 1 29  ? 52.254 -26.652 -19.251 1.00 49.84 ?  29  LYS   B HZ2  1 
ATOM   4394 H  HZ3  . LYS   B 1 29  ? 52.957 -26.769 -17.990 1.00 49.84 ?  29  LYS   B HZ3  1 
ATOM   4395 N  N    . VAL   B 1 30  ? 50.855 -20.230 -16.130 1.00 20.23 ?  30  VAL   B N    1 
ATOM   4396 C  CA   . VAL   B 1 30  ? 49.565 -19.645 -16.502 1.00 20.17 ?  30  VAL   B CA   1 
ATOM   4397 C  C    . VAL   B 1 30  ? 49.566 -18.132 -16.367 1.00 18.89 ?  30  VAL   B C    1 
ATOM   4398 O  O    . VAL   B 1 30  ? 48.819 -17.435 -17.075 1.00 19.62 ?  30  VAL   B O    1 
ATOM   4399 C  CB   . VAL   B 1 30  ? 48.463 -20.255 -15.613 1.00 21.11 ?  30  VAL   B CB   1 
ATOM   4400 C  CG1  . VAL   B 1 30  ? 47.173 -19.457 -15.715 1.00 21.62 ?  30  VAL   B CG1  1 
ATOM   4401 C  CG2  . VAL   B 1 30  ? 48.236 -21.714 -15.977 1.00 21.60 ?  30  VAL   B CG2  1 
ATOM   4402 H  H    . VAL   B 1 30  ? 50.850 -20.608 -15.350 1.00 24.26 ?  30  VAL   B H    1 
ATOM   4403 H  HA   . VAL   B 1 30  ? 49.365 -19.880 -17.421 1.00 24.18 ?  30  VAL   B HA   1 
ATOM   4404 H  HB   . VAL   B 1 30  ? 48.753 -20.230 -14.687 1.00 25.32 ?  30  VAL   B HB   1 
ATOM   4405 H  HG11 . VAL   B 1 30  ? 46.435 -20.042 -15.485 1.00 25.93 ?  30  VAL   B HG11 1 
ATOM   4406 H  HG12 . VAL   B 1 30  ? 47.207 -18.714 -15.097 1.00 25.93 ?  30  VAL   B HG12 1 
ATOM   4407 H  HG13 . VAL   B 1 30  ? 47.064 -19.145 -16.622 1.00 25.93 ?  30  VAL   B HG13 1 
ATOM   4408 H  HG21 . VAL   B 1 30  ? 47.547 -22.085 -15.398 1.00 25.90 ?  30  VAL   B HG21 1 
ATOM   4409 H  HG22 . VAL   B 1 30  ? 47.945 -21.768 -16.903 1.00 25.90 ?  30  VAL   B HG22 1 
ATOM   4410 H  HG23 . VAL   B 1 30  ? 49.062 -22.205 -15.861 1.00 25.90 ?  30  VAL   B HG23 1 
ATOM   4411 N  N    . LYS   B 1 31  ? 50.350 -17.614 -15.430 1.00 18.37 ?  31  LYS   B N    1 
ATOM   4412 C  CA   . LYS   B 1 31  ? 50.376 -16.202 -15.083 1.00 18.79 ?  31  LYS   B CA   1 
ATOM   4413 C  C    . LYS   B 1 31  ? 48.980 -15.718 -14.698 1.00 16.68 ?  31  LYS   B C    1 
ATOM   4414 O  O    . LYS   B 1 31  ? 48.446 -14.800 -15.329 1.00 17.56 ?  31  LYS   B O    1 
ATOM   4415 C  CB   . LYS   B 1 31  ? 51.007 -15.394 -16.222 1.00 22.01 ?  31  LYS   B CB   1 
ATOM   4416 C  CG   . LYS   B 1 31  ? 52.453 -15.814 -16.504 1.00 25.67 ?  31  LYS   B CG   1 
ATOM   4417 C  CD   . LYS   B 1 31  ? 53.043 -15.106 -17.707 1.00 29.44 ?  31  LYS   B CD   1 
ATOM   4418 C  CE   . LYS   B 1 31  ? 54.535 -15.340 -17.805 1.00 32.35 ?  31  LYS   B CE   1 
ATOM   4419 N  NZ   . LYS   B 1 31  ? 55.232 -14.850 -16.584 1.00 33.85 ?  31  LYS   B NZ   1 
ATOM   4420 H  H    . LYS   B 1 31  ? 50.901 -18.094 -14.968 1.00 22.03 ?  31  LYS   B H    1 
ATOM   4421 H  HA   . LYS   B 1 31  ? 50.938 -16.105 -14.310 1.00 22.54 ?  31  LYS   B HA   1 
ATOM   4422 H  HB2  . LYS   B 1 31  ? 50.492 -15.524 -17.034 1.00 26.40 ?  31  LYS   B HB2  1 
ATOM   4423 H  HB3  . LYS   B 1 31  ? 51.008 -14.459 -15.972 1.00 26.40 ?  31  LYS   B HB3  1 
ATOM   4424 H  HG2  . LYS   B 1 31  ? 52.994 -15.604 -15.727 1.00 30.79 ?  31  LYS   B HG2  1 
ATOM   4425 H  HG3  . LYS   B 1 31  ? 52.479 -16.770 -16.675 1.00 30.79 ?  31  LYS   B HG3  1 
ATOM   4426 H  HD2  . LYS   B 1 31  ? 52.625 -15.450 -18.511 1.00 35.31 ?  31  LYS   B HD2  1 
ATOM   4427 H  HD3  . LYS   B 1 31  ? 52.886 -14.156 -17.622 1.00 35.31 ?  31  LYS   B HD3  1 
ATOM   4428 H  HE2  . LYS   B 1 31  ? 54.707 -16.291 -17.897 1.00 38.81 ?  31  LYS   B HE2  1 
ATOM   4429 H  HE3  . LYS   B 1 31  ? 54.882 -14.858 -18.572 1.00 38.81 ?  31  LYS   B HE3  1 
ATOM   4430 H  HZ1  . LYS   B 1 31  ? 56.110 -14.843 -16.717 1.00 40.60 ?  31  LYS   B HZ1  1 
ATOM   4431 H  HZ2  . LYS   B 1 31  ? 54.960 -14.025 -16.390 1.00 40.60 ?  31  LYS   B HZ2  1 
ATOM   4432 H  HZ3  . LYS   B 1 31  ? 55.048 -15.383 -15.894 1.00 40.60 ?  31  LYS   B HZ3  1 
ATOM   4433 N  N    . PRO   B 1 32  ? 48.370 -16.303 -13.663 1.00 15.04 ?  32  PRO   B N    1 
ATOM   4434 C  CA   . PRO   B 1 32  ? 46.997 -15.935 -13.298 1.00 14.38 ?  32  PRO   B CA   1 
ATOM   4435 C  C    . PRO   B 1 32  ? 46.927 -14.588 -12.596 1.00 14.14 ?  32  PRO   B C    1 
ATOM   4436 O  O    . PRO   B 1 32  ? 47.855 -14.169 -11.898 1.00 15.52 ?  32  PRO   B O    1 
ATOM   4437 C  CB   . PRO   B 1 32  ? 46.598 -17.046 -12.321 1.00 14.52 ?  32  PRO   B CB   1 
ATOM   4438 C  CG   . PRO   B 1 32  ? 47.902 -17.400 -11.650 1.00 14.82 ?  32  PRO   B CG   1 
ATOM   4439 C  CD   . PRO   B 1 32  ? 48.950 -17.280 -12.719 1.00 15.07 ?  32  PRO   B CD   1 
ATOM   4440 H  HA   . PRO   B 1 32  ? 46.411 -15.951 -14.077 1.00 17.24 ?  32  PRO   B HA   1 
ATOM   4441 H  HB2  . PRO   B 1 32  ? 45.956 -16.707 -11.677 1.00 17.41 ?  32  PRO   B HB2  1 
ATOM   4442 H  HB3  . PRO   B 1 32  ? 46.241 -17.808 -12.803 1.00 17.41 ?  32  PRO   B HB3  1 
ATOM   4443 H  HG2  . PRO   B 1 32  ? 48.073 -16.775 -10.924 1.00 17.77 ?  32  PRO   B HG2  1 
ATOM   4444 H  HG3  . PRO   B 1 32  ? 47.859 -18.308 -11.311 1.00 17.77 ?  32  PRO   B HG3  1 
ATOM   4445 H  HD2  . PRO   B 1 32  ? 49.774 -16.930 -12.348 1.00 18.07 ?  32  PRO   B HD2  1 
ATOM   4446 H  HD3  . PRO   B 1 32  ? 49.084 -18.129 -13.159 1.00 18.07 ?  32  PRO   B HD3  1 
ATOM   4447 N  N    . THR   B 1 33  ? 45.777 -13.926 -12.761 1.00 13.70 ?  33  THR   B N    1 
ATOM   4448 C  CA   . THR   B 1 33  ? 45.485 -12.751 -11.949 1.00 14.18 ?  33  THR   B CA   1 
ATOM   4449 C  C    . THR   B 1 33  ? 45.449 -13.105 -10.467 1.00 13.66 ?  33  THR   B C    1 
ATOM   4450 O  O    . THR   B 1 33  ? 45.930 -12.332 -9.625  1.00 14.63 ?  33  THR   B O    1 
ATOM   4451 C  CB   . THR   B 1 33  ? 44.162 -12.116 -12.392 1.00 14.93 ?  33  THR   B CB   1 
ATOM   4452 O  OG1  . THR   B 1 33  ? 44.200 -11.865 -13.799 1.00 14.79 ?  33  THR   B OG1  1 
ATOM   4453 C  CG2  . THR   B 1 33  ? 43.915 -10.812 -11.645 1.00 16.54 ?  33  THR   B CG2  1 
ATOM   4454 H  H    . THR   B 1 33  ? 45.159 -14.138 -13.329 1.00 16.42 ?  33  THR   B H    1 
ATOM   4455 H  HA   . THR   B 1 33  ? 46.185 -12.099 -12.084 1.00 17.00 ?  33  THR   B HA   1 
ATOM   4456 H  HB   . THR   B 1 33  ? 43.429 -12.725 -12.197 1.00 17.89 ?  33  THR   B HB   1 
ATOM   4457 H  HG1  . THR   B 1 33  ? 43.479 -11.502 -14.048 1.00 17.73 ?  33  THR   B HG1  1 
ATOM   4458 H  HG21 . THR   B 1 33  ? 43.151 -10.352 -12.022 1.00 19.83 ?  33  THR   B HG21 1 
ATOM   4459 H  HG22 . THR   B 1 33  ? 43.744 -10.992 -10.707 1.00 19.83 ?  33  THR   B HG22 1 
ATOM   4460 H  HG23 . THR   B 1 33  ? 44.696 -10.238 -11.717 1.00 19.83 ?  33  THR   B HG23 1 
ATOM   4461 N  N    . VAL   B 1 34  ? 44.893 -14.273 -10.127 1.00 13.26 ?  34  VAL   B N    1 
ATOM   4462 C  CA   . VAL   B 1 34  ? 44.683 -14.663 -8.737  1.00 12.79 ?  34  VAL   B CA   1 
ATOM   4463 C  C    . VAL   B 1 34  ? 45.103 -16.113 -8.560  1.00 11.65 ?  34  VAL   B C    1 
ATOM   4464 O  O    . VAL   B 1 34  ? 44.581 -17.002 -9.242  1.00 12.65 ?  34  VAL   B O    1 
ATOM   4465 C  CB   . VAL   B 1 34  ? 43.208 -14.516 -8.305  1.00 13.93 ?  34  VAL   B CB   1 
ATOM   4466 C  CG1  . VAL   B 1 34  ? 43.033 -14.972 -6.864  1.00 14.36 ?  34  VAL   B CG1  1 
ATOM   4467 C  CG2  . VAL   B 1 34  ? 42.718 -13.094 -8.485  1.00 14.90 ?  34  VAL   B CG2  1 
ATOM   4468 H  H    . VAL   B 1 34  ? 44.634 -14.870 -10.694 1.00 15.90 ?  34  VAL   B H    1 
ATOM   4469 H  HA   . VAL   B 1 34  ? 45.232 -14.109 -8.156  1.00 15.34 ?  34  VAL   B HA   1 
ATOM   4470 H  HB   . VAL   B 1 34  ? 42.663 -15.086 -8.867  1.00 16.70 ?  34  VAL   B HB   1 
ATOM   4471 H  HG11 . VAL   B 1 34  ? 42.182 -14.641 -6.530  1.00 17.21 ?  34  VAL   B HG11 1 
ATOM   4472 H  HG12 . VAL   B 1 34  ? 43.038 -15.942 -6.834  1.00 17.21 ?  34  VAL   B HG12 1 
ATOM   4473 H  HG13 . VAL   B 1 34  ? 43.756 -14.617 -6.327  1.00 17.21 ?  34  VAL   B HG13 1 
ATOM   4474 H  HG21 . VAL   B 1 34  ? 41.795 -13.034 -8.193  1.00 17.86 ?  34  VAL   B HG21 1 
ATOM   4475 H  HG22 . VAL   B 1 34  ? 43.271 -12.495 -7.958  1.00 17.86 ?  34  VAL   B HG22 1 
ATOM   4476 H  HG23 . VAL   B 1 34  ? 42.779 -12.852 -9.426  1.00 17.86 ?  34  VAL   B HG23 1 
ATOM   4477 N  N    . VAL   B 1 35  ? 46.001 -16.364 -7.611  1.00 11.05 ?  35  VAL   B N    1 
ATOM   4478 C  CA   . VAL   B 1 35  ? 46.231 -17.709 -7.093  1.00 10.92 ?  35  VAL   B CA   1 
ATOM   4479 C  C    . VAL   B 1 35  ? 45.698 -17.764 -5.672  1.00 10.73 ?  35  VAL   B C    1 
ATOM   4480 O  O    . VAL   B 1 35  ? 45.918 -16.839 -4.881  1.00 11.10 ?  35  VAL   B O    1 
ATOM   4481 C  CB   . VAL   B 1 35  ? 47.712 -18.142 -7.179  1.00 11.89 ?  35  VAL   B CB   1 
ATOM   4482 C  CG1  . VAL   B 1 35  ? 48.615 -17.313 -6.250  1.00 12.46 ?  35  VAL   B CG1  1 
ATOM   4483 C  CG2  . VAL   B 1 35  ? 47.845 -19.641 -6.884  1.00 12.34 ?  35  VAL   B CG2  1 
ATOM   4484 H  H    . VAL   B 1 35  ? 46.497 -15.764 -7.244  1.00 13.24 ?  35  VAL   B H    1 
ATOM   4485 H  HA   . VAL   B 1 35  ? 45.711 -18.338 -7.618  1.00 13.08 ?  35  VAL   B HA   1 
ATOM   4486 H  HB   . VAL   B 1 35  ? 48.016 -18.003 -8.090  1.00 14.26 ?  35  VAL   B HB   1 
ATOM   4487 H  HG11 . VAL   B 1 35  ? 49.537 -17.537 -6.440  1.00 14.94 ?  35  VAL   B HG11 1 
ATOM   4488 H  HG12 . VAL   B 1 35  ? 48.450 -16.379 -6.414  1.00 14.94 ?  35  VAL   B HG12 1 
ATOM   4489 H  HG13 . VAL   B 1 35  ? 48.400 -17.540 -5.330  1.00 14.94 ?  35  VAL   B HG13 1 
ATOM   4490 H  HG21 . VAL   B 1 35  ? 48.766 -19.913 -6.990  1.00 14.80 ?  35  VAL   B HG21 1 
ATOM   4491 H  HG22 . VAL   B 1 35  ? 47.548 -19.819 -5.975  1.00 14.80 ?  35  VAL   B HG22 1 
ATOM   4492 H  HG23 . VAL   B 1 35  ? 47.282 -20.144 -7.508  1.00 14.80 ?  35  VAL   B HG23 1 
ATOM   4493 N  N    . VAL   B 1 36  ? 44.978 -18.843 -5.355  1.00 10.75 ?  36  VAL   B N    1 
ATOM   4494 C  CA   . VAL   B 1 36  ? 44.429 -19.044 -4.025  1.00 10.29 ?  36  VAL   B CA   1 
ATOM   4495 C  C    . VAL   B 1 36  ? 45.440 -19.802 -3.175  1.00 10.35 ?  36  VAL   B C    1 
ATOM   4496 O  O    . VAL   B 1 36  ? 45.981 -20.837 -3.597  1.00 11.35 ?  36  VAL   B O    1 
ATOM   4497 C  CB   . VAL   B 1 36  ? 43.093 -19.803 -4.098  1.00 11.12 ?  36  VAL   B CB   1 
ATOM   4498 C  CG1  . VAL   B 1 36  ? 42.586 -20.159 -2.708  1.00 11.73 ?  36  VAL   B CG1  1 
ATOM   4499 C  CG2  . VAL   B 1 36  ? 42.062 -18.978 -4.850  1.00 11.50 ?  36  VAL   B CG2  1 
ATOM   4500 H  H    . VAL   B 1 36  ? 44.806 -19.485 -5.901  1.00 12.89 ?  36  VAL   B H    1 
ATOM   4501 H  HA   . VAL   B 1 36  ? 44.264 -18.181 -3.611  1.00 12.33 ?  36  VAL   B HA   1 
ATOM   4502 H  HB   . VAL   B 1 36  ? 43.223 -20.627 -4.589  1.00 13.33 ?  36  VAL   B HB   1 
ATOM   4503 H  HG11 . VAL   B 1 36  ? 41.647 -20.401 -2.765  1.00 14.07 ?  36  VAL   B HG11 1 
ATOM   4504 H  HG12 . VAL   B 1 36  ? 43.097 -20.905 -2.362  1.00 14.07 ?  36  VAL   B HG12 1 
ATOM   4505 H  HG13 . VAL   B 1 36  ? 42.688 -19.387 -2.126  1.00 14.07 ?  36  VAL   B HG13 1 
ATOM   4506 H  HG21 . VAL   B 1 36  ? 41.219 -19.459 -4.873  1.00 13.79 ?  36  VAL   B HG21 1 
ATOM   4507 H  HG22 . VAL   B 1 36  ? 41.941 -18.126 -4.397  1.00 13.79 ?  36  VAL   B HG22 1 
ATOM   4508 H  HG23 . VAL   B 1 36  ? 42.375 -18.823 -5.757  1.00 13.79 ?  36  VAL   B HG23 1 
ATOM   4509 N  N    . ASN   B 1 37  ? 45.655 -19.312 -1.958  1.00 10.61 ?  37  ASN   B N    1 
ATOM   4510 C  CA   . ASN   B 1 37  ? 46.407 -20.035 -0.947  1.00 11.13 ?  37  ASN   B CA   1 
ATOM   4511 C  C    . ASN   B 1 37  ? 45.460 -20.705 0.037   1.00 11.14 ?  37  ASN   B C    1 
ATOM   4512 O  O    . ASN   B 1 37  ? 44.446 -20.127 0.442   1.00 11.75 ?  37  ASN   B O    1 
ATOM   4513 C  CB   . ASN   B 1 37  ? 47.330 -19.087 -0.185  1.00 10.87 ?  37  ASN   B CB   1 
ATOM   4514 C  CG   . ASN   B 1 37  ? 48.188 -19.802 0.824   1.00 11.31 ?  37  ASN   B CG   1 
ATOM   4515 O  OD1  . ASN   B 1 37  ? 48.524 -20.980 0.650   1.00 12.13 ?  37  ASN   B OD1  1 
ATOM   4516 N  ND2  . ASN   B 1 37  ? 48.541 -19.101 1.895   1.00 11.36 ?  37  ASN   B ND2  1 
ATOM   4517 H  H    . ASN   B 1 37  ? 45.365 -18.545 -1.684  1.00 12.72 ?  37  ASN   B H    1 
ATOM   4518 H  HA   . ASN   B 1 37  ? 46.944 -20.720 -1.362  1.00 13.34 ?  37  ASN   B HA   1 
ATOM   4519 H  HB2  . ASN   B 1 37  ? 47.919 -18.650 -0.815  1.00 13.02 ?  37  ASN   B HB2  1 
ATOM   4520 H  HB3  . ASN   B 1 37  ? 46.798 -18.430 0.290   1.00 13.02 ?  37  ASN   B HB3  1 
ATOM   4521 H  HD21 . ASN   B 1 37  ? 49.043 -19.456 2.498   1.00 13.62 ?  37  ASN   B HD21 1 
ATOM   4522 H  HD22 . ASN   B 1 37  ? 48.294 -18.285 1.980   1.00 13.62 ?  37  ASN   B HD22 1 
ATOM   4523 N  N    . ALA   B 1 38  ? 45.807 -21.938 0.414   1.00 11.41 ?  38  ALA   B N    1 
ATOM   4524 C  CA   . ALA   B 1 38  ? 45.153 -22.682 1.491   1.00 11.95 ?  38  ALA   B CA   1 
ATOM   4525 C  C    . ALA   B 1 38  ? 45.740 -22.198 2.813   1.00 11.78 ?  38  ALA   B C    1 
ATOM   4526 O  O    . ALA   B 1 38  ? 46.644 -22.805 3.396   1.00 12.62 ?  38  ALA   B O    1 
ATOM   4527 C  CB   . ALA   B 1 38  ? 45.389 -24.172 1.308   1.00 13.08 ?  38  ALA   B CB   1 
ATOM   4528 H  H    . ALA   B 1 38  ? 46.455 -22.376 0.059   1.00 13.67 ?  38  ALA   B H    1 
ATOM   4529 H  HA   . ALA   B 1 38  ? 44.199 -22.505 1.488   1.00 14.32 ?  38  ALA   B HA   1 
ATOM   4530 H  HB1  . ALA   B 1 38  ? 44.945 -24.653 2.031   1.00 15.68 ?  38  ALA   B HB1  1 
ATOM   4531 H  HB2  . ALA   B 1 38  ? 45.019 -24.446 0.458   1.00 15.68 ?  38  ALA   B HB2  1 
ATOM   4532 H  HB3  . ALA   B 1 38  ? 46.340 -24.348 1.335   1.00 15.68 ?  38  ALA   B HB3  1 
ATOM   4533 N  N    . ALA   B 1 39  ? 45.224 -21.058 3.273   1.00 11.33 ?  39  ALA   B N    1 
ATOM   4534 C  CA   . ALA   B 1 39  ? 45.775 -20.324 4.398   1.00 11.71 ?  39  ALA   B CA   1 
ATOM   4535 C  C    . ALA   B 1 39  ? 45.156 -20.767 5.721   1.00 11.64 ?  39  ALA   B C    1 
ATOM   4536 O  O    . ALA   B 1 39  ? 44.126 -21.439 5.770   1.00 12.83 ?  39  ALA   B O    1 
ATOM   4537 C  CB   . ALA   B 1 39  ? 45.537 -18.823 4.201   1.00 12.21 ?  39  ALA   B CB   1 
ATOM   4538 H  H    . ALA   B 1 39  ? 44.528 -20.678 2.932   1.00 13.58 ?  39  ALA   B H    1 
ATOM   4539 H  HA   . ALA   B 1 39  ? 46.730 -20.473 4.443   1.00 14.03 ?  39  ALA   B HA   1 
ATOM   4540 H  HB1  . ALA   B 1 39  ? 45.906 -18.340 4.956   1.00 14.64 ?  39  ALA   B HB1  1 
ATOM   4541 H  HB2  . ALA   B 1 39  ? 45.971 -18.539 3.381   1.00 14.64 ?  39  ALA   B HB2  1 
ATOM   4542 H  HB3  . ALA   B 1 39  ? 44.581 -18.658 4.140   1.00 14.64 ?  39  ALA   B HB3  1 
ATOM   4543 N  N    . ASN   B 1 40  ? 45.797 -20.344 6.807   1.00 12.23 ?  40  ASN   B N    1 
ATOM   4544 C  CA   . ASN   B 1 40  ? 45.234 -20.396 8.145   1.00 13.08 ?  40  ASN   B CA   1 
ATOM   4545 C  C    . ASN   B 1 40  ? 45.047 -18.970 8.667   1.00 13.12 ?  40  ASN   B C    1 
ATOM   4546 O  O    . ASN   B 1 40  ? 45.451 -17.988 8.036   1.00 13.08 ?  40  ASN   B O    1 
ATOM   4547 C  CB   . ASN   B 1 40  ? 46.090 -21.264 9.083   1.00 14.04 ?  40  ASN   B CB   1 
ATOM   4548 C  CG   . ASN   B 1 40  ? 47.540 -20.853 9.105   1.00 15.02 ?  40  ASN   B CG   1 
ATOM   4549 O  OD1  . ASN   B 1 40  ? 47.859 -19.669 9.174   1.00 16.94 ?  40  ASN   B OD1  1 
ATOM   4550 N  ND2  . ASN   B 1 40  ? 48.431 -21.828 9.061   1.00 14.99 ?  40  ASN   B ND2  1 
ATOM   4551 H  H    . ASN   B 1 40  ? 46.594 -20.018 6.788   1.00 14.67 ?  40  ASN   B H    1 
ATOM   4552 H  HA   . ASN   B 1 40  ? 44.356 -20.799 8.097   1.00 15.68 ?  40  ASN   B HA   1 
ATOM   4553 H  HB2  . ASN   B 1 40  ? 45.741 -21.191 9.985   1.00 16.83 ?  40  ASN   B HB2  1 
ATOM   4554 H  HB3  . ASN   B 1 40  ? 46.043 -22.187 8.784   1.00 16.83 ?  40  ASN   B HB3  1 
ATOM   4555 H  HD21 . ASN   B 1 40  ? 49.271 -21.648 9.073   1.00 17.97 ?  40  ASN   B HD21 1 
ATOM   4556 H  HD22 . ASN   B 1 40  ? 48.169 -22.648 9.013   1.00 17.97 ?  40  ASN   B HD22 1 
ATOM   4557 N  N    . VAL   B 1 41  ? 44.396 -18.847 9.825   1.00 13.51 ?  41  VAL   B N    1 
ATOM   4558 C  CA   . VAL   B 1 41  ? 43.936 -17.528 10.270  1.00 14.00 ?  41  VAL   B CA   1 
ATOM   4559 C  C    . VAL   B 1 41  ? 45.087 -16.572 10.555  1.00 13.84 ?  41  VAL   B C    1 
ATOM   4560 O  O    . VAL   B 1 41  ? 44.912 -15.350 10.453  1.00 13.96 ?  41  VAL   B O    1 
ATOM   4561 C  CB   . VAL   B 1 41  ? 42.968 -17.607 11.468  1.00 15.67 ?  41  VAL   B CB   1 
ATOM   4562 C  CG1  . VAL   B 1 41  ? 41.667 -18.293 11.073  1.00 16.32 ?  41  VAL   B CG1  1 
ATOM   4563 C  CG2  . VAL   B 1 41  ? 43.630 -18.285 12.662  1.00 16.61 ?  41  VAL   B CG2  1 
ATOM   4564 H  H    . VAL   B 1 41  ? 44.213 -19.491 10.357  1.00 16.20 ?  41  VAL   B H    1 
ATOM   4565 H  HA   . VAL   B 1 41  ? 43.435 -17.135 9.543   1.00 16.78 ?  41  VAL   B HA   1 
ATOM   4566 H  HB   . VAL   B 1 41  ? 42.744 -16.703 11.741  1.00 18.78 ?  41  VAL   B HB   1 
ATOM   4567 H  HG11 . VAL   B 1 41  ? 41.070 -18.305 11.837  1.00 19.56 ?  41  VAL   B HG11 1 
ATOM   4568 H  HG12 . VAL   B 1 41  ? 41.261 -17.802 10.342  1.00 19.56 ?  41  VAL   B HG12 1 
ATOM   4569 H  HG13 . VAL   B 1 41  ? 41.863 -19.202 10.793  1.00 19.56 ?  41  VAL   B HG13 1 
ATOM   4570 H  HG21 . VAL   B 1 41  ? 42.997 -18.322 13.396  1.00 19.92 ?  41  VAL   B HG21 1 
ATOM   4571 H  HG22 . VAL   B 1 41  ? 43.895 -19.184 12.409  1.00 19.92 ?  41  VAL   B HG22 1 
ATOM   4572 H  HG23 . VAL   B 1 41  ? 44.411 -17.773 12.925  1.00 19.92 ?  41  VAL   B HG23 1 
ATOM   4573 N  N    . TYR   B 1 42  ? 46.256 -17.087 10.943  1.00 14.10 ?  42  TYR   B N    1 
ATOM   4574 C  CA   . TYR   B 1 42  ? 47.407 -16.240 11.219  1.00 14.40 ?  42  TYR   B CA   1 
ATOM   4575 C  C    . TYR   B 1 42  ? 48.376 -16.163 10.041  1.00 13.83 ?  42  TYR   B C    1 
ATOM   4576 O  O    . TYR   B 1 42  ? 49.465 -15.595 10.179  1.00 14.82 ?  42  TYR   B O    1 
ATOM   4577 C  CB   . TYR   B 1 42  ? 48.090 -16.655 12.529  1.00 15.88 ?  42  TYR   B CB   1 
ATOM   4578 C  CG   . TYR   B 1 42  ? 47.509 -15.948 13.753  1.00 15.96 ?  42  TYR   B CG   1 
ATOM   4579 C  CD1  . TYR   B 1 42  ? 47.735 -14.593 13.957  1.00 15.26 ?  42  TYR   B CD1  1 
ATOM   4580 C  CD2  . TYR   B 1 42  ? 46.747 -16.627 14.696  1.00 17.38 ?  42  TYR   B CD2  1 
ATOM   4581 C  CE1  . TYR   B 1 42  ? 47.224 -13.932 15.050  1.00 15.83 ?  42  TYR   B CE1  1 
ATOM   4582 C  CE2  . TYR   B 1 42  ? 46.232 -15.968 15.806  1.00 17.41 ?  42  TYR   B CE2  1 
ATOM   4583 C  CZ   . TYR   B 1 42  ? 46.477 -14.615 15.976  1.00 17.19 ?  42  TYR   B CZ   1 
ATOM   4584 O  OH   . TYR   B 1 42  ? 45.989 -13.920 17.067  1.00 19.64 ?  42  TYR   B OH   1 
ATOM   4585 H  H    . TYR   B 1 42  ? 46.407 -17.934 11.040  1.00 16.90 ?  42  TYR   B H    1 
ATOM   4586 H  HA   . TYR   B 1 42  ? 47.077 -15.343 11.357  1.00 17.27 ?  42  TYR   B HA   1 
ATOM   4587 H  HB2  . TYR   B 1 42  ? 47.982 -17.610 12.653  1.00 19.04 ?  42  TYR   B HB2  1 
ATOM   4588 H  HB3  . TYR   B 1 42  ? 49.035 -16.435 12.472  1.00 19.04 ?  42  TYR   B HB3  1 
ATOM   4589 H  HD1  . TYR   B 1 42  ? 48.248 -14.120 13.330  1.00 18.30 ?  42  TYR   B HD1  1 
ATOM   4590 H  HD2  . TYR   B 1 42  ? 46.583 -17.539 14.579  1.00 20.84 ?  42  TYR   B HD2  1 
ATOM   4591 H  HE1  . TYR   B 1 42  ? 47.394 -13.024 15.161  1.00 18.98 ?  42  TYR   B HE1  1 
ATOM   4592 H  HE2  . TYR   B 1 42  ? 45.721 -16.434 16.426  1.00 20.87 ?  42  TYR   B HE2  1 
ATOM   4593 H  HH   . TYR   B 1 42  ? 46.218 -13.118 17.015  1.00 23.56 ?  42  TYR   B HH   1 
ATOM   4594 N  N    . LEU   B 1 43  ? 47.979 -16.668 8.876   1.00 12.93 ?  43  LEU   B N    1 
ATOM   4595 C  CA   . LEU   B 1 43  ? 48.795 -16.601 7.667   1.00 12.71 ?  43  LEU   B CA   1 
ATOM   4596 C  C    . LEU   B 1 43  ? 50.208 -17.108 7.926   1.00 12.73 ?  43  LEU   B C    1 
ATOM   4597 O  O    . LEU   B 1 43  ? 51.190 -16.519 7.474   1.00 13.62 ?  43  LEU   B O    1 
ATOM   4598 C  CB   . LEU   B 1 43  ? 48.811 -15.202 7.046   1.00 12.61 ?  43  LEU   B CB   1 
ATOM   4599 C  CG   . LEU   B 1 43  ? 47.455 -14.584 6.684   1.00 13.06 ?  43  LEU   B CG   1 
ATOM   4600 C  CD1  . LEU   B 1 43  ? 47.669 -13.187 6.100   1.00 14.24 ?  43  LEU   B CD1  1 
ATOM   4601 C  CD2  . LEU   B 1 43  ? 46.678 -15.476 5.719   1.00 13.32 ?  43  LEU   B CD2  1 
ATOM   4602 H  H    . LEU   B 1 43  ? 47.229 -17.064 8.755   1.00 15.50 ?  43  LEU   B H    1 
ATOM   4603 H  HA   . LEU   B 1 43  ? 48.401 -17.195 7.007   1.00 15.23 ?  43  LEU   B HA   1 
ATOM   4604 H  HB2  . LEU   B 1 43  ? 49.249 -14.601 7.667   1.00 15.12 ?  43  LEU   B HB2  1 
ATOM   4605 H  HB3  . LEU   B 1 43  ? 49.333 -15.245 6.225   1.00 15.12 ?  43  LEU   B HB3  1 
ATOM   4606 H  HG   . LEU   B 1 43  ? 46.934 -14.486 7.492   1.00 15.65 ?  43  LEU   B HG   1 
ATOM   4607 H  HD11 . LEU   B 1 43  ? 46.806 -12.802 5.878   1.00 17.07 ?  43  LEU   B HD11 1 
ATOM   4608 H  HD12 . LEU   B 1 43  ? 48.115 -12.631 6.762   1.00 17.07 ?  43  LEU   B HD12 1 
ATOM   4609 H  HD13 . LEU   B 1 43  ? 48.217 -13.254 5.303   1.00 17.07 ?  43  LEU   B HD13 1 
ATOM   4610 H  HD21 . LEU   B 1 43  ? 45.869 -15.010 5.445   1.00 15.97 ?  43  LEU   B HD21 1 
ATOM   4611 H  HD22 . LEU   B 1 43  ? 47.229 -15.663 4.946   1.00 15.97 ?  43  LEU   B HD22 1 
ATOM   4612 H  HD23 . LEU   B 1 43  ? 46.446 -16.299 6.173   1.00 15.97 ?  43  LEU   B HD23 1 
ATOM   4613 N  N    . LYS   B 1 44  ? 50.304 -18.234 8.637   1.00 12.99 ?  44  LYS   B N    1 
ATOM   4614 C  CA   . LYS   B 1 44  ? 51.571 -18.912 8.881   1.00 13.60 ?  44  LYS   B CA   1 
ATOM   4615 C  C    . LYS   B 1 44  ? 51.690 -20.031 7.856   1.00 13.07 ?  44  LYS   B C    1 
ATOM   4616 O  O    . LYS   B 1 44  ? 50.994 -21.048 7.946   1.00 14.52 ?  44  LYS   B O    1 
ATOM   4617 C  CB   . LYS   B 1 44  ? 51.617 -19.424 10.318  1.00 15.71 ?  44  LYS   B CB   1 
ATOM   4618 C  CG   . LYS   B 1 44  ? 51.821 -18.316 11.337  1.00 18.19 ?  44  LYS   B CG   1 
ATOM   4619 C  CD   . LYS   B 1 44  ? 52.996 -17.435 10.902  1.00 21.29 ?  44  LYS   B CD   1 
ATOM   4620 C  CE   . LYS   B 1 44  ? 53.636 -16.681 12.039  1.00 24.02 ?  44  LYS   B CE   1 
ATOM   4621 N  NZ   . LYS   B 1 44  ? 54.724 -15.783 11.592  1.00 25.04 ?  44  LYS   B NZ   1 
ATOM   4622 H  H    . LYS   B 1 44  ? 49.629 -18.627 8.997   1.00 15.57 ?  44  LYS   B H    1 
ATOM   4623 H  HA   . LYS   B 1 44  ? 52.300 -18.297 8.718   1.00 16.31 ?  44  LYS   B HA   1 
ATOM   4624 H  HB2  . LYS   B 1 44  ? 50.770 -19.864 10.523  1.00 18.83 ?  44  LYS   B HB2  1 
ATOM   4625 H  HB3  . LYS   B 1 44  ? 52.343 -20.055 10.408  1.00 18.83 ?  44  LYS   B HB3  1 
ATOM   4626 H  HG2  . LYS   B 1 44  ? 51.023 -17.772 11.394  1.00 21.82 ?  44  LYS   B HG2  1 
ATOM   4627 H  HG3  . LYS   B 1 44  ? 52.032 -18.707 12.202  1.00 21.82 ?  44  LYS   B HG3  1 
ATOM   4628 H  HD2  . LYS   B 1 44  ? 53.670 -18.003 10.485  1.00 25.53 ?  44  LYS   B HD2  1 
ATOM   4629 H  HD3  . LYS   B 1 44  ? 52.670 -16.788 10.254  1.00 25.53 ?  44  LYS   B HD3  1 
ATOM   4630 H  HE2  . LYS   B 1 44  ? 52.973 -16.106 12.420  1.00 28.80 ?  44  LYS   B HE2  1 
ATOM   4631 H  HE3  . LYS   B 1 44  ? 53.979 -17.309 12.699  1.00 28.80 ?  44  LYS   B HE3  1 
ATOM   4632 H  HZ1  . LYS   B 1 44  ? 55.069 -15.354 12.291  1.00 30.03 ?  44  LYS   B HZ1  1 
ATOM   4633 H  HZ2  . LYS   B 1 44  ? 55.364 -16.249 11.191  1.00 30.03 ?  44  LYS   B HZ2  1 
ATOM   4634 H  HZ3  . LYS   B 1 44  ? 54.401 -15.180 11.017  1.00 30.03 ?  44  LYS   B HZ3  1 
ATOM   4635 N  N    . HIS   B 1 45  ? 52.544 -19.817 6.857   1.00 12.90 ?  45  HIS   B N    1 
ATOM   4636 C  CA   . HIS   B 1 45  ? 52.563 -20.649 5.656   1.00 13.01 ?  45  HIS   B CA   1 
ATOM   4637 C  C    . HIS   B 1 45  ? 53.575 -21.779 5.820   1.00 14.84 ?  45  HIS   B C    1 
ATOM   4638 O  O    . HIS   B 1 45  ? 54.630 -21.808 5.196   1.00 17.30 ?  45  HIS   B O    1 
ATOM   4639 C  CB   . HIS   B 1 45  ? 52.876 -19.796 4.438   1.00 13.02 ?  45  HIS   B CB   1 
ATOM   4640 C  CG   . HIS   B 1 45  ? 52.010 -18.591 4.329   1.00 12.90 ?  45  HIS   B CG   1 
ATOM   4641 N  ND1  . HIS   B 1 45  ? 50.634 -18.671 4.300   1.00 12.85 ?  45  HIS   B ND1  1 
ATOM   4642 C  CD2  . HIS   B 1 45  ? 52.328 -17.277 4.253   1.00 13.43 ?  45  HIS   B CD2  1 
ATOM   4643 C  CE1  . HIS   B 1 45  ? 50.147 -17.447 4.197   1.00 12.47 ?  45  HIS   B CE1  1 
ATOM   4644 N  NE2  . HIS   B 1 45  ? 51.150 -16.583 4.166   1.00 12.94 ?  45  HIS   B NE2  1 
ATOM   4645 H  H    . HIS   B 1 45  ? 53.118 -19.175 6.844   1.00 15.46 ?  45  HIS   B H    1 
ATOM   4646 H  HA   . HIS   B 1 45  ? 51.680 -21.039 5.527   1.00 15.59 ?  45  HIS   B HA   1 
ATOM   4647 H  HB2  . HIS   B 1 45  ? 53.797 -19.502 4.488   1.00 15.61 ?  45  HIS   B HB2  1 
ATOM   4648 H  HB3  . HIS   B 1 45  ? 52.745 -20.334 3.636   1.00 15.61 ?  45  HIS   B HB3  1 
ATOM   4649 H  HD2  . HIS   B 1 45  ? 53.184 -16.912 4.253   1.00 16.10 ?  45  HIS   B HD2  1 
ATOM   4650 H  HE1  . HIS   B 1 45  ? 49.243 -17.229 4.149   1.00 14.95 ?  45  HIS   B HE1  1 
ATOM   4651 H  HE2  . HIS   B 1 45  ? 51.070 -15.729 4.109   1.00 15.51 ?  45  HIS   B HE2  1 
ATOM   4652 N  N    . GLY   B 1 46  ? 53.209 -22.740 6.659   1.00 16.01 ?  46  GLY   B N    1 
ATOM   4653 C  CA   . GLY   B 1 46  ? 54.133 -23.794 7.030   1.00 17.97 ?  46  GLY   B CA   1 
ATOM   4654 C  C    . GLY   B 1 46  ? 54.192 -24.989 6.098   1.00 19.30 ?  46  GLY   B C    1 
ATOM   4655 O  O    . GLY   B 1 46  ? 55.271 -25.398 5.662   1.00 22.59 ?  46  GLY   B O    1 
ATOM   4656 H  H    . GLY   B 1 46  ? 52.434 -22.785 7.041   1.00 19.19 ?  46  GLY   B H    1 
ATOM   4657 H  HA2  . GLY   B 1 46  ? 55.021 -23.416 7.090   1.00 21.55 ?  46  GLY   B HA2  1 
ATOM   4658 H  HA3  . GLY   B 1 46  ? 53.887 -24.120 7.910   1.00 21.55 ?  46  GLY   B HA3  1 
ATOM   4659 N  N    . GLY   B 1 47  ? 53.039 -25.565 5.776   1.00 18.73 ?  47  GLY   B N    1 
ATOM   4660 C  CA   . GLY   B 1 47  ? 52.989 -26.858 5.121   1.00 16.98 ?  47  GLY   B CA   1 
ATOM   4661 C  C    . GLY   B 1 47  ? 52.067 -26.845 3.917   1.00 14.98 ?  47  GLY   B C    1 
ATOM   4662 O  O    . GLY   B 1 47  ? 51.407 -25.848 3.632   1.00 15.05 ?  47  GLY   B O    1 
ATOM   4663 H  H    . GLY   B 1 47  ? 52.261 -25.227 5.941   1.00 22.46 ?  47  GLY   B H    1 
ATOM   4664 H  HA2  . GLY   B 1 47  ? 53.877 -27.109 4.827   1.00 20.35 ?  47  GLY   B HA2  1 
ATOM   4665 H  HA3  . GLY   B 1 47  ? 52.672 -27.527 5.751   1.00 20.35 ?  47  GLY   B HA3  1 
ATOM   4666 N  N    . GLY   B 1 48  ? 52.025 -27.984 3.230   1.00 14.03 ?  48  GLY   B N    1 
ATOM   4667 C  CA   . GLY   B 1 48  ? 51.091 -28.128 2.129   1.00 14.00 ?  48  GLY   B CA   1 
ATOM   4668 C  C    . GLY   B 1 48  ? 51.228 -27.018 1.115   1.00 13.20 ?  48  GLY   B C    1 
ATOM   4669 O  O    . GLY   B 1 48  ? 52.332 -26.552 0.804   1.00 13.81 ?  48  GLY   B O    1 
ATOM   4670 H  H    . GLY   B 1 48  ? 52.518 -28.668 3.378   1.00 16.82 ?  48  GLY   B H    1 
ATOM   4671 H  HA2  . GLY   B 1 48  ? 51.244 -28.977 1.681   1.00 16.79 ?  48  GLY   B HA2  1 
ATOM   4672 H  HA3  . GLY   B 1 48  ? 50.180 -28.122 2.466   1.00 16.79 ?  48  GLY   B HA3  1 
ATOM   4673 N  N    . VAL   B 1 49  ? 50.082 -26.585 0.587   1.00 12.81 ?  49  VAL   B N    1 
ATOM   4674 C  CA   . VAL   B 1 49  ? 50.069 -25.565 -0.459  1.00 13.08 ?  49  VAL   B CA   1 
ATOM   4675 C  C    . VAL   B 1 49  ? 50.731 -24.279 0.028   1.00 12.16 ?  49  VAL   B C    1 
ATOM   4676 O  O    . VAL   B 1 49  ? 51.527 -23.662 -0.687  1.00 13.10 ?  49  VAL   B O    1 
ATOM   4677 C  CB   . VAL   B 1 49  ? 48.624 -25.309 -0.936  1.00 14.31 ?  49  VAL   B CB   1 
ATOM   4678 C  CG1  . VAL   B 1 49  ? 48.552 -24.065 -1.813  1.00 14.26 ?  49  VAL   B CG1  1 
ATOM   4679 C  CG2  . VAL   B 1 49  ? 48.072 -26.520 -1.681  1.00 15.86 ?  49  VAL   B CG2  1 
ATOM   4680 H  H    . VAL   B 1 49  ? 49.294 -26.860 0.815   1.00 15.36 ?  49  VAL   B H    1 
ATOM   4681 H  HA   . VAL   B 1 49  ? 50.570 -25.889 -1.221  1.00 15.68 ?  49  VAL   B HA   1 
ATOM   4682 H  HB   . VAL   B 1 49  ? 48.057 -25.154 -0.166  1.00 17.15 ?  49  VAL   B HB   1 
ATOM   4683 H  HG11 . VAL   B 1 49  ? 47.719 -24.076 -2.313  1.00 17.10 ?  49  VAL   B HG11 1 
ATOM   4684 H  HG12 . VAL   B 1 49  ? 48.580 -23.274 -1.248  1.00 17.10 ?  49  VAL   B HG12 1 
ATOM   4685 H  HG13 . VAL   B 1 49  ? 49.302 -24.063 -2.425  1.00 17.10 ?  49  VAL   B HG13 1 
ATOM   4686 H  HG21 . VAL   B 1 49  ? 47.163 -26.331 -1.965  1.00 19.01 ?  49  VAL   B HG21 1 
ATOM   4687 H  HG22 . VAL   B 1 49  ? 48.630 -26.694 -2.455  1.00 19.01 ?  49  VAL   B HG22 1 
ATOM   4688 H  HG23 . VAL   B 1 49  ? 48.082 -27.283 -1.086  1.00 19.01 ?  49  VAL   B HG23 1 
ATOM   4689 N  N    . ALA   B 1 50  ? 50.383 -23.833 1.236   1.00 12.07 ?  50  ALA   B N    1 
ATOM   4690 C  CA   . ALA   B 1 50  ? 50.905 -22.556 1.715   1.00 11.87 ?  50  ALA   B CA   1 
ATOM   4691 C  C    . ALA   B 1 50  ? 52.422 -22.589 1.827   1.00 12.14 ?  50  ALA   B C    1 
ATOM   4692 O  O    . ALA   B 1 50  ? 53.104 -21.625 1.456   1.00 12.37 ?  50  ALA   B O    1 
ATOM   4693 C  CB   . ALA   B 1 50  ? 50.283 -22.203 3.061   1.00 12.16 ?  50  ALA   B CB   1 
ATOM   4694 H  H    . ALA   B 1 50  ? 49.856 -24.236 1.782   1.00 14.46 ?  50  ALA   B H    1 
ATOM   4695 H  HA   . ALA   B 1 50  ? 50.674 -21.860 1.084   1.00 14.23 ?  50  ALA   B HA   1 
ATOM   4696 H  HB1  . ALA   B 1 50  ? 50.643 -21.350 3.361   1.00 14.57 ?  50  ALA   B HB1  1 
ATOM   4697 H  HB2  . ALA   B 1 50  ? 49.321 -22.133 2.954   1.00 14.57 ?  50  ALA   B HB2  1 
ATOM   4698 H  HB3  . ALA   B 1 50  ? 50.498 -22.895 3.702   1.00 14.57 ?  50  ALA   B HB3  1 
ATOM   4699 N  N    . GLY   B 1 51  ? 52.972 -23.685 2.342   1.00 12.68 ?  51  GLY   B N    1 
ATOM   4700 C  CA   . GLY   B 1 51  ? 54.415 -23.793 2.411   1.00 13.27 ?  51  GLY   B CA   1 
ATOM   4701 C  C    . GLY   B 1 51  ? 55.059 -23.743 1.042   1.00 13.03 ?  51  GLY   B C    1 
ATOM   4702 O  O    . GLY   B 1 51  ? 56.102 -23.109 0.859   1.00 14.07 ?  51  GLY   B O    1 
ATOM   4703 H  H    . GLY   B 1 51  ? 52.542 -24.363 2.647   1.00 15.20 ?  51  GLY   B H    1 
ATOM   4704 H  HA2  . GLY   B 1 51  ? 54.773 -23.062 2.942   1.00 15.91 ?  51  GLY   B HA2  1 
ATOM   4705 H  HA3  . GLY   B 1 51  ? 54.662 -24.629 2.835   1.00 15.91 ?  51  GLY   B HA3  1 
ATOM   4706 N  N    . ALA   B 1 52  ? 54.455 -24.413 0.062   1.00 12.72 ?  52  ALA   B N    1 
ATOM   4707 C  CA   . ALA   B 1 52  ? 55.018 -24.416 -1.281  1.00 13.13 ?  52  ALA   B CA   1 
ATOM   4708 C  C    . ALA   B 1 52  ? 54.942 -23.035 -1.927  1.00 12.38 ?  52  ALA   B C    1 
ATOM   4709 O  O    . ALA   B 1 52  ? 55.915 -22.582 -2.548  1.00 13.22 ?  52  ALA   B O    1 
ATOM   4710 C  CB   . ALA   B 1 52  ? 54.312 -25.456 -2.143  1.00 13.91 ?  52  ALA   B CB   1 
ATOM   4711 H  H    . ALA   B 1 52  ? 53.716 -24.851 0.146   1.00 15.25 ?  52  ALA   B H    1 
ATOM   4712 H  HA   . ALA   B 1 52  ? 55.950 -24.663 -1.221  1.00 15.74 ?  52  ALA   B HA   1 
ATOM   4713 H  HB1  . ALA   B 1 52  ? 54.705 -25.448 -3.031  1.00 16.68 ?  52  ALA   B HB1  1 
ATOM   4714 H  HB2  . ALA   B 1 52  ? 54.432 -26.332 -1.739  1.00 16.68 ?  52  ALA   B HB2  1 
ATOM   4715 H  HB3  . ALA   B 1 52  ? 53.370 -25.242 -2.195  1.00 16.68 ?  52  ALA   B HB3  1 
ATOM   4716 N  N    . LEU   B 1 53  ? 53.796 -22.355 -1.812  1.00 12.08 ?  53  LEU   B N    1 
ATOM   4717 C  CA   . LEU   B 1 53  ? 53.689 -21.014 -2.380  1.00 12.36 ?  53  LEU   B CA   1 
ATOM   4718 C  C    . LEU   B 1 53  ? 54.699 -20.078 -1.732  1.00 12.21 ?  53  LEU   B C    1 
ATOM   4719 O  O    . LEU   B 1 53  ? 55.404 -19.329 -2.420  1.00 12.78 ?  53  LEU   B O    1 
ATOM   4720 C  CB   . LEU   B 1 53  ? 52.272 -20.464 -2.209  1.00 12.87 ?  53  LEU   B CB   1 
ATOM   4721 C  CG   . LEU   B 1 53  ? 51.134 -21.189 -2.930  1.00 13.00 ?  53  LEU   B CG   1 
ATOM   4722 C  CD1  . LEU   B 1 53  ? 49.797 -20.575 -2.581  1.00 14.37 ?  53  LEU   B CD1  1 
ATOM   4723 C  CD2  . LEU   B 1 53  ? 51.334 -21.190 -4.438  1.00 14.97 ?  53  LEU   B CD2  1 
ATOM   4724 H  H    . LEU   B 1 53  ? 53.088 -22.640 -1.421  1.00 14.48 ?  53  LEU   B H    1 
ATOM   4725 H  HA   . LEU   B 1 53  ? 53.889 -21.058 -3.334  1.00 14.82 ?  53  LEU   B HA   1 
ATOM   4726 H  HB2  . LEU   B 1 53  ? 52.064 -20.479 -1.266  1.00 15.42 ?  53  LEU   B HB2  1 
ATOM   4727 H  HB3  . LEU   B 1 53  ? 52.270 -19.550 -2.527  1.00 15.42 ?  53  LEU   B HB3  1 
ATOM   4728 H  HG   . LEU   B 1 53  ? 51.114 -22.113 -2.637  1.00 15.58 ?  53  LEU   B HG   1 
ATOM   4729 H  HD11 . LEU   B 1 53  ? 49.094 -21.057 -3.049  1.00 17.22 ?  53  LEU   B HD11 1 
ATOM   4730 H  HD12 . LEU   B 1 53  ? 49.658 -20.645 -1.622  1.00 17.22 ?  53  LEU   B HD12 1 
ATOM   4731 H  HD13 . LEU   B 1 53  ? 49.794 -19.645 -2.849  1.00 17.22 ?  53  LEU   B HD13 1 
ATOM   4732 H  HD21 . LEU   B 1 53  ? 50.623 -21.707 -4.852  1.00 17.94 ?  53  LEU   B HD21 1 
ATOM   4733 H  HD22 . LEU   B 1 53  ? 51.306 -20.278 -4.762  1.00 17.94 ?  53  LEU   B HD22 1 
ATOM   4734 H  HD23 . LEU   B 1 53  ? 52.192 -21.592 -4.646  1.00 17.94 ?  53  LEU   B HD23 1 
ATOM   4735 N  N    . ASN   B 1 54  ? 54.788 -20.108 -0.403  1.00 12.09 ?  54  ASN   B N    1 
ATOM   4736 C  CA   . ASN   B 1 54  ? 55.705 -19.197 0.268   1.00 12.84 ?  54  ASN   B CA   1 
ATOM   4737 C  C    . ASN   B 1 54  ? 57.149 -19.479 -0.126  1.00 13.25 ?  54  ASN   B C    1 
ATOM   4738 O  O    . ASN   B 1 54  ? 57.925 -18.543 -0.360  1.00 13.49 ?  54  ASN   B O    1 
ATOM   4739 C  CB   . ASN   B 1 54  ? 55.540 -19.266 1.780   1.00 13.76 ?  54  ASN   B CB   1 
ATOM   4740 C  CG   . ASN   B 1 54  ? 56.519 -18.349 2.488   1.00 13.68 ?  54  ASN   B CG   1 
ATOM   4741 O  OD1  . ASN   B 1 54  ? 56.542 -17.142 2.236   1.00 13.69 ?  54  ASN   B OD1  1 
ATOM   4742 N  ND2  . ASN   B 1 54  ? 57.354 -18.915 3.349   1.00 15.10 ?  54  ASN   B ND2  1 
ATOM   4743 H  H    . ASN   B 1 54  ? 54.346 -20.638 0.111   1.00 14.50 ?  54  ASN   B H    1 
ATOM   4744 H  HA   . ASN   B 1 54  ? 55.492 -18.296 -0.011  1.00 15.40 ?  54  ASN   B HA   1 
ATOM   4745 H  HB2  . ASN   B 1 54  ? 54.637 -18.990 2.018   1.00 16.49 ?  54  ASN   B HB2  1 
ATOM   4746 H  HB3  . ASN   B 1 54  ? 55.699 -20.173 2.082   1.00 16.49 ?  54  ASN   B HB3  1 
ATOM   4747 H  HD21 . ASN   B 1 54  ? 57.933 -18.432 3.768   1.00 18.11 ?  54  ASN   B HD21 1 
ATOM   4748 H  HD22 . ASN   B 1 54  ? 57.319 -19.761 3.493   1.00 18.11 ?  54  ASN   B HD22 1 
ATOM   4749 N  N    . LYS   B 1 55  ? 57.537 -20.756 -0.186  1.00 13.60 ?  55  LYS   B N    1 
ATOM   4750 C  CA   . LYS   B 1 55  ? 58.892 -21.097 -0.607  1.00 14.77 ?  55  LYS   B CA   1 
ATOM   4751 C  C    . LYS   B 1 55  ? 59.186 -20.558 -2.000  1.00 14.25 ?  55  LYS   B C    1 
ATOM   4752 O  O    . LYS   B 1 55  ? 60.285 -20.054 -2.258  1.00 15.10 ?  55  LYS   B O    1 
ATOM   4753 C  CB   . LYS   B 1 55  ? 59.085 -22.613 -0.556  1.00 16.44 ?  55  LYS   B CB   1 
ATOM   4754 C  CG   . LYS   B 1 55  ? 60.448 -23.085 -1.017  1.00 20.29 ?  55  LYS   B CG   1 
ATOM   4755 C  CD   . LYS   B 1 55  ? 60.614 -24.584 -0.832  1.00 23.83 ?  55  LYS   B CD   1 
ATOM   4756 C  CE   . LYS   B 1 55  ? 60.663 -24.969 0.645   1.00 26.66 ?  55  LYS   B CE   1 
ATOM   4757 N  NZ   . LYS   B 1 55  ? 61.050 -26.385 0.839   1.00 28.12 ?  55  LYS   B NZ   1 
ATOM   4758 H  H    . LYS   B 1 55  ? 57.037 -21.428 0.006   1.00 16.30 ?  55  LYS   B H    1 
ATOM   4759 H  HA   . LYS   B 1 55  ? 59.522 -20.693 0.008   1.00 17.71 ?  55  LYS   B HA   1 
ATOM   4760 H  HB2  . LYS   B 1 55  ? 58.961 -22.901 0.362   1.00 19.72 ?  55  LYS   B HB2  1 
ATOM   4761 H  HB3  . LYS   B 1 55  ? 58.420 -23.030 -1.123  1.00 19.72 ?  55  LYS   B HB3  1 
ATOM   4762 H  HG2  . LYS   B 1 55  ? 60.556 -22.883 -1.959  1.00 24.34 ?  55  LYS   B HG2  1 
ATOM   4763 H  HG3  . LYS   B 1 55  ? 61.134 -22.635 -0.497  1.00 24.34 ?  55  LYS   B HG3  1 
ATOM   4764 H  HD2  . LYS   B 1 55  ? 59.865 -25.046 -1.239  1.00 28.58 ?  55  LYS   B HD2  1 
ATOM   4765 H  HD3  . LYS   B 1 55  ? 61.448 -24.870 -1.243  1.00 28.58 ?  55  LYS   B HD3  1 
ATOM   4766 H  HE2  . LYS   B 1 55  ? 61.313 -24.403 1.095   1.00 31.97 ?  55  LYS   B HE2  1 
ATOM   4767 H  HE3  . LYS   B 1 55  ? 59.783 -24.834 1.034   1.00 31.97 ?  55  LYS   B HE3  1 
ATOM   4768 H  HZ1  . LYS   B 1 55  ? 61.051 -26.579 1.707   1.00 33.73 ?  55  LYS   B HZ1  1 
ATOM   4769 H  HZ2  . LYS   B 1 55  ? 60.469 -26.914 0.423   1.00 33.73 ?  55  LYS   B HZ2  1 
ATOM   4770 H  HZ3  . LYS   B 1 55  ? 61.861 -26.524 0.507   1.00 33.73 ?  55  LYS   B HZ3  1 
ATOM   4771 N  N    . ALA   B 1 56  ? 58.214 -20.641 -2.912  1.00 13.99 ?  56  ALA   B N    1 
ATOM   4772 C  CA   . ALA   B 1 56  ? 58.435 -20.141 -4.262  1.00 14.73 ?  56  ALA   B CA   1 
ATOM   4773 C  C    . ALA   B 1 56  ? 58.713 -18.647 -4.263  1.00 14.34 ?  56  ALA   B C    1 
ATOM   4774 O  O    . ALA   B 1 56  ? 59.446 -18.154 -5.131  1.00 15.67 ?  56  ALA   B O    1 
ATOM   4775 C  CB   . ALA   B 1 56  ? 57.238 -20.474 -5.154  1.00 15.58 ?  56  ALA   B CB   1 
ATOM   4776 H  H    . ALA   B 1 56  ? 57.426 -20.963 -2.772  1.00 16.77 ?  56  ALA   B H    1 
ATOM   4777 H  HA   . ALA   B 1 56  ? 59.212 -20.580 -4.631  1.00 17.66 ?  56  ALA   B HA   1 
ATOM   4778 H  HB1  . ALA   B 1 56  ? 57.411 -20.143 -6.051  1.00 18.68 ?  56  ALA   B HB1  1 
ATOM   4779 H  HB2  . ALA   B 1 56  ? 57.124 -21.438 -5.176  1.00 18.68 ?  56  ALA   B HB2  1 
ATOM   4780 H  HB3  . ALA   B 1 56  ? 56.444 -20.054 -4.793  1.00 18.68 ?  56  ALA   B HB3  1 
ATOM   4781 N  N    . THR   B 1 57  ? 58.145 -17.908 -3.308  1.00 14.09 ?  57  THR   B N    1 
ATOM   4782 C  CA   . THR   B 1 57  ? 58.381 -16.473 -3.192  1.00 14.42 ?  57  THR   B CA   1 
ATOM   4783 C  C    . THR   B 1 57  ? 59.631 -16.141 -2.382  1.00 14.99 ?  57  THR   B C    1 
ATOM   4784 O  O    . THR   B 1 57  ? 59.867 -14.965 -2.082  1.00 15.44 ?  57  THR   B O    1 
ATOM   4785 C  CB   . THR   B 1 57  ? 57.180 -15.743 -2.559  1.00 13.90 ?  57  THR   B CB   1 
ATOM   4786 O  OG1  . THR   B 1 57  ? 57.156 -15.962 -1.143  1.00 14.29 ?  57  THR   B OG1  1 
ATOM   4787 C  CG2  . THR   B 1 57  ? 55.866 -16.161 -3.197  1.00 13.67 ?  57  THR   B CG2  1 
ATOM   4788 H  H    . THR   B 1 57  ? 57.600 -18.218 -2.715  1.00 16.89 ?  57  THR   B H    1 
ATOM   4789 H  HA   . THR   B 1 57  ? 58.499 -16.109 -4.084  1.00 17.29 ?  57  THR   B HA   1 
ATOM   4790 H  HB   . THR   B 1 57  ? 57.284 -14.791 -2.720  1.00 16.66 ?  57  THR   B HB   1 
ATOM   4791 H  HG1  . THR   B 1 57  ? 57.081 -16.784 -0.984  1.00 17.14 ?  57  THR   B HG1  1 
ATOM   4792 H  HG21 . THR   B 1 57  ? 55.141 -15.619 -2.854  1.00 16.39 ?  57  THR   B HG21 1 
ATOM   4793 H  HG22 . THR   B 1 57  ? 55.914 -16.052 -4.161  1.00 16.39 ?  57  THR   B HG22 1 
ATOM   4794 H  HG23 . THR   B 1 57  ? 55.683 -17.093 -3.000  1.00 16.39 ?  57  THR   B HG23 1 
ATOM   4795 N  N    . ASN   B 1 58  ? 60.427 -17.142 -2.017  1.00 16.05 ?  58  ASN   B N    1 
ATOM   4796 C  CA   . ASN   B 1 58  ? 61.624 -16.926 -1.212  1.00 19.36 ?  58  ASN   B CA   1 
ATOM   4797 C  C    . ASN   B 1 58  ? 61.284 -16.217 0.099   1.00 16.82 ?  58  ASN   B C    1 
ATOM   4798 O  O    . ASN   B 1 58  ? 62.021 -15.344 0.566   1.00 17.27 ?  58  ASN   B O    1 
ATOM   4799 C  CB   . ASN   B 1 58  ? 62.706 -16.174 -1.995  1.00 28.45 ?  58  ASN   B CB   1 
ATOM   4800 C  CG   . ASN   B 1 58  ? 64.082 -16.318 -1.374  1.00 38.42 ?  58  ASN   B CG   1 
ATOM   4801 O  OD1  . ASN   B 1 58  ? 64.386 -17.328 -0.738  1.00 41.32 ?  58  ASN   B OD1  1 
ATOM   4802 N  ND2  . ASN   B 1 58  ? 64.923 -15.306 -1.555  1.00 45.14 ?  58  ASN   B ND2  1 
ATOM   4803 H  H    . ASN   B 1 58  ? 60.291 -17.968 -2.224  1.00 19.24 ?  58  ASN   B H    1 
ATOM   4804 H  HA   . ASN   B 1 58  ? 61.991 -17.797 -0.989  1.00 23.22 ?  58  ASN   B HA   1 
ATOM   4805 H  HB2  . ASN   B 1 58  ? 62.747 -16.525 -2.902  1.00 34.13 ?  58  ASN   B HB2  1 
ATOM   4806 H  HB3  . ASN   B 1 58  ? 62.486 -15.231 -2.016  1.00 34.13 ?  58  ASN   B HB3  1 
ATOM   4807 H  HD21 . ASN   B 1 58  ? 65.716 -15.342 -1.223  1.00 54.15 ?  58  ASN   B HD21 1 
ATOM   4808 H  HD22 . ASN   B 1 58  ? 64.676 -14.616 -2.003  1.00 54.15 ?  58  ASN   B HD22 1 
ATOM   4809 N  N    . ASN   B 1 59  ? 60.158 -16.603 0.703   1.00 15.76 ?  59  ASN   B N    1 
ATOM   4810 C  CA   . ASN   B 1 59  ? 59.683 -16.128 2.002   1.00 15.36 ?  59  ASN   B CA   1 
ATOM   4811 C  C    . ASN   B 1 59  ? 59.087 -14.724 1.942   1.00 14.66 ?  59  ASN   B C    1 
ATOM   4812 O  O    . ASN   B 1 59  ? 58.661 -14.217 2.988   1.00 14.76 ?  59  ASN   B O    1 
ATOM   4813 C  CB   . ASN   B 1 59  ? 60.755 -16.178 3.107   1.00 16.07 ?  59  ASN   B CB   1 
ATOM   4814 C  CG   . ASN   B 1 59  ? 60.164 -16.350 4.492   1.00 17.34 ?  59  ASN   B CG   1 
ATOM   4815 O  OD1  . ASN   B 1 59  ? 59.335 -17.236 4.723   1.00 17.72 ?  59  ASN   B OD1  1 
ATOM   4816 N  ND2  . ASN   B 1 59  ? 60.581 -15.501 5.422   1.00 18.27 ?  59  ASN   B ND2  1 
ATOM   4817 H  H    . ASN   B 1 59  ? 59.625 -17.187 0.358   1.00 18.90 ?  59  ASN   B H    1 
ATOM   4818 H  HA   . ASN   B 1 59  ? 58.976 -16.724 2.285   1.00 18.42 ?  59  ASN   B HA   1 
ATOM   4819 H  HB2  . ASN   B 1 59  ? 61.348 -16.927 2.950   1.00 19.26 ?  59  ASN   B HB2  1 
ATOM   4820 H  HB3  . ASN   B 1 59  ? 61.257 -15.349 3.105   1.00 19.26 ?  59  ASN   B HB3  1 
ATOM   4821 H  HD21 . ASN   B 1 59  ? 60.273 -15.555 6.225   1.00 21.91 ?  59  ASN   B HD21 1 
ATOM   4822 H  HD22 . ASN   B 1 59  ? 61.158 -14.895 5.226   1.00 21.91 ?  59  ASN   B HD22 1 
ATOM   4823 N  N    . ALA   B 1 60  ? 59.021 -14.082 0.770   1.00 14.45 ?  60  ALA   B N    1 
ATOM   4824 C  CA   . ALA   B 1 60  ? 58.426 -12.749 0.700   1.00 14.37 ?  60  ALA   B CA   1 
ATOM   4825 C  C    . ALA   B 1 60  ? 56.959 -12.775 1.096   1.00 13.55 ?  60  ALA   B C    1 
ATOM   4826 O  O    . ALA   B 1 60  ? 56.460 -11.819 1.705   1.00 14.16 ?  60  ALA   B O    1 
ATOM   4827 C  CB   . ALA   B 1 60  ? 58.583 -12.165 -0.705  1.00 15.26 ?  60  ALA   B CB   1 
ATOM   4828 H  H    . ALA   B 1 60  ? 59.306 -14.397 0.020   1.00 17.32 ?  60  ALA   B H    1 
ATOM   4829 H  HA   . ALA   B 1 60  ? 58.891 -12.169 1.319   1.00 17.23 ?  60  ALA   B HA   1 
ATOM   4830 H  HB1  . ALA   B 1 60  ? 58.185 -11.283 -0.724  1.00 18.30 ?  60  ALA   B HB1  1 
ATOM   4831 H  HB2  . ALA   B 1 60  ? 59.529 -12.106 -0.920  1.00 18.30 ?  60  ALA   B HB2  1 
ATOM   4832 H  HB3  . ALA   B 1 60  ? 58.137 -12.746 -1.342  1.00 18.30 ?  60  ALA   B HB3  1 
ATOM   4833 N  N    . MET   B 1 61  ? 56.252 -13.855 0.756   1.00 13.04 ?  61  MET   B N    1 
ATOM   4834 C  CA   . MET   B 1 61  ? 54.856 -13.974 1.148   1.00 12.48 ?  61  MET   B CA   1 
ATOM   4835 C  C    . MET   B 1 61  ? 54.717 -13.981 2.668   1.00 12.54 ?  61  MET   B C    1 
ATOM   4836 O  O    . MET   B 1 61  ? 53.814 -13.335 3.217   1.00 12.49 ?  61  MET   B O    1 
ATOM   4837 C  CB   . MET   B 1 61  ? 54.270 -15.240 0.515   1.00 12.58 ?  61  MET   B CB   1 
ATOM   4838 C  CG   . MET   B 1 61  ? 52.836 -15.543 0.937   1.00 12.13 ?  61  MET   B CG   1 
ATOM   4839 S  SD   . MET   B 1 61  ? 52.194 -17.041 0.168   1.00 12.84 ?  61  MET   B SD   1 
ATOM   4840 C  CE   . MET   B 1 61  ? 51.938 -16.448 -1.502  1.00 14.35 ?  61  MET   B CE   1 
ATOM   4841 H  H    . MET   B 1 61  ? 56.560 -14.528 0.303   1.00 15.63 ?  61  MET   B H    1 
ATOM   4842 H  HA   . MET   B 1 61  ? 54.369 -13.219 0.789   1.00 14.96 ?  61  MET   B HA   1 
ATOM   4843 H  HB2  . MET   B 1 61  ? 54.270 -15.136 -0.453  1.00 15.07 ?  61  MET   B HB2  1 
ATOM   4844 H  HB3  . MET   B 1 61  ? 54.815 -15.999 0.760   1.00 15.07 ?  61  MET   B HB3  1 
ATOM   4845 H  HG2  . MET   B 1 61  ? 52.807 -15.671 1.900   1.00 14.54 ?  61  MET   B HG2  1 
ATOM   4846 H  HG3  . MET   B 1 61  ? 52.264 -14.801 0.685   1.00 14.54 ?  61  MET   B HG3  1 
ATOM   4847 H  HE1  . MET   B 1 61  ? 51.543 -17.155 -2.031  1.00 17.21 ?  61  MET   B HE1  1 
ATOM   4848 H  HE2  . MET   B 1 61  ? 51.344 -15.679 -1.478  1.00 17.21 ?  61  MET   B HE2  1 
ATOM   4849 H  HE3  . MET   B 1 61  ? 52.794 -16.189 -1.878  1.00 17.21 ?  61  MET   B HE3  1 
ATOM   4850 N  N    . GLN   B 1 62  ? 55.598 -14.698 3.369   1.00 12.65 ?  62  GLN   B N    1 
ATOM   4851 C  CA   . GLN   B 1 62  ? 55.490 -14.757 4.822   1.00 13.12 ?  62  GLN   B CA   1 
ATOM   4852 C  C    . GLN   B 1 62  ? 55.770 -13.403 5.455   1.00 13.41 ?  62  GLN   B C    1 
ATOM   4853 O  O    . GLN   B 1 62  ? 55.086 -13.002 6.404   1.00 13.75 ?  62  GLN   B O    1 
ATOM   4854 C  CB   . GLN   B 1 62  ? 56.439 -15.811 5.391   1.00 13.54 ?  62  GLN   B CB   1 
ATOM   4855 C  CG   . GLN   B 1 62  ? 56.214 -16.074 6.871   1.00 13.77 ?  62  GLN   B CG   1 
ATOM   4856 C  CD   . GLN   B 1 62  ? 54.836 -16.669 7.115   1.00 13.53 ?  62  GLN   B CD   1 
ATOM   4857 O  OE1  . GLN   B 1 62  ? 54.580 -17.821 6.763   1.00 13.66 ?  62  GLN   B OE1  1 
ATOM   4858 N  NE2  . GLN   B 1 62  ? 53.925 -15.875 7.671   1.00 13.76 ?  62  GLN   B NE2  1 
ATOM   4859 H  H    . GLN   B 1 62  ? 56.252 -15.148 3.032   1.00 15.17 ?  62  GLN   B H    1 
ATOM   4860 H  HA   . GLN   B 1 62  ? 54.584 -15.011 5.055   1.00 15.72 ?  62  GLN   B HA   1 
ATOM   4861 H  HB2  . GLN   B 1 62  ? 56.308 -16.649 4.917   1.00 16.23 ?  62  GLN   B HB2  1 
ATOM   4862 H  HB3  . GLN   B 1 62  ? 57.355 -15.510 5.280   1.00 16.23 ?  62  GLN   B HB3  1 
ATOM   4863 H  HG2  . GLN   B 1 62  ? 56.876 -16.707 7.190   1.00 16.50 ?  62  GLN   B HG2  1 
ATOM   4864 H  HG3  . GLN   B 1 62  ? 56.279 -15.242 7.363   1.00 16.50 ?  62  GLN   B HG3  1 
ATOM   4865 H  HE21 . GLN   B 1 62  ? 54.133 -15.072 7.895   1.00 16.50 ?  62  GLN   B HE21 1 
ATOM   4866 H  HE22 . GLN   B 1 62  ? 53.132 -16.173 7.820   1.00 16.50 ?  62  GLN   B HE22 1 
ATOM   4867 N  N    . VAL   B 1 63  ? 56.783 -12.689 4.961   1.00 13.94 ?  63  VAL   B N    1 
ATOM   4868 C  CA   . VAL   B 1 63  ? 57.089 -11.372 5.513   1.00 14.71 ?  63  VAL   B CA   1 
ATOM   4869 C  C    . VAL   B 1 63  ? 55.898 -10.438 5.331   1.00 13.86 ?  63  VAL   B C    1 
ATOM   4870 O  O    . VAL   B 1 63  ? 55.489 -9.726  6.259   1.00 14.51 ?  63  VAL   B O    1 
ATOM   4871 C  CB   . VAL   B 1 63  ? 58.380 -10.812 4.888   1.00 15.67 ?  63  VAL   B CB   1 
ATOM   4872 C  CG1  . VAL   B 1 63  ? 58.606 -9.373  5.325   1.00 16.58 ?  63  VAL   B CG1  1 
ATOM   4873 C  CG2  . VAL   B 1 63  ? 59.561 -11.678 5.289   1.00 16.33 ?  63  VAL   B CG2  1 
ATOM   4874 H  H    . VAL   B 1 63  ? 57.291 -12.938 4.310   1.00 16.72 ?  63  VAL   B H    1 
ATOM   4875 H  HA   . VAL   B 1 63  ? 57.246 -11.468 6.462   1.00 17.64 ?  63  VAL   B HA   1 
ATOM   4876 H  HB   . VAL   B 1 63  ? 58.312 -10.834 3.920   1.00 18.79 ?  63  VAL   B HB   1 
ATOM   4877 H  HG11 . VAL   B 1 63  ? 59.525 -9.130  5.138   1.00 19.87 ?  63  VAL   B HG11 1 
ATOM   4878 H  HG12 . VAL   B 1 63  ? 58.002 -8.799  4.835   1.00 19.87 ?  63  VAL   B HG12 1 
ATOM   4879 H  HG13 . VAL   B 1 63  ? 58.434 -9.309  6.278   1.00 19.87 ?  63  VAL   B HG13 1 
ATOM   4880 H  HG21 . VAL   B 1 63  ? 60.373 -11.307 4.906   1.00 19.57 ?  63  VAL   B HG21 1 
ATOM   4881 H  HG22 . VAL   B 1 63  ? 59.632 -11.685 6.260   1.00 19.57 ?  63  VAL   B HG22 1 
ATOM   4882 H  HG23 . VAL   B 1 63  ? 59.424 -12.580 4.964   1.00 19.57 ?  63  VAL   B HG23 1 
ATOM   4883 N  N    . GLU   B 1 64  ? 55.330 -10.426 4.125   1.00 13.31 ?  64  GLU   B N    1 
ATOM   4884 C  CA   . GLU   B 1 64  ? 54.167 -9.587  3.853   1.00 13.20 ?  64  GLU   B CA   1 
ATOM   4885 C  C    . GLU   B 1 64  ? 52.984 -9.988  4.726   1.00 12.98 ?  64  GLU   B C    1 
ATOM   4886 O  O    . GLU   B 1 64  ? 52.239 -9.126  5.228   1.00 13.46 ?  64  GLU   B O    1 
ATOM   4887 C  CB   . GLU   B 1 64  ? 53.809 -9.726  2.373   1.00 13.59 ?  64  GLU   B CB   1 
ATOM   4888 C  CG   . GLU   B 1 64  ? 52.537 -9.006  1.948   1.00 13.92 ?  64  GLU   B CG   1 
ATOM   4889 C  CD   . GLU   B 1 64  ? 52.011 -9.498  0.603   1.00 14.49 ?  64  GLU   B CD   1 
ATOM   4890 O  OE1  . GLU   B 1 64  ? 52.192 -10.705 0.286   1.00 15.33 ?  64  GLU   B OE1  1 
ATOM   4891 O  OE2  . GLU   B 1 64  ? 51.394 -8.683  -0.127  1.00 15.14 -1 64  GLU   B OE2  1 
ATOM   4892 H  H    . GLU   B 1 64  ? 55.605 -10.884 3.444   1.00 15.96 ?  64  GLU   B H    1 
ATOM   4893 H  HA   . GLU   B 1 64  ? 54.382 -8.660  4.028   1.00 15.82 ?  64  GLU   B HA   1 
ATOM   4894 H  HB2  . GLU   B 1 64  ? 54.531 -9.356  1.837   1.00 16.29 ?  64  GLU   B HB2  1 
ATOM   4895 H  HB3  . GLU   B 1 64  ? 53.696 -10.663 2.164   1.00 16.29 ?  64  GLU   B HB3  1 
ATOM   4896 H  HG2  . GLU   B 1 64  ? 51.832 -9.157  2.603   1.00 16.68 ?  64  GLU   B HG2  1 
ATOM   4897 H  HG3  . GLU   B 1 64  ? 52.711 -8.057  1.869   1.00 16.68 ?  64  GLU   B HG3  1 
ATOM   4898 N  N    . SER   B 1 65  ? 52.802 -11.296 4.917   1.00 12.58 ?  65  SER   B N    1 
ATOM   4899 C  CA   . SER   B 1 65  ? 51.692 -11.802 5.716   1.00 12.61 ?  65  SER   B CA   1 
ATOM   4900 C  C    . SER   B 1 65  ? 51.822 -11.401 7.180   1.00 12.84 ?  65  SER   B C    1 
ATOM   4901 O  O    . SER   B 1 65  ? 50.823 -11.033 7.814   1.00 13.12 ?  65  SER   B O    1 
ATOM   4902 C  CB   . SER   B 1 65  ? 51.614 -13.323 5.586   1.00 13.02 ?  65  SER   B CB   1 
ATOM   4903 O  OG   . SER   B 1 65  ? 51.259 -13.718 4.272   1.00 13.14 ?  65  SER   B OG   1 
ATOM   4904 H  H    . SER   B 1 65  ? 53.313 -11.914 4.595   1.00 15.08 ?  65  SER   B H    1 
ATOM   4905 H  HA   . SER   B 1 65  ? 50.864 -11.432 5.375   1.00 15.12 ?  65  SER   B HA   1 
ATOM   4906 H  HB2  . SER   B 1 65  ? 52.476 -13.703 5.805   1.00 15.60 ?  65  SER   B HB2  1 
ATOM   4907 H  HB3  . SER   B 1 65  ? 50.940 -13.654 6.204   1.00 15.60 ?  65  SER   B HB3  1 
ATOM   4908 H  HG   . SER   B 1 65  ? 51.831 -13.431 3.719   1.00 15.76 ?  65  SER   B HG   1 
ATOM   4909 N  N    . ASP   B 1 66  ? 53.028 -11.501 7.751   1.00 13.50 ?  66  ASP   B N    1 
ATOM   4910 C  CA   . ASP   B 1 66  ? 53.209 -11.104 9.145   1.00 13.30 ?  66  ASP   B CA   1 
ATOM   4911 C  C    . ASP   B 1 66  ? 52.898 -9.624  9.339   1.00 13.66 ?  66  ASP   B C    1 
ATOM   4912 O  O    . ASP   B 1 66  ? 52.316 -9.232  10.357  1.00 14.25 ?  66  ASP   B O    1 
ATOM   4913 C  CB   . ASP   B 1 66  ? 54.636 -11.412 9.602   1.00 14.57 ?  66  ASP   B CB   1 
ATOM   4914 C  CG   . ASP   B 1 66  ? 54.906 -12.905 9.756   1.00 16.75 ?  66  ASP   B CG   1 
ATOM   4915 O  OD1  . ASP   B 1 66  ? 53.955 -13.722 9.686   1.00 17.44 ?  66  ASP   B OD1  1 
ATOM   4916 O  OD2  . ASP   B 1 66  ? 56.090 -13.263 9.959   1.00 19.30 -1 66  ASP   B OD2  1 
ATOM   4917 H  H    . ASP   B 1 66  ? 53.731 -11.804 7.365   1.00 16.18 ?  66  ASP   B H    1 
ATOM   4918 H  HA   . ASP   B 1 66  ? 52.602 -11.609 9.707   1.00 15.94 ?  66  ASP   B HA   1 
ATOM   4919 H  HB2  . ASP   B 1 66  ? 55.263 -11.065 8.950   1.00 17.47 ?  66  ASP   B HB2  1 
ATOM   4920 H  HB3  . ASP   B 1 66  ? 54.792 -10.990 10.466  1.00 17.47 ?  66  ASP   B HB3  1 
ATOM   4921 N  N    . ASP   B 1 67  ? 53.276 -8.786  8.372   1.00 13.43 ?  67  ASP   B N    1 
ATOM   4922 C  CA   . ASP   B 1 67  ? 52.933 -7.374  8.450   1.00 14.04 ?  67  ASP   B CA   1 
ATOM   4923 C  C    . ASP   B 1 67  ? 51.424 -7.166  8.365   1.00 13.97 ?  67  ASP   B C    1 
ATOM   4924 O  O    . ASP   B 1 67  ? 50.864 -6.355  9.111   1.00 14.47 ?  67  ASP   B O    1 
ATOM   4925 C  CB   . ASP   B 1 67  ? 53.656 -6.610  7.346   1.00 15.38 ?  67  ASP   B CB   1 
ATOM   4926 C  CG   . ASP   B 1 67  ? 53.232 -5.167  7.288   1.00 16.54 ?  67  ASP   B CG   1 
ATOM   4927 O  OD1  . ASP   B 1 67  ? 53.731 -4.348  8.094   1.00 17.99 ?  67  ASP   B OD1  1 
ATOM   4928 O  OD2  . ASP   B 1 67  ? 52.358 -4.872  6.459   1.00 17.48 -1 67  ASP   B OD2  1 
ATOM   4929 H  H    . ASP   B 1 67  ? 53.731 -9.010  7.678   1.00 16.10 ?  67  ASP   B H    1 
ATOM   4930 H  HA   . ASP   B 1 67  ? 53.236 -7.020  9.301   1.00 16.83 ?  67  ASP   B HA   1 
ATOM   4931 H  HB2  . ASP   B 1 67  ? 54.614 -6.644  7.508   1.00 18.44 ?  67  ASP   B HB2  1 
ATOM   4932 H  HB3  . ASP   B 1 67  ? 53.457 -7.029  6.488   1.00 18.44 ?  67  ASP   B HB3  1 
ATOM   4933 N  N    . TYR   B 1 68  ? 50.746 -7.904  7.478   1.00 13.79 ?  68  TYR   B N    1 
ATOM   4934 C  CA   . TYR   B 1 68  ? 49.291 -7.817  7.403   1.00 14.43 ?  68  TYR   B CA   1 
ATOM   4935 C  C    . TYR   B 1 68  ? 48.654 -8.154  8.748   1.00 13.94 ?  68  TYR   B C    1 
ATOM   4936 O  O    . TYR   B 1 68  ? 47.718 -7.477  9.192   1.00 14.84 ?  68  TYR   B O    1 
ATOM   4937 C  CB   . TYR   B 1 68  ? 48.753 -8.744  6.306   1.00 15.15 ?  68  TYR   B CB   1 
ATOM   4938 C  CG   . TYR   B 1 68  ? 47.251 -8.898  6.366   1.00 16.19 ?  68  TYR   B CG   1 
ATOM   4939 C  CD1  . TYR   B 1 68  ? 46.665 -9.854  7.187   1.00 16.83 ?  68  TYR   B CD1  1 
ATOM   4940 C  CD2  . TYR   B 1 68  ? 46.420 -8.067  5.634   1.00 17.22 ?  68  TYR   B CD2  1 
ATOM   4941 C  CE1  . TYR   B 1 68  ? 45.302 -9.980  7.275   1.00 17.93 ?  68  TYR   B CE1  1 
ATOM   4942 C  CE2  . TYR   B 1 68  ? 45.037 -8.196  5.709   1.00 17.41 ?  68  TYR   B CE2  1 
ATOM   4943 C  CZ   . TYR   B 1 68  ? 44.497 -9.151  6.536   1.00 17.82 ?  68  TYR   B CZ   1 
ATOM   4944 O  OH   . TYR   B 1 68  ? 43.131 -9.276  6.628   1.00 18.73 ?  68  TYR   B OH   1 
ATOM   4945 H  H    . TYR   B 1 68  ? 51.104 -8.465  6.924   1.00 16.53 ?  68  TYR   B H    1 
ATOM   4946 H  HA   . TYR   B 1 68  ? 49.047 -6.909  7.179   1.00 17.30 ?  68  TYR   B HA   1 
ATOM   4947 H  HB2  . TYR   B 1 68  ? 48.980 -8.372  5.441   1.00 18.16 ?  68  TYR   B HB2  1 
ATOM   4948 H  HB3  . TYR   B 1 68  ? 49.148 -9.622  6.409   1.00 18.16 ?  68  TYR   B HB3  1 
ATOM   4949 H  HD1  . TYR   B 1 68  ? 47.204 -10.420 7.692   1.00 20.18 ?  68  TYR   B HD1  1 
ATOM   4950 H  HD2  . TYR   B 1 68  ? 46.790 -7.413  5.090   1.00 20.65 ?  68  TYR   B HD2  1 
ATOM   4951 H  HE1  . TYR   B 1 68  ? 44.921 -10.636 7.819   1.00 21.50 ?  68  TYR   B HE1  1 
ATOM   4952 H  HE2  . TYR   B 1 68  ? 44.482 -7.631  5.218   1.00 20.88 ?  68  TYR   B HE2  1 
ATOM   4953 H  HH   . TYR   B 1 68  ? 42.741 -8.722  6.118   1.00 22.46 ?  68  TYR   B HH   1 
ATOM   4954 N  N    . ILE   B 1 69  ? 49.132 -9.220  9.398   1.00 13.67 ?  69  ILE   B N    1 
ATOM   4955 C  CA   . ILE   B 1 69  ? 48.571 -9.644  10.677  1.00 14.26 ?  69  ILE   B CA   1 
ATOM   4956 C  C    . ILE   B 1 69  ? 48.828 -8.599  11.754  1.00 14.13 ?  69  ILE   B C    1 
ATOM   4957 O  O    . ILE   B 1 69  ? 47.956 -8.317  12.582  1.00 14.25 ?  69  ILE   B O    1 
ATOM   4958 C  CB   . ILE   B 1 69  ? 49.142 -11.021 11.067  1.00 15.07 ?  69  ILE   B CB   1 
ATOM   4959 C  CG1  . ILE   B 1 69  ? 48.613 -12.114 10.133  1.00 15.44 ?  69  ILE   B CG1  1 
ATOM   4960 C  CG2  . ILE   B 1 69  ? 48.849 -11.341 12.531  1.00 15.89 ?  69  ILE   B CG2  1 
ATOM   4961 C  CD1  . ILE   B 1 69  ? 47.143 -12.442 10.312  1.00 15.65 ?  69  ILE   B CD1  1 
ATOM   4962 H  H    . ILE   B 1 69  ? 49.782 -9.708  9.124   1.00 16.39 ?  69  ILE   B H    1 
ATOM   4963 H  HA   . ILE   B 1 69  ? 47.610 -9.738  10.580  1.00 17.10 ?  69  ILE   B HA   1 
ATOM   4964 H  HB   . ILE   B 1 69  ? 50.106 -10.981 10.963  1.00 18.07 ?  69  ILE   B HB   1 
ATOM   4965 H  HG12 . ILE   B 1 69  ? 48.741 -11.822 9.215   1.00 18.52 ?  69  ILE   B HG12 1 
ATOM   4966 H  HG13 . ILE   B 1 69  ? 49.121 -12.925 10.289  1.00 18.52 ?  69  ILE   B HG13 1 
ATOM   4967 H  HG21 . ILE   B 1 69  ? 48.986 -12.290 12.676  1.00 19.05 ?  69  ILE   B HG21 1 
ATOM   4968 H  HG22 . ILE   B 1 69  ? 49.451 -10.832 13.097  1.00 19.05 ?  69  ILE   B HG22 1 
ATOM   4969 H  HG23 . ILE   B 1 69  ? 47.928 -11.107 12.727  1.00 19.05 ?  69  ILE   B HG23 1 
ATOM   4970 H  HD11 . ILE   B 1 69  ? 46.898 -13.126 9.671   1.00 18.76 ?  69  ILE   B HD11 1 
ATOM   4971 H  HD12 . ILE   B 1 69  ? 47.001 -12.770 11.214  1.00 18.76 ?  69  ILE   B HD12 1 
ATOM   4972 H  HD13 . ILE   B 1 69  ? 46.618 -11.644 10.161  1.00 18.76 ?  69  ILE   B HD13 1 
ATOM   4973 N  N    . ALA   B 1 70  ? 50.027 -8.017  11.776  1.00 14.30 ?  70  ALA   B N    1 
ATOM   4974 C  CA   . ALA   B 1 70  ? 50.313 -6.978  12.759  1.00 14.13 ?  70  ALA   B CA   1 
ATOM   4975 C  C    . ALA   B 1 70  ? 49.317 -5.831  12.647  1.00 14.23 ?  70  ALA   B C    1 
ATOM   4976 O  O    . ALA   B 1 70  ? 48.880 -5.275  13.660  1.00 14.61 ?  70  ALA   B O    1 
ATOM   4977 C  CB   . ALA   B 1 70  ? 51.743 -6.471  12.579  1.00 14.69 ?  70  ALA   B CB   1 
ATOM   4978 H  H    . ALA   B 1 70  ? 50.669 -8.208  11.247  1.00 17.14 ?  70  ALA   B H    1 
ATOM   4979 H  HA   . ALA   B 1 70  ? 50.240 -7.355  13.650  1.00 16.94 ?  70  ALA   B HA   1 
ATOM   4980 H  HB1  . ALA   B 1 70  ? 51.934 -5.811  13.263  1.00 17.61 ?  70  ALA   B HB1  1 
ATOM   4981 H  HB2  . ALA   B 1 70  ? 52.359 -7.221  12.667  1.00 17.61 ?  70  ALA   B HB2  1 
ATOM   4982 H  HB3  . ALA   B 1 70  ? 51.834 -6.076  11.699  1.00 17.61 ?  70  ALA   B HB3  1 
ATOM   4983 N  N    . THR   B 1 71  ? 48.938 -5.472  11.422  1.00 14.69 ?  71  THR   B N    1 
ATOM   4984 C  CA   . THR   B 1 71  ? 48.043 -4.340  11.207  1.00 15.51 ?  71  THR   B CA   1 
ATOM   4985 C  C    . THR   B 1 71  ? 46.576 -4.709  11.408  1.00 16.46 ?  71  THR   B C    1 
ATOM   4986 O  O    . THR   B 1 71  ? 45.791 -3.891  11.910  1.00 17.87 ?  71  THR   B O    1 
ATOM   4987 C  CB   . THR   B 1 71  ? 48.264 -3.774  9.801   1.00 17.40 ?  71  THR   B CB   1 
ATOM   4988 O  OG1  . THR   B 1 71  ? 49.582 -3.223  9.711   1.00 19.78 ?  71  THR   B OG1  1 
ATOM   4989 C  CG2  . THR   B 1 71  ? 47.241 -2.699  9.468   1.00 18.33 ?  71  THR   B CG2  1 
ATOM   4990 H  H    . THR   B 1 71  ? 49.191 -5.870  10.701  1.00 17.61 ?  71  THR   B H    1 
ATOM   4991 H  HA   . THR   B 1 71  ? 48.265 -3.644  11.842  1.00 18.59 ?  71  THR   B HA   1 
ATOM   4992 H  HB   . THR   B 1 71  ? 48.186 -4.484  9.147   1.00 20.87 ?  71  THR   B HB   1 
ATOM   4993 H  HG1  . THR   B 1 71  ? 49.717 -2.896  8.945   1.00 23.72 ?  71  THR   B HG1  1 
ATOM   4994 H  HG21 . THR   B 1 71  ? 47.547 -2.171  8.711   1.00 21.98 ?  71  THR   B HG21 1 
ATOM   4995 H  HG22 . THR   B 1 71  ? 46.392 -3.105  9.245   1.00 21.98 ?  71  THR   B HG22 1 
ATOM   4996 H  HG23 . THR   B 1 71  ? 47.123 -2.107  10.229  1.00 21.98 ?  71  THR   B HG23 1 
ATOM   4997 N  N    . ASN   B 1 72  ? 46.186 -5.928  11.023  1.00 16.20 ?  72  ASN   B N    1 
ATOM   4998 C  CA   . ASN   B 1 72  ? 44.783 -6.293  10.896  1.00 16.46 ?  72  ASN   B CA   1 
ATOM   4999 C  C    . ASN   B 1 72  ? 44.309 -7.382  11.848  1.00 16.91 ?  72  ASN   B C    1 
ATOM   5000 O  O    . ASN   B 1 72  ? 43.092 -7.532  12.019  1.00 18.46 ?  72  ASN   B O    1 
ATOM   5001 C  CB   . ASN   B 1 72  ? 44.481 -6.729  9.454   1.00 17.10 ?  72  ASN   B CB   1 
ATOM   5002 C  CG   . ASN   B 1 72  ? 44.754 -5.628  8.451   1.00 17.87 ?  72  ASN   B CG   1 
ATOM   5003 O  OD1  . ASN   B 1 72  ? 45.772 -5.634  7.753   1.00 19.28 ?  72  ASN   B OD1  1 
ATOM   5004 N  ND2  . ASN   B 1 72  ? 43.872 -4.654  8.404   1.00 19.52 ?  72  ASN   B ND2  1 
ATOM   5005 H  H    . ASN   B 1 72  ? 46.731 -6.575  10.826  1.00 19.43 ?  72  ASN   B H    1 
ATOM   5006 H  HA   . ASN   B 1 72  ? 44.252 -5.506  11.075  1.00 19.74 ?  72  ASN   B HA   1 
ATOM   5007 H  HB2  . ASN   B 1 72  ? 45.042 -7.491  9.227   1.00 20.51 ?  72  ASN   B HB2  1 
ATOM   5008 H  HB3  . ASN   B 1 72  ? 43.547 -6.972  9.384   1.00 20.51 ?  72  ASN   B HB3  1 
ATOM   5009 H  HD21 . ASN   B 1 72  ? 43.979 -4.002  7.852   1.00 23.41 ?  72  ASN   B HD21 1 
ATOM   5010 H  HD22 . ASN   B 1 72  ? 43.176 -4.679  8.908   1.00 23.41 ?  72  ASN   B HD22 1 
ATOM   5011 N  N    . GLY   B 1 73  ? 45.209 -8.143  12.465  1.00 16.44 ?  73  GLY   B N    1 
ATOM   5012 C  CA   . GLY   B 1 73  ? 44.804 -9.278  13.256  1.00 15.98 ?  73  GLY   B CA   1 
ATOM   5013 C  C    . GLY   B 1 73  ? 44.451 -10.464 12.386  1.00 14.77 ?  73  GLY   B C    1 
ATOM   5014 O  O    . GLY   B 1 73  ? 44.443 -10.382 11.155  1.00 14.61 ?  73  GLY   B O    1 
ATOM   5015 H  H    . GLY   B 1 73  ? 46.061 -8.016  12.441  1.00 19.71 ?  73  GLY   B H    1 
ATOM   5016 H  HA2  . GLY   B 1 73  ? 45.522 -9.530  13.857  1.00 19.16 ?  73  GLY   B HA2  1 
ATOM   5017 H  HA3  . GLY   B 1 73  ? 44.026 -9.042  13.790  1.00 19.16 ?  73  GLY   B HA3  1 
ATOM   5018 N  N    . PRO   B 1 74  ? 44.150 -11.591 13.025  1.00 14.91 ?  74  PRO   B N    1 
ATOM   5019 C  CA   . PRO   B 1 74  ? 43.899 -12.823 12.279  1.00 14.54 ?  74  PRO   B CA   1 
ATOM   5020 C  C    . PRO   B 1 74  ? 42.601 -12.765 11.490  1.00 14.08 ?  74  PRO   B C    1 
ATOM   5021 O  O    . PRO   B 1 74  ? 41.661 -12.027 11.815  1.00 15.01 ?  74  PRO   B O    1 
ATOM   5022 C  CB   . PRO   B 1 74  ? 43.824 -13.887 13.380  1.00 15.68 ?  74  PRO   B CB   1 
ATOM   5023 C  CG   . PRO   B 1 74  ? 43.384 -13.137 14.591  1.00 16.93 ?  74  PRO   B CG   1 
ATOM   5024 C  CD   . PRO   B 1 74  ? 44.049 -11.796 14.479  1.00 16.36 ?  74  PRO   B CD   1 
ATOM   5025 H  HA   . PRO   B 1 74  ? 44.641 -13.019 11.680  1.00 17.43 ?  74  PRO   B HA   1 
ATOM   5026 H  HB2  . PRO   B 1 74  ? 43.175 -14.565 13.134  1.00 18.81 ?  74  PRO   B HB2  1 
ATOM   5027 H  HB3  . PRO   B 1 74  ? 44.700 -14.281 13.515  1.00 18.81 ?  74  PRO   B HB3  1 
ATOM   5028 H  HG2  . PRO   B 1 74  ? 42.418 -13.042 14.581  1.00 20.30 ?  74  PRO   B HG2  1 
ATOM   5029 H  HG3  . PRO   B 1 74  ? 43.677 -13.602 15.388  1.00 20.30 ?  74  PRO   B HG3  1 
ATOM   5030 H  HD2  . PRO   B 1 74  ? 43.493 -11.109 14.885  1.00 19.62 ?  74  PRO   B HD2  1 
ATOM   5031 H  HD3  . PRO   B 1 74  ? 44.931 -11.821 14.882  1.00 19.62 ?  74  PRO   B HD3  1 
ATOM   5032 N  N    . LEU   B 1 75  ? 42.569 -13.569 10.435  1.00 13.49 ?  75  LEU   B N    1 
ATOM   5033 C  CA   . LEU   B 1 75  ? 41.355 -13.784 9.670   1.00 13.58 ?  75  LEU   B CA   1 
ATOM   5034 C  C    . LEU   B 1 75  ? 40.380 -14.641 10.472  1.00 13.91 ?  75  LEU   B C    1 
ATOM   5035 O  O    . LEU   B 1 75  ? 40.722 -15.222 11.503  1.00 15.01 ?  75  LEU   B O    1 
ATOM   5036 C  CB   . LEU   B 1 75  ? 41.676 -14.502 8.360   1.00 13.71 ?  75  LEU   B CB   1 
ATOM   5037 C  CG   . LEU   B 1 75  ? 42.518 -13.750 7.322   1.00 15.27 ?  75  LEU   B CG   1 
ATOM   5038 C  CD1  . LEU   B 1 75  ? 42.704 -14.591 6.059   1.00 16.58 ?  75  LEU   B CD1  1 
ATOM   5039 C  CD2  . LEU   B 1 75  ? 41.914 -12.413 6.987   1.00 18.44 ?  75  LEU   B CD2  1 
ATOM   5040 H  H    . LEU   B 1 75  ? 43.244 -14.012 10.141  1.00 16.17 ?  75  LEU   B H    1 
ATOM   5041 H  HA   . LEU   B 1 75  ? 40.932 -12.936 9.474   1.00 16.28 ?  75  LEU   B HA   1 
ATOM   5042 H  HB2  . LEU   B 1 75  ? 42.154 -15.319 8.574   1.00 16.43 ?  75  LEU   B HB2  1 
ATOM   5043 H  HB3  . LEU   B 1 75  ? 40.837 -14.732 7.930   1.00 16.43 ?  75  LEU   B HB3  1 
ATOM   5044 H  HG   . LEU   B 1 75  ? 43.397 -13.592 7.697   1.00 18.31 ?  75  LEU   B HG   1 
ATOM   5045 H  HD11 . LEU   B 1 75  ? 43.245 -14.091 5.423   1.00 19.88 ?  75  LEU   B HD11 1 
ATOM   5046 H  HD12 . LEU   B 1 75  ? 43.158 -15.419 6.291   1.00 19.88 ?  75  LEU   B HD12 1 
ATOM   5047 H  HD13 . LEU   B 1 75  ? 41.838 -14.785 5.672   1.00 19.88 ?  75  LEU   B HD13 1 
ATOM   5048 H  HD21 . LEU   B 1 75  ? 42.413 -12.016 6.257   1.00 22.11 ?  75  LEU   B HD21 1 
ATOM   5049 H  HD22 . LEU   B 1 75  ? 40.990 -12.540 6.728   1.00 22.11 ?  75  LEU   B HD22 1 
ATOM   5050 H  HD23 . LEU   B 1 75  ? 41.964 -11.840 7.770   1.00 22.11 ?  75  LEU   B HD23 1 
ATOM   5051 N  N    . LYS   B 1 76  ? 39.147 -14.719 9.976   1.00 15.27 ?  76  LYS   B N    1 
ATOM   5052 C  CA   . LYS   B 1 76  ? 38.165 -15.682 10.454  1.00 16.72 ?  76  LYS   B CA   1 
ATOM   5053 C  C    . LYS   B 1 76  ? 38.260 -16.957 9.619   1.00 15.66 ?  76  LYS   B C    1 
ATOM   5054 O  O    . LYS   B 1 76  ? 38.541 -16.907 8.422   1.00 15.22 ?  76  LYS   B O    1 
ATOM   5055 C  CB   . LYS   B 1 76  ? 36.747 -15.119 10.278  1.00 18.36 ?  76  LYS   B CB   1 
ATOM   5056 C  CG   . LYS   B 1 76  ? 36.459 -13.753 10.921  1.00 20.15 ?  76  LYS   B CG   1 
ATOM   5057 C  CD   . LYS   B 1 76  ? 35.057 -13.234 10.544  1.00 21.43 ?  76  LYS   B CD   1 
ATOM   5058 C  CE   . LYS   B 1 76  ? 34.759 -11.883 11.183  1.00 23.29 ?  76  LYS   B CE   1 
ATOM   5059 N  NZ   . LYS   B 1 76  ? 33.508 -11.256 10.666  1.00 24.06 ?  76  LYS   B NZ   1 
ATOM   5060 H  H    . LYS   B 1 76  ? 38.854 -14.220 9.343   1.00 18.31 ?  76  LYS   B H    1 
ATOM   5061 H  HA   . LYS   B 1 76  ? 38.319 -15.899 11.387  1.00 20.05 ?  76  LYS   B HA   1 
ATOM   5062 H  HB2  . LYS   B 1 76  ? 36.574 -15.030 9.328   1.00 22.01 ?  76  LYS   B HB2  1 
ATOM   5063 H  HB3  . LYS   B 1 76  ? 36.120 -15.752 10.660  1.00 22.01 ?  76  LYS   B HB3  1 
ATOM   5064 H  HG2  . LYS   B 1 76  ? 36.505 -13.838 11.886  1.00 24.16 ?  76  LYS   B HG2  1 
ATOM   5065 H  HG3  . LYS   B 1 76  ? 37.117 -13.109 10.610  1.00 24.16 ?  76  LYS   B HG3  1 
ATOM   5066 H  HD2  . LYS   B 1 76  ? 35.003 -13.133 9.580   1.00 25.70 ?  76  LYS   B HD2  1 
ATOM   5067 H  HD3  . LYS   B 1 76  ? 34.390 -13.869 10.850  1.00 25.70 ?  76  LYS   B HD3  1 
ATOM   5068 H  HE2  . LYS   B 1 76  ? 34.659 -12.004 12.140  1.00 27.94 ?  76  LYS   B HE2  1 
ATOM   5069 H  HE3  . LYS   B 1 76  ? 35.494 -11.279 10.998  1.00 27.94 ?  76  LYS   B HE3  1 
ATOM   5070 H  HZ1  . LYS   B 1 76  ? 33.371 -10.471 11.065  1.00 28.86 ?  76  LYS   B HZ1  1 
ATOM   5071 H  HZ2  . LYS   B 1 76  ? 33.570 -11.125 9.787   1.00 28.86 ?  76  LYS   B HZ2  1 
ATOM   5072 H  HZ3  . LYS   B 1 76  ? 32.809 -11.785 10.828  1.00 28.86 ?  76  LYS   B HZ3  1 
ATOM   5073 N  N    . VAL   B 1 77  ? 38.011 -18.108 10.252  1.00 16.30 ?  77  VAL   B N    1 
ATOM   5074 C  CA   . VAL   B 1 77  ? 37.810 -19.324 9.473   1.00 16.29 ?  77  VAL   B CA   1 
ATOM   5075 C  C    . VAL   B 1 77  ? 36.616 -19.098 8.557   1.00 15.25 ?  77  VAL   B C    1 
ATOM   5076 O  O    . VAL   B 1 77  ? 35.549 -18.661 9.003   1.00 15.31 ?  77  VAL   B O    1 
ATOM   5077 C  CB   . VAL   B 1 77  ? 37.608 -20.536 10.394  1.00 17.89 ?  77  VAL   B CB   1 
ATOM   5078 C  CG1  . VAL   B 1 77  ? 37.307 -21.779 9.564   1.00 18.36 ?  77  VAL   B CG1  1 
ATOM   5079 C  CG2  . VAL   B 1 77  ? 38.842 -20.755 11.270  1.00 19.42 ?  77  VAL   B CG2  1 
ATOM   5080 H  H    . VAL   B 1 77  ? 37.949 -18.208 11.098  1.00 19.55 ?  77  VAL   B H    1 
ATOM   5081 H  HA   . VAL   B 1 77  ? 38.581 -19.487 8.916   1.00 19.53 ?  77  VAL   B HA   1 
ATOM   5082 H  HB   . VAL   B 1 77  ? 36.844 -20.373 10.973  1.00 21.46 ?  77  VAL   B HB   1 
ATOM   5083 H  HG11 . VAL   B 1 77  ? 37.356 -22.558 10.140  1.00 22.01 ?  77  VAL   B HG11 1 
ATOM   5084 H  HG12 . VAL   B 1 77  ? 36.413 -21.707 9.189   1.00 22.01 ?  77  VAL   B HG12 1 
ATOM   5085 H  HG13 . VAL   B 1 77  ? 37.960 -21.850 8.854   1.00 22.01 ?  77  VAL   B HG13 1 
ATOM   5086 H  HG21 . VAL   B 1 77  ? 38.705 -21.548 11.808  1.00 23.29 ?  77  VAL   B HG21 1 
ATOM   5087 H  HG22 . VAL   B 1 77  ? 39.613 -20.866 10.697  1.00 23.29 ?  77  VAL   B HG22 1 
ATOM   5088 H  HG23 . VAL   B 1 77  ? 38.957 -19.980 11.841  1.00 23.29 ?  77  VAL   B HG23 1 
ATOM   5089 N  N    . GLY   B 1 78  ? 36.798 -19.374 7.268   1.00 14.50 ?  78  GLY   B N    1 
ATOM   5090 C  CA   . GLY   B 1 78  ? 35.823 -19.059 6.250   1.00 14.08 ?  78  GLY   B CA   1 
ATOM   5091 C  C    . GLY   B 1 78  ? 36.063 -17.742 5.549   1.00 13.66 ?  78  GLY   B C    1 
ATOM   5092 O  O    . GLY   B 1 78  ? 35.374 -17.453 4.565   1.00 14.09 ?  78  GLY   B O    1 
ATOM   5093 H  H    . GLY   B 1 78  ? 37.500 -19.759 6.952   1.00 17.38 ?  78  GLY   B H    1 
ATOM   5094 H  HA2  . GLY   B 1 78  ? 35.824 -19.753 5.577   1.00 16.88 ?  78  GLY   B HA2  1 
ATOM   5095 H  HA3  . GLY   B 1 78  ? 34.941 -19.025 6.651   1.00 16.88 ?  78  GLY   B HA3  1 
ATOM   5096 N  N    . GLY   B 1 79  ? 37.017 -16.938 6.029   1.00 13.54 ?  79  GLY   B N    1 
ATOM   5097 C  CA   . GLY   B 1 79  ? 37.308 -15.641 5.455   1.00 13.22 ?  79  GLY   B CA   1 
ATOM   5098 C  C    . GLY   B 1 79  ? 38.546 -15.658 4.568   1.00 12.70 ?  79  GLY   B C    1 
ATOM   5099 O  O    . GLY   B 1 79  ? 39.167 -16.694 4.331   1.00 13.28 ?  79  GLY   B O    1 
ATOM   5100 H  H    . GLY   B 1 79  ? 37.525 -17.133 6.695   1.00 16.24 ?  79  GLY   B H    1 
ATOM   5101 H  HA2  . GLY   B 1 79  ? 36.555 -15.344 4.919   1.00 15.85 ?  79  GLY   B HA2  1 
ATOM   5102 H  HA3  . GLY   B 1 79  ? 37.452 -14.996 6.164   1.00 15.85 ?  79  GLY   B HA3  1 
ATOM   5103 N  N    . SER   B 1 80  ? 38.910 -14.464 4.092   1.00 12.72 ?  80  SER   B N    1 
ATOM   5104 C  CA   . SER   B 1 80  ? 40.021 -14.336 3.157   1.00 12.39 ?  80  SER   B CA   1 
ATOM   5105 C  C    . SER   B 1 80  ? 40.601 -12.929 3.211   1.00 12.08 ?  80  SER   B C    1 
ATOM   5106 O  O    . SER   B 1 80  ? 39.984 -11.993 3.725   1.00 13.53 ?  80  SER   B O    1 
ATOM   5107 C  CB   . SER   B 1 80  ? 39.580 -14.631 1.721   1.00 12.84 ?  80  SER   B CB   1 
ATOM   5108 O  OG   . SER   B 1 80  ? 38.737 -13.606 1.224   1.00 13.79 ?  80  SER   B OG   1 
ATOM   5109 H  H    . SER   B 1 80  ? 38.541 -13.720 4.301   1.00 15.25 ?  80  SER   B H    1 
ATOM   5110 H  HA   . SER   B 1 80  ? 40.716 -14.964 3.407   1.00 14.85 ?  80  SER   B HA   1 
ATOM   5111 H  HB2  . SER   B 1 80  ? 40.365 -14.692 1.154   1.00 15.39 ?  80  SER   B HB2  1 
ATOM   5112 H  HB3  . SER   B 1 80  ? 39.097 -15.473 1.708   1.00 15.39 ?  80  SER   B HB3  1 
ATOM   5113 H  HG   . SER   B 1 80  ? 38.048 -13.544 1.710   1.00 16.53 ?  80  SER   B HG   1 
ATOM   5114 N  N    . CYS   B 1 81  ? 41.788 -12.789 2.623   1.00 11.88 ?  81  CYS   B N    1 
ATOM   5115 C  CA   . CYS   B 1 81  ? 42.338 -11.476 2.316   1.00 12.02 ?  81  CYS   B CA   1 
ATOM   5116 C  C    . CYS   B 1 81  ? 43.107 -11.560 1.006   1.00 11.22 ?  81  CYS   B C    1 
ATOM   5117 O  O    . CYS   B 1 81  ? 43.610 -12.624 0.630   1.00 12.37 ?  81  CYS   B O    1 
ATOM   5118 C  CB   . CYS   B 1 81  ? 43.232 -10.927 3.440   1.00 12.92 ?  81  CYS   B CB   1 
ATOM   5119 S  SG   . CYS   B 1 81  ? 44.747 -11.858 3.681   1.00 12.99 ?  81  CYS   B SG   1 
ATOM   5120 H  H    . CYS   B 1 81  ? 42.296 -13.444 2.386   1.00 14.24 ?  81  CYS   B H    1 
ATOM   5121 H  HA   . CYS   B 1 81  ? 41.606 -10.851 2.190   1.00 14.40 ?  81  CYS   B HA   1 
ATOM   5122 H  HB2  . CYS   B 1 81  ? 43.477 -10.012 3.232   1.00 15.49 ?  81  CYS   B HB2  1 
ATOM   5123 H  HB3  . CYS   B 1 81  ? 42.731 -10.946 4.276   1.00 15.49 ?  81  CYS   B HB3  1 
ATOM   5124 H  HG   . CYS   B 1 81  ? 45.370 -11.360 4.583   1.00 15.57 ?  81  CYS   B HG   1 
ATOM   5125 N  N    . VAL   B 1 82  ? 43.211 -10.417 0.327   1.00 11.75 ?  82  VAL   B N    1 
ATOM   5126 C  CA   . VAL   B 1 82  ? 43.977 -10.295 -0.910  1.00 11.82 ?  82  VAL   B CA   1 
ATOM   5127 C  C    . VAL   B 1 82  ? 45.319 -9.656  -0.588  1.00 12.09 ?  82  VAL   B C    1 
ATOM   5128 O  O    . VAL   B 1 82  ? 45.371 -8.537  -0.061  1.00 13.22 ?  82  VAL   B O    1 
ATOM   5129 C  CB   . VAL   B 1 82  ? 43.232 -9.454  -1.958  1.00 13.08 ?  82  VAL   B CB   1 
ATOM   5130 C  CG1  . VAL   B 1 82  ? 44.081 -9.296  -3.212  1.00 14.54 ?  82  VAL   B CG1  1 
ATOM   5131 C  CG2  . VAL   B 1 82  ? 41.877 -10.055 -2.281  1.00 14.17 ?  82  VAL   B CG2  1 
ATOM   5132 H  H    . VAL   B 1 82  ? 42.830 -9.682  0.568   1.00 14.09 ?  82  VAL   B H    1 
ATOM   5133 H  HA   . VAL   B 1 82  ? 44.135 -11.175 -1.280  1.00 14.17 ?  82  VAL   B HA   1 
ATOM   5134 H  HB   . VAL   B 1 82  ? 43.079 -8.570  -1.596  1.00 15.68 ?  82  VAL   B HB   1 
ATOM   5135 H  HG11 . VAL   B 1 82  ? 43.520 -8.979  -3.938  1.00 17.43 ?  82  VAL   B HG11 1 
ATOM   5136 H  HG12 . VAL   B 1 82  ? 44.788 -8.649  -3.040  1.00 17.43 ?  82  VAL   B HG12 1 
ATOM   5137 H  HG13 . VAL   B 1 82  ? 44.469 -10.153 -3.446  1.00 17.43 ?  82  VAL   B HG13 1 
ATOM   5138 H  HG21 . VAL   B 1 82  ? 41.445 -9.520  -2.969  1.00 16.99 ?  82  VAL   B HG21 1 
ATOM   5139 H  HG22 . VAL   B 1 82  ? 41.997 -10.964 -2.602  1.00 16.99 ?  82  VAL   B HG22 1 
ATOM   5140 H  HG23 . VAL   B 1 82  ? 41.330 -10.060 -1.479  1.00 16.99 ?  82  VAL   B HG23 1 
ATOM   5141 N  N    . LEU   B 1 83  ? 46.398 -10.347 -0.945  1.00 11.84 ?  83  LEU   B N    1 
ATOM   5142 C  CA   . LEU   B 1 83  ? 47.752 -9.825  -0.833  1.00 11.81 ?  83  LEU   B CA   1 
ATOM   5143 C  C    . LEU   B 1 83  ? 48.445 -9.974  -2.185  1.00 11.61 ?  83  LEU   B C    1 
ATOM   5144 O  O    . LEU   B 1 83  ? 47.841 -10.393 -3.176  1.00 11.78 ?  83  LEU   B O    1 
ATOM   5145 C  CB   . LEU   B 1 83  ? 48.514 -10.504 0.313   1.00 12.42 ?  83  LEU   B CB   1 
ATOM   5146 C  CG   . LEU   B 1 83  ? 48.009 -10.147 1.715   1.00 13.51 ?  83  LEU   B CG   1 
ATOM   5147 C  CD1  . LEU   B 1 83  ? 48.632 -11.018 2.784   1.00 13.96 ?  83  LEU   B CD1  1 
ATOM   5148 C  CD2  . LEU   B 1 83  ? 48.209 -8.657  2.040   1.00 14.34 ?  83  LEU   B CD2  1 
ATOM   5149 H  H    . LEU   B 1 83  ? 46.362 -11.146 -1.268  1.00 14.19 ?  83  LEU   B H    1 
ATOM   5150 H  HA   . LEU   B 1 83  ? 47.700 -8.881  -0.639  1.00 14.16 ?  83  LEU   B HA   1 
ATOM   5151 H  HB2  . LEU   B 1 83  ? 48.443 -11.464 0.206   1.00 14.89 ?  83  LEU   B HB2  1 
ATOM   5152 H  HB3  . LEU   B 1 83  ? 49.446 -10.238 0.256   1.00 14.89 ?  83  LEU   B HB3  1 
ATOM   5153 H  HG   . LEU   B 1 83  ? 47.055 -10.311 1.731   1.00 16.19 ?  83  LEU   B HG   1 
ATOM   5154 H  HD11 . LEU   B 1 83  ? 48.272 -10.760 3.649   1.00 16.73 ?  83  LEU   B HD11 1 
ATOM   5155 H  HD12 . LEU   B 1 83  ? 48.407 -11.948 2.602   1.00 16.73 ?  83  LEU   B HD12 1 
ATOM   5156 H  HD13 . LEU   B 1 83  ? 49.591 -10.902 2.774   1.00 16.73 ?  83  LEU   B HD13 1 
ATOM   5157 H  HD21 . LEU   B 1 83  ? 48.002 -8.509  2.975   1.00 17.19 ?  83  LEU   B HD21 1 
ATOM   5158 H  HD22 . LEU   B 1 83  ? 49.129 -8.414  1.859   1.00 17.19 ?  83  LEU   B HD22 1 
ATOM   5159 H  HD23 . LEU   B 1 83  ? 47.612 -8.128  1.483   1.00 17.19 ?  83  LEU   B HD23 1 
ATOM   5160 N  N    . SER   B 1 84  ? 49.721 -9.603  -2.238  1.00 12.52 ?  84  SER   B N    1 
ATOM   5161 C  CA   . SER   B 1 84  ? 50.459 -9.722  -3.485  1.00 12.83 ?  84  SER   B CA   1 
ATOM   5162 C  C    . SER   B 1 84  ? 50.622 -11.181 -3.888  1.00 12.14 ?  84  SER   B C    1 
ATOM   5163 O  O    . SER   B 1 84  ? 50.736 -12.074 -3.047  1.00 12.10 ?  84  SER   B O    1 
ATOM   5164 C  CB   . SER   B 1 84  ? 51.850 -9.114  -3.333  1.00 14.57 ?  84  SER   B CB   1 
ATOM   5165 O  OG   . SER   B 1 84  ? 52.597 -9.326  -4.515  1.00 16.21 ?  84  SER   B OG   1 
ATOM   5166 H  H    . SER   B 1 84  ? 50.167 -9.269  -1.583  1.00 15.01 ?  84  SER   B H    1 
ATOM   5167 H  HA   . SER   B 1 84  ? 49.989 -9.252  -4.193  1.00 15.38 ?  84  SER   B HA   1 
ATOM   5168 H  HB2  . SER   B 1 84  ? 51.765 -8.156  -3.171  1.00 17.47 ?  84  SER   B HB2  1 
ATOM   5169 H  HB3  . SER   B 1 84  ? 52.305 -9.535  -2.587  1.00 17.47 ?  84  SER   B HB3  1 
ATOM   5170 H  HG   . SER   B 1 84  ? 53.365 -8.982  -4.434  1.00 19.44 ?  84  SER   B HG   1 
ATOM   5171 N  N    . GLY   B 1 85  ? 50.688 -11.410 -5.193  1.00 13.32 ?  85  GLY   B N    1 
ATOM   5172 C  CA   . GLY   B 1 85  ? 51.036 -12.703 -5.726  1.00 14.08 ?  85  GLY   B CA   1 
ATOM   5173 C  C    . GLY   B 1 85  ? 52.508 -12.899 -6.026  1.00 13.22 ?  85  GLY   B C    1 
ATOM   5174 O  O    . GLY   B 1 85  ? 52.887 -13.981 -6.478  1.00 13.52 ?  85  GLY   B O    1 
ATOM   5175 H  H    . GLY   B 1 85  ? 50.535 -10.822 -5.797  1.00 15.97 ?  85  GLY   B H    1 
ATOM   5176 H  HA2  . GLY   B 1 85  ? 50.769 -13.391 -5.091  1.00 16.88 ?  85  GLY   B HA2  1 
ATOM   5177 H  HA3  . GLY   B 1 85  ? 50.549 -12.853 -6.547  1.00 16.88 ?  85  GLY   B HA3  1 
ATOM   5178 N  N    . HIS   B 1 86  ? 53.360 -11.899 -5.811  1.00 13.40 ?  86  HIS   B N    1 
ATOM   5179 C  CA   . HIS   B 1 86  ? 54.822 -12.067 -5.893  1.00 13.38 ?  86  HIS   B CA   1 
ATOM   5180 C  C    . HIS   B 1 86  ? 55.198 -12.579 -7.282  1.00 13.34 ?  86  HIS   B C    1 
ATOM   5181 O  O    . HIS   B 1 86  ? 54.803 -11.968 -8.287  1.00 14.09 ?  86  HIS   B O    1 
ATOM   5182 C  CB   . HIS   B 1 86  ? 55.311 -12.905 -4.713  1.00 13.60 ?  86  HIS   B CB   1 
ATOM   5183 C  CG   . HIS   B 1 86  ? 54.994 -12.296 -3.388  1.00 13.79 ?  86  HIS   B CG   1 
ATOM   5184 N  ND1  . HIS   B 1 86  ? 55.826 -11.390 -2.767  1.00 15.55 ?  86  HIS   B ND1  1 
ATOM   5185 C  CD2  . HIS   B 1 86  ? 53.914 -12.434 -2.583  1.00 14.35 ?  86  HIS   B CD2  1 
ATOM   5186 C  CE1  . HIS   B 1 86  ? 55.270 -10.997 -1.635  1.00 15.41 ?  86  HIS   B CE1  1 
ATOM   5187 N  NE2  . HIS   B 1 86  ? 54.106 -11.609 -1.503  1.00 14.56 ?  86  HIS   B NE2  1 
ATOM   5188 H  H    . HIS   B 1 86  ? 53.120 -11.100 -5.611  1.00 16.07 ?  86  HIS   B H    1 
ATOM   5189 H  HA   . HIS   B 1 86  ? 55.229 -11.194 -5.798  1.00 16.04 ?  86  HIS   B HA   1 
ATOM   5190 H  HB2  . HIS   B 1 86  ? 54.899 -13.779 -4.748  1.00 16.31 ?  86  HIS   B HB2  1 
ATOM   5191 H  HB3  . HIS   B 1 86  ? 56.279 -12.994 -4.768  1.00 16.31 ?  86  HIS   B HB3  1 
ATOM   5192 H  HD2  . HIS   B 1 86  ? 53.166 -12.972 -2.742  1.00 17.21 ?  86  HIS   B HD2  1 
ATOM   5193 H  HE1  . HIS   B 1 86  ? 55.635 -10.400 -1.024  1.00 18.48 ?  86  HIS   B HE1  1 
ATOM   5194 H  HE2  . HIS   B 1 86  ? 53.563 -11.526 -0.836  1.00 17.46 ?  86  HIS   B HE2  1 
ATOM   5195 N  N    . ASN   B 1 87  ? 55.970 -13.659 -7.390  1.00 13.77 ?  87  ASN   B N    1 
ATOM   5196 C  CA   . ASN   B 1 87  ? 56.359 -14.234 -8.668  1.00 14.69 ?  87  ASN   B CA   1 
ATOM   5197 C  C    . ASN   B 1 87  ? 55.375 -15.278 -9.172  1.00 14.22 ?  87  ASN   B C    1 
ATOM   5198 O  O    . ASN   B 1 87  ? 55.695 -15.992 -10.130 1.00 16.18 ?  87  ASN   B O    1 
ATOM   5199 C  CB   . ASN   B 1 87  ? 57.750 -14.870 -8.553  1.00 16.28 ?  87  ASN   B CB   1 
ATOM   5200 C  CG   . ASN   B 1 87  ? 57.804 -15.979 -7.508  1.00 17.11 ?  87  ASN   B CG   1 
ATOM   5201 O  OD1  . ASN   B 1 87  ? 57.161 -15.898 -6.456  1.00 16.42 ?  87  ASN   B OD1  1 
ATOM   5202 N  ND2  . ASN   B 1 87  ? 58.559 -17.039 -7.810  1.00 19.25 ?  87  ASN   B ND2  1 
ATOM   5203 H  H    . ASN   B 1 87  ? 56.279 -14.093 -6.715  1.00 16.51 ?  87  ASN   B H    1 
ATOM   5204 H  HA   . ASN   B 1 87  ? 56.404 -13.530 -9.328  1.00 17.61 ?  87  ASN   B HA   1 
ATOM   5205 H  HB2  . ASN   B 1 87  ? 57.995 -15.253 -9.414  1.00 19.52 ?  87  ASN   B HB2  1 
ATOM   5206 H  HB3  . ASN   B 1 87  ? 58.389 -14.187 -8.303  1.00 19.52 ?  87  ASN   B HB3  1 
ATOM   5207 H  HD21 . ASN   B 1 87  ? 58.627 -17.690 -7.255  1.00 23.09 ?  87  ASN   B HD21 1 
ATOM   5208 H  HD22 . ASN   B 1 87  ? 58.989 -17.066 -8.558  1.00 23.09 ?  87  ASN   B HD22 1 
ATOM   5209 N  N    . LEU   B 1 88  ? 54.197 -15.381 -8.552  1.00 13.52 ?  88  LEU   B N    1 
ATOM   5210 C  CA   . LEU   B 1 88  ? 53.216 -16.412 -8.875  1.00 13.58 ?  88  LEU   B CA   1 
ATOM   5211 C  C    . LEU   B 1 88  ? 51.985 -15.893 -9.595  1.00 13.42 ?  88  LEU   B C    1 
ATOM   5212 O  O    . LEU   B 1 88  ? 51.382 -16.634 -10.379 1.00 15.23 ?  88  LEU   B O    1 
ATOM   5213 C  CB   . LEU   B 1 88  ? 52.745 -17.092 -7.586  1.00 14.51 ?  88  LEU   B CB   1 
ATOM   5214 C  CG   . LEU   B 1 88  ? 53.863 -17.758 -6.796  1.00 16.92 ?  88  LEU   B CG   1 
ATOM   5215 C  CD1  . LEU   B 1 88  ? 53.376 -18.158 -5.416  1.00 18.48 ?  88  LEU   B CD1  1 
ATOM   5216 C  CD2  . LEU   B 1 88  ? 54.383 -18.958 -7.563  1.00 19.71 ?  88  LEU   B CD2  1 
ATOM   5217 H  H    . LEU   B 1 88  ? 53.939 -14.857 -7.914  1.00 16.21 ?  88  LEU   B H    1 
ATOM   5218 H  HA   . LEU   B 1 88  ? 53.629 -17.081 -9.433  1.00 16.28 ?  88  LEU   B HA   1 
ATOM   5219 H  HB2  . LEU   B 1 88  ? 52.329 -16.431 -7.010  1.00 17.39 ?  88  LEU   B HB2  1 
ATOM   5220 H  HB3  . LEU   B 1 88  ? 52.095 -17.780 -7.814  1.00 17.39 ?  88  LEU   B HB3  1 
ATOM   5221 H  HG   . LEU   B 1 88  ? 54.592 -17.129 -6.687  1.00 20.29 ?  88  LEU   B HG   1 
ATOM   5222 H  HD11 . LEU   B 1 88  ? 54.039 -18.730 -5.000  1.00 22.16 ?  88  LEU   B HD11 1 
ATOM   5223 H  HD12 . LEU   B 1 88  ? 53.244 -17.359 -4.883  1.00 22.16 ?  88  LEU   B HD12 1 
ATOM   5224 H  HD13 . LEU   B 1 88  ? 52.537 -18.637 -5.507  1.00 22.16 ?  88  LEU   B HD13 1 
ATOM   5225 H  HD21 . LEU   B 1 88  ? 55.002 -19.446 -6.999  1.00 23.64 ?  88  LEU   B HD21 1 
ATOM   5226 H  HD22 . LEU   B 1 88  ? 53.636 -19.526 -7.805  1.00 23.64 ?  88  LEU   B HD22 1 
ATOM   5227 H  HD23 . LEU   B 1 88  ? 54.837 -18.650 -8.363  1.00 23.64 ?  88  LEU   B HD23 1 
ATOM   5228 N  N    . ALA   B 1 89  ? 51.582 -14.659 -9.325  1.00 12.55 ?  89  ALA   B N    1 
ATOM   5229 C  CA   . ALA   B 1 89  ? 50.292 -14.161 -9.777  1.00 12.04 ?  89  ALA   B CA   1 
ATOM   5230 C  C    . ALA   B 1 89  ? 50.267 -12.671 -9.490  1.00 12.56 ?  89  ALA   B C    1 
ATOM   5231 O  O    . ALA   B 1 89  ? 51.100 -12.157 -8.743  1.00 13.14 ?  89  ALA   B O    1 
ATOM   5232 C  CB   . ALA   B 1 89  ? 49.151 -14.841 -9.027  1.00 12.42 ?  89  ALA   B CB   1 
ATOM   5233 H  H    . ALA   B 1 89  ? 52.031 -14.083 -8.868  1.00 15.05 ?  89  ALA   B H    1 
ATOM   5234 H  HA   . ALA   B 1 89  ? 50.185 -14.306 -10.733 1.00 14.43 ?  89  ALA   B HA   1 
ATOM   5235 H  HB1  . ALA   B 1 89  ? 48.304 -14.505 -9.366  1.00 14.89 ?  89  ALA   B HB1  1 
ATOM   5236 H  HB2  . ALA   B 1 89  ? 49.206 -15.799 -9.178  1.00 14.89 ?  89  ALA   B HB2  1 
ATOM   5237 H  HB3  . ALA   B 1 89  ? 49.234 -14.647 -8.085  1.00 14.89 ?  89  ALA   B HB3  1 
ATOM   5238 N  N    . LYS   B 1 90  ? 49.282 -11.976 -10.059 1.00 13.41 ?  90  LYS   B N    1 
ATOM   5239 C  CA   . LYS   B 1 90  ? 49.096 -10.587 -9.657  1.00 13.67 ?  90  LYS   B CA   1 
ATOM   5240 C  C    . LYS   B 1 90  ? 48.771 -10.510 -8.170  1.00 13.29 ?  90  LYS   B C    1 
ATOM   5241 O  O    . LYS   B 1 90  ? 49.414 -9.761  -7.418  1.00 14.26 ?  90  LYS   B O    1 
ATOM   5242 C  CB   . LYS   B 1 90  ? 48.029 -9.916  -10.519 1.00 15.23 ?  90  LYS   B CB   1 
ATOM   5243 C  CG   . LYS   B 1 90  ? 47.729 -8.481  -10.124 1.00 15.69 ?  90  LYS   B CG   1 
ATOM   5244 C  CD   . LYS   B 1 90  ? 48.942 -7.586  -10.172 1.00 17.83 ?  90  LYS   B CD   1 
ATOM   5245 C  CE   . LYS   B 1 90  ? 48.477 -6.164  -9.985  1.00 20.05 ?  90  LYS   B CE   1 
ATOM   5246 N  NZ   . LYS   B 1 90  ? 49.607 -5.226  -9.831  1.00 19.93 ?  90  LYS   B NZ   1 
ATOM   5247 H  H    . LYS   B 1 90  ? 48.730 -12.275 -10.652 1.00 16.07 ?  90  LYS   B H    1 
ATOM   5248 H  HA   . LYS   B 1 90  ? 49.926 -10.115 -9.803  1.00 16.39 ?  90  LYS   B HA   1 
ATOM   5249 H  HB2  . LYS   B 1 90  ? 48.330 -9.909  -11.444 1.00 18.26 ?  90  LYS   B HB2  1 
ATOM   5250 H  HB3  . LYS   B 1 90  ? 47.203 -10.421 -10.451 1.00 18.26 ?  90  LYS   B HB3  1 
ATOM   5251 H  HG2  . LYS   B 1 90  ? 47.069 -8.119  -10.735 1.00 18.81 ?  90  LYS   B HG2  1 
ATOM   5252 H  HG3  . LYS   B 1 90  ? 47.379 -8.467  -9.218  1.00 18.81 ?  90  LYS   B HG3  1 
ATOM   5253 H  HD2  . LYS   B 1 90  ? 49.555 -7.816  -9.452  1.00 21.38 ?  90  LYS   B HD2  1 
ATOM   5254 H  HD3  . LYS   B 1 90  ? 49.382 -7.668  -11.035 1.00 21.38 ?  90  LYS   B HD3  1 
ATOM   5255 H  HE2  . LYS   B 1 90  ? 47.964 -5.887  -10.763 1.00 24.05 ?  90  LYS   B HE2  1 
ATOM   5256 H  HE3  . LYS   B 1 90  ? 47.929 -6.103  -9.188  1.00 24.05 ?  90  LYS   B HE3  1 
ATOM   5257 H  HZ1  . LYS   B 1 90  ? 49.306 -4.394  -9.725  1.00 23.91 ?  90  LYS   B HZ1  1 
ATOM   5258 H  HZ2  . LYS   B 1 90  ? 50.094 -5.449  -9.121  1.00 23.91 ?  90  LYS   B HZ2  1 
ATOM   5259 H  HZ3  . LYS   B 1 90  ? 50.127 -5.252  -10.556 1.00 23.91 ?  90  LYS   B HZ3  1 
ATOM   5260 N  N    . HIS   B 1 91  ? 47.807 -11.324 -7.724  1.00 11.91 ?  91  HIS   B N    1 
ATOM   5261 C  CA   . HIS   B 1 91  ? 47.339 -11.346 -6.351  1.00 11.86 ?  91  HIS   B CA   1 
ATOM   5262 C  C    . HIS   B 1 91  ? 47.334 -12.772 -5.832  1.00 11.00 ?  91  HIS   B C    1 
ATOM   5263 O  O    . HIS   B 1 91  ? 47.103 -13.723 -6.586  1.00 11.81 ?  91  HIS   B O    1 
ATOM   5264 C  CB   . HIS   B 1 91  ? 45.890 -10.860 -6.239  1.00 13.26 ?  91  HIS   B CB   1 
ATOM   5265 C  CG   . HIS   B 1 91  ? 45.686 -9.449  -6.666  1.00 16.84 ?  91  HIS   B CG   1 
ATOM   5266 N  ND1  . HIS   B 1 91  ? 46.314 -8.385  -6.055  1.00 19.15 ?  91  HIS   B ND1  1 
ATOM   5267 C  CD2  . HIS   B 1 91  ? 44.901 -8.922  -7.629  1.00 19.19 ?  91  HIS   B CD2  1 
ATOM   5268 C  CE1  . HIS   B 1 91  ? 45.936 -7.260  -6.635  1.00 20.04 ?  91  HIS   B CE1  1 
ATOM   5269 N  NE2  . HIS   B 1 91  ? 45.070 -7.558  -7.589  1.00 20.33 ?  91  HIS   B NE2  1 
ATOM   5270 H  H    . HIS   B 1 91  ? 47.390 -11.884 -8.227  1.00 14.27 ?  91  HIS   B H    1 
ATOM   5271 H  HA   . HIS   B 1 91  ? 47.911 -10.787 -5.789  1.00 14.22 ?  91  HIS   B HA   1 
ATOM   5272 H  HB2  . HIS   B 1 91  ? 45.329 -11.420 -6.797  1.00 15.89 ?  91  HIS   B HB2  1 
ATOM   5273 H  HB3  . HIS   B 1 91  ? 45.605 -10.933 -5.312  1.00 15.89 ?  91  HIS   B HB3  1 
ATOM   5274 H  HD1  . HIS   B 1 91  ? 46.873 -8.445  -5.400  1.00 22.97 ?  91  HIS   B HD1  1 
ATOM   5275 H  HD2  . HIS   B 1 91  ? 44.348 -9.382  -8.213  1.00 23.01 ?  91  HIS   B HD2  1 
ATOM   5276 H  HE1  . HIS   B 1 91  ? 46.228 -6.404  -6.403  1.00 24.03 ?  91  HIS   B HE1  1 
ATOM   5277 N  N    . CYS   B 1 92  ? 47.527 -12.904 -4.530  1.00 11.05 ?  92  CYS   B N    1 
ATOM   5278 C  CA   . CYS   B 1 92  ? 47.221 -14.134 -3.814  1.00 10.83 ?  92  CYS   B CA   1 
ATOM   5279 C  C    . CYS   B 1 92  ? 46.002 -13.894 -2.935  1.00 10.64 ?  92  CYS   B C    1 
ATOM   5280 O  O    . CYS   B 1 92  ? 46.000 -12.989 -2.089  1.00 11.83 ?  92  CYS   B O    1 
ATOM   5281 C  CB   . CYS   B 1 92  ? 48.398 -14.593 -2.960  1.00 11.38 ?  92  CYS   B CB   1 
ATOM   5282 S  SG   . CYS   B 1 92  ? 48.040 -16.133 -2.064  1.00 11.37 ?  92  CYS   B SG   1 
ATOM   5283 H  H    . CYS   B 1 92  ? 47.860 -12.282 -4.025  1.00 13.24 ?  92  CYS   B H    1 
ATOM   5284 H  HA   . CYS   B 1 92  ? 47.017 -14.830 -4.457  1.00 12.97 ?  92  CYS   B HA   1 
ATOM   5285 H  HB2  . CYS   B 1 92  ? 49.164 -14.741 -3.528  1.00 13.64 ?  92  CYS   B HB2  1 
ATOM   5286 H  HB3  . CYS   B 1 92  ? 48.593 -13.904 -2.304  1.00 13.64 ?  92  CYS   B HB3  1 
ATOM   5287 H  HG   . CYS   B 1 92  ? 49.017 -16.452 -1.437  1.00 13.62 ?  92  CYS   B HG   1 
ATOM   5288 N  N    . LEU   B 1 93  ? 44.966 -14.703 -3.146  1.00 10.84 ?  93  LEU   B N    1 
ATOM   5289 C  CA   . LEU   B 1 93  ? 43.790 -14.718 -2.288  1.00 10.87 ?  93  LEU   B CA   1 
ATOM   5290 C  C    . LEU   B 1 93  ? 44.013 -15.778 -1.221  1.00 10.30 ?  93  LEU   B C    1 
ATOM   5291 O  O    . LEU   B 1 93  ? 43.965 -16.978 -1.511  1.00 11.26 ?  93  LEU   B O    1 
ATOM   5292 C  CB   . LEU   B 1 93  ? 42.532 -15.017 -3.098  1.00 11.50 ?  93  LEU   B CB   1 
ATOM   5293 C  CG   . LEU   B 1 93  ? 41.228 -15.023 -2.288  1.00 12.15 ?  93  LEU   B CG   1 
ATOM   5294 C  CD1  . LEU   B 1 93  ? 40.884 -13.630 -1.815  1.00 12.34 ?  93  LEU   B CD1  1 
ATOM   5295 C  CD2  . LEU   B 1 93  ? 40.093 -15.612 -3.111  1.00 12.44 ?  93  LEU   B CD2  1 
ATOM   5296 H  H    . LEU   B 1 93  ? 44.923 -15.277 -3.795  1.00 12.99 ?  93  LEU   B H    1 
ATOM   5297 H  HA   . LEU   B 1 93  ? 43.691 -13.856 -1.860  1.00 13.02 ?  93  LEU   B HA   1 
ATOM   5298 H  HB2  . LEU   B 1 93  ? 42.442 -14.339 -3.787  1.00 13.78 ?  93  LEU   B HB2  1 
ATOM   5299 H  HB3  . LEU   B 1 93  ? 42.626 -15.887 -3.507  1.00 13.78 ?  93  LEU   B HB3  1 
ATOM   5300 H  HG   . LEU   B 1 93  ? 41.342 -15.581 -1.507  1.00 14.56 ?  93  LEU   B HG   1 
ATOM   5301 H  HD11 . LEU   B 1 93  ? 40.023 -13.645 -1.374  1.00 14.79 ?  93  LEU   B HD11 1 
ATOM   5302 H  HD12 . LEU   B 1 93  ? 41.569 -13.327 -1.199  1.00 14.79 ?  93  LEU   B HD12 1 
ATOM   5303 H  HD13 . LEU   B 1 93  ? 40.849 -13.033 -2.585  1.00 14.79 ?  93  LEU   B HD13 1 
ATOM   5304 H  HD21 . LEU   B 1 93  ? 39.277 -15.599 -2.582  1.00 14.91 ?  93  LEU   B HD21 1 
ATOM   5305 H  HD22 . LEU   B 1 93  ? 39.971 -15.083 -3.915  1.00 14.91 ?  93  LEU   B HD22 1 
ATOM   5306 H  HD23 . LEU   B 1 93  ? 40.313 -16.528 -3.349  1.00 14.91 ?  93  LEU   B HD23 1 
ATOM   5307 N  N    . HIS   B 1 94  ? 44.287 -15.342 0.002   1.00 10.53 ?  94  HIS   B N    1 
ATOM   5308 C  CA   . HIS   B 1 94  ? 44.504 -16.249 1.123   1.00 10.81 ?  94  HIS   B CA   1 
ATOM   5309 C  C    . HIS   B 1 94  ? 43.145 -16.605 1.703   1.00 11.38 ?  94  HIS   B C    1 
ATOM   5310 O  O    . HIS   B 1 94  ? 42.472 -15.730 2.249   1.00 12.48 ?  94  HIS   B O    1 
ATOM   5311 C  CB   . HIS   B 1 94  ? 45.375 -15.570 2.180   1.00 11.29 ?  94  HIS   B CB   1 
ATOM   5312 C  CG   . HIS   B 1 94  ? 46.758 -15.272 1.711   1.00 11.00 ?  94  HIS   B CG   1 
ATOM   5313 N  ND1  . HIS   B 1 94  ? 47.783 -16.190 1.790   1.00 11.48 ?  94  HIS   B ND1  1 
ATOM   5314 C  CD2  . HIS   B 1 94  ? 47.269 -14.167 1.116   1.00 11.31 ?  94  HIS   B CD2  1 
ATOM   5315 C  CE1  . HIS   B 1 94  ? 48.873 -15.642 1.280   1.00 11.44 ?  94  HIS   B CE1  1 
ATOM   5316 N  NE2  . HIS   B 1 94  ? 48.590 -14.418 0.864   1.00 11.52 ?  94  HIS   B NE2  1 
ATOM   5317 H  H    . HIS   B 1 94  ? 44.352 -14.507 0.208   1.00 12.62 ?  94  HIS   B H    1 
ATOM   5318 H  HA   . HIS   B 1 94  ? 44.940 -17.055 0.815   1.00 12.95 ?  94  HIS   B HA   1 
ATOM   5319 H  HB2  . HIS   B 1 94  ? 44.960 -14.731 2.430   1.00 13.53 ?  94  HIS   B HB2  1 
ATOM   5320 H  HB3  . HIS   B 1 94  ? 45.439 -16.154 2.945   1.00 13.53 ?  94  HIS   B HB3  1 
ATOM   5321 H  HD2  . HIS   B 1 94  ? 46.816 -13.381 0.925   1.00 13.56 ?  94  HIS   B HD2  1 
ATOM   5322 H  HE1  . HIS   B 1 94  ? 49.702 -16.066 1.213   1.00 13.71 ?  94  HIS   B HE1  1 
ATOM   5323 H  HE2  . HIS   B 1 94  ? 49.149 -13.880 0.498   1.00 13.81 ?  94  HIS   B HE2  1 
ATOM   5324 N  N    . VAL   B 1 95  ? 42.711 -17.858 1.556   1.00 11.05 ?  95  VAL   B N    1 
ATOM   5325 C  CA   . VAL   B 1 95  ? 41.385 -18.289 1.989   1.00 11.11 ?  95  VAL   B CA   1 
ATOM   5326 C  C    . VAL   B 1 95  ? 41.552 -19.325 3.085   1.00 11.61 ?  95  VAL   B C    1 
ATOM   5327 O  O    . VAL   B 1 95  ? 42.326 -20.277 2.929   1.00 12.41 ?  95  VAL   B O    1 
ATOM   5328 C  CB   . VAL   B 1 95  ? 40.564 -18.893 0.833   1.00 11.48 ?  95  VAL   B CB   1 
ATOM   5329 C  CG1  . VAL   B 1 95  ? 39.196 -19.352 1.324   1.00 12.96 ?  95  VAL   B CG1  1 
ATOM   5330 C  CG2  . VAL   B 1 95  ? 40.434 -17.916 -0.305  1.00 11.40 ?  95  VAL   B CG2  1 
ATOM   5331 H  H    . VAL   B 1 95  ? 43.173 -18.485 1.190   1.00 13.24 ?  95  VAL   B H    1 
ATOM   5332 H  HA   . VAL   B 1 95  ? 40.894 -17.532 2.353   1.00 13.31 ?  95  VAL   B HA   1 
ATOM   5333 H  HB   . VAL   B 1 95  ? 41.031 -19.668 0.497   1.00 13.76 ?  95  VAL   B HB   1 
ATOM   5334 H  HG11 . VAL   B 1 95  ? 38.628 -19.536 0.555   1.00 15.54 ?  95  VAL   B HG11 1 
ATOM   5335 H  HG12 . VAL   B 1 95  ? 39.298 -20.161 1.852   1.00 15.54 ?  95  VAL   B HG12 1 
ATOM   5336 H  HG13 . VAL   B 1 95  ? 38.795 -18.653 1.864   1.00 15.54 ?  95  VAL   B HG13 1 
ATOM   5337 H  HG21 . VAL   B 1 95  ? 39.859 -18.305 -0.986  1.00 13.66 ?  95  VAL   B HG21 1 
ATOM   5338 H  HG22 . VAL   B 1 95  ? 40.033 -17.095 0.030   1.00 13.66 ?  95  VAL   B HG22 1 
ATOM   5339 H  HG23 . VAL   B 1 95  ? 41.308 -17.735 -0.669  1.00 13.66 ?  95  VAL   B HG23 1 
ATOM   5340 N  N    . VAL   B 1 96  ? 40.817 -19.157 4.178   1.00 12.05 ?  96  VAL   B N    1 
ATOM   5341 C  CA   . VAL   B 1 96  ? 40.902 -20.074 5.316   1.00 12.29 ?  96  VAL   B CA   1 
ATOM   5342 C  C    . VAL   B 1 96  ? 39.714 -21.030 5.269   1.00 13.04 ?  96  VAL   B C    1 
ATOM   5343 O  O    . VAL   B 1 96  ? 38.597 -20.676 5.654   1.00 13.76 ?  96  VAL   B O    1 
ATOM   5344 C  CB   . VAL   B 1 96  ? 40.952 -19.325 6.651   1.00 13.37 ?  96  VAL   B CB   1 
ATOM   5345 C  CG1  . VAL   B 1 96  ? 41.123 -20.317 7.793   1.00 13.82 ?  96  VAL   B CG1  1 
ATOM   5346 C  CG2  . VAL   B 1 96  ? 42.069 -18.291 6.657   1.00 14.06 ?  96  VAL   B CG2  1 
ATOM   5347 H  H    . VAL   B 1 96  ? 40.250 -18.521 4.289   1.00 14.44 ?  96  VAL   B H    1 
ATOM   5348 H  HA   . VAL   B 1 96  ? 41.714 -20.601 5.240   1.00 14.73 ?  96  VAL   B HA   1 
ATOM   5349 H  HB   . VAL   B 1 96  ? 40.111 -18.860 6.783   1.00 16.03 ?  96  VAL   B HB   1 
ATOM   5350 H  HG11 . VAL   B 1 96  ? 41.318 -19.831 8.610   1.00 16.57 ?  96  VAL   B HG11 1 
ATOM   5351 H  HG12 . VAL   B 1 96  ? 40.306 -20.828 7.902   1.00 16.57 ?  96  VAL   B HG12 1 
ATOM   5352 H  HG13 . VAL   B 1 96  ? 41.861 -20.916 7.586   1.00 16.57 ?  96  VAL   B HG13 1 
ATOM   5353 H  HG21 . VAL   B 1 96  ? 42.119 -17.883 7.536   1.00 16.86 ?  96  VAL   B HG21 1 
ATOM   5354 H  HG22 . VAL   B 1 96  ? 42.908 -18.728 6.446   1.00 16.86 ?  96  VAL   B HG22 1 
ATOM   5355 H  HG23 . VAL   B 1 96  ? 41.875 -17.610 5.990   1.00 16.86 ?  96  VAL   B HG23 1 
ATOM   5356 N  N    . GLY   B 1 97  ? 39.948 -22.261 4.824   1.00 13.07 ?  97  GLY   B N    1 
ATOM   5357 C  CA   . GLY   B 1 97  ? 38.969 -23.313 4.979   1.00 14.24 ?  97  GLY   B CA   1 
ATOM   5358 C  C    . GLY   B 1 97  ? 39.099 -23.927 6.353   1.00 15.36 ?  97  GLY   B C    1 
ATOM   5359 O  O    . GLY   B 1 97  ? 40.141 -23.796 7.009   1.00 15.65 ?  97  GLY   B O    1 
ATOM   5360 H  H    . GLY   B 1 97  ? 40.674 -22.504 4.424   1.00 15.67 ?  97  GLY   B H    1 
ATOM   5361 H  HA2  . GLY   B 1 97  ? 38.076 -22.938 4.869   1.00 17.07 ?  97  GLY   B HA2  1 
ATOM   5362 H  HA3  . GLY   B 1 97  ? 39.106 -23.994 4.304   1.00 17.07 ?  97  GLY   B HA3  1 
ATOM   5363 N  N    . PRO   B 1 98  ? 38.057 -24.618 6.816   1.00 16.14 ?  98  PRO   B N    1 
ATOM   5364 C  CA   . PRO   B 1 98  ? 38.156 -25.314 8.103   1.00 17.21 ?  98  PRO   B CA   1 
ATOM   5365 C  C    . PRO   B 1 98  ? 39.179 -26.437 8.058   1.00 16.79 ?  98  PRO   B C    1 
ATOM   5366 O  O    . PRO   B 1 98  ? 39.285 -27.170 7.075   1.00 16.97 ?  98  PRO   B O    1 
ATOM   5367 C  CB   . PRO   B 1 98  ? 36.739 -25.859 8.320   1.00 17.37 ?  98  PRO   B CB   1 
ATOM   5368 C  CG   . PRO   B 1 98  ? 36.165 -25.981 6.954   1.00 16.95 ?  98  PRO   B CG   1 
ATOM   5369 C  CD   . PRO   B 1 98  ? 36.730 -24.800 6.197   1.00 16.30 ?  98  PRO   B CD   1 
ATOM   5370 H  HA   . PRO   B 1 98  ? 38.385 -24.693 8.806   1.00 20.64 ?  98  PRO   B HA   1 
ATOM   5371 H  HB2  . PRO   B 1 98  ? 36.787 -26.726 8.753   1.00 20.83 ?  98  PRO   B HB2  1 
ATOM   5372 H  HB3  . PRO   B 1 98  ? 36.230 -25.233 8.853   1.00 20.83 ?  98  PRO   B HB3  1 
ATOM   5373 H  HG2  . PRO   B 1 98  ? 36.452 -26.818 6.553   1.00 20.33 ?  98  PRO   B HG2  1 
ATOM   5374 H  HG3  . PRO   B 1 98  ? 35.199 -25.935 7.001   1.00 20.33 ?  98  PRO   B HG3  1 
ATOM   5375 H  HD2  . PRO   B 1 98  ? 36.814 -25.012 5.251   1.00 19.54 ?  98  PRO   B HD2  1 
ATOM   5376 H  HD3  . PRO   B 1 98  ? 36.181 -24.012 6.336   1.00 19.54 ?  98  PRO   B HD3  1 
ATOM   5377 N  N    . ASN   B 1 99  ? 39.937 -26.560 9.141   1.00 18.32 ?  99  ASN   B N    1 
ATOM   5378 C  CA   . ASN   B 1 99  ? 40.918 -27.630 9.306   1.00 19.37 ?  99  ASN   B CA   1 
ATOM   5379 C  C    . ASN   B 1 99  ? 40.295 -28.706 10.192  1.00 22.40 ?  99  ASN   B C    1 
ATOM   5380 O  O    . ASN   B 1 99  ? 40.231 -28.557 11.414  1.00 22.91 ?  99  ASN   B O    1 
ATOM   5381 C  CB   . ASN   B 1 99  ? 42.190 -27.071 9.930   1.00 19.28 ?  99  ASN   B CB   1 
ATOM   5382 C  CG   . ASN   B 1 99  ? 43.322 -28.076 9.941   1.00 20.13 ?  99  ASN   B CG   1 
ATOM   5383 O  OD1  . ASN   B 1 99  ? 43.101 -29.266 10.108  1.00 20.74 ?  99  ASN   B OD1  1 
ATOM   5384 N  ND2  . ASN   B 1 99  ? 44.537 -27.599 9.752   1.00 20.05 ?  99  ASN   B ND2  1 
ATOM   5385 H  H    . ASN   B 1 99  ? 39.905 -26.019 9.803   1.00 21.96 ?  99  ASN   B H    1 
ATOM   5386 H  HA   . ASN   B 1 99  ? 41.131 -28.025 8.447   1.00 23.23 ?  99  ASN   B HA   1 
ATOM   5387 H  HB2  . ASN   B 1 99  ? 42.473 -26.301 9.426   1.00 23.12 ?  99  ASN   B HB2  1 
ATOM   5388 H  HB3  . ASN   B 1 99  ? 41.999 -26.821 10.851  1.00 23.12 ?  99  ASN   B HB3  1 
ATOM   5389 H  HD21 . ASN   B 1 99  ? 45.209 -28.132 9.747   1.00 24.04 ?  99  ASN   B HD21 1 
ATOM   5390 H  HD22 . ASN   B 1 99  ? 44.647 -26.757 9.637   1.00 24.04 ?  99  ASN   B HD22 1 
ATOM   5391 N  N    A VAL   B 1 100 ? 39.829 -29.792 9.572   0.64 24.11 ?  100 VAL   B N    1 
ATOM   5392 N  N    B VAL   B 1 100 ? 39.839 -29.793 9.564   0.36 24.30 ?  100 VAL   B N    1 
ATOM   5393 C  CA   A VAL   B 1 100 ? 39.208 -30.871 10.338  0.64 26.63 ?  100 VAL   B CA   1 
ATOM   5394 C  CA   B VAL   B 1 100 ? 39.212 -30.886 10.304  0.36 26.52 ?  100 VAL   B CA   1 
ATOM   5395 C  C    A VAL   B 1 100 ? 40.218 -31.524 11.271  0.64 27.37 ?  100 VAL   B C    1 
ATOM   5396 C  C    B VAL   B 1 100 ? 40.209 -31.552 11.243  0.36 27.31 ?  100 VAL   B C    1 
ATOM   5397 O  O    A VAL   B 1 100 ? 39.859 -31.988 12.360  0.64 27.95 ?  100 VAL   B O    1 
ATOM   5398 O  O    B VAL   B 1 100 ? 39.831 -32.050 12.311  0.36 27.59 ?  100 VAL   B O    1 
ATOM   5399 C  CB   A VAL   B 1 100 ? 38.546 -31.891 9.390   0.64 28.66 ?  100 VAL   B CB   1 
ATOM   5400 C  CB   B VAL   B 1 100 ? 38.576 -31.888 9.318   0.36 28.01 ?  100 VAL   B CB   1 
ATOM   5401 C  CG1  A VAL   B 1 100 ? 38.063 -33.109 10.164  0.64 29.48 ?  100 VAL   B CG1  1 
ATOM   5402 C  CG1  B VAL   B 1 100 ? 38.096 -33.136 10.045  0.36 28.58 ?  100 VAL   B CG1  1 
ATOM   5403 C  CG2  A VAL   B 1 100 ? 37.389 -31.241 8.647   0.64 29.21 ?  100 VAL   B CG2  1 
ATOM   5404 C  CG2  B VAL   B 1 100 ? 37.425 -31.229 8.573   0.36 28.48 ?  100 VAL   B CG2  1 
ATOM   5405 H  H    A VAL   B 1 100 ? 39.857 -29.924 8.723   0.64 28.91 ?  100 VAL   B H    1 
ATOM   5406 H  H    B VAL   B 1 100 ? 39.880 -29.919 8.714   0.36 29.15 ?  100 VAL   B H    1 
ATOM   5407 H  HA   A VAL   B 1 100 ? 38.501 -30.492 10.885  0.64 31.94 ?  100 VAL   B HA   1 
ATOM   5408 H  HA   B VAL   B 1 100 ? 38.496 -30.521 10.846  0.36 31.81 ?  100 VAL   B HA   1 
ATOM   5409 H  HB   A VAL   B 1 100 ? 39.198 -32.190 8.738   0.64 34.38 ?  100 VAL   B HB   1 
ATOM   5410 H  HB   B VAL   B 1 100 ? 39.240 -32.159 8.666   0.36 33.60 ?  100 VAL   B HB   1 
ATOM   5411 H  HG11 A VAL   B 1 100 ? 37.460 -33.621 9.601   0.64 35.37 ?  100 VAL   B HG11 1 
ATOM   5412 H  HG11 B VAL   B 1 100 ? 37.511 -33.638 9.454   0.36 34.29 ?  100 VAL   B HG11 1 
ATOM   5413 H  HG12 A VAL   B 1 100 ? 38.825 -33.656 10.411  0.64 35.37 ?  100 VAL   B HG12 1 
ATOM   5414 H  HG12 B VAL   B 1 100 ? 38.863 -33.679 10.286  0.36 34.29 ?  100 VAL   B HG12 1 
ATOM   5415 H  HG13 A VAL   B 1 100 ? 37.595 -32.813 10.961  0.64 35.37 ?  100 VAL   B HG13 1 
ATOM   5416 H  HG13 B VAL   B 1 100 ? 37.611 -32.872 10.841  0.36 34.29 ?  100 VAL   B HG13 1 
ATOM   5417 H  HG21 A VAL   B 1 100 ? 36.982 -31.899 8.061   0.64 35.03 ?  100 VAL   B HG21 1 
ATOM   5418 H  HG21 B VAL   B 1 100 ? 37.028 -31.875 7.969   0.36 34.15 ?  100 VAL   B HG21 1 
ATOM   5419 H  HG22 A VAL   B 1 100 ? 36.738 -30.925 9.293   0.64 35.03 ?  100 VAL   B HG22 1 
ATOM   5420 H  HG22 B VAL   B 1 100 ? 36.764 -30.928 9.217   0.36 34.15 ?  100 VAL   B HG22 1 
ATOM   5421 H  HG23 A VAL   B 1 100 ? 37.728 -30.497 8.127   0.64 35.03 ?  100 VAL   B HG23 1 
ATOM   5422 H  HG23 B VAL   B 1 100 ? 37.767 -30.473 8.072   0.36 34.15 ?  100 VAL   B HG23 1 
ATOM   5423 N  N    . ASN   B 1 101 ? 41.489 -31.585 10.865  1.00 27.92 ?  101 ASN   B N    1 
ATOM   5424 C  CA   . ASN   B 1 101 ? 42.528 -32.122 11.740  1.00 29.58 ?  101 ASN   B CA   1 
ATOM   5425 C  C    . ASN   B 1 101 ? 42.737 -31.278 12.992  1.00 32.24 ?  101 ASN   B C    1 
ATOM   5426 O  O    . ASN   B 1 101 ? 43.388 -31.748 13.934  1.00 33.20 ?  101 ASN   B O    1 
ATOM   5427 C  CB   . ASN   B 1 101 ? 43.848 -32.266 10.976  1.00 29.29 ?  101 ASN   B CB   1 
ATOM   5428 C  CG   . ASN   B 1 101 ? 43.824 -33.416 9.987   1.00 28.80 ?  101 ASN   B CG   1 
ATOM   5429 O  OD1  . ASN   B 1 101 ? 43.147 -34.413 10.204  1.00 29.34 ?  101 ASN   B OD1  1 
ATOM   5430 N  ND2  . ASN   B 1 101 ? 44.557 -33.277 8.892   1.00 28.41 ?  101 ASN   B ND2  1 
ATOM   5431 H  H    A ASN   B 1 101 ? 41.764 -31.339 10.089  0.64 33.49 ?  101 ASN   B H    1 
ATOM   5432 H  H    B ASN   B 1 101 ? 41.774 -31.313 10.101  0.36 33.49 ?  101 ASN   B H    1 
ATOM   5433 H  HA   . ASN   B 1 101 ? 42.259 -33.003 12.030  1.00 35.47 ?  101 ASN   B HA   1 
ATOM   5434 H  HB2  . ASN   B 1 101 ? 44.025 -31.454 10.481  1.00 35.13 ?  101 ASN   B HB2  1 
ATOM   5435 H  HB3  . ASN   B 1 101 ? 44.563 -32.432 11.611  1.00 35.13 ?  101 ASN   B HB3  1 
ATOM   5436 H  HD21 . ASN   B 1 101 ? 44.573 -33.905 8.304   1.00 34.07 ?  101 ASN   B HD21 1 
ATOM   5437 H  HD22 . ASN   B 1 101 ? 45.012 -32.560 8.770   1.00 34.07 ?  101 ASN   B HD22 1 
ATOM   5438 N  N    . LYS   B 1 102 ? 42.215 -30.050 13.019  1.00 35.09 ?  102 LYS   B N    1 
ATOM   5439 C  CA   . LYS   B 1 102 ? 42.174 -29.222 14.217  1.00 38.12 ?  102 LYS   B CA   1 
ATOM   5440 C  C    . LYS   B 1 102 ? 40.781 -29.168 14.832  1.00 37.59 ?  102 LYS   B C    1 
ATOM   5441 O  O    . LYS   B 1 102 ? 40.539 -28.347 15.722  1.00 37.91 ?  102 LYS   B O    1 
ATOM   5442 C  CB   . LYS   B 1 102 ? 42.641 -27.799 13.902  1.00 41.72 ?  102 LYS   B CB   1 
ATOM   5443 C  CG   . LYS   B 1 102 ? 44.104 -27.668 13.521  1.00 44.95 ?  102 LYS   B CG   1 
ATOM   5444 C  CD   . LYS   B 1 102 ? 44.393 -26.251 13.051  1.00 47.89 ?  102 LYS   B CD   1 
ATOM   5445 C  CE   . LYS   B 1 102 ? 45.877 -25.998 12.856  1.00 50.09 ?  102 LYS   B CE   1 
ATOM   5446 N  NZ   . LYS   B 1 102 ? 46.123 -24.604 12.380  1.00 51.36 ?  102 LYS   B NZ   1 
ATOM   5447 H  H    . LYS   B 1 102 ? 41.867 -29.666 12.333  1.00 42.09 ?  102 LYS   B H    1 
ATOM   5448 H  HA   . LYS   B 1 102 ? 42.782 -29.592 14.875  1.00 45.73 ?  102 LYS   B HA   1 
ATOM   5449 H  HB2  . LYS   B 1 102 ? 42.115 -27.457 13.164  1.00 50.04 ?  102 LYS   B HB2  1 
ATOM   5450 H  HB3  . LYS   B 1 102 ? 42.496 -27.246 14.688  1.00 50.04 ?  102 LYS   B HB3  1 
ATOM   5451 H  HG2  . LYS   B 1 102 ? 44.661 -27.856 14.293  1.00 53.93 ?  102 LYS   B HG2  1 
ATOM   5452 H  HG3  . LYS   B 1 102 ? 44.307 -28.281 12.797  1.00 53.93 ?  102 LYS   B HG3  1 
ATOM   5453 H  HD2  . LYS   B 1 102 ? 43.947 -26.102 12.202  1.00 57.45 ?  102 LYS   B HD2  1 
ATOM   5454 H  HD3  . LYS   B 1 102 ? 44.064 -25.624 13.714  1.00 57.45 ?  102 LYS   B HD3  1 
ATOM   5455 H  HE2  . LYS   B 1 102 ? 46.338 -26.118 13.701  1.00 60.09 ?  102 LYS   B HE2  1 
ATOM   5456 H  HE3  . LYS   B 1 102 ? 46.224 -26.614 12.192  1.00 60.09 ?  102 LYS   B HE3  1 
ATOM   5457 H  HZ1  . LYS   B 1 102 ? 46.995 -24.469 12.270  1.00 61.61 ?  102 LYS   B HZ1  1 
ATOM   5458 H  HZ2  . LYS   B 1 102 ? 45.709 -24.471 11.603  1.00 61.61 ?  102 LYS   B HZ2  1 
ATOM   5459 H  HZ3  . LYS   B 1 102 ? 45.812 -24.020 12.976  1.00 61.61 ?  102 LYS   B HZ3  1 
ATOM   5460 N  N    . GLY   B 1 103 ? 39.856 -30.005 14.365  1.00 37.05 ?  103 GLY   B N    1 
ATOM   5461 C  CA   . GLY   B 1 103 ? 38.522 -30.071 14.929  1.00 36.65 ?  103 GLY   B CA   1 
ATOM   5462 C  C    . GLY   B 1 103 ? 37.569 -28.990 14.472  1.00 35.64 ?  103 GLY   B C    1 
ATOM   5463 O  O    . GLY   B 1 103 ? 36.459 -28.902 15.009  1.00 36.05 ?  103 GLY   B O    1 
ATOM   5464 H  H    . GLY   B 1 103 ? 39.984 -30.548 13.714  1.00 44.45 ?  103 GLY   B H    1 
ATOM   5465 H  HA2  . GLY   B 1 103 ? 38.131 -30.929 14.703  1.00 43.97 ?  103 GLY   B HA2  1 
ATOM   5466 H  HA3  . GLY   B 1 103 ? 38.587 -30.018 15.895  1.00 43.97 ?  103 GLY   B HA3  1 
ATOM   5467 N  N    A GLU   B 1 104 ? 37.968 -28.157 13.514  0.64 34.69 ?  104 GLU   B N    1 
ATOM   5468 N  N    B GLU   B 1 104 ? 37.948 -28.181 13.487  0.36 34.77 ?  104 GLU   B N    1 
ATOM   5469 C  CA   A GLU   B 1 104 ? 37.123 -27.061 13.070  0.64 33.61 ?  104 GLU   B CA   1 
ATOM   5470 C  CA   B GLU   B 1 104 ? 37.082 -27.108 13.026  0.36 33.73 ?  104 GLU   B CA   1 
ATOM   5471 C  C    A GLU   B 1 104 ? 35.939 -27.587 12.257  0.64 33.56 ?  104 GLU   B C    1 
ATOM   5472 C  C    B GLU   B 1 104 ? 35.921 -27.665 12.201  0.36 33.71 ?  104 GLU   B C    1 
ATOM   5473 O  O    A GLU   B 1 104 ? 35.978 -28.675 11.676  0.64 33.81 ?  104 GLU   B O    1 
ATOM   5474 O  O    B GLU   B 1 104 ? 35.989 -28.758 11.632  0.36 33.85 ?  104 GLU   B O    1 
ATOM   5475 C  CB   A GLU   B 1 104 ? 37.946 -26.056 12.262  0.64 32.74 ?  104 GLU   B CB   1 
ATOM   5476 C  CB   B GLU   B 1 104 ? 37.890 -26.085 12.229  0.36 32.73 ?  104 GLU   B CB   1 
ATOM   5477 C  CG   A GLU   B 1 104 ? 39.062 -25.416 13.080  0.64 31.77 ?  104 GLU   B CG   1 
ATOM   5478 C  CG   B GLU   B 1 104 ? 38.988 -25.434 13.060  0.36 31.76 ?  104 GLU   B CG   1 
ATOM   5479 C  CD   A GLU   B 1 104 ? 39.979 -24.530 12.264  0.64 30.69 ?  104 GLU   B CD   1 
ATOM   5480 C  CD   B GLU   B 1 104 ? 39.935 -24.581 12.240  0.36 30.86 ?  104 GLU   B CD   1 
ATOM   5481 O  OE1  A GLU   B 1 104 ? 39.960 -24.618 11.018  0.64 29.48 ?  104 GLU   B OE1  1 
ATOM   5482 O  OE1  B GLU   B 1 104 ? 39.859 -24.621 10.994  0.36 30.17 ?  104 GLU   B OE1  1 
ATOM   5483 O  OE2  A GLU   B 1 104 ? 40.728 -23.742 12.878  0.64 30.50 -1 104 GLU   B OE2  1 
ATOM   5484 O  OE2  B GLU   B 1 104 ? 40.760 -23.868 12.848  0.36 30.61 -1 104 GLU   B OE2  1 
ATOM   5485 H  H    A GLU   B 1 104 ? 38.728 -28.202 13.114  0.64 41.61 ?  104 GLU   B H    1 
ATOM   5486 H  H    B GLU   B 1 104 ? 38.702 -28.231 13.076  0.36 41.71 ?  104 GLU   B H    1 
ATOM   5487 H  HA   A GLU   B 1 104 ? 36.774 -26.598 13.849  0.64 40.32 ?  104 GLU   B HA   1 
ATOM   5488 H  HA   B GLU   B 1 104 ? 36.709 -26.655 13.796  0.36 40.45 ?  104 GLU   B HA   1 
ATOM   5489 H  HB2  A GLU   B 1 104 ? 38.351 -26.511 11.507  0.64 39.27 ?  104 GLU   B HB2  1 
ATOM   5490 H  HB2  B GLU   B 1 104 ? 38.307 -26.527 11.473  0.36 39.26 ?  104 GLU   B HB2  1 
ATOM   5491 H  HB3  A GLU   B 1 104 ? 37.362 -25.347 11.948  0.64 39.27 ?  104 GLU   B HB3  1 
ATOM   5492 H  HB3  B GLU   B 1 104 ? 37.295 -25.384 11.916  0.36 39.26 ?  104 GLU   B HB3  1 
ATOM   5493 H  HG2  A GLU   B 1 104 ? 38.670 -24.871 13.781  0.64 38.10 ?  104 GLU   B HG2  1 
ATOM   5494 H  HG2  B GLU   B 1 104 ? 38.579 -24.865 13.732  0.36 38.10 ?  104 GLU   B HG2  1 
ATOM   5495 H  HG3  A GLU   B 1 104 ? 39.609 -26.114 13.473  0.64 38.10 ?  104 GLU   B HG3  1 
ATOM   5496 H  HG3  B GLU   B 1 104 ? 39.511 -26.129 13.492  0.36 38.10 ?  104 GLU   B HG3  1 
ATOM   5497 N  N    A ASP   B 1 105 ? 34.874 -26.788 12.224  0.64 33.01 ?  105 ASP   B N    1 
ATOM   5498 N  N    B ASP   B 1 105 ? 34.840 -26.887 12.144  0.36 33.39 ?  105 ASP   B N    1 
ATOM   5499 C  CA   A ASP   B 1 105 ? 33.599 -27.232 11.673  0.64 33.00 ?  105 ASP   B CA   1 
ATOM   5500 C  CA   B ASP   B 1 105 ? 33.579 -27.353 11.580  0.36 33.29 ?  105 ASP   B CA   1 
ATOM   5501 C  C    A ASP   B 1 105 ? 33.664 -27.286 10.151  0.64 30.72 ?  105 ASP   B C    1 
ATOM   5502 C  C    B ASP   B 1 105 ? 33.659 -27.371 10.058  0.36 31.86 ?  105 ASP   B C    1 
ATOM   5503 O  O    A ASP   B 1 105 ? 33.850 -26.259 9.493   0.64 29.51 ?  105 ASP   B O    1 
ATOM   5504 O  O    B ASP   B 1 105 ? 33.881 -26.332 9.427   0.36 31.41 ?  105 ASP   B O    1 
ATOM   5505 C  CB   A ASP   B 1 105 ? 32.487 -26.284 12.118  0.64 35.55 ?  105 ASP   B CB   1 
ATOM   5506 C  CB   B ASP   B 1 105 ? 32.437 -26.450 12.044  0.36 34.61 ?  105 ASP   B CB   1 
ATOM   5507 C  CG   A ASP   B 1 105 ? 31.114 -26.743 11.669  0.64 37.77 ?  105 ASP   B CG   1 
ATOM   5508 C  CG   B ASP   B 1 105 ? 31.072 -26.988 11.655  0.36 35.80 ?  105 ASP   B CG   1 
ATOM   5509 O  OD1  A ASP   B 1 105 ? 31.000 -27.870 11.144  0.64 38.04 ?  105 ASP   B OD1  1 
ATOM   5510 O  OD1  B ASP   B 1 105 ? 31.013 -28.054 11.005  0.36 36.05 ?  105 ASP   B OD1  1 
ATOM   5511 O  OD2  A ASP   B 1 105 ? 30.145 -25.969 11.836  0.64 38.93 -1 105 ASP   B OD2  1 
ATOM   5512 O  OD2  B ASP   B 1 105 ? 30.055 -26.349 12.002  0.36 36.28 -1 105 ASP   B OD2  1 
ATOM   5513 H  H    A ASP   B 1 105 ? 34.870 -25.980 12.516  0.64 39.60 ?  105 ASP   B H    1 
ATOM   5514 H  H    B ASP   B 1 105 ? 34.815 -26.076 12.426  0.36 40.05 ?  105 ASP   B H    1 
ATOM   5515 H  HA   A ASP   B 1 105 ? 33.396 -28.120 12.005  0.64 39.58 ?  105 ASP   B HA   1 
ATOM   5516 H  HA   B ASP   B 1 105 ? 33.397 -28.254 11.888  0.36 39.93 ?  105 ASP   B HA   1 
ATOM   5517 H  HB2  A ASP   B 1 105 ? 32.498 -26.215 13.087  0.64 42.65 ?  105 ASP   B HB2  1 
ATOM   5518 H  HB2  B ASP   B 1 105 ? 32.465 -26.374 13.012  0.36 41.52 ?  105 ASP   B HB2  1 
ATOM   5519 H  HB3  A ASP   B 1 105 ? 32.635 -25.413 11.722  0.64 42.65 ?  105 ASP   B HB3  1 
ATOM   5520 H  HB3  B ASP   B 1 105 ? 32.541 -25.572 11.641  0.36 41.52 ?  105 ASP   B HB3  1 
ATOM   5521 N  N    A ILE   B 1 106 ? 33.475 -28.486 9.595   0.64 29.73 ?  106 ILE   B N    1 
ATOM   5522 N  N    B ILE   B 1 106 ? 33.461 -28.555 9.471   0.36 30.88 ?  106 ILE   B N    1 
ATOM   5523 C  CA   A ILE   B 1 106 ? 33.480 -28.670 8.149   0.64 28.58 ?  106 ILE   B CA   1 
ATOM   5524 C  CA   B ILE   B 1 106 ? 33.473 -28.702 8.020   0.36 30.03 ?  106 ILE   B CA   1 
ATOM   5525 C  C    A ILE   B 1 106 ? 32.393 -27.848 7.469   0.64 27.47 ?  106 ILE   B C    1 
ATOM   5526 C  C    B ILE   B 1 106 ? 32.379 -27.875 7.358   0.36 29.10 ?  106 ILE   B C    1 
ATOM   5527 O  O    A ILE   B 1 106 ? 32.506 -27.538 6.278   0.64 26.77 ?  106 ILE   B O    1 
ATOM   5528 O  O    B ILE   B 1 106 ? 32.465 -27.581 6.161   0.36 28.77 ?  106 ILE   B O    1 
ATOM   5529 C  CB   A ILE   B 1 106 ? 33.362 -30.176 7.820   0.64 29.16 ?  106 ILE   B CB   1 
ATOM   5530 C  CB   B ILE   B 1 106 ? 33.371 -30.201 7.650   0.36 30.33 ?  106 ILE   B CB   1 
ATOM   5531 C  CG1  A ILE   B 1 106 ? 33.612 -30.436 6.334   0.64 29.62 ?  106 ILE   B CG1  1 
ATOM   5532 C  CG1  B ILE   B 1 106 ? 33.667 -30.421 6.164   0.36 30.44 ?  106 ILE   B CG1  1 
ATOM   5533 C  CG2  A ILE   B 1 106 ? 31.993 -30.708 8.229   0.64 29.62 ?  106 ILE   B CG2  1 
ATOM   5534 C  CG2  B ILE   B 1 106 ? 31.995 -30.749 8.002   0.36 30.64 ?  106 ILE   B CG2  1 
ATOM   5535 C  CD1  A ILE   B 1 106 ? 34.985 -30.013 5.868   0.64 29.67 ?  106 ILE   B CD1  1 
ATOM   5536 C  CD1  B ILE   B 1 106 ? 35.034 -29.941 5.739   0.36 30.48 ?  106 ILE   B CD1  1 
ATOM   5537 H  H    A ILE   B 1 106 ? 33.341 -29.206 10.041  0.64 35.66 ?  106 ILE   B H    1 
ATOM   5538 H  H    B ILE   B 1 106 ? 33.327 -29.288 9.896   0.36 37.04 ?  106 ILE   B H    1 
ATOM   5539 H  HA   A ILE   B 1 106 ? 34.330 -28.359 7.810   0.64 34.28 ?  106 ILE   B HA   1 
ATOM   5540 H  HA   B ILE   B 1 106 ? 34.320 -28.372 7.692   0.36 36.02 ?  106 ILE   B HA   1 
ATOM   5541 H  HB   A ILE   B 1 106 ? 34.035 -30.653 8.330   0.64 34.98 ?  106 ILE   B HB   1 
ATOM   5542 H  HB   B ILE   B 1 106 ? 34.031 -30.687 8.166   0.36 36.37 ?  106 ILE   B HB   1 
ATOM   5543 H  HG12 A ILE   B 1 106 ? 33.525 -31.388 6.165   0.64 35.53 ?  106 ILE   B HG12 1 
ATOM   5544 H  HG12 B ILE   B 1 106 ? 33.618 -31.373 5.974   0.36 36.51 ?  106 ILE   B HG12 1 
ATOM   5545 H  HG13 A ILE   B 1 106 ? 32.957 -29.950 5.812   0.64 35.53 ?  106 ILE   B HG13 1 
ATOM   5546 H  HG13 B ILE   B 1 106 ? 33.008 -29.948 5.636   0.36 36.51 ?  106 ILE   B HG13 1 
ATOM   5547 H  HG21 A ILE   B 1 106 ? 31.996 -31.675 8.155   0.64 35.52 ?  106 ILE   B HG21 1 
ATOM   5548 H  HG21 B ILE   B 1 106 ? 32.011 -31.716 7.922   0.36 36.75 ?  106 ILE   B HG21 1 
ATOM   5549 H  HG22 A ILE   B 1 106 ? 31.815 -30.449 9.147   0.64 35.52 ?  106 ILE   B HG22 1 
ATOM   5550 H  HG22 B ILE   B 1 106 ? 31.780 -30.496 8.913   0.36 36.75 ?  106 ILE   B HG22 1 
ATOM   5551 H  HG23 A ILE   B 1 106 ? 31.318 -30.333 7.643   0.64 35.52 ?  106 ILE   B HG23 1 
ATOM   5552 H  HG23 B ILE   B 1 106 ? 31.338 -30.378 7.392   0.36 36.75 ?  106 ILE   B HG23 1 
ATOM   5553 H  HD11 A ILE   B 1 106 ? 35.163 -30.417 5.006   0.64 35.59 ?  106 ILE   B HD11 1 
ATOM   5554 H  HD11 B ILE   B 1 106 ? 35.257 -30.343 4.887   0.36 36.56 ?  106 ILE   B HD11 1 
ATOM   5555 H  HD12 A ILE   B 1 106 ? 35.009 -29.046 5.791   0.64 35.59 ?  106 ILE   B HD12 1 
ATOM   5556 H  HD12 B ILE   B 1 106 ? 35.017 -28.975 5.656   0.36 36.56 ?  106 ILE   B HD12 1 
ATOM   5557 H  HD13 A ILE   B 1 106 ? 35.644 -30.311 6.515   0.64 35.59 ?  106 ILE   B HD13 1 
ATOM   5558 H  HD13 B ILE   B 1 106 ? 35.683 -30.206 6.410   0.36 36.56 ?  106 ILE   B HD13 1 
ATOM   5559 N  N    A GLN   B 1 107 ? 31.343 -27.469 8.202   0.64 27.60 ?  107 GLN   B N    1 
ATOM   5560 N  N    B GLN   B 1 107 ? 31.345 -27.488 8.109   0.36 28.82 ?  107 GLN   B N    1 
ATOM   5561 C  CA   A GLN   B 1 107 ? 30.267 -26.679 7.611   0.64 27.72 ?  107 GLN   B CA   1 
ATOM   5562 C  CA   B GLN   B 1 107 ? 30.268 -26.682 7.545   0.36 28.53 ?  107 GLN   B CA   1 
ATOM   5563 C  C    A GLN   B 1 107 ? 30.757 -25.334 7.092   0.64 25.44 ?  107 GLN   B C    1 
ATOM   5564 C  C    B GLN   B 1 107 ? 30.751 -25.312 7.085   0.36 26.07 ?  107 GLN   B C    1 
ATOM   5565 O  O    A GLN   B 1 107 ? 30.122 -24.759 6.203   0.64 25.53 ?  107 GLN   B O    1 
ATOM   5566 O  O    B GLN   B 1 107 ? 30.098 -24.692 6.239   0.36 26.17 ?  107 GLN   B O    1 
ATOM   5567 C  CB   A GLN   B 1 107 ? 29.152 -26.468 8.639   0.64 31.19 ?  107 GLN   B CB   1 
ATOM   5568 C  CB   B GLN   B 1 107 ? 29.141 -26.533 8.571   0.36 31.08 ?  107 GLN   B CB   1 
ATOM   5569 C  CG   A GLN   B 1 107 ? 27.829 -25.975 8.059   0.64 34.43 ?  107 GLN   B CG   1 
ATOM   5570 C  CG   B GLN   B 1 107 ? 27.810 -26.061 7.996   0.36 33.42 ?  107 GLN   B CG   1 
ATOM   5571 C  CD   A GLN   B 1 107 ? 27.760 -24.462 7.933   0.64 36.93 ?  107 GLN   B CD   1 
ATOM   5572 C  CD   B GLN   B 1 107 ? 27.682 -24.549 7.966   0.36 35.28 ?  107 GLN   B CD   1 
ATOM   5573 O  OE1  A GLN   B 1 107 ? 28.593 -23.742 8.486   0.64 37.85 ?  107 GLN   B OE1  1 
ATOM   5574 O  OE1  B GLN   B 1 107 ? 28.490 -23.832 8.558   0.36 35.93 ?  107 GLN   B OE1  1 
ATOM   5575 N  NE2  A GLN   B 1 107 ? 26.759 -23.974 7.205   0.64 37.81 ?  107 GLN   B NE2  1 
ATOM   5576 N  NE2  B GLN   B 1 107 ? 26.658 -24.057 7.276   0.36 35.95 ?  107 GLN   B NE2  1 
ATOM   5577 H  H    A GLN   B 1 107 ? 31.237 -27.645 9.034   0.64 33.10 ?  107 GLN   B H    1 
ATOM   5578 H  H    B GLN   B 1 107 ? 31.243 -27.680 8.939   0.36 34.57 ?  107 GLN   B H    1 
ATOM   5579 H  HA   A GLN   B 1 107 ? 29.892 -27.172 6.863   0.64 33.25 ?  107 GLN   B HA   1 
ATOM   5580 H  HA   B GLN   B 1 107 ? 29.905 -27.144 6.774   0.36 34.22 ?  107 GLN   B HA   1 
ATOM   5581 H  HB2  A GLN   B 1 107 ? 28.979 -27.311 9.080   0.64 37.42 ?  107 GLN   B HB2  1 
ATOM   5582 H  HB2  B GLN   B 1 107 ? 28.989 -27.394 8.985   0.36 37.28 ?  107 GLN   B HB2  1 
ATOM   5583 H  HB3  A GLN   B 1 107 ? 29.451 -25.814 9.290   0.64 37.42 ?  107 GLN   B HB3  1 
ATOM   5584 H  HB3  B GLN   B 1 107 ? 29.417 -25.893 9.245   0.36 37.28 ?  107 GLN   B HB3  1 
ATOM   5585 H  HG2  A GLN   B 1 107 ? 27.709 -26.351 7.174   0.64 41.30 ?  107 GLN   B HG2  1 
ATOM   5586 H  HG2  B GLN   B 1 107 ? 27.724 -26.386 7.087   0.36 40.09 ?  107 GLN   B HG2  1 
ATOM   5587 H  HG3  A GLN   B 1 107 ? 27.104 -26.262 8.640   0.64 41.30 ?  107 GLN   B HG3  1 
ATOM   5588 H  HG3  B GLN   B 1 107 ? 27.088 -26.415 8.543   0.36 40.09 ?  107 GLN   B HG3  1 
ATOM   5589 H  HE21 A GLN   B 1 107 ? 26.196 -24.509 6.833   0.64 45.35 ?  107 GLN   B HE21 1 
ATOM   5590 H  HE21 B GLN   B 1 107 ? 26.114 -24.588 6.874   0.36 43.12 ?  107 GLN   B HE21 1 
ATOM   5591 H  HE22 A GLN   B 1 107 ? 26.672 -23.124 7.106   0.64 45.35 ?  107 GLN   B HE22 1 
ATOM   5592 H  HE22 B GLN   B 1 107 ? 26.540 -23.206 7.231   0.36 43.12 ?  107 GLN   B HE22 1 
ATOM   5593 N  N    . LEU   B 1 108 ? 31.879 -24.828 7.612   1.00 23.79 ?  108 LEU   B N    1 
ATOM   5594 C  CA   . LEU   B 1 108 ? 32.423 -23.531 7.204   1.00 20.74 ?  108 LEU   B CA   1 
ATOM   5595 C  C    . LEU   B 1 108 ? 33.077 -23.556 5.832   1.00 17.87 ?  108 LEU   B C    1 
ATOM   5596 O  O    . LEU   B 1 108 ? 33.505 -22.498 5.343   1.00 17.19 ?  108 LEU   B O    1 
ATOM   5597 C  CB   . LEU   B 1 108 ? 33.417 -23.028 8.250   1.00 21.31 ?  108 LEU   B CB   1 
ATOM   5598 C  CG   . LEU   B 1 108 ? 32.778 -22.530 9.547   1.00 22.76 ?  108 LEU   B CG   1 
ATOM   5599 C  CD1  . LEU   B 1 108 ? 33.802 -22.459 10.662  1.00 23.05 ?  108 LEU   B CD1  1 
ATOM   5600 C  CD2  . LEU   B 1 108 ? 32.148 -21.165 9.324   1.00 23.47 ?  108 LEU   B CD2  1 
ATOM   5601 H  H    A LEU   B 1 108 ? 32.337 -25.219 8.221   0.64 28.53 ?  108 LEU   B H    1 
ATOM   5602 H  H    B LEU   B 1 108 ? 32.339 -25.229 8.213   0.36 28.53 ?  108 LEU   B H    1 
ATOM   5603 H  HA   . LEU   B 1 108 ? 31.695 -22.896 7.165   1.00 24.87 ?  108 LEU   B HA   1 
ATOM   5604 H  HB2  . LEU   B 1 108 ? 34.017 -23.752 8.484   1.00 25.56 ?  108 LEU   B HB2  1 
ATOM   5605 H  HB3  . LEU   B 1 108 ? 33.920 -22.293 7.874   1.00 25.56 ?  108 LEU   B HB3  1 
ATOM   5606 H  HG   . LEU   B 1 108 ? 32.077 -23.145 9.819   1.00 27.29 ?  108 LEU   B HG   1 
ATOM   5607 H  HD11 . LEU   B 1 108 ? 33.359 -22.184 11.481  1.00 27.64 ?  108 LEU   B HD11 1 
ATOM   5608 H  HD12 . LEU   B 1 108 ? 34.201 -23.334 10.779  1.00 27.64 ?  108 LEU   B HD12 1 
ATOM   5609 H  HD13 . LEU   B 1 108 ? 34.483 -21.811 10.422  1.00 27.64 ?  108 LEU   B HD13 1 
ATOM   5610 H  HD21 . LEU   B 1 108 ? 31.806 -20.832 10.169  1.00 28.15 ?  108 LEU   B HD21 1 
ATOM   5611 H  HD22 . LEU   B 1 108 ? 32.822 -20.560 8.978   1.00 28.15 ?  108 LEU   B HD22 1 
ATOM   5612 H  HD23 . LEU   B 1 108 ? 31.422 -21.251 8.686   1.00 28.15 ?  108 LEU   B HD23 1 
ATOM   5613 N  N    . LEU   B 1 109 ? 33.130 -24.725 5.196   1.00 16.78 ?  109 LEU   B N    1 
ATOM   5614 C  CA   . LEU   B 1 109 ? 33.757 -24.837 3.887   1.00 15.71 ?  109 LEU   B CA   1 
ATOM   5615 C  C    . LEU   B 1 109 ? 32.990 -24.057 2.827   1.00 14.89 ?  109 LEU   B C    1 
ATOM   5616 O  O    . LEU   B 1 109 ? 33.607 -23.469 1.932   1.00 14.53 ?  109 LEU   B O    1 
ATOM   5617 C  CB   . LEU   B 1 109 ? 33.872 -26.311 3.507   1.00 16.00 ?  109 LEU   B CB   1 
ATOM   5618 C  CG   . LEU   B 1 109 ? 34.648 -26.660 2.239   1.00 15.59 ?  109 LEU   B CG   1 
ATOM   5619 C  CD1  . LEU   B 1 109 ? 36.025 -26.005 2.236   1.00 15.05 ?  109 LEU   B CD1  1 
ATOM   5620 C  CD2  . LEU   B 1 109 ? 34.779 -28.172 2.109   1.00 16.31 ?  109 LEU   B CD2  1 
ATOM   5621 H  H    . LEU   B 1 109 ? 32.818 -25.463 5.498   1.00 20.11 ?  109 LEU   B H    1 
ATOM   5622 H  HA   . LEU   B 1 109 ? 34.651 -24.474 3.931   1.00 18.84 ?  109 LEU   B HA   1 
ATOM   5623 H  HB2  . LEU   B 1 109 ? 34.310 -26.779 4.236   1.00 19.18 ?  109 LEU   B HB2  1 
ATOM   5624 H  HB3  . LEU   B 1 109 ? 32.976 -26.671 3.396   1.00 19.18 ?  109 LEU   B HB3  1 
ATOM   5625 H  HG   . LEU   B 1 109 ? 34.153 -26.344 1.462   1.00 18.69 ?  109 LEU   B HG   1 
ATOM   5626 H  HD11 . LEU   B 1 109 ? 36.547 -26.370 1.503   1.00 18.04 ?  109 LEU   B HD11 1 
ATOM   5627 H  HD12 . LEU   B 1 109 ? 35.915 -25.051 2.122   1.00 18.04 ?  109 LEU   B HD12 1 
ATOM   5628 H  HD13 . LEU   B 1 109 ? 36.462 -26.196 3.079   1.00 18.04 ?  109 LEU   B HD13 1 
ATOM   5629 H  HD21 . LEU   B 1 109 ? 35.352 -28.379 1.353   1.00 19.55 ?  109 LEU   B HD21 1 
ATOM   5630 H  HD22 . LEU   B 1 109 ? 35.165 -28.527 2.923   1.00 19.55 ?  109 LEU   B HD22 1 
ATOM   5631 H  HD23 . LEU   B 1 109 ? 33.897 -28.560 1.967   1.00 19.55 ?  109 LEU   B HD23 1 
ATOM   5632 N  N    . LYS   B 1 110 ? 31.655 -24.028 2.902   1.00 14.85 ?  110 LYS   B N    1 
ATOM   5633 C  CA   . LYS   B 1 110 ? 30.900 -23.267 1.910   1.00 14.76 ?  110 LYS   B CA   1 
ATOM   5634 C  C    . LYS   B 1 110 ? 31.241 -21.781 1.996   1.00 14.42 ?  110 LYS   B C    1 
ATOM   5635 O  O    . LYS   B 1 110 ? 31.491 -21.130 0.975   1.00 14.19 ?  110 LYS   B O    1 
ATOM   5636 C  CB   . LYS   B 1 110 ? 29.394 -23.511 2.065   1.00 15.22 ?  110 LYS   B CB   1 
ATOM   5637 C  CG   . LYS   B 1 110 ? 28.582 -22.893 0.930   1.00 15.75 ?  110 LYS   B CG   1 
ATOM   5638 C  CD   . LYS   B 1 110 ? 27.119 -23.329 0.965   1.00 15.99 ?  110 LYS   B CD   1 
ATOM   5639 C  CE   . LYS   B 1 110 ? 26.342 -22.806 -0.246  1.00 16.80 ?  110 LYS   B CE   1 
ATOM   5640 N  NZ   . LYS   B 1 110 ? 26.678 -23.518 -1.507  1.00 17.10 ?  110 LYS   B NZ   1 
ATOM   5641 H  H    . LYS   B 1 110 ? 31.183 -24.435 3.488   1.00 17.80 ?  110 LYS   B H    1 
ATOM   5642 H  HA   . LYS   B 1 110 ? 31.151 -23.572 1.022   1.00 17.69 ?  110 LYS   B HA   1 
ATOM   5643 H  HB2  . LYS   B 1 110 ? 29.226 -24.470 2.066   1.00 18.25 ?  110 LYS   B HB2  1 
ATOM   5644 H  HB3  . LYS   B 1 110 ? 29.092 -23.123 2.899   1.00 18.25 ?  110 LYS   B HB3  1 
ATOM   5645 H  HG2  . LYS   B 1 110 ? 28.601 -21.928 1.010   1.00 18.88 ?  110 LYS   B HG2  1 
ATOM   5646 H  HG3  . LYS   B 1 110 ? 28.952 -23.169 0.080   1.00 18.88 ?  110 LYS   B HG3  1 
ATOM   5647 H  HD2  . LYS   B 1 110 ? 27.071 -24.303 0.957   1.00 19.18 ?  110 LYS   B HD2  1 
ATOM   5648 H  HD3  . LYS   B 1 110 ? 26.695 -22.986 1.770   1.00 19.18 ?  110 LYS   B HD3  1 
ATOM   5649 H  HE2  . LYS   B 1 110 ? 25.392 -22.914 -0.087  1.00 20.15 ?  110 LYS   B HE2  1 
ATOM   5650 H  HE3  . LYS   B 1 110 ? 26.553 -21.867 -0.369  1.00 20.15 ?  110 LYS   B HE3  1 
ATOM   5651 H  HZ1  . LYS   B 1 110 ? 26.211 -23.182 -2.183  1.00 20.50 ?  110 LYS   B HZ1  1 
ATOM   5652 H  HZ2  . LYS   B 1 110 ? 27.549 -23.430 -1.684  1.00 20.50 ?  110 LYS   B HZ2  1 
ATOM   5653 H  HZ3  . LYS   B 1 110 ? 26.490 -24.386 -1.427  1.00 20.50 ?  110 LYS   B HZ3  1 
ATOM   5654 N  N    . SER   B 1 111 ? 31.263 -21.230 3.217   1.00 14.98 ?  111 SER   B N    1 
ATOM   5655 C  CA   . SER   B 1 111 ? 31.656 -19.835 3.401   1.00 14.87 ?  111 SER   B CA   1 
ATOM   5656 C  C    . SER   B 1 111 ? 33.032 -19.573 2.806   1.00 14.02 ?  111 SER   B C    1 
ATOM   5657 O  O    . SER   B 1 111 ? 33.251 -18.541 2.153   1.00 14.02 ?  111 SER   B O    1 
ATOM   5658 C  CB   . SER   B 1 111 ? 31.652 -19.484 4.889   1.00 16.01 ?  111 SER   B CB   1 
ATOM   5659 O  OG   . SER   B 1 111 ? 30.348 -19.469 5.422   1.00 17.57 ?  111 SER   B OG   1 
ATOM   5660 H  H    . SER   B 1 111 ? 31.061 -21.649 3.941   1.00 17.96 ?  111 SER   B H    1 
ATOM   5661 H  HA   . SER   B 1 111 ? 31.019 -19.264 2.953   1.00 17.83 ?  111 SER   B HA   1 
ATOM   5662 H  HB2  . SER   B 1 111 ? 32.172 -20.150 5.372   1.00 19.20 ?  111 SER   B HB2  1 
ATOM   5663 H  HB3  . SER   B 1 111 ? 32.044 -18.611 5.008   1.00 19.20 ?  111 SER   B HB3  1 
ATOM   5664 H  HG   . SER   B 1 111 ? 30.368 -19.276 6.246   1.00 21.07 ?  111 SER   B HG   1 
ATOM   5665 N  N    . ALA   B 1 112 ? 33.974 -20.492 3.027   1.00 14.17 ?  112 ALA   B N    1 
ATOM   5666 C  CA   . ALA   B 1 112 ? 35.317 -20.317 2.486   1.00 13.86 ?  112 ALA   B CA   1 
ATOM   5667 C  C    . ALA   B 1 112 ? 35.287 -20.222 0.964   1.00 13.23 ?  112 ALA   B C    1 
ATOM   5668 O  O    . ALA   B 1 112 ? 35.909 -19.330 0.371   1.00 13.43 ?  112 ALA   B O    1 
ATOM   5669 C  CB   . ALA   B 1 112 ? 36.221 -21.456 2.963   1.00 14.30 ?  112 ALA   B CB   1 
ATOM   5670 H  H    . ALA   B 1 112 ? 33.860 -21.217 3.492   1.00 16.99 ?  112 ALA   B H    1 
ATOM   5671 H  HA   . ALA   B 1 112 ? 35.679 -19.487 2.831   1.00 16.62 ?  112 ALA   B HA   1 
ATOM   5672 H  HB1  . ALA   B 1 112 ? 37.112 -21.318 2.599   1.00 17.14 ?  112 ALA   B HB1  1 
ATOM   5673 H  HB2  . ALA   B 1 112 ? 36.261 -21.444 3.935   1.00 17.14 ?  112 ALA   B HB2  1 
ATOM   5674 H  HB3  . ALA   B 1 112 ? 35.862 -22.298 2.657   1.00 17.14 ?  112 ALA   B HB3  1 
ATOM   5675 N  N    . TYR   B 1 113 ? 34.556 -21.130 0.308   1.00 13.18 ?  113 TYR   B N    1 
ATOM   5676 C  CA   . TYR   B 1 113 ? 34.479 -21.087 -1.148  1.00 12.98 ?  113 TYR   B CA   1 
ATOM   5677 C  C    . TYR   B 1 113 ? 33.764 -19.837 -1.661  1.00 12.83 ?  113 TYR   B C    1 
ATOM   5678 O  O    . TYR   B 1 113 ? 34.030 -19.404 -2.787  1.00 12.82 ?  113 TYR   B O    1 
ATOM   5679 C  CB   . TYR   B 1 113 ? 33.804 -22.345 -1.694  1.00 13.11 ?  113 TYR   B CB   1 
ATOM   5680 C  CG   . TYR   B 1 113 ? 34.765 -23.493 -1.949  1.00 13.44 ?  113 TYR   B CG   1 
ATOM   5681 C  CD1  . TYR   B 1 113 ? 35.770 -23.390 -2.903  1.00 14.08 ?  113 TYR   B CD1  1 
ATOM   5682 C  CD2  . TYR   B 1 113 ? 34.657 -24.683 -1.248  1.00 13.64 ?  113 TYR   B CD2  1 
ATOM   5683 C  CE1  . TYR   B 1 113 ? 36.653 -24.428 -3.137  1.00 13.99 ?  113 TYR   B CE1  1 
ATOM   5684 C  CE2  . TYR   B 1 113 ? 35.533 -25.735 -1.482  1.00 14.06 ?  113 TYR   B CE2  1 
ATOM   5685 C  CZ   . TYR   B 1 113 ? 36.520 -25.604 -2.433  1.00 13.92 ?  113 TYR   B CZ   1 
ATOM   5686 O  OH   . TYR   B 1 113 ? 37.406 -26.619 -2.696  1.00 14.90 ?  113 TYR   B OH   1 
ATOM   5687 H  H    . TYR   B 1 113 ? 34.094 -21.762 0.680   1.00 15.80 ?  113 TYR   B H    1 
ATOM   5688 H  HA   . TYR   B 1 113 ? 35.384 -21.067 -1.487  1.00 15.56 ?  113 TYR   B HA   1 
ATOM   5689 H  HB2  . TYR   B 1 113 ? 33.142 -22.653 -1.053  1.00 15.72 ?  113 TYR   B HB2  1 
ATOM   5690 H  HB3  . TYR   B 1 113 ? 33.371 -22.127 -2.533  1.00 15.72 ?  113 TYR   B HB3  1 
ATOM   5691 H  HD1  . TYR   B 1 113 ? 35.862 -22.597 -3.382  1.00 16.88 ?  113 TYR   B HD1  1 
ATOM   5692 H  HD2  . TYR   B 1 113 ? 33.985 -24.779 -0.614  1.00 16.35 ?  113 TYR   B HD2  1 
ATOM   5693 H  HE1  . TYR   B 1 113 ? 37.318 -24.341 -3.783  1.00 16.77 ?  113 TYR   B HE1  1 
ATOM   5694 H  HE2  . TYR   B 1 113 ? 35.441 -26.534 -1.011  1.00 16.85 ?  113 TYR   B HE2  1 
ATOM   5695 H  HH   . TYR   B 1 113 ? 37.223 -27.288 -2.221  1.00 17.87 ?  113 TYR   B HH   1 
ATOM   5696 N  N    . GLU   B 1 114 ? 32.841 -19.262 -0.880  1.00 12.88 ?  114 GLU   B N    1 
ATOM   5697 C  CA   . GLU   B 1 114 ? 32.155 -18.053 -1.334  1.00 12.81 ?  114 GLU   B CA   1 
ATOM   5698 C  C    . GLU   B 1 114 ? 33.140 -16.930 -1.636  1.00 12.62 ?  114 GLU   B C    1 
ATOM   5699 O  O    . GLU   B 1 114 ? 32.861 -16.070 -2.474  1.00 12.85 ?  114 GLU   B O    1 
ATOM   5700 C  CB   . GLU   B 1 114 ? 31.100 -17.626 -0.313  1.00 13.17 ?  114 GLU   B CB   1 
ATOM   5701 C  CG   . GLU   B 1 114 ? 29.878 -18.542 -0.384  1.00 13.35 ?  114 GLU   B CG   1 
ATOM   5702 C  CD   . GLU   B 1 114 ? 28.863 -18.356 0.726   1.00 13.60 ?  114 GLU   B CD   1 
ATOM   5703 O  OE1  . GLU   B 1 114 ? 29.149 -17.742 1.771   1.00 13.84 ?  114 GLU   B OE1  1 
ATOM   5704 O  OE2  . GLU   B 1 114 ? 27.741 -18.895 0.564   1.00 14.69 -1 114 GLU   B OE2  1 
ATOM   5705 H  H    . GLU   B 1 114 ? 32.599 -19.556 -0.108  1.00 15.44 ?  114 GLU   B H    1 
ATOM   5706 H  HA   . GLU   B 1 114 ? 31.699 -18.257 -2.157  1.00 15.35 ?  114 GLU   B HA   1 
ATOM   5707 H  HB2  . GLU   B 1 114 ? 31.473 -17.683 0.583   1.00 15.78 ?  114 GLU   B HB2  1 
ATOM   5708 H  HB3  . GLU   B 1 114 ? 30.816 -16.722 -0.504  1.00 15.78 ?  114 GLU   B HB3  1 
ATOM   5709 H  HG2  . GLU   B 1 114 ? 29.426 -18.381 -1.222  1.00 16.00 ?  114 GLU   B HG2  1 
ATOM   5710 H  HG3  . GLU   B 1 114 ? 30.183 -19.462 -0.347  1.00 16.00 ?  114 GLU   B HG3  1 
ATOM   5711 N  N    . ASN   B 1 115 ? 34.305 -16.921 -0.984  1.00 12.47 ?  115 ASN   B N    1 
ATOM   5712 C  CA   . ASN   B 1 115 ? 35.296 -15.887 -1.287  1.00 11.96 ?  115 ASN   B CA   1 
ATOM   5713 C  C    . ASN   B 1 115 ? 35.709 -15.913 -2.752  1.00 12.01 ?  115 ASN   B C    1 
ATOM   5714 O  O    . ASN   B 1 115 ? 36.098 -14.876 -3.309  1.00 12.64 ?  115 ASN   B O    1 
ATOM   5715 C  CB   . ASN   B 1 115 ? 36.535 -16.061 -0.405  1.00 12.88 ?  115 ASN   B CB   1 
ATOM   5716 C  CG   . ASN   B 1 115 ? 36.265 -15.796 1.058   1.00 13.26 ?  115 ASN   B CG   1 
ATOM   5717 O  OD1  . ASN   B 1 115 ? 36.266 -14.650 1.504   1.00 15.15 ?  115 ASN   B OD1  1 
ATOM   5718 N  ND2  . ASN   B 1 115 ? 36.106 -16.866 1.834   1.00 13.51 ?  115 ASN   B ND2  1 
ATOM   5719 H  H    . ASN   B 1 115 ? 34.545 -17.477 -0.365  1.00 14.95 ?  115 ASN   B H    1 
ATOM   5720 H  HA   . ASN   B 1 115 ? 34.918 -15.015 -1.094  1.00 14.34 ?  115 ASN   B HA   1 
ATOM   5721 H  HB2  . ASN   B 1 115 ? 36.865 -16.970 -0.492  1.00 15.44 ?  115 ASN   B HB2  1 
ATOM   5722 H  HB3  . ASN   B 1 115 ? 37.222 -15.435 -0.695  1.00 15.44 ?  115 ASN   B HB3  1 
ATOM   5723 H  HD21 . ASN   B 1 115 ? 35.960 -16.768 2.676   1.00 16.20 ?  115 ASN   B HD21 1 
ATOM   5724 H  HD22 . ASN   B 1 115 ? 36.130 -17.655 1.491   1.00 16.20 ?  115 ASN   B HD22 1 
ATOM   5725 N  N    . PHE   B 1 116 ? 35.679 -17.091 -3.383  1.00 11.95 ?  116 PHE   B N    1 
ATOM   5726 C  CA   . PHE   B 1 116 ? 36.113 -17.189 -4.772  1.00 12.27 ?  116 PHE   B CA   1 
ATOM   5727 C  C    . PHE   B 1 116 ? 35.210 -16.368 -5.688  1.00 12.06 ?  116 PHE   B C    1 
ATOM   5728 O  O    . PHE   B 1 116 ? 35.644 -15.932 -6.761  1.00 12.62 ?  116 PHE   B O    1 
ATOM   5729 C  CB   . PHE   B 1 116 ? 36.075 -18.636 -5.288  1.00 11.83 ?  116 PHE   B CB   1 
ATOM   5730 C  CG   . PHE   B 1 116 ? 37.150 -19.585 -4.744  1.00 11.83 ?  116 PHE   B CG   1 
ATOM   5731 C  CD1  . PHE   B 1 116 ? 37.793 -19.405 -3.537  1.00 12.63 ?  116 PHE   B CD1  1 
ATOM   5732 C  CD2  . PHE   B 1 116 ? 37.446 -20.725 -5.474  1.00 12.34 ?  116 PHE   B CD2  1 
ATOM   5733 C  CE1  . PHE   B 1 116 ? 38.733 -20.342 -3.086  1.00 12.92 ?  116 PHE   B CE1  1 
ATOM   5734 C  CE2  . PHE   B 1 116 ? 38.377 -21.664 -5.030  1.00 12.26 ?  116 PHE   B CE2  1 
ATOM   5735 C  CZ   . PHE   B 1 116 ? 39.012 -21.475 -3.839  1.00 12.08 ?  116 PHE   B CZ   1 
ATOM   5736 H  H    . PHE   B 1 116 ? 35.413 -17.836 -3.032  1.00 14.32 ?  116 PHE   B H    1 
ATOM   5737 H  HA   . PHE   B 1 116 ? 37.019 -16.861 -4.850  1.00 14.71 ?  116 PHE   B HA   1 
ATOM   5738 H  HB2  . PHE   B 1 116 ? 35.207 -19.018 -5.058  1.00 14.18 ?  116 PHE   B HB2  1 
ATOM   5739 H  HB3  . PHE   B 1 116 ? 36.166 -18.617 -6.252  1.00 14.18 ?  116 PHE   B HB3  1 
ATOM   5740 H  HD1  . PHE   B 1 116 ? 37.595 -18.652 -3.019  1.00 15.14 ?  116 PHE   B HD1  1 
ATOM   5741 H  HD2  . PHE   B 1 116 ? 37.008 -20.872 -6.282  1.00 14.79 ?  116 PHE   B HD2  1 
ATOM   5742 H  HE1  . PHE   B 1 116 ? 39.163 -20.200 -2.274  1.00 15.49 ?  116 PHE   B HE1  1 
ATOM   5743 H  HE2  . PHE   B 1 116 ? 38.562 -22.409 -5.548  1.00 14.70 ?  116 PHE   B HE2  1 
ATOM   5744 H  HZ   . PHE   B 1 116 ? 39.646 -22.082 -3.545  1.00 14.48 ?  116 PHE   B HZ   1 
ATOM   5745 N  N    . ASN   B 1 117 ? 33.940 -16.167 -5.304  1.00 12.53 ?  117 ASN   B N    1 
ATOM   5746 C  CA   . ASN   B 1 117 ? 32.993 -15.459 -6.166  1.00 12.66 ?  117 ASN   B CA   1 
ATOM   5747 C  C    . ASN   B 1 117 ? 33.311 -13.981 -6.320  1.00 13.18 ?  117 ASN   B C    1 
ATOM   5748 O  O    . ASN   B 1 117 ? 32.710 -13.326 -7.175  1.00 14.39 ?  117 ASN   B O    1 
ATOM   5749 C  CB   . ASN   B 1 117 ? 31.571 -15.680 -5.668  1.00 12.96 ?  117 ASN   B CB   1 
ATOM   5750 C  CG   . ASN   B 1 117 ? 31.115 -17.084 -5.923  1.00 13.60 ?  117 ASN   B CG   1 
ATOM   5751 O  OD1  . ASN   B 1 117 ? 31.474 -17.678 -6.941  1.00 14.28 ?  117 ASN   B OD1  1 
ATOM   5752 N  ND2  . ASN   B 1 117 ? 30.375 -17.653 -4.987  1.00 13.65 ?  117 ASN   B ND2  1 
ATOM   5753 H  H    . ASN   B 1 117 ? 33.611 -16.431 -4.547  1.00 15.02 ?  117 ASN   B H    1 
ATOM   5754 H  HA   . ASN   B 1 117 ? 33.051 -15.860 -7.043  1.00 15.18 ?  117 ASN   B HA   1 
ATOM   5755 H  HB2  . ASN   B 1 117 ? 31.535 -15.519 -4.708  1.00 15.53 ?  117 ASN   B HB2  1 
ATOM   5756 H  HB3  . ASN   B 1 117 ? 30.975 -15.069 -6.129  1.00 15.53 ?  117 ASN   B HB3  1 
ATOM   5757 H  HD21 . ASN   B 1 117 ? 30.088 -18.457 -5.092  1.00 16.37 ?  117 ASN   B HD21 1 
ATOM   5758 H  HD22 . ASN   B 1 117 ? 30.150 -17.207 -4.284  1.00 16.37 ?  117 ASN   B HD22 1 
ATOM   5759 N  N    . GLN   B 1 118 ? 34.247 -13.456 -5.542  1.00 12.79 ?  118 GLN   B N    1 
ATOM   5760 C  CA   . GLN   B 1 118 ? 34.673 -12.072 -5.683  1.00 13.50 ?  118 GLN   B CA   1 
ATOM   5761 C  C    . GLN   B 1 118 ? 35.743 -11.883 -6.753  1.00 13.50 ?  118 GLN   B C    1 
ATOM   5762 O  O    . GLN   B 1 118 ? 36.211 -10.753 -6.937  1.00 14.80 ?  118 GLN   B O    1 
ATOM   5763 C  CB   . GLN   B 1 118 ? 35.143 -11.533 -4.328  1.00 14.06 ?  118 GLN   B CB   1 
ATOM   5764 C  CG   . GLN   B 1 118 ? 34.064 -11.577 -3.258  1.00 14.11 ?  118 GLN   B CG   1 
ATOM   5765 C  CD   . GLN   B 1 118 ? 32.893 -10.669 -3.586  1.00 14.08 ?  118 GLN   B CD   1 
ATOM   5766 O  OE1  . GLN   B 1 118 ? 33.080 -9.531  -4.026  1.00 14.84 ?  118 GLN   B OE1  1 
ATOM   5767 N  NE2  . GLN   B 1 118 ? 31.678 -11.163 -3.381  1.00 14.50 ?  118 GLN   B NE2  1 
ATOM   5768 H  H    . GLN   B 1 118 ? 34.666 -13.883 -4.921  1.00 15.33 ?  118 GLN   B H    1 
ATOM   5769 H  HA   . GLN   B 1 118 ? 33.908 -11.543 -5.959  1.00 16.18 ?  118 GLN   B HA   1 
ATOM   5770 H  HB2  . GLN   B 1 118 ? 35.891 -12.058 -4.021  1.00 16.85 ?  118 GLN   B HB2  1 
ATOM   5771 H  HB3  . GLN   B 1 118 ? 35.411 -10.603 -4.436  1.00 16.85 ?  118 GLN   B HB3  1 
ATOM   5772 H  HG2  . GLN   B 1 118 ? 33.729 -12.486 -3.181  1.00 16.92 ?  118 GLN   B HG2  1 
ATOM   5773 H  HG3  . GLN   B 1 118 ? 34.441 -11.289 -2.413  1.00 16.92 ?  118 GLN   B HG3  1 
ATOM   5774 H  HE21 . GLN   B 1 118 ? 31.586 -11.961 -3.072  1.00 17.38 ?  118 GLN   B HE21 1 
ATOM   5775 H  HE22 . GLN   B 1 118 ? 30.990 -10.683 -3.552  1.00 17.38 ?  118 GLN   B HE22 1 
ATOM   5776 N  N    . HIS   B 1 119 ? 36.097 -12.940 -7.486  1.00 12.78 ?  119 HIS   B N    1 
ATOM   5777 C  CA   . HIS   B 1 119 ? 37.142 -12.893 -8.501  1.00 13.14 ?  119 HIS   B CA   1 
ATOM   5778 C  C    . HIS   B 1 119 ? 36.667 -13.622 -9.742  1.00 12.88 ?  119 HIS   B C    1 
ATOM   5779 O  O    . HIS   B 1 119 ? 36.160 -14.739 -9.645  1.00 13.87 ?  119 HIS   B O    1 
ATOM   5780 C  CB   . HIS   B 1 119 ? 38.423 -13.524 -7.951  1.00 13.60 ?  119 HIS   B CB   1 
ATOM   5781 C  CG   . HIS   B 1 119 ? 38.903 -12.828 -6.724  1.00 14.42 ?  119 HIS   B CG   1 
ATOM   5782 N  ND1  . HIS   B 1 119 ? 39.702 -11.706 -6.775  1.00 16.04 ?  119 HIS   B ND1  1 
ATOM   5783 C  CD2  . HIS   B 1 119 ? 38.610 -13.028 -5.419  1.00 15.43 ?  119 HIS   B CD2  1 
ATOM   5784 C  CE1  . HIS   B 1 119 ? 39.912 -11.270 -5.547  1.00 16.89 ?  119 HIS   B CE1  1 
ATOM   5785 N  NE2  . HIS   B 1 119 ? 39.253 -12.046 -4.706  1.00 16.78 ?  119 HIS   B NE2  1 
ATOM   5786 H  H    . HIS   B 1 119 ? 35.724 -13.719 -7.417  1.00 15.32 ?  119 HIS   B H    1 
ATOM   5787 H  HA   . HIS   B 1 119 ? 37.323 -11.965 -8.733  1.00 15.75 ?  119 HIS   B HA   1 
ATOM   5788 H  HB2  . HIS   B 1 119 ? 38.249 -14.450 -7.728  1.00 16.31 ?  119 HIS   B HB2  1 
ATOM   5789 H  HB3  . HIS   B 1 119 ? 39.119 -13.465 -8.625  1.00 16.31 ?  119 HIS   B HB3  1 
ATOM   5790 H  HD2  . HIS   B 1 119 ? 38.079 -13.707 -5.069  1.00 18.50 ?  119 HIS   B HD2  1 
ATOM   5791 H  HE1  . HIS   B 1 119 ? 40.446 -10.546 -5.309  1.00 20.25 ?  119 HIS   B HE1  1 
ATOM   5792 H  HE2  . HIS   B 1 119 ? 39.261 -11.977 -3.847  1.00 20.12 ?  119 HIS   B HE2  1 
ATOM   5793 N  N    . GLU   B 1 120 ? 36.818 -12.999 -10.909 1.00 13.58 ?  120 GLU   B N    1 
ATOM   5794 C  CA   . GLU   B 1 120 ? 36.236 -13.581 -12.115 1.00 15.53 ?  120 GLU   B CA   1 
ATOM   5795 C  C    . GLU   B 1 120 ? 36.910 -14.889 -12.524 1.00 14.13 ?  120 GLU   B C    1 
ATOM   5796 O  O    . GLU   B 1 120 ? 36.249 -15.763 -13.095 1.00 14.44 ?  120 GLU   B O    1 
ATOM   5797 C  CB   . GLU   B 1 120 ? 36.254 -12.570 -13.260 1.00 20.27 ?  120 GLU   B CB   1 
ATOM   5798 C  CG   . GLU   B 1 120 ? 35.291 -11.412 -13.050 1.00 26.57 ?  120 GLU   B CG   1 
ATOM   5799 C  CD   . GLU   B 1 120 ? 35.156 -10.528 -14.274 1.00 32.59 ?  120 GLU   B CD   1 
ATOM   5800 O  OE1  . GLU   B 1 120 ? 36.155 -10.362 -15.006 1.00 34.68 ?  120 GLU   B OE1  1 
ATOM   5801 O  OE2  . GLU   B 1 120 ? 34.046 -10.003 -14.506 1.00 35.37 -1 120 GLU   B OE2  1 
ATOM   5802 H  H    . GLU   B 1 120 ? 37.232 -12.250 -11.025 1.00 16.28 ?  120 GLU   B H    1 
ATOM   5803 H  HA   . GLU   B 1 120 ? 35.308 -13.784 -11.932 1.00 18.63 ?  120 GLU   B HA   1 
ATOM   5804 H  HB2  . GLU   B 1 120 ? 37.143 -12.200 -13.349 1.00 24.31 ?  120 GLU   B HB2  1 
ATOM   5805 H  HB3  . GLU   B 1 120 ? 35.996 -13.019 -14.082 1.00 24.31 ?  120 GLU   B HB3  1 
ATOM   5806 H  HG2  . GLU   B 1 120 ? 34.407 -11.762 -12.849 1.00 31.87 ?  120 GLU   B HG2  1 
ATOM   5807 H  HG3  . GLU   B 1 120 ? 35.604 -10.865 -12.313 1.00 31.87 ?  120 GLU   B HG3  1 
ATOM   5808 N  N    . VAL   B 1 121 ? 38.210 -15.033 -12.269 1.00 13.38 ?  121 VAL   B N    1 
ATOM   5809 C  CA   . VAL   B 1 121 ? 38.958 -16.242 -12.615 1.00 13.35 ?  121 VAL   B CA   1 
ATOM   5810 C  C    . VAL   B 1 121 ? 40.068 -16.445 -11.593 1.00 12.78 ?  121 VAL   B C    1 
ATOM   5811 O  O    . VAL   B 1 121 ? 40.747 -15.489 -11.200 1.00 13.34 ?  121 VAL   B O    1 
ATOM   5812 C  CB   . VAL   B 1 121 ? 39.478 -16.196 -14.072 1.00 15.44 ?  121 VAL   B CB   1 
ATOM   5813 C  CG1  . VAL   B 1 121 ? 40.342 -14.962 -14.319 1.00 16.62 ?  121 VAL   B CG1  1 
ATOM   5814 C  CG2  . VAL   B 1 121 ? 40.225 -17.482 -14.430 1.00 16.86 ?  121 VAL   B CG2  1 
ATOM   5815 H  H    . VAL   B 1 121 ? 38.697 -14.423 -11.905 1.00 16.04 ?  121 VAL   B H    1 
ATOM   5816 H  HA   . VAL   B 1 121 ? 38.349 -16.994 -12.552 1.00 16.01 ?  121 VAL   B HA   1 
ATOM   5817 H  HB   . VAL   B 1 121 ? 38.713 -16.137 -14.670 1.00 18.51 ?  121 VAL   B HB   1 
ATOM   5818 H  HG11 . VAL   B 1 121 ? 40.659 -14.976 -15.235 1.00 19.93 ?  121 VAL   B HG11 1 
ATOM   5819 H  HG12 . VAL   B 1 121 ? 39.808 -14.167 -14.167 1.00 19.93 ?  121 VAL   B HG12 1 
ATOM   5820 H  HG13 . VAL   B 1 121 ? 41.095 -14.977 -13.708 1.00 19.93 ?  121 VAL   B HG13 1 
ATOM   5821 H  HG21 . VAL   B 1 121 ? 40.441 -17.470 -15.379 1.00 20.22 ?  121 VAL   B HG21 1 
ATOM   5822 H  HG22 . VAL   B 1 121 ? 41.043 -17.532 -13.910 1.00 20.22 ?  121 VAL   B HG22 1 
ATOM   5823 H  HG23 . VAL   B 1 121 ? 39.660 -18.246 -14.234 1.00 20.22 ?  121 VAL   B HG23 1 
ATOM   5824 N  N    . LEU   B 1 122 ? 40.244 -17.697 -11.158 1.00 12.17 ?  122 LEU   B N    1 
ATOM   5825 C  CA   . LEU   B 1 122 ? 41.225 -18.048 -10.136 1.00 12.05 ?  122 LEU   B CA   1 
ATOM   5826 C  C    . LEU   B 1 122 ? 41.878 -19.380 -10.463 1.00 11.86 ?  122 LEU   B C    1 
ATOM   5827 O  O    . LEU   B 1 122 ? 41.216 -20.301 -10.964 1.00 13.04 ?  122 LEU   B O    1 
ATOM   5828 C  CB   . LEU   B 1 122 ? 40.572 -18.276 -8.757  1.00 14.07 ?  122 LEU   B CB   1 
ATOM   5829 C  CG   . LEU   B 1 122 ? 39.543 -17.253 -8.264  1.00 13.80 ?  122 LEU   B CG   1 
ATOM   5830 C  CD1  . LEU   B 1 122 ? 38.153 -17.612 -8.749  1.00 14.88 ?  122 LEU   B CD1  1 
ATOM   5831 C  CD2  . LEU   B 1 122 ? 39.572 -17.146 -6.753  1.00 13.34 ?  122 LEU   B CD2  1 
ATOM   5832 H  H    . LEU   B 1 122 ? 39.795 -18.372 -11.445 1.00 14.58 ?  122 LEU   B H    1 
ATOM   5833 H  HA   . LEU   B 1 122 ? 41.900 -17.357 -10.057 1.00 14.45 ?  122 LEU   B HA   1 
ATOM   5834 H  HB2  . LEU   B 1 122 ? 40.123 -19.136 -8.778  1.00 16.87 ?  122 LEU   B HB2  1 
ATOM   5835 H  HB3  . LEU   B 1 122 ? 41.277 -18.304 -8.093  1.00 16.87 ?  122 LEU   B HB3  1 
ATOM   5836 H  HG   . LEU   B 1 122 ? 39.768 -16.384 -8.625  1.00 16.55 ?  122 LEU   B HG   1 
ATOM   5837 H  HD11 . LEU   B 1 122 ? 37.519 -16.975 -8.384  1.00 17.83 ?  122 LEU   B HD11 1 
ATOM   5838 H  HD12 . LEU   B 1 122 ? 38.137 -17.574 -9.719  1.00 17.83 ?  122 LEU   B HD12 1 
ATOM   5839 H  HD13 . LEU   B 1 122 ? 37.934 -18.506 -8.449  1.00 17.83 ?  122 LEU   B HD13 1 
ATOM   5840 H  HD21 . LEU   B 1 122 ? 38.897 -16.511 -6.464  1.00 16.00 ?  122 LEU   B HD21 1 
ATOM   5841 H  HD22 . LEU   B 1 122 ? 39.390 -18.019 -6.367  1.00 16.00 ?  122 LEU   B HD22 1 
ATOM   5842 H  HD23 . LEU   B 1 122 ? 40.451 -16.841 -6.472  1.00 16.00 ?  122 LEU   B HD23 1 
ATOM   5843 N  N    . LEU   B 1 123 ? 43.165 -19.486 -10.104 1.00 11.71 ?  123 LEU   B N    1 
ATOM   5844 C  CA   . LEU   B 1 123 ? 43.875 -20.755 -9.978  1.00 11.68 ?  123 LEU   B CA   1 
ATOM   5845 C  C    . LEU   B 1 123 ? 43.846 -21.147 -8.506  1.00 11.35 ?  123 LEU   B C    1 
ATOM   5846 O  O    . LEU   B 1 123 ? 44.196 -20.324 -7.653  1.00 11.88 ?  123 LEU   B O    1 
ATOM   5847 C  CB   . LEU   B 1 123 ? 45.323 -20.580 -10.441 1.00 12.15 ?  123 LEU   B CB   1 
ATOM   5848 C  CG   . LEU   B 1 123 ? 46.265 -21.764 -10.205 1.00 12.71 ?  123 LEU   B CG   1 
ATOM   5849 C  CD1  . LEU   B 1 123 ? 45.844 -23.009 -10.986 1.00 13.22 ?  123 LEU   B CD1  1 
ATOM   5850 C  CD2  . LEU   B 1 123 ? 47.678 -21.360 -10.575 1.00 13.29 ?  123 LEU   B CD2  1 
ATOM   5851 H  H    . LEU   B 1 123 ? 43.660 -18.806 -9.915  1.00 14.04 ?  123 LEU   B H    1 
ATOM   5852 H  HA   . LEU   B 1 123 ? 43.434 -21.444 -10.505 1.00 14.00 ?  123 LEU   B HA   1 
ATOM   5853 H  HB2  . LEU   B 1 123 ? 45.310 -20.408 -11.394 1.00 14.56 ?  123 LEU   B HB2  1 
ATOM   5854 H  HB3  . LEU   B 1 123 ? 45.695 -19.820 -9.977  1.00 14.56 ?  123 LEU   B HB3  1 
ATOM   5855 H  HG   . LEU   B 1 123 ? 46.259 -21.993 -9.263  1.00 15.23 ?  123 LEU   B HG   1 
ATOM   5856 H  HD11 . LEU   B 1 123 ? 46.481 -23.719 -10.810 1.00 15.85 ?  123 LEU   B HD11 1 
ATOM   5857 H  HD12 . LEU   B 1 123 ? 44.958 -23.278 -10.700 1.00 15.85 ?  123 LEU   B HD12 1 
ATOM   5858 H  HD13 . LEU   B 1 123 ? 45.838 -22.798 -11.933 1.00 15.85 ?  123 LEU   B HD13 1 
ATOM   5859 H  HD21 . LEU   B 1 123 ? 48.272 -22.111 -10.429 1.00 15.93 ?  123 LEU   B HD21 1 
ATOM   5860 H  HD22 . LEU   B 1 123 ? 47.697 -21.099 -11.511 1.00 15.93 ?  123 LEU   B HD22 1 
ATOM   5861 H  HD23 . LEU   B 1 123 ? 47.946 -20.610 -10.019 1.00 15.93 ?  123 LEU   B HD23 1 
ATOM   5862 N  N    . ALA   B 1 124 ? 43.414 -22.377 -8.197  1.00 11.26 ?  124 ALA   B N    1 
ATOM   5863 C  CA   . ALA   B 1 124 ? 43.159 -22.694 -6.800  1.00 11.33 ?  124 ALA   B CA   1 
ATOM   5864 C  C    . ALA   B 1 124 ? 43.428 -24.154 -6.467  1.00 11.06 ?  124 ALA   B C    1 
ATOM   5865 O  O    . ALA   B 1 124 ? 43.293 -25.032 -7.332  1.00 11.85 ?  124 ALA   B O    1 
ATOM   5866 C  CB   . ALA   B 1 124 ? 41.704 -22.379 -6.427  1.00 11.85 ?  124 ALA   B CB   1 
ATOM   5867 H  H    . ALA   B 1 124 ? 43.246 -23.017 -8.754  1.00 13.49 ?  124 ALA   B H    1 
ATOM   5868 H  HA   . ALA   B 1 124 ? 43.733 -22.139 -6.251  1.00 13.58 ?  124 ALA   B HA   1 
ATOM   5869 H  HB1  . ALA   B 1 124 ? 41.553 -22.591 -5.492  1.00 14.20 ?  124 ALA   B HB1  1 
ATOM   5870 H  HB2  . ALA   B 1 124 ? 41.534 -21.431 -6.576  1.00 14.20 ?  124 ALA   B HB2  1 
ATOM   5871 H  HB3  . ALA   B 1 124 ? 41.107 -22.906 -6.984  1.00 14.20 ?  124 ALA   B HB3  1 
ATOM   5872 N  N    . PRO   B 1 125 ? 43.727 -24.446 -5.205  1.00 11.58 ?  125 PRO   B N    1 
ATOM   5873 C  CA   . PRO   B 1 125 ? 43.663 -25.811 -4.682  1.00 12.36 ?  125 PRO   B CA   1 
ATOM   5874 C  C    . PRO   B 1 125 ? 42.265 -26.084 -4.131  1.00 12.40 ?  125 PRO   B C    1 
ATOM   5875 O  O    . PRO   B 1 125 ? 41.475 -25.166 -3.918  1.00 12.90 ?  125 PRO   B O    1 
ATOM   5876 C  CB   . PRO   B 1 125 ? 44.648 -25.734 -3.512  1.00 13.23 ?  125 PRO   B CB   1 
ATOM   5877 C  CG   . PRO   B 1 125 ? 44.402 -24.347 -2.948  1.00 13.09 ?  125 PRO   B CG   1 
ATOM   5878 C  CD   . PRO   B 1 125 ? 44.060 -23.477 -4.146  1.00 12.18 ?  125 PRO   B CD   1 
ATOM   5879 H  HA   . PRO   B 1 125 ? 43.935 -26.483 -5.332  1.00 14.81 ?  125 PRO   B HA   1 
ATOM   5880 H  HB2  . PRO   B 1 125 ? 44.437 -26.420 -2.853  1.00 15.86 ?  125 PRO   B HB2  1 
ATOM   5881 H  HB3  . PRO   B 1 125 ? 45.557 -25.828 -3.831  1.00 15.86 ?  125 PRO   B HB3  1 
ATOM   5882 H  HG2  . PRO   B 1 125 ? 43.659 -24.367 -2.323  1.00 15.70 ?  125 PRO   B HG2  1 
ATOM   5883 H  HG3  . PRO   B 1 125 ? 45.206 -24.021 -2.508  1.00 15.70 ?  125 PRO   B HG3  1 
ATOM   5884 H  HD2  . PRO   B 1 125 ? 43.296 -22.915 -3.958  1.00 14.60 ?  125 PRO   B HD2  1 
ATOM   5885 H  HD3  . PRO   B 1 125 ? 44.835 -22.944 -4.408  1.00 14.60 ?  125 PRO   B HD3  1 
ATOM   5886 N  N    . LEU   B 1 126 ? 41.991 -27.361 -3.847  1.00 12.71 ?  126 LEU   B N    1 
ATOM   5887 C  CA   . LEU   B 1 126 ? 40.770 -27.725 -3.133  1.00 13.75 ?  126 LEU   B CA   1 
ATOM   5888 C  C    . LEU   B 1 126 ? 40.889 -27.328 -1.669  1.00 14.09 ?  126 LEU   B C    1 
ATOM   5889 O  O    . LEU   B 1 126 ? 41.785 -27.788 -0.958  1.00 16.02 ?  126 LEU   B O    1 
ATOM   5890 C  CB   . LEU   B 1 126 ? 40.504 -29.219 -3.253  1.00 14.93 ?  126 LEU   B CB   1 
ATOM   5891 C  CG   . LEU   B 1 126 ? 39.980 -29.713 -4.603  1.00 15.84 ?  126 LEU   B CG   1 
ATOM   5892 C  CD1  . LEU   B 1 126 ? 40.006 -31.221 -4.667  1.00 17.65 ?  126 LEU   B CD1  1 
ATOM   5893 C  CD2  . LEU   B 1 126 ? 38.571 -29.209 -4.865  1.00 16.14 ?  126 LEU   B CD2  1 
ATOM   5894 H  H    . LEU   B 1 126 ? 42.499 -28.029 -4.038  1.00 15.24 ?  126 LEU   B H    1 
ATOM   5895 H  HA   . LEU   B 1 126 ? 40.021 -27.241 -3.515  1.00 16.49 ?  126 LEU   B HA   1 
ATOM   5896 H  HB2  . LEU   B 1 126 ? 41.332 -29.686 -3.077  1.00 17.89 ?  126 LEU   B HB2  1 
ATOM   5897 H  HB3  . LEU   B 1 126 ? 39.846 -29.462 -2.583  1.00 17.89 ?  126 LEU   B HB3  1 
ATOM   5898 H  HG   . LEU   B 1 126 ? 40.555 -29.371 -5.308  1.00 18.99 ?  126 LEU   B HG   1 
ATOM   5899 H  HD11 . LEU   B 1 126 ? 39.667 -31.505 -5.532  1.00 21.16 ?  126 LEU   B HD11 1 
ATOM   5900 H  HD12 . LEU   B 1 126 ? 40.913 -31.529 -4.547  1.00 21.16 ?  126 LEU   B HD12 1 
ATOM   5901 H  HD13 . LEU   B 1 126 ? 39.437 -31.574 -3.961  1.00 21.16 ?  126 LEU   B HD13 1 
ATOM   5902 H  HD21 . LEU   B 1 126 ? 38.239 -29.612 -5.684  1.00 19.35 ?  126 LEU   B HD21 1 
ATOM   5903 H  HD22 . LEU   B 1 126 ? 38.003 -29.456 -4.121  1.00 19.35 ?  126 LEU   B HD22 1 
ATOM   5904 H  HD23 . LEU   B 1 126 ? 38.590 -28.242 -4.960  1.00 19.35 ?  126 LEU   B HD23 1 
ATOM   5905 N  N    . LEU   B 1 127 ? 39.964 -26.494 -1.206  1.00 14.04 ?  127 LEU   B N    1 
ATOM   5906 C  CA   . LEU   B 1 127 ? 40.024 -26.002 0.157   1.00 14.42 ?  127 LEU   B CA   1 
ATOM   5907 C  C    . LEU   B 1 127 ? 39.751 -27.122 1.148   1.00 14.06 ?  127 LEU   B C    1 
ATOM   5908 O  O    . LEU   B 1 127 ? 38.931 -28.019 0.918   1.00 14.59 ?  127 LEU   B O    1 
ATOM   5909 C  CB   . LEU   B 1 127 ? 39.007 -24.879 0.371   1.00 14.95 ?  127 LEU   B CB   1 
ATOM   5910 C  CG   . LEU   B 1 127 ? 39.182 -23.623 -0.481  1.00 15.24 ?  127 LEU   B CG   1 
ATOM   5911 C  CD1  . LEU   B 1 127 ? 38.070 -22.646 -0.158  1.00 15.43 ?  127 LEU   B CD1  1 
ATOM   5912 C  CD2  . LEU   B 1 127 ? 40.547 -22.978 -0.263  1.00 15.83 ?  127 LEU   B CD2  1 
ATOM   5913 H  H    . LEU   B 1 127 ? 39.295 -26.193 -1.659  1.00 16.83 ?  127 LEU   B H    1 
ATOM   5914 H  HA   . LEU   B 1 127 ? 40.911 -25.644 0.332   1.00 17.28 ?  127 LEU   B HA   1 
ATOM   5915 H  HB2  . LEU   B 1 127 ? 38.123 -25.233 0.186   1.00 17.92 ?  127 LEU   B HB2  1 
ATOM   5916 H  HB3  . LEU   B 1 127 ? 39.050 -24.604 1.302   1.00 17.92 ?  127 LEU   B HB3  1 
ATOM   5917 H  HG   . LEU   B 1 127 ? 39.099 -23.857 -1.414  1.00 18.28 ?  127 LEU   B HG   1 
ATOM   5918 H  HD11 . LEU   B 1 127 ? 38.189 -21.842 -0.696  1.00 18.50 ?  127 LEU   B HD11 1 
ATOM   5919 H  HD12 . LEU   B 1 127 ? 37.215 -23.051 -0.357  1.00 18.50 ?  127 LEU   B HD12 1 
ATOM   5920 H  HD13 . LEU   B 1 127 ? 38.115 -22.411 0.786   1.00 18.50 ?  127 LEU   B HD13 1 
ATOM   5921 H  HD21 . LEU   B 1 127 ? 40.580 -22.133 -0.737  1.00 18.98 ?  127 LEU   B HD21 1 
ATOM   5922 H  HD22 . LEU   B 1 127 ? 40.681 -22.829 0.687   1.00 18.98 ?  127 LEU   B HD22 1 
ATOM   5923 H  HD23 . LEU   B 1 127 ? 41.232 -23.575 -0.603  1.00 18.98 ?  127 LEU   B HD23 1 
ATOM   5924 N  N    . SER   B 1 128 ? 40.435 -27.038 2.278   1.00 14.04 ?  128 SER   B N    1 
ATOM   5925 C  CA   . SER   B 1 128 ? 40.304 -27.955 3.396   1.00 14.74 ?  128 SER   B CA   1 
ATOM   5926 C  C    . SER   B 1 128 ? 40.793 -29.363 3.079   1.00 16.06 ?  128 SER   B C    1 
ATOM   5927 O  O    . SER   B 1 128 ? 40.685 -30.243 3.930   1.00 17.53 ?  128 SER   B O    1 
ATOM   5928 C  CB   . SER   B 1 128 ? 38.882 -27.946 3.965   1.00 14.98 ?  128 SER   B CB   1 
ATOM   5929 O  OG   . SER   B 1 128 ? 38.598 -26.679 4.550   1.00 15.87 ?  128 SER   B OG   1 
ATOM   5930 H  H    . SER   B 1 128 ? 41.020 -26.418 2.427   1.00 16.83 ?  128 SER   B H    1 
ATOM   5931 H  HA   . SER   B 1 128 ? 40.873 -27.633 4.100   1.00 17.67 ?  128 SER   B HA   1 
ATOM   5932 H  HB2  . SER   B 1 128 ? 38.245 -28.121 3.242   1.00 17.96 ?  128 SER   B HB2  1 
ATOM   5933 H  HB3  . SER   B 1 128 ? 38.804 -28.642 4.636   1.00 17.96 ?  128 SER   B HB3  1 
ATOM   5934 H  HG   . SER   B 1 128 ? 39.142 -26.531 5.167   1.00 19.03 ?  128 SER   B HG   1 
ATOM   5935 N  N    . ALA   B 1 129 ? 41.375 -29.584 1.899   1.00 17.15 ?  129 ALA   B N    1 
ATOM   5936 C  CA   . ALA   B 1 129 ? 41.920 -30.884 1.540   1.00 17.89 ?  129 ALA   B CA   1 
ATOM   5937 C  C    . ALA   B 1 129 ? 43.316 -31.061 2.128   1.00 16.88 ?  129 ALA   B C    1 
ATOM   5938 O  O    . ALA   B 1 129 ? 43.876 -30.164 2.771   1.00 16.64 ?  129 ALA   B O    1 
ATOM   5939 C  CB   . ALA   B 1 129 ? 41.966 -31.042 0.021   1.00 19.76 ?  129 ALA   B CB   1 
ATOM   5940 H  H    . ALA   B 1 129 ? 41.470 -28.982 1.284   1.00 20.56 ?  129 ALA   B H    1 
ATOM   5941 H  HA   . ALA   B 1 129 ? 41.351 -31.576 1.899   1.00 21.45 ?  129 ALA   B HA   1 
ATOM   5942 H  HB1  . ALA   B 1 129 ? 42.322 -31.918 -0.195  1.00 23.69 ?  129 ALA   B HB1  1 
ATOM   5943 H  HB2  . ALA   B 1 129 ? 41.067 -30.953 -0.331  1.00 23.69 ?  129 ALA   B HB2  1 
ATOM   5944 H  HB3  . ALA   B 1 129 ? 42.537 -30.351 -0.353  1.00 23.69 ?  129 ALA   B HB3  1 
ATOM   5945 N  N    . GLY   B 1 130 ? 43.887 -32.243 1.892   1.00 16.77 ?  130 GLY   B N    1 
ATOM   5946 C  CA   . GLY   B 1 130 ? 45.275 -32.477 2.243   1.00 17.24 ?  130 GLY   B CA   1 
ATOM   5947 C  C    . GLY   B 1 130 ? 45.491 -32.386 3.734   1.00 17.47 ?  130 GLY   B C    1 
ATOM   5948 O  O    . GLY   B 1 130 ? 44.796 -33.031 4.529   1.00 18.20 ?  130 GLY   B O    1 
ATOM   5949 H  H    . GLY   B 1 130 ? 43.497 -32.915 1.524   1.00 20.11 ?  130 GLY   B H    1 
ATOM   5950 H  HA2  . GLY   B 1 130 ? 45.544 -33.360 1.944   1.00 20.68 ?  130 GLY   B HA2  1 
ATOM   5951 H  HA3  . GLY   B 1 130 ? 45.839 -31.819 1.806   1.00 20.68 ?  130 GLY   B HA3  1 
ATOM   5952 N  N    . ILE   B 1 131 ? 46.467 -31.557 4.121   1.00 17.76 ?  131 ILE   B N    1 
ATOM   5953 C  CA   . ILE   B 1 131 ? 46.834 -31.426 5.523   1.00 18.60 ?  131 ILE   B CA   1 
ATOM   5954 C  C    . ILE   B 1 131 ? 45.718 -30.831 6.362   1.00 17.71 ?  131 ILE   B C    1 
ATOM   5955 O  O    . ILE   B 1 131 ? 45.784 -30.911 7.591   1.00 19.24 ?  131 ILE   B O    1 
ATOM   5956 C  CB   . ILE   B 1 131 ? 48.160 -30.652 5.699   1.00 20.26 ?  131 ILE   B CB   1 
ATOM   5957 C  CG1  . ILE   B 1 131 ? 47.980 -29.167 5.351   1.00 21.35 ?  131 ILE   B CG1  1 
ATOM   5958 C  CG2  . ILE   B 1 131 ? 49.261 -31.279 4.844   1.00 21.16 ?  131 ILE   B CG2  1 
ATOM   5959 C  CD1  . ILE   B 1 131 ? 49.189 -28.310 5.667   1.00 22.29 ?  131 ILE   B CD1  1 
ATOM   5960 H  H    . ILE   B 1 131 ? 46.925 -31.056 3.596   1.00 21.30 ?  131 ILE   B H    1 
ATOM   5961 H  HA   . ILE   B 1 131 ? 46.986 -32.315 5.871   1.00 22.30 ?  131 ILE   B HA   1 
ATOM   5962 H  HB   . ILE   B 1 131 ? 48.424 -30.711 6.630   1.00 24.30 ?  131 ILE   B HB   1 
ATOM   5963 H  HG12 . ILE   B 1 131 ? 47.797 -29.092 4.402   1.00 25.61 ?  131 ILE   B HG12 1 
ATOM   5964 H  HG13 . ILE   B 1 131 ? 47.230 -28.808 5.856   1.00 25.61 ?  131 ILE   B HG13 1 
ATOM   5965 H  HG21 . ILE   B 1 131 ? 50.109 -30.880 5.084   1.00 25.37 ?  131 ILE   B HG21 1 
ATOM   5966 H  HG22 . ILE   B 1 131 ? 49.278 -32.232 5.010   1.00 25.37 ?  131 ILE   B HG22 1 
ATOM   5967 H  HG23 . ILE   B 1 131 ? 49.065 -31.107 3.908   1.00 25.37 ?  131 ILE   B HG23 1 
ATOM   5968 H  HD11 . ILE   B 1 131 ? 48.964 -27.381 5.504   1.00 26.73 ?  131 ILE   B HD11 1 
ATOM   5969 H  HD12 . ILE   B 1 131 ? 49.426 -28.435 6.599   1.00 26.73 ?  131 ILE   B HD12 1 
ATOM   5970 H  HD13 . ILE   B 1 131 ? 49.922 -28.581 5.096   1.00 26.73 ?  131 ILE   B HD13 1 
ATOM   5971 N  N    . PHE   B 1 132 ? 44.692 -30.247 5.731   1.00 16.67 ?  132 PHE   B N    1 
ATOM   5972 C  CA   . PHE   B 1 132 ? 43.531 -29.745 6.457   1.00 17.11 ?  132 PHE   B CA   1 
ATOM   5973 C  C    . PHE   B 1 132 ? 42.510 -30.836 6.787   1.00 18.93 ?  132 PHE   B C    1 
ATOM   5974 O  O    . PHE   B 1 132 ? 41.603 -30.583 7.586   1.00 20.50 ?  132 PHE   B O    1 
ATOM   5975 C  CB   . PHE   B 1 132 ? 42.847 -28.616 5.672   1.00 16.28 ?  132 PHE   B CB   1 
ATOM   5976 C  CG   . PHE   B 1 132 ? 43.540 -27.274 5.778   1.00 16.20 ?  132 PHE   B CG   1 
ATOM   5977 C  CD1  . PHE   B 1 132 ? 44.834 -27.099 5.313   1.00 16.84 ?  132 PHE   B CD1  1 
ATOM   5978 C  CD2  . PHE   B 1 132 ? 42.869 -26.174 6.299   1.00 16.07 ?  132 PHE   B CD2  1 
ATOM   5979 C  CE1  . PHE   B 1 132 ? 45.458 -25.864 5.403   1.00 17.54 ?  132 PHE   B CE1  1 
ATOM   5980 C  CE2  . PHE   B 1 132 ? 43.487 -24.933 6.380   1.00 16.51 ?  132 PHE   B CE2  1 
ATOM   5981 C  CZ   . PHE   B 1 132 ? 44.778 -24.783 5.931   1.00 17.23 ?  132 PHE   B CZ   1 
ATOM   5982 H  H    . PHE   B 1 132 ? 44.645 -30.135 4.880   1.00 19.99 ?  132 PHE   B H    1 
ATOM   5983 H  HA   . PHE   B 1 132 ? 43.837 -29.368 7.294   1.00 20.52 ?  132 PHE   B HA   1 
ATOM   5984 H  HB2  . PHE   B 1 132 ? 42.830 -28.862 4.735   1.00 19.51 ?  132 PHE   B HB2  1 
ATOM   5985 H  HB3  . PHE   B 1 132 ? 41.942 -28.511 6.004   1.00 19.51 ?  132 PHE   B HB3  1 
ATOM   5986 H  HD1  . PHE   B 1 132 ? 45.297 -27.827 4.961   1.00 20.19 ?  132 PHE   B HD1  1 
ATOM   5987 H  HD2  . PHE   B 1 132 ? 41.997 -26.274 6.606   1.00 19.27 ?  132 PHE   B HD2  1 
ATOM   5988 H  HE1  . PHE   B 1 132 ? 46.331 -25.763 5.099   1.00 21.03 ?  132 PHE   B HE1  1 
ATOM   5989 H  HE2  . PHE   B 1 132 ? 43.032 -24.205 6.744   1.00 19.80 ?  132 PHE   B HE2  1 
ATOM   5990 H  HZ   . PHE   B 1 132 ? 45.197 -23.952 5.993   1.00 20.66 ?  132 PHE   B HZ   1 
ATOM   5991 N  N    . GLY   B 1 133 ? 42.612 -32.031 6.190   1.00 18.64 ?  133 GLY   B N    1 
ATOM   5992 C  CA   . GLY   B 1 133 ? 41.898 -33.195 6.689   1.00 19.46 ?  133 GLY   B CA   1 
ATOM   5993 C  C    . GLY   B 1 133 ? 40.499 -33.455 6.160   1.00 19.79 ?  133 GLY   B C    1 
ATOM   5994 O  O    . GLY   B 1 133 ? 39.910 -34.475 6.530   1.00 21.48 ?  133 GLY   B O    1 
ATOM   5995 H  H    . GLY   B 1 133 ? 43.093 -32.182 5.492   1.00 22.36 ?  133 GLY   B H    1 
ATOM   5996 H  HA2  . GLY   B 1 133 ? 42.436 -33.978 6.500   1.00 23.34 ?  133 GLY   B HA2  1 
ATOM   5997 H  HA3  . GLY   B 1 133 ? 41.831 -33.112 7.653   1.00 23.34 ?  133 GLY   B HA3  1 
ATOM   5998 N  N    . ALA   B 1 134 ? 39.935 -32.588 5.325   1.00 18.82 ?  134 ALA   B N    1 
ATOM   5999 C  CA   . ALA   B 1 134 ? 38.607 -32.874 4.800   1.00 18.69 ?  134 ALA   B CA   1 
ATOM   6000 C  C    . ALA   B 1 134 ? 38.692 -33.856 3.636   1.00 18.49 ?  134 ALA   B C    1 
ATOM   6001 O  O    . ALA   B 1 134 ? 39.743 -34.037 3.013   1.00 19.54 ?  134 ALA   B O    1 
ATOM   6002 C  CB   . ALA   B 1 134 ? 37.918 -31.590 4.342   1.00 19.30 ?  134 ALA   B CB   1 
ATOM   6003 H  H    . ALA   B 1 134 ? 40.286 -31.845 5.064   1.00 22.57 ?  134 ALA   B H    1 
ATOM   6004 H  HA   . ALA   B 1 134 ? 38.069 -33.273 5.501   1.00 22.42 ?  134 ALA   B HA   1 
ATOM   6005 H  HB1  . ALA   B 1 134 ? 37.028 -31.810 4.026   1.00 23.14 ?  134 ALA   B HB1  1 
ATOM   6006 H  HB2  . ALA   B 1 134 ? 37.861 -30.977 5.092   1.00 23.14 ?  134 ALA   B HB2  1 
ATOM   6007 H  HB3  . ALA   B 1 134 ? 38.436 -31.192 3.627   1.00 23.14 ?  134 ALA   B HB3  1 
ATOM   6008 N  N    . ASP   B 1 135 ? 37.560 -34.487 3.349   1.00 19.01 ?  135 ASP   B N    1 
ATOM   6009 C  CA   . ASP   B 1 135 ? 37.456 -35.374 2.201   1.00 19.76 ?  135 ASP   B CA   1 
ATOM   6010 C  C    . ASP   B 1 135 ? 37.555 -34.538 0.932   1.00 18.52 ?  135 ASP   B C    1 
ATOM   6011 O  O    . ASP   B 1 135 ? 36.699 -33.671 0.706   1.00 18.69 ?  135 ASP   B O    1 
ATOM   6012 C  CB   . ASP   B 1 135 ? 36.109 -36.093 2.254   1.00 21.72 ?  135 ASP   B CB   1 
ATOM   6013 C  CG   . ASP   B 1 135 ? 35.935 -37.101 1.139   1.00 23.74 ?  135 ASP   B CG   1 
ATOM   6014 O  OD1  . ASP   B 1 135 ? 36.797 -37.161 0.239   1.00 23.80 ?  135 ASP   B OD1  1 
ATOM   6015 O  OD2  . ASP   B 1 135 ? 34.938 -37.859 1.175   1.00 26.36 -1 135 ASP   B OD2  1 
ATOM   6016 H  H    . ASP   B 1 135 ? 36.834 -34.414 3.807   1.00 22.80 ?  135 ASP   B H    1 
ATOM   6017 H  HA   . ASP   B 1 135 ? 38.170 -36.035 2.233   1.00 23.70 ?  135 ASP   B HA   1 
ATOM   6018 H  HB2  . ASP   B 1 135 ? 36.036 -36.561 3.098   1.00 26.05 ?  135 ASP   B HB2  1 
ATOM   6019 H  HB3  . ASP   B 1 135 ? 35.404 -35.436 2.172   1.00 26.05 ?  135 ASP   B HB3  1 
ATOM   6020 N  N    . PRO   B 1 136 ? 38.567 -34.741 0.087   1.00 18.51 ?  136 PRO   B N    1 
ATOM   6021 C  CA   . PRO   B 1 136 ? 38.660 -33.923 -1.130  1.00 17.71 ?  136 PRO   B CA   1 
ATOM   6022 C  C    . PRO   B 1 136 ? 37.465 -34.076 -2.051  1.00 16.91 ?  136 PRO   B C    1 
ATOM   6023 O  O    . PRO   B 1 136 ? 37.139 -33.129 -2.773  1.00 16.32 ?  136 PRO   B O    1 
ATOM   6024 C  CB   . PRO   B 1 136 ? 39.969 -34.397 -1.779  1.00 18.52 ?  136 PRO   B CB   1 
ATOM   6025 C  CG   . PRO   B 1 136 ? 40.174 -35.784 -1.239  1.00 19.76 ?  136 PRO   B CG   1 
ATOM   6026 C  CD   . PRO   B 1 136 ? 39.643 -35.745 0.164   1.00 19.50 ?  136 PRO   B CD   1 
ATOM   6027 H  HA   . PRO   B 1 136 ? 38.748 -32.991 -0.895  1.00 21.23 ?  136 PRO   B HA   1 
ATOM   6028 H  HB2  . PRO   B 1 136 ? 39.876 -34.415 -2.745  1.00 22.21 ?  136 PRO   B HB2  1 
ATOM   6029 H  HB3  . PRO   B 1 136 ? 40.696 -33.813 -1.513  1.00 22.21 ?  136 PRO   B HB3  1 
ATOM   6030 H  HG2  . PRO   B 1 136 ? 39.677 -36.424 -1.773  1.00 23.69 ?  136 PRO   B HG2  1 
ATOM   6031 H  HG3  . PRO   B 1 136 ? 41.121 -36.002 -1.239  1.00 23.69 ?  136 PRO   B HG3  1 
ATOM   6032 H  HD2  . PRO   B 1 136 ? 39.288 -36.611 0.418   1.00 23.39 ?  136 PRO   B HD2  1 
ATOM   6033 H  HD3  . PRO   B 1 136 ? 40.332 -35.449 0.783   1.00 23.39 ?  136 PRO   B HD3  1 
ATOM   6034 N  N    . ILE   B 1 137 ? 36.810 -35.243 -2.055  1.00 17.64 ?  137 ILE   B N    1 
ATOM   6035 C  CA   . ILE   B 1 137 ? 35.588 -35.410 -2.839  1.00 17.99 ?  137 ILE   B CA   1 
ATOM   6036 C  C    . ILE   B 1 137 ? 34.517 -34.434 -2.363  1.00 17.71 ?  137 ILE   B C    1 
ATOM   6037 O  O    . ILE   B 1 137 ? 33.797 -33.828 -3.166  1.00 16.92 ?  137 ILE   B O    1 
ATOM   6038 C  CB   . ILE   B 1 137 ? 35.112 -36.876 -2.773  1.00 20.00 ?  137 ILE   B CB   1 
ATOM   6039 C  CG1  . ILE   B 1 137 ? 36.115 -37.784 -3.488  1.00 22.36 ?  137 ILE   B CG1  1 
ATOM   6040 C  CG2  . ILE   B 1 137 ? 33.715 -37.025 -3.374  1.00 20.38 ?  137 ILE   B CG2  1 
ATOM   6041 C  CD1  . ILE   B 1 137 ? 35.819 -39.266 -3.345  1.00 24.52 ?  137 ILE   B CD1  1 
ATOM   6042 H  H    . ILE   B 1 137 ? 37.049 -35.946 -1.622  1.00 21.15 ?  137 ILE   B H    1 
ATOM   6043 H  HA   . ILE   B 1 137 ? 35.778 -35.207 -3.771  1.00 21.58 ?  137 ILE   B HA   1 
ATOM   6044 H  HB   . ILE   B 1 137 ? 35.069 -37.143 -1.845  1.00 23.98 ?  137 ILE   B HB   1 
ATOM   6045 H  HG12 . ILE   B 1 137 ? 36.110 -37.579 -4.436  1.00 26.82 ?  137 ILE   B HG12 1 
ATOM   6046 H  HG13 . ILE   B 1 137 ? 36.997 -37.629 -3.121  1.00 26.82 ?  137 ILE   B HG13 1 
ATOM   6047 H  HG21 . ILE   B 1 137 ? 33.488 -37.969 -3.441  1.00 24.44 ?  137 ILE   B HG21 1 
ATOM   6048 H  HG22 . ILE   B 1 137 ? 33.069 -36.584 -2.802  1.00 24.44 ?  137 ILE   B HG22 1 
ATOM   6049 H  HG23 . ILE   B 1 137 ? 33.703 -36.626 -4.258  1.00 24.44 ?  137 ILE   B HG23 1 
ATOM   6050 H  HD11 . ILE   B 1 137 ? 36.552 -39.765 -3.736  1.00 29.40 ?  137 ILE   B HD11 1 
ATOM   6051 H  HD12 . ILE   B 1 137 ? 35.734 -39.485 -2.403  1.00 29.40 ?  137 ILE   B HD12 1 
ATOM   6052 H  HD13 . ILE   B 1 137 ? 34.995 -39.479 -3.811  1.00 29.40 ?  137 ILE   B HD13 1 
ATOM   6053 N  N    . HIS   B 1 138 ? 34.389 -34.282 -1.048  1.00 17.91 ?  138 HIS   B N    1 
ATOM   6054 C  CA   . HIS   B 1 138 ? 33.437 -33.320 -0.508  1.00 18.06 ?  138 HIS   B CA   1 
ATOM   6055 C  C    . HIS   B 1 138 ? 33.850 -31.891 -0.834  1.00 17.15 ?  138 HIS   B C    1 
ATOM   6056 O  O    . HIS   B 1 138 ? 33.000 -31.050 -1.147  1.00 17.49 ?  138 HIS   B O    1 
ATOM   6057 C  CB   . HIS   B 1 138 ? 33.329 -33.497 0.999   1.00 19.28 ?  138 HIS   B CB   1 
ATOM   6058 C  CG   . HIS   B 1 138 ? 32.404 -32.516 1.642   1.00 20.71 ?  138 HIS   B CG   1 
ATOM   6059 N  ND1  . HIS   B 1 138 ? 31.064 -32.442 1.328   1.00 21.89 ?  138 HIS   B ND1  1 
ATOM   6060 C  CD2  . HIS   B 1 138 ? 32.632 -31.540 2.552   1.00 21.12 ?  138 HIS   B CD2  1 
ATOM   6061 C  CE1  . HIS   B 1 138 ? 30.501 -31.477 2.033   1.00 21.95 ?  138 HIS   B CE1  1 
ATOM   6062 N  NE2  . HIS   B 1 138 ? 31.431 -30.915 2.785   1.00 21.24 ?  138 HIS   B NE2  1 
ATOM   6063 H  H    . HIS   B 1 138 ? 34.838 -34.720 -0.459  1.00 21.48 ?  138 HIS   B H    1 
ATOM   6064 H  HA   . HIS   B 1 138 ? 32.563 -33.489 -0.898  1.00 21.65 ?  138 HIS   B HA   1 
ATOM   6065 H  HB2  . HIS   B 1 138 ? 32.995 -34.389 1.189   1.00 23.12 ?  138 HIS   B HB2  1 
ATOM   6066 H  HB3  . HIS   B 1 138 ? 34.207 -33.382 1.392   1.00 23.12 ?  138 HIS   B HB3  1 
ATOM   6067 H  HD1  . HIS   B 1 138 ? 30.657 -32.954 0.767   1.00 26.25 ?  138 HIS   B HD1  1 
ATOM   6068 H  HD2  . HIS   B 1 138 ? 33.440 -31.341 2.960   1.00 25.32 ?  138 HIS   B HD2  1 
ATOM   6069 H  HE1  . HIS   B 1 138 ? 29.599 -31.244 2.009   1.00 26.33 ?  138 HIS   B HE1  1 
ATOM   6070 N  N    . SER   B 1 139 ? 35.143 -31.588 -0.758  1.00 16.61 ?  139 SER   B N    1 
ATOM   6071 C  CA   . SER   B 1 139 ? 35.579 -30.238 -1.078  1.00 15.99 ?  139 SER   B CA   1 
ATOM   6072 C  C    . SER   B 1 139 ? 35.254 -29.896 -2.523  1.00 15.08 ?  139 SER   B C    1 
ATOM   6073 O  O    . SER   B 1 139 ? 34.808 -28.781 -2.812  1.00 15.16 ?  139 SER   B O    1 
ATOM   6074 C  CB   . SER   B 1 139 ? 37.071 -30.101 -0.802  1.00 16.75 ?  139 SER   B CB   1 
ATOM   6075 O  OG   . SER   B 1 139 ? 37.488 -28.773 -1.050  1.00 16.55 ?  139 SER   B OG   1 
ATOM   6076 H  H    . SER   B 1 139 ? 35.765 -32.130 -0.538  1.00 19.92 ?  139 SER   B H    1 
ATOM   6077 H  HA   . SER   B 1 139 ? 35.100 -29.610 -0.517  1.00 19.17 ?  139 SER   B HA   1 
ATOM   6078 H  HB2  . SER   B 1 139 ? 37.237 -30.317 0.128   1.00 20.09 ?  139 SER   B HB2  1 
ATOM   6079 H  HB3  . SER   B 1 139 ? 37.560 -30.698 -1.381  1.00 20.09 ?  139 SER   B HB3  1 
ATOM   6080 H  HG   . SER   B 1 139 ? 38.315 -28.695 -0.888  1.00 19.84 ?  139 SER   B HG   1 
ATOM   6081 N  N    . LEU   B 1 140 ? 35.439 -30.849 -3.441  1.00 14.93 ?  140 LEU   B N    1 
ATOM   6082 C  CA   . LEU   B 1 140 ? 35.079 -30.603 -4.831  1.00 14.87 ?  140 LEU   B CA   1 
ATOM   6083 C  C    . LEU   B 1 140 ? 33.577 -30.370 -4.970  1.00 15.15 ?  140 LEU   B C    1 
ATOM   6084 O  O    . LEU   B 1 140 ? 33.146 -29.482 -5.711  1.00 15.16 ?  140 LEU   B O    1 
ATOM   6085 C  CB   . LEU   B 1 140 ? 35.553 -31.760 -5.708  1.00 15.16 ?  140 LEU   B CB   1 
ATOM   6086 C  CG   . LEU   B 1 140 ? 35.186 -31.656 -7.180  1.00 15.13 ?  140 LEU   B CG   1 
ATOM   6087 C  CD1  . LEU   B 1 140 ? 35.741 -30.381 -7.770  1.00 15.90 ?  140 LEU   B CD1  1 
ATOM   6088 C  CD2  . LEU   B 1 140 ? 35.685 -32.877 -7.916  1.00 16.31 ?  140 LEU   B CD2  1 
ATOM   6089 H  H    . LEU   B 1 140 ? 35.769 -31.625 -3.289  1.00 17.90 ?  140 LEU   B H    1 
ATOM   6090 H  HA   . LEU   B 1 140 ? 35.537 -29.801 -5.137  1.00 17.83 ?  140 LEU   B HA   1 
ATOM   6091 H  HB2  . LEU   B 1 140 ? 36.520 -31.819 -5.658  1.00 18.17 ?  140 LEU   B HB2  1 
ATOM   6092 H  HB3  . LEU   B 1 140 ? 35.160 -32.583 -5.377  1.00 18.17 ?  140 LEU   B HB3  1 
ATOM   6093 H  HG   . LEU   B 1 140 ? 34.220 -31.624 -7.267  1.00 18.14 ?  140 LEU   B HG   1 
ATOM   6094 H  HD11 . LEU   B 1 140 ? 35.639 -30.412 -8.732  1.00 19.06 ?  140 LEU   B HD11 1 
ATOM   6095 H  HD12 . LEU   B 1 140 ? 35.246 -29.625 -7.410  1.00 19.06 ?  140 LEU   B HD12 1 
ATOM   6096 H  HD13 . LEU   B 1 140 ? 36.677 -30.308 -7.535  1.00 19.06 ?  140 LEU   B HD13 1 
ATOM   6097 H  HD21 . LEU   B 1 140 ? 35.443 -32.795 -8.852  1.00 19.55 ?  140 LEU   B HD21 1 
ATOM   6098 H  HD22 . LEU   B 1 140 ? 36.645 -32.927 -7.822  1.00 19.55 ?  140 LEU   B HD22 1 
ATOM   6099 H  HD23 . LEU   B 1 140 ? 35.266 -33.660 -7.531  1.00 19.55 ?  140 LEU   B HD23 1 
ATOM   6100 N  N    . ARG   B 1 141 ? 32.771 -31.160 -4.259  1.00 15.25 ?  141 ARG   B N    1 
ATOM   6101 C  CA   . ARG   B 1 141 ? 31.323 -30.979 -4.242  1.00 16.42 ?  141 ARG   B CA   1 
ATOM   6102 C  C    . ARG   B 1 141 ? 30.950 -29.570 -3.812  1.00 16.14 ?  141 ARG   B C    1 
ATOM   6103 O  O    . ARG   B 1 141 ? 30.146 -28.895 -4.468  1.00 16.31 ?  141 ARG   B O    1 
ATOM   6104 C  CB   . ARG   B 1 141 ? 30.741 -32.012 -3.269  1.00 17.54 ?  141 ARG   B CB   1 
ATOM   6105 C  CG   . ARG   B 1 141 ? 29.274 -31.904 -2.941  1.00 19.29 ?  141 ARG   B CG   1 
ATOM   6106 C  CD   . ARG   B 1 141 ? 28.481 -32.545 -4.009  1.00 21.02 ?  141 ARG   B CD   1 
ATOM   6107 N  NE   . ARG   B 1 141 ? 28.217 -31.623 -5.103  1.00 21.21 ?  141 ARG   B NE   1 
ATOM   6108 C  CZ   . ARG   B 1 141 ? 28.194 -31.966 -6.383  1.00 20.54 ?  141 ARG   B CZ   1 
ATOM   6109 N  NH1  . ARG   B 1 141 ? 28.587 -33.164 -6.787  1.00 20.29 ?  141 ARG   B NH1  1 
ATOM   6110 N  NH2  . ARG   B 1 141 ? 27.763 -31.085 -7.280  1.00 21.05 ?  141 ARG   B NH2  1 
ATOM   6111 H  H    . ARG   B 1 141 ? 33.051 -31.812 -3.777  1.00 18.28 ?  141 ARG   B H    1 
ATOM   6112 H  HA   . ARG   B 1 141 ? 30.963 -31.139 -5.126  1.00 19.69 ?  141 ARG   B HA   1 
ATOM   6113 H  HB2  . ARG   B 1 141 ? 30.900 -32.896 -3.643  1.00 21.03 ?  141 ARG   B HB2  1 
ATOM   6114 H  HB3  . ARG   B 1 141 ? 31.226 -31.940 -2.434  1.00 21.03 ?  141 ARG   B HB3  1 
ATOM   6115 H  HG2  . ARG   B 1 141 ? 29.103 -32.355 -2.105  1.00 23.13 ?  141 ARG   B HG2  1 
ATOM   6116 H  HG3  . ARG   B 1 141 ? 29.017 -30.966 -2.878  1.00 23.13 ?  141 ARG   B HG3  1 
ATOM   6117 H  HD2  . ARG   B 1 141 ? 28.969 -33.312 -4.353  1.00 25.21 ?  141 ARG   B HD2  1 
ATOM   6118 H  HD3  . ARG   B 1 141 ? 27.638 -32.834 -3.640  1.00 25.21 ?  141 ARG   B HD3  1 
ATOM   6119 H  HE   . ARG   B 1 141 ? 28.048 -30.804 -4.903  1.00 25.44 ?  141 ARG   B HE   1 
ATOM   6120 H  HH11 . ARG   B 1 141 ? 28.855 -33.751 -6.220  1.00 24.33 ?  141 ARG   B HH11 1 
ATOM   6121 H  HH12 . ARG   B 1 141 ? 28.568 -33.359 -7.623  1.00 24.33 ?  141 ARG   B HH12 1 
ATOM   6122 H  HH21 . ARG   B 1 141 ? 27.511 -30.301 -7.029  1.00 25.24 ?  141 ARG   B HH21 1 
ATOM   6123 H  HH22 . ARG   B 1 141 ? 27.760 -31.288 -8.116  1.00 25.24 ?  141 ARG   B HH22 1 
ATOM   6124 N  N    . VAL   B 1 142 ? 31.499 -29.123 -2.686  1.00 15.79 ?  142 VAL   B N    1 
ATOM   6125 C  CA   . VAL   B 1 142 ? 31.160 -27.791 -2.204  1.00 15.42 ?  142 VAL   B CA   1 
ATOM   6126 C  C    . VAL   B 1 142 ? 31.635 -26.734 -3.193  1.00 15.12 ?  142 VAL   B C    1 
ATOM   6127 O  O    . VAL   B 1 142 ? 30.939 -25.746 -3.450  1.00 15.93 ?  142 VAL   B O    1 
ATOM   6128 C  CB   . VAL   B 1 142 ? 31.706 -27.564 -0.781  1.00 15.98 ?  142 VAL   B CB   1 
ATOM   6129 C  CG1  . VAL   B 1 142 ? 31.408 -26.142 -0.307  1.00 15.91 ?  142 VAL   B CG1  1 
ATOM   6130 C  CG2  . VAL   B 1 142 ? 31.118 -28.588 0.178   1.00 16.73 ?  142 VAL   B CG2  1 
ATOM   6131 H  H    . VAL   B 1 142 ? 32.059 -29.559 -2.195  1.00 18.93 ?  142 VAL   B H    1 
ATOM   6132 H  HA   . VAL   B 1 142 ? 30.201 -27.724 -2.152  1.00 18.49 ?  142 VAL   B HA   1 
ATOM   6133 H  HB   . VAL   B 1 142 ? 32.671 -27.684 -0.785  1.00 19.16 ?  142 VAL   B HB   1 
ATOM   6134 H  HG11 . VAL   B 1 142 ? 31.606 -26.077 0.640   1.00 19.08 ?  142 VAL   B HG11 1 
ATOM   6135 H  HG12 . VAL   B 1 142 ? 31.965 -25.520 -0.803  1.00 19.08 ?  142 VAL   B HG12 1 
ATOM   6136 H  HG13 . VAL   B 1 142 ? 30.473 -25.948 -0.464  1.00 19.08 ?  142 VAL   B HG13 1 
ATOM   6137 H  HG21 . VAL   B 1 142 ? 31.435 -28.403 1.074   1.00 20.06 ?  142 VAL   B HG21 1 
ATOM   6138 H  HG22 . VAL   B 1 142 ? 30.149 -28.523 0.149   1.00 20.06 ?  142 VAL   B HG22 1 
ATOM   6139 H  HG23 . VAL   B 1 142 ? 31.395 -29.477 -0.096  1.00 20.06 ?  142 VAL   B HG23 1 
ATOM   6140 N  N    . CYS   B 1 143 ? 32.820 -26.927 -3.774  1.00 14.59 ?  143 CYS   B N    1 
ATOM   6141 C  CA   . CYS   B 1 143 ? 33.310 -25.991 -4.780  1.00 14.67 ?  143 CYS   B CA   1 
ATOM   6142 C  C    . CYS   B 1 143 ? 32.305 -25.844 -5.917  1.00 14.51 ?  143 CYS   B C    1 
ATOM   6143 O  O    . CYS   B 1 143 ? 31.902 -24.732 -6.278  1.00 14.60 ?  143 CYS   B O    1 
ATOM   6144 C  CB   . CYS   B 1 143 ? 34.662 -26.478 -5.312  1.00 14.80 ?  143 CYS   B CB   1 
ATOM   6145 S  SG   . CYS   B 1 143 ? 35.416 -25.376 -6.528  1.00 15.01 ?  143 CYS   B SG   1 
ATOM   6146 H  H    . CYS   B 1 143 ? 33.355 -27.575 -3.605  1.00 17.49 ?  143 CYS   B H    1 
ATOM   6147 H  HA   . CYS   B 1 143 ? 33.444 -25.115 -4.378  1.00 17.59 ?  143 CYS   B HA   1 
ATOM   6148 H  HB2  . CYS   B 1 143 ? 35.283 -26.568 -4.572  1.00 17.74 ?  143 CYS   B HB2  1 
ATOM   6149 H  HB3  . CYS   B 1 143 ? 34.538 -27.340 -5.736  1.00 17.74 ?  143 CYS   B HB3  1 
ATOM   6150 H  HG   . CYS   B 1 143 ? 36.495 -25.811 -6.838  1.00 17.99 ?  143 CYS   B HG   1 
ATOM   6151 N  N    . VAL   B 1 144 ? 31.906 -26.966 -6.511  1.00 15.23 ?  144 VAL   B N    1 
ATOM   6152 C  CA   . VAL   B 1 144 ? 30.996 -26.912 -7.650  1.00 16.22 ?  144 VAL   B CA   1 
ATOM   6153 C  C    . VAL   B 1 144 ? 29.654 -26.301 -7.271  1.00 16.44 ?  144 VAL   B C    1 
ATOM   6154 O  O    . VAL   B 1 144 ? 29.039 -25.590 -8.077  1.00 17.69 ?  144 VAL   B O    1 
ATOM   6155 C  CB   . VAL   B 1 144 ? 30.840 -28.327 -8.217  1.00 18.66 ?  144 VAL   B CB   1 
ATOM   6156 C  CG1  . VAL   B 1 144 ? 29.548 -28.468 -9.020  1.00 20.68 ?  144 VAL   B CG1  1 
ATOM   6157 C  CG2  . VAL   B 1 144 ? 32.069 -28.710 -9.038  1.00 19.09 ?  144 VAL   B CG2  1 
ATOM   6158 H  H    . VAL   B 1 144 ? 32.144 -27.756 -6.282  1.00 18.26 ?  144 VAL   B H    1 
ATOM   6159 H  HA   . VAL   B 1 144 ? 31.379 -26.356 -8.344  1.00 19.45 ?  144 VAL   B HA   1 
ATOM   6160 H  HB   . VAL   B 1 144 ? 30.783 -28.951 -7.475  1.00 22.38 ?  144 VAL   B HB   1 
ATOM   6161 H  HG11 . VAL   B 1 144 ? 29.616 -29.263 -9.579  1.00 24.80 ?  144 VAL   B HG11 1 
ATOM   6162 H  HG12 . VAL   B 1 144 ? 28.801 -28.566 -8.409  1.00 24.80 ?  144 VAL   B HG12 1 
ATOM   6163 H  HG13 . VAL   B 1 144 ? 29.432 -27.687 -9.576  1.00 24.80 ?  144 VAL   B HG13 1 
ATOM   6164 H  HG21 . VAL   B 1 144 ? 31.952 -29.609 -9.379  1.00 22.90 ?  144 VAL   B HG21 1 
ATOM   6165 H  HG22 . VAL   B 1 144 ? 32.156 -28.085 -9.777  1.00 22.90 ?  144 VAL   B HG22 1 
ATOM   6166 H  HG23 . VAL   B 1 144 ? 32.850 -28.665 -8.470  1.00 22.90 ?  144 VAL   B HG23 1 
ATOM   6167 N  N    . ASP   B 1 145 ? 29.185 -26.547 -6.051  1.00 16.59 ?  145 ASP   B N    1 
ATOM   6168 C  CA   . ASP   B 1 145 ? 27.878 -26.070 -5.617  1.00 17.13 ?  145 ASP   B CA   1 
ATOM   6169 C  C    . ASP   B 1 145 ? 27.911 -24.649 -5.074  1.00 16.87 ?  145 ASP   B C    1 
ATOM   6170 O  O    . ASP   B 1 145 ? 26.853 -24.106 -4.729  1.00 18.67 ?  145 ASP   B O    1 
ATOM   6171 C  CB   . ASP   B 1 145 ? 27.294 -26.984 -4.532  1.00 18.78 ?  145 ASP   B CB   1 
ATOM   6172 C  CG   . ASP   B 1 145 ? 26.937 -28.362 -5.039  1.00 20.61 ?  145 ASP   B CG   1 
ATOM   6173 O  OD1  . ASP   B 1 145 ? 26.834 -28.556 -6.267  1.00 20.90 ?  145 ASP   B OD1  1 
ATOM   6174 O  OD2  . ASP   B 1 145 ? 26.752 -29.247 -4.184  1.00 22.63 -1 145 ASP   B OD2  1 
ATOM   6175 H  H    . ASP   B 1 145 ? 29.619 -26.975 -5.446  1.00 19.89 ?  145 ASP   B H    1 
ATOM   6176 H  HA   . ASP   B 1 145 ? 27.280 -26.069 -6.377  1.00 20.54 ?  145 ASP   B HA   1 
ATOM   6177 H  HB2  . ASP   B 1 145 ? 27.943 -27.090 -3.828  1.00 22.52 ?  145 ASP   B HB2  1 
ATOM   6178 H  HB3  . ASP   B 1 145 ? 26.484 -26.574 -4.187  1.00 22.52 ?  145 ASP   B HB3  1 
ATOM   6179 N  N    . THR   B 1 146 ? 29.088 -24.036 -4.978  1.00 14.84 ?  146 THR   B N    1 
ATOM   6180 C  CA   . THR   B 1 146 ? 29.217 -22.716 -4.374  1.00 14.71 ?  146 THR   B CA   1 
ATOM   6181 C  C    . THR   B 1 146 ? 29.849 -21.690 -5.295  1.00 14.36 ?  146 THR   B C    1 
ATOM   6182 O  O    . THR   B 1 146 ? 29.397 -20.530 -5.341  1.00 14.75 ?  146 THR   B O    1 
ATOM   6183 C  CB   . THR   B 1 146 ? 30.051 -22.816 -3.092  1.00 14.76 ?  146 THR   B CB   1 
ATOM   6184 O  OG1  . THR   B 1 146 ? 29.473 -23.800 -2.227  1.00 15.05 ?  146 THR   B OG1  1 
ATOM   6185 C  CG2  . THR   B 1 146 ? 30.126 -21.477 -2.384  1.00 15.59 ?  146 THR   B CG2  1 
ATOM   6186 H  H    . THR   B 1 146 ? 29.840 -24.358 -5.258  1.00 17.79 ?  146 THR   B H    1 
ATOM   6187 H  HA   . THR   B 1 146 ? 28.342 -22.385 -4.132  1.00 17.63 ?  146 THR   B HA   1 
ATOM   6188 H  HB   . THR   B 1 146 ? 30.958 -23.077 -3.320  1.00 17.70 ?  146 THR   B HB   1 
ATOM   6189 H  HG1  . THR   B 1 146 ? 29.505 -24.561 -2.599  1.00 18.04 ?  146 THR   B HG1  1 
ATOM   6190 H  HG21 . THR   B 1 146 ? 30.459 -21.592 -1.482  1.00 18.69 ?  146 THR   B HG21 1 
ATOM   6191 H  HG22 . THR   B 1 146 ? 30.725 -20.876 -2.863  1.00 18.69 ?  146 THR   B HG22 1 
ATOM   6192 H  HG23 . THR   B 1 146 ? 29.245 -21.071 -2.346  1.00 18.69 ?  146 THR   B HG23 1 
ATOM   6193 N  N    . VAL   B 1 147 ? 30.916 -22.063 -5.994  1.00 14.22 ?  147 VAL   B N    1 
ATOM   6194 C  CA   . VAL   B 1 147 ? 31.639 -21.118 -6.833  1.00 13.91 ?  147 VAL   B CA   1 
ATOM   6195 C  C    . VAL   B 1 147 ? 30.904 -20.983 -8.155  1.00 14.03 ?  147 VAL   B C    1 
ATOM   6196 O  O    . VAL   B 1 147 ? 30.537 -21.987 -8.782  1.00 15.06 ?  147 VAL   B O    1 
ATOM   6197 C  CB   . VAL   B 1 147 ? 33.090 -21.577 -7.036  1.00 14.00 ?  147 VAL   B CB   1 
ATOM   6198 C  CG1  . VAL   B 1 147 ? 33.851 -20.551 -7.853  1.00 13.92 ?  147 VAL   B CG1  1 
ATOM   6199 C  CG2  . VAL   B 1 147 ? 33.771 -21.787 -5.688  1.00 14.02 ?  147 VAL   B CG2  1 
ATOM   6200 H  H    . VAL   B 1 147 ? 31.237 -22.864 -6.006  1.00 17.05 ?  147 VAL   B H    1 
ATOM   6201 H  HA   . VAL   B 1 147 ? 31.658 -20.252 -6.399  1.00 16.68 ?  147 VAL   B HA   1 
ATOM   6202 H  HB   . VAL   B 1 147 ? 33.103 -22.423 -7.518  1.00 16.79 ?  147 VAL   B HB   1 
ATOM   6203 H  HG11 . VAL   B 1 147 ? 34.796 -20.768 -7.840  1.00 16.68 ?  147 VAL   B HG11 1 
ATOM   6204 H  HG12 . VAL   B 1 147 ? 33.522 -20.560 -8.765  1.00 16.68 ?  147 VAL   B HG12 1 
ATOM   6205 H  HG13 . VAL   B 1 147 ? 33.711 -19.672 -7.461  1.00 16.68 ?  147 VAL   B HG13 1 
ATOM   6206 H  HG21 . VAL   B 1 147 ? 34.711 -21.982 -5.830  1.00 16.81 ?  147 VAL   B HG21 1 
ATOM   6207 H  HG22 . VAL   B 1 147 ? 33.677 -20.980 -5.158  1.00 16.81 ?  147 VAL   B HG22 1 
ATOM   6208 H  HG23 . VAL   B 1 147 ? 33.347 -22.533 -5.229  1.00 16.81 ?  147 VAL   B HG23 1 
ATOM   6209 N  N    . ARG   B 1 148 ? 30.697 -19.736 -8.579  1.00 14.10 ?  148 ARG   B N    1 
ATOM   6210 C  CA   . ARG   B 1 148 ? 30.077 -19.423 -9.854  1.00 14.31 ?  148 ARG   B CA   1 
ATOM   6211 C  C    . ARG   B 1 148 ? 31.032 -18.747 -10.824 1.00 14.38 ?  148 ARG   B C    1 
ATOM   6212 O  O    . ARG   B 1 148 ? 30.745 -18.718 -12.023 1.00 15.74 ?  148 ARG   B O    1 
ATOM   6213 C  CB   . ARG   B 1 148 ? 28.837 -18.537 -9.642  1.00 14.58 ?  148 ARG   B CB   1 
ATOM   6214 C  CG   . ARG   B 1 148 ? 27.760 -19.234 -8.827  1.00 15.70 ?  148 ARG   B CG   1 
ATOM   6215 C  CD   . ARG   B 1 148 ? 26.553 -18.345 -8.521  1.00 16.87 ?  148 ARG   B CD   1 
ATOM   6216 N  NE   . ARG   B 1 148 ? 26.934 -17.149 -7.780  1.00 16.62 ?  148 ARG   B NE   1 
ATOM   6217 C  CZ   . ARG   B 1 148 ? 27.236 -17.121 -6.488  1.00 15.69 ?  148 ARG   B CZ   1 
ATOM   6218 N  NH1  . ARG   B 1 148 ? 27.171 -18.210 -5.734  1.00 15.73 ?  148 ARG   B NH1  1 
ATOM   6219 N  NH2  . ARG   B 1 148 ? 27.638 -15.974 -5.943  1.00 15.30 ?  148 ARG   B NH2  1 
ATOM   6220 H  H    . ARG   B 1 148 ? 30.923 -19.032 -8.127  1.00 16.90 ?  148 ARG   B H    1 
ATOM   6221 H  HA   . ARG   B 1 148 ? 29.784 -20.247 -10.264 1.00 17.15 ?  148 ARG   B HA   1 
ATOM   6222 H  HB2  . ARG   B 1 148 ? 29.099 -17.733 -9.168  1.00 17.48 ?  148 ARG   B HB2  1 
ATOM   6223 H  HB3  . ARG   B 1 148 ? 28.462 -18.308 -10.506 1.00 17.48 ?  148 ARG   B HB3  1 
ATOM   6224 H  HG2  . ARG   B 1 148 ? 27.442 -20.008 -9.326  1.00 18.82 ?  148 ARG   B HG2  1 
ATOM   6225 H  HG3  . ARG   B 1 148 ? 28.139 -19.525 -7.984  1.00 18.82 ?  148 ARG   B HG3  1 
ATOM   6226 H  HD2  . ARG   B 1 148 ? 26.143 -18.069 -9.355  1.00 20.23 ?  148 ARG   B HD2  1 
ATOM   6227 H  HD3  . ARG   B 1 148 ? 25.916 -18.848 -7.987  1.00 20.23 ?  148 ARG   B HD3  1 
ATOM   6228 H  HE   . ARG   B 1 148 ? 26.977 -16.412 -8.214  1.00 19.93 ?  148 ARG   B HE   1 
ATOM   6229 H  HH11 . ARG   B 1 148 ? 26.906 -18.959 -6.072  1.00 18.86 ?  148 ARG   B HH11 1 
ATOM   6230 H  HH12 . ARG   B 1 148 ? 27.362 -18.168 -4.896  1.00 18.86 ?  148 ARG   B HH12 1 
ATOM   6231 H  HH21 . ARG   B 1 148 ? 27.693 -15.267 -6.426  1.00 18.34 ?  148 ARG   B HH21 1 
ATOM   6232 H  HH22 . ARG   B 1 148 ? 27.837 -15.943 -5.107  1.00 18.34 ?  148 ARG   B HH22 1 
ATOM   6233 N  N    . THR   B 1 149 ? 32.137 -18.192 -10.334 1.00 14.18 ?  149 THR   B N    1 
ATOM   6234 C  CA   . THR   B 1 149 ? 33.179 -17.633 -11.180 1.00 14.21 ?  149 THR   B CA   1 
ATOM   6235 C  C    . THR   B 1 149 ? 34.059 -18.775 -11.693 1.00 13.78 ?  149 THR   B C    1 
ATOM   6236 O  O    . THR   B 1 149 ? 33.864 -19.944 -11.349 1.00 14.14 ?  149 THR   B O    1 
ATOM   6237 C  CB   . THR   B 1 149 ? 33.951 -16.578 -10.400 1.00 14.13 ?  149 THR   B CB   1 
ATOM   6238 O  OG1  . THR   B 1 149 ? 34.408 -17.175 -9.187  1.00 14.15 ?  149 THR   B OG1  1 
ATOM   6239 C  CG2  . THR   B 1 149 ? 33.058 -15.370 -10.107 1.00 14.82 ?  149 THR   B CG2  1 
ATOM   6240 H  H    . THR   B 1 149 ? 32.302 -18.124 -9.492  1.00 17.00 ?  149 THR   B H    1 
ATOM   6241 H  HA   . THR   B 1 149 ? 32.767 -17.200 -11.942 1.00 17.04 ?  149 THR   B HA   1 
ATOM   6242 H  HB   . THR   B 1 149 ? 34.712 -16.287 -10.917 1.00 16.94 ?  149 THR   B HB   1 
ATOM   6243 H  HG1  . THR   B 1 149 ? 34.825 -16.599 -8.722  1.00 16.96 ?  149 THR   B HG1  1 
ATOM   6244 H  HG21 . THR   B 1 149 ? 33.562 -14.695 -9.624  1.00 17.77 ?  149 THR   B HG21 1 
ATOM   6245 H  HG22 . THR   B 1 149 ? 32.739 -14.985 -10.940 1.00 17.77 ?  149 THR   B HG22 1 
ATOM   6246 H  HG23 . THR   B 1 149 ? 32.295 -15.636 -9.572  1.00 17.77 ?  149 THR   B HG23 1 
ATOM   6247 N  N    . ASN   B 1 150 ? 35.022 -18.454 -12.546 1.00 13.86 ?  150 ASN   B N    1 
ATOM   6248 C  CA   . ASN   B 1 150 ? 35.790 -19.478 -13.247 1.00 14.21 ?  150 ASN   B CA   1 
ATOM   6249 C  C    . ASN   B 1 150 ? 36.955 -19.925 -12.374 1.00 13.79 ?  150 ASN   B C    1 
ATOM   6250 O  O    . ASN   B 1 150 ? 37.888 -19.157 -12.127 1.00 14.29 ?  150 ASN   B O    1 
ATOM   6251 C  CB   . ASN   B 1 150 ? 36.261 -18.947 -14.594 1.00 16.19 ?  150 ASN   B CB   1 
ATOM   6252 C  CG   . ASN   B 1 150 ? 35.116 -18.733 -15.542 1.00 18.73 ?  150 ASN   B CG   1 
ATOM   6253 O  OD1  . ASN   B 1 150 ? 34.209 -19.552 -15.606 1.00 19.40 ?  150 ASN   B OD1  1 
ATOM   6254 N  ND2  . ASN   B 1 150 ? 35.127 -17.621 -16.258 1.00 20.22 ?  150 ASN   B ND2  1 
ATOM   6255 H  H    . ASN   B 1 150 ? 35.257 -17.645 -12.732 1.00 16.62 ?  150 ASN   B H    1 
ATOM   6256 H  HA   . ASN   B 1 150 ? 35.214 -20.245 -13.407 1.00 17.04 ?  150 ASN   B HA   1 
ATOM   6257 H  HB2  . ASN   B 1 150 ? 36.704 -18.094 -14.460 1.00 19.41 ?  150 ASN   B HB2  1 
ATOM   6258 H  HB3  . ASN   B 1 150 ? 36.865 -19.584 -14.994 1.00 19.41 ?  150 ASN   B HB3  1 
ATOM   6259 H  HD21 . ASN   B 1 150 ? 34.488 -17.451 -16.813 1.00 24.25 ?  150 ASN   B HD21 1 
ATOM   6260 H  HD22 . ASN   B 1 150 ? 35.780 -17.066 -16.180 1.00 24.25 ?  150 ASN   B HD22 1 
ATOM   6261 N  N    . VAL   B 1 151 ? 36.911 -21.171 -11.914 1.00 13.52 ?  151 VAL   B N    1 
ATOM   6262 C  CA   . VAL   B 1 151 ? 37.929 -21.695 -11.017 1.00 13.81 ?  151 VAL   B CA   1 
ATOM   6263 C  C    . VAL   B 1 151 ? 38.632 -22.871 -11.681 1.00 13.60 ?  151 VAL   B C    1 
ATOM   6264 O  O    . VAL   B 1 151 ? 37.988 -23.808 -12.179 1.00 14.50 ?  151 VAL   B O    1 
ATOM   6265 C  CB   . VAL   B 1 151 ? 37.365 -22.033 -9.620  1.00 15.00 ?  151 VAL   B CB   1 
ATOM   6266 C  CG1  . VAL   B 1 151 ? 36.191 -23.023 -9.700  1.00 15.88 ?  151 VAL   B CG1  1 
ATOM   6267 C  CG2  . VAL   B 1 151 ? 38.477 -22.526 -8.699  1.00 15.43 ?  151 VAL   B CG2  1 
ATOM   6268 H  H    . VAL   B 1 151 ? 36.291 -21.739 -12.116 1.00 16.21 ?  151 VAL   B H    1 
ATOM   6269 H  HA   . VAL   B 1 151 ? 38.593 -21.000 -10.888 1.00 16.56 ?  151 VAL   B HA   1 
ATOM   6270 H  HB   . VAL   B 1 151 ? 37.018 -21.212 -9.232  1.00 17.98 ?  151 VAL   B HB   1 
ATOM   6271 H  HG11 . VAL   B 1 151 ? 35.873 -23.210 -8.802  1.00 19.04 ?  151 VAL   B HG11 1 
ATOM   6272 H  HG12 . VAL   B 1 151 ? 35.475 -22.627 -10.225 1.00 19.04 ?  151 VAL   B HG12 1 
ATOM   6273 H  HG13 . VAL   B 1 151 ? 36.493 -23.842 -10.121 1.00 19.04 ?  151 VAL   B HG13 1 
ATOM   6274 H  HG21 . VAL   B 1 151 ? 38.123 -22.604 -7.798  1.00 18.50 ?  151 VAL   B HG21 1 
ATOM   6275 H  HG22 . VAL   B 1 151 ? 38.783 -23.392 -9.008  1.00 18.50 ?  151 VAL   B HG22 1 
ATOM   6276 H  HG23 . VAL   B 1 151 ? 39.206 -21.889 -8.713  1.00 18.50 ?  151 VAL   B HG23 1 
ATOM   6277 N  N    . TYR   B 1 152 ? 39.961 -22.784 -11.708 1.00 12.89 ?  152 TYR   B N    1 
ATOM   6278 C  CA   . TYR   B 1 152 ? 40.860 -23.768 -12.293 1.00 13.21 ?  152 TYR   B CA   1 
ATOM   6279 C  C    . TYR   B 1 152 ? 41.580 -24.447 -11.134 1.00 12.40 ?  152 TYR   B C    1 
ATOM   6280 O  O    . TYR   B 1 152 ? 42.427 -23.830 -10.479 1.00 12.98 ?  152 TYR   B O    1 
ATOM   6281 C  CB   . TYR   B 1 152 ? 41.831 -23.062 -13.242 1.00 13.83 ?  152 TYR   B CB   1 
ATOM   6282 C  CG   . TYR   B 1 152 ? 41.148 -22.593 -14.505 1.00 14.57 ?  152 TYR   B CG   1 
ATOM   6283 C  CD1  . TYR   B 1 152 ? 40.494 -21.363 -14.568 1.00 14.96 ?  152 TYR   B CD1  1 
ATOM   6284 C  CD2  . TYR   B 1 152 ? 41.140 -23.395 -15.633 1.00 16.04 ?  152 TYR   B CD2  1 
ATOM   6285 C  CE1  . TYR   B 1 152 ? 39.852 -20.955 -15.728 1.00 16.42 ?  152 TYR   B CE1  1 
ATOM   6286 C  CE2  . TYR   B 1 152 ? 40.499 -23.002 -16.789 1.00 16.96 ?  152 TYR   B CE2  1 
ATOM   6287 C  CZ   . TYR   B 1 152 ? 39.860 -21.782 -16.836 1.00 17.11 ?  152 TYR   B CZ   1 
ATOM   6288 O  OH   . TYR   B 1 152 ? 39.230 -21.403 -17.997 1.00 19.57 ?  152 TYR   B OH   1 
ATOM   6289 H  H    . TYR   B 1 152 ? 40.393 -22.112 -11.367 1.00 15.45 ?  152 TYR   B H    1 
ATOM   6290 H  HA   . TYR   B 1 152 ? 40.351 -24.428 -12.788 1.00 15.84 ?  152 TYR   B HA   1 
ATOM   6291 H  HB2  . TYR   B 1 152 ? 42.206 -22.286 -12.793 1.00 16.58 ?  152 TYR   B HB2  1 
ATOM   6292 H  HB3  . TYR   B 1 152 ? 42.541 -23.675 -13.488 1.00 16.58 ?  152 TYR   B HB3  1 
ATOM   6293 H  HD1  . TYR   B 1 152 ? 40.484 -20.807 -13.819 1.00 17.93 ?  152 TYR   B HD1  1 
ATOM   6294 H  HD2  . TYR   B 1 152 ? 41.562 -24.223 -15.605 1.00 19.23 ?  152 TYR   B HD2  1 
ATOM   6295 H  HE1  . TYR   B 1 152 ? 39.420 -20.131 -15.761 1.00 19.68 ?  152 TYR   B HE1  1 
ATOM   6296 H  HE2  . TYR   B 1 152 ? 40.509 -23.555 -17.535 1.00 20.33 ?  152 TYR   B HE2  1 
ATOM   6297 H  HH   . TYR   B 1 152 ? 38.885 -20.641 -17.896 1.00 23.47 ?  152 TYR   B HH   1 
ATOM   6298 N  N    . LEU   B 1 153 ? 41.205 -25.696 -10.857 1.00 12.64 ?  153 LEU   B N    1 
ATOM   6299 C  CA   . LEU   B 1 153 ? 41.719 -26.441 -9.718  1.00 12.36 ?  153 LEU   B CA   1 
ATOM   6300 C  C    . LEU   B 1 153 ? 42.951 -27.240 -10.119 1.00 12.79 ?  153 LEU   B C    1 
ATOM   6301 O  O    . LEU   B 1 153 ? 42.932 -27.970 -11.114 1.00 14.12 ?  153 LEU   B O    1 
ATOM   6302 C  CB   . LEU   B 1 153 ? 40.648 -27.401 -9.194  1.00 13.24 ?  153 LEU   B CB   1 
ATOM   6303 C  CG   . LEU   B 1 153 ? 39.391 -26.744 -8.627  1.00 13.80 ?  153 LEU   B CG   1 
ATOM   6304 C  CD1  . LEU   B 1 153 ? 38.273 -27.768 -8.465  1.00 14.82 ?  153 LEU   B CD1  1 
ATOM   6305 C  CD2  . LEU   B 1 153 ? 39.696 -26.076 -7.297  1.00 14.18 ?  153 LEU   B CD2  1 
ATOM   6306 H  H    . LEU   B 1 153 ? 40.627 -26.138 -11.326 1.00 15.16 ?  153 LEU   B H    1 
ATOM   6307 H  HA   . LEU   B 1 153 ? 41.952 -25.824 -9.013  1.00 14.82 ?  153 LEU   B HA   1 
ATOM   6308 H  HB2  . LEU   B 1 153 ? 40.369 -27.981 -9.916  1.00 15.87 ?  153 LEU   B HB2  1 
ATOM   6309 H  HB3  . LEU   B 1 153 ? 41.038 -27.935 -8.481  1.00 15.87 ?  153 LEU   B HB3  1 
ATOM   6310 H  HG   . LEU   B 1 153 ? 39.082 -26.055 -9.240  1.00 16.54 ?  153 LEU   B HG   1 
ATOM   6311 H  HD11 . LEU   B 1 153 ? 37.462 -27.304 -8.189  1.00 17.76 ?  153 LEU   B HD11 1 
ATOM   6312 H  HD12 . LEU   B 1 153 ? 38.128 -28.205 -9.314  1.00 17.76 ?  153 LEU   B HD12 1 
ATOM   6313 H  HD13 . LEU   B 1 153 ? 38.533 -28.408 -7.791  1.00 17.76 ?  153 LEU   B HD13 1 
ATOM   6314 H  HD21 . LEU   B 1 153 ? 38.884 -25.702 -6.926  1.00 17.00 ?  153 LEU   B HD21 1 
ATOM   6315 H  HD22 . LEU   B 1 153 ? 40.067 -26.735 -6.688  1.00 17.00 ?  153 LEU   B HD22 1 
ATOM   6316 H  HD23 . LEU   B 1 153 ? 40.348 -25.365 -7.440  1.00 17.00 ?  153 LEU   B HD23 1 
ATOM   6317 N  N    . ALA   B 1 154 ? 44.005 -27.130 -9.320  1.00 12.74 ?  154 ALA   B N    1 
ATOM   6318 C  CA   . ALA   B 1 154 ? 45.231 -27.897 -9.504  1.00 14.22 ?  154 ALA   B CA   1 
ATOM   6319 C  C    . ALA   B 1 154 ? 45.298 -28.970 -8.425  1.00 14.54 ?  154 ALA   B C    1 
ATOM   6320 O  O    . ALA   B 1 154 ? 45.231 -28.663 -7.228  1.00 15.97 ?  154 ALA   B O    1 
ATOM   6321 C  CB   . ALA   B 1 154 ? 46.456 -26.987 -9.447  1.00 14.76 ?  154 ALA   B CB   1 
ATOM   6322 H  H    . ALA   B 1 154 ? 44.032 -26.592 -8.646  1.00 15.27 ?  154 ALA   B H    1 
ATOM   6323 H  HA   . ALA   B 1 154 ? 45.210 -28.329 -10.368 1.00 17.04 ?  154 ALA   B HA   1 
ATOM   6324 H  HB1  . ALA   B 1 154 ? 47.252 -27.525 -9.571  1.00 17.70 ?  154 ALA   B HB1  1 
ATOM   6325 H  HB2  . ALA   B 1 154 ? 46.391 -26.324 -10.155 1.00 17.70 ?  154 ALA   B HB2  1 
ATOM   6326 H  HB3  . ALA   B 1 154 ? 46.485 -26.544 -8.584  1.00 17.70 ?  154 ALA   B HB3  1 
ATOM   6327 N  N    . VAL   B 1 155 ? 45.422 -30.221 -8.851  1.00 13.80 ?  155 VAL   B N    1 
ATOM   6328 C  CA   . VAL   B 1 155 ? 45.525 -31.367 -7.956  1.00 14.18 ?  155 VAL   B CA   1 
ATOM   6329 C  C    . VAL   B 1 155 ? 46.861 -32.046 -8.239  1.00 14.02 ?  155 VAL   B C    1 
ATOM   6330 O  O    . VAL   B 1 155 ? 47.094 -32.532 -9.354  1.00 16.09 ?  155 VAL   B O    1 
ATOM   6331 C  CB   . VAL   B 1 155 ? 44.361 -32.355 -8.141  1.00 15.75 ?  155 VAL   B CB   1 
ATOM   6332 C  CG1  . VAL   B 1 155 ? 44.556 -33.547 -7.224  1.00 15.96 ?  155 VAL   B CG1  1 
ATOM   6333 C  CG2  . VAL   B 1 155 ? 43.023 -31.664 -7.870  1.00 16.76 ?  155 VAL   B CG2  1 
ATOM   6334 H  H    . VAL   B 1 155 ? 45.460 -30.440 -9.683  1.00 16.55 ?  155 VAL   B H    1 
ATOM   6335 H  HA   . VAL   B 1 155 ? 45.520 -31.062 -7.035  1.00 17.00 ?  155 VAL   B HA   1 
ATOM   6336 H  HB   . VAL   B 1 155 ? 44.353 -32.670 -9.058  1.00 18.88 ?  155 VAL   B HB   1 
ATOM   6337 H  HG11 . VAL   B 1 155 ? 43.722 -34.041 -7.162  1.00 19.13 ?  155 VAL   B HG11 1 
ATOM   6338 H  HG12 . VAL   B 1 155 ? 45.249 -34.122 -7.588  1.00 19.13 ?  155 VAL   B HG12 1 
ATOM   6339 H  HG13 . VAL   B 1 155 ? 44.816 -33.233 -6.343  1.00 19.13 ?  155 VAL   B HG13 1 
ATOM   6340 H  HG21 . VAL   B 1 155 ? 42.307 -32.315 -7.960  1.00 20.09 ?  155 VAL   B HG21 1 
ATOM   6341 H  HG22 . VAL   B 1 155 ? 43.028 -31.305 -6.968  1.00 20.09 ?  155 VAL   B HG22 1 
ATOM   6342 H  HG23 . VAL   B 1 155 ? 42.897 -30.946 -8.510  1.00 20.09 ?  155 VAL   B HG23 1 
ATOM   6343 N  N    . PHE   B 1 156 ? 47.729 -32.088 -7.228  1.00 14.54 ?  156 PHE   B N    1 
ATOM   6344 C  CA   . PHE   B 1 156 ? 49.106 -32.541 -7.434  1.00 15.73 ?  156 PHE   B CA   1 
ATOM   6345 C  C    . PHE   B 1 156 ? 49.199 -34.040 -7.720  1.00 17.05 ?  156 PHE   B C    1 
ATOM   6346 O  O    . PHE   B 1 156 ? 49.916 -34.467 -8.637  1.00 19.03 ?  156 PHE   B O    1 
ATOM   6347 C  CB   . PHE   B 1 156 ? 49.935 -32.179 -6.204  1.00 15.73 ?  156 PHE   B CB   1 
ATOM   6348 C  CG   . PHE   B 1 156 ? 51.361 -32.636 -6.266  1.00 16.36 ?  156 PHE   B CG   1 
ATOM   6349 C  CD1  . PHE   B 1 156 ? 52.240 -32.097 -7.187  1.00 17.79 ?  156 PHE   B CD1  1 
ATOM   6350 C  CD2  . PHE   B 1 156 ? 51.827 -33.591 -5.386  1.00 16.86 ?  156 PHE   B CD2  1 
ATOM   6351 C  CE1  . PHE   B 1 156 ? 53.560 -32.507 -7.234  1.00 18.43 ?  156 PHE   B CE1  1 
ATOM   6352 C  CE2  . PHE   B 1 156 ? 53.145 -34.006 -5.430  1.00 18.01 ?  156 PHE   B CE2  1 
ATOM   6353 C  CZ   . PHE   B 1 156 ? 54.003 -33.466 -6.359  1.00 18.46 ?  156 PHE   B CZ   1 
ATOM   6354 H  H    . PHE   B 1 156 ? 47.543 -31.867 -6.416  1.00 17.43 ?  156 PHE   B H    1 
ATOM   6355 H  HA   . PHE   B 1 156 ? 49.473 -32.069 -8.193  1.00 18.86 ?  156 PHE   B HA   1 
ATOM   6356 H  HB2  . PHE   B 1 156 ? 49.940 -31.212 -6.109  1.00 18.87 ?  156 PHE   B HB2  1 
ATOM   6357 H  HB3  . PHE   B 1 156 ? 49.531 -32.582 -5.421  1.00 18.87 ?  156 PHE   B HB3  1 
ATOM   6358 H  HD1  . PHE   B 1 156 ? 51.943 -31.444 -7.783  1.00 21.33 ?  156 PHE   B HD1  1 
ATOM   6359 H  HD2  . PHE   B 1 156 ? 51.243 -33.961 -4.761  1.00 20.21 ?  156 PHE   B HD2  1 
ATOM   6360 H  HE1  . PHE   B 1 156 ? 54.144 -32.140 -7.861  1.00 22.10 ?  156 PHE   B HE1  1 
ATOM   6361 H  HE2  . PHE   B 1 156 ? 53.445 -34.659 -4.836  1.00 21.59 ?  156 PHE   B HE2  1 
ATOM   6362 H  HZ   . PHE   B 1 156 ? 54.891 -33.748 -6.387  1.00 22.14 ?  156 PHE   B HZ   1 
ATOM   6363 N  N    . ASP   B 1 157 ? 48.533 -34.859 -6.919  1.00 17.39 ?  157 ASP   B N    1 
ATOM   6364 C  CA   . ASP   B 1 157 ? 48.678 -36.305 -7.016  1.00 18.58 ?  157 ASP   B CA   1 
ATOM   6365 C  C    . ASP   B 1 157 ? 47.761 -36.848 -8.107  1.00 19.08 ?  157 ASP   B C    1 
ATOM   6366 O  O    . ASP   B 1 157 ? 46.537 -36.728 -8.005  1.00 18.37 ?  157 ASP   B O    1 
ATOM   6367 C  CB   . ASP   B 1 157 ? 48.323 -36.916 -5.667  1.00 20.11 ?  157 ASP   B CB   1 
ATOM   6368 C  CG   . ASP   B 1 157 ? 48.454 -38.423 -5.652  1.00 21.76 ?  157 ASP   B CG   1 
ATOM   6369 O  OD1  . ASP   B 1 157 ? 48.779 -39.025 -6.702  1.00 22.09 ?  157 ASP   B OD1  1 
ATOM   6370 O  OD2  . ASP   B 1 157 ? 48.237 -39.000 -4.571  1.00 23.61 -1 157 ASP   B OD2  1 
ATOM   6371 H  H    . ASP   B 1 157 ? 47.988 -34.605 -6.311  1.00 20.85 ?  157 ASP   B H    1 
ATOM   6372 H  HA   . ASP   B 1 157 ? 49.596 -36.538 -7.234  1.00 22.28 ?  157 ASP   B HA   1 
ATOM   6373 H  HB2  . ASP   B 1 157 ? 48.902 -36.538 -4.989  1.00 24.11 ?  157 ASP   B HB2  1 
ATOM   6374 H  HB3  . ASP   B 1 157 ? 47.396 -36.696 -5.461  1.00 24.11 ?  157 ASP   B HB3  1 
ATOM   6375 N  N    . LYS   B 1 158 ? 48.354 -37.469 -9.136  1.00 20.13 ?  158 LYS   B N    1 
ATOM   6376 C  CA   . LYS   B 1 158 ? 47.573 -38.080 -10.215 1.00 21.33 ?  158 LYS   B CA   1 
ATOM   6377 C  C    . LYS   B 1 158 ? 46.514 -39.045 -9.683  1.00 21.25 ?  158 LYS   B C    1 
ATOM   6378 O  O    . LYS   B 1 158 ? 45.408 -39.133 -10.233 1.00 21.32 ?  158 LYS   B O    1 
ATOM   6379 C  CB   . LYS   B 1 158 ? 48.516 -38.799 -11.191 1.00 23.23 ?  158 LYS   B CB   1 
ATOM   6380 C  CG   . LYS   B 1 158 ? 47.833 -39.707 -12.209 1.00 25.40 ?  158 LYS   B CG   1 
ATOM   6381 C  CD   . LYS   B 1 158 ? 46.965 -38.930 -13.179 1.00 27.55 ?  158 LYS   B CD   1 
ATOM   6382 C  CE   . LYS   B 1 158 ? 46.360 -39.855 -14.224 1.00 29.35 ?  158 LYS   B CE   1 
ATOM   6383 N  NZ   . LYS   B 1 158 ? 45.291 -39.185 -15.016 1.00 29.82 ?  158 LYS   B NZ   1 
ATOM   6384 H  H    . LYS   B 1 158 ? 49.207 -37.555 -9.231  1.00 24.13 ?  158 LYS   B H    1 
ATOM   6385 H  HA   . LYS   B 1 158 ? 47.121 -37.380 -10.712 1.00 25.58 ?  158 LYS   B HA   1 
ATOM   6386 H  HB2  . LYS   B 1 158 ? 49.014 -38.129 -11.694 1.00 27.86 ?  158 LYS   B HB2  1 
ATOM   6387 H  HB3  . LYS   B 1 158 ? 49.136 -39.343 -10.683 1.00 27.86 ?  158 LYS   B HB3  1 
ATOM   6388 H  HG2  . LYS   B 1 158 ? 48.516 -40.165 -12.725 1.00 30.46 ?  158 LYS   B HG2  1 
ATOM   6389 H  HG3  . LYS   B 1 158 ? 47.280 -40.362 -11.754 1.00 30.46 ?  158 LYS   B HG3  1 
ATOM   6390 H  HD2  . LYS   B 1 158 ? 46.242 -38.502 -12.694 1.00 33.04 ?  158 LYS   B HD2  1 
ATOM   6391 H  HD3  . LYS   B 1 158 ? 47.505 -38.266 -13.636 1.00 33.04 ?  158 LYS   B HD3  1 
ATOM   6392 H  HE2  . LYS   B 1 158 ? 47.054 -40.140 -14.837 1.00 35.20 ?  158 LYS   B HE2  1 
ATOM   6393 H  HE3  . LYS   B 1 158 ? 45.970 -40.626 -13.782 1.00 35.20 ?  158 LYS   B HE3  1 
ATOM   6394 H  HZ1  . LYS   B 1 158 ? 44.956 -39.749 -15.617 1.00 35.77 ?  158 LYS   B HZ1  1 
ATOM   6395 H  HZ2  . LYS   B 1 158 ? 44.635 -38.915 -14.476 1.00 35.77 ?  158 LYS   B HZ2  1 
ATOM   6396 H  HZ3  . LYS   B 1 158 ? 45.625 -38.477 -15.440 1.00 35.77 ?  158 LYS   B HZ3  1 
ATOM   6397 N  N    . ASN   B 1 159 ? 46.835 -39.797 -8.629  1.00 21.52 ?  159 ASN   B N    1 
ATOM   6398 C  CA   . ASN   B 1 159 ? 45.881 -40.782 -8.122  1.00 21.93 ?  159 ASN   B CA   1 
ATOM   6399 C  C    . ASN   B 1 159 ? 44.685 -40.111 -7.440  1.00 20.80 ?  159 ASN   B C    1 
ATOM   6400 O  O    . ASN   B 1 159 ? 43.551 -40.602 -7.537  1.00 21.17 ?  159 ASN   B O    1 
ATOM   6401 C  CB   . ASN   B 1 159 ? 46.590 -41.762 -7.191  1.00 23.48 ?  159 ASN   B CB   1 
ATOM   6402 C  CG   . ASN   B 1 159 ? 47.616 -42.610 -7.915  1.00 25.60 ?  159 ASN   B CG   1 
ATOM   6403 O  OD1  . ASN   B 1 159 ? 47.369 -43.093 -9.027  1.00 26.20 ?  159 ASN   B OD1  1 
ATOM   6404 N  ND2  . ASN   B 1 159 ? 48.773 -42.804 -7.286  1.00 26.20 ?  159 ASN   B ND2  1 
ATOM   6405 H  H    . ASN   B 1 159 ? 47.577 -39.748 -8.203  1.00 25.81 ?  159 ASN   B H    1 
ATOM   6406 H  HA   . ASN   B 1 159 ? 45.544 -41.288 -8.879  1.00 26.30 ?  159 ASN   B HA   1 
ATOM   6407 H  HB2  . ASN   B 1 159 ? 47.048 -41.265 -6.496  1.00 28.16 ?  159 ASN   B HB2  1 
ATOM   6408 H  HB3  . ASN   B 1 159 ? 45.935 -42.358 -6.807  1.00 28.16 ?  159 ASN   B HB3  1 
ATOM   6409 H  HD21 . ASN   B 1 159 ? 49.393 -43.281 -7.653  1.00 31.42 ?  159 ASN   B HD21 1 
ATOM   6410 H  HD22 . ASN   B 1 159 ? 48.902 -42.473 -6.503  1.00 31.42 ?  159 ASN   B HD22 1 
ATOM   6411 N  N    . LEU   B 1 160 ? 44.907 -38.987 -6.750  1.00 19.79 ?  160 LEU   B N    1 
ATOM   6412 C  CA   . LEU   B 1 160 ? 43.777 -38.247 -6.202  1.00 18.70 ?  160 LEU   B CA   1 
ATOM   6413 C  C    . LEU   B 1 160 ? 42.987 -37.578 -7.313  1.00 18.13 ?  160 LEU   B C    1 
ATOM   6414 O  O    . LEU   B 1 160 ? 41.752 -37.579 -7.291  1.00 18.06 ?  160 LEU   B O    1 
ATOM   6415 C  CB   . LEU   B 1 160 ? 44.245 -37.212 -5.184  1.00 18.51 ?  160 LEU   B CB   1 
ATOM   6416 C  CG   . LEU   B 1 160 ? 43.117 -36.312 -4.659  1.00 18.23 ?  160 LEU   B CG   1 
ATOM   6417 C  CD1  . LEU   B 1 160 ? 41.999 -37.144 -4.045  1.00 18.85 ?  160 LEU   B CD1  1 
ATOM   6418 C  CD2  . LEU   B 1 160 ? 43.658 -35.317 -3.650  1.00 18.36 ?  160 LEU   B CD2  1 
ATOM   6419 H  H    . LEU   B 1 160 ? 45.682 -38.645 -6.595  1.00 23.73 ?  160 LEU   B H    1 
ATOM   6420 H  HA   . LEU   B 1 160 ? 43.189 -38.875 -5.757  1.00 22.43 ?  160 LEU   B HA   1 
ATOM   6421 H  HB2  . LEU   B 1 160 ? 44.636 -37.679 -4.428  1.00 22.20 ?  160 LEU   B HB2  1 
ATOM   6422 H  HB3  . LEU   B 1 160 ? 44.913 -36.645 -5.602  1.00 22.20 ?  160 LEU   B HB3  1 
ATOM   6423 H  HG   . LEU   B 1 160 ? 42.742 -35.813 -5.400  1.00 21.86 ?  160 LEU   B HG   1 
ATOM   6424 H  HD11 . LEU   B 1 160 ? 41.375 -36.551 -3.603  1.00 22.60 ?  160 LEU   B HD11 1 
ATOM   6425 H  HD12 . LEU   B 1 160 ? 41.543 -37.641 -4.745  1.00 22.60 ?  160 LEU   B HD12 1 
ATOM   6426 H  HD13 . LEU   B 1 160 ? 42.381 -37.763 -3.400  1.00 22.60 ?  160 LEU   B HD13 1 
ATOM   6427 H  HD21 . LEU   B 1 160 ? 42.933 -34.743 -3.363  1.00 22.02 ?  160 LEU   B HD21 1 
ATOM   6428 H  HD22 . LEU   B 1 160 ? 44.018 -35.803 -2.893  1.00 22.02 ?  160 LEU   B HD22 1 
ATOM   6429 H  HD23 . LEU   B 1 160 ? 44.355 -34.792 -4.071  1.00 22.02 ?  160 LEU   B HD23 1 
ATOM   6430 N  N    . TYR   B 1 161 ? 43.684 -37.012 -8.302  1.00 18.25 ?  161 TYR   B N    1 
ATOM   6431 C  CA   . TYR   B 1 161 ? 43.010 -36.444 -9.464  1.00 18.11 ?  161 TYR   B CA   1 
ATOM   6432 C  C    . TYR   B 1 161 ? 42.055 -37.461 -10.081 1.00 18.07 ?  161 TYR   B C    1 
ATOM   6433 O  O    . TYR   B 1 161 ? 40.884 -37.159 -10.331 1.00 18.00 ?  161 TYR   B O    1 
ATOM   6434 C  CB   . TYR   B 1 161 ? 44.051 -35.974 -10.489 1.00 18.62 ?  161 TYR   B CB   1 
ATOM   6435 C  CG   . TYR   B 1 161 ? 43.468 -35.501 -11.802 1.00 19.00 ?  161 TYR   B CG   1 
ATOM   6436 C  CD1  . TYR   B 1 161 ? 43.078 -34.176 -11.967 1.00 19.11 ?  161 TYR   B CD1  1 
ATOM   6437 C  CD2  . TYR   B 1 161 ? 43.297 -36.376 -12.872 1.00 19.46 ?  161 TYR   B CD2  1 
ATOM   6438 C  CE1  . TYR   B 1 161 ? 42.541 -33.736 -13.153 1.00 20.19 ?  161 TYR   B CE1  1 
ATOM   6439 C  CE2  . TYR   B 1 161 ? 42.756 -35.940 -14.065 1.00 20.62 ?  161 TYR   B CE2  1 
ATOM   6440 C  CZ   . TYR   B 1 161 ? 42.383 -34.618 -14.200 1.00 20.82 ?  161 TYR   B CZ   1 
ATOM   6441 O  OH   . TYR   B 1 161 ? 41.841 -34.175 -15.383 1.00 22.96 ?  161 TYR   B OH   1 
ATOM   6442 H  H    . TYR   B 1 161 ? 44.539 -36.958 -8.331  1.00 21.89 ?  161 TYR   B H    1 
ATOM   6443 H  HA   . TYR   B 1 161 ? 42.491 -35.676 -9.189  1.00 21.72 ?  161 TYR   B HA   1 
ATOM   6444 H  HB2  . TYR   B 1 161 ? 44.550 -35.233 -10.108 1.00 22.33 ?  161 TYR   B HB2  1 
ATOM   6445 H  HB3  . TYR   B 1 161 ? 44.655 -36.706 -10.685 1.00 22.33 ?  161 TYR   B HB3  1 
ATOM   6446 H  HD1  . TYR   B 1 161 ? 43.187 -33.573 -11.266 1.00 22.92 ?  161 TYR   B HD1  1 
ATOM   6447 H  HD2  . TYR   B 1 161 ? 43.544 -37.268 -12.785 1.00 23.33 ?  161 TYR   B HD2  1 
ATOM   6448 H  HE1  . TYR   B 1 161 ? 42.290 -32.841 -13.249 1.00 24.21 ?  161 TYR   B HE1  1 
ATOM   6449 H  HE2  . TYR   B 1 161 ? 42.643 -36.529 -14.774 1.00 24.73 ?  161 TYR   B HE2  1 
ATOM   6450 H  HH   . TYR   B 1 161 ? 41.809 -34.805 -15.939 1.00 27.54 ?  161 TYR   B HH   1 
ATOM   6451 N  N    . ASP   B 1 162 ? 42.542 -38.681 -10.318 1.00 18.67 ?  162 ASP   B N    1 
ATOM   6452 C  CA   . ASP   B 1 162 ? 41.706 -39.707 -10.932 1.00 19.35 ?  162 ASP   B CA   1 
ATOM   6453 C  C    . ASP   B 1 162 ? 40.506 -40.042 -10.053 1.00 18.85 ?  162 ASP   B C    1 
ATOM   6454 O  O    . ASP   B 1 162 ? 39.395 -40.247 -10.557 1.00 19.09 ?  162 ASP   B O    1 
ATOM   6455 C  CB   . ASP   B 1 162 ? 42.525 -40.973 -11.192 1.00 20.63 ?  162 ASP   B CB   1 
ATOM   6456 C  CG   . ASP   B 1 162 ? 43.541 -40.809 -12.310 1.00 22.23 ?  162 ASP   B CG   1 
ATOM   6457 O  OD1  . ASP   B 1 162 ? 43.414 -39.868 -13.117 1.00 22.86 ?  162 ASP   B OD1  1 
ATOM   6458 O  OD2  . ASP   B 1 162 ? 44.459 -41.654 -12.398 1.00 23.77 -1 162 ASP   B OD2  1 
ATOM   6459 H  H    . ASP   B 1 162 ? 43.342 -38.934 -10.139 1.00 22.39 ?  162 ASP   B H    1 
ATOM   6460 H  HA   . ASP   B 1 162 ? 41.371 -39.384 -11.781 1.00 23.20 ?  162 ASP   B HA   1 
ATOM   6461 H  HB2  . ASP   B 1 162 ? 43.014 -41.206 -10.390 1.00 24.74 ?  162 ASP   B HB2  1 
ATOM   6462 H  HB3  . ASP   B 1 162 ? 41.924 -41.693 -11.439 1.00 24.74 ?  162 ASP   B HB3  1 
ATOM   6463 N  N    . LYS   B 1 163 ? 40.712 -40.126 -8.737  1.00 18.16 ?  163 LYS   B N    1 
ATOM   6464 C  CA   . LYS   B 1 163 ? 39.595 -40.400 -7.839  1.00 18.84 ?  163 LYS   B CA   1 
ATOM   6465 C  C    . LYS   B 1 163 ? 38.554 -39.287 -7.895  1.00 17.31 ?  163 LYS   B C    1 
ATOM   6466 O  O    . LYS   B 1 163 ? 37.342 -39.553 -7.876  1.00 17.98 ?  163 LYS   B O    1 
ATOM   6467 C  CB   . LYS   B 1 163 ? 40.091 -40.583 -6.408  1.00 22.22 ?  163 LYS   B CB   1 
ATOM   6468 C  CG   . LYS   B 1 163 ? 39.008 -41.077 -5.472  1.00 27.85 ?  163 LYS   B CG   1 
ATOM   6469 C  CD   . LYS   B 1 163 ? 39.507 -41.294 -4.058  1.00 33.03 ?  163 LYS   B CD   1 
ATOM   6470 C  CE   . LYS   B 1 163 ? 38.423 -41.944 -3.210  1.00 36.91 ?  163 LYS   B CE   1 
ATOM   6471 N  NZ   . LYS   B 1 163 ? 38.581 -41.657 -1.758  1.00 39.57 ?  163 LYS   B NZ   1 
ATOM   6472 H  H    . LYS   B 1 163 ? 41.473 -40.024 -8.349  1.00 21.78 ?  163 LYS   B H    1 
ATOM   6473 H  HA   . LYS   B 1 163 ? 39.167 -41.221 -8.116  1.00 22.59 ?  163 LYS   B HA   1 
ATOM   6474 H  HB2  . LYS   B 1 163 ? 40.810 -41.234 -6.405  1.00 26.64 ?  163 LYS   B HB2  1 
ATOM   6475 H  HB3  . LYS   B 1 163 ? 40.412 -39.732 -6.072  1.00 26.64 ?  163 LYS   B HB3  1 
ATOM   6476 H  HG2  . LYS   B 1 163 ? 38.293 -40.423 -5.439  1.00 33.41 ?  163 LYS   B HG2  1 
ATOM   6477 H  HG3  . LYS   B 1 163 ? 38.666 -41.924 -5.804  1.00 33.41 ?  163 LYS   B HG3  1 
ATOM   6478 H  HD2  . LYS   B 1 163 ? 40.279 -41.883 -4.073  1.00 39.62 ?  163 LYS   B HD2  1 
ATOM   6479 H  HD3  . LYS   B 1 163 ? 39.740 -40.441 -3.661  1.00 39.62 ?  163 LYS   B HD3  1 
ATOM   6480 H  HE2  . LYS   B 1 163 ? 37.555 -41.618 -3.495  1.00 44.28 ?  163 LYS   B HE2  1 
ATOM   6481 H  HE3  . LYS   B 1 163 ? 38.466 -42.905 -3.331  1.00 44.28 ?  163 LYS   B HE3  1 
ATOM   6482 H  HZ1  . LYS   B 1 163 ? 37.928 -42.052 -1.299  1.00 47.47 ?  163 LYS   B HZ1  1 
ATOM   6483 H  HZ2  . LYS   B 1 163 ? 39.364 -41.965 -1.472  1.00 47.47 ?  163 LYS   B HZ2  1 
ATOM   6484 H  HZ3  . LYS   B 1 163 ? 38.544 -40.779 -1.616  1.00 47.47 ?  163 LYS   B HZ3  1 
ATOM   6485 N  N    . LEU   B 1 164 ? 39.011 -38.035 -7.955  1.00 16.30 ?  164 LEU   B N    1 
ATOM   6486 C  CA   . LEU   B 1 164 ? 38.102 -36.895 -8.008  1.00 16.02 ?  164 LEU   B CA   1 
ATOM   6487 C  C    . LEU   B 1 164 ? 37.317 -36.875 -9.314  1.00 16.44 ?  164 LEU   B C    1 
ATOM   6488 O  O    . LEU   B 1 164 ? 36.093 -36.682 -9.314  1.00 17.45 ?  164 LEU   B O    1 
ATOM   6489 C  CB   . LEU   B 1 164 ? 38.900 -35.602 -7.842  1.00 15.50 ?  164 LEU   B CB   1 
ATOM   6490 C  CG   . LEU   B 1 164 ? 39.440 -35.325 -6.441  1.00 16.07 ?  164 LEU   B CG   1 
ATOM   6491 C  CD1  . LEU   B 1 164 ? 40.523 -34.253 -6.491  1.00 16.09 ?  164 LEU   B CD1  1 
ATOM   6492 C  CD2  . LEU   B 1 164 ? 38.328 -34.904 -5.501  1.00 17.66 ?  164 LEU   B CD2  1 
ATOM   6493 H  H    . LEU   B 1 164 ? 39.849 -37.821 -7.964  1.00 19.54 ?  164 LEU   B H    1 
ATOM   6494 H  HA   . LEU   B 1 164 ? 37.474 -36.959 -7.281  1.00 19.21 ?  164 LEU   B HA   1 
ATOM   6495 H  HB2  . LEU   B 1 164 ? 39.665 -35.630 -8.445  1.00 18.58 ?  164 LEU   B HB2  1 
ATOM   6496 H  HB3  . LEU   B 1 164 ? 38.333 -34.857 -8.083  1.00 18.58 ?  164 LEU   B HB3  1 
ATOM   6497 H  HG   . LEU   B 1 164 ? 39.848 -36.132 -6.091  1.00 19.27 ?  164 LEU   B HG   1 
ATOM   6498 H  HD11 . LEU   B 1 164 ? 40.850 -34.085 -5.590  1.00 19.29 ?  164 LEU   B HD11 1 
ATOM   6499 H  HD12 . LEU   B 1 164 ? 41.257 -34.560 -7.050  1.00 19.29 ?  164 LEU   B HD12 1 
ATOM   6500 H  HD13 . LEU   B 1 164 ? 40.150 -33.436 -6.860  1.00 19.29 ?  164 LEU   B HD13 1 
ATOM   6501 H  HD21 . LEU   B 1 164 ? 38.708 -34.681 -4.638  1.00 21.18 ?  164 LEU   B HD21 1 
ATOM   6502 H  HD22 . LEU   B 1 164 ? 37.875 -34.132 -5.873  1.00 21.18 ?  164 LEU   B HD22 1 
ATOM   6503 H  HD23 . LEU   B 1 164 ? 37.704 -35.642 -5.408  1.00 21.18 ?  164 LEU   B HD23 1 
ATOM   6504 N  N    . VAL   B 1 165 ? 38.006 -37.050 -10.442 1.00 18.15 ?  165 VAL   B N    1 
ATOM   6505 C  CA   . VAL   B 1 165 ? 37.343 -36.994 -11.740 1.00 19.79 ?  165 VAL   B CA   1 
ATOM   6506 C  C    . VAL   B 1 165 ? 36.413 -38.187 -11.912 1.00 21.47 ?  165 VAL   B C    1 
ATOM   6507 O  O    . VAL   B 1 165 ? 35.246 -38.041 -12.298 1.00 22.94 ?  165 VAL   B O    1 
ATOM   6508 C  CB   . VAL   B 1 165 ? 38.382 -36.923 -12.874 1.00 20.57 ?  165 VAL   B CB   1 
ATOM   6509 C  CG1  . VAL   B 1 165 ? 37.704 -37.042 -14.217 1.00 21.72 ?  165 VAL   B CG1  1 
ATOM   6510 C  CG2  . VAL   B 1 165 ? 39.168 -35.628 -12.797 1.00 20.22 ?  165 VAL   B CG2  1 
ATOM   6511 H  H    . VAL   B 1 165 ? 38.856 -37.197 -10.483 1.00 21.77 ?  165 VAL   B H    1 
ATOM   6512 H  HA   . VAL   B 1 165 ? 36.807 -36.189 -11.784 1.00 23.74 ?  165 VAL   B HA   1 
ATOM   6513 H  HB   . VAL   B 1 165 ? 39.013 -37.654 -12.781 1.00 24.67 ?  165 VAL   B HB   1 
ATOM   6514 H  HG11 . VAL   B 1 165 ? 38.308 -36.731 -14.906 1.00 26.05 ?  165 VAL   B HG11 1 
ATOM   6515 H  HG12 . VAL   B 1 165 ? 37.487 -37.976 -14.371 1.00 26.05 ?  165 VAL   B HG12 1 
ATOM   6516 H  HG13 . VAL   B 1 165 ? 36.897 -36.510 -14.211 1.00 26.05 ?  165 VAL   B HG13 1 
ATOM   6517 H  HG21 . VAL   B 1 165 ? 39.805 -35.596 -13.530 1.00 24.25 ?  165 VAL   B HG21 1 
ATOM   6518 H  HG22 . VAL   B 1 165 ? 38.553 -34.878 -12.866 1.00 24.25 ?  165 VAL   B HG22 1 
ATOM   6519 H  HG23 . VAL   B 1 165 ? 39.640 -35.588 -11.950 1.00 24.25 ?  165 VAL   B HG23 1 
ATOM   6520 N  N    . SER   B 1 166 ? 36.922 -39.390 -11.627 1.00 22.26 ?  166 SER   B N    1 
ATOM   6521 C  CA   . SER   B 1 166 ? 36.167 -40.599 -11.921 1.00 23.31 ?  166 SER   B CA   1 
ATOM   6522 C  C    . SER   B 1 166 ? 34.914 -40.693 -11.068 1.00 23.59 ?  166 SER   B C    1 
ATOM   6523 O  O    . SER   B 1 166 ? 33.944 -41.323 -11.485 1.00 24.68 ?  166 SER   B O    1 
ATOM   6524 C  CB   . SER   B 1 166 ? 37.036 -41.854 -11.766 1.00 24.14 ?  166 SER   B CB   1 
ATOM   6525 O  OG   . SER   B 1 166 ? 37.414 -42.069 -10.417 1.00 24.29 ?  166 SER   B OG   1 
ATOM   6526 H  H    . SER   B 1 166 ? 37.697 -39.526 -11.268 1.00 26.69 ?  166 SER   B H    1 
ATOM   6527 H  HA   . SER   B 1 166 ? 35.886 -40.564 -12.846 1.00 27.95 ?  166 SER   B HA   1 
ATOM   6528 H  HB2  . SER   B 1 166 ? 36.533 -42.624 -12.075 1.00 28.96 ?  166 SER   B HB2  1 
ATOM   6529 H  HB3  . SER   B 1 166 ? 37.836 -41.750 -12.311 1.00 28.96 ?  166 SER   B HB3  1 
ATOM   6530 H  HG   . SER   B 1 166 ? 37.871 -41.416 -10.145 1.00 29.14 ?  166 SER   B HG   1 
ATOM   6531 N  N    . SER   B 1 167 ? 34.900 -40.076 -9.890  1.00 22.09 ?  167 SER   B N    1 
ATOM   6532 C  CA   . SER   B 1 167 ? 33.750 -40.132 -8.994  1.00 21.40 ?  167 SER   B CA   1 
ATOM   6533 C  C    . SER   B 1 167 ? 32.835 -38.909 -9.089  1.00 20.83 ?  167 SER   B C    1 
ATOM   6534 O  O    . SER   B 1 167 ? 31.756 -38.912 -8.487  1.00 21.23 ?  167 SER   B O    1 
ATOM   6535 C  CB   . SER   B 1 167 ? 34.211 -40.313 -7.542  1.00 21.26 ?  167 SER   B CB   1 
ATOM   6536 O  OG   . SER   B 1 167 ? 34.879 -39.149 -7.074  1.00 20.92 ?  167 SER   B OG   1 
ATOM   6537 H  H    . SER   B 1 167 ? 35.550 -39.612 -9.589  1.00 26.49 ?  167 SER   B H    1 
ATOM   6538 H  HA   . SER   B 1 167 ? 33.215 -40.907 -9.228  1.00 25.66 ?  167 SER   B HA   1 
ATOM   6539 H  HB2  . SER   B 1 167 ? 33.435 -40.488 -6.985  1.00 25.50 ?  167 SER   B HB2  1 
ATOM   6540 H  HB3  . SER   B 1 167 ? 34.816 -41.080 -7.501  1.00 25.50 ?  167 SER   B HB3  1 
ATOM   6541 H  HG   . SER   B 1 167 ? 35.560 -39.012 -7.542  1.00 25.09 ?  167 SER   B HG   1 
ATOM   6542 N  N    . PHE   B 1 168 ? 33.217 -37.871 -9.836  1.00 20.40 ?  168 PHE   B N    1 
ATOM   6543 C  CA   . PHE   B 1 168 ? 32.382 -36.670 -9.901  1.00 19.68 ?  168 PHE   B CA   1 
ATOM   6544 C  C    . PHE   B 1 168 ? 31.077 -36.929 -10.645 1.00 17.45 ?  168 PHE   B C    1 
ATOM   6545 O  O    . PHE   B 1 168 ? 30.030 -36.343 -10.307 1.00 17.76 ?  168 PHE   B O    1 
ATOM   6546 C  CB   . PHE   B 1 168 ? 33.149 -35.529 -10.566 1.00 20.38 ?  168 PHE   B CB   1 
ATOM   6547 C  CG   . PHE   B 1 168 ? 32.334 -34.285 -10.739 1.00 20.51 ?  168 PHE   B CG   1 
ATOM   6548 C  CD1  . PHE   B 1 168 ? 31.972 -33.523 -9.637  1.00 21.60 ?  168 PHE   B CD1  1 
ATOM   6549 C  CD2  . PHE   B 1 168 ? 31.916 -33.882 -11.994 1.00 19.89 ?  168 PHE   B CD2  1 
ATOM   6550 C  CE1  . PHE   B 1 168 ? 31.205 -32.382 -9.782  1.00 21.80 ?  168 PHE   B CE1  1 
ATOM   6551 C  CE2  . PHE   B 1 168 ? 31.166 -32.727 -12.153 1.00 21.11 ?  168 PHE   B CE2  1 
ATOM   6552 C  CZ   . PHE   B 1 168 ? 30.802 -31.978 -11.043 1.00 21.29 ?  168 PHE   B CZ   1 
ATOM   6553 H  H    . PHE   B 1 168 ? 33.938 -37.835 -10.301 1.00 24.47 ?  168 PHE   B H    1 
ATOM   6554 H  HA   . PHE   B 1 168 ? 32.155 -36.395 -9.003  1.00 23.61 ?  168 PHE   B HA   1 
ATOM   6555 H  HB2  . PHE   B 1 168 ? 33.916 -35.305 -10.018 1.00 24.44 ?  168 PHE   B HB2  1 
ATOM   6556 H  HB3  . PHE   B 1 168 ? 33.441 -35.811 -11.446 1.00 24.44 ?  168 PHE   B HB3  1 
ATOM   6557 H  HD1  . PHE   B 1 168 ? 32.236 -33.794 -8.789  1.00 25.90 ?  168 PHE   B HD1  1 
ATOM   6558 H  HD2  . PHE   B 1 168 ? 32.158 -34.375 -12.741 1.00 23.86 ?  168 PHE   B HD2  1 
ATOM   6559 H  HE1  . PHE   B 1 168 ? 30.966 -31.881 -9.037  1.00 26.14 ?  168 PHE   B HE1  1 
ATOM   6560 H  HE2  . PHE   B 1 168 ? 30.890 -32.464 -13.004 1.00 25.32 ?  168 PHE   B HE2  1 
ATOM   6561 H  HZ   . PHE   B 1 168 ? 30.289 -31.209 -11.151 1.00 25.53 ?  168 PHE   B HZ   1 
ATOM   6562 N  N    . LEU   B 1 169 ? 31.123 -37.797 -11.654 1.00 17.40 ?  169 LEU   B N    1 
ATOM   6563 C  CA   . LEU   B 1 169 ? 29.948 -38.121 -12.454 1.00 19.67 ?  169 LEU   B CA   1 
ATOM   6564 C  C    . LEU   B 1 169 ? 29.953 -39.562 -12.942 1.00 22.44 ?  169 LEU   B C    1 
ATOM   6565 O  O    . LEU   B 1 169 ? 29.060 -39.974 -13.684 1.00 24.56 ?  169 LEU   B O    1 
ATOM   6566 C  CB   . LEU   B 1 169 ? 29.865 -37.195 -13.665 1.00 21.34 ?  169 LEU   B CB   1 
ATOM   6567 C  CG   . LEU   B 1 169 ? 28.605 -36.337 -13.778 1.00 23.75 ?  169 LEU   B CG   1 
ATOM   6568 C  CD1  . LEU   B 1 169 ? 28.550 -35.712 -15.153 1.00 24.56 ?  169 LEU   B CD1  1 
ATOM   6569 C  CD2  . LEU   B 1 169 ? 27.345 -37.143 -13.505 1.00 23.54 ?  169 LEU   B CD2  1 
ATOM   6570 O  OXT  . LEU   B 1 169 ? 30.851 -40.332 -12.621 1.00 23.59 -1 169 LEU   B OXT  1 
ATOM   6571 H  H    . LEU   B 1 169 ? 31.836 -38.211 -11.908 1.00 20.87 ?  169 LEU   B H    1 
ATOM   6572 H  HA   . LEU   B 1 169 ? 29.164 -37.983 -11.908 1.00 23.59 ?  169 LEU   B HA   1 
ATOM   6573 H  HB2  . LEU   B 1 169 ? 30.620 -36.588 -13.646 1.00 25.59 ?  169 LEU   B HB2  1 
ATOM   6574 H  HB3  . LEU   B 1 169 ? 29.908 -37.735 -14.472 1.00 25.59 ?  169 LEU   B HB3  1 
ATOM   6575 H  HG   . LEU   B 1 169 ? 28.648 -35.618 -13.127 1.00 28.48 ?  169 LEU   B HG   1 
ATOM   6576 H  HD11 . LEU   B 1 169 ? 27.767 -35.143 -15.210 1.00 29.46 ?  169 LEU   B HD11 1 
ATOM   6577 H  HD12 . LEU   B 1 169 ? 29.353 -35.187 -15.289 1.00 29.46 ?  169 LEU   B HD12 1 
ATOM   6578 H  HD13 . LEU   B 1 169 ? 28.498 -36.418 -15.815 1.00 29.46 ?  169 LEU   B HD13 1 
ATOM   6579 H  HD21 . LEU   B 1 169 ? 26.591 -36.714 -13.932 1.00 28.23 ?  169 LEU   B HD21 1 
ATOM   6580 H  HD22 . LEU   B 1 169 ? 27.464 -38.040 -13.862 1.00 28.23 ?  169 LEU   B HD22 1 
ATOM   6581 H  HD23 . LEU   B 1 169 ? 27.204 -37.188 -12.547 1.00 28.23 ?  169 LEU   B HD23 1 
HETATM 6582 C  C1   T TFA   C 2 .   ? 12.138 -1.264  1.431   0.30 11.85 ?  201 TFA   A C1   1 
HETATM 6583 C  C2   T TFA   C 2 .   ? 12.762 -1.709  0.087   0.30 13.88 ?  201 TFA   A C2   1 
HETATM 6584 O  O    T TFA   C 2 .   ? 12.842 -1.544  2.407   0.30 10.33 ?  201 TFA   A O    1 
HETATM 6585 F  F1   T TFA   C 2 .   ? 12.824 -3.052  0.047   0.30 15.36 ?  201 TFA   A F1   1 
HETATM 6586 F  F2   T TFA   C 2 .   ? 12.034 -1.332  -0.978  0.30 14.37 ?  201 TFA   A F2   1 
HETATM 6587 F  F3   T TFA   C 2 .   ? 13.995 -1.222  -0.101  0.30 15.35 ?  201 TFA   A F3   1 
HETATM 6588 O  OXT  T TFA   C 2 .   ? 11.053 -0.694  1.340   0.30 12.17 ?  201 TFA   A OXT  1 
HETATM 6589 N  N2   B A1A9T D 3 .   ? 14.638 -0.248  4.100   0.18 13.87 ?  202 A1A9T A N2   1 
HETATM 6590 C  C3   B A1A9T D 3 .   ? 14.737 0.868   3.292   0.18 13.91 ?  202 A1A9T A C3   1 
HETATM 6591 C  C6   B A1A9T D 3 .   ? 15.126 2.125   3.896   0.18 13.55 ?  202 A1A9T A C6   1 
HETATM 6592 C  C9   B A1A9T D 3 .   ? 15.402 -1.469  0.947   0.18 15.11 ?  202 A1A9T A C9   1 
HETATM 6593 C  C1   B A1A9T D 3 .   ? 12.894 -1.307  1.643   0.18 14.96 ?  202 A1A9T A C1   1 
HETATM 6594 C  C10  B A1A9T D 3 .   ? 15.547 -0.931  -0.487  0.18 15.23 ?  202 A1A9T A C10  1 
HETATM 6595 C  C11  B A1A9T D 3 .   ? 14.165 -0.246  -0.328  0.18 15.36 ?  202 A1A9T A C11  1 
HETATM 6596 C  C2   B A1A9T D 3 .   ? 14.177 -0.513  1.193   0.18 15.08 ?  202 A1A9T A C2   1 
HETATM 6597 C  C4   B A1A9T D 3 .   ? 14.908 -0.136  5.445   0.18 13.69 ?  202 A1A9T A C4   1 
HETATM 6598 C  C5   B A1A9T D 3 .   ? 15.368 2.065   5.307   0.18 13.40 ?  202 A1A9T A C5   1 
HETATM 6599 C  C7   B A1A9T D 3 .   ? 15.375 3.520   3.555   0.18 13.77 ?  202 A1A9T A C7   1 
HETATM 6600 C  C8   B A1A9T D 3 .   ? 15.734 4.206   4.709   0.18 13.50 ?  202 A1A9T A C8   1 
HETATM 6601 N  N1   B A1A9T D 3 .   ? 14.459 0.727   1.935   0.18 14.62 ?  202 A1A9T A N1   1 
HETATM 6602 N  N3   B A1A9T D 3 .   ? 15.269 0.965   6.101   0.18 13.51 ?  202 A1A9T A N3   1 
HETATM 6603 N  N4   B A1A9T D 3 .   ? 15.726 3.308   5.756   0.18 13.17 ?  202 A1A9T A N4   1 
HETATM 6604 O  O1   B A1A9T D 3 .   ? 11.882 -0.377  1.937   0.18 15.21 ?  202 A1A9T A O1   1 
HETATM 6605 H  H10  B A1A9T D 3 .   ? 16.257 -1.285  1.626   0.18 18.11 ?  202 A1A9T A H10  1 
HETATM 6606 H  H9   B A1A9T D 3 .   ? 15.168 -2.534  1.064   0.18 18.11 ?  202 A1A9T A H9   1 
HETATM 6607 H  H2   B A1A9T D 3 .   ? 13.180 -1.943  2.504   0.18 17.93 ?  202 A1A9T A H2   1 
HETATM 6608 H  H3   B A1A9T D 3 .   ? 12.564 -2.051  0.871   0.18 17.93 ?  202 A1A9T A H3   1 
HETATM 6609 H  H12  B A1A9T D 3 .   ? 16.417 -0.266  -0.721  0.18 18.27 ?  202 A1A9T A H12  1 
HETATM 6610 H  H11  B A1A9T D 3 .   ? 15.647 -1.677  -1.264  0.18 18.27 ?  202 A1A9T A H11  1 
HETATM 6611 H  H13  B A1A9T D 3 .   ? 13.290 -0.707  -0.801  0.18 18.41 ?  202 A1A9T A H13  1 
HETATM 6612 H  H14  B A1A9T D 3 .   ? 14.111 0.829   -0.563  0.18 18.41 ?  202 A1A9T A H14  1 
HETATM 6613 H  H5   B A1A9T D 3 .   ? 14.827 -1.032  6.099   0.18 16.42 ?  202 A1A9T A H5   1 
HETATM 6614 H  H6   B A1A9T D 3 .   ? 15.314 4.015   2.603   0.18 16.51 ?  202 A1A9T A H6   1 
HETATM 6615 H  H7   B A1A9T D 3 .   ? 16.005 5.235   4.953   0.18 16.18 ?  202 A1A9T A H7   1 
HETATM 6616 H  H4   B A1A9T D 3 .   ? 14.452 1.573   1.366   0.18 17.53 ?  202 A1A9T A H4   1 
HETATM 6617 H  H8   B A1A9T D 3 .   ? 15.959 3.556   6.754   0.18 15.79 ?  202 A1A9T A H8   1 
HETATM 6618 H  H1   B A1A9T D 3 .   ? 11.049 -0.833  2.079   0.18 18.24 ?  202 A1A9T A H1   1 
HETATM 6619 N  N2   C A1A9T E 3 .   ? 14.746 -0.361  4.261   0.18 13.68 ?  203 A1A9T A N2   1 
HETATM 6620 C  C3   C A1A9T E 3 .   ? 14.919 0.691   3.379   0.18 13.90 ?  203 A1A9T A C3   1 
HETATM 6621 C  C6   C A1A9T E 3 .   ? 15.227 1.993   3.944   0.18 13.33 ?  203 A1A9T A C6   1 
HETATM 6622 C  C9   C A1A9T E 3 .   ? 14.045 -0.566  -0.270  0.18 16.60 ?  203 A1A9T A C9   1 
HETATM 6623 C  C1   C A1A9T E 3 .   ? 15.305 -2.013  1.405   0.18 16.46 ?  203 A1A9T A C1   1 
HETATM 6624 C  C10  C A1A9T E 3 .   ? 12.543 -0.899  -0.037  0.18 16.78 ?  203 A1A9T A C10  1 
HETATM 6625 C  C11  C A1A9T E 3 .   ? 12.859 -1.127  1.473   0.18 16.76 ?  203 A1A9T A C11  1 
HETATM 6626 C  C2   C A1A9T E 3 .   ? 14.366 -0.766  1.256   0.18 16.33 ?  203 A1A9T A C2   1 
HETATM 6627 C  C4   C A1A9T E 3 .   ? 14.870 -0.152  5.626   0.18 13.63 ?  203 A1A9T A C4   1 
HETATM 6628 C  C5   C A1A9T E 3 .   ? 15.319 2.039   5.386   0.18 13.24 ?  203 A1A9T A C5   1 
HETATM 6629 C  C7   C A1A9T E 3 .   ? 15.501 3.369   3.528   0.18 13.33 ?  203 A1A9T A C7   1 
HETATM 6630 C  C8   C A1A9T E 3 .   ? 15.727 4.142   4.659   0.18 13.19 ?  203 A1A9T A C8   1 
HETATM 6631 N  N1   C A1A9T E 3 .   ? 14.795 0.463   1.988   0.18 15.24 ?  203 A1A9T A N1   1 
HETATM 6632 N  N3   C A1A9T E 3 .   ? 15.147 0.996   6.264   0.18 13.48 ?  203 A1A9T A N3   1 
HETATM 6633 N  N4   C A1A9T E 3 .   ? 15.615 3.322   5.764   0.18 12.95 ?  203 A1A9T A N4   1 
HETATM 6634 O  O1   C A1A9T E 3 .   ? 15.189 -2.554  2.691   0.18 16.68 ?  203 A1A9T A O1   1 
HETATM 6635 H  H10  C A1A9T E 3 .   ? 14.280 0.461   -0.630  0.18 19.91 ?  203 A1A9T A H10  1 
HETATM 6636 H  H9   C A1A9T E 3 .   ? 14.627 -1.224  -0.932  0.18 19.91 ?  203 A1A9T A H9   1 
HETATM 6637 H  H2   C A1A9T E 3 .   ? 16.335 -1.671  1.184   0.18 19.73 ?  203 A1A9T A H2   1 
HETATM 6638 H  H3   C A1A9T E 3 .   ? 15.110 -2.777  0.598   0.18 19.73 ?  203 A1A9T A H3   1 
HETATM 6639 H  H12  C A1A9T E 3 .   ? 11.794 -0.102  -0.279  0.18 20.13 ?  203 A1A9T A H12  1 
HETATM 6640 H  H11  C A1A9T E 3 .   ? 12.122 -1.760  -0.600  0.18 20.13 ?  203 A1A9T A H11  1 
HETATM 6641 H  H13  C A1A9T E 3 .   ? 12.747 -2.143  1.878   0.18 20.09 ?  203 A1A9T A H13  1 
HETATM 6642 H  H14  C A1A9T E 3 .   ? 12.357 -0.453  2.192   0.18 20.09 ?  203 A1A9T A H14  1 
HETATM 6643 H  H5   C A1A9T E 3 .   ? 14.723 -1.007  6.308   0.18 16.35 ?  203 A1A9T A H5   1 
HETATM 6644 H  H6   C A1A9T E 3 .   ? 15.532 3.808   2.536   0.18 15.98 ?  203 A1A9T A H6   1 
HETATM 6645 H  H7   C A1A9T E 3 .   ? 15.962 5.199   4.852   0.18 15.81 ?  203 A1A9T A H7   1 
HETATM 6646 H  H4   C A1A9T E 3 .   ? 15.023 1.247   1.368   0.18 18.28 ?  203 A1A9T A H4   1 
HETATM 6647 H  H8   C A1A9T E 3 .   ? 15.741 3.649   6.755   0.18 15.53 ?  203 A1A9T A H8   1 
HETATM 6648 H  H1   C A1A9T E 3 .   ? 15.697 -3.370  2.744   0.18 20.00 ?  203 A1A9T A H1   1 
HETATM 6649 CL CL   B CL    F 4 .   ? 15.800 2.754   -1.276  0.36 20.03 ?  204 CL    A CL   1 
HETATM 6650 O  O    . HOH   G 5 .   ? 14.761 -4.661  20.464  1.00 45.95 ?  301 HOH   A O    1 
HETATM 6651 O  O    . HOH   G 5 .   ? 11.739 -10.853 -10.147 1.00 44.02 ?  302 HOH   A O    1 
HETATM 6652 O  O    . HOH   G 5 .   ? 14.648 -13.930 16.647  1.00 26.61 ?  303 HOH   A O    1 
HETATM 6653 O  O    . HOH   G 5 .   ? 18.596 -2.336  -16.369 1.00 45.43 ?  304 HOH   A O    1 
HETATM 6654 O  O    . HOH   G 5 .   ? 17.103 -18.029 14.979  1.00 26.66 ?  305 HOH   A O    1 
HETATM 6655 O  O    . HOH   G 5 .   ? 24.546 2.004   -6.992  1.00 20.88 ?  306 HOH   A O    1 
HETATM 6656 O  O    A HOH   G 5 .   ? 4.677  3.928   0.619   0.64 21.38 ?  307 HOH   A O    1 
HETATM 6657 O  O    . HOH   G 5 .   ? 7.974  -21.539 4.086   1.00 45.81 ?  308 HOH   A O    1 
HETATM 6658 O  O    . HOH   G 5 .   ? 34.346 -1.868  12.519  1.00 38.97 ?  309 HOH   A O    1 
HETATM 6659 O  O    . HOH   G 5 .   ? 0.805  -4.302  0.088   1.00 33.61 ?  310 HOH   A O    1 
HETATM 6660 O  O    . HOH   G 5 .   ? 13.558 -15.253 -7.523  1.00 26.61 ?  311 HOH   A O    1 
HETATM 6661 O  O    . HOH   G 5 .   ? 7.928  -12.582 -0.940  1.00 23.87 ?  312 HOH   A O    1 
HETATM 6662 O  O    . HOH   G 5 .   ? -0.403 -2.813  2.944   1.00 38.73 ?  313 HOH   A O    1 
HETATM 6663 O  O    . HOH   G 5 .   ? 8.898  -12.009 17.170  1.00 45.17 ?  314 HOH   A O    1 
HETATM 6664 O  O    . HOH   G 5 .   ? -0.606 -8.436  2.128   1.00 43.51 ?  315 HOH   A O    1 
HETATM 6665 O  O    B HOH   G 5 .   ? 5.298  3.952   0.473   0.36 30.08 ?  316 HOH   A O    1 
HETATM 6666 O  O    . HOH   G 5 .   ? 28.909 0.488   -9.717  1.00 23.35 ?  317 HOH   A O    1 
HETATM 6667 O  O    . HOH   G 5 .   ? 15.051 -12.217 18.649  1.00 39.81 ?  318 HOH   A O    1 
HETATM 6668 O  O    . HOH   G 5 .   ? 11.856 0.387   14.726  1.00 34.55 ?  319 HOH   A O    1 
HETATM 6669 O  O    . HOH   G 5 .   ? 14.967 3.929   17.635  1.00 41.10 ?  320 HOH   A O    1 
HETATM 6670 O  O    . HOH   G 5 .   ? 28.291 -0.126  -13.384 1.00 38.61 ?  321 HOH   A O    1 
HETATM 6671 O  O    . HOH   G 5 .   ? 19.910 -12.496 -8.892  1.00 27.51 ?  322 HOH   A O    1 
HETATM 6672 O  O    . HOH   G 5 .   ? 30.204 -13.314 -8.532  1.00 27.32 ?  323 HOH   A O    1 
HETATM 6673 O  O    A HOH   G 5 .   ? 14.619 -3.643  3.102   0.64 16.06 ?  324 HOH   A O    1 
HETATM 6674 O  O    . HOH   G 5 .   ? 42.417 10.537  5.079   1.00 20.20 ?  325 HOH   A O    1 
HETATM 6675 O  O    . HOH   G 5 .   ? 6.843  -8.017  11.807  1.00 19.99 ?  326 HOH   A O    1 
HETATM 6676 O  O    . HOH   G 5 .   ? 28.230 -6.276  19.598  1.00 41.48 ?  327 HOH   A O    1 
HETATM 6677 O  O    . HOH   G 5 .   ? 18.652 -19.373 13.569  1.00 38.24 ?  328 HOH   A O    1 
HETATM 6678 O  O    . HOH   G 5 .   ? 14.110 -4.535  -11.910 1.00 32.37 ?  329 HOH   A O    1 
HETATM 6679 O  O    . HOH   G 5 .   ? 9.851  -21.356 5.665   1.00 19.89 ?  330 HOH   A O    1 
HETATM 6680 O  O    . HOH   G 5 .   ? 34.000 -1.043  -8.897  1.00 28.22 ?  331 HOH   A O    1 
HETATM 6681 O  O    . HOH   G 5 .   ? 7.607  -6.143  -6.627  1.00 42.44 ?  332 HOH   A O    1 
HETATM 6682 O  O    . HOH   G 5 .   ? 26.481 -19.326 -1.769  1.00 15.73 ?  333 HOH   A O    1 
HETATM 6683 O  O    . HOH   G 5 .   ? 3.622  -9.402  9.687   1.00 29.06 ?  334 HOH   A O    1 
HETATM 6684 O  O    . HOH   G 5 .   ? 38.235 10.181  7.106   1.00 46.45 ?  335 HOH   A O    1 
HETATM 6685 O  O    . HOH   G 5 .   ? 27.280 13.774  2.875   1.00 31.37 ?  336 HOH   A O    1 
HETATM 6686 O  O    . HOH   G 5 .   ? 37.501 2.812   10.221  1.00 28.27 ?  337 HOH   A O    1 
HETATM 6687 O  O    . HOH   G 5 .   ? 22.180 -19.279 11.338  1.00 34.63 ?  338 HOH   A O    1 
HETATM 6688 O  O    . HOH   G 5 .   ? 31.026 -18.096 7.814   1.00 20.83 ?  339 HOH   A O    1 
HETATM 6689 O  O    . HOH   G 5 .   ? 44.303 7.167   6.370   1.00 26.95 ?  340 HOH   A O    1 
HETATM 6690 O  O    . HOH   G 5 .   ? 20.631 -19.764 -5.017  1.00 27.74 ?  341 HOH   A O    1 
HETATM 6691 O  O    . HOH   G 5 .   ? 9.167  -10.096 19.337  1.00 41.93 ?  342 HOH   A O    1 
HETATM 6692 O  O    A HOH   G 5 .   ? 14.259 0.586   6.803   0.64 19.30 ?  343 HOH   A O    1 
HETATM 6693 O  O    . HOH   G 5 .   ? 30.903 6.218   -12.277 1.00 28.15 ?  344 HOH   A O    1 
HETATM 6694 O  O    . HOH   G 5 .   ? 18.881 -21.981 7.044   1.00 34.37 ?  345 HOH   A O    1 
HETATM 6695 O  O    . HOH   G 5 .   ? 27.907 0.814   -7.130  1.00 15.05 ?  346 HOH   A O    1 
HETATM 6696 O  O    . HOH   G 5 .   ? 21.268 -2.284  -2.370  1.00 16.48 ?  347 HOH   A O    1 
HETATM 6697 O  O    . HOH   G 5 .   ? 15.203 -8.018  -9.875  1.00 23.58 ?  348 HOH   A O    1 
HETATM 6698 O  O    . HOH   G 5 .   ? 38.530 4.986   7.006   1.00 15.72 ?  349 HOH   A O    1 
HETATM 6699 O  O    . HOH   G 5 .   ? 13.911 -4.930  17.351  1.00 28.30 ?  350 HOH   A O    1 
HETATM 6700 O  O    . HOH   G 5 .   ? 39.731 -1.048  -5.148  1.00 22.32 ?  351 HOH   A O    1 
HETATM 6701 O  O    A HOH   G 5 .   ? 17.480 -1.703  0.446   0.82 26.01 ?  352 HOH   A O    1 
HETATM 6702 O  O    . HOH   G 5 .   ? 42.510 4.265   5.462   1.00 34.17 ?  353 HOH   A O    1 
HETATM 6703 O  O    . HOH   G 5 .   ? 22.255 5.363   19.014  1.00 40.78 ?  354 HOH   A O    1 
HETATM 6704 O  O    B HOH   G 5 .   ? 11.816 -1.593  -3.222  0.36 18.09 ?  355 HOH   A O    1 
HETATM 6705 O  O    . HOH   G 5 .   ? 36.247 -5.089  -0.530  1.00 32.61 ?  356 HOH   A O    1 
HETATM 6706 O  O    . HOH   G 5 .   ? 26.810 11.410  1.663   1.00 17.22 ?  357 HOH   A O    1 
HETATM 6707 O  O    . HOH   G 5 .   ? 35.762 -12.650 6.835   1.00 16.98 ?  358 HOH   A O    1 
HETATM 6708 O  O    . HOH   G 5 .   ? 28.593 -10.645 -14.001 1.00 44.29 ?  359 HOH   A O    1 
HETATM 6709 O  O    . HOH   G 5 .   ? 14.342 -21.226 -4.228  1.00 29.63 ?  360 HOH   A O    1 
HETATM 6710 O  O    . HOH   G 5 .   ? 31.646 8.184   14.862  1.00 25.01 ?  361 HOH   A O    1 
HETATM 6711 O  O    . HOH   G 5 .   ? 43.354 7.757   2.710   1.00 31.07 ?  362 HOH   A O    1 
HETATM 6712 O  O    . HOH   G 5 .   ? 17.143 -17.787 -5.026  1.00 26.92 ?  363 HOH   A O    1 
HETATM 6713 O  O    . HOH   G 5 .   ? 13.247 -1.463  -6.708  1.00 18.09 ?  364 HOH   A O    1 
HETATM 6714 O  O    . HOH   G 5 .   ? 24.012 -2.114  -2.081  1.00 11.61 ?  365 HOH   A O    1 
HETATM 6715 O  O    . HOH   G 5 .   ? 31.783 -9.371  -6.666  1.00 22.81 ?  366 HOH   A O    1 
HETATM 6716 O  O    . HOH   G 5 .   ? 30.797 3.087   8.277   1.00 13.01 ?  367 HOH   A O    1 
HETATM 6717 O  O    . HOH   G 5 .   ? 25.685 -0.769  -7.324  1.00 16.68 ?  368 HOH   A O    1 
HETATM 6718 O  O    . HOH   G 5 .   ? 21.200 10.192  15.003  1.00 34.43 ?  369 HOH   A O    1 
HETATM 6719 O  O    . HOH   G 5 .   ? 14.423 -24.670 11.546  1.00 39.98 ?  370 HOH   A O    1 
HETATM 6720 O  O    . HOH   G 5 .   ? 33.620 -7.146  4.328   1.00 17.72 ?  371 HOH   A O    1 
HETATM 6721 O  O    . HOH   G 5 .   ? 16.968 -19.266 4.875   1.00 16.78 ?  372 HOH   A O    1 
HETATM 6722 O  O    . HOH   G 5 .   ? 31.080 -13.940 -2.457  1.00 15.16 ?  373 HOH   A O    1 
HETATM 6723 O  O    . HOH   G 5 .   ? 37.292 11.977  4.940   1.00 31.16 ?  374 HOH   A O    1 
HETATM 6724 O  O    . HOH   G 5 .   ? 43.876 8.448   -3.054  1.00 26.80 ?  375 HOH   A O    1 
HETATM 6725 O  O    . HOH   G 5 .   ? 27.433 -10.609 14.075  1.00 18.87 ?  376 HOH   A O    1 
HETATM 6726 O  O    . HOH   G 5 .   ? 22.687 12.472  1.613   1.00 15.86 ?  377 HOH   A O    1 
HETATM 6727 O  O    . HOH   G 5 .   ? 24.214 -7.774  14.442  1.00 18.51 ?  378 HOH   A O    1 
HETATM 6728 O  O    . HOH   G 5 .   ? 18.871 -0.727  -1.699  1.00 15.80 ?  379 HOH   A O    1 
HETATM 6729 O  O    . HOH   G 5 .   ? 37.211 -2.912  9.719   1.00 42.07 ?  380 HOH   A O    1 
HETATM 6730 O  O    . HOH   G 5 .   ? 24.637 -17.473 12.804  1.00 25.71 ?  381 HOH   A O    1 
HETATM 6731 O  O    . HOH   G 5 .   ? 18.505 9.422   8.999   1.00 23.09 ?  382 HOH   A O    1 
HETATM 6732 O  O    . HOH   G 5 .   ? 6.398  -5.485  11.038  1.00 20.08 ?  383 HOH   A O    1 
HETATM 6733 O  O    . HOH   G 5 .   ? 21.865 -21.923 8.441   1.00 29.50 ?  384 HOH   A O    1 
HETATM 6734 O  O    T HOH   G 5 .   ? 15.391 -0.410  2.390   0.30 13.05 ?  385 HOH   A O    1 
HETATM 6735 O  O    . HOH   G 5 .   ? 24.364 3.570   -1.784  1.00 15.32 ?  386 HOH   A O    1 
HETATM 6736 O  O    . HOH   G 5 .   ? 16.505 -22.047 0.993   1.00 28.29 ?  387 HOH   A O    1 
HETATM 6737 O  O    B HOH   G 5 .   ? 15.088 -2.941  3.469   0.18 14.09 ?  388 HOH   A O    1 
HETATM 6738 O  O    . HOH   G 5 .   ? 33.502 -16.936 8.115   1.00 20.45 ?  389 HOH   A O    1 
HETATM 6739 O  O    . HOH   G 5 .   ? 37.526 -2.068  5.853   1.00 26.54 ?  390 HOH   A O    1 
HETATM 6740 O  O    . HOH   G 5 .   ? 20.046 4.529   -7.482  1.00 20.32 ?  391 HOH   A O    1 
HETATM 6741 O  O    . HOH   G 5 .   ? 22.599 -11.900 21.809  1.00 45.81 ?  392 HOH   A O    1 
HETATM 6742 O  O    . HOH   G 5 .   ? 32.753 -9.240  5.985   1.00 20.51 ?  393 HOH   A O    1 
HETATM 6743 O  O    . HOH   G 5 .   ? 31.785 -7.333  -9.845  1.00 23.02 ?  394 HOH   A O    1 
HETATM 6744 O  O    . HOH   G 5 .   ? 10.414 -22.313 -1.180  1.00 50.25 ?  395 HOH   A O    1 
HETATM 6745 O  O    . HOH   G 5 .   ? 14.055 -23.042 7.427   1.00 19.47 ?  396 HOH   A O    1 
HETATM 6746 O  O    . HOH   G 5 .   ? 21.283 3.013   -0.252  1.00 14.31 ?  397 HOH   A O    1 
HETATM 6747 O  O    . HOH   G 5 .   ? 27.471 -6.118  -13.976 1.00 38.13 ?  398 HOH   A O    1 
HETATM 6748 O  O    . HOH   G 5 .   ? 6.668  -3.183  12.731  1.00 29.50 ?  399 HOH   A O    1 
HETATM 6749 O  O    A HOH   G 5 .   ? 11.051 -0.369  1.937   0.34 20.82 ?  400 HOH   A O    1 
HETATM 6750 O  O    . HOH   G 5 .   ? 15.486 11.777  7.862   1.00 37.36 ?  401 HOH   A O    1 
HETATM 6751 O  O    B HOH   G 5 .   ? 12.029 6.673   9.942   0.36 27.28 ?  402 HOH   A O    1 
HETATM 6752 O  O    . HOH   G 5 .   ? 21.715 -13.812 -8.195  1.00 37.36 ?  403 HOH   A O    1 
HETATM 6753 O  O    A HOH   G 5 .   ? 15.784 -0.933  5.274   0.64 19.61 ?  404 HOH   A O    1 
HETATM 6754 O  O    . HOH   G 5 .   ? 23.905 -15.685 -9.159  1.00 37.99 ?  405 HOH   A O    1 
HETATM 6755 O  O    . HOH   G 5 .   ? 27.311 2.326   18.715  1.00 30.77 ?  406 HOH   A O    1 
HETATM 6756 O  O    . HOH   G 5 .   ? 15.183 -21.518 14.202  1.00 19.27 ?  407 HOH   A O    1 
HETATM 6757 O  O    . HOH   G 5 .   ? 23.438 11.369  4.097   1.00 13.31 ?  408 HOH   A O    1 
HETATM 6758 O  O    B HOH   G 5 .   ? 10.874 2.404   11.873  0.36 24.83 ?  409 HOH   A O    1 
HETATM 6759 O  O    . HOH   G 5 .   ? 15.845 2.095   24.707  1.00 42.56 ?  410 HOH   A O    1 
HETATM 6760 O  O    . HOH   G 5 .   ? 20.524 -20.006 2.794   1.00 20.35 ?  411 HOH   A O    1 
HETATM 6761 O  O    . HOH   G 5 .   ? 30.678 1.875   16.694  1.00 22.11 ?  412 HOH   A O    1 
HETATM 6762 O  O    . HOH   G 5 .   ? 23.993 3.942   -4.806  1.00 22.04 ?  413 HOH   A O    1 
HETATM 6763 O  O    . HOH   G 5 .   ? 14.499 -0.536  -12.181 1.00 23.22 ?  414 HOH   A O    1 
HETATM 6764 O  O    . HOH   G 5 .   ? 26.904 4.165   -0.646  1.00 13.22 ?  415 HOH   A O    1 
HETATM 6765 O  O    . HOH   G 5 .   ? 16.185 16.634  8.616   1.00 32.98 ?  416 HOH   A O    1 
HETATM 6766 O  O    . HOH   G 5 .   ? 30.042 -10.093 13.031  1.00 24.04 ?  417 HOH   A O    1 
HETATM 6767 O  O    . HOH   G 5 .   ? 40.880 -8.205  -6.811  1.00 36.34 ?  418 HOH   A O    1 
HETATM 6768 O  O    . HOH   G 5 .   ? 38.071 -1.337  -1.910  1.00 19.81 ?  419 HOH   A O    1 
HETATM 6769 O  O    . HOH   G 5 .   ? 32.653 -4.291  -9.842  1.00 29.49 ?  420 HOH   A O    1 
HETATM 6770 O  O    . HOH   G 5 .   ? 23.923 -20.274 -1.347  1.00 18.44 ?  421 HOH   A O    1 
HETATM 6771 O  O    . HOH   G 5 .   ? 30.313 -12.911 13.507  1.00 21.76 ?  422 HOH   A O    1 
HETATM 6772 O  O    . HOH   G 5 .   ? 15.979 6.865   2.928   1.00 20.01 ?  423 HOH   A O    1 
HETATM 6773 O  O    . HOH   G 5 .   ? 41.575 1.448   5.033   1.00 36.36 ?  424 HOH   A O    1 
HETATM 6774 O  O    . HOH   G 5 .   ? 10.363 -13.707 -1.687  1.00 18.26 ?  425 HOH   A O    1 
HETATM 6775 O  O    . HOH   G 5 .   ? 35.084 -5.227  -3.083  1.00 19.12 ?  426 HOH   A O    1 
HETATM 6776 O  O    . HOH   G 5 .   ? 36.714 -4.934  5.408   1.00 26.01 ?  427 HOH   A O    1 
HETATM 6777 O  O    . HOH   G 5 .   ? 32.502 -10.637 3.227   1.00 32.41 ?  428 HOH   A O    1 
HETATM 6778 O  O    . HOH   G 5 .   ? 5.414  2.907   4.897   1.00 36.21 ?  429 HOH   A O    1 
HETATM 6779 O  O    . HOH   G 5 .   ? 16.204 -14.194 20.134  1.00 50.33 ?  430 HOH   A O    1 
HETATM 6780 O  O    A HOH   G 5 .   ? 11.019 1.565   12.755  0.64 21.82 ?  431 HOH   A O    1 
HETATM 6781 O  O    . HOH   G 5 .   ? 44.980 -0.631  3.020   1.00 41.04 ?  432 HOH   A O    1 
HETATM 6782 O  O    . HOH   G 5 .   ? 19.427 -11.022 23.979  1.00 65.88 ?  433 HOH   A O    1 
HETATM 6783 O  O    . HOH   G 5 .   ? -1.440 -5.002  7.530   1.00 47.78 ?  434 HOH   A O    1 
HETATM 6784 O  O    . HOH   G 5 .   ? 11.667 -10.709 16.960  1.00 26.35 ?  435 HOH   A O    1 
HETATM 6785 O  O    . HOH   G 5 .   ? 18.335 -15.988 16.339  1.00 39.04 ?  436 HOH   A O    1 
HETATM 6786 O  O    . HOH   G 5 .   ? 22.625 8.164   18.396  1.00 47.61 ?  437 HOH   A O    1 
HETATM 6787 O  O    . HOH   G 5 .   ? 27.060 -3.137  19.367  1.00 36.43 ?  438 HOH   A O    1 
HETATM 6788 O  O    . HOH   G 5 .   ? 23.373 -20.911 1.354   1.00 20.62 ?  439 HOH   A O    1 
HETATM 6789 O  O    . HOH   G 5 .   ? 9.482  -16.306 -1.987  1.00 43.94 ?  440 HOH   A O    1 
HETATM 6790 O  O    . HOH   G 5 .   ? 37.714 -8.826  -3.427  1.00 24.70 ?  441 HOH   A O    1 
HETATM 6791 O  O    . HOH   G 5 .   ? 18.478 4.967   -15.133 1.00 49.57 ?  442 HOH   A O    1 
HETATM 6792 O  O    . HOH   G 5 .   ? 23.478 -8.032  17.084  1.00 23.53 ?  443 HOH   A O    1 
HETATM 6793 O  O    . HOH   G 5 .   ? 18.788 1.959   -0.694  1.00 14.69 ?  444 HOH   A O    1 
HETATM 6794 O  O    . HOH   G 5 .   ? 34.394 -8.108  -0.551  1.00 31.09 ?  445 HOH   A O    1 
HETATM 6795 O  O    A HOH   G 5 .   ? 14.011 -0.327  3.465   0.34 28.08 ?  446 HOH   A O    1 
HETATM 6796 O  O    . HOH   G 5 .   ? 21.275 -9.270  21.364  1.00 48.62 ?  447 HOH   A O    1 
HETATM 6797 O  O    A HOH   G 5 .   ? 16.242 2.958   -1.438  0.64 15.75 ?  448 HOH   A O    1 
HETATM 6798 O  O    . HOH   G 5 .   ? 30.566 14.745  2.759   1.00 19.16 ?  449 HOH   A O    1 
HETATM 6799 O  O    . HOH   G 5 .   ? 29.759 -1.925  -12.691 1.00 44.68 ?  450 HOH   A O    1 
HETATM 6800 O  O    . HOH   G 5 .   ? 31.322 -12.769 0.011   1.00 21.11 ?  451 HOH   A O    1 
HETATM 6801 O  O    . HOH   G 5 .   ? 23.175 7.598   -3.239  1.00 30.96 ?  452 HOH   A O    1 
HETATM 6802 O  O    . HOH   G 5 .   ? 20.604 -17.739 24.825  1.00 49.99 ?  453 HOH   A O    1 
HETATM 6803 O  O    . HOH   G 5 .   ? 21.438 -14.739 17.910  1.00 51.24 ?  454 HOH   A O    1 
HETATM 6804 O  O    B HOH   G 5 .   ? 3.165  3.259   -1.693  0.36 28.05 ?  455 HOH   A O    1 
HETATM 6805 O  O    . HOH   G 5 .   ? 27.733 6.989   -6.532  1.00 36.33 ?  456 HOH   A O    1 
HETATM 6806 O  O    . HOH   G 5 .   ? 29.827 -16.064 10.808  1.00 36.53 ?  457 HOH   A O    1 
HETATM 6807 O  O    . HOH   G 5 .   ? 32.462 -15.898 10.861  1.00 30.84 ?  458 HOH   A O    1 
HETATM 6808 O  O    . HOH   G 5 .   ? 25.386 8.256   -4.854  1.00 29.79 ?  459 HOH   A O    1 
HETATM 6809 O  O    . HOH   G 5 .   ? 24.812 5.598   20.756  1.00 52.76 ?  460 HOH   A O    1 
HETATM 6810 O  O    B HOH   G 5 .   ? 10.881 -0.005  -1.359  0.36 24.93 ?  461 HOH   A O    1 
HETATM 6811 O  O    . HOH   G 5 .   ? 19.865 -17.336 -5.031  1.00 24.83 ?  462 HOH   A O    1 
HETATM 6812 O  O    . HOH   G 5 .   ? 23.239 -22.335 -3.251  1.00 39.15 ?  463 HOH   A O    1 
HETATM 6813 O  O    . HOH   G 5 .   ? 24.624 14.641  7.764   1.00 36.71 ?  464 HOH   A O    1 
HETATM 6814 O  O    . HOH   G 5 .   ? 18.088 -16.325 -8.834  1.00 40.17 ?  465 HOH   A O    1 
HETATM 6815 O  O    . HOH   G 5 .   ? 8.035  -3.198  -5.829  1.00 52.27 ?  466 HOH   A O    1 
HETATM 6816 O  O    . HOH   G 5 .   ? 21.822 5.152   -5.834  1.00 32.20 ?  467 HOH   A O    1 
HETATM 6817 O  O    . HOH   G 5 .   ? 39.613 -7.050  -3.520  1.00 47.24 ?  468 HOH   A O    1 
HETATM 6818 O  O    . HOH   G 5 .   ? 15.696 -21.500 3.680   1.00 24.54 ?  469 HOH   A O    1 
HETATM 6819 O  O    . HOH   G 5 .   ? 18.721 10.818  11.282  1.00 32.83 ?  470 HOH   A O    1 
HETATM 6820 O  O    . HOH   G 5 .   ? 12.366 1.659   17.303  1.00 39.31 ?  471 HOH   A O    1 
HETATM 6821 O  O    . HOH   G 5 .   ? 27.449 -11.365 16.585  1.00 39.31 ?  472 HOH   A O    1 
HETATM 6822 O  O    . HOH   G 5 .   ? 11.046 -15.011 -6.094  1.00 34.29 ?  473 HOH   A O    1 
HETATM 6823 O  O    . HOH   G 5 .   ? 26.903 11.620  -1.340  1.00 33.60 ?  474 HOH   A O    1 
HETATM 6824 O  O    . HOH   G 5 .   ? 15.775 -17.133 -6.949  1.00 32.23 ?  475 HOH   A O    1 
HETATM 6825 O  O    . HOH   G 5 .   ? 11.964 -13.406 16.341  1.00 51.22 ?  476 HOH   A O    1 
HETATM 6826 O  O    . HOH   G 5 .   ? 23.447 13.708  5.533   1.00 19.27 ?  477 HOH   A O    1 
HETATM 6827 O  O    . HOH   G 5 .   ? 25.805 10.771  -3.708  1.00 25.30 ?  478 HOH   A O    1 
HETATM 6828 O  O    . HOH   G 5 .   ? 16.784 -20.509 16.110  1.00 28.95 ?  479 HOH   A O    1 
HETATM 6829 O  O    . HOH   G 5 .   ? 28.531 -4.652  -12.311 1.00 38.24 ?  480 HOH   A O    1 
HETATM 6830 O  O    . HOH   G 5 .   ? 35.131 7.446   12.229  1.00 45.94 ?  481 HOH   A O    1 
HETATM 6831 O  O    . HOH   G 5 .   ? 13.973 -10.359 -10.908 1.00 32.67 ?  482 HOH   A O    1 
HETATM 6832 O  O    . HOH   G 5 .   ? 28.805 9.025   17.496  1.00 38.02 ?  483 HOH   A O    1 
HETATM 6833 O  O    . HOH   G 5 .   ? 15.967 -6.737  -11.922 1.00 46.97 ?  484 HOH   A O    1 
HETATM 6834 O  O    . HOH   G 5 .   ? 41.062 -3.926  -0.421  1.00 37.55 ?  485 HOH   A O    1 
HETATM 6835 O  O    . HOH   G 5 .   ? 17.351 -18.722 19.864  1.00 51.45 ?  486 HOH   A O    1 
HETATM 6836 O  O    . HOH   G 5 .   ? 44.467 10.318  -1.734  1.00 34.12 ?  487 HOH   A O    1 
HETATM 6837 O  O    . HOH   G 5 .   ? 30.880 0.708   19.127  1.00 41.98 ?  488 HOH   A O    1 
HETATM 6838 O  O    . HOH   G 5 .   ? 28.661 -7.993  -15.220 1.00 51.77 ?  489 HOH   A O    1 
HETATM 6839 O  O    . HOH   G 5 .   ? 23.103 11.823  -4.050  1.00 20.17 ?  490 HOH   A O    1 
HETATM 6840 O  O    . HOH   G 5 .   ? 41.703 9.310   -3.936  1.00 32.16 ?  491 HOH   A O    1 
HETATM 6841 O  O    . HOH   G 5 .   ? 39.133 2.433   7.372   1.00 32.04 ?  492 HOH   A O    1 
HETATM 6842 O  O    . HOH   G 5 .   ? 18.422 -23.153 1.912   1.00 44.86 ?  493 HOH   A O    1 
HETATM 6843 O  O    . HOH   G 5 .   ? 31.435 -0.551  -10.567 1.00 31.29 ?  494 HOH   A O    1 
HETATM 6844 O  O    . HOH   G 5 .   ? 23.250 -12.784 19.351  1.00 45.12 ?  495 HOH   A O    1 
HETATM 6845 O  O    . HOH   G 5 .   ? 20.497 -16.054 -7.407  1.00 29.34 ?  496 HOH   A O    1 
HETATM 6846 O  O    . HOH   G 5 .   ? 13.870 -25.219 8.888   1.00 34.00 ?  497 HOH   A O    1 
HETATM 6847 O  O    . HOH   G 5 .   ? 40.575 -0.268  -7.754  1.00 33.66 ?  498 HOH   A O    1 
HETATM 6848 O  O    . HOH   G 5 .   ? 16.184 -23.361 5.774   1.00 29.42 ?  499 HOH   A O    1 
HETATM 6849 O  O    . HOH   G 5 .   ? 20.055 -22.358 4.245   1.00 30.16 ?  500 HOH   A O    1 
HETATM 6850 O  O    . HOH   G 5 .   ? 30.685 5.794   -14.728 1.00 35.91 ?  501 HOH   A O    1 
HETATM 6851 O  O    . HOH   G 5 .   ? 30.712 -5.777  -11.851 1.00 49.55 ?  502 HOH   A O    1 
HETATM 6852 O  O    . HOH   G 5 .   ? 37.382 -6.644  7.646   1.00 26.50 ?  503 HOH   A O    1 
HETATM 6853 O  O    . HOH   G 5 .   ? 39.521 -0.006  6.638   1.00 30.48 ?  504 HOH   A O    1 
HETATM 6854 O  O    B HOH   G 5 .   ? 14.837 7.901   4.648   0.36 28.73 ?  505 HOH   A O    1 
HETATM 6855 O  O    . HOH   G 5 .   ? 29.003 14.401  0.855   1.00 48.65 ?  506 HOH   A O    1 
HETATM 6856 O  O    . HOH   G 5 .   ? 37.968 13.959  6.671   1.00 45.30 ?  507 HOH   A O    1 
HETATM 6857 O  O    . HOH   G 5 .   ? 36.419 -6.471  10.170  1.00 48.18 ?  508 HOH   A O    1 
HETATM 6858 O  O    . HOH   G 5 .   ? 22.010 -23.997 4.528   1.00 26.87 ?  509 HOH   A O    1 
HETATM 6859 O  O    T HOH   G 5 .   ? 11.905 -2.139  -3.650  0.30 11.67 ?  510 HOH   A O    1 
HETATM 6860 O  O    . HOH   G 5 .   ? 17.340 -6.577  -14.190 1.00 42.49 ?  511 HOH   A O    1 
HETATM 6861 O  O    A HOH   G 5 .   ? 14.833 8.663   4.891   0.64 41.81 ?  512 HOH   A O    1 
HETATM 6862 O  O    . HOH   G 5 .   ? 24.053 8.998   -7.234  1.00 37.57 ?  513 HOH   A O    1 
HETATM 6863 O  O    . HOH   G 5 .   ? 16.316 -21.083 18.743  1.00 39.49 ?  514 HOH   A O    1 
HETATM 6864 O  O    . HOH   G 5 .   ? 15.820 -12.266 27.353  1.00 44.32 ?  515 HOH   A O    1 
HETATM 6865 O  O    . HOH   G 5 .   ? 14.689 -22.708 19.803  1.00 35.70 ?  516 HOH   A O    1 
HETATM 6866 O  O    . HOH   H 5 .   ? 29.857 -22.428 5.525   1.00 21.53 ?  201 HOH   B O    1 
HETATM 6867 O  O    . HOH   H 5 .   ? 27.699 -29.154 -1.878  1.00 36.09 ?  202 HOH   B O    1 
HETATM 6868 O  O    . HOH   H 5 .   ? 41.647 -36.030 -17.066 1.00 35.12 ?  203 HOH   B O    1 
HETATM 6869 O  O    . HOH   H 5 .   ? 29.982 -26.269 4.142   1.00 29.04 ?  204 HOH   B O    1 
HETATM 6870 O  O    . HOH   H 5 .   ? 49.329 -22.730 -19.765 1.00 48.58 ?  205 HOH   B O    1 
HETATM 6871 O  O    . HOH   H 5 .   ? 52.935 -13.442 -20.261 1.00 35.98 ?  206 HOH   B O    1 
HETATM 6872 O  O    . HOH   H 5 .   ? 59.125 -18.727 6.842   1.00 36.25 ?  207 HOH   B O    1 
HETATM 6873 O  O    . HOH   H 5 .   ? 41.357 -7.784  5.443   1.00 39.60 ?  208 HOH   B O    1 
HETATM 6874 O  O    . HOH   H 5 .   ? 30.219 -40.998 -8.064  1.00 18.09 ?  209 HOH   B O    1 
HETATM 6875 O  O    . HOH   H 5 .   ? 58.183 -12.863 8.424   1.00 32.72 ?  210 HOH   B O    1 
HETATM 6876 O  O    . HOH   H 5 .   ? 56.327 -19.705 7.313   1.00 31.29 ?  211 HOH   B O    1 
HETATM 6877 O  O    . HOH   H 5 .   ? 54.495 -9.385  -8.671  1.00 19.78 ?  212 HOH   B O    1 
HETATM 6878 O  O    . HOH   H 5 .   ? 30.942 -28.762 4.368   1.00 29.03 ?  213 HOH   B O    1 
HETATM 6879 O  O    . HOH   H 5 .   ? 27.876 -41.816 -15.145 1.00 35.69 ?  214 HOH   B O    1 
HETATM 6880 O  O    . HOH   H 5 .   ? 56.671 -30.740 -7.758  1.00 33.87 ?  215 HOH   B O    1 
HETATM 6881 O  O    . HOH   H 5 .   ? 50.177 -3.335  7.143   1.00 37.59 ?  216 HOH   B O    1 
HETATM 6882 O  O    . HOH   H 5 .   ? 37.126 -19.815 -18.138 1.00 38.74 ?  217 HOH   B O    1 
HETATM 6883 O  O    . HOH   H 5 .   ? 47.386 -7.408  -3.847  1.00 39.16 ?  218 HOH   B O    1 
HETATM 6884 O  O    . HOH   H 5 .   ? 38.058 -39.459 -0.159  1.00 41.09 ?  219 HOH   B O    1 
HETATM 6885 O  O    . HOH   H 5 .   ? 47.990 -6.929  15.533  1.00 39.49 ?  220 HOH   B O    1 
HETATM 6886 O  O    . HOH   H 5 .   ? 41.512 -39.163 -14.847 1.00 22.59 ?  221 HOH   B O    1 
HETATM 6887 O  O    . HOH   H 5 .   ? 34.906 -24.634 13.796  1.00 34.80 ?  222 HOH   B O    1 
HETATM 6888 O  O    . HOH   H 5 .   ? 44.426 -7.173  2.027   1.00 34.02 ?  223 HOH   B O    1 
HETATM 6889 O  O    . HOH   H 5 .   ? 57.181 -26.927 -7.634  1.00 40.93 ?  224 HOH   B O    1 
HETATM 6890 O  O    . HOH   H 5 .   ? 34.522 -36.379 -7.169  1.00 19.90 ?  225 HOH   B O    1 
HETATM 6891 O  O    . HOH   H 5 .   ? 57.716 -24.493 5.049   1.00 35.82 ?  226 HOH   B O    1 
HETATM 6892 O  O    . HOH   H 5 .   ? 48.558 -36.485 -15.442 1.00 44.62 ?  227 HOH   B O    1 
HETATM 6893 O  O    . HOH   H 5 .   ? 55.341 -16.497 -14.313 1.00 31.02 ?  228 HOH   B O    1 
HETATM 6894 O  O    . HOH   H 5 .   ? 50.735 -6.078  0.142   1.00 27.13 ?  229 HOH   B O    1 
HETATM 6895 O  O    . HOH   H 5 .   ? 57.380 -16.260 -12.227 1.00 19.00 ?  230 HOH   B O    1 
HETATM 6896 O  O    . HOH   H 5 .   ? 51.660 -6.461  4.371   1.00 20.19 ?  231 HOH   B O    1 
HETATM 6897 O  O    . HOH   H 5 .   ? 32.789 -43.771 -11.268 1.00 22.65 ?  232 HOH   B O    1 
HETATM 6898 O  O    . HOH   H 5 .   ? 40.633 -16.035 14.099  1.00 23.54 ?  233 HOH   B O    1 
HETATM 6899 O  O    . HOH   H 5 .   ? 38.525 -11.038 -2.278  1.00 19.73 ?  234 HOH   B O    1 
HETATM 6900 O  O    . HOH   H 5 .   ? 35.089 -7.997  -2.996  1.00 18.60 ?  235 HOH   B O    1 
HETATM 6901 O  O    . HOH   H 5 .   ? 41.345 -9.600  13.027  1.00 22.25 ?  236 HOH   B O    1 
HETATM 6902 O  O    . HOH   H 5 .   ? 29.840 -34.143 -0.426  1.00 38.03 ?  237 HOH   B O    1 
HETATM 6903 O  O    . HOH   H 5 .   ? 48.031 -24.580 -17.728 1.00 32.39 ?  238 HOH   B O    1 
HETATM 6904 O  O    . HOH   H 5 .   ? 44.866 -43.569 -10.490 1.00 28.22 ?  239 HOH   B O    1 
HETATM 6905 O  O    . HOH   H 5 .   ? 39.299 -10.875 6.124   1.00 26.35 ?  240 HOH   B O    1 
HETATM 6906 O  O    . HOH   H 5 .   ? 25.409 -25.929 -1.252  1.00 33.91 ?  241 HOH   B O    1 
HETATM 6907 O  O    . HOH   H 5 .   ? 46.415 -1.539  13.170  1.00 27.36 ?  242 HOH   B O    1 
HETATM 6908 O  O    . HOH   H 5 .   ? 57.611 -24.356 -3.770  1.00 21.42 ?  243 HOH   B O    1 
HETATM 6909 O  O    . HOH   H 5 .   ? 42.568 -25.359 2.679   1.00 16.44 ?  244 HOH   B O    1 
HETATM 6910 O  O    . HOH   H 5 .   ? 43.047 -43.226 -8.165  1.00 29.91 ?  245 HOH   B O    1 
HETATM 6911 O  O    . HOH   H 5 .   ? 44.513 -27.725 -0.659  1.00 22.55 ?  246 HOH   B O    1 
HETATM 6912 O  O    . HOH   H 5 .   ? 50.739 -12.975 -0.452  1.00 12.74 ?  247 HOH   B O    1 
HETATM 6913 O  O    . HOH   H 5 .   ? 42.637 -22.849 3.858   1.00 12.83 ?  248 HOH   B O    1 
HETATM 6914 O  O    . HOH   H 5 .   ? 28.392 -19.683 -13.087 1.00 25.87 ?  249 HOH   B O    1 
HETATM 6915 O  O    . HOH   H 5 .   ? 51.554 -13.855 11.036  1.00 26.85 ?  250 HOH   B O    1 
HETATM 6916 O  O    . HOH   H 5 .   ? 50.939 -39.960 -8.147  1.00 36.42 ?  251 HOH   B O    1 
HETATM 6917 O  O    . HOH   H 5 .   ? 45.182 -35.018 6.839   1.00 42.20 ?  252 HOH   B O    1 
HETATM 6918 O  O    . HOH   H 5 .   ? 39.514 -11.110 0.324   1.00 17.72 ?  253 HOH   B O    1 
HETATM 6919 O  O    . HOH   H 5 .   ? 31.798 -17.905 -14.449 1.00 31.60 ?  254 HOH   B O    1 
HETATM 6920 O  O    . HOH   H 5 .   ? 58.170 -10.649 -4.054  1.00 21.09 ?  255 HOH   B O    1 
HETATM 6921 O  O    . HOH   H 5 .   ? 40.350 -12.759 -11.499 1.00 16.08 ?  256 HOH   B O    1 
HETATM 6922 O  O    . HOH   H 5 .   ? 29.708 -25.207 -10.743 1.00 18.54 ?  257 HOH   B O    1 
HETATM 6923 O  O    . HOH   H 5 .   ? 43.177 -32.383 -17.031 1.00 25.40 ?  258 HOH   B O    1 
HETATM 6924 O  O    . HOH   H 5 .   ? 34.243 -18.418 11.442  1.00 26.88 ?  259 HOH   B O    1 
HETATM 6925 O  O    . HOH   H 5 .   ? 28.473 -30.884 -14.695 1.00 32.32 ?  260 HOH   B O    1 
HETATM 6926 O  O    . HOH   H 5 .   ? 27.115 -31.816 -9.898  1.00 21.43 ?  261 HOH   B O    1 
HETATM 6927 O  O    . HOH   H 5 .   ? 36.010 -43.348 -8.357  1.00 35.91 ?  262 HOH   B O    1 
HETATM 6928 O  O    . HOH   H 5 .   ? 30.854 -15.712 2.681   1.00 15.29 ?  263 HOH   B O    1 
HETATM 6929 O  O    . HOH   H 5 .   ? 56.144 -23.587 -14.693 1.00 26.90 ?  264 HOH   B O    1 
HETATM 6930 O  O    . HOH   H 5 .   ? 48.015 -22.766 5.841   1.00 18.50 ?  265 HOH   B O    1 
HETATM 6931 O  O    . HOH   H 5 .   ? 41.866 -23.500 9.292   1.00 19.40 ?  266 HOH   B O    1 
HETATM 6932 O  O    . HOH   H 5 .   ? 57.459 -9.215  1.408   1.00 20.35 ?  267 HOH   B O    1 
HETATM 6933 O  O    . HOH   H 5 .   ? 34.953 -33.298 -19.150 1.00 31.60 ?  268 HOH   B O    1 
HETATM 6934 O  O    . HOH   H 5 .   ? 46.620 -31.254 -4.788  1.00 25.19 ?  269 HOH   B O    1 
HETATM 6935 O  O    . HOH   H 5 .   ? 42.343 -9.902  9.339   1.00 21.30 ?  270 HOH   B O    1 
HETATM 6936 O  O    . HOH   H 5 .   ? 49.301 -28.697 -6.870  1.00 16.51 ?  271 HOH   B O    1 
HETATM 6937 O  O    . HOH   H 5 .   ? 49.717 -0.440  10.201  1.00 31.33 ?  272 HOH   B O    1 
HETATM 6938 O  O    . HOH   H 5 .   ? 38.892 -11.959 12.397  1.00 36.95 ?  273 HOH   B O    1 
HETATM 6939 O  O    . HOH   H 5 .   ? 56.938 -8.641  8.437   1.00 20.16 ?  274 HOH   B O    1 
HETATM 6940 O  O    . HOH   H 5 .   ? 43.391 -15.780 -12.176 1.00 15.14 ?  275 HOH   B O    1 
HETATM 6941 O  O    . HOH   H 5 .   ? 42.384 -34.682 3.811   1.00 27.30 ?  276 HOH   B O    1 
HETATM 6942 O  O    . HOH   H 5 .   ? 46.884 -29.572 9.836   1.00 34.84 ?  277 HOH   B O    1 
HETATM 6943 O  O    . HOH   H 5 .   ? 34.466 -12.769 2.643   1.00 26.36 ?  278 HOH   B O    1 
HETATM 6944 O  O    . HOH   H 5 .   ? 30.496 -42.268 -10.570 1.00 31.44 ?  279 HOH   B O    1 
HETATM 6945 O  O    . HOH   H 5 .   ? 28.247 -34.339 -9.359  1.00 19.97 ?  280 HOH   B O    1 
HETATM 6946 O  O    . HOH   H 5 .   ? 27.956 -22.876 -7.965  1.00 19.02 ?  281 HOH   B O    1 
HETATM 6947 O  O    . HOH   H 5 .   ? 42.917 -20.285 -20.738 1.00 40.76 ?  282 HOH   B O    1 
HETATM 6948 O  O    . HOH   H 5 .   ? 48.401 -25.035 3.128   1.00 14.67 ?  283 HOH   B O    1 
HETATM 6949 O  O    . HOH   H 5 .   ? 45.309 -33.392 -15.869 1.00 25.51 ?  284 HOH   B O    1 
HETATM 6950 O  O    . HOH   H 5 .   ? 59.761 -15.260 8.149   1.00 32.58 ?  285 HOH   B O    1 
HETATM 6951 O  O    . HOH   H 5 .   ? 41.171 -5.462  11.500  1.00 44.49 ?  286 HOH   B O    1 
HETATM 6952 O  O    . HOH   H 5 .   ? 27.562 -26.690 -15.601 1.00 33.42 ?  287 HOH   B O    1 
HETATM 6953 O  O    . HOH   H 5 .   ? 49.992 -24.625 5.823   1.00 34.72 ?  288 HOH   B O    1 
HETATM 6954 O  O    . HOH   H 5 .   ? 48.699 -20.034 5.948   1.00 14.82 ?  289 HOH   B O    1 
HETATM 6955 O  O    . HOH   H 5 .   ? 36.838 -12.760 -1.493  1.00 27.97 ?  290 HOH   B O    1 
HETATM 6956 O  O    . HOH   H 5 .   ? 33.524 -15.290 -13.928 1.00 22.83 ?  291 HOH   B O    1 
HETATM 6957 O  O    . HOH   H 5 .   ? 47.054 -33.982 -4.595  1.00 18.82 ?  292 HOH   B O    1 
HETATM 6958 O  O    . HOH   H 5 .   ? 42.792 -12.242 -18.492 1.00 28.28 ?  293 HOH   B O    1 
HETATM 6959 O  O    . HOH   H 5 .   ? 37.501 -18.042 13.099  1.00 32.97 ?  294 HOH   B O    1 
HETATM 6960 O  O    . HOH   H 5 .   ? 45.905 -40.413 -3.600  1.00 30.96 ?  295 HOH   B O    1 
HETATM 6961 O  O    . HOH   H 5 .   ? 52.516 -10.382 13.006  1.00 23.21 ?  296 HOH   B O    1 
HETATM 6962 O  O    . HOH   H 5 .   ? 42.354 -9.908  -14.878 1.00 37.49 ?  297 HOH   B O    1 
HETATM 6963 O  O    . HOH   H 5 .   ? 51.213 -37.588 -9.619  1.00 27.82 ?  298 HOH   B O    1 
HETATM 6964 O  O    . HOH   H 5 .   ? 52.566 -35.654 -8.636  1.00 30.98 ?  299 HOH   B O    1 
HETATM 6965 O  O    . HOH   H 5 .   ? 52.987 -15.986 -12.722 1.00 26.58 ?  300 HOH   B O    1 
HETATM 6966 O  O    . HOH   H 5 .   ? 44.622 -27.449 2.018   1.00 17.12 ?  301 HOH   B O    1 
HETATM 6967 O  O    . HOH   H 5 .   ? 57.108 -12.023 12.393  1.00 38.27 ?  302 HOH   B O    1 
HETATM 6968 O  O    . HOH   H 5 .   ? 53.464 -30.191 4.509   1.00 19.91 ?  303 HOH   B O    1 
HETATM 6969 O  O    . HOH   H 5 .   ? 35.063 -33.594 4.597   1.00 32.40 ?  304 HOH   B O    1 
HETATM 6970 O  O    . HOH   H 5 .   ? 40.263 -10.846 -9.522  1.00 18.17 ?  305 HOH   B O    1 
HETATM 6971 O  O    . HOH   H 5 .   ? 48.590 -12.069 -14.267 1.00 27.30 ?  306 HOH   B O    1 
HETATM 6972 O  O    . HOH   H 5 .   ? 62.703 -13.575 4.789   1.00 26.87 ?  307 HOH   B O    1 
HETATM 6973 O  O    . HOH   H 5 .   ? 44.041 -29.336 -4.625  1.00 23.54 ?  308 HOH   B O    1 
HETATM 6974 O  O    . HOH   H 5 .   ? 53.654 -12.578 -22.173 1.00 35.21 ?  309 HOH   B O    1 
HETATM 6975 O  O    . HOH   H 5 .   ? 52.503 -29.257 -13.024 1.00 26.01 ?  310 HOH   B O    1 
HETATM 6976 O  O    . HOH   H 5 .   ? 25.959 -21.465 -3.501  1.00 18.20 ?  311 HOH   B O    1 
HETATM 6977 O  O    . HOH   H 5 .   ? 37.861 -10.242 -10.754 1.00 18.58 ?  312 HOH   B O    1 
HETATM 6978 O  O    . HOH   H 5 .   ? 37.085 -30.612 -20.940 1.00 32.78 ?  313 HOH   B O    1 
HETATM 6979 O  O    . HOH   H 5 .   ? 37.315 -35.697 7.256   1.00 34.95 ?  314 HOH   B O    1 
HETATM 6980 O  O    . HOH   H 5 .   ? 43.195 -21.410 10.712  1.00 17.58 ?  315 HOH   B O    1 
HETATM 6981 O  O    . HOH   H 5 .   ? 32.803 -34.591 -5.855  1.00 18.23 ?  316 HOH   B O    1 
HETATM 6982 O  O    . HOH   H 5 .   ? 41.771 -8.045  1.394   1.00 25.37 ?  317 HOH   B O    1 
HETATM 6983 O  O    . HOH   H 5 .   ? 38.328 -12.704 7.941   1.00 19.70 ?  318 HOH   B O    1 
HETATM 6984 O  O    . HOH   H 5 .   ? 26.334 -21.031 -6.205  1.00 18.15 ?  319 HOH   B O    1 
HETATM 6985 O  O    . HOH   H 5 .   ? 51.728 -5.987  -7.876  1.00 45.12 ?  320 HOH   B O    1 
HETATM 6986 O  O    . HOH   H 5 .   ? 62.852 -20.163 -0.731  1.00 36.74 ?  321 HOH   B O    1 
HETATM 6987 O  O    . HOH   H 5 .   ? 51.407 -33.004 -10.781 1.00 41.25 ?  322 HOH   B O    1 
HETATM 6988 O  O    . HOH   H 5 .   ? 48.051 -32.623 -16.625 1.00 43.45 ?  323 HOH   B O    1 
HETATM 6989 O  O    . HOH   H 5 .   ? 59.948 -17.207 -10.479 1.00 34.22 ?  324 HOH   B O    1 
HETATM 6990 O  O    . HOH   H 5 .   ? 36.717 -12.404 4.293   1.00 18.89 ?  325 HOH   B O    1 
HETATM 6991 O  O    . HOH   H 5 .   ? 44.656 -24.587 9.593   1.00 21.77 ?  326 HOH   B O    1 
HETATM 6992 O  O    . HOH   H 5 .   ? 44.114 -1.743  7.614   1.00 45.41 ?  327 HOH   B O    1 
HETATM 6993 O  O    . HOH   H 5 .   ? 43.114 -34.593 0.127   1.00 21.72 ?  328 HOH   B O    1 
HETATM 6994 O  O    . HOH   H 5 .   ? 38.429 -9.355  -13.254 1.00 28.08 ?  329 HOH   B O    1 
HETATM 6995 O  O    . HOH   H 5 .   ? 47.182 -24.483 8.179   1.00 27.25 ?  330 HOH   B O    1 
HETATM 6996 O  O    . HOH   H 5 .   ? 27.858 -14.749 -9.462  1.00 36.19 ?  331 HOH   B O    1 
HETATM 6997 O  O    . HOH   H 5 .   ? 43.504 -15.389 18.127  1.00 30.39 ?  332 HOH   B O    1 
HETATM 6998 O  O    . HOH   H 5 .   ? 57.594 -22.036 3.327   1.00 30.72 ?  333 HOH   B O    1 
HETATM 6999 O  O    . HOH   H 5 .   ? 33.616 -31.191 11.072  1.00 35.24 ?  334 HOH   B O    1 
HETATM 7000 O  O    . HOH   H 5 .   ? 47.484 -27.435 2.019   1.00 15.85 ?  335 HOH   B O    1 
HETATM 7001 O  O    . HOH   H 5 .   ? 41.306 -24.574 15.808  1.00 45.24 ?  336 HOH   B O    1 
HETATM 7002 O  O    . HOH   H 5 .   ? 45.678 -36.259 -16.060 1.00 35.89 ?  337 HOH   B O    1 
HETATM 7003 O  O    . HOH   H 5 .   ? 37.051 -15.160 -16.487 1.00 40.88 ?  338 HOH   B O    1 
HETATM 7004 O  O    . HOH   H 5 .   ? 42.847 -43.492 -14.379 1.00 40.52 ?  339 HOH   B O    1 
HETATM 7005 O  O    . HOH   H 5 .   ? 46.782 -19.907 12.318  1.00 31.08 ?  340 HOH   B O    1 
HETATM 7006 O  O    . HOH   H 5 .   ? 37.053 -45.161 -9.671  1.00 38.37 ?  341 HOH   B O    1 
HETATM 7007 O  O    . HOH   H 5 .   ? 38.488 -12.237 -16.188 1.00 46.22 ?  342 HOH   B O    1 
HETATM 7008 O  O    . HOH   H 5 .   ? 28.895 -42.898 -12.338 1.00 38.81 ?  343 HOH   B O    1 
HETATM 7009 O  O    . HOH   H 5 .   ? 39.548 -23.596 -20.383 1.00 38.75 ?  344 HOH   B O    1 
HETATM 7010 O  O    . HOH   H 5 .   ? 32.987 -14.685 1.079   1.00 20.88 ?  345 HOH   B O    1 
HETATM 7011 O  O    . HOH   H 5 .   ? 39.796 -44.245 -11.156 1.00 40.10 ?  346 HOH   B O    1 
HETATM 7012 O  O    . HOH   H 5 .   ? 34.535 -10.323 7.651   1.00 24.17 ?  347 HOH   B O    1 
HETATM 7013 O  O    . HOH   H 5 .   ? 38.604 -22.364 15.044  1.00 43.14 ?  348 HOH   B O    1 
HETATM 7014 O  O    . HOH   H 5 .   ? 40.410 -43.481 -9.087  1.00 26.46 ?  349 HOH   B O    1 
HETATM 7015 O  O    . HOH   H 5 .   ? 33.692 -9.535  -8.857  1.00 33.52 ?  350 HOH   B O    1 
HETATM 7016 O  O    . HOH   H 5 .   ? 27.767 -26.589 -0.550  1.00 30.62 ?  351 HOH   B O    1 
HETATM 7017 O  O    . HOH   H 5 .   ? 62.537 -20.129 -4.853  1.00 42.28 ?  352 HOH   B O    1 
HETATM 7018 O  O    . HOH   H 5 .   ? 55.642 -8.255  10.820  1.00 24.90 ?  353 HOH   B O    1 
HETATM 7019 O  O    . HOH   H 5 .   ? 44.184 -37.338 -17.734 1.00 36.15 ?  354 HOH   B O    1 
HETATM 7020 O  O    . HOH   H 5 .   ? 23.227 -23.636 6.868   1.00 37.04 ?  355 HOH   B O    1 
HETATM 7021 O  O    . HOH   H 5 .   ? 36.125 -8.515  -9.718  1.00 35.66 ?  356 HOH   B O    1 
HETATM 7022 O  O    . HOH   H 5 .   ? 56.563 -7.251  3.045   1.00 26.94 ?  357 HOH   B O    1 
HETATM 7023 O  O    . HOH   H 5 .   ? 33.968 -7.798  11.510  1.00 39.51 ?  358 HOH   B O    1 
HETATM 7024 O  O    . HOH   H 5 .   ? 61.502 -19.866 1.730   1.00 37.91 ?  359 HOH   B O    1 
HETATM 7025 O  O    . HOH   H 5 .   ? 56.875 -21.592 -16.343 1.00 40.70 ?  360 HOH   B O    1 
HETATM 7026 O  O    . HOH   H 5 .   ? 40.244 -8.803  9.869   1.00 36.33 ?  361 HOH   B O    1 
HETATM 7027 O  O    . HOH   H 5 .   ? 27.135 -25.901 -11.382 1.00 35.08 ?  362 HOH   B O    1 
HETATM 7028 O  O    . HOH   H 5 .   ? 43.173 -12.712 -21.169 1.00 37.59 ?  363 HOH   B O    1 
HETATM 7029 O  O    . HOH   H 5 .   ? 40.265 -11.323 -13.930 1.00 33.28 ?  364 HOH   B O    1 
HETATM 7030 O  O    . HOH   H 5 .   ? 54.178 -5.750  2.984   1.00 34.98 ?  365 HOH   B O    1 
HETATM 7031 O  O    . HOH   H 5 .   ? 32.565 -23.631 14.076  1.00 39.99 ?  366 HOH   B O    1 
HETATM 7032 O  O    . HOH   H 5 .   ? 48.327 -26.486 8.814   1.00 41.17 ?  367 HOH   B O    1 
HETATM 7033 O  O    . HOH   H 5 .   ? 58.939 -10.453 9.228   1.00 37.67 ?  368 HOH   B O    1 
HETATM 7034 O  O    . HOH   H 5 .   ? 36.157 -8.663  8.981   1.00 40.25 ?  369 HOH   B O    1 
HETATM 7035 O  O    . HOH   H 5 .   ? 41.772 -10.084 -17.405 1.00 54.24 ?  370 HOH   B O    1 
HETATM 7036 O  O    . HOH   H 5 .   ? 39.846 -7.023  7.836   1.00 39.59 ?  371 HOH   B O    1 
HETATM 7037 O  O    . HOH   H 5 .   ? 52.040 -12.907 13.375  1.00 29.34 ?  372 HOH   B O    1 
HETATM 7038 O  O    . HOH   H 5 .   ? 55.990 -7.746  -0.613  1.00 34.08 ?  373 HOH   B O    1 
HETATM 7039 O  O    . HOH   H 5 .   ? 38.044 -10.588 10.081  1.00 29.63 ?  374 HOH   B O    1 
HETATM 7040 O  O    . HOH   H 5 .   ? 41.874 -6.743  -4.837  1.00 47.96 ?  375 HOH   B O    1 
HETATM 7041 O  O    . HOH   H 5 .   ? 63.005 -12.304 6.967   1.00 37.35 ?  376 HOH   B O    1 
HETATM 7042 O  O    . HOH   H 5 .   ? 36.527 -22.868 13.287  1.00 29.73 ?  377 HOH   B O    1 
HETATM 7043 O  O    . HOH   H 5 .   ? 42.600 -17.115 -23.154 1.00 41.74 ?  378 HOH   B O    1 
HETATM 7044 O  O    . HOH   H 5 .   ? 44.091 -5.613  -3.499  1.00 42.22 ?  379 HOH   B O    1 
HETATM 7045 O  O    . HOH   H 5 .   ? 40.083 -7.649  3.175   1.00 39.13 ?  380 HOH   B O    1 
HETATM 7046 O  O    . HOH   H 5 .   ? 60.497 -22.270 2.854   1.00 48.64 ?  381 HOH   B O    1 
HETATM 7047 O  O    . HOH   H 5 .   ? 52.868 -29.868 7.236   1.00 24.48 ?  382 HOH   B O    1 
HETATM 7048 O  O    . HOH   H 5 .   ? 39.625 -14.004 15.701  1.00 45.98 ?  383 HOH   B O    1 
HETATM 7049 O  O    . HOH   H 5 .   ? 46.728 -5.390  2.879   1.00 40.38 ?  384 HOH   B O    1 
HETATM 7050 O  O    . HOH   H 5 .   ? 25.759 -18.914 -11.825 1.00 39.83 ?  385 HOH   B O    1 
HETATM 7051 O  O    . HOH   H 5 .   ? 40.977 -9.778  15.766  1.00 45.34 ?  386 HOH   B O    1 
HETATM 7052 O  O    . HOH   H 5 .   ? 23.902 -20.858 -7.595  1.00 29.67 ?  387 HOH   B O    1 
HETATM 7053 O  O    . HOH   H 5 .   ? 35.422 -33.724 7.355   1.00 41.50 ?  388 HOH   B O    1 
HETATM 7054 O  O    . HOH   H 5 .   ? 35.215 -20.365 13.271  1.00 33.31 ?  389 HOH   B O    1 
HETATM 7055 O  O    . HOH   H 5 .   ? 23.236 -23.810 1.604   1.00 32.75 ?  390 HOH   B O    1 
HETATM 7056 O  O    . HOH   H 5 .   ? 40.713 -6.616  -0.898  1.00 26.75 ?  391 HOH   B O    1 
HETATM 7057 O  O    . HOH   H 5 .   ? 28.020 -27.068 2.281   1.00 30.19 ?  392 HOH   B O    1 
HETATM 7058 O  O    . HOH   H 5 .   ? 44.068 -31.724 -3.732  1.00 37.72 ?  393 HOH   B O    1 
HETATM 7059 O  O    . HOH   H 5 .   ? 26.608 -27.933 -13.420 1.00 35.92 ?  394 HOH   B O    1 
HETATM 7060 O  O    . HOH   H 5 .   ? 24.593 -20.567 -10.483 1.00 36.73 ?  395 HOH   B O    1 
HETATM 7061 O  O    . HOH   H 5 .   ? 50.653 -30.824 8.748   1.00 29.99 ?  396 HOH   B O    1 
HETATM 7062 O  O    . HOH   H 5 .   ? 34.359 -33.489 9.639   1.00 38.10 ?  397 HOH   B O    1 
HETATM 7063 O  O    . HOH   H 5 .   ? 26.826 -30.674 -12.573 1.00 29.51 ?  398 HOH   B O    1 
HETATM 7064 O  O    . HOH   H 5 .   ? 57.600 -6.480  -2.266  1.00 34.26 ?  399 HOH   B O    1 
HETATM 7065 O  O    . HOH   H 5 .   ? 45.730 -20.139 15.253  1.00 45.85 ?  400 HOH   B O    1 
HETATM 7066 O  O    . HOH   H 5 .   ? 40.901 -11.748 -22.300 1.00 39.08 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . VAL   A 3   ? 0.6724 0.6800 0.7551 -0.0142 -0.0424 0.1081  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6678 0.6754 0.7410 -0.0158 -0.0413 0.1067  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6414 0.6523 0.7014 -0.0254 -0.0402 0.1074  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6466 0.6568 0.7221 -0.0239 -0.0422 0.1115  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.6848 0.6897 0.7540 -0.0100 -0.0402 0.1050  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.6906 0.6946 0.7567 -0.0079 -0.0398 0.1046  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.6900 0.6940 0.7574 -0.0079 -0.0397 0.1046  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.6049 0.6206 0.6262 -0.0376 -0.0350 0.1034  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5644 0.5851 0.5416 -0.0515 -0.0288 0.0964  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5062 0.5425 0.4823 -0.0655 -0.0115 0.0618  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5086 0.5445 0.4732 -0.0653 -0.0155 0.0649  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5775 0.5895 0.5099 -0.0526 -0.0398 0.1229  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.5864 0.5908 0.4788 -0.0552 -0.0482 0.1471  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.5908 0.5898 0.4671 -0.0558 -0.0522 0.1574  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.5881 0.5914 0.4702 -0.0556 -0.0499 0.1573  4   ASN   A ND2 
30   N  N   A SER   A 5   ? 0.4707 0.5211 0.4525 -0.0783 0.0003  0.0426  5   SER   A N   
31   N  N   B SER   A 5   ? 0.4788 0.5154 0.4599 -0.0688 -0.0026 0.0441  5   SER   A N   
32   C  CA  A SER   A 5   ? 0.4327 0.4977 0.4248 -0.0897 0.0134  0.0252  5   SER   A CA  
33   C  CA  B SER   A 5   ? 0.4490 0.4866 0.4374 -0.0716 0.0074  0.0281  5   SER   A CA  
34   C  C   A SER   A 5   ? 0.3888 0.4631 0.3768 -0.0999 0.0276  0.0201  5   SER   A C   
35   C  C   B SER   A 5   ? 0.4133 0.4503 0.3940 -0.0744 0.0166  0.0218  5   SER   A C   
36   O  O   A SER   A 5   ? 0.3932 0.4689 0.3752 -0.0941 0.0268  0.0129  5   SER   A O   
37   O  O   B SER   A 5   ? 0.4164 0.4538 0.3953 -0.0708 0.0171  0.0177  5   SER   A O   
38   C  CB  A SER   A 5   ? 0.4389 0.5066 0.4468 -0.0907 0.0140  0.0146  5   SER   A CB  
39   C  CB  B SER   A 5   ? 0.4541 0.4925 0.4580 -0.0719 0.0089  0.0204  5   SER   A CB  
40   O  OG  A SER   A 5   ? 0.4429 0.5118 0.4591 -0.0905 0.0154  0.0088  5   SER   A OG  
41   O  OG  B SER   A 5   ? 0.4572 0.4960 0.4692 -0.0718 0.0100  0.0160  5   SER   A OG  
52   N  N   A PHE   A 6   ? 0.3379 0.4211 0.3272 -0.1154 0.0438  0.0278  6   PHE   A N   
53   N  N   B PHE   A 6   ? 0.3726 0.4093 0.3472 -0.0813 0.0260  0.0232  6   PHE   A N   
54   C  CA  A PHE   A 6   ? 0.2935 0.3793 0.2785 -0.1242 0.0483  0.0385  6   PHE   A CA  
55   C  CA  B PHE   A 6   ? 0.3331 0.3675 0.3012 -0.0866 0.0316  0.0276  6   PHE   A CA  
56   C  C   A PHE   A 6   ? 0.2850 0.3707 0.2706 -0.1238 0.0570  0.0321  6   PHE   A C   
57   C  C   B PHE   A 6   ? 0.3228 0.3539 0.2928 -0.0819 0.0437  0.0252  6   PHE   A C   
58   O  O   A PHE   A 6   ? 0.2881 0.3784 0.2960 -0.1257 0.0614  0.0420  6   PHE   A O   
59   O  O   B PHE   A 6   ? 0.3231 0.3543 0.2936 -0.0863 0.0459  0.0332  6   PHE   A O   
60   C  CB  A PHE   A 6   ? 0.2709 0.3488 0.2506 -0.1213 0.0349  0.0533  6   PHE   A CB  
61   C  CB  B PHE   A 6   ? 0.3097 0.3421 0.2722 -0.0901 0.0213  0.0320  6   PHE   A CB  
62   C  CG  A PHE   A 6   ? 0.2537 0.3243 0.2334 -0.1140 0.0228  0.0557  6   PHE   A CG  
63   C  CG  B PHE   A 6   ? 0.2898 0.3208 0.2518 -0.0909 0.0115  0.0306  6   PHE   A CG  
64   C  CD1 A PHE   A 6   ? 0.2448 0.3138 0.2274 -0.1050 0.0169  0.0518  6   PHE   A CD1 
65   C  CD1 B PHE   A 6   ? 0.2810 0.3113 0.2430 -0.0889 0.0080  0.0290  6   PHE   A CD1 
66   C  CD2 A PHE   A 6   ? 0.2604 0.3186 0.2456 -0.0971 0.0172  0.0540  6   PHE   A CD2 
67   C  CD2 B PHE   A 6   ? 0.2865 0.3132 0.2509 -0.0860 0.0069  0.0286  6   PHE   A CD2 
68   C  CE1 A PHE   A 6   ? 0.2425 0.3072 0.2353 -0.1010 0.0203  0.0541  6   PHE   A CE1 
69   C  CE1 B PHE   A 6   ? 0.2767 0.3058 0.2439 -0.0878 0.0068  0.0288  6   PHE   A CE1 
70   C  CE2 A PHE   A 6   ? 0.2584 0.3134 0.2519 -0.0911 0.0173  0.0493  6   PHE   A CE2 
71   C  CE2 B PHE   A 6   ? 0.2819 0.3074 0.2512 -0.0849 0.0048  0.0254  6   PHE   A CE2 
72   C  CZ  A PHE   A 6   ? 0.2494 0.3073 0.2441 -0.0957 0.0182  0.0481  6   PHE   A CZ  
73   C  CZ  B PHE   A 6   ? 0.2779 0.3046 0.2460 -0.0860 0.0048  0.0252  6   PHE   A CZ  
92   N  N   A SER   A 7   ? 0.2716 0.3517 0.2375 -0.1193 0.0623  0.0172  7   SER   A N   
93   N  N   B SER   A 7   ? 0.3125 0.3391 0.2881 -0.0706 0.0496  0.0134  7   SER   A N   
94   C  CA  A SER   A 7   ? 0.2679 0.3380 0.2303 -0.1055 0.0564  -0.0044 7   SER   A CA  
95   C  CA  B SER   A 7   ? 0.3062 0.3268 0.2967 -0.0544 0.0486  0.0000  7   SER   A CA  
96   C  C   A SER   A 7   ? 0.2519 0.2995 0.1972 -0.1026 0.0616  -0.0088 7   SER   A C   
97   C  C   B SER   A 7   ? 0.2904 0.3054 0.2721 -0.0449 0.0539  -0.0042 7   SER   A C   
98   O  O   A SER   A 7   ? 0.2613 0.2889 0.1962 -0.1099 0.0597  -0.0144 7   SER   A O   
99   O  O   B SER   A 7   ? 0.2959 0.3070 0.2713 -0.0433 0.0496  -0.0066 7   SER   A O   
100  C  CB  A SER   A 7   ? 0.2840 0.3593 0.2547 -0.0920 0.0502  -0.0087 7   SER   A CB  
101  C  CB  B SER   A 7   ? 0.3138 0.3341 0.3228 -0.0496 0.0428  -0.0026 7   SER   A CB  
102  O  OG  A SER   A 7   ? 0.2975 0.3742 0.2720 -0.0796 0.0440  -0.0109 7   SER   A OG  
103  O  OG  B SER   A 7   ? 0.3191 0.3383 0.3433 -0.0457 0.0364  -0.0024 7   SER   A OG  
114  N  N   A GLY   A 8   ? 0.2287 0.2688 0.1895 -0.0946 0.0550  -0.0168 8   GLY   A N   
115  N  N   B GLY   A 8   ? 0.2706 0.2848 0.2477 -0.0367 0.0601  -0.0038 8   GLY   A N   
116  C  CA  A GLY   A 8   ? 0.2100 0.2439 0.1900 -0.0726 0.0502  -0.0129 8   GLY   A CA  
117  C  CA  B GLY   A 8   ? 0.2508 0.2614 0.2311 -0.0301 0.0556  -0.0032 8   GLY   A CA  
118  C  C   A GLY   A 8   ? 0.1874 0.2215 0.1849 -0.0507 0.0410  -0.0117 8   GLY   A C   
119  C  C   B GLY   A 8   ? 0.2267 0.2381 0.2077 -0.0210 0.0507  0.0015  8   GLY   A C   
120  O  O   A GLY   A 8   ? 0.1918 0.2243 0.1966 -0.0356 0.0498  -0.0301 8   GLY   A O   
121  O  O   B GLY   A 8   ? 0.2277 0.2411 0.2125 -0.0159 0.0510  -0.0082 8   GLY   A O   
128  N  N   A TYR   A 9   ? 0.1676 0.2040 0.1801 -0.0377 0.0397  0.0029  9   TYR   A N   
129  N  N   B TYR   A 9   ? 0.2052 0.2145 0.1914 -0.0174 0.0391  0.0122  9   TYR   A N   
130  C  CA  A TYR   A 9   ? 0.1571 0.1856 0.1701 -0.0340 0.0283  0.0053  9   TYR   A CA  
131  C  CA  B TYR   A 9   ? 0.1896 0.1941 0.1772 -0.0161 0.0334  0.0168  9   TYR   A CA  
132  C  C   A TYR   A 9   ? 0.1603 0.1680 0.1528 -0.0236 0.0288  0.0206  9   TYR   A C   
133  C  C   B TYR   A 9   ? 0.1873 0.1784 0.1665 -0.0120 0.0366  0.0135  9   TYR   A C   
134  O  O   A TYR   A 9   ? 0.1843 0.1790 0.1602 -0.0215 0.0267  0.0117  9   TYR   A O   
135  O  O   B TYR   A 9   ? 0.1987 0.1865 0.1864 -0.0126 0.0350  0.0111  9   TYR   A O   
136  C  CB  A TYR   A 9   ? 0.1526 0.1942 0.1749 -0.0285 0.0311  -0.0024 9   TYR   A CB  
137  C  CB  B TYR   A 9   ? 0.1814 0.1959 0.1908 -0.0159 0.0242  0.0138  9   TYR   A CB  
138  C  CG  A TYR   A 9   ? 0.1516 0.2001 0.1842 -0.0176 0.0422  -0.0086 9   TYR   A CG  
139  C  CG  B TYR   A 9   ? 0.1737 0.1943 0.1910 -0.0189 0.0211  0.0082  9   TYR   A CG  
140  C  CD1 A TYR   A 9   ? 0.1512 0.2022 0.1977 -0.0220 0.0463  -0.0082 9   TYR   A CD1 
141  C  CD1 B TYR   A 9   ? 0.1752 0.1905 0.1968 -0.0219 0.0237  -0.0004 9   TYR   A CD1 
142  C  CD2 A TYR   A 9   ? 0.1557 0.2001 0.2037 -0.0160 0.0338  -0.0034 9   TYR   A CD2 
143  C  CD2 B TYR   A 9   ? 0.1694 0.1963 0.1826 -0.0167 0.0148  0.0124  9   TYR   A CD2 
144  C  CE1 A TYR   A 9   ? 0.1619 0.2025 0.2209 -0.0186 0.0435  -0.0165 9   TYR   A CE1 
145  C  CE1 B TYR   A 9   ? 0.1735 0.1894 0.2016 -0.0241 0.0311  0.0046  9   TYR   A CE1 
146  C  CE2 A TYR   A 9   ? 0.1635 0.2041 0.2177 -0.0168 0.0345  -0.0083 9   TYR   A CE2 
147  C  CE2 B TYR   A 9   ? 0.1658 0.1952 0.1837 -0.0156 0.0231  0.0174  9   TYR   A CE2 
148  C  CZ  A TYR   A 9   ? 0.1623 0.2042 0.2384 -0.0272 0.0494  -0.0131 9   TYR   A CZ  
149  C  CZ  B TYR   A 9   ? 0.1651 0.1915 0.2011 -0.0217 0.0416  0.0140  9   TYR   A CZ  
150  O  OH  A TYR   A 9   ? 0.1736 0.2116 0.2706 -0.0377 0.0459  -0.0123 9   TYR   A OH  
151  O  OH  B TYR   A 9   ? 0.1584 0.1934 0.2133 -0.0283 0.0583  0.0159  9   TYR   A OH  
170  N  N   A LEU   A 10  ? 0.1570 0.1551 0.1642 -0.0242 0.0168  0.0145  10  LEU   A N   
171  N  N   B LEU   A 10  ? 0.1821 0.1660 0.1621 -0.0116 0.0330  0.0087  10  LEU   A N   
172  C  CA  A LEU   A 10  ? 0.1474 0.1518 0.1661 -0.0255 0.0167  0.0235  10  LEU   A CA  
173  C  CA  B LEU   A 10  ? 0.1760 0.1631 0.1647 -0.0089 0.0334  0.0019  10  LEU   A CA  
174  C  C   A LEU   A 10  ? 0.1426 0.1448 0.1710 -0.0205 0.0185  0.0272  10  LEU   A C   
175  C  C   B LEU   A 10  ? 0.1684 0.1531 0.1567 -0.0127 0.0282  0.0115  10  LEU   A C   
176  O  O   A LEU   A 10  ? 0.1471 0.1404 0.1801 -0.0151 0.0336  0.0225  10  LEU   A O   
177  O  O   B LEU   A 10  ? 0.1721 0.1450 0.1481 -0.0109 0.0425  0.0136  10  LEU   A O   
178  C  CB  A LEU   A 10  ? 0.1511 0.1541 0.2008 -0.0188 0.0133  0.0315  10  LEU   A CB  
179  C  CB  B LEU   A 10  ? 0.1816 0.1691 0.1793 -0.0113 0.0216  -0.0030 10  LEU   A CB  
180  C  CG  A LEU   A 10  ? 0.1776 0.1655 0.2479 -0.0083 -0.0023 0.0275  10  LEU   A CG  
181  C  CG  B LEU   A 10  ? 0.1897 0.1778 0.2040 -0.0056 0.0058  -0.0004 10  LEU   A CG  
182  C  CD1 A LEU   A 10  ? 0.1934 0.1784 0.2694 -0.0170 0.0056  0.0298  10  LEU   A CD1 
183  C  CD1 B LEU   A 10  ? 0.1966 0.1824 0.2277 -0.0138 0.0065  -0.0016 10  LEU   A CD1 
184  C  CD2 A LEU   A 10  ? 0.1912 0.1822 0.2595 0.0023  0.0104  0.0116  10  LEU   A CD2 
185  C  CD2 B LEU   A 10  ? 0.2006 0.1852 0.2258 0.0026  -0.0057 0.0023  10  LEU   A CD2 
208  N  N   A LYS   A 11  ? 0.1508 0.1491 0.1709 -0.0228 0.0206  0.0312  11  LYS   A N   
209  N  N   B LYS   A 11  ? 0.1693 0.1502 0.1657 -0.0182 0.0166  0.0131  11  LYS   A N   
210  C  CA  A LYS   A 11  ? 0.1513 0.1458 0.1835 -0.0307 0.0200  0.0275  11  LYS   A CA  
211  C  CA  B LYS   A 11  ? 0.1686 0.1470 0.1670 -0.0211 0.0147  0.0132  11  LYS   A CA  
212  C  C   A LYS   A 11  ? 0.1413 0.1518 0.1828 -0.0239 0.0220  0.0161  11  LYS   A C   
213  C  C   B LYS   A 11  ? 0.1513 0.1365 0.1655 -0.0236 0.0161  0.0021  11  LYS   A C   
214  O  O   A LYS   A 11  ? 0.1489 0.1704 0.2220 -0.0446 0.0264  -0.0085 11  LYS   A O   
215  O  O   B LYS   A 11  ? 0.1468 0.1351 0.1831 -0.0204 0.0195  -0.0169 11  LYS   A O   
216  C  CB  A LYS   A 11  ? 0.1598 0.1464 0.1882 -0.0357 0.0129  0.0204  11  LYS   A CB  
217  C  CB  B LYS   A 11  ? 0.1821 0.1428 0.1692 -0.0212 0.0068  0.0091  11  LYS   A CB  
218  C  CG  A LYS   A 11  ? 0.1789 0.1436 0.1897 -0.0348 0.0157  0.0286  11  LYS   A CG  
219  C  CG  B LYS   A 11  ? 0.1958 0.1493 0.1612 -0.0229 0.0042  0.0176  11  LYS   A CG  
220  C  CD  A LYS   A 11  ? 0.2022 0.1527 0.1992 -0.0261 0.0062  0.0340  11  LYS   A CD  
221  C  CD  B LYS   A 11  ? 0.2098 0.1581 0.1638 -0.0214 0.0032  0.0226  11  LYS   A CD  
222  C  CE  A LYS   A 11  ? 0.2091 0.1502 0.2108 -0.0223 0.0034  0.0379  11  LYS   A CE  
223  C  CE  B LYS   A 11  ? 0.2168 0.1650 0.1601 -0.0193 0.0044  0.0233  11  LYS   A CE  
224  N  NZ  A LYS   A 11  ? 0.2037 0.1426 0.2090 -0.0124 -0.0102 0.0242  11  LYS   A NZ  
225  N  NZ  B LYS   A 11  ? 0.2157 0.1683 0.1488 -0.0140 0.0028  0.0295  11  LYS   A NZ  
252  N  N   A LEU   A 12  ? 0.1374 0.1439 0.1672 -0.0224 0.0209  0.0160  12  LEU   A N   
253  N  N   B LEU   A 12  ? 0.1449 0.1462 0.1682 -0.0078 0.0123  -0.0027 12  LEU   A N   
254  C  CA  A LEU   A 12  ? 0.1395 0.1480 0.1686 -0.0189 0.0105  0.0171  12  LEU   A CA  
255  C  CA  B LEU   A 12  ? 0.1435 0.1558 0.1726 -0.0011 0.0139  -0.0019 12  LEU   A CA  
256  C  C   A LEU   A 12  ? 0.1442 0.1390 0.1808 -0.0220 0.0164  0.0189  12  LEU   A C   
257  C  C   B LEU   A 12  ? 0.1424 0.1573 0.1688 -0.0003 0.0195  0.0044  12  LEU   A C   
258  O  O   A LEU   A 12  ? 0.1438 0.1430 0.1895 -0.0166 0.0284  0.0012  12  LEU   A O   
259  O  O   B LEU   A 12  ? 0.1543 0.1591 0.1573 0.0081  0.0116  0.0004  12  LEU   A O   
260  C  CB  A LEU   A 12  ? 0.1489 0.1440 0.1671 -0.0142 0.0054  0.0232  12  LEU   A CB  
261  C  CB  B LEU   A 12  ? 0.1528 0.1670 0.1856 0.0008  0.0207  -0.0022 12  LEU   A CB  
262  C  CG  A LEU   A 12  ? 0.1568 0.1556 0.1857 -0.0032 0.0151  0.0201  12  LEU   A CG  
263  C  CG  B LEU   A 12  ? 0.1560 0.1738 0.1946 -0.0007 0.0265  0.0008  12  LEU   A CG  
264  C  CD1 A LEU   A 12  ? 0.1724 0.1625 0.1909 0.0139  0.0212  0.0330  12  LEU   A CD1 
265  C  CD1 B LEU   A 12  ? 0.1597 0.1811 0.1988 0.0020  0.0337  -0.0028 12  LEU   A CD1 
266  C  CD2 A LEU   A 12  ? 0.1610 0.1652 0.2098 -0.0067 0.0096  0.0185  12  LEU   A CD2 
267  C  CD2 B LEU   A 12  ? 0.1575 0.1782 0.2026 -0.0000 0.0235  -0.0073 12  LEU   A CD2 
290  N  N   A THR   A 13  ? 0.1422 0.1357 0.1962 -0.0210 0.0119  0.0188  13  THR   A N   
291  N  N   B THR   A 13  ? 0.1353 0.1536 0.1800 -0.0041 0.0229  0.0098  13  THR   A N   
292  C  CA  A THR   A 13  ? 0.1429 0.1419 0.2186 -0.0177 0.0171  0.0208  13  THR   A CA  
293  C  CA  B THR   A 13  ? 0.1367 0.1560 0.1880 -0.0117 0.0251  0.0168  13  THR   A CA  
294  C  C   A THR   A 13  ? 0.1474 0.1490 0.2310 -0.0214 0.0048  0.0400  13  THR   A C   
295  C  C   B THR   A 13  ? 0.1437 0.1716 0.1986 -0.0172 0.0202  0.0311  13  THR   A C   
296  O  O   A THR   A 13  ? 0.1509 0.1511 0.2265 -0.0179 0.0041  0.0343  13  THR   A O   
297  O  O   B THR   A 13  ? 0.1515 0.1783 0.1971 -0.0255 0.0095  0.0427  13  THR   A O   
298  C  CB  A THR   A 13  ? 0.1473 0.1508 0.2421 -0.0101 0.0188  0.0240  13  THR   A CB  
299  C  CB  B THR   A 13  ? 0.1362 0.1560 0.2000 -0.0056 0.0305  0.0165  13  THR   A CB  
300  O  OG1 A THR   A 13  ? 0.1568 0.1469 0.2583 -0.0109 0.0091  0.0320  13  THR   A OG1 
301  O  OG1 B THR   A 13  ? 0.1245 0.1575 0.2130 -0.0082 0.0491  0.0345  13  THR   A OG1 
302  C  CG2 A THR   A 13  ? 0.1598 0.1686 0.2456 -0.0034 0.0281  0.0168  13  THR   A CG2 
303  C  CG2 B THR   A 13  ? 0.1411 0.1602 0.1980 0.0038  0.0271  0.0077  13  THR   A CG2 
318  N  N   A ASP   A 14  ? 0.1529 0.1529 0.2513 -0.0277 0.0017  0.0667  14  ASP   A N   
319  N  N   B ASP   A 14  ? 0.1469 0.1772 0.2218 -0.0193 0.0120  0.0342  14  ASP   A N   
320  C  CA  A ASP   A 14  ? 0.1573 0.1689 0.2818 -0.0299 -0.0086 0.0790  14  ASP   A CA  
321  C  CA  B ASP   A 14  ? 0.1539 0.1883 0.2402 -0.0176 -0.0002 0.0450  14  ASP   A CA  
322  C  C   A ASP   A 14  ? 0.1520 0.1690 0.2702 -0.0287 -0.0076 0.0753  14  ASP   A C   
323  C  C   B ASP   A 14  ? 0.1474 0.1789 0.2242 -0.0138 -0.0067 0.0537  14  ASP   A C   
324  O  O   A ASP   A 14  ? 0.1530 0.1790 0.2680 -0.0279 -0.0118 0.0750  14  ASP   A O   
325  O  O   B ASP   A 14  ? 0.1439 0.1815 0.2206 -0.0081 -0.0121 0.0543  14  ASP   A O   
326  C  CB  A ASP   A 14  ? 0.1743 0.1837 0.3280 -0.0433 -0.0157 0.0931  14  ASP   A CB  
327  C  CB  B ASP   A 14  ? 0.1686 0.2095 0.2756 -0.0221 -0.0066 0.0471  14  ASP   A CB  
328  C  CG  A ASP   A 14  ? 0.1997 0.2232 0.3931 -0.0419 -0.0193 0.0852  14  ASP   A CG  
329  C  CG  B ASP   A 14  ? 0.1740 0.2337 0.3055 -0.0296 -0.0056 0.0481  14  ASP   A CG  
330  O  OD1 A ASP   A 14  ? 0.2218 0.2511 0.4198 -0.0241 -0.0344 0.0852  14  ASP   A OD1 
331  O  OD1 B ASP   A 14  ? 0.1846 0.2448 0.3156 -0.0246 -0.0058 0.0520  14  ASP   A OD1 
332  O  OD2 A ASP   A 14  ? 0.2173 0.2408 0.4307 -0.0465 -0.0277 0.0600  14  ASP   A OD2 
333  O  OD2 B ASP   A 14  ? 0.1757 0.2460 0.3302 -0.0327 -0.0115 0.0399  14  ASP   A OD2 
342  N  N   A ASN   A 15  ? 0.1411 0.1548 0.2724 -0.0269 -0.0046 0.0698  15  ASN   A N   
343  N  N   B ASN   A 15  ? 0.1414 0.1660 0.2188 -0.0175 -0.0025 0.0625  15  ASN   A N   
344  C  CA  A ASN   A 15  ? 0.1430 0.1569 0.2937 -0.0210 -0.0150 0.0581  15  ASN   A CA  
345  C  CA  B ASN   A 15  ? 0.1429 0.1644 0.2297 -0.0169 -0.0066 0.0568  15  ASN   A CA  
346  C  C   A ASN   A 15  ? 0.1367 0.1515 0.3079 -0.0277 -0.0040 0.0501  15  ASN   A C   
347  C  C   B ASN   A 15  ? 0.1415 0.1617 0.2394 -0.0230 0.0043  0.0564  15  ASN   A C   
348  O  O   A ASN   A 15  ? 0.1403 0.1518 0.3463 -0.0179 -0.0205 0.0471  15  ASN   A O   
349  O  O   B ASN   A 15  ? 0.1516 0.1733 0.2596 -0.0210 -0.0037 0.0491  15  ASN   A O   
350  C  CB  A ASN   A 15  ? 0.1409 0.1565 0.2915 -0.0106 -0.0100 0.0624  15  ASN   A CB  
351  C  CB  B ASN   A 15  ? 0.1417 0.1631 0.2262 -0.0146 -0.0057 0.0564  15  ASN   A CB  
352  C  CG  A ASN   A 15  ? 0.1409 0.1643 0.2990 -0.0055 -0.0033 0.0498  15  ASN   A CG  
353  C  CG  B ASN   A 15  ? 0.1384 0.1665 0.2342 -0.0139 0.0010  0.0414  15  ASN   A CG  
354  O  OD1 A ASN   A 15  ? 0.1604 0.1751 0.3137 -0.0275 0.0013  0.0530  15  ASN   A OD1 
355  O  OD1 B ASN   A 15  ? 0.1522 0.1696 0.2516 -0.0280 0.0024  0.0432  15  ASN   A OD1 
356  N  ND2 A ASN   A 15  ? 0.1398 0.1669 0.2895 -0.0064 0.0043  0.0560  15  ASN   A ND2 
357  N  ND2 B ASN   A 15  ? 0.1336 0.1641 0.2226 -0.0094 0.0038  0.0438  15  ASN   A ND2 
370  N  N   A VAL   A 16  ? 0.1419 0.1544 0.2873 -0.0142 -0.0021 0.0499  16  VAL   A N   
371  N  N   B VAL   A 16  ? 0.1394 0.1515 0.2292 -0.0215 0.0074  0.0640  16  VAL   A N   
372  C  CA  A VAL   A 16  ? 0.1345 0.1586 0.2628 -0.0154 0.0088  0.0439  16  VAL   A CA  
373  C  CA  B VAL   A 16  ? 0.1401 0.1553 0.2139 -0.0151 0.0161  0.0603  16  VAL   A CA  
374  C  C   A VAL   A 16  ? 0.1328 0.1497 0.2409 -0.0237 0.0047  0.0388  16  VAL   A C   
375  C  C   B VAL   A 16  ? 0.1368 0.1653 0.2000 -0.0187 0.0108  0.0524  16  VAL   A C   
376  O  O   A VAL   A 16  ? 0.1306 0.1464 0.2296 -0.0270 0.0104  0.0266  16  VAL   A O   
377  O  O   B VAL   A 16  ? 0.1369 0.1665 0.1958 -0.0161 0.0163  0.0457  16  VAL   A O   
378  C  CB  A VAL   A 16  ? 0.1418 0.1768 0.2525 0.0060  0.0276  0.0531  16  VAL   A CB  
379  C  CB  B VAL   A 16  ? 0.1498 0.1623 0.2074 0.0029  0.0380  0.0552  16  VAL   A CB  
380  C  CG1 A VAL   A 16  ? 0.1588 0.1884 0.2569 0.0128  0.0294  0.0565  16  VAL   A CG1 
381  C  CG1 B VAL   A 16  ? 0.1584 0.1676 0.2106 0.0110  0.0391  0.0543  16  VAL   A CG1 
382  C  CG2 A VAL   A 16  ? 0.1487 0.1905 0.2487 0.0115  0.0428  0.0497  16  VAL   A CG2 
383  C  CG2 B VAL   A 16  ? 0.1535 0.1720 0.2121 0.0054  0.0512  0.0497  16  VAL   A CG2 
402  N  N   A TYR   A 17  ? 0.1349 0.1421 0.2349 -0.0192 0.0188  0.0434  17  TYR   A N   
403  N  N   B TYR   A 17  ? 0.1372 0.1664 0.1945 -0.0211 0.0050  0.0490  17  TYR   A N   
404  C  CA  A TYR   A 17  ? 0.1416 0.1491 0.2006 -0.0285 0.0158  0.0378  17  TYR   A CA  
405  C  CA  B TYR   A 17  ? 0.1369 0.1667 0.1644 -0.0223 0.0011  0.0448  17  TYR   A CA  
406  C  C   A TYR   A 17  ? 0.1442 0.1412 0.1904 -0.0229 0.0134  0.0223  17  TYR   A C   
407  C  C   B TYR   A 17  ? 0.1377 0.1601 0.1444 -0.0209 0.0069  0.0333  17  TYR   A C   
408  O  O   A TYR   A 17  ? 0.1448 0.1386 0.1774 -0.0253 0.0154  0.0235  17  TYR   A O   
409  O  O   B TYR   A 17  ? 0.1333 0.1628 0.1406 -0.0252 0.0041  0.0323  17  TYR   A O   
410  C  CB  A TYR   A 17  ? 0.1621 0.1567 0.2004 -0.0369 -0.0047 0.0472  17  TYR   A CB  
411  C  CB  B TYR   A 17  ? 0.1459 0.1761 0.1741 -0.0224 -0.0074 0.0422  17  TYR   A CB  
412  C  CG  A TYR   A 17  ? 0.1784 0.1727 0.2201 -0.0398 -0.0337 0.0554  17  TYR   A CG  
413  C  CG  B TYR   A 17  ? 0.1558 0.1866 0.1850 -0.0202 -0.0167 0.0357  17  TYR   A CG  
414  C  CD1 A TYR   A 17  ? 0.1879 0.1815 0.2355 -0.0333 -0.0361 0.0528  17  TYR   A CD1 
415  C  CD1 B TYR   A 17  ? 0.1645 0.1905 0.1949 -0.0100 -0.0126 0.0373  17  TYR   A CD1 
416  C  CD2 A TYR   A 17  ? 0.1838 0.1775 0.2142 -0.0475 -0.0420 0.0625  17  TYR   A CD2 
417  C  CD2 B TYR   A 17  ? 0.1596 0.1912 0.1835 -0.0180 -0.0166 0.0360  17  TYR   A CD2 
418  C  CE1 A TYR   A 17  ? 0.1853 0.1806 0.2400 -0.0357 -0.0454 0.0574  17  TYR   A CE1 
419  C  CE1 B TYR   A 17  ? 0.1718 0.1931 0.2052 -0.0051 -0.0102 0.0386  17  TYR   A CE1 
420  C  CE2 A TYR   A 17  ? 0.1900 0.1753 0.2282 -0.0451 -0.0501 0.0532  17  TYR   A CE2 
421  C  CE2 B TYR   A 17  ? 0.1644 0.1902 0.1902 -0.0104 -0.0163 0.0337  17  TYR   A CE2 
422  C  CZ  A TYR   A 17  ? 0.1892 0.1746 0.2368 -0.0409 -0.0439 0.0579  17  TYR   A CZ  
423  C  CZ  B TYR   A 17  ? 0.1682 0.1899 0.2008 -0.0039 -0.0170 0.0383  17  TYR   A CZ  
424  O  OH  A TYR   A 17  ? 0.1986 0.1716 0.2453 -0.0304 -0.0338 0.0513  17  TYR   A OH  
425  O  OH  B TYR   A 17  ? 0.1697 0.1878 0.2129 0.0048  -0.0175 0.0381  17  TYR   A OH  
444  N  N   A ILE   A 18  ? 0.1462 0.1454 0.1788 -0.0237 0.0203  0.0303  18  ILE   A N   
445  N  N   B ILE   A 18  ? 0.1368 0.1572 0.1447 -0.0206 0.0149  0.0287  18  ILE   A N   
446  C  CA  A ILE   A 18  ? 0.1521 0.1421 0.1714 -0.0138 0.0228  0.0200  18  ILE   A CA  
447  C  CA  B ILE   A 18  ? 0.1368 0.1559 0.1297 -0.0134 0.0180  0.0236  18  ILE   A CA  
448  C  C   A ILE   A 18  ? 0.1552 0.1524 0.1738 -0.0259 0.0248  0.0191  18  ILE   A C   
449  C  C   B ILE   A 18  ? 0.1338 0.1667 0.1280 -0.0200 0.0137  0.0220  18  ILE   A C   
450  O  O   A ILE   A 18  ? 0.1580 0.1668 0.1758 -0.0311 0.0316  0.0184  18  ILE   A O   
451  O  O   B ILE   A 18  ? 0.1346 0.1690 0.1463 -0.0230 0.0253  0.0170  18  ILE   A O   
452  C  CB  A ILE   A 18  ? 0.1593 0.1401 0.1690 -0.0006 0.0271  0.0200  18  ILE   A CB  
453  C  CB  B ILE   A 18  ? 0.1414 0.1461 0.1163 -0.0112 0.0276  0.0244  18  ILE   A CB  
454  C  CG1 A ILE   A 18  ? 0.1682 0.1407 0.1647 0.0109  0.0125  0.0061  18  ILE   A CG1 
455  C  CG1 B ILE   A 18  ? 0.1570 0.1579 0.1290 -0.0079 0.0342  0.0205  18  ILE   A CG1 
456  C  CG2 A ILE   A 18  ? 0.1569 0.1380 0.1713 0.0023  0.0241  0.0098  18  ILE   A CG2 
457  C  CG2 B ILE   A 18  ? 0.1481 0.1508 0.1245 -0.0150 0.0229  0.0242  18  ILE   A CG2 
458  C  CD1 A ILE   A 18  ? 0.1910 0.1589 0.1833 0.0235  0.0116  0.0156  18  ILE   A CD1 
459  C  CD1 B ILE   A 18  ? 0.1678 0.1645 0.1429 -0.0057 0.0342  0.0015  18  ILE   A CD1 
482  N  N   A LYS   A 19  ? 0.1558 0.1510 0.1671 -0.0198 0.0269  0.0166  19  LYS   A N   
483  N  N   B LYS   A 19  ? 0.1369 0.1702 0.1290 -0.0182 0.0221  0.0164  19  LYS   A N   
484  C  CA  A LYS   A 19  ? 0.1633 0.1612 0.1814 -0.0241 0.0271  0.0161  19  LYS   A CA  
485  C  CA  B LYS   A 19  ? 0.1523 0.1803 0.1497 -0.0145 0.0314  0.0099  19  LYS   A CA  
486  C  C   A LYS   A 19  ? 0.1545 0.1583 0.2012 -0.0116 0.0345  0.0338  19  LYS   A C   
487  C  C   B LYS   A 19  ? 0.1542 0.1823 0.1591 -0.0061 0.0357  0.0116  19  LYS   A C   
488  O  O   A LYS   A 19  ? 0.1489 0.1572 0.2090 -0.0036 0.0326  0.0410  19  LYS   A O   
489  O  O   B LYS   A 19  ? 0.1526 0.1789 0.1598 -0.0089 0.0279  0.0089  19  LYS   A O   
490  C  CB  A LYS   A 19  ? 0.1859 0.1828 0.1898 -0.0270 0.0307  0.0089  19  LYS   A CB  
491  C  CB  B LYS   A 19  ? 0.1585 0.1846 0.1624 -0.0194 0.0439  -0.0066 19  LYS   A CB  
492  C  CG  A LYS   A 19  ? 0.2143 0.1960 0.2010 -0.0250 0.0343  -0.0035 19  LYS   A CG  
493  C  CG  B LYS   A 19  ? 0.1845 0.1980 0.1759 -0.0166 0.0479  -0.0105 19  LYS   A CG  
494  C  CD  A LYS   A 19  ? 0.2390 0.2099 0.2134 -0.0208 0.0393  -0.0115 19  LYS   A CD  
495  C  CD  B LYS   A 19  ? 0.2062 0.2096 0.1855 -0.0168 0.0531  -0.0117 19  LYS   A CD  
496  C  CE  A LYS   A 19  ? 0.2568 0.2170 0.2278 -0.0223 0.0460  -0.0191 19  LYS   A CE  
497  C  CE  B LYS   A 19  ? 0.2231 0.2218 0.1989 -0.0193 0.0550  -0.0163 19  LYS   A CE  
498  N  NZ  A LYS   A 19  ? 0.2669 0.2229 0.2333 -0.0249 0.0550  -0.0272 19  LYS   A NZ  
499  N  NZ  B LYS   A 19  ? 0.2351 0.2279 0.2071 -0.0255 0.0586  -0.0251 19  LYS   A NZ  
526  N  N   A ASN   A 20  ? 0.1614 0.1632 0.2290 -0.0129 0.0410  0.0493  20  ASN   A N   
527  N  N   B ASN   A 20  ? 0.1625 0.1937 0.1870 0.0047  0.0443  0.0164  20  ASN   A N   
528  C  CA  A ASN   A 20  ? 0.1752 0.1806 0.2634 0.0072  0.0575  0.0464  20  ASN   A CA  
529  C  CA  B ASN   A 20  ? 0.1668 0.2062 0.2138 0.0149  0.0466  0.0236  20  ASN   A CA  
530  C  C   A ASN   A 20  ? 0.1921 0.1826 0.2753 -0.0002 0.0740  0.0368  20  ASN   A C   
531  C  C   B ASN   A 20  ? 0.1794 0.2044 0.2326 0.0178  0.0629  0.0228  20  ASN   A C   
532  O  O   A ASN   A 20  ? 0.2065 0.1813 0.2777 -0.0080 0.0733  0.0239  20  ASN   A O   
533  O  O   B ASN   A 20  ? 0.1856 0.2031 0.2483 0.0225  0.0643  0.0222  20  ASN   A O   
534  C  CB  A ASN   A 20  ? 0.1849 0.1893 0.2767 0.0202  0.0630  0.0581  20  ASN   A CB  
535  C  CB  B ASN   A 20  ? 0.1639 0.2167 0.2234 0.0194  0.0393  0.0298  20  ASN   A CB  
536  C  CG  A ASN   A 20  ? 0.1980 0.1904 0.3007 0.0308  0.0683  0.0514  20  ASN   A CG  
537  C  CG  B ASN   A 20  ? 0.1603 0.2207 0.2355 0.0212  0.0393  0.0245  20  ASN   A CG  
538  O  OD1 A ASN   A 20  ? 0.2272 0.2043 0.3363 0.0354  0.0758  0.0295  20  ASN   A OD1 
539  O  OD1 B ASN   A 20  ? 0.1585 0.2167 0.2379 0.0266  0.0407  0.0174  20  ASN   A OD1 
540  N  ND2 A ASN   A 20  ? 0.1968 0.1768 0.3041 0.0374  0.0592  0.0712  20  ASN   A ND2 
541  N  ND2 B ASN   A 20  ? 0.1706 0.2254 0.2541 0.0156  0.0376  0.0276  20  ASN   A ND2 
554  N  N   A ALA   A 21  ? 0.1982 0.1850 0.2735 -0.0004 0.0676  0.0335  21  ALA   A N   
555  N  N   B ALA   A 21  ? 0.1877 0.2045 0.2352 0.0154  0.0591  0.0180  21  ALA   A N   
556  C  CA  A ALA   A 21  ? 0.1999 0.1817 0.2651 -0.0034 0.0588  0.0416  21  ALA   A CA  
557  C  CA  B ALA   A 21  ? 0.1940 0.2020 0.2333 0.0103  0.0569  0.0206  21  ALA   A CA  
558  C  C   A ALA   A 21  ? 0.1889 0.1812 0.2691 -0.0065 0.0521  0.0444  21  ALA   A C   
559  C  C   B ALA   A 21  ? 0.1896 0.1936 0.2205 0.0096  0.0640  0.0248  21  ALA   A C   
560  O  O   A ALA   A 21  ? 0.1823 0.1857 0.2734 -0.0024 0.0481  0.0486  21  ALA   A O   
561  O  O   B ALA   A 21  ? 0.1862 0.1862 0.2282 0.0207  0.0676  0.0172  21  ALA   A O   
562  C  CB  A ALA   A 21  ? 0.2104 0.1824 0.2572 -0.0030 0.0508  0.0470  21  ALA   A CB  
563  C  CB  B ALA   A 21  ? 0.2004 0.2027 0.2477 0.0093  0.0463  0.0173  21  ALA   A CB  
574  N  N   A ASP   A 22  ? 0.1868 0.1776 0.2726 -0.0151 0.0545  0.0386  22  ASP   A N   
575  N  N   B ASP   A 22  ? 0.1920 0.1896 0.2105 -0.0003 0.0620  0.0314  22  ASP   A N   
576  C  CA  A ASP   A 22  ? 0.1941 0.1816 0.2636 -0.0096 0.0477  0.0381  22  ASP   A CA  
577  C  CA  B ASP   A 22  ? 0.1943 0.1878 0.2116 -0.0046 0.0516  0.0316  22  ASP   A CA  
578  C  C   A ASP   A 22  ? 0.1818 0.1814 0.2273 -0.0086 0.0453  0.0335  22  ASP   A C   
579  C  C   B ASP   A 22  ? 0.1813 0.1828 0.1860 -0.0146 0.0540  0.0244  22  ASP   A C   
580  O  O   A ASP   A 22  ? 0.1861 0.1869 0.2353 -0.0131 0.0436  0.0222  22  ASP   A O   
581  O  O   B ASP   A 22  ? 0.1762 0.1860 0.1963 -0.0182 0.0558  0.0087  22  ASP   A O   
582  C  CB  A ASP   A 22  ? 0.2178 0.1868 0.3129 -0.0159 0.0342  0.0340  22  ASP   A CB  
583  C  CB  B ASP   A 22  ? 0.2064 0.1920 0.2465 0.0003  0.0447  0.0314  22  ASP   A CB  
584  C  CG  A ASP   A 22  ? 0.2392 0.1965 0.3617 -0.0195 0.0042  0.0417  22  ASP   A CG  
585  C  CG  B ASP   A 22  ? 0.2151 0.1911 0.2699 0.0006  0.0414  0.0387  22  ASP   A CG  
586  O  OD1 A ASP   A 22  ? 0.2372 0.1929 0.3782 -0.0361 -0.0176 0.0521  22  ASP   A OD1 
587  O  OD1 B ASP   A 22  ? 0.2145 0.1855 0.2620 0.0026  0.0445  0.0365  22  ASP   A OD1 
588  O  OD2 A ASP   A 22  ? 0.2602 0.2085 0.3910 -0.0054 0.0022  0.0378  22  ASP   A OD2 
589  O  OD2 B ASP   A 22  ? 0.2201 0.1980 0.2897 -0.0019 0.0401  0.0401  22  ASP   A OD2 
598  N  N   A ILE   A 23  ? 0.1779 0.1814 0.2136 -0.0035 0.0461  0.0268  23  ILE   A N   
599  N  N   B ILE   A 23  ? 0.1768 0.1754 0.1674 -0.0145 0.0440  0.0252  23  ILE   A N   
600  C  CA  A ILE   A 23  ? 0.1803 0.1733 0.2021 -0.0063 0.0430  0.0214  23  ILE   A CA  
601  C  CA  B ILE   A 23  ? 0.1699 0.1764 0.1515 -0.0156 0.0316  0.0210  23  ILE   A CA  
602  C  C   A ILE   A 23  ? 0.1761 0.1774 0.1997 -0.0082 0.0604  0.0181  23  ILE   A C   
603  C  C   B ILE   A 23  ? 0.1756 0.1819 0.1633 -0.0264 0.0363  0.0106  23  ILE   A C   
604  O  O   A ILE   A 23  ? 0.1818 0.1823 0.2055 -0.0061 0.0557  0.0138  23  ILE   A O   
605  O  O   B ILE   A 23  ? 0.1803 0.1756 0.1698 -0.0235 0.0291  0.0088  23  ILE   A O   
606  C  CB  A ILE   A 23  ? 0.1913 0.1715 0.1816 -0.0018 0.0413  0.0214  23  ILE   A CB  
607  C  CB  B ILE   A 23  ? 0.1653 0.1689 0.1414 -0.0093 0.0192  0.0267  23  ILE   A CB  
608  C  CG1 A ILE   A 23  ? 0.1962 0.1701 0.1820 0.0052  0.0387  0.0156  23  ILE   A CG1 
609  C  CG1 B ILE   A 23  ? 0.1692 0.1644 0.1427 -0.0059 0.0097  0.0207  23  ILE   A CG1 
610  C  CG2 A ILE   A 23  ? 0.1965 0.1744 0.1839 0.0002  0.0405  0.0288  23  ILE   A CG2 
611  C  CG2 B ILE   A 23  ? 0.1633 0.1673 0.1392 -0.0027 0.0138  0.0288  23  ILE   A CG2 
612  C  CD1 A ILE   A 23  ? 0.2011 0.1707 0.1928 0.0041  0.0290  0.0063  23  ILE   A CD1 
613  C  CD1 B ILE   A 23  ? 0.1633 0.1641 0.1529 0.0026  -0.0009 0.0140  23  ILE   A CD1 
636  N  N   A VAL   A 24  ? 0.1807 0.1814 0.2136 -0.0133 0.0543  0.0116  24  VAL   A N   
637  N  N   B VAL   A 24  ? 0.1841 0.1927 0.1872 -0.0346 0.0394  -0.0026 24  VAL   A N   
638  C  CA  A VAL   A 24  ? 0.1970 0.1975 0.2287 -0.0207 0.0529  0.0007  24  VAL   A CA  
639  C  CA  B VAL   A 24  ? 0.2021 0.2021 0.2112 -0.0368 0.0427  -0.0045 24  VAL   A CA  
640  C  C   A VAL   A 24  ? 0.2022 0.2144 0.2304 -0.0345 0.0473  -0.0039 24  VAL   A C   
641  C  C   B VAL   A 24  ? 0.2097 0.2223 0.2144 -0.0379 0.0449  -0.0125 24  VAL   A C   
642  O  O   A VAL   A 24  ? 0.2168 0.2213 0.2364 -0.0336 0.0492  -0.0041 24  VAL   A O   
643  O  O   B VAL   A 24  ? 0.2167 0.2290 0.2274 -0.0317 0.0436  -0.0089 24  VAL   A O   
644  C  CB  A VAL   A 24  ? 0.2019 0.2009 0.2446 -0.0133 0.0551  0.0023  24  VAL   A CB  
645  C  CB  B VAL   A 24  ? 0.2092 0.2001 0.2357 -0.0369 0.0424  -0.0005 24  VAL   A CB  
646  C  CG1 A VAL   A 24  ? 0.2065 0.2092 0.2499 -0.0060 0.0552  -0.0118 24  VAL   A CG1 
647  C  CG1 B VAL   A 24  ? 0.2177 0.2043 0.2544 -0.0344 0.0368  -0.0025 24  VAL   A CG1 
648  C  CG2 A VAL   A 24  ? 0.2131 0.2051 0.2476 -0.0119 0.0692  0.0164  24  VAL   A CG2 
649  C  CG2 B VAL   A 24  ? 0.2121 0.1974 0.2370 -0.0382 0.0473  0.0008  24  VAL   A CG2 
668  N  N   A GLU   A 25  ? 0.2028 0.2339 0.2322 -0.0423 0.0542  -0.0128 25  GLU   A N   
669  N  N   B GLU   A 25  ? 0.2125 0.2367 0.2145 -0.0406 0.0630  -0.0147 25  GLU   A N   
670  C  CA  A GLU   A 25  ? 0.2235 0.2566 0.2309 -0.0309 0.0582  -0.0173 25  GLU   A CA  
671  C  CA  B GLU   A 25  ? 0.2254 0.2556 0.2226 -0.0428 0.0640  -0.0195 25  GLU   A CA  
672  C  C   A GLU   A 25  ? 0.2093 0.2582 0.1905 -0.0430 0.0674  -0.0176 25  GLU   A C   
673  C  C   B GLU   A 25  ? 0.2235 0.2616 0.2015 -0.0428 0.0679  -0.0224 25  GLU   A C   
674  O  O   A GLU   A 25  ? 0.2120 0.2685 0.2040 -0.0406 0.0625  -0.0213 25  GLU   A O   
675  O  O   B GLU   A 25  ? 0.2277 0.2612 0.2033 -0.0423 0.0672  -0.0324 25  GLU   A O   
676  C  CB  A GLU   A 25  ? 0.2521 0.2800 0.2712 -0.0214 0.0525  -0.0142 25  GLU   A CB  
677  C  CB  B GLU   A 25  ? 0.2376 0.2660 0.2512 -0.0451 0.0647  -0.0174 25  GLU   A CB  
678  C  CG  A GLU   A 25  ? 0.2831 0.3007 0.3346 -0.0197 0.0333  -0.0165 25  GLU   A CG  
679  C  CG  B GLU   A 25  ? 0.2548 0.2773 0.2952 -0.0453 0.0532  -0.0179 25  GLU   A CG  
680  C  CD  A GLU   A 25  ? 0.3069 0.3177 0.3910 -0.0188 0.0169  -0.0201 25  GLU   A CD  
681  C  CD  B GLU   A 25  ? 0.2678 0.2861 0.3368 -0.0467 0.0370  -0.0153 25  GLU   A CD  
682  O  OE1 A GLU   A 25  ? 0.3167 0.3247 0.4043 -0.0156 0.0028  -0.0272 25  GLU   A OE1 
683  O  OE1 B GLU   A 25  ? 0.2738 0.2880 0.3592 -0.0473 0.0308  -0.0139 25  GLU   A OE1 
684  O  OE2 A GLU   A 25  ? 0.3128 0.3252 0.4211 -0.0218 0.0121  -0.0261 25  GLU   A OE2 
685  O  OE2 B GLU   A 25  ? 0.2745 0.2911 0.3524 -0.0441 0.0327  -0.0124 25  GLU   A OE2 
698  N  N   A GLU   A 26  ? 0.1989 0.2531 0.1926 -0.0573 0.0651  -0.0216 26  GLU   A N   
699  N  N   B GLU   A 26  ? 0.2219 0.2653 0.1924 -0.0438 0.0687  -0.0214 26  GLU   A N   
700  C  CA  A GLU   A 26  ? 0.2074 0.2582 0.1807 -0.0682 0.0582  -0.0158 26  GLU   A CA  
701  C  CA  B GLU   A 26  ? 0.2262 0.2687 0.1927 -0.0433 0.0597  -0.0181 26  GLU   A CA  
702  C  C   A GLU   A 26  ? 0.2051 0.2515 0.1677 -0.0662 0.0595  -0.0119 26  GLU   A C   
703  C  C   B GLU   A 26  ? 0.2259 0.2647 0.1814 -0.0369 0.0559  -0.0110 26  GLU   A C   
704  O  O   A GLU   A 26  ? 0.2098 0.2479 0.1722 -0.0701 0.0598  -0.0177 26  GLU   A O   
705  O  O   B GLU   A 26  ? 0.2263 0.2610 0.1765 -0.0363 0.0616  -0.0092 26  GLU   A O   
706  C  CB  A GLU   A 26  ? 0.2266 0.2685 0.1997 -0.0775 0.0541  -0.0101 26  GLU   A CB  
707  C  CB  B GLU   A 26  ? 0.2329 0.2783 0.2075 -0.0479 0.0469  -0.0206 26  GLU   A CB  
708  C  CG  A GLU   A 26  ? 0.2525 0.2875 0.2667 -0.0821 0.0523  -0.0137 26  GLU   A CG  
709  C  CG  B GLU   A 26  ? 0.2370 0.2860 0.2135 -0.0574 0.0540  -0.0150 26  GLU   A CG  
710  C  CD  A GLU   A 26  ? 0.2690 0.3031 0.3102 -0.0910 0.0635  -0.0111 26  GLU   A CD  
711  C  CD  B GLU   A 26  ? 0.2397 0.2926 0.2158 -0.0712 0.0626  -0.0096 26  GLU   A CD  
712  O  OE1 A GLU   A 26  ? 0.2672 0.3284 0.3229 -0.0788 0.0886  -0.0282 26  GLU   A OE1 
713  O  OE1 B GLU   A 26  ? 0.2433 0.3099 0.2269 -0.0666 0.0776  -0.0094 26  GLU   A OE1 
714  O  OE2 A GLU   A 26  ? 0.2908 0.3084 0.3237 -0.0930 0.0512  -0.0020 26  GLU   A OE2 
715  O  OE2 B GLU   A 26  ? 0.2403 0.2893 0.1836 -0.0800 0.0690  -0.0078 26  GLU   A OE2 
728  N  N   A ALA   A 27  ? 0.1951 0.2446 0.1627 -0.0724 0.0589  -0.0042 27  ALA   A N   
729  N  N   B ALA   A 27  ? 0.2212 0.2643 0.1777 -0.0317 0.0475  -0.0050 27  ALA   A N   
730  C  CA  A ALA   A 27  ? 0.2058 0.2604 0.1742 -0.0704 0.0482  -0.0070 27  ALA   A CA  
731  C  CA  B ALA   A 27  ? 0.2245 0.2724 0.1810 -0.0244 0.0345  -0.0034 27  ALA   A CA  
732  C  C   A ALA   A 27  ? 0.2289 0.2758 0.1860 -0.0843 0.0445  -0.0235 27  ALA   A C   
733  C  C   B ALA   A 27  ? 0.2374 0.2861 0.1931 -0.0245 0.0280  -0.0100 27  ALA   A C   
734  O  O   A ALA   A 27  ? 0.2396 0.2687 0.1971 -0.0888 0.0331  -0.0216 27  ALA   A O   
735  O  O   B ALA   A 27  ? 0.2366 0.2829 0.1958 -0.0237 0.0243  -0.0100 27  ALA   A O   
736  C  CB  A ALA   A 27  ? 0.1941 0.2555 0.1760 -0.0702 0.0512  -0.0006 27  ALA   A CB  
737  C  CB  B ALA   A 27  ? 0.2180 0.2678 0.1781 -0.0236 0.0335  -0.0018 27  ALA   A CB  
748  N  N   A LYS   A 28  ? 0.2586 0.3038 0.2051 -0.0812 0.0313  -0.0488 28  LYS   A N   
749  N  N   B LYS   A 28  ? 0.2573 0.3039 0.2122 -0.0230 0.0164  -0.0204 28  LYS   A N   
750  C  CA  A LYS   A 28  ? 0.2945 0.3384 0.2305 -0.0694 0.0340  -0.0611 28  LYS   A CA  
751  C  CA  B LYS   A 28  ? 0.2798 0.3255 0.2301 -0.0191 0.0087  -0.0290 28  LYS   A CA  
752  C  C   A LYS   A 28  ? 0.3120 0.3645 0.2282 -0.0700 0.0551  -0.0486 28  LYS   A C   
753  C  C   B LYS   A 28  ? 0.3024 0.3478 0.2340 -0.0271 0.0158  -0.0227 28  LYS   A C   
754  O  O   A LYS   A 28  ? 0.3154 0.3691 0.2563 -0.0650 0.0430  -0.0488 28  LYS   A O   
755  O  O   B LYS   A 28  ? 0.3066 0.3498 0.2404 -0.0234 0.0063  -0.0242 28  LYS   A O   
756  C  CB  A LYS   A 28  ? 0.3124 0.3519 0.2740 -0.0517 0.0203  -0.0697 28  LYS   A CB  
757  C  CB  B LYS   A 28  ? 0.2843 0.3282 0.2533 -0.0072 -0.0037 -0.0392 28  LYS   A CB  
758  C  CG  A LYS   A 28  ? 0.3277 0.3624 0.3209 -0.0368 0.0101  -0.0723 28  LYS   A CG  
759  C  CG  B LYS   A 28  ? 0.2919 0.3325 0.2838 0.0015  -0.0149 -0.0464 28  LYS   A CG  
760  C  CD  A LYS   A 28  ? 0.3408 0.3763 0.3733 -0.0245 -0.0014 -0.0721 28  LYS   A CD  
761  C  CD  B LYS   A 28  ? 0.3025 0.3406 0.3212 0.0094  -0.0248 -0.0527 28  LYS   A CD  
762  C  CE  A LYS   A 28  ? 0.3518 0.3863 0.4101 -0.0163 -0.0119 -0.0749 28  LYS   A CE  
763  C  CE  B LYS   A 28  ? 0.3125 0.3473 0.3512 0.0130  -0.0312 -0.0588 28  LYS   A CE  
764  N  NZ  A LYS   A 28  ? 0.3601 0.3917 0.4368 -0.0102 -0.0134 -0.0769 28  LYS   A NZ  
765  N  NZ  B LYS   A 28  ? 0.3168 0.3505 0.3638 0.0141  -0.0392 -0.0647 28  LYS   A NZ  
792  N  N   A LYS   A 29  ? 0.3233 0.3859 0.2219 -0.0772 0.0871  -0.0287 29  LYS   A N   
793  N  N   B LYS   A 29  ? 0.3202 0.3683 0.2475 -0.0407 0.0362  -0.0122 29  LYS   A N   
794  C  CA  A LYS   A 29  ? 0.3425 0.4100 0.2481 -0.0786 0.1014  -0.0114 29  LYS   A CA  
795  C  CA  B LYS   A 29  ? 0.3398 0.3896 0.2755 -0.0526 0.0527  -0.0028 29  LYS   A CA  
796  C  C   A LYS   A 29  ? 0.3483 0.4064 0.2331 -0.0837 0.0850  0.0028  29  LYS   A C   
797  C  C   B LYS   A 29  ? 0.3440 0.3934 0.2487 -0.0721 0.0600  0.0066  29  LYS   A C   
798  O  O   A LYS   A 29  ? 0.3600 0.4173 0.2418 -0.0778 0.0785  0.0047  29  LYS   A O   
799  O  O   B LYS   A 29  ? 0.3494 0.3990 0.2525 -0.0707 0.0584  0.0105  29  LYS   A O   
800  C  CB  A LYS   A 29  ? 0.3571 0.4357 0.3072 -0.0710 0.1137  -0.0093 29  LYS   A CB  
801  C  CB  B LYS   A 29  ? 0.3542 0.4055 0.3316 -0.0440 0.0562  -0.0027 29  LYS   A CB  
802  C  CG  A LYS   A 29  ? 0.3746 0.4575 0.3712 -0.0617 0.1147  -0.0098 29  LYS   A CG  
803  C  CG  B LYS   A 29  ? 0.3688 0.4189 0.3848 -0.0353 0.0567  -0.0037 29  LYS   A CG  
804  C  CD  A LYS   A 29  ? 0.3898 0.4759 0.4325 -0.0537 0.1119  -0.0119 29  LYS   A CD  
805  C  CD  B LYS   A 29  ? 0.3806 0.4302 0.4325 -0.0277 0.0560  -0.0048 29  LYS   A CD  
806  C  CE  A LYS   A 29  ? 0.4009 0.4888 0.4765 -0.0482 0.1092  -0.0143 29  LYS   A CE  
807  C  CE  B LYS   A 29  ? 0.3889 0.4384 0.4667 -0.0226 0.0554  -0.0063 29  LYS   A CE  
808  N  NZ  A LYS   A 29  ? 0.4061 0.4957 0.5048 -0.0446 0.1062  -0.0171 29  LYS   A NZ  
809  N  NZ  B LYS   A 29  ? 0.3933 0.4428 0.4876 -0.0196 0.0539  -0.0068 29  LYS   A NZ  
836  N  N   . VAL   A 30  ? 0.3409 0.3901 0.2247 -0.0922 0.0702  0.0115  30  VAL   A N   
837  C  CA  . VAL   A 30  ? 0.3404 0.3732 0.2027 -0.1111 0.0403  0.0238  30  VAL   A CA  
838  C  C   . VAL   A 30  ? 0.3432 0.3563 0.1731 -0.1150 0.0300  0.0332  30  VAL   A C   
839  O  O   . VAL   A 30  ? 0.3505 0.3609 0.1822 -0.1126 0.0261  0.0340  30  VAL   A O   
840  C  CB  . VAL   A 30  ? 0.3382 0.3674 0.2311 -0.1252 0.0181  0.0281  30  VAL   A CB  
841  C  CG1 . VAL   A 30  ? 0.3426 0.3659 0.2509 -0.1255 0.0074  0.0307  30  VAL   A CG1 
842  C  CG2 . VAL   A 30  ? 0.3360 0.3667 0.2523 -0.1343 0.0205  0.0269  30  VAL   A CG2 
853  N  N   A LYS   A 31  ? 0.3402 0.3448 0.1639 -0.1187 0.0139  0.0277  31  LYS   A N   
854  N  N   B LYS   A 31  ? 0.3418 0.3470 0.1883 -0.1110 0.0178  0.0296  31  LYS   A N   
855  C  CA  A LYS   A 31  ? 0.3493 0.3424 0.1900 -0.1065 -0.0071 0.0300  31  LYS   A CA  
856  C  CA  B LYS   A 31  ? 0.3458 0.3426 0.2192 -0.0989 0.0013  0.0299  31  LYS   A CA  
857  C  C   A LYS   A 31  ? 0.3296 0.3291 0.1572 -0.0946 -0.0144 0.0605  31  LYS   A C   
858  C  C   B LYS   A 31  ? 0.3269 0.3269 0.1811 -0.0936 -0.0073 0.0509  31  LYS   A C   
859  O  O   A LYS   A 31  ? 0.3342 0.3390 0.1697 -0.0882 -0.0253 0.0695  31  LYS   A O   
860  O  O   B LYS   A 31  ? 0.3305 0.3331 0.1916 -0.0902 -0.0117 0.0549  31  LYS   A O   
861  C  CB  A LYS   A 31  ? 0.3821 0.3603 0.2874 -0.0952 -0.0226 0.0053  31  LYS   A CB  
862  C  CB  B LYS   A 31  ? 0.3700 0.3572 0.3030 -0.0866 -0.0092 0.0109  31  LYS   A CB  
863  C  CG  A LYS   A 31  ? 0.4145 0.3784 0.3972 -0.0811 -0.0365 -0.0114 31  LYS   A CG  
864  C  CG  B LYS   A 31  ? 0.3928 0.3715 0.3889 -0.0735 -0.0195 -0.0033 31  LYS   A CG  
865  C  CD  A LYS   A 31  ? 0.4410 0.3937 0.4804 -0.0684 -0.0497 -0.0261 31  LYS   A CD  
866  C  CD  B LYS   A 31  ? 0.4115 0.3837 0.4552 -0.0621 -0.0292 -0.0153 31  LYS   A CD  
867  C  CE  A LYS   A 31  ? 0.4592 0.4056 0.5341 -0.0581 -0.0589 -0.0362 31  LYS   A CE  
868  C  CE  B LYS   A 31  ? 0.4244 0.3928 0.4985 -0.0534 -0.0358 -0.0231 31  LYS   A CE  
869  N  NZ  A LYS   A 31  ? 0.4685 0.4110 0.5633 -0.0525 -0.0645 -0.0416 31  LYS   A NZ  
870  N  NZ  B LYS   A 31  ? 0.4313 0.3970 0.5225 -0.0485 -0.0393 -0.0271 31  LYS   A NZ  
897  N  N   . PRO   A 32  ? 0.3013 0.3029 0.1519 -0.0954 -0.0117 0.0575  32  PRO   A N   
898  C  CA  . PRO   A 32  ? 0.2851 0.2826 0.1685 -0.0869 -0.0241 0.0706  32  PRO   A CA  
899  C  C   . PRO   A 32  ? 0.2775 0.2717 0.1807 -0.0735 -0.0341 0.0795  32  PRO   A C   
900  O  O   . PRO   A 32  ? 0.2706 0.2620 0.1944 -0.0734 -0.0517 0.0792  32  PRO   A O   
901  C  CB  . PRO   A 32  ? 0.2747 0.2811 0.1775 -0.0875 -0.0265 0.0583  32  PRO   A CB  
902  C  CG  . PRO   A 32  ? 0.2757 0.2865 0.1417 -0.0796 -0.0367 0.0452  32  PRO   A CG  
903  C  CD  . PRO   A 32  ? 0.2825 0.2918 0.1382 -0.0888 -0.0273 0.0453  32  PRO   A CD  
911  N  N   . THR   A 33  ? 0.2800 0.2673 0.1801 -0.0680 -0.0303 0.0780  33  THR   A N   
912  C  CA  . THR   A 33  ? 0.2760 0.2651 0.1852 -0.0535 -0.0400 0.0785  33  THR   A CA  
913  C  C   . THR   A 33  ? 0.2424 0.2431 0.1787 -0.0563 -0.0371 0.0633  33  THR   A C   
914  O  O   . THR   A 33  ? 0.2354 0.2418 0.1855 -0.0572 -0.0486 0.0619  33  THR   A O   
915  C  CB  . THR   A 33  ? 0.2999 0.2841 0.1988 -0.0417 -0.0478 0.0894  33  THR   A CB  
916  O  OG1 . THR   A 33  ? 0.3213 0.2970 0.2317 -0.0243 -0.0402 0.0951  33  THR   A OG1 
917  C  CG2 . THR   A 33  ? 0.3047 0.2926 0.2095 -0.0348 -0.0573 0.0852  33  THR   A CG2 
925  N  N   . VAL   A 34  ? 0.2141 0.2230 0.1599 -0.0571 -0.0290 0.0571  34  VAL   A N   
926  C  CA  . VAL   A 34  ? 0.1932 0.2038 0.1535 -0.0495 -0.0153 0.0522  34  VAL   A CA  
927  C  C   . VAL   A 34  ? 0.1802 0.1910 0.1489 -0.0442 -0.0094 0.0358  34  VAL   A C   
928  O  O   . VAL   A 34  ? 0.1830 0.1917 0.1773 -0.0446 -0.0083 0.0502  34  VAL   A O   
929  C  CB  . VAL   A 34  ? 0.1949 0.2055 0.1779 -0.0386 -0.0113 0.0421  34  VAL   A CB  
930  C  CG1 . VAL   A 34  ? 0.2039 0.2059 0.1828 -0.0315 0.0020  0.0302  34  VAL   A CG1 
931  C  CG2 . VAL   A 34  ? 0.1963 0.2185 0.1996 -0.0301 -0.0181 0.0391  34  VAL   A CG2 
941  N  N   . VAL   A 35  ? 0.1651 0.1791 0.1572 -0.0397 -0.0073 0.0344  35  VAL   A N   
942  C  CA  . VAL   A 35  ? 0.1565 0.1708 0.1562 -0.0318 0.0036  0.0292  35  VAL   A CA  
943  C  C   . VAL   A 35  ? 0.1441 0.1575 0.1493 -0.0259 0.0071  0.0305  35  VAL   A C   
944  O  O   . VAL   A 35  ? 0.1401 0.1667 0.1640 -0.0293 0.0189  0.0202  35  VAL   A O   
945  C  CB  . VAL   A 35  ? 0.1627 0.1699 0.1599 -0.0212 0.0107  0.0160  35  VAL   A CB  
946  C  CG1 . VAL   A 35  ? 0.1748 0.1784 0.1574 -0.0135 0.0068  0.0086  35  VAL   A CG1 
947  C  CG2 . VAL   A 35  ? 0.1610 0.1668 0.1821 -0.0162 0.0123  0.0105  35  VAL   A CG2 
957  N  N   . VAL   A 36  ? 0.1314 0.1562 0.1458 -0.0235 0.0101  0.0270  36  VAL   A N   
958  C  CA  . VAL   A 36  ? 0.1319 0.1427 0.1482 -0.0159 0.0093  0.0193  36  VAL   A CA  
959  C  C   . VAL   A 36  ? 0.1289 0.1442 0.1516 -0.0170 0.0102  0.0156  36  VAL   A C   
960  O  O   . VAL   A 36  ? 0.1338 0.1420 0.1718 -0.0115 0.0199  0.0204  36  VAL   A O   
961  C  CB  . VAL   A 36  ? 0.1326 0.1334 0.1606 -0.0169 0.0080  0.0218  36  VAL   A CB  
962  C  CG1 . VAL   A 36  ? 0.1422 0.1369 0.1672 -0.0227 0.0092  0.0043  36  VAL   A CG1 
963  C  CG2 . VAL   A 36  ? 0.1424 0.1420 0.1820 -0.0155 -0.0024 0.0236  36  VAL   A CG2 
973  N  N   . ASN   A 37  ? 0.1233 0.1337 0.1479 -0.0100 0.0102  0.0230  37  ASN   A N   
974  C  CA  . ASN   A 37  ? 0.1206 0.1309 0.1409 -0.0061 0.0059  0.0235  37  ASN   A CA  
975  C  C   . ASN   A 37  ? 0.1171 0.1287 0.1475 -0.0078 0.0130  0.0272  37  ASN   A C   
976  O  O   . ASN   A 37  ? 0.1322 0.1383 0.1470 0.0048  0.0133  0.0116  37  ASN   A O   
977  C  CB  . ASN   A 37  ? 0.1266 0.1297 0.1498 -0.0025 0.0074  0.0190  37  ASN   A CB  
978  C  CG  . ASN   A 37  ? 0.1203 0.1286 0.1603 -0.0048 0.0078  0.0144  37  ASN   A CG  
979  O  OD1 . ASN   A 37  ? 0.1218 0.1357 0.1717 -0.0042 0.0054  0.0194  37  ASN   A OD1 
980  N  ND2 . ASN   A 37  ? 0.1263 0.1270 0.1718 -0.0030 0.0015  0.0309  37  ASN   A ND2 
987  N  N   A ALA   A 38  ? 0.1206 0.1384 0.1463 -0.0033 0.0208  0.0094  38  ALA   A N   
988  N  N   B ALA   A 38  ? 0.1195 0.1370 0.1459 -0.0023 0.0075  0.0159  38  ALA   A N   
989  C  CA  A ALA   A 38  ? 0.1303 0.1346 0.1440 -0.0070 0.0115  -0.0017 38  ALA   A CA  
990  C  CA  B ALA   A 38  ? 0.1250 0.1388 0.1465 -0.0028 -0.0053 0.0098  38  ALA   A CA  
991  C  C   A ALA   A 38  ? 0.1302 0.1354 0.1490 -0.0056 -0.0005 -0.0016 38  ALA   A C   
992  C  C   B ALA   A 38  ? 0.1232 0.1384 0.1473 0.0011  -0.0088 0.0049  38  ALA   A C   
993  O  O   A ALA   A 38  ? 0.1326 0.1256 0.1480 -0.0051 -0.0077 -0.0058 38  ALA   A O   
994  O  O   B ALA   A 38  ? 0.1218 0.1359 0.1527 0.0052  -0.0208 0.0056  38  ALA   A O   
995  C  CB  A ALA   A 38  ? 0.1343 0.1532 0.1476 -0.0133 0.0054  -0.0065 38  ALA   A CB  
996  C  CB  B ALA   A 38  ? 0.1271 0.1478 0.1527 -0.0065 -0.0179 0.0088  38  ALA   A CB  
1007 N  N   . ALA   A 39  ? 0.1234 0.1389 0.1551 -0.0031 0.0053  0.0144  39  ALA   A N   
1008 C  CA  . ALA   A 39  ? 0.1294 0.1397 0.1502 -0.0042 0.0134  0.0115  39  ALA   A CA  
1009 C  C   . ALA   A 39  ? 0.1272 0.1295 0.1477 -0.0010 0.0077  0.0090  39  ALA   A C   
1010 O  O   . ALA   A 39  ? 0.1413 0.1328 0.1565 -0.0080 0.0059  0.0088  39  ALA   A O   
1011 C  CB  . ALA   A 39  ? 0.1316 0.1571 0.1576 -0.0059 -0.0066 0.0075  39  ALA   A CB  
1018 N  N   A ASN   A 40  ? 0.1310 0.1357 0.1558 -0.0044 0.0198  0.0088  40  ASN   A N   
1019 N  N   B ASN   A 40  ? 0.1385 0.1284 0.1456 -0.0002 0.0170  0.0118  40  ASN   A N   
1020 C  CA  A ASN   A 40  ? 0.1313 0.1297 0.1589 -0.0004 0.0062  0.0077  40  ASN   A CA  
1021 C  CA  B ASN   A 40  ? 0.1474 0.1239 0.1446 0.0030  0.0067  0.0117  40  ASN   A CA  
1022 C  C   A ASN   A 40  ? 0.1296 0.1203 0.1406 -0.0006 0.0127  0.0199  40  ASN   A C   
1023 C  C   B ASN   A 40  ? 0.1481 0.1215 0.1242 0.0024  0.0133  0.0212  40  ASN   A C   
1024 O  O   A ASN   A 40  ? 0.1300 0.1295 0.1423 -0.0065 0.0134  0.0204  40  ASN   A O   
1025 O  O   B ASN   A 40  ? 0.1472 0.1250 0.1266 -0.0017 0.0089  0.0214  40  ASN   A O   
1026 C  CB  A ASN   A 40  ? 0.1442 0.1396 0.1708 0.0085  0.0013  0.0115  40  ASN   A CB  
1027 C  CB  B ASN   A 40  ? 0.1573 0.1254 0.1594 0.0055  0.0014  0.0106  40  ASN   A CB  
1028 C  CG  A ASN   A 40  ? 0.1516 0.1444 0.1808 0.0088  0.0048  0.0203  40  ASN   A CG  
1029 C  CG  B ASN   A 40  ? 0.1595 0.1279 0.1756 0.0054  -0.0073 0.0086  40  ASN   A CG  
1030 O  OD1 A ASN   A 40  ? 0.1545 0.1447 0.2012 0.0075  0.0057  0.0229  40  ASN   A OD1 
1031 O  OD1 B ASN   A 40  ? 0.1653 0.1311 0.2043 0.0020  -0.0145 0.0044  40  ASN   A OD1 
1032 N  ND2 A ASN   A 40  ? 0.1584 0.1560 0.1784 0.0089  0.0102  0.0050  40  ASN   A ND2 
1033 N  ND2 B ASN   A 40  ? 0.1557 0.1361 0.1780 -0.0000 0.0076  -0.0017 40  ASN   A ND2 
1046 N  N   A VAL   A 41  ? 0.1331 0.1232 0.1504 0.0007  0.0119  0.0179  41  VAL   A N   
1047 N  N   B VAL   A 41  ? 0.1498 0.1268 0.1280 0.0040  0.0086  0.0285  41  VAL   A N   
1048 C  CA  A VAL   A 41  ? 0.1342 0.1297 0.1482 0.0005  0.0116  0.0201  41  VAL   A CA  
1049 C  CA  B VAL   A 41  ? 0.1521 0.1292 0.1357 0.0046  0.0113  0.0326  41  VAL   A CA  
1050 C  C   A VAL   A 41  ? 0.1359 0.1293 0.1471 0.0026  0.0155  0.0211  41  VAL   A C   
1051 C  C   B VAL   A 41  ? 0.1522 0.1260 0.1313 -0.0026 0.0193  0.0293  41  VAL   A C   
1052 O  O   A VAL   A 41  ? 0.1426 0.1317 0.1344 0.0021  -0.0049 0.0081  41  VAL   A O   
1053 O  O   B VAL   A 41  ? 0.1552 0.1201 0.1103 -0.0036 0.0137  0.0217  41  VAL   A O   
1054 C  CB  A VAL   A 41  ? 0.1381 0.1364 0.1408 0.0053  0.0203  0.0141  41  VAL   A CB  
1055 C  CB  B VAL   A 41  ? 0.1599 0.1414 0.1460 0.0068  0.0155  0.0329  41  VAL   A CB  
1056 C  CG1 A VAL   A 41  ? 0.1523 0.1459 0.1601 0.0062  0.0067  0.0065  41  VAL   A CG1 
1057 C  CG1 B VAL   A 41  ? 0.1714 0.1495 0.1590 0.0051  0.0219  0.0199  41  VAL   A CG1 
1058 C  CG2 A VAL   A 41  ? 0.1398 0.1452 0.1312 0.0016  0.0305  0.0145  41  VAL   A CG2 
1059 C  CG2 B VAL   A 41  ? 0.1624 0.1498 0.1566 0.0070  0.0068  0.0304  41  VAL   A CG2 
1078 N  N   A TYR   A 42  ? 0.1266 0.1227 0.1847 0.0018  0.0235  0.0261  42  TYR   A N   
1079 N  N   B TYR   A 42  ? 0.1517 0.1307 0.1523 0.0035  0.0287  0.0274  42  TYR   A N   
1080 C  CA  A TYR   A 42  ? 0.1357 0.1200 0.1930 -0.0077 0.0259  0.0253  42  TYR   A CA  
1081 C  CA  B TYR   A 42  ? 0.1506 0.1342 0.1608 0.0056  0.0289  0.0266  42  TYR   A CA  
1082 C  C   A TYR   A 42  ? 0.1328 0.1195 0.1849 -0.0036 0.0174  0.0271  42  TYR   A C   
1083 C  C   B TYR   A 42  ? 0.1446 0.1305 0.1600 0.0008  0.0227  0.0279  42  TYR   A C   
1084 O  O   A TYR   A 42  ? 0.1317 0.1227 0.2030 -0.0109 0.0137  0.0103  42  TYR   A O   
1085 O  O   B TYR   A 42  ? 0.1419 0.1351 0.1717 -0.0047 0.0297  0.0229  42  TYR   A O   
1086 C  CB  A TYR   A 42  ? 0.1567 0.1330 0.1840 -0.0118 0.0334  0.0328  42  TYR   A CB  
1087 C  CB  B TYR   A 42  ? 0.1642 0.1446 0.1613 0.0068  0.0210  0.0337  42  TYR   A CB  
1088 C  CG  A TYR   A 42  ? 0.1735 0.1421 0.1768 -0.0114 0.0334  0.0351  42  TYR   A CG  
1089 C  CG  B TYR   A 42  ? 0.1771 0.1549 0.1646 0.0096  0.0132  0.0337  42  TYR   A CG  
1090 C  CD1 A TYR   A 42  ? 0.1836 0.1551 0.1790 -0.0224 0.0357  0.0274  42  TYR   A CD1 
1091 C  CD1 B TYR   A 42  ? 0.1819 0.1614 0.1668 0.0065  0.0127  0.0329  42  TYR   A CD1 
1092 C  CD2 A TYR   A 42  ? 0.1875 0.1599 0.1900 -0.0067 0.0286  0.0325  42  TYR   A CD2 
1093 C  CD2 B TYR   A 42  ? 0.1890 0.1701 0.1809 0.0128  0.0099  0.0265  42  TYR   A CD2 
1094 C  CE1 A TYR   A 42  ? 0.1979 0.1645 0.1732 -0.0191 0.0361  0.0222  42  TYR   A CE1 
1095 C  CE1 B TYR   A 42  ? 0.1909 0.1698 0.1707 0.0081  0.0134  0.0295  42  TYR   A CE1 
1096 C  CE2 A TYR   A 42  ? 0.1989 0.1705 0.2011 -0.0153 0.0252  0.0328  42  TYR   A CE2 
1097 C  CE2 B TYR   A 42  ? 0.1990 0.1782 0.1890 0.0117  0.0100  0.0240  42  TYR   A CE2 
1098 C  CZ  A TYR   A 42  ? 0.2092 0.1725 0.1801 -0.0207 0.0386  0.0222  42  TYR   A CZ  
1099 C  CZ  B TYR   A 42  ? 0.2010 0.1791 0.1779 0.0101  0.0162  0.0210  42  TYR   A CZ  
1100 O  OH  A TYR   A 42  ? 0.2209 0.1877 0.1978 -0.0263 0.0356  0.0127  42  TYR   A OH  
1101 O  OH  B TYR   A 42  ? 0.2094 0.1929 0.1890 0.0025  0.0185  0.0144  42  TYR   A OH  
1120 N  N   . LEU   A 43  ? 0.1365 0.1236 0.1656 -0.0031 0.0171  0.0147  43  LEU   A N   
1121 C  CA  . LEU   A 43  ? 0.1292 0.1265 0.1617 -0.0075 0.0116  0.0122  43  LEU   A CA  
1122 C  C   . LEU   A 43  ? 0.1323 0.1296 0.1600 -0.0042 0.0087  0.0088  43  LEU   A C   
1123 O  O   . LEU   A 43  ? 0.1454 0.1324 0.1853 0.0030  -0.0061 0.0083  43  LEU   A O   
1124 C  CB  . LEU   A 43  ? 0.1334 0.1248 0.1763 -0.0109 0.0086  0.0153  43  LEU   A CB  
1125 C  CG  . LEU   A 43  ? 0.1385 0.1290 0.1857 -0.0036 0.0043  0.0120  43  LEU   A CG  
1126 C  CD1 . LEU   A 43  ? 0.1482 0.1354 0.1984 0.0007  0.0016  0.0182  43  LEU   A CD1 
1127 C  CD2 . LEU   A 43  ? 0.1539 0.1282 0.1831 -0.0034 0.0101  0.0243  43  LEU   A CD2 
1140 N  N   A LYS   A 44  ? 0.1417 0.1270 0.1587 0.0013  0.0092  0.0122  44  LYS   A N   
1141 N  N   B LYS   A 44  ? 0.1428 0.1365 0.1614 -0.0013 0.0089  0.0120  44  LYS   A N   
1142 C  CA  A LYS   A 44  ? 0.1464 0.1226 0.1680 -0.0039 0.0120  0.0224  44  LYS   A CA  
1143 C  CA  B LYS   A 44  ? 0.1505 0.1413 0.1740 -0.0048 0.0096  0.0181  44  LYS   A CA  
1144 C  C   A LYS   A 44  ? 0.1382 0.1285 0.1585 0.0040  0.0017  0.0148  44  LYS   A C   
1145 C  C   B LYS   A 44  ? 0.1389 0.1376 0.1611 -0.0018 0.0020  0.0159  44  LYS   A C   
1146 O  O   A LYS   A 44  ? 0.1466 0.1440 0.1798 0.0078  -0.0011 -0.0013 44  LYS   A O   
1147 O  O   B LYS   A 44  ? 0.1407 0.1444 0.1701 -0.0069 -0.0000 0.0128  44  LYS   A O   
1148 C  CB  A LYS   A 44  ? 0.1757 0.1386 0.2034 0.0010  0.0265  0.0344  44  LYS   A CB  
1149 C  CB  B LYS   A 44  ? 0.1768 0.1606 0.2143 -0.0017 0.0201  0.0229  44  LYS   A CB  
1150 C  CG  A LYS   A 44  ? 0.2090 0.1689 0.2591 -0.0040 0.0481  0.0431  44  LYS   A CG  
1151 C  CG  B LYS   A 44  ? 0.2011 0.1864 0.2665 -0.0001 0.0278  0.0300  44  LYS   A CG  
1152 C  CD  A LYS   A 44  ? 0.2449 0.2201 0.3485 -0.0025 0.0376  0.0361  44  LYS   A CD  
1153 C  CD  B LYS   A 44  ? 0.2255 0.2186 0.3277 -0.0023 0.0180  0.0301  44  LYS   A CD  
1154 C  CE  A LYS   A 44  ? 0.2610 0.2478 0.4077 0.0023  0.0329  0.0345  44  LYS   A CE  
1155 C  CE  B LYS   A 44  ? 0.2376 0.2371 0.3682 -0.0037 0.0116  0.0376  44  LYS   A CE  
1156 N  NZ  A LYS   A 44  ? 0.2673 0.2641 0.4365 0.0064  0.0293  0.0337  44  LYS   A NZ  
1157 N  NZ  B LYS   A 44  ? 0.2501 0.2522 0.3966 -0.0069 0.0083  0.0400  44  LYS   A NZ  
1184 N  N   . HIS   A 45  ? 0.1301 0.1311 0.1547 0.0019  -0.0005 0.0184  45  HIS   A N   
1185 C  CA  . HIS   A 45  ? 0.1262 0.1283 0.1589 0.0019  -0.0027 0.0122  45  HIS   A CA  
1186 C  C   . HIS   A 45  ? 0.1342 0.1409 0.1655 0.0017  -0.0015 0.0090  45  HIS   A C   
1187 O  O   . HIS   A 45  ? 0.1560 0.1608 0.1989 0.0225  -0.0084 -0.0059 45  HIS   A O   
1188 C  CB  . HIS   A 45  ? 0.1265 0.1301 0.1525 0.0005  -0.0083 0.0067  45  HIS   A CB  
1189 C  CG  . HIS   A 45  ? 0.1243 0.1284 0.1503 -0.0076 0.0013  0.0077  45  HIS   A CG  
1190 N  ND1 . HIS   A 45  ? 0.1186 0.1350 0.1687 -0.0040 -0.0000 0.0209  45  HIS   A ND1 
1191 C  CD2 . HIS   A 45  ? 0.1292 0.1318 0.1511 -0.0130 -0.0034 0.0208  45  HIS   A CD2 
1192 C  CE1 . HIS   A 45  ? 0.1240 0.1407 0.1552 -0.0119 0.0006  0.0244  45  HIS   A CE1 
1193 N  NE2 . HIS   A 45  ? 0.1279 0.1421 0.1524 -0.0062 0.0026  0.0264  45  HIS   A NE2 
1202 N  N   . GLY   A 46  ? 0.1499 0.1479 0.1912 0.0088  -0.0167 0.0205  46  GLY   A N   
1203 C  CA  . GLY   A 46  ? 0.1556 0.1562 0.2016 0.0161  -0.0243 0.0183  46  GLY   A CA  
1204 C  C   . GLY   A 46  ? 0.1588 0.1530 0.1993 0.0227  -0.0282 0.0223  46  GLY   A C   
1205 O  O   . GLY   A 46  ? 0.1600 0.1641 0.2404 0.0233  -0.0435 0.0054  46  GLY   A O   
1209 N  N   A GLY   A 47  ? 0.1633 0.1511 0.1944 0.0229  -0.0248 0.0158  47  GLY   A N   
1210 N  N   B GLY   A 47  ? 0.1592 0.1522 0.1810 0.0224  -0.0169 0.0124  47  GLY   A N   
1211 C  CA  A GLY   A 47  ? 0.1652 0.1569 0.1951 0.0235  -0.0421 0.0058  47  GLY   A CA  
1212 C  CA  B GLY   A 47  ? 0.1578 0.1544 0.1680 0.0220  -0.0180 0.0039  47  GLY   A CA  
1213 C  C   A GLY   A 47  ? 0.1558 0.1464 0.1877 0.0208  -0.0461 0.0029  47  GLY   A C   
1214 C  C   B GLY   A 47  ? 0.1492 0.1440 0.1414 0.0240  -0.0089 -0.0054 47  GLY   A C   
1215 O  O   A GLY   A 47  ? 0.1523 0.1414 0.1979 0.0192  -0.0400 0.0172  47  GLY   A O   
1216 O  O   B GLY   A 47  ? 0.1502 0.1391 0.1355 0.0312  -0.0037 0.0077  47  GLY   A O   
1223 N  N   A GLY   A 48  ? 0.1491 0.1461 0.1885 0.0256  -0.0457 -0.0146 48  GLY   A N   
1224 N  N   B GLY   A 48  ? 0.1451 0.1477 0.1537 0.0164  -0.0111 -0.0087 48  GLY   A N   
1225 C  CA  A GLY   A 48  ? 0.1416 0.1404 0.2040 0.0181  -0.0331 -0.0155 48  GLY   A CA  
1226 C  CA  B GLY   A 48  ? 0.1364 0.1367 0.1515 0.0139  -0.0028 -0.0117 48  GLY   A CA  
1227 C  C   A GLY   A 48  ? 0.1313 0.1383 0.2001 0.0059  -0.0162 -0.0073 48  GLY   A C   
1228 C  C   B GLY   A 48  ? 0.1323 0.1410 0.1579 -0.0016 0.0037  -0.0019 48  GLY   A C   
1229 O  O   A GLY   A 48  ? 0.1412 0.1340 0.1956 0.0036  -0.0135 0.0020  48  GLY   A O   
1230 O  O   B GLY   A 48  ? 0.1414 0.1450 0.1552 -0.0004 0.0122  -0.0038 48  GLY   A O   
1237 N  N   A VAL   A 49  ? 0.1221 0.1337 0.2101 -0.0015 -0.0137 -0.0071 49  VAL   A N   
1238 N  N   B VAL   A 49  ? 0.1196 0.1354 0.1670 -0.0081 -0.0021 -0.0014 49  VAL   A N   
1239 C  CA  A VAL   A 49  ? 0.1347 0.1347 0.1914 0.0001  0.0098  -0.0009 49  VAL   A CA  
1240 C  CA  B VAL   A 49  ? 0.1170 0.1352 0.1655 -0.0093 0.0037  0.0076  49  VAL   A CA  
1241 C  C   A VAL   A 49  ? 0.1292 0.1195 0.1677 0.0029  0.0117  0.0056  49  VAL   A C   
1242 C  C   B VAL   A 49  ? 0.1206 0.1228 0.1531 -0.0020 0.0084  0.0012  49  VAL   A C   
1243 O  O   A VAL   A 49  ? 0.1366 0.1238 0.1779 0.0004  0.0144  0.0081  49  VAL   A O   
1244 O  O   B VAL   A 49  ? 0.1212 0.1124 0.1440 -0.0021 0.0202  0.0015  49  VAL   A O   
1245 C  CB  A VAL   A 49  ? 0.1528 0.1388 0.1992 -0.0025 0.0223  -0.0071 49  VAL   A CB  
1246 C  CB  B VAL   A 49  ? 0.1116 0.1317 0.1677 -0.0053 0.0053  0.0016  49  VAL   A CB  
1247 C  CG1 A VAL   A 49  ? 0.1630 0.1293 0.1992 0.0071  0.0253  -0.0089 49  VAL   A CG1 
1248 C  CG1 B VAL   A 49  ? 0.1080 0.1255 0.1545 0.0105  0.0122  -0.0067 49  VAL   A CG1 
1249 C  CG2 A VAL   A 49  ? 0.1678 0.1536 0.2318 -0.0172 0.0253  -0.0069 49  VAL   A CG2 
1250 C  CG2 B VAL   A 49  ? 0.1150 0.1376 0.1755 -0.0126 0.0091  0.0029  49  VAL   A CG2 
1269 N  N   . ALA   A 50  ? 0.1212 0.1257 0.1544 0.0019  -0.0068 0.0087  50  ALA   A N   
1270 C  CA  . ALA   A 50  ? 0.1164 0.1282 0.1528 -0.0095 -0.0031 0.0093  50  ALA   A CA  
1271 C  C   . ALA   A 50  ? 0.1182 0.1342 0.1519 -0.0104 -0.0012 0.0061  50  ALA   A C   
1272 O  O   . ALA   A 50  ? 0.1211 0.1293 0.1661 0.0000  -0.0016 0.0021  50  ALA   A O   
1273 C  CB  . ALA   A 50  ? 0.1177 0.1255 0.1495 -0.0041 0.0075  0.0056  50  ALA   A CB  
1280 N  N   . GLY   A 51  ? 0.1212 0.1278 0.1648 0.0020  -0.0064 0.0086  51  GLY   A N   
1281 C  CA  . GLY   A 51  ? 0.1394 0.1216 0.1717 0.0014  -0.0184 0.0022  51  GLY   A CA  
1282 C  C   . GLY   A 51  ? 0.1279 0.1347 0.1647 0.0041  -0.0070 -0.0123 51  GLY   A C   
1283 O  O   . GLY   A 51  ? 0.1292 0.1446 0.1755 0.0026  -0.0085 -0.0138 51  GLY   A O   
1287 N  N   . ALA   A 52  ? 0.1226 0.1445 0.1687 -0.0006 0.0030  -0.0156 52  ALA   A N   
1288 C  CA  . ALA   A 52  ? 0.1222 0.1561 0.1748 -0.0019 0.0095  -0.0141 52  ALA   A CA  
1289 C  C   . ALA   A 52  ? 0.1254 0.1513 0.1572 -0.0088 0.0116  -0.0100 52  ALA   A C   
1290 O  O   . ALA   A 52  ? 0.1348 0.1622 0.1759 -0.0071 0.0062  -0.0115 52  ALA   A O   
1291 C  CB  . ALA   A 52  ? 0.1294 0.1853 0.1950 -0.0098 0.0083  -0.0064 52  ALA   A CB  
1297 N  N   A LEU   A 53  ? 0.1233 0.1483 0.1550 -0.0081 0.0050  -0.0052 53  LEU   A N   
1298 N  N   B LEU   A 53  ? 0.1233 0.1489 0.1466 -0.0065 0.0082  -0.0027 53  LEU   A N   
1299 C  CA  A LEU   A 53  ? 0.1409 0.1534 0.1495 -0.0103 0.0072  -0.0018 53  LEU   A CA  
1300 C  CA  B LEU   A 53  ? 0.1326 0.1513 0.1362 -0.0057 0.0091  0.0032  53  LEU   A CA  
1301 C  C   A LEU   A 53  ? 0.1346 0.1533 0.1297 0.0009  0.0094  0.0059  53  LEU   A C   
1302 C  C   B LEU   A 53  ? 0.1311 0.1517 0.1243 -0.0032 0.0104  0.0038  53  LEU   A C   
1303 O  O   A LEU   A 53  ? 0.1412 0.1602 0.1513 -0.0029 0.0022  0.0061  53  LEU   A O   
1304 O  O   B LEU   A 53  ? 0.1353 0.1542 0.1347 -0.0112 0.0087  -0.0027 53  LEU   A O   
1305 C  CB  A LEU   A 53  ? 0.1524 0.1562 0.1581 -0.0185 0.0063  0.0025  53  LEU   A CB  
1306 C  CB  B LEU   A 53  ? 0.1365 0.1478 0.1348 -0.0053 0.0086  0.0108  53  LEU   A CB  
1307 C  CG  A LEU   A 53  ? 0.1704 0.1597 0.1713 -0.0246 0.0052  0.0070  53  LEU   A CG  
1308 C  CG  B LEU   A 53  ? 0.1422 0.1439 0.1286 -0.0038 0.0025  0.0147  53  LEU   A CG  
1309 C  CD1 A LEU   A 53  ? 0.1804 0.1663 0.1748 -0.0187 -0.0006 0.0061  53  LEU   A CD1 
1310 C  CD1 B LEU   A 53  ? 0.1519 0.1516 0.1326 0.0056  -0.0031 0.0208  53  LEU   A CD1 
1311 C  CD2 A LEU   A 53  ? 0.1806 0.1726 0.1684 -0.0246 0.0045  0.0096  53  LEU   A CD2 
1312 C  CD2 B LEU   A 53  ? 0.1412 0.1444 0.1204 -0.0047 -0.0002 0.0099  53  LEU   A CD2 
1335 N  N   . ASN   A 54  ? 0.1274 0.1453 0.1307 -0.0043 0.0007  0.0034  54  ASN   A N   
1336 C  CA  . ASN   A 54  ? 0.1178 0.1361 0.1560 -0.0054 0.0001  0.0015  54  ASN   A CA  
1337 C  C   . ASN   A 54  ? 0.1301 0.1442 0.1603 -0.0138 0.0036  0.0013  54  ASN   A C   
1338 O  O   . ASN   A 54  ? 0.1349 0.1521 0.1688 -0.0081 -0.0042 -0.0061 54  ASN   A O   
1339 C  CB  . ASN   A 54  ? 0.1164 0.1372 0.1659 -0.0093 -0.0070 0.0039  54  ASN   A CB  
1340 C  CG  . ASN   A 54  ? 0.1217 0.1427 0.1597 -0.0013 -0.0015 0.0006  54  ASN   A CG  
1341 O  OD1 . ASN   A 54  ? 0.1206 0.1430 0.1655 -0.0018 -0.0086 0.0048  54  ASN   A OD1 
1342 N  ND2 . ASN   A 54  ? 0.1294 0.1469 0.1768 -0.0135 -0.0134 0.0181  54  ASN   A ND2 
1350 N  N   . LYS   A 55  ? 0.1316 0.1463 0.1682 -0.0072 -0.0044 -0.0074 55  LYS   A N   
1351 C  CA  . LYS   A 55  ? 0.1399 0.1536 0.1779 0.0008  -0.0059 -0.0169 55  LYS   A CA  
1352 C  C   . LYS   A 55  ? 0.1356 0.1581 0.1762 -0.0042 0.0040  -0.0246 55  LYS   A C   
1353 O  O   . LYS   A 55  ? 0.1435 0.1728 0.1794 0.0005  -0.0052 -0.0269 55  LYS   A O   
1354 C  CB  . LYS   A 55  ? 0.1448 0.1620 0.1950 0.0131  -0.0046 -0.0264 55  LYS   A CB  
1355 C  CG  . LYS   A 55  ? 0.1623 0.1943 0.2106 0.0270  -0.0150 -0.0301 55  LYS   A CG  
1356 C  CD  . LYS   A 55  ? 0.1784 0.2286 0.2154 0.0427  -0.0156 -0.0297 55  LYS   A CD  
1357 C  CE  . LYS   A 55  ? 0.2003 0.2543 0.2331 0.0611  -0.0205 -0.0350 55  LYS   A CE  
1358 N  NZ  . LYS   A 55  ? 0.2099 0.2690 0.2334 0.0696  -0.0279 -0.0287 55  LYS   A NZ  
1372 N  N   . ALA   A 56  ? 0.1399 0.1711 0.1795 -0.0132 0.0023  -0.0251 56  ALA   A N   
1373 C  CA  . ALA   A 56  ? 0.1517 0.1929 0.1716 -0.0185 0.0130  -0.0199 56  ALA   A CA  
1374 C  C   . ALA   A 56  ? 0.1539 0.2026 0.1474 -0.0198 0.0189  -0.0195 56  ALA   A C   
1375 O  O   . ALA   A 56  ? 0.1658 0.2317 0.1611 -0.0027 0.0199  -0.0141 56  ALA   A O   
1376 C  CB  . ALA   A 56  ? 0.1575 0.2107 0.1726 -0.0233 0.0116  -0.0078 56  ALA   A CB  
1382 N  N   . THR   A 57  ? 0.1408 0.1844 0.1518 -0.0152 0.0162  -0.0150 57  THR   A N   
1383 C  CA  . THR   A 57  ? 0.1476 0.1736 0.1502 -0.0164 0.0024  -0.0064 57  THR   A CA  
1384 C  C   . THR   A 57  ? 0.1503 0.1804 0.1549 -0.0073 -0.0025 -0.0167 57  THR   A C   
1385 O  O   . THR   A 57  ? 0.1473 0.1834 0.1740 -0.0120 -0.0094 -0.0258 57  THR   A O   
1386 C  CB  . THR   A 57  ? 0.1402 0.1730 0.1529 -0.0148 0.0038  -0.0042 57  THR   A CB  
1387 O  OG1 . THR   A 57  ? 0.1335 0.1669 0.1595 -0.0083 0.0010  -0.0056 57  THR   A OG1 
1388 C  CG2 . THR   A 57  ? 0.1461 0.1760 0.1453 -0.0092 0.0004  0.0039  57  THR   A CG2 
1396 N  N   . ASN   A 58  ? 0.1522 0.1739 0.1752 -0.0082 0.0039  -0.0352 58  ASN   A N   
1397 C  CA  . ASN   A 58  ? 0.1655 0.1688 0.1932 -0.0097 0.0107  -0.0401 58  ASN   A CA  
1398 C  C   . ASN   A 58  ? 0.1437 0.1558 0.1848 -0.0025 -0.0012 -0.0241 58  ASN   A C   
1399 O  O   . ASN   A 58  ? 0.1486 0.1681 0.1942 -0.0173 -0.0020 -0.0269 58  ASN   A O   
1400 C  CB  . ASN   A 58  ? 0.2146 0.1869 0.2280 -0.0178 0.0345  -0.0444 58  ASN   A CB  
1401 C  CG  . ASN   A 58  ? 0.2573 0.2111 0.2950 -0.0176 0.0350  -0.0278 58  ASN   A CG  
1402 O  OD1 . ASN   A 58  ? 0.2860 0.2038 0.3375 0.0101  0.0658  -0.0153 58  ASN   A OD1 
1403 N  ND2 . ASN   A 58  ? 0.2670 0.2219 0.3207 -0.0187 0.0231  -0.0346 58  ASN   A ND2 
1410 N  N   . ASN   A 59  ? 0.1313 0.1483 0.1744 -0.0042 -0.0099 -0.0188 59  ASN   A N   
1411 C  CA  . ASN   A 59  ? 0.1335 0.1361 0.1729 0.0001  -0.0023 -0.0033 59  ASN   A CA  
1412 C  C   . ASN   A 59  ? 0.1375 0.1336 0.1554 -0.0096 -0.0059 -0.0083 59  ASN   A C   
1413 O  O   . ASN   A 59  ? 0.1338 0.1426 0.1671 -0.0070 0.0012  0.0003  59  ASN   A O   
1414 C  CB  . ASN   A 59  ? 0.1402 0.1382 0.1782 0.0041  -0.0184 -0.0126 59  ASN   A CB  
1415 C  CG  . ASN   A 59  ? 0.1408 0.1419 0.1841 -0.0015 -0.0248 0.0060  59  ASN   A CG  
1416 O  OD1 . ASN   A 59  ? 0.1520 0.1474 0.1747 -0.0128 -0.0237 0.0095  59  ASN   A OD1 
1417 N  ND2 . ASN   A 59  ? 0.1518 0.1419 0.1911 -0.0103 -0.0190 0.0048  59  ASN   A ND2 
1424 N  N   . ALA   A 60  ? 0.1287 0.1483 0.1608 -0.0049 -0.0014 0.0030  60  ALA   A N   
1425 C  CA  . ALA   A 60  ? 0.1302 0.1469 0.1696 -0.0057 -0.0055 0.0010  60  ALA   A CA  
1426 C  C   . ALA   A 60  ? 0.1324 0.1422 0.1761 -0.0049 -0.0101 0.0031  60  ALA   A C   
1427 O  O   . ALA   A 60  ? 0.1246 0.1405 0.2017 -0.0038 -0.0074 -0.0077 60  ALA   A O   
1428 C  CB  . ALA   A 60  ? 0.1426 0.1602 0.1750 -0.0045 -0.0106 -0.0132 60  ALA   A CB  
1434 N  N   . MET   A 61  ? 0.1274 0.1415 0.1625 -0.0121 -0.0044 0.0007  61  MET   A N   
1435 C  CA  . MET   A 61  ? 0.1260 0.1326 0.1574 -0.0077 0.0012  0.0036  61  MET   A CA  
1436 C  C   . MET   A 61  ? 0.1268 0.1317 0.1627 -0.0112 -0.0014 -0.0030 61  MET   A C   
1437 O  O   . MET   A 61  ? 0.1325 0.1307 0.1687 -0.0046 0.0081  0.0098  61  MET   A O   
1438 C  CB  . MET   A 61  ? 0.1340 0.1362 0.1560 -0.0046 0.0057  0.0075  61  MET   A CB  
1439 C  CG  . MET   A 61  ? 0.1358 0.1421 0.1733 -0.0034 0.0046  0.0063  61  MET   A CG  
1440 S  SD  . MET   A 61  ? 0.1380 0.1462 0.1954 -0.0127 -0.0011 -0.0130 61  MET   A SD  
1441 C  CE  . MET   A 61  ? 0.1620 0.1558 0.2329 -0.0202 0.0125  -0.0041 61  MET   A CE  
1451 N  N   . GLN   A 62  ? 0.1289 0.1288 0.1612 -0.0144 -0.0014 -0.0017 62  GLN   A N   
1452 C  CA  . GLN   A 62  ? 0.1281 0.1290 0.1741 -0.0082 0.0039  0.0074  62  GLN   A CA  
1453 C  C   . GLN   A 62  ? 0.1309 0.1167 0.1726 -0.0016 0.0025  0.0018  62  GLN   A C   
1454 O  O   . GLN   A 62  ? 0.1319 0.1327 0.1727 -0.0047 0.0059  -0.0005 62  GLN   A O   
1455 C  CB  . GLN   A 62  ? 0.1276 0.1227 0.1787 -0.0029 0.0045  0.0103  62  GLN   A CB  
1456 C  CG  . GLN   A 62  ? 0.1311 0.1217 0.1733 -0.0065 -0.0002 0.0190  62  GLN   A CG  
1457 C  CD  . GLN   A 62  ? 0.1381 0.1301 0.1661 0.0014  0.0083  0.0145  62  GLN   A CD  
1458 O  OE1 . GLN   A 62  ? 0.1387 0.1425 0.1731 -0.0019 -0.0009 0.0072  62  GLN   A OE1 
1459 N  NE2 . GLN   A 62  ? 0.1437 0.1359 0.1830 0.0024  0.0049  -0.0023 62  GLN   A NE2 
1468 N  N   . VAL   A 63  ? 0.1226 0.1276 0.1918 -0.0088 0.0069  -0.0139 63  VAL   A N   
1469 C  CA  . VAL   A 63  ? 0.1275 0.1399 0.2089 -0.0098 0.0052  -0.0101 63  VAL   A CA  
1470 C  C   . VAL   A 63  ? 0.1180 0.1418 0.1952 -0.0131 -0.0038 -0.0072 63  VAL   A C   
1471 O  O   . VAL   A 63  ? 0.1196 0.1383 0.2166 -0.0179 -0.0010 -0.0061 63  VAL   A O   
1472 C  CB  . VAL   A 63  ? 0.1399 0.1547 0.2322 -0.0157 -0.0049 -0.0325 63  VAL   A CB  
1473 C  CG1 . VAL   A 63  ? 0.1538 0.1746 0.2591 -0.0141 -0.0145 -0.0522 63  VAL   A CG1 
1474 C  CG2 . VAL   A 63  ? 0.1463 0.1524 0.2435 -0.0144 0.0078  -0.0348 63  VAL   A CG2 
1484 N  N   . GLU   A 64  ? 0.1259 0.1425 0.1853 -0.0050 -0.0055 0.0011  64  GLU   A N   
1485 C  CA  . GLU   A 64  ? 0.1241 0.1439 0.1838 -0.0075 -0.0113 0.0055  64  GLU   A CA  
1486 C  C   . GLU   A 64  ? 0.1166 0.1372 0.1820 -0.0097 0.0000  0.0072  64  GLU   A C   
1487 O  O   . GLU   A 64  ? 0.1236 0.1397 0.1950 -0.0056 0.0033  0.0018  64  GLU   A O   
1488 C  CB  . GLU   A 64  ? 0.1332 0.1510 0.1922 -0.0095 0.0007  0.0030  64  GLU   A CB  
1489 C  CG  . GLU   A 64  ? 0.1432 0.1582 0.2041 -0.0075 0.0001  0.0050  64  GLU   A CG  
1490 C  CD  . GLU   A 64  ? 0.1574 0.1647 0.2135 -0.0126 0.0102  0.0046  64  GLU   A CD  
1491 O  OE1 . GLU   A 64  ? 0.1517 0.1789 0.2325 -0.0200 0.0161  0.0097  64  GLU   A OE1 
1492 O  OE2 . GLU   A 64  ? 0.1772 0.1637 0.2016 -0.0214 -0.0011 0.0121  64  GLU   A OE2 
1499 N  N   . SER   A 65  ? 0.1138 0.1299 0.1777 -0.0039 0.0021  0.0046  65  SER   A N   
1500 C  CA  . SER   A 65  ? 0.1247 0.1279 0.1718 -0.0069 0.0025  -0.0056 65  SER   A CA  
1501 C  C   . SER   A 65  ? 0.1268 0.1386 0.1632 -0.0059 -0.0001 -0.0007 65  SER   A C   
1502 O  O   . SER   A 65  ? 0.1355 0.1439 0.1861 -0.0001 0.0159  -0.0019 65  SER   A O   
1503 C  CB  . SER   A 65  ? 0.1281 0.1348 0.1692 -0.0066 0.0037  0.0110  65  SER   A CB  
1504 O  OG  . SER   A 65  ? 0.1265 0.1461 0.1757 -0.0113 -0.0033 0.0163  65  SER   A OG  
1510 N  N   . ASP   A 66  ? 0.1262 0.1361 0.1812 -0.0072 0.0127  0.0097  66  ASP   A N   
1511 C  CA  . ASP   A 66  ? 0.1352 0.1492 0.1957 -0.0025 0.0140  0.0230  66  ASP   A CA  
1512 C  C   . ASP   A 66  ? 0.1336 0.1387 0.1932 -0.0086 0.0118  0.0226  66  ASP   A C   
1513 O  O   . ASP   A 66  ? 0.1414 0.1516 0.2147 -0.0052 0.0276  0.0245  66  ASP   A O   
1514 C  CB  . ASP   A 66  ? 0.1456 0.1542 0.2256 0.0084  0.0207  0.0393  66  ASP   A CB  
1515 C  CG  . ASP   A 66  ? 0.1719 0.1685 0.2540 -0.0022 0.0034  0.0523  66  ASP   A CG  
1516 O  OD1 . ASP   A 66  ? 0.1720 0.1998 0.2344 -0.0115 -0.0061 0.0591  66  ASP   A OD1 
1517 O  OD2 . ASP   A 66  ? 0.1914 0.1839 0.3264 0.0168  -0.0152 0.0252  66  ASP   A OD2 
1522 N  N   . ASP   A 67  ? 0.1289 0.1443 0.1963 -0.0057 0.0127  0.0189  67  ASP   A N   
1523 C  CA  . ASP   A 67  ? 0.1264 0.1569 0.2233 -0.0034 0.0053  0.0257  67  ASP   A CA  
1524 C  C   . ASP   A 67  ? 0.1303 0.1582 0.2289 0.0004  0.0109  0.0291  67  ASP   A C   
1525 O  O   . ASP   A 67  ? 0.1281 0.1636 0.2506 0.0040  0.0295  0.0321  67  ASP   A O   
1526 C  CB  . ASP   A 67  ? 0.1366 0.1640 0.2471 -0.0090 -0.0047 0.0295  67  ASP   A CB  
1527 C  CG  . ASP   A 67  ? 0.1316 0.1799 0.2889 -0.0117 -0.0227 0.0402  67  ASP   A CG  
1528 O  OD1 . ASP   A 67  ? 0.1391 0.2013 0.3584 -0.0141 -0.0323 0.0537  67  ASP   A OD1 
1529 O  OD2 . ASP   A 67  ? 0.1373 0.1837 0.2820 0.0012  -0.0202 0.0305  67  ASP   A OD2 
1534 N  N   . TYR   A 68  ? 0.1293 0.1455 0.2168 0.0013  0.0152  0.0279  68  TYR   A N   
1535 C  CA  . TYR   A 68  ? 0.1424 0.1437 0.2098 -0.0009 0.0165  0.0313  68  TYR   A CA  
1536 C  C   . TYR   A 68  ? 0.1351 0.1440 0.2114 -0.0027 0.0146  0.0166  68  TYR   A C   
1537 O  O   . TYR   A 68  ? 0.1385 0.1461 0.2156 0.0063  0.0225  0.0184  68  TYR   A O   
1538 C  CB  . TYR   A 68  ? 0.1449 0.1449 0.2218 0.0074  0.0341  0.0345  68  TYR   A CB  
1539 C  CG  . TYR   A 68  ? 0.1499 0.1557 0.2560 0.0020  0.0453  0.0341  68  TYR   A CG  
1540 C  CD1 . TYR   A 68  ? 0.1602 0.1615 0.2768 -0.0215 0.0430  -0.0034 68  TYR   A CD1 
1541 C  CD2 . TYR   A 68  ? 0.1723 0.1545 0.2879 0.0107  0.0484  0.0438  68  TYR   A CD2 
1542 C  CE1 . TYR   A 68  ? 0.1703 0.1700 0.3061 -0.0178 0.0508  -0.0069 68  TYR   A CE1 
1543 C  CE2 . TYR   A 68  ? 0.1759 0.1617 0.3069 -0.0002 0.0611  0.0206  68  TYR   A CE2 
1544 C  CZ  . TYR   A 68  ? 0.1765 0.1654 0.3155 -0.0177 0.0473  -0.0073 68  TYR   A CZ  
1545 O  OH  . TYR   A 68  ? 0.2019 0.1673 0.3247 -0.0161 0.0215  -0.0245 68  TYR   A OH  
1555 N  N   . ILE   A 69  ? 0.1276 0.1375 0.2051 -0.0010 0.0177  0.0198  69  ILE   A N   
1556 C  CA  . ILE   A 69  ? 0.1378 0.1391 0.1990 0.0049  0.0184  0.0099  69  ILE   A CA  
1557 C  C   . ILE   A 69  ? 0.1428 0.1422 0.1955 0.0064  0.0222  0.0154  69  ILE   A C   
1558 O  O   . ILE   A 69  ? 0.1500 0.1501 0.2013 -0.0018 0.0336  0.0189  69  ILE   A O   
1559 C  CB  . ILE   A 69  ? 0.1455 0.1579 0.2015 0.0034  0.0222  0.0064  69  ILE   A CB  
1560 C  CG1 . ILE   A 69  ? 0.1452 0.1714 0.2135 0.0104  0.0159  -0.0110 69  ILE   A CG1 
1561 C  CG2 . ILE   A 69  ? 0.1701 0.1776 0.2100 0.0096  0.0123  -0.0038 69  ILE   A CG2 
1562 C  CD1 . ILE   A 69  ? 0.1458 0.1783 0.2223 -0.0019 0.0155  -0.0110 69  ILE   A CD1 
1574 N  N   . ALA   A 70  ? 0.1495 0.1464 0.2103 -0.0070 0.0283  0.0214  70  ALA   A N   
1575 C  CA  . ALA   A 70  ? 0.1523 0.1561 0.2348 -0.0159 0.0340  0.0225  70  ALA   A CA  
1576 C  C   . ALA   A 70  ? 0.1444 0.1700 0.2418 -0.0145 0.0332  0.0173  70  ALA   A C   
1577 O  O   . ALA   A 70  ? 0.1646 0.2019 0.2585 0.0077  0.0586  0.0310  70  ALA   A O   
1578 C  CB  . ALA   A 70  ? 0.1600 0.1491 0.2476 -0.0195 0.0316  0.0117  70  ALA   A CB  
1584 N  N   . THR   A 71  ? 0.1371 0.1663 0.2337 -0.0021 0.0257  0.0187  71  THR   A N   
1585 C  CA  . THR   A 71  ? 0.1492 0.1871 0.2642 0.0035  0.0234  0.0191  71  THR   A CA  
1586 C  C   . THR   A 71  ? 0.1365 0.1784 0.2816 0.0129  0.0317  0.0169  71  THR   A C   
1587 O  O   . THR   A 71  ? 0.1425 0.2053 0.3324 0.0080  0.0419  -0.0133 71  THR   A O   
1588 C  CB  . THR   A 71  ? 0.1771 0.2139 0.2942 0.0154  -0.0121 0.0309  71  THR   A CB  
1589 O  OG1 . THR   A 71  ? 0.2054 0.2300 0.3097 0.0063  -0.0341 0.0272  71  THR   A OG1 
1590 C  CG2 . THR   A 71  ? 0.1902 0.2324 0.3194 0.0234  -0.0245 0.0446  71  THR   A CG2 
1598 N  N   . ASN   A 72  ? 0.1432 0.1596 0.2447 0.0116  0.0298  0.0206  72  ASN   A N   
1599 C  CA  . ASN   A 72  ? 0.1481 0.1615 0.2485 0.0134  0.0386  0.0198  72  ASN   A CA  
1600 C  C   . ASN   A 72  ? 0.1628 0.1585 0.2402 0.0060  0.0487  0.0198  72  ASN   A C   
1601 O  O   . ASN   A 72  ? 0.1803 0.1570 0.2656 0.0101  0.0480  -0.0001 72  ASN   A O   
1602 C  CB  . ASN   A 72  ? 0.1739 0.1684 0.2504 0.0127  0.0379  0.0238  72  ASN   A CB  
1603 C  CG  . ASN   A 72  ? 0.1960 0.1809 0.2532 0.0213  0.0352  0.0300  72  ASN   A CG  
1604 O  OD1 . ASN   A 72  ? 0.2136 0.2151 0.2720 0.0240  0.0443  0.0347  72  ASN   A OD1 
1605 N  ND2 . ASN   A 72  ? 0.2119 0.1804 0.2569 0.0492  0.0188  0.0189  72  ASN   A ND2 
1612 N  N   . GLY   A 73  ? 0.1673 0.1547 0.2186 -0.0008 0.0465  0.0118  73  GLY   A N   
1613 C  CA  . GLY   A 73  ? 0.1710 0.1502 0.2068 -0.0047 0.0458  0.0085  73  GLY   A CA  
1614 C  C   . GLY   A 73  ? 0.1674 0.1411 0.2037 0.0028  0.0506  0.0238  73  GLY   A C   
1615 O  O   . GLY   A 73  ? 0.1685 0.1486 0.2246 0.0102  0.0407  0.0292  73  GLY   A O   
1619 N  N   . PRO   A 74  ? 0.1815 0.1471 0.1992 -0.0144 0.0506  0.0102  74  PRO   A N   
1620 C  CA  . PRO   A 74  ? 0.1735 0.1459 0.2090 -0.0032 0.0485  0.0115  74  PRO   A CA  
1621 C  C   . PRO   A 74  ? 0.1683 0.1334 0.2077 -0.0011 0.0348  0.0006  74  PRO   A C   
1622 O  O   . PRO   A 74  ? 0.1734 0.1408 0.2274 0.0070  0.0367  -0.0027 74  PRO   A O   
1623 C  CB  . PRO   A 74  ? 0.1903 0.1756 0.2325 0.0012  0.0462  0.0194  74  PRO   A CB  
1624 C  CG  . PRO   A 74  ? 0.2212 0.2099 0.2703 -0.0204 0.0354  0.0093  74  PRO   A CG  
1625 C  CD  . PRO   A 74  ? 0.2009 0.1795 0.2243 -0.0277 0.0349  -0.0004 74  PRO   A CD  
1633 N  N   . LEU   A 75  ? 0.1643 0.1262 0.1931 0.0002  0.0247  0.0050  75  LEU   A N   
1634 C  CA  . LEU   A 75  ? 0.1622 0.1270 0.1740 0.0025  0.0115  0.0129  75  LEU   A CA  
1635 C  C   . LEU   A 75  ? 0.1709 0.1408 0.1850 0.0060  0.0068  0.0153  75  LEU   A C   
1636 O  O   . LEU   A 75  ? 0.2000 0.1572 0.1931 0.0134  0.0051  0.0116  75  LEU   A O   
1637 C  CB  . LEU   A 75  ? 0.1698 0.1262 0.1803 -0.0066 0.0104  0.0201  75  LEU   A CB  
1638 C  CG  . LEU   A 75  ? 0.1831 0.1629 0.1793 -0.0318 0.0035  0.0163  75  LEU   A CG  
1639 C  CD1 . LEU   A 75  ? 0.1954 0.2123 0.2018 -0.0295 0.0038  -0.0016 75  LEU   A CD1 
1640 C  CD2 . LEU   A 75  ? 0.2070 0.2074 0.2288 -0.0064 -0.0046 0.0183  75  LEU   A CD2 
1652 N  N   . LYS   A 76  ? 0.1727 0.1409 0.1940 -0.0077 0.0120  -0.0031 76  LYS   A N   
1653 C  CA  . LYS   A 76  ? 0.1697 0.1583 0.1965 -0.0107 0.0157  -0.0069 76  LYS   A CA  
1654 C  C   . LYS   A 76  ? 0.1633 0.1435 0.1661 -0.0018 0.0124  0.0039  76  LYS   A C   
1655 O  O   . LYS   A 76  ? 0.1683 0.1387 0.1739 0.0023  0.0160  0.0119  76  LYS   A O   
1656 C  CB  . LYS   A 76  ? 0.1687 0.1777 0.2300 0.0016  0.0089  -0.0329 76  LYS   A CB  
1657 C  CG  . LYS   A 76  ? 0.1804 0.1790 0.2772 0.0075  0.0078  -0.0359 76  LYS   A CG  
1658 C  CD  . LYS   A 76  ? 0.1902 0.1800 0.3230 0.0075  0.0032  -0.0396 76  LYS   A CD  
1659 C  CE  . LYS   A 76  ? 0.2065 0.1966 0.3780 -0.0005 0.0097  -0.0406 76  LYS   A CE  
1660 N  NZ  . LYS   A 76  ? 0.2063 0.1850 0.4159 -0.0182 0.0021  -0.0466 76  LYS   A NZ  
1674 N  N   . VAL   A 77  ? 0.1770 0.1500 0.1624 0.0006  0.0223  0.0084  77  VAL   A N   
1675 C  CA  . VAL   A 77  ? 0.1719 0.1510 0.1663 0.0069  0.0133  0.0090  77  VAL   A CA  
1676 C  C   . VAL   A 77  ? 0.1636 0.1443 0.1688 0.0078  0.0135  0.0053  77  VAL   A C   
1677 O  O   . VAL   A 77  ? 0.1725 0.1491 0.1771 0.0100  0.0308  -0.0068 77  VAL   A O   
1678 C  CB  . VAL   A 77  ? 0.1888 0.1700 0.1623 0.0009  0.0089  0.0131  77  VAL   A CB  
1679 C  CG1 . VAL   A 77  ? 0.1870 0.1878 0.1767 0.0154  0.0055  0.0080  77  VAL   A CG1 
1680 C  CG2 . VAL   A 77  ? 0.2146 0.1807 0.1842 -0.0085 -0.0018 0.0278  77  VAL   A CG2 
1690 N  N   . GLY   A 78  ? 0.1570 0.1402 0.1730 0.0016  0.0245  0.0028  78  GLY   A N   
1691 C  CA  . GLY   A 78  ? 0.1595 0.1376 0.1823 0.0019  0.0216  0.0119  78  GLY   A CA  
1692 C  C   . GLY   A 78  ? 0.1430 0.1301 0.1863 0.0054  0.0221  0.0154  78  GLY   A C   
1693 O  O   . GLY   A 78  ? 0.1425 0.1388 0.2074 0.0003  0.0149  0.0256  78  GLY   A O   
1697 N  N   . GLY   A 79  ? 0.1508 0.1301 0.1765 -0.0024 0.0223  0.0162  79  GLY   A N   
1698 C  CA  . GLY   A 79  ? 0.1466 0.1355 0.1904 0.0014  0.0155  0.0181  79  GLY   A CA  
1699 C  C   . GLY   A 79  ? 0.1338 0.1303 0.1791 -0.0032 0.0116  0.0098  79  GLY   A C   
1700 O  O   . GLY   A 79  ? 0.1389 0.1391 0.1937 0.0149  0.0120  0.0115  79  GLY   A O   
1704 N  N   . SER   A 80  ? 0.1332 0.1411 0.2000 -0.0051 0.0143  0.0006  80  SER   A N   
1705 C  CA  . SER   A 80  ? 0.1301 0.1380 0.1928 0.0003  0.0072  0.0103  80  SER   A CA  
1706 C  C   . SER   A 80  ? 0.1259 0.1393 0.1826 -0.0076 0.0105  0.0129  80  SER   A C   
1707 O  O   . SER   A 80  ? 0.1277 0.1665 0.2107 0.0041  0.0141  0.0040  80  SER   A O   
1708 C  CB  . SER   A 80  ? 0.1484 0.1375 0.2206 -0.0028 0.0154  0.0108  80  SER   A CB  
1709 O  OG  . SER   A 80  ? 0.1746 0.1363 0.2439 0.0042  0.0018  0.0256  80  SER   A OG  
1715 N  N   . CYS   A 81  ? 0.1263 0.1328 0.1819 -0.0031 -0.0027 0.0224  81  CYS   A N   
1716 C  CA  . CYS   A 81  ? 0.1298 0.1457 0.1841 -0.0036 -0.0039 0.0298  81  CYS   A CA  
1717 C  C   . CYS   A 81  ? 0.1281 0.1357 0.1773 -0.0062 -0.0023 0.0293  81  CYS   A C   
1718 O  O   . CYS   A 81  ? 0.1218 0.1660 0.1992 -0.0029 -0.0016 0.0373  81  CYS   A O   
1719 C  CB  . CYS   A 81  ? 0.1343 0.1522 0.1996 -0.0108 0.0002  0.0333  81  CYS   A CB  
1720 S  SG  . CYS   A 81  ? 0.1477 0.1396 0.1841 -0.0140 -0.0006 0.0177  81  CYS   A SG  
1726 N  N   . VAL   A 82  ? 0.1332 0.1483 0.1763 -0.0027 -0.0161 0.0267  82  VAL   A N   
1727 C  CA  . VAL   A 82  ? 0.1474 0.1521 0.1810 -0.0004 -0.0070 0.0372  82  VAL   A CA  
1728 C  C   . VAL   A 82  ? 0.1451 0.1613 0.1872 -0.0019 -0.0122 0.0391  82  VAL   A C   
1729 O  O   . VAL   A 82  ? 0.1315 0.1692 0.2055 -0.0028 -0.0062 0.0131  82  VAL   A O   
1730 C  CB  . VAL   A 82  ? 0.1756 0.1669 0.2057 0.0017  -0.0017 0.0387  82  VAL   A CB  
1731 C  CG1 . VAL   A 82  ? 0.1904 0.1823 0.2296 0.0071  -0.0017 0.0366  82  VAL   A CG1 
1732 C  CG2 . VAL   A 82  ? 0.1815 0.1691 0.2293 -0.0012 -0.0018 0.0421  82  VAL   A CG2 
1742 N  N   . LEU   A 83  ? 0.1365 0.1559 0.1740 -0.0129 -0.0103 0.0259  83  LEU   A N   
1743 C  CA  . LEU   A 83  ? 0.1372 0.1560 0.1612 -0.0150 -0.0116 0.0179  83  LEU   A CA  
1744 C  C   . LEU   A 83  ? 0.1436 0.1585 0.1620 -0.0121 -0.0141 0.0237  83  LEU   A C   
1745 O  O   . LEU   A 83  ? 0.1526 0.1659 0.1792 -0.0184 -0.0068 0.0315  83  LEU   A O   
1746 C  CB  . LEU   A 83  ? 0.1458 0.1618 0.1699 -0.0171 -0.0140 0.0166  83  LEU   A CB  
1747 C  CG  . LEU   A 83  ? 0.1540 0.1688 0.1764 -0.0151 -0.0030 0.0107  83  LEU   A CG  
1748 C  CD1 . LEU   A 83  ? 0.1684 0.1738 0.1866 -0.0292 0.0002  0.0222  83  LEU   A CD1 
1749 C  CD2 . LEU   A 83  ? 0.1545 0.1856 0.1871 -0.0146 0.0108  0.0209  83  LEU   A CD2 
1761 N  N   . SER   A 84  ? 0.1601 0.1650 0.1682 -0.0163 -0.0117 0.0283  84  SER   A N   
1762 C  CA  . SER   A 84  ? 0.1707 0.1725 0.1477 -0.0155 -0.0135 0.0250  84  SER   A CA  
1763 C  C   . SER   A 84  ? 0.1719 0.1757 0.1449 -0.0223 -0.0005 0.0173  84  SER   A C   
1764 O  O   . SER   A 84  ? 0.1648 0.1854 0.1483 -0.0150 -0.0090 0.0214  84  SER   A O   
1765 C  CB  . SER   A 84  ? 0.1747 0.1939 0.1567 -0.0161 -0.0195 0.0120  84  SER   A CB  
1766 O  OG  . SER   A 84  ? 0.1807 0.2181 0.1774 -0.0174 -0.0255 -0.0026 84  SER   A OG  
1772 N  N   . GLY   A 85  ? 0.1874 0.1924 0.1509 -0.0281 0.0124  0.0192  85  GLY   A N   
1773 C  CA  . GLY   A 85  ? 0.1852 0.1987 0.1660 -0.0298 0.0131  -0.0007 85  GLY   A CA  
1774 C  C   . GLY   A 85  ? 0.1800 0.2031 0.1556 -0.0298 0.0004  0.0039  85  GLY   A C   
1775 O  O   . GLY   A 85  ? 0.1804 0.2114 0.1769 -0.0381 0.0116  -0.0064 85  GLY   A O   
1779 N  N   . HIS   A 86  ? 0.1833 0.1961 0.1481 -0.0248 -0.0058 0.0094  86  HIS   A N   
1780 C  CA  . HIS   A 86  ? 0.2000 0.2040 0.1338 -0.0307 -0.0028 0.0095  86  HIS   A CA  
1781 C  C   . HIS   A 86  ? 0.2245 0.2174 0.1322 -0.0356 -0.0060 0.0036  86  HIS   A C   
1782 O  O   . HIS   A 86  ? 0.2375 0.2421 0.1488 -0.0333 0.0088  0.0100  86  HIS   A O   
1783 C  CB  . HIS   A 86  ? 0.1952 0.1947 0.1489 -0.0280 -0.0020 0.0102  86  HIS   A CB  
1784 C  CG  . HIS   A 86  ? 0.1909 0.1913 0.1495 -0.0150 -0.0020 0.0183  86  HIS   A CG  
1785 N  ND1 . HIS   A 86  ? 0.2012 0.1899 0.1881 -0.0250 -0.0020 0.0121  86  HIS   A ND1 
1786 C  CD2 . HIS   A 86  ? 0.1889 0.1825 0.1470 -0.0032 0.0021  0.0166  86  HIS   A CD2 
1787 C  CE1 . HIS   A 86  ? 0.1940 0.1851 0.1830 -0.0155 0.0162  0.0202  86  HIS   A CE1 
1788 N  NE2 . HIS   A 86  ? 0.1933 0.1797 0.1640 0.0008  0.0128  0.0274  86  HIS   A NE2 
1796 N  N   . ASN   A 87  ? 0.2411 0.2293 0.1529 -0.0290 0.0159  -0.0079 87  ASN   A N   
1797 C  CA  . ASN   A 87  ? 0.2627 0.2384 0.1523 -0.0266 0.0381  -0.0138 87  ASN   A CA  
1798 C  C   . ASN   A 87  ? 0.2654 0.2553 0.1802 -0.0322 0.0581  -0.0053 87  ASN   A C   
1799 O  O   . ASN   A 87  ? 0.2873 0.2724 0.2225 -0.0446 0.0822  -0.0130 87  ASN   A O   
1800 C  CB  . ASN   A 87  ? 0.2766 0.2440 0.1626 -0.0166 0.0410  -0.0107 87  ASN   A CB  
1801 C  CG  . ASN   A 87  ? 0.2891 0.2569 0.1739 -0.0041 0.0519  0.0008  87  ASN   A CG  
1802 O  OD1 . ASN   A 87  ? 0.3002 0.2552 0.1761 0.0117  0.0497  0.0138  87  ASN   A OD1 
1803 N  ND2 . ASN   A 87  ? 0.2955 0.2787 0.1836 -0.0015 0.0517  0.0066  87  ASN   A ND2 
1810 N  N   . LEU   A 88  ? 0.2380 0.2439 0.1753 -0.0351 0.0423  0.0078  88  LEU   A N   
1811 C  CA  . LEU   A 88  ? 0.2149 0.2379 0.1935 -0.0390 0.0359  0.0203  88  LEU   A CA  
1812 C  C   . LEU   A 88  ? 0.2016 0.2412 0.1875 -0.0391 0.0337  0.0353  88  LEU   A C   
1813 O  O   . LEU   A 88  ? 0.2067 0.2439 0.2214 -0.0373 0.0404  0.0531  88  LEU   A O   
1814 C  CB  . LEU   A 88  ? 0.2107 0.2409 0.2066 -0.0432 0.0061  0.0250  88  LEU   A CB  
1815 C  CG  . LEU   A 88  ? 0.2297 0.2533 0.2311 -0.0436 -0.0051 0.0274  88  LEU   A CG  
1816 C  CD1 . LEU   A 88  ? 0.2415 0.2643 0.2301 -0.0415 -0.0086 0.0210  88  LEU   A CD1 
1817 C  CD2 . LEU   A 88  ? 0.2424 0.2632 0.2683 -0.0373 -0.0044 0.0214  88  LEU   A CD2 
1829 N  N   . ALA   A 89  ? 0.1994 0.2349 0.1648 -0.0375 0.0175  0.0155  89  ALA   A N   
1830 C  CA  . ALA   A 89  ? 0.2064 0.2344 0.1551 -0.0310 0.0047  0.0271  89  ALA   A CA  
1831 C  C   . ALA   A 89  ? 0.2158 0.2372 0.1645 -0.0288 -0.0094 0.0247  89  ALA   A C   
1832 O  O   . ALA   A 89  ? 0.2094 0.2282 0.1921 -0.0385 -0.0153 0.0023  89  ALA   A O   
1833 C  CB  . ALA   A 89  ? 0.2018 0.2318 0.1452 -0.0249 0.0062  0.0267  89  ALA   A CB  
1839 N  N   . LYS   A 90  ? 0.2280 0.2551 0.1658 -0.0350 -0.0131 0.0274  90  LYS   A N   
1840 C  CA  . LYS   A 90  ? 0.2389 0.2694 0.1655 -0.0342 -0.0293 0.0312  90  LYS   A CA  
1841 C  C   . LYS   A 90  ? 0.2134 0.2449 0.1655 -0.0339 -0.0293 0.0212  90  LYS   A C   
1842 O  O   . LYS   A 90  ? 0.2153 0.2565 0.1899 -0.0319 -0.0371 0.0133  90  LYS   A O   
1843 C  CB  . LYS   A 90  ? 0.2700 0.3091 0.2070 -0.0325 -0.0314 0.0598  90  LYS   A CB  
1844 C  CG  . LYS   A 90  ? 0.3172 0.3495 0.3144 -0.0325 -0.0259 0.0668  90  LYS   A CG  
1845 C  CD  . LYS   A 90  ? 0.3706 0.3937 0.4215 -0.0350 -0.0090 0.0724  90  LYS   A CD  
1846 C  CE  . LYS   A 90  ? 0.4108 0.4288 0.5052 -0.0364 0.0026  0.0708  90  LYS   A CE  
1847 N  NZ  . LYS   A 90  ? 0.4305 0.4396 0.5570 -0.0371 0.0085  0.0679  90  LYS   A NZ  
1861 N  N   . HIS   A 91  ? 0.1969 0.2148 0.1435 -0.0343 -0.0353 0.0284  91  HIS   A N   
1862 C  CA  . HIS   A 91  ? 0.1840 0.1924 0.1524 -0.0239 -0.0311 0.0289  91  HIS   A CA  
1863 C  C   . HIS   A 91  ? 0.1650 0.1755 0.1530 -0.0236 -0.0139 0.0322  91  HIS   A C   
1864 O  O   . HIS   A 91  ? 0.1621 0.1934 0.1619 -0.0253 -0.0019 0.0331  91  HIS   A O   
1865 C  CB  . HIS   A 91  ? 0.2026 0.2155 0.1991 -0.0036 -0.0429 0.0286  91  HIS   A CB  
1866 C  CG  . HIS   A 91  ? 0.2453 0.2660 0.2627 0.0104  -0.0652 0.0137  91  HIS   A CG  
1867 N  ND1 . HIS   A 91  ? 0.2572 0.2928 0.2982 0.0201  -0.0754 -0.0060 91  HIS   A ND1 
1868 C  CD2 . HIS   A 91  ? 0.2696 0.2884 0.2828 0.0161  -0.0786 0.0200  91  HIS   A CD2 
1869 C  CE1 . HIS   A 91  ? 0.2700 0.3029 0.3097 0.0240  -0.0763 0.0067  91  HIS   A CE1 
1870 N  NE2 . HIS   A 91  ? 0.2792 0.3026 0.3007 0.0270  -0.0849 0.0132  91  HIS   A NE2 
1878 N  N   . CYS   A 92  ? 0.1523 0.1642 0.1587 -0.0251 -0.0126 0.0297  92  CYS   A N   
1879 C  CA  . CYS   A 92  ? 0.1423 0.1578 0.1669 -0.0199 -0.0020 0.0205  92  CYS   A CA  
1880 C  C   . CYS   A 92  ? 0.1413 0.1535 0.1561 -0.0177 0.0011  0.0228  92  CYS   A C   
1881 O  O   . CYS   A 92  ? 0.1379 0.1602 0.1720 -0.0193 -0.0068 0.0221  92  CYS   A O   
1882 C  CB  . CYS   A 92  ? 0.1455 0.1610 0.1674 -0.0128 -0.0045 0.0169  92  CYS   A CB  
1883 S  SG  . CYS   A 92  ? 0.1470 0.1499 0.1482 -0.0158 -0.0035 0.0160  92  CYS   A SG  
1889 N  N   . LEU   A 93  ? 0.1398 0.1390 0.1578 -0.0158 0.0065  0.0207  93  LEU   A N   
1890 C  CA  . LEU   A 93  ? 0.1270 0.1347 0.1624 -0.0102 -0.0015 0.0244  93  LEU   A CA  
1891 C  C   . LEU   A 93  ? 0.1299 0.1273 0.1598 -0.0034 0.0047  0.0196  93  LEU   A C   
1892 O  O   . LEU   A 93  ? 0.1234 0.1364 0.1617 -0.0064 -0.0008 0.0194  93  LEU   A O   
1893 C  CB  . LEU   A 93  ? 0.1368 0.1372 0.1705 -0.0075 -0.0047 0.0294  93  LEU   A CB  
1894 C  CG  . LEU   A 93  ? 0.1396 0.1373 0.1816 -0.0057 0.0013  0.0318  93  LEU   A CG  
1895 C  CD1 . LEU   A 93  ? 0.1485 0.1413 0.2057 -0.0030 0.0063  0.0246  93  LEU   A CD1 
1896 C  CD2 . LEU   A 93  ? 0.1581 0.1424 0.1985 -0.0099 0.0018  0.0236  93  LEU   A CD2 
1908 N  N   . HIS   A 94  ? 0.1228 0.1239 0.1567 -0.0033 0.0045  0.0287  94  HIS   A N   
1909 C  CA  . HIS   A 94  ? 0.1233 0.1210 0.1662 -0.0067 0.0018  0.0191  94  HIS   A CA  
1910 C  C   . HIS   A 94  ? 0.1177 0.1218 0.1677 -0.0069 0.0014  0.0179  94  HIS   A C   
1911 O  O   . HIS   A 94  ? 0.1190 0.1466 0.2031 -0.0027 -0.0008 -0.0026 94  HIS   A O   
1912 C  CB  . HIS   A 94  ? 0.1185 0.1222 0.1668 -0.0042 0.0039  0.0184  94  HIS   A CB  
1913 C  CG  . HIS   A 94  ? 0.1265 0.1211 0.1536 -0.0085 -0.0036 0.0202  94  HIS   A CG  
1914 N  ND1 . HIS   A 94  ? 0.1243 0.1232 0.1578 -0.0037 -0.0024 0.0193  94  HIS   A ND1 
1915 C  CD2 . HIS   A 94  ? 0.1324 0.1342 0.1617 -0.0113 -0.0070 0.0117  94  HIS   A CD2 
1916 C  CE1 . HIS   A 94  ? 0.1339 0.1285 0.1531 -0.0111 -0.0125 0.0157  94  HIS   A CE1 
1917 N  NE2 . HIS   A 94  ? 0.1327 0.1329 0.1562 -0.0162 -0.0090 0.0067  94  HIS   A NE2 
1925 N  N   . VAL   A 95  ? 0.1125 0.1218 0.1533 -0.0041 0.0091  0.0134  95  VAL   A N   
1926 C  CA  . VAL   A 95  ? 0.1256 0.1204 0.1512 -0.0088 0.0104  0.0112  95  VAL   A CA  
1927 C  C   . VAL   A 95  ? 0.1228 0.1221 0.1416 -0.0127 0.0059  0.0138  95  VAL   A C   
1928 O  O   . VAL   A 95  ? 0.1275 0.1326 0.1587 0.0054  0.0022  0.0066  95  VAL   A O   
1929 C  CB  . VAL   A 95  ? 0.1300 0.1253 0.1679 -0.0144 0.0074  0.0145  95  VAL   A CB  
1930 C  CG1 . VAL   A 95  ? 0.1471 0.1276 0.1854 -0.0206 0.0057  0.0022  95  VAL   A CG1 
1931 C  CG2 . VAL   A 95  ? 0.1384 0.1322 0.1662 -0.0103 0.0114  0.0268  95  VAL   A CG2 
1941 N  N   . VAL   A 96  ? 0.1261 0.1252 0.1390 -0.0036 0.0047  0.0140  96  VAL   A N   
1942 C  CA  . VAL   A 96  ? 0.1379 0.1256 0.1514 -0.0021 0.0107  0.0145  96  VAL   A CA  
1943 C  C   . VAL   A 96  ? 0.1413 0.1357 0.1556 -0.0064 0.0127  0.0117  96  VAL   A C   
1944 O  O   . VAL   A 96  ? 0.1494 0.1403 0.1793 -0.0071 0.0181  -0.0035 96  VAL   A O   
1945 C  CB  . VAL   A 96  ? 0.1389 0.1338 0.1643 -0.0029 0.0179  0.0135  96  VAL   A CB  
1946 C  CG1 . VAL   A 96  ? 0.1462 0.1410 0.1422 -0.0022 0.0109  0.0076  96  VAL   A CG1 
1947 C  CG2 . VAL   A 96  ? 0.1389 0.1399 0.1672 -0.0115 0.0183  0.0135  96  VAL   A CG2 
1957 N  N   A GLY   A 97  ? 0.1370 0.1349 0.1532 -0.0103 0.0094  0.0110  97  GLY   A N   
1958 N  N   B GLY   A 97  ? 0.1413 0.1418 0.1497 -0.0077 0.0055  0.0111  97  GLY   A N   
1959 C  CA  A GLY   A 97  ? 0.1451 0.1479 0.1636 -0.0092 0.0026  0.0124  97  GLY   A CA  
1960 C  CA  B GLY   A 97  ? 0.1470 0.1532 0.1514 -0.0071 -0.0018 0.0125  97  GLY   A CA  
1961 C  C   A GLY   A 97  ? 0.1440 0.1600 0.1614 -0.0134 0.0016  0.0087  97  GLY   A C   
1962 C  C   B GLY   A 97  ? 0.1478 0.1639 0.1478 -0.0089 -0.0071 0.0105  97  GLY   A C   
1963 O  O   A GLY   A 97  ? 0.1497 0.1600 0.1797 -0.0147 0.0070  0.0166  97  GLY   A O   
1964 O  O   B GLY   A 97  ? 0.1493 0.1665 0.1499 -0.0070 -0.0163 0.0157  97  GLY   A O   
1971 N  N   . PRO   A 98  ? 0.1508 0.1687 0.1487 -0.0064 -0.0019 0.0157  98  PRO   A N   
1972 C  CA  . PRO   A 98  ? 0.1664 0.1996 0.1600 -0.0143 -0.0009 0.0084  98  PRO   A CA  
1973 C  C   . PRO   A 98  ? 0.1742 0.2142 0.1490 -0.0276 -0.0098 0.0310  98  PRO   A C   
1974 O  O   . PRO   A 98  ? 0.1640 0.1841 0.1780 -0.0171 -0.0056 0.0266  98  PRO   A O   
1975 C  CB  . PRO   A 98  ? 0.1820 0.2108 0.1507 -0.0034 -0.0047 -0.0097 98  PRO   A CB  
1976 C  CG  . PRO   A 98  ? 0.1794 0.1963 0.1599 -0.0063 -0.0004 -0.0185 98  PRO   A CG  
1977 C  CD  . PRO   A 98  ? 0.1622 0.1730 0.1512 0.0025  -0.0028 -0.0012 98  PRO   A CD  
1985 N  N   A ASN   A 99  ? 0.1771 0.2465 0.1460 -0.0356 -0.0079 0.0481  99  ASN   A N   
1986 N  N   B ASN   A 99  ? 0.1991 0.2216 0.1499 -0.0293 -0.0169 0.0534  99  ASN   A N   
1987 C  CA  A ASN   A 99  ? 0.1945 0.2651 0.1312 -0.0372 -0.0101 0.0551  99  ASN   A CA  
1988 C  CA  B ASN   A 99  ? 0.2288 0.2206 0.1448 -0.0275 -0.0249 0.0687  99  ASN   A CA  
1989 C  C   A ASN   A 99  ? 0.2078 0.2866 0.1301 -0.0455 -0.0050 0.0505  99  ASN   A C   
1990 C  C   B ASN   A 99  ? 0.2451 0.2103 0.1503 -0.0227 -0.0219 0.0561  99  ASN   A C   
1991 O  O   A ASN   A 99  ? 0.2136 0.2947 0.1347 -0.0355 -0.0103 0.0399  99  ASN   A O   
1992 O  O   B ASN   A 99  ? 0.2471 0.1897 0.1451 -0.0154 -0.0283 0.0439  99  ASN   A O   
1993 C  CB  A ASN   A 99  ? 0.1934 0.2598 0.1167 -0.0345 -0.0192 0.0623  99  ASN   A CB  
1994 C  CB  B ASN   A 99  ? 0.2403 0.2292 0.1578 -0.0333 -0.0392 0.0824  99  ASN   A CB  
1995 C  CG  A ASN   A 99  ? 0.1938 0.2545 0.1137 -0.0302 -0.0288 0.0565  99  ASN   A CG  
1996 C  CG  B ASN   A 99  ? 0.2503 0.2347 0.1721 -0.0370 -0.0410 0.0970  99  ASN   A CG  
1997 O  OD1 A ASN   A 99  ? 0.2044 0.2599 0.1280 -0.0190 -0.0259 0.0509  99  ASN   A OD1 
1998 O  OD1 B ASN   A 99  ? 0.2582 0.2464 0.1656 -0.0387 -0.0373 0.0987  99  ASN   A OD1 
1999 N  ND2 A ASN   A 99  ? 0.1953 0.2500 0.1278 -0.0243 -0.0301 0.0717  99  ASN   A ND2 
2000 N  ND2 B ASN   A 99  ? 0.2541 0.2364 0.1908 -0.0279 -0.0531 0.0870  99  ASN   A ND2 
2013 N  N   A VAL   A 100 ? 0.2218 0.2950 0.1315 -0.0597 -0.0265 0.0487  100 VAL   A N   
2014 N  N   B VAL   A 100 ? 0.2585 0.2215 0.1671 -0.0172 -0.0240 0.0507  100 VAL   A N   
2015 C  CA  A VAL   A 100 ? 0.2467 0.3043 0.1584 -0.0632 -0.0366 0.0440  100 VAL   A CA  
2016 C  CA  B VAL   A 100 ? 0.2708 0.2285 0.1936 -0.0134 -0.0249 0.0378  100 VAL   A CA  
2017 C  C   A VAL   A 100 ? 0.2532 0.3084 0.1329 -0.0678 -0.0437 0.0597  100 VAL   A C   
2018 C  C   B VAL   A 100 ? 0.2721 0.2197 0.1889 -0.0038 -0.0354 0.0290  100 VAL   A C   
2019 O  O   A VAL   A 100 ? 0.2622 0.3120 0.1402 -0.0625 -0.0243 0.0578  100 VAL   A O   
2020 O  O   B VAL   A 100 ? 0.2724 0.2072 0.1906 -0.0040 -0.0378 0.0227  100 VAL   A O   
2021 C  CB  A VAL   A 100 ? 0.2647 0.3072 0.2068 -0.0641 -0.0433 0.0342  100 VAL   A CB  
2022 C  CB  B VAL   A 100 ? 0.2802 0.2460 0.2228 -0.0131 -0.0232 0.0258  100 VAL   A CB  
2023 C  CG1 A VAL   A 100 ? 0.2599 0.3078 0.2289 -0.0692 -0.0364 0.0340  100 VAL   A CG1 
2024 C  CG1 B VAL   A 100 ? 0.2799 0.2492 0.2378 -0.0146 -0.0210 0.0247  100 VAL   A CG1 
2025 C  CG2 A VAL   A 100 ? 0.2789 0.3102 0.2144 -0.0614 -0.0434 0.0314  100 VAL   A CG2 
2026 C  CG2 B VAL   A 100 ? 0.2838 0.2536 0.2289 -0.0126 -0.0213 0.0237  100 VAL   A CG2 
2045 N  N   A ASN   A 101 ? 0.2544 0.3159 0.1576 -0.0758 -0.0407 0.0795  101 ASN   A N   
2046 N  N   B ASN   A 101 ? 0.2743 0.2240 0.1915 0.0026  -0.0401 0.0262  101 ASN   A N   
2047 C  CA  A ASN   A 101 ? 0.2729 0.3234 0.1703 -0.0809 -0.0355 0.0994  101 ASN   A CA  
2048 C  CA  B ASN   A 101 ? 0.2826 0.2322 0.2075 0.0097  -0.0309 0.0215  101 ASN   A CA  
2049 C  C   A ASN   A 101 ? 0.3007 0.3537 0.1965 -0.0865 -0.0100 0.1199  101 ASN   A C   
2050 C  C   B ASN   A 101 ? 0.2994 0.2448 0.2231 0.0094  -0.0189 0.0350  101 ASN   A C   
2051 O  O   A ASN   A 101 ? 0.3149 0.3579 0.2457 -0.0871 -0.0138 0.1070  101 ASN   A O   
2052 O  O   B ASN   A 101 ? 0.3061 0.2469 0.2212 0.0083  -0.0191 0.0482  101 ASN   A O   
2053 C  CB  A ASN   A 101 ? 0.2681 0.3030 0.1743 -0.0777 -0.0506 0.0881  101 ASN   A CB  
2054 C  CB  B ASN   A 101 ? 0.2737 0.2304 0.2094 0.0114  -0.0292 0.0098  101 ASN   A CB  
2055 C  CG  A ASN   A 101 ? 0.2658 0.2847 0.1766 -0.0707 -0.0560 0.0636  101 ASN   A CG  
2056 C  CG  B ASN   A 101 ? 0.2691 0.2376 0.2222 0.0078  -0.0311 0.0039  101 ASN   A CG  
2057 O  OD1 A ASN   A 101 ? 0.2593 0.2830 0.1963 -0.0532 -0.0522 0.0366  101 ASN   A OD1 
2058 O  OD1 B ASN   A 101 ? 0.2756 0.2452 0.2350 0.0008  -0.0330 0.0069  101 ASN   A OD1 
2059 N  ND2 A ASN   A 101 ? 0.2704 0.2766 0.1829 -0.0728 -0.0554 0.0692  101 ASN   A ND2 
2060 N  ND2 B ASN   A 101 ? 0.2632 0.2373 0.2304 0.0131  -0.0284 -0.0058 101 ASN   A ND2 
2073 N  N   A LYS   A 102 ? 0.3085 0.3817 0.2310 -0.0915 0.0009  0.1158  102 LYS   A N   
2074 N  N   B LYS   A 102 ? 0.3098 0.2575 0.2442 0.0098  -0.0037 0.0335  102 LYS   A N   
2075 C  CA  A LYS   A 102 ? 0.3222 0.4066 0.2538 -0.0897 -0.0065 0.0992  102 LYS   A CA  
2076 C  CA  B LYS   A 102 ? 0.3207 0.2728 0.2507 0.0039  0.0121  0.0319  102 LYS   A CA  
2077 C  C   A LYS   A 102 ? 0.3333 0.4270 0.2596 -0.0783 -0.0030 0.0853  102 LYS   A C   
2078 C  C   B LYS   A 102 ? 0.3191 0.2734 0.2335 0.0046  0.0154  0.0420  102 LYS   A C   
2079 O  O   A LYS   A 102 ? 0.3360 0.4355 0.2606 -0.0733 0.0019  0.0790  102 LYS   A O   
2080 O  O   B LYS   A 102 ? 0.3201 0.2713 0.2295 0.0033  0.0196  0.0482  102 LYS   A O   
2081 C  CB  A LYS   A 102 ? 0.3318 0.4120 0.2928 -0.0942 -0.0210 0.0815  102 LYS   A CB  
2082 C  CB  B LYS   A 102 ? 0.3330 0.2855 0.2873 -0.0015 0.0166  0.0163  102 LYS   A CB  
2083 C  CG  A LYS   A 102 ? 0.3405 0.4153 0.3270 -0.0980 -0.0365 0.0570  102 LYS   A CG  
2084 C  CG  B LYS   A 102 ? 0.3435 0.2966 0.3260 -0.0060 0.0203  0.0037  102 LYS   A CG  
2085 C  CD  A LYS   A 102 ? 0.3534 0.4200 0.3668 -0.0982 -0.0490 0.0313  102 LYS   A CD  
2086 C  CD  B LYS   A 102 ? 0.3540 0.3101 0.3683 -0.0093 0.0244  -0.0079 102 LYS   A CD  
2087 C  CE  A LYS   A 102 ? 0.3642 0.4230 0.3995 -0.0981 -0.0563 0.0168  102 LYS   A CE  
2088 C  CE  B LYS   A 102 ? 0.3617 0.3201 0.4000 -0.0123 0.0249  -0.0158 102 LYS   A CE  
2089 N  NZ  A LYS   A 102 ? 0.3696 0.4245 0.4165 -0.1005 -0.0574 0.0065  102 LYS   A NZ  
2090 N  NZ  B LYS   A 102 ? 0.3665 0.3266 0.4234 -0.0135 0.0239  -0.0221 102 LYS   A NZ  
2117 N  N   A GLY   A 103 ? 0.3409 0.4397 0.2819 -0.0677 -0.0057 0.0652  103 GLY   A N   
2118 N  N   B GLY   A 103 ? 0.3146 0.2780 0.2223 0.0063  0.0073  0.0401  103 GLY   A N   
2119 C  CA  A GLY   A 103 ? 0.3492 0.4497 0.2924 -0.0559 -0.0000 0.0486  103 GLY   A CA  
2120 C  CA  B GLY   A 103 ? 0.3078 0.2783 0.2213 0.0057  -0.0016 0.0477  103 GLY   A CA  
2121 C  C   A GLY   A 103 ? 0.3521 0.4586 0.2966 -0.0477 0.0120  0.0392  103 GLY   A C   
2122 C  C   B GLY   A 103 ? 0.2973 0.2746 0.2074 0.0017  -0.0039 0.0559  103 GLY   A C   
2123 O  O   A GLY   A 103 ? 0.3603 0.4620 0.3121 -0.0455 0.0139  0.0370  103 GLY   A O   
2124 O  O   B GLY   A 103 ? 0.3024 0.2759 0.2085 -0.0009 -0.0091 0.0605  103 GLY   A O   
2131 N  N   A GLU   A 104 ? 0.3426 0.4607 0.2669 -0.0465 0.0282  0.0312  104 GLU   A N   
2132 N  N   B GLU   A 104 ? 0.2813 0.2682 0.1907 0.0010  -0.0094 0.0578  104 GLU   A N   
2133 C  CA  A GLU   A 104 ? 0.3298 0.4587 0.2450 -0.0497 0.0348  0.0231  104 GLU   A CA  
2134 C  CA  B GLU   A 104 ? 0.2655 0.2605 0.1708 -0.0055 -0.0165 0.0535  104 GLU   A CA  
2135 C  C   A GLU   A 104 ? 0.3360 0.4684 0.2408 -0.0463 0.0285  0.0007  104 GLU   A C   
2136 C  C   B GLU   A 104 ? 0.2629 0.2595 0.1792 0.0021  -0.0132 0.0313  104 GLU   A C   
2137 O  O   A GLU   A 104 ? 0.3337 0.4714 0.2357 -0.0466 0.0185  -0.0015 104 GLU   A O   
2138 O  O   B GLU   A 104 ? 0.2591 0.2495 0.1910 0.0050  -0.0109 0.0373  104 GLU   A O   
2139 C  CB  A GLU   A 104 ? 0.3067 0.4457 0.2301 -0.0564 0.0463  0.0412  104 GLU   A CB  
2140 C  CB  B GLU   A 104 ? 0.2541 0.2578 0.1704 -0.0162 -0.0229 0.0606  104 GLU   A CB  
2141 C  CG  A GLU   A 104 ? 0.2866 0.4321 0.2258 -0.0608 0.0498  0.0584  104 GLU   A CG  
2142 C  CG  B GLU   A 104 ? 0.2471 0.2638 0.1862 -0.0243 -0.0366 0.0612  104 GLU   A CG  
2143 C  CD  A GLU   A 104 ? 0.2695 0.4186 0.2203 -0.0645 0.0536  0.0753  104 GLU   A CD  
2144 C  CD  B GLU   A 104 ? 0.2318 0.2648 0.1849 -0.0344 -0.0486 0.0655  104 GLU   A CD  
2145 O  OE1 A GLU   A 104 ? 0.2535 0.4096 0.1935 -0.0673 0.0539  0.0857  104 GLU   A OE1 
2146 O  OE1 B GLU   A 104 ? 0.2200 0.2642 0.1740 -0.0393 -0.0649 0.0596  104 GLU   A OE1 
2147 O  OE2 A GLU   A 104 ? 0.2776 0.4155 0.2330 -0.0619 0.0512  0.0809  104 GLU   A OE2 
2148 O  OE2 B GLU   A 104 ? 0.2357 0.2646 0.1969 -0.0383 -0.0416 0.0698  104 GLU   A OE2 
2161 N  N   A ASP   A 105 ? 0.3430 0.4741 0.2547 -0.0409 0.0322  -0.0227 105 ASP   A N   
2162 N  N   B ASP   A 105 ? 0.2715 0.2696 0.1967 0.0009  -0.0106 0.0074  105 ASP   A N   
2163 C  CA  A ASP   A 105 ? 0.3431 0.4777 0.2825 -0.0378 0.0349  -0.0454 105 ASP   A CA  
2164 C  CA  B ASP   A 105 ? 0.2757 0.2798 0.2225 0.0035  -0.0029 -0.0261 105 ASP   A CA  
2165 C  C   A ASP   A 105 ? 0.3147 0.4653 0.2529 -0.0518 0.0267  -0.0656 105 ASP   A C   
2166 C  C   B ASP   A 105 ? 0.2711 0.2796 0.2044 -0.0098 -0.0017 -0.0422 105 ASP   A C   
2167 O  O   A ASP   A 105 ? 0.3052 0.4665 0.2172 -0.0542 0.0301  -0.0842 105 ASP   A O   
2168 O  O   B ASP   A 105 ? 0.2591 0.2726 0.1580 -0.0135 0.0002  -0.0532 105 ASP   A O   
2169 C  CB  A ASP   A 105 ? 0.3679 0.4909 0.3430 -0.0226 0.0411  -0.0472 105 ASP   A CB  
2170 C  CB  B ASP   A 105 ? 0.2845 0.2912 0.2728 0.0178  0.0034  -0.0400 105 ASP   A CB  
2171 C  CG  A ASP   A 105 ? 0.3881 0.5014 0.3960 -0.0104 0.0434  -0.0497 105 ASP   A CG  
2172 C  CG  B ASP   A 105 ? 0.2927 0.2995 0.3167 0.0313  0.0095  -0.0543 105 ASP   A CG  
2173 O  OD1 A ASP   A 105 ? 0.3929 0.5063 0.4085 -0.0074 0.0449  -0.0564 105 ASP   A OD1 
2174 O  OD1 B ASP   A 105 ? 0.2969 0.3002 0.3230 0.0319  0.0081  -0.0623 105 ASP   A OD1 
2175 O  OD2 A ASP   A 105 ? 0.3991 0.5052 0.4228 -0.0060 0.0457  -0.0449 105 ASP   A OD2 
2176 O  OD2 B ASP   A 105 ? 0.2958 0.3037 0.3422 0.0368  0.0100  -0.0549 105 ASP   A OD2 
2185 N  N   A ILE   A 106 ? 0.2937 0.4476 0.2641 -0.0660 0.0041  -0.0700 106 ILE   A N   
2186 N  N   B ILE   A 106 ? 0.2755 0.2884 0.2316 -0.0181 -0.0076 -0.0421 106 ILE   A N   
2187 C  CA  A ILE   A 106 ? 0.2648 0.4254 0.2754 -0.0832 -0.0148 -0.0791 106 ILE   A CA  
2188 C  CA  B ILE   A 106 ? 0.2775 0.2998 0.2600 -0.0338 -0.0128 -0.0447 106 ILE   A CA  
2189 C  C   A ILE   A 106 ? 0.2441 0.3952 0.2835 -0.1053 -0.0086 -0.0972 106 ILE   A C   
2190 C  C   B ILE   A 106 ? 0.2812 0.3035 0.2732 -0.0458 -0.0012 -0.0434 106 ILE   A C   
2191 O  O   A ILE   A 106 ? 0.2184 0.3852 0.2843 -0.1205 0.0048  -0.1026 106 ILE   A O   
2192 O  O   B ILE   A 106 ? 0.2781 0.3040 0.2745 -0.0488 0.0047  -0.0432 106 ILE   A O   
2193 C  CB  A ILE   A 106 ? 0.2674 0.4353 0.3111 -0.0693 -0.0263 -0.0537 106 ILE   A CB  
2194 C  CB  B ILE   A 106 ? 0.2810 0.3127 0.2898 -0.0336 -0.0236 -0.0362 106 ILE   A CB  
2195 C  CG1 A ILE   A 106 ? 0.2588 0.4373 0.3397 -0.0559 -0.0269 -0.0344 106 ILE   A CG1 
2196 C  CG1 B ILE   A 106 ? 0.2794 0.3207 0.3111 -0.0279 -0.0238 -0.0265 106 ILE   A CG1 
2197 C  CG2 A ILE   A 106 ? 0.2757 0.4393 0.3229 -0.0667 -0.0303 -0.0509 106 ILE   A CG2 
2198 C  CG2 B ILE   A 106 ? 0.2851 0.3158 0.2972 -0.0350 -0.0277 -0.0384 106 ILE   A CG2 
2199 C  CD1 A ILE   A 106 ? 0.2570 0.4365 0.3568 -0.0443 -0.0198 -0.0227 106 ILE   A CD1 
2200 C  CD1 B ILE   A 106 ? 0.2793 0.3233 0.3235 -0.0227 -0.0197 -0.0208 106 ILE   A CD1 
2223 N  N   A GLN   A 107 ? 0.2599 0.3758 0.3061 -0.0985 0.0082  -0.1064 107 GLN   A N   
2224 N  N   B GLN   A 107 ? 0.2880 0.3032 0.2922 -0.0515 0.0100  -0.0447 107 GLN   A N   
2225 C  CA  A GLN   A 107 ? 0.2810 0.3531 0.3611 -0.0829 0.0302  -0.1047 107 GLN   A CA  
2226 C  CA  B GLN   A 107 ? 0.2961 0.3060 0.3331 -0.0566 0.0223  -0.0462 107 GLN   A CA  
2227 C  C   A GLN   A 107 ? 0.2519 0.3026 0.3434 -0.0703 0.0605  -0.0856 107 GLN   A C   
2228 C  C   B GLN   A 107 ? 0.2644 0.2810 0.3185 -0.0627 0.0456  -0.0567 107 GLN   A C   
2229 O  O   A GLN   A 107 ? 0.2498 0.2955 0.3887 -0.0611 0.0835  -0.0879 107 GLN   A O   
2230 O  O   B GLN   A 107 ? 0.2680 0.2798 0.3429 -0.0677 0.0498  -0.0580 107 GLN   A O   
2231 C  CB  A GLN   A 107 ? 0.3220 0.3768 0.4397 -0.0848 0.0150  -0.1094 107 GLN   A CB  
2232 C  CB  B GLN   A 107 ? 0.3295 0.3317 0.3895 -0.0586 0.0080  -0.0358 107 GLN   A CB  
2233 C  CG  A GLN   A 107 ? 0.3626 0.4008 0.5248 -0.0829 -0.0000 -0.1014 107 GLN   A CG  
2234 C  CG  B GLN   A 107 ? 0.3585 0.3539 0.4479 -0.0589 -0.0064 -0.0217 107 GLN   A CG  
2235 C  CD  A GLN   A 107 ? 0.3930 0.4176 0.5972 -0.0809 -0.0095 -0.0901 107 GLN   A CD  
2236 C  CD  B GLN   A 107 ? 0.3830 0.3736 0.5000 -0.0568 -0.0163 -0.0072 107 GLN   A CD  
2237 O  OE1 A GLN   A 107 ? 0.4043 0.4241 0.6269 -0.0801 -0.0133 -0.0852 107 GLN   A OE1 
2238 O  OE1 B GLN   A 107 ? 0.3918 0.3819 0.5170 -0.0549 -0.0193 -0.0007 107 GLN   A OE1 
2239 N  NE2 A GLN   A 107 ? 0.4037 0.4226 0.6195 -0.0815 -0.0137 -0.0899 107 GLN   A NE2 
2240 N  NE2 B GLN   A 107 ? 0.3909 0.3793 0.5162 -0.0559 -0.0230 -0.0028 107 GLN   A NE2 
2257 N  N   . LEU   A 108 ? 0.2283 0.2557 0.2906 -0.0654 0.0527  -0.0700 108 LEU   A N   
2258 C  CA  . LEU   A 108 ? 0.1994 0.2002 0.2552 -0.0311 0.0482  -0.0316 108 LEU   A CA  
2259 C  C   . LEU   A 108 ? 0.1742 0.1478 0.2531 -0.0131 0.0402  -0.0014 108 LEU   A C   
2260 O  O   . LEU   A 108 ? 0.1685 0.1503 0.2709 -0.0056 0.0446  0.0046  108 LEU   A O   
2261 C  CB  . LEU   A 108 ? 0.2020 0.2117 0.2375 -0.0318 0.0538  -0.0262 108 LEU   A CB  
2262 C  CG  . LEU   A 108 ? 0.2166 0.2375 0.2576 -0.0262 0.0607  -0.0323 108 LEU   A CG  
2263 C  CD1 . LEU   A 108 ? 0.2360 0.2472 0.2642 -0.0326 0.0576  -0.0305 108 LEU   A CD1 
2264 C  CD2 . LEU   A 108 ? 0.2144 0.2576 0.3008 -0.0180 0.0573  -0.0270 108 LEU   A CD2 
2277 N  N   . LEU   A 109 ? 0.1561 0.1441 0.2429 0.0014  0.0315  0.0142  109 LEU   A N   
2278 C  CA  . LEU   A 109 ? 0.1536 0.1408 0.2182 0.0010  0.0153  0.0131  109 LEU   A CA  
2279 C  C   . LEU   A 109 ? 0.1411 0.1343 0.2107 -0.0114 0.0107  0.0062  109 LEU   A C   
2280 O  O   . LEU   A 109 ? 0.1545 0.1297 0.2333 -0.0069 0.0013  0.0040  109 LEU   A O   
2281 C  CB  . LEU   A 109 ? 0.1595 0.1489 0.2359 0.0114  0.0084  0.0290  109 LEU   A CB  
2282 C  CG  . LEU   A 109 ? 0.1485 0.1553 0.2491 0.0098  0.0118  0.0344  109 LEU   A CG  
2283 C  CD1 . LEU   A 109 ? 0.1587 0.1504 0.2615 0.0019  0.0238  0.0172  109 LEU   A CD1 
2284 C  CD2 . LEU   A 109 ? 0.1450 0.1768 0.2699 0.0052  0.0092  0.0380  109 LEU   A CD2 
2296 N  N   . LYS   A 110 ? 0.1433 0.1312 0.2074 -0.0047 0.0053  0.0039  110 LYS   A N   
2297 C  CA  . LYS   A 110 ? 0.1388 0.1292 0.2180 -0.0062 0.0017  0.0107  110 LYS   A CA  
2298 C  C   . LYS   A 110 ? 0.1362 0.1254 0.2095 -0.0089 0.0048  -0.0017 110 LYS   A C   
2299 O  O   . LYS   A 110 ? 0.1355 0.1278 0.2261 -0.0090 0.0095  -0.0079 110 LYS   A O   
2300 C  CB  . LYS   A 110 ? 0.1515 0.1393 0.2406 -0.0038 -0.0067 -0.0000 110 LYS   A CB  
2301 C  CG  . LYS   A 110 ? 0.1546 0.1324 0.2487 -0.0035 -0.0117 -0.0039 110 LYS   A CG  
2302 C  CD  . LYS   A 110 ? 0.1517 0.1411 0.2622 -0.0101 -0.0098 -0.0076 110 LYS   A CD  
2303 C  CE  . LYS   A 110 ? 0.1629 0.1437 0.2842 -0.0063 0.0029  -0.0091 110 LYS   A CE  
2304 N  NZ  . LYS   A 110 ? 0.1693 0.1489 0.2958 -0.0191 0.0083  -0.0024 110 LYS   A NZ  
2318 N  N   . SER   A 111 ? 0.1410 0.1254 0.2150 -0.0011 0.0069  -0.0015 111 SER   A N   
2319 C  CA  . SER   A 111 ? 0.1354 0.1388 0.2170 -0.0009 0.0128  0.0013  111 SER   A CA  
2320 C  C   . SER   A 111 ? 0.1297 0.1285 0.2172 -0.0075 0.0144  0.0066  111 SER   A C   
2321 O  O   . SER   A 111 ? 0.1406 0.1231 0.2346 -0.0044 0.0158  0.0043  111 SER   A O   
2322 C  CB  . SER   A 111 ? 0.1545 0.1534 0.2298 -0.0026 0.0236  -0.0091 111 SER   A CB  
2323 O  OG  . SER   A 111 ? 0.2003 0.1691 0.2344 0.0039  0.0226  -0.0190 111 SER   A OG  
2329 N  N   . ALA   A 112 ? 0.1415 0.1243 0.2191 -0.0077 0.0227  0.0077  112 ALA   A N   
2330 C  CA  . ALA   A 112 ? 0.1430 0.1216 0.2129 -0.0108 0.0221  0.0049  112 ALA   A CA  
2331 C  C   . ALA   A 112 ? 0.1326 0.1200 0.2191 -0.0070 0.0159  0.0052  112 ALA   A C   
2332 O  O   . ALA   A 112 ? 0.1366 0.1197 0.2327 -0.0125 0.0220  0.0074  112 ALA   A O   
2333 C  CB  . ALA   A 112 ? 0.1520 0.1256 0.2083 -0.0056 0.0182  0.0038  112 ALA   A CB  
2339 N  N   . TYR   A 113 ? 0.1256 0.1342 0.2201 -0.0060 0.0212  0.0149  113 TYR   A N   
2340 C  CA  . TYR   A 113 ? 0.1242 0.1247 0.2192 -0.0051 0.0159  0.0167  113 TYR   A CA  
2341 C  C   . TYR   A 113 ? 0.1242 0.1272 0.2167 -0.0091 0.0181  0.0124  113 TYR   A C   
2342 O  O   . TYR   A 113 ? 0.1315 0.1265 0.2248 -0.0084 0.0213  0.0070  113 TYR   A O   
2343 C  CB  . TYR   A 113 ? 0.1239 0.1330 0.2208 -0.0020 0.0029  0.0251  113 TYR   A CB  
2344 C  CG  . TYR   A 113 ? 0.1294 0.1325 0.2052 -0.0107 0.0149  0.0262  113 TYR   A CG  
2345 C  CD1 . TYR   A 113 ? 0.1315 0.1398 0.2028 -0.0022 0.0140  0.0300  113 TYR   A CD1 
2346 C  CD2 . TYR   A 113 ? 0.1317 0.1391 0.2059 -0.0119 0.0100  0.0272  113 TYR   A CD2 
2347 C  CE1 . TYR   A 113 ? 0.1347 0.1469 0.1998 -0.0050 0.0120  0.0289  113 TYR   A CE1 
2348 C  CE2 . TYR   A 113 ? 0.1338 0.1480 0.2040 -0.0140 0.0064  0.0246  113 TYR   A CE2 
2349 C  CZ  . TYR   A 113 ? 0.1304 0.1477 0.1938 -0.0006 0.0145  0.0318  113 TYR   A CZ  
2350 O  OH  . TYR   A 113 ? 0.1308 0.1563 0.2128 0.0080  0.0094  0.0344  113 TYR   A OH  
2360 N  N   . GLU   A 114 ? 0.1255 0.1239 0.2177 -0.0051 0.0172  0.0127  114 GLU   A N   
2361 C  CA  . GLU   A 114 ? 0.1304 0.1200 0.2243 0.0010  0.0111  0.0120  114 GLU   A CA  
2362 C  C   . GLU   A 114 ? 0.1268 0.1267 0.2181 -0.0034 0.0146  0.0116  114 GLU   A C   
2363 O  O   . GLU   A 114 ? 0.1372 0.1271 0.2174 -0.0054 0.0050  0.0125  114 GLU   A O   
2364 C  CB  . GLU   A 114 ? 0.1293 0.1217 0.2315 -0.0065 0.0060  0.0215  114 GLU   A CB  
2365 C  CG  . GLU   A 114 ? 0.1431 0.1231 0.2391 0.0001  0.0164  0.0122  114 GLU   A CG  
2366 C  CD  . GLU   A 114 ? 0.1482 0.1224 0.2466 -0.0014 0.0059  0.0104  114 GLU   A CD  
2367 O  OE1 . GLU   A 114 ? 0.1470 0.1278 0.2508 -0.0119 0.0152  -0.0011 114 GLU   A OE1 
2368 O  OE2 . GLU   A 114 ? 0.1677 0.1305 0.2661 -0.0097 0.0096  -0.0078 114 GLU   A OE2 
2375 N  N   . ASN   A 115 ? 0.1312 0.1297 0.2037 -0.0065 0.0184  0.0121  115 ASN   A N   
2376 C  CA  . ASN   A 115 ? 0.1327 0.1312 0.2189 -0.0107 0.0187  0.0128  115 ASN   A CA  
2377 C  C   . ASN   A 115 ? 0.1321 0.1294 0.2160 -0.0101 0.0133  0.0165  115 ASN   A C   
2378 O  O   . ASN   A 115 ? 0.1336 0.1450 0.2177 -0.0131 0.0190  0.0290  115 ASN   A O   
2379 C  CB  . ASN   A 115 ? 0.1447 0.1371 0.2150 -0.0134 0.0194  0.0130  115 ASN   A CB  
2380 C  CG  . ASN   A 115 ? 0.1390 0.1548 0.2169 -0.0210 0.0239  0.0060  115 ASN   A CG  
2381 O  OD1 . ASN   A 115 ? 0.1431 0.2484 0.2379 -0.0167 0.0270  0.0229  115 ASN   A OD1 
2382 N  ND2 . ASN   A 115 ? 0.1442 0.1344 0.2101 -0.0154 0.0286  0.0145  115 ASN   A ND2 
2389 N  N   . PHE   A 116 ? 0.1294 0.1299 0.2229 -0.0042 0.0180  0.0238  116 PHE   A N   
2390 C  CA  . PHE   A 116 ? 0.1284 0.1424 0.2082 -0.0064 0.0161  0.0157  116 PHE   A CA  
2391 C  C   . PHE   A 116 ? 0.1254 0.1454 0.2073 -0.0122 0.0144  0.0220  116 PHE   A C   
2392 O  O   . PHE   A 116 ? 0.1361 0.1512 0.2189 -0.0020 0.0150  0.0366  116 PHE   A O   
2393 C  CB  . PHE   A 116 ? 0.1346 0.1308 0.2221 -0.0047 0.0239  0.0156  116 PHE   A CB  
2394 C  CG  . PHE   A 116 ? 0.1352 0.1276 0.2050 -0.0094 0.0161  0.0134  116 PHE   A CG  
2395 C  CD1 . PHE   A 116 ? 0.1360 0.1283 0.2039 -0.0082 0.0188  0.0145  116 PHE   A CD1 
2396 C  CD2 . PHE   A 116 ? 0.1433 0.1342 0.2144 -0.0078 0.0284  0.0191  116 PHE   A CD2 
2397 C  CE1 . PHE   A 116 ? 0.1391 0.1269 0.2129 -0.0240 0.0113  0.0091  116 PHE   A CE1 
2398 C  CE2 . PHE   A 116 ? 0.1401 0.1323 0.2162 -0.0091 0.0213  0.0152  116 PHE   A CE2 
2399 C  CZ  . PHE   A 116 ? 0.1433 0.1171 0.2030 -0.0073 0.0056  0.0115  116 PHE   A CZ  
2409 N  N   . ASN   A 117 ? 0.1302 0.1381 0.2264 -0.0122 0.0177  0.0279  117 ASN   A N   
2410 C  CA  . ASN   A 117 ? 0.1307 0.1322 0.2360 -0.0065 0.0157  0.0353  117 ASN   A CA  
2411 C  C   . ASN   A 117 ? 0.1365 0.1435 0.2485 -0.0067 0.0192  0.0317  117 ASN   A C   
2412 O  O   . ASN   A 117 ? 0.1420 0.1497 0.2758 -0.0086 -0.0017 0.0494  117 ASN   A O   
2413 C  CB  . ASN   A 117 ? 0.1301 0.1394 0.2348 -0.0046 0.0181  0.0327  117 ASN   A CB  
2414 C  CG  . ASN   A 117 ? 0.1309 0.1386 0.2390 -0.0066 0.0195  0.0337  117 ASN   A CG  
2415 O  OD1 . ASN   A 117 ? 0.1314 0.1573 0.2504 -0.0140 0.0197  0.0275  117 ASN   A OD1 
2416 N  ND2 . ASN   A 117 ? 0.1245 0.1367 0.2374 -0.0027 0.0158  0.0215  117 ASN   A ND2 
2423 N  N   . GLN   A 118 ? 0.1304 0.1439 0.2373 -0.0111 0.0072  0.0363  118 GLN   A N   
2424 C  CA  . GLN   A 118 ? 0.1359 0.1606 0.2393 -0.0116 -0.0005 0.0322  118 GLN   A CA  
2425 C  C   . GLN   A 118 ? 0.1424 0.1662 0.2295 -0.0115 -0.0015 0.0383  118 GLN   A C   
2426 O  O   . GLN   A 118 ? 0.1382 0.1948 0.2588 -0.0068 -0.0087 0.0209  118 GLN   A O   
2427 C  CB  . GLN   A 118 ? 0.1359 0.1605 0.2589 -0.0050 0.0164  0.0365  118 GLN   A CB  
2428 C  CG  . GLN   A 118 ? 0.1342 0.1612 0.2542 -0.0018 0.0145  0.0371  118 GLN   A CG  
2429 C  CD  . GLN   A 118 ? 0.1319 0.1621 0.2627 -0.0015 0.0168  0.0265  118 GLN   A CD  
2430 O  OE1 . GLN   A 118 ? 0.1325 0.1791 0.2766 0.0037  0.0056  0.0195  118 GLN   A OE1 
2431 N  NE2 . GLN   A 118 ? 0.1401 0.1532 0.2581 0.0021  0.0117  0.0294  118 GLN   A NE2 
2440 N  N   . HIS   A 119 ? 0.1457 0.1648 0.2159 -0.0043 0.0051  0.0415  119 HIS   A N   
2441 C  CA  . HIS   A 119 ? 0.1518 0.1745 0.2192 -0.0089 0.0028  0.0504  119 HIS   A CA  
2442 C  C   . HIS   A 119 ? 0.1600 0.1837 0.2172 -0.0139 0.0059  0.0463  119 HIS   A C   
2443 O  O   . HIS   A 119 ? 0.1609 0.1871 0.2265 -0.0277 -0.0008 0.0489  119 HIS   A O   
2444 C  CB  . HIS   A 119 ? 0.1561 0.1711 0.2377 -0.0058 0.0235  0.0484  119 HIS   A CB  
2445 C  CG  . HIS   A 119 ? 0.1543 0.1774 0.2759 -0.0011 0.0199  0.0490  119 HIS   A CG  
2446 N  ND1 . HIS   A 119 ? 0.1675 0.1991 0.3304 -0.0141 0.0120  0.0398  119 HIS   A ND1 
2447 C  CD2 . HIS   A 119 ? 0.1676 0.1801 0.2949 0.0128  0.0388  0.0606  119 HIS   A CD2 
2448 C  CE1 . HIS   A 119 ? 0.1646 0.1939 0.3358 -0.0227 0.0321  0.0624  119 HIS   A CE1 
2449 N  NE2 . HIS   A 119 ? 0.1785 0.1861 0.3233 -0.0014 0.0498  0.0687  119 HIS   A NE2 
2457 N  N   . GLU   A 120 ? 0.1669 0.2122 0.2264 -0.0145 -0.0037 0.0721  120 GLU   A N   
2458 C  CA  . GLU   A 120 ? 0.1943 0.2450 0.2536 -0.0071 -0.0052 0.1177  120 GLU   A CA  
2459 C  C   . GLU   A 120 ? 0.1695 0.2316 0.2271 -0.0179 0.0006  0.1065  120 GLU   A C   
2460 O  O   . GLU   A 120 ? 0.1699 0.2253 0.2353 -0.0189 0.0010  0.1022  120 GLU   A O   
2461 C  CB  . GLU   A 120 ? 0.2711 0.3119 0.3121 0.0084  -0.0047 0.1576  120 GLU   A CB  
2462 C  CG  . GLU   A 120 ? 0.3634 0.3792 0.4235 0.0179  -0.0037 0.1582  120 GLU   A CG  
2463 C  CD  . GLU   A 120 ? 0.4428 0.4369 0.5356 0.0277  0.0035  0.1434  120 GLU   A CD  
2464 O  OE1 . GLU   A 120 ? 0.4728 0.4613 0.5624 0.0308  0.0066  0.1366  120 GLU   A OE1 
2465 O  OE2 . GLU   A 120 ? 0.4739 0.4739 0.5870 0.0297  0.0066  0.1356  120 GLU   A OE2 
2472 N  N   . VAL   A 121 ? 0.1647 0.2314 0.1958 -0.0197 0.0091  0.0870  121 VAL   A N   
2473 C  CA  . VAL   A 121 ? 0.1727 0.2362 0.1820 -0.0257 0.0149  0.0734  121 VAL   A CA  
2474 C  C   . VAL   A 121 ? 0.1624 0.2146 0.1711 -0.0337 0.0059  0.0549  121 VAL   A C   
2475 O  O   . VAL   A 121 ? 0.1688 0.2174 0.1935 -0.0372 -0.0091 0.0534  121 VAL   A O   
2476 C  CB  . VAL   A 121 ? 0.2115 0.2720 0.2184 -0.0103 0.0260  0.0749  121 VAL   A CB  
2477 C  CG1 . VAL   A 121 ? 0.2129 0.2857 0.2214 -0.0070 0.0370  0.0783  121 VAL   A CG1 
2478 C  CG2 . VAL   A 121 ? 0.2350 0.2860 0.2552 -0.0141 0.0234  0.0652  121 VAL   A CG2 
2488 N  N   . LEU   A 122 ? 0.1537 0.1836 0.1778 -0.0288 0.0054  0.0483  122 LEU   A N   
2489 C  CA  . LEU   A 122 ? 0.1630 0.1675 0.1828 -0.0278 0.0213  0.0468  122 LEU   A CA  
2490 C  C   . LEU   A 122 ? 0.1560 0.1684 0.1848 -0.0327 0.0037  0.0402  122 LEU   A C   
2491 O  O   . LEU   A 122 ? 0.1570 0.1779 0.2141 -0.0361 0.0050  0.0485  122 LEU   A O   
2492 C  CB  . LEU   A 122 ? 0.1824 0.1671 0.2108 -0.0143 0.0115  0.0553  122 LEU   A CB  
2493 C  CG  . LEU   A 122 ? 0.1813 0.1744 0.2084 -0.0122 0.0242  0.0434  122 LEU   A CG  
2494 C  CD1 . LEU   A 122 ? 0.1996 0.1737 0.2185 -0.0178 0.0186  0.0402  122 LEU   A CD1 
2495 C  CD2 . LEU   A 122 ? 0.1736 0.1653 0.2038 -0.0107 0.0298  0.0381  122 LEU   A CD2 
2507 N  N   A LEU   A 123 ? 0.1482 0.1673 0.1799 -0.0333 0.0072  0.0378  123 LEU   A N   
2508 N  N   B LEU   A 123 ? 0.1531 0.1630 0.1728 -0.0269 0.0031  0.0348  123 LEU   A N   
2509 C  CA  A LEU   A 123 ? 0.1470 0.1667 0.1655 -0.0338 0.0093  0.0372  123 LEU   A CA  
2510 C  CA  B LEU   A 123 ? 0.1532 0.1586 0.1616 -0.0207 0.0006  0.0305  123 LEU   A CA  
2511 C  C   A LEU   A 123 ? 0.1418 0.1501 0.1650 -0.0268 0.0097  0.0337  123 LEU   A C   
2512 C  C   B LEU   A 123 ? 0.1516 0.1485 0.1500 -0.0111 0.0021  0.0265  123 LEU   A C   
2513 O  O   A LEU   A 123 ? 0.1259 0.1442 0.1658 -0.0282 0.0144  0.0291  123 LEU   A O   
2514 O  O   B LEU   A 123 ? 0.1473 0.1473 0.1541 -0.0032 0.0106  0.0155  123 LEU   A O   
2515 C  CB  A LEU   A 123 ? 0.1605 0.1847 0.1608 -0.0361 0.0206  0.0383  123 LEU   A CB  
2516 C  CB  B LEU   A 123 ? 0.1597 0.1657 0.1692 -0.0234 0.0001  0.0328  123 LEU   A CB  
2517 C  CG  A LEU   A 123 ? 0.1673 0.2010 0.1691 -0.0282 0.0173  0.0132  123 LEU   A CG  
2518 C  CG  B LEU   A 123 ? 0.1621 0.1735 0.1674 -0.0226 0.0013  0.0278  123 LEU   A CG  
2519 C  CD1 A LEU   A 123 ? 0.1697 0.2061 0.1766 -0.0206 0.0203  0.0039  123 LEU   A CD1 
2520 C  CD1 B LEU   A 123 ? 0.1660 0.1768 0.1713 -0.0176 0.0041  0.0229  123 LEU   A CD1 
2521 C  CD2 A LEU   A 123 ? 0.1759 0.2066 0.1711 -0.0303 0.0055  0.0098  123 LEU   A CD2 
2522 C  CD2 B LEU   A 123 ? 0.1661 0.1769 0.1686 -0.0232 -0.0041 0.0308  123 LEU   A CD2 
2545 N  N   A ALA   A 124 ? 0.1347 0.1324 0.1645 -0.0196 0.0201  0.0337  124 ALA   A N   
2546 N  N   B ALA   A 124 ? 0.1485 0.1338 0.1526 -0.0116 0.0014  0.0242  124 ALA   A N   
2547 C  CA  A ALA   A 124 ? 0.1254 0.1272 0.1609 -0.0071 0.0097  0.0270  124 ALA   A CA  
2548 C  CA  B ALA   A 124 ? 0.1481 0.1401 0.1676 -0.0171 -0.0023 0.0237  124 ALA   A CA  
2549 C  C   A ALA   A 124 ? 0.1204 0.1340 0.1652 -0.0094 0.0130  0.0324  124 ALA   A C   
2550 C  C   B ALA   A 124 ? 0.1434 0.1399 0.1677 -0.0135 -0.0009 0.0300  124 ALA   A C   
2551 O  O   A ALA   A 124 ? 0.1201 0.1452 0.1923 -0.0108 0.0290  0.0353  124 ALA   A O   
2552 O  O   B ALA   A 124 ? 0.1400 0.1440 0.1841 -0.0052 -0.0014 0.0387  124 ALA   A O   
2553 C  CB  A ALA   A 124 ? 0.1272 0.1191 0.1853 -0.0037 0.0079  0.0261  124 ALA   A CB  
2554 C  CB  B ALA   A 124 ? 0.1578 0.1420 0.1872 -0.0201 0.0013  0.0214  124 ALA   A CB  
2565 N  N   A PRO   A 125 ? 0.1152 0.1382 0.1738 -0.0091 0.0110  0.0348  125 PRO   A N   
2566 N  N   B PRO   A 125 ? 0.1326 0.1345 0.1460 -0.0100 -0.0036 0.0395  125 PRO   A N   
2567 C  CA  A PRO   A 125 ? 0.1227 0.1418 0.1850 -0.0122 0.0028  0.0254  125 PRO   A CA  
2568 C  CA  B PRO   A 125 ? 0.1367 0.1383 0.1546 -0.0100 0.0024  0.0330  125 PRO   A CA  
2569 C  C   A PRO   A 125 ? 0.1145 0.1391 0.1783 -0.0120 0.0098  0.0294  125 PRO   A C   
2570 C  C   B PRO   A 125 ? 0.1511 0.1502 0.1589 -0.0065 0.0044  0.0260  125 PRO   A C   
2571 O  O   A PRO   A 125 ? 0.1199 0.1400 0.1809 -0.0078 0.0034  0.0292  125 PRO   A O   
2572 O  O   B PRO   A 125 ? 0.1551 0.1522 0.1548 -0.0081 0.0141  0.0242  125 PRO   A O   
2573 C  CB  A PRO   A 125 ? 0.1338 0.1446 0.1829 -0.0165 0.0015  0.0190  125 PRO   A CB  
2574 C  CB  B PRO   A 125 ? 0.1254 0.1291 0.1458 -0.0120 -0.0028 0.0408  125 PRO   A CB  
2575 C  CG  A PRO   A 125 ? 0.1416 0.1427 0.1853 -0.0135 0.0085  0.0307  125 PRO   A CG  
2576 C  CG  B PRO   A 125 ? 0.1157 0.1205 0.1465 -0.0045 -0.0022 0.0380  125 PRO   A CG  
2577 C  CD  A PRO   A 125 ? 0.1228 0.1434 0.1810 -0.0091 0.0139  0.0261  125 PRO   A CD  
2578 C  CD  B PRO   A 125 ? 0.1176 0.1153 0.1435 -0.0053 0.0008  0.0373  125 PRO   A CD  
2593 N  N   A LEU   A 126 ? 0.1070 0.1391 0.1717 -0.0038 0.0187  0.0279  126 LEU   A N   
2594 N  N   B LEU   A 126 ? 0.1610 0.1593 0.1718 -0.0018 -0.0063 0.0196  126 LEU   A N   
2595 C  CA  A LEU   A 126 ? 0.1175 0.1400 0.1788 -0.0026 0.0123  0.0248  126 LEU   A CA  
2596 C  CA  B LEU   A 126 ? 0.1640 0.1630 0.1892 0.0025  -0.0057 0.0116  126 LEU   A CA  
2597 C  C   A LEU   A 126 ? 0.1277 0.1403 0.1772 0.0003  0.0043  0.0291  126 LEU   A C   
2598 C  C   B LEU   A 126 ? 0.1538 0.1468 0.1750 0.0109  -0.0048 0.0005  126 LEU   A C   
2599 O  O   A LEU   A 126 ? 0.1385 0.1442 0.2002 0.0089  0.0184  0.0440  126 LEU   A O   
2600 O  O   B LEU   A 126 ? 0.1587 0.1418 0.1925 0.0049  -0.0168 0.0032  126 LEU   A O   
2601 C  CB  A LEU   A 126 ? 0.1212 0.1479 0.1797 -0.0081 0.0107  0.0197  126 LEU   A CB  
2602 C  CB  B LEU   A 126 ? 0.1799 0.1896 0.2278 -0.0073 -0.0090 0.0097  126 LEU   A CB  
2603 C  CG  A LEU   A 126 ? 0.1181 0.1710 0.1857 -0.0155 0.0149  0.0241  126 LEU   A CG  
2604 C  CG  B LEU   A 126 ? 0.1911 0.2062 0.2562 -0.0156 -0.0153 0.0135  126 LEU   A CG  
2605 C  CD1 A LEU   A 126 ? 0.1260 0.1883 0.2017 -0.0171 0.0079  0.0232  126 LEU   A CD1 
2606 C  CD1 B LEU   A 126 ? 0.1941 0.2104 0.2645 -0.0178 -0.0159 0.0130  126 LEU   A CD1 
2607 C  CD2 A LEU   A 126 ? 0.1333 0.1612 0.1826 -0.0238 0.0105  0.0430  126 LEU   A CD2 
2608 C  CD2 B LEU   A 126 ? 0.1938 0.2071 0.2575 -0.0237 -0.0197 0.0155  126 LEU   A CD2 
2631 N  N   A LEU   A 127 ? 0.1313 0.1361 0.1557 0.0000  0.0131  0.0209  127 LEU   A N   
2632 N  N   B LEU   A 127 ? 0.1502 0.1467 0.1579 0.0150  0.0064  0.0058  127 LEU   A N   
2633 C  CA  A LEU   A 127 ? 0.1347 0.1403 0.1536 -0.0001 0.0002  0.0121  127 LEU   A CA  
2634 C  CA  B LEU   A 127 ? 0.1475 0.1502 0.1496 0.0150  0.0055  0.0130  127 LEU   A CA  
2635 C  C   A LEU   A 127 ? 0.1329 0.1255 0.1544 0.0010  -0.0036 0.0074  127 LEU   A C   
2636 C  C   B LEU   A 127 ? 0.1514 0.1493 0.1428 0.0107  0.0050  0.0065  127 LEU   A C   
2637 O  O   A LEU   A 127 ? 0.1389 0.1182 0.1578 -0.0178 -0.0014 0.0152  127 LEU   A O   
2638 O  O   B LEU   A 127 ? 0.1592 0.1552 0.1456 0.0079  0.0115  0.0012  127 LEU   A O   
2639 C  CB  A LEU   A 127 ? 0.1434 0.1487 0.1654 0.0143  0.0055  0.0122  127 LEU   A CB  
2640 C  CB  B LEU   A 127 ? 0.1436 0.1616 0.1536 0.0135  0.0044  0.0170  127 LEU   A CB  
2641 C  CG  A LEU   A 127 ? 0.1450 0.1433 0.1773 0.0105  -0.0009 0.0193  127 LEU   A CG  
2642 C  CG  B LEU   A 127 ? 0.1376 0.1688 0.1512 0.0119  -0.0033 0.0242  127 LEU   A CG  
2643 C  CD1 A LEU   A 127 ? 0.1522 0.1388 0.1947 0.0039  -0.0019 0.0138  127 LEU   A CD1 
2644 C  CD1 B LEU   A 127 ? 0.1352 0.1700 0.1621 0.0171  0.0044  0.0282  127 LEU   A CD1 
2645 C  CD2 A LEU   A 127 ? 0.1605 0.1388 0.1928 0.0170  -0.0149 0.0168  127 LEU   A CD2 
2646 C  CD2 B LEU   A 127 ? 0.1448 0.1779 0.1526 0.0072  -0.0160 0.0191  127 LEU   A CD2 
2669 N  N   A SER   A 128 ? 0.1347 0.1302 0.1556 -0.0056 -0.0045 0.0098  128 SER   A N   
2670 N  N   B SER   A 128 ? 0.1448 0.1462 0.1340 0.0016  -0.0011 0.0109  128 SER   A N   
2671 C  CA  A SER   A 128 ? 0.1505 0.1380 0.1519 -0.0077 0.0054  0.0059  128 SER   A CA  
2672 C  CA  B SER   A 128 ? 0.1488 0.1447 0.1349 -0.0023 -0.0157 0.0149  128 SER   A CA  
2673 C  C   A SER   A 128 ? 0.1591 0.1431 0.1571 -0.0032 0.0004  0.0178  128 SER   A C   
2674 C  C   B SER   A 128 ? 0.1515 0.1397 0.1340 -0.0028 -0.0226 0.0251  128 SER   A C   
2675 O  O   A SER   A 128 ? 0.1735 0.1582 0.1752 0.0043  0.0042  0.0106  128 SER   A O   
2676 O  O   B SER   A 128 ? 0.1544 0.1427 0.1443 -0.0053 -0.0212 0.0266  128 SER   A O   
2677 C  CB  A SER   A 128 ? 0.1549 0.1503 0.1581 -0.0107 0.0093  0.0124  128 SER   A CB  
2678 C  CB  B SER   A 128 ? 0.1458 0.1475 0.1300 -0.0061 -0.0219 0.0109  128 SER   A CB  
2679 O  OG  A SER   A 128 ? 0.1581 0.1613 0.1695 -0.0095 0.0212  0.0130  128 SER   A OG  
2680 O  OG  B SER   A 128 ? 0.1433 0.1489 0.1409 -0.0058 -0.0179 0.0020  128 SER   A OG  
2691 N  N   A ALA   A 129 ? 0.1511 0.1519 0.1821 -0.0037 -0.0019 0.0277  129 ALA   A N   
2692 N  N   B ALA   A 129 ? 0.1513 0.1459 0.1492 0.0003  -0.0253 0.0204  129 ALA   A N   
2693 C  CA  A ALA   A 129 ? 0.1378 0.1557 0.1933 0.0005  -0.0046 0.0393  129 ALA   A CA  
2694 C  CA  B ALA   A 129 ? 0.1518 0.1521 0.1582 0.0032  -0.0261 0.0158  129 ALA   A CA  
2695 C  C   A ALA   A 129 ? 0.1386 0.1516 0.1777 -0.0041 -0.0167 0.0240  129 ALA   A C   
2696 C  C   B ALA   A 129 ? 0.1624 0.1575 0.1478 0.0084  -0.0233 0.0084  129 ALA   A C   
2697 O  O   A ALA   A 129 ? 0.1449 0.1544 0.1851 -0.0139 -0.0121 0.0324  129 ALA   A O   
2698 O  O   B ALA   A 129 ? 0.1687 0.1651 0.1499 0.0031  -0.0201 0.0163  129 ALA   A O   
2699 C  CB  A ALA   A 129 ? 0.1384 0.1719 0.2121 0.0072  0.0001  0.0551  129 ALA   A CB  
2700 C  CB  B ALA   A 129 ? 0.1491 0.1616 0.1742 -0.0049 -0.0285 0.0152  129 ALA   A CB  
2711 N  N   A GLY   A 130 ? 0.1405 0.1480 0.1831 -0.0048 -0.0187 0.0156  130 GLY   A N   
2712 N  N   B GLY   A 130 ? 0.1676 0.1561 0.1407 0.0090  -0.0280 0.0086  130 GLY   A N   
2713 C  CA  A GLY   A 130 ? 0.1604 0.1470 0.1772 -0.0079 -0.0205 0.0136  130 GLY   A CA  
2714 C  CA  B GLY   A 130 ? 0.1794 0.1560 0.1436 0.0109  -0.0248 0.0083  130 GLY   A CA  
2715 C  C   A GLY   A 130 ? 0.1780 0.1481 0.1753 -0.0100 -0.0163 0.0133  130 GLY   A C   
2716 C  C   B GLY   A 130 ? 0.1909 0.1573 0.1530 0.0150  -0.0223 0.0072  130 GLY   A C   
2717 O  O   A GLY   A 130 ? 0.1725 0.1439 0.1702 -0.0165 -0.0111 0.0163  130 GLY   A O   
2718 O  O   B GLY   A 130 ? 0.1937 0.1599 0.1628 0.0171  -0.0229 0.0131  130 GLY   A O   
2725 N  N   A ILE   A 131 ? 0.1951 0.1456 0.1818 -0.0175 -0.0260 0.0199  131 ILE   A N   
2726 N  N   B ILE   A 131 ? 0.1977 0.1539 0.1666 0.0111  -0.0177 0.0079  131 ILE   A N   
2727 C  CA  A ILE   A 131 ? 0.2129 0.1439 0.1642 -0.0243 -0.0378 0.0157  131 ILE   A CA  
2728 C  CA  B ILE   A 131 ? 0.2056 0.1513 0.1658 0.0027  -0.0278 0.0092  131 ILE   A CA  
2729 C  C   A ILE   A 131 ? 0.1947 0.1483 0.1637 -0.0220 -0.0276 0.0324  131 ILE   A C   
2730 C  C   B ILE   A 131 ? 0.1925 0.1548 0.1611 0.0003  -0.0246 0.0142  131 ILE   A C   
2731 O  O   A ILE   A 131 ? 0.1975 0.1581 0.1837 -0.0124 -0.0225 0.0378  131 ILE   A O   
2732 O  O   B ILE   A 131 ? 0.1877 0.1530 0.1736 0.0037  -0.0276 0.0221  131 ILE   A O   
2733 C  CB  A ILE   A 131 ? 0.2421 0.1553 0.1604 -0.0332 -0.0475 0.0104  131 ILE   A CB  
2734 C  CB  B ILE   A 131 ? 0.2241 0.1585 0.1798 -0.0061 -0.0453 0.0067  131 ILE   A CB  
2735 C  CG1 A ILE   A 131 ? 0.2482 0.1820 0.1772 -0.0415 -0.0466 0.0198  131 ILE   A CG1 
2736 C  CG1 B ILE   A 131 ? 0.2310 0.1737 0.1944 -0.0099 -0.0546 0.0114  131 ILE   A CG1 
2737 C  CG2 A ILE   A 131 ? 0.2602 0.1463 0.1631 -0.0233 -0.0379 -0.0019 131 ILE   A CG2 
2738 C  CG2 B ILE   A 131 ? 0.2294 0.1573 0.1884 -0.0050 -0.0515 -0.0029 131 ILE   A CG2 
2739 C  CD1 A ILE   A 131 ? 0.2480 0.1895 0.2009 -0.0448 -0.0527 0.0151  131 ILE   A CD1 
2740 C  CD1 B ILE   A 131 ? 0.2357 0.1783 0.2036 -0.0113 -0.0560 0.0111  131 ILE   A CD1 
2763 N  N   A PHE   A 132 ? 0.1809 0.1447 0.1650 -0.0156 -0.0185 0.0329  132 PHE   A N   
2764 N  N   B PHE   A 132 ? 0.1888 0.1597 0.1654 -0.0001 -0.0150 0.0167  132 PHE   A N   
2765 C  CA  A PHE   A 132 ? 0.1842 0.1501 0.1623 -0.0166 -0.0178 0.0238  132 PHE   A CA  
2766 C  CA  B PHE   A 132 ? 0.1936 0.1666 0.1598 -0.0038 -0.0120 0.0130  132 PHE   A CA  
2767 C  C   A PHE   A 132 ? 0.1928 0.1614 0.1593 -0.0229 -0.0195 0.0226  132 PHE   A C   
2768 C  C   B PHE   A 132 ? 0.2003 0.1775 0.1629 -0.0089 -0.0160 0.0167  132 PHE   A C   
2769 O  O   A PHE   A 132 ? 0.2034 0.1627 0.1617 -0.0242 -0.0134 0.0231  132 PHE   A O   
2770 O  O   B PHE   A 132 ? 0.2066 0.1782 0.1617 -0.0138 -0.0150 0.0150  132 PHE   A O   
2771 C  CB  A PHE   A 132 ? 0.1739 0.1440 0.1671 -0.0121 -0.0188 0.0297  132 PHE   A CB  
2772 C  CB  B PHE   A 132 ? 0.1895 0.1614 0.1519 -0.0014 -0.0063 0.0055  132 PHE   A CB  
2773 C  CG  A PHE   A 132 ? 0.1691 0.1444 0.1648 -0.0042 -0.0222 0.0248  132 PHE   A CG  
2774 C  CG  B PHE   A 132 ? 0.1862 0.1634 0.1479 0.0036  -0.0021 -0.0054 132 PHE   A CG  
2775 C  CD1 A PHE   A 132 ? 0.1657 0.1644 0.1773 0.0080  -0.0217 0.0027  132 PHE   A CD1 
2776 C  CD1 B PHE   A 132 ? 0.1867 0.1744 0.1573 0.0087  -0.0010 -0.0151 132 PHE   A CD1 
2777 C  CD2 A PHE   A 132 ? 0.1713 0.1555 0.1737 0.0013  -0.0287 0.0198  132 PHE   A CD2 
2778 C  CD2 B PHE   A 132 ? 0.1858 0.1644 0.1475 0.0108  0.0016  -0.0161 132 PHE   A CD2 
2779 C  CE1 A PHE   A 132 ? 0.1691 0.1670 0.1880 0.0019  -0.0294 0.0025  132 PHE   A CE1 
2780 C  CE1 B PHE   A 132 ? 0.1873 0.1772 0.1654 0.0081  0.0025  -0.0171 132 PHE   A CE1 
2781 C  CE2 A PHE   A 132 ? 0.1671 0.1553 0.1904 0.0047  -0.0322 0.0217  132 PHE   A CE2 
2782 C  CE2 B PHE   A 132 ? 0.1832 0.1692 0.1621 0.0192  0.0063  -0.0204 132 PHE   A CE2 
2783 C  CZ  A PHE   A 132 ? 0.1636 0.1602 0.1867 -0.0037 -0.0369 0.0168  132 PHE   A CZ  
2784 C  CZ  B PHE   A 132 ? 0.1833 0.1729 0.1639 0.0103  0.0071  -0.0194 132 PHE   A CZ  
2803 N  N   A GLY   A 133 ? 0.1947 0.1730 0.1606 -0.0212 -0.0322 0.0238  133 GLY   A N   
2804 N  N   B GLY   A 133 ? 0.2019 0.1868 0.1665 -0.0100 -0.0253 0.0212  133 GLY   A N   
2805 C  CA  A GLY   A 133 ? 0.1985 0.1877 0.1708 -0.0239 -0.0384 0.0196  133 GLY   A CA  
2806 C  CA  B GLY   A 133 ? 0.2049 0.1992 0.1752 -0.0127 -0.0270 0.0189  133 GLY   A CA  
2807 C  C   A GLY   A 133 ? 0.1984 0.1970 0.1747 -0.0293 -0.0447 0.0060  133 GLY   A C   
2808 C  C   B GLY   A 133 ? 0.2037 0.2093 0.1822 -0.0135 -0.0306 0.0080  133 GLY   A C   
2809 O  O   A GLY   A 133 ? 0.2180 0.2137 0.1943 -0.0337 -0.0504 -0.0096 133 GLY   A O   
2810 O  O   B GLY   A 133 ? 0.2146 0.2163 0.1900 -0.0141 -0.0340 -0.0057 133 GLY   A O   
2817 N  N   A ALA   A 134 ? 0.1879 0.1784 0.1658 -0.0310 -0.0250 -0.0001 134 ALA   A N   
2818 N  N   B ALA   A 134 ? 0.1968 0.2081 0.1833 -0.0132 -0.0212 0.0062  134 ALA   A N   
2819 C  CA  A ALA   A 134 ? 0.1805 0.1783 0.1760 -0.0205 -0.0173 0.0002  134 ALA   A CA  
2820 C  CA  B ALA   A 134 ? 0.1915 0.2140 0.1942 -0.0144 -0.0158 0.0088  134 ALA   A CA  
2821 C  C   A ALA   A 134 ? 0.1815 0.1847 0.1742 -0.0162 -0.0110 0.0016  134 ALA   A C   
2822 C  C   B ALA   A 134 ? 0.1886 0.2172 0.1977 -0.0164 -0.0100 0.0117  134 ALA   A C   
2823 O  O   A ALA   A 134 ? 0.1965 0.1922 0.2002 -0.0140 0.0130  0.0040  134 ALA   A O   
2824 O  O   B ALA   A 134 ? 0.1973 0.2190 0.2125 -0.0205 -0.0059 0.0133  134 ALA   A O   
2825 C  CB  A ALA   A 134 ? 0.1845 0.1720 0.2051 -0.0205 -0.0132 -0.0108 134 ALA   A CB  
2826 C  CB  B ALA   A 134 ? 0.1959 0.2152 0.2088 -0.0121 -0.0124 0.0042  134 ALA   A CB  
2837 N  N   A ASP   A 135 ? 0.1798 0.1918 0.1767 -0.0264 -0.0153 0.0193  135 ASP   A N   
2838 N  N   B ASP   A 135 ? 0.1842 0.2211 0.2010 -0.0119 -0.0045 0.0128  135 ASP   A N   
2839 C  CA  A ASP   A 135 ? 0.1792 0.2063 0.2043 -0.0335 -0.0230 0.0231  135 ASP   A CA  
2840 C  CA  B ASP   A 135 ? 0.1858 0.2293 0.2094 -0.0143 -0.0018 0.0173  135 ASP   A CA  
2841 C  C   A ASP   A 135 ? 0.1716 0.1907 0.2017 -0.0238 -0.0186 0.0364  135 ASP   A C   
2842 C  C   B ASP   A 135 ? 0.1844 0.2222 0.1956 -0.0147 -0.0009 0.0269  135 ASP   A C   
2843 O  O   A ASP   A 135 ? 0.1688 0.1775 0.2182 -0.0210 -0.0172 0.0399  135 ASP   A O   
2844 O  O   B ASP   A 135 ? 0.1826 0.2149 0.2003 -0.0161 0.0011  0.0349  135 ASP   A O   
2845 C  CB  A ASP   A 135 ? 0.1973 0.2415 0.2452 -0.0516 -0.0423 0.0135  135 ASP   A CB  
2846 C  CB  B ASP   A 135 ? 0.1936 0.2473 0.2487 -0.0186 -0.0033 0.0147  135 ASP   A CB  
2847 C  CG  A ASP   A 135 ? 0.2110 0.2768 0.2841 -0.0608 -0.0540 0.0145  135 ASP   A CG  
2848 C  CG  B ASP   A 135 ? 0.2008 0.2627 0.2897 -0.0214 -0.0048 0.0137  135 ASP   A CG  
2849 O  OD1 A ASP   A 135 ? 0.2152 0.2934 0.2788 -0.0677 -0.0563 0.0414  135 ASP   A OD1 
2850 O  OD1 B ASP   A 135 ? 0.2089 0.2741 0.2988 -0.0269 0.0016  0.0143  135 ASP   A OD1 
2851 O  OD2 A ASP   A 135 ? 0.2296 0.2970 0.3254 -0.0567 -0.0546 0.0086  135 ASP   A OD2 
2852 O  OD2 B ASP   A 135 ? 0.2038 0.2684 0.3175 -0.0177 -0.0038 0.0162  135 ASP   A OD2 
2861 N  N   A PRO   A 136 ? 0.1617 0.1882 0.2095 -0.0047 -0.0001 0.0553  136 PRO   A N   
2862 N  N   B PRO   A 136 ? 0.1824 0.2213 0.1901 -0.0099 -0.0007 0.0362  136 PRO   A N   
2863 C  CA  A PRO   A 136 ? 0.1534 0.1857 0.2136 -0.0055 0.0043  0.0418  136 PRO   A CA  
2864 C  CA  B PRO   A 136 ? 0.1817 0.2187 0.1880 -0.0140 -0.0039 0.0356  136 PRO   A CA  
2865 C  C   A PRO   A 136 ? 0.1343 0.1779 0.1981 -0.0009 0.0056  0.0433  136 PRO   A C   
2866 C  C   B PRO   A 136 ? 0.1769 0.2136 0.1902 -0.0123 -0.0143 0.0341  136 PRO   A C   
2867 O  O   A PRO   A 136 ? 0.1304 0.1729 0.1917 -0.0095 0.0079  0.0360  136 PRO   A O   
2868 O  O   B PRO   A 136 ? 0.1762 0.2126 0.1923 -0.0150 -0.0197 0.0397  136 PRO   A O   
2869 C  CB  A PRO   A 136 ? 0.1692 0.1887 0.2335 0.0015  0.0083  0.0400  136 PRO   A CB  
2870 C  CB  B PRO   A 136 ? 0.1886 0.2198 0.1818 -0.0118 0.0010  0.0437  136 PRO   A CB  
2871 C  CG  A PRO   A 136 ? 0.1828 0.1968 0.2454 0.0104  0.0088  0.0521  136 PRO   A CG  
2872 C  CG  B PRO   A 136 ? 0.1952 0.2240 0.1817 -0.0066 -0.0014 0.0413  136 PRO   A CG  
2873 C  CD  A PRO   A 136 ? 0.1765 0.1927 0.2255 0.0101  0.0156  0.0661  136 PRO   A CD  
2874 C  CD  B PRO   A 136 ? 0.1914 0.2246 0.1886 -0.0062 -0.0024 0.0376  136 PRO   A CD  
2889 N  N   A ILE   A 137 ? 0.1286 0.1785 0.2050 0.0005  -0.0119 0.0487  137 ILE   A N   
2890 N  N   B ILE   A 137 ? 0.1763 0.2121 0.1933 -0.0144 -0.0151 0.0289  137 ILE   A N   
2891 C  CA  A ILE   A 137 ? 0.1305 0.1895 0.2028 -0.0100 -0.0123 0.0472  137 ILE   A CA  
2892 C  CA  B ILE   A 137 ? 0.1852 0.2156 0.2056 -0.0154 -0.0175 0.0298  137 ILE   A CA  
2893 C  C   A ILE   A 137 ? 0.1332 0.1857 0.2070 -0.0168 -0.0039 0.0389  137 ILE   A C   
2894 C  C   B ILE   A 137 ? 0.1813 0.2146 0.2161 -0.0164 -0.0185 0.0160  137 ILE   A C   
2895 O  O   A ILE   A 137 ? 0.1413 0.1812 0.2171 -0.0180 -0.0110 0.0308  137 ILE   A O   
2896 O  O   B ILE   A 137 ? 0.1825 0.2125 0.2259 -0.0151 -0.0209 0.0087  137 ILE   A O   
2897 C  CB  A ILE   A 137 ? 0.1380 0.2144 0.2075 -0.0160 -0.0205 0.0494  137 ILE   A CB  
2898 C  CB  B ILE   A 137 ? 0.1979 0.2213 0.2114 -0.0160 -0.0198 0.0371  137 ILE   A CB  
2899 C  CG1 A ILE   A 137 ? 0.1458 0.2381 0.2170 -0.0097 -0.0265 0.0593  137 ILE   A CG1 
2900 C  CG1 B ILE   A 137 ? 0.2109 0.2307 0.2113 -0.0065 -0.0196 0.0424  137 ILE   A CG1 
2901 C  CG2 A ILE   A 137 ? 0.1504 0.2159 0.2227 -0.0248 -0.0362 0.0373  137 ILE   A CG2 
2902 C  CG2 B ILE   A 137 ? 0.2020 0.2183 0.2122 -0.0188 -0.0219 0.0377  137 ILE   A CG2 
2903 C  CD1 A ILE   A 137 ? 0.1594 0.2527 0.2363 -0.0043 -0.0208 0.0551  137 ILE   A CD1 
2904 C  CD1 B ILE   A 137 ? 0.2156 0.2327 0.2193 -0.0022 -0.0167 0.0451  137 ILE   A CD1 
2927 N  N   A HIS   A 138 ? 0.1345 0.1970 0.2140 -0.0175 0.0129  0.0293  138 HIS   A N   
2928 N  N   B HIS   A 138 ? 0.1764 0.2188 0.2231 -0.0143 -0.0139 0.0110  138 HIS   A N   
2929 C  CA  A HIS   A 138 ? 0.1444 0.1943 0.2183 -0.0143 0.0106  0.0159  138 HIS   A CA  
2930 C  CA  B HIS   A 138 ? 0.1738 0.2144 0.2191 -0.0129 -0.0124 0.0140  138 HIS   A CA  
2931 C  C   A HIS   A 138 ? 0.1420 0.1868 0.2225 -0.0081 0.0128  0.0285  138 HIS   A C   
2932 C  C   B HIS   A 138 ? 0.1539 0.1985 0.2191 -0.0101 -0.0077 0.0238  138 HIS   A C   
2933 O  O   A HIS   A 138 ? 0.1521 0.1889 0.2245 -0.0080 0.0165  0.0315  138 HIS   A O   
2934 O  O   B HIS   A 138 ? 0.1544 0.2008 0.2150 -0.0110 -0.0073 0.0234  138 HIS   A O   
2935 C  CB  A HIS   A 138 ? 0.1505 0.2026 0.2106 -0.0132 0.0063  -0.0049 138 HIS   A CB  
2936 C  CB  B HIS   A 138 ? 0.1948 0.2253 0.2194 -0.0127 -0.0185 0.0112  138 HIS   A CB  
2937 C  CG  A HIS   A 138 ? 0.1655 0.2054 0.2197 -0.0218 0.0028  -0.0210 138 HIS   A CG  
2938 C  CG  B HIS   A 138 ? 0.2125 0.2296 0.2292 -0.0117 -0.0124 0.0084  138 HIS   A CG  
2939 N  ND1 A HIS   A 138 ? 0.1806 0.2120 0.2433 -0.0273 0.0032  -0.0312 138 HIS   A ND1 
2940 N  ND1 B HIS   A 138 ? 0.2214 0.2313 0.2412 -0.0131 -0.0053 0.0062  138 HIS   A ND1 
2941 C  CD2 A HIS   A 138 ? 0.1639 0.2023 0.2191 -0.0104 0.0008  -0.0185 138 HIS   A CD2 
2942 C  CD2 B HIS   A 138 ? 0.2193 0.2348 0.2336 -0.0086 -0.0093 0.0064  138 HIS   A CD2 
2943 C  CE1 A HIS   A 138 ? 0.1824 0.2139 0.2423 -0.0187 0.0008  -0.0283 138 HIS   A CE1 
2944 C  CE1 B HIS   A 138 ? 0.2245 0.2328 0.2460 -0.0105 -0.0086 0.0036  138 HIS   A CE1 
2945 N  NE2 A HIS   A 138 ? 0.1730 0.2131 0.2278 -0.0095 0.0043  -0.0224 138 HIS   A NE2 
2946 N  NE2 B HIS   A 138 ? 0.2207 0.2332 0.2383 -0.0076 -0.0056 0.0033  138 HIS   A NE2 
2961 N  N   . SER   A 139 ? 0.1377 0.1794 0.2177 -0.0078 -0.0001 0.0349  139 SER   A N   
2962 C  CA  . SER   A 139 ? 0.1357 0.1729 0.2165 -0.0063 -0.0018 0.0377  139 SER   A CA  
2963 C  C   . SER   A 139 ? 0.1337 0.1622 0.2203 -0.0078 0.0033  0.0268  139 SER   A C   
2964 O  O   . SER   A 139 ? 0.1306 0.1590 0.2288 -0.0101 0.0031  0.0317  139 SER   A O   
2965 C  CB  . SER   A 139 ? 0.1356 0.1704 0.2124 -0.0137 -0.0069 0.0389  139 SER   A CB  
2966 O  OG  . SER   A 139 ? 0.1432 0.1688 0.2177 -0.0204 -0.0082 0.0510  139 SER   A OG  
2973 N  N   . LEU   A 140 ? 0.1271 0.1650 0.2159 -0.0068 0.0074  0.0435  140 LEU   A N   
2974 C  CA  . LEU   A 140 ? 0.1308 0.1624 0.2187 -0.0116 0.0058  0.0405  140 LEU   A CA  
2975 C  C   . LEU   A 140 ? 0.1273 0.1700 0.2241 -0.0158 0.0110  0.0435  140 LEU   A C   
2976 O  O   . LEU   A 140 ? 0.1354 0.1701 0.2481 -0.0103 0.0005  0.0431  140 LEU   A O   
2977 C  CB  . LEU   A 140 ? 0.1353 0.1763 0.2241 -0.0185 0.0070  0.0412  140 LEU   A CB  
2978 C  CG  . LEU   A 140 ? 0.1339 0.1922 0.2308 -0.0252 0.0050  0.0505  140 LEU   A CG  
2979 C  CD1 . LEU   A 140 ? 0.1393 0.1955 0.2434 -0.0177 0.0024  0.0491  140 LEU   A CD1 
2980 C  CD2 . LEU   A 140 ? 0.1356 0.2160 0.2337 -0.0198 0.0099  0.0451  140 LEU   A CD2 
2992 N  N   . ARG   A 141 ? 0.1364 0.1736 0.2289 -0.0123 0.0027  0.0315  141 ARG   A N   
2993 C  CA  . ARG   A 141 ? 0.1475 0.1889 0.2425 -0.0264 -0.0069 0.0161  141 ARG   A CA  
2994 C  C   . ARG   A 141 ? 0.1454 0.1697 0.2404 -0.0222 -0.0018 0.0141  141 ARG   A C   
2995 O  O   . ARG   A 141 ? 0.1429 0.1642 0.2576 -0.0194 0.0089  0.0132  141 ARG   A O   
2996 C  CB  . ARG   A 141 ? 0.1618 0.2178 0.2597 -0.0364 -0.0045 -0.0097 141 ARG   A CB  
2997 C  CG  . ARG   A 141 ? 0.2047 0.2570 0.2839 -0.0425 0.0145  -0.0192 141 ARG   A CG  
2998 C  CD  . ARG   A 141 ? 0.2473 0.2848 0.3152 -0.0539 0.0154  -0.0256 141 ARG   A CD  
2999 N  NE  . ARG   A 141 ? 0.2460 0.3141 0.3393 -0.0624 0.0084  -0.0210 141 ARG   A NE  
3000 C  CZ  . ARG   A 141 ? 0.2469 0.3341 0.3476 -0.0853 0.0186  -0.0113 141 ARG   A CZ  
3001 N  NH1 . ARG   A 141 ? 0.2268 0.3364 0.3318 -0.1039 0.0422  -0.0295 141 ARG   A NH1 
3002 N  NH2 . ARG   A 141 ? 0.2556 0.3482 0.3686 -0.0795 0.0040  0.0035  141 ARG   A NH2 
3016 N  N   . VAL   A 142 ? 0.1396 0.1655 0.2224 -0.0146 0.0039  0.0129  142 VAL   A N   
3017 C  CA  . VAL   A 142 ? 0.1435 0.1616 0.2275 -0.0082 0.0165  0.0082  142 VAL   A CA  
3018 C  C   . VAL   A 142 ? 0.1286 0.1555 0.2280 -0.0119 0.0065  0.0127  142 VAL   A C   
3019 O  O   . VAL   A 142 ? 0.1354 0.1552 0.2363 -0.0037 0.0100  0.0174  142 VAL   A O   
3020 C  CB  . VAL   A 142 ? 0.1500 0.1695 0.2217 -0.0127 0.0170  0.0117  142 VAL   A CB  
3021 C  CG1 . VAL   A 142 ? 0.1569 0.1642 0.2266 -0.0257 0.0294  0.0006  142 VAL   A CG1 
3022 C  CG2 . VAL   A 142 ? 0.1651 0.1833 0.2356 -0.0063 0.0188  0.0170  142 VAL   A CG2 
3032 N  N   . CYS   A 143 ? 0.1340 0.1491 0.2228 -0.0183 0.0034  0.0237  143 CYS   A N   
3033 C  CA  . CYS   A 143 ? 0.1332 0.1486 0.2309 -0.0102 0.0080  0.0309  143 CYS   A CA  
3034 C  C   . CYS   A 143 ? 0.1326 0.1532 0.2404 -0.0132 0.0080  0.0319  143 CYS   A C   
3035 O  O   . CYS   A 143 ? 0.1288 0.1552 0.2338 -0.0071 0.0027  0.0367  143 CYS   A O   
3036 C  CB  . CYS   A 143 ? 0.1410 0.1532 0.2324 -0.0095 0.0080  0.0398  143 CYS   A CB  
3037 S  SG  . CYS   A 143 ? 0.1605 0.1644 0.2121 -0.0015 0.0128  0.0265  143 CYS   A SG  
3043 N  N   . VAL   A 144 ? 0.1313 0.1540 0.2703 -0.0120 0.0105  0.0473  144 VAL   A N   
3044 C  CA  . VAL   A 144 ? 0.1404 0.1635 0.2964 -0.0088 0.0192  0.0507  144 VAL   A CA  
3045 C  C   . VAL   A 144 ? 0.1396 0.1562 0.2939 -0.0226 -0.0065 0.0392  144 VAL   A C   
3046 O  O   . VAL   A 144 ? 0.1571 0.1591 0.2988 -0.0087 -0.0117 0.0484  144 VAL   A O   
3047 C  CB  . VAL   A 144 ? 0.1651 0.1867 0.3447 0.0004  0.0384  0.0570  144 VAL   A CB  
3048 C  CG1 . VAL   A 144 ? 0.1829 0.2032 0.3788 -0.0071 0.0197  0.0586  144 VAL   A CG1 
3049 C  CG2 . VAL   A 144 ? 0.1507 0.1969 0.3553 -0.0019 0.0477  0.0667  144 VAL   A CG2 
3059 N  N   . ASP   A 145 ? 0.1431 0.1519 0.2972 -0.0195 0.0015  0.0259  145 ASP   A N   
3060 C  CA  . ASP   A 145 ? 0.1591 0.1563 0.3001 -0.0194 -0.0014 0.0141  145 ASP   A CA  
3061 C  C   . ASP   A 145 ? 0.1612 0.1490 0.3021 -0.0146 -0.0030 -0.0011 145 ASP   A C   
3062 O  O   . ASP   A 145 ? 0.1757 0.1536 0.3478 -0.0166 -0.0063 -0.0287 145 ASP   A O   
3063 C  CB  . ASP   A 145 ? 0.1673 0.1889 0.3195 -0.0277 -0.0185 0.0091  145 ASP   A CB  
3064 C  CG  . ASP   A 145 ? 0.1856 0.2261 0.3444 -0.0467 -0.0312 0.0184  145 ASP   A CG  
3065 O  OD1 . ASP   A 145 ? 0.1801 0.2420 0.3535 -0.0571 -0.0213 0.0264  145 ASP   A OD1 
3066 O  OD2 . ASP   A 145 ? 0.2083 0.2525 0.3604 -0.0556 -0.0492 0.0161  145 ASP   A OD2 
3071 N  N   . THR   A 146 ? 0.1402 0.1411 0.2632 -0.0157 0.0025  0.0065  146 THR   A N   
3072 C  CA  . THR   A 146 ? 0.1383 0.1423 0.2511 -0.0082 0.0051  0.0135  146 THR   A CA  
3073 C  C   . THR   A 146 ? 0.1308 0.1372 0.2524 -0.0035 0.0118  0.0204  146 THR   A C   
3074 O  O   . THR   A 146 ? 0.1466 0.1531 0.2632 0.0003  0.0044  0.0142  146 THR   A O   
3075 C  CB  . THR   A 146 ? 0.1324 0.1442 0.2517 -0.0026 0.0077  0.0171  146 THR   A CB  
3076 O  OG1 . THR   A 146 ? 0.1360 0.1601 0.2583 -0.0029 0.0010  0.0077  146 THR   A OG1 
3077 C  CG2 . THR   A 146 ? 0.1331 0.1494 0.2675 -0.0095 0.0054  0.0141  146 THR   A CG2 
3085 N  N   . VAL   A 147 ? 0.1297 0.1449 0.2546 -0.0031 0.0125  0.0178  147 VAL   A N   
3086 C  CA  . VAL   A 147 ? 0.1283 0.1467 0.2545 -0.0126 0.0298  0.0334  147 VAL   A CA  
3087 C  C   . VAL   A 147 ? 0.1305 0.1432 0.2691 -0.0142 0.0219  0.0324  147 VAL   A C   
3088 O  O   . VAL   A 147 ? 0.1368 0.1499 0.2814 -0.0166 0.0111  0.0407  147 VAL   A O   
3089 C  CB  . VAL   A 147 ? 0.1455 0.1476 0.2428 -0.0143 0.0248  0.0307  147 VAL   A CB  
3090 C  CG1 . VAL   A 147 ? 0.1722 0.1537 0.2506 -0.0097 0.0201  0.0410  147 VAL   A CG1 
3091 C  CG2 . VAL   A 147 ? 0.1545 0.1459 0.2400 -0.0099 0.0163  0.0255  147 VAL   A CG2 
3101 N  N   . ARG   A 148 ? 0.1350 0.1456 0.2760 -0.0135 0.0198  0.0552  148 ARG   A N   
3102 C  CA  . ARG   A 148 ? 0.1455 0.1514 0.2730 -0.0164 0.0106  0.0541  148 ARG   A CA  
3103 C  C   . ARG   A 148 ? 0.1530 0.1488 0.2682 -0.0185 0.0137  0.0738  148 ARG   A C   
3104 O  O   . ARG   A 148 ? 0.1798 0.1647 0.2862 -0.0224 0.0226  0.0671  148 ARG   A O   
3105 C  CB  . ARG   A 148 ? 0.1530 0.1548 0.2739 -0.0028 0.0232  0.0551  148 ARG   A CB  
3106 C  CG  . ARG   A 148 ? 0.1674 0.1582 0.3034 -0.0061 0.0383  0.0441  148 ARG   A CG  
3107 C  CD  . ARG   A 148 ? 0.1813 0.1549 0.3276 -0.0101 0.0496  0.0601  148 ARG   A CD  
3108 N  NE  . ARG   A 148 ? 0.1776 0.1565 0.3278 0.0035  0.0534  0.0639  148 ARG   A NE  
3109 C  CZ  . ARG   A 148 ? 0.1745 0.1472 0.3134 -0.0019 0.0461  0.0508  148 ARG   A CZ  
3110 N  NH1 . ARG   A 148 ? 0.1769 0.1461 0.3266 -0.0154 0.0389  0.0226  148 ARG   A NH1 
3111 N  NH2 . ARG   A 148 ? 0.1672 0.1622 0.3158 0.0122  0.0460  0.0524  148 ARG   A NH2 
3125 N  N   . THR   A 149 ? 0.1530 0.1636 0.2667 -0.0155 -0.0009 0.0657  149 THR   A N   
3126 C  CA  . THR   A 149 ? 0.1551 0.1719 0.2631 -0.0185 0.0023  0.0649  149 THR   A CA  
3127 C  C   . THR   A 149 ? 0.1492 0.1710 0.2481 -0.0261 0.0083  0.0678  149 THR   A C   
3128 O  O   . THR   A 149 ? 0.1504 0.1801 0.2565 -0.0259 0.0072  0.0589  149 THR   A O   
3129 C  CB  . THR   A 149 ? 0.1516 0.1833 0.2622 -0.0205 0.0045  0.0581  149 THR   A CB  
3130 O  OG1 . THR   A 149 ? 0.1577 0.1705 0.2659 -0.0265 0.0096  0.0519  149 THR   A OG1 
3131 C  CG2 . THR   A 149 ? 0.1482 0.1947 0.2682 -0.0154 -0.0070 0.0461  149 THR   A CG2 
3139 N  N   . ASN   A 150 ? 0.1549 0.1782 0.2461 -0.0148 -0.0046 0.0797  150 ASN   A N   
3140 C  CA  . ASN   A 150 ? 0.1668 0.1849 0.2400 -0.0203 0.0042  0.0655  150 ASN   A CA  
3141 C  C   . ASN   A 150 ? 0.1469 0.1747 0.2318 -0.0256 0.0005  0.0587  150 ASN   A C   
3142 O  O   . ASN   A 150 ? 0.1544 0.1915 0.2546 -0.0223 -0.0105 0.0531  150 ASN   A O   
3143 C  CB  . ASN   A 150 ? 0.2158 0.2126 0.2708 -0.0308 0.0267  0.0796  150 ASN   A CB  
3144 C  CG  . ASN   A 150 ? 0.2693 0.2421 0.3301 -0.0300 0.0106  0.0859  150 ASN   A CG  
3145 O  OD1 . ASN   A 150 ? 0.2917 0.2482 0.3483 -0.0350 0.0134  0.0999  150 ASN   A OD1 
3146 N  ND2 . ASN   A 150 ? 0.2944 0.2672 0.3707 -0.0235 -0.0014 0.0785  150 ASN   A ND2 
3153 N  N   . VAL   A 151 ? 0.1502 0.1598 0.2264 -0.0267 0.0023  0.0553  151 VAL   A N   
3154 C  CA  . VAL   A 151 ? 0.1584 0.1662 0.2201 -0.0296 0.0024  0.0508  151 VAL   A CA  
3155 C  C   . VAL   A 151 ? 0.1483 0.1623 0.2243 -0.0349 0.0045  0.0533  151 VAL   A C   
3156 O  O   . VAL   A 151 ? 0.1599 0.1714 0.2530 -0.0304 0.0075  0.0473  151 VAL   A O   
3157 C  CB  . VAL   A 151 ? 0.1894 0.1823 0.2216 -0.0168 0.0001  0.0406  151 VAL   A CB  
3158 C  CG1 . VAL   A 151 ? 0.1864 0.1993 0.2425 -0.0150 -0.0073 0.0325  151 VAL   A CG1 
3159 C  CG2 . VAL   A 151 ? 0.2021 0.1749 0.2207 -0.0105 0.0158  0.0391  151 VAL   A CG2 
3169 N  N   A TYR   A 152 ? 0.1457 0.1627 0.2316 -0.0317 0.0062  0.0546  152 TYR   A N   
3170 N  N   B TYR   A 152 ? 0.1501 0.1700 0.2038 -0.0331 0.0001  0.0485  152 TYR   A N   
3171 C  CA  A TYR   A 152 ? 0.1462 0.1703 0.2076 -0.0278 0.0083  0.0615  152 TYR   A CA  
3172 C  CA  B TYR   A 152 ? 0.1524 0.1798 0.1684 -0.0310 -0.0061 0.0466  152 TYR   A CA  
3173 C  C   A TYR   A 152 ? 0.1450 0.1546 0.1908 -0.0297 0.0211  0.0463  152 TYR   A C   
3174 C  C   B TYR   A 152 ? 0.1467 0.1735 0.1485 -0.0281 -0.0051 0.0399  152 TYR   A C   
3175 O  O   A TYR   A 152 ? 0.1567 0.1522 0.1836 -0.0340 0.0268  0.0348  152 TYR   A O   
3176 O  O   B TYR   A 152 ? 0.1546 0.1756 0.1539 -0.0259 -0.0042 0.0322  152 TYR   A O   
3177 C  CB  A TYR   A 152 ? 0.1592 0.1824 0.2118 -0.0233 0.0187  0.0753  152 TYR   A CB  
3178 C  CB  B TYR   A 152 ? 0.1638 0.1903 0.1740 -0.0295 -0.0006 0.0442  152 TYR   A CB  
3179 C  CG  A TYR   A 152 ? 0.1689 0.2072 0.2115 -0.0243 0.0246  0.0745  152 TYR   A CG  
3180 C  CG  B TYR   A 152 ? 0.1745 0.2061 0.1815 -0.0320 0.0135  0.0444  152 TYR   A CG  
3181 C  CD1 A TYR   A 152 ? 0.1799 0.2237 0.2314 -0.0163 0.0309  0.0747  152 TYR   A CD1 
3182 C  CD1 B TYR   A 152 ? 0.1830 0.2142 0.1922 -0.0308 0.0275  0.0534  152 TYR   A CD1 
3183 C  CD2 A TYR   A 152 ? 0.1737 0.2172 0.2092 -0.0331 0.0251  0.0693  152 TYR   A CD2 
3184 C  CD2 B TYR   A 152 ? 0.1789 0.2113 0.1796 -0.0393 0.0155  0.0393  152 TYR   A CD2 
3185 C  CE1 A TYR   A 152 ? 0.2016 0.2366 0.2311 -0.0132 0.0281  0.0864  152 TYR   A CE1 
3186 C  CE1 B TYR   A 152 ? 0.1991 0.2240 0.2066 -0.0293 0.0243  0.0576  152 TYR   A CE1 
3187 C  CE2 A TYR   A 152 ? 0.1933 0.2295 0.2263 -0.0312 0.0312  0.0719  152 TYR   A CE2 
3188 C  CE2 B TYR   A 152 ? 0.1961 0.2221 0.2017 -0.0384 0.0204  0.0423  152 TYR   A CE2 
3189 C  CZ  A TYR   A 152 ? 0.2091 0.2387 0.2284 -0.0193 0.0286  0.0923  152 TYR   A CZ  
3190 C  CZ  B TYR   A 152 ? 0.2072 0.2295 0.2095 -0.0341 0.0255  0.0567  152 TYR   A CZ  
3191 O  OH  A TYR   A 152 ? 0.2255 0.2580 0.2489 -0.0083 0.0340  0.1041  152 TYR   A OH  
3192 O  OH  B TYR   A 152 ? 0.2234 0.2481 0.2351 -0.0318 0.0324  0.0637  152 TYR   A OH  
3211 N  N   A LEU   A 153 ? 0.1451 0.1497 0.1951 -0.0282 0.0254  0.0451  153 LEU   A N   
3212 N  N   B LEU   A 153 ? 0.1407 0.1680 0.1504 -0.0293 -0.0058 0.0342  153 LEU   A N   
3213 C  CA  A LEU   A 153 ? 0.1400 0.1392 0.1926 -0.0135 0.0231  0.0348  153 LEU   A CA  
3214 C  CA  B LEU   A 153 ? 0.1346 0.1604 0.1425 -0.0169 0.0043  0.0186  153 LEU   A CA  
3215 C  C   A LEU   A 153 ? 0.1425 0.1408 0.1832 -0.0147 0.0293  0.0231  153 LEU   A C   
3216 C  C   B LEU   A 153 ? 0.1361 0.1656 0.1355 -0.0057 0.0096  0.0112  153 LEU   A C   
3217 O  O   A LEU   A 153 ? 0.1462 0.1479 0.1986 -0.0211 0.0381  0.0204  153 LEU   A O   
3218 O  O   B LEU   A 153 ? 0.1371 0.1720 0.1303 -0.0040 0.0150  0.0175  153 LEU   A O   
3219 C  CB  A LEU   A 153 ? 0.1336 0.1306 0.1961 -0.0144 0.0146  0.0210  153 LEU   A CB  
3220 C  CB  B LEU   A 153 ? 0.1327 0.1551 0.1494 -0.0154 0.0078  0.0174  153 LEU   A CB  
3221 C  CG  A LEU   A 153 ? 0.1340 0.1380 0.2032 -0.0134 0.0186  0.0107  153 LEU   A CG  
3222 C  CG  B LEU   A 153 ? 0.1417 0.1608 0.1483 -0.0051 0.0066  0.0123  153 LEU   A CG  
3223 C  CD1 A LEU   A 153 ? 0.1451 0.1264 0.2108 -0.0076 0.0148  0.0136  153 LEU   A CD1 
3224 C  CD1 B LEU   A 153 ? 0.1488 0.1593 0.1553 0.0049  0.0034  0.0167  153 LEU   A CD1 
3225 C  CD2 A LEU   A 153 ? 0.1383 0.1477 0.1832 -0.0200 0.0191  -0.0071 153 LEU   A CD2 
3226 C  CD2 B LEU   A 153 ? 0.1468 0.1700 0.1518 -0.0082 -0.0008 0.0146  153 LEU   A CD2 
3249 N  N   A ALA   A 154 ? 0.1453 0.1372 0.1740 -0.0181 0.0261  0.0209  154 ALA   A N   
3250 N  N   B ALA   A 154 ? 0.1377 0.1654 0.1336 -0.0046 0.0162  0.0016  154 ALA   A N   
3251 C  CA  A ALA   A 154 ? 0.1561 0.1444 0.1754 -0.0133 0.0320  0.0128  154 ALA   A CA  
3252 C  CA  B ALA   A 154 ? 0.1427 0.1670 0.1436 -0.0032 0.0144  0.0008  154 ALA   A CA  
3253 C  C   A ALA   A 154 ? 0.1487 0.1347 0.1775 -0.0106 0.0325  0.0253  154 ALA   A C   
3254 C  C   B ALA   A 154 ? 0.1374 0.1719 0.1558 -0.0061 0.0125  0.0163  154 ALA   A C   
3255 O  O   A ALA   A 154 ? 0.1551 0.1485 0.1919 -0.0121 0.0283  0.0243  154 ALA   A O   
3256 O  O   B ALA   A 154 ? 0.1452 0.1729 0.1466 -0.0074 0.0092  0.0268  154 ALA   A O   
3257 C  CB  A ALA   A 154 ? 0.1656 0.1525 0.1796 0.0016  0.0325  0.0036  154 ALA   A CB  
3258 C  CB  B ALA   A 154 ? 0.1457 0.1644 0.1445 -0.0014 0.0060  -0.0095 154 ALA   A CB  
3269 N  N   A VAL   A 155 ? 0.1317 0.1099 0.1528 -0.0040 0.0383  0.0412  155 VAL   A N   
3270 N  N   B VAL   A 155 ? 0.1348 0.1736 0.1749 -0.0072 0.0226  0.0319  155 VAL   A N   
3271 C  CA  A VAL   A 155 ? 0.1474 0.1286 0.1936 -0.0029 0.0240  0.0532  155 VAL   A CA  
3272 C  CA  B VAL   A 155 ? 0.1595 0.1957 0.2090 -0.0055 0.0141  0.0382  155 VAL   A CA  
3273 C  CA  T VAL   A 155 ? 0.1620 0.1724 0.2094 -0.0121 0.0353  0.0522  155 VAL   A CA  
3274 C  C   A VAL   A 155 ? 0.1574 0.1434 0.2205 0.0146  0.0324  0.0616  155 VAL   A C   
3275 C  C   B VAL   A 155 ? 0.1730 0.2053 0.2414 0.0036  0.0212  0.0498  155 VAL   A C   
3276 C  C   T VAL   A 155 ? 0.1630 0.1736 0.2024 0.0020  0.0459  0.0552  155 VAL   A C   
3277 O  O   A VAL   A 155 ? 0.1545 0.1523 0.2402 0.0207  0.0375  0.0574  155 VAL   A O   
3278 O  O   B VAL   A 155 ? 0.1731 0.2084 0.2619 0.0070  0.0288  0.0526  155 VAL   A O   
3279 O  O   T VAL   A 155 ? 0.1553 0.1845 0.1938 0.0113  0.0482  0.0491  155 VAL   A O   
3280 C  CB  A VAL   A 155 ? 0.1466 0.1386 0.2052 -0.0052 0.0032  0.0488  155 VAL   A CB  
3281 C  CB  B VAL   A 155 ? 0.1618 0.2048 0.2044 -0.0030 -0.0065 0.0385  155 VAL   A CB  
3282 C  CB  T VAL   A 155 ? 0.1573 0.1752 0.2074 -0.0146 0.0203  0.0520  155 VAL   A CB  
3283 C  CG1 A VAL   A 155 ? 0.1514 0.1500 0.2078 -0.0001 -0.0013 0.0471  155 VAL   A CG1 
3284 C  CG1 B VAL   A 155 ? 0.1632 0.2108 0.2020 -0.0032 -0.0167 0.0318  155 VAL   A CG1 
3285 C  CG1 T VAL   A 155 ? 0.1591 0.1802 0.2005 -0.0130 0.0213  0.0570  155 VAL   A CG1 
3286 C  CG2 A VAL   A 155 ? 0.1532 0.1458 0.2171 -0.0011 -0.0115 0.0410  155 VAL   A CG2 
3287 C  CG2 B VAL   A 155 ? 0.1590 0.2052 0.2043 -0.0032 -0.0104 0.0410  155 VAL   A CG2 
3288 C  CG2 T VAL   A 155 ? 0.1612 0.1803 0.2166 -0.0104 0.0076  0.0448  155 VAL   A CG2 
3314 N  N   A PHE   A 156 ? 0.1699 0.1527 0.2310 0.0284  0.0354  0.0706  156 PHE   A N   
3315 N  N   B PHE   A 156 ? 0.1863 0.2118 0.2448 0.0107  0.0199  0.0570  156 PHE   A N   
3316 N  N   T PHE   A 156 ? 0.1759 0.1662 0.2021 0.0084  0.0502  0.0661  156 PHE   A N   
3317 C  CA  A PHE   A 156 ? 0.1915 0.1700 0.2550 0.0466  0.0382  0.0696  156 PHE   A CA  
3318 C  CA  B PHE   A 156 ? 0.2113 0.2228 0.2673 0.0174  0.0269  0.0635  156 PHE   A CA  
3319 C  CA  T PHE   A 156 ? 0.1994 0.1671 0.2006 0.0172  0.0554  0.0720  156 PHE   A CA  
3320 C  C   A PHE   A 156 ? 0.1949 0.1795 0.2648 0.0560  0.0489  0.0761  156 PHE   A C   
3321 C  C   B PHE   A 156 ? 0.2145 0.2282 0.2725 0.0135  0.0366  0.0794  156 PHE   A C   
3322 C  C   T PHE   A 156 ? 0.1990 0.1815 0.2122 0.0251  0.0706  0.0784  156 PHE   A C   
3323 O  O   A PHE   A 156 ? 0.1973 0.1797 0.2736 0.0445  0.0694  0.0675  156 PHE   A O   
3324 O  O   B PHE   A 156 ? 0.2145 0.2296 0.2840 0.0071  0.0441  0.0806  156 PHE   A O   
3325 O  O   T PHE   A 156 ? 0.2041 0.1841 0.2166 0.0276  0.0880  0.0593  156 PHE   A O   
3326 C  CB  A PHE   A 156 ? 0.2083 0.1828 0.2640 0.0481  0.0349  0.0618  156 PHE   A CB  
3327 C  CB  B PHE   A 156 ? 0.2313 0.2323 0.2861 0.0223  0.0207  0.0593  156 PHE   A CB  
3328 C  CB  T PHE   A 156 ? 0.2121 0.1546 0.1834 0.0176  0.0492  0.0665  156 PHE   A CB  
3329 C  CG  A PHE   A 156 ? 0.2271 0.1981 0.2816 0.0523  0.0281  0.0475  156 PHE   A CG  
3330 C  CG  B PHE   A 156 ? 0.2501 0.2410 0.3109 0.0310  0.0057  0.0483  156 PHE   A CG  
3331 C  CG  T PHE   A 156 ? 0.2233 0.1552 0.1702 0.0196  0.0400  0.0672  156 PHE   A CG  
3332 C  CD1 A PHE   A 156 ? 0.2342 0.2037 0.2885 0.0595  0.0318  0.0362  156 PHE   A CD1 
3333 C  CD1 B PHE   A 156 ? 0.2595 0.2457 0.3187 0.0379  -0.0016 0.0454  156 PHE   A CD1 
3334 C  CD1 T PHE   A 156 ? 0.2290 0.1650 0.1877 0.0200  0.0308  0.0556  156 PHE   A CD1 
3335 C  CD2 A PHE   A 156 ? 0.2387 0.2115 0.2917 0.0527  0.0198  0.0477  156 PHE   A CD2 
3336 C  CD2 B PHE   A 156 ? 0.2575 0.2500 0.3242 0.0348  -0.0026 0.0426  156 PHE   A CD2 
3337 C  CD2 T PHE   A 156 ? 0.2286 0.1550 0.1722 0.0239  0.0381  0.0681  156 PHE   A CD2 
3338 C  CE1 A PHE   A 156 ? 0.2384 0.2075 0.2933 0.0641  0.0342  0.0309  156 PHE   A CE1 
3339 C  CE1 B PHE   A 156 ? 0.2640 0.2469 0.3257 0.0414  -0.0079 0.0473  156 PHE   A CE1 
3340 C  CE1 T PHE   A 156 ? 0.2347 0.1682 0.2047 0.0189  0.0266  0.0472  156 PHE   A CE1 
3341 C  CE2 A PHE   A 156 ? 0.2458 0.2190 0.2982 0.0570  0.0187  0.0363  156 PHE   A CE2 
3342 C  CE2 B PHE   A 156 ? 0.2605 0.2515 0.3267 0.0382  -0.0084 0.0424  156 PHE   A CE2 
3343 C  CE2 T PHE   A 156 ? 0.2361 0.1622 0.1869 0.0233  0.0282  0.0589  156 PHE   A CE2 
3344 C  CZ  A PHE   A 156 ? 0.2421 0.2166 0.2936 0.0636  0.0318  0.0295  156 PHE   A CZ  
3345 C  CZ  B PHE   A 156 ? 0.2650 0.2503 0.3316 0.0412  -0.0122 0.0440  156 PHE   A CZ  
3346 C  CZ  T PHE   A 156 ? 0.2381 0.1618 0.2053 0.0155  0.0252  0.0511  156 PHE   A CZ  
3374 N  N   A ASP   A 157 ? 0.1993 0.1999 0.2789 0.0641  0.0382  0.0779  157 ASP   A N   
3375 N  N   B ASP   A 157 ? 0.2130 0.2350 0.2629 0.0108  0.0361  0.0850  157 ASP   A N   
3376 N  N   T ASP   A 157 ? 0.1905 0.2005 0.2318 0.0258  0.0638  0.0959  157 ASP   A N   
3377 C  CA  A ASP   A 157 ? 0.2087 0.2325 0.2829 0.0628  0.0348  0.0794  157 ASP   A CA  
3378 C  CA  B ASP   A 157 ? 0.2171 0.2492 0.2606 0.0121  0.0259  0.0889  157 ASP   A CA  
3379 C  CA  T ASP   A 157 ? 0.1891 0.2252 0.2409 0.0326  0.0554  0.1033  157 ASP   A CA  
3380 C  C   A ASP   A 157 ? 0.1997 0.2549 0.2924 0.0643  0.0264  0.0865  157 ASP   A C   
3381 C  C   B ASP   A 157 ? 0.2213 0.2629 0.2525 0.0238  0.0338  0.0933  157 ASP   A C   
3382 C  C   T ASP   A 157 ? 0.1805 0.2453 0.2430 0.0380  0.0608  0.1170  157 ASP   A C   
3383 O  O   A ASP   A 157 ? 0.1888 0.2550 0.2907 0.0673  0.0144  0.0910  157 ASP   A O   
3384 O  O   B ASP   A 157 ? 0.2206 0.2617 0.2642 0.0278  0.0335  0.0870  157 ASP   A O   
3385 O  O   T ASP   A 157 ? 0.1646 0.2445 0.2426 0.0409  0.0582  0.1203  157 ASP   A O   
3386 C  CB  A ASP   A 157 ? 0.2221 0.2388 0.2852 0.0673  0.0414  0.0732  157 ASP   A CB  
3387 C  CB  B ASP   A 157 ? 0.2159 0.2462 0.2680 0.0073  0.0091  0.0898  157 ASP   A CB  
3388 C  CB  T ASP   A 157 ? 0.1954 0.2263 0.2504 0.0417  0.0415  0.0951  157 ASP   A CB  
3389 C  CG  A ASP   A 157 ? 0.2354 0.2454 0.2978 0.0696  0.0495  0.0635  157 ASP   A CG  
3390 C  CG  B ASP   A 157 ? 0.2141 0.2390 0.2741 0.0019  -0.0030 0.0954  157 ASP   A CG  
3391 C  CG  T ASP   A 157 ? 0.1990 0.2243 0.2610 0.0447  0.0313  0.0859  157 ASP   A CG  
3392 O  OD1 A ASP   A 157 ? 0.2476 0.2456 0.3078 0.0687  0.0439  0.0593  157 ASP   A OD1 
3393 O  OD1 B ASP   A 157 ? 0.2204 0.2401 0.2778 0.0077  -0.0199 0.1008  157 ASP   A OD1 
3394 O  OD1 T ASP   A 157 ? 0.1979 0.2159 0.2688 0.0399  0.0459  0.0768  157 ASP   A OD1 
3395 O  OD2 A ASP   A 157 ? 0.2281 0.2438 0.2997 0.0672  0.0667  0.0725  157 ASP   A OD2 
3396 O  OD2 B ASP   A 157 ? 0.2193 0.2354 0.2898 -0.0011 -0.0079 0.0835  157 ASP   A OD2 
3397 O  OD2 T ASP   A 157 ? 0.1973 0.2243 0.2636 0.0484  0.0053  0.0912  157 ASP   A OD2 
3410 N  N   A LYS   A 158 ? 0.2064 0.2769 0.3059 0.0607  0.0355  0.0850  158 LYS   A N   
3411 N  N   B LYS   A 158 ? 0.2251 0.2762 0.2468 0.0313  0.0420  0.0963  158 LYS   A N   
3412 N  N   T LYS   A 158 ? 0.1928 0.2666 0.2503 0.0375  0.0729  0.1151  158 LYS   A N   
3413 C  CA  A LYS   A 158 ? 0.2052 0.2965 0.3147 0.0609  0.0454  0.0830  158 LYS   A CA  
3414 C  CA  B LYS   A 158 ? 0.2260 0.2896 0.2573 0.0405  0.0341  0.0878  158 LYS   A CA  
3415 C  CA  T LYS   A 158 ? 0.2014 0.2864 0.2716 0.0425  0.0697  0.1029  158 LYS   A CA  
3416 C  C   A LYS   A 158 ? 0.1889 0.3088 0.3049 0.0665  0.0399  0.0941  158 LYS   A C   
3417 C  C   B LYS   A 158 ? 0.2199 0.2961 0.2600 0.0466  0.0338  0.0960  158 LYS   A C   
3418 C  C   T LYS   A 158 ? 0.1952 0.2950 0.2706 0.0506  0.0583  0.1054  158 LYS   A C   
3419 O  O   A LYS   A 158 ? 0.1846 0.3162 0.3063 0.0597  0.0434  0.1014  158 LYS   A O   
3420 O  O   B LYS   A 158 ? 0.2155 0.3003 0.2634 0.0441  0.0399  0.0901  158 LYS   A O   
3421 O  O   T LYS   A 158 ? 0.1924 0.3000 0.2755 0.0488  0.0543  0.1105  158 LYS   A O   
3422 C  CB  A LYS   A 158 ? 0.2194 0.3004 0.3288 0.0564  0.0625  0.0759  158 LYS   A CB  
3423 C  CB  B LYS   A 158 ? 0.2362 0.2973 0.2787 0.0383  0.0272  0.0597  158 LYS   A CB  
3424 C  CB  T LYS   A 158 ? 0.2185 0.2950 0.3005 0.0389  0.0755  0.0855  158 LYS   A CB  
3425 C  CG  A LYS   A 158 ? 0.2339 0.3052 0.3411 0.0502  0.0717  0.0715  158 LYS   A CG  
3426 C  CG  B LYS   A 158 ? 0.2446 0.3048 0.2999 0.0347  0.0214  0.0330  158 LYS   A CG  
3427 C  CG  T LYS   A 158 ? 0.2362 0.3024 0.3241 0.0367  0.0747  0.0753  158 LYS   A CG  
3428 C  CD  A LYS   A 158 ? 0.2415 0.3097 0.3493 0.0440  0.0851  0.0712  158 LYS   A CD  
3429 C  CD  B LYS   A 158 ? 0.2515 0.3130 0.3212 0.0300  0.0175  0.0104  158 LYS   A CD  
3430 C  CD  T LYS   A 158 ? 0.2513 0.3087 0.3462 0.0376  0.0734  0.0691  158 LYS   A CD  
3431 C  CE  A LYS   A 158 ? 0.2448 0.3125 0.3513 0.0365  0.0972  0.0762  158 LYS   A CE  
3432 C  CE  B LYS   A 158 ? 0.2588 0.3180 0.3390 0.0276  0.0104  -0.0059 158 LYS   A CE  
3433 C  CE  T LYS   A 158 ? 0.2619 0.3119 0.3604 0.0369  0.0712  0.0681  158 LYS   A CE  
3434 N  NZ  A LYS   A 158 ? 0.2465 0.3142 0.3554 0.0293  0.1042  0.0795  158 LYS   A NZ  
3435 N  NZ  B LYS   A 158 ? 0.2636 0.3199 0.3471 0.0252  0.0075  -0.0153 158 LYS   A NZ  
3436 N  NZ  T LYS   A 158 ? 0.2691 0.3133 0.3686 0.0355  0.0696  0.0677  158 LYS   A NZ  
3476 N  N   A ASN   A 159 ? 0.1804 0.3124 0.3004 0.0711  0.0318  0.0970  159 ASN   A N   
3477 N  N   B ASN   A 159 ? 0.2204 0.2996 0.2704 0.0514  0.0346  0.0959  159 ASN   A N   
3478 N  N   T ASN   A 159 ? 0.1956 0.2969 0.2756 0.0528  0.0528  0.0991  159 ASN   A N   
3479 C  CA  A ASN   A 159 ? 0.1744 0.3161 0.2843 0.0662  0.0193  0.1013  159 ASN   A CA  
3480 C  CA  B ASN   A 159 ? 0.2251 0.3055 0.2962 0.0492  0.0345  0.0844  159 ASN   A CA  
3481 C  CA  T ASN   A 159 ? 0.2032 0.2999 0.2769 0.0468  0.0392  0.0917  159 ASN   A CA  
3482 C  C   A ASN   A 159 ? 0.1506 0.3149 0.2546 0.0593  0.0221  0.1014  159 ASN   A C   
3483 C  C   B ASN   A 159 ? 0.2163 0.3076 0.2784 0.0491  0.0304  0.0774  159 ASN   A C   
3484 C  C   T ASN   A 159 ? 0.2043 0.3018 0.2676 0.0377  0.0448  0.0804  159 ASN   A C   
3485 O  O   A ASN   A 159 ? 0.1354 0.3180 0.2396 0.0628  0.0124  0.0985  159 ASN   A O   
3486 O  O   B ASN   A 159 ? 0.2050 0.3092 0.2804 0.0470  0.0253  0.0779  159 ASN   A O   
3487 O  O   T ASN   A 159 ? 0.2060 0.3031 0.2642 0.0352  0.0467  0.0683  159 ASN   A O   
3488 C  CB  A ASN   A 159 ? 0.1886 0.3212 0.3050 0.0649  0.0101  0.0999  159 ASN   A CB  
3489 C  CB  B ASN   A 159 ? 0.2393 0.3110 0.3392 0.0458  0.0410  0.0770  159 ASN   A CB  
3490 C  CB  T ASN   A 159 ? 0.2086 0.3019 0.2942 0.0478  0.0228  0.0939  159 ASN   A CB  
3491 C  CG  A ASN   A 159 ? 0.2033 0.3272 0.3324 0.0598  0.0063  0.0895  159 ASN   A CG  
3492 C  CG  B ASN   A 159 ? 0.2536 0.3183 0.3836 0.0391  0.0513  0.0649  159 ASN   A CG  
3493 C  CG  T ASN   A 159 ? 0.2145 0.3044 0.3181 0.0465  0.0112  0.0885  159 ASN   A CG  
3494 O  OD1 A ASN   A 159 ? 0.2136 0.3322 0.3484 0.0557  0.0125  0.0892  159 ASN   A OD1 
3495 O  OD1 B ASN   A 159 ? 0.2614 0.3229 0.3999 0.0351  0.0599  0.0547  159 ASN   A OD1 
3496 O  OD1 T ASN   A 159 ? 0.2191 0.3078 0.3316 0.0433  0.0163  0.0881  159 ASN   A OD1 
3497 N  ND2 A ASN   A 159 ? 0.2058 0.3304 0.3447 0.0557  0.0060  0.0792  159 ASN   A ND2 
3498 N  ND2 B ASN   A 159 ? 0.2583 0.3246 0.4037 0.0365  0.0532  0.0640  159 ASN   A ND2 
3499 N  ND2 T ASN   A 159 ? 0.2148 0.3068 0.3278 0.0451  0.0050  0.0824  159 ASN   A ND2 
3518 N  N   A LEU   A 160 ? 0.1413 0.3033 0.2428 0.0470  0.0206  0.1100  160 LEU   A N   
3519 N  N   B LEU   A 160 ? 0.2126 0.3037 0.2523 0.0501  0.0310  0.0771  160 LEU   A N   
3520 N  N   T LEU   A 160 ? 0.2017 0.2961 0.2646 0.0295  0.0391  0.0850  160 LEU   A N   
3521 C  CA  A LEU   A 160 ? 0.1350 0.2905 0.2293 0.0306  0.0359  0.1159  160 LEU   A CA  
3522 C  CA  B LEU   A 160 ? 0.2129 0.2975 0.2446 0.0459  0.0289  0.0724  160 LEU   A CA  
3523 C  CA  T LEU   A 160 ? 0.2012 0.2889 0.2567 0.0193  0.0432  0.0910  160 LEU   A CA  
3524 C  C   A LEU   A 160 ? 0.1163 0.2851 0.2114 0.0208  0.0402  0.1168  160 LEU   A C   
3525 C  C   B LEU   A 160 ? 0.2050 0.2946 0.2305 0.0339  0.0299  0.0765  160 LEU   A C   
3526 O  O   A LEU   A 160 ? 0.1053 0.2952 0.2109 0.0198  0.0315  0.1134  160 LEU   A O   
3527 O  O   B LEU   A 160 ? 0.1986 0.3009 0.2256 0.0303  0.0284  0.0810  160 LEU   A O   
3528 C  CB  A LEU   A 160 ? 0.1453 0.2853 0.2328 0.0284  0.0325  0.1150  160 LEU   A CB  
3529 C  CB  B LEU   A 160 ? 0.2217 0.2956 0.2565 0.0454  0.0288  0.0599  160 LEU   A CB  
3530 C  CB  T LEU   A 160 ? 0.1991 0.2831 0.2504 0.0116  0.0418  0.0927  160 LEU   A CB  
3531 C  CG  A LEU   A 160 ? 0.1554 0.2847 0.2479 0.0258  0.0350  0.0962  160 LEU   A CG  
3532 C  CG  B LEU   A 160 ? 0.2305 0.2948 0.2718 0.0423  0.0188  0.0438  160 LEU   A CG  
3533 C  CG  T LEU   A 160 ? 0.1998 0.2810 0.2504 0.0044  0.0446  0.0827  160 LEU   A CG  
3534 C  CD1 A LEU   A 160 ? 0.1665 0.2855 0.2553 0.0254  0.0345  0.0877  160 LEU   A CD1 
3535 C  CD1 B LEU   A 160 ? 0.2294 0.2927 0.2707 0.0388  0.0149  0.0438  160 LEU   A CD1 
3536 C  CD1 T LEU   A 160 ? 0.2047 0.2819 0.2548 0.0043  0.0442  0.0764  160 LEU   A CD1 
3537 C  CD2 A LEU   A 160 ? 0.1551 0.2823 0.2452 0.0255  0.0389  0.0892  160 LEU   A CD2 
3538 C  CD2 B LEU   A 160 ? 0.2362 0.2946 0.2768 0.0402  0.0182  0.0370  160 LEU   A CD2 
3539 C  CD2 T LEU   A 160 ? 0.1982 0.2782 0.2429 0.0006  0.0489  0.0803  160 LEU   A CD2 
3572 N  N   A TYR   A 161 ? 0.1334 0.2705 0.2388 0.0140  0.0374  0.1136  161 TYR   A N   
3573 N  N   B TYR   A 161 ? 0.2070 0.2845 0.2221 0.0247  0.0388  0.0723  161 TYR   A N   
3574 C  CA  A TYR   A 161 ? 0.1393 0.2624 0.2282 0.0144  0.0326  0.1045  161 TYR   A CA  
3575 C  CA  B TYR   A 161 ? 0.2120 0.2786 0.2208 0.0092  0.0335  0.0685  161 TYR   A CA  
3576 C  C   A TYR   A 161 ? 0.1382 0.2823 0.2366 0.0133  0.0203  0.1074  161 TYR   A C   
3577 C  C   B TYR   A 161 ? 0.2243 0.2942 0.2417 -0.0000 0.0309  0.0584  161 TYR   A C   
3578 O  O   A TYR   A 161 ? 0.1198 0.2872 0.2324 0.0040  0.0192  0.1020  161 TYR   A O   
3579 O  O   B TYR   A 161 ? 0.2229 0.2954 0.2396 -0.0037 0.0274  0.0545  161 TYR   A O   
3580 C  CB  A TYR   A 161 ? 0.1526 0.2487 0.2347 0.0093  0.0410  0.0838  161 TYR   A CB  
3581 C  CB  B TYR   A 161 ? 0.2074 0.2616 0.2080 0.0026  0.0295  0.0692  161 TYR   A CB  
3582 C  CG  A TYR   A 161 ? 0.1438 0.2293 0.2407 0.0079  0.0295  0.0588  161 TYR   A CG  
3583 C  CG  B TYR   A 161 ? 0.1973 0.2448 0.2086 -0.0027 0.0205  0.0596  161 TYR   A CG  
3584 C  CD1 A TYR   A 161 ? 0.1441 0.2153 0.2496 0.0012  0.0259  0.0488  161 TYR   A CD1 
3585 C  CD1 B TYR   A 161 ? 0.1972 0.2423 0.2158 -0.0042 0.0118  0.0555  161 TYR   A CD1 
3586 C  CD2 A TYR   A 161 ? 0.1447 0.2222 0.2379 0.0159  0.0207  0.0497  161 TYR   A CD2 
3587 C  CD2 B TYR   A 161 ? 0.1925 0.2305 0.2100 -0.0039 0.0161  0.0550  161 TYR   A CD2 
3588 C  CE1 A TYR   A 161 ? 0.1448 0.1995 0.2390 0.0015  0.0242  0.0474  161 TYR   A CE1 
3589 C  CE1 B TYR   A 161 ? 0.1982 0.2372 0.2165 -0.0064 0.0094  0.0564  161 TYR   A CE1 
3590 C  CE2 A TYR   A 161 ? 0.1510 0.2146 0.2437 0.0030  0.0260  0.0530  161 TYR   A CE2 
3591 C  CE2 B TYR   A 161 ? 0.1910 0.2291 0.2138 -0.0033 0.0111  0.0510  161 TYR   A CE2 
3592 C  CZ  A TYR   A 161 ? 0.1541 0.2007 0.2356 -0.0066 0.0174  0.0564  161 TYR   A CZ  
3593 C  CZ  B TYR   A 161 ? 0.1993 0.2321 0.2211 -0.0066 0.0084  0.0579  161 TYR   A CZ  
3594 O  OH  A TYR   A 161 ? 0.1659 0.1923 0.2371 -0.0045 0.0122  0.0521  161 TYR   A OH  
3595 O  OH  B TYR   A 161 ? 0.2096 0.2325 0.2419 -0.0066 0.0051  0.0585  161 TYR   A OH  
3614 N  N   A ASP   A 162 ? 0.1345 0.2958 0.2373 0.0199  0.0373  0.1113  162 ASP   A N   
3615 N  N   B ASP   A 162 ? 0.2316 0.3059 0.2652 -0.0026 0.0427  0.0520  162 ASP   A N   
3616 C  CA  A ASP   A 162 ? 0.1308 0.3143 0.2439 0.0082  0.0384  0.0992  162 ASP   A CA  
3617 C  CA  B ASP   A 162 ? 0.2425 0.3142 0.2999 -0.0029 0.0427  0.0380  162 ASP   A CA  
3618 C  C   A ASP   A 162 ? 0.1195 0.3099 0.2280 0.0079  0.0235  0.0907  162 ASP   A C   
3619 C  C   B ASP   A 162 ? 0.2476 0.3100 0.3198 0.0001  0.0329  0.0180  162 ASP   A C   
3620 O  O   A ASP   A 162 ? 0.1176 0.3208 0.2307 0.0086  0.0212  0.0676  162 ASP   A O   
3621 O  O   B ASP   A 162 ? 0.2562 0.3170 0.3415 0.0003  0.0302  0.0144  162 ASP   A O   
3622 C  CB  A ASP   A 162 ? 0.1352 0.3330 0.2761 0.0087  0.0480  0.0899  162 ASP   A CB  
3623 C  CB  B ASP   A 162 ? 0.2445 0.3223 0.3108 -0.0061 0.0493  0.0481  162 ASP   A CB  
3624 C  CG  A ASP   A 162 ? 0.1489 0.3562 0.3073 0.0049  0.0671  0.0770  162 ASP   A CG  
3625 C  CG  B ASP   A 162 ? 0.2468 0.3289 0.3193 -0.0128 0.0614  0.0613  162 ASP   A CG  
3626 O  OD1 A ASP   A 162 ? 0.1595 0.3681 0.3164 0.0004  0.0732  0.0742  162 ASP   A OD1 
3627 O  OD1 B ASP   A 162 ? 0.2543 0.3323 0.3283 -0.0138 0.0605  0.0717  162 ASP   A OD1 
3628 O  OD2 A ASP   A 162 ? 0.1609 0.3630 0.3341 0.0154  0.0631  0.0648  162 ASP   A OD2 
3629 O  OD2 B ASP   A 162 ? 0.2400 0.3331 0.3126 -0.0199 0.0770  0.0663  162 ASP   A OD2 
3638 N  N   A LYS   A 163 ? 0.1335 0.3063 0.2426 0.0164  0.0111  0.0627  163 LYS   A N   
3639 N  N   B LYS   A 163 ? 0.2415 0.2967 0.3039 0.0039  0.0253  0.0133  163 LYS   A N   
3640 C  CA  A LYS   A 163 ? 0.1550 0.3021 0.2551 0.0151  -0.0044 0.0343  163 LYS   A CA  
3641 C  CA  B LYS   A 163 ? 0.2321 0.2817 0.2844 0.0048  0.0159  0.0078  163 LYS   A CA  
3642 C  C   A LYS   A 163 ? 0.1539 0.2759 0.2387 0.0040  0.0130  0.0248  163 LYS   A C   
3643 C  C   B LYS   A 163 ? 0.2067 0.2506 0.2417 -0.0048 0.0126  -0.0011 163 LYS   A C   
3644 O  O   A LYS   A 163 ? 0.1432 0.2666 0.2476 -0.0144 0.0193  0.0148  163 LYS   A O   
3645 O  O   B LYS   A 163 ? 0.2046 0.2555 0.2455 -0.0081 0.0116  -0.0045 163 LYS   A O   
3646 C  CB  A LYS   A 163 ? 0.1936 0.3219 0.2932 0.0323  -0.0186 0.0269  163 LYS   A CB  
3647 C  CB  B LYS   A 163 ? 0.2537 0.2984 0.3149 0.0130  0.0108  0.0072  163 LYS   A CB  
3648 C  CG  A LYS   A 163 ? 0.2274 0.3381 0.3488 0.0347  -0.0152 0.0191  163 LYS   A CG  
3649 C  CG  B LYS   A 163 ? 0.2749 0.3129 0.3522 0.0147  0.0108  0.0070  163 LYS   A CG  
3650 C  CD  A LYS   A 163 ? 0.2524 0.3498 0.3970 0.0383  -0.0131 0.0194  163 LYS   A CD  
3651 C  CD  B LYS   A 163 ? 0.2917 0.3230 0.3858 0.0142  0.0108  0.0082  163 LYS   A CD  
3652 C  CE  A LYS   A 163 ? 0.2736 0.3584 0.4336 0.0370  -0.0071 0.0203  163 LYS   A CE  
3653 C  CE  B LYS   A 163 ? 0.3044 0.3310 0.4114 0.0113  0.0142  0.0114  163 LYS   A CE  
3654 N  NZ  A LYS   A 163 ? 0.2855 0.3636 0.4547 0.0329  -0.0040 0.0234  163 LYS   A NZ  
3655 N  NZ  B LYS   A 163 ? 0.3129 0.3366 0.4292 0.0085  0.0148  0.0123  163 LYS   A NZ  
3682 N  N   A LEU   A 164 ? 0.1455 0.2454 0.2136 -0.0025 0.0251  0.0219  164 LEU   A N   
3683 N  N   B LEU   A 164 ? 0.1811 0.2232 0.2088 -0.0132 0.0135  0.0013  164 LEU   A N   
3684 C  CA  A LEU   A 164 ? 0.1550 0.2215 0.2043 -0.0149 0.0309  0.0169  164 LEU   A CA  
3685 C  CA  B LEU   A 164 ? 0.1695 0.2025 0.1957 -0.0154 0.0234  0.0034  164 LEU   A CA  
3686 C  C   A LEU   A 164 ? 0.1647 0.2177 0.2102 -0.0171 0.0304  0.0085  164 LEU   A C   
3687 C  C   B LEU   A 164 ? 0.1660 0.1974 0.1952 -0.0186 0.0270  0.0046  164 LEU   A C   
3688 O  O   A LEU   A 164 ? 0.1672 0.2125 0.2204 -0.0197 0.0410  0.0047  164 LEU   A O   
3689 O  O   B LEU   A 164 ? 0.1679 0.1971 0.1949 -0.0173 0.0448  -0.0104 164 LEU   A O   
3690 C  CB  A LEU   A 164 ? 0.1536 0.2042 0.1989 -0.0136 0.0385  0.0137  164 LEU   A CB  
3691 C  CB  B LEU   A 164 ? 0.1723 0.1937 0.1943 -0.0219 0.0217  0.0061  164 LEU   A CB  
3692 C  CG  A LEU   A 164 ? 0.1647 0.1924 0.2053 -0.0052 0.0341  0.0162  164 LEU   A CG  
3693 C  CG  B LEU   A 164 ? 0.1759 0.1931 0.2024 -0.0193 0.0137  -0.0071 164 LEU   A CG  
3694 C  CD1 A LEU   A 164 ? 0.1572 0.1843 0.2022 0.0024  0.0307  0.0186  164 LEU   A CD1 
3695 C  CD1 B LEU   A 164 ? 0.1779 0.1944 0.2133 -0.0196 0.0090  -0.0093 164 LEU   A CD1 
3696 C  CD2 A LEU   A 164 ? 0.1763 0.1921 0.2071 -0.0122 0.0501  0.0055  164 LEU   A CD2 
3697 C  CD2 B LEU   A 164 ? 0.1801 0.1965 0.2079 -0.0137 0.0086  -0.0203 164 LEU   A CD2 
3720 N  N   A VAL   A 165 ? 0.1537 0.2221 0.2039 -0.0236 0.0261  0.0146  165 VAL   A N   
3721 N  N   B VAL   A 165 ? 0.1585 0.1961 0.1938 -0.0172 0.0254  0.0130  165 VAL   A N   
3722 C  CA  A VAL   A 165 ? 0.1662 0.2318 0.2000 -0.0184 0.0293  0.0194  165 VAL   A CA  
3723 C  CA  B VAL   A 165 ? 0.1599 0.2018 0.1792 -0.0162 0.0287  0.0168  165 VAL   A CA  
3724 C  C   A VAL   A 165 ? 0.1573 0.2305 0.2069 -0.0118 0.0314  0.0170  165 VAL   A C   
3725 C  C   B VAL   A 165 ? 0.1588 0.2052 0.1876 -0.0118 0.0212  0.0147  165 VAL   A C   
3726 O  O   A VAL   A 165 ? 0.1523 0.2269 0.2109 -0.0131 0.0311  0.0143  165 VAL   A O   
3727 O  O   B VAL   A 165 ? 0.1525 0.2034 0.1849 -0.0080 0.0356  0.0110  165 VAL   A O   
3728 C  CB  A VAL   A 165 ? 0.1891 0.2471 0.2006 -0.0192 0.0314  0.0192  165 VAL   A CB  
3729 C  CB  B VAL   A 165 ? 0.1672 0.2088 0.1857 -0.0169 0.0295  0.0115  165 VAL   A CB  
3730 C  CG1 A VAL   A 165 ? 0.1945 0.2532 0.2070 -0.0170 0.0414  0.0133  165 VAL   A CG1 
3731 C  CG1 B VAL   A 165 ? 0.1661 0.2128 0.1943 -0.0179 0.0382  0.0131  165 VAL   A CG1 
3732 C  CG2 A VAL   A 165 ? 0.1992 0.2572 0.1926 -0.0173 0.0205  0.0226  165 VAL   A CG2 
3733 C  CG2 B VAL   A 165 ? 0.1759 0.2178 0.1909 -0.0146 0.0255  0.0133  165 VAL   A CG2 
3752 N  N   A SER   A 166 ? 0.1442 0.2358 0.2183 -0.0114 0.0324  0.0238  166 SER   A N   
3753 N  N   B SER   A 166 ? 0.1605 0.2068 0.1957 -0.0105 0.0057  0.0122  166 SER   A N   
3754 C  CA  A SER   A 166 ? 0.1486 0.2426 0.2326 -0.0160 0.0273  0.0203  166 SER   A CA  
3755 C  CA  B SER   A 166 ? 0.1658 0.2155 0.2174 -0.0119 -0.0020 0.0129  166 SER   A CA  
3756 C  C   A SER   A 166 ? 0.1507 0.2425 0.2360 -0.0074 0.0020  0.0112  166 SER   A C   
3757 C  C   B SER   A 166 ? 0.1675 0.2118 0.2246 -0.0215 0.0041  0.0165  166 SER   A C   
3758 O  O   A SER   A 166 ? 0.1722 0.2507 0.2694 -0.0118 0.0004  -0.0003 166 SER   A O   
3759 O  O   B SER   A 166 ? 0.1676 0.1979 0.2445 -0.0359 0.0142  0.0200  166 SER   A O   
3760 C  CB  A SER   A 166 ? 0.1576 0.2534 0.2575 -0.0103 0.0181  0.0188  166 SER   A CB  
3761 C  CB  B SER   A 166 ? 0.1748 0.2330 0.2351 -0.0103 -0.0057 0.0136  166 SER   A CB  
3762 O  OG  A SER   A 166 ? 0.1856 0.2739 0.2835 -0.0052 0.0094  0.0240  166 SER   A OG  
3763 O  OG  B SER   A 166 ? 0.1806 0.2472 0.2553 -0.0078 -0.0067 0.0185  166 SER   A OG  
3774 N  N   A SER   A 167 ? 0.1497 0.2446 0.2111 0.0094  -0.0037 0.0172  167 SER   A N   
3775 N  N   B SER   A 167 ? 0.1742 0.2266 0.2141 -0.0172 0.0099  0.0182  167 SER   A N   
3776 C  CA  A SER   A 167 ? 0.1748 0.2452 0.2167 0.0124  -0.0047 0.0196  167 SER   A CA  
3777 C  CA  B SER   A 167 ? 0.1929 0.2425 0.2098 -0.0089 0.0152  0.0171  167 SER   A CA  
3778 C  C   A SER   A 167 ? 0.1806 0.2500 0.2261 0.0179  0.0177  0.0296  167 SER   A C   
3779 C  C   B SER   A 167 ? 0.1940 0.2602 0.2078 0.0031  0.0198  0.0175  167 SER   A C   
3780 O  O   A SER   A 167 ? 0.1983 0.2455 0.2288 0.0239  0.0070  0.0345  167 SER   A O   
3781 O  O   B SER   A 167 ? 0.1957 0.2625 0.2104 0.0098  0.0178  0.0157  167 SER   A O   
3782 C  CB  A SER   A 167 ? 0.1788 0.2433 0.2207 0.0113  0.0022  0.0225  167 SER   A CB  
3783 C  CB  B SER   A 167 ? 0.2045 0.2467 0.2138 -0.0111 0.0249  0.0109  167 SER   A CB  
3784 O  OG  A SER   A 167 ? 0.1865 0.2441 0.2294 0.0071  0.0160  0.0193  167 SER   A OG  
3785 O  OG  B SER   A 167 ? 0.2119 0.2482 0.2110 -0.0119 0.0411  0.0040  167 SER   A OG  
3796 N  N   A PHE   A 168 ? 0.1709 0.2612 0.2337 0.0251  0.0259  0.0367  168 PHE   A N   
3797 N  N   B PHE   A 168 ? 0.1991 0.2789 0.2163 0.0077  0.0189  0.0169  168 PHE   A N   
3798 C  CA  A PHE   A 168 ? 0.1640 0.2845 0.2386 0.0192  0.0322  0.0398  168 PHE   A CA  
3799 C  CA  B PHE   A 168 ? 0.2113 0.3013 0.2312 0.0061  0.0246  0.0217  168 PHE   A CA  
3800 C  C   A PHE   A 168 ? 0.1696 0.3065 0.2703 0.0176  0.0702  0.0293  168 PHE   A C   
3801 C  C   B PHE   A 168 ? 0.2413 0.3225 0.2758 0.0013  0.0231  0.0094  168 PHE   A C   
3802 O  O   A PHE   A 168 ? 0.1719 0.3102 0.3186 0.0101  0.0718  0.0320  168 PHE   A O   
3803 O  O   B PHE   A 168 ? 0.2390 0.3203 0.2893 0.0046  0.0174  0.0082  168 PHE   A O   
3804 C  CB  A PHE   A 168 ? 0.1603 0.2878 0.2137 0.0080  0.0143  0.0400  168 PHE   A CB  
3805 C  CB  B PHE   A 168 ? 0.2032 0.3035 0.2195 0.0031  0.0323  0.0381  168 PHE   A CB  
3806 C  CG  A PHE   A 168 ? 0.1539 0.2909 0.1892 -0.0033 0.0089  0.0406  168 PHE   A CG  
3807 C  CG  B PHE   A 168 ? 0.1978 0.3058 0.2230 0.0031  0.0322  0.0547  168 PHE   A CG  
3808 C  CD1 A PHE   A 168 ? 0.1534 0.2972 0.1880 -0.0120 0.0090  0.0414  168 PHE   A CD1 
3809 C  CD1 B PHE   A 168 ? 0.1953 0.3084 0.2243 0.0041  0.0362  0.0630  168 PHE   A CD1 
3810 C  CD2 A PHE   A 168 ? 0.1499 0.2914 0.1886 -0.0103 0.0198  0.0395  168 PHE   A CD2 
3811 C  CD2 B PHE   A 168 ? 0.1973 0.3049 0.2304 0.0055  0.0219  0.0613  168 PHE   A CD2 
3812 C  CE1 A PHE   A 168 ? 0.1436 0.2942 0.1848 -0.0171 0.0040  0.0387  168 PHE   A CE1 
3813 C  CE1 B PHE   A 168 ? 0.1950 0.3089 0.2298 0.0060  0.0310  0.0675  168 PHE   A CE1 
3814 C  CE2 A PHE   A 168 ? 0.1561 0.2880 0.1937 -0.0124 0.0123  0.0399  168 PHE   A CE2 
3815 C  CE2 B PHE   A 168 ? 0.1993 0.3052 0.2356 0.0083  0.0160  0.0673  168 PHE   A CE2 
3816 C  CZ  A PHE   A 168 ? 0.1467 0.2906 0.1899 -0.0171 0.0045  0.0378  168 PHE   A CZ  
3817 C  CZ  B PHE   A 168 ? 0.1980 0.3067 0.2355 0.0065  0.0231  0.0674  168 PHE   A CZ  
3836 N  N   A LEU   A 169 ? 0.2110 0.3219 0.3001 0.0085  0.0753  0.0168  169 LEU   A N   
3837 N  N   B LEU   A 169 ? 0.2743 0.3479 0.3210 -0.0075 0.0244  -0.0013 169 LEU   A N   
3838 C  CA  A LEU   A 169 ? 0.2663 0.3386 0.3649 0.0134  0.0301  0.0175  169 LEU   A CA  
3839 C  CA  B LEU   A 169 ? 0.3197 0.3752 0.3850 -0.0155 0.0228  -0.0097 169 LEU   A CA  
3840 C  C   A LEU   A 169 ? 0.2724 0.3358 0.3886 0.0124  0.0125  0.0386  169 LEU   A C   
3841 C  C   B LEU   A 169 ? 0.3373 0.3862 0.4089 -0.0176 0.0260  -0.0099 169 LEU   A C   
3842 O  O   A LEU   A 169 ? 0.2778 0.3392 0.3996 0.0158  -0.0009 0.0337  169 LEU   A O   
3843 O  O   B LEU   A 169 ? 0.3451 0.3886 0.4147 -0.0186 0.0268  -0.0108 169 LEU   A O   
3844 C  CB  A LEU   A 169 ? 0.3025 0.3556 0.3899 0.0108  0.0031  -0.0038 169 LEU   A CB  
3845 C  CB  B LEU   A 169 ? 0.3435 0.3883 0.4127 -0.0196 0.0221  -0.0164 169 LEU   A CB  
3846 C  CG  A LEU   A 169 ? 0.3333 0.3707 0.4126 0.0066  -0.0154 -0.0271 169 LEU   A CG  
3847 C  CG  B LEU   A 169 ? 0.3614 0.3985 0.4329 -0.0214 0.0213  -0.0224 169 LEU   A CG  
3848 C  CD1 A LEU   A 169 ? 0.3461 0.3752 0.4221 0.0043  -0.0219 -0.0321 169 LEU   A CD1 
3849 C  CD1 B LEU   A 169 ? 0.3679 0.4022 0.4416 -0.0214 0.0199  -0.0249 169 LEU   A CD1 
3850 C  CD2 A LEU   A 169 ? 0.3437 0.3774 0.4171 0.0030  -0.0193 -0.0355 169 LEU   A CD2 
3851 C  CD2 B LEU   A 169 ? 0.3673 0.4021 0.4387 -0.0217 0.0224  -0.0236 169 LEU   A CD2 
3852 O  OXT A LEU   A 169 ? 0.2603 0.3318 0.3880 0.0056  0.0194  0.0507  169 LEU   A OXT 
3853 O  OXT B LEU   A 169 ? 0.3400 0.3902 0.4106 -0.0170 0.0292  -0.0097 169 LEU   A OXT 
3876 N  N   A SER   B 1   ? 0.3706 0.3650 0.3587 -0.1043 -0.0671 0.0177  1   SER   B N   
3877 N  N   B SER   B 1   ? 0.3437 0.3376 0.3465 -0.0837 -0.0472 0.0093  1   SER   B N   
3878 C  CA  A SER   B 1   ? 0.3618 0.3673 0.3608 -0.1114 -0.0744 0.0165  1   SER   B CA  
3879 C  CA  B SER   B 1   ? 0.3374 0.3402 0.3455 -0.0883 -0.0508 0.0092  1   SER   B CA  
3880 C  C   A SER   B 1   ? 0.3367 0.3692 0.3470 -0.1166 -0.0835 0.0359  1   SER   B C   
3881 C  C   B SER   B 1   ? 0.3209 0.3449 0.3373 -0.0899 -0.0591 0.0283  1   SER   B C   
3882 O  O   A SER   B 1   ? 0.3431 0.3729 0.3350 -0.1119 -0.0805 0.0339  1   SER   B O   
3883 O  O   B SER   B 1   ? 0.3250 0.3479 0.3317 -0.0877 -0.0556 0.0237  1   SER   B O   
3884 C  CB  A SER   B 1   ? 0.3751 0.3645 0.3755 -0.1115 -0.0663 0.0015  1   SER   B CB  
3885 C  CB  B SER   B 1   ? 0.3451 0.3356 0.3527 -0.0899 -0.0437 -0.0066 1   SER   B CB  
3886 O  OG  A SER   B 1   ? 0.3880 0.3709 0.4102 -0.1082 -0.0549 -0.0046 1   SER   B OG  
3887 O  OG  B SER   B 1   ? 0.3524 0.3376 0.3726 -0.0904 -0.0378 -0.0149 1   SER   B OG  
3902 N  N   A MET   B 2   ? 0.3149 0.3657 0.3445 -0.1212 -0.0811 0.0714  2   MET   B N   
3903 N  N   B MET   B 2   ? 0.3050 0.3451 0.3317 -0.0915 -0.0643 0.0614  2   MET   B N   
3904 C  CA  A MET   B 2   ? 0.3043 0.3689 0.3588 -0.1025 -0.0836 0.0950  2   MET   B CA  
3905 C  CA  B MET   B 2   ? 0.2935 0.3483 0.3342 -0.0823 -0.0731 0.0907  2   MET   B CA  
3906 C  C   A MET   B 2   ? 0.2727 0.3509 0.3269 -0.0837 -0.0969 0.1205  2   MET   B C   
3907 C  C   B MET   B 2   ? 0.2689 0.3358 0.3145 -0.0786 -0.0845 0.1169  2   MET   B C   
3908 O  O   A MET   B 2   ? 0.2694 0.3643 0.3278 -0.0720 -0.1142 0.1194  2   MET   B O   
3909 O  O   B MET   B 2   ? 0.2671 0.3422 0.3147 -0.0739 -0.0926 0.1148  2   MET   B O   
3910 C  CB  A MET   B 2   ? 0.3339 0.3962 0.4294 -0.0872 -0.0653 0.0785  2   MET   B CB  
3911 C  CB  B MET   B 2   ? 0.3109 0.3673 0.3705 -0.0685 -0.0658 0.0864  2   MET   B CB  
3912 C  CG  A MET   B 2   ? 0.3625 0.4205 0.4984 -0.0681 -0.0460 0.0680  2   MET   B CG  
3913 C  CG  B MET   B 2   ? 0.3266 0.3836 0.3991 -0.0531 -0.0584 0.0897  2   MET   B CG  
3914 S  SD  A MET   B 2   ? 0.3900 0.4439 0.5644 -0.0501 -0.0329 0.0600  2   MET   B SD  
3915 S  SD  B MET   B 2   ? 0.3415 0.4003 0.4202 -0.0383 -0.0557 0.0945  2   MET   B SD  
3916 C  CE  A MET   B 2   ? 0.3937 0.4476 0.5666 -0.0494 -0.0254 0.0608  2   MET   B CE  
3917 C  CE  B MET   B 2   ? 0.3437 0.4031 0.4298 -0.0372 -0.0521 0.0896  2   MET   B CE  
3936 N  N   . VAL   B 3   ? 0.2457 0.3122 0.3004 -0.0845 -0.0846 0.1431  3   VAL   B N   
3937 C  CA  . VAL   B 3   ? 0.2284 0.2702 0.3038 -0.0701 -0.0804 0.1275  3   VAL   B CA  
3938 C  C   . VAL   B 3   ? 0.2025 0.2532 0.2686 -0.0638 -0.0751 0.1103  3   VAL   B C   
3939 O  O   . VAL   B 3   ? 0.2022 0.2694 0.2775 -0.0663 -0.0744 0.1165  3   VAL   B O   
3940 C  CB  . VAL   B 3   ? 0.2374 0.2569 0.3529 -0.0712 -0.0747 0.1133  3   VAL   B CB  
3941 C  CG1 . VAL   B 3   ? 0.2440 0.2471 0.3716 -0.0726 -0.0736 0.1078  3   VAL   B CG1 
3942 C  CG2 . VAL   B 3   ? 0.2394 0.2626 0.3673 -0.0651 -0.0609 0.1206  3   VAL   B CG2 
3953 N  N   . ASN   B 4   ? 0.1881 0.2192 0.2403 -0.0593 -0.0666 0.0901  4   ASN   B N   
3954 C  CA  . ASN   B 4   ? 0.1938 0.2179 0.2085 -0.0563 -0.0549 0.0534  4   ASN   B CA  
3955 C  C   . ASN   B 4   ? 0.1959 0.2314 0.2044 -0.0587 -0.0471 0.0379  4   ASN   B C   
3956 O  O   . ASN   B 4   ? 0.1975 0.2365 0.2198 -0.0549 -0.0363 0.0233  4   ASN   B O   
3957 C  CB  . ASN   B 4   ? 0.1959 0.2136 0.1846 -0.0502 -0.0702 0.0392  4   ASN   B CB  
3958 C  CG  . ASN   B 4   ? 0.1963 0.1935 0.1822 -0.0490 -0.0585 0.0344  4   ASN   B CG  
3959 O  OD1 . ASN   B 4   ? 0.1985 0.1826 0.1896 -0.0492 -0.0555 0.0346  4   ASN   B OD1 
3960 N  ND2 . ASN   B 4   ? 0.2171 0.1992 0.2029 -0.0243 -0.0360 0.0267  4   ASN   B ND2 
3967 N  N   . SER   B 5   ? 0.2101 0.2492 0.2069 -0.0608 -0.0419 0.0278  5   SER   B N   
3968 C  CA  . SER   B 5   ? 0.2416 0.2861 0.2295 -0.0532 -0.0200 0.0258  5   SER   B CA  
3969 C  C   . SER   B 5   ? 0.2652 0.2926 0.2614 -0.0738 0.0087  0.0308  5   SER   B C   
3970 O  O   . SER   B 5   ? 0.2828 0.2859 0.3192 -0.0676 0.0467  0.0243  5   SER   B O   
3971 C  CB  . SER   B 5   ? 0.2547 0.3061 0.2571 -0.0393 -0.0104 0.0349  5   SER   B CB  
3972 O  OG  . SER   B 5   ? 0.2799 0.3312 0.3110 -0.0241 -0.0090 0.0407  5   SER   B OG  
3978 N  N   . PHE   B 6   ? 0.2880 0.3179 0.2526 -0.0828 0.0212  0.0441  6   PHE   B N   
3979 C  CA  . PHE   B 6   ? 0.3024 0.3263 0.2324 -0.1047 0.0271  0.0281  6   PHE   B CA  
3980 C  C   . PHE   B 6   ? 0.3613 0.3621 0.2866 -0.1108 0.0604  -0.0019 6   PHE   B C   
3981 O  O   . PHE   B 6   ? 0.3732 0.3915 0.3153 -0.1008 0.0510  -0.0117 6   PHE   B O   
3982 C  CB  . PHE   B 6   ? 0.2685 0.3049 0.2131 -0.0981 -0.0000 0.0260  6   PHE   B CB  
3983 C  CG  . PHE   B 6   ? 0.2330 0.2705 0.2074 -0.0938 -0.0159 0.0273  6   PHE   B CG  
3984 C  CD1 . PHE   B 6   ? 0.2340 0.2427 0.1962 -0.0862 -0.0270 0.0238  6   PHE   B CD1 
3985 C  CD2 . PHE   B 6   ? 0.2109 0.2667 0.2035 -0.0780 -0.0175 0.0528  6   PHE   B CD2 
3986 C  CE1 . PHE   B 6   ? 0.2321 0.2179 0.1913 -0.0768 -0.0335 0.0234  6   PHE   B CE1 
3987 C  CE2 . PHE   B 6   ? 0.2148 0.2492 0.2261 -0.0681 -0.0118 0.0510  6   PHE   B CE2 
3988 C  CZ  . PHE   B 6   ? 0.2227 0.2253 0.2148 -0.0704 -0.0234 0.0326  6   PHE   B CZ  
3998 N  N   A SER   B 7   ? 0.3872 0.3535 0.3001 -0.1241 0.0832  -0.0189 7   SER   B N   
3999 N  N   B SER   B 7   ? 0.3831 0.3599 0.3127 -0.1192 0.0770  -0.0138 7   SER   B N   
4000 C  CA  A SER   B 7   ? 0.4113 0.3587 0.3399 -0.1239 0.0986  -0.0249 7   SER   B CA  
4001 C  CA  B SER   B 7   ? 0.4031 0.3624 0.3502 -0.1198 0.0889  -0.0210 7   SER   B CA  
4002 C  C   A SER   B 7   ? 0.4119 0.3483 0.3268 -0.1283 0.1073  -0.0394 7   SER   B C   
4003 C  C   B SER   B 7   ? 0.4085 0.3529 0.3386 -0.1227 0.0997  -0.0358 7   SER   B C   
4004 O  O   A SER   B 7   ? 0.4179 0.3465 0.3330 -0.1340 0.1066  -0.0430 7   SER   B O   
4005 O  O   B SER   B 7   ? 0.4132 0.3528 0.3459 -0.1254 0.0976  -0.0369 7   SER   B O   
4006 C  CB  A SER   B 7   ? 0.4268 0.3714 0.3902 -0.1191 0.1063  -0.0165 7   SER   B CB  
4007 C  CB  B SER   B 7   ? 0.4127 0.3705 0.3932 -0.1170 0.0902  -0.0144 7   SER   B CB  
4008 O  OG  A SER   B 7   ? 0.4367 0.3818 0.4299 -0.1154 0.1073  -0.0119 7   SER   B OG  
4009 O  OG  B SER   B 7   ? 0.4186 0.3761 0.4237 -0.1154 0.0893  -0.0104 7   SER   B OG  
4020 N  N   . GLY   B 8   ? 0.4108 0.3435 0.3246 -0.1179 0.1077  -0.0499 8   GLY   B N   
4021 C  CA  . GLY   B 8   ? 0.4004 0.3233 0.3145 -0.1108 0.1142  -0.0637 8   GLY   B CA  
4022 C  C   . GLY   B 8   ? 0.3844 0.2923 0.3014 -0.1105 0.1196  -0.0630 8   GLY   B C   
4023 O  O   . GLY   B 8   ? 0.3956 0.2980 0.3320 -0.1014 0.1218  -0.0730 8   GLY   B O   
4028 N  N   . TYR   B 9   ? 0.3700 0.2667 0.2790 -0.1023 0.0936  -0.0715 9   TYR   B N   
4029 C  CA  . TYR   B 9   ? 0.3543 0.2348 0.2522 -0.0931 0.0678  -0.0592 9   TYR   B CA  
4030 C  C   . TYR   B 9   ? 0.3496 0.2306 0.2455 -0.0864 0.0404  -0.0447 9   TYR   B C   
4031 O  O   . TYR   B 9   ? 0.3581 0.2488 0.2822 -0.0848 0.0457  -0.0386 9   TYR   B O   
4032 C  CB  . TYR   B 9   ? 0.3494 0.2139 0.2604 -0.0843 0.0633  -0.0571 9   TYR   B CB  
4033 C  CG  . TYR   B 9   ? 0.3407 0.1953 0.2634 -0.0914 0.0566  -0.0584 9   TYR   B CG  
4034 C  CD1 . TYR   B 9   ? 0.3431 0.1933 0.2753 -0.1009 0.0596  -0.0506 9   TYR   B CD1 
4035 C  CD2 . TYR   B 9   ? 0.3273 0.1921 0.2536 -0.0843 0.0546  -0.0574 9   TYR   B CD2 
4036 C  CE1 . TYR   B 9   ? 0.3380 0.2021 0.2730 -0.1000 0.0690  -0.0599 9   TYR   B CE1 
4037 C  CE2 . TYR   B 9   ? 0.3259 0.1908 0.2548 -0.0846 0.0602  -0.0551 9   TYR   B CE2 
4038 C  CZ  . TYR   B 9   ? 0.3291 0.2056 0.2660 -0.0924 0.0679  -0.0665 9   TYR   B CZ  
4039 O  OH  . TYR   B 9   ? 0.3232 0.2168 0.2773 -0.0977 0.0717  -0.0779 9   TYR   B OH  
4049 N  N   . LEU   B 10  ? 0.3360 0.2054 0.2290 -0.0869 0.0130  -0.0432 10  LEU   B N   
4050 C  CA  . LEU   B 10  ? 0.3332 0.2051 0.2294 -0.0956 -0.0210 -0.0362 10  LEU   B CA  
4051 C  C   . LEU   B 10  ? 0.3148 0.2040 0.2338 -0.0916 -0.0385 -0.0248 10  LEU   B C   
4052 O  O   . LEU   B 10  ? 0.2944 0.2044 0.2337 -0.0798 -0.0330 -0.0123 10  LEU   B O   
4053 C  CB  . LEU   B 10  ? 0.3505 0.2014 0.2457 -0.0962 -0.0350 -0.0216 10  LEU   B CB  
4054 C  CG  . LEU   B 10  ? 0.3673 0.2087 0.2789 -0.0898 -0.0583 -0.0115 10  LEU   B CG  
4055 C  CD1 . LEU   B 10  ? 0.3783 0.2176 0.2953 -0.0834 -0.0545 -0.0085 10  LEU   B CD1 
4056 C  CD2 . LEU   B 10  ? 0.3740 0.2117 0.3052 -0.0866 -0.0564 0.0099  10  LEU   B CD2 
4068 N  N   . LYS   B 11  ? 0.3263 0.2263 0.2353 -0.0884 -0.0498 -0.0174 11  LYS   B N   
4069 C  CA  . LYS   B 11  ? 0.3435 0.2532 0.2747 -0.0714 -0.0579 -0.0228 11  LYS   B CA  
4070 C  C   . LYS   B 11  ? 0.3208 0.2322 0.2737 -0.0857 -0.0624 -0.0334 11  LYS   B C   
4071 O  O   . LYS   B 11  ? 0.3355 0.2468 0.3018 -0.0989 -0.0594 -0.0630 11  LYS   B O   
4072 C  CB  . LYS   B 11  ? 0.3767 0.3046 0.3433 -0.0487 -0.0569 -0.0285 11  LYS   B CB  
4073 C  CG  . LYS   B 11  ? 0.4045 0.3380 0.4145 -0.0344 -0.0557 -0.0340 11  LYS   B CG  
4074 C  CD  . LYS   B 11  ? 0.4256 0.3609 0.4800 -0.0243 -0.0513 -0.0381 11  LYS   B CD  
4075 C  CE  . LYS   B 11  ? 0.4397 0.3770 0.5262 -0.0196 -0.0488 -0.0422 11  LYS   B CE  
4076 N  NZ  . LYS   B 11  ? 0.4479 0.3864 0.5513 -0.0171 -0.0494 -0.0421 11  LYS   B NZ  
4090 N  N   . LEU   B 12  ? 0.2792 0.2112 0.2751 -0.0778 -0.0640 -0.0342 12  LEU   B N   
4091 C  CA  . LEU   B 12  ? 0.2610 0.1904 0.2891 -0.0674 -0.0517 -0.0273 12  LEU   B CA  
4092 C  C   . LEU   B 12  ? 0.2475 0.1901 0.2975 -0.0677 -0.0614 -0.0183 12  LEU   B C   
4093 O  O   . LEU   B 12  ? 0.2428 0.1891 0.3113 -0.0734 -0.0730 -0.0143 12  LEU   B O   
4094 C  CB  . LEU   B 12  ? 0.2569 0.1696 0.2842 -0.0501 -0.0452 -0.0213 12  LEU   B CB  
4095 C  CG  . LEU   B 12  ? 0.2575 0.1631 0.2789 -0.0478 -0.0350 -0.0077 12  LEU   B CG  
4096 C  CD1 . LEU   B 12  ? 0.2673 0.1660 0.2761 -0.0347 -0.0385 0.0098  12  LEU   B CD1 
4097 C  CD2 . LEU   B 12  ? 0.2596 0.1681 0.2836 -0.0501 -0.0251 -0.0100 12  LEU   B CD2 
4109 N  N   . THR   B 13  ? 0.2378 0.1963 0.2990 -0.0697 -0.0649 -0.0301 13  THR   B N   
4110 C  CA  . THR   B 13  ? 0.2319 0.2065 0.2920 -0.0745 -0.0768 -0.0095 13  THR   B CA  
4111 C  C   . THR   B 13  ? 0.2731 0.2275 0.3077 -0.0792 -0.0904 -0.0070 13  THR   B C   
4112 O  O   . THR   B 13  ? 0.2926 0.2244 0.3217 -0.0747 -0.0635 -0.0033 13  THR   B O   
4113 C  CB  . THR   B 13  ? 0.2108 0.2082 0.2976 -0.0633 -0.0744 -0.0008 13  THR   B CB  
4114 O  OG1 . THR   B 13  ? 0.1970 0.2010 0.3058 -0.0526 -0.0608 -0.0046 13  THR   B OG1 
4115 C  CG2 . THR   B 13  ? 0.2195 0.2154 0.3053 -0.0590 -0.0646 0.0064  13  THR   B CG2 
4123 N  N   A ASP   B 14  ? 0.2885 0.2414 0.3185 -0.0801 -0.1132 0.0024  14  ASP   B N   
4124 N  N   B ASP   B 14  ? 0.2849 0.2388 0.3153 -0.0765 -0.0962 0.0003  14  ASP   B N   
4125 C  CA  A ASP   B 14  ? 0.2979 0.2542 0.3400 -0.0804 -0.1178 0.0181  14  ASP   B CA  
4126 C  CA  B ASP   B 14  ? 0.2925 0.2485 0.3304 -0.0738 -0.0931 0.0108  14  ASP   B CA  
4127 C  C   A ASP   B 14  ? 0.2866 0.2357 0.3037 -0.0824 -0.1058 0.0245  14  ASP   B C   
4128 C  C   B ASP   B 14  ? 0.2797 0.2302 0.2989 -0.0762 -0.0958 0.0160  14  ASP   B C   
4129 O  O   A ASP   B 14  ? 0.3106 0.2480 0.3049 -0.0817 -0.0990 0.0366  14  ASP   B O   
4130 O  O   B ASP   B 14  ? 0.2946 0.2336 0.2963 -0.0756 -0.0935 0.0187  14  ASP   B O   
4131 C  CB  A ASP   B 14  ? 0.3173 0.2867 0.4087 -0.0750 -0.1258 0.0152  14  ASP   B CB  
4132 C  CB  B ASP   B 14  ? 0.3111 0.2762 0.3835 -0.0662 -0.0842 0.0103  14  ASP   B CB  
4133 C  CG  A ASP   B 14  ? 0.3403 0.3154 0.4800 -0.0674 -0.1159 0.0023  14  ASP   B CG  
4134 C  CG  B ASP   B 14  ? 0.3298 0.3001 0.4346 -0.0573 -0.0713 0.0034  14  ASP   B CG  
4135 O  OD1 A ASP   B 14  ? 0.3520 0.3231 0.4998 -0.0693 -0.1134 -0.0100 14  ASP   B OD1 
4136 O  OD1 B ASP   B 14  ? 0.3375 0.3088 0.4487 -0.0540 -0.0656 -0.0020 14  ASP   B OD1 
4137 O  OD2 A ASP   B 14  ? 0.3449 0.3283 0.5110 -0.0644 -0.1084 0.0050  14  ASP   B OD2 
4138 O  OD2 B ASP   B 14  ? 0.3348 0.3088 0.4555 -0.0570 -0.0668 0.0039  14  ASP   B OD2 
4147 N  N   . ASN   B 15  ? 0.2534 0.2094 0.2854 -0.0704 -0.1003 0.0188  15  ASN   B N   
4148 C  CA  . ASN   B 15  ? 0.2089 0.1774 0.2721 -0.0501 -0.0809 0.0091  15  ASN   B CA  
4149 C  C   . ASN   B 15  ? 0.1891 0.1629 0.2519 -0.0318 -0.0691 0.0057  15  ASN   B C   
4150 O  O   . ASN   B 15  ? 0.1847 0.1568 0.2569 -0.0297 -0.0665 -0.0089 15  ASN   B O   
4151 C  CB  . ASN   B 15  ? 0.2022 0.1688 0.2840 -0.0327 -0.0791 0.0124  15  ASN   B CB  
4152 C  CG  . ASN   B 15  ? 0.1822 0.1675 0.2999 -0.0356 -0.0489 0.0217  15  ASN   B CG  
4153 O  OD1 . ASN   B 15  ? 0.1831 0.1971 0.3285 -0.0504 -0.0523 0.0277  15  ASN   B OD1 
4154 N  ND2 . ASN   B 15  ? 0.1799 0.1480 0.2879 -0.0250 -0.0241 0.0049  15  ASN   B ND2 
4162 N  N   . VAL   B 16  ? 0.1911 0.1524 0.2498 -0.0389 -0.0664 0.0030  16  VAL   B N   
4163 C  CA  . VAL   B 16  ? 0.1909 0.1561 0.2399 -0.0356 -0.0546 -0.0184 16  VAL   B CA  
4164 C  C   . VAL   B 16  ? 0.1861 0.1708 0.2383 -0.0441 -0.0516 -0.0084 16  VAL   B C   
4165 O  O   . VAL   B 16  ? 0.1914 0.1813 0.2544 -0.0463 -0.0483 -0.0172 16  VAL   B O   
4166 C  CB  . VAL   B 16  ? 0.1904 0.1541 0.2486 -0.0214 -0.0403 -0.0133 16  VAL   B CB  
4167 C  CG1 . VAL   B 16  ? 0.1990 0.1531 0.2362 -0.0095 -0.0339 -0.0012 16  VAL   B CG1 
4168 C  CG2 . VAL   B 16  ? 0.1901 0.1562 0.2695 -0.0120 -0.0304 -0.0136 16  VAL   B CG2 
4178 N  N   . TYR   B 17  ? 0.1944 0.1823 0.2357 -0.0411 -0.0459 -0.0201 17  TYR   B N   
4179 C  CA  . TYR   B 17  ? 0.2018 0.1961 0.2172 -0.0513 -0.0431 0.0059  17  TYR   B CA  
4180 C  C   . TYR   B 17  ? 0.1964 0.1645 0.2189 -0.0521 -0.0294 -0.0023 17  TYR   B C   
4181 O  O   . TYR   B 17  ? 0.1915 0.1668 0.2292 -0.0402 -0.0340 -0.0289 17  TYR   B O   
4182 C  CB  . TYR   B 17  ? 0.2363 0.2401 0.2439 -0.0399 -0.0492 0.0337  17  TYR   B CB  
4183 C  CG  . TYR   B 17  ? 0.2663 0.2906 0.2922 -0.0316 -0.0643 0.0472  17  TYR   B CG  
4184 C  CD1 . TYR   B 17  ? 0.2844 0.3090 0.3169 -0.0278 -0.0750 0.0561  17  TYR   B CD1 
4185 C  CD2 . TYR   B 17  ? 0.2861 0.3167 0.3225 -0.0212 -0.0721 0.0477  17  TYR   B CD2 
4186 C  CE1 . TYR   B 17  ? 0.3012 0.3342 0.3335 -0.0181 -0.0893 0.0528  17  TYR   B CE1 
4187 C  CE2 . TYR   B 17  ? 0.3025 0.3375 0.3390 -0.0089 -0.0896 0.0524  17  TYR   B CE2 
4188 C  CZ  . TYR   B 17  ? 0.3139 0.3472 0.3454 -0.0089 -0.0978 0.0530  17  TYR   B CZ  
4189 O  OH  . TYR   B 17  ? 0.3300 0.3645 0.3585 -0.0009 -0.1077 0.0545  17  TYR   B OH  
4199 N  N   . ILE   B 18  ? 0.2098 0.1663 0.2137 -0.0452 -0.0190 -0.0082 18  ILE   B N   
4200 C  CA  . ILE   B 18  ? 0.2140 0.1585 0.2107 -0.0506 -0.0141 -0.0247 18  ILE   B CA  
4201 C  C   . ILE   B 18  ? 0.2250 0.1639 0.2068 -0.0583 -0.0121 -0.0333 18  ILE   B C   
4202 O  O   . ILE   B 18  ? 0.2446 0.1799 0.2206 -0.0543 -0.0010 -0.0364 18  ILE   B O   
4203 C  CB  . ILE   B 18  ? 0.2182 0.1590 0.2193 -0.0530 -0.0160 -0.0139 18  ILE   B CB  
4204 C  CG1 . ILE   B 18  ? 0.2172 0.1647 0.2271 -0.0509 -0.0096 -0.0070 18  ILE   B CG1 
4205 C  CG2 . ILE   B 18  ? 0.2194 0.1680 0.2201 -0.0523 -0.0202 -0.0102 18  ILE   B CG2 
4206 C  CD1 . ILE   B 18  ? 0.2250 0.1940 0.2520 -0.0439 -0.0236 0.0191  18  ILE   B CD1 
4218 N  N   . LYS   B 19  ? 0.2262 0.1622 0.2218 -0.0348 0.0229  -0.0434 19  LYS   B N   
4219 C  CA  . LYS   B 19  ? 0.2359 0.1661 0.2434 -0.0355 0.0227  -0.0447 19  LYS   B CA  
4220 C  C   . LYS   B 19  ? 0.2154 0.1649 0.2649 -0.0304 0.0376  -0.0553 19  LYS   B C   
4221 O  O   . LYS   B 19  ? 0.2065 0.1697 0.2438 -0.0271 0.0291  -0.0419 19  LYS   B O   
4222 C  CB  . LYS   B 19  ? 0.2630 0.1834 0.2515 -0.0430 0.0374  -0.0375 19  LYS   B CB  
4223 C  CG  . LYS   B 19  ? 0.2945 0.2057 0.2802 -0.0508 0.0470  -0.0409 19  LYS   B CG  
4224 C  CD  . LYS   B 19  ? 0.3217 0.2333 0.2893 -0.0583 0.0611  -0.0383 19  LYS   B CD  
4225 C  CE  . LYS   B 19  ? 0.3480 0.2607 0.3076 -0.0574 0.0582  -0.0371 19  LYS   B CE  
4226 N  NZ  . LYS   B 19  ? 0.3643 0.2774 0.3142 -0.0620 0.0635  -0.0310 19  LYS   B NZ  
4240 N  N   . ASN   B 20  ? 0.2075 0.1771 0.2981 -0.0297 0.0428  -0.0717 20  ASN   B N   
4241 C  CA  . ASN   B 20  ? 0.2123 0.1910 0.3277 -0.0241 0.0447  -0.0896 20  ASN   B CA  
4242 C  C   . ASN   B 20  ? 0.2111 0.2076 0.3273 -0.0279 0.0565  -0.0970 20  ASN   B C   
4243 O  O   . ASN   B 20  ? 0.2312 0.2425 0.3388 -0.0417 0.0562  -0.0931 20  ASN   B O   
4244 C  CB  . ASN   B 20  ? 0.2397 0.1908 0.3587 -0.0041 0.0386  -0.0906 20  ASN   B CB  
4245 C  CG  . ASN   B 20  ? 0.2688 0.2005 0.3821 0.0261  0.0386  -0.0947 20  ASN   B CG  
4246 O  OD1 . ASN   B 20  ? 0.2985 0.2304 0.4055 0.0419  0.0337  -0.0957 20  ASN   B OD1 
4247 N  ND2 . ASN   B 20  ? 0.2611 0.2000 0.3755 0.0292  0.0306  -0.0904 20  ASN   B ND2 
4254 N  N   . ALA   B 21  ? 0.2117 0.1904 0.3280 -0.0301 0.0601  -0.0806 21  ALA   B N   
4255 C  CA  . ALA   B 21  ? 0.2178 0.1954 0.3314 -0.0379 0.0454  -0.0628 21  ALA   B CA  
4256 C  C   . ALA   B 21  ? 0.2145 0.1745 0.3092 -0.0270 0.0519  -0.0403 21  ALA   B C   
4257 O  O   . ALA   B 21  ? 0.2177 0.1641 0.3105 -0.0358 0.0433  -0.0354 21  ALA   B O   
4258 C  CB  . ALA   B 21  ? 0.2311 0.2213 0.3400 -0.0497 0.0459  -0.0475 21  ALA   B CB  
4264 N  N   . ASP   B 22  ? 0.2015 0.1691 0.2916 -0.0259 0.0382  -0.0296 22  ASP   B N   
4265 C  CA  . ASP   B 22  ? 0.1981 0.1598 0.2672 -0.0102 0.0280  -0.0258 22  ASP   B CA  
4266 C  C   . ASP   B 22  ? 0.1880 0.1563 0.2360 -0.0184 0.0166  -0.0101 22  ASP   B C   
4267 O  O   . ASP   B 22  ? 0.1933 0.1612 0.2374 -0.0157 0.0133  -0.0095 22  ASP   B O   
4268 C  CB  . ASP   B 22  ? 0.2011 0.1669 0.3068 -0.0058 0.0323  -0.0099 22  ASP   B CB  
4269 C  CG  . ASP   B 22  ? 0.2013 0.1916 0.3513 -0.0003 0.0111  -0.0114 22  ASP   B CG  
4270 O  OD1 . ASP   B 22  ? 0.2085 0.1869 0.3524 -0.0042 -0.0117 -0.0069 22  ASP   B OD1 
4271 O  OD2 . ASP   B 22  ? 0.2105 0.2198 0.4017 0.0130  -0.0077 -0.0236 22  ASP   B OD2 
4276 N  N   . ILE   B 23  ? 0.1869 0.1508 0.2212 -0.0103 0.0052  0.0138  23  ILE   B N   
4277 C  CA  . ILE   B 23  ? 0.1775 0.1491 0.2022 -0.0133 -0.0040 0.0091  23  ILE   B CA  
4278 C  C   . ILE   B 23  ? 0.1667 0.1468 0.1990 -0.0114 -0.0133 0.0060  23  ILE   B C   
4279 O  O   . ILE   B 23  ? 0.1634 0.1474 0.1819 -0.0110 -0.0106 0.0133  23  ILE   B O   
4280 C  CB  . ILE   B 23  ? 0.1737 0.1563 0.2093 -0.0208 0.0020  0.0177  23  ILE   B CB  
4281 C  CG1 . ILE   B 23  ? 0.1771 0.1666 0.2195 -0.0169 0.0042  0.0275  23  ILE   B CG1 
4282 C  CG2 . ILE   B 23  ? 0.1810 0.1749 0.2097 -0.0215 0.0057  0.0122  23  ILE   B CG2 
4283 C  CD1 . ILE   B 23  ? 0.1818 0.1825 0.2263 -0.0082 0.0084  0.0223  23  ILE   B CD1 
4295 N  N   . VAL   B 24  ? 0.1709 0.1487 0.2005 -0.0135 -0.0113 0.0004  24  VAL   B N   
4296 C  CA  . VAL   B 24  ? 0.1707 0.1570 0.2186 -0.0079 -0.0190 0.0016  24  VAL   B CA  
4297 C  C   . VAL   B 24  ? 0.1630 0.1587 0.2245 -0.0150 -0.0154 0.0040  24  VAL   B C   
4298 O  O   . VAL   B 24  ? 0.1654 0.1687 0.2376 -0.0135 -0.0106 0.0172  24  VAL   B O   
4299 C  CB  . VAL   B 24  ? 0.1766 0.1749 0.2249 -0.0011 -0.0233 0.0031  24  VAL   B CB  
4300 C  CG1 . VAL   B 24  ? 0.1723 0.1793 0.2520 -0.0119 -0.0312 0.0005  24  VAL   B CG1 
4301 C  CG2 . VAL   B 24  ? 0.1845 0.2016 0.2233 0.0040  -0.0283 -0.0069 24  VAL   B CG2 
4311 N  N   . GLU   B 25  ? 0.1868 0.1713 0.2326 -0.0167 -0.0062 -0.0014 25  GLU   B N   
4312 C  CA  . GLU   B 25  ? 0.2060 0.2027 0.2470 -0.0061 0.0081  -0.0066 25  GLU   B CA  
4313 C  C   . GLU   B 25  ? 0.1949 0.1952 0.2118 -0.0184 0.0104  0.0013  25  GLU   B C   
4314 O  O   . GLU   B 25  ? 0.2020 0.2090 0.2228 -0.0230 0.0120  0.0004  25  GLU   B O   
4315 C  CB  . GLU   B 25  ? 0.2583 0.2596 0.3230 0.0233  0.0172  -0.0103 25  GLU   B CB  
4316 C  CG  . GLU   B 25  ? 0.3059 0.3305 0.4408 0.0338  0.0090  -0.0128 25  GLU   B CG  
4317 C  CD  . GLU   B 25  ? 0.3656 0.3929 0.5375 0.0349  0.0016  -0.0154 25  GLU   B CD  
4318 O  OE1 . GLU   B 25  ? 0.3905 0.4142 0.5683 0.0388  0.0030  -0.0140 25  GLU   B OE1 
4319 O  OE2 . GLU   B 25  ? 0.3878 0.4109 0.5693 0.0353  -0.0035 -0.0207 25  GLU   B OE2 
4326 N  N   . GLU   B 26  ? 0.1873 0.1796 0.1988 -0.0345 0.0047  -0.0004 26  GLU   B N   
4327 C  CA  . GLU   B 26  ? 0.1871 0.1960 0.2046 -0.0439 -0.0123 -0.0019 26  GLU   B CA  
4328 C  C   . GLU   B 26  ? 0.1738 0.1916 0.1932 -0.0314 0.0003  0.0118  26  GLU   B C   
4329 O  O   . GLU   B 26  ? 0.1978 0.2103 0.1949 -0.0290 0.0005  0.0207  26  GLU   B O   
4330 C  CB  . GLU   B 26  ? 0.2210 0.2140 0.2164 -0.0506 -0.0031 0.0153  26  GLU   B CB  
4331 C  CG  . GLU   B 26  ? 0.2655 0.2576 0.2722 -0.0564 0.0147  -0.0060 26  GLU   B CG  
4332 C  CD  . GLU   B 26  ? 0.2891 0.2809 0.2815 -0.0793 0.0287  -0.0423 26  GLU   B CD  
4333 O  OE1 . GLU   B 26  ? 0.3144 0.2721 0.3002 -0.0928 0.0629  -0.0399 26  GLU   B OE1 
4334 O  OE2 . GLU   B 26  ? 0.2934 0.3203 0.3292 -0.0681 0.0247  -0.0356 26  GLU   B OE2 
4341 N  N   . ALA   B 27  ? 0.1596 0.1700 0.1950 -0.0208 0.0044  0.0199  27  ALA   B N   
4342 C  CA  . ALA   B 27  ? 0.1572 0.1734 0.2011 -0.0117 0.0003  0.0300  27  ALA   B CA  
4343 C  C   . ALA   B 27  ? 0.1603 0.1848 0.2272 -0.0153 0.0115  0.0457  27  ALA   B C   
4344 O  O   . ALA   B 27  ? 0.1702 0.1929 0.2404 -0.0062 0.0075  0.0446  27  ALA   B O   
4345 C  CB  . ALA   B 27  ? 0.1745 0.1602 0.2058 -0.0180 0.0015  0.0275  27  ALA   B CB  
4351 N  N   . LYS   B 28  ? 0.1571 0.2038 0.2592 -0.0248 0.0133  0.0595  28  LYS   B N   
4352 C  CA  . LYS   B 28  ? 0.1782 0.2436 0.2784 -0.0106 0.0464  0.0848  28  LYS   B CA  
4353 C  C   . LYS   B 28  ? 0.2050 0.2549 0.2731 -0.0069 0.0573  0.0798  28  LYS   B C   
4354 O  O   . LYS   B 28  ? 0.2272 0.2608 0.2875 -0.0087 0.0608  0.0774  28  LYS   B O   
4355 C  CB  . LYS   B 28  ? 0.2055 0.2825 0.3229 0.0008  0.0732  0.1024  28  LYS   B CB  
4356 C  CG  . LYS   B 28  ? 0.2396 0.3388 0.3662 0.0069  0.0838  0.1150  28  LYS   B CG  
4357 C  CD  . LYS   B 28  ? 0.2912 0.4035 0.4210 0.0119  0.1060  0.1188  28  LYS   B CD  
4358 C  CE  . LYS   B 28  ? 0.3325 0.4500 0.4736 0.0189  0.1144  0.1214  28  LYS   B CE  
4359 N  NZ  . LYS   B 28  ? 0.3684 0.4748 0.4987 0.0240  0.1152  0.1245  28  LYS   B NZ  
4373 N  N   . LYS   B 29  ? 0.2280 0.2782 0.2743 0.0082  0.0545  0.0674  29  LYS   B N   
4374 C  CA  . LYS   B 29  ? 0.2731 0.3139 0.3031 0.0076  0.0534  0.0600  29  LYS   B CA  
4375 C  C   . LYS   B 29  ? 0.2604 0.3104 0.2686 0.0054  0.0380  0.0695  29  LYS   B C   
4376 O  O   . LYS   B 29  ? 0.2787 0.3301 0.2828 0.0149  0.0410  0.0699  29  LYS   B O   
4377 C  CB  . LYS   B 29  ? 0.3393 0.3572 0.3874 0.0041  0.0564  0.0469  29  LYS   B CB  
4378 C  CG  . LYS   B 29  ? 0.3973 0.3953 0.4774 -0.0004 0.0601  0.0380  29  LYS   B CG  
4379 C  CD  . LYS   B 29  ? 0.4471 0.4233 0.5488 -0.0057 0.0689  0.0279  29  LYS   B CD  
4380 C  CE  . LYS   B 29  ? 0.4839 0.4430 0.5978 -0.0103 0.0775  0.0217  29  LYS   B CE  
4381 N  NZ  . LYS   B 29  ? 0.5005 0.4519 0.6263 -0.0125 0.0817  0.0184  29  LYS   B NZ  
4395 N  N   . VAL   B 30  ? 0.2253 0.2923 0.2512 -0.0105 0.0220  0.0658  30  VAL   B N   
4396 C  CA  . VAL   B 30  ? 0.2096 0.2825 0.2740 -0.0232 -0.0148 0.0662  30  VAL   B CA  
4397 C  C   . VAL   B 30  ? 0.1885 0.2725 0.2567 -0.0221 -0.0115 0.0842  30  VAL   B C   
4398 O  O   . VAL   B 30  ? 0.1998 0.2834 0.2623 -0.0160 -0.0095 0.0948  30  VAL   B O   
4399 C  CB  . VAL   B 30  ? 0.2141 0.2795 0.3086 -0.0433 -0.0364 0.0657  30  VAL   B CB  
4400 C  CG1 . VAL   B 30  ? 0.2228 0.2887 0.3101 -0.0428 -0.0266 0.0642  30  VAL   B CG1 
4401 C  CG2 . VAL   B 30  ? 0.2233 0.2777 0.3195 -0.0520 -0.0476 0.0563  30  VAL   B CG2 
4411 N  N   . LYS   B 31  ? 0.1829 0.2354 0.2798 -0.0351 -0.0137 0.0966  31  LYS   B N   
4412 C  CA  . LYS   B 31  ? 0.1700 0.2308 0.3133 -0.0449 -0.0197 0.0952  31  LYS   B CA  
4413 C  C   . LYS   B 31  ? 0.1598 0.1924 0.2815 -0.0381 -0.0330 0.0746  31  LYS   B C   
4414 O  O   . LYS   B 31  ? 0.1638 0.2055 0.2978 -0.0308 -0.0233 0.0881  31  LYS   B O   
4415 C  CB  . LYS   B 31  ? 0.1858 0.2837 0.3669 -0.0419 0.0094  0.1088  31  LYS   B CB  
4416 C  CG  . LYS   B 31  ? 0.2256 0.3379 0.4120 -0.0455 0.0262  0.1070  31  LYS   B CG  
4417 C  CD  . LYS   B 31  ? 0.2687 0.3950 0.4547 -0.0426 0.0226  0.0973  31  LYS   B CD  
4418 C  CE  . LYS   B 31  ? 0.2991 0.4327 0.4975 -0.0413 0.0151  0.0889  31  LYS   B CE  
4419 N  NZ  . LYS   B 31  ? 0.3181 0.4534 0.5146 -0.0340 0.0058  0.0799  31  LYS   B NZ  
4433 N  N   . PRO   B 32  ? 0.1774 0.1627 0.2315 -0.0362 -0.0481 0.0465  32  PRO   B N   
4434 C  CA  . PRO   B 32  ? 0.1885 0.1575 0.2005 -0.0387 -0.0469 0.0301  32  PRO   B CA  
4435 C  C   . PRO   B 32  ? 0.1970 0.1510 0.1894 -0.0381 -0.0619 0.0325  32  PRO   B C   
4436 O  O   . PRO   B 32  ? 0.2086 0.1510 0.2303 -0.0402 -0.0769 0.0326  32  PRO   B O   
4437 C  CB  . PRO   B 32  ? 0.2018 0.1490 0.2010 -0.0450 -0.0416 0.0218  32  PRO   B CB  
4438 C  CG  . PRO   B 32  ? 0.2203 0.1418 0.2010 -0.0308 -0.0562 0.0229  32  PRO   B CG  
4439 C  CD  . PRO   B 32  ? 0.2062 0.1481 0.2185 -0.0242 -0.0617 0.0255  32  PRO   B CD  
4447 N  N   . THR   B 33  ? 0.2010 0.1389 0.1805 -0.0334 -0.0603 0.0226  33  THR   B N   
4448 C  CA  . THR   B 33  ? 0.2127 0.1423 0.1839 -0.0348 -0.0536 0.0256  33  THR   B CA  
4449 C  C   . THR   B 33  ? 0.2156 0.1303 0.1731 -0.0342 -0.0555 0.0158  33  THR   B C   
4450 O  O   . THR   B 33  ? 0.2354 0.1336 0.1867 -0.0453 -0.0639 0.0151  33  THR   B O   
4451 C  CB  . THR   B 33  ? 0.2162 0.1533 0.1976 -0.0207 -0.0543 0.0328  33  THR   B CB  
4452 O  OG1 . THR   B 33  ? 0.1991 0.1615 0.2012 -0.0207 -0.0519 0.0375  33  THR   B OG1 
4453 C  CG2 . THR   B 33  ? 0.2404 0.1643 0.2237 -0.0163 -0.0489 0.0294  33  THR   B CG2 
4461 N  N   . VAL   B 34  ? 0.1993 0.1340 0.1707 -0.0375 -0.0467 0.0156  34  VAL   B N   
4462 C  CA  . VAL   B 34  ? 0.1802 0.1321 0.1738 -0.0344 -0.0433 0.0065  34  VAL   B CA  
4463 C  C   . VAL   B 34  ? 0.1604 0.1272 0.1550 -0.0303 -0.0280 0.0061  34  VAL   B C   
4464 O  O   . VAL   B 34  ? 0.1814 0.1320 0.1673 -0.0226 -0.0436 0.0118  34  VAL   B O   
4465 C  CB  . VAL   B 34  ? 0.1846 0.1437 0.2009 -0.0148 -0.0410 0.0106  34  VAL   B CB  
4466 C  CG1 . VAL   B 34  ? 0.1792 0.1590 0.2074 -0.0153 -0.0257 -0.0025 34  VAL   B CG1 
4467 C  CG2 . VAL   B 34  ? 0.1897 0.1506 0.2258 -0.0146 -0.0374 0.0099  34  VAL   B CG2 
4477 N  N   . VAL   B 35  ? 0.1514 0.1250 0.1434 -0.0245 -0.0189 0.0085  35  VAL   B N   
4478 C  CA  . VAL   B 35  ? 0.1464 0.1261 0.1422 -0.0239 -0.0119 0.0075  35  VAL   B CA  
4479 C  C   . VAL   B 35  ? 0.1402 0.1227 0.1448 -0.0181 -0.0197 0.0086  35  VAL   B C   
4480 O  O   . VAL   B 35  ? 0.1454 0.1247 0.1517 -0.0239 -0.0084 0.0004  35  VAL   B O   
4481 C  CB  . VAL   B 35  ? 0.1466 0.1465 0.1587 -0.0205 -0.0022 0.0063  35  VAL   B CB  
4482 C  CG1 . VAL   B 35  ? 0.1391 0.1548 0.1796 -0.0252 -0.0055 0.0025  35  VAL   B CG1 
4483 C  CG2 . VAL   B 35  ? 0.1499 0.1468 0.1723 -0.0100 -0.0029 -0.0010 35  VAL   B CG2 
4493 N  N   . VAL   B 36  ? 0.1384 0.1214 0.1489 -0.0200 -0.0177 0.0121  36  VAL   B N   
4494 C  CA  . VAL   B 36  ? 0.1326 0.1156 0.1426 -0.0159 -0.0064 0.0090  36  VAL   B CA  
4495 C  C   . VAL   B 36  ? 0.1332 0.1225 0.1377 -0.0143 -0.0082 0.0039  36  VAL   B C   
4496 O  O   . VAL   B 36  ? 0.1410 0.1329 0.1573 -0.0143 -0.0043 -0.0060 36  VAL   B O   
4497 C  CB  . VAL   B 36  ? 0.1346 0.1279 0.1600 -0.0156 -0.0073 0.0110  36  VAL   B CB  
4498 C  CG1 . VAL   B 36  ? 0.1350 0.1398 0.1711 -0.0203 -0.0040 0.0076  36  VAL   B CG1 
4499 C  CG2 . VAL   B 36  ? 0.1389 0.1309 0.1673 -0.0157 -0.0178 0.0101  36  VAL   B CG2 
4509 N  N   . ASN   B 37  ? 0.1354 0.1246 0.1431 -0.0037 -0.0141 0.0039  37  ASN   B N   
4510 C  CA  . ASN   B 37  ? 0.1343 0.1301 0.1586 -0.0061 -0.0171 0.0097  37  ASN   B CA  
4511 C  C   . ASN   B 37  ? 0.1319 0.1317 0.1597 -0.0016 -0.0113 0.0064  37  ASN   B C   
4512 O  O   . ASN   B 37  ? 0.1431 0.1408 0.1625 -0.0025 -0.0025 0.0123  37  ASN   B O   
4513 C  CB  . ASN   B 37  ? 0.1365 0.1341 0.1422 -0.0064 -0.0159 0.0044  37  ASN   B CB  
4514 C  CG  . ASN   B 37  ? 0.1420 0.1302 0.1574 -0.0054 -0.0134 0.0020  37  ASN   B CG  
4515 O  OD1 . ASN   B 37  ? 0.1533 0.1349 0.1726 0.0083  -0.0219 0.0007  37  ASN   B OD1 
4516 N  ND2 . ASN   B 37  ? 0.1446 0.1308 0.1562 -0.0028 -0.0184 0.0065  37  ASN   B ND2 
4523 N  N   . ALA   B 38  ? 0.1489 0.1243 0.1602 0.0072  -0.0023 0.0079  38  ALA   B N   
4524 C  CA  . ALA   B 38  ? 0.1630 0.1332 0.1578 -0.0030 0.0012  0.0149  38  ALA   B CA  
4525 C  C   . ALA   B 38  ? 0.1575 0.1318 0.1583 -0.0046 0.0060  0.0132  38  ALA   B C   
4526 O  O   . ALA   B 38  ? 0.1686 0.1435 0.1673 0.0064  -0.0022 0.0109  38  ALA   B O   
4527 C  CB  . ALA   B 38  ? 0.1864 0.1405 0.1701 -0.0129 0.0050  0.0153  38  ALA   B CB  
4533 N  N   . ALA   B 39  ? 0.1529 0.1297 0.1479 0.0067  -0.0086 0.0081  39  ALA   B N   
4534 C  CA  . ALA   B 39  ? 0.1600 0.1339 0.1510 0.0038  -0.0075 0.0097  39  ALA   B CA  
4535 C  C   . ALA   B 39  ? 0.1667 0.1402 0.1356 0.0078  -0.0068 0.0022  39  ALA   B C   
4536 O  O   . ALA   B 39  ? 0.1697 0.1469 0.1708 -0.0044 -0.0040 0.0078  39  ALA   B O   
4537 C  CB  . ALA   B 39  ? 0.1570 0.1384 0.1687 -0.0070 0.0013  0.0028  39  ALA   B CB  
4543 N  N   . ASN   B 40  ? 0.1664 0.1620 0.1364 -0.0002 0.0018  -0.0067 40  ASN   B N   
4544 C  CA  . ASN   B 40  ? 0.1758 0.1694 0.1516 0.0066  -0.0048 -0.0072 40  ASN   B CA  
4545 C  C   . ASN   B 40  ? 0.1826 0.1688 0.1470 0.0109  -0.0094 -0.0001 40  ASN   B C   
4546 O  O   . ASN   B 40  ? 0.1774 0.1610 0.1587 0.0108  -0.0125 0.0011  40  ASN   B O   
4547 C  CB  . ASN   B 40  ? 0.1903 0.1662 0.1770 0.0141  -0.0143 0.0132  40  ASN   B CB  
4548 C  CG  . ASN   B 40  ? 0.1949 0.1718 0.2041 0.0104  -0.0267 0.0177  40  ASN   B CG  
4549 O  OD1 . ASN   B 40  ? 0.1965 0.1682 0.2788 0.0098  -0.0368 0.0220  40  ASN   B OD1 
4550 N  ND2 . ASN   B 40  ? 0.1994 0.1708 0.1994 0.0064  -0.0184 0.0220  40  ASN   B ND2 
4557 N  N   . VAL   B 41  ? 0.1909 0.1708 0.1517 0.0164  0.0045  -0.0038 41  VAL   B N   
4558 C  CA  . VAL   B 41  ? 0.1981 0.1831 0.1508 0.0076  0.0032  -0.0016 41  VAL   B CA  
4559 C  C   . VAL   B 41  ? 0.1974 0.1813 0.1472 0.0144  -0.0008 -0.0044 41  VAL   B C   
4560 O  O   . VAL   B 41  ? 0.1904 0.1792 0.1608 0.0124  -0.0051 -0.0059 41  VAL   B O   
4561 C  CB  . VAL   B 41  ? 0.2174 0.2016 0.1762 -0.0067 0.0261  -0.0199 41  VAL   B CB  
4562 C  CG1 . VAL   B 41  ? 0.2178 0.2039 0.1983 -0.0138 0.0327  -0.0253 41  VAL   B CG1 
4563 C  CG2 . VAL   B 41  ? 0.2275 0.2192 0.1845 -0.0173 0.0248  -0.0151 41  VAL   B CG2 
4573 N  N   . TYR   B 42  ? 0.2043 0.1834 0.1480 0.0170  -0.0163 0.0023  42  TYR   B N   
4574 C  CA  . TYR   B 42  ? 0.2062 0.1867 0.1543 0.0228  -0.0220 -0.0143 42  TYR   B CA  
4575 C  C   . TYR   B 42  ? 0.1867 0.1702 0.1685 0.0234  -0.0215 -0.0091 42  TYR   B C   
4576 O  O   . TYR   B 42  ? 0.1855 0.1780 0.1997 0.0174  -0.0277 -0.0118 42  TYR   B O   
4577 C  CB  . TYR   B 42  ? 0.2238 0.2091 0.1705 0.0176  -0.0318 -0.0027 42  TYR   B CB  
4578 C  CG  . TYR   B 42  ? 0.2251 0.2186 0.1626 0.0035  -0.0280 0.0079  42  TYR   B CG  
4579 C  CD1 . TYR   B 42  ? 0.2160 0.2181 0.1458 -0.0064 -0.0146 0.0057  42  TYR   B CD1 
4580 C  CD2 . TYR   B 42  ? 0.2377 0.2271 0.1955 0.0031  -0.0122 0.0118  42  TYR   B CD2 
4581 C  CE1 . TYR   B 42  ? 0.2287 0.2266 0.1462 -0.0028 -0.0141 0.0065  42  TYR   B CE1 
4582 C  CE2 . TYR   B 42  ? 0.2388 0.2365 0.1862 0.0045  0.0106  0.0270  42  TYR   B CE2 
4583 C  CZ  . TYR   B 42  ? 0.2452 0.2418 0.1661 0.0157  0.0065  0.0081  42  TYR   B CZ  
4584 O  OH  . TYR   B 42  ? 0.2767 0.2653 0.2044 0.0290  0.0118  0.0151  42  TYR   B OH  
4594 N  N   . LEU   B 43  ? 0.1751 0.1568 0.1593 0.0117  -0.0146 -0.0127 43  LEU   B N   
4595 C  CA  . LEU   B 43  ? 0.1776 0.1580 0.1473 0.0032  -0.0206 -0.0054 43  LEU   B CA  
4596 C  C   . LEU   B 43  ? 0.1788 0.1563 0.1486 0.0058  -0.0141 0.0016  43  LEU   B C   
4597 O  O   . LEU   B 43  ? 0.1771 0.1584 0.1820 0.0072  -0.0200 0.0043  43  LEU   B O   
4598 C  CB  . LEU   B 43  ? 0.1752 0.1491 0.1548 -0.0032 -0.0238 -0.0085 43  LEU   B CB  
4599 C  CG  . LEU   B 43  ? 0.1771 0.1478 0.1712 -0.0010 -0.0313 -0.0056 43  LEU   B CG  
4600 C  CD1 . LEU   B 43  ? 0.1862 0.1543 0.2006 -0.0004 -0.0407 -0.0095 43  LEU   B CD1 
4601 C  CD2 . LEU   B 43  ? 0.1743 0.1507 0.1812 -0.0079 -0.0321 -0.0053 43  LEU   B CD2 
4613 N  N   . LYS   B 44  ? 0.1770 0.1578 0.1586 0.0135  -0.0125 -0.0049 44  LYS   B N   
4614 C  CA  . LYS   B 44  ? 0.1899 0.1667 0.1602 0.0113  -0.0152 0.0021  44  LYS   B CA  
4615 C  C   . LYS   B 44  ? 0.1800 0.1629 0.1536 0.0128  -0.0138 0.0001  44  LYS   B C   
4616 O  O   . LYS   B 44  ? 0.2040 0.1598 0.1879 0.0060  -0.0079 0.0004  44  LYS   B O   
4617 C  CB  . LYS   B 44  ? 0.2182 0.1900 0.1886 0.0206  -0.0315 -0.0048 44  LYS   B CB  
4618 C  CG  . LYS   B 44  ? 0.2540 0.2189 0.2185 0.0159  -0.0601 0.0058  44  LYS   B CG  
4619 C  CD  . LYS   B 44  ? 0.2896 0.2411 0.2783 0.0045  -0.0668 0.0048  44  LYS   B CD  
4620 C  CE  . LYS   B 44  ? 0.3201 0.2657 0.3267 -0.0013 -0.0724 0.0181  44  LYS   B CE  
4621 N  NZ  . LYS   B 44  ? 0.3277 0.2729 0.3509 -0.0011 -0.0799 0.0312  44  LYS   B NZ  
4635 N  N   . HIS   B 45  ? 0.1690 0.1635 0.1576 0.0057  -0.0132 0.0101  45  HIS   B N   
4636 C  CA  . HIS   B 45  ? 0.1721 0.1583 0.1638 0.0106  -0.0146 -0.0026 45  HIS   B CA  
4637 C  C   . HIS   B 45  ? 0.1923 0.1756 0.1957 0.0158  -0.0183 -0.0057 45  HIS   B C   
4638 O  O   . HIS   B 45  ? 0.2070 0.2057 0.2447 0.0412  0.0036  -0.0035 45  HIS   B O   
4639 C  CB  . HIS   B 45  ? 0.1662 0.1629 0.1657 -0.0002 -0.0133 -0.0025 45  HIS   B CB  
4640 C  CG  . HIS   B 45  ? 0.1654 0.1575 0.1672 0.0007  -0.0174 -0.0003 45  HIS   B CG  
4641 N  ND1 . HIS   B 45  ? 0.1728 0.1486 0.1671 0.0027  -0.0244 -0.0068 45  HIS   B ND1 
4642 C  CD2 . HIS   B 45  ? 0.1737 0.1614 0.1754 -0.0104 -0.0205 -0.0003 45  HIS   B CD2 
4643 C  CE1 . HIS   B 45  ? 0.1780 0.1413 0.1547 0.0011  -0.0281 -0.0082 45  HIS   B CE1 
4644 N  NE2 . HIS   B 45  ? 0.1804 0.1500 0.1613 -0.0022 -0.0222 -0.0035 45  HIS   B NE2 
4652 N  N   . GLY   B 46  ? 0.2082 0.1700 0.2301 0.0167  -0.0377 0.0014  46  GLY   B N   
4653 C  CA  . GLY   B 46  ? 0.2210 0.1888 0.2729 0.0118  -0.0495 0.0066  46  GLY   B CA  
4654 C  C   . GLY   B 46  ? 0.2140 0.2068 0.3125 0.0243  -0.0446 0.0132  46  GLY   B C   
4655 O  O   . GLY   B 46  ? 0.2214 0.2295 0.4073 0.0254  -0.0212 -0.0211 46  GLY   B O   
4659 N  N   . GLY   B 47  ? 0.2091 0.2141 0.2886 0.0097  -0.0206 0.0089  47  GLY   B N   
4660 C  CA  . GLY   B 47  ? 0.1975 0.1874 0.2601 0.0059  -0.0188 0.0088  47  GLY   B CA  
4661 C  C   . GLY   B 47  ? 0.1787 0.1648 0.2255 0.0033  -0.0047 0.0103  47  GLY   B C   
4662 O  O   . GLY   B 47  ? 0.1936 0.1487 0.2293 0.0018  -0.0171 0.0113  47  GLY   B O   
4666 N  N   . GLY   B 48  ? 0.1651 0.1551 0.2130 0.0026  -0.0141 0.0176  48  GLY   B N   
4667 C  CA  . GLY   B 48  ? 0.1615 0.1538 0.2167 -0.0011 -0.0120 0.0167  48  GLY   B CA  
4668 C  C   . GLY   B 48  ? 0.1538 0.1495 0.1983 0.0009  -0.0050 0.0027  48  GLY   B C   
4669 O  O   . GLY   B 48  ? 0.1509 0.1494 0.2244 0.0051  -0.0123 0.0001  48  GLY   B O   
4673 N  N   . VAL   B 49  ? 0.1561 0.1515 0.1792 0.0081  -0.0009 0.0065  49  VAL   B N   
4674 C  CA  . VAL   B 49  ? 0.1588 0.1612 0.1768 0.0088  -0.0176 -0.0064 49  VAL   B CA  
4675 C  C   . VAL   B 49  ? 0.1462 0.1501 0.1656 0.0115  -0.0126 0.0006  49  VAL   B C   
4676 O  O   . VAL   B 49  ? 0.1576 0.1551 0.1852 0.0013  -0.0054 0.0029  49  VAL   B O   
4677 C  CB  . VAL   B 49  ? 0.1606 0.1758 0.2072 0.0007  -0.0268 -0.0082 49  VAL   B CB  
4678 C  CG1 . VAL   B 49  ? 0.1644 0.1825 0.1950 0.0101  -0.0362 -0.0023 49  VAL   B CG1 
4679 C  CG2 . VAL   B 49  ? 0.1803 0.1920 0.2303 -0.0080 -0.0427 -0.0123 49  VAL   B CG2 
4689 N  N   . ALA   B 50  ? 0.1454 0.1463 0.1667 0.0020  -0.0081 0.0031  50  ALA   B N   
4690 C  CA  . ALA   B 50  ? 0.1454 0.1390 0.1665 0.0065  -0.0035 0.0046  50  ALA   B CA  
4691 C  C   . ALA   B 50  ? 0.1593 0.1421 0.1600 0.0025  -0.0052 0.0068  50  ALA   B C   
4692 O  O   . ALA   B 50  ? 0.1575 0.1459 0.1664 0.0029  -0.0069 0.0018  50  ALA   B O   
4693 C  CB  . ALA   B 50  ? 0.1508 0.1411 0.1701 0.0017  -0.0045 0.0092  50  ALA   B CB  
4699 N  N   . GLY   B 51  ? 0.1585 0.1534 0.1700 0.0079  -0.0104 0.0151  51  GLY   B N   
4700 C  CA  . GLY   B 51  ? 0.1526 0.1619 0.1898 0.0187  -0.0151 0.0067  51  GLY   B CA  
4701 C  C   . GLY   B 51  ? 0.1550 0.1544 0.1857 0.0191  -0.0058 0.0007  51  GLY   B C   
4702 O  O   . GLY   B 51  ? 0.1588 0.1668 0.2091 0.0086  -0.0094 -0.0001 51  GLY   B O   
4706 N  N   . ALA   B 52  ? 0.1537 0.1514 0.1782 0.0142  -0.0070 0.0008  52  ALA   B N   
4707 C  CA  . ALA   B 52  ? 0.1567 0.1527 0.1895 0.0117  -0.0004 -0.0029 52  ALA   B CA  
4708 C  C   . ALA   B 52  ? 0.1439 0.1524 0.1739 0.0047  -0.0022 -0.0050 52  ALA   B C   
4709 O  O   . ALA   B 52  ? 0.1467 0.1610 0.1944 0.0083  -0.0016 -0.0017 52  ALA   B O   
4710 C  CB  . ALA   B 52  ? 0.1795 0.1522 0.1970 0.0030  0.0048  -0.0039 52  ALA   B CB  
4716 N  N   . LEU   B 53  ? 0.1392 0.1501 0.1696 0.0123  -0.0003 -0.0004 53  LEU   B N   
4717 C  CA  . LEU   B 53  ? 0.1419 0.1602 0.1675 0.0100  -0.0070 -0.0021 53  LEU   B CA  
4718 C  C   . LEU   B 53  ? 0.1487 0.1542 0.1608 0.0126  0.0022  0.0068  53  LEU   B C   
4719 O  O   . LEU   B 53  ? 0.1553 0.1602 0.1699 0.0018  0.0053  0.0120  53  LEU   B O   
4720 C  CB  . LEU   B 53  ? 0.1418 0.1633 0.1838 0.0080  -0.0043 0.0107  53  LEU   B CB  
4721 C  CG  . LEU   B 53  ? 0.1424 0.1723 0.1791 0.0016  -0.0100 0.0188  53  LEU   B CG  
4722 C  CD1 . LEU   B 53  ? 0.1491 0.1943 0.2025 0.0081  -0.0102 0.0071  53  LEU   B CD1 
4723 C  CD2 . LEU   B 53  ? 0.1625 0.2011 0.2051 -0.0080 -0.0177 -0.0097 53  LEU   B CD2 
4735 N  N   . ASN   B 54  ? 0.1499 0.1429 0.1667 0.0039  -0.0064 0.0037  54  ASN   B N   
4736 C  CA  . ASN   B 54  ? 0.1568 0.1555 0.1757 0.0030  -0.0103 -0.0065 54  ASN   B CA  
4737 C  C   . ASN   B 54  ? 0.1497 0.1586 0.1953 0.0007  0.0006  -0.0014 54  ASN   B C   
4738 O  O   . ASN   B 54  ? 0.1451 0.1640 0.2035 -0.0051 0.0030  -0.0005 54  ASN   B O   
4739 C  CB  . ASN   B 54  ? 0.1636 0.1704 0.1887 0.0044  -0.0061 -0.0003 54  ASN   B CB  
4740 C  CG  . ASN   B 54  ? 0.1575 0.1762 0.1860 0.0040  -0.0108 0.0019  54  ASN   B CG  
4741 O  OD1 . ASN   B 54  ? 0.1510 0.1697 0.1997 0.0009  -0.0181 -0.0102 54  ASN   B OD1 
4742 N  ND2 . ASN   B 54  ? 0.1737 0.1940 0.2061 0.0024  -0.0304 0.0155  54  ASN   B ND2 
4749 N  N   . LYS   B 55  ? 0.1477 0.1632 0.2057 0.0100  -0.0060 -0.0038 55  LYS   B N   
4750 C  CA  . LYS   B 55  ? 0.1515 0.1787 0.2310 0.0164  -0.0096 -0.0019 55  LYS   B CA  
4751 C  C   . LYS   B 55  ? 0.1477 0.1728 0.2210 0.0131  -0.0004 -0.0100 55  LYS   B C   
4752 O  O   . LYS   B 55  ? 0.1458 0.1894 0.2385 0.0086  0.0056  -0.0052 55  LYS   B O   
4753 C  CB  . LYS   B 55  ? 0.1613 0.1898 0.2737 0.0270  -0.0018 0.0090  55  LYS   B CB  
4754 C  CG  . LYS   B 55  ? 0.2018 0.2198 0.3495 0.0325  0.0154  0.0237  55  LYS   B CG  
4755 C  CD  . LYS   B 55  ? 0.2438 0.2426 0.4191 0.0408  0.0284  0.0390  55  LYS   B CD  
4756 C  CE  . LYS   B 55  ? 0.2706 0.2641 0.4781 0.0408  0.0450  0.0476  55  LYS   B CE  
4757 N  NZ  . LYS   B 55  ? 0.2784 0.2781 0.5121 0.0408  0.0321  0.0585  55  LYS   B NZ  
4771 N  N   . ALA   B 56  ? 0.1474 0.1815 0.2027 0.0035  0.0024  -0.0131 56  ALA   B N   
4772 C  CA  . ALA   B 56  ? 0.1598 0.1998 0.2000 -0.0002 0.0105  -0.0133 56  ALA   B CA  
4773 C  C   . ALA   B 56  ? 0.1592 0.1932 0.1922 0.0006  0.0135  -0.0070 56  ALA   B C   
4774 O  O   . ALA   B 56  ? 0.1739 0.2080 0.2135 0.0082  0.0289  -0.0013 56  ALA   B O   
4775 C  CB  . ALA   B 56  ? 0.1751 0.2188 0.1979 -0.0104 0.0093  -0.0092 56  ALA   B CB  
4781 N  N   . THR   B 57  ? 0.1579 0.1779 0.1996 0.0005  0.0170  -0.0005 57  THR   B N   
4782 C  CA  . THR   B 57  ? 0.1621 0.1809 0.2050 -0.0038 0.0209  -0.0003 57  THR   B CA  
4783 C  C   . THR   B 57  ? 0.1604 0.1879 0.2214 0.0017  0.0158  -0.0028 57  THR   B C   
4784 O  O   . THR   B 57  ? 0.1677 0.1885 0.2302 -0.0202 0.0107  -0.0059 57  THR   B O   
4785 C  CB  . THR   B 57  ? 0.1689 0.1663 0.1930 -0.0019 0.0174  0.0076  57  THR   B CB  
4786 O  OG1 . THR   B 57  ? 0.1662 0.1588 0.2181 -0.0057 0.0136  -0.0009 57  THR   B OG1 
4787 C  CG2 . THR   B 57  ? 0.1657 0.1658 0.1879 -0.0004 0.0221  0.0076  57  THR   B CG2 
4795 N  N   . ASN   B 58  ? 0.1456 0.2144 0.2498 -0.0169 0.0067  -0.0204 58  ASN   B N   
4796 C  CA  . ASN   B 58  ? 0.1785 0.2713 0.2857 -0.0350 0.0372  -0.0091 58  ASN   B CA  
4797 C  C   . ASN   B 58  ? 0.1543 0.2409 0.2439 -0.0221 -0.0014 -0.0136 58  ASN   B C   
4798 O  O   . ASN   B 58  ? 0.1602 0.2441 0.2518 -0.0261 -0.0015 -0.0233 58  ASN   B O   
4799 C  CB  . ASN   B 58  ? 0.2951 0.3710 0.4150 -0.0502 0.0772  0.0062  58  ASN   B CB  
4800 C  CG  . ASN   B 58  ? 0.4289 0.4643 0.5664 -0.0528 0.0938  0.0244  58  ASN   B CG  
4801 O  OD1 . ASN   B 58  ? 0.4598 0.4906 0.6195 -0.0542 0.0990  0.0302  58  ASN   B OD1 
4802 N  ND2 . ASN   B 58  ? 0.5463 0.5463 0.6225 -0.0559 0.1000  0.0304  58  ASN   B ND2 
4809 N  N   . ASN   B 59  ? 0.1512 0.2199 0.2278 -0.0133 -0.0067 -0.0059 59  ASN   B N   
4810 C  CA  . ASN   B 59  ? 0.1520 0.2102 0.2215 -0.0143 -0.0197 0.0040  59  ASN   B CA  
4811 C  C   . ASN   B 59  ? 0.1493 0.1994 0.2083 -0.0144 -0.0207 -0.0046 59  ASN   B C   
4812 O  O   . ASN   B 59  ? 0.1549 0.1983 0.2074 -0.0129 -0.0116 -0.0023 59  ASN   B O   
4813 C  CB  . ASN   B 59  ? 0.1618 0.2267 0.2220 -0.0090 -0.0320 0.0009  59  ASN   B CB  
4814 C  CG  . ASN   B 59  ? 0.1792 0.2459 0.2338 -0.0032 -0.0438 -0.0031 59  ASN   B CG  
4815 O  OD1 . ASN   B 59  ? 0.1845 0.2540 0.2348 -0.0013 -0.0319 0.0123  59  ASN   B OD1 
4816 N  ND2 . ASN   B 59  ? 0.1869 0.2600 0.2475 -0.0081 -0.0480 -0.0079 59  ASN   B ND2 
4823 N  N   . ALA   B 60  ? 0.1537 0.1885 0.2069 -0.0181 -0.0049 -0.0098 60  ALA   B N   
4824 C  CA  . ALA   B 60  ? 0.1614 0.1765 0.2082 -0.0231 -0.0048 -0.0016 60  ALA   B CA  
4825 C  C   . ALA   B 60  ? 0.1617 0.1638 0.1896 -0.0132 -0.0096 0.0008  60  ALA   B C   
4826 O  O   . ALA   B 60  ? 0.1655 0.1679 0.2047 -0.0169 0.0012  -0.0081 60  ALA   B O   
4827 C  CB  . ALA   B 60  ? 0.1733 0.1764 0.2302 -0.0244 0.0046  -0.0035 60  ALA   B CB  
4833 N  N   . MET   B 61  ? 0.1571 0.1576 0.1807 -0.0104 -0.0061 0.0029  61  MET   B N   
4834 C  CA  . MET   B 61  ? 0.1478 0.1554 0.1712 -0.0108 -0.0168 0.0027  61  MET   B CA  
4835 C  C   . MET   B 61  ? 0.1541 0.1487 0.1737 -0.0116 -0.0166 0.0045  61  MET   B C   
4836 O  O   . MET   B 61  ? 0.1563 0.1479 0.1703 -0.0016 -0.0120 -0.0099 61  MET   B O   
4837 C  CB  . MET   B 61  ? 0.1441 0.1548 0.1790 -0.0006 -0.0086 0.0015  61  MET   B CB  
4838 C  CG  . MET   B 61  ? 0.1394 0.1510 0.1704 0.0001  -0.0074 0.0039  61  MET   B CG  
4839 S  SD  . MET   B 61  ? 0.1484 0.1582 0.1812 -0.0031 -0.0079 -0.0101 61  MET   B SD  
4840 C  CE  . MET   B 61  ? 0.1606 0.1767 0.2080 -0.0010 -0.0019 -0.0172 61  MET   B CE  
4850 N  N   . GLN   B 62  ? 0.1536 0.1546 0.1725 -0.0013 -0.0222 0.0049  62  GLN   B N   
4851 C  CA  . GLN   B 62  ? 0.1585 0.1603 0.1796 0.0015  -0.0236 -0.0089 62  GLN   B CA  
4852 C  C   . GLN   B 62  ? 0.1569 0.1670 0.1854 -0.0006 -0.0317 -0.0091 62  GLN   B C   
4853 O  O   . GLN   B 62  ? 0.1697 0.1691 0.1836 -0.0033 -0.0347 -0.0121 62  GLN   B O   
4854 C  CB  . GLN   B 62  ? 0.1615 0.1659 0.1869 0.0048  -0.0185 0.0022  62  GLN   B CB  
4855 C  CG  . GLN   B 62  ? 0.1683 0.1727 0.1820 0.0018  -0.0232 -0.0051 62  GLN   B CG  
4856 C  CD  . GLN   B 62  ? 0.1689 0.1705 0.1746 0.0054  -0.0237 0.0063  62  GLN   B CD  
4857 O  OE1 . GLN   B 62  ? 0.1642 0.1630 0.1918 0.0022  -0.0327 -0.0076 62  GLN   B OE1 
4858 N  NE2 . GLN   B 62  ? 0.1686 0.1775 0.1769 0.0084  -0.0198 -0.0090 62  GLN   B NE2 
4867 N  N   . VAL   B 63  ? 0.1592 0.1695 0.2011 -0.0076 -0.0300 -0.0129 63  VAL   B N   
4868 C  CA  . VAL   B 63  ? 0.1716 0.1723 0.2151 -0.0084 -0.0336 -0.0076 63  VAL   B CA  
4869 C  C   . VAL   B 63  ? 0.1731 0.1641 0.1895 -0.0173 -0.0321 -0.0182 63  VAL   B C   
4870 O  O   . VAL   B 63  ? 0.1837 0.1597 0.2080 -0.0129 -0.0439 -0.0132 63  VAL   B O   
4871 C  CB  . VAL   B 63  ? 0.1663 0.1888 0.2405 -0.0130 -0.0324 -0.0144 63  VAL   B CB  
4872 C  CG1 . VAL   B 63  ? 0.1779 0.1940 0.2578 -0.0250 -0.0218 -0.0156 63  VAL   B CG1 
4873 C  CG2 . VAL   B 63  ? 0.1586 0.2069 0.2548 -0.0118 -0.0263 -0.0187 63  VAL   B CG2 
4883 N  N   . GLU   B 64  ? 0.1656 0.1558 0.1843 -0.0106 -0.0283 -0.0092 64  GLU   B N   
4884 C  CA  . GLU   B 64  ? 0.1651 0.1491 0.1873 -0.0140 -0.0340 -0.0039 64  GLU   B CA  
4885 C  C   . GLU   B 64  ? 0.1588 0.1469 0.1876 -0.0054 -0.0285 -0.0155 64  GLU   B C   
4886 O  O   . GLU   B 64  ? 0.1737 0.1555 0.1824 -0.0067 -0.0277 -0.0150 64  GLU   B O   
4887 C  CB  . GLU   B 64  ? 0.1695 0.1578 0.1890 -0.0169 -0.0282 0.0010  64  GLU   B CB  
4888 C  CG  . GLU   B 64  ? 0.1803 0.1584 0.1900 -0.0290 -0.0292 -0.0129 64  GLU   B CG  
4889 C  CD  . GLU   B 64  ? 0.1788 0.1731 0.1987 -0.0314 -0.0307 -0.0029 64  GLU   B CD  
4890 O  OE1 . GLU   B 64  ? 0.1810 0.1912 0.2102 -0.0316 -0.0237 -0.0200 64  GLU   B OE1 
4891 O  OE2 . GLU   B 64  ? 0.1906 0.1828 0.2018 -0.0310 -0.0404 -0.0098 64  GLU   B OE2 
4898 N  N   . SER   B 65  ? 0.1605 0.1458 0.1718 -0.0041 -0.0162 -0.0187 65  SER   B N   
4899 C  CA  . SER   B 65  ? 0.1639 0.1417 0.1737 0.0003  -0.0184 -0.0157 65  SER   B CA  
4900 C  C   . SER   B 65  ? 0.1703 0.1462 0.1713 0.0051  -0.0207 -0.0140 65  SER   B C   
4901 O  O   . SER   B 65  ? 0.1701 0.1591 0.1694 0.0014  -0.0234 -0.0222 65  SER   B O   
4902 C  CB  . SER   B 65  ? 0.1642 0.1471 0.1833 -0.0126 -0.0227 -0.0141 65  SER   B CB  
4903 O  OG  . SER   B 65  ? 0.1625 0.1505 0.1865 -0.0058 -0.0207 -0.0249 65  SER   B OG  
4909 N  N   . ASP   B 66  ? 0.1810 0.1590 0.1729 -0.0002 -0.0319 -0.0170 66  ASP   B N   
4910 C  CA  . ASP   B 66  ? 0.1852 0.1590 0.1611 0.0021  -0.0317 -0.0108 66  ASP   B CA  
4911 C  C   . ASP   B 66  ? 0.1895 0.1663 0.1632 -0.0029 -0.0300 -0.0122 66  ASP   B C   
4912 O  O   . ASP   B 66  ? 0.1892 0.1744 0.1778 0.0089  -0.0266 -0.0221 66  ASP   B O   
4913 C  CB  . ASP   B 66  ? 0.2009 0.1713 0.1815 0.0110  -0.0458 -0.0186 66  ASP   B CB  
4914 C  CG  . ASP   B 66  ? 0.2280 0.1942 0.2141 0.0165  -0.0540 -0.0052 66  ASP   B CG  
4915 O  OD1 . ASP   B 66  ? 0.2460 0.1918 0.2246 0.0126  -0.0568 -0.0023 66  ASP   B OD1 
4916 O  OD2 . ASP   B 66  ? 0.2462 0.2184 0.2687 0.0348  -0.0481 -0.0057 66  ASP   B OD2 
4921 N  N   . ASP   B 67  ? 0.1849 0.1612 0.1642 -0.0073 -0.0338 -0.0226 67  ASP   B N   
4922 C  CA  . ASP   B 67  ? 0.1962 0.1502 0.1871 -0.0110 -0.0317 -0.0137 67  ASP   B CA  
4923 C  C   . ASP   B 67  ? 0.1879 0.1565 0.1865 0.0019  -0.0282 -0.0159 67  ASP   B C   
4924 O  O   . ASP   B 67  ? 0.1913 0.1642 0.1942 0.0003  -0.0203 -0.0250 67  ASP   B O   
4925 C  CB  . ASP   B 67  ? 0.2200 0.1619 0.2025 -0.0193 -0.0436 -0.0070 67  ASP   B CB  
4926 C  CG  . ASP   B 67  ? 0.2570 0.1731 0.1983 -0.0132 -0.0638 -0.0101 67  ASP   B CG  
4927 O  OD1 . ASP   B 67  ? 0.2786 0.1839 0.2210 -0.0115 -0.0675 -0.0114 67  ASP   B OD1 
4928 O  OD2 . ASP   B 67  ? 0.2711 0.1810 0.2121 0.0038  -0.0668 -0.0073 67  ASP   B OD2 
4933 N  N   . TYR   B 68  ? 0.1820 0.1591 0.1827 0.0033  -0.0365 -0.0272 68  TYR   B N   
4934 C  CA  . TYR   B 68  ? 0.1779 0.1727 0.1978 0.0089  -0.0344 -0.0308 68  TYR   B CA  
4935 C  C   . TYR   B 68  ? 0.1705 0.1667 0.1926 0.0031  -0.0356 -0.0338 68  TYR   B C   
4936 O  O   . TYR   B 68  ? 0.1763 0.1791 0.2085 0.0106  -0.0330 -0.0487 68  TYR   B O   
4937 C  CB  . TYR   B 68  ? 0.1824 0.1922 0.2010 0.0081  -0.0437 -0.0418 68  TYR   B CB  
4938 C  CG  . TYR   B 68  ? 0.1973 0.2089 0.2089 0.0132  -0.0349 -0.0517 68  TYR   B CG  
4939 C  CD1 . TYR   B 68  ? 0.1986 0.2141 0.2267 -0.0026 -0.0368 -0.0550 68  TYR   B CD1 
4940 C  CD2 . TYR   B 68  ? 0.2013 0.2276 0.2252 0.0187  -0.0485 -0.0443 68  TYR   B CD2 
4941 C  CE1 . TYR   B 68  ? 0.2014 0.2272 0.2526 -0.0003 -0.0322 -0.0537 68  TYR   B CE1 
4942 C  CE2 . TYR   B 68  ? 0.2009 0.2311 0.2297 0.0194  -0.0332 -0.0586 68  TYR   B CE2 
4943 C  CZ  . TYR   B 68  ? 0.1954 0.2343 0.2475 0.0081  -0.0324 -0.0568 68  TYR   B CZ  
4944 O  OH  . TYR   B 68  ? 0.1884 0.2515 0.2719 0.0026  -0.0290 -0.0338 68  TYR   B OH  
4954 N  N   . ILE   B 69  ? 0.1683 0.1613 0.1900 0.0057  -0.0349 -0.0349 69  ILE   B N   
4955 C  CA  . ILE   B 69  ? 0.1800 0.1663 0.1955 0.0014  -0.0196 -0.0357 69  ILE   B CA  
4956 C  C   . ILE   B 69  ? 0.1785 0.1660 0.1924 0.0084  -0.0260 -0.0286 69  ILE   B C   
4957 O  O   . ILE   B 69  ? 0.1811 0.1734 0.1869 0.0070  -0.0176 -0.0292 69  ILE   B O   
4958 C  CB  . ILE   B 69  ? 0.1903 0.1699 0.2123 -0.0030 0.0035  -0.0332 69  ILE   B CB  
4959 C  CG1 . ILE   B 69  ? 0.1901 0.1751 0.2216 -0.0018 0.0076  -0.0350 69  ILE   B CG1 
4960 C  CG2 . ILE   B 69  ? 0.2013 0.1771 0.2253 -0.0051 0.0005  -0.0255 69  ILE   B CG2 
4961 C  CD1 . ILE   B 69  ? 0.1867 0.1819 0.2260 -0.0134 0.0053  -0.0352 69  ILE   B CD1 
4973 N  N   . ALA   B 70  ? 0.1797 0.1643 0.1993 0.0093  -0.0373 -0.0253 70  ALA   B N   
4974 C  CA  . ALA   B 70  ? 0.1841 0.1686 0.1842 0.0047  -0.0439 -0.0297 70  ALA   B CA  
4975 C  C   . ALA   B 70  ? 0.1871 0.1642 0.1895 0.0026  -0.0452 -0.0328 70  ALA   B C   
4976 O  O   . ALA   B 70  ? 0.1950 0.1643 0.1958 0.0054  -0.0420 -0.0292 70  ALA   B O   
4977 C  CB  . ALA   B 70  ? 0.1863 0.1847 0.1870 0.0034  -0.0440 -0.0323 70  ALA   B CB  
4983 N  N   . THR   B 71  ? 0.1946 0.1660 0.1976 0.0019  -0.0526 -0.0319 71  THR   B N   
4984 C  CA  . THR   B 71  ? 0.2070 0.1689 0.2132 0.0155  -0.0667 -0.0326 71  THR   B CA  
4985 C  C   . THR   B 71  ? 0.2027 0.1757 0.2469 0.0302  -0.0633 -0.0473 71  THR   B C   
4986 O  O   . THR   B 71  ? 0.2129 0.1806 0.2856 0.0335  -0.0543 -0.0541 71  THR   B O   
4987 C  CB  . THR   B 71  ? 0.2328 0.1906 0.2378 0.0096  -0.0718 -0.0118 71  THR   B CB  
4988 O  OG1 . THR   B 71  ? 0.2501 0.2210 0.2805 -0.0090 -0.0676 0.0062  71  THR   B OG1 
4989 C  CG2 . THR   B 71  ? 0.2509 0.1882 0.2573 0.0091  -0.0626 -0.0055 71  THR   B CG2 
4997 N  N   . ASN   B 72  ? 0.1924 0.1813 0.2420 0.0248  -0.0628 -0.0628 72  ASN   B N   
4998 C  CA  . ASN   B 72  ? 0.1897 0.1922 0.2436 0.0246  -0.0473 -0.0737 72  ASN   B CA  
4999 C  C   . ASN   B 72  ? 0.1878 0.2061 0.2488 0.0106  -0.0246 -0.0713 72  ASN   B C   
5000 O  O   . ASN   B 72  ? 0.1928 0.2258 0.2827 0.0125  -0.0097 -0.0748 72  ASN   B O   
5001 C  CB  . ASN   B 72  ? 0.1982 0.2074 0.2443 0.0160  -0.0656 -0.0584 72  ASN   B CB  
5002 C  CG  . ASN   B 72  ? 0.2084 0.2205 0.2499 0.0275  -0.0632 -0.0356 72  ASN   B CG  
5003 O  OD1 . ASN   B 72  ? 0.2289 0.2404 0.2633 0.0167  -0.0434 -0.0366 72  ASN   B OD1 
5004 N  ND2 . ASN   B 72  ? 0.2238 0.2283 0.2898 0.0400  -0.0537 -0.0071 72  ASN   B ND2 
5011 N  N   . GLY   B 73  ? 0.1911 0.2038 0.2297 0.0011  -0.0325 -0.0705 73  GLY   B N   
5012 C  CA  . GLY   B 73  ? 0.1885 0.2109 0.2078 0.0008  -0.0206 -0.0525 73  GLY   B CA  
5013 C  C   . GLY   B 73  ? 0.1838 0.2088 0.1687 0.0055  -0.0198 -0.0382 73  GLY   B C   
5014 O  O   . GLY   B 73  ? 0.1783 0.1961 0.1807 0.0066  -0.0149 -0.0296 73  GLY   B O   
5018 N  N   . PRO   B 74  ? 0.1832 0.2149 0.1684 0.0068  -0.0270 -0.0302 74  PRO   B N   
5019 C  CA  . PRO   B 74  ? 0.1775 0.2161 0.1588 0.0108  -0.0181 -0.0183 74  PRO   B CA  
5020 C  C   . PRO   B 74  ? 0.1661 0.2006 0.1684 0.0092  -0.0124 -0.0124 74  PRO   B C   
5021 O  O   . PRO   B 74  ? 0.1676 0.2015 0.2012 0.0087  -0.0068 -0.0323 74  PRO   B O   
5022 C  CB  . PRO   B 74  ? 0.1940 0.2313 0.1707 0.0086  -0.0188 -0.0100 74  PRO   B CB  
5023 C  CG  . PRO   B 74  ? 0.2102 0.2393 0.1937 0.0102  -0.0153 -0.0073 74  PRO   B CG  
5024 C  CD  . PRO   B 74  ? 0.2067 0.2305 0.1846 0.0106  -0.0170 -0.0185 74  PRO   B CD  
5032 N  N   . LEU   B 75  ? 0.1654 0.1902 0.1569 0.0092  -0.0200 -0.0172 75  LEU   B N   
5033 C  CA  . LEU   B 75  ? 0.1728 0.1899 0.1532 0.0024  -0.0204 -0.0027 75  LEU   B CA  
5034 C  C   . LEU   B 75  ? 0.1761 0.1992 0.1530 0.0080  -0.0056 -0.0033 75  LEU   B C   
5035 O  O   . LEU   B 75  ? 0.1929 0.2093 0.1681 -0.0017 -0.0029 0.0027  75  LEU   B O   
5036 C  CB  . LEU   B 75  ? 0.1835 0.1903 0.1471 -0.0090 -0.0214 0.0116  75  LEU   B CB  
5037 C  CG  . LEU   B 75  ? 0.2150 0.2072 0.1581 -0.0275 -0.0083 0.0073  75  LEU   B CG  
5038 C  CD1 . LEU   B 75  ? 0.2438 0.2216 0.1647 -0.0368 0.0092  -0.0032 75  LEU   B CD1 
5039 C  CD2 . LEU   B 75  ? 0.2510 0.2299 0.2197 -0.0196 0.0037  0.0107  75  LEU   B CD2 
5051 N  N   . LYS   B 76  ? 0.1758 0.2227 0.1818 0.0043  0.0050  0.0081  76  LYS   B N   
5052 C  CA  . LYS   B 76  ? 0.1880 0.2300 0.2173 -0.0077 0.0241  0.0042  76  LYS   B CA  
5053 C  C   . LYS   B 76  ? 0.1818 0.2138 0.1993 -0.0025 0.0151  0.0245  76  LYS   B C   
5054 O  O   . LYS   B 76  ? 0.1822 0.1946 0.2014 -0.0032 0.0099  0.0192  76  LYS   B O   
5055 C  CB  . LYS   B 76  ? 0.1979 0.2329 0.2666 -0.0204 0.0404  -0.0219 76  LYS   B CB  
5056 C  CG  . LYS   B 76  ? 0.2056 0.2536 0.3063 -0.0156 0.0362  -0.0282 76  LYS   B CG  
5057 C  CD  . LYS   B 76  ? 0.2094 0.2646 0.3403 -0.0050 0.0281  -0.0387 76  LYS   B CD  
5058 C  CE  . LYS   B 76  ? 0.2142 0.2816 0.3893 -0.0021 0.0102  -0.0465 76  LYS   B CE  
5059 N  NZ  . LYS   B 76  ? 0.2165 0.2893 0.4084 -0.0016 -0.0138 -0.0586 76  LYS   B NZ  
5073 N  N   . VAL   B 77  ? 0.1921 0.2294 0.1979 0.0068  0.0217  0.0314  77  VAL   B N   
5074 C  CA  . VAL   B 77  ? 0.1939 0.2193 0.2055 0.0152  0.0260  0.0623  77  VAL   B CA  
5075 C  C   . VAL   B 77  ? 0.1786 0.1979 0.2030 0.0128  0.0375  0.0475  77  VAL   B C   
5076 O  O   . VAL   B 77  ? 0.1825 0.1947 0.2047 0.0220  0.0381  0.0316  77  VAL   B O   
5077 C  CB  . VAL   B 77  ? 0.2066 0.2304 0.2429 0.0136  0.0356  0.0774  77  VAL   B CB  
5078 C  CG1 . VAL   B 77  ? 0.2094 0.2239 0.2642 0.0047  0.0363  0.0896  77  VAL   B CG1 
5079 C  CG2 . VAL   B 77  ? 0.2237 0.2501 0.2640 0.0132  0.0175  0.0751  77  VAL   B CG2 
5089 N  N   . GLY   B 78  ? 0.1723 0.1794 0.1991 0.0066  0.0279  0.0383  78  GLY   B N   
5090 C  CA  . GLY   B 78  ? 0.1724 0.1698 0.1928 0.0106  0.0344  0.0269  78  GLY   B CA  
5091 C  C   . GLY   B 78  ? 0.1690 0.1646 0.1855 0.0114  0.0225  0.0248  78  GLY   B C   
5092 O  O   . GLY   B 78  ? 0.1668 0.1646 0.2039 0.0212  0.0202  0.0279  78  GLY   B O   
5096 N  N   . GLY   B 79  ? 0.1626 0.1676 0.1844 0.0068  0.0165  0.0126  79  GLY   B N   
5097 C  CA  . GLY   B 79  ? 0.1610 0.1586 0.1826 0.0108  0.0088  0.0134  79  GLY   B CA  
5098 C  C   . GLY   B 79  ? 0.1475 0.1543 0.1806 0.0077  0.0084  0.0093  79  GLY   B C   
5099 O  O   . GLY   B 79  ? 0.1562 0.1547 0.1936 0.0107  0.0201  0.0220  79  GLY   B O   
5103 N  N   . SER   B 80  ? 0.1449 0.1446 0.1939 0.0041  0.0180  0.0137  80  SER   B N   
5104 C  CA  . SER   B 80  ? 0.1403 0.1463 0.1842 0.0014  0.0088  0.0037  80  SER   B CA  
5105 C  C   . SER   B 80  ? 0.1412 0.1397 0.1780 0.0063  -0.0049 0.0021  80  SER   B C   
5106 O  O   . SER   B 80  ? 0.1586 0.1465 0.2089 0.0078  0.0050  0.0033  80  SER   B O   
5107 C  CB  . SER   B 80  ? 0.1506 0.1492 0.1878 -0.0052 0.0001  0.0074  80  SER   B CB  
5108 O  OG  . SER   B 80  ? 0.1563 0.1647 0.2029 -0.0057 -0.0117 0.0092  80  SER   B OG  
5114 N  N   . CYS   B 81  ? 0.1434 0.1281 0.1799 0.0036  -0.0106 -0.0012 81  CYS   B N   
5115 C  CA  . CYS   B 81  ? 0.1506 0.1290 0.1769 0.0055  -0.0091 -0.0013 81  CYS   B CA  
5116 C  C   . CYS   B 81  ? 0.1422 0.1271 0.1570 0.0011  -0.0120 -0.0018 81  CYS   B C   
5117 O  O   . CYS   B 81  ? 0.1647 0.1326 0.1725 0.0078  -0.0017 -0.0039 81  CYS   B O   
5118 C  CB  . CYS   B 81  ? 0.1652 0.1437 0.1820 -0.0047 -0.0166 0.0001  81  CYS   B CB  
5119 S  SG  . CYS   B 81  ? 0.1668 0.1640 0.1627 -0.0048 -0.0203 -0.0084 81  CYS   B SG  
5125 N  N   . VAL   B 82  ? 0.1490 0.1261 0.1714 -0.0024 -0.0084 -0.0055 82  VAL   B N   
5126 C  CA  . VAL   B 82  ? 0.1550 0.1360 0.1582 -0.0097 -0.0058 0.0025  82  VAL   B CA  
5127 C  C   . VAL   B 82  ? 0.1637 0.1238 0.1717 -0.0064 -0.0043 -0.0002 82  VAL   B C   
5128 O  O   . VAL   B 82  ? 0.1739 0.1266 0.2018 -0.0061 -0.0096 -0.0119 82  VAL   B O   
5129 C  CB  . VAL   B 82  ? 0.1623 0.1505 0.1841 -0.0039 -0.0150 0.0091  82  VAL   B CB  
5130 C  CG1 . VAL   B 82  ? 0.1848 0.1749 0.1928 0.0006  -0.0121 0.0158  82  VAL   B CG1 
5131 C  CG2 . VAL   B 82  ? 0.1691 0.1661 0.2033 -0.0073 -0.0304 0.0131  82  VAL   B CG2 
5141 N  N   . LEU   B 83  ? 0.1507 0.1264 0.1726 -0.0171 -0.0178 -0.0078 83  LEU   B N   
5142 C  CA  . LEU   B 83  ? 0.1527 0.1334 0.1627 -0.0139 -0.0149 -0.0026 83  LEU   B CA  
5143 C  C   . LEU   B 83  ? 0.1500 0.1309 0.1602 -0.0196 -0.0169 0.0001  83  LEU   B C   
5144 O  O   . LEU   B 83  ? 0.1557 0.1415 0.1505 -0.0211 -0.0190 0.0052  83  LEU   B O   
5145 C  CB  . LEU   B 83  ? 0.1616 0.1492 0.1612 -0.0150 -0.0270 -0.0049 83  LEU   B CB  
5146 C  CG  . LEU   B 83  ? 0.1768 0.1699 0.1665 -0.0177 -0.0199 -0.0068 83  LEU   B CG  
5147 C  CD1 . LEU   B 83  ? 0.1852 0.1780 0.1671 -0.0149 -0.0239 -0.0013 83  LEU   B CD1 
5148 C  CD2 . LEU   B 83  ? 0.1987 0.1682 0.1781 -0.0122 -0.0185 -0.0268 83  LEU   B CD2 
5160 N  N   . SER   B 84  ? 0.1591 0.1410 0.1755 -0.0243 -0.0201 0.0003  84  SER   B N   
5161 C  CA  . SER   B 84  ? 0.1585 0.1622 0.1668 -0.0249 -0.0174 0.0153  84  SER   B CA  
5162 C  C   . SER   B 84  ? 0.1483 0.1781 0.1348 -0.0222 -0.0165 0.0175  84  SER   B C   
5163 O  O   . SER   B 84  ? 0.1576 0.1667 0.1356 -0.0184 -0.0122 0.0027  84  SER   B O   
5164 C  CB  . SER   B 84  ? 0.1783 0.1644 0.2110 -0.0313 0.0052  0.0085  84  SER   B CB  
5165 O  OG  . SER   B 84  ? 0.1755 0.1831 0.2573 -0.0426 0.0040  0.0197  84  SER   B OG  
5171 N  N   . GLY   B 85  ? 0.1525 0.1992 0.1545 -0.0297 -0.0165 0.0244  85  GLY   B N   
5172 C  CA  . GLY   B 85  ? 0.1555 0.2057 0.1737 -0.0387 -0.0032 -0.0035 85  GLY   B CA  
5173 C  C   . GLY   B 85  ? 0.1546 0.1876 0.1600 -0.0410 -0.0051 0.0061  85  GLY   B C   
5174 O  O   . GLY   B 85  ? 0.1609 0.1812 0.1717 -0.0502 0.0154  -0.0137 85  GLY   B O   
5178 N  N   . HIS   B 86  ? 0.1526 0.1762 0.1805 -0.0322 -0.0185 0.0145  86  HIS   B N   
5179 C  CA  . HIS   B 86  ? 0.1563 0.1717 0.1804 -0.0294 -0.0175 0.0183  86  HIS   B CA  
5180 C  C   . HIS   B 86  ? 0.1573 0.1850 0.1645 -0.0433 -0.0070 0.0297  86  HIS   B C   
5181 O  O   . HIS   B 86  ? 0.1705 0.1960 0.1688 -0.0319 0.0093  0.0249  86  HIS   B O   
5182 C  CB  . HIS   B 86  ? 0.1616 0.1728 0.1824 -0.0238 -0.0267 0.0054  86  HIS   B CB  
5183 C  CG  . HIS   B 86  ? 0.1630 0.1796 0.1813 -0.0128 -0.0249 0.0093  86  HIS   B CG  
5184 N  ND1 . HIS   B 86  ? 0.1773 0.2077 0.2058 -0.0209 -0.0329 -0.0080 86  HIS   B ND1 
5185 C  CD2 . HIS   B 86  ? 0.1700 0.1857 0.1897 -0.0121 -0.0211 0.0078  86  HIS   B CD2 
5186 C  CE1 . HIS   B 86  ? 0.1861 0.2043 0.1952 -0.0188 -0.0140 -0.0223 86  HIS   B CE1 
5187 N  NE2 . HIS   B 86  ? 0.1761 0.1928 0.1845 -0.0020 -0.0115 -0.0067 86  HIS   B NE2 
5195 N  N   . ASN   B 87  ? 0.1602 0.1893 0.1738 -0.0387 -0.0026 0.0217  87  ASN   B N   
5196 C  CA  . ASN   B 87  ? 0.1653 0.2102 0.1827 -0.0374 0.0214  0.0166  87  ASN   B CA  
5197 C  C   . ASN   B 87  ? 0.1809 0.1929 0.1667 -0.0367 0.0312  0.0168  87  ASN   B C   
5198 O  O   . ASN   B 87  ? 0.2090 0.2014 0.2045 -0.0295 0.0495  0.0106  87  ASN   B O   
5199 C  CB  . ASN   B 87  ? 0.1638 0.2460 0.2087 -0.0319 0.0265  0.0085  87  ASN   B CB  
5200 C  CG  . ASN   B 87  ? 0.1696 0.2649 0.2157 0.0020  0.0310  0.0282  87  ASN   B CG  
5201 O  OD1 . ASN   B 87  ? 0.1648 0.2543 0.2046 0.0016  0.0430  0.0383  87  ASN   B OD1 
5202 N  ND2 . ASN   B 87  ? 0.2040 0.2745 0.2530 0.0063  0.0340  0.0279  87  ASN   B ND2 
5209 N  N   . LEU   B 88  ? 0.1710 0.1818 0.1611 -0.0399 0.0146  0.0116  88  LEU   B N   
5210 C  CA  . LEU   B 88  ? 0.1800 0.1770 0.1589 -0.0404 0.0058  -0.0012 88  LEU   B CA  
5211 C  C   . LEU   B 88  ? 0.1801 0.1636 0.1663 -0.0432 -0.0059 0.0048  88  LEU   B C   
5212 O  O   . LEU   B 88  ? 0.2044 0.1728 0.2016 -0.0264 -0.0302 -0.0083 88  LEU   B O   
5213 C  CB  . LEU   B 88  ? 0.1944 0.1778 0.1789 -0.0459 -0.0040 0.0065  88  LEU   B CB  
5214 C  CG  . LEU   B 88  ? 0.2322 0.2062 0.2044 -0.0414 -0.0237 0.0239  88  LEU   B CG  
5215 C  CD1 . LEU   B 88  ? 0.2497 0.2315 0.2209 -0.0489 -0.0186 0.0402  88  LEU   B CD1 
5216 C  CD2 . LEU   B 88  ? 0.2677 0.2326 0.2487 -0.0021 -0.0469 0.0079  88  LEU   B CD2 
5228 N  N   . ALA   B 89  ? 0.1657 0.1592 0.1520 -0.0433 0.0159  -0.0002 89  ALA   B N   
5229 C  CA  . ALA   B 89  ? 0.1614 0.1551 0.1407 -0.0404 0.0038  0.0066  89  ALA   B CA  
5230 C  C   . ALA   B 89  ? 0.1714 0.1645 0.1414 -0.0421 0.0085  0.0046  89  ALA   B C   
5231 O  O   . ALA   B 89  ? 0.1512 0.1730 0.1750 -0.0406 0.0169  -0.0260 89  ALA   B O   
5232 C  CB  . ALA   B 89  ? 0.1525 0.1579 0.1616 -0.0386 0.0089  0.0167  89  ALA   B CB  
5238 N  N   . LYS   B 90  ? 0.2076 0.1461 0.1558 -0.0478 -0.0133 0.0083  90  LYS   B N   
5239 C  CA  . LYS   B 90  ? 0.2229 0.1422 0.1545 -0.0458 -0.0127 0.0093  90  LYS   B CA  
5240 C  C   . LYS   B 90  ? 0.2051 0.1343 0.1654 -0.0433 -0.0113 -0.0005 90  LYS   B C   
5241 O  O   . LYS   B 90  ? 0.2143 0.1488 0.1786 -0.0586 -0.0019 0.0019  90  LYS   B O   
5242 C  CB  . LYS   B 90  ? 0.2491 0.1496 0.1800 -0.0408 -0.0016 0.0204  90  LYS   B CB  
5243 C  CG  . LYS   B 90  ? 0.2553 0.1660 0.1747 -0.0280 0.0285  0.0210  90  LYS   B CG  
5244 C  CD  . LYS   B 90  ? 0.2800 0.1866 0.2110 -0.0172 0.0515  0.0015  90  LYS   B CD  
5245 C  CE  . LYS   B 90  ? 0.2985 0.2012 0.2622 -0.0240 0.0621  -0.0112 90  LYS   B CE  
5246 N  NZ  . LYS   B 90  ? 0.3127 0.1905 0.2543 -0.0334 0.0807  -0.0155 90  LYS   B NZ  
5260 N  N   . HIS   B 91  ? 0.1768 0.1266 0.1492 -0.0341 -0.0184 0.0085  91  HIS   B N   
5261 C  CA  . HIS   B 91  ? 0.1627 0.1333 0.1547 -0.0244 -0.0196 0.0074  91  HIS   B CA  
5262 C  C   . HIS   B 91  ? 0.1517 0.1366 0.1297 -0.0273 -0.0006 0.0071  91  HIS   B C   
5263 O  O   . HIS   B 91  ? 0.1687 0.1397 0.1402 -0.0283 -0.0226 0.0052  91  HIS   B O   
5264 C  CB  . HIS   B 91  ? 0.1808 0.1353 0.1876 -0.0110 -0.0072 0.0154  91  HIS   B CB  
5265 C  CG  . HIS   B 91  ? 0.2243 0.1538 0.2617 -0.0009 0.0208  0.0229  91  HIS   B CG  
5266 N  ND1 . HIS   B 91  ? 0.2514 0.1581 0.3183 0.0013  0.0321  0.0054  91  HIS   B ND1 
5267 C  CD2 . HIS   B 91  ? 0.2342 0.1860 0.3088 0.0155  0.0094  0.0502  91  HIS   B CD2 
5268 C  CE1 . HIS   B 91  ? 0.2542 0.1745 0.3326 0.0166  0.0350  0.0111  91  HIS   B CE1 
5269 N  NE2 . HIS   B 91  ? 0.2472 0.1889 0.3366 0.0307  0.0239  0.0522  91  HIS   B NE2 
5277 N  N   . CYS   B 92  ? 0.1450 0.1340 0.1407 -0.0295 -0.0137 0.0027  92  CYS   B N   
5278 C  CA  . CYS   B 92  ? 0.1437 0.1295 0.1381 -0.0251 -0.0076 -0.0008 92  CYS   B CA  
5279 C  C   . CYS   B 92  ? 0.1417 0.1213 0.1414 -0.0190 -0.0024 0.0062  92  CYS   B C   
5280 O  O   . CYS   B 92  ? 0.1532 0.1306 0.1656 -0.0163 -0.0042 -0.0029 92  CYS   B O   
5281 C  CB  . CYS   B 92  ? 0.1467 0.1397 0.1459 -0.0168 -0.0080 0.0034  92  CYS   B CB  
5282 S  SG  . CYS   B 92  ? 0.1476 0.1418 0.1425 -0.0145 -0.0119 0.0056  92  CYS   B SG  
5288 N  N   . LEU   B 93  ? 0.1343 0.1285 0.1490 -0.0132 -0.0096 -0.0013 93  LEU   B N   
5289 C  CA  . LEU   B 93  ? 0.1330 0.1251 0.1548 -0.0066 -0.0133 0.0061  93  LEU   B CA  
5290 C  C   . LEU   B 93  ? 0.1301 0.1253 0.1361 -0.0078 -0.0103 0.0083  93  LEU   B C   
5291 O  O   . LEU   B 93  ? 0.1385 0.1229 0.1664 -0.0075 -0.0122 0.0030  93  LEU   B O   
5292 C  CB  . LEU   B 93  ? 0.1389 0.1263 0.1717 -0.0016 -0.0186 0.0052  93  LEU   B CB  
5293 C  CG  . LEU   B 93  ? 0.1388 0.1403 0.1824 -0.0077 -0.0131 0.0157  93  LEU   B CG  
5294 C  CD1 . LEU   B 93  ? 0.1395 0.1485 0.1808 0.0046  -0.0049 0.0035  93  LEU   B CD1 
5295 C  CD2 . LEU   B 93  ? 0.1403 0.1383 0.1939 -0.0050 -0.0167 0.0070  93  LEU   B CD2 
5307 N  N   . HIS   B 94  ? 0.1361 0.1259 0.1381 -0.0067 -0.0149 0.0067  94  HIS   B N   
5308 C  CA  . HIS   B 94  ? 0.1381 0.1281 0.1445 -0.0031 -0.0106 0.0079  94  HIS   B CA  
5309 C  C   . HIS   B 94  ? 0.1378 0.1265 0.1679 -0.0032 -0.0068 0.0112  94  HIS   B C   
5310 O  O   . HIS   B 94  ? 0.1408 0.1389 0.1945 -0.0056 0.0154  -0.0007 94  HIS   B O   
5311 C  CB  . HIS   B 94  ? 0.1358 0.1313 0.1618 -0.0007 -0.0210 0.0035  94  HIS   B CB  
5312 C  CG  . HIS   B 94  ? 0.1399 0.1269 0.1513 -0.0080 -0.0234 0.0042  94  HIS   B CG  
5313 N  ND1 . HIS   B 94  ? 0.1472 0.1329 0.1560 -0.0076 -0.0197 0.0044  94  HIS   B ND1 
5314 C  CD2 . HIS   B 94  ? 0.1421 0.1348 0.1529 -0.0044 -0.0168 0.0066  94  HIS   B CD2 
5315 C  CE1 . HIS   B 94  ? 0.1529 0.1324 0.1492 -0.0164 -0.0217 0.0065  94  HIS   B CE1 
5316 N  NE2 . HIS   B 94  ? 0.1409 0.1386 0.1584 -0.0227 -0.0185 0.0077  94  HIS   B NE2 
5324 N  N   . VAL   B 95  ? 0.1287 0.1224 0.1686 0.0014  -0.0018 0.0030  95  VAL   B N   
5325 C  CA  . VAL   B 95  ? 0.1304 0.1316 0.1601 -0.0033 0.0054  0.0147  95  VAL   B CA  
5326 C  C   . VAL   B 95  ? 0.1417 0.1308 0.1688 -0.0025 0.0092  0.0107  95  VAL   B C   
5327 O  O   . VAL   B 95  ? 0.1481 0.1300 0.1936 0.0051  0.0047  0.0221  95  VAL   B O   
5328 C  CB  . VAL   B 95  ? 0.1404 0.1330 0.1628 -0.0071 -0.0086 0.0125  95  VAL   B CB  
5329 C  CG1 . VAL   B 95  ? 0.1534 0.1499 0.1892 -0.0105 -0.0025 0.0185  95  VAL   B CG1 
5330 C  CG2 . VAL   B 95  ? 0.1455 0.1309 0.1566 0.0023  -0.0091 0.0059  95  VAL   B CG2 
5340 N  N   . VAL   B 96  ? 0.1536 0.1372 0.1670 0.0061  0.0067  0.0191  96  VAL   B N   
5341 C  CA  . VAL   B 96  ? 0.1613 0.1472 0.1585 0.0062  0.0106  0.0212  96  VAL   B CA  
5342 C  C   . VAL   B 96  ? 0.1675 0.1539 0.1741 0.0037  0.0145  0.0222  96  VAL   B C   
5343 O  O   . VAL   B 96  ? 0.1650 0.1652 0.1925 -0.0008 0.0176  0.0085  96  VAL   B O   
5344 C  CB  . VAL   B 96  ? 0.1685 0.1711 0.1685 0.0081  0.0090  0.0151  96  VAL   B CB  
5345 C  CG1 . VAL   B 96  ? 0.1639 0.1914 0.1699 0.0158  0.0136  0.0108  96  VAL   B CG1 
5346 C  CG2 . VAL   B 96  ? 0.1748 0.1768 0.1825 0.0015  0.0090  0.0046  96  VAL   B CG2 
5356 N  N   . GLY   B 97  ? 0.1766 0.1546 0.1654 0.0021  0.0029  0.0310  97  GLY   B N   
5357 C  CA  . GLY   B 97  ? 0.1964 0.1579 0.1868 0.0036  0.0161  0.0277  97  GLY   B CA  
5358 C  C   . GLY   B 97  ? 0.2154 0.1693 0.1989 0.0144  0.0166  0.0239  97  GLY   B C   
5359 O  O   . GLY   B 97  ? 0.2298 0.1761 0.1888 0.0049  0.0144  0.0142  97  GLY   B O   
5363 N  N   . PRO   B 98  ? 0.2306 0.1710 0.2116 0.0117  0.0377  0.0423  98  PRO   B N   
5364 C  CA  . PRO   B 98  ? 0.2438 0.1942 0.2160 0.0250  0.0518  0.0363  98  PRO   B CA  
5365 C  C   . PRO   B 98  ? 0.2597 0.1938 0.1843 0.0424  0.0591  0.0592  98  PRO   B C   
5366 O  O   . PRO   B 98  ? 0.2491 0.1857 0.2101 0.0319  0.0584  0.0578  98  PRO   B O   
5367 C  CB  . PRO   B 98  ? 0.2307 0.2007 0.2286 0.0181  0.0621  0.0347  98  PRO   B CB  
5368 C  CG  . PRO   B 98  ? 0.2241 0.1888 0.2312 0.0101  0.0560  0.0529  98  PRO   B CG  
5369 C  CD  . PRO   B 98  ? 0.2155 0.1755 0.2282 0.0166  0.0458  0.0505  98  PRO   B CD  
5377 N  N   . ASN   B 99  ? 0.2747 0.2189 0.2024 0.0609  0.0616  0.0405  99  ASN   B N   
5378 C  CA  . ASN   B 99  ? 0.2968 0.2264 0.2128 0.0684  0.0491  0.0638  99  ASN   B CA  
5379 C  C   . ASN   B 99  ? 0.3257 0.2661 0.2592 0.0623  0.0660  0.0955  99  ASN   B C   
5380 O  O   . ASN   B 99  ? 0.3327 0.2743 0.2635 0.0628  0.0575  0.0948  99  ASN   B O   
5381 C  CB  . ASN   B 99  ? 0.3050 0.2213 0.2062 0.0675  0.0365  0.0537  99  ASN   B CB  
5382 C  CG  . ASN   B 99  ? 0.3084 0.2284 0.2282 0.0622  0.0262  0.0472  99  ASN   B CG  
5383 O  OD1 . ASN   B 99  ? 0.3079 0.2299 0.2501 0.0696  0.0310  0.0509  99  ASN   B OD1 
5384 N  ND2 . ASN   B 99  ? 0.3030 0.2246 0.2341 0.0655  0.0006  0.0469  99  ASN   B ND2 
5391 N  N   A VAL   B 100 ? 0.3430 0.2789 0.2941 0.0510  0.0729  0.1219  100 VAL   B N   
5392 N  N   B VAL   B 100 ? 0.3466 0.2814 0.2954 0.0534  0.0600  0.1108  100 VAL   B N   
5393 C  CA  A VAL   B 100 ? 0.3710 0.3010 0.3398 0.0384  0.0655  0.1410  100 VAL   B CA  
5394 C  CA  B VAL   B 100 ? 0.3730 0.3014 0.3332 0.0435  0.0482  0.1225  100 VAL   B CA  
5395 C  C   A VAL   B 100 ? 0.3948 0.3115 0.3336 0.0442  0.0575  0.1557  100 VAL   B C   
5396 C  C   B VAL   B 100 ? 0.3944 0.3107 0.3325 0.0468  0.0440  0.1425  100 VAL   B C   
5397 O  O   A VAL   B 100 ? 0.4021 0.3228 0.3369 0.0413  0.0659  0.1515  100 VAL   B O   
5398 O  O   B VAL   B 100 ? 0.3986 0.3167 0.3329 0.0436  0.0469  0.1384  100 VAL   B O   
5399 C  CB  A VAL   B 100 ? 0.3763 0.3149 0.3979 0.0168  0.0636  0.1468  100 VAL   B CB  
5400 C  CB  B VAL   B 100 ? 0.3781 0.3130 0.3732 0.0289  0.0413  0.1173  100 VAL   B CB  
5401 C  CG1 A VAL   B 100 ? 0.3796 0.3208 0.4199 0.0109  0.0631  0.1473  100 VAL   B CG1 
5402 C  CG1 B VAL   B 100 ? 0.3806 0.3177 0.3878 0.0245  0.0397  0.1155  100 VAL   B CG1 
5403 C  CG2 A VAL   B 100 ? 0.3756 0.3193 0.4148 0.0090  0.0660  0.1512  100 VAL   B CG2 
5404 C  CG2 B VAL   B 100 ? 0.3787 0.3169 0.3863 0.0238  0.0399  0.1161  100 VAL   B CG2 
5423 N  N   . ASN   B 101 ? 0.4105 0.3150 0.3353 0.0546  0.0377  0.1574  101 ASN   B N   
5424 C  CA  . ASN   B 101 ? 0.4476 0.3315 0.3446 0.0640  0.0189  0.1608  101 ASN   B CA  
5425 C  C   . ASN   B 101 ? 0.4890 0.3787 0.3572 0.0613  0.0101  0.1652  101 ASN   B C   
5426 O  O   . ASN   B 101 ? 0.4914 0.3904 0.3795 0.0672  0.0124  0.1401  101 ASN   B O   
5427 C  CB  . ASN   B 101 ? 0.4464 0.3121 0.3543 0.0633  0.0215  0.1363  101 ASN   B CB  
5428 C  CG  . ASN   B 101 ? 0.4425 0.2926 0.3593 0.0651  0.0229  0.1260  101 ASN   B CG  
5429 O  OD1 . ASN   B 101 ? 0.4440 0.2900 0.3807 0.0570  0.0380  0.1190  101 ASN   B OD1 
5430 N  ND2 . ASN   B 101 ? 0.4379 0.2841 0.3572 0.0692  0.0196  0.1119  101 ASN   B ND2 
5438 N  N   . LYS   B 102 ? 0.5255 0.4202 0.3877 0.0475  0.0129  0.1615  102 LYS   B N   
5439 C  CA  . LYS   B 102 ? 0.5592 0.4653 0.4240 0.0304  0.0201  0.1356  102 LYS   B CA  
5440 C  C   . LYS   B 102 ? 0.5553 0.4677 0.4053 0.0259  0.0248  0.1463  102 LYS   B C   
5441 O  O   . LYS   B 102 ? 0.5637 0.4712 0.4054 0.0246  0.0139  0.1507  102 LYS   B O   
5442 C  CB  . LYS   B 102 ? 0.5919 0.5047 0.4884 0.0198  0.0302  0.0877  102 LYS   B CB  
5443 C  CG  . LYS   B 102 ? 0.6190 0.5381 0.5509 0.0113  0.0397  0.0412  102 LYS   B CG  
5444 C  CD  . LYS   B 102 ? 0.6418 0.5654 0.6125 0.0044  0.0489  0.0032  102 LYS   B CD  
5445 C  CE  . LYS   B 102 ? 0.6583 0.5850 0.6600 -0.0012 0.0552  -0.0233 102 LYS   B CE  
5446 N  NZ  . LYS   B 102 ? 0.6675 0.5961 0.6878 -0.0043 0.0569  -0.0379 102 LYS   B NZ  
5460 N  N   . GLY   B 103 ? 0.5388 0.4634 0.4057 0.0221  0.0402  0.1399  103 GLY   B N   
5461 C  CA  . GLY   B 103 ? 0.5199 0.4570 0.4157 0.0206  0.0552  0.1210  103 GLY   B CA  
5462 C  C   . GLY   B 103 ? 0.4965 0.4465 0.4112 0.0171  0.0683  0.0998  103 GLY   B C   
5463 O  O   . GLY   B 103 ? 0.5011 0.4519 0.4169 0.0174  0.0697  0.1036  103 GLY   B O   
5467 N  N   A GLU   B 104 ? 0.4821 0.4378 0.3982 0.0152  0.0834  0.0860  104 GLU   B N   
5468 N  N   B GLU   B 104 ? 0.4801 0.4368 0.4041 0.0145  0.0647  0.0795  104 GLU   B N   
5469 C  CA  A GLU   B 104 ? 0.4667 0.4279 0.3824 0.0163  0.0930  0.0681  104 GLU   B CA  
5470 C  CA  B GLU   B 104 ? 0.4627 0.4258 0.3929 0.0133  0.0591  0.0558  104 GLU   B CA  
5471 C  C   A GLU   B 104 ? 0.4638 0.4246 0.3868 0.0033  0.1316  0.0729  104 GLU   B C   
5472 C  C   B GLU   B 104 ? 0.4570 0.4237 0.4000 0.0068  0.0744  0.0494  104 GLU   B C   
5473 O  O   A GLU   B 104 ? 0.4624 0.4271 0.3953 0.0005  0.1379  0.0734  104 GLU   B O   
5474 O  O   B GLU   B 104 ? 0.4566 0.4245 0.4048 0.0053  0.0772  0.0483  104 GLU   B O   
5475 C  CB  A GLU   B 104 ? 0.4568 0.4195 0.3676 0.0312  0.0596  0.0369  104 GLU   B CB  
5476 C  CB  B GLU   B 104 ? 0.4522 0.4157 0.3758 0.0188  0.0372  0.0339  104 GLU   B CB  
5477 C  CG  A GLU   B 104 ? 0.4472 0.4119 0.3478 0.0457  0.0232  0.0037  104 GLU   B CG  
5478 C  CG  B GLU   B 104 ? 0.4427 0.4065 0.3576 0.0242  0.0144  0.0110  104 GLU   B CG  
5479 C  CD  A GLU   B 104 ? 0.4385 0.4040 0.3237 0.0583  -0.0057 -0.0213 104 GLU   B CD  
5480 C  CD  B GLU   B 104 ? 0.4350 0.3980 0.3396 0.0286  -0.0034 -0.0065 104 GLU   B CD  
5481 O  OE1 A GLU   B 104 ? 0.4299 0.3951 0.2950 0.0649  -0.0076 -0.0315 104 GLU   B OE1 
5482 O  OE1 B GLU   B 104 ? 0.4298 0.3923 0.3242 0.0298  -0.0052 -0.0119 104 GLU   B OE1 
5483 O  OE2 A GLU   B 104 ? 0.4377 0.4053 0.3159 0.0618  -0.0258 -0.0345 104 GLU   B OE2 
5484 O  OE2 B GLU   B 104 ? 0.4333 0.3965 0.3331 0.0306  -0.0152 -0.0155 104 GLU   B OE2 
5497 N  N   A ASP   B 105 ? 0.4581 0.4174 0.3788 -0.0055 0.1617  0.0742  105 ASP   B N   
5498 N  N   B ASP   B 105 ? 0.4502 0.4197 0.3987 0.0024  0.0860  0.0427  105 ASP   B N   
5499 C  CA  A ASP   B 105 ? 0.4533 0.4114 0.3892 -0.0123 0.1837  0.0591  105 ASP   B CA  
5500 C  CA  B ASP   B 105 ? 0.4440 0.4153 0.4055 -0.0015 0.0941  0.0296  105 ASP   B CA  
5501 C  C   A ASP   B 105 ? 0.4340 0.3835 0.3498 -0.0258 0.1925  0.0562  105 ASP   B C   
5502 C  C   B ASP   B 105 ? 0.4311 0.4007 0.3788 -0.0075 0.0973  0.0234  105 ASP   B C   
5503 O  O   A ASP   B 105 ? 0.4242 0.3786 0.3184 -0.0238 0.2014  0.0610  105 ASP   B O   
5504 O  O   B ASP   B 105 ? 0.4300 0.3994 0.3641 -0.0065 0.1022  0.0247  105 ASP   B O   
5505 C  CB  A ASP   B 105 ? 0.4681 0.4298 0.4530 -0.0036 0.1845  0.0395  105 ASP   B CB  
5506 C  CB  B ASP   B 105 ? 0.4487 0.4239 0.4424 0.0021  0.0964  0.0208  105 ASP   B CB  
5507 C  CG  A ASP   B 105 ? 0.4783 0.4433 0.5134 0.0017  0.1876  0.0256  105 ASP   B CG  
5508 C  CG  B ASP   B 105 ? 0.4522 0.4297 0.4782 0.0038  0.0992  0.0151  105 ASP   B CG  
5509 O  OD1 A ASP   B 105 ? 0.4771 0.4463 0.5220 -0.0019 0.2005  0.0299  105 ASP   B OD1 
5510 O  OD1 B ASP   B 105 ? 0.4519 0.4314 0.4863 0.0018  0.1028  0.0165  105 ASP   B OD1 
5511 O  OD2 A ASP   B 105 ? 0.4839 0.4496 0.5457 0.0081  0.1801  0.0125  105 ASP   B OD2 
5512 O  OD2 B ASP   B 105 ? 0.4530 0.4323 0.4932 0.0054  0.0995  0.0112  105 ASP   B OD2 
5521 N  N   A ILE   B 106 ? 0.4200 0.3589 0.3506 -0.0369 0.1867  0.0533  106 ILE   B N   
5522 N  N   B ILE   B 106 ? 0.4184 0.3864 0.3685 -0.0122 0.0926  0.0184  106 ILE   B N   
5523 C  CA  A ILE   B 106 ? 0.3997 0.3312 0.3551 -0.0538 0.1901  0.0500  106 ILE   B CA  
5524 C  CA  B ILE   B 106 ? 0.4038 0.3726 0.3647 -0.0175 0.0915  0.0130  106 ILE   B CA  
5525 C  C   A ILE   B 106 ? 0.3703 0.3231 0.3502 -0.0472 0.1877  0.0355  106 ILE   B C   
5526 C  C   B ILE   B 106 ? 0.3832 0.3639 0.3587 -0.0143 0.0913  0.0049  106 ILE   B C   
5527 O  O   A ILE   B 106 ? 0.3624 0.3073 0.3473 -0.0506 0.1924  0.0350  106 ILE   B O   
5528 O  O   B ILE   B 106 ? 0.3810 0.3586 0.3537 -0.0163 0.0891  0.0015  106 ILE   B O   
5529 C  CB  A ILE   B 106 ? 0.4145 0.3195 0.3741 -0.0683 0.1802  0.0527  106 ILE   B CB  
5530 C  CB  B ILE   B 106 ? 0.4107 0.3709 0.3707 -0.0240 0.0889  0.0138  106 ILE   B CB  
5531 C  CG1 A ILE   B 106 ? 0.4214 0.3192 0.3850 -0.0626 0.1637  0.0395  106 ILE   B CG1 
5532 C  CG1 B ILE   B 106 ? 0.4133 0.3699 0.3734 -0.0233 0.0830  0.0119  106 ILE   B CG1 
5533 C  CG2 A ILE   B 106 ? 0.4192 0.3186 0.3875 -0.0777 0.1830  0.0608  106 ILE   B CG2 
5534 C  CG2 B ILE   B 106 ? 0.4135 0.3728 0.3778 -0.0271 0.0903  0.0151  106 ILE   B CG2 
5535 C  CD1 A ILE   B 106 ? 0.4248 0.3207 0.3819 -0.0584 0.1572  0.0358  106 ILE   B CD1 
5536 C  CD1 B ILE   B 106 ? 0.4145 0.3696 0.3739 -0.0223 0.0800  0.0112  106 ILE   B CD1 
5559 N  N   A GLN   B 107 ? 0.3514 0.3332 0.3641 -0.0406 0.1744  0.0305  107 GLN   B N   
5560 N  N   B GLN   B 107 ? 0.3660 0.3619 0.3673 -0.0114 0.0907  0.0033  107 GLN   B N   
5561 C  CA  A GLN   B 107 ? 0.3313 0.3421 0.3797 -0.0333 0.1503  0.0257  107 GLN   B CA  
5562 C  CA  B GLN   B 107 ? 0.3482 0.3581 0.3777 -0.0081 0.0868  0.0056  107 GLN   B CA  
5563 C  C   A GLN   B 107 ? 0.2982 0.3204 0.3480 -0.0196 0.1286  0.0136  107 GLN   B C   
5564 C  C   B GLN   B 107 ? 0.3132 0.3315 0.3459 -0.0035 0.0944  0.0044  107 GLN   B C   
5565 O  O   A GLN   B 107 ? 0.2862 0.3199 0.3637 -0.0160 0.1110  -0.0047 107 GLN   B O   
5566 O  O   B GLN   B 107 ? 0.3098 0.3337 0.3510 -0.0020 0.0850  -0.0056 107 GLN   B O   
5567 C  CB  A GLN   B 107 ? 0.3588 0.3760 0.4505 -0.0296 0.1200  0.0243  107 GLN   B CB  
5568 C  CB  B GLN   B 107 ? 0.3685 0.3808 0.4316 -0.0068 0.0687  0.0064  107 GLN   B CB  
5569 C  CG  A GLN   B 107 ? 0.3867 0.4056 0.5160 -0.0219 0.0844  0.0235  107 GLN   B CG  
5570 C  CG  B GLN   B 107 ? 0.3873 0.4004 0.4822 -0.0036 0.0493  0.0080  107 GLN   B CG  
5571 C  CD  A GLN   B 107 ? 0.4080 0.4282 0.5670 -0.0182 0.0593  0.0258  107 GLN   B CD  
5572 C  CD  B GLN   B 107 ? 0.4021 0.4154 0.5232 -0.0022 0.0346  0.0103  107 GLN   B CD  
5573 O  OE1 A GLN   B 107 ? 0.4158 0.4372 0.5851 -0.0152 0.0549  0.0232  107 GLN   B OE1 
5574 O  OE1 B GLN   B 107 ? 0.4073 0.4211 0.5369 -0.0014 0.0326  0.0098  107 GLN   B OE1 
5575 N  NE2 A GLN   B 107 ? 0.4167 0.4350 0.5848 -0.0154 0.0479  0.0302  107 GLN   B NE2 
5576 N  NE2 B GLN   B 107 ? 0.4080 0.4200 0.5379 -0.0007 0.0280  0.0127  107 GLN   B NE2 
5593 N  N   . LEU   B 108 ? 0.2808 0.3021 0.3209 0.0045  0.1057  0.0113  108 LEU   B N   
5594 C  CA  . LEU   B 108 ? 0.2497 0.2645 0.2737 0.0241  0.0847  0.0291  108 LEU   B CA  
5595 C  C   . LEU   B 108 ? 0.2050 0.2111 0.2627 0.0265  0.0568  0.0348  108 LEU   B C   
5596 O  O   . LEU   B 108 ? 0.2000 0.1968 0.2561 0.0264  0.0433  0.0340  108 LEU   B O   
5597 C  CB  . LEU   B 108 ? 0.2631 0.2828 0.2639 0.0292  0.0810  0.0442  108 LEU   B CB  
5598 C  CG  . LEU   B 108 ? 0.2782 0.3108 0.2757 0.0304  0.0778  0.0207  108 LEU   B CG  
5599 C  CD1 . LEU   B 108 ? 0.2894 0.3240 0.2623 0.0266  0.0816  0.0196  108 LEU   B CD1 
5600 C  CD2 . LEU   B 108 ? 0.2854 0.3205 0.2858 0.0381  0.0681  0.0020  108 LEU   B CD2 
5613 N  N   . LEU   B 109 ? 0.1857 0.1874 0.2643 0.0115  0.0502  0.0321  109 LEU   B N   
5614 C  CA  . LEU   B 109 ? 0.1656 0.1542 0.2771 0.0059  0.0466  0.0354  109 LEU   B CA  
5615 C  C   . LEU   B 109 ? 0.1534 0.1404 0.2721 0.0007  0.0413  0.0219  109 LEU   B C   
5616 O  O   . LEU   B 109 ? 0.1526 0.1400 0.2593 0.0016  0.0373  0.0342  109 LEU   B O   
5617 C  CB  . LEU   B 109 ? 0.1746 0.1494 0.2839 0.0034  0.0311  0.0427  109 LEU   B CB  
5618 C  CG  . LEU   B 109 ? 0.1706 0.1487 0.2730 0.0030  0.0250  0.0227  109 LEU   B CG  
5619 C  CD1 . LEU   B 109 ? 0.1634 0.1538 0.2547 0.0163  0.0315  0.0221  109 LEU   B CD1 
5620 C  CD2 . LEU   B 109 ? 0.1827 0.1519 0.2850 0.0037  0.0184  0.0335  109 LEU   B CD2 
5632 N  N   . LYS   B 110 ? 0.1504 0.1436 0.2702 -0.0072 0.0394  0.0276  110 LYS   B N   
5633 C  CA  . LYS   B 110 ? 0.1502 0.1419 0.2686 -0.0068 0.0299  0.0217  110 LYS   B CA  
5634 C  C   . LYS   B 110 ? 0.1436 0.1427 0.2618 -0.0015 0.0318  0.0154  110 LYS   B C   
5635 O  O   . LYS   B 110 ? 0.1416 0.1421 0.2555 -0.0045 0.0288  0.0106  110 LYS   B O   
5636 C  CB  . LYS   B 110 ? 0.1530 0.1420 0.2835 -0.0043 0.0331  0.0230  110 LYS   B CB  
5637 C  CG  . LYS   B 110 ? 0.1532 0.1445 0.3006 -0.0028 0.0191  0.0260  110 LYS   B CG  
5638 C  CD  . LYS   B 110 ? 0.1586 0.1429 0.3061 -0.0113 0.0190  0.0246  110 LYS   B CD  
5639 C  CE  . LYS   B 110 ? 0.1572 0.1581 0.3232 -0.0056 0.0098  0.0107  110 LYS   B CE  
5640 N  NZ  . LYS   B 110 ? 0.1580 0.1771 0.3145 0.0008  0.0024  0.0072  110 LYS   B NZ  
5654 N  N   . SER   B 111 ? 0.1497 0.1456 0.2739 -0.0049 0.0349  0.0192  111 SER   B N   
5655 C  CA  . SER   B 111 ? 0.1609 0.1450 0.2593 -0.0030 0.0290  0.0263  111 SER   B CA  
5656 C  C   . SER   B 111 ? 0.1527 0.1384 0.2415 -0.0015 0.0244  0.0141  111 SER   B C   
5657 O  O   . SER   B 111 ? 0.1442 0.1421 0.2464 -0.0017 0.0144  0.0041  111 SER   B O   
5658 C  CB  . SER   B 111 ? 0.1679 0.1694 0.2711 0.0032  0.0433  0.0373  111 SER   B CB  
5659 O  OG  . SER   B 111 ? 0.1823 0.2027 0.2826 0.0097  0.0529  0.0403  111 SER   B OG  
5665 N  N   . ALA   B 112 ? 0.1426 0.1424 0.2534 0.0070  0.0282  0.0201  112 ALA   B N   
5666 C  CA  . ALA   B 112 ? 0.1421 0.1496 0.2351 0.0008  0.0108  0.0064  112 ALA   B CA  
5667 C  C   . ALA   B 112 ? 0.1350 0.1391 0.2287 -0.0019 0.0083  0.0032  112 ALA   B C   
5668 O  O   . ALA   B 112 ? 0.1371 0.1410 0.2321 -0.0092 0.0112  0.0023  112 ALA   B O   
5669 C  CB  . ALA   B 112 ? 0.1419 0.1497 0.2517 0.0075  0.0156  0.0170  112 ALA   B CB  
5675 N  N   . TYR   B 113 ? 0.1319 0.1284 0.2406 -0.0035 0.0146  0.0066  113 TYR   B N   
5676 C  CA  . TYR   B 113 ? 0.1320 0.1241 0.2370 -0.0038 0.0132  0.0018  113 TYR   B CA  
5677 C  C   . TYR   B 113 ? 0.1306 0.1213 0.2357 -0.0138 0.0161  0.0055  113 TYR   B C   
5678 O  O   . TYR   B 113 ? 0.1323 0.1268 0.2279 -0.0097 0.0063  0.0021  113 TYR   B O   
5679 C  CB  . TYR   B 113 ? 0.1392 0.1233 0.2358 -0.0020 0.0185  0.0106  113 TYR   B CB  
5680 C  CG  . TYR   B 113 ? 0.1378 0.1237 0.2491 -0.0041 0.0100  0.0134  113 TYR   B CG  
5681 C  CD1 . TYR   B 113 ? 0.1417 0.1348 0.2584 -0.0076 0.0132  0.0187  113 TYR   B CD1 
5682 C  CD2 . TYR   B 113 ? 0.1452 0.1245 0.2486 -0.0059 0.0101  0.0140  113 TYR   B CD2 
5683 C  CE1 . TYR   B 113 ? 0.1419 0.1348 0.2547 -0.0049 0.0215  0.0088  113 TYR   B CE1 
5684 C  CE2 . TYR   B 113 ? 0.1529 0.1196 0.2616 -0.0030 0.0189  0.0161  113 TYR   B CE2 
5685 C  CZ  . TYR   B 113 ? 0.1423 0.1236 0.2631 0.0010  0.0147  0.0116  113 TYR   B CZ  
5686 O  OH  . TYR   B 113 ? 0.1513 0.1195 0.2955 0.0102  0.0252  0.0113  113 TYR   B OH  
5696 N  N   . GLU   B 114 ? 0.1265 0.1170 0.2458 -0.0066 0.0192  0.0055  114 GLU   B N   
5697 C  CA  . GLU   B 114 ? 0.1275 0.1181 0.2410 0.0010  0.0113  0.0037  114 GLU   B CA  
5698 C  C   . GLU   B 114 ? 0.1276 0.1190 0.2329 -0.0059 0.0087  0.0048  114 GLU   B C   
5699 O  O   . GLU   B 114 ? 0.1263 0.1187 0.2430 -0.0016 0.0021  0.0078  114 GLU   B O   
5700 C  CB  . GLU   B 114 ? 0.1311 0.1261 0.2430 -0.0007 0.0177  0.0080  114 GLU   B CB  
5701 C  CG  . GLU   B 114 ? 0.1379 0.1260 0.2433 -0.0058 0.0123  0.0104  114 GLU   B CG  
5702 C  CD  . GLU   B 114 ? 0.1311 0.1325 0.2532 -0.0105 0.0088  0.0104  114 GLU   B CD  
5703 O  OE1 . GLU   B 114 ? 0.1302 0.1451 0.2505 -0.0098 0.0260  0.0144  114 GLU   B OE1 
5704 O  OE2 . GLU   B 114 ? 0.1339 0.1516 0.2729 -0.0185 0.0177  0.0085  114 GLU   B OE2 
5711 N  N   . ASN   B 115 ? 0.1328 0.1145 0.2267 -0.0046 -0.0033 0.0060  115 ASN   B N   
5712 C  CA  . ASN   B 115 ? 0.1314 0.1245 0.1986 -0.0135 -0.0002 0.0087  115 ASN   B CA  
5713 C  C   . ASN   B 115 ? 0.1258 0.1197 0.2107 -0.0169 -0.0022 -0.0014 115 ASN   B C   
5714 O  O   . ASN   B 115 ? 0.1387 0.1212 0.2204 -0.0146 0.0018  0.0044  115 ASN   B O   
5715 C  CB  . ASN   B 115 ? 0.1464 0.1339 0.2091 -0.0115 0.0072  0.0016  115 ASN   B CB  
5716 C  CG  . ASN   B 115 ? 0.1551 0.1405 0.2083 -0.0001 0.0050  -0.0007 115 ASN   B CG  
5717 O  OD1 . ASN   B 115 ? 0.1943 0.1564 0.2248 0.0044  0.0108  -0.0052 115 ASN   B OD1 
5718 N  ND2 . ASN   B 115 ? 0.1486 0.1523 0.2125 -0.0061 0.0082  0.0074  115 ASN   B ND2 
5725 N  N   . PHE   B 116 ? 0.1274 0.1224 0.2040 -0.0052 0.0018  -0.0038 116 PHE   B N   
5726 C  CA  . PHE   B 116 ? 0.1340 0.1257 0.2064 -0.0124 -0.0091 0.0090  116 PHE   B CA  
5727 C  C   . PHE   B 116 ? 0.1349 0.1122 0.2112 -0.0158 -0.0094 0.0090  116 PHE   B C   
5728 O  O   . PHE   B 116 ? 0.1399 0.1261 0.2136 -0.0054 -0.0087 0.0103  116 PHE   B O   
5729 C  CB  . PHE   B 116 ? 0.1292 0.1216 0.1988 -0.0085 -0.0136 0.0089  116 PHE   B CB  
5730 C  CG  . PHE   B 116 ? 0.1245 0.1227 0.2025 -0.0101 -0.0027 0.0066  116 PHE   B CG  
5731 C  CD1 . PHE   B 116 ? 0.1372 0.1290 0.2138 -0.0035 -0.0007 0.0062  116 PHE   B CD1 
5732 C  CD2 . PHE   B 116 ? 0.1297 0.1333 0.2058 -0.0087 0.0022  0.0027  116 PHE   B CD2 
5733 C  CE1 . PHE   B 116 ? 0.1399 0.1327 0.2183 -0.0030 -0.0121 0.0086  116 PHE   B CE1 
5734 C  CE2 . PHE   B 116 ? 0.1277 0.1327 0.2055 -0.0056 -0.0036 0.0036  116 PHE   B CE2 
5735 C  CZ  . PHE   B 116 ? 0.1232 0.1318 0.2040 -0.0028 -0.0100 0.0095  116 PHE   B CZ  
5745 N  N   . ASN   B 117 ? 0.1328 0.1211 0.2222 -0.0090 -0.0097 0.0075  117 ASN   B N   
5746 C  CA  . ASN   B 117 ? 0.1381 0.1190 0.2240 0.0013  -0.0101 0.0035  117 ASN   B CA  
5747 C  C   . ASN   B 117 ? 0.1449 0.1207 0.2353 -0.0007 -0.0141 0.0038  117 ASN   B C   
5748 O  O   . ASN   B 117 ? 0.1521 0.1250 0.2697 -0.0056 -0.0372 0.0116  117 ASN   B O   
5749 C  CB  . ASN   B 117 ? 0.1396 0.1215 0.2313 -0.0037 -0.0129 0.0012  117 ASN   B CB  
5750 C  CG  . ASN   B 117 ? 0.1341 0.1317 0.2508 0.0043  -0.0064 -0.0066 117 ASN   B CG  
5751 O  OD1 . ASN   B 117 ? 0.1510 0.1264 0.2650 -0.0155 -0.0014 -0.0028 117 ASN   B OD1 
5752 N  ND2 . ASN   B 117 ? 0.1382 0.1358 0.2448 -0.0015 -0.0000 -0.0049 117 ASN   B ND2 
5759 N  N   . GLN   B 118 ? 0.1414 0.1187 0.2258 -0.0106 -0.0169 0.0003  118 GLN   B N   
5760 C  CA  . GLN   B 118 ? 0.1422 0.1222 0.2484 -0.0044 -0.0146 -0.0025 118 GLN   B CA  
5761 C  C   . GLN   B 118 ? 0.1466 0.1194 0.2470 -0.0014 -0.0132 -0.0011 118 GLN   B C   
5762 O  O   . GLN   B 118 ? 0.1699 0.1208 0.2718 -0.0102 -0.0035 0.0044  118 GLN   B O   
5763 C  CB  . GLN   B 118 ? 0.1516 0.1264 0.2561 -0.0058 -0.0196 -0.0010 118 GLN   B CB  
5764 C  CG  . GLN   B 118 ? 0.1597 0.1278 0.2487 0.0010  -0.0096 -0.0094 118 GLN   B CG  
5765 C  CD  . GLN   B 118 ? 0.1636 0.1251 0.2462 0.0021  -0.0097 -0.0146 118 GLN   B CD  
5766 O  OE1 . GLN   B 118 ? 0.1703 0.1220 0.2714 0.0008  0.0047  0.0021  118 GLN   B OE1 
5767 N  NE2 . GLN   B 118 ? 0.1705 0.1301 0.2503 -0.0050 -0.0112 0.0025  118 GLN   B NE2 
5776 N  N   . HIS   B 119 ? 0.1488 0.1246 0.2122 -0.0112 -0.0177 0.0073  119 HIS   B N   
5777 C  CA  . HIS   B 119 ? 0.1560 0.1394 0.2039 -0.0083 -0.0232 0.0108  119 HIS   B CA  
5778 C  C   . HIS   B 119 ? 0.1600 0.1373 0.1920 -0.0090 -0.0381 0.0040  119 HIS   B C   
5779 O  O   . HIS   B 119 ? 0.1697 0.1363 0.2208 -0.0295 -0.0310 0.0091  119 HIS   B O   
5780 C  CB  . HIS   B 119 ? 0.1625 0.1493 0.2050 -0.0097 -0.0256 -0.0001 119 HIS   B CB  
5781 C  CG  . HIS   B 119 ? 0.1663 0.1738 0.2077 0.0041  -0.0397 -0.0153 119 HIS   B CG  
5782 N  ND1 . HIS   B 119 ? 0.1802 0.1876 0.2416 -0.0018 -0.0415 -0.0286 119 HIS   B ND1 
5783 C  CD2 . HIS   B 119 ? 0.1863 0.1920 0.2081 0.0344  -0.0456 -0.0151 119 HIS   B CD2 
5784 C  CE1 . HIS   B 119 ? 0.1977 0.2041 0.2400 0.0141  -0.0515 -0.0396 119 HIS   B CE1 
5785 N  NE2 . HIS   B 119 ? 0.2001 0.2125 0.2248 0.0295  -0.0495 -0.0404 119 HIS   B NE2 
5793 N  N   . GLU   B 120 ? 0.1798 0.1422 0.1942 -0.0176 -0.0462 0.0203  120 GLU   B N   
5794 C  CA  . GLU   B 120 ? 0.2160 0.1570 0.2172 -0.0104 -0.0579 0.0359  120 GLU   B CA  
5795 C  C   . GLU   B 120 ? 0.1924 0.1436 0.2011 -0.0203 -0.0437 0.0312  120 GLU   B C   
5796 O  O   . GLU   B 120 ? 0.1823 0.1537 0.2125 -0.0181 -0.0495 0.0176  120 GLU   B O   
5797 C  CB  . GLU   B 120 ? 0.2906 0.1958 0.2840 0.0128  -0.0811 0.0610  120 GLU   B CB  
5798 C  CG  . GLU   B 120 ? 0.3542 0.2738 0.3816 0.0215  -0.0971 0.0767  120 GLU   B CG  
5799 C  CD  . GLU   B 120 ? 0.4055 0.3479 0.4847 0.0267  -0.1003 0.0859  120 GLU   B CD  
5800 O  OE1 . GLU   B 120 ? 0.4260 0.3716 0.5203 0.0246  -0.0962 0.0986  120 GLU   B OE1 
5801 O  OE2 . GLU   B 120 ? 0.4292 0.3795 0.5350 0.0287  -0.0978 0.0773  120 GLU   B OE2 
5808 N  N   . VAL   B 121 ? 0.1790 0.1416 0.1877 -0.0280 -0.0327 0.0268  121 VAL   B N   
5809 C  CA  . VAL   B 121 ? 0.1775 0.1511 0.1788 -0.0275 -0.0344 0.0242  121 VAL   B CA  
5810 C  C   . VAL   B 121 ? 0.1689 0.1461 0.1705 -0.0268 -0.0298 0.0100  121 VAL   B C   
5811 O  O   . VAL   B 121 ? 0.1769 0.1409 0.1891 -0.0333 -0.0386 0.0123  121 VAL   B O   
5812 C  CB  . VAL   B 121 ? 0.2033 0.1945 0.1889 -0.0131 -0.0417 0.0265  121 VAL   B CB  
5813 C  CG1 . VAL   B 121 ? 0.2074 0.2068 0.2173 -0.0235 -0.0249 0.0219  121 VAL   B CG1 
5814 C  CG2 . VAL   B 121 ? 0.2261 0.2156 0.1991 -0.0064 -0.0326 0.0216  121 VAL   B CG2 
5824 N  N   . LEU   B 122 ? 0.1552 0.1388 0.1682 -0.0197 -0.0306 0.0111  122 LEU   B N   
5825 C  CA  . LEU   B 122 ? 0.1474 0.1470 0.1635 -0.0219 -0.0209 0.0114  122 LEU   B CA  
5826 C  C   . LEU   B 122 ? 0.1497 0.1336 0.1671 -0.0280 -0.0219 0.0137  122 LEU   B C   
5827 O  O   . LEU   B 122 ? 0.1579 0.1344 0.2033 -0.0349 -0.0315 0.0051  122 LEU   B O   
5828 C  CB  . LEU   B 122 ? 0.1742 0.1598 0.2006 -0.0112 -0.0270 0.0087  122 LEU   B CB  
5829 C  CG  . LEU   B 122 ? 0.1569 0.1625 0.2051 -0.0200 -0.0167 0.0117  122 LEU   B CG  
5830 C  CD1 . LEU   B 122 ? 0.1696 0.1875 0.2082 -0.0235 -0.0178 0.0125  122 LEU   B CD1 
5831 C  CD2 . LEU   B 122 ? 0.1592 0.1615 0.1863 -0.0153 -0.0136 -0.0093 122 LEU   B CD2 
5843 N  N   . LEU   B 123 ? 0.1505 0.1250 0.1694 -0.0268 -0.0236 0.0110  123 LEU   B N   
5844 C  CA  . LEU   B 123 ? 0.1541 0.1262 0.1634 -0.0272 -0.0255 0.0060  123 LEU   B CA  
5845 C  C   . LEU   B 123 ? 0.1486 0.1242 0.1585 -0.0284 -0.0196 0.0089  123 LEU   B C   
5846 O  O   . LEU   B 123 ? 0.1588 0.1289 0.1637 -0.0328 -0.0234 0.0040  123 LEU   B O   
5847 C  CB  . LEU   B 123 ? 0.1600 0.1331 0.1684 -0.0254 -0.0182 0.0008  123 LEU   B CB  
5848 C  CG  . LEU   B 123 ? 0.1561 0.1379 0.1888 -0.0172 -0.0143 0.0085  123 LEU   B CG  
5849 C  CD1 . LEU   B 123 ? 0.1624 0.1404 0.1996 -0.0223 -0.0084 -0.0030 123 LEU   B CD1 
5850 C  CD2 . LEU   B 123 ? 0.1617 0.1495 0.1938 -0.0182 -0.0045 0.0133  123 LEU   B CD2 
5862 N  N   . ALA   B 124 ? 0.1430 0.1247 0.1601 -0.0205 -0.0108 0.0034  124 ALA   B N   
5863 C  CA  . ALA   B 124 ? 0.1385 0.1264 0.1658 -0.0176 -0.0142 -0.0014 124 ALA   B CA  
5864 C  C   . ALA   B 124 ? 0.1351 0.1244 0.1607 -0.0191 -0.0151 0.0003  124 ALA   B C   
5865 O  O   . ALA   B 124 ? 0.1434 0.1255 0.1815 -0.0142 -0.0170 -0.0018 124 ALA   B O   
5866 C  CB  . ALA   B 124 ? 0.1448 0.1357 0.1696 -0.0082 0.0007  0.0008  124 ALA   B CB  
5872 N  N   . PRO   B 125 ? 0.1421 0.1261 0.1718 -0.0168 -0.0182 0.0124  125 PRO   B N   
5873 C  CA  . PRO   B 125 ? 0.1508 0.1308 0.1879 -0.0187 -0.0185 0.0229  125 PRO   B CA  
5874 C  C   . PRO   B 125 ? 0.1462 0.1245 0.2005 -0.0117 -0.0130 0.0098  125 PRO   B C   
5875 O  O   . PRO   B 125 ? 0.1497 0.1266 0.2140 -0.0139 -0.0027 0.0185  125 PRO   B O   
5876 C  CB  . PRO   B 125 ? 0.1509 0.1563 0.1955 -0.0216 -0.0212 0.0331  125 PRO   B CB  
5877 C  CG  . PRO   B 125 ? 0.1604 0.1558 0.1813 -0.0254 -0.0229 0.0146  125 PRO   B CG  
5878 C  CD  . PRO   B 125 ? 0.1543 0.1374 0.1712 -0.0286 -0.0109 0.0134  125 PRO   B CD  
5886 N  N   . LEU   B 126 ? 0.1479 0.1199 0.2153 -0.0105 0.0107  0.0186  126 LEU   B N   
5887 C  CA  . LEU   B 126 ? 0.1575 0.1359 0.2291 -0.0116 0.0156  0.0237  126 LEU   B CA  
5888 C  C   . LEU   B 126 ? 0.1551 0.1445 0.2359 -0.0003 0.0194  0.0289  126 LEU   B C   
5889 O  O   . LEU   B 126 ? 0.1751 0.1703 0.2632 0.0167  -0.0038 0.0030  126 LEU   B O   
5890 C  CB  . LEU   B 126 ? 0.1812 0.1379 0.2479 -0.0166 0.0263  0.0193  126 LEU   B CB  
5891 C  CG  . LEU   B 126 ? 0.1937 0.1471 0.2610 -0.0207 0.0229  -0.0010 126 LEU   B CG  
5892 C  CD1 . LEU   B 126 ? 0.2077 0.1516 0.3112 -0.0159 0.0161  -0.0113 126 LEU   B CD1 
5893 C  CD2 . LEU   B 126 ? 0.1952 0.1555 0.2625 -0.0261 0.0166  -0.0087 126 LEU   B CD2 
5905 N  N   . LEU   B 127 ? 0.1530 0.1293 0.2511 0.0022  0.0310  0.0195  127 LEU   B N   
5906 C  CA  . LEU   B 127 ? 0.1507 0.1385 0.2586 -0.0050 0.0370  0.0228  127 LEU   B CA  
5907 C  C   . LEU   B 127 ? 0.1470 0.1315 0.2556 -0.0004 0.0248  0.0214  127 LEU   B C   
5908 O  O   . LEU   B 127 ? 0.1524 0.1351 0.2667 -0.0117 0.0152  0.0273  127 LEU   B O   
5909 C  CB  . LEU   B 127 ? 0.1609 0.1349 0.2723 -0.0027 0.0357  0.0256  127 LEU   B CB  
5910 C  CG  . LEU   B 127 ? 0.1747 0.1363 0.2682 0.0061  0.0344  0.0217  127 LEU   B CG  
5911 C  CD1 . LEU   B 127 ? 0.1872 0.1376 0.2615 0.0045  0.0260  0.0172  127 LEU   B CD1 
5912 C  CD2 . LEU   B 127 ? 0.1745 0.1461 0.2810 -0.0119 0.0263  0.0277  127 LEU   B CD2 
5924 N  N   . SER   B 128 ? 0.1533 0.1348 0.2453 0.0037  0.0062  0.0217  128 SER   B N   
5925 C  CA  . SER   B 128 ? 0.1670 0.1433 0.2498 0.0066  -0.0022 0.0319  128 SER   B CA  
5926 C  C   . SER   B 128 ? 0.1816 0.1506 0.2780 0.0042  -0.0212 0.0327  128 SER   B C   
5927 O  O   . SER   B 128 ? 0.2009 0.1517 0.3136 0.0041  -0.0189 0.0393  128 SER   B O   
5928 C  CB  . SER   B 128 ? 0.1740 0.1470 0.2482 0.0064  0.0101  0.0459  128 SER   B CB  
5929 O  OG  . SER   B 128 ? 0.1787 0.1681 0.2564 0.0148  0.0241  0.0490  128 SER   B OG  
5935 N  N   . ALA   B 129 ? 0.1930 0.1588 0.2997 0.0223  -0.0127 0.0165  129 ALA   B N   
5936 C  CA  . ALA   B 129 ? 0.2092 0.1628 0.3076 0.0280  -0.0093 0.0066  129 ALA   B CA  
5937 C  C   . ALA   B 129 ? 0.1977 0.1546 0.2892 0.0186  0.0041  0.0053  129 ALA   B C   
5938 O  O   . ALA   B 129 ? 0.1859 0.1595 0.2870 0.0193  -0.0024 0.0072  129 ALA   B O   
5939 C  CB  . ALA   B 129 ? 0.2290 0.1840 0.3378 0.0332  0.0062  -0.0020 129 ALA   B CB  
5945 N  N   . GLY   B 130 ? 0.1948 0.1525 0.2901 0.0213  0.0038  -0.0016 130 GLY   B N   
5946 C  CA  . GLY   B 130 ? 0.1988 0.1645 0.2919 0.0199  0.0264  0.0028  130 GLY   B CA  
5947 C  C   . GLY   B 130 ? 0.2059 0.1708 0.2872 0.0149  0.0225  0.0148  130 GLY   B C   
5948 O  O   . GLY   B 130 ? 0.2190 0.1788 0.2939 0.0146  0.0143  0.0186  130 GLY   B O   
5952 N  N   . ILE   B 131 ? 0.2001 0.1812 0.2935 0.0316  0.0227  0.0077  131 ILE   B N   
5953 C  CA  . ILE   B 131 ? 0.2166 0.1965 0.2934 0.0282  0.0124  0.0240  131 ILE   B CA  
5954 C  C   . ILE   B 131 ? 0.2260 0.1871 0.2599 0.0201  0.0136  0.0289  131 ILE   B C   
5955 O  O   . ILE   B 131 ? 0.2570 0.2054 0.2688 0.0242  -0.0052 0.0257  131 ILE   B O   
5956 C  CB  . ILE   B 131 ? 0.2163 0.2322 0.3212 0.0240  0.0019  0.0275  131 ILE   B CB  
5957 C  CG1 . ILE   B 131 ? 0.2210 0.2530 0.3374 0.0006  0.0019  0.0258  131 ILE   B CG1 
5958 C  CG2 . ILE   B 131 ? 0.2139 0.2509 0.3391 0.0318  0.0059  0.0214  131 ILE   B CG2 
5959 C  CD1 . ILE   B 131 ? 0.2250 0.2705 0.3513 -0.0156 -0.0057 0.0254  131 ILE   B CD1 
5971 N  N   . PHE   B 132 ? 0.2104 0.1703 0.2529 0.0098  0.0295  0.0297  132 PHE   B N   
5972 C  CA  . PHE   B 132 ? 0.2214 0.1716 0.2571 0.0047  0.0447  0.0215  132 PHE   B CA  
5973 C  C   . PHE   B 132 ? 0.2448 0.1914 0.2830 0.0092  0.0503  0.0233  132 PHE   B C   
5974 O  O   . PHE   B 132 ? 0.2634 0.2153 0.3003 0.0070  0.0629  0.0298  132 PHE   B O   
5975 C  CB  . PHE   B 132 ? 0.2091 0.1683 0.2410 0.0093  0.0426  0.0200  132 PHE   B CB  
5976 C  CG  . PHE   B 132 ? 0.2057 0.1710 0.2387 0.0198  0.0296  0.0232  132 PHE   B CG  
5977 C  CD1 . PHE   B 132 ? 0.2135 0.1655 0.2608 0.0175  0.0260  0.0217  132 PHE   B CD1 
5978 C  CD2 . PHE   B 132 ? 0.2074 0.1768 0.2264 0.0318  0.0266  0.0347  132 PHE   B CD2 
5979 C  CE1 . PHE   B 132 ? 0.2178 0.1749 0.2736 0.0082  0.0229  0.0251  132 PHE   B CE1 
5980 C  CE2 . PHE   B 132 ? 0.2166 0.1848 0.2260 0.0243  0.0176  0.0337  132 PHE   B CE2 
5981 C  CZ  . PHE   B 132 ? 0.2202 0.1816 0.2528 0.0147  0.0092  0.0404  132 PHE   B CZ  
5991 N  N   . GLY   B 133 ? 0.2421 0.1783 0.2880 0.0036  0.0334  0.0464  133 GLY   B N   
5992 C  CA  . GLY   B 133 ? 0.2521 0.1897 0.2975 -0.0174 0.0354  0.0487  133 GLY   B CA  
5993 C  C   . GLY   B 133 ? 0.2589 0.1964 0.2967 -0.0293 0.0414  0.0512  133 GLY   B C   
5994 O  O   . GLY   B 133 ? 0.2727 0.2104 0.3332 -0.0405 0.0438  0.0621  133 GLY   B O   
5998 N  N   . ALA   B 134 ? 0.2417 0.1955 0.2779 -0.0307 0.0454  0.0334  134 ALA   B N   
5999 C  CA  . ALA   B 134 ? 0.2380 0.1903 0.2820 -0.0225 0.0488  0.0178  134 ALA   B CA  
6000 C  C   . ALA   B 134 ? 0.2408 0.1774 0.2842 -0.0144 0.0460  0.0371  134 ALA   B C   
6001 O  O   . ALA   B 134 ? 0.2456 0.1963 0.3006 -0.0001 0.0440  0.0331  134 ALA   B O   
6002 C  CB  . ALA   B 134 ? 0.2367 0.1925 0.3041 -0.0186 0.0366  0.0032  134 ALA   B CB  
6008 N  N   . ASP   B 135 ? 0.2546 0.1757 0.2921 -0.0202 0.0257  0.0420  135 ASP   B N   
6009 C  CA  . ASP   B 135 ? 0.2737 0.1695 0.3078 -0.0187 0.0105  0.0465  135 ASP   B CA  
6010 C  C   . ASP   B 135 ? 0.2544 0.1561 0.2933 -0.0077 0.0081  0.0469  135 ASP   B C   
6011 O  O   . ASP   B 135 ? 0.2482 0.1542 0.3079 -0.0095 0.0084  0.0425  135 ASP   B O   
6012 C  CB  . ASP   B 135 ? 0.3040 0.1798 0.3415 -0.0376 0.0032  0.0398  135 ASP   B CB  
6013 C  CG  . ASP   B 135 ? 0.3311 0.1817 0.3892 -0.0541 0.0047  0.0353  135 ASP   B CG  
6014 O  OD1 . ASP   B 135 ? 0.3396 0.1681 0.3966 -0.0378 0.0019  0.0397  135 ASP   B OD1 
6015 O  OD2 . ASP   B 135 ? 0.3519 0.2137 0.4360 -0.0679 0.0027  0.0163  135 ASP   B OD2 
6020 N  N   . PRO   B 136 ? 0.2401 0.1599 0.3032 0.0127  -0.0067 0.0346  136 PRO   B N   
6021 C  CA  . PRO   B 136 ? 0.2144 0.1509 0.3074 0.0152  -0.0060 0.0207  136 PRO   B CA  
6022 C  C   . PRO   B 136 ? 0.1908 0.1338 0.3178 0.0126  -0.0049 0.0197  136 PRO   B C   
6023 O  O   . PRO   B 136 ? 0.1744 0.1345 0.3113 0.0029  0.0009  0.0163  136 PRO   B O   
6024 C  CB  . PRO   B 136 ? 0.2219 0.1739 0.3081 0.0311  -0.0137 0.0090  136 PRO   B CB  
6025 C  CG  . PRO   B 136 ? 0.2426 0.1833 0.3248 0.0312  -0.0035 0.0092  136 PRO   B CG  
6026 C  CD  . PRO   B 136 ? 0.2462 0.1783 0.3166 0.0341  -0.0027 0.0186  136 PRO   B CD  
6034 N  N   . ILE   B 137 ? 0.2024 0.1295 0.3383 0.0124  -0.0101 0.0131  137 ILE   B N   
6035 C  CA  . ILE   B 137 ? 0.2114 0.1282 0.3442 0.0002  -0.0025 0.0105  137 ILE   B CA  
6036 C  C   . ILE   B 137 ? 0.2036 0.1378 0.3315 -0.0084 0.0088  0.0154  137 ILE   B C   
6037 O  O   . ILE   B 137 ? 0.1908 0.1406 0.3114 -0.0117 0.0126  0.0080  137 ILE   B O   
6038 C  CB  . ILE   B 137 ? 0.2417 0.1359 0.3823 -0.0062 -0.0010 0.0147  137 ILE   B CB  
6039 C  CG1 . ILE   B 137 ? 0.2696 0.1595 0.4207 0.0020  0.0070  0.0048  137 ILE   B CG1 
6040 C  CG2 . ILE   B 137 ? 0.2464 0.1370 0.3910 -0.0297 -0.0028 0.0149  137 ILE   B CG2 
6041 C  CD1 . ILE   B 137 ? 0.2903 0.1877 0.4535 0.0127  0.0093  0.0046  137 ILE   B CD1 
6053 N  N   . HIS   B 138 ? 0.2076 0.1384 0.3345 -0.0132 0.0200  0.0197  138 HIS   B N   
6054 C  CA  . HIS   B 138 ? 0.2158 0.1459 0.3243 -0.0072 0.0367  0.0234  138 HIS   B CA  
6055 C  C   . HIS   B 138 ? 0.1912 0.1455 0.3149 -0.0087 0.0335  0.0285  138 HIS   B C   
6056 O  O   . HIS   B 138 ? 0.1817 0.1454 0.3372 -0.0038 0.0341  0.0312  138 HIS   B O   
6057 C  CB  . HIS   B 138 ? 0.2499 0.1556 0.3272 -0.0077 0.0577  0.0186  138 HIS   B CB  
6058 C  CG  . HIS   B 138 ? 0.2797 0.1743 0.3328 -0.0114 0.0760  0.0355  138 HIS   B CG  
6059 N  ND1 . HIS   B 138 ? 0.2904 0.1870 0.3543 -0.0092 0.0866  0.0328  138 HIS   B ND1 
6060 C  CD2 . HIS   B 138 ? 0.2966 0.1784 0.3273 -0.0083 0.0817  0.0303  138 HIS   B CD2 
6061 C  CE1 . HIS   B 138 ? 0.2952 0.1897 0.3491 -0.0081 0.0876  0.0283  138 HIS   B CE1 
6062 N  NE2 . HIS   B 138 ? 0.3024 0.1769 0.3279 -0.0039 0.0886  0.0171  138 HIS   B NE2 
6070 N  N   . SER   B 139 ? 0.1864 0.1338 0.3110 0.0006  0.0291  0.0237  139 SER   B N   
6071 C  CA  . SER   B 139 ? 0.1867 0.1272 0.2937 -0.0038 0.0312  0.0128  139 SER   B CA  
6072 C  C   . SER   B 139 ? 0.1628 0.1182 0.2921 -0.0042 0.0221  0.0090  139 SER   B C   
6073 O  O   . SER   B 139 ? 0.1577 0.1216 0.2969 -0.0024 0.0032  0.0135  139 SER   B O   
6074 C  CB  . SER   B 139 ? 0.1978 0.1307 0.3080 0.0030  0.0118  0.0119  139 SER   B CB  
6075 O  OG  . SER   B 139 ? 0.1908 0.1257 0.3122 0.0024  -0.0004 0.0205  139 SER   B OG  
6081 N  N   . LEU   B 140 ? 0.1638 0.1169 0.2866 -0.0081 0.0215  0.0003  140 LEU   B N   
6082 C  CA  . LEU   B 140 ? 0.1590 0.1190 0.2871 -0.0056 0.0162  0.0037  140 LEU   B CA  
6083 C  C   . LEU   B 140 ? 0.1542 0.1200 0.3013 -0.0058 0.0037  0.0046  140 LEU   B C   
6084 O  O   . LEU   B 140 ? 0.1490 0.1310 0.2961 -0.0052 0.0004  0.0065  140 LEU   B O   
6085 C  CB  . LEU   B 140 ? 0.1604 0.1220 0.2935 -0.0098 0.0185  -0.0059 140 LEU   B CB  
6086 C  CG  . LEU   B 140 ? 0.1648 0.1246 0.2854 -0.0132 0.0052  0.0054  140 LEU   B CG  
6087 C  CD1 . LEU   B 140 ? 0.1705 0.1357 0.2978 -0.0173 0.0114  0.0034  140 LEU   B CD1 
6088 C  CD2 . LEU   B 140 ? 0.1895 0.1329 0.2972 -0.0144 -0.0006 -0.0093 140 LEU   B CD2 
6100 N  N   . ARG   B 141 ? 0.1482 0.1216 0.3095 -0.0133 0.0127  -0.0016 141 ARG   B N   
6101 C  CA  . ARG   B 141 ? 0.1518 0.1262 0.3459 -0.0162 0.0237  0.0010  141 ARG   B CA  
6102 C  C   . ARG   B 141 ? 0.1449 0.1276 0.3408 -0.0194 0.0137  -0.0023 141 ARG   B C   
6103 O  O   . ARG   B 141 ? 0.1497 0.1308 0.3393 -0.0163 0.0037  -0.0102 141 ARG   B O   
6104 C  CB  . ARG   B 141 ? 0.1684 0.1382 0.3599 -0.0221 0.0350  -0.0009 141 ARG   B CB  
6105 C  CG  . ARG   B 141 ? 0.1997 0.1679 0.3653 -0.0217 0.0388  -0.0032 141 ARG   B CG  
6106 C  CD  . ARG   B 141 ? 0.2430 0.1960 0.3598 -0.0160 0.0273  -0.0161 141 ARG   B CD  
6107 N  NE  . ARG   B 141 ? 0.2683 0.1905 0.3472 -0.0281 0.0307  -0.0244 141 ARG   B NE  
6108 C  CZ  . ARG   B 141 ? 0.2821 0.1803 0.3178 -0.0251 0.0350  -0.0292 141 ARG   B CZ  
6109 N  NH1 . ARG   B 141 ? 0.2937 0.1659 0.3114 -0.0231 0.0283  -0.0265 141 ARG   B NH1 
6110 N  NH2 . ARG   B 141 ? 0.2891 0.1917 0.3190 -0.0162 0.0247  -0.0207 141 ARG   B NH2 
6124 N  N   . VAL   B 142 ? 0.1489 0.1227 0.3282 -0.0141 0.0190  -0.0050 142 VAL   B N   
6125 C  CA  . VAL   B 142 ? 0.1442 0.1272 0.3146 -0.0083 0.0206  0.0006  142 VAL   B CA  
6126 C  C   . VAL   B 142 ? 0.1419 0.1238 0.3087 -0.0047 0.0074  -0.0019 142 VAL   B C   
6127 O  O   . VAL   B 142 ? 0.1542 0.1232 0.3279 -0.0014 0.0119  0.0007  142 VAL   B O   
6128 C  CB  . VAL   B 142 ? 0.1629 0.1344 0.3098 -0.0013 0.0221  0.0104  142 VAL   B CB  
6129 C  CG1 . VAL   B 142 ? 0.1568 0.1401 0.3076 0.0050  0.0302  0.0085  142 VAL   B CG1 
6130 C  CG2 . VAL   B 142 ? 0.1814 0.1399 0.3144 0.0009  0.0205  0.0106  142 VAL   B CG2 
6140 N  N   . CYS   B 143 ? 0.1375 0.1251 0.2918 -0.0059 0.0095  0.0094  143 CYS   B N   
6141 C  CA  . CYS   B 143 ? 0.1369 0.1245 0.2960 -0.0093 0.0015  0.0121  143 CYS   B CA  
6142 C  C   . CYS   B 143 ? 0.1350 0.1254 0.2908 -0.0057 0.0001  -0.0054 143 CYS   B C   
6143 O  O   . CYS   B 143 ? 0.1399 0.1314 0.2835 -0.0073 -0.0056 -0.0043 143 CYS   B O   
6144 C  CB  . CYS   B 143 ? 0.1431 0.1326 0.2865 -0.0068 0.0008  0.0096  143 CYS   B CB  
6145 S  SG  . CYS   B 143 ? 0.1461 0.1488 0.2753 -0.0062 0.0018  0.0081  143 CYS   B SG  
6151 N  N   . VAL   B 144 ? 0.1470 0.1266 0.3051 -0.0099 -0.0052 -0.0140 144 VAL   B N   
6152 C  CA  . VAL   B 144 ? 0.1490 0.1382 0.3291 -0.0144 -0.0181 -0.0220 144 VAL   B CA  
6153 C  C   . VAL   B 144 ? 0.1471 0.1410 0.3365 -0.0135 -0.0147 -0.0029 144 VAL   B C   
6154 O  O   . VAL   B 144 ? 0.1527 0.1632 0.3563 -0.0048 -0.0145 0.0215  144 VAL   B O   
6155 C  CB  . VAL   B 144 ? 0.1771 0.1567 0.3753 -0.0169 -0.0307 -0.0380 144 VAL   B CB  
6156 C  CG1 . VAL   B 144 ? 0.1978 0.1928 0.3951 -0.0105 -0.0293 -0.0354 144 VAL   B CG1 
6157 C  CG2 . VAL   B 144 ? 0.1933 0.1608 0.3714 -0.0042 -0.0414 -0.0442 144 VAL   B CG2 
6167 N  N   . ASP   B 145 ? 0.1489 0.1355 0.3458 -0.0126 -0.0052 -0.0134 145 ASP   B N   
6168 C  CA  . ASP   B 145 ? 0.1470 0.1366 0.3674 -0.0104 0.0026  -0.0054 145 ASP   B CA  
6169 C  C   . ASP   B 145 ? 0.1429 0.1439 0.3543 -0.0127 0.0011  -0.0073 145 ASP   B C   
6170 O  O   . ASP   B 145 ? 0.1432 0.1562 0.4098 -0.0140 0.0072  -0.0235 145 ASP   B O   
6171 C  CB  . ASP   B 145 ? 0.1587 0.1450 0.4098 -0.0161 0.0124  -0.0031 145 ASP   B CB  
6172 C  CG  . ASP   B 145 ? 0.1745 0.1484 0.4601 -0.0218 0.0239  -0.0084 145 ASP   B CG  
6173 O  OD1 . ASP   B 145 ? 0.1760 0.1478 0.4703 -0.0226 -0.0081 -0.0136 145 ASP   B OD1 
6174 O  OD2 . ASP   B 145 ? 0.2028 0.1576 0.4996 -0.0350 0.0435  -0.0039 145 ASP   B OD2 
6179 N  N   . THR   B 146 ? 0.1356 0.1254 0.3029 -0.0137 -0.0011 0.0006  146 THR   B N   
6180 C  CA  . THR   B 146 ? 0.1446 0.1273 0.2870 -0.0089 0.0060  0.0029  146 THR   B CA  
6181 C  C   . THR   B 146 ? 0.1403 0.1263 0.2789 -0.0058 -0.0025 0.0043  146 THR   B C   
6182 O  O   . THR   B 146 ? 0.1419 0.1281 0.2906 -0.0099 -0.0043 -0.0002 146 THR   B O   
6183 C  CB  . THR   B 146 ? 0.1504 0.1269 0.2835 -0.0086 0.0187  0.0045  146 THR   B CB  
6184 O  OG1 . THR   B 146 ? 0.1506 0.1268 0.2943 -0.0071 0.0194  0.0148  146 THR   B OG1 
6185 C  CG2 . THR   B 146 ? 0.1652 0.1368 0.2905 -0.0078 0.0133  -0.0033 146 THR   B CG2 
6193 N  N   . VAL   B 147 ? 0.1461 0.1358 0.2585 -0.0064 0.0084  0.0087  147 VAL   B N   
6194 C  CA  . VAL   B 147 ? 0.1474 0.1269 0.2543 -0.0072 -0.0119 0.0019  147 VAL   B CA  
6195 C  C   . VAL   B 147 ? 0.1387 0.1278 0.2664 -0.0217 -0.0188 -0.0066 147 VAL   B C   
6196 O  O   . VAL   B 147 ? 0.1524 0.1387 0.2810 -0.0245 -0.0363 -0.0077 147 VAL   B O   
6197 C  CB  . VAL   B 147 ? 0.1502 0.1380 0.2440 -0.0084 -0.0126 -0.0005 147 VAL   B CB  
6198 C  CG1 . VAL   B 147 ? 0.1475 0.1525 0.2288 -0.0131 -0.0091 0.0054  147 VAL   B CG1 
6199 C  CG2 . VAL   B 147 ? 0.1511 0.1329 0.2487 -0.0146 -0.0053 0.0032  147 VAL   B CG2 
6209 N  N   . ARG   B 148 ? 0.1439 0.1287 0.2630 -0.0103 -0.0298 -0.0064 148 ARG   B N   
6210 C  CA  . ARG   B 148 ? 0.1474 0.1420 0.2542 -0.0081 -0.0373 -0.0125 148 ARG   B CA  
6211 C  C   . ARG   B 148 ? 0.1529 0.1492 0.2442 -0.0087 -0.0373 -0.0011 148 ARG   B C   
6212 O  O   . ARG   B 148 ? 0.1751 0.1750 0.2481 -0.0218 -0.0451 0.0065  148 ARG   B O   
6213 C  CB  . ARG   B 148 ? 0.1497 0.1480 0.2563 -0.0071 -0.0339 -0.0225 148 ARG   B CB  
6214 C  CG  . ARG   B 148 ? 0.1518 0.1672 0.2775 -0.0127 -0.0301 -0.0375 148 ARG   B CG  
6215 C  CD  . ARG   B 148 ? 0.1583 0.1862 0.2965 0.0061  -0.0322 -0.0408 148 ARG   B CD  
6216 N  NE  . ARG   B 148 ? 0.1625 0.1803 0.2886 0.0198  -0.0400 -0.0368 148 ARG   B NE  
6217 C  CZ  . ARG   B 148 ? 0.1538 0.1666 0.2758 0.0152  -0.0298 -0.0288 148 ARG   B CZ  
6218 N  NH1 . ARG   B 148 ? 0.1443 0.1681 0.2853 -0.0008 -0.0095 -0.0273 148 ARG   B NH1 
6219 N  NH2 . ARG   B 148 ? 0.1709 0.1510 0.2593 0.0186  -0.0197 -0.0155 148 ARG   B NH2 
6233 N  N   . THR   B 149 ? 0.1541 0.1401 0.2448 -0.0140 -0.0361 0.0027  149 THR   B N   
6234 C  CA  . THR   B 149 ? 0.1597 0.1461 0.2342 -0.0173 -0.0386 0.0082  149 THR   B CA  
6235 C  C   . THR   B 149 ? 0.1617 0.1408 0.2209 -0.0148 -0.0399 0.0048  149 THR   B C   
6236 O  O   . THR   B 149 ? 0.1655 0.1389 0.2330 -0.0190 -0.0265 0.0052  149 THR   B O   
6237 C  CB  . THR   B 149 ? 0.1625 0.1404 0.2339 -0.0202 -0.0334 0.0027  149 THR   B CB  
6238 O  OG1 . THR   B 149 ? 0.1651 0.1492 0.2232 -0.0232 -0.0379 0.0032  149 THR   B OG1 
6239 C  CG2 . THR   B 149 ? 0.1768 0.1417 0.2447 -0.0107 -0.0274 0.0036  149 THR   B CG2 
6247 N  N   . ASN   B 150 ? 0.1674 0.1446 0.2148 -0.0188 -0.0407 0.0017  150 ASN   B N   
6248 C  CA  . ASN   B 150 ? 0.1753 0.1565 0.2082 -0.0292 -0.0394 -0.0008 150 ASN   B CA  
6249 C  C   . ASN   B 150 ? 0.1636 0.1544 0.2059 -0.0216 -0.0392 -0.0046 150 ASN   B C   
6250 O  O   . ASN   B 150 ? 0.1699 0.1498 0.2231 -0.0294 -0.0483 -0.0008 150 ASN   B O   
6251 C  CB  . ASN   B 150 ? 0.1986 0.1903 0.2262 -0.0365 -0.0528 0.0142  150 ASN   B CB  
6252 C  CG  . ASN   B 150 ? 0.2250 0.2296 0.2569 -0.0325 -0.0490 0.0300  150 ASN   B CG  
6253 O  OD1 . ASN   B 150 ? 0.2311 0.2481 0.2580 -0.0402 -0.0621 0.0270  150 ASN   B OD1 
6254 N  ND2 . ASN   B 150 ? 0.2365 0.2466 0.2853 -0.0244 -0.0529 0.0693  150 ASN   B ND2 
6261 N  N   . VAL   B 151 ? 0.1543 0.1491 0.2104 -0.0213 -0.0397 -0.0013 151 VAL   B N   
6262 C  CA  . VAL   B 151 ? 0.1567 0.1511 0.2169 -0.0314 -0.0280 -0.0046 151 VAL   B CA  
6263 C  C   . VAL   B 151 ? 0.1623 0.1463 0.2081 -0.0379 -0.0362 -0.0042 151 VAL   B C   
6264 O  O   . VAL   B 151 ? 0.1685 0.1544 0.2280 -0.0323 -0.0251 -0.0052 151 VAL   B O   
6265 C  CB  . VAL   B 151 ? 0.1800 0.1603 0.2295 -0.0145 -0.0278 0.0003  151 VAL   B CB  
6266 C  CG1 . VAL   B 151 ? 0.1875 0.1635 0.2523 -0.0190 -0.0169 -0.0116 151 VAL   B CG1 
6267 C  CG2 . VAL   B 151 ? 0.1945 0.1737 0.2180 -0.0019 -0.0308 0.0128  151 VAL   B CG2 
6277 N  N   . TYR   B 152 ? 0.1563 0.1345 0.1988 -0.0252 -0.0303 0.0042  152 TYR   B N   
6278 C  CA  . TYR   B 152 ? 0.1599 0.1516 0.1904 -0.0294 -0.0243 -0.0048 152 TYR   B CA  
6279 C  C   . TYR   B 152 ? 0.1567 0.1349 0.1795 -0.0234 -0.0234 -0.0122 152 TYR   B C   
6280 O  O   . TYR   B 152 ? 0.1652 0.1390 0.1889 -0.0265 -0.0218 -0.0013 152 TYR   B O   
6281 C  CB  . TYR   B 152 ? 0.1725 0.1679 0.1850 -0.0347 -0.0219 0.0104  152 TYR   B CB  
6282 C  CG  . TYR   B 152 ? 0.1916 0.1809 0.1812 -0.0476 -0.0278 0.0028  152 TYR   B CG  
6283 C  CD1 . TYR   B 152 ? 0.2036 0.1919 0.1728 -0.0432 -0.0352 0.0109  152 TYR   B CD1 
6284 C  CD2 . TYR   B 152 ? 0.2184 0.1964 0.1947 -0.0528 -0.0217 0.0016  152 TYR   B CD2 
6285 C  CE1 . TYR   B 152 ? 0.2228 0.2118 0.1892 -0.0433 -0.0418 0.0215  152 TYR   B CE1 
6286 C  CE2 . TYR   B 152 ? 0.2289 0.2219 0.1935 -0.0500 -0.0298 -0.0015 152 TYR   B CE2 
6287 C  CZ  . TYR   B 152 ? 0.2316 0.2326 0.1857 -0.0458 -0.0530 0.0208  152 TYR   B CZ  
6288 O  OH  . TYR   B 152 ? 0.2489 0.2680 0.2269 -0.0345 -0.0529 0.0265  152 TYR   B OH  
6298 N  N   . LEU   B 153 ? 0.1566 0.1309 0.1929 -0.0318 -0.0141 -0.0004 153 LEU   B N   
6299 C  CA  . LEU   B 153 ? 0.1592 0.1252 0.1853 -0.0243 -0.0118 -0.0037 153 LEU   B CA  
6300 C  C   . LEU   B 153 ? 0.1627 0.1241 0.1991 -0.0252 -0.0106 -0.0112 153 LEU   B C   
6301 O  O   . LEU   B 153 ? 0.1797 0.1461 0.2109 -0.0163 -0.0132 -0.0316 153 LEU   B O   
6302 C  CB  . LEU   B 153 ? 0.1630 0.1326 0.2073 -0.0274 -0.0076 -0.0027 153 LEU   B CB  
6303 C  CG  . LEU   B 153 ? 0.1582 0.1404 0.2258 -0.0292 -0.0109 -0.0013 153 LEU   B CG  
6304 C  CD1 . LEU   B 153 ? 0.1720 0.1521 0.2389 -0.0268 -0.0054 0.0137  153 LEU   B CD1 
6305 C  CD2 . LEU   B 153 ? 0.1590 0.1545 0.2254 -0.0284 -0.0013 0.0092  153 LEU   B CD2 
6317 N  N   . ALA   B 154 ? 0.1546 0.1307 0.1987 -0.0088 -0.0149 -0.0064 154 ALA   B N   
6318 C  CA  . ALA   B 154 ? 0.1666 0.1477 0.2258 -0.0093 -0.0153 -0.0195 154 ALA   B CA  
6319 C  C   . ALA   B 154 ? 0.1767 0.1478 0.2280 -0.0003 -0.0238 -0.0242 154 ALA   B C   
6320 O  O   . ALA   B 154 ? 0.2099 0.1522 0.2448 0.0049  -0.0138 -0.0032 154 ALA   B O   
6321 C  CB  . ALA   B 154 ? 0.1639 0.1607 0.2363 -0.0020 -0.0156 -0.0241 154 ALA   B CB  
6327 N  N   . VAL   B 155 ? 0.1486 0.1362 0.2397 -0.0063 0.0023  -0.0175 155 VAL   B N   
6328 C  CA  . VAL   B 155 ? 0.1443 0.1341 0.2604 -0.0049 -0.0150 -0.0054 155 VAL   B CA  
6329 C  C   . VAL   B 155 ? 0.1472 0.1352 0.2502 -0.0078 -0.0184 -0.0238 155 VAL   B C   
6330 O  O   . VAL   B 155 ? 0.1688 0.1567 0.2858 -0.0016 -0.0141 -0.0422 155 VAL   B O   
6331 C  CB  . VAL   B 155 ? 0.1481 0.1529 0.2973 -0.0052 -0.0211 0.0103  155 VAL   B CB  
6332 C  CG1 . VAL   B 155 ? 0.1532 0.1498 0.3033 -0.0123 -0.0179 0.0094  155 VAL   B CG1 
6333 C  CG2 . VAL   B 155 ? 0.1490 0.1697 0.3180 -0.0107 -0.0174 0.0350  155 VAL   B CG2 
6343 N  N   . PHE   B 156 ? 0.1333 0.1497 0.2696 -0.0002 -0.0053 -0.0170 156 PHE   B N   
6344 C  CA  . PHE   B 156 ? 0.1409 0.1557 0.3010 0.0011  -0.0051 -0.0170 156 PHE   B CA  
6345 C  C   . PHE   B 156 ? 0.1448 0.1643 0.3388 0.0118  -0.0106 -0.0338 156 PHE   B C   
6346 O  O   . PHE   B 156 ? 0.1644 0.1872 0.3713 0.0215  -0.0006 -0.0438 156 PHE   B O   
6347 C  CB  . PHE   B 156 ? 0.1515 0.1540 0.2924 0.0012  -0.0084 -0.0096 156 PHE   B CB  
6348 C  CG  . PHE   B 156 ? 0.1513 0.1663 0.3040 -0.0026 -0.0090 0.0100  156 PHE   B CG  
6349 C  CD1 . PHE   B 156 ? 0.1507 0.1909 0.3345 0.0050  -0.0042 0.0348  156 PHE   B CD1 
6350 C  CD2 . PHE   B 156 ? 0.1576 0.1779 0.3050 0.0064  -0.0154 0.0153  156 PHE   B CD2 
6351 C  CE1 . PHE   B 156 ? 0.1555 0.2026 0.3422 0.0019  -0.0045 0.0319  156 PHE   B CE1 
6352 C  CE2 . PHE   B 156 ? 0.1638 0.1979 0.3225 0.0119  -0.0137 0.0098  156 PHE   B CE2 
6353 C  CZ  . PHE   B 156 ? 0.1558 0.2036 0.3422 0.0159  -0.0209 0.0181  156 PHE   B CZ  
6363 N  N   . ASP   B 157 ? 0.1481 0.1580 0.3546 0.0145  -0.0236 -0.0193 157 ASP   B N   
6364 C  CA  . ASP   B 157 ? 0.1611 0.1665 0.3783 0.0120  -0.0213 -0.0288 157 ASP   B CA  
6365 C  C   . ASP   B 157 ? 0.1641 0.1655 0.3954 0.0123  -0.0212 -0.0437 157 ASP   B C   
6366 O  O   . ASP   B 157 ? 0.1500 0.1620 0.3860 0.0047  -0.0183 -0.0385 157 ASP   B O   
6367 C  CB  . ASP   B 157 ? 0.1933 0.1881 0.3826 0.0095  -0.0406 -0.0155 157 ASP   B CB  
6368 C  CG  . ASP   B 157 ? 0.2300 0.1962 0.4006 0.0051  -0.0376 -0.0146 157 ASP   B CG  
6369 O  OD1 . ASP   B 157 ? 0.2332 0.1868 0.4191 0.0131  -0.0345 -0.0129 157 ASP   B OD1 
6370 O  OD2 . ASP   B 157 ? 0.2632 0.2132 0.4208 0.0037  -0.0246 -0.0066 157 ASP   B OD2 
6375 N  N   . LYS   B 158 ? 0.1690 0.1891 0.4065 0.0108  -0.0113 -0.0736 158 LYS   B N   
6376 C  CA  . LYS   B 158 ? 0.1849 0.2089 0.4168 0.0052  0.0017  -0.0893 158 LYS   B CA  
6377 C  C   . LYS   B 158 ? 0.1859 0.1909 0.4305 0.0103  -0.0080 -0.0802 158 LYS   B C   
6378 O  O   . LYS   B 158 ? 0.1854 0.1882 0.4364 -0.0026 -0.0059 -0.0829 158 LYS   B O   
6379 C  CB  . LYS   B 158 ? 0.2117 0.2576 0.4133 0.0058  0.0133  -0.1103 158 LYS   B CB  
6380 C  CG  . LYS   B 158 ? 0.2455 0.3018 0.4177 0.0099  0.0170  -0.1227 158 LYS   B CG  
6381 C  CD  . LYS   B 158 ? 0.2711 0.3456 0.4300 0.0083  0.0213  -0.1177 158 LYS   B CD  
6382 C  CE  . LYS   B 158 ? 0.2934 0.3792 0.4425 0.0104  0.0204  -0.1152 158 LYS   B CE  
6383 N  NZ  . LYS   B 158 ? 0.2936 0.3952 0.4442 0.0083  0.0183  -0.1135 158 LYS   B NZ  
6397 N  N   . ASN   B 159 ? 0.1878 0.1830 0.4468 0.0100  -0.0222 -0.0688 159 ASN   B N   
6398 C  CA  . ASN   B 159 ? 0.1991 0.1742 0.4599 0.0203  -0.0391 -0.0544 159 ASN   B CA  
6399 C  C   . ASN   B 159 ? 0.1799 0.1546 0.4556 0.0172  -0.0505 -0.0404 159 ASN   B C   
6400 O  O   . ASN   B 159 ? 0.1795 0.1479 0.4771 -0.0000 -0.0593 -0.0243 159 ASN   B O   
6401 C  CB  . ASN   B 159 ? 0.2216 0.1919 0.4787 0.0270  -0.0444 -0.0489 159 ASN   B CB  
6402 C  CG  . ASN   B 159 ? 0.2490 0.2228 0.5009 0.0261  -0.0516 -0.0597 159 ASN   B CG  
6403 O  OD1 . ASN   B 159 ? 0.2643 0.2254 0.5059 0.0326  -0.0542 -0.0683 159 ASN   B OD1 
6404 N  ND2 . ASN   B 159 ? 0.2505 0.2304 0.5146 0.0242  -0.0524 -0.0545 159 ASN   B ND2 
6411 N  N   . LEU   B 160 ? 0.1660 0.1545 0.4312 0.0081  -0.0462 -0.0311 160 LEU   B N   
6412 C  CA  . LEU   B 160 ? 0.1611 0.1552 0.3943 0.0091  -0.0389 -0.0162 160 LEU   B CA  
6413 C  C   . LEU   B 160 ? 0.1566 0.1469 0.3854 0.0015  -0.0267 -0.0241 160 LEU   B C   
6414 O  O   . LEU   B 160 ? 0.1458 0.1548 0.3854 -0.0039 -0.0317 -0.0147 160 LEU   B O   
6415 C  CB  . LEU   B 160 ? 0.1599 0.1668 0.3767 0.0046  -0.0313 -0.0058 160 LEU   B CB  
6416 C  CG  . LEU   B 160 ? 0.1616 0.1802 0.3508 0.0067  -0.0301 -0.0033 160 LEU   B CG  
6417 C  CD1 . LEU   B 160 ? 0.1745 0.1962 0.3455 0.0011  -0.0202 -0.0029 160 LEU   B CD1 
6418 C  CD2 . LEU   B 160 ? 0.1656 0.1865 0.3457 0.0227  -0.0288 -0.0123 160 LEU   B CD2 
6430 N  N   . TYR   B 161 ? 0.1587 0.1499 0.3850 -0.0040 0.0021  -0.0351 161 TYR   B N   
6431 C  CA  . TYR   B 161 ? 0.1728 0.1502 0.3654 -0.0144 0.0210  -0.0466 161 TYR   B CA  
6432 C  C   . TYR   B 161 ? 0.1763 0.1490 0.3613 -0.0144 0.0218  -0.0388 161 TYR   B C   
6433 O  O   . TYR   B 161 ? 0.1785 0.1487 0.3566 -0.0238 0.0084  -0.0289 161 TYR   B O   
6434 C  CB  . TYR   B 161 ? 0.1863 0.1649 0.3562 -0.0262 0.0317  -0.0519 161 TYR   B CB  
6435 C  CG  . TYR   B 161 ? 0.2152 0.1686 0.3381 -0.0379 0.0363  -0.0588 161 TYR   B CG  
6436 C  CD1 . TYR   B 161 ? 0.2242 0.1713 0.3306 -0.0455 0.0427  -0.0547 161 TYR   B CD1 
6437 C  CD2 . TYR   B 161 ? 0.2373 0.1771 0.3249 -0.0338 0.0270  -0.0612 161 TYR   B CD2 
6438 C  CE1 . TYR   B 161 ? 0.2454 0.1894 0.3323 -0.0478 0.0376  -0.0557 161 TYR   B CE1 
6439 C  CE2 . TYR   B 161 ? 0.2606 0.1950 0.3278 -0.0396 0.0263  -0.0630 161 TYR   B CE2 
6440 C  CZ  . TYR   B 161 ? 0.2623 0.2015 0.3274 -0.0541 0.0225  -0.0546 161 TYR   B CZ  
6441 O  OH  . TYR   B 161 ? 0.2908 0.2272 0.3544 -0.0574 0.0191  -0.0511 161 TYR   B OH  
6451 N  N   . ASP   B 162 ? 0.1835 0.1491 0.3768 -0.0127 0.0018  -0.0535 162 ASP   B N   
6452 C  CA  . ASP   B 162 ? 0.1920 0.1572 0.3860 -0.0113 -0.0083 -0.0475 162 ASP   B CA  
6453 C  C   . ASP   B 162 ? 0.1868 0.1542 0.3751 -0.0122 -0.0126 -0.0429 162 ASP   B C   
6454 O  O   . ASP   B 162 ? 0.1896 0.1559 0.3798 -0.0171 -0.0332 -0.0333 162 ASP   B O   
6455 C  CB  . ASP   B 162 ? 0.2088 0.1703 0.4049 -0.0059 -0.0126 -0.0669 162 ASP   B CB  
6456 C  CG  . ASP   B 162 ? 0.2169 0.1971 0.4305 0.0031  -0.0097 -0.0862 162 ASP   B CG  
6457 O  OD1 . ASP   B 162 ? 0.2220 0.2177 0.4290 -0.0017 0.0043  -0.0777 162 ASP   B OD1 
6458 O  OD2 . ASP   B 162 ? 0.2299 0.2213 0.4521 0.0177  -0.0091 -0.0852 162 ASP   B OD2 
6463 N  N   . LYS   B 163 ? 0.1830 0.1408 0.3662 -0.0088 -0.0228 -0.0296 163 LYS   B N   
6464 C  CA  . LYS   B 163 ? 0.1980 0.1494 0.3683 -0.0215 -0.0139 -0.0109 163 LYS   B CA  
6465 C  C   . LYS   B 163 ? 0.1628 0.1453 0.3497 -0.0202 -0.0191 0.0077  163 LYS   B C   
6466 O  O   . LYS   B 163 ? 0.1548 0.1576 0.3707 -0.0214 -0.0188 0.0092  163 LYS   B O   
6467 C  CB  . LYS   B 163 ? 0.2520 0.1864 0.4058 -0.0226 -0.0192 0.0080  163 LYS   B CB  
6468 C  CG  . LYS   B 163 ? 0.3313 0.2684 0.4585 -0.0271 -0.0098 0.0113  163 LYS   B CG  
6469 C  CD  . LYS   B 163 ? 0.3973 0.3424 0.5152 -0.0364 -0.0082 0.0057  163 LYS   B CD  
6470 C  CE  . LYS   B 163 ? 0.4484 0.3983 0.5557 -0.0429 -0.0058 0.0034  163 LYS   B CE  
6471 N  NZ  . LYS   B 163 ? 0.4778 0.4448 0.5811 -0.0461 -0.0049 -0.0015 163 LYS   B NZ  
6485 N  N   . LEU   B 164 ? 0.1513 0.1358 0.3322 -0.0133 -0.0194 0.0045  164 LEU   B N   
6486 C  CA  . LEU   B 164 ? 0.1544 0.1371 0.3172 -0.0151 -0.0268 0.0035  164 LEU   B CA  
6487 C  C   . LEU   B 164 ? 0.1646 0.1397 0.3205 -0.0202 -0.0375 0.0100  164 LEU   B C   
6488 O  O   . LEU   B 164 ? 0.1634 0.1650 0.3348 -0.0154 -0.0342 0.0079  164 LEU   B O   
6489 C  CB  . LEU   B 164 ? 0.1458 0.1400 0.3031 -0.0106 -0.0194 -0.0003 164 LEU   B CB  
6490 C  CG  . LEU   B 164 ? 0.1568 0.1532 0.3006 -0.0112 -0.0138 0.0079  164 LEU   B CG  
6491 C  CD1 . LEU   B 164 ? 0.1624 0.1541 0.2950 -0.0100 -0.0155 -0.0055 164 LEU   B CD1 
6492 C  CD2 . LEU   B 164 ? 0.1708 0.1866 0.3137 -0.0129 -0.0035 -0.0034 164 LEU   B CD2 
6504 N  N   . VAL   B 165 ? 0.2061 0.1486 0.3350 -0.0287 -0.0495 0.0051  165 VAL   B N   
6505 C  CA  . VAL   B 165 ? 0.2438 0.1627 0.3456 -0.0410 -0.0676 0.0026  165 VAL   B CA  
6506 C  C   . VAL   B 165 ? 0.2709 0.1700 0.3748 -0.0478 -0.0946 0.0058  165 VAL   B C   
6507 O  O   . VAL   B 165 ? 0.2946 0.1883 0.3889 -0.0536 -0.1054 0.0037  165 VAL   B O   
6508 C  CB  . VAL   B 165 ? 0.2672 0.1762 0.3382 -0.0249 -0.0434 -0.0115 165 VAL   B CB  
6509 C  CG1 . VAL   B 165 ? 0.2831 0.1873 0.3550 -0.0231 -0.0311 -0.0123 165 VAL   B CG1 
6510 C  CG2 . VAL   B 165 ? 0.2632 0.1805 0.3248 -0.0194 -0.0336 -0.0096 165 VAL   B CG2 
6520 N  N   . SER   B 166 ? 0.2799 0.1606 0.4052 -0.0406 -0.1023 -0.0167 166 SER   B N   
6521 C  CA  . SER   B 166 ? 0.2726 0.1621 0.4509 -0.0412 -0.0886 -0.0270 166 SER   B CA  
6522 C  C   . SER   B 166 ? 0.2569 0.1752 0.4641 -0.0403 -0.0864 -0.0020 166 SER   B C   
6523 O  O   . SER   B 166 ? 0.2601 0.1944 0.4833 -0.0522 -0.1003 -0.0271 166 SER   B O   
6524 C  CB  . SER   B 166 ? 0.2690 0.1719 0.4764 -0.0346 -0.0832 -0.0341 166 SER   B CB  
6525 O  OG  . SER   B 166 ? 0.2542 0.1716 0.4972 -0.0252 -0.0843 -0.0148 166 SER   B OG  
6531 N  N   . SER   B 167 ? 0.2352 0.1653 0.4388 -0.0483 -0.0868 0.0320  167 SER   B N   
6532 C  CA  . SER   B 167 ? 0.2236 0.1732 0.4163 -0.0384 -0.0644 0.0348  167 SER   B CA  
6533 C  C   . SER   B 167 ? 0.2155 0.1836 0.3923 -0.0550 -0.0603 0.0516  167 SER   B C   
6534 O  O   . SER   B 167 ? 0.2135 0.1972 0.3959 -0.0600 -0.0534 0.0503  167 SER   B O   
6535 C  CB  . SER   B 167 ? 0.2109 0.1776 0.4195 -0.0323 -0.0365 0.0315  167 SER   B CB  
6536 O  OG  . SER   B 167 ? 0.1994 0.1850 0.4106 -0.0249 -0.0198 0.0300  167 SER   B OG  
6542 N  N   . PHE   B 168 ? 0.2147 0.1828 0.3777 -0.0494 -0.0492 0.0570  168 PHE   B N   
6543 C  CA  . PHE   B 168 ? 0.2191 0.1815 0.3474 -0.0503 -0.0418 0.0383  168 PHE   B CA  
6544 C  C   . PHE   B 168 ? 0.1904 0.1727 0.3001 -0.0311 -0.0253 0.0150  168 PHE   B C   
6545 O  O   . PHE   B 168 ? 0.2202 0.1622 0.2923 -0.0053 -0.0262 0.0063  168 PHE   B O   
6546 C  CB  . PHE   B 168 ? 0.2400 0.1846 0.3498 -0.0598 -0.0514 0.0534  168 PHE   B CB  
6547 C  CG  . PHE   B 168 ? 0.2662 0.1731 0.3399 -0.0640 -0.0565 0.0301  168 PHE   B CG  
6548 C  CD1 . PHE   B 168 ? 0.2924 0.1788 0.3493 -0.0592 -0.0537 0.0278  168 PHE   B CD1 
6549 C  CD2 . PHE   B 168 ? 0.2568 0.1648 0.3343 -0.0621 -0.0551 0.0363  168 PHE   B CD2 
6550 C  CE1 . PHE   B 168 ? 0.3037 0.1856 0.3387 -0.0521 -0.0474 0.0334  168 PHE   B CE1 
6551 C  CE2 . PHE   B 168 ? 0.2858 0.1770 0.3394 -0.0427 -0.0540 0.0278  168 PHE   B CE2 
6552 C  CZ  . PHE   B 168 ? 0.2968 0.1747 0.3374 -0.0374 -0.0577 0.0403  168 PHE   B CZ  
6562 N  N   . LEU   B 169 ? 0.1886 0.1792 0.2935 -0.0039 -0.0077 0.0036  169 LEU   B N   
6563 C  CA  . LEU   B 169 ? 0.2148 0.2137 0.3189 -0.0061 0.0019  -0.0216 169 LEU   B CA  
6564 C  C   . LEU   B 169 ? 0.2506 0.2371 0.3650 0.0087  -0.0030 -0.0427 169 LEU   B C   
6565 O  O   . LEU   B 169 ? 0.2739 0.2555 0.4038 0.0080  0.0017  -0.0594 169 LEU   B O   
6566 C  CB  . LEU   B 169 ? 0.2339 0.2568 0.3202 -0.0130 0.0081  0.0011  169 LEU   B CB  
6567 C  CG  . LEU   B 169 ? 0.2673 0.2927 0.3425 -0.0039 0.0112  0.0097  169 LEU   B CG  
6568 C  CD1 . LEU   B 169 ? 0.2809 0.3100 0.3424 -0.0048 0.0086  0.0232  169 LEU   B CD1 
6569 C  CD2 . LEU   B 169 ? 0.2588 0.2981 0.3374 0.0121  0.0265  -0.0022 169 LEU   B CD2 
6570 O  OXT . LEU   B 169 ? 0.2709 0.2511 0.3743 0.0305  -0.0003 -0.0453 169 LEU   B OXT 
6582 C  C1  T TFA   C .   ? 0.1512 0.1611 0.1379 -0.0137 0.0185  0.0176  201 TFA   A C1  
6583 C  C2  T TFA   C .   ? 0.1789 0.1822 0.1665 -0.0162 0.0134  0.0082  201 TFA   A C2  
6584 O  O   T TFA   C .   ? 0.1185 0.1418 0.1320 -0.0193 0.0152  0.0290  201 TFA   A O   
6585 F  F1  T TFA   C .   ? 0.1954 0.1951 0.1930 -0.0089 0.0057  0.0029  201 TFA   A F1  
6586 F  F2  T TFA   C .   ? 0.1868 0.1897 0.1694 -0.0199 0.0121  0.0071  201 TFA   A F2  
6587 F  F3  T TFA   C .   ? 0.1934 0.1947 0.1950 -0.0197 0.0242  0.0010  201 TFA   A F3  
6588 O  OXT T TFA   C .   ? 0.1567 0.1597 0.1462 0.0071  0.0230  0.0220  201 TFA   A OXT 
6589 N  N2  B A1A9T D .   ? 0.1566 0.1926 0.1778 -0.0018 0.0141  0.0281  202 A1A9T A N2  
6590 C  C3  B A1A9T D .   ? 0.1564 0.1968 0.1754 -0.0061 0.0184  0.0318  202 A1A9T A C3  
6591 C  C6  B A1A9T D .   ? 0.1479 0.1931 0.1740 -0.0038 0.0166  0.0348  202 A1A9T A C6  
6592 C  C9  B A1A9T D .   ? 0.1773 0.2119 0.1849 -0.0129 0.0296  0.0254  202 A1A9T A C9  
6593 C  C1  B A1A9T D .   ? 0.1720 0.2130 0.1833 -0.0072 0.0296  0.0384  202 A1A9T A C1  
6594 C  C10 B A1A9T D .   ? 0.1812 0.2139 0.1837 -0.0097 0.0300  0.0231  202 A1A9T A C10 
6595 C  C11 B A1A9T D .   ? 0.1822 0.2147 0.1867 -0.0091 0.0278  0.0234  202 A1A9T A C11 
6596 C  C2  B A1A9T D .   ? 0.1766 0.2111 0.1852 -0.0095 0.0271  0.0292  202 A1A9T A C2  
6597 C  C4  B A1A9T D .   ? 0.1548 0.1896 0.1759 -0.0006 0.0157  0.0335  202 A1A9T A C4  
6598 C  C5  B A1A9T D .   ? 0.1473 0.1846 0.1771 -0.0037 0.0099  0.0384  202 A1A9T A C5  
6599 C  C7  B A1A9T D .   ? 0.1476 0.1956 0.1801 -0.0035 0.0154  0.0347  202 A1A9T A C7  
6600 C  C8  B A1A9T D .   ? 0.1394 0.1872 0.1863 -0.0056 0.0041  0.0388  202 A1A9T A C8  
6601 N  N1  B A1A9T D .   ? 0.1689 0.2029 0.1838 -0.0094 0.0246  0.0331  202 A1A9T A N1  
6602 N  N3  B A1A9T D .   ? 0.1530 0.1864 0.1740 -0.0029 0.0134  0.0401  202 A1A9T A N3  
6603 N  N4  B A1A9T D .   ? 0.1406 0.1795 0.1803 -0.0039 0.0038  0.0427  202 A1A9T A N4  
6604 O  O1  B A1A9T D .   ? 0.1734 0.2137 0.1909 -0.0050 0.0275  0.0412  202 A1A9T A O1  
6619 N  N2  C A1A9T E .   ? 0.1660 0.1825 0.1714 0.0084  -0.0006 0.0284  203 A1A9T A N2  
6620 C  C3  C A1A9T E .   ? 0.1670 0.1883 0.1727 0.0074  -0.0018 0.0301  203 A1A9T A C3  
6621 C  C6  C A1A9T E .   ? 0.1545 0.1815 0.1704 0.0128  -0.0004 0.0373  203 A1A9T A C6  
6622 C  C9  C A1A9T E .   ? 0.2051 0.2152 0.2106 0.0085  -0.0059 0.0091  203 A1A9T A C9  
6623 C  C1  C A1A9T E .   ? 0.2017 0.2163 0.2074 0.0130  -0.0083 0.0131  203 A1A9T A C1  
6624 C  C10 C A1A9T E .   ? 0.2049 0.2208 0.2121 0.0077  -0.0077 0.0068  203 A1A9T A C10 
6625 C  C11 C A1A9T E .   ? 0.2023 0.2202 0.2142 0.0097  -0.0076 0.0079  203 A1A9T A C11 
6626 C  C2  C A1A9T E .   ? 0.1997 0.2129 0.2080 0.0092  -0.0056 0.0116  203 A1A9T A C2  
6627 C  C4  C A1A9T E .   ? 0.1638 0.1810 0.1733 0.0094  0.0021  0.0305  203 A1A9T A C4  
6628 C  C5  C A1A9T E .   ? 0.1530 0.1748 0.1751 0.0123  -0.0059 0.0379  203 A1A9T A C5  
6629 C  C7  C A1A9T E .   ? 0.1483 0.1830 0.1753 0.0182  0.0004  0.0369  203 A1A9T A C7  
6630 C  C8  C A1A9T E .   ? 0.1414 0.1773 0.1823 0.0148  -0.0123 0.0389  203 A1A9T A C8  
6631 N  N1  C A1A9T E .   ? 0.1846 0.2011 0.1936 0.0058  -0.0010 0.0174  203 A1A9T A N1  
6632 N  N3  C A1A9T E .   ? 0.1612 0.1785 0.1725 0.0100  -0.0003 0.0350  203 A1A9T A N3  
6633 N  N4  C A1A9T E .   ? 0.1439 0.1701 0.1782 0.0151  -0.0151 0.0432  203 A1A9T A N4  
6634 O  O1  C A1A9T E .   ? 0.2035 0.2208 0.2093 0.0138  -0.0109 0.0155  203 A1A9T A O1  
6649 CL CL  B CL    F .   ? 0.2101 0.1806 0.3705 -0.0223 -0.0719 -0.0198 204 CL    A CL  
6650 O  O   . HOH   G .   ? 0.4251 0.8144 0.5064 -0.1111 0.0640  0.0954  301 HOH   A O   
6651 O  O   . HOH   G .   ? 0.5416 0.5972 0.5336 -0.1248 -0.1190 -0.0972 302 HOH   A O   
6652 O  O   . HOH   G .   ? 0.3638 0.3536 0.2939 -0.1444 -0.0162 0.0884  303 HOH   A O   
6653 O  O   . HOH   G .   ? 0.7177 0.6376 0.3710 -0.1342 0.0090  0.2020  304 HOH   A O   
6654 O  O   . HOH   G .   ? 0.2886 0.2799 0.4444 -0.0321 -0.1028 0.1142  305 HOH   A O   
6655 O  O   . HOH   G .   ? 0.2073 0.2246 0.3613 -0.0074 -0.0626 0.0411  306 HOH   A O   
6656 O  O   A HOH   G .   ? 0.2393 0.2579 0.3152 -0.0482 -0.0395 0.0618  307 HOH   A O   
6657 O  O   . HOH   G .   ? 0.8212 0.3755 0.5438 -0.0559 -0.1362 0.0906  308 HOH   A O   
6658 O  O   . HOH   G .   ? 0.6468 0.5111 0.3229 0.2241  -0.1174 0.0597  309 HOH   A O   
6659 O  O   . HOH   G .   ? 0.3033 0.5956 0.3780 0.0295  -0.0587 0.0356  310 HOH   A O   
6660 O  O   . HOH   G .   ? 0.3449 0.3094 0.3567 -0.0899 0.0001  -0.0276 311 HOH   A O   
6661 O  O   . HOH   G .   ? 0.1574 0.4806 0.2691 -0.0006 0.0347  0.0728  312 HOH   A O   
6662 O  O   . HOH   G .   ? 0.2937 0.5741 0.6038 0.1442  0.0579  0.1058  313 HOH   A O   
6663 O  O   . HOH   G .   ? 0.6470 0.5703 0.4990 -0.1431 0.0238  0.2175  314 HOH   A O   
6664 O  O   . HOH   G .   ? 0.5668 0.5099 0.5766 0.0323  -0.0535 0.0466  315 HOH   A O   
6665 O  O   B HOH   G .   ? 0.4484 0.3515 0.3431 0.2157  -0.0018 0.0371  316 HOH   A O   
6666 O  O   . HOH   G .   ? 0.3005 0.3867 0.1999 -0.0628 0.0371  0.0564  317 HOH   A O   
6667 O  O   . HOH   G .   ? 0.5770 0.4145 0.5211 -0.0641 0.1479  0.1261  318 HOH   A O   
6668 O  O   . HOH   G .   ? 0.4951 0.3574 0.4601 -0.0214 0.1482  0.0011  319 HOH   A O   
6669 O  O   . HOH   G .   ? 0.4605 0.5385 0.5625 0.1540  0.0673  -0.0884 320 HOH   A O   
6670 O  O   . HOH   G .   ? 0.5523 0.5441 0.3707 -0.1442 0.1898  0.0560  321 HOH   A O   
6671 O  O   . HOH   G .   ? 0.2140 0.3695 0.4619 -0.0540 0.0609  -0.1277 322 HOH   A O   
6672 O  O   . HOH   G .   ? 0.1880 0.5149 0.3352 0.0983  0.0153  0.0570  323 HOH   A O   
6673 O  O   A HOH   G .   ? 0.1564 0.2028 0.2509 0.0397  0.0587  0.0640  324 HOH   A O   
6674 O  O   . HOH   G .   ? 0.2108 0.1869 0.3698 -0.0448 0.0204  -0.0177 325 HOH   A O   
6675 O  O   . HOH   G .   ? 0.2270 0.2677 0.2649 -0.0195 0.0445  0.0652  326 HOH   A O   
6676 O  O   . HOH   G .   ? 0.6038 0.5739 0.3985 -0.0212 -0.0413 0.1382  327 HOH   A O   
6677 O  O   . HOH   G .   ? 0.5283 0.4349 0.4898 -0.1717 -0.0597 0.2327  328 HOH   A O   
6678 O  O   . HOH   G .   ? 0.5647 0.3461 0.3192 -0.1428 -0.1112 0.0191  329 HOH   A O   
6679 O  O   . HOH   G .   ? 0.2469 0.2317 0.2773 -0.0290 0.0073  -0.0114 330 HOH   A O   
6680 O  O   . HOH   G .   ? 0.3404 0.4477 0.2843 -0.0537 0.0556  0.0308  331 HOH   A O   
6681 O  O   . HOH   G .   ? 0.3365 0.7327 0.5434 -0.0681 -0.0811 0.1888  332 HOH   A O   
6682 O  O   . HOH   G .   ? 0.1616 0.1566 0.2795 -0.0254 0.0036  0.0152  333 HOH   A O   
6683 O  O   . HOH   G .   ? 0.2472 0.3688 0.4880 -0.0169 0.0992  0.1896  334 HOH   A O   
6684 O  O   . HOH   G .   ? 0.6200 0.6636 0.4814 0.0351  -0.0130 -0.1140 335 HOH   A O   
6685 O  O   . HOH   G .   ? 0.5422 0.1941 0.4557 0.0170  -0.1786 0.0508  336 HOH   A O   
6686 O  O   . HOH   G .   ? 0.2261 0.4450 0.4030 -0.0469 -0.0791 0.1740  337 HOH   A O   
6687 O  O   . HOH   G .   ? 0.5939 0.3858 0.3361 -0.0057 -0.0187 0.1260  338 HOH   A O   
6688 O  O   . HOH   G .   ? 0.2547 0.2284 0.3084 0.0424  0.0306  0.0427  339 HOH   A O   
6689 O  O   . HOH   G .   ? 0.2470 0.4054 0.3715 0.0958  -0.0636 -0.0379 340 HOH   A O   
6690 O  O   . HOH   G .   ? 0.2787 0.3916 0.3836 -0.0853 -0.0507 -0.0088 341 HOH   A O   
6691 O  O   . HOH   G .   ? 0.6417 0.5003 0.4510 -0.0810 0.1314  0.2053  342 HOH   A O   
6692 O  O   A HOH   G .   ? 0.1851 0.3107 0.2375 0.0237  0.0279  0.0104  343 HOH   A O   
6693 O  O   . HOH   G .   ? 0.4873 0.2768 0.3054 -0.1090 0.0410  0.0422  344 HOH   A O   
6694 O  O   . HOH   G .   ? 0.5223 0.2201 0.5633 0.0747  -0.0136 0.0116  345 HOH   A O   
6695 O  O   . HOH   G .   ? 0.2148 0.1699 0.1871 -0.0061 0.0180  0.0269  346 HOH   A O   
6696 O  O   . HOH   G .   ? 0.1605 0.1947 0.2709 0.0112  -0.0369 -0.0634 347 HOH   A O   
6697 O  O   . HOH   G .   ? 0.2529 0.2917 0.3515 -0.0025 -0.0224 -0.0729 348 HOH   A O   
6698 O  O   . HOH   G .   ? 0.1481 0.2140 0.2350 0.0023  -0.0086 0.0519  349 HOH   A O   
6699 O  O   . HOH   G .   ? 0.3208 0.3970 0.3575 -0.1506 0.0893  -0.0106 350 HOH   A O   
6700 O  O   . HOH   G .   ? 0.1948 0.2054 0.4478 0.0170  0.1031  -0.0091 351 HOH   A O   
6701 O  O   A HOH   G .   ? 0.5498 0.1921 0.2464 -0.0177 0.0320  0.0051  352 HOH   A O   
6702 O  O   . HOH   G .   ? 0.3982 0.4529 0.4471 0.2063  0.0763  0.0385  353 HOH   A O   
6703 O  O   . HOH   G .   ? 0.5932 0.4883 0.4681 0.0829  0.1682  -0.0941 354 HOH   A O   
6704 O  O   B HOH   G .   ? 0.1769 0.1818 0.3288 -0.0222 -0.0069 0.0017  355 HOH   A O   
6705 O  O   . HOH   G .   ? 0.4171 0.3730 0.4489 -0.0293 0.1928  0.0742  356 HOH   A O   
6706 O  O   . HOH   G .   ? 0.2072 0.1750 0.2721 0.0303  -0.0299 -0.0071 357 HOH   A O   
6707 O  O   . HOH   G .   ? 0.1524 0.2016 0.2911 0.0062  -0.0066 0.0153  358 HOH   A O   
6708 O  O   . HOH   G .   ? 0.6086 0.6528 0.4214 0.2392  -0.0406 -0.0191 359 HOH   A O   
6709 O  O   . HOH   G .   ? 0.2901 0.3372 0.4985 -0.0753 -0.0831 -0.0883 360 HOH   A O   
6710 O  O   . HOH   G .   ? 0.3415 0.3828 0.2261 -0.1122 -0.0074 -0.0680 361 HOH   A O   
6711 O  O   . HOH   G .   ? 0.3190 0.4692 0.3922 -0.0480 -0.0389 0.1309  362 HOH   A O   
6712 O  O   . HOH   G .   ? 0.2665 0.4157 0.3407 -0.0474 0.0577  -0.0054 363 HOH   A O   
6713 O  O   . HOH   G .   ? 0.2378 0.1801 0.2696 -0.0137 -0.0480 0.0016  364 HOH   A O   
6714 O  O   . HOH   G .   ? 0.1408 0.1355 0.1650 -0.0048 0.0158  0.0115  365 HOH   A O   
6715 O  O   . HOH   G .   ? 0.3917 0.2157 0.2592 0.0931  0.0578  0.0235  366 HOH   A O   
6716 O  O   . HOH   G .   ? 0.1462 0.1607 0.1873 -0.0061 -0.0181 -0.0065 367 HOH   A O   
6717 O  O   . HOH   G .   ? 0.1836 0.2402 0.2100 -0.0204 -0.0065 0.0646  368 HOH   A O   
6718 O  O   . HOH   G .   ? 0.3194 0.6382 0.3507 0.1240  0.0715  -0.0429 369 HOH   A O   
6719 O  O   . HOH   G .   ? 0.5673 0.3952 0.5566 0.0298  0.1447  -0.1408 370 HOH   A O   
6720 O  O   . HOH   G .   ? 0.1915 0.1968 0.2851 -0.0376 0.0043  0.0375  371 HOH   A O   
6721 O  O   . HOH   G .   ? 0.1726 0.1826 0.2824 -0.0220 0.0041  0.0545  372 HOH   A O   
6722 O  O   . HOH   G .   ? 0.1649 0.1424 0.2686 -0.0114 0.0181  -0.0062 373 HOH   A O   
6723 O  O   . HOH   G .   ? 0.4721 0.3059 0.4060 -0.1829 0.1631  -0.0634 374 HOH   A O   
6724 O  O   . HOH   G .   ? 0.2700 0.4497 0.2987 0.0626  0.0797  0.1788  375 HOH   A O   
6725 O  O   . HOH   G .   ? 0.2134 0.2480 0.2556 -0.0405 -0.0412 0.0588  376 HOH   A O   
6726 O  O   . HOH   G .   ? 0.1803 0.1724 0.2498 0.0161  -0.0340 0.0287  377 HOH   A O   
6727 O  O   . HOH   G .   ? 0.2704 0.2264 0.2063 -0.0742 0.0077  0.0420  378 HOH   A O   
6728 O  O   . HOH   G .   ? 0.1743 0.1893 0.2366 0.0047  -0.0241 -0.0032 379 HOH   A O   
6729 O  O   . HOH   G .   ? 0.3887 0.6890 0.5209 -0.0476 -0.1248 0.0131  380 HOH   A O   
6730 O  O   . HOH   G .   ? 0.3407 0.2912 0.3451 -0.0158 -0.0323 0.1087  381 HOH   A O   
6731 O  O   . HOH   G .   ? 0.2065 0.2956 0.3751 0.0446  0.0731  -0.0551 382 HOH   A O   
6732 O  O   . HOH   G .   ? 0.1803 0.2704 0.3123 -0.0215 0.0669  0.0789  383 HOH   A O   
6733 O  O   . HOH   G .   ? 0.4047 0.2454 0.4706 -0.1138 0.0915  0.0343  384 HOH   A O   
6734 O  O   T HOH   G .   ? 0.1199 0.1232 0.2526 -0.0152 0.0250  0.0251  385 HOH   A O   
6735 O  O   . HOH   G .   ? 0.1913 0.1964 0.1945 0.0084  0.0054  0.0150  386 HOH   A O   
6736 O  O   . HOH   G .   ? 0.3314 0.2426 0.5008 -0.0731 -0.0258 0.0060  387 HOH   A O   
6737 O  O   B HOH   G .   ? 0.1758 0.1613 0.1981 0.0052  -0.0397 -0.0027 388 HOH   A O   
6738 O  O   . HOH   G .   ? 0.1966 0.2800 0.3003 0.0433  0.0436  0.0917  389 HOH   A O   
6739 O  O   . HOH   G .   ? 0.2506 0.4166 0.3411 -0.0236 0.0800  -0.0779 390 HOH   A O   
6740 O  O   . HOH   G .   ? 0.2407 0.2231 0.3080 -0.0014 0.0005  0.0718  391 HOH   A O   
6741 O  O   . HOH   G .   ? 0.5427 0.5345 0.6633 -0.0771 -0.0029 0.1364  392 HOH   A O   
6742 O  O   . HOH   G .   ? 0.1913 0.1900 0.3979 0.0267  0.0939  0.0979  393 HOH   A O   
6743 O  O   . HOH   G .   ? 0.3264 0.3132 0.2351 0.0120  0.0677  0.0027  394 HOH   A O   
6744 O  O   . HOH   G .   ? 0.5795 0.6927 0.6372 -0.0360 0.0526  0.0013  395 HOH   A O   
6745 O  O   . HOH   G .   ? 0.2481 0.2003 0.2913 -0.0068 0.0166  0.0384  396 HOH   A O   
6746 O  O   . HOH   G .   ? 0.1489 0.1814 0.2133 0.0159  -0.0339 -0.0354 397 HOH   A O   
6747 O  O   . HOH   G .   ? 0.3932 0.6467 0.4088 -0.0737 -0.0160 0.1446  398 HOH   A O   
6748 O  O   . HOH   G .   ? 0.3313 0.3962 0.3935 -0.0704 0.1551  0.0134  399 HOH   A O   
6749 O  O   A HOH   G .   ? 0.2611 0.2860 0.2441 0.1198  0.1010  0.0528  400 HOH   A O   
6750 O  O   . HOH   G .   ? 0.3261 0.5722 0.5210 -0.0104 -0.0324 0.1811  401 HOH   A O   
6751 O  O   B HOH   G .   ? 0.3824 0.3031 0.3510 0.0481  0.0569  -0.0205 402 HOH   A O   
6752 O  O   . HOH   G .   ? 0.3364 0.6028 0.4802 0.0371  0.0987  -0.0044 403 HOH   A O   
6753 O  O   A HOH   G .   ? 0.2003 0.1876 0.3571 -0.0089 0.0485  -0.0031 404 HOH   A O   
6754 O  O   . HOH   G .   ? 0.5651 0.2982 0.5801 0.1084  -0.0398 -0.0211 405 HOH   A O   
6755 O  O   . HOH   G .   ? 0.4727 0.4829 0.2136 -0.0394 0.0857  0.0477  406 HOH   A O   
6756 O  O   . HOH   G .   ? 0.2076 0.2263 0.2982 -0.0222 -0.0339 0.0949  407 HOH   A O   
6757 O  O   . HOH   G .   ? 0.1367 0.1527 0.2164 -0.0008 -0.0196 0.0059  408 HOH   A O   
6758 O  O   B HOH   G .   ? 0.3297 0.4166 0.1971 -0.0353 0.0073  -0.0052 409 HOH   A O   
6759 O  O   . HOH   G .   ? 0.5697 0.5714 0.4761 0.0707  0.0584  0.0922  410 HOH   A O   
6760 O  O   . HOH   G .   ? 0.2394 0.1801 0.3536 0.0092  -0.0405 0.0209  411 HOH   A O   
6761 O  O   . HOH   G .   ? 0.3155 0.2835 0.2413 -0.0880 -0.0880 0.0360  412 HOH   A O   
6762 O  O   . HOH   G .   ? 0.2094 0.2485 0.3796 0.0063  -0.0194 -0.0231 413 HOH   A O   
6763 O  O   . HOH   G .   ? 0.3151 0.3436 0.2236 -0.0330 -0.0737 0.0284  414 HOH   A O   
6764 O  O   . HOH   G .   ? 0.1670 0.1486 0.1866 -0.0186 0.0098  0.0045  415 HOH   A O   
6765 O  O   . HOH   G .   ? 0.4055 0.4577 0.3900 0.1501  -0.0813 -0.1579 416 HOH   A O   
6766 O  O   . HOH   G .   ? 0.1983 0.2903 0.4248 0.0002  -0.0200 0.0465  417 HOH   A O   
6767 O  O   . HOH   G .   ? 0.3293 0.3707 0.6808 -0.0159 0.0904  -0.0648 418 HOH   A O   
6768 O  O   . HOH   G .   ? 0.2669 0.2138 0.2719 -0.0590 -0.0116 0.0590  419 HOH   A O   
6769 O  O   . HOH   G .   ? 0.2855 0.6452 0.1897 -0.0367 0.0442  0.0311  420 HOH   A O   
6770 O  O   . HOH   G .   ? 0.1642 0.1710 0.3655 -0.0020 -0.0057 0.0303  421 HOH   A O   
6771 O  O   . HOH   G .   ? 0.2201 0.3163 0.2904 -0.0265 -0.0546 0.0676  422 HOH   A O   
6772 O  O   . HOH   G .   ? 0.2171 0.1968 0.3464 0.0238  -0.0669 0.0290  423 HOH   A O   
6773 O  O   . HOH   G .   ? 0.4389 0.6191 0.3236 -0.0732 -0.0016 0.1081  424 HOH   A O   
6774 O  O   . HOH   G .   ? 0.1686 0.2146 0.3104 -0.0112 0.0059  0.0498  425 HOH   A O   
6775 O  O   . HOH   G .   ? 0.3617 0.1333 0.2315 -0.0013 -0.0611 0.0127  426 HOH   A O   
6776 O  O   . HOH   G .   ? 0.2467 0.4647 0.2768 0.1695  0.0020  0.0453  427 HOH   A O   
6777 O  O   . HOH   G .   ? 0.4402 0.2326 0.5586 -0.0975 -0.2225 0.1039  428 HOH   A O   
6778 O  O   . HOH   G .   ? 0.5005 0.5276 0.3476 0.2771  0.0148  -0.0500 429 HOH   A O   
6779 O  O   . HOH   G .   ? 0.5518 0.6876 0.6730 -0.0576 -0.0570 -0.0418 430 HOH   A O   
6780 O  O   A HOH   G .   ? 0.2576 0.3074 0.2642 -0.0265 0.0884  -0.0203 431 HOH   A O   
6781 O  O   . HOH   G .   ? 0.6830 0.3975 0.4790 0.1778  -0.1079 0.1301  432 HOH   A O   
6782 O  O   . HOH   G .   ? 0.8638 0.9112 0.7281 -0.0122 -0.0206 -0.0938 433 HOH   A O   
6783 O  O   . HOH   G .   ? 0.8149 0.5279 0.4727 -0.0143 0.1506  0.1893  434 HOH   A O   
6784 O  O   . HOH   G .   ? 0.3699 0.3759 0.2555 -0.0617 -0.0495 0.0435  435 HOH   A O   
6785 O  O   . HOH   G .   ? 0.5191 0.4702 0.4941 -0.0707 -0.0967 -0.1230 436 HOH   A O   
6786 O  O   . HOH   G .   ? 0.6180 0.7548 0.4361 0.0850  0.2691  -0.0523 437 HOH   A O   
6787 O  O   . HOH   G .   ? 0.5221 0.4954 0.3666 -0.0243 -0.1433 0.0186  438 HOH   A O   
6788 O  O   . HOH   G .   ? 0.2763 0.1721 0.3350 0.0171  0.0078  0.0145  439 HOH   A O   
6789 O  O   . HOH   G .   ? 0.4882 0.5679 0.6134 0.1117  0.1420  -0.1017 440 HOH   A O   
6790 O  O   . HOH   G .   ? 0.1939 0.2243 0.5203 -0.0245 -0.0864 0.0567  441 HOH   A O   
6791 O  O   . HOH   G .   ? 0.5824 0.8496 0.4513 0.1896  -0.1133 0.2095  442 HOH   A O   
6792 O  O   . HOH   G .   ? 0.3770 0.3013 0.2159 -0.0812 0.0152  0.0724  443 HOH   A O   
6793 O  O   . HOH   G .   ? 0.1841 0.1763 0.1979 -0.0023 -0.0189 -0.0154 444 HOH   A O   
6794 O  O   . HOH   G .   ? 0.4625 0.3520 0.3667 0.2331  -0.0597 -0.0213 445 HOH   A O   
6795 O  O   A HOH   G .   ? 0.4640 0.3148 0.2879 -0.0506 0.0994  0.0411  446 HOH   A O   
6796 O  O   . HOH   G .   ? 0.5839 0.5730 0.6904 -0.1427 0.0260  -0.1278 447 HOH   A O   
6797 O  O   A HOH   G .   ? 0.2118 0.1730 0.2136 -0.0344 -0.0150 -0.0156 448 HOH   A O   
6798 O  O   . HOH   G .   ? 0.2358 0.2058 0.2863 0.0093  0.0201  0.0332  449 HOH   A O   
6799 O  O   . HOH   G .   ? 0.6312 0.5886 0.4780 -0.0838 0.0771  0.1147  450 HOH   A O   
6800 O  O   . HOH   G .   ? 0.2282 0.2965 0.2775 -0.0077 -0.0111 -0.0533 451 HOH   A O   
6801 O  O   . HOH   G .   ? 0.2734 0.4055 0.4976 0.0000  0.0719  -0.1655 452 HOH   A O   
6802 O  O   . HOH   G .   ? 0.6170 0.6714 0.6112 0.1005  -0.1025 -0.0434 453 HOH   A O   
6803 O  O   . HOH   G .   ? 0.6584 0.5312 0.7571 0.1155  -0.0934 0.1662  454 HOH   A O   
6804 O  O   B HOH   G .   ? 0.2772 0.3168 0.4717 0.0897  -0.1264 -0.0640 455 HOH   A O   
6805 O  O   . HOH   G .   ? 0.4026 0.5256 0.4522 0.0513  -0.0053 0.0840  456 HOH   A O   
6806 O  O   . HOH   G .   ? 0.5265 0.4245 0.4370 0.0051  0.1124  0.0525  457 HOH   A O   
6807 O  O   . HOH   G .   ? 0.3726 0.3442 0.4552 0.0167  0.0584  0.0235  458 HOH   A O   
6808 O  O   . HOH   G .   ? 0.3217 0.3989 0.4113 0.1244  -0.0363 0.0915  459 HOH   A O   
6809 O  O   . HOH   G .   ? 0.7323 0.7744 0.4980 0.0750  -0.0800 -0.0719 460 HOH   A O   
6810 O  O   B HOH   G .   ? 0.2791 0.3152 0.3529 0.0095  0.0699  -0.1079 461 HOH   A O   
6811 O  O   . HOH   G .   ? 0.2757 0.2781 0.3897 -0.0454 0.0335  -0.0734 462 HOH   A O   
6812 O  O   . HOH   G .   ? 0.3741 0.6122 0.5013 -0.1260 0.1321  -0.0941 463 HOH   A O   
6813 O  O   . HOH   G .   ? 0.3290 0.5690 0.4969 0.0780  -0.0525 0.1669  464 HOH   A O   
6814 O  O   . HOH   G .   ? 0.4936 0.5382 0.4945 0.0501  -0.0527 -0.0679 465 HOH   A O   
6815 O  O   . HOH   G .   ? 0.7414 0.6950 0.5498 0.1828  -0.1474 -0.0454 466 HOH   A O   
6816 O  O   . HOH   G .   ? 0.3002 0.2794 0.6437 0.0657  -0.1408 -0.0541 467 HOH   A O   
6817 O  O   . HOH   G .   ? 0.6659 0.3993 0.7296 0.0817  0.0221  0.2785  468 HOH   A O   
6818 O  O   . HOH   G .   ? 0.2681 0.3040 0.3603 -0.1054 0.0384  -0.0304 469 HOH   A O   
6819 O  O   . HOH   G .   ? 0.2687 0.4407 0.5379 0.0607  0.0110  -0.1591 470 HOH   A O   
6820 O  O   . HOH   G .   ? 0.5336 0.4982 0.4618 0.0002  0.0868  0.0502  471 HOH   A O   
6821 O  O   . HOH   G .   ? 0.4096 0.6696 0.4144 -0.0684 -0.0820 0.2411  472 HOH   A O   
6822 O  O   . HOH   G .   ? 0.4045 0.5121 0.3864 0.0430  -0.0395 -0.0574 473 HOH   A O   
6823 O  O   . HOH   G .   ? 0.4070 0.4910 0.3786 -0.1105 -0.0110 0.0065  474 HOH   A O   
6824 O  O   . HOH   G .   ? 0.4569 0.4801 0.2874 0.0282  0.0072  -0.0123 475 HOH   A O   
6825 O  O   . HOH   G .   ? 0.6405 0.6473 0.6584 0.0924  0.1374  0.2494  476 HOH   A O   
6826 O  O   . HOH   G .   ? 0.2683 0.1806 0.2831 0.0275  -0.0781 -0.0361 477 HOH   A O   
6827 O  O   . HOH   G .   ? 0.3661 0.2611 0.3342 0.0102  0.0562  0.0066  478 HOH   A O   
6828 O  O   . HOH   G .   ? 0.4530 0.2957 0.3514 -0.0710 -0.1173 0.0701  479 HOH   A O   
6829 O  O   . HOH   G .   ? 0.6019 0.3880 0.4629 -0.0233 0.1037  -0.0311 480 HOH   A O   
6830 O  O   . HOH   G .   ? 0.5312 0.5801 0.6341 -0.1651 -0.1375 0.0445  481 HOH   A O   
6831 O  O   . HOH   G .   ? 0.4239 0.5009 0.3166 0.0018  -0.0389 -0.0492 482 HOH   A O   
6832 O  O   . HOH   G .   ? 0.4749 0.4618 0.5078 -0.1807 -0.0556 -0.0272 483 HOH   A O   
6833 O  O   . HOH   G .   ? 0.6764 0.5615 0.5469 -0.0894 -0.1041 -0.0986 484 HOH   A O   
6834 O  O   . HOH   G .   ? 0.5689 0.4004 0.4575 0.0378  -0.0384 -0.1211 485 HOH   A O   
6835 O  O   . HOH   G .   ? 0.6879 0.6100 0.6568 -0.1011 0.0760  -0.0856 486 HOH   A O   
6836 O  O   . HOH   G .   ? 0.3510 0.4330 0.5126 0.0254  0.1550  0.1428  487 HOH   A O   
6837 O  O   . HOH   G .   ? 0.8371 0.4041 0.3537 -0.0264 -0.1315 0.0369  488 HOH   A O   
6838 O  O   . HOH   G .   ? 0.6521 0.6281 0.6868 0.1005  0.2609  -0.1148 489 HOH   A O   
6839 O  O   . HOH   G .   ? 0.2602 0.2280 0.2784 0.0261  -0.0162 -0.0007 490 HOH   A O   
6840 O  O   . HOH   G .   ? 0.2883 0.5635 0.3700 0.1336  0.1040  0.2412  491 HOH   A O   
6841 O  O   . HOH   G .   ? 0.2611 0.2524 0.7037 -0.0028 -0.1242 0.0238  492 HOH   A O   
6842 O  O   . HOH   G .   ? 0.5672 0.5762 0.5609 0.0427  -0.1105 0.1035  493 HOH   A O   
6843 O  O   . HOH   G .   ? 0.5078 0.3995 0.2816 -0.1236 0.1499  -0.0758 494 HOH   A O   
6844 O  O   . HOH   G .   ? 0.5925 0.6800 0.4418 -0.0657 0.1261  0.1587  495 HOH   A O   
6845 O  O   . HOH   G .   ? 0.3175 0.4564 0.3411 -0.0114 -0.0510 -0.0696 496 HOH   A O   
6846 O  O   . HOH   G .   ? 0.4427 0.3336 0.5154 -0.1158 0.0085  0.1053  497 HOH   A O   
6847 O  O   . HOH   G .   ? 0.4870 0.3257 0.4660 -0.0088 0.2354  0.0121  498 HOH   A O   
6848 O  O   . HOH   G .   ? 0.2624 0.3651 0.4902 -0.0048 0.0853  -0.0651 499 HOH   A O   
6849 O  O   . HOH   G .   ? 0.3159 0.2329 0.5972 0.0054  0.0297  0.0821  500 HOH   A O   
6850 O  O   . HOH   G .   ? 0.6831 0.2504 0.4310 -0.0636 0.0807  0.0494  501 HOH   A O   
6851 O  O   . HOH   G .   ? 0.4650 0.8243 0.5932 -0.1231 -0.0897 0.2080  502 HOH   A O   
6852 O  O   . HOH   G .   ? 0.2625 0.4176 0.3267 0.0805  -0.0249 0.0677  503 HOH   A O   
6853 O  O   . HOH   G .   ? 0.2577 0.4284 0.4719 0.0291  -0.0558 0.0055  504 HOH   A O   
6854 O  O   B HOH   G .   ? 0.2576 0.4518 0.3821 0.0226  0.0562  0.0489  505 HOH   A O   
6855 O  O   . HOH   G .   ? 0.5851 0.7496 0.5139 0.1200  -0.0863 0.0430  506 HOH   A O   
6856 O  O   . HOH   G .   ? 0.7799 0.3833 0.5578 0.1312  -0.0458 0.0672  507 HOH   A O   
6857 O  O   . HOH   G .   ? 0.5728 0.7163 0.5414 0.3308  -0.0040 0.1670  508 HOH   A O   
6858 O  O   . HOH   G .   ? 0.3026 0.2444 0.4739 0.0120  0.0216  0.0579  509 HOH   A O   
6859 O  O   T HOH   G .   ? 0.1205 0.1082 0.2148 -0.0155 -0.0014 0.0395  510 HOH   A O   
6860 O  O   . HOH   G .   ? 0.5627 0.6017 0.4502 -0.0815 -0.0681 -0.1270 511 HOH   A O   
6861 O  O   A HOH   G .   ? 0.4067 0.8218 0.3601 0.1857  0.0816  -0.0384 512 HOH   A O   
6862 O  O   . HOH   G .   ? 0.2997 0.6799 0.4479 0.0457  0.0393  -0.0594 513 HOH   A O   
6863 O  O   . HOH   G .   ? 0.5470 0.4392 0.5144 0.1506  -0.0079 0.1190  514 HOH   A O   
6864 O  O   . HOH   G .   ? 0.4778 0.6577 0.5483 -0.0565 -0.0704 0.0371  515 HOH   A O   
6865 O  O   . HOH   G .   ? 0.3346 0.4428 0.5792 -0.0101 -0.0954 0.2717  516 HOH   A O   
6866 O  O   . HOH   H .   ? 0.2423 0.2364 0.3394 0.0121  0.0856  0.0344  201 HOH   B O   
6867 O  O   . HOH   H .   ? 0.3571 0.3571 0.6569 -0.0573 0.0314  -0.0569 202 HOH   B O   
6868 O  O   . HOH   H .   ? 0.5090 0.3883 0.4369 -0.0168 -0.0206 -0.1371 203 HOH   B O   
6869 O  O   . HOH   H .   ? 0.3011 0.2113 0.5910 0.0083  0.1902  0.0803  204 HOH   B O   
6870 O  O   . HOH   H .   ? 0.6670 0.5954 0.5835 0.2323  0.0291  0.0105  205 HOH   B O   
6871 O  O   . HOH   H .   ? 0.3948 0.4466 0.5256 -0.1018 0.0094  -0.1324 206 HOH   B O   
6872 O  O   . HOH   H .   ? 0.3283 0.6794 0.3697 0.0826  0.0095  0.2209  207 HOH   B O   
6873 O  O   . HOH   H .   ? 0.4817 0.6318 0.3910 0.2966  -0.1045 -0.0188 208 HOH   B O   
6874 O  O   . HOH   H .   ? 0.1727 0.2125 0.3020 -0.0176 -0.0146 0.0040  209 HOH   B O   
6875 O  O   . HOH   H .   ? 0.4782 0.4110 0.3540 0.0280  -0.1196 0.0706  210 HOH   B O   
6876 O  O   . HOH   H .   ? 0.2890 0.2651 0.6350 0.0533  -0.1033 0.0603  211 HOH   B O   
6877 O  O   . HOH   H .   ? 0.1920 0.2260 0.3334 -0.0029 0.0285  -0.0301 212 HOH   B O   
6878 O  O   . HOH   H .   ? 0.3277 0.2391 0.5361 -0.0127 0.1852  0.0218  213 HOH   B O   
6879 O  O   . HOH   H .   ? 0.2835 0.5664 0.5063 -0.0316 0.1389  -0.1847 214 HOH   B O   
6880 O  O   . HOH   H .   ? 0.3850 0.3981 0.5039 0.0924  -0.0460 0.0537  215 HOH   B O   
6881 O  O   . HOH   H .   ? 0.4721 0.5329 0.4233 0.2574  -0.0406 0.0361  216 HOH   B O   
6882 O  O   . HOH   H .   ? 0.4778 0.6212 0.3730 0.2231  0.0436  0.0171  217 HOH   B O   
6883 O  O   . HOH   H .   ? 0.4849 0.4148 0.5883 0.0314  -0.1096 0.2597  218 HOH   B O   
6884 O  O   . HOH   H .   ? 0.7288 0.3534 0.4790 0.1153  0.1345  0.0230  219 HOH   B O   
6885 O  O   . HOH   H .   ? 0.5781 0.6274 0.2948 0.0887  -0.0291 -0.1494 220 HOH   B O   
6886 O  O   . HOH   H .   ? 0.2378 0.2245 0.3961 -0.0366 0.0001  -0.0442 221 HOH   B O   
6887 O  O   . HOH   H .   ? 0.6503 0.3965 0.2752 -0.0685 0.0194  -0.0032 222 HOH   B O   
6888 O  O   . HOH   H .   ? 0.3955 0.5128 0.3844 0.0268  0.0396  -0.1615 223 HOH   B O   
6889 O  O   . HOH   H .   ? 0.4785 0.4893 0.5875 -0.0255 -0.1597 -0.1111 224 HOH   B O   
6890 O  O   . HOH   H .   ? 0.1756 0.2274 0.3531 -0.0234 0.0017  -0.0068 225 HOH   B O   
6891 O  O   . HOH   H .   ? 0.3531 0.5217 0.4864 0.2332  0.0380  -0.0377 226 HOH   B O   
6892 O  O   . HOH   H .   ? 0.7343 0.5167 0.4446 0.2122  -0.0347 -0.1266 227 HOH   B O   
6893 O  O   . HOH   H .   ? 0.5040 0.2985 0.3763 -0.1308 -0.0144 0.0018  228 HOH   B O   
6894 O  O   . HOH   H .   ? 0.5023 0.2159 0.3124 -0.0004 -0.0992 0.0096  229 HOH   B O   
6895 O  O   . HOH   H .   ? 0.2446 0.1868 0.2906 -0.0269 0.0980  -0.0026 230 HOH   B O   
6896 O  O   . HOH   H .   ? 0.3745 0.1764 0.2164 0.0092  -0.0753 -0.0061 231 HOH   B O   
6897 O  O   . HOH   H .   ? 0.2310 0.2892 0.3402 -0.0779 0.0010  -0.0106 232 HOH   B O   
6898 O  O   . HOH   H .   ? 0.3578 0.3135 0.2231 0.0218  0.0427  0.0353  233 HOH   B O   
6899 O  O   . HOH   H .   ? 0.2516 0.2111 0.2871 0.0709  -0.0815 -0.0589 234 HOH   B O   
6900 O  O   . HOH   H .   ? 0.2091 0.1428 0.3547 0.0069  -0.0494 -0.0083 235 HOH   B O   
6901 O  O   . HOH   H .   ? 0.2747 0.2593 0.3115 0.0351  0.0174  -0.0788 236 HOH   B O   
6902 O  O   . HOH   H .   ? 0.4091 0.5024 0.5335 -0.1534 -0.0215 0.0679  237 HOH   B O   
6903 O  O   . HOH   H .   ? 0.5053 0.3803 0.3448 -0.1044 0.0700  -0.0932 238 HOH   B O   
6904 O  O   . HOH   H .   ? 0.3764 0.2816 0.4143 0.0737  -0.0314 -0.0411 239 HOH   B O   
6905 O  O   . HOH   H .   ? 0.2839 0.4048 0.3126 -0.0990 0.0274  -0.0413 240 HOH   B O   
6906 O  O   . HOH   H .   ? 0.5909 0.2950 0.4024 -0.2179 -0.0329 0.0313  241 HOH   B O   
6907 O  O   . HOH   H .   ? 0.3665 0.2578 0.4154 0.0326  -0.0783 -0.1256 242 HOH   B O   
6908 O  O   . HOH   H .   ? 0.2797 0.2424 0.2917 0.0783  0.0640  0.0022  243 HOH   B O   
6909 O  O   . HOH   H .   ? 0.1695 0.1589 0.2963 -0.0021 0.0050  -0.0038 244 HOH   B O   
6910 O  O   . HOH   H .   ? 0.3071 0.1850 0.6444 -0.0159 -0.1106 -0.0302 245 HOH   B O   
6911 O  O   . HOH   H .   ? 0.2280 0.3813 0.2477 -0.0456 -0.0239 0.0519  246 HOH   B O   
6912 O  O   . HOH   H .   ? 0.1566 0.1537 0.1739 -0.0147 -0.0109 -0.0007 247 HOH   B O   
6913 O  O   . HOH   H .   ? 0.1579 0.1406 0.1891 -0.0030 -0.0124 0.0073  248 HOH   B O   
6914 O  O   . HOH   H .   ? 0.2340 0.4017 0.3471 -0.0685 -0.0579 -0.0513 249 HOH   B O   
6915 O  O   . HOH   H .   ? 0.3060 0.4258 0.2885 -0.0946 -0.0408 -0.0549 250 HOH   B O   
6916 O  O   . HOH   H .   ? 0.2485 0.5773 0.5580 0.1417  -0.0670 -0.1184 251 HOH   B O   
6917 O  O   . HOH   H .   ? 0.6058 0.6219 0.3756 0.0046  -0.0498 0.0272  252 HOH   B O   
6918 O  O   . HOH   H .   ? 0.2338 0.1977 0.2418 -0.0336 -0.0367 0.0116  253 HOH   B O   
6919 O  O   . HOH   H .   ? 0.3527 0.4916 0.3565 -0.0354 -0.1277 0.1050  254 HOH   B O   
6920 O  O   . HOH   H .   ? 0.2401 0.3282 0.2329 -0.0676 0.0340  0.0384  255 HOH   B O   
6921 O  O   . HOH   H .   ? 0.2222 0.1585 0.2302 -0.0309 -0.0478 0.0263  256 HOH   B O   
6922 O  O   . HOH   H .   ? 0.1685 0.1818 0.3543 -0.0264 -0.0299 0.0214  257 HOH   B O   
6923 O  O   . HOH   H .   ? 0.3753 0.2688 0.3208 -0.0398 0.0238  -0.0609 258 HOH   B O   
6924 O  O   . HOH   H .   ? 0.3374 0.4353 0.2486 0.0137  0.0737  0.0242  259 HOH   B O   
6925 O  O   . HOH   H .   ? 0.2253 0.4480 0.5547 -0.0491 -0.0550 -0.1139 260 HOH   B O   
6926 O  O   . HOH   H .   ? 0.2228 0.1932 0.3983 0.0017  -0.0643 -0.0343 261 HOH   B O   
6927 O  O   . HOH   H .   ? 0.3606 0.3345 0.6694 0.0052  0.0555  0.0121  262 HOH   B O   
6928 O  O   . HOH   H .   ? 0.1426 0.1741 0.2644 -0.0093 0.0085  0.0155  263 HOH   B O   
6929 O  O   . HOH   H .   ? 0.2729 0.3903 0.3590 0.0195  0.1119  0.0378  264 HOH   B O   
6930 O  O   . HOH   H .   ? 0.2584 0.2153 0.2292 0.0157  -0.0176 -0.0128 265 HOH   B O   
6931 O  O   . HOH   H .   ? 0.2870 0.2262 0.2240 0.0127  -0.0098 -0.0029 266 HOH   B O   
6932 O  O   . HOH   H .   ? 0.2637 0.1989 0.3105 -0.0581 0.0242  -0.0115 267 HOH   B O   
6933 O  O   . HOH   H .   ? 0.3426 0.3564 0.5017 0.0214  -0.0045 -0.0048 268 HOH   B O   
6934 O  O   . HOH   H .   ? 0.2693 0.4547 0.2330 0.1603  -0.0342 -0.0503 269 HOH   B O   
6935 O  O   . HOH   H .   ? 0.2599 0.2891 0.2602 -0.0481 -0.0829 0.0354  270 HOH   B O   
6936 O  O   . HOH   H .   ? 0.2161 0.1603 0.2511 -0.0299 -0.0175 0.0142  271 HOH   B O   
6937 O  O   . HOH   H .   ? 0.4198 0.2947 0.4760 -0.0176 -0.1240 -0.0604 272 HOH   B O   
6938 O  O   . HOH   H .   ? 0.2388 0.5793 0.5860 0.0365  0.0461  -0.1213 273 HOH   B O   
6939 O  O   . HOH   H .   ? 0.2517 0.2543 0.2601 -0.0368 -0.0747 -0.0335 274 HOH   B O   
6940 O  O   . HOH   H .   ? 0.1964 0.1810 0.1978 -0.0448 -0.0510 0.0193  275 HOH   B O   
6941 O  O   . HOH   H .   ? 0.3156 0.2263 0.4952 0.0114  0.0530  0.0520  276 HOH   B O   
6942 O  O   . HOH   H .   ? 0.3944 0.4229 0.5063 0.1666  -0.0822 -0.1202 277 HOH   B O   
6943 O  O   . HOH   H .   ? 0.2507 0.3905 0.3602 -0.0756 0.0386  -0.1316 278 HOH   B O   
6944 O  O   . HOH   H .   ? 0.4764 0.4130 0.3050 0.0438  -0.0008 -0.0733 279 HOH   B O   
6945 O  O   . HOH   H .   ? 0.1939 0.1456 0.4191 -0.0099 -0.0332 -0.0096 280 HOH   B O   
6946 O  O   . HOH   H .   ? 0.1737 0.1639 0.3850 -0.0134 0.0013  -0.0057 281 HOH   B O   
6947 O  O   . HOH   H .   ? 0.5454 0.7384 0.2650 0.0165  -0.0557 0.0046  282 HOH   B O   
6948 O  O   . HOH   H .   ? 0.1843 0.1574 0.2157 0.0024  0.0103  0.0010  283 HOH   B O   
6949 O  O   . HOH   H .   ? 0.3559 0.3047 0.3088 -0.0512 0.0028  -0.1245 284 HOH   B O   
6950 O  O   . HOH   H .   ? 0.2592 0.7149 0.2639 0.0722  -0.0352 -0.0704 285 HOH   B O   
6951 O  O   . HOH   H .   ? 0.2792 0.7146 0.6966 0.1586  -0.0656 -0.0956 286 HOH   B O   
6952 O  O   . HOH   H .   ? 0.3048 0.5004 0.4645 -0.1221 -0.1281 0.0873  287 HOH   B O   
6953 O  O   . HOH   H .   ? 0.5945 0.3889 0.3358 0.2648  0.1225  0.0941  288 HOH   B O   
6954 O  O   . HOH   H .   ? 0.1803 0.2058 0.1768 -0.0166 -0.0188 0.0046  289 HOH   B O   
6955 O  O   . HOH   H .   ? 0.4095 0.2310 0.4221 -0.1186 -0.2008 0.0947  290 HOH   B O   
6956 O  O   . HOH   H .   ? 0.2736 0.2811 0.3127 0.0153  -0.0886 0.0221  291 HOH   B O   
6957 O  O   . HOH   H .   ? 0.1761 0.2232 0.3156 0.0152  -0.0010 0.0052  292 HOH   B O   
6958 O  O   . HOH   H .   ? 0.4293 0.3783 0.2670 0.0847  -0.0875 0.0654  293 HOH   B O   
6959 O  O   . HOH   H .   ? 0.4712 0.5058 0.2755 0.0230  0.0923  0.1016  294 HOH   B O   
6960 O  O   . HOH   H .   ? 0.3273 0.3173 0.5319 -0.0500 -0.1003 0.1298  295 HOH   B O   
6961 O  O   . HOH   H .   ? 0.3753 0.2711 0.2356 0.0245  -0.0904 -0.0150 296 HOH   B O   
6962 O  O   . HOH   H .   ? 0.3798 0.7068 0.3378 0.1671  -0.0382 0.0630  297 HOH   B O   
6963 O  O   . HOH   H .   ? 0.1819 0.3683 0.5069 0.0302  0.0023  -0.1512 298 HOH   B O   
6964 O  O   . HOH   H .   ? 0.2044 0.3268 0.6459 0.0517  -0.0638 -0.1181 299 HOH   B O   
6965 O  O   . HOH   H .   ? 0.4714 0.2943 0.2443 -0.1745 0.0395  -0.0142 300 HOH   B O   
6966 O  O   . HOH   H .   ? 0.2207 0.1681 0.2617 0.0063  0.0193  0.0182  301 HOH   B O   
6967 O  O   . HOH   H .   ? 0.4445 0.5190 0.4907 0.0200  -0.1502 0.0331  302 HOH   B O   
6968 O  O   . HOH   H .   ? 0.2183 0.1656 0.3725 0.0439  -0.0901 -0.0123 303 HOH   B O   
6969 O  O   . HOH   H .   ? 0.4157 0.4209 0.3943 -0.1885 0.1260  -0.0514 304 HOH   B O   
6970 O  O   . HOH   H .   ? 0.2220 0.1701 0.2981 -0.0319 -0.0402 -0.0009 305 HOH   B O   
6971 O  O   . HOH   H .   ? 0.2320 0.2348 0.5706 -0.0508 0.0072  0.1335  306 HOH   B O   
6972 O  O   . HOH   H .   ? 0.2359 0.3160 0.4691 -0.0238 -0.0571 -0.0071 307 HOH   B O   
6973 O  O   . HOH   H .   ? 0.3606 0.1957 0.3379 0.0658  0.1027  0.0381  308 HOH   B O   
6974 O  O   . HOH   H .   ? 0.2197 0.5880 0.5302 -0.0781 -0.0380 0.0189  309 HOH   B O   
6975 O  O   . HOH   H .   ? 0.3148 0.3050 0.3683 -0.0440 0.1179  -0.0882 310 HOH   B O   
6976 O  O   . HOH   H .   ? 0.1652 0.1586 0.3677 0.0083  -0.0059 -0.0021 311 HOH   B O   
6977 O  O   . HOH   H .   ? 0.2604 0.1595 0.2860 -0.0257 -0.0321 0.0376  312 HOH   B O   
6978 O  O   . HOH   H .   ? 0.5680 0.3910 0.2864 -0.0119 -0.0738 -0.0582 313 HOH   B O   
6979 O  O   . HOH   H .   ? 0.4700 0.3699 0.4879 -0.0693 0.0260  0.1245  314 HOH   B O   
6980 O  O   . HOH   H .   ? 0.2379 0.2027 0.2273 -0.0103 0.0177  0.0263  315 HOH   B O   
6981 O  O   . HOH   H .   ? 0.1706 0.1947 0.3274 -0.0271 -0.0165 0.0181  316 HOH   B O   
6982 O  O   . HOH   H .   ? 0.4324 0.2507 0.2811 0.1658  0.1087  0.0394  317 HOH   B O   
6983 O  O   . HOH   H .   ? 0.1756 0.3093 0.2635 -0.0250 -0.0112 0.0802  318 HOH   B O   
6984 O  O   . HOH   H .   ? 0.1686 0.1725 0.3484 -0.0135 -0.0196 -0.0121 319 HOH   B O   
6985 O  O   . HOH   H .   ? 0.6047 0.6060 0.5036 0.2810  -0.0022 0.0172  320 HOH   B O   
6986 O  O   . HOH   H .   ? 0.4428 0.3970 0.5561 0.0498  -0.0026 0.0558  321 HOH   B O   
6987 O  O   . HOH   H .   ? 0.3683 0.4333 0.7658 -0.0481 -0.1069 0.2447  322 HOH   B O   
6988 O  O   . HOH   H .   ? 0.6075 0.4770 0.5666 0.0819  0.1603  -0.0001 323 HOH   B O   
6989 O  O   . HOH   H .   ? 0.4463 0.3251 0.5288 0.1305  0.2120  0.1628  324 HOH   B O   
6990 O  O   . HOH   H .   ? 0.2006 0.2078 0.3093 0.0312  0.0406  0.0231  325 HOH   B O   
6991 O  O   . HOH   H .   ? 0.3417 0.2422 0.2434 0.0335  -0.0235 0.0245  326 HOH   B O   
6992 O  O   . HOH   H .   ? 0.5890 0.4682 0.6682 0.1268  -0.0862 0.1702  327 HOH   B O   
6993 O  O   . HOH   H .   ? 0.1882 0.2911 0.3461 0.0389  -0.0137 -0.0526 328 HOH   B O   
6994 O  O   . HOH   H .   ? 0.4812 0.2662 0.3193 0.0194  0.0234  0.0846  329 HOH   B O   
6995 O  O   . HOH   H .   ? 0.2889 0.2188 0.5276 -0.0270 0.0052  0.0430  330 HOH   B O   
6996 O  O   . HOH   H .   ? 0.8093 0.2118 0.3541 0.0161  -0.0894 0.0017  331 HOH   B O   
6997 O  O   . HOH   H .   ? 0.4790 0.4466 0.2292 0.1439  -0.0922 -0.0559 332 HOH   B O   
6998 O  O   . HOH   H .   ? 0.2819 0.3372 0.5482 -0.0565 -0.1697 0.1461  333 HOH   B O   
6999 O  O   . HOH   H .   ? 0.5290 0.3988 0.4111 0.0873  0.1283  0.1673  334 HOH   B O   
7000 O  O   . HOH   H .   ? 0.1858 0.1528 0.2637 0.0084  -0.0181 0.0058  335 HOH   B O   
7001 O  O   . HOH   H .   ? 0.6011 0.5780 0.5396 -0.1179 -0.0797 0.1773  336 HOH   B O   
7002 O  O   . HOH   H .   ? 0.5437 0.3693 0.4505 -0.0182 0.0759  -0.1412 337 HOH   B O   
7003 O  O   . HOH   H .   ? 0.4534 0.7124 0.3876 -0.0049 -0.0537 0.2035  338 HOH   B O   
7004 O  O   . HOH   H .   ? 0.5443 0.4482 0.5473 -0.0369 -0.0922 -0.0938 339 HOH   B O   
7005 O  O   . HOH   H .   ? 0.5657 0.3049 0.3102 0.0577  -0.1376 -0.0835 340 HOH   B O   
7006 O  O   . HOH   H .   ? 0.4136 0.6393 0.4051 -0.1274 -0.1008 -0.0659 341 HOH   B O   
7007 O  O   . HOH   H .   ? 0.7211 0.7195 0.3153 0.0023  -0.0682 0.0700  342 HOH   B O   
7008 O  O   . HOH   H .   ? 0.2189 0.5939 0.6619 0.0314  -0.0570 0.0155  343 HOH   B O   
7009 O  O   . HOH   H .   ? 0.5391 0.5546 0.3788 0.0325  -0.1251 -0.0055 344 HOH   B O   
7010 O  O   . HOH   H .   ? 0.2119 0.2112 0.3701 -0.0146 0.0678  -0.0151 345 HOH   B O   
7011 O  O   . HOH   H .   ? 0.4203 0.5521 0.5513 0.0090  -0.0860 0.0661  346 HOH   B O   
7012 O  O   . HOH   H .   ? 0.3181 0.1977 0.4025 0.0229  -0.1118 -0.0493 347 HOH   B O   
7013 O  O   . HOH   H .   ? 0.5030 0.5854 0.5506 -0.1232 0.0413  0.1306  348 HOH   B O   
7014 O  O   . HOH   H .   ? 0.2796 0.2370 0.4887 -0.0324 -0.0777 -0.0527 349 HOH   B O   
7015 O  O   . HOH   H .   ? 0.2592 0.6565 0.3580 0.1719  -0.0619 -0.1357 350 HOH   B O   
7016 O  O   . HOH   H .   ? 0.2285 0.4299 0.5049 0.0258  0.0183  -0.0107 351 HOH   B O   
7017 O  O   . HOH   H .   ? 0.4393 0.5433 0.6239 -0.0286 -0.0007 -0.0898 352 HOH   B O   
7018 O  O   . HOH   H .   ? 0.4011 0.2191 0.3260 -0.0668 0.0224  -0.0680 353 HOH   B O   
7019 O  O   . HOH   H .   ? 0.3623 0.5071 0.5043 -0.1453 -0.0094 -0.0826 354 HOH   B O   
7020 O  O   . HOH   H .   ? 0.4516 0.4144 0.5414 -0.1311 0.1234  0.0878  355 HOH   B O   
7021 O  O   . HOH   H .   ? 0.5633 0.3867 0.4048 0.0536  0.1448  -0.0319 356 HOH   B O   
7022 O  O   . HOH   H .   ? 0.3567 0.2867 0.3802 -0.1019 0.0000  -0.0556 357 HOH   B O   
7023 O  O   . HOH   H .   ? 0.4715 0.5704 0.4592 0.1611  -0.0932 0.1674  358 HOH   B O   
7024 O  O   . HOH   H .   ? 0.5614 0.3766 0.5024 -0.0241 -0.1404 -0.0503 359 HOH   B O   
7025 O  O   . HOH   H .   ? 0.5455 0.4209 0.5799 0.0119  0.0589  0.1479  360 HOH   B O   
7026 O  O   . HOH   H .   ? 0.4901 0.6019 0.2885 0.2005  0.0041  0.0194  361 HOH   B O   
7027 O  O   . HOH   H .   ? 0.2319 0.4184 0.6824 -0.0881 -0.0641 -0.0907 362 HOH   B O   
7028 O  O   . HOH   H .   ? 0.4751 0.4356 0.5176 -0.0227 -0.0221 0.0133  363 HOH   B O   
7029 O  O   . HOH   H .   ? 0.6275 0.2412 0.3957 -0.0187 -0.0088 0.0774  364 HOH   B O   
7030 O  O   . HOH   H .   ? 0.5053 0.3140 0.5097 -0.1283 -0.0483 0.0220  365 HOH   B O   
7031 O  O   . HOH   H .   ? 0.6079 0.5060 0.4054 0.1537  0.0559  0.0894  366 HOH   B O   
7032 O  O   . HOH   H .   ? 0.5324 0.5352 0.4968 -0.0671 -0.0448 -0.1117 367 HOH   B O   
7033 O  O   . HOH   H .   ? 0.5440 0.5318 0.3556 0.1251  -0.1783 0.0572  368 HOH   B O   
7034 O  O   . HOH   H .   ? 0.5415 0.4509 0.5369 0.1673  -0.1308 0.0539  369 HOH   B O   
7035 O  O   . HOH   H .   ? 0.7501 0.7702 0.5404 0.2030  -0.1373 0.0873  370 HOH   B O   
7036 O  O   . HOH   H .   ? 0.4240 0.5812 0.4989 0.2682  0.1110  0.1298  371 HOH   B O   
7037 O  O   . HOH   H .   ? 0.3951 0.3481 0.3717 0.0686  -0.1272 -0.0252 372 HOH   B O   
7038 O  O   . HOH   H .   ? 0.5769 0.4009 0.3173 -0.0834 -0.0921 -0.0668 373 HOH   B O   
7039 O  O   . HOH   H .   ? 0.2490 0.4793 0.3975 0.0279  -0.0403 -0.0704 374 HOH   B O   
7040 O  O   . HOH   H .   ? 0.4920 0.7316 0.5987 0.1674  0.0453  0.2923  375 HOH   B O   
7041 O  O   . HOH   H .   ? 0.4576 0.4984 0.4633 -0.0789 -0.0162 0.0185  376 HOH   B O   
7042 O  O   . HOH   H .   ? 0.3666 0.5427 0.2202 -0.0574 0.0368  0.0073  377 HOH   B O   
7043 O  O   . HOH   H .   ? 0.5188 0.6605 0.4065 -0.1283 0.0002  -0.1505 378 HOH   B O   
7044 O  O   . HOH   H .   ? 0.7261 0.3814 0.4968 -0.1029 -0.0381 0.0033  379 HOH   B O   
7045 O  O   . HOH   H .   ? 0.3795 0.5333 0.5737 0.1323  -0.0133 0.0282  380 HOH   B O   
7046 O  O   . HOH   H .   ? 0.4732 0.8371 0.5377 0.0562  0.1951  0.0690  381 HOH   B O   
7047 O  O   . HOH   H .   ? 0.3254 0.2845 0.3203 0.0205  0.0420  0.0292  382 HOH   B O   
7048 O  O   . HOH   H .   ? 0.5038 0.6292 0.6142 -0.0153 0.1373  0.1977  383 HOH   B O   
7049 O  O   . HOH   H .   ? 0.7050 0.4325 0.3966 0.1215  0.0968  -0.0383 384 HOH   B O   
7050 O  O   . HOH   H .   ? 0.6088 0.4778 0.4266 0.0017  -0.0592 -0.0457 385 HOH   B O   
7051 O  O   . HOH   H .   ? 0.7213 0.5619 0.4394 0.2092  -0.0017 -0.0635 386 HOH   B O   
7052 O  O   . HOH   H .   ? 0.2547 0.4328 0.4398 -0.0792 -0.0986 -0.0263 387 HOH   B O   
7053 O  O   . HOH   H .   ? 0.5679 0.4757 0.5332 -0.0806 0.0520  -0.0112 388 HOH   B O   
7054 O  O   . HOH   H .   ? 0.4791 0.4164 0.3699 0.0360  0.0869  0.0060  389 HOH   B O   
7055 O  O   . HOH   H .   ? 0.4907 0.3034 0.4501 -0.1534 -0.0008 0.0392  390 HOH   B O   
7056 O  O   . HOH   H .   ? 0.4131 0.2534 0.3497 0.0951  -0.0396 0.0069  391 HOH   B O   
7057 O  O   . HOH   H .   ? 0.4507 0.2334 0.4631 -0.0451 0.0333  0.0559  392 HOH   B O   
7058 O  O   . HOH   H .   ? 0.5010 0.4523 0.4799 0.0460  0.0849  0.0493  393 HOH   B O   
7059 O  O   . HOH   H .   ? 0.2465 0.4363 0.6820 -0.1127 -0.0611 -0.0244 394 HOH   B O   
7060 O  O   . HOH   H .   ? 0.3798 0.5734 0.4424 0.0298  -0.0083 -0.1088 395 HOH   B O   
7061 O  O   . HOH   H .   ? 0.3271 0.3941 0.4185 0.0142  0.0237  -0.0689 396 HOH   B O   
7062 O  O   . HOH   H .   ? 0.4588 0.4837 0.5051 0.0371  0.1329  0.1101  397 HOH   B O   
7063 O  O   . HOH   H .   ? 0.2185 0.2723 0.6306 -0.0545 -0.0928 0.0274  398 HOH   B O   
7064 O  O   . HOH   H .   ? 0.5515 0.4435 0.3068 -0.2228 -0.0416 0.1065  399 HOH   B O   
7065 O  O   . HOH   H .   ? 0.5674 0.5752 0.5993 0.0636  -0.1195 0.2099  400 HOH   B O   
7066 O  O   . HOH   H .   ? 0.5660 0.5590 0.3600 0.1539  0.0068  -0.0453 401 HOH   B O   
# 
