data_7HFL
# 
_entry.id   7HFL 
# 
_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   7HFL         pdb_00007hfl 10.2210/pdb7hfl/pdb 
WWPDB D_1001407411 ?            ?                   
# 
_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                        7HFL 
_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 '4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}thian-4-ol' 264.347   1   ?                      ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                 35.453    1   ?                      ? ? ? 
4 water       nat water                                                          18.015    416 ?                      ? ? ? 
# 
_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 '4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}thian-4-ol' A1BBM 
3 'CHLORIDE ION'                                                 CL    
4 water                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BBM non-polymer         . '4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}thian-4-ol' ? 'C12 H16 N4 O S' 264.347 
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 
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 A1BBM 1   201 201  A1BBM LA1 A . 
D 3 CL    1   202 1    CL    CL  A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 209  HOH   HOH A . 
E 4 HOH   3   303 153  HOH   HOH A . 
E 4 HOH   4   304 229  HOH   HOH A . 
E 4 HOH   5   305 1289 HOH   HOH A . 
E 4 HOH   6   306 196  HOH   HOH A . 
E 4 HOH   7   307 661  HOH   HOH A . 
E 4 HOH   8   308 93   HOH   HOH A . 
E 4 HOH   9   309 625  HOH   HOH A . 
E 4 HOH   10  310 109  HOH   HOH A . 
E 4 HOH   11  311 493  HOH   HOH A . 
E 4 HOH   12  312 247  HOH   HOH A . 
E 4 HOH   13  313 1295 HOH   HOH A . 
E 4 HOH   14  314 36   HOH   HOH A . 
E 4 HOH   15  315 320  HOH   HOH A . 
E 4 HOH   16  316 124  HOH   HOH A . 
E 4 HOH   17  317 76   HOH   HOH A . 
E 4 HOH   18  318 85   HOH   HOH A . 
E 4 HOH   19  319 199  HOH   HOH A . 
E 4 HOH   20  320 337  HOH   HOH A . 
E 4 HOH   21  321 405  HOH   HOH A . 
E 4 HOH   22  322 409  HOH   HOH A . 
E 4 HOH   23  323 136  HOH   HOH A . 
E 4 HOH   24  324 1310 HOH   HOH A . 
E 4 HOH   25  325 151  HOH   HOH A . 
E 4 HOH   26  326 662  HOH   HOH A . 
E 4 HOH   27  327 86   HOH   HOH A . 
E 4 HOH   28  328 393  HOH   HOH A . 
E 4 HOH   29  329 70   HOH   HOH A . 
E 4 HOH   30  330 1301 HOH   HOH A . 
E 4 HOH   31  331 192  HOH   HOH A . 
E 4 HOH   32  332 15   HOH   HOH A . 
E 4 HOH   33  333 225  HOH   HOH A . 
E 4 HOH   34  334 1290 HOH   HOH A . 
E 4 HOH   35  335 164  HOH   HOH A . 
E 4 HOH   36  336 469  HOH   HOH A . 
E 4 HOH   37  337 236  HOH   HOH A . 
E 4 HOH   38  338 241  HOH   HOH A . 
E 4 HOH   39  339 630  HOH   HOH A . 
E 4 HOH   40  340 18   HOH   HOH A . 
E 4 HOH   41  341 140  HOH   HOH A . 
E 4 HOH   42  342 964  HOH   HOH A . 
E 4 HOH   43  343 105  HOH   HOH A . 
E 4 HOH   44  344 49   HOH   HOH A . 
E 4 HOH   45  345 17   HOH   HOH A . 
E 4 HOH   46  346 33   HOH   HOH A . 
E 4 HOH   47  347 102  HOH   HOH A . 
E 4 HOH   48  348 1283 HOH   HOH A . 
E 4 HOH   49  349 57   HOH   HOH A . 
E 4 HOH   50  350 1300 HOH   HOH A . 
E 4 HOH   51  351 42   HOH   HOH A . 
E 4 HOH   52  352 21   HOH   HOH A . 
E 4 HOH   53  353 92   HOH   HOH A . 
E 4 HOH   54  354 139  HOH   HOH A . 
E 4 HOH   55  355 396  HOH   HOH A . 
E 4 HOH   56  356 169  HOH   HOH A . 
E 4 HOH   57  357 165  HOH   HOH A . 
E 4 HOH   58  358 66   HOH   HOH A . 
E 4 HOH   59  359 2    HOH   HOH A . 
E 4 HOH   60  360 354  HOH   HOH A . 
E 4 HOH   61  361 8    HOH   HOH A . 
E 4 HOH   62  362 162  HOH   HOH A . 
E 4 HOH   63  363 45   HOH   HOH A . 
E 4 HOH   64  364 132  HOH   HOH A . 
E 4 HOH   65  365 26   HOH   HOH A . 
E 4 HOH   66  366 5    HOH   HOH A . 
E 4 HOH   67  367 19   HOH   HOH A . 
E 4 HOH   68  368 155  HOH   HOH A . 
E 4 HOH   69  369 81   HOH   HOH A . 
E 4 HOH   70  370 218  HOH   HOH A . 
E 4 HOH   71  371 56   HOH   HOH A . 
E 4 HOH   72  372 939  HOH   HOH A . 
E 4 HOH   73  373 461  HOH   HOH A . 
E 4 HOH   74  374 1275 HOH   HOH A . 
E 4 HOH   75  375 138  HOH   HOH A . 
E 4 HOH   76  376 46   HOH   HOH A . 
E 4 HOH   77  377 366  HOH   HOH A . 
E 4 HOH   78  378 1309 HOH   HOH A . 
E 4 HOH   79  379 4    HOH   HOH A . 
E 4 HOH   80  380 35   HOH   HOH A . 
E 4 HOH   81  381 159  HOH   HOH A . 
E 4 HOH   82  382 96   HOH   HOH A . 
E 4 HOH   83  383 1296 HOH   HOH A . 
E 4 HOH   84  384 27   HOH   HOH A . 
E 4 HOH   85  385 154  HOH   HOH A . 
E 4 HOH   86  386 39   HOH   HOH A . 
E 4 HOH   87  387 134  HOH   HOH A . 
E 4 HOH   88  388 83   HOH   HOH A . 
E 4 HOH   89  389 74   HOH   HOH A . 
E 4 HOH   90  390 186  HOH   HOH A . 
E 4 HOH   91  391 78   HOH   HOH A . 
E 4 HOH   92  392 148  HOH   HOH A . 
E 4 HOH   93  393 278  HOH   HOH A . 
E 4 HOH   94  394 12   HOH   HOH A . 
E 4 HOH   95  395 3    HOH   HOH A . 
E 4 HOH   96  396 6    HOH   HOH A . 
E 4 HOH   97  397 25   HOH   HOH A . 
E 4 HOH   98  398 116  HOH   HOH A . 
E 4 HOH   99  399 1313 HOH   HOH A . 
E 4 HOH   100 400 24   HOH   HOH A . 
E 4 HOH   101 401 2    HOH   HOH A . 
E 4 HOH   102 402 351  HOH   HOH A . 
E 4 HOH   103 403 34   HOH   HOH A . 
E 4 HOH   104 404 67   HOH   HOH A . 
E 4 HOH   105 405 58   HOH   HOH A . 
E 4 HOH   106 406 121  HOH   HOH A . 
E 4 HOH   107 407 303  HOH   HOH A . 
E 4 HOH   108 408 195  HOH   HOH A . 
E 4 HOH   109 409 1308 HOH   HOH A . 
E 4 HOH   110 410 296  HOH   HOH A . 
E 4 HOH   111 411 6    HOH   HOH A . 
E 4 HOH   112 412 1315 HOH   HOH A . 
E 4 HOH   113 413 123  HOH   HOH A . 
E 4 HOH   114 414 397  HOH   HOH A . 
E 4 HOH   115 415 7    HOH   HOH A . 
E 4 HOH   116 416 125  HOH   HOH A . 
E 4 HOH   117 417 8    HOH   HOH A . 
E 4 HOH   118 418 68   HOH   HOH A . 
E 4 HOH   119 419 281  HOH   HOH A . 
E 4 HOH   120 420 1222 HOH   HOH A . 
E 4 HOH   121 421 53   HOH   HOH A . 
E 4 HOH   122 422 381  HOH   HOH A . 
E 4 HOH   123 423 51   HOH   HOH A . 
E 4 HOH   124 424 122  HOH   HOH A . 
E 4 HOH   125 425 1068 HOH   HOH A . 
E 4 HOH   126 426 95   HOH   HOH A . 
E 4 HOH   127 427 333  HOH   HOH A . 
E 4 HOH   128 428 156  HOH   HOH A . 
E 4 HOH   129 429 1286 HOH   HOH A . 
E 4 HOH   130 430 115  HOH   HOH A . 
E 4 HOH   131 431 1279 HOH   HOH A . 
E 4 HOH   132 432 582  HOH   HOH A . 
E 4 HOH   133 433 16   HOH   HOH A . 
E 4 HOH   134 434 212  HOH   HOH A . 
E 4 HOH   135 435 188  HOH   HOH A . 
E 4 HOH   136 436 71   HOH   HOH A . 
E 4 HOH   137 437 1238 HOH   HOH A . 
E 4 HOH   138 438 80   HOH   HOH A . 
E 4 HOH   139 439 73   HOH   HOH A . 
E 4 HOH   140 440 10   HOH   HOH A . 
E 4 HOH   141 441 94   HOH   HOH A . 
E 4 HOH   142 442 1189 HOH   HOH A . 
E 4 HOH   143 443 104  HOH   HOH A . 
E 4 HOH   144 444 97   HOH   HOH A . 
E 4 HOH   145 445 40   HOH   HOH A . 
E 4 HOH   146 446 1094 HOH   HOH A . 
E 4 HOH   147 447 944  HOH   HOH A . 
E 4 HOH   148 448 952  HOH   HOH A . 
E 4 HOH   149 449 11   HOH   HOH A . 
E 4 HOH   150 450 5    HOH   HOH A . 
E 4 HOH   151 451 79   HOH   HOH A . 
E 4 HOH   152 452 576  HOH   HOH A . 
E 4 HOH   153 453 330  HOH   HOH A . 
E 4 HOH   154 454 1134 HOH   HOH A . 
E 4 HOH   155 455 163  HOH   HOH A . 
E 4 HOH   156 456 509  HOH   HOH A . 
E 4 HOH   157 457 107  HOH   HOH A . 
E 4 HOH   158 458 1119 HOH   HOH A . 
E 4 HOH   159 459 408  HOH   HOH A . 
E 4 HOH   160 460 726  HOH   HOH A . 
E 4 HOH   161 461 1276 HOH   HOH A . 
E 4 HOH   162 462 756  HOH   HOH A . 
E 4 HOH   163 463 280  HOH   HOH A . 
E 4 HOH   164 464 126  HOH   HOH A . 
E 4 HOH   165 465 319  HOH   HOH A . 
E 4 HOH   166 466 556  HOH   HOH A . 
E 4 HOH   167 467 361  HOH   HOH A . 
E 4 HOH   168 468 63   HOH   HOH A . 
E 4 HOH   169 469 1307 HOH   HOH A . 
E 4 HOH   170 470 250  HOH   HOH A . 
E 4 HOH   171 471 801  HOH   HOH A . 
E 4 HOH   172 472 342  HOH   HOH A . 
E 4 HOH   173 473 1287 HOH   HOH A . 
E 4 HOH   174 474 202  HOH   HOH A . 
E 4 HOH   175 475 1306 HOH   HOH A . 
E 4 HOH   176 476 135  HOH   HOH A . 
E 4 HOH   177 477 370  HOH   HOH A . 
E 4 HOH   178 478 674  HOH   HOH A . 
E 4 HOH   179 479 695  HOH   HOH A . 
E 4 HOH   180 480 919  HOH   HOH A . 
E 4 HOH   181 481 224  HOH   HOH A . 
E 4 HOH   182 482 7    HOH   HOH A . 
E 4 HOH   183 483 318  HOH   HOH A . 
E 4 HOH   184 484 315  HOH   HOH A . 
E 4 HOH   185 485 309  HOH   HOH A . 
E 4 HOH   186 486 805  HOH   HOH A . 
E 4 HOH   187 487 267  HOH   HOH A . 
E 4 HOH   188 488 1299 HOH   HOH A . 
E 4 HOH   189 489 331  HOH   HOH A . 
E 4 HOH   190 490 521  HOH   HOH A . 
E 4 HOH   191 491 152  HOH   HOH A . 
E 4 HOH   192 492 711  HOH   HOH A . 
E 4 HOH   193 493 1    HOH   HOH A . 
E 4 HOH   194 494 981  HOH   HOH A . 
E 4 HOH   195 495 941  HOH   HOH A . 
E 4 HOH   196 496 263  HOH   HOH A . 
E 4 HOH   197 497 1314 HOH   HOH A . 
E 4 HOH   198 498 1284 HOH   HOH A . 
E 4 HOH   199 499 326  HOH   HOH A . 
E 4 HOH   200 500 208  HOH   HOH A . 
E 4 HOH   201 501 1071 HOH   HOH A . 
E 4 HOH   202 502 356  HOH   HOH A . 
E 4 HOH   203 503 350  HOH   HOH A . 
E 4 HOH   204 504 180  HOH   HOH A . 
E 4 HOH   205 505 363  HOH   HOH A . 
E 4 HOH   206 506 371  HOH   HOH A . 
E 4 HOH   207 507 313  HOH   HOH A . 
E 4 HOH   208 508 4    HOH   HOH A . 
E 4 HOH   209 509 429  HOH   HOH A . 
E 4 HOH   210 510 185  HOH   HOH A . 
E 4 HOH   211 511 772  HOH   HOH A . 
E 4 HOH   212 512 376  HOH   HOH A . 
E 4 HOH   213 513 1074 HOH   HOH A . 
E 4 HOH   214 514 346  HOH   HOH A . 
E 4 HOH   215 515 1292 HOH   HOH A . 
E 4 HOH   216 516 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 240  HOH   HOH B . 
F 4 HOH   3   203 549  HOH   HOH B . 
F 4 HOH   4   204 398  HOH   HOH B . 
F 4 HOH   5   205 232  HOH   HOH B . 
F 4 HOH   6   206 1249 HOH   HOH B . 
F 4 HOH   7   207 758  HOH   HOH B . 
F 4 HOH   8   208 364  HOH   HOH B . 
F 4 HOH   9   209 358  HOH   HOH B . 
F 4 HOH   10  210 120  HOH   HOH B . 
F 4 HOH   11  211 264  HOH   HOH B . 
F 4 HOH   12  212 531  HOH   HOH B . 
F 4 HOH   13  213 353  HOH   HOH B . 
F 4 HOH   14  214 900  HOH   HOH B . 
F 4 HOH   15  215 50   HOH   HOH B . 
F 4 HOH   16  216 452  HOH   HOH B . 
F 4 HOH   17  217 343  HOH   HOH B . 
F 4 HOH   18  218 131  HOH   HOH B . 
F 4 HOH   19  219 332  HOH   HOH B . 
F 4 HOH   20  220 743  HOH   HOH B . 
F 4 HOH   21  221 1312 HOH   HOH B . 
F 4 HOH   22  222 82   HOH   HOH B . 
F 4 HOH   23  223 205  HOH   HOH B . 
F 4 HOH   24  224 166  HOH   HOH B . 
F 4 HOH   25  225 75   HOH   HOH B . 
F 4 HOH   26  226 444  HOH   HOH B . 
F 4 HOH   27  227 1140 HOH   HOH B . 
F 4 HOH   28  228 654  HOH   HOH B . 
F 4 HOH   29  229 128  HOH   HOH B . 
F 4 HOH   30  230 54   HOH   HOH B . 
F 4 HOH   31  231 69   HOH   HOH B . 
F 4 HOH   32  232 300  HOH   HOH B . 
F 4 HOH   33  233 127  HOH   HOH B . 
F 4 HOH   34  234 1278 HOH   HOH B . 
F 4 HOH   35  235 723  HOH   HOH B . 
F 4 HOH   36  236 272  HOH   HOH B . 
F 4 HOH   37  237 60   HOH   HOH B . 
F 4 HOH   38  238 1    HOH   HOH B . 
F 4 HOH   39  239 129  HOH   HOH B . 
F 4 HOH   40  240 110  HOH   HOH B . 
F 4 HOH   41  241 9    HOH   HOH B . 
F 4 HOH   42  242 325  HOH   HOH B . 
F 4 HOH   43  243 172  HOH   HOH B . 
F 4 HOH   44  244 143  HOH   HOH B . 
F 4 HOH   45  245 276  HOH   HOH B . 
F 4 HOH   46  246 52   HOH   HOH B . 
F 4 HOH   47  247 181  HOH   HOH B . 
F 4 HOH   48  248 231  HOH   HOH B . 
F 4 HOH   49  249 30   HOH   HOH B . 
F 4 HOH   50  250 150  HOH   HOH B . 
F 4 HOH   51  251 14   HOH   HOH B . 
F 4 HOH   52  252 133  HOH   HOH B . 
F 4 HOH   53  253 271  HOH   HOH B . 
F 4 HOH   54  254 416  HOH   HOH B . 
F 4 HOH   55  255 41   HOH   HOH B . 
F 4 HOH   56  256 31   HOH   HOH B . 
F 4 HOH   57  257 243  HOH   HOH B . 
F 4 HOH   58  258 144  HOH   HOH B . 
F 4 HOH   59  259 72   HOH   HOH B . 
F 4 HOH   60  260 347  HOH   HOH B . 
F 4 HOH   61  261 1277 HOH   HOH B . 
F 4 HOH   62  262 287  HOH   HOH B . 
F 4 HOH   63  263 62   HOH   HOH B . 
F 4 HOH   64  264 10   HOH   HOH B . 
F 4 HOH   65  265 282  HOH   HOH B . 
F 4 HOH   66  266 47   HOH   HOH B . 
F 4 HOH   67  267 59   HOH   HOH B . 
F 4 HOH   68  268 84   HOH   HOH B . 
F 4 HOH   69  269 117  HOH   HOH B . 
F 4 HOH   70  270 103  HOH   HOH B . 
F 4 HOH   71  271 61   HOH   HOH B . 
F 4 HOH   72  272 1106 HOH   HOH B . 
F 4 HOH   73  273 391  HOH   HOH B . 
F 4 HOH   74  274 20   HOH   HOH B . 
F 4 HOH   75  275 11   HOH   HOH B . 
F 4 HOH   76  276 175  HOH   HOH B . 
F 4 HOH   77  277 77   HOH   HOH B . 
F 4 HOH   78  278 242  HOH   HOH B . 
F 4 HOH   79  279 302  HOH   HOH B . 
F 4 HOH   80  280 1305 HOH   HOH B . 
F 4 HOH   81  281 147  HOH   HOH B . 
F 4 HOH   82  282 43   HOH   HOH B . 
F 4 HOH   83  283 22   HOH   HOH B . 
F 4 HOH   84  284 221  HOH   HOH B . 
F 4 HOH   85  285 235  HOH   HOH B . 
F 4 HOH   86  286 13   HOH   HOH B . 
F 4 HOH   87  287 114  HOH   HOH B . 
F 4 HOH   88  288 88   HOH   HOH B . 
F 4 HOH   89  289 216  HOH   HOH B . 
F 4 HOH   90  290 341  HOH   HOH B . 
F 4 HOH   91  291 106  HOH   HOH B . 
F 4 HOH   92  292 297  HOH   HOH B . 
F 4 HOH   93  293 1066 HOH   HOH B . 
F 4 HOH   94  294 387  HOH   HOH B . 
F 4 HOH   95  295 252  HOH   HOH B . 
F 4 HOH   96  296 89   HOH   HOH B . 
F 4 HOH   97  297 99   HOH   HOH B . 
F 4 HOH   98  298 137  HOH   HOH B . 
F 4 HOH   99  299 311  HOH   HOH B . 
F 4 HOH   100 300 118  HOH   HOH B . 
F 4 HOH   101 301 112  HOH   HOH B . 
F 4 HOH   102 302 32   HOH   HOH B . 
F 4 HOH   103 303 160  HOH   HOH B . 
F 4 HOH   104 304 316  HOH   HOH B . 
F 4 HOH   105 305 1285 HOH   HOH B . 
F 4 HOH   106 306 299  HOH   HOH B . 
F 4 HOH   107 307 220  HOH   HOH B . 
F 4 HOH   108 308 101  HOH   HOH B . 
F 4 HOH   109 309 38   HOH   HOH B . 
F 4 HOH   110 310 142  HOH   HOH B . 
F 4 HOH   111 311 37   HOH   HOH B . 
F 4 HOH   112 312 48   HOH   HOH B . 
F 4 HOH   113 313 1291 HOH   HOH B . 
F 4 HOH   114 314 215  HOH   HOH B . 
F 4 HOH   115 315 170  HOH   HOH B . 
F 4 HOH   116 316 445  HOH   HOH B . 
F 4 HOH   117 317 91   HOH   HOH B . 
F 4 HOH   118 318 177  HOH   HOH B . 
F 4 HOH   119 319 23   HOH   HOH B . 
F 4 HOH   120 320 635  HOH   HOH B . 
F 4 HOH   121 321 28   HOH   HOH B . 
F 4 HOH   122 322 44   HOH   HOH B . 
F 4 HOH   123 323 161  HOH   HOH B . 
F 4 HOH   124 324 197  HOH   HOH B . 
F 4 HOH   125 325 100  HOH   HOH B . 
F 4 HOH   126 326 704  HOH   HOH B . 
F 4 HOH   127 327 55   HOH   HOH B . 
F 4 HOH   128 328 717  HOH   HOH B . 
F 4 HOH   129 329 1294 HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 1274 HOH   HOH B . 
F 4 HOH   132 332 98   HOH   HOH B . 
F 4 HOH   133 333 141  HOH   HOH B . 
F 4 HOH   134 334 1126 HOH   HOH B . 
F 4 HOH   135 335 234  HOH   HOH B . 
F 4 HOH   136 336 65   HOH   HOH B . 
F 4 HOH   137 337 207  HOH   HOH B . 
F 4 HOH   138 338 182  HOH   HOH B . 
F 4 HOH   139 339 1293 HOH   HOH B . 
F 4 HOH   140 340 960  HOH   HOH B . 
F 4 HOH   141 341 334  HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 339  HOH   HOH B . 
F 4 HOH   146 346 87   HOH   HOH B . 
F 4 HOH   147 347 90   HOH   HOH B . 
F 4 HOH   148 348 463  HOH   HOH B . 
F 4 HOH   149 349 623  HOH   HOH B . 
F 4 HOH   150 350 1304 HOH   HOH B . 
F 4 HOH   151 351 1046 HOH   HOH B . 
F 4 HOH   152 352 335  HOH   HOH B . 
F 4 HOH   153 353 191  HOH   HOH B . 
F 4 HOH   154 354 1280 HOH   HOH B . 
F 4 HOH   155 355 304  HOH   HOH B . 
F 4 HOH   156 356 203  HOH   HOH B . 
F 4 HOH   157 357 1077 HOH   HOH B . 
F 4 HOH   158 358 479  HOH   HOH B . 
F 4 HOH   159 359 290  HOH   HOH B . 
F 4 HOH   160 360 541  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 291  HOH   HOH B . 
F 4 HOH   166 366 373  HOH   HOH B . 
F 4 HOH   167 367 1316 HOH   HOH B . 
F 4 HOH   168 368 615  HOH   HOH B . 
F 4 HOH   169 369 340  HOH   HOH B . 
F 4 HOH   170 370 898  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 1303 HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 190  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 1163 HOH   HOH B . 
F 4 HOH   178 378 1000 HOH   HOH B . 
F 4 HOH   179 379 183  HOH   HOH B . 
F 4 HOH   180 380 418  HOH   HOH B . 
F 4 HOH   181 381 1173 HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 1298 HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 470  HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 410  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 274  HOH   HOH B . 
F 4 HOH   195 395 314  HOH   HOH B . 
F 4 HOH   196 396 157  HOH   HOH B . 
F 4 HOH   197 397 566  HOH   HOH B . 
F 4 HOH   198 398 792  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFL 
_cell.length_a           88.753 
_cell.length_b           88.753 
_cell.length_c           39.503 
_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                         7HFL 
_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          7HFL 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.61 
_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   2023-10-07 
_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                     7HFL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165627 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.070 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        9.500 
_reflns.B_iso_Wilson_estimate        12.400 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.076 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1052397 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 36473 7787 ? 2.135 ? ? ? 4.700 ? 0.400  ? ? ? ? ? ? 95.200 2.401 1.076 0.355 
1 2 5.480 44.380 ? 7469  1095 ? 0.043 ? ? ? 6.800 ? 31.700 ? ? ? ? ? ? 99.900 0.047 0.018 0.998 
# 
_refine.entry_id                                 7HFL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4100 
_refine.ls_number_reflns_obs                     164963 
_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                          0.1463 
_refine.ls_R_factor_R_work                       0.1456 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1593 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7948 
_refine.ls_number_reflns_R_work                  157015 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.6901 
_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                            0.1400 
_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                                78.430 
_refine.B_iso_min                                9.070 
_refine.pdbx_overall_phase_error                 18.6300 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             416 
_refine_hist.number_atoms_total               2993 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.81 
_refine_hist.pdbx_B_iso_mean_solvent          31.76 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 85.0000  4468 . 0.4673 0.4487 . 229 0.0000 4697 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 99.0000  5191 . 0.4084 0.4433 . 225 0.0000 5416 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5258 . 0.3628 0.3524 . 258 0.0000 5516 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5195 . 0.3106 0.3109 . 272 0.0000 5467 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5171 . 0.2777 0.2965 . 330 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5250 . 0.2823 0.2959 . 244 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5239 . 0.2497 0.2633 . 270 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5239 . 0.2223 0.2308 . 241 0.0000 5480 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5213 . 0.1993 0.2005 . 278 0.0000 5491 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5271 . 0.1799 0.1863 . 247 0.0000 5518 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5268 . 0.1642 0.1800 . 260 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5249 . 0.1472 0.1755 . 266 0.0000 5515 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5169 . 0.1366 0.1762 . 291 0.0000 5460 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5335 . 0.1290 0.1601 . 235 0.0000 5570 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5184 . 0.1307 0.1469 . 255 0.0000 5439 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5272 . 0.1294 0.1524 . 280 0.0000 5552 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5236 . 0.1293 0.1415 . 281 0.0000 5517 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5229 . 0.1336 0.1500 . 278 0.0000 5507 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5283 . 0.1349 0.1770 . 248 0.0000 5531 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5234 . 0.1276 0.1591 . 262 0.0000 5496 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5301 . 0.1189 0.1206 . 255 0.0000 5556 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5221 . 0.1128 0.1220 . 276 0.0000 5497 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5291 . 0.1165 0.1289 . 263 0.0000 5554 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5300 . 0.1224 0.1452 . 268 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5276 . 0.1299 0.1358 . 250 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5274 . 0.1275 0.1255 . 281 0.0000 5555 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5286 . 0.1332 0.1384 . 288 0.0000 5574 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5298 . 0.1310 0.1427 . 291 0.0000 5589 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5333 . 0.1447 0.1608 . 256 0.0000 5589 . 'X-RAY DIFFRACTION' 
3.1100 44.3800 30 100.0000 5481 . 0.1472 0.1668 . 270 0.0000 5751 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFL 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004319' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFL 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HFL A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFL 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 7HFL SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFL MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFL SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFL MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   H 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLY 
_pdbx_validate_close_contact.auth_seq_id_1    8 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    307 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.58 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.00 -133.15 
2 1 SER A 128 ? B 72.77 -11.42  
3 1 HIS B 86  ? ? 56.96 -127.24 
# 
_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 ? 5.94 . 
2 1 O ? A HOH 515 ? 6.01 . 
3 1 O ? A HOH 516 ? 7.61 . 
4 1 O ? B HOH 400 ? 6.32 . 
# 
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 
A1BBM N2   N  Y N 1   
A1BBM C3   C  Y N 2   
A1BBM C6   C  Y N 3   
A1BBM C9   C  N N 4   
A1BBM C12  C  N N 5   
A1BBM C1   C  N N 6   
A1BBM C10  C  N N 7   
A1BBM C11  C  N N 8   
A1BBM C2   C  N N 9   
A1BBM C4   C  Y N 10  
A1BBM C5   C  Y N 11  
A1BBM C7   C  Y N 12  
A1BBM C8   C  Y N 13  
A1BBM N1   N  N N 14  
A1BBM N3   N  Y N 15  
A1BBM N4   N  Y N 16  
A1BBM O1   O  N N 17  
A1BBM S1   S  N N 18  
A1BBM H10  H  N N 19  
A1BBM H9   H  N N 20  
A1BBM H16  H  N N 21  
A1BBM H15  H  N N 22  
A1BBM H12  H  N N 23  
A1BBM H11  H  N N 24  
A1BBM H13  H  N N 25  
A1BBM H14  H  N N 26  
A1BBM H2   H  N N 27  
A1BBM H3   H  N N 28  
A1BBM H5   H  N N 29  
A1BBM H6   H  N N 30  
A1BBM H7   H  N N 31  
A1BBM H4   H  N N 32  
A1BBM H8   H  N N 33  
A1BBM H1   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HIS   N    N  N N 172 
HIS   CA   C  N S 173 
HIS   C    C  N N 174 
HIS   O    O  N N 175 
HIS   CB   C  N N 176 
HIS   CG   C  Y N 177 
HIS   ND1  N  Y N 178 
HIS   CD2  C  Y N 179 
HIS   CE1  C  Y N 180 
HIS   NE2  N  Y N 181 
HIS   OXT  O  N N 182 
HIS   H    H  N N 183 
HIS   H2   H  N N 184 
HIS   HA   H  N N 185 
HIS   HB2  H  N N 186 
HIS   HB3  H  N N 187 
HIS   HD1  H  N N 188 
HIS   HD2  H  N N 189 
HIS   HE1  H  N N 190 
HIS   HE2  H  N N 191 
HIS   HXT  H  N N 192 
HOH   O    O  N N 193 
HOH   H1   H  N N 194 
HOH   H2   H  N N 195 
ILE   N    N  N N 196 
ILE   CA   C  N S 197 
ILE   C    C  N N 198 
ILE   O    O  N N 199 
ILE   CB   C  N S 200 
ILE   CG1  C  N N 201 
ILE   CG2  C  N N 202 
ILE   CD1  C  N N 203 
ILE   OXT  O  N N 204 
ILE   H    H  N N 205 
ILE   H2   H  N N 206 
ILE   HA   H  N N 207 
ILE   HB   H  N N 208 
ILE   HG12 H  N N 209 
ILE   HG13 H  N N 210 
ILE   HG21 H  N N 211 
ILE   HG22 H  N N 212 
ILE   HG23 H  N N 213 
ILE   HD11 H  N N 214 
ILE   HD12 H  N N 215 
ILE   HD13 H  N N 216 
ILE   HXT  H  N N 217 
LEU   N    N  N N 218 
LEU   CA   C  N S 219 
LEU   C    C  N N 220 
LEU   O    O  N N 221 
LEU   CB   C  N N 222 
LEU   CG   C  N N 223 
LEU   CD1  C  N N 224 
LEU   CD2  C  N N 225 
LEU   OXT  O  N N 226 
LEU   H    H  N N 227 
LEU   H2   H  N N 228 
LEU   HA   H  N N 229 
LEU   HB2  H  N N 230 
LEU   HB3  H  N N 231 
LEU   HG   H  N N 232 
LEU   HD11 H  N N 233 
LEU   HD12 H  N N 234 
LEU   HD13 H  N N 235 
LEU   HD21 H  N N 236 
LEU   HD22 H  N N 237 
LEU   HD23 H  N N 238 
LEU   HXT  H  N N 239 
LYS   N    N  N N 240 
LYS   CA   C  N S 241 
LYS   C    C  N N 242 
LYS   O    O  N N 243 
LYS   CB   C  N N 244 
LYS   CG   C  N N 245 
LYS   CD   C  N N 246 
LYS   CE   C  N N 247 
LYS   NZ   N  N N 248 
LYS   OXT  O  N N 249 
LYS   H    H  N N 250 
LYS   H2   H  N N 251 
LYS   HA   H  N N 252 
LYS   HB2  H  N N 253 
LYS   HB3  H  N N 254 
LYS   HG2  H  N N 255 
LYS   HG3  H  N N 256 
LYS   HD2  H  N N 257 
LYS   HD3  H  N N 258 
LYS   HE2  H  N N 259 
LYS   HE3  H  N N 260 
LYS   HZ1  H  N N 261 
LYS   HZ2  H  N N 262 
LYS   HZ3  H  N N 263 
LYS   HXT  H  N N 264 
MET   N    N  N N 265 
MET   CA   C  N S 266 
MET   C    C  N N 267 
MET   O    O  N N 268 
MET   CB   C  N N 269 
MET   CG   C  N N 270 
MET   SD   S  N N 271 
MET   CE   C  N N 272 
MET   OXT  O  N N 273 
MET   H    H  N N 274 
MET   H2   H  N N 275 
MET   HA   H  N N 276 
MET   HB2  H  N N 277 
MET   HB3  H  N N 278 
MET   HG2  H  N N 279 
MET   HG3  H  N N 280 
MET   HE1  H  N N 281 
MET   HE2  H  N N 282 
MET   HE3  H  N N 283 
MET   HXT  H  N N 284 
PHE   N    N  N N 285 
PHE   CA   C  N S 286 
PHE   C    C  N N 287 
PHE   O    O  N N 288 
PHE   CB   C  N N 289 
PHE   CG   C  Y N 290 
PHE   CD1  C  Y N 291 
PHE   CD2  C  Y N 292 
PHE   CE1  C  Y N 293 
PHE   CE2  C  Y N 294 
PHE   CZ   C  Y N 295 
PHE   OXT  O  N N 296 
PHE   H    H  N N 297 
PHE   H2   H  N N 298 
PHE   HA   H  N N 299 
PHE   HB2  H  N N 300 
PHE   HB3  H  N N 301 
PHE   HD1  H  N N 302 
PHE   HD2  H  N N 303 
PHE   HE1  H  N N 304 
PHE   HE2  H  N N 305 
PHE   HZ   H  N N 306 
PHE   HXT  H  N N 307 
PRO   N    N  N N 308 
PRO   CA   C  N S 309 
PRO   C    C  N N 310 
PRO   O    O  N N 311 
PRO   CB   C  N N 312 
PRO   CG   C  N N 313 
PRO   CD   C  N N 314 
PRO   OXT  O  N N 315 
PRO   H    H  N N 316 
PRO   HA   H  N N 317 
PRO   HB2  H  N N 318 
PRO   HB3  H  N N 319 
PRO   HG2  H  N N 320 
PRO   HG3  H  N N 321 
PRO   HD2  H  N N 322 
PRO   HD3  H  N N 323 
PRO   HXT  H  N N 324 
SER   N    N  N N 325 
SER   CA   C  N S 326 
SER   C    C  N N 327 
SER   O    O  N N 328 
SER   CB   C  N N 329 
SER   OG   O  N N 330 
SER   OXT  O  N N 331 
SER   H    H  N N 332 
SER   H2   H  N N 333 
SER   HA   H  N N 334 
SER   HB2  H  N N 335 
SER   HB3  H  N N 336 
SER   HG   H  N N 337 
SER   HXT  H  N N 338 
THR   N    N  N N 339 
THR   CA   C  N S 340 
THR   C    C  N N 341 
THR   O    O  N N 342 
THR   CB   C  N R 343 
THR   OG1  O  N N 344 
THR   CG2  C  N N 345 
THR   OXT  O  N N 346 
THR   H    H  N N 347 
THR   H2   H  N N 348 
THR   HA   H  N N 349 
THR   HB   H  N N 350 
THR   HG1  H  N N 351 
THR   HG21 H  N N 352 
THR   HG22 H  N N 353 
THR   HG23 H  N N 354 
THR   HXT  H  N N 355 
TYR   N    N  N N 356 
TYR   CA   C  N S 357 
TYR   C    C  N N 358 
TYR   O    O  N N 359 
TYR   CB   C  N N 360 
TYR   CG   C  Y N 361 
TYR   CD1  C  Y N 362 
TYR   CD2  C  Y N 363 
TYR   CE1  C  Y N 364 
TYR   CE2  C  Y N 365 
TYR   CZ   C  Y N 366 
TYR   OH   O  N N 367 
TYR   OXT  O  N N 368 
TYR   H    H  N N 369 
TYR   H2   H  N N 370 
TYR   HA   H  N N 371 
TYR   HB2  H  N N 372 
TYR   HB3  H  N N 373 
TYR   HD1  H  N N 374 
TYR   HD2  H  N N 375 
TYR   HE1  H  N N 376 
TYR   HE2  H  N N 377 
TYR   HH   H  N N 378 
TYR   HXT  H  N N 379 
VAL   N    N  N N 380 
VAL   CA   C  N S 381 
VAL   C    C  N N 382 
VAL   O    O  N N 383 
VAL   CB   C  N N 384 
VAL   CG1  C  N N 385 
VAL   CG2  C  N N 386 
VAL   OXT  O  N N 387 
VAL   H    H  N N 388 
VAL   H2   H  N N 389 
VAL   HA   H  N N 390 
VAL   HB   H  N N 391 
VAL   HG11 H  N N 392 
VAL   HG12 H  N N 393 
VAL   HG13 H  N N 394 
VAL   HG21 H  N N 395 
VAL   HG22 H  N N 396 
VAL   HG23 H  N N 397 
VAL   HXT  H  N N 398 
# 
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 
A1BBM S1  C10  sing N N 1   
A1BBM S1  C11  sing N N 2   
A1BBM C9  C10  sing N N 3   
A1BBM C9  C1   sing N N 4   
A1BBM C12 C11  sing N N 5   
A1BBM C12 C1   sing N N 6   
A1BBM C2  C1   sing N N 7   
A1BBM C2  N1   sing N N 8   
A1BBM C1  O1   sing N N 9   
A1BBM N1  C3   sing N N 10  
A1BBM C3  C6   doub Y N 11  
A1BBM C3  N2   sing Y N 12  
A1BBM C7  C6   sing Y N 13  
A1BBM C7  C8   doub Y N 14  
A1BBM C6  C5   sing Y N 15  
A1BBM N2  C4   doub Y N 16  
A1BBM C8  N4   sing Y N 17  
A1BBM C5  N4   sing Y N 18  
A1BBM C5  N3   doub Y N 19  
A1BBM C4  N3   sing Y N 20  
A1BBM C9  H10  sing N N 21  
A1BBM C9  H9   sing N N 22  
A1BBM C12 H16  sing N N 23  
A1BBM C12 H15  sing N N 24  
A1BBM C10 H12  sing N N 25  
A1BBM C10 H11  sing N N 26  
A1BBM C11 H13  sing N N 27  
A1BBM C11 H14  sing N N 28  
A1BBM C2  H2   sing N N 29  
A1BBM C2  H3   sing N N 30  
A1BBM C4  H5   sing N N 31  
A1BBM C7  H6   sing N N 32  
A1BBM C8  H7   sing N N 33  
A1BBM N1  H4   sing N N 34  
A1BBM N4  H8   sing N N 35  
A1BBM O1  H1   sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7HFL 
_atom_sites.fract_transf_matrix[1][1]   0.011267 
_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]   0.011267 
_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]   0.025315 
_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 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.691 -16.195 22.248  0.68 61.72 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.598 -16.151 22.391  0.32 60.70 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.720 -15.124 22.432  0.68 61.27 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.646 -15.061 22.557  0.32 60.35 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.374 -13.771 22.164  0.68 59.48 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.318 -13.724 22.264  0.32 58.93 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.500 -13.522 22.595  0.68 60.02 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.406 -13.444 22.767  0.32 59.38 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.088 -15.177 23.838  0.68 62.19 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.024 -15.071 23.968  0.32 61.10 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.050 -14.074 24.001  0.68 62.47 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.007 -13.947 24.108  0.32 61.34 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.463 -16.543 24.089  0.68 62.48 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.380 -16.419 24.258  0.32 61.34 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.007 -15.238 21.788  0.68 73.52 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.925 -15.173 21.921  0.32 72.42 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.779 -15.039 24.503  0.68 74.63 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.722 -14.927 24.624  0.32 73.32 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.556 -14.227 24.822  0.68 74.96 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.509 -14.074 24.931  0.32 73.60 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.501 -13.217 24.042  0.68 74.96 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.474 -13.097 24.133  0.32 73.60 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.445 -14.096 23.243  0.68 74.96 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.403 -13.972 23.350  0.32 73.60 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.005 -16.528 24.944  0.68 74.98 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.925 -16.373 25.113  0.32 73.60 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.832 -16.736 23.378  0.68 74.98 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.744 -16.622 23.555  0.32 73.60 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.163 -17.214 24.101  0.68 74.98 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.070 -17.100 24.287  0.32 73.60 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.665 -12.904 21.443  1.00 56.66 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.134 -11.559 21.134  1.00 51.10 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 18.016 -10.558 21.408  1.00 45.60 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.898 -10.927 21.781  1.00 45.80 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.668 -11.444 19.697  1.00 50.60 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.668 -11.900 18.659  1.00 50.03 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.498 -11.522 18.698  1.00 49.90 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.129 -12.718 17.718  1.00 49.76 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.889 -13.082 21.115  0.68 67.99 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.928 -13.112 21.049  0.32 67.99 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.868 -11.346 21.724  1.00 61.31 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.892 -10.516 19.515  1.00 60.72 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.461 -11.995 19.611  1.00 60.72 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.604 -13.004 17.101  1.00 59.70 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.955 -12.962 17.726  1.00 59.70 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.293 -9.277  21.162  0.68 42.31 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.362 -9.278  21.278  0.32 42.76 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.380 -8.201  21.529  0.68 38.78 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.463 -8.179  21.599  0.32 39.71 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.520 -7.697  20.371  0.68 34.41 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.590 -7.768  20.422  0.32 35.98 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.920 -6.624  20.491  0.68 34.46 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.765 -6.860  20.569  0.32 35.97 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.152 -7.032  22.142  0.68 39.78 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.257 -6.975  22.124  0.32 40.41 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.125 -6.537  21.239  0.68 40.26 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.173 -6.498  21.154  0.32 40.75 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 19.009 -9.006  20.774  0.68 50.76 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 19.133 -9.019  20.997  0.32 51.31 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.782 -8.534  22.215  0.68 46.54 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.869 -8.462  22.307  0.32 47.65 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.527 -6.319  22.355  0.68 47.73 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.639 -6.263  22.353  0.32 48.49 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.593 -7.335  22.949  0.68 47.73 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.752 -7.245  22.918  0.32 48.49 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.541 -5.896  21.589  0.68 48.31 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.599 -5.840  21.461  0.32 48.89 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.441 -8.428  19.261  0.68 29.48 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.751 -8.404  19.265  0.32 32.15 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.540 -8.044  18.180  0.68 24.64 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.801 -8.217  18.179  0.32 28.44 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.102 -8.393  18.551  0.68 24.25 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.438 -8.726  18.619  0.32 27.18 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.838 -9.455  19.117  0.68 25.13 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 14.268 -9.922  18.875  0.32 27.43 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.929 -8.750  16.882  0.68 21.58 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 16.257 -8.999  16.950  0.32 26.36 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.196 -8.224  16.259  0.68 19.27 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.536 -8.499  16.345  0.32 24.57 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.196 -7.023  15.570  0.68 18.42 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.552 -7.350  15.574  0.32 23.81 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.379 -8.936  16.354  0.68 19.33 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.720 -9.192  16.530  0.32 24.00 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.355 -6.536  14.991  0.68 18.12 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.728 -6.894  15.009  0.32 23.45 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.542 -8.457  15.779  0.68 19.22 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.898 -8.744  15.969  0.32 23.46 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.531 -7.255  15.096  0.68 18.48 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.903 -7.593  15.206  0.32 23.21 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.896 -9.146  19.109  0.68 35.37 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 17.398 -8.944  19.087  0.32 38.57 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.590 -7.091  18.042  0.68 29.56 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.733 -7.276  17.954  0.32 34.13 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.060 -9.695  17.067  0.68 25.89 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 16.388 -9.926  17.204  0.32 31.63 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.211 -8.640  16.239  0.68 25.89 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.565 -8.939  16.275  0.32 31.63 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.404 -6.534  15.498  0.68 22.10 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.763 -6.877  15.440  0.32 28.56 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.391 -9.744  16.815  0.68 23.19 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.721 -9.969  17.042  0.32 28.79 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.340 -5.723  14.533  0.68 21.74 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.730 -6.119  14.496  0.32 28.14 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.332 -8.940  15.852  0.68 23.06 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.688 -9.218  16.103  0.32 28.15 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.309 -6.926  14.709  0.68 22.18 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.697 -7.289  14.827  0.32 27.84 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.166 -7.498  18.224  0.68 22.86 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.464 -7.824  18.700  0.32 25.85 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.787 -7.613  18.693  0.68 22.68 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 12.130 -8.175  19.157  0.32 24.66 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.804 -7.344  17.559  0.68 20.87 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 11.101 -7.679  18.155  0.32 22.64 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 11.030 -6.463  16.728  0.68 20.18 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 11.310 -6.678  17.463  0.32 22.56 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.542 -6.618  19.838  0.68 24.21 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.831 -7.585  20.541  0.32 25.59 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.216 -6.704  20.327  0.68 26.03 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 10.605 -8.082  21.047  0.32 26.42 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.308 -6.816  17.726  0.68 27.42 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.554 -6.997  18.481  0.32 31.01 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.626 -8.507  19.027  0.68 27.21 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 12.052 -9.139  19.215  0.32 29.58 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.154 -6.819  20.565  0.68 29.04 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 12.546 -7.829  21.150  0.32 30.70 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.707 -5.717  19.512  0.68 29.04 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 11.773 -6.620  20.469  0.32 30.70 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.104 -6.143  20.944  0.68 31.23 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.641 -8.919  21.118  0.32 31.70 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.708  -8.106  17.530  0.68 19.80 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 9.987  -8.400  18.077  0.32 20.95 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.632  -7.844  16.590  0.68 18.94 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.929  -8.050  17.157  0.32 19.61 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.829  -8.378  15.187  0.68 17.53 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 9.104  -8.573  15.752  0.32 18.16 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.118  -7.953  14.271  0.68 17.65 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.290  -8.240  14.884  0.32 18.02 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.569  -8.777  18.048  0.68 23.75 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.826  -9.099  18.550  0.32 25.13 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.812  -8.222  16.946  0.68 22.72 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 8.091  -8.393  17.494  0.32 23.52 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.506  -6.883  16.523  0.68 22.72 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.863  -7.083  17.108  0.32 23.52 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.768  -9.300  14.982  0.68 15.84 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.131 -9.379  15.496  0.32 16.93 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.032 -9.854  13.660  0.68 14.49 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.372 -9.875  14.150  0.32 15.71 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.161  -11.073 13.384  0.68 14.32 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.534  -11.115 13.858  0.32 15.03 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 8.871  -11.868 14.282  0.68 15.90 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 9.264  -11.939 14.738  0.32 15.38 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.506 -10.256 13.527  0.68 14.64 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.857 -10.187 13.946  0.32 15.39 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.437 -9.080  13.357  0.68 15.24 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.698 -8.947  13.749  0.32 14.69 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.772 -8.282  14.439  0.68 15.88 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 13.050 -8.147  14.826  0.32 15.01 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 12.958 -8.758  12.113  0.68 14.97 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.121 -8.564  12.482  0.32 14.30 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.607 -7.192  14.292  0.68 16.44 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.806 -7.004  14.652  0.32 15.16 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.791 -7.670  11.953  0.68 15.49 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.878 -7.421  12.297  0.32 14.70 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.113 -6.889  13.044  0.68 16.42 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.217 -6.645  13.387  0.32 15.07 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 14.941 -5.805  12.882  0.68 17.69 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 14.966 -5.505  13.210  0.32 16.00 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.263 -9.625  15.602  0.68 19.01 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.705 -9.648  16.081  0.32 20.31 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.837  -9.179  12.990  0.68 17.39 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 10.127 -9.186  13.512  0.32 18.85 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.772 -10.742 14.322  0.68 17.56 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 12.197 -10.665 14.719  0.32 18.47 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.592 -10.826 12.746  0.68 17.56 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.947 -10.735 13.152  0.32 18.47 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.422 -8.484  15.281  0.68 19.05 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.772 -8.385  15.681  0.32 18.01 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.735 -9.279  11.374  0.68 17.95 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.895 -9.084  11.745  0.32 17.16 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.823 -6.670  15.029  0.68 19.72 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 14.035 -6.479  15.383  0.32 18.19 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.137 -7.468  11.115  0.68 18.58 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.160 -7.177  11.443  0.32 17.64 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.066 -5.430  13.624  0.68 21.22 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 15.103 -5.129  13.948  0.32 19.19 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.748  -11.209 12.126  0.68 13.83 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 9.126  -11.233 12.597  0.32 14.26 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.174  -12.453 11.635  0.68 13.84 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.400  -12.394 12.101  0.32 14.44 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.309  -13.382 11.213  0.68 13.76 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.410  -13.385 11.533  0.32 13.86 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.300 -12.942 10.616  0.68 13.95 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.177 -13.042 10.625  0.32 13.99 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.274  -12.160 10.434  0.68 14.87 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.420  -11.951 11.015  0.32 14.81 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.619  -13.365 9.757   0.68 17.44 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.656  -13.032 10.247  0.32 15.59 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.576  -13.997 10.666  0.68 19.44 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.630  -13.713 11.134  0.32 16.39 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 6.007  -12.971 8.423   0.68 18.57 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 6.000  -12.423 9.016   0.32 16.54 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.790  -10.586 11.528  0.68 16.59 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 9.269  -10.637 11.993  0.32 17.11 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.640  -12.875 12.335  0.68 16.61 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.907  -12.815 12.824  0.32 17.32 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.553  -11.575 10.719  0.68 17.84 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.756  -11.378 11.427  0.32 17.77 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.803  -11.712 9.760   0.68 17.84 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.917  -11.438 10.359  0.32 17.77 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.298  -14.036 9.580   0.68 20.92 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 7.281  -13.707 9.942   0.32 18.71 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.216  -14.789 10.236  0.68 23.32 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 5.293  -14.502 10.679  0.32 19.67 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 5.994  -14.241 11.508  0.68 23.32 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.053  -13.967 11.968  0.32 19.67 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.865  -13.356 10.826  0.68 23.32 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 4.902  -13.096 11.307  0.32 19.67 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.601  -13.754 8.021   0.68 22.28 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 5.512  -13.116 8.544   0.32 19.85 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.337  -12.289 8.576   0.68 22.28 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 5.391  -11.722 9.297   0.32 19.85 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.708  -12.627 7.848   0.68 22.28 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.689  -12.053 8.442   0.32 19.85 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.172  -14.666 11.540  0.68 13.62 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.421  -14.600 12.075  0.32 13.17 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.187 -15.663 11.230  0.68 14.39 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.333 -15.626 11.590  0.32 12.99 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.854  -16.281 9.879   0.68 14.59 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.864  -16.120 10.228  0.32 12.62 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.808  -16.915 9.731   0.68 16.27 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.689  -16.458 10.050  0.32 12.79 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.207 -16.718 12.337  0.68 14.46 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.383 -16.783 12.586  0.32 13.06 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.247 -17.816 12.186  0.68 14.77 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.376 -17.888 12.242  0.32 13.42 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.347 -18.625 13.481  0.68 14.25 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.428 -18.924 13.360  0.32 13.34 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.294 -19.813 13.347  0.68 14.93 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.515 -19.966 13.133  0.32 13.32 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.683 -19.396 13.018  0.68 15.33 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.873 -19.358 13.072  0.32 13.48 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.474  -14.988 11.934  0.68 16.33 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.914  -14.847 12.722  0.32 15.80 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.052 -15.240 11.175  0.68 17.26 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 11.223 -15.252 11.496  0.32 15.59 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.378 -16.268 13.180  0.68 17.35 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.628 -16.429 13.455  0.32 15.67 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.335  -17.143 12.372  0.68 17.35 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.502  -17.184 12.634  0.32 15.67 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 10.984 -18.414 11.469  0.68 17.72 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 11.096 -18.331 11.424  0.32 16.10 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.112 -17.421 12.004  0.68 17.72 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 12.260 -17.506 12.134  0.32 16.10 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.674 -18.053 14.193  0.68 17.09 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.608 -18.477 14.200  0.32 16.01 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.464 -18.967 13.713  0.68 17.09 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.573 -19.385 13.404  0.32 16.01 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.317 -20.298 14.188  0.68 17.91 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.501 -20.604 13.865  0.32 15.98 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 11.977 -20.393 12.638  0.68 17.91 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 12.348 -20.420 12.293  0.32 15.98 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.204 -20.116 12.934  0.68 18.39 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.487 -19.998 12.985  0.32 16.17 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.692 -18.944 12.252  0.68 18.39 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.929 -18.809 12.376  0.32 16.17 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.008 -18.880 13.665  0.68 18.39 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 14.036 -18.902 13.818  0.32 16.17 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.728 -16.084 8.890   0.68 13.52 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.783 -16.150 9.262   0.32 12.54 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.491 -16.689 7.585   0.68 13.65 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.489 -16.630 7.916   0.32 13.18 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.111 -18.070 7.476   0.68 13.76 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 11.057 -18.019 7.640   0.32 13.44 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.519 -18.961 6.857   0.68 14.04 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.365 -18.865 7.067   0.32 13.61 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.051 -15.817 6.461   0.68 13.70 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 11.010 -15.632 6.871   0.32 13.33 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.394 -14.453 6.263   0.68 14.17 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.332 -14.258 6.825   0.32 13.35 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.138 -13.685 5.192   0.68 14.80 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.861 -13.428 5.659   0.32 13.92 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.921  -14.605 5.903   0.68 14.57 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.824  -14.419 6.726   0.32 13.59 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.453 -15.624 8.948   0.68 16.22 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.598 -15.889 9.370   0.32 15.04 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.535  -16.783 7.448   0.68 16.38 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.532  -16.686 7.813   0.32 15.82 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 11.990 -15.664 6.639   0.68 16.43 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.952 -15.470 7.039   0.32 15.99 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 10.959 -16.308 5.627   0.68 16.43 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.903 -16.024 5.993   0.32 15.99 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.452 -13.954 7.089   0.68 16.99 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.528 -13.770 7.643   0.32 16.02 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.714 -12.822 5.073   0.68 17.76 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.419 -12.562 5.654   0.32 16.70 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.060 -13.566 5.473   0.68 17.76 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.818 -13.307 5.764   0.32 16.70 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.108 -14.188 4.362   0.68 17.76 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.676 -13.895 4.829   0.32 16.70 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.563  -13.738 5.665   0.68 17.48 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.428  -13.571 6.474   0.32 16.31 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.840  -15.214 5.148   0.68 17.48 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.626  -15.092 6.058   0.32 16.31 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.442  -14.965 6.666   0.68 17.48 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.483  -14.700 7.591   0.32 16.31 ?  12  LEU   A HD23 1 
ATOM   306  N  N    . THR   A 1 13  ? 12.303 -18.260 8.037   1.00 13.65 ?  13  THR   A N    1 
ATOM   307  C  CA   . THR   A 1 13  ? 12.982 -19.543 7.930   1.00 13.69 ?  13  THR   A CA   1 
ATOM   308  C  C    . THR   A 1 13  ? 13.771 -19.768 9.213   1.00 13.89 ?  13  THR   A C    1 
ATOM   309  O  O    . THR   A 1 13  ? 13.676 -19.002 10.177  1.00 14.12 ?  13  THR   A O    1 
ATOM   310  C  CB   . THR   A 1 13  ? 13.954 -19.580 6.742   1.00 14.61 ?  13  THR   A CB   1 
ATOM   311  O  OG1  . THR   A 1 13  ? 15.025 -18.665 6.989   1.00 14.79 ?  13  THR   A OG1  1 
ATOM   312  C  CG2  . THR   A 1 13  ? 13.276 -19.237 5.417   1.00 16.03 ?  13  THR   A CG2  1 
ATOM   313  H  H    A THR   A 1 13  ? 12.739 -17.659 8.472   0.68 16.37 ?  13  THR   A H    1 
ATOM   314  H  H    B THR   A 1 13  ? 12.803 -17.657 8.393   0.32 16.37 ?  13  THR   A H    1 
ATOM   315  H  HA   . THR   A 1 13  ? 12.331 -20.258 7.828   1.00 16.43 ?  13  THR   A HA   1 
ATOM   316  H  HB   . THR   A 1 13  ? 14.320 -20.471 6.661   1.00 17.53 ?  13  THR   A HB   1 
ATOM   317  H  HG1  . THR   A 1 13  ? 15.566 -18.674 6.338   1.00 17.74 ?  13  THR   A HG1  1 
ATOM   318  H  HG21 . THR   A 1 13  ? 13.898 -19.389 4.682   1.00 19.23 ?  13  THR   A HG21 1 
ATOM   319  H  HG22 . THR   A 1 13  ? 12.501 -19.807 5.286   1.00 19.23 ?  13  THR   A HG22 1 
ATOM   320  H  HG23 . THR   A 1 13  ? 12.998 -18.314 5.409   1.00 19.23 ?  13  THR   A HG23 1 
ATOM   321  N  N    A ASP   A 1 14  ? 14.597 -20.811 9.223   0.68 14.51 ?  14  ASP   A N    1 
ATOM   322  N  N    B ASP   A 1 14  ? 14.560 -20.842 9.193   0.32 14.17 ?  14  ASP   A N    1 
ATOM   323  C  CA   A ASP   A 1 14  ? 15.418 -21.078 10.396  0.68 15.10 ?  14  ASP   A CA   1 
ATOM   324  C  CA   B ASP   A 1 14  ? 15.455 -21.154 10.294  0.32 14.58 ?  14  ASP   A CA   1 
ATOM   325  C  C    A ASP   A 1 14  ? 16.223 -19.852 10.822  0.68 14.73 ?  14  ASP   A C    1 
ATOM   326  C  C    B ASP   A 1 14  ? 16.339 -19.969 10.662  0.32 13.26 ?  14  ASP   A C    1 
ATOM   327  O  O    A ASP   A 1 14  ? 16.385 -19.591 12.020  0.68 15.06 ?  14  ASP   A O    1 
ATOM   328  O  O    B ASP   A 1 14  ? 16.720 -19.822 11.829  0.32 12.80 ?  14  ASP   A O    1 
ATOM   329  C  CB   A ASP   A 1 14  ? 16.362 -22.242 10.110  0.68 17.51 ?  14  ASP   A CB   1 
ATOM   330  C  CB   B ASP   A 1 14  ? 16.329 -22.349 9.904   0.32 17.09 ?  14  ASP   A CB   1 
ATOM   331  C  CG   A ASP   A 1 14  ? 17.199 -22.597 11.304  0.68 21.06 ?  14  ASP   A CG   1 
ATOM   332  C  CG   B ASP   A 1 14  ? 17.476 -22.563 10.869  0.32 19.71 ?  14  ASP   A CG   1 
ATOM   333  O  OD1  A ASP   A 1 14  ? 16.628 -23.049 12.318  0.68 22.16 ?  14  ASP   A OD1  1 
ATOM   334  O  OD1  B ASP   A 1 14  ? 17.217 -22.923 12.037  0.32 20.49 ?  14  ASP   A OD1  1 
ATOM   335  O  OD2  A ASP   A 1 14  ? 18.426 -22.421 11.234  0.68 23.45 -1 14  ASP   A OD2  1 
ATOM   336  O  OD2  B ASP   A 1 14  ? 18.637 -22.354 10.460  0.32 21.01 -1 14  ASP   A OD2  1 
ATOM   337  H  H    A ASP   A 1 14  ? 14.709 -21.359 8.572   0.68 17.41 ?  14  ASP   A H    1 
ATOM   338  H  H    B ASP   A 1 14  ? 14.597 -21.401 8.541   0.32 17.00 ?  14  ASP   A H    1 
ATOM   339  H  HA   A ASP   A 1 14  ? 14.845 -21.333 11.135  0.68 18.11 ?  14  ASP   A HA   1 
ATOM   340  H  HA   B ASP   A 1 14  ? 14.936 -21.404 11.073  0.32 17.49 ?  14  ASP   A HA   1 
ATOM   341  H  HB2  A ASP   A 1 14  ? 15.835 -23.028 9.882   0.68 21.00 ?  14  ASP   A HB2  1 
ATOM   342  H  HB2  B ASP   A 1 14  ? 15.776 -23.156 9.878   0.32 20.50 ?  14  ASP   A HB2  1 
ATOM   343  H  HB3  A ASP   A 1 14  ? 16.938 -22.009 9.361   0.68 21.00 ?  14  ASP   A HB3  1 
ATOM   344  H  HB3  B ASP   A 1 14  ? 16.706 -22.195 9.018   0.32 20.50 ?  14  ASP   A HB3  1 
ATOM   345  N  N    A ASN   A 1 15  ? 16.741 -19.085 9.857   0.68 14.06 ?  15  ASN   A N    1 
ATOM   346  N  N    B ASN   A 1 15  ? 16.671 -19.106 9.690   0.32 12.28 ?  15  ASN   A N    1 
ATOM   347  C  CA   A ASN   A 1 15  ? 17.703 -18.026 10.147  0.68 14.40 ?  15  ASN   A CA   1 
ATOM   348  C  CA   B ASN   A 1 15  ? 17.696 -18.094 9.926   0.32 12.26 ?  15  ASN   A CA   1 
ATOM   349  C  C    A ASN   A 1 15  ? 17.308 -16.641 9.647   0.68 13.91 ?  15  ASN   A C    1 
ATOM   350  C  C    B ASN   A 1 15  ? 17.360 -16.706 9.383   0.32 12.44 ?  15  ASN   A C    1 
ATOM   351  O  O    A ASN   A 1 15  ? 18.020 -15.680 9.961   0.68 13.61 ?  15  ASN   A O    1 
ATOM   352  O  O    B ASN   A 1 15  ? 18.247 -15.841 9.366   0.32 12.52 ?  15  ASN   A O    1 
ATOM   353  C  CB   A ASN   A 1 15  ? 19.083 -18.372 9.556   0.68 14.59 ?  15  ASN   A CB   1 
ATOM   354  C  CB   B ASN   A 1 15  ? 19.050 -18.555 9.364   0.32 11.64 ?  15  ASN   A CB   1 
ATOM   355  C  CG   A ASN   A 1 15  ? 19.040 -18.560 8.055   0.68 14.34 ?  15  ASN   A CG   1 
ATOM   356  C  CG   B ASN   A 1 15  ? 19.092 -18.527 7.852   0.32 12.06 ?  15  ASN   A CG   1 
ATOM   357  O  OD1  A ASN   A 1 15  ? 18.243 -19.350 7.541   0.68 14.55 ?  15  ASN   A OD1  1 
ATOM   358  O  OD1  B ASN   A 1 15  ? 18.535 -19.403 7.184   0.32 12.40 ?  15  ASN   A OD1  1 
ATOM   359  N  ND2  A ASN   A 1 15  ? 19.884 -17.818 7.336   0.68 14.37 ?  15  ASN   A ND2  1 
ATOM   360  N  ND2  B ASN   A 1 15  ? 19.759 -17.518 7.299   0.32 11.90 ?  15  ASN   A ND2  1 
ATOM   361  H  H    A ASN   A 1 15  ? 16.550 -19.160 9.030   0.68 16.87 ?  15  ASN   A H    1 
ATOM   362  H  H    B ASN   A 1 15  ? 16.314 -19.089 8.907   0.32 14.73 ?  15  ASN   A H    1 
ATOM   363  H  HA   A ASN   A 1 15  ? 17.819 -17.962 11.111  0.68 17.27 ?  15  ASN   A HA   1 
ATOM   364  H  HA   B ASN   A 1 15  ? 17.810 -18.005 10.880  0.32 14.71 ?  15  ASN   A HA   1 
ATOM   365  H  HB2  A ASN   A 1 15  ? 19.704 -17.646 9.756   0.68 17.50 ?  15  ASN   A HB2  1 
ATOM   366  H  HB2  B ASN   A 1 15  ? 19.747 -17.961 9.698   0.32 13.96 ?  15  ASN   A HB2  1 
ATOM   367  H  HB3  A ASN   A 1 15  ? 19.402 -19.194 9.957   0.68 17.50 ?  15  ASN   A HB3  1 
ATOM   368  H  HB3  B ASN   A 1 15  ? 19.226 -19.463 9.659   0.32 13.96 ?  15  ASN   A HB3  1 
ATOM   369  H  HD21 A ASN   A 1 15  ? 19.895 -17.890 6.478   0.68 17.24 ?  15  ASN   A HD21 1 
ATOM   370  H  HD21 B ASN   A 1 15  ? 19.816 -17.459 6.444   0.32 14.27 ?  15  ASN   A HD21 1 
ATOM   371  H  HD22 A ASN   A 1 15  ? 20.427 -17.273 7.725   0.68 17.24 ?  15  ASN   A HD22 1 
ATOM   372  H  HD22 B ASN   A 1 15  ? 20.131 -16.920 7.796   0.32 14.27 ?  15  ASN   A HD22 1 
ATOM   373  N  N    A VAL   A 1 16  ? 16.222 -16.503 8.882   0.68 13.89 ?  16  VAL   A N    1 
ATOM   374  N  N    B VAL   A 1 16  ? 16.124 -16.446 8.962   0.32 12.70 ?  16  VAL   A N    1 
ATOM   375  C  CA   A VAL   A 1 16  ? 15.817 -15.227 8.295   0.68 13.70 ?  16  VAL   A CA   1 
ATOM   376  C  CA   B VAL   A 1 16  ? 15.740 -15.157 8.398   0.32 12.93 ?  16  VAL   A CA   1 
ATOM   377  C  C    A VAL   A 1 16  ? 14.528 -14.740 8.945   0.68 13.15 ?  16  VAL   A C    1 
ATOM   378  C  C    B VAL   A 1 16  ? 14.508 -14.646 9.135   0.32 13.05 ?  16  VAL   A C    1 
ATOM   379  O  O    A VAL   A 1 16  ? 13.516 -15.456 8.975   0.68 12.61 ?  16  VAL   A O    1 
ATOM   380  O  O    B VAL   A 1 16  ? 13.558 -15.398 9.381   0.32 13.10 ?  16  VAL   A O    1 
ATOM   381  C  CB   A VAL   A 1 16  ? 15.663 -15.304 6.766   0.68 14.01 ?  16  VAL   A CB   1 
ATOM   382  C  CB   B VAL   A 1 16  ? 15.485 -15.254 6.878   0.32 13.06 ?  16  VAL   A CB   1 
ATOM   383  C  CG1  A VAL   A 1 16  ? 15.230 -13.941 6.211   0.68 14.90 ?  16  VAL   A CG1  1 
ATOM   384  C  CG1  B VAL   A 1 16  ? 15.035 -13.909 6.305   0.32 13.39 ?  16  VAL   A CG1  1 
ATOM   385  C  CG2  A VAL   A 1 16  ? 16.952 -15.766 6.109   0.68 15.00 ?  16  VAL   A CG2  1 
ATOM   386  C  CG2  B VAL   A 1 16  ? 16.730 -15.763 6.151   0.32 13.64 ?  16  VAL   A CG2  1 
ATOM   387  H  H    A VAL   A 1 16  ? 15.703 -17.157 8.690   0.68 16.66 ?  16  VAL   A H    1 
ATOM   388  H  H    B VAL   A 1 16  ? 15.476 -17.007 9.002   0.32 15.23 ?  16  VAL   A H    1 
ATOM   389  H  HA   A VAL   A 1 16  ? 16.508 -14.572 8.481   0.68 16.44 ?  16  VAL   A HA   1 
ATOM   390  H  HA   B VAL   A 1 16  ? 16.459 -14.518 8.539   0.32 15.51 ?  16  VAL   A HA   1 
ATOM   391  H  HB   A VAL   A 1 16  ? 14.974 -15.952 6.553   0.68 16.81 ?  16  VAL   A HB   1 
ATOM   392  H  HB   B VAL   A 1 16  ? 14.775 -15.893 6.728   0.32 15.67 ?  16  VAL   A HB   1 
ATOM   393  H  HG11 A VAL   A 1 16  ? 15.350 -13.942 5.251   0.68 17.88 ?  16  VAL   A HG11 1 
ATOM   394  H  HG11 B VAL   A 1 16  ? 15.049 -13.964 5.336   0.32 16.06 ?  16  VAL   A HG11 1 
ATOM   395  H  HG12 A VAL   A 1 16  ? 14.295 -13.796 6.428   0.68 17.88 ?  16  VAL   A HG12 1 
ATOM   396  H  HG12 B VAL   A 1 16  ? 14.135 -13.719 6.611   0.32 16.06 ?  16  VAL   A HG12 1 
ATOM   397  H  HG13 A VAL   A 1 16  ? 15.776 -13.250 6.614   0.68 17.88 ?  16  VAL   A HG13 1 
ATOM   398  H  HG13 B VAL   A 1 16  ? 15.643 -13.217 6.604   0.32 16.06 ?  16  VAL   A HG13 1 
ATOM   399  H  HG21 A VAL   A 1 16  ? 16.840 -15.742 5.146   0.68 18.00 ?  16  VAL   A HG21 1 
ATOM   400  H  HG21 B VAL   A 1 16  ? 16.557 -15.770 5.196   0.32 16.36 ?  16  VAL   A HG21 1 
ATOM   401  H  HG22 A VAL   A 1 16  ? 17.671 -15.173 6.373   0.68 18.00 ?  16  VAL   A HG22 1 
ATOM   402  H  HG22 B VAL   A 1 16  ? 17.476 -15.173 6.345   0.32 16.36 ?  16  VAL   A HG22 1 
ATOM   403  H  HG23 A VAL   A 1 16  ? 17.148 -16.671 6.397   0.68 18.00 ?  16  VAL   A HG23 1 
ATOM   404  H  HG23 B VAL   A 1 16  ? 16.933 -16.661 6.457   0.32 16.36 ?  16  VAL   A HG23 1 
ATOM   405  N  N    A TYR   A 1 17  ? 14.565 -13.485 9.393   0.68 13.28 ?  17  TYR   A N    1 
ATOM   406  N  N    B TYR   A 1 17  ? 14.531 -13.356 9.477   0.32 12.89 ?  17  TYR   A N    1 
ATOM   407  C  CA   A TYR   A 1 17  ? 13.473 -12.791 10.060  0.68 13.18 ?  17  TYR   A CA   1 
ATOM   408  C  CA   B TYR   A 1 17  ? 13.491 -12.702 10.258  0.32 12.31 ?  17  TYR   A CA   1 
ATOM   409  C  C    A TYR   A 1 17  ? 13.191 -11.483 9.327   0.68 13.29 ?  17  TYR   A C    1 
ATOM   410  C  C    B TYR   A 1 17  ? 13.220 -11.338 9.641   0.32 12.18 ?  17  TYR   A C    1 
ATOM   411  O  O    A TYR   A 1 17  ? 14.072 -10.932 8.662   0.68 12.11 ?  17  TYR   A O    1 
ATOM   412  O  O    B TYR   A 1 17  ? 14.152 -10.681 9.171   0.32 11.76 ?  17  TYR   A O    1 
ATOM   413  C  CB   A TYR   A 1 17  ? 13.873 -12.490 11.506  0.68 14.02 ?  17  TYR   A CB   1 
ATOM   414  C  CB   B TYR   A 1 17  ? 13.961 -12.529 11.707  0.32 12.85 ?  17  TYR   A CB   1 
ATOM   415  C  CG   A TYR   A 1 17  ? 14.024 -13.733 12.356  0.68 14.96 ?  17  TYR   A CG   1 
ATOM   416  C  CG   B TYR   A 1 17  ? 14.241 -13.831 12.430  0.32 13.18 ?  17  TYR   A CG   1 
ATOM   417  C  CD1  A TYR   A 1 17  ? 15.171 -14.518 12.291  0.68 15.88 ?  17  TYR   A CD1  1 
ATOM   418  C  CD1  B TYR   A 1 17  ? 15.465 -14.482 12.307  0.32 13.72 ?  17  TYR   A CD1  1 
ATOM   419  C  CD2  A TYR   A 1 17  ? 13.006 -14.133 13.213  0.68 15.33 ?  17  TYR   A CD2  1 
ATOM   420  C  CD2  B TYR   A 1 17  ? 13.276 -14.407 13.243  0.32 13.47 ?  17  TYR   A CD2  1 
ATOM   421  C  CE1  A TYR   A 1 17  ? 15.301 -15.669 13.062  0.68 16.14 ?  17  TYR   A CE1  1 
ATOM   422  C  CE1  B TYR   A 1 17  ? 15.712 -15.678 12.973  0.32 14.17 ?  17  TYR   A CE1  1 
ATOM   423  C  CE2  A TYR   A 1 17  ? 13.123 -15.288 13.985  0.68 15.50 ?  17  TYR   A CE2  1 
ATOM   424  C  CE2  B TYR   A 1 17  ? 13.511 -15.594 13.909  0.32 13.56 ?  17  TYR   A CE2  1 
ATOM   425  C  CZ   A TYR   A 1 17  ? 14.275 -16.048 13.909  0.68 15.68 ?  17  TYR   A CZ   1 
ATOM   426  C  CZ   B TYR   A 1 17  ? 14.726 -16.226 13.774  0.32 13.66 ?  17  TYR   A CZ   1 
ATOM   427  O  OH   A TYR   A 1 17  ? 14.401 -17.189 14.676  0.68 16.07 ?  17  TYR   A OH   1 
ATOM   428  O  OH   B TYR   A 1 17  ? 14.941 -17.406 14.450  0.32 13.33 ?  17  TYR   A OH   1 
ATOM   429  H  H    A TYR   A 1 17  ? 15.263 -12.995 9.311   0.68 15.93 ?  17  TYR   A H    1 
ATOM   430  H  H    B TYR   A 1 17  ? 15.167 -12.815 9.257   0.32 15.47 ?  17  TYR   A H    1 
ATOM   431  H  HA   A TYR   A 1 17  ? 12.676 -13.349 10.051  0.68 15.82 ?  17  TYR   A HA   1 
ATOM   432  H  HA   B TYR   A 1 17  ? 12.675 -13.228 10.246  0.32 14.77 ?  17  TYR   A HA   1 
ATOM   433  H  HB2  A TYR   A 1 17  ? 14.723 -12.024 11.500  0.68 16.81 ?  17  TYR   A HB2  1 
ATOM   434  H  HB2  B TYR   A 1 17  ? 14.778 -12.009 11.709  0.32 15.42 ?  17  TYR   A HB2  1 
ATOM   435  H  HB3  A TYR   A 1 17  ? 13.192 -11.935 11.903  0.68 16.81 ?  17  TYR   A HB3  1 
ATOM   436  H  HB3  B TYR   A 1 17  ? 13.274 -12.062 12.204  0.32 15.42 ?  17  TYR   A HB3  1 
ATOM   437  H  HD1  A TYR   A 1 17  ? 15.867 -14.275 11.721  0.68 19.05 ?  17  TYR   A HD1  1 
ATOM   438  H  HD1  B TYR   A 1 17  ? 16.128 -14.117 11.766  0.32 16.46 ?  17  TYR   A HD1  1 
ATOM   439  H  HD2  A TYR   A 1 17  ? 12.229 -13.627 13.269  0.68 18.39 ?  17  TYR   A HD2  1 
ATOM   440  H  HD2  B TYR   A 1 17  ? 12.453 -13.988 13.338  0.32 16.16 ?  17  TYR   A HD2  1 
ATOM   441  H  HE1  A TYR   A 1 17  ? 16.079 -16.188 13.009  0.68 19.37 ?  17  TYR   A HE1  1 
ATOM   442  H  HE1  B TYR   A 1 17  ? 16.535 -16.108 12.883  0.32 17.00 ?  17  TYR   A HE1  1 
ATOM   443  H  HE2  A TYR   A 1 17  ? 12.433 -15.538 14.559  0.68 18.60 ?  17  TYR   A HE2  1 
ATOM   444  H  HE2  B TYR   A 1 17  ? 12.851 -15.965 14.450  0.32 16.27 ?  17  TYR   A HE2  1 
ATOM   445  H  HH   A TYR   A 1 17  ? 13.640 -17.431 14.952  0.68 19.28 ?  17  TYR   A HH   1 
ATOM   446  H  HH   B TYR   A 1 17  ? 15.701 -17.716 14.258  0.32 16.00 ?  17  TYR   A HH   1 
ATOM   447  N  N    A ILE   A 1 18  ? 11.972 -10.955 9.464   0.68 13.88 ?  18  ILE   A N    1 
ATOM   448  N  N    B ILE   A 1 18  ? 11.953 -10.902 9.634   0.32 12.49 ?  18  ILE   A N    1 
ATOM   449  C  CA   A ILE   A 1 18  ? 11.579 -9.767  8.700   0.68 14.55 ?  18  ILE   A CA   1 
ATOM   450  C  CA   B ILE   A 1 18  ? 11.565 -9.695  8.911   0.32 12.65 ?  18  ILE   A CA   1 
ATOM   451  C  C    A ILE   A 1 18  ? 10.611 -8.912  9.516   0.68 15.28 ?  18  ILE   A C    1 
ATOM   452  C  C    B ILE   A 1 18  ? 10.653 -8.818  9.765   0.32 13.13 ?  18  ILE   A C    1 
ATOM   453  O  O    A ILE   A 1 18  ? 9.737  -9.431  10.219  0.68 14.80 ?  18  ILE   A O    1 
ATOM   454  O  O    B ILE   A 1 18  ? 9.953  -9.291  10.665  0.32 13.11 ?  18  ILE   A O    1 
ATOM   455  C  CB   A ILE   A 1 18  ? 11.042 -10.169 7.306   0.68 14.22 ?  18  ILE   A CB   1 
ATOM   456  C  CB   B ILE   A 1 18  ? 10.895 -10.040 7.561   0.32 12.36 ?  18  ILE   A CB   1 
ATOM   457  C  CG1  A ILE   A 1 18  ? 10.941 -8.959  6.381   0.68 15.11 ?  18  ILE   A CG1  1 
ATOM   458  C  CG1  B ILE   A 1 18  ? 10.963 -8.860  6.587   0.32 13.10 ?  18  ILE   A CG1  1 
ATOM   459  C  CG2  A ILE   A 1 18  ? 9.710  -10.931 7.416   0.68 13.69 ?  18  ILE   A CG2  1 
ATOM   460  C  CG2  B ILE   A 1 18  ? 9.457  -10.508 7.775   0.32 12.37 ?  18  ILE   A CG2  1 
ATOM   461  C  CD1  A ILE   A 1 18  ? 10.714 -9.336  4.939   0.68 17.30 ?  18  ILE   A CD1  1 
ATOM   462  C  CD1  B ILE   A 1 18  ? 10.620 -9.243  5.162   0.32 14.27 ?  18  ILE   A CD1  1 
ATOM   463  H  H    A ILE   A 1 18  ? 11.361 -11.270 9.984   0.68 16.65 ?  18  ILE   A H    1 
ATOM   464  H  H    B ILE   A 1 18  ? 11.300 -11.303 10.030  0.32 14.98 ?  18  ILE   A H    1 
ATOM   465  H  HA   A ILE   A 1 18  ? 12.375 -9.238  8.548   0.68 17.45 ?  18  ILE   A HA   1 
ATOM   466  H  HA   B ILE   A 1 18  ? 12.369 -9.185  8.716   0.32 15.18 ?  18  ILE   A HA   1 
ATOM   467  H  HB   A ILE   A 1 18  ? 11.685 -10.781 6.907   0.68 17.05 ?  18  ILE   A HB   1 
ATOM   468  H  HB   B ILE   A 1 18  ? 11.387 -10.772 7.168   0.32 14.82 ?  18  ILE   A HB   1 
ATOM   469  H  HG12 A ILE   A 1 18  ? 10.202 -8.405  6.665   0.68 18.12 ?  18  ILE   A HG12 1 
ATOM   470  H  HG12 B ILE   A 1 18  ? 10.336 -8.177  6.867   0.32 15.71 ?  18  ILE   A HG12 1 
ATOM   471  H  HG13 A ILE   A 1 18  ? 11.772 -8.459  6.428   0.68 18.12 ?  18  ILE   A HG13 1 
ATOM   472  H  HG13 B ILE   A 1 18  ? 11.865 -8.501  6.585   0.32 15.71 ?  18  ILE   A HG13 1 
ATOM   473  H  HG21 A ILE   A 1 18  ? 9.468  -11.281 6.538   0.68 16.42 ?  18  ILE   A HG21 1 
ATOM   474  H  HG21 B ILE   A 1 18  ? 9.141  -10.934 6.961   0.32 14.84 ?  18  ILE   A HG21 1 
ATOM   475  H  HG22 A ILE   A 1 18  ? 9.817  -11.669 8.038   0.68 16.42 ?  18  ILE   A HG22 1 
ATOM   476  H  HG22 B ILE   A 1 18  ? 9.437  -11.141 8.508   0.32 14.84 ?  18  ILE   A HG22 1 
ATOM   477  H  HG23 A ILE   A 1 18  ? 9.022  -10.329 7.729   0.68 16.42 ?  18  ILE   A HG23 1 
ATOM   478  H  HG23 B ILE   A 1 18  ? 8.896  -9.743  7.983   0.32 14.84 ?  18  ILE   A HG23 1 
ATOM   479  H  HD11 A ILE   A 1 18  ? 10.739 -8.531  4.397   0.68 20.75 ?  18  ILE   A HD11 1 
ATOM   480  H  HD11 B ILE   A 1 18  ? 10.778 -8.482  4.579   0.32 17.12 ?  18  ILE   A HD11 1 
ATOM   481  H  HD12 A ILE   A 1 18  ? 11.411 -9.947  4.657   0.68 20.75 ?  18  ILE   A HD12 1 
ATOM   482  H  HD12 B ILE   A 1 18  ? 11.181 -9.987  4.889   0.32 17.12 ?  18  ILE   A HD12 1 
ATOM   483  H  HD13 A ILE   A 1 18  ? 9.846  -9.762  4.858   0.68 20.75 ?  18  ILE   A HD13 1 
ATOM   484  H  HD13 B ILE   A 1 18  ? 9.686  -9.502  5.119   0.32 17.12 ?  18  ILE   A HD13 1 
ATOM   485  N  N    A LYS   A 1 19  ? 10.767 -7.586  9.406   0.68 15.42 ?  19  LYS   A N    1 
ATOM   486  N  N    B LYS   A 1 19  ? 10.651 -7.519  9.449   0.32 13.75 ?  19  LYS   A N    1 
ATOM   487  C  CA   A LYS   A 1 19  ? 9.951  -6.620  10.134  0.68 16.54 ?  19  LYS   A CA   1 
ATOM   488  C  CA   B LYS   A 1 19  ? 9.866  -6.551  10.203  0.32 14.86 ?  19  LYS   A CA   1 
ATOM   489  C  C    A LYS   A 1 19  ? 9.719  -5.393  9.263   0.68 16.58 ?  19  LYS   A C    1 
ATOM   490  C  C    B LYS   A 1 19  ? 9.727  -5.266  9.394   0.32 14.76 ?  19  LYS   A C    1 
ATOM   491  O  O    A LYS   A 1 19  ? 10.571 -5.025  8.450   0.68 16.19 ?  19  LYS   A O    1 
ATOM   492  O  O    B LYS   A 1 19  ? 10.686 -4.823  8.758   0.32 14.61 ?  19  LYS   A O    1 
ATOM   493  C  CB   A LYS   A 1 19  ? 10.683 -6.185  11.415  0.68 17.56 ?  19  LYS   A CB   1 
ATOM   494  C  CB   B LYS   A 1 19  ? 10.542 -6.250  11.544  0.32 15.96 ?  19  LYS   A CB   1 
ATOM   495  C  CG   A LYS   A 1 19  ? 9.930  -5.283  12.390  0.68 19.30 ?  19  LYS   A CG   1 
ATOM   496  C  CG   B LYS   A 1 19  ? 9.791  -5.263  12.409  0.32 17.15 ?  19  LYS   A CG   1 
ATOM   497  C  CD   A LYS   A 1 19  ? 10.847 -4.994  13.583  0.68 20.28 ?  19  LYS   A CD   1 
ATOM   498  C  CD   B LYS   A 1 19  ? 10.572 -4.965  13.668  0.32 18.14 ?  19  LYS   A CD   1 
ATOM   499  C  CE   A LYS   A 1 19  ? 10.227 -4.087  14.633  0.68 21.24 ?  19  LYS   A CE   1 
ATOM   500  C  CE   B LYS   A 1 19  ? 9.858  -3.953  14.538  0.32 18.95 ?  19  LYS   A CE   1 
ATOM   501  N  NZ   A LYS   A 1 19  ? 11.156 -3.912  15.793  0.68 21.45 ?  19  LYS   A NZ   1 
ATOM   502  N  NZ   B LYS   A 1 19  ? 10.675 -3.607  15.728  0.32 19.02 ?  19  LYS   A NZ   1 
ATOM   503  H  H    A LYS   A 1 19  ? 11.369 -7.220  8.910   0.68 18.50 ?  19  LYS   A H    1 
ATOM   504  H  H    B LYS   A 1 19  ? 11.095 -7.172  8.794   0.32 16.50 ?  19  LYS   A H    1 
ATOM   505  H  HA   A LYS   A 1 19  ? 9.098  -7.019  10.370  0.68 19.84 ?  19  LYS   A HA   1 
ATOM   506  H  HA   B LYS   A 1 19  ? 8.983  -6.910  10.375  0.32 17.82 ?  19  LYS   A HA   1 
ATOM   507  H  HB2  A LYS   A 1 19  ? 10.925 -6.983  11.904  0.68 21.06 ?  19  LYS   A HB2  1 
ATOM   508  H  HB2  B LYS   A 1 19  ? 10.624 -7.078  12.046  0.32 19.15 ?  19  LYS   A HB2  1 
ATOM   509  H  HB3  A LYS   A 1 19  ? 11.487 -5.712  11.152  0.68 21.06 ?  19  LYS   A HB3  1 
ATOM   510  H  HB3  B LYS   A 1 19  ? 11.424 -5.883  11.375  0.32 19.15 ?  19  LYS   A HB3  1 
ATOM   511  H  HG2  A LYS   A 1 19  ? 9.702  -4.443  11.961  0.68 23.16 ?  19  LYS   A HG2  1 
ATOM   512  H  HG2  B LYS   A 1 19  ? 9.667  -4.432  11.924  0.32 20.57 ?  19  LYS   A HG2  1 
ATOM   513  H  HG3  A LYS   A 1 19  ? 9.132  -5.733  12.711  0.68 23.16 ?  19  LYS   A HG3  1 
ATOM   514  H  HG3  B LYS   A 1 19  ? 8.934  -5.642  12.660  0.32 20.57 ?  19  LYS   A HG3  1 
ATOM   515  H  HD2  A LYS   A 1 19  ? 11.071 -5.834  14.015  0.68 24.33 ?  19  LYS   A HD2  1 
ATOM   516  H  HD2  B LYS   A 1 19  ? 10.682 -5.784  14.176  0.32 21.76 ?  19  LYS   A HD2  1 
ATOM   517  H  HD3  A LYS   A 1 19  ? 11.653 -4.565  13.260  0.68 24.33 ?  19  LYS   A HD3  1 
ATOM   518  H  HD3  B LYS   A 1 19  ? 11.439 -4.602  13.425  0.32 21.76 ?  19  LYS   A HD3  1 
ATOM   519  H  HE2  A LYS   A 1 19  ? 10.055 -3.213  14.247  0.68 25.48 ?  19  LYS   A HE2  1 
ATOM   520  H  HE2  B LYS   A 1 19  ? 9.702  -3.144  14.026  0.32 22.73 ?  19  LYS   A HE2  1 
ATOM   521  H  HE3  A LYS   A 1 19  ? 9.403  -4.480  14.959  0.68 25.48 ?  19  LYS   A HE3  1 
ATOM   522  H  HE3  B LYS   A 1 19  ? 9.017  -4.329  14.841  0.32 22.73 ?  19  LYS   A HE3  1 
ATOM   523  H  HZ1  A LYS   A 1 19  ? 10.774 -3.404  16.416  0.68 25.74 ?  19  LYS   A HZ1  1 
ATOM   524  H  HZ1  B LYS   A 1 19  ? 10.245 -3.014  16.230  0.32 22.82 ?  19  LYS   A HZ1  1 
ATOM   525  H  HZ2  A LYS   A 1 19  ? 11.352 -4.705  16.146  0.68 25.74 ?  19  LYS   A HZ2  1 
ATOM   526  H  HZ2  B LYS   A 1 19  ? 10.831 -4.338  16.212  0.32 22.82 ?  19  LYS   A HZ2  1 
ATOM   527  H  HZ3  A LYS   A 1 19  ? 11.908 -3.522  15.524  0.68 25.74 ?  19  LYS   A HZ3  1 
ATOM   528  H  HZ3  B LYS   A 1 19  ? 11.454 -3.260  15.471  0.32 22.82 ?  19  LYS   A HZ3  1 
ATOM   529  N  N    A ASN   A 1 20  ? 8.559  -4.758  9.438   0.68 17.68 ?  20  ASN   A N    1 
ATOM   530  N  N    B ASN   A 1 20  ? 8.531  -4.675  9.428   0.32 15.11 ?  20  ASN   A N    1 
ATOM   531  C  CA   A ASN   A 1 20  ? 8.327  -3.433  8.873   0.68 18.80 ?  20  ASN   A CA   1 
ATOM   532  C  CA   B ASN   A 1 20  ? 8.271  -3.380  8.796   0.32 15.75 ?  20  ASN   A CA   1 
ATOM   533  C  C    A ASN   A 1 20  ? 8.954  -2.435  9.834   0.68 19.05 ?  20  ASN   A C    1 
ATOM   534  C  C    B ASN   A 1 20  ? 8.851  -2.285  9.682   0.32 16.27 ?  20  ASN   A C    1 
ATOM   535  O  O    A ASN   A 1 20  ? 8.458  -2.240  10.949  0.68 19.74 ?  20  ASN   A O    1 
ATOM   536  O  O    B ASN   A 1 20  ? 8.225  -1.859  10.657  0.32 16.94 ?  20  ASN   A O    1 
ATOM   537  C  CB   A ASN   A 1 20  ? 6.831  -3.179  8.690   0.68 19.91 ?  20  ASN   A CB   1 
ATOM   538  C  CB   B ASN   A 1 20  ? 6.768  -3.189  8.599   0.32 15.84 ?  20  ASN   A CB   1 
ATOM   539  C  CG   A ASN   A 1 20  ? 6.509  -1.727  8.342   0.68 21.09 ?  20  ASN   A CG   1 
ATOM   540  C  CG   B ASN   A 1 20  ? 6.401  -1.817  8.036   0.32 16.09 ?  20  ASN   A CG   1 
ATOM   541  O  OD1  A ASN   A 1 20  ? 5.640  -1.110  8.963   0.68 22.67 ?  20  ASN   A OD1  1 
ATOM   542  O  OD1  B ASN   A 1 20  ? 5.254  -1.374  8.169   0.32 16.27 ?  20  ASN   A OD1  1 
ATOM   543  N  ND2  A ASN   A 1 20  ? 7.202  -1.184  7.345   0.68 21.69 ?  20  ASN   A ND2  1 
ATOM   544  N  ND2  B ASN   A 1 20  ? 7.360  -1.145  7.400   0.32 16.89 ?  20  ASN   A ND2  1 
ATOM   545  H  H    A ASN   A 1 20  ? 7.901  -5.068  9.895   0.68 21.21 ?  20  ASN   A H    1 
ATOM   546  H  H    B ASN   A 1 20  ? 7.839  -5.023  9.803   0.32 18.12 ?  20  ASN   A H    1 
ATOM   547  H  HA   A ASN   A 1 20  ? 8.762  -3.361  8.010   0.68 22.56 ?  20  ASN   A HA   1 
ATOM   548  H  HA   B ASN   A 1 20  ? 8.712  -3.345  7.934   0.32 18.90 ?  20  ASN   A HA   1 
ATOM   549  H  HB2  A ASN   A 1 20  ? 6.504  -3.740  7.967   0.68 23.88 ?  20  ASN   A HB2  1 
ATOM   550  H  HB2  B ASN   A 1 20  ? 6.445  -3.860  7.983   0.32 19.00 ?  20  ASN   A HB2  1 
ATOM   551  H  HB3  A ASN   A 1 20  ? 6.370  -3.400  9.512   0.68 23.88 ?  20  ASN   A HB3  1 
ATOM   552  H  HB3  B ASN   A 1 20  ? 6.326  -3.286  9.458   0.32 19.00 ?  20  ASN   A HB3  1 
ATOM   553  H  HD21 A ASN   A 1 20  ? 7.055  -0.370  7.113   0.68 26.02 ?  20  ASN   A HD21 1 
ATOM   554  H  HD21 B ASN   A 1 20  ? 7.192  -0.371  7.074   0.32 20.26 ?  20  ASN   A HD21 1 
ATOM   555  H  HD22 A ASN   A 1 20  ? 7.806  -1.645  6.938   0.68 26.02 ?  20  ASN   A HD22 1 
ATOM   556  H  HD22 B ASN   A 1 20  ? 8.149  -1.479  7.317   0.32 20.26 ?  20  ASN   A HD22 1 
ATOM   557  N  N    A ALA   A 1 21  ? 10.072 -1.841  9.433   0.68 19.08 ?  21  ALA   A N    1 
ATOM   558  N  N    B ALA   A 1 21  ? 10.043 -1.806  9.332   0.32 16.51 ?  21  ALA   A N    1 
ATOM   559  C  CA   A ALA   A 1 21  ? 10.777 -0.946  10.333  0.68 18.81 ?  21  ALA   A CA   1 
ATOM   560  C  CA   B ALA   A 1 21  ? 10.714 -0.796  10.138  0.32 16.54 ?  21  ALA   A CA   1 
ATOM   561  C  C    A ALA   A 1 21  ? 11.713 -0.063  9.532   0.68 18.10 ?  21  ALA   A C    1 
ATOM   562  C  C    B ALA   A 1 21  ? 11.799 -0.126  9.312   0.32 15.75 ?  21  ALA   A C    1 
ATOM   563  O  O    A ALA   A 1 21  ? 12.129 -0.408  8.423   0.68 17.96 ?  21  ALA   A O    1 
ATOM   564  O  O    B ALA   A 1 21  ? 12.309 -0.694  8.342   0.32 15.65 ?  21  ALA   A O    1 
ATOM   565  C  CB   A ALA   A 1 21  ? 11.561 -1.729  11.387  0.68 19.74 ?  21  ALA   A CB   1 
ATOM   566  C  CB   B ALA   A 1 21  ? 11.318 -1.401  11.410  0.32 17.58 ?  21  ALA   A CB   1 
ATOM   567  H  H    A ALA   A 1 21  ? 10.439 -1.945  8.662   0.68 22.90 ?  21  ALA   A H    1 
ATOM   568  H  H    B ALA   A 1 21  ? 10.476 -2.042  8.627   0.32 19.80 ?  21  ALA   A H    1 
ATOM   569  H  HA   A ALA   A 1 21  ? 10.134 -0.376  10.787  0.68 22.57 ?  21  ALA   A HA   1 
ATOM   570  H  HA   B ALA   A 1 21  ? 10.071 -0.121  10.401  0.32 19.84 ?  21  ALA   A HA   1 
ATOM   571  H  HB1  A ALA   A 1 21  ? 11.962 -1.100  12.001  0.68 23.68 ?  21  ALA   A HB1  1 
ATOM   572  H  HB1  B ALA   A 1 21  ? 11.754 -0.699  11.918  0.32 21.09 ?  21  ALA   A HB1  1 
ATOM   573  H  HB2  A ALA   A 1 21  ? 10.945 -2.311  11.862  0.68 23.68 ?  21  ALA   A HB2  1 
ATOM   574  H  HB2  B ALA   A 1 21  ? 10.608 -1.799  11.939  0.32 21.09 ?  21  ALA   A HB2  1 
ATOM   575  H  HB3  A ALA   A 1 21  ? 12.241 -2.255  10.945  0.68 23.68 ?  21  ALA   A HB3  1 
ATOM   576  H  HB3  B ALA   A 1 21  ? 11.965 -2.081  11.162  0.32 21.09 ?  21  ALA   A HB3  1 
ATOM   577  N  N    A ASP   A 1 22  ? 12.021 1.090   10.120  0.68 17.78 ?  22  ASP   A N    1 
ATOM   578  N  N    B ASP   A 1 22  ? 12.129 1.102   9.709   0.32 15.72 ?  22  ASP   A N    1 
ATOM   579  C  CA   A ASP   A 1 22  ? 13.064 1.976   9.624   0.68 17.65 ?  22  ASP   A CA   1 
ATOM   580  C  CA   B ASP   A 1 22  ? 13.290 1.813   9.191   0.32 15.34 ?  22  ASP   A CA   1 
ATOM   581  C  C    A ASP   A 1 22  ? 14.395 1.484   10.179  0.68 16.06 ?  22  ASP   A C    1 
ATOM   582  C  C    B ASP   A 1 22  ? 14.541 1.228   9.838   0.32 14.00 ?  22  ASP   A C    1 
ATOM   583  O  O    A ASP   A 1 22  ? 14.602 1.492   11.397  0.68 16.36 ?  22  ASP   A O    1 
ATOM   584  O  O    B ASP   A 1 22  ? 14.626 1.137   11.067  0.32 14.06 ?  22  ASP   A O    1 
ATOM   585  C  CB   A ASP   A 1 22  ? 12.775 3.396   10.107  0.68 19.19 ?  22  ASP   A CB   1 
ATOM   586  C  CB   B ASP   A 1 22  ? 13.155 3.299   9.544   0.32 16.38 ?  22  ASP   A CB   1 
ATOM   587  C  CG   A ASP   A 1 22  ? 13.791 4.414   9.611   0.68 20.69 ?  22  ASP   A CG   1 
ATOM   588  C  CG   B ASP   A 1 22  ? 14.234 4.167   8.914   0.32 16.66 ?  22  ASP   A CG   1 
ATOM   589  O  OD1  A ASP   A 1 22  ? 14.884 4.026   9.153   0.68 20.95 ?  22  ASP   A OD1  1 
ATOM   590  O  OD1  B ASP   A 1 22  ? 15.215 3.619   8.370   0.32 16.17 ?  22  ASP   A OD1  1 
ATOM   591  O  OD2  A ASP   A 1 22  ? 13.490 5.625   9.693   0.68 22.70 -1 22  ASP   A OD2  1 
ATOM   592  O  OD2  B ASP   A 1 22  ? 14.099 5.409   8.967   0.32 17.47 -1 22  ASP   A OD2  1 
ATOM   593  H  H    A ASP   A 1 22  ? 11.620 1.391   10.820  0.68 21.33 ?  22  ASP   A H    1 
ATOM   594  H  H    B ASP   A 1 22  ? 11.677 1.554   10.286  0.32 18.86 ?  22  ASP   A H    1 
ATOM   595  H  HA   A ASP   A 1 22  ? 13.093 1.959   8.656   0.68 21.18 ?  22  ASP   A HA   1 
ATOM   596  H  HA   B ASP   A 1 22  ? 13.345 1.714   8.226   0.32 18.40 ?  22  ASP   A HA   1 
ATOM   597  H  HB2  A ASP   A 1 22  ? 11.901 3.666   9.780   0.68 23.02 ?  22  ASP   A HB2  1 
ATOM   598  H  HB2  B ASP   A 1 22  ? 12.293 3.620   9.237   0.32 19.65 ?  22  ASP   A HB2  1 
ATOM   599  H  HB3  A ASP   A 1 22  ? 12.779 3.405   11.078  0.68 23.02 ?  22  ASP   A HB3  1 
ATOM   600  H  HB3  B ASP   A 1 22  ? 13.222 3.400   10.507  0.32 19.65 ?  22  ASP   A HB3  1 
ATOM   601  N  N    A ILE   A 1 23  ? 15.290 1.046   9.288   0.68 15.66 ?  23  ILE   A N    1 
ATOM   602  N  N    B ILE   A 1 23  ? 15.507 0.814   9.011   0.32 13.50 ?  23  ILE   A N    1 
ATOM   603  C  CA   A ILE   A 1 23  ? 16.554 0.451   9.718   0.68 14.84 ?  23  ILE   A CA   1 
ATOM   604  C  CA   B ILE   A 1 23  ? 16.732 0.206   9.530   0.32 13.38 ?  23  ILE   A CA   1 
ATOM   605  C  C    A ILE   A 1 23  ? 17.350 1.410   10.593  0.68 14.73 ?  23  ILE   A C    1 
ATOM   606  C  C    B ILE   A 1 23  ? 17.465 1.168   10.454  0.32 14.03 ?  23  ILE   A C    1 
ATOM   607  O  O    A ILE   A 1 23  ? 18.072 0.979   11.500  0.68 15.02 ?  23  ILE   A O    1 
ATOM   608  O  O    B ILE   A 1 23  ? 18.143 0.743   11.397  0.32 14.06 ?  23  ILE   A O    1 
ATOM   609  C  CB   A ILE   A 1 23  ? 17.358 -0.044  8.496   0.68 14.53 ?  23  ILE   A CB   1 
ATOM   610  C  CB   B ILE   A 1 23  ? 17.632 -0.314  8.384   0.32 12.56 ?  23  ILE   A CB   1 
ATOM   611  C  CG1  A ILE   A 1 23  ? 18.529 -0.924  8.944   0.68 14.75 ?  23  ILE   A CG1  1 
ATOM   612  C  CG1  B ILE   A 1 23  ? 18.694 -1.277  8.930   0.32 12.05 ?  23  ILE   A CG1  1 
ATOM   613  C  CG2  A ILE   A 1 23  ? 17.817 1.129   7.629   0.68 14.29 ?  23  ILE   A CG2  1 
ATOM   614  C  CG2  B ILE   A 1 23  ? 18.295 0.838   7.629   0.32 12.28 ?  23  ILE   A CG2  1 
ATOM   615  C  CD1  A ILE   A 1 23  ? 19.232 -1.636  7.803   0.68 14.94 ?  23  ILE   A CD1  1 
ATOM   616  C  CD1  B ILE   A 1 23  ? 19.548 -1.939  7.855   0.32 11.92 ?  23  ILE   A CD1  1 
ATOM   617  H  H    A ILE   A 1 23  ? 15.184 1.079   8.439   0.68 18.79 ?  23  ILE   A H    1 
ATOM   618  H  H    B ILE   A 1 23  ? 15.477 0.869   8.162   0.32 16.19 ?  23  ILE   A H    1 
ATOM   619  H  HA   A ILE   A 1 23  ? 16.356 -0.328  10.258  0.68 17.80 ?  23  ILE   A HA   1 
ATOM   620  H  HA   B ILE   A 1 23  ? 16.481 -0.563  10.058  0.32 16.05 ?  23  ILE   A HA   1 
ATOM   621  H  HB   A ILE   A 1 23  ? 16.769 -0.592  7.958   0.68 17.43 ?  23  ILE   A HB   1 
ATOM   622  H  HB   B ILE   A 1 23  ? 17.079 -0.805  7.758   0.32 15.07 ?  23  ILE   A HB   1 
ATOM   623  H  HG12 A ILE   A 1 23  ? 19.186 -0.372  9.396   0.68 17.69 ?  23  ILE   A HG12 1 
ATOM   624  H  HG12 B ILE   A 1 23  ? 19.292 -0.789  9.518   0.32 14.45 ?  23  ILE   A HG12 1 
ATOM   625  H  HG13 A ILE   A 1 23  ? 18.196 -1.602  9.553   0.68 17.69 ?  23  ILE   A HG13 1 
ATOM   626  H  HG13 B ILE   A 1 23  ? 18.251 -1.983  9.428   0.32 14.45 ?  23  ILE   A HG13 1 
ATOM   627  H  HG21 A ILE   A 1 23  ? 18.190 0.786   6.801   0.68 17.15 ?  23  ILE   A HG21 1 
ATOM   628  H  HG21 B ILE   A 1 23  ? 18.681 0.496   6.803   0.32 14.73 ?  23  ILE   A HG21 1 
ATOM   629  H  HG22 A ILE   A 1 23  ? 17.051 1.695   7.433   0.68 17.15 ?  23  ILE   A HG22 1 
ATOM   630  H  HG22 B ILE   A 1 23  ? 17.626 1.507   7.425   0.32 14.73 ?  23  ILE   A HG22 1 
ATOM   631  H  HG23 A ILE   A 1 23  ? 18.488 1.639   8.108   0.68 17.15 ?  23  ILE   A HG23 1 
ATOM   632  H  HG23 B ILE   A 1 23  ? 18.994 1.223   8.181   0.32 14.73 ?  23  ILE   A HG23 1 
ATOM   633  H  HD11 A ILE   A 1 23  ? 19.916 -2.217  8.169   0.68 17.92 ?  23  ILE   A HD11 1 
ATOM   634  H  HD11 B ILE   A 1 23  ? 20.127 -2.599  8.272   0.32 14.30 ?  23  ILE   A HD11 1 
ATOM   635  H  HD12 A ILE   A 1 23  ? 18.580 -2.160  7.311   0.68 17.92 ?  23  ILE   A HD12 1 
ATOM   636  H  HD12 B ILE   A 1 23  ? 18.965 -2.373  7.212   0.32 14.30 ?  23  ILE   A HD12 1 
ATOM   637  H  HD13 A ILE   A 1 23  ? 19.634 -0.975  7.220   0.68 17.92 ?  23  ILE   A HD13 1 
ATOM   638  H  HD13 B ILE   A 1 23  ? 20.084 -1.263  7.413   0.32 14.30 ?  23  ILE   A HD13 1 
ATOM   639  N  N    A VAL   A 1 24  ? 17.224 2.716   10.354  0.68 15.19 ?  24  VAL   A N    1 
ATOM   640  N  N    B VAL   A 1 24  ? 17.337 2.472   10.207  0.32 15.15 ?  24  VAL   A N    1 
ATOM   641  C  CA   A VAL   A 1 24  ? 17.909 3.695   11.195  0.68 16.20 ?  24  VAL   A CA   1 
ATOM   642  C  CA   B VAL   A 1 24  ? 17.974 3.469   11.063  0.32 16.27 ?  24  VAL   A CA   1 
ATOM   643  C  C    A VAL   A 1 24  ? 17.391 3.617   12.623  0.68 16.65 ?  24  VAL   A C    1 
ATOM   644  C  C    B VAL   A 1 24  ? 17.396 3.410   12.472  0.32 16.85 ?  24  VAL   A C    1 
ATOM   645  O  O    A VAL   A 1 24  ? 18.167 3.549   13.585  0.68 16.96 ?  24  VAL   A O    1 
ATOM   646  O  O    B VAL   A 1 24  ? 18.130 3.436   13.466  0.32 17.22 ?  24  VAL   A O    1 
ATOM   647  C  CB   A VAL   A 1 24  ? 17.746 5.109   10.613  0.68 17.14 ?  24  VAL   A CB   1 
ATOM   648  C  CB   B VAL   A 1 24  ? 17.830 4.869   10.441  0.32 17.37 ?  24  VAL   A CB   1 
ATOM   649  C  CG1  A VAL   A 1 24  ? 18.228 6.162   11.608  0.68 18.23 ?  24  VAL   A CG1  1 
ATOM   650  C  CG1  B VAL   A 1 24  ? 18.414 5.929   11.359  0.32 18.51 ?  24  VAL   A CG1  1 
ATOM   651  C  CG2  A VAL   A 1 24  ? 18.488 5.224   9.293   0.68 18.26 ?  24  VAL   A CG2  1 
ATOM   652  C  CG2  B VAL   A 1 24  ? 18.494 4.904   9.074   0.32 17.72 ?  24  VAL   A CG2  1 
ATOM   653  H  H    A VAL   A 1 24  ? 16.752 3.055   9.723   0.68 18.22 ?  24  VAL   A H    1 
ATOM   654  H  H    B VAL   A 1 24  ? 16.894 2.803   9.553   0.32 18.18 ?  24  VAL   A H    1 
ATOM   655  H  HA   A VAL   A 1 24  ? 18.854 3.489   11.214  0.68 19.44 ?  24  VAL   A HA   1 
ATOM   656  H  HA   B VAL   A 1 24  ? 18.920 3.270   11.130  0.32 19.52 ?  24  VAL   A HA   1 
ATOM   657  H  HB   A VAL   A 1 24  ? 16.806 5.273   10.438  0.68 20.57 ?  24  VAL   A HB   1 
ATOM   658  H  HB   B VAL   A 1 24  ? 16.889 5.063   10.318  0.32 20.84 ?  24  VAL   A HB   1 
ATOM   659  H  HG11 A VAL   A 1 24  ? 18.382 6.992   11.132  0.68 21.87 ?  24  VAL   A HG11 1 
ATOM   660  H  HG11 B VAL   A 1 24  ? 18.503 6.757   10.863  0.32 22.21 ?  24  VAL   A HG11 1 
ATOM   661  H  HG12 A VAL   A 1 24  ? 17.549 6.290   12.287  0.68 21.87 ?  24  VAL   A HG12 1 
ATOM   662  H  HG12 B VAL   A 1 24  ? 17.816 6.059   12.112  0.32 22.21 ?  24  VAL   A HG12 1 
ATOM   663  H  HG13 A VAL   A 1 24  ? 19.054 5.855   12.012  0.68 21.87 ?  24  VAL   A HG13 1 
ATOM   664  H  HG13 B VAL   A 1 24  ? 19.282 5.633   11.669  0.32 22.21 ?  24  VAL   A HG13 1 
ATOM   665  H  HG21 A VAL   A 1 24  ? 18.223 6.045   8.850   0.68 21.90 ?  24  VAL   A HG21 1 
ATOM   666  H  HG21 B VAL   A 1 24  ? 18.511 5.819   8.756   0.32 21.26 ?  24  VAL   A HG21 1 
ATOM   667  H  HG22 A VAL   A 1 24  ? 19.443 5.238   9.467   0.68 21.90 ?  24  VAL   A HG22 1 
ATOM   668  H  HG22 B VAL   A 1 24  ? 19.400 4.565   9.155   0.32 21.26 ?  24  VAL   A HG22 1 
ATOM   669  H  HG23 A VAL   A 1 24  ? 18.266 4.462   8.734   0.68 21.90 ?  24  VAL   A HG23 1 
ATOM   670  H  HG23 B VAL   A 1 24  ? 17.988 4.347   8.461   0.32 21.26 ?  24  VAL   A HG23 1 
ATOM   671  N  N    A GLU   A 1 25  ? 16.067 3.634   12.782  0.68 17.56 ?  25  GLU   A N    1 
ATOM   672  N  N    B GLU   A 1 25  ? 16.067 3.326   12.579  0.32 17.37 ?  25  GLU   A N    1 
ATOM   673  C  CA   A GLU   A 1 25  ? 15.485 3.569   14.118  0.68 19.47 ?  25  GLU   A CA   1 
ATOM   674  C  CA   B GLU   A 1 25  ? 15.440 3.276   13.896  0.32 18.96 ?  25  GLU   A CA   1 
ATOM   675  C  C    A GLU   A 1 25  ? 15.724 2.208   14.759  0.68 18.47 ?  25  GLU   A C    1 
ATOM   676  C  C    B GLU   A 1 25  ? 15.688 1.935   14.577  0.32 18.69 ?  25  GLU   A C    1 
ATOM   677  O  O    A GLU   A 1 25  ? 15.967 2.123   15.968  0.68 19.13 ?  25  GLU   A O    1 
ATOM   678  O  O    B GLU   A 1 25  ? 15.868 1.878   15.799  0.32 19.23 ?  25  GLU   A O    1 
ATOM   679  C  CB   A GLU   A 1 25  ? 13.993 3.910   14.062  0.68 22.57 ?  25  GLU   A CB   1 
ATOM   680  C  CB   B GLU   A 1 25  ? 13.944 3.577   13.785  0.32 20.78 ?  25  GLU   A CB   1 
ATOM   681  C  CG   A GLU   A 1 25  ? 13.722 5.362   13.679  0.68 26.04 ?  25  GLU   A CG   1 
ATOM   682  C  CG   B GLU   A 1 25  ? 13.645 5.004   13.346  0.32 23.20 ?  25  GLU   A CG   1 
ATOM   683  C  CD   A GLU   A 1 25  ? 14.482 6.356   14.549  0.68 28.88 ?  25  GLU   A CD   1 
ATOM   684  C  CD   B GLU   A 1 25  ? 14.249 6.036   14.272  0.32 25.20 ?  25  GLU   A CD   1 
ATOM   685  O  OE1  A GLU   A 1 25  ? 14.517 6.172   15.785  0.68 30.04 ?  25  GLU   A OE1  1 
ATOM   686  O  OE1  B GLU   A 1 25  ? 14.316 5.772   15.493  0.32 26.19 ?  25  GLU   A OE1  1 
ATOM   687  O  OE2  A GLU   A 1 25  ? 15.066 7.309   13.990  0.68 30.00 -1 25  GLU   A OE2  1 
ATOM   688  O  OE2  B GLU   A 1 25  ? 14.663 7.106   13.780  0.32 25.89 -1 25  GLU   A OE2  1 
ATOM   689  H  H    A GLU   A 1 25  ? 15.492 3.691   12.143  0.68 21.07 ?  25  GLU   A H    1 
ATOM   690  H  H    B GLU   A 1 25  ? 15.517 3.301   11.917  0.32 20.84 ?  25  GLU   A H    1 
ATOM   691  H  HA   A GLU   A 1 25  ? 15.915 4.227   14.681  0.68 23.36 ?  25  GLU   A HA   1 
ATOM   692  H  HA   B GLU   A 1 25  ? 15.839 3.959   14.454  0.32 22.74 ?  25  GLU   A HA   1 
ATOM   693  H  HB2  A GLU   A 1 25  ? 13.559 3.346   13.399  0.68 27.08 ?  25  GLU   A HB2  1 
ATOM   694  H  HB2  B GLU   A 1 25  ? 13.546 2.981   13.132  0.32 24.93 ?  25  GLU   A HB2  1 
ATOM   695  H  HB3  A GLU   A 1 25  ? 13.593 3.756   14.933  0.68 27.08 ?  25  GLU   A HB3  1 
ATOM   696  H  HB3  B GLU   A 1 25  ? 13.528 3.442   14.652  0.32 24.93 ?  25  GLU   A HB3  1 
ATOM   697  H  HG2  A GLU   A 1 25  ? 14.007 5.503   12.765  0.68 31.25 ?  25  GLU   A HG2  1 
ATOM   698  H  HG2  B GLU   A 1 25  ? 14.005 5.147   12.457  0.32 27.83 ?  25  GLU   A HG2  1 
ATOM   699  H  HG3  A GLU   A 1 25  ? 12.769 5.536   13.762  0.68 31.25 ?  25  GLU   A HG3  1 
ATOM   700  H  HG3  B GLU   A 1 25  ? 12.688 5.149   13.347  0.32 27.83 ?  25  GLU   A HG3  1 
ATOM   701  N  N    A GLU   A 1 26  ? 15.680 1.135   13.964  0.68 18.08 ?  26  GLU   A N    1 
ATOM   702  N  N    B GLU   A 1 26  ? 15.707 0.845   13.807  0.32 18.17 ?  26  GLU   A N    1 
ATOM   703  C  CA   A GLU   A 1 26  ? 16.005 -0.188  14.491  0.68 18.09 ?  26  GLU   A CA   1 
ATOM   704  C  CA   B GLU   A 1 26  ? 16.056 -0.450  14.382  0.32 18.16 ?  26  GLU   A CA   1 
ATOM   705  C  C    A GLU   A 1 26  ? 17.427 -0.219  15.036  0.68 16.87 ?  26  GLU   A C    1 
ATOM   706  C  C    B GLU   A 1 26  ? 17.484 -0.460  14.904  0.32 17.06 ?  26  GLU   A C    1 
ATOM   707  O  O    A GLU   A 1 26  ? 17.668 -0.681  16.157  0.68 16.59 ?  26  GLU   A O    1 
ATOM   708  O  O    B GLU   A 1 26  ? 17.774 -1.123  15.906  0.32 16.67 ?  26  GLU   A O    1 
ATOM   709  C  CB   A GLU   A 1 26  ? 15.849 -1.245  13.396  0.68 19.81 ?  26  GLU   A CB   1 
ATOM   710  C  CB   B GLU   A 1 26  ? 15.882 -1.554  13.340  0.32 19.24 ?  26  GLU   A CB   1 
ATOM   711  C  CG   A GLU   A 1 26  ? 14.471 -1.857  13.258  0.68 22.33 ?  26  GLU   A CG   1 
ATOM   712  C  CG   B GLU   A 1 26  ? 14.442 -1.921  13.068  0.32 20.14 ?  26  GLU   A CG   1 
ATOM   713  C  CD   A GLU   A 1 26  ? 14.044 -2.663  14.475  0.68 23.11 ?  26  GLU   A CD   1 
ATOM   714  C  CD   B GLU   A 1 26  ? 13.725 -2.425  14.298  0.32 20.27 ?  26  GLU   A CD   1 
ATOM   715  O  OE1  A GLU   A 1 26  ? 14.447 -3.841  14.640  0.68 23.42 ?  26  GLU   A OE1  1 
ATOM   716  O  OE1  B GLU   A 1 26  ? 14.320 -3.225  15.051  0.32 20.64 ?  26  GLU   A OE1  1 
ATOM   717  O  OE2  A GLU   A 1 26  ? 13.288 -2.102  15.277  0.68 23.44 -1 26  GLU   A OE2  1 
ATOM   718  O  OE2  B GLU   A 1 26  ? 12.574 -2.000  14.517  0.32 19.52 -1 26  GLU   A OE2  1 
ATOM   719  H  H    A GLU   A 1 26  ? 15.475 1.154   13.127  0.68 21.70 ?  26  GLU   A H    1 
ATOM   720  H  H    B GLU   A 1 26  ? 15.524 0.829   12.969  0.32 21.80 ?  26  GLU   A H    1 
ATOM   721  H  HA   A GLU   A 1 26  ? 15.397 -0.398  15.212  0.68 21.70 ?  26  GLU   A HA   1 
ATOM   722  H  HA   B GLU   A 1 26  ? 15.469 -0.635  15.129  0.32 21.78 ?  26  GLU   A HA   1 
ATOM   723  H  HB2  A GLU   A 1 26  ? 16.073 -0.835  12.542  0.68 23.76 ?  26  GLU   A HB2  1 
ATOM   724  H  HB2  B GLU   A 1 26  ? 16.276 -1.257  12.503  0.32 23.09 ?  26  GLU   A HB2  1 
ATOM   725  H  HB3  A GLU   A 1 26  ? 16.471 -1.964  13.579  0.68 23.76 ?  26  GLU   A HB3  1 
ATOM   726  H  HB3  B GLU   A 1 26  ? 16.342 -2.351  13.651  0.32 23.09 ?  26  GLU   A HB3  1 
ATOM   727  H  HG2  A GLU   A 1 26  ? 13.830 -1.139  13.117  0.68 26.79 ?  26  GLU   A HG2  1 
ATOM   728  H  HG2  B GLU   A 1 26  ? 13.967 -1.135  12.766  0.32 24.16 ?  26  GLU   A HG2  1 
ATOM   729  H  HG3  A GLU   A 1 26  ? 14.465 -2.460  12.505  0.68 26.79 ?  26  GLU   A HG3  1 
ATOM   730  H  HG3  B GLU   A 1 26  ? 14.414 -2.614  12.393  0.32 24.16 ?  26  GLU   A HG3  1 
ATOM   731  N  N    . ALA   A 1 27  ? 18.388 0.263   14.244  1.00 16.20 ?  27  ALA   A N    1 
ATOM   732  C  CA   . ALA   A 1 27  ? 19.779 0.263   14.682  1.00 16.44 ?  27  ALA   A CA   1 
ATOM   733  C  C    . ALA   A 1 27  ? 19.950 1.064   15.967  1.00 18.61 ?  27  ALA   A C    1 
ATOM   734  O  O    . ALA   A 1 27  ? 20.623 0.618   16.902  1.00 18.66 ?  27  ALA   A O    1 
ATOM   735  C  CB   . ALA   A 1 27  ? 20.681 0.805   13.571  1.00 15.69 ?  27  ALA   A CB   1 
ATOM   736  H  H    A ALA   A 1 27  ? 18.261 0.598   13.461  0.68 19.44 ?  27  ALA   A H    1 
ATOM   737  H  H    B ALA   A 1 27  ? 18.225 0.757   13.557  0.32 19.44 ?  27  ALA   A H    1 
ATOM   738  H  HA   . ALA   A 1 27  ? 20.049 -0.647  14.864  1.00 19.72 ?  27  ALA   A HA   1 
ATOM   739  H  HB1  . ALA   A 1 27  ? 21.604 0.797   13.878  1.00 18.82 ?  27  ALA   A HB1  1 
ATOM   740  H  HB2  . ALA   A 1 27  ? 20.593 0.241   12.786  1.00 18.82 ?  27  ALA   A HB2  1 
ATOM   741  H  HB3  . ALA   A 1 27  ? 20.416 1.713   13.356  1.00 18.82 ?  27  ALA   A HB3  1 
ATOM   742  N  N    A LYS   A 1 28  ? 19.335 2.246   16.042  0.68 20.33 ?  28  LYS   A N    1 
ATOM   743  N  N    B LYS   A 1 28  ? 19.340 2.252   16.034  0.32 20.95 ?  28  LYS   A N    1 
ATOM   744  C  CA   A LYS   A 1 28  ? 19.479 3.065   17.242  0.68 23.63 ?  28  LYS   A CA   1 
ATOM   745  C  CA   B LYS   A 1 28  ? 19.467 3.085   17.226  0.32 24.04 ?  28  LYS   A CA   1 
ATOM   746  C  C    A LYS   A 1 28  ? 18.912 2.372   18.474  0.68 24.63 ?  28  LYS   A C    1 
ATOM   747  C  C    B LYS   A 1 28  ? 18.876 2.405   18.454  0.32 25.29 ?  28  LYS   A C    1 
ATOM   748  O  O    A LYS   A 1 28  ? 19.399 2.597   19.586  0.68 26.36 ?  28  LYS   A O    1 
ATOM   749  O  O    B LYS   A 1 28  ? 19.375 2.597   19.568  0.32 26.02 ?  28  LYS   A O    1 
ATOM   750  C  CB   A LYS   A 1 28  ? 18.844 4.441   17.032  0.68 26.15 ?  28  LYS   A CB   1 
ATOM   751  C  CB   B LYS   A 1 28  ? 18.807 4.448   16.995  0.32 25.90 ?  28  LYS   A CB   1 
ATOM   752  C  CG   A LYS   A 1 28  ? 19.696 5.359   16.172  0.68 28.38 ?  28  LYS   A CG   1 
ATOM   753  C  CG   B LYS   A 1 28  ? 19.600 5.365   16.077  0.32 27.60 ?  28  LYS   A CG   1 
ATOM   754  C  CD   A LYS   A 1 28  ? 19.216 6.797   16.212  0.68 30.88 ?  28  LYS   A CD   1 
ATOM   755  C  CD   B LYS   A 1 28  ? 19.123 6.808   16.150  0.32 29.35 ?  28  LYS   A CD   1 
ATOM   756  C  CE   A LYS   A 1 28  ? 17.904 6.960   15.479  0.68 32.63 ?  28  LYS   A CE   1 
ATOM   757  C  CE   B LYS   A 1 28  ? 17.781 6.996   15.468  0.32 30.58 ?  28  LYS   A CE   1 
ATOM   758  N  NZ   A LYS   A 1 28  ? 17.516 8.394   15.378  0.68 33.91 ?  28  LYS   A NZ   1 
ATOM   759  N  NZ   B LYS   A 1 28  ? 17.426 8.439   15.345  0.32 31.44 ?  28  LYS   A NZ   1 
ATOM   760  H  H    A LYS   A 1 28  ? 18.846 2.590   15.427  0.68 24.39 ?  28  LYS   A H    1 
ATOM   761  H  H    B LYS   A 1 28  ? 18.856 2.592   15.413  0.32 25.14 ?  28  LYS   A H    1 
ATOM   762  H  HA   A LYS   A 1 28  ? 20.422 3.208   17.409  0.68 28.35 ?  28  LYS   A HA   1 
ATOM   763  H  HA   B LYS   A 1 28  ? 20.406 3.242   17.405  0.32 28.84 ?  28  LYS   A HA   1 
ATOM   764  H  HB2  A LYS   A 1 28  ? 17.987 4.333   16.593  0.68 31.38 ?  28  LYS   A HB2  1 
ATOM   765  H  HB2  B LYS   A 1 28  ? 17.936 4.312   16.591  0.32 31.07 ?  28  LYS   A HB2  1 
ATOM   766  H  HB3  A LYS   A 1 28  ? 18.723 4.871   17.894  0.68 31.38 ?  28  LYS   A HB3  1 
ATOM   767  H  HB3  B LYS   A 1 28  ? 18.708 4.900   17.847  0.32 31.07 ?  28  LYS   A HB3  1 
ATOM   768  H  HG2  A LYS   A 1 28  ? 20.611 5.339   16.494  0.68 34.05 ?  28  LYS   A HG2  1 
ATOM   769  H  HG2  B LYS   A 1 28  ? 20.534 5.344   16.336  0.32 33.12 ?  28  LYS   A HG2  1 
ATOM   770  H  HG3  A LYS   A 1 28  ? 19.660 5.056   15.252  0.68 34.05 ?  28  LYS   A HG3  1 
ATOM   771  H  HG3  B LYS   A 1 28  ? 19.501 5.062   15.161  0.32 33.12 ?  28  LYS   A HG3  1 
ATOM   772  H  HD2  A LYS   A 1 28  ? 19.086 7.066   17.135  0.68 37.05 ?  28  LYS   A HD2  1 
ATOM   773  H  HD2  B LYS   A 1 28  ? 19.028 7.067   17.081  0.32 35.21 ?  28  LYS   A HD2  1 
ATOM   774  H  HD3  A LYS   A 1 28  ? 19.876 7.367   15.786  0.68 37.05 ?  28  LYS   A HD3  1 
ATOM   775  H  HD3  B LYS   A 1 28  ? 19.770 7.381   15.709  0.32 35.21 ?  28  LYS   A HD3  1 
ATOM   776  H  HE2  A LYS   A 1 28  ? 17.993 6.603   14.581  0.68 39.15 ?  28  LYS   A HE2  1 
ATOM   777  H  HE2  B LYS   A 1 28  ? 17.820 6.615   14.577  0.32 36.69 ?  28  LYS   A HE2  1 
ATOM   778  H  HE3  A LYS   A 1 28  ? 17.207 6.488   15.961  0.68 39.15 ?  28  LYS   A HE3  1 
ATOM   779  H  HE3  B LYS   A 1 28  ? 17.092 6.557   15.991  0.32 36.69 ?  28  LYS   A HE3  1 
ATOM   780  H  HZ1  A LYS   A 1 28  ? 16.744 8.469   14.944  0.68 40.69 ?  28  LYS   A HZ1  1 
ATOM   781  H  HZ1  B LYS   A 1 28  ? 16.638 8.525   14.942  0.32 37.72 ?  28  LYS   A HZ1  1 
ATOM   782  H  HZ2  A LYS   A 1 28  ? 17.428 8.742   16.192  0.68 40.69 ?  28  LYS   A HZ2  1 
ATOM   783  H  HZ2  B LYS   A 1 28  ? 17.382 8.811   16.152  0.32 37.72 ?  28  LYS   A HZ2  1 
ATOM   784  H  HZ3  A LYS   A 1 28  ? 18.142 8.847   14.936  0.68 40.69 ?  28  LYS   A HZ3  1 
ATOM   785  H  HZ3  B LYS   A 1 28  ? 18.045 8.864   14.865  0.32 37.72 ?  28  LYS   A HZ3  1 
ATOM   786  N  N    A LYS   A 1 29  ? 17.901 1.520   18.300  0.68 25.00 ?  29  LYS   A N    1 
ATOM   787  N  N    B LYS   A 1 29  ? 17.822 1.608   18.273  0.32 26.15 ?  29  LYS   A N    1 
ATOM   788  C  CA   A LYS   A 1 29  ? 17.307 0.819   19.435  0.68 26.51 ?  29  LYS   A CA   1 
ATOM   789  C  CA   B LYS   A 1 29  ? 17.195 0.930   19.403  0.32 27.25 ?  29  LYS   A CA   1 
ATOM   790  C  C    A LYS   A 1 29  ? 18.129 -0.403  19.832  0.68 25.91 ?  29  LYS   A C    1 
ATOM   791  C  C    B LYS   A 1 29  ? 17.974 -0.311  19.817  0.32 26.34 ?  29  LYS   A C    1 
ATOM   792  O  O    A LYS   A 1 29  ? 18.431 -0.600  21.015  0.68 26.94 ?  29  LYS   A O    1 
ATOM   793  O  O    B LYS   A 1 29  ? 18.161 -0.559  21.014  0.32 26.37 ?  29  LYS   A O    1 
ATOM   794  C  CB   A LYS   A 1 29  ? 15.876 0.398   19.095  0.68 29.07 ?  29  LYS   A CB   1 
ATOM   795  C  CB   B LYS   A 1 29  ? 15.765 0.534   19.039  0.32 29.37 ?  29  LYS   A CB   1 
ATOM   796  C  CG   A LYS   A 1 29  ? 15.143 -0.307  20.229  0.68 32.43 ?  29  LYS   A CG   1 
ATOM   797  C  CG   B LYS   A 1 29  ? 14.990 -0.135  20.165  0.32 31.50 ?  29  LYS   A CG   1 
ATOM   798  C  CD   A LYS   A 1 29  ? 14.822 0.652   21.364  0.68 35.45 ?  29  LYS   A CD   1 
ATOM   799  C  CD   B LYS   A 1 29  ? 14.693 0.841   21.289  0.32 33.38 ?  29  LYS   A CD   1 
ATOM   800  C  CE   A LYS   A 1 29  ? 13.981 -0.019  22.439  0.68 37.48 ?  29  LYS   A CE   1 
ATOM   801  C  CE   B LYS   A 1 29  ? 13.843 0.196   22.370  0.32 34.72 ?  29  LYS   A CE   1 
ATOM   802  N  NZ   A LYS   A 1 29  ? 13.550 0.950   23.484  0.68 38.65 ?  29  LYS   A NZ   1 
ATOM   803  N  NZ   B LYS   A 1 29  ? 13.477 1.168   23.435  0.32 35.50 ?  29  LYS   A NZ   1 
ATOM   804  H  H    A LYS   A 1 29  ? 17.542 1.335   17.542  0.68 30.00 ?  29  LYS   A H    1 
ATOM   805  H  H    B LYS   A 1 29  ? 17.455 1.450   17.514  0.32 31.37 ?  29  LYS   A H    1 
ATOM   806  H  HA   A LYS   A 1 29  ? 17.274 1.416   20.198  0.68 31.81 ?  29  LYS   A HA   1 
ATOM   807  H  HA   B LYS   A 1 29  ? 17.165 1.533   20.160  0.32 32.70 ?  29  LYS   A HA   1 
ATOM   808  H  HB2  A LYS   A 1 29  ? 15.366 1.189   18.866  0.68 34.88 ?  29  LYS   A HB2  1 
ATOM   809  H  HB2  B LYS   A 1 29  ? 15.281 1.331   18.782  0.32 35.24 ?  29  LYS   A HB2  1 
ATOM   810  H  HB3  A LYS   A 1 29  ? 15.900 -0.209  18.340  0.68 34.88 ?  29  LYS   A HB3  1 
ATOM   811  H  HB3  B LYS   A 1 29  ? 15.796 -0.088  18.295  0.32 35.24 ?  29  LYS   A HB3  1 
ATOM   812  H  HG2  A LYS   A 1 29  ? 14.308 -0.665  19.892  0.68 38.91 ?  29  LYS   A HG2  1 
ATOM   813  H  HG2  B LYS   A 1 29  ? 14.146 -0.463  19.818  0.32 37.80 ?  29  LYS   A HG2  1 
ATOM   814  H  HG3  A LYS   A 1 29  ? 15.694 -1.024  20.581  0.68 38.91 ?  29  LYS   A HG3  1 
ATOM   815  H  HG3  B LYS   A 1 29  ? 15.509 -0.871  20.529  0.32 37.80 ?  29  LYS   A HG3  1 
ATOM   816  H  HD2  A LYS   A 1 29  ? 15.649 0.955   21.771  0.68 42.53 ?  29  LYS   A HD2  1 
ATOM   817  H  HD2  B LYS   A 1 29  ? 15.526 1.133   21.691  0.32 40.05 ?  29  LYS   A HD2  1 
ATOM   818  H  HD3  A LYS   A 1 29  ? 14.324 1.407   21.014  0.68 42.53 ?  29  LYS   A HD3  1 
ATOM   819  H  HD3  B LYS   A 1 29  ? 14.207 1.602   20.932  0.32 40.05 ?  29  LYS   A HD3  1 
ATOM   820  H  HE2  A LYS   A 1 29  ? 13.187 -0.401  22.032  0.68 44.97 ?  29  LYS   A HE2  1 
ATOM   821  H  HE2  B LYS   A 1 29  ? 13.025 -0.143  21.973  0.32 41.66 ?  29  LYS   A HE2  1 
ATOM   822  H  HE3  A LYS   A 1 29  ? 14.505 -0.715  22.867  0.68 44.97 ?  29  LYS   A HE3  1 
ATOM   823  H  HE3  B LYS   A 1 29  ? 14.342 -0.529  22.778  0.32 41.66 ?  29  LYS   A HE3  1 
ATOM   824  H  HZ1  A LYS   A 1 29  ? 13.060 0.535   24.100  0.68 46.38 ?  29  LYS   A HZ1  1 
ATOM   825  H  HZ1  B LYS   A 1 29  ? 12.981 0.767   24.054  0.32 42.59 ?  29  LYS   A HZ1  1 
ATOM   826  H  HZ2  A LYS   A 1 29  ? 14.263 1.311   23.876  0.68 46.38 ?  29  LYS   A HZ2  1 
ATOM   827  H  HZ2  B LYS   A 1 29  ? 14.213 1.491   23.817  0.32 42.59 ?  29  LYS   A HZ2  1 
ATOM   828  H  HZ3  A LYS   A 1 29  ? 13.063 1.598   23.115  0.68 46.38 ?  29  LYS   A HZ3  1 
ATOM   829  H  HZ3  B LYS   A 1 29  ? 13.013 1.842   23.084  0.32 42.59 ?  29  LYS   A HZ3  1 
ATOM   830  N  N    A VAL   A 1 30  ? 18.471 -1.248  18.858  0.68 24.46 ?  30  VAL   A N    1 
ATOM   831  N  N    B VAL   A 1 30  ? 18.421 -1.105  18.848  0.32 25.47 ?  30  VAL   A N    1 
ATOM   832  C  CA   A VAL   A 1 30  ? 19.135 -2.512  19.159  0.68 23.62 ?  30  VAL   A CA   1 
ATOM   833  C  CA   B VAL   A 1 30  ? 19.049 -2.383  19.158  0.32 24.92 ?  30  VAL   A CA   1 
ATOM   834  C  C    A VAL   A 1 30  ? 20.632 -2.328  19.376  0.68 22.14 ?  30  VAL   A C    1 
ATOM   835  C  C    B VAL   A 1 30  ? 20.553 -2.248  19.373  0.32 24.20 ?  30  VAL   A C    1 
ATOM   836  O  O    A VAL   A 1 30  ? 21.239 -3.049  20.175  0.68 22.53 ?  30  VAL   A O    1 
ATOM   837  O  O    B VAL   A 1 30  ? 21.127 -2.966  20.197  0.32 24.17 ?  30  VAL   A O    1 
ATOM   838  C  CB   A VAL   A 1 30  ? 18.849 -3.524  18.034  0.68 24.41 ?  30  VAL   A CB   1 
ATOM   839  C  CB   B VAL   A 1 30  ? 18.740 -3.398  18.044  0.32 25.14 ?  30  VAL   A CB   1 
ATOM   840  C  CG1  A VAL   A 1 30  ? 19.646 -4.809  18.240  0.68 24.73 ?  30  VAL   A CG1  1 
ATOM   841  C  CG1  B VAL   A 1 30  ? 19.488 -4.702  18.284  0.32 25.26 ?  30  VAL   A CG1  1 
ATOM   842  C  CG2  A VAL   A 1 30  ? 17.358 -3.822  17.953  0.68 25.40 ?  30  VAL   A CG2  1 
ATOM   843  C  CG2  B VAL   A 1 30  ? 17.242 -3.640  17.947  0.32 25.49 ?  30  VAL   A CG2  1 
ATOM   844  H  H    A VAL   A 1 30  ? 18.316 -1.122  18.022  0.68 29.35 ?  30  VAL   A H    1 
ATOM   845  H  H    B VAL   A 1 30  ? 18.376 -0.926  18.006  0.32 30.55 ?  30  VAL   A H    1 
ATOM   846  H  HA   A VAL   A 1 30  ? 18.759 -2.875  19.975  0.68 28.34 ?  30  VAL   A HA   1 
ATOM   847  H  HA   B VAL   A 1 30  ? 18.656 -2.723  19.976  0.32 29.90 ?  30  VAL   A HA   1 
ATOM   848  H  HB   A VAL   A 1 30  ? 19.123 -3.142  17.187  0.68 29.29 ?  30  VAL   A HB   1 
ATOM   849  H  HB   B VAL   A 1 30  ? 19.041 -3.039  17.195  0.32 30.16 ?  30  VAL   A HB   1 
ATOM   850  H  HG11 A VAL   A 1 30  ? 19.282 -5.501  17.662  0.68 29.67 ?  30  VAL   A HG11 1 
ATOM   851  H  HG11 B VAL   A 1 30  ? 19.107 -5.392  17.718  0.32 30.31 ?  30  VAL   A HG11 1 
ATOM   852  H  HG12 A VAL   A 1 30  ? 20.575 -4.649  18.014  0.68 29.67 ?  30  VAL   A HG12 1 
ATOM   853  H  HG12 B VAL   A 1 30  ? 20.425 -4.577  18.063  0.32 30.31 ?  30  VAL   A HG12 1 
ATOM   854  H  HG13 A VAL   A 1 30  ? 19.569 -5.084  19.167  0.68 29.67 ?  30  VAL   A HG13 1 
ATOM   855  H  HG13 B VAL   A 1 30  ? 19.396 -4.951  19.216  0.32 30.31 ?  30  VAL   A HG13 1 
ATOM   856  H  HG21 A VAL   A 1 30  ? 17.207 -4.492  17.268  0.68 30.47 ?  30  VAL   A HG21 1 
ATOM   857  H  HG21 B VAL   A 1 30  ? 17.073 -4.313  17.269  0.32 30.59 ?  30  VAL   A HG21 1 
ATOM   858  H  HG22 A VAL   A 1 30  ? 17.056 -4.155  18.813  0.68 30.47 ?  30  VAL   A HG22 1 
ATOM   859  H  HG22 B VAL   A 1 30  ? 16.917 -3.947  18.807  0.32 30.59 ?  30  VAL   A HG22 1 
ATOM   860  H  HG23 A VAL   A 1 30  ? 16.887 -3.006  17.728  0.68 30.47 ?  30  VAL   A HG23 1 
ATOM   861  H  HG23 B VAL   A 1 30  ? 16.806 -2.809  17.705  0.32 30.59 ?  30  VAL   A HG23 1 
ATOM   862  N  N    A LYS   A 1 31  ? 21.249 -1.376  18.684  0.68 20.97 ?  31  LYS   A N    1 
ATOM   863  N  N    B LYS   A 1 31  ? 21.198 -1.339  18.653  0.32 23.61 ?  31  LYS   A N    1 
ATOM   864  C  CA   A LYS   A 1 31  ? 22.700 -1.253  18.619  0.68 21.44 ?  31  LYS   A CA   1 
ATOM   865  C  CA   B LYS   A 1 31  ? 22.652 -1.249  18.599  0.32 23.56 ?  31  LYS   A CA   1 
ATOM   866  C  C    A LYS   A 1 31  ? 23.319 -2.610  18.272  0.68 19.35 ?  31  LYS   A C    1 
ATOM   867  C  C    B LYS   A 1 31  ? 23.261 -2.620  18.292  0.32 20.84 ?  31  LYS   A C    1 
ATOM   868  O  O    A LYS   A 1 31  ? 24.108 -3.158  19.048  0.68 20.40 ?  31  LYS   A O    1 
ATOM   869  O  O    B LYS   A 1 31  ? 23.991 -3.183  19.113  0.32 21.48 ?  31  LYS   A O    1 
ATOM   870  C  CB   A LYS   A 1 31  ? 23.285 -0.703  19.913  0.68 25.93 ?  31  LYS   A CB   1 
ATOM   871  C  CB   B LYS   A 1 31  ? 23.239 -0.660  19.874  0.32 26.58 ?  31  LYS   A CB   1 
ATOM   872  C  CG   A LYS   A 1 31  ? 22.587 0.537   20.433  0.68 31.02 ?  31  LYS   A CG   1 
ATOM   873  C  CG   B LYS   A 1 31  ? 22.569 0.629   20.318  0.32 29.72 ?  31  LYS   A CG   1 
ATOM   874  C  CD   A LYS   A 1 31  ? 23.587 1.613   20.826  0.68 34.73 ?  31  LYS   A CD   1 
ATOM   875  C  CD   B LYS   A 1 31  ? 23.558 1.571   20.983  0.32 32.16 ?  31  LYS   A CD   1 
ATOM   876  C  CE   A LYS   A 1 31  ? 22.959 2.645   21.750  0.68 37.08 ?  31  LYS   A CE   1 
ATOM   877  C  CE   B LYS   A 1 31  ? 22.848 2.631   21.809  0.32 33.72 ?  31  LYS   A CE   1 
ATOM   878  N  NZ   A LYS   A 1 31  ? 21.721 3.243   21.179  0.68 38.36 ?  31  LYS   A NZ   1 
ATOM   879  N  NZ   B LYS   A 1 31  ? 21.776 3.327   21.045  0.32 34.64 ?  31  LYS   A NZ   1 
ATOM   880  H  H    A LYS   A 1 31  ? 20.834 -0.775  18.231  0.68 25.16 ?  31  LYS   A H    1 
ATOM   881  H  H    B LYS   A 1 31  ? 20.799 -0.755  18.169  0.32 28.33 ?  31  LYS   A H    1 
ATOM   882  H  HA   A LYS   A 1 31  ? 22.923 -0.633  17.910  0.68 25.72 ?  31  LYS   A HA   1 
ATOM   883  H  HA   B LYS   A 1 31  ? 22.882 -0.654  17.879  0.32 28.26 ?  31  LYS   A HA   1 
ATOM   884  H  HB2  A LYS   A 1 31  ? 23.228 -1.387  20.595  0.68 31.11 ?  31  LYS   A HB2  1 
ATOM   885  H  HB2  B LYS   A 1 31  ? 23.146 -1.306  20.584  0.32 31.89 ?  31  LYS   A HB2  1 
ATOM   886  H  HB3  A LYS   A 1 31  ? 24.217 -0.475  19.756  0.68 31.11 ?  31  LYS   A HB3  1 
ATOM   887  H  HB3  B LYS   A 1 31  ? 24.180 -0.469  19.723  0.32 31.89 ?  31  LYS   A HB3  1 
ATOM   888  H  HG2  A LYS   A 1 31  ? 22.010 0.896   19.741  0.68 37.21 ?  31  LYS   A HG2  1 
ATOM   889  H  HG2  B LYS   A 1 31  ? 22.194 1.079   19.544  0.32 35.65 ?  31  LYS   A HG2  1 
ATOM   890  H  HG3  A LYS   A 1 31  ? 22.065 0.305   21.218  0.68 37.21 ?  31  LYS   A HG3  1 
ATOM   891  H  HG3  B LYS   A 1 31  ? 21.870 0.423   20.958  0.32 35.65 ?  31  LYS   A HG3  1 
ATOM   892  H  HD2  A LYS   A 1 31  ? 24.334 1.203   21.290  0.68 41.67 ?  31  LYS   A HD2  1 
ATOM   893  H  HD2  B LYS   A 1 31  ? 24.137 1.063   21.571  0.32 38.59 ?  31  LYS   A HD2  1 
ATOM   894  H  HD3  A LYS   A 1 31  ? 23.898 2.069   20.027  0.68 41.67 ?  31  LYS   A HD3  1 
ATOM   895  H  HD3  B LYS   A 1 31  ? 24.082 2.018   20.299  0.32 38.59 ?  31  LYS   A HD3  1 
ATOM   896  H  HE2  A LYS   A 1 31  ? 22.727 2.217   22.589  0.68 44.50 ?  31  LYS   A HE2  1 
ATOM   897  H  HE2  B LYS   A 1 31  ? 22.442 2.209   22.582  0.32 40.46 ?  31  LYS   A HE2  1 
ATOM   898  H  HE3  A LYS   A 1 31  ? 23.595 3.360   21.906  0.68 44.50 ?  31  LYS   A HE3  1 
ATOM   899  H  HE3  B LYS   A 1 31  ? 23.494 3.296   22.094  0.32 40.46 ?  31  LYS   A HE3  1 
ATOM   900  H  HZ1  A LYS   A 1 31  ? 21.398 3.860   21.734  0.68 46.02 ?  31  LYS   A HZ1  1 
ATOM   901  H  HZ1  B LYS   A 1 31  ? 21.416 3.970   21.545  0.32 41.56 ?  31  LYS   A HZ1  1 
ATOM   902  H  HZ2  A LYS   A 1 31  ? 21.902 3.625   20.396  0.68 46.02 ?  31  LYS   A HZ2  1 
ATOM   903  H  HZ2  B LYS   A 1 31  ? 22.114 3.690   20.307  0.32 41.56 ?  31  LYS   A HZ2  1 
ATOM   904  H  HZ3  A LYS   A 1 31  ? 21.105 2.612   21.058  0.68 46.02 ?  31  LYS   A HZ3  1 
ATOM   905  H  HZ3  B LYS   A 1 31  ? 21.139 2.748   20.818  0.32 41.56 ?  31  LYS   A HZ3  1 
ATOM   906  N  N    . PRO   A 1 32  ? 22.976 -3.176  17.118  1.00 18.08 ?  32  PRO   A N    1 
ATOM   907  C  CA   . PRO   A 1 32  ? 23.457 -4.517  16.792  1.00 18.08 ?  32  PRO   A CA   1 
ATOM   908  C  C    . PRO   A 1 32  ? 24.959 -4.530  16.582  1.00 17.91 ?  32  PRO   A C    1 
ATOM   909  O  O    . PRO   A 1 32  ? 25.598 -3.501  16.355  1.00 17.79 ?  32  PRO   A O    1 
ATOM   910  C  CB   . PRO   A 1 32  ? 22.728 -4.827  15.481  1.00 18.19 ?  32  PRO   A CB   1 
ATOM   911  C  CG   . PRO   A 1 32  ? 22.557 -3.473  14.846  1.00 16.76 ?  32  PRO   A CG   1 
ATOM   912  C  CD   . PRO   A 1 32  ? 22.247 -2.563  15.997  1.00 16.90 ?  32  PRO   A CD   1 
ATOM   913  H  HA   . PRO   A 1 32  ? 23.203 -5.158  17.473  1.00 21.69 ?  32  PRO   A HA   1 
ATOM   914  H  HB2  . PRO   A 1 32  ? 23.275 -5.408  14.924  1.00 21.82 ?  32  PRO   A HB2  1 
ATOM   915  H  HB3  . PRO   A 1 32  ? 21.867 -5.239  15.665  1.00 21.82 ?  32  PRO   A HB3  1 
ATOM   916  H  HG2  . PRO   A 1 32  ? 23.378 -3.218  14.402  1.00 20.10 ?  32  PRO   A HG2  1 
ATOM   917  H  HG3  . PRO   A 1 32  ? 21.818 -3.506  14.213  1.00 20.10 ?  32  PRO   A HG3  1 
ATOM   918  H  HD2  . PRO   A 1 32  ? 22.587 -1.674  15.804  1.00 20.28 ?  32  PRO   A HD2  1 
ATOM   919  H  HD3  . PRO   A 1 32  ? 21.295 -2.555  16.164  1.00 20.28 ?  32  PRO   A HD3  1 
ATOM   920  N  N    . THR   A 1 33  ? 25.518 -5.738  16.629  1.00 17.39 ?  33  THR   A N    1 
ATOM   921  C  CA   . THR   A 1 33  ? 26.929 -5.898  16.306  1.00 17.77 ?  33  THR   A CA   1 
ATOM   922  C  C    . THR   A 1 33  ? 27.222 -5.450  14.879  1.00 16.08 ?  33  THR   A C    1 
ATOM   923  O  O    . THR   A 1 33  ? 28.251 -4.810  14.623  1.00 16.57 ?  33  THR   A O    1 
ATOM   924  C  CB   . THR   A 1 33  ? 27.349 -7.352  16.519  1.00 19.77 ?  33  THR   A CB   1 
ATOM   925  O  OG1  . THR   A 1 33  ? 27.053 -7.736  17.865  1.00 21.49 ?  33  THR   A OG1  1 
ATOM   926  C  CG2  . THR   A 1 33  ? 28.838 -7.526  16.263  1.00 20.60 ?  33  THR   A CG2  1 
ATOM   927  H  H    . THR   A 1 33  ? 25.107 -6.467  16.837  1.00 20.86 ?  33  THR   A H    1 
ATOM   928  H  HA   . THR   A 1 33  ? 27.452 -5.348  16.912  1.00 21.32 ?  33  THR   A HA   1 
ATOM   929  H  HB   . THR   A 1 33  ? 26.862 -7.929  15.908  1.00 23.72 ?  33  THR   A HB   1 
ATOM   930  H  HG1  . THR   A 1 33  ? 27.486 -7.255  18.406  1.00 25.79 ?  33  THR   A HG1  1 
ATOM   931  H  HG21 . THR   A 1 33  ? 29.126 -8.403  16.559  1.00 24.72 ?  33  THR   A HG21 1 
ATOM   932  H  HG22 . THR   A 1 33  ? 29.026 -7.437  15.316  1.00 24.72 ?  33  THR   A HG22 1 
ATOM   933  H  HG23 . THR   A 1 33  ? 29.337 -6.851  16.749  1.00 24.72 ?  33  THR   A HG23 1 
ATOM   934  N  N    . VAL   A 1 34  ? 26.330 -5.774  13.940  1.00 14.42 ?  34  VAL   A N    1 
ATOM   935  C  CA   . VAL   A 1 34  ? 26.520 -5.449  12.529  1.00 13.52 ?  34  VAL   A CA   1 
ATOM   936  C  C    . VAL   A 1 34  ? 25.220 -4.896  11.963  1.00 12.60 ?  34  VAL   A C    1 
ATOM   937  O  O    . VAL   A 1 34  ? 24.181 -5.567  12.019  1.00 13.40 ?  34  VAL   A O    1 
ATOM   938  C  CB   . VAL   A 1 34  ? 26.973 -6.661  11.691  1.00 13.88 ?  34  VAL   A CB   1 
ATOM   939  C  CG1  . VAL   A 1 34  ? 27.158 -6.256  10.235  1.00 14.21 ?  34  VAL   A CG1  1 
ATOM   940  C  CG2  . VAL   A 1 34  ? 28.258 -7.274  12.251  1.00 15.33 ?  34  VAL   A CG2  1 
ATOM   941  H  H    . VAL   A 1 34  ? 25.597 -6.195  14.102  1.00 17.30 ?  34  VAL   A H    1 
ATOM   942  H  HA   . VAL   A 1 34  ? 27.198 -4.760  12.450  1.00 16.22 ?  34  VAL   A HA   1 
ATOM   943  H  HB   . VAL   A 1 34  ? 26.283 -7.341  11.728  1.00 16.65 ?  34  VAL   A HB   1 
ATOM   944  H  HG11 . VAL   A 1 34  ? 27.657 -6.951  9.779   1.00 17.05 ?  34  VAL   A HG11 1 
ATOM   945  H  HG12 . VAL   A 1 34  ? 26.290 -6.146  9.823   1.00 17.05 ?  34  VAL   A HG12 1 
ATOM   946  H  HG13 . VAL   A 1 34  ? 27.653 -5.421  10.202  1.00 17.05 ?  34  VAL   A HG13 1 
ATOM   947  H  HG21 . VAL   A 1 34  ? 28.526 -8.016  11.686  1.00 18.39 ?  34  VAL   A HG21 1 
ATOM   948  H  HG22 . VAL   A 1 34  ? 28.953 -6.598  12.261  1.00 18.39 ?  34  VAL   A HG22 1 
ATOM   949  H  HG23 . VAL   A 1 34  ? 28.093 -7.591  13.154  1.00 18.39 ?  34  VAL   A HG23 1 
ATOM   950  N  N    . VAL   A 1 35  ? 25.279 -3.688  11.401  1.00 11.95 ?  35  VAL   A N    1 
ATOM   951  C  CA   . VAL   A 1 35  ? 24.243 -3.174  10.514  1.00 11.42 ?  35  VAL   A CA   1 
ATOM   952  C  C    . VAL   A 1 35  ? 24.794 -3.173  9.095   1.00 11.23 ?  35  VAL   A C    1 
ATOM   953  O  O    . VAL   A 1 35  ? 25.943 -2.775  8.864   1.00 11.78 ?  35  VAL   A O    1 
ATOM   954  C  CB   . VAL   A 1 35  ? 23.722 -1.779  10.929  1.00 12.32 ?  35  VAL   A CB   1 
ATOM   955  C  CG1  . VAL   A 1 35  ? 24.789 -0.687  10.799  1.00 12.75 ?  35  VAL   A CG1  1 
ATOM   956  C  CG2  . VAL   A 1 35  ? 22.479 -1.415  10.107  1.00 12.99 ?  35  VAL   A CG2  1 
ATOM   957  H  H    . VAL   A 1 35  ? 25.929 -3.135  11.520  1.00 14.33 ?  35  VAL   A H    1 
ATOM   958  H  HA   . VAL   A 1 35  ? 23.488 -3.785  10.535  1.00 13.70 ?  35  VAL   A HA   1 
ATOM   959  H  HB   . VAL   A 1 35  ? 23.447 -1.815  11.853  1.00 14.78 ?  35  VAL   A HB   1 
ATOM   960  H  HG11 . VAL   A 1 35  ? 24.440 0.141   11.166  1.00 15.29 ?  35  VAL   A HG11 1 
ATOM   961  H  HG12 . VAL   A 1 35  ? 25.578 -0.961  11.291  1.00 15.29 ?  35  VAL   A HG12 1 
ATOM   962  H  HG13 . VAL   A 1 35  ? 25.011 -0.564  9.862   1.00 15.29 ?  35  VAL   A HG13 1 
ATOM   963  H  HG21 . VAL   A 1 35  ? 22.132 -0.568  10.417  1.00 15.59 ?  35  VAL   A HG21 1 
ATOM   964  H  HG22 . VAL   A 1 35  ? 22.728 -1.347  9.168   1.00 15.59 ?  35  VAL   A HG22 1 
ATOM   965  H  HG23 . VAL   A 1 35  ? 21.812 -2.111  10.218  1.00 15.59 ?  35  VAL   A HG23 1 
ATOM   966  N  N    . VAL   A 1 36  ? 23.976 -3.631  8.146   1.00 10.30 ?  36  VAL   A N    1 
ATOM   967  C  CA   . VAL   A 1 36  ? 24.344 -3.646  6.738   1.00 10.42 ?  36  VAL   A CA   1 
ATOM   968  C  C    . VAL   A 1 36  ? 23.885 -2.355  6.076   1.00 10.35 ?  36  VAL   A C    1 
ATOM   969  O  O    . VAL   A 1 36  ? 22.723 -1.952  6.215   1.00 11.15 ?  36  VAL   A O    1 
ATOM   970  C  CB   . VAL   A 1 36  ? 23.734 -4.859  6.022   1.00 10.20 ?  36  VAL   A CB   1 
ATOM   971  C  CG1  . VAL   A 1 36  ? 23.990 -4.787  4.535   1.00 11.10 ?  36  VAL   A CG1  1 
ATOM   972  C  CG2  . VAL   A 1 36  ? 24.290 -6.156  6.599   1.00 11.47 ?  36  VAL   A CG2  1 
ATOM   973  H  H    . VAL   A 1 36  ? 23.185 -3.951  8.299   1.00 12.35 ?  36  VAL   A H    1 
ATOM   974  H  HA   . VAL   A 1 36  ? 25.313 -3.707  6.662   1.00 12.50 ?  36  VAL   A HA   1 
ATOM   975  H  HB   . VAL   A 1 36  ? 22.776 -4.853  6.157   1.00 12.23 ?  36  VAL   A HB   1 
ATOM   976  H  HG11 . VAL   A 1 36  ? 23.847 -5.665  4.148   1.00 13.31 ?  36  VAL   A HG11 1 
ATOM   977  H  HG12 . VAL   A 1 36  ? 23.375 -4.149  4.135   1.00 13.31 ?  36  VAL   A HG12 1 
ATOM   978  H  HG13 . VAL   A 1 36  ? 24.905 -4.505  4.383   1.00 13.31 ?  36  VAL   A HG13 1 
ATOM   979  H  HG21 . VAL   A 1 36  ? 23.895 -6.909  6.123   1.00 13.76 ?  36  VAL   A HG21 1 
ATOM   980  H  HG22 . VAL   A 1 36  ? 25.252 -6.170  6.491   1.00 13.76 ?  36  VAL   A HG22 1 
ATOM   981  H  HG23 . VAL   A 1 36  ? 24.060 -6.210  7.540   1.00 13.76 ?  36  VAL   A HG23 1 
ATOM   982  N  N    . ASN   A 1 37  ? 24.797 -1.726  5.332   1.00 10.13 ?  37  ASN   A N    1 
ATOM   983  C  CA   . ASN   A 1 37  ? 24.470 -0.604  4.465   1.00 10.06 ?  37  ASN   A CA   1 
ATOM   984  C  C    . ASN   A 1 37  ? 24.332 -1.082  3.031   1.00 9.81  ?  37  ASN   A C    1 
ATOM   985  O  O    . ASN   A 1 37  ? 25.124 -1.905  2.553   1.00 10.53 ?  37  ASN   A O    1 
ATOM   986  C  CB   . ASN   A 1 37  ? 25.554 0.468   4.535   1.00 10.19 ?  37  ASN   A CB   1 
ATOM   987  C  CG   . ASN   A 1 37  ? 25.227 1.667   3.684   1.00 10.51 ?  37  ASN   A CG   1 
ATOM   988  O  OD1  . ASN   A 1 37  ? 24.054 2.005   3.503   1.00 11.24 ?  37  ASN   A OD1  1 
ATOM   989  N  ND2  . ASN   A 1 37  ? 26.256 2.321   3.157   1.00 10.82 ?  37  ASN   A ND2  1 
ATOM   990  H  H    . ASN   A 1 37  ? 25.636 -1.928  5.333   1.00 12.15 ?  37  ASN   A H    1 
ATOM   991  H  HA   . ASN   A 1 37  ? 23.634 -0.207  4.754   1.00 12.07 ?  37  ASN   A HA   1 
ATOM   992  H  HB2  . ASN   A 1 37  ? 25.650 0.768   5.458   1.00 12.22 ?  37  ASN   A HB2  1 
ATOM   993  H  HB3  . ASN   A 1 37  ? 26.395 0.094   4.225   1.00 12.22 ?  37  ASN   A HB3  1 
ATOM   994  H  HD21 . ASN   A 1 37  ? 26.117 3.011   2.660   1.00 12.97 ?  37  ASN   A HD21 1 
ATOM   995  H  HD22 . ASN   A 1 37  ? 27.055 2.061   3.305   1.00 12.97 ?  37  ASN   A HD22 1 
ATOM   996  N  N    . ALA   A 1 38  ? 23.319 -0.543  2.346   1.00 10.32 ?  38  ALA   A N    1 
ATOM   997  C  CA   . ALA   A 1 38  ? 23.127 -0.718  0.908   1.00 10.37 ?  38  ALA   A CA   1 
ATOM   998  C  C    . ALA   A 1 38  ? 24.024 0.287   0.180   1.00 10.45 ?  38  ALA   A C    1 
ATOM   999  O  O    . ALA   A 1 38  ? 23.600 1.366   -0.243  1.00 10.66 ?  38  ALA   A O    1 
ATOM   1000 C  CB   . ALA   A 1 38  ? 21.659 -0.538  0.543   1.00 12.24 ?  38  ALA   A CB   1 
ATOM   1001 H  H    . ALA   A 1 38  ? 22.720 -0.041  2.713   1.00 12.37 ?  38  ALA   A H    1 
ATOM   1002 H  HA   . ALA   A 1 38  ? 23.402 -1.613  0.660   1.00 12.44 ?  38  ALA   A HA   1 
ATOM   1003 H  HB1  . ALA   A 1 38  ? 21.545 -0.729  -0.401  1.00 14.68 ?  38  ALA   A HB1  1 
ATOM   1004 H  HB2  . ALA   A 1 38  ? 21.124 -1.156  1.071   1.00 14.68 ?  38  ALA   A HB2  1 
ATOM   1005 H  HB3  . ALA   A 1 38  ? 21.394 0.372   0.733   1.00 14.68 ?  38  ALA   A HB3  1 
ATOM   1006 N  N    . ALA   A 1 39  ? 25.298 -0.079  0.042   1.00 10.59 ?  39  ALA   A N    1 
ATOM   1007 C  CA   . ALA   A 1 39  ? 26.335 0.811   -0.449  1.00 10.57 ?  39  ALA   A CA   1 
ATOM   1008 C  C    . ALA   A 1 39  ? 26.452 0.748   -1.965  1.00 10.38 ?  39  ALA   A C    1 
ATOM   1009 O  O    . ALA   A 1 39  ? 25.971 -0.182  -2.615  1.00 10.93 ?  39  ALA   A O    1 
ATOM   1010 C  CB   . ALA   A 1 39  ? 27.667 0.430   0.196   1.00 11.33 ?  39  ALA   A CB   1 
ATOM   1011 H  H    . ALA   A 1 39  ? 25.584 -0.873  0.231   1.00 12.70 ?  39  ALA   A H    1 
ATOM   1012 H  HA   . ALA   A 1 39  ? 26.111 1.722   -0.193  1.00 12.68 ?  39  ALA   A HA   1 
ATOM   1013 H  HB1  . ALA   A 1 39  ? 28.350 1.034   -0.131  1.00 13.59 ?  39  ALA   A HB1  1 
ATOM   1014 H  HB2  . ALA   A 1 39  ? 27.582 0.519   1.161   1.00 13.59 ?  39  ALA   A HB2  1 
ATOM   1015 H  HB3  . ALA   A 1 39  ? 27.879 -0.481  -0.038  1.00 13.59 ?  39  ALA   A HB3  1 
ATOM   1016 N  N    . ASN   A 1 40  ? 27.106 1.765   -2.526  1.00 11.05 ?  40  ASN   A N    1 
ATOM   1017 C  CA   . ASN   A 1 40  ? 27.630 1.715   -3.884  1.00 10.95 ?  40  ASN   A CA   1 
ATOM   1018 C  C    . ASN   A 1 40  ? 29.157 1.608   -3.839  1.00 10.72 ?  40  ASN   A C    1 
ATOM   1019 O  O    . ASN   A 1 40  ? 29.768 1.705   -2.774  1.00 10.87 ?  40  ASN   A O    1 
ATOM   1020 C  CB   . ASN   A 1 40  ? 27.144 2.904   -4.730  1.00 11.91 ?  40  ASN   A CB   1 
ATOM   1021 C  CG   . ASN   A 1 40  ? 27.524 4.247   -4.143  1.00 13.02 ?  40  ASN   A CG   1 
ATOM   1022 O  OD1  . ASN   A 1 40  ? 28.702 4.514   -3.875  1.00 13.65 ?  40  ASN   A OD1  1 
ATOM   1023 N  ND2  . ASN   A 1 40  ? 26.524 5.108   -3.947  1.00 14.08 ?  40  ASN   A ND2  1 
ATOM   1024 H  H    . ASN   A 1 40  ? 27.268 2.506   -2.127  1.00 13.25 ?  40  ASN   A H    1 
ATOM   1025 H  HA   . ASN   A 1 40  ? 27.296 0.906   -4.310  1.00 13.13 ?  40  ASN   A HA   1 
ATOM   1026 H  HB2  . ASN   A 1 40  ? 27.541 2.838   -5.616  1.00 14.29 ?  40  ASN   A HB2  1 
ATOM   1027 H  HB3  . ASN   A 1 40  ? 26.178 2.866   -4.801  1.00 14.29 ?  40  ASN   A HB3  1 
ATOM   1028 H  HD21 . ASN   A 1 40  ? 26.685 5.888   -3.620  1.00 16.90 ?  40  ASN   A HD21 1 
ATOM   1029 H  HD22 . ASN   A 1 40  ? 25.716 4.885   -4.145  1.00 16.90 ?  40  ASN   A HD22 1 
ATOM   1030 N  N    . VAL   A 1 41  ? 29.765 1.367   -5.004  1.00 11.39 ?  41  VAL   A N    1 
ATOM   1031 C  CA   . VAL   A 1 41  ? 31.194 1.059   -5.040  1.00 11.73 ?  41  VAL   A CA   1 
ATOM   1032 C  C    . VAL   A 1 41  ? 32.057 2.208   -4.561  1.00 11.62 ?  41  VAL   A C    1 
ATOM   1033 O  O    . VAL   A 1 41  ? 33.203 1.983   -4.152  1.00 12.36 ?  41  VAL   A O    1 
ATOM   1034 C  CB   . VAL   A 1 41  ? 31.676 0.577   -6.428  1.00 13.01 ?  41  VAL   A CB   1 
ATOM   1035 C  CG1  . VAL   A 1 41  ? 30.985 -0.717  -6.825  1.00 14.03 ?  41  VAL   A CG1  1 
ATOM   1036 C  CG2  . VAL   A 1 41  ? 31.500 1.654   -7.493  1.00 13.67 ?  41  VAL   A CG2  1 
ATOM   1037 H  H    . VAL   A 1 41  ? 29.377 1.364   -5.772  1.00 13.66 ?  41  VAL   A H    1 
ATOM   1038 H  HA   . VAL   A 1 41  ? 31.352 0.321   -4.428  1.00 14.07 ?  41  VAL   A HA   1 
ATOM   1039 H  HB   . VAL   A 1 41  ? 32.627 0.379   -6.372  1.00 15.60 ?  41  VAL   A HB   1 
ATOM   1040 H  HG11 . VAL   A 1 41  ? 31.317 -1.005  -7.692  1.00 16.83 ?  41  VAL   A HG11 1 
ATOM   1041 H  HG12 . VAL   A 1 41  ? 31.175 -1.398  -6.159  1.00 16.83 ?  41  VAL   A HG12 1 
ATOM   1042 H  HG13 . VAL   A 1 41  ? 30.028 -0.562  -6.874  1.00 16.83 ?  41  VAL   A HG13 1 
ATOM   1043 H  HG21 . VAL   A 1 41  ? 31.731 1.280   -8.361  1.00 16.40 ?  41  VAL   A HG21 1 
ATOM   1044 H  HG22 . VAL   A 1 41  ? 30.579 1.947   -7.494  1.00 16.40 ?  41  VAL   A HG22 1 
ATOM   1045 H  HG23 . VAL   A 1 41  ? 32.089 2.396   -7.289  1.00 16.40 ?  41  VAL   A HG23 1 
ATOM   1046 N  N    . TYR   A 1 42  ? 31.552 3.440   -4.630  1.00 11.52 ?  42  TYR   A N    1 
ATOM   1047 C  CA   . TYR   A 1 42  ? 32.298 4.623   -4.216  1.00 11.72 ?  42  TYR   A CA   1 
ATOM   1048 C  C    . TYR   A 1 42  ? 32.043 4.996   -2.766  1.00 11.17 ?  42  TYR   A C    1 
ATOM   1049 O  O    . TYR   A 1 42  ? 32.603 5.988   -2.283  1.00 11.95 ?  42  TYR   A O    1 
ATOM   1050 C  CB   . TYR   A 1 42  ? 31.952 5.811   -5.131  1.00 12.48 ?  42  TYR   A CB   1 
ATOM   1051 C  CG   . TYR   A 1 42  ? 32.132 5.498   -6.603  1.00 13.34 ?  42  TYR   A CG   1 
ATOM   1052 C  CD1  . TYR   A 1 42  ? 33.393 5.294   -7.141  1.00 13.95 ?  42  TYR   A CD1  1 
ATOM   1053 C  CD2  . TYR   A 1 42  ? 31.042 5.383   -7.450  1.00 14.87 ?  42  TYR   A CD2  1 
ATOM   1054 C  CE1  . TYR   A 1 42  ? 33.564 4.992   -8.482  1.00 14.68 ?  42  TYR   A CE1  1 
ATOM   1055 C  CE2  . TYR   A 1 42  ? 31.204 5.088   -8.795  1.00 16.19 ?  42  TYR   A CE2  1 
ATOM   1056 C  CZ   . TYR   A 1 42  ? 32.468 4.888   -9.305  1.00 15.86 ?  42  TYR   A CZ   1 
ATOM   1057 O  OH   . TYR   A 1 42  ? 32.624 4.593   -10.639 1.00 17.46 ?  42  TYR   A OH   1 
ATOM   1058 H  H    . TYR   A 1 42  ? 30.759 3.616   -4.917  1.00 13.82 ?  42  TYR   A H    1 
ATOM   1059 H  HA   . TYR   A 1 42  ? 33.245 4.445   -4.315  1.00 14.06 ?  42  TYR   A HA   1 
ATOM   1060 H  HB2  . TYR   A 1 42  ? 31.025 6.061   -4.989  1.00 14.97 ?  42  TYR   A HB2  1 
ATOM   1061 H  HB3  . TYR   A 1 42  ? 32.532 6.559   -4.910  1.00 14.97 ?  42  TYR   A HB3  1 
ATOM   1062 H  HD1  . TYR   A 1 42  ? 34.138 5.355   -6.589  1.00 16.73 ?  42  TYR   A HD1  1 
ATOM   1063 H  HD2  . TYR   A 1 42  ? 30.187 5.521   -7.112  1.00 17.84 ?  42  TYR   A HD2  1 
ATOM   1064 H  HE1  . TYR   A 1 42  ? 34.418 4.855   -8.828  1.00 17.61 ?  42  TYR   A HE1  1 
ATOM   1065 H  HE2  . TYR   A 1 42  ? 30.460 5.023   -9.350  1.00 19.42 ?  42  TYR   A HE2  1 
ATOM   1066 H  HH   . TYR   A 1 42  ? 33.443 4.494   -10.816 1.00 20.95 ?  42  TYR   A HH   1 
ATOM   1067 N  N    . LEU   A 1 43  ? 31.192 4.236   -2.075  1.00 10.99 ?  43  LEU   A N    1 
ATOM   1068 C  CA   . LEU   A 1 43  ? 30.745 4.575   -0.724  1.00 10.86 ?  43  LEU   A CA   1 
ATOM   1069 C  C    . LEU   A 1 43  ? 30.268 6.028   -0.629  1.00 11.16 ?  43  LEU   A C    1 
ATOM   1070 O  O    . LEU   A 1 43  ? 30.530 6.727   0.353   1.00 12.01 ?  43  LEU   A O    1 
ATOM   1071 C  CB   . LEU   A 1 43  ? 31.801 4.266   0.335   1.00 11.25 ?  43  LEU   A CB   1 
ATOM   1072 C  CG   . LEU   A 1 43  ? 32.305 2.817   0.417   1.00 11.62 ?  43  LEU   A CG   1 
ATOM   1073 C  CD1  . LEU   A 1 43  ? 33.363 2.703   1.503   1.00 12.36 ?  43  LEU   A CD1  1 
ATOM   1074 C  CD2  . LEU   A 1 43  ? 31.160 1.840   0.674   1.00 11.76 ?  43  LEU   A CD2  1 
ATOM   1075 H  H    . LEU   A 1 43  ? 30.856 3.495   -2.367  1.00 13.18 ?  43  LEU   A H    1 
ATOM   1076 H  HA   . LEU   A 1 43  ? 29.976 4.018   -0.518  1.00 13.03 ?  43  LEU   A HA   1 
ATOM   1077 H  HB2  . LEU   A 1 43  ? 32.571 4.830   0.172   1.00 13.49 ?  43  LEU   A HB2  1 
ATOM   1078 H  HB3  . LEU   A 1 43  ? 31.426 4.483   1.207   1.00 13.49 ?  43  LEU   A HB3  1 
ATOM   1079 H  HG   . LEU   A 1 43  ? 32.718 2.579   -0.427  1.00 13.93 ?  43  LEU   A HG   1 
ATOM   1080 H  HD11 . LEU   A 1 43  ? 33.676 1.784   1.543   1.00 14.83 ?  43  LEU   A HD11 1 
ATOM   1081 H  HD12 . LEU   A 1 43  ? 34.102 3.293   1.286   1.00 14.83 ?  43  LEU   A HD12 1 
ATOM   1082 H  HD13 . LEU   A 1 43  ? 32.973 2.957   2.352   1.00 14.83 ?  43  LEU   A HD13 1 
ATOM   1083 H  HD21 . LEU   A 1 43  ? 31.528 0.953   0.814   1.00 14.10 ?  43  LEU   A HD21 1 
ATOM   1084 H  HD22 . LEU   A 1 43  ? 30.676 2.124   1.466   1.00 14.10 ?  43  LEU   A HD22 1 
ATOM   1085 H  HD23 . LEU   A 1 43  ? 30.569 1.838   -0.092  1.00 14.10 ?  43  LEU   A HD23 1 
ATOM   1086 N  N    . LYS   A 1 44  ? 29.535 6.473   -1.654  1.00 10.94 ?  44  LYS   A N    1 
ATOM   1087 C  CA   . LYS   A 1 44  ? 28.889 7.786   -1.653  1.00 11.64 ?  44  LYS   A CA   1 
ATOM   1088 C  C    . LYS   A 1 44  ? 27.467 7.591   -1.143  1.00 10.84 ?  44  LYS   A C    1 
ATOM   1089 O  O    . LYS   A 1 44  ? 26.597 7.079   -1.856  1.00 11.97 ?  44  LYS   A O    1 
ATOM   1090 C  CB   . LYS   A 1 44  ? 28.926 8.405   -3.044  1.00 13.67 ?  44  LYS   A CB   1 
ATOM   1091 C  CG   . LYS   A 1 44  ? 30.293 8.888   -3.467  1.00 16.66 ?  44  LYS   A CG   1 
ATOM   1092 C  CD   . LYS   A 1 44  ? 30.935 9.799   -2.423  1.00 22.80 ?  44  LYS   A CD   1 
ATOM   1093 C  CE   . LYS   A 1 44  ? 32.232 10.404  -2.930  1.00 26.39 ?  44  LYS   A CE   1 
ATOM   1094 N  NZ   . LYS   A 1 44  ? 33.087 10.905  -1.816  1.00 28.84 ?  44  LYS   A NZ   1 
ATOM   1095 H  H    . LYS   A 1 44  ? 29.393 6.019   -2.371  1.00 13.12 ?  44  LYS   A H    1 
ATOM   1096 H  HA   . LYS   A 1 44  ? 29.341 8.365   -1.020  1.00 13.96 ?  44  LYS   A HA   1 
ATOM   1097 H  HB2  . LYS   A 1 44  ? 28.632 7.743   -3.686  1.00 16.40 ?  44  LYS   A HB2  1 
ATOM   1098 H  HB3  . LYS   A 1 44  ? 28.325 9.167   -3.058  1.00 16.40 ?  44  LYS   A HB3  1 
ATOM   1099 H  HG2  . LYS   A 1 44  ? 30.876 8.125   -3.603  1.00 19.99 ?  44  LYS   A HG2  1 
ATOM   1100 H  HG3  . LYS   A 1 44  ? 30.210 9.395   -4.294  1.00 19.99 ?  44  LYS   A HG3  1 
ATOM   1101 H  HD2  . LYS   A 1 44  ? 30.318 10.513  -2.201  1.00 27.35 ?  44  LYS   A HD2  1 
ATOM   1102 H  HD3  . LYS   A 1 44  ? 31.143 9.275   -1.631  1.00 27.35 ?  44  LYS   A HD3  1 
ATOM   1103 H  HE2  . LYS   A 1 44  ? 32.732 9.726   -3.412  1.00 31.66 ?  44  LYS   A HE2  1 
ATOM   1104 H  HE3  . LYS   A 1 44  ? 32.027 11.148  -3.515  1.00 31.66 ?  44  LYS   A HE3  1 
ATOM   1105 H  HZ1  . LYS   A 1 44  ? 33.836 11.255  -2.143  1.00 34.60 ?  44  LYS   A HZ1  1 
ATOM   1106 H  HZ2  . LYS   A 1 44  ? 32.650 11.534  -1.359  1.00 34.60 ?  44  LYS   A HZ2  1 
ATOM   1107 H  HZ3  . LYS   A 1 44  ? 33.292 10.238  -1.265  1.00 34.60 ?  44  LYS   A HZ3  1 
ATOM   1108 N  N    A HIS   A 1 45  ? 27.241 7.967   0.111   0.68 10.29 ?  45  HIS   A N    1 
ATOM   1109 N  N    B HIS   A 1 45  ? 27.232 7.991   0.106   0.32 11.22 ?  45  HIS   A N    1 
ATOM   1110 C  CA   A HIS   A 1 45  ? 26.012 7.614   0.818   0.68 10.40 ?  45  HIS   A CA   1 
ATOM   1111 C  CA   B HIS   A 1 45  ? 25.975 7.714   0.802   0.32 11.81 ?  45  HIS   A CA   1 
ATOM   1112 C  C    A HIS   A 1 45  ? 24.979 8.736   0.663   0.68 10.93 ?  45  HIS   A C    1 
ATOM   1113 C  C    B HIS   A 1 45  ? 25.030 8.889   0.594   0.32 12.69 ?  45  HIS   A C    1 
ATOM   1114 O  O    A HIS   A 1 45  ? 24.623 9.447   1.606   0.68 10.88 ?  45  HIS   A O    1 
ATOM   1115 O  O    B HIS   A 1 45  ? 24.999 9.836   1.380   0.32 13.47 ?  45  HIS   A O    1 
ATOM   1116 C  CB   A HIS   A 1 45  ? 26.324 7.337   2.280   0.68 10.21 ?  45  HIS   A CB   1 
ATOM   1117 C  CB   B HIS   A 1 45  ? 26.243 7.500   2.284   0.32 10.96 ?  45  HIS   A CB   1 
ATOM   1118 C  CG   A HIS   A 1 45  ? 27.441 6.363   2.482   0.68 10.14 ?  45  HIS   A CG   1 
ATOM   1119 C  CG   B HIS   A 1 45  ? 27.366 6.554   2.560   0.32 10.31 ?  45  HIS   A CG   1 
ATOM   1120 N  ND1  A HIS   A 1 45  ? 27.429 5.082   1.965   0.68 10.25 ?  45  HIS   A ND1  1 
ATOM   1121 N  ND1  B HIS   A 1 45  ? 27.386 5.262   2.081   0.32 10.47 ?  45  HIS   A ND1  1 
ATOM   1122 C  CD2  A HIS   A 1 45  ? 28.614 6.496   3.145   0.68 10.81 ?  45  HIS   A CD2  1 
ATOM   1123 C  CD2  B HIS   A 1 45  ? 28.513 6.718   3.260   0.32 9.73  ?  45  HIS   A CD2  1 
ATOM   1124 C  CE1  A HIS   A 1 45  ? 28.548 4.469   2.314   0.68 10.50 ?  45  HIS   A CE1  1 
ATOM   1125 C  CE1  B HIS   A 1 45  ? 28.497 4.669   2.481   0.32 9.30  ?  45  HIS   A CE1  1 
ATOM   1126 N  NE2  A HIS   A 1 45  ? 29.283 5.302   3.030   0.68 10.74 ?  45  HIS   A NE2  1 
ATOM   1127 N  NE2  B HIS   A 1 45  ? 29.198 5.529   3.199   0.32 9.07  ?  45  HIS   A NE2  1 
ATOM   1128 H  H    A HIS   A 1 45  ? 27.788 8.433   0.582   0.68 12.34 ?  45  HIS   A H    1 
ATOM   1129 H  H    B HIS   A 1 45  ? 27.795 8.433   0.585   0.32 13.46 ?  45  HIS   A H    1 
ATOM   1130 H  HA   A HIS   A 1 45  ? 25.638 6.807   0.431   0.68 12.48 ?  45  HIS   A HA   1 
ATOM   1131 H  HA   B HIS   A 1 45  ? 25.564 6.912   0.440   0.32 14.17 ?  45  HIS   A HA   1 
ATOM   1132 H  HB2  A HIS   A 1 45  ? 26.569 8.169   2.712   0.68 12.25 ?  45  HIS   A HB2  1 
ATOM   1133 H  HB2  B HIS   A 1 45  ? 26.466 8.354   2.688   0.32 13.15 ?  45  HIS   A HB2  1 
ATOM   1134 H  HB3  A HIS   A 1 45  ? 25.527 6.971   2.706   0.68 12.25 ?  45  HIS   A HB3  1 
ATOM   1135 H  HB3  B HIS   A 1 45  ? 25.442 7.141   2.699   0.32 13.15 ?  45  HIS   A HB3  1 
ATOM   1136 H  HD2  A HIS   A 1 45  ? 28.911 7.254   3.599   0.68 12.97 ?  45  HIS   A HD2  1 
ATOM   1137 H  HD2  B HIS   A 1 45  ? 28.784 7.491   3.702   0.32 11.67 ?  45  HIS   A HD2  1 
ATOM   1138 H  HE1  A HIS   A 1 45  ? 28.780 3.593   2.104   0.68 12.60 ?  45  HIS   A HE1  1 
ATOM   1139 H  HE1  B HIS   A 1 45  ? 28.745 3.794   2.292   0.32 11.16 ?  45  HIS   A HE1  1 
ATOM   1140 H  HE2  A HIS   A 1 45  ? 30.058 5.130   3.369   0.68 12.88 ?  45  HIS   A HE2  1 
ATOM   1141 H  HE2  B HIS   A 1 45  ? 29.959 5.374   3.565   0.32 10.88 ?  45  HIS   A HE2  1 
ATOM   1142 N  N    A GLY   A 1 46  ? 24.490 8.884   -0.566  0.68 11.94 ?  46  GLY   A N    1 
ATOM   1143 N  N    B GLY   A 1 46  ? 24.231 8.824   -0.467  0.32 12.51 ?  46  GLY   A N    1 
ATOM   1144 C  CA   A GLY   A 1 46  ? 23.692 10.047  -0.919  0.68 12.49 ?  46  GLY   A CA   1 
ATOM   1145 C  CA   B GLY   A 1 46  ? 23.374 9.942   -0.804  0.32 11.80 ?  46  GLY   A CA   1 
ATOM   1146 C  C    A GLY   A 1 46  ? 22.201 9.921   -0.684  0.68 12.40 ?  46  GLY   A C    1 
ATOM   1147 C  C    B GLY   A 1 46  ? 21.936 9.796   -0.352  0.32 10.86 ?  46  GLY   A C    1 
ATOM   1148 O  O    A GLY   A 1 46  ? 21.525 10.917  -0.399  0.68 12.76 ?  46  GLY   A O    1 
ATOM   1149 O  O    B GLY   A 1 46  ? 21.341 10.755  0.151   0.32 10.76 ?  46  GLY   A O    1 
ATOM   1150 H  H    A GLY   A 1 46  ? 24.598 8.318   -1.201  0.68 14.32 ?  46  GLY   A H    1 
ATOM   1151 H  H    B GLY   A 1 46  ? 24.171 8.150   -1.002  0.32 15.00 ?  46  GLY   A H    1 
ATOM   1152 H  HA2  A GLY   A 1 46  ? 24.016 10.810  -0.413  0.68 14.99 ?  46  GLY   A HA2  1 
ATOM   1153 H  HA2  B GLY   A 1 46  ? 23.727 10.748  -0.396  0.32 14.16 ?  46  GLY   A HA2  1 
ATOM   1154 H  HA3  A GLY   A 1 46  ? 23.821 10.235  -1.859  0.68 14.99 ?  46  GLY   A HA3  1 
ATOM   1155 H  HA3  B GLY   A 1 46  ? 23.382 10.065  -1.763  0.32 14.16 ?  46  GLY   A HA3  1 
ATOM   1156 N  N    A GLY   A 1 47  ? 21.670 8.712   -0.826  0.68 12.07 ?  47  GLY   A N    1 
ATOM   1157 N  N    B GLY   A 1 47  ? 21.364 8.611   -0.526  0.32 10.98 ?  47  GLY   A N    1 
ATOM   1158 C  CA   A GLY   A 1 47  ? 20.237 8.505   -0.765  0.68 12.47 ?  47  GLY   A CA   1 
ATOM   1159 C  CA   B GLY   A 1 47  ? 19.958 8.417   -0.255  0.32 10.68 ?  47  GLY   A CA   1 
ATOM   1160 C  C    A GLY   A 1 47  ? 19.921 7.063   -0.437  0.68 11.52 ?  47  GLY   A C    1 
ATOM   1161 C  C    B GLY   A 1 47  ? 19.649 6.967   0.041   0.32 9.74  ?  47  GLY   A C    1 
ATOM   1162 O  O    A GLY   A 1 47  ? 20.814 6.232   -0.255  0.68 11.95 ?  47  GLY   A O    1 
ATOM   1163 O  O    B GLY   A 1 47  ? 20.548 6.129   0.148   0.32 9.60  ?  47  GLY   A O    1 
ATOM   1164 H  H    A GLY   A 1 47  ? 22.124 7.995   -0.946  0.68 14.48 ?  47  GLY   A H    1 
ATOM   1165 H  H    B GLY   A 1 47  ? 21.775 7.902   -0.792  0.32 13.17 ?  47  GLY   A H    1 
ATOM   1166 H  HA2  A GLY   A 1 47  ? 19.843 9.088   -0.093  0.68 14.96 ?  47  GLY   A HA2  1 
ATOM   1167 H  HA2  B GLY   A 1 47  ? 19.697 8.942   0.516   0.32 12.81 ?  47  GLY   A HA2  1 
ATOM   1168 H  HA3  A GLY   A 1 47  ? 19.845 8.712   -1.627  0.68 14.96 ?  47  GLY   A HA3  1 
ATOM   1169 H  HA3  B GLY   A 1 47  ? 19.433 8.705   -1.020  0.32 12.81 ?  47  GLY   A HA3  1 
ATOM   1170 N  N    A GLY   A 1 48  ? 18.629 6.763   -0.392  0.68 11.54 ?  48  GLY   A N    1 
ATOM   1171 N  N    B GLY   A 1 48  ? 18.354 6.680   0.174   0.32 9.81  ?  48  GLY   A N    1 
ATOM   1172 C  CA   A GLY   A 1 48  ? 18.217 5.433   -0.006  0.68 11.86 ?  48  GLY   A CA   1 
ATOM   1173 C  CA   B GLY   A 1 48  ? 17.956 5.339   0.552   0.32 9.45  ?  48  GLY   A CA   1 
ATOM   1174 C  C    A GLY   A 1 48  ? 18.637 5.112   1.415   0.68 11.41 ?  48  GLY   A C    1 
ATOM   1175 C  C    B GLY   A 1 48  ? 18.547 4.951   1.894   0.32 9.66  ?  48  GLY   A C    1 
ATOM   1176 O  O    A GLY   A 1 48  ? 18.807 5.998   2.260   0.68 11.44 ?  48  GLY   A O    1 
ATOM   1177 O  O    B GLY   A 1 48  ? 18.701 5.774   2.805   0.32 9.90  ?  48  GLY   A O    1 
ATOM   1178 H  H    A GLY   A 1 48  ? 17.993 7.301   -0.577  0.68 13.85 ?  48  GLY   A H    1 
ATOM   1179 H  H    B GLY   A 1 48  ? 17.696 7.232   0.052   0.32 11.77 ?  48  GLY   A H    1 
ATOM   1180 H  HA2  A GLY   A 1 48  ? 17.258 5.354   -0.072  0.68 14.22 ?  48  GLY   A HA2  1 
ATOM   1181 H  HA2  B GLY   A 1 48  ? 16.987 5.280   0.606   0.32 11.34 ?  48  GLY   A HA2  1 
ATOM   1182 H  HA3  A GLY   A 1 48  ? 18.630 4.779   -0.590  0.68 14.22 ?  48  GLY   A HA3  1 
ATOM   1183 H  HA3  B GLY   A 1 48  ? 18.262 4.703   -0.120  0.32 11.34 ?  48  GLY   A HA3  1 
ATOM   1184 N  N    A VAL   A 1 49  ? 18.815 3.816   1.681   0.68 11.88 ?  49  VAL   A N    1 
ATOM   1185 N  N    B VAL   A 1 49  ? 18.873 3.663   2.020   0.32 9.77  ?  49  VAL   A N    1 
ATOM   1186 C  CA   A VAL   A 1 49  ? 19.270 3.381   2.998   0.68 11.60 ?  49  VAL   A CA   1 
ATOM   1187 C  CA   B VAL   A 1 49  ? 19.510 3.160   3.234   0.32 9.91  ?  49  VAL   A CA   1 
ATOM   1188 C  C    A VAL   A 1 49  ? 20.587 4.053   3.364   0.68 10.72 ?  49  VAL   A C    1 
ATOM   1189 C  C    B VAL   A 1 49  ? 20.773 3.953   3.550   0.32 9.61  ?  49  VAL   A C    1 
ATOM   1190 O  O    A VAL   A 1 49  ? 20.778 4.482   4.506   0.68 10.85 ?  49  VAL   A O    1 
ATOM   1191 O  O    B VAL   A 1 49  ? 20.996 4.370   4.693   0.32 9.72  ?  49  VAL   A O    1 
ATOM   1192 C  CB   A VAL   A 1 49  ? 19.383 1.845   3.038   0.68 13.03 ?  49  VAL   A CB   1 
ATOM   1193 C  CB   B VAL   A 1 49  ? 19.812 1.658   3.090   0.32 10.11 ?  49  VAL   A CB   1 
ATOM   1194 C  CG1  A VAL   A 1 49  ? 20.159 1.387   4.273   0.68 13.70 ?  49  VAL   A CG1  1 
ATOM   1195 C  CG1  B VAL   A 1 49  ? 20.669 1.184   4.243   0.32 9.64  ?  49  VAL   A CG1  1 
ATOM   1196 C  CG2  A VAL   A 1 49  ? 18.000 1.203   3.001   0.68 15.09 ?  49  VAL   A CG2  1 
ATOM   1197 C  CG2  B VAL   A 1 49  ? 18.520 0.849   3.011   0.32 10.61 ?  49  VAL   A CG2  1 
ATOM   1198 H  H    A VAL   A 1 49  ? 18.686 3.174   1.125   0.68 14.26 ?  49  VAL   A H    1 
ATOM   1199 H  H    B VAL   A 1 49  ? 18.729 3.061   1.420   0.32 11.72 ?  49  VAL   A H    1 
ATOM   1200 H  HA   A VAL   A 1 49  ? 18.615 3.634   3.667   0.68 13.91 ?  49  VAL   A HA   1 
ATOM   1201 H  HA   B VAL   A 1 49  ? 18.902 3.266   3.979   0.32 11.88 ?  49  VAL   A HA   1 
ATOM   1202 H  HB   A VAL   A 1 49  ? 19.874 1.539   2.259   0.68 15.63 ?  49  VAL   A HB   1 
ATOM   1203 H  HB   B VAL   A 1 49  ? 20.306 1.509   2.268   0.32 12.13 ?  49  VAL   A HB   1 
ATOM   1204 H  HG11 A VAL   A 1 49  ? 19.975 0.446   4.432   0.68 16.44 ?  49  VAL   A HG11 1 
ATOM   1205 H  HG11 B VAL   A 1 49  ? 20.605 0.219   4.310   0.32 11.57 ?  49  VAL   A HG11 1 
ATOM   1206 H  HG12 A VAL   A 1 49  ? 21.107 1.515   4.122   0.68 16.44 ?  49  VAL   A HG12 1 
ATOM   1207 H  HG12 B VAL   A 1 49  ? 21.592 1.440   4.080   0.32 11.57 ?  49  VAL   A HG12 1 
ATOM   1208 H  HG13 A VAL   A 1 49  ? 19.868 1.909   5.038   0.68 16.44 ?  49  VAL   A HG13 1 
ATOM   1209 H  HG13 B VAL   A 1 49  ? 20.351 1.593   5.062   0.32 11.57 ?  49  VAL   A HG13 1 
ATOM   1210 H  HG21 A VAL   A 1 49  ? 18.096 0.235   3.021   0.68 18.11 ?  49  VAL   A HG21 1 
ATOM   1211 H  HG21 B VAL   A 1 49  ? 18.736 -0.092  2.919   0.32 12.73 ?  49  VAL   A HG21 1 
ATOM   1212 H  HG22 A VAL   A 1 49  ? 17.494 1.498   3.774   0.68 18.11 ?  49  VAL   A HG22 1 
ATOM   1213 H  HG22 B VAL   A 1 49  ? 18.008 0.991   3.825   0.32 12.73 ?  49  VAL   A HG22 1 
ATOM   1214 H  HG23 A VAL   A 1 49  ? 17.551 1.473   2.187   0.68 18.11 ?  49  VAL   A HG23 1 
ATOM   1215 H  HG23 B VAL   A 1 49  ? 18.005 1.146   2.244   0.32 12.73 ?  49  VAL   A HG23 1 
ATOM   1216 N  N    A ALA   A 1 50  ? 21.527 4.117   2.417   0.68 10.48 ?  50  ALA   A N    1 
ATOM   1217 N  N    B ALA   A 1 50  ? 21.630 4.147   2.544   0.32 9.40  ?  50  ALA   A N    1 
ATOM   1218 C  CA   A ALA   A 1 50  ? 22.848 4.668   2.709   0.68 10.38 ?  50  ALA   A CA   1 
ATOM   1219 C  CA   B ALA   A 1 50  ? 22.942 4.738   2.794   0.32 9.39  ?  50  ALA   A CA   1 
ATOM   1220 C  C    A ALA   A 1 50  ? 22.761 6.134   3.114   0.68 10.29 ?  50  ALA   A C    1 
ATOM   1221 C  C    B ALA   A 1 50  ? 22.819 6.181   3.270   0.32 9.25  ?  50  ALA   A C    1 
ATOM   1222 O  O    A ALA   A 1 50  ? 23.404 6.565   4.076   0.68 11.05 ?  50  ALA   A O    1 
ATOM   1223 O  O    B ALA   A 1 50  ? 23.435 6.571   4.270   0.32 9.10  ?  50  ALA   A O    1 
ATOM   1224 C  CB   A ALA   A 1 50  ? 23.747 4.525   1.486   0.68 10.82 ?  50  ALA   A CB   1 
ATOM   1225 C  CB   B ALA   A 1 50  ? 23.806 4.648   1.536   0.32 9.35  ?  50  ALA   A CB   1 
ATOM   1226 H  H    A ALA   A 1 50  ? 21.420 3.855   1.606   0.68 12.57 ?  50  ALA   A H    1 
ATOM   1227 H  H    B ALA   A 1 50  ? 21.473 3.956   1.716   0.32 11.28 ?  50  ALA   A H    1 
ATOM   1228 H  HA   A ALA   A 1 50  ? 23.248 4.179   3.444   0.68 12.45 ?  50  ALA   A HA   1 
ATOM   1229 H  HA   B ALA   A 1 50  ? 23.382 4.238   3.492   0.32 11.26 ?  50  ALA   A HA   1 
ATOM   1230 H  HB1  A ALA   A 1 50  ? 24.619 4.899   1.691   0.68 12.98 ?  50  ALA   A HB1  1 
ATOM   1231 H  HB1  B ALA   A 1 50  ? 24.674 5.042   1.718   0.32 11.21 ?  50  ALA   A HB1  1 
ATOM   1232 H  HB2  A ALA   A 1 50  ? 23.829 3.589   1.262   0.68 12.98 ?  50  ALA   A HB2  1 
ATOM   1233 H  HB2  B ALA   A 1 50  ? 23.915 3.712   1.294   0.32 11.21 ?  50  ALA   A HB2  1 
ATOM   1234 H  HB3  A ALA   A 1 50  ? 23.347 5.012   0.745   0.68 12.98 ?  50  ALA   A HB3  1 
ATOM   1235 H  HB3  B ALA   A 1 50  ? 23.371 5.126   0.813   0.32 11.21 ?  50  ALA   A HB3  1 
ATOM   1236 N  N    A GLY   A 1 51  ? 21.984 6.926   2.376   0.68 10.26 ?  51  GLY   A N    1 
ATOM   1237 N  N    B GLY   A 1 51  ? 22.026 6.991   2.568   0.32 9.96  ?  51  GLY   A N    1 
ATOM   1238 C  CA   A GLY   A 1 51  ? 21.829 8.322   2.745   0.68 10.91 ?  51  GLY   A CA   1 
ATOM   1239 C  CA   B GLY   A 1 51  ? 21.847 8.369   2.990   0.32 9.69  ?  51  GLY   A CA   1 
ATOM   1240 C  C    A GLY   A 1 51  ? 21.231 8.484   4.126   0.68 10.42 ?  51  GLY   A C    1 
ATOM   1241 C  C    B GLY   A 1 51  ? 21.216 8.478   4.363   0.32 9.99  ?  51  GLY   A C    1 
ATOM   1242 O  O    A GLY   A 1 51  ? 21.636 9.361   4.889   0.68 11.24 ?  51  GLY   A O    1 
ATOM   1243 O  O    B GLY   A 1 51  ? 21.546 9.383   5.135   0.32 10.41 ?  51  GLY   A O    1 
ATOM   1244 H  H    A GLY   A 1 51  ? 21.554 6.687   1.675   0.68 12.31 ?  51  GLY   A H    1 
ATOM   1245 H  H    B GLY   A 1 51  ? 21.591 6.767   1.858   0.32 11.95 ?  51  GLY   A H    1 
ATOM   1246 H  HA2  A GLY   A 1 51  ? 22.691 8.763   2.740   0.68 13.09 ?  51  GLY   A HA2  1 
ATOM   1247 H  HA2  B GLY   A 1 51  ? 22.709 8.813   3.011   0.32 11.63 ?  51  GLY   A HA2  1 
ATOM   1248 H  HA3  A GLY   A 1 51  ? 21.248 8.769   2.110   0.68 13.09 ?  51  GLY   A HA3  1 
ATOM   1249 H  HA3  B GLY   A 1 51  ? 21.284 8.830   2.342   0.32 11.63 ?  51  GLY   A HA3  1 
ATOM   1250 N  N    A ALA   A 1 52  ? 20.254 7.639   4.464   0.68 10.51 ?  52  ALA   A N    1 
ATOM   1251 N  N    B ALA   A 1 52  ? 20.307 7.557   4.690   0.32 9.83  ?  52  ALA   A N    1 
ATOM   1252 C  CA   A ALA   A 1 52  ? 19.610 7.717   5.771   0.68 11.17 ?  52  ALA   A CA   1 
ATOM   1253 C  CA   B ALA   A 1 52  ? 19.642 7.596   5.988   0.32 10.37 ?  52  ALA   A CA   1 
ATOM   1254 C  C    A ALA   A 1 52  ? 20.558 7.293   6.891   0.68 10.95 ?  52  ALA   A C    1 
ATOM   1255 C  C    B ALA   A 1 52  ? 20.592 7.192   7.111   0.32 10.05 ?  52  ALA   A C    1 
ATOM   1256 O  O    A ALA   A 1 52  ? 20.643 7.960   7.928   0.68 11.80 ?  52  ALA   A O    1 
ATOM   1257 O  O    B ALA   A 1 52  ? 20.642 7.844   8.162   0.32 10.55 ?  52  ALA   A O    1 
ATOM   1258 C  CB   A ALA   A 1 52  ? 18.336 6.868   5.771   0.68 12.84 ?  52  ALA   A CB   1 
ATOM   1259 C  CB   B ALA   A 1 52  ? 18.409 6.691   5.958   0.32 11.84 ?  52  ALA   A CB   1 
ATOM   1260 H  H    A ALA   A 1 52  ? 19.959 7.009   3.962   0.68 12.61 ?  52  ALA   A H    1 
ATOM   1261 H  H    B ALA   A 1 52  ? 20.066 6.904   4.178   0.32 11.79 ?  52  ALA   A H    1 
ATOM   1262 H  HA   A ALA   A 1 52  ? 19.351 8.633   5.939   0.68 13.40 ?  52  ALA   A HA   1 
ATOM   1263 H  HA   B ALA   A 1 52  ? 19.346 8.503   6.154   0.32 12.44 ?  52  ALA   A HA   1 
ATOM   1264 H  HB1  A ALA   A 1 52  ? 17.913 6.928   6.645   0.68 15.41 ?  52  ALA   A HB1  1 
ATOM   1265 H  HB1  B ALA   A 1 52  ? 17.947 6.767   6.807   0.32 14.20 ?  52  ALA   A HB1  1 
ATOM   1266 H  HB2  A ALA   A 1 52  ? 17.732 7.206   5.091   0.68 15.41 ?  52  ALA   A HB2  1 
ATOM   1267 H  HB2  B ALA   A 1 52  ? 17.824 6.979   5.239   0.32 14.20 ?  52  ALA   A HB2  1 
ATOM   1268 H  HB3  A ALA   A 1 52  ? 18.566 5.945   5.581   0.68 15.41 ?  52  ALA   A HB3  1 
ATOM   1269 H  HB3  B ALA   A 1 52  ? 18.691 5.777   5.810   0.32 14.20 ?  52  ALA   A HB3  1 
ATOM   1270 N  N    A LEU   A 1 53  ? 21.272 6.177   6.713   0.68 10.87 ?  53  LEU   A N    1 
ATOM   1271 N  N    B LEU   A 1 53  ? 21.345 6.106   6.918   0.32 10.01 ?  53  LEU   A N    1 
ATOM   1272 C  CA   A LEU   A 1 53  ? 22.225 5.754   7.738   0.68 11.20 ?  53  LEU   A CA   1 
ATOM   1273 C  CA   B LEU   A 1 53  ? 22.360 5.739   7.902   0.32 9.92  ?  53  LEU   A CA   1 
ATOM   1274 C  C    A LEU   A 1 53  ? 23.297 6.811   7.942   0.68 10.48 ?  53  LEU   A C    1 
ATOM   1275 C  C    B LEU   A 1 53  ? 23.367 6.869   8.078   0.32 10.17 ?  53  LEU   A C    1 
ATOM   1276 O  O    A LEU   A 1 53  ? 23.653 7.136   9.078   0.68 11.33 ?  53  LEU   A O    1 
ATOM   1277 O  O    B LEU   A 1 53  ? 23.642 7.304   9.201   0.32 10.74 ?  53  LEU   A O    1 
ATOM   1278 C  CB   A LEU   A 1 53  ? 22.870 4.415   7.371   0.68 11.99 ?  53  LEU   A CB   1 
ATOM   1279 C  CB   B LEU   A 1 53  ? 23.073 4.449   7.486   0.32 9.59  ?  53  LEU   A CB   1 
ATOM   1280 C  CG   A LEU   A 1 53  ? 21.972 3.174   7.435   0.68 11.93 ?  53  LEU   A CG   1 
ATOM   1281 C  CG   B LEU   A 1 53  ? 22.311 3.121   7.561   0.32 10.00 ?  53  LEU   A CG   1 
ATOM   1282 C  CD1  A LEU   A 1 53  ? 22.706 1.972   6.870   0.68 12.13 ?  53  LEU   A CD1  1 
ATOM   1283 C  CD1  B LEU   A 1 53  ? 23.158 2.012   6.949   0.32 10.45 ?  53  LEU   A CD1  1 
ATOM   1284 C  CD2  A LEU   A 1 53  ? 21.497 2.883   8.855   0.68 13.61 ?  53  LEU   A CD2  1 
ATOM   1285 C  CD2  B LEU   A 1 53  ? 21.945 2.764   8.992   0.32 10.22 ?  53  LEU   A CD2  1 
ATOM   1286 H  H    A LEU   A 1 53  ? 21.225 5.659   6.031   0.68 13.04 ?  53  LEU   A H    1 
ATOM   1287 H  H    B LEU   A 1 53  ? 21.284 5.571   6.242   0.32 12.01 ?  53  LEU   A H    1 
ATOM   1288 H  HA   A LEU   A 1 53  ? 21.758 5.637   8.581   0.68 13.43 ?  53  LEU   A HA   1 
ATOM   1289 H  HA   B LEU   A 1 53  ? 21.927 5.583   8.754   0.32 11.90 ?  53  LEU   A HA   1 
ATOM   1290 H  HB2  A LEU   A 1 53  ? 23.208 4.479   6.464   0.68 14.39 ?  53  LEU   A HB2  1 
ATOM   1291 H  HB2  B LEU   A 1 53  ? 23.359 4.550   6.566   0.32 11.50 ?  53  LEU   A HB2  1 
ATOM   1292 H  HB3  A LEU   A 1 53  ? 23.615 4.258   7.977   0.68 14.39 ?  53  LEU   A HB3  1 
ATOM   1293 H  HB3  B LEU   A 1 53  ? 23.855 4.349   8.050   0.32 11.50 ?  53  LEU   A HB3  1 
ATOM   1294 H  HG   A LEU   A 1 53  ? 21.190 3.327   6.883   0.68 14.31 ?  53  LEU   A HG   1 
ATOM   1295 H  HG   B LEU   A 1 53  ? 21.494 3.189   7.045   0.32 11.99 ?  53  LEU   A HG   1 
ATOM   1296 H  HD11 A LEU   A 1 53  ? 22.125 1.196   6.918   0.68 14.55 ?  53  LEU   A HD11 1 
ATOM   1297 H  HD11 B LEU   A 1 53  ? 22.670 1.174   7.003   0.32 12.53 ?  53  LEU   A HD11 1 
ATOM   1298 H  HD12 A LEU   A 1 53  ? 22.946 2.149   5.948   0.68 14.55 ?  53  LEU   A HD12 1 
ATOM   1299 H  HD12 B LEU   A 1 53  ? 23.340 2.228   6.021   0.32 12.53 ?  53  LEU   A HD12 1 
ATOM   1300 H  HD13 A LEU   A 1 53  ? 23.507 1.815   7.397   0.68 14.55 ?  53  LEU   A HD13 1 
ATOM   1301 H  HD13 B LEU   A 1 53  ? 23.990 1.940   7.443   0.32 12.53 ?  53  LEU   A HD13 1 
ATOM   1302 H  HD21 A LEU   A 1 53  ? 20.992 2.055   8.856   0.68 16.32 ?  53  LEU   A HD21 1 
ATOM   1303 H  HD21 B LEU   A 1 53  ? 21.461 1.922   8.994   0.32 12.26 ?  53  LEU   A HD21 1 
ATOM   1304 H  HD22 A LEU   A 1 53  ? 22.270 2.799   9.436   0.68 16.32 ?  53  LEU   A HD22 1 
ATOM   1305 H  HD22 B LEU   A 1 53  ? 22.755 2.682   9.515   0.32 12.26 ?  53  LEU   A HD22 1 
ATOM   1306 H  HD23 A LEU   A 1 53  ? 20.935 3.613   9.157   0.68 16.32 ?  53  LEU   A HD23 1 
ATOM   1307 H  HD23 B LEU   A 1 53  ? 21.383 3.466   9.356   0.32 12.26 ?  53  LEU   A HD23 1 
ATOM   1308 N  N    A ASN   A 1 54  ? 23.809 7.377   6.857   0.68 10.33 ?  54  ASN   A N    1 
ATOM   1309 N  N    B ASN   A 1 54  ? 23.909 7.377   6.970   0.32 10.50 ?  54  ASN   A N    1 
ATOM   1310 C  CA   A ASN   A 1 54  ? 24.875 8.356   7.010   0.68 10.27 ?  54  ASN   A CA   1 
ATOM   1311 C  CA   B ASN   A 1 54  ? 24.938 8.405   7.075   0.32 10.43 ?  54  ASN   A CA   1 
ATOM   1312 C  C    A ASN   A 1 54  ? 24.379 9.600   7.750   0.68 10.59 ?  54  ASN   A C    1 
ATOM   1313 C  C    B ASN   A 1 54  ? 24.401 9.662   7.751   0.32 10.42 ?  54  ASN   A C    1 
ATOM   1314 O  O    A ASN   A 1 54  ? 25.071 10.132  8.630   0.68 11.23 ?  54  ASN   A O    1 
ATOM   1315 O  O    B ASN   A 1 54  ? 25.090 10.274  8.577   0.32 10.18 ?  54  ASN   A O    1 
ATOM   1316 C  CB   A ASN   A 1 54  ? 25.445 8.724   5.650   0.68 10.58 ?  54  ASN   A CB   1 
ATOM   1317 C  CB   B ASN   A 1 54  ? 25.509 8.745   5.702   0.32 10.89 ?  54  ASN   A CB   1 
ATOM   1318 C  CG   A ASN   A 1 54  ? 26.491 9.803   5.764   0.68 10.71 ?  54  ASN   A CG   1 
ATOM   1319 C  CG   B ASN   A 1 54  ? 26.473 9.915   5.765   0.32 10.99 ?  54  ASN   A CG   1 
ATOM   1320 O  OD1  A ASN   A 1 54  ? 27.478 9.646   6.495   0.68 10.72 ?  54  ASN   A OD1  1 
ATOM   1321 O  OD1  B ASN   A 1 54  ? 27.547 9.810   6.359   0.32 11.51 ?  54  ASN   A OD1  1 
ATOM   1322 N  ND2  A ASN   A 1 54  ? 26.278 10.916  5.080   0.68 11.31 ?  54  ASN   A ND2  1 
ATOM   1323 N  ND2  B ASN   A 1 54  ? 26.085 11.041  5.182   0.32 11.05 ?  54  ASN   A ND2  1 
ATOM   1324 H  H    A ASN   A 1 54  ? 23.560 7.218   6.052   0.68 12.39 ?  54  ASN   A H    1 
ATOM   1325 H  H    B ASN   A 1 54  ? 23.695 7.152   6.169   0.32 12.59 ?  54  ASN   A H    1 
ATOM   1326 H  HA   A ASN   A 1 54  ? 25.582 7.963   7.537   0.68 12.31 ?  54  ASN   A HA   1 
ATOM   1327 H  HA   B ASN   A 1 54  ? 25.658 8.064   7.623   0.32 12.51 ?  54  ASN   A HA   1 
ATOM   1328 H  HB2  A ASN   A 1 54  ? 25.856 7.931   5.258   0.68 12.69 ?  54  ASN   A HB2  1 
ATOM   1329 H  HB2  B ASN   A 1 54  ? 25.989 7.973   5.363   0.32 13.06 ?  54  ASN   A HB2  1 
ATOM   1330 H  HB3  A ASN   A 1 54  ? 24.732 9.045   5.078   0.68 12.69 ?  54  ASN   A HB3  1 
ATOM   1331 H  HB3  B ASN   A 1 54  ? 24.784 8.979   5.104   0.32 13.06 ?  54  ASN   A HB3  1 
ATOM   1332 H  HD21 A ASN   A 1 54  ? 26.846 11.555  5.122   0.68 13.57 ?  54  ASN   A HD21 1 
ATOM   1333 H  HD21 B ASN   A 1 54  ? 26.598 11.732  5.203   0.32 13.25 ?  54  ASN   A HD21 1 
ATOM   1334 H  HD22 A ASN   A 1 54  ? 25.572 10.991  4.598   0.68 13.57 ?  54  ASN   A HD22 1 
ATOM   1335 H  HD22 B ASN   A 1 54  ? 25.328 11.079  4.781   0.32 13.25 ?  54  ASN   A HD22 1 
ATOM   1336 N  N    . LYS   A 1 55  ? 23.176 10.073  7.410   1.00 10.90 ?  55  LYS   A N    1 
ATOM   1337 C  CA   . LYS   A 1 55  ? 22.598 11.233  8.079   1.00 11.63 ?  55  LYS   A CA   1 
ATOM   1338 C  C    . LYS   A 1 55  ? 22.506 10.999  9.580   1.00 11.49 ?  55  LYS   A C    1 
ATOM   1339 O  O    . LYS   A 1 55  ? 22.789 11.899  10.382  1.00 12.55 ?  55  LYS   A O    1 
ATOM   1340 C  CB   . LYS   A 1 55  ? 21.229 11.539  7.474   1.00 12.35 ?  55  LYS   A CB   1 
ATOM   1341 C  CG   . LYS   A 1 55  ? 20.477 12.695  8.126   1.00 14.07 ?  55  LYS   A CG   1 
ATOM   1342 C  CD   . LYS   A 1 55  ? 19.151 12.939  7.411   1.00 15.79 ?  55  LYS   A CD   1 
ATOM   1343 C  CE   . LYS   A 1 55  ? 18.318 14.031  8.068   1.00 17.73 ?  55  LYS   A CE   1 
ATOM   1344 N  NZ   . LYS   A 1 55  ? 16.985 14.196  7.405   1.00 19.04 ?  55  LYS   A NZ   1 
ATOM   1345 H  H    A LYS   A 1 55  ? 22.670 9.734   6.801   0.68 13.08 ?  55  LYS   A H    1 
ATOM   1346 H  H    B LYS   A 1 55  ? 22.668 9.704   6.821   0.32 13.08 ?  55  LYS   A H    1 
ATOM   1347 H  HA   . LYS   A 1 55  ? 23.172 12.002  7.931   1.00 13.96 ?  55  LYS   A HA   1 
ATOM   1348 H  HB2  . LYS   A 1 55  ? 21.349 11.765  6.538   1.00 14.81 ?  55  LYS   A HB2  1 
ATOM   1349 H  HB3  . LYS   A 1 55  ? 20.672 10.751  7.550   1.00 14.81 ?  55  LYS   A HB3  1 
ATOM   1350 H  HG2  . LYS   A 1 55  ? 20.288 12.476  9.054   1.00 16.88 ?  55  LYS   A HG2  1 
ATOM   1351 H  HG3  . LYS   A 1 55  ? 21.012 13.502  8.072   1.00 16.88 ?  55  LYS   A HG3  1 
ATOM   1352 H  HD2  . LYS   A 1 55  ? 19.336 13.207  6.498   1.00 18.94 ?  55  LYS   A HD2  1 
ATOM   1353 H  HD3  . LYS   A 1 55  ? 18.636 12.118  7.420   1.00 18.94 ?  55  LYS   A HD3  1 
ATOM   1354 H  HE2  . LYS   A 1 55  ? 18.166 13.800  8.998   1.00 21.28 ?  55  LYS   A HE2  1 
ATOM   1355 H  HE3  . LYS   A 1 55  ? 18.793 14.875  8.007   1.00 21.28 ?  55  LYS   A HE3  1 
ATOM   1356 H  HZ1  . LYS   A 1 55  ? 16.434 14.652  7.937   1.00 22.84 ?  55  LYS   A HZ1  1 
ATOM   1357 H  HZ2  . LYS   A 1 55  ? 17.076 14.642  6.639   1.00 22.84 ?  55  LYS   A HZ2  1 
ATOM   1358 H  HZ3  . LYS   A 1 55  ? 16.625 13.400  7.236   1.00 22.84 ?  55  LYS   A HZ3  1 
ATOM   1359 N  N    . ALA   A 1 56  ? 22.113 9.789   9.984   1.00 11.93 ?  56  ALA   A N    1 
ATOM   1360 C  CA   . ALA   A 1 56  ? 21.994 9.464   11.398  1.00 12.78 ?  56  ALA   A CA   1 
ATOM   1361 C  C    . ALA   A 1 56  ? 23.338 9.491   12.119  1.00 12.40 ?  56  ALA   A C    1 
ATOM   1362 O  O    . ALA   A 1 56  ? 23.360 9.666   13.337  1.00 13.87 ?  56  ALA   A O    1 
ATOM   1363 C  CB   . ALA   A 1 56  ? 21.298 8.110   11.576  1.00 13.57 ?  56  ALA   A CB   1 
ATOM   1364 H  H    . ALA   A 1 56  ? 21.912 9.146   9.455   1.00 14.31 ?  56  ALA   A H    1 
ATOM   1365 H  HA   . ALA   A 1 56  ? 21.437 10.128  11.823  1.00 15.33 ?  56  ALA   A HA   1 
ATOM   1366 H  HB1  . ALA   A 1 56  ? 21.229 7.909   12.525  1.00 16.27 ?  56  ALA   A HB1  1 
ATOM   1367 H  HB2  . ALA   A 1 56  ? 20.410 8.160   11.187  1.00 16.27 ?  56  ALA   A HB2  1 
ATOM   1368 H  HB3  . ALA   A 1 56  ? 21.816 7.422   11.131  1.00 16.27 ?  56  ALA   A HB3  1 
ATOM   1369 N  N    . THR   A 1 57  ? 24.453 9.311   11.400  1.00 11.75 ?  57  THR   A N    1 
ATOM   1370 C  CA   . THR   A 1 57  ? 25.796 9.439   11.975  1.00 11.77 ?  57  THR   A CA   1 
ATOM   1371 C  C    . THR   A 1 57  ? 26.345 10.856  11.891  1.00 12.05 ?  57  THR   A C    1 
ATOM   1372 O  O    . THR   A 1 57  ? 27.530 11.063  12.173  1.00 12.55 ?  57  THR   A O    1 
ATOM   1373 C  CB   . THR   A 1 57  ? 26.807 8.489   11.303  1.00 11.70 ?  57  THR   A CB   1 
ATOM   1374 O  OG1  . THR   A 1 57  ? 27.185 8.983   10.006  1.00 11.50 ?  57  THR   A OG1  1 
ATOM   1375 C  CG2  . THR   A 1 57  ? 26.283 7.062   11.210  1.00 11.89 ?  57  THR   A CG2  1 
ATOM   1376 H  H    . THR   A 1 57  ? 24.457 9.088   10.567  1.00 14.10 ?  57  THR   A H    1 
ATOM   1377 H  HA   . THR   A 1 57  ? 25.754 9.184   12.914  1.00 14.12 ?  57  THR   A HA   1 
ATOM   1378 H  HB   . THR   A 1 57  ? 27.609 8.454   11.857  1.00 14.04 ?  57  THR   A HB   1 
ATOM   1379 H  HG1  . THR   A 1 57  ? 26.501 9.040   9.517   1.00 13.80 ?  57  THR   A HG1  1 
ATOM   1380 H  HG21 . THR   A 1 57  ? 26.969 6.474   10.847  1.00 14.26 ?  57  THR   A HG21 1 
ATOM   1381 H  HG22 . THR   A 1 57  ? 26.027 6.739   12.087  1.00 14.26 ?  57  THR   A HG22 1 
ATOM   1382 H  HG23 . THR   A 1 57  ? 25.510 7.029   10.626  1.00 14.26 ?  57  THR   A HG23 1 
ATOM   1383 N  N    . ASN   A 1 58  ? 25.532 11.829  11.489  1.00 12.43 ?  58  ASN   A N    1 
ATOM   1384 C  CA   . ASN   A 1 58  ? 26.003 13.210  11.393  1.00 13.52 ?  58  ASN   A CA   1 
ATOM   1385 C  C    . ASN   A 1 58  ? 27.146 13.339  10.376  1.00 12.09 ?  58  ASN   A C    1 
ATOM   1386 O  O    . ASN   A 1 58  ? 28.040 14.177  10.523  1.00 13.06 ?  58  ASN   A O    1 
ATOM   1387 C  CB   . ASN   A 1 58  ? 26.389 13.740  12.790  1.00 15.76 ?  58  ASN   A CB   1 
ATOM   1388 C  CG   . ASN   A 1 58  ? 26.815 15.193  12.796  1.00 19.25 ?  58  ASN   A CG   1 
ATOM   1389 O  OD1  . ASN   A 1 58  ? 26.190 16.032  12.158  1.00 21.07 ?  58  ASN   A OD1  1 
ATOM   1390 N  ND2  . ASN   A 1 58  ? 27.881 15.501  13.544  1.00 20.44 ?  58  ASN   A ND2  1 
ATOM   1391 H  H    . ASN   A 1 58  ? 24.712 11.705  11.256  1.00 14.91 ?  58  ASN   A H    1 
ATOM   1392 H  HA   . ASN   A 1 58  ? 25.268 13.745  11.073  1.00 16.22 ?  58  ASN   A HA   1 
ATOM   1393 H  HB2  . ASN   A 1 58  ? 25.615 13.650  13.380  1.00 18.91 ?  58  ASN   A HB2  1 
ATOM   1394 H  HB3  . ASN   A 1 58  ? 27.121 13.213  13.142  1.00 18.91 ?  58  ASN   A HB3  1 
ATOM   1395 H  HD21 . ASN   A 1 58  ? 28.159 16.313  13.583  1.00 24.52 ?  58  ASN   A HD21 1 
ATOM   1396 H  HD22 . ASN   A 1 58  ? 28.289 14.884  13.982  1.00 24.52 ?  58  ASN   A HD22 1 
ATOM   1397 N  N    . ASN   A 1 59  ? 27.119 12.519  9.323   1.00 11.62 ?  59  ASN   A N    1 
ATOM   1398 C  CA   . ASN   A 1 59  ? 28.096 12.490  8.228   1.00 11.35 ?  59  ASN   A CA   1 
ATOM   1399 C  C    . ASN   A 1 59  ? 29.408 11.809  8.619   1.00 10.94 ?  59  ASN   A C    1 
ATOM   1400 O  O    . ASN   A 1 59  ? 30.330 11.776  7.796   1.00 11.15 ?  59  ASN   A O    1 
ATOM   1401 C  CB   . ASN   A 1 59  ? 28.384 13.875  7.618   1.00 11.39 ?  59  ASN   A CB   1 
ATOM   1402 C  CG   . ASN   A 1 59  ? 28.739 13.806  6.151   1.00 11.73 ?  59  ASN   A CG   1 
ATOM   1403 O  OD1  . ASN   A 1 59  ? 28.035 13.183  5.358   1.00 11.93 ?  59  ASN   A OD1  1 
ATOM   1404 N  ND2  . ASN   A 1 59  ? 29.829 14.467  5.772   1.00 12.48 ?  59  ASN   A ND2  1 
ATOM   1405 H  H    . ASN   A 1 59  ? 26.508 11.921  9.216   1.00 13.93 ?  59  ASN   A H    1 
ATOM   1406 H  HA   . ASN   A 1 59  ? 27.715 11.958  7.517   1.00 13.61 ?  59  ASN   A HA   1 
ATOM   1407 H  HB2  . ASN   A 1 59  ? 27.597 14.434  7.705   1.00 13.66 ?  59  ASN   A HB2  1 
ATOM   1408 H  HB3  . ASN   A 1 59  ? 29.132 14.282  8.086   1.00 13.66 ?  59  ASN   A HB3  1 
ATOM   1409 H  HD21 . ASN   A 1 59  ? 30.078 14.462  4.947   1.00 14.97 ?  59  ASN   A HD21 1 
ATOM   1410 H  HD22 . ASN   A 1 59  ? 30.304 14.896  6.354   1.00 14.97 ?  59  ASN   A HD22 1 
ATOM   1411 N  N    . ALA   A 1 60  ? 29.531 11.263  9.828   1.00 10.88 ?  60  ALA   A N    1 
ATOM   1412 C  CA   . ALA   A 1 60  ? 30.770 10.583  10.191  1.00 11.30 ?  60  ALA   A CA   1 
ATOM   1413 C  C    . ALA   A 1 60  ? 31.003 9.351   9.324   1.00 11.43 ?  60  ALA   A C    1 
ATOM   1414 O  O    . ALA   A 1 60  ? 32.148 9.027   8.991   1.00 11.55 ?  60  ALA   A O    1 
ATOM   1415 C  CB   . ALA   A 1 60  ? 30.768 10.217  11.672  1.00 11.77 ?  60  ALA   A CB   1 
ATOM   1416 H  H    . ALA   A 1 60  ? 28.934 11.278  10.445  1.00 13.05 ?  60  ALA   A H    1 
ATOM   1417 H  HA   . ALA   A 1 60  ? 31.515 11.189  10.042  1.00 13.56 ?  60  ALA   A HA   1 
ATOM   1418 H  HB1  . ALA   A 1 60  ? 31.595 9.768   11.892  1.00 14.11 ?  60  ALA   A HB1  1 
ATOM   1419 H  HB2  . ALA   A 1 60  ? 30.683 11.032  12.198  1.00 14.11 ?  60  ALA   A HB2  1 
ATOM   1420 H  HB3  . ALA   A 1 60  ? 30.012 9.634   11.851  1.00 14.11 ?  60  ALA   A HB3  1 
ATOM   1421 N  N    . MET   A 1 61  ? 29.932 8.648   8.944   1.00 10.86 ?  61  MET   A N    1 
ATOM   1422 C  CA   . MET   A 1 61  ? 30.075 7.509   8.041   1.00 11.01 ?  61  MET   A CA   1 
ATOM   1423 C  C    . MET   A 1 61  ? 30.704 7.934   6.717   1.00 10.86 ?  61  MET   A C    1 
ATOM   1424 O  O    . MET   A 1 61  ? 31.597 7.256   6.201   1.00 11.00 ?  61  MET   A O    1 
ATOM   1425 C  CB   . MET   A 1 61  ? 28.707 6.855   7.828   1.00 10.92 ?  61  MET   A CB   1 
ATOM   1426 C  CG   . MET   A 1 61  ? 28.712 5.683   6.862   1.00 11.50 ?  61  MET   A CG   1 
ATOM   1427 S  SD   . MET   A 1 61  ? 27.094 4.939   6.647   1.00 12.58 ?  61  MET   A SD   1 
ATOM   1428 C  CE   . MET   A 1 61  ? 26.948 4.051   8.202   1.00 14.20 ?  61  MET   A CE   1 
ATOM   1429 H  H    . MET   A 1 61  ? 29.125 8.804   9.193   1.00 13.03 ?  61  MET   A H    1 
ATOM   1430 H  HA   . MET   A 1 61  ? 30.650 6.847   8.458   1.00 13.21 ?  61  MET   A HA   1 
ATOM   1431 H  HB2  . MET   A 1 61  ? 28.382 6.531   8.678   1.00 13.09 ?  61  MET   A HB2  1 
ATOM   1432 H  HB3  . MET   A 1 61  ? 28.097 7.519   7.473   1.00 13.09 ?  61  MET   A HB3  1 
ATOM   1433 H  HG2  . MET   A 1 61  ? 29.007 5.979   5.988   1.00 13.79 ?  61  MET   A HG2  1 
ATOM   1434 H  HG3  . MET   A 1 61  ? 29.306 4.992   7.196   1.00 13.79 ?  61  MET   A HG3  1 
ATOM   1435 H  HE1  . MET   A 1 61  ? 26.105 3.572   8.215   1.00 17.03 ?  61  MET   A HE1  1 
ATOM   1436 H  HE2  . MET   A 1 61  ? 27.686 3.429   8.278   1.00 17.03 ?  61  MET   A HE2  1 
ATOM   1437 H  HE3  . MET   A 1 61  ? 26.976 4.688   8.936   1.00 17.03 ?  61  MET   A HE3  1 
ATOM   1438 N  N    . GLN   A 1 62  ? 30.251 9.060   6.153   1.00 10.82 ?  62  GLN   A N    1 
ATOM   1439 C  CA   . GLN   A 1 62  ? 30.812 9.531   4.888   1.00 11.21 ?  62  GLN   A CA   1 
ATOM   1440 C  C    . GLN   A 1 62  ? 32.285 9.907   5.029   1.00 10.94 ?  62  GLN   A C    1 
ATOM   1441 O  O    . GLN   A 1 62  ? 33.094 9.593   4.150   1.00 11.46 ?  62  GLN   A O    1 
ATOM   1442 C  CB   . GLN   A 1 62  ? 30.015 10.718  4.352   1.00 11.14 ?  62  GLN   A CB   1 
ATOM   1443 C  CG   . GLN   A 1 62  ? 30.397 11.077  2.927   1.00 10.89 ?  62  GLN   A CG   1 
ATOM   1444 C  CD   . GLN   A 1 62  ? 30.061 9.952   1.981   1.00 11.23 ?  62  GLN   A CD   1 
ATOM   1445 O  OE1  . GLN   A 1 62  ? 28.878 9.652   1.763   1.00 11.86 ?  62  GLN   A OE1  1 
ATOM   1446 N  NE2  . GLN   A 1 62  ? 31.079 9.279   1.458   1.00 11.35 ?  62  GLN   A NE2  1 
ATOM   1447 H  H    . GLN   A 1 62  ? 29.634 9.555   6.482   1.00 12.98 ?  62  GLN   A H    1 
ATOM   1448 H  HA   . GLN   A 1 62  ? 30.757 8.811   4.243   1.00 13.44 ?  62  GLN   A HA   1 
ATOM   1449 H  HB2  . GLN   A 1 62  ? 29.072 10.499  4.366   1.00 13.36 ?  62  GLN   A HB2  1 
ATOM   1450 H  HB3  . GLN   A 1 62  ? 30.186 11.493  4.913   1.00 13.36 ?  62  GLN   A HB3  1 
ATOM   1451 H  HG2  . GLN   A 1 62  ? 29.900 11.861  2.654   1.00 13.07 ?  62  GLN   A HG2  1 
ATOM   1452 H  HG3  . GLN   A 1 62  ? 31.351 11.244  2.880   1.00 13.07 ?  62  GLN   A HG3  1 
ATOM   1453 H  HE21 . GLN   A 1 62  ? 31.887 9.505   1.646   1.00 13.61 ?  62  GLN   A HE21 1 
ATOM   1454 H  HE22 . GLN   A 1 62  ? 30.930 8.622   0.924   1.00 13.61 ?  62  GLN   A HE22 1 
ATOM   1455 N  N    . VAL   A 1 63  ? 32.651 10.597  6.115   1.00 11.59 ?  63  VAL   A N    1 
ATOM   1456 C  CA   . VAL   A 1 63  ? 34.049 10.986  6.323   1.00 12.08 ?  63  VAL   A CA   1 
ATOM   1457 C  C    . VAL   A 1 63  ? 34.942 9.750   6.396   1.00 11.41 ?  63  VAL   A C    1 
ATOM   1458 O  O    . VAL   A 1 63  ? 35.997 9.677   5.749   1.00 12.21 ?  63  VAL   A O    1 
ATOM   1459 C  CB   . VAL   A 1 63  ? 34.165 11.871  7.577   1.00 14.00 ?  63  VAL   A CB   1 
ATOM   1460 C  CG1  . VAL   A 1 63  ? 35.618 12.115  7.935   1.00 16.16 ?  63  VAL   A CG1  1 
ATOM   1461 C  CG2  . VAL   A 1 63  ? 33.435 13.200  7.359   1.00 14.32 ?  63  VAL   A CG2  1 
ATOM   1462 H  H    . VAL   A 1 63  ? 32.111 10.849  6.739   1.00 13.91 ?  63  VAL   A H    1 
ATOM   1463 H  HA   . VAL   A 1 63  ? 34.335 11.515  5.565   1.00 14.49 ?  63  VAL   A HA   1 
ATOM   1464 H  HB   . VAL   A 1 63  ? 33.746 11.421  8.326   1.00 16.80 ?  63  VAL   A HB   1 
ATOM   1465 H  HG11 . VAL   A 1 63  ? 35.667 12.854  8.560   1.00 19.39 ?  63  VAL   A HG11 1 
ATOM   1466 H  HG12 . VAL   A 1 63  ? 35.983 11.315  8.338   1.00 19.39 ?  63  VAL   A HG12 1 
ATOM   1467 H  HG13 . VAL   A 1 63  ? 36.106 12.335  7.125   1.00 19.39 ?  63  VAL   A HG13 1 
ATOM   1468 H  HG21 . VAL   A 1 63  ? 33.531 13.748  8.156   1.00 17.17 ?  63  VAL   A HG21 1 
ATOM   1469 H  HG22 . VAL   A 1 63  ? 33.824 13.654  6.597   1.00 17.17 ?  63  VAL   A HG22 1 
ATOM   1470 H  HG23 . VAL   A 1 63  ? 32.495 13.021  7.196   1.00 17.17 ?  63  VAL   A HG23 1 
ATOM   1471 N  N    . GLU   A 1 64  ? 34.519 8.744   7.167   1.00 11.71 ?  64  GLU   A N    1 
ATOM   1472 C  CA   . GLU   A 1 64  ? 35.286 7.507   7.265   1.00 11.60 ?  64  GLU   A CA   1 
ATOM   1473 C  C    . GLU   A 1 64  ? 35.369 6.812   5.911   1.00 11.51 ?  64  GLU   A C    1 
ATOM   1474 O  O    . GLU   A 1 64  ? 36.418 6.273   5.529   1.00 11.86 ?  64  GLU   A O    1 
ATOM   1475 C  CB   . GLU   A 1 64  ? 34.604 6.603   8.292   1.00 12.25 ?  64  GLU   A CB   1 
ATOM   1476 C  CG   . GLU   A 1 64  ? 35.272 5.266   8.478   1.00 13.22 ?  64  GLU   A CG   1 
ATOM   1477 C  CD   . GLU   A 1 64  ? 34.393 4.266   9.197   1.00 13.94 ?  64  GLU   A CD   1 
ATOM   1478 O  OE1  . GLU   A 1 64  ? 33.152 4.357   9.062   1.00 15.04 ?  64  GLU   A OE1  1 
ATOM   1479 O  OE2  . GLU   A 1 64  ? 34.944 3.364   9.872   1.00 14.22 -1 64  GLU   A OE2  1 
ATOM   1480 H  H    . GLU   A 1 64  ? 33.793 8.749   7.629   1.00 14.05 ?  64  GLU   A H    1 
ATOM   1481 H  HA   . GLU   A 1 64  ? 36.186 7.707   7.575   1.00 13.91 ?  64  GLU   A HA   1 
ATOM   1482 H  HB2  . GLU   A 1 64  ? 34.608 7.059   9.156   1.00 14.69 ?  64  GLU   A HB2  1 
ATOM   1483 H  HB3  . GLU   A 1 64  ? 33.692 6.452   8.012   1.00 14.69 ?  64  GLU   A HB3  1 
ATOM   1484 H  HG2  . GLU   A 1 64  ? 35.499 4.895   7.612   1.00 15.85 ?  64  GLU   A HG2  1 
ATOM   1485 H  HG3  . GLU   A 1 64  ? 36.076 5.389   9.006   1.00 15.85 ?  64  GLU   A HG3  1 
ATOM   1486 N  N    . SER   A 1 65  ? 34.252 6.812   5.177   1.00 11.14 ?  65  SER   A N    1 
ATOM   1487 C  CA   . SER   A 1 65  ? 34.199 6.149   3.879   1.00 10.95 ?  65  SER   A CA   1 
ATOM   1488 C  C    . SER   A 1 65  ? 35.118 6.816   2.864   1.00 11.12 ?  65  SER   A C    1 
ATOM   1489 O  O    . SER   A 1 65  ? 35.763 6.134   2.060   1.00 12.05 ?  65  SER   A O    1 
ATOM   1490 C  CB   . SER   A 1 65  ? 32.765 6.148   3.354   1.00 10.98 ?  65  SER   A CB   1 
ATOM   1491 O  OG   . SER   A 1 65  ? 31.918 5.338   4.162   1.00 11.58 ?  65  SER   A OG   1 
ATOM   1492 H  H    . SER   A 1 65  ? 33.520 7.194   5.412   1.00 13.36 ?  65  SER   A H    1 
ATOM   1493 H  HA   . SER   A 1 65  ? 34.486 5.231   3.982   1.00 13.13 ?  65  SER   A HA   1 
ATOM   1494 H  HB2  . SER   A 1 65  ? 32.429 7.056   3.355   1.00 13.17 ?  65  SER   A HB2  1 
ATOM   1495 H  HB3  . SER   A 1 65  ? 32.768 5.795   2.451   1.00 13.17 ?  65  SER   A HB3  1 
ATOM   1496 H  HG   . SER   A 1 65  ? 31.915 5.634   4.954   1.00 13.89 ?  65  SER   A HG   1 
ATOM   1497 N  N    . ASP   A 1 66  ? 35.187 8.149   2.872   1.00 11.38 ?  66  ASP   A N    1 
ATOM   1498 C  CA   . ASP   A 1 66  ? 36.055 8.842   1.924   1.00 12.15 ?  66  ASP   A CA   1 
ATOM   1499 C  C    . ASP   A 1 66  ? 37.518 8.486   2.163   1.00 12.25 ?  66  ASP   A C    1 
ATOM   1500 O  O    . ASP   A 1 66  ? 38.290 8.311   1.210   1.00 13.26 ?  66  ASP   A O    1 
ATOM   1501 C  CB   . ASP   A 1 66  ? 35.840 10.352  2.018   1.00 13.75 ?  66  ASP   A CB   1 
ATOM   1502 C  CG   . ASP   A 1 66  ? 34.505 10.812  1.420   1.00 15.37 ?  66  ASP   A CG   1 
ATOM   1503 O  OD1  . ASP   A 1 66  ? 33.794 10.008  0.774   1.00 15.72 ?  66  ASP   A OD1  1 
ATOM   1504 O  OD2  . ASP   A 1 66  ? 34.189 12.010  1.576   1.00 18.39 -1 66  ASP   A OD2  1 
ATOM   1505 H  H    . ASP   A 1 66  ? 34.739 8.666   3.398   1.00 13.65 ?  66  ASP   A H    1 
ATOM   1506 H  HA   . ASP   A 1 66  ? 35.821 8.561   1.025   1.00 14.57 ?  66  ASP   A HA   1 
ATOM   1507 H  HB2  . ASP   A 1 66  ? 35.850 10.618  2.947   1.00 16.49 ?  66  ASP   A HB2  1 
ATOM   1508 H  HB3  . ASP   A 1 66  ? 36.551 10.800  1.533   1.00 16.49 ?  66  ASP   A HB3  1 
ATOM   1509 N  N    . ASP   A 1 67  ? 37.916 8.360   3.429   1.00 12.58 ?  67  ASP   A N    1 
ATOM   1510 C  CA   . ASP   A 1 67  ? 39.272 7.913   3.728   1.00 13.54 ?  67  ASP   A CA   1 
ATOM   1511 C  C    . ASP   A 1 67  ? 39.494 6.477   3.260   1.00 13.38 ?  67  ASP   A C    1 
ATOM   1512 O  O    . ASP   A 1 67  ? 40.556 6.150   2.716   1.00 13.94 ?  67  ASP   A O    1 
ATOM   1513 C  CB   . ASP   A 1 67  ? 39.545 8.049   5.223   1.00 15.05 ?  67  ASP   A CB   1 
ATOM   1514 C  CG   . ASP   A 1 67  ? 40.842 7.386   5.637   1.00 16.30 ?  67  ASP   A CG   1 
ATOM   1515 O  OD1  . ASP   A 1 67  ? 41.915 8.021   5.493   1.00 19.27 ?  67  ASP   A OD1  1 
ATOM   1516 O  OD2  . ASP   A 1 67  ? 40.792 6.223   6.099   1.00 15.54 -1 67  ASP   A OD2  1 
ATOM   1517 H  H    . ASP   A 1 67  ? 37.432 8.533   4.118   1.00 15.09 ?  67  ASP   A H    1 
ATOM   1518 H  HA   . ASP   A 1 67  ? 39.901 8.481   3.255   1.00 16.24 ?  67  ASP   A HA   1 
ATOM   1519 H  HB2  . ASP   A 1 67  ? 39.600 8.989   5.447   1.00 18.05 ?  67  ASP   A HB2  1 
ATOM   1520 H  HB3  . ASP   A 1 67  ? 38.821 7.629   5.713   1.00 18.05 ?  67  ASP   A HB3  1 
ATOM   1521 N  N    . TYR   A 1 68  ? 38.499 5.602   3.451   1.00 13.04 ?  68  TYR   A N    1 
ATOM   1522 C  CA   . TYR   A 1 68  ? 38.618 4.223   2.980   1.00 12.64 ?  68  TYR   A CA   1 
ATOM   1523 C  C    . TYR   A 1 68  ? 38.852 4.175   1.473   1.00 12.33 ?  68  TYR   A C    1 
ATOM   1524 O  O    . TYR   A 1 68  ? 39.728 3.440   0.996   1.00 13.20 ?  68  TYR   A O    1 
ATOM   1525 C  CB   . TYR   A 1 68  ? 37.371 3.402   3.361   1.00 13.31 ?  68  TYR   A CB   1 
ATOM   1526 C  CG   . TYR   A 1 68  ? 37.403 2.012   2.736   1.00 14.92 ?  68  TYR   A CG   1 
ATOM   1527 C  CD1  . TYR   A 1 68  ? 36.944 1.811   1.439   1.00 16.26 ?  68  TYR   A CD1  1 
ATOM   1528 C  CD2  . TYR   A 1 68  ? 37.953 0.930   3.406   1.00 17.22 ?  68  TYR   A CD2  1 
ATOM   1529 C  CE1  . TYR   A 1 68  ? 37.014 0.589   0.830   1.00 17.67 ?  68  TYR   A CE1  1 
ATOM   1530 C  CE2  . TYR   A 1 68  ? 38.015 -0.332  2.798   1.00 17.76 ?  68  TYR   A CE2  1 
ATOM   1531 C  CZ   . TYR   A 1 68  ? 37.554 -0.476  1.511   1.00 18.05 ?  68  TYR   A CZ   1 
ATOM   1532 O  OH   . TYR   A 1 68  ? 37.637 -1.691  0.893   1.00 19.88 ?  68  TYR   A OH   1 
ATOM   1533 H  H    . TYR   A 1 68  ? 37.753 5.781   3.850   1.00 15.64 ?  68  TYR   A H    1 
ATOM   1534 H  HA   . TYR   A 1 68  ? 39.380 3.812   3.412   1.00 15.16 ?  68  TYR   A HA   1 
ATOM   1535 H  HB2  . TYR   A 1 68  ? 37.336 3.300   4.325   1.00 15.97 ?  68  TYR   A HB2  1 
ATOM   1536 H  HB3  . TYR   A 1 68  ? 36.575 3.861   3.044   1.00 15.97 ?  68  TYR   A HB3  1 
ATOM   1537 H  HD1  . TYR   A 1 68  ? 36.589 2.535   0.969   1.00 19.51 ?  68  TYR   A HD1  1 
ATOM   1538 H  HD2  . TYR   A 1 68  ? 38.284 1.041   4.266   1.00 20.65 ?  68  TYR   A HD2  1 
ATOM   1539 H  HE1  . TYR   A 1 68  ? 36.695 0.482   -0.039  1.00 21.20 ?  68  TYR   A HE1  1 
ATOM   1540 H  HE2  . TYR   A 1 68  ? 38.391 -1.057  3.240   1.00 21.31 ?  68  TYR   A HE2  1 
ATOM   1541 H  HH   . TYR   A 1 68  ? 37.979 -2.254  1.413   1.00 23.85 ?  68  TYR   A HH   1 
ATOM   1542 N  N    . ILE   A 1 69  ? 38.068 4.937   0.703   1.00 12.12 ?  69  ILE   A N    1 
ATOM   1543 C  CA   . ILE   A 1 69  ? 38.205 4.918   -0.753  1.00 12.56 ?  69  ILE   A CA   1 
ATOM   1544 C  C    . ILE   A 1 69  ? 39.538 5.527   -1.184  1.00 12.33 ?  69  ILE   A C    1 
ATOM   1545 O  O    . ILE   A 1 69  ? 40.186 5.046   -2.121  1.00 12.70 ?  69  ILE   A O    1 
ATOM   1546 C  CB   . ILE   A 1 69  ? 37.007 5.633   -1.411  1.00 13.32 ?  69  ILE   A CB   1 
ATOM   1547 C  CG1  . ILE   A 1 69  ? 35.690 4.903   -1.134  1.00 13.79 ?  69  ILE   A CG1  1 
ATOM   1548 C  CG2  . ILE   A 1 69  ? 37.243 5.815   -2.915  1.00 15.01 ?  69  ILE   A CG2  1 
ATOM   1549 C  CD1  . ILE   A 1 69  ? 35.533 3.604   -1.890  1.00 14.48 ?  69  ILE   A CD1  1 
ATOM   1550 H  H    . ILE   A 1 69  ? 37.460 5.471   0.999   1.00 14.54 ?  69  ILE   A H    1 
ATOM   1551 H  HA   . ILE   A 1 69  ? 38.196 3.996   -1.048  1.00 15.07 ?  69  ILE   A HA   1 
ATOM   1552 H  HB   . ILE   A 1 69  ? 36.941 6.514   -1.018  1.00 15.97 ?  69  ILE   A HB   1 
ATOM   1553 H  HG12 . ILE   A 1 69  ? 35.644 4.703   -0.183  1.00 16.54 ?  69  ILE   A HG12 1 
ATOM   1554 H  HG13 . ILE   A 1 69  ? 34.956 5.486   -1.379  1.00 16.54 ?  69  ILE   A HG13 1 
ATOM   1555 H  HG21 . ILE   A 1 69  ? 36.397 6.021   -3.345  1.00 18.00 ?  69  ILE   A HG21 1 
ATOM   1556 H  HG22 . ILE   A 1 69  ? 37.865 6.551   -3.053  1.00 18.00 ?  69  ILE   A HG22 1 
ATOM   1557 H  HG23 . ILE   A 1 69  ? 37.610 4.999   -3.283  1.00 18.00 ?  69  ILE   A HG23 1 
ATOM   1558 H  HD11 . ILE   A 1 69  ? 34.730 3.161   -1.579  1.00 17.37 ?  69  ILE   A HD11 1 
ATOM   1559 H  HD12 . ILE   A 1 69  ? 35.457 3.800   -2.837  1.00 17.37 ?  69  ILE   A HD12 1 
ATOM   1560 H  HD13 . ILE   A 1 69  ? 36.306 3.046   -1.725  1.00 17.37 ?  69  ILE   A HD13 1 
ATOM   1561 N  N    . ALA   A 1 70  ? 39.956 6.605   -0.527  1.00 12.51 ?  70  ALA   A N    1 
ATOM   1562 C  CA   . ALA   A 1 70  ? 41.232 7.218   -0.878  1.00 13.71 ?  70  ALA   A CA   1 
ATOM   1563 C  C    . ALA   A 1 70  ? 42.389 6.242   -0.704  1.00 14.21 ?  70  ALA   A C    1 
ATOM   1564 O  O    . ALA   A 1 70  ? 43.368 6.300   -1.454  1.00 15.72 ?  70  ALA   A O    1 
ATOM   1565 C  CB   . ALA   A 1 70  ? 41.456 8.468   -0.027  1.00 14.39 ?  70  ALA   A CB   1 
ATOM   1566 H  H    . ALA   A 1 70  ? 39.522 6.998   0.103   1.00 15.00 ?  70  ALA   A H    1 
ATOM   1567 H  HA   . ALA   A 1 70  ? 41.205 7.497   -1.809  1.00 16.45 ?  70  ALA   A HA   1 
ATOM   1568 H  HB1  . ALA   A 1 70  ? 42.312 8.863   -0.268  1.00 17.26 ?  70  ALA   A HB1  1 
ATOM   1569 H  HB2  . ALA   A 1 70  ? 40.743 9.101   -0.191  1.00 17.26 ?  70  ALA   A HB2  1 
ATOM   1570 H  HB3  . ALA   A 1 70  ? 41.468 8.212   0.910   1.00 17.26 ?  70  ALA   A HB3  1 
ATOM   1571 N  N    . THR   A 1 71  ? 42.289 5.338   0.270   1.00 13.95 ?  71  THR   A N    1 
ATOM   1572 C  CA   . THR   A 1 71  ? 43.339 4.355   0.522   1.00 15.27 ?  71  THR   A CA   1 
ATOM   1573 C  C    . THR   A 1 71  ? 43.218 3.130   -0.373  1.00 15.45 ?  71  THR   A C    1 
ATOM   1574 O  O    . THR   A 1 71  ? 44.232 2.615   -0.861  1.00 17.49 ?  71  THR   A O    1 
ATOM   1575 C  CB   . THR   A 1 71  ? 43.267 3.918   1.981   1.00 17.50 ?  71  THR   A CB   1 
ATOM   1576 O  OG1  . THR   A 1 71  ? 43.529 5.046   2.822   1.00 19.01 ?  71  THR   A OG1  1 
ATOM   1577 C  CG2  . THR   A 1 71  ? 44.259 2.793   2.277   1.00 19.01 ?  71  THR   A CG2  1 
ATOM   1578 H  H    . THR   A 1 71  ? 41.614 5.269   0.796   1.00 16.73 ?  71  THR   A H    1 
ATOM   1579 H  HA   . THR   A 1 71  ? 44.202 4.762   0.362   1.00 18.32 ?  71  THR   A HA   1 
ATOM   1580 H  HB   . THR   A 1 71  ? 42.372 3.582   2.164   1.00 21.00 ?  71  THR   A HB   1 
ATOM   1581 H  HG1  . THR   A 1 71  ? 42.951 5.640   2.684   1.00 22.81 ?  71  THR   A HG1  1 
ATOM   1582 H  HG21 . THR   A 1 71  ? 44.390 2.714   3.235   1.00 22.80 ?  71  THR   A HG21 1 
ATOM   1583 H  HG22 . THR   A 1 71  ? 43.925 1.949   1.936   1.00 22.80 ?  71  THR   A HG22 1 
ATOM   1584 H  HG23 . THR   A 1 71  ? 45.114 2.988   1.860   1.00 22.80 ?  71  THR   A HG23 1 
ATOM   1585 N  N    . ASN   A 1 72  ? 41.995 2.630   -0.573  1.00 14.57 ?  72  ASN   A N    1 
ATOM   1586 C  CA   . ASN   A 1 72  ? 41.777 1.304   -1.137  1.00 14.57 ?  72  ASN   A CA   1 
ATOM   1587 C  C    . ASN   A 1 72  ? 41.160 1.297   -2.525  1.00 14.86 ?  72  ASN   A C    1 
ATOM   1588 O  O    . ASN   A 1 72  ? 41.169 0.243   -3.175  1.00 16.04 ?  72  ASN   A O    1 
ATOM   1589 C  CB   . ASN   A 1 72  ? 40.887 0.477   -0.197  1.00 15.22 ?  72  ASN   A CB   1 
ATOM   1590 C  CG   . ASN   A 1 72  ? 41.500 0.318   1.173   1.00 16.69 ?  72  ASN   A CG   1 
ATOM   1591 O  OD1  . ASN   A 1 72  ? 41.038 0.903   2.149   1.00 18.66 ?  72  ASN   A OD1  1 
ATOM   1592 N  ND2  . ASN   A 1 72  ? 42.559 -0.459  1.249   1.00 17.28 ?  72  ASN   A ND2  1 
ATOM   1593 H  H    . ASN   A 1 72  ? 41.262 3.049   -0.386  1.00 17.48 ?  72  ASN   A H    1 
ATOM   1594 H  HA   . ASN   A 1 72  ? 42.630 0.855   -1.202  1.00 17.48 ?  72  ASN   A HA   1 
ATOM   1595 H  HB2  . ASN   A 1 72  ? 40.031 0.919   -0.095  1.00 18.26 ?  72  ASN   A HB2  1 
ATOM   1596 H  HB3  . ASN   A 1 72  ? 40.765 -0.409  -0.573  1.00 18.26 ?  72  ASN   A HB3  1 
ATOM   1597 H  HD21 . ASN   A 1 72  ? 42.953 -0.574  2.008   1.00 20.73 ?  72  ASN   A HD21 1 
ATOM   1598 H  HD22 . ASN   A 1 72  ? 42.862 -0.845  0.546   1.00 20.73 ?  72  ASN   A HD22 1 
ATOM   1599 N  N    . GLY   A 1 73  ? 40.603 2.411   -2.986  1.00 14.09 ?  73  GLY   A N    1 
ATOM   1600 C  CA   . GLY   A 1 73  ? 39.861 2.421   -4.223  1.00 13.84 ?  73  GLY   A CA   1 
ATOM   1601 C  C    . GLY   A 1 73  ? 38.469 1.840   -4.053  1.00 13.06 ?  73  GLY   A C    1 
ATOM   1602 O  O    . GLY   A 1 73  ? 38.085 1.393   -2.969  1.00 13.86 ?  73  GLY   A O    1 
ATOM   1603 H  H    . GLY   A 1 73  ? 40.646 3.186   -2.600  1.00 16.90 ?  73  GLY   A H    1 
ATOM   1604 H  HA2  . GLY   A 1 73  ? 39.780 3.335   -4.544  1.00 16.60 ?  73  GLY   A HA2  1 
ATOM   1605 H  HA3  . GLY   A 1 73  ? 40.334 1.901   -4.889  1.00 16.60 ?  73  GLY   A HA3  1 
ATOM   1606 N  N    . PRO   A 1 74  ? 37.687 1.856   -5.129  1.00 13.64 ?  74  PRO   A N    1 
ATOM   1607 C  CA   . PRO   A 1 74  ? 36.288 1.426   -5.041  1.00 13.49 ?  74  PRO   A CA   1 
ATOM   1608 C  C    . PRO   A 1 74  ? 36.139 -0.053  -4.715  1.00 13.15 ?  74  PRO   A C    1 
ATOM   1609 O  O    . PRO   A 1 74  ? 37.006 -0.885  -5.001  1.00 14.27 ?  74  PRO   A O    1 
ATOM   1610 C  CB   . PRO   A 1 74  ? 35.739 1.719   -6.443  1.00 15.17 ?  74  PRO   A CB   1 
ATOM   1611 C  CG   . PRO   A 1 74  ? 36.690 2.705   -7.051  1.00 17.85 ?  74  PRO   A CG   1 
ATOM   1612 C  CD   . PRO   A 1 74  ? 38.027 2.378   -6.463  1.00 15.61 ?  74  PRO   A CD   1 
ATOM   1613 H  HA   . PRO   A 1 74  ? 35.805 1.957   -4.385  1.00 16.19 ?  74  PRO   A HA   1 
ATOM   1614 H  HB2  . PRO   A 1 74  ? 35.713 0.899   -6.959  1.00 18.19 ?  74  PRO   A HB2  1 
ATOM   1615 H  HB3  . PRO   A 1 74  ? 34.848 2.104   -6.369  1.00 18.19 ?  74  PRO   A HB3  1 
ATOM   1616 H  HG2  . PRO   A 1 74  ? 36.705 2.592   -8.013  1.00 21.42 ?  74  PRO   A HG2  1 
ATOM   1617 H  HG3  . PRO   A 1 74  ? 36.424 3.605   -6.814  1.00 21.42 ?  74  PRO   A HG3  1 
ATOM   1618 H  HD2  . PRO   A 1 74  ? 38.479 1.697   -6.988  1.00 18.73 ?  74  PRO   A HD2  1 
ATOM   1619 H  HD3  . PRO   A 1 74  ? 38.568 3.185   -6.393  1.00 18.73 ?  74  PRO   A HD3  1 
ATOM   1620 N  N    . LEU   A 1 75  ? 34.994 -0.372  -4.122  1.00 12.36 ?  75  LEU   A N    1 
ATOM   1621 C  CA   . LEU   A 1 75  ? 34.595 -1.759  -3.970  1.00 11.91 ?  75  LEU   A CA   1 
ATOM   1622 C  C    . LEU   A 1 75  ? 34.206 -2.341  -5.328  1.00 12.21 ?  75  LEU   A C    1 
ATOM   1623 O  O    . LEU   A 1 75  ? 34.077 -1.632  -6.329  1.00 14.11 ?  75  LEU   A O    1 
ATOM   1624 C  CB   . LEU   A 1 75  ? 33.411 -1.880  -3.014  1.00 12.10 ?  75  LEU   A CB   1 
ATOM   1625 C  CG   . LEU   A 1 75  ? 33.629 -1.477  -1.559  1.00 13.75 ?  75  LEU   A CG   1 
ATOM   1626 C  CD1  . LEU   A 1 75  ? 32.352 -1.690  -0.752  1.00 15.85 ?  75  LEU   A CD1  1 
ATOM   1627 C  CD2  . LEU   A 1 75  ? 34.776 -2.206  -0.924  1.00 17.09 ?  75  LEU   A CD2  1 
ATOM   1628 H  H    . LEU   A 1 75  ? 34.431 0.200   -3.804  1.00 14.82 ?  75  LEU   A H    1 
ATOM   1629 H  HA   . LEU   A 1 75  ? 35.339 -2.268  -3.619  1.00 14.28 ?  75  LEU   A HA   1 
ATOM   1630 H  HB2  . LEU   A 1 75  ? 32.690 -1.336  -3.357  1.00 14.52 ?  75  LEU   A HB2  1 
ATOM   1631 H  HB3  . LEU   A 1 75  ? 33.131 -2.813  -3.010  1.00 14.52 ?  75  LEU   A HB3  1 
ATOM   1632 H  HG   . LEU   A 1 75  ? 33.838 -0.531  -1.531  1.00 16.50 ?  75  LEU   A HG   1 
ATOM   1633 H  HD11 . LEU   A 1 75  ? 32.511 -1.422  0.168   1.00 19.02 ?  75  LEU   A HD11 1 
ATOM   1634 H  HD12 . LEU   A 1 75  ? 31.644 -1.148  -1.135  1.00 19.02 ?  75  LEU   A HD12 1 
ATOM   1635 H  HD13 . LEU   A 1 75  ? 32.108 -2.627  -0.786  1.00 19.02 ?  75  LEU   A HD13 1 
ATOM   1636 H  HD21 . LEU   A 1 75  ? 34.821 -1.972  0.017   1.00 20.51 ?  75  LEU   A HD21 1 
ATOM   1637 H  HD22 . LEU   A 1 75  ? 34.638 -3.162  -1.020  1.00 20.51 ?  75  LEU   A HD22 1 
ATOM   1638 H  HD23 . LEU   A 1 75  ? 35.602 -1.947  -1.366  1.00 20.51 ?  75  LEU   A HD23 1 
ATOM   1639 N  N    . LYS   A 1 76  ? 34.035 -3.662  -5.348  1.00 12.68 ?  76  LYS   A N    1 
ATOM   1640 C  CA   . LYS   A 1 76  ? 33.438 -4.379  -6.469  1.00 13.31 ?  76  LYS   A CA   1 
ATOM   1641 C  C    . LYS   A 1 76  ? 31.926 -4.473  -6.273  1.00 12.15 ?  76  LYS   A C    1 
ATOM   1642 O  O    . LYS   A 1 76  ? 31.444 -4.592  -5.147  1.00 12.06 ?  76  LYS   A O    1 
ATOM   1643 C  CB   . LYS   A 1 76  ? 33.988 -5.816  -6.527  1.00 15.12 ?  76  LYS   A CB   1 
ATOM   1644 C  CG   . LYS   A 1 76  ? 35.495 -5.920  -6.739  1.00 16.20 ?  76  LYS   A CG   1 
ATOM   1645 C  CD   . LYS   A 1 76  ? 36.016 -7.324  -6.493  1.00 17.62 ?  76  LYS   A CD   1 
ATOM   1646 C  CE   . LYS   A 1 76  ? 37.510 -7.389  -6.714  1.00 20.21 ?  76  LYS   A CE   1 
ATOM   1647 N  NZ   . LYS   A 1 76  ? 38.040 -8.735  -6.448  1.00 21.31 ?  76  LYS   A NZ   1 
ATOM   1648 H  H    . LYS   A 1 76  ? 34.266 -4.182  -4.700  1.00 15.21 ?  76  LYS   A H    1 
ATOM   1649 H  HA   . LYS   A 1 76  ? 33.635 -3.927  -7.306  1.00 15.96 ?  76  LYS   A HA   1 
ATOM   1650 H  HB2  . LYS   A 1 76  ? 33.781 -6.260  -5.690  1.00 18.14 ?  76  LYS   A HB2  1 
ATOM   1651 H  HB3  . LYS   A 1 76  ? 33.557 -6.282  -7.260  1.00 18.14 ?  76  LYS   A HB3  1 
ATOM   1652 H  HG2  . LYS   A 1 76  ? 35.704 -5.675  -7.656  1.00 19.44 ?  76  LYS   A HG2  1 
ATOM   1653 H  HG3  . LYS   A 1 76  ? 35.945 -5.317  -6.125  1.00 19.44 ?  76  LYS   A HG3  1 
ATOM   1654 H  HD2  . LYS   A 1 76  ? 35.827 -7.579  -5.576  1.00 21.14 ?  76  LYS   A HD2  1 
ATOM   1655 H  HD3  . LYS   A 1 76  ? 35.585 -7.938  -7.109  1.00 21.14 ?  76  LYS   A HD3  1 
ATOM   1656 H  HE2  . LYS   A 1 76  ? 37.704 -7.161  -7.636  1.00 24.25 ?  76  LYS   A HE2  1 
ATOM   1657 H  HE3  . LYS   A 1 76  ? 37.947 -6.767  -6.113  1.00 24.25 ?  76  LYS   A HE3  1 
ATOM   1658 H  HZ1  . LYS   A 1 76  ? 38.917 -8.756  -6.586  1.00 25.57 ?  76  LYS   A HZ1  1 
ATOM   1659 H  HZ2  . LYS   A 1 76  ? 37.873 -8.974  -5.606  1.00 25.57 ?  76  LYS   A HZ2  1 
ATOM   1660 H  HZ3  . LYS   A 1 76  ? 37.652 -9.332  -6.992  1.00 25.57 ?  76  LYS   A HZ3  1 
ATOM   1661 N  N    . VAL   A 1 77  ? 31.173 -4.444  -7.378  1.00 12.37 ?  77  VAL   A N    1 
ATOM   1662 C  CA   . VAL   A 1 77  ? 29.766 -4.836  -7.289  1.00 12.19 ?  77  VAL   A CA   1 
ATOM   1663 C  C    . VAL   A 1 77  ? 29.702 -6.289  -6.841  1.00 11.92 ?  77  VAL   A C    1 
ATOM   1664 O  O    . VAL   A 1 77  ? 30.362 -7.159  -7.421  1.00 12.22 ?  77  VAL   A O    1 
ATOM   1665 C  CB   . VAL   A 1 77  ? 29.038 -4.625  -8.624  1.00 13.32 ?  77  VAL   A CB   1 
ATOM   1666 C  CG1  . VAL   A 1 77  ? 27.579 -5.065  -8.501  1.00 14.52 ?  77  VAL   A CG1  1 
ATOM   1667 C  CG2  . VAL   A 1 77  ? 29.122 -3.173  -9.058  1.00 14.65 ?  77  VAL   A CG2  1 
ATOM   1668 H  H    . VAL   A 1 77  ? 31.451 -4.214  -8.162  1.00 14.84 ?  77  VAL   A H    1 
ATOM   1669 H  HA   . VAL   A 1 77  ? 29.333 -4.289  -6.618  1.00 14.62 ?  77  VAL   A HA   1 
ATOM   1670 H  HB   . VAL   A 1 77  ? 29.465 -5.166  -9.309  1.00 15.98 ?  77  VAL   A HB   1 
ATOM   1671 H  HG11 . VAL   A 1 77  ? 27.098 -4.765  -9.285  1.00 17.41 ?  77  VAL   A HG11 1 
ATOM   1672 H  HG12 . VAL   A 1 77  ? 27.548 -6.031  -8.440  1.00 17.41 ?  77  VAL   A HG12 1 
ATOM   1673 H  HG13 . VAL   A 1 77  ? 27.202 -4.665  -7.704  1.00 17.41 ?  77  VAL   A HG13 1 
ATOM   1674 H  HG21 . VAL   A 1 77  ? 28.611 -3.059  -9.875  1.00 17.57 ?  77  VAL   A HG21 1 
ATOM   1675 H  HG22 . VAL   A 1 77  ? 28.751 -2.615  -8.356  1.00 17.57 ?  77  VAL   A HG22 1 
ATOM   1676 H  HG23 . VAL   A 1 77  ? 30.050 -2.939  -9.212  1.00 17.57 ?  77  VAL   A HG23 1 
ATOM   1677 N  N    . GLY   A 1 78  ? 28.921 -6.555  -5.789  1.00 11.89 ?  78  GLY   A N    1 
ATOM   1678 C  CA   . GLY   A 1 78  ? 28.907 -7.844  -5.130  1.00 12.24 ?  78  GLY   A CA   1 
ATOM   1679 C  C    . GLY   A 1 78  ? 29.831 -7.933  -3.935  1.00 11.57 ?  78  GLY   A C    1 
ATOM   1680 O  O    . GLY   A 1 78  ? 29.772 -8.930  -3.201  1.00 12.20 ?  78  GLY   A O    1 
ATOM   1681 H  H    . GLY   A 1 78  ? 28.375 -5.980  -5.447  1.00 14.26 ?  78  GLY   A H    1 
ATOM   1682 H  HA2  . GLY   A 1 78  ? 28.006 -8.033  -4.833  1.00 14.69 ?  78  GLY   A HA2  1 
ATOM   1683 H  HA3  . GLY   A 1 78  ? 29.167 -8.525  -5.770  1.00 14.69 ?  78  GLY   A HA3  1 
ATOM   1684 N  N    . GLY   A 1 79  ? 30.680 -6.922  -3.717  1.00 11.66 ?  79  GLY   A N    1 
ATOM   1685 C  CA   . GLY   A 1 79  ? 31.649 -6.935  -2.646  1.00 11.95 ?  79  GLY   A CA   1 
ATOM   1686 C  C    . GLY   A 1 79  ? 31.203 -6.134  -1.428  1.00 11.20 ?  79  GLY   A C    1 
ATOM   1687 O  O    . GLY   A 1 79  ? 30.091 -5.617  -1.348  1.00 11.62 ?  79  GLY   A O    1 
ATOM   1688 H  H    . GLY   A 1 79  ? 30.711 -6.205  -4.196  1.00 13.99 ?  79  GLY   A H    1 
ATOM   1689 H  HA2  . GLY   A 1 79  ? 31.806 -7.856  -2.370  1.00 14.33 ?  79  GLY   A HA2  1 
ATOM   1690 H  HA3  . GLY   A 1 79  ? 32.487 -6.569  -2.964  1.00 14.33 ?  79  GLY   A HA3  1 
ATOM   1691 N  N    . SER   A 1 80  ? 32.111 -6.039  -0.460  1.00 11.97 ?  80  SER   A N    1 
ATOM   1692 C  CA   . SER   A 1 80  ? 31.794 -5.406  0.811   1.00 11.29 ?  80  SER   A CA   1 
ATOM   1693 C  C    . SER   A 1 80  ? 33.069 -4.957  1.510   1.00 11.45 ?  80  SER   A C    1 
ATOM   1694 O  O    . SER   A 1 80  ? 34.180 -5.393  1.183   1.00 12.81 ?  80  SER   A O    1 
ATOM   1695 C  CB   . SER   A 1 80  ? 31.041 -6.370  1.734   1.00 12.14 ?  80  SER   A CB   1 
ATOM   1696 O  OG   . SER   A 1 80  ? 31.879 -7.414  2.212   1.00 14.24 ?  80  SER   A OG   1 
ATOM   1697 H  H    . SER   A 1 80  ? 32.921 -6.318  -0.522  1.00 14.36 ?  80  SER   A H    1 
ATOM   1698 H  HA   . SER   A 1 80  ? 31.237 -4.628  0.641   1.00 13.55 ?  80  SER   A HA   1 
ATOM   1699 H  HB2  . SER   A 1 80  ? 30.697 -5.873  2.491   1.00 14.57 ?  80  SER   A HB2  1 
ATOM   1700 H  HB3  . SER   A 1 80  ? 30.303 -6.763  1.237   1.00 14.57 ?  80  SER   A HB3  1 
ATOM   1701 H  HG   . SER   A 1 80  ? 32.186 -7.846  1.555   1.00 17.09 ?  80  SER   A HG   1 
ATOM   1702 N  N    . CYS   A 1 81  ? 32.881 -4.107  2.519   1.00 11.23 ?  81  CYS   A N    1 
ATOM   1703 C  CA   . CYS   A 1 81  ? 33.928 -3.816  3.485   1.00 11.08 ?  81  CYS   A CA   1 
ATOM   1704 C  C    . CYS   A 1 81  ? 33.285 -3.579  4.844   1.00 11.15 ?  81  CYS   A C    1 
ATOM   1705 O  O    . CYS   A 1 81  ? 32.119 -3.176  4.934   1.00 12.29 ?  81  CYS   A O    1 
ATOM   1706 C  CB   . CYS   A 1 81  ? 34.793 -2.618  3.069   1.00 12.27 ?  81  CYS   A CB   1 
ATOM   1707 S  SG   . CYS   A 1 81  ? 33.900 -1.051  3.079   1.00 12.31 ?  81  CYS   A SG   1 
ATOM   1708 H  H    . CYS   A 1 81  ? 32.143 -3.685  2.667   1.00 13.47 ?  81  CYS   A H    1 
ATOM   1709 H  HA   . CYS   A 1 81  ? 34.511 -4.587  3.557   1.00 13.29 ?  81  CYS   A HA   1 
ATOM   1710 H  HB2  . CYS   A 1 81  ? 35.544 -2.543  3.684   1.00 14.71 ?  81  CYS   A HB2  1 
ATOM   1711 H  HB3  . CYS   A 1 81  ? 35.131 -2.770  2.168   1.00 14.71 ?  81  CYS   A HB3  1 
ATOM   1712 H  HG   . CYS   A 1 81  ? 34.652 -0.172  2.742   1.00 14.77 ?  81  CYS   A HG   1 
ATOM   1713 N  N    . VAL   A 1 82  ? 34.056 -3.843  5.897   1.00 11.52 ?  82  VAL   A N    1 
ATOM   1714 C  CA   . VAL   A 1 82  ? 33.640 -3.603  7.272   1.00 11.94 ?  82  VAL   A CA   1 
ATOM   1715 C  C    . VAL   A 1 82  ? 34.240 -2.288  7.742   1.00 12.11 ?  82  VAL   A C    1 
ATOM   1716 O  O    . VAL   A 1 82  ? 35.465 -2.112  7.727   1.00 13.12 ?  82  VAL   A O    1 
ATOM   1717 C  CB   . VAL   A 1 82  ? 34.062 -4.750  8.204   1.00 13.76 ?  82  VAL   A CB   1 
ATOM   1718 C  CG1  . VAL   A 1 82  ? 33.629 -4.454  9.636   1.00 15.07 ?  82  VAL   A CG1  1 
ATOM   1719 C  CG2  . VAL   A 1 82  ? 33.491 -6.074  7.726   1.00 14.72 ?  82  VAL   A CG2  1 
ATOM   1720 H  H    . VAL   A 1 82  ? 34.852 -4.185  5.835   1.00 13.82 ?  82  VAL   A H    1 
ATOM   1721 H  HA   . VAL   A 1 82  ? 32.673 -3.524  7.298   1.00 14.32 ?  82  VAL   A HA   1 
ATOM   1722 H  HB   . VAL   A 1 82  ? 35.027 -4.815  8.194   1.00 16.51 ?  82  VAL   A HB   1 
ATOM   1723 H  HG11 . VAL   A 1 82  ? 33.722 -5.262  10.164  1.00 18.08 ?  82  VAL   A HG11 1 
ATOM   1724 H  HG12 . VAL   A 1 82  ? 34.189 -3.753  10.004  1.00 18.08 ?  82  VAL   A HG12 1 
ATOM   1725 H  HG13 . VAL   A 1 82  ? 32.700 -4.168  9.635   1.00 18.08 ?  82  VAL   A HG13 1 
ATOM   1726 H  HG21 . VAL   A 1 82  ? 33.739 -6.768  8.357   1.00 17.66 ?  82  VAL   A HG21 1 
ATOM   1727 H  HG22 . VAL   A 1 82  ? 32.525 -6.003  7.675   1.00 17.66 ?  82  VAL   A HG22 1 
ATOM   1728 H  HG23 . VAL   A 1 82  ? 33.855 -6.278  6.850   1.00 17.66 ?  82  VAL   A HG23 1 
ATOM   1729 N  N    . LEU   A 1 83  ? 33.382 -1.364  8.159   1.00 11.74 ?  83  LEU   A N    1 
ATOM   1730 C  CA   . LEU   A 1 83  ? 33.802 -0.095  8.736   1.00 11.62 ?  83  LEU   A CA   1 
ATOM   1731 C  C    . LEU   A 1 83  ? 33.088 0.088   10.071  1.00 11.86 ?  83  LEU   A C    1 
ATOM   1732 O  O    . LEU   A 1 83  ? 32.363 -0.798  10.538  1.00 12.56 ?  83  LEU   A O    1 
ATOM   1733 C  CB   . LEU   A 1 83  ? 33.548 1.063   7.760   1.00 12.07 ?  83  LEU   A CB   1 
ATOM   1734 C  CG   . LEU   A 1 83  ? 34.442 1.062   6.510   1.00 13.02 ?  83  LEU   A CG   1 
ATOM   1735 C  CD1  . LEU   A 1 83  ? 33.999 2.108   5.507   1.00 13.50 ?  83  LEU   A CD1  1 
ATOM   1736 C  CD2  . LEU   A 1 83  ? 35.914 1.272   6.873   1.00 13.83 ?  83  LEU   A CD2  1 
ATOM   1737 H  H    . LEU   A 1 83  ? 32.528 -1.449  8.113   1.00 14.09 ?  83  LEU   A H    1 
ATOM   1738 H  HA   . LEU   A 1 83  ? 34.755 -0.122  8.910   1.00 13.94 ?  83  LEU   A HA   1 
ATOM   1739 H  HB2  . LEU   A 1 83  ? 32.626 1.025   7.455   1.00 14.48 ?  83  LEU   A HB2  1 
ATOM   1740 H  HB3  . LEU   A 1 83  ? 33.697 1.907   8.220   1.00 14.48 ?  83  LEU   A HB3  1 
ATOM   1741 H  HG   . LEU   A 1 83  ? 34.369 0.195   6.084   1.00 15.62 ?  83  LEU   A HG   1 
ATOM   1742 H  HD11 . LEU   A 1 83  ? 34.583 2.067   4.731   1.00 16.20 ?  83  LEU   A HD11 1 
ATOM   1743 H  HD12 . LEU   A 1 83  ? 33.085 1.919   5.240   1.00 16.20 ?  83  LEU   A HD12 1 
ATOM   1744 H  HD13 . LEU   A 1 83  ? 34.052 2.983   5.916   1.00 16.20 ?  83  LEU   A HD13 1 
ATOM   1745 H  HD21 . LEU   A 1 83  ? 36.426 1.411   6.058   1.00 16.59 ?  83  LEU   A HD21 1 
ATOM   1746 H  HD22 . LEU   A 1 83  ? 35.993 2.054   7.445   1.00 16.59 ?  83  LEU   A HD22 1 
ATOM   1747 H  HD23 . LEU   A 1 83  ? 36.246 0.489   7.339   1.00 16.59 ?  83  LEU   A HD23 1 
ATOM   1748 N  N    . SER   A 1 84  ? 33.312 1.236   10.704  1.00 12.44 ?  84  SER   A N    1 
ATOM   1749 C  CA   . SER   A 1 84  ? 32.665 1.498   11.982  1.00 12.73 ?  84  SER   A CA   1 
ATOM   1750 C  C    . SER   A 1 84  ? 31.146 1.580   11.832  1.00 12.66 ?  84  SER   A C    1 
ATOM   1751 O  O    . SER   A 1 84  ? 30.623 2.052   10.823  1.00 12.84 ?  84  SER   A O    1 
ATOM   1752 C  CB   . SER   A 1 84  ? 33.168 2.818   12.558  1.00 13.98 ?  84  SER   A CB   1 
ATOM   1753 O  OG   . SER   A 1 84  ? 32.524 3.110   13.781  1.00 14.39 ?  84  SER   A OG   1 
ATOM   1754 H  H    . SER   A 1 84  ? 33.814 1.875   10.411  1.00 14.93 ?  84  SER   A H    1 
ATOM   1755 H  HA   . SER   A 1 84  ? 32.880 0.784   12.597  1.00 15.27 ?  84  SER   A HA   1 
ATOM   1756 H  HB2  . SER   A 1 84  ? 34.127 2.751   12.696  1.00 16.77 ?  84  SER   A HB2  1 
ATOM   1757 H  HB3  . SER   A 1 84  ? 32.976 3.527   11.923  1.00 16.77 ?  84  SER   A HB3  1 
ATOM   1758 H  HG   . SER   A 1 84  ? 32.821 3.829   14.090  1.00 17.26 ?  84  SER   A HG   1 
ATOM   1759 N  N    . GLY   A 1 85  ? 30.438 1.171   12.883  1.00 13.09 ?  85  GLY   A N    1 
ATOM   1760 C  CA   . GLY   A 1 85  ? 29.015 1.409   12.973  1.00 14.19 ?  85  GLY   A CA   1 
ATOM   1761 C  C    . GLY   A 1 85  ? 28.640 2.724   13.621  1.00 13.68 ?  85  GLY   A C    1 
ATOM   1762 O  O    . GLY   A 1 85  ? 27.450 3.037   13.736  1.00 14.43 ?  85  GLY   A O    1 
ATOM   1763 H  H    . GLY   A 1 85  ? 30.772 0.756   13.560  1.00 15.71 ?  85  GLY   A H    1 
ATOM   1764 H  HA2  . GLY   A 1 85  ? 28.640 1.391   12.077  1.00 17.03 ?  85  GLY   A HA2  1 
ATOM   1765 H  HA3  . GLY   A 1 85  ? 28.610 0.699   13.484  1.00 17.03 ?  85  GLY   A HA3  1 
ATOM   1766 N  N    . HIS   A 1 86  ? 29.623 3.504   14.060  1.00 13.07 ?  86  HIS   A N    1 
ATOM   1767 C  CA   . HIS   A 1 86  ? 29.391 4.844   14.617  1.00 13.87 ?  86  HIS   A CA   1 
ATOM   1768 C  C    . HIS   A 1 86  ? 28.408 4.727   15.776  1.00 14.31 ?  86  HIS   A C    1 
ATOM   1769 O  O    . HIS   A 1 86  ? 28.604 3.858   16.640  1.00 15.61 ?  86  HIS   A O    1 
ATOM   1770 C  CB   . HIS   A 1 86  ? 29.009 5.815   13.506  1.00 13.88 ?  86  HIS   A CB   1 
ATOM   1771 C  CG   . HIS   A 1 86  ? 30.065 5.917   12.467  1.00 13.96 ?  86  HIS   A CG   1 
ATOM   1772 N  ND1  . HIS   A 1 86  ? 31.150 6.758   12.595  1.00 15.25 ?  86  HIS   A ND1  1 
ATOM   1773 C  CD2  . HIS   A 1 86  ? 30.250 5.229   11.319  1.00 13.63 ?  86  HIS   A CD2  1 
ATOM   1774 C  CE1  . HIS   A 1 86  ? 31.949 6.591   11.557  1.00 15.05 ?  86  HIS   A CE1  1 
ATOM   1775 N  NE2  . HIS   A 1 86  ? 31.429 5.667   10.771  1.00 14.50 ?  86  HIS   A NE2  1 
ATOM   1776 H  H    . HIS   A 1 86  ? 30.446 3.285   14.050  1.00 15.68 ?  86  HIS   A H    1 
ATOM   1777 H  HA   . HIS   A 1 86  ? 30.224 5.164   14.987  1.00 16.64 ?  86  HIS   A HA   1 
ATOM   1778 H  HB2  . HIS   A 1 86  ? 28.189 5.517   13.077  1.00 16.66 ?  86  HIS   A HB2  1 
ATOM   1779 H  HB3  . HIS   A 1 86  ? 28.874 6.705   13.882  1.00 16.66 ?  86  HIS   A HB3  1 
ATOM   1780 H  HD2  . HIS   A 1 86  ? 29.688 4.572   10.966  1.00 16.36 ?  86  HIS   A HD2  1 
ATOM   1781 H  HE1  . HIS   A 1 86  ? 32.739 7.054   11.393  1.00 18.06 ?  86  HIS   A HE1  1 
ATOM   1782 H  HE2  . HIS   A 1 86  ? 31.766 5.394   10.021  1.00 17.39 ?  86  HIS   A HE2  1 
ATOM   1783 N  N    . ASN   A 1 87  ? 27.389 5.573   15.842  1.00 15.41 ?  87  ASN   A N    1 
ATOM   1784 C  CA   . ASN   A 1 87  ? 26.405 5.557   16.909  1.00 16.33 ?  87  ASN   A CA   1 
ATOM   1785 C  C    . ASN   A 1 87  ? 25.290 4.547   16.678  1.00 17.85 ?  87  ASN   A C    1 
ATOM   1786 O  O    . ASN   A 1 87  ? 24.375 4.466   17.503  1.00 20.09 ?  87  ASN   A O    1 
ATOM   1787 C  CB   . ASN   A 1 87  ? 25.799 6.959   17.067  1.00 17.52 ?  87  ASN   A CB   1 
ATOM   1788 C  CG   . ASN   A 1 87  ? 25.285 7.528   15.753  1.00 17.90 ?  87  ASN   A CG   1 
ATOM   1789 O  OD1  . ASN   A 1 87  ? 25.932 7.414   14.716  1.00 18.17 ?  87  ASN   A OD1  1 
ATOM   1790 N  ND2  . ASN   A 1 87  ? 24.120 8.152   15.797  1.00 18.66 ?  87  ASN   A ND2  1 
ATOM   1791 H  H    . ASN   A 1 87  ? 27.240 6.186   15.259  1.00 18.48 ?  87  ASN   A H    1 
ATOM   1792 H  HA   . ASN   A 1 87  ? 26.845 5.327   17.748  1.00 19.59 ?  87  ASN   A HA   1 
ATOM   1793 H  HB2  . ASN   A 1 87  ? 25.053 6.911   17.691  1.00 21.02 ?  87  ASN   A HB2  1 
ATOM   1794 H  HB3  . ASN   A 1 87  ? 26.478 7.559   17.412  1.00 21.02 ?  87  ASN   A HB3  1 
ATOM   1795 H  HD21 . ASN   A 1 87  ? 23.788 8.488   15.080  1.00 22.39 ?  87  ASN   A HD21 1 
ATOM   1796 H  HD22 . ASN   A 1 87  ? 23.697 8.223   16.543  1.00 22.39 ?  87  ASN   A HD22 1 
ATOM   1797 N  N    . LEU   A 1 88  ? 25.346 3.772   15.598  1.00 16.51 ?  88  LEU   A N    1 
ATOM   1798 C  CA   . LEU   A 1 88  ? 24.240 2.904   15.206  1.00 16.44 ?  88  LEU   A CA   1 
ATOM   1799 C  C    . LEU   A 1 88  ? 24.465 1.427   15.506  1.00 16.14 ?  88  LEU   A C    1 
ATOM   1800 O  O    . LEU   A 1 88  ? 23.491 0.685   15.658  1.00 16.92 ?  88  LEU   A O    1 
ATOM   1801 C  CB   . LEU   A 1 88  ? 23.989 3.053   13.705  1.00 16.81 ?  88  LEU   A CB   1 
ATOM   1802 C  CG   . LEU   A 1 88  ? 23.690 4.476   13.228  1.00 18.35 ?  88  LEU   A CG   1 
ATOM   1803 C  CD1  . LEU   A 1 88  ? 23.514 4.499   11.720  1.00 18.68 ?  88  LEU   A CD1  1 
ATOM   1804 C  CD2  . LEU   A 1 88  ? 22.463 5.050   13.930  1.00 19.91 ?  88  LEU   A CD2  1 
ATOM   1805 H  H    . LEU   A 1 88  ? 26.027 3.726   15.082  1.00 19.80 ?  88  LEU   A H    1 
ATOM   1806 H  HA   . LEU   A 1 88  ? 23.442 3.185   15.678  1.00 19.72 ?  88  LEU   A HA   1 
ATOM   1807 H  HB2  . LEU   A 1 88  ? 24.774 2.748   13.229  1.00 20.17 ?  88  LEU   A HB2  1 
ATOM   1808 H  HB3  . LEU   A 1 88  ? 23.228 2.503   13.468  1.00 20.17 ?  88  LEU   A HB3  1 
ATOM   1809 H  HG   . LEU   A 1 88  ? 24.446 5.044   13.444  1.00 22.02 ?  88  LEU   A HG   1 
ATOM   1810 H  HD11 . LEU   A 1 88  ? 23.346 5.412   11.435  1.00 22.41 ?  88  LEU   A HD11 1 
ATOM   1811 H  HD12 . LEU   A 1 88  ? 24.323 4.166   11.302  1.00 22.41 ?  88  LEU   A HD12 1 
ATOM   1812 H  HD13 . LEU   A 1 88  ? 22.761 3.936   11.481  1.00 22.41 ?  88  LEU   A HD13 1 
ATOM   1813 H  HD21 . LEU   A 1 88  ? 22.232 5.896   13.516  1.00 23.89 ?  88  LEU   A HD21 1 
ATOM   1814 H  HD22 . LEU   A 1 88  ? 21.730 4.424   13.842  1.00 23.89 ?  88  LEU   A HD22 1 
ATOM   1815 H  HD23 . LEU   A 1 88  ? 22.674 5.186   14.867  1.00 23.89 ?  88  LEU   A HD23 1 
ATOM   1816 N  N    . ALA   A 1 89  ? 25.714 0.983   15.569  1.00 15.36 ?  89  ALA   A N    1 
ATOM   1817 C  CA   . ALA   A 1 89  ? 26.060 -0.429  15.651  1.00 14.93 ?  89  ALA   A CA   1 
ATOM   1818 C  C    . ALA   A 1 89  ? 27.544 -0.487  15.972  1.00 15.27 ?  89  ALA   A C    1 
ATOM   1819 O  O    . ALA   A 1 89  ? 28.251 0.513   15.855  1.00 16.15 ?  89  ALA   A O    1 
ATOM   1820 C  CB   . ALA   A 1 89  ? 25.792 -1.130  14.319  1.00 14.20 ?  89  ALA   A CB   1 
ATOM   1821 H  H    . ALA   A 1 89  ? 26.399 1.498   15.564  1.00 18.43 ?  89  ALA   A H    1 
ATOM   1822 H  HA   . ALA   A 1 89  ? 25.557 -0.864  16.359  1.00 17.91 ?  89  ALA   A HA   1 
ATOM   1823 H  HB1  . ALA   A 1 89  ? 26.042 -2.066  14.397  1.00 17.03 ?  89  ALA   A HB1  1 
ATOM   1824 H  HB2  . ALA   A 1 89  ? 24.846 -1.061  14.106  1.00 17.03 ?  89  ALA   A HB2  1 
ATOM   1825 H  HB3  . ALA   A 1 89  ? 26.318 -0.706  13.624  1.00 17.03 ?  89  ALA   A HB3  1 
ATOM   1826 N  N    . LYS   A 1 90  ? 28.025 -1.667  16.357  1.00 15.88 ?  90  LYS   A N    1 
ATOM   1827 C  CA   . LYS   A 1 90  ? 29.470 -1.813  16.503  1.00 16.38 ?  90  LYS   A CA   1 
ATOM   1828 C  C    . LYS   A 1 90  ? 30.165 -1.624  15.158  1.00 15.43 ?  90  LYS   A C    1 
ATOM   1829 O  O    . LYS   A 1 90  ? 31.094 -0.808  15.029  1.00 16.80 ?  90  LYS   A O    1 
ATOM   1830 C  CB   . LYS   A 1 90  ? 29.819 -3.168  17.119  1.00 19.08 ?  90  LYS   A CB   1 
ATOM   1831 C  CG   . LYS   A 1 90  ? 31.310 -3.322  17.404  1.00 23.97 ?  90  LYS   A CG   1 
ATOM   1832 C  CD   . LYS   A 1 90  ? 31.581 -4.564  18.239  1.00 29.46 ?  90  LYS   A CD   1 
ATOM   1833 C  CE   . LYS   A 1 90  ? 32.972 -4.541  18.857  1.00 33.93 ?  90  LYS   A CE   1 
ATOM   1834 N  NZ   . LYS   A 1 90  ? 34.033 -4.968  17.905  1.00 36.72 ?  90  LYS   A NZ   1 
ATOM   1835 H  H    . LYS   A 1 90  ? 27.557 -2.365  16.534  1.00 19.05 ?  90  LYS   A H    1 
ATOM   1836 H  HA   . LYS   A 1 90  ? 29.795 -1.122  17.095  1.00 19.65 ?  90  LYS   A HA   1 
ATOM   1837 H  HB2  . LYS   A 1 90  ? 29.340 -3.262  17.959  1.00 22.90 ?  90  LYS   A HB2  1 
ATOM   1838 H  HB3  . LYS   A 1 90  ? 29.555 -3.873  16.508  1.00 22.90 ?  90  LYS   A HB3  1 
ATOM   1839 H  HG2  . LYS   A 1 90  ? 31.793 -3.405  16.567  1.00 28.76 ?  90  LYS   A HG2  1 
ATOM   1840 H  HG3  . LYS   A 1 90  ? 31.624 -2.547  17.898  1.00 28.76 ?  90  LYS   A HG3  1 
ATOM   1841 H  HD2  . LYS   A 1 90  ? 30.931 -4.615  18.958  1.00 35.35 ?  90  LYS   A HD2  1 
ATOM   1842 H  HD3  . LYS   A 1 90  ? 31.513 -5.350  17.673  1.00 35.35 ?  90  LYS   A HD3  1 
ATOM   1843 H  HE2  . LYS   A 1 90  ? 33.175 -3.638  19.147  1.00 40.71 ?  90  LYS   A HE2  1 
ATOM   1844 H  HE3  . LYS   A 1 90  ? 32.990 -5.144  19.616  1.00 40.71 ?  90  LYS   A HE3  1 
ATOM   1845 H  HZ1  . LYS   A 1 90  ? 33.876 -5.800  17.629  1.00 44.05 ?  90  LYS   A HZ1  1 
ATOM   1846 H  HZ2  . LYS   A 1 90  ? 34.045 -4.427  17.200  1.00 44.05 ?  90  LYS   A HZ2  1 
ATOM   1847 H  HZ3  . LYS   A 1 90  ? 34.828 -4.942  18.305  1.00 44.05 ?  90  LYS   A HZ3  1 
ATOM   1848 N  N    . HIS   A 1 91  ? 29.697 -2.345  14.137  1.00 13.44 ?  91  HIS   A N    1 
ATOM   1849 C  CA   . HIS   A 1 91  ? 30.272 -2.331  12.809  1.00 12.98 ?  91  HIS   A CA   1 
ATOM   1850 C  C    . HIS   A 1 91  ? 29.181 -2.057  11.791  1.00 11.78 ?  91  HIS   A C    1 
ATOM   1851 O  O    . HIS   A 1 91  ? 28.012 -2.413  11.991  1.00 12.78 ?  91  HIS   A O    1 
ATOM   1852 C  CB   . HIS   A 1 91  ? 30.868 -3.701  12.443  1.00 15.87 ?  91  HIS   A CB   1 
ATOM   1853 C  CG   . HIS   A 1 91  ? 31.871 -4.210  13.427  1.00 20.02 ?  91  HIS   A CG   1 
ATOM   1854 N  ND1  . HIS   A 1 91  ? 33.151 -3.709  13.511  1.00 22.23 ?  91  HIS   A ND1  1 
ATOM   1855 C  CD2  . HIS   A 1 91  ? 31.787 -5.187  14.360  1.00 22.13 ?  91  HIS   A CD2  1 
ATOM   1856 C  CE1  . HIS   A 1 91  ? 33.813 -4.352  14.458  1.00 23.48 ?  91  HIS   A CE1  1 
ATOM   1857 N  NE2  . HIS   A 1 91  ? 33.007 -5.256  14.988  1.00 23.47 ?  91  HIS   A NE2  1 
ATOM   1858 H  H    . HIS   A 1 91  ? 29.021 -2.891  14.205  1.00 16.12 ?  91  HIS   A H    1 
ATOM   1859 H  HA   . HIS   A 1 91  ? 30.959 -1.660  12.740  1.00 15.57 ?  91  HIS   A HA   1 
ATOM   1860 H  HB2  . HIS   A 1 91  ? 30.151 -4.356  12.391  1.00 19.03 ?  91  HIS   A HB2  1 
ATOM   1861 H  HB3  . HIS   A 1 91  ? 31.307 -3.632  11.580  1.00 19.03 ?  91  HIS   A HB3  1 
ATOM   1862 H  HD1  . HIS   A 1 91  ? 33.472 -3.077  13.020  1.00 26.67 ?  91  HIS   A HD1  1 
ATOM   1863 H  HD2  . HIS   A 1 91  ? 31.048 -5.715  14.544  1.00 26.55 ?  91  HIS   A HD2  1 
ATOM   1864 H  HE1  . HIS   A 1 91  ? 34.699 -4.191  14.707  1.00 28.17 ?  91  HIS   A HE1  1 
ATOM   1865 N  N    . CYS   A 1 92  ? 29.583 -1.459  10.675  1.00 11.58 ?  92  CYS   A N    1 
ATOM   1866 C  CA   . CYS   A 1 92  ? 28.748 -1.386  9.486   1.00 11.52 ?  92  CYS   A CA   1 
ATOM   1867 C  C    . CYS   A 1 92  ? 29.393 -2.206  8.379   1.00 10.90 ?  92  CYS   A C    1 
ATOM   1868 O  O    . CYS   A 1 92  ? 30.549 -1.954  8.005   1.00 11.89 ?  92  CYS   A O    1 
ATOM   1869 C  CB   . CYS   A 1 92  ? 28.541 0.057   9.019   1.00 12.14 ?  92  CYS   A CB   1 
ATOM   1870 S  SG   . CYS   A 1 92  ? 27.519 0.164   7.513   1.00 11.58 ?  92  CYS   A SG   1 
ATOM   1871 H  H    . CYS   A 1 92  ? 30.349 -1.070  10.584  1.00 13.89 ?  92  CYS   A H    1 
ATOM   1872 H  HA   . CYS   A 1 92  ? 27.881 -1.766  9.680   1.00 13.82 ?  92  CYS   A HA   1 
ATOM   1873 H  HB2  . CYS   A 1 92  ? 28.094 0.558   9.721   1.00 14.57 ?  92  CYS   A HB2  1 
ATOM   1874 H  HB3  . CYS   A 1 92  ? 29.402 0.457   8.822   1.00 14.57 ?  92  CYS   A HB3  1 
ATOM   1875 H  HG   . CYS   A 1 92  ? 27.385 1.316   7.217   1.00 13.89 ?  92  CYS   A HG   1 
ATOM   1876 N  N    . LEU   A 1 93  ? 28.655 -3.194  7.875   1.00 10.93 ?  93  LEU   A N    1 
ATOM   1877 C  CA   . LEU   A 1 93  ? 29.058 -3.953  6.697   1.00 10.71 ?  93  LEU   A CA   1 
ATOM   1878 C  C    . LEU   A 1 93  ? 28.459 -3.262  5.478   1.00 10.20 ?  93  LEU   A C    1 
ATOM   1879 O  O    . LEU   A 1 93  ? 27.244 -3.320  5.258   1.00 10.67 ?  93  LEU   A O    1 
ATOM   1880 C  CB   . LEU   A 1 93  ? 28.582 -5.401  6.806   1.00 11.20 ?  93  LEU   A CB   1 
ATOM   1881 C  CG   . LEU   A 1 93  ? 28.963 -6.304  5.636   1.00 11.49 ?  93  LEU   A CG   1 
ATOM   1882 C  CD1  . LEU   A 1 93  ? 30.468 -6.554  5.605   1.00 12.15 ?  93  LEU   A CD1  1 
ATOM   1883 C  CD2  . LEU   A 1 93  ? 28.188 -7.618  5.701   1.00 12.64 ?  93  LEU   A CD2  1 
ATOM   1884 H  H    . LEU   A 1 93  ? 27.902 -3.443  8.213   1.00 13.11 ?  93  LEU   A H    1 
ATOM   1885 H  HA   . LEU   A 1 93  ? 30.021 -3.942  6.624   1.00 12.84 ?  93  LEU   A HA   1 
ATOM   1886 H  HB2  . LEU   A 1 93  ? 28.961 -5.786  7.614   1.00 13.43 ?  93  LEU   A HB2  1 
ATOM   1887 H  HB3  . LEU   A 1 93  ? 27.615 -5.403  6.873   1.00 13.43 ?  93  LEU   A HB3  1 
ATOM   1888 H  HG   . LEU   A 1 93  ? 28.729 -5.864  4.813   1.00 13.78 ?  93  LEU   A HG   1 
ATOM   1889 H  HD11 . LEU   A 1 93  ? 30.677 -7.163  4.883   1.00 14.57 ?  93  LEU   A HD11 1 
ATOM   1890 H  HD12 . LEU   A 1 93  ? 30.929 -5.708  5.466   1.00 14.57 ?  93  LEU   A HD12 1 
ATOM   1891 H  HD13 . LEU   A 1 93  ? 30.749 -6.939  6.454   1.00 14.57 ?  93  LEU   A HD13 1 
ATOM   1892 H  HD21 . LEU   A 1 93  ? 28.452 -8.178  4.951   1.00 15.16 ?  93  LEU   A HD21 1 
ATOM   1893 H  HD22 . LEU   A 1 93  ? 28.391 -8.071  6.535   1.00 15.16 ?  93  LEU   A HD22 1 
ATOM   1894 H  HD23 . LEU   A 1 93  ? 27.239 -7.427  5.651   1.00 15.16 ?  93  LEU   A HD23 1 
ATOM   1895 N  N    . HIS   A 1 94  ? 29.306 -2.572  4.711   1.00 10.46 ?  94  HIS   A N    1 
ATOM   1896 C  CA   . HIS   A 1 94  ? 28.881 -1.902  3.484   1.00 10.20 ?  94  HIS   A CA   1 
ATOM   1897 C  C    . HIS   A 1 94  ? 28.891 -2.940  2.374   1.00 10.08 ?  94  HIS   A C    1 
ATOM   1898 O  O    . HIS   A 1 94  ? 29.957 -3.456  2.030   1.00 11.77 ?  94  HIS   A O    1 
ATOM   1899 C  CB   . HIS   A 1 94  ? 29.839 -0.758  3.150   1.00 10.36 ?  94  HIS   A CB   1 
ATOM   1900 C  CG   . HIS   A 1 94  ? 29.836 0.341   4.161   1.00 10.35 ?  94  HIS   A CG   1 
ATOM   1901 N  ND1  . HIS   A 1 94  ? 28.955 1.402   4.105   1.00 10.53 ?  94  HIS   A ND1  1 
ATOM   1902 C  CD2  . HIS   A 1 94  ? 30.577 0.516   5.279   1.00 11.28 ?  94  HIS   A CD2  1 
ATOM   1903 C  CE1  . HIS   A 1 94  ? 29.173 2.189   5.143   1.00 10.90 ?  94  HIS   A CE1  1 
ATOM   1904 N  NE2  . HIS   A 1 94  ? 30.149 1.676   5.869   1.00 11.22 ?  94  HIS   A NE2  1 
ATOM   1905 H  H    . HIS   A 1 94  ? 30.145 -2.470  4.887   1.00 12.55 ?  94  HIS   A H    1 
ATOM   1906 H  HA   . HIS   A 1 94  ? 27.981 -1.551  3.587   1.00 12.23 ?  94  HIS   A HA   1 
ATOM   1907 H  HB2  . HIS   A 1 94  ? 30.736 -1.107  3.095   1.00 12.43 ?  94  HIS   A HB2  1 
ATOM   1908 H  HB3  . HIS   A 1 94  ? 29.576 -0.374  2.296   1.00 12.43 ?  94  HIS   A HB3  1 
ATOM   1909 H  HD2  . HIS   A 1 94  ? 31.252 -0.039  5.584   1.00 13.53 ?  94  HIS   A HD2  1 
ATOM   1910 H  HE1  . HIS   A 1 94  ? 28.706 2.975   5.329   1.00 13.08 ?  94  HIS   A HE1  1 
ATOM   1911 H  HE2  . HIS   A 1 94  ? 30.463 2.021   6.590   1.00 13.45 ?  94  HIS   A HE2  1 
ATOM   1912 N  N    . VAL   A 1 95  ? 27.723 -3.264  1.824   1.00 9.73  ?  95  VAL   A N    1 
ATOM   1913 C  CA   . VAL   A 1 95  ? 27.583 -4.298  0.804   1.00 9.82  ?  95  VAL   A CA   1 
ATOM   1914 C  C    . VAL   A 1 95  ? 27.028 -3.665  -0.457  1.00 9.80  ?  95  VAL   A C    1 
ATOM   1915 O  O    . VAL   A 1 95  ? 26.017 -2.953  -0.403  1.00 10.63 ?  95  VAL   A O    1 
ATOM   1916 C  CB   . VAL   A 1 95  ? 26.664 -5.446  1.263   1.00 10.63 ?  95  VAL   A CB   1 
ATOM   1917 C  CG1  . VAL   A 1 95  ? 26.570 -6.493  0.162   1.00 11.64 ?  95  VAL   A CG1  1 
ATOM   1918 C  CG2  . VAL   A 1 95  ? 27.179 -6.054  2.556   1.00 10.90 ?  95  VAL   A CG2  1 
ATOM   1919 H  H    . VAL   A 1 95  ? 26.971 -2.896  2.037   1.00 11.67 ?  95  VAL   A H    1 
ATOM   1920 H  HA   . VAL   A 1 95  ? 28.453 -4.670  0.598   1.00 11.78 ?  95  VAL   A HA   1 
ATOM   1921 H  HB   . VAL   A 1 95  ? 25.775 -5.102  1.423   1.00 12.75 ?  95  VAL   A HB   1 
ATOM   1922 H  HG11 . VAL   A 1 95  ? 26.186 -7.308  0.527   1.00 13.97 ?  95  VAL   A HG11 1 
ATOM   1923 H  HG12 . VAL   A 1 95  ? 26.006 -6.161  -0.555  1.00 13.97 ?  95  VAL   A HG12 1 
ATOM   1924 H  HG13 . VAL   A 1 95  ? 27.461 -6.681  -0.181  1.00 13.97 ?  95  VAL   A HG13 1 
ATOM   1925 H  HG21 . VAL   A 1 95  ? 26.636 -6.825  2.778   1.00 13.07 ?  95  VAL   A HG21 1 
ATOM   1926 H  HG22 . VAL   A 1 95  ? 28.102 -6.321  2.433   1.00 13.07 ?  95  VAL   A HG22 1 
ATOM   1927 H  HG23 . VAL   A 1 95  ? 27.115 -5.389  3.258   1.00 13.07 ?  95  VAL   A HG23 1 
ATOM   1928 N  N    . VAL   A 1 96  ? 27.653 -3.954  -1.595  1.00 9.54  ?  96  VAL   A N    1 
ATOM   1929 C  CA   . VAL   A 1 96  ? 27.235 -3.404  -2.878  1.00 10.60 ?  96  VAL   A CA   1 
ATOM   1930 C  C    . VAL   A 1 96  ? 26.431 -4.458  -3.632  1.00 10.86 ?  96  VAL   A C    1 
ATOM   1931 O  O    . VAL   A 1 96  ? 26.993 -5.402  -4.196  1.00 11.84 ?  96  VAL   A O    1 
ATOM   1932 C  CB   . VAL   A 1 96  ? 28.428 -2.932  -3.709  1.00 11.08 ?  96  VAL   A CB   1 
ATOM   1933 C  CG1  . VAL   A 1 96  ? 27.924 -2.302  -4.986  1.00 11.49 ?  96  VAL   A CG1  1 
ATOM   1934 C  CG2  . VAL   A 1 96  ? 29.291 -1.958  -2.926  1.00 11.65 ?  96  VAL   A CG2  1 
ATOM   1935 H  H    . VAL   A 1 96  ? 28.348 -4.466  -1.650  1.00 11.44 ?  96  VAL   A H    1 
ATOM   1936 H  HA   . VAL   A 1 96  ? 26.660 -2.639  -2.723  1.00 12.71 ?  96  VAL   A HA   1 
ATOM   1937 H  HB   . VAL   A 1 96  ? 28.973 -3.695  -3.949  1.00 13.30 ?  96  VAL   A HB   1 
ATOM   1938 H  HG11 . VAL   A 1 96  ? 28.657 -1.829  -5.412  1.00 13.78 ?  96  VAL   A HG11 1 
ATOM   1939 H  HG12 . VAL   A 1 96  ? 27.590 -2.993  -5.575  1.00 13.78 ?  96  VAL   A HG12 1 
ATOM   1940 H  HG13 . VAL   A 1 96  ? 27.214 -1.675  -4.769  1.00 13.78 ?  96  VAL   A HG13 1 
ATOM   1941 H  HG21 . VAL   A 1 96  ? 29.989 -1.616  -3.503  1.00 13.97 ?  96  VAL   A HG21 1 
ATOM   1942 H  HG22 . VAL   A 1 96  ? 28.734 -1.225  -2.611  1.00 13.97 ?  96  VAL   A HG22 1 
ATOM   1943 H  HG23 . VAL   A 1 96  ? 29.681 -2.420  -2.168  1.00 13.97 ?  96  VAL   A HG23 1 
ATOM   1944 N  N    . GLY   A 1 97  ? 25.115 -4.298  -3.667  1.00 11.02 ?  97  GLY   A N    1 
ATOM   1945 C  CA   . GLY   A 1 97  ? 24.302 -5.072  -4.571  1.00 11.34 ?  97  GLY   A CA   1 
ATOM   1946 C  C    . GLY   A 1 97  ? 24.301 -4.427  -5.943  1.00 11.28 ?  97  GLY   A C    1 
ATOM   1947 O  O    . GLY   A 1 97  ? 24.578 -3.231  -6.088  1.00 12.22 ?  97  GLY   A O    1 
ATOM   1948 H  H    . GLY   A 1 97  ? 24.670 -3.747  -3.169  1.00 13.22 ?  97  GLY   A H    1 
ATOM   1949 H  HA2  . GLY   A 1 97  ? 24.660 -5.971  -4.624  1.00 13.61 ?  97  GLY   A HA2  1 
ATOM   1950 H  HA3  . GLY   A 1 97  ? 23.389 -5.117  -4.241  1.00 13.61 ?  97  GLY   A HA3  1 
ATOM   1951 N  N    A PRO   A 1 98  ? 23.951 -5.182  -6.980  0.68 11.40 ?  98  PRO   A N    1 
ATOM   1952 N  N    B PRO   A 1 98  ? 24.031 -5.225  -6.975  0.32 11.59 ?  98  PRO   A N    1 
ATOM   1953 C  CA   A PRO   A 1 98  ? 23.830 -4.570  -8.309  0.68 12.35 ?  98  PRO   A CA   1 
ATOM   1954 C  CA   B PRO   A 1 98  ? 23.978 -4.681  -8.334  0.32 12.43 ?  98  PRO   A CA   1 
ATOM   1955 C  C    A PRO   A 1 98  ? 22.719 -3.527  -8.341  0.68 12.37 ?  98  PRO   A C    1 
ATOM   1956 C  C    B PRO   A 1 98  ? 22.836 -3.689  -8.491  0.32 12.90 ?  98  PRO   A C    1 
ATOM   1957 O  O    A PRO   A 1 98  ? 21.645 -3.711  -7.764  0.68 12.81 ?  98  PRO   A O    1 
ATOM   1958 O  O    B PRO   A 1 98  ? 21.770 -3.825  -7.886  0.32 13.84 ?  98  PRO   A O    1 
ATOM   1959 C  CB   A PRO   A 1 98  ? 23.513 -5.761  -9.222  0.68 12.59 ?  98  PRO   A CB   1 
ATOM   1960 C  CB   B PRO   A 1 98  ? 23.756 -5.925  -9.205  0.32 12.39 ?  98  PRO   A CB   1 
ATOM   1961 C  CG   A PRO   A 1 98  ? 22.885 -6.780  -8.315  0.68 12.44 ?  98  PRO   A CG   1 
ATOM   1962 C  CG   B PRO   A 1 98  ? 23.150 -6.938  -8.274  0.32 12.59 ?  98  PRO   A CG   1 
ATOM   1963 C  CD   A PRO   A 1 98  ? 23.611 -6.618  -6.996  0.68 12.00 ?  98  PRO   A CD   1 
ATOM   1964 C  CD   B PRO   A 1 98  ? 23.818 -6.683  -6.956  0.32 11.73 ?  98  PRO   A CD   1 
ATOM   1965 H  HA   A PRO   A 1 98  ? 24.671 -4.168  -8.574  0.68 14.81 ?  98  PRO   A HA   1 
ATOM   1966 H  HA   B PRO   A 1 98  ? 24.822 -4.261  -8.571  0.32 14.91 ?  98  PRO   A HA   1 
ATOM   1967 H  HB2  A PRO   A 1 98  ? 22.890 -5.484  -9.912  0.68 15.10 ?  98  PRO   A HB2  1 
ATOM   1968 H  HB2  B PRO   A 1 98  ? 23.145 -5.714  -9.927  0.32 14.86 ?  98  PRO   A HB2  1 
ATOM   1969 H  HB3  A PRO   A 1 98  ? 24.332 -6.102  -9.613  0.68 15.10 ?  98  PRO   A HB3  1 
ATOM   1970 H  HB3  B PRO   A 1 98  ? 24.604 -6.244  -9.551  0.32 14.86 ?  98  PRO   A HB3  1 
ATOM   1971 H  HG2  A PRO   A 1 98  ? 21.941 -6.594  -8.214  0.68 14.93 ?  98  PRO   A HG2  1 
ATOM   1972 H  HG2  B PRO   A 1 98  ? 22.192 -6.792  -8.208  0.32 15.10 ?  98  PRO   A HG2  1 
ATOM   1973 H  HG3  A PRO   A 1 98  ? 23.026 -7.670  -8.677  0.68 14.93 ?  98  PRO   A HG3  1 
ATOM   1974 H  HG3  B PRO   A 1 98  ? 23.340 -7.834  -8.591  0.32 15.10 ?  98  PRO   A HG3  1 
ATOM   1975 H  HD2  A PRO   A 1 98  ? 23.019 -6.839  -6.255  0.68 14.40 ?  98  PRO   A HD2  1 
ATOM   1976 H  HD2  B PRO   A 1 98  ? 23.231 -6.935  -6.223  0.32 14.07 ?  98  PRO   A HD2  1 
ATOM   1977 H  HD3  A PRO   A 1 98  ? 24.415 -7.162  -6.978  0.68 14.40 ?  98  PRO   A HD3  1 
ATOM   1978 H  HD3  B PRO   A 1 98  ? 24.666 -7.156  -6.907  0.32 14.07 ?  98  PRO   A HD3  1 
ATOM   1979 N  N    A ASN   A 1 99  ? 22.999 -2.411  -9.011  0.68 13.23 ?  99  ASN   A N    1 
ATOM   1980 N  N    B ASN   A 1 99  ? 23.077 -2.680  -9.316  0.32 13.03 ?  99  ASN   A N    1 
ATOM   1981 C  CA   A ASN   A 1 99  ? 22.019 -1.353  -9.235  0.68 14.45 ?  99  ASN   A CA   1 
ATOM   1982 C  CA   B ASN   A 1 99  ? 22.093 -1.644  -9.605  0.32 13.84 ?  99  ASN   A CA   1 
ATOM   1983 C  C    A ASN   A 1 99  ? 21.463 -1.528  -10.643 0.68 15.78 ?  99  ASN   A C    1 
ATOM   1984 C  C    B ASN   A 1 99  ? 21.482 -1.942  -10.968 0.32 14.84 ?  99  ASN   A C    1 
ATOM   1985 O  O    A ASN   A 1 99  ? 22.148 -1.245  -11.632 0.68 16.92 ?  99  ASN   A O    1 
ATOM   1986 O  O    B ASN   A 1 99  ? 22.161 -1.852  -11.998 0.32 14.71 ?  99  ASN   A O    1 
ATOM   1987 C  CB   A ASN   A 1 99  ? 22.657 0.024   -9.058  0.68 14.51 ?  99  ASN   A CB   1 
ATOM   1988 C  CB   B ASN   A 1 99  ? 22.757 -0.271  -9.594  0.32 14.94 ?  99  ASN   A CB   1 
ATOM   1989 C  CG   A ASN   A 1 99  ? 21.629 1.158   -9.033  0.68 15.16 ?  99  ASN   A CG   1 
ATOM   1990 C  CG   B ASN   A 1 99  ? 21.766 0.859   -9.763  0.32 15.63 ?  99  ASN   A CG   1 
ATOM   1991 O  OD1  A ASN   A 1 99  ? 20.617 1.113   -9.733  0.68 16.01 ?  99  ASN   A OD1  1 
ATOM   1992 O  OD1  B ASN   A 1 99  ? 20.795 0.736   -10.502 0.32 15.55 ?  99  ASN   A OD1  1 
ATOM   1993 N  ND2  A ASN   A 1 99  ? 21.901 2.187   -8.234  0.68 15.18 ?  99  ASN   A ND2  1 
ATOM   1994 N  ND2  B ASN   A 1 99  ? 22.006 1.966   -9.069  0.32 16.33 ?  99  ASN   A ND2  1 
ATOM   1995 H  H    A ASN   A 1 99  ? 23.773 -2.237  -9.340  0.68 15.87 ?  99  ASN   A H    1 
ATOM   1996 H  H    B ASN   A 1 99  ? 23.826 -2.570  -9.721  0.32 15.63 ?  99  ASN   A H    1 
ATOM   1997 H  HA   A ASN   A 1 99  ? 21.291 -1.442  -8.595  0.68 17.33 ?  99  ASN   A HA   1 
ATOM   1998 H  HA   B ASN   A 1 99  ? 21.391 -1.667  -8.932  0.32 16.60 ?  99  ASN   A HA   1 
ATOM   1999 H  HB2  A ASN   A 1 99  ? 23.147 0.044   -8.225  0.68 17.41 ?  99  ASN   A HB2  1 
ATOM   2000 H  HB2  B ASN   A 1 99  ? 23.212 -0.152  -8.751  0.32 17.93 ?  99  ASN   A HB2  1 
ATOM   2001 H  HB3  A ASN   A 1 99  ? 23.263 0.182   -9.803  0.68 17.41 ?  99  ASN   A HB3  1 
ATOM   2002 H  HB3  B ASN   A 1 99  ? 23.388 -0.232  -10.324 0.32 17.93 ?  99  ASN   A HB3  1 
ATOM   2003 H  HD21 A ASN   A 1 99  ? 21.357 2.851   -8.188  0.68 18.22 ?  99  ASN   A HD21 1 
ATOM   2004 H  HD21 B ASN   A 1 99  ? 21.469 2.636   -9.123  0.32 19.59 ?  99  ASN   A HD21 1 
ATOM   2005 H  HD22 A ASN   A 1 99  ? 22.620 2.185   -7.763  0.68 18.22 ?  99  ASN   A HD22 1 
ATOM   2006 H  HD22 B ASN   A 1 99  ? 22.699 2.011   -8.562  0.32 19.59 ?  99  ASN   A HD22 1 
ATOM   2007 N  N    A VAL   A 1 100 ? 20.218 -2.005  -10.727 0.68 17.05 ?  100 VAL   A N    1 
ATOM   2008 N  N    B VAL   A 1 100 ? 20.195 -2.293  -10.965 0.32 16.83 ?  100 VAL   A N    1 
ATOM   2009 C  CA   A VAL   A 1 100 ? 19.586 -2.241  -12.021 0.68 19.26 ?  100 VAL   A CA   1 
ATOM   2010 C  CA   B VAL   A 1 100 ? 19.505 -2.649  -12.202 0.32 18.95 ?  100 VAL   A CA   1 
ATOM   2011 C  C    A VAL   A 1 100 ? 19.467 -0.946  -12.813 0.68 20.38 ?  100 VAL   A C    1 
ATOM   2012 C  C    B VAL   A 1 100 ? 19.509 -1.473  -13.164 0.32 19.78 ?  100 VAL   A C    1 
ATOM   2013 O  O    A VAL   A 1 100 ? 19.548 -0.953  -14.047 0.68 21.19 ?  100 VAL   A O    1 
ATOM   2014 O  O    B VAL   A 1 100 ? 19.618 -1.648  -14.384 0.32 20.20 ?  100 VAL   A O    1 
ATOM   2015 C  CB   A VAL   A 1 100 ? 18.229 -2.954  -11.827 0.68 20.96 ?  100 VAL   A CB   1 
ATOM   2016 C  CB   B VAL   A 1 100 ? 18.070 -3.116  -11.897 0.32 20.42 ?  100 VAL   A CB   1 
ATOM   2017 C  CG1  A VAL   A 1 100 ? 17.470 -3.064  -13.145 0.68 21.15 ?  100 VAL   A CG1  1 
ATOM   2018 C  CG1  B VAL   A 1 100 ? 17.520 -3.925  -13.061 0.32 20.75 ?  100 VAL   A CG1  1 
ATOM   2019 C  CG2  A VAL   A 1 100 ? 18.449 -4.336  -11.224 0.68 20.97 ?  100 VAL   A CG2  1 
ATOM   2020 C  CG2  B VAL   A 1 100 ? 18.035 -3.912  -10.608 0.32 21.08 ?  100 VAL   A CG2  1 
ATOM   2021 H  H    A VAL   A 1 100 ? 19.720 -2.203  -10.048 0.68 20.46 ?  100 VAL   A H    1 
ATOM   2022 H  H    B VAL   A 1 100 ? 19.708 -2.324  -10.257 0.32 20.20 ?  100 VAL   A H    1 
ATOM   2023 H  HA   A VAL   A 1 100 ? 20.149 -2.842  -12.531 0.68 23.11 ?  100 VAL   A HA   1 
ATOM   2024 H  HA   B VAL   A 1 100 ? 19.972 -3.382  -12.632 0.32 22.74 ?  100 VAL   A HA   1 
ATOM   2025 H  HB   A VAL   A 1 100 ? 17.684 -2.443  -11.209 0.68 25.15 ?  100 VAL   A HB   1 
ATOM   2026 H  HB   B VAL   A 1 100 ? 17.503 -2.335  -11.787 0.32 24.50 ?  100 VAL   A HB   1 
ATOM   2027 H  HG11 A VAL   A 1 100 ? 16.732 -3.687  -13.033 0.68 25.38 ?  100 VAL   A HG11 1 
ATOM   2028 H  HG11 B VAL   A 1 100 ? 16.613 -4.198  -12.853 0.32 24.90 ?  100 VAL   A HG11 1 
ATOM   2029 H  HG12 A VAL   A 1 100 ? 17.128 -2.191  -13.390 0.68 25.38 ?  100 VAL   A HG12 1 
ATOM   2030 H  HG12 B VAL   A 1 100 ? 17.525 -3.376  -13.860 0.32 24.90 ?  100 VAL   A HG12 1 
ATOM   2031 H  HG13 A VAL   A 1 100 ? 18.073 -3.392  -13.830 0.68 25.38 ?  100 VAL   A HG13 1 
ATOM   2032 H  HG13 B VAL   A 1 100 ? 18.079 -4.706  -13.193 0.32 24.90 ?  100 VAL   A HG13 1 
ATOM   2033 H  HG21 A VAL   A 1 100 ? 17.593 -4.785  -11.138 0.68 25.15 ?  100 VAL   A HG21 1 
ATOM   2034 H  HG21 B VAL   A 1 100 ? 17.253 -4.477  -10.612 0.32 25.30 ?  100 VAL   A HG21 1 
ATOM   2035 H  HG22 A VAL   A 1 100 ? 19.032 -4.846  -11.809 0.68 25.15 ?  100 VAL   A HG22 1 
ATOM   2036 H  HG22 B VAL   A 1 100 ? 18.839 -4.451  -10.552 0.32 25.30 ?  100 VAL   A HG22 1 
ATOM   2037 H  HG23 A VAL   A 1 100 ? 18.860 -4.238  -10.351 0.68 25.15 ?  100 VAL   A HG23 1 
ATOM   2038 H  HG23 B VAL   A 1 100 ? 17.997 -3.294  -9.859  0.32 25.30 ?  100 VAL   A HG23 1 
ATOM   2039 N  N    A ASN   A 1 101 ? 19.284 0.184   -12.132 0.68 21.49 ?  101 ASN   A N    1 
ATOM   2040 N  N    B ASN   A 1 101 ? 19.369 -0.257  -12.631 0.32 19.90 ?  101 ASN   A N    1 
ATOM   2041 C  CA   A ASN   A 1 101 ? 19.216 1.464   -12.831 0.68 22.68 ?  101 ASN   A CA   1 
ATOM   2042 C  CA   B ASN   A 1 101 ? 19.341 0.936   -13.468 0.32 20.51 ?  101 ASN   A CA   1 
ATOM   2043 C  C    A ASN   A 1 101 ? 20.567 1.903   -13.401 0.68 24.78 ?  101 ASN   A C    1 
ATOM   2044 C  C    B ASN   A 1 101 ? 20.688 1.206   -14.121 0.32 21.37 ?  101 ASN   A C    1 
ATOM   2045 O  O    A ASN   A 1 101 ? 20.625 2.933   -14.086 0.68 26.78 ?  101 ASN   A O    1 
ATOM   2046 O  O    B ASN   A 1 101 ? 20.737 1.872   -15.162 0.32 21.08 ?  101 ASN   A O    1 
ATOM   2047 C  CB   A ASN   A 1 101 ? 18.613 2.527   -11.910 0.68 21.50 ?  101 ASN   A CB   1 
ATOM   2048 C  CB   B ASN   A 1 101 ? 18.903 2.140   -12.630 0.32 20.30 ?  101 ASN   A CB   1 
ATOM   2049 C  CG   A ASN   A 1 101 ? 17.242 2.126   -11.381 0.68 20.83 ?  101 ASN   A CG   1 
ATOM   2050 C  CG   B ASN   A 1 101 ? 17.685 1.839   -11.770 0.32 20.65 ?  101 ASN   A CG   1 
ATOM   2051 O  OD1  A ASN   A 1 101 ? 16.378 1.670   -12.136 0.68 21.49 ?  101 ASN   A OD1  1 
ATOM   2052 O  OD1  B ASN   A 1 101 ? 16.733 1.201   -12.221 0.32 21.31 ?  101 ASN   A OD1  1 
ATOM   2053 N  ND2  A ASN   A 1 101 ? 17.040 2.283   -10.080 0.68 20.16 ?  101 ASN   A ND2  1 
ATOM   2054 N  ND2  B ASN   A 1 101 ? 17.720 2.282   -10.519 0.32 20.63 ?  101 ASN   A ND2  1 
ATOM   2055 H  H    A ASN   A 1 101 ? 19.187 0.232   -11.280 0.68 25.79 ?  101 ASN   A H    1 
ATOM   2056 H  H    B ASN   A 1 101 ? 19.289 -0.099  -11.786 0.32 23.87 ?  101 ASN   A H    1 
ATOM   2057 H  HA   A ASN   A 1 101 ? 18.615 1.363   -13.581 0.68 27.21 ?  101 ASN   A HA   1 
ATOM   2058 H  HA   B ASN   A 1 101 ? 18.691 0.814   -14.172 0.32 24.61 ?  101 ASN   A HA   1 
ATOM   2059 H  HB2  A ASN   A 1 101 ? 19.201 2.664   -11.152 0.68 25.80 ?  101 ASN   A HB2  1 
ATOM   2060 H  HB2  B ASN   A 1 101 ? 19.628 2.403   -12.040 0.32 24.36 ?  101 ASN   A HB2  1 
ATOM   2061 H  HB3  A ASN   A 1 101 ? 18.512 3.354   -12.408 0.68 25.80 ?  101 ASN   A HB3  1 
ATOM   2062 H  HB3  B ASN   A 1 101 ? 18.677 2.876   -13.223 0.32 24.36 ?  101 ASN   A HB3  1 
ATOM   2063 H  HD21 A ASN   A 1 101 ? 16.282 2.067   -9.733  0.68 24.19 ?  101 ASN   A HD21 1 
ATOM   2064 H  HD21 B ASN   A 1 101 ? 17.056 2.136   -9.993  0.32 24.76 ?  101 ASN   A HD21 1 
ATOM   2065 H  HD22 A ASN   A 1 101 ? 17.663 2.604   -9.582  0.68 24.19 ?  101 ASN   A HD22 1 
ATOM   2066 H  HD22 B ASN   A 1 101 ? 18.405 2.720   -10.235 0.32 24.76 ?  101 ASN   A HD22 1 
ATOM   2067 N  N    A LYS   A 1 102 ? 21.638 1.145   -13.147 0.68 26.60 ?  102 LYS   A N    1 
ATOM   2068 N  N    B LYS   A 1 102 ? 21.775 0.705   -13.536 0.32 23.10 ?  102 LYS   A N    1 
ATOM   2069 C  CA   A LYS   A 1 102 ? 22.926 1.338   -13.801 0.68 27.94 ?  102 LYS   A CA   1 
ATOM   2070 C  CA   B LYS   A 1 102 ? 23.109 0.819   -14.107 0.32 24.17 ?  102 LYS   A CA   1 
ATOM   2071 C  C    A LYS   A 1 102 ? 23.241 0.242   -14.810 0.68 27.79 ?  102 LYS   A C    1 
ATOM   2072 C  C    B LYS   A 1 102 ? 23.448 -0.345  -15.033 0.32 23.75 ?  102 LYS   A C    1 
ATOM   2073 O  O    A LYS   A 1 102 ? 24.310 0.279   -15.428 0.68 28.25 ?  102 LYS   A O    1 
ATOM   2074 O  O    B LYS   A 1 102 ? 24.601 -0.472  -15.456 0.32 23.24 ?  102 LYS   A O    1 
ATOM   2075 C  CB   A LYS   A 1 102 ? 24.055 1.401   -12.763 0.68 29.80 ?  102 LYS   A CB   1 
ATOM   2076 C  CB   B LYS   A 1 102 ? 24.154 0.920   -12.989 0.32 25.89 ?  102 LYS   A CB   1 
ATOM   2077 C  CG   A LYS   A 1 102 ? 23.964 2.550   -11.776 0.68 31.46 ?  102 LYS   A CG   1 
ATOM   2078 C  CG   B LYS   A 1 102 ? 24.281 2.315   -12.391 0.32 27.39 ?  102 LYS   A CG   1 
ATOM   2079 C  CD   A LYS   A 1 102 ? 25.140 2.514   -10.805 0.68 33.29 ?  102 LYS   A CD   1 
ATOM   2080 C  CD   B LYS   A 1 102 ? 24.877 2.297   -10.989 0.32 28.96 ?  102 LYS   A CD   1 
ATOM   2081 C  CE   A LYS   A 1 102 ? 25.091 3.661   -9.811  0.68 34.77 ?  102 LYS   A CE   1 
ATOM   2082 C  CE   B LYS   A 1 102 ? 24.955 3.705   -10.414 0.32 30.13 ?  102 LYS   A CE   1 
ATOM   2083 N  NZ   A LYS   A 1 102 ? 26.174 3.555   -8.789  0.68 35.24 ?  102 LYS   A NZ   1 
ATOM   2084 N  NZ   B LYS   A 1 102 ? 24.971 3.723   -8.923  0.32 30.68 ?  102 LYS   A NZ   1 
ATOM   2085 H  H    A LYS   A 1 102 ? 21.640 0.489   -12.587 0.68 31.92 ?  102 LYS   A H    1 
ATOM   2086 H  H    B LYS   A 1 102 ? 21.759 0.278   -12.787 0.32 27.71 ?  102 LYS   A H    1 
ATOM   2087 H  HA   A LYS   A 1 102 ? 22.915 2.181   -14.273 0.68 33.52 ?  102 LYS   A HA   1 
ATOM   2088 H  HA   B LYS   A 1 102 ? 23.153 1.643   -14.616 0.32 29.00 ?  102 LYS   A HA   1 
ATOM   2089 H  HB2  A LYS   A 1 102 ? 24.051 0.578   -12.251 0.68 35.76 ?  102 LYS   A HB2  1 
ATOM   2090 H  HB2  B LYS   A 1 102 ? 23.909 0.310   -12.276 0.32 31.06 ?  102 LYS   A HB2  1 
ATOM   2091 H  HB3  A LYS   A 1 102 ? 24.900 1.488   -13.231 0.68 35.76 ?  102 LYS   A HB3  1 
ATOM   2092 H  HB3  B LYS   A 1 102 ? 25.020 0.673   -13.345 0.32 31.06 ?  102 LYS   A HB3  1 
ATOM   2093 H  HG2  A LYS   A 1 102 ? 23.987 3.392   -12.257 0.68 37.74 ?  102 LYS   A HG2  1 
ATOM   2094 H  HG2  B LYS   A 1 102 ? 24.863 2.849   -12.955 0.32 32.87 ?  102 LYS   A HG2  1 
ATOM   2095 H  HG3  A LYS   A 1 102 ? 23.142 2.474   -11.266 0.68 37.74 ?  102 LYS   A HG3  1 
ATOM   2096 H  HG3  B LYS   A 1 102 ? 23.403 2.720   -12.339 0.32 32.87 ?  102 LYS   A HG3  1 
ATOM   2097 H  HD2  A LYS   A 1 102 ? 25.117 1.681   -10.308 0.68 39.94 ?  102 LYS   A HD2  1 
ATOM   2098 H  HD2  B LYS   A 1 102 ? 24.316 1.764   -10.405 0.32 34.74 ?  102 LYS   A HD2  1 
ATOM   2099 H  HD3  A LYS   A 1 102 ? 25.968 2.581   -11.307 0.68 39.94 ?  102 LYS   A HD3  1 
ATOM   2100 H  HD3  B LYS   A 1 102 ? 25.774 1.929   -11.023 0.32 34.74 ?  102 LYS   A HD3  1 
ATOM   2101 H  HE2  A LYS   A 1 102 ? 25.204 4.500   -10.287 0.68 41.71 ?  102 LYS   A HE2  1 
ATOM   2102 H  HE2  B LYS   A 1 102 ? 25.770 4.129   -10.726 0.32 36.15 ?  102 LYS   A HE2  1 
ATOM   2103 H  HE3  A LYS   A 1 102 ? 24.237 3.650   -9.352  0.68 41.71 ?  102 LYS   A HE3  1 
ATOM   2104 H  HE3  B LYS   A 1 102 ? 24.183 4.211   -10.711 0.32 36.15 ?  102 LYS   A HE3  1 
ATOM   2105 H  HZ1  A LYS   A 1 102 ? 26.124 4.238   -8.221  0.68 42.28 ?  102 LYS   A HZ1  1 
ATOM   2106 H  HZ1  B LYS   A 1 102 ? 25.018 4.563   -8.629  0.32 36.81 ?  102 LYS   A HZ1  1 
ATOM   2107 H  HZ2  A LYS   A 1 102 ? 26.090 2.794   -8.336  0.68 42.28 ?  102 LYS   A HZ2  1 
ATOM   2108 H  HZ2  B LYS   A 1 102 ? 24.227 3.349   -8.606  0.32 36.81 ?  102 LYS   A HZ2  1 
ATOM   2109 H  HZ3  A LYS   A 1 102 ? 26.970 3.568   -9.188  0.68 42.28 ?  102 LYS   A HZ3  1 
ATOM   2110 H  HZ3  B LYS   A 1 102 ? 25.674 3.271   -8.619  0.32 36.81 ?  102 LYS   A HZ3  1 
ATOM   2111 N  N    A GLY   A 1 103 ? 22.351 -0.735  -14.985 0.68 27.90 ?  103 GLY   A N    1 
ATOM   2112 N  N    B GLY   A 1 103 ? 22.475 -1.196  -15.350 0.32 23.73 ?  103 GLY   A N    1 
ATOM   2113 C  CA   A GLY   A 1 103 ? 22.587 -1.832  -15.905 0.68 27.46 ?  103 GLY   A CA   1 
ATOM   2114 C  CA   B GLY   A 1 103 ? 22.729 -2.330  -16.218 0.32 23.50 ?  103 GLY   A CA   1 
ATOM   2115 C  C    A GLY   A 1 103 ? 23.394 -2.984  -15.347 0.68 27.03 ?  103 GLY   A C    1 
ATOM   2116 C  C    B GLY   A 1 103 ? 23.554 -3.435  -15.599 0.32 22.73 ?  103 GLY   A C    1 
ATOM   2117 O  O    A GLY   A 1 103 ? 23.876 -3.817  -16.121 0.68 28.37 ?  103 GLY   A O    1 
ATOM   2118 O  O    B GLY   A 1 103 ? 24.102 -4.270  -16.323 0.32 23.32 ?  103 GLY   A O    1 
ATOM   2119 H  H    A GLY   A 1 103 ? 21.598 -0.777  -14.581 0.68 33.47 ?  103 GLY   A H    1 
ATOM   2120 H  H    B GLY   A 1 103 ? 21.662 -1.129  -15.076 0.32 28.48 ?  103 GLY   A H    1 
ATOM   2121 H  HA2  A GLY   A 1 103 ? 21.729 -2.178  -16.204 0.68 32.95 ?  103 GLY   A HA2  1 
ATOM   2122 H  HA2  B GLY   A 1 103 ? 21.882 -2.706  -16.500 0.32 28.19 ?  103 GLY   A HA2  1 
ATOM   2123 H  HA3  A GLY   A 1 103 ? 23.056 -1.494  -16.684 0.68 32.95 ?  103 GLY   A HA3  1 
ATOM   2124 H  HA3  B GLY   A 1 103 ? 23.193 -2.008  -17.008 0.32 28.19 ?  103 GLY   A HA3  1 
ATOM   2125 N  N    A GLU   A 1 104 ? 23.547 -3.072  -14.030 0.68 24.52 ?  104 GLU   A N    1 
ATOM   2126 N  N    B GLU   A 1 104 ? 23.648 -3.477  -14.275 0.32 21.01 ?  104 GLU   A N    1 
ATOM   2127 C  CA   A GLU   A 1 104 ? 24.423 -4.070  -13.433 0.68 22.81 ?  104 GLU   A CA   1 
ATOM   2128 C  CA   B GLU   A 1 104 ? 24.531 -4.424  -13.615 0.32 19.55 ?  104 GLU   A CA   1 
ATOM   2129 C  C    A GLU   A 1 104 ? 23.738 -5.431  -13.327 0.68 23.18 ?  104 GLU   A C    1 
ATOM   2130 C  C    B GLU   A 1 104 ? 23.852 -5.785  -13.449 0.32 18.43 ?  104 GLU   A C    1 
ATOM   2131 O  O    A GLU   A 1 104 ? 22.526 -5.534  -13.117 0.68 23.61 ?  104 GLU   A O    1 
ATOM   2132 O  O    B GLU   A 1 104 ? 22.624 -5.908  -13.456 0.32 18.42 ?  104 GLU   A O    1 
ATOM   2133 C  CB   A GLU   A 1 104 ? 24.923 -3.576  -12.073 0.68 20.62 ?  104 GLU   A CB   1 
ATOM   2134 C  CB   B GLU   A 1 104 ? 25.003 -3.856  -12.275 0.32 19.66 ?  104 GLU   A CB   1 
ATOM   2135 C  CG   A GLU   A 1 104 ? 25.880 -2.395  -12.241 0.68 19.45 ?  104 GLU   A CG   1 
ATOM   2136 C  CG   B GLU   A 1 104 ? 25.820 -2.574  -12.439 0.32 20.59 ?  104 GLU   A CG   1 
ATOM   2137 C  CD   A GLU   A 1 104 ? 26.219 -1.645  -10.969 0.68 18.39 ?  104 GLU   A CD   1 
ATOM   2138 C  CD   B GLU   A 1 104 ? 26.038 -1.821  -11.141 0.32 21.16 ?  104 GLU   A CD   1 
ATOM   2139 O  OE1  A GLU   A 1 104 ? 25.606 -1.889  -9.913  0.68 16.51 ?  104 GLU   A OE1  1 
ATOM   2140 O  OE1  B GLU   A 1 104 ? 25.618 -2.314  -10.074 0.32 21.67 ?  104 GLU   A OE1  1 
ATOM   2141 O  OE2  A GLU   A 1 104 ? 27.112 -0.772  -11.054 0.68 19.28 -1 104 GLU   A OE2  1 
ATOM   2142 O  OE2  B GLU   A 1 104 ? 26.627 -0.720  -11.195 0.32 21.33 -1 104 GLU   A OE2  1 
ATOM   2143 H  H    A GLU   A 1 104 ? 23.160 -2.558  -13.464 0.68 29.42 ?  104 GLU   A H    1 
ATOM   2144 H  H    B GLU   A 1 104 ? 23.208 -2.966  -13.744 0.32 25.21 ?  104 GLU   A H    1 
ATOM   2145 H  HA   A GLU   A 1 104 ? 25.197 -4.177  -14.005 0.68 27.37 ?  104 GLU   A HA   1 
ATOM   2146 H  HA   B GLU   A 1 104 ? 25.316 -4.549  -14.170 0.32 23.45 ?  104 GLU   A HA   1 
ATOM   2147 H  HB2  A GLU   A 1 104 ? 24.167 -3.286  -11.539 0.68 24.74 ?  104 GLU   A HB2  1 
ATOM   2148 H  HB2  B GLU   A 1 104 ? 24.232 -3.652  -11.726 0.32 23.59 ?  104 GLU   A HB2  1 
ATOM   2149 H  HB3  A GLU   A 1 104 ? 25.397 -4.294  -11.626 0.68 24.74 ?  104 GLU   A HB3  1 
ATOM   2150 H  HB3  B GLU   A 1 104 ? 25.564 -4.514  -11.835 0.32 23.59 ?  104 GLU   A HB3  1 
ATOM   2151 H  HG2  A GLU   A 1 104 ? 26.712 -2.721  -12.613 0.68 23.33 ?  104 GLU   A HG2  1 
ATOM   2152 H  HG2  B GLU   A 1 104 ? 26.691 -2.800  -12.803 0.32 24.70 ?  104 GLU   A HG2  1 
ATOM   2153 H  HG3  A GLU   A 1 104 ? 25.479 -1.754  -12.848 0.68 23.33 ?  104 GLU   A HG3  1 
ATOM   2154 H  HG3  B GLU   A 1 104 ? 25.355 -1.978  -13.047 0.32 24.70 ?  104 GLU   A HG3  1 
ATOM   2155 N  N    A ASP   A 1 105 ? 24.546 -6.482  -13.462 0.68 23.42 ?  105 ASP   A N    1 
ATOM   2156 N  N    B ASP   A 1 105 ? 24.683 -6.813  -13.291 0.32 18.12 ?  105 ASP   A N    1 
ATOM   2157 C  CA   A ASP   A 1 105 ? 24.048 -7.846  -13.603 0.68 24.51 ?  105 ASP   A CA   1 
ATOM   2158 C  CA   B ASP   A 1 105 ? 24.250 -8.206  -13.367 0.32 17.96 ?  105 ASP   A CA   1 
ATOM   2159 C  C    A ASP   A 1 105 ? 23.371 -8.309  -12.317 0.68 22.35 ?  105 ASP   A C    1 
ATOM   2160 C  C    B ASP   A 1 105 ? 23.520 -8.603  -12.087 0.32 16.58 ?  105 ASP   A C    1 
ATOM   2161 O  O    A ASP   A 1 105 ? 24.019 -8.427  -11.275 0.68 20.43 ?  105 ASP   A O    1 
ATOM   2162 O  O    B ASP   A 1 105 ? 24.116 -8.622  -11.005 0.32 15.30 ?  105 ASP   A O    1 
ATOM   2163 C  CB   A ASP   A 1 105 ? 25.220 -8.763  -13.942 0.68 27.76 ?  105 ASP   A CB   1 
ATOM   2164 C  CB   B ASP   A 1 105 ? 25.485 -9.082  -13.578 0.32 19.17 ?  105 ASP   A CB   1 
ATOM   2165 C  CG   A ASP   A 1 105 ? 24.797 -10.202 -14.130 0.68 30.67 ?  105 ASP   A CG   1 
ATOM   2166 C  CG   B ASP   A 1 105 ? 25.151 -10.541 -13.820 0.32 19.95 ?  105 ASP   A CG   1 
ATOM   2167 O  OD1  A ASP   A 1 105 ? 23.578 -10.457 -14.210 0.68 31.37 ?  105 ASP   A OD1  1 
ATOM   2168 O  OD1  B ASP   A 1 105 ? 23.955 -10.896 -13.859 0.32 19.59 ?  105 ASP   A OD1  1 
ATOM   2169 O  OD2  A ASP   A 1 105 ? 25.688 -11.077 -14.197 0.68 32.44 -1 105 ASP   A OD2  1 
ATOM   2170 O  OD2  B ASP   A 1 105 ? 26.106 -11.338 -13.968 0.32 21.23 -1 105 ASP   A OD2  1 
ATOM   2171 H  H    A ASP   A 1 105 ? 25.404 -6.429  -13.465 0.68 28.10 ?  105 ASP   A H    1 
ATOM   2172 H  H    B ASP   A 1 105 ? 25.522 -6.720  -13.130 0.32 21.74 ?  105 ASP   A H    1 
ATOM   2173 H  HA   A ASP   A 1 105 ? 23.402 -7.890  -14.322 0.68 29.41 ?  105 ASP   A HA   1 
ATOM   2174 H  HA   B ASP   A 1 105 ? 23.648 -8.318  -14.119 0.32 21.54 ?  105 ASP   A HA   1 
ATOM   2175 H  HB2  A ASP   A 1 105 ? 25.631 -8.459  -14.768 0.68 33.31 ?  105 ASP   A HB2  1 
ATOM   2176 H  HB2  B ASP   A 1 105 ? 25.980 -8.741  -14.340 0.32 23.00 ?  105 ASP   A HB2  1 
ATOM   2177 H  HB3  A ASP   A 1 105 ? 25.870 -8.731  -13.221 0.68 33.31 ?  105 ASP   A HB3  1 
ATOM   2178 H  HB3  B ASP   A 1 105 ? 26.032 -9.045  -12.782 0.32 23.00 ?  105 ASP   A HB3  1 
ATOM   2179 N  N    A ILE   A 1 106 ? 22.071 -8.607  -12.398 0.68 22.26 ?  106 ILE   A N    1 
ATOM   2180 N  N    B ILE   A 1 106 ? 22.231 -8.934  -12.211 0.32 17.04 ?  106 ILE   A N    1 
ATOM   2181 C  CA   A ILE   A 1 106 ? 21.320 -9.019  -11.218 0.68 21.43 ?  106 ILE   A CA   1 
ATOM   2182 C  CA   B ILE   A 1 106 ? 21.443 -9.328  -11.048 0.32 17.60 ?  106 ILE   A CA   1 
ATOM   2183 C  C    A ILE   A 1 106 ? 21.860 -10.311 -10.625 0.68 20.09 ?  106 ILE   A C    1 
ATOM   2184 C  C    B ILE   A 1 106 ? 21.998 -10.585 -10.395 0.32 17.53 ?  106 ILE   A C    1 
ATOM   2185 O  O    A ILE   A 1 106 ? 21.665 -10.566 -9.433  0.68 19.48 ?  106 ILE   A O    1 
ATOM   2186 O  O    B ILE   A 1 106 ? 21.756 -10.817 -9.206  0.32 17.52 ?  106 ILE   A O    1 
ATOM   2187 C  CB   A ILE   A 1 106 ? 19.809 -9.114  -11.535 0.68 23.16 ?  106 ILE   A CB   1 
ATOM   2188 C  CB   B ILE   A 1 106 ? 19.949 -9.474  -11.422 0.32 19.05 ?  106 ILE   A CB   1 
ATOM   2189 C  CG1  A ILE   A 1 106 ? 18.984 -9.215  -10.249 0.68 24.10 ?  106 ILE   A CG1  1 
ATOM   2190 C  CG1  B ILE   A 1 106 ? 19.068 -9.515  -10.168 0.32 19.71 ?  106 ILE   A CG1  1 
ATOM   2191 C  CG2  A ILE   A 1 106 ? 19.522 -10.312 -12.419 0.68 23.84 ?  106 ILE   A CG2  1 
ATOM   2192 C  CG2  B ILE   A 1 106 ? 19.717 -10.715 -12.263 0.32 19.65 ?  106 ILE   A CG2  1 
ATOM   2193 C  CD1  A ILE   A 1 106 ? 19.172 -8.047  -9.303  0.68 24.56 ?  106 ILE   A CD1  1 
ATOM   2194 C  CD1  B ILE   A 1 106 ? 18.912 -8.174  -9.479  0.32 19.81 ?  106 ILE   A CD1  1 
ATOM   2195 H  H    A ILE   A 1 106 ? 21.611 -8.577  -13.117 0.68 26.71 ?  106 ILE   A H    1 
ATOM   2196 H  H    B ILE   A 1 106 ? 21.796 -8.933  -12.949 0.32 20.44 ?  106 ILE   A H    1 
ATOM   2197 H  HA   A ILE   A 1 106 ? 21.436 -8.340  -10.541 0.68 25.71 ?  106 ILE   A HA   1 
ATOM   2198 H  HA   B ILE   A 1 106 ? 21.505 -8.627  -10.386 0.32 21.11 ?  106 ILE   A HA   1 
ATOM   2199 H  HB   A ILE   A 1 106 ? 19.546 -8.312  -12.008 0.68 27.79 ?  106 ILE   A HB   1 
ATOM   2200 H  HB   B ILE   A 1 106 ? 19.693 -8.699  -11.944 0.32 22.85 ?  106 ILE   A HB   1 
ATOM   2201 H  HG12 A ILE   A 1 106 ? 18.044 -9.253  -10.484 0.68 28.92 ?  106 ILE   A HG12 1 
ATOM   2202 H  HG12 B ILE   A 1 106 ? 18.182 -9.818  -10.420 0.32 23.64 ?  106 ILE   A HG12 1 
ATOM   2203 H  HG13 A ILE   A 1 106 ? 19.236 -10.022 -9.775  0.68 28.92 ?  106 ILE   A HG13 1 
ATOM   2204 H  HG13 B ILE   A 1 106 ? 19.453 -10.131 -9.527  0.32 23.64 ?  106 ILE   A HG13 1 
ATOM   2205 H  HG21 A ILE   A 1 106 ? 18.629 -10.222 -12.785 0.68 28.61 ?  106 ILE   A HG21 1 
ATOM   2206 H  HG21 B ILE   A 1 106 ? 18.827 -10.670 -12.646 0.32 23.58 ?  106 ILE   A HG21 1 
ATOM   2207 H  HG22 A ILE   A 1 106 ? 20.175 -10.336 -13.133 0.68 28.61 ?  106 ILE   A HG22 1 
ATOM   2208 H  HG22 B ILE   A 1 106 ? 20.381 -10.743 -12.967 0.32 23.58 ?  106 ILE   A HG22 1 
ATOM   2209 H  HG23 A ILE   A 1 106 ? 19.583 -11.119 -11.885 0.68 28.61 ?  106 ILE   A HG23 1 
ATOM   2210 H  HG23 B ILE   A 1 106 ? 19.795 -11.499 -11.698 0.32 23.58 ?  106 ILE   A HG23 1 
ATOM   2211 H  HD11 A ILE   A 1 106 ? 18.440 -8.034  -8.670  0.68 29.47 ?  106 ILE   A HD11 1 
ATOM   2212 H  HD11 B ILE   A 1 106 ? 18.275 -8.265  -8.751  0.32 23.76 ?  106 ILE   A HD11 1 
ATOM   2213 H  HD12 A ILE   A 1 106 ? 20.015 -8.153  -8.832  0.68 29.47 ?  106 ILE   A HD12 1 
ATOM   2214 H  HD12 B ILE   A 1 106 ? 19.772 -7.893  -9.130  0.32 23.76 ?  106 ILE   A HD12 1 
ATOM   2215 H  HD13 A ILE   A 1 106 ? 19.181 -7.224  -9.817  0.68 29.47 ?  106 ILE   A HD13 1 
ATOM   2216 H  HD13 B ILE   A 1 106 ? 18.586 -7.524  -10.122 0.32 23.76 ?  106 ILE   A HD13 1 
ATOM   2217 N  N    A GLN   A 1 107 ? 22.556 -11.128 -11.426 0.68 20.85 ?  107 GLN   A N    1 
ATOM   2218 N  N    B GLN   A 1 107 ? 22.757 -11.397 -11.139 0.32 18.22 ?  107 GLN   A N    1 
ATOM   2219 C  CA   A GLN   A 1 107 ? 23.170 -12.344 -10.904 0.68 22.95 ?  107 GLN   A CA   1 
ATOM   2220 C  CA   B GLN   A 1 107 ? 23.390 -12.569 -10.544 0.32 19.43 ?  107 GLN   A CA   1 
ATOM   2221 C  C    A GLN   A 1 107 ? 24.159 -12.039 -9.788  0.68 20.48 ?  107 GLN   A C    1 
ATOM   2222 C  C    B GLN   A 1 107 ? 24.350 -12.179 -9.428  0.32 17.05 ?  107 GLN   A C    1 
ATOM   2223 O  O    A GLN   A 1 107 ? 24.400 -12.896 -8.932  0.68 22.19 ?  107 GLN   A O    1 
ATOM   2224 O  O    B GLN   A 1 107 ? 24.595 -12.981 -8.520  0.32 16.31 ?  107 GLN   A O    1 
ATOM   2225 C  CB   A GLN   A 1 107 ? 23.877 -13.108 -12.031 0.68 27.42 ?  107 GLN   A CB   1 
ATOM   2226 C  CB   B GLN   A 1 107 ? 24.119 -13.375 -11.625 0.32 22.86 ?  107 GLN   A CB   1 
ATOM   2227 C  CG   A GLN   A 1 107 ? 22.997 -13.385 -13.241 0.68 32.70 ?  107 GLN   A CG   1 
ATOM   2228 C  CG   B GLN   A 1 107 ? 23.208 -13.867 -12.743 0.32 26.34 ?  107 GLN   A CG   1 
ATOM   2229 C  CD   A GLN   A 1 107 ? 21.728 -14.132 -12.882 0.68 37.05 ?  107 GLN   A CD   1 
ATOM   2230 C  CD   B GLN   A 1 107 ? 22.256 -14.955 -12.285 0.32 29.35 ?  107 GLN   A CD   1 
ATOM   2231 O  OE1  A GLN   A 1 107 ? 21.767 -15.150 -12.189 0.68 38.71 ?  107 GLN   A OE1  1 
ATOM   2232 O  OE1  B GLN   A 1 107 ? 22.589 -15.761 -11.415 0.32 30.10 ?  107 GLN   A OE1  1 
ATOM   2233 N  NE2  A GLN   A 1 107 ? 20.592 -13.624 -13.346 0.68 38.30 ?  107 GLN   A NE2  1 
ATOM   2234 N  NE2  B GLN   A 1 107 ? 21.061 -14.982 -12.867 0.32 30.20 ?  107 GLN   A NE2  1 
ATOM   2235 H  H    A GLN   A 1 107 ? 22.698 -10.992 -12.262 0.68 25.02 ?  107 GLN   A H    1 
ATOM   2236 H  H    B GLN   A 1 107 ? 22.930 -11.284 -11.975 0.32 21.85 ?  107 GLN   A H    1 
ATOM   2237 H  HA   A GLN   A 1 107 ? 22.481 -12.924 -10.550 0.68 27.53 ?  107 GLN   A HA   1 
ATOM   2238 H  HA   B GLN   A 1 107 ? 22.705 -13.143 -10.174 0.32 23.31 ?  107 GLN   A HA   1 
ATOM   2239 H  HB2  A GLN   A 1 107 ? 24.640 -12.591 -12.336 0.68 32.90 ?  107 GLN   A HB2  1 
ATOM   2240 H  HB2  B GLN   A 1 107 ? 24.804 -12.819 -12.027 0.32 27.43 ?  107 GLN   A HB2  1 
ATOM   2241 H  HB3  A GLN   A 1 107 ? 24.182 -13.967 -11.693 0.68 32.90 ?  107 GLN   A HB3  1 
ATOM   2242 H  HB3  B GLN   A 1 107 ? 24.528 -14.156 -11.217 0.32 27.43 ?  107 GLN   A HB3  1 
ATOM   2243 H  HG2  A GLN   A 1 107 ? 22.742 -12.543 -13.648 0.68 39.24 ?  107 GLN   A HG2  1 
ATOM   2244 H  HG2  B GLN   A 1 107 ? 22.679 -13.123 -13.072 0.32 31.60 ?  107 GLN   A HG2  1 
ATOM   2245 H  HG3  A GLN   A 1 107 ? 23.495 -13.921 -13.879 0.68 39.24 ?  107 GLN   A HG3  1 
ATOM   2246 H  HG3  B GLN   A 1 107 ? 23.754 -14.226 -13.461 0.32 31.60 ?  107 GLN   A HG3  1 
ATOM   2247 H  HE21 A GLN   A 1 107 ? 20.603 -12.910 -13.825 0.68 45.95 ?  107 GLN   A HE21 1 
ATOM   2248 H  HE21 B GLN   A 1 107 ? 20.861 -14.402 -13.470 0.32 36.23 ?  107 GLN   A HE21 1 
ATOM   2249 H  HE22 A GLN   A 1 107 ? 19.846 -14.012 -13.169 0.68 45.95 ?  107 GLN   A HE22 1 
ATOM   2250 H  HE22 B GLN   A 1 107 ? 20.486 -15.582 -12.642 0.32 36.23 ?  107 GLN   A HE22 1 
ATOM   2251 N  N    A LEU   A 1 108 ? 24.724 -10.831 -9.769  0.68 16.89 ?  108 LEU   A N    1 
ATOM   2252 N  N    B LEU   A 1 108 ? 24.880 -10.955 -9.465  0.32 15.37 ?  108 LEU   A N    1 
ATOM   2253 C  CA   A LEU   A 1 108 ? 25.638 -10.433 -8.708  0.68 15.09 ?  108 LEU   A CA   1 
ATOM   2254 C  CA   B LEU   A 1 108 ? 25.793 -10.482 -8.433  0.32 14.72 ?  108 LEU   A CA   1 
ATOM   2255 C  C    A LEU   A 1 108 ? 24.938 -10.277 -7.367  0.68 13.32 ?  108 LEU   A C    1 
ATOM   2256 C  C    B LEU   A 1 108 ? 25.099 -10.229 -7.098  0.32 13.50 ?  108 LEU   A C    1 
ATOM   2257 O  O    A LEU   A 1 108 ? 25.616 -10.114 -6.349  0.68 13.75 ?  108 LEU   A O    1 
ATOM   2258 O  O    B LEU   A 1 108 ? 25.787 -10.060 -6.086  0.32 13.89 ?  108 LEU   A O    1 
ATOM   2259 C  CB   A LEU   A 1 108 ? 26.358 -9.139  -9.093  0.68 15.25 ?  108 LEU   A CB   1 
ATOM   2260 C  CB   B LEU   A 1 108 ? 26.519 -9.224  -8.920  0.32 15.19 ?  108 LEU   A CB   1 
ATOM   2261 C  CG   A LEU   A 1 108 ? 27.388 -9.319  -10.210 0.68 16.98 ?  108 LEU   A CG   1 
ATOM   2262 C  CG   B LEU   A 1 108 ? 27.417 -9.416  -10.148 0.32 16.24 ?  108 LEU   A CG   1 
ATOM   2263 C  CD1  A LEU   A 1 108 ? 27.832 -7.979  -10.776 0.68 17.99 ?  108 LEU   A CD1  1 
ATOM   2264 C  CD1  B LEU   A 1 108 ? 27.984 -8.086  -10.624 0.32 16.73 ?  108 LEU   A CD1  1 
ATOM   2265 C  CD2  A LEU   A 1 108 ? 28.596 -10.101 -9.709  0.68 18.48 ?  108 LEU   A CD2  1 
ATOM   2266 C  CD2  B LEU   A 1 108 ? 28.545 -10.397 -9.857  0.32 17.11 ?  108 LEU   A CD2  1 
ATOM   2267 H  H    A LEU   A 1 108 ? 24.589 -10.233 -10.365 0.68 20.26 ?  108 LEU   A H    1 
ATOM   2268 H  H    B LEU   A 1 108 ? 24.722 -10.387 -10.088 0.32 18.44 ?  108 LEU   A H    1 
ATOM   2269 H  HA   A LEU   A 1 108 ? 26.306 -11.126 -8.603  0.68 18.11 ?  108 LEU   A HA   1 
ATOM   2270 H  HA   B LEU   A 1 108 ? 26.464 -11.165 -8.283  0.32 17.65 ?  108 LEU   A HA   1 
ATOM   2271 H  HB2  A LEU   A 1 108 ? 25.700 -8.495  -9.399  0.68 18.29 ?  108 LEU   A HB2  1 
ATOM   2272 H  HB2  B LEU   A 1 108 ? 25.857 -8.555  -9.150  0.32 18.22 ?  108 LEU   A HB2  1 
ATOM   2273 H  HB3  A LEU   A 1 108 ? 26.820 -8.796  -8.315  0.68 18.29 ?  108 LEU   A HB3  1 
ATOM   2274 H  HB3  B LEU   A 1 108 ? 27.080 -8.895  -8.203  0.32 18.22 ?  108 LEU   A HB3  1 
ATOM   2275 H  HG   A LEU   A 1 108 ? 26.986 -9.828  -10.932 0.68 20.37 ?  108 LEU   A HG   1 
ATOM   2276 H  HG   B LEU   A 1 108 ? 26.887 -9.786  -10.872 0.32 19.48 ?  108 LEU   A HG   1 
ATOM   2277 H  HD11 A LEU   A 1 108 ? 28.444 -8.135  -11.515 0.68 21.59 ?  108 LEU   A HD11 1 
ATOM   2278 H  HD11 B LEU   A 1 108 ? 28.543 -8.239  -11.404 0.32 20.07 ?  108 LEU   A HD11 1 
ATOM   2279 H  HD12 A LEU   A 1 108 ? 27.054 -7.494  -11.088 0.68 21.59 ?  108 LEU   A HD12 1 
ATOM   2280 H  HD12 B LEU   A 1 108 ? 27.251 -7.494  -10.857 0.32 20.07 ?  108 LEU   A HD12 1 
ATOM   2281 H  HD13 A LEU   A 1 108 ? 28.281 -7.475  -10.079 0.68 21.59 ?  108 LEU   A HD13 1 
ATOM   2282 H  HD13 B LEU   A 1 108 ? 28.513 -7.694  -9.912  0.32 20.07 ?  108 LEU   A HD13 1 
ATOM   2283 H  HD21 A LEU   A 1 108 ? 29.293 -10.071 -10.382 0.68 22.17 ?  108 LEU   A HD21 1 
ATOM   2284 H  HD21 B LEU   A 1 108 ? 29.176 -10.382 -10.594 0.32 20.52 ?  108 LEU   A HD21 1 
ATOM   2285 H  HD22 A LEU   A 1 108 ? 28.912 -9.699  -8.885  0.68 22.17 ?  108 LEU   A HD22 1 
ATOM   2286 H  HD22 B LEU   A 1 108 ? 28.988 -10.129 -9.036  0.32 20.52 ?  108 LEU   A HD22 1 
ATOM   2287 H  HD23 A LEU   A 1 108 ? 28.332 -11.021 -9.548  0.68 22.17 ?  108 LEU   A HD23 1 
ATOM   2288 H  HD23 B LEU   A 1 108 ? 28.172 -11.286 -9.758  0.32 20.52 ?  108 LEU   A HD23 1 
ATOM   2289 N  N    A LEU   A 1 109 ? 23.604 -10.345 -7.335  0.68 12.80 ?  109 LEU   A N    1 
ATOM   2290 N  N    B LEU   A 1 109 ? 23.763 -10.213 -7.065  0.32 12.78 ?  109 LEU   A N    1 
ATOM   2291 C  CA   A LEU   A 1 109 ? 22.898 -10.228 -6.065  0.68 12.41 ?  109 LEU   A CA   1 
ATOM   2292 C  CA   B LEU   A 1 109 ? 23.060 -10.075 -5.793  0.32 11.74 ?  109 LEU   A CA   1 
ATOM   2293 C  C    A LEU   A 1 109 ? 23.272 -11.364 -5.116  0.68 12.01 ?  109 LEU   A C    1 
ATOM   2294 C  C    B LEU   A 1 109 ? 23.327 -11.272 -4.888  0.32 11.62 ?  109 LEU   A C    1 
ATOM   2295 O  O    A LEU   A 1 109 ? 23.417 -11.149 -3.907  0.68 12.67 ?  109 LEU   A O    1 
ATOM   2296 O  O    B LEU   A 1 109 ? 23.440 -11.124 -3.665  0.32 11.58 ?  109 LEU   A O    1 
ATOM   2297 C  CB   A LEU   A 1 109 ? 21.391 -10.190 -6.317  0.68 13.42 ?  109 LEU   A CB   1 
ATOM   2298 C  CB   B LEU   A 1 109 ? 21.559 -9.904  -6.037  0.32 11.61 ?  109 LEU   A CB   1 
ATOM   2299 C  CG   A LEU   A 1 109 ? 20.491 -9.890  -5.120  0.68 13.95 ?  109 LEU   A CG   1 
ATOM   2300 C  CG   B LEU   A 1 109 ? 20.665 -9.689  -4.810  0.32 11.48 ?  109 LEU   A CG   1 
ATOM   2301 C  CD1  A LEU   A 1 109 ? 20.902 -8.582  -4.451  0.68 13.87 ?  109 LEU   A CD1  1 
ATOM   2302 C  CD1  B LEU   A 1 109 ? 21.180 -8.537  -3.968  0.32 10.61 ?  109 LEU   A CD1  1 
ATOM   2303 C  CD2  A LEU   A 1 109 ? 19.031 -9.840  -5.559  0.68 14.56 ?  109 LEU   A CD2  1 
ATOM   2304 C  CD2  B LEU   A 1 109 ? 19.210 -9.450  -5.221  0.32 11.36 ?  109 LEU   A CD2  1 
ATOM   2305 H  H    A LEU   A 1 109 ? 23.095 -10.462 -8.019  0.68 15.36 ?  109 LEU   A H    1 
ATOM   2306 H  H    B LEU   A 1 109 ? 23.255 -10.278 -7.752  0.32 15.33 ?  109 LEU   A H    1 
ATOM   2307 H  HA   A LEU   A 1 109 ? 23.153 -9.393  -5.647  0.68 14.89 ?  109 LEU   A HA   1 
ATOM   2308 H  HA   B LEU   A 1 109 ? 23.385 -9.283  -5.342  0.32 14.09 ?  109 LEU   A HA   1 
ATOM   2309 H  HB2  A LEU   A 1 109 ? 21.214 -9.505  -6.983  0.68 16.10 ?  109 LEU   A HB2  1 
ATOM   2310 H  HB2  B LEU   A 1 109 ? 21.436 -9.134  -6.615  0.32 13.93 ?  109 LEU   A HB2  1 
ATOM   2311 H  HB3  A LEU   A 1 109 ? 21.119 -11.051 -6.665  0.68 16.10 ?  109 LEU   A HB3  1 
ATOM   2312 H  HB3  B LEU   A 1 109 ? 21.233 -10.696 -6.488  0.32 13.93 ?  109 LEU   A HB3  1 
ATOM   2313 H  HG   A LEU   A 1 109 ? 20.581 -10.597 -4.466  0.68 16.74 ?  109 LEU   A HG   1 
ATOM   2314 H  HG   B LEU   A 1 109 ? 20.686 -10.486 -4.262  0.32 13.77 ?  109 LEU   A HG   1 
ATOM   2315 H  HD11 A LEU   A 1 109 ? 20.225 -8.326  -3.803  0.68 16.64 ?  109 LEU   A HD11 1 
ATOM   2316 H  HD11 B LEU   A 1 109 ? 20.515 -8.309  -3.300  0.32 12.73 ?  109 LEU   A HD11 1 
ATOM   2317 H  HD12 A LEU   A 1 109 ? 21.754 -8.705  -4.005  0.68 16.64 ?  109 LEU   A HD12 1 
ATOM   2318 H  HD12 B LEU   A 1 109 ? 22.006 -8.805  -3.535  0.32 12.73 ?  109 LEU   A HD12 1 
ATOM   2319 H  HD13 A LEU   A 1 109 ? 20.982 -7.888  -5.129  0.68 16.64 ?  109 LEU   A HD13 1 
ATOM   2320 H  HD13 B LEU   A 1 109 ? 21.343 -7.771  -4.544  0.32 12.73 ?  109 LEU   A HD13 1 
ATOM   2321 H  HD21 A LEU   A 1 109 ? 18.489 -9.494  -4.831  0.68 17.47 ?  109 LEU   A HD21 1 
ATOM   2322 H  HD21 B LEU   A 1 109 ? 18.678 -9.281  -4.426  0.32 13.63 ?  109 LEU   A HD21 1 
ATOM   2323 H  HD22 A LEU   A 1 109 ? 18.949 -9.263  -6.334  0.68 17.47 ?  109 LEU   A HD22 1 
ATOM   2324 H  HD22 B LEU   A 1 109 ? 19.168 -8.684  -5.814  0.32 13.63 ?  109 LEU   A HD22 1 
ATOM   2325 H  HD23 A LEU   A 1 109 ? 18.739 -10.740 -5.787  0.68 17.47 ?  109 LEU   A HD23 1 
ATOM   2326 H  HD23 B LEU   A 1 109 ? 18.876 -10.239 -5.677  0.32 13.63 ?  109 LEU   A HD23 1 
ATOM   2327 N  N    A LYS   A 1 110 ? 23.438 -12.583 -5.637  0.68 11.98 ?  110 LYS   A N    1 
ATOM   2328 N  N    B LYS   A 1 110 ? 23.424 -12.471 -5.468  0.32 12.06 ?  110 LYS   A N    1 
ATOM   2329 C  CA   A LYS   A 1 110 ? 23.815 -13.691 -4.758  0.68 12.09 ?  110 LYS   A CA   1 
ATOM   2330 C  CA   B LYS   A 1 110 ? 23.800 -13.633 -4.669  0.32 12.42 ?  110 LYS   A CA   1 
ATOM   2331 C  C    A LYS   A 1 110 ? 25.187 -13.449 -4.131  0.68 11.56 ?  110 LYS   A C    1 
ATOM   2332 C  C    B LYS   A 1 110 ? 25.210 -13.470 -4.109  0.32 11.95 ?  110 LYS   A C    1 
ATOM   2333 O  O    A LYS   A 1 110 ? 25.367 -13.628 -2.923  0.68 11.61 ?  110 LYS   A O    1 
ATOM   2334 O  O    B LYS   A 1 110 ? 25.448 -13.739 -2.927  0.32 12.11 ?  110 LYS   A O    1 
ATOM   2335 C  CB   A LYS   A 1 110 ? 23.758 -15.031 -5.499  0.68 13.02 ?  110 LYS   A CB   1 
ATOM   2336 C  CB   B LYS   A 1 110 ? 23.661 -14.921 -5.485  0.32 12.93 ?  110 LYS   A CB   1 
ATOM   2337 C  CG   A LYS   A 1 110 ? 23.961 -16.230 -4.565  0.68 13.30 ?  110 LYS   A CG   1 
ATOM   2338 C  CG   B LYS   A 1 110 ? 23.829 -16.185 -4.645  0.32 13.10 ?  110 LYS   A CG   1 
ATOM   2339 C  CD   A LYS   A 1 110 ? 23.741 -17.563 -5.254  0.68 13.56 ?  110 LYS   A CD   1 
ATOM   2340 C  CD   B LYS   A 1 110 ? 23.621 -17.450 -5.458  0.32 13.32 ?  110 LYS   A CD   1 
ATOM   2341 C  CE   A LYS   A 1 110 ? 23.864 -18.730 -4.281  0.68 14.22 ?  110 LYS   A CE   1 
ATOM   2342 C  CE   B LYS   A 1 110 ? 23.688 -18.692 -4.582  0.32 13.38 ?  110 LYS   A CE   1 
ATOM   2343 N  NZ   A LYS   A 1 110 ? 22.678 -18.872 -3.391  0.68 14.88 ?  110 LYS   A NZ   1 
ATOM   2344 N  NZ   B LYS   A 1 110 ? 22.546 -18.772 -3.630  0.32 13.97 ?  110 LYS   A NZ   1 
ATOM   2345 H  H    A LYS   A 1 110 ? 23.345 -12.788 -6.467  0.68 14.38 ?  110 LYS   A H    1 
ATOM   2346 H  H    B LYS   A 1 110 ? 23.277 -12.634 -6.298  0.32 14.47 ?  110 LYS   A H    1 
ATOM   2347 H  HA   A LYS   A 1 110 ? 23.165 -13.735 -4.036  0.68 14.50 ?  110 LYS   A HA   1 
ATOM   2348 H  HA   B LYS   A 1 110 ? 23.191 -13.700 -3.915  0.32 14.90 ?  110 LYS   A HA   1 
ATOM   2349 H  HB2  A LYS   A 1 110 ? 22.888 -15.123 -5.921  0.68 15.61 ?  110 LYS   A HB2  1 
ATOM   2350 H  HB2  B LYS   A 1 110 ? 22.776 -14.949 -5.886  0.32 15.51 ?  110 LYS   A HB2  1 
ATOM   2351 H  HB3  A LYS   A 1 110 ? 24.457 -15.050 -6.168  0.68 15.61 ?  110 LYS   A HB3  1 
ATOM   2352 H  HB3  B LYS   A 1 110 ? 24.338 -14.933 -6.177  0.32 15.51 ?  110 LYS   A HB3  1 
ATOM   2353 H  HG2  A LYS   A 1 110 ? 24.867 -16.212 -4.222  0.68 15.96 ?  110 LYS   A HG2  1 
ATOM   2354 H  HG2  B LYS   A 1 110 ? 24.726 -16.207 -4.277  0.32 15.71 ?  110 LYS   A HG2  1 
ATOM   2355 H  HG3  A LYS   A 1 110 ? 23.329 -16.165 -3.829  0.68 15.96 ?  110 LYS   A HG3  1 
ATOM   2356 H  HG3  B LYS   A 1 110 ? 23.176 -16.178 -3.927  0.32 15.71 ?  110 LYS   A HG3  1 
ATOM   2357 H  HD2  A LYS   A 1 110 ? 22.852 -17.583 -5.638  0.68 16.27 ?  110 LYS   A HD2  1 
ATOM   2358 H  HD2  B LYS   A 1 110 ? 22.747 -17.422 -5.877  0.32 15.98 ?  110 LYS   A HD2  1 
ATOM   2359 H  HD3  A LYS   A 1 110 ? 24.409 -17.675 -5.949  0.68 16.27 ?  110 LYS   A HD3  1 
ATOM   2360 H  HD3  B LYS   A 1 110 ? 24.316 -17.516 -6.131  0.32 15.98 ?  110 LYS   A HD3  1 
ATOM   2361 H  HE2  A LYS   A 1 110 ? 23.964 -19.553 -4.784  0.68 17.06 ?  110 LYS   A HE2  1 
ATOM   2362 H  HE2  B LYS   A 1 110 ? 23.668 -19.481 -5.145  0.32 16.05 ?  110 LYS   A HE2  1 
ATOM   2363 H  HE3  A LYS   A 1 110 ? 24.646 -18.591 -3.719  0.68 17.06 ?  110 LYS   A HE3  1 
ATOM   2364 H  HE3  B LYS   A 1 110 ? 24.510 -18.673 -4.065  0.32 16.05 ?  110 LYS   A HE3  1 
ATOM   2365 H  HZ1  A LYS   A 1 110 ? 22.790 -19.560 -2.841  0.68 17.85 ?  110 LYS   A HZ1  1 
ATOM   2366 H  HZ1  B LYS   A 1 110 ? 22.603 -19.517 -3.148  0.32 16.76 ?  110 LYS   A HZ1  1 
ATOM   2367 H  HZ2  A LYS   A 1 110 ? 22.569 -18.129 -2.910  0.68 17.85 ?  110 LYS   A HZ2  1 
ATOM   2368 H  HZ2  B LYS   A 1 110 ? 22.558 -18.071 -3.081  0.32 16.76 ?  110 LYS   A HZ2  1 
ATOM   2369 H  HZ3  A LYS   A 1 110 ? 21.947 -19.007 -3.882  0.68 17.85 ?  110 LYS   A HZ3  1 
ATOM   2370 H  HZ3  B LYS   A 1 110 ? 21.777 -18.774 -4.078  0.32 16.76 ?  110 LYS   A HZ3  1 
ATOM   2371 N  N    . SER   A 1 111 ? 26.153 -13.004 -4.934  1.00 11.71 ?  111 SER   A N    1 
ATOM   2372 C  CA   . SER   A 1 111 ? 27.486 -12.708 -4.416  1.00 11.94 ?  111 SER   A CA   1 
ATOM   2373 C  C    . SER   A 1 111 ? 27.426 -11.660 -3.309  1.00 11.57 ?  111 SER   A C    1 
ATOM   2374 O  O    . SER   A 1 111 ? 28.125 -11.769 -2.296  1.00 12.43 ?  111 SER   A O    1 
ATOM   2375 C  CB   . SER   A 1 111 ? 28.378 -12.220 -5.554  1.00 13.39 ?  111 SER   A CB   1 
ATOM   2376 O  OG   . SER   A 1 111 ? 28.434 -13.193 -6.582  1.00 15.53 ?  111 SER   A OG   1 
ATOM   2377 H  H    A SER   A 1 111 ? 26.058 -12.868 -5.775  0.68 14.05 ?  111 SER   A H    1 
ATOM   2378 H  H    B SER   A 1 111 ? 26.042 -12.851 -5.770  0.32 14.05 ?  111 SER   A H    1 
ATOM   2379 H  HA   . SER   A 1 111 ? 27.874 -13.520 -4.049  1.00 14.32 ?  111 SER   A HA   1 
ATOM   2380 H  HB2  . SER   A 1 111 ? 28.004 -11.403 -5.920  1.00 16.06 ?  111 SER   A HB2  1 
ATOM   2381 H  HB3  . SER   A 1 111 ? 29.269 -12.052 -5.208  1.00 16.06 ?  111 SER   A HB3  1 
ATOM   2382 H  HG   . SER   A 1 111 ? 28.948 -12.917 -7.202  1.00 18.63 ?  111 SER   A HG   1 
ATOM   2383 N  N    . ALA   A 1 112 ? 26.587 -10.636 -3.486  1.00 11.65 ?  112 ALA   A N    1 
ATOM   2384 C  CA   . ALA   A 1 112 ? 26.439 -9.599  -2.465  1.00 11.19 ?  112 ALA   A CA   1 
ATOM   2385 C  C    . ALA   A 1 112 ? 25.960 -10.199 -1.143  1.00 11.29 ?  112 ALA   A C    1 
ATOM   2386 O  O    . ALA   A 1 112 ? 26.512 -9.911  -0.074  1.00 11.61 ?  112 ALA   A O    1 
ATOM   2387 C  CB   . ALA   A 1 112 ? 25.471 -8.518  -2.957  1.00 11.73 ?  112 ALA   A CB   1 
ATOM   2388 H  H    . ALA   A 1 112 ? 26.094 -10.516 -4.180  1.00 13.98 ?  112 ALA   A H    1 
ATOM   2389 H  HA   . ALA   A 1 112 ? 27.298 -9.176  -2.308  1.00 13.42 ?  112 ALA   A HA   1 
ATOM   2390 H  HB1  . ALA   A 1 112 ? 25.398 -7.820  -2.277  1.00 14.07 ?  112 ALA   A HB1  1 
ATOM   2391 H  HB2  . ALA   A 1 112 ? 25.809 -8.135  -3.779  1.00 14.07 ?  112 ALA   A HB2  1 
ATOM   2392 H  HB3  . ALA   A 1 112 ? 24.598 -8.913  -3.108  1.00 14.07 ?  112 ALA   A HB3  1 
ATOM   2393 N  N    . TYR   A 1 113 ? 24.925 -11.044 -1.193  1.00 11.58 ?  113 TYR   A N    1 
ATOM   2394 C  CA   . TYR   A 1 113 ? 24.412 -11.655 0.031   1.00 11.10 ?  113 TYR   A CA   1 
ATOM   2395 C  C    . TYR   A 1 113 ? 25.418 -12.608 0.677   1.00 10.50 ?  113 TYR   A C    1 
ATOM   2396 O  O    . TYR   A 1 113 ? 25.384 -12.793 1.899   1.00 11.33 ?  113 TYR   A O    1 
ATOM   2397 C  CB   . TYR   A 1 113 ? 23.096 -12.388 -0.253  1.00 11.78 ?  113 TYR   A CB   1 
ATOM   2398 C  CG   . TYR   A 1 113 ? 21.875 -11.501 -0.162  1.00 11.49 ?  113 TYR   A CG   1 
ATOM   2399 C  CD1  . TYR   A 1 113 ? 21.520 -10.898 1.039   1.00 11.58 ?  113 TYR   A CD1  1 
ATOM   2400 C  CD2  . TYR   A 1 113 ? 21.058 -11.287 -1.265  1.00 11.76 ?  113 TYR   A CD2  1 
ATOM   2401 C  CE1  . TYR   A 1 113 ? 20.387 -10.109 1.142   1.00 12.18 ?  113 TYR   A CE1  1 
ATOM   2402 C  CE2  . TYR   A 1 113 ? 19.910 -10.492 -1.172  1.00 12.07 ?  113 TYR   A CE2  1 
ATOM   2403 C  CZ   . TYR   A 1 113 ? 19.584 -9.917  0.037   1.00 12.02 ?  113 TYR   A CZ   1 
ATOM   2404 O  OH   . TYR   A 1 113 ? 18.458 -9.124  0.164   1.00 12.72 ?  113 TYR   A OH   1 
ATOM   2405 H  H    . TYR   A 1 113 ? 24.516 -11.274 -1.911  1.00 13.90 ?  113 TYR   A H    1 
ATOM   2406 H  HA   . TYR   A 1 113 ? 24.229 -10.956 0.672   1.00 13.31 ?  113 TYR   A HA   1 
ATOM   2407 H  HB2  . TYR   A 1 113 ? 23.130 -12.751 -1.151  1.00 14.13 ?  113 TYR   A HB2  1 
ATOM   2408 H  HB3  . TYR   A 1 113 ? 22.994 -13.105 0.390   1.00 14.13 ?  113 TYR   A HB3  1 
ATOM   2409 H  HD1  . TYR   A 1 113 ? 22.054 -11.036 1.792   1.00 13.89 ?  113 TYR   A HD1  1 
ATOM   2410 H  HD2  . TYR   A 1 113 ? 21.266 -11.691 -2.075  1.00 14.11 ?  113 TYR   A HD2  1 
ATOM   2411 H  HE1  . TYR   A 1 113 ? 20.168 -9.714  1.955   1.00 14.61 ?  113 TYR   A HE1  1 
ATOM   2412 H  HE2  . TYR   A 1 113 ? 19.362 -10.358 -1.914  1.00 14.48 ?  113 TYR   A HE2  1 
ATOM   2413 H  HH   . TYR   A 1 113 ? 18.058 -9.090  -0.576  1.00 15.26 ?  113 TYR   A HH   1 
ATOM   2414 N  N    . GLU   A 1 114 ? 26.314 -13.221 -0.109  1.00 11.03 ?  114 GLU   A N    1 
ATOM   2415 C  CA   . GLU   A 1 114 ? 27.312 -14.115 0.486   1.00 11.31 ?  114 GLU   A CA   1 
ATOM   2416 C  C    . GLU   A 1 114 ? 28.161 -13.403 1.537   1.00 11.13 ?  114 GLU   A C    1 
ATOM   2417 O  O    . GLU   A 1 114 ? 28.646 -14.037 2.485   1.00 11.58 ?  114 GLU   A O    1 
ATOM   2418 C  CB   . GLU   A 1 114 ? 28.182 -14.757 -0.601  1.00 11.63 ?  114 GLU   A CB   1 
ATOM   2419 C  CG   . GLU   A 1 114 ? 27.418 -15.799 -1.385  1.00 11.99 ?  114 GLU   A CG   1 
ATOM   2420 C  CD   . GLU   A 1 114 ? 28.134 -16.332 -2.618  1.00 12.57 ?  114 GLU   A CD   1 
ATOM   2421 O  OE1  . GLU   A 1 114 ? 29.088 -15.700 -3.114  1.00 13.05 ?  114 GLU   A OE1  1 
ATOM   2422 O  OE2  . GLU   A 1 114 ? 27.696 -17.380 -3.126  1.00 13.84 -1 114 GLU   A OE2  1 
ATOM   2423 H  H    . GLU   A 1 114 ? 26.368 -13.131 -0.968  1.00 13.23 ?  114 GLU   A H    1 
ATOM   2424 H  HA   . GLU   A 1 114 ? 26.841 -14.831 0.934   1.00 13.57 ?  114 GLU   A HA   1 
ATOM   2425 H  HB2  . GLU   A 1 114 ? 28.480 -14.072 -1.224  1.00 13.96 ?  114 GLU   A HB2  1 
ATOM   2426 H  HB3  . GLU   A 1 114 ? 28.944 -15.190 -0.191  1.00 13.96 ?  114 GLU   A HB3  1 
ATOM   2427 H  HG2  . GLU   A 1 114 ? 27.250 -16.556 -0.808  1.00 14.38 ?  114 GLU   A HG2  1 
ATOM   2428 H  HG3  . GLU   A 1 114 ? 26.576 -15.416 -1.676  1.00 14.38 ?  114 GLU   A HG3  1 
ATOM   2429 N  N    . ASN   A 1 115 ? 28.344 -12.088 1.401   1.00 11.07 ?  115 ASN   A N    1 
ATOM   2430 C  CA   . ASN   A 1 115 ? 29.108 -11.351 2.404   1.00 11.49 ?  115 ASN   A CA   1 
ATOM   2431 C  C    . ASN   A 1 115 ? 28.485 -11.478 3.791   1.00 11.21 ?  115 ASN   A C    1 
ATOM   2432 O  O    . ASN   A 1 115 ? 29.192 -11.397 4.802   1.00 11.86 ?  115 ASN   A O    1 
ATOM   2433 C  CB   . ASN   A 1 115 ? 29.218 -9.874  2.019   1.00 11.84 ?  115 ASN   A CB   1 
ATOM   2434 C  CG   . ASN   A 1 115 ? 30.013 -9.663  0.754   1.00 12.65 ?  115 ASN   A CG   1 
ATOM   2435 O  OD1  . ASN   A 1 115 ? 31.230 -9.802  0.755   1.00 16.02 ?  115 ASN   A OD1  1 
ATOM   2436 N  ND2  . ASN   A 1 115 ? 29.332 -9.342  -0.331  1.00 12.15 ?  115 ASN   A ND2  1 
ATOM   2437 H  H    . ASN   A 1 115 ? 28.043 -11.603 0.751   1.00 13.27 ?  115 ASN   A H    1 
ATOM   2438 H  HA   . ASN   A 1 115 ? 30.003 -11.714 2.448   1.00 13.78 ?  115 ASN   A HA   1 
ATOM   2439 H  HB2  . ASN   A 1 115 ? 28.322 -9.518  1.890   1.00 14.21 ?  115 ASN   A HB2  1 
ATOM   2440 H  HB3  . ASN   A 1 115 ? 29.659 -9.396  2.740   1.00 14.21 ?  115 ASN   A HB3  1 
ATOM   2441 H  HD21 . ASN   A 1 115 ? 29.741 -9.211  -1.075  1.00 14.57 ?  115 ASN   A HD21 1 
ATOM   2442 H  HD22 . ASN   A 1 115 ? 28.472 -9.263  -0.296  1.00 14.57 ?  115 ASN   A HD22 1 
ATOM   2443 N  N    . PHE   A 1 116 ? 27.156 -11.650 3.868   1.00 11.05 ?  116 PHE   A N    1 
ATOM   2444 C  CA   . PHE   A 1 116 ? 26.508 -11.746 5.173   1.00 11.30 ?  116 PHE   A CA   1 
ATOM   2445 C  C    . PHE   A 1 116 ? 26.990 -12.976 5.945   1.00 11.60 ?  116 PHE   A C    1 
ATOM   2446 O  O    . PHE   A 1 116 ? 26.916 -12.997 7.175   1.00 12.01 ?  116 PHE   A O    1 
ATOM   2447 C  CB   . PHE   A 1 116 ? 24.982 -11.879 5.040   1.00 11.50 ?  116 PHE   A CB   1 
ATOM   2448 C  CG   . PHE   A 1 116 ? 24.228 -10.631 4.572   1.00 11.19 ?  116 PHE   A CG   1 
ATOM   2449 C  CD1  . PHE   A 1 116 ? 24.803 -9.607  3.825   1.00 11.39 ?  116 PHE   A CD1  1 
ATOM   2450 C  CD2  . PHE   A 1 116 ? 22.876 -10.536 4.888   1.00 11.68 ?  116 PHE   A CD2  1 
ATOM   2451 C  CE1  . PHE   A 1 116 ? 24.035 -8.525  3.405   1.00 11.64 ?  116 PHE   A CE1  1 
ATOM   2452 C  CE2  . PHE   A 1 116 ? 22.110 -9.458  4.481   1.00 12.00 ?  116 PHE   A CE2  1 
ATOM   2453 C  CZ   . PHE   A 1 116 ? 22.683 -8.451  3.740   1.00 11.35 ?  116 PHE   A CZ   1 
ATOM   2454 H  H    . PHE   A 1 116 ? 26.624 -11.708 3.190   1.00 13.26 ?  116 PHE   A H    1 
ATOM   2455 H  HA   . PHE   A 1 116 ? 26.701 -10.953 5.692   1.00 13.56 ?  116 PHE   A HA   1 
ATOM   2456 H  HB2  . PHE   A 1 116 ? 24.793 -12.586 4.400   1.00 13.79 ?  116 PHE   A HB2  1 
ATOM   2457 H  HB3  . PHE   A 1 116 ? 24.624 -12.129 5.906   1.00 13.79 ?  116 PHE   A HB3  1 
ATOM   2458 H  HD1  . PHE   A 1 116 ? 25.699 -9.667  3.596   1.00 13.66 ?  116 PHE   A HD1  1 
ATOM   2459 H  HD2  . PHE   A 1 116 ? 22.474 -11.223 5.384   1.00 14.01 ?  116 PHE   A HD2  1 
ATOM   2460 H  HE1  . PHE   A 1 116 ? 24.432 -7.847  2.912   1.00 13.96 ?  116 PHE   A HE1  1 
ATOM   2461 H  HE2  . PHE   A 1 116 ? 21.206 -9.421  4.712   1.00 14.39 ?  116 PHE   A HE2  1 
ATOM   2462 H  HZ   . PHE   A 1 116 ? 22.171 -7.722  3.474   1.00 13.62 ?  116 PHE   A HZ   1 
ATOM   2463 N  N    . ASN   A 1 117 ? 27.437 -14.024 5.240   1.00 11.80 ?  117 ASN   A N    1 
ATOM   2464 C  CA   . ASN   A 1 117 ? 27.805 -15.271 5.908   1.00 12.11 ?  117 ASN   A CA   1 
ATOM   2465 C  C    . ASN   A 1 117 ? 29.065 -15.152 6.745   1.00 12.43 ?  117 ASN   A C    1 
ATOM   2466 O  O    . ASN   A 1 117 ? 29.367 -16.074 7.511   1.00 13.51 ?  117 ASN   A O    1 
ATOM   2467 C  CB   . ASN   A 1 117 ? 27.919 -16.400 4.886   1.00 12.38 ?  117 ASN   A CB   1 
ATOM   2468 C  CG   . ASN   A 1 117 ? 26.570 -16.783 4.346   1.00 12.23 ?  117 ASN   A CG   1 
ATOM   2469 O  OD1  . ASN   A 1 117 ? 25.589 -16.809 5.094   1.00 13.11 ?  117 ASN   A OD1  1 
ATOM   2470 N  ND2  . ASN   A 1 117 ? 26.491 -17.040 3.054   1.00 11.92 ?  117 ASN   A ND2  1 
ATOM   2471 H  H    . ASN   A 1 117 ? 27.515 -14.036 4.381   1.00 14.15 ?  117 ASN   A H    1 
ATOM   2472 H  HA   . ASN   A 1 117 ? 27.083 -15.504 6.510   1.00 14.52 ?  117 ASN   A HA   1 
ATOM   2473 H  HB2  . ASN   A 1 117 ? 28.477 -16.107 4.145   1.00 14.85 ?  117 ASN   A HB2  1 
ATOM   2474 H  HB3  . ASN   A 1 117 ? 28.306 -17.176 5.314   1.00 14.85 ?  117 ASN   A HB3  1 
ATOM   2475 H  HD21 . ASN   A 1 117 ? 25.738 -17.253 2.706   1.00 14.30 ?  117 ASN   A HD21 1 
ATOM   2476 H  HD22 . ASN   A 1 117 ? 27.198 -16.996 2.564   1.00 14.30 ?  117 ASN   A HD22 1 
ATOM   2477 N  N    . GLN   A 1 118 ? 29.793 -14.046 6.626   1.00 12.68 ?  118 GLN   A N    1 
ATOM   2478 C  CA   . GLN   A 1 118 ? 30.966 -13.810 7.453   1.00 13.03 ?  118 GLN   A CA   1 
ATOM   2479 C  C    . GLN   A 1 118 ? 30.620 -13.236 8.822   1.00 13.06 ?  118 GLN   A C    1 
ATOM   2480 O  O    . GLN   A 1 118 ? 31.538 -12.954 9.603   1.00 14.57 ?  118 GLN   A O    1 
ATOM   2481 C  CB   . GLN   A 1 118 ? 31.957 -12.899 6.726   1.00 13.05 ?  118 GLN   A CB   1 
ATOM   2482 C  CG   . GLN   A 1 118 ? 32.438 -13.473 5.402   1.00 13.37 ?  118 GLN   A CG   1 
ATOM   2483 C  CD   . GLN   A 1 118 ? 33.281 -14.730 5.580   1.00 13.64 ?  118 GLN   A CD   1 
ATOM   2484 O  OE1  . GLN   A 1 118 ? 34.138 -14.794 6.466   1.00 14.62 ?  118 GLN   A OE1  1 
ATOM   2485 N  NE2  . GLN   A 1 118 ? 33.033 -15.738 4.740   1.00 14.11 ?  118 GLN   A NE2  1 
ATOM   2486 H  H    . GLN   A 1 118 ? 29.617 -13.398 6.074   1.00 15.21 ?  118 GLN   A H    1 
ATOM   2487 H  HA   . GLN   A 1 118 ? 31.400 -14.666 7.596   1.00 15.63 ?  118 GLN   A HA   1 
ATOM   2488 H  HB2  . GLN   A 1 118 ? 31.530 -12.048 6.551   1.00 15.66 ?  118 GLN   A HB2  1 
ATOM   2489 H  HB3  . GLN   A 1 118 ? 32.733 -12.770 7.296   1.00 15.66 ?  118 GLN   A HB3  1 
ATOM   2490 H  HG2  . GLN   A 1 118 ? 31.670 -13.696 4.851   1.00 16.04 ?  118 GLN   A HG2  1 
ATOM   2491 H  HG3  . GLN   A 1 118 ? 32.986 -12.809 4.949   1.00 16.04 ?  118 GLN   A HG3  1 
ATOM   2492 H  HE21 . GLN   A 1 118 ? 32.422 -15.653 4.137   1.00 16.92 ?  118 GLN   A HE21 1 
ATOM   2493 H  HE22 . GLN   A 1 118 ? 33.477 -16.468 4.802   1.00 16.92 ?  118 GLN   A HE22 1 
ATOM   2494 N  N    . HIS   A 1 119 ? 29.333 -13.073 9.132   1.00 12.67 ?  119 HIS   A N    1 
ATOM   2495 C  CA   . HIS   A 1 119 ? 28.877 -12.457 10.373  1.00 13.08 ?  119 HIS   A CA   1 
ATOM   2496 C  C    . HIS   A 1 119 ? 27.737 -13.275 10.957  1.00 13.27 ?  119 HIS   A C    1 
ATOM   2497 O  O    . HIS   A 1 119 ? 26.783 -13.606 10.247  1.00 14.15 ?  119 HIS   A O    1 
ATOM   2498 C  CB   . HIS   A 1 119 ? 28.421 -11.024 10.095  1.00 13.54 ?  119 HIS   A CB   1 
ATOM   2499 C  CG   . HIS   A 1 119 ? 29.500 -10.217 9.468   1.00 14.65 ?  119 HIS   A CG   1 
ATOM   2500 N  ND1  . HIS   A 1 119 ? 30.477 -9.594  10.210  1.00 17.02 ?  119 HIS   A ND1  1 
ATOM   2501 C  CD2  . HIS   A 1 119 ? 29.832 -10.036 8.170   1.00 15.81 ?  119 HIS   A CD2  1 
ATOM   2502 C  CE1  . HIS   A 1 119 ? 31.338 -9.016  9.393   1.00 17.29 ?  119 HIS   A CE1  1 
ATOM   2503 N  NE2  . HIS   A 1 119 ? 30.979 -9.281  8.149   1.00 17.41 ?  119 HIS   A NE2  1 
ATOM   2504 H  H    . HIS   A 1 119 ? 28.681 -13.328 8.623   1.00 15.20 ?  119 HIS   A H    1 
ATOM   2505 H  HA   . HIS   A 1 119 ? 29.608 -12.439 11.013  1.00 15.69 ?  119 HIS   A HA   1 
ATOM   2506 H  HB2  . HIS   A 1 119 ? 27.663 -11.049 9.491   1.00 16.24 ?  119 HIS   A HB2  1 
ATOM   2507 H  HB3  . HIS   A 1 119 ? 28.171 -10.608 10.934  1.00 16.24 ?  119 HIS   A HB3  1 
ATOM   2508 H  HD1  . HIS   A 1 119 ? 30.509 -9.567  11.069  1.00 20.42 ?  119 HIS   A HD1  1 
ATOM   2509 H  HD2  . HIS   A 1 119 ? 29.371 -10.362 7.430   1.00 18.97 ?  119 HIS   A HD2  1 
ATOM   2510 H  HE1  . HIS   A 1 119 ? 32.072 -8.505  9.648   1.00 20.74 ?  119 HIS   A HE1  1 
ATOM   2511 N  N    . GLU   A 1 120 ? 27.826 -13.578 12.255  1.00 14.38 ?  120 GLU   A N    1 
ATOM   2512 C  CA   . GLU   A 1 120 ? 26.874 -14.505 12.866  1.00 16.33 ?  120 GLU   A CA   1 
ATOM   2513 C  C    . GLU   A 1 120 ? 25.454 -13.945 12.899  1.00 14.95 ?  120 GLU   A C    1 
ATOM   2514 O  O    . GLU   A 1 120 ? 24.480 -14.707 12.790  1.00 15.33 ?  120 GLU   A O    1 
ATOM   2515 C  CB   . GLU   A 1 120 ? 27.334 -14.874 14.278  1.00 20.62 ?  120 GLU   A CB   1 
ATOM   2516 C  CG   . GLU   A 1 120 ? 28.532 -15.804 14.308  1.00 27.82 ?  120 GLU   A CG   1 
ATOM   2517 C  CD   . GLU   A 1 120 ? 28.656 -16.552 15.618  1.00 34.21 ?  120 GLU   A CD   1 
ATOM   2518 O  OE1  . GLU   A 1 120 ? 28.234 -16.003 16.659  1.00 35.57 ?  120 GLU   A OE1  1 
ATOM   2519 O  OE2  . GLU   A 1 120 ? 29.170 -17.691 15.606  1.00 37.01 -1 120 GLU   A OE2  1 
ATOM   2520 H  H    . GLU   A 1 120 ? 28.424 -13.268 12.797  1.00 17.25 ?  120 GLU   A H    1 
ATOM   2521 H  HA   . GLU   A 1 120 ? 26.858 -15.319 12.347  1.00 19.59 ?  120 GLU   A HA   1 
ATOM   2522 H  HB2  . GLU   A 1 120 ? 27.580 -14.065 14.755  1.00 24.74 ?  120 GLU   A HB2  1 
ATOM   2523 H  HB3  . GLU   A 1 120 ? 26.605 -15.318 14.742  1.00 24.74 ?  120 GLU   A HB3  1 
ATOM   2524 H  HG2  . GLU   A 1 120 ? 28.454 -16.447 13.586  1.00 33.38 ?  120 GLU   A HG2  1 
ATOM   2525 H  HG3  . GLU   A 1 120 ? 29.343 -15.285 14.207  1.00 33.38 ?  120 GLU   A HG3  1 
ATOM   2526 N  N    . VAL   A 1 121 ? 25.316 -12.632 13.102  1.00 14.10 ?  121 VAL   A N    1 
ATOM   2527 C  CA   . VAL   A 1 121 ? 24.020 -11.966 13.221  1.00 14.53 ?  121 VAL   A CA   1 
ATOM   2528 C  C    . VAL   A 1 121 ? 24.126 -10.584 12.587  1.00 13.39 ?  121 VAL   A C    1 
ATOM   2529 O  O    . VAL   A 1 121 ? 25.091 -9.853  12.837  1.00 14.09 ?  121 VAL   A O    1 
ATOM   2530 C  CB   . VAL   A 1 121 ? 23.584 -11.819 14.697  1.00 17.89 ?  121 VAL   A CB   1 
ATOM   2531 C  CG1  . VAL   A 1 121 ? 22.197 -11.189 14.791  1.00 18.59 ?  121 VAL   A CG1  1 
ATOM   2532 C  CG2  . VAL   A 1 121 ? 23.594 -13.148 15.431  1.00 20.49 ?  121 VAL   A CG2  1 
ATOM   2533 H  H    . VAL   A 1 121 ? 25.979 -12.088 13.178  1.00 16.91 ?  121 VAL   A H    1 
ATOM   2534 H  HA   . VAL   A 1 121 ? 23.346 -12.482 12.753  1.00 17.43 ?  121 VAL   A HA   1 
ATOM   2535 H  HB   . VAL   A 1 121 ? 24.202 -11.232 15.152  1.00 21.46 ?  121 VAL   A HB   1 
ATOM   2536 H  HG11 . VAL   A 1 121 ? 21.881 -11.251 15.707  1.00 22.30 ?  121 VAL   A HG11 1 
ATOM   2537 H  HG12 . VAL   A 1 121 ? 22.255 -10.257 14.527  1.00 22.30 ?  121 VAL   A HG12 1 
ATOM   2538 H  HG13 . VAL   A 1 121 ? 21.591 -11.664 14.201  1.00 22.30 ?  121 VAL   A HG13 1 
ATOM   2539 H  HG21 . VAL   A 1 121 ? 23.246 -13.016 16.332  1.00 24.59 ?  121 VAL   A HG21 1 
ATOM   2540 H  HG22 . VAL   A 1 121 ? 23.030 -13.779 14.956  1.00 24.59 ?  121 VAL   A HG22 1 
ATOM   2541 H  HG23 . VAL   A 1 121 ? 24.501 -13.480 15.476  1.00 24.59 ?  121 VAL   A HG23 1 
ATOM   2542 N  N    . LEU   A 1 122 ? 23.114 -10.201 11.802  1.00 12.79 ?  122 LEU   A N    1 
ATOM   2543 C  CA   . LEU   A 1 122 ? 23.116 -8.905  11.129  1.00 12.64 ?  122 LEU   A CA   1 
ATOM   2544 C  C    . LEU   A 1 122 ? 21.718 -8.315  11.101  1.00 12.53 ?  122 LEU   A C    1 
ATOM   2545 O  O    . LEU   A 1 122 ? 20.730 -9.035  10.959  1.00 13.48 ?  122 LEU   A O    1 
ATOM   2546 C  CB   . LEU   A 1 122 ? 23.537 -9.012  9.658   1.00 13.85 ?  122 LEU   A CB   1 
ATOM   2547 C  CG   . LEU   A 1 122 ? 24.753 -9.854  9.300   1.00 13.85 ?  122 LEU   A CG   1 
ATOM   2548 C  CD1  . LEU   A 1 122 ? 24.373 -11.314 9.084   1.00 14.67 ?  122 LEU   A CD1  1 
ATOM   2549 C  CD2  . LEU   A 1 122 ? 25.443 -9.277  8.063   1.00 13.48 ?  122 LEU   A CD2  1 
ATOM   2550 H  H    . LEU   A 1 122 ? 22.408 -10.674 11.646  1.00 15.34 ?  122 LEU   A H    1 
ATOM   2551 H  HA   . LEU   A 1 122 ? 23.716 -8.291  11.586  1.00 15.16 ?  122 LEU   A HA   1 
ATOM   2552 H  HB2  . LEU   A 1 122 ? 22.798 -9.383  9.161   1.00 16.62 ?  122 LEU   A HB2  1 
ATOM   2553 H  HB3  . LEU   A 1 122 ? 23.723 -8.118  9.334   1.00 16.62 ?  122 LEU   A HB3  1 
ATOM   2554 H  HG   . LEU   A 1 122 ? 25.399 -9.822  10.023  1.00 16.62 ?  122 LEU   A HG   1 
ATOM   2555 H  HD11 . LEU   A 1 122 ? 25.159 -11.816 8.811   1.00 17.60 ?  122 LEU   A HD11 1 
ATOM   2556 H  HD12 . LEU   A 1 122 ? 24.027 -11.673 9.915   1.00 17.60 ?  122 LEU   A HD12 1 
ATOM   2557 H  HD13 . LEU   A 1 122 ? 23.695 -11.366 8.392   1.00 17.60 ?  122 LEU   A HD13 1 
ATOM   2558 H  HD21 . LEU   A 1 122 ? 26.197 -9.844  7.816   1.00 16.17 ?  122 LEU   A HD21 1 
ATOM   2559 H  HD22 . LEU   A 1 122 ? 24.809 -9.245  7.328   1.00 16.17 ?  122 LEU   A HD22 1 
ATOM   2560 H  HD23 . LEU   A 1 122 ? 25.762 -8.382  8.261   1.00 16.17 ?  122 LEU   A HD23 1 
ATOM   2561 N  N    . LEU   A 1 123 ? 21.655 -6.986  11.197  1.00 12.04 ?  123 LEU   A N    1 
ATOM   2562 C  CA   . LEU   A 1 123 ? 20.481 -6.196  10.831  1.00 12.11 ?  123 LEU   A CA   1 
ATOM   2563 C  C    . LEU   A 1 123 ? 20.724 -5.667  9.424   1.00 11.30 ?  123 LEU   A C    1 
ATOM   2564 O  O    . LEU   A 1 123 ? 21.778 -5.080  9.176   1.00 12.16 ?  123 LEU   A O    1 
ATOM   2565 C  CB   . LEU   A 1 123 ? 20.355 -5.020  11.797  1.00 12.25 ?  123 LEU   A CB   1 
ATOM   2566 C  CG   . LEU   A 1 123 ? 19.314 -3.954  11.453  1.00 13.02 ?  123 LEU   A CG   1 
ATOM   2567 C  CD1  . LEU   A 1 123 ? 17.908 -4.539  11.465  1.00 13.81 ?  123 LEU   A CD1  1 
ATOM   2568 C  CD2  . LEU   A 1 123 ? 19.421 -2.783  12.425  1.00 13.99 ?  123 LEU   A CD2  1 
ATOM   2569 H  H    . LEU   A 1 123 ? 22.309 -6.500  11.477  1.00 14.44 ?  123 LEU   A H    1 
ATOM   2570 H  HA   . LEU   A 1 123 ? 19.674 -6.736  10.856  1.00 14.52 ?  123 LEU   A HA   1 
ATOM   2571 H  HB2  . LEU   A 1 123 ? 20.124 -5.362  12.675  1.00 14.70 ?  123 LEU   A HB2  1 
ATOM   2572 H  HB3  . LEU   A 1 123 ? 21.212 -4.569  11.846  1.00 14.70 ?  123 LEU   A HB3  1 
ATOM   2573 H  HG   . LEU   A 1 123 ? 19.484 -3.608  10.560  1.00 15.62 ?  123 LEU   A HG   1 
ATOM   2574 H  HD11 . LEU   A 1 123 ? 17.266 -3.839  11.282  1.00 16.56 ?  123 LEU   A HD11 1 
ATOM   2575 H  HD12 . LEU   A 1 123 ? 17.849 -5.231  10.785  1.00 16.56 ?  123 LEU   A HD12 1 
ATOM   2576 H  HD13 . LEU   A 1 123 ? 17.737 -4.926  12.341  1.00 16.56 ?  123 LEU   A HD13 1 
ATOM   2577 H  HD21 . LEU   A 1 123 ? 18.756 -2.116  12.196  1.00 16.79 ?  123 LEU   A HD21 1 
ATOM   2578 H  HD22 . LEU   A 1 123 ? 19.265 -3.110  13.326  1.00 16.79 ?  123 LEU   A HD22 1 
ATOM   2579 H  HD23 . LEU   A 1 123 ? 20.310 -2.402  12.362  1.00 16.79 ?  123 LEU   A HD23 1 
ATOM   2580 N  N    A ALA   A 1 124 ? 19.758 -5.837  8.524   0.68 11.00 ?  124 ALA   A N    1 
ATOM   2581 N  N    B ALA   A 1 124 ? 19.792 -5.904  8.497   0.32 11.45 ?  124 ALA   A N    1 
ATOM   2582 C  CA   A ALA   A 1 124 ? 20.035 -5.534  7.129   0.68 10.35 ?  124 ALA   A CA   1 
ATOM   2583 C  CA   B ALA   A 1 124 ? 20.119 -5.716  7.087   0.32 11.60 ?  124 ALA   A CA   1 
ATOM   2584 C  C    A ALA   A 1 124 ? 18.782 -5.055  6.417   0.68 10.32 ?  124 ALA   A C    1 
ATOM   2585 C  C    B ALA   A 1 124 ? 18.899 -5.332  6.260   0.32 10.86 ?  124 ALA   A C    1 
ATOM   2586 O  O    A ALA   A 1 124 ? 17.657 -5.391  6.814   0.68 10.98 ?  124 ALA   A O    1 
ATOM   2587 O  O    B ALA   A 1 124 ? 17.765 -5.657  6.633   0.32 11.06 ?  124 ALA   A O    1 
ATOM   2588 C  CB   A ALA   A 1 124 ? 20.592 -6.754  6.392   0.68 10.60 ?  124 ALA   A CB   1 
ATOM   2589 C  CB   B ALA   A 1 124 ? 20.759 -6.984  6.499   0.32 12.72 ?  124 ALA   A CB   1 
ATOM   2590 H  H    A ALA   A 1 124 ? 18.958 -6.120  8.691   0.68 13.20 ?  124 ALA   A H    1 
ATOM   2591 H  H    B ALA   A 1 124 ? 18.984 -6.160  8.650   0.32 13.74 ?  124 ALA   A H    1 
ATOM   2592 H  HA   A ALA   A 1 124 ? 20.700 -4.826  7.101   0.68 12.42 ?  124 ALA   A HA   1 
ATOM   2593 H  HA   B ALA   A 1 124 ? 20.771 -5.005  7.018   0.32 13.92 ?  124 ALA   A HA   1 
ATOM   2594 H  HB1  A ALA   A 1 124 ? 20.771 -6.511  5.469   0.68 12.71 ?  124 ALA   A HB1  1 
ATOM   2595 H  HB1  B ALA   A 1 124 ? 20.971 -6.830  5.564   0.32 15.26 ?  124 ALA   A HB1  1 
ATOM   2596 H  HB2  A ALA   A 1 124 ? 21.419 -7.032  6.823   0.68 12.71 ?  124 ALA   A HB2  1 
ATOM   2597 H  HB2  B ALA   A 1 124 ? 21.575 -7.188  6.989   0.32 15.26 ?  124 ALA   A HB2  1 
ATOM   2598 H  HB3  A ALA   A 1 124 ? 19.943 -7.470  6.428   0.68 12.71 ?  124 ALA   A HB3  1 
ATOM   2599 H  HB3  B ALA   A 1 124 ? 20.136 -7.723  6.579   0.32 15.26 ?  124 ALA   A HB3  1 
ATOM   2600 N  N    A PRO   A 1 125 ? 18.949 -4.295  5.343   0.68 10.21 ?  125 PRO   A N    1 
ATOM   2601 N  N    B PRO   A 1 125 ? 19.104 -4.646  5.117   0.32 9.92  ?  125 PRO   A N    1 
ATOM   2602 C  CA   A PRO   A 1 125 ? 17.875 -4.058  4.385   0.68 10.89 ?  125 PRO   A CA   1 
ATOM   2603 C  CA   B PRO   A 1 125 ? 18.011 -4.396  4.171   0.32 10.32 ?  125 PRO   A CA   1 
ATOM   2604 C  C    A PRO   A 1 125 ? 17.939 -5.132  3.306   0.68 10.87 ?  125 PRO   A C    1 
ATOM   2605 C  C    B PRO   A 1 125 ? 18.030 -5.397  3.024   0.32 10.33 ?  125 PRO   A C    1 
ATOM   2606 O  O    A PRO   A 1 125 ? 18.890 -5.915  3.225   0.68 10.90 ?  125 PRO   A O    1 
ATOM   2607 O  O    B PRO   A 1 125 ? 19.041 -6.072  2.804   0.32 10.33 ?  125 PRO   A O    1 
ATOM   2608 C  CB   A PRO   A 1 125 ? 18.296 -2.712  3.785   0.68 11.57 ?  125 PRO   A CB   1 
ATOM   2609 C  CB   B PRO   A 1 125 ? 18.354 -2.998  3.648   0.32 10.34 ?  125 PRO   A CB   1 
ATOM   2610 C  CG   A PRO   A 1 125 ? 19.801 -2.859  3.682   0.68 12.24 ?  125 PRO   A CG   1 
ATOM   2611 C  CG   B PRO   A 1 125 ? 19.872 -3.039  3.572   0.32 10.03 ?  125 PRO   A CG   1 
ATOM   2612 C  CD   A PRO   A 1 125 ? 20.189 -3.593  4.952   0.68 11.56 ?  125 PRO   A CD   1 
ATOM   2613 C  CD   B PRO   A 1 125 ? 20.335 -3.940  4.712   0.32 9.27  ?  125 PRO   A CD   1 
ATOM   2614 H  HA   A PRO   A 1 125 ? 16.999 -4.018  4.805   0.68 13.07 ?  125 PRO   A HA   1 
ATOM   2615 H  HA   B PRO   A 1 125 ? 17.144 -4.394  4.614   0.32 12.38 ?  125 PRO   A HA   1 
ATOM   2616 H  HB2  A PRO   A 1 125 ? 17.886 -2.596  2.915   0.68 13.88 ?  125 PRO   A HB2  1 
ATOM   2617 H  HB2  B PRO   A 1 125 ? 17.958 -2.867  2.770   0.32 12.40 ?  125 PRO   A HB2  1 
ATOM   2618 H  HB3  A PRO   A 1 125 ? 18.051 -1.993  4.390   0.68 13.88 ?  125 PRO   A HB3  1 
ATOM   2619 H  HB3  B PRO   A 1 125 ? 18.048 -2.324  4.274   0.32 12.40 ?  125 PRO   A HB3  1 
ATOM   2620 H  HG2  A PRO   A 1 125 ? 20.031 -3.385  2.895   0.68 14.68 ?  125 PRO   A HG2  1 
ATOM   2621 H  HG2  B PRO   A 1 125 ? 20.141 -3.410  2.716   0.32 12.03 ?  125 PRO   A HG2  1 
ATOM   2622 H  HG3  A PRO   A 1 125 ? 20.217 -1.985  3.643   0.68 14.68 ?  125 PRO   A HG3  1 
ATOM   2623 H  HG3  B PRO   A 1 125 ? 20.223 -2.143  3.680   0.32 12.03 ?  125 PRO   A HG3  1 
ATOM   2624 H  HD2  A PRO   A 1 125 ? 20.902 -4.226  4.777   0.68 13.87 ?  125 PRO   A HD2  1 
ATOM   2625 H  HD2  B PRO   A 1 125 ? 21.001 -4.573  4.398   0.32 11.12 ?  125 PRO   A HD2  1 
ATOM   2626 H  HD3  A PRO   A 1 125 ? 20.443 -2.957  5.643   0.68 13.87 ?  125 PRO   A HD3  1 
ATOM   2627 H  HD3  B PRO   A 1 125 ? 20.677 -3.403  5.447   0.32 11.12 ?  125 PRO   A HD3  1 
ATOM   2628 N  N    A LEU   A 1 126 ? 16.918 -5.136  2.455   0.68 11.32 ?  126 LEU   A N    1 
ATOM   2629 N  N    B LEU   A 1 126 ? 16.938 -5.489  2.269   0.32 10.87 ?  126 LEU   A N    1 
ATOM   2630 C  CA   A LEU   A 1 126 ? 16.940 -5.991  1.276   0.68 11.66 ?  126 LEU   A CA   1 
ATOM   2631 C  CA   B LEU   A 1 126 ? 16.930 -6.295  1.052   0.32 11.07 ?  126 LEU   A CA   1 
ATOM   2632 C  C    A LEU   A 1 126 ? 17.891 -5.408  0.236   0.68 11.60 ?  126 LEU   A C    1 
ATOM   2633 C  C    B LEU   A 1 126 ? 17.755 -5.588  -0.016  0.32 11.00 ?  126 LEU   A C    1 
ATOM   2634 O  O    A LEU   A 1 126 ? 17.719 -4.271  -0.214  0.68 12.40 ?  126 LEU   A O    1 
ATOM   2635 O  O    B LEU   A 1 126 ? 17.346 -4.554  -0.557  0.32 11.38 ?  126 LEU   A O    1 
ATOM   2636 C  CB   A LEU   A 1 126 ? 15.535 -6.141  0.701   0.68 13.09 ?  126 LEU   A CB   1 
ATOM   2637 C  CB   B LEU   A 1 126 ? 15.497 -6.531  0.588   0.32 11.21 ?  126 LEU   A CB   1 
ATOM   2638 C  CG   A LEU   A 1 126 ? 14.583 -7.067  1.458   0.68 13.68 ?  126 LEU   A CG   1 
ATOM   2639 C  CG   B LEU   A 1 126 ? 14.717 -7.513  1.465   0.32 11.54 ?  126 LEU   A CG   1 
ATOM   2640 C  CD1  A LEU   A 1 126 ? 13.181 -6.901  0.908   0.68 14.50 ?  126 LEU   A CD1  1 
ATOM   2641 C  CD1  B LEU   A 1 126 ? 13.248 -7.530  1.086   0.32 11.79 ?  126 LEU   A CD1  1 
ATOM   2642 C  CD2  A LEU   A 1 126 ? 15.024 -8.524  1.352   0.68 14.21 ?  126 LEU   A CD2  1 
ATOM   2643 C  CD2  B LEU   A 1 126 ? 15.317 -8.906  1.356   0.32 11.25 ?  126 LEU   A CD2  1 
ATOM   2644 H  H    A LEU   A 1 126 ? 16.210 -4.649  2.529   0.68 13.57 ?  126 LEU   A H    1 
ATOM   2645 H  H    B LEU   A 1 126 ? 16.197 -5.092  2.436   0.32 13.04 ?  126 LEU   A H    1 
ATOM   2646 H  HA   A LEU   A 1 126 ? 17.263 -6.866  1.520   0.68 13.99 ?  126 LEU   A HA   1 
ATOM   2647 H  HA   B LEU   A 1 126 ? 17.340 -7.156  1.233   0.32 13.28 ?  126 LEU   A HA   1 
ATOM   2648 H  HB2  A LEU   A 1 126 ? 15.119 -5.265  0.680   0.68 15.71 ?  126 LEU   A HB2  1 
ATOM   2649 H  HB2  B LEU   A 1 126 ? 15.021 -5.688  0.598   0.32 13.45 ?  126 LEU   A HB2  1 
ATOM   2650 H  HB3  A LEU   A 1 126 ? 15.608 -6.485  -0.200  0.68 15.71 ?  126 LEU   A HB3  1 
ATOM   2651 H  HB3  B LEU   A 1 126 ? 15.513 -6.891  -0.313  0.32 13.45 ?  126 LEU   A HB3  1 
ATOM   2652 H  HG   A LEU   A 1 126 ? 14.567 -6.821  2.396   0.68 16.41 ?  126 LEU   A HG   1 
ATOM   2653 H  HG   B LEU   A 1 126 ? 14.785 -7.231  2.390   0.32 13.84 ?  126 LEU   A HG   1 
ATOM   2654 H  HD11 A LEU   A 1 126 ? 12.580 -7.497  1.381   0.68 17.39 ?  126 LEU   A HD11 1 
ATOM   2655 H  HD11 B LEU   A 1 126 ? 12.781 -8.155  1.665   0.32 14.15 ?  126 LEU   A HD11 1 
ATOM   2656 H  HD12 A LEU   A 1 126 ? 12.899 -5.981  1.031   0.68 17.39 ?  126 LEU   A HD12 1 
ATOM   2657 H  HD12 B LEU   A 1 126 ? 12.883 -6.639  1.201   0.32 14.15 ?  126 LEU   A HD12 1 
ATOM   2658 H  HD13 A LEU   A 1 126 ? 13.186 -7.121  -0.039  0.68 17.39 ?  126 LEU   A HD13 1 
ATOM   2659 H  HD13 B LEU   A 1 126 ? 13.163 -7.809  0.162   0.32 14.15 ?  126 LEU   A HD13 1 
ATOM   2660 H  HD21 A LEU   A 1 126 ? 14.351 -9.091  1.760   0.68 17.05 ?  126 LEU   A HD21 1 
ATOM   2661 H  HD21 B LEU   A 1 126 ? 14.692 -9.547  1.724   0.32 13.49 ?  126 LEU   A HD21 1 
ATOM   2662 H  HD22 A LEU   A 1 126 ? 15.128 -8.756  0.415   0.68 17.05 ?  126 LEU   A HD22 1 
ATOM   2663 H  HD22 B LEU   A 1 126 ? 15.485 -9.103  0.421   0.32 13.49 ?  126 LEU   A HD22 1 
ATOM   2664 H  HD23 A LEU   A 1 126 ? 15.871 -8.632  1.814   0.68 17.05 ?  126 LEU   A HD23 1 
ATOM   2665 H  HD23 B LEU   A 1 126 ? 16.150 -8.930  1.854   0.32 13.49 ?  126 LEU   A HD23 1 
ATOM   2666 N  N    A LEU   A 1 127 ? 18.897 -6.186  -0.148  0.68 12.27 ?  127 LEU   A N    1 
ATOM   2667 N  N    B LEU   A 1 127 ? 18.922 -6.145  -0.316  0.32 10.56 ?  127 LEU   A N    1 
ATOM   2668 C  CA   A LEU   A 1 127 ? 19.892 -5.710  -1.096  0.68 11.84 ?  127 LEU   A CA   1 
ATOM   2669 C  CA   B LEU   A 1 127 ? 19.861 -5.500  -1.218  0.32 10.79 ?  127 LEU   A CA   1 
ATOM   2670 C  C    A LEU   A 1 127 ? 19.264 -5.495  -2.464  0.68 10.80 ?  127 LEU   A C    1 
ATOM   2671 C  C    B LEU   A 1 127 ? 19.327 -5.475  -2.649  0.32 10.91 ?  127 LEU   A C    1 
ATOM   2672 O  O    A LEU   A 1 127 ? 18.414 -6.273  -2.914  0.68 11.60 ?  127 LEU   A O    1 
ATOM   2673 O  O    B LEU   A 1 127 ? 18.546 -6.336  -3.071  0.32 10.79 ?  127 LEU   A O    1 
ATOM   2674 C  CB   A LEU   A 1 127 ? 21.053 -6.703  -1.213  0.68 11.61 ?  127 LEU   A CB   1 
ATOM   2675 C  CB   B LEU   A 1 127 ? 21.207 -6.227  -1.168  0.32 11.28 ?  127 LEU   A CB   1 
ATOM   2676 C  CG   A LEU   A 1 127 ? 21.888 -6.925  0.047   0.68 12.08 ?  127 LEU   A CG   1 
ATOM   2677 C  CG   B LEU   A 1 127 ? 21.934 -6.221  0.182   0.32 11.69 ?  127 LEU   A CG   1 
ATOM   2678 C  CD1  A LEU   A 1 127 ? 23.004 -7.897  -0.243  0.68 12.42 ?  127 LEU   A CD1  1 
ATOM   2679 C  CD1  B LEU   A 1 127 ? 23.113 -7.181  0.154   0.32 12.47 ?  127 LEU   A CD1  1 
ATOM   2680 C  CD2  A LEU   A 1 127 ? 22.459 -5.616  0.559   0.68 13.08 ?  127 LEU   A CD2  1 
ATOM   2681 C  CD2  B LEU   A 1 127 ? 22.399 -4.816  0.547   0.32 11.93 ?  127 LEU   A CD2  1 
ATOM   2682 H  H    A LEU   A 1 127 ? 19.027 -6.987  0.129   0.68 14.72 ?  127 LEU   A H    1 
ATOM   2683 H  H    B LEU   A 1 127 ? 19.199 -6.897  0.012   0.32 12.67 ?  127 LEU   A H    1 
ATOM   2684 H  HA   A LEU   A 1 127 ? 20.245 -4.863  -0.794  0.68 14.21 ?  127 LEU   A HA   1 
ATOM   2685 H  HA   B LEU   A 1 127 ? 20.002 -4.586  -0.921  0.32 12.95 ?  127 LEU   A HA   1 
ATOM   2686 H  HB2  A LEU   A 1 127 ? 20.689 -7.563  -1.479  0.68 13.92 ?  127 LEU   A HB2  1 
ATOM   2687 H  HB2  B LEU   A 1 127 ? 21.063 -7.154  -1.409  0.32 13.53 ?  127 LEU   A HB2  1 
ATOM   2688 H  HB3  A LEU   A 1 127 ? 21.654 -6.384  -1.907  0.68 13.92 ?  127 LEU   A HB3  1 
ATOM   2689 H  HB3  B LEU   A 1 127 ? 21.799 -5.811  -1.812  0.32 13.53 ?  127 LEU   A HB3  1 
ATOM   2690 H  HG   A LEU   A 1 127 ? 21.324 -7.305  0.739   0.68 14.49 ?  127 LEU   A HG   1 
ATOM   2691 H  HG   B LEU   A 1 127 ? 21.323 -6.523  0.873   0.32 14.02 ?  127 LEU   A HG   1 
ATOM   2692 H  HD11 A LEU   A 1 127 ? 23.513 -8.043  0.570   0.68 14.90 ?  127 LEU   A HD11 1 
ATOM   2693 H  HD11 B LEU   A 1 127 ? 23.589 -7.121  0.996   0.32 14.96 ?  127 LEU   A HD11 1 
ATOM   2694 H  HD12 A LEU   A 1 127 ? 22.624 -8.734  -0.551  0.68 14.90 ?  127 LEU   A HD12 1 
ATOM   2695 H  HD12 B LEU   A 1 127 ? 22.779 -8.084  0.026   0.32 14.96 ?  127 LEU   A HD12 1 
ATOM   2696 H  HD13 A LEU   A 1 127 ? 23.578 -7.522  -0.929  0.68 14.90 ?  127 LEU   A HD13 1 
ATOM   2697 H  HD13 B LEU   A 1 127 ? 23.699 -6.938  -0.578  0.32 14.96 ?  127 LEU   A HD13 1 
ATOM   2698 H  HD21 A LEU   A 1 127 ? 23.101 -5.806  1.259   0.68 15.69 ?  127 LEU   A HD21 1 
ATOM   2699 H  HD21 B LEU   A 1 127 ? 22.910 -4.856  1.371   0.32 14.31 ?  127 LEU   A HD21 1 
ATOM   2700 H  HD22 A LEU   A 1 127 ? 22.898 -5.156  -0.176  0.68 15.69 ?  127 LEU   A HD22 1 
ATOM   2701 H  HD22 B LEU   A 1 127 ? 22.953 -4.473  -0.171  0.32 14.31 ?  127 LEU   A HD22 1 
ATOM   2702 H  HD23 A LEU   A 1 127 ? 21.739 -5.069  0.906   0.68 15.69 ?  127 LEU   A HD23 1 
ATOM   2703 H  HD23 B LEU   A 1 127 ? 21.622 -4.249  0.666   0.32 14.31 ?  127 LEU   A HD23 1 
ATOM   2704 N  N    A SER   A 1 128 ? 19.712 -4.437  -3.129  0.68 10.83 ?  128 SER   A N    1 
ATOM   2705 N  N    B SER   A 1 128 ? 19.777 -4.469  -3.395  0.32 11.32 ?  128 SER   A N    1 
ATOM   2706 C  CA   A SER   A 1 128 ? 19.303 -4.033  -4.469  0.68 10.94 ?  128 SER   A CA   1 
ATOM   2707 C  CA   B SER   A 1 128 ? 19.419 -4.240  -4.792  0.32 11.07 ?  128 SER   A CA   1 
ATOM   2708 C  C    A SER   A 1 128 ? 17.844 -3.594  -4.557  0.68 11.37 ?  128 SER   A C    1 
ATOM   2709 C  C    B SER   A 1 128 ? 17.991 -3.729  -4.986  0.32 10.47 ?  128 SER   A C    1 
ATOM   2710 O  O    A SER   A 1 128 ? 17.364 -3.324  -5.658  0.68 12.63 ?  128 SER   A O    1 
ATOM   2711 O  O    B SER   A 1 128 ? 17.645 -3.278  -6.083  0.32 10.78 ?  128 SER   A O    1 
ATOM   2712 C  CB   A SER   A 1 128 ? 19.646 -5.064  -5.553  0.68 10.98 ?  128 SER   A CB   1 
ATOM   2713 C  CB   B SER   A 1 128 ? 19.711 -5.468  -5.665  0.32 11.56 ?  128 SER   A CB   1 
ATOM   2714 O  OG   A SER   A 1 128 ? 21.053 -5.268  -5.637  0.68 11.58 ?  128 SER   A OG   1 
ATOM   2715 O  OG   B SER   A 1 128 ? 21.110 -5.680  -5.796  0.32 11.26 ?  128 SER   A OG   1 
ATOM   2716 H  H    A SER   A 1 128 ? 20.303 -3.898  -2.802  0.68 12.99 ?  128 SER   A H    1 
ATOM   2717 H  H    B SER   A 1 128 ? 20.332 -3.887  -3.094  0.32 13.58 ?  128 SER   A H    1 
ATOM   2718 H  HA   A SER   A 1 128 ? 19.825 -3.251  -4.690  0.68 13.12 ?  128 SER   A HA   1 
ATOM   2719 H  HA   B SER   A 1 128 ? 19.995 -3.540  -5.114  0.32 13.28 ?  128 SER   A HA   1 
ATOM   2720 H  HB2  A SER   A 1 128 ? 19.211 -5.904  -5.342  0.68 13.17 ?  128 SER   A HB2  1 
ATOM   2721 H  HB2  B SER   A 1 128 ? 19.308 -6.256  -5.275  0.32 13.87 ?  128 SER   A HB2  1 
ATOM   2722 H  HB3  A SER   A 1 128 ? 19.329 -4.735  -6.412  0.68 13.17 ?  128 SER   A HB3  1 
ATOM   2723 H  HB3  B SER   A 1 128 ? 19.345 -5.312  -6.551  0.32 13.87 ?  128 SER   A HB3  1 
ATOM   2724 H  HG   A SER   A 1 128 ? 21.440 -4.547  -5.810  0.68 13.89 ?  128 SER   A HG   1 
ATOM   2725 H  HG   B SER   A 1 128 ? 21.472 -4.996  -6.126  0.32 13.51 ?  128 SER   A HG   1 
ATOM   2726 N  N    A ALA   A 1 129 ? 17.140 -3.488  -3.430  0.68 11.63 ?  129 ALA   A N    1 
ATOM   2727 N  N    B ALA   A 1 129 ? 17.169 -3.770  -3.936  0.32 10.37 ?  129 ALA   A N    1 
ATOM   2728 C  CA   A ALA   A 1 129 ? 15.774 -2.986  -3.419  0.68 12.10 ?  129 ALA   A CA   1 
ATOM   2729 C  CA   B ALA   A 1 129 ? 15.801 -3.277  -3.997  0.32 10.98 ?  129 ALA   A CA   1 
ATOM   2730 C  C    A ALA   A 1 129 ? 15.785 -1.457  -3.441  0.68 12.01 ?  129 ALA   A C    1 
ATOM   2731 C  C    B ALA   A 1 129 ? 15.791 -1.771  -3.724  0.32 11.91 ?  129 ALA   A C    1 
ATOM   2732 O  O    A ALA   A 1 129 ? 16.839 -0.815  -3.518  0.68 12.20 ?  129 ALA   A O    1 
ATOM   2733 O  O    B ALA   A 1 129 ? 16.829 -1.105  -3.771  0.32 11.89 ?  129 ALA   A O    1 
ATOM   2734 C  CB   A ALA   A 1 129 ? 15.009 -3.541  -2.216  0.68 13.67 ?  129 ALA   A CB   1 
ATOM   2735 C  CB   B ALA   A 1 129 ? 14.915 -4.076  -3.038  0.32 10.58 ?  129 ALA   A CB   1 
ATOM   2736 H  H    A ALA   A 1 129 ? 17.437 -3.708  -2.651  0.68 13.95 ?  129 ALA   A H    1 
ATOM   2737 H  H    B ALA   A 1 129 ? 17.383 -4.092  -3.165  0.32 12.44 ?  129 ALA   A H    1 
ATOM   2738 H  HA   A ALA   A 1 129 ? 15.325 -3.289  -4.218  0.68 14.51 ?  129 ALA   A HA   1 
ATOM   2739 H  HA   B ALA   A 1 129 ? 15.461 -3.418  -4.892  0.32 13.17 ?  129 ALA   A HA   1 
ATOM   2740 H  HB1  A ALA   A 1 129 ? 14.101 -3.200  -2.232  0.68 16.40 ?  129 ALA   A HB1  1 
ATOM   2741 H  HB1  B ALA   A 1 129 ? 14.005 -3.748  -3.104  0.32 12.69 ?  129 ALA   A HB1  1 
ATOM   2742 H  HB2  A ALA   A 1 129 ? 14.996 -4.511  -2.269  0.68 16.40 ?  129 ALA   A HB2  1 
ATOM   2743 H  HB2  B ALA   A 1 129 ? 14.947 -5.014  -3.285  0.32 12.69 ?  129 ALA   A HB2  1 
ATOM   2744 H  HB3  A ALA   A 1 129 ? 15.452 -3.263  -1.398  0.68 16.40 ?  129 ALA   A HB3  1 
ATOM   2745 H  HB3  B ALA   A 1 129 ? 15.245 -3.961  -2.133  0.32 12.69 ?  129 ALA   A HB3  1 
ATOM   2746 N  N    A GLY   A 1 130 ? 14.598 -0.862  -3.392  0.68 13.23 ?  130 GLY   A N    1 
ATOM   2747 N  N    B GLY   A 1 130 ? 14.612 -1.215  -3.452  0.32 12.73 ?  130 GLY   A N    1 
ATOM   2748 C  CA   A GLY   A 1 130 ? 14.520 0.590   -3.394  0.68 13.93 ?  130 GLY   A CA   1 
ATOM   2749 C  CA   B GLY   A 1 130 ? 14.521 0.210   -3.181  0.32 12.69 ?  130 GLY   A CA   1 
ATOM   2750 C  C    A GLY   A 1 130 ? 15.164 1.173   -4.638  0.68 13.77 ?  130 GLY   A C    1 
ATOM   2751 C  C    B GLY   A 1 130 ? 14.987 1.013   -4.378  0.32 12.44 ?  130 GLY   A C    1 
ATOM   2752 O  O    A GLY   A 1 130 ? 14.940 0.697   -5.758  0.68 14.08 ?  130 GLY   A O    1 
ATOM   2753 O  O    B GLY   A 1 130 ? 14.680 0.689   -5.530  0.32 12.22 ?  130 GLY   A O    1 
ATOM   2754 H  H    A GLY   A 1 130 ? 13.839 -1.270  -3.356  0.68 15.87 ?  130 GLY   A H    1 
ATOM   2755 H  H    B GLY   A 1 130 ? 13.862 -1.634  -3.430  0.32 15.28 ?  130 GLY   A H    1 
ATOM   2756 H  HA2  A GLY   A 1 130 ? 13.588 0.864   -3.362  0.68 16.71 ?  130 GLY   A HA2  1 
ATOM   2757 H  HA2  B GLY   A 1 130 ? 13.599 0.445   -2.970  0.32 15.23 ?  130 GLY   A HA2  1 
ATOM   2758 H  HA3  A GLY   A 1 130 ? 14.972 0.941   -2.612  0.68 16.71 ?  130 GLY   A HA3  1 
ATOM   2759 H  HA3  B GLY   A 1 130 ? 15.077 0.438   -2.422  0.32 15.23 ?  130 GLY   A HA3  1 
ATOM   2760 N  N    A ILE   A 1 131 ? 15.991 2.206   -4.443  0.68 13.39 ?  131 ILE   A N    1 
ATOM   2761 N  N    B ILE   A 1 131 ? 15.759 2.072   -4.109  0.32 12.53 ?  131 ILE   A N    1 
ATOM   2762 C  CA   A ILE   A 1 131 ? 16.559 2.951   -5.566  0.68 12.84 ?  131 ILE   A CA   1 
ATOM   2763 C  CA   B ILE   A 1 131 ? 16.264 2.925   -5.182  0.32 12.44 ?  131 ILE   A CA   1 
ATOM   2764 C  C    A ILE   A 1 131 ? 17.566 2.157   -6.385  0.68 12.21 ?  131 ILE   A C    1 
ATOM   2765 C  C    B ILE   A 1 131 ? 17.272 2.221   -6.081  0.32 12.27 ?  131 ILE   A C    1 
ATOM   2766 O  O    A ILE   A 1 131 ? 17.977 2.631   -7.452  0.68 13.18 ?  131 ILE   A O    1 
ATOM   2767 O  O    B ILE   A 1 131 ? 17.669 2.788   -7.105  0.32 12.48 ?  131 ILE   A O    1 
ATOM   2768 C  CB   A ILE   A 1 131 ? 17.149 4.312   -5.133  0.68 13.93 ?  131 ILE   A CB   1 
ATOM   2769 C  CB   B ILE   A 1 131 ? 16.856 4.242   -4.633  0.32 12.70 ?  131 ILE   A CB   1 
ATOM   2770 C  CG1  A ILE   A 1 131 ? 18.397 4.134   -4.259  0.68 15.25 ?  131 ILE   A CG1  1 
ATOM   2771 C  CG1  B ILE   A 1 131 ? 18.074 3.963   -3.746  0.32 13.16 ?  131 ILE   A CG1  1 
ATOM   2772 C  CG2  A ILE   A 1 131 ? 16.097 5.140   -4.407  0.68 14.17 ?  131 ILE   A CG2  1 
ATOM   2773 C  CG2  B ILE   A 1 131 ? 15.793 5.024   -3.864  0.32 12.99 ?  131 ILE   A CG2  1 
ATOM   2774 C  CD1  A ILE   A 1 131 ? 19.041 5.462   -3.847  0.68 15.98 ?  131 ILE   A CD1  1 
ATOM   2775 C  CD1  B ILE   A 1 131 ? 18.735 5.218   -3.199  0.32 13.68 ?  131 ILE   A CD1  1 
ATOM   2776 H  H    A ILE   A 1 131 ? 16.226 2.498   -3.669  0.68 16.06 ?  131 ILE   A H    1 
ATOM   2777 H  H    B ILE   A 1 131 ? 15.992 2.321   -3.319  0.32 15.04 ?  131 ILE   A H    1 
ATOM   2778 H  HA   A ILE   A 1 131 ? 15.833 3.154   -6.168  0.68 15.41 ?  131 ILE   A HA   1 
ATOM   2779 H  HA   B ILE   A 1 131 ? 15.512 3.175   -5.741  0.32 14.92 ?  131 ILE   A HA   1 
ATOM   2780 H  HB   A ILE   A 1 131 ? 17.407 4.793   -5.933  0.68 16.72 ?  131 ILE   A HB   1 
ATOM   2781 H  HB   B ILE   A 1 131 ? 17.142 4.786   -5.384  0.32 15.23 ?  131 ILE   A HB   1 
ATOM   2782 H  HG12 A ILE   A 1 131 ? 18.154 3.656   -3.453  0.68 18.30 ?  131 ILE   A HG12 1 
ATOM   2783 H  HG12 B ILE   A 1 131 ? 17.793 3.424   -2.992  0.32 15.79 ?  131 ILE   A HG12 1 
ATOM   2784 H  HG13 A ILE   A 1 131 ? 19.063 3.629   -4.755  0.68 18.30 ?  131 ILE   A HG13 1 
ATOM   2785 H  HG13 B ILE   A 1 131 ? 18.737 3.486   -4.266  0.32 15.79 ?  131 ILE   A HG13 1 
ATOM   2786 H  HG21 A ILE   A 1 131 ? 16.416 6.050   -4.319  0.68 17.00 ?  131 ILE   A HG21 1 
ATOM   2787 H  HG21 B ILE   A 1 131 ? 16.148 5.895   -3.625  0.32 15.58 ?  131 ILE   A HG21 1 
ATOM   2788 H  HG22 A ILE   A 1 131 ? 15.277 5.124   -4.924  0.68 17.00 ?  131 ILE   A HG22 1 
ATOM   2789 H  HG22 B ILE   A 1 131 ? 15.013 5.133   -4.430  0.32 15.58 ?  131 ILE   A HG22 1 
ATOM   2790 H  HG23 A ILE   A 1 131 ? 15.943 4.753   -3.531  0.68 17.00 ?  131 ILE   A HG23 1 
ATOM   2791 H  HG23 B ILE   A 1 131 ? 15.555 4.531   -3.064  0.32 15.58 ?  131 ILE   A HG23 1 
ATOM   2792 H  HD11 A ILE   A 1 131 ? 19.895 5.282   -3.425  0.68 19.17 ?  131 ILE   A HD11 1 
ATOM   2793 H  HD11 B ILE   A 1 131 ? 19.577 4.973   -2.784  0.32 16.41 ?  131 ILE   A HD11 1 
ATOM   2794 H  HD12 A ILE   A 1 131 ? 19.172 6.009   -4.638  0.68 19.17 ?  131 ILE   A HD12 1 
ATOM   2795 H  HD12 B ILE   A 1 131 ? 18.894 5.835   -3.930  0.32 16.41 ?  131 ILE   A HD12 1 
ATOM   2796 H  HD13 A ILE   A 1 131 ? 18.454 5.919   -3.224  0.68 19.17 ?  131 ILE   A HD13 1 
ATOM   2797 H  HD13 B ILE   A 1 131 ? 18.149 5.626   -2.543  0.32 16.41 ?  131 ILE   A HD13 1 
ATOM   2798 N  N    A PHE   A 1 132 ? 17.980 0.969   -5.924  0.68 11.80 ?  132 PHE   A N    1 
ATOM   2799 N  N    B PHE   A 1 132 ? 17.702 1.004   -5.732  0.32 12.66 ?  132 PHE   A N    1 
ATOM   2800 C  CA   A PHE   A 1 132 ? 18.816 0.099   -6.748  0.68 12.21 ?  132 PHE   A CA   1 
ATOM   2801 C  CA   B PHE   A 1 132 ? 18.632 0.262   -6.578  0.32 12.82 ?  132 PHE   A CA   1 
ATOM   2802 C  C    A PHE   A 1 132 ? 18.013 -0.672  -7.797  0.68 13.11 ?  132 PHE   A C    1 
ATOM   2803 C  C    B PHE   A 1 132 ? 17.956 -0.450  -7.749  0.32 13.51 ?  132 PHE   A C    1 
ATOM   2804 O  O    A PHE   A 1 132 ? 18.613 -1.348  -8.639  0.68 13.75 ?  132 PHE   A O    1 
ATOM   2805 O  O    B PHE   A 1 132 ? 18.658 -0.893  -8.664  0.32 13.94 ?  132 PHE   A O    1 
ATOM   2806 C  CB   A PHE   A 1 132 ? 19.629 -0.873  -5.882  0.68 11.68 ?  132 PHE   A CB   1 
ATOM   2807 C  CB   B PHE   A 1 132 ? 19.456 -0.729  -5.747  0.32 12.66 ?  132 PHE   A CB   1 
ATOM   2808 C  CG   A PHE   A 1 132 ? 20.837 -0.259  -5.205  0.68 11.85 ?  132 PHE   A CG   1 
ATOM   2809 C  CG   B PHE   A 1 132 ? 20.672 -0.120  -5.091  0.32 12.58 ?  132 PHE   A CG   1 
ATOM   2810 C  CD1  A PHE   A 1 132 ? 20.706 0.777   -4.295  0.68 12.85 ?  132 PHE   A CD1  1 
ATOM   2811 C  CD1  B PHE   A 1 132 ? 20.539 0.831   -4.094  0.32 12.99 ?  132 PHE   A CD1  1 
ATOM   2812 C  CD2  A PHE   A 1 132 ? 22.102 -0.777  -5.442  0.68 12.61 ?  132 PHE   A CD2  1 
ATOM   2813 C  CD2  B PHE   A 1 132 ? 21.946 -0.523  -5.459  0.32 12.76 ?  132 PHE   A CD2  1 
ATOM   2814 C  CE1  A PHE   A 1 132 ? 21.826 1.314   -3.664  0.68 13.32 ?  132 PHE   A CE1  1 
ATOM   2815 C  CE1  B PHE   A 1 132 ? 21.656 1.383   -3.486  0.32 13.41 ?  132 PHE   A CE1  1 
ATOM   2816 C  CE2  A PHE   A 1 132 ? 23.219 -0.253  -4.814  0.68 13.27 ?  132 PHE   A CE2  1 
ATOM   2817 C  CE2  B PHE   A 1 132 ? 23.067 0.024   -4.854  0.32 13.54 ?  132 PHE   A CE2  1 
ATOM   2818 C  CZ   A PHE   A 1 132 ? 23.079 0.796   -3.922  0.68 13.34 ?  132 PHE   A CZ   1 
ATOM   2819 C  CZ   B PHE   A 1 132 ? 22.918 0.978   -3.865  0.32 13.41 ?  132 PHE   A CZ   1 
ATOM   2820 H  H    A PHE   A 1 132 ? 17.799 0.648   -5.142  0.68 14.15 ?  132 PHE   A H    1 
ATOM   2821 H  H    B PHE   A 1 132 ? 17.475 0.597   -5.010  0.32 15.19 ?  132 PHE   A H    1 
ATOM   2822 H  HA   A PHE   A 1 132 ? 19.454 0.654   -7.217  0.68 14.65 ?  132 PHE   A HA   1 
ATOM   2823 H  HA   B PHE   A 1 132 ? 19.254 0.897   -6.959  0.32 15.37 ?  132 PHE   A HA   1 
ATOM   2824 H  HB2  A PHE   A 1 132 ? 19.054 -1.225  -5.183  0.68 14.02 ?  132 PHE   A HB2  1 
ATOM   2825 H  HB2  B PHE   A 1 132 ? 18.896 -1.092  -5.044  0.32 15.19 ?  132 PHE   A HB2  1 
ATOM   2826 H  HB3  A PHE   A 1 132 ? 19.945 -1.605  -6.440  0.68 14.02 ?  132 PHE   A HB3  1 
ATOM   2827 H  HB3  B PHE   A 1 132 ? 19.761 -1.443  -6.327  0.32 15.19 ?  132 PHE   A HB3  1 
ATOM   2828 H  HD1  A PHE   A 1 132 ? 19.867 1.128   -4.112  0.68 15.42 ?  132 PHE   A HD1  1 
ATOM   2829 H  HD1  B PHE   A 1 132 ? 19.690 1.109   -3.835  0.32 15.58 ?  132 PHE   A HD1  1 
ATOM   2830 H  HD2  A PHE   A 1 132 ? 22.210 -1.484  -6.039  0.68 15.12 ?  132 PHE   A HD2  1 
ATOM   2831 H  HD2  B PHE   A 1 132 ? 22.053 -1.165  -6.124  0.32 15.31 ?  132 PHE   A HD2  1 
ATOM   2832 H  HE1  A PHE   A 1 132 ? 21.729 2.018   -3.060  0.68 15.98 ?  132 PHE   A HE1  1 
ATOM   2833 H  HE1  B PHE   A 1 132 ? 21.554 2.025   -2.821  0.32 16.09 ?  132 PHE   A HE1  1 
ATOM   2834 H  HE2  A PHE   A 1 132 ? 24.064 -0.600  -4.993  0.68 15.92 ?  132 PHE   A HE2  1 
ATOM   2835 H  HE2  B PHE   A 1 132 ? 23.918 -0.252  -5.112  0.32 16.24 ?  132 PHE   A HE2  1 
ATOM   2836 H  HZ   A PHE   A 1 132 ? 23.828 1.157   -3.501  0.68 16.00 ?  132 PHE   A HZ   1 
ATOM   2837 H  HZ   B PHE   A 1 132 ? 23.669 1.348   -3.457  0.32 16.09 ?  132 PHE   A HZ   1 
ATOM   2838 N  N    A GLY   A 1 133 ? 16.681 -0.610  -7.757  0.68 13.43 ?  133 GLY   A N    1 
ATOM   2839 N  N    B GLY   A 1 133 ? 16.627 -0.580  -7.755  0.32 13.78 ?  133 GLY   A N    1 
ATOM   2840 C  CA   A GLY   A 1 133 ? 15.864 -0.976  -8.900  0.68 14.31 ?  133 GLY   A CA   1 
ATOM   2841 C  CA   B GLY   A 1 133 ? 15.890 -0.948  -8.949  0.32 14.28 ?  133 GLY   A CA   1 
ATOM   2842 C  C    A GLY   A 1 133 ? 15.551 -2.446  -9.103  0.68 14.33 ?  133 GLY   A C    1 
ATOM   2843 C  C    B GLY   A 1 133 ? 15.307 -2.348  -8.975  0.32 14.32 ?  133 GLY   A C    1 
ATOM   2844 O  O    A GLY   A 1 133 ? 14.899 -2.775  -10.102 0.68 14.95 ?  133 GLY   A O    1 
ATOM   2845 O  O    B GLY   A 1 133 ? 14.414 -2.603  -9.793  0.32 14.38 ?  133 GLY   A O    1 
ATOM   2846 H  H    A GLY   A 1 133 ? 16.224 -0.358  -7.070  0.68 16.12 ?  133 GLY   A H    1 
ATOM   2847 H  H    B GLY   A 1 133 ? 16.125 -0.450  -7.068  0.32 16.53 ?  133 GLY   A H    1 
ATOM   2848 H  HA2  A GLY   A 1 133 ? 15.016 -0.510  -8.833  0.68 17.17 ?  133 GLY   A HA2  1 
ATOM   2849 H  HA2  B GLY   A 1 133 ? 15.150 -0.336  -9.059  0.32 17.13 ?  133 GLY   A HA2  1 
ATOM   2850 H  HA3  A GLY   A 1 133 ? 16.306 -0.663  -9.705  0.68 17.17 ?  133 GLY   A HA3  1 
ATOM   2851 H  HA3  B GLY   A 1 133 ? 16.470 -0.856  -9.721  0.32 17.13 ?  133 GLY   A HA3  1 
ATOM   2852 N  N    A ALA   A 1 134 ? 15.981 -3.341  -8.216  0.68 13.73 ?  134 ALA   A N    1 
ATOM   2853 N  N    B ALA   A 1 134 ? 15.770 -3.262  -8.130  0.32 14.03 ?  134 ALA   A N    1 
ATOM   2854 C  CA   A ALA   A 1 134 ? 15.628 -4.746  -8.366  0.68 14.22 ?  134 ALA   A CA   1 
ATOM   2855 C  CA   B ALA   A 1 134 ? 15.323 -4.644  -8.234  0.32 13.90 ?  134 ALA   A CA   1 
ATOM   2856 C  C    A ALA   A 1 134 ? 14.256 -5.029  -7.744  0.68 14.30 ?  134 ALA   A C    1 
ATOM   2857 C  C    B ALA   A 1 134 ? 14.043 -4.879  -7.439  0.32 13.31 ?  134 ALA   A C    1 
ATOM   2858 O  O    A ALA   A 1 134 ? 13.703 -4.230  -6.985  0.68 15.52 ?  134 ALA   A O    1 
ATOM   2859 O  O    B ALA   A 1 134 ? 13.715 -4.151  -6.499  0.32 13.45 ?  134 ALA   A O    1 
ATOM   2860 C  CB   A ALA   A 1 134 ? 16.704 -5.635  -7.743  0.68 15.12 ?  134 ALA   A CB   1 
ATOM   2861 C  CB   B ALA   A 1 134 ? 16.401 -5.612  -7.754  0.32 14.32 ?  134 ALA   A CB   1 
ATOM   2862 H  H    A ALA   A 1 134 ? 16.484 -3.158  -7.540  0.68 16.48 ?  134 ALA   A H    1 
ATOM   2863 H  H    B ALA   A 1 134 ? 16.331 -3.107  -7.496  0.32 16.83 ?  134 ALA   A H    1 
ATOM   2864 H  HA   A ALA   A 1 134 ? 15.582 -4.957  -9.312  0.68 17.06 ?  134 ALA   A HA   1 
ATOM   2865 H  HA   B ALA   A 1 134 ? 15.134 -4.838  -9.163  0.32 16.68 ?  134 ALA   A HA   1 
ATOM   2866 H  HB1  A ALA   A 1 134 ? 16.456 -6.563  -7.867  0.68 18.14 ?  134 ALA   A HB1  1 
ATOM   2867 H  HB1  B ALA   A 1 134 ? 16.069 -6.519  -7.857  0.32 17.18 ?  134 ALA   A HB1  1 
ATOM   2868 H  HB2  A ALA   A 1 134 ? 17.556 -5.460  -8.181  0.68 18.14 ?  134 ALA   A HB2  1 
ATOM   2869 H  HB2  B ALA   A 1 134 ? 17.193 -5.484  -8.294  0.32 17.18 ?  134 ALA   A HB2  1 
ATOM   2870 H  HB3  A ALA   A 1 134 ? 16.776 -5.432  -6.798  0.68 18.14 ?  134 ALA   A HB3  1 
ATOM   2871 H  HB3  B ALA   A 1 134 ? 16.594 -5.432  -6.824  0.32 17.18 ?  134 ALA   A HB3  1 
ATOM   2872 N  N    A ASP   A 1 135 ? 13.713 -6.195  -8.075  0.68 14.60 ?  135 ASP   A N    1 
ATOM   2873 N  N    B ASP   A 1 135 ? 13.328 -5.926  -7.832  0.32 13.24 ?  135 ASP   A N    1 
ATOM   2874 C  CA   A ASP   A 1 135 ? 12.450 -6.655  -7.497  0.68 15.85 ?  135 ASP   A CA   1 
ATOM   2875 C  CA   B ASP   A 1 135 ? 12.101 -6.328  -7.158  0.32 13.65 ?  135 ASP   A CA   1 
ATOM   2876 C  C    A ASP   A 1 135 ? 12.695 -7.106  -6.062  0.68 15.49 ?  135 ASP   A C    1 
ATOM   2877 C  C    B ASP   A 1 135 ? 12.436 -6.861  -5.772  0.32 13.40 ?  135 ASP   A C    1 
ATOM   2878 O  O    A ASP   A 1 135 ? 13.472 -8.045  -5.845  0.68 15.26 ?  135 ASP   A O    1 
ATOM   2879 O  O    B ASP   A 1 135 ? 13.204 -7.828  -5.661  0.32 13.79 ?  135 ASP   A O    1 
ATOM   2880 C  CB   A ASP   A 1 135 ? 11.934 -7.828  -8.329  0.68 17.85 ?  135 ASP   A CB   1 
ATOM   2881 C  CB   B ASP   A 1 135 ? 11.440 -7.428  -7.979  0.32 14.68 ?  135 ASP   A CB   1 
ATOM   2882 C  CG   A ASP   A 1 135 ? 10.627 -8.425  -7.799  0.68 20.16 ?  135 ASP   A CG   1 
ATOM   2883 C  CG   B ASP   A 1 135 ? 10.064 -7.800  -7.468  0.32 16.03 ?  135 ASP   A CG   1 
ATOM   2884 O  OD1  A ASP   A 1 135 ? 10.102 -7.959  -6.768  0.68 20.11 ?  135 ASP   A OD1  1 
ATOM   2885 O  OD1  B ASP   A 1 135 ? 9.750  -7.496  -6.297  0.32 16.40 ?  135 ASP   A OD1  1 
ATOM   2886 O  OD2  A ASP   A 1 135 ? 10.117 -9.370  -8.439  0.68 22.88 -1 135 ASP   A OD2  1 
ATOM   2887 O  OD2  B ASP   A 1 135 ? 9.300  -8.411  -8.241  0.32 16.96 -1 135 ASP   A OD2  1 
ATOM   2888 H  H    A ASP   A 1 135 ? 14.059 -6.742  -8.640  0.68 17.51 ?  135 ASP   A H    1 
ATOM   2889 H  H    B ASP   A 1 135 ? 13.531 -6.428  -8.496  0.32 15.88 ?  135 ASP   A H    1 
ATOM   2890 H  HA   A ASP   A 1 135 ? 11.802 -5.934  -7.523  0.68 19.02 ?  135 ASP   A HA   1 
ATOM   2891 H  HA   B ASP   A 1 135 ? 11.490 -5.574  -7.096  0.32 16.38 ?  135 ASP   A HA   1 
ATOM   2892 H  HB2  A ASP   A 1 135 ? 11.771 -7.523  -9.232  0.68 21.41 ?  135 ASP   A HB2  1 
ATOM   2893 H  HB2  B ASP   A 1 135 ? 11.360 -7.131  -8.898  0.32 17.61 ?  135 ASP   A HB2  1 
ATOM   2894 H  HB3  A ASP   A 1 135 ? 12.606 -8.527  -8.328  0.68 21.41 ?  135 ASP   A HB3  1 
ATOM   2895 H  HB3  B ASP   A 1 135 ? 11.985 -8.227  -7.933  0.32 17.61 ?  135 ASP   A HB3  1 
ATOM   2896 N  N    A PRO   A 1 136 ? 12.073 -6.479  -5.061  0.68 15.38 ?  136 PRO   A N    1 
ATOM   2897 N  N    B PRO   A 1 136 ? 11.897 -6.281  -4.696  0.32 13.25 ?  136 PRO   A N    1 
ATOM   2898 C  CA   A PRO   A 1 136 ? 12.338 -6.886  -3.667  0.68 15.71 ?  136 PRO   A CA   1 
ATOM   2899 C  CA   B PRO   A 1 136 ? 12.180 -6.821  -3.357  0.32 13.71 ?  136 PRO   A CA   1 
ATOM   2900 C  C    A PRO   A 1 136 ? 11.908 -8.307  -3.342  0.68 14.81 ?  136 PRO   A C    1 
ATOM   2901 C  C    B PRO   A 1 136 ? 11.783 -8.278  -3.176  0.32 13.58 ?  136 PRO   A C    1 
ATOM   2902 O  O    A PRO   A 1 136 ? 12.537 -8.954  -2.496  0.68 14.39 ?  136 PRO   A O    1 
ATOM   2903 O  O    B PRO   A 1 136 ? 12.346 -8.943  -2.297  0.32 12.81 ?  136 PRO   A O    1 
ATOM   2904 C  CB   A PRO   A 1 136 ? 11.564 -5.846  -2.846  0.68 17.03 ?  136 PRO   A CB   1 
ATOM   2905 C  CB   B PRO   A 1 136 ? 11.391 -5.891  -2.421  0.32 14.45 ?  136 PRO   A CB   1 
ATOM   2906 C  CG   A PRO   A 1 136 ? 10.501 -5.347  -3.777  0.68 17.82 ?  136 PRO   A CG   1 
ATOM   2907 C  CG   B PRO   A 1 136 ? 10.373 -5.228  -3.299  0.32 14.68 ?  136 PRO   A CG   1 
ATOM   2908 C  CD   A PRO   A 1 136 ? 11.096 -5.380  -5.147  0.68 16.78 ?  136 PRO   A CD   1 
ATOM   2909 C  CD   B PRO   A 1 136 ? 11.039 -5.087  -4.633  0.32 13.59 ?  136 PRO   A CD   1 
ATOM   2910 H  HA   A PRO   A 1 136 ? 13.286 -6.797  -3.471  0.68 18.85 ?  136 PRO   A HA   1 
ATOM   2911 H  HA   B PRO   A 1 136 ? 13.127 -6.728  -3.158  0.32 16.44 ?  136 PRO   A HA   1 
ATOM   2912 H  HB2  A PRO   A 1 136 ? 11.169 -6.273  -2.069  0.68 20.43 ?  136 PRO   A HB2  1 
ATOM   2913 H  HB2  B PRO   A 1 136 ? 10.960 -6.410  -1.725  0.32 17.33 ?  136 PRO   A HB2  1 
ATOM   2914 H  HB3  A PRO   A 1 136 ? 12.159 -5.129  -2.582  0.68 20.43 ?  136 PRO   A HB3  1 
ATOM   2915 H  HB3  B PRO   A 1 136 ? 11.989 -5.232  -2.035  0.32 17.33 ?  136 PRO   A HB3  1 
ATOM   2916 H  HG2  A PRO   A 1 136 ? 9.728  -5.929  -3.730  0.68 21.38 ?  136 PRO   A HG2  1 
ATOM   2917 H  HG2  B PRO   A 1 136 ? 9.585  -5.789  -3.369  0.32 17.61 ?  136 PRO   A HG2  1 
ATOM   2918 H  HG3  A PRO   A 1 136 ? 10.261 -4.440  -3.536  0.68 21.38 ?  136 PRO   A HG3  1 
ATOM   2919 H  HG3  B PRO   A 1 136 ? 10.145 -4.358  -2.938  0.32 17.61 ?  136 PRO   A HG3  1 
ATOM   2920 H  HD2  A PRO   A 1 136 ? 10.412 -5.588  -5.807  0.68 20.13 ?  136 PRO   A HD2  1 
ATOM   2921 H  HD2  B PRO   A 1 136 ? 10.374 -5.106  -5.341  0.32 16.31 ?  136 PRO   A HD2  1 
ATOM   2922 H  HD3  A PRO   A 1 136 ? 11.540 -4.543  -5.350  0.68 20.13 ?  136 PRO   A HD3  1 
ATOM   2923 H  HD3  B PRO   A 1 136 ? 11.574 -4.278  -4.668  0.32 16.31 ?  136 PRO   A HD3  1 
ATOM   2924 N  N    . ILE   A 1 137 ? 10.840 -8.802  -3.968  1.00 14.76 ?  137 ILE   A N    1 
ATOM   2925 C  CA   . ILE   A 1 137 ? 10.456 -10.204 -3.803  1.00 15.44 ?  137 ILE   A CA   1 
ATOM   2926 C  C    . ILE   A 1 137 ? 11.607 -11.110 -4.214  1.00 15.11 ?  137 ILE   A C    1 
ATOM   2927 O  O    . ILE   A 1 137 ? 11.918 -12.100 -3.539  1.00 15.45 ?  137 ILE   A O    1 
ATOM   2928 C  CB   . ILE   A 1 137 ? 9.167  -10.512 -4.591  1.00 17.54 ?  137 ILE   A CB   1 
ATOM   2929 C  CG1  . ILE   A 1 137 ? 7.990  -9.674  -4.075  1.00 19.91 ?  137 ILE   A CG1  1 
ATOM   2930 C  CG2  . ILE   A 1 137 ? 8.833  -12.005 -4.517  1.00 18.57 ?  137 ILE   A CG2  1 
ATOM   2931 C  CD1  . ILE   A 1 137 ? 6.713  -9.870  -4.865  1.00 21.85 ?  137 ILE   A CD1  1 
ATOM   2932 H  H    A ILE   A 1 137 ? 10.330 -8.350  -4.491  0.68 17.71 ?  137 ILE   A H    1 
ATOM   2933 H  H    B ILE   A 1 137 ? 10.422 -8.378  -4.587  0.32 17.71 ?  137 ILE   A H    1 
ATOM   2934 H  HA   . ILE   A 1 137 ? 10.277 -10.370 -2.869  1.00 18.52 ?  137 ILE   A HA   1 
ATOM   2935 H  HB   . ILE   A 1 137 ? 9.312  -10.279 -5.519  1.00 21.04 ?  137 ILE   A HB   1 
ATOM   2936 H  HG12 . ILE   A 1 137 ? 7.815  -9.911  -3.151  1.00 23.89 ?  137 ILE   A HG12 1 
ATOM   2937 H  HG13 . ILE   A 1 137 ? 8.231  -8.730  -4.129  1.00 23.89 ?  137 ILE   A HG13 1 
ATOM   2938 H  HG21 . ILE   A 1 137 ? 8.107  -12.206 -5.124  1.00 22.27 ?  137 ILE   A HG21 1 
ATOM   2939 H  HG22 . ILE   A 1 137 ? 9.607  -12.523 -4.774  1.00 22.27 ?  137 ILE   A HG22 1 
ATOM   2940 H  HG23 . ILE   A 1 137 ? 8.575  -12.220 -3.609  1.00 22.27 ?  137 ILE   A HG23 1 
ATOM   2941 H  HD11 . ILE   A 1 137 ? 5.971  -9.886  -4.247  1.00 26.22 ?  137 ILE   A HD11 1 
ATOM   2942 H  HD12 . ILE   A 1 137 ? 6.624  -9.136  -5.485  1.00 26.22 ?  137 ILE   A HD12 1 
ATOM   2943 H  HD13 . ILE   A 1 137 ? 6.746  -10.705 -5.356  1.00 26.22 ?  137 ILE   A HD13 1 
ATOM   2944 N  N    . HIS   A 1 138 ? 12.250 -10.786 -5.334  1.00 15.02 ?  138 HIS   A N    1 
ATOM   2945 C  CA   . HIS   A 1 138 ? 13.417 -11.543 -5.765  1.00 14.70 ?  138 HIS   A CA   1 
ATOM   2946 C  C    . HIS   A 1 138 ? 14.564 -11.412 -4.770  1.00 14.17 ?  138 HIS   A C    1 
ATOM   2947 O  O    . HIS   A 1 138 ? 15.227 -12.403 -4.441  1.00 14.49 ?  138 HIS   A O    1 
ATOM   2948 C  CB   . HIS   A 1 138 ? 13.837 -11.090 -7.160  1.00 15.50 ?  138 HIS   A CB   1 
ATOM   2949 C  CG   . HIS   A 1 138 ? 15.101 -11.732 -7.632  1.00 16.51 ?  138 HIS   A CG   1 
ATOM   2950 N  ND1  . HIS   A 1 138 ? 15.203 -13.085 -7.879  1.00 17.81 ?  138 HIS   A ND1  1 
ATOM   2951 C  CD2  . HIS   A 1 138 ? 16.325 -11.211 -7.876  1.00 16.70 ?  138 HIS   A CD2  1 
ATOM   2952 C  CE1  . HIS   A 1 138 ? 16.434 -13.365 -8.268  1.00 18.16 ?  138 HIS   A CE1  1 
ATOM   2953 N  NE2  . HIS   A 1 138 ? 17.135 -12.246 -8.275  1.00 17.36 ?  138 HIS   A NE2  1 
ATOM   2954 H  H    . HIS   A 1 138 ? 12.034 -10.135 -5.860  1.00 18.02 ?  138 HIS   A H    1 
ATOM   2955 H  HA   . HIS   A 1 138 ? 13.178 -12.478 -5.824  1.00 17.63 ?  138 HIS   A HA   1 
ATOM   2956 H  HB2  . HIS   A 1 138 ? 13.130 -11.319 -7.793  1.00 18.60 ?  138 HIS   A HB2  1 
ATOM   2957 H  HB3  . HIS   A 1 138 ? 13.971 -10.130 -7.158  1.00 18.60 ?  138 HIS   A HB3  1 
ATOM   2958 H  HD1  . HIS   A 1 138 ? 14.561 -13.656 -7.800  1.00 21.37 ?  138 HIS   A HD1  1 
ATOM   2959 H  HD2  . HIS   A 1 138 ? 16.565 -10.316 -7.796  1.00 20.03 ?  138 HIS   A HD2  1 
ATOM   2960 H  HE1  . HIS   A 1 138 ? 16.752 -14.207 -8.498  1.00 21.79 ?  138 HIS   A HE1  1 
ATOM   2961 N  N    . SER   A 1 139 ? 14.817 -10.199 -4.278  1.00 13.57 ?  139 SER   A N    1 
ATOM   2962 C  CA   . SER   A 1 139 ? 15.892 -10.016 -3.312  1.00 13.25 ?  139 SER   A CA   1 
ATOM   2963 C  C    . SER   A 1 139 ? 15.675 -10.868 -2.066  1.00 13.02 ?  139 SER   A C    1 
ATOM   2964 O  O    . SER   A 1 139 ? 16.627 -11.455 -1.538  1.00 13.30 ?  139 SER   A O    1 
ATOM   2965 C  CB   . SER   A 1 139 ? 16.017 -8.539  -2.947  1.00 13.04 ?  139 SER   A CB   1 
ATOM   2966 O  OG   . SER   A 1 139 ? 17.105 -8.361  -2.058  1.00 13.50 ?  139 SER   A OG   1 
ATOM   2967 H  H    . SER   A 1 139 ? 14.386 -9.484  -4.478  1.00 16.28 ?  139 SER   A H    1 
ATOM   2968 H  HA   . SER   A 1 139 ? 16.728 -10.290 -3.715  1.00 15.89 ?  139 SER   A HA   1 
ATOM   2969 H  HB2  . SER   A 1 139 ? 16.172 -8.019  -3.755  1.00 15.64 ?  139 SER   A HB2  1 
ATOM   2970 H  HB3  . SER   A 1 139 ? 15.199 -8.242  -2.515  1.00 15.64 ?  139 SER   A HB3  1 
ATOM   2971 H  HG   . SER   A 1 139 ? 17.181 -7.546  -1.856  1.00 16.20 ?  139 SER   A HG   1 
ATOM   2972 N  N    . LEU   A 1 140 ? 14.436 -10.942 -1.577  1.00 13.08 ?  140 LEU   A N    1 
ATOM   2973 C  CA   . LEU   A 1 140 ? 14.161 -11.762 -0.401  1.00 12.64 ?  140 LEU   A CA   1 
ATOM   2974 C  C    . LEU   A 1 140 ? 14.427 -13.233 -0.690  1.00 12.95 ?  140 LEU   A C    1 
ATOM   2975 O  O    . LEU   A 1 140 ? 14.979 -13.950 0.155   1.00 13.73 ?  140 LEU   A O    1 
ATOM   2976 C  CB   . LEU   A 1 140 ? 12.721 -11.540 0.059   1.00 13.00 ?  140 LEU   A CB   1 
ATOM   2977 C  CG   . LEU   A 1 140 ? 12.249 -12.394 1.236   1.00 13.95 ?  140 LEU   A CG   1 
ATOM   2978 C  CD1  . LEU   A 1 140 ? 13.165 -12.224 2.444   1.00 14.52 ?  140 LEU   A CD1  1 
ATOM   2979 C  CD2  . LEU   A 1 140 ? 10.791 -12.062 1.598   1.00 14.94 ?  140 LEU   A CD2  1 
ATOM   2980 H  H    . LEU   A 1 140 ? 13.753 -10.533 -1.901  1.00 15.69 ?  140 LEU   A H    1 
ATOM   2981 H  HA   . LEU   A 1 140 ? 14.749 -11.490 0.316   1.00 15.16 ?  140 LEU   A HA   1 
ATOM   2982 H  HB2  . LEU   A 1 140 ? 12.625 -10.614 0.321   1.00 15.59 ?  140 LEU   A HB2  1 
ATOM   2983 H  HB3  . LEU   A 1 140 ? 12.130 -11.729 -0.686  1.00 15.59 ?  140 LEU   A HB3  1 
ATOM   2984 H  HG   . LEU   A 1 140 ? 12.274 -13.329 0.976   1.00 16.74 ?  140 LEU   A HG   1 
ATOM   2985 H  HD11 . LEU   A 1 140 ? 12.784 -12.702 3.198   1.00 17.42 ?  140 LEU   A HD11 1 
ATOM   2986 H  HD12 . LEU   A 1 140 ? 14.038 -12.592 2.230   1.00 17.42 ?  140 LEU   A HD12 1 
ATOM   2987 H  HD13 . LEU   A 1 140 ? 13.242 -11.283 2.652   1.00 17.42 ?  140 LEU   A HD13 1 
ATOM   2988 H  HD21 . LEU   A 1 140 ? 10.517 -12.617 2.348   1.00 17.92 ?  140 LEU   A HD21 1 
ATOM   2989 H  HD22 . LEU   A 1 140 ? 10.732 -11.126 1.844   1.00 17.92 ?  140 LEU   A HD22 1 
ATOM   2990 H  HD23 . LEU   A 1 140 ? 10.225 -12.241 0.832   1.00 17.92 ?  140 LEU   A HD23 1 
ATOM   2991 N  N    . ARG   A 1 141 ? 14.048 -13.700 -1.881  1.00 13.37 ?  141 ARG   A N    1 
ATOM   2992 C  CA   . ARG   A 1 141 ? 14.287 -15.093 -2.244  1.00 14.75 ?  141 ARG   A CA   1 
ATOM   2993 C  C    . ARG   A 1 141 ? 15.783 -15.394 -2.265  1.00 13.49 ?  141 ARG   A C    1 
ATOM   2994 O  O    . ARG   A 1 141 ? 16.234 -16.411 -1.728  1.00 13.76 ?  141 ARG   A O    1 
ATOM   2995 C  CB   . ARG   A 1 141 ? 13.663 -15.368 -3.612  1.00 16.31 ?  141 ARG   A CB   1 
ATOM   2996 C  CG   . ARG   A 1 141 ? 13.657 -16.823 -4.025  1.00 19.82 ?  141 ARG   A CG   1 
ATOM   2997 C  CD   . ARG   A 1 141 ? 12.621 -17.583 -3.254  1.00 23.30 ?  141 ARG   A CD   1 
ATOM   2998 N  NE   . ARG   A 1 141 ? 13.234 -18.465 -2.276  1.00 24.60 ?  141 ARG   A NE   1 
ATOM   2999 C  CZ   . ARG   A 1 141 ? 12.578 -19.040 -1.277  1.00 25.25 ?  141 ARG   A CZ   1 
ATOM   3000 N  NH1  . ARG   A 1 141 ? 11.306 -18.761 -1.032  1.00 24.79 ?  141 ARG   A NH1  1 
ATOM   3001 N  NH2  . ARG   A 1 141 ? 13.216 -19.907 -0.496  1.00 26.27 ?  141 ARG   A NH2  1 
ATOM   3002 H  H    . ARG   A 1 141 ? 13.652 -13.238 -2.489  1.00 16.04 ?  141 ARG   A H    1 
ATOM   3003 H  HA   . ARG   A 1 141 ? 13.870 -15.678 -1.594  1.00 17.70 ?  141 ARG   A HA   1 
ATOM   3004 H  HB2  . ARG   A 1 141 ? 12.743 -15.057 -3.602  1.00 19.57 ?  141 ARG   A HB2  1 
ATOM   3005 H  HB3  . ARG   A 1 141 ? 14.162 -14.877 -4.282  1.00 19.57 ?  141 ARG   A HB3  1 
ATOM   3006 H  HG2  . ARG   A 1 141 ? 13.450 -16.893 -4.971  1.00 23.78 ?  141 ARG   A HG2  1 
ATOM   3007 H  HG3  . ARG   A 1 141 ? 14.526 -17.220 -3.843  1.00 23.78 ?  141 ARG   A HG3  1 
ATOM   3008 H  HD2  . ARG   A 1 141 ? 12.052 -16.959 -2.773  1.00 27.96 ?  141 ARG   A HD2  1 
ATOM   3009 H  HD3  . ARG   A 1 141 ? 12.083 -18.112 -3.869  1.00 27.96 ?  141 ARG   A HD3  1 
ATOM   3010 H  HE   . ARG   A 1 141 ? 14.036 -18.731 -2.426  1.00 29.52 ?  141 ARG   A HE   1 
ATOM   3011 H  HH11 . ARG   A 1 141 ? 10.875 -18.213 -1.538  1.00 29.74 ?  141 ARG   A HH11 1 
ATOM   3012 H  HH12 . ARG   A 1 141 ? 10.898 -19.143 -0.376  1.00 29.74 ?  141 ARG   A HH12 1 
ATOM   3013 H  HH21 . ARG   A 1 141 ? 14.037 -20.097 -0.648  1.00 31.52 ?  141 ARG   A HH21 1 
ATOM   3014 H  HH22 . ARG   A 1 141 ? 12.800 -20.279 0.162   1.00 31.52 ?  141 ARG   A HH22 1 
ATOM   3015 N  N    . VAL   A 1 142 ? 16.572 -14.519 -2.891  1.00 12.91 ?  142 VAL   A N    1 
ATOM   3016 C  CA   . VAL   A 1 142 ? 18.019 -14.725 -2.919  1.00 13.14 ?  142 VAL   A CA   1 
ATOM   3017 C  C    . VAL   A 1 142 ? 18.583 -14.705 -1.505  1.00 12.45 ?  142 VAL   A C    1 
ATOM   3018 O  O    . VAL   A 1 142 ? 19.453 -15.512 -1.157  1.00 13.11 ?  142 VAL   A O    1 
ATOM   3019 C  CB   . VAL   A 1 142 ? 18.711 -13.700 -3.838  1.00 13.23 ?  142 VAL   A CB   1 
ATOM   3020 C  CG1  . VAL   A 1 142 ? 20.223 -13.902 -3.810  1.00 13.53 ?  142 VAL   A CG1  1 
ATOM   3021 C  CG2  . VAL   A 1 142 ? 18.204 -13.826 -5.270  1.00 15.11 ?  142 VAL   A CG2  1 
ATOM   3022 H  H    . VAL   A 1 142 ? 16.299 -13.811 -3.305  1.00 15.49 ?  142 VAL   A H    1 
ATOM   3023 H  HA   . VAL   A 1 142 ? 18.198 -15.597 -3.291  1.00 15.77 ?  142 VAL   A HA   1 
ATOM   3024 H  HB   . VAL   A 1 142 ? 18.525 -12.796 -3.528  1.00 15.87 ?  142 VAL   A HB   1 
ATOM   3025 H  HG11 . VAL   A 1 142 ? 20.627 -13.397 -4.534  1.00 16.23 ?  142 VAL   A HG11 1 
ATOM   3026 H  HG12 . VAL   A 1 142 ? 20.573 -13.588 -2.959  1.00 16.23 ?  142 VAL   A HG12 1 
ATOM   3027 H  HG13 . VAL   A 1 142 ? 20.417 -14.846 -3.919  1.00 16.23 ?  142 VAL   A HG13 1 
ATOM   3028 H  HG21 . VAL   A 1 142 ? 18.679 -13.191 -5.831  1.00 18.12 ?  142 VAL   A HG21 1 
ATOM   3029 H  HG22 . VAL   A 1 142 ? 18.376 -14.731 -5.580  1.00 18.12 ?  142 VAL   A HG22 1 
ATOM   3030 H  HG23 . VAL   A 1 142 ? 17.257 -13.642 -5.284  1.00 18.12 ?  142 VAL   A HG23 1 
ATOM   3031 N  N    . CYS   A 1 143 ? 18.110 -13.779 -0.672  1.00 12.33 ?  143 CYS   A N    1 
ATOM   3032 C  CA   . CYS   A 1 143 ? 18.568 -13.731 0.712   1.00 12.77 ?  143 CYS   A CA   1 
ATOM   3033 C  C    . CYS   A 1 143 ? 18.346 -15.071 1.403   1.00 12.71 ?  143 CYS   A C    1 
ATOM   3034 O  O    . CYS   A 1 143 ? 19.269 -15.651 1.983   1.00 12.63 ?  143 CYS   A O    1 
ATOM   3035 C  CB   . CYS   A 1 143 ? 17.832 -12.618 1.456   1.00 13.43 ?  143 CYS   A CB   1 
ATOM   3036 S  SG   . CYS   A 1 143 ? 18.312 -12.437 3.193   1.00 13.39 ?  143 CYS   A SG   1 
ATOM   3037 H  H    . CYS   A 1 143 ? 17.530 -13.178 -0.882  1.00 14.79 ?  143 CYS   A H    1 
ATOM   3038 H  HA   . CYS   A 1 143 ? 19.515 -13.538 0.726   1.00 15.32 ?  143 CYS   A HA   1 
ATOM   3039 H  HB2  . CYS   A 1 143 ? 18.002 -11.777 1.005   1.00 16.11 ?  143 CYS   A HB2  1 
ATOM   3040 H  HB3  . CYS   A 1 143 ? 16.882 -12.809 1.432   1.00 16.11 ?  143 CYS   A HB3  1 
ATOM   3041 H  HG   . CYS   A 1 143 ? 17.742 -11.487 3.645   1.00 16.07 ?  143 CYS   A HG   1 
ATOM   3042 N  N    . VAL   A 1 144 ? 17.117 -15.584 1.347   1.00 13.00 ?  144 VAL   A N    1 
ATOM   3043 C  CA   . VAL   A 1 144 ? 16.784 -16.819 2.049   1.00 14.48 ?  144 VAL   A CA   1 
ATOM   3044 C  C    . VAL   A 1 144 ? 17.600 -17.989 1.517   1.00 14.55 ?  144 VAL   A C    1 
ATOM   3045 O  O    . VAL   A 1 144 ? 17.964 -18.903 2.272   1.00 14.80 ?  144 VAL   A O    1 
ATOM   3046 C  CB   . VAL   A 1 144 ? 15.267 -17.073 1.944   1.00 17.46 ?  144 VAL   A CB   1 
ATOM   3047 C  CG1  . VAL   A 1 144 ? 14.920 -18.513 2.281   1.00 19.87 ?  144 VAL   A CG1  1 
ATOM   3048 C  CG2  . VAL   A 1 144 ? 14.521 -16.081 2.835   1.00 17.39 ?  144 VAL   A CG2  1 
ATOM   3049 H  H    . VAL   A 1 144 ? 16.454 -15.232 0.909   1.00 15.60 ?  144 VAL   A H    1 
ATOM   3050 H  HA   . VAL   A 1 144 ? 16.996 -16.707 2.983   1.00 17.38 ?  144 VAL   A HA   1 
ATOM   3051 H  HB   . VAL   A 1 144 ? 14.985 -16.905 1.028   1.00 20.95 ?  144 VAL   A HB   1 
ATOM   3052 H  HG11 . VAL   A 1 144 ? 13.969 -18.570 2.474   1.00 23.84 ?  144 VAL   A HG11 1 
ATOM   3053 H  HG12 . VAL   A 1 144 ? 15.134 -19.078 1.523   1.00 23.84 ?  144 VAL   A HG12 1 
ATOM   3054 H  HG13 . VAL   A 1 144 ? 15.429 -18.787 3.059   1.00 23.84 ?  144 VAL   A HG13 1 
ATOM   3055 H  HG21 . VAL   A 1 144 ? 13.563 -16.229 2.748   1.00 20.86 ?  144 VAL   A HG21 1 
ATOM   3056 H  HG22 . VAL   A 1 144 ? 14.791 -16.211 3.756   1.00 20.86 ?  144 VAL   A HG22 1 
ATOM   3057 H  HG23 . VAL   A 1 144 ? 14.734 -15.172 2.555   1.00 20.86 ?  144 VAL   A HG23 1 
ATOM   3058 N  N    . ASP   A 1 145 ? 17.869 -18.004 0.215   1.00 14.36 ?  145 ASP   A N    1 
ATOM   3059 C  CA   . ASP   A 1 145 ? 18.589 -19.104 -0.418  1.00 14.79 ?  145 ASP   A CA   1 
ATOM   3060 C  C    . ASP   A 1 145 ? 20.110 -18.951 -0.361  1.00 14.65 ?  145 ASP   A C    1 
ATOM   3061 O  O    . ASP   A 1 145 ? 20.823 -19.842 -0.840  1.00 16.88 ?  145 ASP   A O    1 
ATOM   3062 C  CB   . ASP   A 1 145 ? 18.158 -19.240 -1.882  1.00 16.55 ?  145 ASP   A CB   1 
ATOM   3063 C  CG   . ASP   A 1 145 ? 16.718 -19.708 -2.036  1.00 18.47 ?  145 ASP   A CG   1 
ATOM   3064 O  OD1  . ASP   A 1 145 ? 16.146 -20.261 -1.072  1.00 19.03 ?  145 ASP   A OD1  1 
ATOM   3065 O  OD2  . ASP   A 1 145 ? 16.163 -19.524 -3.136  1.00 20.11 -1 145 ASP   A OD2  1 
ATOM   3066 H  H    . ASP   A 1 145 ? 17.631 -17.383 -0.337  1.00 17.23 ?  145 ASP   A H    1 
ATOM   3067 H  HA   . ASP   A 1 145 ? 18.355 -19.927 0.037   1.00 17.75 ?  145 ASP   A HA   1 
ATOM   3068 H  HB2  . ASP   A 1 145 ? 18.245 -18.380 -2.317  1.00 19.85 ?  145 ASP   A HB2  1 
ATOM   3069 H  HB3  . ASP   A 1 145 ? 18.730 -19.894 -2.314  1.00 19.85 ?  145 ASP   A HB3  1 
ATOM   3070 N  N    . THR   A 1 146 ? 20.627 -17.861 0.201   1.00 12.96 ?  146 THR   A N    1 
ATOM   3071 C  CA   . THR   A 1 146 ? 22.066 -17.597 0.215   1.00 12.48 ?  146 THR   A CA   1 
ATOM   3072 C  C    . THR   A 1 146 ? 22.628 -17.403 1.611   1.00 12.48 ?  146 THR   A C    1 
ATOM   3073 O  O    . THR   A 1 146 ? 23.703 -17.939 1.924   1.00 13.56 ?  146 THR   A O    1 
ATOM   3074 C  CB   . THR   A 1 146 ? 22.387 -16.348 -0.627  1.00 12.79 ?  146 THR   A CB   1 
ATOM   3075 O  OG1  . THR   A 1 146 ? 21.860 -16.513 -1.944  1.00 13.15 ?  146 THR   A OG1  1 
ATOM   3076 C  CG2  . THR   A 1 146 ? 23.885 -16.104 -0.704  1.00 13.27 ?  146 THR   A CG2  1 
ATOM   3077 H  H    . THR   A 1 146 ? 20.156 -17.244 0.580   1.00 15.55 ?  146 THR   A H    1 
ATOM   3078 H  HA   . THR   A 1 146 ? 22.526 -18.343 -0.186  1.00 14.97 ?  146 THR   A HA   1 
ATOM   3079 H  HB   . THR   A 1 146 ? 21.974 -15.570 -0.218  1.00 15.35 ?  146 THR   A HB   1 
ATOM   3080 H  HG1  . THR   A 1 146 ? 21.028 -16.600 -1.915  1.00 15.78 ?  146 THR   A HG1  1 
ATOM   3081 H  HG21 . THR   A 1 146 ? 24.075 -15.451 -1.394  1.00 15.92 ?  146 THR   A HG21 1 
ATOM   3082 H  HG22 . THR   A 1 146 ? 24.209 -15.766 0.146   1.00 15.92 ?  146 THR   A HG22 1 
ATOM   3083 H  HG23 . THR   A 1 146 ? 24.342 -16.930 -0.915  1.00 15.92 ?  146 THR   A HG23 1 
ATOM   3084 N  N    . VAL   A 1 147 ? 21.942 -16.631 2.448   1.00 12.47 ?  147 VAL   A N    1 
ATOM   3085 C  CA   . VAL   A 1 147 ? 22.431 -16.328 3.784   1.00 12.64 ?  147 VAL   A CA   1 
ATOM   3086 C  C    . VAL   A 1 147 ? 22.115 -17.497 4.707   1.00 12.92 ?  147 VAL   A C    1 
ATOM   3087 O  O    . VAL   A 1 147 ? 20.974 -17.982 4.759   1.00 13.40 ?  147 VAL   A O    1 
ATOM   3088 C  CB   . VAL   A 1 147 ? 21.809 -15.021 4.302   1.00 12.61 ?  147 VAL   A CB   1 
ATOM   3089 C  CG1  . VAL   A 1 147 ? 22.345 -14.707 5.676   1.00 13.82 ?  147 VAL   A CG1  1 
ATOM   3090 C  CG2  . VAL   A 1 147 ? 22.061 -13.873 3.330   1.00 13.00 ?  147 VAL   A CG2  1 
ATOM   3091 H  H    . VAL   A 1 147 ? 21.179 -16.272 2.268   1.00 14.96 ?  147 VAL   A H    1 
ATOM   3092 H  HA   . VAL   A 1 147 ? 23.391 -16.216 3.755   1.00 15.16 ?  147 VAL   A HA   1 
ATOM   3093 H  HB   . VAL   A 1 147 ? 20.850 -15.143 4.383   1.00 15.12 ?  147 VAL   A HB   1 
ATOM   3094 H  HG11 . VAL   A 1 147 ? 22.100 -13.802 5.911   1.00 16.58 ?  147 VAL   A HG11 1 
ATOM   3095 H  HG12 . VAL   A 1 147 ? 21.962 -15.331 6.317   1.00 16.58 ?  147 VAL   A HG12 1 
ATOM   3096 H  HG13 . VAL   A 1 147 ? 23.311 -14.799 5.666   1.00 16.58 ?  147 VAL   A HG13 1 
ATOM   3097 H  HG21 . VAL   A 1 147 ? 21.723 -13.052 3.724   1.00 15.59 ?  147 VAL   A HG21 1 
ATOM   3098 H  HG22 . VAL   A 1 147 ? 23.009 -13.801 3.167   1.00 15.59 ?  147 VAL   A HG22 1 
ATOM   3099 H  HG23 . VAL   A 1 147 ? 21.590 -14.058 2.501   1.00 15.59 ?  147 VAL   A HG23 1 
ATOM   3100 N  N    . ARG   A 1 148 ? 23.136 -17.957 5.429   1.00 13.30 ?  148 ARG   A N    1 
ATOM   3101 C  CA   . ARG   A 1 148 ? 23.012 -19.031 6.401   1.00 13.52 ?  148 ARG   A CA   1 
ATOM   3102 C  C    . ARG   A 1 148 ? 23.138 -18.551 7.836   1.00 13.69 ?  148 ARG   A C    1 
ATOM   3103 O  O    . ARG   A 1 148 ? 22.731 -19.273 8.756   1.00 15.08 ?  148 ARG   A O    1 
ATOM   3104 C  CB   . ARG   A 1 148 ? 24.061 -20.121 6.134   1.00 14.08 ?  148 ARG   A CB   1 
ATOM   3105 C  CG   . ARG   A 1 148 ? 23.917 -20.765 4.770   1.00 15.30 ?  148 ARG   A CG   1 
ATOM   3106 C  CD   . ARG   A 1 148 ? 25.011 -21.793 4.498   1.00 16.40 ?  148 ARG   A CD   1 
ATOM   3107 N  NE   . ARG   A 1 148 ? 26.350 -21.212 4.514   1.00 16.11 ?  148 ARG   A NE   1 
ATOM   3108 C  CZ   . ARG   A 1 148 ? 26.859 -20.487 3.528   1.00 14.95 ?  148 ARG   A CZ   1 
ATOM   3109 N  NH1  . ARG   A 1 148 ? 26.184 -20.270 2.412   1.00 15.56 ?  148 ARG   A NH1  1 
ATOM   3110 N  NH2  . ARG   A 1 148 ? 28.075 -19.955 3.670   1.00 15.53 ?  148 ARG   A NH2  1 
ATOM   3111 H  H    . ARG   A 1 148 ? 23.937 -17.646 5.363   1.00 15.95 ?  148 ARG   A H    1 
ATOM   3112 H  HA   . ARG   A 1 148 ? 22.142 -19.436 6.306   1.00 16.21 ?  148 ARG   A HA   1 
ATOM   3113 H  HB2  . ARG   A 1 148 ? 24.948 -19.740 6.191   1.00 16.89 ?  148 ARG   A HB2  1 
ATOM   3114 H  HB3  . ARG   A 1 148 ? 23.961 -20.827 6.798   1.00 16.89 ?  148 ARG   A HB3  1 
ATOM   3115 H  HG2  . ARG   A 1 148 ? 23.056 -21.202 4.718   1.00 18.36 ?  148 ARG   A HG2  1 
ATOM   3116 H  HG3  . ARG   A 1 148 ? 23.979 -20.067 4.094   1.00 18.36 ?  148 ARG   A HG3  1 
ATOM   3117 H  HD2  . ARG   A 1 148 ? 24.971 -22.478 5.186   1.00 19.67 ?  148 ARG   A HD2  1 
ATOM   3118 H  HD3  . ARG   A 1 148 ? 24.858 -22.189 3.627   1.00 19.67 ?  148 ARG   A HD3  1 
ATOM   3119 H  HE   . ARG   A 1 148 ? 26.836 -21.346 5.207   1.00 19.33 ?  148 ARG   A HE   1 
ATOM   3120 H  HH11 . ARG   A 1 148 ? 25.399 -20.598 2.308   1.00 18.66 ?  148 ARG   A HH11 1 
ATOM   3121 H  HH12 . ARG   A 1 148 ? 26.535 -19.789 1.786   1.00 18.66 ?  148 ARG   A HH12 1 
ATOM   3122 H  HH21 . ARG   A 1 148 ? 28.518 -20.086 4.394   1.00 18.64 ?  148 ARG   A HH21 1 
ATOM   3123 H  HH22 . ARG   A 1 148 ? 28.414 -19.479 3.038   1.00 18.64 ?  148 ARG   A HH22 1 
ATOM   3124 N  N    . THR   A 1 149 ? 23.675 -17.353 8.042   1.00 13.83 ?  149 THR   A N    1 
ATOM   3125 C  CA   . THR   A 1 149 ? 23.754 -16.749 9.357   1.00 14.13 ?  149 THR   A CA   1 
ATOM   3126 C  C    . THR   A 1 149 ? 22.426 -16.054 9.661   1.00 13.55 ?  149 THR   A C    1 
ATOM   3127 O  O    . THR   A 1 149 ? 21.497 -16.048 8.845   1.00 13.89 ?  149 THR   A O    1 
ATOM   3128 C  CB   . THR   A 1 149 ? 24.959 -15.814 9.413   1.00 14.29 ?  149 THR   A CB   1 
ATOM   3129 O  OG1  . THR   A 1 149 ? 24.840 -14.884 8.336   1.00 14.03 ?  149 THR   A OG1  1 
ATOM   3130 C  CG2  . THR   A 1 149 ? 26.272 -16.601 9.293   1.00 14.85 ?  149 THR   A CG2  1 
ATOM   3131 H  H    . THR   A 1 149 ? 24.022 -16.863 7.417   1.00 16.59 ?  149 THR   A H    1 
ATOM   3132 H  HA   . THR   A 1 149 ? 23.885 -17.448 10.014  1.00 16.95 ?  149 THR   A HA   1 
ATOM   3133 H  HB   . THR   A 1 149 ? 24.954 -15.339 10.256  1.00 17.14 ?  149 THR   A HB   1 
ATOM   3134 H  HG1  . THR   A 1 149 ? 25.490 -14.347 8.340   1.00 16.83 ?  149 THR   A HG1  1 
ATOM   3135 H  HG21 . THR   A 1 149 ? 27.029 -15.997 9.344   1.00 17.81 ?  149 THR   A HG21 1 
ATOM   3136 H  HG22 . THR   A 1 149 ? 26.339 -17.251 10.012  1.00 17.81 ?  149 THR   A HG22 1 
ATOM   3137 H  HG23 . THR   A 1 149 ? 26.305 -17.073 8.443   1.00 17.81 ?  149 THR   A HG23 1 
ATOM   3138 N  N    . ASN   A 1 150 ? 22.302 -15.510 10.865  1.00 13.83 ?  150 ASN   A N    1 
ATOM   3139 C  CA   . ASN   A 1 150 ? 21.022 -14.989 11.338  1.00 14.15 ?  150 ASN   A CA   1 
ATOM   3140 C  C    . ASN   A 1 150 ? 20.844 -13.551 10.876  1.00 13.47 ?  150 ASN   A C    1 
ATOM   3141 O  O    . ASN   A 1 150 ? 21.601 -12.659 11.283  1.00 14.82 ?  150 ASN   A O    1 
ATOM   3142 C  CB   . ASN   A 1 150 ? 20.953 -15.086 12.856  1.00 16.93 ?  150 ASN   A CB   1 
ATOM   3143 C  CG   . ASN   A 1 150 ? 20.860 -16.515 13.328  1.00 21.05 ?  150 ASN   A CG   1 
ATOM   3144 O  OD1  . ASN   A 1 150 ? 20.256 -17.353 12.660  1.00 22.35 ?  150 ASN   A OD1  1 
ATOM   3145 N  ND2  . ASN   A 1 150 ? 21.473 -16.810 14.469  1.00 23.64 ?  150 ASN   A ND2  1 
ATOM   3146 H  H    . ASN   A 1 150 ? 22.947 -15.428 11.429  1.00 16.59 ?  150 ASN   A H    1 
ATOM   3147 H  HA   . ASN   A 1 150 ? 20.301 -15.527 10.965  1.00 16.97 ?  150 ASN   A HA   1 
ATOM   3148 H  HB2  . ASN   A 1 150 ? 21.752 -14.695 13.237  1.00 20.31 ?  150 ASN   A HB2  1 
ATOM   3149 H  HB3  . ASN   A 1 150 ? 20.165 -14.617 13.170  1.00 20.31 ?  150 ASN   A HB3  1 
ATOM   3150 H  HD21 . ASN   A 1 150 ? 21.452 -17.615 14.782  1.00 28.37 ?  150 ASN   A HD21 1 
ATOM   3151 H  HD22 . ASN   A 1 150 ? 21.891 -16.197 14.907  1.00 28.37 ?  150 ASN   A HD22 1 
ATOM   3152 N  N    . VAL   A 1 151 ? 19.846 -13.323 10.029  1.00 13.17 ?  151 VAL   A N    1 
ATOM   3153 C  CA   . VAL   A 1 151 ? 19.631 -12.018 9.427   1.00 13.22 ?  151 VAL   A CA   1 
ATOM   3154 C  C    . VAL   A 1 151 ? 18.245 -11.505 9.790   1.00 12.75 ?  151 VAL   A C    1 
ATOM   3155 O  O    . VAL   A 1 151 ? 17.235 -12.216 9.646   1.00 14.22 ?  151 VAL   A O    1 
ATOM   3156 C  CB   . VAL   A 1 151 ? 19.918 -12.014 7.911   1.00 14.69 ?  151 VAL   A CB   1 
ATOM   3157 C  CG1  . VAL   A 1 151 ? 19.092 -13.045 7.173   1.00 15.86 ?  151 VAL   A CG1  1 
ATOM   3158 C  CG2  . VAL   A 1 151 ? 19.719 -10.611 7.334   1.00 14.45 ?  151 VAL   A CG2  1 
ATOM   3159 H  H    . VAL   A 1 151 ? 19.273 -13.918 9.785   1.00 15.79 ?  151 VAL   A H    1 
ATOM   3160 H  HA   . VAL   A 1 151 ? 20.268 -11.402 9.823   1.00 15.86 ?  151 VAL   A HA   1 
ATOM   3161 H  HB   . VAL   A 1 151 ? 20.854 -12.248 7.778   1.00 17.62 ?  151 VAL   A HB   1 
ATOM   3162 H  HG11 . VAL   A 1 151 ? 19.290 -12.999 6.224   1.00 19.03 ?  151 VAL   A HG11 1 
ATOM   3163 H  HG12 . VAL   A 1 151 ? 19.315 -13.934 7.509   1.00 19.03 ?  151 VAL   A HG12 1 
ATOM   3164 H  HG13 . VAL   A 1 151 ? 18.150 -12.869 7.323   1.00 19.03 ?  151 VAL   A HG13 1 
ATOM   3165 H  HG21 . VAL   A 1 151 ? 20.046 -10.597 6.417   1.00 17.34 ?  151 VAL   A HG21 1 
ATOM   3166 H  HG22 . VAL   A 1 151 ? 18.777 -10.389 7.349   1.00 17.34 ?  151 VAL   A HG22 1 
ATOM   3167 H  HG23 . VAL   A 1 151 ? 20.222 -9.973  7.867   1.00 17.34 ?  151 VAL   A HG23 1 
ATOM   3168 N  N    . TYR   A 1 152 ? 18.226 -10.263 10.267  1.00 12.85 ?  152 TYR   A N    1 
ATOM   3169 C  CA   . TYR   A 1 152 ? 17.030 -9.532  10.654  1.00 12.78 ?  152 TYR   A CA   1 
ATOM   3170 C  C    . TYR   A 1 152 ? 16.829 -8.426  9.627   1.00 12.36 ?  152 TYR   A C    1 
ATOM   3171 O  O    . TYR   A 1 152 ? 17.603 -7.463  9.582   1.00 12.73 ?  152 TYR   A O    1 
ATOM   3172 C  CB   . TYR   A 1 152 ? 17.215 -8.987  12.066  1.00 13.91 ?  152 TYR   A CB   1 
ATOM   3173 C  CG   . TYR   A 1 152 ? 17.182 -10.108 13.072  1.00 14.91 ?  152 TYR   A CG   1 
ATOM   3174 C  CD1  . TYR   A 1 152 ? 18.314 -10.858 13.357  1.00 16.57 ?  152 TYR   A CD1  1 
ATOM   3175 C  CD2  . TYR   A 1 152 ? 15.996 -10.459 13.700  1.00 15.14 ?  152 TYR   A CD2  1 
ATOM   3176 C  CE1  . TYR   A 1 152 ? 18.277 -11.909 14.251  1.00 18.01 ?  152 TYR   A CE1  1 
ATOM   3177 C  CE2  . TYR   A 1 152 ? 15.944 -11.520 14.603  1.00 17.03 ?  152 TYR   A CE2  1 
ATOM   3178 C  CZ   . TYR   A 1 152 ? 17.094 -12.239 14.873  1.00 18.01 ?  152 TYR   A CZ   1 
ATOM   3179 O  OH   . TYR   A 1 152 ? 17.063 -13.296 15.765  1.00 20.73 ?  152 TYR   A OH   1 
ATOM   3180 H  H    . TYR   A 1 152 ? 18.943 -9.787  10.362  1.00 15.41 ?  152 TYR   A H    1 
ATOM   3181 H  HA   . TYR   A 1 152 ? 16.264 -10.129 10.638  1.00 15.33 ?  152 TYR   A HA   1 
ATOM   3182 H  HB2  . TYR   A 1 152 ? 18.075 -8.549  12.131  1.00 16.69 ?  152 TYR   A HB2  1 
ATOM   3183 H  HB3  . TYR   A 1 152 ? 16.498 -8.371  12.269  1.00 16.69 ?  152 TYR   A HB3  1 
ATOM   3184 H  HD1  . TYR   A 1 152 ? 19.114 -10.645 12.935  1.00 19.88 ?  152 TYR   A HD1  1 
ATOM   3185 H  HD2  . TYR   A 1 152 ? 15.215 -9.979  13.515  1.00 18.16 ?  152 TYR   A HD2  1 
ATOM   3186 H  HE1  . TYR   A 1 152 ? 19.046 -12.393 14.435  1.00 21.61 ?  152 TYR   A HE1  1 
ATOM   3187 H  HE2  . TYR   A 1 152 ? 15.142 -11.736 15.023  1.00 20.43 ?  152 TYR   A HE2  1 
ATOM   3188 H  HH   . TYR   A 1 152 ? 16.287 -13.378 16.077  1.00 24.87 ?  152 TYR   A HH   1 
ATOM   3189 N  N    A LEU   A 1 153 ? 15.818 -8.603  8.773   0.68 12.52 ?  153 LEU   A N    1 
ATOM   3190 N  N    B LEU   A 1 153 ? 15.789 -8.557  8.813   0.32 12.23 ?  153 LEU   A N    1 
ATOM   3191 C  CA   A LEU   A 1 153 ? 15.560 -7.728  7.634   0.68 12.85 ?  153 LEU   A CA   1 
ATOM   3192 C  CA   B LEU   A 1 153 ? 15.527 -7.600  7.751   0.32 12.20 ?  153 LEU   A CA   1 
ATOM   3193 C  C    A LEU   A 1 153 ? 14.554 -6.648  8.012   0.68 13.20 ?  153 LEU   A C    1 
ATOM   3194 C  C    B LEU   A 1 153 ? 14.567 -6.523  8.239   0.32 12.53 ?  153 LEU   A C    1 
ATOM   3195 O  O    A LEU   A 1 153 ? 13.430 -6.954  8.432   0.68 13.57 ?  153 LEU   A O    1 
ATOM   3196 O  O    B LEU   A 1 153 ? 13.541 -6.827  8.858   0.32 12.92 ?  153 LEU   A O    1 
ATOM   3197 C  CB   A LEU   A 1 153 ? 15.002 -8.540  6.463   0.68 12.52 ?  153 LEU   A CB   1 
ATOM   3198 C  CB   B LEU   A 1 153 ? 14.939 -8.313  6.534   0.32 12.34 ?  153 LEU   A CB   1 
ATOM   3199 C  CG   A LEU   A 1 153 ? 15.955 -9.530  5.787   0.68 12.58 ?  153 LEU   A CG   1 
ATOM   3200 C  CG   B LEU   A 1 153 ? 15.835 -9.388  5.917   0.32 12.42 ?  153 LEU   A CG   1 
ATOM   3201 C  CD1  A LEU   A 1 153 ? 15.184 -10.441 4.840   0.68 13.09 ?  153 LEU   A CD1  1 
ATOM   3202 C  CD1  B LEU   A 1 153 ? 15.035 -10.237 4.941   0.32 12.50 ?  153 LEU   A CD1  1 
ATOM   3203 C  CD2  A LEU   A 1 153 ? 17.061 -8.790  5.040   0.68 13.11 ?  153 LEU   A CD2  1 
ATOM   3204 C  CD2  B LEU   A 1 153 ? 17.047 -8.763  5.231   0.32 13.18 ?  153 LEU   A CD2  1 
ATOM   3205 H  H    A LEU   A 1 153 ? 15.248 -9.254  8.836   0.68 15.01 ?  153 LEU   A H    1 
ATOM   3206 H  H    B LEU   A 1 153 ? 15.213 -9.199  8.858   0.32 14.67 ?  153 LEU   A H    1 
ATOM   3207 H  HA   A LEU   A 1 153 ? 16.385 -7.307  7.360   0.68 15.41 ?  153 LEU   A HA   1 
ATOM   3208 H  HA   B LEU   A 1 153 ? 16.359 -7.182  7.495   0.32 14.63 ?  153 LEU   A HA   1 
ATOM   3209 H  HB2  A LEU   A 1 153 ? 14.239 -9.048  6.783   0.68 15.01 ?  153 LEU   A HB2  1 
ATOM   3210 H  HB2  B LEU   A 1 153 ? 14.112 -8.740  6.802   0.32 14.81 ?  153 LEU   A HB2  1 
ATOM   3211 H  HB3  A LEU   A 1 153 ? 14.706 -7.917  5.781   0.68 15.01 ?  153 LEU   A HB3  1 
ATOM   3212 H  HB3  B LEU   A 1 153 ? 14.760 -7.651  5.850   0.32 14.81 ?  153 LEU   A HB3  1 
ATOM   3213 H  HG   A LEU   A 1 153 ? 16.372 -10.085 6.468   0.68 15.09 ?  153 LEU   A HG   1 
ATOM   3214 H  HG   B LEU   A 1 153 ? 16.160 -9.970  6.623   0.32 14.90 ?  153 LEU   A HG   1 
ATOM   3215 H  HD11 A LEU   A 1 153 ? 15.761 -11.169 4.561   0.68 15.71 ?  153 LEU   A HD11 1 
ATOM   3216 H  HD11 B LEU   A 1 153 ? 15.618 -10.910 4.557   0.32 15.00 ?  153 LEU   A HD11 1 
ATOM   3217 H  HD12 A LEU   A 1 153 ? 14.408 -10.790 5.299   0.68 15.71 ?  153 LEU   A HD12 1 
ATOM   3218 H  HD12 B LEU   A 1 153 ? 14.305 -10.662 5.417   0.32 15.00 ?  153 LEU   A HD12 1 
ATOM   3219 H  HD13 A LEU   A 1 153 ? 14.907 -9.923  4.065   0.68 15.71 ?  153 LEU   A HD13 1 
ATOM   3220 H  HD13 B LEU   A 1 153 ? 14.684 -9.664  4.241   0.32 15.00 ?  153 LEU   A HD13 1 
ATOM   3221 H  HD21 A LEU   A 1 153 ? 17.630 -9.437  4.601   0.68 15.72 ?  153 LEU   A HD21 1 
ATOM   3222 H  HD21 B LEU   A 1 153 ? 17.572 -9.466  4.817   0.32 15.81 ?  153 LEU   A HD21 1 
ATOM   3223 H  HD22 A LEU   A 1 153 ? 16.655 -8.201  4.386   0.68 15.72 ?  153 LEU   A HD22 1 
ATOM   3224 H  HD22 B LEU   A 1 153 ? 16.741 -8.137  4.557   0.32 15.81 ?  153 LEU   A HD22 1 
ATOM   3225 H  HD23 A LEU   A 1 153 ? 17.577 -8.271  5.678   0.68 15.72 ?  153 LEU   A HD23 1 
ATOM   3226 H  HD23 B LEU   A 1 153 ? 17.583 -8.299  5.895   0.32 15.81 ?  153 LEU   A HD23 1 
ATOM   3227 N  N    A ALA   A 1 154 ? 14.946 -5.392  7.822   0.68 12.86 ?  154 ALA   A N    1 
ATOM   3228 N  N    B ALA   A 1 154 ? 14.913 -5.265  7.962   0.32 12.43 ?  154 ALA   A N    1 
ATOM   3229 C  CA   A ALA   A 1 154 ? 14.081 -4.243  8.045   0.68 13.23 ?  154 ALA   A CA   1 
ATOM   3230 C  CA   B ALA   A 1 154 ? 14.063 -4.113  8.240   0.32 13.07 ?  154 ALA   A CA   1 
ATOM   3231 C  C    A ALA   A 1 154 ? 13.584 -3.733  6.699   0.68 13.43 ?  154 ALA   A C    1 
ATOM   3232 C  C    B ALA   A 1 154 ? 13.567 -3.572  6.903   0.32 13.22 ?  154 ALA   A C    1 
ATOM   3233 O  O    A ALA   A 1 154 ? 14.389 -3.396  5.821   0.68 13.46 ?  154 ALA   A O    1 
ATOM   3234 O  O    B ALA   A 1 154 ? 14.353 -3.034  6.115   0.32 12.92 ?  154 ALA   A O    1 
ATOM   3235 C  CB   A ALA   A 1 154 ? 14.840 -3.138  8.774   0.68 13.81 ?  154 ALA   A CB   1 
ATOM   3236 C  CB   B ALA   A 1 154 ? 14.841 -3.042  9.001   0.32 13.74 ?  154 ALA   A CB   1 
ATOM   3237 H  H    A ALA   A 1 154 ? 15.735 -5.181  7.555   0.68 15.42 ?  154 ALA   A H    1 
ATOM   3238 H  H    B ALA   A 1 154 ? 15.666 -5.049  7.605   0.32 14.92 ?  154 ALA   A H    1 
ATOM   3239 H  HA   A ALA   A 1 154 ? 13.316 -4.508  8.581   0.68 15.87 ?  154 ALA   A HA   1 
ATOM   3240 H  HA   B ALA   A 1 154 ? 13.299 -4.383  8.773   0.32 15.68 ?  154 ALA   A HA   1 
ATOM   3241 H  HB1  A ALA   A 1 154 ? 14.243 -2.385  8.908   0.68 16.56 ?  154 ALA   A HB1  1 
ATOM   3242 H  HB1  B ALA   A 1 154 ? 14.255 -2.287  9.172   0.32 16.48 ?  154 ALA   A HB1  1 
ATOM   3243 H  HB2  A ALA   A 1 154 ? 15.146 -3.477  9.628   0.68 16.56 ?  154 ALA   A HB2  1 
ATOM   3244 H  HB2  B ALA   A 1 154 ? 15.154 -3.414  9.840   0.32 16.48 ?  154 ALA   A HB2  1 
ATOM   3245 H  HB3  A ALA   A 1 154 ? 15.598 -2.868  8.232   0.68 16.56 ?  154 ALA   A HB3  1 
ATOM   3246 H  HB3  B ALA   A 1 154 ? 15.596 -2.758  8.462   0.32 16.48 ?  154 ALA   A HB3  1 
ATOM   3247 N  N    A VAL   A 1 155 ? 12.264 -3.665  6.549   0.68 14.13 ?  155 VAL   A N    1 
ATOM   3248 N  N    B VAL   A 1 155 ? 12.267 -3.711  6.653   0.32 13.89 ?  155 VAL   A N    1 
ATOM   3249 C  CA   A VAL   A 1 155 ? 11.609 -3.207  5.329   0.68 15.27 ?  155 VAL   A CA   1 
ATOM   3250 C  CA   B VAL   A 1 155 ? 11.640 -3.275  5.410   0.32 14.24 ?  155 VAL   A CA   1 
ATOM   3251 C  C    A VAL   A 1 155 ? 10.845 -1.935  5.681   0.68 16.59 ?  155 VAL   A C    1 
ATOM   3252 C  C    B VAL   A 1 155 ? 10.977 -1.926  5.656   0.32 14.85 ?  155 VAL   A C    1 
ATOM   3253 O  O    A VAL   A 1 155 ? 9.863  -1.986  6.430   0.68 16.66 ?  155 VAL   A O    1 
ATOM   3254 O  O    B VAL   A 1 155 ? 10.166 -1.785  6.580   0.32 14.59 ?  155 VAL   A O    1 
ATOM   3255 C  CB   A VAL   A 1 155 ? 10.678 -4.278  4.744   0.68 15.09 ?  155 VAL   A CB   1 
ATOM   3256 C  CB   B VAL   A 1 155 ? 10.622 -4.316  4.911   0.32 14.16 ?  155 VAL   A CB   1 
ATOM   3257 C  CG1  A VAL   A 1 155 ? 9.945  -3.741  3.527   0.68 16.14 ?  155 VAL   A CG1  1 
ATOM   3258 C  CG1  B VAL   A 1 155 ? 9.969  -3.858  3.613   0.32 14.69 ?  155 VAL   A CG1  1 
ATOM   3259 C  CG2  A VAL   A 1 155 ? 11.477 -5.520  4.373   0.68 15.40 ?  155 VAL   A CG2  1 
ATOM   3260 C  CG2  B VAL   A 1 155 ? 11.299 -5.664  4.716   0.32 14.16 ?  155 VAL   A CG2  1 
ATOM   3261 H  H    A VAL   A 1 155 ? 11.706 -3.890  7.168   0.68 16.95 ?  155 VAL   A H    1 
ATOM   3262 H  H    B VAL   A 1 155 ? 11.713 -4.061  7.209   0.32 16.66 ?  155 VAL   A H    1 
ATOM   3263 H  HA   A VAL   A 1 155 ? 12.279 -2.990  4.666   0.68 18.32 ?  155 VAL   A HA   1 
ATOM   3264 H  HA   B VAL   A 1 155 ? 12.317 -3.165  4.726   0.32 17.08 ?  155 VAL   A HA   1 
ATOM   3265 H  HB   A VAL   A 1 155 ? 10.016 -4.530  5.412   0.68 18.11 ?  155 VAL   A HB   1 
ATOM   3266 H  HB   B VAL   A 1 155 ? 9.923  -4.425  5.578   0.32 16.98 ?  155 VAL   A HB   1 
ATOM   3267 H  HG11 A VAL   A 1 155 ? 9.517  -4.481  3.067   0.68 19.36 ?  155 VAL   A HG11 1 
ATOM   3268 H  HG11 B VAL   A 1 155 ? 9.444  -4.589  3.247   0.32 17.63 ?  155 VAL   A HG11 1 
ATOM   3269 H  HG12 A VAL   A 1 155 ? 9.272  -3.103  3.815   0.68 19.36 ?  155 VAL   A HG12 1 
ATOM   3270 H  HG12 B VAL   A 1 155 ? 9.391  -3.100  3.796   0.32 17.63 ?  155 VAL   A HG12 1 
ATOM   3271 H  HG13 A VAL   A 1 155 ? 10.583 -3.311  2.940   0.68 19.36 ?  155 VAL   A HG13 1 
ATOM   3272 H  HG13 B VAL   A 1 155 ? 10.661 -3.603  2.984   0.32 17.63 ?  155 VAL   A HG13 1 
ATOM   3273 H  HG21 A VAL   A 1 155 ? 10.881 -6.176  3.978   0.68 18.47 ?  155 VAL   A HG21 1 
ATOM   3274 H  HG21 B VAL   A 1 155 ? 10.677 -6.269  4.283   0.32 16.99 ?  155 VAL   A HG21 1 
ATOM   3275 H  HG22 A VAL   A 1 155 ? 12.165 -5.272  3.735   0.68 18.47 ?  155 VAL   A HG22 1 
ATOM   3276 H  HG22 B VAL   A 1 155 ? 12.084 -5.543  4.159   0.32 16.99 ?  155 VAL   A HG22 1 
ATOM   3277 H  HG23 A VAL   A 1 155 ? 11.886 -5.886  5.174   0.68 18.47 ?  155 VAL   A HG23 1 
ATOM   3278 H  HG23 B VAL   A 1 155 ? 11.558 -6.017  5.582   0.32 16.99 ?  155 VAL   A HG23 1 
ATOM   3279 N  N    A PHE   A 1 156 ? 11.303 -0.794  5.150   0.68 17.67 ?  156 PHE   A N    1 
ATOM   3280 N  N    B PHE   A 1 156 ? 11.317 -0.933  4.825   0.32 15.45 ?  156 PHE   A N    1 
ATOM   3281 C  CA   A PHE   A 1 156 ? 10.749 0.505   5.539   0.68 19.31 ?  156 PHE   A CA   1 
ATOM   3282 C  CA   B PHE   A 1 156 ? 10.886 0.443   5.065   0.32 16.31 ?  156 PHE   A CA   1 
ATOM   3283 C  C    A PHE   A 1 156 ? 9.279  0.647   5.151   0.68 19.41 ?  156 PHE   A C    1 
ATOM   3284 C  C    B PHE   A 1 156 ? 9.427  0.684   4.689   0.32 17.87 ?  156 PHE   A C    1 
ATOM   3285 O  O    A PHE   A 1 156 ? 8.473  1.175   5.927   0.68 20.27 ?  156 PHE   A O    1 
ATOM   3286 O  O    B PHE   A 1 156 ? 8.753  1.493   5.338   0.32 18.57 ?  156 PHE   A O    1 
ATOM   3287 C  CB   A PHE   A 1 156 ? 11.585 1.614   4.898   0.68 20.81 ?  156 PHE   A CB   1 
ATOM   3288 C  CB   B PHE   A 1 156 ? 11.791 1.406   4.291   0.32 15.82 ?  156 PHE   A CB   1 
ATOM   3289 C  CG   A PHE   A 1 156 ? 11.112 3.004   5.223   0.68 22.40 ?  156 PHE   A CG   1 
ATOM   3290 C  CG   B PHE   A 1 156 ? 11.529 2.865   4.582   0.32 15.80 ?  156 PHE   A CG   1 
ATOM   3291 C  CD1  A PHE   A 1 156 ? 11.012 3.422   6.538   0.68 23.25 ?  156 PHE   A CD1  1 
ATOM   3292 C  CD1  B PHE   A 1 156 ? 12.076 3.473   5.704   0.32 15.98 ?  156 PHE   A CD1  1 
ATOM   3293 C  CD2  A PHE   A 1 156 ? 10.790 3.899   4.212   0.68 23.69 ?  156 PHE   A CD2  1 
ATOM   3294 C  CD2  B PHE   A 1 156 ? 10.752 3.631   3.727   0.32 16.39 ?  156 PHE   A CD2  1 
ATOM   3295 C  CE1  A PHE   A 1 156 ? 10.584 4.702   6.843   0.68 24.17 ?  156 PHE   A CE1  1 
ATOM   3296 C  CE1  B PHE   A 1 156 ? 11.844 4.814   5.974   0.32 16.33 ?  156 PHE   A CE1  1 
ATOM   3297 C  CE2  A PHE   A 1 156 ? 10.360 5.183   4.509   0.68 24.74 ?  156 PHE   A CE2  1 
ATOM   3298 C  CE2  B PHE   A 1 156 ? 10.516 4.972   3.991   0.32 16.90 ?  156 PHE   A CE2  1 
ATOM   3299 C  CZ   A PHE   A 1 156 ? 10.262 5.586   5.826   0.68 24.83 ?  156 PHE   A CZ   1 
ATOM   3300 C  CZ   B PHE   A 1 156 ? 11.064 5.564   5.117   0.32 16.50 ?  156 PHE   A CZ   1 
ATOM   3301 H  H    A PHE   A 1 156 ? 11.947 -0.748  4.581   0.68 21.20 ?  156 PHE   A H    1 
ATOM   3302 H  H    B PHE   A 1 156 ? 11.801 -1.035  4.121   0.32 18.54 ?  156 PHE   A H    1 
ATOM   3303 H  HA   A PHE   A 1 156 ? 10.817 0.604   6.502   0.68 23.17 ?  156 PHE   A HA   1 
ATOM   3304 H  HA   B PHE   A 1 156 ? 10.987 0.640   6.008   0.32 19.57 ?  156 PHE   A HA   1 
ATOM   3305 H  HB2  A PHE   A 1 156 ? 12.502 1.536   5.207   0.68 24.97 ?  156 PHE   A HB2  1 
ATOM   3306 H  HB2  B PHE   A 1 156 ? 12.714 1.220   4.525   0.32 18.98 ?  156 PHE   A HB2  1 
ATOM   3307 H  HB3  A PHE   A 1 156 ? 11.555 1.510   3.934   0.68 24.97 ?  156 PHE   A HB3  1 
ATOM   3308 H  HB3  B PHE   A 1 156 ? 11.659 1.264   3.340   0.32 18.98 ?  156 PHE   A HB3  1 
ATOM   3309 H  HD1  A PHE   A 1 156 ? 11.230 2.830   7.224   0.68 27.90 ?  156 PHE   A HD1  1 
ATOM   3310 H  HD1  B PHE   A 1 156 ? 12.602 2.969   6.286   0.32 19.17 ?  156 PHE   A HD1  1 
ATOM   3311 H  HD2  A PHE   A 1 156 ? 10.858 3.626   3.324   0.68 28.42 ?  156 PHE   A HD2  1 
ATOM   3312 H  HD2  B PHE   A 1 156 ? 10.381 3.241   2.970   0.32 19.67 ?  156 PHE   A HD2  1 
ATOM   3313 H  HE1  A PHE   A 1 156 ? 10.519 4.969   7.731   0.68 29.00 ?  156 PHE   A HE1  1 
ATOM   3314 H  HE1  B PHE   A 1 156 ? 12.215 5.202   6.735   0.32 19.59 ?  156 PHE   A HE1  1 
ATOM   3315 H  HE2  A PHE   A 1 156 ? 10.146 5.769   3.822   0.68 29.68 ?  156 PHE   A HE2  1 
ATOM   3316 H  HE2  B PHE   A 1 156 ? 9.991  5.476   3.414   0.32 20.27 ?  156 PHE   A HE2  1 
ATOM   3317 H  HZ   A PHE   A 1 156 ? 9.975  6.444   6.031   0.68 29.79 ?  156 PHE   A HZ   1 
ATOM   3318 H  HZ   B PHE   A 1 156 ? 10.907 6.461   5.300   0.32 19.79 ?  156 PHE   A HZ   1 
ATOM   3319 N  N    A ASP   A 1 157 ? 8.914  0.186   3.958   0.68 18.75 ?  157 ASP   A N    1 
ATOM   3320 N  N    B ASP   A 1 157 ? 8.926  0.004   3.662   0.32 18.96 ?  157 ASP   A N    1 
ATOM   3321 C  CA   A ASP   A 1 157 ? 7.601  0.436   3.376   0.68 19.61 ?  157 ASP   A CA   1 
ATOM   3322 C  CA   B ASP   A 1 157 ? 7.615  0.284   3.091   0.32 19.78 ?  157 ASP   A CA   1 
ATOM   3323 C  C    A ASP   A 1 157 ? 6.613  -0.630  3.846   0.68 19.49 ?  157 ASP   A C    1 
ATOM   3324 C  C    B ASP   A 1 157 ? 6.586  -0.709  3.621   0.32 19.93 ?  157 ASP   A C    1 
ATOM   3325 O  O    A ASP   A 1 157 ? 6.799  -1.821  3.568   0.68 18.63 ?  157 ASP   A O    1 
ATOM   3326 O  O    B ASP   A 1 157 ? 6.780  -1.926  3.523   0.32 19.74 ?  157 ASP   A O    1 
ATOM   3327 C  CB   A ASP   A 1 157 ? 7.735  0.398   1.857   0.68 21.01 ?  157 ASP   A CB   1 
ATOM   3328 C  CB   B ASP   A 1 157 ? 7.685  0.191   1.568   0.32 20.53 ?  157 ASP   A CB   1 
ATOM   3329 C  CG   A ASP   A 1 157 ? 6.532  0.934   1.153   0.68 23.15 ?  157 ASP   A CG   1 
ATOM   3330 C  CG   B ASP   A 1 157 ? 6.412  0.673   0.895   0.32 21.72 ?  157 ASP   A CG   1 
ATOM   3331 O  OD1  A ASP   A 1 157 ? 6.515  2.146   0.860   0.68 25.40 ?  157 ASP   A OD1  1 
ATOM   3332 O  OD1  B ASP   A 1 157 ? 6.065  1.865   1.042   0.32 22.76 ?  157 ASP   A OD1  1 
ATOM   3333 O  OD2  A ASP   A 1 157 ? 5.606  0.144   0.884   0.68 22.67 -1 157 ASP   A OD2  1 
ATOM   3334 O  OD2  B ASP   A 1 157 ? 5.751  -0.145  0.222   0.32 21.65 -1 157 ASP   A OD2  1 
ATOM   3335 H  H    A ASP   A 1 157 ? 9.430  -0.289  3.454   0.68 22.49 ?  157 ASP   A H    1 
ATOM   3336 H  H    B ASP   A 1 157 ? 9.339  -0.640  3.269   0.32 22.74 ?  157 ASP   A H    1 
ATOM   3337 H  HA   A ASP   A 1 157 ? 7.282  1.306   3.652   0.68 23.53 ?  157 ASP   A HA   1 
ATOM   3338 H  HA   B ASP   A 1 157 ? 7.340  1.183   3.337   0.32 23.74 ?  157 ASP   A HA   1 
ATOM   3339 H  HB2  A ASP   A 1 157 ? 8.491  0.939   1.595   0.68 25.21 ?  157 ASP   A HB2  1 
ATOM   3340 H  HB2  B ASP   A 1 157 ? 8.449  0.710   1.258   0.32 24.63 ?  157 ASP   A HB2  1 
ATOM   3341 H  HB3  A ASP   A 1 157 ? 7.859  -0.516  1.573   0.68 25.21 ?  157 ASP   A HB3  1 
ATOM   3342 H  HB3  B ASP   A 1 157 ? 7.802  -0.739  1.319   0.32 24.63 ?  157 ASP   A HB3  1 
ATOM   3343 N  N    A LYS   A 1 158 ? 5.559  -0.198  4.547   0.68 20.86 ?  158 LYS   A N    1 
ATOM   3344 N  N    B LYS   A 1 158 ? 5.485  -0.183  4.164   0.32 20.44 ?  158 LYS   A N    1 
ATOM   3345 C  CA   A LYS   A 1 158 ? 4.602  -1.149  5.106   0.68 21.87 ?  158 LYS   A CA   1 
ATOM   3346 C  CA   B LYS   A 1 158 ? 4.460  -1.036  4.762   0.32 21.29 ?  158 LYS   A CA   1 
ATOM   3347 C  C    A LYS   A 1 158 ? 3.879  -1.917  4.005   0.68 21.60 ?  158 LYS   A C    1 
ATOM   3348 C  C    B LYS   A 1 158 ? 3.769  -1.905  3.716   0.32 20.91 ?  158 LYS   A C    1 
ATOM   3349 O  O    A LYS   A 1 158 ? 3.695  -3.137  4.104   0.68 21.89 ?  158 LYS   A O    1 
ATOM   3350 O  O    B LYS   A 1 158 ? 3.519  -3.093  3.954   0.32 20.62 ?  158 LYS   A O    1 
ATOM   3351 C  CB   A LYS   A 1 158 ? 3.611  -0.416  6.016   0.68 23.12 ?  158 LYS   A CB   1 
ATOM   3352 C  CB   B LYS   A 1 158 ? 3.453  -0.163  5.517   0.32 22.59 ?  158 LYS   A CB   1 
ATOM   3353 C  CG   A LYS   A 1 158 ? 2.416  -1.245  6.466   0.68 24.56 ?  158 LYS   A CG   1 
ATOM   3354 C  CG   B LYS   A 1 158 ? 2.046  -0.727  5.641   0.32 23.94 ?  158 LYS   A CG   1 
ATOM   3355 C  CD   A LYS   A 1 158 ? 2.823  -2.485  7.254   0.68 25.64 ?  158 LYS   A CD   1 
ATOM   3356 C  CD   B LYS   A 1 158 ? 1.238  0.086   6.647   0.32 25.02 ?  158 LYS   A CD   1 
ATOM   3357 C  CE   A LYS   A 1 158 ? 1.607  -3.096  7.939   0.68 26.20 ?  158 LYS   A CE   1 
ATOM   3358 C  CE   B LYS   A 1 158 ? -0.166 0.388   6.150   0.32 25.82 ?  158 LYS   A CE   1 
ATOM   3359 N  NZ   A LYS   A 1 158 ? 1.791  -4.518  8.338   0.68 26.33 ?  158 LYS   A NZ   1 
ATOM   3360 N  NZ   B LYS   A 1 158 ? -0.895 1.296   7.080   0.32 26.39 ?  158 LYS   A NZ   1 
ATOM   3361 H  H    A LYS   A 1 158 ? 5.384  0.627   4.712   0.68 25.02 ?  158 LYS   A H    1 
ATOM   3362 H  H    B LYS   A 1 158 ? 5.315  0.660   4.204   0.32 24.52 ?  158 LYS   A H    1 
ATOM   3363 H  HA   A LYS   A 1 158 ? 5.079  -1.790  5.657   0.68 26.23 ?  158 LYS   A HA   1 
ATOM   3364 H  HA   B LYS   A 1 158 ? 4.881  -1.623  5.409   0.32 25.54 ?  158 LYS   A HA   1 
ATOM   3365 H  HB2  A LYS   A 1 158 ? 4.078  -0.123  6.818   0.68 27.74 ?  158 LYS   A HB2  1 
ATOM   3366 H  HB2  B LYS   A 1 158 ? 3.785  -0.021  6.419   0.32 27.10 ?  158 LYS   A HB2  1 
ATOM   3367 H  HB3  A LYS   A 1 158 ? 3.267  0.359   5.544   0.68 27.74 ?  158 LYS   A HB3  1 
ATOM   3368 H  HB3  B LYS   A 1 158 ? 3.381  0.690   5.063   0.32 27.10 ?  158 LYS   A HB3  1 
ATOM   3369 H  HG2  A LYS   A 1 158 ? 1.855  -0.701  7.042   0.68 29.47 ?  158 LYS   A HG2  1 
ATOM   3370 H  HG2  B LYS   A 1 158 ? 1.598  -0.677  4.781   0.32 28.73 ?  158 LYS   A HG2  1 
ATOM   3371 H  HG3  A LYS   A 1 158 ? 1.907  -1.530  5.691   0.68 29.47 ?  158 LYS   A HG3  1 
ATOM   3372 H  HG3  B LYS   A 1 158 ? 2.087  -1.644  5.950   0.32 28.73 ?  158 LYS   A HG3  1 
ATOM   3373 H  HD2  A LYS   A 1 158 ? 3.195  -3.146  6.651   0.68 30.77 ?  158 LYS   A HD2  1 
ATOM   3374 H  HD2  B LYS   A 1 158 ? 1.164  -0.415  7.475   0.32 30.01 ?  158 LYS   A HD2  1 
ATOM   3375 H  HD3  A LYS   A 1 158 ? 3.473  -2.239  7.932   0.68 30.77 ?  158 LYS   A HD3  1 
ATOM   3376 H  HD3  B LYS   A 1 158 ? 1.689  0.931   6.809   0.32 30.01 ?  158 LYS   A HD3  1 
ATOM   3377 H  HE2  A LYS   A 1 158 ? 1.401  -2.589  8.736   0.68 31.43 ?  158 LYS   A HE2  1 
ATOM   3378 H  HE2  B LYS   A 1 158 ? -0.113 0.822   5.284   0.32 30.98 ?  158 LYS   A HE2  1 
ATOM   3379 H  HE3  A LYS   A 1 158 ? 0.857  -3.052  7.335   0.68 31.43 ?  158 LYS   A HE3  1 
ATOM   3380 H  HE3  B LYS   A 1 158 ? -0.667 -0.439  6.081   0.32 30.98 ?  158 LYS   A HE3  1 
ATOM   3381 H  HZ1  A LYS   A 1 158 ? 1.055  -4.822  8.737   0.68 31.59 ?  158 LYS   A HZ1  1 
ATOM   3382 H  HZ1  B LYS   A 1 158 ? -1.713 1.459   6.770   0.32 31.66 ?  158 LYS   A HZ1  1 
ATOM   3383 H  HZ2  A LYS   A 1 158 ? 1.953  -5.013  7.616   0.68 31.59 ?  158 LYS   A HZ2  1 
ATOM   3384 H  HZ2  B LYS   A 1 158 ? -0.961 0.920   7.884   0.32 31.66 ?  158 LYS   A HZ2  1 
ATOM   3385 H  HZ3  A LYS   A 1 158 ? 2.477  -4.595  8.900   0.68 31.59 ?  158 LYS   A HZ3  1 
ATOM   3386 H  HZ3  B LYS   A 1 158 ? -0.457 2.068   7.159   0.32 31.66 ?  158 LYS   A HZ3  1 
ATOM   3387 N  N    A ASN   A 1 159 ? 3.463  -1.225  2.943   0.68 22.25 ?  159 ASN   A N    1 
ATOM   3388 N  N    B ASN   A 1 159 ? 3.453  -1.336  2.551   0.32 21.22 ?  159 ASN   A N    1 
ATOM   3389 C  CA   A ASN   A 1 159 ? 2.809  -1.921  1.841   0.68 22.78 ?  159 ASN   A CA   1 
ATOM   3390 C  CA   B ASN   A 1 159 ? 2.737  -2.097  1.532   0.32 21.46 ?  159 ASN   A CA   1 
ATOM   3391 C  C    A ASN   A 1 159 ? 3.726  -2.985  1.243   0.68 21.31 ?  159 ASN   A C    1 
ATOM   3392 C  C    B ASN   A 1 159 ? 3.621  -3.178  0.911   0.32 19.72 ?  159 ASN   A C    1 
ATOM   3393 O  O    A ASN   A 1 159 ? 3.288  -4.107  0.960   0.68 20.80 ?  159 ASN   A O    1 
ATOM   3394 O  O    B ASN   A 1 159 ? 3.154  -4.294  0.653   0.32 19.96 ?  159 ASN   A O    1 
ATOM   3395 C  CB   A ASN   A 1 159 ? 2.340  -0.913  0.789   0.68 25.40 ?  159 ASN   A CB   1 
ATOM   3396 C  CB   B ASN   A 1 159 ? 2.171  -1.143  0.477   0.32 23.70 ?  159 ASN   A CB   1 
ATOM   3397 C  CG   A ASN   A 1 159 ? 1.135  -0.114  1.250   0.68 29.13 ?  159 ASN   A CG   1 
ATOM   3398 C  CG   B ASN   A 1 159 ? 1.126  -0.197  1.050   0.32 26.06 ?  159 ASN   A CG   1 
ATOM   3399 O  OD1  A ASN   A 1 159 ? 0.283  -0.630  1.972   0.68 30.72 ?  159 ASN   A OD1  1 
ATOM   3400 O  OD1  B ASN   A 1 159 ? 0.267  -0.610  1.829   0.32 26.94 ?  159 ASN   A OD1  1 
ATOM   3401 N  ND2  A ASN   A 1 159 ? 1.057  1.148   0.839   0.68 30.83 ?  159 ASN   A ND2  1 
ATOM   3402 N  ND2  B ASN   A 1 159 ? 1.199  1.078   0.675   0.32 27.15 ?  159 ASN   A ND2  1 
ATOM   3403 H  H    A ASN   A 1 159 ? 3.551  -0.376  2.843   0.68 26.70 ?  159 ASN   A H    1 
ATOM   3404 H  H    B ASN   A 1 159 ? 3.631  -0.525  2.338   0.32 25.46 ?  159 ASN   A H    1 
ATOM   3405 H  HA   A ASN   A 1 159 ? 2.024  -2.372  2.188   0.68 27.33 ?  159 ASN   A HA   1 
ATOM   3406 H  HA   B ASN   A 1 159 ? 1.986  -2.543  1.952   0.32 25.75 ?  159 ASN   A HA   1 
ATOM   3407 H  HB2  A ASN   A 1 159 ? 3.058  -0.291  0.603   0.68 30.47 ?  159 ASN   A HB2  1 
ATOM   3408 H  HB2  B ASN   A 1 159 ? 2.889  -0.604  0.114   0.32 28.44 ?  159 ASN   A HB2  1 
ATOM   3409 H  HB3  A ASN   A 1 159 ? 2.091  -1.392  -0.015  0.68 30.47 ?  159 ASN   A HB3  1 
ATOM   3410 H  HB3  B ASN   A 1 159 ? 1.748  -1.659  -0.226  0.32 28.44 ?  159 ASN   A HB3  1 
ATOM   3411 H  HD21 A ASN   A 1 159 ? 0.398  1.638   1.073   0.68 36.99 ?  159 ASN   A HD21 1 
ATOM   3412 H  HD21 B ASN   A 1 159 ? 0.630  1.652   0.975   0.32 32.57 ?  159 ASN   A HD21 1 
ATOM   3413 H  HD22 A ASN   A 1 159 ? 1.672  1.476   0.341   0.68 36.99 ?  159 ASN   A HD22 1 
ATOM   3414 H  HD22 B ASN   A 1 159 ? 1.815  1.330   0.133   0.32 32.57 ?  159 ASN   A HD22 1 
ATOM   3415 N  N    A LEU   A 1 160 ? 5.010  -2.666  1.078   0.68 19.84 ?  160 LEU   A N    1 
ATOM   3416 N  N    B LEU   A 1 160 ? 4.902  -2.876  0.679   0.32 17.95 ?  160 LEU   A N    1 
ATOM   3417 C  CA   A LEU   A 1 160 ? 5.945  -3.661  0.561   0.68 18.87 ?  160 LEU   A CA   1 
ATOM   3418 C  CA   B LEU   A 1 160 ? 5.811  -3.886  0.138   0.32 16.83 ?  160 LEU   A CA   1 
ATOM   3419 C  C    A LEU   A 1 160 ? 6.142  -4.798  1.554   0.68 17.58 ?  160 LEU   A C    1 
ATOM   3420 C  C    B LEU   A 1 160 ? 6.096  -4.980  1.162   0.32 16.32 ?  160 LEU   A C    1 
ATOM   3421 O  O    A LEU   A 1 160 ? 6.191  -5.971  1.162   0.68 18.64 ?  160 LEU   A O    1 
ATOM   3422 O  O    B LEU   A 1 160 ? 6.205  -6.159  0.804   0.32 16.55 ?  160 LEU   A O    1 
ATOM   3423 C  CB   A LEU   A 1 160 ? 7.281  -3.006  0.222   0.68 18.82 ?  160 LEU   A CB   1 
ATOM   3424 C  CB   B LEU   A 1 160 ? 7.110  -3.229  -0.332  0.32 16.36 ?  160 LEU   A CB   1 
ATOM   3425 C  CG   A LEU   A 1 160 ? 8.354  -4.005  -0.214  0.68 19.29 ?  160 LEU   A CG   1 
ATOM   3426 C  CG   B LEU   A 1 160 ? 7.005  -2.392  -1.611  0.32 16.46 ?  160 LEU   A CG   1 
ATOM   3427 C  CD1  A LEU   A 1 160 ? 7.896  -4.769  -1.442  0.68 19.71 ?  160 LEU   A CD1  1 
ATOM   3428 C  CD1  B LEU   A 1 160 ? 8.283  -1.609  -1.868  0.32 16.52 ?  160 LEU   A CD1  1 
ATOM   3429 C  CD2  A LEU   A 1 160 ? 9.670  -3.302  -0.481  0.68 19.63 ?  160 LEU   A CD2  1 
ATOM   3430 C  CD2  B LEU   A 1 160 ? 6.678  -3.290  -2.796  0.32 16.70 ?  160 LEU   A CD2  1 
ATOM   3431 H  H    A LEU   A 1 160 ? 5.358  -1.900  1.264   0.68 23.81 ?  160 LEU   A H    1 
ATOM   3432 H  H    B LEU   A 1 160 ? 5.261  -2.109  0.823   0.32 21.53 ?  160 LEU   A H    1 
ATOM   3433 H  HA   A LEU   A 1 160 ? 5.578  -4.031  -0.252  0.68 22.64 ?  160 LEU   A HA   1 
ATOM   3434 H  HA   B LEU   A 1 160 ? 5.393  -4.300  -0.631  0.32 20.19 ?  160 LEU   A HA   1 
ATOM   3435 H  HB2  A LEU   A 1 160 ? 7.149  -2.365  -0.500  0.68 22.57 ?  160 LEU   A HB2  1 
ATOM   3436 H  HB2  B LEU   A 1 160 ? 7.434  -2.646  0.372   0.32 19.62 ?  160 LEU   A HB2  1 
ATOM   3437 H  HB3  A LEU   A 1 160 ? 7.613  -2.547  1.010   0.68 22.57 ?  160 LEU   A HB3  1 
ATOM   3438 H  HB3  B LEU   A 1 160 ? 7.764  -3.926  -0.497  0.32 19.62 ?  160 LEU   A HB3  1 
ATOM   3439 H  HG   A LEU   A 1 160 ? 8.504  -4.643  0.497   0.68 23.14 ?  160 LEU   A HG   1 
ATOM   3440 H  HG   B LEU   A 1 160 ? 6.285  -1.754  -1.509  0.32 19.75 ?  160 LEU   A HG   1 
ATOM   3441 H  HD11 A LEU   A 1 160 ? 8.636  -5.296  -1.775  0.68 23.65 ?  160 LEU   A HD11 1 
ATOM   3442 H  HD11 B LEU   A 1 160 ? 8.175  -1.081  -2.675  0.32 19.82 ?  160 LEU   A HD11 1 
ATOM   3443 H  HD12 A LEU   A 1 160 ? 7.159  -5.352  -1.197  0.68 23.65 ?  160 LEU   A HD12 1 
ATOM   3444 H  HD12 B LEU   A 1 160 ? 8.455  -1.025  -1.112  0.32 19.82 ?  160 LEU   A HD12 1 
ATOM   3445 H  HD13 A LEU   A 1 160 ? 7.606  -4.136  -2.118  0.68 23.65 ?  160 LEU   A HD13 1 
ATOM   3446 H  HD13 B LEU   A 1 160 ? 9.020  -2.231  -1.977  0.32 19.82 ?  160 LEU   A HD13 1 
ATOM   3447 H  HD21 A LEU   A 1 160 ? 10.329 -3.961  -0.753  0.68 23.55 ?  160 LEU   A HD21 1 
ATOM   3448 H  HD21 B LEU   A 1 160 ? 6.792  -2.785  -3.615  0.32 20.03 ?  160 LEU   A HD21 1 
ATOM   3449 H  HD22 A LEU   A 1 160 ? 9.544  -2.650  -1.189  0.68 23.55 ?  160 LEU   A HD22 1 
ATOM   3450 H  HD22 B LEU   A 1 160 ? 7.283  -4.050  -2.790  0.32 20.03 ?  160 LEU   A HD22 1 
ATOM   3451 H  HD23 A LEU   A 1 160 ? 9.962  -2.858  0.330   0.68 23.55 ?  160 LEU   A HD23 1 
ATOM   3452 H  HD23 B LEU   A 1 160 ? 5.763  -3.597  -2.718  0.32 20.03 ?  160 LEU   A HD23 1 
ATOM   3453 N  N    A TYR   A 1 161 ? 6.260  -4.474  2.842   0.68 16.91 ?  161 TYR   A N    1 
ATOM   3454 N  N    B TYR   A 1 161 ? 6.223  -4.609  2.438   0.32 15.95 ?  161 TYR   A N    1 
ATOM   3455 C  CA   A TYR   A 1 161 ? 6.400  -5.516  3.852   0.68 16.92 ?  161 TYR   A CA   1 
ATOM   3456 C  CA   B TYR   A 1 161 ? 6.371  -5.606  3.494   0.32 15.97 ?  161 TYR   A CA   1 
ATOM   3457 C  C    A TYR   A 1 161 ? 5.264  -6.531  3.761   0.68 17.40 ?  161 TYR   A C    1 
ATOM   3458 C  C    B TYR   A 1 161 ? 5.209  -6.592  3.477   0.32 16.28 ?  161 TYR   A C    1 
ATOM   3459 O  O    A TYR   A 1 161 ? 5.490  -7.745  3.806   0.68 17.30 ?  161 TYR   A O    1 
ATOM   3460 O  O    B TYR   A 1 161 ? 5.413  -7.811  3.444   0.32 15.44 ?  161 TYR   A O    1 
ATOM   3461 C  CB   A TYR   A 1 161 ? 6.458  -4.893  5.246   0.68 17.39 ?  161 TYR   A CB   1 
ATOM   3462 C  CB   B TYR   A 1 161 ? 6.474  -4.907  4.853   0.32 15.95 ?  161 TYR   A CB   1 
ATOM   3463 C  CG   A TYR   A 1 161 ? 6.375  -5.934  6.326   0.68 17.14 ?  161 TYR   A CG   1 
ATOM   3464 C  CG   B TYR   A 1 161 ? 6.384  -5.833  6.049   0.32 15.96 ?  161 TYR   A CG   1 
ATOM   3465 C  CD1  A TYR   A 1 161 ? 7.505  -6.624  6.730   0.68 16.94 ?  161 TYR   A CD1  1 
ATOM   3466 C  CD1  B TYR   A 1 161 ? 7.511  -6.478  6.541   0.32 16.07 ?  161 TYR   A CD1  1 
ATOM   3467 C  CD2  A TYR   A 1 161 ? 5.162  -6.248  6.923   0.68 17.31 ?  161 TYR   A CD2  1 
ATOM   3468 C  CD2  B TYR   A 1 161 ? 5.172  -6.050  6.697   0.32 16.07 ?  161 TYR   A CD2  1 
ATOM   3469 C  CE1  A TYR   A 1 161 ? 7.434  -7.596  7.703   0.68 17.48 ?  161 TYR   A CE1  1 
ATOM   3470 C  CE1  B TYR   A 1 161 ? 7.435  -7.322  7.636   0.32 16.40 ?  161 TYR   A CE1  1 
ATOM   3471 C  CE2  A TYR   A 1 161 ? 5.081  -7.215  7.898   0.68 17.32 ?  161 TYR   A CE2  1 
ATOM   3472 C  CE2  B TYR   A 1 161 ? 5.086  -6.895  7.793   0.32 16.25 ?  161 TYR   A CE2  1 
ATOM   3473 C  CZ   A TYR   A 1 161 ? 6.220  -7.886  8.285   0.68 17.78 ?  161 TYR   A CZ   1 
ATOM   3474 C  CZ   B TYR   A 1 161 ? 6.221  -7.527  8.257   0.32 16.80 ?  161 TYR   A CZ   1 
ATOM   3475 O  OH   A TYR   A 1 161 ? 6.153  -8.852  9.258   0.68 18.84 ?  161 TYR   A OH   1 
ATOM   3476 O  OH   B TYR   A 1 161 ? 6.144  -8.364  9.346   0.32 17.75 ?  161 TYR   A OH   1 
ATOM   3477 H  H    A TYR   A 1 161 ? 6.252  -3.668  3.150   0.68 20.29 ?  161 TYR   A H    1 
ATOM   3478 H  H    B TYR   A 1 161 ? 6.221  -3.797  2.710   0.32 19.14 ?  161 TYR   A H    1 
ATOM   3479 H  HA   A TYR   A 1 161 ? 7.226  -5.985  3.701   0.68 20.30 ?  161 TYR   A HA   1 
ATOM   3480 H  HA   B TYR   A 1 161 ? 7.189  -6.104  3.349   0.32 19.16 ?  161 TYR   A HA   1 
ATOM   3481 H  HB2  A TYR   A 1 161 ? 7.296  -4.417  5.346   0.68 20.86 ?  161 TYR   A HB2  1 
ATOM   3482 H  HB2  B TYR   A 1 161 ? 7.328  -4.450  4.900   0.32 19.13 ?  161 TYR   A HB2  1 
ATOM   3483 H  HB3  A TYR   A 1 161 ? 5.711  -4.281  5.357   0.68 20.86 ?  161 TYR   A HB3  1 
ATOM   3484 H  HB3  B TYR   A 1 161 ? 5.754  -4.261  4.925   0.32 19.13 ?  161 TYR   A HB3  1 
ATOM   3485 H  HD1  A TYR   A 1 161 ? 8.326  -6.428  6.333   0.68 20.33 ?  161 TYR   A HD1  1 
ATOM   3486 H  HD1  B TYR   A 1 161 ? 8.331  -6.343  6.124   0.32 19.28 ?  161 TYR   A HD1  1 
ATOM   3487 H  HD2  A TYR   A 1 161 ? 4.389  -5.798  6.659   0.68 20.76 ?  161 TYR   A HD2  1 
ATOM   3488 H  HD2  B TYR   A 1 161 ? 4.403  -5.628  6.388   0.32 19.27 ?  161 TYR   A HD2  1 
ATOM   3489 H  HE1  A TYR   A 1 161 ? 8.201  -8.049  7.967   0.68 20.97 ?  161 TYR   A HE1  1 
ATOM   3490 H  HE1  B TYR   A 1 161 ? 8.199  -7.750  7.954   0.32 19.68 ?  161 TYR   A HE1  1 
ATOM   3491 H  HE2  A TYR   A 1 161 ? 4.257  -7.413  8.289   0.68 20.78 ?  161 TYR   A HE2  1 
ATOM   3492 H  HE2  B TYR   A 1 161 ? 4.266  -7.034  8.216   0.32 19.50 ?  161 TYR   A HE2  1 
ATOM   3493 H  HH   A TYR   A 1 161 ? 5.353  -8.931  9.523   0.68 22.60 ?  161 TYR   A HH   1 
ATOM   3494 H  HH   B TYR   A 1 161 ? 6.898  -8.683  9.527   0.32 21.29 ?  161 TYR   A HH   1 
ATOM   3495 N  N    A ASP   A 1 162 ? 4.026  -6.050  3.634   0.68 18.21 ?  162 ASP   A N    1 
ATOM   3496 N  N    B ASP   A 1 162 ? 3.976  -6.079  3.492   0.32 17.48 ?  162 ASP   A N    1 
ATOM   3497 C  CA   A ASP   A 1 162 ? 2.884  -6.963  3.602   0.68 18.92 ?  162 ASP   A CA   1 
ATOM   3498 C  CA   B ASP   A 1 162 ? 2.809  -6.953  3.412   0.32 18.47 ?  162 ASP   A CA   1 
ATOM   3499 C  C    A ASP   A 1 162 ? 2.920  -7.853  2.364   0.68 18.72 ?  162 ASP   A C    1 
ATOM   3500 C  C    B ASP   A 1 162 ? 2.867  -7.826  2.164   0.32 18.72 ?  162 ASP   A C    1 
ATOM   3501 O  O    A ASP   A 1 162 ? 2.571  -9.038  2.433   0.68 19.37 ?  162 ASP   A O    1 
ATOM   3502 O  O    B ASP   A 1 162 ? 2.479  -8.999  2.195   0.32 18.78 ?  162 ASP   A O    1 
ATOM   3503 C  CB   A ASP   A 1 162 ? 1.566  -6.181  3.661   0.68 20.36 ?  162 ASP   A CB   1 
ATOM   3504 C  CB   B ASP   A 1 162 ? 1.525  -6.118  3.414   0.32 19.49 ?  162 ASP   A CB   1 
ATOM   3505 C  CG   A ASP   A 1 162 ? 1.265  -5.619  5.041   0.68 22.31 ?  162 ASP   A CG   1 
ATOM   3506 C  CG   B ASP   A 1 162 ? 1.193  -5.540  4.778   0.32 20.54 ?  162 ASP   A CG   1 
ATOM   3507 O  OD1  A ASP   A 1 162 ? 1.909  -6.025  6.027   0.68 23.04 ?  162 ASP   A OD1  1 
ATOM   3508 O  OD1  B ASP   A 1 162 ? 1.854  -5.903  5.771   0.32 20.82 ?  162 ASP   A OD1  1 
ATOM   3509 O  OD2  A ASP   A 1 162 ? 0.353  -4.768  5.136   0.68 23.87 -1 162 ASP   A OD2  1 
ATOM   3510 O  OD2  B ASP   A 1 162 ? 0.252  -4.721  4.853   0.32 21.23 -1 162 ASP   A OD2  1 
ATOM   3511 H  H    A ASP   A 1 162 ? 3.816  -5.218  3.565   0.68 21.85 ?  162 ASP   A H    1 
ATOM   3512 H  H    B ASP   A 1 162 ? 3.793  -5.242  3.544   0.32 20.97 ?  162 ASP   A H    1 
ATOM   3513 H  HA   A ASP   A 1 162 ? 2.915  -7.542  4.378   0.68 22.70 ?  162 ASP   A HA   1 
ATOM   3514 H  HA   B ASP   A 1 162 ? 2.791  -7.537  4.185   0.32 22.15 ?  162 ASP   A HA   1 
ATOM   3515 H  HB2  A ASP   A 1 162 ? 1.605  -5.435  3.047   0.68 24.43 ?  162 ASP   A HB2  1 
ATOM   3516 H  HB2  B ASP   A 1 162 ? 1.624  -5.376  2.799   0.32 23.38 ?  162 ASP   A HB2  1 
ATOM   3517 H  HB3  A ASP   A 1 162 ? 0.829  -6.769  3.428   0.68 24.43 ?  162 ASP   A HB3  1 
ATOM   3518 H  HB3  B ASP   A 1 162 ? 0.779  -6.675  3.148   0.32 23.38 ?  162 ASP   A HB3  1 
ATOM   3519 N  N    A LYS   A 1 163 ? 3.338  -7.303  1.223   0.68 19.69 ?  163 LYS   A N    1 
ATOM   3520 N  N    B LYS   A 1 163 ? 3.347  -7.265  1.053   0.32 19.59 ?  163 LYS   A N    1 
ATOM   3521 C  CA   A LYS   A 1 163 ? 3.411  -8.098  0.000   0.68 20.08 ?  163 LYS   A CA   1 
ATOM   3522 C  CA   B LYS   A 1 163 ? 3.485  -8.041  -0.175  0.32 20.11 ?  163 LYS   A CA   1 
ATOM   3523 C  C    A LYS   A 1 163 ? 4.511  -9.150  0.089   0.68 19.60 ?  163 LYS   A C    1 
ATOM   3524 C  C    B LYS   A 1 163 ? 4.568  -9.106  -0.036  0.32 19.17 ?  163 LYS   A C    1 
ATOM   3525 O  O    A LYS   A 1 163 ? 4.334  -10.287 -0.363  0.68 20.60 ?  163 LYS   A O    1 
ATOM   3526 O  O    B LYS   A 1 163 ? 4.430  -10.214 -0.568  0.32 19.53 ?  163 LYS   A O    1 
ATOM   3527 C  CB   A LYS   A 1 163 ? 3.628  -7.174  -1.199  0.68 22.99 ?  163 LYS   A CB   1 
ATOM   3528 C  CB   B LYS   A 1 163 ? 3.807  -7.093  -1.329  0.32 22.37 ?  163 LYS   A CB   1 
ATOM   3529 C  CG   A LYS   A 1 163 ? 3.710  -7.885  -2.537  0.68 25.76 ?  163 LYS   A CG   1 
ATOM   3530 C  CG   B LYS   A 1 163 ? 3.875  -7.741  -2.695  0.32 24.55 ?  163 LYS   A CG   1 
ATOM   3531 C  CD   A LYS   A 1 163 ? 4.060  -6.907  -3.646  0.68 28.99 ?  163 LYS   A CD   1 
ATOM   3532 C  CD   B LYS   A 1 163 ? 4.346  -6.728  -3.725  0.32 26.71 ?  163 LYS   A CD   1 
ATOM   3533 C  CE   A LYS   A 1 163 ? 4.003  -7.569  -5.013  0.68 31.48 ?  163 LYS   A CE   1 
ATOM   3534 C  CE   B LYS   A 1 163 ? 4.307  -7.289  -5.134  0.32 28.37 ?  163 LYS   A CE   1 
ATOM   3535 N  NZ   A LYS   A 1 163 ? 4.678  -6.746  -6.054  0.68 32.43 ?  163 LYS   A NZ   1 
ATOM   3536 N  NZ   B LYS   A 1 163 ? 5.041  -6.412  -6.087  0.32 29.17 ?  163 LYS   A NZ   1 
ATOM   3537 H  H    A LYS   A 1 163 ? 3.586  -6.483  1.135   0.68 23.63 ?  163 LYS   A H    1 
ATOM   3538 H  H    B LYS   A 1 163 ? 3.591  -6.443  0.986   0.32 23.50 ?  163 LYS   A H    1 
ATOM   3539 H  HA   A LYS   A 1 163 ? 2.567  -8.556  -0.127  0.68 24.10 ?  163 LYS   A HA   1 
ATOM   3540 H  HA   B LYS   A 1 163 ? 2.643  -8.482  -0.369  0.32 24.13 ?  163 LYS   A HA   1 
ATOM   3541 H  HB2  A LYS   A 1 163 ? 2.885  -6.546  -1.248  0.68 27.58 ?  163 LYS   A HB2  1 
ATOM   3542 H  HB2  B LYS   A 1 163 ? 3.121  -6.407  -1.366  0.32 26.84 ?  163 LYS   A HB2  1 
ATOM   3543 H  HB3  A LYS   A 1 163 ? 4.455  -6.685  -1.074  0.68 27.58 ?  163 LYS   A HB3  1 
ATOM   3544 H  HB3  B LYS   A 1 163 ? 4.668  -6.682  -1.159  0.32 26.84 ?  163 LYS   A HB3  1 
ATOM   3545 H  HG2  A LYS   A 1 163 ? 4.402  -8.563  -2.503  0.68 30.90 ?  163 LYS   A HG2  1 
ATOM   3546 H  HG2  B LYS   A 1 163 ? 4.506  -8.478  -2.676  0.32 29.45 ?  163 LYS   A HG2  1 
ATOM   3547 H  HG3  A LYS   A 1 163 ? 2.852  -8.288  -2.742  0.68 30.90 ?  163 LYS   A HG3  1 
ATOM   3548 H  HG3  B LYS   A 1 163 ? 2.992  -8.055  -2.949  0.32 29.45 ?  163 LYS   A HG3  1 
ATOM   3549 H  HD2  A LYS   A 1 163 ? 3.425  -6.173  -3.638  0.68 34.78 ?  163 LYS   A HD2  1 
ATOM   3550 H  HD2  B LYS   A 1 163 ? 3.766  -5.950  -3.693  0.32 32.05 ?  163 LYS   A HD2  1 
ATOM   3551 H  HD3  A LYS   A 1 163 ? 4.960  -6.573  -3.507  0.68 34.78 ?  163 LYS   A HD3  1 
ATOM   3552 H  HD3  B LYS   A 1 163 ? 5.259  -6.472  -3.524  0.32 32.05 ?  163 LYS   A HD3  1 
ATOM   3553 H  HE2  A LYS   A 1 163 ? 4.446  -8.430  -4.970  0.68 37.77 ?  163 LYS   A HE2  1 
ATOM   3554 H  HE2  B LYS   A 1 163 ? 4.714  -8.168  -5.142  0.32 34.03 ?  163 LYS   A HE2  1 
ATOM   3555 H  HE3  A LYS   A 1 163 ? 3.076  -7.683  -5.272  0.68 37.77 ?  163 LYS   A HE3  1 
ATOM   3556 H  HE3  B LYS   A 1 163 ? 3.385  -7.348  -5.427  0.32 34.03 ?  163 LYS   A HE3  1 
ATOM   3557 H  HZ1  A LYS   A 1 163 ? 4.631  -7.156  -6.843  0.68 38.91 ?  163 LYS   A HZ1  1 
ATOM   3558 H  HZ1  B LYS   A 1 163 ? 5.013  -6.761  -6.904  0.32 35.00 ?  163 LYS   A HZ1  1 
ATOM   3559 H  HZ2  A LYS   A 1 163 ? 4.282  -5.951  -6.117  0.68 38.91 ?  163 LYS   A HZ2  1 
ATOM   3560 H  HZ2  B LYS   A 1 163 ? 4.668  -5.604  -6.103  0.32 35.00 ?  163 LYS   A HZ2  1 
ATOM   3561 H  HZ3  A LYS   A 1 163 ? 5.534  -6.627  -5.841  0.68 38.91 ?  163 LYS   A HZ3  1 
ATOM   3562 H  HZ3  B LYS   A 1 163 ? 5.891  -6.333  -5.834  0.32 35.00 ?  163 LYS   A HZ3  1 
ATOM   3563 N  N    . LEU   A 1 164 ? 5.654  -8.787  0.672   1.00 18.11 ?  164 LEU   A N    1 
ATOM   3564 C  CA   . LEU   A 1 164 ? 6.748  -9.742  0.837   1.00 17.26 ?  164 LEU   A CA   1 
ATOM   3565 C  C    . LEU   A 1 164 ? 6.325  -10.915 1.708   1.00 17.66 ?  164 LEU   A C    1 
ATOM   3566 O  O    . LEU   A 1 164 ? 6.652  -12.070 1.414   1.00 18.48 ?  164 LEU   A O    1 
ATOM   3567 C  CB   . LEU   A 1 164 ? 7.940  -9.032  1.472   1.00 16.99 ?  164 LEU   A CB   1 
ATOM   3568 C  CG   . LEU   A 1 164 ? 8.704  -8.066  0.566   1.00 17.20 ?  164 LEU   A CG   1 
ATOM   3569 C  CD1  . LEU   A 1 164 ? 9.582  -7.133  1.390   1.00 16.77 ?  164 LEU   A CD1  1 
ATOM   3570 C  CD2  . LEU   A 1 164 ? 9.542  -8.825  -0.442  1.00 17.80 ?  164 LEU   A CD2  1 
ATOM   3571 H  H    A LEU   A 1 164 ? 5.818  -8.001  0.986   0.68 21.73 ?  164 LEU   A H    1 
ATOM   3572 H  H    B LEU   A 1 164 ? 5.784  -8.027  1.057   0.32 21.73 ?  164 LEU   A H    1 
ATOM   3573 H  HA   . LEU   A 1 164 ? 7.015  -10.083 -0.030  1.00 20.70 ?  164 LEU   A HA   1 
ATOM   3574 H  HB2  . LEU   A 1 164 ? 7.625  -8.523  2.234   1.00 20.38 ?  164 LEU   A HB2  1 
ATOM   3575 H  HB3  . LEU   A 1 164 ? 8.573  -9.703  1.770   1.00 20.38 ?  164 LEU   A HB3  1 
ATOM   3576 H  HG   . LEU   A 1 164 ? 8.070  -7.517  0.078   1.00 20.63 ?  164 LEU   A HG   1 
ATOM   3577 H  HD11 . LEU   A 1 164 ? 10.062 -6.537  0.795   1.00 20.12 ?  164 LEU   A HD11 1 
ATOM   3578 H  HD12 . LEU   A 1 164 ? 9.019  -6.615  1.991   1.00 20.12 ?  164 LEU   A HD12 1 
ATOM   3579 H  HD13 . LEU   A 1 164 ? 10.210 -7.663  1.906   1.00 20.12 ?  164 LEU   A HD13 1 
ATOM   3580 H  HD21 . LEU   A 1 164 ? 9.910  -8.194  -1.082  1.00 21.35 ?  164 LEU   A HD21 1 
ATOM   3581 H  HD22 . LEU   A 1 164 ? 10.259 -9.280  0.023   1.00 21.35 ?  164 LEU   A HD22 1 
ATOM   3582 H  HD23 . LEU   A 1 164 ? 8.979  -9.464  -0.900  1.00 21.35 ?  164 LEU   A HD23 1 
ATOM   3583 N  N    . VAL   A 1 165 ? 5.618  -10.630 2.799   1.00 17.34 ?  165 VAL   A N    1 
ATOM   3584 C  CA   . VAL   A 1 165 ? 5.138  -11.690 3.679   1.00 17.46 ?  165 VAL   A CA   1 
ATOM   3585 C  C    . VAL   A 1 165 ? 4.106  -12.554 2.962   1.00 17.64 ?  165 VAL   A C    1 
ATOM   3586 O  O    . VAL   A 1 165 ? 4.206  -13.788 2.939   1.00 17.66 ?  165 VAL   A O    1 
ATOM   3587 C  CB   . VAL   A 1 165 ? 4.567  -11.075 4.969   1.00 18.56 ?  165 VAL   A CB   1 
ATOM   3588 C  CG1  . VAL   A 1 165 ? 3.814  -12.123 5.778   1.00 19.28 ?  165 VAL   A CG1  1 
ATOM   3589 C  CG2  . VAL   A 1 165 ? 5.676  -10.428 5.789   1.00 19.28 ?  165 VAL   A CG2  1 
ATOM   3590 H  H    . VAL   A 1 165 ? 5.405  -9.836  3.051   1.00 20.80 ?  165 VAL   A H    1 
ATOM   3591 H  HA   . VAL   A 1 165 ? 5.884  -12.258 3.927   1.00 20.95 ?  165 VAL   A HA   1 
ATOM   3592 H  HB   . VAL   A 1 165 ? 3.935  -10.379 4.729   1.00 22.27 ?  165 VAL   A HB   1 
ATOM   3593 H  HG11 . VAL   A 1 165 ? 3.695  -11.795 6.683   1.00 23.13 ?  165 VAL   A HG11 1 
ATOM   3594 H  HG12 . VAL   A 1 165 ? 2.943  -12.273 5.370   1.00 23.13 ?  165 VAL   A HG12 1 
ATOM   3595 H  HG13 . VAL   A 1 165 ? 4.323  -12.943 5.786   1.00 23.13 ?  165 VAL   A HG13 1 
ATOM   3596 H  HG21 . VAL   A 1 165 ? 5.293  -10.049 6.597   1.00 23.13 ?  165 VAL   A HG21 1 
ATOM   3597 H  HG22 . VAL   A 1 165 ? 6.334  -11.101 6.020   1.00 23.13 ?  165 VAL   A HG22 1 
ATOM   3598 H  HG23 . VAL   A 1 165 ? 6.090  -9.726  5.262   1.00 23.13 ?  165 VAL   A HG23 1 
ATOM   3599 N  N    . SER   A 1 166 ? 3.100  -11.917 2.358   1.00 18.65 ?  166 SER   A N    1 
ATOM   3600 C  CA   . SER   A 1 166 ? 1.981  -12.666 1.799   1.00 20.25 ?  166 SER   A CA   1 
ATOM   3601 C  C    . SER   A 1 166 ? 2.403  -13.554 0.640   1.00 21.30 ?  166 SER   A C    1 
ATOM   3602 O  O    . SER   A 1 166 ? 1.771  -14.593 0.403   1.00 23.43 ?  166 SER   A O    1 
ATOM   3603 C  CB   . SER   A 1 166 ? 0.882  -11.707 1.341   1.00 21.96 ?  166 SER   A CB   1 
ATOM   3604 O  OG   . SER   A 1 166 ? 0.260  -11.074 2.442   1.00 24.61 ?  166 SER   A OG   1 
ATOM   3605 H  H    . SER   A 1 166 ? 3.046  -11.069 2.260   1.00 22.38 ?  166 SER   A H    1 
ATOM   3606 H  HA   . SER   A 1 166 ? 1.607  -13.242 2.483   1.00 24.30 ?  166 SER   A HA   1 
ATOM   3607 H  HB2  . SER   A 1 166 ? 1.266  -11.036 0.759   1.00 26.34 ?  166 SER   A HB2  1 
ATOM   3608 H  HB3  . SER   A 1 166 ? 0.200  -12.208 0.860   1.00 26.34 ?  166 SER   A HB3  1 
ATOM   3609 H  HG   . SER   A 1 166 ? -0.329 -10.538 2.176   1.00 29.53 ?  166 SER   A HG   1 
ATOM   3610 N  N    . SER   A 1 167 ? 3.444  -13.166 -0.096  1.00 20.25 ?  167 SER   A N    1 
ATOM   3611 C  CA   . SER   A 1 167 ? 3.891  -13.917 -1.258  1.00 21.09 ?  167 SER   A CA   1 
ATOM   3612 C  C    . SER   A 1 167 ? 5.037  -14.866 -0.945  1.00 21.32 ?  167 SER   A C    1 
ATOM   3613 O  O    . SER   A 1 167 ? 5.544  -15.519 -1.861  1.00 22.48 ?  167 SER   A O    1 
ATOM   3614 C  CB   . SER   A 1 167 ? 4.312  -12.959 -2.382  1.00 22.05 ?  167 SER   A CB   1 
ATOM   3615 O  OG   . SER   A 1 167 ? 5.408  -12.149 -1.986  1.00 22.17 ?  167 SER   A OG   1 
ATOM   3616 H  H    . SER   A 1 167 ? 3.909  -12.455 0.058   1.00 24.30 ?  167 SER   A H    1 
ATOM   3617 H  HA   . SER   A 1 167 ? 3.149  -14.445 -1.590  1.00 25.31 ?  167 SER   A HA   1 
ATOM   3618 H  HB2  . SER   A 1 167 ? 4.571  -13.481 -3.160  1.00 26.46 ?  167 SER   A HB2  1 
ATOM   3619 H  HB3  . SER   A 1 167 ? 3.558  -12.388 -2.609  1.00 26.46 ?  167 SER   A HB3  1 
ATOM   3620 H  HG   . SER   A 1 167 ? 5.187  -11.685 -1.319  1.00 26.60 ?  167 SER   A HG   1 
ATOM   3621 N  N    . PHE   A 1 168 ? 5.455  -14.964 0.316   1.00 20.76 ?  168 PHE   A N    1 
ATOM   3622 C  CA   . PHE   A 1 168 ? 6.651  -15.734 0.633   1.00 22.20 ?  168 PHE   A CA   1 
ATOM   3623 C  C    . PHE   A 1 168 ? 6.379  -17.225 0.528   1.00 28.16 ?  168 PHE   A C    1 
ATOM   3624 O  O    . PHE   A 1 168 ? 5.418  -17.739 1.110   1.00 27.81 ?  168 PHE   A O    1 
ATOM   3625 C  CB   . PHE   A 1 168 ? 7.157  -15.419 2.036   1.00 20.18 ?  168 PHE   A CB   1 
ATOM   3626 C  CG   . PHE   A 1 168 ? 8.441  -16.129 2.367   1.00 18.96 ?  168 PHE   A CG   1 
ATOM   3627 C  CD1  . PHE   A 1 168 ? 9.621  -15.736 1.766   1.00 19.10 ?  168 PHE   A CD1  1 
ATOM   3628 C  CD2  . PHE   A 1 168 ? 8.470  -17.209 3.239   1.00 18.58 ?  168 PHE   A CD2  1 
ATOM   3629 C  CE1  . PHE   A 1 168 ? 10.805 -16.384 2.037   1.00 18.78 ?  168 PHE   A CE1  1 
ATOM   3630 C  CE2  . PHE   A 1 168 ? 9.663  -17.857 3.518   1.00 18.58 ?  168 PHE   A CE2  1 
ATOM   3631 C  CZ   . PHE   A 1 168 ? 10.827 -17.442 2.914   1.00 18.49 ?  168 PHE   A CZ   1 
ATOM   3632 H  H    . PHE   A 1 168 ? 5.074  -14.593 0.991   1.00 24.91 ?  168 PHE   A H    1 
ATOM   3633 H  HA   . PHE   A 1 168 ? 7.351  -15.508 -0.001  1.00 26.63 ?  168 PHE   A HA   1 
ATOM   3634 H  HB2  . PHE   A 1 168 ? 7.316  -14.463 2.106   1.00 24.21 ?  168 PHE   A HB2  1 
ATOM   3635 H  HB3  . PHE   A 1 168 ? 6.488  -15.691 2.681   1.00 24.21 ?  168 PHE   A HB3  1 
ATOM   3636 H  HD1  . PHE   A 1 168 ? 9.620  -15.018 1.173   1.00 22.91 ?  168 PHE   A HD1  1 
ATOM   3637 H  HD2  . PHE   A 1 168 ? 7.683  -17.492 3.648   1.00 22.29 ?  168 PHE   A HD2  1 
ATOM   3638 H  HE1  . PHE   A 1 168 ? 11.599 -16.102 1.634   1.00 22.53 ?  168 PHE   A HE1  1 
ATOM   3639 H  HE2  . PHE   A 1 168 ? 9.676  -18.578 4.108   1.00 22.29 ?  168 PHE   A HE2  1 
ATOM   3640 H  HZ   . PHE   A 1 168 ? 11.631 -17.878 3.099   1.00 22.19 ?  168 PHE   A HZ   1 
ATOM   3641 N  N    A LEU   A 1 169 ? 7.242  -17.922 -0.204  0.68 32.61 ?  169 LEU   A N    1 
ATOM   3642 N  N    B LEU   A 1 169 ? 7.239  -17.925 -0.204  0.32 31.72 ?  169 LEU   A N    1 
ATOM   3643 C  CA   A LEU   A 1 169 ? 7.098  -19.357 -0.372  0.68 37.99 ?  169 LEU   A CA   1 
ATOM   3644 C  CA   B LEU   A 1 169 ? 7.081  -19.359 -0.374  0.32 35.62 ?  169 LEU   A CA   1 
ATOM   3645 C  C    A LEU   A 1 169 ? 8.055  -20.078 0.568   0.68 40.55 ?  169 LEU   A C    1 
ATOM   3646 C  C    B LEU   A 1 169 ? 7.904  -20.112 0.664   0.32 37.12 ?  169 LEU   A C    1 
ATOM   3647 O  O    A LEU   A 1 169 ? 7.659  -20.537 1.641   0.68 41.36 ?  169 LEU   A O    1 
ATOM   3648 O  O    B LEU   A 1 169 ? 7.356  -20.678 1.611   0.32 37.59 ?  169 LEU   A O    1 
ATOM   3649 C  CB   A LEU   A 1 169 ? 7.376  -19.757 -1.823  0.68 39.86 ?  169 LEU   A CB   1 
ATOM   3650 C  CB   B LEU   A 1 169 ? 7.494  -19.780 -1.788  0.32 37.35 ?  169 LEU   A CB   1 
ATOM   3651 C  CG   A LEU   A 1 169 ? 7.015  -21.194 -2.206  0.68 41.41 ?  169 LEU   A CG   1 
ATOM   3652 C  CG   B LEU   A 1 169 ? 7.097  -21.195 -2.215  0.32 38.73 ?  169 LEU   A CG   1 
ATOM   3653 C  CD1  A LEU   A 1 169 ? 5.591  -21.518 -1.782  0.68 41.98 ?  169 LEU   A CD1  1 
ATOM   3654 C  CD1  B LEU   A 1 169 ? 5.672  -21.504 -1.788  0.32 39.24 ?  169 LEU   A CD1  1 
ATOM   3655 C  CD2  A LEU   A 1 169 ? 7.189  -21.406 -3.704  0.68 41.88 ?  169 LEU   A CD2  1 
ATOM   3656 C  CD2  B LEU   A 1 169 ? 7.245  -21.350 -3.722  0.32 39.19 ?  169 LEU   A CD2  1 
ATOM   3657 O  OXT  A LEU   A 1 169 ? 9.245  -20.206 0.283   0.68 40.98 -1 169 LEU   A OXT  1 
ATOM   3658 O  OXT  B LEU   A 1 169 ? 9.132  -20.163 0.588   0.32 37.27 -1 169 LEU   A OXT  1 
ATOM   3659 H  H    A LEU   A 1 169 ? 7.920  -17.584 -0.611  0.68 39.13 ?  169 LEU   A H    1 
ATOM   3660 H  H    B LEU   A 1 169 ? 7.918  -17.591 -0.614  0.32 38.06 ?  169 LEU   A H    1 
ATOM   3661 H  HA   A LEU   A 1 169 ? 6.190  -19.608 -0.148  0.68 45.58 ?  169 LEU   A HA   1 
ATOM   3662 H  HA   B LEU   A 1 169 ? 6.148  -19.578 -0.239  0.32 42.73 ?  169 LEU   A HA   1 
ATOM   3663 H  HB2  A LEU   A 1 169 ? 6.872  -19.169 -2.405  0.68 47.83 ?  169 LEU   A HB2  1 
ATOM   3664 H  HB2  B LEU   A 1 169 ? 7.091  -19.166 -2.419  0.32 44.81 ?  169 LEU   A HB2  1 
ATOM   3665 H  HB3  A LEU   A 1 169 ? 8.325  -19.645 -1.993  0.68 47.83 ?  169 LEU   A HB3  1 
ATOM   3666 H  HB3  B LEU   A 1 169 ? 8.461  -19.721 -1.853  0.32 44.81 ?  169 LEU   A HB3  1 
ATOM   3667 H  HG   A LEU   A 1 169 ? 7.613  -21.806 -1.747  0.68 49.69 ?  169 LEU   A HG   1 
ATOM   3668 H  HG   B LEU   A 1 169 ? 7.688  -21.835 -1.787  0.32 46.47 ?  169 LEU   A HG   1 
ATOM   3669 H  HD11 A LEU   A 1 169 ? 5.300  -22.318 -2.244  0.68 50.37 ?  169 LEU   A HD11 1 
ATOM   3670 H  HD11 B LEU   A 1 169 ? 5.355  -22.272 -2.283  0.32 47.08 ?  169 LEU   A HD11 1 
ATOM   3671 H  HD12 A LEU   A 1 169 ? 5.572  -21.664 -0.823  0.68 50.37 ?  169 LEU   A HD12 1 
ATOM   3672 H  HD12 B LEU   A 1 169 ? 5.661  -21.694 -0.836  0.32 47.08 ?  169 LEU   A HD12 1 
ATOM   3673 H  HD13 A LEU   A 1 169 ? 5.016  -20.772 -2.017  0.68 50.37 ?  169 LEU   A HD13 1 
ATOM   3674 H  HD13 B LEU   A 1 169 ? 5.113  -20.732 -1.979  0.32 47.08 ?  169 LEU   A HD13 1 
ATOM   3675 H  HD21 A LEU   A 1 169 ? 6.962  -22.324 -3.921  0.68 50.25 ?  169 LEU   A HD21 1 
ATOM   3676 H  HD21 B LEU   A 1 169 ? 7.004  -22.256 -3.971  0.32 47.02 ?  169 LEU   A HD21 1 
ATOM   3677 H  HD22 A LEU   A 1 169 ? 6.598  -20.799 -4.178  0.68 50.25 ?  169 LEU   A HD22 1 
ATOM   3678 H  HD22 B LEU   A 1 169 ? 6.656  -20.717 -4.163  0.32 47.02 ?  169 LEU   A HD22 1 
ATOM   3679 H  HD23 A LEU   A 1 169 ? 8.111  -21.226 -3.944  0.68 50.25 ?  169 LEU   A HD23 1 
ATOM   3680 H  HD23 B LEU   A 1 169 ? 8.166  -21.173 -3.969  0.32 47.02 ?  169 LEU   A HD23 1 
ATOM   3681 N  N    A SER   B 1 1   ? 50.792 -9.225  -23.777 0.68 29.89 ?  1   SER   B N    1 
ATOM   3682 N  N    B SER   B 1 1   ? 50.831 -9.283  -23.838 0.32 25.96 ?  1   SER   B N    1 
ATOM   3683 C  CA   A SER   B 1 1   ? 51.287 -10.266 -22.855 0.68 29.74 ?  1   SER   B CA   1 
ATOM   3684 C  CA   B SER   B 1 1   ? 51.270 -10.219 -22.781 0.32 26.00 ?  1   SER   B CA   1 
ATOM   3685 C  C    A SER   B 1 1   ? 50.216 -11.313 -22.589 0.68 28.01 ?  1   SER   B C    1 
ATOM   3686 C  C    B SER   B 1 1   ? 50.197 -11.263 -22.504 0.32 25.38 ?  1   SER   B C    1 
ATOM   3687 O  O    A SER   B 1 1   ? 49.022 -11.112 -22.861 0.68 27.14 ?  1   SER   B O    1 
ATOM   3688 O  O    B SER   B 1 1   ? 49.022 -11.085 -22.844 0.32 24.93 ?  1   SER   B O    1 
ATOM   3689 C  CB   A SER   B 1 1   ? 51.751 -9.650  -21.538 0.68 30.65 ?  1   SER   B CB   1 
ATOM   3690 C  CB   B SER   B 1 1   ? 51.607 -9.464  -21.499 0.32 26.27 ?  1   SER   B CB   1 
ATOM   3691 O  OG   A SER   B 1 1   ? 50.645 -9.319  -20.720 0.68 32.79 ?  1   SER   B OG   1 
ATOM   3692 O  OG   B SER   B 1 1   ? 50.591 -9.642  -20.530 0.32 27.30 ?  1   SER   B OG   1 
ATOM   3693 H  H1   A SER   B 1 1   ? 50.714 -9.573  -24.590 0.68 35.86 ?  1   SER   B H1   1 
ATOM   3694 H  H1   B SER   B 1 1   ? 51.546 -8.889  -24.188 0.32 31.14 ?  1   SER   B H1   1 
ATOM   3695 H  H2   A SER   B 1 1   ? 50.005 -8.936  -23.491 0.68 35.86 ?  1   SER   B H2   1 
ATOM   3696 H  H2   B SER   B 1 1   ? 50.399 -9.737  -24.466 0.32 31.14 ?  1   SER   B H2   1 
ATOM   3697 H  H3   A SER   B 1 1   ? 51.376 -8.555  -23.791 0.68 35.86 ?  1   SER   B H3   1 
ATOM   3698 H  H3   B SER   B 1 1   ? 50.295 -8.674  -23.481 0.32 31.14 ?  1   SER   B H3   1 
ATOM   3699 H  HA   A SER   B 1 1   ? 52.043 -10.703 -23.271 0.68 35.69 ?  1   SER   B HA   1 
ATOM   3700 H  HA   B SER   B 1 1   ? 52.067 -10.669 -23.090 0.32 31.20 ?  1   SER   B HA   1 
ATOM   3701 H  HB2  A SER   B 1 1   ? 52.312 -10.294 -21.077 0.68 36.77 ?  1   SER   B HB2  1 
ATOM   3702 H  HB2  B SER   B 1 1   ? 52.445 -9.804  -21.152 0.32 31.52 ?  1   SER   B HB2  1 
ATOM   3703 H  HB3  A SER   B 1 1   ? 52.256 -8.843  -21.724 0.68 36.77 ?  1   SER   B HB3  1 
ATOM   3704 H  HB3  B SER   B 1 1   ? 51.691 -8.518  -21.702 0.32 31.52 ?  1   SER   B HB3  1 
ATOM   3705 H  HG   A SER   B 1 1   ? 50.907 -8.874  -20.058 0.68 39.34 ?  1   SER   B HG   1 
ATOM   3706 H  HG   B SER   B 1 1   ? 50.625 -9.018  -19.969 0.32 32.75 ?  1   SER   B HG   1 
ATOM   3707 N  N    A MET   B 1 2   ? 50.667 -12.434 -22.046 0.68 27.06 ?  2   MET   B N    1 
ATOM   3708 N  N    B MET   B 1 2   ? 50.619 -12.350 -21.871 0.32 25.09 ?  2   MET   B N    1 
ATOM   3709 C  CA   A MET   B 1 2   ? 49.852 -13.627 -21.872 0.68 27.18 ?  2   MET   B CA   1 
ATOM   3710 C  CA   B MET   B 1 2   ? 49.795 -13.537 -21.682 0.32 25.05 ?  2   MET   B CA   1 
ATOM   3711 C  C    A MET   B 1 2   ? 49.614 -13.827 -20.383 0.68 24.86 ?  2   MET   B C    1 
ATOM   3712 C  C    B MET   B 1 2   ? 49.530 -13.702 -20.192 0.32 23.52 ?  2   MET   B C    1 
ATOM   3713 O  O    A MET   B 1 2   ? 50.553 -14.096 -19.630 0.68 24.85 ?  2   MET   B O    1 
ATOM   3714 O  O    B MET   B 1 2   ? 50.444 -14.020 -19.424 0.32 23.70 ?  2   MET   B O    1 
ATOM   3715 C  CB   A MET   B 1 2   ? 50.582 -14.818 -22.477 0.68 31.18 ?  2   MET   B CB   1 
ATOM   3716 C  CB   B MET   B 1 2   ? 50.539 -14.741 -22.242 0.32 27.12 ?  2   MET   B CB   1 
ATOM   3717 C  CG   A MET   B 1 2   ? 49.746 -16.078 -22.620 0.68 35.01 ?  2   MET   B CG   1 
ATOM   3718 C  CG   B MET   B 1 2   ? 49.660 -15.887 -22.722 0.32 28.88 ?  2   MET   B CG   1 
ATOM   3719 S  SD   A MET   B 1 2   ? 50.590 -17.300 -23.640 0.68 38.58 ?  2   MET   B SD   1 
ATOM   3720 S  SD   B MET   B 1 2   ? 50.572 -16.995 -23.802 0.32 30.51 ?  2   MET   B SD   1 
ATOM   3721 C  CE   A MET   B 1 2   ? 51.139 -16.247 -24.977 0.68 38.62 ?  2   MET   B CE   1 
ATOM   3722 C  CE   B MET   B 1 2   ? 51.561 -15.819 -24.705 0.32 30.70 ?  2   MET   B CE   1 
ATOM   3723 H  H    A MET   B 1 2   ? 51.475 -12.539 -21.765 0.68 32.46 ?  2   MET   B H    1 
ATOM   3724 H  H    B MET   B 1 2   ? 51.410 -12.434 -21.540 0.32 30.10 ?  2   MET   B H    1 
ATOM   3725 H  HA   A MET   B 1 2   ? 49.007 -13.524 -22.331 0.68 32.61 ?  2   MET   B HA   1 
ATOM   3726 H  HA   B MET   B 1 2   ? 48.964 -13.448 -22.173 0.32 30.06 ?  2   MET   B HA   1 
ATOM   3727 H  HB2  A MET   B 1 2   ? 50.884 -14.531 -23.348 0.68 37.41 ?  2   MET   B HB2  1 
ATOM   3728 H  HB2  B MET   B 1 2   ? 51.061 -14.390 -22.974 0.32 32.54 ?  2   MET   B HB2  1 
ATOM   3729 H  HB3  A MET   B 1 2   ? 51.345 -15.048 -21.929 0.68 37.41 ?  2   MET   B HB3  1 
ATOM   3730 H  HB3  B MET   B 1 2   ? 51.130 -15.112 -21.577 0.32 32.54 ?  2   MET   B HB3  1 
ATOM   3731 H  HG2  A MET   B 1 2   ? 49.594 -16.464 -21.740 0.68 42.00 ?  2   MET   B HG2  1 
ATOM   3732 H  HG2  B MET   B 1 2   ? 49.348 -16.399 -21.955 0.32 34.65 ?  2   MET   B HG2  1 
ATOM   3733 H  HG3  A MET   B 1 2   ? 48.902 -15.866 -23.045 0.68 42.00 ?  2   MET   B HG3  1 
ATOM   3734 H  HG3  B MET   B 1 2   ? 48.908 -15.549 -23.222 0.32 34.65 ?  2   MET   B HG3  1 
ATOM   3735 H  HE1  A MET   B 1 2   ? 51.306 -16.791 -25.748 0.68 46.34 ?  2   MET   B HE1  1 
ATOM   3736 H  HE1  B MET   B 1 2   ? 51.872 -16.256 -25.487 0.32 36.83 ?  2   MET   B HE1  1 
ATOM   3737 H  HE2  A MET   B 1 2   ? 50.439 -15.597 -25.168 0.68 46.34 ?  2   MET   B HE2  1 
ATOM   3738 H  HE2  B MET   B 1 2   ? 51.008 -15.053 -24.946 0.32 36.83 ?  2   MET   B HE2  1 
ATOM   3739 H  HE3  A MET   B 1 2   ? 51.953 -15.781 -24.710 0.68 46.34 ?  2   MET   B HE3  1 
ATOM   3740 H  HE3  B MET   B 1 2   ? 52.317 -15.533 -24.157 0.32 36.83 ?  2   MET   B HE3  1 
ATOM   3741 N  N    A VAL   B 1 3   ? 48.365 -13.673 -19.959 0.68 22.27 ?  3   VAL   B N    1 
ATOM   3742 N  N    B VAL   B 1 3   ? 48.288 -13.466 -19.785 0.32 21.76 ?  3   VAL   B N    1 
ATOM   3743 C  CA   A VAL   B 1 3   ? 47.956 -13.927 -18.586 0.68 20.95 ?  3   VAL   B CA   1 
ATOM   3744 C  CA   B VAL   B 1 3   ? 47.847 -13.733 -18.423 0.32 20.40 ?  3   VAL   B CA   1 
ATOM   3745 C  C    A VAL   B 1 3   ? 46.722 -14.818 -18.614 0.68 19.20 ?  3   VAL   B C    1 
ATOM   3746 C  C    B VAL   B 1 3   ? 46.590 -14.587 -18.470 0.32 18.83 ?  3   VAL   B C    1 
ATOM   3747 O  O    A VAL   B 1 3   ? 46.023 -14.922 -19.625 0.68 19.36 ?  3   VAL   B O    1 
ATOM   3748 O  O    B VAL   B 1 3   ? 45.754 -14.450 -19.369 0.32 18.72 ?  3   VAL   B O    1 
ATOM   3749 C  CB   A VAL   B 1 3   ? 47.670 -12.621 -17.809 0.68 22.64 ?  3   VAL   B CB   1 
ATOM   3750 C  CB   B VAL   B 1 3   ? 47.599 -12.445 -17.605 0.32 21.07 ?  3   VAL   B CB   1 
ATOM   3751 C  CG1  A VAL   B 1 3   ? 48.934 -11.766 -17.705 0.68 23.39 ?  3   VAL   B CG1  1 
ATOM   3752 C  CG1  B VAL   B 1 3   ? 48.879 -11.629 -17.485 0.32 21.37 ?  3   VAL   B CG1  1 
ATOM   3753 C  CG2  A VAL   B 1 3   ? 46.537 -11.846 -18.469 0.68 23.28 ?  3   VAL   B CG2  1 
ATOM   3754 C  CG2  B VAL   B 1 3   ? 46.476 -11.624 -18.222 0.32 21.26 ?  3   VAL   B CG2  1 
ATOM   3755 H  H    A VAL   B 1 3   ? 47.723 -13.413 -20.465 0.68 26.72 ?  3   VAL   B H    1 
ATOM   3756 H  H    B VAL   B 1 3   ? 47.678 -13.143 -20.298 0.32 26.10 ?  3   VAL   B H    1 
ATOM   3757 H  HA   A VAL   B 1 3   ? 48.665 -14.401 -18.123 0.68 25.13 ?  3   VAL   B HA   1 
ATOM   3758 H  HA   B VAL   B 1 3   ? 48.535 -14.241 -17.972 0.32 24.47 ?  3   VAL   B HA   1 
ATOM   3759 H  HB   A VAL   B 1 3   ? 47.391 -12.850 -16.908 0.68 27.17 ?  3   VAL   B HB   1 
ATOM   3760 H  HB   B VAL   B 1 3   ? 47.324 -12.700 -16.712 0.32 25.28 ?  3   VAL   B HB   1 
ATOM   3761 H  HG11 A VAL   B 1 3   ? 48.728 -10.962 -17.203 0.68 28.06 ?  3   VAL   B HG11 1 
ATOM   3762 H  HG11 B VAL   B 1 3   ? 48.697 -10.838 -16.956 0.32 25.63 ?  3   VAL   B HG11 1 
ATOM   3763 H  HG12 A VAL   B 1 3   ? 49.621 -12.275 -17.247 0.68 28.06 ?  3   VAL   B HG12 1 
ATOM   3764 H  HG12 B VAL   B 1 3   ? 49.557 -12.170 -17.051 0.32 25.63 ?  3   VAL   B HG12 1 
ATOM   3765 H  HG13 A VAL   B 1 3   ? 49.231 -11.534 -18.597 0.68 28.06 ?  3   VAL   B HG13 1 
ATOM   3766 H  HG13 B VAL   B 1 3   ? 49.175 -11.375 -18.372 0.32 25.63 ?  3   VAL   B HG13 1 
ATOM   3767 H  HG21 A VAL   B 1 3   ? 46.468 -10.974 -18.051 0.68 27.93 ?  3   VAL   B HG21 1 
ATOM   3768 H  HG21 B VAL   B 1 3   ? 46.445 -10.759 -17.786 0.32 25.51 ?  3   VAL   B HG21 1 
ATOM   3769 H  HG22 A VAL   B 1 3   ? 46.731 -11.746 -19.414 0.68 27.93 ?  3   VAL   B HG22 1 
ATOM   3770 H  HG22 B VAL   B 1 3   ? 46.650 -11.512 -19.169 0.32 25.51 ?  3   VAL   B HG22 1 
ATOM   3771 H  HG23 A VAL   B 1 3   ? 45.707 -12.335 -18.352 0.68 27.93 ?  3   VAL   B HG23 1 
ATOM   3772 H  HG23 B VAL   B 1 3   ? 45.634 -12.090 -18.094 0.32 25.51 ?  3   VAL   B HG23 1 
ATOM   3773 N  N    . ASN   B 1 4   ? 46.462 -15.472 -17.483 1.00 17.76 ?  4   ASN   B N    1 
ATOM   3774 C  CA   . ASN   B 1 4   ? 45.322 -16.380 -17.373 1.00 16.43 ?  4   ASN   B CA   1 
ATOM   3775 C  C    . ASN   B 1 4   ? 45.270 -17.346 -18.553 1.00 16.78 ?  4   ASN   B C    1 
ATOM   3776 O  O    . ASN   B 1 4   ? 44.209 -17.616 -19.108 1.00 17.21 ?  4   ASN   B O    1 
ATOM   3777 C  CB   . ASN   B 1 4   ? 44.001 -15.619 -17.216 1.00 15.72 ?  4   ASN   B CB   1 
ATOM   3778 C  CG   . ASN   B 1 4   ? 43.947 -14.812 -15.932 1.00 14.93 ?  4   ASN   B CG   1 
ATOM   3779 O  OD1  . ASN   B 1 4   ? 44.233 -15.325 -14.851 1.00 14.79 ?  4   ASN   B OD1  1 
ATOM   3780 N  ND2  . ASN   B 1 4   ? 43.594 -13.534 -16.047 1.00 16.12 ?  4   ASN   B ND2  1 
ATOM   3781 H  H    A ASN   B 1 4   ? 46.935 -15.411 -16.769 0.68 21.31 ?  4   ASN   B H    1 
ATOM   3782 H  H    B ASN   B 1 4   ? 47.039 -15.567 -16.854 0.32 21.31 ?  4   ASN   B H    1 
ATOM   3783 H  HA   . ASN   B 1 4   ? 45.440 -16.911 -16.571 1.00 19.71 ?  4   ASN   B HA   1 
ATOM   3784 H  HB2  . ASN   B 1 4   ? 43.890 -15.009 -17.961 1.00 18.86 ?  4   ASN   B HB2  1 
ATOM   3785 H  HB3  . ASN   B 1 4   ? 43.269 -16.258 -17.200 1.00 18.86 ?  4   ASN   B HB3  1 
ATOM   3786 H  HD21 . ASN   B 1 4   ? 43.555 -13.032 -15.346 1.00 19.34 ?  4   ASN   B HD21 1 
ATOM   3787 H  HD22 . ASN   B 1 4   ? 43.409 -13.202 -16.818 1.00 19.34 ?  4   ASN   B HD22 1 
ATOM   3788 N  N    . SER   B 1 5   ? 46.430 -17.873 -18.941 1.00 17.43 ?  5   SER   B N    1 
ATOM   3789 C  CA   . SER   B 1 5   ? 46.516 -18.779 -20.088 1.00 19.75 ?  5   SER   B CA   1 
ATOM   3790 C  C    . SER   B 1 5   ? 46.463 -20.220 -19.591 1.00 21.43 ?  5   SER   B C    1 
ATOM   3791 O  O    . SER   B 1 5   ? 47.435 -20.966 -19.633 1.00 24.31 ?  5   SER   B O    1 
ATOM   3792 C  CB   . SER   B 1 5   ? 47.781 -18.503 -20.898 1.00 21.35 ?  5   SER   B CB   1 
ATOM   3793 O  OG   . SER   B 1 5   ? 48.945 -18.626 -20.097 1.00 24.28 ?  5   SER   B OG   1 
ATOM   3794 H  H    . SER   B 1 5   ? 47.187 -17.723 -18.559 1.00 20.92 ?  5   SER   B H    1 
ATOM   3795 H  HA   . SER   B 1 5   ? 45.757 -18.631 -20.668 1.00 23.69 ?  5   SER   B HA   1 
ATOM   3796 H  HB2  . SER   B 1 5   ? 47.828 -19.138 -21.634 1.00 25.62 ?  5   SER   B HB2  1 
ATOM   3797 H  HB3  . SER   B 1 5   ? 47.723 -17.601 -21.250 1.00 25.62 ?  5   SER   B HB3  1 
ATOM   3798 H  HG   . SER   B 1 5   ? 49.004 -19.407 -19.800 1.00 29.13 ?  5   SER   B HG   1 
ATOM   3799 N  N    . PHE   B 1 6   ? 45.288 -20.589 -19.096 1.00 21.09 ?  6   PHE   B N    1 
ATOM   3800 C  CA   . PHE   B 1 6   ? 45.064 -21.947 -18.622 1.00 20.85 ?  6   PHE   B CA   1 
ATOM   3801 C  C    . PHE   B 1 6   ? 44.955 -22.893 -19.809 1.00 24.51 ?  6   PHE   B C    1 
ATOM   3802 O  O    . PHE   B 1 6   ? 44.299 -22.583 -20.806 1.00 26.79 ?  6   PHE   B O    1 
ATOM   3803 C  CB   . PHE   B 1 6   ? 43.780 -21.997 -17.795 1.00 18.83 ?  6   PHE   B CB   1 
ATOM   3804 C  CG   . PHE   B 1 6   ? 43.823 -21.150 -16.552 1.00 17.15 ?  6   PHE   B CG   1 
ATOM   3805 C  CD1  . PHE   B 1 6   ? 44.329 -21.662 -15.373 1.00 16.41 ?  6   PHE   B CD1  1 
ATOM   3806 C  CD2  . PHE   B 1 6   ? 43.358 -19.842 -16.566 1.00 16.77 ?  6   PHE   B CD2  1 
ATOM   3807 C  CE1  . PHE   B 1 6   ? 44.365 -20.892 -14.221 1.00 15.94 ?  6   PHE   B CE1  1 
ATOM   3808 C  CE2  . PHE   B 1 6   ? 43.397 -19.058 -15.422 1.00 17.44 ?  6   PHE   B CE2  1 
ATOM   3809 C  CZ   . PHE   B 1 6   ? 43.908 -19.577 -14.250 1.00 16.27 ?  6   PHE   B CZ   1 
ATOM   3810 H  H    . PHE   B 1 6   ? 44.606 -20.075 -19.028 1.00 25.31 ?  6   PHE   B H    1 
ATOM   3811 H  HA   . PHE   B 1 6   ? 45.805 -22.231 -18.068 1.00 25.01 ?  6   PHE   B HA   1 
ATOM   3812 H  HB2  . PHE   B 1 6   ? 43.041 -21.684 -18.343 1.00 22.59 ?  6   PHE   B HB2  1 
ATOM   3813 H  HB3  . PHE   B 1 6   ? 43.615 -22.914 -17.523 1.00 22.59 ?  6   PHE   B HB3  1 
ATOM   3814 H  HD1  . PHE   B 1 6   ? 44.646 -22.537 -15.351 1.00 19.69 ?  6   PHE   B HD1  1 
ATOM   3815 H  HD2  . PHE   B 1 6   ? 43.013 -19.488 -17.356 1.00 20.12 ?  6   PHE   B HD2  1 
ATOM   3816 H  HE1  . PHE   B 1 6   ? 44.718 -21.244 -13.434 1.00 19.12 ?  6   PHE   B HE1  1 
ATOM   3817 H  HE2  . PHE   B 1 6   ? 43.079 -18.184 -15.447 1.00 20.92 ?  6   PHE   B HE2  1 
ATOM   3818 H  HZ   . PHE   B 1 6   ? 43.933 -19.060 -13.479 1.00 19.51 ?  6   PHE   B HZ   1 
ATOM   3819 N  N    A SER   B 1 7   ? 45.613 -24.049 -19.695 0.68 25.32 ?  7   SER   B N    1 
ATOM   3820 N  N    B SER   B 1 7   ? 45.607 -24.051 -19.705 0.32 25.28 ?  7   SER   B N    1 
ATOM   3821 C  CA   A SER   B 1 7   ? 45.691 -25.020 -20.776 0.68 27.81 ?  7   SER   B CA   1 
ATOM   3822 C  CA   B SER   B 1 7   ? 45.618 -25.016 -20.794 0.32 26.69 ?  7   SER   B CA   1 
ATOM   3823 C  C    A SER   B 1 7   ? 45.631 -26.429 -20.205 0.68 27.28 ?  7   SER   B C    1 
ATOM   3824 C  C    B SER   B 1 7   ? 45.616 -26.432 -20.238 0.32 26.64 ?  7   SER   B C    1 
ATOM   3825 O  O    A SER   B 1 7   ? 46.216 -26.714 -19.157 0.68 28.02 ?  7   SER   B O    1 
ATOM   3826 O  O    B SER   B 1 7   ? 46.251 -26.711 -19.217 0.32 27.15 ?  7   SER   B O    1 
ATOM   3827 C  CB   A SER   B 1 7   ? 46.992 -24.839 -21.576 0.68 30.18 ?  7   SER   B CB   1 
ATOM   3828 C  CB   B SER   B 1 7   ? 46.843 -24.817 -21.699 0.32 27.82 ?  7   SER   B CB   1 
ATOM   3829 O  OG   A SER   B 1 7   ? 47.098 -25.802 -22.610 0.68 32.21 ?  7   SER   B OG   1 
ATOM   3830 O  OG   B SER   B 1 7   ? 46.701 -25.535 -22.912 0.32 28.78 ?  7   SER   B OG   1 
ATOM   3831 H  H    A SER   B 1 7   ? 46.037 -24.294 -18.986 0.68 30.38 ?  7   SER   B H    1 
ATOM   3832 H  H    B SER   B 1 7   ? 46.057 -24.298 -19.012 0.32 30.34 ?  7   SER   B H    1 
ATOM   3833 H  HA   A SER   B 1 7   ? 44.944 -24.903 -21.378 0.68 33.37 ?  7   SER   B HA   1 
ATOM   3834 H  HA   B SER   B 1 7   ? 44.824 -24.905 -21.334 0.32 32.03 ?  7   SER   B HA   1 
ATOM   3835 H  HB2  A SER   B 1 7   ? 46.999 -23.950 -21.972 0.68 36.21 ?  7   SER   B HB2  1 
ATOM   3836 H  HB2  B SER   B 1 7   ? 46.934 -23.872 -21.904 0.32 33.38 ?  7   SER   B HB2  1 
ATOM   3837 H  HB3  A SER   B 1 7   ? 47.751 -24.935 -20.979 0.68 36.21 ?  7   SER   B HB3  1 
ATOM   3838 H  HB3  B SER   B 1 7   ? 47.636 -25.131 -21.235 0.32 33.38 ?  7   SER   B HB3  1 
ATOM   3839 H  HG   A SER   B 1 7   ? 47.812 -25.686 -23.040 0.68 38.65 ?  7   SER   B HG   1 
ATOM   3840 H  HG   B SER   B 1 7   ? 47.380 -25.418 -23.396 0.32 34.53 ?  7   SER   B HG   1 
ATOM   3841 N  N    A GLY   B 1 8   ? 44.913 -27.307 -20.901 0.68 27.18 ?  8   GLY   B N    1 
ATOM   3842 N  N    B GLY   B 1 8   ? 44.896 -27.320 -20.920 0.32 26.44 ?  8   GLY   B N    1 
ATOM   3843 C  CA   A GLY   B 1 8   ? 44.890 -28.707 -20.539 0.68 26.45 ?  8   GLY   B CA   1 
ATOM   3844 C  CA   B GLY   B 1 8   ? 44.881 -28.719 -20.547 0.32 25.78 ?  8   GLY   B CA   1 
ATOM   3845 C  C    A GLY   B 1 8   ? 43.975 -29.055 -19.393 0.68 25.24 ?  8   GLY   B C    1 
ATOM   3846 C  C    B GLY   B 1 8   ? 43.955 -29.070 -19.410 0.32 24.81 ?  8   GLY   B C    1 
ATOM   3847 O  O    A GLY   B 1 8   ? 44.147 -30.116 -18.782 0.68 27.04 ?  8   GLY   B O    1 
ATOM   3848 O  O    B GLY   B 1 8   ? 44.104 -30.145 -18.819 0.32 25.73 ?  8   GLY   B O    1 
ATOM   3849 H  H    A GLY   B 1 8   ? 44.433 -27.108 -21.580 0.68 32.61 ?  8   GLY   B H    1 
ATOM   3850 H  H    B GLY   B 1 8   ? 44.410 -27.132 -21.602 0.32 31.73 ?  8   GLY   B H    1 
ATOM   3851 H  HA2  A GLY   B 1 8   ? 44.613 -29.226 -21.308 0.68 31.73 ?  8   GLY   B HA2  1 
ATOM   3852 H  HA2  B GLY   B 1 8   ? 44.618 -29.246 -21.317 0.32 30.93 ?  8   GLY   B HA2  1 
ATOM   3853 H  HA3  A GLY   B 1 8   ? 45.785 -28.988 -20.293 0.68 31.73 ?  8   GLY   B HA3  1 
ATOM   3854 H  HA3  B GLY   B 1 8   ? 45.776 -28.987 -20.291 0.32 30.93 ?  8   GLY   B HA3  1 
ATOM   3855 N  N    . TYR   B 1 9   ? 42.996 -28.209 -19.085 1.00 23.28 ?  9   TYR   B N    1 
ATOM   3856 C  CA   . TYR   B 1 9   ? 42.060 -28.492 -18.009 1.00 20.25 ?  9   TYR   B CA   1 
ATOM   3857 C  C    . TYR   B 1 9   ? 40.874 -29.291 -18.516 1.00 19.90 ?  9   TYR   B C    1 
ATOM   3858 O  O    . TYR   B 1 9   ? 40.444 -29.154 -19.666 1.00 22.24 ?  9   TYR   B O    1 
ATOM   3859 C  CB   . TYR   B 1 9   ? 41.552 -27.213 -17.351 1.00 19.37 ?  9   TYR   B CB   1 
ATOM   3860 C  CG   . TYR   B 1 9   ? 42.585 -26.586 -16.447 1.00 18.76 ?  9   TYR   B CG   1 
ATOM   3861 C  CD1  . TYR   B 1 9   ? 43.670 -25.903 -16.977 1.00 19.39 ?  9   TYR   B CD1  1 
ATOM   3862 C  CD2  . TYR   B 1 9   ? 42.499 -26.706 -15.069 1.00 18.16 ?  9   TYR   B CD2  1 
ATOM   3863 C  CE1  . TYR   B 1 9   ? 44.636 -25.340 -16.156 1.00 19.68 ?  9   TYR   B CE1  1 
ATOM   3864 C  CE2  . TYR   B 1 9   ? 43.458 -26.146 -14.240 1.00 18.72 ?  9   TYR   B CE2  1 
ATOM   3865 C  CZ   . TYR   B 1 9   ? 44.528 -25.462 -14.790 1.00 19.37 ?  9   TYR   B CZ   1 
ATOM   3866 O  OH   . TYR   B 1 9   ? 45.487 -24.914 -13.971 1.00 20.41 ?  9   TYR   B OH   1 
ATOM   3867 H  H    A TYR   B 1 9   ? 42.844 -27.467 -19.494 0.68 27.93 ?  9   TYR   B H    1 
ATOM   3868 H  H    B TYR   B 1 9   ? 42.857 -27.458 -19.481 0.32 27.93 ?  9   TYR   B H    1 
ATOM   3869 H  HA   . TYR   B 1 9   ? 42.502 -29.019 -17.332 1.00 24.30 ?  9   TYR   B HA   1 
ATOM   3870 H  HB2  . TYR   B 1 9   ? 41.308 -26.567 -18.036 1.00 23.24 ?  9   TYR   B HB2  1 
ATOM   3871 H  HB3  . TYR   B 1 9   ? 40.778 -27.436 -16.814 1.00 23.24 ?  9   TYR   B HB3  1 
ATOM   3872 H  HD1  . TYR   B 1 9   ? 43.746 -25.818 -17.901 1.00 23.27 ?  9   TYR   B HD1  1 
ATOM   3873 H  HD2  . TYR   B 1 9   ? 41.776 -27.169 -14.696 1.00 21.79 ?  9   TYR   B HD2  1 
ATOM   3874 H  HE1  . TYR   B 1 9   ? 45.350 -24.887 -16.528 1.00 23.62 ?  9   TYR   B HE1  1 
ATOM   3875 H  HE2  . TYR   B 1 9   ? 43.375 -26.240 -13.317 1.00 22.46 ?  9   TYR   B HE2  1 
ATOM   3876 H  HH   . TYR   B 1 9   ? 46.067 -24.532 -14.435 1.00 24.48 ?  9   TYR   B HH   1 
ATOM   3877 N  N    . LEU   B 1 10  ? 40.357 -30.143 -17.636 1.00 17.89 ?  10  LEU   B N    1 
ATOM   3878 C  CA   . LEU   B 1 10  ? 39.151 -30.911 -17.892 1.00 17.70 ?  10  LEU   B CA   1 
ATOM   3879 C  C    . LEU   B 1 10  ? 37.963 -30.151 -17.321 1.00 17.78 ?  10  LEU   B C    1 
ATOM   3880 O  O    . LEU   B 1 10  ? 37.986 -29.727 -16.160 1.00 17.34 ?  10  LEU   B O    1 
ATOM   3881 C  CB   . LEU   B 1 10  ? 39.261 -32.274 -17.212 1.00 18.92 ?  10  LEU   B CB   1 
ATOM   3882 C  CG   . LEU   B 1 10  ? 38.108 -33.234 -17.488 1.00 20.87 ?  10  LEU   B CG   1 
ATOM   3883 C  CD1  . LEU   B 1 10  ? 38.199 -33.766 -18.913 1.00 22.49 ?  10  LEU   B CD1  1 
ATOM   3884 C  CD2  . LEU   B 1 10  ? 38.082 -34.371 -16.477 1.00 22.12 ?  10  LEU   B CD2  1 
ATOM   3885 H  H    . LEU   B 1 10  ? 40.698 -30.296 -16.858 1.00 21.47 ?  10  LEU   B H    1 
ATOM   3886 H  HA   . LEU   B 1 10  ? 39.027 -31.042 -18.844 1.00 21.24 ?  10  LEU   B HA   1 
ATOM   3887 H  HB2  . LEU   B 1 10  ? 40.077 -32.708 -17.511 1.00 22.70 ?  10  LEU   B HB2  1 
ATOM   3888 H  HB3  . LEU   B 1 10  ? 39.301 -32.141 -16.251 1.00 22.70 ?  10  LEU   B HB3  1 
ATOM   3889 H  HG   . LEU   B 1 10  ? 37.270 -32.753 -17.408 1.00 25.04 ?  10  LEU   B HG   1 
ATOM   3890 H  HD11 . LEU   B 1 10  ? 37.484 -34.407 -19.056 1.00 26.99 ?  10  LEU   B HD11 1 
ATOM   3891 H  HD12 . LEU   B 1 10  ? 38.107 -33.025 -19.533 1.00 26.99 ?  10  LEU   B HD12 1 
ATOM   3892 H  HD13 . LEU   B 1 10  ? 39.059 -34.196 -19.035 1.00 26.99 ?  10  LEU   B HD13 1 
ATOM   3893 H  HD21 . LEU   B 1 10  ? 37.341 -34.959 -16.686 1.00 26.54 ?  10  LEU   B HD21 1 
ATOM   3894 H  HD22 . LEU   B 1 10  ? 38.918 -34.854 -16.528 1.00 26.54 ?  10  LEU   B HD22 1 
ATOM   3895 H  HD23 . LEU   B 1 10  ? 37.967 -33.994 -15.590 1.00 26.54 ?  10  LEU   B HD23 1 
ATOM   3896 N  N    . LYS   B 1 11  ? 36.932 -29.977 -18.138 1.00 19.08 ?  11  LYS   B N    1 
ATOM   3897 C  CA   . LYS   B 1 11  ? 35.737 -29.265 -17.715 1.00 20.90 ?  11  LYS   B CA   1 
ATOM   3898 C  C    . LYS   B 1 11  ? 34.879 -30.186 -16.852 1.00 19.95 ?  11  LYS   B C    1 
ATOM   3899 O  O    . LYS   B 1 11  ? 34.503 -31.282 -17.284 1.00 22.22 ?  11  LYS   B O    1 
ATOM   3900 C  CB   . LYS   B 1 11  ? 34.967 -28.816 -18.956 1.00 24.99 ?  11  LYS   B CB   1 
ATOM   3901 C  CG   . LYS   B 1 11  ? 33.839 -27.835 -18.698 1.00 28.96 ?  11  LYS   B CG   1 
ATOM   3902 C  CD   . LYS   B 1 11  ? 33.112 -27.509 -19.997 1.00 32.39 ?  11  LYS   B CD   1 
ATOM   3903 C  CE   . LYS   B 1 11  ? 32.087 -26.402 -19.815 1.00 34.88 ?  11  LYS   B CE   1 
ATOM   3904 N  NZ   . LYS   B 1 11  ? 32.728 -25.077 -19.598 1.00 36.18 ?  11  LYS   B NZ   1 
ATOM   3905 H  H    . LYS   B 1 11  ? 36.901 -30.266 -18.949 1.00 22.89 ?  11  LYS   B H    1 
ATOM   3906 H  HA   . LYS   B 1 11  ? 35.988 -28.482 -17.198 1.00 25.08 ?  11  LYS   B HA   1 
ATOM   3907 H  HB2  . LYS   B 1 11  ? 35.588 -28.388 -19.569 1.00 29.98 ?  11  LYS   B HB2  1 
ATOM   3908 H  HB3  . LYS   B 1 11  ? 34.582 -29.598 -19.379 1.00 29.98 ?  11  LYS   B HB3  1 
ATOM   3909 H  HG2  . LYS   B 1 11  ? 33.203 -28.229 -18.081 1.00 34.75 ?  11  LYS   B HG2  1 
ATOM   3910 H  HG3  . LYS   B 1 11  ? 34.201 -27.012 -18.334 1.00 34.75 ?  11  LYS   B HG3  1 
ATOM   3911 H  HD2  . LYS   B 1 11  ? 33.759 -27.217 -20.659 1.00 38.86 ?  11  LYS   B HD2  1 
ATOM   3912 H  HD3  . LYS   B 1 11  ? 32.650 -28.303 -20.311 1.00 38.86 ?  11  LYS   B HD3  1 
ATOM   3913 H  HE2  . LYS   B 1 11  ? 31.535 -26.345 -20.611 1.00 41.85 ?  11  LYS   B HE2  1 
ATOM   3914 H  HE3  . LYS   B 1 11  ? 31.538 -26.605 -19.042 1.00 41.85 ?  11  LYS   B HE3  1 
ATOM   3915 H  HZ1  . LYS   B 1 11  ? 32.104 -24.448 -19.509 1.00 43.41 ?  11  LYS   B HZ1  1 
ATOM   3916 H  HZ2  . LYS   B 1 11  ? 33.227 -25.096 -18.862 1.00 43.41 ?  11  LYS   B HZ2  1 
ATOM   3917 H  HZ3  . LYS   B 1 11  ? 33.246 -24.872 -20.294 1.00 43.41 ?  11  LYS   B HZ3  1 
ATOM   3918 N  N    . LEU   B 1 12  ? 34.563 -29.742 -15.637 1.00 17.86 ?  12  LEU   B N    1 
ATOM   3919 C  CA   . LEU   B 1 12  ? 33.610 -30.444 -14.786 1.00 17.54 ?  12  LEU   B CA   1 
ATOM   3920 C  C    . LEU   B 1 12  ? 32.221 -29.832 -14.865 1.00 17.57 ?  12  LEU   B C    1 
ATOM   3921 O  O    . LEU   B 1 12  ? 31.235 -30.547 -15.031 1.00 18.65 ?  12  LEU   B O    1 
ATOM   3922 C  CB   . LEU   B 1 12  ? 34.086 -30.463 -13.331 1.00 17.08 ?  12  LEU   B CB   1 
ATOM   3923 C  CG   . LEU   B 1 12  ? 35.420 -31.157 -13.067 1.00 17.14 ?  12  LEU   B CG   1 
ATOM   3924 C  CD1  . LEU   B 1 12  ? 35.756 -31.100 -11.587 1.00 17.35 ?  12  LEU   B CD1  1 
ATOM   3925 C  CD2  . LEU   B 1 12  ? 35.417 -32.593 -13.574 1.00 18.08 ?  12  LEU   B CD2  1 
ATOM   3926 H  H    . LEU   B 1 12  ? 34.883 -29.022 -15.287 1.00 21.43 ?  12  LEU   B H    1 
ATOM   3927 H  HA   . LEU   B 1 12  ? 33.536 -31.358 -15.090 1.00 21.04 ?  12  LEU   B HA   1 
ATOM   3928 H  HB2  . LEU   B 1 12  ? 34.170 -29.547 -13.028 1.00 20.49 ?  12  LEU   B HB2  1 
ATOM   3929 H  HB3  . LEU   B 1 12  ? 33.414 -30.918 -12.801 1.00 20.49 ?  12  LEU   B HB3  1 
ATOM   3930 H  HG   . LEU   B 1 12  ? 36.116 -30.676 -13.544 1.00 20.57 ?  12  LEU   B HG   1 
ATOM   3931 H  HD11 . LEU   B 1 12  ? 36.609 -31.542 -11.442 1.00 20.82 ?  12  LEU   B HD11 1 
ATOM   3932 H  HD12 . LEU   B 1 12  ? 35.816 -30.172 -11.310 1.00 20.82 ?  12  LEU   B HD12 1 
ATOM   3933 H  HD13 . LEU   B 1 12  ? 35.060 -31.552 -11.087 1.00 20.82 ?  12  LEU   B HD13 1 
ATOM   3934 H  HD21 . LEU   B 1 12  ? 36.227 -33.033 -13.274 1.00 21.69 ?  12  LEU   B HD21 1 
ATOM   3935 H  HD22 . LEU   B 1 12  ? 34.639 -33.049 -13.223 1.00 21.69 ?  12  LEU   B HD22 1 
ATOM   3936 H  HD23 . LEU   B 1 12  ? 35.387 -32.584 -14.545 1.00 21.69 ?  12  LEU   B HD23 1 
ATOM   3937 N  N    . THR   B 1 13  ? 32.132 -28.514 -14.748 1.00 17.58 ?  13  THR   B N    1 
ATOM   3938 C  CA   . THR   B 1 13  ? 30.907 -27.759 -14.949 1.00 17.51 ?  13  THR   B CA   1 
ATOM   3939 C  C    . THR   B 1 13  ? 31.240 -26.565 -15.836 1.00 20.08 ?  13  THR   B C    1 
ATOM   3940 O  O    . THR   B 1 13  ? 32.381 -26.382 -16.270 1.00 20.68 ?  13  THR   B O    1 
ATOM   3941 C  CB   . THR   B 1 13  ? 30.313 -27.276 -13.621 1.00 17.44 ?  13  THR   B CB   1 
ATOM   3942 O  OG1  . THR   B 1 13  ? 31.166 -26.263 -13.076 1.00 16.95 ?  13  THR   B OG1  1 
ATOM   3943 C  CG2  . THR   B 1 13  ? 30.187 -28.421 -12.626 1.00 18.20 ?  13  THR   B CG2  1 
ATOM   3944 H  H    . THR   B 1 13  ? 32.801 -28.011 -14.544 1.00 21.09 ?  13  THR   B H    1 
ATOM   3945 H  HA   . THR   B 1 13  ? 30.250 -28.313 -15.394 1.00 21.01 ?  13  THR   B HA   1 
ATOM   3946 H  HB   . THR   B 1 13  ? 29.426 -26.903 -13.773 1.00 20.92 ?  13  THR   B HB   1 
ATOM   3947 H  HG1  . THR   B 1 13  ? 30.866 -25.496 -13.263 1.00 20.34 ?  13  THR   B HG1  1 
ATOM   3948 H  HG21 . THR   B 1 13  ? 29.702 -28.127 -11.838 1.00 21.83 ?  13  THR   B HG21 1 
ATOM   3949 H  HG22 . THR   B 1 13  ? 29.709 -29.159 -13.033 1.00 21.83 ?  13  THR   B HG22 1 
ATOM   3950 H  HG23 . THR   B 1 13  ? 31.068 -28.724 -12.358 1.00 21.83 ?  13  THR   B HG23 1 
ATOM   3951 N  N    A ASP   B 1 14  ? 30.232 -25.738 -16.103 0.68 21.12 ?  14  ASP   B N    1 
ATOM   3952 N  N    B ASP   B 1 14  ? 30.234 -25.726 -16.091 0.32 20.82 ?  14  ASP   B N    1 
ATOM   3953 C  CA   A ASP   B 1 14  ? 30.456 -24.580 -16.960 0.68 22.78 ?  14  ASP   B CA   1 
ATOM   3954 C  CA   B ASP   B 1 14  ? 30.436 -24.568 -16.957 0.32 21.72 ?  14  ASP   B CA   1 
ATOM   3955 C  C    A ASP   B 1 14  ? 31.567 -23.683 -16.425 0.68 20.68 ?  14  ASP   B C    1 
ATOM   3956 C  C    B ASP   B 1 14  ? 31.451 -23.579 -16.398 0.32 19.89 ?  14  ASP   B C    1 
ATOM   3957 O  O    A ASP   B 1 14  ? 32.259 -23.022 -17.210 0.68 21.81 ?  14  ASP   B O    1 
ATOM   3958 O  O    B ASP   B 1 14  ? 31.923 -22.713 -17.143 0.32 20.29 ?  14  ASP   B O    1 
ATOM   3959 C  CB   A ASP   B 1 14  ? 29.159 -23.791 -17.132 0.68 26.82 ?  14  ASP   B CB   1 
ATOM   3960 C  CB   B ASP   B 1 14  ? 29.115 -23.836 -17.187 0.32 24.56 ?  14  ASP   B CB   1 
ATOM   3961 C  CG   A ASP   B 1 14  ? 28.179 -24.475 -18.054 0.68 30.48 ?  14  ASP   B CG   1 
ATOM   3962 C  CG   B ASP   B 1 14  ? 28.214 -24.562 -18.165 0.32 27.01 ?  14  ASP   B CG   1 
ATOM   3963 O  OD1  A ASP   B 1 14  ? 28.528 -25.522 -18.646 0.68 31.66 ?  14  ASP   B OD1  1 
ATOM   3964 O  OD1  B ASP   B 1 14  ? 28.745 -25.195 -19.103 0.32 27.73 ?  14  ASP   B OD1  1 
ATOM   3965 O  OD2  A ASP   B 1 14  ? 27.048 -23.963 -18.182 0.68 31.90 -1 14  ASP   B OD2  1 
ATOM   3966 O  OD2  B ASP   B 1 14  ? 26.978 -24.508 -17.997 0.32 27.87 -1 14  ASP   B OD2  1 
ATOM   3967 H  H    A ASP   B 1 14  ? 29.433 -25.815 -15.799 0.68 25.34 ?  14  ASP   B H    1 
ATOM   3968 H  H    B ASP   B 1 14  ? 29.439 -25.805 -15.779 0.32 24.98 ?  14  ASP   B H    1 
ATOM   3969 H  HA   A ASP   B 1 14  ? 30.733 -24.884 -17.834 0.68 27.33 ?  14  ASP   B HA   1 
ATOM   3970 H  HA   B ASP   B 1 14  ? 30.759 -24.877 -17.818 0.32 26.06 ?  14  ASP   B HA   1 
ATOM   3971 H  HB2  A ASP   B 1 14  ? 28.718 -23.700 -16.276 0.68 32.18 ?  14  ASP   B HB2  1 
ATOM   3972 H  HB2  B ASP   B 1 14  ? 28.647 -23.759 -16.341 0.32 29.47 ?  14  ASP   B HB2  1 
ATOM   3973 H  HB3  A ASP   B 1 14  ? 29.358 -22.918 -17.503 0.68 32.18 ?  14  ASP   B HB3  1 
ATOM   3974 H  HB3  B ASP   B 1 14  ? 29.308 -22.948 -17.537 0.32 29.47 ?  14  ASP   B HB3  1 
ATOM   3975 N  N    . ASN   B 1 15  ? 31.774 -23.659 -15.105 1.00 18.03 ?  15  ASN   B N    1 
ATOM   3976 C  CA   . ASN   B 1 15  ? 32.741 -22.744 -14.505 1.00 15.51 ?  15  ASN   B CA   1 
ATOM   3977 C  C    . ASN   B 1 15  ? 33.833 -23.403 -13.672 1.00 14.21 ?  15  ASN   B C    1 
ATOM   3978 O  O    . ASN   B 1 15  ? 34.692 -22.680 -13.158 1.00 14.99 ?  15  ASN   B O    1 
ATOM   3979 C  CB   . ASN   B 1 15  ? 32.036 -21.689 -13.639 1.00 15.89 ?  15  ASN   B CB   1 
ATOM   3980 C  CG   . ASN   B 1 15  ? 31.412 -22.287 -12.401 1.00 15.53 ?  15  ASN   B CG   1 
ATOM   3981 O  OD1  . ASN   B 1 15  ? 30.472 -23.086 -12.490 1.00 17.59 ?  15  ASN   B OD1  1 
ATOM   3982 N  ND2  . ASN   B 1 15  ? 31.935 -21.937 -11.243 1.00 14.62 ?  15  ASN   B ND2  1 
ATOM   3983 H  H    A ASN   B 1 15  ? 31.367 -24.165 -14.540 0.68 21.64 ?  15  ASN   B H    1 
ATOM   3984 H  H    B ASN   B 1 15  ? 31.420 -24.213 -14.550 0.32 21.64 ?  15  ASN   B H    1 
ATOM   3985 H  HA   . ASN   B 1 15  ? 33.188 -22.264 -15.213 1.00 18.61 ?  15  ASN   B HA   1 
ATOM   3986 H  HB2  . ASN   B 1 15  ? 32.692 -21.018 -13.362 1.00 19.07 ?  15  ASN   B HB2  1 
ATOM   3987 H  HB3  . ASN   B 1 15  ? 31.336 -21.259 -14.158 1.00 19.07 ?  15  ASN   B HB3  1 
ATOM   3988 H  HD21 . ASN   B 1 15  ? 31.610 -22.248 -10.510 1.00 17.53 ?  15  ASN   B HD21 1 
ATOM   3989 H  HD22 . ASN   B 1 15  ? 32.596 -21.380 -11.210 1.00 17.53 ?  15  ASN   B HD22 1 
ATOM   3990 N  N    . VAL   B 1 16  ? 33.828 -24.725 -13.508 1.00 14.12 ?  16  VAL   B N    1 
ATOM   3991 C  CA   . VAL   B 1 16  ? 34.834 -25.422 -12.709 1.00 13.96 ?  16  VAL   B CA   1 
ATOM   3992 C  C    . VAL   B 1 16  ? 35.618 -26.357 -13.616 1.00 14.29 ?  16  VAL   B C    1 
ATOM   3993 O  O    . VAL   B 1 16  ? 35.035 -27.241 -14.265 1.00 15.12 ?  16  VAL   B O    1 
ATOM   3994 C  CB   . VAL   B 1 16  ? 34.214 -26.191 -11.533 1.00 14.08 ?  16  VAL   B CB   1 
ATOM   3995 C  CG1  . VAL   B 1 16  ? 35.295 -26.921 -10.739 1.00 14.39 ?  16  VAL   B CG1  1 
ATOM   3996 C  CG2  . VAL   B 1 16  ? 33.416 -25.249 -10.637 1.00 14.93 ?  16  VAL   B CG2  1 
ATOM   3997 H  H    . VAL   B 1 16  ? 33.233 -25.252 -13.850 1.00 16.93 ?  16  VAL   B H    1 
ATOM   3998 H  HA   . VAL   B 1 16  ? 35.450 -24.772 -12.342 1.00 16.75 ?  16  VAL   B HA   1 
ATOM   3999 H  HB   . VAL   B 1 16  ? 33.602 -26.859 -11.880 1.00 16.89 ?  16  VAL   B HB   1 
ATOM   4000 H  HG11 . VAL   B 1 16  ? 34.912 -27.232 -9.902  1.00 17.26 ?  16  VAL   B HG11 1 
ATOM   4001 H  HG12 . VAL   B 1 16  ? 35.616 -27.673 -11.254 1.00 17.26 ?  16  VAL   B HG12 1 
ATOM   4002 H  HG13 . VAL   B 1 16  ? 36.020 -26.303 -10.557 1.00 17.26 ?  16  VAL   B HG13 1 
ATOM   4003 H  HG21 . VAL   B 1 16  ? 33.082 -25.748 -9.874  1.00 17.91 ?  16  VAL   B HG21 1 
ATOM   4004 H  HG22 . VAL   B 1 16  ? 33.993 -24.532 -10.339 1.00 17.91 ?  16  VAL   B HG22 1 
ATOM   4005 H  HG23 . VAL   B 1 16  ? 32.671 -24.889 -11.145 1.00 17.91 ?  16  VAL   B HG23 1 
ATOM   4006 N  N    . TYR   B 1 17  ? 36.939 -26.180 -13.620 1.00 14.83 ?  17  TYR   B N    1 
ATOM   4007 C  CA   . TYR   B 1 17  ? 37.876 -26.938 -14.432 1.00 15.10 ?  17  TYR   B CA   1 
ATOM   4008 C  C    . TYR   B 1 17  ? 38.932 -27.549 -13.520 1.00 13.98 ?  17  TYR   B C    1 
ATOM   4009 O  O    . TYR   B 1 17  ? 39.225 -27.012 -12.446 1.00 14.56 ?  17  TYR   B O    1 
ATOM   4010 C  CB   . TYR   B 1 17  ? 38.580 -26.014 -15.430 1.00 18.35 ?  17  TYR   B CB   1 
ATOM   4011 C  CG   . TYR   B 1 17  ? 37.654 -25.241 -16.336 1.00 21.85 ?  17  TYR   B CG   1 
ATOM   4012 C  CD1  . TYR   B 1 17  ? 37.110 -24.024 -15.940 1.00 23.71 ?  17  TYR   B CD1  1 
ATOM   4013 C  CD2  . TYR   B 1 17  ? 37.324 -25.729 -17.591 1.00 24.32 ?  17  TYR   B CD2  1 
ATOM   4014 C  CE1  . TYR   B 1 17  ? 36.260 -23.314 -16.773 1.00 25.68 ?  17  TYR   B CE1  1 
ATOM   4015 C  CE2  . TYR   B 1 17  ? 36.479 -25.028 -18.430 1.00 26.36 ?  17  TYR   B CE2  1 
ATOM   4016 C  CZ   . TYR   B 1 17  ? 35.948 -23.823 -18.015 1.00 27.20 ?  17  TYR   B CZ   1 
ATOM   4017 O  OH   . TYR   B 1 17  ? 35.109 -23.121 -18.847 1.00 28.58 ?  17  TYR   B OH   1 
ATOM   4018 H  H    . TYR   B 1 17  ? 37.337 -25.590 -13.132 1.00 17.79 ?  17  TYR   B H    1 
ATOM   4019 H  HA   . TYR   B 1 17  ? 37.411 -27.645 -14.914 1.00 18.12 ?  17  TYR   B HA   1 
ATOM   4020 H  HB2  . TYR   B 1 17  ? 39.120 -25.378 -14.940 1.00 22.01 ?  17  TYR   B HB2  1 
ATOM   4021 H  HB3  . TYR   B 1 17  ? 39.144 -26.557 -15.997 1.00 22.01 ?  17  TYR   B HB3  1 
ATOM   4022 H  HD1  . TYR   B 1 17  ? 37.320 -23.680 -15.103 1.00 28.44 ?  17  TYR   B HD1  1 
ATOM   4023 H  HD2  . TYR   B 1 17  ? 37.674 -26.541 -17.876 1.00 29.18 ?  17  TYR   B HD2  1 
ATOM   4024 H  HE1  . TYR   B 1 17  ? 35.902 -22.500 -16.497 1.00 30.81 ?  17  TYR   B HE1  1 
ATOM   4025 H  HE2  . TYR   B 1 17  ? 36.260 -25.369 -19.271 1.00 31.63 ?  17  TYR   B HE2  1 
ATOM   4026 H  HH   . TYR   B 1 17  ? 34.994 -23.536 -19.569 1.00 34.29 ?  17  TYR   B HH   1 
ATOM   4027 N  N    . ILE   B 1 18  ? 39.535 -28.659 -13.957 1.00 13.97 ?  18  ILE   B N    1 
ATOM   4028 C  CA   . ILE   B 1 18  ? 40.475 -29.385 -13.109 1.00 14.13 ?  18  ILE   B CA   1 
ATOM   4029 C  C    . ILE   B 1 18  ? 41.628 -29.940 -13.939 1.00 14.57 ?  18  ILE   B C    1 
ATOM   4030 O  O    . ILE   B 1 18  ? 41.464 -30.314 -15.104 1.00 15.88 ?  18  ILE   B O    1 
ATOM   4031 C  CB   . ILE   B 1 18  ? 39.732 -30.486 -12.305 1.00 14.86 ?  18  ILE   B CB   1 
ATOM   4032 C  CG1  . ILE   B 1 18  ? 40.594 -31.038 -11.169 1.00 15.36 ?  18  ILE   B CG1  1 
ATOM   4033 C  CG2  . ILE   B 1 18  ? 39.223 -31.604 -13.225 1.00 15.20 ?  18  ILE   B CG2  1 
ATOM   4034 C  CD1  . ILE   B 1 18  ? 39.798 -31.861 -10.160 1.00 16.87 ?  18  ILE   B CD1  1 
ATOM   4035 H  H    . ILE   B 1 18  ? 39.422 -29.006 -14.735 1.00 16.76 ?  18  ILE   B H    1 
ATOM   4036 H  HA   . ILE   B 1 18  ? 40.846 -28.767 -12.460 1.00 16.95 ?  18  ILE   B HA   1 
ATOM   4037 H  HB   . ILE   B 1 18  ? 38.952 -30.078 -11.893 1.00 17.83 ?  18  ILE   B HB   1 
ATOM   4038 H  HG12 . ILE   B 1 18  ? 41.281 -31.608 -11.540 1.00 18.42 ?  18  ILE   B HG12 1 
ATOM   4039 H  HG13 . ILE   B 1 18  ? 40.996 -30.295 -10.690 1.00 18.42 ?  18  ILE   B HG13 1 
ATOM   4040 H  HG21 . ILE   B 1 18  ? 38.634 -32.189 -12.718 1.00 18.24 ?  18  ILE   B HG21 1 
ATOM   4041 H  HG22 . ILE   B 1 18  ? 38.734 -31.204 -13.959 1.00 18.24 ?  18  ILE   B HG22 1 
ATOM   4042 H  HG23 . ILE   B 1 18  ? 39.979 -32.106 -13.561 1.00 18.24 ?  18  ILE   B HG23 1 
ATOM   4043 H  HD11 . ILE   B 1 18  ? 40.387 -32.132 -9.437  1.00 20.24 ?  18  ILE   B HD11 1 
ATOM   4044 H  HD12 . ILE   B 1 18  ? 39.073 -31.319 -9.808  1.00 20.24 ?  18  ILE   B HD12 1 
ATOM   4045 H  HD13 . ILE   B 1 18  ? 39.438 -32.645 -10.603 1.00 20.24 ?  18  ILE   B HD13 1 
ATOM   4046 N  N    . LYS   B 1 19  ? 42.811 -29.984 -13.324 1.00 14.80 ?  19  LYS   B N    1 
ATOM   4047 C  CA   . LYS   B 1 19  ? 44.017 -30.454 -13.986 1.00 16.16 ?  19  LYS   B CA   1 
ATOM   4048 C  C    . LYS   B 1 19  ? 44.919 -31.131 -12.967 1.00 16.20 ?  19  LYS   B C    1 
ATOM   4049 O  O    . LYS   B 1 19  ? 45.005 -30.701 -11.813 1.00 15.32 ?  19  LYS   B O    1 
ATOM   4050 C  CB   . LYS   B 1 19  ? 44.784 -29.289 -14.623 1.00 17.69 ?  19  LYS   B CB   1 
ATOM   4051 C  CG   . LYS   B 1 19  ? 45.956 -29.699 -15.497 1.00 20.28 ?  19  LYS   B CG   1 
ATOM   4052 C  CD   . LYS   B 1 19  ? 46.657 -28.467 -16.048 1.00 22.60 ?  19  LYS   B CD   1 
ATOM   4053 C  CE   . LYS   B 1 19  ? 47.869 -28.833 -16.879 1.00 24.85 ?  19  LYS   B CE   1 
ATOM   4054 N  NZ   . LYS   B 1 19  ? 48.592 -27.629 -17.367 1.00 25.75 ?  19  LYS   B NZ   1 
ATOM   4055 H  H    . LYS   B 1 19  ? 42.929 -29.740 -12.507 1.00 17.75 ?  19  LYS   B H    1 
ATOM   4056 H  HA   . LYS   B 1 19  ? 43.776 -31.094 -14.678 1.00 19.39 ?  19  LYS   B HA   1 
ATOM   4057 H  HB2  . LYS   B 1 19  ? 44.168 -28.785 -15.176 1.00 21.22 ?  19  LYS   B HB2  1 
ATOM   4058 H  HB3  . LYS   B 1 19  ? 45.122 -28.722 -13.910 1.00 21.22 ?  19  LYS   B HB3  1 
ATOM   4059 H  HG2  . LYS   B 1 19  ? 46.587 -30.209 -14.969 1.00 24.34 ?  19  LYS   B HG2  1 
ATOM   4060 H  HG3  . LYS   B 1 19  ? 45.627 -30.231 -16.241 1.00 24.34 ?  19  LYS   B HG3  1 
ATOM   4061 H  HD2  . LYS   B 1 19  ? 46.037 -27.973 -16.610 1.00 27.12 ?  19  LYS   B HD2  1 
ATOM   4062 H  HD3  . LYS   B 1 19  ? 46.949 -27.911 -15.308 1.00 27.12 ?  19  LYS   B HD3  1 
ATOM   4063 H  HE2  . LYS   B 1 19  ? 48.479 -29.357 -16.335 1.00 29.81 ?  19  LYS   B HE2  1 
ATOM   4064 H  HE3  . LYS   B 1 19  ? 47.581 -29.350 -17.649 1.00 29.81 ?  19  LYS   B HE3  1 
ATOM   4065 H  HZ1  . LYS   B 1 19  ? 49.251 -27.872 -17.916 1.00 30.89 ?  19  LYS   B HZ1  1 
ATOM   4066 H  HZ2  . LYS   B 1 19  ? 48.033 -27.095 -17.807 1.00 30.89 ?  19  LYS   B HZ2  1 
ATOM   4067 H  HZ3  . LYS   B 1 19  ? 48.939 -27.183 -16.681 1.00 30.89 ?  19  LYS   B HZ3  1 
ATOM   4068 N  N    . ASN   B 1 20  ? 45.597 -32.186 -13.406 1.00 17.40 ?  20  ASN   B N    1 
ATOM   4069 C  CA   . ASN   B 1 20  ? 46.633 -32.817 -12.602 1.00 18.10 ?  20  ASN   B CA   1 
ATOM   4070 C  C    . ASN   B 1 20  ? 47.903 -31.993 -12.780 1.00 18.61 ?  20  ASN   B C    1 
ATOM   4071 O  O    . ASN   B 1 20  ? 48.542 -32.053 -13.837 1.00 20.57 ?  20  ASN   B O    1 
ATOM   4072 C  CB   . ASN   B 1 20  ? 46.814 -34.263 -13.062 1.00 20.58 ?  20  ASN   B CB   1 
ATOM   4073 C  CG   . ASN   B 1 20  ? 47.965 -34.981 -12.367 1.00 22.33 ?  20  ASN   B CG   1 
ATOM   4074 O  OD1  . ASN   B 1 20  ? 48.635 -35.824 -12.974 1.00 24.54 ?  20  ASN   B OD1  1 
ATOM   4075 N  ND2  . ASN   B 1 20  ? 48.195 -34.669 -11.097 1.00 22.01 ?  20  ASN   B ND2  1 
ATOM   4076 H  H    . ASN   B 1 20  ? 45.468 -32.557 -14.173 1.00 20.87 ?  20  ASN   B H    1 
ATOM   4077 H  HA   . ASN   B 1 20  ? 46.363 -32.814 -11.666 1.00 21.72 ?  20  ASN   B HA   1 
ATOM   4078 H  HB2  . ASN   B 1 20  ? 45.998 -34.758 -12.877 1.00 24.69 ?  20  ASN   B HB2  1 
ATOM   4079 H  HB3  . ASN   B 1 20  ? 46.989 -34.263 -14.015 1.00 24.69 ?  20  ASN   B HB3  1 
ATOM   4080 H  HD21 . ASN   B 1 20  ? 48.838 -35.047 -10.671 1.00 26.41 ?  20  ASN   B HD21 1 
ATOM   4081 H  HD22 . ASN   B 1 20  ? 47.708 -34.079 -10.699 1.00 26.41 ?  20  ASN   B HD22 1 
ATOM   4082 N  N    . ALA   B 1 21  ? 48.260 -31.204 -11.766 1.00 18.25 ?  21  ALA   B N    1 
ATOM   4083 C  CA   . ALA   B 1 21  ? 49.371 -30.278 -11.918 1.00 19.10 ?  21  ALA   B CA   1 
ATOM   4084 C  C    . ALA   B 1 21  ? 49.837 -29.780 -10.557 1.00 18.01 ?  21  ALA   B C    1 
ATOM   4085 O  O    . ALA   B 1 21  ? 49.099 -29.804 -9.568  1.00 17.92 ?  21  ALA   B O    1 
ATOM   4086 C  CB   . ALA   B 1 21  ? 48.970 -29.105 -12.809 1.00 20.36 ?  21  ALA   B CB   1 
ATOM   4087 H  H    . ALA   B 1 21  ? 47.878 -31.194 -10.992 1.00 21.89 ?  21  ALA   B H    1 
ATOM   4088 H  HA   . ALA   B 1 21  ? 50.110 -30.746 -12.338 1.00 22.92 ?  21  ALA   B HA   1 
ATOM   4089 H  HB1  . ALA   B 1 21  ? 49.757 -28.584 -12.990 1.00 24.43 ?  21  ALA   B HB1  1 
ATOM   4090 H  HB2  . ALA   B 1 21  ? 48.604 -29.462 -13.634 1.00 24.43 ?  21  ALA   B HB2  1 
ATOM   4091 H  HB3  . ALA   B 1 21  ? 48.300 -28.581 -12.348 1.00 24.43 ?  21  ALA   B HB3  1 
ATOM   4092 N  N    . ASP   B 1 22  ? 51.095 -29.336 -10.540 1.00 17.09 ?  22  ASP   B N    1 
ATOM   4093 C  CA   . ASP   B 1 22  ? 51.720 -28.656 -9.409  1.00 16.26 ?  22  ASP   B CA   1 
ATOM   4094 C  C    . ASP   B 1 22  ? 51.317 -27.184 -9.466  1.00 14.83 ?  22  ASP   B C    1 
ATOM   4095 O  O    . ASP   B 1 22  ? 51.628 -26.498 -10.444 1.00 15.36 ?  22  ASP   B O    1 
ATOM   4096 C  CB   . ASP   B 1 22  ? 53.238 -28.827 -9.574  1.00 17.80 ?  22  ASP   B CB   1 
ATOM   4097 C  CG   . ASP   B 1 22  ? 54.071 -28.081 -8.533  1.00 19.67 ?  22  ASP   B CG   1 
ATOM   4098 O  OD1  . ASP   B 1 22  ? 53.697 -26.981 -8.097  1.00 19.93 ?  22  ASP   B OD1  1 
ATOM   4099 O  OD2  . ASP   B 1 22  ? 55.155 -28.596 -8.176  1.00 22.17 -1 22  ASP   B OD2  1 
ATOM   4100 H  H    . ASP   B 1 22  ? 51.635 -29.431 -11.208 1.00 20.50 ?  22  ASP   B H    1 
ATOM   4101 H  HA   . ASP   B 1 22  ? 51.436 -29.052 -8.567  1.00 19.51 ?  22  ASP   B HA   1 
ATOM   4102 H  HB2  . ASP   B 1 22  ? 53.464 -29.762 -9.509  1.00 21.36 ?  22  ASP   B HB2  1 
ATOM   4103 H  HB3  . ASP   B 1 22  ? 53.496 -28.480 -10.444 1.00 21.36 ?  22  ASP   B HB3  1 
ATOM   4104 N  N    . ILE   B 1 23  ? 50.608 -26.704 -8.434  1.00 14.07 ?  23  ILE   B N    1 
ATOM   4105 C  CA   . ILE   B 1 23  ? 50.025 -25.359 -8.482  1.00 13.33 ?  23  ILE   B CA   1 
ATOM   4106 C  C    . ILE   B 1 23  ? 51.088 -24.276 -8.623  1.00 13.03 ?  23  ILE   B C    1 
ATOM   4107 O  O    . ILE   B 1 23  ? 50.830 -23.230 -9.231  1.00 12.60 ?  23  ILE   B O    1 
ATOM   4108 C  CB   . ILE   B 1 23  ? 49.094 -25.117 -7.277  1.00 13.68 ?  23  ILE   B CB   1 
ATOM   4109 C  CG1  . ILE   B 1 23  ? 48.274 -23.841 -7.474  1.00 14.45 ?  23  ILE   B CG1  1 
ATOM   4110 C  CG2  . ILE   B 1 23  ? 49.866 -25.089 -5.972  1.00 14.49 ?  23  ILE   B CG2  1 
ATOM   4111 C  CD1  . ILE   B 1 23  ? 47.153 -23.677 -6.451  1.00 15.24 ?  23  ILE   B CD1  1 
ATOM   4112 H  H    . ILE   B 1 23  ? 50.450 -27.137 -7.709  1.00 16.88 ?  23  ILE   B H    1 
ATOM   4113 H  HA   . ILE   B 1 23  ? 49.473 -25.306 -9.273  1.00 15.99 ?  23  ILE   B HA   1 
ATOM   4114 H  HB   . ILE   B 1 23  ? 48.470 -25.860 -7.235  1.00 16.41 ?  23  ILE   B HB   1 
ATOM   4115 H  HG12 . ILE   B 1 23  ? 48.864 -23.075 -7.396  1.00 17.33 ?  23  ILE   B HG12 1 
ATOM   4116 H  HG13 . ILE   B 1 23  ? 47.873 -23.858 -8.359  1.00 17.33 ?  23  ILE   B HG13 1 
ATOM   4117 H  HG21 . ILE   B 1 23  ? 49.237 -25.088 -5.233  1.00 17.38 ?  23  ILE   B HG21 1 
ATOM   4118 H  HG22 . ILE   B 1 23  ? 50.430 -25.877 -5.924  1.00 17.38 ?  23  ILE   B HG22 1 
ATOM   4119 H  HG23 . ILE   B 1 23  ? 50.412 -24.289 -5.944  1.00 17.38 ?  23  ILE   B HG23 1 
ATOM   4120 H  HD11 . ILE   B 1 23  ? 46.629 -22.897 -6.684  1.00 18.28 ?  23  ILE   B HD11 1 
ATOM   4121 H  HD12 . ILE   B 1 23  ? 46.594 -24.471 -6.472  1.00 18.28 ?  23  ILE   B HD12 1 
ATOM   4122 H  HD13 . ILE   B 1 23  ? 47.543 -23.569 -5.572  1.00 18.28 ?  23  ILE   B HD13 1 
ATOM   4123 N  N    . VAL   B 1 24  ? 52.285 -24.485 -8.064  1.00 13.56 ?  24  VAL   B N    1 
ATOM   4124 C  CA   . VAL   B 1 24  ? 53.361 -23.504 -8.220  1.00 14.24 ?  24  VAL   B CA   1 
ATOM   4125 C  C    . VAL   B 1 24  ? 53.815 -23.447 -9.673  1.00 14.08 ?  24  VAL   B C    1 
ATOM   4126 O  O    . VAL   B 1 24  ? 53.951 -22.367 -10.259 1.00 14.61 ?  24  VAL   B O    1 
ATOM   4127 C  CB   . VAL   B 1 24  ? 54.536 -23.833 -7.277  1.00 15.06 ?  24  VAL   B CB   1 
ATOM   4128 C  CG1  . VAL   B 1 24  ? 55.759 -22.967 -7.600  1.00 16.29 ?  24  VAL   B CG1  1 
ATOM   4129 C  CG2  . VAL   B 1 24  ? 54.126 -23.650 -5.835  1.00 16.23 ?  24  VAL   B CG2  1 
ATOM   4130 H  H    . VAL   B 1 24  ? 52.496 -25.173 -7.594  1.00 16.26 ?  24  VAL   B H    1 
ATOM   4131 H  HA   . VAL   B 1 24  ? 53.025 -22.627 -7.977  1.00 17.08 ?  24  VAL   B HA   1 
ATOM   4132 H  HB   . VAL   B 1 24  ? 54.790 -24.761 -7.397  1.00 18.07 ?  24  VAL   B HB   1 
ATOM   4133 H  HG11 . VAL   B 1 24  ? 56.365 -22.981 -6.841  1.00 19.54 ?  24  VAL   B HG11 1 
ATOM   4134 H  HG12 . VAL   B 1 24  ? 56.203 -23.325 -8.383  1.00 19.54 ?  24  VAL   B HG12 1 
ATOM   4135 H  HG13 . VAL   B 1 24  ? 55.466 -22.057 -7.768  1.00 19.54 ?  24  VAL   B HG13 1 
ATOM   4136 H  HG21 . VAL   B 1 24  ? 54.846 -23.951 -5.260  1.00 19.48 ?  24  VAL   B HG21 1 
ATOM   4137 H  HG22 . VAL   B 1 24  ? 53.946 -22.710 -5.676  1.00 19.48 ?  24  VAL   B HG22 1 
ATOM   4138 H  HG23 . VAL   B 1 24  ? 53.326 -24.174 -5.666  1.00 19.48 ?  24  VAL   B HG23 1 
ATOM   4139 N  N    . GLU   B 1 25  ? 54.077 -24.613 -10.269 1.00 15.20 ?  25  GLU   B N    1 
ATOM   4140 C  CA   . GLU   B 1 25  ? 54.472 -24.640 -11.672 1.00 16.68 ?  25  GLU   B CA   1 
ATOM   4141 C  C    . GLU   B 1 25  ? 53.360 -24.101 -12.561 1.00 15.67 ?  25  GLU   B C    1 
ATOM   4142 O  O    . GLU   B 1 25  ? 53.626 -23.396 -13.542 1.00 16.85 ?  25  GLU   B O    1 
ATOM   4143 C  CB   . GLU   B 1 25  ? 54.879 -26.057 -12.073 1.00 21.02 ?  25  GLU   B CB   1 
ATOM   4144 C  CG   . GLU   B 1 25  ? 56.167 -26.511 -11.401 1.00 27.13 ?  25  GLU   B CG   1 
ATOM   4145 C  CD   . GLU   B 1 25  ? 57.292 -25.492 -11.526 1.00 32.40 ?  25  GLU   B CD   1 
ATOM   4146 O  OE1  . GLU   B 1 25  ? 57.652 -25.139 -12.669 1.00 34.48 ?  25  GLU   B OE1  1 
ATOM   4147 O  OE2  . GLU   B 1 25  ? 57.805 -25.025 -10.481 1.00 34.51 -1 25  GLU   B OE2  1 
ATOM   4148 H  H    . GLU   B 1 25  ? 54.027 -25.382 -9.888  1.00 18.23 ?  25  GLU   B H    1 
ATOM   4149 H  HA   . GLU   B 1 25  ? 55.227 -24.052 -11.791 1.00 20.01 ?  25  GLU   B HA   1 
ATOM   4150 H  HB2  . GLU   B 1 25  ? 54.174 -26.675 -11.816 1.00 25.22 ?  25  GLU   B HB2  1 
ATOM   4151 H  HB3  . GLU   B 1 25  ? 55.010 -26.088 -13.033 1.00 25.22 ?  25  GLU   B HB3  1 
ATOM   4152 H  HG2  . GLU   B 1 25  ? 56.001 -26.649 -10.460 1.00 32.56 ?  25  GLU   B HG2  1 
ATOM   4153 H  HG3  . GLU   B 1 25  ? 56.466 -27.333 -11.818 1.00 32.56 ?  25  GLU   B HG3  1 
ATOM   4154 N  N    A GLU   B 1 26  ? 52.106 -24.416 -12.231 0.68 14.50 ?  26  GLU   B N    1 
ATOM   4155 N  N    B GLU   B 1 26  ? 52.105 -24.415 -12.230 0.32 14.97 ?  26  GLU   B N    1 
ATOM   4156 C  CA   A GLU   B 1 26  ? 50.983 -23.889 -12.999 0.68 15.31 ?  26  GLU   B CA   1 
ATOM   4157 C  CA   B GLU   B 1 26  ? 50.980 -23.890 -12.998 0.32 15.21 ?  26  GLU   B CA   1 
ATOM   4158 C  C    A GLU   B 1 26  ? 50.932 -22.371 -12.920 0.68 14.50 ?  26  GLU   B C    1 
ATOM   4159 C  C    B GLU   B 1 26  ? 50.928 -22.372 -12.919 0.32 14.33 ?  26  GLU   B C    1 
ATOM   4160 O  O    A GLU   B 1 26  ? 50.736 -21.693 -13.934 0.68 15.54 ?  26  GLU   B O    1 
ATOM   4161 O  O    B GLU   B 1 26  ? 50.739 -21.692 -13.934 0.32 14.90 ?  26  GLU   B O    1 
ATOM   4162 C  CB   A GLU   B 1 26  ? 49.667 -24.472 -12.484 0.68 17.48 ?  26  GLU   B CB   1 
ATOM   4163 C  CB   B GLU   B 1 26  ? 49.666 -24.486 -12.490 0.32 16.61 ?  26  GLU   B CB   1 
ATOM   4164 C  CG   A GLU   B 1 26  ? 49.280 -25.791 -13.109 0.68 21.43 ?  26  GLU   B CG   1 
ATOM   4165 C  CG   B GLU   B 1 26  ? 49.235 -25.744 -13.213 0.32 18.83 ?  26  GLU   B CG   1 
ATOM   4166 C  CD   A GLU   B 1 26  ? 49.044 -25.708 -14.611 0.68 22.98 ?  26  GLU   B CD   1 
ATOM   4167 C  CD   B GLU   B 1 26  ? 48.915 -25.493 -14.686 0.32 19.26 ?  26  GLU   B CD   1 
ATOM   4168 O  OE1  A GLU   B 1 26  ? 48.218 -24.881 -15.054 0.68 22.98 ?  26  GLU   B OE1  1 
ATOM   4169 O  OE1  B GLU   B 1 26  ? 47.795 -25.023 -14.996 0.32 19.45 ?  26  GLU   B OE1  1 
ATOM   4170 O  OE2  A GLU   B 1 26  ? 49.685 -26.485 -15.345 0.68 24.24 -1 26  GLU   B OE2  1 
ATOM   4171 O  OE2  B GLU   B 1 26  ? 49.790 -25.750 -15.531 0.32 19.66 -1 26  GLU   B OE2  1 
ATOM   4172 H  H    A GLU   B 1 26  ? 51.879 -24.925 -11.571 0.68 17.40 ?  26  GLU   B H    1 
ATOM   4173 H  H    B GLU   B 1 26  ? 51.879 -24.922 -11.570 0.32 17.96 ?  26  GLU   B H    1 
ATOM   4174 H  HA   A GLU   B 1 26  ? 51.087 -24.138 -13.926 0.68 18.36 ?  26  GLU   B HA   1 
ATOM   4175 H  HA   B GLU   B 1 26  ? 51.090 -24.136 -13.927 0.32 18.24 ?  26  GLU   B HA   1 
ATOM   4176 H  HB2  A GLU   B 1 26  ? 49.744 -24.609 -11.523 0.68 20.97 ?  26  GLU   B HB2  1 
ATOM   4177 H  HB2  B GLU   B 1 26  ? 49.762 -24.699 -11.548 0.32 19.93 ?  26  GLU   B HB2  1 
ATOM   4178 H  HB3  A GLU   B 1 26  ? 48.955 -23.834 -12.661 0.68 20.97 ?  26  GLU   B HB3  1 
ATOM   4179 H  HB3  B GLU   B 1 26  ? 48.961 -23.827 -12.603 0.32 19.93 ?  26  GLU   B HB3  1 
ATOM   4180 H  HG2  A GLU   B 1 26  ? 49.999 -26.412 -12.960 0.68 25.71 ?  26  GLU   B HG2  1 
ATOM   4181 H  HG2  B GLU   B 1 26  ? 49.949 -26.398 -13.126 0.32 22.60 ?  26  GLU   B HG2  1 
ATOM   4182 H  HG3  A GLU   B 1 26  ? 48.464 -26.097 -12.691 0.68 25.71 ?  26  GLU   B HG3  1 
ATOM   4183 H  HG3  B GLU   B 1 26  ? 48.426 -26.077 -12.802 0.32 22.60 ?  26  GLU   B HG3  1 
ATOM   4184 N  N    . ALA   B 1 27  ? 51.079 -21.821 -11.713 1.00 13.35 ?  27  ALA   B N    1 
ATOM   4185 C  CA   . ALA   B 1 27  ? 51.045 -20.374 -11.561 1.00 13.94 ?  27  ALA   B CA   1 
ATOM   4186 C  C    . ALA   B 1 27  ? 52.125 -19.711 -12.406 1.00 14.90 ?  27  ALA   B C    1 
ATOM   4187 O  O    . ALA   B 1 27  ? 51.873 -18.701 -13.077 1.00 15.71 ?  27  ALA   B O    1 
ATOM   4188 C  CB   . ALA   B 1 27  ? 51.187 -20.002 -10.087 1.00 14.05 ?  27  ALA   B CB   1 
ATOM   4189 H  H    A ALA   B 1 27  ? 51.193 -22.257 -10.981 0.68 16.01 ?  27  ALA   B H    1 
ATOM   4190 H  H    B ALA   B 1 27  ? 51.198 -22.256 -10.981 0.32 16.01 ?  27  ALA   B H    1 
ATOM   4191 H  HA   . ALA   B 1 27  ? 50.190 -20.041 -11.867 1.00 16.73 ?  27  ALA   B HA   1 
ATOM   4192 H  HB1  . ALA   B 1 27  ? 51.156 -19.035 -9.998  1.00 16.86 ?  27  ALA   B HB1  1 
ATOM   4193 H  HB2  . ALA   B 1 27  ? 50.451 -20.399 -9.591  1.00 16.86 ?  27  ALA   B HB2  1 
ATOM   4194 H  HB3  . ALA   B 1 27  ? 52.030 -20.338 -9.752  1.00 16.86 ?  27  ALA   B HB3  1 
ATOM   4195 N  N    . LYS   B 1 28  ? 53.335 -20.272 -12.407 1.00 16.36 ?  28  LYS   B N    1 
ATOM   4196 C  CA   . LYS   B 1 28  ? 54.413 -19.655 -13.171 1.00 18.44 ?  28  LYS   B CA   1 
ATOM   4197 C  C    . LYS   B 1 28  ? 54.160 -19.734 -14.671 1.00 18.92 ?  28  LYS   B C    1 
ATOM   4198 O  O    . LYS   B 1 28  ? 54.580 -18.840 -15.415 1.00 20.28 ?  28  LYS   B O    1 
ATOM   4199 C  CB   . LYS   B 1 28  ? 55.766 -20.256 -12.776 1.00 21.75 ?  28  LYS   B CB   1 
ATOM   4200 C  CG   . LYS   B 1 28  ? 56.162 -19.903 -11.346 1.00 24.62 ?  28  LYS   B CG   1 
ATOM   4201 C  CD   . LYS   B 1 28  ? 57.591 -20.290 -11.003 1.00 29.46 ?  28  LYS   B CD   1 
ATOM   4202 C  CE   . LYS   B 1 28  ? 57.716 -21.764 -10.704 1.00 33.19 ?  28  LYS   B CE   1 
ATOM   4203 N  NZ   . LYS   B 1 28  ? 59.071 -22.098 -10.178 1.00 34.96 ?  28  LYS   B NZ   1 
ATOM   4204 H  H    . LYS   B 1 28  ? 53.551 -20.988 -11.985 1.00 19.63 ?  28  LYS   B H    1 
ATOM   4205 H  HA   . LYS   B 1 28  ? 54.447 -18.715 -12.947 1.00 22.12 ?  28  LYS   B HA   1 
ATOM   4206 H  HB2  . LYS   B 1 28  ? 55.720 -21.220 -12.844 1.00 26.09 ?  28  LYS   B HB2  1 
ATOM   4207 H  HB3  . LYS   B 1 28  ? 56.453 -19.911 -13.369 1.00 26.09 ?  28  LYS   B HB3  1 
ATOM   4208 H  HG2  . LYS   B 1 28  ? 56.070 -18.943 -11.226 1.00 29.54 ?  28  LYS   B HG2  1 
ATOM   4209 H  HG3  . LYS   B 1 28  ? 55.568 -20.367 -10.736 1.00 29.54 ?  28  LYS   B HG3  1 
ATOM   4210 H  HD2  . LYS   B 1 28  ? 58.164 -20.079 -11.756 1.00 35.35 ?  28  LYS   B HD2  1 
ATOM   4211 H  HD3  . LYS   B 1 28  ? 57.871 -19.792 -10.219 1.00 35.35 ?  28  LYS   B HD3  1 
ATOM   4212 H  HE2  . LYS   B 1 28  ? 57.059 -22.012 -10.034 1.00 39.82 ?  28  LYS   B HE2  1 
ATOM   4213 H  HE3  . LYS   B 1 28  ? 57.572 -22.270 -11.519 1.00 39.82 ?  28  LYS   B HE3  1 
ATOM   4214 H  HZ1  . LYS   B 1 28  ? 59.125 -22.969 -10.008 1.00 41.94 ?  28  LYS   B HZ1  1 
ATOM   4215 H  HZ2  . LYS   B 1 28  ? 59.691 -21.880 -10.778 1.00 41.94 ?  28  LYS   B HZ2  1 
ATOM   4216 H  HZ3  . LYS   B 1 28  ? 59.225 -21.646 -9.426  1.00 41.94 ?  28  LYS   B HZ3  1 
ATOM   4217 N  N    . LYS   B 1 29  ? 53.449 -20.764 -15.130 1.00 19.91 ?  29  LYS   B N    1 
ATOM   4218 C  CA   . LYS   B 1 29  ? 53.159 -20.904 -16.553 1.00 22.93 ?  29  LYS   B CA   1 
ATOM   4219 C  C    . LYS   B 1 29  ? 51.912 -20.138 -16.987 1.00 21.92 ?  29  LYS   B C    1 
ATOM   4220 O  O    . LYS   B 1 29  ? 51.907 -19.526 -18.061 1.00 23.32 ?  29  LYS   B O    1 
ATOM   4221 C  CB   . LYS   B 1 29  ? 53.016 -22.385 -16.914 1.00 27.97 ?  29  LYS   B CB   1 
ATOM   4222 C  CG   . LYS   B 1 29  ? 52.846 -22.650 -18.398 1.00 33.06 ?  29  LYS   B CG   1 
ATOM   4223 C  CD   . LYS   B 1 29  ? 53.065 -24.122 -18.726 1.00 36.97 ?  29  LYS   B CD   1 
ATOM   4224 C  CE   . LYS   B 1 29  ? 51.975 -25.006 -18.137 1.00 39.73 ?  29  LYS   B CE   1 
ATOM   4225 N  NZ   . LYS   B 1 29  ? 52.202 -26.446 -18.455 1.00 41.41 ?  29  LYS   B NZ   1 
ATOM   4226 H  H    . LYS   B 1 29  ? 53.121 -21.393 -14.633 1.00 23.88 ?  29  LYS   B H    1 
ATOM   4227 H  HA   . LYS   B 1 29  ? 53.908 -20.556 -17.052 1.00 27.51 ?  29  LYS   B HA   1 
ATOM   4228 H  HB2  . LYS   B 1 29  ? 53.817 -22.854 -16.625 1.00 33.56 ?  29  LYS   B HB2  1 
ATOM   4229 H  HB3  . LYS   B 1 29  ? 52.243 -22.747 -16.461 1.00 33.56 ?  29  LYS   B HB3  1 
ATOM   4230 H  HG2  . LYS   B 1 29  ? 51.945 -22.407 -18.664 1.00 39.67 ?  29  LYS   B HG2  1 
ATOM   4231 H  HG3  . LYS   B 1 29  ? 53.495 -22.126 -18.895 1.00 39.67 ?  29  LYS   B HG3  1 
ATOM   4232 H  HD2  . LYS   B 1 29  ? 53.061 -24.239 -19.688 1.00 44.36 ?  29  LYS   B HD2  1 
ATOM   4233 H  HD3  . LYS   B 1 29  ? 53.916 -24.408 -18.357 1.00 44.36 ?  29  LYS   B HD3  1 
ATOM   4234 H  HE2  . LYS   B 1 29  ? 51.966 -24.908 -17.172 1.00 47.67 ?  29  LYS   B HE2  1 
ATOM   4235 H  HE3  . LYS   B 1 29  ? 51.117 -24.745 -18.508 1.00 47.67 ?  29  LYS   B HE3  1 
ATOM   4236 H  HZ1  . LYS   B 1 29  ? 51.553 -26.943 -18.102 1.00 49.69 ?  29  LYS   B HZ1  1 
ATOM   4237 H  HZ2  . LYS   B 1 29  ? 52.209 -26.566 -19.337 1.00 49.69 ?  29  LYS   B HZ2  1 
ATOM   4238 H  HZ3  . LYS   B 1 29  ? 52.983 -26.712 -18.121 1.00 49.69 ?  29  LYS   B HZ3  1 
ATOM   4239 N  N    . VAL   B 1 30  ? 50.854 -20.169 -16.172 1.00 20.25 ?  30  VAL   B N    1 
ATOM   4240 C  CA   . VAL   B 1 30  ? 49.567 -19.570 -16.539 1.00 20.49 ?  30  VAL   B CA   1 
ATOM   4241 C  C    . VAL   B 1 30  ? 49.575 -18.056 -16.371 1.00 19.43 ?  30  VAL   B C    1 
ATOM   4242 O  O    . VAL   B 1 30  ? 48.840 -17.339 -17.070 1.00 20.52 ?  30  VAL   B O    1 
ATOM   4243 C  CB   . VAL   B 1 30  ? 48.454 -20.203 -15.680 1.00 21.85 ?  30  VAL   B CB   1 
ATOM   4244 C  CG1  . VAL   B 1 30  ? 47.162 -19.401 -15.764 1.00 22.35 ?  30  VAL   B CG1  1 
ATOM   4245 C  CG2  . VAL   B 1 30  ? 48.228 -21.650 -16.088 1.00 22.92 ?  30  VAL   B CG2  1 
ATOM   4246 H  H    . VAL   B 1 30  ? 50.848 -20.559 -15.396 1.00 24.30 ?  30  VAL   B H    1 
ATOM   4247 H  HA   . VAL   B 1 30  ? 49.379 -19.783 -17.464 1.00 24.58 ?  30  VAL   B HA   1 
ATOM   4248 H  HB   . VAL   B 1 30  ? 48.736 -20.212 -14.752 1.00 26.21 ?  30  VAL   B HB   1 
ATOM   4249 H  HG11 . VAL   B 1 30  ? 46.420 -19.989 -15.546 1.00 26.82 ?  30  VAL   B HG11 1 
ATOM   4250 H  HG12 . VAL   B 1 30  ? 47.199 -18.673 -15.127 1.00 26.82 ?  30  VAL   B HG12 1 
ATOM   4251 H  HG13 . VAL   B 1 30  ? 47.054 -19.066 -16.662 1.00 26.82 ?  30  VAL   B HG13 1 
ATOM   4252 H  HG21 . VAL   B 1 30  ? 47.532 -22.035 -15.528 1.00 27.50 ?  30  VAL   B HG21 1 
ATOM   4253 H  HG22 . VAL   B 1 30  ? 47.951 -21.678 -17.018 1.00 27.50 ?  30  VAL   B HG22 1 
ATOM   4254 H  HG23 . VAL   B 1 30  ? 49.052 -22.146 -15.973 1.00 27.50 ?  30  VAL   B HG23 1 
ATOM   4255 N  N    . LYS   B 1 31  ? 50.357 -17.562 -15.428 1.00 19.07 ?  31  LYS   B N    1 
ATOM   4256 C  CA   . LYS   B 1 31  ? 50.381 -16.155 -15.065 1.00 19.51 ?  31  LYS   B CA   1 
ATOM   4257 C  C    . LYS   B 1 31  ? 48.980 -15.684 -14.680 1.00 17.51 ?  31  LYS   B C    1 
ATOM   4258 O  O    . LYS   B 1 31  ? 48.441 -14.759 -15.296 1.00 18.27 ?  31  LYS   B O    1 
ATOM   4259 C  CB   . LYS   B 1 31  ? 51.013 -15.341 -16.200 1.00 22.99 ?  31  LYS   B CB   1 
ATOM   4260 C  CG   . LYS   B 1 31  ? 52.444 -15.784 -16.514 1.00 26.29 ?  31  LYS   B CG   1 
ATOM   4261 C  CD   . LYS   B 1 31  ? 53.022 -15.051 -17.711 1.00 29.67 ?  31  LYS   B CD   1 
ATOM   4262 C  CE   . LYS   B 1 31  ? 54.502 -15.317 -17.859 1.00 32.05 ?  31  LYS   B CE   1 
ATOM   4263 N  NZ   . LYS   B 1 31  ? 55.228 -14.891 -16.633 1.00 33.32 ?  31  LYS   B NZ   1 
ATOM   4264 H  H    . LYS   B 1 31  ? 50.904 -18.051 -14.979 1.00 22.88 ?  31  LYS   B H    1 
ATOM   4265 H  HA   . LYS   B 1 31  ? 50.942 -16.067 -14.291 1.00 23.40 ?  31  LYS   B HA   1 
ATOM   4266 H  HB2  . LYS   B 1 31  ? 50.489 -15.448 -17.010 1.00 27.58 ?  31  LYS   B HB2  1 
ATOM   4267 H  HB3  . LYS   B 1 31  ? 51.043 -14.412 -15.938 1.00 27.58 ?  31  LYS   B HB3  1 
ATOM   4268 H  HG2  . LYS   B 1 31  ? 53.003 -15.607 -15.741 1.00 31.54 ?  31  LYS   B HG2  1 
ATOM   4269 H  HG3  . LYS   B 1 31  ? 52.450 -16.737 -16.712 1.00 31.54 ?  31  LYS   B HG3  1 
ATOM   4270 H  HD2  . LYS   B 1 31  ? 52.573 -15.357 -18.513 1.00 35.60 ?  31  LYS   B HD2  1 
ATOM   4271 H  HD3  . LYS   B 1 31  ? 52.892 -14.101 -17.589 1.00 35.60 ?  31  LYS   B HD3  1 
ATOM   4272 H  HE2  . LYS   B 1 31  ? 54.652 -16.268 -17.991 1.00 38.45 ?  31  LYS   B HE2  1 
ATOM   4273 H  HE3  . LYS   B 1 31  ? 54.847 -14.813 -18.613 1.00 38.45 ?  31  LYS   B HE3  1 
ATOM   4274 H  HZ1  . LYS   B 1 31  ? 56.103 -14.882 -16.785 1.00 39.98 ?  31  LYS   B HZ1  1 
ATOM   4275 H  HZ2  . LYS   B 1 31  ? 54.964 -14.075 -16.395 1.00 39.98 ?  31  LYS   B HZ2  1 
ATOM   4276 H  HZ3  . LYS   B 1 31  ? 55.055 -15.456 -15.966 1.00 39.98 ?  31  LYS   B HZ3  1 
ATOM   4277 N  N    . PRO   B 1 32  ? 48.368 -16.284 -13.655 1.00 14.93 ?  32  PRO   B N    1 
ATOM   4278 C  CA   . PRO   B 1 32  ? 46.991 -15.923 -13.305 1.00 13.85 ?  32  PRO   B CA   1 
ATOM   4279 C  C    . PRO   B 1 32  ? 46.915 -14.577 -12.605 1.00 14.04 ?  32  PRO   B C    1 
ATOM   4280 O  O    . PRO   B 1 32  ? 47.844 -14.153 -11.909 1.00 15.79 ?  32  PRO   B O    1 
ATOM   4281 C  CB   . PRO   B 1 32  ? 46.579 -17.036 -12.338 1.00 14.20 ?  32  PRO   B CB   1 
ATOM   4282 C  CG   . PRO   B 1 32  ? 47.873 -17.387 -11.653 1.00 14.32 ?  32  PRO   B CG   1 
ATOM   4283 C  CD   . PRO   B 1 32  ? 48.931 -17.275 -12.717 1.00 14.70 ?  32  PRO   B CD   1 
ATOM   4284 H  HA   . PRO   B 1 32  ? 46.410 -15.934 -14.091 1.00 16.61 ?  32  PRO   B HA   1 
ATOM   4285 H  HB2  . PRO   B 1 32  ? 45.930 -16.701 -11.700 1.00 17.04 ?  32  PRO   B HB2  1 
ATOM   4286 H  HB3  . PRO   B 1 32  ? 46.230 -17.797 -12.826 1.00 17.04 ?  32  PRO   B HB3  1 
ATOM   4287 H  HG2  . PRO   B 1 32  ? 48.044 -16.758 -10.931 1.00 17.18 ?  32  PRO   B HG2  1 
ATOM   4288 H  HG3  . PRO   B 1 32  ? 47.831 -18.295 -11.310 1.00 17.18 ?  32  PRO   B HG3  1 
ATOM   4289 H  HD2  . PRO   B 1 32  ? 49.756 -16.939 -12.342 1.00 17.64 ?  32  PRO   B HD2  1 
ATOM   4290 H  HD3  . PRO   B 1 32  ? 49.053 -18.123 -13.163 1.00 17.64 ?  32  PRO   B HD3  1 
ATOM   4291 N  N    . THR   B 1 33  ? 45.761 -13.924 -12.768 1.00 13.77 ?  33  THR   B N    1 
ATOM   4292 C  CA   . THR   B 1 33  ? 45.468 -12.747 -11.962 1.00 14.18 ?  33  THR   B CA   1 
ATOM   4293 C  C    . THR   B 1 33  ? 45.424 -13.099 -10.480 1.00 13.41 ?  33  THR   B C    1 
ATOM   4294 O  O    . THR   B 1 33  ? 45.895 -12.320 -9.639  1.00 14.36 ?  33  THR   B O    1 
ATOM   4295 C  CB   . THR   B 1 33  ? 44.149 -12.111 -12.404 1.00 14.73 ?  33  THR   B CB   1 
ATOM   4296 O  OG1  . THR   B 1 33  ? 44.184 -11.855 -13.811 1.00 14.76 ?  33  THR   B OG1  1 
ATOM   4297 C  CG2  . THR   B 1 33  ? 43.913 -10.806 -11.659 1.00 16.01 ?  33  THR   B CG2  1 
ATOM   4298 H  H    . THR   B 1 33  ? 45.138 -14.145 -13.327 1.00 16.52 ?  33  THR   B H    1 
ATOM   4299 H  HA   . THR   B 1 33  ? 46.170 -12.097 -12.096 1.00 17.01 ?  33  THR   B HA   1 
ATOM   4300 H  HB   . THR   B 1 33  ? 43.413 -12.718 -12.207 1.00 17.67 ?  33  THR   B HB   1 
ATOM   4301 H  HG1  . THR   B 1 33  ? 43.462 -11.488 -14.055 1.00 17.71 ?  33  THR   B HG1  1 
ATOM   4302 H  HG21 . THR   B 1 33  ? 43.165 -10.335 -12.047 1.00 19.21 ?  33  THR   B HG21 1 
ATOM   4303 H  HG22 . THR   B 1 33  ? 43.726 -10.987 -10.724 1.00 19.21 ?  33  THR   B HG22 1 
ATOM   4304 H  HG23 . THR   B 1 33  ? 44.707 -10.249 -11.719 1.00 19.21 ?  33  THR   B HG23 1 
ATOM   4305 N  N    . VAL   B 1 34  ? 44.868 -14.264 -10.138 1.00 12.74 ?  34  VAL   B N    1 
ATOM   4306 C  CA   . VAL   B 1 34  ? 44.684 -14.664 -8.746  1.00 12.07 ?  34  VAL   B CA   1 
ATOM   4307 C  C    . VAL   B 1 34  ? 45.106 -16.116 -8.582  1.00 10.92 ?  34  VAL   B C    1 
ATOM   4308 O  O    . VAL   B 1 34  ? 44.582 -17.001 -9.267  1.00 12.21 ?  34  VAL   B O    1 
ATOM   4309 C  CB   . VAL   B 1 34  ? 43.215 -14.519 -8.290  1.00 13.18 ?  34  VAL   B CB   1 
ATOM   4310 C  CG1  . VAL   B 1 34  ? 43.058 -14.984 -6.850  1.00 13.62 ?  34  VAL   B CG1  1 
ATOM   4311 C  CG2  . VAL   B 1 34  ? 42.720 -13.094 -8.467  1.00 14.28 ?  34  VAL   B CG2  1 
ATOM   4312 H  H    . VAL   B 1 34  ? 44.590 -14.853 -10.704 1.00 15.28 ?  34  VAL   B H    1 
ATOM   4313 H  HA   . VAL   B 1 34  ? 45.238 -14.114 -8.170  1.00 14.48 ?  34  VAL   B HA   1 
ATOM   4314 H  HB   . VAL   B 1 34  ? 42.661 -15.089 -8.846  1.00 15.82 ?  34  VAL   B HB   1 
ATOM   4315 H  HG11 . VAL   B 1 34  ? 42.211 -14.657 -6.504  1.00 16.34 ?  34  VAL   B HG11 1 
ATOM   4316 H  HG12 . VAL   B 1 34  ? 43.068 -15.954 -6.826  1.00 16.34 ?  34  VAL   B HG12 1 
ATOM   4317 H  HG13 . VAL   B 1 34  ? 43.788 -14.629 -6.322  1.00 16.34 ?  34  VAL   B HG13 1 
ATOM   4318 H  HG21 . VAL   B 1 34  ? 41.802 -13.036 -8.152  1.00 17.13 ?  34  VAL   B HG21 1 
ATOM   4319 H  HG22 . VAL   B 1 34  ? 43.283 -12.495 -7.956  1.00 17.13 ?  34  VAL   B HG22 1 
ATOM   4320 H  HG23 . VAL   B 1 34  ? 42.757 -12.860 -9.410  1.00 17.13 ?  34  VAL   B HG23 1 
ATOM   4321 N  N    . VAL   B 1 35  ? 46.011 -16.370 -7.643  1.00 11.00 ?  35  VAL   B N    1 
ATOM   4322 C  CA   . VAL   B 1 35  ? 46.244 -17.715 -7.134  1.00 10.84 ?  35  VAL   B CA   1 
ATOM   4323 C  C    . VAL   B 1 35  ? 45.716 -17.771 -5.710  1.00 10.16 ?  35  VAL   B C    1 
ATOM   4324 O  O    . VAL   B 1 35  ? 45.940 -16.849 -4.919  1.00 10.78 ?  35  VAL   B O    1 
ATOM   4325 C  CB   . VAL   B 1 35  ? 47.727 -18.139 -7.222  1.00 11.23 ?  35  VAL   B CB   1 
ATOM   4326 C  CG1  . VAL   B 1 35  ? 48.624 -17.302 -6.304  1.00 12.20 ?  35  VAL   B CG1  1 
ATOM   4327 C  CG2  . VAL   B 1 35  ? 47.870 -19.632 -6.899  1.00 12.34 ?  35  VAL   B CG2  1 
ATOM   4328 H  H    . VAL   B 1 35  ? 46.512 -15.770 -7.282  1.00 13.20 ?  35  VAL   B H    1 
ATOM   4329 H  HA   . VAL   B 1 35  ? 45.725 -18.343 -7.661  1.00 13.01 ?  35  VAL   B HA   1 
ATOM   4330 H  HB   . VAL   B 1 35  ? 48.030 -18.013 -8.139  1.00 13.47 ?  35  VAL   B HB   1 
ATOM   4331 H  HG11 . VAL   B 1 35  ? 49.548 -17.516 -6.498  1.00 14.64 ?  35  VAL   B HG11 1 
ATOM   4332 H  HG12 . VAL   B 1 35  ? 48.450 -16.368 -6.470  1.00 14.64 ?  35  VAL   B HG12 1 
ATOM   4333 H  HG13 . VAL   B 1 35  ? 48.417 -17.526 -5.383  1.00 14.64 ?  35  VAL   B HG13 1 
ATOM   4334 H  HG21 . VAL   B 1 35  ? 48.789 -19.903 -7.019  1.00 14.80 ?  35  VAL   B HG21 1 
ATOM   4335 H  HG22 . VAL   B 1 35  ? 47.594 -19.787 -5.978  1.00 14.80 ?  35  VAL   B HG22 1 
ATOM   4336 H  HG23 . VAL   B 1 35  ? 47.294 -20.149 -7.496  1.00 14.80 ?  35  VAL   B HG23 1 
ATOM   4337 N  N    . VAL   B 1 36  ? 45.000 -18.847 -5.390  1.00 10.23 ?  36  VAL   B N    1 
ATOM   4338 C  CA   . VAL   B 1 36  ? 44.454 -19.049 -4.058  1.00 10.10 ?  36  VAL   B CA   1 
ATOM   4339 C  C    . VAL   B 1 36  ? 45.457 -19.815 -3.206  1.00 9.81  ?  36  VAL   B C    1 
ATOM   4340 O  O    . VAL   B 1 36  ? 45.994 -20.850 -3.628  1.00 10.97 ?  36  VAL   B O    1 
ATOM   4341 C  CB   . VAL   B 1 36  ? 43.115 -19.808 -4.126  1.00 10.50 ?  36  VAL   B CB   1 
ATOM   4342 C  CG1  . VAL   B 1 36  ? 42.622 -20.171 -2.730  1.00 11.22 ?  36  VAL   B CG1  1 
ATOM   4343 C  CG2  . VAL   B 1 36  ? 42.088 -18.982 -4.876  1.00 10.99 ?  36  VAL   B CG2  1 
ATOM   4344 H  H    . VAL   B 1 36  ? 44.827 -19.487 -5.939  1.00 12.27 ?  36  VAL   B H    1 
ATOM   4345 H  HA   . VAL   B 1 36  ? 44.297 -18.189 -3.641  1.00 12.11 ?  36  VAL   B HA   1 
ATOM   4346 H  HB   . VAL   B 1 36  ? 43.249 -20.634 -4.617  1.00 12.60 ?  36  VAL   B HB   1 
ATOM   4347 H  HG11 . VAL   B 1 36  ? 41.681 -20.396 -2.780  1.00 13.46 ?  36  VAL   B HG11 1 
ATOM   4348 H  HG12 . VAL   B 1 36  ? 43.129 -20.923 -2.397  1.00 13.46 ?  36  VAL   B HG12 1 
ATOM   4349 H  HG13 . VAL   B 1 36  ? 42.744 -19.401 -2.146  1.00 13.46 ?  36  VAL   B HG13 1 
ATOM   4350 H  HG21 . VAL   B 1 36  ? 41.247 -19.461 -4.892  1.00 13.18 ?  36  VAL   B HG21 1 
ATOM   4351 H  HG22 . VAL   B 1 36  ? 41.979 -18.129 -4.428  1.00 13.18 ?  36  VAL   B HG22 1 
ATOM   4352 H  HG23 . VAL   B 1 36  ? 42.403 -18.838 -5.786  1.00 13.18 ?  36  VAL   B HG23 1 
ATOM   4353 N  N    . ASN   B 1 37  ? 45.680 -19.323 -1.993  1.00 10.23 ?  37  ASN   B N    1 
ATOM   4354 C  CA   . ASN   B 1 37  ? 46.439 -20.043 -0.984  1.00 10.13 ?  37  ASN   B CA   1 
ATOM   4355 C  C    . ASN   B 1 37  ? 45.492 -20.716 0.005   1.00 10.60 ?  37  ASN   B C    1 
ATOM   4356 O  O    . ASN   B 1 37  ? 44.486 -20.136 0.420   1.00 11.13 ?  37  ASN   B O    1 
ATOM   4357 C  CB   . ASN   B 1 37  ? 47.367 -19.091 -0.226  1.00 10.18 ?  37  ASN   B CB   1 
ATOM   4358 C  CG   . ASN   B 1 37  ? 48.226 -19.807 0.790   1.00 10.71 ?  37  ASN   B CG   1 
ATOM   4359 O  OD1  . ASN   B 1 37  ? 48.568 -20.983 0.610   1.00 11.85 ?  37  ASN   B OD1  1 
ATOM   4360 N  ND2  . ASN   B 1 37  ? 48.572 -19.116 1.865   1.00 10.96 ?  37  ASN   B ND2  1 
ATOM   4361 H  H    . ASN   B 1 37  ? 45.394 -18.556 -1.718  1.00 12.27 ?  37  ASN   B H    1 
ATOM   4362 H  HA   . ASN   B 1 37  ? 46.977 -20.731 -1.401  1.00 12.15 ?  37  ASN   B HA   1 
ATOM   4363 H  HB2  . ASN   B 1 37  ? 47.958 -18.660 -0.861  1.00 12.22 ?  37  ASN   B HB2  1 
ATOM   4364 H  HB3  . ASN   B 1 37  ? 46.836 -18.430 0.242   1.00 12.22 ?  37  ASN   B HB3  1 
ATOM   4365 H  HD21 . ASN   B 1 37  ? 49.061 -19.476 2.475   1.00 13.15 ?  37  ASN   B HD21 1 
ATOM   4366 H  HD22 . ASN   B 1 37  ? 48.315 -18.302 1.960   1.00 13.15 ?  37  ASN   B HD22 1 
ATOM   4367 N  N    . ALA   B 1 38  ? 45.843 -21.948 0.389   1.00 10.65 ?  38  ALA   B N    1 
ATOM   4368 C  CA   . ALA   B 1 38  ? 45.191 -22.688 1.474   1.00 10.99 ?  38  ALA   B CA   1 
ATOM   4369 C  C    . ALA   B 1 38  ? 45.785 -22.204 2.798   1.00 10.75 ?  38  ALA   B C    1 
ATOM   4370 O  O    . ALA   B 1 38  ? 46.691 -22.813 3.379   1.00 11.87 ?  38  ALA   B O    1 
ATOM   4371 C  CB   . ALA   B 1 38  ? 45.408 -24.186 1.286   1.00 12.09 ?  38  ALA   B CB   1 
ATOM   4372 H  H    . ALA   B 1 38  ? 46.491 -22.387 0.036   1.00 12.77 ?  38  ALA   B H    1 
ATOM   4373 H  HA   . ALA   B 1 38  ? 44.238 -22.506 1.474   1.00 13.18 ?  38  ALA   B HA   1 
ATOM   4374 H  HB1  . ALA   B 1 38  ? 44.963 -24.663 2.016   1.00 14.50 ?  38  ALA   B HB1  1 
ATOM   4375 H  HB2  . ALA   B 1 38  ? 45.021 -24.457 0.441   1.00 14.50 ?  38  ALA   B HB2  1 
ATOM   4376 H  HB3  . ALA   B 1 38  ? 46.354 -24.376 1.302   1.00 14.50 ?  38  ALA   B HB3  1 
ATOM   4377 N  N    . ALA   B 1 39  ? 45.266 -21.065 3.269   1.00 10.91 ?  39  ALA   B N    1 
ATOM   4378 C  CA   . ALA   B 1 39  ? 45.817 -20.328 4.397   1.00 11.37 ?  39  ALA   B CA   1 
ATOM   4379 C  C    . ALA   B 1 39  ? 45.204 -20.775 5.721   1.00 11.02 ?  39  ALA   B C    1 
ATOM   4380 O  O    . ALA   B 1 39  ? 44.174 -21.452 5.772   1.00 12.08 ?  39  ALA   B O    1 
ATOM   4381 C  CB   . ALA   B 1 39  ? 45.565 -18.829 4.209   1.00 12.03 ?  39  ALA   B CB   1 
ATOM   4382 H  H    . ALA   B 1 39  ? 44.567 -20.693 2.934   1.00 13.08 ?  39  ALA   B H    1 
ATOM   4383 H  HA   . ALA   B 1 39  ? 46.773 -20.469 4.437   1.00 13.64 ?  39  ALA   B HA   1 
ATOM   4384 H  HB1  . ALA   B 1 39  ? 45.935 -18.346 4.965   1.00 14.43 ?  39  ALA   B HB1  1 
ATOM   4385 H  HB2  . ALA   B 1 39  ? 45.991 -18.533 3.388   1.00 14.43 ?  39  ALA   B HB2  1 
ATOM   4386 H  HB3  . ALA   B 1 39  ? 44.607 -18.670 4.156   1.00 14.43 ?  39  ALA   B HB3  1 
ATOM   4387 N  N    . ASN   B 1 40  ? 45.851 -20.359 6.805   1.00 11.97 ?  40  ASN   B N    1 
ATOM   4388 C  CA   . ASN   B 1 40  ? 45.292 -20.404 8.147   1.00 12.55 ?  40  ASN   B CA   1 
ATOM   4389 C  C    . ASN   B 1 40  ? 45.110 -18.975 8.667   1.00 12.23 ?  40  ASN   B C    1 
ATOM   4390 O  O    . ASN   B 1 40  ? 45.517 -17.998 8.030   1.00 12.27 ?  40  ASN   B O    1 
ATOM   4391 C  CB   . ASN   B 1 40  ? 46.145 -21.271 9.087   1.00 13.56 ?  40  ASN   B CB   1 
ATOM   4392 C  CG   . ASN   B 1 40  ? 47.599 -20.866 9.099   1.00 14.68 ?  40  ASN   B CG   1 
ATOM   4393 O  OD1  . ASN   B 1 40  ? 47.916 -19.686 9.183   1.00 16.59 ?  40  ASN   B OD1  1 
ATOM   4394 N  ND2  . ASN   B 1 40  ? 48.494 -21.838 9.023   1.00 14.72 ?  40  ASN   B ND2  1 
ATOM   4395 H  H    . ASN   B 1 40  ? 46.651 -20.042 6.785   1.00 14.36 ?  40  ASN   B H    1 
ATOM   4396 H  HA   . ASN   B 1 40  ? 44.411 -20.807 8.105   1.00 15.05 ?  40  ASN   B HA   1 
ATOM   4397 H  HB2  . ASN   B 1 40  ? 45.804 -21.188 9.993   1.00 16.27 ?  40  ASN   B HB2  1 
ATOM   4398 H  HB3  . ASN   B 1 40  ? 46.094 -22.195 8.798   1.00 16.27 ?  40  ASN   B HB3  1 
ATOM   4399 H  HD21 . ASN   B 1 40  ? 49.334 -21.653 9.029   1.00 17.65 ?  40  ASN   B HD21 1 
ATOM   4400 H  HD22 . ASN   B 1 40  ? 48.234 -22.655 8.967   1.00 17.65 ?  40  ASN   B HD22 1 
ATOM   4401 N  N    . VAL   B 1 41  ? 44.461 -18.848 9.827   1.00 13.07 ?  41  VAL   B N    1 
ATOM   4402 C  CA   . VAL   B 1 41  ? 44.003 -17.528 10.276  1.00 13.54 ?  41  VAL   B CA   1 
ATOM   4403 C  C    . VAL   B 1 41  ? 45.153 -16.573 10.563  1.00 13.27 ?  41  VAL   B C    1 
ATOM   4404 O  O    . VAL   B 1 41  ? 44.971 -15.353 10.478  1.00 13.82 ?  41  VAL   B O    1 
ATOM   4405 C  CB   . VAL   B 1 41  ? 43.028 -17.606 11.472  1.00 15.34 ?  41  VAL   B CB   1 
ATOM   4406 C  CG1  . VAL   B 1 41  ? 41.725 -18.286 11.072  1.00 15.33 ?  41  VAL   B CG1  1 
ATOM   4407 C  CG2  . VAL   B 1 41  ? 43.674 -18.292 12.667  1.00 16.37 ?  41  VAL   B CG2  1 
ATOM   4408 H  H    . VAL   B 1 41  ? 44.271 -19.494 10.358  1.00 15.68 ?  41  VAL   B H    1 
ATOM   4409 H  HA   . VAL   B 1 41  ? 43.499 -17.135 9.546   1.00 16.24 ?  41  VAL   B HA   1 
ATOM   4410 H  HB   . VAL   B 1 41  ? 42.804 -16.702 11.745  1.00 18.41 ?  41  VAL   B HB   1 
ATOM   4411 H  HG11 . VAL   B 1 41  ? 41.124 -18.295 11.837  1.00 18.39 ?  41  VAL   B HG11 1 
ATOM   4412 H  HG12 . VAL   B 1 41  ? 41.319 -17.791 10.343  1.00 18.39 ?  41  VAL   B HG12 1 
ATOM   4413 H  HG13 . VAL   B 1 41  ? 41.914 -19.194 10.791  1.00 18.39 ?  41  VAL   B HG13 1 
ATOM   4414 H  HG21 . VAL   B 1 41  ? 43.037 -18.323 13.397  1.00 19.64 ?  41  VAL   B HG21 1 
ATOM   4415 H  HG22 . VAL   B 1 41  ? 43.929 -19.194 12.414  1.00 19.64 ?  41  VAL   B HG22 1 
ATOM   4416 H  HG23 . VAL   B 1 41  ? 44.459 -17.789 12.932  1.00 19.64 ?  41  VAL   B HG23 1 
ATOM   4417 N  N    . TYR   B 1 42  ? 46.329 -17.085 10.929  1.00 13.57 ?  42  TYR   B N    1 
ATOM   4418 C  CA   . TYR   B 1 42  ? 47.484 -16.235 11.193  1.00 13.89 ?  42  TYR   B CA   1 
ATOM   4419 C  C    . TYR   B 1 42  ? 48.444 -16.163 10.011  1.00 13.24 ?  42  TYR   B C    1 
ATOM   4420 O  O    . TYR   B 1 42  ? 49.537 -15.600 10.141  1.00 14.56 ?  42  TYR   B O    1 
ATOM   4421 C  CB   . TYR   B 1 42  ? 48.189 -16.640 12.492  1.00 15.74 ?  42  TYR   B CB   1 
ATOM   4422 C  CG   . TYR   B 1 42  ? 47.581 -15.965 13.713  1.00 16.25 ?  42  TYR   B CG   1 
ATOM   4423 C  CD1  . TYR   B 1 42  ? 47.795 -14.612 13.954  1.00 15.67 ?  42  TYR   B CD1  1 
ATOM   4424 C  CD2  . TYR   B 1 42  ? 46.790 -16.669 14.609  1.00 18.24 ?  42  TYR   B CD2  1 
ATOM   4425 C  CE1  . TYR   B 1 42  ? 47.240 -13.980 15.046  1.00 16.73 ?  42  TYR   B CE1  1 
ATOM   4426 C  CE2  . TYR   B 1 42  ? 46.232 -16.044 15.713  1.00 18.62 ?  42  TYR   B CE2  1 
ATOM   4427 C  CZ   . TYR   B 1 42  ? 46.463 -14.695 15.927  1.00 18.69 ?  42  TYR   B CZ   1 
ATOM   4428 O  OH   . TYR   B 1 42  ? 45.922 -14.052 17.021  1.00 21.71 ?  42  TYR   B OH   1 
ATOM   4429 H  H    . TYR   B 1 42  ? 46.478 -17.931 11.028  1.00 16.27 ?  42  TYR   B H    1 
ATOM   4430 H  HA   . TYR   B 1 42  ? 47.152 -15.338 11.328  1.00 16.67 ?  42  TYR   B HA   1 
ATOM   4431 H  HB2  . TYR   B 1 42  ? 48.113 -17.598 12.610  1.00 18.88 ?  42  TYR   B HB2  1 
ATOM   4432 H  HB3  . TYR   B 1 42  ? 49.120 -16.380 12.436  1.00 18.88 ?  42  TYR   B HB3  1 
ATOM   4433 H  HD1  . TYR   B 1 42  ? 48.321 -14.123 13.356  1.00 18.80 ?  42  TYR   B HD1  1 
ATOM   4434 H  HD2  . TYR   B 1 42  ? 46.631 -17.575 14.461  1.00 21.89 ?  42  TYR   B HD2  1 
ATOM   4435 H  HE1  . TYR   B 1 42  ? 47.403 -13.077 15.190  1.00 20.07 ?  42  TYR   B HE1  1 
ATOM   4436 H  HE2  . TYR   B 1 42  ? 45.707 -16.531 16.304  1.00 22.34 ?  42  TYR   B HE2  1 
ATOM   4437 H  HH   . TYR   B 1 42  ? 46.153 -13.248 17.013  1.00 26.05 ?  42  TYR   B HH   1 
ATOM   4438 N  N    . LEU   B 1 43  ? 48.042 -16.684 8.855   1.00 12.07 ?  43  LEU   B N    1 
ATOM   4439 C  CA   . LEU   B 1 43  ? 48.855 -16.621 7.644   1.00 11.94 ?  43  LEU   B CA   1 
ATOM   4440 C  C    . LEU   B 1 43  ? 50.271 -17.128 7.899   1.00 12.32 ?  43  LEU   B C    1 
ATOM   4441 O  O    . LEU   B 1 43  ? 51.249 -16.537 7.438   1.00 13.15 ?  43  LEU   B O    1 
ATOM   4442 C  CB   . LEU   B 1 43  ? 48.875 -15.216 7.039   1.00 12.25 ?  43  LEU   B CB   1 
ATOM   4443 C  CG   . LEU   B 1 43  ? 47.520 -14.601 6.666   1.00 12.51 ?  43  LEU   B CG   1 
ATOM   4444 C  CD1  . LEU   B 1 43  ? 47.718 -13.201 6.091   1.00 14.13 ?  43  LEU   B CD1  1 
ATOM   4445 C  CD2  . LEU   B 1 43  ? 46.745 -15.494 5.701   1.00 12.78 ?  43  LEU   B CD2  1 
ATOM   4446 H  H    . LEU   B 1 43  ? 47.295 -17.099 8.747   1.00 14.47 ?  43  LEU   B H    1 
ATOM   4447 H  HA   . LEU   B 1 43  ? 48.455 -17.210 6.983   1.00 14.32 ?  43  LEU   B HA   1 
ATOM   4448 H  HB2  . LEU   B 1 43  ? 49.297 -14.619 7.676   1.00 14.70 ?  43  LEU   B HB2  1 
ATOM   4449 H  HB3  . LEU   B 1 43  ? 49.408 -15.248 6.229   1.00 14.70 ?  43  LEU   B HB3  1 
ATOM   4450 H  HG   . LEU   B 1 43  ? 46.991 -14.514 7.471   1.00 15.00 ?  43  LEU   B HG   1 
ATOM   4451 H  HD11 . LEU   B 1 43  ? 46.849 -12.829 5.863   1.00 16.95 ?  43  LEU   B HD11 1 
ATOM   4452 H  HD12 . LEU   B 1 43  ? 48.147 -12.643 6.760   1.00 16.95 ?  43  LEU   B HD12 1 
ATOM   4453 H  HD13 . LEU   B 1 43  ? 48.272 -13.256 5.299   1.00 16.95 ?  43  LEU   B HD13 1 
ATOM   4454 H  HD21 . LEU   B 1 43  ? 45.946 -15.032 5.409   1.00 15.33 ?  43  LEU   B HD21 1 
ATOM   4455 H  HD22 . LEU   B 1 43  ? 47.307 -15.701 4.936   1.00 15.33 ?  43  LEU   B HD22 1 
ATOM   4456 H  HD23 . LEU   B 1 43  ? 46.502 -16.319 6.158   1.00 15.33 ?  43  LEU   B HD23 1 
ATOM   4457 N  N    . LYS   B 1 44  ? 50.375 -18.245 8.622   1.00 12.30 ?  44  LYS   B N    1 
ATOM   4458 C  CA   . LYS   B 1 44  ? 51.641 -18.926 8.858   1.00 13.06 ?  44  LYS   B CA   1 
ATOM   4459 C  C    . LYS   B 1 44  ? 51.755 -20.044 7.830   1.00 12.58 ?  44  LYS   B C    1 
ATOM   4460 O  O    . LYS   B 1 44  ? 51.061 -21.061 7.922   1.00 13.98 ?  44  LYS   B O    1 
ATOM   4461 C  CB   . LYS   B 1 44  ? 51.694 -19.445 10.293  1.00 14.91 ?  44  LYS   B CB   1 
ATOM   4462 C  CG   . LYS   B 1 44  ? 51.863 -18.341 11.327  1.00 17.34 ?  44  LYS   B CG   1 
ATOM   4463 C  CD   . LYS   B 1 44  ? 53.056 -17.457 10.947  1.00 20.33 ?  44  LYS   B CD   1 
ATOM   4464 C  CE   . LYS   B 1 44  ? 53.555 -16.596 12.077  1.00 23.15 ?  44  LYS   B CE   1 
ATOM   4465 N  NZ   . LYS   B 1 44  ? 54.722 -15.767 11.682  1.00 24.73 ?  44  LYS   B NZ   1 
ATOM   4466 H  H    . LYS   B 1 44  ? 49.701 -18.628 9.001   1.00 14.76 ?  44  LYS   B H    1 
ATOM   4467 H  HA   . LYS   B 1 44  ? 52.372 -18.310 8.701   1.00 15.67 ?  44  LYS   B HA   1 
ATOM   4468 H  HB2  . LYS   B 1 44  ? 50.859 -19.909 10.490  1.00 17.89 ?  44  LYS   B HB2  1 
ATOM   4469 H  HB3  . LYS   B 1 44  ? 52.437 -20.054 10.381  1.00 17.89 ?  44  LYS   B HB3  1 
ATOM   4470 H  HG2  . LYS   B 1 44  ? 51.062 -17.794 11.356  1.00 20.80 ?  44  LYS   B HG2  1 
ATOM   4471 H  HG3  . LYS   B 1 44  ? 52.035 -18.738 12.198  1.00 20.80 ?  44  LYS   B HG3  1 
ATOM   4472 H  HD2  . LYS   B 1 44  ? 53.780 -18.032 10.642  1.00 24.39 ?  44  LYS   B HD2  1 
ATOM   4473 H  HD3  . LYS   B 1 44  ? 52.781 -16.867 10.226  1.00 24.39 ?  44  LYS   B HD3  1 
ATOM   4474 H  HE2  . LYS   B 1 44  ? 52.850 -15.987 12.313  1.00 27.78 ?  44  LYS   B HE2  1 
ATOM   4475 H  HE3  . LYS   B 1 44  ? 53.802 -17.158 12.832  1.00 27.78 ?  44  LYS   B HE3  1 
ATOM   4476 H  HZ1  . LYS   B 1 44  ? 54.989 -15.273 12.371  1.00 29.67 ?  44  LYS   B HZ1  1 
ATOM   4477 H  HZ2  . LYS   B 1 44  ? 55.393 -16.285 11.416  1.00 29.67 ?  44  LYS   B HZ2  1 
ATOM   4478 H  HZ3  . LYS   B 1 44  ? 54.492 -15.224 11.011  1.00 29.67 ?  44  LYS   B HZ3  1 
ATOM   4479 N  N    . HIS   B 1 45  ? 52.598 -19.827 6.824   1.00 12.48 ?  45  HIS   B N    1 
ATOM   4480 C  CA   . HIS   B 1 45  ? 52.613 -20.661 5.622   1.00 12.72 ?  45  HIS   B CA   1 
ATOM   4481 C  C    . HIS   B 1 45  ? 53.634 -21.784 5.777   1.00 14.71 ?  45  HIS   B C    1 
ATOM   4482 O  O    . HIS   B 1 45  ? 54.694 -21.794 5.160   1.00 17.04 ?  45  HIS   B O    1 
ATOM   4483 C  CB   . HIS   B 1 45  ? 52.931 -19.807 4.406   1.00 12.53 ?  45  HIS   B CB   1 
ATOM   4484 C  CG   . HIS   B 1 45  ? 52.065 -18.601 4.294   1.00 12.49 ?  45  HIS   B CG   1 
ATOM   4485 N  ND1  . HIS   B 1 45  ? 50.687 -18.674 4.273   1.00 12.53 ?  45  HIS   B ND1  1 
ATOM   4486 C  CD2  . HIS   B 1 45  ? 52.385 -17.290 4.203   1.00 13.29 ?  45  HIS   B CD2  1 
ATOM   4487 C  CE1  . HIS   B 1 45  ? 50.204 -17.449 4.164   1.00 12.01 ?  45  HIS   B CE1  1 
ATOM   4488 N  NE2  . HIS   B 1 45  ? 51.210 -16.592 4.121   1.00 12.93 ?  45  HIS   B NE2  1 
ATOM   4489 H  H    . HIS   B 1 45  ? 53.167 -19.183 6.809   1.00 14.97 ?  45  HIS   B H    1 
ATOM   4490 H  HA   . HIS   B 1 45  ? 51.735 -21.060 5.496   1.00 15.25 ?  45  HIS   B HA   1 
ATOM   4491 H  HB2  . HIS   B 1 45  ? 53.851 -19.517 4.458   1.00 15.03 ?  45  HIS   B HB2  1 
ATOM   4492 H  HB3  . HIS   B 1 45  ? 52.801 -20.350 3.605   1.00 15.03 ?  45  HIS   B HB3  1 
ATOM   4493 H  HD2  . HIS   B 1 45  ? 53.243 -16.932 4.199   1.00 15.95 ?  45  HIS   B HD2  1 
ATOM   4494 H  HE1  . HIS   B 1 45  ? 49.303 -17.228 4.119   1.00 14.41 ?  45  HIS   B HE1  1 
ATOM   4495 H  HE2  . HIS   B 1 45  ? 51.136 -15.739 4.058   1.00 15.51 ?  45  HIS   B HE2  1 
ATOM   4496 N  N    A GLY   B 1 46  ? 53.271 -22.761 6.601   0.68 15.65 ?  46  GLY   B N    1 
ATOM   4497 N  N    B GLY   B 1 46  ? 53.280 -22.748 6.618   0.32 15.62 ?  46  GLY   B N    1 
ATOM   4498 C  CA   A GLY   B 1 46  ? 54.201 -23.814 6.968   0.68 17.29 ?  46  GLY   B CA   1 
ATOM   4499 C  CA   B GLY   B 1 46  ? 54.204 -23.813 6.951   0.32 16.84 ?  46  GLY   B CA   1 
ATOM   4500 C  C    A GLY   B 1 46  ? 54.236 -25.035 6.070   0.68 19.20 ?  46  GLY   B C    1 
ATOM   4501 C  C    B GLY   B 1 46  ? 54.216 -24.962 5.963   0.32 18.21 ?  46  GLY   B C    1 
ATOM   4502 O  O    A GLY   B 1 46  ? 55.310 -25.463 5.634   0.68 22.00 ?  46  GLY   B O    1 
ATOM   4503 O  O    B GLY   B 1 46  ? 55.240 -25.238 5.330   0.32 19.01 ?  46  GLY   B O    1 
ATOM   4504 H  H    A GLY   B 1 46  ? 52.494 -22.825 6.973   0.68 18.78 ?  46  GLY   B H    1 
ATOM   4505 H  H    B GLY   B 1 46  ? 52.513 -22.802 7.011   0.32 18.74 ?  46  GLY   B H    1 
ATOM   4506 H  HA2  A GLY   B 1 46  ? 55.095 -23.440 6.995   0.68 20.75 ?  46  GLY   B HA2  1 
ATOM   4507 H  HA2  B GLY   B 1 46  ? 55.100 -23.447 6.998   0.32 20.20 ?  46  GLY   B HA2  1 
ATOM   4508 H  HA3  A GLY   B 1 46  ? 53.981 -24.126 7.858   0.68 20.75 ?  46  GLY   B HA3  1 
ATOM   4509 H  HA3  B GLY   B 1 46  ? 53.977 -24.162 7.829   0.32 20.20 ?  46  GLY   B HA3  1 
ATOM   4510 N  N    . GLY   B 1 47  ? 53.076 -25.633 5.806   1.00 18.71 ?  47  GLY   B N    1 
ATOM   4511 C  CA   . GLY   B 1 47  ? 53.012 -26.897 5.103   1.00 16.82 ?  47  GLY   B CA   1 
ATOM   4512 C  C    . GLY   B 1 47  ? 52.093 -26.860 3.897   1.00 14.65 ?  47  GLY   B C    1 
ATOM   4513 O  O    . GLY   B 1 47  ? 51.441 -25.854 3.613   1.00 14.47 ?  47  GLY   B O    1 
ATOM   4514 H  H    A GLY   B 1 47  ? 52.306 -25.332 6.053   0.68 22.45 ?  47  GLY   B H    1 
ATOM   4515 H  H    B GLY   B 1 47  ? 52.313 -25.363 6.104   0.32 22.45 ?  47  GLY   B H    1 
ATOM   4516 H  HA2  . GLY   B 1 47  ? 53.895 -27.151 4.798   1.00 20.18 ?  47  GLY   B HA2  1 
ATOM   4517 H  HA3  . GLY   B 1 47  ? 52.691 -27.584 5.709   1.00 20.18 ?  47  GLY   B HA3  1 
ATOM   4518 N  N    . GLY   B 1 48  ? 52.038 -28.000 3.206   1.00 13.77 ?  48  GLY   B N    1 
ATOM   4519 C  CA   . GLY   B 1 48  ? 51.104 -28.141 2.106   1.00 13.47 ?  48  GLY   B CA   1 
ATOM   4520 C  C    . GLY   B 1 48  ? 51.251 -27.036 1.083   1.00 12.55 ?  48  GLY   B C    1 
ATOM   4521 O  O    . GLY   B 1 48  ? 52.357 -26.580 0.771   1.00 13.23 ?  48  GLY   B O    1 
ATOM   4522 H  H    . GLY   B 1 48  ? 52.533 -28.685 3.346   1.00 16.51 ?  48  GLY   B H    1 
ATOM   4523 H  HA2  . GLY   B 1 48  ? 51.244 -28.995 1.666   1.00 16.16 ?  48  GLY   B HA2  1 
ATOM   4524 H  HA3  . GLY   B 1 48  ? 50.193 -28.120 2.447   1.00 16.16 ?  48  GLY   B HA3  1 
ATOM   4525 N  N    . VAL   B 1 49  ? 50.109 -26.601 0.548   1.00 12.37 ?  49  VAL   B N    1 
ATOM   4526 C  CA   . VAL   B 1 49  ? 50.099 -25.582 -0.498  1.00 12.46 ?  49  VAL   B CA   1 
ATOM   4527 C  C    . VAL   B 1 49  ? 50.757 -24.293 -0.010  1.00 11.61 ?  49  VAL   B C    1 
ATOM   4528 O  O    . VAL   B 1 49  ? 51.547 -23.671 -0.731  1.00 12.35 ?  49  VAL   B O    1 
ATOM   4529 C  CB   . VAL   B 1 49  ? 48.658 -25.336 -0.989  1.00 13.97 ?  49  VAL   B CB   1 
ATOM   4530 C  CG1  . VAL   B 1 49  ? 48.580 -24.080 -1.862  1.00 13.63 ?  49  VAL   B CG1  1 
ATOM   4531 C  CG2  . VAL   B 1 49  ? 48.128 -26.552 -1.741  1.00 15.63 ?  49  VAL   B CG2  1 
ATOM   4532 H  H    . VAL   B 1 49  ? 49.323 -26.883 0.767   1.00 14.84 ?  49  VAL   B H    1 
ATOM   4533 H  HA   . VAL   B 1 49  ? 50.611 -25.904 -1.256  1.00 14.95 ?  49  VAL   B HA   1 
ATOM   4534 H  HB   . VAL   B 1 49  ? 48.086 -25.194 -0.223  1.00 16.76 ?  49  VAL   B HB   1 
ATOM   4535 H  HG11 . VAL   B 1 49  ? 47.747 -24.093 -2.362  1.00 16.35 ?  49  VAL   B HG11 1 
ATOM   4536 H  HG12 . VAL   B 1 49  ? 48.607 -23.294 -1.293  1.00 16.35 ?  49  VAL   B HG12 1 
ATOM   4537 H  HG13 . VAL   B 1 49  ? 49.331 -24.071 -2.476  1.00 16.35 ?  49  VAL   B HG13 1 
ATOM   4538 H  HG21 . VAL   B 1 49  ? 47.224 -26.372 -2.039  1.00 18.75 ?  49  VAL   B HG21 1 
ATOM   4539 H  HG22 . VAL   B 1 49  ? 48.701 -26.726 -2.507  1.00 18.75 ?  49  VAL   B HG22 1 
ATOM   4540 H  HG23 . VAL   B 1 49  ? 48.135 -27.317 -1.145  1.00 18.75 ?  49  VAL   B HG23 1 
ATOM   4541 N  N    . ALA   B 1 50  ? 50.415 -23.850 1.205   1.00 11.53 ?  50  ALA   B N    1 
ATOM   4542 C  CA   . ALA   B 1 50  ? 50.941 -22.576 1.687   1.00 11.13 ?  50  ALA   B CA   1 
ATOM   4543 C  C    . ALA   B 1 50  ? 52.460 -22.611 1.792   1.00 11.40 ?  50  ALA   B C    1 
ATOM   4544 O  O    . ALA   B 1 50  ? 53.141 -21.647 1.422   1.00 11.63 ?  50  ALA   B O    1 
ATOM   4545 C  CB   . ALA   B 1 50  ? 50.318 -22.221 3.035   1.00 11.62 ?  50  ALA   B CB   1 
ATOM   4546 H  H    . ALA   B 1 50  ? 49.899 -24.261 1.756   1.00 13.83 ?  50  ALA   B H    1 
ATOM   4547 H  HA   . ALA   B 1 50  ? 50.710 -21.881 1.058   1.00 13.35 ?  50  ALA   B HA   1 
ATOM   4548 H  HB1  . ALA   B 1 50  ? 50.678 -21.369 3.336   1.00 13.94 ?  50  ALA   B HB1  1 
ATOM   4549 H  HB2  . ALA   B 1 50  ? 49.356 -22.149 2.927   1.00 13.94 ?  50  ALA   B HB2  1 
ATOM   4550 H  HB3  . ALA   B 1 50  ? 50.529 -22.914 3.678   1.00 13.94 ?  50  ALA   B HB3  1 
ATOM   4551 N  N    . GLY   B 1 51  ? 53.013 -23.704 2.306   1.00 12.17 ?  51  GLY   B N    1 
ATOM   4552 C  CA   . GLY   B 1 51  ? 54.457 -23.807 2.371   1.00 12.81 ?  51  GLY   B CA   1 
ATOM   4553 C  C    . GLY   B 1 51  ? 55.102 -23.754 1.001   1.00 12.60 ?  51  GLY   B C    1 
ATOM   4554 O  O    . GLY   B 1 51  ? 56.144 -23.115 0.821   1.00 13.51 ?  51  GLY   B O    1 
ATOM   4555 H  H    . GLY   B 1 51  ? 52.589 -24.386 2.611   1.00 14.60 ?  51  GLY   B H    1 
ATOM   4556 H  HA2  . GLY   B 1 51  ? 54.815 -23.076 2.902   1.00 15.37 ?  51  GLY   B HA2  1 
ATOM   4557 H  HA3  . GLY   B 1 51  ? 54.710 -24.643 2.794   1.00 15.37 ?  51  GLY   B HA3  1 
ATOM   4558 N  N    . ALA   B 1 52  ? 54.496 -24.421 0.020   1.00 12.21 ?  52  ALA   B N    1 
ATOM   4559 C  CA   . ALA   B 1 52  ? 55.052 -24.439 -1.329  1.00 12.67 ?  52  ALA   B CA   1 
ATOM   4560 C  C    . ALA   B 1 52  ? 54.980 -23.060 -1.976  1.00 12.16 ?  52  ALA   B C    1 
ATOM   4561 O  O    . ALA   B 1 52  ? 55.951 -22.610 -2.603  1.00 12.96 ?  52  ALA   B O    1 
ATOM   4562 C  CB   . ALA   B 1 52  ? 54.332 -25.472 -2.191  1.00 13.27 ?  52  ALA   B CB   1 
ATOM   4563 H  H    . ALA   B 1 52  ? 53.762 -24.866 0.107   1.00 14.65 ?  52  ALA   B H    1 
ATOM   4564 H  HA   . ALA   B 1 52  ? 55.985 -24.690 -1.277  1.00 15.20 ?  52  ALA   B HA   1 
ATOM   4565 H  HB1  . ALA   B 1 52  ? 54.723 -25.461 -3.080  1.00 15.92 ?  52  ALA   B HB1  1 
ATOM   4566 H  HB2  . ALA   B 1 52  ? 54.445 -26.346 -1.790  1.00 15.92 ?  52  ALA   B HB2  1 
ATOM   4567 H  HB3  . ALA   B 1 52  ? 53.393 -25.244 -2.238  1.00 15.92 ?  52  ALA   B HB3  1 
ATOM   4568 N  N    . LEU   B 1 53  ? 53.833 -22.381 -1.861  1.00 11.64 ?  53  LEU   B N    1 
ATOM   4569 C  CA   . LEU   B 1 53  ? 53.722 -21.041 -2.431  1.00 11.71 ?  53  LEU   B CA   1 
ATOM   4570 C  C    . LEU   B 1 53  ? 54.728 -20.096 -1.785  1.00 11.91 ?  53  LEU   B C    1 
ATOM   4571 O  O    . LEU   B 1 53  ? 55.428 -19.345 -2.475  1.00 12.79 ?  53  LEU   B O    1 
ATOM   4572 C  CB   . LEU   B 1 53  ? 52.299 -20.503 -2.256  1.00 12.33 ?  53  LEU   B CB   1 
ATOM   4573 C  CG   . LEU   B 1 53  ? 51.161 -21.231 -2.976  1.00 12.69 ?  53  LEU   B CG   1 
ATOM   4574 C  CD1  . LEU   B 1 53  ? 49.832 -20.594 -2.632  1.00 14.31 ?  53  LEU   B CD1  1 
ATOM   4575 C  CD2  . LEU   B 1 53  ? 51.372 -21.238 -4.479  1.00 14.66 ?  53  LEU   B CD2  1 
ATOM   4576 H  H    . LEU   B 1 53  ? 53.124 -22.667 -1.466  1.00 13.97 ?  53  LEU   B H    1 
ATOM   4577 H  HA   . LEU   B 1 53  ? 53.918 -21.086 -3.384  1.00 14.04 ?  53  LEU   B HA   1 
ATOM   4578 H  HB2  . LEU   B 1 53  ? 52.094 -20.516 -1.312  1.00 14.80 ?  53  LEU   B HB2  1 
ATOM   4579 H  HB3  . LEU   B 1 53  ? 52.291 -19.588 -2.575  1.00 14.80 ?  53  LEU   B HB3  1 
ATOM   4580 H  HG   . LEU   B 1 53  ? 51.134 -22.152 -2.670  1.00 15.22 ?  53  LEU   B HG   1 
ATOM   4581 H  HD11 . LEU   B 1 53  ? 49.121 -21.073 -3.091  1.00 17.16 ?  53  LEU   B HD11 1 
ATOM   4582 H  HD12 . LEU   B 1 53  ? 49.691 -20.647 -1.670  1.00 17.16 ?  53  LEU   B HD12 1 
ATOM   4583 H  HD13 . LEU   B 1 53  ? 49.840 -19.667 -2.912  1.00 17.16 ?  53  LEU   B HD13 1 
ATOM   4584 H  HD21 . LEU   B 1 53  ? 50.635 -21.706 -4.900  1.00 17.59 ?  53  LEU   B HD21 1 
ATOM   4585 H  HD22 . LEU   B 1 53  ? 51.408 -20.323 -4.797  1.00 17.59 ?  53  LEU   B HD22 1 
ATOM   4586 H  HD23 . LEU   B 1 53  ? 52.207 -21.691 -4.680  1.00 17.59 ?  53  LEU   B HD23 1 
ATOM   4587 N  N    . ASN   B 1 54  ? 54.815 -20.119 -0.458  1.00 11.40 ?  54  ASN   B N    1 
ATOM   4588 C  CA   . ASN   B 1 54  ? 55.735 -19.210 0.214   1.00 12.33 ?  54  ASN   B CA   1 
ATOM   4589 C  C    . ASN   B 1 54  ? 57.179 -19.487 -0.184  1.00 12.81 ?  54  ASN   B C    1 
ATOM   4590 O  O    . ASN   B 1 54  ? 57.951 -18.549 -0.427  1.00 13.14 ?  54  ASN   B O    1 
ATOM   4591 C  CB   . ASN   B 1 54  ? 55.577 -19.283 1.724   1.00 13.30 ?  54  ASN   B CB   1 
ATOM   4592 C  CG   . ASN   B 1 54  ? 56.553 -18.367 2.436   1.00 13.20 ?  54  ASN   B CG   1 
ATOM   4593 O  OD1  . ASN   B 1 54  ? 56.578 -17.158 2.187   1.00 13.39 ?  54  ASN   B OD1  1 
ATOM   4594 N  ND2  . ASN   B 1 54  ? 57.395 -18.938 3.288   1.00 14.59 ?  54  ASN   B ND2  1 
ATOM   4595 H  H    . ASN   B 1 54  ? 54.369 -20.642 0.063   1.00 13.67 ?  54  ASN   B H    1 
ATOM   4596 H  HA   . ASN   B 1 54  ? 55.524 -18.306 -0.063  1.00 14.79 ?  54  ASN   B HA   1 
ATOM   4597 H  HB2  . ASN   B 1 54  ? 54.677 -19.004 1.964   1.00 15.96 ?  54  ASN   B HB2  1 
ATOM   4598 H  HB3  . ASN   B 1 54  ? 55.740 -20.187 2.022   1.00 15.96 ?  54  ASN   B HB3  1 
ATOM   4599 H  HD21 . ASN   B 1 54  ? 57.973 -18.454 3.709   1.00 17.51 ?  54  ASN   B HD21 1 
ATOM   4600 H  HD22 . ASN   B 1 54  ? 57.361 -19.782 3.429   1.00 17.51 ?  54  ASN   B HD22 1 
ATOM   4601 N  N    . LYS   B 1 55  ? 57.566 -20.767 -0.243  1.00 13.16 ?  55  LYS   B N    1 
ATOM   4602 C  CA   . LYS   B 1 55  ? 58.918 -21.114 -0.671  1.00 14.00 ?  55  LYS   B CA   1 
ATOM   4603 C  C    . LYS   B 1 55  ? 59.209 -20.579 -2.068  1.00 13.93 ?  55  LYS   B C    1 
ATOM   4604 O  O    . LYS   B 1 55  ? 60.310 -20.079 -2.327  1.00 14.77 ?  55  LYS   B O    1 
ATOM   4605 C  CB   . LYS   B 1 55  ? 59.107 -22.631 -0.619  1.00 15.57 ?  55  LYS   B CB   1 
ATOM   4606 C  CG   . LYS   B 1 55  ? 60.485 -23.096 -1.055  1.00 20.32 ?  55  LYS   B CG   1 
ATOM   4607 C  CD   . LYS   B 1 55  ? 60.655 -24.596 -0.882  1.00 24.26 ?  55  LYS   B CD   1 
ATOM   4608 C  CE   . LYS   B 1 55  ? 60.625 -25.004 0.589   1.00 27.34 ?  55  LYS   B CE   1 
ATOM   4609 N  NZ   . LYS   B 1 55  ? 61.003 -26.424 0.788   1.00 29.18 ?  55  LYS   B NZ   1 
ATOM   4610 H  H    . LYS   B 1 55  ? 57.067 -21.438 -0.040  1.00 15.79 ?  55  LYS   B H    1 
ATOM   4611 H  HA   . LYS   B 1 55  ? 59.553 -20.714 -0.058  1.00 16.79 ?  55  LYS   B HA   1 
ATOM   4612 H  HB2  . LYS   B 1 55  ? 58.962 -22.926 0.296   1.00 18.68 ?  55  LYS   B HB2  1 
ATOM   4613 H  HB3  . LYS   B 1 55  ? 58.454 -23.050 -1.202  1.00 18.68 ?  55  LYS   B HB3  1 
ATOM   4614 H  HG2  . LYS   B 1 55  ? 60.614 -22.882 -1.993  1.00 24.38 ?  55  LYS   B HG2  1 
ATOM   4615 H  HG3  . LYS   B 1 55  ? 61.158 -22.647 -0.516  1.00 24.38 ?  55  LYS   B HG3  1 
ATOM   4616 H  HD2  . LYS   B 1 55  ? 59.933 -25.057 -1.338  1.00 29.11 ?  55  LYS   B HD2  1 
ATOM   4617 H  HD3  . LYS   B 1 55  ? 61.511 -24.868 -1.251  1.00 29.11 ?  55  LYS   B HD3  1 
ATOM   4618 H  HE2  . LYS   B 1 55  ? 61.248 -24.444 1.082   1.00 32.81 ?  55  LYS   B HE2  1 
ATOM   4619 H  HE3  . LYS   B 1 55  ? 59.725 -24.876 0.932   1.00 32.81 ?  55  LYS   B HE3  1 
ATOM   4620 H  HZ1  . LYS   B 1 55  ? 60.963 -26.625 1.653   1.00 35.01 ?  55  LYS   B HZ1  1 
ATOM   4621 H  HZ2  . LYS   B 1 55  ? 60.442 -26.949 0.340   1.00 35.01 ?  55  LYS   B HZ2  1 
ATOM   4622 H  HZ3  . LYS   B 1 55  ? 61.829 -26.559 0.493   1.00 35.01 ?  55  LYS   B HZ3  1 
ATOM   4623 N  N    . ALA   B 1 56  ? 58.233 -20.657 -2.978  1.00 13.45 ?  56  ALA   B N    1 
ATOM   4624 C  CA   . ALA   B 1 56  ? 58.457 -20.161 -4.332  1.00 14.27 ?  56  ALA   B CA   1 
ATOM   4625 C  C    . ALA   B 1 56  ? 58.731 -18.663 -4.335  1.00 13.96 ?  56  ALA   B C    1 
ATOM   4626 O  O    . ALA   B 1 56  ? 59.458 -18.163 -5.206  1.00 15.31 ?  56  ALA   B O    1 
ATOM   4627 C  CB   . ALA   B 1 56  ? 57.258 -20.489 -5.222  1.00 15.07 ?  56  ALA   B CB   1 
ATOM   4628 H  H    . ALA   B 1 56  ? 57.443 -20.974 -2.832  1.00 16.13 ?  56  ALA   B H    1 
ATOM   4629 H  HA   . ALA   B 1 56  ? 59.232 -20.605 -4.699  1.00 17.12 ?  56  ALA   B HA   1 
ATOM   4630 H  HB1  . ALA   B 1 56  ? 57.430 -20.157 -6.118  1.00 18.08 ?  56  ALA   B HB1  1 
ATOM   4631 H  HB2  . ALA   B 1 56  ? 57.136 -21.452 -5.246  1.00 18.08 ?  56  ALA   B HB2  1 
ATOM   4632 H  HB3  . ALA   B 1 56  ? 56.465 -20.065 -4.860  1.00 18.08 ?  56  ALA   B HB3  1 
ATOM   4633 N  N    . THR   B 1 57  ? 58.164 -17.933 -3.375  1.00 13.81 ?  57  THR   B N    1 
ATOM   4634 C  CA   . THR   B 1 57  ? 58.401 -16.497 -3.254  1.00 14.09 ?  57  THR   B CA   1 
ATOM   4635 C  C    . THR   B 1 57  ? 59.655 -16.167 -2.448  1.00 14.68 ?  57  THR   B C    1 
ATOM   4636 O  O    . THR   B 1 57  ? 59.897 -14.989 -2.153  1.00 14.94 ?  57  THR   B O    1 
ATOM   4637 C  CB   . THR   B 1 57  ? 57.202 -15.767 -2.617  1.00 13.22 ?  57  THR   B CB   1 
ATOM   4638 O  OG1  . THR   B 1 57  ? 57.185 -15.979 -1.197  1.00 13.44 ?  57  THR   B OG1  1 
ATOM   4639 C  CG2  . THR   B 1 57  ? 55.880 -16.189 -3.252  1.00 13.28 ?  57  THR   B CG2  1 
ATOM   4640 H  H    . THR   B 1 57  ? 57.617 -18.243 -2.787  1.00 16.57 ?  57  THR   B H    1 
ATOM   4641 H  HA   . THR   B 1 57  ? 58.517 -16.131 -4.147  1.00 16.90 ?  57  THR   B HA   1 
ATOM   4642 H  HB   . THR   B 1 57  ? 57.305 -14.816 -2.787  1.00 15.86 ?  57  THR   B HB   1 
ATOM   4643 H  HG1  . THR   B 1 57  ? 57.123 -16.798 -1.034  1.00 16.12 ?  57  THR   B HG1  1 
ATOM   4644 H  HG21 . THR   B 1 57  ? 55.156 -15.650 -2.903  1.00 15.93 ?  57  THR   B HG21 1 
ATOM   4645 H  HG22 . THR   B 1 57  ? 55.922 -16.077 -4.216  1.00 15.93 ?  57  THR   B HG22 1 
ATOM   4646 H  HG23 . THR   B 1 57  ? 55.701 -17.122 -3.056  1.00 15.93 ?  57  THR   B HG23 1 
ATOM   4647 N  N    . ASN   B 1 58  ? 60.445 -17.171 -2.078  1.00 15.11 ?  58  ASN   B N    1 
ATOM   4648 C  CA   . ASN   B 1 58  ? 61.648 -16.953 -1.277  1.00 17.88 ?  58  ASN   B CA   1 
ATOM   4649 C  C    . ASN   B 1 58  ? 61.318 -16.239 0.034   1.00 15.75 ?  58  ASN   B C    1 
ATOM   4650 O  O    . ASN   B 1 58  ? 62.054 -15.361 0.493   1.00 16.39 ?  58  ASN   B O    1 
ATOM   4651 C  CB   . ASN   B 1 58  ? 62.731 -16.209 -2.064  1.00 26.18 ?  58  ASN   B CB   1 
ATOM   4652 C  CG   . ASN   B 1 58  ? 64.104 -16.348 -1.435  1.00 35.97 ?  58  ASN   B CG   1 
ATOM   4653 O  OD1  . ASN   B 1 58  ? 64.399 -17.344 -0.773  1.00 38.72 ?  58  ASN   B OD1  1 
ATOM   4654 N  ND2  . ASN   B 1 58  ? 64.951 -15.347 -1.635  1.00 41.43 ?  58  ASN   B ND2  1 
ATOM   4655 H  H    . ASN   B 1 58  ? 60.305 -18.000 -2.280  1.00 18.13 ?  58  ASN   B H    1 
ATOM   4656 H  HA   . ASN   B 1 58  ? 62.009 -17.824 -1.051  1.00 21.45 ?  58  ASN   B HA   1 
ATOM   4657 H  HB2  . ASN   B 1 58  ? 62.773 -16.572 -2.965  1.00 31.41 ?  58  ASN   B HB2  1 
ATOM   4658 H  HB3  . ASN   B 1 58  ? 62.510 -15.268 -2.095  1.00 31.41 ?  58  ASN   B HB3  1 
ATOM   4659 H  HD21 . ASN   B 1 58  ? 65.742 -15.381 -1.299  1.00 49.71 ?  58  ASN   B HD21 1 
ATOM   4660 H  HD22 . ASN   B 1 58  ? 64.708 -14.667 -2.100  1.00 49.71 ?  58  ASN   B HD22 1 
ATOM   4661 N  N    . ASN   B 1 59  ? 60.201 -16.629 0.649   1.00 14.87 ?  59  ASN   B N    1 
ATOM   4662 C  CA   . ASN   B 1 59  ? 59.724 -16.152 1.950   1.00 15.28 ?  59  ASN   B CA   1 
ATOM   4663 C  C    . ASN   B 1 59  ? 59.129 -14.745 1.892   1.00 14.69 ?  59  ASN   B C    1 
ATOM   4664 O  O    . ASN   B 1 59  ? 58.696 -14.244 2.933   1.00 14.38 ?  59  ASN   B O    1 
ATOM   4665 C  CB   . ASN   B 1 59  ? 60.796 -16.206 3.053   1.00 16.17 ?  59  ASN   B CB   1 
ATOM   4666 C  CG   . ASN   B 1 59  ? 60.210 -16.380 4.437   1.00 17.09 ?  59  ASN   B CG   1 
ATOM   4667 O  OD1  . ASN   B 1 59  ? 59.387 -17.269 4.667   1.00 17.13 ?  59  ASN   B OD1  1 
ATOM   4668 N  ND2  . ASN   B 1 59  ? 60.627 -15.534 5.368   1.00 17.88 ?  59  ASN   B ND2  1 
ATOM   4669 H  H    . ASN   B 1 59  ? 59.662 -17.215 0.310   1.00 17.84 ?  59  ASN   B H    1 
ATOM   4670 H  HA   . ASN   B 1 59  ? 59.014 -16.748 2.234   1.00 18.33 ?  59  ASN   B HA   1 
ATOM   4671 H  HB2  . ASN   B 1 59  ? 61.386 -16.958 2.892   1.00 19.40 ?  59  ASN   B HB2  1 
ATOM   4672 H  HB3  . ASN   B 1 59  ? 61.298 -15.379 3.052   1.00 19.40 ?  59  ASN   B HB3  1 
ATOM   4673 H  HD21 . ASN   B 1 59  ? 60.317 -15.590 6.171   1.00 21.45 ?  59  ASN   B HD21 1 
ATOM   4674 H  HD22 . ASN   B 1 59  ? 61.200 -14.928 5.171   1.00 21.45 ?  59  ASN   B HD22 1 
ATOM   4675 N  N    . ALA   B 1 60  ? 59.061 -14.106 0.721   1.00 14.15 ?  60  ALA   B N    1 
ATOM   4676 C  CA   . ALA   B 1 60  ? 58.470 -12.772 0.644   1.00 14.07 ?  60  ALA   B CA   1 
ATOM   4677 C  C    . ALA   B 1 60  ? 57.001 -12.795 1.046   1.00 12.88 ?  60  ALA   B C    1 
ATOM   4678 O  O    . ALA   B 1 60  ? 56.500 -11.844 1.659   1.00 13.67 ?  60  ALA   B O    1 
ATOM   4679 C  CB   . ALA   B 1 60  ? 58.629 -12.207 -0.767  1.00 15.46 ?  60  ALA   B CB   1 
ATOM   4680 H  H    . ALA   B 1 60  ? 59.348 -14.422 -0.026  1.00 16.97 ?  60  ALA   B H    1 
ATOM   4681 H  HA   . ALA   B 1 60  ? 58.939 -12.188 1.257   1.00 16.87 ?  60  ALA   B HA   1 
ATOM   4682 H  HB1  . ALA   B 1 60  ? 58.235 -11.323 -0.798  1.00 18.55 ?  60  ALA   B HB1  1 
ATOM   4683 H  HB2  . ALA   B 1 60  ? 59.577 -12.155 -0.982  1.00 18.55 ?  60  ALA   B HB2  1 
ATOM   4684 H  HB3  . ALA   B 1 60  ? 58.182 -12.794 -1.397  1.00 18.55 ?  60  ALA   B HB3  1 
ATOM   4685 N  N    . MET   B 1 61  ? 56.289 -13.870 0.698   1.00 12.79 ?  61  MET   B N    1 
ATOM   4686 C  CA   . MET   B 1 61  ? 54.892 -13.996 1.094   1.00 12.29 ?  61  MET   B CA   1 
ATOM   4687 C  C    . MET   B 1 61  ? 54.758 -13.996 2.615   1.00 12.24 ?  61  MET   B C    1 
ATOM   4688 O  O    . MET   B 1 61  ? 53.857 -13.351 3.165   1.00 12.32 ?  61  MET   B O    1 
ATOM   4689 C  CB   . MET   B 1 61  ? 54.313 -15.265 0.464   1.00 11.84 ?  61  MET   B CB   1 
ATOM   4690 C  CG   . MET   B 1 61  ? 52.880 -15.567 0.890   1.00 12.04 ?  61  MET   B CG   1 
ATOM   4691 S  SD   . MET   B 1 61  ? 52.223 -17.062 0.129   1.00 12.90 ?  61  MET   B SD   1 
ATOM   4692 C  CE   . MET   B 1 61  ? 51.969 -16.473 -1.543  1.00 14.35 ?  61  MET   B CE   1 
ATOM   4693 H  H    . MET   B 1 61  ? 56.593 -14.538 0.237   1.00 15.35 ?  61  MET   B H    1 
ATOM   4694 H  HA   . MET   B 1 61  ? 54.400 -13.244 0.733   1.00 14.74 ?  61  MET   B HA   1 
ATOM   4695 H  HB2  . MET   B 1 61  ? 54.320 -15.167 -0.504  1.00 14.20 ?  61  MET   B HB2  1 
ATOM   4696 H  HB3  . MET   B 1 61  ? 54.865 -16.022 0.718   1.00 14.20 ?  61  MET   B HB3  1 
ATOM   4697 H  HG2  . MET   B 1 61  ? 52.856 -15.688 1.850   1.00 14.44 ?  61  MET   B HG2  1 
ATOM   4698 H  HG3  . MET   B 1 61  ? 52.315 -14.823 0.633   1.00 14.44 ?  61  MET   B HG3  1 
ATOM   4699 H  HE1  . MET   B 1 61  ? 51.572 -17.181 -2.072  1.00 17.21 ?  61  MET   B HE1  1 
ATOM   4700 H  HE2  . MET   B 1 61  ? 51.378 -15.703 -1.521  1.00 17.21 ?  61  MET   B HE2  1 
ATOM   4701 H  HE3  . MET   B 1 61  ? 52.827 -16.217 -1.922  1.00 17.21 ?  61  MET   B HE3  1 
ATOM   4702 N  N    . GLN   B 1 62  ? 55.639 -14.711 3.317   1.00 12.11 ?  62  GLN   B N    1 
ATOM   4703 C  CA   . GLN   B 1 62  ? 55.539 -14.766 4.773   1.00 12.55 ?  62  GLN   B CA   1 
ATOM   4704 C  C    . GLN   B 1 62  ? 55.825 -13.411 5.405   1.00 12.70 ?  62  GLN   B C    1 
ATOM   4705 O  O    . GLN   B 1 62  ? 55.142 -13.010 6.353   1.00 13.39 ?  62  GLN   B O    1 
ATOM   4706 C  CB   . GLN   B 1 62  ? 56.488 -15.822 5.337   1.00 12.86 ?  62  GLN   B CB   1 
ATOM   4707 C  CG   . GLN   B 1 62  ? 56.272 -16.083 6.818   1.00 13.37 ?  62  GLN   B CG   1 
ATOM   4708 C  CD   . GLN   B 1 62  ? 54.899 -16.669 7.077   1.00 13.08 ?  62  GLN   B CD   1 
ATOM   4709 O  OE1  . GLN   B 1 62  ? 54.634 -17.820 6.728   1.00 13.29 ?  62  GLN   B OE1  1 
ATOM   4710 N  NE2  . GLN   B 1 62  ? 53.998 -15.872 7.646   1.00 13.91 ?  62  GLN   B NE2  1 
ATOM   4711 H  H    . GLN   B 1 62  ? 56.284 -15.168 2.978   1.00 14.53 ?  62  GLN   B H    1 
ATOM   4712 H  HA   . GLN   B 1 62  ? 54.633 -15.022 5.011   1.00 15.05 ?  62  GLN   B HA   1 
ATOM   4713 H  HB2  . GLN   B 1 62  ? 56.354 -16.658 4.863   1.00 15.43 ?  62  GLN   B HB2  1 
ATOM   4714 H  HB3  . GLN   B 1 62  ? 57.403 -15.519 5.217   1.00 15.43 ?  62  GLN   B HB3  1 
ATOM   4715 H  HG2  . GLN   B 1 62  ? 56.937 -16.720 7.129   1.00 16.04 ?  62  GLN   B HG2  1 
ATOM   4716 H  HG3  . GLN   B 1 62  ? 56.350 -15.252 7.309   1.00 16.04 ?  62  GLN   B HG3  1 
ATOM   4717 H  HE21 . GLN   B 1 62  ? 54.212 -15.068 7.863   1.00 16.68 ?  62  GLN   B HE21 1 
ATOM   4718 H  HE22 . GLN   B 1 62  ? 53.205 -16.164 7.801   1.00 16.68 ?  62  GLN   B HE22 1 
ATOM   4719 N  N    . VAL   B 1 63  ? 56.837 -12.694 4.909   1.00 13.42 ?  63  VAL   B N    1 
ATOM   4720 C  CA   . VAL   B 1 63  ? 57.145 -11.378 5.464   1.00 14.48 ?  63  VAL   B CA   1 
ATOM   4721 C  C    . VAL   B 1 63  ? 55.956 -10.442 5.284   1.00 13.56 ?  63  VAL   B C    1 
ATOM   4722 O  O    . VAL   B 1 63  ? 55.545 -9.733  6.214   1.00 14.09 ?  63  VAL   B O    1 
ATOM   4723 C  CB   . VAL   B 1 63  ? 58.434 -10.819 4.835   1.00 16.23 ?  63  VAL   B CB   1 
ATOM   4724 C  CG1  . VAL   B 1 63  ? 58.661 -9.378  5.275   1.00 16.73 ?  63  VAL   B CG1  1 
ATOM   4725 C  CG2  . VAL   B 1 63  ? 59.620 -11.693 5.216   1.00 16.74 ?  63  VAL   B CG2  1 
ATOM   4726 H  H    . VAL   B 1 63  ? 57.342 -12.944 4.255   1.00 16.09 ?  63  VAL   B H    1 
ATOM   4727 H  HA   . VAL   B 1 63  ? 57.302 -11.478 6.412   1.00 17.37 ?  63  VAL   B HA   1 
ATOM   4728 H  HB   . VAL   B 1 63  ? 58.354 -10.834 3.868   1.00 19.47 ?  63  VAL   B HB   1 
ATOM   4729 H  HG11 . VAL   B 1 63  ? 59.578 -9.133  5.086   1.00 20.07 ?  63  VAL   B HG11 1 
ATOM   4730 H  HG12 . VAL   B 1 63  ? 58.054 -8.801  4.791   1.00 20.07 ?  63  VAL   B HG12 1 
ATOM   4731 H  HG13 . VAL   B 1 63  ? 58.493 -9.314  6.230   1.00 20.07 ?  63  VAL   B HG13 1 
ATOM   4732 H  HG21 . VAL   B 1 63  ? 60.428 -11.316 4.832   1.00 20.08 ?  63  VAL   B HG21 1 
ATOM   4733 H  HG22 . VAL   B 1 63  ? 59.697 -11.712 6.186   1.00 20.08 ?  63  VAL   B HG22 1 
ATOM   4734 H  HG23 . VAL   B 1 63  ? 59.479 -12.589 4.880   1.00 20.08 ?  63  VAL   B HG23 1 
ATOM   4735 N  N    . GLU   B 1 64  ? 55.381 -10.434 4.079   1.00 13.36 ?  64  GLU   B N    1 
ATOM   4736 C  CA   . GLU   B 1 64  ? 54.213 -9.601  3.806   1.00 12.99 ?  64  GLU   B CA   1 
ATOM   4737 C  C    . GLU   B 1 64  ? 53.033 -9.997  4.689   1.00 12.64 ?  64  GLU   B C    1 
ATOM   4738 O  O    . GLU   B 1 64  ? 52.287 -9.135  5.188   1.00 13.19 ?  64  GLU   B O    1 
ATOM   4739 C  CB   . GLU   B 1 64  ? 53.846 -9.753  2.327   1.00 13.27 ?  64  GLU   B CB   1 
ATOM   4740 C  CG   . GLU   B 1 64  ? 52.598 -8.999  1.886   1.00 13.87 ?  64  GLU   B CG   1 
ATOM   4741 C  CD   . GLU   B 1 64  ? 52.049 -9.494  0.552   1.00 14.79 ?  64  GLU   B CD   1 
ATOM   4742 O  OE1  . GLU   B 1 64  ? 52.223 -10.703 0.225   1.00 15.59 ?  64  GLU   B OE1  1 
ATOM   4743 O  OE2  . GLU   B 1 64  ? 51.420 -8.672  -0.161  1.00 14.98 -1 64  GLU   B OE2  1 
ATOM   4744 H  H    . GLU   B 1 64  ? 55.654 -10.897 3.403   1.00 16.03 ?  64  GLU   B H    1 
ATOM   4745 H  HA   . GLU   B 1 64  ? 54.432 -8.672  3.975   1.00 15.59 ?  64  GLU   B HA   1 
ATOM   4746 H  HB2  . GLU   B 1 64  ? 54.587 -9.421  1.788   1.00 15.92 ?  64  GLU   B HB2  1 
ATOM   4747 H  HB3  . GLU   B 1 64  ? 53.705 -10.690 2.138   1.00 15.92 ?  64  GLU   B HB3  1 
ATOM   4748 H  HG2  . GLU   B 1 64  ? 51.898 -9.106  2.552   1.00 16.64 ?  64  GLU   B HG2  1 
ATOM   4749 H  HG3  . GLU   B 1 64  ? 52.813 -8.057  1.787   1.00 16.64 ?  64  GLU   B HG3  1 
ATOM   4750 N  N    . SER   B 1 65  ? 52.846 -11.303 4.880   1.00 12.14 ?  65  SER   B N    1 
ATOM   4751 C  CA   . SER   B 1 65  ? 51.734 -11.805 5.677   1.00 12.29 ?  65  SER   B CA   1 
ATOM   4752 C  C    . SER   B 1 65  ? 51.871 -11.408 7.141   1.00 12.51 ?  65  SER   B C    1 
ATOM   4753 O  O    . SER   B 1 65  ? 50.875 -11.034 7.778   1.00 12.94 ?  65  SER   B O    1 
ATOM   4754 C  CB   . SER   B 1 65  ? 51.653 -13.328 5.546   1.00 12.83 ?  65  SER   B CB   1 
ATOM   4755 O  OG   . SER   B 1 65  ? 51.303 -13.733 4.227   1.00 12.94 ?  65  SER   B OG   1 
ATOM   4756 H  H    . SER   B 1 65  ? 53.352 -11.927 4.558   1.00 14.56 ?  65  SER   B H    1 
ATOM   4757 H  HA   . SER   B 1 65  ? 50.905 -11.428 5.337   1.00 14.75 ?  65  SER   B HA   1 
ATOM   4758 H  HB2  . SER   B 1 65  ? 52.514 -13.706 5.771   1.00 15.39 ?  65  SER   B HB2  1 
ATOM   4759 H  HB3  . SER   B 1 65  ? 50.978 -13.655 6.164   1.00 15.39 ?  65  SER   B HB3  1 
ATOM   4760 H  HG   . SER   B 1 65  ? 51.876 -13.448 3.680   1.00 15.53 ?  65  SER   B HG   1 
ATOM   4761 N  N    . ASP   B 1 66  ? 53.083 -11.508 7.705   1.00 12.90 ?  66  ASP   B N    1 
ATOM   4762 C  CA   . ASP   B 1 66  ? 53.272 -11.115 9.100   1.00 13.57 ?  66  ASP   B CA   1 
ATOM   4763 C  C    . ASP   B 1 66  ? 52.958 -9.634  9.300   1.00 13.66 ?  66  ASP   B C    1 
ATOM   4764 O  O    . ASP   B 1 66  ? 52.383 -9.240  10.322  1.00 13.91 ?  66  ASP   B O    1 
ATOM   4765 C  CB   . ASP   B 1 66  ? 54.704 -11.415 9.549   1.00 14.42 ?  66  ASP   B CB   1 
ATOM   4766 C  CG   . ASP   B 1 66  ? 54.985 -12.909 9.700   1.00 16.41 ?  66  ASP   B CG   1 
ATOM   4767 O  OD1  . ASP   B 1 66  ? 54.041 -13.727 9.634   1.00 16.93 ?  66  ASP   B OD1  1 
ATOM   4768 O  OD2  . ASP   B 1 66  ? 56.166 -13.274 9.896   1.00 19.37 -1 66  ASP   B OD2  1 
ATOM   4769 H  H    . ASP   B 1 66  ? 53.784 -11.808 7.315   1.00 15.47 ?  66  ASP   B H    1 
ATOM   4770 H  HA   . ASP   B 1 66  ? 52.667 -11.622 9.664   1.00 16.27 ?  66  ASP   B HA   1 
ATOM   4771 H  HB2  . ASP   B 1 66  ? 55.320 -11.055 8.892   1.00 17.30 ?  66  ASP   B HB2  1 
ATOM   4772 H  HB3  . ASP   B 1 66  ? 54.857 -10.987 10.411  1.00 17.30 ?  66  ASP   B HB3  1 
ATOM   4773 N  N    . ASP   B 1 67  ? 53.331 -8.793  8.335   1.00 13.24 ?  67  ASP   B N    1 
ATOM   4774 C  CA   . ASP   B 1 67  ? 52.983 -7.381  8.418   1.00 13.56 ?  67  ASP   B CA   1 
ATOM   4775 C  C    . ASP   B 1 67  ? 51.471 -7.176  8.336   1.00 13.76 ?  67  ASP   B C    1 
ATOM   4776 O  O    . ASP   B 1 67  ? 50.907 -6.377  9.093   1.00 14.40 ?  67  ASP   B O    1 
ATOM   4777 C  CB   . ASP   B 1 67  ? 53.697 -6.621  7.312   1.00 14.95 ?  67  ASP   B CB   1 
ATOM   4778 C  CG   . ASP   B 1 67  ? 53.281 -5.181  7.262   1.00 16.81 ?  67  ASP   B CG   1 
ATOM   4779 O  OD1  . ASP   B 1 67  ? 53.773 -4.371  8.083   1.00 18.19 ?  67  ASP   B OD1  1 
ATOM   4780 O  OD2  . ASP   B 1 67  ? 52.424 -4.873  6.421   1.00 18.24 -1 67  ASP   B OD2  1 
ATOM   4781 H  H    . ASP   B 1 67  ? 53.784 -9.013  7.637   1.00 15.88 ?  67  ASP   B H    1 
ATOM   4782 H  HA   . ASP   B 1 67  ? 53.288 -7.026  9.265   1.00 16.27 ?  67  ASP   B HA   1 
ATOM   4783 H  HB2  . ASP   B 1 67  ? 54.657 -6.654  7.462   1.00 17.94 ?  67  ASP   B HB2  1 
ATOM   4784 H  HB3  . ASP   B 1 67  ? 53.487 -7.028  6.451   1.00 17.94 ?  67  ASP   B HB3  1 
ATOM   4785 N  N    . TYR   B 1 68  ? 50.792 -7.906  7.440   1.00 13.21 ?  68  TYR   B N    1 
ATOM   4786 C  CA   . TYR   B 1 68  ? 49.334 -7.831  7.369   1.00 14.09 ?  68  TYR   B CA   1 
ATOM   4787 C  C    . TYR   B 1 68  ? 48.702 -8.177  8.713   1.00 13.87 ?  68  TYR   B C    1 
ATOM   4788 O  O    . TYR   B 1 68  ? 47.771 -7.500  9.167   1.00 14.50 ?  68  TYR   B O    1 
ATOM   4789 C  CB   . TYR   B 1 68  ? 48.803 -8.763  6.270   1.00 15.41 ?  68  TYR   B CB   1 
ATOM   4790 C  CG   . TYR   B 1 68  ? 47.297 -8.912  6.325   1.00 16.15 ?  68  TYR   B CG   1 
ATOM   4791 C  CD1  . TYR   B 1 68  ? 46.705 -9.869  7.144   1.00 16.72 ?  68  TYR   B CD1  1 
ATOM   4792 C  CD2  . TYR   B 1 68  ? 46.470 -8.070  5.602   1.00 17.26 ?  68  TYR   B CD2  1 
ATOM   4793 C  CE1  . TYR   B 1 68  ? 45.341 -9.987  7.234   1.00 17.93 ?  68  TYR   B CE1  1 
ATOM   4794 C  CE2  . TYR   B 1 68  ? 45.089 -8.194  5.675   1.00 17.75 ?  68  TYR   B CE2  1 
ATOM   4795 C  CZ   . TYR   B 1 68  ? 44.544 -9.149  6.498   1.00 18.00 ?  68  TYR   B CZ   1 
ATOM   4796 O  OH   . TYR   B 1 68  ? 43.174 -9.264  6.587   1.00 19.47 ?  68  TYR   B OH   1 
ATOM   4797 H  H    . TYR   B 1 68  ? 51.152 -8.453  6.873   1.00 15.85 ?  68  TYR   B H    1 
ATOM   4798 H  HA   . TYR   B 1 68  ? 49.081 -6.925  7.144   1.00 16.90 ?  68  TYR   B HA   1 
ATOM   4799 H  HB2  . TYR   B 1 68  ? 49.036 -8.397  5.405   1.00 18.49 ?  68  TYR   B HB2  1 
ATOM   4800 H  HB3  . TYR   B 1 68  ? 49.198 -9.642  6.382   1.00 18.49 ?  68  TYR   B HB3  1 
ATOM   4801 H  HD1  . TYR   B 1 68  ? 47.245 -10.441 7.646   1.00 20.06 ?  68  TYR   B HD1  1 
ATOM   4802 H  HD2  . TYR   B 1 68  ? 46.847 -7.417  5.062   1.00 20.70 ?  68  TYR   B HD2  1 
ATOM   4803 H  HE1  . TYR   B 1 68  ? 44.958 -10.646 7.774   1.00 21.51 ?  68  TYR   B HE1  1 
ATOM   4804 H  HE2  . TYR   B 1 68  ? 44.537 -7.625  5.190   1.00 21.29 ?  68  TYR   B HE2  1 
ATOM   4805 H  HH   . TYR   B 1 68  ? 42.794 -8.706  6.079   1.00 23.36 ?  68  TYR   B HH   1 
ATOM   4806 N  N    . ILE   B 1 69  ? 49.189 -9.242  9.358   1.00 13.70 ?  69  ILE   B N    1 
ATOM   4807 C  CA   . ILE   B 1 69  ? 48.637 -9.671  10.640  1.00 13.92 ?  69  ILE   B CA   1 
ATOM   4808 C  C    . ILE   B 1 69  ? 48.890 -8.625  11.717  1.00 13.60 ?  69  ILE   B C    1 
ATOM   4809 O  O    . ILE   B 1 69  ? 48.019 -8.350  12.550  1.00 13.99 ?  69  ILE   B O    1 
ATOM   4810 C  CB   . ILE   B 1 69  ? 49.213 -11.046 11.032  1.00 14.70 ?  69  ILE   B CB   1 
ATOM   4811 C  CG1  . ILE   B 1 69  ? 48.678 -12.153 10.113  1.00 15.22 ?  69  ILE   B CG1  1 
ATOM   4812 C  CG2  . ILE   B 1 69  ? 48.932 -11.358 12.494  1.00 15.88 ?  69  ILE   B CG2  1 
ATOM   4813 C  CD1  . ILE   B 1 69  ? 47.198 -12.451 10.270  1.00 16.17 ?  69  ILE   B CD1  1 
ATOM   4814 H  H    . ILE   B 1 69  ? 49.841 -9.729  9.074   1.00 16.44 ?  69  ILE   B H    1 
ATOM   4815 H  HA   . ILE   B 1 69  ? 47.680 -9.766  10.545  1.00 16.70 ?  69  ILE   B HA   1 
ATOM   4816 H  HB   . ILE   B 1 69  ? 50.177 -11.010 10.916  1.00 17.64 ?  69  ILE   B HB   1 
ATOM   4817 H  HG12 . ILE   B 1 69  ? 48.828 -11.891 9.190   1.00 18.26 ?  69  ILE   B HG12 1 
ATOM   4818 H  HG13 . ILE   B 1 69  ? 49.164 -12.973 10.300  1.00 18.26 ?  69  ILE   B HG13 1 
ATOM   4819 H  HG21 . ILE   B 1 69  ? 49.060 -12.308 12.643  1.00 19.05 ?  69  ILE   B HG21 1 
ATOM   4820 H  HG22 . ILE   B 1 69  ? 49.545 -10.854 13.052  1.00 19.05 ?  69  ILE   B HG22 1 
ATOM   4821 H  HG23 . ILE   B 1 69  ? 48.016 -11.113 12.700  1.00 19.05 ?  69  ILE   B HG23 1 
ATOM   4822 H  HD11 . ILE   B 1 69  ? 46.959 -13.176 9.674   1.00 19.40 ?  69  ILE   B HD11 1 
ATOM   4823 H  HD12 . ILE   B 1 69  ? 47.020 -12.708 11.189  1.00 19.40 ?  69  ILE   B HD12 1 
ATOM   4824 H  HD13 . ILE   B 1 69  ? 46.688 -11.657 10.045  1.00 19.40 ?  69  ILE   B HD13 1 
ATOM   4825 N  N    . ALA   B 1 70  ? 50.085 -8.035  11.738  1.00 13.92 ?  70  ALA   B N    1 
ATOM   4826 C  CA   . ALA   B 1 70  ? 50.362 -6.997  12.724  1.00 13.53 ?  70  ALA   B CA   1 
ATOM   4827 C  C    . ALA   B 1 70  ? 49.360 -5.856  12.616  1.00 14.31 ?  70  ALA   B C    1 
ATOM   4828 O  O    . ALA   B 1 70  ? 48.917 -5.311  13.632  1.00 14.98 ?  70  ALA   B O    1 
ATOM   4829 C  CB   . ALA   B 1 70  ? 51.789 -6.476  12.556  1.00 14.47 ?  70  ALA   B CB   1 
ATOM   4830 H  H    . ALA   B 1 70  ? 50.731 -8.211  11.204  1.00 16.70 ?  70  ALA   B H    1 
ATOM   4831 H  HA   . ALA   B 1 70  ? 50.291 -7.377  13.614  1.00 16.24 ?  70  ALA   B HA   1 
ATOM   4832 H  HB1  . ALA   B 1 70  ? 51.971 -5.815  13.244  1.00 17.36 ?  70  ALA   B HB1  1 
ATOM   4833 H  HB2  . ALA   B 1 70  ? 52.412 -7.218  12.645  1.00 17.36 ?  70  ALA   B HB2  1 
ATOM   4834 H  HB3  . ALA   B 1 70  ? 51.883 -6.075  11.678  1.00 17.36 ?  70  ALA   B HB3  1 
ATOM   4835 N  N    . THR   B 1 71  ? 48.989 -5.484  11.394  1.00 14.69 ?  71  THR   B N    1 
ATOM   4836 C  CA   . THR   B 1 71  ? 48.101 -4.346  11.181  1.00 15.58 ?  71  THR   B CA   1 
ATOM   4837 C  C    . THR   B 1 71  ? 46.633 -4.712  11.384  1.00 16.15 ?  71  THR   B C    1 
ATOM   4838 O  O    . THR   B 1 71  ? 45.852 -3.896  11.892  1.00 17.77 ?  71  THR   B O    1 
ATOM   4839 C  CB   . THR   B 1 71  ? 48.318 -3.786  9.773   1.00 17.84 ?  71  THR   B CB   1 
ATOM   4840 O  OG1  . THR   B 1 71  ? 49.652 -3.275  9.662   1.00 20.15 ?  71  THR   B OG1  1 
ATOM   4841 C  CG2  . THR   B 1 71  ? 47.314 -2.684  9.456   1.00 18.85 ?  71  THR   B CG2  1 
ATOM   4842 H  H    . THR   B 1 71  ? 49.241 -5.878  10.672  1.00 17.62 ?  71  THR   B H    1 
ATOM   4843 H  HA   . THR   B 1 71  ? 48.327 -3.649  11.816  1.00 18.69 ?  71  THR   B HA   1 
ATOM   4844 H  HB   . THR   B 1 71  ? 48.204 -4.498  9.124   1.00 21.41 ?  71  THR   B HB   1 
ATOM   4845 H  HG1  . THR   B 1 71  ? 49.780 -2.958  8.889   1.00 24.18 ?  71  THR   B HG1  1 
ATOM   4846 H  HG21 . THR   B 1 71  ? 47.616 -2.170  8.690   1.00 22.61 ?  71  THR   B HG21 1 
ATOM   4847 H  HG22 . THR   B 1 71  ? 46.448 -3.068  9.253   1.00 22.61 ?  71  THR   B HG22 1 
ATOM   4848 H  HG23 . THR   B 1 71  ? 47.226 -2.086  10.216  1.00 22.61 ?  71  THR   B HG23 1 
ATOM   4849 N  N    . ASN   B 1 72  ? 46.237 -5.926  10.996  1.00 15.64 ?  72  ASN   B N    1 
ATOM   4850 C  CA   . ASN   B 1 72  ? 44.831 -6.280  10.871  1.00 16.21 ?  72  ASN   B CA   1 
ATOM   4851 C  C    . ASN   B 1 72  ? 44.357 -7.373  11.816  1.00 16.89 ?  72  ASN   B C    1 
ATOM   4852 O  O    . ASN   B 1 72  ? 43.140 -7.537  11.978  1.00 18.15 ?  72  ASN   B O    1 
ATOM   4853 C  CB   . ASN   B 1 72  ? 44.518 -6.710  9.430   1.00 17.24 ?  72  ASN   B CB   1 
ATOM   4854 C  CG   . ASN   B 1 72  ? 44.797 -5.616  8.433   1.00 18.45 ?  72  ASN   B CG   1 
ATOM   4855 O  OD1  . ASN   B 1 72  ? 45.813 -5.631  7.735   1.00 19.80 ?  72  ASN   B OD1  1 
ATOM   4856 N  ND2  . ASN   B 1 72  ? 43.914 -4.636  8.385   1.00 19.95 ?  72  ASN   B ND2  1 
ATOM   4857 H  H    . ASN   B 1 72  ? 46.776 -6.571  10.792  1.00 18.76 ?  72  ASN   B H    1 
ATOM   4858 H  HA   . ASN   B 1 72  ? 44.301 -5.491  11.053  1.00 19.45 ?  72  ASN   B HA   1 
ATOM   4859 H  HB2  . ASN   B 1 72  ? 45.075 -7.475  9.198   1.00 20.69 ?  72  ASN   B HB2  1 
ATOM   4860 H  HB3  . ASN   B 1 72  ? 43.584 -6.948  9.362   1.00 20.69 ?  72  ASN   B HB3  1 
ATOM   4861 H  HD21 . ASN   B 1 72  ? 44.022 -3.983  7.834   1.00 23.93 ?  72  ASN   B HD21 1 
ATOM   4862 H  HD22 . ASN   B 1 72  ? 43.218 -4.658  8.891   1.00 23.93 ?  72  ASN   B HD22 1 
ATOM   4863 N  N    . GLY   B 1 73  ? 45.260 -8.123  12.440  1.00 16.26 ?  73  GLY   B N    1 
ATOM   4864 C  CA   . GLY   B 1 73  ? 44.865 -9.261  13.233  1.00 15.87 ?  73  GLY   B CA   1 
ATOM   4865 C  C    . GLY   B 1 73  ? 44.510 -10.456 12.373  1.00 14.37 ?  73  GLY   B C    1 
ATOM   4866 O  O    . GLY   B 1 73  ? 44.505 -10.385 11.145  1.00 14.54 ?  73  GLY   B O    1 
ATOM   4867 H  H    . GLY   B 1 73  ? 46.111 -7.987  12.415  1.00 19.51 ?  73  GLY   B H    1 
ATOM   4868 H  HA2  . GLY   B 1 73  ? 45.592 -9.508  13.827  1.00 19.04 ?  73  GLY   B HA2  1 
ATOM   4869 H  HA3  . GLY   B 1 73  ? 44.093 -9.026  13.773  1.00 19.04 ?  73  GLY   B HA3  1 
ATOM   4870 N  N    . PRO   B 1 74  ? 44.205 -11.577 13.021  1.00 14.54 ?  74  PRO   B N    1 
ATOM   4871 C  CA   . PRO   B 1 74  ? 43.955 -12.818 12.285  1.00 14.07 ?  74  PRO   B CA   1 
ATOM   4872 C  C    . PRO   B 1 74  ? 42.655 -12.771 11.495  1.00 13.75 ?  74  PRO   B C    1 
ATOM   4873 O  O    . PRO   B 1 74  ? 41.716 -12.034 11.816  1.00 15.00 ?  74  PRO   B O    1 
ATOM   4874 C  CB   . PRO   B 1 74  ? 43.877 -13.868 13.398  1.00 15.54 ?  74  PRO   B CB   1 
ATOM   4875 C  CG   . PRO   B 1 74  ? 43.420 -13.102 14.596  1.00 17.16 ?  74  PRO   B CG   1 
ATOM   4876 C  CD   . PRO   B 1 74  ? 44.094 -11.767 14.476  1.00 16.32 ?  74  PRO   B CD   1 
ATOM   4877 H  HA   . PRO   B 1 74  ? 44.699 -13.019 11.689  1.00 16.88 ?  74  PRO   B HA   1 
ATOM   4878 H  HB2  . PRO   B 1 74  ? 43.234 -14.551 13.154  1.00 18.64 ?  74  PRO   B HB2  1 
ATOM   4879 H  HB3  . PRO   B 1 74  ? 44.754 -14.253 13.547  1.00 18.64 ?  74  PRO   B HB3  1 
ATOM   4880 H  HG2  . PRO   B 1 74  ? 42.453 -13.003 14.570  1.00 20.59 ?  74  PRO   B HG2  1 
ATOM   4881 H  HG3  . PRO   B 1 74  ? 43.698 -13.558 15.402  1.00 20.59 ?  74  PRO   B HG3  1 
ATOM   4882 H  HD2  . PRO   B 1 74  ? 43.540 -11.071 14.870  1.00 19.58 ?  74  PRO   B HD2  1 
ATOM   4883 H  HD3  . PRO   B 1 74  ? 44.973 -11.792 14.884  1.00 19.58 ?  74  PRO   B HD3  1 
ATOM   4884 N  N    . LEU   B 1 75  ? 42.620 -13.579 10.441  1.00 13.04 ?  75  LEU   B N    1 
ATOM   4885 C  CA   . LEU   B 1 75  ? 41.404 -13.792 9.677   1.00 12.99 ?  75  LEU   B CA   1 
ATOM   4886 C  C    . LEU   B 1 75  ? 40.428 -14.646 10.483  1.00 13.33 ?  75  LEU   B C    1 
ATOM   4887 O  O    . LEU   B 1 75  ? 40.771 -15.222 11.516  1.00 14.57 ?  75  LEU   B O    1 
ATOM   4888 C  CB   . LEU   B 1 75  ? 41.726 -14.515 8.372   1.00 12.98 ?  75  LEU   B CB   1 
ATOM   4889 C  CG   . LEU   B 1 75  ? 42.568 -13.773 7.330   1.00 15.08 ?  75  LEU   B CG   1 
ATOM   4890 C  CD1  . LEU   B 1 75  ? 42.748 -14.604 6.066   1.00 16.60 ?  75  LEU   B CD1  1 
ATOM   4891 C  CD2  . LEU   B 1 75  ? 41.974 -12.432 6.996   1.00 18.65 ?  75  LEU   B CD2  1 
ATOM   4892 H  H    . LEU   B 1 75  ? 43.296 -14.022 10.148  1.00 15.65 ?  75  LEU   B H    1 
ATOM   4893 H  HA   . LEU   B 1 75  ? 40.984 -12.941 9.473   1.00 15.59 ?  75  LEU   B HA   1 
ATOM   4894 H  HB2  . LEU   B 1 75  ? 42.202 -15.333 8.590   1.00 15.57 ?  75  LEU   B HB2  1 
ATOM   4895 H  HB3  . LEU   B 1 75  ? 40.887 -14.747 7.940   1.00 15.57 ?  75  LEU   B HB3  1 
ATOM   4896 H  HG   . LEU   B 1 75  ? 43.451 -13.620 7.703   1.00 18.09 ?  75  LEU   B HG   1 
ATOM   4897 H  HD11 . LEU   B 1 75  ? 43.293 -14.106 5.433   1.00 19.91 ?  75  LEU   B HD11 1 
ATOM   4898 H  HD12 . LEU   B 1 75  ? 43.190 -15.439 6.292   1.00 19.91 ?  75  LEU   B HD12 1 
ATOM   4899 H  HD13 . LEU   B 1 75  ? 41.878 -14.786 5.678   1.00 19.91 ?  75  LEU   B HD13 1 
ATOM   4900 H  HD21 . LEU   B 1 75  ? 42.463 -12.045 6.254   1.00 22.37 ?  75  LEU   B HD21 1 
ATOM   4901 H  HD22 . LEU   B 1 75  ? 41.043 -12.551 6.757   1.00 22.37 ?  75  LEU   B HD22 1 
ATOM   4902 H  HD23 . LEU   B 1 75  ? 42.045 -11.854 7.774   1.00 22.37 ?  75  LEU   B HD23 1 
ATOM   4903 N  N    . LYS   B 1 76  ? 39.191 -14.722 9.989   1.00 14.60 ?  76  LYS   B N    1 
ATOM   4904 C  CA   . LYS   B 1 76  ? 38.205 -15.683 10.465  1.00 15.64 ?  76  LYS   B CA   1 
ATOM   4905 C  C    . LYS   B 1 76  ? 38.314 -16.964 9.644   1.00 14.24 ?  76  LYS   B C    1 
ATOM   4906 O  O    . LYS   B 1 76  ? 38.594 -16.920 8.448   1.00 14.23 ?  76  LYS   B O    1 
ATOM   4907 C  CB   . LYS   B 1 76  ? 36.787 -15.127 10.257  1.00 17.97 ?  76  LYS   B CB   1 
ATOM   4908 C  CG   . LYS   B 1 76  ? 36.496 -13.740 10.860  1.00 19.87 ?  76  LYS   B CG   1 
ATOM   4909 C  CD   . LYS   B 1 76  ? 35.100 -13.213 10.477  1.00 21.13 ?  76  LYS   B CD   1 
ATOM   4910 C  CE   . LYS   B 1 76  ? 34.823 -11.851 11.093  1.00 23.32 ?  76  LYS   B CE   1 
ATOM   4911 N  NZ   . LYS   B 1 76  ? 33.544 -11.258 10.618  1.00 23.88 ?  76  LYS   B NZ   1 
ATOM   4912 H  H    . LYS   B 1 76  ? 38.898 -14.218 9.357   1.00 17.52 ?  76  LYS   B H    1 
ATOM   4913 H  HA   . LYS   B 1 76  ? 38.342 -15.885 11.402  1.00 18.77 ?  76  LYS   B HA   1 
ATOM   4914 H  HB2  . LYS   B 1 76  ? 36.620 -15.064 9.303   1.00 21.56 ?  76  LYS   B HB2  1 
ATOM   4915 H  HB3  . LYS   B 1 76  ? 36.154 -15.748 10.652  1.00 21.56 ?  76  LYS   B HB3  1 
ATOM   4916 H  HG2  . LYS   B 1 76  ? 36.541 -13.797 11.828  1.00 23.83 ?  76  LYS   B HG2  1 
ATOM   4917 H  HG3  . LYS   B 1 76  ? 37.157 -13.106 10.535  1.00 23.83 ?  76  LYS   B HG3  1 
ATOM   4918 H  HD2  . LYS   B 1 76  ? 35.044 -13.124 9.511   1.00 25.35 ?  76  LYS   B HD2  1 
ATOM   4919 H  HD3  . LYS   B 1 76  ? 34.424 -13.831 10.795  1.00 25.35 ?  76  LYS   B HD3  1 
ATOM   4920 H  HE2  . LYS   B 1 76  ? 34.772 -11.944 12.057  1.00 27.98 ?  76  LYS   B HE2  1 
ATOM   4921 H  HE3  . LYS   B 1 76  ? 35.541 -11.243 10.855  1.00 27.98 ?  76  LYS   B HE3  1 
ATOM   4922 H  HZ1  . LYS   B 1 76  ? 33.412 -10.463 10.998  1.00 28.65 ?  76  LYS   B HZ1  1 
ATOM   4923 H  HZ2  . LYS   B 1 76  ? 33.562 -11.154 9.733   1.00 28.65 ?  76  LYS   B HZ2  1 
ATOM   4924 H  HZ3  . LYS   B 1 76  ? 32.861 -11.792 10.829  1.00 28.65 ?  76  LYS   B HZ3  1 
ATOM   4925 N  N    . VAL   B 1 77  ? 38.064 -18.111 10.284  1.00 14.87 ?  77  VAL   B N    1 
ATOM   4926 C  CA   . VAL   B 1 77  ? 37.861 -19.330 9.508   1.00 15.34 ?  77  VAL   B CA   1 
ATOM   4927 C  C    . VAL   B 1 77  ? 36.671 -19.108 8.586   1.00 14.09 ?  77  VAL   B C    1 
ATOM   4928 O  O    . VAL   B 1 77  ? 35.600 -18.673 9.027   1.00 13.83 ?  77  VAL   B O    1 
ATOM   4929 C  CB   . VAL   B 1 77  ? 37.656 -20.546 10.424  1.00 16.94 ?  77  VAL   B CB   1 
ATOM   4930 C  CG1  . VAL   B 1 77  ? 37.402 -21.793 9.580   1.00 17.55 ?  77  VAL   B CG1  1 
ATOM   4931 C  CG2  . VAL   B 1 77  ? 38.869 -20.752 11.338  1.00 18.35 ?  77  VAL   B CG2  1 
ATOM   4932 H  H    . VAL   B 1 77  ? 38.008 -18.204 11.133  1.00 17.84 ?  77  VAL   B H    1 
ATOM   4933 H  HA   . VAL   B 1 77  ? 38.638 -19.489 8.955   1.00 18.40 ?  77  VAL   B HA   1 
ATOM   4934 H  HB   . VAL   B 1 77  ? 36.874 -20.394 10.981  1.00 20.32 ?  77  VAL   B HB   1 
ATOM   4935 H  HG11 . VAL   B 1 77  ? 37.452 -22.572 10.153  1.00 21.05 ?  77  VAL   B HG11 1 
ATOM   4936 H  HG12 . VAL   B 1 77  ? 36.520 -21.734 9.179   1.00 21.05 ?  77  VAL   B HG12 1 
ATOM   4937 H  HG13 . VAL   B 1 77  ? 38.078 -21.846 8.888   1.00 21.05 ?  77  VAL   B HG13 1 
ATOM   4938 H  HG21 . VAL   B 1 77  ? 38.726 -21.548 11.867  1.00 22.02 ?  77  VAL   B HG21 1 
ATOM   4939 H  HG22 . VAL   B 1 77  ? 39.658 -20.850 10.787  1.00 22.02 ?  77  VAL   B HG22 1 
ATOM   4940 H  HG23 . VAL   B 1 77  ? 38.958 -19.977 11.915  1.00 22.02 ?  77  VAL   B HG23 1 
ATOM   4941 N  N    . GLY   B 1 78  ? 36.858 -19.389 7.298   1.00 13.76 ?  78  GLY   B N    1 
ATOM   4942 C  CA   . GLY   B 1 78  ? 35.881 -19.073 6.281   1.00 13.14 ?  78  GLY   B CA   1 
ATOM   4943 C  C    . GLY   B 1 78  ? 36.122 -17.759 5.574   1.00 12.83 ?  78  GLY   B C    1 
ATOM   4944 O  O    . GLY   B 1 78  ? 35.429 -17.476 4.589   1.00 13.25 ?  78  GLY   B O    1 
ATOM   4945 H  H    . GLY   B 1 78  ? 37.560 -19.775 6.988   1.00 16.50 ?  78  GLY   B H    1 
ATOM   4946 H  HA2  . GLY   B 1 78  ? 35.879 -19.771 5.613   1.00 15.76 ?  78  GLY   B HA2  1 
ATOM   4947 H  HA3  . GLY   B 1 78  ? 35.000 -19.034 6.685   1.00 15.76 ?  78  GLY   B HA3  1 
ATOM   4948 N  N    . GLY   B 1 79  ? 37.068 -16.947 6.056   1.00 12.85 ?  79  GLY   B N    1 
ATOM   4949 C  CA   . GLY   B 1 79  ? 37.360 -15.652 5.479   1.00 12.68 ?  79  GLY   B CA   1 
ATOM   4950 C  C    . GLY   B 1 79  ? 38.591 -15.668 4.582   1.00 12.07 ?  79  GLY   B C    1 
ATOM   4951 O  O    . GLY   B 1 79  ? 39.206 -16.705 4.337   1.00 12.56 ?  79  GLY   B O    1 
ATOM   4952 H  H    . GLY   B 1 79  ? 37.567 -17.137 6.731   1.00 15.41 ?  79  GLY   B H    1 
ATOM   4953 H  HA2  . GLY   B 1 79  ? 36.606 -15.355 4.948   1.00 15.21 ?  79  GLY   B HA2  1 
ATOM   4954 H  HA3  . GLY   B 1 79  ? 37.510 -15.007 6.188   1.00 15.21 ?  79  GLY   B HA3  1 
ATOM   4955 N  N    . SER   B 1 80  ? 38.953 -14.476 4.099   1.00 11.80 ?  80  SER   B N    1 
ATOM   4956 C  CA   . SER   B 1 80  ? 40.060 -14.345 3.162   1.00 11.72 ?  80  SER   B CA   1 
ATOM   4957 C  C    . SER   B 1 80  ? 40.637 -12.939 3.212   1.00 11.70 ?  80  SER   B C    1 
ATOM   4958 O  O    . SER   B 1 80  ? 40.018 -12.004 3.728   1.00 12.79 ?  80  SER   B O    1 
ATOM   4959 C  CB   . SER   B 1 80  ? 39.619 -14.640 1.725   1.00 12.59 ?  80  SER   B CB   1 
ATOM   4960 O  OG   . SER   B 1 80  ? 38.776 -13.622 1.209   1.00 13.16 ?  80  SER   B OG   1 
ATOM   4961 H  H    . SER   B 1 80  ? 38.577 -13.731 4.308   1.00 14.15 ?  80  SER   B H    1 
ATOM   4962 H  HA   . SER   B 1 80  ? 40.756 -14.971 3.411   1.00 14.06 ?  80  SER   B HA   1 
ATOM   4963 H  HB2  . SER   B 1 80  ? 40.405 -14.701 1.160   1.00 15.10 ?  80  SER   B HB2  1 
ATOM   4964 H  HB3  . SER   B 1 80  ? 39.136 -15.480 1.711   1.00 15.10 ?  80  SER   B HB3  1 
ATOM   4965 H  HG   . SER   B 1 80  ? 38.083 -13.552 1.692   1.00 15.79 ?  80  SER   B HG   1 
ATOM   4966 N  N    . CYS   B 1 81  ? 41.829 -12.795 2.634   1.00 11.64 ?  81  CYS   B N    1 
ATOM   4967 C  CA   . CYS   B 1 81  ? 42.378 -11.485 2.314   1.00 11.64 ?  81  CYS   B CA   1 
ATOM   4968 C  C    . CYS   B 1 81  ? 43.138 -11.571 0.998   1.00 11.10 ?  81  CYS   B C    1 
ATOM   4969 O  O    . CYS   B 1 81  ? 43.631 -12.637 0.609   1.00 12.14 ?  81  CYS   B O    1 
ATOM   4970 C  CB   . CYS   B 1 81  ? 43.283 -10.931 3.425   1.00 12.45 ?  81  CYS   B CB   1 
ATOM   4971 S  SG   . CYS   B 1 81  ? 44.794 -11.878 3.672   1.00 12.85 ?  81  CYS   B SG   1 
ATOM   4972 H  H    . CYS   B 1 81  ? 42.347 -13.451 2.415   1.00 13.96 ?  81  CYS   B H    1 
ATOM   4973 H  HA   . CYS   B 1 81  ? 41.644 -10.859 2.194   1.00 13.96 ?  81  CYS   B HA   1 
ATOM   4974 H  HB2  . CYS   B 1 81  ? 43.536 -10.020 3.199   1.00 14.94 ?  81  CYS   B HB2  1 
ATOM   4975 H  HB3  . CYS   B 1 81  ? 42.787 -10.931 4.262   1.00 14.94 ?  81  CYS   B HB3  1 
ATOM   4976 H  HG   . CYS   B 1 81  ? 45.434 -11.378 4.557   1.00 15.42 ?  81  CYS   B HG   1 
ATOM   4977 N  N    . VAL   B 1 82  ? 43.252 -10.425 0.329   1.00 11.36 ?  82  VAL   B N    1 
ATOM   4978 C  CA   . VAL   B 1 82  ? 44.007 -10.300 -0.915  1.00 11.71 ?  82  VAL   B CA   1 
ATOM   4979 C  C    . VAL   B 1 82  ? 45.353 -9.663  -0.607  1.00 12.02 ?  82  VAL   B C    1 
ATOM   4980 O  O    . VAL   B 1 82  ? 45.409 -8.550  -0.070  1.00 13.13 ?  82  VAL   B O    1 
ATOM   4981 C  CB   . VAL   B 1 82  ? 43.250 -9.458  -1.954  1.00 12.84 ?  82  VAL   B CB   1 
ATOM   4982 C  CG1  . VAL   B 1 82  ? 44.086 -9.313  -3.224  1.00 14.05 ?  82  VAL   B CG1  1 
ATOM   4983 C  CG2  . VAL   B 1 82  ? 41.894 -10.069 -2.259  1.00 14.02 ?  82  VAL   B CG2  1 
ATOM   4984 H  H    . VAL   B 1 82  ? 42.882 -9.682  0.579   1.00 13.63 ?  82  VAL   B H    1 
ATOM   4985 H  HA   . VAL   B 1 82  ? 44.160 -11.179 -1.288  1.00 14.04 ?  82  VAL   B HA   1 
ATOM   4986 H  HB   . VAL   B 1 82  ? 43.103 -8.569  -1.596  1.00 15.40 ?  82  VAL   B HB   1 
ATOM   4987 H  HG11 . VAL   B 1 82  ? 43.520 -8.989  -3.942  1.00 16.86 ?  82  VAL   B HG11 1 
ATOM   4988 H  HG12 . VAL   B 1 82  ? 44.806 -8.679  -3.063  1.00 16.86 ?  82  VAL   B HG12 1 
ATOM   4989 H  HG13 . VAL   B 1 82  ? 44.456 -10.178 -3.461  1.00 16.86 ?  82  VAL   B HG13 1 
ATOM   4990 H  HG21 . VAL   B 1 82  ? 41.455 -9.545  -2.950  1.00 16.82 ?  82  VAL   B HG21 1 
ATOM   4991 H  HG22 . VAL   B 1 82  ? 42.018 -10.981 -2.567  1.00 16.82 ?  82  VAL   B HG22 1 
ATOM   4992 H  HG23 . VAL   B 1 82  ? 41.355 -10.065 -1.452  1.00 16.82 ?  82  VAL   B HG23 1 
ATOM   4993 N  N    . LEU   B 1 83  ? 46.431 -10.350 -0.974  1.00 11.53 ?  83  LEU   B N    1 
ATOM   4994 C  CA   . LEU   B 1 83  ? 47.786 -9.829  -0.861  1.00 11.28 ?  83  LEU   B CA   1 
ATOM   4995 C  C    . LEU   B 1 83  ? 48.479 -9.976  -2.216  1.00 11.53 ?  83  LEU   B C    1 
ATOM   4996 O  O    . LEU   B 1 83  ? 47.870 -10.399 -3.205  1.00 11.72 ?  83  LEU   B O    1 
ATOM   4997 C  CB   . LEU   B 1 83  ? 48.541 -10.504 0.290   1.00 12.09 ?  83  LEU   B CB   1 
ATOM   4998 C  CG   . LEU   B 1 83  ? 48.034 -10.146 1.694   1.00 13.24 ?  83  LEU   B CG   1 
ATOM   4999 C  CD1  . LEU   B 1 83  ? 48.673 -11.015 2.755   1.00 13.92 ?  83  LEU   B CD1  1 
ATOM   5000 C  CD2  . LEU   B 1 83  ? 48.241 -8.673  2.022   1.00 14.34 ?  83  LEU   B CD2  1 
ATOM   5001 H  H    . LEU   B 1 83  ? 46.394 -11.144 -1.305  1.00 13.83 ?  83  LEU   B H    1 
ATOM   5002 H  HA   . LEU   B 1 83  ? 47.731 -8.881  -0.667  1.00 13.53 ?  83  LEU   B HA   1 
ATOM   5003 H  HB2  . LEU   B 1 83  ? 48.469 -11.462 0.187   1.00 14.50 ?  83  LEU   B HB2  1 
ATOM   5004 H  HB3  . LEU   B 1 83  ? 49.472 -10.237 0.239   1.00 14.50 ?  83  LEU   B HB3  1 
ATOM   5005 H  HG   . LEU   B 1 83  ? 47.081 -10.314 1.720   1.00 15.89 ?  83  LEU   B HG   1 
ATOM   5006 H  HD11 . LEU   B 1 83  ? 48.317 -10.768 3.623   1.00 16.69 ?  83  LEU   B HD11 1 
ATOM   5007 H  HD12 . LEU   B 1 83  ? 48.461 -11.947 2.569   1.00 16.69 ?  83  LEU   B HD12 1 
ATOM   5008 H  HD13 . LEU   B 1 83  ? 49.632 -10.887 2.739   1.00 16.69 ?  83  LEU   B HD13 1 
ATOM   5009 H  HD21 . LEU   B 1 83  ? 48.027 -8.526  2.957   1.00 17.20 ?  83  LEU   B HD21 1 
ATOM   5010 H  HD22 . LEU   B 1 83  ? 49.166 -8.438  1.853   1.00 17.20 ?  83  LEU   B HD22 1 
ATOM   5011 H  HD23 . LEU   B 1 83  ? 47.655 -8.139  1.462   1.00 17.20 ?  83  LEU   B HD23 1 
ATOM   5012 N  N    . SER   B 1 84  ? 49.754 -9.596  -2.278  1.00 12.68 ?  84  SER   B N    1 
ATOM   5013 C  CA   . SER   B 1 84  ? 50.489 -9.717  -3.529  1.00 12.68 ?  84  SER   B CA   1 
ATOM   5014 C  C    . SER   B 1 84  ? 50.651 -11.179 -3.929  1.00 11.98 ?  84  SER   B C    1 
ATOM   5015 O  O    . SER   B 1 84  ? 50.768 -12.070 -3.086  1.00 12.08 ?  84  SER   B O    1 
ATOM   5016 C  CB   . SER   B 1 84  ? 51.882 -9.107  -3.391  1.00 14.93 ?  84  SER   B CB   1 
ATOM   5017 O  OG   . SER   B 1 84  ? 52.628 -9.334  -4.575  1.00 16.55 ?  84  SER   B OG   1 
ATOM   5018 H  H    . SER   B 1 84  ? 50.199 -9.262  -1.624  1.00 15.21 ?  84  SER   B H    1 
ATOM   5019 H  HA   . SER   B 1 84  ? 50.014 -9.255  -4.234  1.00 15.21 ?  84  SER   B HA   1 
ATOM   5020 H  HB2  . SER   B 1 84  ? 51.797 -8.150  -3.241  1.00 17.91 ?  84  SER   B HB2  1 
ATOM   5021 H  HB3  . SER   B 1 84  ? 52.341 -9.520  -2.643  1.00 17.91 ?  84  SER   B HB3  1 
ATOM   5022 H  HG   . SER   B 1 84  ? 53.395 -8.990  -4.503  1.00 19.86 ?  84  SER   B HG   1 
ATOM   5023 N  N    . GLY   B 1 85  ? 50.717 -11.410 -5.237  1.00 13.02 ?  85  GLY   B N    1 
ATOM   5024 C  CA   . GLY   B 1 85  ? 51.059 -12.702 -5.780  1.00 14.19 ?  85  GLY   B CA   1 
ATOM   5025 C  C    . GLY   B 1 85  ? 52.531 -12.901 -6.073  1.00 12.77 ?  85  GLY   B C    1 
ATOM   5026 O  O    . GLY   B 1 85  ? 52.909 -13.984 -6.523  1.00 13.20 ?  85  GLY   B O    1 
ATOM   5027 H  H    . GLY   B 1 85  ? 50.576 -10.815 -5.837  1.00 15.62 ?  85  GLY   B H    1 
ATOM   5028 H  HA2  . GLY   B 1 85  ? 50.788 -13.390 -5.151  1.00 17.02 ?  85  GLY   B HA2  1 
ATOM   5029 H  HA3  . GLY   B 1 85  ? 50.569 -12.839 -6.602  1.00 17.02 ?  85  GLY   B HA3  1 
ATOM   5030 N  N    . HIS   B 1 86  ? 53.384 -11.902 -5.854  1.00 12.72 ?  86  HIS   B N    1 
ATOM   5031 C  CA   . HIS   B 1 86  ? 54.848 -12.065 -5.948  1.00 12.99 ?  86  HIS   B CA   1 
ATOM   5032 C  C    . HIS   B 1 86  ? 55.213 -12.585 -7.337  1.00 13.16 ?  86  HIS   B C    1 
ATOM   5033 O  O    . HIS   B 1 86  ? 54.816 -11.977 -8.343  1.00 13.85 ?  86  HIS   B O    1 
ATOM   5034 C  CB   . HIS   B 1 86  ? 55.341 -12.904 -4.769  1.00 13.27 ?  86  HIS   B CB   1 
ATOM   5035 C  CG   . HIS   B 1 86  ? 55.025 -12.295 -3.443  1.00 13.40 ?  86  HIS   B CG   1 
ATOM   5036 N  ND1  . HIS   B 1 86  ? 55.850 -11.381 -2.826  1.00 15.13 ?  86  HIS   B ND1  1 
ATOM   5037 C  CD2  . HIS   B 1 86  ? 53.953 -12.445 -2.629  1.00 13.92 ?  86  HIS   B CD2  1 
ATOM   5038 C  CE1  . HIS   B 1 86  ? 55.297 -10.992 -1.691  1.00 14.89 ?  86  HIS   B CE1  1 
ATOM   5039 N  NE2  . HIS   B 1 86  ? 54.144 -11.621 -1.548  1.00 14.47 ?  86  HIS   B NE2  1 
ATOM   5040 H  H    . HIS   B 1 86  ? 53.141 -11.106 -5.649  1.00 15.26 ?  86  HIS   B H    1 
ATOM   5041 H  HA   . HIS   B 1 86  ? 55.252 -11.194 -5.856  1.00 15.58 ?  86  HIS   B HA   1 
ATOM   5042 H  HB2  . HIS   B 1 86  ? 54.927 -13.779 -4.801  1.00 15.92 ?  86  HIS   B HB2  1 
ATOM   5043 H  HB3  . HIS   B 1 86  ? 56.307 -12.994 -4.827  1.00 15.92 ?  86  HIS   B HB3  1 
ATOM   5044 H  HD2  . HIS   B 1 86  ? 53.216 -12.997 -2.779  1.00 16.70 ?  86  HIS   B HD2  1 
ATOM   5045 H  HE1  . HIS   B 1 86  ? 55.662 -10.390 -1.082  1.00 17.86 ?  86  HIS   B HE1  1 
ATOM   5046 H  HE2  . HIS   B 1 86  ? 53.607 -11.546 -0.876  1.00 17.35 ?  86  HIS   B HE2  1 
ATOM   5047 N  N    . ASN   B 1 87  ? 55.972 -13.675 -7.445  1.00 13.48 ?  87  ASN   B N    1 
ATOM   5048 C  CA   . ASN   B 1 87  ? 56.361 -14.250 -8.723  1.00 14.39 ?  87  ASN   B CA   1 
ATOM   5049 C  C    . ASN   B 1 87  ? 55.370 -15.290 -9.226  1.00 13.81 ?  87  ASN   B C    1 
ATOM   5050 O  O    . ASN   B 1 87  ? 55.673 -15.997 -10.193 1.00 15.55 ?  87  ASN   B O    1 
ATOM   5051 C  CB   . ASN   B 1 87  ? 57.754 -14.883 -8.615  1.00 16.19 ?  87  ASN   B CB   1 
ATOM   5052 C  CG   . ASN   B 1 87  ? 57.815 -16.001 -7.574  1.00 16.90 ?  87  ASN   B CG   1 
ATOM   5053 O  OD1  . ASN   B 1 87  ? 57.184 -15.922 -6.514  1.00 15.79 ?  87  ASN   B OD1  1 
ATOM   5054 N  ND2  . ASN   B 1 87  ? 58.567 -17.061 -7.887  1.00 19.57 ?  87  ASN   B ND2  1 
ATOM   5055 H  H    . ASN   B 1 87  ? 56.275 -14.116 -6.770  1.00 16.18 ?  87  ASN   B H    1 
ATOM   5056 H  HA   . ASN   B 1 87  ? 56.407 -13.545 -9.382  1.00 17.26 ?  87  ASN   B HA   1 
ATOM   5057 H  HB2  . ASN   B 1 87  ? 57.999 -15.259 -9.478  1.00 19.42 ?  87  ASN   B HB2  1 
ATOM   5058 H  HB3  . ASN   B 1 87  ? 58.392 -14.200 -8.360  1.00 19.42 ?  87  ASN   B HB3  1 
ATOM   5059 H  HD21 . ASN   B 1 87  ? 58.640 -17.716 -7.338  1.00 23.47 ?  87  ASN   B HD21 1 
ATOM   5060 H  HD22 . ASN   B 1 87  ? 58.992 -17.084 -8.640  1.00 23.47 ?  87  ASN   B HD22 1 
ATOM   5061 N  N    . LEU   B 1 88  ? 54.196 -15.398 -8.598  1.00 12.85 ?  88  LEU   B N    1 
ATOM   5062 C  CA   . LEU   B 1 88  ? 53.211 -16.424 -8.922  1.00 13.08 ?  88  LEU   B CA   1 
ATOM   5063 C  C    . LEU   B 1 88  ? 51.979 -15.900 -9.642  1.00 12.92 ?  88  LEU   B C    1 
ATOM   5064 O  O    . LEU   B 1 88  ? 51.370 -16.645 -10.420 1.00 14.69 ?  88  LEU   B O    1 
ATOM   5065 C  CB   . LEU   B 1 88  ? 52.744 -17.114 -7.636  1.00 13.73 ?  88  LEU   B CB   1 
ATOM   5066 C  CG   . LEU   B 1 88  ? 53.873 -17.771 -6.854  1.00 15.89 ?  88  LEU   B CG   1 
ATOM   5067 C  CD1  . LEU   B 1 88  ? 53.390 -18.140 -5.462  1.00 17.87 ?  88  LEU   B CD1  1 
ATOM   5068 C  CD2  . LEU   B 1 88  ? 54.360 -18.992 -7.603  1.00 19.60 ?  88  LEU   B CD2  1 
ATOM   5069 H  H    . LEU   B 1 88  ? 53.944 -14.873 -7.960  1.00 15.41 ?  88  LEU   B H    1 
ATOM   5070 H  HA   . LEU   B 1 88  ? 53.621 -17.088 -9.487  1.00 15.69 ?  88  LEU   B HA   1 
ATOM   5071 H  HB2  . LEU   B 1 88  ? 52.322 -16.458 -7.058  1.00 16.47 ?  88  LEU   B HB2  1 
ATOM   5072 H  HB3  . LEU   B 1 88  ? 52.100 -17.805 -7.869  1.00 16.47 ?  88  LEU   B HB3  1 
ATOM   5073 H  HG   . LEU   B 1 88  ? 54.610 -17.147 -6.770  1.00 19.07 ?  88  LEU   B HG   1 
ATOM   5074 H  HD11 . LEU   B 1 88  ? 54.045 -18.724 -5.049  1.00 21.43 ?  88  LEU   B HD11 1 
ATOM   5075 H  HD12 . LEU   B 1 88  ? 53.290 -17.329 -4.939  1.00 21.43 ?  88  LEU   B HD12 1 
ATOM   5076 H  HD13 . LEU   B 1 88  ? 52.539 -18.594 -5.538  1.00 21.43 ?  88  LEU   B HD13 1 
ATOM   5077 H  HD21 . LEU   B 1 88  ? 55.005 -19.459 -7.052  1.00 23.51 ?  88  LEU   B HD21 1 
ATOM   5078 H  HD22 . LEU   B 1 88  ? 53.602 -19.569 -7.789  1.00 23.51 ?  88  LEU   B HD22 1 
ATOM   5079 H  HD23 . LEU   B 1 88  ? 54.773 -18.711 -8.434  1.00 23.51 ?  88  LEU   B HD23 1 
ATOM   5080 N  N    . ALA   B 1 89  ? 51.583 -14.660 -9.378  1.00 12.34 ?  89  ALA   B N    1 
ATOM   5081 C  CA   . ALA   B 1 89  ? 50.294 -14.154 -9.821  1.00 11.54 ?  89  ALA   B CA   1 
ATOM   5082 C  C    . ALA   B 1 89  ? 50.273 -12.664 -9.534  1.00 12.30 ?  89  ALA   B C    1 
ATOM   5083 O  O    . ALA   B 1 89  ? 51.111 -12.150 -8.792  1.00 12.96 ?  89  ALA   B O    1 
ATOM   5084 C  CB   . ALA   B 1 89  ? 49.155 -14.828 -9.065  1.00 11.69 ?  89  ALA   B CB   1 
ATOM   5085 H  H    . ALA   B 1 89  ? 52.044 -14.079 -8.936  1.00 14.81 ?  89  ALA   B H    1 
ATOM   5086 H  HA   . ALA   B 1 89  ? 50.181 -14.299 -10.779 1.00 13.85 ?  89  ALA   B HA   1 
ATOM   5087 H  HB1  . ALA   B 1 89  ? 48.308 -14.489 -9.405  1.00 14.02 ?  89  ALA   B HB1  1 
ATOM   5088 H  HB2  . ALA   B 1 89  ? 49.205 -15.786 -9.215  1.00 14.02 ?  89  ALA   B HB2  1 
ATOM   5089 H  HB3  . ALA   B 1 89  ? 49.241 -14.630 -8.127  1.00 14.02 ?  89  ALA   B HB3  1 
ATOM   5090 N  N    . LYS   B 1 90  ? 49.290 -11.969 -10.101 1.00 13.03 ?  90  LYS   B N    1 
ATOM   5091 C  CA   . LYS   B 1 90  ? 49.099 -10.582 -9.695  1.00 13.10 ?  90  LYS   B CA   1 
ATOM   5092 C  C    . LYS   B 1 90  ? 48.785 -10.509 -8.206  1.00 12.80 ?  90  LYS   B C    1 
ATOM   5093 O  O    . LYS   B 1 90  ? 49.423 -9.749  -7.462  1.00 13.57 ?  90  LYS   B O    1 
ATOM   5094 C  CB   . LYS   B 1 90  ? 48.012 -9.920  -10.543 1.00 14.70 ?  90  LYS   B CB   1 
ATOM   5095 C  CG   . LYS   B 1 90  ? 47.716 -8.473  -10.161 1.00 15.16 ?  90  LYS   B CG   1 
ATOM   5096 C  CD   . LYS   B 1 90  ? 48.924 -7.575  -10.245 1.00 18.38 ?  90  LYS   B CD   1 
ATOM   5097 C  CE   . LYS   B 1 90  ? 48.484 -6.149  -10.005 1.00 20.76 ?  90  LYS   B CE   1 
ATOM   5098 N  NZ   . LYS   B 1 90  ? 49.635 -5.226  -9.870  1.00 20.41 ?  90  LYS   B NZ   1 
ATOM   5099 H  H    . LYS   B 1 90  ? 48.737 -12.267 -10.694 1.00 15.63 ?  90  LYS   B H    1 
ATOM   5100 H  HA   . LYS   B 1 90  ? 49.920 -10.100 -9.851  1.00 15.72 ?  90  LYS   B HA   1 
ATOM   5101 H  HB2  . LYS   B 1 90  ? 48.290 -9.925  -11.475 1.00 17.63 ?  90  LYS   B HB2  1 
ATOM   5102 H  HB3  . LYS   B 1 90  ? 47.185 -10.426 -10.453 1.00 17.63 ?  90  LYS   B HB3  1 
ATOM   5103 H  HG2  . LYS   B 1 90  ? 47.036 -8.122  -10.763 1.00 18.19 ?  90  LYS   B HG2  1 
ATOM   5104 H  HG3  . LYS   B 1 90  ? 47.379 -8.450  -9.248  1.00 18.19 ?  90  LYS   B HG3  1 
ATOM   5105 H  HD2  . LYS   B 1 90  ? 49.564 -7.823  -9.560  1.00 22.05 ?  90  LYS   B HD2  1 
ATOM   5106 H  HD3  . LYS   B 1 90  ? 49.319 -7.639  -11.127 1.00 22.05 ?  90  LYS   B HD3  1 
ATOM   5107 H  HE2  . LYS   B 1 90  ? 47.947 -5.846  -10.757 1.00 24.90 ?  90  LYS   B HE2  1 
ATOM   5108 H  HE3  . LYS   B 1 90  ? 47.966 -6.101  -9.187  1.00 24.90 ?  90  LYS   B HE3  1 
ATOM   5109 H  HZ1  . LYS   B 1 90  ? 49.349 -4.393  -9.733  1.00 24.49 ?  90  LYS   B HZ1  1 
ATOM   5110 H  HZ2  . LYS   B 1 90  ? 50.145 -5.472  -9.184  1.00 24.49 ?  90  LYS   B HZ2  1 
ATOM   5111 H  HZ3  . LYS   B 1 90  ? 50.127 -5.240  -10.614 1.00 24.49 ?  90  LYS   B HZ3  1 
ATOM   5112 N  N    . HIS   B 1 91  ? 47.824 -11.320 -7.753  1.00 11.27 ?  91  HIS   B N    1 
ATOM   5113 C  CA   . HIS   B 1 91  ? 47.369 -11.339 -6.378  1.00 11.70 ?  91  HIS   B CA   1 
ATOM   5114 C  C    . HIS   B 1 91  ? 47.357 -12.766 -5.858  1.00 10.86 ?  91  HIS   B C    1 
ATOM   5115 O  O    . HIS   B 1 91  ? 47.125 -13.717 -6.611  1.00 11.59 ?  91  HIS   B O    1 
ATOM   5116 C  CB   . HIS   B 1 91  ? 45.919 -10.850 -6.254  1.00 13.19 ?  91  HIS   B CB   1 
ATOM   5117 C  CG   . HIS   B 1 91  ? 45.712 -9.439  -6.688  1.00 16.15 ?  91  HIS   B CG   1 
ATOM   5118 N  ND1  . HIS   B 1 91  ? 46.323 -8.370  -6.069  1.00 18.95 ?  91  HIS   B ND1  1 
ATOM   5119 C  CD2  . HIS   B 1 91  ? 44.936 -8.917  -7.664  1.00 19.26 ?  91  HIS   B CD2  1 
ATOM   5120 C  CE1  . HIS   B 1 91  ? 45.944 -7.248  -6.657  1.00 20.32 ?  91  HIS   B CE1  1 
ATOM   5121 N  NE2  . HIS   B 1 91  ? 45.098 -7.552  -7.626  1.00 20.81 ?  91  HIS   B NE2  1 
ATOM   5122 H  H    . HIS   B 1 91  ? 47.406 -11.883 -8.249  1.00 13.52 ?  91  HIS   B H    1 
ATOM   5123 H  HA   . HIS   B 1 91  ? 47.949 -10.786 -5.816  1.00 14.03 ?  91  HIS   B HA   1 
ATOM   5124 H  HB2  . HIS   B 1 91  ? 45.355 -11.413 -6.802  1.00 15.83 ?  91  HIS   B HB2  1 
ATOM   5125 H  HB3  . HIS   B 1 91  ? 45.645 -10.916 -5.323  1.00 15.83 ?  91  HIS   B HB3  1 
ATOM   5126 H  HD2  . HIS   B 1 91  ? 44.399 -9.387  -8.256  1.00 23.10 ?  91  HIS   B HD2  1 
ATOM   5127 H  HE1  . HIS   B 1 91  ? 46.219 -6.387  -6.424  1.00 24.38 ?  91  HIS   B HE1  1 
ATOM   5128 H  HE2  . HIS   B 1 91  ? 44.721 -6.984  -8.154  1.00 24.97 ?  91  HIS   B HE2  1 
ATOM   5129 N  N    . CYS   B 1 92  ? 47.541 -12.900 -4.554  1.00 10.84 ?  92  CYS   B N    1 
ATOM   5130 C  CA   . CYS   B 1 92  ? 47.246 -14.138 -3.850  1.00 10.72 ?  92  CYS   B CA   1 
ATOM   5131 C  C    . CYS   B 1 92  ? 46.029 -13.902 -2.964  1.00 10.40 ?  92  CYS   B C    1 
ATOM   5132 O  O    . CYS   B 1 92  ? 46.032 -13.000 -2.117  1.00 11.25 ?  92  CYS   B O    1 
ATOM   5133 C  CB   . CYS   B 1 92  ? 48.428 -14.603 -3.001  1.00 11.29 ?  92  CYS   B CB   1 
ATOM   5134 S  SG   . CYS   B 1 92  ? 48.068 -16.136 -2.095  1.00 11.46 ?  92  CYS   B SG   1 
ATOM   5135 H  H    . CYS   B 1 92  ? 47.851 -12.277 -4.042  1.00 13.00 ?  92  CYS   B H    1 
ATOM   5136 H  HA   . CYS   B 1 92  ? 47.039 -14.834 -4.496  1.00 12.86 ?  92  CYS   B HA   1 
ATOM   5137 H  HB2  . CYS   B 1 92  ? 49.185 -14.762 -3.578  1.00 13.54 ?  92  CYS   B HB2  1 
ATOM   5138 H  HB3  . CYS   B 1 92  ? 48.632 -13.914 -2.353  1.00 13.54 ?  92  CYS   B HB3  1 
ATOM   5139 H  HG   . CYS   B 1 92  ? 49.045 -16.450 -1.474  1.00 13.75 ?  92  CYS   B HG   1 
ATOM   5140 N  N    . LEU   B 1 93  ? 44.988 -14.707 -3.173  1.00 10.44 ?  93  LEU   B N    1 
ATOM   5141 C  CA   . LEU   B 1 93  ? 43.815 -14.727 -2.307  1.00 10.65 ?  93  LEU   B CA   1 
ATOM   5142 C  C    . LEU   B 1 93  ? 44.042 -15.792 -1.241  1.00 9.89  ?  93  LEU   B C    1 
ATOM   5143 O  O    . LEU   B 1 93  ? 43.995 -16.993 -1.532  1.00 10.70 ?  93  LEU   B O    1 
ATOM   5144 C  CB   . LEU   B 1 93  ? 42.552 -15.014 -3.118  1.00 10.68 ?  93  LEU   B CB   1 
ATOM   5145 C  CG   . LEU   B 1 93  ? 41.255 -15.032 -2.305  1.00 11.60 ?  93  LEU   B CG   1 
ATOM   5146 C  CD1  . LEU   B 1 93  ? 40.878 -13.653 -1.791  1.00 12.20 ?  93  LEU   B CD1  1 
ATOM   5147 C  CD2  . LEU   B 1 93  ? 40.122 -15.643 -3.123  1.00 11.69 ?  93  LEU   B CD2  1 
ATOM   5148 H  H    . LEU   B 1 93  ? 44.941 -15.279 -3.826  1.00 12.52 ?  93  LEU   B H    1 
ATOM   5149 H  HA   . LEU   B 1 93  ? 43.723 -13.868 -1.874  1.00 12.77 ?  93  LEU   B HA   1 
ATOM   5150 H  HB2  . LEU   B 1 93  ? 42.462 -14.321 -3.794  1.00 12.81 ?  93  LEU   B HB2  1 
ATOM   5151 H  HB3  . LEU   B 1 93  ? 42.644 -15.875 -3.543  1.00 12.81 ?  93  LEU   B HB3  1 
ATOM   5152 H  HG   . LEU   B 1 93  ? 41.387 -15.599 -1.534  1.00 13.92 ?  93  LEU   B HG   1 
ATOM   5153 H  HD11 . LEU   B 1 93  ? 40.034 -13.716 -1.318  1.00 14.64 ?  93  LEU   B HD11 1 
ATOM   5154 H  HD12 . LEU   B 1 93  ? 41.572 -13.341 -1.191  1.00 14.64 ?  93  LEU   B HD12 1 
ATOM   5155 H  HD13 . LEU   B 1 93  ? 40.792 -13.048 -2.544  1.00 14.64 ?  93  LEU   B HD13 1 
ATOM   5156 H  HD21 . LEU   B 1 93  ? 39.310 -15.640 -2.589  1.00 14.02 ?  93  LEU   B HD21 1 
ATOM   5157 H  HD22 . LEU   B 1 93  ? 39.989 -15.120 -3.928  1.00 14.02 ?  93  LEU   B HD22 1 
ATOM   5158 H  HD23 . LEU   B 1 93  ? 40.357 -16.556 -3.357  1.00 14.02 ?  93  LEU   B HD23 1 
ATOM   5159 N  N    . HIS   B 1 94  ? 44.323 -15.357 -0.021  1.00 10.11 ?  94  HIS   B N    1 
ATOM   5160 C  CA   . HIS   B 1 94  ? 44.543 -16.257 1.105   1.00 10.23 ?  94  HIS   B CA   1 
ATOM   5161 C  C    . HIS   B 1 94  ? 43.184 -16.612 1.693   1.00 10.73 ?  94  HIS   B C    1 
ATOM   5162 O  O    . HIS   B 1 94  ? 42.513 -15.740 2.247   1.00 12.15 ?  94  HIS   B O    1 
ATOM   5163 C  CB   . HIS   B 1 94  ? 45.418 -15.577 2.158   1.00 10.59 ?  94  HIS   B CB   1 
ATOM   5164 C  CG   . HIS   B 1 94  ? 46.797 -15.276 1.682   1.00 10.65 ?  94  HIS   B CG   1 
ATOM   5165 N  ND1  . HIS   B 1 94  ? 47.822 -16.194 1.761   1.00 10.88 ?  94  HIS   B ND1  1 
ATOM   5166 C  CD2  . HIS   B 1 94  ? 47.305 -14.168 1.092   1.00 10.76 ?  94  HIS   B CD2  1 
ATOM   5167 C  CE1  . HIS   B 1 94  ? 48.912 -15.650 1.249   1.00 11.17 ?  94  HIS   B CE1  1 
ATOM   5168 N  NE2  . HIS   B 1 94  ? 48.628 -14.423 0.837   1.00 11.19 ?  94  HIS   B NE2  1 
ATOM   5169 H  H    . HIS   B 1 94  ? 44.403 -14.521 0.184   1.00 12.12 ?  94  HIS   B H    1 
ATOM   5170 H  HA   . HIS   B 1 94  ? 44.983 -17.067 0.802   1.00 12.27 ?  94  HIS   B HA   1 
ATOM   5171 H  HB2  . HIS   B 1 94  ? 45.003 -14.740 2.415   1.00 12.70 ?  94  HIS   B HB2  1 
ATOM   5172 H  HB3  . HIS   B 1 94  ? 45.490 -16.162 2.927   1.00 12.70 ?  94  HIS   B HB3  1 
ATOM   5173 H  HD2  . HIS   B 1 94  ? 46.848 -13.384 0.899   1.00 12.91 ?  94  HIS   B HD2  1 
ATOM   5174 H  HE1  . HIS   B 1 94  ? 49.741 -16.069 1.192   1.00 13.40 ?  94  HIS   B HE1  1 
ATOM   5175 H  HE2  . HIS   B 1 94  ? 49.184 -13.884 0.470   1.00 13.42 ?  94  HIS   B HE2  1 
ATOM   5176 N  N    . VAL   B 1 95  ? 42.749 -17.865 1.541   1.00 10.70 ?  95  VAL   B N    1 
ATOM   5177 C  CA   . VAL   B 1 95  ? 41.422 -18.307 1.973   1.00 10.66 ?  95  VAL   B CA   1 
ATOM   5178 C  C    . VAL   B 1 95  ? 41.588 -19.344 3.071   1.00 10.91 ?  95  VAL   B C    1 
ATOM   5179 O  O    . VAL   B 1 95  ? 42.362 -20.296 2.916   1.00 11.51 ?  95  VAL   B O    1 
ATOM   5180 C  CB   . VAL   B 1 95  ? 40.609 -18.910 0.811   1.00 10.87 ?  95  VAL   B CB   1 
ATOM   5181 C  CG1  . VAL   B 1 95  ? 39.225 -19.364 1.290   1.00 12.30 ?  95  VAL   B CG1  1 
ATOM   5182 C  CG2  . VAL   B 1 95  ? 40.479 -17.919 -0.320  1.00 11.06 ?  95  VAL   B CG2  1 
ATOM   5183 H  H    . VAL   B 1 95  ? 43.215 -18.490 1.175   1.00 12.84 ?  95  VAL   B H    1 
ATOM   5184 H  HA   . VAL   B 1 95  ? 40.927 -17.556 2.331   1.00 12.79 ?  95  VAL   B HA   1 
ATOM   5185 H  HB   . VAL   B 1 95  ? 41.069 -19.689 0.469   1.00 13.04 ?  95  VAL   B HB   1 
ATOM   5186 H  HG11 . VAL   B 1 95  ? 38.670 -19.562 0.515   1.00 14.75 ?  95  VAL   B HG11 1 
ATOM   5187 H  HG12 . VAL   B 1 95  ? 39.320 -20.161 1.833   1.00 14.75 ?  95  VAL   B HG12 1 
ATOM   5188 H  HG13 . VAL   B 1 95  ? 38.818 -18.653 1.808   1.00 14.75 ?  95  VAL   B HG13 1 
ATOM   5189 H  HG21 . VAL   B 1 95  ? 39.903 -18.298 -1.002  1.00 13.26 ?  95  VAL   B HG21 1 
ATOM   5190 H  HG22 . VAL   B 1 95  ? 40.091 -17.102 0.027   1.00 13.26 ?  95  VAL   B HG22 1 
ATOM   5191 H  HG23 . VAL   B 1 95  ? 41.358 -17.748 -0.681  1.00 13.26 ?  95  VAL   B HG23 1 
ATOM   5192 N  N    . VAL   B 1 96  ? 40.865 -19.168 4.171   1.00 11.42 ?  96  VAL   B N    1 
ATOM   5193 C  CA   . VAL   B 1 96  ? 40.948 -20.077 5.314   1.00 11.68 ?  96  VAL   B CA   1 
ATOM   5194 C  C    . VAL   B 1 96  ? 39.761 -21.040 5.272   1.00 12.19 ?  96  VAL   B C    1 
ATOM   5195 O  O    . VAL   B 1 96  ? 38.642 -20.685 5.656   1.00 12.61 ?  96  VAL   B O    1 
ATOM   5196 C  CB   . VAL   B 1 96  ? 40.997 -19.325 6.646   1.00 12.19 ?  96  VAL   B CB   1 
ATOM   5197 C  CG1  . VAL   B 1 96  ? 41.165 -20.319 7.791   1.00 13.10 ?  96  VAL   B CG1  1 
ATOM   5198 C  CG2  . VAL   B 1 96  ? 42.115 -18.288 6.658   1.00 12.71 ?  96  VAL   B CG2  1 
ATOM   5199 H  H    . VAL   B 1 96  ? 40.316 -18.515 4.288   1.00 13.70 ?  96  VAL   B H    1 
ATOM   5200 H  HA   . VAL   B 1 96  ? 41.764 -20.600 5.244   1.00 14.01 ?  96  VAL   B HA   1 
ATOM   5201 H  HB   . VAL   B 1 96  ? 40.157 -18.859 6.781   1.00 14.63 ?  96  VAL   B HB   1 
ATOM   5202 H  HG11 . VAL   B 1 96  ? 41.366 -19.832 8.611   1.00 15.72 ?  96  VAL   B HG11 1 
ATOM   5203 H  HG12 . VAL   B 1 96  ? 40.341 -20.819 7.908   1.00 15.72 ?  96  VAL   B HG12 1 
ATOM   5204 H  HG13 . VAL   B 1 96  ? 41.894 -20.924 7.586   1.00 15.72 ?  96  VAL   B HG13 1 
ATOM   5205 H  HG21 . VAL   B 1 96  ? 42.158 -17.873 7.537   1.00 15.25 ?  96  VAL   B HG21 1 
ATOM   5206 H  HG22 . VAL   B 1 96  ? 42.956 -18.722 6.456   1.00 15.25 ?  96  VAL   B HG22 1 
ATOM   5207 H  HG23 . VAL   B 1 96  ? 41.923 -17.609 5.988   1.00 15.25 ?  96  VAL   B HG23 1 
ATOM   5208 N  N    . GLY   B 1 97  ? 39.999 -22.271 4.827   1.00 12.18 ?  97  GLY   B N    1 
ATOM   5209 C  CA   . GLY   B 1 97  ? 39.029 -23.329 4.995   1.00 12.84 ?  97  GLY   B CA   1 
ATOM   5210 C  C    . GLY   B 1 97  ? 39.170 -23.935 6.372   1.00 14.21 ?  97  GLY   B C    1 
ATOM   5211 O  O    . GLY   B 1 97  ? 40.214 -23.803 7.022   1.00 14.72 ?  97  GLY   B O    1 
ATOM   5212 H  H    . GLY   B 1 97  ? 40.724 -22.507 4.418   1.00 14.61 ?  97  GLY   B H    1 
ATOM   5213 H  HA2  . GLY   B 1 97  ? 38.135 -22.961 4.885   1.00 15.40 ?  97  GLY   B HA2  1 
ATOM   5214 H  HA3  . GLY   B 1 97  ? 39.170 -24.012 4.322   1.00 15.40 ?  97  GLY   B HA3  1 
ATOM   5215 N  N    . PRO   B 1 98  ? 38.125 -24.610 6.848   1.00 14.77 ?  98  PRO   B N    1 
ATOM   5216 C  CA   . PRO   B 1 98  ? 38.222 -25.296 8.142   1.00 15.97 ?  98  PRO   B CA   1 
ATOM   5217 C  C    . PRO   B 1 98  ? 39.241 -26.424 8.100   1.00 15.96 ?  98  PRO   B C    1 
ATOM   5218 O  O    . PRO   B 1 98  ? 39.340 -27.164 7.122   1.00 15.71 ?  98  PRO   B O    1 
ATOM   5219 C  CB   . PRO   B 1 98  ? 36.799 -25.828 8.367   1.00 16.67 ?  98  PRO   B CB   1 
ATOM   5220 C  CG   . PRO   B 1 98  ? 36.221 -25.963 7.006   1.00 16.28 ?  98  PRO   B CG   1 
ATOM   5221 C  CD   . PRO   B 1 98  ? 36.799 -24.801 6.226   1.00 15.16 ?  98  PRO   B CD   1 
ATOM   5222 H  HA   . PRO   B 1 98  ? 38.453 -24.668 8.840   1.00 19.16 ?  98  PRO   B HA   1 
ATOM   5223 H  HB2  . PRO   B 1 98  ? 36.838 -26.690 8.808   1.00 20.00 ?  98  PRO   B HB2  1 
ATOM   5224 H  HB3  . PRO   B 1 98  ? 36.290 -25.192 8.892   1.00 20.00 ?  98  PRO   B HB3  1 
ATOM   5225 H  HG2  . PRO   B 1 98  ? 36.491 -26.809 6.615   1.00 19.53 ?  98  PRO   B HG2  1 
ATOM   5226 H  HG3  . PRO   B 1 98  ? 35.253 -25.900 7.051   1.00 19.53 ?  98  PRO   B HG3  1 
ATOM   5227 H  HD2  . PRO   B 1 98  ? 36.888 -25.037 5.284   1.00 18.19 ?  98  PRO   B HD2  1 
ATOM   5228 H  HD3  . PRO   B 1 98  ? 36.251 -24.009 6.339   1.00 18.19 ?  98  PRO   B HD3  1 
ATOM   5229 N  N    . ASN   B 1 99  ? 40.001 -26.548 9.180   1.00 17.18 ?  99  ASN   B N    1 
ATOM   5230 C  CA   . ASN   B 1 99  ? 40.979 -27.622 9.342   1.00 17.78 ?  99  ASN   B CA   1 
ATOM   5231 C  C    . ASN   B 1 99  ? 40.356 -28.702 10.223  1.00 19.90 ?  99  ASN   B C    1 
ATOM   5232 O  O    . ASN   B 1 99  ? 40.290 -28.555 11.444  1.00 21.52 ?  99  ASN   B O    1 
ATOM   5233 C  CB   . ASN   B 1 99  ? 42.256 -27.067 9.959   1.00 18.38 ?  99  ASN   B CB   1 
ATOM   5234 C  CG   . ASN   B 1 99  ? 43.392 -28.068 9.951   1.00 18.96 ?  99  ASN   B CG   1 
ATOM   5235 O  OD1  . ASN   B 1 99  ? 43.181 -29.257 10.146  1.00 19.50 ?  99  ASN   B OD1  1 
ATOM   5236 N  ND2  . ASN   B 1 99  ? 44.598 -27.589 9.715   1.00 19.19 ?  99  ASN   B ND2  1 
ATOM   5237 H  H    . ASN   B 1 99  ? 39.964 -26.008 9.846   1.00 20.62 ?  99  ASN   B H    1 
ATOM   5238 H  HA   . ASN   B 1 99  ? 41.182 -28.012 8.480   1.00 21.33 ?  99  ASN   B HA   1 
ATOM   5239 H  HB2  . ASN   B 1 99  ? 42.525 -26.290 9.459   1.00 22.05 ?  99  ASN   B HB2  1 
ATOM   5240 H  HB3  . ASN   B 1 99  ? 42.069 -26.827 10.883  1.00 22.05 ?  99  ASN   B HB3  1 
ATOM   5241 H  HD21 . ASN   B 1 99  ? 45.271 -28.116 9.694   1.00 23.02 ?  99  ASN   B HD21 1 
ATOM   5242 H  HD22 . ASN   B 1 99  ? 44.699 -26.746 9.584   1.00 23.02 ?  99  ASN   B HD22 1 
ATOM   5243 N  N    . VAL   B 1 100 ? 39.876 -29.779 9.590   1.00 22.56 ?  100 VAL   B N    1 
ATOM   5244 C  CA   . VAL   B 1 100 ? 39.268 -30.882 10.334  1.00 25.65 ?  100 VAL   B CA   1 
ATOM   5245 C  C    . VAL   B 1 100 ? 40.283 -31.545 11.258  1.00 26.11 ?  100 VAL   B C    1 
ATOM   5246 O  O    . VAL   B 1 100 ? 39.924 -32.036 12.334  1.00 27.54 ?  100 VAL   B O    1 
ATOM   5247 C  CB   . VAL   B 1 100 ? 38.610 -31.890 9.365   1.00 28.36 ?  100 VAL   B CB   1 
ATOM   5248 C  CG1  . VAL   B 1 100 ? 38.133 -33.127 10.112  1.00 29.43 ?  100 VAL   B CG1  1 
ATOM   5249 C  CG2  . VAL   B 1 100 ? 37.445 -31.233 8.638   1.00 29.07 ?  100 VAL   B CG2  1 
ATOM   5250 H  H    . VAL   B 1 100 ? 39.877 -29.888 8.731   1.00 27.06 ?  100 VAL   B H    1 
ATOM   5251 H  HA   . VAL   B 1 100 ? 38.558 -30.528 10.889  1.00 30.78 ?  100 VAL   B HA   1 
ATOM   5252 H  HB   . VAL   B 1 100 ? 39.258 -32.173 8.701   1.00 34.02 ?  100 VAL   B HB   1 
ATOM   5253 H  HG11 . VAL   B 1 100 ? 37.527 -33.630 9.540   1.00 35.31 ?  100 VAL   B HG11 1 
ATOM   5254 H  HG12 . VAL   B 1 100 ? 38.897 -33.679 10.341  1.00 35.31 ?  100 VAL   B HG12 1 
ATOM   5255 H  HG13 . VAL   B 1 100 ? 37.667 -32.852 10.917  1.00 35.31 ?  100 VAL   B HG13 1 
ATOM   5256 H  HG21 . VAL   B 1 100 ? 37.038 -31.880 8.040   1.00 34.88 ?  100 VAL   B HG21 1 
ATOM   5257 H  HG22 . VAL   B 1 100 ? 36.794 -30.935 9.293   1.00 34.88 ?  100 VAL   B HG22 1 
ATOM   5258 H  HG23 . VAL   B 1 100 ? 37.776 -30.477 8.132   1.00 34.88 ?  100 VAL   B HG23 1 
ATOM   5259 N  N    . ASN   B 1 101 ? 41.559 -31.583 10.859  1.00 26.74 ?  101 ASN   B N    1 
ATOM   5260 C  CA   . ASN   B 1 101 ? 42.595 -32.124 11.738  1.00 28.56 ?  101 ASN   B CA   1 
ATOM   5261 C  C    . ASN   B 1 101 ? 42.768 -31.290 13.001  1.00 31.69 ?  101 ASN   B C    1 
ATOM   5262 O  O    . ASN   B 1 101 ? 43.362 -31.774 13.973  1.00 32.68 ?  101 ASN   B O    1 
ATOM   5263 C  CB   . ASN   B 1 101 ? 43.922 -32.256 10.986  1.00 27.99 ?  101 ASN   B CB   1 
ATOM   5264 C  CG   . ASN   B 1 101 ? 43.908 -33.398 9.984   1.00 27.03 ?  101 ASN   B CG   1 
ATOM   5265 O  OD1  . ASN   B 1 101 ? 43.226 -34.401 10.184  1.00 27.77 ?  101 ASN   B OD1  1 
ATOM   5266 N  ND2  . ASN   B 1 101 ? 44.654 -33.246 8.896   1.00 26.52 ?  101 ASN   B ND2  1 
ATOM   5267 H  H    . ASN   B 1 101 ? 41.839 -31.322 10.089  1.00 32.08 ?  101 ASN   B H    1 
ATOM   5268 H  HA   . ASN   B 1 101 ? 42.330 -33.011 12.015  1.00 34.27 ?  101 ASN   B HA   1 
ATOM   5269 H  HB2  . ASN   B 1 101 ? 44.104 -31.436 10.502  1.00 33.58 ?  101 ASN   B HB2  1 
ATOM   5270 H  HB3  . ASN   B 1 101 ? 44.633 -32.428 11.624  1.00 33.58 ?  101 ASN   B HB3  1 
ATOM   5271 H  HD21 . ASN   B 1 101 ? 44.676 -33.865 8.300   1.00 31.82 ?  101 ASN   B HD21 1 
ATOM   5272 H  HD22 . ASN   B 1 101 ? 45.117 -32.529 8.787   1.00 31.82 ?  101 ASN   B HD22 1 
ATOM   5273 N  N    A LYS   B 1 102 ? 42.270 -30.053 13.006  0.68 33.50 ?  102 LYS   B N    1 
ATOM   5274 N  N    B LYS   B 1 102 ? 42.269 -30.054 13.010  0.32 33.51 ?  102 LYS   B N    1 
ATOM   5275 C  CA   A LYS   B 1 102 ? 42.244 -29.207 14.191  0.68 35.52 ?  102 LYS   B CA   1 
ATOM   5276 C  CA   B LYS   B 1 102 ? 42.249 -29.219 14.203  0.32 35.29 ?  102 LYS   B CA   1 
ATOM   5277 C  C    A LYS   B 1 102 ? 40.871 -29.175 14.852  0.68 35.00 ?  102 LYS   B C    1 
ATOM   5278 C  C    B LYS   B 1 102 ? 40.874 -29.180 14.859  0.32 35.04 ?  102 LYS   B C    1 
ATOM   5279 O  O    A LYS   B 1 102 ? 40.656 -28.380 15.772  0.68 35.76 ?  102 LYS   B O    1 
ATOM   5280 O  O    B LYS   B 1 102 ? 40.664 -28.395 15.788  0.32 35.58 ?  102 LYS   B O    1 
ATOM   5281 C  CB   A LYS   B 1 102 ? 42.656 -27.777 13.837  0.68 38.24 ?  102 LYS   B CB   1 
ATOM   5282 C  CB   B LYS   B 1 102 ? 42.702 -27.797 13.868  0.32 37.32 ?  102 LYS   B CB   1 
ATOM   5283 C  CG   A LYS   B 1 102 ? 44.119 -27.586 13.480  0.68 40.69 ?  102 LYS   B CG   1 
ATOM   5284 C  CG   B LYS   B 1 102 ? 44.174 -27.664 13.518  0.32 39.04 ?  102 LYS   B CG   1 
ATOM   5285 C  CD   A LYS   B 1 102 ? 44.361 -26.137 13.083  0.68 43.07 ?  102 LYS   B CD   1 
ATOM   5286 C  CD   B LYS   B 1 102 ? 44.487 -26.243 13.075  0.32 40.67 ?  102 LYS   B CD   1 
ATOM   5287 C  CE   A LYS   B 1 102 ? 45.826 -25.843 12.819  0.68 44.80 ?  102 LYS   B CE   1 
ATOM   5288 C  CE   B LYS   B 1 102 ? 45.981 -26.003 12.945  0.32 41.83 ?  102 LYS   B CE   1 
ATOM   5289 N  NZ   A LYS   B 1 102 ? 46.026 -24.416 12.426  0.68 45.84 ?  102 LYS   B NZ   1 
ATOM   5290 N  NZ   B LYS   B 1 102 ? 46.268 -24.598 12.537  0.32 42.55 ?  102 LYS   B NZ   1 
ATOM   5291 H  H    A LYS   B 1 102 ? 41.928 -29.673 12.312  0.68 40.20 ?  102 LYS   B H    1 
ATOM   5292 H  H    B LYS   B 1 102 ? 41.927 -29.670 12.319  0.32 40.21 ?  102 LYS   B H    1 
ATOM   5293 H  HA   A LYS   B 1 102 ? 42.881 -29.548 14.836  0.68 42.62 ?  102 LYS   B HA   1 
ATOM   5294 H  HA   B LYS   B 1 102 ? 42.875 -29.581 14.847  0.32 42.35 ?  102 LYS   B HA   1 
ATOM   5295 H  HB2  A LYS   B 1 102 ? 42.131 -27.485 13.077  0.68 45.88 ?  102 LYS   B HB2  1 
ATOM   5296 H  HB2  B LYS   B 1 102 ? 42.191 -27.477 13.110  0.32 44.77 ?  102 LYS   B HB2  1 
ATOM   5297 H  HB3  A LYS   B 1 102 ? 42.469 -27.206 14.599  0.68 45.88 ?  102 LYS   B HB3  1 
ATOM   5298 H  HB3  B LYS   B 1 102 ? 42.533 -27.229 14.637  0.32 44.77 ?  102 LYS   B HB3  1 
ATOM   5299 H  HG2  A LYS   B 1 102 ? 44.674 -27.793 14.249  0.68 48.82 ?  102 LYS   B HG2  1 
ATOM   5300 H  HG2  B LYS   B 1 102 ? 44.714 -27.868 14.298  0.32 46.85 ?  102 LYS   B HG2  1 
ATOM   5301 H  HG3  A LYS   B 1 102 ? 44.350 -28.156 12.729  0.68 48.82 ?  102 LYS   B HG3  1 
ATOM   5302 H  HG3  B LYS   B 1 102 ? 44.390 -28.268 12.790  0.32 46.85 ?  102 LYS   B HG3  1 
ATOM   5303 H  HD2  A LYS   B 1 102 ? 43.864 -25.944 12.272  0.68 51.68 ?  102 LYS   B HD2  1 
ATOM   5304 H  HD2  B LYS   B 1 102 ? 44.079 -26.082 12.210  0.32 48.80 ?  102 LYS   B HD2  1 
ATOM   5305 H  HD3  A LYS   B 1 102 ? 44.062 -25.558 13.802  0.68 51.68 ?  102 LYS   B HD3  1 
ATOM   5306 H  HD3  B LYS   B 1 102 ? 44.136 -25.621 13.731  0.32 48.80 ?  102 LYS   B HD3  1 
ATOM   5307 H  HE2  A LYS   B 1 102 ? 46.338 -26.012 13.625  0.68 53.76 ?  102 LYS   B HE2  1 
ATOM   5308 H  HE2  B LYS   B 1 102 ? 46.407 -26.164 13.802  0.32 50.19 ?  102 LYS   B HE2  1 
ATOM   5309 H  HE3  A LYS   B 1 102 ? 46.142 -26.406 12.095  0.68 53.76 ?  102 LYS   B HE3  1 
ATOM   5310 H  HE3  B LYS   B 1 102 ? 46.345 -26.597 12.271  0.32 50.19 ?  102 LYS   B HE3  1 
ATOM   5311 H  HZ1  A LYS   B 1 102 ? 46.888 -24.260 12.275  0.68 55.01 ?  102 LYS   B HZ1  1 
ATOM   5312 H  HZ1  B LYS   B 1 102 ? 47.146 -24.475 12.466  0.32 51.05 ?  102 LYS   B HZ1  1 
ATOM   5313 H  HZ2  A LYS   B 1 102 ? 45.565 -24.238 11.685  0.68 55.01 ?  102 LYS   B HZ2  1 
ATOM   5314 H  HZ2  B LYS   B 1 102 ? 45.887 -24.427 11.751  0.32 51.05 ?  102 LYS   B HZ2  1 
ATOM   5315 H  HZ3  A LYS   B 1 102 ? 45.744 -23.879 13.078  0.68 55.01 ?  102 LYS   B HZ3  1 
ATOM   5316 H  HZ3  B LYS   B 1 102 ? 45.944 -24.033 13.144  0.32 51.05 ?  102 LYS   B HZ3  1 
ATOM   5317 N  N    . GLY   B 1 103 ? 39.934 -29.999 14.392  1.00 34.46 ?  103 GLY   B N    1 
ATOM   5318 C  CA   . GLY   B 1 103 ? 38.610 -30.050 14.976  1.00 34.11 ?  103 GLY   B CA   1 
ATOM   5319 C  C    . GLY   B 1 103 ? 37.656 -28.968 14.525  1.00 33.01 ?  103 GLY   B C    1 
ATOM   5320 O  O    . GLY   B 1 103 ? 36.571 -28.845 15.105  1.00 33.75 ?  103 GLY   B O    1 
ATOM   5321 H  H    A GLY   B 1 103 ? 40.045 -30.539 13.733  0.68 41.35 ?  103 GLY   B H    1 
ATOM   5322 H  H    B GLY   B 1 103 ? 40.044 -30.536 13.730  0.32 41.35 ?  103 GLY   B H    1 
ATOM   5323 H  HA2  . GLY   B 1 103 ? 38.208 -30.906 14.765  1.00 40.93 ?  103 GLY   B HA2  1 
ATOM   5324 H  HA3  . GLY   B 1 103 ? 38.690 -29.988 15.941  1.00 40.93 ?  103 GLY   B HA3  1 
ATOM   5325 N  N    A GLU   B 1 104 ? 38.023 -28.179 13.519  0.68 31.44 ?  104 GLU   B N    1 
ATOM   5326 N  N    B GLU   B 1 104 ? 38.010 -28.186 13.510  0.32 32.62 ?  104 GLU   B N    1 
ATOM   5327 C  CA   A GLU   B 1 104 ? 37.173 -27.093 13.059  0.68 29.70 ?  104 GLU   B CA   1 
ATOM   5328 C  CA   B GLU   B 1 104 ? 37.151 -27.098 13.068  0.32 31.96 ?  104 GLU   B CA   1 
ATOM   5329 C  C    A GLU   B 1 104 ? 36.000 -27.634 12.244  0.68 30.43 ?  104 GLU   B C    1 
ATOM   5330 C  C    B GLU   B 1 104 ? 35.981 -27.629 12.245  0.32 32.28 ?  104 GLU   B C    1 
ATOM   5331 O  O    A GLU   B 1 104 ? 36.052 -28.727 11.673  0.68 31.49 ?  104 GLU   B O    1 
ATOM   5332 O  O    B GLU   B 1 104 ? 36.057 -28.695 11.627  0.32 32.72 ?  104 GLU   B O    1 
ATOM   5333 C  CB   A GLU   B 1 104 ? 37.993 -26.087 12.249  0.68 28.54 ?  104 GLU   B CB   1 
ATOM   5334 C  CB   B GLU   B 1 104 ? 37.961 -26.079 12.267  0.32 31.23 ?  104 GLU   B CB   1 
ATOM   5335 C  CG   A GLU   B 1 104 ? 39.107 -25.454 13.073  0.68 27.54 ?  104 GLU   B CG   1 
ATOM   5336 C  CG   B GLU   B 1 104 ? 39.087 -25.464 13.085  0.32 30.59 ?  104 GLU   B CG   1 
ATOM   5337 C  CD   A GLU   B 1 104 ? 40.024 -24.549 12.278  0.68 26.41 ?  104 GLU   B CD   1 
ATOM   5338 C  CD   B GLU   B 1 104 ? 39.992 -24.561 12.274  0.32 30.00 ?  104 GLU   B CD   1 
ATOM   5339 O  OE1  A GLU   B 1 104 ? 40.038 -24.623 11.031  0.68 24.61 ?  104 GLU   B OE1  1 
ATOM   5340 O  OE1  B GLU   B 1 104 ? 39.913 -24.589 11.028  0.32 29.41 ?  104 GLU   B OE1  1 
ATOM   5341 O  OE2  A GLU   B 1 104 ? 40.743 -23.754 12.917  0.68 26.90 -1 104 GLU   B OE2  1 
ATOM   5342 O  OE2  B GLU   B 1 104 ? 40.787 -23.821 12.890  0.32 30.00 -1 104 GLU   B OE2  1 
ATOM   5343 H  H    A GLU   B 1 104 ? 38.767 -28.248 13.092  0.68 37.72 ?  104 GLU   B H    1 
ATOM   5344 H  H    B GLU   B 1 104 ? 38.744 -28.260 13.068  0.32 39.13 ?  104 GLU   B H    1 
ATOM   5345 H  HA   A GLU   B 1 104 ? 36.814 -26.628 13.832  0.68 35.63 ?  104 GLU   B HA   1 
ATOM   5346 H  HA   B GLU   B 1 104 ? 36.790 -26.648 13.845  0.32 38.34 ?  104 GLU   B HA   1 
ATOM   5347 H  HB2  A GLU   B 1 104 ? 38.396 -26.541 11.494  0.68 34.24 ?  104 GLU   B HB2  1 
ATOM   5348 H  HB2  B GLU   B 1 104 ? 38.352 -26.517 11.496  0.32 37.47 ?  104 GLU   B HB2  1 
ATOM   5349 H  HB3  A GLU   B 1 104 ? 37.408 -25.377 11.939  0.68 34.24 ?  104 GLU   B HB3  1 
ATOM   5350 H  HB3  B GLU   B 1 104 ? 37.372 -25.362 11.980  0.32 37.47 ?  104 GLU   B HB3  1 
ATOM   5351 H  HG2  A GLU   B 1 104 ? 38.712 -24.917 13.777  0.68 33.05 ?  104 GLU   B HG2  1 
ATOM   5352 H  HG2  B GLU   B 1 104 ? 38.702 -24.934 13.801  0.32 36.71 ?  104 GLU   B HG2  1 
ATOM   5353 H  HG3  A GLU   B 1 104 ? 39.651 -26.156 13.461  0.68 33.05 ?  104 GLU   B HG3  1 
ATOM   5354 H  HG3  B GLU   B 1 104 ? 39.629 -26.177 13.459  0.32 36.71 ?  104 GLU   B HG3  1 
ATOM   5355 N  N    A ASP   B 1 105 ? 34.930 -26.843 12.198  0.68 30.36 ?  105 ASP   B N    1 
ATOM   5356 N  N    B ASP   B 1 105 ? 34.890 -26.866 12.245  0.32 32.09 ?  105 ASP   B N    1 
ATOM   5357 C  CA   A ASP   B 1 105 ? 33.655 -27.296 11.653  0.68 31.02 ?  105 ASP   B CA   1 
ATOM   5358 C  CA   B ASP   B 1 105 ? 33.633 -27.332 11.670  0.32 32.13 ?  105 ASP   B CA   1 
ATOM   5359 C  C    A ASP   B 1 105 ? 33.721 -27.340 10.133  0.68 29.20 ?  105 ASP   B C    1 
ATOM   5360 C  C    B ASP   B 1 105 ? 33.724 -27.349 10.149  0.32 30.43 ?  105 ASP   B C    1 
ATOM   5361 O  O    A ASP   B 1 105 ? 33.888 -26.302 9.483   0.68 28.22 ?  105 ASP   B O    1 
ATOM   5362 O  O    B ASP   B 1 105 ? 33.931 -26.309 9.516   0.32 30.11 ?  105 ASP   B O    1 
ATOM   5363 C  CB   A ASP   B 1 105 ? 32.539 -26.357 12.105  0.68 33.89 ?  105 ASP   B CB   1 
ATOM   5364 C  CB   B ASP   B 1 105 ? 32.486 -26.432 12.126  0.32 33.67 ?  105 ASP   B CB   1 
ATOM   5365 C  CG   A ASP   B 1 105 ? 31.163 -26.849 11.700  0.68 36.34 ?  105 ASP   B CG   1 
ATOM   5366 C  CG   B ASP   B 1 105 ? 31.124 -27.000 11.771  0.32 35.06 ?  105 ASP   B CG   1 
ATOM   5367 O  OD1  A ASP   B 1 105 ? 31.068 -27.945 11.108  0.68 36.31 ?  105 ASP   B OD1  1 
ATOM   5368 O  OD1  B ASP   B 1 105 ? 31.072 -28.032 11.067  0.32 35.46 ?  105 ASP   B OD1  1 
ATOM   5369 O  OD2  A ASP   B 1 105 ? 30.171 -26.140 11.979  0.68 38.09 -1 105 ASP   B OD2  1 
ATOM   5370 O  OD2  B ASP   B 1 105 ? 30.104 -26.423 12.203  0.32 35.55 -1 105 ASP   B OD2  1 
ATOM   5371 H  H    A ASP   B 1 105 ? 34.918 -26.030 12.478  0.68 36.43 ?  105 ASP   B H    1 
ATOM   5372 H  H    B ASP   B 1 105 ? 34.853 -26.071 12.569  0.32 38.51 ?  105 ASP   B H    1 
ATOM   5373 H  HA   A ASP   B 1 105 ? 33.460 -28.188 11.978  0.68 37.22 ?  105 ASP   B HA   1 
ATOM   5374 H  HA   B ASP   B 1 105 ? 33.449 -28.234 11.974  0.32 38.55 ?  105 ASP   B HA   1 
ATOM   5375 H  HB2  A ASP   B 1 105 ? 32.565 -26.280 13.072  0.68 40.66 ?  105 ASP   B HB2  1 
ATOM   5376 H  HB2  B ASP   B 1 105 ? 32.522 -26.334 13.091  0.32 40.39 ?  105 ASP   B HB2  1 
ATOM   5377 H  HB3  A ASP   B 1 105 ? 32.678 -25.485 11.700  0.68 40.66 ?  105 ASP   B HB3  1 
ATOM   5378 H  HB3  B ASP   B 1 105 ? 32.575 -25.562 11.703  0.32 40.39 ?  105 ASP   B HB3  1 
ATOM   5379 N  N    . ILE   B 1 106 ? 33.556 -28.539 9.566   1.00 29.06 ?  106 ILE   B N    1 
ATOM   5380 C  CA   . ILE   B 1 106 ? 33.565 -28.700 8.118   1.00 27.30 ?  106 ILE   B CA   1 
ATOM   5381 C  C    . ILE   B 1 106 ? 32.466 -27.879 7.450   1.00 25.64 ?  106 ILE   B C    1 
ATOM   5382 O  O    . ILE   B 1 106 ? 32.564 -27.572 6.260   1.00 24.83 ?  106 ILE   B O    1 
ATOM   5383 C  CB   . ILE   B 1 106 ? 33.478 -30.208 7.774   1.00 27.83 ?  106 ILE   B CB   1 
ATOM   5384 C  CG1  . ILE   B 1 106 ? 33.729 -30.454 6.286   1.00 28.01 ?  106 ILE   B CG1  1 
ATOM   5385 C  CG2  . ILE   B 1 106 ? 32.128 -30.781 8.188   1.00 28.91 ?  106 ILE   B CG2  1 
ATOM   5386 C  CD1  . ILE   B 1 106 ? 35.078 -29.969 5.821   1.00 27.72 ?  106 ILE   B CD1  1 
ATOM   5387 H  H    A ILE   B 1 106 ? 33.432 -29.269 10.000  0.68 34.87 ?  106 ILE   B H    1 
ATOM   5388 H  H    B ILE   B 1 106 ? 33.437 -29.273 9.995   0.32 34.87 ?  106 ILE   B H    1 
ATOM   5389 H  HA   . ILE   B 1 106 ? 34.407 -28.367 7.782   1.00 32.75 ?  106 ILE   B HA   1 
ATOM   5390 H  HB   . ILE   B 1 106 ? 34.167 -30.669 8.276   1.00 33.39 ?  106 ILE   B HB   1 
ATOM   5391 H  HG12 . ILE   B 1 106 ? 33.687 -31.411 6.114   1.00 33.61 ?  106 ILE   B HG12 1 
ATOM   5392 H  HG13 . ILE   B 1 106 ? 33.053 -29.997 5.767   1.00 33.61 ?  106 ILE   B HG13 1 
ATOM   5393 H  HG21 . ILE   B 1 106 ? 32.147 -31.744 8.070   1.00 34.69 ?  106 ILE   B HG21 1 
ATOM   5394 H  HG22 . ILE   B 1 106 ? 31.967 -30.566 9.120   1.00 34.69 ?  106 ILE   B HG22 1 
ATOM   5395 H  HG23 . ILE   B 1 106 ? 31.434 -30.393 7.633   1.00 34.69 ?  106 ILE   B HG23 1 
ATOM   5396 H  HD11 . ILE   B 1 106 ? 35.280 -30.372 4.963   1.00 33.26 ?  106 ILE   B HD11 1 
ATOM   5397 H  HD12 . ILE   B 1 106 ? 35.055 -29.003 5.735   1.00 33.26 ?  106 ILE   B HD12 1 
ATOM   5398 H  HD13 . ILE   B 1 106 ? 35.750 -30.228 6.473   1.00 33.26 ?  106 ILE   B HD13 1 
ATOM   5399 N  N    A GLN   B 1 107 ? 31.412 -27.524 8.189   0.68 26.28 ?  107 GLN   B N    1 
ATOM   5400 N  N    B GLN   B 1 107 ? 31.426 -27.501 8.195   0.32 26.05 ?  107 GLN   B N    1 
ATOM   5401 C  CA   A GLN   B 1 107 ? 30.334 -26.719 7.623   0.68 26.28 ?  107 GLN   B CA   1 
ATOM   5402 C  CA   B GLN   B 1 107 ? 30.337 -26.713 7.626   0.32 26.13 ?  107 GLN   B CA   1 
ATOM   5403 C  C    A GLN   B 1 107 ? 30.818 -25.364 7.122   0.68 24.13 ?  107 GLN   B C    1 
ATOM   5404 C  C    B GLN   B 1 107 ? 30.806 -25.348 7.141   0.32 24.06 ?  107 GLN   B C    1 
ATOM   5405 O  O    A GLN   B 1 107 ? 30.173 -24.782 6.246   0.68 24.98 ?  107 GLN   B O    1 
ATOM   5406 O  O    B GLN   B 1 107 ? 30.133 -24.740 6.303   0.32 24.64 ?  107 GLN   B O    1 
ATOM   5407 C  CB   A GLN   B 1 107 ? 29.221 -26.531 8.658   0.68 30.15 ?  107 GLN   B CB   1 
ATOM   5408 C  CB   B GLN   B 1 107 ? 29.223 -26.548 8.664   0.32 28.92 ?  107 GLN   B CB   1 
ATOM   5409 C  CG   A GLN   B 1 107 ? 27.892 -26.046 8.082   0.68 33.98 ?  107 GLN   B CG   1 
ATOM   5410 C  CG   B GLN   B 1 107 ? 27.883 -26.085 8.102   0.32 31.54 ?  107 GLN   B CG   1 
ATOM   5411 C  CD   A GLN   B 1 107 ? 27.810 -24.532 7.960   0.68 36.90 ?  107 GLN   B CD   1 
ATOM   5412 C  CD   B GLN   B 1 107 ? 27.752 -24.572 8.047   0.32 33.58 ?  107 GLN   B CD   1 
ATOM   5413 O  OE1  A GLN   B 1 107 ? 28.630 -23.806 8.523   0.68 37.84 ?  107 GLN   B OE1  1 
ATOM   5414 O  OE1  B GLN   B 1 107 ? 28.563 -23.845 8.621   0.32 34.27 ?  107 GLN   B OE1  1 
ATOM   5415 N  NE2  A GLN   B 1 107 ? 26.811 -24.050 7.222   0.68 37.82 ?  107 GLN   B NE2  1 
ATOM   5416 N  NE2  B GLN   B 1 107 ? 26.722 -24.092 7.356   0.32 34.30 ?  107 GLN   B NE2  1 
ATOM   5417 H  H    A GLN   B 1 107 ? 31.295 -27.739 9.008   0.68 31.53 ?  107 GLN   B H    1 
ATOM   5418 H  H    B GLN   B 1 107 ? 31.331 -27.678 9.025   0.32 31.25 ?  107 GLN   B H    1 
ATOM   5419 H  HA   A GLN   B 1 107 ? 29.953 -27.192 6.865   0.68 31.53 ?  107 GLN   B HA   1 
ATOM   5420 H  HA   B GLN   B 1 107 ? 29.965 -27.188 6.865   0.32 31.35 ?  107 GLN   B HA   1 
ATOM   5421 H  HB2  A GLN   B 1 107 ? 29.059 -27.380 9.090   0.68 36.17 ?  107 GLN   B HB2  1 
ATOM   5422 H  HB2  B GLN   B 1 107 ? 29.078 -27.402 9.092   0.32 34.70 ?  107 GLN   B HB2  1 
ATOM   5423 H  HB3  A GLN   B 1 107 ? 29.515 -25.879 9.313   0.68 36.17 ?  107 GLN   B HB3  1 
ATOM   5424 H  HB3  B GLN   B 1 107 ? 29.509 -25.896 9.322   0.32 34.70 ?  107 GLN   B HB3  1 
ATOM   5425 H  HG2  A GLN   B 1 107 ? 27.772 -26.421 7.196   0.68 40.77 ?  107 GLN   B HG2  1 
ATOM   5426 H  HG2  B GLN   B 1 107 ? 27.780 -26.425 7.200   0.32 37.84 ?  107 GLN   B HG2  1 
ATOM   5427 H  HG3  A GLN   B 1 107 ? 27.171 -26.340 8.664   0.68 40.77 ?  107 GLN   B HG3  1 
ATOM   5428 H  HG3  B GLN   B 1 107 ? 27.170 -26.429 8.667   0.32 37.84 ?  107 GLN   B HG3  1 
ATOM   5429 H  HE21 A GLN   B 1 107 ? 26.256 -24.588 6.842   0.68 45.38 ?  107 GLN   B HE21 1 
ATOM   5430 H  HE21 B GLN   B 1 107 ? 26.174 -24.630 6.967   0.32 41.15 ?  107 GLN   B HE21 1 
ATOM   5431 H  HE22 A GLN   B 1 107 ? 26.717 -23.199 7.125   0.68 45.38 ?  107 GLN   B HE22 1 
ATOM   5432 H  HE22 B GLN   B 1 107 ? 26.602 -23.242 7.298   0.32 41.15 ?  107 GLN   B HE22 1 
ATOM   5433 N  N    . LEU   B 1 108 ? 31.940 -24.855 7.643   1.00 21.80 ?  108 LEU   B N    1 
ATOM   5434 C  CA   . LEU   B 1 108 ? 32.482 -23.560 7.227   1.00 19.28 ?  108 LEU   B CA   1 
ATOM   5435 C  C    . LEU   B 1 108 ? 33.127 -23.590 5.850   1.00 16.62 ?  108 LEU   B C    1 
ATOM   5436 O  O    . LEU   B 1 108 ? 33.555 -22.537 5.361   1.00 15.82 ?  108 LEU   B O    1 
ATOM   5437 C  CB   . LEU   B 1 108 ? 33.486 -23.051 8.262   1.00 20.05 ?  108 LEU   B CB   1 
ATOM   5438 C  CG   . LEU   B 1 108 ? 32.858 -22.536 9.557   1.00 21.27 ?  108 LEU   B CG   1 
ATOM   5439 C  CD1  . LEU   B 1 108 ? 33.857 -22.560 10.697  1.00 22.03 ?  108 LEU   B CD1  1 
ATOM   5440 C  CD2  . LEU   B 1 108 ? 32.336 -21.124 9.343   1.00 22.24 ?  108 LEU   B CD2  1 
ATOM   5441 H  H    A LEU   B 1 108 ? 32.400 -25.242 8.254   0.68 26.16 ?  108 LEU   B H    1 
ATOM   5442 H  H    B LEU   B 1 108 ? 32.410 -25.253 8.239   0.32 26.16 ?  108 LEU   B H    1 
ATOM   5443 H  HA   . LEU   B 1 108 ? 31.754 -22.923 7.191   1.00 23.13 ?  108 LEU   B HA   1 
ATOM   5444 H  HB2  . LEU   B 1 108 ? 34.081 -23.778 8.498   1.00 24.06 ?  108 LEU   B HB2  1 
ATOM   5445 H  HB3  . LEU   B 1 108 ? 33.990 -22.324 7.873   1.00 24.06 ?  108 LEU   B HB3  1 
ATOM   5446 H  HG   . LEU   B 1 108 ? 32.106 -23.102 9.799   1.00 25.52 ?  108 LEU   B HG   1 
ATOM   5447 H  HD11 . LEU   B 1 108 ? 33.423 -22.239 11.504  1.00 26.43 ?  108 LEU   B HD11 1 
ATOM   5448 H  HD12 . LEU   B 1 108 ? 34.164 -23.470 10.828  1.00 26.43 ?  108 LEU   B HD12 1 
ATOM   5449 H  HD13 . LEU   B 1 108 ? 34.604 -21.986 10.473  1.00 26.43 ?  108 LEU   B HD13 1 
ATOM   5450 H  HD21 . LEU   B 1 108 ? 31.945 -20.804 10.170  1.00 26.68 ?  108 LEU   B HD21 1 
ATOM   5451 H  HD22 . LEU   B 1 108 ? 33.076 -20.553 9.084   1.00 26.68 ?  108 LEU   B HD22 1 
ATOM   5452 H  HD23 . LEU   B 1 108 ? 31.666 -21.138 8.642   1.00 26.68 ?  108 LEU   B HD23 1 
ATOM   5453 N  N    . LEU   B 1 109 ? 33.192 -24.757 5.216   1.00 15.30 ?  109 LEU   B N    1 
ATOM   5454 C  CA   . LEU   B 1 109 ? 33.817 -24.865 3.904   1.00 14.59 ?  109 LEU   B CA   1 
ATOM   5455 C  C    . LEU   B 1 109 ? 33.039 -24.089 2.843   1.00 14.03 ?  109 LEU   B C    1 
ATOM   5456 O  O    . LEU   B 1 109 ? 33.645 -23.501 1.938   1.00 13.91 ?  109 LEU   B O    1 
ATOM   5457 C  CB   . LEU   B 1 109 ? 33.952 -26.343 3.533   1.00 15.01 ?  109 LEU   B CB   1 
ATOM   5458 C  CG   . LEU   B 1 109 ? 34.709 -26.687 2.252   1.00 14.73 ?  109 LEU   B CG   1 
ATOM   5459 C  CD1  . LEU   B 1 109 ? 36.080 -26.032 2.241   1.00 14.33 ?  109 LEU   B CD1  1 
ATOM   5460 C  CD2  . LEU   B 1 109 ? 34.829 -28.201 2.101   1.00 15.03 ?  109 LEU   B CD2  1 
ATOM   5461 H  H    . LEU   B 1 109 ? 32.889 -25.499 5.521   1.00 18.36 ?  109 LEU   B H    1 
ATOM   5462 H  HA   . LEU   B 1 109 ? 34.710 -24.489 3.949   1.00 17.51 ?  109 LEU   B HA   1 
ATOM   5463 H  HB2  . LEU   B 1 109 ? 34.411 -26.794 4.257   1.00 18.00 ?  109 LEU   B HB2  1 
ATOM   5464 H  HB3  . LEU   B 1 109 ? 33.061 -26.713 3.440   1.00 18.00 ?  109 LEU   B HB3  1 
ATOM   5465 H  HG   . LEU   B 1 109 ? 34.210 -26.358 1.487   1.00 17.68 ?  109 LEU   B HG   1 
ATOM   5466 H  HD11 . LEU   B 1 109 ? 36.595 -26.389 1.500   1.00 17.19 ?  109 LEU   B HD11 1 
ATOM   5467 H  HD12 . LEU   B 1 109 ? 35.970 -25.077 2.139   1.00 17.19 ?  109 LEU   B HD12 1 
ATOM   5468 H  HD13 . LEU   B 1 109 ? 36.529 -26.231 3.078   1.00 17.19 ?  109 LEU   B HD13 1 
ATOM   5469 H  HD21 . LEU   B 1 109 ? 35.395 -28.400 1.336   1.00 18.03 ?  109 LEU   B HD21 1 
ATOM   5470 H  HD22 . LEU   B 1 109 ? 35.221 -28.571 2.906   1.00 18.03 ?  109 LEU   B HD22 1 
ATOM   5471 H  HD23 . LEU   B 1 109 ? 33.944 -28.579 1.960   1.00 18.03 ?  109 LEU   B HD23 1 
ATOM   5472 N  N    . LYS   B 1 110 ? 31.706 -24.058 2.932   1.00 13.71 ?  110 LYS   B N    1 
ATOM   5473 C  CA   . LYS   B 1 110 ? 30.946 -23.296 1.944   1.00 13.42 ?  110 LYS   B CA   1 
ATOM   5474 C  C    . LYS   B 1 110 ? 31.282 -21.808 2.027   1.00 13.19 ?  110 LYS   B C    1 
ATOM   5475 O  O    . LYS   B 1 110 ? 31.532 -21.160 1.004   1.00 13.27 ?  110 LYS   B O    1 
ATOM   5476 C  CB   . LYS   B 1 110 ? 29.443 -23.542 2.102   1.00 14.02 ?  110 LYS   B CB   1 
ATOM   5477 C  CG   . LYS   B 1 110 ? 28.634 -22.926 0.961   1.00 14.80 ?  110 LYS   B CG   1 
ATOM   5478 C  CD   . LYS   B 1 110 ? 27.170 -23.357 0.985   1.00 14.68 ?  110 LYS   B CD   1 
ATOM   5479 C  CE   . LYS   B 1 110 ? 26.398 -22.814 -0.220  1.00 15.67 ?  110 LYS   B CE   1 
ATOM   5480 N  NZ   . LYS   B 1 110 ? 26.727 -23.531 -1.486  1.00 15.97 ?  110 LYS   B NZ   1 
ATOM   5481 H  H    . LYS   B 1 110 ? 31.241 -24.463 3.529   1.00 16.45 ?  110 LYS   B H    1 
ATOM   5482 H  HA   . LYS   B 1 110 ? 31.204 -23.604 1.059   1.00 16.10 ?  110 LYS   B HA   1 
ATOM   5483 H  HB2  . LYS   B 1 110 ? 29.279 -24.501 2.109   1.00 16.82 ?  110 LYS   B HB2  1 
ATOM   5484 H  HB3  . LYS   B 1 110 ? 29.144 -23.149 2.935   1.00 16.82 ?  110 LYS   B HB3  1 
ATOM   5485 H  HG2  . LYS   B 1 110 ? 28.662 -21.962 1.036   1.00 17.76 ?  110 LYS   B HG2  1 
ATOM   5486 H  HG3  . LYS   B 1 110 ? 29.012 -23.209 0.114   1.00 17.76 ?  110 LYS   B HG3  1 
ATOM   5487 H  HD2  . LYS   B 1 110 ? 27.118 -24.329 0.967   1.00 17.61 ?  110 LYS   B HD2  1 
ATOM   5488 H  HD3  . LYS   B 1 110 ? 26.748 -23.020 1.794   1.00 17.61 ?  110 LYS   B HD3  1 
ATOM   5489 H  HE2  . LYS   B 1 110 ? 25.447 -22.909 -0.061  1.00 18.80 ?  110 LYS   B HE2  1 
ATOM   5490 H  HE3  . LYS   B 1 110 ? 26.623 -21.877 -0.340  1.00 18.80 ?  110 LYS   B HE3  1 
ATOM   5491 H  HZ1  . LYS   B 1 110 ? 26.265 -23.185 -2.161  1.00 19.16 ?  110 LYS   B HZ1  1 
ATOM   5492 H  HZ2  . LYS   B 1 110 ? 27.598 -23.453 -1.661  1.00 19.16 ?  110 LYS   B HZ2  1 
ATOM   5493 H  HZ3  . LYS   B 1 110 ? 26.526 -24.394 -1.406  1.00 19.16 ?  110 LYS   B HZ3  1 
ATOM   5494 N  N    . SER   B 1 111 ? 31.314 -21.256 3.245   1.00 13.77 ?  111 SER   B N    1 
ATOM   5495 C  CA   . SER   B 1 111 ? 31.700 -19.858 3.418   1.00 13.60 ?  111 SER   B CA   1 
ATOM   5496 C  C    . SER   B 1 111 ? 33.076 -19.596 2.822   1.00 12.88 ?  111 SER   B C    1 
ATOM   5497 O  O    . SER   B 1 111 ? 33.296 -18.570 2.162   1.00 13.08 ?  111 SER   B O    1 
ATOM   5498 C  CB   . SER   B 1 111 ? 31.704 -19.501 4.903   1.00 14.60 ?  111 SER   B CB   1 
ATOM   5499 O  OG   . SER   B 1 111 ? 30.402 -19.498 5.442   1.00 15.93 ?  111 SER   B OG   1 
ATOM   5500 H  H    . SER   B 1 111 ? 31.128 -21.675 3.979   1.00 16.52 ?  111 SER   B H    1 
ATOM   5501 H  HA   . SER   B 1 111 ? 31.059 -19.295 2.967   1.00 16.31 ?  111 SER   B HA   1 
ATOM   5502 H  HB2  . SER   B 1 111 ? 32.229 -20.158 5.387   1.00 17.51 ?  111 SER   B HB2  1 
ATOM   5503 H  HB3  . SER   B 1 111 ? 32.089 -18.622 5.015   1.00 17.51 ?  111 SER   B HB3  1 
ATOM   5504 H  HG   . SER   B 1 111 ? 30.424 -19.290 6.264   1.00 19.11 ?  111 SER   B HG   1 
ATOM   5505 N  N    . ALA   B 1 112 ? 34.018 -20.513 3.049   1.00 12.82 ?  112 ALA   B N    1 
ATOM   5506 C  CA   . ALA   B 1 112 ? 35.359 -20.344 2.499   1.00 12.74 ?  112 ALA   B CA   1 
ATOM   5507 C  C    . ALA   B 1 112 ? 35.319 -20.247 0.976   1.00 12.18 ?  112 ALA   B C    1 
ATOM   5508 O  O    . ALA   B 1 112 ? 35.944 -19.359 0.381   1.00 12.49 ?  112 ALA   B O    1 
ATOM   5509 C  CB   . ALA   B 1 112 ? 36.265 -21.489 2.961   1.00 13.58 ?  112 ALA   B CB   1 
ATOM   5510 H  H    . ALA   B 1 112 ? 33.910 -21.231 3.521   1.00 15.38 ?  112 ALA   B H    1 
ATOM   5511 H  HA   . ALA   B 1 112 ? 35.730 -19.518 2.841   1.00 15.28 ?  112 ALA   B HA   1 
ATOM   5512 H  HB1  . ALA   B 1 112 ? 37.153 -21.354 2.590   1.00 16.29 ?  112 ALA   B HB1  1 
ATOM   5513 H  HB2  . ALA   B 1 112 ? 36.314 -21.482 3.933   1.00 16.29 ?  112 ALA   B HB2  1 
ATOM   5514 H  HB3  . ALA   B 1 112 ? 35.900 -22.330 2.655   1.00 16.29 ?  112 ALA   B HB3  1 
ATOM   5515 N  N    . TYR   B 1 113 ? 34.589 -21.156 0.321   1.00 12.13 ?  113 TYR   B N    1 
ATOM   5516 C  CA   . TYR   B 1 113 ? 34.513 -21.105 -1.135  1.00 11.78 ?  113 TYR   B CA   1 
ATOM   5517 C  C    . TYR   B 1 113 ? 33.800 -19.854 -1.650  1.00 11.39 ?  113 TYR   B C    1 
ATOM   5518 O  O    . TYR   B 1 113 ? 34.061 -19.421 -2.778  1.00 11.78 ?  113 TYR   B O    1 
ATOM   5519 C  CB   . TYR   B 1 113 ? 33.841 -22.362 -1.684  1.00 11.89 ?  113 TYR   B CB   1 
ATOM   5520 C  CG   . TYR   B 1 113 ? 34.805 -23.510 -1.945  1.00 12.29 ?  113 TYR   B CG   1 
ATOM   5521 C  CD1  . TYR   B 1 113 ? 35.793 -23.406 -2.916  1.00 12.92 ?  113 TYR   B CD1  1 
ATOM   5522 C  CD2  . TYR   B 1 113 ? 34.706 -24.703 -1.241  1.00 12.78 ?  113 TYR   B CD2  1 
ATOM   5523 C  CE1  . TYR   B 1 113 ? 36.675 -24.443 -3.165  1.00 13.34 ?  113 TYR   B CE1  1 
ATOM   5524 C  CE2  . TYR   B 1 113 ? 35.576 -25.753 -1.487  1.00 13.23 ?  113 TYR   B CE2  1 
ATOM   5525 C  CZ   . TYR   B 1 113 ? 36.557 -25.621 -2.453  1.00 13.07 ?  113 TYR   B CZ   1 
ATOM   5526 O  OH   . TYR   B 1 113 ? 37.434 -26.638 -2.723  1.00 14.00 ?  113 TYR   B OH   1 
ATOM   5527 H  H    . TYR   B 1 113 ? 34.130 -21.789 0.694   1.00 14.55 ?  113 TYR   B H    1 
ATOM   5528 H  HA   . TYR   B 1 113 ? 35.414 -21.085 -1.474  1.00 14.13 ?  113 TYR   B HA   1 
ATOM   5529 H  HB2  . TYR   B 1 113 ? 33.178 -22.677 -1.047  1.00 14.26 ?  113 TYR   B HB2  1 
ATOM   5530 H  HB3  . TYR   B 1 113 ? 33.406 -22.142 -2.524  1.00 14.26 ?  113 TYR   B HB3  1 
ATOM   5531 H  HD1  . TYR   B 1 113 ? 35.878 -22.611 -3.400  1.00 15.50 ?  113 TYR   B HD1  1 
ATOM   5532 H  HD2  . TYR   B 1 113 ? 34.041 -24.794 -0.600  1.00 15.33 ?  113 TYR   B HD2  1 
ATOM   5533 H  HE1  . TYR   B 1 113 ? 37.334 -24.354 -3.821  1.00 16.00 ?  113 TYR   B HE1  1 
ATOM   5534 H  HE2  . TYR   B 1 113 ? 35.493 -26.547 -1.012  1.00 15.88 ?  113 TYR   B HE2  1 
ATOM   5535 H  HH   . TYR   B 1 113 ? 37.259 -27.303 -2.241  1.00 16.80 ?  113 TYR   B HH   1 
ATOM   5536 N  N    . GLU   B 1 114 ? 32.876 -19.283 -0.873  1.00 11.71 ?  114 GLU   B N    1 
ATOM   5537 C  CA   . GLU   B 1 114 ? 32.192 -18.071 -1.328  1.00 11.76 ?  114 GLU   B CA   1 
ATOM   5538 C  C    . GLU   B 1 114 ? 33.174 -16.947 -1.626  1.00 11.62 ?  114 GLU   B C    1 
ATOM   5539 O  O    . GLU   B 1 114 ? 32.890 -16.083 -2.460  1.00 12.01 ?  114 GLU   B O    1 
ATOM   5540 C  CB   . GLU   B 1 114 ? 31.135 -17.641 -0.307  1.00 12.25 ?  114 GLU   B CB   1 
ATOM   5541 C  CG   . GLU   B 1 114 ? 29.927 -18.575 -0.356  1.00 12.59 ?  114 GLU   B CG   1 
ATOM   5542 C  CD   . GLU   B 1 114 ? 28.897 -18.385 0.750   1.00 12.91 ?  114 GLU   B CD   1 
ATOM   5543 O  OE1  . GLU   B 1 114 ? 29.181 -17.765 1.795   1.00 13.12 ?  114 GLU   B OE1  1 
ATOM   5544 O  OE2  . GLU   B 1 114 ? 27.772 -18.920 0.576   1.00 13.90 -1 114 GLU   B OE2  1 
ATOM   5545 H  H    . GLU   B 1 114 ? 32.621 -19.579 -0.100  1.00 14.04 ?  114 GLU   B H    1 
ATOM   5546 H  HA   . GLU   B 1 114 ? 31.728 -18.273 -2.151  1.00 14.11 ?  114 GLU   B HA   1 
ATOM   5547 H  HB2  . GLU   B 1 114 ? 31.510 -17.677 0.589   1.00 14.69 ?  114 GLU   B HB2  1 
ATOM   5548 H  HB3  . GLU   B 1 114 ? 30.831 -16.744 -0.511  1.00 14.69 ?  114 GLU   B HB3  1 
ATOM   5549 H  HG2  . GLU   B 1 114 ? 29.478 -18.444 -1.201  1.00 15.11 ?  114 GLU   B HG2  1 
ATOM   5550 H  HG3  . GLU   B 1 114 ? 30.251 -19.490 -0.298  1.00 15.11 ?  114 GLU   B HG3  1 
ATOM   5551 N  N    . ASN   B 1 115 ? 34.342 -16.944 -0.976  1.00 11.49 ?  115 ASN   B N    1 
ATOM   5552 C  CA   . ASN   B 1 115 ? 35.331 -15.911 -1.277  1.00 11.38 ?  115 ASN   B CA   1 
ATOM   5553 C  C    . ASN   B 1 115 ? 35.739 -15.927 -2.747  1.00 11.21 ?  115 ASN   B C    1 
ATOM   5554 O  O    . ASN   B 1 115 ? 36.126 -14.890 -3.303  1.00 11.72 ?  115 ASN   B O    1 
ATOM   5555 C  CB   . ASN   B 1 115 ? 36.574 -16.086 -0.394  1.00 12.19 ?  115 ASN   B CB   1 
ATOM   5556 C  CG   . ASN   B 1 115 ? 36.308 -15.818 1.070   1.00 12.53 ?  115 ASN   B CG   1 
ATOM   5557 O  OD1  . ASN   B 1 115 ? 36.310 -14.669 1.509   1.00 14.38 ?  115 ASN   B OD1  1 
ATOM   5558 N  ND2  . ASN   B 1 115 ? 36.140 -16.882 1.850   1.00 12.66 ?  115 ASN   B ND2  1 
ATOM   5559 H  H    . ASN   B 1 115 ? 34.580 -17.508 -0.365  1.00 13.78 ?  115 ASN   B H    1 
ATOM   5560 H  HA   . ASN   B 1 115 ? 34.953 -15.041 -1.080  1.00 13.65 ?  115 ASN   B HA   1 
ATOM   5561 H  HB2  . ASN   B 1 115 ? 36.896 -16.999 -0.478  1.00 14.62 ?  115 ASN   B HB2  1 
ATOM   5562 H  HB3  . ASN   B 1 115 ? 37.261 -15.467 -0.688  1.00 14.62 ?  115 ASN   B HB3  1 
ATOM   5563 H  HD21 . ASN   B 1 115 ? 35.997 -16.779 2.694   1.00 15.18 ?  115 ASN   B HD21 1 
ATOM   5564 H  HD22 . ASN   B 1 115 ? 36.160 -17.672 1.513   1.00 15.18 ?  115 ASN   B HD22 1 
ATOM   5565 N  N    . PHE   B 1 116 ? 35.704 -17.102 -3.386  1.00 11.12 ?  116 PHE   B N    1 
ATOM   5566 C  CA   . PHE   B 1 116 ? 36.134 -17.193 -4.775  1.00 11.32 ?  116 PHE   B CA   1 
ATOM   5567 C  C    . PHE   B 1 116 ? 35.229 -16.369 -5.685  1.00 11.03 ?  116 PHE   B C    1 
ATOM   5568 O  O    . PHE   B 1 116 ? 35.658 -15.934 -6.759  1.00 11.68 ?  116 PHE   B O    1 
ATOM   5569 C  CB   . PHE   B 1 116 ? 36.098 -18.639 -5.300  1.00 11.38 ?  116 PHE   B CB   1 
ATOM   5570 C  CG   . PHE   B 1 116 ? 37.173 -19.600 -4.758  1.00 11.11 ?  116 PHE   B CG   1 
ATOM   5571 C  CD1  . PHE   B 1 116 ? 37.821 -19.419 -3.545  1.00 11.99 ?  116 PHE   B CD1  1 
ATOM   5572 C  CD2  . PHE   B 1 116 ? 37.476 -20.736 -5.500  1.00 11.01 ?  116 PHE   B CD2  1 
ATOM   5573 C  CE1  . PHE   B 1 116 ? 38.754 -20.360 -3.094  1.00 12.09 ?  116 PHE   B CE1  1 
ATOM   5574 C  CE2  . PHE   B 1 116 ? 38.404 -21.669 -5.059  1.00 11.53 ?  116 PHE   B CE2  1 
ATOM   5575 C  CZ   . PHE   B 1 116 ? 39.039 -21.487 -3.857  1.00 11.85 ?  116 PHE   B CZ   1 
ATOM   5576 H  H    . PHE   B 1 116 ? 35.439 -17.848 -3.039  1.00 13.33 ?  116 PHE   B H    1 
ATOM   5577 H  HA   . PHE   B 1 116 ? 37.039 -16.862 -4.857  1.00 13.58 ?  116 PHE   B HA   1 
ATOM   5578 H  HB2  . PHE   B 1 116 ? 35.227 -19.019 -5.078  1.00 13.65 ?  116 PHE   B HB2  1 
ATOM   5579 H  HB3  . PHE   B 1 116 ? 36.192 -18.614 -6.265  1.00 13.65 ?  116 PHE   B HB3  1 
ATOM   5580 H  HD1  . PHE   B 1 116 ? 37.617 -18.677 -3.023  1.00 14.39 ?  116 PHE   B HD1  1 
ATOM   5581 H  HD2  . PHE   B 1 116 ? 37.037 -20.877 -6.313  1.00 13.21 ?  116 PHE   B HD2  1 
ATOM   5582 H  HE1  . PHE   B 1 116 ? 39.185 -20.227 -2.284  1.00 14.51 ?  116 PHE   B HE1  1 
ATOM   5583 H  HE2  . PHE   B 1 116 ? 38.594 -22.416 -5.580  1.00 13.83 ?  116 PHE   B HE2  1 
ATOM   5584 H  HZ   . PHE   B 1 116 ? 39.671 -22.100 -3.569  1.00 14.22 ?  116 PHE   B HZ   1 
ATOM   5585 N  N    . ASN   B 1 117 ? 33.965 -16.170 -5.296  1.00 11.19 ?  117 ASN   B N    1 
ATOM   5586 C  CA   . ASN   B 1 117 ? 33.021 -15.466 -6.159  1.00 11.73 ?  117 ASN   B CA   1 
ATOM   5587 C  C    . ASN   B 1 117 ? 33.332 -13.987 -6.311  1.00 12.09 ?  117 ASN   B C    1 
ATOM   5588 O  O    . ASN   B 1 117 ? 32.718 -13.327 -7.155  1.00 13.38 ?  117 ASN   B O    1 
ATOM   5589 C  CB   . ASN   B 1 117 ? 31.596 -15.688 -5.666  1.00 12.15 ?  117 ASN   B CB   1 
ATOM   5590 C  CG   . ASN   B 1 117 ? 31.144 -17.096 -5.923  1.00 12.32 ?  117 ASN   B CG   1 
ATOM   5591 O  OD1  . ASN   B 1 117 ? 31.497 -17.683 -6.945  1.00 13.15 ?  117 ASN   B OD1  1 
ATOM   5592 N  ND2  . ASN   B 1 117 ? 30.408 -17.673 -4.986  1.00 12.30 ?  117 ASN   B ND2  1 
ATOM   5593 H  H    . ASN   B 1 117 ? 33.643 -16.417 -4.532  1.00 13.42 ?  117 ASN   B H    1 
ATOM   5594 H  HA   . ASN   B 1 117 ? 33.081 -15.862 -7.034  1.00 14.07 ?  117 ASN   B HA   1 
ATOM   5595 H  HB2  . ASN   B 1 117 ? 31.552 -15.528 -4.705  1.00 14.57 ?  117 ASN   B HB2  1 
ATOM   5596 H  HB3  . ASN   B 1 117 ? 30.997 -15.080 -6.128  1.00 14.57 ?  117 ASN   B HB3  1 
ATOM   5597 H  HD21 . ASN   B 1 117 ? 30.125 -18.480 -5.093  1.00 14.76 ?  117 ASN   B HD21 1 
ATOM   5598 H  HD22 . ASN   B 1 117 ? 30.185 -17.234 -4.278  1.00 14.76 ?  117 ASN   B HD22 1 
ATOM   5599 N  N    . GLN   B 1 118 ? 34.266 -13.459 -5.534  1.00 11.98 ?  118 GLN   B N    1 
ATOM   5600 C  CA   . GLN   B 1 118 ? 34.688 -12.071 -5.673  1.00 12.61 ?  118 GLN   B CA   1 
ATOM   5601 C  C    . GLN   B 1 118 ? 35.757 -11.873 -6.745  1.00 12.64 ?  118 GLN   B C    1 
ATOM   5602 O  O    . GLN   B 1 118 ? 36.227 -10.744 -6.922  1.00 14.04 ?  118 GLN   B O    1 
ATOM   5603 C  CB   . GLN   B 1 118 ? 35.161 -11.542 -4.317  1.00 12.96 ?  118 GLN   B CB   1 
ATOM   5604 C  CG   . GLN   B 1 118 ? 34.079 -11.584 -3.248  1.00 13.29 ?  118 GLN   B CG   1 
ATOM   5605 C  CD   . GLN   B 1 118 ? 32.915 -10.675 -3.581  1.00 13.16 ?  118 GLN   B CD   1 
ATOM   5606 O  OE1  . GLN   B 1 118 ? 33.101 -9.539  -4.032  1.00 13.94 ?  118 GLN   B OE1  1 
ATOM   5607 N  NE2  . GLN   B 1 118 ? 31.705 -11.168 -3.367  1.00 13.61 ?  118 GLN   B NE2  1 
ATOM   5608 H  H    . GLN   B 1 118 ? 34.688 -13.885 -4.913  1.00 14.37 ?  118 GLN   B H    1 
ATOM   5609 H  HA   . GLN   B 1 118 ? 33.922 -11.546 -5.942  1.00 15.13 ?  118 GLN   B HA   1 
ATOM   5610 H  HB2  . GLN   B 1 118 ? 35.908 -12.069 -4.007  1.00 15.55 ?  118 GLN   B HB2  1 
ATOM   5611 H  HB3  . GLN   B 1 118 ? 35.431 -10.611 -4.417  1.00 15.55 ?  118 GLN   B HB3  1 
ATOM   5612 H  HG2  . GLN   B 1 118 ? 33.742 -12.496 -3.174  1.00 15.95 ?  118 GLN   B HG2  1 
ATOM   5613 H  HG3  . GLN   B 1 118 ? 34.454 -11.303 -2.399  1.00 15.95 ?  118 GLN   B HG3  1 
ATOM   5614 H  HE21 . GLN   B 1 118 ? 31.610 -11.959 -3.046  1.00 16.33 ?  118 GLN   B HE21 1 
ATOM   5615 H  HE22 . GLN   B 1 118 ? 31.016 -10.685 -3.539  1.00 16.33 ?  118 GLN   B HE22 1 
ATOM   5616 N  N    . HIS   B 1 119 ? 36.115 -12.927 -7.483  1.00 12.10 ?  119 HIS   B N    1 
ATOM   5617 C  CA   . HIS   B 1 119 ? 37.157 -12.876 -8.500  1.00 12.40 ?  119 HIS   B CA   1 
ATOM   5618 C  C    . HIS   B 1 119 ? 36.676 -13.604 -9.743  1.00 12.46 ?  119 HIS   B C    1 
ATOM   5619 O  O    . HIS   B 1 119 ? 36.172 -14.724 -9.647  1.00 13.26 ?  119 HIS   B O    1 
ATOM   5620 C  CB   . HIS   B 1 119 ? 38.435 -13.510 -7.950  1.00 13.10 ?  119 HIS   B CB   1 
ATOM   5621 C  CG   . HIS   B 1 119 ? 38.916 -12.820 -6.719  1.00 13.75 ?  119 HIS   B CG   1 
ATOM   5622 N  ND1  . HIS   B 1 119 ? 39.706 -11.691 -6.766  1.00 15.87 ?  119 HIS   B ND1  1 
ATOM   5623 C  CD2  . HIS   B 1 119 ? 38.626 -13.025 -5.413  1.00 15.11 ?  119 HIS   B CD2  1 
ATOM   5624 C  CE1  . HIS   B 1 119 ? 39.918 -11.259 -5.537  1.00 16.65 ?  119 HIS   B CE1  1 
ATOM   5625 N  NE2  . HIS   B 1 119 ? 39.271 -12.048 -4.698  1.00 16.57 ?  119 HIS   B NE2  1 
ATOM   5626 H  H    . HIS   B 1 119 ? 35.744 -13.705 -7.420  1.00 14.52 ?  119 HIS   B H    1 
ATOM   5627 H  HA   . HIS   B 1 119 ? 37.341 -11.952 -8.733  1.00 14.87 ?  119 HIS   B HA   1 
ATOM   5628 H  HB2  . HIS   B 1 119 ? 38.264 -14.438 -7.735  1.00 15.71 ?  119 HIS   B HB2  1 
ATOM   5629 H  HB3  . HIS   B 1 119 ? 39.134 -13.448 -8.625  1.00 15.71 ?  119 HIS   B HB3  1 
ATOM   5630 H  HD2  . HIS   B 1 119 ? 38.102 -13.713 -5.065  1.00 18.12 ?  119 HIS   B HD2  1 
ATOM   5631 H  HE1  . HIS   B 1 119 ? 40.446 -10.533 -5.299  1.00 19.97 ?  119 HIS   B HE1  1 
ATOM   5632 H  HE2  . HIS   B 1 119 ? 39.277 -11.978 -3.839  1.00 19.88 ?  119 HIS   B HE2  1 
ATOM   5633 N  N    . GLU   B 1 120 ? 36.832 -12.976 -10.910 1.00 12.99 ?  120 GLU   B N    1 
ATOM   5634 C  CA   . GLU   B 1 120 ? 36.246 -13.544 -12.119 1.00 14.34 ?  120 GLU   B CA   1 
ATOM   5635 C  C    . GLU   B 1 120 ? 36.911 -14.849 -12.532 1.00 13.09 ?  120 GLU   B C    1 
ATOM   5636 O  O    . GLU   B 1 120 ? 36.242 -15.721 -13.102 1.00 13.50 ?  120 GLU   B O    1 
ATOM   5637 C  CB   . GLU   B 1 120 ? 36.289 -12.527 -13.259 1.00 18.94 ?  120 GLU   B CB   1 
ATOM   5638 C  CG   . GLU   B 1 120 ? 35.355 -11.352 -13.045 1.00 25.86 ?  120 GLU   B CG   1 
ATOM   5639 C  CD   . GLU   B 1 120 ? 35.202 -10.492 -14.282 1.00 31.96 ?  120 GLU   B CD   1 
ATOM   5640 O  OE1  . GLU   B 1 120 ? 36.169 -10.408 -15.070 1.00 34.22 ?  120 GLU   B OE1  1 
ATOM   5641 O  OE2  . GLU   B 1 120 ? 34.117 -9.903  -14.466 1.00 35.04 -1 120 GLU   B OE2  1 
ATOM   5642 H  H    . GLU   B 1 120 ? 37.263 -12.235 -11.028 1.00 15.59 ?  120 GLU   B H    1 
ATOM   5643 H  HA   . GLU   B 1 120 ? 35.319 -13.741 -11.943 1.00 17.20 ?  120 GLU   B HA   1 
ATOM   5644 H  HB2  . GLU   B 1 120 ? 37.190 -12.178 -13.343 1.00 22.72 ?  120 GLU   B HB2  1 
ATOM   5645 H  HB3  . GLU   B 1 120 ? 36.028 -12.967 -14.085 1.00 22.72 ?  120 GLU   B HB3  1 
ATOM   5646 H  HG2  . GLU   B 1 120 ? 34.477 -11.686 -12.797 1.00 31.03 ?  120 GLU   B HG2  1 
ATOM   5647 H  HG3  . GLU   B 1 120 ? 35.706 -10.790 -12.338 1.00 31.03 ?  120 GLU   B HG3  1 
ATOM   5648 N  N    . VAL   B 1 121 ? 38.209 -15.002 -12.262 1.00 12.88 ?  121 VAL   B N    1 
ATOM   5649 C  CA   . VAL   B 1 121 ? 38.953 -16.207 -12.621 1.00 12.82 ?  121 VAL   B CA   1 
ATOM   5650 C  C    . VAL   B 1 121 ? 40.070 -16.419 -11.605 1.00 12.12 ?  121 VAL   B C    1 
ATOM   5651 O  O    . VAL   B 1 121 ? 40.743 -15.465 -11.201 1.00 12.88 ?  121 VAL   B O    1 
ATOM   5652 C  CB   . VAL   B 1 121 ? 39.460 -16.150 -14.081 1.00 14.66 ?  121 VAL   B CB   1 
ATOM   5653 C  CG1  . VAL   B 1 121 ? 40.328 -14.912 -14.327 1.00 16.14 ?  121 VAL   B CG1  1 
ATOM   5654 C  CG2  . VAL   B 1 121 ? 40.194 -17.427 -14.455 1.00 15.74 ?  121 VAL   B CG2  1 
ATOM   5655 H  H    . VAL   B 1 121 ? 38.697 -14.404 -11.873 1.00 15.45 ?  121 VAL   B H    1 
ATOM   5656 H  HA   . VAL   B 1 121 ? 38.346 -16.961 -12.559 1.00 15.38 ?  121 VAL   B HA   1 
ATOM   5657 H  HB   . VAL   B 1 121 ? 38.690 -16.079 -14.670 1.00 17.59 ?  121 VAL   B HB   1 
ATOM   5658 H  HG11 . VAL   B 1 121 ? 40.637 -14.917 -15.248 1.00 19.36 ?  121 VAL   B HG11 1 
ATOM   5659 H  HG12 . VAL   B 1 121 ? 39.799 -14.114 -14.163 1.00 19.36 ?  121 VAL   B HG12 1 
ATOM   5660 H  HG13 . VAL   B 1 121 ? 41.088 -14.932 -13.725 1.00 19.36 ?  121 VAL   B HG13 1 
ATOM   5661 H  HG21 . VAL   B 1 121 ? 40.395 -17.408 -15.405 1.00 18.88 ?  121 VAL   B HG21 1 
ATOM   5662 H  HG22 . VAL   B 1 121 ? 41.018 -17.479 -13.946 1.00 18.88 ?  121 VAL   B HG22 1 
ATOM   5663 H  HG23 . VAL   B 1 121 ? 39.628 -18.186 -14.252 1.00 18.88 ?  121 VAL   B HG23 1 
ATOM   5664 N  N    . LEU   B 1 122 ? 40.255 -17.675 -11.183 1.00 11.79 ?  122 LEU   B N    1 
ATOM   5665 C  CA   . LEU   B 1 122 ? 41.229 -18.038 -10.157 1.00 11.34 ?  122 LEU   B CA   1 
ATOM   5666 C  C    . LEU   B 1 122 ? 41.886 -19.370 -10.485 1.00 11.34 ?  122 LEU   B C    1 
ATOM   5667 O  O    . LEU   B 1 122 ? 41.227 -20.288 -10.991 1.00 12.69 ?  122 LEU   B O    1 
ATOM   5668 C  CB   . LEU   B 1 122 ? 40.578 -18.273 -8.778  1.00 13.35 ?  122 LEU   B CB   1 
ATOM   5669 C  CG   . LEU   B 1 122 ? 39.548 -17.259 -8.275  1.00 13.54 ?  122 LEU   B CG   1 
ATOM   5670 C  CD1  . LEU   B 1 122 ? 38.141 -17.615 -8.746  1.00 14.13 ?  122 LEU   B CD1  1 
ATOM   5671 C  CD2  . LEU   B 1 122 ? 39.599 -17.155 -6.764  1.00 12.76 ?  122 LEU   B CD2  1 
ATOM   5672 H  H    . LEU   B 1 122 ? 39.817 -18.353 -11.485 1.00 14.15 ?  122 LEU   B H    1 
ATOM   5673 H  HA   . LEU   B 1 122 ? 41.910 -17.350 -10.075 1.00 13.60 ?  122 LEU   B HA   1 
ATOM   5674 H  HB2  . LEU   B 1 122 ? 40.133 -19.132 -8.802  1.00 16.01 ?  122 LEU   B HB2  1 
ATOM   5675 H  HB3  . LEU   B 1 122 ? 41.284 -18.299 -8.115  1.00 16.01 ?  122 LEU   B HB3  1 
ATOM   5676 H  HG   . LEU   B 1 122 ? 39.765 -16.387 -8.637  1.00 16.24 ?  122 LEU   B HG   1 
ATOM   5677 H  HD11 . LEU   B 1 122 ? 37.514 -16.964 -8.388  1.00 16.95 ?  122 LEU   B HD11 1 
ATOM   5678 H  HD12 . LEU   B 1 122 ? 38.117 -17.593 -9.716  1.00 16.95 ?  122 LEU   B HD12 1 
ATOM   5679 H  HD13 . LEU   B 1 122 ? 37.914 -18.501 -8.429  1.00 16.95 ?  122 LEU   B HD13 1 
ATOM   5680 H  HD21 . LEU   B 1 122 ? 38.920 -16.532 -6.463  1.00 15.31 ?  122 LEU   B HD21 1 
ATOM   5681 H  HD22 . LEU   B 1 122 ? 39.442 -18.029 -6.377  1.00 15.31 ?  122 LEU   B HD22 1 
ATOM   5682 H  HD23 . LEU   B 1 122 ? 40.479 -16.832 -6.500  1.00 15.31 ?  122 LEU   B HD23 1 
ATOM   5683 N  N    . LEU   B 1 123 ? 43.171 -19.484 -10.119 1.00 11.11 ?  123 LEU   B N    1 
ATOM   5684 C  CA   . LEU   B 1 123 ? 43.879 -20.758 -10.012 1.00 11.31 ?  123 LEU   B CA   1 
ATOM   5685 C  C    . LEU   B 1 123 ? 43.857 -21.152 -8.541  1.00 10.85 ?  123 LEU   B C    1 
ATOM   5686 O  O    . LEU   B 1 123 ? 44.202 -20.326 -7.687  1.00 11.21 ?  123 LEU   B O    1 
ATOM   5687 C  CB   . LEU   B 1 123 ? 45.326 -20.577 -10.481 1.00 11.91 ?  123 LEU   B CB   1 
ATOM   5688 C  CG   . LEU   B 1 123 ? 46.264 -21.768 -10.247 1.00 12.08 ?  123 LEU   B CG   1 
ATOM   5689 C  CD1  . LEU   B 1 123 ? 45.828 -23.012 -11.017 1.00 12.52 ?  123 LEU   B CD1  1 
ATOM   5690 C  CD2  . LEU   B 1 123 ? 47.684 -21.381 -10.628 1.00 12.65 ?  123 LEU   B CD2  1 
ATOM   5691 H  H    . LEU   B 1 123 ? 43.671 -18.803 -9.921  1.00 13.33 ?  123 LEU   B H    1 
ATOM   5692 H  HA   . LEU   B 1 123 ? 43.440 -21.438 -10.543 1.00 13.57 ?  123 LEU   B HA   1 
ATOM   5693 H  HB2  . LEU   B 1 123 ? 45.316 -20.401 -11.435 1.00 14.29 ?  123 LEU   B HB2  1 
ATOM   5694 H  HB3  . LEU   B 1 123 ? 45.706 -19.818 -10.016 1.00 14.29 ?  123 LEU   B HB3  1 
ATOM   5695 H  HG   . LEU   B 1 123 ? 46.262 -21.993 -9.304  1.00 14.49 ?  123 LEU   B HG   1 
ATOM   5696 H  HD11 . LEU   B 1 123 ? 46.462 -23.726 -10.848 1.00 15.02 ?  123 LEU   B HD11 1 
ATOM   5697 H  HD12 . LEU   B 1 123 ? 44.943 -23.277 -10.717 1.00 15.02 ?  123 LEU   B HD12 1 
ATOM   5698 H  HD13 . LEU   B 1 123 ? 45.807 -22.805 -11.964 1.00 15.02 ?  123 LEU   B HD13 1 
ATOM   5699 H  HD21 . LEU   B 1 123 ? 48.266 -22.142 -10.479 1.00 15.18 ?  123 LEU   B HD21 1 
ATOM   5700 H  HD22 . LEU   B 1 123 ? 47.699 -21.130 -11.564 1.00 15.18 ?  123 LEU   B HD22 1 
ATOM   5701 H  HD23 . LEU   B 1 123 ? 47.962 -20.635 -10.077 1.00 15.18 ?  123 LEU   B HD23 1 
ATOM   5702 N  N    . ALA   B 1 124 ? 43.425 -22.381 -8.234  1.00 11.13 ?  124 ALA   B N    1 
ATOM   5703 C  CA   . ALA   B 1 124 ? 43.159 -22.701 -6.838  1.00 11.16 ?  124 ALA   B CA   1 
ATOM   5704 C  C    . ALA   B 1 124 ? 43.446 -24.160 -6.514  1.00 10.70 ?  124 ALA   B C    1 
ATOM   5705 O  O    . ALA   B 1 124 ? 43.311 -25.038 -7.378  1.00 11.62 ?  124 ALA   B O    1 
ATOM   5706 C  CB   . ALA   B 1 124 ? 41.706 -22.401 -6.463  1.00 11.80 ?  124 ALA   B CB   1 
ATOM   5707 H  H    . ALA   B 1 124 ? 43.264 -23.014 -8.800  1.00 13.35 ?  124 ALA   B H    1 
ATOM   5708 H  HA   . ALA   B 1 124 ? 43.732 -22.151 -6.292  1.00 13.39 ?  124 ALA   B HA   1 
ATOM   5709 H  HB1  . ALA   B 1 124 ? 41.563 -22.626 -5.533  1.00 14.15 ?  124 ALA   B HB1  1 
ATOM   5710 H  HB2  . ALA   B 1 124 ? 41.536 -21.454 -6.604  1.00 14.15 ?  124 ALA   B HB2  1 
ATOM   5711 H  HB3  . ALA   B 1 124 ? 41.115 -22.927 -7.027  1.00 14.15 ?  124 ALA   B HB3  1 
ATOM   5712 N  N    . PRO   B 1 125 ? 43.739 -24.454 -5.250  1.00 10.85 ?  125 PRO   B N    1 
ATOM   5713 C  CA   . PRO   B 1 125 ? 43.681 -25.821 -4.729  1.00 11.95 ?  125 PRO   B CA   1 
ATOM   5714 C  C    . PRO   B 1 125 ? 42.284 -26.099 -4.172  1.00 12.11 ?  125 PRO   B C    1 
ATOM   5715 O  O    . PRO   B 1 125 ? 41.484 -25.186 -3.969  1.00 12.33 ?  125 PRO   B O    1 
ATOM   5716 C  CB   . PRO   B 1 125 ? 44.680 -25.750 -3.566  1.00 13.18 ?  125 PRO   B CB   1 
ATOM   5717 C  CG   . PRO   B 1 125 ? 44.432 -24.371 -2.988  1.00 12.85 ?  125 PRO   B CG   1 
ATOM   5718 C  CD   . PRO   B 1 125 ? 44.074 -23.488 -4.187  1.00 11.63 ?  125 PRO   B CD   1 
ATOM   5719 H  HA   . PRO   B 1 125 ? 43.950 -26.487 -5.384  1.00 14.33 ?  125 PRO   B HA   1 
ATOM   5720 H  HB2  . PRO   B 1 125 ? 44.480 -26.441 -2.913  1.00 15.81 ?  125 PRO   B HB2  1 
ATOM   5721 H  HB3  . PRO   B 1 125 ? 45.586 -25.833 -3.897  1.00 15.81 ?  125 PRO   B HB3  1 
ATOM   5722 H  HG2  . PRO   B 1 125 ? 43.696 -24.399 -2.355  1.00 15.42 ?  125 PRO   B HG2  1 
ATOM   5723 H  HG3  . PRO   B 1 125 ? 45.240 -24.045 -2.550  1.00 15.42 ?  125 PRO   B HG3  1 
ATOM   5724 H  HD2  . PRO   B 1 125 ? 43.312 -22.929 -3.985  1.00 13.95 ?  125 PRO   B HD2  1 
ATOM   5725 H  HD3  . PRO   B 1 125 ? 44.846 -22.952 -4.450  1.00 13.95 ?  125 PRO   B HD3  1 
ATOM   5726 N  N    . LEU   B 1 126 ? 42.021 -27.376 -3.880  1.00 12.66 ?  126 LEU   B N    1 
ATOM   5727 C  CA   . LEU   B 1 126 ? 40.803 -27.743 -3.162  1.00 13.11 ?  126 LEU   B CA   1 
ATOM   5728 C  C    . LEU   B 1 126 ? 40.926 -27.344 -1.696  1.00 13.13 ?  126 LEU   B C    1 
ATOM   5729 O  O    . LEU   B 1 126 ? 41.818 -27.815 -0.984  1.00 15.27 ?  126 LEU   B O    1 
ATOM   5730 C  CB   . LEU   B 1 126 ? 40.567 -29.245 -3.275  1.00 14.51 ?  126 LEU   B CB   1 
ATOM   5731 C  CG   . LEU   B 1 126 ? 40.034 -29.730 -4.625  1.00 15.36 ?  126 LEU   B CG   1 
ATOM   5732 C  CD1  . LEU   B 1 126 ? 40.085 -31.241 -4.705  1.00 17.11 ?  126 LEU   B CD1  1 
ATOM   5733 C  CD2  . LEU   B 1 126 ? 38.618 -29.227 -4.873  1.00 15.51 ?  126 LEU   B CD2  1 
ATOM   5734 H  H    . LEU   B 1 126 ? 42.531 -28.039 -4.079  1.00 15.19 ?  126 LEU   B H    1 
ATOM   5735 H  HA   . LEU   B 1 126 ? 40.045 -27.274 -3.550  1.00 15.72 ?  126 LEU   B HA   1 
ATOM   5736 H  HB2  . LEU   B 1 126 ? 41.407 -29.698 -3.114  1.00 17.40 ?  126 LEU   B HB2  1 
ATOM   5737 H  HB3  . LEU   B 1 126 ? 39.921 -29.503 -2.600  1.00 17.40 ?  126 LEU   B HB3  1 
ATOM   5738 H  HG   . LEU   B 1 126 ? 40.603 -29.370 -5.329  1.00 18.42 ?  126 LEU   B HG   1 
ATOM   5739 H  HD11 . LEU   B 1 126 ? 39.745 -31.520 -5.568  1.00 20.53 ?  126 LEU   B HD11 1 
ATOM   5740 H  HD12 . LEU   B 1 126 ? 41.003 -31.530 -4.597  1.00 20.53 ?  126 LEU   B HD12 1 
ATOM   5741 H  HD13 . LEU   B 1 126 ? 39.534 -31.608 -3.995  1.00 20.53 ?  126 LEU   B HD13 1 
ATOM   5742 H  HD21 . LEU   B 1 126 ? 38.268 -29.655 -5.669  1.00 18.60 ?  126 LEU   B HD21 1 
ATOM   5743 H  HD22 . LEU   B 1 126 ? 38.068 -29.446 -4.107  1.00 18.60 ?  126 LEU   B HD22 1 
ATOM   5744 H  HD23 . LEU   B 1 126 ? 38.639 -28.263 -5.000  1.00 18.60 ?  126 LEU   B HD23 1 
ATOM   5745 N  N    . LEU   B 1 127 ? 40.001 -26.513 -1.231  1.00 12.99 ?  127 LEU   B N    1 
ATOM   5746 C  CA   . LEU   B 1 127 ? 40.058 -26.024 0.136   1.00 13.48 ?  127 LEU   B CA   1 
ATOM   5747 C  C    . LEU   B 1 127 ? 39.773 -27.140 1.136   1.00 13.12 ?  127 LEU   B C    1 
ATOM   5748 O  O    . LEU   B 1 127 ? 38.954 -28.037 0.907   1.00 13.60 ?  127 LEU   B O    1 
ATOM   5749 C  CB   . LEU   B 1 127 ? 39.056 -24.887 0.343   1.00 13.84 ?  127 LEU   B CB   1 
ATOM   5750 C  CG   . LEU   B 1 127 ? 39.238 -23.633 -0.500  1.00 14.44 ?  127 LEU   B CG   1 
ATOM   5751 C  CD1  . LEU   B 1 127 ? 38.111 -22.662 -0.186  1.00 14.72 ?  127 LEU   B CD1  1 
ATOM   5752 C  CD2  . LEU   B 1 127 ? 40.591 -22.984 -0.251  1.00 15.38 ?  127 LEU   B CD2  1 
ATOM   5753 H  H    . LEU   B 1 127 ? 39.330 -26.215 -1.690  1.00 15.59 ?  127 LEU   B H    1 
ATOM   5754 H  HA   . LEU   B 1 127 ? 40.951 -25.673 0.303   1.00 16.18 ?  127 LEU   B HA   1 
ATOM   5755 H  HB2  . LEU   B 1 127 ? 38.170 -25.235 0.148   1.00 16.60 ?  127 LEU   B HB2  1 
ATOM   5756 H  HB3  . LEU   B 1 127 ? 39.098 -24.619 1.271   1.00 16.60 ?  127 LEU   B HB3  1 
ATOM   5757 H  HG   . LEU   B 1 127 ? 39.176 -23.859 -1.438  1.00 17.32 ?  127 LEU   B HG   1 
ATOM   5758 H  HD11 . LEU   B 1 127 ? 38.232 -21.851 -0.711  1.00 17.66 ?  127 LEU   B HD11 1 
ATOM   5759 H  HD12 . LEU   B 1 127 ? 37.262 -23.072 -0.406  1.00 17.66 ?  127 LEU   B HD12 1 
ATOM   5760 H  HD13 . LEU   B 1 127 ? 38.136 -22.440 0.761   1.00 17.66 ?  127 LEU   B HD13 1 
ATOM   5761 H  HD21 . LEU   B 1 127 ? 40.634 -22.139 -0.727  1.00 18.45 ?  127 LEU   B HD21 1 
ATOM   5762 H  HD22 . LEU   B 1 127 ? 40.700 -22.829 0.702   1.00 18.45 ?  127 LEU   B HD22 1 
ATOM   5763 H  HD23 . LEU   B 1 127 ? 41.288 -23.578 -0.570  1.00 18.45 ?  127 LEU   B HD23 1 
ATOM   5764 N  N    . SER   B 1 128 ? 40.458 -27.057 2.270   1.00 13.28 ?  128 SER   B N    1 
ATOM   5765 C  CA   . SER   B 1 128 ? 40.343 -27.968 3.400   1.00 13.67 ?  128 SER   B CA   1 
ATOM   5766 C  C    . SER   B 1 128 ? 40.829 -29.381 3.089   1.00 15.14 ?  128 SER   B C    1 
ATOM   5767 O  O    . SER   B 1 128 ? 40.731 -30.257 3.951   1.00 16.99 ?  128 SER   B O    1 
ATOM   5768 C  CB   . SER   B 1 128 ? 38.941 -27.961 4.028   1.00 14.13 ?  128 SER   B CB   1 
ATOM   5769 O  OG   . SER   B 1 128 ? 38.638 -26.684 4.588   1.00 14.89 ?  128 SER   B OG   1 
ATOM   5770 H  H    . SER   B 1 128 ? 41.032 -26.428 2.410   1.00 15.93 ?  128 SER   B H    1 
ATOM   5771 H  HA   . SER   B 1 128 ? 40.936 -27.629 4.078   1.00 16.40 ?  128 SER   B HA   1 
ATOM   5772 H  HB2  . SER   B 1 128 ? 38.281 -28.180 3.351   1.00 16.95 ?  128 SER   B HB2  1 
ATOM   5773 H  HB3  . SER   B 1 128 ? 38.915 -28.634 4.737   1.00 16.95 ?  128 SER   B HB3  1 
ATOM   5774 H  HG   . SER   B 1 128 ? 39.211 -26.494 5.175   1.00 17.86 ?  128 SER   B HG   1 
ATOM   5775 N  N    . ALA   B 1 129 ? 41.390 -29.613 1.902   1.00 16.25 ?  129 ALA   B N    1 
ATOM   5776 C  CA   . ALA   B 1 129 ? 41.931 -30.915 1.551   1.00 17.73 ?  129 ALA   B CA   1 
ATOM   5777 C  C    . ALA   B 1 129 ? 43.332 -31.081 2.130   1.00 16.44 ?  129 ALA   B C    1 
ATOM   5778 O  O    . ALA   B 1 129 ? 43.886 -30.182 2.776   1.00 15.86 ?  129 ALA   B O    1 
ATOM   5779 C  CB   . ALA   B 1 129 ? 41.958 -31.086 0.034   1.00 19.97 ?  129 ALA   B CB   1 
ATOM   5780 H  H    . ALA   B 1 129 ? 41.472 -29.029 1.273   1.00 19.50 ?  129 ALA   B H    1 
ATOM   5781 H  HA   . ALA   B 1 129 ? 41.366 -31.609 1.922   1.00 21.27 ?  129 ALA   B HA   1 
ATOM   5782 H  HB1  . ALA   B 1 129 ? 42.312 -31.966 -0.180  1.00 23.96 ?  129 ALA   B HB1  1 
ATOM   5783 H  HB2  . ALA   B 1 129 ? 41.056 -31.001 -0.309  1.00 23.96 ?  129 ALA   B HB2  1 
ATOM   5784 H  HB3  . ALA   B 1 129 ? 42.527 -30.401 -0.352  1.00 23.96 ?  129 ALA   B HB3  1 
ATOM   5785 N  N    . GLY   B 1 130 ? 43.913 -32.253 1.879   1.00 16.21 ?  130 GLY   B N    1 
ATOM   5786 C  CA   . GLY   B 1 130 ? 45.307 -32.472 2.219   1.00 16.51 ?  130 GLY   B CA   1 
ATOM   5787 C  C    . GLY   B 1 130 ? 45.524 -32.388 3.711   1.00 16.24 ?  130 GLY   B C    1 
ATOM   5788 O  O    . GLY   B 1 130 ? 44.829 -33.044 4.504   1.00 17.12 ?  130 GLY   B O    1 
ATOM   5789 H  H    . GLY   B 1 130 ? 43.530 -32.927 1.507   1.00 19.45 ?  130 GLY   B H    1 
ATOM   5790 H  HA2  . GLY   B 1 130 ? 45.586 -33.352 1.914   1.00 19.81 ?  130 GLY   B HA2  1 
ATOM   5791 H  HA3  . GLY   B 1 130 ? 45.863 -31.806 1.784   1.00 19.81 ?  130 GLY   B HA3  1 
ATOM   5792 N  N    . ILE   B 1 131 ? 46.499 -31.559 4.103   1.00 16.65 ?  131 ILE   B N    1 
ATOM   5793 C  CA   . ILE   B 1 131 ? 46.863 -31.438 5.508   1.00 17.19 ?  131 ILE   B CA   1 
ATOM   5794 C  C    . ILE   B 1 131 ? 45.748 -30.843 6.353   1.00 16.87 ?  131 ILE   B C    1 
ATOM   5795 O  O    . ILE   B 1 131 ? 45.827 -30.912 7.583   1.00 18.42 ?  131 ILE   B O    1 
ATOM   5796 C  CB   . ILE   B 1 131 ? 48.186 -30.663 5.709   1.00 19.20 ?  131 ILE   B CB   1 
ATOM   5797 C  CG1  . ILE   B 1 131 ? 48.023 -29.182 5.344   1.00 20.08 ?  131 ILE   B CG1  1 
ATOM   5798 C  CG2  . ILE   B 1 131 ? 49.307 -31.298 4.888   1.00 20.42 ?  131 ILE   B CG2  1 
ATOM   5799 C  CD1  . ILE   B 1 131 ? 49.239 -28.330 5.666   1.00 21.28 ?  131 ILE   B CD1  1 
ATOM   5800 H  H    . ILE   B 1 131 ? 46.956 -31.053 3.575   1.00 19.97 ?  131 ILE   B H    1 
ATOM   5801 H  HA   . ILE   B 1 131 ? 47.009 -32.328 5.848   1.00 20.63 ?  131 ILE   B HA   1 
ATOM   5802 H  HB   . ILE   B 1 131 ? 48.426 -30.717 6.647   1.00 23.04 ?  131 ILE   B HB   1 
ATOM   5803 H  HG12 . ILE   B 1 131 ? 47.854 -29.114 4.392   1.00 24.10 ?  131 ILE   B HG12 1 
ATOM   5804 H  HG13 . ILE   B 1 131 ? 47.271 -28.811 5.835   1.00 24.10 ?  131 ILE   B HG13 1 
ATOM   5805 H  HG21 . ILE   B 1 131 ? 50.149 -30.895 5.144   1.00 24.50 ?  131 ILE   B HG21 1 
ATOM   5806 H  HG22 . ILE   B 1 131 ? 49.322 -32.248 5.066   1.00 24.50 ?  131 ILE   B HG22 1 
ATOM   5807 H  HG23 . ILE   B 1 131 ? 49.132 -31.138 3.947   1.00 24.50 ?  131 ILE   B HG23 1 
ATOM   5808 H  HD11 . ILE   B 1 131 ? 49.020 -27.398 5.504   1.00 25.53 ?  131 ILE   B HD11 1 
ATOM   5809 H  HD12 . ILE   B 1 131 ? 49.473 -28.456 6.599   1.00 25.53 ?  131 ILE   B HD12 1 
ATOM   5810 H  HD13 . ILE   B 1 131 ? 49.974 -28.601 5.099   1.00 25.53 ?  131 ILE   B HD13 1 
ATOM   5811 N  N    . PHE   B 1 132 ? 44.713 -30.264 5.732   1.00 15.65 ?  132 PHE   B N    1 
ATOM   5812 C  CA   . PHE   B 1 132 ? 43.560 -29.756 6.470   1.00 16.16 ?  132 PHE   B CA   1 
ATOM   5813 C  C    . PHE   B 1 132 ? 42.543 -30.847 6.807   1.00 17.58 ?  132 PHE   B C    1 
ATOM   5814 O  O    . PHE   B 1 132 ? 41.652 -30.600 7.623   1.00 19.49 ?  132 PHE   B O    1 
ATOM   5815 C  CB   . PHE   B 1 132 ? 42.874 -28.627 5.690   1.00 15.29 ?  132 PHE   B CB   1 
ATOM   5816 C  CG   . PHE   B 1 132 ? 43.573 -27.286 5.784   1.00 14.82 ?  132 PHE   B CG   1 
ATOM   5817 C  CD1  . PHE   B 1 132 ? 44.864 -27.108 5.309   1.00 16.22 ?  132 PHE   B CD1  1 
ATOM   5818 C  CD2  . PHE   B 1 132 ? 42.905 -26.185 6.307   1.00 14.56 ?  132 PHE   B CD2  1 
ATOM   5819 C  CE1  . PHE   B 1 132 ? 45.486 -25.868 5.391   1.00 16.59 ?  132 PHE   B CE1  1 
ATOM   5820 C  CE2  . PHE   B 1 132 ? 43.514 -24.941 6.381   1.00 15.10 ?  132 PHE   B CE2  1 
ATOM   5821 C  CZ   . PHE   B 1 132 ? 44.804 -24.784 5.925   1.00 15.94 ?  132 PHE   B CZ   1 
ATOM   5822 H  H    . PHE   B 1 132 ? 44.653 -30.158 4.878   1.00 18.77 ?  132 PHE   B H    1 
ATOM   5823 H  HA   . PHE   B 1 132 ? 43.875 -29.383 7.306   1.00 19.38 ?  132 PHE   B HA   1 
ATOM   5824 H  HB2  . PHE   B 1 132 ? 42.846 -28.875 4.754   1.00 18.34 ?  132 PHE   B HB2  1 
ATOM   5825 H  HB3  . PHE   B 1 132 ? 41.973 -28.516 6.030   1.00 18.34 ?  132 PHE   B HB3  1 
ATOM   5826 H  HD1  . PHE   B 1 132 ? 45.327 -27.836 4.955   1.00 19.46 ?  132 PHE   B HD1  1 
ATOM   5827 H  HD2  . PHE   B 1 132 ? 42.034 -26.288 6.619   1.00 17.46 ?  132 PHE   B HD2  1 
ATOM   5828 H  HE1  . PHE   B 1 132 ? 46.356 -25.764 5.080   1.00 19.90 ?  132 PHE   B HE1  1 
ATOM   5829 H  HE2  . PHE   B 1 132 ? 43.052 -24.218 6.747   1.00 18.11 ?  132 PHE   B HE2  1 
ATOM   5830 H  HZ   . PHE   B 1 132 ? 45.216 -23.951 5.980   1.00 19.13 ?  132 PHE   B HZ   1 
ATOM   5831 N  N    . GLY   B 1 133 ? 42.643 -32.037 6.198   1.00 17.09 ?  133 GLY   B N    1 
ATOM   5832 C  CA   . GLY   B 1 133 ? 41.946 -33.214 6.684   1.00 18.10 ?  133 GLY   B CA   1 
ATOM   5833 C  C    . GLY   B 1 133 ? 40.548 -33.476 6.157   1.00 18.86 ?  133 GLY   B C    1 
ATOM   5834 O  O    . GLY   B 1 133 ? 39.961 -34.496 6.531   1.00 21.15 ?  133 GLY   B O    1 
ATOM   5835 H  H    . GLY   B 1 133 ? 43.121 -32.177 5.494   1.00 20.50 ?  133 GLY   B H    1 
ATOM   5836 H  HA2  . GLY   B 1 133 ? 42.483 -33.992 6.471   1.00 21.71 ?  133 GLY   B HA2  1 
ATOM   5837 H  HA3  . GLY   B 1 133 ? 41.890 -33.152 7.649   1.00 21.71 ?  133 GLY   B HA3  1 
ATOM   5838 N  N    . ALA   B 1 134 ? 39.988 -32.615 5.316   1.00 17.87 ?  134 ALA   B N    1 
ATOM   5839 C  CA   . ALA   B 1 134 ? 38.664 -32.903 4.785   1.00 18.26 ?  134 ALA   B CA   1 
ATOM   5840 C  C    . ALA   B 1 134 ? 38.761 -33.874 3.613   1.00 18.13 ?  134 ALA   B C    1 
ATOM   5841 O  O    . ALA   B 1 134 ? 39.815 -34.045 2.996   1.00 18.80 ?  134 ALA   B O    1 
ATOM   5842 C  CB   . ALA   B 1 134 ? 37.963 -31.619 4.346   1.00 18.72 ?  134 ALA   B CB   1 
ATOM   5843 H  H    . ALA   B 1 134 ? 40.341 -31.875 5.049   1.00 21.44 ?  134 ALA   B H    1 
ATOM   5844 H  HA   . ALA   B 1 134 ? 38.128 -33.317 5.478   1.00 21.91 ?  134 ALA   B HA   1 
ATOM   5845 H  HB1  . ALA   B 1 134 ? 37.076 -31.844 4.020   1.00 22.46 ?  134 ALA   B HB1  1 
ATOM   5846 H  HB2  . ALA   B 1 134 ? 37.894 -31.021 5.106   1.00 22.46 ?  134 ALA   B HB2  1 
ATOM   5847 H  HB3  . ALA   B 1 134 ? 38.479 -31.202 3.640   1.00 22.46 ?  134 ALA   B HB3  1 
ATOM   5848 N  N    . ASP   B 1 135 ? 37.639 -34.512 3.314   1.00 18.38 ?  135 ASP   B N    1 
ATOM   5849 C  CA   . ASP   B 1 135 ? 37.552 -35.402 2.164   1.00 19.10 ?  135 ASP   B CA   1 
ATOM   5850 C  C    . ASP   B 1 135 ? 37.633 -34.561 0.896   1.00 17.77 ?  135 ASP   B C    1 
ATOM   5851 O  O    . ASP   B 1 135 ? 36.774 -33.689 0.688   1.00 17.91 ?  135 ASP   B O    1 
ATOM   5852 C  CB   . ASP   B 1 135 ? 36.219 -36.148 2.225   1.00 21.08 ?  135 ASP   B CB   1 
ATOM   5853 C  CG   . ASP   B 1 135 ? 36.042 -37.143 1.090   1.00 23.20 ?  135 ASP   B CG   1 
ATOM   5854 O  OD1  . ASP   B 1 135 ? 36.906 -37.194 0.189   1.00 22.45 ?  135 ASP   B OD1  1 
ATOM   5855 O  OD2  . ASP   B 1 135 ? 35.039 -37.891 1.111   1.00 26.53 -1 135 ASP   B OD2  1 
ATOM   5856 H  H    . ASP   B 1 135 ? 36.911 -34.445 3.763   1.00 22.05 ?  135 ASP   B H    1 
ATOM   5857 H  HA   . ASP   B 1 135 ? 38.280 -36.044 2.189   1.00 22.92 ?  135 ASP   B HA   1 
ATOM   5858 H  HB2  . ASP   B 1 135 ? 36.175 -36.633 3.063   1.00 25.29 ?  135 ASP   B HB2  1 
ATOM   5859 H  HB3  . ASP   B 1 135 ? 35.501 -35.501 2.175   1.00 25.29 ?  135 ASP   B HB3  1 
ATOM   5860 N  N    . PRO   B 1 136 ? 38.634 -34.764 0.034   1.00 18.16 ?  136 PRO   B N    1 
ATOM   5861 C  CA   . PRO   B 1 136 ? 38.715 -33.937 -1.182  1.00 17.24 ?  136 PRO   B CA   1 
ATOM   5862 C  C    . PRO   B 1 136 ? 37.515 -34.092 -2.098  1.00 16.41 ?  136 PRO   B C    1 
ATOM   5863 O  O    . PRO   B 1 136 ? 37.174 -33.146 -2.817  1.00 15.81 ?  136 PRO   B O    1 
ATOM   5864 C  CB   . PRO   B 1 136 ? 40.022 -34.403 -1.842  1.00 18.41 ?  136 PRO   B CB   1 
ATOM   5865 C  CG   . PRO   B 1 136 ? 40.232 -35.789 -1.311  1.00 19.61 ?  136 PRO   B CG   1 
ATOM   5866 C  CD   . PRO   B 1 136 ? 39.719 -35.755 0.098   1.00 19.04 ?  136 PRO   B CD   1 
ATOM   5867 H  HA   . PRO   B 1 136 ? 38.801 -33.000 -0.944  1.00 20.68 ?  136 PRO   B HA   1 
ATOM   5868 H  HB2  . PRO   B 1 136 ? 39.920 -34.413 -2.808  1.00 22.09 ?  136 PRO   B HB2  1 
ATOM   5869 H  HB3  . PRO   B 1 136 ? 40.749 -33.816 -1.580  1.00 22.09 ?  136 PRO   B HB3  1 
ATOM   5870 H  HG2  . PRO   B 1 136 ? 39.725 -36.427 -1.840  1.00 23.52 ?  136 PRO   B HG2  1 
ATOM   5871 H  HG3  . PRO   B 1 136 ? 41.176 -36.010 -1.323  1.00 23.52 ?  136 PRO   B HG3  1 
ATOM   5872 H  HD2  . PRO   B 1 136 ? 39.369 -36.621 0.355   1.00 22.84 ?  136 PRO   B HD2  1 
ATOM   5873 H  HD3  . PRO   B 1 136 ? 40.413 -35.454 0.707   1.00 22.84 ?  136 PRO   B HD3  1 
ATOM   5874 N  N    . ILE   B 1 137 ? 36.859 -35.256 -2.094  1.00 16.51 ?  137 ILE   B N    1 
ATOM   5875 C  CA   . ILE   B 1 137 ? 35.638 -35.424 -2.879  1.00 17.12 ?  137 ILE   B CA   1 
ATOM   5876 C  C    . ILE   B 1 137 ? 34.563 -34.462 -2.388  1.00 16.78 ?  137 ILE   B C    1 
ATOM   5877 O  O    . ILE   B 1 137 ? 33.836 -33.851 -3.181  1.00 16.42 ?  137 ILE   B O    1 
ATOM   5878 C  CB   . ILE   B 1 137 ? 35.169 -36.895 -2.824  1.00 19.25 ?  137 ILE   B CB   1 
ATOM   5879 C  CG1  . ILE   B 1 137 ? 36.156 -37.799 -3.568  1.00 21.91 ?  137 ILE   B CG1  1 
ATOM   5880 C  CG2  . ILE   B 1 137 ? 33.762 -37.040 -3.398  1.00 19.49 ?  137 ILE   B CG2  1 
ATOM   5881 C  CD1  . ILE   B 1 137 ? 35.831 -39.285 -3.468  1.00 24.39 ?  137 ILE   B CD1  1 
ATOM   5882 H  H    . ILE   B 1 137 ? 37.097 -35.955 -1.654  1.00 19.81 ?  137 ILE   B H    1 
ATOM   5883 H  HA   . ILE   B 1 137 ? 35.827 -35.212 -3.808  1.00 20.54 ?  137 ILE   B HA   1 
ATOM   5884 H  HB   . ILE   B 1 137 ? 35.146 -37.173 -1.900  1.00 23.09 ?  137 ILE   B HB   1 
ATOM   5885 H  HG12 . ILE   B 1 137 ? 36.157 -37.566 -4.509  1.00 26.29 ?  137 ILE   B HG12 1 
ATOM   5886 H  HG13 . ILE   B 1 137 ? 37.042 -37.672 -3.196  1.00 26.29 ?  137 ILE   B HG13 1 
ATOM   5887 H  HG21 . ILE   B 1 137 ? 33.499 -37.974 -3.388  1.00 23.39 ?  137 ILE   B HG21 1 
ATOM   5888 H  HG22 . ILE   B 1 137 ? 33.139 -36.536 -2.855  1.00 23.39 ?  137 ILE   B HG22 1 
ATOM   5889 H  HG23 . ILE   B 1 137 ? 33.755 -36.708 -4.308  1.00 23.39 ?  137 ILE   B HG23 1 
ATOM   5890 H  HD11 . ILE   B 1 137 ? 36.427 -39.765 -4.060  1.00 29.26 ?  137 ILE   B HD11 1 
ATOM   5891 H  HD12 . ILE   B 1 137 ? 35.959 -39.580 -2.552  1.00 29.26 ?  137 ILE   B HD12 1 
ATOM   5892 H  HD13 . ILE   B 1 137 ? 34.915 -39.446 -3.742  1.00 29.26 ?  137 ILE   B HD13 1 
ATOM   5893 N  N    . HIS   B 1 138 ? 34.443 -34.315 -1.071  1.00 16.96 ?  138 HIS   B N    1 
ATOM   5894 C  CA   . HIS   B 1 138 ? 33.495 -33.352 -0.525  1.00 17.17 ?  138 HIS   B CA   1 
ATOM   5895 C  C    . HIS   B 1 138 ? 33.905 -31.922 -0.854  1.00 16.05 ?  138 HIS   B C    1 
ATOM   5896 O  O    . HIS   B 1 138 ? 33.054 -31.082 -1.171  1.00 16.44 ?  138 HIS   B O    1 
ATOM   5897 C  CB   . HIS   B 1 138 ? 33.392 -33.533 0.983   1.00 18.80 ?  138 HIS   B CB   1 
ATOM   5898 C  CG   . HIS   B 1 138 ? 32.471 -32.555 1.633   1.00 20.08 ?  138 HIS   B CG   1 
ATOM   5899 N  ND1  . HIS   B 1 138 ? 31.128 -32.488 1.330   1.00 21.89 ?  138 HIS   B ND1  1 
ATOM   5900 C  CD2  . HIS   B 1 138 ? 32.700 -31.580 2.543   1.00 20.70 ?  138 HIS   B CD2  1 
ATOM   5901 C  CE1  . HIS   B 1 138 ? 30.566 -31.525 2.038   1.00 22.03 ?  138 HIS   B CE1  1 
ATOM   5902 N  NE2  . HIS   B 1 138 ? 31.499 -30.959 2.784   1.00 21.38 ?  138 HIS   B NE2  1 
ATOM   5903 H  H    . HIS   B 1 138 ? 34.896 -34.756 -0.488  1.00 20.35 ?  138 HIS   B H    1 
ATOM   5904 H  HA   . HIS   B 1 138 ? 32.623 -33.518 -0.914  1.00 20.60 ?  138 HIS   B HA   1 
ATOM   5905 H  HB2  . HIS   B 1 138 ? 33.057 -34.426 1.168   1.00 22.55 ?  138 HIS   B HB2  1 
ATOM   5906 H  HB3  . HIS   B 1 138 ? 34.271 -33.423 1.373   1.00 22.55 ?  138 HIS   B HB3  1 
ATOM   5907 H  HD1  . HIS   B 1 138 ? 30.719 -33.003 0.768   1.00 26.26 ?  138 HIS   B HD1  1 
ATOM   5908 H  HD2  . HIS   B 1 138 ? 33.512 -31.377 2.941   1.00 24.83 ?  138 HIS   B HD2  1 
ATOM   5909 H  HE1  . HIS   B 1 138 ? 29.664 -31.295 2.017   1.00 26.43 ?  138 HIS   B HE1  1 
ATOM   5910 N  N    . SER   B 1 139 ? 35.201 -31.621 -0.781  1.00 15.46 ?  139 SER   B N    1 
ATOM   5911 C  CA   . SER   B 1 139 ? 35.641 -30.272 -1.104  1.00 14.93 ?  139 SER   B CA   1 
ATOM   5912 C  C    . SER   B 1 139 ? 35.295 -29.916 -2.542  1.00 14.07 ?  139 SER   B C    1 
ATOM   5913 O  O    . SER   B 1 139 ? 34.846 -28.797 -2.816  1.00 14.26 ?  139 SER   B O    1 
ATOM   5914 C  CB   . SER   B 1 139 ? 37.137 -30.130 -0.846  1.00 15.08 ?  139 SER   B CB   1 
ATOM   5915 O  OG   . SER   B 1 139 ? 37.538 -28.798 -1.113  1.00 15.13 ?  139 SER   B OG   1 
ATOM   5916 H  H    . SER   B 1 139 ? 35.826 -32.165 -0.558  1.00 18.55 ?  139 SER   B H    1 
ATOM   5917 H  HA   . SER   B 1 139 ? 35.175 -29.647 -0.530  1.00 17.91 ?  139 SER   B HA   1 
ATOM   5918 H  HB2  . SER   B 1 139 ? 37.321 -30.343 0.083   1.00 18.09 ?  139 SER   B HB2  1 
ATOM   5919 H  HB3  . SER   B 1 139 ? 37.623 -30.732 -1.430  1.00 18.09 ?  139 SER   B HB3  1 
ATOM   5920 H  HG   . SER   B 1 139 ? 38.362 -28.710 -0.965  1.00 18.15 ?  139 SER   B HG   1 
ATOM   5921 N  N    . LEU   B 1 140 ? 35.476 -30.859 -3.470  1.00 13.93 ?  140 LEU   B N    1 
ATOM   5922 C  CA   . LEU   B 1 140 ? 35.102 -30.608 -4.857  1.00 13.76 ?  140 LEU   B CA   1 
ATOM   5923 C  C    . LEU   B 1 140 ? 33.598 -30.385 -4.984  1.00 13.80 ?  140 LEU   B C    1 
ATOM   5924 O  O    . LEU   B 1 140 ? 33.159 -29.501 -5.725  1.00 14.11 ?  140 LEU   B O    1 
ATOM   5925 C  CB   . LEU   B 1 140 ? 35.579 -31.765 -5.742  1.00 13.92 ?  140 LEU   B CB   1 
ATOM   5926 C  CG   . LEU   B 1 140 ? 35.204 -31.655 -7.213  1.00 14.19 ?  140 LEU   B CG   1 
ATOM   5927 C  CD1  . LEU   B 1 140 ? 35.750 -30.371 -7.812  1.00 15.29 ?  140 LEU   B CD1  1 
ATOM   5928 C  CD2  . LEU   B 1 140 ? 35.690 -32.876 -7.975  1.00 15.28 ?  140 LEU   B CD2  1 
ATOM   5929 H  H    . LEU   B 1 140 ? 35.802 -31.640 -3.326  1.00 16.72 ?  140 LEU   B H    1 
ATOM   5930 H  HA   . LEU   B 1 140 ? 35.551 -29.803 -5.161  1.00 16.51 ?  140 LEU   B HA   1 
ATOM   5931 H  HB2  . LEU   B 1 140 ? 36.549 -31.817 -5.694  1.00 16.69 ?  140 LEU   B HB2  1 
ATOM   5932 H  HB3  . LEU   B 1 140 ? 35.196 -32.592 -5.410  1.00 16.69 ?  140 LEU   B HB3  1 
ATOM   5933 H  HG   . LEU   B 1 140 ? 34.239 -31.621 -7.286  1.00 17.02 ?  140 LEU   B HG   1 
ATOM   5934 H  HD11 . LEU   B 1 140 ? 35.623 -30.395 -8.772  1.00 18.34 ?  140 LEU   B HD11 1 
ATOM   5935 H  HD12 . LEU   B 1 140 ? 35.270 -29.614 -7.435  1.00 18.34 ?  140 LEU   B HD12 1 
ATOM   5936 H  HD13 . LEU   B 1 140 ? 36.694 -30.300 -7.604  1.00 18.34 ?  140 LEU   B HD13 1 
ATOM   5937 H  HD21 . LEU   B 1 140 ? 35.437 -32.780 -8.906  1.00 18.33 ?  140 LEU   B HD21 1 
ATOM   5938 H  HD22 . LEU   B 1 140 ? 36.651 -32.936 -7.892  1.00 18.33 ?  140 LEU   B HD22 1 
ATOM   5939 H  HD23 . LEU   B 1 140 ? 35.269 -33.662 -7.595  1.00 18.33 ?  140 LEU   B HD23 1 
ATOM   5940 N  N    . ARG   B 1 141 ? 32.800 -31.174 -4.257  1.00 14.03 ?  141 ARG   B N    1 
ATOM   5941 C  CA   . ARG   B 1 141 ? 31.352 -30.997 -4.232  1.00 15.39 ?  141 ARG   B CA   1 
ATOM   5942 C  C    . ARG   B 1 141 ? 30.977 -29.584 -3.803  1.00 14.97 ?  141 ARG   B C    1 
ATOM   5943 O  O    . ARG   B 1 141 ? 30.171 -28.910 -4.460  1.00 14.87 ?  141 ARG   B O    1 
ATOM   5944 C  CB   . ARG   B 1 141 ? 30.773 -32.018 -3.249  1.00 16.78 ?  141 ARG   B CB   1 
ATOM   5945 C  CG   . ARG   B 1 141 ? 29.298 -31.903 -2.952  1.00 18.80 ?  141 ARG   B CG   1 
ATOM   5946 C  CD   . ARG   B 1 141 ? 28.516 -32.554 -4.025  1.00 20.58 ?  141 ARG   B CD   1 
ATOM   5947 N  NE   . ARG   B 1 141 ? 28.226 -31.646 -5.122  1.00 20.58 ?  141 ARG   B NE   1 
ATOM   5948 C  CZ   . ARG   B 1 141 ? 28.233 -31.985 -6.404  1.00 20.00 ?  141 ARG   B CZ   1 
ATOM   5949 N  NH1  . ARG   B 1 141 ? 28.703 -33.155 -6.810  1.00 19.86 ?  141 ARG   B NH1  1 
ATOM   5950 N  NH2  . ARG   B 1 141 ? 27.750 -31.128 -7.301  1.00 20.99 ?  141 ARG   B NH2  1 
ATOM   5951 H  H    . ARG   B 1 141 ? 33.086 -31.814 -3.760  1.00 16.83 ?  141 ARG   B H    1 
ATOM   5952 H  HA   . ARG   B 1 141 ? 30.989 -31.161 -5.111  1.00 18.46 ?  141 ARG   B HA   1 
ATOM   5953 H  HB2  . ARG   B 1 141 ? 30.941 -32.905 -3.600  1.00 20.14 ?  141 ARG   B HB2  1 
ATOM   5954 H  HB3  . ARG   B 1 141 ? 31.241 -31.922 -2.404  1.00 20.14 ?  141 ARG   B HB3  1 
ATOM   5955 H  HG2  . ARG   B 1 141 ? 29.110 -32.343 -2.113  1.00 22.56 ?  141 ARG   B HG2  1 
ATOM   5956 H  HG3  . ARG   B 1 141 ? 29.039 -30.964 -2.902  1.00 22.56 ?  141 ARG   B HG3  1 
ATOM   5957 H  HD2  . ARG   B 1 141 ? 29.020 -33.312 -4.368  1.00 24.69 ?  141 ARG   B HD2  1 
ATOM   5958 H  HD3  . ARG   B 1 141 ? 27.679 -32.863 -3.656  1.00 24.69 ?  141 ARG   B HD3  1 
ATOM   5959 H  HE   . ARG   B 1 141 ? 28.015 -30.834 -4.923  1.00 24.69 ?  141 ARG   B HE   1 
ATOM   5960 H  HH11 . ARG   B 1 141 ? 29.010 -33.722 -6.243  1.00 23.83 ?  141 ARG   B HH11 1 
ATOM   5961 H  HH12 . ARG   B 1 141 ? 28.706 -33.345 -7.646  1.00 23.83 ?  141 ARG   B HH12 1 
ATOM   5962 H  HH21 . ARG   B 1 141 ? 27.448 -30.363 -7.049  1.00 25.18 ?  141 ARG   B HH21 1 
ATOM   5963 H  HH22 . ARG   B 1 141 ? 27.767 -31.327 -8.138  1.00 25.18 ?  141 ARG   B HH22 1 
ATOM   5964 N  N    . VAL   B 1 142 ? 31.523 -29.137 -2.673  1.00 14.80 ?  142 VAL   B N    1 
ATOM   5965 C  CA   . VAL   B 1 142 ? 31.202 -27.801 -2.187  1.00 14.38 ?  142 VAL   B CA   1 
ATOM   5966 C  C    . VAL   B 1 142 ? 31.673 -26.745 -3.180  1.00 14.12 ?  142 VAL   B C    1 
ATOM   5967 O  O    . VAL   B 1 142 ? 30.969 -25.760 -3.437  1.00 14.53 ?  142 VAL   B O    1 
ATOM   5968 C  CB   . VAL   B 1 142 ? 31.759 -27.577 -0.767  1.00 14.94 ?  142 VAL   B CB   1 
ATOM   5969 C  CG1  . VAL   B 1 142 ? 31.433 -26.154 -0.290  1.00 14.81 ?  142 VAL   B CG1  1 
ATOM   5970 C  CG2  . VAL   B 1 142 ? 31.192 -28.608 0.196   1.00 15.83 ?  142 VAL   B CG2  1 
ATOM   5971 H  H    . VAL   B 1 142 ? 32.078 -29.577 -2.181  1.00 17.76 ?  142 VAL   B H    1 
ATOM   5972 H  HA   . VAL   B 1 142 ? 30.244 -27.726 -2.123  1.00 17.25 ?  142 VAL   B HA   1 
ATOM   5973 H  HB   . VAL   B 1 142 ? 32.727 -27.678 -0.779  1.00 17.93 ?  142 VAL   B HB   1 
ATOM   5974 H  HG11 . VAL   B 1 142 ? 31.624 -26.089 0.658   1.00 17.77 ?  142 VAL   B HG11 1 
ATOM   5975 H  HG12 . VAL   B 1 142 ? 31.985 -25.523 -0.780  1.00 17.77 ?  142 VAL   B HG12 1 
ATOM   5976 H  HG13 . VAL   B 1 142 ? 30.497 -25.976 -0.454  1.00 17.77 ?  142 VAL   B HG13 1 
ATOM   5977 H  HG21 . VAL   B 1 142 ? 31.515 -28.417 1.090   1.00 18.99 ?  142 VAL   B HG21 1 
ATOM   5978 H  HG22 . VAL   B 1 142 ? 30.226 -28.560 0.173   1.00 18.99 ?  142 VAL   B HG22 1 
ATOM   5979 H  HG23 . VAL   B 1 142 ? 31.487 -29.492 -0.079  1.00 18.99 ?  142 VAL   B HG23 1 
ATOM   5980 N  N    . CYS   B 1 143 ? 32.844 -26.948 -3.784  1.00 13.46 ?  143 CYS   B N    1 
ATOM   5981 C  CA   . CYS   B 1 143 ? 33.334 -26.007 -4.788  1.00 13.54 ?  143 CYS   B CA   1 
ATOM   5982 C  C    . CYS   B 1 143 ? 32.330 -25.860 -5.928  1.00 13.22 ?  143 CYS   B C    1 
ATOM   5983 O  O    . CYS   B 1 143 ? 31.926 -24.748 -6.284  1.00 13.71 ?  143 CYS   B O    1 
ATOM   5984 C  CB   . CYS   B 1 143 ? 34.688 -26.487 -5.320  1.00 13.80 ?  143 CYS   B CB   1 
ATOM   5985 S  SG   . CYS   B 1 143 ? 35.437 -25.390 -6.544  1.00 14.14 ?  143 CYS   B SG   1 
ATOM   5986 H  H    . CYS   B 1 143 ? 33.371 -27.611 -3.626  1.00 16.15 ?  143 CYS   B H    1 
ATOM   5987 H  HA   . CYS   B 1 143 ? 33.461 -25.138 -4.379  1.00 16.24 ?  143 CYS   B HA   1 
ATOM   5988 H  HB2  . CYS   B 1 143 ? 35.313 -26.565 -4.579  1.00 16.55 ?  143 CYS   B HB2  1 
ATOM   5989 H  HB3  . CYS   B 1 143 ? 34.574 -27.354 -5.734  1.00 16.55 ?  143 CYS   B HB3  1 
ATOM   5990 H  HG   . CYS   B 1 143 ? 36.510 -25.819 -6.870  1.00 16.97 ?  143 CYS   B HG   1 
ATOM   5991 N  N    . VAL   B 1 144 ? 31.921 -26.979 -6.518  1.00 13.89 ?  144 VAL   B N    1 
ATOM   5992 C  CA   . VAL   B 1 144 ? 31.012 -26.919 -7.658  1.00 14.83 ?  144 VAL   B CA   1 
ATOM   5993 C  C    . VAL   B 1 144 ? 29.673 -26.304 -7.278  1.00 15.05 ?  144 VAL   B C    1 
ATOM   5994 O  O    . VAL   B 1 144 ? 29.050 -25.601 -8.086  1.00 16.37 ?  144 VAL   B O    1 
ATOM   5995 C  CB   . VAL   B 1 144 ? 30.857 -28.336 -8.223  1.00 17.40 ?  144 VAL   B CB   1 
ATOM   5996 C  CG1  . VAL   B 1 144 ? 29.576 -28.482 -9.045  1.00 20.44 ?  144 VAL   B CG1  1 
ATOM   5997 C  CG2  . VAL   B 1 144 ? 32.096 -28.736 -9.014  1.00 17.74 ?  144 VAL   B CG2  1 
ATOM   5998 H  H    . VAL   B 1 144 ? 32.155 -27.774 -6.285  1.00 16.66 ?  144 VAL   B H    1 
ATOM   5999 H  HA   . VAL   B 1 144 ? 31.406 -26.368 -8.349  1.00 17.80 ?  144 VAL   B HA   1 
ATOM   6000 H  HB   . VAL   B 1 144 ? 30.790 -28.957 -7.479  1.00 20.87 ?  144 VAL   B HB   1 
ATOM   6001 H  HG11 . VAL   B 1 144 ? 29.653 -29.278 -9.601  1.00 24.52 ?  144 VAL   B HG11 1 
ATOM   6002 H  HG12 . VAL   B 1 144 ? 28.824 -28.579 -8.443  1.00 24.52 ?  144 VAL   B HG12 1 
ATOM   6003 H  HG13 . VAL   B 1 144 ? 29.469 -27.702 -9.604  1.00 24.52 ?  144 VAL   B HG13 1 
ATOM   6004 H  HG21 . VAL   B 1 144 ? 31.981 -29.636 -9.357  1.00 21.28 ?  144 VAL   B HG21 1 
ATOM   6005 H  HG22 . VAL   B 1 144 ? 32.213 -28.115 -9.752  1.00 21.28 ?  144 VAL   B HG22 1 
ATOM   6006 H  HG23 . VAL   B 1 144 ? 32.870 -28.702 -8.430  1.00 21.28 ?  144 VAL   B HG23 1 
ATOM   6007 N  N    . ASP   B 1 145 ? 29.210 -26.551 -6.057  1.00 15.06 ?  145 ASP   B N    1 
ATOM   6008 C  CA   . ASP   B 1 145 ? 27.905 -26.083 -5.618  1.00 15.81 ?  145 ASP   B CA   1 
ATOM   6009 C  C    . ASP   B 1 145 ? 27.934 -24.659 -5.078  1.00 15.06 ?  145 ASP   B C    1 
ATOM   6010 O  O    . ASP   B 1 145 ? 26.873 -24.116 -4.746  1.00 16.79 ?  145 ASP   B O    1 
ATOM   6011 C  CB   . ASP   B 1 145 ? 27.342 -27.004 -4.528  1.00 17.88 ?  145 ASP   B CB   1 
ATOM   6012 C  CG   . ASP   B 1 145 ? 26.951 -28.371 -5.044  1.00 19.83 ?  145 ASP   B CG   1 
ATOM   6013 O  OD1  . ASP   B 1 145 ? 26.842 -28.565 -6.273  1.00 20.25 ?  145 ASP   B OD1  1 
ATOM   6014 O  OD2  . ASP   B 1 145 ? 26.750 -29.258 -4.194  1.00 21.92 -1 145 ASP   B OD2  1 
ATOM   6015 H  H    . ASP   B 1 145 ? 29.652 -26.975 -5.455  1.00 18.07 ?  145 ASP   B H    1 
ATOM   6016 H  HA   . ASP   B 1 145 ? 27.301 -26.089 -6.370  1.00 18.97 ?  145 ASP   B HA   1 
ATOM   6017 H  HB2  . ASP   B 1 145 ? 28.013 -27.130 -3.844  1.00 21.45 ?  145 ASP   B HB2  1 
ATOM   6018 H  HB3  . ASP   B 1 145 ? 26.550 -26.591 -4.152  1.00 21.45 ?  145 ASP   B HB3  1 
ATOM   6019 N  N    . THR   B 1 146 ? 29.114 -24.046 -4.975  1.00 13.61 ?  146 THR   B N    1 
ATOM   6020 C  CA   . THR   B 1 146 ? 29.249 -22.726 -4.369  1.00 13.33 ?  146 THR   B CA   1 
ATOM   6021 C  C    . THR   B 1 146 ? 29.872 -21.696 -5.293  1.00 13.09 ?  146 THR   B C    1 
ATOM   6022 O  O    . THR   B 1 146 ? 29.413 -20.539 -5.335  1.00 13.32 ?  146 THR   B O    1 
ATOM   6023 C  CB   . THR   B 1 146 ? 30.084 -22.831 -3.086  1.00 13.88 ?  146 THR   B CB   1 
ATOM   6024 O  OG1  . THR   B 1 146 ? 29.514 -23.818 -2.214  1.00 14.08 ?  146 THR   B OG1  1 
ATOM   6025 C  CG2  . THR   B 1 146 ? 30.170 -21.489 -2.377  1.00 14.01 ?  146 THR   B CG2  1 
ATOM   6026 H  H    . THR   B 1 146 ? 29.864 -24.373 -5.255  1.00 16.33 ?  146 THR   B H    1 
ATOM   6027 H  HA   . THR   B 1 146 ? 28.375 -22.400 -4.122  1.00 15.99 ?  146 THR   B HA   1 
ATOM   6028 H  HB   . THR   B 1 146 ? 30.991 -23.093 -3.317  1.00 16.66 ?  146 THR   B HB   1 
ATOM   6029 H  HG1  . THR   B 1 146 ? 29.544 -24.575 -2.590  1.00 16.89 ?  146 THR   B HG1  1 
ATOM   6030 H  HG21 . THR   B 1 146 ? 30.512 -21.609 -1.478  1.00 16.81 ?  146 THR   B HG21 1 
ATOM   6031 H  HG22 . THR   B 1 146 ? 30.768 -20.892 -2.860  1.00 16.81 ?  146 THR   B HG22 1 
ATOM   6032 H  HG23 . THR   B 1 146 ? 29.292 -21.083 -2.329  1.00 16.81 ?  146 THR   B HG23 1 
ATOM   6033 N  N    . VAL   B 1 147 ? 30.932 -22.067 -6.002  1.00 13.14 ?  147 VAL   B N    1 
ATOM   6034 C  CA   . VAL   B 1 147 ? 31.658 -21.124 -6.841  1.00 13.10 ?  147 VAL   B CA   1 
ATOM   6035 C  C    . VAL   B 1 147 ? 30.919 -20.984 -8.160  1.00 13.21 ?  147 VAL   B C    1 
ATOM   6036 O  O    . VAL   B 1 147 ? 30.542 -21.984 -8.787  1.00 14.03 ?  147 VAL   B O    1 
ATOM   6037 C  CB   . VAL   B 1 147 ? 33.109 -21.585 -7.055  1.00 13.09 ?  147 VAL   B CB   1 
ATOM   6038 C  CG1  . VAL   B 1 147 ? 33.871 -20.559 -7.871  1.00 13.27 ?  147 VAL   B CG1  1 
ATOM   6039 C  CG2  . VAL   B 1 147 ? 33.794 -21.794 -5.717  1.00 13.45 ?  147 VAL   B CG2  1 
ATOM   6040 H  H    . VAL   B 1 147 ? 31.253 -22.872 -6.020  1.00 15.76 ?  147 VAL   B H    1 
ATOM   6041 H  HA   . VAL   B 1 147 ? 31.679 -20.260 -6.406  1.00 15.72 ?  147 VAL   B HA   1 
ATOM   6042 H  HB   . VAL   B 1 147 ? 33.116 -22.428 -7.542  1.00 15.70 ?  147 VAL   B HB   1 
ATOM   6043 H  HG11 . VAL   B 1 147 ? 34.813 -20.786 -7.872  1.00 15.91 ?  147 VAL   B HG11 1 
ATOM   6044 H  HG12 . VAL   B 1 147 ? 33.532 -20.551 -8.780  1.00 15.91 ?  147 VAL   B HG12 1 
ATOM   6045 H  HG13 . VAL   B 1 147 ? 33.747 -19.681 -7.467  1.00 15.91 ?  147 VAL   B HG13 1 
ATOM   6046 H  HG21 . VAL   B 1 147 ? 34.731 -21.989 -5.869  1.00 16.14 ?  147 VAL   B HG21 1 
ATOM   6047 H  HG22 . VAL   B 1 147 ? 33.703 -20.986 -5.190  1.00 16.14 ?  147 VAL   B HG22 1 
ATOM   6048 H  HG23 . VAL   B 1 147 ? 33.371 -22.538 -5.259  1.00 16.14 ?  147 VAL   B HG23 1 
ATOM   6049 N  N    . ARG   B 1 148 ? 30.712 -19.734 -8.579  1.00 13.06 ?  148 ARG   B N    1 
ATOM   6050 C  CA   . ARG   B 1 148 ? 30.084 -19.415 -9.850  1.00 13.37 ?  148 ARG   B CA   1 
ATOM   6051 C  C    . ARG   B 1 148 ? 31.031 -18.726 -10.823 1.00 13.15 ?  148 ARG   B C    1 
ATOM   6052 O  O    . ARG   B 1 148 ? 30.733 -18.683 -12.019 1.00 14.45 ?  148 ARG   B O    1 
ATOM   6053 C  CB   . ARG   B 1 148 ? 28.839 -18.543 -9.620  1.00 13.98 ?  148 ARG   B CB   1 
ATOM   6054 C  CG   . ARG   B 1 148 ? 27.774 -19.259 -8.792  1.00 14.59 ?  148 ARG   B CG   1 
ATOM   6055 C  CD   . ARG   B 1 148 ? 26.557 -18.378 -8.494  1.00 15.49 ?  148 ARG   B CD   1 
ATOM   6056 N  NE   . ARG   B 1 148 ? 26.923 -17.175 -7.757  1.00 15.28 ?  148 ARG   B NE   1 
ATOM   6057 C  CZ   . ARG   B 1 148 ? 27.238 -17.145 -6.469  1.00 14.24 ?  148 ARG   B CZ   1 
ATOM   6058 N  NH1  . ARG   B 1 148 ? 27.193 -18.236 -5.718  1.00 14.02 ?  148 ARG   B NH1  1 
ATOM   6059 N  NH2  . ARG   B 1 148 ? 27.619 -15.993 -5.922  1.00 14.59 ?  148 ARG   B NH2  1 
ATOM   6060 H  H    . ARG   B 1 148 ? 30.945 -19.036 -8.124  1.00 15.67 ?  148 ARG   B H    1 
ATOM   6061 H  HA   . ARG   B 1 148 ? 29.793 -20.242 -10.260 1.00 16.04 ?  148 ARG   B HA   1 
ATOM   6062 H  HB2  . ARG   B 1 148 ? 29.100 -17.740 -9.142  1.00 16.77 ?  148 ARG   B HB2  1 
ATOM   6063 H  HB3  . ARG   B 1 148 ? 28.454 -18.315 -10.476 1.00 16.77 ?  148 ARG   B HB3  1 
ATOM   6064 H  HG2  . ARG   B 1 148 ? 27.465 -20.038 -9.282  1.00 17.50 ?  148 ARG   B HG2  1 
ATOM   6065 H  HG3  . ARG   B 1 148 ? 28.159 -19.532 -7.945  1.00 17.50 ?  148 ARG   B HG3  1 
ATOM   6066 H  HD2  . ARG   B 1 148 ? 26.149 -18.106 -9.330  1.00 18.59 ?  148 ARG   B HD2  1 
ATOM   6067 H  HD3  . ARG   B 1 148 ? 25.923 -18.879 -7.959  1.00 18.59 ?  148 ARG   B HD3  1 
ATOM   6068 H  HE   . ARG   B 1 148 ? 26.949 -16.433 -8.189  1.00 18.33 ?  148 ARG   B HE   1 
ATOM   6069 H  HH11 . ARG   B 1 148 ? 26.947 -18.988 -6.057  1.00 16.82 ?  148 ARG   B HH11 1 
ATOM   6070 H  HH12 . ARG   B 1 148 ? 27.398 -18.194 -4.881  1.00 16.82 ?  148 ARG   B HH12 1 
ATOM   6071 H  HH21 . ARG   B 1 148 ? 27.662 -15.283 -6.401  1.00 17.50 ?  148 ARG   B HH21 1 
ATOM   6072 H  HH22 . ARG   B 1 148 ? 27.829 -15.962 -5.087  1.00 17.50 ?  148 ARG   B HH22 1 
ATOM   6073 N  N    . THR   B 1 149 ? 32.138 -18.170 -10.336 1.00 13.05 ?  149 THR   B N    1 
ATOM   6074 C  CA   . THR   B 1 149 ? 33.178 -17.610 -11.185 1.00 13.26 ?  149 THR   B CA   1 
ATOM   6075 C  C    . THR   B 1 149 ? 34.060 -18.746 -11.705 1.00 13.10 ?  149 THR   B C    1 
ATOM   6076 O  O    . THR   B 1 149 ? 33.860 -19.917 -11.376 1.00 13.50 ?  149 THR   B O    1 
ATOM   6077 C  CB   . THR   B 1 149 ? 33.957 -16.568 -10.398 1.00 13.38 ?  149 THR   B CB   1 
ATOM   6078 O  OG1  . THR   B 1 149 ? 34.419 -17.173 -9.191  1.00 13.01 ?  149 THR   B OG1  1 
ATOM   6079 C  CG2  . THR   B 1 149 ? 33.072 -15.365 -10.080 1.00 14.25 ?  149 THR   B CG2  1 
ATOM   6080 H  H    . THR   B 1 149 ? 32.306 -18.096 -9.496  1.00 15.66 ?  149 THR   B H    1 
ATOM   6081 H  HA   . THR   B 1 149 ? 32.768 -17.169 -11.946 1.00 15.90 ?  149 THR   B HA   1 
ATOM   6082 H  HB   . THR   B 1 149 ? 34.717 -16.269 -10.916 1.00 16.05 ?  149 THR   B HB   1 
ATOM   6083 H  HG1  . THR   B 1 149 ? 34.841 -16.607 -8.727  1.00 15.60 ?  149 THR   B HG1  1 
ATOM   6084 H  HG21 . THR   B 1 149 ? 33.584 -14.695 -9.595  1.00 17.10 ?  149 THR   B HG21 1 
ATOM   6085 H  HG22 . THR   B 1 149 ? 32.745 -14.967 -10.904 1.00 17.10 ?  149 THR   B HG22 1 
ATOM   6086 H  HG23 . THR   B 1 149 ? 32.316 -15.635 -9.539  1.00 17.10 ?  149 THR   B HG23 1 
ATOM   6087 N  N    . ASN   B 1 150 ? 35.026 -18.422 -12.556 1.00 12.96 ?  150 ASN   B N    1 
ATOM   6088 C  CA   . ASN   B 1 150 ? 35.788 -19.445 -13.264 1.00 13.60 ?  150 ASN   B CA   1 
ATOM   6089 C  C    . ASN   B 1 150 ? 36.957 -19.898 -12.400 1.00 12.91 ?  150 ASN   B C    1 
ATOM   6090 O  O    . ASN   B 1 150 ? 37.894 -19.131 -12.155 1.00 13.69 ?  150 ASN   B O    1 
ATOM   6091 C  CB   . ASN   B 1 150 ? 36.252 -18.916 -14.614 1.00 15.23 ?  150 ASN   B CB   1 
ATOM   6092 C  CG   . ASN   B 1 150 ? 35.101 -18.684 -15.554 1.00 18.18 ?  150 ASN   B CG   1 
ATOM   6093 O  OD1  . ASN   B 1 150 ? 34.188 -19.498 -15.622 1.00 19.74 ?  150 ASN   B OD1  1 
ATOM   6094 N  ND2  . ASN   B 1 150 ? 35.114 -17.562 -16.256 1.00 20.31 ?  150 ASN   B ND2  1 
ATOM   6095 H  H    . ASN   B 1 150 ? 35.260 -17.613 -12.743 1.00 15.55 ?  150 ASN   B H    1 
ATOM   6096 H  HA   . ASN   B 1 150 ? 35.209 -20.212 -13.428 1.00 16.32 ?  150 ASN   B HA   1 
ATOM   6097 H  HB2  . ASN   B 1 150 ? 36.709 -18.070 -14.484 1.00 18.27 ?  150 ASN   B HB2  1 
ATOM   6098 H  HB3  . ASN   B 1 150 ? 36.849 -19.560 -15.022 1.00 18.27 ?  150 ASN   B HB3  1 
ATOM   6099 H  HD21 . ASN   B 1 150 ? 34.476 -17.387 -16.807 1.00 24.36 ?  150 ASN   B HD21 1 
ATOM   6100 H  HD22 . ASN   B 1 150 ? 35.770 -17.009 -16.174 1.00 24.36 ?  150 ASN   B HD22 1 
ATOM   6101 N  N    . VAL   B 1 151 ? 36.909 -21.143 -11.942 1.00 12.61 ?  151 VAL   B N    1 
ATOM   6102 C  CA   . VAL   B 1 151 ? 37.933 -21.676 -11.058 1.00 12.82 ?  151 VAL   B CA   1 
ATOM   6103 C  C    . VAL   B 1 151 ? 38.630 -22.849 -11.736 1.00 12.60 ?  151 VAL   B C    1 
ATOM   6104 O  O    . VAL   B 1 151 ? 37.982 -23.782 -12.237 1.00 13.55 ?  151 VAL   B O    1 
ATOM   6105 C  CB   . VAL   B 1 151 ? 37.381 -22.016 -9.660  1.00 13.83 ?  151 VAL   B CB   1 
ATOM   6106 C  CG1  . VAL   B 1 151 ? 36.206 -23.000 -9.734  1.00 15.26 ?  151 VAL   B CG1  1 
ATOM   6107 C  CG2  . VAL   B 1 151 ? 38.496 -22.532 -8.763  1.00 14.39 ?  151 VAL   B CG2  1 
ATOM   6108 H  H    . VAL   B 1 151 ? 36.282 -21.705 -12.139 1.00 15.13 ?  151 VAL   B H    1 
ATOM   6109 H  HA   . VAL   B 1 151 ? 38.601 -20.982 -10.934 1.00 15.38 ?  151 VAL   B HA   1 
ATOM   6110 H  HB   . VAL   B 1 151 ? 37.048 -21.196 -9.260  1.00 16.59 ?  151 VAL   B HB   1 
ATOM   6111 H  HG11 . VAL   B 1 151 ? 35.898 -23.193 -8.833  1.00 18.30 ?  151 VAL   B HG11 1 
ATOM   6112 H  HG12 . VAL   B 1 151 ? 35.484 -22.595 -10.246 1.00 18.30 ?  151 VAL   B HG12 1 
ATOM   6113 H  HG13 . VAL   B 1 151 ? 36.498 -23.815 -10.166 1.00 18.30 ?  151 VAL   B HG13 1 
ATOM   6114 H  HG21 . VAL   B 1 151 ? 38.163 -22.597 -7.855  1.00 17.26 ?  151 VAL   B HG21 1 
ATOM   6115 H  HG22 . VAL   B 1 151 ? 38.777 -23.405 -9.076  1.00 17.26 ?  151 VAL   B HG22 1 
ATOM   6116 H  HG23 . VAL   B 1 151 ? 39.243 -21.911 -8.796  1.00 17.26 ?  151 VAL   B HG23 1 
ATOM   6117 N  N    . TYR   B 1 152 ? 39.960 -22.766 -11.759 1.00 12.19 ?  152 TYR   B N    1 
ATOM   6118 C  CA   . TYR   B 1 152 ? 40.855 -23.749 -12.347 1.00 12.13 ?  152 TYR   B CA   1 
ATOM   6119 C  C    . TYR   B 1 152 ? 41.577 -24.435 -11.190 1.00 11.57 ?  152 TYR   B C    1 
ATOM   6120 O  O    . TYR   B 1 152 ? 42.429 -23.826 -10.535 1.00 12.62 ?  152 TYR   B O    1 
ATOM   6121 C  CB   . TYR   B 1 152 ? 41.826 -23.042 -13.295 1.00 13.37 ?  152 TYR   B CB   1 
ATOM   6122 C  CG   . TYR   B 1 152 ? 41.148 -22.570 -14.559 1.00 13.92 ?  152 TYR   B CG   1 
ATOM   6123 C  CD1  . TYR   B 1 152 ? 40.495 -21.340 -14.616 1.00 14.35 ?  152 TYR   B CD1  1 
ATOM   6124 C  CD2  . TYR   B 1 152 ? 41.136 -23.373 -15.688 1.00 15.54 ?  152 TYR   B CD2  1 
ATOM   6125 C  CE1  . TYR   B 1 152 ? 39.861 -20.925 -15.772 1.00 16.06 ?  152 TYR   B CE1  1 
ATOM   6126 C  CE2  . TYR   B 1 152 ? 40.512 -22.967 -16.845 1.00 16.33 ?  152 TYR   B CE2  1 
ATOM   6127 C  CZ   . TYR   B 1 152 ? 39.874 -21.742 -16.884 1.00 16.46 ?  152 TYR   B CZ   1 
ATOM   6128 O  OH   . TYR   B 1 152 ? 39.249 -21.340 -18.040 1.00 19.18 ?  152 TYR   B OH   1 
ATOM   6129 H  H    . TYR   B 1 152 ? 40.392 -22.102 -11.411 1.00 14.62 ?  152 TYR   B H    1 
ATOM   6130 H  HA   . TYR   B 1 152 ? 40.345 -24.407 -12.843 1.00 14.55 ?  152 TYR   B HA   1 
ATOM   6131 H  HB2  . TYR   B 1 152 ? 42.200 -22.268 -12.842 1.00 16.04 ?  152 TYR   B HB2  1 
ATOM   6132 H  HB3  . TYR   B 1 152 ? 42.535 -23.656 -13.539 1.00 16.04 ?  152 TYR   B HB3  1 
ATOM   6133 H  HD1  . TYR   B 1 152 ? 40.484 -20.788 -13.864 1.00 17.22 ?  152 TYR   B HD1  1 
ATOM   6134 H  HD2  . TYR   B 1 152 ? 41.565 -24.198 -15.664 1.00 18.64 ?  152 TYR   B HD2  1 
ATOM   6135 H  HE1  . TYR   B 1 152 ? 39.431 -20.101 -15.805 1.00 19.27 ?  152 TYR   B HE1  1 
ATOM   6136 H  HE2  . TYR   B 1 152 ? 40.521 -23.518 -17.594 1.00 19.60 ?  152 TYR   B HE2  1 
ATOM   6137 H  HH   . TYR   B 1 152 ? 39.341 -21.933 -18.634 1.00 23.01 ?  152 TYR   B HH   1 
ATOM   6138 N  N    . LEU   B 1 153 ? 41.215 -25.690 -10.926 1.00 12.03 ?  153 LEU   B N    1 
ATOM   6139 C  CA   . LEU   B 1 153 ? 41.725 -26.443 -9.790  1.00 12.01 ?  153 LEU   B CA   1 
ATOM   6140 C  C    . LEU   B 1 153 ? 42.954 -27.244 -10.192 1.00 11.90 ?  153 LEU   B C    1 
ATOM   6141 O  O    . LEU   B 1 153 ? 42.930 -27.974 -11.184 1.00 13.39 ?  153 LEU   B O    1 
ATOM   6142 C  CB   . LEU   B 1 153 ? 40.646 -27.405 -9.283  1.00 12.17 ?  153 LEU   B CB   1 
ATOM   6143 C  CG   . LEU   B 1 153 ? 39.401 -26.752 -8.684  1.00 13.24 ?  153 LEU   B CG   1 
ATOM   6144 C  CD1  . LEU   B 1 153 ? 38.290 -27.788 -8.536  1.00 14.13 ?  153 LEU   B CD1  1 
ATOM   6145 C  CD2  . LEU   B 1 153 ? 39.718 -26.103 -7.337  1.00 13.39 ?  153 LEU   B CD2  1 
ATOM   6146 H  H    . LEU   B 1 153 ? 40.650 -26.135 -11.409 1.00 14.43 ?  153 LEU   B H    1 
ATOM   6147 H  HA   . LEU   B 1 153 ? 41.953 -25.829 -9.078  1.00 14.40 ?  153 LEU   B HA   1 
ATOM   6148 H  HB2  . LEU   B 1 153 ? 40.350 -27.957 -10.021 1.00 14.60 ?  153 LEU   B HB2  1 
ATOM   6149 H  HB3  . LEU   B 1 153 ? 41.035 -27.964 -8.593  1.00 14.60 ?  153 LEU   B HB3  1 
ATOM   6150 H  HG   . LEU   B 1 153 ? 39.083 -26.053 -9.279  1.00 15.89 ?  153 LEU   B HG   1 
ATOM   6151 H  HD11 . LEU   B 1 153 ? 37.493 -27.349 -8.194  1.00 16.95 ?  153 LEU   B HD11 1 
ATOM   6152 H  HD12 . LEU   B 1 153 ? 38.109 -28.175 -9.403  1.00 16.95 ?  153 LEU   B HD12 1 
ATOM   6153 H  HD13 . LEU   B 1 153 ? 38.581 -28.472 -7.916  1.00 16.95 ?  153 LEU   B HD13 1 
ATOM   6154 H  HD21 . LEU   B 1 153 ? 38.907 -25.739 -6.955  1.00 16.07 ?  153 LEU   B HD21 1 
ATOM   6155 H  HD22 . LEU   B 1 153 ? 40.091 -26.777 -6.743  1.00 16.07 ?  153 LEU   B HD22 1 
ATOM   6156 H  HD23 . LEU   B 1 153 ? 40.368 -25.393 -7.473  1.00 16.07 ?  153 LEU   B HD23 1 
ATOM   6157 N  N    . ALA   B 1 154 ? 44.008 -27.135 -9.391  1.00 12.36 ?  154 ALA   B N    1 
ATOM   6158 C  CA   . ALA   B 1 154 ? 45.238 -27.890 -9.586  1.00 13.45 ?  154 ALA   B CA   1 
ATOM   6159 C  C    . ALA   B 1 154 ? 45.321 -28.972 -8.515  1.00 14.24 ?  154 ALA   B C    1 
ATOM   6160 O  O    . ALA   B 1 154 ? 45.282 -28.672 -7.314  1.00 16.16 ?  154 ALA   B O    1 
ATOM   6161 C  CB   . ALA   B 1 154 ? 46.453 -26.966 -9.524  1.00 14.75 ?  154 ALA   B CB   1 
ATOM   6162 H  H    . ALA   B 1 154 ? 44.026 -26.608 -8.707  1.00 14.83 ?  154 ALA   B H    1 
ATOM   6163 H  HA   . ALA   B 1 154 ? 45.217 -28.312 -10.455 1.00 16.13 ?  154 ALA   B HA   1 
ATOM   6164 H  HB1  . ALA   B 1 154 ? 47.254 -27.491 -9.657  1.00 17.70 ?  154 ALA   B HB1  1 
ATOM   6165 H  HB2  . ALA   B 1 154 ? 46.377 -26.294 -10.224 1.00 17.70 ?  154 ALA   B HB2  1 
ATOM   6166 H  HB3  . ALA   B 1 154 ? 46.479 -26.531 -8.657  1.00 17.70 ?  154 ALA   B HB3  1 
ATOM   6167 N  N    . VAL   B 1 155 ? 45.415 -30.222 -8.953  1.00 13.65 ?  155 VAL   B N    1 
ATOM   6168 C  CA   . VAL   B 1 155 ? 45.528 -31.373 -8.065  1.00 13.97 ?  155 VAL   B CA   1 
ATOM   6169 C  C    . VAL   B 1 155 ? 46.865 -32.050 -8.353  1.00 14.32 ?  155 VAL   B C    1 
ATOM   6170 O  O    . VAL   B 1 155 ? 47.101 -32.533 -9.469  1.00 15.90 ?  155 VAL   B O    1 
ATOM   6171 C  CB   . VAL   B 1 155 ? 44.358 -32.353 -8.244  1.00 15.34 ?  155 VAL   B CB   1 
ATOM   6172 C  CG1  . VAL   B 1 155 ? 44.536 -33.546 -7.323  1.00 15.32 ?  155 VAL   B CG1  1 
ATOM   6173 C  CG2  . VAL   B 1 155 ? 43.024 -31.650 -7.974  1.00 16.49 ?  155 VAL   B CG2  1 
ATOM   6174 H  H    . VAL   B 1 155 ? 45.422 -30.435 -9.789  1.00 16.37 ?  155 VAL   B H    1 
ATOM   6175 H  HA   . VAL   B 1 155 ? 45.531 -31.070 -7.146  1.00 16.76 ?  155 VAL   B HA   1 
ATOM   6176 H  HB   . VAL   B 1 155 ? 44.347 -32.675 -9.160  1.00 18.40 ?  155 VAL   B HB   1 
ATOM   6177 H  HG11 . VAL   B 1 155 ? 43.707 -34.050 -7.291  1.00 18.37 ?  155 VAL   B HG11 1 
ATOM   6178 H  HG12 . VAL   B 1 155 ? 45.250 -34.110 -7.663  1.00 18.37 ?  155 VAL   B HG12 1 
ATOM   6179 H  HG13 . VAL   B 1 155 ? 44.761 -33.229 -6.433  1.00 18.37 ?  155 VAL   B HG13 1 
ATOM   6180 H  HG21 . VAL   B 1 155 ? 42.305 -32.297 -8.050  1.00 19.78 ?  155 VAL   B HG21 1 
ATOM   6181 H  HG22 . VAL   B 1 155 ? 43.040 -31.279 -7.077  1.00 19.78 ?  155 VAL   B HG22 1 
ATOM   6182 H  HG23 . VAL   B 1 155 ? 42.901 -30.941 -8.623  1.00 19.78 ?  155 VAL   B HG23 1 
ATOM   6183 N  N    . PHE   B 1 156 ? 47.737 -32.086 -7.345  1.00 14.86 ?  156 PHE   B N    1 
ATOM   6184 C  CA   . PHE   B 1 156 ? 49.113 -32.544 -7.552  1.00 15.83 ?  156 PHE   B CA   1 
ATOM   6185 C  C    . PHE   B 1 156 ? 49.203 -34.043 -7.830  1.00 16.59 ?  156 PHE   B C    1 
ATOM   6186 O  O    . PHE   B 1 156 ? 49.921 -34.475 -8.743  1.00 18.71 ?  156 PHE   B O    1 
ATOM   6187 C  CB   . PHE   B 1 156 ? 49.946 -32.182 -6.325  1.00 15.48 ?  156 PHE   B CB   1 
ATOM   6188 C  CG   . PHE   B 1 156 ? 51.367 -32.646 -6.389  1.00 15.94 ?  156 PHE   B CG   1 
ATOM   6189 C  CD1  . PHE   B 1 156 ? 52.243 -32.116 -7.319  1.00 17.71 ?  156 PHE   B CD1  1 
ATOM   6190 C  CD2  . PHE   B 1 156 ? 51.838 -33.590 -5.498  1.00 16.17 ?  156 PHE   B CD2  1 
ATOM   6191 C  CE1  . PHE   B 1 156 ? 53.562 -32.531 -7.371  1.00 18.68 ?  156 PHE   B CE1  1 
ATOM   6192 C  CE2  . PHE   B 1 156 ? 53.156 -34.009 -5.547  1.00 17.66 ?  156 PHE   B CE2  1 
ATOM   6193 C  CZ   . PHE   B 1 156 ? 54.014 -33.478 -6.487  1.00 18.40 ?  156 PHE   B CZ   1 
ATOM   6194 H  H    . PHE   B 1 156 ? 47.557 -31.855 -6.538  1.00 17.83 ?  156 PHE   B H    1 
ATOM   6195 H  HA   . PHE   B 1 156 ? 49.488 -32.078 -8.312  1.00 18.99 ?  156 PHE   B HA   1 
ATOM   6196 H  HB2  . PHE   B 1 156 ? 49.956 -31.217 -6.231  1.00 18.57 ?  156 PHE   B HB2  1 
ATOM   6197 H  HB3  . PHE   B 1 156 ? 49.541 -32.583 -5.540  1.00 18.57 ?  156 PHE   B HB3  1 
ATOM   6198 H  HD1  . PHE   B 1 156 ? 51.941 -31.473 -7.920  1.00 21.25 ?  156 PHE   B HD1  1 
ATOM   6199 H  HD2  . PHE   B 1 156 ? 51.259 -33.956 -4.866  1.00 19.39 ?  156 PHE   B HD2  1 
ATOM   6200 H  HE1  . PHE   B 1 156 ? 54.141 -32.172 -8.005  1.00 22.41 ?  156 PHE   B HE1  1 
ATOM   6201 H  HE2  . PHE   B 1 156 ? 53.461 -34.656 -4.950  1.00 21.18 ?  156 PHE   B HE2  1 
ATOM   6202 H  HZ   . PHE   B 1 156 ? 54.899 -33.764 -6.520  1.00 22.07 ?  156 PHE   B HZ   1 
ATOM   6203 N  N    . ASP   B 1 157 ? 48.536 -34.857 -7.024  1.00 17.03 ?  157 ASP   B N    1 
ATOM   6204 C  CA   . ASP   B 1 157 ? 48.682 -36.304 -7.116  1.00 18.50 ?  157 ASP   B CA   1 
ATOM   6205 C  C    . ASP   B 1 157 ? 47.767 -36.852 -8.206  1.00 18.32 ?  157 ASP   B C    1 
ATOM   6206 O  O    . ASP   B 1 157 ? 46.543 -36.723 -8.111  1.00 17.51 ?  157 ASP   B O    1 
ATOM   6207 C  CB   . ASP   B 1 157 ? 48.326 -36.915 -5.767  1.00 20.40 ?  157 ASP   B CB   1 
ATOM   6208 C  CG   . ASP   B 1 157 ? 48.477 -38.422 -5.748  1.00 22.70 ?  157 ASP   B CG   1 
ATOM   6209 O  OD1  . ASP   B 1 157 ? 48.819 -39.022 -6.794  1.00 22.99 ?  157 ASP   B OD1  1 
ATOM   6210 O  OD2  . ASP   B 1 157 ? 48.265 -39.011 -4.671  1.00 24.85 -1 157 ASP   B OD2  1 
ATOM   6211 H  H    . ASP   B 1 157 ? 47.995 -34.598 -6.411  1.00 20.43 ?  157 ASP   B H    1 
ATOM   6212 H  HA   . ASP   B 1 157 ? 49.600 -36.533 -7.334  1.00 22.20 ?  157 ASP   B HA   1 
ATOM   6213 H  HB2  . ASP   B 1 157 ? 48.899 -36.529 -5.089  1.00 24.47 ?  157 ASP   B HB2  1 
ATOM   6214 H  HB3  . ASP   B 1 157 ? 47.398 -36.709 -5.568  1.00 24.47 ?  157 ASP   B HB3  1 
ATOM   6215 N  N    A LYS   B 1 158 ? 48.361 -37.500 -9.215  0.68 19.25 ?  158 LYS   B N    1 
ATOM   6216 N  N    B LYS   B 1 158 ? 48.365 -37.454 -9.242  0.32 18.80 ?  158 LYS   B N    1 
ATOM   6217 C  CA   A LYS   B 1 158 ? 47.587 -38.109 -10.297 0.68 20.46 ?  158 LYS   B CA   1 
ATOM   6218 C  CA   B LYS   B 1 158 ? 47.593 -38.015 -10.348 0.32 19.54 ?  158 LYS   B CA   1 
ATOM   6219 C  C    A LYS   B 1 158 ? 46.522 -39.067 -9.765  0.68 20.86 ?  158 LYS   B C    1 
ATOM   6220 C  C    B LYS   B 1 158 ? 46.539 -39.002 -9.862  0.32 19.44 ?  158 LYS   B C    1 
ATOM   6221 O  O    A LYS   B 1 158 ? 45.405 -39.124 -10.294 0.68 21.13 ?  158 LYS   B O    1 
ATOM   6222 O  O    B LYS   B 1 158 ? 45.454 -39.095 -10.449 0.32 19.50 ?  158 LYS   B O    1 
ATOM   6223 C  CB   A LYS   B 1 158 ? 48.535 -38.838 -11.258 0.68 22.29 ?  158 LYS   B CB   1 
ATOM   6224 C  CB   B LYS   B 1 158 ? 48.544 -38.695 -11.343 0.32 20.77 ?  158 LYS   B CB   1 
ATOM   6225 C  CG   A LYS   B 1 158 ? 47.853 -39.750 -12.272 0.68 24.35 ?  158 LYS   B CG   1 
ATOM   6226 C  CG   B LYS   B 1 158 ? 47.879 -39.613 -12.367 0.32 22.06 ?  158 LYS   B CG   1 
ATOM   6227 C  CD   A LYS   B 1 158 ? 46.989 -38.976 -13.246 0.68 26.27 ?  158 LYS   B CD   1 
ATOM   6228 C  CD   B LYS   B 1 158 ? 46.975 -38.852 -13.318 0.32 23.54 ?  158 LYS   B CD   1 
ATOM   6229 C  CE   A LYS   B 1 158 ? 46.399 -39.895 -14.301 0.68 27.99 ?  158 LYS   B CE   1 
ATOM   6230 C  CE   B LYS   B 1 158 ? 46.404 -39.774 -14.386 0.32 24.69 ?  158 LYS   B CE   1 
ATOM   6231 N  NZ   A LYS   B 1 158 ? 45.339 -39.219 -15.101 0.68 28.33 ?  158 LYS   B NZ   1 
ATOM   6232 N  NZ   B LYS   B 1 158 ? 45.368 -39.095 -15.215 0.32 25.08 ?  158 LYS   B NZ   1 
ATOM   6233 H  H    A LYS   B 1 158 ? 49.214 -37.607 -9.291  0.68 23.09 ?  158 LYS   B H    1 
ATOM   6234 H  H    B LYS   B 1 158 ? 49.217 -37.552 -9.325  0.32 22.55 ?  158 LYS   B H    1 
ATOM   6235 H  HA   A LYS   B 1 158 ? 47.141 -37.412 -10.799 0.68 24.55 ?  158 LYS   B HA   1 
ATOM   6236 H  HA   B LYS   B 1 158 ? 47.140 -37.298 -10.817 0.32 23.44 ?  158 LYS   B HA   1 
ATOM   6237 H  HB2  A LYS   B 1 158 ? 49.039 -38.176 -11.762 0.68 26.75 ?  158 LYS   B HB2  1 
ATOM   6238 H  HB2  B LYS   B 1 158 ? 49.017 -38.007 -11.841 0.32 24.92 ?  158 LYS   B HB2  1 
ATOM   6239 H  HB3  A LYS   B 1 158 ? 49.149 -39.384 -10.742 0.68 26.75 ?  158 LYS   B HB3  1 
ATOM   6240 H  HB3  B LYS   B 1 158 ? 49.182 -39.230 -10.847 0.32 24.92 ?  158 LYS   B HB3  1 
ATOM   6241 H  HG2  A LYS   B 1 158 ? 48.536 -40.211 -12.785 0.68 29.22 ?  158 LYS   B HG2  1 
ATOM   6242 H  HG2  B LYS   B 1 158 ? 48.571 -40.041 -12.895 0.32 26.47 ?  158 LYS   B HG2  1 
ATOM   6243 H  HG3  A LYS   B 1 158 ? 47.298 -40.402 -11.815 0.68 29.22 ?  158 LYS   B HG3  1 
ATOM   6244 H  HG3  B LYS   B 1 158 ? 47.351 -40.291 -11.914 0.32 26.47 ?  158 LYS   B HG3  1 
ATOM   6245 H  HD2  A LYS   B 1 158 ? 46.260 -38.553 -12.766 0.68 31.52 ?  158 LYS   B HD2  1 
ATOM   6246 H  HD2  B LYS   B 1 158 ? 46.236 -38.466 -12.823 0.32 28.24 ?  158 LYS   B HD2  1 
ATOM   6247 H  HD3  A LYS   B 1 158 ? 47.530 -38.306 -13.695 0.68 31.52 ?  158 LYS   B HD3  1 
ATOM   6248 H  HD3  B LYS   B 1 158 ? 47.487 -38.155 -13.759 0.32 28.24 ?  158 LYS   B HD3  1 
ATOM   6249 H  HE2  A LYS   B 1 158 ? 47.100 -40.177 -14.908 0.68 33.59 ?  158 LYS   B HE2  1 
ATOM   6250 H  HE2  B LYS   B 1 158 ? 47.120 -40.063 -14.975 0.32 29.62 ?  158 LYS   B HE2  1 
ATOM   6251 H  HE3  A LYS   B 1 158 ? 46.004 -40.668 -13.867 0.68 33.59 ?  158 LYS   B HE3  1 
ATOM   6252 H  HE3  B LYS   B 1 158 ? 45.994 -40.543 -13.959 0.32 29.62 ?  158 LYS   B HE3  1 
ATOM   6253 H  HZ1  A LYS   B 1 158 ? 45.010 -39.779 -15.709 0.68 34.00 ?  158 LYS   B HZ1  1 
ATOM   6254 H  HZ1  B LYS   B 1 158 ? 45.053 -39.657 -15.829 0.32 30.09 ?  158 LYS   B HZ1  1 
ATOM   6255 H  HZ2  A LYS   B 1 158 ? 44.678 -38.951 -14.567 0.68 34.00 ?  158 LYS   B HZ2  1 
ATOM   6256 H  HZ2  B LYS   B 1 158 ? 44.696 -38.824 -14.698 0.32 30.09 ?  158 LYS   B HZ2  1 
ATOM   6257 H  HZ3  A LYS   B 1 158 ? 45.678 -38.508 -15.516 0.68 34.00 ?  158 LYS   B HZ3  1 
ATOM   6258 H  HZ3  B LYS   B 1 158 ? 45.722 -38.388 -15.624 0.32 30.09 ?  158 LYS   B HZ3  1 
ATOM   6259 N  N    A ASN   B 1 159 ? 46.855 -39.845 -8.734  0.68 20.92 ?  159 ASN   B N    1 
ATOM   6260 N  N    B ASN   B 1 159 ? 46.839 -39.754 -8.803  0.32 19.36 ?  159 ASN   B N    1 
ATOM   6261 C  CA   A ASN   B 1 159 ? 45.891 -40.813 -8.216  0.68 21.26 ?  159 ASN   B CA   1 
ATOM   6262 C  CA   B ASN   B 1 159 ? 45.886 -40.744 -8.311  0.32 19.52 ?  159 ASN   B CA   1 
ATOM   6263 C  C    A ASN   B 1 159 ? 44.702 -40.127 -7.549  0.68 20.23 ?  159 ASN   B C    1 
ATOM   6264 C  C    B ASN   B 1 159 ? 44.693 -40.079 -7.629  0.32 19.17 ?  159 ASN   B C    1 
ATOM   6265 O  O    A ASN   B 1 159 ? 43.571 -40.624 -7.634  0.68 20.54 ?  159 ASN   B O    1 
ATOM   6266 O  O    B ASN   B 1 159 ? 43.555 -40.543 -7.770  0.32 19.08 ?  159 ASN   B O    1 
ATOM   6267 C  CB   A ASN   B 1 159 ? 46.582 -41.784 -7.260  0.68 23.07 ?  159 ASN   B CB   1 
ATOM   6268 C  CB   B ASN   B 1 159 ? 46.591 -41.733 -7.382  0.32 20.17 ?  159 ASN   B CB   1 
ATOM   6269 C  CG   A ASN   B 1 159 ? 47.615 -42.644 -7.958  0.68 25.24 ?  159 ASN   B CG   1 
ATOM   6270 C  CG   B ASN   B 1 159 ? 47.619 -42.584 -8.110  0.32 21.20 ?  159 ASN   B CG   1 
ATOM   6271 O  OD1  A ASN   B 1 159 ? 47.375 -43.152 -9.058  0.68 26.05 ?  159 ASN   B OD1  1 
ATOM   6272 O  OD1  B ASN   B 1 159 ? 47.389 -43.029 -9.237  0.32 21.63 ?  159 ASN   B OD1  1 
ATOM   6273 N  ND2  A ASN   B 1 159 ? 48.775 -42.810 -7.326  0.68 26.06 ?  159 ASN   B ND2  1 
ATOM   6274 N  ND2  B ASN   B 1 159 ? 48.762 -42.809 -7.471  0.32 21.70 ?  159 ASN   B ND2  1 
ATOM   6275 H  H    A ASN   B 1 159 ? 47.613 -39.832 -8.331  0.68 25.10 ?  159 ASN   B H    1 
ATOM   6276 H  H    B ASN   B 1 159 ? 47.576 -39.711 -8.366  0.32 23.23 ?  159 ASN   B H    1 
ATOM   6277 H  HA   A ASN   B 1 159 ? 45.548 -41.330 -8.962  0.68 25.51 ?  159 ASN   B HA   1 
ATOM   6278 H  HA   B ASN   B 1 159 ? 45.549 -41.246 -9.069  0.32 23.42 ?  159 ASN   B HA   1 
ATOM   6279 H  HB2  A ASN   B 1 159 ? 47.027 -41.280 -6.563  0.68 27.67 ?  159 ASN   B HB2  1 
ATOM   6280 H  HB2  B ASN   B 1 159 ? 47.049 -41.242 -6.683  0.32 24.19 ?  159 ASN   B HB2  1 
ATOM   6281 H  HB3  A ASN   B 1 159 ? 45.916 -42.373 -6.876  0.68 27.67 ?  159 ASN   B HB3  1 
ATOM   6282 H  HB3  B ASN   B 1 159 ? 45.929 -42.328 -6.995  0.32 24.19 ?  159 ASN   B HB3  1 
ATOM   6283 H  HD21 A ASN   B 1 159 ? 49.396 -43.292 -7.679  0.68 31.27 ?  159 ASN   B HD21 1 
ATOM   6284 H  HD21 B ASN   B 1 159 ? 49.375 -43.286 -7.842  0.32 26.04 ?  159 ASN   B HD21 1 
ATOM   6285 H  HD22 A ASN   B 1 159 ? 48.901 -42.450 -6.554  0.68 31.27 ?  159 ASN   B HD22 1 
ATOM   6286 H  HD22 B ASN   B 1 159 ? 48.886 -42.487 -6.684  0.32 26.04 ?  159 ASN   B HD22 1 
ATOM   6287 N  N    . LEU   B 1 160 ? 44.922 -38.984 -6.894  1.00 19.04 ?  160 LEU   B N    1 
ATOM   6288 C  CA   . LEU   B 1 160 ? 43.796 -38.248 -6.331  1.00 18.16 ?  160 LEU   B CA   1 
ATOM   6289 C  C    . LEU   B 1 160 ? 42.996 -37.582 -7.437  1.00 17.67 ?  160 LEU   B C    1 
ATOM   6290 O  O    . LEU   B 1 160 ? 41.758 -37.586 -7.405  1.00 17.19 ?  160 LEU   B O    1 
ATOM   6291 C  CB   . LEU   B 1 160 ? 44.259 -37.223 -5.296  1.00 17.78 ?  160 LEU   B CB   1 
ATOM   6292 C  CG   . LEU   B 1 160 ? 43.135 -36.323 -4.756  1.00 17.31 ?  160 LEU   B CG   1 
ATOM   6293 C  CD1  . LEU   B 1 160 ? 42.010 -37.141 -4.125  1.00 18.23 ?  160 LEU   B CD1  1 
ATOM   6294 C  CD2  . LEU   B 1 160 ? 43.684 -35.314 -3.757  1.00 17.63 ?  160 LEU   B CD2  1 
ATOM   6295 H  H    A LEU   B 1 160 ? 45.695 -38.624 -6.772  0.68 22.84 ?  160 LEU   B H    1 
ATOM   6296 H  H    B LEU   B 1 160 ? 45.700 -38.657 -6.722  0.32 22.84 ?  160 LEU   B H    1 
ATOM   6297 H  HA   . LEU   B 1 160 ? 43.212 -38.876 -5.886  1.00 21.78 ?  160 LEU   B HA   1 
ATOM   6298 H  HB2  . LEU   B 1 160 ? 44.651 -37.703 -4.543  1.00 21.33 ?  160 LEU   B HB2  1 
ATOM   6299 H  HB3  . LEU   B 1 160 ? 44.936 -36.654 -5.700  1.00 21.33 ?  160 LEU   B HB3  1 
ATOM   6300 H  HG   . LEU   B 1 160 ? 42.758 -35.826 -5.495  1.00 20.77 ?  160 LEU   B HG   1 
ATOM   6301 H  HD11 . LEU   B 1 160 ? 41.373 -36.537 -3.719  1.00 21.87 ?  160 LEU   B HD11 1 
ATOM   6302 H  HD12 . LEU   B 1 160 ? 41.574 -37.670 -4.813  1.00 21.87 ?  160 LEU   B HD12 1 
ATOM   6303 H  HD13 . LEU   B 1 160 ? 42.386 -37.730 -3.449  1.00 21.87 ?  160 LEU   B HD13 1 
ATOM   6304 H  HD21 . LEU   B 1 160 ? 42.958 -34.741 -3.465  1.00 21.15 ?  160 LEU   B HD21 1 
ATOM   6305 H  HD22 . LEU   B 1 160 ? 44.058 -35.788 -3.001  1.00 21.15 ?  160 LEU   B HD22 1 
ATOM   6306 H  HD23 . LEU   B 1 160 ? 44.370 -34.783 -4.191  1.00 21.15 ?  160 LEU   B HD23 1 
ATOM   6307 N  N    . TYR   B 1 161 ? 43.686 -37.008 -8.428  1.00 18.01 ?  161 TYR   B N    1 
ATOM   6308 C  CA   . TYR   B 1 161 ? 43.003 -36.439 -9.586  1.00 17.32 ?  161 TYR   B CA   1 
ATOM   6309 C  C    . TYR   B 1 161 ? 42.058 -37.461 -10.205 1.00 17.24 ?  161 TYR   B C    1 
ATOM   6310 O  O    . TYR   B 1 161 ? 40.888 -37.163 -10.468 1.00 16.90 ?  161 TYR   B O    1 
ATOM   6311 C  CB   . TYR   B 1 161 ? 44.039 -35.962 -10.613 1.00 17.66 ?  161 TYR   B CB   1 
ATOM   6312 C  CG   . TYR   B 1 161 ? 43.456 -35.493 -11.925 1.00 18.13 ?  161 TYR   B CG   1 
ATOM   6313 C  CD1  . TYR   B 1 161 ? 43.053 -34.175 -12.088 1.00 18.06 ?  161 TYR   B CD1  1 
ATOM   6314 C  CD2  . TYR   B 1 161 ? 43.294 -36.365 -12.998 1.00 18.77 ?  161 TYR   B CD2  1 
ATOM   6315 C  CE1  . TYR   B 1 161 ? 42.513 -33.735 -13.276 1.00 19.51 ?  161 TYR   B CE1  1 
ATOM   6316 C  CE2  . TYR   B 1 161 ? 42.749 -35.932 -14.189 1.00 20.38 ?  161 TYR   B CE2  1 
ATOM   6317 C  CZ   . TYR   B 1 161 ? 42.363 -34.617 -14.323 1.00 20.20 ?  161 TYR   B CZ   1 
ATOM   6318 O  OH   . TYR   B 1 161 ? 41.819 -34.178 -15.505 1.00 22.14 ?  161 TYR   B OH   1 
ATOM   6319 H  H    . TYR   B 1 161 ? 44.540 -36.944 -8.457  1.00 21.61 ?  161 TYR   B H    1 
ATOM   6320 H  HA   . TYR   B 1 161 ? 42.478 -35.672 -9.306  1.00 20.78 ?  161 TYR   B HA   1 
ATOM   6321 H  HB2  . TYR   B 1 161 ? 44.534 -35.220 -10.234 1.00 21.19 ?  161 TYR   B HB2  1 
ATOM   6322 H  HB3  . TYR   B 1 161 ? 44.642 -36.693 -10.810 1.00 21.19 ?  161 TYR   B HB3  1 
ATOM   6323 H  HD1  . TYR   B 1 161 ? 43.151 -33.570 -11.385 1.00 21.67 ?  161 TYR   B HD1  1 
ATOM   6324 H  HD2  . TYR   B 1 161 ? 43.548 -37.254 -12.914 1.00 22.51 ?  161 TYR   B HD2  1 
ATOM   6325 H  HE1  . TYR   B 1 161 ? 42.250 -32.842 -13.367 1.00 23.41 ?  161 TYR   B HE1  1 
ATOM   6326 H  HE2  . TYR   B 1 161 ? 42.644 -36.520 -14.900 1.00 24.45 ?  161 TYR   B HE2  1 
ATOM   6327 H  HH   . TYR   B 1 161 ? 41.787 -34.810 -16.059 1.00 26.56 ?  161 TYR   B HH   1 
ATOM   6328 N  N    . ASP   B 1 162 ? 42.549 -38.685 -10.424 1.00 18.06 ?  162 ASP   B N    1 
ATOM   6329 C  CA   . ASP   B 1 162 ? 41.720 -39.720 -11.031 1.00 18.34 ?  162 ASP   B CA   1 
ATOM   6330 C  C    . ASP   B 1 162 ? 40.519 -40.053 -10.154 1.00 17.63 ?  162 ASP   B C    1 
ATOM   6331 O  O    . ASP   B 1 162 ? 39.411 -40.264 -10.662 1.00 17.75 ?  162 ASP   B O    1 
ATOM   6332 C  CB   . ASP   B 1 162 ? 42.551 -40.984 -11.280 1.00 20.00 ?  162 ASP   B CB   1 
ATOM   6333 C  CG   . ASP   B 1 162 ? 43.563 -40.828 -12.406 1.00 21.66 ?  162 ASP   B CG   1 
ATOM   6334 O  OD1  . ASP   B 1 162 ? 43.446 -39.885 -13.209 1.00 21.78 ?  162 ASP   B OD1  1 
ATOM   6335 O  OD2  . ASP   B 1 162 ? 44.465 -41.688 -12.504 1.00 23.24 -1 162 ASP   B OD2  1 
ATOM   6336 H  H    . ASP   B 1 162 ? 43.351 -38.931 -10.233 1.00 21.67 ?  162 ASP   B H    1 
ATOM   6337 H  HA   . ASP   B 1 162 ? 41.389 -39.401 -11.881 1.00 22.00 ?  162 ASP   B HA   1 
ATOM   6338 H  HB2  . ASP   B 1 162 ? 43.046 -41.204 -10.479 1.00 23.99 ?  162 ASP   B HB2  1 
ATOM   6339 H  HB3  . ASP   B 1 162 ? 41.955 -41.710 -11.518 1.00 23.99 ?  162 ASP   B HB3  1 
ATOM   6340 N  N    A LYS   B 1 163 ? 40.720 -40.123 -8.836  0.68 16.89 ?  163 LYS   B N    1 
ATOM   6341 N  N    B LYS   B 1 163 ? 40.720 -40.119 -8.835  0.32 17.71 ?  163 LYS   B N    1 
ATOM   6342 C  CA   A LYS   B 1 163 ? 39.602 -40.402 -7.941  0.68 17.55 ?  163 LYS   B CA   1 
ATOM   6343 C  CA   B LYS   B 1 163 ? 39.603 -40.400 -7.938  0.32 18.43 ?  163 LYS   B CA   1 
ATOM   6344 C  C    A LYS   B 1 163 ? 38.561 -39.288 -7.993  0.68 16.67 ?  163 LYS   B C    1 
ATOM   6345 C  C    B LYS   B 1 163 ? 38.563 -39.286 -7.990  0.32 17.08 ?  163 LYS   B C    1 
ATOM   6346 O  O    A LYS   B 1 163 ? 37.349 -39.552 -7.981  0.68 17.62 ?  163 LYS   B O    1 
ATOM   6347 O  O    B LYS   B 1 163 ? 37.354 -39.551 -7.976  0.32 17.46 ?  163 LYS   B O    1 
ATOM   6348 C  CB   A LYS   B 1 163 ? 40.100 -40.604 -6.510  0.68 20.39 ?  163 LYS   B CB   1 
ATOM   6349 C  CB   B LYS   B 1 163 ? 40.110 -40.591 -6.509  0.32 21.01 ?  163 LYS   B CB   1 
ATOM   6350 C  CG   A LYS   B 1 163 ? 39.016 -41.105 -5.572  0.68 24.94 ?  163 LYS   B CG   1 
ATOM   6351 C  CG   B LYS   B 1 163 ? 39.030 -41.047 -5.543  0.32 24.04 ?  163 LYS   B CG   1 
ATOM   6352 C  CD   A LYS   B 1 163 ? 39.464 -41.160 -4.123  0.68 29.03 ?  163 LYS   B CD   1 
ATOM   6353 C  CD   B LYS   B 1 163 ? 39.552 -41.208 -4.126  0.32 26.97 ?  163 LYS   B CD   1 
ATOM   6354 C  CE   A LYS   B 1 163 ? 38.395 -41.830 -3.265  0.68 31.85 ?  163 LYS   B CE   1 
ATOM   6355 C  CE   B LYS   B 1 163 ? 38.497 -41.850 -3.237  0.32 29.17 ?  163 LYS   B CE   1 
ATOM   6356 N  NZ   A LYS   B 1 163 ? 38.542 -41.531 -1.812  0.68 33.70 ?  163 LYS   B NZ   1 
ATOM   6357 N  NZ   B LYS   B 1 163 ? 38.792 -41.687 -1.788  0.32 30.27 ?  163 LYS   B NZ   1 
ATOM   6358 H  H    A LYS   B 1 163 ? 41.481 -40.012 -8.445  0.68 20.26 ?  163 LYS   B H    1 
ATOM   6359 H  H    B LYS   B 1 163 ? 41.480 -40.009 -8.443  0.32 21.24 ?  163 LYS   B H    1 
ATOM   6360 H  HA   A LYS   B 1 163 ? 39.175 -41.222 -8.223  0.68 21.05 ?  163 LYS   B HA   1 
ATOM   6361 H  HA   B LYS   B 1 163 ? 39.176 -41.222 -8.216  0.32 22.11 ?  163 LYS   B HA   1 
ATOM   6362 H  HB2  A LYS   B 1 163 ? 40.819 -41.260 -6.513  0.68 24.47 ?  163 LYS   B HB2  1 
ATOM   6363 H  HB2  B LYS   B 1 163 ? 40.811 -41.264 -6.510  0.32 25.21 ?  163 LYS   B HB2  1 
ATOM   6364 H  HB3  A LYS   B 1 163 ? 40.429 -39.760 -6.163  0.68 24.47 ?  163 LYS   B HB3  1 
ATOM   6365 H  HB3  B LYS   B 1 163 ? 40.464 -39.749 -6.182  0.32 25.21 ?  163 LYS   B HB3  1 
ATOM   6366 H  HG2  A LYS   B 1 163 ? 38.251 -40.513 -5.624  0.68 29.93 ?  163 LYS   B HG2  1 
ATOM   6367 H  HG2  B LYS   B 1 163 ? 38.317 -40.390 -5.527  0.32 28.84 ?  163 LYS   B HG2  1 
ATOM   6368 H  HG3  A LYS   B 1 163 ? 38.758 -42.003 -5.839  0.68 29.93 ?  163 LYS   B HG3  1 
ATOM   6369 H  HG3  B LYS   B 1 163 ? 38.685 -41.906 -5.836  0.32 28.84 ?  163 LYS   B HG3  1 
ATOM   6370 H  HD2  A LYS   B 1 163 ? 40.281 -41.679 -4.055  0.68 34.83 ?  163 LYS   B HD2  1 
ATOM   6371 H  HD2  B LYS   B 1 163 ? 40.336 -41.779 -4.133  0.32 32.36 ?  163 LYS   B HD2  1 
ATOM   6372 H  HD3  A LYS   B 1 163 ? 39.605 -40.260 -3.793  0.68 34.83 ?  163 LYS   B HD3  1 
ATOM   6373 H  HD3  B LYS   B 1 163 ? 39.771 -40.336 -3.762  0.32 32.36 ?  163 LYS   B HD3  1 
ATOM   6374 H  HE2  A LYS   B 1 163 ? 37.520 -41.526 -3.550  0.68 38.21 ?  163 LYS   B HE2  1 
ATOM   6375 H  HE2  B LYS   B 1 163 ? 37.636 -41.443 -3.418  0.32 35.00 ?  163 LYS   B HE2  1 
ATOM   6376 H  HE3  A LYS   B 1 163 ? 38.460 -42.790 -3.379  0.68 38.21 ?  163 LYS   B HE3  1 
ATOM   6377 H  HE3  B LYS   B 1 163 ? 38.459 -42.800 -3.430  0.32 35.00 ?  163 LYS   B HE3  1 
ATOM   6378 H  HZ1  A LYS   B 1 163 ? 37.898 -41.939 -1.352  0.68 40.44 ?  163 LYS   B HZ1  1 
ATOM   6379 H  HZ1  B LYS   B 1 163 ? 38.153 -42.074 -1.303  0.32 36.32 ?  163 LYS   B HZ1  1 
ATOM   6380 H  HZ2  A LYS   B 1 163 ? 39.332 -41.818 -1.522  0.68 40.44 ?  163 LYS   B HZ2  1 
ATOM   6381 H  HZ2  B LYS   B 1 163 ? 39.573 -42.065 -1.593  0.32 36.32 ?  163 LYS   B HZ2  1 
ATOM   6382 H  HZ3  A LYS   B 1 163 ? 38.483 -40.654 -1.675  0.68 40.44 ?  163 LYS   B HZ3  1 
ATOM   6383 H  HZ3  B LYS   B 1 163 ? 38.828 -40.822 -1.581  0.32 36.32 ?  163 LYS   B HZ3  1 
ATOM   6384 N  N    . LEU   B 1 164 ? 39.019 -38.034 -8.051  1.00 15.83 ?  164 LEU   B N    1 
ATOM   6385 C  CA   . LEU   B 1 164 ? 38.102 -36.901 -8.095  1.00 15.47 ?  164 LEU   B CA   1 
ATOM   6386 C  C    . LEU   B 1 164 ? 37.309 -36.881 -9.398  1.00 15.57 ?  164 LEU   B C    1 
ATOM   6387 O  O    . LEU   B 1 164 ? 36.086 -36.675 -9.392  1.00 16.41 ?  164 LEU   B O    1 
ATOM   6388 C  CB   . LEU   B 1 164 ? 38.899 -35.602 -7.929  1.00 14.73 ?  164 LEU   B CB   1 
ATOM   6389 C  CG   . LEU   B 1 164 ? 39.446 -35.333 -6.530  1.00 15.42 ?  164 LEU   B CG   1 
ATOM   6390 C  CD1  . LEU   B 1 164 ? 40.534 -34.270 -6.585  1.00 15.61 ?  164 LEU   B CD1  1 
ATOM   6391 C  CD2  . LEU   B 1 164 ? 38.350 -34.904 -5.580  1.00 17.19 ?  164 LEU   B CD2  1 
ATOM   6392 H  H    A LEU   B 1 164 ? 39.853 -37.814 -8.066  0.68 18.99 ?  164 LEU   B H    1 
ATOM   6393 H  H    B LEU   B 1 164 ? 39.853 -37.814 -8.065  0.32 18.99 ?  164 LEU   B H    1 
ATOM   6394 H  HA   . LEU   B 1 164 ? 37.476 -36.966 -7.364  1.00 18.55 ?  164 LEU   B HA   1 
ATOM   6395 H  HB2  . LEU   B 1 164 ? 39.655 -35.626 -8.537  1.00 17.67 ?  164 LEU   B HB2  1 
ATOM   6396 H  HB3  . LEU   B 1 164 ? 38.323 -34.858 -8.162  1.00 17.67 ?  164 LEU   B HB3  1 
ATOM   6397 H  HG   . LEU   B 1 164 ? 39.845 -36.145 -6.186  1.00 18.50 ?  164 LEU   B HG   1 
ATOM   6398 H  HD11 . LEU   B 1 164 ? 40.866 -34.107 -5.686  1.00 18.72 ?  164 LEU   B HD11 1 
ATOM   6399 H  HD12 . LEU   B 1 164 ? 41.262 -34.585 -7.149  1.00 18.72 ?  164 LEU   B HD12 1 
ATOM   6400 H  HD13 . LEU   B 1 164 ? 40.166 -33.452 -6.953  1.00 18.72 ?  164 LEU   B HD13 1 
ATOM   6401 H  HD21 . LEU   B 1 164 ? 38.739 -34.707 -4.715  1.00 20.63 ?  164 LEU   B HD21 1 
ATOM   6402 H  HD22 . LEU   B 1 164 ? 37.913 -34.115 -5.935  1.00 20.63 ?  164 LEU   B HD22 1 
ATOM   6403 H  HD23 . LEU   B 1 164 ? 37.708 -35.628 -5.496  1.00 20.63 ?  164 LEU   B HD23 1 
ATOM   6404 N  N    . VAL   B 1 165 ? 37.993 -37.048 -10.531 1.00 17.06 ?  165 VAL   B N    1 
ATOM   6405 C  CA   . VAL   B 1 165 ? 37.326 -36.979 -11.828 1.00 18.41 ?  165 VAL   B CA   1 
ATOM   6406 C  C    . VAL   B 1 165 ? 36.394 -38.169 -12.007 1.00 20.35 ?  165 VAL   B C    1 
ATOM   6407 O  O    . VAL   B 1 165 ? 35.231 -38.023 -12.408 1.00 21.74 ?  165 VAL   B O    1 
ATOM   6408 C  CB   . VAL   B 1 165 ? 38.365 -36.909 -12.964 1.00 19.53 ?  165 VAL   B CB   1 
ATOM   6409 C  CG1  . VAL   B 1 165 ? 37.689 -37.028 -14.310 1.00 20.80 ?  165 VAL   B CG1  1 
ATOM   6410 C  CG2  . VAL   B 1 165 ? 39.164 -35.620 -12.883 1.00 19.13 ?  165 VAL   B CG2  1 
ATOM   6411 H  H    . VAL   B 1 165 ? 38.844 -37.192 -10.576 1.00 20.47 ?  165 VAL   B H    1 
ATOM   6412 H  HA   . VAL   B 1 165 ? 36.794 -36.172 -11.868 1.00 22.08 ?  165 VAL   B HA   1 
ATOM   6413 H  HB   . VAL   B 1 165 ? 38.991 -37.644 -12.871 1.00 23.43 ?  165 VAL   B HB   1 
ATOM   6414 H  HG11 . VAL   B 1 165 ? 38.295 -36.721 -14.999 1.00 24.95 ?  165 VAL   B HG11 1 
ATOM   6415 H  HG12 . VAL   B 1 165 ? 37.467 -37.962 -14.464 1.00 24.95 ?  165 VAL   B HG12 1 
ATOM   6416 H  HG13 . VAL   B 1 165 ? 36.884 -36.492 -14.308 1.00 24.95 ?  165 VAL   B HG13 1 
ATOM   6417 H  HG21 . VAL   B 1 165 ? 39.798 -35.591 -13.619 1.00 22.95 ?  165 VAL   B HG21 1 
ATOM   6418 H  HG22 . VAL   B 1 165 ? 38.555 -34.866 -12.946 1.00 22.95 ?  165 VAL   B HG22 1 
ATOM   6419 H  HG23 . VAL   B 1 165 ? 39.639 -35.590 -12.038 1.00 22.95 ?  165 VAL   B HG23 1 
ATOM   6420 N  N    . SER   B 1 166 ? 36.901 -39.371 -11.719 1.00 21.64 ?  166 SER   B N    1 
ATOM   6421 C  CA   . SER   B 1 166 ? 36.147 -40.581 -12.013 1.00 23.46 ?  166 SER   B CA   1 
ATOM   6422 C  C    . SER   B 1 166 ? 34.893 -40.677 -11.160 1.00 23.98 ?  166 SER   B C    1 
ATOM   6423 O  O    . SER   B 1 166 ? 33.922 -41.303 -11.581 1.00 25.45 ?  166 SER   B O    1 
ATOM   6424 C  CB   . SER   B 1 166 ? 37.016 -41.837 -11.851 1.00 24.45 ?  166 SER   B CB   1 
ATOM   6425 O  OG   . SER   B 1 166 ? 37.388 -42.061 -10.501 1.00 24.34 ?  166 SER   B OG   1 
ATOM   6426 H  H    . SER   B 1 166 ? 37.675 -39.509 -11.365 1.00 25.96 ?  166 SER   B H    1 
ATOM   6427 H  HA   . SER   B 1 166 ? 35.865 -40.552 -12.940 1.00 28.14 ?  166 SER   B HA   1 
ATOM   6428 H  HB2  . SER   B 1 166 ? 36.517 -42.608 -12.165 1.00 29.34 ?  166 SER   B HB2  1 
ATOM   6429 H  HB3  . SER   B 1 166 ? 37.822 -41.731 -12.384 1.00 29.34 ?  166 SER   B HB3  1 
ATOM   6430 H  HG   . SER   B 1 166 ? 37.831 -41.404 -10.215 1.00 29.20 ?  166 SER   B HG   1 
ATOM   6431 N  N    . SER   B 1 167 ? 34.881 -40.064 -9.978  1.00 22.18 ?  167 SER   B N    1 
ATOM   6432 C  CA   . SER   B 1 167 ? 33.735 -40.119 -9.079  1.00 21.98 ?  167 SER   B CA   1 
ATOM   6433 C  C    . SER   B 1 167 ? 32.825 -38.895 -9.167  1.00 21.46 ?  167 SER   B C    1 
ATOM   6434 O  O    . SER   B 1 167 ? 31.750 -38.896 -8.556  1.00 21.69 ?  167 SER   B O    1 
ATOM   6435 C  CB   . SER   B 1 167 ? 34.198 -40.302 -7.626  1.00 21.71 ?  167 SER   B CB   1 
ATOM   6436 O  OG   . SER   B 1 167 ? 34.867 -39.144 -7.150  1.00 21.26 ?  167 SER   B OG   1 
ATOM   6437 H  H    . SER   B 1 167 ? 35.537 -39.612 -9.674  1.00 26.61 ?  167 SER   B H    1 
ATOM   6438 H  HA   . SER   B 1 167 ? 33.198 -40.893 -9.309  1.00 26.37 ?  167 SER   B HA   1 
ATOM   6439 H  HB2  . SER   B 1 167 ? 33.421 -40.472 -7.069  1.00 26.05 ?  167 SER   B HB2  1 
ATOM   6440 H  HB3  . SER   B 1 167 ? 34.803 -41.063 -7.583  1.00 26.05 ?  167 SER   B HB3  1 
ATOM   6441 H  HG   . SER   B 1 167 ? 35.545 -38.995 -7.619  1.00 25.51 ?  167 SER   B HG   1 
ATOM   6442 N  N    . PHE   B 1 168 ? 33.209 -37.854 -9.909  1.00 21.06 ?  168 PHE   B N    1 
ATOM   6443 C  CA   . PHE   B 1 168 ? 32.373 -36.655 -9.976  1.00 19.76 ?  168 PHE   B CA   1 
ATOM   6444 C  C    . PHE   B 1 168 ? 31.069 -36.922 -10.723 1.00 16.99 ?  168 PHE   B C    1 
ATOM   6445 O  O    . PHE   B 1 168 ? 30.016 -36.344 -10.389 1.00 17.21 ?  168 PHE   B O    1 
ATOM   6446 C  CB   . PHE   B 1 168 ? 33.144 -35.511 -10.634 1.00 20.57 ?  168 PHE   B CB   1 
ATOM   6447 C  CG   . PHE   B 1 168 ? 32.336 -34.268 -10.778 1.00 20.41 ?  168 PHE   B CG   1 
ATOM   6448 C  CD1  . PHE   B 1 168 ? 31.996 -33.524 -9.660  1.00 21.65 ?  168 PHE   B CD1  1 
ATOM   6449 C  CD2  . PHE   B 1 168 ? 31.886 -33.856 -12.015 1.00 19.78 ?  168 PHE   B CD2  1 
ATOM   6450 C  CE1  . PHE   B 1 168 ? 31.228 -32.387 -9.772  1.00 21.82 ?  168 PHE   B CE1  1 
ATOM   6451 C  CE2  . PHE   B 1 168 ? 31.126 -32.702 -12.143 1.00 21.02 ?  168 PHE   B CE2  1 
ATOM   6452 C  CZ   . PHE   B 1 168 ? 30.792 -31.965 -11.017 1.00 21.05 ?  168 PHE   B CZ   1 
ATOM   6453 H  H    . PHE   B 1 168 ? 33.936 -37.816 -10.371 1.00 25.26 ?  168 PHE   B H    1 
ATOM   6454 H  HA   . PHE   B 1 168 ? 32.146 -36.381 -9.077  1.00 23.71 ?  168 PHE   B HA   1 
ATOM   6455 H  HB2  . PHE   B 1 168 ? 33.919 -35.299 -10.090 1.00 24.68 ?  168 PHE   B HB2  1 
ATOM   6456 H  HB3  . PHE   B 1 168 ? 33.427 -35.784 -11.520 1.00 24.68 ?  168 PHE   B HB3  1 
ATOM   6457 H  HD1  . PHE   B 1 168 ? 32.284 -33.805 -8.821  1.00 25.98 ?  168 PHE   B HD1  1 
ATOM   6458 H  HD2  . PHE   B 1 168 ? 32.108 -34.343 -12.773 1.00 23.73 ?  168 PHE   B HD2  1 
ATOM   6459 H  HE1  . PHE   B 1 168 ? 31.010 -31.897 -9.013  1.00 26.18 ?  168 PHE   B HE1  1 
ATOM   6460 H  HE2  . PHE   B 1 168 ? 30.828 -32.429 -12.983 1.00 25.22 ?  168 PHE   B HE2  1 
ATOM   6461 H  HZ   . PHE   B 1 168 ? 30.274 -31.197 -11.098 1.00 25.26 ?  168 PHE   B HZ   1 
ATOM   6462 N  N    . LEU   B 1 169 ? 31.123 -37.792 -11.728 1.00 18.02 ?  169 LEU   B N    1 
ATOM   6463 C  CA   . LEU   B 1 169 ? 29.956 -38.125 -12.535 1.00 20.64 ?  169 LEU   B CA   1 
ATOM   6464 C  C    . LEU   B 1 169 ? 29.941 -39.572 -13.006 1.00 23.71 ?  169 LEU   B C    1 
ATOM   6465 O  O    . LEU   B 1 169 ? 29.036 -39.989 -13.732 1.00 25.98 ?  169 LEU   B O    1 
ATOM   6466 C  CB   . LEU   B 1 169 ? 29.894 -37.221 -13.762 1.00 22.48 ?  169 LEU   B CB   1 
ATOM   6467 C  CG   . LEU   B 1 169 ? 28.667 -36.321 -13.859 1.00 25.55 ?  169 LEU   B CG   1 
ATOM   6468 C  CD1  . LEU   B 1 169 ? 28.607 -35.698 -15.236 1.00 26.35 ?  169 LEU   B CD1  1 
ATOM   6469 C  CD2  . LEU   B 1 169 ? 27.389 -37.088 -13.557 1.00 26.10 ?  169 LEU   B CD2  1 
ATOM   6470 O  OXT  . LEU   B 1 169 ? 30.832 -40.350 -12.690 1.00 24.49 -1 169 LEU   B OXT  1 
ATOM   6471 H  H    . LEU   B 1 169 ? 31.841 -38.201 -11.973 1.00 21.62 ?  169 LEU   B H    1 
ATOM   6472 H  HA   . LEU   B 1 169 ? 29.169 -37.979 -11.996 1.00 24.76 ?  169 LEU   B HA   1 
ATOM   6473 H  HB2  . LEU   B 1 169 ? 30.675 -36.647 -13.763 1.00 26.97 ?  169 LEU   B HB2  1 
ATOM   6474 H  HB3  . LEU   B 1 169 ? 29.903 -37.779 -14.557 1.00 26.97 ?  169 LEU   B HB3  1 
ATOM   6475 H  HG   . LEU   B 1 169 ? 28.747 -35.602 -13.210 1.00 30.65 ?  169 LEU   B HG   1 
ATOM   6476 H  HD11 . LEU   B 1 169 ? 27.842 -35.105 -15.280 1.00 31.61 ?  169 LEU   B HD11 1 
ATOM   6477 H  HD12 . LEU   B 1 169 ? 29.424 -35.199 -15.390 1.00 31.61 ?  169 LEU   B HD12 1 
ATOM   6478 H  HD13 . LEU   B 1 169 ? 28.519 -36.404 -15.894 1.00 31.61 ?  169 LEU   B HD13 1 
ATOM   6479 H  HD21 . LEU   B 1 169 ? 26.648 -36.663 -14.009 1.00 31.32 ?  169 LEU   B HD21 1 
ATOM   6480 H  HD22 . LEU   B 1 169 ? 27.491 -38.002 -13.873 1.00 31.32 ?  169 LEU   B HD22 1 
ATOM   6481 H  HD23 . LEU   B 1 169 ? 27.240 -37.088 -12.598 1.00 31.32 ?  169 LEU   B HD23 1 
HETATM 6482 N  N2   B A1BBM C 2 .   ? 15.026 -0.118  4.045   0.32 12.32 ?  201 A1BBM A N2   1 
HETATM 6483 C  C3   B A1BBM C 2 .   ? 15.162 1.005   3.278   0.32 11.91 ?  201 A1BBM A C3   1 
HETATM 6484 C  C6   B A1BBM C 2 .   ? 15.374 2.278   3.911   0.32 11.89 ?  201 A1BBM A C6   1 
HETATM 6485 C  C9   B A1BBM C 2 .   ? 13.974 -2.559  0.347   0.32 13.07 ?  201 A1BBM A C9   1 
HETATM 6486 C  C12  B A1BBM C 2 .   ? 12.600 -0.478  0.701   0.32 13.28 ?  201 A1BBM A C12  1 
HETATM 6487 C  C1   B A1BBM C 2 .   ? 13.801 -1.293  1.233   0.32 12.51 ?  201 A1BBM A C1   1 
HETATM 6488 C  C10  B A1BBM C 2 .   ? 12.781 -3.493  0.447   0.32 13.86 ?  201 A1BBM A C10  1 
HETATM 6489 C  C11  B A1BBM C 2 .   ? 11.266 -1.194  0.811   0.32 14.14 ?  201 A1BBM A C11  1 
HETATM 6490 C  C2   B A1BBM C 2 .   ? 15.136 -0.452  1.207   0.32 11.51 ?  201 A1BBM A C2   1 
HETATM 6491 C  C4   B A1BBM C 2 .   ? 15.082 0.021   5.411   0.32 12.28 ?  201 A1BBM A C4   1 
HETATM 6492 C  C5   B A1BBM C 2 .   ? 15.414 2.217   5.335   0.32 12.03 ?  201 A1BBM A C5   1 
HETATM 6493 C  C7   B A1BBM C 2 .   ? 15.576 3.644   3.571   0.32 11.65 ?  201 A1BBM A C7   1 
HETATM 6494 C  C8   B A1BBM C 2 .   ? 15.722 4.382   4.751   0.32 11.55 ?  201 A1BBM A C8   1 
HETATM 6495 N  N1   B A1BBM C 2 .   ? 15.092 0.861   1.907   0.32 11.77 ?  201 A1BBM A N1   1 
HETATM 6496 N  N3   B A1BBM C 2 .   ? 15.273 1.129   6.118   0.32 12.37 ?  201 A1BBM A N3   1 
HETATM 6497 N  N4   B A1BBM C 2 .   ? 15.625 3.498   5.835   0.32 12.12 ?  201 A1BBM A N4   1 
HETATM 6498 O  O1   B A1BBM C 2 .   ? 13.499 -1.699  2.532   0.32 12.54 ?  201 A1BBM A O1   1 
HETATM 6499 S  S1   B A1BBM C 2 .   ? 11.243 -2.741  -0.115  0.32 14.52 ?  201 A1BBM A S1   1 
HETATM 6500 H  H10  B A1BBM C 2 .   ? 14.172 -2.302  -0.714  0.32 15.68 ?  201 A1BBM A H10  1 
HETATM 6501 H  H9   B A1BBM C 2 .   ? 14.870 -3.126  0.655   0.32 15.68 ?  201 A1BBM A H9   1 
HETATM 6502 H  H16  B A1BBM C 2 .   ? 12.536 0.501   1.208   0.32 15.94 ?  201 A1BBM A H16  1 
HETATM 6503 H  H15  B A1BBM C 2 .   ? 12.776 -0.226  -0.367  0.32 15.94 ?  201 A1BBM A H15  1 
HETATM 6504 H  H12  B A1BBM C 2 .   ? 12.933 -4.416  -0.154  0.32 16.63 ?  201 A1BBM A H12  1 
HETATM 6505 H  H11  B A1BBM C 2 .   ? 12.634 -3.895  1.466   0.32 16.63 ?  201 A1BBM A H11  1 
HETATM 6506 H  H13  B A1BBM C 2 .   ? 10.968 -1.385  1.853   0.32 16.97 ?  201 A1BBM A H13  1 
HETATM 6507 H  H14  B A1BBM C 2 .   ? 10.440 -0.576  0.403   0.32 16.97 ?  201 A1BBM A H14  1 
HETATM 6508 H  H2   B A1BBM C 2 .   ? 15.434 -0.277  0.151   0.32 13.81 ?  201 A1BBM A H2   1 
HETATM 6509 H  H3   B A1BBM C 2 .   ? 15.926 -1.077  1.636   0.32 13.81 ?  201 A1BBM A H3   1 
HETATM 6510 H  H5   B A1BBM C 2 .   ? 14.956 -0.892  6.050   0.32 14.74 ?  201 A1BBM A H5   1 
HETATM 6511 H  H6   B A1BBM C 2 .   ? 15.606 4.092   2.607   0.32 13.97 ?  201 A1BBM A H6   1 
HETATM 6512 H  H7   B A1BBM C 2 .   ? 15.884 5.407   4.951   0.32 13.86 ?  201 A1BBM A H7   1 
HETATM 6513 H  H4   B A1BBM C 2 .   ? 15.006 1.691   1.367   0.32 14.12 ?  201 A1BBM A H4   1 
HETATM 6514 H  H8   B A1BBM C 2 .   ? 15.688 3.724   6.812   0.32 14.54 ?  201 A1BBM A H8   1 
HETATM 6515 H  H1   B A1BBM C 2 .   ? 14.250 -2.218  2.843   0.32 15.04 ?  201 A1BBM A H1   1 
HETATM 6516 CL CL   B CL    D 3 .   ? 15.789 2.670   -0.802  0.32 13.70 ?  202 CL    A CL   1 
HETATM 6517 O  O    . HOH   E 4 .   ? 14.686 -4.720  20.524  1.00 47.30 ?  301 HOH   A O    1 
HETATM 6518 O  O    . HOH   E 4 .   ? 15.246 -12.255 18.711  1.00 47.92 ?  302 HOH   A O    1 
HETATM 6519 O  O    . HOH   E 4 .   ? 17.162 -18.012 15.084  1.00 28.15 ?  303 HOH   A O    1 
HETATM 6520 O  O    . HOH   E 4 .   ? 12.027 0.330   14.845  1.00 37.78 ?  304 HOH   A O    1 
HETATM 6521 O  O    . HOH   E 4 .   ? 18.527 -2.421  -16.397 1.00 49.68 ?  305 HOH   A O    1 
HETATM 6522 O  O    . HOH   E 4 .   ? 4.705  3.832   0.685   1.00 27.40 ?  306 HOH   A O    1 
HETATM 6523 O  O    . HOH   E 4 .   ? 9.193  -10.254 19.417  1.00 47.41 ?  307 HOH   A O    1 
HETATM 6524 O  O    . HOH   E 4 .   ? 26.831 11.409  1.642   1.00 16.87 ?  308 HOH   A O    1 
HETATM 6525 O  O    . HOH   E 4 .   ? 34.407 -1.860  12.514  1.00 41.26 ?  309 HOH   A O    1 
HETATM 6526 O  O    . HOH   E 4 .   ? 28.867 0.453   -9.742  1.00 22.22 ?  310 HOH   A O    1 
HETATM 6527 O  O    . HOH   E 4 .   ? 7.543  -6.266  -6.455  1.00 42.69 ?  311 HOH   A O    1 
HETATM 6528 O  O    . HOH   E 4 .   ? 0.671  -4.579  0.230   1.00 32.83 ?  312 HOH   A O    1 
HETATM 6529 O  O    . HOH   E 4 .   ? 28.225 -6.306  19.619  1.00 42.72 ?  313 HOH   A O    1 
HETATM 6530 O  O    . HOH   E 4 .   ? 17.697 -1.804  0.429   1.00 22.90 ?  314 HOH   A O    1 
HETATM 6531 O  O    . HOH   E 4 .   ? 20.624 -19.753 -5.017  1.00 26.84 ?  315 HOH   A O    1 
HETATM 6532 O  O    . HOH   E 4 .   ? 30.206 -13.294 -8.449  1.00 26.62 ?  316 HOH   A O    1 
HETATM 6533 O  O    . HOH   E 4 .   ? 42.414 10.525  5.144   1.00 20.96 ?  317 HOH   A O    1 
HETATM 6534 O  O    . HOH   E 4 .   ? 24.533 1.973   -7.066  1.00 21.01 ?  318 HOH   A O    1 
HETATM 6535 O  O    . HOH   E 4 .   ? 23.800 -15.763 -9.125  1.00 38.23 ?  319 HOH   A O    1 
HETATM 6536 O  O    . HOH   E 4 .   ? 18.940 -21.954 6.919   1.00 33.69 ?  320 HOH   A O    1 
HETATM 6537 O  O    . HOH   E 4 .   ? 8.857  -11.952 17.313  1.00 45.57 ?  321 HOH   A O    1 
HETATM 6538 O  O    . HOH   E 4 .   ? -0.423 -2.985  3.026   1.00 43.07 ?  322 HOH   A O    1 
HETATM 6539 O  O    . HOH   E 4 .   ? 14.729 -13.908 16.774  1.00 29.00 ?  323 HOH   A O    1 
HETATM 6540 O  O    . HOH   E 4 .   ? 28.603 -10.558 -14.067 1.00 40.45 ?  324 HOH   A O    1 
HETATM 6541 O  O    . HOH   E 4 .   ? 19.883 -12.604 -8.764  1.00 26.06 ?  325 HOH   A O    1 
HETATM 6542 O  O    . HOH   E 4 .   ? 8.201  -21.512 4.019   1.00 58.93 ?  326 HOH   A O    1 
HETATM 6543 O  O    . HOH   E 4 .   ? 6.935  -8.123  11.840  1.00 22.51 ?  327 HOH   A O    1 
HETATM 6544 O  O    . HOH   E 4 .   ? 3.646  -9.277  9.920   1.00 37.54 ?  328 HOH   A O    1 
HETATM 6545 O  O    . HOH   E 4 .   ? 11.730 -10.760 17.075  1.00 30.99 ?  329 HOH   A O    1 
HETATM 6546 O  O    . HOH   E 4 .   ? 11.679 -10.802 -10.034 1.00 45.45 ?  330 HOH   A O    1 
HETATM 6547 O  O    . HOH   E 4 .   ? 14.065 -4.605  -11.836 1.00 33.89 ?  331 HOH   A O    1 
HETATM 6548 O  O    . HOH   E 4 .   ? 26.505 -19.339 -1.763  1.00 14.92 ?  332 HOH   A O    1 
HETATM 6549 O  O    . HOH   E 4 .   ? 33.980 -1.126  -8.952  1.00 27.53 ?  333 HOH   A O    1 
HETATM 6550 O  O    . HOH   E 4 .   ? -0.687 -8.594  2.121   1.00 44.02 ?  334 HOH   A O    1 
HETATM 6551 O  O    . HOH   E 4 .   ? 37.538 2.818   10.245  1.00 30.19 ?  335 HOH   A O    1 
HETATM 6552 O  O    . HOH   E 4 .   ? 38.245 10.139  7.131   1.00 41.47 ?  336 HOH   A O    1 
HETATM 6553 O  O    . HOH   E 4 .   ? 36.242 -5.061  -0.499  1.00 30.92 ?  337 HOH   A O    1 
HETATM 6554 O  O    . HOH   E 4 .   ? 27.337 13.786  2.836   1.00 30.08 ?  338 HOH   A O    1 
HETATM 6555 O  O    . HOH   E 4 .   ? 18.702 -19.371 13.585  1.00 35.66 ?  339 HOH   A O    1 
HETATM 6556 O  O    . HOH   E 4 .   ? 22.725 12.518  1.638   1.00 14.83 ?  340 HOH   A O    1 
HETATM 6557 O  O    . HOH   E 4 .   ? 31.067 -18.145 7.809   1.00 19.44 ?  341 HOH   A O    1 
HETATM 6558 O  O    . HOH   E 4 .   ? 28.252 -0.151  -13.417 1.00 37.02 ?  342 HOH   A O    1 
HETATM 6559 O  O    . HOH   E 4 .   ? 7.966  -12.729 -0.849  1.00 21.08 ?  343 HOH   A O    1 
HETATM 6560 O  O    . HOH   E 4 .   ? 17.023 -19.291 4.946   1.00 15.88 ?  344 HOH   A O    1 
HETATM 6561 O  O    . HOH   E 4 .   ? 21.252 -2.385  -2.266  1.00 17.47 ?  345 HOH   A O    1 
HETATM 6562 O  O    A HOH   E 4 .   ? 14.271 0.557   6.824   0.68 24.49 ?  346 HOH   A O    1 
HETATM 6563 O  O    . HOH   E 4 .   ? 31.645 8.276   14.787  1.00 25.90 ?  347 HOH   A O    1 
HETATM 6564 O  O    . HOH   E 4 .   ? 15.048 3.978   17.722  1.00 40.88 ?  348 HOH   A O    1 
HETATM 6565 O  O    . HOH   E 4 .   ? 9.904  -21.357 5.736   1.00 18.83 ?  349 HOH   A O    1 
HETATM 6566 O  O    . HOH   E 4 .   ? 22.322 5.368   19.041  1.00 43.32 ?  350 HOH   A O    1 
HETATM 6567 O  O    . HOH   E 4 .   ? 38.538 4.973   6.969   1.00 16.26 ?  351 HOH   A O    1 
HETATM 6568 O  O    A HOH   E 4 .   ? 14.630 -3.670  3.121   0.68 17.32 ?  352 HOH   A O    1 
HETATM 6569 O  O    . HOH   E 4 .   ? 39.723 -1.020  -5.206  1.00 20.42 ?  353 HOH   A O    1 
HETATM 6570 O  O    . HOH   E 4 .   ? 17.141 -17.799 -5.010  1.00 26.58 ?  354 HOH   A O    1 
HETATM 6571 O  O    . HOH   E 4 .   ? 22.204 -19.248 11.435  1.00 33.47 ?  355 HOH   A O    1 
HETATM 6572 O  O    . HOH   E 4 .   ? 14.333 -21.259 -4.197  1.00 29.13 ?  356 HOH   A O    1 
HETATM 6573 O  O    . HOH   E 4 .   ? 44.320 7.110   6.428   1.00 27.20 ?  357 HOH   A O    1 
HETATM 6574 O  O    . HOH   E 4 .   ? 35.799 -12.651 6.839   1.00 16.01 ?  358 HOH   A O    1 
HETATM 6575 O  O    . HOH   E 4 .   ? 24.013 -2.139  -2.081  1.00 11.29 ?  359 HOH   A O    1 
HETATM 6576 O  O    . HOH   E 4 .   ? 42.579 4.282   5.366   1.00 32.62 ?  360 HOH   A O    1 
HETATM 6577 O  O    B HOH   E 4 .   ? 13.277 -1.341  -6.724  0.32 15.45 ?  361 HOH   A O    1 
HETATM 6578 O  O    . HOH   E 4 .   ? 37.289 11.949  4.905   1.00 34.78 ?  362 HOH   A O    1 
HETATM 6579 O  O    . HOH   E 4 .   ? 33.657 -7.171  4.294   1.00 17.46 ?  363 HOH   A O    1 
HETATM 6580 O  O    . HOH   E 4 .   ? 10.980 1.671   12.601  1.00 25.55 ?  364 HOH   A O    1 
HETATM 6581 O  O    . HOH   E 4 .   ? 25.674 -0.845  -7.362  1.00 15.91 ?  365 HOH   A O    1 
HETATM 6582 O  O    . HOH   E 4 .   ? 30.809 3.109   8.283   1.00 13.05 ?  366 HOH   A O    1 
HETATM 6583 O  O    . HOH   E 4 .   ? 31.098 -13.935 -2.438  1.00 14.61 ?  367 HOH   A O    1 
HETATM 6584 O  O    . HOH   E 4 .   ? 13.541 -15.261 -7.488  1.00 27.24 ?  368 HOH   A O    1 
HETATM 6585 O  O    . HOH   E 4 .   ? 31.797 -9.401  -6.661  1.00 25.00 ?  369 HOH   A O    1 
HETATM 6586 O  O    . HOH   E 4 .   ? 43.335 7.800   2.616   1.00 31.02 ?  370 HOH   A O    1 
HETATM 6587 O  O    . HOH   E 4 .   ? 18.546 9.428   9.046   1.00 22.51 ?  371 HOH   A O    1 
HETATM 6588 O  O    . HOH   E 4 .   ? 37.234 -2.792  9.750   1.00 43.30 ?  372 HOH   A O    1 
HETATM 6589 O  O    . HOH   E 4 .   ? 22.697 -11.981 21.885  1.00 50.31 ?  373 HOH   A O    1 
HETATM 6590 O  O    . HOH   E 4 .   ? 14.471 -24.634 11.572  1.00 39.82 ?  374 HOH   A O    1 
HETATM 6591 O  O    . HOH   E 4 .   ? 21.858 -21.898 8.469   1.00 29.19 ?  375 HOH   A O    1 
HETATM 6592 O  O    . HOH   E 4 .   ? 27.481 -10.585 14.084  1.00 17.49 ?  376 HOH   A O    1 
HETATM 6593 O  O    . HOH   E 4 .   ? 21.193 10.308  14.980  1.00 34.30 ?  377 HOH   A O    1 
HETATM 6594 O  O    . HOH   E 4 .   ? 10.394 -22.219 -1.280  1.00 50.67 ?  378 HOH   A O    1 
HETATM 6595 O  O    . HOH   E 4 .   ? 18.943 -0.706  -1.678  1.00 14.19 ?  379 HOH   A O    1 
HETATM 6596 O  O    . HOH   E 4 .   ? 24.228 -7.737  14.451  1.00 17.41 ?  380 HOH   A O    1 
HETATM 6597 O  O    . HOH   E 4 .   ? 43.957 8.533   -3.035  1.00 28.41 ?  381 HOH   A O    1 
HETATM 6598 O  O    A HOH   E 4 .   ? 15.188 -8.010  -9.626  0.68 22.34 ?  382 HOH   A O    1 
HETATM 6599 O  O    . HOH   E 4 .   ? 19.540 -11.136 24.115  1.00 78.43 ?  383 HOH   A O    1 
HETATM 6600 O  O    . HOH   E 4 .   ? 24.380 3.565   -1.809  1.00 15.74 ?  384 HOH   A O    1 
HETATM 6601 O  O    . HOH   E 4 .   ? 24.708 -17.508 12.767  1.00 24.36 ?  385 HOH   A O    1 
HETATM 6602 O  O    A HOH   E 4 .   ? 13.287 -1.454  -6.498  0.68 17.71 ?  386 HOH   A O    1 
HETATM 6603 O  O    . HOH   E 4 .   ? 31.785 -7.245  -9.845  1.00 22.94 ?  387 HOH   A O    1 
HETATM 6604 O  O    . HOH   E 4 .   ? 30.645 1.920   16.722  1.00 21.80 ?  388 HOH   A O    1 
HETATM 6605 O  O    . HOH   E 4 .   ? 15.240 -21.540 14.252  1.00 18.98 ?  389 HOH   A O    1 
HETATM 6606 O  O    . HOH   E 4 .   ? 16.525 -22.108 1.033   1.00 28.67 ?  390 HOH   A O    1 
HETATM 6607 O  O    . HOH   E 4 .   ? 20.068 4.532   -7.560  1.00 23.39 ?  391 HOH   A O    1 
HETATM 6608 O  O    . HOH   E 4 .   ? 13.949 -4.888  17.465  1.00 26.93 ?  392 HOH   A O    1 
HETATM 6609 O  O    . HOH   E 4 .   ? 16.225 16.608  8.673   1.00 34.74 ?  393 HOH   A O    1 
HETATM 6610 O  O    . HOH   E 4 .   ? 23.441 11.390  4.091   1.00 12.68 ?  394 HOH   A O    1 
HETATM 6611 O  O    . HOH   E 4 .   ? 26.913 4.146   -0.657  1.00 13.39 ?  395 HOH   A O    1 
HETATM 6612 O  O    . HOH   E 4 .   ? 21.329 3.060   -0.281  1.00 13.87 ?  396 HOH   A O    1 
HETATM 6613 O  O    . HOH   E 4 .   ? 23.958 -20.300 -1.302  1.00 17.33 ?  397 HOH   A O    1 
HETATM 6614 O  O    . HOH   E 4 .   ? 37.583 -2.029  5.840   1.00 27.20 ?  398 HOH   A O    1 
HETATM 6615 O  O    . HOH   E 4 .   ? 15.815 2.104   24.757  1.00 48.92 ?  399 HOH   A O    1 
HETATM 6616 O  O    . HOH   E 4 .   ? 6.434  -5.565  11.150  1.00 21.14 ?  400 HOH   A O    1 
HETATM 6617 O  O    B HOH   E 4 .   ? 14.652 -4.332  3.511   0.32 16.20 ?  401 HOH   A O    1 
HETATM 6618 O  O    . HOH   E 4 .   ? 6.708  -3.354  12.900  1.00 32.60 ?  402 HOH   A O    1 
HETATM 6619 O  O    . HOH   E 4 .   ? 14.113 -23.049 7.448   1.00 19.60 ?  403 HOH   A O    1 
HETATM 6620 O  O    . HOH   E 4 .   ? 20.560 -20.046 2.836   1.00 19.27 ?  404 HOH   A O    1 
HETATM 6621 O  O    . HOH   E 4 .   ? 32.768 -9.289  5.927   1.00 19.57 ?  405 HOH   A O    1 
HETATM 6622 O  O    . HOH   E 4 .   ? 30.072 -10.063 12.996  1.00 22.16 ?  406 HOH   A O    1 
HETATM 6623 O  O    A HOH   E 4 .   ? 15.795 -0.960  5.292   0.68 27.52 ?  407 HOH   A O    1 
HETATM 6624 O  O    A HOH   E 4 .   ? 14.451 -0.461  -12.015 0.68 22.65 ?  408 HOH   A O    1 
HETATM 6625 O  O    . HOH   E 4 .   ? 27.378 -6.076  -13.984 1.00 36.10 ?  409 HOH   A O    1 
HETATM 6626 O  O    . HOH   E 4 .   ? 15.409 11.843  7.929   1.00 42.07 ?  410 HOH   A O    1 
HETATM 6627 O  O    B HOH   E 4 .   ? 11.858 -2.057  -3.357  0.32 13.12 ?  411 HOH   A O    1 
HETATM 6628 O  O    . HOH   E 4 .   ? 27.335 2.330   18.743  1.00 34.56 ?  412 HOH   A O    1 
HETATM 6629 O  O    . HOH   E 4 .   ? 30.331 -12.910 13.557  1.00 21.04 ?  413 HOH   A O    1 
HETATM 6630 O  O    . HOH   E 4 .   ? 41.604 1.450   4.942   1.00 36.87 ?  414 HOH   A O    1 
HETATM 6631 O  O    . HOH   E 4 .   ? 16.036 6.938   2.972   1.00 19.06 ?  415 HOH   A O    1 
HETATM 6632 O  O    . HOH   E 4 .   ? 32.648 -4.345  -9.894  1.00 29.42 ?  416 HOH   A O    1 
HETATM 6633 O  O    . HOH   E 4 .   ? 27.879 0.806   -7.167  1.00 14.82 ?  417 HOH   A O    1 
HETATM 6634 O  O    . HOH   E 4 .   ? 38.094 -1.366  -1.984  1.00 20.14 ?  418 HOH   A O    1 
HETATM 6635 O  O    . HOH   E 4 .   ? 30.869 6.221   -12.336 1.00 31.29 ?  419 HOH   A O    1 
HETATM 6636 O  O    . HOH   E 4 .   ? 22.651 8.169   18.341  1.00 47.35 ?  420 HOH   A O    1 
HETATM 6637 O  O    . HOH   E 4 .   ? 35.081 -5.227  -3.092  1.00 18.39 ?  421 HOH   A O    1 
HETATM 6638 O  O    . HOH   E 4 .   ? 5.211  2.660   5.156   1.00 31.18 ?  422 HOH   A O    1 
HETATM 6639 O  O    . HOH   E 4 .   ? 10.388 -13.804 -1.688  1.00 17.20 ?  423 HOH   A O    1 
HETATM 6640 O  O    . HOH   E 4 .   ? 23.986 3.931   -4.868  1.00 23.22 ?  424 HOH   A O    1 
HETATM 6641 O  O    . HOH   E 4 .   ? 40.922 -8.219  -6.774  1.00 37.07 ?  425 HOH   A O    1 
HETATM 6642 O  O    . HOH   E 4 .   ? 36.738 -4.961  5.386   1.00 25.78 ?  426 HOH   A O    1 
HETATM 6643 O  O    . HOH   E 4 .   ? 21.758 -13.899 -8.079  1.00 49.47 ?  427 HOH   A O    1 
HETATM 6644 O  O    . HOH   E 4 .   ? 32.540 -10.664 3.270   1.00 31.86 ?  428 HOH   A O    1 
HETATM 6645 O  O    . HOH   E 4 .   ? 21.330 -9.173  21.369  1.00 52.92 ?  429 HOH   A O    1 
HETATM 6646 O  O    A HOH   E 4 .   ? 11.057 -0.400  1.963   0.68 24.34 ?  430 HOH   A O    1 
HETATM 6647 O  O    . HOH   E 4 .   ? 45.018 -0.594  2.943   1.00 46.45 ?  431 HOH   A O    1 
HETATM 6648 O  O    . HOH   E 4 .   ? 16.246 -14.230 20.252  1.00 54.13 ?  432 HOH   A O    1 
HETATM 6649 O  O    A HOH   E 4 .   ? 18.846 2.021   -0.734  0.68 12.22 ?  433 HOH   A O    1 
HETATM 6650 O  O    . HOH   E 4 .   ? 27.103 -3.134  19.363  1.00 35.17 ?  434 HOH   A O    1 
HETATM 6651 O  O    . HOH   E 4 .   ? 23.193 7.642   -3.223  1.00 29.04 ?  435 HOH   A O    1 
HETATM 6652 O  O    . HOH   E 4 .   ? 23.547 -8.002  17.110  1.00 22.05 ?  436 HOH   A O    1 
HETATM 6653 O  O    . HOH   E 4 .   ? 18.563 4.948   -15.087 1.00 51.90 ?  437 HOH   A O    1 
HETATM 6654 O  O    . HOH   E 4 .   ? 23.398 -20.959 1.342   1.00 19.96 ?  438 HOH   A O    1 
HETATM 6655 O  O    . HOH   E 4 .   ? 37.734 -8.800  -3.396  1.00 22.85 ?  439 HOH   A O    1 
HETATM 6656 O  O    B HOH   E 4 .   ? 14.610 -1.151  -12.493 0.32 23.21 ?  440 HOH   A O    1 
HETATM 6657 O  O    . HOH   E 4 .   ? 34.421 -8.086  -0.518  1.00 29.40 ?  441 HOH   A O    1 
HETATM 6658 O  O    . HOH   E 4 .   ? 20.582 -17.711 24.873  1.00 53.46 ?  442 HOH   A O    1 
HETATM 6659 O  O    . HOH   E 4 .   ? 31.358 -12.815 0.049   1.00 20.92 ?  443 HOH   A O    1 
HETATM 6660 O  O    . HOH   E 4 .   ? 30.544 14.766  2.753   1.00 19.25 ?  444 HOH   A O    1 
HETATM 6661 O  O    A HOH   E 4 .   ? 16.240 2.933   -1.420  0.68 16.47 ?  445 HOH   A O    1 
HETATM 6662 O  O    . HOH   E 4 .   ? -1.370 -4.079  7.656   1.00 60.41 ?  446 HOH   A O    1 
HETATM 6663 O  O    . HOH   E 4 .   ? 18.426 -16.054 16.351  1.00 41.25 ?  447 HOH   A O    1 
HETATM 6664 O  O    . HOH   E 4 .   ? 9.480  -16.359 -2.003  1.00 45.93 ?  448 HOH   A O    1 
HETATM 6665 O  O    B HOH   E 4 .   ? 14.643 -7.938  -9.905  0.32 25.35 ?  449 HOH   A O    1 
HETATM 6666 O  O    B HOH   E 4 .   ? 18.740 1.545   -0.364  0.32 14.59 ?  450 HOH   A O    1 
HETATM 6667 O  O    A HOH   E 4 .   ? 14.019 -0.355  3.486   0.68 21.56 ?  451 HOH   A O    1 
HETATM 6668 O  O    . HOH   E 4 .   ? 21.622 -14.814 17.906  1.00 57.72 ?  452 HOH   A O    1 
HETATM 6669 O  O    . HOH   E 4 .   ? 29.874 -16.102 10.781  1.00 34.99 ?  453 HOH   A O    1 
HETATM 6670 O  O    . HOH   E 4 .   ? 29.758 -1.990  -12.706 1.00 48.71 ?  454 HOH   A O    1 
HETATM 6671 O  O    . HOH   E 4 .   ? 19.848 -17.364 -5.058  1.00 25.00 ?  455 HOH   A O    1 
HETATM 6672 O  O    . HOH   E 4 .   ? 32.503 -15.969 10.871  1.00 32.04 ?  456 HOH   A O    1 
HETATM 6673 O  O    . HOH   E 4 .   ? 25.355 8.225   -4.828  1.00 26.08 ?  457 HOH   A O    1 
HETATM 6674 O  O    . HOH   E 4 .   ? 27.733 7.027   -6.531  1.00 36.77 ?  458 HOH   A O    1 
HETATM 6675 O  O    . HOH   E 4 .   ? 23.195 -22.279 -3.361  1.00 38.58 ?  459 HOH   A O    1 
HETATM 6676 O  O    . HOH   E 4 .   ? 24.869 5.660   20.751  1.00 52.05 ?  460 HOH   A O    1 
HETATM 6677 O  O    . HOH   E 4 .   ? 12.015 -13.372 16.451  1.00 51.24 ?  461 HOH   A O    1 
HETATM 6678 O  O    . HOH   E 4 .   ? 24.599 14.622  7.837   1.00 38.70 ?  462 HOH   A O    1 
HETATM 6679 O  O    . HOH   E 4 .   ? 21.920 5.189   -6.069  1.00 33.75 ?  463 HOH   A O    1 
HETATM 6680 O  O    . HOH   E 4 .   ? 15.745 -21.500 3.722   1.00 24.62 ?  464 HOH   A O    1 
HETATM 6681 O  O    . HOH   E 4 .   ? 18.776 10.897  11.299  1.00 32.92 ?  465 HOH   A O    1 
HETATM 6682 O  O    . HOH   E 4 .   ? 39.625 -7.032  -3.492  1.00 48.45 ?  466 HOH   A O    1 
HETATM 6683 O  O    . HOH   E 4 .   ? 26.926 11.656  -1.306  1.00 31.35 ?  467 HOH   A O    1 
HETATM 6684 O  O    . HOH   E 4 .   ? 23.447 13.707  5.530   1.00 19.16 ?  468 HOH   A O    1 
HETATM 6685 O  O    . HOH   E 4 .   ? 12.328 1.717   17.316  1.00 41.34 ?  469 HOH   A O    1 
HETATM 6686 O  O    . HOH   E 4 .   ? 25.819 10.785  -3.645  1.00 24.71 ?  470 HOH   A O    1 
HETATM 6687 O  O    . HOH   E 4 .   ? 27.582 -11.339 16.587  1.00 39.09 ?  471 HOH   A O    1 
HETATM 6688 O  O    . HOH   E 4 .   ? 10.968 -15.019 -6.072  1.00 35.85 ?  472 HOH   A O    1 
HETATM 6689 O  O    . HOH   E 4 .   ? 28.805 8.973   17.473  1.00 36.86 ?  473 HOH   A O    1 
HETATM 6690 O  O    . HOH   E 4 .   ? 16.847 -20.525 16.163  1.00 30.00 ?  474 HOH   A O    1 
HETATM 6691 O  O    . HOH   E 4 .   ? 35.107 7.486   12.205  1.00 49.59 ?  475 HOH   A O    1 
HETATM 6692 O  O    . HOH   E 4 .   ? 23.176 11.893  -3.984  1.00 20.59 ?  476 HOH   A O    1 
HETATM 6693 O  O    . HOH   E 4 .   ? 18.152 -16.291 -8.802  1.00 43.29 ?  477 HOH   A O    1 
HETATM 6694 O  O    . HOH   E 4 .   ? 40.928 -3.964  -0.405  1.00 40.42 ?  478 HOH   A O    1 
HETATM 6695 O  O    . HOH   E 4 .   ? 17.399 -18.746 19.774  1.00 51.55 ?  479 HOH   A O    1 
HETATM 6696 O  O    . HOH   E 4 .   ? 30.878 0.735   19.174  1.00 42.02 ?  480 HOH   A O    1 
HETATM 6697 O  O    . HOH   E 4 .   ? 15.709 -17.190 -6.939  1.00 31.92 ?  481 HOH   A O    1 
HETATM 6698 O  O    B HOH   E 4 .   ? 10.382 -1.695  -5.413  0.32 20.15 ?  482 HOH   A O    1 
HETATM 6699 O  O    . HOH   E 4 .   ? 44.443 10.469  -1.649  1.00 32.63 ?  483 HOH   A O    1 
HETATM 6700 O  O    . HOH   E 4 .   ? 31.416 -0.596  -10.627 1.00 28.53 ?  484 HOH   A O    1 
HETATM 6701 O  O    . HOH   E 4 .   ? 41.688 9.381   -4.000  1.00 31.43 ?  485 HOH   A O    1 
HETATM 6702 O  O    . HOH   E 4 .   ? 18.467 -23.205 2.023   1.00 50.73 ?  486 HOH   A O    1 
HETATM 6703 O  O    . HOH   E 4 .   ? 13.966 -10.279 -10.953 1.00 35.95 ?  487 HOH   A O    1 
HETATM 6704 O  O    . HOH   E 4 .   ? 23.272 -12.956 19.301  1.00 56.13 ?  488 HOH   A O    1 
HETATM 6705 O  O    . HOH   E 4 .   ? 39.190 2.404   7.483   1.00 32.30 ?  489 HOH   A O    1 
HETATM 6706 O  O    . HOH   E 4 .   ? 28.563 -4.724  -12.310 1.00 38.83 ?  490 HOH   A O    1 
HETATM 6707 O  O    . HOH   E 4 .   ? 20.082 -22.362 4.311   1.00 31.93 ?  491 HOH   A O    1 
HETATM 6708 O  O    . HOH   E 4 .   ? 15.961 -6.918  -11.795 1.00 44.73 ?  492 HOH   A O    1 
HETATM 6709 O  O    B HOH   E 4 .   ? 5.906  -2.087  -6.096  0.32 23.28 ?  493 HOH   A O    1 
HETATM 6710 O  O    . HOH   E 4 .   ? 25.729 -18.900 -11.892 1.00 38.71 ?  494 HOH   A O    1 
HETATM 6711 O  O    . HOH   E 4 .   ? 13.997 -25.264 8.928   1.00 35.47 ?  495 HOH   A O    1 
HETATM 6712 O  O    . HOH   E 4 .   ? 40.532 -0.267  -7.860  1.00 34.77 ?  496 HOH   A O    1 
HETATM 6713 O  O    . HOH   E 4 .   ? 28.712 -7.894  -15.282 1.00 48.07 ?  497 HOH   A O    1 
HETATM 6714 O  O    . HOH   E 4 .   ? 8.142  -3.143  -5.725  1.00 57.25 ?  498 HOH   A O    1 
HETATM 6715 O  O    . HOH   E 4 .   ? 20.541 -16.020 -7.380  1.00 30.84 ?  499 HOH   A O    1 
HETATM 6716 O  O    . HOH   E 4 .   ? 16.207 -23.387 5.784   1.00 30.97 ?  500 HOH   A O    1 
HETATM 6717 O  O    . HOH   E 4 .   ? 30.742 -5.855  -11.871 1.00 49.81 ?  501 HOH   A O    1 
HETATM 6718 O  O    . HOH   E 4 .   ? 30.752 5.778   -14.752 1.00 36.58 ?  502 HOH   A O    1 
HETATM 6719 O  O    . HOH   E 4 .   ? 23.207 -23.805 1.619   1.00 34.01 ?  503 HOH   A O    1 
HETATM 6720 O  O    . HOH   E 4 .   ? 37.452 -6.622  7.593   1.00 26.00 ?  504 HOH   A O    1 
HETATM 6721 O  O    . HOH   E 4 .   ? 39.548 -0.041  6.591   1.00 30.50 ?  505 HOH   A O    1 
HETATM 6722 O  O    . HOH   E 4 .   ? 28.942 14.438  0.840   1.00 52.59 ?  506 HOH   A O    1 
HETATM 6723 O  O    . HOH   E 4 .   ? 37.993 13.933  6.694   1.00 53.48 ?  507 HOH   A O    1 
HETATM 6724 O  O    B HOH   E 4 .   ? 14.698 8.255   5.074   0.32 19.54 ?  508 HOH   A O    1 
HETATM 6725 O  O    . HOH   E 4 .   ? 36.430 -6.532  10.181  1.00 48.72 ?  509 HOH   A O    1 
HETATM 6726 O  O    . HOH   E 4 .   ? 22.039 -24.040 4.535   1.00 28.03 ?  510 HOH   A O    1 
HETATM 6727 O  O    . HOH   E 4 .   ? 17.329 -6.947  -14.157 1.00 42.35 ?  511 HOH   A O    1 
HETATM 6728 O  O    A HOH   E 4 .   ? 14.836 8.635   4.912   0.68 37.26 ?  512 HOH   A O    1 
HETATM 6729 O  O    . HOH   E 4 .   ? 24.044 9.003   -7.260  1.00 36.43 ?  513 HOH   A O    1 
HETATM 6730 O  O    . HOH   E 4 .   ? 16.314 -21.185 18.819  1.00 39.70 ?  514 HOH   A O    1 
HETATM 6731 O  O    . HOH   E 4 .   ? 15.796 -12.366 27.516  1.00 47.39 ?  515 HOH   A O    1 
HETATM 6732 O  O    . HOH   E 4 .   ? 14.687 -22.755 19.859  1.00 34.91 ?  516 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 4 .   ? 29.877 -22.435 5.544   1.00 19.77 ?  201 HOH   B O    1 
HETATM 6734 O  O    . HOH   F 4 .   ? 27.681 -29.175 -1.875  1.00 38.10 ?  202 HOH   B O    1 
HETATM 6735 O  O    . HOH   F 4 .   ? 41.641 -36.040 -17.247 1.00 34.35 ?  203 HOH   B O    1 
HETATM 6736 O  O    . HOH   F 4 .   ? 27.907 -41.829 -15.124 1.00 37.36 ?  204 HOH   B O    1 
HETATM 6737 O  O    . HOH   F 4 .   ? 30.023 -26.294 4.157   1.00 27.35 ?  205 HOH   B O    1 
HETATM 6738 O  O    . HOH   F 4 .   ? 38.114 -39.450 -0.198  1.00 42.89 ?  206 HOH   B O    1 
HETATM 6739 O  O    . HOH   F 4 .   ? 41.333 -7.825  5.467   1.00 40.38 ?  207 HOH   B O    1 
HETATM 6740 O  O    . HOH   F 4 .   ? 59.157 -18.724 6.805   1.00 38.23 ?  208 HOH   B O    1 
HETATM 6741 O  O    . HOH   F 4 .   ? 48.102 -6.893  15.524  1.00 30.25 ?  209 HOH   B O    1 
HETATM 6742 O  O    . HOH   F 4 .   ? 54.485 -9.434  -8.763  1.00 19.76 ?  210 HOH   B O    1 
HETATM 6743 O  O    . HOH   F 4 .   ? 58.232 -12.939 8.355   1.00 31.28 ?  211 HOH   B O    1 
HETATM 6744 O  O    . HOH   F 4 .   ? 52.982 -13.425 -20.289 1.00 34.72 ?  212 HOH   B O    1 
HETATM 6745 O  O    . HOH   F 4 .   ? 50.209 -3.355  7.109   1.00 35.00 ?  213 HOH   B O    1 
HETATM 6746 O  O    . HOH   F 4 .   ? 49.386 -22.714 -19.803 1.00 49.53 ?  214 HOH   B O    1 
HETATM 6747 O  O    . HOH   F 4 .   ? 30.208 -40.974 -8.101  1.00 17.45 ?  215 HOH   B O    1 
HETATM 6748 O  O    . HOH   F 4 .   ? 57.740 -24.429 5.070   1.00 38.00 ?  216 HOH   B O    1 
HETATM 6749 O  O    . HOH   F 4 .   ? 55.416 -16.527 -14.396 1.00 34.78 ?  217 HOH   B O    1 
HETATM 6750 O  O    . HOH   F 4 .   ? 50.789 -6.099  0.152   1.00 27.60 ?  218 HOH   B O    1 
HETATM 6751 O  O    . HOH   F 4 .   ? 56.696 -30.743 -7.793  1.00 29.02 ?  219 HOH   B O    1 
HETATM 6752 O  O    . HOH   F 4 .   ? 56.452 -19.772 6.981   1.00 30.18 ?  220 HOH   B O    1 
HETATM 6753 O  O    . HOH   F 4 .   ? 48.520 -36.515 -15.566 1.00 46.66 ?  221 HOH   B O    1 
HETATM 6754 O  O    . HOH   F 4 .   ? 41.516 -39.172 -14.941 1.00 22.73 ?  222 HOH   B O    1 
HETATM 6755 O  O    . HOH   F 4 .   ? 31.016 -28.774 4.416   1.00 29.44 ?  223 HOH   B O    1 
HETATM 6756 O  O    . HOH   F 4 .   ? 44.949 -43.547 -10.616 1.00 28.83 ?  224 HOH   B O    1 
HETATM 6757 O  O    . HOH   F 4 .   ? 34.546 -36.385 -7.201  1.00 19.25 ?  225 HOH   B O    1 
HETATM 6758 O  O    . HOH   F 4 .   ? 44.484 -7.047  1.966   1.00 36.08 ?  226 HOH   B O    1 
HETATM 6759 O  O    . HOH   F 4 .   ? 57.159 -26.864 -7.653  1.00 39.96 ?  227 HOH   B O    1 
HETATM 6760 O  O    . HOH   F 4 .   ? 47.392 -7.293  -3.830  1.00 41.78 ?  228 HOH   B O    1 
HETATM 6761 O  O    . HOH   F 4 .   ? 40.588 -16.096 14.074  1.00 24.87 ?  229 HOH   B O    1 
HETATM 6762 O  O    . HOH   F 4 .   ? 57.407 -16.281 -12.259 1.00 18.95 ?  230 HOH   B O    1 
HETATM 6763 O  O    . HOH   F 4 .   ? 32.748 -43.743 -11.385 1.00 22.81 ?  231 HOH   B O    1 
HETATM 6764 O  O    . HOH   F 4 .   ? 25.435 -25.914 -1.277  1.00 34.90 ?  232 HOH   B O    1 
HETATM 6765 O  O    . HOH   F 4 .   ? 41.436 -9.624  13.066  1.00 22.58 ?  233 HOH   B O    1 
HETATM 6766 O  O    . HOH   F 4 .   ? 37.081 -19.684 -18.154 1.00 44.14 ?  234 HOH   B O    1 
HETATM 6767 O  O    . HOH   F 4 .   ? 45.204 -34.966 6.844   1.00 39.55 ?  235 HOH   B O    1 
HETATM 6768 O  O    . HOH   F 4 .   ? 39.361 -10.868 6.128   1.00 26.39 ?  236 HOH   B O    1 
HETATM 6769 O  O    . HOH   F 4 .   ? 51.704 -6.499  4.342   1.00 20.37 ?  237 HOH   B O    1 
HETATM 6770 O  O    . HOH   F 4 .   ? 50.786 -12.969 -0.500  1.00 12.61 ?  238 HOH   B O    1 
HETATM 6771 O  O    . HOH   F 4 .   ? 43.049 -43.239 -8.266  1.00 30.53 ?  239 HOH   B O    1 
HETATM 6772 O  O    . HOH   F 4 .   ? 35.108 -7.989  -2.989  1.00 18.92 ?  240 HOH   B O    1 
HETATM 6773 O  O    . HOH   F 4 .   ? 42.678 -22.853 3.855   1.00 12.03 ?  241 HOH   B O    1 
HETATM 6774 O  O    . HOH   F 4 .   ? 46.424 -1.555  13.207  1.00 30.10 ?  242 HOH   B O    1 
HETATM 6775 O  O    . HOH   F 4 .   ? 34.965 -24.632 13.845  1.00 35.35 ?  243 HOH   B O    1 
HETATM 6776 O  O    . HOH   F 4 .   ? 43.107 -32.374 -17.131 1.00 24.98 ?  244 HOH   B O    1 
HETATM 6777 O  O    . HOH   F 4 .   ? 29.870 -34.194 -0.423  1.00 35.35 ?  245 HOH   B O    1 
HETATM 6778 O  O    . HOH   F 4 .   ? 57.670 -24.358 -3.855  1.00 20.36 ?  246 HOH   B O    1 
HETATM 6779 O  O    . HOH   F 4 .   ? 28.401 -19.667 -13.110 1.00 25.23 ?  247 HOH   B O    1 
HETATM 6780 O  O    . HOH   F 4 .   ? 51.624 -13.847 10.955  1.00 27.78 ?  248 HOH   B O    1 
HETATM 6781 O  O    . HOH   F 4 .   ? 39.543 -11.122 0.331   1.00 17.15 ?  249 HOH   B O    1 
HETATM 6782 O  O    . HOH   F 4 .   ? 58.204 -10.666 -4.074  1.00 20.09 ?  250 HOH   B O    1 
HETATM 6783 O  O    . HOH   F 4 .   ? 42.610 -25.370 2.645   1.00 15.55 ?  251 HOH   B O    1 
HETATM 6784 O  O    . HOH   F 4 .   ? 44.567 -27.805 -0.733  1.00 22.22 ?  252 HOH   B O    1 
HETATM 6785 O  O    . HOH   F 4 .   ? 31.773 -17.873 -14.447 1.00 30.49 ?  253 HOH   B O    1 
HETATM 6786 O  O    . HOH   F 4 .   ? 42.804 -20.256 -20.704 1.00 38.86 ?  254 HOH   B O    1 
HETATM 6787 O  O    . HOH   F 4 .   ? 38.488 -11.060 -2.234  1.00 19.37 ?  255 HOH   B O    1 
HETATM 6788 O  O    . HOH   F 4 .   ? 40.354 -12.741 -11.520 1.00 15.61 ?  256 HOH   B O    1 
HETATM 6789 O  O    . HOH   F 4 .   ? 28.480 -30.814 -14.799 1.00 29.90 ?  257 HOH   B O    1 
HETATM 6790 O  O    . HOH   F 4 .   ? 34.319 -18.430 11.487  1.00 25.43 ?  258 HOH   B O    1 
HETATM 6791 O  O    . HOH   F 4 .   ? 41.927 -23.512 9.309   1.00 18.77 ?  259 HOH   B O    1 
HETATM 6792 O  O    . HOH   F 4 .   ? 38.975 -11.957 12.320  1.00 34.90 ?  260 HOH   B O    1 
HETATM 6793 O  O    . HOH   F 4 .   ? 34.911 -33.183 -19.286 1.00 33.25 ?  261 HOH   B O    1 
HETATM 6794 O  O    . HOH   F 4 .   ? 46.880 -29.576 9.798   1.00 31.11 ?  262 HOH   B O    1 
HETATM 6795 O  O    . HOH   F 4 .   ? 33.565 -16.985 8.118   1.00 19.41 ?  263 HOH   B O    1 
HETATM 6796 O  O    . HOH   F 4 .   ? 30.889 -15.750 2.712   1.00 14.20 ?  264 HOH   B O    1 
HETATM 6797 O  O    . HOH   F 4 .   ? 36.002 -43.393 -8.467  1.00 41.96 ?  265 HOH   B O    1 
HETATM 6798 O  O    . HOH   F 4 .   ? 29.734 -25.193 -10.773 1.00 17.43 ?  266 HOH   B O    1 
HETATM 6799 O  O    . HOH   F 4 .   ? 48.084 -22.800 5.825   1.00 17.75 ?  267 HOH   B O    1 
HETATM 6800 O  O    . HOH   F 4 .   ? 57.012 -8.654  8.361   1.00 19.99 ?  268 HOH   B O    1 
HETATM 6801 O  O    . HOH   F 4 .   ? 42.394 -9.903  9.340   1.00 21.11 ?  269 HOH   B O    1 
HETATM 6802 O  O    . HOH   F 4 .   ? 27.136 -31.806 -9.968  1.00 21.54 ?  270 HOH   B O    1 
HETATM 6803 O  O    . HOH   F 4 .   ? 57.502 -9.227  1.340   1.00 20.22 ?  271 HOH   B O    1 
HETATM 6804 O  O    . HOH   F 4 .   ? 57.207 -12.106 12.246  1.00 37.32 ?  272 HOH   B O    1 
HETATM 6805 O  O    . HOH   F 4 .   ? 50.996 -39.939 -8.341  1.00 35.92 ?  273 HOH   B O    1 
HETATM 6806 O  O    . HOH   F 4 .   ? 49.299 -28.722 -6.953  1.00 16.18 ?  274 HOH   B O    1 
HETATM 6807 O  O    . HOH   F 4 .   ? 43.389 -15.793 -12.192 1.00 14.73 ?  275 HOH   B O    1 
HETATM 6808 O  O    . HOH   F 4 .   ? 34.515 -12.806 2.690   1.00 24.53 ?  276 HOH   B O    1 
HETATM 6809 O  O    . HOH   F 4 .   ? 28.276 -34.324 -9.399  1.00 19.67 ?  277 HOH   B O    1 
HETATM 6810 O  O    . HOH   F 4 .   ? 56.184 -23.502 -14.787 1.00 26.94 ?  278 HOH   B O    1 
HETATM 6811 O  O    . HOH   F 4 .   ? 49.763 -0.476  10.172  1.00 33.83 ?  279 HOH   B O    1 
HETATM 6812 O  O    . HOH   F 4 .   ? 41.230 -5.481  11.488  1.00 46.46 ?  280 HOH   B O    1 
HETATM 6813 O  O    . HOH   F 4 .   ? 42.473 -34.696 3.804   1.00 25.45 ?  281 HOH   B O    1 
HETATM 6814 O  O    . HOH   F 4 .   ? 27.971 -22.890 -7.939  1.00 17.92 ?  282 HOH   B O    1 
HETATM 6815 O  O    . HOH   F 4 .   ? 48.434 -25.060 3.088   1.00 14.08 ?  283 HOH   B O    1 
HETATM 6816 O  O    . HOH   F 4 .   ? 30.443 -42.286 -10.620 1.00 30.23 ?  284 HOH   B O    1 
HETATM 6817 O  O    . HOH   F 4 .   ? 27.567 -26.668 -15.629 1.00 36.02 ?  285 HOH   B O    1 
HETATM 6818 O  O    . HOH   F 4 .   ? 48.758 -20.015 5.912   1.00 14.32 ?  286 HOH   B O    1 
HETATM 6819 O  O    . HOH   F 4 .   ? 46.611 -31.231 -4.845  1.00 25.98 ?  287 HOH   B O    1 
HETATM 6820 O  O    . HOH   F 4 .   ? 52.592 -10.387 12.954  1.00 23.56 ?  288 HOH   B O    1 
HETATM 6821 O  O    . HOH   F 4 .   ? 59.843 -15.346 8.133   1.00 31.95 ?  289 HOH   B O    1 
HETATM 6822 O  O    . HOH   F 4 .   ? 43.643 -15.413 18.143  1.00 31.51 ?  290 HOH   B O    1 
HETATM 6823 O  O    . HOH   F 4 .   ? 33.519 -15.270 -13.934 1.00 21.46 ?  291 HOH   B O    1 
HETATM 6824 O  O    . HOH   F 4 .   ? 35.165 -33.694 4.572   1.00 31.20 ?  292 HOH   B O    1 
HETATM 6825 O  O    . HOH   F 4 .   ? 36.831 -12.751 -1.484  1.00 27.56 ?  293 HOH   B O    1 
HETATM 6826 O  O    . HOH   F 4 .   ? 42.387 -9.846  -14.877 1.00 40.22 ?  294 HOH   B O    1 
HETATM 6827 O  O    . HOH   F 4 .   ? 47.868 -24.449 -17.901 1.00 34.12 ?  295 HOH   B O    1 
HETATM 6828 O  O    . HOH   F 4 .   ? 47.087 -33.961 -4.675  1.00 18.87 ?  296 HOH   B O    1 
HETATM 6829 O  O    . HOH   F 4 .   ? 45.318 -33.351 -16.049 1.00 23.89 ?  297 HOH   B O    1 
HETATM 6830 O  O    . HOH   F 4 .   ? 51.227 -37.565 -9.714  1.00 26.43 ?  298 HOH   B O    1 
HETATM 6831 O  O    . HOH   F 4 .   ? 37.542 -18.046 13.140  1.00 31.06 ?  299 HOH   B O    1 
HETATM 6832 O  O    . HOH   F 4 .   ? 52.504 -29.244 -13.081 1.00 24.41 ?  300 HOH   B O    1 
HETATM 6833 O  O    . HOH   F 4 .   ? 44.645 -27.483 2.001   1.00 16.23 ?  301 HOH   B O    1 
HETATM 6834 O  O    . HOH   F 4 .   ? 40.234 -10.824 -9.493  1.00 17.49 ?  302 HOH   B O    1 
HETATM 6835 O  O    . HOH   F 4 .   ? 42.677 -12.262 -18.507 1.00 28.70 ?  303 HOH   B O    1 
HETATM 6836 O  O    . HOH   F 4 .   ? 52.606 -35.633 -8.754  1.00 31.97 ?  304 HOH   B O    1 
HETATM 6837 O  O    . HOH   F 4 .   ? 51.712 -5.923  -7.927  1.00 43.15 ?  305 HOH   B O    1 
HETATM 6838 O  O    . HOH   F 4 .   ? 45.894 -40.414 -3.650  1.00 31.28 ?  306 HOH   B O    1 
HETATM 6839 O  O    . HOH   F 4 .   ? 50.070 -24.610 5.899   1.00 36.68 ?  307 HOH   B O    1 
HETATM 6840 O  O    . HOH   F 4 .   ? 53.491 -30.219 4.484   1.00 18.71 ?  308 HOH   B O    1 
HETATM 6841 O  O    . HOH   F 4 .   ? 25.951 -21.486 -3.464  1.00 16.96 ?  309 HOH   B O    1 
HETATM 6842 O  O    . HOH   F 4 .   ? 44.029 -29.373 -4.735  1.00 23.51 ?  310 HOH   B O    1 
HETATM 6843 O  O    . HOH   F 4 .   ? 37.857 -10.213 -10.724 1.00 17.60 ?  311 HOH   B O    1 
HETATM 6844 O  O    . HOH   F 4 .   ? 32.848 -34.603 -5.864  1.00 17.55 ?  312 HOH   B O    1 
HETATM 6845 O  O    . HOH   F 4 .   ? 48.116 -32.660 -16.699 1.00 43.94 ?  313 HOH   B O    1 
HETATM 6846 O  O    . HOH   F 4 .   ? 53.155 -16.058 -12.740 1.00 29.58 ?  314 HOH   B O    1 
HETATM 6847 O  O    . HOH   F 4 .   ? 62.751 -13.564 4.736   1.00 25.85 ?  315 HOH   B O    1 
HETATM 6848 O  O    . HOH   F 4 .   ? 45.684 -36.292 -16.145 1.00 36.49 ?  316 HOH   B O    1 
HETATM 6849 O  O    . HOH   F 4 .   ? 41.780 -8.069  1.380   1.00 25.03 ?  317 HOH   B O    1 
HETATM 6850 O  O    . HOH   F 4 .   ? 37.064 -30.540 -21.052 1.00 31.22 ?  318 HOH   B O    1 
HETATM 6851 O  O    . HOH   F 4 .   ? 43.263 -21.425 10.704  1.00 16.31 ?  319 HOH   B O    1 
HETATM 6852 O  O    . HOH   F 4 .   ? 37.336 -35.672 7.290   1.00 32.61 ?  320 HOH   B O    1 
HETATM 6853 O  O    . HOH   F 4 .   ? 26.343 -21.048 -6.204  1.00 16.72 ?  321 HOH   B O    1 
HETATM 6854 O  O    . HOH   F 4 .   ? 38.375 -12.727 7.932   1.00 18.05 ?  322 HOH   B O    1 
HETATM 6855 O  O    . HOH   F 4 .   ? 59.936 -17.241 -10.552 1.00 35.03 ?  323 HOH   B O    1 
HETATM 6856 O  O    . HOH   F 4 .   ? 53.661 -12.533 -22.255 1.00 38.29 ?  324 HOH   B O    1 
HETATM 6857 O  O    . HOH   F 4 .   ? 44.708 -24.588 9.583   1.00 20.41 ?  325 HOH   B O    1 
HETATM 6858 O  O    . HOH   F 4 .   ? 62.906 -20.156 -0.806  1.00 40.86 ?  326 HOH   B O    1 
HETATM 6859 O  O    . HOH   F 4 .   ? 43.204 -34.551 0.053   1.00 22.88 ?  327 HOH   B O    1 
HETATM 6860 O  O    . HOH   F 4 .   ? 33.721 -31.131 11.111  1.00 37.21 ?  328 HOH   B O    1 
HETATM 6861 O  O    . HOH   F 4 .   ? 44.164 -1.717  7.632   1.00 46.90 ?  329 HOH   B O    1 
HETATM 6862 O  O    . HOH   F 4 .   ? 36.756 -12.406 4.328   1.00 18.42 ?  330 HOH   B O    1 
HETATM 6863 O  O    . HOH   F 4 .   ? 51.422 -33.038 -10.962 1.00 43.44 ?  331 HOH   B O    1 
HETATM 6864 O  O    . HOH   F 4 .   ? 47.273 -24.500 8.171   1.00 24.22 ?  332 HOH   B O    1 
HETATM 6865 O  O    . HOH   F 4 .   ? 57.608 -22.014 3.284   1.00 31.00 ?  333 HOH   B O    1 
HETATM 6866 O  O    . HOH   F 4 .   ? 41.355 -24.512 15.829  1.00 46.08 ?  334 HOH   B O    1 
HETATM 6867 O  O    . HOH   F 4 .   ? 42.889 -43.517 -14.423 1.00 44.37 ?  335 HOH   B O    1 
HETATM 6868 O  O    . HOH   F 4 .   ? 47.500 -27.416 2.011   1.00 15.32 ?  336 HOH   B O    1 
HETATM 6869 O  O    . HOH   F 4 .   ? 48.614 -11.954 -13.977 1.00 27.56 ?  337 HOH   B O    1 
HETATM 6870 O  O    . HOH   F 4 .   ? 38.470 -9.337  -13.281 1.00 33.84 ?  338 HOH   B O    1 
HETATM 6871 O  O    . HOH   F 4 .   ? 37.035 -15.112 -16.574 1.00 42.04 ?  339 HOH   B O    1 
HETATM 6872 O  O    . HOH   F 4 .   ? 38.427 -12.228 -16.272 1.00 46.54 ?  340 HOH   B O    1 
HETATM 6873 O  O    . HOH   F 4 .   ? 27.715 -14.698 -9.528  1.00 41.10 ?  341 HOH   B O    1 
HETATM 6874 O  O    . HOH   F 4 .   ? 37.049 -45.107 -9.781  1.00 36.52 ?  342 HOH   B O    1 
HETATM 6875 O  O    . HOH   F 4 .   ? 46.846 -19.888 12.276  1.00 32.36 ?  343 HOH   B O    1 
HETATM 6876 O  O    . HOH   F 4 .   ? 28.891 -42.841 -12.388 1.00 44.69 ?  344 HOH   B O    1 
HETATM 6877 O  O    . HOH   F 4 .   ? 39.576 -23.552 -20.351 1.00 39.36 ?  345 HOH   B O    1 
HETATM 6878 O  O    . HOH   F 4 .   ? 34.580 -10.325 7.618   1.00 23.24 ?  346 HOH   B O    1 
HETATM 6879 O  O    . HOH   F 4 .   ? 33.028 -14.691 1.079   1.00 20.32 ?  347 HOH   B O    1 
HETATM 6880 O  O    . HOH   F 4 .   ? 39.783 -44.242 -11.238 1.00 42.67 ?  348 HOH   B O    1 
HETATM 6881 O  O    . HOH   F 4 .   ? 33.627 -9.785  -8.778  1.00 31.93 ?  349 HOH   B O    1 
HETATM 6882 O  O    . HOH   F 4 .   ? 38.587 -22.290 15.060  1.00 42.85 ?  350 HOH   B O    1 
HETATM 6883 O  O    . HOH   F 4 .   ? 62.571 -20.111 -4.849  1.00 47.85 ?  351 HOH   B O    1 
HETATM 6884 O  O    . HOH   F 4 .   ? 27.785 -26.625 -0.561  1.00 31.70 ?  352 HOH   B O    1 
HETATM 6885 O  O    . HOH   F 4 .   ? 40.388 -43.490 -9.191  1.00 27.94 ?  353 HOH   B O    1 
HETATM 6886 O  O    . HOH   F 4 .   ? 44.127 -37.348 -17.881 1.00 35.62 ?  354 HOH   B O    1 
HETATM 6887 O  O    . HOH   F 4 .   ? 55.673 -8.229  10.790  1.00 24.52 ?  355 HOH   B O    1 
HETATM 6888 O  O    . HOH   F 4 .   ? 23.266 -23.698 6.839   1.00 36.58 ?  356 HOH   B O    1 
HETATM 6889 O  O    . HOH   F 4 .   ? 33.982 -7.844  11.523  1.00 42.77 ?  357 HOH   B O    1 
HETATM 6890 O  O    . HOH   F 4 .   ? 43.222 -12.728 -21.194 1.00 41.87 ?  358 HOH   B O    1 
HETATM 6891 O  O    . HOH   F 4 .   ? 56.661 -7.284  2.944   1.00 29.41 ?  359 HOH   B O    1 
HETATM 6892 O  O    . HOH   F 4 .   ? 36.117 -8.454  -9.771  1.00 37.28 ?  360 HOH   B O    1 
HETATM 6893 O  O    . HOH   F 4 .   ? 61.551 -19.891 1.633   1.00 35.95 ?  361 HOH   B O    1 
HETATM 6894 O  O    . HOH   F 4 .   ? 56.893 -21.564 -16.471 1.00 41.96 ?  362 HOH   B O    1 
HETATM 6895 O  O    . HOH   F 4 .   ? 40.266 -8.840  9.905   1.00 37.59 ?  363 HOH   B O    1 
HETATM 6896 O  O    . HOH   F 4 .   ? 27.179 -25.929 -11.382 1.00 34.58 ?  364 HOH   B O    1 
HETATM 6897 O  O    . HOH   F 4 .   ? 40.319 -11.280 -13.884 1.00 33.42 ?  365 HOH   B O    1 
HETATM 6898 O  O    . HOH   F 4 .   ? 58.998 -10.520 9.142   1.00 41.03 ?  366 HOH   B O    1 
HETATM 6899 O  O    . HOH   F 4 .   ? 54.235 -5.723  2.896   1.00 39.74 ?  367 HOH   B O    1 
HETATM 6900 O  O    . HOH   F 4 .   ? 48.377 -26.435 8.768   1.00 43.30 ?  368 HOH   B O    1 
HETATM 6901 O  O    . HOH   F 4 .   ? 36.228 -8.712  8.908   1.00 34.15 ?  369 HOH   B O    1 
HETATM 6902 O  O    . HOH   F 4 .   ? 32.568 -23.580 14.063  1.00 44.14 ?  370 HOH   B O    1 
HETATM 6903 O  O    . HOH   F 4 .   ? 39.860 -7.085  7.828   1.00 44.99 ?  371 HOH   B O    1 
HETATM 6904 O  O    . HOH   F 4 .   ? 41.746 -10.075 -17.467 1.00 60.08 ?  372 HOH   B O    1 
HETATM 6905 O  O    . HOH   F 4 .   ? 52.130 -12.891 13.259  1.00 32.48 ?  373 HOH   B O    1 
HETATM 6906 O  O    . HOH   F 4 .   ? 56.031 -7.767  -0.646  1.00 39.27 ?  374 HOH   B O    1 
HETATM 6907 O  O    . HOH   F 4 .   ? 63.095 -12.418 6.930   1.00 38.27 ?  375 HOH   B O    1 
HETATM 6908 O  O    . HOH   F 4 .   ? 38.115 -10.528 10.034  1.00 30.00 ?  376 HOH   B O    1 
HETATM 6909 O  O    . HOH   F 4 .   ? 44.141 -5.627  -3.571  1.00 44.77 ?  377 HOH   B O    1 
HETATM 6910 O  O    . HOH   F 4 .   ? 42.718 -17.186 -23.129 1.00 46.01 ?  378 HOH   B O    1 
HETATM 6911 O  O    . HOH   F 4 .   ? 36.533 -22.857 13.320  1.00 27.62 ?  379 HOH   B O    1 
HETATM 6912 O  O    . HOH   F 4 .   ? 40.186 -7.714  3.134   1.00 42.59 ?  380 HOH   B O    1 
HETATM 6913 O  O    . HOH   F 4 .   ? 41.840 -6.736  -4.883  1.00 49.01 ?  381 HOH   B O    1 
HETATM 6914 O  O    . HOH   F 4 .   ? 39.704 -14.061 15.660  1.00 52.14 ?  382 HOH   B O    1 
HETATM 6915 O  O    . HOH   F 4 .   ? 52.903 -29.903 7.179   1.00 23.08 ?  383 HOH   B O    1 
HETATM 6916 O  O    . HOH   F 4 .   ? 60.533 -22.202 2.871   1.00 51.64 ?  384 HOH   B O    1 
HETATM 6917 O  O    . HOH   F 4 .   ? 46.824 -5.399  2.937   1.00 41.31 ?  385 HOH   B O    1 
HETATM 6918 O  O    . HOH   F 4 .   ? 41.039 -9.697  15.792  1.00 49.93 ?  386 HOH   B O    1 
HETATM 6919 O  O    . HOH   F 4 .   ? 23.914 -20.917 -7.595  1.00 27.82 ?  387 HOH   B O    1 
HETATM 6920 O  O    . HOH   F 4 .   ? 35.455 -33.709 7.394   1.00 42.73 ?  388 HOH   B O    1 
HETATM 6921 O  O    . HOH   F 4 .   ? 35.309 -20.372 13.363  1.00 32.85 ?  389 HOH   B O    1 
HETATM 6922 O  O    . HOH   F 4 .   ? 40.719 -6.639  -0.796  1.00 28.25 ?  390 HOH   B O    1 
HETATM 6923 O  O    . HOH   F 4 .   ? 44.184 -31.778 -3.883  1.00 37.82 ?  391 HOH   B O    1 
HETATM 6924 O  O    . HOH   F 4 .   ? 27.988 -27.071 2.338   1.00 30.22 ?  392 HOH   B O    1 
HETATM 6925 O  O    . HOH   F 4 .   ? 26.635 -27.894 -13.451 1.00 39.26 ?  393 HOH   B O    1 
HETATM 6926 O  O    . HOH   F 4 .   ? 24.616 -20.626 -10.439 1.00 40.17 ?  394 HOH   B O    1 
HETATM 6927 O  O    . HOH   F 4 .   ? 50.650 -30.837 8.677   1.00 29.68 ?  395 HOH   B O    1 
HETATM 6928 O  O    . HOH   F 4 .   ? 26.859 -30.616 -12.675 1.00 27.67 ?  396 HOH   B O    1 
HETATM 6929 O  O    . HOH   F 4 .   ? 34.438 -33.479 9.641   1.00 34.93 ?  397 HOH   B O    1 
HETATM 6930 O  O    . HOH   F 4 .   ? 45.759 -20.167 15.275  1.00 49.86 ?  398 HOH   B O    1 
HETATM 6931 O  O    . HOH   F 4 .   ? 57.649 -6.502  -2.366  1.00 35.24 ?  399 HOH   B O    1 
HETATM 6932 O  O    . HOH   F 4 .   ? 40.832 -11.792 -22.319 1.00 42.51 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.7560 0.7473 0.8418 0.0099  -0.0243 0.0830  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.7506 0.7439 0.8117 0.0057  -0.0228 0.0619  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.7523 0.7440 0.8318 0.0083  -0.0232 0.0831  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.7473 0.7410 0.8048 0.0046  -0.0221 0.0632  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.7318 0.7282 0.8001 0.0030  -0.0237 0.0835  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.7297 0.7265 0.7827 0.0007  -0.0229 0.0721  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.7345 0.7312 0.8147 0.0042  -0.0260 0.0855  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.7332 0.7295 0.7936 0.0011  -0.0246 0.0725  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.7654 0.7534 0.8442 0.0105  -0.0216 0.0826  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.7583 0.7496 0.8137 0.0065  -0.0205 0.0569  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.7701 0.7562 0.8472 0.0120  -0.0218 0.0822  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7621 0.7522 0.8162 0.0076  -0.0203 0.0547  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.7694 0.7568 0.8478 0.0106  -0.0208 0.0830  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7616 0.7525 0.8164 0.0069  -0.0199 0.0551  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.7052 0.7064 0.7413 -0.0038 -0.0208 0.0805  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.6504 0.6611 0.6299 -0.0154 -0.0131 0.0836  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5756 0.6025 0.5545 -0.0307 0.0050  0.0559  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5781 0.6063 0.5557 -0.0319 0.0047  0.0600  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.6653 0.6711 0.5862 -0.0124 -0.0219 0.1127  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.6763 0.6780 0.5466 -0.0103 -0.0322 0.1387  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6819 0.6816 0.5326 -0.0108 -0.0417 0.1464  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6784 0.6787 0.5334 -0.0076 -0.0314 0.1519  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.5309 0.5693 0.5073 -0.0444 0.0206  0.0417  5   SER   A N   
47   N  N   B SER   A 5   ? 0.5399 0.5686 0.5162 -0.0317 0.0096  0.0390  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4829 0.5335 0.4572 -0.0587 0.0415  0.0266  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.5012 0.5327 0.4750 -0.0332 0.0170  0.0231  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.4280 0.4843 0.3952 -0.0683 0.0629  0.0192  5   SER   A C   
51   C  C   B SER   A 5   ? 0.4566 0.4892 0.4214 -0.0328 0.0248  0.0126  5   SER   A C   
52   O  O   A SER   A 5   ? 0.4335 0.4896 0.3864 -0.0610 0.0705  0.0113  5   SER   A O   
53   O  O   B SER   A 5   ? 0.4579 0.4905 0.4183 -0.0312 0.0264  0.0092  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4888 0.5450 0.4778 -0.0628 0.0418  0.0194  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.5060 0.5390 0.4905 -0.0351 0.0173  0.0189  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4916 0.5507 0.4876 -0.0650 0.0430  0.0159  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.5083 0.5424 0.4976 -0.0361 0.0173  0.0166  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3639 0.4287 0.3274 -0.0861 0.0813  0.0232  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.4093 0.4441 0.3680 -0.0341 0.0326  0.0071  6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.3061 0.3699 0.2601 -0.0971 0.0840  0.0420  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3635 0.3984 0.3188 -0.0349 0.0387  0.0055  6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2942 0.3593 0.2678 -0.0991 0.0904  0.0384  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3410 0.3793 0.3125 -0.0358 0.0474  0.0049  6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2958 0.3611 0.2977 -0.1023 0.0975  0.0427  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3418 0.3805 0.3200 -0.0361 0.0512  0.0062  6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2742 0.3266 0.2191 -0.0906 0.0555  0.0544  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.3427 0.3727 0.2862 -0.0325 0.0343  0.0006  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2459 0.2917 0.1947 -0.0800 0.0287  0.0510  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.3234 0.3482 0.2619 -0.0317 0.0302  -0.0020 6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2293 0.2804 0.1902 -0.0755 0.0135  0.0504  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.3146 0.3387 0.2513 -0.0304 0.0256  -0.0009 6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2437 0.2761 0.2146 -0.0666 0.0202  0.0440  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.3180 0.3363 0.2575 -0.0273 0.0310  -0.0053 6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2235 0.2713 0.1938 -0.0693 0.0105  0.0534  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.3105 0.3322 0.2485 -0.0294 0.0288  0.0020  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2352 0.2720 0.2233 -0.0610 0.0142  0.0309  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.3124 0.3289 0.2503 -0.0264 0.0322  -0.0034 6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2294 0.2687 0.2042 -0.0622 0.0059  0.0356  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.3094 0.3280 0.2443 -0.0267 0.0315  -0.0010 6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2806 0.3393 0.2486 -0.0962 0.0871  0.0375  7   SER   A N   
109  N  N   B SER   A 7   ? 0.3176 0.3591 0.3054 -0.0370 0.0502  0.0003  7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2776 0.3294 0.2546 -0.0828 0.0761  0.0245  7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.2979 0.3382 0.3007 -0.0379 0.0539  -0.0009 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2536 0.2951 0.2441 -0.0820 0.0695  0.0143  7   SER   A C   
113  C  C   B SER   A 7   ? 0.2756 0.3151 0.2694 -0.0396 0.0607  0.0033  7   SER   A C   
114  O  O   A SER   A 7   ? 0.2621 0.2862 0.2183 -0.0888 0.0729  0.0189  7   SER   A O   
115  O  O   B SER   A 7   ? 0.2770 0.3139 0.2663 -0.0378 0.0549  -0.0007 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2985 0.3524 0.2688 -0.0689 0.0735  0.0274  7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.3020 0.3395 0.3307 -0.0363 0.0502  -0.0083 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.3180 0.3681 0.3027 -0.0546 0.0610  0.0162  7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.3052 0.3412 0.3573 -0.0344 0.0471  -0.0149 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2289 0.2719 0.2515 -0.0698 0.0583  0.0036  8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2564 0.2948 0.2447 -0.0409 0.0673  0.0058  8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.2144 0.2470 0.2583 -0.0449 0.0555  0.0002  8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2402 0.2744 0.2303 -0.0359 0.0601  0.0076  8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1928 0.2285 0.2447 -0.0296 0.0409  -0.0014 8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2228 0.2564 0.2106 -0.0336 0.0557  0.0133  8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1874 0.2228 0.2604 -0.0126 0.0423  -0.0143 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2209 0.2518 0.2118 -0.0316 0.0578  0.0172  8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1715 0.2127 0.2178 -0.0275 0.0339  0.0186  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.2025 0.2407 0.2000 -0.0305 0.0444  0.0198  9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1547 0.1975 0.1984 -0.0225 0.0322  0.0207  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1830 0.2205 0.1935 -0.0227 0.0281  0.0294  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1516 0.1798 0.2127 -0.0191 0.0249  0.0335  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1767 0.2038 0.1906 -0.0214 0.0222  0.0434  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1676 0.2035 0.2331 -0.0204 0.0170  0.0288  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1715 0.2116 0.2013 -0.0248 0.0093  0.0578  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1575 0.2107 0.1880 -0.0131 0.0294  0.0118  9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1713 0.2211 0.1925 -0.0137 0.0168  0.0215  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1605 0.2160 0.2023 -0.0120 0.0384  -0.0054 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1605 0.2196 0.1781 -0.0049 0.0215  0.0104  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1634 0.2303 0.2098 -0.0285 0.0387  -0.0206 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1637 0.2259 0.1808 -0.0030 0.0253  0.0068  9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1579 0.2072 0.2035 -0.0091 0.0343  0.0034  9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1604 0.2159 0.1673 0.0042  0.0113  0.0047  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1717 0.2331 0.2198 -0.0267 0.0431  -0.0365 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1660 0.2238 0.1862 -0.0022 0.0307  -0.0027 9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1675 0.2152 0.2059 -0.0162 0.0391  -0.0157 9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1659 0.2190 0.1737 0.0026  0.0216  -0.0014 9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1662 0.2275 0.2299 -0.0340 0.0538  -0.0278 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1659 0.2182 0.1883 -0.0021 0.0381  -0.0043 9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1704 0.2371 0.2644 -0.0502 0.0513  -0.0359 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1744 0.2212 0.2123 -0.0090 0.0471  -0.0046 9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1445 0.1627 0.2182 -0.0189 0.0176  0.0283  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1764 0.1864 0.1790 -0.0153 0.0206  0.0431  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1478 0.1642 0.2140 -0.0245 0.0139  0.0409  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1771 0.1807 0.1909 -0.0151 0.0216  0.0286  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1468 0.1596 0.2164 -0.0305 0.0211  0.0371  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1659 0.1737 0.1871 -0.0140 0.0189  0.0298  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1520 0.1473 0.2308 -0.0322 0.0341  0.0404  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1695 0.1712 0.1910 -0.0121 0.0249  0.0334  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1622 0.1735 0.2293 -0.0248 0.0157  0.0524  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1844 0.1762 0.2022 -0.0233 0.0180  0.0197  10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1972 0.1823 0.2830 -0.0125 -0.0118 0.0564  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1991 0.1736 0.2198 -0.0238 0.0102  0.0145  10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.2206 0.1931 0.3249 -0.0138 -0.0074 0.0520  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.2080 0.1797 0.2352 -0.0298 0.0076  0.0120  10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.2149 0.1931 0.2976 -0.0024 0.0033  0.0357  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.2089 0.1802 0.2395 -0.0226 0.0053  0.0079  10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1473 0.1624 0.2076 -0.0354 0.0117  0.0410  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1549 0.1654 0.1803 -0.0171 0.0129  0.0299  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1572 0.1602 0.2292 -0.0422 0.0172  0.0402  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1537 0.1552 0.1848 -0.0147 0.0126  0.0338  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1536 0.1685 0.2323 -0.0395 0.0262  0.0258  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1508 0.1439 0.1846 -0.0218 0.0151  0.0223  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1614 0.1860 0.2710 -0.0635 0.0248  0.0028  11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1533 0.1319 0.2009 -0.0323 0.0215  -0.0013 11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1734 0.1553 0.2208 -0.0379 0.0117  0.0304  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1595 0.1533 0.1836 -0.0064 0.0138  0.0369  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1849 0.1551 0.2212 -0.0345 0.0207  0.0304  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1675 0.1554 0.1872 0.0011  0.0154  0.0357  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1872 0.1473 0.2068 -0.0316 0.0204  0.0235  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.1741 0.1532 0.1796 0.0039  0.0114  0.0387  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1922 0.1507 0.2245 -0.0288 0.0261  0.0168  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.1781 0.1503 0.1777 0.0062  0.0122  0.0486  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1949 0.1558 0.2318 -0.0171 0.0096  0.0230  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1784 0.1499 0.1840 0.0183  -0.0003 0.0576  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1449 0.1609 0.2080 -0.0311 0.0173  0.0290  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1440 0.1505 0.1820 -0.0209 0.0049  0.0282  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1500 0.1708 0.1979 -0.0264 0.0118  0.0407  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1435 0.1665 0.1909 -0.0139 0.0018  0.0268  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1542 0.1633 0.2052 -0.0282 0.0162  0.0424  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1466 0.1631 0.2010 -0.0182 0.0093  0.0296  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1552 0.1656 0.2126 -0.0278 0.0120  0.0387  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1478 0.1644 0.2049 -0.0154 0.0045  0.0232  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1567 0.1610 0.2028 -0.0191 0.0069  0.0332  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1407 0.1733 0.1922 -0.0006 -0.0027 0.0170  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1630 0.1648 0.2104 -0.0116 0.0289  0.0284  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1347 0.1771 0.1955 0.0050  0.0088  0.0079  12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1719 0.1758 0.2146 0.0049  0.0438  0.0405  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1397 0.1821 0.2071 0.0127  0.0228  0.0098  12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1620 0.1696 0.2221 -0.0129 0.0251  0.0297  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1289 0.1779 0.2097 0.0078  0.0038  -0.0066 12  LEU   A CD2 
306  N  N   . THR   A 13  ? 0.1480 0.1589 0.2116 -0.0206 0.0103  0.0294  13  THR   A N   
307  C  CA  . THR   A 13  ? 0.1494 0.1577 0.2133 -0.0181 0.0196  0.0267  13  THR   A CA  
308  C  C   . THR   A 13  ? 0.1507 0.1571 0.2197 -0.0254 0.0186  0.0261  13  THR   A C   
309  O  O   . THR   A 13  ? 0.1517 0.1558 0.2290 -0.0175 0.0196  0.0338  13  THR   A O   
310  C  CB  . THR   A 13  ? 0.1568 0.1735 0.2249 -0.0228 0.0132  0.0406  13  THR   A CB  
311  O  OG1 . THR   A 13  ? 0.1592 0.1731 0.2296 -0.0298 0.0233  0.0331  13  THR   A OG1 
312  C  CG2 . THR   A 13  ? 0.1658 0.1924 0.2510 -0.0191 0.0145  0.0261  13  THR   A CG2 
321  N  N   A ASP   A 14  ? 0.1579 0.1543 0.2391 -0.0293 0.0123  0.0386  14  ASP   A N   
322  N  N   B ASP   A 14  ? 0.1553 0.1609 0.2223 -0.0230 0.0101  0.0231  14  ASP   A N   
323  C  CA  A ASP   A 14  ? 0.1578 0.1595 0.2563 -0.0222 0.0106  0.0651  14  ASP   A CA  
324  C  CA  B ASP   A 14  ? 0.1585 0.1687 0.2268 -0.0159 0.0005  0.0257  14  ASP   A CA  
325  C  C   A ASP   A 14  ? 0.1601 0.1621 0.2376 -0.0138 0.0043  0.0583  14  ASP   A C   
326  C  C   B ASP   A 14  ? 0.1436 0.1624 0.1977 -0.0104 -0.0018 0.0318  14  ASP   A C   
327  O  O   A ASP   A 14  ? 0.1679 0.1664 0.2378 -0.0223 0.0105  0.0495  14  ASP   A O   
328  O  O   B ASP   A 14  ? 0.1385 0.1665 0.1814 -0.0063 -0.0019 0.0431  14  ASP   A O   
329  C  CB  A ASP   A 14  ? 0.1682 0.1888 0.3081 -0.0252 0.0116  0.0877  14  ASP   A CB  
330  C  CB  B ASP   A 14  ? 0.1840 0.1944 0.2708 -0.0110 -0.0065 0.0261  14  ASP   A CB  
331  C  CG  A ASP   A 14  ? 0.1780 0.2449 0.3772 -0.0250 0.0157  0.0896  14  ASP   A CG  
332  C  CG  B ASP   A 14  ? 0.2064 0.2255 0.3170 -0.0106 -0.0108 0.0267  14  ASP   A CG  
333  O  OD1 A ASP   A 14  ? 0.1781 0.2579 0.4059 -0.0206 0.0107  0.0943  14  ASP   A OD1 
334  O  OD1 B ASP   A 14  ? 0.2104 0.2353 0.3327 -0.0109 -0.0116 0.0317  14  ASP   A OD1 
335  O  OD2 A ASP   A 14  ? 0.1951 0.2872 0.4088 -0.0136 0.0109  0.0731  14  ASP   A OD2 
336  O  OD2 B ASP   A 14  ? 0.2199 0.2411 0.3371 -0.0042 -0.0132 0.0245  14  ASP   A OD2 
345  N  N   A ASN   A 15  ? 0.1534 0.1532 0.2277 -0.0221 0.0064  0.0672  15  ASN   A N   
346  N  N   B ASN   A 15  ? 0.1322 0.1489 0.1854 -0.0205 0.0061  0.0348  15  ASN   A N   
347  C  CA  A ASN   A 15  ? 0.1557 0.1579 0.2334 -0.0205 0.0011  0.0490  15  ASN   A CA  
348  C  CA  B ASN   A 15  ? 0.1316 0.1469 0.1876 -0.0161 0.0072  0.0254  15  ASN   A CA  
349  C  C   A ASN   A 15  ? 0.1476 0.1504 0.2306 -0.0229 0.0095  0.0426  15  ASN   A C   
350  C  C   B ASN   A 15  ? 0.1316 0.1457 0.1953 -0.0082 0.0139  0.0269  15  ASN   A C   
351  O  O   A ASN   A 15  ? 0.1442 0.1474 0.2257 -0.0177 0.0115  0.0314  15  ASN   A O   
352  O  O   B ASN   A 15  ? 0.1295 0.1406 0.2055 0.0035  0.0212  0.0236  15  ASN   A O   
353  C  CB  A ASN   A 15  ? 0.1591 0.1646 0.2304 -0.0093 0.0079  0.0496  15  ASN   A CB  
354  C  CB  B ASN   A 15  ? 0.1266 0.1426 0.1731 -0.0164 0.0049  0.0176  15  ASN   A CB  
355  C  CG  A ASN   A 15  ? 0.1568 0.1625 0.2255 -0.0075 0.0268  0.0360  15  ASN   A CG  
356  C  CG  B ASN   A 15  ? 0.1280 0.1484 0.1821 -0.0105 0.0128  0.0154  15  ASN   A CG  
357  O  OD1 A ASN   A 15  ? 0.1592 0.1608 0.2329 -0.0191 0.0344  0.0382  15  ASN   A OD1 
358  O  OD1 B ASN   A 15  ? 0.1251 0.1560 0.1900 -0.0094 0.0245  0.0085  15  ASN   A OD1 
359  N  ND2 A ASN   A 15  ? 0.1580 0.1635 0.2244 -0.0034 0.0246  0.0329  15  ASN   A ND2 
360  N  ND2 B ASN   A 15  ? 0.1283 0.1459 0.1778 -0.0112 0.0088  0.0176  15  ASN   A ND2 
373  N  N   A VAL   A 16  ? 0.1484 0.1473 0.2320 -0.0190 0.0134  0.0468  16  VAL   A N   
374  N  N   B VAL   A 16  ? 0.1367 0.1512 0.1944 -0.0070 0.0136  0.0323  16  VAL   A N   
375  C  CA  A VAL   A 16  ? 0.1448 0.1471 0.2287 -0.0148 0.0094  0.0419  16  VAL   A CA  
376  C  CA  B VAL   A 16  ? 0.1417 0.1577 0.1919 -0.0061 0.0139  0.0390  16  VAL   A CA  
377  C  C   A VAL   A 16  ? 0.1414 0.1428 0.2153 -0.0216 0.0065  0.0372  16  VAL   A C   
378  C  C   B VAL   A 16  ? 0.1393 0.1670 0.1894 -0.0111 0.0132  0.0424  16  VAL   A C   
379  O  O   A VAL   A 16  ? 0.1342 0.1341 0.2110 -0.0176 0.0111  0.0238  16  VAL   A O   
380  O  O   B VAL   A 16  ? 0.1379 0.1714 0.1884 -0.0076 0.0183  0.0404  16  VAL   A O   
381  C  CB  A VAL   A 16  ? 0.1433 0.1642 0.2249 0.0031  0.0203  0.0506  16  VAL   A CB  
382  C  CB  B VAL   A 16  ? 0.1480 0.1615 0.1869 0.0017  0.0225  0.0386  16  VAL   A CB  
383  C  CG1 A VAL   A 16  ? 0.1604 0.1741 0.2318 0.0061  0.0259  0.0483  16  VAL   A CG1 
384  C  CG1 B VAL   A 16  ? 0.1554 0.1648 0.1885 0.0089  0.0253  0.0360  16  VAL   A CG1 
385  C  CG2 A VAL   A 16  ? 0.1420 0.1813 0.2467 0.0105  0.0271  0.0513  16  VAL   A CG2 
386  C  CG2 B VAL   A 16  ? 0.1471 0.1671 0.2040 -0.0015 0.0224  0.0350  16  VAL   A CG2 
405  N  N   A TYR   A 17  ? 0.1395 0.1364 0.2285 -0.0152 0.0187  0.0385  17  TYR   A N   
406  N  N   B TYR   A 17  ? 0.1367 0.1637 0.1894 -0.0119 0.0106  0.0345  17  TYR   A N   
407  C  CA  A TYR   A 17  ? 0.1483 0.1424 0.2102 -0.0214 0.0209  0.0398  17  TYR   A CA  
408  C  CA  B TYR   A 17  ? 0.1375 0.1611 0.1693 -0.0122 0.0115  0.0325  17  TYR   A CA  
409  C  C   A TYR   A 17  ? 0.1527 0.1386 0.2138 -0.0188 0.0230  0.0258  17  TYR   A C   
410  C  C   B TYR   A 17  ? 0.1399 0.1604 0.1627 -0.0128 0.0100  0.0291  17  TYR   A C   
411  O  O   A TYR   A 17  ? 0.1472 0.1311 0.1820 -0.0190 0.0252  0.0206  17  TYR   A O   
412  O  O   B TYR   A 17  ? 0.1335 0.1590 0.1546 -0.0195 0.0010  0.0263  17  TYR   A O   
413  C  CB  A TYR   A 17  ? 0.1663 0.1463 0.2199 -0.0262 0.0108  0.0509  17  TYR   A CB  
414  C  CB  B TYR   A 17  ? 0.1430 0.1623 0.1830 -0.0054 0.0124  0.0339  17  TYR   A CB  
415  C  CG  A TYR   A 17  ? 0.1836 0.1622 0.2227 -0.0293 -0.0005 0.0451  17  TYR   A CG  
416  C  CG  B TYR   A 17  ? 0.1505 0.1665 0.1839 -0.0023 0.0132  0.0310  17  TYR   A CG  
417  C  CD1 A TYR   A 17  ? 0.1864 0.1778 0.2390 -0.0229 -0.0025 0.0389  17  TYR   A CD1 
418  C  CD1 B TYR   A 17  ? 0.1562 0.1691 0.1962 0.0007  0.0124  0.0335  17  TYR   A CD1 
419  C  CD2 A TYR   A 17  ? 0.1967 0.1626 0.2231 -0.0412 0.0012  0.0477  17  TYR   A CD2 
420  C  CD2 B TYR   A 17  ? 0.1542 0.1671 0.1906 -0.0010 0.0130  0.0334  17  TYR   A CD2 
421  C  CE1 A TYR   A 17  ? 0.1909 0.1801 0.2424 -0.0215 -0.0055 0.0445  17  TYR   A CE1 
422  C  CE1 B TYR   A 17  ? 0.1630 0.1696 0.2060 -0.0032 0.0126  0.0381  17  TYR   A CE1 
423  C  CE2 A TYR   A 17  ? 0.1988 0.1659 0.2243 -0.0356 -0.0090 0.0392  17  TYR   A CE2 
424  C  CE2 B TYR   A 17  ? 0.1573 0.1631 0.1949 -0.0012 0.0146  0.0293  17  TYR   A CE2 
425  C  CZ  A TYR   A 17  ? 0.2016 0.1709 0.2234 -0.0247 -0.0068 0.0452  17  TYR   A CZ  
426  C  CZ  B TYR   A 17  ? 0.1566 0.1639 0.1987 0.0026  0.0119  0.0368  17  TYR   A CZ  
427  O  OH  A TYR   A 17  ? 0.2163 0.1668 0.2273 -0.0178 0.0060  0.0348  17  TYR   A OH  
428  O  OH  B TYR   A 17  ? 0.1485 0.1607 0.1974 0.0150  0.0232  0.0344  17  TYR   A OH  
447  N  N   A ILE   A 18  ? 0.1490 0.1440 0.2343 -0.0198 0.0271  0.0495  18  ILE   A N   
448  N  N   B ILE   A 18  ? 0.1404 0.1598 0.1743 -0.0113 0.0156  0.0366  18  ILE   A N   
449  C  CA  A ILE   A 18  ? 0.1522 0.1494 0.2511 -0.0097 0.0302  0.0355  18  ILE   A CA  
450  C  CA  B ILE   A 18  ? 0.1446 0.1576 0.1786 -0.0087 0.0247  0.0330  18  ILE   A CA  
451  C  C   A ILE   A 18  ? 0.1560 0.1614 0.2631 -0.0184 0.0312  0.0448  18  ILE   A C   
452  C  C   B ILE   A 18  ? 0.1511 0.1675 0.1801 -0.0126 0.0204  0.0309  18  ILE   A C   
453  O  O   A ILE   A 18  ? 0.1466 0.1705 0.2451 -0.0281 0.0306  0.0481  18  ILE   A O   
454  O  O   B ILE   A 18  ? 0.1500 0.1723 0.1757 -0.0184 0.0221  0.0263  18  ILE   A O   
455  C  CB  A ILE   A 18  ? 0.1551 0.1506 0.2345 -0.0021 0.0182  0.0419  18  ILE   A CB  
456  C  CB  B ILE   A 18  ? 0.1494 0.1498 0.1703 0.0013  0.0314  0.0393  18  ILE   A CB  
457  C  CG1 A ILE   A 18  ? 0.1669 0.1668 0.2403 -0.0042 -0.0045 0.0459  18  ILE   A CG1 
458  C  CG1 B ILE   A 18  ? 0.1601 0.1598 0.1777 -0.0037 0.0249  0.0578  18  ILE   A CG1 
459  C  CG2 A ILE   A 18  ? 0.1481 0.1385 0.2336 0.0058  0.0305  0.0359  18  ILE   A CG2 
460  C  CG2 B ILE   A 18  ? 0.1529 0.1451 0.1719 -0.0009 0.0418  0.0432  18  ILE   A CG2 
461  C  CD1 A ILE   A 18  ? 0.1937 0.1896 0.2739 0.0029  -0.0093 0.0478  18  ILE   A CD1 
462  C  CD1 B ILE   A 18  ? 0.1768 0.1732 0.1924 -0.0045 0.0197  0.0662  18  ILE   A CD1 
485  N  N   A LYS   A 19  ? 0.1490 0.1627 0.2743 -0.0114 0.0579  0.0482  19  LYS   A N   
486  N  N   B LYS   A 19  ? 0.1530 0.1710 0.1986 -0.0045 0.0394  0.0220  19  LYS   A N   
487  C  CA  A LYS   A 19  ? 0.1596 0.1724 0.2964 -0.0106 0.0665  0.0509  19  LYS   A CA  
488  C  CA  B LYS   A 19  ? 0.1606 0.1800 0.2239 0.0024  0.0453  0.0167  19  LYS   A CA  
489  C  C   A LYS   A 19  ? 0.1530 0.1606 0.3164 -0.0013 0.0510  0.0420  19  LYS   A C   
490  C  C   B LYS   A 19  ? 0.1509 0.1713 0.2385 0.0037  0.0387  0.0167  19  LYS   A C   
491  O  O   A LYS   A 19  ? 0.1459 0.1552 0.3143 -0.0042 0.0364  0.0578  19  LYS   A O   
492  O  O   B LYS   A 19  ? 0.1481 0.1656 0.2413 0.0053  0.0251  0.0182  19  LYS   A O   
493  C  CB  A LYS   A 19  ? 0.1732 0.1940 0.2998 -0.0046 0.0787  0.0397  19  LYS   A CB  
494  C  CB  B LYS   A 19  ? 0.1762 0.1959 0.2343 0.0093  0.0530  0.0051  19  LYS   A CB  
495  C  CG  A LYS   A 19  ? 0.2050 0.2137 0.3146 -0.0048 0.0774  0.0251  19  LYS   A CG  
496  C  CG  B LYS   A 19  ? 0.1938 0.2109 0.2468 0.0114  0.0516  -0.0038 19  LYS   A CG  
497  C  CD  A LYS   A 19  ? 0.2353 0.2318 0.3035 -0.0047 0.0800  0.0212  19  LYS   A CD  
498  C  CD  B LYS   A 19  ? 0.2131 0.2269 0.2491 0.0127  0.0514  -0.0048 19  LYS   A CD  
499  C  CE  A LYS   A 19  ? 0.2518 0.2402 0.3151 -0.0074 0.0759  0.0069  19  LYS   A CE  
500  C  CE  B LYS   A 19  ? 0.2276 0.2368 0.2555 0.0071  0.0546  -0.0043 19  LYS   A CE  
501  N  NZ  A LYS   A 19  ? 0.2612 0.2425 0.3114 -0.0123 0.0911  -0.0075 19  LYS   A NZ  
502  N  NZ  B LYS   A 19  ? 0.2326 0.2418 0.2482 0.0063  0.0585  -0.0103 19  LYS   A NZ  
529  N  N   A ASN   A 20  ? 0.1647 0.1651 0.3419 0.0017  0.0452  0.0392  20  ASN   A N   
530  N  N   B ASN   A 20  ? 0.1504 0.1731 0.2505 -0.0020 0.0456  0.0249  20  ASN   A N   
531  C  CA  A ASN   A 20  ? 0.1792 0.1829 0.3524 0.0278  0.0418  0.0264  20  ASN   A CA  
532  C  CA  B ASN   A 20  ? 0.1524 0.1838 0.2623 0.0059  0.0486  0.0225  20  ASN   A CA  
533  C  C   A ASN   A 20  ? 0.1956 0.1818 0.3463 0.0167  0.0482  0.0253  20  ASN   A C   
534  C  C   B ASN   A 20  ? 0.1646 0.1844 0.2691 -0.0071 0.0615  0.0137  20  ASN   A C   
535  O  O   A ASN   A 20  ? 0.2181 0.1874 0.3444 0.0035  0.0424  0.0248  20  ASN   A O   
536  O  O   B ASN   A 20  ? 0.1766 0.1873 0.2799 -0.0102 0.0612  0.0051  20  ASN   A O   
537  C  CB  A ASN   A 20  ? 0.1893 0.2028 0.3642 0.0341  0.0423  0.0233  20  ASN   A CB  
538  C  CB  B ASN   A 20  ? 0.1453 0.1942 0.2624 0.0120  0.0473  0.0288  20  ASN   A CB  
539  C  CG  A ASN   A 20  ? 0.2032 0.2136 0.3845 0.0462  0.0327  0.0289  20  ASN   A CG  
540  C  CG  B ASN   A 20  ? 0.1414 0.2001 0.2698 0.0233  0.0374  0.0394  20  ASN   A CG  
541  O  OD1 A ASN   A 20  ? 0.2271 0.2279 0.4062 0.0457  0.0264  0.0212  20  ASN   A OD1 
542  O  OD1 B ASN   A 20  ? 0.1436 0.2028 0.2717 0.0336  0.0330  0.0325  20  ASN   A OD1 
543  N  ND2 A ASN   A 20  ? 0.2117 0.2114 0.4010 0.0528  0.0137  0.0458  20  ASN   A ND2 
544  N  ND2 B ASN   A 20  ? 0.1522 0.2014 0.2879 0.0196  0.0280  0.0461  20  ASN   A ND2 
557  N  N   A ALA   A 21  ? 0.1964 0.1820 0.3467 0.0168  0.0367  0.0180  21  ALA   A N   
558  N  N   B ALA   A 21  ? 0.1722 0.1811 0.2738 -0.0139 0.0560  0.0113  21  ALA   A N   
559  C  CA  A ALA   A 21  ? 0.2024 0.1853 0.3270 0.0130  0.0323  0.0271  21  ALA   A CA  
560  C  CA  B ALA   A 21  ? 0.1831 0.1799 0.2655 -0.0202 0.0561  0.0149  21  ALA   A CA  
561  C  C   A ALA   A 21  ? 0.1899 0.1862 0.3115 0.0062  0.0326  0.0233  21  ALA   A C   
562  C  C   B ALA   A 21  ? 0.1774 0.1756 0.2455 -0.0180 0.0627  0.0095  21  ALA   A C   
563  O  O   A ALA   A 21  ? 0.1868 0.1892 0.3064 0.0084  0.0262  0.0168  21  ALA   A O   
564  O  O   B ALA   A 21  ? 0.1752 0.1705 0.2489 -0.0062 0.0581  -0.0094 21  ALA   A O   
565  C  CB  A ALA   A 21  ? 0.2214 0.1924 0.3361 0.0157  0.0298  0.0298  21  ALA   A CB  
566  C  CB  B ALA   A 21  ? 0.1966 0.1858 0.2856 -0.0206 0.0483  0.0135  21  ALA   A CB  
577  N  N   A ASP   A 22  ? 0.1887 0.1764 0.3106 0.0034  0.0346  0.0251  22  ASP   A N   
578  N  N   B ASP   A 22  ? 0.1810 0.1737 0.2425 -0.0178 0.0641  0.0116  22  ASP   A N   
579  C  CA  A ASP   A 22  ? 0.1941 0.1754 0.3012 0.0052  0.0310  0.0204  22  ASP   A CA  
580  C  CA  B ASP   A 22  ? 0.1846 0.1726 0.2255 -0.0164 0.0584  0.0161  22  ASP   A CA  
581  C  C   A ASP   A 22  ? 0.1793 0.1810 0.2497 -0.0034 0.0308  0.0258  22  ASP   A C   
582  C  C   B ASP   A 22  ? 0.1736 0.1686 0.1897 -0.0230 0.0613  0.0146  22  ASP   A C   
583  O  O   A ASP   A 22  ? 0.1829 0.1900 0.2486 -0.0078 0.0308  0.0236  22  ASP   A O   
584  O  O   B ASP   A 22  ? 0.1724 0.1742 0.1875 -0.0291 0.0601  0.0008  22  ASP   A O   
585  C  CB  A ASP   A 22  ? 0.2123 0.1748 0.3419 0.0090  0.0317  0.0089  22  ASP   A CB  
586  C  CB  B ASP   A 22  ? 0.1935 0.1788 0.2501 -0.0042 0.0557  0.0089  22  ASP   A CB  
587  C  CG  A ASP   A 22  ? 0.2282 0.1813 0.3767 0.0063  0.0087  0.0205  22  ASP   A CG  
588  C  CG  B ASP   A 22  ? 0.1985 0.1808 0.2538 0.0030  0.0604  0.0112  22  ASP   A CG  
589  O  OD1 A ASP   A 22  ? 0.2283 0.1807 0.3871 -0.0137 -0.0224 0.0349  22  ASP   A OD1 
590  O  OD1 B ASP   A 22  ? 0.1981 0.1754 0.2410 0.0051  0.0554  0.0152  22  ASP   A OD1 
591  O  OD2 A ASP   A 22  ? 0.2501 0.1952 0.4171 0.0182  0.0229  0.0099  22  ASP   A OD2 
592  O  OD2 B ASP   A 22  ? 0.2008 0.1936 0.2691 0.0023  0.0746  0.0093  22  ASP   A OD2 
601  N  N   A ILE   A 23  ? 0.1813 0.1856 0.2281 -0.0043 0.0280  0.0218  23  ILE   A N   
602  N  N   B ILE   A 23  ? 0.1722 0.1643 0.1763 -0.0188 0.0509  0.0157  23  ILE   A N   
603  C  CA  A ILE   A 23  ? 0.1767 0.1785 0.2086 -0.0051 0.0296  0.0251  23  ILE   A CA  
604  C  CA  B ILE   A 23  ? 0.1688 0.1694 0.1703 -0.0148 0.0305  0.0254  23  ILE   A CA  
605  C  C   A ILE   A 23  ? 0.1755 0.1855 0.1988 -0.0047 0.0480  0.0190  23  ILE   A C   
606  C  C   B ILE   A 23  ? 0.1751 0.1822 0.1758 -0.0219 0.0354  0.0158  23  ILE   A C   
607  O  O   A ILE   A 23  ? 0.1827 0.1944 0.1935 0.0039  0.0424  0.0163  23  ILE   A O   
608  O  O   B ILE   A 23  ? 0.1790 0.1812 0.1740 -0.0185 0.0350  0.0074  23  ILE   A O   
609  C  CB  A ILE   A 23  ? 0.1841 0.1823 0.1856 0.0012  0.0208  0.0211  23  ILE   A CB  
610  C  CB  B ILE   A 23  ? 0.1637 0.1643 0.1492 -0.0049 0.0115  0.0313  23  ILE   A CB  
611  C  CG1 A ILE   A 23  ? 0.1892 0.1867 0.1845 0.0042  0.0201  0.0081  23  ILE   A CG1 
612  C  CG1 B ILE   A 23  ? 0.1631 0.1608 0.1339 -0.0078 0.0014  0.0207  23  ILE   A CG1 
613  C  CG2 A ILE   A 23  ? 0.1836 0.1840 0.1756 -0.0018 0.0187  0.0202  23  ILE   A CG2 
614  C  CG2 B ILE   A 23  ? 0.1618 0.1608 0.1438 0.0054  0.0063  0.0357  23  ILE   A CG2 
615  C  CD1 A ILE   A 23  ? 0.1930 0.1875 0.1872 0.0031  0.0146  0.0048  23  ILE   A CD1 
616  C  CD1 B ILE   A 23  ? 0.1561 0.1608 0.1362 -0.0109 -0.0067 0.0112  23  ILE   A CD1 
639  N  N   A VAL   A 24  ? 0.1805 0.1883 0.2083 -0.0151 0.0468  0.0108  24  VAL   A N   
640  N  N   B VAL   A 24  ? 0.1835 0.1959 0.1962 -0.0297 0.0268  0.0114  24  VAL   A N   
641  C  CA  A VAL   A 24  ? 0.1990 0.1937 0.2230 -0.0202 0.0420  0.0036  24  VAL   A CA  
642  C  CA  B VAL   A 24  ? 0.1994 0.2105 0.2083 -0.0282 0.0300  0.0093  24  VAL   A CA  
643  C  C   A VAL   A 24  ? 0.2030 0.2061 0.2236 -0.0274 0.0396  0.0010  24  VAL   A C   
644  C  C   B VAL   A 24  ? 0.2052 0.2280 0.2069 -0.0255 0.0395  0.0031  24  VAL   A C   
645  O  O   A VAL   A 24  ? 0.2152 0.2088 0.2204 -0.0209 0.0428  -0.0080 24  VAL   A O   
646  O  O   B VAL   A 24  ? 0.2096 0.2319 0.2128 -0.0218 0.0401  0.0040  24  VAL   A O   
647  C  CB  A VAL   A 24  ? 0.2111 0.1954 0.2449 -0.0218 0.0411  0.0053  24  VAL   A CB  
648  C  CB  B VAL   A 24  ? 0.2097 0.2152 0.2351 -0.0307 0.0203  0.0210  24  VAL   A CB  
649  C  CG1 A VAL   A 24  ? 0.2230 0.2117 0.2577 -0.0183 0.0510  -0.0059 24  VAL   A CG1 
650  C  CG1 B VAL   A 24  ? 0.2206 0.2247 0.2579 -0.0314 0.0150  0.0218  24  VAL   A CG1 
651  C  CG2 A VAL   A 24  ? 0.2271 0.2018 0.2648 -0.0160 0.0502  0.0223  24  VAL   A CG2 
652  C  CG2 B VAL   A 24  ? 0.2174 0.2157 0.2401 -0.0314 0.0245  0.0242  24  VAL   A CG2 
671  N  N   A GLU   A 25  ? 0.2109 0.2323 0.2240 -0.0283 0.0510  -0.0064 25  GLU   A N   
672  N  N   B GLU   A 25  ? 0.2113 0.2446 0.2042 -0.0241 0.0540  -0.0051 25  GLU   A N   
673  C  CA  A GLU   A 25  ? 0.2330 0.2621 0.2447 -0.0227 0.0685  -0.0088 25  GLU   A CA  
674  C  CA  B GLU   A 25  ? 0.2266 0.2654 0.2282 -0.0255 0.0607  -0.0035 25  GLU   A CA  
675  C  C   A GLU   A 25  ? 0.2247 0.2630 0.2140 -0.0354 0.0685  -0.0091 25  GLU   A C   
676  C  C   B GLU   A 25  ? 0.2233 0.2702 0.2167 -0.0326 0.0544  -0.0047 25  GLU   A C   
677  O  O   A GLU   A 25  ? 0.2316 0.2753 0.2201 -0.0377 0.0691  -0.0172 25  GLU   A O   
678  O  O   B GLU   A 25  ? 0.2280 0.2767 0.2261 -0.0324 0.0530  -0.0109 25  GLU   A O   
679  C  CB  A GLU   A 25  ? 0.2633 0.2955 0.2989 -0.0150 0.0784  -0.0016 25  GLU   A CB  
680  C  CB  B GLU   A 25  ? 0.2464 0.2799 0.2632 -0.0219 0.0660  -0.0009 25  GLU   A CB  
681  C  CG  A GLU   A 25  ? 0.2975 0.3249 0.3672 -0.0106 0.0661  -0.0042 25  GLU   A CG  
682  C  CG  B GLU   A 25  ? 0.2720 0.2952 0.3142 -0.0209 0.0582  -0.0007 25  GLU   A CG  
683  C  CD  A GLU   A 25  ? 0.3231 0.3490 0.4252 -0.0070 0.0541  -0.0038 25  GLU   A CD  
684  C  CD  B GLU   A 25  ? 0.2921 0.3082 0.3573 -0.0214 0.0466  0.0010  25  GLU   A CD  
685  O  OE1 A GLU   A 25  ? 0.3375 0.3599 0.4440 -0.0001 0.0385  -0.0129 25  GLU   A OE1 
686  O  OE1 B GLU   A 25  ? 0.3026 0.3146 0.3779 -0.0199 0.0383  0.0033  25  GLU   A OE1 
687  O  OE2 A GLU   A 25  ? 0.3277 0.3588 0.4534 -0.0096 0.0501  -0.0098 25  GLU   A OE2 
688  O  OE2 B GLU   A 25  ? 0.2993 0.3115 0.3728 -0.0236 0.0448  -0.0034 25  GLU   A OE2 
701  N  N   A GLU   A 26  ? 0.2157 0.2518 0.2196 -0.0510 0.0698  -0.0138 26  GLU   A N   
702  N  N   B GLU   A 26  ? 0.2181 0.2669 0.2056 -0.0415 0.0567  -0.0038 26  GLU   A N   
703  C  CA  A GLU   A 26  ? 0.2321 0.2504 0.2049 -0.0606 0.0630  -0.0093 26  GLU   A CA  
704  C  CA  B GLU   A 26  ? 0.2235 0.2672 0.1992 -0.0464 0.0531  0.0027  26  GLU   A CA  
705  C  C   A GLU   A 26  ? 0.2281 0.2439 0.1689 -0.0561 0.0527  -0.0015 26  GLU   A C   
706  C  C   B GLU   A 26  ? 0.2219 0.2509 0.1753 -0.0494 0.0565  0.0035  26  GLU   A C   
707  O  O   A GLU   A 26  ? 0.2302 0.2420 0.1582 -0.0684 0.0475  -0.0006 26  GLU   A O   
708  O  O   B GLU   A 26  ? 0.2266 0.2488 0.1581 -0.0491 0.0641  0.0010  26  GLU   A O   
709  C  CB  A GLU   A 26  ? 0.2572 0.2497 0.2457 -0.0741 0.0634  0.0004  26  GLU   A CB  
710  C  CB  B GLU   A 26  ? 0.2319 0.2806 0.2187 -0.0503 0.0342  0.0076  26  GLU   A CB  
711  C  CG  A GLU   A 26  ? 0.2771 0.2586 0.3129 -0.0802 0.0810  -0.0150 26  GLU   A CG  
712  C  CG  B GLU   A 26  ? 0.2371 0.2912 0.2369 -0.0529 0.0281  0.0024  26  GLU   A CG  
713  C  CD  A GLU   A 26  ? 0.2865 0.2581 0.3336 -0.0898 0.1149  -0.0263 26  GLU   A CD  
714  C  CD  B GLU   A 26  ? 0.2391 0.2965 0.2347 -0.0584 0.0269  -0.0007 26  GLU   A CD  
715  O  OE1 A GLU   A 26  ? 0.2767 0.2734 0.3396 -0.0806 0.1365  -0.0823 26  GLU   A OE1 
716  O  OE1 B GLU   A 26  ? 0.2479 0.3052 0.2312 -0.0530 0.0284  -0.0107 26  GLU   A OE1 
717  O  OE2 A GLU   A 26  ? 0.3001 0.2569 0.3334 -0.0895 0.1274  -0.0150 26  GLU   A OE2 
718  O  OE2 B GLU   A 26  ? 0.2321 0.2945 0.2152 -0.0663 0.0276  -0.0068 26  GLU   A OE2 
731  N  N   . ALA   A 27  ? 0.2106 0.2360 0.1691 -0.0563 0.0520  0.0028  27  ALA   A N   
732  C  CA  . ALA   A 27  ? 0.2185 0.2505 0.1556 -0.0546 0.0472  -0.0022 27  ALA   A CA  
733  C  C   . ALA   A 27  ? 0.2578 0.2820 0.1675 -0.0661 0.0578  -0.0208 27  ALA   A C   
734  O  O   . ALA   A 27  ? 0.2600 0.2790 0.1701 -0.0714 0.0391  -0.0154 27  ALA   A O   
735  C  CB  . ALA   A 27  ? 0.1958 0.2388 0.1616 -0.0550 0.0397  0.0043  27  ALA   A CB  
742  N  N   A LYS   A 28  ? 0.2854 0.3022 0.1849 -0.0667 0.0596  -0.0525 28  LYS   A N   
743  N  N   B LYS   A 28  ? 0.2870 0.3056 0.2035 -0.0577 0.0491  -0.0319 28  LYS   A N   
744  C  CA  A LYS   A 28  ? 0.3258 0.3404 0.2318 -0.0597 0.0660  -0.0692 28  LYS   A CA  
745  C  CA  B LYS   A 28  ? 0.3210 0.3364 0.2559 -0.0470 0.0417  -0.0384 28  LYS   A CA  
746  C  C   A LYS   A 28  ? 0.3475 0.3750 0.2135 -0.0653 0.0865  -0.0515 28  LYS   A C   
747  C  C   B LYS   A 28  ? 0.3405 0.3584 0.2621 -0.0452 0.0423  -0.0300 28  LYS   A C   
748  O  O   A LYS   A 28  ? 0.3614 0.3889 0.2513 -0.0621 0.0638  -0.0508 28  LYS   A O   
749  O  O   B LYS   A 28  ? 0.3479 0.3660 0.2749 -0.0436 0.0354  -0.0304 28  LYS   A O   
750  C  CB  A LYS   A 28  ? 0.3448 0.3504 0.2986 -0.0448 0.0590  -0.0879 28  LYS   A CB  
751  C  CB  B LYS   A 28  ? 0.3352 0.3467 0.3021 -0.0378 0.0354  -0.0472 28  LYS   A CB  
752  C  CG  A LYS   A 28  ? 0.3618 0.3602 0.3563 -0.0326 0.0572  -0.0945 28  LYS   A CG  
753  C  CG  B LYS   A 28  ? 0.3486 0.3556 0.3445 -0.0296 0.0318  -0.0508 28  LYS   A CG  
754  C  CD  A LYS   A 28  ? 0.3775 0.3772 0.4186 -0.0224 0.0511  -0.0891 28  LYS   A CD  
755  C  CD  B LYS   A 28  ? 0.3609 0.3668 0.3873 -0.0223 0.0273  -0.0493 28  LYS   A CD  
756  C  CE  A LYS   A 28  ? 0.3894 0.3891 0.4613 -0.0157 0.0478  -0.0917 28  LYS   A CE  
757  C  CE  B LYS   A 28  ? 0.3704 0.3743 0.4171 -0.0180 0.0250  -0.0512 28  LYS   A CE  
758  N  NZ  A LYS   A 28  ? 0.3987 0.3968 0.4930 -0.0097 0.0490  -0.0977 28  LYS   A NZ  
759  N  NZ  B LYS   A 28  ? 0.3773 0.3789 0.4382 -0.0141 0.0249  -0.0545 28  LYS   A NZ  
786  N  N   A LYS   A 29  ? 0.3547 0.3955 0.1999 -0.0758 0.1187  -0.0237 29  LYS   A N   
787  N  N   B LYS   A 29  ? 0.3515 0.3718 0.2701 -0.0460 0.0481  -0.0175 29  LYS   A N   
788  C  CA  A LYS   A 29  ? 0.3700 0.4182 0.2193 -0.0824 0.1346  -0.0021 29  LYS   A CA  
789  C  CA  B LYS   A 29  ? 0.3642 0.3855 0.2858 -0.0459 0.0507  -0.0065 29  LYS   A CA  
790  C  C   A LYS   A 29  ? 0.3701 0.4128 0.2014 -0.0931 0.1129  0.0092  29  LYS   A C   
791  C  C   B LYS   A 29  ? 0.3629 0.3807 0.2573 -0.0504 0.0409  0.0013  29  LYS   A C   
792  O  O   A LYS   A 29  ? 0.3826 0.4296 0.2115 -0.0818 0.1016  0.0038  29  LYS   A O   
793  O  O   B LYS   A 29  ? 0.3653 0.3881 0.2483 -0.0476 0.0452  0.0040  29  LYS   A O   
794  C  CB  A LYS   A 29  ? 0.3828 0.4462 0.2755 -0.0730 0.1603  0.0022  29  LYS   A CB  
795  C  CB  B LYS   A 29  ? 0.3769 0.4028 0.3364 -0.0394 0.0602  -0.0034 29  LYS   A CB  
796  C  CG  A LYS   A 29  ? 0.3987 0.4712 0.3621 -0.0623 0.1629  0.0035  29  LYS   A CG  
797  C  CG  B LYS   A 29  ? 0.3897 0.4181 0.3892 -0.0335 0.0647  -0.0008 29  LYS   A CG  
798  C  CD  A LYS   A 29  ? 0.4126 0.4933 0.4409 -0.0538 0.1608  0.0003  29  LYS   A CD  
799  C  CD  B LYS   A 29  ? 0.4004 0.4314 0.4366 -0.0285 0.0679  0.0001  29  LYS   A CD  
800  C  CE  A LYS   A 29  ? 0.4230 0.5090 0.4920 -0.0476 0.1600  -0.0055 29  LYS   A CE  
801  C  CE  B LYS   A 29  ? 0.4084 0.4408 0.4699 -0.0247 0.0703  -0.0018 29  LYS   A CE  
802  N  NZ  A LYS   A 29  ? 0.4265 0.5175 0.5247 -0.0432 0.1597  -0.0110 29  LYS   A NZ  
803  N  NZ  B LYS   A 29  ? 0.4118 0.4459 0.4912 -0.0219 0.0705  -0.0030 29  LYS   A NZ  
830  N  N   A VAL   A 30  ? 0.3533 0.3884 0.1879 -0.1119 0.0991  0.0165  30  VAL   A N   
831  N  N   B VAL   A 30  ? 0.3576 0.3669 0.2431 -0.0578 0.0295  0.0045  30  VAL   A N   
832  C  CA  A VAL   A 30  ? 0.3469 0.3656 0.1849 -0.1229 0.0680  0.0347  30  VAL   A CA  
833  C  CA  B VAL   A 30  ? 0.3553 0.3537 0.2378 -0.0638 0.0137  0.0142  30  VAL   A CA  
834  C  C   A VAL   A 30  ? 0.3470 0.3420 0.1523 -0.1159 0.0521  0.0390  30  VAL   A C   
835  C  C   B VAL   A 30  ? 0.3550 0.3429 0.2216 -0.0648 0.0074  0.0144  30  VAL   A C   
836  O  O   A VAL   A 30  ? 0.3572 0.3411 0.1580 -0.1181 0.0489  0.0411  30  VAL   A O   
837  O  O   B VAL   A 30  ? 0.3588 0.3424 0.2170 -0.0642 0.0044  0.0159  30  VAL   A O   
838  C  CB  A VAL   A 30  ? 0.3416 0.3644 0.2214 -0.1373 0.0475  0.0410  30  VAL   A CB  
839  C  CB  B VAL   A 30  ? 0.3533 0.3508 0.2510 -0.0680 0.0037  0.0196  30  VAL   A CB  
840  C  CG1 A VAL   A 30  ? 0.3438 0.3630 0.2330 -0.1382 0.0280  0.0420  30  VAL   A CG1 
841  C  CG1 B VAL   A 30  ? 0.3542 0.3497 0.2558 -0.0673 -0.0036 0.0200  30  VAL   A CG1 
842  C  CG2 A VAL   A 30  ? 0.3408 0.3710 0.2532 -0.1423 0.0506  0.0407  30  VAL   A CG2 
843  C  CG2 B VAL   A 30  ? 0.3530 0.3515 0.2641 -0.0698 0.0038  0.0239  30  VAL   A CG2 
862  N  N   A LYS   A 31  ? 0.3384 0.3243 0.1342 -0.1131 0.0328  0.0344  31  LYS   A N   
863  N  N   B LYS   A 31  ? 0.3495 0.3327 0.2149 -0.0672 0.0004  0.0129  31  LYS   A N   
864  C  CA  A LYS   A 31  ? 0.3452 0.3212 0.1481 -0.0944 -0.0013 0.0243  31  LYS   A CA  
865  C  CA  B LYS   A 31  ? 0.3478 0.3268 0.2204 -0.0663 -0.0103 0.0153  31  LYS   A CA  
866  C  C   A LYS   A 31  ? 0.3180 0.2999 0.1171 -0.0719 -0.0115 0.0614  31  LYS   A C   
867  C  C   B LYS   A 31  ? 0.3232 0.3059 0.1627 -0.0666 -0.0113 0.0404  31  LYS   A C   
868  O  O   A LYS   A 31  ? 0.3224 0.3133 0.1392 -0.0647 -0.0345 0.0768  31  LYS   A O   
869  O  O   B LYS   A 31  ? 0.3286 0.3143 0.1733 -0.0646 -0.0205 0.0492  31  LYS   A O   
870  C  CB  A LYS   A 31  ? 0.3838 0.3456 0.2558 -0.0878 -0.0197 -0.0074 31  LYS   A CB  
871  C  CB  B LYS   A 31  ? 0.3711 0.3429 0.2960 -0.0617 -0.0182 -0.0011 31  LYS   A CB  
872  C  CG  A LYS   A 31  ? 0.4239 0.3695 0.3851 -0.0763 -0.0352 -0.0272 31  LYS   A CG  
873  C  CG  B LYS   A 31  ? 0.3927 0.3582 0.3782 -0.0548 -0.0256 -0.0127 31  LYS   A CG  
874  C  CD  A LYS   A 31  ? 0.4542 0.3874 0.4778 -0.0652 -0.0474 -0.0455 31  LYS   A CD  
875  C  CD  B LYS   A 31  ? 0.4088 0.3708 0.4423 -0.0489 -0.0327 -0.0236 31  LYS   A CD  
876  C  CE  A LYS   A 31  ? 0.4741 0.4007 0.5342 -0.0561 -0.0580 -0.0607 31  LYS   A CE  
877  C  CE  B LYS   A 31  ? 0.4182 0.3802 0.4827 -0.0442 -0.0384 -0.0313 31  LYS   A CE  
878  N  NZ  A LYS   A 31  ? 0.4841 0.4064 0.5668 -0.0495 -0.0663 -0.0703 31  LYS   A NZ  
879  N  NZ  B LYS   A 31  ? 0.4233 0.3847 0.5081 -0.0410 -0.0429 -0.0366 31  LYS   A NZ  
906  N  N   . PRO   A 32  ? 0.2941 0.2783 0.1148 -0.0739 -0.0023 0.0430  32  PRO   A N   
907  C  CA  . PRO   A 32  ? 0.2782 0.2541 0.1546 -0.0662 -0.0099 0.0533  32  PRO   A CA  
908  C  C   . PRO   A 32  ? 0.2695 0.2458 0.1650 -0.0542 -0.0199 0.0609  32  PRO   A C   
909  O  O   . PRO   A 32  ? 0.2600 0.2393 0.1766 -0.0603 -0.0365 0.0571  32  PRO   A O   
910  C  CB  . PRO   A 32  ? 0.2716 0.2561 0.1634 -0.0672 -0.0064 0.0425  32  PRO   A CB  
911  C  CG  . PRO   A 32  ? 0.2674 0.2599 0.1094 -0.0645 -0.0167 0.0244  32  PRO   A CG  
912  C  CD  . PRO   A 32  ? 0.2728 0.2667 0.1027 -0.0651 -0.0159 0.0328  32  PRO   A CD  
920  N  N   . THR   A 33  ? 0.2745 0.2417 0.1443 -0.0436 -0.0207 0.0607  33  THR   A N   
921  C  CA  . THR   A 33  ? 0.2743 0.2409 0.1600 -0.0241 -0.0333 0.0557  33  THR   A CA  
922  C  C   . THR   A 33  ? 0.2379 0.2199 0.1533 -0.0294 -0.0307 0.0425  33  THR   A C   
923  O  O   . THR   A 33  ? 0.2294 0.2235 0.1766 -0.0342 -0.0435 0.0477  33  THR   A O   
924  C  CB  . THR   A 33  ? 0.3021 0.2632 0.1860 -0.0159 -0.0396 0.0742  33  THR   A CB  
925  O  OG1 . THR   A 33  ? 0.3241 0.2826 0.2099 -0.0030 -0.0332 0.0896  33  THR   A OG1 
926  C  CG2 . THR   A 33  ? 0.3065 0.2720 0.2043 -0.0134 -0.0448 0.0719  33  THR   A CG2 
934  N  N   . VAL   A 34  ? 0.2093 0.2001 0.1386 -0.0287 -0.0244 0.0465  34  VAL   A N   
935  C  CA  . VAL   A 34  ? 0.1943 0.1842 0.1352 -0.0258 -0.0178 0.0373  34  VAL   A CA  
936  C  C   . VAL   A 34  ? 0.1810 0.1717 0.1261 -0.0270 -0.0053 0.0342  34  VAL   A C   
937  O  O   . VAL   A 34  ? 0.1817 0.1710 0.1564 -0.0317 -0.0003 0.0410  34  VAL   A O   
938  C  CB  . VAL   A 34  ? 0.1956 0.1756 0.1560 -0.0265 -0.0117 0.0244  34  VAL   A CB  
939  C  CG1 . VAL   A 34  ? 0.2030 0.1739 0.1630 -0.0196 -0.0047 0.0222  34  VAL   A CG1 
940  C  CG2 . VAL   A 34  ? 0.2062 0.1898 0.1866 -0.0162 -0.0197 0.0281  34  VAL   A CG2 
950  N  N   . VAL   A 35  ? 0.1633 0.1652 0.1253 -0.0283 -0.0121 0.0190  35  VAL   A N   
951  C  CA  . VAL   A 35  ? 0.1534 0.1601 0.1205 -0.0202 -0.0022 0.0184  35  VAL   A CA  
952  C  C   . VAL   A 35  ? 0.1462 0.1528 0.1276 -0.0173 0.0017  0.0211  35  VAL   A C   
953  O  O   . VAL   A 35  ? 0.1413 0.1646 0.1418 -0.0212 0.0080  0.0174  35  VAL   A O   
954  C  CB  . VAL   A 35  ? 0.1604 0.1689 0.1388 -0.0141 0.0048  0.0098  35  VAL   A CB  
955  C  CG1 . VAL   A 35  ? 0.1702 0.1660 0.1481 -0.0053 -0.0044 0.0050  35  VAL   A CG1 
956  C  CG2 . VAL   A 35  ? 0.1603 0.1678 0.1656 -0.0126 0.0149  0.0033  35  VAL   A CG2 
966  N  N   . VAL   A 36  ? 0.1364 0.1441 0.1106 -0.0169 0.0075  0.0290  36  VAL   A N   
967  C  CA  . VAL   A 36  ? 0.1287 0.1378 0.1295 -0.0121 0.0084  0.0235  36  VAL   A CA  
968  C  C   . VAL   A 36  ? 0.1288 0.1377 0.1266 -0.0148 0.0041  0.0213  36  VAL   A C   
969  O  O   . VAL   A 36  ? 0.1384 0.1392 0.1460 -0.0024 0.0188  0.0209  36  VAL   A O   
970  C  CB  . VAL   A 36  ? 0.1322 0.1257 0.1294 -0.0065 0.0005  0.0161  36  VAL   A CB  
971  C  CG1 . VAL   A 36  ? 0.1381 0.1300 0.1535 -0.0138 0.0000  0.0033  36  VAL   A CG1 
972  C  CG2 . VAL   A 36  ? 0.1411 0.1325 0.1623 -0.0073 0.0011  0.0140  36  VAL   A CG2 
982  N  N   . ASN   A 37  ? 0.1243 0.1294 0.1311 -0.0056 0.0024  0.0165  37  ASN   A N   
983  C  CA  . ASN   A 37  ? 0.1250 0.1257 0.1315 0.0025  0.0020  0.0189  37  ASN   A CA  
984  C  C   . ASN   A 37  ? 0.1203 0.1249 0.1277 -0.0021 0.0109  0.0273  37  ASN   A C   
985  O  O   . ASN   A 37  ? 0.1364 0.1376 0.1260 0.0047  0.0069  0.0096  37  ASN   A O   
986  C  CB  . ASN   A 37  ? 0.1216 0.1249 0.1407 -0.0016 0.0067  0.0228  37  ASN   A CB  
987  C  CG  . ASN   A 37  ? 0.1268 0.1289 0.1438 0.0018  0.0067  0.0159  37  ASN   A CG  
988  O  OD1 . ASN   A 37  ? 0.1263 0.1281 0.1728 0.0020  0.0017  0.0222  37  ASN   A OD1 
989  N  ND2 . ASN   A 37  ? 0.1315 0.1330 0.1463 -0.0026 0.0024  0.0252  37  ASN   A ND2 
996  N  N   . ALA   A 38  ? 0.1246 0.1332 0.1341 0.0009  0.0070  0.0141  38  ALA   A N   
997  C  CA  . ALA   A 38  ? 0.1312 0.1402 0.1228 -0.0032 -0.0068 0.0114  38  ALA   A CA  
998  C  C   . ALA   A 38  ? 0.1323 0.1363 0.1284 0.0055  -0.0020 0.0014  38  ALA   A C   
999  O  O   . ALA   A 38  ? 0.1324 0.1324 0.1404 0.0086  -0.0054 0.0093  38  ALA   A O   
1000 C  CB  . ALA   A 38  ? 0.1367 0.1824 0.1460 -0.0152 -0.0083 0.0081  38  ALA   A CB  
1006 N  N   . ALA   A 39  ? 0.1322 0.1335 0.1366 0.0060  0.0003  0.0085  39  ALA   A N   
1007 C  CA  . ALA   A 39  ? 0.1323 0.1291 0.1403 -0.0000 0.0107  0.0123  39  ALA   A CA  
1008 C  C   . ALA   A 39  ? 0.1301 0.1237 0.1407 0.0011  0.0007  0.0132  39  ALA   A C   
1009 O  O   . ALA   A 39  ? 0.1436 0.1306 0.1410 -0.0068 0.0026  0.0113  39  ALA   A O   
1010 C  CB  . ALA   A 39  ? 0.1365 0.1490 0.1450 0.0030  -0.0106 0.0026  39  ALA   A CB  
1016 N  N   . ASN   A 40  ? 0.1452 0.1265 0.1480 -0.0086 0.0181  0.0118  40  ASN   A N   
1017 C  CA  . ASN   A 40  ? 0.1542 0.1241 0.1377 -0.0058 0.0116  0.0068  40  ASN   A CA  
1018 C  C   . ASN   A 40  ? 0.1541 0.1164 0.1369 -0.0047 0.0270  0.0066  40  ASN   A C   
1019 O  O   . ASN   A 40  ? 0.1468 0.1257 0.1403 -0.0068 0.0206  0.0179  40  ASN   A O   
1020 C  CB  . ASN   A 40  ? 0.1620 0.1409 0.1497 -0.0044 0.0031  0.0032  40  ASN   A CB  
1021 C  CG  . ASN   A 40  ? 0.1703 0.1444 0.1799 -0.0027 -0.0060 0.0090  40  ASN   A CG  
1022 O  OD1 . ASN   A 40  ? 0.1790 0.1415 0.1983 -0.0068 0.0096  0.0038  40  ASN   A OD1 
1023 N  ND2 . ASN   A 40  ? 0.1736 0.1604 0.2011 0.0051  0.0003  -0.0133 40  ASN   A ND2 
1030 N  N   . VAL   A 41  ? 0.1681 0.1204 0.1441 -0.0028 0.0220  0.0096  41  VAL   A N   
1031 C  CA  . VAL   A 41  ? 0.1717 0.1319 0.1421 -0.0022 0.0291  0.0120  41  VAL   A CA  
1032 C  C   . VAL   A 41  ? 0.1647 0.1343 0.1424 0.0013  0.0399  0.0164  41  VAL   A C   
1033 O  O   . VAL   A 41  ? 0.1671 0.1267 0.1756 0.0013  0.0289  0.0075  41  VAL   A O   
1034 C  CB  . VAL   A 41  ? 0.1877 0.1439 0.1625 -0.0150 0.0489  -0.0031 41  VAL   A CB  
1035 C  CG1 . VAL   A 41  ? 0.2009 0.1542 0.1779 -0.0093 0.0492  -0.0066 41  VAL   A CG1 
1036 C  CG2 . VAL   A 41  ? 0.2126 0.1561 0.1508 -0.0233 0.0513  -0.0008 41  VAL   A CG2 
1046 N  N   . TYR   A 42  ? 0.1508 0.1297 0.1572 -0.0024 0.0430  0.0243  42  TYR   A N   
1047 C  CA  . TYR   A 42  ? 0.1504 0.1231 0.1717 -0.0070 0.0368  0.0249  42  TYR   A CA  
1048 C  C   . TYR   A 42  ? 0.1431 0.1220 0.1594 -0.0056 0.0284  0.0197  42  TYR   A C   
1049 O  O   . TYR   A 42  ? 0.1452 0.1228 0.1862 -0.0155 0.0289  0.0049  42  TYR   A O   
1050 C  CB  . TYR   A 42  ? 0.1727 0.1346 0.1666 -0.0060 0.0334  0.0297  42  TYR   A CB  
1051 C  CG  . TYR   A 42  ? 0.1943 0.1465 0.1659 -0.0066 0.0264  0.0279  42  TYR   A CG  
1052 C  CD1 . TYR   A 42  ? 0.1996 0.1602 0.1701 -0.0131 0.0263  0.0258  42  TYR   A CD1 
1053 C  CD2 . TYR   A 42  ? 0.2115 0.1679 0.1857 -0.0036 0.0213  0.0231  42  TYR   A CD2 
1054 C  CE1 . TYR   A 42  ? 0.2122 0.1708 0.1747 -0.0174 0.0302  0.0131  42  TYR   A CE1 
1055 C  CE2 . TYR   A 42  ? 0.2253 0.1831 0.2066 -0.0117 0.0301  0.0282  42  TYR   A CE2 
1056 C  CZ  . TYR   A 42  ? 0.2333 0.1871 0.1824 -0.0213 0.0362  0.0187  42  TYR   A CZ  
1057 O  OH  . TYR   A 42  ? 0.2577 0.2097 0.1961 -0.0306 0.0348  0.0137  42  TYR   A OH  
1067 N  N   . LEU   A 43  ? 0.1402 0.1263 0.1511 -0.0069 0.0166  0.0045  43  LEU   A N   
1068 C  CA  . LEU   A 43  ? 0.1323 0.1230 0.1574 -0.0066 0.0112  0.0098  43  LEU   A CA  
1069 C  C   . LEU   A 43  ? 0.1343 0.1306 0.1591 -0.0047 0.0143  0.0062  43  LEU   A C   
1070 O  O   . LEU   A 43  ? 0.1479 0.1334 0.1752 0.0031  -0.0041 0.0065  43  LEU   A O   
1071 C  CB  . LEU   A 43  ? 0.1386 0.1224 0.1662 -0.0105 0.0154  0.0113  43  LEU   A CB  
1072 C  CG  . LEU   A 43  ? 0.1445 0.1235 0.1734 -0.0025 0.0138  0.0094  43  LEU   A CG  
1073 C  CD1 . LEU   A 43  ? 0.1543 0.1304 0.1851 -0.0028 0.0014  0.0149  43  LEU   A CD1 
1074 C  CD2 . LEU   A 43  ? 0.1539 0.1254 0.1674 -0.0019 0.0032  0.0208  43  LEU   A CD2 
1086 N  N   . LYS   A 44  ? 0.1414 0.1291 0.1452 -0.0030 0.0043  0.0142  44  LYS   A N   
1087 C  CA  . LYS   A 44  ? 0.1554 0.1315 0.1554 -0.0065 0.0128  0.0198  44  LYS   A CA  
1088 C  C   . LYS   A 44  ? 0.1409 0.1302 0.1406 -0.0012 0.0050  0.0066  44  LYS   A C   
1089 O  O   . LYS   A 44  ? 0.1552 0.1461 0.1537 -0.0052 0.0080  -0.0013 44  LYS   A O   
1090 C  CB  . LYS   A 44  ? 0.1856 0.1466 0.1873 -0.0060 0.0276  0.0255  44  LYS   A CB  
1091 C  CG  . LYS   A 44  ? 0.2235 0.1784 0.2312 -0.0079 0.0467  0.0414  44  LYS   A CG  
1092 C  CD  . LYS   A 44  ? 0.2661 0.2413 0.3587 -0.0126 0.0427  0.0359  44  LYS   A CD  
1093 C  CE  . LYS   A 44  ? 0.2790 0.2793 0.4442 -0.0138 0.0357  0.0404  44  LYS   A CE  
1094 N  NZ  . LYS   A 44  ? 0.2967 0.3148 0.4841 -0.0172 0.0310  0.0425  44  LYS   A NZ  
1108 N  N   A HIS   A 45  ? 0.1255 0.1251 0.1403 -0.0037 -0.0038 0.0132  45  HIS   A N   
1109 N  N   B HIS   A 45  ? 0.1391 0.1360 0.1510 -0.0026 -0.0026 0.0088  45  HIS   A N   
1110 C  CA  A HIS   A 45  ? 0.1201 0.1265 0.1487 0.0024  0.0035  0.0132  45  HIS   A CA  
1111 C  CA  B HIS   A 45  ? 0.1399 0.1447 0.1642 -0.0023 -0.0026 0.0062  45  HIS   A CA  
1112 C  C   A HIS   A 45  ? 0.1289 0.1356 0.1506 0.0011  0.0099  0.0265  45  HIS   A C   
1113 C  C   B HIS   A 45  ? 0.1490 0.1564 0.1767 0.0022  -0.0031 0.0137  45  HIS   A C   
1114 O  O   A HIS   A 45  ? 0.1270 0.1262 0.1603 0.0039  0.0120  0.0154  45  HIS   A O   
1115 O  O   B HIS   A 45  ? 0.1542 0.1594 0.1981 0.0092  -0.0058 0.0128  45  HIS   A O   
1116 C  CB  A HIS   A 45  ? 0.1252 0.1224 0.1404 0.0005  -0.0042 0.0065  45  HIS   A CB  
1117 C  CB  B HIS   A 45  ? 0.1319 0.1374 0.1471 -0.0002 -0.0022 0.0041  45  HIS   A CB  
1118 C  CG  A HIS   A 45  ? 0.1318 0.1159 0.1375 -0.0049 0.0024  0.0137  45  HIS   A CG  
1119 C  CG  B HIS   A 45  ? 0.1241 0.1388 0.1286 0.0024  0.0049  0.0040  45  HIS   A CG  
1120 N  ND1 A HIS   A 45  ? 0.1248 0.1185 0.1461 -0.0043 0.0085  0.0066  45  HIS   A ND1 
1121 N  ND1 B HIS   A 45  ? 0.1165 0.1427 0.1386 0.0029  -0.0042 0.0148  45  HIS   A ND1 
1122 C  CD2 A HIS   A 45  ? 0.1348 0.1229 0.1532 -0.0026 -0.0048 0.0146  45  HIS   A CD2 
1123 C  CD2 B HIS   A 45  ? 0.1178 0.1324 0.1194 0.0020  -0.0016 -0.0026 45  HIS   A CD2 
1124 C  CE1 A HIS   A 45  ? 0.1302 0.1265 0.1424 -0.0033 0.0078  0.0160  45  HIS   A CE1 
1125 C  CE1 B HIS   A 45  ? 0.1137 0.1310 0.1087 -0.0015 -0.0055 0.0017  45  HIS   A CE1 
1126 N  NE2 A HIS   A 45  ? 0.1345 0.1254 0.1480 0.0017  0.0037  0.0219  45  HIS   A NE2 
1127 N  NE2 B HIS   A 45  ? 0.1146 0.1327 0.0974 -0.0042 -0.0056 -0.0040 45  HIS   A NE2 
1142 N  N   A GLY   A 46  ? 0.1349 0.1480 0.1707 0.0135  -0.0049 0.0258  46  GLY   A N   
1143 N  N   B GLY   A 46  ? 0.1482 0.1563 0.1706 0.0017  -0.0035 0.0174  46  GLY   A N   
1144 C  CA  A GLY   A 46  ? 0.1319 0.1567 0.1861 0.0162  -0.0080 0.0354  46  GLY   A CA  
1145 C  CA  B GLY   A 46  ? 0.1370 0.1609 0.1505 0.0000  0.0016  0.0244  46  GLY   A CA  
1146 C  C   A GLY   A 46  ? 0.1411 0.1494 0.1807 0.0220  -0.0042 0.0469  46  GLY   A C   
1147 C  C   B GLY   A 46  ? 0.1361 0.1576 0.1188 0.0004  0.0140  0.0278  46  GLY   A C   
1148 O  O   A GLY   A 46  ? 0.1533 0.1517 0.1800 0.0201  -0.0142 0.0436  46  GLY   A O   
1149 O  O   B GLY   A 46  ? 0.1406 0.1635 0.1048 -0.0038 0.0054  0.0212  46  GLY   A O   
1156 N  N   A GLY   A 47  ? 0.1456 0.1467 0.1664 0.0210  -0.0086 0.0363  47  GLY   A N   
1157 N  N   B GLY   A 47  ? 0.1366 0.1559 0.1247 0.0029  0.0139  0.0137  47  GLY   A N   
1158 C  CA  A GLY   A 47  ? 0.1512 0.1604 0.1623 0.0196  -0.0128 0.0275  47  GLY   A CA  
1159 C  CA  B GLY   A 47  ? 0.1314 0.1590 0.1154 -0.0020 0.0099  0.0246  47  GLY   A CA  
1160 C  C   A GLY   A 47  ? 0.1417 0.1563 0.1398 0.0183  -0.0138 0.0150  47  GLY   A C   
1161 C  C   B GLY   A 47  ? 0.1259 0.1507 0.0937 0.0061  0.0073  0.0125  47  GLY   A C   
1162 O  O   A GLY   A 47  ? 0.1417 0.1504 0.1618 0.0182  -0.0163 0.0161  47  GLY   A O   
1163 O  O   B GLY   A 47  ? 0.1270 0.1468 0.0911 0.0100  0.0088  0.0213  47  GLY   A O   
1170 N  N   A GLY   A 48  ? 0.1433 0.1579 0.1373 0.0218  -0.0184 0.0094  48  GLY   A N   
1171 N  N   B GLY   A 48  ? 0.1246 0.1445 0.1036 0.0056  0.0151  0.0087  48  GLY   A N   
1172 C  CA  A GLY   A 48  ? 0.1415 0.1510 0.1580 0.0053  -0.0187 -0.0105 48  GLY   A CA  
1173 C  CA  B GLY   A 48  ? 0.1234 0.1283 0.1073 0.0057  0.0177  -0.0048 48  GLY   A CA  
1174 C  C   A GLY   A 48  ? 0.1369 0.1497 0.1468 -0.0054 -0.0002 -0.0015 48  GLY   A C   
1175 C  C   B GLY   A 48  ? 0.1307 0.1246 0.1117 0.0008  0.0140  0.0070  48  GLY   A C   
1176 O  O   A GLY   A 48  ? 0.1478 0.1467 0.1400 -0.0052 0.0018  0.0068  48  GLY   A O   
1177 O  O   B GLY   A 48  ? 0.1493 0.1244 0.1027 -0.0005 0.0306  0.0043  48  GLY   A O   
1184 N  N   A VAL   A 49  ? 0.1345 0.1473 0.1698 -0.0081 -0.0165 0.0036  49  VAL   A N   
1185 N  N   B VAL   A 49  ? 0.1224 0.1212 0.1274 0.0022  -0.0042 0.0085  49  VAL   A N   
1186 C  CA  A VAL   A 49  ? 0.1441 0.1361 0.1604 -0.0102 0.0047  0.0037  49  VAL   A CA  
1187 C  CA  B VAL   A 49  ? 0.1187 0.1276 0.1302 0.0004  -0.0053 0.0087  49  VAL   A CA  
1188 C  C   A VAL   A 49  ? 0.1388 0.1300 0.1383 -0.0057 -0.0017 0.0097  49  VAL   A C   
1189 C  C   B VAL   A 49  ? 0.1186 0.1284 0.1182 0.0048  -0.0077 -0.0032 49  VAL   A C   
1190 O  O   A VAL   A 49  ? 0.1422 0.1318 0.1384 -0.0128 0.0005  0.0037  49  VAL   A O   
1191 O  O   B VAL   A 49  ? 0.1180 0.1280 0.1233 0.0106  -0.0088 0.0036  49  VAL   A O   
1192 C  CB  A VAL   A 49  ? 0.1616 0.1373 0.1963 -0.0161 0.0057  -0.0036 49  VAL   A CB  
1193 C  CB  B VAL   A 49  ? 0.1166 0.1250 0.1426 0.0048  -0.0005 0.0116  49  VAL   A CB  
1194 C  CG1 A VAL   A 49  ? 0.1716 0.1384 0.2107 -0.0128 0.0009  0.0012  49  VAL   A CG1 
1195 C  CG1 B VAL   A 49  ? 0.1005 0.1301 0.1358 0.0152  -0.0059 0.0240  49  VAL   A CG1 
1196 C  CG2 A VAL   A 49  ? 0.1733 0.1566 0.2436 -0.0359 0.0067  -0.0044 49  VAL   A CG2 
1197 C  CG2 B VAL   A 49  ? 0.1204 0.1224 0.1605 0.0061  -0.0007 0.0220  49  VAL   A CG2 
1216 N  N   A ALA   A 50  ? 0.1307 0.1282 0.1392 -0.0050 -0.0152 0.0156  50  ALA   A N   
1217 N  N   B ALA   A 50  ? 0.1205 0.1271 0.1097 0.0013  -0.0034 -0.0079 50  ALA   A N   
1218 C  CA  A ALA   A 50  ? 0.1280 0.1235 0.1429 -0.0110 -0.0136 0.0171  50  ALA   A CA  
1219 C  CA  B ALA   A 50  ? 0.1229 0.1228 0.1110 -0.0081 -0.0023 -0.0137 50  ALA   A CA  
1220 C  C   A ALA   A 50  ? 0.1204 0.1331 0.1375 -0.0080 -0.0049 0.0122  50  ALA   A C   
1221 C  C   B ALA   A 50  ? 0.1218 0.1258 0.1039 -0.0131 0.0035  -0.0095 50  ALA   A C   
1222 O  O   A ALA   A 50  ? 0.1270 0.1361 0.1567 0.0051  -0.0124 0.0095  50  ALA   A O   
1223 O  O   B ALA   A 50  ? 0.1248 0.1270 0.0938 -0.0150 0.0076  -0.0009 50  ALA   A O   
1224 C  CB  A ALA   A 50  ? 0.1280 0.1309 0.1522 -0.0035 -0.0113 0.0174  50  ALA   A CB  
1225 C  CB  B ALA   A 50  ? 0.1259 0.1222 0.1072 -0.0076 0.0111  -0.0312 50  ALA   A CB  
1236 N  N   A GLY   A 51  ? 0.1231 0.1288 0.1379 0.0027  -0.0134 0.0157  51  GLY   A N   
1237 N  N   B GLY   A 51  ? 0.1290 0.1219 0.1275 -0.0094 -0.0045 -0.0150 51  GLY   A N   
1238 C  CA  A GLY   A 51  ? 0.1406 0.1221 0.1519 0.0037  -0.0153 0.0201  51  GLY   A CA  
1239 C  CA  B GLY   A 51  ? 0.1402 0.1211 0.1070 -0.0062 -0.0081 -0.0284 51  GLY   A CA  
1240 C  C   A GLY   A 51  ? 0.1213 0.1243 0.1504 0.0049  -0.0072 0.0137  51  GLY   A C   
1241 C  C   B GLY   A 51  ? 0.1371 0.1290 0.1136 -0.0025 -0.0039 -0.0288 51  GLY   A C   
1242 O  O   A GLY   A 51  ? 0.1249 0.1366 0.1654 -0.0043 -0.0149 0.0010  51  GLY   A O   
1243 O  O   B GLY   A 51  ? 0.1379 0.1362 0.1214 -0.0045 0.0087  -0.0302 51  GLY   A O   
1250 N  N   A ALA   A 52  ? 0.1195 0.1369 0.1431 0.0037  -0.0087 0.0102  52  ALA   A N   
1251 N  N   B ALA   A 52  ? 0.1415 0.1323 0.0997 -0.0047 -0.0100 -0.0351 52  ALA   A N   
1252 C  CA  A ALA   A 52  ? 0.1286 0.1480 0.1477 -0.0014 -0.0008 0.0124  52  ALA   A CA  
1253 C  CA  B ALA   A 52  ? 0.1411 0.1338 0.1190 -0.0069 -0.0105 -0.0241 52  ALA   A CA  
1254 C  C   A ALA   A 52  ? 0.1304 0.1465 0.1389 -0.0006 0.0069  0.0070  52  ALA   A C   
1255 C  C   B ALA   A 52  ? 0.1353 0.1332 0.1134 -0.0086 0.0028  -0.0224 52  ALA   A C   
1256 O  O   A ALA   A 52  ? 0.1406 0.1599 0.1477 -0.0024 -0.0001 0.0057  52  ALA   A O   
1257 O  O   B ALA   A 52  ? 0.1379 0.1340 0.1288 -0.0132 0.0148  -0.0228 52  ALA   A O   
1258 C  CB  A ALA   A 52  ? 0.1420 0.1740 0.1720 -0.0013 -0.0021 0.0221  52  ALA   A CB  
1259 C  CB  B ALA   A 52  ? 0.1484 0.1518 0.1497 -0.0032 -0.0130 -0.0173 52  ALA   A CB  
1270 N  N   A LEU   A 53  ? 0.1224 0.1419 0.1488 -0.0028 0.0036  0.0133  53  LEU   A N   
1271 N  N   B LEU   A 53  ? 0.1290 0.1373 0.1141 -0.0014 -0.0059 -0.0097 53  LEU   A N   
1272 C  CA  A LEU   A 53  ? 0.1339 0.1470 0.1444 -0.0110 0.0006  0.0091  53  LEU   A CA  
1273 C  CA  B LEU   A 53  ? 0.1296 0.1414 0.1061 -0.0020 -0.0062 -0.0113 53  LEU   A CA  
1274 C  C   A LEU   A 53  ? 0.1402 0.1428 0.1150 -0.0008 0.0018  0.0079  53  LEU   A C   
1275 C  C   B LEU   A 53  ? 0.1355 0.1430 0.1079 0.0063  0.0033  -0.0092 53  LEU   A C   
1276 O  O   A LEU   A 53  ? 0.1516 0.1499 0.1291 -0.0162 0.0008  0.0013  53  LEU   A O   
1277 O  O   B LEU   A 53  ? 0.1438 0.1459 0.1182 -0.0002 0.0112  -0.0121 53  LEU   A O   
1278 C  CB  A LEU   A 53  ? 0.1417 0.1493 0.1647 -0.0097 0.0037  0.0148  53  LEU   A CB  
1279 C  CB  B LEU   A 53  ? 0.1251 0.1422 0.0972 -0.0065 -0.0132 -0.0083 53  LEU   A CB  
1280 C  CG  A LEU   A 53  ? 0.1445 0.1504 0.1583 -0.0043 -0.0015 0.0168  53  LEU   A CG  
1281 C  CG  B LEU   A 53  ? 0.1253 0.1439 0.1107 -0.0088 -0.0187 -0.0068 53  LEU   A CG  
1282 C  CD1 A LEU   A 53  ? 0.1488 0.1594 0.1527 0.0006  -0.0049 0.0254  53  LEU   A CD1 
1283 C  CD1 B LEU   A 53  ? 0.1283 0.1495 0.1192 -0.0176 -0.0154 -0.0140 53  LEU   A CD1 
1284 C  CD2 A LEU   A 53  ? 0.1641 0.1661 0.1867 -0.0165 -0.0021 0.0178  53  LEU   A CD2 
1285 C  CD2 B LEU   A 53  ? 0.1314 0.1433 0.1136 -0.0066 -0.0144 -0.0034 53  LEU   A CD2 
1308 N  N   A ASN   A 54  ? 0.1350 0.1330 0.1245 -0.0085 -0.0072 0.0146  54  ASN   A N   
1309 N  N   B ASN   A 54  ? 0.1332 0.1424 0.1232 0.0076  -0.0011 -0.0034 54  ASN   A N   
1310 C  CA  A ASN   A 54  ? 0.1257 0.1239 0.1404 -0.0064 -0.0071 0.0072  54  ASN   A CA  
1311 C  CA  B ASN   A 54  ? 0.1254 0.1411 0.1299 0.0082  -0.0075 -0.0066 54  ASN   A CA  
1312 C  C   A ASN   A 54  ? 0.1359 0.1349 0.1315 -0.0134 0.0052  0.0052  54  ASN   A C   
1313 C  C   B ASN   A 54  ? 0.1307 0.1372 0.1279 0.0015  -0.0043 -0.0093 54  ASN   A C   
1314 O  O   A ASN   A 54  ? 0.1438 0.1474 0.1355 -0.0170 -0.0050 -0.0022 54  ASN   A O   
1315 O  O   B ASN   A 54  ? 0.1325 0.1323 0.1218 0.0040  -0.0169 -0.0220 54  ASN   A O   
1316 C  CB  A ASN   A 54  ? 0.1259 0.1262 0.1498 -0.0101 -0.0109 0.0012  54  ASN   A CB  
1317 C  CB  B ASN   A 54  ? 0.1278 0.1501 0.1358 0.0143  -0.0071 0.0008  54  ASN   A CB  
1318 C  CG  A ASN   A 54  ? 0.1227 0.1213 0.1630 -0.0104 0.0011  -0.0002 54  ASN   A CG  
1319 C  CG  B ASN   A 54  ? 0.1240 0.1528 0.1406 0.0162  0.0019  0.0038  54  ASN   A CG  
1320 O  OD1 A ASN   A 54  ? 0.1222 0.1255 0.1597 -0.0131 -0.0078 0.0107  54  ASN   A OD1 
1321 O  OD1 B ASN   A 54  ? 0.1216 0.1640 0.1519 0.0103  -0.0040 0.0055  54  ASN   A OD1 
1322 N  ND2 A ASN   A 54  ? 0.1252 0.1307 0.1740 -0.0153 -0.0058 0.0081  54  ASN   A ND2 
1323 N  ND2 B ASN   A 54  ? 0.1291 0.1527 0.1380 0.0151  -0.0007 0.0128  54  ASN   A ND2 
1336 N  N   . LYS   A 55  ? 0.1286 0.1341 0.1516 -0.0007 0.0021  -0.0091 55  LYS   A N   
1337 C  CA  . LYS   A 55  ? 0.1383 0.1468 0.1569 0.0052  -0.0071 -0.0185 55  LYS   A CA  
1338 C  C   . LYS   A 55  ? 0.1307 0.1561 0.1500 -0.0070 -0.0067 -0.0224 55  LYS   A C   
1339 O  O   . LYS   A 55  ? 0.1456 0.1698 0.1616 0.0009  -0.0080 -0.0247 55  LYS   A O   
1340 C  CB  . LYS   A 55  ? 0.1428 0.1587 0.1676 0.0152  -0.0026 -0.0220 55  LYS   A CB  
1341 C  CG  . LYS   A 55  ? 0.1598 0.1905 0.1842 0.0327  -0.0204 -0.0231 55  LYS   A CG  
1342 C  CD  . LYS   A 55  ? 0.1788 0.2150 0.2062 0.0462  -0.0121 -0.0195 55  LYS   A CD  
1343 C  CE  . LYS   A 55  ? 0.2018 0.2458 0.2262 0.0589  -0.0288 -0.0217 55  LYS   A CE  
1344 N  NZ  . LYS   A 55  ? 0.2123 0.2675 0.2437 0.0711  -0.0352 -0.0180 55  LYS   A NZ  
1359 N  N   . ALA   A 56  ? 0.1406 0.1629 0.1498 -0.0074 -0.0046 -0.0158 56  ALA   A N   
1360 C  CA  . ALA   A 56  ? 0.1540 0.1789 0.1526 -0.0103 0.0040  -0.0136 56  ALA   A CA  
1361 C  C   . ALA   A 56  ? 0.1569 0.1904 0.1239 -0.0045 0.0077  -0.0227 56  ALA   A C   
1362 O  O   . ALA   A 56  ? 0.1577 0.2270 0.1422 0.0066  0.0096  -0.0198 56  ALA   A O   
1363 C  CB  . ALA   A 56  ? 0.1610 0.1995 0.1549 -0.0176 0.0092  -0.0088 56  ALA   A CB  
1369 N  N   . THR   A 57  ? 0.1395 0.1688 0.1383 -0.0037 0.0014  -0.0204 57  THR   A N   
1370 C  CA  . THR   A 57  ? 0.1484 0.1677 0.1311 -0.0121 -0.0049 -0.0121 57  THR   A CA  
1371 C  C   . THR   A 57  ? 0.1496 0.1766 0.1315 -0.0066 -0.0062 -0.0141 57  THR   A C   
1372 O  O   . THR   A 57  ? 0.1442 0.1713 0.1614 -0.0100 -0.0125 -0.0201 57  THR   A O   
1373 C  CB  . THR   A 57  ? 0.1423 0.1658 0.1366 -0.0109 0.0052  -0.0134 57  THR   A CB  
1374 O  OG1 . THR   A 57  ? 0.1291 0.1618 0.1461 -0.0030 0.0005  -0.0048 57  THR   A OG1 
1375 C  CG2 . THR   A 57  ? 0.1520 0.1622 0.1374 -0.0068 -0.0026 -0.0017 57  THR   A CG2 
1383 N  N   . ASN   A 58  ? 0.1399 0.1685 0.1638 -0.0096 0.0032  -0.0245 58  ASN   A N   
1384 C  CA  . ASN   A 58  ? 0.1640 0.1639 0.1858 -0.0095 0.0042  -0.0269 58  ASN   A CA  
1385 C  C   . ASN   A 58  ? 0.1482 0.1425 0.1687 0.0038  0.0025  -0.0212 58  ASN   A C   
1386 O  O   . ASN   A 58  ? 0.1535 0.1559 0.1870 -0.0123 -0.0090 -0.0229 58  ASN   A O   
1387 C  CB  . ASN   A 58  ? 0.2137 0.1787 0.2065 -0.0151 0.0344  -0.0479 58  ASN   A CB  
1388 C  CG  . ASN   A 58  ? 0.2521 0.2055 0.2738 -0.0165 0.0275  -0.0263 58  ASN   A CG  
1389 O  OD1 . ASN   A 58  ? 0.2793 0.1988 0.3223 0.0210  0.0559  -0.0169 58  ASN   A OD1 
1390 N  ND2 . ASN   A 58  ? 0.2607 0.2158 0.3001 -0.0247 0.0079  -0.0252 58  ASN   A ND2 
1397 N  N   . ASN   A 59  ? 0.1387 0.1407 0.1620 -0.0031 -0.0168 -0.0134 59  ASN   A N   
1398 C  CA  . ASN   A 59  ? 0.1351 0.1345 0.1616 -0.0064 -0.0002 -0.0088 59  ASN   A CA  
1399 C  C   . ASN   A 59  ? 0.1351 0.1391 0.1413 -0.0065 -0.0030 0.0013  59  ASN   A C   
1400 O  O   . ASN   A 59  ? 0.1372 0.1405 0.1460 -0.0066 -0.0057 0.0029  59  ASN   A O   
1401 C  CB  . ASN   A 59  ? 0.1443 0.1307 0.1577 0.0001  -0.0172 -0.0173 59  ASN   A CB  
1402 C  CG  . ASN   A 59  ? 0.1482 0.1335 0.1639 -0.0023 -0.0279 0.0004  59  ASN   A CG  
1403 O  OD1 . ASN   A 59  ? 0.1566 0.1435 0.1534 -0.0150 -0.0186 0.0013  59  ASN   A OD1 
1404 N  ND2 . ASN   A 59  ? 0.1531 0.1433 0.1779 -0.0190 -0.0197 0.0080  59  ASN   A ND2 
1411 N  N   . ALA   A 60  ? 0.1290 0.1434 0.1408 -0.0044 -0.0063 0.0022  60  ALA   A N   
1412 C  CA  . ALA   A 60  ? 0.1294 0.1433 0.1567 0.0016  -0.0129 -0.0017 60  ALA   A CA  
1413 C  C   . ALA   A 60  ? 0.1337 0.1349 0.1656 -0.0044 -0.0073 -0.0013 60  ALA   A C   
1414 O  O   . ALA   A 60  ? 0.1260 0.1347 0.1782 -0.0048 -0.0093 -0.0049 60  ALA   A O   
1415 C  CB  . ALA   A 60  ? 0.1421 0.1518 0.1532 0.0050  -0.0090 -0.0202 60  ALA   A CB  
1421 N  N   . MET   A 61  ? 0.1305 0.1350 0.1471 -0.0071 -0.0019 -0.0047 61  MET   A N   
1422 C  CA  . MET   A 61  ? 0.1292 0.1348 0.1545 -0.0111 -0.0001 -0.0008 61  MET   A CA  
1423 C  C   . MET   A 61  ? 0.1230 0.1289 0.1607 -0.0089 -0.0009 -0.0049 61  MET   A C   
1424 O  O   . MET   A 61  ? 0.1305 0.1281 0.1594 -0.0032 0.0066  0.0044  61  MET   A O   
1425 C  CB  . MET   A 61  ? 0.1397 0.1340 0.1411 -0.0105 -0.0011 0.0008  61  MET   A CB  
1426 C  CG  . MET   A 61  ? 0.1379 0.1410 0.1580 -0.0049 -0.0062 0.0024  61  MET   A CG  
1427 S  SD  . MET   A 61  ? 0.1425 0.1444 0.1912 -0.0105 -0.0007 -0.0172 61  MET   A SD  
1428 C  CE  . MET   A 61  ? 0.1593 0.1543 0.2258 -0.0132 0.0169  -0.0038 61  MET   A CE  
1438 N  N   . GLN   A 62  ? 0.1316 0.1279 0.1518 -0.0074 -0.0100 0.0017  62  GLN   A N   
1439 C  CA  . GLN   A 62  ? 0.1300 0.1241 0.1716 -0.0037 -0.0022 0.0044  62  GLN   A CA  
1440 C  C   . GLN   A 62  ? 0.1295 0.1166 0.1696 0.0038  0.0005  0.0021  62  GLN   A C   
1441 O  O   . GLN   A 62  ? 0.1335 0.1332 0.1689 0.0004  0.0058  -0.0024 62  GLN   A O   
1442 C  CB  . GLN   A 62  ? 0.1301 0.1201 0.1729 -0.0039 -0.0033 0.0013  62  GLN   A CB  
1443 C  CG  . GLN   A 62  ? 0.1305 0.1241 0.1594 -0.0043 -0.0081 0.0169  62  GLN   A CG  
1444 C  CD  . GLN   A 62  ? 0.1367 0.1304 0.1594 -0.0045 0.0009  0.0131  62  GLN   A CD  
1445 O  OE1 . GLN   A 62  ? 0.1408 0.1415 0.1684 -0.0048 0.0022  0.0017  62  GLN   A OE1 
1446 N  NE2 . GLN   A 62  ? 0.1396 0.1316 0.1599 0.0035  0.0032  0.0009  62  GLN   A NE2 
1455 N  N   . VAL   A 63  ? 0.1286 0.1274 0.1845 -0.0046 0.0049  -0.0132 63  VAL   A N   
1456 C  CA  . VAL   A 63  ? 0.1250 0.1357 0.1981 -0.0139 -0.0021 -0.0085 63  VAL   A CA  
1457 C  C   . VAL   A 63  ? 0.1157 0.1370 0.1807 -0.0074 -0.0073 -0.0095 63  VAL   A C   
1458 O  O   . VAL   A 63  ? 0.1241 0.1400 0.2000 -0.0116 -0.0035 -0.0082 63  VAL   A O   
1459 C  CB  . VAL   A 63  ? 0.1446 0.1606 0.2268 -0.0152 -0.0095 -0.0356 63  VAL   A CB  
1460 C  CG1 . VAL   A 63  ? 0.1551 0.1825 0.2763 -0.0147 -0.0089 -0.0673 63  VAL   A CG1 
1461 C  CG2 . VAL   A 63  ? 0.1497 0.1486 0.2456 -0.0107 0.0140  -0.0309 63  VAL   A CG2 
1471 N  N   . GLU   A 64  ? 0.1251 0.1451 0.1749 -0.0027 -0.0037 -0.0013 64  GLU   A N   
1472 C  CA  . GLU   A 64  ? 0.1272 0.1424 0.1711 -0.0058 -0.0133 0.0088  64  GLU   A CA  
1473 C  C   . GLU   A 64  ? 0.1185 0.1423 0.1764 -0.0034 0.0024  0.0039  64  GLU   A C   
1474 O  O   . GLU   A 64  ? 0.1264 0.1499 0.1745 -0.0055 0.0019  0.0000  64  GLU   A O   
1475 C  CB  . GLU   A 64  ? 0.1346 0.1526 0.1781 -0.0017 -0.0065 -0.0001 64  GLU   A CB  
1476 C  CG  . GLU   A 64  ? 0.1490 0.1550 0.1982 -0.0083 -0.0046 0.0032  64  GLU   A CG  
1477 C  CD  . GLU   A 64  ? 0.1627 0.1643 0.2027 -0.0138 0.0093  0.0041  64  GLU   A CD  
1478 O  OE1 . GLU   A 64  ? 0.1638 0.1788 0.2289 -0.0194 0.0101  0.0051  64  GLU   A OE1 
1479 O  OE2 . GLU   A 64  ? 0.1817 0.1700 0.1887 -0.0199 -0.0059 0.0078  64  GLU   A OE2 
1486 N  N   . SER   A 65  ? 0.1186 0.1375 0.1671 0.0058  -0.0019 0.0060  65  SER   A N   
1487 C  CA  . SER   A 65  ? 0.1280 0.1345 0.1534 0.0008  -0.0006 -0.0023 65  SER   A CA  
1488 C  C   . SER   A 65  ? 0.1222 0.1465 0.1537 -0.0059 -0.0003 0.0037  65  SER   A C   
1489 O  O   . SER   A 65  ? 0.1300 0.1514 0.1767 0.0004  0.0097  -0.0025 65  SER   A O   
1490 C  CB  . SER   A 65  ? 0.1273 0.1299 0.1599 -0.0073 0.0031  0.0088  65  SER   A CB  
1491 O  OG  . SER   A 65  ? 0.1327 0.1377 0.1697 -0.0060 -0.0028 0.0091  65  SER   A OG  
1497 N  N   . ASP   A 66  ? 0.1316 0.1298 0.1709 -0.0081 0.0092  0.0088  66  ASP   A N   
1498 C  CA  . ASP   A 66  ? 0.1430 0.1390 0.1796 -0.0033 0.0135  0.0159  66  ASP   A CA  
1499 C  C   . ASP   A 66  ? 0.1377 0.1397 0.1880 -0.0030 0.0097  0.0159  66  ASP   A C   
1500 O  O   . ASP   A 66  ? 0.1422 0.1492 0.2125 -0.0008 0.0243  0.0250  66  ASP   A O   
1501 C  CB  . ASP   A 66  ? 0.1550 0.1486 0.2188 0.0062  0.0145  0.0348  66  ASP   A CB  
1502 C  CG  . ASP   A 66  ? 0.1761 0.1654 0.2426 0.0028  0.0134  0.0509  66  ASP   A CG  
1503 O  OD1 . ASP   A 66  ? 0.1762 0.1938 0.2274 -0.0049 0.0004  0.0550  66  ASP   A OD1 
1504 O  OD2 . ASP   A 66  ? 0.1919 0.1856 0.3213 0.0198  -0.0057 0.0287  66  ASP   A OD2 
1509 N  N   . ASP   A 67  ? 0.1323 0.1461 0.1996 -0.0008 0.0109  0.0242  67  ASP   A N   
1510 C  CA  . ASP   A 67  ? 0.1349 0.1646 0.2149 0.0020  0.0065  0.0232  67  ASP   A CA  
1511 C  C   . ASP   A 67  ? 0.1352 0.1643 0.2090 0.0044  0.0165  0.0272  67  ASP   A C   
1512 O  O   . ASP   A 67  ? 0.1323 0.1722 0.2250 0.0056  0.0228  0.0335  67  ASP   A O   
1513 C  CB  . ASP   A 67  ? 0.1490 0.1759 0.2469 -0.0025 -0.0115 0.0329  67  ASP   A CB  
1514 C  CG  . ASP   A 67  ? 0.1463 0.1881 0.2848 -0.0108 -0.0272 0.0403  67  ASP   A CG  
1515 O  OD1 . ASP   A 67  ? 0.1479 0.2065 0.3777 -0.0114 -0.0362 0.0511  67  ASP   A OD1 
1516 O  OD2 . ASP   A 67  ? 0.1434 0.1940 0.2531 0.0031  -0.0084 0.0300  67  ASP   A OD2 
1521 N  N   . TYR   A 68  ? 0.1368 0.1477 0.2108 0.0035  0.0203  0.0341  68  TYR   A N   
1522 C  CA  . TYR   A 68  ? 0.1470 0.1428 0.1904 -0.0012 0.0273  0.0225  68  TYR   A CA  
1523 C  C   . TYR   A 68  ? 0.1366 0.1394 0.1926 0.0039  0.0275  0.0149  68  TYR   A C   
1524 O  O   . TYR   A 68  ? 0.1465 0.1455 0.2094 0.0120  0.0287  0.0206  68  TYR   A O   
1525 C  CB  . TYR   A 68  ? 0.1533 0.1414 0.2111 0.0082  0.0418  0.0270  68  TYR   A CB  
1526 C  CG  . TYR   A 68  ? 0.1573 0.1605 0.2490 0.0056  0.0531  0.0308  68  TYR   A CG  
1527 C  CD1 . TYR   A 68  ? 0.1671 0.1708 0.2799 -0.0154 0.0407  -0.0113 68  TYR   A CD1 
1528 C  CD2 . TYR   A 68  ? 0.1766 0.1671 0.3104 0.0116  0.0602  0.0295  68  TYR   A CD2 
1529 C  CE1 . TYR   A 68  ? 0.1789 0.1816 0.3109 -0.0135 0.0503  -0.0192 68  TYR   A CE1 
1530 C  CE2 . TYR   A 68  ? 0.1791 0.1709 0.3247 0.0050  0.0687  0.0014  68  TYR   A CE2 
1531 C  CZ  . TYR   A 68  ? 0.1791 0.1710 0.3356 -0.0185 0.0560  -0.0304 68  TYR   A CZ  
1532 O  OH  . TYR   A 68  ? 0.2059 0.1824 0.3669 -0.0156 0.0414  -0.0580 68  TYR   A OH  
1542 N  N   . ILE   A 69  ? 0.1264 0.1371 0.1972 0.0004  0.0220  0.0165  69  ILE   A N   
1543 C  CA  . ILE   A 69  ? 0.1370 0.1446 0.1957 0.0043  0.0202  0.0044  69  ILE   A CA  
1544 C  C   . ILE   A 69  ? 0.1396 0.1505 0.1784 0.0073  0.0254  0.0231  69  ILE   A C   
1545 O  O   . ILE   A 69  ? 0.1440 0.1547 0.1838 0.0040  0.0239  0.0234  69  ILE   A O   
1546 C  CB  . ILE   A 69  ? 0.1449 0.1670 0.1941 0.0019  0.0187  -0.0108 69  ILE   A CB  
1547 C  CG1 . ILE   A 69  ? 0.1478 0.1760 0.2000 0.0028  0.0189  -0.0177 69  ILE   A CG1 
1548 C  CG2 . ILE   A 69  ? 0.1627 0.1884 0.2190 0.0154  0.0052  -0.0242 69  ILE   A CG2 
1549 C  CD1 . ILE   A 69  ? 0.1487 0.1830 0.2184 -0.0057 0.0150  -0.0202 69  ILE   A CD1 
1561 N  N   . ALA   A 70  ? 0.1423 0.1490 0.1839 -0.0074 0.0205  0.0177  70  ALA   A N   
1562 C  CA  . ALA   A 70  ? 0.1496 0.1604 0.2109 -0.0170 0.0261  0.0298  70  ALA   A CA  
1563 C  C   . ALA   A 70  ? 0.1504 0.1731 0.2166 -0.0070 0.0287  0.0248  70  ALA   A C   
1564 O  O   . ALA   A 70  ? 0.1667 0.2049 0.2257 0.0161  0.0432  0.0377  70  ALA   A O   
1565 C  CB  . ALA   A 70  ? 0.1504 0.1571 0.2392 -0.0194 0.0252  0.0218  70  ALA   A CB  
1571 N  N   . THR   A 71  ? 0.1458 0.1684 0.2157 -0.0002 0.0201  0.0304  71  THR   A N   
1572 C  CA  . THR   A 71  ? 0.1544 0.1895 0.2364 0.0123  0.0260  0.0328  71  THR   A CA  
1573 C  C   . THR   A 71  ? 0.1437 0.1852 0.2581 0.0158  0.0365  0.0301  71  THR   A C   
1574 O  O   . THR   A 71  ? 0.1507 0.2103 0.3036 0.0118  0.0431  0.0049  71  THR   A O   
1575 C  CB  . THR   A 71  ? 0.1881 0.2155 0.2614 0.0244  -0.0098 0.0442  71  THR   A CB  
1576 O  OG1 . THR   A 71  ? 0.2194 0.2322 0.2709 0.0160  -0.0313 0.0263  71  THR   A OG1 
1577 C  CG2 . THR   A 71  ? 0.1977 0.2350 0.2895 0.0316  -0.0216 0.0696  71  THR   A CG2 
1585 N  N   . ASN   A 72  ? 0.1467 0.1673 0.2396 0.0156  0.0329  0.0263  72  ASN   A N   
1586 C  CA  . ASN   A 72  ? 0.1565 0.1649 0.2324 0.0207  0.0391  0.0294  72  ASN   A CA  
1587 C  C   . ASN   A 72  ? 0.1691 0.1652 0.2302 0.0116  0.0471  0.0224  72  ASN   A C   
1588 O  O   . ASN   A 72  ? 0.1903 0.1630 0.2561 0.0121  0.0470  0.0112  72  ASN   A O   
1589 C  CB  . ASN   A 72  ? 0.1748 0.1739 0.2295 0.0199  0.0455  0.0367  72  ASN   A CB  
1590 C  CG  . ASN   A 72  ? 0.2003 0.1970 0.2368 0.0271  0.0428  0.0366  72  ASN   A CG  
1591 O  OD1 . ASN   A 72  ? 0.2191 0.2305 0.2593 0.0259  0.0427  0.0330  72  ASN   A OD1 
1592 N  ND2 . ASN   A 72  ? 0.2125 0.1992 0.2449 0.0503  0.0283  0.0265  72  ASN   A ND2 
1599 N  N   . GLY   A 73  ? 0.1697 0.1577 0.2080 0.0072  0.0420  0.0163  73  GLY   A N   
1600 C  CA  . GLY   A 73  ? 0.1801 0.1542 0.1915 -0.0044 0.0428  0.0183  73  GLY   A CA  
1601 C  C   . GLY   A 73  ? 0.1752 0.1470 0.1741 0.0043  0.0448  0.0363  73  GLY   A C   
1602 O  O   . GLY   A 73  ? 0.1774 0.1523 0.1970 0.0125  0.0368  0.0269  73  GLY   A O   
1606 N  N   . PRO   A 74  ? 0.1832 0.1523 0.1827 -0.0061 0.0470  0.0177  74  PRO   A N   
1607 C  CA  . PRO   A 74  ? 0.1791 0.1454 0.1882 -0.0050 0.0447  0.0153  74  PRO   A CA  
1608 C  C   . PRO   A 74  ? 0.1697 0.1336 0.1963 -0.0054 0.0326  0.0096  74  PRO   A C   
1609 O  O   . PRO   A 74  ? 0.1758 0.1418 0.2247 0.0047  0.0366  -0.0000 74  PRO   A O   
1610 C  CB  . PRO   A 74  ? 0.1933 0.1753 0.2076 0.0024  0.0440  0.0326  74  PRO   A CB  
1611 C  CG  . PRO   A 74  ? 0.2158 0.2106 0.2519 -0.0160 0.0358  0.0236  74  PRO   A CG  
1612 C  CD  . PRO   A 74  ? 0.2002 0.1887 0.2044 -0.0172 0.0354  0.0151  74  PRO   A CD  
1620 N  N   . LEU   A 75  ? 0.1714 0.1262 0.1718 -0.0023 0.0256  0.0048  75  LEU   A N   
1621 C  CA  . LEU   A 75  ? 0.1737 0.1296 0.1491 0.0025  0.0134  0.0125  75  LEU   A CA  
1622 C  C   . LEU   A 75  ? 0.1802 0.1419 0.1417 0.0061  0.0152  0.0179  75  LEU   A C   
1623 O  O   . LEU   A 75  ? 0.2226 0.1578 0.1555 0.0105  0.0095  0.0094  75  LEU   A O   
1624 C  CB  . LEU   A 75  ? 0.1750 0.1386 0.1463 -0.0082 0.0134  0.0227  75  LEU   A CB  
1625 C  CG  . LEU   A 75  ? 0.1863 0.1751 0.1611 -0.0339 0.0133  0.0153  75  LEU   A CG  
1626 C  CD1 . LEU   A 75  ? 0.2015 0.2224 0.1783 -0.0324 0.0151  -0.0008 75  LEU   A CD1 
1627 C  CD2 . LEU   A 75  ? 0.2180 0.2179 0.2136 -0.0106 0.0097  0.0113  75  LEU   A CD2 
1639 N  N   . LYS   A 76  ? 0.1765 0.1372 0.1680 -0.0074 0.0139  -0.0008 76  LYS   A N   
1640 C  CA  . LYS   A 76  ? 0.1697 0.1576 0.1782 -0.0014 0.0150  -0.0076 76  LYS   A CA  
1641 C  C   . LYS   A 76  ? 0.1683 0.1425 0.1507 0.0006  0.0146  0.0051  76  LYS   A C   
1642 O  O   . LYS   A 76  ? 0.1700 0.1368 0.1516 -0.0045 0.0172  0.0102  76  LYS   A O   
1643 C  CB  . LYS   A 76  ? 0.1713 0.1816 0.2216 0.0097  0.0170  -0.0338 76  LYS   A CB  
1644 C  CG  . LYS   A 76  ? 0.1820 0.1696 0.2640 0.0147  0.0106  -0.0294 76  LYS   A CG  
1645 C  CD  . LYS   A 76  ? 0.1904 0.1741 0.3050 0.0161  -0.0022 -0.0249 76  LYS   A CD  
1646 C  CE  . LYS   A 76  ? 0.2092 0.1919 0.3667 0.0069  0.0078  -0.0334 76  LYS   A CE  
1647 N  NZ  . LYS   A 76  ? 0.2086 0.1892 0.4119 -0.0089 0.0009  -0.0405 76  LYS   A NZ  
1661 N  N   . VAL   A 77  ? 0.1819 0.1453 0.1430 -0.0045 0.0279  0.0168  77  VAL   A N   
1662 C  CA  . VAL   A 77  ? 0.1748 0.1429 0.1454 0.0069  0.0148  0.0164  77  VAL   A CA  
1663 C  C   . VAL   A 77  ? 0.1685 0.1443 0.1401 0.0081  0.0120  0.0072  77  VAL   A C   
1664 O  O   . VAL   A 77  ? 0.1752 0.1465 0.1425 0.0154  0.0239  -0.0001 77  VAL   A O   
1665 C  CB  . VAL   A 77  ? 0.1916 0.1615 0.1531 0.0063  0.0157  0.0214  77  VAL   A CB  
1666 C  CG1 . VAL   A 77  ? 0.1892 0.1808 0.1816 0.0144  0.0053  0.0058  77  VAL   A CG1 
1667 C  CG2 . VAL   A 77  ? 0.2135 0.1741 0.1690 0.0040  -0.0015 0.0151  77  VAL   A CG2 
1677 N  N   . GLY   A 78  ? 0.1631 0.1409 0.1477 0.0017  0.0156  0.0138  78  GLY   A N   
1678 C  CA  . GLY   A 78  ? 0.1622 0.1412 0.1618 -0.0028 0.0182  0.0152  78  GLY   A CA  
1679 C  C   . GLY   A 78  ? 0.1499 0.1299 0.1597 0.0013  0.0190  0.0163  78  GLY   A C   
1680 O  O   . GLY   A 78  ? 0.1459 0.1391 0.1785 0.0007  0.0177  0.0282  78  GLY   A O   
1684 N  N   . GLY   A 79  ? 0.1581 0.1313 0.1539 0.0049  0.0124  0.0131  79  GLY   A N   
1685 C  CA  . GLY   A 79  ? 0.1506 0.1388 0.1645 0.0064  0.0123  0.0170  79  GLY   A CA  
1686 C  C   . GLY   A 79  ? 0.1368 0.1320 0.1569 0.0007  0.0143  0.0089  79  GLY   A C   
1687 O  O   . GLY   A 79  ? 0.1422 0.1362 0.1630 0.0187  0.0088  0.0078  79  GLY   A O   
1691 N  N   . SER   A 80  ? 0.1316 0.1451 0.1780 0.0020  0.0181  -0.0029 80  SER   A N   
1692 C  CA  . SER   A 80  ? 0.1342 0.1390 0.1560 0.0011  0.0062  0.0042  80  SER   A CA  
1693 C  C   . SER   A 80  ? 0.1339 0.1442 0.1570 -0.0007 0.0073  0.0219  80  SER   A C   
1694 O  O   . SER   A 80  ? 0.1326 0.1641 0.1899 0.0127  0.0095  0.0012  80  SER   A O   
1695 C  CB  . SER   A 80  ? 0.1463 0.1364 0.1787 -0.0020 0.0090  0.0097  80  SER   A CB  
1696 O  OG  . SER   A 80  ? 0.1715 0.1426 0.2270 0.0026  -0.0033 0.0244  80  SER   A OG  
1702 N  N   . CYS   A 81  ? 0.1309 0.1347 0.1610 0.0029  0.0017  0.0165  81  CYS   A N   
1703 C  CA  . CYS   A 81  ? 0.1260 0.1441 0.1507 -0.0046 -0.0048 0.0212  81  CYS   A CA  
1704 C  C   . CYS   A 81  ? 0.1272 0.1406 0.1558 -0.0112 -0.0088 0.0242  81  CYS   A C   
1705 O  O   . CYS   A 81  ? 0.1237 0.1720 0.1713 0.0025  -0.0019 0.0374  81  CYS   A O   
1706 C  CB  . CYS   A 81  ? 0.1414 0.1510 0.1737 -0.0069 0.0048  0.0256  81  CYS   A CB  
1707 S  SG  . CYS   A 81  ? 0.1518 0.1424 0.1735 -0.0117 0.0020  0.0160  81  CYS   A SG  
1713 N  N   . VAL   A 82  ? 0.1304 0.1469 0.1605 -0.0010 -0.0138 0.0200  82  VAL   A N   
1714 C  CA  . VAL   A 82  ? 0.1427 0.1547 0.1562 0.0045  -0.0088 0.0242  82  VAL   A CA  
1715 C  C   . VAL   A 82  ? 0.1378 0.1584 0.1638 0.0063  -0.0027 0.0242  82  VAL   A C   
1716 O  O   . VAL   A 82  ? 0.1353 0.1640 0.1992 0.0038  -0.0022 -0.0062 82  VAL   A O   
1717 C  CB  . VAL   A 82  ? 0.1763 0.1648 0.1816 0.0068  -0.0049 0.0319  82  VAL   A CB  
1718 C  CG1 . VAL   A 82  ? 0.1979 0.1783 0.1963 0.0066  0.0025  0.0332  82  VAL   A CG1 
1719 C  CG2 . VAL   A 82  ? 0.1829 0.1656 0.2107 -0.0040 -0.0018 0.0317  82  VAL   A CG2 
1729 N  N   . LEU   A 83  ? 0.1338 0.1500 0.1624 -0.0098 -0.0096 0.0133  83  LEU   A N   
1730 C  CA  . LEU   A 83  ? 0.1415 0.1512 0.1487 -0.0097 -0.0152 0.0095  83  LEU   A CA  
1731 C  C   . LEU   A 83  ? 0.1451 0.1516 0.1539 -0.0122 -0.0208 0.0136  83  LEU   A C   
1732 O  O   . LEU   A 83  ? 0.1538 0.1562 0.1673 -0.0168 -0.0143 0.0175  83  LEU   A O   
1733 C  CB  . LEU   A 83  ? 0.1483 0.1564 0.1538 -0.0095 -0.0151 0.0122  83  LEU   A CB  
1734 C  CG  . LEU   A 83  ? 0.1565 0.1723 0.1660 -0.0138 0.0011  0.0070  83  LEU   A CG  
1735 C  CD1 . LEU   A 83  ? 0.1715 0.1767 0.1649 -0.0225 -0.0020 0.0204  83  LEU   A CD1 
1736 C  CD2 . LEU   A 83  ? 0.1548 0.1863 0.1844 -0.0150 0.0131  0.0226  83  LEU   A CD2 
1748 N  N   . SER   A 84  ? 0.1584 0.1596 0.1549 -0.0152 -0.0144 0.0179  84  SER   A N   
1749 C  CA  . SER   A 84  ? 0.1735 0.1632 0.1469 -0.0099 -0.0092 0.0154  84  SER   A CA  
1750 C  C   . SER   A 84  ? 0.1781 0.1612 0.1418 -0.0146 0.0006  0.0124  84  SER   A C   
1751 O  O   . SER   A 84  ? 0.1705 0.1761 0.1411 -0.0081 -0.0112 0.0150  84  SER   A O   
1752 C  CB  . SER   A 84  ? 0.1873 0.1873 0.1566 -0.0162 -0.0091 0.0098  84  SER   A CB  
1753 O  OG  . SER   A 84  ? 0.1853 0.2071 0.1542 -0.0188 -0.0243 0.0043  84  SER   A OG  
1759 N  N   . GLY   A 85  ? 0.1871 0.1721 0.1382 -0.0168 0.0074  0.0090  85  GLY   A N   
1760 C  CA  . GLY   A 85  ? 0.1921 0.1798 0.1675 -0.0177 0.0100  -0.0038 85  GLY   A CA  
1761 C  C   . GLY   A 85  ? 0.1857 0.1900 0.1438 -0.0159 -0.0105 0.0073  85  GLY   A C   
1762 O  O   . GLY   A 85  ? 0.1870 0.2089 0.1523 -0.0256 0.0145  -0.0141 85  GLY   A O   
1766 N  N   . HIS   A 86  ? 0.1793 0.1779 0.1394 -0.0138 -0.0120 0.0085  86  HIS   A N   
1767 C  CA  . HIS   A 86  ? 0.1975 0.1868 0.1427 -0.0150 -0.0150 0.0050  86  HIS   A CA  
1768 C  C   . HIS   A 86  ? 0.2214 0.2037 0.1187 -0.0191 -0.0146 0.0088  86  HIS   A C   
1769 O  O   . HIS   A 86  ? 0.2333 0.2268 0.1329 -0.0209 0.0039  0.0035  86  HIS   A O   
1770 C  CB  . HIS   A 86  ? 0.2005 0.1819 0.1451 -0.0089 -0.0020 0.0117  86  HIS   A CB  
1771 C  CG  . HIS   A 86  ? 0.1971 0.1829 0.1506 -0.0048 0.0072  0.0215  86  HIS   A CG  
1772 N  ND1 . HIS   A 86  ? 0.2037 0.1835 0.1922 -0.0135 -0.0030 0.0168  86  HIS   A ND1 
1773 C  CD2 . HIS   A 86  ? 0.1976 0.1797 0.1407 0.0060  0.0195  0.0203  86  HIS   A CD2 
1774 C  CE1 . HIS   A 86  ? 0.2000 0.1847 0.1872 -0.0108 0.0198  0.0238  86  HIS   A CE1 
1775 N  NE2 . HIS   A 86  ? 0.1974 0.1833 0.1702 0.0081  0.0243  0.0323  86  HIS   A NE2 
1783 N  N   . ASN   A 87  ? 0.2309 0.2146 0.1400 -0.0098 0.0072  -0.0024 87  ASN   A N   
1784 C  CA  . ASN   A 87  ? 0.2514 0.2311 0.1381 -0.0073 0.0230  -0.0128 87  ASN   A CA  
1785 C  C   . ASN   A 87  ? 0.2541 0.2400 0.1840 -0.0164 0.0513  -0.0006 87  ASN   A C   
1786 O  O   . ASN   A 87  ? 0.2769 0.2576 0.2290 -0.0294 0.0902  -0.0116 87  ASN   A O   
1787 C  CB  . ASN   A 87  ? 0.2675 0.2365 0.1616 0.0011  0.0205  -0.0141 87  ASN   A CB  
1788 C  CG  . ASN   A 87  ? 0.2803 0.2419 0.1579 0.0091  0.0426  -0.0025 87  ASN   A CG  
1789 O  OD1 . ASN   A 87  ? 0.2939 0.2356 0.1611 0.0280  0.0389  0.0091  87  ASN   A OD1 
1790 N  ND2 . ASN   A 87  ? 0.2840 0.2651 0.1600 0.0074  0.0459  0.0069  87  ASN   A ND2 
1797 N  N   . LEU   A 88  ? 0.2278 0.2225 0.1769 -0.0216 0.0262  0.0165  88  LEU   A N   
1798 C  CA  . LEU   A 88  ? 0.2090 0.2240 0.1915 -0.0291 0.0277  0.0221  88  LEU   A CA  
1799 C  C   . LEU   A 88  ? 0.2048 0.2306 0.1778 -0.0300 0.0245  0.0342  88  LEU   A C   
1800 O  O   . LEU   A 88  ? 0.2074 0.2326 0.2029 -0.0321 0.0235  0.0547  88  LEU   A O   
1801 C  CB  . LEU   A 88  ? 0.2084 0.2276 0.2026 -0.0356 -0.0067 0.0329  88  LEU   A CB  
1802 C  CG  . LEU   A 88  ? 0.2238 0.2406 0.2328 -0.0372 -0.0192 0.0369  88  LEU   A CG  
1803 C  CD1 . LEU   A 88  ? 0.2336 0.2526 0.2235 -0.0367 -0.0275 0.0218  88  LEU   A CD1 
1804 C  CD2 . LEU   A 88  ? 0.2351 0.2502 0.2714 -0.0319 -0.0215 0.0321  88  LEU   A CD2 
1816 N  N   . ALA   A 89  ? 0.2025 0.2211 0.1601 -0.0288 0.0144  0.0127  89  ALA   A N   
1817 C  CA  . ALA   A 89  ? 0.2032 0.2181 0.1459 -0.0212 0.0011  0.0251  89  ALA   A CA  
1818 C  C   . ALA   A 89  ? 0.2094 0.2183 0.1523 -0.0149 -0.0078 0.0247  89  ALA   A C   
1819 O  O   . ALA   A 89  ? 0.2032 0.2106 0.1997 -0.0257 -0.0108 -0.0040 89  ALA   A O   
1820 C  CB  . ALA   A 89  ? 0.1881 0.2172 0.1341 -0.0222 -0.0028 0.0214  89  ALA   A CB  
1826 N  N   . LYS   A 90  ? 0.2222 0.2350 0.1462 -0.0258 -0.0187 0.0284  90  LYS   A N   
1827 C  CA  . LYS   A 90  ? 0.2345 0.2495 0.1385 -0.0175 -0.0370 0.0232  90  LYS   A CA  
1828 C  C   . LYS   A 90  ? 0.2109 0.2255 0.1501 -0.0211 -0.0337 0.0117  90  LYS   A C   
1829 O  O   . LYS   A 90  ? 0.2126 0.2407 0.1850 -0.0239 -0.0445 -0.0029 90  LYS   A O   
1830 C  CB  . LYS   A 90  ? 0.2656 0.2875 0.1720 -0.0141 -0.0413 0.0528  90  LYS   A CB  
1831 C  CG  . LYS   A 90  ? 0.3110 0.3269 0.2730 -0.0121 -0.0400 0.0751  90  LYS   A CG  
1832 C  CD  . LYS   A 90  ? 0.3658 0.3737 0.3799 -0.0168 -0.0182 0.0795  90  LYS   A CD  
1833 C  CE  . LYS   A 90  ? 0.4105 0.4175 0.4610 -0.0205 -0.0009 0.0752  90  LYS   A CE  
1834 N  NZ  . LYS   A 90  ? 0.4383 0.4385 0.5183 -0.0242 0.0083  0.0729  90  LYS   A NZ  
1848 N  N   . HIS   A 91  ? 0.1972 0.1971 0.1162 -0.0179 -0.0338 0.0268  91  HIS   A N   
1849 C  CA  . HIS   A 91  ? 0.1842 0.1845 0.1246 -0.0158 -0.0261 0.0225  91  HIS   A CA  
1850 C  C   . HIS   A 91  ? 0.1652 0.1732 0.1092 -0.0123 -0.0125 0.0259  91  HIS   A C   
1851 O  O   . HIS   A 91  ? 0.1564 0.1832 0.1461 -0.0213 -0.0096 0.0278  91  HIS   A O   
1852 C  CB  . HIS   A 91  ? 0.2048 0.2153 0.1827 0.0074  -0.0465 0.0252  91  HIS   A CB  
1853 C  CG  . HIS   A 91  ? 0.2457 0.2669 0.2480 0.0203  -0.0696 0.0110  91  HIS   A CG  
1854 N  ND1 . HIS   A 91  ? 0.2567 0.2961 0.2919 0.0248  -0.0760 -0.0104 91  HIS   A ND1 
1855 C  CD2 . HIS   A 91  ? 0.2734 0.2912 0.2762 0.0298  -0.0878 0.0185  91  HIS   A CD2 
1856 C  CE1 . HIS   A 91  ? 0.2708 0.3075 0.3139 0.0287  -0.0804 0.0042  91  HIS   A CE1 
1857 N  NE2 . HIS   A 91  ? 0.2824 0.3037 0.3056 0.0377  -0.0962 0.0134  91  HIS   A NE2 
1865 N  N   . CYS   A 92  ? 0.1558 0.1683 0.1159 -0.0175 -0.0137 0.0204  92  CYS   A N   
1866 C  CA  . CYS   A 92  ? 0.1494 0.1599 0.1284 -0.0087 0.0009  0.0164  92  CYS   A CA  
1867 C  C   . CYS   A 92  ? 0.1383 0.1503 0.1256 -0.0129 -0.0011 0.0128  92  CYS   A C   
1868 O  O   . CYS   A 92  ? 0.1429 0.1534 0.1554 -0.0137 -0.0033 0.0150  92  CYS   A O   
1869 C  CB  . CYS   A 92  ? 0.1548 0.1606 0.1460 -0.0042 -0.0013 0.0127  92  CYS   A CB  
1870 S  SG  . CYS   A 92  ? 0.1469 0.1479 0.1452 -0.0118 -0.0071 0.0123  92  CYS   A SG  
1876 N  N   . LEU   A 93  ? 0.1348 0.1376 0.1430 -0.0083 0.0033  0.0131  93  LEU   A N   
1877 C  CA  . LEU   A 93  ? 0.1289 0.1359 0.1420 -0.0075 0.0019  0.0114  93  LEU   A CA  
1878 C  C   . LEU   A 93  ? 0.1283 0.1227 0.1365 0.0063  0.0032  0.0156  93  LEU   A C   
1879 O  O   . LEU   A 93  ? 0.1284 0.1445 0.1323 -0.0021 0.0005  0.0124  93  LEU   A O   
1880 C  CB  . LEU   A 93  ? 0.1347 0.1401 0.1505 -0.0027 -0.0042 0.0165  93  LEU   A CB  
1881 C  CG  . LEU   A 93  ? 0.1422 0.1386 0.1557 -0.0024 0.0050  0.0213  93  LEU   A CG  
1882 C  CD1 . LEU   A 93  ? 0.1510 0.1378 0.1727 0.0028  0.0144  0.0105  93  LEU   A CD1 
1883 C  CD2 . LEU   A 93  ? 0.1598 0.1373 0.1831 -0.0056 -0.0022 0.0145  93  LEU   A CD2 
1895 N  N   . HIS   A 94  ? 0.1271 0.1237 0.1467 -0.0003 0.0050  0.0201  94  HIS   A N   
1896 C  CA  . HIS   A 94  ? 0.1238 0.1256 0.1380 -0.0071 -0.0018 0.0219  94  HIS   A CA  
1897 C  C   . HIS   A 94  ? 0.1193 0.1215 0.1422 -0.0076 0.0035  0.0108  94  HIS   A C   
1898 O  O   . HIS   A 94  ? 0.1192 0.1430 0.1849 0.0019  0.0027  -0.0128 94  HIS   A O   
1899 C  CB  . HIS   A 94  ? 0.1257 0.1244 0.1436 -0.0049 -0.0110 0.0180  94  HIS   A CB  
1900 C  CG  . HIS   A 94  ? 0.1301 0.1235 0.1398 -0.0062 -0.0075 0.0170  94  HIS   A CG  
1901 N  ND1 . HIS   A 94  ? 0.1256 0.1251 0.1495 -0.0034 -0.0033 0.0135  94  HIS   A ND1 
1902 C  CD2 . HIS   A 94  ? 0.1411 0.1344 0.1531 -0.0062 -0.0047 0.0088  94  HIS   A CD2 
1903 C  CE1 . HIS   A 94  ? 0.1329 0.1258 0.1555 -0.0086 -0.0155 0.0066  94  HIS   A CE1 
1904 N  NE2 . HIS   A 94  ? 0.1425 0.1294 0.1543 -0.0084 -0.0102 0.0011  94  HIS   A NE2 
1912 N  N   . VAL   A 95  ? 0.1194 0.1203 0.1299 -0.0039 0.0062  0.0066  95  VAL   A N   
1913 C  CA  . VAL   A 95  ? 0.1304 0.1255 0.1172 -0.0024 0.0073  0.0143  95  VAL   A CA  
1914 C  C   . VAL   A 95  ? 0.1278 0.1231 0.1214 -0.0193 0.0002  0.0029  95  VAL   A C   
1915 O  O   . VAL   A 95  ? 0.1309 0.1325 0.1406 0.0101  0.0040  0.0021  95  VAL   A O   
1916 C  CB  . VAL   A 95  ? 0.1287 0.1256 0.1495 -0.0116 0.0039  0.0115  95  VAL   A CB  
1917 C  CG1 . VAL   A 95  ? 0.1425 0.1300 0.1698 -0.0173 0.0095  0.0017  95  VAL   A CG1 
1918 C  CG2 . VAL   A 95  ? 0.1329 0.1326 0.1487 -0.0129 0.0034  0.0298  95  VAL   A CG2 
1928 N  N   . VAL   A 96  ? 0.1373 0.1224 0.1027 -0.0074 0.0042  0.0060  96  VAL   A N   
1929 C  CA  . VAL   A 96  ? 0.1417 0.1258 0.1352 -0.0009 0.0120  0.0137  96  VAL   A CA  
1930 C  C   . VAL   A 96  ? 0.1414 0.1336 0.1376 0.0076  0.0090  0.0175  96  VAL   A C   
1931 O  O   . VAL   A 96  ? 0.1465 0.1410 0.1625 -0.0000 0.0164  -0.0003 96  VAL   A O   
1932 C  CB  . VAL   A 96  ? 0.1439 0.1294 0.1479 0.0001  0.0148  0.0199  96  VAL   A CB  
1933 C  CG1 . VAL   A 96  ? 0.1544 0.1362 0.1458 -0.0005 0.0050  0.0061  96  VAL   A CG1 
1934 C  CG2 . VAL   A 96  ? 0.1449 0.1357 0.1619 -0.0137 0.0125  0.0112  96  VAL   A CG2 
1944 N  N   . GLY   A 97  ? 0.1436 0.1342 0.1408 -0.0034 0.0083  0.0086  97  GLY   A N   
1945 C  CA  . GLY   A 97  ? 0.1507 0.1427 0.1376 -0.0057 0.0073  0.0125  97  GLY   A CA  
1946 C  C   . GLY   A 97  ? 0.1482 0.1522 0.1283 -0.0073 0.0052  0.0109  97  GLY   A C   
1947 O  O   . GLY   A 97  ? 0.1576 0.1488 0.1579 -0.0056 0.0050  0.0132  97  GLY   A O   
1951 N  N   A PRO   A 98  ? 0.1531 0.1572 0.1230 -0.0012 -0.0045 0.0151  98  PRO   A N   
1952 N  N   B PRO   A 98  ? 0.1609 0.1511 0.1283 -0.0035 0.0003  0.0167  98  PRO   A N   
1953 C  CA  A PRO   A 98  ? 0.1608 0.1762 0.1322 0.0005  0.0013  0.0043  98  PRO   A CA  
1954 C  CA  B PRO   A 98  ? 0.1747 0.1573 0.1401 -0.0051 0.0008  0.0117  98  PRO   A CA  
1955 C  C   A PRO   A 98  ? 0.1626 0.1853 0.1221 -0.0067 0.0021  0.0186  98  PRO   A C   
1956 C  C   B PRO   A 98  ? 0.1972 0.1553 0.1378 -0.0076 -0.0010 0.0248  98  PRO   A C   
1957 O  O   A PRO   A 98  ? 0.1577 0.1758 0.1532 0.0007  0.0065  0.0202  98  PRO   A O   
1958 O  O   B PRO   A 98  ? 0.1958 0.1539 0.1760 -0.0070 0.0041  0.0236  98  PRO   A O   
1959 C  CB  A PRO   A 98  ? 0.1714 0.1797 0.1273 0.0109  -0.0049 -0.0061 98  PRO   A CB  
1960 C  CB  B PRO   A 98  ? 0.1736 0.1586 0.1385 -0.0007 -0.0007 0.0070  98  PRO   A CB  
1961 C  CG  A PRO   A 98  ? 0.1684 0.1673 0.1370 0.0070  -0.0070 -0.0097 98  PRO   A CG  
1962 C  CG  B PRO   A 98  ? 0.1760 0.1559 0.1464 -0.0027 -0.0003 0.0070  98  PRO   A CG  
1963 C  CD  A PRO   A 98  ? 0.1658 0.1561 0.1341 0.0031  -0.0056 0.0044  98  PRO   A CD  
1964 C  CD  B PRO   A 98  ? 0.1664 0.1476 0.1316 0.0010  -0.0023 0.0176  98  PRO   A CD  
1979 N  N   A ASN   A 99  ? 0.1690 0.2053 0.1283 -0.0081 0.0059  0.0307  99  ASN   A N   
1980 N  N   B ASN   A 99  ? 0.2220 0.1538 0.1194 -0.0036 -0.0070 0.0380  99  ASN   A N   
1981 C  CA  A ASN   A 99  ? 0.1961 0.2216 0.1312 -0.0087 0.0044  0.0354  99  ASN   A CA  
1982 C  CA  B ASN   A 99  ? 0.2506 0.1547 0.1206 0.0069  -0.0112 0.0489  99  ASN   A CA  
1983 C  C   A ASN   A 99  ? 0.2244 0.2492 0.1259 -0.0236 -0.0043 0.0421  99  ASN   A C   
1984 C  C   B ASN   A 99  ? 0.2681 0.1619 0.1339 0.0076  -0.0225 0.0459  99  ASN   A C   
1985 O  O   A ASN   A 99  ? 0.2326 0.2633 0.1471 -0.0161 -0.0139 0.0342  99  ASN   A O   
1986 O  O   B ASN   A 99  ? 0.2703 0.1482 0.1402 0.0106  -0.0296 0.0150  99  ASN   A O   
1987 C  CB  A ASN   A 99  ? 0.1924 0.2168 0.1421 -0.0071 0.0006  0.0395  99  ASN   A CB  
1988 C  CB  B ASN   A 99  ? 0.2611 0.1505 0.1562 0.0132  -0.0109 0.0522  99  ASN   A CB  
1989 C  CG  A ASN   A 99  ? 0.1909 0.2179 0.1670 -0.0031 -0.0115 0.0229  99  ASN   A CG  
1990 C  CG  B ASN   A 99  ? 0.2674 0.1552 0.1711 0.0159  -0.0111 0.0605  99  ASN   A CG  
1991 O  OD1 A ASN   A 99  ? 0.2014 0.2297 0.1773 0.0104  -0.0133 0.0159  99  ASN   A OD1 
1992 O  OD1 B ASN   A 99  ? 0.2725 0.1657 0.1527 0.0104  -0.0148 0.0648  99  ASN   A OD1 
1993 N  ND2 A ASN   A 99  ? 0.1919 0.2208 0.1642 0.0020  -0.0072 0.0277  99  ASN   A ND2 
1994 N  ND2 B ASN   A 99  ? 0.2688 0.1594 0.1922 0.0282  -0.0146 0.0418  99  ASN   A ND2 
2007 N  N   A VAL   A 100 ? 0.2465 0.2690 0.1323 -0.0443 -0.0274 0.0323  100 VAL   A N   
2008 N  N   B VAL   A 100 ? 0.2808 0.1896 0.1692 0.0034  -0.0297 0.0534  100 VAL   A N   
2009 C  CA  A VAL   A 100 ? 0.2779 0.3000 0.1541 -0.0511 -0.0359 0.0371  100 VAL   A CA  
2010 C  CA  B VAL   A 100 ? 0.2942 0.2189 0.2072 -0.0016 -0.0325 0.0478  100 VAL   A CA  
2011 C  C   A VAL   A 100 ? 0.2921 0.3210 0.1614 -0.0462 -0.0454 0.0544  100 VAL   A C   
2012 C  C   B VAL   A 100 ? 0.3026 0.2321 0.2170 0.0008  -0.0397 0.0506  100 VAL   A C   
2013 O  O   A VAL   A 100 ? 0.2996 0.3289 0.1766 -0.0397 -0.0233 0.0521  100 VAL   A O   
2014 O  O   B VAL   A 100 ? 0.3065 0.2344 0.2266 0.0010  -0.0391 0.0370  100 VAL   A O   
2015 C  CB  A VAL   A 100 ? 0.2979 0.3068 0.1917 -0.0615 -0.0364 0.0236  100 VAL   A CB  
2016 C  CB  B VAL   A 100 ? 0.2994 0.2316 0.2450 -0.0017 -0.0311 0.0350  100 VAL   A CB  
2017 C  CG1 A VAL   A 100 ? 0.2996 0.3027 0.2013 -0.0698 -0.0269 0.0314  100 VAL   A CG1 
2018 C  CG1 B VAL   A 100 ? 0.3010 0.2323 0.2552 -0.0016 -0.0337 0.0365  100 VAL   A CG1 
2019 C  CG2 A VAL   A 100 ? 0.3041 0.3086 0.1840 -0.0675 -0.0374 0.0056  100 VAL   A CG2 
2020 C  CG2 B VAL   A 100 ? 0.3017 0.2360 0.2635 -0.0036 -0.0230 0.0256  100 VAL   A CG2 
2039 N  N   A ASN   A 101 ? 0.2995 0.3299 0.1872 -0.0441 -0.0547 0.0930  101 ASN   A N   
2040 N  N   B ASN   A 101 ? 0.3055 0.2376 0.2129 0.0041  -0.0521 0.0654  101 ASN   A N   
2041 C  CA  A ASN   A 101 ? 0.3161 0.3385 0.2072 -0.0416 -0.0479 0.1205  101 ASN   A CA  
2042 C  CA  B ASN   A 101 ? 0.3127 0.2453 0.2214 0.0055  -0.0504 0.0691  101 ASN   A CA  
2043 C  C   A ASN   A 101 ? 0.3433 0.3683 0.2300 -0.0404 -0.0225 0.1495  101 ASN   A C   
2044 C  C   B ASN   A 101 ? 0.3258 0.2623 0.2238 0.0078  -0.0301 0.0767  101 ASN   A C   
2045 O  O   A ASN   A 101 ? 0.3566 0.3773 0.2837 -0.0354 -0.0236 0.1320  101 ASN   A O   
2046 O  O   B ASN   A 101 ? 0.3313 0.2628 0.2070 0.0073  -0.0304 0.0839  101 ASN   A O   
2047 C  CB  A ASN   A 101 ? 0.3044 0.3160 0.1967 -0.0379 -0.0723 0.1142  101 ASN   A CB  
2048 C  CB  B ASN   A 101 ? 0.3067 0.2361 0.2286 0.0021  -0.0574 0.0609  101 ASN   A CB  
2049 C  CG  A ASN   A 101 ? 0.2925 0.2981 0.2008 -0.0337 -0.0940 0.0756  101 ASN   A CG  
2050 C  CG  B ASN   A 101 ? 0.3034 0.2322 0.2490 -0.0012 -0.0612 0.0474  101 ASN   A CG  
2051 O  OD1 A ASN   A 101 ? 0.2916 0.3024 0.2227 -0.0177 -0.0919 0.0333  101 ASN   A OD1 
2052 O  OD1 B ASN   A 101 ? 0.3076 0.2344 0.2675 -0.0053 -0.0616 0.0420  101 ASN   A OD1 
2053 N  ND2 A ASN   A 101 ? 0.2888 0.2824 0.1948 -0.0447 -0.0930 0.0712  101 ASN   A ND2 
2054 N  ND2 B ASN   A 101 ? 0.3014 0.2277 0.2548 0.0000  -0.0574 0.0382  101 ASN   A ND2 
2067 N  N   A LYS   A 102 ? 0.3525 0.3926 0.2658 -0.0444 -0.0078 0.1482  102 LYS   A N   
2068 N  N   B LYS   A 102 ? 0.3321 0.2779 0.2677 0.0077  -0.0047 0.0663  102 LYS   A N   
2069 C  CA  A LYS   A 102 ? 0.3669 0.4146 0.2798 -0.0479 -0.0121 0.1415  102 LYS   A CA  
2070 C  CA  B LYS   A 102 ? 0.3413 0.2913 0.2859 0.0038  0.0116  0.0592  102 LYS   A CA  
2071 C  C   A LYS   A 102 ? 0.3753 0.4307 0.2500 -0.0360 -0.0159 0.1321  102 LYS   A C   
2072 C  C   B LYS   A 102 ? 0.3421 0.2905 0.2697 0.0080  0.0027  0.0787  102 LYS   A C   
2073 O  O   A LYS   A 102 ? 0.3784 0.4441 0.2508 -0.0305 -0.0152 0.1259  102 LYS   A O   
2074 O  O   B LYS   A 102 ? 0.3434 0.2854 0.2544 0.0082  0.0107  0.1013  102 LYS   A O   
2075 C  CB  A LYS   A 102 ? 0.3762 0.4241 0.3320 -0.0596 -0.0270 0.1240  102 LYS   A CB  
2076 C  CB  B LYS   A 102 ? 0.3509 0.3059 0.3267 -0.0007 0.0218  0.0318  102 LYS   A CB  
2077 C  CG  A LYS   A 102 ? 0.3847 0.4333 0.3772 -0.0694 -0.0434 0.0979  102 LYS   A CG  
2078 C  CG  B LYS   A 102 ? 0.3607 0.3192 0.3608 -0.0045 0.0280  0.0095  102 LYS   A CG  
2079 C  CD  A LYS   A 102 ? 0.3953 0.4442 0.4253 -0.0747 -0.0533 0.0674  102 LYS   A CD  
2080 C  CD  B LYS   A 102 ? 0.3712 0.3333 0.3957 -0.0070 0.0344  -0.0093 102 LYS   A CD  
2081 C  CE  A LYS   A 102 ? 0.4034 0.4524 0.4651 -0.0753 -0.0626 0.0492  102 LYS   A CE  
2082 C  CE  B LYS   A 102 ? 0.3782 0.3441 0.4224 -0.0072 0.0384  -0.0231 102 LYS   A CE  
2083 N  NZ  A LYS   A 102 ? 0.4042 0.4549 0.4797 -0.0799 -0.0705 0.0391  102 LYS   A NZ  
2084 N  NZ  B LYS   A 102 ? 0.3816 0.3504 0.4335 -0.0073 0.0427  -0.0280 102 LYS   A NZ  
2111 N  N   A GLY   A 103 ? 0.3767 0.4362 0.2471 -0.0240 -0.0280 0.1031  103 GLY   A N   
2112 N  N   B GLY   A 103 ? 0.3407 0.2976 0.2634 0.0139  -0.0172 0.0675  103 GLY   A N   
2113 C  CA  A GLY   A 103 ? 0.3779 0.4352 0.2305 -0.0150 -0.0284 0.0787  103 GLY   A CA  
2114 C  CA  B GLY   A 103 ? 0.3395 0.2989 0.2545 0.0175  -0.0259 0.0603  103 GLY   A CA  
2115 C  C   A GLY   A 103 ? 0.3720 0.4310 0.2240 -0.0108 -0.0157 0.0537  103 GLY   A C   
2116 C  C   B GLY   A 103 ? 0.3342 0.2948 0.2346 0.0199  -0.0255 0.0455  103 GLY   A C   
2117 O  O   A GLY   A 103 ? 0.3851 0.4425 0.2505 -0.0039 -0.0106 0.0359  103 GLY   A O   
2118 O  O   B GLY   A 103 ? 0.3419 0.3017 0.2424 0.0237  -0.0305 0.0418  103 GLY   A O   
2125 N  N   A GLU   A 104 ? 0.3461 0.4088 0.1768 -0.0178 -0.0100 0.0433  104 GLU   A N   
2126 N  N   B GLU   A 104 ? 0.3165 0.2782 0.2037 0.0182  -0.0257 0.0438  104 GLU   A N   
2127 C  CA  A GLU   A 104 ? 0.3172 0.3849 0.1647 -0.0304 -0.0007 0.0296  104 GLU   A CA  
2128 C  CA  B GLU   A 104 ? 0.2986 0.2609 0.1832 0.0145  -0.0220 0.0352  104 GLU   A CA  
2129 C  C   A GLU   A 104 ? 0.3174 0.3922 0.1711 -0.0354 0.0028  0.0083  104 GLU   A C   
2130 C  C   B GLU   A 104 ? 0.2813 0.2419 0.1771 0.0215  -0.0148 0.0259  104 GLU   A C   
2131 O  O   A GLU   A 104 ? 0.3119 0.3932 0.1920 -0.0426 -0.0005 -0.0072 104 GLU   A O   
2132 O  O   B GLU   A 104 ? 0.2789 0.2350 0.1860 0.0188  -0.0144 0.0228  104 GLU   A O   
2133 C  CB  A GLU   A 104 ? 0.2818 0.3551 0.1465 -0.0406 0.0080  0.0432  104 GLU   A CB  
2134 C  CB  B GLU   A 104 ? 0.2967 0.2646 0.1857 0.0057  -0.0216 0.0366  104 GLU   A CB  
2135 C  CG  A GLU   A 104 ? 0.2559 0.3330 0.1501 -0.0458 0.0058  0.0494  104 GLU   A CG  
2136 C  CG  B GLU   A 104 ? 0.3003 0.2748 0.2071 -0.0004 -0.0221 0.0324  104 GLU   A CG  
2137 C  CD  A GLU   A 104 ? 0.2318 0.3122 0.1548 -0.0463 0.0023  0.0558  104 GLU   A CD  
2138 C  CD  B GLU   A 104 ? 0.3035 0.2839 0.2166 -0.0019 -0.0236 0.0283  104 GLU   A CD  
2139 O  OE1 A GLU   A 104 ? 0.2179 0.2953 0.1140 -0.0352 -0.0047 0.0552  104 GLU   A OE1 
2140 O  OE1 B GLU   A 104 ? 0.3062 0.2880 0.2292 0.0003  -0.0231 0.0248  104 GLU   A OE1 
2141 O  OE2 A GLU   A 104 ? 0.2309 0.3111 0.1907 -0.0565 0.0026  0.0726  104 GLU   A OE2 
2142 O  OE2 B GLU   A 104 ? 0.3045 0.2875 0.2183 -0.0055 -0.0262 0.0313  104 GLU   A OE2 
2155 N  N   A ASP   A 105 ? 0.3230 0.3983 0.1686 -0.0324 0.0083  0.0017  105 ASP   A N   
2156 N  N   B ASP   A 105 ? 0.2693 0.2324 0.1868 0.0313  -0.0076 0.0197  105 ASP   A N   
2157 C  CA  A ASP   A 105 ? 0.3280 0.4041 0.1993 -0.0266 0.0109  -0.0181 105 ASP   A CA  
2158 C  CA  B ASP   A 105 ? 0.2586 0.2241 0.1995 0.0423  0.0048  0.0001  105 ASP   A CA  
2159 C  C   A ASP   A 105 ? 0.2942 0.3848 0.1701 -0.0387 -0.0035 -0.0309 105 ASP   A C   
2160 C  C   B ASP   A 105 ? 0.2435 0.2066 0.1798 0.0371  0.0054  0.0048  105 ASP   A C   
2161 O  O   A ASP   A 105 ? 0.2825 0.3770 0.1168 -0.0425 -0.0121 -0.0486 105 ASP   A O   
2162 O  O   B ASP   A 105 ? 0.2321 0.1934 0.1558 0.0383  0.0043  0.0127  105 ASP   A O   
2163 C  CB  A ASP   A 105 ? 0.3594 0.4269 0.2684 -0.0115 0.0213  -0.0262 105 ASP   A CB  
2164 C  CB  B ASP   A 105 ? 0.2613 0.2366 0.2307 0.0553  0.0079  -0.0197 105 ASP   A CB  
2165 C  CG  A ASP   A 105 ? 0.3840 0.4467 0.3346 0.0014  0.0250  -0.0408 105 ASP   A CG  
2166 C  CG  B ASP   A 105 ? 0.2631 0.2435 0.2514 0.0668  0.0046  -0.0376 105 ASP   A CG  
2167 O  OD1 A ASP   A 105 ? 0.3909 0.4539 0.3471 0.0037  0.0236  -0.0557 105 ASP   A OD1 
2168 O  OD1 B ASP   A 105 ? 0.2646 0.2419 0.2377 0.0615  -0.0061 -0.0457 105 ASP   A OD1 
2169 O  OD2 A ASP   A 105 ? 0.3967 0.4547 0.3813 0.0071  0.0257  -0.0359 105 ASP   A OD2 
2170 O  OD2 B ASP   A 105 ? 0.2663 0.2513 0.2889 0.0732  0.0073  -0.0342 105 ASP   A OD2 
2179 N  N   A ILE   A 106 ? 0.2723 0.3753 0.1984 -0.0464 -0.0286 -0.0292 106 ILE   A N   
2180 N  N   B ILE   A 106 ? 0.2423 0.2105 0.1947 0.0368  -0.0058 0.0065  106 ILE   A N   
2181 C  CA  A ILE   A 106 ? 0.2447 0.3560 0.2136 -0.0580 -0.0480 -0.0464 106 ILE   A CA  
2182 C  CA  B ILE   A 106 ? 0.2468 0.2193 0.2027 0.0200  -0.0118 0.0048  106 ILE   A CA  
2183 C  C   A ILE   A 106 ? 0.2206 0.3279 0.2150 -0.0673 -0.0411 -0.0628 106 ILE   A C   
2184 C  C   B ILE   A 106 ? 0.2511 0.2191 0.1959 0.0152  -0.0024 0.0174  106 ILE   A C   
2185 O  O   A ILE   A 106 ? 0.1982 0.3129 0.2291 -0.0728 -0.0266 -0.0554 106 ILE   A O   
2186 O  O   B ILE   A 106 ? 0.2474 0.2197 0.1988 0.0137  0.0065  0.0228  106 ILE   A O   
2187 C  CB  A ILE   A 106 ? 0.2531 0.3697 0.2573 -0.0484 -0.0674 -0.0229 106 ILE   A CB  
2188 C  CB  B ILE   A 106 ? 0.2516 0.2360 0.2361 0.0107  -0.0272 0.0054  106 ILE   A CB  
2189 C  CG1 A ILE   A 106 ? 0.2534 0.3720 0.2905 -0.0337 -0.0656 -0.0046 106 ILE   A CG1 
2190 C  CG1 B ILE   A 106 ? 0.2508 0.2451 0.2530 0.0129  -0.0304 0.0102  106 ILE   A CG1 
2191 C  CG2 A ILE   A 106 ? 0.2590 0.3761 0.2707 -0.0475 -0.0800 -0.0149 106 ILE   A CG2 
2192 C  CG2 B ILE   A 106 ? 0.2550 0.2433 0.2484 0.0058  -0.0320 0.0034  106 ILE   A CG2 
2193 C  CD1 A ILE   A 106 ? 0.2539 0.3703 0.3090 -0.0246 -0.0595 0.0048  106 ILE   A CD1 
2194 C  CD1 B ILE   A 106 ? 0.2469 0.2470 0.2587 0.0136  -0.0313 0.0121  106 ILE   A CD1 
2217 N  N   A GLN   A 107 ? 0.2407 0.3157 0.2360 -0.0643 -0.0300 -0.0858 107 GLN   A N   
2218 N  N   B GLN   A 107 ? 0.2624 0.2182 0.2115 0.0113  -0.0037 0.0194  107 GLN   A N   
2219 C  CA  A GLN   A 107 ? 0.2619 0.3021 0.3079 -0.0510 -0.0093 -0.0817 107 GLN   A CA  
2220 C  CA  B GLN   A 107 ? 0.2743 0.2215 0.2425 0.0054  -0.0102 0.0156  107 GLN   A CA  
2221 C  C   A GLN   A 107 ? 0.2328 0.2569 0.2884 -0.0408 0.0214  -0.0499 107 GLN   A C   
2222 C  C   B GLN   A 107 ? 0.2540 0.1897 0.2043 0.0026  -0.0109 0.0300  107 GLN   A C   
2223 O  O   A GLN   A 107 ? 0.2431 0.2568 0.3431 -0.0324 0.0299  -0.0417 107 GLN   A O   
2224 O  O   B GLN   A 107 ? 0.2566 0.1756 0.1873 0.0028  -0.0229 0.0398  107 GLN   A O   
2225 C  CB  A GLN   A 107 ? 0.3079 0.3325 0.4014 -0.0578 -0.0260 -0.0986 107 GLN   A CB  
2226 C  CB  B GLN   A 107 ? 0.3029 0.2583 0.3074 -0.0026 -0.0208 0.0077  107 GLN   A CB  
2227 C  CG  A GLN   A 107 ? 0.3596 0.3684 0.5146 -0.0527 -0.0351 -0.0925 107 GLN   A CG  
2228 C  CG  B GLN   A 107 ? 0.3296 0.2945 0.3767 -0.0074 -0.0323 0.0111  107 GLN   A CG  
2229 C  CD  A GLN   A 107 ? 0.4018 0.3947 0.6113 -0.0497 -0.0404 -0.0836 107 GLN   A CD  
2230 C  CD  B GLN   A 107 ? 0.3510 0.3266 0.4374 -0.0113 -0.0411 0.0142  107 GLN   A CD  
2231 O  OE1 A GLN   A 107 ? 0.4177 0.4033 0.6499 -0.0512 -0.0440 -0.0794 107 GLN   A OE1 
2232 O  OE1 B GLN   A 107 ? 0.3581 0.3319 0.4537 -0.0118 -0.0430 0.0190  107 GLN   A OE1 
2233 N  NE2 A GLN   A 107 ? 0.4100 0.4018 0.6433 -0.0479 -0.0420 -0.0851 107 GLN   A NE2 
2234 N  NE2 B GLN   A 107 ? 0.3583 0.3353 0.4537 -0.0134 -0.0472 0.0140  107 GLN   A NE2 
2251 N  N   A LEU   A 108 ? 0.1954 0.2167 0.2296 -0.0372 0.0333  -0.0411 108 LEU   A N   
2252 N  N   B LEU   A 108 ? 0.2322 0.1785 0.1734 -0.0043 -0.0029 0.0194  108 LEU   A N   
2253 C  CA  A LEU   A 108 ? 0.1792 0.1913 0.2029 -0.0101 0.0257  -0.0190 108 LEU   A CA  
2254 C  CA  B LEU   A 108 ? 0.2146 0.1721 0.1724 -0.0036 -0.0021 0.0189  108 LEU   A CA  
2255 C  C   A LEU   A 108 ? 0.1538 0.1589 0.1936 0.0027  0.0216  -0.0079 108 LEU   A C   
2256 C  C   B LEU   A 108 ? 0.1943 0.1559 0.1627 -0.0022 -0.0127 0.0234  108 LEU   A C   
2257 O  O   A LEU   A 108 ? 0.1503 0.1594 0.2127 0.0031  0.0345  -0.0040 108 LEU   A O   
2258 O  O   B LEU   A 108 ? 0.1950 0.1604 0.1723 0.0043  -0.0129 0.0253  108 LEU   A O   
2259 C  CB  A LEU   A 108 ? 0.1947 0.2031 0.1815 -0.0130 0.0270  -0.0249 108 LEU   A CB  
2260 C  CB  B LEU   A 108 ? 0.2187 0.1828 0.1755 -0.0044 0.0077  0.0085  108 LEU   A CB  
2261 C  CG  A LEU   A 108 ? 0.2093 0.2248 0.2109 -0.0169 0.0355  -0.0247 108 LEU   A CG  
2262 C  CG  B LEU   A 108 ? 0.2251 0.1942 0.1977 -0.0012 0.0230  0.0052  108 LEU   A CG  
2263 C  CD1 A LEU   A 108 ? 0.2253 0.2338 0.2245 -0.0313 0.0439  -0.0299 108 LEU   A CD1 
2264 C  CD1 B LEU   A 108 ? 0.2328 0.1994 0.2036 -0.0061 0.0301  0.0032  108 LEU   A CD1 
2265 C  CD2 A LEU   A 108 ? 0.2061 0.2429 0.2529 -0.0096 0.0401  -0.0227 108 LEU   A CD2 
2266 C  CD2 B LEU   A 108 ? 0.2237 0.2037 0.2226 0.0068  0.0293  -0.0018 108 LEU   A CD2 
2289 N  N   A LEU   A 109 ? 0.1378 0.1521 0.1966 0.0082  0.0126  0.0008  109 LEU   A N   
2290 N  N   B LEU   A 109 ? 0.1819 0.1457 0.1579 -0.0042 -0.0080 0.0229  109 LEU   A N   
2291 C  CA  A LEU   A 109 ? 0.1434 0.1453 0.1829 -0.0002 0.0054  -0.0029 109 LEU   A CA  
2292 C  CA  B LEU   A 109 ? 0.1705 0.1306 0.1451 -0.0080 -0.0128 0.0282  109 LEU   A CA  
2293 C  C   A LEU   A 109 ? 0.1371 0.1441 0.1750 -0.0056 0.0099  -0.0119 109 LEU   A C   
2294 C  C   B LEU   A 109 ? 0.1660 0.1277 0.1478 -0.0151 -0.0031 0.0232  109 LEU   A C   
2295 O  O   A LEU   A 109 ? 0.1466 0.1397 0.1951 0.0014  0.0013  -0.0127 109 LEU   A O   
2296 O  O   B LEU   A 109 ? 0.1675 0.1234 0.1492 -0.0144 -0.0026 0.0290  109 LEU   A O   
2297 C  CB  A LEU   A 109 ? 0.1459 0.1475 0.2166 0.0034  -0.0047 0.0144  109 LEU   A CB  
2298 C  CB  B LEU   A 109 ? 0.1664 0.1220 0.1527 -0.0069 -0.0180 0.0347  109 LEU   A CB  
2299 C  CG  A LEU   A 109 ? 0.1418 0.1600 0.2284 0.0030  -0.0061 0.0111  109 LEU   A CG  
2300 C  CG  B LEU   A 109 ? 0.1583 0.1217 0.1561 -0.0124 -0.0114 0.0342  109 LEU   A CG  
2301 C  CD1 A LEU   A 109 ? 0.1388 0.1618 0.2265 0.0014  -0.0052 0.0042  109 LEU   A CD1 
2302 C  CD1 B LEU   A 109 ? 0.1541 0.1165 0.1326 -0.0161 -0.0124 0.0258  109 LEU   A CD1 
2303 C  CD2 A LEU   A 109 ? 0.1410 0.1684 0.2437 0.0010  -0.0090 0.0087  109 LEU   A CD2 
2304 C  CD2 B LEU   A 109 ? 0.1525 0.1105 0.1688 -0.0127 -0.0112 0.0193  109 LEU   A CD2 
2327 N  N   A LYS   A 110 ? 0.1408 0.1404 0.1741 0.0005  -0.0048 -0.0063 110 LYS   A N   
2328 N  N   B LYS   A 110 ? 0.1645 0.1281 0.1656 -0.0140 -0.0011 0.0225  110 LYS   A N   
2329 C  CA  A LYS   A 110 ? 0.1448 0.1355 0.1790 -0.0045 -0.0004 -0.0021 110 LYS   A CA  
2330 C  CA  B LYS   A 110 ? 0.1621 0.1340 0.1759 -0.0134 -0.0050 0.0193  110 LYS   A CA  
2331 C  C   A LYS   A 110 ? 0.1416 0.1261 0.1714 -0.0041 0.0053  0.0018  110 LYS   A C   
2332 C  C   B LYS   A 110 ? 0.1544 0.1280 0.1715 -0.0104 -0.0015 0.0090  110 LYS   A C   
2333 O  O   A LYS   A 110 ? 0.1293 0.1286 0.1831 0.0018  0.0148  -0.0013 110 LYS   A O   
2334 O  O   B LYS   A 110 ? 0.1542 0.1275 0.1786 -0.0132 -0.0003 0.0008  110 LYS   A O   
2335 C  CB  A LYS   A 110 ? 0.1485 0.1376 0.2084 -0.0030 -0.0044 -0.0169 110 LYS   A CB  
2336 C  CB  B LYS   A 110 ? 0.1633 0.1430 0.1851 -0.0122 -0.0119 0.0180  110 LYS   A CB  
2337 C  CG  A LYS   A 110 ? 0.1475 0.1350 0.2230 -0.0007 -0.0055 -0.0135 110 LYS   A CG  
2338 C  CG  B LYS   A 110 ? 0.1620 0.1491 0.1865 -0.0134 -0.0134 0.0130  110 LYS   A CG  
2339 C  CD  A LYS   A 110 ? 0.1496 0.1347 0.2311 -0.0044 -0.0087 -0.0147 110 LYS   A CD  
2340 C  CD  B LYS   A 110 ? 0.1615 0.1533 0.1912 -0.0115 -0.0059 0.0102  110 LYS   A CD  
2341 C  CE  A LYS   A 110 ? 0.1582 0.1383 0.2440 -0.0027 0.0035  -0.0112 110 LYS   A CE  
2342 C  CE  B LYS   A 110 ? 0.1602 0.1574 0.1909 -0.0106 0.0055  0.0077  110 LYS   A CE  
2343 N  NZ  A LYS   A 110 ? 0.1635 0.1391 0.2628 -0.0107 0.0139  -0.0077 110 LYS   A NZ  
2344 N  NZ  B LYS   A 110 ? 0.1645 0.1630 0.2033 -0.0142 0.0151  0.0118  110 LYS   A NZ  
2371 N  N   . SER   A 111 ? 0.1457 0.1311 0.1682 0.0006  -0.0024 0.0031  111 SER   A N   
2372 C  CA  . SER   A 111 ? 0.1377 0.1389 0.1770 0.0021  0.0051  -0.0011 111 SER   A CA  
2373 C  C   . SER   A 111 ? 0.1331 0.1309 0.1756 -0.0067 0.0081  0.0164  111 SER   A C   
2374 O  O   . SER   A 111 ? 0.1464 0.1232 0.2027 -0.0051 0.0050  0.0104  111 SER   A O   
2375 C  CB  . SER   A 111 ? 0.1577 0.1637 0.1872 0.0020  0.0237  -0.0060 111 SER   A CB  
2376 O  OG  . SER   A 111 ? 0.2020 0.1828 0.2053 0.0029  0.0274  -0.0191 111 SER   A OG  
2383 N  N   . ALA   A 112 ? 0.1399 0.1230 0.1800 0.0030  0.0092  0.0110  112 ALA   A N   
2384 C  CA  . ALA   A 112 ? 0.1396 0.1241 0.1614 -0.0015 0.0160  0.0055  112 ALA   A CA  
2385 C  C   . ALA   A 112 ? 0.1353 0.1212 0.1726 0.0025  0.0073  0.0034  112 ALA   A C   
2386 O  O   . ALA   A 112 ? 0.1413 0.1206 0.1792 -0.0087 0.0137  0.0142  112 ALA   A O   
2387 C  CB  . ALA   A 112 ? 0.1539 0.1283 0.1634 -0.0027 0.0166  0.0191  112 ALA   A CB  
2393 N  N   . TYR   A 113 ? 0.1252 0.1219 0.1931 -0.0020 0.0073  0.0150  113 TYR   A N   
2394 C  CA  . TYR   A 113 ? 0.1283 0.1186 0.1748 -0.0055 0.0123  0.0135  113 TYR   A CA  
2395 C  C   . TYR   A 113 ? 0.1230 0.1249 0.1513 -0.0074 0.0118  0.0027  113 TYR   A C   
2396 O  O   . TYR   A 113 ? 0.1265 0.1282 0.1758 -0.0043 0.0173  0.0049  113 TYR   A O   
2397 C  CB  . TYR   A 113 ? 0.1234 0.1294 0.1946 -0.0014 0.0062  0.0156  113 TYR   A CB  
2398 C  CG  . TYR   A 113 ? 0.1307 0.1335 0.1724 -0.0084 0.0102  0.0237  113 TYR   A CG  
2399 C  CD1 . TYR   A 113 ? 0.1285 0.1401 0.1715 -0.0006 0.0074  0.0215  113 TYR   A CD1 
2400 C  CD2 . TYR   A 113 ? 0.1349 0.1397 0.1723 -0.0124 0.0044  0.0286  113 TYR   A CD2 
2401 C  CE1 . TYR   A 113 ? 0.1370 0.1529 0.1727 -0.0025 0.0081  0.0283  113 TYR   A CE1 
2402 C  CE2 . TYR   A 113 ? 0.1337 0.1475 0.1774 -0.0130 -0.0000 0.0373  113 TYR   A CE2 
2403 C  CZ  . TYR   A 113 ? 0.1293 0.1480 0.1793 0.0015  0.0116  0.0327  113 TYR   A CZ  
2404 O  OH  . TYR   A 113 ? 0.1317 0.1519 0.1997 0.0108  0.0056  0.0286  113 TYR   A OH  
2414 N  N   . GLU   A 114 ? 0.1241 0.1227 0.1725 -0.0045 0.0118  0.0143  114 GLU   A N   
2415 C  CA  . GLU   A 114 ? 0.1299 0.1191 0.1808 0.0005  0.0098  0.0200  114 GLU   A CA  
2416 C  C   . GLU   A 114 ? 0.1260 0.1256 0.1711 -0.0012 0.0111  0.0159  114 GLU   A C   
2417 O  O   . GLU   A 114 ? 0.1350 0.1260 0.1790 0.0006  0.0053  0.0105  114 GLU   A O   
2418 C  CB  . GLU   A 114 ? 0.1309 0.1205 0.1906 -0.0035 0.0134  0.0116  114 GLU   A CB  
2419 C  CG  . GLU   A 114 ? 0.1364 0.1268 0.1924 0.0006  0.0113  0.0095  114 GLU   A CG  
2420 C  CD  . GLU   A 114 ? 0.1444 0.1260 0.2070 -0.0022 -0.0005 0.0023  114 GLU   A CD  
2421 O  OE1 . GLU   A 114 ? 0.1489 0.1254 0.2216 -0.0100 0.0083  -0.0086 114 GLU   A OE1 
2422 O  OE2 . GLU   A 114 ? 0.1623 0.1408 0.2226 -0.0089 0.0126  -0.0091 114 GLU   A OE2 
2429 N  N   . ASN   A 115 ? 0.1276 0.1255 0.1674 -0.0073 0.0113  0.0058  115 ASN   A N   
2430 C  CA  . ASN   A 115 ? 0.1352 0.1324 0.1690 -0.0072 0.0105  0.0069  115 ASN   A CA  
2431 C  C   . ASN   A 115 ? 0.1341 0.1298 0.1621 -0.0125 0.0002  0.0007  115 ASN   A C   
2432 O  O   . ASN   A 115 ? 0.1335 0.1402 0.1767 -0.0123 0.0141  0.0103  115 ASN   A O   
2433 C  CB  . ASN   A 115 ? 0.1385 0.1381 0.1734 -0.0104 0.0131  0.0183  115 ASN   A CB  
2434 C  CG  . ASN   A 115 ? 0.1351 0.1624 0.1833 -0.0154 0.0180  0.0129  115 ASN   A CG  
2435 O  OD1 . ASN   A 115 ? 0.1408 0.2590 0.2089 -0.0137 0.0250  0.0279  115 ASN   A OD1 
2436 N  ND2 . ASN   A 115 ? 0.1361 0.1429 0.1825 -0.0179 0.0278  0.0192  115 ASN   A ND2 
2443 N  N   . PHE   A 116 ? 0.1271 0.1293 0.1635 0.0000  0.0095  0.0156  116 PHE   A N   
2444 C  CA  . PHE   A 116 ? 0.1308 0.1382 0.1605 0.0016  0.0128  0.0149  116 PHE   A CA  
2445 C  C   . PHE   A 116 ? 0.1284 0.1420 0.1704 -0.0079 0.0149  0.0250  116 PHE   A C   
2446 O  O   . PHE   A 116 ? 0.1275 0.1467 0.1822 0.0047  0.0139  0.0251  116 PHE   A O   
2447 C  CB  . PHE   A 116 ? 0.1263 0.1323 0.1782 -0.0005 0.0200  0.0154  116 PHE   A CB  
2448 C  CG  . PHE   A 116 ? 0.1278 0.1279 0.1696 -0.0018 0.0116  0.0142  116 PHE   A CG  
2449 C  CD1 . PHE   A 116 ? 0.1357 0.1279 0.1692 -0.0056 0.0102  0.0184  116 PHE   A CD1 
2450 C  CD2 . PHE   A 116 ? 0.1354 0.1333 0.1749 0.0020  0.0174  0.0227  116 PHE   A CD2 
2451 C  CE1 . PHE   A 116 ? 0.1343 0.1257 0.1821 -0.0076 0.0055  0.0064  116 PHE   A CE1 
2452 C  CE2 . PHE   A 116 ? 0.1355 0.1352 0.1851 -0.0028 0.0206  0.0108  116 PHE   A CE2 
2453 C  CZ  . PHE   A 116 ? 0.1374 0.1195 0.1745 -0.0020 0.0035  0.0163  116 PHE   A CZ  
2463 N  N   . ASN   A 117 ? 0.1343 0.1346 0.1794 -0.0078 0.0105  0.0269  117 ASN   A N   
2464 C  CA  . ASN   A 117 ? 0.1361 0.1307 0.1932 -0.0014 0.0122  0.0263  117 ASN   A CA  
2465 C  C   . ASN   A 117 ? 0.1333 0.1366 0.2022 -0.0031 0.0141  0.0208  117 ASN   A C   
2466 O  O   . ASN   A 117 ? 0.1428 0.1455 0.2249 -0.0022 -0.0085 0.0355  117 ASN   A O   
2467 C  CB  . ASN   A 117 ? 0.1370 0.1318 0.2016 -0.0036 0.0074  0.0297  117 ASN   A CB  
2468 C  CG  . ASN   A 117 ? 0.1294 0.1340 0.2012 -0.0032 0.0039  0.0289  117 ASN   A CG  
2469 O  OD1 . ASN   A 117 ? 0.1356 0.1573 0.2053 -0.0097 0.0067  0.0206  117 ASN   A OD1 
2470 N  ND2 . ASN   A 117 ? 0.1243 0.1318 0.1970 -0.0046 0.0058  0.0282  117 ASN   A ND2 
2477 N  N   . GLN   A 118 ? 0.1324 0.1391 0.2101 -0.0021 0.0037  0.0237  118 GLN   A N   
2478 C  CA  . GLN   A 118 ? 0.1425 0.1496 0.2031 -0.0001 -0.0052 0.0231  118 GLN   A CA  
2479 C  C   . GLN   A 118 ? 0.1439 0.1644 0.1880 -0.0016 -0.0092 0.0286  118 GLN   A C   
2480 O  O   . GLN   A 118 ? 0.1407 0.1928 0.2202 0.0063  -0.0171 0.0062  118 GLN   A O   
2481 C  CB  . GLN   A 118 ? 0.1347 0.1513 0.2099 -0.0015 0.0065  0.0224  118 GLN   A CB  
2482 C  CG  . GLN   A 118 ? 0.1359 0.1549 0.2173 -0.0017 0.0083  0.0278  118 GLN   A CG  
2483 C  CD  . GLN   A 118 ? 0.1342 0.1593 0.2249 0.0048  0.0071  0.0261  118 GLN   A CD  
2484 O  OE1 . GLN   A 118 ? 0.1379 0.1759 0.2417 0.0149  0.0034  0.0221  118 GLN   A OE1 
2485 N  NE2 . GLN   A 118 ? 0.1437 0.1619 0.2304 0.0085  0.0039  0.0311  118 GLN   A NE2 
2494 N  N   . HIS   A 119 ? 0.1441 0.1527 0.1848 -0.0009 0.0006  0.0290  119 HIS   A N   
2495 C  CA  . HIS   A 119 ? 0.1492 0.1626 0.1852 -0.0021 -0.0002 0.0306  119 HIS   A CA  
2496 C  C   . HIS   A 119 ? 0.1617 0.1658 0.1765 -0.0062 0.0036  0.0345  119 HIS   A C   
2497 O  O   . HIS   A 119 ? 0.1674 0.1810 0.1891 -0.0288 0.0004  0.0346  119 HIS   A O   
2498 C  CB  . HIS   A 119 ? 0.1504 0.1577 0.2062 0.0015  0.0178  0.0265  119 HIS   A CB  
2499 C  CG  . HIS   A 119 ? 0.1568 0.1645 0.2354 0.0025  0.0079  0.0409  119 HIS   A CG  
2500 N  ND1 . HIS   A 119 ? 0.1775 0.1860 0.2833 -0.0067 0.0039  0.0351  119 HIS   A ND1 
2501 C  CD2 . HIS   A 119 ? 0.1632 0.1774 0.2602 0.0119  0.0244  0.0568  119 HIS   A CD2 
2502 C  CE1 . HIS   A 119 ? 0.1686 0.1838 0.3045 -0.0137 0.0236  0.0559  119 HIS   A CE1 
2503 N  NE2 . HIS   A 119 ? 0.1727 0.1787 0.3102 0.0017  0.0364  0.0632  119 HIS   A NE2 
2511 N  N   . GLU   A 120 ? 0.1640 0.1890 0.1936 -0.0016 -0.0127 0.0558  120 GLU   A N   
2512 C  CA  . GLU   A 120 ? 0.1849 0.2165 0.2189 0.0021  -0.0069 0.0877  120 GLU   A CA  
2513 C  C   . GLU   A 120 ? 0.1736 0.2028 0.1916 -0.0124 0.0017  0.0779  120 GLU   A C   
2514 O  O   . GLU   A 120 ? 0.1736 0.1947 0.2142 -0.0106 0.0027  0.0742  120 GLU   A O   
2515 C  CB  . GLU   A 120 ? 0.2378 0.2761 0.2697 0.0189  -0.0106 0.1338  120 GLU   A CB  
2516 C  CG  . GLU   A 120 ? 0.3274 0.3468 0.3827 0.0324  -0.0027 0.1384  120 GLU   A CG  
2517 C  CD  . GLU   A 120 ? 0.4055 0.4056 0.4885 0.0491  0.0092  0.1345  120 GLU   A CD  
2518 O  OE1 . GLU   A 120 ? 0.4293 0.4224 0.4998 0.0509  0.0151  0.1343  120 GLU   A OE1 
2519 O  OE2 . GLU   A 120 ? 0.4370 0.4299 0.5394 0.0540  0.0118  0.1347  120 GLU   A OE2 
2526 N  N   . VAL   A 121 ? 0.1613 0.2011 0.1733 -0.0129 0.0081  0.0595  121 VAL   A N   
2527 C  CA  . VAL   A 121 ? 0.1757 0.2170 0.1595 -0.0092 0.0245  0.0671  121 VAL   A CA  
2528 C  C   . VAL   A 121 ? 0.1672 0.1982 0.1433 -0.0195 0.0103  0.0529  121 VAL   A C   
2529 O  O   . VAL   A 121 ? 0.1693 0.1942 0.1718 -0.0271 -0.0117 0.0382  121 VAL   A O   
2530 C  CB  . VAL   A 121 ? 0.2171 0.2586 0.2039 0.0060  0.0433  0.0720  121 VAL   A CB  
2531 C  CG1 . VAL   A 121 ? 0.2196 0.2774 0.2092 0.0175  0.0525  0.0632  121 VAL   A CG1 
2532 C  CG2 . VAL   A 121 ? 0.2439 0.2780 0.2567 -0.0031 0.0355  0.0551  121 VAL   A CG2 
2542 N  N   . LEU   A 122 ? 0.1534 0.1758 0.1567 -0.0184 0.0071  0.0517  122 LEU   A N   
2543 C  CA  . LEU   A 122 ? 0.1611 0.1574 0.1616 -0.0178 0.0209  0.0389  122 LEU   A CA  
2544 C  C   . LEU   A 122 ? 0.1577 0.1555 0.1629 -0.0241 0.0103  0.0350  122 LEU   A C   
2545 O  O   . LEU   A 122 ? 0.1566 0.1595 0.1960 -0.0281 0.0104  0.0339  122 LEU   A O   
2546 C  CB  . LEU   A 122 ? 0.1757 0.1604 0.1902 -0.0067 0.0134  0.0473  122 LEU   A CB  
2547 C  CG  . LEU   A 122 ? 0.1756 0.1632 0.1876 -0.0079 0.0244  0.0306  122 LEU   A CG  
2548 C  CD1 . LEU   A 122 ? 0.1881 0.1706 0.1988 -0.0138 0.0276  0.0325  122 LEU   A CD1 
2549 C  CD2 . LEU   A 122 ? 0.1732 0.1543 0.1846 -0.0164 0.0295  0.0271  122 LEU   A CD2 
2561 N  N   . LEU   A 123 ? 0.1479 0.1545 0.1550 -0.0258 0.0015  0.0281  123 LEU   A N   
2562 C  CA  . LEU   A 123 ? 0.1460 0.1546 0.1594 -0.0162 0.0083  0.0259  123 LEU   A CA  
2563 C  C   . LEU   A 123 ? 0.1471 0.1459 0.1363 -0.0153 0.0065  0.0339  123 LEU   A C   
2564 O  O   . LEU   A 123 ? 0.1404 0.1637 0.1578 -0.0263 0.0031  0.0296  123 LEU   A O   
2565 C  CB  . LEU   A 123 ? 0.1554 0.1586 0.1516 -0.0215 0.0102  0.0289  123 LEU   A CB  
2566 C  CG  . LEU   A 123 ? 0.1572 0.1725 0.1649 -0.0168 0.0060  0.0122  123 LEU   A CG  
2567 C  CD1 . LEU   A 123 ? 0.1614 0.1824 0.1808 -0.0075 0.0162  0.0066  123 LEU   A CD1 
2568 C  CD2 . LEU   A 123 ? 0.1781 0.1828 0.1707 -0.0162 0.0057  0.0147  123 LEU   A CD2 
2580 N  N   A ALA   A 124 ? 0.1405 0.1440 0.1336 -0.0080 0.0068  0.0247  124 ALA   A N   
2581 N  N   B ALA   A 124 ? 0.1491 0.1427 0.1434 -0.0213 0.0089  0.0204  124 ALA   A N   
2582 C  CA  A ALA   A 124 ? 0.1267 0.1348 0.1318 -0.0012 -0.0022 0.0218  124 ALA   A CA  
2583 C  CA  B ALA   A 124 ? 0.1485 0.1378 0.1545 -0.0254 0.0066  0.0165  124 ALA   A CA  
2584 C  C   A ALA   A 124 ? 0.1266 0.1298 0.1357 0.0005  0.0172  0.0141  124 ALA   A C   
2585 C  C   B ALA   A 124 ? 0.1408 0.1224 0.1494 -0.0123 0.0148  0.0154  124 ALA   A C   
2586 O  O   A ALA   A 124 ? 0.1277 0.1402 0.1491 -0.0019 0.0189  0.0222  124 ALA   A O   
2587 O  O   B ALA   A 124 ? 0.1390 0.1158 0.1653 -0.0072 0.0204  0.0159  124 ALA   A O   
2588 C  CB  A ALA   A 124 ? 0.1220 0.1277 0.1529 0.0061  -0.0085 0.0321  124 ALA   A CB  
2589 C  CB  B ALA   A 124 ? 0.1617 0.1429 0.1788 -0.0321 0.0094  0.0197  124 ALA   A CB  
2600 N  N   A PRO   A 125 ? 0.1267 0.1230 0.1382 0.0060  0.0132  0.0184  125 PRO   A N   
2601 N  N   B PRO   A 125 ? 0.1273 0.1138 0.1357 -0.0036 0.0080  0.0052  125 PRO   A N   
2602 C  CA  A PRO   A 125 ? 0.1394 0.1269 0.1477 0.0009  0.0018  0.0134  125 PRO   A CA  
2603 C  CA  B PRO   A 125 ? 0.1298 0.1185 0.1438 0.0050  0.0007  0.0095  125 PRO   A CA  
2604 C  C   A PRO   A 125 ? 0.1359 0.1419 0.1353 -0.0054 0.0022  0.0172  125 PRO   A C   
2605 C  C   B PRO   A 125 ? 0.1191 0.1219 0.1516 0.0039  0.0014  0.0117  125 PRO   A C   
2606 O  O   A PRO   A 125 ? 0.1444 0.1453 0.1246 -0.0038 0.0043  0.0132  125 PRO   A O   
2607 O  O   B PRO   A 125 ? 0.1175 0.1261 0.1490 0.0041  0.0074  0.0053  125 PRO   A O   
2608 C  CB  A PRO   A 125 ? 0.1576 0.1275 0.1546 -0.0096 0.0113  0.0181  125 PRO   A CB  
2609 C  CB  B PRO   A 125 ? 0.1350 0.1181 0.1398 0.0059  -0.0028 0.0058  125 PRO   A CB  
2610 C  CG  A PRO   A 125 ? 0.1600 0.1368 0.1682 -0.0075 0.0134  0.0239  125 PRO   A CG  
2611 C  CG  B PRO   A 125 ? 0.1300 0.1157 0.1355 0.0010  0.0045  0.0060  125 PRO   A CG  
2612 C  CD  A PRO   A 125 ? 0.1422 0.1345 0.1625 -0.0017 0.0227  0.0236  125 PRO   A CD  
2613 C  CD  B PRO   A 125 ? 0.1226 0.1081 0.1216 -0.0060 0.0105  0.0016  125 PRO   A CD  
2628 N  N   A LEU   A 126 ? 0.1313 0.1462 0.1524 -0.0041 0.0056  0.0155  126 LEU   A N   
2629 N  N   B LEU   A 126 ? 0.1185 0.1233 0.1710 0.0077  0.0039  0.0074  126 LEU   A N   
2630 C  CA  A LEU   A 126 ? 0.1334 0.1509 0.1589 -0.0139 0.0009  0.0209  126 LEU   A CA  
2631 C  CA  B LEU   A 126 ? 0.1269 0.1272 0.1666 0.0052  -0.0081 0.0174  126 LEU   A CA  
2632 C  C   A LEU   A 126 ? 0.1347 0.1455 0.1607 -0.0109 0.0040  0.0136  126 LEU   A C   
2633 C  C   B LEU   A 126 ? 0.1300 0.1417 0.1460 0.0040  -0.0208 0.0230  126 LEU   A C   
2634 O  O   A LEU   A 126 ? 0.1408 0.1316 0.1986 -0.0076 0.0233  0.0141  126 LEU   A O   
2635 O  O   B LEU   A 126 ? 0.1271 0.1457 0.1594 0.0024  -0.0384 0.0140  126 LEU   A O   
2636 C  CB  A LEU   A 126 ? 0.1417 0.1623 0.1934 -0.0149 0.0030  0.0139  126 LEU   A CB  
2637 C  CB  B LEU   A 126 ? 0.1337 0.1199 0.1722 0.0055  -0.0094 0.0188  126 LEU   A CB  
2638 C  CG  A LEU   A 126 ? 0.1332 0.1723 0.2144 -0.0105 0.0124  0.0116  126 LEU   A CG  
2639 C  CG  B LEU   A 126 ? 0.1386 0.1209 0.1789 0.0056  -0.0016 0.0212  126 LEU   A CG  
2640 C  CD1 A LEU   A 126 ? 0.1404 0.1813 0.2291 -0.0110 0.0041  0.0122  126 LEU   A CD1 
2641 C  CD1 B LEU   A 126 ? 0.1396 0.1174 0.1911 0.0070  0.0032  0.0212  126 LEU   A CD1 
2642 C  CD2 A LEU   A 126 ? 0.1378 0.1773 0.2249 -0.0153 -0.0047 0.0337  126 LEU   A CD2 
2643 C  CD2 B LEU   A 126 ? 0.1456 0.1152 0.1665 0.0110  0.0011  0.0225  126 LEU   A CD2 
2666 N  N   A LEU   A 127 ? 0.1400 0.1536 0.1725 -0.0012 0.0129  0.0182  127 LEU   A N   
2667 N  N   B LEU   A 127 ? 0.1299 0.1444 0.1269 0.0015  -0.0084 0.0389  127 LEU   A N   
2668 C  CA  A LEU   A 127 ? 0.1398 0.1496 0.1605 -0.0056 0.0042  0.0201  127 LEU   A CA  
2669 C  CA  B LEU   A 127 ? 0.1291 0.1469 0.1341 -0.0064 -0.0090 0.0437  127 LEU   A CA  
2670 C  C   A LEU   A 127 ? 0.1350 0.1383 0.1369 -0.0003 0.0029  0.0085  127 LEU   A C   
2671 C  C   B LEU   A 127 ? 0.1235 0.1326 0.1583 -0.0033 -0.0130 0.0312  127 LEU   A C   
2672 O  O   A LEU   A 127 ? 0.1476 0.1425 0.1505 -0.0111 0.0025  0.0023  127 LEU   A O   
2673 O  O   B LEU   A 127 ? 0.1224 0.1286 0.1591 -0.0045 -0.0078 0.0440  127 LEU   A O   
2674 C  CB  A LEU   A 127 ? 0.1313 0.1420 0.1677 0.0050  0.0094  0.0274  127 LEU   A CB  
2675 C  CB  B LEU   A 127 ? 0.1288 0.1642 0.1356 -0.0089 -0.0078 0.0407  127 LEU   A CB  
2676 C  CG  A LEU   A 127 ? 0.1376 0.1502 0.1711 0.0102  -0.0039 0.0282  127 LEU   A CG  
2677 C  CG  B LEU   A 127 ? 0.1356 0.1750 0.1334 -0.0024 -0.0081 0.0374  127 LEU   A CG  
2678 C  CD1 A LEU   A 127 ? 0.1479 0.1401 0.1839 -0.0036 -0.0179 0.0131  127 LEU   A CD1 
2679 C  CD1 B LEU   A 127 ? 0.1399 0.1805 0.1533 0.0107  -0.0057 0.0372  127 LEU   A CD1 
2680 C  CD2 A LEU   A 127 ? 0.1552 0.1570 0.1847 0.0147  -0.0130 0.0335  127 LEU   A CD2 
2681 C  CD2 B LEU   A 127 ? 0.1450 0.1817 0.1265 -0.0061 -0.0164 0.0198  127 LEU   A CD2 
2704 N  N   A SER   A 128 ? 0.1460 0.1399 0.1257 -0.0056 0.0011  0.0213  128 SER   A N   
2705 N  N   B SER   A 128 ? 0.1326 0.1303 0.1673 -0.0102 -0.0135 0.0156  128 SER   A N   
2706 C  CA  A SER   A 128 ? 0.1552 0.1383 0.1219 -0.0047 0.0043  0.0156  128 SER   A CA  
2707 C  CA  B SER   A 128 ? 0.1425 0.1279 0.1505 -0.0058 -0.0049 0.0067  128 SER   A CA  
2708 C  C   A SER   A 128 ? 0.1592 0.1459 0.1269 -0.0000 0.0056  0.0263  128 SER   A C   
2709 C  C   B SER   A 128 ? 0.1341 0.1259 0.1378 -0.0054 -0.0175 0.0115  128 SER   A C   
2710 O  O   A SER   A 128 ? 0.1762 0.1669 0.1366 0.0037  0.0138  0.0184  128 SER   A O   
2711 O  O   B SER   A 128 ? 0.1337 0.1295 0.1463 -0.0135 -0.0206 0.0226  128 SER   A O   
2712 C  CB  A SER   A 128 ? 0.1495 0.1334 0.1342 -0.0094 -0.0042 0.0153  128 SER   A CB  
2713 C  CB  B SER   A 128 ? 0.1553 0.1311 0.1529 0.0011  0.0012  0.0055  128 SER   A CB  
2714 O  OG  A SER   A 128 ? 0.1432 0.1418 0.1548 -0.0061 0.0018  0.0062  128 SER   A OG  
2715 O  OG  B SER   A 128 ? 0.1593 0.1289 0.1396 0.0006  0.0104  0.0170  128 SER   A OG  
2726 N  N   A ALA   A 129 ? 0.1482 0.1520 0.1418 -0.0017 0.0012  0.0231  129 ALA   A N   
2727 N  N   B ALA   A 129 ? 0.1244 0.1285 0.1413 0.0051  -0.0241 0.0055  129 ALA   A N   
2728 C  CA  A ALA   A 129 ? 0.1455 0.1505 0.1638 -0.0003 0.0010  0.0119  129 ALA   A CA  
2729 C  CA  B ALA   A 129 ? 0.1238 0.1326 0.1608 0.0044  -0.0215 0.0014  129 ALA   A CA  
2730 C  C   A ALA   A 129 ? 0.1514 0.1432 0.1617 0.0006  -0.0069 0.0015  129 ALA   A C   
2731 C  C   B ALA   A 129 ? 0.1346 0.1434 0.1745 0.0047  -0.0148 0.0030  129 ALA   A C   
2732 O  O   A ALA   A 129 ? 0.1556 0.1513 0.1567 -0.0046 -0.0018 0.0122  129 ALA   A O   
2733 O  O   B ALA   A 129 ? 0.1331 0.1511 0.1675 0.0050  -0.0180 0.0005  129 ALA   A O   
2734 C  CB  A ALA   A 129 ? 0.1600 0.1709 0.1886 0.0048  0.0057  0.0192  129 ALA   A CB  
2735 C  CB  B ALA   A 129 ? 0.1216 0.1267 0.1536 0.0052  -0.0271 0.0051  129 ALA   A CB  
2746 N  N   A GLY   A 130 ? 0.1565 0.1407 0.2054 0.0034  -0.0026 -0.0011 130 GLY   A N   
2747 N  N   B GLY   A 130 ? 0.1438 0.1454 0.1947 0.0015  -0.0087 0.0118  130 GLY   A N   
2748 C  CA  A GLY   A 130 ? 0.1662 0.1454 0.2176 0.0083  -0.0071 -0.0010 130 GLY   A CA  
2749 C  CA  B GLY   A 130 ? 0.1490 0.1445 0.1887 0.0025  0.0021  0.0225  130 GLY   A CA  
2750 C  C   A GLY   A 130 ? 0.1634 0.1437 0.2163 0.0068  -0.0168 -0.0028 130 GLY   A C   
2751 C  C   B GLY   A 130 ? 0.1505 0.1460 0.1763 0.0044  0.0041  0.0205  130 GLY   A C   
2752 O  O   A GLY   A 130 ? 0.1629 0.1462 0.2258 0.0115  -0.0235 -0.0017 130 GLY   A O   
2753 O  O   B GLY   A 130 ? 0.1505 0.1443 0.1695 -0.0053 0.0001  0.0143  130 GLY   A O   
2760 N  N   A ILE   A 131 ? 0.1715 0.1389 0.1984 -0.0048 -0.0131 0.0073  131 ILE   A N   
2761 N  N   B ILE   A 131 ? 0.1540 0.1484 0.1738 0.0086  0.0084  0.0192  131 ILE   A N   
2762 C  CA  A ILE   A 131 ? 0.1868 0.1402 0.1609 -0.0108 -0.0283 0.0065  131 ILE   A CA  
2763 C  CA  B ILE   A 131 ? 0.1646 0.1500 0.1581 0.0045  0.0078  0.0110  131 ILE   A CA  
2764 C  C   A ILE   A 131 ? 0.1764 0.1426 0.1450 -0.0082 -0.0235 0.0167  131 ILE   A C   
2765 C  C   B ILE   A 131 ? 0.1685 0.1484 0.1491 0.0029  0.0013  0.0123  131 ILE   A C   
2766 O  O   A ILE   A 131 ? 0.1872 0.1505 0.1629 0.0044  -0.0171 0.0204  131 ILE   A O   
2767 O  O   B ILE   A 131 ? 0.1714 0.1427 0.1599 0.0117  -0.0113 0.0101  131 ILE   A O   
2768 C  CB  A ILE   A 131 ? 0.2089 0.1547 0.1658 -0.0161 -0.0299 -0.0001 131 ILE   A CB  
2769 C  CB  B ILE   A 131 ? 0.1707 0.1551 0.1566 -0.0023 0.0107  0.0054  131 ILE   A CB  
2770 C  CG1 A ILE   A 131 ? 0.2180 0.1860 0.1756 -0.0319 -0.0264 0.0080  131 ILE   A CG1 
2771 C  CG1 B ILE   A 131 ? 0.1747 0.1716 0.1538 -0.0143 0.0016  0.0106  131 ILE   A CG1 
2772 C  CG2 A ILE   A 131 ? 0.2196 0.1428 0.1760 -0.0091 -0.0168 -0.0026 131 ILE   A CG2 
2773 C  CG2 B ILE   A 131 ? 0.1748 0.1496 0.1690 -0.0018 0.0101  -0.0069 131 ILE   A CG2 
2774 C  CD1 A ILE   A 131 ? 0.2230 0.1943 0.1898 -0.0454 -0.0253 -0.0025 131 ILE   A CD1 
2775 C  CD1 B ILE   A 131 ? 0.1780 0.1788 0.1628 -0.0204 -0.0017 0.0264  131 ILE   A CD1 
2798 N  N   A PHE   A 132 ? 0.1583 0.1388 0.1512 -0.0006 -0.0189 0.0253  132 PHE   A N   
2799 N  N   B PHE   A 132 ? 0.1726 0.1512 0.1573 -0.0004 0.0020  0.0103  132 PHE   A N   
2800 C  CA  A PHE   A 132 ? 0.1676 0.1367 0.1596 0.0016  -0.0119 0.0134  132 PHE   A CA  
2801 C  CA  B PHE   A 132 ? 0.1831 0.1565 0.1474 -0.0006 -0.0034 -0.0009 132 PHE   A CA  
2802 C  C   A PHE   A 132 ? 0.1790 0.1444 0.1746 0.0020  -0.0216 0.0165  132 PHE   A C   
2803 C  C   B PHE   A 132 ? 0.1927 0.1646 0.1558 -0.0004 -0.0143 -0.0016 132 PHE   A C   
2804 O  O   A PHE   A 132 ? 0.1960 0.1446 0.1818 -0.0054 -0.0195 0.0097  132 PHE   A O   
2805 O  O   B PHE   A 132 ? 0.2038 0.1705 0.1555 -0.0008 -0.0229 -0.0079 132 PHE   A O   
2806 C  CB  A PHE   A 132 ? 0.1610 0.1334 0.1495 -0.0026 -0.0133 0.0253  132 PHE   A CB  
2807 C  CB  B PHE   A 132 ? 0.1820 0.1550 0.1441 0.0021  -0.0048 -0.0136 132 PHE   A CB  
2808 C  CG  A PHE   A 132 ? 0.1660 0.1346 0.1496 0.0048  -0.0136 0.0218  132 PHE   A CG  
2809 C  CG  B PHE   A 132 ? 0.1808 0.1572 0.1399 0.0084  -0.0060 -0.0169 132 PHE   A CG  
2810 C  CD1 A PHE   A 132 ? 0.1632 0.1512 0.1739 0.0161  -0.0170 0.0068  132 PHE   A CD1 
2811 C  CD1 B PHE   A 132 ? 0.1799 0.1657 0.1478 0.0122  -0.0032 -0.0238 132 PHE   A CD1 
2812 C  CD2 A PHE   A 132 ? 0.1706 0.1488 0.1595 0.0086  -0.0211 0.0166  132 PHE   A CD2 
2813 C  CD2 B PHE   A 132 ? 0.1823 0.1599 0.1427 0.0107  -0.0037 -0.0254 132 PHE   A CD2 
2814 C  CE1 A PHE   A 132 ? 0.1672 0.1627 0.1763 0.0148  -0.0275 -0.0017 132 PHE   A CE1 
2815 C  CE1 B PHE   A 132 ? 0.1835 0.1720 0.1542 0.0126  0.0003  -0.0274 132 PHE   A CE1 
2816 C  CE2 A PHE   A 132 ? 0.1702 0.1608 0.1732 0.0102  -0.0342 0.0166  132 PHE   A CE2 
2817 C  CE2 B PHE   A 132 ? 0.1832 0.1703 0.1609 0.0140  0.0043  -0.0249 132 PHE   A CE2 
2818 C  CZ  A PHE   A 132 ? 0.1644 0.1614 0.1810 0.0037  -0.0425 0.0089  132 PHE   A CZ  
2819 C  CZ  B PHE   A 132 ? 0.1814 0.1699 0.1583 0.0122  0.0047  -0.0285 132 PHE   A CZ  
2838 N  N   A GLY   A 133 ? 0.1832 0.1562 0.1710 -0.0020 -0.0421 0.0187  133 GLY   A N   
2839 N  N   B GLY   A 133 ? 0.1920 0.1672 0.1645 -0.0028 -0.0249 0.0046  133 GLY   A N   
2840 C  CA  A GLY   A 133 ? 0.1917 0.1692 0.1828 0.0002  -0.0476 0.0086  133 GLY   A CA  
2841 C  CA  B GLY   A 133 ? 0.1932 0.1708 0.1784 -0.0036 -0.0258 0.0013  133 GLY   A CA  
2842 C  C   A GLY   A 133 ? 0.1868 0.1781 0.1795 0.0022  -0.0494 0.0027  133 GLY   A C   
2843 C  C   B GLY   A 133 ? 0.1882 0.1725 0.1834 -0.0045 -0.0244 -0.0041 133 GLY   A C   
2844 O  O   A GLY   A 133 ? 0.1973 0.1923 0.1784 -0.0024 -0.0409 -0.0164 133 GLY   A O   
2845 O  O   B GLY   A 133 ? 0.1833 0.1764 0.1865 0.0019  -0.0261 -0.0154 133 GLY   A O   
2852 N  N   A ALA   A 134 ? 0.1791 0.1685 0.1743 0.0039  -0.0421 0.0043  134 ALA   A N   
2853 N  N   B ALA   A 134 ? 0.1865 0.1645 0.1820 -0.0101 -0.0240 -0.0034 134 ALA   A N   
2854 C  CA  A ALA   A 134 ? 0.1745 0.1691 0.1968 0.0035  -0.0387 0.0005  134 ALA   A CA  
2855 C  CA  B ALA   A 134 ? 0.1845 0.1583 0.1855 -0.0079 -0.0246 -0.0027 134 ALA   A CA  
2856 C  C   A ALA   A 134 ? 0.1777 0.1732 0.1925 -0.0025 -0.0344 0.0082  134 ALA   A C   
2857 C  C   B ALA   A 134 ? 0.1847 0.1542 0.1670 -0.0032 -0.0239 -0.0074 134 ALA   A C   
2858 O  O   A ALA   A 134 ? 0.1977 0.1795 0.2123 -0.0076 -0.0219 0.0139  134 ALA   A O   
2859 O  O   B ALA   A 134 ? 0.1954 0.1565 0.1591 -0.0021 -0.0110 -0.0080 134 ALA   A O   
2860 C  CB  A ALA   A 134 ? 0.1794 0.1609 0.2342 0.0026  -0.0397 -0.0080 134 ALA   A CB  
2861 C  CB  B ALA   A 134 ? 0.1824 0.1556 0.2061 -0.0117 -0.0240 -0.0022 134 ALA   A CB  
2872 N  N   A ASP   A 135 ? 0.1784 0.1765 0.1997 -0.0069 -0.0272 0.0163  135 ASP   A N   
2873 N  N   B ASP   A 135 ? 0.1823 0.1557 0.1651 -0.0026 -0.0221 -0.0030 135 ASP   A N   
2874 C  CA  A ASP   A 135 ? 0.1829 0.1887 0.2307 -0.0165 -0.0332 0.0222  135 ASP   A CA  
2875 C  CA  B ASP   A 135 ? 0.1798 0.1631 0.1757 -0.0033 -0.0200 0.0010  135 ASP   A CA  
2876 C  C   A ASP   A 135 ? 0.1687 0.1827 0.2372 -0.0109 -0.0279 0.0286  135 ASP   A C   
2877 C  C   B ASP   A 135 ? 0.1656 0.1619 0.1816 0.0057  -0.0168 0.0076  135 ASP   A C   
2878 O  O   A ASP   A 135 ? 0.1616 0.1680 0.2503 -0.0072 -0.0209 0.0375  135 ASP   A O   
2879 O  O   B ASP   A 135 ? 0.1640 0.1611 0.1989 0.0095  -0.0188 0.0103  135 ASP   A O   
2880 C  CB  A ASP   A 135 ? 0.2070 0.2180 0.2531 -0.0382 -0.0541 0.0116  135 ASP   A CB  
2881 C  CB  B ASP   A 135 ? 0.1903 0.1765 0.1908 -0.0045 -0.0293 -0.0047 135 ASP   A CB  
2882 C  CG  A ASP   A 135 ? 0.2288 0.2470 0.2900 -0.0579 -0.0585 0.0044  135 ASP   A CG  
2883 C  CG  B ASP   A 135 ? 0.2011 0.1964 0.2115 -0.0049 -0.0368 -0.0044 135 ASP   A CG  
2884 O  OD1 A ASP   A 135 ? 0.2245 0.2589 0.2806 -0.0630 -0.0625 0.0223  135 ASP   A OD1 
2885 O  OD1 B ASP   A 135 ? 0.2037 0.1965 0.2228 0.0027  -0.0327 0.0006  135 ASP   A OD1 
2886 O  OD2 A ASP   A 135 ? 0.2598 0.2675 0.3419 -0.0613 -0.0403 -0.0001 135 ASP   A OD2 
2887 O  OD2 B ASP   A 135 ? 0.2085 0.2108 0.2251 -0.0084 -0.0488 -0.0141 135 ASP   A OD2 
2896 N  N   A PRO   A 136 ? 0.1583 0.1865 0.2395 0.0043  -0.0160 0.0431  136 PRO   A N   
2897 N  N   B PRO   A 136 ? 0.1612 0.1619 0.1805 0.0133  -0.0079 0.0105  136 PRO   A N   
2898 C  CA  A PRO   A 136 ? 0.1525 0.1940 0.2506 -0.0016 -0.0039 0.0306  136 PRO   A CA  
2899 C  CA  B PRO   A 136 ? 0.1540 0.1705 0.1963 0.0049  0.0014  0.0138  136 PRO   A CA  
2900 C  C   A PRO   A 136 ? 0.1295 0.1866 0.2465 0.0023  -0.0026 0.0303  136 PRO   A C   
2901 C  C   B PRO   A 136 ? 0.1414 0.1731 0.2015 0.0028  0.0006  0.0227  136 PRO   A C   
2902 O  O   A PRO   A 136 ? 0.1216 0.1869 0.2381 -0.0012 0.0042  0.0337  136 PRO   A O   
2903 O  O   B PRO   A 136 ? 0.1405 0.1687 0.1774 0.0032  0.0103  0.0161  136 PRO   A O   
2904 C  CB  A PRO   A 136 ? 0.1735 0.2026 0.2710 0.0001  0.0080  0.0349  136 PRO   A CB  
2905 C  CB  B PRO   A 136 ? 0.1703 0.1729 0.2058 0.0056  0.0072  0.0108  136 PRO   A CB  
2906 C  CG  A PRO   A 136 ? 0.1838 0.2106 0.2827 0.0106  0.0042  0.0312  136 PRO   A CG  
2907 C  CG  B PRO   A 136 ? 0.1744 0.1774 0.2059 0.0116  0.0096  0.0069  136 PRO   A CG  
2908 C  CD  A PRO   A 136 ? 0.1720 0.1997 0.2658 0.0148  -0.0012 0.0411  136 PRO   A CD  
2909 C  CD  B PRO   A 136 ? 0.1674 0.1658 0.1834 0.0198  0.0070  0.0134  136 PRO   A CD  
2924 N  N   . ILE   A 137 ? 0.1409 0.1817 0.2383 -0.0011 -0.0116 0.0360  137 ILE   A N   
2925 C  CA  . ILE   A 137 ? 0.1435 0.1947 0.2484 -0.0122 -0.0211 0.0356  137 ILE   A CA  
2926 C  C   . ILE   A 137 ? 0.1477 0.1866 0.2398 -0.0212 -0.0196 0.0338  137 ILE   A C   
2927 O  O   . ILE   A 137 ? 0.1548 0.1857 0.2465 -0.0169 -0.0183 0.0255  137 ILE   A O   
2928 C  CB  . ILE   A 137 ? 0.1553 0.2172 0.2938 -0.0157 -0.0468 0.0312  137 ILE   A CB  
2929 C  CG1 . ILE   A 137 ? 0.1669 0.2490 0.3407 -0.0072 -0.0516 0.0322  137 ILE   A CG1 
2930 C  CG2 . ILE   A 137 ? 0.1690 0.2196 0.3168 -0.0263 -0.0492 0.0336  137 ILE   A CG2 
2931 C  CD1 . ILE   A 137 ? 0.1953 0.2669 0.3681 0.0005  -0.0431 0.0325  137 ILE   A CD1 
2944 N  N   . HIS   A 138 ? 0.1465 0.1970 0.2273 -0.0110 -0.0130 0.0254  138 HIS   A N   
2945 C  CA  . HIS   A 138 ? 0.1520 0.1955 0.2109 -0.0089 -0.0094 0.0182  138 HIS   A CA  
2946 C  C   . HIS   A 138 ? 0.1399 0.1812 0.2174 -0.0075 -0.0107 0.0269  138 HIS   A C   
2947 O  O   . HIS   A 138 ? 0.1536 0.1770 0.2198 -0.0067 -0.0053 0.0211  138 HIS   A O   
2948 C  CB  . HIS   A 138 ? 0.1725 0.2095 0.2071 -0.0120 -0.0151 0.0025  138 HIS   A CB  
2949 C  CG  . HIS   A 138 ? 0.1935 0.2209 0.2129 -0.0204 -0.0164 -0.0093 138 HIS   A CG  
2950 N  ND1 . HIS   A 138 ? 0.2083 0.2342 0.2343 -0.0167 -0.0160 -0.0213 138 HIS   A ND1 
2951 C  CD2 . HIS   A 138 ? 0.1935 0.2277 0.2132 -0.0151 -0.0139 0.0015  138 HIS   A CD2 
2952 C  CE1 . HIS   A 138 ? 0.2146 0.2430 0.2326 -0.0089 -0.0132 -0.0096 138 HIS   A CE1 
2953 N  NE2 . HIS   A 138 ? 0.2033 0.2408 0.2155 -0.0116 0.0002  0.0022  138 HIS   A NE2 
2961 N  N   . SER   A 139 ? 0.1372 0.1673 0.2111 -0.0032 -0.0063 0.0370  139 SER   A N   
2962 C  CA  . SER   A 139 ? 0.1346 0.1638 0.2049 -0.0078 0.0020  0.0326  139 SER   A CA  
2963 C  C   . SER   A 139 ? 0.1275 0.1575 0.2097 -0.0078 0.0033  0.0251  139 SER   A C   
2964 O  O   . SER   A 139 ? 0.1235 0.1572 0.2246 -0.0115 -0.0007 0.0341  139 SER   A O   
2965 C  CB  . SER   A 139 ? 0.1295 0.1659 0.2001 -0.0111 -0.0078 0.0347  139 SER   A CB  
2966 O  OG  . SER   A 139 ? 0.1409 0.1558 0.2164 -0.0148 -0.0175 0.0379  139 SER   A OG  
2972 N  N   . LEU   A 140 ? 0.1258 0.1587 0.2123 -0.0005 -0.0021 0.0368  140 LEU   A N   
2973 C  CA  . LEU   A 140 ? 0.1281 0.1555 0.1966 -0.0022 -0.0028 0.0334  140 LEU   A CA  
2974 C  C   . LEU   A 140 ? 0.1247 0.1610 0.2063 -0.0140 -0.0008 0.0296  140 LEU   A C   
2975 O  O   . LEU   A 140 ? 0.1334 0.1639 0.2246 -0.0043 -0.0006 0.0364  140 LEU   A O   
2976 C  CB  . LEU   A 140 ? 0.1306 0.1602 0.2030 -0.0052 -0.0007 0.0254  140 LEU   A CB  
2977 C  CG  . LEU   A 140 ? 0.1330 0.1719 0.2252 -0.0162 0.0072  0.0375  140 LEU   A CG  
2978 C  CD1 . LEU   A 140 ? 0.1284 0.1794 0.2439 -0.0040 0.0076  0.0341  140 LEU   A CD1 
2979 C  CD2 . LEU   A 140 ? 0.1386 0.1885 0.2405 -0.0074 0.0092  0.0442  140 LEU   A CD2 
2991 N  N   . ARG   A 141 ? 0.1339 0.1592 0.2147 -0.0085 -0.0013 0.0257  141 ARG   A N   
2992 C  CA  . ARG   A 141 ? 0.1512 0.1729 0.2365 -0.0157 -0.0108 0.0110  141 ARG   A CA  
2993 C  C   . ARG   A 141 ? 0.1433 0.1559 0.2135 -0.0107 -0.0102 0.0073  141 ARG   A C   
2994 O  O   . ARG   A 141 ? 0.1395 0.1519 0.2315 -0.0104 0.0031  0.0180  141 ARG   A O   
2995 C  CB  . ARG   A 141 ? 0.1623 0.2006 0.2569 -0.0208 -0.0131 -0.0127 141 ARG   A CB  
2996 C  CG  . ARG   A 141 ? 0.2056 0.2465 0.3009 -0.0307 0.0015  -0.0215 141 ARG   A CG  
2997 C  CD  . ARG   A 141 ? 0.2440 0.2943 0.3472 -0.0445 0.0055  -0.0301 141 ARG   A CD  
2998 N  NE  . ARG   A 141 ? 0.2340 0.3396 0.3611 -0.0454 -0.0026 -0.0350 141 ARG   A NE  
2999 C  CZ  . ARG   A 141 ? 0.2322 0.3650 0.3621 -0.0708 0.0105  -0.0282 141 ARG   A CZ  
3000 N  NH1 . ARG   A 141 ? 0.2224 0.3684 0.3512 -0.0857 0.0436  -0.0422 141 ARG   A NH1 
3001 N  NH2 . ARG   A 141 ? 0.2328 0.3847 0.3807 -0.0715 -0.0073 -0.0199 141 ARG   A NH2 
3015 N  N   . VAL   A 142 ? 0.1358 0.1541 0.2005 -0.0074 -0.0019 0.0100  142 VAL   A N   
3016 C  CA  . VAL   A 142 ? 0.1383 0.1534 0.2076 -0.0086 0.0164  0.0061  142 VAL   A CA  
3017 C  C   . VAL   A 142 ? 0.1239 0.1522 0.1971 -0.0154 0.0041  0.0133  142 VAL   A C   
3018 O  O   . VAL   A 142 ? 0.1308 0.1559 0.2113 -0.0019 0.0009  0.0185  142 VAL   A O   
3019 C  CB  . VAL   A 142 ? 0.1456 0.1611 0.1959 -0.0049 0.0085  0.0175  142 VAL   A CB  
3020 C  CG1 . VAL   A 142 ? 0.1495 0.1545 0.2101 -0.0072 0.0127  0.0119  142 VAL   A CG1 
3021 C  CG2 . VAL   A 142 ? 0.1614 0.1814 0.2311 0.0047  0.0078  0.0227  142 VAL   A CG2 
3031 N  N   . CYS   A 143 ? 0.1297 0.1463 0.1925 -0.0127 -0.0009 0.0132  143 CYS   A N   
3032 C  CA  . CYS   A 143 ? 0.1289 0.1496 0.2067 -0.0123 0.0081  0.0151  143 CYS   A CA  
3033 C  C   . CYS   A 143 ? 0.1277 0.1437 0.2113 -0.0095 0.0027  0.0219  143 CYS   A C   
3034 O  O   . CYS   A 143 ? 0.1274 0.1506 0.2018 -0.0109 0.0022  0.0252  143 CYS   A O   
3035 C  CB  . CYS   A 143 ? 0.1387 0.1567 0.2149 -0.0035 0.0173  0.0202  143 CYS   A CB  
3036 S  SG  . CYS   A 143 ? 0.1548 0.1576 0.1965 0.0041  0.0108  0.0158  143 CYS   A SG  
3042 N  N   . VAL   A 144 ? 0.1292 0.1401 0.2248 -0.0039 0.0115  0.0318  144 VAL   A N   
3043 C  CA  . VAL   A 144 ? 0.1365 0.1547 0.2592 -0.0078 0.0195  0.0283  144 VAL   A CA  
3044 C  C   . VAL   A 144 ? 0.1463 0.1481 0.2584 -0.0134 -0.0036 0.0247  144 VAL   A C   
3045 O  O   . VAL   A 144 ? 0.1610 0.1518 0.2496 -0.0018 0.0015  0.0315  144 VAL   A O   
3046 C  CB  . VAL   A 144 ? 0.1610 0.1780 0.3245 0.0058  0.0456  0.0370  144 VAL   A CB  
3047 C  CG1 . VAL   A 144 ? 0.1835 0.2058 0.3656 -0.0090 0.0286  0.0321  144 VAL   A CG1 
3048 C  CG2 . VAL   A 144 ? 0.1382 0.1829 0.3397 0.0008  0.0551  0.0495  144 VAL   A CG2 
3058 N  N   . ASP   A 145 ? 0.1415 0.1432 0.2610 -0.0086 -0.0011 0.0194  145 ASP   A N   
3059 C  CA  . ASP   A 145 ? 0.1528 0.1465 0.2627 -0.0132 -0.0057 0.0114  145 ASP   A CA  
3060 C  C   . ASP   A 145 ? 0.1529 0.1442 0.2595 -0.0080 0.0002  0.0043  145 ASP   A C   
3061 O  O   . ASP   A 145 ? 0.1700 0.1544 0.3171 -0.0113 -0.0034 -0.0333 145 ASP   A O   
3062 C  CB  . ASP   A 145 ? 0.1706 0.1757 0.2825 -0.0200 -0.0152 -0.0003 145 ASP   A CB  
3063 C  CG  . ASP   A 145 ? 0.1884 0.2105 0.3028 -0.0336 -0.0260 0.0050  145 ASP   A CG  
3064 O  OD1 . ASP   A 145 ? 0.1810 0.2222 0.3197 -0.0411 -0.0163 0.0091  145 ASP   A OD1 
3065 O  OD2 . ASP   A 145 ? 0.2132 0.2389 0.3120 -0.0417 -0.0484 0.0038  145 ASP   A OD2 
3070 N  N   . THR   A 146 ? 0.1399 0.1373 0.2153 -0.0038 0.0090  0.0153  146 THR   A N   
3071 C  CA  . THR   A 146 ? 0.1339 0.1378 0.2026 -0.0022 0.0036  0.0098  146 THR   A CA  
3072 C  C   . THR   A 146 ? 0.1261 0.1368 0.2114 0.0045  0.0115  0.0188  146 THR   A C   
3073 O  O   . THR   A 146 ? 0.1363 0.1500 0.2290 0.0028  -0.0015 0.0099  146 THR   A O   
3074 C  CB  . THR   A 146 ? 0.1322 0.1458 0.2081 0.0007  0.0042  0.0261  146 THR   A CB  
3075 O  OG1 . THR   A 146 ? 0.1290 0.1609 0.2098 0.0047  0.0034  0.0191  146 THR   A OG1 
3076 C  CG2 . THR   A 146 ? 0.1313 0.1402 0.2326 -0.0047 0.0136  0.0197  146 THR   A CG2 
3084 N  N   . VAL   A 147 ? 0.1259 0.1384 0.2094 -0.0022 0.0100  0.0183  147 VAL   A N   
3085 C  CA  . VAL   A 147 ? 0.1313 0.1435 0.2054 -0.0077 0.0199  0.0172  147 VAL   A CA  
3086 C  C   . VAL   A 147 ? 0.1332 0.1383 0.2194 -0.0097 0.0142  0.0276  147 VAL   A C   
3087 O  O   . VAL   A 147 ? 0.1337 0.1400 0.2354 -0.0133 0.0047  0.0352  147 VAL   A O   
3088 C  CB  . VAL   A 147 ? 0.1423 0.1407 0.1960 -0.0099 0.0168  0.0240  147 VAL   A CB  
3089 C  CG1 . VAL   A 147 ? 0.1850 0.1453 0.1947 -0.0080 0.0164  0.0404  147 VAL   A CG1 
3090 C  CG2 . VAL   A 147 ? 0.1503 0.1464 0.1973 -0.0142 0.0042  0.0282  147 VAL   A CG2 
3100 N  N   . ARG   A 148 ? 0.1356 0.1466 0.2231 -0.0128 0.0228  0.0426  148 ARG   A N   
3101 C  CA  . ARG   A 148 ? 0.1437 0.1465 0.2234 -0.0133 0.0152  0.0454  148 ARG   A CA  
3102 C  C   . ARG   A 148 ? 0.1513 0.1453 0.2236 -0.0155 0.0125  0.0592  148 ARG   A C   
3103 O  O   . ARG   A 148 ? 0.1794 0.1549 0.2388 -0.0196 0.0198  0.0466  148 ARG   A O   
3104 C  CB  . ARG   A 148 ? 0.1487 0.1389 0.2473 -0.0070 0.0157  0.0357  148 ARG   A CB  
3105 C  CG  . ARG   A 148 ? 0.1649 0.1407 0.2759 -0.0053 0.0334  0.0258  148 ARG   A CG  
3106 C  CD  . ARG   A 148 ? 0.1833 0.1440 0.2957 -0.0065 0.0421  0.0399  148 ARG   A CD  
3107 N  NE  . ARG   A 148 ? 0.1788 0.1523 0.2812 0.0091  0.0431  0.0460  148 ARG   A NE  
3108 C  CZ  . ARG   A 148 ? 0.1759 0.1416 0.2504 0.0010  0.0396  0.0491  148 ARG   A CZ  
3109 N  NH1 . ARG   A 148 ? 0.1839 0.1445 0.2627 -0.0086 0.0396  0.0265  148 ARG   A NH1 
3110 N  NH2 . ARG   A 148 ? 0.1703 0.1593 0.2606 0.0130  0.0361  0.0414  148 ARG   A NH2 
3124 N  N   . THR   A 149 ? 0.1494 0.1560 0.2199 -0.0094 0.0035  0.0517  149 THR   A N   
3125 C  CA  . THR   A 149 ? 0.1525 0.1614 0.2229 -0.0128 0.0060  0.0489  149 THR   A CA  
3126 C  C   . THR   A 149 ? 0.1499 0.1596 0.2054 -0.0200 0.0094  0.0539  149 THR   A C   
3127 O  O   . THR   A 149 ? 0.1485 0.1675 0.2117 -0.0175 0.0046  0.0502  149 THR   A O   
3128 C  CB  . THR   A 149 ? 0.1564 0.1679 0.2186 -0.0093 0.0001  0.0409  149 THR   A CB  
3129 O  OG1 . THR   A 149 ? 0.1590 0.1563 0.2176 -0.0203 -0.0001 0.0421  149 THR   A OG1 
3130 C  CG2 . THR   A 149 ? 0.1556 0.1810 0.2276 -0.0003 -0.0028 0.0296  149 THR   A CG2 
3138 N  N   . ASN   A 150 ? 0.1519 0.1669 0.2067 -0.0119 0.0006  0.0545  150 ASN   A N   
3139 C  CA  . ASN   A 150 ? 0.1661 0.1704 0.2010 -0.0132 0.0086  0.0483  150 ASN   A CA  
3140 C  C   . ASN   A 150 ? 0.1470 0.1578 0.2070 -0.0158 0.0123  0.0489  150 ASN   A C   
3141 O  O   . ASN   A 150 ? 0.1595 0.1693 0.2344 -0.0158 -0.0107 0.0468  150 ASN   A O   
3142 C  CB  . ASN   A 150 ? 0.2163 0.1990 0.2277 -0.0234 0.0180  0.0674  150 ASN   A CB  
3143 C  CG  . ASN   A 150 ? 0.2757 0.2358 0.2882 -0.0246 0.0064  0.0747  150 ASN   A CG  
3144 O  OD1 . ASN   A 150 ? 0.2969 0.2458 0.3066 -0.0302 0.0177  0.0943  150 ASN   A OD1 
3145 N  ND2 . ASN   A 150 ? 0.3097 0.2629 0.3257 -0.0205 -0.0068 0.0801  150 ASN   A ND2 
3152 N  N   . VAL   A 151 ? 0.1483 0.1489 0.2030 -0.0168 0.0096  0.0399  151 VAL   A N   
3153 C  CA  . VAL   A 151 ? 0.1577 0.1516 0.1929 -0.0181 0.0061  0.0403  151 VAL   A CA  
3154 C  C   . VAL   A 151 ? 0.1497 0.1449 0.1897 -0.0276 0.0057  0.0426  151 VAL   A C   
3155 O  O   . VAL   A 151 ? 0.1591 0.1469 0.2345 -0.0206 0.0131  0.0430  151 VAL   A O   
3156 C  CB  . VAL   A 151 ? 0.1839 0.1760 0.1982 -0.0068 0.0081  0.0396  151 VAL   A CB  
3157 C  CG1 . VAL   A 151 ? 0.1797 0.1986 0.2245 -0.0131 0.0072  0.0375  151 VAL   A CG1 
3158 C  CG2 . VAL   A 151 ? 0.1988 0.1686 0.1818 -0.0013 0.0179  0.0363  151 VAL   A CG2 
3168 N  N   . TYR   A 152 ? 0.1423 0.1501 0.1957 -0.0227 0.0019  0.0452  152 TYR   A N   
3169 C  CA  . TYR   A 152 ? 0.1449 0.1566 0.1840 -0.0222 0.0070  0.0389  152 TYR   A CA  
3170 C  C   . TYR   A 152 ? 0.1420 0.1527 0.1749 -0.0169 0.0179  0.0399  152 TYR   A C   
3171 O  O   . TYR   A 152 ? 0.1563 0.1458 0.1817 -0.0218 0.0212  0.0343  152 TYR   A O   
3172 C  CB  . TYR   A 152 ? 0.1640 0.1677 0.1969 -0.0188 0.0169  0.0465  152 TYR   A CB  
3173 C  CG  . TYR   A 152 ? 0.1787 0.1940 0.1938 -0.0240 0.0272  0.0468  152 TYR   A CG  
3174 C  CD1 . TYR   A 152 ? 0.1905 0.2168 0.2222 -0.0111 0.0360  0.0574  152 TYR   A CD1 
3175 C  CD2 . TYR   A 152 ? 0.1880 0.2044 0.1828 -0.0383 0.0220  0.0423  152 TYR   A CD2 
3176 C  CE1 . TYR   A 152 ? 0.2280 0.2299 0.2265 -0.0047 0.0241  0.0646  152 TYR   A CE1 
3177 C  CE2 . TYR   A 152 ? 0.2212 0.2200 0.2060 -0.0364 0.0205  0.0475  152 TYR   A CE2 
3178 C  CZ  . TYR   A 152 ? 0.2492 0.2232 0.2118 -0.0218 0.0236  0.0769  152 TYR   A CZ  
3179 O  OH  . TYR   A 152 ? 0.2871 0.2420 0.2586 -0.0193 0.0223  0.0971  152 TYR   A OH  
3189 N  N   A LEU   A 153 ? 0.1350 0.1524 0.1881 -0.0193 0.0260  0.0460  153 LEU   A N   
3190 N  N   B LEU   A 153 ? 0.1391 0.1625 0.1630 -0.0107 0.0182  0.0362  153 LEU   A N   
3191 C  CA  A LEU   A 153 ? 0.1307 0.1507 0.2068 -0.0113 0.0235  0.0394  153 LEU   A CA  
3192 C  CA  B LEU   A 153 ? 0.1367 0.1699 0.1568 0.0022  0.0177  0.0318  153 LEU   A CA  
3193 C  C   A LEU   A 153 ? 0.1377 0.1476 0.2162 -0.0099 0.0283  0.0309  153 LEU   A C   
3194 C  C   B LEU   A 153 ? 0.1400 0.1744 0.1618 0.0098  0.0147  0.0331  153 LEU   A C   
3195 O  O   A LEU   A 153 ? 0.1485 0.1519 0.2154 -0.0184 0.0443  0.0093  153 LEU   A O   
3196 O  O   B LEU   A 153 ? 0.1429 0.1813 0.1665 0.0137  0.0160  0.0312  153 LEU   A O   
3197 C  CB  A LEU   A 153 ? 0.1241 0.1362 0.2152 -0.0133 0.0097  0.0343  153 LEU   A CB  
3198 C  CB  B LEU   A 153 ? 0.1367 0.1685 0.1639 0.0075  0.0060  0.0289  153 LEU   A CB  
3199 C  CG  A LEU   A 153 ? 0.1338 0.1379 0.2063 -0.0117 0.0253  0.0253  153 LEU   A CG  
3200 C  CG  B LEU   A 153 ? 0.1466 0.1691 0.1561 0.0079  0.0079  0.0285  153 LEU   A CG  
3201 C  CD1 A LEU   A 153 ? 0.1504 0.1353 0.2118 -0.0103 0.0113  0.0241  153 LEU   A CD1 
3202 C  CD1 B LEU   A 153 ? 0.1511 0.1682 0.1556 0.0101  0.0107  0.0257  153 LEU   A CD1 
3203 C  CD2 A LEU   A 153 ? 0.1478 0.1436 0.2065 -0.0140 0.0352  0.0035  153 LEU   A CD2 
3204 C  CD2 B LEU   A 153 ? 0.1572 0.1737 0.1698 0.0057  0.0048  0.0223  153 LEU   A CD2 
3227 N  N   A ALA   A 154 ? 0.1353 0.1371 0.2161 -0.0090 0.0310  0.0428  154 ALA   A N   
3228 N  N   B ALA   A 154 ? 0.1433 0.1710 0.1580 0.0094  0.0244  0.0332  154 ALA   A N   
3229 C  CA  A ALA   A 154 ? 0.1446 0.1417 0.2162 -0.0088 0.0310  0.0295  154 ALA   A CA  
3230 C  CA  B ALA   A 154 ? 0.1548 0.1703 0.1715 0.0082  0.0171  0.0261  154 ALA   A CA  
3231 C  C   A ALA   A 154 ? 0.1447 0.1410 0.2245 0.0006  0.0317  0.0390  154 ALA   A C   
3232 C  C   B ALA   A 154 ? 0.1596 0.1692 0.1733 0.0066  0.0130  0.0254  154 ALA   A C   
3233 O  O   A ALA   A 154 ? 0.1498 0.1474 0.2142 -0.0015 0.0360  0.0286  154 ALA   A O   
3234 O  O   B ALA   A 154 ? 0.1630 0.1660 0.1617 0.0031  0.0075  0.0250  154 ALA   A O   
3235 C  CB  A ALA   A 154 ? 0.1604 0.1499 0.2143 -0.0003 0.0270  0.0121  154 ALA   A CB  
3236 C  CB  B ALA   A 154 ? 0.1627 0.1738 0.1855 0.0074  0.0067  0.0230  154 ALA   A CB  
3247 N  N   A VAL   A 155 ? 0.1524 0.1463 0.2382 0.0057  0.0211  0.0513  155 VAL   A N   
3248 N  N   B VAL   A 155 ? 0.1648 0.1709 0.1921 0.0059  0.0103  0.0250  155 VAL   A N   
3249 C  CA  A VAL   A 155 ? 0.1592 0.1547 0.2665 0.0079  0.0154  0.0597  155 VAL   A CA  
3250 C  CA  B VAL   A 155 ? 0.1670 0.1704 0.2037 0.0003  0.0137  0.0305  155 VAL   A CA  
3251 C  C   A VAL   A 155 ? 0.1694 0.1541 0.3068 0.0149  -0.0005 0.0557  155 VAL   A C   
3252 C  C   B VAL   A 155 ? 0.1717 0.1745 0.2178 0.0023  0.0120  0.0338  155 VAL   A C   
3253 O  O   A VAL   A 155 ? 0.1564 0.1493 0.3271 0.0157  0.0087  0.0353  155 VAL   A O   
3254 O  O   B VAL   A 155 ? 0.1630 0.1791 0.2123 0.0023  0.0104  0.0323  155 VAL   A O   
3255 C  CB  A VAL   A 155 ? 0.1553 0.1663 0.2519 0.0101  0.0115  0.0495  155 VAL   A CB  
3256 C  CB  B VAL   A 155 ? 0.1642 0.1715 0.2023 -0.0038 0.0125  0.0193  155 VAL   A CB  
3257 C  CG1 A VAL   A 155 ? 0.1676 0.1864 0.2591 0.0102  0.0003  0.0542  155 VAL   A CG1 
3258 C  CG1 B VAL   A 155 ? 0.1690 0.1804 0.2090 -0.0022 0.0077  0.0189  155 VAL   A CG1 
3259 C  CG2 A VAL   A 155 ? 0.1602 0.1734 0.2515 0.0189  0.0080  0.0472  155 VAL   A CG2 
3260 C  CG2 B VAL   A 155 ? 0.1666 0.1722 0.1993 -0.0027 0.0154  0.0161  155 VAL   A CG2 
3279 N  N   A PHE   A 156 ? 0.1870 0.1626 0.3218 0.0114  -0.0048 0.0724  156 PHE   A N   
3280 N  N   B PHE   A 156 ? 0.1833 0.1755 0.2283 -0.0011 0.0163  0.0397  156 PHE   A N   
3281 C  CA  A PHE   A 156 ? 0.2126 0.1716 0.3497 0.0240  -0.0012 0.0668  156 PHE   A CA  
3282 C  CA  B PHE   A 156 ? 0.1998 0.1807 0.2393 0.0017  0.0149  0.0411  156 PHE   A CA  
3283 C  C   A PHE   A 156 ? 0.2114 0.1710 0.3553 0.0421  0.0120  0.0791  156 PHE   A C   
3284 C  C   B PHE   A 156 ? 0.2197 0.1966 0.2627 0.0073  0.0128  0.0416  156 PHE   A C   
3285 O  O   A PHE   A 156 ? 0.2172 0.1879 0.3651 0.0416  0.0265  0.0815  156 PHE   A O   
3286 O  O   B PHE   A 156 ? 0.2271 0.2058 0.2729 0.0095  0.0182  0.0393  156 PHE   A O   
3287 C  CB  A PHE   A 156 ? 0.2472 0.1826 0.3611 0.0196  -0.0113 0.0783  156 PHE   A CB  
3288 C  CB  B PHE   A 156 ? 0.1961 0.1732 0.2320 0.0048  0.0156  0.0430  156 PHE   A CB  
3289 C  CG  A PHE   A 156 ? 0.2788 0.1921 0.3801 0.0278  -0.0189 0.0739  156 PHE   A CG  
3290 C  CG  B PHE   A 156 ? 0.1934 0.1749 0.2319 0.0101  0.0157  0.0402  156 PHE   A CG  
3291 C  CD1 A PHE   A 156 ? 0.2925 0.1989 0.3922 0.0356  -0.0202 0.0649  156 PHE   A CD1 
3292 C  CD1 B PHE   A 156 ? 0.1901 0.1772 0.2399 0.0151  0.0098  0.0276  156 PHE   A CD1 
3293 C  CD2 A PHE   A 156 ? 0.2959 0.2056 0.3986 0.0423  -0.0245 0.0759  156 PHE   A CD2 
3294 C  CD2 B PHE   A 156 ? 0.1989 0.1813 0.2427 0.0104  0.0131  0.0369  156 PHE   A CD2 
3295 C  CE1 A PHE   A 156 ? 0.3043 0.2051 0.4090 0.0440  -0.0201 0.0562  156 PHE   A CE1 
3296 C  CE1 B PHE   A 156 ? 0.1909 0.1815 0.2480 0.0065  0.0079  0.0135  156 PHE   A CE1 
3297 C  CE2 A PHE   A 156 ? 0.3110 0.2168 0.4121 0.0496  -0.0230 0.0598  156 PHE   A CE2 
3298 C  CE2 B PHE   A 156 ? 0.2045 0.1849 0.2527 0.0043  0.0104  0.0295  156 PHE   A CE2 
3299 C  CZ  A PHE   A 156 ? 0.3127 0.2136 0.4171 0.0513  -0.0212 0.0480  156 PHE   A CZ  
3300 C  CZ  B PHE   A 156 ? 0.1968 0.1784 0.2517 -0.0043 0.0108  0.0170  156 PHE   A CZ  
3319 N  N   A ASP   A 157 ? 0.2046 0.1668 0.3409 0.0405  0.0053  0.0907  157 ASP   A N   
3320 N  N   B ASP   A 157 ? 0.2315 0.2095 0.2793 0.0041  -0.0007 0.0480  157 ASP   A N   
3321 C  CA  A ASP   A 157 ? 0.2095 0.1837 0.3521 0.0345  0.0078  0.0959  157 ASP   A CA  
3322 C  CA  B ASP   A 157 ? 0.2450 0.2214 0.2853 0.0110  -0.0120 0.0509  157 ASP   A CA  
3323 C  C   A ASP   A 157 ? 0.1858 0.2014 0.3533 0.0448  0.0327  0.1058  157 ASP   A C   
3324 C  C   B ASP   A 157 ? 0.2406 0.2349 0.2818 0.0173  -0.0089 0.0537  157 ASP   A C   
3325 O  O   A ASP   A 157 ? 0.1711 0.1925 0.3442 0.0364  0.0392  0.1141  157 ASP   A O   
3326 O  O   B ASP   A 157 ? 0.2360 0.2332 0.2809 0.0184  -0.0100 0.0462  157 ASP   A O   
3327 C  CB  A ASP   A 157 ? 0.2253 0.1953 0.3778 0.0292  -0.0165 0.0920  157 ASP   A CB  
3328 C  CB  B ASP   A 157 ? 0.2591 0.2238 0.2971 0.0183  -0.0240 0.0542  157 ASP   A CB  
3329 C  CG  A ASP   A 157 ? 0.2482 0.2107 0.4210 0.0268  -0.0383 0.0947  157 ASP   A CG  
3330 C  CG  B ASP   A 157 ? 0.2757 0.2262 0.3234 0.0289  -0.0377 0.0575  157 ASP   A CG  
3331 O  OD1 A ASP   A 157 ? 0.2762 0.2266 0.4624 0.0054  -0.0669 0.0809  157 ASP   A OD1 
3332 O  OD1 B ASP   A 157 ? 0.2924 0.2271 0.3453 0.0254  -0.0534 0.0570  157 ASP   A OD1 
3333 O  OD2 A ASP   A 157 ? 0.2340 0.2032 0.4239 0.0282  -0.0281 0.1130  157 ASP   A OD2 
3334 O  OD2 B ASP   A 157 ? 0.2709 0.2263 0.3253 0.0363  -0.0343 0.0613  157 ASP   A OD2 
3343 N  N   A LYS   A 158 ? 0.1935 0.2281 0.3709 0.0537  0.0421  0.0997  158 LYS   A N   
3344 N  N   B LYS   A 158 ? 0.2436 0.2508 0.2822 0.0198  -0.0091 0.0576  158 LYS   A N   
3345 C  CA  A LYS   A 158 ? 0.1909 0.2571 0.3829 0.0631  0.0567  0.0905  158 LYS   A CA  
3346 C  CA  B LYS   A 158 ? 0.2450 0.2695 0.2944 0.0218  -0.0074 0.0542  158 LYS   A CA  
3347 C  C   A LYS   A 158 ? 0.1757 0.2673 0.3778 0.0620  0.0439  0.1112  158 LYS   A C   
3348 C  C   B LYS   A 158 ? 0.2318 0.2725 0.2900 0.0214  -0.0080 0.0708  158 LYS   A C   
3349 O  O   A LYS   A 158 ? 0.1740 0.2670 0.3908 0.0524  0.0478  0.1071  158 LYS   A O   
3350 O  O   B LYS   A 158 ? 0.2253 0.2705 0.2875 0.0197  -0.0208 0.0806  158 LYS   A O   
3351 C  CB  A LYS   A 158 ? 0.2161 0.2727 0.3897 0.0638  0.0830  0.0812  158 LYS   A CB  
3352 C  CB  B LYS   A 158 ? 0.2600 0.2852 0.3131 0.0185  -0.0061 0.0311  158 LYS   A CB  
3353 C  CG  A LYS   A 158 ? 0.2428 0.2926 0.3978 0.0587  0.0948  0.0782  158 LYS   A CG  
3354 C  CG  B LYS   A 158 ? 0.2746 0.2983 0.3368 0.0150  -0.0103 0.0140  158 LYS   A CG  
3355 C  CD  A LYS   A 158 ? 0.2594 0.3107 0.4043 0.0488  0.1193  0.0856  158 LYS   A CD  
3356 C  CD  B LYS   A 158 ? 0.2847 0.3085 0.3574 0.0092  -0.0142 0.0029  158 LYS   A CD  
3357 C  CE  A LYS   A 158 ? 0.2721 0.3198 0.4036 0.0413  0.1395  0.0988  158 LYS   A CE  
3358 C  CE  B LYS   A 158 ? 0.2915 0.3157 0.3739 0.0048  -0.0198 -0.0010 158 LYS   A CE  
3359 N  NZ  A LYS   A 158 ? 0.2807 0.3222 0.3975 0.0386  0.1424  0.1124  158 LYS   A NZ  
3360 N  NZ  B LYS   A 158 ? 0.2945 0.3194 0.3888 0.0034  -0.0227 0.0015  158 LYS   A NZ  
3387 N  N   A ASN   A 159 ? 0.1711 0.2817 0.3927 0.0625  0.0276  0.1199  159 ASN   A N   
3388 N  N   B ASN   A 159 ? 0.2290 0.2774 0.3001 0.0202  0.0058  0.0718  159 ASN   A N   
3389 C  CA  A ASN   A 159 ? 0.1710 0.2931 0.4013 0.0629  0.0079  0.1337  159 ASN   A CA  
3390 C  CA  B ASN   A 159 ? 0.2267 0.2808 0.3079 0.0152  0.0129  0.0749  159 ASN   A CA  
3391 C  C   A ASN   A 159 ? 0.1590 0.2874 0.3633 0.0480  0.0113  0.1224  159 ASN   A C   
3392 C  C   B ASN   A 159 ? 0.2071 0.2663 0.2759 0.0019  0.0102  0.0697  159 ASN   A C   
3393 O  O   A ASN   A 159 ? 0.1417 0.2981 0.3504 0.0463  -0.0042 0.1040  159 ASN   A O   
3394 O  O   B ASN   A 159 ? 0.2050 0.2753 0.2780 0.0003  0.0017  0.0647  159 ASN   A O   
3395 C  CB  A ASN   A 159 ? 0.1972 0.3092 0.4587 0.0707  -0.0038 0.1558  159 ASN   A CB  
3396 C  CB  B ASN   A 159 ? 0.2464 0.2973 0.3569 0.0193  0.0187  0.0808  159 ASN   A CB  
3397 C  CG  A ASN   A 159 ? 0.2307 0.3370 0.5390 0.0583  0.0019  0.1371  159 ASN   A CG  
3398 C  CG  B ASN   A 159 ? 0.2664 0.3131 0.4107 0.0167  0.0237  0.0735  159 ASN   A CG  
3399 O  OD1 A ASN   A 159 ? 0.2437 0.3518 0.5716 0.0513  0.0134  0.1263  159 ASN   A OD1 
3400 O  OD1 B ASN   A 159 ? 0.2719 0.3205 0.4313 0.0160  0.0309  0.0682  159 ASN   A OD1 
3401 N  ND2 A ASN   A 159 ? 0.2430 0.3499 0.5786 0.0532  0.0009  0.1246  159 ASN   A ND2 
3402 N  ND2 B ASN   A 159 ? 0.2758 0.3205 0.4351 0.0135  0.0220  0.0688  159 ASN   A ND2 
3415 N  N   A LEU   A 160 ? 0.1509 0.2655 0.3375 0.0388  -0.0024 0.1197  160 LEU   A N   
3416 N  N   B LEU   A 160 ? 0.1896 0.2429 0.2495 -0.0091 0.0033  0.0726  160 LEU   A N   
3417 C  CA  A LEU   A 160 ? 0.1555 0.2480 0.3134 0.0231  0.0071  0.1105  160 LEU   A CA  
3418 C  CA  B LEU   A 160 ? 0.1815 0.2257 0.2322 -0.0138 0.0033  0.0701  160 LEU   A CA  
3419 C  C   A LEU   A 160 ? 0.1415 0.2399 0.2866 0.0159  0.0172  0.0992  160 LEU   A C   
3420 C  C   B LEU   A 160 ? 0.1753 0.2182 0.2268 -0.0115 0.0029  0.0634  160 LEU   A C   
3421 O  O   A LEU   A 160 ? 0.1456 0.2492 0.3133 0.0099  0.0134  0.0914  160 LEU   A O   
3422 O  O   B LEU   A 160 ? 0.1764 0.2143 0.2384 -0.0116 0.0009  0.0515  160 LEU   A O   
3423 C  CB  A LEU   A 160 ? 0.1689 0.2456 0.3004 0.0170  0.0138  0.1078  160 LEU   A CB  
3424 C  CB  B LEU   A 160 ? 0.1789 0.2201 0.2225 -0.0139 0.0033  0.0751  160 LEU   A CB  
3425 C  CG  A LEU   A 160 ? 0.1822 0.2481 0.3025 0.0014  0.0215  0.0919  160 LEU   A CG  
3426 C  CG  B LEU   A 160 ? 0.1839 0.2222 0.2194 -0.0144 0.0073  0.0747  160 LEU   A CG  
3427 C  CD1 A LEU   A 160 ? 0.1947 0.2587 0.2956 -0.0076 0.0285  0.0778  160 LEU   A CD1 
3428 C  CD1 B LEU   A 160 ? 0.1859 0.2240 0.2179 -0.0164 0.0078  0.0690  160 LEU   A CD1 
3429 C  CD2 A LEU   A 160 ? 0.1916 0.2473 0.3070 -0.0043 0.0279  0.0804  160 LEU   A CD2 
3430 C  CD2 B LEU   A 160 ? 0.1866 0.2260 0.2218 -0.0122 0.0153  0.0701  160 LEU   A CD2 
3453 N  N   A TYR   A 161 ? 0.1431 0.2236 0.2760 0.0187  0.0162  0.0935  161 TYR   A N   
3454 N  N   B TYR   A 161 ? 0.1724 0.2171 0.2167 -0.0090 0.0103  0.0720  161 TYR   A N   
3455 C  CA  A TYR   A 161 ? 0.1410 0.2197 0.2823 0.0213  0.0122  0.0777  161 TYR   A CA  
3456 C  CA  B TYR   A 161 ? 0.1705 0.2195 0.2166 -0.0051 0.0108  0.0729  161 TYR   A CA  
3457 C  C   A TYR   A 161 ? 0.1352 0.2274 0.2985 0.0181  0.0223  0.0790  161 TYR   A C   
3458 C  C   B TYR   A 161 ? 0.1689 0.2271 0.2224 -0.0053 0.0070  0.0716  161 TYR   A C   
3459 O  O   A TYR   A 161 ? 0.1321 0.2253 0.2998 0.0064  0.0218  0.0728  161 TYR   A O   
3460 O  O   B TYR   A 161 ? 0.1618 0.2226 0.2022 -0.0107 -0.0005 0.0733  161 TYR   A O   
3461 C  CB  A TYR   A 161 ? 0.1594 0.2115 0.2898 0.0149  0.0093  0.0636  161 TYR   A CB  
3462 C  CB  B TYR   A 161 ? 0.1733 0.2150 0.2177 0.0009  0.0198  0.0757  161 TYR   A CB  
3463 C  CG  A TYR   A 161 ? 0.1604 0.1995 0.2914 0.0135  0.0124  0.0485  161 TYR   A CG  
3464 C  CG  B TYR   A 161 ? 0.1705 0.2094 0.2264 0.0079  0.0236  0.0741  161 TYR   A CG  
3465 C  CD1 A TYR   A 161 ? 0.1600 0.1911 0.2926 0.0008  0.0120  0.0478  161 TYR   A CD1 
3466 C  CD1 B TYR   A 161 ? 0.1705 0.2068 0.2333 0.0077  0.0179  0.0753  161 TYR   A CD1 
3467 C  CD2 A TYR   A 161 ? 0.1623 0.2014 0.2939 0.0170  0.0090  0.0378  161 TYR   A CD2 
3468 C  CD2 B TYR   A 161 ? 0.1690 0.2069 0.2345 0.0082  0.0273  0.0767  161 TYR   A CD2 
3469 C  CE1 A TYR   A 161 ? 0.1731 0.1867 0.3043 -0.0016 0.0162  0.0519  161 TYR   A CE1 
3470 C  CE1 B TYR   A 161 ? 0.1730 0.2099 0.2404 0.0092  0.0206  0.0785  161 TYR   A CE1 
3471 C  CE2 A TYR   A 161 ? 0.1745 0.1913 0.2924 0.0102  0.0111  0.0468  161 TYR   A CE2 
3472 C  CE2 B TYR   A 161 ? 0.1712 0.2068 0.2395 0.0026  0.0292  0.0817  161 TYR   A CE2 
3473 C  CZ  A TYR   A 161 ? 0.1907 0.1824 0.3025 -0.0014 0.0116  0.0606  161 TYR   A CZ  
3474 C  CZ  B TYR   A 161 ? 0.1809 0.2084 0.2489 0.0037  0.0264  0.0841  161 TYR   A CZ  
3475 O  OH  A TYR   A 161 ? 0.2183 0.1760 0.3214 -0.0120 0.0011  0.0775  161 TYR   A OH  
3476 O  OH  B TYR   A 161 ? 0.1931 0.2102 0.2710 -0.0025 0.0309  0.0866  161 TYR   A OH  
3495 N  N   A ASP   A 162 ? 0.1345 0.2349 0.3227 0.0219  0.0232  0.0892  162 ASP   A N   
3496 N  N   B ASP   A 162 ? 0.1741 0.2372 0.2527 0.0011  0.0092  0.0710  162 ASP   A N   
3497 C  CA  A ASP   A 162 ? 0.1328 0.2585 0.3276 0.0211  0.0348  0.0839  162 ASP   A CA  
3498 C  CA  B ASP   A 162 ? 0.1770 0.2550 0.2696 0.0056  0.0121  0.0630  162 ASP   A CA  
3499 C  C   A ASP   A 162 ? 0.1220 0.2705 0.3188 0.0103  0.0352  0.0877  162 ASP   A C   
3500 C  C   B ASP   A 162 ? 0.1749 0.2665 0.2700 0.0043  0.0124  0.0683  162 ASP   A C   
3501 O  O   A ASP   A 162 ? 0.1333 0.2667 0.3359 0.0032  0.0279  0.0833  162 ASP   A O   
3502 O  O   B ASP   A 162 ? 0.1769 0.2641 0.2724 0.0029  0.0086  0.0707  162 ASP   A O   
3503 C  CB  A ASP   A 162 ? 0.1514 0.2750 0.3473 0.0239  0.0432  0.0762  162 ASP   A CB  
3504 C  CB  B ASP   A 162 ? 0.1842 0.2632 0.2931 0.0106  0.0119  0.0488  162 ASP   A CB  
3505 C  CG  A ASP   A 162 ? 0.1726 0.2986 0.3765 0.0330  0.0528  0.0610  162 ASP   A CG  
3506 C  CG  B ASP   A 162 ? 0.1933 0.2731 0.3139 0.0194  0.0080  0.0385  162 ASP   A CG  
3507 O  OD1 A ASP   A 162 ? 0.1838 0.3095 0.3821 0.0232  0.0528  0.0606  162 ASP   A OD1 
3508 O  OD1 B ASP   A 162 ? 0.1950 0.2763 0.3199 0.0188  0.0072  0.0414  162 ASP   A OD1 
3509 O  OD2 A ASP   A 162 ? 0.1956 0.3086 0.4029 0.0467  0.0568  0.0466  162 ASP   A OD2 
3510 O  OD2 B ASP   A 162 ? 0.2035 0.2775 0.3255 0.0277  0.0051  0.0287  162 ASP   A OD2 
3519 N  N   A LYS   A 163 ? 0.1322 0.2886 0.3274 0.0025  0.0059  0.0872  163 LYS   A N   
3520 N  N   B LYS   A 163 ? 0.1779 0.2814 0.2849 0.0016  0.0075  0.0676  163 LYS   A N   
3521 C  CA  A LYS   A 163 ? 0.1461 0.3056 0.3114 -0.0062 -0.0015 0.0832  163 LYS   A CA  
3522 C  CA  B LYS   A 163 ? 0.1801 0.2932 0.2908 -0.0019 0.0104  0.0668  163 LYS   A CA  
3523 C  C   A LYS   A 163 ? 0.1462 0.2895 0.3091 -0.0142 0.0181  0.0756  163 LYS   A C   
3524 C  C   B LYS   A 163 ? 0.1610 0.2824 0.2851 -0.0104 0.0180  0.0709  163 LYS   A C   
3525 O  O   A LYS   A 163 ? 0.1497 0.3025 0.3304 -0.0168 0.0197  0.0678  163 LYS   A O   
3526 O  O   B LYS   A 163 ? 0.1606 0.2926 0.2890 -0.0131 0.0176  0.0679  163 LYS   A O   
3527 C  CB  A LYS   A 163 ? 0.1840 0.3404 0.3489 -0.0001 -0.0172 0.0832  163 LYS   A CB  
3528 C  CB  B LYS   A 163 ? 0.2108 0.3151 0.3242 0.0052  0.0060  0.0611  163 LYS   A CB  
3529 C  CG  A LYS   A 163 ? 0.2210 0.3720 0.3857 0.0007  -0.0173 0.0854  163 LYS   A CG  
3530 C  CG  B LYS   A 163 ? 0.2388 0.3337 0.3603 0.0057  0.0079  0.0565  163 LYS   A CG  
3531 C  CD  A LYS   A 163 ? 0.2638 0.3977 0.4398 0.0033  -0.0187 0.0785  163 LYS   A CD  
3532 C  CD  B LYS   A 163 ? 0.2652 0.3481 0.4017 0.0076  0.0076  0.0493  163 LYS   A CD  
3533 C  CE  A LYS   A 163 ? 0.3009 0.4139 0.4811 0.0027  -0.0121 0.0756  163 LYS   A CE  
3534 C  CE  B LYS   A 163 ? 0.2879 0.3571 0.4327 0.0083  0.0113  0.0468  163 LYS   A CE  
3535 N  NZ  A LYS   A 163 ? 0.3096 0.4206 0.5019 0.0012  -0.0036 0.0793  163 LYS   A NZ  
3536 N  NZ  B LYS   A 163 ? 0.2948 0.3614 0.4522 0.0092  0.0125  0.0435  163 LYS   A NZ  
3563 N  N   . LEU   A 164 ? 0.1403 0.2599 0.2879 -0.0182 0.0081  0.0734  164 LEU   A N   
3564 C  CA  . LEU   A 164 ? 0.1466 0.2316 0.2775 -0.0236 0.0184  0.0623  164 LEU   A CA  
3565 C  C   . LEU   A 164 ? 0.1565 0.2309 0.2835 -0.0159 0.0232  0.0573  164 LEU   A C   
3566 O  O   . LEU   A 164 ? 0.1678 0.2385 0.2958 -0.0226 0.0535  0.0384  164 LEU   A O   
3567 C  CB  . LEU   A 164 ? 0.1456 0.2227 0.2771 -0.0218 0.0225  0.0628  164 LEU   A CB  
3568 C  CG  . LEU   A 164 ? 0.1497 0.2168 0.2869 -0.0126 0.0168  0.0501  164 LEU   A CG  
3569 C  CD1 . LEU   A 164 ? 0.1467 0.2157 0.2747 -0.0010 0.0104  0.0529  164 LEU   A CD1 
3570 C  CD2 . LEU   A 164 ? 0.1617 0.2201 0.2944 -0.0181 0.0320  0.0406  164 LEU   A CD2 
3583 N  N   . VAL   A 165 ? 0.1519 0.2266 0.2802 -0.0118 0.0219  0.0663  165 VAL   A N   
3584 C  CA  . VAL   A 165 ? 0.1633 0.2264 0.2738 -0.0196 0.0267  0.0736  165 VAL   A CA  
3585 C  C   . VAL   A 165 ? 0.1506 0.2382 0.2815 -0.0159 0.0319  0.0693  165 VAL   A C   
3586 O  O   . VAL   A 165 ? 0.1540 0.2415 0.2756 -0.0219 0.0346  0.0679  165 VAL   A O   
3587 C  CB  . VAL   A 165 ? 0.1887 0.2330 0.2837 -0.0170 0.0333  0.0665  165 VAL   A CB  
3588 C  CG1 . VAL   A 165 ? 0.1926 0.2420 0.2981 -0.0151 0.0390  0.0531  165 VAL   A CG1 
3589 C  CG2 . VAL   A 165 ? 0.2069 0.2372 0.2884 -0.0152 0.0254  0.0734  165 VAL   A CG2 
3599 N  N   . SER   A 166 ? 0.1423 0.2564 0.3101 -0.0104 0.0417  0.0710  166 SER   A N   
3600 C  CA  . SER   A 166 ? 0.1485 0.2836 0.3375 -0.0119 0.0348  0.0617  166 SER   A CA  
3601 C  C   . SER   A 166 ? 0.1554 0.3096 0.3444 -0.0259 0.0221  0.0469  166 SER   A C   
3602 O  O   . SER   A 166 ? 0.1758 0.3212 0.3931 -0.0428 0.0410  0.0078  166 SER   A O   
3603 C  CB  . SER   A 166 ? 0.1661 0.2973 0.3708 0.0087  0.0223  0.0553  166 SER   A CB  
3604 O  OG  . SER   A 166 ? 0.2190 0.3117 0.4045 0.0074  0.0236  0.0783  166 SER   A OG  
3610 N  N   . SER   A 167 ? 0.1558 0.3187 0.2951 -0.0141 0.0029  0.0572  167 SER   A N   
3611 C  CA  . SER   A 167 ? 0.1831 0.3337 0.2846 -0.0017 -0.0135 0.0351  167 SER   A CA  
3612 C  C   . SER   A 167 ? 0.1859 0.3321 0.2919 0.0079  0.0029  0.0296  167 SER   A C   
3613 O  O   . SER   A 167 ? 0.2064 0.3382 0.3095 0.0100  -0.0015 0.0259  167 SER   A O   
3614 C  CB  . SER   A 167 ? 0.1966 0.3515 0.2898 0.0034  -0.0065 0.0225  167 SER   A CB  
3615 O  OG  . SER   A 167 ? 0.1965 0.3604 0.2856 0.0040  0.0212  0.0251  167 SER   A OG  
3621 N  N   . PHE   A 168 ? 0.1740 0.3300 0.2847 0.0199  -0.0018 0.0211  168 PHE   A N   
3622 C  CA  . PHE   A 168 ? 0.1996 0.3353 0.3085 0.0102  0.0088  0.0080  168 PHE   A CA  
3623 C  C   . PHE   A 168 ? 0.2863 0.3929 0.3907 -0.0148 0.0284  -0.0085 168 PHE   A C   
3624 O  O   . PHE   A 168 ? 0.2698 0.3908 0.3961 -0.0340 0.0574  0.0018  168 PHE   A O   
3625 C  CB  . PHE   A 168 ? 0.1823 0.2935 0.2909 0.0024  0.0002  0.0155  168 PHE   A CB  
3626 C  CG  . PHE   A 168 ? 0.1739 0.2651 0.2815 -0.0060 -0.0064 0.0256  168 PHE   A CG  
3627 C  CD1 . PHE   A 168 ? 0.1710 0.2673 0.2873 -0.0135 -0.0086 0.0483  168 PHE   A CD1 
3628 C  CD2 . PHE   A 168 ? 0.1775 0.2524 0.2761 -0.0019 0.0008  0.0288  168 PHE   A CD2 
3629 C  CE1 . PHE   A 168 ? 0.1608 0.2681 0.2845 -0.0158 -0.0143 0.0565  168 PHE   A CE1 
3630 C  CE2 . PHE   A 168 ? 0.1843 0.2497 0.2719 -0.0046 0.0082  0.0430  168 PHE   A CE2 
3631 C  CZ  . PHE   A 168 ? 0.1755 0.2595 0.2677 -0.0132 -0.0024 0.0550  168 PHE   A CZ  
3641 N  N   A LEU   A 169 ? 0.3574 0.4270 0.4546 -0.0250 0.0114  -0.0250 169 LEU   A N   
3642 N  N   B LEU   A 169 ? 0.3403 0.4224 0.4427 -0.0188 0.0157  -0.0131 169 LEU   A N   
3643 C  CA  A LEU   A 169 ? 0.4398 0.4676 0.5360 -0.0297 -0.0133 -0.0320 169 LEU   A CA  
3644 C  CA  B LEU   A 169 ? 0.3975 0.4532 0.5024 -0.0202 0.0008  -0.0133 169 LEU   A CA  
3645 C  C   A LEU   A 169 ? 0.4751 0.4805 0.5852 -0.0344 -0.0213 -0.0257 169 LEU   A C   
3646 C  C   B LEU   A 169 ? 0.4160 0.4630 0.5313 -0.0224 -0.0037 -0.0056 169 LEU   A C   
3647 O  O   A LEU   A 169 ? 0.4864 0.4846 0.6005 -0.0360 -0.0218 -0.0237 169 LEU   A O   
3648 O  O   B LEU   A 169 ? 0.4224 0.4671 0.5389 -0.0235 -0.0041 -0.0026 169 LEU   A O   
3649 C  CB  A LEU   A 169 ? 0.4753 0.4897 0.5495 -0.0323 -0.0253 -0.0440 169 LEU   A CB  
3650 C  CB  B LEU   A 169 ? 0.4282 0.4704 0.5205 -0.0214 -0.0062 -0.0208 169 LEU   A CB  
3651 C  CG  A LEU   A 169 ? 0.5029 0.5074 0.5631 -0.0368 -0.0328 -0.0594 169 LEU   A CG  
3652 C  CG  B LEU   A 169 ? 0.4515 0.4840 0.5360 -0.0235 -0.0110 -0.0300 169 LEU   A CG  
3653 C  CD1 A LEU   A 169 ? 0.5106 0.5138 0.5706 -0.0389 -0.0359 -0.0640 169 LEU   A CD1 
3654 C  CD1 B LEU   A 169 ? 0.4587 0.4891 0.5431 -0.0243 -0.0130 -0.0329 169 LEU   A CD1 
3655 C  CD2 A LEU   A 169 ? 0.5125 0.5136 0.5653 -0.0380 -0.0329 -0.0657 169 LEU   A CD2 
3656 C  CD2 B LEU   A 169 ? 0.4597 0.4885 0.5406 -0.0241 -0.0112 -0.0336 169 LEU   A CD2 
3657 O  OXT A LEU   A 169 ? 0.4761 0.4825 0.5985 -0.0375 -0.0206 -0.0247 169 LEU   A OXT 
3658 O  OXT B LEU   A 169 ? 0.4164 0.4641 0.5356 -0.0241 -0.0017 -0.0032 169 LEU   A OXT 
3681 N  N   A SER   B 1   ? 0.3915 0.3673 0.3769 -0.1149 -0.0874 0.0645  1   SER   B N   
3682 N  N   B SER   B 1   ? 0.3423 0.3165 0.3275 -0.0843 -0.0516 0.0166  1   SER   B N   
3683 C  CA  A SER   B 1   ? 0.3782 0.3690 0.3828 -0.1238 -0.0913 0.0602  1   SER   B CA  
3684 C  CA  B SER   B 1   ? 0.3362 0.3199 0.3319 -0.0882 -0.0540 0.0153  1   SER   B CA  
3685 C  C   A SER   B 1   ? 0.3440 0.3674 0.3528 -0.1258 -0.0996 0.0784  1   SER   B C   
3686 C  C   B SER   B 1   ? 0.3193 0.3242 0.3209 -0.0850 -0.0587 0.0342  1   SER   B C   
3687 O  O   A SER   B 1   ? 0.3517 0.3697 0.3097 -0.1160 -0.0953 0.0762  1   SER   B O   
3688 O  O   B SER   B 1   ? 0.3221 0.3245 0.3006 -0.0791 -0.0553 0.0322  1   SER   B O   
3689 C  CB  A SER   B 1   ? 0.3952 0.3694 0.3999 -0.1262 -0.0822 0.0423  1   SER   B CB  
3690 C  CB  B SER   B 1   ? 0.3451 0.3160 0.3372 -0.0913 -0.0472 -0.0032 1   SER   B CB  
3691 O  OG  A SER   B 1   ? 0.4119 0.3793 0.4546 -0.1250 -0.0782 0.0364  1   SER   B OG  
3692 O  OG  B SER   B 1   ? 0.3549 0.3176 0.3648 -0.0927 -0.0453 -0.0129 1   SER   B OG  
3707 N  N   A MET   B 2   ? 0.3119 0.3623 0.3538 -0.1271 -0.0994 0.1155  2   MET   B N   
3708 N  N   B MET   B 2   ? 0.3051 0.3273 0.3209 -0.0816 -0.0593 0.0644  2   MET   B N   
3709 C  CA  A MET   B 2   ? 0.2896 0.3645 0.3786 -0.1037 -0.0979 0.1296  2   MET   B CA  
3710 C  CA  B MET   B 2   ? 0.2941 0.3314 0.3264 -0.0673 -0.0579 0.0818  2   MET   B CA  
3711 C  C   A MET   B 2   ? 0.2484 0.3457 0.3505 -0.0811 -0.1049 0.1478  2   MET   B C   
3712 C  C   B MET   B 2   ? 0.2734 0.3204 0.2997 -0.0589 -0.0501 0.0876  2   MET   B C   
3713 O  O   A MET   B 2   ? 0.2331 0.3587 0.3523 -0.0647 -0.1275 0.1477  2   MET   B O   
3714 O  O   B MET   B 2   ? 0.2724 0.3260 0.3020 -0.0546 -0.0440 0.0820  2   MET   B O   
3715 C  CB  A MET   B 2   ? 0.3214 0.3978 0.4653 -0.0833 -0.0736 0.1035  2   MET   B CB  
3716 C  CB  B MET   B 2   ? 0.3096 0.3514 0.3694 -0.0536 -0.0580 0.0837  2   MET   B CB  
3717 C  CG  A MET   B 2   ? 0.3520 0.4272 0.5508 -0.0601 -0.0467 0.0869  2   MET   B CG  
3718 C  CG  B MET   B 2   ? 0.3231 0.3691 0.4051 -0.0393 -0.0554 0.0946  2   MET   B CG  
3719 S  SD  A MET   B 2   ? 0.3807 0.4554 0.6297 -0.0405 -0.0264 0.0735  2   MET   B SD  
3720 S  SD  B MET   B 2   ? 0.3364 0.3880 0.4348 -0.0258 -0.0556 0.1023  2   MET   B SD  
3721 C  CE  A MET   B 2   ? 0.3837 0.4602 0.6235 -0.0388 -0.0204 0.0764  2   MET   B CE  
3722 C  CE  B MET   B 2   ? 0.3372 0.3915 0.4377 -0.0261 -0.0533 0.0962  2   MET   B CE  
3741 N  N   A VAL   B 3   ? 0.2217 0.3074 0.3169 -0.0819 -0.0883 0.1671  3   VAL   B N   
3742 N  N   B VAL   B 3   ? 0.2529 0.3017 0.2721 -0.0571 -0.0466 0.0971  3   VAL   B N   
3743 C  CA  A VAL   B 3   ? 0.2111 0.2757 0.3090 -0.0746 -0.0828 0.1433  3   VAL   B CA  
3744 C  CA  B VAL   B 3   ? 0.2352 0.2817 0.2582 -0.0504 -0.0459 0.0915  3   VAL   B CA  
3745 C  C   A VAL   B 3   ? 0.1962 0.2590 0.2744 -0.0667 -0.0724 0.1202  3   VAL   B C   
3746 C  C   B VAL   B 3   ? 0.2118 0.2647 0.2388 -0.0457 -0.0479 0.0928  3   VAL   B C   
3747 O  O   A VAL   B 3   ? 0.1921 0.2599 0.2835 -0.0672 -0.0721 0.1225  3   VAL   B O   
3748 O  O   B VAL   B 3   ? 0.2088 0.2701 0.2323 -0.0274 -0.0475 0.0910  3   VAL   B O   
3749 C  CB  A VAL   B 3   ? 0.2311 0.2728 0.3565 -0.0793 -0.0736 0.1186  3   VAL   B CB  
3750 C  CB  B VAL   B 3   ? 0.2451 0.2789 0.2766 -0.0502 -0.0409 0.0814  3   VAL   B CB  
3751 C  CG1 A VAL   B 3   ? 0.2411 0.2658 0.3817 -0.0841 -0.0712 0.1067  3   VAL   B CG1 
3752 C  CG1 B VAL   B 3   ? 0.2494 0.2753 0.2872 -0.0524 -0.0398 0.0735  3   VAL   B CG1 
3753 C  CG2 A VAL   B 3   ? 0.2348 0.2744 0.3753 -0.0796 -0.0612 0.1296  3   VAL   B CG2 
3754 C  CG2 B VAL   B 3   ? 0.2478 0.2792 0.2808 -0.0489 -0.0380 0.0859  3   VAL   B CG2 
3773 N  N   . ASN   B 4   ? 0.1940 0.2403 0.2406 -0.0577 -0.0573 0.0907  4   ASN   B N   
3774 C  CA  . ASN   B 4   ? 0.1917 0.2371 0.1956 -0.0596 -0.0445 0.0546  4   ASN   B CA  
3775 C  C   . ASN   B 4   ? 0.1995 0.2548 0.1832 -0.0593 -0.0329 0.0359  4   ASN   B C   
3776 O  O   . ASN   B 4   ? 0.1992 0.2519 0.2026 -0.0562 -0.0280 0.0207  4   ASN   B O   
3777 C  CB  . ASN   B 4   ? 0.1910 0.2263 0.1801 -0.0520 -0.0547 0.0412  4   ASN   B CB  
3778 C  CG  . ASN   B 4   ? 0.1930 0.2063 0.1679 -0.0539 -0.0523 0.0340  4   ASN   B CG  
3779 O  OD1 . ASN   B 4   ? 0.1996 0.1889 0.1734 -0.0528 -0.0553 0.0289  4   ASN   B OD1 
3780 N  ND2 . ASN   B 4   ? 0.2140 0.2107 0.1879 -0.0313 -0.0374 0.0302  4   ASN   B ND2 
3788 N  N   . SER   B 5   ? 0.2054 0.2731 0.1839 -0.0627 -0.0312 0.0322  5   SER   B N   
3789 C  CA  . SER   B 5   ? 0.2306 0.3072 0.2125 -0.0519 -0.0118 0.0329  5   SER   B CA  
3790 C  C   . SER   B 5   ? 0.2510 0.3100 0.2532 -0.0668 0.0211  0.0304  5   SER   B C   
3791 O  O   . SER   B 5   ? 0.2671 0.3036 0.3528 -0.0623 0.0683  0.0305  5   SER   B O   
3792 C  CB  . SER   B 5   ? 0.2481 0.3261 0.2370 -0.0401 -0.0084 0.0488  5   SER   B CB  
3793 O  OG  . SER   B 5   ? 0.2770 0.3514 0.2941 -0.0262 -0.0027 0.0593  5   SER   B OG  
3799 N  N   . PHE   B 6   ? 0.2699 0.3209 0.2106 -0.0693 0.0287  0.0292  6   PHE   B N   
3800 C  CA  . PHE   B 6   ? 0.2851 0.3193 0.1877 -0.0880 0.0342  0.0069  6   PHE   B CA  
3801 C  C   . PHE   B 6   ? 0.3402 0.3447 0.2465 -0.1022 0.0719  -0.0205 6   PHE   B C   
3802 O  O   . PHE   B 6   ? 0.3558 0.3742 0.2877 -0.0955 0.0550  -0.0301 6   PHE   B O   
3803 C  CB  . PHE   B 6   ? 0.2535 0.2970 0.1648 -0.0797 0.0121  0.0036  6   PHE   B CB  
3804 C  CG  . PHE   B 6   ? 0.2201 0.2716 0.1598 -0.0747 -0.0021 0.0056  6   PHE   B CG  
3805 C  CD1 . PHE   B 6   ? 0.2244 0.2461 0.1531 -0.0653 -0.0113 0.0055  6   PHE   B CD1 
3806 C  CD2 . PHE   B 6   ? 0.1964 0.2718 0.1690 -0.0623 0.0005  0.0329  6   PHE   B CD2 
3807 C  CE1 . PHE   B 6   ? 0.2180 0.2233 0.1644 -0.0544 -0.0130 0.0049  6   PHE   B CE1 
3808 C  CE2 . PHE   B 6   ? 0.2012 0.2619 0.1994 -0.0478 -0.0022 0.0324  6   PHE   B CE2 
3809 C  CZ  . PHE   B 6   ? 0.2050 0.2342 0.1788 -0.0500 -0.0093 0.0127  6   PHE   B CZ  
3819 N  N   A SER   B 7   ? 0.3681 0.3341 0.2598 -0.1194 0.1084  -0.0390 7   SER   B N   
3820 N  N   B SER   B 7   ? 0.3543 0.3375 0.2689 -0.1083 0.0843  -0.0334 7   SER   B N   
3821 C  CA  A SER   B 7   ? 0.4000 0.3454 0.3113 -0.1120 0.1245  -0.0523 7   SER   B CA  
3822 C  CA  B SER   B 7   ? 0.3692 0.3385 0.3064 -0.1029 0.0886  -0.0438 7   SER   B CA  
3823 C  C   A SER   B 7   ? 0.3949 0.3349 0.3068 -0.1136 0.1445  -0.0672 7   SER   B C   
3824 C  C   B SER   B 7   ? 0.3679 0.3293 0.3152 -0.1024 0.0976  -0.0527 7   SER   B C   
3825 O  O   A SER   B 7   ? 0.3996 0.3348 0.3301 -0.1167 0.1443  -0.0747 7   SER   B O   
3826 O  O   B SER   B 7   ? 0.3713 0.3301 0.3304 -0.1041 0.0946  -0.0545 7   SER   B O   
3827 C  CB  A SER   B 7   ? 0.4251 0.3610 0.3605 -0.1037 0.1243  -0.0510 7   SER   B CB  
3828 C  CB  B SER   B 7   ? 0.3798 0.3451 0.3322 -0.0979 0.0855  -0.0429 7   SER   B CB  
3829 O  OG  A SER   B 7   ? 0.4402 0.3743 0.4095 -0.0990 0.1199  -0.0409 7   SER   B OG  
3830 O  OG  B SER   B 7   ? 0.3859 0.3504 0.3573 -0.0944 0.0807  -0.0353 7   SER   B OG  
3841 N  N   A GLY   B 8   ? 0.3910 0.3284 0.3132 -0.0995 0.1570  -0.0723 8   GLY   B N   
3842 N  N   B GLY   B 8   ? 0.3656 0.3198 0.3194 -0.0942 0.1073  -0.0593 8   GLY   B N   
3843 C  CA  A GLY   B 8   ? 0.3769 0.3142 0.3138 -0.0904 0.1564  -0.0754 8   GLY   B CA  
3844 C  CA  B GLY   B 8   ? 0.3579 0.3062 0.3154 -0.0879 0.1136  -0.0656 8   GLY   B CA  
3845 C  C   A GLY   B 8   ? 0.3557 0.2908 0.3124 -0.0871 0.1467  -0.0758 8   GLY   B C   
3846 C  C   B GLY   B 8   ? 0.3464 0.2874 0.3090 -0.0846 0.1182  -0.0713 8   GLY   B C   
3847 O  O   A GLY   B 8   ? 0.3676 0.2998 0.3599 -0.0764 0.1432  -0.0853 8   GLY   B O   
3848 O  O   B GLY   B 8   ? 0.3527 0.2915 0.3336 -0.0800 0.1171  -0.0744 8   GLY   B O   
3855 N  N   . TYR   B 9   ? 0.3323 0.2677 0.2843 -0.0812 0.1136  -0.0829 9   TYR   B N   
3856 C  CA  . TYR   B 9   ? 0.2952 0.2279 0.2464 -0.0670 0.0795  -0.0626 9   TYR   B CA  
3857 C  C   . TYR   B 9   ? 0.2910 0.2229 0.2421 -0.0632 0.0440  -0.0539 9   TYR   B C   
3858 O  O   . TYR   B 9   ? 0.3124 0.2449 0.2878 -0.0739 0.0468  -0.0366 9   TYR   B O   
3859 C  CB  . TYR   B 9   ? 0.2781 0.2019 0.2558 -0.0558 0.0681  -0.0602 9   TYR   B CB  
3860 C  CG  . TYR   B 9   ? 0.2673 0.1905 0.2550 -0.0649 0.0625  -0.0641 9   TYR   B CG  
3861 C  CD1 . TYR   B 9   ? 0.2738 0.1931 0.2699 -0.0816 0.0674  -0.0575 9   TYR   B CD1 
3862 C  CD2 . TYR   B 9   ? 0.2563 0.1898 0.2439 -0.0628 0.0560  -0.0664 9   TYR   B CD2 
3863 C  CE1 . TYR   B 9   ? 0.2730 0.2061 0.2687 -0.0862 0.0726  -0.0679 9   TYR   B CE1 
3864 C  CE2 . TYR   B 9   ? 0.2636 0.1937 0.2539 -0.0657 0.0589  -0.0572 9   TYR   B CE2 
3865 C  CZ  . TYR   B 9   ? 0.2695 0.2076 0.2589 -0.0815 0.0666  -0.0773 9   TYR   B CZ  
3866 O  OH  . TYR   B 9   ? 0.2766 0.2222 0.2765 -0.0932 0.0633  -0.0857 9   TYR   B OH  
3877 N  N   . LEU   B 10  ? 0.2637 0.1987 0.2174 -0.0564 0.0243  -0.0466 10  LEU   B N   
3878 C  CA  . LEU   B 10  ? 0.2647 0.1966 0.2114 -0.0692 -0.0021 -0.0396 10  LEU   B CA  
3879 C  C   . LEU   B 10  ? 0.2499 0.1990 0.2266 -0.0637 -0.0131 -0.0354 10  LEU   B C   
3880 O  O   . LEU   B 10  ? 0.2296 0.2010 0.2283 -0.0513 -0.0042 -0.0314 10  LEU   B O   
3881 C  CB  . LEU   B 10  ? 0.2920 0.1970 0.2301 -0.0723 -0.0280 -0.0150 10  LEU   B CB  
3882 C  CG  . LEU   B 10  ? 0.3206 0.2059 0.2665 -0.0721 -0.0719 -0.0054 10  LEU   B CG  
3883 C  CD1 . LEU   B 10  ? 0.3407 0.2194 0.2944 -0.0660 -0.0677 -0.0093 10  LEU   B CD1 
3884 C  CD2 . LEU   B 10  ? 0.3305 0.2151 0.2950 -0.0727 -0.0651 0.0268  10  LEU   B CD2 
3896 N  N   . LYS   B 11  ? 0.2678 0.2307 0.2266 -0.0573 -0.0245 -0.0210 11  LYS   B N   
3897 C  CA  . LYS   B 11  ? 0.2927 0.2554 0.2461 -0.0493 -0.0279 -0.0256 11  LYS   B CA  
3898 C  C   . LYS   B 11  ? 0.2780 0.2288 0.2513 -0.0753 -0.0148 -0.0331 11  LYS   B C   
3899 O  O   . LYS   B 11  ? 0.3019 0.2523 0.2901 -0.0922 -0.0101 -0.0735 11  LYS   B O   
3900 C  CB  . LYS   B 11  ? 0.3332 0.3095 0.3069 -0.0183 -0.0354 -0.0294 11  LYS   B CB  
3901 C  CG  . LYS   B 11  ? 0.3694 0.3425 0.3884 -0.0030 -0.0380 -0.0326 11  LYS   B CG  
3902 C  CD  . LYS   B 11  ? 0.4018 0.3636 0.4653 0.0029  -0.0359 -0.0355 11  LYS   B CD  
3903 C  CE  . LYS   B 11  ? 0.4268 0.3774 0.5209 -0.0012 -0.0410 -0.0392 11  LYS   B CE  
3904 N  NZ  . LYS   B 11  ? 0.4389 0.3877 0.5481 -0.0066 -0.0501 -0.0399 11  LYS   B NZ  
3918 N  N   . LEU   B 12  ? 0.2356 0.1999 0.2432 -0.0631 -0.0194 -0.0379 12  LEU   B N   
3919 C  CA  . LEU   B 12  ? 0.2215 0.1788 0.2662 -0.0496 -0.0155 -0.0336 12  LEU   B CA  
3920 C  C   . LEU   B 12  ? 0.2117 0.1772 0.2786 -0.0484 -0.0326 -0.0381 12  LEU   B C   
3921 O  O   . LEU   B 12  ? 0.2159 0.1804 0.3123 -0.0515 -0.0476 -0.0325 12  LEU   B O   
3922 C  CB  . LEU   B 12  ? 0.2242 0.1575 0.2673 -0.0374 -0.0097 -0.0298 12  LEU   B CB  
3923 C  CG  . LEU   B 12  ? 0.2244 0.1564 0.2705 -0.0359 -0.0106 -0.0268 12  LEU   B CG  
3924 C  CD1 . LEU   B 12  ? 0.2333 0.1629 0.2631 -0.0173 -0.0193 -0.0093 12  LEU   B CD1 
3925 C  CD2 . LEU   B 12  ? 0.2336 0.1661 0.2873 -0.0335 -0.0124 -0.0383 12  LEU   B CD2 
3937 N  N   . THR   B 13  ? 0.2078 0.1843 0.2760 -0.0448 -0.0405 -0.0482 13  THR   B N   
3938 C  CA  . THR   B 13  ? 0.2082 0.1976 0.2595 -0.0573 -0.0604 -0.0288 13  THR   B CA  
3939 C  C   . THR   B 13  ? 0.2584 0.2203 0.2842 -0.0683 -0.0706 -0.0219 13  THR   B C   
3940 O  O   . THR   B 13  ? 0.2783 0.2177 0.2898 -0.0716 -0.0318 -0.0371 13  THR   B O   
3941 C  CB  . THR   B 13  ? 0.1972 0.1936 0.2718 -0.0466 -0.0504 -0.0170 13  THR   B CB  
3942 O  OG1 . THR   B 13  ? 0.1868 0.1787 0.2786 -0.0398 -0.0304 -0.0184 13  THR   B OG1 
3943 C  CG2 . THR   B 13  ? 0.2054 0.2010 0.2850 -0.0416 -0.0366 -0.0019 13  THR   B CG2 
3951 N  N   A ASP   B 14  ? 0.2719 0.2347 0.2959 -0.0821 -0.1049 -0.0069 14  ASP   B N   
3952 N  N   B ASP   B 14  ? 0.2672 0.2297 0.2940 -0.0701 -0.0846 -0.0068 14  ASP   B N   
3953 C  CA  A ASP   B 14  ? 0.2881 0.2503 0.3271 -0.0862 -0.1074 0.0164  14  ASP   B CA  
3954 C  CA  B ASP   B 14  ? 0.2771 0.2393 0.3090 -0.0693 -0.0859 0.0095  14  ASP   B CA  
3955 C  C   A ASP   B 14  ? 0.2775 0.2309 0.2774 -0.0867 -0.0858 0.0232  14  ASP   B C   
3956 C  C   B ASP   B 14  ? 0.2637 0.2225 0.2693 -0.0708 -0.0826 0.0144  14  ASP   B C   
3957 O  O   A ASP   B 14  ? 0.3059 0.2460 0.2768 -0.0867 -0.0799 0.0360  14  ASP   B O   
3958 O  O   B ASP   B 14  ? 0.2768 0.2267 0.2675 -0.0657 -0.0863 0.0175  14  ASP   B O   
3959 C  CB  A ASP   B 14  ? 0.3121 0.2913 0.4155 -0.0792 -0.1251 0.0192  14  ASP   B CB  
3960 C  CB  B ASP   B 14  ? 0.2984 0.2680 0.3667 -0.0628 -0.0876 0.0145  14  ASP   B CB  
3961 C  CG  A ASP   B 14  ? 0.3354 0.3243 0.4986 -0.0713 -0.1209 0.0041  14  ASP   B CG  
3962 C  CG  B ASP   B 14  ? 0.3173 0.2908 0.4180 -0.0574 -0.0823 0.0103  14  ASP   B CG  
3963 O  OD1 A ASP   B 14  ? 0.3513 0.3338 0.5179 -0.0712 -0.1231 -0.0149 14  ASP   B OD1 
3964 O  OD1 B ASP   B 14  ? 0.3261 0.3003 0.4270 -0.0569 -0.0783 0.0041  14  ASP   B OD1 
3965 O  OD2 A ASP   B 14  ? 0.3343 0.3382 0.5395 -0.0704 -0.1139 0.0060  14  ASP   B OD2 
3966 O  OD2 B ASP   B 14  ? 0.3204 0.2978 0.4409 -0.0586 -0.0831 0.0111  14  ASP   B OD2 
3975 N  N   . ASN   B 15  ? 0.2386 0.2034 0.2432 -0.0676 -0.0791 0.0212  15  ASN   B N   
3976 C  CA  . ASN   B 15  ? 0.1944 0.1735 0.2215 -0.0414 -0.0461 0.0158  15  ASN   B CA  
3977 C  C   . ASN   B 15  ? 0.1696 0.1554 0.2148 -0.0283 -0.0324 0.0014  15  ASN   B C   
3978 O  O   . ASN   B 15  ? 0.1687 0.1496 0.2513 -0.0256 -0.0446 -0.0150 15  ASN   B O   
3979 C  CB  . ASN   B 15  ? 0.1911 0.1710 0.2418 -0.0210 -0.0554 0.0156  15  ASN   B CB  
3980 C  CG  . ASN   B 15  ? 0.1745 0.1685 0.2472 -0.0260 -0.0271 0.0098  15  ASN   B CG  
3981 O  OD1 . ASN   B 15  ? 0.1802 0.1995 0.2884 -0.0440 -0.0311 0.0089  15  ASN   B OD1 
3982 N  ND2 . ASN   B 15  ? 0.1698 0.1492 0.2363 -0.0133 -0.0015 -0.0021 15  ASN   B ND2 
3990 N  N   . VAL   B 16  ? 0.1680 0.1500 0.2183 -0.0303 -0.0422 -0.0107 16  VAL   B N   
3991 C  CA  . VAL   B 16  ? 0.1638 0.1603 0.2063 -0.0229 -0.0236 -0.0230 16  VAL   B CA  
3992 C  C   . VAL   B 16  ? 0.1665 0.1691 0.2073 -0.0303 -0.0258 -0.0149 16  VAL   B C   
3993 O  O   . VAL   B 16  ? 0.1632 0.1798 0.2316 -0.0224 -0.0228 -0.0287 16  VAL   B O   
3994 C  CB  . VAL   B 16  ? 0.1658 0.1566 0.2126 -0.0141 -0.0120 -0.0229 16  VAL   B CB  
3995 C  CG1 . VAL   B 16  ? 0.1750 0.1525 0.2191 -0.0063 -0.0137 -0.0165 16  VAL   B CG1 
3996 C  CG2 . VAL   B 16  ? 0.1731 0.1632 0.2307 -0.0044 0.0020  -0.0239 16  VAL   B CG2 
4006 N  N   . TYR   B 17  ? 0.1724 0.1793 0.2117 -0.0259 -0.0169 -0.0251 17  TYR   B N   
4007 C  CA  . TYR   B 17  ? 0.1767 0.1875 0.2095 -0.0347 -0.0168 -0.0014 17  TYR   B CA  
4008 C  C   . TYR   B 17  ? 0.1732 0.1574 0.2008 -0.0367 -0.0058 -0.0166 17  TYR   B C   
4009 O  O   . TYR   B 17  ? 0.1752 0.1687 0.2093 -0.0335 -0.0220 -0.0374 17  TYR   B O   
4010 C  CB  . TYR   B 17  ? 0.2096 0.2435 0.2440 -0.0209 -0.0205 0.0365  17  TYR   B CB  
4011 C  CG  . TYR   B 17  ? 0.2436 0.2984 0.2881 -0.0082 -0.0460 0.0467  17  TYR   B CG  
4012 C  CD1 . TYR   B 17  ? 0.2671 0.3186 0.3151 -0.0049 -0.0535 0.0560  17  TYR   B CD1 
4013 C  CD2 . TYR   B 17  ? 0.2746 0.3300 0.3194 0.0001  -0.0568 0.0425  17  TYR   B CD2 
4014 C  CE1 . TYR   B 17  ? 0.2909 0.3463 0.3386 0.0047  -0.0678 0.0485  17  TYR   B CE1 
4015 C  CE2 . TYR   B 17  ? 0.2969 0.3548 0.3500 0.0128  -0.0733 0.0511  17  TYR   B CE2 
4016 C  CZ  . TYR   B 17  ? 0.3082 0.3671 0.3581 0.0147  -0.0797 0.0511  17  TYR   B CZ  
4017 O  OH  . TYR   B 17  ? 0.3273 0.3856 0.3729 0.0216  -0.0856 0.0554  17  TYR   B OH  
4027 N  N   . ILE   B 18  ? 0.1796 0.1650 0.1863 -0.0265 -0.0086 -0.0192 18  ILE   B N   
4028 C  CA  . ILE   B 18  ? 0.1875 0.1579 0.1916 -0.0353 -0.0011 -0.0299 18  ILE   B CA  
4029 C  C   . ILE   B 18  ? 0.1957 0.1635 0.1944 -0.0453 -0.0043 -0.0378 18  ILE   B C   
4030 O  O   . ILE   B 18  ? 0.2144 0.1768 0.2123 -0.0425 0.0059  -0.0442 18  ILE   B O   
4031 C  CB  . ILE   B 18  ? 0.1988 0.1603 0.2056 -0.0458 -0.0012 -0.0222 18  ILE   B CB  
4032 C  CG1 . ILE   B 18  ? 0.2040 0.1641 0.2154 -0.0421 0.0047  -0.0177 18  ILE   B CG1 
4033 C  CG2 . ILE   B 18  ? 0.2021 0.1706 0.2049 -0.0543 -0.0152 -0.0184 18  ILE   B CG2 
4034 C  CD1 . ILE   B 18  ? 0.2181 0.1849 0.2379 -0.0365 -0.0206 0.0103  18  ILE   B CD1 
4046 N  N   . LYS   B 19  ? 0.1955 0.1603 0.2066 -0.0251 0.0288  -0.0410 19  LYS   B N   
4047 C  CA  . LYS   B 19  ? 0.2035 0.1669 0.2436 -0.0258 0.0310  -0.0461 19  LYS   B CA  
4048 C  C   . LYS   B 19  ? 0.1891 0.1679 0.2587 -0.0199 0.0384  -0.0600 19  LYS   B C   
4049 O  O   . LYS   B 19  ? 0.1875 0.1655 0.2289 -0.0154 0.0275  -0.0429 19  LYS   B O   
4050 C  CB  . LYS   B 19  ? 0.2311 0.1923 0.2485 -0.0250 0.0456  -0.0401 19  LYS   B CB  
4051 C  CG  . LYS   B 19  ? 0.2640 0.2186 0.2881 -0.0342 0.0590  -0.0475 19  LYS   B CG  
4052 C  CD  . LYS   B 19  ? 0.2978 0.2518 0.3092 -0.0423 0.0794  -0.0422 19  LYS   B CD  
4053 C  CE  . LYS   B 19  ? 0.3277 0.2796 0.3367 -0.0491 0.0803  -0.0445 19  LYS   B CE  
4054 N  NZ  . LYS   B 19  ? 0.3402 0.2992 0.3389 -0.0560 0.0879  -0.0390 19  LYS   B NZ  
4068 N  N   . ASN   B 20  ? 0.1864 0.1807 0.2939 -0.0117 0.0412  -0.0694 20  ASN   B N   
4069 C  CA  . ASN   B 20  ? 0.1912 0.1869 0.3097 -0.0097 0.0452  -0.0912 20  ASN   B CA  
4070 C  C   . ASN   B 20  ? 0.1899 0.2121 0.3052 -0.0120 0.0484  -0.0961 20  ASN   B C   
4071 O  O   . ASN   B 20  ? 0.2084 0.2561 0.3170 -0.0273 0.0478  -0.0977 20  ASN   B O   
4072 C  CB  . ASN   B 20  ? 0.2295 0.1946 0.3578 0.0122  0.0312  -0.0909 20  ASN   B CB  
4073 C  CG  . ASN   B 20  ? 0.2633 0.2096 0.3757 0.0462  0.0288  -0.0984 20  ASN   B CG  
4074 O  OD1 . ASN   B 20  ? 0.2980 0.2391 0.3953 0.0606  0.0221  -0.0980 20  ASN   B OD1 
4075 N  ND2 . ASN   B 20  ? 0.2550 0.2118 0.3695 0.0497  0.0111  -0.0975 20  ASN   B ND2 
4082 N  N   . ALA   B 21  ? 0.1919 0.1958 0.3055 -0.0212 0.0508  -0.0822 21  ALA   B N   
4083 C  CA  . ALA   B 21  ? 0.2054 0.2021 0.3183 -0.0219 0.0374  -0.0678 21  ALA   B CA  
4084 C  C   . ALA   B 21  ? 0.2036 0.1763 0.3042 -0.0183 0.0463  -0.0560 21  ALA   B C   
4085 O  O   . ALA   B 21  ? 0.2101 0.1672 0.3035 -0.0236 0.0458  -0.0459 21  ALA   B O   
4086 C  CB  . ALA   B 21  ? 0.2194 0.2337 0.3205 -0.0322 0.0416  -0.0500 21  ALA   B CB  
4092 N  N   . ASP   B 22  ? 0.1910 0.1620 0.2963 -0.0183 0.0333  -0.0480 22  ASP   B N   
4093 C  CA  . ASP   B 22  ? 0.1885 0.1578 0.2715 -0.0095 0.0211  -0.0333 22  ASP   B CA  
4094 C  C   . ASP   B 22  ? 0.1894 0.1520 0.2220 -0.0128 0.0147  -0.0194 22  ASP   B C   
4095 O  O   . ASP   B 22  ? 0.1948 0.1611 0.2279 -0.0071 0.0156  -0.0159 22  ASP   B O   
4096 C  CB  . ASP   B 22  ? 0.1948 0.1647 0.3169 -0.0020 0.0194  -0.0181 22  ASP   B CB  
4097 C  CG  . ASP   B 22  ? 0.1979 0.1923 0.3570 0.0052  -0.0004 -0.0168 22  ASP   B CG  
4098 O  OD1 . ASP   B 22  ? 0.2132 0.1868 0.3573 0.0042  -0.0199 -0.0134 22  ASP   B OD1 
4099 O  OD2 . ASP   B 22  ? 0.2072 0.2195 0.4157 0.0112  -0.0213 -0.0346 22  ASP   B OD2 
4104 N  N   . ILE   B 23  ? 0.1879 0.1426 0.2043 -0.0107 0.0044  0.0098  23  ILE   B N   
4105 C  CA  . ILE   B 23  ? 0.1745 0.1435 0.1886 -0.0106 -0.0032 0.0018  23  ILE   B CA  
4106 C  C   . ILE   B 23  ? 0.1682 0.1473 0.1796 0.0001  -0.0065 0.0010  23  ILE   B C   
4107 O  O   . ILE   B 23  ? 0.1617 0.1443 0.1727 -0.0060 -0.0090 0.0022  23  ILE   B O   
4108 C  CB  . ILE   B 23  ? 0.1703 0.1528 0.1967 -0.0138 -0.0012 0.0117  23  ILE   B CB  
4109 C  CG1 . ILE   B 23  ? 0.1728 0.1592 0.2169 -0.0070 0.0049  0.0200  23  ILE   B CG1 
4110 C  CG2 . ILE   B 23  ? 0.1815 0.1731 0.1959 -0.0154 -0.0044 -0.0011 23  ILE   B CG2 
4111 C  CD1 . ILE   B 23  ? 0.1810 0.1707 0.2271 -0.0017 0.0058  0.0190  23  ILE   B CD1 
4123 N  N   . VAL   B 24  ? 0.1745 0.1502 0.1903 -0.0052 -0.0052 -0.0046 24  VAL   B N   
4124 C  CA  . VAL   B 24  ? 0.1684 0.1612 0.2114 -0.0073 -0.0152 -0.0066 24  VAL   B CA  
4125 C  C   . VAL   B 24  ? 0.1644 0.1581 0.2124 -0.0082 -0.0136 -0.0061 24  VAL   B C   
4126 O  O   . VAL   B 24  ? 0.1610 0.1686 0.2254 -0.0142 -0.0077 0.0111  24  VAL   B O   
4127 C  CB  . VAL   B 24  ? 0.1781 0.1729 0.2212 0.0050  -0.0243 0.0053  24  VAL   B CB  
4128 C  CG1 . VAL   B 24  ? 0.1818 0.1774 0.2596 -0.0043 -0.0248 0.0055  24  VAL   B CG1 
4129 C  CG2 . VAL   B 24  ? 0.1921 0.2044 0.2203 0.0084  -0.0289 -0.0123 24  VAL   B CG2 
4139 N  N   . GLU   B 25  ? 0.1908 0.1734 0.2133 -0.0075 -0.0012 -0.0072 25  GLU   B N   
4140 C  CA  . GLU   B 25  ? 0.1998 0.1974 0.2366 0.0060  0.0127  -0.0097 25  GLU   B CA  
4141 C  C   . GLU   B 25  ? 0.1940 0.1898 0.2117 -0.0097 0.0108  -0.0056 25  GLU   B C   
4142 O  O   . GLU   B 25  ? 0.2036 0.2072 0.2293 -0.0066 0.0181  -0.0006 25  GLU   B O   
4143 C  CB  . GLU   B 25  ? 0.2364 0.2491 0.3132 0.0384  0.0339  -0.0080 25  GLU   B CB  
4144 C  CG  . GLU   B 25  ? 0.2811 0.3211 0.4288 0.0433  0.0372  -0.0109 25  GLU   B CG  
4145 C  CD  . GLU   B 25  ? 0.3213 0.3876 0.5220 0.0364  0.0336  -0.0174 25  GLU   B CD  
4146 O  OE1 . GLU   B 25  ? 0.3486 0.4140 0.5476 0.0421  0.0417  -0.0169 25  GLU   B OE1 
4147 O  OE2 . GLU   B 25  ? 0.3446 0.4118 0.5549 0.0313  0.0223  -0.0270 25  GLU   B OE2 
4154 N  N   A GLU   B 26  ? 0.1886 0.1773 0.1851 -0.0271 0.0122  -0.0033 26  GLU   B N   
4155 N  N   B GLU   B 26  ? 0.1899 0.1818 0.1972 -0.0210 0.0067  -0.0021 26  GLU   B N   
4156 C  CA  A GLU   B 26  ? 0.1924 0.1921 0.1970 -0.0356 0.0009  0.0025  26  GLU   B CA  
4157 C  CA  B GLU   B 26  ? 0.1884 0.1854 0.2040 -0.0294 -0.0025 0.0016  26  GLU   B CA  
4158 C  C   A GLU   B 26  ? 0.1738 0.1920 0.1850 -0.0284 0.0061  0.0141  26  GLU   B C   
4159 C  C   B GLU   B 26  ? 0.1733 0.1851 0.1859 -0.0266 0.0051  0.0120  26  GLU   B C   
4160 O  O   A GLU   B 26  ? 0.1903 0.2154 0.1847 -0.0237 -0.0031 0.0201  26  GLU   B O   
4161 O  O   B GLU   B 26  ? 0.1825 0.1991 0.1847 -0.0240 0.0004  0.0162  26  GLU   B O   
4162 C  CB  A GLU   B 26  ? 0.2264 0.2156 0.2222 -0.0465 0.0260  0.0281  26  GLU   B CB  
4163 C  CB  B GLU   B 26  ? 0.2064 0.1933 0.2313 -0.0391 -0.0014 0.0074  26  GLU   B CB  
4164 C  CG  A GLU   B 26  ? 0.2691 0.2529 0.2922 -0.0434 0.0428  0.0092  26  GLU   B CG  
4165 C  CG  B GLU   B 26  ? 0.2287 0.2060 0.2809 -0.0447 -0.0028 -0.0126 26  GLU   B CG  
4166 C  CD  A GLU   B 26  ? 0.2886 0.2707 0.3136 -0.0568 0.0750  -0.0087 26  GLU   B CD  
4167 C  CD  B GLU   B 26  ? 0.2329 0.2029 0.2961 -0.0622 -0.0052 -0.0420 26  GLU   B CD  
4168 O  OE1 A GLU   B 26  ? 0.3002 0.2590 0.3138 -0.0591 0.1265  -0.0005 26  GLU   B OE1 
4169 O  OE1 B GLU   B 26  ? 0.2282 0.1928 0.3180 -0.0818 0.0123  -0.0691 26  GLU   B OE1 
4170 O  OE2 A GLU   B 26  ? 0.2855 0.2885 0.3470 -0.0694 0.0795  -0.0006 26  GLU   B OE2 
4171 O  OE2 B GLU   B 26  ? 0.2363 0.2044 0.3062 -0.0564 -0.0007 -0.0337 26  GLU   B OE2 
4184 N  N   . ALA   B 27  ? 0.1579 0.1726 0.1766 -0.0276 0.0156  0.0158  27  ALA   B N   
4185 C  CA  . ALA   B 27  ? 0.1580 0.1680 0.2038 -0.0156 0.0026  0.0246  27  ALA   B CA  
4186 C  C   . ALA   B 27  ? 0.1606 0.1832 0.2224 -0.0198 0.0174  0.0435  27  ALA   B C   
4187 O  O   . ALA   B 27  ? 0.1719 0.1928 0.2322 -0.0081 0.0158  0.0459  27  ALA   B O   
4188 C  CB  . ALA   B 27  ? 0.1775 0.1538 0.2027 -0.0111 0.0051  0.0183  27  ALA   B CB  
4195 N  N   . LYS   B 28  ? 0.1564 0.2101 0.2551 -0.0223 0.0201  0.0613  28  LYS   B N   
4196 C  CA  . LYS   B 28  ? 0.1772 0.2448 0.2787 -0.0057 0.0501  0.0922  28  LYS   B CA  
4197 C  C   . LYS   B 28  ? 0.2060 0.2620 0.2508 0.0048  0.0580  0.0876  28  LYS   B C   
4198 O  O   . LYS   B 28  ? 0.2348 0.2679 0.2679 0.0034  0.0663  0.0748  28  LYS   B O   
4199 C  CB  . LYS   B 28  ? 0.1977 0.2772 0.3515 0.0141  0.0761  0.1142  28  LYS   B CB  
4200 C  CG  . LYS   B 28  ? 0.2217 0.3250 0.3887 0.0298  0.0811  0.1224  28  LYS   B CG  
4201 C  CD  . LYS   B 28  ? 0.2730 0.3931 0.4533 0.0408  0.0931  0.1174  28  LYS   B CD  
4202 C  CE  . LYS   B 28  ? 0.3145 0.4416 0.5049 0.0522  0.0974  0.1221  28  LYS   B CE  
4203 N  NZ  . LYS   B 28  ? 0.3354 0.4653 0.5275 0.0608  0.0971  0.1255  28  LYS   B NZ  
4217 N  N   . LYS   B 29  ? 0.2225 0.2878 0.2462 0.0255  0.0660  0.0678  29  LYS   B N   
4218 C  CA  . LYS   B 29  ? 0.2693 0.3277 0.2744 0.0244  0.0669  0.0700  29  LYS   B CA  
4219 C  C   . LYS   B 29  ? 0.2629 0.3301 0.2400 0.0173  0.0500  0.0792  29  LYS   B C   
4220 O  O   . LYS   B 29  ? 0.2835 0.3544 0.2481 0.0250  0.0447  0.0784  29  LYS   B O   
4221 C  CB  . LYS   B 29  ? 0.3308 0.3665 0.3655 0.0246  0.0667  0.0574  29  LYS   B CB  
4222 C  CG  . LYS   B 29  ? 0.3853 0.3988 0.4722 0.0217  0.0635  0.0561  29  LYS   B CG  
4223 C  CD  . LYS   B 29  ? 0.4364 0.4225 0.5460 0.0159  0.0688  0.0536  29  LYS   B CD  
4224 C  CE  . LYS   B 29  ? 0.4742 0.4379 0.5973 0.0090  0.0779  0.0521  29  LYS   B CE  
4225 N  NZ  . LYS   B 29  ? 0.4961 0.4461 0.6312 0.0046  0.0809  0.0501  29  LYS   B NZ  
4239 N  N   . VAL   B 30  ? 0.2300 0.3080 0.2315 -0.0010 0.0351  0.0759  30  VAL   B N   
4240 C  CA  . VAL   B 30  ? 0.2144 0.2941 0.2699 -0.0118 -0.0047 0.0788  30  VAL   B CA  
4241 C  C   . VAL   B 30  ? 0.1889 0.2827 0.2668 -0.0131 -0.0003 0.1002  30  VAL   B C   
4242 O  O   . VAL   B 30  ? 0.1970 0.3071 0.2757 -0.0072 0.0088  0.1143  30  VAL   B O   
4243 C  CB  . VAL   B 30  ? 0.2196 0.2859 0.3246 -0.0273 -0.0336 0.0682  30  VAL   B CB  
4244 C  CG1 . VAL   B 30  ? 0.2262 0.2916 0.3315 -0.0293 -0.0199 0.0603  30  VAL   B CG1 
4245 C  CG2 . VAL   B 30  ? 0.2348 0.2892 0.3469 -0.0346 -0.0561 0.0444  30  VAL   B CG2 
4255 N  N   . LYS   B 31  ? 0.1843 0.2391 0.3013 -0.0317 -0.0015 0.1053  31  LYS   B N   
4256 C  CA  . LYS   B 31  ? 0.1705 0.2353 0.3354 -0.0377 -0.0086 0.1119  31  LYS   B CA  
4257 C  C   . LYS   B 31  ? 0.1720 0.2045 0.2887 -0.0367 -0.0295 0.0955  31  LYS   B C   
4258 O  O   . LYS   B 31  ? 0.1714 0.2270 0.2957 -0.0314 -0.0148 0.1140  31  LYS   B O   
4259 C  CB  . LYS   B 31  ? 0.1816 0.2876 0.4042 -0.0265 0.0181  0.1206  31  LYS   B CB  
4260 C  CG  . LYS   B 31  ? 0.2132 0.3359 0.4498 -0.0229 0.0358  0.1181  31  LYS   B CG  
4261 C  CD  . LYS   B 31  ? 0.2532 0.3853 0.4889 -0.0146 0.0312  0.1023  31  LYS   B CD  
4262 C  CE  . LYS   B 31  ? 0.2759 0.4147 0.5271 -0.0090 0.0238  0.0905  31  LYS   B CE  
4263 N  NZ  . LYS   B 31  ? 0.2976 0.4364 0.5320 -0.0015 0.0138  0.0817  31  LYS   B NZ  
4277 N  N   . PRO   B 32  ? 0.1830 0.1691 0.2153 -0.0342 -0.0449 0.0580  32  PRO   B N   
4278 C  CA  . PRO   B 32  ? 0.1897 0.1626 0.1738 -0.0395 -0.0422 0.0330  32  PRO   B CA  
4279 C  C   . PRO   B 32  ? 0.1952 0.1525 0.1859 -0.0469 -0.0552 0.0368  32  PRO   B C   
4280 O  O   . PRO   B 32  ? 0.2099 0.1563 0.2337 -0.0450 -0.0754 0.0393  32  PRO   B O   
4281 C  CB  . PRO   B 32  ? 0.2007 0.1565 0.1824 -0.0429 -0.0267 0.0065  32  PRO   B CB  
4282 C  CG  . PRO   B 32  ? 0.2148 0.1467 0.1828 -0.0331 -0.0434 0.0176  32  PRO   B CG  
4283 C  CD  . PRO   B 32  ? 0.2009 0.1522 0.2055 -0.0290 -0.0577 0.0319  32  PRO   B CD  
4291 N  N   . THR   B 33  ? 0.1993 0.1454 0.1784 -0.0333 -0.0539 0.0190  33  THR   B N   
4292 C  CA  . THR   B 33  ? 0.2046 0.1527 0.1814 -0.0410 -0.0471 0.0250  33  THR   B CA  
4293 C  C   . THR   B 33  ? 0.2034 0.1433 0.1629 -0.0397 -0.0530 0.0227  33  THR   B C   
4294 O  O   . THR   B 33  ? 0.2213 0.1440 0.1803 -0.0434 -0.0578 0.0257  33  THR   B O   
4295 C  CB  . THR   B 33  ? 0.2147 0.1635 0.1814 -0.0218 -0.0564 0.0224  33  THR   B CB  
4296 O  OG1 . THR   B 33  ? 0.2057 0.1696 0.1856 -0.0239 -0.0571 0.0339  33  THR   B OG1 
4297 C  CG2 . THR   B 33  ? 0.2371 0.1721 0.1992 -0.0141 -0.0456 0.0190  33  THR   B CG2 
4305 N  N   . VAL   B 34  ? 0.1894 0.1406 0.1539 -0.0428 -0.0478 0.0200  34  VAL   B N   
4306 C  CA  . VAL   B 34  ? 0.1742 0.1334 0.1511 -0.0302 -0.0386 0.0126  34  VAL   B CA  
4307 C  C   . VAL   B 34  ? 0.1588 0.1301 0.1260 -0.0257 -0.0162 0.0159  34  VAL   B C   
4308 O  O   . VAL   B 34  ? 0.1781 0.1351 0.1506 -0.0224 -0.0340 0.0039  34  VAL   B O   
4309 C  CB  . VAL   B 34  ? 0.1745 0.1417 0.1847 -0.0076 -0.0265 0.0014  34  VAL   B CB  
4310 C  CG1 . VAL   B 34  ? 0.1714 0.1628 0.1834 -0.0081 -0.0044 -0.0066 34  VAL   B CG1 
4311 C  CG2 . VAL   B 34  ? 0.1797 0.1480 0.2147 -0.0084 -0.0289 0.0041  34  VAL   B CG2 
4321 N  N   . VAL   B 35  ? 0.1514 0.1271 0.1395 -0.0264 -0.0108 0.0085  35  VAL   B N   
4322 C  CA  . VAL   B 35  ? 0.1454 0.1248 0.1418 -0.0185 -0.0089 0.0057  35  VAL   B CA  
4323 C  C   . VAL   B 35  ? 0.1377 0.1163 0.1319 -0.0201 -0.0129 0.0040  35  VAL   B C   
4324 O  O   . VAL   B 35  ? 0.1440 0.1246 0.1411 -0.0212 0.0025  -0.0039 35  VAL   B O   
4325 C  CB  . VAL   B 35  ? 0.1417 0.1384 0.1465 -0.0174 0.0013  0.0049  35  VAL   B CB  
4326 C  CG1 . VAL   B 35  ? 0.1407 0.1508 0.1722 -0.0215 0.0007  -0.0004 35  VAL   B CG1 
4327 C  CG2 . VAL   B 35  ? 0.1465 0.1484 0.1738 -0.0086 -0.0058 0.0005  35  VAL   B CG2 
4337 N  N   . VAL   B 36  ? 0.1385 0.1254 0.1249 -0.0158 -0.0205 0.0068  36  VAL   B N   
4338 C  CA  . VAL   B 36  ? 0.1372 0.1233 0.1231 -0.0141 -0.0063 0.0012  36  VAL   B CA  
4339 C  C   . VAL   B 36  ? 0.1307 0.1237 0.1184 -0.0078 -0.0060 -0.0057 36  VAL   B C   
4340 O  O   . VAL   B 36  ? 0.1385 0.1330 0.1453 -0.0121 -0.0044 -0.0086 36  VAL   B O   
4341 C  CB  . VAL   B 36  ? 0.1369 0.1272 0.1350 -0.0155 -0.0048 0.0015  36  VAL   B CB  
4342 C  CG1 . VAL   B 36  ? 0.1363 0.1387 0.1512 -0.0163 -0.0041 0.0042  36  VAL   B CG1 
4343 C  CG2 . VAL   B 36  ? 0.1364 0.1332 0.1479 -0.0163 -0.0169 0.0018  36  VAL   B CG2 
4353 N  N   . ASN   B 37  ? 0.1301 0.1258 0.1328 -0.0000 -0.0070 0.0035  37  ASN   B N   
4354 C  CA  . ASN   B 37  ? 0.1359 0.1243 0.1246 0.0001  -0.0088 0.0038  37  ASN   B CA  
4355 C  C   . ASN   B 37  ? 0.1344 0.1335 0.1349 -0.0009 -0.0096 0.0032  37  ASN   B C   
4356 O  O   . ASN   B 37  ? 0.1419 0.1378 0.1433 -0.0004 0.0060  0.0097  37  ASN   B O   
4357 C  CB  . ASN   B 37  ? 0.1342 0.1345 0.1184 0.0035  -0.0095 0.0027  37  ASN   B CB  
4358 C  CG  . ASN   B 37  ? 0.1366 0.1346 0.1358 -0.0051 -0.0078 -0.0021 37  ASN   B CG  
4359 O  OD1 . ASN   B 37  ? 0.1499 0.1401 0.1603 0.0069  -0.0118 -0.0014 37  ASN   B OD1 
4360 N  ND2 . ASN   B 37  ? 0.1460 0.1309 0.1396 -0.0011 -0.0144 0.0028  37  ASN   B ND2 
4367 N  N   . ALA   B 38  ? 0.1482 0.1297 0.1267 0.0061  0.0016  0.0035  38  ALA   B N   
4368 C  CA  . ALA   B 38  ? 0.1525 0.1319 0.1329 0.0040  0.0034  0.0154  38  ALA   B CA  
4369 C  C   . ALA   B 38  ? 0.1434 0.1292 0.1356 -0.0016 0.0040  0.0035  38  ALA   B C   
4370 O  O   . ALA   B 38  ? 0.1530 0.1401 0.1580 0.0057  -0.0003 0.0093  38  ALA   B O   
4371 C  CB  . ALA   B 38  ? 0.1815 0.1376 0.1403 -0.0029 0.0068  0.0047  38  ALA   B CB  
4377 N  N   . ALA   B 39  ? 0.1489 0.1329 0.1325 0.0065  0.0008  0.0036  39  ALA   B N   
4378 C  CA  . ALA   B 39  ? 0.1578 0.1381 0.1361 0.0052  -0.0030 0.0063  39  ALA   B CA  
4379 C  C   . ALA   B 39  ? 0.1577 0.1413 0.1198 0.0101  -0.0037 0.0080  39  ALA   B C   
4380 O  O   . ALA   B 39  ? 0.1604 0.1503 0.1482 0.0042  -0.0031 0.0133  39  ALA   B O   
4381 C  CB  . ALA   B 39  ? 0.1516 0.1435 0.1618 -0.0060 -0.0030 0.0046  39  ALA   B CB  
4387 N  N   . ASN   B 40  ? 0.1642 0.1665 0.1243 -0.0024 -0.0002 -0.0073 40  ASN   B N   
4388 C  CA  . ASN   B 40  ? 0.1636 0.1690 0.1443 0.0037  -0.0038 -0.0142 40  ASN   B CA  
4389 C  C   . ASN   B 40  ? 0.1725 0.1690 0.1232 0.0063  -0.0082 -0.0018 40  ASN   B C   
4390 O  O   . ASN   B 40  ? 0.1689 0.1644 0.1330 0.0080  -0.0086 0.0078  40  ASN   B O   
4391 C  CB  . ASN   B 40  ? 0.1782 0.1748 0.1623 0.0104  -0.0144 0.0092  40  ASN   B CB  
4392 C  CG  . ASN   B 40  ? 0.1820 0.1802 0.1955 0.0056  -0.0251 0.0220  40  ASN   B CG  
4393 O  OD1 . ASN   B 40  ? 0.1799 0.1717 0.2789 0.0043  -0.0406 0.0175  40  ASN   B OD1 
4394 N  ND2 . ASN   B 40  ? 0.1881 0.1769 0.1941 0.0028  -0.0248 0.0247  40  ASN   B ND2 
4401 N  N   . VAL   B 41  ? 0.1820 0.1766 0.1380 0.0141  0.0076  -0.0017 41  VAL   B N   
4402 C  CA  . VAL   B 41  ? 0.1872 0.1887 0.1384 0.0133  0.0020  -0.0033 41  VAL   B CA  
4403 C  C   . VAL   B 41  ? 0.1812 0.1916 0.1315 0.0153  -0.0052 -0.0110 41  VAL   B C   
4404 O  O   . VAL   B 41  ? 0.1809 0.1901 0.1542 0.0096  -0.0116 -0.0183 41  VAL   B O   
4405 C  CB  . VAL   B 41  ? 0.2064 0.2071 0.1695 -0.0062 0.0222  -0.0193 41  VAL   B CB  
4406 C  CG1 . VAL   B 41  ? 0.2063 0.2061 0.1700 -0.0117 0.0367  -0.0241 41  VAL   B CG1 
4407 C  CG2 . VAL   B 41  ? 0.2163 0.2316 0.1740 -0.0128 0.0302  -0.0138 41  VAL   B CG2 
4417 N  N   . TYR   B 42  ? 0.1864 0.1913 0.1377 0.0173  -0.0185 0.0029  42  TYR   B N   
4418 C  CA  . TYR   B 42  ? 0.1957 0.1942 0.1379 0.0163  -0.0256 -0.0200 42  TYR   B CA  
4419 C  C   . TYR   B 42  ? 0.1744 0.1754 0.1531 0.0205  -0.0232 -0.0133 42  TYR   B C   
4420 O  O   . TYR   B 42  ? 0.1722 0.1833 0.1978 0.0179  -0.0269 -0.0119 42  TYR   B O   
4421 C  CB  . TYR   B 42  ? 0.2197 0.2238 0.1545 0.0092  -0.0345 -0.0086 42  TYR   B CB  
4422 C  CG  . TYR   B 42  ? 0.2225 0.2392 0.1557 -0.0044 -0.0351 0.0098  42  TYR   B CG  
4423 C  CD1 . TYR   B 42  ? 0.2183 0.2382 0.1389 -0.0050 -0.0216 0.0043  42  TYR   B CD1 
4424 C  CD2 . TYR   B 42  ? 0.2407 0.2536 0.1989 -0.0073 -0.0124 0.0233  42  TYR   B CD2 
4425 C  CE1 . TYR   B 42  ? 0.2349 0.2581 0.1426 0.0051  -0.0097 0.0007  42  TYR   B CE1 
4426 C  CE2 . TYR   B 42  ? 0.2464 0.2667 0.1942 -0.0030 0.0152  0.0415  42  TYR   B CE2 
4427 C  CZ  . TYR   B 42  ? 0.2586 0.2798 0.1715 0.0173  0.0139  0.0135  42  TYR   B CZ  
4428 O  OH  . TYR   B 42  ? 0.2959 0.3119 0.2172 0.0372  0.0253  0.0222  42  TYR   B OH  
4438 N  N   . LEU   B 43  ? 0.1594 0.1603 0.1388 0.0068  -0.0175 -0.0148 43  LEU   B N   
4439 C  CA  . LEU   B 43  ? 0.1621 0.1601 0.1314 0.0036  -0.0150 -0.0027 43  LEU   B CA  
4440 C  C   . LEU   B 43  ? 0.1658 0.1593 0.1432 0.0038  -0.0079 -0.0049 43  LEU   B C   
4441 O  O   . LEU   B 43  ? 0.1673 0.1664 0.1661 0.0024  -0.0079 0.0050  43  LEU   B O   
4442 C  CB  . LEU   B 43  ? 0.1603 0.1564 0.1488 -0.0019 -0.0166 -0.0041 43  LEU   B CB  
4443 C  CG  . LEU   B 43  ? 0.1683 0.1471 0.1598 0.0006  -0.0138 -0.0089 43  LEU   B CG  
4444 C  CD1 . LEU   B 43  ? 0.1752 0.1595 0.2021 -0.0024 -0.0336 -0.0041 43  LEU   B CD1 
4445 C  CD2 . LEU   B 43  ? 0.1648 0.1465 0.1742 -0.0062 -0.0253 -0.0065 43  LEU   B CD2 
4457 N  N   . LYS   B 44  ? 0.1605 0.1551 0.1518 0.0079  -0.0011 -0.0081 44  LYS   B N   
4458 C  CA  . LYS   B 44  ? 0.1777 0.1724 0.1461 0.0124  -0.0067 -0.0001 44  LYS   B CA  
4459 C  C   . LYS   B 44  ? 0.1706 0.1578 0.1496 0.0154  -0.0161 0.0038  44  LYS   B C   
4460 O  O   . LYS   B 44  ? 0.1878 0.1593 0.1842 0.0076  -0.0015 0.0006  44  LYS   B O   
4461 C  CB  . LYS   B 44  ? 0.2038 0.2017 0.1611 0.0254  -0.0208 -0.0050 44  LYS   B CB  
4462 C  CG  . LYS   B 44  ? 0.2367 0.2316 0.1905 0.0150  -0.0460 -0.0084 44  LYS   B CG  
4463 C  CD  . LYS   B 44  ? 0.2732 0.2509 0.2482 -0.0059 -0.0583 -0.0127 44  LYS   B CD  
4464 C  CE  . LYS   B 44  ? 0.3059 0.2733 0.3006 -0.0171 -0.0573 0.0020  44  LYS   B CE  
4465 N  NZ  . LYS   B 44  ? 0.3184 0.2837 0.3375 -0.0143 -0.0642 0.0207  44  LYS   B NZ  
4479 N  N   . HIS   B 45  ? 0.1631 0.1671 0.1440 0.0069  -0.0084 0.0131  45  HIS   B N   
4480 C  CA  . HIS   B 45  ? 0.1655 0.1624 0.1552 0.0057  -0.0059 0.0022  45  HIS   B CA  
4481 C  C   . HIS   B 45  ? 0.1871 0.1836 0.1881 0.0170  -0.0128 0.0012  45  HIS   B C   
4482 O  O   . HIS   B 45  ? 0.2011 0.2110 0.2352 0.0406  0.0134  0.0053  45  HIS   B O   
4483 C  CB  . HIS   B 45  ? 0.1586 0.1635 0.1538 0.0017  -0.0115 -0.0115 45  HIS   B CB  
4484 C  CG  . HIS   B 45  ? 0.1590 0.1587 0.1570 -0.0001 -0.0060 -0.0011 45  HIS   B CG  
4485 N  ND1 . HIS   B 45  ? 0.1617 0.1528 0.1614 0.0061  -0.0211 -0.0013 45  HIS   B ND1 
4486 C  CD2 . HIS   B 45  ? 0.1716 0.1598 0.1737 -0.0039 -0.0170 -0.0025 45  HIS   B CD2 
4487 C  CE1 . HIS   B 45  ? 0.1746 0.1403 0.1415 0.0020  -0.0325 -0.0042 45  HIS   B CE1 
4488 N  NE2 . HIS   B 45  ? 0.1822 0.1519 0.1572 -0.0019 -0.0198 -0.0041 45  HIS   B NE2 
4496 N  N   A GLY   B 46  ? 0.1955 0.1779 0.2214 0.0210  -0.0321 0.0174  46  GLY   B N   
4497 N  N   B GLY   B 46  ? 0.1962 0.1889 0.2085 0.0163  -0.0248 0.0137  46  GLY   B N   
4498 C  CA  A GLY   B 46  ? 0.2124 0.1860 0.2587 0.0163  -0.0341 0.0212  46  GLY   B CA  
4499 C  CA  B GLY   B 46  ? 0.2092 0.1996 0.2310 0.0124  -0.0300 0.0210  46  GLY   B CA  
4500 C  C   A GLY   B 46  ? 0.2177 0.2053 0.3065 0.0211  -0.0296 0.0165  46  GLY   B C   
4501 C  C   B GLY   B 46  ? 0.2177 0.2154 0.2588 0.0133  -0.0312 0.0251  46  GLY   B C   
4502 O  O   A GLY   B 46  ? 0.2265 0.2173 0.3921 0.0284  -0.0067 -0.0055 46  GLY   B O   
4503 O  O   B GLY   B 46  ? 0.2248 0.2290 0.2683 0.0171  -0.0315 0.0345  46  GLY   B O   
4510 N  N   . GLY   B 47  ? 0.2205 0.2163 0.2740 0.0013  -0.0191 0.0095  47  GLY   B N   
4511 C  CA  . GLY   B 47  ? 0.2122 0.1864 0.2407 0.0018  -0.0128 -0.0001 47  GLY   B CA  
4512 C  C   . GLY   B 47  ? 0.1869 0.1648 0.2050 0.0026  0.0062  0.0054  47  GLY   B C   
4513 O  O   . GLY   B 47  ? 0.1972 0.1533 0.1993 0.0083  -0.0049 0.0137  47  GLY   B O   
4518 N  N   . GLY   B 48  ? 0.1711 0.1544 0.1976 0.0050  -0.0064 0.0219  48  GLY   B N   
4519 C  CA  . GLY   B 48  ? 0.1663 0.1502 0.1952 0.0003  -0.0007 0.0095  48  GLY   B CA  
4520 C  C   . GLY   B 48  ? 0.1501 0.1438 0.1831 0.0014  0.0082  0.0117  48  GLY   B C   
4521 O  O   . GLY   B 48  ? 0.1413 0.1505 0.2109 0.0066  -0.0055 0.0069  48  GLY   B O   
4525 N  N   . VAL   B 49  ? 0.1478 0.1484 0.1738 0.0070  0.0045  0.0105  49  VAL   B N   
4526 C  CA  . VAL   B 49  ? 0.1558 0.1594 0.1584 0.0106  -0.0068 -0.0012 49  VAL   B CA  
4527 C  C   . VAL   B 49  ? 0.1451 0.1486 0.1473 0.0127  -0.0015 0.0029  49  VAL   B C   
4528 O  O   . VAL   B 49  ? 0.1539 0.1511 0.1641 0.0040  -0.0024 0.0041  49  VAL   B O   
4529 C  CB  . VAL   B 49  ? 0.1566 0.1739 0.2005 0.0005  -0.0270 -0.0054 49  VAL   B CB  
4530 C  CG1 . VAL   B 49  ? 0.1546 0.1737 0.1894 0.0008  -0.0309 -0.0048 49  VAL   B CG1 
4531 C  CG2 . VAL   B 49  ? 0.1746 0.1924 0.2268 -0.0045 -0.0476 -0.0055 49  VAL   B CG2 
4541 N  N   . ALA   B 50  ? 0.1421 0.1447 0.1513 0.0031  0.0023  0.0086  50  ALA   B N   
4542 C  CA  . ALA   B 50  ? 0.1405 0.1371 0.1451 0.0053  -0.0003 0.0059  50  ALA   B CA  
4543 C  C   . ALA   B 50  ? 0.1450 0.1409 0.1473 0.0052  -0.0036 0.0059  50  ALA   B C   
4544 O  O   . ALA   B 50  ? 0.1455 0.1420 0.1543 0.0080  -0.0031 0.0035  50  ALA   B O   
4545 C  CB  . ALA   B 50  ? 0.1493 0.1355 0.1569 -0.0022 -0.0041 0.0146  50  ALA   B CB  
4551 N  N   . GLY   B 51  ? 0.1418 0.1575 0.1631 0.0146  -0.0081 0.0121  51  GLY   B N   
4552 C  CA  . GLY   B 51  ? 0.1493 0.1520 0.1853 0.0179  -0.0133 0.0076  51  GLY   B CA  
4553 C  C   . GLY   B 51  ? 0.1499 0.1509 0.1780 0.0211  -0.0130 0.0067  51  GLY   B C   
4554 O  O   . GLY   B 51  ? 0.1509 0.1656 0.1970 0.0069  -0.0138 -0.0011 51  GLY   B O   
4558 N  N   . ALA   B 52  ? 0.1509 0.1470 0.1661 0.0155  -0.0160 0.0086  52  ALA   B N   
4559 C  CA  . ALA   B 52  ? 0.1558 0.1522 0.1735 0.0155  -0.0032 -0.0040 52  ALA   B CA  
4560 C  C   . ALA   B 52  ? 0.1460 0.1499 0.1662 0.0102  -0.0037 -0.0025 52  ALA   B C   
4561 O  O   . ALA   B 52  ? 0.1463 0.1598 0.1863 0.0100  0.0019  -0.0016 52  ALA   B O   
4562 C  CB  . ALA   B 52  ? 0.1732 0.1529 0.1782 -0.0006 0.0023  -0.0023 52  ALA   B CB  
4568 N  N   . LEU   B 53  ? 0.1375 0.1422 0.1628 0.0123  0.0008  0.0034  53  LEU   B N   
4569 C  CA  . LEU   B 53  ? 0.1421 0.1514 0.1513 0.0158  -0.0019 0.0079  53  LEU   B CA  
4570 C  C   . LEU   B 53  ? 0.1495 0.1413 0.1620 0.0088  0.0002  0.0039  53  LEU   B C   
4571 O  O   . LEU   B 53  ? 0.1542 0.1506 0.1812 -0.0015 -0.0037 0.0143  53  LEU   B O   
4572 C  CB  . LEU   B 53  ? 0.1422 0.1609 0.1656 0.0103  0.0056  0.0149  53  LEU   B CB  
4573 C  CG  . LEU   B 53  ? 0.1376 0.1732 0.1711 0.0021  0.0014  0.0173  53  LEU   B CG  
4574 C  CD1 . LEU   B 53  ? 0.1516 0.1961 0.1959 0.0090  -0.0003 0.0024  53  LEU   B CD1 
4575 C  CD2 . LEU   B 53  ? 0.1553 0.2013 0.2005 -0.0061 -0.0131 -0.0171 53  LEU   B CD2 
4587 N  N   . ASN   B 54  ? 0.1444 0.1358 0.1528 0.0030  0.0027  0.0139  54  ASN   B N   
4588 C  CA  . ASN   B 54  ? 0.1505 0.1514 0.1665 0.0033  -0.0022 -0.0019 54  ASN   B CA  
4589 C  C   . ASN   B 54  ? 0.1493 0.1496 0.1877 0.0046  0.0029  -0.0042 54  ASN   B C   
4590 O  O   . ASN   B 54  ? 0.1456 0.1591 0.1945 -0.0013 0.0053  -0.0023 54  ASN   B O   
4591 C  CB  . ASN   B 54  ? 0.1526 0.1664 0.1864 0.0053  0.0013  -0.0059 54  ASN   B CB  
4592 C  CG  . ASN   B 54  ? 0.1466 0.1735 0.1814 0.0009  -0.0104 -0.0066 54  ASN   B CG  
4593 O  OD1 . ASN   B 54  ? 0.1452 0.1707 0.1929 -0.0028 -0.0076 -0.0194 54  ASN   B OD1 
4594 N  ND2 . ASN   B 54  ? 0.1605 0.1914 0.2025 -0.0002 -0.0275 0.0111  54  ASN   B ND2 
4601 N  N   . LYS   B 55  ? 0.1466 0.1579 0.1956 0.0116  -0.0025 -0.0056 55  LYS   B N   
4602 C  CA  . LYS   B 55  ? 0.1482 0.1731 0.2105 0.0203  -0.0052 -0.0029 55  LYS   B CA  
4603 C  C   . LYS   B 55  ? 0.1408 0.1767 0.2119 0.0140  0.0015  -0.0046 55  LYS   B C   
4604 O  O   . LYS   B 55  ? 0.1396 0.1893 0.2324 0.0153  0.0084  -0.0068 55  LYS   B O   
4605 C  CB  . LYS   B 55  ? 0.1606 0.1841 0.2469 0.0258  0.0097  -0.0007 55  LYS   B CB  
4606 C  CG  . LYS   B 55  ? 0.2067 0.2210 0.3446 0.0367  0.0163  0.0232  55  LYS   B CG  
4607 C  CD  . LYS   B 55  ? 0.2457 0.2522 0.4240 0.0479  0.0381  0.0366  55  LYS   B CD  
4608 C  CE  . LYS   B 55  ? 0.2689 0.2762 0.4938 0.0486  0.0567  0.0448  55  LYS   B CE  
4609 N  NZ  . LYS   B 55  ? 0.2768 0.2970 0.5347 0.0455  0.0428  0.0533  55  LYS   B NZ  
4623 N  N   . ALA   B 56  ? 0.1421 0.1776 0.1912 0.0073  0.0049  -0.0135 56  ALA   B N   
4624 C  CA  . ALA   B 56  ? 0.1602 0.1922 0.1898 0.0047  0.0103  -0.0148 56  ALA   B CA  
4625 C  C   . ALA   B 56  ? 0.1593 0.1848 0.1863 0.0011  0.0159  -0.0055 56  ALA   B C   
4626 O  O   . ALA   B 56  ? 0.1715 0.1979 0.2121 0.0077  0.0330  0.0015  56  ALA   B O   
4627 C  CB  . ALA   B 56  ? 0.1744 0.2120 0.1862 -0.0112 0.0042  -0.0172 56  ALA   B CB  
4633 N  N   . THR   B 57  ? 0.1552 0.1742 0.1955 0.0052  0.0271  -0.0047 57  THR   B N   
4634 C  CA  . THR   B 57  ? 0.1583 0.1745 0.2024 -0.0014 0.0291  -0.0010 57  THR   B CA  
4635 C  C   . THR   B 57  ? 0.1593 0.1823 0.2164 -0.0026 0.0287  0.0075  57  THR   B C   
4636 O  O   . THR   B 57  ? 0.1635 0.1830 0.2213 -0.0179 0.0197  0.0106  57  THR   B O   
4637 C  CB  . THR   B 57  ? 0.1642 0.1611 0.1771 -0.0004 0.0197  0.0073  57  THR   B CB  
4638 O  OG1 . THR   B 57  ? 0.1630 0.1532 0.1945 -0.0007 0.0227  0.0013  57  THR   B OG1 
4639 C  CG2 . THR   B 57  ? 0.1588 0.1603 0.1854 -0.0057 0.0116  -0.0027 57  THR   B CG2 
4647 N  N   . ASN   B 58  ? 0.1472 0.1951 0.2319 -0.0057 0.0140  -0.0153 58  ASN   B N   
4648 C  CA  . ASN   B 58  ? 0.1681 0.2399 0.2714 -0.0199 0.0419  -0.0109 58  ASN   B CA  
4649 C  C   . ASN   B 58  ? 0.1481 0.2181 0.2324 -0.0135 0.0093  -0.0123 58  ASN   B C   
4650 O  O   . ASN   B 58  ? 0.1547 0.2272 0.2408 -0.0157 0.0027  -0.0169 58  ASN   B O   
4651 C  CB  . ASN   B 58  ? 0.2705 0.3256 0.3987 -0.0363 0.0797  -0.0009 58  ASN   B CB  
4652 C  CG  . ASN   B 58  ? 0.3935 0.4171 0.5559 -0.0406 0.1036  0.0258  58  ASN   B CG  
4653 O  OD1 . ASN   B 58  ? 0.4162 0.4366 0.6183 -0.0439 0.1098  0.0334  58  ASN   B OD1 
4654 N  ND2 . ASN   B 58  ? 0.4825 0.4825 0.6090 -0.0418 0.1128  0.0315  58  ASN   B ND2 
4661 N  N   . ASN   B 59  ? 0.1467 0.2073 0.2109 -0.0082 0.0031  -0.0082 59  ASN   B N   
4662 C  CA  . ASN   B 59  ? 0.1534 0.2112 0.2160 -0.0093 -0.0101 0.0020  59  ASN   B CA  
4663 C  C   . ASN   B 59  ? 0.1517 0.1992 0.2072 -0.0105 -0.0133 -0.0097 59  ASN   B C   
4664 O  O   . ASN   B 59  ? 0.1547 0.1981 0.1937 -0.0121 -0.0087 -0.0059 59  ASN   B O   
4665 C  CB  . ASN   B 59  ? 0.1602 0.2306 0.2238 -0.0016 -0.0326 0.0052  59  ASN   B CB  
4666 C  CG  . ASN   B 59  ? 0.1735 0.2425 0.2334 -0.0001 -0.0365 0.0018  59  ASN   B CG  
4667 O  OD1 . ASN   B 59  ? 0.1720 0.2439 0.2349 0.0008  -0.0211 0.0189  59  ASN   B OD1 
4668 N  ND2 . ASN   B 59  ? 0.1851 0.2523 0.2421 -0.0072 -0.0352 -0.0076 59  ASN   B ND2 
4675 N  N   . ALA   B 60  ? 0.1509 0.1819 0.2048 -0.0120 0.0006  -0.0118 60  ALA   B N   
4676 C  CA  . ALA   B 60  ? 0.1665 0.1736 0.1944 -0.0180 0.0029  -0.0010 60  ALA   B CA  
4677 C  C   . ALA   B 60  ? 0.1637 0.1595 0.1663 -0.0111 0.0018  0.0008  60  ALA   B C   
4678 O  O   . ALA   B 60  ? 0.1696 0.1663 0.1836 -0.0143 0.0043  -0.0102 60  ALA   B O   
4679 C  CB  . ALA   B 60  ? 0.1829 0.1714 0.2332 -0.0219 0.0096  0.0029  60  ALA   B CB  
4685 N  N   . MET   B 61  ? 0.1527 0.1494 0.1839 -0.0062 -0.0016 0.0032  61  MET   B N   
4686 C  CA  . MET   B 61  ? 0.1458 0.1495 0.1715 -0.0059 -0.0064 0.0046  61  MET   B CA  
4687 C  C   . MET   B 61  ? 0.1450 0.1510 0.1690 -0.0129 -0.0071 0.0111  61  MET   B C   
4688 O  O   . MET   B 61  ? 0.1528 0.1494 0.1659 0.0006  0.0001  -0.0111 61  MET   B O   
4689 C  CB  . MET   B 61  ? 0.1381 0.1503 0.1614 -0.0011 -0.0040 0.0005  61  MET   B CB  
4690 C  CG  . MET   B 61  ? 0.1418 0.1591 0.1565 -0.0007 -0.0048 0.0135  61  MET   B CG  
4691 S  SD  . MET   B 61  ? 0.1462 0.1571 0.1869 -0.0022 -0.0023 -0.0098 61  MET   B SD  
4692 C  CE  . MET   B 61  ? 0.1564 0.1777 0.2110 -0.0003 -0.0018 -0.0133 61  MET   B CE  
4702 N  N   . GLN   B 62  ? 0.1484 0.1576 0.1542 -0.0013 -0.0144 -0.0030 62  GLN   B N   
4703 C  CA  . GLN   B 62  ? 0.1448 0.1618 0.1701 -0.0024 -0.0164 -0.0005 62  GLN   B CA  
4704 C  C   . GLN   B 62  ? 0.1511 0.1669 0.1645 -0.0005 -0.0175 -0.0086 62  GLN   B C   
4705 O  O   . GLN   B 62  ? 0.1643 0.1722 0.1723 -0.0008 -0.0223 -0.0138 62  GLN   B O   
4706 C  CB  . GLN   B 62  ? 0.1489 0.1721 0.1676 0.0013  -0.0152 0.0004  62  GLN   B CB  
4707 C  CG  . GLN   B 62  ? 0.1520 0.1741 0.1818 0.0042  -0.0193 -0.0024 62  GLN   B CG  
4708 C  CD  . GLN   B 62  ? 0.1558 0.1673 0.1737 -0.0030 -0.0235 0.0058  62  GLN   B CD  
4709 O  OE1 . GLN   B 62  ? 0.1597 0.1610 0.1842 0.0018  -0.0311 -0.0100 62  GLN   B OE1 
4710 N  NE2 . GLN   B 62  ? 0.1607 0.1726 0.1951 0.0015  -0.0149 -0.0142 62  GLN   B NE2 
4719 N  N   . VAL   B 63  ? 0.1538 0.1694 0.1866 -0.0091 -0.0187 -0.0192 63  VAL   B N   
4720 C  CA  . VAL   B 63  ? 0.1642 0.1704 0.2156 -0.0122 -0.0255 -0.0048 63  VAL   B CA  
4721 C  C   . VAL   B 63  ? 0.1643 0.1616 0.1894 -0.0176 -0.0287 -0.0219 63  VAL   B C   
4722 O  O   . VAL   B 63  ? 0.1764 0.1630 0.1960 -0.0140 -0.0365 -0.0186 63  VAL   B O   
4723 C  CB  . VAL   B 63  ? 0.1674 0.1891 0.2602 -0.0140 -0.0215 -0.0178 63  VAL   B CB  
4724 C  CG1 . VAL   B 63  ? 0.1809 0.1872 0.2674 -0.0231 -0.0221 -0.0209 63  VAL   B CG1 
4725 C  CG2 . VAL   B 63  ? 0.1568 0.2085 0.2707 -0.0134 -0.0347 -0.0255 63  VAL   B CG2 
4735 N  N   . GLU   B 64  ? 0.1618 0.1558 0.1901 -0.0091 -0.0153 -0.0156 64  GLU   B N   
4736 C  CA  . GLU   B 64  ? 0.1618 0.1502 0.1817 -0.0146 -0.0260 -0.0101 64  GLU   B CA  
4737 C  C   . GLU   B 64  ? 0.1538 0.1520 0.1745 -0.0045 -0.0213 -0.0098 64  GLU   B C   
4738 O  O   . GLU   B 64  ? 0.1647 0.1610 0.1755 -0.0075 -0.0239 -0.0153 64  GLU   B O   
4739 C  CB  . GLU   B 64  ? 0.1646 0.1563 0.1833 -0.0203 -0.0211 -0.0048 64  GLU   B CB  
4740 C  CG  . GLU   B 64  ? 0.1796 0.1586 0.1888 -0.0259 -0.0257 -0.0102 64  GLU   B CG  
4741 C  CD  . GLU   B 64  ? 0.1758 0.1788 0.2074 -0.0307 -0.0208 -0.0032 64  GLU   B CD  
4742 O  OE1 . GLU   B 64  ? 0.1729 0.2008 0.2185 -0.0391 -0.0085 -0.0316 64  GLU   B OE1 
4743 O  OE2 . GLU   B 64  ? 0.1850 0.1854 0.1989 -0.0345 -0.0256 -0.0076 64  GLU   B OE2 
4750 N  N   . SER   B 65  ? 0.1555 0.1445 0.1612 -0.0091 -0.0093 -0.0079 65  SER   B N   
4751 C  CA  . SER   B 65  ? 0.1554 0.1438 0.1679 -0.0022 -0.0132 -0.0145 65  SER   B CA  
4752 C  C   . SER   B 65  ? 0.1575 0.1462 0.1718 0.0025  -0.0168 -0.0168 65  SER   B C   
4753 O  O   . SER   B 65  ? 0.1673 0.1583 0.1661 0.0045  -0.0178 -0.0228 65  SER   B O   
4754 C  CB  . SER   B 65  ? 0.1595 0.1505 0.1773 -0.0074 -0.0181 -0.0162 65  SER   B CB  
4755 O  OG  . SER   B 65  ? 0.1647 0.1559 0.1711 -0.0049 -0.0116 -0.0251 65  SER   B OG  
4761 N  N   . ASP   B 66  ? 0.1654 0.1572 0.1676 -0.0012 -0.0250 -0.0243 66  ASP   B N   
4762 C  CA  . ASP   B 66  ? 0.1763 0.1694 0.1698 0.0035  -0.0307 -0.0203 66  ASP   B CA  
4763 C  C   . ASP   B 66  ? 0.1804 0.1703 0.1684 -0.0084 -0.0245 -0.0246 66  ASP   B C   
4764 O  O   . ASP   B 66  ? 0.1863 0.1739 0.1682 0.0042  -0.0270 -0.0219 66  ASP   B O   
4765 C  CB  . ASP   B 66  ? 0.1873 0.1802 0.1804 0.0121  -0.0405 -0.0202 66  ASP   B CB  
4766 C  CG  . ASP   B 66  ? 0.2159 0.1995 0.2080 0.0210  -0.0551 -0.0070 66  ASP   B CG  
4767 O  OD1 . ASP   B 66  ? 0.2409 0.1926 0.2097 0.0128  -0.0446 0.0024  66  ASP   B OD1 
4768 O  OD2 . ASP   B 66  ? 0.2357 0.2249 0.2752 0.0460  -0.0552 -0.0124 66  ASP   B OD2 
4773 N  N   . ASP   B 67  ? 0.1723 0.1607 0.1700 -0.0073 -0.0269 -0.0201 67  ASP   B N   
4774 C  CA  . ASP   B 67  ? 0.1843 0.1544 0.1766 -0.0079 -0.0234 -0.0155 67  ASP   B CA  
4775 C  C   . ASP   B 67  ? 0.1850 0.1540 0.1838 0.0051  -0.0166 -0.0159 67  ASP   B C   
4776 O  O   . ASP   B 67  ? 0.1942 0.1636 0.1893 0.0006  -0.0151 -0.0264 67  ASP   B O   
4777 C  CB  . ASP   B 67  ? 0.2096 0.1635 0.1949 -0.0152 -0.0310 -0.0113 67  ASP   B CB  
4778 C  CG  . ASP   B 67  ? 0.2522 0.1728 0.2136 -0.0128 -0.0667 -0.0121 67  ASP   B CG  
4779 O  OD1 . ASP   B 67  ? 0.2794 0.1829 0.2288 -0.0159 -0.0718 -0.0085 67  ASP   B OD1 
4780 O  OD2 . ASP   B 67  ? 0.2704 0.1837 0.2389 0.0136  -0.0757 -0.0103 67  ASP   B OD2 
4785 N  N   . TYR   B 68  ? 0.1755 0.1553 0.1712 0.0021  -0.0288 -0.0279 68  TYR   B N   
4786 C  CA  . TYR   B 68  ? 0.1722 0.1732 0.1899 0.0057  -0.0338 -0.0339 68  TYR   B CA  
4787 C  C   . TYR   B 68  ? 0.1649 0.1709 0.1910 0.0010  -0.0292 -0.0372 68  TYR   B C   
4788 O  O   . TYR   B 68  ? 0.1738 0.1803 0.1967 0.0076  -0.0246 -0.0548 68  TYR   B O   
4789 C  CB  . TYR   B 68  ? 0.1755 0.1965 0.2135 0.0078  -0.0350 -0.0465 68  TYR   B CB  
4790 C  CG  . TYR   B 68  ? 0.1898 0.2111 0.2126 0.0155  -0.0365 -0.0682 68  TYR   B CG  
4791 C  CD1 . TYR   B 68  ? 0.1899 0.2196 0.2258 -0.0043 -0.0288 -0.0765 68  TYR   B CD1 
4792 C  CD2 . TYR   B 68  ? 0.1935 0.2317 0.2305 0.0246  -0.0461 -0.0650 68  TYR   B CD2 
4793 C  CE1 . TYR   B 68  ? 0.1945 0.2361 0.2505 -0.0019 -0.0239 -0.0722 68  TYR   B CE1 
4794 C  CE2 . TYR   B 68  ? 0.1948 0.2407 0.2388 0.0218  -0.0352 -0.0827 68  TYR   B CE2 
4795 C  CZ  . TYR   B 68  ? 0.1885 0.2432 0.2521 0.0063  -0.0352 -0.0767 68  TYR   B CZ  
4796 O  OH  . TYR   B 68  ? 0.1894 0.2661 0.2845 0.0024  -0.0208 -0.0593 68  TYR   B OH  
4806 N  N   . ILE   B 69  ? 0.1711 0.1634 0.1862 -0.0013 -0.0301 -0.0358 69  ILE   B N   
4807 C  CA  . ILE   B 69  ? 0.1759 0.1653 0.1879 -0.0025 -0.0194 -0.0375 69  ILE   B CA  
4808 C  C   . ILE   B 69  ? 0.1722 0.1660 0.1786 0.0069  -0.0314 -0.0351 69  ILE   B C   
4809 O  O   . ILE   B 69  ? 0.1847 0.1759 0.1709 0.0070  -0.0196 -0.0414 69  ILE   B O   
4810 C  CB  . ILE   B 69  ? 0.1841 0.1768 0.1977 -0.0015 0.0057  -0.0340 69  ILE   B CB  
4811 C  CG1 . ILE   B 69  ? 0.1863 0.1867 0.2055 -0.0075 0.0214  -0.0325 69  ILE   B CG1 
4812 C  CG2 . ILE   B 69  ? 0.1982 0.1883 0.2167 0.0004  0.0020  -0.0340 69  ILE   B CG2 
4813 C  CD1 . ILE   B 69  ? 0.1835 0.1944 0.2366 -0.0224 0.0232  -0.0364 69  ILE   B CD1 
4825 N  N   . ALA   B 70  ? 0.1718 0.1673 0.1900 0.0044  -0.0407 -0.0286 70  ALA   B N   
4826 C  CA  . ALA   B 70  ? 0.1742 0.1739 0.1661 -0.0005 -0.0423 -0.0219 70  ALA   B CA  
4827 C  C   . ALA   B 70  ? 0.1839 0.1737 0.1861 -0.0001 -0.0411 -0.0334 70  ALA   B C   
4828 O  O   . ALA   B 70  ? 0.1962 0.1760 0.1968 -0.0000 -0.0406 -0.0415 70  ALA   B O   
4829 C  CB  . ALA   B 70  ? 0.1829 0.1883 0.1787 -0.0038 -0.0361 -0.0307 70  ALA   B CB  
4835 N  N   . THR   B 71  ? 0.1885 0.1781 0.1915 0.0063  -0.0471 -0.0376 71  THR   B N   
4836 C  CA  . THR   B 71  ? 0.2028 0.1767 0.2123 0.0155  -0.0562 -0.0299 71  THR   B CA  
4837 C  C   . THR   B 71  ? 0.1971 0.1841 0.2325 0.0286  -0.0475 -0.0448 71  THR   B C   
4838 O  O   . THR   B 71  ? 0.2113 0.1913 0.2725 0.0238  -0.0473 -0.0680 71  THR   B O   
4839 C  CB  . THR   B 71  ? 0.2362 0.2028 0.2390 0.0030  -0.0670 -0.0119 71  THR   B CB  
4840 O  OG1 . THR   B 71  ? 0.2591 0.2314 0.2752 -0.0202 -0.0640 0.0134  71  THR   B OG1 
4841 C  CG2 . THR   B 71  ? 0.2521 0.2012 0.2627 0.0025  -0.0608 -0.0009 71  THR   B CG2 
4849 N  N   . ASN   B 72  ? 0.1812 0.1895 0.2235 0.0147  -0.0502 -0.0663 72  ASN   B N   
4850 C  CA  . ASN   B 72  ? 0.1840 0.2008 0.2312 0.0214  -0.0427 -0.0788 72  ASN   B CA  
4851 C  C   . ASN   B 72  ? 0.1840 0.2110 0.2467 0.0047  -0.0310 -0.0797 72  ASN   B C   
4852 O  O   . ASN   B 72  ? 0.1849 0.2316 0.2730 0.0143  -0.0079 -0.0771 72  ASN   B O   
4853 C  CB  . ASN   B 72  ? 0.1988 0.2165 0.2399 0.0241  -0.0493 -0.0642 72  ASN   B CB  
4854 C  CG  . ASN   B 72  ? 0.2190 0.2278 0.2543 0.0348  -0.0659 -0.0424 72  ASN   B CG  
4855 O  OD1 . ASN   B 72  ? 0.2435 0.2428 0.2661 0.0246  -0.0521 -0.0522 72  ASN   B OD1 
4856 N  ND2 . ASN   B 72  ? 0.2307 0.2335 0.2937 0.0484  -0.0553 -0.0071 72  ASN   B ND2 
4863 N  N   . GLY   B 73  ? 0.1898 0.2050 0.2230 0.0021  -0.0307 -0.0738 73  GLY   B N   
4864 C  CA  . GLY   B 73  ? 0.1862 0.2166 0.2002 -0.0019 -0.0233 -0.0581 73  GLY   B CA  
4865 C  C   . GLY   B 73  ? 0.1760 0.2137 0.1561 0.0020  -0.0224 -0.0465 73  GLY   B C   
4866 O  O   . GLY   B 73  ? 0.1747 0.2027 0.1750 0.0082  -0.0198 -0.0357 73  GLY   B O   
4870 N  N   . PRO   B 74  ? 0.1810 0.2248 0.1468 0.0049  -0.0239 -0.0381 74  PRO   B N   
4871 C  CA  . PRO   B 74  ? 0.1691 0.2249 0.1407 0.0107  -0.0173 -0.0232 74  PRO   B CA  
4872 C  C   . PRO   B 74  ? 0.1587 0.2083 0.1554 0.0059  -0.0116 -0.0212 74  PRO   B C   
4873 O  O   . PRO   B 74  ? 0.1683 0.2095 0.1919 0.0079  -0.0103 -0.0310 74  PRO   B O   
4874 C  CB  . PRO   B 74  ? 0.1898 0.2466 0.1539 -0.0017 -0.0176 -0.0215 74  PRO   B CB  
4875 C  CG  . PRO   B 74  ? 0.2163 0.2577 0.1780 -0.0009 -0.0132 -0.0150 74  PRO   B CG  
4876 C  CD  . PRO   B 74  ? 0.2097 0.2460 0.1643 0.0083  -0.0149 -0.0271 74  PRO   B CD  
4884 N  N   . LEU   B 75  ? 0.1592 0.1945 0.1419 0.0073  -0.0154 -0.0253 75  LEU   B N   
4885 C  CA  . LEU   B 75  ? 0.1640 0.1943 0.1354 0.0036  -0.0086 -0.0018 75  LEU   B CA  
4886 C  C   . LEU   B 75  ? 0.1724 0.2012 0.1328 0.0061  -0.0054 -0.0061 75  LEU   B C   
4887 O  O   . LEU   B 75  ? 0.1847 0.2144 0.1545 -0.0039 -0.0042 0.0029  75  LEU   B O   
4888 C  CB  . LEU   B 75  ? 0.1728 0.1952 0.1252 -0.0056 -0.0215 0.0068  75  LEU   B CB  
4889 C  CG  . LEU   B 75  ? 0.2033 0.2105 0.1591 -0.0328 -0.0084 0.0073  75  LEU   B CG  
4890 C  CD1 . LEU   B 75  ? 0.2403 0.2287 0.1617 -0.0399 0.0183  0.0036  75  LEU   B CD1 
4891 C  CD2 . LEU   B 75  ? 0.2458 0.2311 0.2316 -0.0226 0.0088  0.0091  75  LEU   B CD2 
4903 N  N   . LYS   B 76  ? 0.1701 0.2125 0.1724 0.0013  -0.0036 0.0017  76  LYS   B N   
4904 C  CA  . LYS   B 76  ? 0.1773 0.2200 0.1970 -0.0024 0.0172  -0.0022 76  LYS   B CA  
4905 C  C   . LYS   B 76  ? 0.1707 0.2089 0.1613 0.0045  0.0089  0.0207  76  LYS   B C   
4906 O  O   . LYS   B 76  ? 0.1780 0.1946 0.1679 0.0000  0.0071  0.0116  76  LYS   B O   
4907 C  CB  . LYS   B 76  ? 0.1925 0.2271 0.2631 -0.0069 0.0399  -0.0318 76  LYS   B CB  
4908 C  CG  . LYS   B 76  ? 0.2038 0.2444 0.3066 0.0061  0.0314  -0.0340 76  LYS   B CG  
4909 C  CD  . LYS   B 76  ? 0.2065 0.2488 0.3475 0.0107  0.0190  -0.0445 76  LYS   B CD  
4910 C  CE  . LYS   B 76  ? 0.2128 0.2676 0.4058 0.0179  0.0057  -0.0573 76  LYS   B CE  
4911 N  NZ  . LYS   B 76  ? 0.2117 0.2730 0.4227 0.0147  -0.0145 -0.0811 76  LYS   B NZ  
4925 N  N   . VAL   B 77  ? 0.1772 0.2214 0.1665 0.0100  0.0076  0.0272  77  VAL   B N   
4926 C  CA  . VAL   B 77  ? 0.1822 0.2111 0.1896 0.0123  0.0158  0.0506  77  VAL   B CA  
4927 C  C   . VAL   B 77  ? 0.1638 0.1882 0.1834 0.0125  0.0278  0.0266  77  VAL   B C   
4928 O  O   . VAL   B 77  ? 0.1658 0.1880 0.1718 0.0247  0.0300  0.0209  77  VAL   B O   
4929 C  CB  . VAL   B 77  ? 0.1958 0.2198 0.2281 0.0130  0.0271  0.0658  77  VAL   B CB  
4930 C  CG1 . VAL   B 77  ? 0.1946 0.2098 0.2624 0.0115  0.0281  0.0824  77  VAL   B CG1 
4931 C  CG2 . VAL   B 77  ? 0.2162 0.2395 0.2416 0.0066  0.0020  0.0729  77  VAL   B CG2 
4941 N  N   . GLY   B 78  ? 0.1598 0.1763 0.1866 0.0104  0.0154  0.0304  78  GLY   B N   
4942 C  CA  . GLY   B 78  ? 0.1612 0.1686 0.1693 0.0104  0.0331  0.0175  78  GLY   B CA  
4943 C  C   . GLY   B 78  ? 0.1608 0.1600 0.1668 0.0116  0.0233  0.0255  78  GLY   B C   
4944 O  O   . GLY   B 78  ? 0.1589 0.1612 0.1834 0.0153  0.0220  0.0235  78  GLY   B O   
4948 N  N   . GLY   B 79  ? 0.1518 0.1620 0.1743 0.0125  0.0188  0.0117  79  GLY   B N   
4949 C  CA  . GLY   B 79  ? 0.1554 0.1595 0.1670 0.0122  0.0134  0.0125  79  GLY   B CA  
4950 C  C   . GLY   B 79  ? 0.1443 0.1515 0.1628 0.0187  0.0096  0.0046  79  GLY   B C   
4951 O  O   . GLY   B 79  ? 0.1493 0.1549 0.1731 0.0132  0.0170  0.0223  79  GLY   B O   
4955 N  N   . SER   B 80  ? 0.1437 0.1437 0.1609 0.0103  0.0144  0.0050  80  SER   B N   
4956 C  CA  . SER   B 80  ? 0.1414 0.1446 0.1592 0.0016  0.0007  0.0057  80  SER   B CA  
4957 C  C   . SER   B 80  ? 0.1439 0.1421 0.1584 0.0059  -0.0028 0.0043  80  SER   B C   
4958 O  O   . SER   B 80  ? 0.1537 0.1439 0.1884 0.0111  0.0057  -0.0013 80  SER   B O   
4959 C  CB  . SER   B 80  ? 0.1479 0.1523 0.1780 -0.0035 0.0038  0.0108  80  SER   B CB  
4960 O  OG  . SER   B 80  ? 0.1546 0.1659 0.1797 0.0015  -0.0145 0.0062  80  SER   B OG  
4966 N  N   . CYS   B 81  ? 0.1430 0.1319 0.1672 0.0057  -0.0059 -0.0037 81  CYS   B N   
4967 C  CA  . CYS   B 81  ? 0.1446 0.1319 0.1657 0.0008  -0.0087 -0.0045 81  CYS   B CA  
4968 C  C   . CYS   B 81  ? 0.1465 0.1316 0.1437 0.0022  -0.0146 -0.0043 81  CYS   B C   
4969 O  O   . CYS   B 81  ? 0.1694 0.1284 0.1634 0.0038  -0.0084 -0.0122 81  CYS   B O   
4970 C  CB  . CYS   B 81  ? 0.1600 0.1469 0.1663 -0.0053 -0.0089 0.0013  81  CYS   B CB  
4971 S  SG  . CYS   B 81  ? 0.1615 0.1647 0.1621 -0.0032 -0.0199 -0.0093 81  CYS   B SG  
4977 N  N   . VAL   B 82  ? 0.1448 0.1319 0.1550 0.0010  -0.0112 -0.0030 82  VAL   B N   
4978 C  CA  . VAL   B 82  ? 0.1580 0.1323 0.1545 -0.0061 -0.0039 0.0006  82  VAL   B CA  
4979 C  C   . VAL   B 82  ? 0.1603 0.1288 0.1675 -0.0115 -0.0004 -0.0019 82  VAL   B C   
4980 O  O   . VAL   B 82  ? 0.1658 0.1316 0.2014 -0.0102 -0.0030 -0.0157 82  VAL   B O   
4981 C  CB  . VAL   B 82  ? 0.1641 0.1571 0.1667 -0.0030 -0.0098 0.0134  82  VAL   B CB  
4982 C  CG1 . VAL   B 82  ? 0.1832 0.1750 0.1758 -0.0021 -0.0164 0.0180  82  VAL   B CG1 
4983 C  CG2 . VAL   B 82  ? 0.1704 0.1698 0.1926 -0.0062 -0.0222 0.0177  82  VAL   B CG2 
4993 N  N   . LEU   B 83  ? 0.1465 0.1300 0.1617 -0.0152 -0.0154 -0.0055 83  LEU   B N   
4994 C  CA  . LEU   B 83  ? 0.1448 0.1307 0.1530 -0.0120 -0.0178 -0.0011 83  LEU   B CA  
4995 C  C   . LEU   B 83  ? 0.1460 0.1292 0.1627 -0.0180 -0.0110 0.0001  83  LEU   B C   
4996 O  O   . LEU   B 83  ? 0.1579 0.1394 0.1480 -0.0182 -0.0113 0.0030  83  LEU   B O   
4997 C  CB  . LEU   B 83  ? 0.1516 0.1463 0.1616 -0.0118 -0.0167 -0.0135 83  LEU   B CB  
4998 C  CG  . LEU   B 83  ? 0.1720 0.1684 0.1628 -0.0157 -0.0084 -0.0114 83  LEU   B CG  
4999 C  CD1 . LEU   B 83  ? 0.1891 0.1742 0.1656 -0.0160 -0.0115 0.0046  83  LEU   B CD1 
5000 C  CD2 . LEU   B 83  ? 0.1956 0.1754 0.1739 -0.0019 -0.0118 -0.0262 83  LEU   B CD2 
5012 N  N   . SER   B 84  ? 0.1552 0.1452 0.1813 -0.0249 -0.0067 -0.0034 84  SER   B N   
5013 C  CA  . SER   B 84  ? 0.1547 0.1641 0.1628 -0.0315 -0.0051 0.0086  84  SER   B CA  
5014 C  C   . SER   B 84  ? 0.1492 0.1777 0.1285 -0.0186 -0.0101 0.0182  84  SER   B C   
5015 O  O   . SER   B 84  ? 0.1621 0.1667 0.1303 -0.0129 -0.0074 0.0022  84  SER   B O   
5016 C  CB  . SER   B 84  ? 0.1812 0.1686 0.2174 -0.0283 0.0151  0.0154  84  SER   B CB  
5017 O  OG  . SER   B 84  ? 0.1766 0.1842 0.2681 -0.0327 0.0159  0.0195  84  SER   B OG  
5023 N  N   . GLY   B 85  ? 0.1534 0.1976 0.1438 -0.0214 -0.0092 0.0210  85  GLY   B N   
5024 C  CA  . GLY   B 85  ? 0.1587 0.2036 0.1768 -0.0320 0.0029  -0.0049 85  GLY   B CA  
5025 C  C   . GLY   B 85  ? 0.1549 0.1855 0.1449 -0.0397 -0.0013 0.0060  85  GLY   B C   
5026 O  O   . GLY   B 85  ? 0.1613 0.1847 0.1556 -0.0517 0.0146  -0.0124 85  GLY   B O   
5030 N  N   . HIS   B 86  ? 0.1490 0.1682 0.1660 -0.0246 -0.0095 0.0096  86  HIS   B N   
5031 C  CA  . HIS   B 86  ? 0.1514 0.1708 0.1713 -0.0305 -0.0152 0.0112  86  HIS   B CA  
5032 C  C   . HIS   B 86  ? 0.1574 0.1797 0.1631 -0.0436 -0.0064 0.0323  86  HIS   B C   
5033 O  O   . HIS   B 86  ? 0.1678 0.1903 0.1683 -0.0262 0.0132  0.0218  86  HIS   B O   
5034 C  CB  . HIS   B 86  ? 0.1632 0.1771 0.1640 -0.0204 -0.0270 -0.0045 86  HIS   B CB  
5035 C  CG  . HIS   B 86  ? 0.1631 0.1829 0.1629 -0.0116 -0.0204 0.0078  86  HIS   B CG  
5036 N  ND1 . HIS   B 86  ? 0.1741 0.2079 0.1928 -0.0233 -0.0191 -0.0149 86  HIS   B ND1 
5037 C  CD2 . HIS   B 86  ? 0.1579 0.1880 0.1832 -0.0114 -0.0226 0.0080  86  HIS   B CD2 
5038 C  CE1 . HIS   B 86  ? 0.1784 0.2063 0.1810 -0.0132 -0.0056 -0.0295 86  HIS   B CE1 
5039 N  NE2 . HIS   B 86  ? 0.1714 0.1988 0.1794 0.0010  -0.0139 -0.0017 86  HIS   B NE2 
5047 N  N   . ASN   B 87  ? 0.1588 0.1814 0.1722 -0.0280 -0.0049 0.0172  87  ASN   B N   
5048 C  CA  . ASN   B 87  ? 0.1700 0.2017 0.1750 -0.0263 0.0191  0.0159  87  ASN   B CA  
5049 C  C   . ASN   B 87  ? 0.1848 0.1836 0.1565 -0.0242 0.0287  0.0138  87  ASN   B C   
5050 O  O   . ASN   B 87  ? 0.2050 0.1951 0.1906 -0.0227 0.0490  0.0059  87  ASN   B O   
5051 C  CB  . ASN   B 87  ? 0.1727 0.2383 0.2040 -0.0188 0.0277  0.0182  87  ASN   B CB  
5052 C  CG  . ASN   B 87  ? 0.1742 0.2574 0.2106 0.0133  0.0374  0.0338  87  ASN   B CG  
5053 O  OD1 . ASN   B 87  ? 0.1680 0.2378 0.1943 0.0193  0.0455  0.0464  87  ASN   B OD1 
5054 N  ND2 . ASN   B 87  ? 0.2098 0.2767 0.2570 0.0183  0.0503  0.0269  87  ASN   B ND2 
5061 N  N   . LEU   B 88  ? 0.1712 0.1719 0.1452 -0.0264 0.0155  0.0171  88  LEU   B N   
5062 C  CA  . LEU   B 88  ? 0.1799 0.1607 0.1561 -0.0318 0.0045  0.0005  88  LEU   B CA  
5063 C  C   . LEU   B 88  ? 0.1844 0.1512 0.1552 -0.0323 0.0013  -0.0010 88  LEU   B C   
5064 O  O   . LEU   B 88  ? 0.2086 0.1602 0.1893 -0.0210 -0.0198 -0.0092 88  LEU   B O   
5065 C  CB  . LEU   B 88  ? 0.1874 0.1665 0.1676 -0.0412 -0.0040 0.0138  88  LEU   B CB  
5066 C  CG  . LEU   B 88  ? 0.2252 0.2039 0.1748 -0.0354 -0.0285 0.0269  88  LEU   B CG  
5067 C  CD1 . LEU   B 88  ? 0.2401 0.2376 0.2011 -0.0488 -0.0197 0.0460  88  LEU   B CD1 
5068 C  CD2 . LEU   B 88  ? 0.2641 0.2357 0.2449 0.0041  -0.0583 0.0084  88  LEU   B CD2 
5080 N  N   . ALA   B 89  ? 0.1654 0.1541 0.1495 -0.0352 0.0219  -0.0061 89  ALA   B N   
5081 C  CA  . ALA   B 89  ? 0.1590 0.1464 0.1332 -0.0332 0.0079  0.0065  89  ALA   B CA  
5082 C  C   . ALA   B 89  ? 0.1685 0.1505 0.1483 -0.0394 0.0155  0.0046  89  ALA   B C   
5083 O  O   . ALA   B 89  ? 0.1473 0.1611 0.1839 -0.0360 0.0105  -0.0230 89  ALA   B O   
5084 C  CB  . ALA   B 89  ? 0.1507 0.1523 0.1410 -0.0340 0.0104  0.0093  89  ALA   B CB  
5090 N  N   . LYS   B 90  ? 0.2020 0.1454 0.1476 -0.0461 -0.0064 0.0092  90  LYS   B N   
5091 C  CA  . LYS   B 90  ? 0.2170 0.1440 0.1368 -0.0447 -0.0092 0.0101  90  LYS   B CA  
5092 C  C   . LYS   B 90  ? 0.1996 0.1317 0.1550 -0.0340 -0.0139 -0.0015 90  LYS   B C   
5093 O  O   . LYS   B 90  ? 0.2036 0.1468 0.1650 -0.0480 -0.0019 0.0045  90  LYS   B O   
5094 C  CB  . LYS   B 90  ? 0.2355 0.1543 0.1686 -0.0374 -0.0043 0.0174  90  LYS   B CB  
5095 C  CG  . LYS   B 90  ? 0.2342 0.1739 0.1678 -0.0243 0.0110  0.0053  90  LYS   B CG  
5096 C  CD  . LYS   B 90  ? 0.2656 0.2034 0.2294 -0.0109 0.0351  -0.0022 90  LYS   B CD  
5097 C  CE  . LYS   B 90  ? 0.2754 0.2205 0.2927 -0.0174 0.0475  -0.0039 90  LYS   B CE  
5098 N  NZ  . LYS   B 90  ? 0.2824 0.2091 0.2840 -0.0333 0.0741  0.0043  90  LYS   B NZ  
5112 N  N   . HIS   B 91  ? 0.1684 0.1235 0.1362 -0.0319 -0.0130 0.0146  91  HIS   B N   
5113 C  CA  . HIS   B 91  ? 0.1598 0.1319 0.1528 -0.0293 -0.0148 -0.0023 91  HIS   B CA  
5114 C  C   . HIS   B 91  ? 0.1494 0.1290 0.1344 -0.0272 -0.0019 0.0053  91  HIS   B C   
5115 O  O   . HIS   B 91  ? 0.1635 0.1383 0.1385 -0.0277 -0.0186 0.0016  91  HIS   B O   
5116 C  CB  . HIS   B 91  ? 0.1786 0.1380 0.1847 -0.0131 -0.0095 0.0093  91  HIS   B CB  
5117 C  CG  . HIS   B 91  ? 0.2177 0.1561 0.2399 0.0025  0.0213  0.0218  91  HIS   B CG  
5118 N  ND1 . HIS   B 91  ? 0.2510 0.1570 0.3122 0.0030  0.0317  0.0144  91  HIS   B ND1 
5119 C  CD2 . HIS   B 91  ? 0.2369 0.1881 0.3067 0.0208  0.0078  0.0477  91  HIS   B CD2 
5120 C  CE1 . HIS   B 91  ? 0.2570 0.1764 0.3386 0.0221  0.0330  0.0175  91  HIS   B CE1 
5121 N  NE2 . HIS   B 91  ? 0.2502 0.1928 0.3478 0.0294  0.0338  0.0538  91  HIS   B NE2 
5129 N  N   . CYS   B 92  ? 0.1468 0.1330 0.1320 -0.0248 -0.0094 0.0034  92  CYS   B N   
5130 C  CA  . CYS   B 92  ? 0.1457 0.1296 0.1319 -0.0187 -0.0069 0.0013  92  CYS   B CA  
5131 C  C   . CYS   B 92  ? 0.1420 0.1209 0.1321 -0.0132 -0.0110 -0.0005 92  CYS   B C   
5132 O  O   . CYS   B 92  ? 0.1453 0.1343 0.1480 -0.0131 -0.0060 0.0066  92  CYS   B O   
5133 C  CB  . CYS   B 92  ? 0.1483 0.1397 0.1408 -0.0126 -0.0032 -0.0045 92  CYS   B CB  
5134 S  SG  . CYS   B 92  ? 0.1464 0.1398 0.1493 -0.0111 -0.0086 0.0094  92  CYS   B SG  
5140 N  N   . LEU   B 93  ? 0.1360 0.1225 0.1381 -0.0071 -0.0064 -0.0077 93  LEU   B N   
5141 C  CA  . LEU   B 93  ? 0.1366 0.1304 0.1376 -0.0005 -0.0091 -0.0011 93  LEU   B CA  
5142 C  C   . LEU   B 93  ? 0.1267 0.1256 0.1235 -0.0040 -0.0077 0.0064  93  LEU   B C   
5143 O  O   . LEU   B 93  ? 0.1362 0.1276 0.1427 -0.0052 -0.0057 0.0026  93  LEU   B O   
5144 C  CB  . LEU   B 93  ? 0.1364 0.1285 0.1411 0.0023  -0.0112 0.0073  93  LEU   B CB  
5145 C  CG  . LEU   B 93  ? 0.1359 0.1409 0.1641 -0.0026 -0.0078 0.0107  93  LEU   B CG  
5146 C  CD1 . LEU   B 93  ? 0.1376 0.1538 0.1722 0.0093  -0.0001 -0.0051 93  LEU   B CD1 
5147 C  CD2 . LEU   B 93  ? 0.1350 0.1390 0.1700 -0.0028 -0.0143 0.0009  93  LEU   B CD2 
5159 N  N   . HIS   B 94  ? 0.1390 0.1220 0.1230 -0.0041 -0.0150 0.0063  94  HIS   B N   
5160 C  CA  . HIS   B 94  ? 0.1371 0.1228 0.1287 -0.0016 -0.0008 0.0017  94  HIS   B CA  
5161 C  C   . HIS   B 94  ? 0.1280 0.1298 0.1498 -0.0020 -0.0049 0.0070  94  HIS   B C   
5162 O  O   . HIS   B 94  ? 0.1339 0.1382 0.1894 -0.0032 0.0191  -0.0079 94  HIS   B O   
5163 C  CB  . HIS   B 94  ? 0.1348 0.1269 0.1406 0.0005  0.0012  0.0004  94  HIS   B CB  
5164 C  CG  . HIS   B 94  ? 0.1311 0.1265 0.1470 -0.0077 -0.0128 -0.0008 94  HIS   B CG  
5165 N  ND1 . HIS   B 94  ? 0.1398 0.1355 0.1381 -0.0081 -0.0190 -0.0009 94  HIS   B ND1 
5166 C  CD2 . HIS   B 94  ? 0.1372 0.1290 0.1428 0.0004  -0.0010 0.0016  94  HIS   B CD2 
5167 C  CE1 . HIS   B 94  ? 0.1477 0.1347 0.1421 -0.0068 -0.0245 0.0001  94  HIS   B CE1 
5168 N  NE2 . HIS   B 94  ? 0.1387 0.1399 0.1465 -0.0116 -0.0125 0.0047  94  HIS   B NE2 
5176 N  N   . VAL   B 95  ? 0.1217 0.1236 0.1613 -0.0030 -0.0027 0.0051  95  VAL   B N   
5177 C  CA  . VAL   B 95  ? 0.1294 0.1344 0.1413 -0.0011 0.0089  0.0106  95  VAL   B CA  
5178 C  C   . VAL   B 95  ? 0.1390 0.1361 0.1396 0.0008  0.0114  0.0056  95  VAL   B C   
5179 O  O   . VAL   B 95  ? 0.1407 0.1305 0.1661 0.0071  0.0074  0.0143  95  VAL   B O   
5180 C  CB  . VAL   B 95  ? 0.1403 0.1297 0.1430 -0.0012 -0.0090 0.0006  95  VAL   B CB  
5181 C  CG1 . VAL   B 95  ? 0.1468 0.1485 0.1719 -0.0052 0.0046  0.0108  95  VAL   B CG1 
5182 C  CG2 . VAL   B 95  ? 0.1429 0.1305 0.1466 0.0026  -0.0102 0.0034  95  VAL   B CG2 
5192 N  N   . VAL   B 96  ? 0.1493 0.1365 0.1481 0.0105  0.0105  0.0126  96  VAL   B N   
5193 C  CA  . VAL   B 96  ? 0.1592 0.1484 0.1362 0.0074  0.0066  0.0173  96  VAL   B CA  
5194 C  C   . VAL   B 96  ? 0.1552 0.1467 0.1611 0.0036  0.0177  0.0156  96  VAL   B C   
5195 O  O   . VAL   B 96  ? 0.1535 0.1562 0.1696 0.0026  0.0146  0.0111  96  VAL   B O   
5196 C  CB  . VAL   B 96  ? 0.1610 0.1724 0.1299 0.0086  0.0030  0.0088  96  VAL   B CB  
5197 C  CG1 . VAL   B 96  ? 0.1577 0.1904 0.1498 0.0180  0.0075  -0.0060 96  VAL   B CG1 
5198 C  CG2 . VAL   B 96  ? 0.1689 0.1720 0.1422 0.0027  0.0130  -0.0014 96  VAL   B CG2 
5208 N  N   . GLY   B 97  ? 0.1638 0.1502 0.1486 0.0037  0.0081  0.0255  97  GLY   B N   
5209 C  CA  . GLY   B 97  ? 0.1841 0.1496 0.1541 0.0050  0.0100  0.0189  97  GLY   B CA  
5210 C  C   . GLY   B 97  ? 0.1981 0.1659 0.1759 0.0127  0.0133  0.0240  97  GLY   B C   
5211 O  O   . GLY   B 97  ? 0.2112 0.1730 0.1751 0.0099  0.0016  0.0159  97  GLY   B O   
5215 N  N   . PRO   B 98  ? 0.2094 0.1676 0.1843 0.0149  0.0439  0.0375  98  PRO   B N   
5216 C  CA  . PRO   B 98  ? 0.2283 0.1841 0.1945 0.0274  0.0539  0.0340  98  PRO   B CA  
5217 C  C   . PRO   B 98  ? 0.2396 0.1874 0.1794 0.0396  0.0564  0.0518  98  PRO   B C   
5218 O  O   . PRO   B 98  ? 0.2253 0.1787 0.1929 0.0363  0.0541  0.0465  98  PRO   B O   
5219 C  CB  . PRO   B 98  ? 0.2231 0.1960 0.2144 0.0221  0.0677  0.0445  98  PRO   B CB  
5220 C  CG  . PRO   B 98  ? 0.2109 0.1887 0.2191 0.0153  0.0588  0.0497  98  PRO   B CG  
5221 C  CD  . PRO   B 98  ? 0.1924 0.1708 0.2129 0.0185  0.0532  0.0459  98  PRO   B CD  
5229 N  N   . ASN   B 99  ? 0.2511 0.2053 0.1965 0.0578  0.0552  0.0419  99  ASN   B N   
5230 C  CA  . ASN   B 99  ? 0.2723 0.2128 0.1905 0.0703  0.0509  0.0547  99  ASN   B CA  
5231 C  C   . ASN   B 99  ? 0.3025 0.2473 0.2061 0.0771  0.0843  0.0783  99  ASN   B C   
5232 O  O   . ASN   B 99  ? 0.3325 0.2617 0.2233 0.0756  0.0786  0.0843  99  ASN   B O   
5233 C  CB  . ASN   B 99  ? 0.2845 0.2141 0.1998 0.0635  0.0292  0.0528  99  ASN   B CB  
5234 C  CG  . ASN   B 99  ? 0.2861 0.2228 0.2115 0.0589  0.0236  0.0409  99  ASN   B CG  
5235 O  OD1 . ASN   B 99  ? 0.2843 0.2208 0.2357 0.0661  0.0321  0.0475  99  ASN   B OD1 
5236 N  ND2 . ASN   B 99  ? 0.2858 0.2254 0.2179 0.0615  -0.0030 0.0198  99  ASN   B ND2 
5243 N  N   . VAL   B 100 ? 0.3251 0.2593 0.2726 0.0644  0.0854  0.1064  100 VAL   B N   
5244 C  CA  . VAL   B 100 ? 0.3535 0.2830 0.3381 0.0508  0.0863  0.1228  100 VAL   B CA  
5245 C  C   . VAL   B 100 ? 0.3833 0.2903 0.3187 0.0598  0.0851  0.1502  100 VAL   B C   
5246 O  O   . VAL   B 100 ? 0.3947 0.3096 0.3421 0.0583  0.1023  0.1379  100 VAL   B O   
5247 C  CB  . VAL   B 100 ? 0.3572 0.2999 0.4203 0.0206  0.0850  0.1262  100 VAL   B CB  
5248 C  CG1 . VAL   B 100 ? 0.3626 0.3087 0.4468 0.0196  0.0896  0.1209  100 VAL   B CG1 
5249 C  CG2 . VAL   B 100 ? 0.3543 0.3061 0.4443 0.0050  0.0840  0.1344  100 VAL   B CG2 
5259 N  N   . ASN   B 101 ? 0.4037 0.2989 0.3133 0.0650  0.0594  0.1580  101 ASN   B N   
5260 C  CA  . ASN   B 101 ? 0.4384 0.3215 0.3253 0.0613  0.0278  0.1592  101 ASN   B CA  
5261 C  C   . ASN   B 101 ? 0.4906 0.3707 0.3428 0.0545  0.0118  0.1563  101 ASN   B C   
5262 O  O   . ASN   B 101 ? 0.4951 0.3826 0.3640 0.0644  0.0142  0.1269  101 ASN   B O   
5263 C  CB  . ASN   B 101 ? 0.4231 0.3035 0.3368 0.0573  0.0220  0.1450  101 ASN   B CB  
5264 C  CG  . ASN   B 101 ? 0.4093 0.2835 0.3343 0.0538  0.0258  0.1508  101 ASN   B CG  
5265 O  OD1 . ASN   B 101 ? 0.4067 0.2851 0.3635 0.0432  0.0549  0.1369  101 ASN   B OD1 
5266 N  ND2 . ASN   B 101 ? 0.4025 0.2803 0.3250 0.0539  0.0174  0.1328  101 ASN   B ND2 
5273 N  N   A LYS   B 102 ? 0.5165 0.3931 0.3633 0.0420  0.0141  0.1504  102 LYS   B N   
5274 N  N   B LYS   B 102 ? 0.5108 0.3948 0.3678 0.0432  0.0099  0.1439  102 LYS   B N   
5275 C  CA  A LYS   B 102 ? 0.5395 0.4227 0.3874 0.0258  0.0206  0.1248  102 LYS   B CA  
5276 C  CA  B LYS   B 102 ? 0.5284 0.4203 0.3923 0.0304  0.0133  0.1224  102 LYS   B CA  
5277 C  C   A LYS   B 102 ? 0.5400 0.4270 0.3627 0.0261  0.0251  0.1278  102 LYS   B C   
5278 C  C   B LYS   B 102 ? 0.5316 0.4251 0.3747 0.0274  0.0236  0.1269  102 LYS   B C   
5279 O  O   A LYS   B 102 ? 0.5497 0.4315 0.3776 0.0258  0.0115  0.1195  102 LYS   B O   
5280 O  O   B LYS   B 102 ? 0.5366 0.4284 0.3870 0.0263  0.0144  0.1232  102 LYS   B O   
5281 C  CB  A LYS   B 102 ? 0.5574 0.4456 0.4500 0.0111  0.0313  0.0862  102 LYS   B CB  
5282 C  CB  B LYS   B 102 ? 0.5397 0.4385 0.4396 0.0222  0.0126  0.0907  102 LYS   B CB  
5283 C  CG  A LYS   B 102 ? 0.5723 0.4661 0.5075 -0.0005 0.0418  0.0512  102 LYS   B CG  
5284 C  CG  B LYS   B 102 ? 0.5484 0.4538 0.4812 0.0163  0.0134  0.0617  102 LYS   B CG  
5285 C  CD  A LYS   B 102 ? 0.5868 0.4836 0.5662 -0.0088 0.0535  0.0260  102 LYS   B CD  
5286 C  CD  B LYS   B 102 ? 0.5563 0.4666 0.5224 0.0121  0.0164  0.0388  102 LYS   B CD  
5287 C  CE  A LYS   B 102 ? 0.5976 0.4957 0.6090 -0.0150 0.0610  0.0058  102 LYS   B CE  
5288 C  CE  B LYS   B 102 ? 0.5619 0.4756 0.5520 0.0093  0.0178  0.0209  102 LYS   B CE  
5289 N  NZ  A LYS   B 102 ? 0.6039 0.5031 0.6349 -0.0173 0.0622  -0.0064 102 LYS   B NZ  
5290 N  NZ  B LYS   B 102 ? 0.5653 0.4808 0.5706 0.0081  0.0171  0.0102  102 LYS   B NZ  
5317 N  N   . GLY   B 103 ? 0.5275 0.4240 0.3578 0.0266  0.0454  0.1270  103 GLY   B N   
5318 C  CA  . GLY   B 103 ? 0.5093 0.4213 0.3656 0.0320  0.0764  0.1005  103 GLY   B CA  
5319 C  C   . GLY   B 103 ? 0.4862 0.4115 0.3564 0.0348  0.1046  0.0777  103 GLY   B C   
5320 O  O   . GLY   B 103 ? 0.4930 0.4202 0.3692 0.0335  0.1088  0.0792  103 GLY   B O   
5325 N  N   A GLU   B 104 ? 0.4642 0.3957 0.3347 0.0449  0.1310  0.0642  104 GLU   B N   
5326 N  N   B GLU   B 104 ? 0.4751 0.4054 0.3589 0.0289  0.0985  0.0598  104 GLU   B N   
5327 C  CA  A GLU   B 104 ? 0.4402 0.3813 0.3068 0.0575  0.1519  0.0529  104 GLU   B CA  
5328 C  CA  B GLU   B 104 ? 0.4623 0.3984 0.3534 0.0238  0.0938  0.0429  104 GLU   B CA  
5329 C  C   A GLU   B 104 ? 0.4404 0.3873 0.3287 0.0415  0.1904  0.0599  104 GLU   B C   
5330 C  C   B GLU   B 104 ? 0.4596 0.3983 0.3685 0.0170  0.1156  0.0429  104 GLU   B C   
5331 O  O   A GLU   B 104 ? 0.4457 0.3932 0.3577 0.0352  0.1884  0.0588  104 GLU   B O   
5332 O  O   B GLU   B 104 ? 0.4615 0.4011 0.3805 0.0144  0.1137  0.0400  104 GLU   B O   
5333 C  CB  A GLU   B 104 ? 0.4234 0.3636 0.2973 0.0865  0.1124  0.0238  104 GLU   B CB  
5334 C  CB  B GLU   B 104 ? 0.4543 0.3914 0.3408 0.0256  0.0659  0.0228  104 GLU   B CB  
5335 C  CG  A GLU   B 104 ? 0.4091 0.3531 0.2843 0.1135  0.0642  -0.0070 104 GLU   B CG  
5336 C  CG  B GLU   B 104 ? 0.4480 0.3865 0.3279 0.0278  0.0375  0.0010  104 GLU   B CG  
5337 C  CD  A GLU   B 104 ? 0.3978 0.3464 0.2592 0.1351  0.0234  -0.0289 104 GLU   B CD  
5338 C  CD  B GLU   B 104 ? 0.4438 0.3829 0.3132 0.0289  0.0140  -0.0168 104 GLU   B CD  
5339 O  OE1 A GLU   B 104 ? 0.3858 0.3380 0.2112 0.1475  0.0256  -0.0233 104 GLU   B OE1 
5340 O  OE1 B GLU   B 104 ? 0.4411 0.3797 0.2968 0.0283  0.0102  -0.0190 104 GLU   B OE1 
5341 O  OE2 A GLU   B 104 ? 0.3995 0.3551 0.2675 0.1334  -0.0140 -0.0420 104 GLU   B OE2 
5342 O  OE2 B GLU   B 104 ? 0.4433 0.3840 0.3125 0.0288  -0.0025 -0.0278 104 GLU   B OE2 
5355 N  N   A ASP   B 105 ? 0.4335 0.3875 0.3326 0.0314  0.2129  0.0696  105 ASP   B N   
5356 N  N   B ASP   B 105 ? 0.4532 0.3945 0.3716 0.0130  0.1360  0.0470  105 ASP   B N   
5357 C  CA  A ASP   B 105 ? 0.4318 0.3901 0.3569 0.0227  0.2275  0.0595  105 ASP   B CA  
5358 C  CA  B ASP   B 105 ? 0.4484 0.3899 0.3823 0.0101  0.1527  0.0455  105 ASP   B CA  
5359 C  C   A ASP   B 105 ? 0.4149 0.3600 0.3347 0.0176  0.2151  0.0554  105 ASP   B C   
5360 C  C   B ASP   B 105 ? 0.4316 0.3657 0.3588 0.0102  0.1779  0.0509  105 ASP   B C   
5361 O  O   A ASP   B 105 ? 0.3952 0.3490 0.3281 0.0183  0.2081  0.0561  105 ASP   B O   
5362 O  O   B ASP   B 105 ? 0.4295 0.3654 0.3491 0.0102  0.1822  0.0536  105 ASP   B O   
5363 C  CB  A ASP   B 105 ? 0.4454 0.4175 0.4248 0.0264  0.2441  0.0440  105 ASP   B CB  
5364 C  CB  B ASP   B 105 ? 0.4571 0.4053 0.4168 0.0090  0.1446  0.0374  105 ASP   B CB  
5365 C  CG  A ASP   B 105 ? 0.4553 0.4398 0.4858 0.0261  0.2646  0.0336  105 ASP   B CG  
5366 C  CG  B ASP   B 105 ? 0.4645 0.4166 0.4509 0.0066  0.1413  0.0328  105 ASP   B CG  
5367 O  OD1 A ASP   B 105 ? 0.4522 0.4451 0.4824 0.0168  0.2774  0.0451  105 ASP   B OD1 
5368 O  OD1 B ASP   B 105 ? 0.4658 0.4206 0.4609 0.0030  0.1417  0.0345  105 ASP   B OD1 
5369 O  OD2 A ASP   B 105 ? 0.4637 0.4521 0.5315 0.0331  0.2580  0.0186  105 ASP   B OD2 
5370 O  OD2 B ASP   B 105 ? 0.4670 0.4212 0.4626 0.0069  0.1406  0.0313  105 ASP   B OD2 
5379 N  N   . ILE   B 106 ? 0.4138 0.3372 0.3531 0.0122  0.1887  0.0563  106 ILE   B N   
5380 C  CA  . ILE   B 106 ? 0.3808 0.2887 0.3678 0.0062  0.1858  0.0477  106 ILE   B CA  
5381 C  C   . ILE   B 106 ? 0.3353 0.2751 0.3638 0.0095  0.1767  0.0313  106 ILE   B C   
5382 O  O   . ILE   B 106 ? 0.3277 0.2416 0.3742 0.0042  0.1686  0.0378  106 ILE   B O   
5383 C  CB  . ILE   B 106 ? 0.4011 0.2698 0.3864 -0.0069 0.1765  0.0539  106 ILE   B CB  
5384 C  CG1 . ILE   B 106 ? 0.4113 0.2634 0.3895 0.0063  0.1618  0.0460  106 ILE   B CG1 
5385 C  CG2 . ILE   B 106 ? 0.4083 0.2738 0.4164 -0.0201 0.1764  0.0537  106 ILE   B CG2 
5386 C  CD1 . ILE   B 106 ? 0.4152 0.2623 0.3758 0.0180  0.1550  0.0502  106 ILE   B CD1 
5399 N  N   A GLN   B 107 ? 0.3201 0.2929 0.3855 0.0006  0.1732  0.0276  107 GLN   B N   
5400 N  N   B GLN   B 107 ? 0.3262 0.2908 0.3728 0.0045  0.1574  0.0232  107 GLN   B N   
5401 C  CA  A GLN   B 107 ? 0.3012 0.3088 0.3885 -0.0120 0.1630  0.0235  107 GLN   B CA  
5402 C  CA  B GLN   B 107 ? 0.3142 0.3037 0.3748 -0.0010 0.1350  0.0172  107 GLN   B CA  
5403 C  C   A GLN   B 107 ? 0.2722 0.2865 0.3580 -0.0088 0.1245  0.0116  107 GLN   B C   
5404 C  C   B GLN   B 107 ? 0.2830 0.2877 0.3435 0.0016  0.1194  0.0106  107 GLN   B C   
5405 O  O   A GLN   B 107 ? 0.2578 0.2887 0.4026 -0.0060 0.0864  -0.0160 107 GLN   B O   
5406 O  O   B GLN   B 107 ? 0.2799 0.2929 0.3632 0.0017  0.1008  -0.0042 107 GLN   B O   
5407 C  CB  A GLN   B 107 ? 0.3361 0.3563 0.4531 -0.0165 0.1452  0.0231  107 GLN   B CB  
5408 C  CB  B GLN   B 107 ? 0.3415 0.3355 0.4217 -0.0049 0.1130  0.0158  107 GLN   B CB  
5409 C  CG  A GLN   B 107 ? 0.3733 0.3987 0.5190 -0.0177 0.1086  0.0230  107 GLN   B CG  
5410 C  CG  B GLN   B 107 ? 0.3670 0.3622 0.4691 -0.0073 0.0845  0.0154  107 GLN   B CG  
5411 C  CD  A GLN   B 107 ? 0.3995 0.4313 0.5712 -0.0225 0.0812  0.0276  107 GLN   B CD  
5412 C  CD  B GLN   B 107 ? 0.3857 0.3823 0.5077 -0.0111 0.0623  0.0170  107 GLN   B CD  
5413 O  OE1 A GLN   B 107 ? 0.4082 0.4413 0.5882 -0.0256 0.0812  0.0256  107 GLN   B OE1 
5414 O  OE1 B GLN   B 107 ? 0.3931 0.3896 0.5192 -0.0137 0.0602  0.0159  107 GLN   B OE1 
5415 N  NE2 A GLN   B 107 ? 0.4095 0.4386 0.5891 -0.0201 0.0640  0.0339  107 GLN   B NE2 
5416 N  NE2 B GLN   B 107 ? 0.3922 0.3890 0.5220 -0.0103 0.0512  0.0199  107 GLN   B NE2 
5433 N  N   . LEU   B 108 ? 0.2500 0.2661 0.3124 0.0137  0.1190  0.0115  108 LEU   B N   
5434 C  CA  . LEU   B 108 ? 0.2267 0.2417 0.2642 0.0316  0.0836  0.0282  108 LEU   B CA  
5435 C  C   . LEU   B 108 ? 0.1921 0.1972 0.2422 0.0247  0.0464  0.0313  108 LEU   B C   
5436 O  O   . LEU   B 108 ? 0.1859 0.1841 0.2312 0.0190  0.0303  0.0248  108 LEU   B O   
5437 C  CB  . LEU   B 108 ? 0.2458 0.2686 0.2475 0.0351  0.0789  0.0404  108 LEU   B CB  
5438 C  CG  . LEU   B 108 ? 0.2630 0.3013 0.2439 0.0409  0.0667  0.0164  108 LEU   B CG  
5439 C  CD1 . LEU   B 108 ? 0.2754 0.3207 0.2410 0.0317  0.0689  0.0168  108 LEU   B CD1 
5440 C  CD2 . LEU   B 108 ? 0.2792 0.3137 0.2521 0.0471  0.0472  0.0014  108 LEU   B CD2 
5453 N  N   . LEU   B 109 ? 0.1754 0.1749 0.2312 0.0164  0.0405  0.0211  109 LEU   B N   
5454 C  CA  . LEU   B 109 ? 0.1591 0.1507 0.2447 0.0083  0.0356  0.0246  109 LEU   B CA  
5455 C  C   . LEU   B 109 ? 0.1530 0.1399 0.2401 0.0057  0.0342  0.0243  109 LEU   B C   
5456 O  O   . LEU   B 109 ? 0.1509 0.1442 0.2334 0.0078  0.0350  0.0355  109 LEU   B O   
5457 C  CB  . LEU   B 109 ? 0.1723 0.1445 0.2535 0.0052  0.0181  0.0370  109 LEU   B CB  
5458 C  CG  . LEU   B 109 ? 0.1634 0.1441 0.2523 0.0047  0.0161  0.0233  109 LEU   B CG  
5459 C  CD1 . LEU   B 109 ? 0.1599 0.1537 0.2307 0.0070  0.0211  0.0163  109 LEU   B CD1 
5460 C  CD2 . LEU   B 109 ? 0.1794 0.1436 0.2481 0.0078  0.0164  0.0150  109 LEU   B CD2 
5472 N  N   . LYS   B 110 ? 0.1489 0.1374 0.2348 -0.0020 0.0257  0.0216  110 LYS   B N   
5473 C  CA  . LYS   B 110 ? 0.1455 0.1374 0.2271 0.0018  0.0244  0.0128  110 LYS   B CA  
5474 C  C   . LYS   B 110 ? 0.1403 0.1411 0.2197 0.0011  0.0264  0.0172  110 LYS   B C   
5475 O  O   . LYS   B 110 ? 0.1409 0.1405 0.2229 -0.0057 0.0233  0.0112  110 LYS   B O   
5476 C  CB  . LYS   B 110 ? 0.1472 0.1388 0.2467 -0.0016 0.0219  0.0076  110 LYS   B CB  
5477 C  CG  . LYS   B 110 ? 0.1499 0.1435 0.2691 -0.0020 0.0111  0.0090  110 LYS   B CG  
5478 C  CD  . LYS   B 110 ? 0.1512 0.1446 0.2620 -0.0052 0.0135  0.0127  110 LYS   B CD  
5479 C  CE  . LYS   B 110 ? 0.1529 0.1567 0.2858 0.0003  0.0137  0.0006  110 LYS   B CE  
5480 N  NZ  . LYS   B 110 ? 0.1581 0.1726 0.2759 -0.0016 -0.0001 -0.0011 110 LYS   B NZ  
5494 N  N   . SER   B 111 ? 0.1531 0.1392 0.2308 -0.0048 0.0276  0.0177  111 SER   B N   
5495 C  CA  . SER   B 111 ? 0.1531 0.1430 0.2206 -0.0001 0.0208  0.0175  111 SER   B CA  
5496 C  C   . SER   B 111 ? 0.1439 0.1375 0.2081 -0.0012 0.0158  0.0071  111 SER   B C   
5497 O  O   . SER   B 111 ? 0.1409 0.1419 0.2141 0.0006  0.0128  0.0077  111 SER   B O   
5498 C  CB  . SER   B 111 ? 0.1680 0.1649 0.2218 0.0113  0.0372  0.0210  111 SER   B CB  
5499 O  OG  . SER   B 111 ? 0.1923 0.2010 0.2120 0.0120  0.0357  0.0254  111 SER   B OG  
5505 N  N   . ALA   B 112 ? 0.1360 0.1424 0.2087 0.0039  0.0226  0.0132  112 ALA   B N   
5506 C  CA  . ALA   B 112 ? 0.1401 0.1446 0.1992 0.0030  0.0172  0.0044  112 ALA   B CA  
5507 C  C   . ALA   B 112 ? 0.1360 0.1319 0.1950 0.0022  0.0151  0.0052  112 ALA   B C   
5508 O  O   . ALA   B 112 ? 0.1349 0.1360 0.2035 -0.0071 0.0111  -0.0014 112 ALA   B O   
5509 C  CB  . ALA   B 112 ? 0.1452 0.1468 0.2239 0.0048  0.0067  0.0167  112 ALA   B CB  
5515 N  N   . TYR   B 113 ? 0.1337 0.1243 0.2029 0.0021  0.0145  0.0101  113 TYR   B N   
5516 C  CA  . TYR   B 113 ? 0.1253 0.1299 0.1923 -0.0025 0.0168  0.0024  113 TYR   B CA  
5517 C  C   . TYR   B 113 ? 0.1227 0.1199 0.1903 -0.0076 0.0128  0.0047  113 TYR   B C   
5518 O  O   . TYR   B 113 ? 0.1325 0.1246 0.1903 -0.0038 0.0099  0.0007  113 TYR   B O   
5519 C  CB  . TYR   B 113 ? 0.1328 0.1223 0.1967 0.0013  0.0171  0.0079  113 TYR   B CB  
5520 C  CG  . TYR   B 113 ? 0.1359 0.1229 0.2084 -0.0030 0.0113  0.0058  113 TYR   B CG  
5521 C  CD1 . TYR   B 113 ? 0.1312 0.1296 0.2301 -0.0022 0.0215  0.0079  113 TYR   B CD1 
5522 C  CD2 . TYR   B 113 ? 0.1415 0.1248 0.2194 -0.0036 0.0009  0.0095  113 TYR   B CD2 
5523 C  CE1 . TYR   B 113 ? 0.1402 0.1383 0.2282 -0.0039 0.0195  0.0078  113 TYR   B CE1 
5524 C  CE2 . TYR   B 113 ? 0.1403 0.1252 0.2373 -0.0001 0.0048  0.0084  113 TYR   B CE2 
5525 C  CZ  . TYR   B 113 ? 0.1317 0.1307 0.2341 0.0062  0.0081  0.0082  113 TYR   B CZ  
5526 O  OH  . TYR   B 113 ? 0.1471 0.1239 0.2610 0.0128  0.0166  0.0014  113 TYR   B OH  
5536 N  N   . GLU   B 114 ? 0.1230 0.1135 0.2084 -0.0034 0.0110  0.0066  114 GLU   B N   
5537 C  CA  . GLU   B 114 ? 0.1240 0.1183 0.2046 0.0030  0.0127  0.0007  114 GLU   B CA  
5538 C  C   . GLU   B 114 ? 0.1290 0.1215 0.1911 0.0057  0.0131  0.0029  114 GLU   B C   
5539 O  O   . GLU   B 114 ? 0.1281 0.1265 0.2018 0.0017  -0.0013 0.0096  114 GLU   B O   
5540 C  CB  . GLU   B 114 ? 0.1283 0.1233 0.2137 0.0001  0.0174  0.0016  114 GLU   B CB  
5541 C  CG  . GLU   B 114 ? 0.1346 0.1267 0.2172 -0.0030 0.0145  0.0006  114 GLU   B CG  
5542 C  CD  . GLU   B 114 ? 0.1322 0.1266 0.2315 -0.0078 0.0031  -0.0005 114 GLU   B CD  
5543 O  OE1 . GLU   B 114 ? 0.1352 0.1459 0.2173 -0.0094 0.0135  0.0090  114 GLU   B OE1 
5544 O  OE2 . GLU   B 114 ? 0.1300 0.1481 0.2498 -0.0108 0.0065  0.0023  114 GLU   B OE2 
5551 N  N   . ASN   B 115 ? 0.1309 0.1143 0.1912 0.0002  0.0072  0.0050  115 ASN   B N   
5552 C  CA  . ASN   B 115 ? 0.1347 0.1230 0.1748 -0.0063 0.0054  0.0104  115 ASN   B CA  
5553 C  C   . ASN   B 115 ? 0.1274 0.1187 0.1798 -0.0112 0.0012  0.0020  115 ASN   B C   
5554 O  O   . ASN   B 115 ? 0.1395 0.1252 0.1807 -0.0107 -0.0008 0.0009  115 ASN   B O   
5555 C  CB  . ASN   B 115 ? 0.1430 0.1396 0.1804 -0.0069 0.0071  0.0108  115 ASN   B CB  
5556 C  CG  . ASN   B 115 ? 0.1478 0.1458 0.1824 0.0021  0.0037  0.0072  115 ASN   B CG  
5557 O  OD1 . ASN   B 115 ? 0.1885 0.1589 0.1988 -0.0043 0.0110  -0.0090 115 ASN   B OD1 
5558 N  ND2 . ASN   B 115 ? 0.1458 0.1539 0.1812 -0.0062 0.0083  0.0104  115 ASN   B ND2 
5565 N  N   . PHE   B 116 ? 0.1305 0.1215 0.1704 -0.0044 0.0034  -0.0041 116 PHE   B N   
5566 C  CA  . PHE   B 116 ? 0.1346 0.1286 0.1671 -0.0117 -0.0004 -0.0066 116 PHE   B CA  
5567 C  C   . PHE   B 116 ? 0.1367 0.1155 0.1670 -0.0075 -0.0060 0.0008  116 PHE   B C   
5568 O  O   . PHE   B 116 ? 0.1388 0.1304 0.1748 -0.0019 -0.0052 0.0068  116 PHE   B O   
5569 C  CB  . PHE   B 116 ? 0.1336 0.1256 0.1731 -0.0067 -0.0089 -0.0007 116 PHE   B CB  
5570 C  CG  . PHE   B 116 ? 0.1271 0.1262 0.1689 -0.0027 -0.0056 -0.0002 116 PHE   B CG  
5571 C  CD1 . PHE   B 116 ? 0.1313 0.1325 0.1920 -0.0012 0.0064  0.0059  116 PHE   B CD1 
5572 C  CD2 . PHE   B 116 ? 0.1317 0.1343 0.1523 -0.0020 0.0004  -0.0030 116 PHE   B CD2 
5573 C  CE1 . PHE   B 116 ? 0.1346 0.1396 0.1853 -0.0009 -0.0100 0.0037  116 PHE   B CE1 
5574 C  CE2 . PHE   B 116 ? 0.1332 0.1370 0.1677 -0.0026 0.0067  0.0075  116 PHE   B CE2 
5575 C  CZ  . PHE   B 116 ? 0.1300 0.1418 0.1786 -0.0016 -0.0028 0.0027  116 PHE   B CZ  
5585 N  N   . ASN   B 117 ? 0.1300 0.1190 0.1762 0.0003  -0.0119 0.0026  117 ASN   B N   
5586 C  CA  . ASN   B 117 ? 0.1409 0.1228 0.1820 -0.0012 -0.0050 0.0024  117 ASN   B CA  
5587 C  C   . ASN   B 117 ? 0.1446 0.1249 0.1899 -0.0030 -0.0100 0.0025  117 ASN   B C   
5588 O  O   . ASN   B 117 ? 0.1489 0.1348 0.2249 -0.0061 -0.0405 0.0101  117 ASN   B O   
5589 C  CB  . ASN   B 117 ? 0.1409 0.1308 0.1899 0.0006  0.0025  0.0020  117 ASN   B CB  
5590 C  CG  . ASN   B 117 ? 0.1371 0.1314 0.1997 -0.0000 0.0004  -0.0073 117 ASN   B CG  
5591 O  OD1 . ASN   B 117 ? 0.1589 0.1300 0.2110 -0.0107 0.0069  -0.0040 117 ASN   B OD1 
5592 N  ND2 . ASN   B 117 ? 0.1374 0.1334 0.1966 -0.0007 0.0007  -0.0047 117 ASN   B ND2 
5599 N  N   . GLN   B 118 ? 0.1458 0.1224 0.1868 -0.0105 -0.0140 -0.0009 118 GLN   B N   
5600 C  CA  . GLN   B 118 ? 0.1461 0.1264 0.2066 -0.0002 -0.0125 0.0016  118 GLN   B CA  
5601 C  C   . GLN   B 118 ? 0.1484 0.1211 0.2109 -0.0026 -0.0163 0.0026  118 GLN   B C   
5602 O  O   . GLN   B 118 ? 0.1663 0.1189 0.2482 -0.0057 0.0062  0.0042  118 GLN   B O   
5603 C  CB  . GLN   B 118 ? 0.1510 0.1278 0.2138 0.0068  -0.0181 -0.0029 118 GLN   B CB  
5604 C  CG  . GLN   B 118 ? 0.1601 0.1380 0.2069 0.0117  -0.0122 -0.0124 118 GLN   B CG  
5605 C  CD  . GLN   B 118 ? 0.1625 0.1293 0.2081 0.0017  -0.0108 -0.0216 118 GLN   B CD  
5606 O  OE1 . GLN   B 118 ? 0.1699 0.1280 0.2316 0.0014  0.0041  -0.0033 118 GLN   B OE1 
5607 N  NE2 . GLN   B 118 ? 0.1702 0.1363 0.2106 0.0052  -0.0132 0.0030  118 GLN   B NE2 
5616 N  N   . HIS   B 119 ? 0.1546 0.1243 0.1809 -0.0091 -0.0101 0.0041  119 HIS   B N   
5617 C  CA  . HIS   B 119 ? 0.1611 0.1325 0.1775 -0.0066 -0.0138 -0.0002 119 HIS   B CA  
5618 C  C   . HIS   B 119 ? 0.1652 0.1347 0.1734 -0.0054 -0.0243 0.0129  119 HIS   B C   
5619 O  O   . HIS   B 119 ? 0.1724 0.1381 0.1932 -0.0253 -0.0173 0.0119  119 HIS   B O   
5620 C  CB  . HIS   B 119 ? 0.1654 0.1435 0.1887 -0.0028 -0.0128 0.0016  119 HIS   B CB  
5621 C  CG  . HIS   B 119 ? 0.1678 0.1582 0.1963 0.0092  -0.0406 -0.0111 119 HIS   B CG  
5622 N  ND1 . HIS   B 119 ? 0.1861 0.1736 0.2432 0.0036  -0.0469 -0.0308 119 HIS   B ND1 
5623 C  CD2 . HIS   B 119 ? 0.1844 0.1872 0.2025 0.0348  -0.0463 -0.0137 119 HIS   B CD2 
5624 C  CE1 . HIS   B 119 ? 0.2040 0.1920 0.2365 0.0196  -0.0559 -0.0440 119 HIS   B CE1 
5625 N  NE2 . HIS   B 119 ? 0.2073 0.2069 0.2153 0.0341  -0.0507 -0.0332 119 HIS   B NE2 
5633 N  N   . GLU   B 120 ? 0.1847 0.1351 0.1739 -0.0101 -0.0339 0.0150  120 GLU   B N   
5634 C  CA  . GLU   B 120 ? 0.2075 0.1566 0.1808 -0.0012 -0.0401 0.0223  120 GLU   B CA  
5635 C  C   . GLU   B 120 ? 0.1820 0.1497 0.1658 -0.0125 -0.0387 0.0243  120 GLU   B C   
5636 O  O   . GLU   B 120 ? 0.1774 0.1645 0.1712 -0.0133 -0.0325 0.0080  120 GLU   B O   
5637 C  CB  . GLU   B 120 ? 0.2786 0.1954 0.2456 0.0231  -0.0652 0.0393  120 GLU   B CB  
5638 C  CG  . GLU   B 120 ? 0.3435 0.2828 0.3564 0.0320  -0.0815 0.0676  120 GLU   B CG  
5639 C  CD  . GLU   B 120 ? 0.3964 0.3607 0.4574 0.0339  -0.0883 0.0908  120 GLU   B CD  
5640 O  OE1 . GLU   B 120 ? 0.4200 0.3903 0.4898 0.0261  -0.0847 0.1115  120 GLU   B OE1 
5641 O  OE2 . GLU   B 120 ? 0.4204 0.4021 0.5089 0.0363  -0.0888 0.0873  120 GLU   B OE2 
5648 N  N   . VAL   B 121 ? 0.1714 0.1391 0.1788 -0.0165 -0.0207 0.0232  121 VAL   B N   
5649 C  CA  . VAL   B 121 ? 0.1731 0.1543 0.1595 -0.0161 -0.0129 0.0190  121 VAL   B CA  
5650 C  C   . VAL   B 121 ? 0.1664 0.1447 0.1494 -0.0237 -0.0112 0.0154  121 VAL   B C   
5651 O  O   . VAL   B 121 ? 0.1753 0.1399 0.1742 -0.0319 -0.0255 0.0063  121 VAL   B O   
5652 C  CB  . VAL   B 121 ? 0.1947 0.1898 0.1726 -0.0054 -0.0236 0.0243  121 VAL   B CB  
5653 C  CG1 . VAL   B 121 ? 0.1980 0.2012 0.2141 -0.0180 -0.0101 0.0171  121 VAL   B CG1 
5654 C  CG2 . VAL   B 121 ? 0.2218 0.2215 0.1547 0.0053  -0.0168 0.0104  121 VAL   B CG2 
5664 N  N   . LEU   B 122 ? 0.1557 0.1408 0.1515 -0.0184 -0.0213 0.0092  122 LEU   B N   
5665 C  CA  . LEU   B 122 ? 0.1447 0.1492 0.1368 -0.0152 -0.0154 0.0107  122 LEU   B CA  
5666 C  C   . LEU   B 122 ? 0.1504 0.1299 0.1507 -0.0233 -0.0100 0.0047  122 LEU   B C   
5667 O  O   . LEU   B 122 ? 0.1611 0.1371 0.1840 -0.0297 -0.0179 -0.0004 122 LEU   B O   
5668 C  CB  . LEU   B 122 ? 0.1670 0.1622 0.1779 -0.0046 -0.0221 0.0082  122 LEU   B CB  
5669 C  CG  . LEU   B 122 ? 0.1540 0.1734 0.1870 -0.0120 -0.0090 0.0058  122 LEU   B CG  
5670 C  CD1 . LEU   B 122 ? 0.1610 0.1937 0.1821 -0.0150 -0.0126 0.0063  122 LEU   B CD1 
5671 C  CD2 . LEU   B 122 ? 0.1600 0.1698 0.1550 -0.0130 -0.0022 -0.0050 122 LEU   B CD2 
5683 N  N   . LEU   B 123 ? 0.1499 0.1281 0.1442 -0.0182 -0.0126 0.0111  123 LEU   B N   
5684 C  CA  . LEU   B 123 ? 0.1505 0.1313 0.1479 -0.0242 -0.0143 -0.0037 123 LEU   B CA  
5685 C  C   . LEU   B 123 ? 0.1449 0.1259 0.1416 -0.0260 -0.0192 -0.0022 123 LEU   B C   
5686 O  O   . LEU   B 123 ? 0.1548 0.1309 0.1403 -0.0302 -0.0131 0.0056  123 LEU   B O   
5687 C  CB  . LEU   B 123 ? 0.1554 0.1353 0.1618 -0.0233 -0.0068 -0.0046 123 LEU   B CB  
5688 C  CG  . LEU   B 123 ? 0.1549 0.1422 0.1617 -0.0169 -0.0036 0.0037  123 LEU   B CG  
5689 C  CD1 . LEU   B 123 ? 0.1642 0.1473 0.1642 -0.0170 0.0022  -0.0143 123 LEU   B CD1 
5690 C  CD2 . LEU   B 123 ? 0.1652 0.1378 0.1778 -0.0122 0.0059  0.0167  123 LEU   B CD2 
5702 N  N   . ALA   B 124 ? 0.1419 0.1285 0.1523 -0.0251 -0.0078 -0.0078 124 ALA   B N   
5703 C  CA  . ALA   B 124 ? 0.1353 0.1282 0.1607 -0.0151 -0.0067 -0.0082 124 ALA   B CA  
5704 C  C   . ALA   B 124 ? 0.1300 0.1232 0.1535 -0.0209 -0.0054 -0.0009 124 ALA   B C   
5705 O  O   . ALA   B 124 ? 0.1474 0.1302 0.1637 -0.0152 -0.0097 -0.0023 124 ALA   B O   
5706 C  CB  . ALA   B 124 ? 0.1397 0.1352 0.1733 -0.0078 0.0041  -0.0092 124 ALA   B CB  
5712 N  N   . PRO   B 125 ? 0.1400 0.1257 0.1465 -0.0157 -0.0067 0.0090  125 PRO   B N   
5713 C  CA  . PRO   B 125 ? 0.1535 0.1312 0.1693 -0.0176 -0.0054 0.0142  125 PRO   B CA  
5714 C  C   . PRO   B 125 ? 0.1464 0.1287 0.1849 -0.0153 -0.0018 0.0072  125 PRO   B C   
5715 O  O   . PRO   B 125 ? 0.1454 0.1270 0.1962 -0.0090 0.0043  0.0107  125 PRO   B O   
5716 C  CB  . PRO   B 125 ? 0.1551 0.1557 0.1899 -0.0216 -0.0158 0.0281  125 PRO   B CB  
5717 C  CG  . PRO   B 125 ? 0.1609 0.1538 0.1736 -0.0328 -0.0173 0.0123  125 PRO   B CG  
5718 C  CD  . PRO   B 125 ? 0.1532 0.1335 0.1553 -0.0317 -0.0120 0.0079  125 PRO   B CD  
5726 N  N   . LEU   B 126 ? 0.1530 0.1235 0.2046 -0.0189 0.0095  0.0127  126 LEU   B N   
5727 C  CA  . LEU   B 126 ? 0.1598 0.1381 0.2002 -0.0147 0.0229  0.0132  126 LEU   B CA  
5728 C  C   . LEU   B 126 ? 0.1488 0.1481 0.2020 0.0047  0.0261  0.0210  126 LEU   B C   
5729 O  O   . LEU   B 126 ? 0.1702 0.1763 0.2335 0.0219  0.0015  -0.0020 126 LEU   B O   
5730 C  CB  . LEU   B 126 ? 0.1787 0.1388 0.2338 -0.0226 0.0219  0.0151  126 LEU   B CB  
5731 C  CG  . LEU   B 126 ? 0.1964 0.1460 0.2411 -0.0233 0.0174  -0.0066 126 LEU   B CG  
5732 C  CD1 . LEU   B 126 ? 0.2070 0.1540 0.2892 -0.0155 0.0082  -0.0206 126 LEU   B CD1 
5733 C  CD2 . LEU   B 126 ? 0.1960 0.1562 0.2370 -0.0354 0.0135  -0.0126 126 LEU   B CD2 
5745 N  N   . LEU   B 127 ? 0.1503 0.1317 0.2117 0.0015  0.0262  0.0111  127 LEU   B N   
5746 C  CA  . LEU   B 127 ? 0.1535 0.1421 0.2168 -0.0069 0.0222  0.0191  127 LEU   B CA  
5747 C  C   . LEU   B 127 ? 0.1504 0.1306 0.2175 -0.0014 0.0224  0.0216  127 LEU   B C   
5748 O  O   . LEU   B 127 ? 0.1519 0.1357 0.2293 -0.0153 0.0077  0.0167  127 LEU   B O   
5749 C  CB  . LEU   B 127 ? 0.1661 0.1378 0.2219 -0.0054 0.0174  0.0198  127 LEU   B CB  
5750 C  CG  . LEU   B 127 ? 0.1810 0.1346 0.2329 -0.0014 0.0230  0.0235  127 LEU   B CG  
5751 C  CD1 . LEU   B 127 ? 0.1833 0.1353 0.2408 0.0004  0.0192  0.0136  127 LEU   B CD1 
5752 C  CD2 . LEU   B 127 ? 0.1798 0.1496 0.2551 -0.0102 0.0268  0.0361  127 LEU   B CD2 
5764 N  N   . SER   B 128 ? 0.1545 0.1373 0.2127 0.0042  0.0059  0.0144  128 SER   B N   
5765 C  CA  . SER   B 128 ? 0.1661 0.1469 0.2063 0.0112  -0.0015 0.0172  128 SER   B CA  
5766 C  C   . SER   B 128 ? 0.1798 0.1465 0.2489 0.0090  -0.0240 0.0164  128 SER   B C   
5767 O  O   . SER   B 128 ? 0.1974 0.1515 0.2968 0.0040  -0.0222 0.0333  128 SER   B O   
5768 C  CB  . SER   B 128 ? 0.1734 0.1495 0.2139 0.0097  0.0036  0.0266  128 SER   B CB  
5769 O  OG  . SER   B 128 ? 0.1814 0.1640 0.2202 0.0100  0.0180  0.0354  128 SER   B OG  
5775 N  N   . ALA   B 129 ? 0.1886 0.1502 0.2786 0.0259  -0.0169 -0.0013 129 ALA   B N   
5776 C  CA  . ALA   B 129 ? 0.2108 0.1645 0.2983 0.0329  -0.0107 -0.0146 129 ALA   B CA  
5777 C  C   . ALA   B 129 ? 0.1930 0.1489 0.2828 0.0238  0.0140  -0.0009 129 ALA   B C   
5778 O  O   . ALA   B 129 ? 0.1773 0.1519 0.2735 0.0200  0.0080  0.0025  129 ALA   B O   
5779 C  CB  . ALA   B 129 ? 0.2384 0.1905 0.3300 0.0423  0.0004  -0.0224 129 ALA   B CB  
5785 N  N   . GLY   B 130 ? 0.1892 0.1484 0.2784 0.0324  0.0147  -0.0098 130 GLY   B N   
5786 C  CA  . GLY   B 130 ? 0.1890 0.1629 0.2755 0.0245  0.0390  -0.0044 130 GLY   B CA  
5787 C  C   . GLY   B 130 ? 0.1920 0.1631 0.2621 0.0184  0.0259  0.0071  130 GLY   B C   
5788 O  O   . GLY   B 130 ? 0.2081 0.1768 0.2655 0.0214  0.0139  0.0137  130 GLY   B O   
5792 N  N   . ILE   B 131 ? 0.1862 0.1776 0.2688 0.0380  0.0229  0.0015  131 ILE   B N   
5793 C  CA  . ILE   B 131 ? 0.2076 0.1861 0.2596 0.0319  0.0161  0.0206  131 ILE   B CA  
5794 C  C   . ILE   B 131 ? 0.2211 0.1867 0.2331 0.0168  0.0062  0.0250  131 ILE   B C   
5795 O  O   . ILE   B 131 ? 0.2486 0.2076 0.2437 0.0165  -0.0223 0.0278  131 ILE   B O   
5796 C  CB  . ILE   B 131 ? 0.2092 0.2222 0.2981 0.0263  0.0046  0.0349  131 ILE   B CB  
5797 C  CG1 . ILE   B 131 ? 0.2137 0.2446 0.3047 -0.0074 0.0127  0.0416  131 ILE   B CG1 
5798 C  CG2 . ILE   B 131 ? 0.2127 0.2406 0.3227 0.0350  -0.0014 0.0315  131 ILE   B CG2 
5799 C  CD1 . ILE   B 131 ? 0.2264 0.2643 0.3179 -0.0236 0.0144  0.0494  131 ILE   B CD1 
5811 N  N   . PHE   B 132 ? 0.2049 0.1663 0.2234 0.0134  0.0238  0.0189  132 PHE   B N   
5812 C  CA  . PHE   B 132 ? 0.2179 0.1689 0.2272 0.0074  0.0418  0.0113  132 PHE   B CA  
5813 C  C   . PHE   B 132 ? 0.2378 0.1826 0.2474 0.0112  0.0510  0.0125  132 PHE   B C   
5814 O  O   . PHE   B 132 ? 0.2547 0.2104 0.2754 0.0104  0.0633  0.0189  132 PHE   B O   
5815 C  CB  . PHE   B 132 ? 0.2021 0.1657 0.2131 0.0105  0.0395  0.0221  132 PHE   B CB  
5816 C  CG  . PHE   B 132 ? 0.1903 0.1707 0.2020 0.0183  0.0271  0.0198  132 PHE   B CG  
5817 C  CD1 . PHE   B 132 ? 0.2014 0.1716 0.2432 0.0174  0.0291  0.0237  132 PHE   B CD1 
5818 C  CD2 . PHE   B 132 ? 0.1910 0.1742 0.1879 0.0241  0.0162  0.0265  132 PHE   B CD2 
5819 C  CE1 . PHE   B 132 ? 0.2013 0.1767 0.2522 0.0110  0.0208  0.0280  132 PHE   B CE1 
5820 C  CE2 . PHE   B 132 ? 0.1970 0.1789 0.1977 0.0208  0.0012  0.0225  132 PHE   B CE2 
5821 C  CZ  . PHE   B 132 ? 0.2021 0.1784 0.2253 0.0168  -0.0068 0.0261  132 PHE   B CZ  
5831 N  N   . GLY   B 133 ? 0.2284 0.1658 0.2551 0.0042  0.0412  0.0409  133 GLY   B N   
5832 C  CA  . GLY   B 133 ? 0.2423 0.1850 0.2603 -0.0203 0.0333  0.0466  133 GLY   B CA  
5833 C  C   . GLY   B 133 ? 0.2502 0.1981 0.2683 -0.0335 0.0421  0.0553  133 GLY   B C   
5834 O  O   . GLY   B 133 ? 0.2722 0.2144 0.3169 -0.0463 0.0407  0.0623  133 GLY   B O   
5838 N  N   . ALA   B 134 ? 0.2258 0.1969 0.2563 -0.0265 0.0418  0.0336  134 ALA   B N   
5839 C  CA  . ALA   B 134 ? 0.2212 0.1938 0.2788 -0.0170 0.0521  0.0151  134 ALA   B CA  
5840 C  C   . ALA   B 134 ? 0.2316 0.1799 0.2775 -0.0121 0.0447  0.0304  134 ALA   B C   
5841 O  O   . ALA   B 134 ? 0.2357 0.1953 0.2832 -0.0014 0.0280  0.0227  134 ALA   B O   
5842 C  CB  . ALA   B 134 ? 0.2137 0.1952 0.3024 -0.0095 0.0388  0.0011  134 ALA   B CB  
5848 N  N   . ASP   B 135 ? 0.2460 0.1718 0.2805 -0.0121 0.0196  0.0334  135 ASP   B N   
5849 C  CA  . ASP   B 135 ? 0.2648 0.1658 0.2952 -0.0148 0.0075  0.0376  135 ASP   B CA  
5850 C  C   . ASP   B 135 ? 0.2428 0.1542 0.2783 -0.0034 0.0110  0.0342  135 ASP   B C   
5851 O  O   . ASP   B 135 ? 0.2302 0.1482 0.3021 -0.0088 0.0134  0.0272  135 ASP   B O   
5852 C  CB  . ASP   B 135 ? 0.2992 0.1801 0.3214 -0.0430 0.0073  0.0366  135 ASP   B CB  
5853 C  CG  . ASP   B 135 ? 0.3285 0.1835 0.3696 -0.0681 0.0154  0.0331  135 ASP   B CG  
5854 O  OD1 . ASP   B 135 ? 0.3378 0.1661 0.3492 -0.0443 0.0130  0.0246  135 ASP   B OD1 
5855 O  OD2 . ASP   B 135 ? 0.3536 0.2275 0.4268 -0.0855 0.0137  0.0161  135 ASP   B OD2 
5860 N  N   . PRO   B 136 ? 0.2367 0.1624 0.2910 0.0205  -0.0180 0.0221  136 PRO   B N   
5861 C  CA  . PRO   B 136 ? 0.2072 0.1529 0.2948 0.0179  -0.0142 0.0145  136 PRO   B CA  
5862 C  C   . PRO   B 136 ? 0.1860 0.1425 0.2948 0.0149  0.0011  0.0042  136 PRO   B C   
5863 O  O   . PRO   B 136 ? 0.1729 0.1385 0.2892 0.0091  0.0052  0.0133  136 PRO   B O   
5864 C  CB  . PRO   B 136 ? 0.2106 0.1760 0.3129 0.0341  -0.0126 0.0095  136 PRO   B CB  
5865 C  CG  . PRO   B 136 ? 0.2332 0.1814 0.3304 0.0379  -0.0066 0.0042  136 PRO   B CG  
5866 C  CD  . PRO   B 136 ? 0.2430 0.1747 0.3058 0.0386  -0.0139 0.0102  136 PRO   B CD  
5874 N  N   . ILE   B 137 ? 0.1970 0.1308 0.2997 0.0178  -0.0065 0.0032  137 ILE   B N   
5875 C  CA  . ILE   B 137 ? 0.2052 0.1316 0.3138 -0.0076 -0.0033 0.0045  137 ILE   B CA  
5876 C  C   . ILE   B 137 ? 0.1940 0.1386 0.3048 -0.0119 0.0111  0.0080  137 ILE   B C   
5877 O  O   . ILE   B 137 ? 0.1861 0.1418 0.2960 -0.0121 0.0011  0.0085  137 ILE   B O   
5878 C  CB  . ILE   B 137 ? 0.2354 0.1393 0.3565 -0.0073 -0.0152 0.0031  137 ILE   B CB  
5879 C  CG1 . ILE   B 137 ? 0.2683 0.1578 0.4066 0.0038  -0.0188 -0.0107 137 ILE   B CG1 
5880 C  CG2 . ILE   B 137 ? 0.2381 0.1428 0.3597 -0.0344 -0.0123 0.0129  137 ILE   B CG2 
5881 C  CD1 . ILE   B 137 ? 0.2987 0.1847 0.4433 0.0160  -0.0197 -0.0059 137 ILE   B CD1 
5893 N  N   . HIS   B 138 ? 0.1996 0.1393 0.3057 -0.0102 0.0196  0.0062  138 HIS   B N   
5894 C  CA  . HIS   B 138 ? 0.2052 0.1507 0.2966 -0.0057 0.0365  0.0141  138 HIS   B CA  
5895 C  C   . HIS   B 138 ? 0.1897 0.1490 0.2712 -0.0039 0.0315  0.0211  138 HIS   B C   
5896 O  O   . HIS   B 138 ? 0.1773 0.1524 0.2950 -0.0004 0.0314  0.0248  138 HIS   B O   
5897 C  CB  . HIS   B 138 ? 0.2341 0.1614 0.3186 -0.0121 0.0555  0.0089  138 HIS   B CB  
5898 C  CG  . HIS   B 138 ? 0.2628 0.1803 0.3198 -0.0176 0.0865  0.0355  138 HIS   B CG  
5899 N  ND1 . HIS   B 138 ? 0.2763 0.2017 0.3537 -0.0088 0.1002  0.0286  138 HIS   B ND1 
5900 C  CD2 . HIS   B 138 ? 0.2846 0.1960 0.3058 -0.0150 0.1009  0.0244  138 HIS   B CD2 
5901 C  CE1 . HIS   B 138 ? 0.2873 0.2042 0.3454 -0.0124 0.1094  0.0294  138 HIS   B CE1 
5902 N  NE2 . HIS   B 138 ? 0.2947 0.1976 0.3200 -0.0078 0.1073  0.0241  138 HIS   B NE2 
5910 N  N   . SER   B 139 ? 0.1878 0.1354 0.2642 0.0034  0.0219  0.0132  139 SER   B N   
5911 C  CA  . SER   B 139 ? 0.1846 0.1269 0.2558 -0.0056 0.0179  0.0043  139 SER   B CA  
5912 C  C   . SER   B 139 ? 0.1569 0.1231 0.2547 -0.0026 0.0133  0.0016  139 SER   B C   
5913 O  O   . SER   B 139 ? 0.1591 0.1275 0.2553 -0.0013 0.0051  0.0045  139 SER   B O   
5914 C  CB  . SER   B 139 ? 0.1927 0.1285 0.2516 -0.0036 0.0052  0.0027  139 SER   B CB  
5915 O  OG  . SER   B 139 ? 0.1933 0.1297 0.2519 -0.0054 -0.0045 0.0137  139 SER   B OG  
5921 N  N   . LEU   B 140 ? 0.1567 0.1199 0.2528 -0.0063 0.0149  -0.0017 140 LEU   B N   
5922 C  CA  . LEU   B 140 ? 0.1529 0.1224 0.2475 -0.0030 0.0061  0.0021  140 LEU   B CA  
5923 C  C   . LEU   B 140 ? 0.1525 0.1204 0.2513 -0.0052 0.0067  0.0019  140 LEU   B C   
5924 O  O   . LEU   B 140 ? 0.1556 0.1347 0.2457 -0.0028 0.0132  0.0051  140 LEU   B O   
5925 C  CB  . LEU   B 140 ? 0.1545 0.1222 0.2520 -0.0136 0.0116  -0.0044 140 LEU   B CB  
5926 C  CG  . LEU   B 140 ? 0.1648 0.1243 0.2499 -0.0164 0.0039  0.0030  140 LEU   B CG  
5927 C  CD1 . LEU   B 140 ? 0.1749 0.1361 0.2700 -0.0173 0.0193  -0.0020 140 LEU   B CD1 
5928 C  CD2 . LEU   B 140 ? 0.1815 0.1361 0.2629 -0.0125 0.0072  -0.0008 140 LEU   B CD2 
5940 N  N   . ARG   B 141 ? 0.1459 0.1270 0.2602 -0.0018 0.0180  -0.0022 141 ARG   B N   
5941 C  CA  . ARG   B 141 ? 0.1530 0.1242 0.3074 -0.0070 0.0274  -0.0021 141 ARG   B CA  
5942 C  C   . ARG   B 141 ? 0.1472 0.1233 0.2984 -0.0103 0.0163  -0.0062 141 ARG   B C   
5943 O  O   . ARG   B 141 ? 0.1505 0.1326 0.2818 -0.0130 0.0007  -0.0113 141 ARG   B O   
5944 C  CB  . ARG   B 141 ? 0.1713 0.1354 0.3310 -0.0147 0.0367  -0.0004 141 ARG   B CB  
5945 C  CG  . ARG   B 141 ? 0.2035 0.1615 0.3494 -0.0164 0.0325  0.0023  141 ARG   B CG  
5946 C  CD  . ARG   B 141 ? 0.2394 0.1872 0.3554 -0.0112 0.0099  -0.0092 141 ARG   B CD  
5947 N  NE  . ARG   B 141 ? 0.2535 0.1836 0.3449 -0.0258 0.0222  -0.0129 141 ARG   B NE  
5948 C  CZ  . ARG   B 141 ? 0.2668 0.1688 0.3243 -0.0220 0.0342  -0.0232 141 ARG   B CZ  
5949 N  NH1 . ARG   B 141 ? 0.2834 0.1612 0.3100 -0.0167 0.0343  -0.0182 141 ARG   B NH1 
5950 N  NH2 . ARG   B 141 ? 0.2820 0.1777 0.3378 -0.0115 0.0138  -0.0180 141 ARG   B NH2 
5964 N  N   . VAL   B 142 ? 0.1507 0.1222 0.2895 -0.0098 0.0157  -0.0148 142 VAL   B N   
5965 C  CA  . VAL   B 142 ? 0.1440 0.1253 0.2771 -0.0079 0.0188  -0.0093 142 VAL   B CA  
5966 C  C   . VAL   B 142 ? 0.1402 0.1269 0.2695 -0.0028 0.0136  -0.0067 142 VAL   B C   
5967 O  O   . VAL   B 142 ? 0.1485 0.1270 0.2764 0.0061  0.0241  -0.0024 142 VAL   B O   
5968 C  CB  . VAL   B 142 ? 0.1552 0.1368 0.2758 -0.0037 0.0251  0.0085  142 VAL   B CB  
5969 C  CG1 . VAL   B 142 ? 0.1487 0.1323 0.2818 0.0083  0.0222  0.0025  142 VAL   B CG1 
5970 C  CG2 . VAL   B 142 ? 0.1843 0.1368 0.2803 0.0001  0.0205  0.0066  142 VAL   B CG2 
5980 N  N   . CYS   B 143 ? 0.1397 0.1295 0.2422 0.0010  0.0139  0.0077  143 CYS   B N   
5981 C  CA  . CYS   B 143 ? 0.1354 0.1289 0.2501 -0.0022 0.0085  0.0069  143 CYS   B CA  
5982 C  C   . CYS   B 143 ? 0.1305 0.1287 0.2431 -0.0049 0.0128  0.0040  143 CYS   B C   
5983 O  O   . CYS   B 143 ? 0.1383 0.1322 0.2502 -0.0013 0.0014  -0.0004 143 CYS   B O   
5984 C  CB  . CYS   B 143 ? 0.1444 0.1300 0.2498 -0.0069 -0.0014 -0.0027 143 CYS   B CB  
5985 S  SG  . CYS   B 143 ? 0.1469 0.1497 0.2408 -0.0045 0.0048  0.0012  143 CYS   B SG  
5991 N  N   . VAL   B 144 ? 0.1344 0.1266 0.2666 -0.0082 0.0035  -0.0094 144 VAL   B N   
5992 C  CA  . VAL   B 144 ? 0.1429 0.1399 0.2808 -0.0153 -0.0040 -0.0100 144 VAL   B CA  
5993 C  C   . VAL   B 144 ? 0.1392 0.1395 0.2932 -0.0123 -0.0101 -0.0038 144 VAL   B C   
5994 O  O   . VAL   B 144 ? 0.1503 0.1586 0.3129 -0.0024 -0.0062 0.0147  144 VAL   B O   
5995 C  CB  . VAL   B 144 ? 0.1658 0.1531 0.3421 -0.0100 -0.0188 -0.0251 144 VAL   B CB  
5996 C  CG1 . VAL   B 144 ? 0.2000 0.1949 0.3815 -0.0009 -0.0292 -0.0195 144 VAL   B CG1 
5997 C  CG2 . VAL   B 144 ? 0.1780 0.1526 0.3435 -0.0080 -0.0310 -0.0330 144 VAL   B CG2 
6007 N  N   . ASP   B 145 ? 0.1404 0.1349 0.2968 -0.0078 0.0036  -0.0179 145 ASP   B N   
6008 C  CA  . ASP   B 145 ? 0.1485 0.1343 0.3179 -0.0090 0.0131  -0.0058 145 ASP   B CA  
6009 C  C   . ASP   B 145 ? 0.1428 0.1386 0.2908 -0.0100 0.0153  -0.0007 145 ASP   B C   
6010 O  O   . ASP   B 145 ? 0.1428 0.1534 0.3416 -0.0120 0.0125  -0.0239 145 ASP   B O   
6011 C  CB  . ASP   B 145 ? 0.1620 0.1439 0.3734 -0.0117 0.0206  0.0031  145 ASP   B CB  
6012 C  CG  . ASP   B 145 ? 0.1776 0.1491 0.4266 -0.0199 0.0379  0.0026  145 ASP   B CG  
6013 O  OD1 . ASP   B 145 ? 0.1796 0.1499 0.4397 -0.0241 0.0016  -0.0101 145 ASP   B OD1 
6014 O  OD2 . ASP   B 145 ? 0.2080 0.1533 0.4715 -0.0266 0.0656  0.0121  145 ASP   B OD2 
6019 N  N   . THR   B 146 ? 0.1339 0.1248 0.2584 -0.0113 0.0051  0.0034  146 THR   B N   
6020 C  CA  . THR   B 146 ? 0.1401 0.1243 0.2421 -0.0070 0.0044  -0.0046 146 THR   B CA  
6021 C  C   . THR   B 146 ? 0.1419 0.1222 0.2332 -0.0010 -0.0042 -0.0009 146 THR   B C   
6022 O  O   . THR   B 146 ? 0.1479 0.1269 0.2314 -0.0014 -0.0026 0.0013  146 THR   B O   
6023 C  CB  . THR   B 146 ? 0.1461 0.1277 0.2537 -0.0043 0.0145  0.0023  146 THR   B CB  
6024 O  OG1 . THR   B 146 ? 0.1489 0.1266 0.2595 -0.0046 0.0221  0.0146  146 THR   B OG1 
6025 C  CG2 . THR   B 146 ? 0.1540 0.1362 0.2423 -0.0043 0.0124  -0.0051 146 THR   B CG2 
6033 N  N   . VAL   B 147 ? 0.1491 0.1273 0.2227 0.0001  0.0110  0.0039  147 VAL   B N   
6034 C  CA  . VAL   B 147 ? 0.1452 0.1225 0.2302 -0.0082 0.0002  0.0002  147 VAL   B CA  
6035 C  C   . VAL   B 147 ? 0.1368 0.1273 0.2377 -0.0202 -0.0077 -0.0020 147 VAL   B C   
6036 O  O   . VAL   B 147 ? 0.1523 0.1378 0.2430 -0.0210 -0.0286 -0.0020 147 VAL   B O   
6037 C  CB  . VAL   B 147 ? 0.1464 0.1386 0.2124 -0.0074 -0.0108 -0.0005 147 VAL   B CB  
6038 C  CG1 . VAL   B 147 ? 0.1500 0.1536 0.2004 -0.0095 -0.0159 0.0063  147 VAL   B CG1 
6039 C  CG2 . VAL   B 147 ? 0.1534 0.1375 0.2203 -0.0020 -0.0058 0.0087  147 VAL   B CG2 
6049 N  N   . ARG   B 148 ? 0.1424 0.1310 0.2229 -0.0146 -0.0171 -0.0062 148 ARG   B N   
6050 C  CA  . ARG   B 148 ? 0.1475 0.1360 0.2244 -0.0104 -0.0248 -0.0109 148 ARG   B CA  
6051 C  C   . ARG   B 148 ? 0.1547 0.1473 0.1974 -0.0108 -0.0302 -0.0114 148 ARG   B C   
6052 O  O   . ARG   B 148 ? 0.1715 0.1802 0.1974 -0.0286 -0.0356 -0.0062 148 ARG   B O   
6053 C  CB  . ARG   B 148 ? 0.1517 0.1496 0.2297 -0.0071 -0.0314 -0.0176 148 ARG   B CB  
6054 C  CG  . ARG   B 148 ? 0.1512 0.1622 0.2409 -0.0080 -0.0278 -0.0372 148 ARG   B CG  
6055 C  CD  . ARG   B 148 ? 0.1623 0.1825 0.2438 0.0053  -0.0261 -0.0302 148 ARG   B CD  
6056 N  NE  . ARG   B 148 ? 0.1654 0.1771 0.2381 0.0185  -0.0350 -0.0261 148 ARG   B NE  
6057 C  CZ  . ARG   B 148 ? 0.1570 0.1686 0.2154 0.0131  -0.0234 -0.0147 148 ARG   B CZ  
6058 N  NH1 . ARG   B 148 ? 0.1455 0.1766 0.2107 0.0052  -0.0055 -0.0157 148 ARG   B NH1 
6059 N  NH2 . ARG   B 148 ? 0.1792 0.1510 0.2241 0.0183  -0.0151 -0.0059 148 ARG   B NH2 
6073 N  N   . THR   B 149 ? 0.1578 0.1443 0.1939 -0.0116 -0.0256 -0.0044 149 THR   B N   
6074 C  CA  . THR   B 149 ? 0.1624 0.1497 0.1917 -0.0175 -0.0283 0.0067  149 THR   B CA  
6075 C  C   . THR   B 149 ? 0.1648 0.1481 0.1848 -0.0170 -0.0232 -0.0015 149 THR   B C   
6076 O  O   . THR   B 149 ? 0.1695 0.1410 0.2023 -0.0218 -0.0140 -0.0040 149 THR   B O   
6077 C  CB  . THR   B 149 ? 0.1625 0.1435 0.2023 -0.0142 -0.0246 -0.0092 149 THR   B CB  
6078 O  OG1 . THR   B 149 ? 0.1642 0.1483 0.1817 -0.0215 -0.0312 -0.0021 149 THR   B OG1 
6079 C  CG2 . THR   B 149 ? 0.1730 0.1531 0.2155 -0.0079 -0.0164 -0.0027 149 THR   B CG2 
6087 N  N   . ASN   B 150 ? 0.1665 0.1492 0.1768 -0.0149 -0.0274 -0.0011 150 ASN   B N   
6088 C  CA  . ASN   B 150 ? 0.1744 0.1622 0.1802 -0.0196 -0.0233 -0.0117 150 ASN   B CA  
6089 C  C   . ASN   B 150 ? 0.1645 0.1505 0.1756 -0.0209 -0.0175 -0.0055 150 ASN   B C   
6090 O  O   . ASN   B 150 ? 0.1721 0.1467 0.2012 -0.0323 -0.0405 0.0004  150 ASN   B O   
6091 C  CB  . ASN   B 150 ? 0.2008 0.1927 0.1853 -0.0177 -0.0337 0.0016  150 ASN   B CB  
6092 C  CG  . ASN   B 150 ? 0.2300 0.2342 0.2265 -0.0207 -0.0410 0.0286  150 ASN   B CG  
6093 O  OD1 . ASN   B 150 ? 0.2442 0.2554 0.2505 -0.0344 -0.0590 0.0272  150 ASN   B OD1 
6094 N  ND2 . ASN   B 150 ? 0.2406 0.2589 0.2720 -0.0151 -0.0478 0.0751  150 ASN   B ND2 
6101 N  N   . VAL   B 151 ? 0.1508 0.1485 0.1799 -0.0214 -0.0227 -0.0040 151 VAL   B N   
6102 C  CA  . VAL   B 151 ? 0.1523 0.1492 0.1856 -0.0224 -0.0183 -0.0048 151 VAL   B CA  
6103 C  C   . VAL   B 151 ? 0.1560 0.1429 0.1797 -0.0279 -0.0173 -0.0119 151 VAL   B C   
6104 O  O   . VAL   B 151 ? 0.1643 0.1497 0.2007 -0.0245 -0.0074 -0.0156 151 VAL   B O   
6105 C  CB  . VAL   B 151 ? 0.1742 0.1556 0.1955 -0.0127 -0.0133 -0.0038 151 VAL   B CB  
6106 C  CG1 . VAL   B 151 ? 0.1862 0.1649 0.2286 -0.0187 -0.0056 -0.0086 151 VAL   B CG1 
6107 C  CG2 . VAL   B 151 ? 0.1902 0.1771 0.1793 0.0111  -0.0083 0.0043  151 VAL   B CG2 
6117 N  N   . TYR   B 152 ? 0.1508 0.1364 0.1759 -0.0185 -0.0100 -0.0087 152 TYR   B N   
6118 C  CA  . TYR   B 152 ? 0.1562 0.1552 0.1494 -0.0281 -0.0076 -0.0044 152 TYR   B CA  
6119 C  C   . TYR   B 152 ? 0.1568 0.1334 0.1494 -0.0193 -0.0046 -0.0173 152 TYR   B C   
6120 O  O   . TYR   B 152 ? 0.1655 0.1384 0.1754 -0.0241 -0.0034 -0.0079 152 TYR   B O   
6121 C  CB  . TYR   B 152 ? 0.1741 0.1666 0.1673 -0.0302 -0.0110 0.0010  152 TYR   B CB  
6122 C  CG  . TYR   B 152 ? 0.1897 0.1722 0.1672 -0.0428 -0.0146 0.0014  152 TYR   B CG  
6123 C  CD1 . TYR   B 152 ? 0.2006 0.1865 0.1583 -0.0332 -0.0204 0.0027  152 TYR   B CD1 
6124 C  CD2 . TYR   B 152 ? 0.2125 0.1947 0.1831 -0.0390 -0.0137 -0.0073 152 TYR   B CD2 
6125 C  CE1 . TYR   B 152 ? 0.2187 0.2079 0.1837 -0.0257 -0.0298 0.0186  152 TYR   B CE1 
6126 C  CE2 . TYR   B 152 ? 0.2230 0.2189 0.1787 -0.0391 -0.0243 -0.0212 152 TYR   B CE2 
6127 C  CZ  . TYR   B 152 ? 0.2296 0.2299 0.1659 -0.0359 -0.0427 0.0108  152 TYR   B CZ  
6128 O  OH  . TYR   B 152 ? 0.2620 0.2717 0.1952 -0.0260 -0.0411 0.0133  152 TYR   B OH  
6138 N  N   . LEU   B 153 ? 0.1591 0.1318 0.1663 -0.0263 -0.0077 -0.0135 153 LEU   B N   
6139 C  CA  . LEU   B 153 ? 0.1587 0.1297 0.1678 -0.0250 0.0002  -0.0122 153 LEU   B CA  
6140 C  C   . LEU   B 153 ? 0.1597 0.1294 0.1630 -0.0253 -0.0003 -0.0167 153 LEU   B C   
6141 O  O   . LEU   B 153 ? 0.1697 0.1566 0.1825 -0.0173 -0.0053 -0.0329 153 LEU   B O   
6142 C  CB  . LEU   B 153 ? 0.1624 0.1232 0.1767 -0.0270 0.0019  -0.0126 153 LEU   B CB  
6143 C  CG  . LEU   B 153 ? 0.1599 0.1407 0.2027 -0.0268 0.0063  -0.0069 153 LEU   B CG  
6144 C  CD1 . LEU   B 153 ? 0.1678 0.1528 0.2164 -0.0283 0.0139  0.0016  153 LEU   B CD1 
6145 C  CD2 . LEU   B 153 ? 0.1591 0.1521 0.1976 -0.0318 0.0179  -0.0021 153 LEU   B CD2 
6157 N  N   . ALA   B 154 ? 0.1541 0.1337 0.1819 -0.0092 -0.0060 -0.0159 154 ALA   B N   
6158 C  CA  . ALA   B 154 ? 0.1686 0.1467 0.1956 -0.0035 -0.0110 -0.0228 154 ALA   B CA  
6159 C  C   . ALA   B 154 ? 0.1851 0.1450 0.2108 0.0013  -0.0263 -0.0269 154 ALA   B C   
6160 O  O   . ALA   B 154 ? 0.2289 0.1473 0.2378 0.0076  -0.0256 -0.0152 154 ALA   B O   
6161 C  CB  . ALA   B 154 ? 0.1627 0.1668 0.2310 -0.0022 -0.0078 -0.0360 154 ALA   B CB  
6167 N  N   . VAL   B 155 ? 0.1507 0.1332 0.2347 -0.0031 0.0023  -0.0207 155 VAL   B N   
6168 C  CA  . VAL   B 155 ? 0.1449 0.1334 0.2524 -0.0047 -0.0036 -0.0136 155 VAL   B CA  
6169 C  C   . VAL   B 155 ? 0.1442 0.1425 0.2576 0.0029  -0.0068 -0.0291 155 VAL   B C   
6170 O  O   . VAL   B 155 ? 0.1564 0.1607 0.2870 0.0065  -0.0068 -0.0407 155 VAL   B O   
6171 C  CB  . VAL   B 155 ? 0.1545 0.1507 0.2776 -0.0079 -0.0160 -0.0020 155 VAL   B CB  
6172 C  CG1 . VAL   B 155 ? 0.1577 0.1494 0.2749 -0.0179 -0.0167 -0.0020 155 VAL   B CG1 
6173 C  CG2 . VAL   B 155 ? 0.1551 0.1659 0.3056 -0.0019 -0.0183 0.0193  155 VAL   B CG2 
6183 N  N   . PHE   B 156 ? 0.1376 0.1505 0.2767 0.0084  -0.0030 -0.0323 156 PHE   B N   
6184 C  CA  . PHE   B 156 ? 0.1409 0.1567 0.3037 0.0090  -0.0095 -0.0277 156 PHE   B CA  
6185 C  C   . PHE   B 156 ? 0.1340 0.1651 0.3311 0.0134  -0.0184 -0.0474 156 PHE   B C   
6186 O  O   . PHE   B 156 ? 0.1657 0.1871 0.3582 0.0247  -0.0036 -0.0517 156 PHE   B O   
6187 C  CB  . PHE   B 156 ? 0.1481 0.1548 0.2852 0.0035  -0.0152 -0.0231 156 PHE   B CB  
6188 C  CG  . PHE   B 156 ? 0.1513 0.1679 0.2863 0.0009  -0.0185 -0.0029 156 PHE   B CG  
6189 C  CD1 . PHE   B 156 ? 0.1576 0.1885 0.3268 0.0032  -0.0143 0.0340  156 PHE   B CD1 
6190 C  CD2 . PHE   B 156 ? 0.1575 0.1769 0.2798 0.0113  -0.0257 -0.0006 156 PHE   B CD2 
6191 C  CE1 . PHE   B 156 ? 0.1619 0.2068 0.3409 0.0106  -0.0104 0.0353  156 PHE   B CE1 
6192 C  CE2 . PHE   B 156 ? 0.1648 0.1972 0.3088 0.0146  -0.0233 0.0121  156 PHE   B CE2 
6193 C  CZ  . PHE   B 156 ? 0.1601 0.2052 0.3338 0.0188  -0.0207 0.0216  156 PHE   B CZ  
6203 N  N   . ASP   B 157 ? 0.1434 0.1542 0.3495 0.0120  -0.0292 -0.0301 157 ASP   B N   
6204 C  CA  . ASP   B 157 ? 0.1626 0.1609 0.3795 0.0108  -0.0228 -0.0322 157 ASP   B CA  
6205 C  C   . ASP   B 157 ? 0.1629 0.1631 0.3701 0.0101  -0.0213 -0.0599 157 ASP   B C   
6206 O  O   . ASP   B 157 ? 0.1443 0.1598 0.3613 0.0112  -0.0213 -0.0421 157 ASP   B O   
6207 C  CB  . ASP   B 157 ? 0.1920 0.1779 0.4051 0.0037  -0.0463 -0.0138 157 ASP   B CB  
6208 C  CG  . ASP   B 157 ? 0.2366 0.1990 0.4269 -0.0010 -0.0410 -0.0125 157 ASP   B CG  
6209 O  OD1 . ASP   B 157 ? 0.2411 0.1923 0.4399 0.0090  -0.0407 -0.0057 157 ASP   B OD1 
6210 O  OD2 . ASP   B 157 ? 0.2732 0.2188 0.4520 -0.0035 -0.0284 -0.0125 157 ASP   B OD2 
6215 N  N   A LYS   B 158 ? 0.1568 0.1844 0.3900 0.0056  -0.0078 -0.0865 158 LYS   B N   
6216 N  N   B LYS   B 158 ? 0.1769 0.1818 0.3556 0.0107  -0.0138 -0.0691 158 LYS   B N   
6217 C  CA  A LYS   B 158 ? 0.1704 0.2036 0.4035 0.0067  -0.0001 -0.1047 158 LYS   B CA  
6218 C  CA  B LYS   B 158 ? 0.1984 0.1996 0.3443 0.0147  -0.0106 -0.0750 158 LYS   B CA  
6219 C  C   A LYS   B 158 ? 0.1752 0.1905 0.4267 0.0075  -0.0148 -0.0941 158 LYS   B C   
6220 C  C   B LYS   B 158 ? 0.2005 0.1987 0.3396 0.0156  -0.0190 -0.0672 158 LYS   B C   
6221 O  O   A LYS   B 158 ? 0.1784 0.1859 0.4383 -0.0027 -0.0098 -0.1042 158 LYS   B O   
6222 O  O   B LYS   B 158 ? 0.2041 0.2007 0.3362 0.0111  -0.0174 -0.0684 158 LYS   B O   
6223 C  CB  A LYS   B 158 ? 0.1980 0.2484 0.4006 0.0089  0.0108  -0.1219 158 LYS   B CB  
6224 C  CB  B LYS   B 158 ? 0.2225 0.2224 0.3444 0.0174  -0.0036 -0.0850 158 LYS   B CB  
6225 C  CG  A LYS   B 158 ? 0.2305 0.2969 0.3979 0.0095  0.0152  -0.1273 158 LYS   B CG  
6226 C  CG  B LYS   B 158 ? 0.2461 0.2434 0.3487 0.0186  0.0017  -0.0886 158 LYS   B CG  
6227 C  CD  A LYS   B 158 ? 0.2503 0.3449 0.4029 0.0087  0.0209  -0.1199 158 LYS   B CD  
6228 C  CD  B LYS   B 158 ? 0.2647 0.2694 0.3604 0.0185  0.0070  -0.0844 158 LYS   B CD  
6229 C  CE  A LYS   B 158 ? 0.2674 0.3840 0.4122 0.0105  0.0187  -0.1094 158 LYS   B CE  
6230 C  CE  B LYS   B 158 ? 0.2793 0.2871 0.3717 0.0208  0.0078  -0.0802 158 LYS   B CE  
6231 N  NZ  A LYS   B 158 ? 0.2660 0.4024 0.4081 0.0071  0.0167  -0.1009 158 LYS   B NZ  
6232 N  NZ  B LYS   B 158 ? 0.2834 0.2952 0.3742 0.0203  0.0076  -0.0769 158 LYS   B NZ  
6259 N  N   A ASN   B 159 ? 0.1743 0.1800 0.4405 0.0110  -0.0400 -0.0693 159 ASN   B N   
6260 N  N   B ASN   B 159 ? 0.1974 0.1932 0.3451 0.0161  -0.0314 -0.0555 159 ASN   B N   
6261 C  CA  A ASN   B 159 ? 0.1903 0.1689 0.4485 0.0223  -0.0458 -0.0620 159 ASN   B CA  
6262 C  CA  B ASN   B 159 ? 0.1983 0.1865 0.3568 0.0213  -0.0360 -0.0525 159 ASN   B CA  
6263 C  C   A ASN   B 159 ? 0.1795 0.1562 0.4330 0.0121  -0.0556 -0.0518 159 ASN   B C   
6264 C  C   B ASN   B 159 ? 0.1821 0.1695 0.3769 0.0176  -0.0451 -0.0499 159 ASN   B C   
6265 O  O   A ASN   B 159 ? 0.1829 0.1460 0.4516 -0.0062 -0.0644 -0.0356 159 ASN   B O   
6266 O  O   B ASN   B 159 ? 0.1821 0.1641 0.3786 0.0155  -0.0441 -0.0443 159 ASN   B O   
6267 C  CB  A ASN   B 159 ? 0.2159 0.1890 0.4716 0.0292  -0.0491 -0.0628 159 ASN   B CB  
6268 C  CB  B ASN   B 159 ? 0.2126 0.2006 0.3530 0.0255  -0.0360 -0.0504 159 ASN   B CB  
6269 C  CG  A ASN   B 159 ? 0.2468 0.2117 0.5003 0.0301  -0.0577 -0.0682 159 ASN   B CG  
6270 C  CG  B ASN   B 159 ? 0.2290 0.2152 0.3614 0.0291  -0.0384 -0.0473 159 ASN   B CG  
6271 O  OD1 A ASN   B 159 ? 0.2663 0.2158 0.5076 0.0368  -0.0494 -0.0762 159 ASN   B OD1 
6272 O  OD1 B ASN   B 159 ? 0.2398 0.2200 0.3621 0.0344  -0.0337 -0.0446 159 ASN   B OD1 
6273 N  ND2 A ASN   B 159 ? 0.2512 0.2250 0.5140 0.0290  -0.0699 -0.0555 159 ASN   B ND2 
6274 N  ND2 B ASN   B 159 ? 0.2312 0.2231 0.3702 0.0305  -0.0433 -0.0404 159 ASN   B ND2 
6287 N  N   . LEU   B 160 ? 0.1647 0.1609 0.3978 0.0120  -0.0524 -0.0457 160 LEU   B N   
6288 C  CA  . LEU   B 160 ? 0.1608 0.1595 0.3696 0.0141  -0.0415 -0.0345 160 LEU   B CA  
6289 C  C   . LEU   B 160 ? 0.1554 0.1458 0.3703 0.0068  -0.0313 -0.0390 160 LEU   B C   
6290 O  O   . LEU   B 160 ? 0.1438 0.1510 0.3585 0.0053  -0.0328 -0.0183 160 LEU   B O   
6291 C  CB  . LEU   B 160 ? 0.1603 0.1636 0.3518 0.0073  -0.0427 -0.0264 160 LEU   B CB  
6292 C  CG  . LEU   B 160 ? 0.1588 0.1740 0.3250 0.0099  -0.0368 -0.0114 160 LEU   B CG  
6293 C  CD1 . LEU   B 160 ? 0.1780 0.1892 0.3253 0.0029  -0.0237 -0.0139 160 LEU   B CD1 
6294 C  CD2 . LEU   B 160 ? 0.1682 0.1793 0.3223 0.0256  -0.0346 -0.0152 160 LEU   B CD2 
6307 N  N   . TYR   B 161 ? 0.1556 0.1509 0.3778 0.0001  -0.0071 -0.0530 161 TYR   B N   
6308 C  CA  . TYR   B 161 ? 0.1600 0.1487 0.3493 -0.0115 0.0121  -0.0541 161 TYR   B CA  
6309 C  C   . TYR   B 161 ? 0.1644 0.1514 0.3391 -0.0088 0.0145  -0.0470 161 TYR   B C   
6310 O  O   . TYR   B 161 ? 0.1653 0.1519 0.3249 -0.0154 0.0138  -0.0400 161 TYR   B O   
6311 C  CB  . TYR   B 161 ? 0.1742 0.1556 0.3414 -0.0214 0.0296  -0.0535 161 TYR   B CB  
6312 C  CG  . TYR   B 161 ? 0.1974 0.1608 0.3307 -0.0276 0.0298  -0.0544 161 TYR   B CG  
6313 C  CD1 . TYR   B 161 ? 0.2020 0.1565 0.3277 -0.0368 0.0289  -0.0539 161 TYR   B CD1 
6314 C  CD2 . TYR   B 161 ? 0.2208 0.1735 0.3188 -0.0216 0.0211  -0.0560 161 TYR   B CD2 
6315 C  CE1 . TYR   B 161 ? 0.2213 0.1863 0.3338 -0.0383 0.0296  -0.0478 161 TYR   B CE1 
6316 C  CE2 . TYR   B 161 ? 0.2410 0.1967 0.3367 -0.0256 0.0257  -0.0567 161 TYR   B CE2 
6317 C  CZ  . TYR   B 161 ? 0.2399 0.1981 0.3297 -0.0425 0.0189  -0.0469 161 TYR   B CZ  
6318 O  OH  . TYR   B 161 ? 0.2721 0.2245 0.3445 -0.0471 0.0129  -0.0472 161 TYR   B OH  
6328 N  N   . ASP   B 162 ? 0.1705 0.1529 0.3628 -0.0061 -0.0008 -0.0627 162 ASP   B N   
6329 C  CA  . ASP   B 162 ? 0.1811 0.1551 0.3606 -0.0062 -0.0033 -0.0644 162 ASP   B CA  
6330 C  C   . ASP   B 162 ? 0.1819 0.1459 0.3418 -0.0108 -0.0080 -0.0471 162 ASP   B C   
6331 O  O   . ASP   B 162 ? 0.1834 0.1504 0.3407 -0.0146 -0.0261 -0.0313 162 ASP   B O   
6332 C  CB  . ASP   B 162 ? 0.2029 0.1710 0.3860 -0.0022 -0.0019 -0.0848 162 ASP   B CB  
6333 C  CG  . ASP   B 162 ? 0.2099 0.1986 0.4144 0.0103  0.0003  -0.0944 162 ASP   B CG  
6334 O  OD1 . ASP   B 162 ? 0.2082 0.2168 0.4027 -0.0006 0.0158  -0.0951 162 ASP   B OD1 
6335 O  OD2 . ASP   B 162 ? 0.2250 0.2217 0.4362 0.0289  -0.0048 -0.0920 162 ASP   B OD2 
6340 N  N   A LYS   B 163 ? 0.1793 0.1315 0.3309 -0.0107 -0.0316 -0.0376 163 LYS   B N   
6341 N  N   B LYS   B 163 ? 0.1860 0.1534 0.3334 -0.0110 -0.0179 -0.0320 163 LYS   B N   
6342 C  CA  A LYS   B 163 ? 0.1871 0.1404 0.3392 -0.0189 -0.0229 -0.0171 163 LYS   B CA  
6343 C  CA  B LYS   B 163 ? 0.1945 0.1695 0.3361 -0.0136 -0.0150 -0.0159 163 LYS   B CA  
6344 C  C   A LYS   B 163 ? 0.1561 0.1406 0.3367 -0.0203 -0.0231 -0.0002 163 LYS   B C   
6345 C  C   B LYS   B 163 ? 0.1684 0.1548 0.3257 -0.0155 -0.0158 -0.0056 163 LYS   B C   
6346 O  O   A LYS   B 163 ? 0.1530 0.1500 0.3662 -0.0237 -0.0185 0.0047  163 LYS   B O   
6347 O  O   B LYS   B 163 ? 0.1684 0.1591 0.3361 -0.0177 -0.0115 -0.0027 163 LYS   B O   
6348 C  CB  A LYS   B 163 ? 0.2339 0.1701 0.3708 -0.0193 -0.0160 -0.0013 163 LYS   B CB  
6349 C  CB  B LYS   B 163 ? 0.2304 0.2052 0.3627 -0.0135 -0.0142 -0.0071 163 LYS   B CB  
6350 C  CG  A LYS   B 163 ? 0.3043 0.2316 0.4118 -0.0238 -0.0054 0.0056  163 LYS   B CG  
6351 C  CG  B LYS   B 163 ? 0.2740 0.2453 0.3941 -0.0157 -0.0114 -0.0016 163 LYS   B CG  
6352 C  CD  A LYS   B 163 ? 0.3656 0.2811 0.4564 -0.0313 -0.0066 0.0011  163 LYS   B CD  
6353 C  CD  B LYS   B 163 ? 0.3122 0.2834 0.4293 -0.0191 -0.0122 -0.0005 163 LYS   B CD  
6354 C  CE  A LYS   B 163 ? 0.4101 0.3216 0.4783 -0.0326 -0.0048 -0.0005 163 LYS   B CE  
6355 C  CE  B LYS   B 163 ? 0.3391 0.3173 0.4518 -0.0205 -0.0114 0.0010  163 LYS   B CE  
6356 N  NZ  A LYS   B 163 ? 0.4417 0.3431 0.4957 -0.0316 -0.0023 -0.0060 163 LYS   B NZ  
6357 N  NZ  B LYS   B 163 ? 0.3570 0.3264 0.4668 -0.0202 -0.0104 -0.0000 163 LYS   B NZ  
6384 N  N   . LEU   B 164 ? 0.1511 0.1389 0.3115 -0.0135 -0.0167 -0.0066 164 LEU   B N   
6385 C  CA  . LEU   B 164 ? 0.1513 0.1421 0.2943 -0.0083 -0.0210 0.0028  164 LEU   B CA  
6386 C  C   . LEU   B 164 ? 0.1598 0.1369 0.2947 -0.0147 -0.0344 0.0100  164 LEU   B C   
6387 O  O   . LEU   B 164 ? 0.1586 0.1540 0.3108 -0.0137 -0.0293 0.0030  164 LEU   B O   
6388 C  CB  . LEU   B 164 ? 0.1484 0.1397 0.2716 -0.0126 -0.0185 -0.0048 164 LEU   B CB  
6389 C  CG  . LEU   B 164 ? 0.1551 0.1561 0.2748 -0.0128 -0.0061 0.0058  164 LEU   B CG  
6390 C  CD1 . LEU   B 164 ? 0.1685 0.1503 0.2741 -0.0211 -0.0158 -0.0007 164 LEU   B CD1 
6391 C  CD2 . LEU   B 164 ? 0.1691 0.1890 0.2951 -0.0121 0.0039  -0.0159 164 LEU   B CD2 
6404 N  N   . VAL   B 165 ? 0.1889 0.1475 0.3118 -0.0262 -0.0372 -0.0063 165 VAL   B N   
6405 C  CA  . VAL   B 165 ? 0.2277 0.1634 0.3082 -0.0356 -0.0599 -0.0028 165 VAL   B CA  
6406 C  C   . VAL   B 165 ? 0.2559 0.1730 0.3443 -0.0456 -0.0938 0.0024  165 VAL   B C   
6407 O  O   . VAL   B 165 ? 0.2786 0.1903 0.3570 -0.0495 -0.0983 0.0145  165 VAL   B O   
6408 C  CB  . VAL   B 165 ? 0.2508 0.1845 0.3066 -0.0206 -0.0311 -0.0306 165 VAL   B CB  
6409 C  CG1 . VAL   B 165 ? 0.2656 0.1901 0.3346 -0.0219 -0.0199 -0.0319 165 VAL   B CG1 
6410 C  CG2 . VAL   B 165 ? 0.2490 0.1892 0.2885 -0.0212 -0.0219 -0.0324 165 VAL   B CG2 
6420 N  N   . SER   B 166 ? 0.2690 0.1574 0.3957 -0.0443 -0.1013 -0.0201 166 SER   B N   
6421 C  CA  . SER   B 166 ? 0.2668 0.1629 0.4615 -0.0424 -0.0879 -0.0298 166 SER   B CA  
6422 C  C   . SER   B 166 ? 0.2470 0.1851 0.4791 -0.0457 -0.0802 0.0016  166 SER   B C   
6423 O  O   . SER   B 166 ? 0.2481 0.2038 0.5149 -0.0626 -0.0857 -0.0379 166 SER   B O   
6424 C  CB  . SER   B 166 ? 0.2661 0.1704 0.4926 -0.0314 -0.0828 -0.0350 166 SER   B CB  
6425 O  OG  . SER   B 166 ? 0.2503 0.1694 0.5050 -0.0225 -0.0868 -0.0140 166 SER   B OG  
6431 N  N   . SER   B 167 ? 0.2233 0.1768 0.4427 -0.0415 -0.0917 0.0494  167 SER   B N   
6432 C  CA  . SER   B 167 ? 0.2180 0.1841 0.4330 -0.0394 -0.0594 0.0461  167 SER   B CA  
6433 C  C   . SER   B 167 ? 0.2064 0.1927 0.4162 -0.0484 -0.0517 0.0625  167 SER   B C   
6434 O  O   . SER   B 167 ? 0.2072 0.2092 0.4076 -0.0556 -0.0518 0.0609  167 SER   B O   
6435 C  CB  . SER   B 167 ? 0.2074 0.1860 0.4317 -0.0420 -0.0300 0.0376  167 SER   B CB  
6436 O  OG  . SER   B 167 ? 0.2026 0.1935 0.4118 -0.0341 -0.0144 0.0387  167 SER   B OG  
6442 N  N   . PHE   B 168 ? 0.2031 0.1905 0.4064 -0.0424 -0.0334 0.0674  168 PHE   B N   
6443 C  CA  . PHE   B 168 ? 0.2058 0.1823 0.3626 -0.0477 -0.0256 0.0491  168 PHE   B CA  
6444 C  C   . PHE   B 168 ? 0.1778 0.1714 0.2962 -0.0262 -0.0128 0.0287  168 PHE   B C   
6445 O  O   . PHE   B 168 ? 0.2057 0.1601 0.2881 -0.0023 -0.0106 0.0005  168 PHE   B O   
6446 C  CB  . PHE   B 168 ? 0.2247 0.1879 0.3690 -0.0571 -0.0417 0.0598  168 PHE   B CB  
6447 C  CG  . PHE   B 168 ? 0.2487 0.1700 0.3569 -0.0634 -0.0393 0.0420  168 PHE   B CG  
6448 C  CD1 . PHE   B 168 ? 0.2780 0.1804 0.3644 -0.0587 -0.0542 0.0370  168 PHE   B CD1 
6449 C  CD2 . PHE   B 168 ? 0.2374 0.1631 0.3512 -0.0589 -0.0388 0.0500  168 PHE   B CD2 
6450 C  CE1 . PHE   B 168 ? 0.2887 0.1821 0.3582 -0.0457 -0.0475 0.0550  168 PHE   B CE1 
6451 C  CE2 . PHE   B 168 ? 0.2653 0.1732 0.3602 -0.0436 -0.0478 0.0424  168 PHE   B CE2 
6452 C  CZ  . PHE   B 168 ? 0.2765 0.1677 0.3557 -0.0348 -0.0538 0.0587  168 PHE   B CZ  
6462 N  N   . LEU   B 169 ? 0.2024 0.1919 0.2903 0.0044  0.0012  0.0101  169 LEU   B N   
6463 C  CA  . LEU   B 169 ? 0.2366 0.2238 0.3238 -0.0003 0.0055  -0.0311 169 LEU   B CA  
6464 C  C   . LEU   B 169 ? 0.2640 0.2506 0.3863 0.0098  0.0041  -0.0588 169 LEU   B C   
6465 O  O   . LEU   B 169 ? 0.2829 0.2688 0.4353 0.0058  0.0106  -0.0788 169 LEU   B O   
6466 C  CB  . LEU   B 169 ? 0.2627 0.2608 0.3305 -0.0075 -0.0076 -0.0087 169 LEU   B CB  
6467 C  CG  . LEU   B 169 ? 0.3069 0.2944 0.3693 0.0007  -0.0077 -0.0006 169 LEU   B CG  
6468 C  CD1 . LEU   B 169 ? 0.3194 0.3118 0.3698 0.0009  -0.0076 0.0186  169 LEU   B CD1 
6469 C  CD2 . LEU   B 169 ? 0.3090 0.3024 0.3805 0.0115  0.0061  -0.0148 169 LEU   B CD2 
6470 O  OXT . LEU   B 169 ? 0.2783 0.2653 0.3867 0.0353  0.0101  -0.0658 169 LEU   B OXT 
6482 N  N2  B A1BBM C .   ? 0.1212 0.1648 0.1821 -0.0219 -0.0171 -0.0072 201 A1BBM A N2  
6483 C  C3  B A1BBM C .   ? 0.1226 0.1542 0.1758 -0.0108 -0.0074 0.0129  201 A1BBM A C3  
6484 C  C6  B A1BBM C .   ? 0.1152 0.1543 0.1822 -0.0083 0.0008  0.0249  201 A1BBM A C6  
6485 C  C9  B A1BBM C .   ? 0.1458 0.1532 0.1976 -0.0122 -0.0130 0.0151  201 A1BBM A C9  
6486 C  C12 B A1BBM C .   ? 0.1516 0.1543 0.1988 -0.0076 -0.0061 0.0281  201 A1BBM A C12 
6487 C  C1  B A1BBM C .   ? 0.1404 0.1434 0.1916 -0.0181 -0.0060 0.0241  201 A1BBM A C1  
6488 C  C10 B A1BBM C .   ? 0.1506 0.1747 0.2013 -0.0152 -0.0237 0.0154  201 A1BBM A C10 
6489 C  C11 B A1BBM C .   ? 0.1609 0.1721 0.2044 -0.0090 -0.0103 0.0169  201 A1BBM A C11 
6490 C  C2  B A1BBM C .   ? 0.1126 0.1292 0.1956 -0.0120 0.0053  0.0227  201 A1BBM A C2  
6491 C  C4  B A1BBM C .   ? 0.1176 0.1706 0.1786 -0.0146 -0.0126 0.0032  201 A1BBM A C4  
6492 C  C5  B A1BBM C .   ? 0.1166 0.1573 0.1834 -0.0096 0.0000  0.0126  201 A1BBM A C5  
6493 C  C7  B A1BBM C .   ? 0.1024 0.1538 0.1864 -0.0112 0.0051  0.0282  201 A1BBM A C7  
6494 C  C8  B A1BBM C .   ? 0.0959 0.1484 0.1946 -0.0123 -0.0083 0.0214  201 A1BBM A C8  
6495 N  N1  B A1BBM C .   ? 0.1223 0.1379 0.1870 -0.0109 -0.0044 0.0209  201 A1BBM A N1  
6496 N  N3  B A1BBM C .   ? 0.1256 0.1664 0.1778 -0.0163 0.0075  0.0212  201 A1BBM A N3  
6497 N  N4  B A1BBM C .   ? 0.1118 0.1570 0.1918 0.0019  -0.0079 0.0111  201 A1BBM A N4  
6498 O  O1  B A1BBM C .   ? 0.1618 0.1409 0.1736 -0.0251 -0.0166 0.0212  201 A1BBM A O1  
6499 S  S1  B A1BBM C .   ? 0.1565 0.1834 0.2116 -0.0149 -0.0276 0.0137  201 A1BBM A S1  
6516 CL CL  B CL    D .   ? 0.1685 0.1363 0.2157 -0.0250 -0.0023 0.0137  202 CL    A CL  
6517 O  O   . HOH   E .   ? 0.4304 0.8678 0.4989 -0.1300 0.0755  -0.0149 301 HOH   A O   
6518 O  O   . HOH   E .   ? 0.6428 0.4927 0.6853 -0.0731 0.1903  0.2519  302 HOH   A O   
6519 O  O   . HOH   E .   ? 0.3163 0.2790 0.4743 -0.0402 -0.1288 0.1342  303 HOH   A O   
6520 O  O   . HOH   E .   ? 0.4737 0.3837 0.5780 -0.0137 0.1857  -0.0497 304 HOH   A O   
6521 O  O   . HOH   E .   ? 0.7971 0.7278 0.3628 -0.1325 -0.0236 0.2382  305 HOH   A O   
6522 O  O   . HOH   E .   ? 0.3177 0.2493 0.4739 -0.0193 0.0113  0.0554  306 HOH   A O   
6523 O  O   . HOH   E .   ? 0.6597 0.5759 0.5659 -0.1037 0.2042  0.2304  307 HOH   A O   
6524 O  O   . HOH   E .   ? 0.2170 0.1787 0.2452 0.0229  -0.0387 -0.0047 308 HOH   A O   
6525 O  O   . HOH   E .   ? 0.6770 0.5385 0.3521 0.2236  -0.1493 0.0673  309 HOH   A O   
6526 O  O   . HOH   E .   ? 0.3443 0.3344 0.1657 -0.0495 0.0416  0.0314  310 HOH   A O   
6527 O  O   . HOH   E .   ? 0.3038 0.6755 0.6428 -0.0575 -0.0778 0.2494  311 HOH   A O   
6528 O  O   . HOH   E .   ? 0.2684 0.5746 0.4045 -0.0115 -0.0375 0.0907  312 HOH   A O   
6529 O  O   . HOH   E .   ? 0.6520 0.5957 0.3756 -0.0819 -0.0679 0.1038  313 HOH   A O   
6530 O  O   . HOH   E .   ? 0.4320 0.2153 0.2229 -0.0436 0.0206  -0.0074 314 HOH   A O   
6531 O  O   . HOH   E .   ? 0.2728 0.3928 0.3544 -0.0882 -0.0392 -0.0530 315 HOH   A O   
6532 O  O   . HOH   E .   ? 0.1803 0.4930 0.3381 0.0945  0.0100  0.0756  316 HOH   A O   
6533 O  O   . HOH   E .   ? 0.2105 0.1964 0.3896 -0.0513 0.0220  -0.0187 317 HOH   A O   
6534 O  O   . HOH   E .   ? 0.2227 0.2263 0.3495 0.0195  -0.0544 0.0204  318 HOH   A O   
6535 O  O   . HOH   E .   ? 0.5738 0.3805 0.4983 0.1217  0.0493  0.0788  319 HOH   A O   
6536 O  O   . HOH   E .   ? 0.4945 0.2107 0.5748 0.0719  -0.0150 -0.0108 320 HOH   A O   
6537 O  O   . HOH   E .   ? 0.6392 0.5209 0.5714 -0.1422 0.0140  0.1635  321 HOH   A O   
6538 O  O   . HOH   E .   ? 0.2978 0.6897 0.6490 0.1624  0.1095  0.2154  322 HOH   A O   
6539 O  O   . HOH   E .   ? 0.4116 0.3552 0.3352 -0.1501 -0.0002 0.0685  323 HOH   A O   
6540 O  O   . HOH   E .   ? 0.5217 0.6217 0.3936 0.2435  -0.0052 -0.0758 324 HOH   A O   
6541 O  O   . HOH   E .   ? 0.2078 0.3343 0.4482 -0.0243 0.0352  -0.0732 325 HOH   A O   
6542 O  O   . HOH   E .   ? 1.0250 0.5284 0.6858 -0.0443 -0.1351 0.0612  326 HOH   A O   
6543 O  O   . HOH   E .   ? 0.2575 0.2369 0.3607 -0.0205 0.0926  0.0577  327 HOH   A O   
6544 O  O   . HOH   E .   ? 0.2962 0.4804 0.6500 -0.0334 0.0964  0.2545  328 HOH   A O   
6545 O  O   . HOH   E .   ? 0.5556 0.3365 0.2853 -0.0772 0.0909  0.0272  329 HOH   A O   
6546 O  O   . HOH   E .   ? 0.6305 0.6305 0.4660 -0.0540 -0.1097 -0.1060 330 HOH   A O   
6547 O  O   . HOH   E .   ? 0.4998 0.4703 0.3175 -0.1287 -0.1130 -0.0379 331 HOH   A O   
6548 O  O   . HOH   E .   ? 0.1707 0.1647 0.2317 -0.0237 0.0046  0.0044  332 HOH   A O   
6549 O  O   . HOH   E .   ? 0.3470 0.4344 0.2645 -0.0604 0.0594  0.0570  333 HOH   A O   
6550 O  O   . HOH   E .   ? 0.5543 0.5006 0.6175 0.0111  -0.1215 -0.0209 334 HOH   A O   
6551 O  O   . HOH   E .   ? 0.2222 0.4461 0.4790 -0.0575 -0.0912 0.2165  335 HOH   A O   
6552 O  O   . HOH   E .   ? 0.5572 0.5398 0.4786 0.0220  -0.0855 -0.0960 336 HOH   A O   
6553 O  O   . HOH   E .   ? 0.4088 0.3870 0.3789 -0.0435 0.1802  0.0346  337 HOH   A O   
6554 O  O   . HOH   E .   ? 0.5004 0.2013 0.4412 0.0318  -0.1222 0.0314  338 HOH   A O   
6555 O  O   . HOH   E .   ? 0.4532 0.3917 0.5101 -0.1660 -0.0093 0.2000  339 HOH   A O   
6556 O  O   . HOH   E .   ? 0.1822 0.1724 0.2088 0.0146  -0.0260 0.0224  340 HOH   A O   
6557 O  O   . HOH   E .   ? 0.2305 0.2056 0.3025 0.0326  0.0217  0.0295  341 HOH   A O   
6558 O  O   . HOH   E .   ? 0.5529 0.5470 0.3068 -0.0983 0.1666  0.1105  342 HOH   A O   
6559 O  O   . HOH   E .   ? 0.1531 0.3424 0.3054 -0.0063 0.0193  0.0344  343 HOH   A O   
6560 O  O   . HOH   E .   ? 0.1724 0.1692 0.2617 -0.0156 0.0206  0.0375  344 HOH   A O   
6561 O  O   . HOH   E .   ? 0.1579 0.1846 0.3214 0.0067  -0.0318 -0.0480 345 HOH   A O   
6562 O  O   A HOH   E .   ? 0.2188 0.4798 0.2319 0.1077  -0.0136 -0.0064 346 HOH   A O   
6563 O  O   . HOH   E .   ? 0.3411 0.4090 0.2342 -0.1151 -0.0351 -0.0557 347 HOH   A O   
6564 O  O   . HOH   E .   ? 0.4748 0.4772 0.6015 0.1787  0.1342  -0.0653 348 HOH   A O   
6565 O  O   . HOH   E .   ? 0.2520 0.2072 0.2560 -0.0318 0.0236  -0.0007 349 HOH   A O   
6566 O  O   . HOH   E .   ? 0.6137 0.4975 0.5348 0.0293  0.2554  -0.0689 350 HOH   A O   
6567 O  O   . HOH   E .   ? 0.1529 0.2346 0.2302 0.0069  -0.0050 0.0571  351 HOH   A O   
6568 O  O   A HOH   E .   ? 0.1474 0.3073 0.2032 0.0590  0.0320  0.0803  352 HOH   A O   
6569 O  O   . HOH   E .   ? 0.2089 0.2101 0.3568 0.0228  0.0924  -0.0019 353 HOH   A O   
6570 O  O   . HOH   E .   ? 0.2573 0.4135 0.3390 -0.0466 0.0367  0.0207  354 HOH   A O   
6571 O  O   . HOH   E .   ? 0.5880 0.3697 0.3140 0.0455  0.0944  0.1175  355 HOH   A O   
6572 O  O   . HOH   E .   ? 0.2890 0.3405 0.4774 -0.0442 -0.0944 -0.1030 356 HOH   A O   
6573 O  O   . HOH   E .   ? 0.2497 0.4262 0.3577 0.1067  -0.0712 -0.0078 357 HOH   A O   
6574 O  O   . HOH   E .   ? 0.1473 0.1942 0.2666 0.0108  -0.0080 0.0095  358 HOH   A O   
6575 O  O   . HOH   E .   ? 0.1348 0.1332 0.1609 0.0001  0.0098  0.0130  359 HOH   A O   
6576 O  O   . HOH   E .   ? 0.3703 0.4633 0.4057 0.1824  0.0526  0.0315  360 HOH   A O   
6577 O  O   B HOH   E .   ? 0.1756 0.2149 0.1964 -0.0261 -0.0643 -0.0347 361 HOH   A O   
6578 O  O   . HOH   E .   ? 0.5671 0.2932 0.4612 -0.1700 0.2379  -0.0859 362 HOH   A O   
6579 O  O   . HOH   E .   ? 0.1997 0.2181 0.2458 -0.0375 0.0091  0.0401  363 HOH   A O   
6580 O  O   . HOH   E .   ? 0.2538 0.3376 0.3794 -0.0390 0.0801  -0.0593 364 HOH   A O   
6581 O  O   . HOH   E .   ? 0.1822 0.2252 0.1973 -0.0128 0.0023  0.0695  365 HOH   A O   
6582 O  O   . HOH   E .   ? 0.1572 0.1685 0.1701 -0.0055 -0.0152 0.0026  366 HOH   A O   
6583 O  O   . HOH   E .   ? 0.1702 0.1470 0.2380 -0.0167 0.0178  -0.0142 367 HOH   A O   
6584 O  O   . HOH   E .   ? 0.3370 0.2957 0.4023 -0.0775 -0.0193 -0.0157 368 HOH   A O   
6585 O  O   . HOH   E .   ? 0.4447 0.2288 0.2765 0.1336  0.0401  0.0251  369 HOH   A O   
6586 O  O   . HOH   E .   ? 0.3535 0.4808 0.3441 0.0042  -0.0463 0.0928  370 HOH   A O   
6587 O  O   . HOH   E .   ? 0.2085 0.2704 0.3762 0.0390  0.0927  -0.0479 371 HOH   A O   
6588 O  O   . HOH   E .   ? 0.4208 0.7034 0.5210 -0.0739 -0.1469 0.0518  372 HOH   A O   
6589 O  O   . HOH   E .   ? 0.5655 0.6305 0.7157 -0.0835 -0.1081 0.1209  373 HOH   A O   
6590 O  O   . HOH   E .   ? 0.4701 0.4246 0.6183 0.1473  0.1057  -0.1317 374 HOH   A O   
6591 O  O   . HOH   E .   ? 0.4248 0.2310 0.4533 -0.1055 0.0779  0.0197  375 HOH   A O   
6592 O  O   . HOH   E .   ? 0.2014 0.2271 0.2360 -0.0256 -0.0323 0.0395  376 HOH   A O   
6593 O  O   . HOH   E .   ? 0.2855 0.6789 0.3388 0.1040  0.0473  -0.1023 377 HOH   A O   
6594 O  O   . HOH   E .   ? 0.5983 0.6885 0.6384 -0.0280 0.0708  -0.0205 378 HOH   A O   
6595 O  O   . HOH   E .   ? 0.1678 0.1710 0.2004 0.0037  -0.0254 0.0058  379 HOH   A O   
6596 O  O   . HOH   E .   ? 0.2552 0.2018 0.2045 -0.0544 0.0132  0.0323  380 HOH   A O   
6597 O  O   . HOH   E .   ? 0.2754 0.4484 0.3555 0.0789  0.0953  0.1987  381 HOH   A O   
6598 O  O   A HOH   E .   ? 0.2285 0.2879 0.3324 -0.0073 -0.0572 -0.0591 382 HOH   A O   
6599 O  O   . HOH   E .   ? 1.0622 1.1254 0.7923 0.0325  -0.0284 -0.0950 383 HOH   A O   
6600 O  O   . HOH   E .   ? 0.2083 0.1884 0.2014 0.0042  0.0148  0.0140  384 HOH   A O   
6601 O  O   . HOH   E .   ? 0.3298 0.2475 0.3484 -0.0106 -0.0409 0.0801  385 HOH   A O   
6602 O  O   A HOH   E .   ? 0.2325 0.1484 0.2919 0.0139  -0.0290 -0.0086 386 HOH   A O   
6603 O  O   . HOH   E .   ? 0.3354 0.3001 0.2362 0.0275  0.0768  -0.0093 387 HOH   A O   
6604 O  O   . HOH   E .   ? 0.3138 0.2664 0.2481 -0.0646 -0.0892 0.0275  388 HOH   A O   
6605 O  O   . HOH   E .   ? 0.2094 0.2186 0.2932 -0.0196 -0.0205 0.0779  389 HOH   A O   
6606 O  O   . HOH   E .   ? 0.3169 0.2317 0.5406 -0.0461 -0.0063 -0.0201 390 HOH   A O   
6607 O  O   . HOH   E .   ? 0.2472 0.2737 0.3678 0.0190  0.0043  0.1079  391 HOH   A O   
6608 O  O   . HOH   E .   ? 0.3007 0.3308 0.3918 -0.1018 0.1077  -0.0343 392 HOH   A O   
6609 O  O   . HOH   E .   ? 0.4546 0.4861 0.3795 0.1754  -0.0933 -0.1678 393 HOH   A O   
6610 O  O   . HOH   E .   ? 0.1404 0.1473 0.1941 -0.0009 -0.0186 0.0029  394 HOH   A O   
6611 O  O   . HOH   E .   ? 0.1888 0.1427 0.1773 -0.0222 0.0139  0.0036  395 HOH   A O   
6612 O  O   . HOH   E .   ? 0.1501 0.1746 0.2022 0.0087  -0.0237 -0.0265 396 HOH   A O   
6613 O  O   . HOH   E .   ? 0.1561 0.1802 0.3223 0.0011  0.0060  0.0308  397 HOH   A O   
6614 O  O   . HOH   E .   ? 0.2850 0.3965 0.3518 -0.0250 0.0989  -0.0786 398 HOH   A O   
6615 O  O   . HOH   E .   ? 0.5445 0.7077 0.6064 0.1028  -0.0445 0.0328  399 HOH   A O   
6616 O  O   . HOH   E .   ? 0.1764 0.2514 0.3753 -0.0257 0.0706  0.0275  400 HOH   A O   
6617 O  O   B HOH   E .   ? 0.1853 0.2545 0.1759 -0.0211 -0.0058 0.0381  401 HOH   A O   
6618 O  O   . HOH   E .   ? 0.3171 0.3831 0.5385 -0.0452 0.1562  -0.0250 402 HOH   A O   
6619 O  O   . HOH   E .   ? 0.2783 0.1934 0.2730 0.0151  0.0278  0.0197  403 HOH   A O   
6620 O  O   . HOH   E .   ? 0.2357 0.1852 0.3113 0.0080  -0.0314 0.0120  404 HOH   A O   
6621 O  O   . HOH   E .   ? 0.1913 0.2015 0.3507 0.0407  0.0953  0.0833  405 HOH   A O   
6622 O  O   . HOH   E .   ? 0.2257 0.2639 0.3525 -0.0224 -0.0228 0.0291  406 HOH   A O   
6623 O  O   A HOH   E .   ? 0.3131 0.3021 0.4303 -0.0299 0.1103  0.0429  407 HOH   A O   
6624 O  O   A HOH   E .   ? 0.3710 0.2824 0.2073 0.0485  -0.0950 -0.0254 408 HOH   A O   
6625 O  O   . HOH   E .   ? 0.3690 0.5948 0.4078 -0.0676 0.0436  0.1275  409 HOH   A O   
6626 O  O   . HOH   E .   ? 0.4068 0.5823 0.6094 0.0664  -0.0465 0.1887  410 HOH   A O   
6627 O  O   B HOH   E .   ? 0.0996 0.1515 0.2475 -0.0112 0.0252  0.0674  411 HOH   A O   
6628 O  O   . HOH   E .   ? 0.5712 0.5057 0.2364 0.0432  0.1121  0.1169  412 HOH   A O   
6629 O  O   . HOH   E .   ? 0.2334 0.2854 0.2805 -0.0118 -0.0707 0.0543  413 HOH   A O   
6630 O  O   . HOH   E .   ? 0.4129 0.6253 0.3628 -0.0807 -0.0187 0.1438  414 HOH   A O   
6631 O  O   . HOH   E .   ? 0.2248 0.2014 0.2980 0.0136  -0.0665 0.0191  415 HOH   A O   
6632 O  O   . HOH   E .   ? 0.2829 0.6511 0.1840 -0.0382 0.0327  0.0117  416 HOH   A O   
6633 O  O   . HOH   E .   ? 0.2207 0.1720 0.1703 -0.0118 0.0130  0.0160  417 HOH   A O   
6634 O  O   . HOH   E .   ? 0.2590 0.2144 0.2919 -0.0496 0.0028  0.0480  418 HOH   A O   
6635 O  O   . HOH   E .   ? 0.5945 0.2827 0.3116 -0.1553 0.0402  0.0420  419 HOH   A O   
6636 O  O   . HOH   E .   ? 0.5996 0.7797 0.4196 0.0612  0.2756  -0.0863 420 HOH   A O   
6637 O  O   . HOH   E .   ? 0.3332 0.1352 0.2303 -0.0065 -0.0508 0.0177  421 HOH   A O   
6638 O  O   . HOH   E .   ? 0.3946 0.2739 0.5163 0.0730  0.0837  0.0225  422 HOH   A O   
6639 O  O   . HOH   E .   ? 0.1756 0.2061 0.2719 -0.0155 0.0006  0.0365  423 HOH   A O   
6640 O  O   . HOH   E .   ? 0.2336 0.2711 0.3776 0.0083  -0.0319 -0.0379 424 HOH   A O   
6641 O  O   . HOH   E .   ? 0.2946 0.3718 0.7420 -0.0168 0.0991  -0.0666 425 HOH   A O   
6642 O  O   . HOH   E .   ? 0.2465 0.4504 0.2825 0.1707  -0.0081 0.0221  426 HOH   A O   
6643 O  O   . HOH   E .   ? 0.5274 0.6650 0.6874 0.3262  0.1327  0.1621  427 HOH   A O   
6644 O  O   . HOH   E .   ? 0.3960 0.2417 0.5728 -0.0813 -0.2415 0.1118  428 HOH   A O   
6645 O  O   . HOH   E .   ? 0.7060 0.5800 0.7247 -0.1526 -0.0025 -0.1270 429 HOH   A O   
6646 O  O   A HOH   E .   ? 0.3609 0.2071 0.3567 0.0457  0.0982  0.0746  430 HOH   A O   
6647 O  O   . HOH   E .   ? 0.7085 0.4646 0.5917 0.2120  -0.0840 0.1700  431 HOH   A O   
6648 O  O   . HOH   E .   ? 0.5641 0.7335 0.7592 0.0140  -0.0895 -0.0330 432 HOH   A O   
6649 O  O   A HOH   E .   ? 0.2106 0.1227 0.1311 -0.0004 -0.0006 0.0145  433 HOH   A O   
6650 O  O   . HOH   E .   ? 0.4802 0.4820 0.3740 -0.0356 -0.1504 0.0158  434 HOH   A O   
6651 O  O   . HOH   E .   ? 0.2750 0.3305 0.4978 -0.0172 0.0730  -0.1198 435 HOH   A O   
6652 O  O   . HOH   E .   ? 0.3685 0.2870 0.1823 -0.0765 0.0240  0.0367  436 HOH   A O   
6653 O  O   . HOH   E .   ? 0.7479 0.7523 0.4715 0.2206  -0.1192 0.1948  437 HOH   A O   
6654 O  O   . HOH   E .   ? 0.2833 0.1801 0.2948 0.0176  0.0042  0.0108  438 HOH   A O   
6655 O  O   . HOH   E .   ? 0.2014 0.2164 0.4503 -0.0211 -0.0805 0.0467  439 HOH   A O   
6656 O  O   B HOH   E .   ? 0.3751 0.2503 0.2566 0.0351  -0.0982 -0.0086 440 HOH   A O   
6657 O  O   . HOH   E .   ? 0.4577 0.3587 0.3005 0.2371  -0.0539 -0.0390 441 HOH   A O   
6658 O  O   . HOH   E .   ? 0.7831 0.6049 0.6433 0.0604  -0.1063 -0.0153 442 HOH   A O   
6659 O  O   . HOH   E .   ? 0.2439 0.3095 0.2416 0.0130  -0.0090 -0.0366 443 HOH   A O   
6660 O  O   . HOH   E .   ? 0.2290 0.2142 0.2883 0.0195  0.0391  0.0283  444 HOH   A O   
6661 O  O   A HOH   E .   ? 0.1890 0.1514 0.2853 0.0094  -0.0547 -0.0226 445 HOH   A O   
6662 O  O   . HOH   E .   ? 0.5587 1.0752 0.6613 0.0216  -0.0703 0.1222  446 HOH   A O   
6663 O  O   . HOH   E .   ? 0.5065 0.5166 0.5440 -0.0796 -0.1110 -0.1401 447 HOH   A O   
6664 O  O   . HOH   E .   ? 0.5530 0.4862 0.7059 0.0149  -0.0134 -0.1548 448 HOH   A O   
6665 O  O   B HOH   E .   ? 0.2804 0.3375 0.3453 -0.1084 -0.0489 -0.1374 449 HOH   A O   
6666 O  O   B HOH   E .   ? 0.1453 0.1903 0.2188 -0.0180 -0.0461 0.0377  450 HOH   A O   
6667 O  O   A HOH   E .   ? 0.2689 0.1945 0.3558 0.0269  0.0684  0.0870  451 HOH   A O   
6668 O  O   . HOH   E .   ? 0.7393 0.6176 0.8363 0.0462  -0.0929 0.2133  452 HOH   A O   
6669 O  O   . HOH   E .   ? 0.5148 0.4491 0.3655 0.0552  0.0465  0.0689  453 HOH   A O   
6670 O  O   . HOH   E .   ? 0.6932 0.6312 0.5262 -0.1040 0.1678  0.0669  454 HOH   A O   
6671 O  O   . HOH   E .   ? 0.2891 0.2873 0.3734 -0.0439 0.0356  -0.0770 455 HOH   A O   
6672 O  O   . HOH   E .   ? 0.4797 0.3271 0.4106 0.0524  0.1062  0.0021  456 HOH   A O   
6673 O  O   . HOH   E .   ? 0.2819 0.3423 0.3666 0.0832  -0.0231 0.0707  457 HOH   A O   
6674 O  O   . HOH   E .   ? 0.4914 0.4454 0.4605 0.0502  -0.0405 0.0705  458 HOH   A O   
6675 O  O   . HOH   E .   ? 0.3511 0.5731 0.5417 -0.1431 0.1268  -0.1217 459 HOH   A O   
6676 O  O   . HOH   E .   ? 0.7424 0.7614 0.4738 0.0728  -0.1156 -0.0709 460 HOH   A O   
6677 O  O   . HOH   E .   ? 0.6820 0.6342 0.6305 0.1363  0.2113  0.2099  461 HOH   A O   
6678 O  O   . HOH   E .   ? 0.3669 0.5761 0.5275 0.0738  -0.0783 0.1935  462 HOH   A O   
6679 O  O   . HOH   E .   ? 0.2768 0.3984 0.6073 0.0328  -0.0651 -0.0566 463 HOH   A O   
6680 O  O   . HOH   E .   ? 0.2913 0.2792 0.3649 -0.0986 0.0623  -0.0506 464 HOH   A O   
6681 O  O   . HOH   E .   ? 0.2769 0.4245 0.5494 0.0407  0.0358  -0.1685 465 HOH   A O   
6682 O  O   . HOH   E .   ? 0.6062 0.3853 0.8493 0.0547  0.0256  0.2818  466 HOH   A O   
6683 O  O   . HOH   E .   ? 0.3604 0.4274 0.4035 -0.1048 -0.0052 0.0158  467 HOH   A O   
6684 O  O   . HOH   E .   ? 0.2745 0.1864 0.2671 0.0326  -0.0805 -0.0223 468 HOH   A O   
6685 O  O   . HOH   E .   ? 0.6215 0.4635 0.4859 0.0712  0.1104  0.0455  469 HOH   A O   
6686 O  O   . HOH   E .   ? 0.2848 0.2652 0.3888 0.0164  0.0685  -0.0119 470 HOH   A O   
6687 O  O   . HOH   E .   ? 0.3871 0.6459 0.4522 -0.0748 -0.1120 0.2540  471 HOH   A O   
6688 O  O   . HOH   E .   ? 0.4271 0.5668 0.3681 0.0552  -0.0691 -0.0540 472 HOH   A O   
6689 O  O   . HOH   E .   ? 0.4396 0.4730 0.4877 -0.2453 0.0054  0.0099  473 HOH   A O   
6690 O  O   . HOH   E .   ? 0.5106 0.2577 0.3714 -0.0322 -0.1201 0.0683  474 HOH   A O   
6691 O  O   . HOH   E .   ? 0.5590 0.6821 0.6430 -0.1696 -0.1423 0.0733  475 HOH   A O   
6692 O  O   . HOH   E .   ? 0.2494 0.2581 0.2747 0.0284  0.0065  0.0242  476 HOH   A O   
6693 O  O   . HOH   E .   ? 0.5748 0.5885 0.4815 0.1156  -0.0843 -0.1051 477 HOH   A O   
6694 O  O   . HOH   E .   ? 0.5718 0.5099 0.4540 0.0322  0.0014  -0.1382 478 HOH   A O   
6695 O  O   . HOH   E .   ? 0.7320 0.5539 0.6727 -0.0840 0.0689  -0.0894 479 HOH   A O   
6696 O  O   . HOH   E .   ? 0.8083 0.4468 0.3414 -0.0631 -0.1059 -0.0160 480 HOH   A O   
6697 O  O   . HOH   E .   ? 0.4316 0.4827 0.2983 0.0250  0.0051  0.0248  481 HOH   A O   
6698 O  O   B HOH   E .   ? 0.2946 0.1916 0.2794 0.1195  -0.0434 0.0422  482 HOH   A O   
6699 O  O   . HOH   E .   ? 0.2944 0.4334 0.5120 0.0214  0.1278  0.0990  483 HOH   A O   
6700 O  O   . HOH   E .   ? 0.4153 0.3874 0.2812 -0.0664 0.1163  -0.0467 484 HOH   A O   
6701 O  O   . HOH   E .   ? 0.2675 0.5334 0.3936 0.1072  0.1030  0.2529  485 HOH   A O   
6702 O  O   . HOH   E .   ? 0.6229 0.6934 0.6111 0.0959  -0.1344 0.0816  486 HOH   A O   
6703 O  O   . HOH   E .   ? 0.5026 0.4857 0.3777 -0.0678 -0.0775 0.0079  487 HOH   A O   
6704 O  O   . HOH   E .   ? 0.7915 0.7790 0.5624 -0.0908 0.2170  0.1364  488 HOH   A O   
6705 O  O   . HOH   E .   ? 0.2579 0.2641 0.7054 -0.0095 -0.1152 0.0514  489 HOH   A O   
6706 O  O   . HOH   E .   ? 0.6431 0.3710 0.4614 -0.0558 0.1095  -0.0106 490 HOH   A O   
6707 O  O   . HOH   E .   ? 0.3154 0.2328 0.6652 0.0203  0.0743  0.0994  491 HOH   A O   
6708 O  O   . HOH   E .   ? 0.6911 0.5014 0.5071 -0.0972 -0.0934 -0.0813 492 HOH   A O   
6709 O  O   B HOH   E .   ? 0.3461 0.2416 0.2970 0.0035  -0.0380 -0.0336 493 HOH   A O   
6710 O  O   . HOH   E .   ? 0.5053 0.5274 0.4380 -0.0115 -0.0225 -0.0364 494 HOH   A O   
6711 O  O   . HOH   E .   ? 0.4261 0.3824 0.5392 -0.1355 0.1113  0.0744  495 HOH   A O   
6712 O  O   . HOH   E .   ? 0.4558 0.3535 0.5118 -0.0189 0.2461  0.0371  496 HOH   A O   
6713 O  O   . HOH   E .   ? 0.5923 0.5579 0.6763 0.0961  0.2301  -0.1040 497 HOH   A O   
6714 O  O   . HOH   E .   ? 0.8493 0.7800 0.5459 0.1837  -0.1522 0.0926  498 HOH   A O   
6715 O  O   . HOH   E .   ? 0.3003 0.5176 0.3538 -0.0289 -0.0448 -0.0721 499 HOH   A O   
6716 O  O   . HOH   E .   ? 0.2740 0.3453 0.5573 -0.0119 0.1333  -0.0811 500 HOH   A O   
6717 O  O   . HOH   E .   ? 0.3864 0.9163 0.5900 -0.1093 -0.0404 0.2385  501 HOH   A O   
6718 O  O   . HOH   E .   ? 0.6335 0.2770 0.4794 -0.0731 0.1300  0.0532  502 HOH   A O   
6719 O  O   . HOH   E .   ? 0.4903 0.3235 0.4783 -0.1801 -0.0150 0.0633  503 HOH   A O   
6720 O  O   . HOH   E .   ? 0.2547 0.3420 0.3912 0.0481  -0.0397 0.0746  504 HOH   A O   
6721 O  O   . HOH   E .   ? 0.2689 0.4434 0.4466 0.0297  -0.0556 0.0357  505 HOH   A O   
6722 O  O   . HOH   E .   ? 0.6246 0.8289 0.5446 0.1551  0.0265  0.2075  506 HOH   A O   
6723 O  O   . HOH   E .   ? 0.8443 0.5341 0.6535 -0.0562 -0.0056 0.0687  507 HOH   A O   
6724 O  O   B HOH   E .   ? 0.2827 0.2457 0.2141 0.0272  0.0450  -0.0296 508 HOH   A O   
6725 O  O   . HOH   E .   ? 0.5439 0.7592 0.5481 0.3380  -0.0135 0.1498  509 HOH   A O   
6726 O  O   . HOH   E .   ? 0.3323 0.2517 0.4810 0.0122  -0.0066 0.0826  510 HOH   A O   
6727 O  O   . HOH   E .   ? 0.5414 0.6301 0.4375 -0.0007 -0.0501 -0.1076 511 HOH   A O   
6728 O  O   A HOH   E .   ? 0.4215 0.7151 0.2792 0.1307  0.0935  0.1683  512 HOH   A O   
6729 O  O   . HOH   E .   ? 0.2856 0.7318 0.3668 0.0631  0.0417  0.0510  513 HOH   A O   
6730 O  O   . HOH   E .   ? 0.5037 0.5762 0.4286 0.1762  -0.0727 0.1226  514 HOH   A O   
6731 O  O   . HOH   E .   ? 0.4782 0.7411 0.5814 -0.0837 -0.0498 0.1461  515 HOH   A O   
6732 O  O   . HOH   E .   ? 0.3031 0.4548 0.5684 0.0057  -0.0706 0.2516  516 HOH   A O   
6733 O  O   . HOH   F .   ? 0.2238 0.2182 0.3093 0.0077  0.0589  0.0310  201 HOH   B O   
6734 O  O   . HOH   F .   ? 0.3482 0.3530 0.7464 -0.0158 0.0723  -0.0566 202 HOH   B O   
6735 O  O   . HOH   F .   ? 0.4738 0.4048 0.4265 -0.0020 -0.0046 -0.1996 203 HOH   B O   
6736 O  O   . HOH   F .   ? 0.3345 0.5924 0.4925 -0.0249 0.1762  -0.1905 204 HOH   B O   
6737 O  O   . HOH   F .   ? 0.3189 0.1995 0.5208 0.0148  0.1792  0.0813  205 HOH   B O   
6738 O  O   . HOH   F .   ? 0.8154 0.3463 0.4679 0.0625  0.1241  -0.0308 206 HOH   B O   
6739 O  O   . HOH   F .   ? 0.5095 0.6453 0.3796 0.3063  -0.1121 -0.0247 207 HOH   B O   
6740 O  O   . HOH   F .   ? 0.3123 0.7526 0.3878 0.1260  0.0591  0.2602  208 HOH   B O   
6741 O  O   . HOH   F .   ? 0.3571 0.5392 0.2529 -0.0155 -0.0241 -0.1259 209 HOH   B O   
6742 O  O   . HOH   F .   ? 0.2030 0.2347 0.3129 -0.0047 0.0245  -0.0237 210 HOH   B O   
6743 O  O   . HOH   F .   ? 0.4292 0.3735 0.3860 -0.0056 -0.1187 0.0491  211 HOH   B O   
6744 O  O   . HOH   F .   ? 0.3456 0.4590 0.5146 -0.1031 0.0321  -0.1648 212 HOH   B O   
6745 O  O   . HOH   F .   ? 0.4116 0.5118 0.4063 0.2048  -0.0134 -0.0038 213 HOH   B O   
6746 O  O   . HOH   F .   ? 0.6660 0.6678 0.5482 0.2620  0.0729  0.0441  214 HOH   B O   
6747 O  O   . HOH   F .   ? 0.1557 0.2086 0.2987 -0.0206 -0.0118 0.0168  215 HOH   B O   
6748 O  O   . HOH   F .   ? 0.3425 0.5207 0.5806 0.1827  0.0455  -0.0783 216 HOH   B O   
6749 O  O   . HOH   F .   ? 0.6566 0.3072 0.3577 -0.2011 0.0132  0.0033  217 HOH   B O   
6750 O  O   . HOH   F .   ? 0.5202 0.2199 0.3085 -0.0001 -0.0824 0.0123  218 HOH   B O   
6751 O  O   . HOH   F .   ? 0.3858 0.2626 0.4543 0.0278  -0.1252 -0.0468 219 HOH   B O   
6752 O  O   . HOH   F .   ? 0.2576 0.2710 0.6181 0.0473  -0.0644 0.0555  220 HOH   B O   
6753 O  O   . HOH   F .   ? 0.8077 0.4807 0.4845 0.2365  -0.0094 -0.1240 221 HOH   B O   
6754 O  O   . HOH   F .   ? 0.2258 0.2306 0.4071 -0.0351 0.0135  -0.0538 222 HOH   B O   
6755 O  O   . HOH   F .   ? 0.3161 0.2311 0.5713 0.0052  0.1916  0.0411  223 HOH   B O   
6756 O  O   . HOH   F .   ? 0.4195 0.2647 0.4111 0.0778  -0.0458 -0.0617 224 HOH   B O   
6757 O  O   . HOH   F .   ? 0.1788 0.2185 0.3341 -0.0141 0.0240  -0.0200 225 HOH   B O   
6758 O  O   . HOH   F .   ? 0.4524 0.4771 0.4415 0.0259  0.0768  -0.2156 226 HOH   B O   
6759 O  O   . HOH   F .   ? 0.4262 0.4044 0.6878 -0.0299 -0.1721 -0.1136 227 HOH   B O   
6760 O  O   . HOH   F .   ? 0.5202 0.4483 0.6190 0.0781  -0.0553 0.2840  228 HOH   B O   
6761 O  O   . HOH   F .   ? 0.4005 0.3275 0.2171 0.0320  0.0744  0.0472  229 HOH   B O   
6762 O  O   . HOH   F .   ? 0.2538 0.1723 0.2939 -0.0271 0.1002  -0.0078 230 HOH   B O   
6763 O  O   . HOH   F .   ? 0.2491 0.2889 0.3287 -0.0759 0.0219  -0.0185 231 HOH   B O   
6764 O  O   . HOH   F .   ? 0.6057 0.3107 0.4096 -0.2316 -0.0104 0.0099  232 HOH   B O   
6765 O  O   . HOH   F .   ? 0.2611 0.2720 0.3247 0.0344  0.0035  -0.0917 233 HOH   B O   
6766 O  O   . HOH   F .   ? 0.5213 0.7706 0.3852 0.2893  0.0789  0.0575  234 HOH   B O   
6767 O  O   . HOH   F .   ? 0.5104 0.6577 0.3347 -0.0272 -0.0418 0.0566  235 HOH   B O   
6768 O  O   . HOH   F .   ? 0.2952 0.3913 0.3162 -0.0909 0.0749  -0.0455 236 HOH   B O   
6769 O  O   . HOH   F .   ? 0.3700 0.1982 0.2057 0.0278  -0.0710 -0.0192 237 HOH   B O   
6770 O  O   . HOH   F .   ? 0.1593 0.1536 0.1664 -0.0101 -0.0010 -0.0051 238 HOH   B O   
6771 O  O   . HOH   F .   ? 0.3380 0.1842 0.6378 -0.0266 -0.1515 -0.0126 239 HOH   B O   
6772 O  O   . HOH   F .   ? 0.2083 0.1450 0.3654 0.0164  -0.0632 -0.0176 240 HOH   B O   
6773 O  O   . HOH   F .   ? 0.1521 0.1340 0.1712 -0.0047 -0.0047 0.0094  241 HOH   B O   
6774 O  O   . HOH   F .   ? 0.3767 0.2886 0.4782 0.0547  -0.0891 -0.1676 242 HOH   B O   
6775 O  O   . HOH   F .   ? 0.6676 0.3776 0.2980 -0.0076 0.0470  -0.0398 243 HOH   B O   
6776 O  O   . HOH   F .   ? 0.3343 0.2637 0.3512 -0.0267 0.0255  -0.0595 244 HOH   B O   
6777 O  O   . HOH   F .   ? 0.4089 0.3876 0.5468 -0.1603 0.0037  0.0892  245 HOH   B O   
6778 O  O   . HOH   F .   ? 0.2661 0.2330 0.2746 0.0691  0.0502  -0.0051 246 HOH   B O   
6779 O  O   . HOH   F .   ? 0.2428 0.3873 0.3285 -0.0546 -0.0578 -0.0568 247 HOH   B O   
6780 O  O   . HOH   F .   ? 0.2878 0.4136 0.3540 -0.0906 -0.0641 -0.0366 248 HOH   B O   
6781 O  O   . HOH   F .   ? 0.2290 0.2012 0.2214 -0.0267 -0.0461 0.0100  249 HOH   B O   
6782 O  O   . HOH   F .   ? 0.2470 0.3004 0.2159 -0.0562 0.0081  0.0383  250 HOH   B O   
6783 O  O   . HOH   F .   ? 0.1644 0.1491 0.2773 -0.0079 -0.0005 -0.0086 251 HOH   B O   
6784 O  O   . HOH   F .   ? 0.2212 0.3653 0.2579 -0.0367 -0.0161 0.0440  252 HOH   B O   
6785 O  O   . HOH   F .   ? 0.3260 0.4766 0.3557 -0.0448 -0.1159 0.1001  253 HOH   B O   
6786 O  O   . HOH   F .   ? 0.5361 0.6592 0.2813 -0.0315 -0.0886 0.0404  254 HOH   B O   
6787 O  O   . HOH   F .   ? 0.2460 0.2158 0.2743 0.0744  -0.0779 -0.0569 255 HOH   B O   
6788 O  O   . HOH   F .   ? 0.2176 0.1592 0.2161 -0.0301 -0.0358 0.0189  256 HOH   B O   
6789 O  O   . HOH   F .   ? 0.2213 0.4141 0.5005 -0.0354 -0.0061 -0.1537 257 HOH   B O   
6790 O  O   . HOH   F .   ? 0.3320 0.3749 0.2595 0.0372  0.0912  0.0157  258 HOH   B O   
6791 O  O   . HOH   F .   ? 0.2777 0.2331 0.2023 0.0122  -0.0200 0.0013  259 HOH   B O   
6792 O  O   . HOH   F .   ? 0.2550 0.4611 0.6099 0.0193  0.0003  -0.1368 260 HOH   B O   
6793 O  O   . HOH   F .   ? 0.3346 0.4321 0.4966 -0.0760 0.0626  -0.0322 261 HOH   B O   
6794 O  O   . HOH   F .   ? 0.3491 0.3742 0.4586 0.1309  -0.0674 -0.1003 262 HOH   B O   
6795 O  O   . HOH   F .   ? 0.1829 0.2783 0.2763 0.0401  0.0361  0.0930  263 HOH   B O   
6796 O  O   . HOH   F .   ? 0.1476 0.1793 0.2128 -0.0057 0.0085  0.0210  264 HOH   B O   
6797 O  O   . HOH   F .   ? 0.4795 0.4326 0.6823 0.0743  0.0652  -0.0235 265 HOH   B O   
6798 O  O   . HOH   F .   ? 0.1701 0.1687 0.3237 -0.0194 -0.0144 0.0033  266 HOH   B O   
6799 O  O   . HOH   F .   ? 0.2373 0.2310 0.2060 0.0068  -0.0053 -0.0108 267 HOH   B O   
6800 O  O   . HOH   F .   ? 0.2518 0.2598 0.2479 -0.0471 -0.0621 -0.0372 268 HOH   B O   
6801 O  O   . HOH   F .   ? 0.2553 0.2977 0.2489 -0.0465 -0.0779 0.0255  269 HOH   B O   
6802 O  O   . HOH   F .   ? 0.2132 0.2032 0.4021 0.0012  -0.0394 -0.0333 270 HOH   B O   
6803 O  O   . HOH   F .   ? 0.2622 0.1997 0.3065 -0.0531 0.0287  -0.0094 271 HOH   B O   
6804 O  O   . HOH   F .   ? 0.4389 0.4974 0.4815 -0.0264 -0.1560 0.0359  272 HOH   B O   
6805 O  O   . HOH   F .   ? 0.2586 0.5082 0.5980 0.1471  -0.0687 -0.0676 273 HOH   B O   
6806 O  O   . HOH   F .   ? 0.2140 0.1586 0.2424 -0.0235 -0.0144 0.0145  274 HOH   B O   
6807 O  O   . HOH   F .   ? 0.2001 0.1825 0.1770 -0.0500 -0.0482 0.0163  275 HOH   B O   
6808 O  O   . HOH   F .   ? 0.2572 0.3640 0.3109 -0.0558 0.0489  -0.1125 276 HOH   B O   
6809 O  O   . HOH   F .   ? 0.1803 0.1431 0.4238 -0.0074 -0.0201 -0.0187 277 HOH   B O   
6810 O  O   . HOH   F .   ? 0.2668 0.3755 0.3812 0.0270  0.1099  0.0095  278 HOH   B O   
6811 O  O   . HOH   F .   ? 0.4138 0.3802 0.4914 -0.0285 -0.1069 -0.0456 279 HOH   B O   
6812 O  O   . HOH   F .   ? 0.2825 0.6926 0.7899 0.1696  -0.0500 -0.0835 280 HOH   B O   
6813 O  O   . HOH   F .   ? 0.2979 0.2094 0.4597 0.0121  0.0391  0.0424  281 HOH   B O   
6814 O  O   . HOH   F .   ? 0.1682 0.1625 0.3503 -0.0114 0.0046  -0.0113 282 HOH   B O   
6815 O  O   . HOH   F .   ? 0.1716 0.1629 0.2005 0.0023  0.0086  0.0051  283 HOH   B O   
6816 O  O   . HOH   F .   ? 0.4414 0.4053 0.3019 0.0410  -0.0181 -0.0788 284 HOH   B O   
6817 O  O   . HOH   F .   ? 0.2867 0.4933 0.5886 -0.1094 -0.1171 0.1030  285 HOH   B O   
6818 O  O   . HOH   F .   ? 0.1620 0.2183 0.1638 -0.0154 -0.0189 0.0106  286 HOH   B O   
6819 O  O   . HOH   F .   ? 0.2742 0.4520 0.2607 0.1602  -0.0429 -0.0495 287 HOH   B O   
6820 O  O   . HOH   F .   ? 0.3844 0.2840 0.2266 0.0414  -0.0964 -0.0152 288 HOH   B O   
6821 O  O   . HOH   F .   ? 0.2538 0.6941 0.2660 0.0825  -0.0501 -0.0865 289 HOH   B O   
6822 O  O   . HOH   F .   ? 0.5148 0.4324 0.2500 0.1384  -0.0883 -0.0068 290 HOH   B O   
6823 O  O   . HOH   F .   ? 0.2536 0.2686 0.2932 0.0074  -0.0804 0.0258  291 HOH   B O   
6824 O  O   . HOH   F .   ? 0.3286 0.4547 0.4022 -0.1587 0.1211  -0.0649 292 HOH   B O   
6825 O  O   . HOH   F .   ? 0.3768 0.2385 0.4321 -0.1054 -0.2031 0.1025  293 HOH   B O   
6826 O  O   . HOH   F .   ? 0.3940 0.7523 0.3820 0.1539  -0.0460 0.1124  294 HOH   B O   
6827 O  O   . HOH   F .   ? 0.4322 0.4369 0.4273 -0.1102 0.1472  -0.1512 295 HOH   B O   
6828 O  O   . HOH   F .   ? 0.1795 0.2165 0.3211 0.0162  -0.0090 0.0134  296 HOH   B O   
6829 O  O   . HOH   F .   ? 0.2929 0.3104 0.3042 -0.0170 0.0053  -0.1361 297 HOH   B O   
6830 O  O   . HOH   F .   ? 0.1852 0.3580 0.4612 0.0356  -0.0262 -0.1343 298 HOH   B O   
6831 O  O   . HOH   F .   ? 0.4382 0.5114 0.2304 0.0153  0.0704  0.0731  299 HOH   B O   
6832 O  O   . HOH   F .   ? 0.2765 0.3094 0.3416 -0.0423 0.0858  -0.0917 300 HOH   B O   
6833 O  O   . HOH   F .   ? 0.1946 0.1692 0.2526 0.0141  0.0104  0.0214  301 HOH   B O   
6834 O  O   . HOH   F .   ? 0.2214 0.1706 0.2728 -0.0249 -0.0310 -0.0026 302 HOH   B O   
6835 O  O   . HOH   F .   ? 0.4403 0.4046 0.2456 0.1202  -0.0563 0.0645  303 HOH   B O   
6836 O  O   . HOH   F .   ? 0.2131 0.3275 0.6740 0.0514  -0.0592 -0.1918 304 HOH   B O   
6837 O  O   . HOH   F .   ? 0.6158 0.5321 0.4916 0.2410  0.0514  0.1237  305 HOH   B O   
6838 O  O   . HOH   F .   ? 0.3395 0.3058 0.5432 -0.0660 -0.0920 0.1164  306 HOH   B O   
6839 O  O   . HOH   F .   ? 0.6080 0.4370 0.3486 0.2883  0.1473  0.1103  307 HOH   B O   
6840 O  O   . HOH   F .   ? 0.2095 0.1629 0.3385 0.0292  -0.0856 0.0128  308 HOH   B O   
6841 O  O   . HOH   F .   ? 0.1685 0.1582 0.3175 0.0060  0.0025  -0.0063 309 HOH   B O   
6842 O  O   . HOH   F .   ? 0.3404 0.2003 0.3524 0.0796  0.0999  0.0493  310 HOH   B O   
6843 O  O   . HOH   F .   ? 0.2514 0.1600 0.2572 -0.0169 -0.0334 0.0320  311 HOH   B O   
6844 O  O   . HOH   F .   ? 0.1720 0.1948 0.3001 -0.0294 -0.0127 0.0093  312 HOH   B O   
6845 O  O   . HOH   F .   ? 0.7131 0.4928 0.4637 0.1465  0.1358  0.0485  313 HOH   B O   
6846 O  O   . HOH   F .   ? 0.5590 0.2961 0.2687 -0.2028 0.0782  -0.0174 314 HOH   B O   
6847 O  O   . HOH   F .   ? 0.2254 0.2932 0.4635 -0.0173 -0.0260 0.0036  315 HOH   B O   
6848 O  O   . HOH   F .   ? 0.5631 0.3819 0.4412 0.0114  0.0927  -0.1466 316 HOH   B O   
6849 O  O   . HOH   F .   ? 0.4204 0.2272 0.3033 0.1412  0.1062  0.0287  317 HOH   B O   
6850 O  O   . HOH   F .   ? 0.5051 0.3852 0.2960 0.0131  -0.0494 -0.0491 318 HOH   B O   
6851 O  O   . HOH   F .   ? 0.2230 0.2109 0.1859 -0.0050 0.0147  0.0249  319 HOH   B O   
6852 O  O   . HOH   F .   ? 0.4748 0.3282 0.4360 -0.0412 0.0563  0.0467  320 HOH   B O   
6853 O  O   . HOH   F .   ? 0.1672 0.1714 0.2967 -0.0086 -0.0130 -0.0143 321 HOH   B O   
6854 O  O   . HOH   F .   ? 0.1729 0.2713 0.2418 -0.0042 -0.0234 0.0567  322 HOH   B O   
6855 O  O   . HOH   F .   ? 0.4578 0.3517 0.5214 0.1351  0.2368  0.2024  323 HOH   B O   
6856 O  O   . HOH   F .   ? 0.2226 0.6921 0.5400 -0.1088 -0.0168 0.0107  324 HOH   B O   
6857 O  O   . HOH   F .   ? 0.2888 0.2341 0.2528 0.0272  -0.0312 0.0329  325 HOH   B O   
6858 O  O   . HOH   F .   ? 0.4772 0.4121 0.6634 0.0526  -0.0161 0.0424  326 HOH   B O   
6859 O  O   . HOH   F .   ? 0.2269 0.3080 0.3343 0.0730  -0.0278 -0.0762 327 HOH   B O   
6860 O  O   . HOH   F .   ? 0.6297 0.3805 0.4038 0.0499  0.1588  0.1479  328 HOH   B O   
6861 O  O   . HOH   F .   ? 0.5789 0.5119 0.6913 0.0853  -0.0582 0.2326  329 HOH   B O   
6862 O  O   . HOH   F .   ? 0.1961 0.2059 0.2978 0.0326  0.0358  0.0205  330 HOH   B O   
6863 O  O   . HOH   F .   ? 0.3651 0.4568 0.8287 -0.0328 -0.1014 0.2307  331 HOH   B O   
6864 O  O   . HOH   F .   ? 0.2698 0.2196 0.4309 0.0106  0.0036  0.0254  332 HOH   B O   
6865 O  O   . HOH   F .   ? 0.2793 0.3453 0.5533 -0.0866 -0.1693 0.1575  333 HOH   B O   
6866 O  O   . HOH   F .   ? 0.6064 0.5485 0.5958 -0.1050 -0.0787 0.1542  334 HOH   B O   
6867 O  O   . HOH   F .   ? 0.6124 0.4664 0.6069 -0.0758 -0.0962 -0.1196 335 HOH   B O   
6868 O  O   . HOH   F .   ? 0.1825 0.1538 0.2459 0.0083  -0.0171 0.0145  336 HOH   B O   
6869 O  O   . HOH   F .   ? 0.2343 0.2474 0.5656 -0.0613 -0.0089 0.1412  337 HOH   B O   
6870 O  O   . HOH   F .   ? 0.6104 0.3431 0.3324 0.1372  -0.0093 0.0607  338 HOH   B O   
6871 O  O   . HOH   F .   ? 0.4499 0.7739 0.3737 -0.0645 -0.0837 0.1972  339 HOH   B O   
6872 O  O   . HOH   F .   ? 0.7272 0.7083 0.3327 0.0093  -0.0477 0.1285  340 HOH   B O   
6873 O  O   . HOH   F .   ? 0.8778 0.2925 0.3913 0.0937  -0.1274 -0.0313 341 HOH   B O   
6874 O  O   . HOH   F .   ? 0.4117 0.5840 0.3921 -0.0720 -0.0941 -0.0344 342 HOH   B O   
6875 O  O   . HOH   F .   ? 0.5458 0.3449 0.3390 0.0566  -0.1436 -0.1083 343 HOH   B O   
6876 O  O   . HOH   F .   ? 0.2880 0.6351 0.7750 0.0038  -0.0596 -0.0122 344 HOH   B O   
6877 O  O   . HOH   F .   ? 0.5114 0.6034 0.3806 0.0198  -0.1133 0.0387  345 HOH   B O   
6878 O  O   . HOH   F .   ? 0.2906 0.1969 0.3958 0.0418  -0.1013 -0.0312 346 HOH   B O   
6879 O  O   . HOH   F .   ? 0.2205 0.2078 0.3436 -0.0052 0.0728  0.0013  347 HOH   B O   
6880 O  O   . HOH   F .   ? 0.4579 0.5666 0.5965 0.0365  -0.1163 0.0541  348 HOH   B O   
6881 O  O   . HOH   F .   ? 0.2495 0.6630 0.3008 0.1586  -0.0616 -0.1592 349 HOH   B O   
6882 O  O   . HOH   F .   ? 0.4830 0.6070 0.5381 -0.1074 0.0171  0.1695  350 HOH   B O   
6883 O  O   . HOH   F .   ? 0.4507 0.7280 0.6392 0.1176  0.0505  0.0011  351 HOH   B O   
6884 O  O   . HOH   F .   ? 0.2423 0.4511 0.5109 -0.0100 0.0519  0.0474  352 HOH   B O   
6885 O  O   . HOH   F .   ? 0.3222 0.2437 0.4959 -0.0402 -0.1056 -0.0477 353 HOH   B O   
6886 O  O   . HOH   F .   ? 0.3648 0.4519 0.5366 -0.1587 0.0375  -0.0480 354 HOH   B O   
6887 O  O   . HOH   F .   ? 0.3589 0.2273 0.3455 -0.0573 0.0073  -0.0703 355 HOH   B O   
6888 O  O   . HOH   F .   ? 0.5059 0.3034 0.5807 -0.1067 0.1628  0.0524  356 HOH   B O   
6889 O  O   . HOH   F .   ? 0.5130 0.5999 0.5123 0.2078  -0.1144 0.1575  357 HOH   B O   
6890 O  O   . HOH   F .   ? 0.5636 0.4832 0.5440 0.0076  -0.0346 -0.0390 358 HOH   B O   
6891 O  O   . HOH   F .   ? 0.3811 0.3073 0.4288 -0.1087 0.0072  -0.0755 359 HOH   B O   
6892 O  O   . HOH   F .   ? 0.5556 0.3480 0.5128 0.0227  0.1982  -0.0501 360 HOH   B O   
6893 O  O   . HOH   F .   ? 0.4753 0.3546 0.5361 0.0326  -0.1698 -0.0419 361 HOH   B O   
6894 O  O   . HOH   F .   ? 0.5468 0.4158 0.6318 0.0282  0.1071  0.1080  362 HOH   B O   
6895 O  O   . HOH   F .   ? 0.4126 0.7281 0.2876 0.2075  0.0109  0.0284  363 HOH   B O   
6896 O  O   . HOH   F .   ? 0.2235 0.3556 0.7349 -0.0474 -0.0662 -0.0985 364 HOH   B O   
6897 O  O   . HOH   F .   ? 0.6916 0.2562 0.3219 -0.0169 0.0423  0.0762  365 HOH   B O   
6898 O  O   . HOH   F .   ? 0.6198 0.5916 0.3475 0.2025  -0.1621 0.0477  366 HOH   B O   
6899 O  O   . HOH   F .   ? 0.5044 0.3200 0.6858 -0.1323 -0.0667 0.0448  367 HOH   B O   
6900 O  O   . HOH   F .   ? 0.5282 0.6418 0.4752 -0.0787 -0.0356 -0.1209 368 HOH   B O   
6901 O  O   . HOH   F .   ? 0.4312 0.3409 0.5255 0.0339  -0.1722 0.0081  369 HOH   B O   
6902 O  O   . HOH   F .   ? 0.6849 0.5158 0.4763 0.1669  0.1332  0.0987  370 HOH   B O   
6903 O  O   . HOH   F .   ? 0.4543 0.6475 0.6076 0.2854  0.1157  0.1545  371 HOH   B O   
6904 O  O   . HOH   F .   ? 0.8408 0.8664 0.5755 0.3425  -0.1437 0.1045  372 HOH   B O   
6905 O  O   . HOH   F .   ? 0.4857 0.3598 0.3887 0.0799  -0.1678 -0.0494 373 HOH   B O   
6906 O  O   . HOH   F .   ? 0.6933 0.4736 0.3252 -0.1078 -0.1080 -0.0925 374 HOH   B O   
6907 O  O   . HOH   F .   ? 0.4770 0.4775 0.4996 -0.0353 -0.0839 -0.0013 375 HOH   B O   
6908 O  O   . HOH   F .   ? 0.2495 0.4042 0.4863 0.0288  -0.0497 -0.1056 376 HOH   B O   
6909 O  O   . HOH   F .   ? 0.8315 0.3853 0.4842 -0.0652 -0.0134 -0.0131 377 HOH   B O   
6910 O  O   . HOH   F .   ? 0.5130 0.8067 0.4286 -0.1478 0.0901  -0.1531 378 HOH   B O   
6911 O  O   . HOH   F .   ? 0.3220 0.4581 0.2693 0.0955  0.0260  0.0431  379 HOH   B O   
6912 O  O   . HOH   F .   ? 0.3719 0.6819 0.5644 0.0469  -0.0395 0.0073  380 HOH   B O   
6913 O  O   . HOH   F .   ? 0.5160 0.7699 0.5761 0.1931  0.0639  0.2871  381 HOH   B O   
6914 O  O   . HOH   F .   ? 0.5799 0.7266 0.6746 -0.0384 0.2623  0.1315  382 HOH   B O   
6915 O  O   . HOH   F .   ? 0.2905 0.2495 0.3371 0.0196  0.0226  0.0256  383 HOH   B O   
6916 O  O   . HOH   F .   ? 0.5124 0.8730 0.5767 0.1184  0.2304  0.0708  384 HOH   B O   
6917 O  O   . HOH   F .   ? 0.7174 0.3744 0.4776 0.0724  0.1280  -0.0809 385 HOH   B O   
6918 O  O   . HOH   F .   ? 0.7847 0.6830 0.4293 0.3269  0.0148  -0.0050 386 HOH   B O   
6919 O  O   . HOH   F .   ? 0.2496 0.4117 0.3957 -0.0448 -0.0881 -0.0411 387 HOH   B O   
6920 O  O   . HOH   F .   ? 0.6290 0.4394 0.5550 -0.0703 0.1132  -0.0507 388 HOH   B O   
6921 O  O   . HOH   F .   ? 0.5080 0.4124 0.3277 0.0059  0.0467  -0.0134 389 HOH   B O   
6922 O  O   . HOH   F .   ? 0.4706 0.2604 0.3424 0.1075  -0.0347 0.0349  390 HOH   B O   
6923 O  O   . HOH   F .   ? 0.5978 0.4431 0.3960 0.0742  0.0566  0.0748  391 HOH   B O   
6924 O  O   . HOH   F .   ? 0.4322 0.2230 0.4932 -0.0545 0.0382  0.0555  392 HOH   B O   
6925 O  O   . HOH   F .   ? 0.2579 0.5313 0.7025 -0.1520 -0.0564 -0.0537 393 HOH   B O   
6926 O  O   . HOH   F .   ? 0.4996 0.5993 0.4273 0.1463  -0.0051 -0.0951 394 HOH   B O   
6927 O  O   . HOH   F .   ? 0.3332 0.3867 0.4079 0.0124  0.0249  -0.0845 395 HOH   B O   
6928 O  O   . HOH   F .   ? 0.2222 0.2981 0.5310 -0.0565 -0.0504 -0.0212 396 HOH   B O   
6929 O  O   . HOH   F .   ? 0.4449 0.4167 0.4654 0.0265  0.1106  0.0953  397 HOH   B O   
6930 O  O   . HOH   F .   ? 0.5891 0.6447 0.6608 0.1389  -0.1253 0.2250  398 HOH   B O   
6931 O  O   . HOH   F .   ? 0.5483 0.4448 0.3457 -0.2445 -0.0647 0.1262  399 HOH   B O   
6932 O  O   . HOH   F .   ? 0.6400 0.6026 0.3726 0.1396  -0.0435 -0.0226 400 HOH   B O   
# 
