data_7HCG
# 
_entry.id   7HCG 
# 
_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   7HCG         pdb_00007hcg 10.2210/pdb7hcg/pdb 
WWPDB D_1001407298 ?            ?                   
# 
_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                        7HCG 
_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 '3-[(2H-1,3-benzodioxole-5-carbonyl)amino]thiophene-2-carboxylic acid' 291.279   1   ?                      ? ? 
?                                                                                    
3 water       nat water                                                                  18.015    413 ?                      ? ? 
?                                                                                    
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '3-[(2H-1,3-benzodioxole-5-carbonyl)amino]thiophene-2-carboxylic acid' A1A5B 
3 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 
A1A5B non-polymer         . '3-[(2H-1,3-benzodioxole-5-carbonyl)amino]thiophene-2-carboxylic acid' ? 'C13 H9 N O5 S'  291.279 
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A5B 1   201 201  A1A5B LA1 A . 
D 3 HOH   1   301 93   HOH   HOH A . 
D 3 HOH   2   302 86   HOH   HOH A . 
D 3 HOH   3   303 493  HOH   HOH A . 
D 3 HOH   4   304 196  HOH   HOH A . 
D 3 HOH   5   305 625  HOH   HOH A . 
D 3 HOH   6   306 1309 HOH   HOH A . 
D 3 HOH   7   307 132  HOH   HOH A . 
D 3 HOH   8   308 292  HOH   HOH A . 
D 3 HOH   9   309 1295 HOH   HOH A . 
D 3 HOH   10  310 109  HOH   HOH A . 
D 3 HOH   11  311 3    HOH   HOH A . 
D 3 HOH   12  312 76   HOH   HOH A . 
D 3 HOH   13  313 225  HOH   HOH A . 
D 3 HOH   14  314 153  HOH   HOH A . 
D 3 HOH   15  315 964  HOH   HOH A . 
D 3 HOH   16  316 662  HOH   HOH A . 
D 3 HOH   17  317 209  HOH   HOH A . 
D 3 HOH   18  318 236  HOH   HOH A . 
D 3 HOH   19  319 151  HOH   HOH A . 
D 3 HOH   20  320 17   HOH   HOH A . 
D 3 HOH   21  321 124  HOH   HOH A . 
D 3 HOH   22  322 661  HOH   HOH A . 
D 3 HOH   23  323 136  HOH   HOH A . 
D 3 HOH   24  324 105  HOH   HOH A . 
D 3 HOH   25  325 15   HOH   HOH A . 
D 3 HOH   26  326 192  HOH   HOH A . 
D 3 HOH   27  327 140  HOH   HOH A . 
D 3 HOH   28  328 229  HOH   HOH A . 
D 3 HOH   29  329 1    HOH   HOH A . 
D 3 HOH   30  330 241  HOH   HOH A . 
D 3 HOH   31  331 164  HOH   HOH A . 
D 3 HOH   32  332 139  HOH   HOH A . 
D 3 HOH   33  333 36   HOH   HOH A . 
D 3 HOH   34  334 337  HOH   HOH A . 
D 3 HOH   35  335 393  HOH   HOH A . 
D 3 HOH   36  336 1300 HOH   HOH A . 
D 3 HOH   37  337 469  HOH   HOH A . 
D 3 HOH   38  338 320  HOH   HOH A . 
D 3 HOH   39  339 247  HOH   HOH A . 
D 3 HOH   40  340 2    HOH   HOH A . 
D 3 HOH   41  341 42   HOH   HOH A . 
D 3 HOH   42  342 162  HOH   HOH A . 
D 3 HOH   43  343 102  HOH   HOH A . 
D 3 HOH   44  344 66   HOH   HOH A . 
D 3 HOH   45  345 8    HOH   HOH A . 
D 3 HOH   46  346 6    HOH   HOH A . 
D 3 HOH   47  347 630  HOH   HOH A . 
D 3 HOH   48  348 396  HOH   HOH A . 
D 3 HOH   49  349 354  HOH   HOH A . 
D 3 HOH   50  350 45   HOH   HOH A . 
D 3 HOH   51  351 165  HOH   HOH A . 
D 3 HOH   52  352 1290 HOH   HOH A . 
D 3 HOH   53  353 1301 HOH   HOH A . 
D 3 HOH   54  354 939  HOH   HOH A . 
D 3 HOH   55  355 2    HOH   HOH A . 
D 3 HOH   56  356 92   HOH   HOH A . 
D 3 HOH   57  357 19   HOH   HOH A . 
D 3 HOH   58  358 3    HOH   HOH A . 
D 3 HOH   59  359 39   HOH   HOH A . 
D 3 HOH   60  360 138  HOH   HOH A . 
D 3 HOH   61  361 381  HOH   HOH A . 
D 3 HOH   62  362 122  HOH   HOH A . 
D 3 HOH   63  363 18   HOH   HOH A . 
D 3 HOH   64  364 1283 HOH   HOH A . 
D 3 HOH   65  365 296  HOH   HOH A . 
D 3 HOH   66  366 186  HOH   HOH A . 
D 3 HOH   67  367 81   HOH   HOH A . 
D 3 HOH   68  368 5    HOH   HOH A . 
D 3 HOH   69  369 159  HOH   HOH A . 
D 3 HOH   70  370 169  HOH   HOH A . 
D 3 HOH   71  371 57   HOH   HOH A . 
D 3 HOH   72  372 46   HOH   HOH A . 
D 3 HOH   73  373 56   HOH   HOH A . 
D 3 HOH   74  374 134  HOH   HOH A . 
D 3 HOH   75  375 49   HOH   HOH A . 
D 3 HOH   76  376 33   HOH   HOH A . 
D 3 HOH   77  377 1289 HOH   HOH A . 
D 3 HOH   78  378 35   HOH   HOH A . 
D 3 HOH   79  379 155  HOH   HOH A . 
D 3 HOH   80  380 27   HOH   HOH A . 
D 3 HOH   81  381 405  HOH   HOH A . 
D 3 HOH   82  382 148  HOH   HOH A . 
D 3 HOH   83  383 26   HOH   HOH A . 
D 3 HOH   84  384 78   HOH   HOH A . 
D 3 HOH   85  385 85   HOH   HOH A . 
D 3 HOH   86  386 154  HOH   HOH A . 
D 3 HOH   87  387 21   HOH   HOH A . 
D 3 HOH   88  388 409  HOH   HOH A . 
D 3 HOH   89  389 218  HOH   HOH A . 
D 3 HOH   90  390 366  HOH   HOH A . 
D 3 HOH   91  391 116  HOH   HOH A . 
D 3 HOH   92  392 12   HOH   HOH A . 
D 3 HOH   93  393 24   HOH   HOH A . 
D 3 HOH   94  394 1310 HOH   HOH A . 
D 3 HOH   95  395 351  HOH   HOH A . 
D 3 HOH   96  396 67   HOH   HOH A . 
D 3 HOH   97  397 461  HOH   HOH A . 
D 3 HOH   98  398 1315 HOH   HOH A . 
D 3 HOH   99  399 1308 HOH   HOH A . 
D 3 HOH   100 400 58   HOH   HOH A . 
D 3 HOH   101 401 333  HOH   HOH A . 
D 3 HOH   102 402 303  HOH   HOH A . 
D 3 HOH   103 403 1275 HOH   HOH A . 
D 3 HOH   104 404 83   HOH   HOH A . 
D 3 HOH   105 405 6    HOH   HOH A . 
D 3 HOH   106 406 96   HOH   HOH A . 
D 3 HOH   107 407 4    HOH   HOH A . 
D 3 HOH   108 408 74   HOH   HOH A . 
D 3 HOH   109 409 199  HOH   HOH A . 
D 3 HOH   110 410 397  HOH   HOH A . 
D 3 HOH   111 411 34   HOH   HOH A . 
D 3 HOH   112 412 278  HOH   HOH A . 
D 3 HOH   113 413 212  HOH   HOH A . 
D 3 HOH   114 414 68   HOH   HOH A . 
D 3 HOH   115 415 125  HOH   HOH A . 
D 3 HOH   116 416 25   HOH   HOH A . 
D 3 HOH   117 417 121  HOH   HOH A . 
D 3 HOH   118 418 51   HOH   HOH A . 
D 3 HOH   119 419 53   HOH   HOH A . 
D 3 HOH   120 420 1238 HOH   HOH A . 
D 3 HOH   121 421 4    HOH   HOH A . 
D 3 HOH   122 422 123  HOH   HOH A . 
D 3 HOH   123 423 281  HOH   HOH A . 
D 3 HOH   124 424 1222 HOH   HOH A . 
D 3 HOH   125 425 95   HOH   HOH A . 
D 3 HOH   126 426 7    HOH   HOH A . 
D 3 HOH   127 427 1068 HOH   HOH A . 
D 3 HOH   128 428 1279 HOH   HOH A . 
D 3 HOH   129 429 156  HOH   HOH A . 
D 3 HOH   130 430 582  HOH   HOH A . 
D 3 HOH   131 431 195  HOH   HOH A . 
D 3 HOH   132 432 1189 HOH   HOH A . 
D 3 HOH   133 433 1313 HOH   HOH A . 
D 3 HOH   134 434 70   HOH   HOH A . 
D 3 HOH   135 435 40   HOH   HOH A . 
D 3 HOH   136 436 1286 HOH   HOH A . 
D 3 HOH   137 437 115  HOH   HOH A . 
D 3 HOH   138 438 1094 HOH   HOH A . 
D 3 HOH   139 439 71   HOH   HOH A . 
D 3 HOH   140 440 80   HOH   HOH A . 
D 3 HOH   141 441 16   HOH   HOH A . 
D 3 HOH   142 442 188  HOH   HOH A . 
D 3 HOH   143 443 94   HOH   HOH A . 
D 3 HOH   144 444 97   HOH   HOH A . 
D 3 HOH   145 445 952  HOH   HOH A . 
D 3 HOH   146 446 576  HOH   HOH A . 
D 3 HOH   147 447 104  HOH   HOH A . 
D 3 HOH   148 448 1296 HOH   HOH A . 
D 3 HOH   149 449 73   HOH   HOH A . 
D 3 HOH   150 450 330  HOH   HOH A . 
D 3 HOH   151 451 944  HOH   HOH A . 
D 3 HOH   152 452 5    HOH   HOH A . 
D 3 HOH   153 453 107  HOH   HOH A . 
D 3 HOH   154 454 1119 HOH   HOH A . 
D 3 HOH   155 455 79   HOH   HOH A . 
D 3 HOH   156 456 1134 HOH   HOH A . 
D 3 HOH   157 457 509  HOH   HOH A . 
D 3 HOH   158 458 163  HOH   HOH A . 
D 3 HOH   159 459 408  HOH   HOH A . 
D 3 HOH   160 460 756  HOH   HOH A . 
D 3 HOH   161 461 726  HOH   HOH A . 
D 3 HOH   162 462 361  HOH   HOH A . 
D 3 HOH   163 463 63   HOH   HOH A . 
D 3 HOH   164 464 556  HOH   HOH A . 
D 3 HOH   165 465 801  HOH   HOH A . 
D 3 HOH   166 466 126  HOH   HOH A . 
D 3 HOH   167 467 280  HOH   HOH A . 
D 3 HOH   168 468 319  HOH   HOH A . 
D 3 HOH   169 469 1276 HOH   HOH A . 
D 3 HOH   170 470 250  HOH   HOH A . 
D 3 HOH   171 471 1307 HOH   HOH A . 
D 3 HOH   172 472 342  HOH   HOH A . 
D 3 HOH   173 473 1306 HOH   HOH A . 
D 3 HOH   174 474 267  HOH   HOH A . 
D 3 HOH   175 475 1287 HOH   HOH A . 
D 3 HOH   176 476 674  HOH   HOH A . 
D 3 HOH   177 477 695  HOH   HOH A . 
D 3 HOH   178 478 224  HOH   HOH A . 
D 3 HOH   179 479 919  HOH   HOH A . 
D 3 HOH   180 480 370  HOH   HOH A . 
D 3 HOH   181 481 202  HOH   HOH A . 
D 3 HOH   182 482 135  HOH   HOH A . 
D 3 HOH   183 483 309  HOH   HOH A . 
D 3 HOH   184 484 318  HOH   HOH A . 
D 3 HOH   185 485 805  HOH   HOH A . 
D 3 HOH   186 486 1299 HOH   HOH A . 
D 3 HOH   187 487 521  HOH   HOH A . 
D 3 HOH   188 488 152  HOH   HOH A . 
D 3 HOH   189 489 315  HOH   HOH A . 
D 3 HOH   190 490 263  HOH   HOH A . 
D 3 HOH   191 491 711  HOH   HOH A . 
D 3 HOH   192 492 331  HOH   HOH A . 
D 3 HOH   193 493 1314 HOH   HOH A . 
D 3 HOH   194 494 941  HOH   HOH A . 
D 3 HOH   195 495 1071 HOH   HOH A . 
D 3 HOH   196 496 208  HOH   HOH A . 
D 3 HOH   197 497 1284 HOH   HOH A . 
D 3 HOH   198 498 356  HOH   HOH A . 
D 3 HOH   199 499 326  HOH   HOH A . 
D 3 HOH   200 500 180  HOH   HOH A . 
D 3 HOH   201 501 350  HOH   HOH A . 
D 3 HOH   202 502 371  HOH   HOH A . 
D 3 HOH   203 503 363  HOH   HOH A . 
D 3 HOH   204 504 313  HOH   HOH A . 
D 3 HOH   205 505 429  HOH   HOH A . 
D 3 HOH   206 506 772  HOH   HOH A . 
D 3 HOH   207 507 185  HOH   HOH A . 
D 3 HOH   208 508 376  HOH   HOH A . 
D 3 HOH   209 509 1074 HOH   HOH A . 
D 3 HOH   210 510 346  HOH   HOH A . 
D 3 HOH   211 511 1292 HOH   HOH A . 
D 3 HOH   212 512 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 358  HOH   HOH B . 
E 3 HOH   3   203 398  HOH   HOH B . 
E 3 HOH   4   204 654  HOH   HOH B . 
E 3 HOH   5   205 900  HOH   HOH B . 
E 3 HOH   6   206 758  HOH   HOH B . 
E 3 HOH   7   207 364  HOH   HOH B . 
E 3 HOH   8   208 549  HOH   HOH B . 
E 3 HOH   9   209 1249 HOH   HOH B . 
E 3 HOH   10  210 240  HOH   HOH B . 
E 3 HOH   11  211 343  HOH   HOH B . 
E 3 HOH   12  212 120  HOH   HOH B . 
E 3 HOH   13  213 264  HOH   HOH B . 
E 3 HOH   14  214 743  HOH   HOH B . 
E 3 HOH   15  215 276  HOH   HOH B . 
E 3 HOH   16  216 131  HOH   HOH B . 
E 3 HOH   17  217 353  HOH   HOH B . 
E 3 HOH   18  218 452  HOH   HOH B . 
E 3 HOH   19  219 50   HOH   HOH B . 
E 3 HOH   20  220 723  HOH   HOH B . 
E 3 HOH   21  221 272  HOH   HOH B . 
E 3 HOH   22  222 332  HOH   HOH B . 
E 3 HOH   23  223 282  HOH   HOH B . 
E 3 HOH   24  224 1278 HOH   HOH B . 
E 3 HOH   25  225 54   HOH   HOH B . 
E 3 HOH   26  226 531  HOH   HOH B . 
E 3 HOH   27  227 444  HOH   HOH B . 
E 3 HOH   28  228 128  HOH   HOH B . 
E 3 HOH   29  229 127  HOH   HOH B . 
E 3 HOH   30  230 82   HOH   HOH B . 
E 3 HOH   31  231 1140 HOH   HOH B . 
E 3 HOH   32  232 232  HOH   HOH B . 
E 3 HOH   33  233 75   HOH   HOH B . 
E 3 HOH   34  234 205  HOH   HOH B . 
E 3 HOH   35  235 181  HOH   HOH B . 
E 3 HOH   36  236 9    HOH   HOH B . 
E 3 HOH   37  237 133  HOH   HOH B . 
E 3 HOH   38  238 30   HOH   HOH B . 
E 3 HOH   39  239 1    HOH   HOH B . 
E 3 HOH   40  240 60   HOH   HOH B . 
E 3 HOH   41  241 69   HOH   HOH B . 
E 3 HOH   42  242 231  HOH   HOH B . 
E 3 HOH   43  243 110  HOH   HOH B . 
E 3 HOH   44  244 14   HOH   HOH B . 
E 3 HOH   45  245 300  HOH   HOH B . 
E 3 HOH   46  246 1312 HOH   HOH B . 
E 3 HOH   47  247 166  HOH   HOH B . 
E 3 HOH   48  248 143  HOH   HOH B . 
E 3 HOH   49  249 52   HOH   HOH B . 
E 3 HOH   50  250 347  HOH   HOH B . 
E 3 HOH   51  251 129  HOH   HOH B . 
E 3 HOH   52  252 72   HOH   HOH B . 
E 3 HOH   53  253 10   HOH   HOH B . 
E 3 HOH   54  254 47   HOH   HOH B . 
E 3 HOH   55  255 31   HOH   HOH B . 
E 3 HOH   56  256 150  HOH   HOH B . 
E 3 HOH   57  257 325  HOH   HOH B . 
E 3 HOH   58  258 391  HOH   HOH B . 
E 3 HOH   59  259 1106 HOH   HOH B . 
E 3 HOH   60  260 62   HOH   HOH B . 
E 3 HOH   61  261 61   HOH   HOH B . 
E 3 HOH   62  262 172  HOH   HOH B . 
E 3 HOH   63  263 252  HOH   HOH B . 
E 3 HOH   64  264 387  HOH   HOH B . 
E 3 HOH   65  265 271  HOH   HOH B . 
E 3 HOH   66  266 341  HOH   HOH B . 
E 3 HOH   67  267 302  HOH   HOH B . 
E 3 HOH   68  268 59   HOH   HOH B . 
E 3 HOH   69  269 103  HOH   HOH B . 
E 3 HOH   70  270 77   HOH   HOH B . 
E 3 HOH   71  271 144  HOH   HOH B . 
E 3 HOH   72  272 41   HOH   HOH B . 
E 3 HOH   73  273 20   HOH   HOH B . 
E 3 HOH   74  274 84   HOH   HOH B . 
E 3 HOH   75  275 11   HOH   HOH B . 
E 3 HOH   76  276 242  HOH   HOH B . 
E 3 HOH   77  277 1305 HOH   HOH B . 
E 3 HOH   78  278 243  HOH   HOH B . 
E 3 HOH   79  279 43   HOH   HOH B . 
E 3 HOH   80  280 117  HOH   HOH B . 
E 3 HOH   81  281 1277 HOH   HOH B . 
E 3 HOH   82  282 175  HOH   HOH B . 
E 3 HOH   83  283 635  HOH   HOH B . 
E 3 HOH   84  284 221  HOH   HOH B . 
E 3 HOH   85  285 114  HOH   HOH B . 
E 3 HOH   86  286 22   HOH   HOH B . 
E 3 HOH   87  287 13   HOH   HOH B . 
E 3 HOH   88  288 1126 HOH   HOH B . 
E 3 HOH   89  289 137  HOH   HOH B . 
E 3 HOH   90  290 88   HOH   HOH B . 
E 3 HOH   91  291 287  HOH   HOH B . 
E 3 HOH   92  292 106  HOH   HOH B . 
E 3 HOH   93  293 216  HOH   HOH B . 
E 3 HOH   94  294 1066 HOH   HOH B . 
E 3 HOH   95  295 99   HOH   HOH B . 
E 3 HOH   96  296 235  HOH   HOH B . 
E 3 HOH   97  297 32   HOH   HOH B . 
E 3 HOH   98  298 297  HOH   HOH B . 
E 3 HOH   99  299 160  HOH   HOH B . 
E 3 HOH   100 300 112  HOH   HOH B . 
E 3 HOH   101 301 182  HOH   HOH B . 
E 3 HOH   102 302 147  HOH   HOH B . 
E 3 HOH   103 303 316  HOH   HOH B . 
E 3 HOH   104 304 416  HOH   HOH B . 
E 3 HOH   105 305 89   HOH   HOH B . 
E 3 HOH   106 306 215  HOH   HOH B . 
E 3 HOH   107 307 220  HOH   HOH B . 
E 3 HOH   108 308 118  HOH   HOH B . 
E 3 HOH   109 309 141  HOH   HOH B . 
E 3 HOH   110 310 38   HOH   HOH B . 
E 3 HOH   111 311 142  HOH   HOH B . 
E 3 HOH   112 312 299  HOH   HOH B . 
E 3 HOH   113 313 48   HOH   HOH B . 
E 3 HOH   114 314 1291 HOH   HOH B . 
E 3 HOH   115 315 704  HOH   HOH B . 
E 3 HOH   116 316 311  HOH   HOH B . 
E 3 HOH   117 317 91   HOH   HOH B . 
E 3 HOH   118 318 37   HOH   HOH B . 
E 3 HOH   119 319 101  HOH   HOH B . 
E 3 HOH   120 320 23   HOH   HOH B . 
E 3 HOH   121 321 161  HOH   HOH B . 
E 3 HOH   122 322 100  HOH   HOH B . 
E 3 HOH   123 323 170  HOH   HOH B . 
E 3 HOH   124 324 339  HOH   HOH B . 
E 3 HOH   125 325 44   HOH   HOH B . 
E 3 HOH   126 326 28   HOH   HOH B . 
E 3 HOH   127 327 177  HOH   HOH B . 
E 3 HOH   128 328 334  HOH   HOH B . 
E 3 HOH   129 329 29   HOH   HOH B . 
E 3 HOH   130 330 717  HOH   HOH B . 
E 3 HOH   131 331 1274 HOH   HOH B . 
E 3 HOH   132 332 98   HOH   HOH B . 
E 3 HOH   133 333 445  HOH   HOH B . 
E 3 HOH   134 334 1294 HOH   HOH B . 
E 3 HOH   135 335 1285 HOH   HOH B . 
E 3 HOH   136 336 207  HOH   HOH B . 
E 3 HOH   137 337 65   HOH   HOH B . 
E 3 HOH   138 338 55   HOH   HOH B . 
E 3 HOH   139 339 234  HOH   HOH B . 
E 3 HOH   140 340 197  HOH   HOH B . 
E 3 HOH   141 341 619  HOH   HOH B . 
E 3 HOH   142 342 1293 HOH   HOH B . 
E 3 HOH   143 343 362  HOH   HOH B . 
E 3 HOH   144 344 463  HOH   HOH B . 
E 3 HOH   145 345 178  HOH   HOH B . 
E 3 HOH   146 346 90   HOH   HOH B . 
E 3 HOH   147 347 335  HOH   HOH B . 
E 3 HOH   148 348 191  HOH   HOH B . 
E 3 HOH   149 349 623  HOH   HOH B . 
E 3 HOH   150 350 1046 HOH   HOH B . 
E 3 HOH   151 351 960  HOH   HOH B . 
E 3 HOH   152 352 1304 HOH   HOH B . 
E 3 HOH   153 353 541  HOH   HOH B . 
E 3 HOH   154 354 1280 HOH   HOH B . 
E 3 HOH   155 355 304  HOH   HOH B . 
E 3 HOH   156 356 203  HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 389  HOH   HOH B . 
E 3 HOH   159 359 87   HOH   HOH B . 
E 3 HOH   160 360 479  HOH   HOH B . 
E 3 HOH   161 361 1077 HOH   HOH B . 
E 3 HOH   162 362 283  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 718  HOH   HOH B . 
E 3 HOH   165 365 373  HOH   HOH B . 
E 3 HOH   166 366 898  HOH   HOH B . 
E 3 HOH   167 367 1316 HOH   HOH B . 
E 3 HOH   168 368 340  HOH   HOH B . 
E 3 HOH   169 369 667  HOH   HOH B . 
E 3 HOH   170 370 291  HOH   HOH B . 
E 3 HOH   171 371 310  HOH   HOH B . 
E 3 HOH   172 372 190  HOH   HOH B . 
E 3 HOH   173 373 1303 HOH   HOH B . 
E 3 HOH   174 374 615  HOH   HOH B . 
E 3 HOH   175 375 149  HOH   HOH B . 
E 3 HOH   176 376 431  HOH   HOH B . 
E 3 HOH   177 377 1163 HOH   HOH B . 
E 3 HOH   178 378 1173 HOH   HOH B . 
E 3 HOH   179 379 183  HOH   HOH B . 
E 3 HOH   180 380 418  HOH   HOH B . 
E 3 HOH   181 381 1000 HOH   HOH B . 
E 3 HOH   182 382 176  HOH   HOH B . 
E 3 HOH   183 383 424  HOH   HOH B . 
E 3 HOH   184 384 1311 HOH   HOH B . 
E 3 HOH   185 385 1298 HOH   HOH B . 
E 3 HOH   186 386 265  HOH   HOH B . 
E 3 HOH   187 387 491  HOH   HOH B . 
E 3 HOH   188 388 470  HOH   HOH B . 
E 3 HOH   189 389 248  HOH   HOH B . 
E 3 HOH   190 390 981  HOH   HOH B . 
E 3 HOH   191 391 360  HOH   HOH B . 
E 3 HOH   192 392 184  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 355  HOH   HOH B . 
E 3 HOH   195 395 274  HOH   HOH B . 
E 3 HOH   196 396 566  HOH   HOH B . 
E 3 HOH   197 397 792  HOH   HOH B . 
E 3 HOH   198 398 157  HOH   HOH B . 
E 3 HOH   199 399 314  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCG 
_cell.length_a           88.838 
_cell.length_b           88.838 
_cell.length_c           39.682 
_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                         7HCG 
_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          7HCG 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.16 
_exptl_crystal.density_percent_sol   42.98 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2022-06-29 
_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                     7HCG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.420 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165874 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.300 
_reflns.pdbx_Rmerge_I_obs            0.046 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.300 
_reflns.B_iso_Wilson_estimate        10.350 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.050 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1050024 
_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                      ? 
_reflns.pdbx_CC_star                 ? 
# 
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 
_reflns_shell.pdbx_CC_star 
1 1 1.000 1.020  ? 33463 7347 ? 0.663 ? ? ? 4.600 ? 1.400  ? ? ? ? ? ? 89.100 0.750 0.341 0.745 ? 
1 2 5.480 44.420 ? 7578  1102 ? 0.026 ? ? ? 6.900 ? 45.400 ? ? ? ? ? ? 99.800 0.029 0.011 0.999 ? 
# 
_refine.entry_id                                 7HCG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.4200 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2600 
_refine.ls_number_reflns_obs                     165808 
_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                          0.1378 
_refine.ls_R_factor_R_work                       0.1373 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1486 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8100 
_refine.ls_number_reflns_R_free                  7983 
_refine.ls_number_reflns_R_work                  157825 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.6148 
_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                            0.0800 
_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                                50.340 
_refine.B_iso_min                                7.590 
_refine.pdbx_overall_phase_error                 13.6200 
_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                        44.4200 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             413 
_refine_hist.number_atoms_total               2983 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.73 
_refine_hist.pdbx_B_iso_mean_solvent          27.20 
_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 
_refine_ls_shell.R_factor_obs 
1.0000 1.0100  30 86.0000  4550 . 0.3037 0.2607 . 228 0.0000 4778 . 'X-RAY DIFFRACTION' . 
1.0100 1.0200  30 95.0000  5047 . 0.2376 0.2295 . 249 0.0000 5296 . 'X-RAY DIFFRACTION' . 
1.0200 1.0400  30 100.0000 5259 . 0.2038 0.2187 . 228 0.0000 5487 . 'X-RAY DIFFRACTION' . 
1.0400 1.0500  30 100.0000 5258 . 0.1731 0.1845 . 291 0.0000 5549 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5217 . 0.1612 0.1713 . 301 0.0000 5518 . 'X-RAY DIFFRACTION' . 
1.0600 1.0800  30 100.0000 5308 . 0.1630 0.1690 . 271 0.0000 5579 . 'X-RAY DIFFRACTION' . 
1.0800 1.0900  30 100.0000 5295 . 0.1502 0.1572 . 266 0.0000 5561 . 'X-RAY DIFFRACTION' . 
1.0900 1.1100  30 100.0000 5258 . 0.1378 0.1563 . 260 0.0000 5518 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5240 . 0.1292 0.1536 . 281 0.0000 5521 . 'X-RAY DIFFRACTION' . 
1.1300 1.1400  30 100.0000 5333 . 0.1219 0.1262 . 237 0.0000 5570 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5261 . 0.1170 0.1398 . 241 0.0000 5502 . 'X-RAY DIFFRACTION' . 
1.1600 1.1900  30 100.0000 5275 . 0.1147 0.1333 . 272 0.0000 5547 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 5255 . 0.1109 0.1453 . 290 0.0000 5545 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5294 . 0.1095 0.1206 . 251 0.0000 5545 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 5257 . 0.1124 0.1286 . 270 0.0000 5527 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 5317 . 0.1157 0.1252 . 258 0.0000 5575 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 5249 . 0.1167 0.1275 . 293 0.0000 5542 . 'X-RAY DIFFRACTION' . 
1.3200 1.3600  30 100.0000 5274 . 0.1211 0.1277 . 278 0.0000 5552 . 'X-RAY DIFFRACTION' . 
1.3600 1.4000  30 100.0000 5302 . 0.1171 0.1435 . 255 0.0000 5557 . 'X-RAY DIFFRACTION' . 
1.4000 1.4400  30 100.0000 5271 . 0.1153 0.1402 . 258 0.0000 5529 . 'X-RAY DIFFRACTION' . 
1.4400 1.4900  30 100.0000 5314 . 0.1162 0.1244 . 259 0.0000 5573 . 'X-RAY DIFFRACTION' . 
1.4900 1.5500  30 100.0000 5297 . 0.1156 0.1197 . 277 0.0000 5574 . 'X-RAY DIFFRACTION' . 
1.5500 1.6200  30 100.0000 5275 . 0.1157 0.1343 . 264 0.0000 5539 . 'X-RAY DIFFRACTION' . 
1.6200 1.7100  30 100.0000 5325 . 0.1224 0.1395 . 263 0.0000 5588 . 'X-RAY DIFFRACTION' . 
1.7100 1.8200  30 100.0000 5306 . 0.1312 0.1427 . 253 0.0000 5559 . 'X-RAY DIFFRACTION' . 
1.8200 1.9600  30 100.0000 5298 . 0.1340 0.1265 . 285 0.0000 5583 . 'X-RAY DIFFRACTION' . 
1.9600 2.1500  30 100.0000 5313 . 0.1382 0.1418 . 278 0.0000 5591 . 'X-RAY DIFFRACTION' . 
2.1500 2.4700  30 100.0000 5306 . 0.1405 0.1387 . 297 0.0000 5603 . 'X-RAY DIFFRACTION' . 
2.4700 3.1100  30 100.0000 5370 . 0.1539 0.1674 . 260 0.0000 5630 . 'X-RAY DIFFRACTION' . 
3.1100 44.4200 30 100.0000 5501 . 0.1496 0.1725 . 269 0.0000 5770 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCG 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000316' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCG 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_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 7HCG A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCG 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 7HCG SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCG MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCG SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCG 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 
2 1 B,E   
# 
_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 TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCG 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.53 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.59 
3 1 OH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 2.10 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.15 -133.53 
2 1 SER A 128 ? B 74.81 -6.25   
3 1 HIS B 86  ? ? 56.62 -128.15 
# 
_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 510 ? 5.95 . 
2 1 O ? A HOH 511 ? 6.06 . 
3 1 O ? A HOH 512 ? 7.60 . 
4 1 O ? B HOH 401 ? 6.35 . 
# 
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 
A1A5B C3   C Y N 1   
A1A5B C6   C Y N 2   
A1A5B C9   C Y N 3   
A1A5B C12  C Y N 4   
A1A5B C1   C N N 5   
A1A5B C10  C Y N 6   
A1A5B C11  C N N 7   
A1A5B C13  C Y N 8   
A1A5B C2   C Y N 9   
A1A5B C4   C N N 10  
A1A5B C5   C Y N 11  
A1A5B C7   C Y N 12  
A1A5B C8   C Y N 13  
A1A5B N1   N N N 14  
A1A5B O1   O N N 15  
A1A5B O2   O N N 16  
A1A5B O3   O N N 17  
A1A5B O4   O N N 18  
A1A5B O5   O N N 19  
A1A5B S1   S Y N 20  
A1A5B H3   H N N 21  
A1A5B H5   H N N 22  
A1A5B H7   H N N 23  
A1A5B H6   H N N 24  
A1A5B H8   H N N 25  
A1A5B H2   H N N 26  
A1A5B H4   H N N 27  
A1A5B H1   H N N 28  
A1A5B H9   H N N 29  
ALA   N    N N N 30  
ALA   CA   C N S 31  
ALA   C    C N N 32  
ALA   O    O N N 33  
ALA   CB   C N N 34  
ALA   OXT  O N N 35  
ALA   H    H N N 36  
ALA   H2   H N N 37  
ALA   HA   H N N 38  
ALA   HB1  H N N 39  
ALA   HB2  H N N 40  
ALA   HB3  H N N 41  
ALA   HXT  H N N 42  
ARG   N    N N N 43  
ARG   CA   C N S 44  
ARG   C    C N N 45  
ARG   O    O N N 46  
ARG   CB   C N N 47  
ARG   CG   C N N 48  
ARG   CD   C N N 49  
ARG   NE   N N N 50  
ARG   CZ   C N N 51  
ARG   NH1  N N N 52  
ARG   NH2  N N N 53  
ARG   OXT  O N N 54  
ARG   H    H N N 55  
ARG   H2   H N N 56  
ARG   HA   H N N 57  
ARG   HB2  H N N 58  
ARG   HB3  H N N 59  
ARG   HG2  H N N 60  
ARG   HG3  H N N 61  
ARG   HD2  H N N 62  
ARG   HD3  H N N 63  
ARG   HE   H N N 64  
ARG   HH11 H N N 65  
ARG   HH12 H N N 66  
ARG   HH21 H N N 67  
ARG   HH22 H N N 68  
ARG   HXT  H N N 69  
ASN   N    N N N 70  
ASN   CA   C N S 71  
ASN   C    C N N 72  
ASN   O    O N N 73  
ASN   CB   C N N 74  
ASN   CG   C N N 75  
ASN   OD1  O N N 76  
ASN   ND2  N N N 77  
ASN   OXT  O N N 78  
ASN   H    H N N 79  
ASN   H2   H N N 80  
ASN   HA   H N N 81  
ASN   HB2  H N N 82  
ASN   HB3  H N N 83  
ASN   HD21 H N N 84  
ASN   HD22 H N N 85  
ASN   HXT  H N N 86  
ASP   N    N N N 87  
ASP   CA   C N S 88  
ASP   C    C N N 89  
ASP   O    O N N 90  
ASP   CB   C N N 91  
ASP   CG   C N N 92  
ASP   OD1  O N N 93  
ASP   OD2  O N N 94  
ASP   OXT  O N N 95  
ASP   H    H N N 96  
ASP   H2   H N N 97  
ASP   HA   H N N 98  
ASP   HB2  H N N 99  
ASP   HB3  H N N 100 
ASP   HD2  H N N 101 
ASP   HXT  H N N 102 
CYS   N    N N N 103 
CYS   CA   C N R 104 
CYS   C    C N N 105 
CYS   O    O N N 106 
CYS   CB   C N N 107 
CYS   SG   S N N 108 
CYS   OXT  O N N 109 
CYS   H    H N N 110 
CYS   H2   H N N 111 
CYS   HA   H N N 112 
CYS   HB2  H N N 113 
CYS   HB3  H N N 114 
CYS   HG   H N N 115 
CYS   HXT  H N N 116 
GLN   N    N N N 117 
GLN   CA   C N S 118 
GLN   C    C N N 119 
GLN   O    O N N 120 
GLN   CB   C N N 121 
GLN   CG   C N N 122 
GLN   CD   C N N 123 
GLN   OE1  O N N 124 
GLN   NE2  N N N 125 
GLN   OXT  O N N 126 
GLN   H    H N N 127 
GLN   H2   H N N 128 
GLN   HA   H N N 129 
GLN   HB2  H N N 130 
GLN   HB3  H N N 131 
GLN   HG2  H N N 132 
GLN   HG3  H N N 133 
GLN   HE21 H N N 134 
GLN   HE22 H N N 135 
GLN   HXT  H N N 136 
GLU   N    N N N 137 
GLU   CA   C N S 138 
GLU   C    C N N 139 
GLU   O    O N N 140 
GLU   CB   C N N 141 
GLU   CG   C N N 142 
GLU   CD   C N N 143 
GLU   OE1  O N N 144 
GLU   OE2  O N N 145 
GLU   OXT  O N N 146 
GLU   H    H N N 147 
GLU   H2   H N N 148 
GLU   HA   H N N 149 
GLU   HB2  H N N 150 
GLU   HB3  H N N 151 
GLU   HG2  H N N 152 
GLU   HG3  H N N 153 
GLU   HE2  H N N 154 
GLU   HXT  H N N 155 
GLY   N    N N N 156 
GLY   CA   C N N 157 
GLY   C    C N N 158 
GLY   O    O N N 159 
GLY   OXT  O N N 160 
GLY   H    H N N 161 
GLY   H2   H N N 162 
GLY   HA2  H N N 163 
GLY   HA3  H N N 164 
GLY   HXT  H N N 165 
HIS   N    N N N 166 
HIS   CA   C N S 167 
HIS   C    C N N 168 
HIS   O    O N N 169 
HIS   CB   C N N 170 
HIS   CG   C Y N 171 
HIS   ND1  N Y N 172 
HIS   CD2  C Y N 173 
HIS   CE1  C Y N 174 
HIS   NE2  N Y N 175 
HIS   OXT  O N N 176 
HIS   H    H N N 177 
HIS   H2   H N N 178 
HIS   HA   H N N 179 
HIS   HB2  H N N 180 
HIS   HB3  H N N 181 
HIS   HD1  H N N 182 
HIS   HD2  H N N 183 
HIS   HE1  H N N 184 
HIS   HE2  H N N 185 
HIS   HXT  H N N 186 
HOH   O    O N N 187 
HOH   H1   H N N 188 
HOH   H2   H N N 189 
ILE   N    N N N 190 
ILE   CA   C N S 191 
ILE   C    C N N 192 
ILE   O    O N N 193 
ILE   CB   C N S 194 
ILE   CG1  C N N 195 
ILE   CG2  C N N 196 
ILE   CD1  C N N 197 
ILE   OXT  O N N 198 
ILE   H    H N N 199 
ILE   H2   H N N 200 
ILE   HA   H N N 201 
ILE   HB   H N N 202 
ILE   HG12 H N N 203 
ILE   HG13 H N N 204 
ILE   HG21 H N N 205 
ILE   HG22 H N N 206 
ILE   HG23 H N N 207 
ILE   HD11 H N N 208 
ILE   HD12 H N N 209 
ILE   HD13 H N N 210 
ILE   HXT  H N N 211 
LEU   N    N N N 212 
LEU   CA   C N S 213 
LEU   C    C N N 214 
LEU   O    O N N 215 
LEU   CB   C N N 216 
LEU   CG   C N N 217 
LEU   CD1  C N N 218 
LEU   CD2  C N N 219 
LEU   OXT  O N N 220 
LEU   H    H N N 221 
LEU   H2   H N N 222 
LEU   HA   H N N 223 
LEU   HB2  H N N 224 
LEU   HB3  H N N 225 
LEU   HG   H N N 226 
LEU   HD11 H N N 227 
LEU   HD12 H N N 228 
LEU   HD13 H N N 229 
LEU   HD21 H N N 230 
LEU   HD22 H N N 231 
LEU   HD23 H N N 232 
LEU   HXT  H N N 233 
LYS   N    N N N 234 
LYS   CA   C N S 235 
LYS   C    C N N 236 
LYS   O    O N N 237 
LYS   CB   C N N 238 
LYS   CG   C N N 239 
LYS   CD   C N N 240 
LYS   CE   C N N 241 
LYS   NZ   N N N 242 
LYS   OXT  O N N 243 
LYS   H    H N N 244 
LYS   H2   H N N 245 
LYS   HA   H N N 246 
LYS   HB2  H N N 247 
LYS   HB3  H N N 248 
LYS   HG2  H N N 249 
LYS   HG3  H N N 250 
LYS   HD2  H N N 251 
LYS   HD3  H N N 252 
LYS   HE2  H N N 253 
LYS   HE3  H N N 254 
LYS   HZ1  H N N 255 
LYS   HZ2  H N N 256 
LYS   HZ3  H N N 257 
LYS   HXT  H N N 258 
MET   N    N N N 259 
MET   CA   C N S 260 
MET   C    C N N 261 
MET   O    O N N 262 
MET   CB   C N N 263 
MET   CG   C N N 264 
MET   SD   S N N 265 
MET   CE   C N N 266 
MET   OXT  O N N 267 
MET   H    H N N 268 
MET   H2   H N N 269 
MET   HA   H N N 270 
MET   HB2  H N N 271 
MET   HB3  H N N 272 
MET   HG2  H N N 273 
MET   HG3  H N N 274 
MET   HE1  H N N 275 
MET   HE2  H N N 276 
MET   HE3  H N N 277 
MET   HXT  H N N 278 
PHE   N    N N N 279 
PHE   CA   C N S 280 
PHE   C    C N N 281 
PHE   O    O N N 282 
PHE   CB   C N N 283 
PHE   CG   C Y N 284 
PHE   CD1  C Y N 285 
PHE   CD2  C Y N 286 
PHE   CE1  C Y N 287 
PHE   CE2  C Y N 288 
PHE   CZ   C Y N 289 
PHE   OXT  O N N 290 
PHE   H    H N N 291 
PHE   H2   H N N 292 
PHE   HA   H N N 293 
PHE   HB2  H N N 294 
PHE   HB3  H N N 295 
PHE   HD1  H N N 296 
PHE   HD2  H N N 297 
PHE   HE1  H N N 298 
PHE   HE2  H N N 299 
PHE   HZ   H N N 300 
PHE   HXT  H N N 301 
PRO   N    N N N 302 
PRO   CA   C N S 303 
PRO   C    C N N 304 
PRO   O    O N N 305 
PRO   CB   C N N 306 
PRO   CG   C N N 307 
PRO   CD   C N N 308 
PRO   OXT  O N N 309 
PRO   H    H N N 310 
PRO   HA   H N N 311 
PRO   HB2  H N N 312 
PRO   HB3  H N N 313 
PRO   HG2  H N N 314 
PRO   HG3  H N N 315 
PRO   HD2  H N N 316 
PRO   HD3  H N N 317 
PRO   HXT  H N N 318 
SER   N    N N N 319 
SER   CA   C N S 320 
SER   C    C N N 321 
SER   O    O N N 322 
SER   CB   C N N 323 
SER   OG   O N N 324 
SER   OXT  O N N 325 
SER   H    H N N 326 
SER   H2   H N N 327 
SER   HA   H N N 328 
SER   HB2  H N N 329 
SER   HB3  H N N 330 
SER   HG   H N N 331 
SER   HXT  H N N 332 
THR   N    N N N 333 
THR   CA   C N S 334 
THR   C    C N N 335 
THR   O    O N N 336 
THR   CB   C N R 337 
THR   OG1  O N N 338 
THR   CG2  C N N 339 
THR   OXT  O N N 340 
THR   H    H N N 341 
THR   H2   H N N 342 
THR   HA   H N N 343 
THR   HB   H N N 344 
THR   HG1  H N N 345 
THR   HG21 H N N 346 
THR   HG22 H N N 347 
THR   HG23 H N N 348 
THR   HXT  H N N 349 
TYR   N    N N N 350 
TYR   CA   C N S 351 
TYR   C    C N N 352 
TYR   O    O N N 353 
TYR   CB   C N N 354 
TYR   CG   C Y N 355 
TYR   CD1  C Y N 356 
TYR   CD2  C Y N 357 
TYR   CE1  C Y N 358 
TYR   CE2  C Y N 359 
TYR   CZ   C Y N 360 
TYR   OH   O N N 361 
TYR   OXT  O N N 362 
TYR   H    H N N 363 
TYR   H2   H N N 364 
TYR   HA   H N N 365 
TYR   HB2  H N N 366 
TYR   HB3  H N N 367 
TYR   HD1  H N N 368 
TYR   HD2  H N N 369 
TYR   HE1  H N N 370 
TYR   HE2  H N N 371 
TYR   HH   H N N 372 
TYR   HXT  H N N 373 
VAL   N    N N N 374 
VAL   CA   C N S 375 
VAL   C    C N N 376 
VAL   O    O N N 377 
VAL   CB   C N N 378 
VAL   CG1  C N N 379 
VAL   CG2  C N N 380 
VAL   OXT  O N N 381 
VAL   H    H N N 382 
VAL   H2   H N N 383 
VAL   HA   H N N 384 
VAL   HB   H N N 385 
VAL   HG11 H N N 386 
VAL   HG12 H N N 387 
VAL   HG13 H N N 388 
VAL   HG21 H N N 389 
VAL   HG22 H N N 390 
VAL   HG23 H N N 391 
VAL   HXT  H N N 392 
# 
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 
A1A5B C5  S1   sing Y N 1   
A1A5B C5  C6   doub Y N 2   
A1A5B S1  C3   sing Y N 3   
A1A5B C6  C2   sing Y N 4   
A1A5B O1  C1   doub N N 5   
A1A5B C2  C3   doub Y N 6   
A1A5B C2  N1   sing N N 7   
A1A5B C3  C4   sing N N 8   
A1A5B O5  C4   doub N N 9   
A1A5B C1  N1   sing N N 10  
A1A5B C1  C7   sing N N 11  
A1A5B C4  O2   sing N N 12  
A1A5B C13 C7   doub Y N 13  
A1A5B C13 C12  sing Y N 14  
A1A5B C7  C8   sing Y N 15  
A1A5B O4  C12  sing N N 16  
A1A5B O4  C11  sing N N 17  
A1A5B C12 C10  doub Y N 18  
A1A5B C8  C9   doub Y N 19  
A1A5B C10 C9   sing Y N 20  
A1A5B C10 O3   sing N N 21  
A1A5B C11 O3   sing N N 22  
A1A5B C6  H3   sing N N 23  
A1A5B C9  H5   sing N N 24  
A1A5B C11 H7   sing N N 25  
A1A5B C11 H6   sing N N 26  
A1A5B C13 H8   sing N N 27  
A1A5B C5  H2   sing N N 28  
A1A5B C8  H4   sing N N 29  
A1A5B N1  H1   sing N N 30  
A1A5B O2  H9   sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
PHE   N   CA   sing N N 268 
PHE   N   H    sing N N 269 
PHE   N   H2   sing N N 270 
PHE   CA  C    sing N N 271 
PHE   CA  CB   sing N N 272 
PHE   CA  HA   sing N N 273 
PHE   C   O    doub N N 274 
PHE   C   OXT  sing N N 275 
PHE   CB  CG   sing N N 276 
PHE   CB  HB2  sing N N 277 
PHE   CB  HB3  sing N N 278 
PHE   CG  CD1  doub Y N 279 
PHE   CG  CD2  sing Y N 280 
PHE   CD1 CE1  sing Y N 281 
PHE   CD1 HD1  sing N N 282 
PHE   CD2 CE2  doub Y N 283 
PHE   CD2 HD2  sing N N 284 
PHE   CE1 CZ   doub Y N 285 
PHE   CE1 HE1  sing N N 286 
PHE   CE2 CZ   sing Y N 287 
PHE   CE2 HE2  sing N N 288 
PHE   CZ  HZ   sing N N 289 
PHE   OXT HXT  sing N N 290 
PRO   N   CA   sing N N 291 
PRO   N   CD   sing N N 292 
PRO   N   H    sing N N 293 
PRO   CA  C    sing N N 294 
PRO   CA  CB   sing N N 295 
PRO   CA  HA   sing N N 296 
PRO   C   O    doub N N 297 
PRO   C   OXT  sing N N 298 
PRO   CB  CG   sing N N 299 
PRO   CB  HB2  sing N N 300 
PRO   CB  HB3  sing N N 301 
PRO   CG  CD   sing N N 302 
PRO   CG  HG2  sing N N 303 
PRO   CG  HG3  sing N N 304 
PRO   CD  HD2  sing N N 305 
PRO   CD  HD3  sing N N 306 
PRO   OXT HXT  sing N N 307 
SER   N   CA   sing N N 308 
SER   N   H    sing N N 309 
SER   N   H2   sing N N 310 
SER   CA  C    sing N N 311 
SER   CA  CB   sing N N 312 
SER   CA  HA   sing N N 313 
SER   C   O    doub N N 314 
SER   C   OXT  sing N N 315 
SER   CB  OG   sing N N 316 
SER   CB  HB2  sing N N 317 
SER   CB  HB3  sing N N 318 
SER   OG  HG   sing N N 319 
SER   OXT HXT  sing N N 320 
THR   N   CA   sing N N 321 
THR   N   H    sing N N 322 
THR   N   H2   sing N N 323 
THR   CA  C    sing N N 324 
THR   CA  CB   sing N N 325 
THR   CA  HA   sing N N 326 
THR   C   O    doub N N 327 
THR   C   OXT  sing N N 328 
THR   CB  OG1  sing N N 329 
THR   CB  CG2  sing N N 330 
THR   CB  HB   sing N N 331 
THR   OG1 HG1  sing N N 332 
THR   CG2 HG21 sing N N 333 
THR   CG2 HG22 sing N N 334 
THR   CG2 HG23 sing N N 335 
THR   OXT HXT  sing N N 336 
TYR   N   CA   sing N N 337 
TYR   N   H    sing N N 338 
TYR   N   H2   sing N N 339 
TYR   CA  C    sing N N 340 
TYR   CA  CB   sing N N 341 
TYR   CA  HA   sing N N 342 
TYR   C   O    doub N N 343 
TYR   C   OXT  sing N N 344 
TYR   CB  CG   sing N N 345 
TYR   CB  HB2  sing N N 346 
TYR   CB  HB3  sing N N 347 
TYR   CG  CD1  doub Y N 348 
TYR   CG  CD2  sing Y N 349 
TYR   CD1 CE1  sing Y N 350 
TYR   CD1 HD1  sing N N 351 
TYR   CD2 CE2  doub Y N 352 
TYR   CD2 HD2  sing N N 353 
TYR   CE1 CZ   doub Y N 354 
TYR   CE1 HE1  sing N N 355 
TYR   CE2 CZ   sing Y N 356 
TYR   CE2 HE2  sing N N 357 
TYR   CZ  OH   sing N N 358 
TYR   OH  HH   sing N N 359 
TYR   OXT HXT  sing N N 360 
VAL   N   CA   sing N N 361 
VAL   N   H    sing N N 362 
VAL   N   H2   sing N N 363 
VAL   CA  C    sing N N 364 
VAL   CA  CB   sing N N 365 
VAL   CA  HA   sing N N 366 
VAL   C   O    doub N N 367 
VAL   C   OXT  sing N N 368 
VAL   CB  CG1  sing N N 369 
VAL   CB  CG2  sing N N 370 
VAL   CB  HB   sing N N 371 
VAL   CG1 HG11 sing N N 372 
VAL   CG1 HG12 sing N N 373 
VAL   CG1 HG13 sing N N 374 
VAL   CG2 HG21 sing N N 375 
VAL   CG2 HG22 sing N N 376 
VAL   CG2 HG23 sing N N 377 
VAL   OXT HXT  sing N N 378 
# 
_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                    7HCG 
_atom_sites.fract_transf_matrix[1][1]   0.011256 
_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]   0.011256 
_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]   0.025200 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.763 -16.416 22.356  0.86 40.96 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.674 -16.387 22.431  0.14 40.68 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.795 -15.336 22.516  0.86 40.65 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.738 -15.285 22.613  0.14 40.39 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.447 -13.992 22.214  0.86 39.06 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.408 -13.958 22.283  0.14 39.04 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.573 -13.728 22.636  0.86 39.17 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.510 -13.675 22.752  0.14 39.39 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.164 -15.355 23.924  0.86 41.63 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.158 -15.271 24.040  0.14 41.16 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.172 -14.210 24.085  0.86 41.94 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.212 -14.092 24.220  0.14 41.40 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.484 -16.691 24.179  0.86 41.91 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.445 -16.581 24.336  0.14 41.40 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.080 -15.461 21.877  0.86 48.79 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.997 -15.396 22.000  0.14 48.48 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.862 -15.243 24.588  0.86 49.96 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.883 -15.174 24.677  0.14 49.40 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.653 -14.355 24.893  0.86 50.34 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.708 -14.216 25.039  0.14 49.69 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.658 -13.374 24.152  0.86 50.34 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.729 -13.273 24.273  0.14 49.69 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.582 -14.192 23.315  0.86 50.34 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.607 -14.055 23.463  0.14 49.69 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.045 -16.663 25.043  0.86 50.31 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.042 -16.529 25.217  0.14 49.69 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.830 -16.849 23.480  0.86 50.31 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.758 -16.724 23.666  0.14 49.69 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.153 -17.393 24.169  0.86 50.31 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.090 -17.305 24.310  0.14 49.69 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.735 -13.147 21.469  1.00 36.98 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.187 -11.799 21.152  1.00 32.71 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.035 -10.828 21.373  1.00 29.38 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.903 -11.226 21.672  1.00 28.95 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.758 -11.688 19.729  1.00 31.60 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.745 -12.034 18.660  1.00 30.46 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.684 -11.417 18.575  1.00 30.01 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.080 -13.006 17.816  1.00 30.21 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.968 -13.341 21.128  0.86 44.39 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.993 -13.360 21.087  0.14 44.39 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.892 -11.556 21.768  1.00 39.26 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.048 -10.773 19.576  1.00 37.93 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.509 -12.292 19.641  1.00 37.93 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.540 -13.237 17.187  1.00 36.26 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.835 -13.410 17.902  1.00 36.26 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.328 -9.539  21.218  1.00 26.32 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.392 -8.490  21.594  1.00 23.92 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.498 -8.019  20.451  1.00 21.22 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.706 -7.094  20.653  1.00 21.88 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.145 -7.299  22.193  1.00 24.65 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.044 -6.744  21.253  1.00 24.97 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.076 -9.246  20.895  1.00 31.59 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.815 -8.836  22.286  1.00 28.71 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.506 -6.618  22.455  1.00 29.59 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.647 -7.597  22.970  1.00 29.59 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.455 -6.087  21.596  1.00 29.97 ?  5   SER   A HG   1 
ATOM   57   N N    . PHE   A 1 6   ? 16.577 -8.625  19.271  1.00 17.96 ?  6   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 6   ? 15.685 -8.227  18.187  1.00 16.01 ?  6   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 6   ? 14.248 -8.589  18.549  1.00 16.60 ?  6   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 6   ? 13.972 -9.710  18.986  1.00 18.07 ?  6   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 6   ? 16.088 -8.919  16.889  1.00 14.76 ?  6   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 6   ? 17.357 -8.380  16.280  1.00 13.93 ?  6   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 6   ? 17.358 -7.182  15.589  1.00 14.24 ?  6   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 6   ? 18.541 -9.089  16.376  1.00 15.04 ?  6   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 6   ? 18.524 -6.695  15.019  1.00 14.35 ?  6   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 6   ? 19.705 -8.611  15.807  1.00 15.34 ?  6   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 6   ? 19.696 -7.415  15.126  1.00 15.08 ?  6   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 6   ? 17.120 -9.265  19.078  1.00 21.56 ?  6   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 6   ? 15.739 -7.271  18.060  1.00 19.22 ?  6   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 6   ? 16.222 -9.866  17.065  1.00 17.72 ?  6   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 6   ? 15.375 -8.808  16.240  1.00 17.72 ?  6   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 6   ? 16.568 -6.694  15.508  1.00 17.09 ?  6   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 6   ? 18.553 -9.899  16.832  1.00 18.06 ?  6   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 6   ? 18.517 -5.882  14.558  1.00 17.23 ?  6   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 6   ? 20.495 -9.093  15.886  1.00 18.42 ?  6   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 6   ? 20.481 -7.081  14.747  1.00 18.10 ?  6   PHE   A HZ   1 
ATOM   77   N N    . SER   A 1 7   ? 13.325 -7.642  18.367  1.00 16.55 ?  7   SER   A N    1 
ATOM   78   C CA   . SER   A 1 7   ? 11.960 -7.789  18.857  1.00 17.82 ?  7   SER   A CA   1 
ATOM   79   C C    . SER   A 1 7   ? 10.950 -7.511  17.751  1.00 16.63 ?  7   SER   A C    1 
ATOM   80   O O    . SER   A 1 7   ? 11.154 -6.621  16.920  1.00 16.91 ?  7   SER   A O    1 
ATOM   81   C CB   . SER   A 1 7   ? 11.714 -6.832  20.029  1.00 20.45 ?  7   SER   A CB   1 
ATOM   82   O OG   . SER   A 1 7   ? 10.362 -6.872  20.447  1.00 22.59 ?  7   SER   A OG   1 
ATOM   83   H H    . SER   A 1 7   ? 13.469 -6.897  17.955  1.00 19.87 ?  7   SER   A H    1 
ATOM   84   H HA   . SER   A 1 7   ? 11.822 -8.694  19.171  1.00 21.39 ?  7   SER   A HA   1 
ATOM   85   H HB2  . SER   A 1 7   ? 12.281 -7.093  20.774  1.00 24.55 ?  7   SER   A HB2  1 
ATOM   86   H HB3  . SER   A 1 7   ? 11.931 -5.927  19.752  1.00 24.55 ?  7   SER   A HB3  1 
ATOM   87   H HG   . SER   A 1 7   ? 10.242 -6.345  21.090  1.00 27.12 ?  7   SER   A HG   1 
ATOM   88   N N    . GLY   A 1 8   ? 9.852  -8.271  17.755  1.00 16.24 ?  8   GLY   A N    1 
ATOM   89   C CA   . GLY   A 1 8   ? 8.763  -8.021  16.835  1.00 16.01 ?  8   GLY   A CA   1 
ATOM   90   C C    . GLY   A 1 8   ? 8.964  -8.522  15.425  1.00 14.94 ?  8   GLY   A C    1 
ATOM   91   O O    . GLY   A 1 8   ? 8.212  -8.112  14.532  1.00 16.10 ?  8   GLY   A O    1 
ATOM   92   H H    . GLY   A 1 8   ? 9.720  -8.934  18.288  1.00 19.49 ?  8   GLY   A H    1 
ATOM   93   H HA2  . GLY   A 1 8   ? 7.961  -8.441  17.182  1.00 19.23 ?  8   GLY   A HA2  1 
ATOM   94   H HA3  . GLY   A 1 8   ? 8.605  -7.066  16.791  1.00 19.23 ?  8   GLY   A HA3  1 
ATOM   95   N N    . TYR   A 1 9   ? 9.946  -9.390  15.189  1.00 13.52 ?  9   TYR   A N    1 
ATOM   96   C CA   . TYR   A 1 9   ? 10.187 -9.931  13.860  1.00 12.47 ?  9   TYR   A CA   1 
ATOM   97   C C    . TYR   A 1 9   ? 9.302  -11.144 13.591  1.00 12.47 ?  9   TYR   A C    1 
ATOM   98   O O    . TYR   A 1 9   ? 9.015  -11.952 14.482  1.00 14.37 ?  9   TYR   A O    1 
ATOM   99   C CB   . TYR   A 1 9   ? 11.662 -10.336 13.682  1.00 12.60 ?  9   TYR   A CB   1 
ATOM   100  C CG   . TYR   A 1 9   ? 12.583 -9.150  13.528  1.00 12.44 ?  9   TYR   A CG   1 
ATOM   101  C CD1  . TYR   A 1 9   ? 12.914 -8.359  14.618  1.00 13.20 ?  9   TYR   A CD1  1 
ATOM   102  C CD2  . TYR   A 1 9   ? 13.100 -8.801  12.288  1.00 12.27 ?  9   TYR   A CD2  1 
ATOM   103  C CE1  . TYR   A 1 9   ? 13.728 -7.250  14.481  1.00 13.44 ?  9   TYR   A CE1  1 
ATOM   104  C CE2  . TYR   A 1 9   ? 13.914 -7.693  12.137  1.00 12.84 ?  9   TYR   A CE2  1 
ATOM   105  C CZ   . TYR   A 1 9   ? 14.226 -6.920  13.238  1.00 13.41 ?  9   TYR   A CZ   1 
ATOM   106  O OH   . TYR   A 1 9   ? 15.026 -5.818  13.095  1.00 14.55 ?  9   TYR   A OH   1 
ATOM   107  H H    . TYR   A 1 9   ? 10.501 -9.675  15.789  1.00 16.23 ?  9   TYR   A H    1 
ATOM   108  H HA   . TYR   A 1 9   ? 9.990  -9.246  13.197  1.00 14.98 ?  9   TYR   A HA   1 
ATOM   109  H HB2  . TYR   A 1 9   ? 11.954 -10.854 14.447  1.00 15.13 ?  9   TYR   A HB2  1 
ATOM   110  H HB3  . TYR   A 1 9   ? 11.724 -10.869 12.874  1.00 15.13 ?  9   TYR   A HB3  1 
ATOM   111  H HD1  . TYR   A 1 9   ? 12.564 -8.575  15.453  1.00 15.85 ?  9   TYR   A HD1  1 
ATOM   112  H HD2  . TYR   A 1 9   ? 12.889 -9.317  11.540  1.00 14.73 ?  9   TYR   A HD2  1 
ATOM   113  H HE1  . TYR   A 1 9   ? 13.933 -6.732  15.224  1.00 16.14 ?  9   TYR   A HE1  1 
ATOM   114  H HE2  . TYR   A 1 9   ? 14.262 -7.475  11.298  1.00 15.41 ?  9   TYR   A HE2  1 
ATOM   115  H HH   . TYR   A 1 9   ? 15.144 -5.448  13.844  1.00 17.47 ?  9   TYR   A HH   1 
ATOM   116  N N    . LEU   A 1 10  ? 8.880  -11.270 12.336  1.00 11.85 ?  10  LEU   A N    1 
ATOM   117  C CA   . LEU   A 1 10  ? 8.265  -12.491 11.836  1.00 11.87 ?  10  LEU   A CA   1 
ATOM   118  C C    . LEU   A 1 10  ? 9.378  -13.429 11.376  1.00 11.10 ?  10  LEU   A C    1 
ATOM   119  O O    . LEU   A 1 10  ? 10.333 -13.006 10.717  1.00 11.77 ?  10  LEU   A O    1 
ATOM   120  C CB   . LEU   A 1 10  ? 7.348  -12.156 10.657  1.00 13.24 ?  10  LEU   A CB   1 
ATOM   121  C CG   . LEU   A 1 10  ? 6.627  -13.324 9.973   1.00 16.35 ?  10  LEU   A CG   1 
ATOM   122  C CD1  . LEU   A 1 10  ? 5.276  -13.549 10.590  1.00 20.29 ?  10  LEU   A CD1  1 
ATOM   123  C CD2  . LEU   A 1 10  ? 6.487  -13.055 8.486   1.00 19.81 ?  10  LEU   A CD2  1 
ATOM   124  H H    . LEU   A 1 10  ? 8.954  -10.646 11.736  1.00 14.23 ?  10  LEU   A H    1 
ATOM   125  H HA   . LEU   A 1 10  ? 7.746  -12.912 12.544  1.00 14.25 ?  10  LEU   A HA   1 
ATOM   126  H HB2  . LEU   A 1 10  ? 6.665  -11.542 10.970  1.00 15.89 ?  10  LEU   A HB2  1 
ATOM   127  H HB3  . LEU   A 1 10  ? 7.885  -11.716 9.980   1.00 15.89 ?  10  LEU   A HB3  1 
ATOM   128  H HG   . LEU   A 1 10  ? 7.146  -14.135 10.092  1.00 19.63 ?  10  LEU   A HG   1 
ATOM   129  H HD11 . LEU   A 1 10  ? 4.992  -14.453 10.408  1.00 24.36 ?  10  LEU   A HD11 1 
ATOM   130  H HD12 . LEU   A 1 10  ? 5.335  -13.389 11.541  1.00 24.36 ?  10  LEU   A HD12 1 
ATOM   131  H HD13 . LEU   A 1 10  ? 4.649  -12.916 10.191  1.00 24.36 ?  10  LEU   A HD13 1 
ATOM   132  H HD21 . LEU   A 1 10  ? 6.005  -13.788 8.082   1.00 23.78 ?  10  LEU   A HD21 1 
ATOM   133  H HD22 . LEU   A 1 10  ? 6.010  -12.224 8.362   1.00 23.78 ?  10  LEU   A HD22 1 
ATOM   134  H HD23 . LEU   A 1 10  ? 7.378  -12.989 8.099   1.00 23.78 ?  10  LEU   A HD23 1 
ATOM   135  N N    . LYS   A 1 11  ? 9.266  -14.702 11.738  1.00 10.93 ?  11  LYS   A N    1 
ATOM   136  C CA   . LYS   A 1 11  ? 10.262 -15.704 11.372  1.00 10.92 ?  11  LYS   A CA   1 
ATOM   137  C C    . LYS   A 1 11  ? 9.905  -16.273 10.006  1.00 11.17 ?  11  LYS   A C    1 
ATOM   138  O O    . LYS   A 1 11  ? 8.825  -16.841 9.844   1.00 13.10 ?  11  LYS   A O    1 
ATOM   139  C CB   . LYS   A 1 11  ? 10.282 -16.807 12.430  1.00 11.13 ?  11  LYS   A CB   1 
ATOM   140  C CG   . LYS   A 1 11  ? 11.316 -17.901 12.224  1.00 11.15 ?  11  LYS   A CG   1 
ATOM   141  C CD   . LYS   A 1 11  ? 11.385 -18.788 13.470  1.00 11.85 ?  11  LYS   A CD   1 
ATOM   142  C CE   . LYS   A 1 11  ? 12.380 -19.932 13.345  1.00 11.87 ?  11  LYS   A CE   1 
ATOM   143  N NZ   . LYS   A 1 11  ? 13.764 -19.470 13.073  1.00 11.80 ?  11  LYS   A NZ   1 
ATOM   144  H H    . LYS   A 1 11  ? 8.601  -15.019 12.189  1.00 13.13 ?  11  LYS   A H    1 
ATOM   145  H HA   . LYS   A 1 11  ? 11.135 -15.292 11.321  1.00 13.11 ?  11  LYS   A HA   1 
ATOM   146  H HB2  . LYS   A 1 11  ? 10.458 -16.396 13.289  1.00 13.36 ?  11  LYS   A HB2  1 
ATOM   147  H HB3  . LYS   A 1 11  ? 9.408  -17.229 12.447  1.00 13.36 ?  11  LYS   A HB3  1 
ATOM   148  H HG2  . LYS   A 1 11  ? 11.059 -18.451 11.465  1.00 13.39 ?  11  LYS   A HG2  1 
ATOM   149  H HG3  . LYS   A 1 11  ? 12.186 -17.503 12.079  1.00 13.39 ?  11  LYS   A HG3  1 
ATOM   150  H HD2  . LYS   A 1 11  ? 11.640 -18.241 14.228  1.00 14.23 ?  11  LYS   A HD2  1 
ATOM   151  H HD3  . LYS   A 1 11  ? 10.502 -19.171 13.626  1.00 14.23 ?  11  LYS   A HD3  1 
ATOM   152  H HE2  . LYS   A 1 11  ? 12.391 -20.430 14.179  1.00 14.26 ?  11  LYS   A HE2  1 
ATOM   153  H HE3  . LYS   A 1 11  ? 12.106 -20.512 12.619  1.00 14.26 ?  11  LYS   A HE3  1 
ATOM   154  H HZ1  . LYS   A 1 11  ? 14.309 -20.169 12.997  1.00 14.17 ?  11  LYS   A HZ1  1 
ATOM   155  H HZ2  . LYS   A 1 11  ? 13.784 -19.006 12.310  1.00 14.17 ?  11  LYS   A HZ2  1 
ATOM   156  H HZ3  . LYS   A 1 11  ? 14.049 -18.948 13.733  1.00 14.17 ?  11  LYS   A HZ3  1 
ATOM   157  N N    . LEU   A 1 12  ? 10.791 -16.116 9.020   1.00 10.39 ?  12  LEU   A N    1 
ATOM   158  C CA   . LEU   A 1 12  ? 10.524 -16.688 7.703   1.00 10.75 ?  12  LEU   A CA   1 
ATOM   159  C C    . LEU   A 1 12  ? 11.094 -18.090 7.550   1.00 10.53 ?  12  LEU   A C    1 
ATOM   160  O O    . LEU   A 1 12  ? 10.455 -18.952 6.940   1.00 11.12 ?  12  LEU   A O    1 
ATOM   161  C CB   . LEU   A 1 12  ? 11.082 -15.791 6.593   1.00 11.69 ?  12  LEU   A CB   1 
ATOM   162  C CG   . LEU   A 1 12  ? 10.439 -14.412 6.445   1.00 12.48 ?  12  LEU   A CG   1 
ATOM   163  C CD1  . LEU   A 1 12  ? 11.162 -13.604 5.388   1.00 13.31 ?  12  LEU   A CD1  1 
ATOM   164  C CD2  . LEU   A 1 12  ? 8.968  -14.548 6.089   1.00 13.35 ?  12  LEU   A CD2  1 
ATOM   165  H H    . LEU   A 1 12  ? 11.543 -15.688 9.083   1.00 12.47 ?  12  LEU   A H    1 
ATOM   166  H HA   . LEU   A 1 12  ? 9.563  -16.748 7.580   1.00 12.91 ?  12  LEU   A HA   1 
ATOM   167  H HB2  . LEU   A 1 12  ? 12.023 -15.652 6.757   1.00 14.04 ?  12  LEU   A HB2  1 
ATOM   168  H HB3  . LEU   A 1 12  ? 10.965 -16.253 5.746   1.00 14.04 ?  12  LEU   A HB3  1 
ATOM   169  H HG   . LEU   A 1 12  ? 10.502 -13.934 7.283   1.00 14.99 ?  12  LEU   A HG   1 
ATOM   170  H HD11 . LEU   A 1 12  ? 10.741 -12.732 5.309   1.00 15.98 ?  12  LEU   A HD11 1 
ATOM   171  H HD12 . LEU   A 1 12  ? 12.089 -13.499 5.651   1.00 15.98 ?  12  LEU   A HD12 1 
ATOM   172  H HD13 . LEU   A 1 12  ? 11.110 -14.071 4.539   1.00 15.98 ?  12  LEU   A HD13 1 
ATOM   173  H HD21 . LEU   A 1 12  ? 8.614  -13.677 5.849   1.00 16.03 ?  12  LEU   A HD21 1 
ATOM   174  H HD22 . LEU   A 1 12  ? 8.877  -15.159 5.340   1.00 16.03 ?  12  LEU   A HD22 1 
ATOM   175  H HD23 . LEU   A 1 12  ? 8.488  -14.898 6.858   1.00 16.03 ?  12  LEU   A HD23 1 
ATOM   176  N N    . THR   A 1 13  ? 12.308 -18.309 8.054   1.00 10.67 ?  13  THR   A N    1 
ATOM   177  C CA   . THR   A 1 13  ? 12.999 -19.591 7.947   1.00 11.09 ?  13  THR   A CA   1 
ATOM   178  C C    . THR   A 1 13  ? 13.779 -19.826 9.236   1.00 10.81 ?  13  THR   A C    1 
ATOM   179  O O    . THR   A 1 13  ? 13.704 -19.046 10.191  1.00 11.07 ?  13  THR   A O    1 
ATOM   180  C CB   . THR   A 1 13  ? 13.964 -19.619 6.754   1.00 11.57 ?  13  THR   A CB   1 
ATOM   181  O OG1  . THR   A 1 13  ? 15.031 -18.709 7.016   1.00 11.55 ?  13  THR   A OG1  1 
ATOM   182  C CG2  . THR   A 1 13  ? 13.275 -19.228 5.455   1.00 12.83 ?  13  THR   A CG2  1 
ATOM   183  H H    . THR   A 1 13  ? 12.767 -17.713 8.467   1.00 12.81 ?  13  THR   A H    1 
ATOM   184  H HA   . THR   A 1 13  ? 12.351 -20.306 7.840   1.00 13.32 ?  13  THR   A HA   1 
ATOM   185  H HB   . THR   A 1 13  ? 14.323 -20.513 6.649   1.00 13.89 ?  13  THR   A HB   1 
ATOM   186  H HG1  . THR   A 1 13  ? 15.702 -19.123 7.294   1.00 13.87 ?  13  THR   A HG1  1 
ATOM   187  H HG21 . THR   A 1 13  ? 13.879 -19.367 4.707   1.00 15.40 ?  13  THR   A HG21 1 
ATOM   188  H HG22 . THR   A 1 13  ? 12.484 -19.774 5.323   1.00 15.40 ?  13  THR   A HG22 1 
ATOM   189  H HG23 . THR   A 1 13  ? 13.015 -18.296 5.483   1.00 15.40 ?  13  THR   A HG23 1 
ATOM   190  N N    . ASP   A 1 14  ? 14.575 -20.894 9.239   1.00 11.29 ?  14  ASP   A N    1 
ATOM   191  C CA   . ASP   A 1 14  ? 15.432 -21.177 10.382  1.00 11.34 ?  14  ASP   A CA   1 
ATOM   192  C C    . ASP   A 1 14  ? 16.270 -19.963 10.774  1.00 11.05 ?  14  ASP   A C    1 
ATOM   193  O O    . ASP   A 1 14  ? 16.502 -19.728 11.965  1.00 12.60 ?  14  ASP   A O    1 
ATOM   194  C CB   . ASP   A 1 14  ? 16.345 -22.354 10.060  1.00 13.60 ?  14  ASP   A CB   1 
ATOM   195  C CG   . ASP   A 1 14  ? 17.243 -22.704 11.212  1.00 17.52 ?  14  ASP   A CG   1 
ATOM   196  O OD1  . ASP   A 1 14  ? 16.715 -23.155 12.253  1.00 18.69 ?  14  ASP   A OD1  1 
ATOM   197  O OD2  . ASP   A 1 14  ? 18.468 -22.524 11.075  1.00 20.58 -1 14  ASP   A OD2  1 
ATOM   198  H H    . ASP   A 1 14  ? 14.635 -21.456 8.593   1.00 13.55 ?  14  ASP   A H    1 
ATOM   199  H HA   . ASP   A 1 14  ? 14.876 -21.420 11.139  1.00 13.61 ?  14  ASP   A HA   1 
ATOM   200  H HB2  . ASP   A 1 14  ? 15.789 -23.130 9.845   1.00 16.33 ?  14  ASP   A HB2  1 
ATOM   201  H HB3  . ASP   A 1 14  ? 16.898 -22.129 9.300   1.00 16.33 ?  14  ASP   A HB3  1 
ATOM   202  N N    . ASN   A 1 15  ? 16.741 -19.181 9.788   1.00 10.68 ?  15  ASN   A N    1 
ATOM   203  C CA   . ASN   A 1 15  ? 17.734 -18.145 10.051  1.00 10.79 ?  15  ASN   A CA   1 
ATOM   204  C C    . ASN   A 1 15  ? 17.365 -16.743 9.582   1.00 11.15 ?  15  ASN   A C    1 
ATOM   205  O O    . ASN   A 1 15  ? 18.130 -15.811 9.853   1.00 12.77 ?  15  ASN   A O    1 
ATOM   206  C CB   . ASN   A 1 15  ? 19.100 -18.539 9.456   1.00 10.93 ?  15  ASN   A CB   1 
ATOM   207  C CG   . ASN   A 1 15  ? 19.076 -18.628 7.946   1.00 10.97 ?  15  ASN   A CG   1 
ATOM   208  O OD1  . ASN   A 1 15  ? 18.335 -19.429 7.373   1.00 12.03 ?  15  ASN   A OD1  1 
ATOM   209  N ND2  . ASN   A 1 15  ? 19.882 -17.799 7.287   1.00 11.26 ?  15  ASN   A ND2  1 
ATOM   210  H H    . ASN   A 1 15  ? 16.496 -19.240 8.968   1.00 12.83 ?  15  ASN   A H    1 
ATOM   211  H HA   . ASN   A 1 15  ? 17.858 -18.092 11.009  1.00 12.96 ?  15  ASN   A HA   1 
ATOM   212  H HB2  . ASN   A 1 15  ? 19.760 -17.871 9.710   1.00 13.13 ?  15  ASN   A HB2  1 
ATOM   213  H HB3  . ASN   A 1 15  ? 19.362 -19.407 9.799   1.00 13.13 ?  15  ASN   A HB3  1 
ATOM   214  H HD21 . ASN   A 1 15  ? 19.901 -17.809 6.424   1.00 13.52 ?  15  ASN   A HD21 1 
ATOM   215  H HD22 . ASN   A 1 15  ? 20.390 -17.248 7.715   1.00 13.52 ?  15  ASN   A HD22 1 
ATOM   216  N N    . VAL   A 1 16  ? 16.230 -16.558 8.907   1.00 10.66 ?  16  VAL   A N    1 
ATOM   217  C CA   . VAL   A 1 16  ? 15.845 -15.270 8.342   1.00 10.58 ?  16  VAL   A CA   1 
ATOM   218  C C    . VAL   A 1 16  ? 14.571 -14.771 9.018   1.00 10.23 ?  16  VAL   A C    1 
ATOM   219  O O    . VAL   A 1 16  ? 13.563 -15.492 9.094   1.00 10.27 ?  16  VAL   A O    1 
ATOM   220  C CB   . VAL   A 1 16  ? 15.670 -15.330 6.814   1.00 11.60 ?  16  VAL   A CB   1 
ATOM   221  C CG1  . VAL   A 1 16  ? 15.245 -13.965 6.267   1.00 12.11 ?  16  VAL   A CG1  1 
ATOM   222  C CG2  . VAL   A 1 16  ? 16.946 -15.799 6.134   1.00 12.56 ?  16  VAL   A CG2  1 
ATOM   223  H H    . VAL   A 1 16  ? 15.648 -17.179 8.771   1.00 12.80 ?  16  VAL   A H    1 
ATOM   224  H HA   . VAL   A 1 16  ? 16.552 -14.629 8.527   1.00 12.70 ?  16  VAL   A HA   1 
ATOM   225  H HB   . VAL   A 1 16  ? 14.973 -15.966 6.601   1.00 13.93 ?  16  VAL   A HB   1 
ATOM   226  H HG11 . VAL   A 1 16  ? 15.339 -13.971 5.301   1.00 14.54 ?  16  VAL   A HG11 1 
ATOM   227  H HG12 . VAL   A 1 16  ? 14.318 -13.805 6.505   1.00 14.54 ?  16  VAL   A HG12 1 
ATOM   228  H HG13 . VAL   A 1 16  ? 15.812 -13.281 6.650   1.00 14.54 ?  16  VAL   A HG13 1 
ATOM   229  H HG21 . VAL   A 1 16  ? 16.821 -15.773 5.171   1.00 15.08 ?  16  VAL   A HG21 1 
ATOM   230  H HG22 . VAL   A 1 16  ? 17.675 -15.208 6.384   1.00 15.08 ?  16  VAL   A HG22 1 
ATOM   231  H HG23 . VAL   A 1 16  ? 17.142 -16.703 6.418   1.00 15.08 ?  16  VAL   A HG23 1 
ATOM   232  N N    A TYR   A 1 17  ? 14.620 -13.517 9.462   0.86 10.24 ?  17  TYR   A N    1 
ATOM   233  N N    B TYR   A 1 17  ? 14.623 -13.520 9.485   0.14 10.22 ?  17  TYR   A N    1 
ATOM   234  C CA   A TYR   A 1 17  ? 13.553 -12.835 10.175  0.86 10.19 ?  17  TYR   A CA   1 
ATOM   235  C CA   B TYR   A 1 17  ? 13.525 -12.843 10.159  0.14 10.29 ?  17  TYR   A CA   1 
ATOM   236  C C    A TYR   A 1 17  ? 13.282 -11.507 9.480   0.86 10.54 ?  17  TYR   A C    1 
ATOM   237  C C    B TYR   A 1 17  ? 13.278 -11.509 9.466   0.14 10.52 ?  17  TYR   A C    1 
ATOM   238  O O    A TYR   A 1 17  ? 14.181 -10.937 8.864   0.86 10.89 ?  17  TYR   A O    1 
ATOM   239  O O    B TYR   A 1 17  ? 14.177 -10.946 8.838   0.14 10.55 ?  17  TYR   A O    1 
ATOM   240  C CB   A TYR   A 1 17  ? 13.999 -12.583 11.619  0.86 10.74 ?  17  TYR   A CB   1 
ATOM   241  C CB   B TYR   A 1 17  ? 13.872 -12.589 11.631  0.14 10.29 ?  17  TYR   A CB   1 
ATOM   242  C CG   A TYR   A 1 17  ? 14.199 -13.858 12.417  0.86 11.17 ?  17  TYR   A CG   1 
ATOM   243  C CG   B TYR   A 1 17  ? 13.999 -13.847 12.457  0.14 10.25 ?  17  TYR   A CG   1 
ATOM   244  C CD1  A TYR   A 1 17  ? 15.363 -14.611 12.307  0.86 11.89 ?  17  TYR   A CD1  1 
ATOM   245  C CD1  B TYR   A 1 17  ? 15.148 -14.629 12.403  0.14 10.18 ?  17  TYR   A CD1  1 
ATOM   246  C CD2  A TYR   A 1 17  ? 13.210 -14.315 13.274  0.86 11.38 ?  17  TYR   A CD2  1 
ATOM   247  C CD2  B TYR   A 1 17  ? 12.970 -14.251 13.293  0.14 10.19 ?  17  TYR   A CD2  1 
ATOM   248  C CE1  A TYR   A 1 17  ? 15.529 -15.793 13.030  0.86 12.33 ?  17  TYR   A CE1  1 
ATOM   249  C CE1  B TYR   A 1 17  ? 15.261 -15.785 13.159  0.14 10.00 ?  17  TYR   A CE1  1 
ATOM   250  C CE2  A TYR   A 1 17  ? 13.369 -15.494 14.003  0.86 12.03 ?  17  TYR   A CE2  1 
ATOM   251  C CE2  B TYR   A 1 17  ? 13.073 -15.402 14.050  0.14 10.09 ?  17  TYR   A CE2  1 
ATOM   252  C CZ   A TYR   A 1 17  ? 14.531 -16.228 13.879  0.86 12.15 ?  17  TYR   A CZ   1 
ATOM   253  C CZ   B TYR   A 1 17  ? 14.219 -16.165 13.982  0.14 9.92  ?  17  TYR   A CZ   1 
ATOM   254  O OH   A TYR   A 1 17  ? 14.695 -17.390 14.604  0.86 12.92 ?  17  TYR   A OH   1 
ATOM   255  O OH   B TYR   A 1 17  ? 14.312 -17.310 14.742  0.14 9.88  ?  17  TYR   A OH   1 
ATOM   256  H H    A TYR   A 1 17  ? 15.307 -13.007 9.336   0.86 12.30 ?  17  TYR   A H    1 
ATOM   257  H H    B TYR   A 1 17  ? 15.322 -13.018 9.410   0.14 12.27 ?  17  TYR   A H    1 
ATOM   258  H HA   A TYR   A 1 17  ? 12.746 -13.375 10.165  0.86 12.24 ?  17  TYR   A HA   1 
ATOM   259  H HA   B TYR   A 1 17  ? 12.718 -13.380 10.108  0.14 12.35 ?  17  TYR   A HA   1 
ATOM   260  H HB2  A TYR   A 1 17  ? 14.841 -12.110 11.610  0.86 12.90 ?  17  TYR   A HB2  1 
ATOM   261  H HB2  B TYR   A 1 17  ? 14.718 -12.119 11.678  0.14 12.36 ?  17  TYR   A HB2  1 
ATOM   262  H HB3  A TYR   A 1 17  ? 13.323 -12.058 12.067  0.86 12.90 ?  17  TYR   A HB3  1 
ATOM   263  H HB3  B TYR   A 1 17  ? 13.174 -12.050 12.026  0.14 12.36 ?  17  TYR   A HB3  1 
ATOM   264  H HD1  A TYR   A 1 17  ? 16.038 -14.335 11.732  0.86 14.28 ?  17  TYR   A HD1  1 
ATOM   265  H HD1  B TYR   A 1 17  ? 15.849 -14.374 11.847  0.14 12.23 ?  17  TYR   A HD1  1 
ATOM   266  H HD2  A TYR   A 1 17  ? 12.418 -13.837 13.363  0.86 13.67 ?  17  TYR   A HD2  1 
ATOM   267  H HD2  B TYR   A 1 17  ? 12.194 -13.741 13.343  0.14 12.24 ?  17  TYR   A HD2  1 
ATOM   268  H HE1  A TYR   A 1 17  ? 16.314 -16.290 12.946  0.86 14.81 ?  17  TYR   A HE1  1 
ATOM   269  H HE1  B TYR   A 1 17  ? 16.035 -16.301 13.112  0.14 12.01 ?  17  TYR   A HE1  1 
ATOM   270  H HE2  A TYR   A 1 17  ? 12.692 -15.789 14.576  0.86 14.45 ?  17  TYR   A HE2  1 
ATOM   271  H HE2  B TYR   A 1 17  ? 12.374 -15.660 14.606  0.14 12.12 ?  17  TYR   A HE2  1 
ATOM   272  H HH   A TYR   A 1 17  ? 15.450 -17.726 14.450  0.86 15.52 ?  17  TYR   A HH   1 
ATOM   273  H HH   B TYR   A 1 17  ? 13.552 -17.523 15.029  0.14 11.86 ?  17  TYR   A HH   1 
ATOM   274  N N    . ILE   A 1 18  ? 12.051 -10.994 9.584   1.00 10.81 ?  18  ILE   A N    1 
ATOM   275  C CA   . ILE   A 1 18  ? 11.667 -9.772  8.878   1.00 11.01 ?  18  ILE   A CA   1 
ATOM   276  C C    . ILE   A 1 18  ? 10.718 -8.917  9.710   1.00 11.61 ?  18  ILE   A C    1 
ATOM   277  O O    . ILE   A 1 18  ? 9.881  -9.432  10.460  1.00 11.89 ?  18  ILE   A O    1 
ATOM   278  C CB   . ILE   A 1 18  ? 11.075 -10.131 7.496   1.00 11.50 ?  18  ILE   A CB   1 
ATOM   279  C CG1  . ILE   A 1 18  ? 11.020 -8.917  6.570   1.00 12.61 ?  18  ILE   A CG1  1 
ATOM   280  C CG2  . ILE   A 1 18  ? 9.717  -10.823 7.645   1.00 12.43 ?  18  ILE   A CG2  1 
ATOM   281  C CD1  . ILE   A 1 18  ? 10.738 -9.286  5.138   1.00 14.67 ?  18  ILE   A CD1  1 
ATOM   282  H H    A ILE   A 1 18  ? 11.420 -11.344 10.056  0.86 12.98 ?  18  ILE   A H    1 
ATOM   283  H H    B ILE   A 1 18  ? 11.417 -11.349 10.048  0.14 12.98 ?  18  ILE   A H    1 
ATOM   284  H HA   . ILE   A 1 18  ? 12.471 -9.244  8.724   1.00 13.22 ?  18  ILE   A HA   1 
ATOM   285  H HB   . ILE   A 1 18  ? 11.677 -10.768 7.088   1.00 13.81 ?  18  ILE   A HB   1 
ATOM   286  H HG12 . ILE   A 1 18  ? 10.325 -8.319  6.865   1.00 15.14 ?  18  ILE   A HG12 1 
ATOM   287  H HG13 . ILE   A 1 18  ? 11.882 -8.466  6.589   1.00 15.14 ?  18  ILE   A HG13 1 
ATOM   288  H HG21 . ILE   A 1 18  ? 9.452  -11.184 6.783   1.00 14.92 ?  18  ILE   A HG21 1 
ATOM   289  H HG22 . ILE   A 1 18  ? 9.798  -11.538 8.292   1.00 14.92 ?  18  ILE   A HG22 1 
ATOM   290  H HG23 . ILE   A 1 18  ? 9.059  -10.175 7.946   1.00 14.92 ?  18  ILE   A HG23 1 
ATOM   291  H HD11 . ILE   A 1 18  ? 10.783 -8.484  4.590   1.00 17.61 ?  18  ILE   A HD11 1 
ATOM   292  H HD12 . ILE   A 1 18  ? 11.400 -9.928  4.836   1.00 17.61 ?  18  ILE   A HD12 1 
ATOM   293  H HD13 . ILE   A 1 18  ? 9.851  -9.673  5.081   1.00 17.61 ?  18  ILE   A HD13 1 
ATOM   294  N N    A LYS   A 1 19  ? 10.840 -7.595  9.553   0.86 12.12 ?  19  LYS   A N    1 
ATOM   295  N N    B LYS   A 1 19  ? 10.836 -7.597  9.557   0.14 12.14 ?  19  LYS   A N    1 
ATOM   296  C CA   A LYS   A 1 19  ? 10.030 -6.639  10.303  0.86 13.61 ?  19  LYS   A CA   1 
ATOM   297  C CA   B LYS   A 1 19  ? 10.033 -6.671  10.344  0.14 12.91 ?  19  LYS   A CA   1 
ATOM   298  C C    A LYS   A 1 19  ? 9.806  -5.390  9.456   0.86 13.74 ?  19  LYS   A C    1 
ATOM   299  C C    B LYS   A 1 19  ? 9.922  -5.343  9.608   0.14 12.98 ?  19  LYS   A C    1 
ATOM   300  O O    A LYS   A 1 19  ? 10.682 -4.985  8.688   0.86 13.55 ?  19  LYS   A O    1 
ATOM   301  O O    B LYS   A 1 19  ? 10.889 -4.886  8.994   0.14 12.77 ?  19  LYS   A O    1 
ATOM   302  C CB   A LYS   A 1 19  ? 10.759 -6.256  11.599  0.86 14.59 ?  19  LYS   A CB   1 
ATOM   303  C CB   B LYS   A 1 19  ? 10.668 -6.449  11.722  0.14 13.54 ?  19  LYS   A CB   1 
ATOM   304  C CG   A LYS   A 1 19  ? 10.012 -5.380  12.593  0.86 16.46 ?  19  LYS   A CG   1 
ATOM   305  C CG   B LYS   A 1 19  ? 9.988  -5.402  12.587  0.14 14.30 ?  19  LYS   A CG   1 
ATOM   306  C CD   A LYS   A 1 19  ? 10.946 -5.064  13.763  0.86 17.90 ?  19  LYS   A CD   1 
ATOM   307  C CD   B LYS   A 1 19  ? 10.813 -5.128  13.832  0.14 14.96 ?  19  LYS   A CD   1 
ATOM   308  C CE   A LYS   A 1 19  ? 10.315 -4.173  14.819  0.86 18.83 ?  19  LYS   A CE   1 
ATOM   309  C CE   B LYS   A 1 19  ? 10.140 -4.117  14.742  0.14 15.33 ?  19  LYS   A CE   1 
ATOM   310  N NZ   A LYS   A 1 19  ? 11.256 -3.968  15.963  0.86 19.12 ?  19  LYS   A NZ   1 
ATOM   311  N NZ   B LYS   A 1 19  ? 10.964 -3.845  15.952  0.14 15.46 ?  19  LYS   A NZ   1 
ATOM   312  H H    A LYS   A 1 19  ? 11.399 -7.222  9.013   0.86 14.55 ?  19  LYS   A H    1 
ATOM   313  H H    B LYS   A 1 19  ? 11.375 -7.211  9.004   0.14 14.58 ?  19  LYS   A H    1 
ATOM   314  H HA   A LYS   A 1 19  ? 9.170  -7.041  10.527  0.86 16.34 ?  19  LYS   A HA   1 
ATOM   315  H HA   B LYS   A 1 19  ? 9.142  -7.031  10.466  0.14 15.50 ?  19  LYS   A HA   1 
ATOM   316  H HB2  A LYS   A 1 19  ? 10.994 -7.073  12.062  0.86 17.51 ?  19  LYS   A HB2  1 
ATOM   317  H HB2  B LYS   A 1 19  ? 10.645 -7.288  12.209  0.14 16.26 ?  19  LYS   A HB2  1 
ATOM   318  H HB3  A LYS   A 1 19  ? 11.569 -5.783  11.352  0.86 17.51 ?  19  LYS   A HB3  1 
ATOM   319  H HB3  B LYS   A 1 19  ? 11.587 -6.170  11.597  0.14 16.26 ?  19  LYS   A HB3  1 
ATOM   320  H HG2  A LYS   A 1 19  ? 9.750  -4.549  12.169  0.86 19.76 ?  19  LYS   A HG2  1 
ATOM   321  H HG2  B LYS   A 1 19  ? 9.902  -4.570  12.096  0.14 17.17 ?  19  LYS   A HG2  1 
ATOM   322  H HG3  A LYS   A 1 19  ? 9.236  -5.855  12.931  0.86 19.76 ?  19  LYS   A HG3  1 
ATOM   323  H HG3  B LYS   A 1 19  ? 9.116  -5.726  12.861  0.14 17.17 ?  19  LYS   A HG3  1 
ATOM   324  H HD2  A LYS   A 1 19  ? 11.202 -5.896  14.192  0.86 21.49 ?  19  LYS   A HD2  1 
ATOM   325  H HD2  B LYS   A 1 19  ? 10.927 -5.954  14.327  0.14 17.96 ?  19  LYS   A HD2  1 
ATOM   326  H HD3  A LYS   A 1 19  ? 11.732 -4.612  13.423  0.86 21.49 ?  19  LYS   A HD3  1 
ATOM   327  H HD3  B LYS   A 1 19  ? 11.677 -4.773  13.570  0.14 17.96 ?  19  LYS   A HD3  1 
ATOM   328  H HE2  A LYS   A 1 19  ? 10.110 -3.307  14.432  0.86 22.60 ?  19  LYS   A HE2  1 
ATOM   329  H HE2  B LYS   A 1 19  ? 10.019 -3.283  14.262  0.14 18.41 ?  19  LYS   A HE2  1 
ATOM   330  H HE3  A LYS   A 1 19  ? 9.507  -4.591  15.158  0.86 22.60 ?  19  LYS   A HE3  1 
ATOM   331  H HE3  B LYS   A 1 19  ? 9.282  -4.466  15.030  0.14 18.41 ?  19  LYS   A HE3  1 
ATOM   332  H HZ1  A LYS   A 1 19  ? 10.859 -3.493  16.603  0.86 22.95 ?  19  LYS   A HZ1  1 
ATOM   333  H HZ1  B LYS   A 1 19  ? 10.552 -3.255  16.475  0.14 18.56 ?  19  LYS   A HZ1  1 
ATOM   334  H HZ2  A LYS   A 1 19  ? 11.502 -4.755  16.299  0.86 22.95 ?  19  LYS   A HZ2  1 
ATOM   335  H HZ2  B LYS   A 1 19  ? 11.091 -4.598  16.409  0.14 18.56 ?  19  LYS   A HZ2  1 
ATOM   336  H HZ3  A LYS   A 1 19  ? 11.980 -3.532  15.688  0.86 22.95 ?  19  LYS   A HZ3  1 
ATOM   337  H HZ3  B LYS   A 1 19  ? 11.756 -3.516  15.713  0.14 18.56 ?  19  LYS   A HZ3  1 
ATOM   338  N N    A ASN   A 1 20  ? 8.626  -4.780  9.596   0.86 14.83 ?  20  ASN   A N    1 
ATOM   339  N N    B ASN   A 1 20  ? 8.740  -4.728  9.679   0.14 13.37 ?  20  ASN   A N    1 
ATOM   340  C CA   A ASN   A 1 20  ? 8.385  -3.453  9.035   0.86 16.15 ?  20  ASN   A CA   1 
ATOM   341  C CA   B ASN   A 1 20  ? 8.542  -3.377  9.163   0.14 13.78 ?  20  ASN   A CA   1 
ATOM   342  C C    A ASN   A 1 20  ? 9.020  -2.450  9.986   0.86 16.49 ?  20  ASN   A C    1 
ATOM   343  C C    B ASN   A 1 20  ? 9.092  -2.394  10.187  0.14 14.05 ?  20  ASN   A C    1 
ATOM   344  O O    A ASN   A 1 20  ? 8.513  -2.227  11.090  0.86 18.00 ?  20  ASN   A O    1 
ATOM   345  O O    B ASN   A 1 20  ? 8.523  -2.234  11.272  0.14 14.38 ?  20  ASN   A O    1 
ATOM   346  C CB   A ASN   A 1 20  ? 6.884  -3.208  8.880   0.86 17.74 ?  20  ASN   A CB   1 
ATOM   347  C CB   B ASN   A 1 20  ? 7.061  -3.115  8.901   0.14 13.96 ?  20  ASN   A CB   1 
ATOM   348  C CG   A ASN   A 1 20  ? 6.544  -1.779  8.450   0.86 19.24 ?  20  ASN   A CG   1 
ATOM   349  C CG   B ASN   A 1 20  ? 6.745  -1.635  8.765   0.14 14.11 ?  20  ASN   A CG   1 
ATOM   350  O OD1  A ASN   A 1 20  ? 5.580  -1.189  8.944   0.86 20.89 ?  20  ASN   A OD1  1 
ATOM   351  O OD1  B ASN   A 1 20  ? 5.899  -1.102  9.483   0.14 14.38 ?  20  ASN   A OD1  1 
ATOM   352  N ND2  A ASN   A 1 20  ? 7.324  -1.228  7.527   0.86 19.99 ?  20  ASN   A ND2  1 
ATOM   353  N ND2  B ASN   A 1 20  ? 7.434  -0.961  7.850   0.14 14.04 ?  20  ASN   A ND2  1 
ATOM   354  H H    A ASN   A 1 20  ? 7.950  -5.114  10.015  0.86 17.80 ?  20  ASN   A H    1 
ATOM   355  H H    B ASN   A 1 20  ? 8.032  -5.074  10.025  0.14 16.06 ?  20  ASN   A H    1 
ATOM   356  H HA   A ASN   A 1 20  ? 8.811  -3.383  8.169   0.86 19.39 ?  20  ASN   A HA   1 
ATOM   357  H HA   B ASN   A 1 20  ? 9.025  -3.267  8.332   0.14 16.54 ?  20  ASN   A HA   1 
ATOM   358  H HB2  A ASN   A 1 20  ? 6.538  -3.809  8.207   0.86 21.30 ?  20  ASN   A HB2  1 
ATOM   359  H HB2  B ASN   A 1 20  ? 6.802  -3.553  8.073   0.14 16.77 ?  20  ASN   A HB2  1 
ATOM   360  H HB3  A ASN   A 1 20  ? 6.452  -3.377  9.733   0.86 21.30 ?  20  ASN   A HB3  1 
ATOM   361  H HB3  B ASN   A 1 20  ? 6.537  -3.467  9.638   0.14 16.77 ?  20  ASN   A HB3  1 
ATOM   362  H HD21 A ASN   A 1 20  ? 7.171  -0.427  7.261   0.86 23.99 ?  20  ASN   A HD21 1 
ATOM   363  H HD21 B ASN   A 1 20  ? 7.290  -0.121  7.734   0.14 16.86 ?  20  ASN   A HD21 1 
ATOM   364  H HD22 A ASN   A 1 20  ? 7.985  -1.672  7.199   0.86 23.99 ?  20  ASN   A HD22 1 
ATOM   365  H HD22 B ASN   A 1 20  ? 8.023  -1.366  7.373   0.14 16.86 ?  20  ASN   A HD22 1 
ATOM   366  N N    A ALA   A 1 21  ? 10.152 -1.873  9.585   0.86 16.38 ?  21  ALA   A N    1 
ATOM   367  N N    B ALA   A 1 21  ? 10.201 -1.739  9.855   0.14 14.25 ?  21  ALA   A N    1 
ATOM   368  C CA   A ALA   A 1 21  ? 10.867 -0.979  10.483  0.86 16.26 ?  21  ALA   A CA   1 
ATOM   369  C CA   B ALA   A 1 21  ? 10.817 -0.817  10.797  0.14 14.54 ?  21  ALA   A CA   1 
ATOM   370  C C    A ALA   A 1 21  ? 11.823 -0.104  9.691   0.86 15.46 ?  21  ALA   A C    1 
ATOM   371  C C    B ALA   A 1 21  ? 11.839 0.049   10.077  0.14 14.54 ?  21  ALA   A C    1 
ATOM   372  O O    A ALA   A 1 21  ? 12.257 -0.463  8.593   0.86 15.83 ?  21  ALA   A O    1 
ATOM   373  O O    B ALA   A 1 21  ? 12.342 -0.305  9.007   0.14 14.62 ?  21  ALA   A O    1 
ATOM   374  C CB   A ALA   A 1 21  ? 11.640 -1.764  11.547  0.86 17.66 ?  21  ALA   A CB   1 
ATOM   375  C CB   B ALA   A 1 21  ? 11.480 -1.565  11.955  0.14 14.89 ?  21  ALA   A CB   1 
ATOM   376  H H    A ALA   A 1 21  ? 10.518 -1.981  8.812   0.86 19.67 ?  21  ALA   A H    1 
ATOM   377  H H    B ALA   A 1 21  ? 10.609 -1.815  9.102   0.14 17.11 ?  21  ALA   A H    1 
ATOM   378  H HA   A ALA   A 1 21  ? 10.224 -0.406  10.933  0.86 19.52 ?  21  ALA   A HA   1 
ATOM   379  H HA   B ALA   A 1 21  ? 10.135 -0.234  11.161  0.14 17.46 ?  21  ALA   A HA   1 
ATOM   380  H HB1  A ALA   A 1 21  ? 12.043 -1.135  12.162  0.86 21.20 ?  21  ALA   A HB1  1 
ATOM   381  H HB1  B ALA   A 1 21  ? 11.880 -0.919  12.556  0.14 17.88 ?  21  ALA   A HB1  1 
ATOM   382  H HB2  A ALA   A 1 21  ? 11.017 -2.339  12.026  0.86 21.20 ?  21  ALA   A HB2  1 
ATOM   383  H HB2  B ALA   A 1 21  ? 10.804 -2.080  12.421  0.14 17.88 ?  21  ALA   A HB2  1 
ATOM   384  H HB3  A ALA   A 1 21  ? 12.318 -2.300  11.115  0.86 21.20 ?  21  ALA   A HB3  1 
ATOM   385  H HB3  B ALA   A 1 21  ? 12.162 -2.155  11.599  0.14 17.88 ?  21  ALA   A HB3  1 
ATOM   386  N N    A ASP   A 1 22  ? 12.125 1.055   10.274  0.86 15.40 ?  22  ASP   A N    1 
ATOM   387  N N    B ASP   A 1 22  ? 12.131 1.194   10.691  0.14 14.60 ?  22  ASP   A N    1 
ATOM   388  C CA   A ASP   A 1 22  ? 13.160 1.951   9.784   0.86 15.49 ?  22  ASP   A CA   1 
ATOM   389  C CA   B ASP   A 1 22  ? 13.167 2.099   10.213  0.14 14.63 ?  22  ASP   A CA   1 
ATOM   390  C C    A ASP   A 1 22  ? 14.495 1.451   10.326  0.86 14.57 ?  22  ASP   A C    1 
ATOM   391  C C    B ASP   A 1 22  ? 14.523 1.543   10.631  0.14 14.19 ?  22  ASP   A C    1 
ATOM   392  O O    A ASP   A 1 22  ? 14.702 1.432   11.544  0.86 15.56 ?  22  ASP   A O    1 
ATOM   393  O O    B ASP   A 1 22  ? 14.792 1.386   11.827  0.14 14.21 ?  22  ASP   A O    1 
ATOM   394  C CB   A ASP   A 1 22  ? 12.849 3.353   10.307  0.86 17.83 ?  22  ASP   A CB   1 
ATOM   395  C CB   B ASP   A 1 22  ? 12.943 3.477   10.833  0.14 15.08 ?  22  ASP   A CB   1 
ATOM   396  C CG   A ASP   A 1 22  ? 13.841 4.398   9.835   0.86 20.45 ?  22  ASP   A CG   1 
ATOM   397  C CG   B ASP   A 1 22  ? 13.770 4.561   10.174  0.14 15.37 ?  22  ASP   A CG   1 
ATOM   398  O OD1  A ASP   A 1 22  ? 14.908 4.029   9.307   0.86 20.78 ?  22  ASP   A OD1  1 
ATOM   399  O OD1  B ASP   A 1 22  ? 14.883 4.260   9.697   0.14 15.23 ?  22  ASP   A OD1  1 
ATOM   400  O OD2  A ASP   A 1 22  ? 13.558 5.602   10.010  0.86 22.58 -1 22  ASP   A OD2  1 
ATOM   401  O OD2  B ASP   A 1 22  ? 13.304 5.721   10.141  0.14 15.73 -1 22  ASP   A OD2  1 
ATOM   402  H H    A ASP   A 1 22  ? 11.718 1.349   10.980  0.86 18.48 ?  22  ASP   A H    1 
ATOM   403  H H    B ASP   A 1 22  ? 11.732 1.473   11.400  0.14 17.53 ?  22  ASP   A H    1 
ATOM   404  H HA   A ASP   A 1 22  ? 13.173 1.951   8.816   0.86 18.60 ?  22  ASP   A HA   1 
ATOM   405  H HA   B ASP   A 1 22  ? 13.132 2.173   9.245   0.14 17.56 ?  22  ASP   A HA   1 
ATOM   406  H HB2  A ASP   A 1 22  ? 11.958 3.608   10.015  0.86 21.40 ?  22  ASP   A HB2  1 
ATOM   407  H HB2  B ASP   A 1 22  ? 12.007 3.715   10.749  0.14 18.10 ?  22  ASP   A HB2  1 
ATOM   408  H HB3  A ASP   A 1 22  ? 12.882 3.338   11.278  0.86 21.40 ?  22  ASP   A HB3  1 
ATOM   409  H HB3  B ASP   A 1 22  ? 13.193 3.445   11.770  0.14 18.10 ?  22  ASP   A HB3  1 
ATOM   410  N N    A ILE   A 1 23  ? 15.388 1.019   9.428   0.86 13.99 ?  23  ILE   A N    1 
ATOM   411  N N    B ILE   A 1 23  ? 15.375 1.242   9.648   0.14 13.89 ?  23  ILE   A N    1 
ATOM   412  C CA   A ILE   A 1 23  ? 16.646 0.408   9.855   0.86 13.23 ?  23  ILE   A CA   1 
ATOM   413  C CA   B ILE   A 1 23  ? 16.653 0.598   9.945   0.14 13.54 ?  23  ILE   A CA   1 
ATOM   414  C C    A ILE   A 1 23  ? 17.453 1.354   10.735  0.86 13.41 ?  23  ILE   A C    1 
ATOM   415  C C    B ILE   A 1 23  ? 17.522 1.473   10.840  0.14 13.70 ?  23  ILE   A C    1 
ATOM   416  O O    A ILE   A 1 23  ? 18.194 0.906   11.618  0.86 13.78 ?  23  ILE   A O    1 
ATOM   417  O O    B ILE   A 1 23  ? 18.276 0.961   11.677  0.14 13.75 ?  23  ILE   A O    1 
ATOM   418  C CB   A ILE   A 1 23  ? 17.444 -0.110  8.635   0.86 12.45 ?  23  ILE   A CB   1 
ATOM   419  C CB   B ILE   A 1 23  ? 17.367 0.177   8.642   0.14 13.24 ?  23  ILE   A CB   1 
ATOM   420  C CG1  A ILE   A 1 23  ? 18.595 -1.018  9.084   0.86 12.42 ?  23  ILE   A CG1  1 
ATOM   421  C CG1  B ILE   A 1 23  ? 18.663 -0.574  8.962   0.14 12.99 ?  23  ILE   A CG1  1 
ATOM   422  C CG2  A ILE   A 1 23  ? 17.949 1.044   7.771   0.86 12.77 ?  23  ILE   A CG2  1 
ATOM   423  C CG2  B ILE   A 1 23  ? 17.632 1.387   7.749   0.14 13.25 ?  23  ILE   A CG2  1 
ATOM   424  C CD1  A ILE   A 1 23  ? 19.302 -1.728  7.936   0.86 12.49 ?  23  ILE   A CD1  1 
ATOM   425  C CD1  B ILE   A 1 23  ? 19.289 -1.250  7.762   0.14 12.80 ?  23  ILE   A CD1  1 
ATOM   426  H H    A ILE   A 1 23  ? 15.279 1.065   8.581   0.86 16.80 ?  23  ILE   A H    1 
ATOM   427  H H    B ILE   A 1 23  ? 15.233 1.393   8.816   0.14 16.67 ?  23  ILE   A H    1 
ATOM   428  H HA   A ILE   A 1 23  ? 16.433 -0.365  10.400  0.86 15.89 ?  23  ILE   A HA   1 
ATOM   429  H HA   B ILE   A 1 23  ? 16.471 -0.214  10.440  0.14 16.26 ?  23  ILE   A HA   1 
ATOM   430  H HB   A ILE   A 1 23  ? 16.841 -0.646  8.094   0.86 14.95 ?  23  ILE   A HB   1 
ATOM   431  H HB   B ILE   A 1 23  ? 16.781 -0.427  8.162   0.14 15.90 ?  23  ILE   A HB   1 
ATOM   432  H HG12 A ILE   A 1 23  ? 19.255 -0.485  9.550   0.86 14.91 ?  23  ILE   A HG12 1 
ATOM   433  H HG12 B ILE   A 1 23  ? 19.311 0.053   9.316   0.14 15.59 ?  23  ILE   A HG12 1 
ATOM   434  H HG13 A ILE   A 1 23  ? 18.244 -1.702  9.679   0.86 14.91 ?  23  ILE   A HG13 1 
ATOM   435  H HG13 B ILE   A 1 23  ? 18.472 -1.260  9.620   0.14 15.59 ?  23  ILE   A HG13 1 
ATOM   436  H HG21 A ILE   A 1 23  ? 18.300 0.685   6.940   0.86 15.33 ?  23  ILE   A HG21 1 
ATOM   437  H HG21 B ILE   A 1 23  ? 18.056 1.086   6.929   0.14 15.91 ?  23  ILE   A HG21 1 
ATOM   438  H HG22 A ILE   A 1 23  ? 17.210 1.643   7.586   0.86 15.33 ?  23  ILE   A HG22 1 
ATOM   439  H HG22 B ILE   A 1 23  ? 16.788 1.818   7.539   0.14 15.91 ?  23  ILE   A HG22 1 
ATOM   440  H HG23 A ILE   A 1 23  ? 18.647 1.515   8.250   0.86 15.33 ?  23  ILE   A HG23 1 
ATOM   441  H HG23 B ILE   A 1 23  ? 18.214 2.005   8.215   0.14 15.91 ?  23  ILE   A HG23 1 
ATOM   442  H HD11 A ILE   A 1 23  ? 19.962 -2.341  8.300   0.86 15.00 ?  23  ILE   A HD11 1 
ATOM   443  H HD11 B ILE   A 1 23  ? 20.039 -1.788  8.061   0.14 15.37 ?  23  ILE   A HD11 1 
ATOM   444  H HD12 A ILE   A 1 23  ? 18.647 -2.221  7.416   0.86 15.00 ?  23  ILE   A HD12 1 
ATOM   445  H HD12 B ILE   A 1 23  ? 18.625 -1.815  7.337   0.14 15.37 ?  23  ILE   A HD12 1 
ATOM   446  H HD13 A ILE   A 1 23  ? 19.739 -1.068  7.376   0.86 15.00 ?  23  ILE   A HD13 1 
ATOM   447  H HD13 B ILE   A 1 23  ? 19.595 -0.572  7.141   0.14 15.37 ?  23  ILE   A HD13 1 
ATOM   448  N N    A VAL   A 1 24  ? 17.324 2.666   10.517  0.86 14.39 ?  24  VAL   A N    1 
ATOM   449  N N    B VAL   A 1 24  ? 17.438 2.797   10.686  0.14 14.00 ?  24  VAL   A N    1 
ATOM   450  C CA   A VAL   A 1 24  ? 18.018 3.638   11.360  0.86 15.71 ?  24  VAL   A CA   1 
ATOM   451  C CA   B VAL   A 1 24  ? 18.151 3.695   11.591  0.14 14.38 ?  24  VAL   A CA   1 
ATOM   452  C C    A VAL   A 1 24  ? 17.520 3.541   12.796  0.86 16.30 ?  24  VAL   A C    1 
ATOM   453  C C    B VAL   A 1 24  ? 17.636 3.534   13.016  0.14 15.13 ?  24  VAL   A C    1 
ATOM   454  O O    A VAL   A 1 24  ? 18.308 3.465   13.745  0.86 16.39 ?  24  VAL   A O    1 
ATOM   455  O O    B VAL   A 1 24  ? 18.415 3.505   13.976  0.14 15.04 ?  24  VAL   A O    1 
ATOM   456  C CB   A VAL   A 1 24  ? 17.837 5.059   10.795  0.86 16.81 ?  24  VAL   A CB   1 
ATOM   457  C CB   B VAL   A 1 24  ? 18.036 5.151   11.100  0.14 14.11 ?  24  VAL   A CB   1 
ATOM   458  C CG1  A VAL   A 1 24  ? 18.384 6.101   11.769  0.86 17.58 ?  24  VAL   A CG1  1 
ATOM   459  C CG1  B VAL   A 1 24  ? 18.451 6.125   12.195  0.14 14.06 ?  24  VAL   A CG1  1 
ATOM   460  C CG2  A VAL   A 1 24  ? 18.504 5.178   9.432   0.86 17.74 ?  24  VAL   A CG2  1 
ATOM   461  C CG2  B VAL   A 1 24  ? 18.881 5.358   9.853   0.14 14.12 ?  24  VAL   A CG2  1 
ATOM   462  H H    A VAL   A 1 24  ? 16.848 3.012   9.893   0.86 17.27 ?  24  VAL   A H    1 
ATOM   463  H H    B VAL   A 1 24  ? 16.987 3.193   10.073  0.14 16.81 ?  24  VAL   A H    1 
ATOM   464  H HA   A VAL   A 1 24  ? 18.967 3.438   11.360  0.86 18.87 ?  24  VAL   A HA   1 
ATOM   465  H HA   B VAL   A 1 24  ? 19.092 3.458   11.590  0.14 17.26 ?  24  VAL   A HA   1 
ATOM   466  H HB   A VAL   A 1 24  ? 16.891 5.231   10.676  0.86 20.18 ?  24  VAL   A HB   1 
ATOM   467  H HB   B VAL   A 1 24  ? 17.113 5.335   10.870  0.14 16.94 ?  24  VAL   A HB   1 
ATOM   468  H HG11 A VAL   A 1 24  ? 18.513 6.936   11.293  0.86 21.11 ?  24  VAL   A HG11 1 
ATOM   469  H HG11 B VAL   A 1 24  ? 18.621 6.992   11.795  0.14 16.88 ?  24  VAL   A HG11 1 
ATOM   470  H HG12 A VAL   A 1 24  ? 17.745 6.226   12.488  0.86 21.11 ?  24  VAL   A HG12 1 
ATOM   471  H HG12 B VAL   A 1 24  ? 17.734 6.199   12.844  0.14 16.88 ?  24  VAL   A HG12 1 
ATOM   472  H HG13 A VAL   A 1 24  ? 19.230 5.788   12.123  0.86 21.11 ?  24  VAL   A HG13 1 
ATOM   473  H HG13 B VAL   A 1 24  ? 19.257 5.796   12.622  0.14 16.88 ?  24  VAL   A HG13 1 
ATOM   474  H HG21 A VAL   A 1 24  ? 18.361 6.072   9.087   0.86 21.30 ?  24  VAL   A HG21 1 
ATOM   475  H HG21 B VAL   A 1 24  ? 18.757 6.266   9.535   0.14 16.95 ?  24  VAL   A HG21 1 
ATOM   476  H HG22 A VAL   A 1 24  ? 19.455 5.009   9.529   0.86 21.30 ?  24  VAL   A HG22 1 
ATOM   477  H HG22 B VAL   A 1 24  ? 19.813 5.210   10.076  0.14 16.95 ?  24  VAL   A HG22 1 
ATOM   478  H HG23 A VAL   A 1 24  ? 18.113 4.525   8.830   0.86 21.30 ?  24  VAL   A HG23 1 
ATOM   479  H HG23 B VAL   A 1 24  ? 18.598 4.727   9.173   0.14 16.95 ?  24  VAL   A HG23 1 
ATOM   480  N N    A GLU   A 1 25  ? 16.197 3.547   12.974  0.86 17.64 ?  25  GLU   A N    1 
ATOM   481  N N    B GLU   A 1 25  ? 16.315 3.428   13.175  0.14 16.17 ?  25  GLU   A N    1 
ATOM   482  C CA   A GLU   A 1 25  ? 15.629 3.468   14.315  0.86 19.20 ?  25  GLU   A CA   1 
ATOM   483  C CA   B GLU   A 1 25  ? 15.735 3.295   14.507  0.14 17.27 ?  25  GLU   A CA   1 
ATOM   484  C C    A GLU   A 1 25  ? 15.875 2.101   14.939  0.86 18.34 ?  25  GLU   A C    1 
ATOM   485  C C    B GLU   A 1 25  ? 16.048 1.932   15.114  0.14 17.24 ?  25  GLU   A C    1 
ATOM   486  O O    A GLU   A 1 25  ? 16.133 1.999   16.144  0.86 19.01 ?  25  GLU   A O    1 
ATOM   487  O O    B GLU   A 1 25  ? 16.378 1.837   16.302  0.14 17.16 ?  25  GLU   A O    1 
ATOM   488  C CB   A GLU   A 1 25  ? 14.135 3.792   14.266  0.86 21.61 ?  25  GLU   A CB   1 
ATOM   489  C CB   B GLU   A 1 25  ? 14.226 3.531   14.440  0.14 18.34 ?  25  GLU   A CB   1 
ATOM   490  C CG   A GLU   A 1 25  ? 13.851 5.222   13.838  0.86 24.47 ?  25  GLU   A CG   1 
ATOM   491  C CG   B GLU   A 1 25  ? 13.844 4.944   14.020  0.14 19.37 ?  25  GLU   A CG   1 
ATOM   492  C CD   A GLU   A 1 25  ? 14.590 6.231   14.698  0.86 26.70 ?  25  GLU   A CD   1 
ATOM   493  C CD   B GLU   A 1 25  ? 14.145 5.964   15.099  0.14 20.17 ?  25  GLU   A CD   1 
ATOM   494  O OE1  A GLU   A 1 25  ? 14.579 6.069   15.938  0.86 27.48 ?  25  GLU   A OE1  1 
ATOM   495  O OE1  B GLU   A 1 25  ? 13.617 5.817   16.221  0.14 20.42 ?  25  GLU   A OE1  1 
ATOM   496  O OE2  A GLU   A 1 25  ? 15.202 7.165   14.138  0.86 27.75 -1 25  GLU   A OE2  1 
ATOM   497  O OE2  B GLU   A 1 25  ? 14.921 6.905   14.831  0.14 20.34 -1 25  GLU   A OE2  1 
ATOM   498  H H    A GLU   A 1 25  ? 15.618 3.598   12.341  0.86 21.17 ?  25  GLU   A H    1 
ATOM   499  H H    B GLU   A 1 25  ? 15.744 3.434   12.534  0.14 19.42 ?  25  GLU   A H    1 
ATOM   500  H HA   A GLU   A 1 25  ? 16.063 4.124   14.881  0.86 23.05 ?  25  GLU   A HA   1 
ATOM   501  H HA   B GLU   A 1 25  ? 16.116 3.974   15.085  0.14 20.74 ?  25  GLU   A HA   1 
ATOM   502  H HB2  A GLU   A 1 25  ? 13.700 3.201   13.631  0.86 25.95 ?  25  GLU   A HB2  1 
ATOM   503  H HB2  B GLU   A 1 25  ? 13.837 2.916   13.801  0.14 22.01 ?  25  GLU   A HB2  1 
ATOM   504  H HB3  A GLU   A 1 25  ? 13.751 3.668   15.148  0.86 25.95 ?  25  GLU   A HB3  1 
ATOM   505  H HB3  B GLU   A 1 25  ? 13.845 3.377   15.318  0.14 22.01 ?  25  GLU   A HB3  1 
ATOM   506  H HG2  A GLU   A 1 25  ? 14.139 5.340   12.919  0.86 29.37 ?  25  GLU   A HG2  1 
ATOM   507  H HG2  B GLU   A 1 25  ? 14.347 5.189   13.226  0.14 23.25 ?  25  GLU   A HG2  1 
ATOM   508  H HG3  A GLU   A 1 25  ? 12.895 5.390   13.908  0.86 29.37 ?  25  GLU   A HG3  1 
ATOM   509  H HG3  B GLU   A 1 25  ? 12.892 4.975   13.830  0.14 23.25 ?  25  GLU   A HG3  1 
ATOM   510  N N    A GLU   A 1 26  ? 15.822 1.039   14.131  0.86 17.51 ?  26  GLU   A N    1 
ATOM   511  N N    B GLU   A 1 26  ? 15.955 0.865   14.316  0.14 17.32 ?  26  GLU   A N    1 
ATOM   512  C CA   A GLU   A 1 26  ? 16.131 -0.296  14.638  0.86 17.06 ?  26  GLU   A CA   1 
ATOM   513  C CA   B GLU   A 1 26  ? 16.287 -0.464  14.820  0.14 17.52 ?  26  GLU   A CA   1 
ATOM   514  C C    A GLU   A 1 26  ? 17.564 -0.362  15.149  0.86 15.62 ?  26  GLU   A C    1 
ATOM   515  C C    B GLU   A 1 26  ? 17.744 -0.538  15.258  0.14 17.34 ?  26  GLU   A C    1 
ATOM   516  O O    A GLU   A 1 26  ? 17.831 -0.894  16.233  0.86 15.74 ?  26  GLU   A O    1 
ATOM   517  O O    B GLU   A 1 26  ? 18.057 -1.109  16.309  0.14 17.15 ?  26  GLU   A O    1 
ATOM   518  C CB   A GLU   A 1 26  ? 15.936 -1.331  13.530  0.86 18.81 ?  26  GLU   A CB   1 
ATOM   519  C CB   B GLU   A 1 26  ? 16.000 -1.517  13.750  0.14 18.11 ?  26  GLU   A CB   1 
ATOM   520  C CG   A GLU   A 1 26  ? 14.549 -1.907  13.396  0.86 21.12 ?  26  GLU   A CG   1 
ATOM   521  C CG   B GLU   A 1 26  ? 14.529 -1.832  13.568  0.14 18.86 ?  26  GLU   A CG   1 
ATOM   522  C CD   A GLU   A 1 26  ? 14.118 -2.712  14.613  0.86 22.01 ?  26  GLU   A CD   1 
ATOM   523  C CD   B GLU   A 1 26  ? 13.963 -2.666  14.700  0.14 19.41 ?  26  GLU   A CD   1 
ATOM   524  O OE1  A GLU   A 1 26  ? 14.569 -3.869  14.836  0.86 22.58 ?  26  GLU   A OE1  1 
ATOM   525  O OE1  B GLU   A 1 26  ? 14.617 -3.654  15.100  0.14 19.50 ?  26  GLU   A OE1  1 
ATOM   526  O OE2  A GLU   A 1 26  ? 13.301 -2.161  15.355  0.86 22.70 -1 26  GLU   A OE2  1 
ATOM   527  O OE2  B GLU   A 1 26  ? 12.866 -2.331  15.193  0.14 19.66 -1 26  GLU   A OE2  1 
ATOM   528  H H    A GLU   A 1 26  ? 15.623 1.070   13.295  0.86 21.03 ?  26  GLU   A H    1 
ATOM   529  H H    B GLU   A 1 26  ? 15.709 0.887   13.493  0.14 20.80 ?  26  GLU   A H    1 
ATOM   530  H HA   A GLU   A 1 26  ? 15.532 -0.505  15.369  0.86 20.49 ?  26  GLU   A HA   1 
ATOM   531  H HA   B GLU   A 1 26  ? 15.731 -0.660  15.589  0.14 21.04 ?  26  GLU   A HA   1 
ATOM   532  H HB2  A GLU   A 1 26  ? 16.162 -0.915  12.681  0.86 22.58 ?  26  GLU   A HB2  1 
ATOM   533  H HB2  B GLU   A 1 26  ? 16.341 -1.199  12.899  0.14 21.74 ?  26  GLU   A HB2  1 
ATOM   534  H HB3  A GLU   A 1 26  ? 16.539 -2.070  13.696  0.86 22.58 ?  26  GLU   A HB3  1 
ATOM   535  H HB3  B GLU   A 1 26  ? 16.450 -2.341  13.994  0.14 21.74 ?  26  GLU   A HB3  1 
ATOM   536  H HG2  A GLU   A 1 26  ? 13.924 -1.169  13.261  0.86 25.35 ?  26  GLU   A HG2  1 
ATOM   537  H HG2  B GLU   A 1 26  ? 14.033 -1.001  13.535  0.14 22.64 ?  26  GLU   A HG2  1 
ATOM   538  H HG3  A GLU   A 1 26  ? 14.522 -2.500  12.634  0.86 25.35 ?  26  GLU   A HG3  1 
ATOM   539  H HG3  B GLU   A 1 26  ? 14.414 -2.323  12.740  0.14 22.64 ?  26  GLU   A HG3  1 
ATOM   540  N N    A ALA   A 1 27  ? 18.507 0.172   14.372  0.86 13.91 ?  27  ALA   A N    1 
ATOM   541  N N    B ALA   A 1 27  ? 18.651 0.032   14.462  0.14 17.51 ?  27  ALA   A N    1 
ATOM   542  C CA   A ALA   A 1 27  ? 19.904 0.134   14.787  0.86 13.65 ?  27  ALA   A CA   1 
ATOM   543  C CA   B ALA   A 1 27  ? 20.062 0.018   14.831  0.14 17.91 ?  27  ALA   A CA   1 
ATOM   544  C C    A ALA   A 1 27  ? 20.120 0.923   16.073  0.86 14.86 ?  27  ALA   A C    1 
ATOM   545  C C    B ALA   A 1 27  ? 20.311 0.837   16.090  0.14 18.66 ?  27  ALA   A C    1 
ATOM   546  O O    A ALA   A 1 27  ? 20.811 0.460   16.988  0.86 15.06 ?  27  ALA   A O    1 
ATOM   547  O O    B ALA   A 1 27  ? 21.079 0.421   16.966  0.14 18.58 ?  27  ALA   A O    1 
ATOM   548  C CB   A ALA   A 1 27  ? 20.796 0.670   13.665  0.86 13.37 ?  27  ALA   A CB   1 
ATOM   549  C CB   B ALA   A 1 27  ? 20.914 0.532   13.671  0.14 17.79 ?  27  ALA   A CB   1 
ATOM   550  H H    A ALA   A 1 27  ? 18.362 0.561   13.620  0.86 16.70 ?  27  ALA   A H    1 
ATOM   551  H H    B ALA   A 1 27  ? 18.476 0.422   13.717  0.14 21.03 ?  27  ALA   A H    1 
ATOM   552  H HA   A ALA   A 1 27  ? 20.156 -0.781  14.959  0.86 16.39 ?  27  ALA   A HA   1 
ATOM   553  H HA   B ALA   A 1 27  ? 20.329 -0.895  15.015  0.14 21.51 ?  27  ALA   A HA   1 
ATOM   554  H HB1  A ALA   A 1 27  ? 21.723 0.639   13.957  0.86 16.06 ?  27  ALA   A HB1  1 
ATOM   555  H HB1  B ALA   A 1 27  ? 21.848 0.514   13.935  0.14 21.36 ?  27  ALA   A HB1  1 
ATOM   556  H HB2  A ALA   A 1 27  ? 20.679 0.116   12.879  0.86 16.06 ?  27  ALA   A HB2  1 
ATOM   557  H HB2  B ALA   A 1 27  ? 20.777 -0.043  12.902  0.14 21.36 ?  27  ALA   A HB2  1 
ATOM   558  H HB3  A ALA   A 1 27  ? 20.545 1.586   13.467  0.86 16.06 ?  27  ALA   A HB3  1 
ATOM   559  H HB3  B ALA   A 1 27  ? 20.647 1.439   13.460  0.14 21.36 ?  27  ALA   A HB3  1 
ATOM   560  N N    A LYS   A 1 28  ? 19.526 2.116   16.170  0.86 16.97 ?  28  LYS   A N    1 
ATOM   561  N N    B LYS   A 1 28  ? 19.673 2.005   16.202  0.14 19.66 ?  28  LYS   A N    1 
ATOM   562  C CA   A LYS   A 1 28  ? 19.696 2.925   17.375  0.86 20.07 ?  28  LYS   A CA   1 
ATOM   563  C CA   B LYS   A 1 28  ? 19.823 2.805   17.413  0.14 20.74 ?  28  LYS   A CA   1 
ATOM   564  C C    A LYS   A 1 28  ? 19.180 2.209   18.618  0.86 20.69 ?  28  LYS   A C    1 
ATOM   565  C C    B LYS   A 1 28  ? 19.273 2.069   18.627  0.14 20.83 ?  28  LYS   A C    1 
ATOM   566  O O    A LYS   A 1 28  ? 19.746 2.368   19.705  0.86 22.40 ?  28  LYS   A O    1 
ATOM   567  O O    B LYS   A 1 28  ? 19.883 2.088   19.702  0.14 21.11 ?  28  LYS   A O    1 
ATOM   568  C CB   A LYS   A 1 28  ? 19.022 4.290   17.202  0.86 22.23 ?  28  LYS   A CB   1 
ATOM   569  C CB   B LYS   A 1 28  ? 19.129 4.156   17.245  0.14 21.58 ?  28  LYS   A CB   1 
ATOM   570  C CG   A LYS   A 1 28  ? 19.789 5.219   16.271  0.86 24.30 ?  28  LYS   A CG   1 
ATOM   571  C CG   B LYS   A 1 28  ? 19.933 5.181   16.460  0.14 22.33 ?  28  LYS   A CG   1 
ATOM   572  C CD   A LYS   A 1 28  ? 19.300 6.656   16.347  0.86 26.89 ?  28  LYS   A CD   1 
ATOM   573  C CD   B LYS   A 1 28  ? 19.276 6.553   16.522  0.14 23.01 ?  28  LYS   A CD   1 
ATOM   574  C CE   A LYS   A 1 28  ? 17.979 6.834   15.630  0.86 28.74 ?  28  LYS   A CE   1 
ATOM   575  C CE   B LYS   A 1 28  ? 17.819 6.489   16.085  0.14 23.44 ?  28  LYS   A CE   1 
ATOM   576  N NZ   A LYS   A 1 28  ? 17.578 8.268   15.580  0.86 29.90 ?  28  LYS   A NZ   1 
ATOM   577  N NZ   B LYS   A 1 28  ? 17.164 7.819   16.116  0.14 23.69 ?  28  LYS   A NZ   1 
ATOM   578  H H    A LYS   A 1 28  ? 19.028 2.474   15.568  0.86 20.38 ?  28  LYS   A H    1 
ATOM   579  H H    B LYS   A 1 28  ? 19.155 2.346   15.606  0.14 23.60 ?  28  LYS   A H    1 
ATOM   580  H HA   A LYS   A 1 28  ? 20.639 3.085   17.515  0.86 24.09 ?  28  LYS   A HA   1 
ATOM   581  H HA   B LYS   A 1 28  ? 20.761 2.972   17.570  0.14 24.89 ?  28  LYS   A HA   1 
ATOM   582  H HB2  A LYS   A 1 28  ? 18.135 4.165   16.831  0.86 26.69 ?  28  LYS   A HB2  1 
ATOM   583  H HB2  B LYS   A 1 28  ? 18.297 4.009   16.770  0.14 25.90 ?  28  LYS   A HB2  1 
ATOM   584  H HB3  A LYS   A 1 28  ? 18.958 4.728   18.067  0.86 26.69 ?  28  LYS   A HB3  1 
ATOM   585  H HB3  B LYS   A 1 28  ? 18.947 4.537   18.120  0.14 25.90 ?  28  LYS   A HB3  1 
ATOM   586  H HG2  A LYS   A 1 28  ? 20.727 5.208   16.515  0.86 29.17 ?  28  LYS   A HG2  1 
ATOM   587  H HG2  B LYS   A 1 28  ? 20.824 5.253   16.840  0.14 26.80 ?  28  LYS   A HG2  1 
ATOM   588  H HG3  A LYS   A 1 28  ? 19.678 4.913   15.358  0.86 29.17 ?  28  LYS   A HG3  1 
ATOM   589  H HG3  B LYS   A 1 28  ? 19.984 4.910   15.531  0.14 26.80 ?  28  LYS   A HG3  1 
ATOM   590  H HD2  A LYS   A 1 28  ? 19.176 6.905   17.277  0.86 32.28 ?  28  LYS   A HD2  1 
ATOM   591  H HD2  B LYS   A 1 28  ? 19.309 6.883   17.434  0.14 27.62 ?  28  LYS   A HD2  1 
ATOM   592  H HD3  A LYS   A 1 28  ? 19.953 7.239   15.929  0.86 32.28 ?  28  LYS   A HD3  1 
ATOM   593  H HD3  B LYS   A 1 28  ? 19.747 7.160   15.928  0.14 27.62 ?  28  LYS   A HD3  1 
ATOM   594  H HE2  A LYS   A 1 28  ? 18.063 6.510   14.719  0.86 34.50 ?  28  LYS   A HE2  1 
ATOM   595  H HE2  B LYS   A 1 28  ? 17.776 6.140   15.180  0.14 28.14 ?  28  LYS   A HE2  1 
ATOM   596  H HE3  A LYS   A 1 28  ? 17.289 6.341   16.100  0.86 34.50 ?  28  LYS   A HE3  1 
ATOM   597  H HE3  B LYS   A 1 28  ? 17.325 5.912   16.689  0.14 28.14 ?  28  LYS   A HE3  1 
ATOM   598  H HZ1  A LYS   A 1 28  ? 16.802 8.352   15.155  0.86 35.89 ?  28  LYS   A HZ1  1 
ATOM   599  H HZ1  B LYS   A 1 28  ? 16.316 7.743   15.857  0.14 28.44 ?  28  LYS   A HZ1  1 
ATOM   600  H HZ2  A LYS   A 1 28  ? 17.493 8.588   16.406  0.86 35.89 ?  28  LYS   A HZ2  1 
ATOM   601  H HZ2  B LYS   A 1 28  ? 17.186 8.148   16.943  0.14 28.44 ?  28  LYS   A HZ2  1 
ATOM   602  H HZ3  A LYS   A 1 28  ? 18.197 8.741   15.149  0.86 35.89 ?  28  LYS   A HZ3  1 
ATOM   603  H HZ3  B LYS   A 1 28  ? 17.586 8.378   15.570  0.14 28.44 ?  28  LYS   A HZ3  1 
ATOM   604  N N    . LYS   A 1 29  ? 18.125 1.406   18.474  1.00 20.72 ?  29  LYS   A N    1 
ATOM   605  C CA   . LYS   A 1 29  ? 17.532 0.701   19.608  1.00 22.41 ?  29  LYS   A CA   1 
ATOM   606  C C    . LYS   A 1 29  ? 18.349 -0.529  19.989  1.00 20.95 ?  29  LYS   A C    1 
ATOM   607  O O    . LYS   A 1 29  ? 18.645 -0.752  21.169  1.00 21.88 ?  29  LYS   A O    1 
ATOM   608  C CB   . LYS   A 1 29  ? 16.100 0.292   19.256  1.00 25.55 ?  29  LYS   A CB   1 
ATOM   609  C CG   . LYS   A 1 29  ? 15.354 -0.416  20.374  1.00 28.90 ?  29  LYS   A CG   1 
ATOM   610  C CD   . LYS   A 1 29  ? 14.965 0.556   21.474  1.00 32.08 ?  29  LYS   A CD   1 
ATOM   611  C CE   . LYS   A 1 29  ? 14.054 -0.096  22.499  1.00 34.36 ?  29  LYS   A CE   1 
ATOM   612  N NZ   . LYS   A 1 29  ? 13.556 0.892   23.493  1.00 35.63 ?  29  LYS   A NZ   1 
ATOM   613  H H    A LYS   A 1 29  ? 17.734 1.251   17.724  0.86 24.87 ?  29  LYS   A H    1 
ATOM   614  H H    B LYS   A 1 29  ? 17.680 1.346   17.739  0.14 24.87 ?  29  LYS   A H    1 
ATOM   615  H HA   . LYS   A 1 29  ? 17.497 1.294   20.374  1.00 26.91 ?  29  LYS   A HA   1 
ATOM   616  H HB2  . LYS   A 1 29  ? 15.595 1.088   19.026  1.00 30.66 ?  29  LYS   A HB2  1 
ATOM   617  H HB3  . LYS   A 1 29  ? 16.125 -0.309  18.495  1.00 30.66 ?  29  LYS   A HB3  1 
ATOM   618  H HG2  . LYS   A 1 29  ? 14.541 -0.810  20.018  1.00 34.69 ?  29  LYS   A HG2  1 
ATOM   619  H HG3  . LYS   A 1 29  ? 15.915 -1.108  20.761  1.00 34.69 ?  29  LYS   A HG3  1 
ATOM   620  H HD2  . LYS   A 1 29  ? 15.766 0.860   21.930  1.00 38.51 ?  29  LYS   A HD2  1 
ATOM   621  H HD3  . LYS   A 1 29  ? 14.495 1.309   21.084  1.00 38.51 ?  29  LYS   A HD3  1 
ATOM   622  H HE2  . LYS   A 1 29  ? 13.289 -0.485  22.045  1.00 41.24 ?  29  LYS   A HE2  1 
ATOM   623  H HE3  . LYS   A 1 29  ? 14.547 -0.784  22.973  1.00 41.24 ?  29  LYS   A HE3  1 
ATOM   624  H HZ1  . LYS   A 1 29  ? 13.024 0.489   24.082  1.00 42.76 ?  29  LYS   A HZ1  1 
ATOM   625  H HZ2  . LYS   A 1 29  ? 14.240 1.260   23.926  1.00 42.76 ?  29  LYS   A HZ2  1 
ATOM   626  H HZ3  . LYS   A 1 29  ? 13.096 1.533   23.080  1.00 42.76 ?  29  LYS   A HZ3  1 
ATOM   627  N N    . VAL   A 1 30  ? 18.701 -1.351  19.001  1.00 19.64 ?  30  VAL   A N    1 
ATOM   628  C CA   . VAL   A 1 30  ? 19.331 -2.638  19.270  1.00 18.80 ?  30  VAL   A CA   1 
ATOM   629  C C    . VAL   A 1 30  ? 20.841 -2.508  19.461  1.00 17.70 ?  30  VAL   A C    1 
ATOM   630  O O    . VAL   A 1 30  ? 21.439 -3.261  20.238  1.00 18.04 ?  30  VAL   A O    1 
ATOM   631  C CB   . VAL   A 1 30  ? 18.988 -3.606  18.124  1.00 19.42 ?  30  VAL   A CB   1 
ATOM   632  C CG1  . VAL   A 1 30  ? 19.745 -4.918  18.274  1.00 19.87 ?  30  VAL   A CG1  1 
ATOM   633  C CG2  . VAL   A 1 30  ? 17.485 -3.849  18.066  1.00 20.51 ?  30  VAL   A CG2  1 
ATOM   634  H H    . VAL   A 1 30  ? 18.573 -1.189  18.162  1.00 23.57 ?  30  VAL   A H    1 
ATOM   635  H HA   . VAL   A 1 30  ? 18.951 -3.000  20.085  1.00 22.57 ?  30  VAL   A HA   1 
ATOM   636  H HB   . VAL   A 1 30  ? 19.251 -3.206  17.283  1.00 23.31 ?  30  VAL   A HB   1 
ATOM   637  H HG11 . VAL   A 1 30  ? 19.342 -5.581  17.689  1.00 23.86 ?  30  VAL   A HG11 1 
ATOM   638  H HG12 . VAL   A 1 30  ? 20.670 -4.781  18.028  1.00 23.86 ?  30  VAL   A HG12 1 
ATOM   639  H HG13 . VAL   A 1 30  ? 19.682 -5.214  19.196  1.00 23.86 ?  30  VAL   A HG13 1 
ATOM   640  H HG21 . VAL   A 1 30  ? 17.294 -4.502  17.373  1.00 24.62 ?  30  VAL   A HG21 1 
ATOM   641  H HG22 . VAL   A 1 30  ? 17.185 -4.188  18.926  1.00 24.62 ?  30  VAL   A HG22 1 
ATOM   642  H HG23 . VAL   A 1 30  ? 17.033 -3.015  17.867  1.00 24.62 ?  30  VAL   A HG23 1 
ATOM   643  N N    A LYS   A 1 31  ? 21.477 -1.566  18.772  0.86 16.27 ?  31  LYS   A N    1 
ATOM   644  N N    B LYS   A 1 31  ? 21.467 -1.547  18.790  0.14 18.14 ?  31  LYS   A N    1 
ATOM   645  C CA   A LYS   A 1 31  ? 22.931 -1.462  18.720  0.86 16.64 ?  31  LYS   A CA   1 
ATOM   646  C CA   B LYS   A 1 31  ? 22.919 -1.453  18.709  0.14 18.70 ?  31  LYS   A CA   1 
ATOM   647  C C    A LYS   A 1 31  ? 23.541 -2.810  18.327  0.86 15.53 ?  31  LYS   A C    1 
ATOM   648  C C    B LYS   A 1 31  ? 23.520 -2.811  18.336  0.14 16.75 ?  31  LYS   A C    1 
ATOM   649  O O    A LYS   A 1 31  ? 24.335 -3.386  19.077  0.86 16.59 ?  31  LYS   A O    1 
ATOM   650  O O    B LYS   A 1 31  ? 24.300 -3.385  19.100  0.14 17.09 ?  31  LYS   A O    1 
ATOM   651  C CB   A LYS   A 1 31  ? 23.518 -0.953  20.030  0.86 20.40 ?  31  LYS   A CB   1 
ATOM   652  C CB   B LYS   A 1 31  ? 23.529 -0.918  19.998  0.14 21.24 ?  31  LYS   A CB   1 
ATOM   653  C CG   A LYS   A 1 31  ? 22.805 0.274   20.590  0.86 25.71 ?  31  LYS   A CG   1 
ATOM   654  C CG   B LYS   A 1 31  ? 22.885 0.372   20.485  0.14 23.67 ?  31  LYS   A CG   1 
ATOM   655  C CD   A LYS   A 1 31  ? 23.768 1.423   20.850  0.86 29.81 ?  31  LYS   A CD   1 
ATOM   656  C CD   B LYS   A 1 31  ? 23.910 1.324   21.081  0.14 25.57 ?  31  LYS   A CD   1 
ATOM   657  C CE   A LYS   A 1 31  ? 23.155 2.475   21.769  0.86 32.38 ?  31  LYS   A CE   1 
ATOM   658  C CE   B LYS   A 1 31  ? 23.239 2.448   21.860  0.14 26.81 ?  31  LYS   A CE   1 
ATOM   659  N NZ   A LYS   A 1 31  ? 21.938 3.116   21.195  0.86 33.68 ?  31  LYS   A NZ   1 
ATOM   660  N NZ   B LYS   A 1 31  ? 22.225 3.184   21.054  0.14 27.45 ?  31  LYS   A NZ   1 
ATOM   661  H H    A LYS   A 1 31  ? 21.074 -0.950  18.326  0.86 19.53 ?  31  LYS   A H    1 
ATOM   662  H H    B LYS   A 1 31  ? 21.059 -0.919  18.367  0.14 21.78 ?  31  LYS   A H    1 
ATOM   663  H HA   A LYS   A 1 31  ? 23.161 -0.826  18.031  0.86 19.98 ?  31  LYS   A HA   1 
ATOM   664  H HA   B LYS   A 1 31  ? 23.140 -0.832  18.006  0.14 22.45 ?  31  LYS   A HA   1 
ATOM   665  H HB2  A LYS   A 1 31  ? 23.465 -1.658  20.693  0.86 24.49 ?  31  LYS   A HB2  1 
ATOM   666  H HB2  B LYS   A 1 31  ? 23.430 -1.582  20.695  0.14 25.50 ?  31  LYS   A HB2  1 
ATOM   667  H HB3  A LYS   A 1 31  ? 24.447 -0.715  19.877  0.86 24.49 ?  31  LYS   A HB3  1 
ATOM   668  H HB3  B LYS   A 1 31  ? 24.471 -0.739  19.843  0.14 25.50 ?  31  LYS   A HB3  1 
ATOM   669  H HG2  A LYS   A 1 31  ? 22.141 0.578   19.951  0.86 30.86 ?  31  LYS   A HG2  1 
ATOM   670  H HG2  B LYS   A 1 31  ? 22.456 0.817   19.737  0.14 28.41 ?  31  LYS   A HG2  1 
ATOM   671  H HG3  A LYS   A 1 31  ? 22.377 0.038   21.428  0.86 30.86 ?  31  LYS   A HG3  1 
ATOM   672  H HG3  B LYS   A 1 31  ? 22.231 0.162   21.169  0.14 28.41 ?  31  LYS   A HG3  1 
ATOM   673  H HD2  A LYS   A 1 31  ? 24.569 1.080   21.275  0.86 35.78 ?  31  LYS   A HD2  1 
ATOM   674  H HD2  B LYS   A 1 31  ? 24.487 0.835   21.687  0.14 30.69 ?  31  LYS   A HD2  1 
ATOM   675  H HD3  A LYS   A 1 31  ? 23.992 1.849   20.007  0.86 35.78 ?  31  LYS   A HD3  1 
ATOM   676  H HD3  B LYS   A 1 31  ? 24.433 1.720   20.365  0.14 30.69 ?  31  LYS   A HD3  1 
ATOM   677  H HE2  A LYS   A 1 31  ? 22.903 2.053   22.606  0.86 38.86 ?  31  LYS   A HE2  1 
ATOM   678  H HE2  B LYS   A 1 31  ? 22.792 2.072   22.634  0.14 32.18 ?  31  LYS   A HE2  1 
ATOM   679  H HE3  A LYS   A 1 31  ? 23.810 3.171   21.933  0.86 38.86 ?  31  LYS   A HE3  1 
ATOM   680  H HE3  B LYS   A 1 31  ? 23.915 3.083   22.143  0.14 32.18 ?  31  LYS   A HE3  1 
ATOM   681  H HZ1  A LYS   A 1 31  ? 21.615 3.721   21.764  0.86 40.42 ?  31  LYS   A HZ1  1 
ATOM   682  H HZ1  B LYS   A 1 31  ? 21.874 3.845   21.537  0.14 32.95 ?  31  LYS   A HZ1  1 
ATOM   683  H HZ2  A LYS   A 1 31  ? 22.139 3.521   20.428  0.86 40.42 ?  31  LYS   A HZ2  1 
ATOM   684  H HZ2  B LYS   A 1 31  ? 22.605 3.528   20.327  0.14 32.95 ?  31  LYS   A HZ2  1 
ATOM   685  H HZ3  A LYS   A 1 31  ? 21.312 2.502   21.042  0.86 40.42 ?  31  LYS   A HZ3  1 
ATOM   686  H HZ3  B LYS   A 1 31  ? 21.573 2.630   20.806  0.14 32.95 ?  31  LYS   A HZ3  1 
ATOM   687  N N    . PRO   A 1 32  ? 23.172 -3.343  17.168  1.00 14.48 ?  32  PRO   A N    1 
ATOM   688  C CA   . PRO   A 1 32  ? 23.643 -4.673  16.789  1.00 14.29 ?  32  PRO   A CA   1 
ATOM   689  C C    . PRO   A 1 32  ? 25.142 -4.681  16.558  1.00 14.10 ?  32  PRO   A C    1 
ATOM   690  O O    . PRO   A 1 32  ? 25.774 -3.649  16.321  1.00 14.13 ?  32  PRO   A O    1 
ATOM   691  C CB   . PRO   A 1 32  ? 22.888 -4.942  15.482  1.00 14.70 ?  32  PRO   A CB   1 
ATOM   692  C CG   . PRO   A 1 32  ? 22.705 -3.566  14.894  1.00 13.72 ?  32  PRO   A CG   1 
ATOM   693  C CD   . PRO   A 1 32  ? 22.426 -2.689  16.079  1.00 13.62 ?  32  PRO   A CD   1 
ATOM   694  H HA   . PRO   A 1 32  ? 23.408 -5.335  17.452  1.00 17.16 ?  32  PRO   A HA   1 
ATOM   695  H HB2  . PRO   A 1 32  ? 23.419 -5.508  14.895  1.00 17.65 ?  32  PRO   A HB2  1 
ATOM   696  H HB3  . PRO   A 1 32  ? 22.030 -5.358  15.674  1.00 17.65 ?  32  PRO   A HB3  1 
ATOM   697  H HG2  . PRO   A 1 32  ? 23.515 -3.305  14.435  1.00 16.47 ?  32  PRO   A HG2  1 
ATOM   698  H HG3  . PRO   A 1 32  ? 21.950 -3.582  14.279  1.00 16.47 ?  32  PRO   A HG3  1 
ATOM   699  H HD2  . PRO   A 1 32  ? 22.773 -1.801  15.904  1.00 16.36 ?  32  PRO   A HD2  1 
ATOM   700  H HD3  . PRO   A 1 32  ? 21.480 -2.679  16.265  1.00 16.36 ?  32  PRO   A HD3  1 
ATOM   701  N N    . THR   A 1 33  ? 25.709 -5.885  16.604  1.00 14.41 ?  33  THR   A N    1 
ATOM   702  C CA   . THR   A 1 33  ? 27.113 -6.042  16.254  1.00 14.49 ?  33  THR   A CA   1 
ATOM   703  C C    . THR   A 1 33  ? 27.376 -5.571  14.831  1.00 12.85 ?  33  THR   A C    1 
ATOM   704  O O    . THR   A 1 33  ? 28.400 -4.927  14.564  1.00 13.21 ?  33  THR   A O    1 
ATOM   705  C CB   . THR   A 1 33  ? 27.521 -7.503  16.439  1.00 16.10 ?  33  THR   A CB   1 
ATOM   706  O OG1  . THR   A 1 33  ? 27.224 -7.900  17.782  1.00 17.86 ?  33  THR   A OG1  1 
ATOM   707  C CG2  . THR   A 1 33  ? 29.007 -7.692  16.171  1.00 17.22 ?  33  THR   A CG2  1 
ATOM   708  H H    . THR   A 1 33  ? 25.308 -6.613  16.819  1.00 17.30 ?  33  THR   A H    1 
ATOM   709  H HA   . THR   A 1 33  ? 27.653 -5.505  16.849  1.00 17.40 ?  33  THR   A HA   1 
ATOM   710  H HB   . THR   A 1 33  ? 27.027 -8.067  15.819  1.00 19.33 ?  33  THR   A HB   1 
ATOM   711  H HG1  . THR   A 1 33  ? 27.661 -7.428  18.325  1.00 21.45 ?  33  THR   A HG1  1 
ATOM   712  H HG21 . THR   A 1 33  ? 29.283 -8.585  16.436  1.00 20.68 ?  33  THR   A HG21 1 
ATOM   713  H HG22 . THR   A 1 33  ? 29.195 -7.575  15.227  1.00 20.68 ?  33  THR   A HG22 1 
ATOM   714  H HG23 . THR   A 1 33  ? 29.519 -7.043  16.678  1.00 20.68 ?  33  THR   A HG23 1 
ATOM   715  N N    . VAL   A 1 34  ? 26.462 -5.875  13.906  1.00 11.70 ?  34  VAL   A N    1 
ATOM   716  C CA   . VAL   A 1 34  ? 26.623 -5.529  12.497  1.00 10.66 ?  34  VAL   A CA   1 
ATOM   717  C C    . VAL   A 1 34  ? 25.314 -4.965  11.952  1.00 10.05 ?  34  VAL   A C    1 
ATOM   718  O O    . VAL   A 1 34  ? 24.272 -5.633  12.006  1.00 10.83 ?  34  VAL   A O    1 
ATOM   719  C CB   . VAL   A 1 34  ? 27.063 -6.732  11.641  1.00 11.25 ?  34  VAL   A CB   1 
ATOM   720  C CG1  . VAL   A 1 34  ? 27.221 -6.312  10.184  1.00 11.65 ?  34  VAL   A CG1  1 
ATOM   721  C CG2  . VAL   A 1 34  ? 28.357 -7.341  12.173  1.00 12.38 ?  34  VAL   A CG2  1 
ATOM   722  H H    . VAL   A 1 34  ? 25.727 -6.291  14.072  1.00 14.05 ?  34  VAL   A H    1 
ATOM   723  H HA   . VAL   A 1 34  ? 27.302 -4.839  12.412  1.00 12.80 ?  34  VAL   A HA   1 
ATOM   724  H HB   . VAL   A 1 34  ? 26.373 -7.411  11.675  1.00 13.51 ?  34  VAL   A HB   1 
ATOM   725  H HG11 . VAL   A 1 34  ? 27.714 -7.000  9.708   1.00 13.99 ?  34  VAL   A HG11 1 
ATOM   726  H HG12 . VAL   A 1 34  ? 26.348 -6.194  9.783   1.00 13.99 ?  34  VAL   A HG12 1 
ATOM   727  H HG13 . VAL   A 1 34  ? 27.718 -5.474  10.148  1.00 13.99 ?  34  VAL   A HG13 1 
ATOM   728  H HG21 . VAL   A 1 34  ? 28.629 -8.071  11.590  1.00 14.87 ?  34  VAL   A HG21 1 
ATOM   729  H HG22 . VAL   A 1 34  ? 29.049 -6.661  12.190  1.00 14.87 ?  34  VAL   A HG22 1 
ATOM   730  H HG23 . VAL   A 1 34  ? 28.204 -7.679  13.070  1.00 14.87 ?  34  VAL   A HG23 1 
ATOM   731  N N    . VAL   A 1 35  ? 25.376 -3.752  11.394  1.00 9.63  ?  35  VAL   A N    1 
ATOM   732  C CA   . VAL   A 1 35  ? 24.330 -3.230  10.521  1.00 9.28  ?  35  VAL   A CA   1 
ATOM   733  C C    . VAL   A 1 35  ? 24.870 -3.221  9.101   1.00 8.60  ?  35  VAL   A C    1 
ATOM   734  O O    . VAL   A 1 35  ? 26.011 -2.810  8.862   1.00 9.28  ?  35  VAL   A O    1 
ATOM   735  C CB   . VAL   A 1 35  ? 23.799 -1.843  10.952  1.00 9.92  ?  35  VAL   A CB   1 
ATOM   736  C CG1  . VAL   A 1 35  ? 24.866 -0.742  10.812  1.00 10.65 ?  35  VAL   A CG1  1 
ATOM   737  C CG2  . VAL   A 1 35  ? 22.539 -1.487  10.155  1.00 10.48 ?  35  VAL   A CG2  1 
ATOM   738  H H    . VAL   A 1 35  ? 26.028 -3.200  11.505  1.00 11.56 ?  35  VAL   A H    1 
ATOM   739  H HA   . VAL   A 1 35  ? 23.574 -3.843  10.547  1.00 11.15 ?  35  VAL   A HA   1 
ATOM   740  H HB   . VAL   A 1 35  ? 23.539 -1.881  11.885  1.00 11.91 ?  35  VAL   A HB   1 
ATOM   741  H HG11 . VAL   A 1 35  ? 24.526 0.086   11.195  1.00 12.79 ?  35  VAL   A HG11 1 
ATOM   742  H HG12 . VAL   A 1 35  ? 25.666 -1.016  11.285  1.00 12.79 ?  35  VAL   A HG12 1 
ATOM   743  H HG13 . VAL   A 1 35  ? 25.068 -0.606  9.872   1.00 12.79 ?  35  VAL   A HG13 1 
ATOM   744  H HG21 . VAL   A 1 35  ? 22.186 -0.640  10.468  1.00 12.58 ?  35  VAL   A HG21 1 
ATOM   745  H HG22 . VAL   A 1 35  ? 22.767 -1.418  9.211   1.00 12.58 ?  35  VAL   A HG22 1 
ATOM   746  H HG23 . VAL   A 1 35  ? 21.875 -2.186  10.278  1.00 12.58 ?  35  VAL   A HG23 1 
ATOM   747  N N    . VAL   A 1 36  ? 24.048 -3.673  8.159   1.00 8.33  ?  36  VAL   A N    1 
ATOM   748  C CA   . VAL   A 1 36  ? 24.409 -3.669  6.747   1.00 8.16  ?  36  VAL   A CA   1 
ATOM   749  C C    . VAL   A 1 36  ? 23.943 -2.370  6.099   1.00 8.05  ?  36  VAL   A C    1 
ATOM   750  O O    . VAL   A 1 36  ? 22.786 -1.956  6.259   1.00 8.89  ?  36  VAL   A O    1 
ATOM   751  C CB   . VAL   A 1 36  ? 23.796 -4.881  6.024   1.00 8.34  ?  36  VAL   A CB   1 
ATOM   752  C CG1  . VAL   A 1 36  ? 24.044 -4.799  4.532   1.00 8.79  ?  36  VAL   A CG1  1 
ATOM   753  C CG2  . VAL   A 1 36  ? 24.340 -6.188  6.597   1.00 8.98  ?  36  VAL   A CG2  1 
ATOM   754  H H    . VAL   A 1 36  ? 23.261 -4.002  8.313   1.00 10.00 ?  36  VAL   A H    1 
ATOM   755  H HA   . VAL   A 1 36  ? 25.377 -3.725  6.666   1.00 9.80  ?  36  VAL   A HA   1 
ATOM   756  H HB   . VAL   A 1 36  ? 22.841 -4.873  6.163   1.00 10.01 ?  36  VAL   A HB   1 
ATOM   757  H HG11 . VAL   A 1 36  ? 23.898 -5.672  4.142   1.00 10.56 ?  36  VAL   A HG11 1 
ATOM   758  H HG12 . VAL   A 1 36  ? 23.428 -4.156  4.144   1.00 10.56 ?  36  VAL   A HG12 1 
ATOM   759  H HG13 . VAL   A 1 36  ? 24.960 -4.516  4.379   1.00 10.56 ?  36  VAL   A HG13 1 
ATOM   760  H HG21 . VAL   A 1 36  ? 23.952 -6.936  6.114   1.00 10.79 ?  36  VAL   A HG21 1 
ATOM   761  H HG22 . VAL   A 1 36  ? 25.308 -6.204  6.501   1.00 10.79 ?  36  VAL   A HG22 1 
ATOM   762  H HG23 . VAL   A 1 36  ? 24.105 -6.247  7.538   1.00 10.79 ?  36  VAL   A HG23 1 
ATOM   763  N N    . ASN   A 1 37  ? 24.842 -1.748  5.340   1.00 7.97  ?  37  ASN   A N    1 
ATOM   764  C CA   . ASN   A 1 37  ? 24.513 -0.616  4.486   1.00 7.69  ?  37  ASN   A CA   1 
ATOM   765  C C    . ASN   A 1 37  ? 24.365 -1.070  3.040   1.00 7.91  ?  37  ASN   A C    1 
ATOM   766  O O    . ASN   A 1 37  ? 25.140 -1.901  2.547   1.00 8.35  ?  37  ASN   A O    1 
ATOM   767  C CB   . ASN   A 1 37  ? 25.598 0.455   4.568   1.00 8.29  ?  37  ASN   A CB   1 
ATOM   768  C CG   . ASN   A 1 37  ? 25.269 1.672   3.731   1.00 8.49  ?  37  ASN   A CG   1 
ATOM   769  O OD1  . ASN   A 1 37  ? 24.094 2.021   3.573   1.00 9.07  ?  37  ASN   A OD1  1 
ATOM   770  N ND2  . ASN   A 1 37  ? 26.296 2.322   3.197   1.00 8.72  ?  37  ASN   A ND2  1 
ATOM   771  H H    . ASN   A 1 37  ? 25.674 -1.974  5.298   1.00 9.58  ?  37  ASN   A H    1 
ATOM   772  H HA   . ASN   A 1 37  ? 23.679 -0.224  4.778   1.00 9.24  ?  37  ASN   A HA   1 
ATOM   773  H HB2  . ASN   A 1 37  ? 25.696 0.747   5.490   1.00 9.95  ?  37  ASN   A HB2  1 
ATOM   774  H HB3  . ASN   A 1 37  ? 26.442 0.089   4.249   1.00 9.95  ?  37  ASN   A HB3  1 
ATOM   775  H HD21 . ASN   A 1 37  ? 26.152 3.017   2.706   1.00 10.48 ?  37  ASN   A HD21 1 
ATOM   776  H HD22 . ASN   A 1 37  ? 27.094 2.054   3.327   1.00 10.48 ?  37  ASN   A HD22 1 
ATOM   777  N N    A ALA   A 1 38  ? 23.355 -0.506  2.372   0.86 8.37  ?  38  ALA   A N    1 
ATOM   778  N N    B ALA   A 1 38  ? 23.372 -0.500  2.352   0.14 8.23  ?  38  ALA   A N    1 
ATOM   779  C CA   A ALA   A 1 38  ? 23.138 -0.643  0.933   0.86 8.62  ?  38  ALA   A CA   1 
ATOM   780  C CA   B ALA   A 1 38  ? 23.172 -0.736  0.921   0.14 8.59  ?  38  ALA   A CA   1 
ATOM   781  C C    A ALA   A 1 38  ? 24.061 0.343   0.219   0.86 8.46  ?  38  ALA   A C    1 
ATOM   782  C C    B ALA   A 1 38  ? 24.036 0.265   0.154   0.14 8.47  ?  38  ALA   A C    1 
ATOM   783  O O    A ALA   A 1 38  ? 23.660 1.438   -0.192  0.86 8.93  ?  38  ALA   A O    1 
ATOM   784  O O    B ALA   A 1 38  ? 23.573 1.285   -0.363  0.14 8.49  ?  38  ALA   A O    1 
ATOM   785  C CB   A ALA   A 1 38  ? 21.675 -0.370  0.598   0.86 10.10 ?  38  ALA   A CB   1 
ATOM   786  C CB   B ALA   A 1 38  ? 21.696 -0.623  0.561   0.14 9.15  ?  38  ALA   A CB   1 
ATOM   787  H H    A ALA   A 1 38  ? 22.761 -0.016  2.753   0.86 10.05 ?  38  ALA   A H    1 
ATOM   788  H H    B ALA   A 1 38  ? 22.795 0.038   2.697   0.14 9.88  ?  38  ALA   A H    1 
ATOM   789  H HA   A ALA   A 1 38  ? 23.364 -1.542  0.648   0.86 10.35 ?  38  ALA   A HA   1 
ATOM   790  H HA   B ALA   A 1 38  ? 23.468 -1.635  0.702   0.14 10.31 ?  38  ALA   A HA   1 
ATOM   791  H HB1  A ALA   A 1 38  ? 21.544 -0.468  -0.358  0.86 12.13 ?  38  ALA   A HB1  1 
ATOM   792  H HB1  B ALA   A 1 38  ? 21.591 -0.776  -0.389  0.14 10.98 ?  38  ALA   A HB1  1 
ATOM   793  H HB2  A ALA   A 1 38  ? 21.119 -1.011  1.073   0.86 12.13 ?  38  ALA   A HB2  1 
ATOM   794  H HB2  B ALA   A 1 38  ? 21.194 -1.288  1.062   0.14 10.98 ?  38  ALA   A HB2  1 
ATOM   795  H HB3  A ALA   A 1 38  ? 21.448 0.530   0.875   0.86 12.13 ?  38  ALA   A HB3  1 
ATOM   796  H HB3  B ALA   A 1 38  ? 21.386 0.265   0.787   0.14 10.98 ?  38  ALA   A HB3  1 
ATOM   797  N N    . ALA   A 1 39  ? 25.325 -0.053  0.085   1.00 8.56  ?  39  ALA   A N    1 
ATOM   798  C CA   . ALA   A 1 39  ? 26.366 0.828   -0.416  1.00 8.71  ?  39  ALA   A CA   1 
ATOM   799  C C    . ALA   A 1 39  ? 26.490 0.766   -1.936  1.00 8.53  ?  39  ALA   A C    1 
ATOM   800  O O    . ALA   A 1 39  ? 25.993 -0.147  -2.599  1.00 8.87  ?  39  ALA   A O    1 
ATOM   801  C CB   . ALA   A 1 39  ? 27.702 0.424   0.212   1.00 9.60  ?  39  ALA   A CB   1 
ATOM   802  H H    A ALA   A 1 39  ? 25.603 -0.847  0.274   0.86 10.28 ?  39  ALA   A H    1 
ATOM   803  H H    B ALA   A 1 39  ? 25.633 -0.817  0.339   0.14 10.28 ?  39  ALA   A H    1 
ATOM   804  H HA   . ALA   A 1 39  ? 26.162 1.743   -0.158  1.00 10.46 ?  39  ALA   A HA   1 
ATOM   805  H HB1  . ALA   A 1 39  ? 28.392 1.018   -0.120  1.00 11.53 ?  39  ALA   A HB1  1 
ATOM   806  H HB2  . ALA   A 1 39  ? 27.630 0.510   1.178   1.00 11.53 ?  39  ALA   A HB2  1 
ATOM   807  H HB3  . ALA   A 1 39  ? 27.898 -0.489  -0.028  1.00 11.53 ?  39  ALA   A HB3  1 
ATOM   808  N N    A ASN   A 1 40  ? 27.176 1.771   -2.485  0.86 9.27  ?  40  ASN   A N    1 
ATOM   809  N N    B ASN   A 1 40  ? 27.198 1.748   -2.483  0.14 8.76  ?  40  ASN   A N    1 
ATOM   810  C CA   A ASN   A 1 40  ? 27.697 1.730   -3.845  0.86 9.49  ?  40  ASN   A CA   1 
ATOM   811  C CA   B ASN   A 1 40  ? 27.621 1.748   -3.876  0.14 8.88  ?  40  ASN   A CA   1 
ATOM   812  C C    A ASN   A 1 40  ? 29.224 1.634   -3.799  0.86 8.76  ?  40  ASN   A C    1 
ATOM   813  C C    B ASN   A 1 40  ? 29.140 1.614   -3.941  0.14 9.24  ?  40  ASN   A C    1 
ATOM   814  O O    A ASN   A 1 40  ? 29.839 1.745   -2.737  0.86 8.77  ?  40  ASN   A O    1 
ATOM   815  O O    B ASN   A 1 40  ? 29.830 1.578   -2.919  0.14 9.15  ?  40  ASN   A O    1 
ATOM   816  C CB   A ASN   A 1 40  ? 27.202 2.919   -4.687  0.86 10.28 ?  40  ASN   A CB   1 
ATOM   817  C CB   B ASN   A 1 40  ? 27.121 2.996   -4.607  0.14 8.61  ?  40  ASN   A CB   1 
ATOM   818  C CG   A ASN   A 1 40  ? 27.592 4.267   -4.108  0.86 10.69 ?  40  ASN   A CG   1 
ATOM   819  C CG   B ASN   A 1 40  ? 27.263 4.258   -3.782  0.14 8.44  ?  40  ASN   A CG   1 
ATOM   820  O OD1  A ASN   A 1 40  ? 28.765 4.528   -3.821  0.86 11.16 ?  40  ASN   A OD1  1 
ATOM   821  O OD1  B ASN   A 1 40  ? 28.146 4.368   -2.929  0.14 7.79  ?  40  ASN   A OD1  1 
ATOM   822  N ND2  A ASN   A 1 40  ? 26.596 5.133   -3.927  0.86 11.94 ?  40  ASN   A ND2  1 
ATOM   823  N ND2  B ASN   A 1 40  ? 26.384 5.219   -4.029  0.14 8.85  ?  40  ASN   A ND2  1 
ATOM   824  H H    A ASN   A 1 40  ? 27.357 2.501   -2.074  0.86 11.14 ?  40  ASN   A H    1 
ATOM   825  H H    B ASN   A 1 40  ? 27.459 2.441   -2.046  0.14 10.53 ?  40  ASN   A H    1 
ATOM   826  H HA   A ASN   A 1 40  ? 27.371 0.924   -4.273  0.86 11.39 ?  40  ASN   A HA   1 
ATOM   827  H HA   B ASN   A 1 40  ? 27.240 0.973   -4.319  0.14 10.66 ?  40  ASN   A HA   1 
ATOM   828  H HB2  A ASN   A 1 40  ? 27.580 2.851   -5.579  0.86 12.35 ?  40  ASN   A HB2  1 
ATOM   829  H HB2  B ASN   A 1 40  ? 27.635 3.112   -5.421  0.14 10.35 ?  40  ASN   A HB2  1 
ATOM   830  H HB3  A ASN   A 1 40  ? 26.232 2.884   -4.740  0.86 12.35 ?  40  ASN   A HB3  1 
ATOM   831  H HB3  B ASN   A 1 40  ? 26.183 2.877   -4.823  0.14 10.35 ?  40  ASN   A HB3  1 
ATOM   832  H HD21 A ASN   A 1 40  ? 26.762 5.919   -3.611  0.86 14.34 ?  40  ASN   A HD21 1 
ATOM   833  H HD21 B ASN   A 1 40  ? 26.419 5.955   -3.588  0.14 10.62 ?  40  ASN   A HD21 1 
ATOM   834  H HD22 A ASN   A 1 40  ? 25.791 4.921   -4.141  0.86 14.34 ?  40  ASN   A HD22 1 
ATOM   835  H HD22 B ASN   A 1 40  ? 25.785 5.107   -4.636  0.14 10.62 ?  40  ASN   A HD22 1 
ATOM   836  N N    A VAL   A 1 41  ? 29.834 1.382   -4.962  0.86 9.14  ?  41  VAL   A N    1 
ATOM   837  N N    B VAL   A 1 41  ? 29.663 1.535   -5.166  0.14 9.70  ?  41  VAL   A N    1 
ATOM   838  C CA   A VAL   A 1 41  ? 31.266 1.078   -5.002  0.86 9.69  ?  41  VAL   A CA   1 
ATOM   839  C CA   B VAL   A 1 41  ? 31.084 1.246   -5.336  0.14 9.90  ?  41  VAL   A CA   1 
ATOM   840  C C    A VAL   A 1 41  ? 32.130 2.232   -4.528  0.86 9.74  ?  41  VAL   A C    1 
ATOM   841  C C    B VAL   A 1 41  ? 31.959 2.372   -4.799  0.14 10.44 ?  41  VAL   A C    1 
ATOM   842  O O    A VAL   A 1 41  ? 33.282 2.008   -4.135  0.86 10.27 ?  41  VAL   A O    1 
ATOM   843  O O    B VAL   A 1 41  ? 33.073 2.121   -4.322  0.14 10.59 ?  41  VAL   A O    1 
ATOM   844  C CB   A VAL   A 1 41  ? 31.744 0.592   -6.392  0.86 10.20 ?  41  VAL   A CB   1 
ATOM   845  C CB   B VAL   A 1 41  ? 31.418 0.900   -6.799  0.14 9.78  ?  41  VAL   A CB   1 
ATOM   846  C CG1  A VAL   A 1 41  ? 31.068 -0.720  -6.770  0.86 10.80 ?  41  VAL   A CG1  1 
ATOM   847  C CG1  B VAL   A 1 41  ? 30.839 -0.456  -7.166  0.14 9.76  ?  41  VAL   A CG1  1 
ATOM   848  C CG2  A VAL   A 1 41  ? 31.559 1.667   -7.478  0.86 11.04 ?  41  VAL   A CG2  1 
ATOM   849  C CG2  B VAL   A 1 41  ? 30.911 1.983   -7.739  0.14 9.92  ?  41  VAL   A CG2  1 
ATOM   850  H H    A VAL   A 1 41  ? 29.446 1.375   -5.730  0.86 10.98 ?  41  VAL   A H    1 
ATOM   851  H H    B VAL   A 1 41  ? 29.217 1.637   -5.894  0.14 11.65 ?  41  VAL   A H    1 
ATOM   852  H HA   A VAL   A 1 41  ? 31.428 0.346   -4.388  0.86 11.63 ?  41  VAL   A HA   1 
ATOM   853  H HA   B VAL   A 1 41  ? 31.288 0.462   -4.808  0.14 11.89 ?  41  VAL   A HA   1 
ATOM   854  H HB   A VAL   A 1 41  ? 32.695 0.410   -6.334  0.86 12.25 ?  41  VAL   A HB   1 
ATOM   855  H HB   B VAL   A 1 41  ? 32.381 0.848   -6.897  0.14 11.75 ?  41  VAL   A HB   1 
ATOM   856  H HG11 A VAL   A 1 41  ? 31.402 -1.013  -7.634  0.86 12.97 ?  41  VAL   A HG11 1 
ATOM   857  H HG11 B VAL   A 1 41  ? 31.001 -0.624  -8.106  0.14 11.72 ?  41  VAL   A HG11 1 
ATOM   858  H HG12 A VAL   A 1 41  ? 31.273 -1.389  -6.096  0.86 12.97 ?  41  VAL   A HG12 1 
ATOM   859  H HG12 B VAL   A 1 41  ? 31.274 -1.138  -6.628  0.14 11.72 ?  41  VAL   A HG12 1 
ATOM   860  H HG13 A VAL   A 1 41  ? 30.109 -0.582  -6.817  0.86 12.97 ?  41  VAL   A HG13 1 
ATOM   861  H HG13 B VAL   A 1 41  ? 29.888 -0.453  -6.987  0.14 11.72 ?  41  VAL   A HG13 1 
ATOM   862  H HG21 A VAL   A 1 41  ? 31.809 1.289   -8.339  0.86 13.25 ?  41  VAL   A HG21 1 
ATOM   863  H HG21 B VAL   A 1 41  ? 31.289 1.832   -8.619  0.14 11.92 ?  41  VAL   A HG21 1 
ATOM   864  H HG22 A VAL   A 1 41  ? 30.633 1.944   -7.494  0.86 13.25 ?  41  VAL   A HG22 1 
ATOM   865  H HG22 B VAL   A 1 41  ? 29.944 1.940   -7.785  0.14 11.92 ?  41  VAL   A HG22 1 
ATOM   866  H HG23 A VAL   A 1 41  ? 32.131 2.423   -7.273  0.86 13.25 ?  41  VAL   A HG23 1 
ATOM   867  H HG23 B VAL   A 1 41  ? 31.191 2.847   -7.403  0.14 11.92 ?  41  VAL   A HG23 1 
ATOM   868  N N    A TYR   A 1 42  ? 31.620 3.466   -4.598  0.86 9.61  ?  42  TYR   A N    1 
ATOM   869  N N    B TYR   A 1 42  ? 31.494 3.619   -4.868  0.14 10.67 ?  42  TYR   A N    1 
ATOM   870  C CA   A TYR   A 1 42  ? 32.352 4.656   -4.182  0.86 9.79  ?  42  TYR   A CA   1 
ATOM   871  C CA   B TYR   A 1 42  ? 32.283 4.749   -4.389  0.14 11.11 ?  42  TYR   A CA   1 
ATOM   872  C C    A TYR   A 1 42  ? 32.099 5.020   -2.727  0.86 9.45  ?  42  TYR   A C    1 
ATOM   873  C C    B TYR   A 1 42  ? 31.959 5.139   -2.954  0.14 10.67 ?  42  TYR   A C    1 
ATOM   874  O O    A TYR   A 1 42  ? 32.665 6.003   -2.231  0.86 10.14 ?  42  TYR   A O    1 
ATOM   875  O O    B TYR   A 1 42  ? 32.522 6.118   -2.452  0.14 10.71 ?  42  TYR   A O    1 
ATOM   876  C CB   A TYR   A 1 42  ? 32.001 5.846   -5.099  0.86 10.66 ?  42  TYR   A CB   1 
ATOM   877  C CB   B TYR   A 1 42  ? 32.108 5.965   -5.304  0.14 12.06 ?  42  TYR   A CB   1 
ATOM   878  C CG   A TYR   A 1 42  ? 32.174 5.542   -6.577  0.86 11.83 ?  42  TYR   A CG   1 
ATOM   879  C CG   B TYR   A 1 42  ? 32.418 5.678   -6.749  0.14 12.93 ?  42  TYR   A CG   1 
ATOM   880  C CD1  A TYR   A 1 42  ? 33.430 5.334   -7.120  0.86 12.43 ?  42  TYR   A CD1  1 
ATOM   881  C CD1  B TYR   A 1 42  ? 33.715 5.406   -7.163  0.14 13.51 ?  42  TYR   A CD1  1 
ATOM   882  C CD2  A TYR   A 1 42  ? 31.076 5.429   -7.420  0.86 13.07 ?  42  TYR   A CD2  1 
ATOM   883  C CD2  B TYR   A 1 42  ? 31.412 5.681   -7.701  0.14 13.45 ?  42  TYR   A CD2  1 
ATOM   884  C CE1  A TYR   A 1 42  ? 33.593 5.040   -8.466  0.86 12.77 ?  42  TYR   A CE1  1 
ATOM   885  C CE1  B TYR   A 1 42  ? 33.997 5.140   -8.489  0.14 13.96 ?  42  TYR   A CE1  1 
ATOM   886  C CE2  A TYR   A 1 42  ? 31.232 5.142   -8.770  0.86 13.99 ?  42  TYR   A CE2  1 
ATOM   887  C CE2  B TYR   A 1 42  ? 31.682 5.419   -9.022  0.14 13.92 ?  42  TYR   A CE2  1 
ATOM   888  C CZ   A TYR   A 1 42  ? 32.494 4.948   -9.286  0.86 13.61 ?  42  TYR   A CZ   1 
ATOM   889  C CZ   B TYR   A 1 42  ? 32.972 5.152   -9.414  0.14 14.14 ?  42  TYR   A CZ   1 
ATOM   890  O OH   A TYR   A 1 42  ? 32.651 4.653   -10.623 0.86 15.10 ?  42  TYR   A OH   1 
ATOM   891  O OH   B TYR   A 1 42  ? 33.228 4.892   -10.738 0.14 14.58 ?  42  TYR   A OH   1 
ATOM   892  H H    A TYR   A 1 42  ? 30.834 3.641   -4.902  0.86 11.54 ?  42  TYR   A H    1 
ATOM   893  H H    B TYR   A 1 42  ? 30.723 3.832   -5.190  0.14 12.81 ?  42  TYR   A H    1 
ATOM   894  H HA   A TYR   A 1 42  ? 33.303 4.490   -4.282  0.86 11.75 ?  42  TYR   A HA   1 
ATOM   895  H HA   B TYR   A 1 42  ? 33.217 4.500   -4.419  0.14 13.34 ?  42  TYR   A HA   1 
ATOM   896  H HB2  A TYR   A 1 42  ? 31.076 6.097   -4.953  0.86 12.80 ?  42  TYR   A HB2  1 
ATOM   897  H HB2  B TYR   A 1 42  ? 31.190 6.270   -5.255  0.14 14.49 ?  42  TYR   A HB2  1 
ATOM   898  H HB3  A TYR   A 1 42  ? 32.583 6.595   -4.884  0.86 12.80 ?  42  TYR   A HB3  1 
ATOM   899  H HB3  B TYR   A 1 42  ? 32.707 6.668   -5.006  0.14 14.49 ?  42  TYR   A HB3  1 
ATOM   900  H HD1  A TYR   A 1 42  ? 34.180 5.392   -6.574  0.86 14.93 ?  42  TYR   A HD1  1 
ATOM   901  H HD1  B TYR   A 1 42  ? 34.405 5.399   -6.537  0.14 16.22 ?  42  TYR   A HD1  1 
ATOM   902  H HD2  A TYR   A 1 42  ? 30.220 5.567   -7.080  0.86 15.69 ?  42  TYR   A HD2  1 
ATOM   903  H HD2  B TYR   A 1 42  ? 30.540 5.863   -7.439  0.14 16.15 ?  42  TYR   A HD2  1 
ATOM   904  H HE1  A TYR   A 1 42  ? 34.448 4.905   -8.814  0.86 15.33 ?  42  TYR   A HE1  1 
ATOM   905  H HE1  B TYR   A 1 42  ? 34.870 4.957   -8.755  0.14 16.76 ?  42  TYR   A HE1  1 
ATOM   906  H HE2  A TYR   A 1 42  ? 30.486 5.078   -9.325  0.86 16.80 ?  42  TYR   A HE2  1 
ATOM   907  H HE2  B TYR   A 1 42  ? 30.996 5.424   -9.648  0.14 16.71 ?  42  TYR   A HE2  1 
ATOM   908  H HH   A TYR   A 1 42  ? 33.469 4.555   -10.801 0.86 18.13 ?  42  TYR   A HH   1 
ATOM   909  H HH   B TYR   A 1 42  ? 33.801 4.287   -10.799 0.14 17.51 ?  42  TYR   A HH   1 
ATOM   910  N N    A LEU   A 1 43  ? 31.257 4.247   -2.036  0.86 9.11  ?  43  LEU   A N    1 
ATOM   911  N N    B LEU   A 1 43  ? 31.071 4.405   -2.286  0.14 10.49 ?  43  LEU   A N    1 
ATOM   912  C CA   A LEU   A 1 43  ? 30.812 4.579   -0.682  0.86 8.74  ?  43  LEU   A CA   1 
ATOM   913  C CA   B LEU   A 1 43  ? 30.706 4.689   -0.900  0.14 10.43 ?  43  LEU   A CA   1 
ATOM   914  C C    A LEU   A 1 43  ? 30.328 6.029   -0.585  0.86 9.07  ?  43  LEU   A C    1 
ATOM   915  C C    B LEU   A 1 43  ? 30.268 6.142   -0.725  0.14 10.63 ?  43  LEU   A C    1 
ATOM   916  O O    A LEU   A 1 43  ? 30.588 6.728   0.397   0.86 10.12 ?  43  LEU   A O    1 
ATOM   917  O O    B LEU   A 1 43  ? 30.655 6.821   0.227   0.14 10.59 ?  43  LEU   A O    1 
ATOM   918  C CB   A LEU   A 1 43  ? 31.872 4.271   0.376   0.86 8.96  ?  43  LEU   A CB   1 
ATOM   919  C CB   B LEU   A 1 43  ? 31.836 4.327   0.068   0.14 10.17 ?  43  LEU   A CB   1 
ATOM   920  C CG   A LEU   A 1 43  ? 32.357 2.818   0.470   0.86 9.25  ?  43  LEU   A CG   1 
ATOM   921  C CG   B LEU   A 1 43  ? 32.275 2.860   0.086   0.14 9.83  ?  43  LEU   A CG   1 
ATOM   922  C CD1  A LEU   A 1 43  ? 33.411 2.709   1.568   0.86 10.05 ?  43  LEU   A CD1  1 
ATOM   923  C CD1  B LEU   A 1 43  ? 33.444 2.673   1.041   0.14 9.70  ?  43  LEU   A CD1  1 
ATOM   924  C CD2  A LEU   A 1 43  ? 31.218 1.835   0.709   0.86 9.96  ?  43  LEU   A CD2  1 
ATOM   925  C CD2  B LEU   A 1 43  ? 31.117 1.949   0.468   0.14 9.67  ?  43  LEU   A CD2  1 
ATOM   926  H H    A LEU   A 1 43  ? 30.922 3.509   -2.332  0.86 10.94 ?  43  LEU   A H    1 
ATOM   927  H H    B LEU   A 1 43  ? 30.656 3.732   -2.620  0.14 12.60 ?  43  LEU   A H    1 
ATOM   928  H HA   A LEU   A 1 43  ? 30.048 4.018   -0.480  0.86 10.50 ?  43  LEU   A HA   1 
ATOM   929  H HA   B LEU   A 1 43  ? 29.948 4.133   -0.673  0.14 12.52 ?  43  LEU   A HA   1 
ATOM   930  H HB2  A LEU   A 1 43  ? 32.648 4.823   0.201   0.86 10.76 ?  43  LEU   A HB2  1 
ATOM   931  H HB2  B LEU   A 1 43  ? 32.613 4.858   -0.159  0.14 12.21 ?  43  LEU   A HB2  1 
ATOM   932  H HB3  A LEU   A 1 43  ? 31.503 4.500   1.243   0.86 10.76 ?  43  LEU   A HB3  1 
ATOM   933  H HB3  B LEU   A 1 43  ? 31.545 4.549   0.967   0.14 12.21 ?  43  LEU   A HB3  1 
ATOM   934  H HG   A LEU   A 1 43  ? 32.785 2.581   -0.367  0.86 11.10 ?  43  LEU   A HG   1 
ATOM   935  H HG   B LEU   A 1 43  ? 32.573 2.609   -0.802  0.14 11.81 ?  43  LEU   A HG   1 
ATOM   936  H HD11 A LEU   A 1 43  ? 33.718 1.792   1.626   0.86 12.07 ?  43  LEU   A HD11 1 
ATOM   937  H HD11 B LEU   A 1 43  ? 33.708 1.740   1.038   0.14 11.64 ?  43  LEU   A HD11 1 
ATOM   938  H HD12 A LEU   A 1 43  ? 34.157 3.294   1.354   0.86 12.07 ?  43  LEU   A HD12 1 
ATOM   939  H HD12 B LEU   A 1 43  ? 34.184 3.227   0.748   0.14 11.64 ?  43  LEU   A HD12 1 
ATOM   940  H HD13 A LEU   A 1 43  ? 33.017 2.979   2.415   0.86 12.07 ?  43  LEU   A HD13 1 
ATOM   941  H HD13 B LEU   A 1 43  ? 33.167 2.936   1.934   0.14 11.64 ?  43  LEU   A HD13 1 
ATOM   942  H HD21 A LEU   A 1 43  ? 31.592 0.950   0.847   0.86 11.96 ?  43  LEU   A HD21 1 
ATOM   943  H HD21 B LEU   A 1 43  ? 31.454 1.050   0.604   0.14 11.61 ?  43  LEU   A HD21 1 
ATOM   944  H HD22 A LEU   A 1 43  ? 30.724 2.111   1.497   0.86 11.96 ?  43  LEU   A HD22 1 
ATOM   945  H HD22 B LEU   A 1 43  ? 30.713 2.278   1.286   0.14 11.61 ?  43  LEU   A HD22 1 
ATOM   946  H HD23 A LEU   A 1 43  ? 30.637 1.833   -0.065  0.86 11.96 ?  43  LEU   A HD23 1 
ATOM   947  H HD23 B LEU   A 1 43  ? 30.464 1.953   -0.249  0.14 11.61 ?  43  LEU   A HD23 1 
ATOM   948  N N    A LYS   A 1 44  ? 29.592 6.473   -1.608  0.86 9.09  ?  44  LYS   A N    1 
ATOM   949  N N    B LYS   A 1 44  ? 29.452 6.624   -1.662  0.14 11.05 ?  44  LYS   A N    1 
ATOM   950  C CA   A LYS   A 1 44  ? 28.947 7.788   -1.608  0.86 9.43  ?  44  LYS   A CA   1 
ATOM   951  C CA   B LYS   A 1 44  ? 28.846 7.951   -1.579  0.14 11.66 ?  44  LYS   A CA   1 
ATOM   952  C C    A LYS   A 1 44  ? 27.522 7.592   -1.103  0.86 8.99  ?  44  LYS   A C    1 
ATOM   953  C C    B LYS   A 1 44  ? 27.436 7.769   -1.030  0.14 10.97 ?  44  LYS   A C    1 
ATOM   954  O O    A LYS   A 1 44  ? 26.656 7.075   -1.813  0.86 9.75  ?  44  LYS   A O    1 
ATOM   955  O O    B LYS   A 1 44  ? 26.509 7.425   -1.767  0.14 10.84 ?  44  LYS   A O    1 
ATOM   956  C CB   A LYS   A 1 44  ? 28.987 8.417   -2.995  0.86 11.63 ?  44  LYS   A CB   1 
ATOM   957  C CB   B LYS   A 1 44  ? 28.828 8.630   -2.945  0.14 13.17 ?  44  LYS   A CB   1 
ATOM   958  C CG   A LYS   A 1 44  ? 30.367 8.912   -3.413  0.86 14.95 ?  44  LYS   A CG   1 
ATOM   959  C CG   B LYS   A 1 44  ? 30.204 8.882   -3.542  0.14 14.65 ?  44  LYS   A CG   1 
ATOM   960  C CD   A LYS   A 1 44  ? 31.027 9.803   -2.361  0.86 20.87 ?  44  LYS   A CD   1 
ATOM   961  C CD   B LYS   A 1 44  ? 31.146 9.535   -2.542  0.14 16.21 ?  44  LYS   A CD   1 
ATOM   962  C CE   A LYS   A 1 44  ? 32.333 10.382  -2.877  0.86 24.24 ?  44  LYS   A CE   1 
ATOM   963  C CE   B LYS   A 1 44  ? 32.403 10.044  -3.225  0.14 17.08 ?  44  LYS   A CE   1 
ATOM   964  N NZ   A LYS   A 1 44  ? 33.176 10.941  -1.787  0.86 25.82 ?  44  LYS   A NZ   1 
ATOM   965  N NZ   B LYS   A 1 44  ? 33.452 10.437  -2.245  0.14 17.35 ?  44  LYS   A NZ   1 
ATOM   966  H H    A LYS   A 1 44  ? 29.451 6.017   -2.325  0.86 10.91 ?  44  LYS   A H    1 
ATOM   967  H H    B LYS   A 1 44  ? 29.231 6.192   -2.372  0.14 13.27 ?  44  LYS   A H    1 
ATOM   968  H HA   A LYS   A 1 44  ? 29.401 8.365   -0.978  0.86 11.32 ?  44  LYS   A HA   1 
ATOM   969  H HA   B LYS   A 1 44  ? 29.342 8.502   -0.956  0.14 14.00 ?  44  LYS   A HA   1 
ATOM   970  H HB2  A LYS   A 1 44  ? 28.702 7.760   -3.647  0.86 13.96 ?  44  LYS   A HB2  1 
ATOM   971  H HB2  B LYS   A 1 44  ? 28.338 8.068   -3.565  0.14 15.82 ?  44  LYS   A HB2  1 
ATOM   972  H HB3  A LYS   A 1 44  ? 28.387 9.178   -3.009  0.86 13.96 ?  44  LYS   A HB3  1 
ATOM   973  H HB3  B LYS   A 1 44  ? 28.382 9.487   -2.860  0.14 15.82 ?  44  LYS   A HB3  1 
ATOM   974  H HG2  A LYS   A 1 44  ? 30.945 8.150   -3.568  0.86 17.95 ?  44  LYS   A HG2  1 
ATOM   975  H HG2  B LYS   A 1 44  ? 30.592 8.038   -3.817  0.14 17.59 ?  44  LYS   A HG2  1 
ATOM   976  H HG3  A LYS   A 1 44  ? 30.282 9.434   -4.230  0.86 17.95 ?  44  LYS   A HG3  1 
ATOM   977  H HG3  B LYS   A 1 44  ? 30.116 9.476   -4.305  0.14 17.59 ?  44  LYS   A HG3  1 
ATOM   978  H HD2  A LYS   A 1 44  ? 30.425 10.527  -2.133  0.86 25.06 ?  44  LYS   A HD2  1 
ATOM   979  H HD2  B LYS   A 1 44  ? 30.696 10.286  -2.120  0.14 19.46 ?  44  LYS   A HD2  1 
ATOM   980  H HD3  A LYS   A 1 44  ? 31.226 9.268   -1.574  0.86 25.06 ?  44  LYS   A HD3  1 
ATOM   981  H HD3  B LYS   A 1 44  ? 31.406 8.881   -1.873  0.14 19.46 ?  44  LYS   A HD3  1 
ATOM   982  H HE2  A LYS   A 1 44  ? 32.837 9.678   -3.317  0.86 29.09 ?  44  LYS   A HE2  1 
ATOM   983  H HE2  B LYS   A 1 44  ? 32.763 9.345   -3.792  0.14 20.50 ?  44  LYS   A HE2  1 
ATOM   984  H HE3  A LYS   A 1 44  ? 32.135 11.092  -3.504  0.86 29.09 ?  44  LYS   A HE3  1 
ATOM   985  H HE3  B LYS   A 1 44  ? 32.180 10.824  -3.759  0.14 20.50 ?  44  LYS   A HE3  1 
ATOM   986  H HZ1  A LYS   A 1 44  ? 33.931 11.270  -2.126  0.86 30.99 ?  44  LYS   A HZ1  1 
ATOM   987  H HZ1  B LYS   A 1 44  ? 33.147 11.084  -1.715  0.14 20.82 ?  44  LYS   A HZ1  1 
ATOM   988  H HZ2  A LYS   A 1 44  ? 32.739 11.597  -1.371  0.86 30.99 ?  44  LYS   A HZ2  1 
ATOM   989  H HZ2  B LYS   A 1 44  ? 33.678 9.736   -1.745  0.14 20.82 ?  44  LYS   A HZ2  1 
ATOM   990  H HZ3  A LYS   A 1 44  ? 33.375 10.307  -1.197  0.86 30.99 ?  44  LYS   A HZ3  1 
ATOM   991  H HZ3  B LYS   A 1 44  ? 34.174 10.731  -2.674  0.14 20.82 ?  44  LYS   A HZ3  1 
ATOM   992  N N    A HIS   A 1 45  ? 27.289 7.986   0.142   0.86 8.75  ?  45  HIS   A N    1 
ATOM   993  N N    B HIS   A 1 45  ? 27.277 8.007   0.271   0.14 10.72 ?  45  HIS   A N    1 
ATOM   994  C CA   A HIS   A 1 45  ? 26.059 7.632   0.846   0.86 8.77  ?  45  HIS   A CA   1 
ATOM   995  C CA   B HIS   A 1 45  ? 26.002 7.784   0.950   0.14 10.50 ?  45  HIS   A CA   1 
ATOM   996  C C    A HIS   A 1 45  ? 25.021 8.747   0.702   0.86 9.53  ?  45  HIS   A C    1 
ATOM   997  C C    B HIS   A 1 45  ? 25.120 9.009   0.731   0.14 10.89 ?  45  HIS   A C    1 
ATOM   998  O O    A HIS   A 1 45  ? 24.689 9.461   1.648   0.86 10.54 ?  45  HIS   A O    1 
ATOM   999  O O    B HIS   A 1 45  ? 25.037 9.920   1.558   0.14 11.11 ?  45  HIS   A O    1 
ATOM   1000 C CB   A HIS   A 1 45  ? 26.365 7.357   2.308   0.86 8.81  ?  45  HIS   A CB   1 
ATOM   1001 C CB   B HIS   A 1 45  ? 26.231 7.510   2.429   0.14 10.00 ?  45  HIS   A CB   1 
ATOM   1002 C CG   A HIS   A 1 45  ? 27.479 6.384   2.519   0.86 8.24  ?  45  HIS   A CG   1 
ATOM   1003 C CG   B HIS   A 1 45  ? 27.384 6.596   2.699   0.14 9.37  ?  45  HIS   A CG   1 
ATOM   1004 N ND1  A HIS   A 1 45  ? 27.460 5.097   2.018   0.86 8.65  ?  45  HIS   A ND1  1 
ATOM   1005 N ND1  B HIS   A 1 45  ? 27.459 5.322   2.179   0.14 9.35  ?  45  HIS   A ND1  1 
ATOM   1006 C CD2  A HIS   A 1 45  ? 28.654 6.523   3.181   0.86 8.79  ?  45  HIS   A CD2  1 
ATOM   1007 C CD2  B HIS   A 1 45  ? 28.510 6.774   3.429   0.14 8.70  ?  45  HIS   A CD2  1 
ATOM   1008 C CE1  A HIS   A 1 45  ? 28.586 4.493   2.365   0.86 8.50  ?  45  HIS   A CE1  1 
ATOM   1009 C CE1  B HIS   A 1 45  ? 28.583 4.753   2.579   0.14 8.41  ?  45  HIS   A CE1  1 
ATOM   1010 N NE2  A HIS   A 1 45  ? 29.323 5.331   3.075   0.86 8.80  ?  45  HIS   A NE2  1 
ATOM   1011 N NE2  B HIS   A 1 45  ? 29.238 5.612   3.339   0.14 8.06  ?  45  HIS   A NE2  1 
ATOM   1012 H H    A HIS   A 1 45  ? 27.831 8.467   0.610   0.86 10.51 ?  45  HIS   A H    1 
ATOM   1013 H H    B HIS   A 1 45  ? 27.896 8.308   0.787   0.14 12.87 ?  45  HIS   A H    1 
ATOM   1014 H HA   A HIS   A 1 45  ? 25.690 6.822   0.458   0.86 10.53 ?  45  HIS   A HA   1 
ATOM   1015 H HA   B HIS   A 1 45  ? 25.561 7.014   0.560   0.14 12.61 ?  45  HIS   A HA   1 
ATOM   1016 H HB2  A HIS   A 1 45  ? 26.610 8.191   2.738   0.86 10.58 ?  45  HIS   A HB2  1 
ATOM   1017 H HB2  B HIS   A 1 45  ? 26.402 8.349   2.883   0.14 12.01 ?  45  HIS   A HB2  1 
ATOM   1018 H HB3  A HIS   A 1 45  ? 25.569 6.992   2.731   0.86 10.58 ?  45  HIS   A HB3  1 
ATOM   1019 H HB3  B HIS   A 1 45  ? 25.436 7.095   2.794   0.14 12.01 ?  45  HIS   A HB3  1 
ATOM   1020 H HD2  A HIS   A 1 45  ? 28.957 7.286   3.623   0.86 10.56 ?  45  HIS   A HD2  1 
ATOM   1021 H HD2  B HIS   A 1 45  ? 28.744 7.540   3.903   0.14 10.45 ?  45  HIS   A HD2  1 
ATOM   1022 H HE1  A HIS   A 1 45  ? 28.810 3.612   2.160   0.86 10.21 ?  45  HIS   A HE1  1 
ATOM   1023 H HE1  B HIS   A 1 45  ? 28.862 3.894   2.363   0.14 10.10 ?  45  HIS   A HE1  1 
ATOM   1024 H HE2  A HIS   A 1 45  ? 30.097 5.155   3.409   0.86 10.57 ?  45  HIS   A HE2  1 
ATOM   1025 H HE2  B HIS   A 1 45  ? 29.996 5.470   3.716   0.14 9.68  ?  45  HIS   A HE2  1 
ATOM   1026 N N    A GLY   A 1 46  ? 24.487 8.871   -0.510  0.86 10.68 ?  46  GLY   A N    1 
ATOM   1027 N N    B GLY   A 1 46  ? 24.452 9.025   -0.418  0.14 11.11 ?  46  GLY   A N    1 
ATOM   1028 C CA   A GLY   A 1 46  ? 23.679 10.031  -0.845  0.86 11.54 ?  46  GLY   A CA   1 
ATOM   1029 C CA   B GLY   A 1 46  ? 23.614 10.150  -0.776  0.14 11.15 ?  46  GLY   A CA   1 
ATOM   1030 C C    A GLY   A 1 46  ? 22.194 9.923   -0.554  0.86 11.26 ?  46  GLY   A C    1 
ATOM   1031 C C    B GLY   A 1 46  ? 22.144 9.941   -0.483  0.14 10.94 ?  46  GLY   A C    1 
ATOM   1032 O O    A GLY   A 1 46  ? 21.539 10.922  -0.241  0.86 12.44 ?  46  GLY   A O    1 
ATOM   1033 O O    B GLY   A 1 46  ? 21.454 10.878  -0.071  0.14 10.92 ?  46  GLY   A O    1 
ATOM   1034 H H    A GLY   A 1 46  ? 24.564 8.298   -1.144  0.86 12.82 ?  46  GLY   A H    1 
ATOM   1035 H H    B GLY   A 1 46  ? 24.473 8.398   -1.007  0.14 13.34 ?  46  GLY   A H    1 
ATOM   1036 H HA2  A GLY   A 1 46  ? 24.013 10.798  -0.354  0.86 13.86 ?  46  GLY   A HA2  1 
ATOM   1037 H HA2  B GLY   A 1 46  ? 23.908 10.937  -0.292  0.14 13.38 ?  46  GLY   A HA2  1 
ATOM   1038 H HA3  A GLY   A 1 46  ? 23.774 10.216  -1.790  0.86 13.86 ?  46  GLY   A HA3  1 
ATOM   1039 H HA3  B GLY   A 1 46  ? 23.706 10.325  -1.723  0.14 13.38 ?  46  GLY   A HA3  1 
ATOM   1040 N N    . GLY   A 1 47  ? 21.646 8.724   -0.686  1.00 11.15 ?  47  GLY   A N    1 
ATOM   1041 C CA   . GLY   A 1 47  ? 20.216 8.512   -0.587  1.00 11.54 ?  47  GLY   A CA   1 
ATOM   1042 C C    . GLY   A 1 47  ? 19.897 7.069   -0.260  1.00 10.67 ?  47  GLY   A C    1 
ATOM   1043 O O    . GLY   A 1 47  ? 20.791 6.240   -0.077  1.00 10.73 ?  47  GLY   A O    1 
ATOM   1044 H H    A GLY   A 1 47  ? 22.091 8.005   -0.830  0.86 13.39 ?  47  GLY   A H    1 
ATOM   1045 H H    B GLY   A 1 47  ? 22.104 8.023   -0.873  0.14 13.39 ?  47  GLY   A H    1 
ATOM   1046 H HA2  . GLY   A 1 47  ? 19.841 9.076   0.110   1.00 13.86 ?  47  GLY   A HA2  1 
ATOM   1047 H HA3  . GLY   A 1 47  ? 19.790 8.738   -1.429  1.00 13.86 ?  47  GLY   A HA3  1 
ATOM   1048 N N    A GLY   A 1 48  ? 18.600 6.770   -0.263  0.86 11.14 ?  48  GLY   A N    1 
ATOM   1049 N N    B GLY   A 1 48  ? 18.607 6.779   -0.107  0.14 10.70 ?  48  GLY   A N    1 
ATOM   1050 C CA   A GLY   A 1 48  ? 18.156 5.454   0.127   0.86 11.24 ?  48  GLY   A CA   1 
ATOM   1051 C CA   B GLY   A 1 48  ? 18.233 5.421   0.274   0.14 10.55 ?  48  GLY   A CA   1 
ATOM   1052 C C    A GLY   A 1 48  ? 18.600 5.133   1.539   0.86 10.20 ?  48  GLY   A C    1 
ATOM   1053 C C    B GLY   A 1 48  ? 18.751 5.040   1.654   0.14 10.23 ?  48  GLY   A C    1 
ATOM   1054 O O    A GLY   A 1 48  ? 18.753 6.018   2.395   0.86 10.74 ?  48  GLY   A O    1 
ATOM   1055 O O    B GLY   A 1 48  ? 18.843 5.869   2.567   0.14 10.29 ?  48  GLY   A O    1 
ATOM   1056 H H    A GLY   A 1 48  ? 17.969 7.311   -0.480  0.86 13.38 ?  48  GLY   A H    1 
ATOM   1057 H H    B GLY   A 1 48  ? 17.951 7.327   -0.209  0.14 12.85 ?  48  GLY   A H    1 
ATOM   1058 H HA2  A GLY   A 1 48  ? 17.187 5.403   0.086   0.86 13.50 ?  48  GLY   A HA2  1 
ATOM   1059 H HA2  B GLY   A 1 48  ? 17.266 5.337   0.265   0.14 12.67 ?  48  GLY   A HA2  1 
ATOM   1060 H HA3  A GLY   A 1 48  ? 18.528 4.787   -0.471  0.86 13.50 ?  48  GLY   A HA3  1 
ATOM   1061 H HA3  B GLY   A 1 48  ? 18.600 4.793   -0.366  0.14 12.67 ?  48  GLY   A HA3  1 
ATOM   1062 N N    A VAL   A 1 49  ? 18.812 3.838   1.785   0.86 9.48  ?  49  VAL   A N    1 
ATOM   1063 N N    B VAL   A 1 49  ? 19.092 3.755   1.812   0.14 10.03 ?  49  VAL   A N    1 
ATOM   1064 C CA   A VAL   A 1 49  ? 19.285 3.387   3.090   0.86 9.58  ?  49  VAL   A CA   1 
ATOM   1065 C CA   B VAL   A 1 49  ? 19.654 3.279   3.078   0.14 9.62  ?  49  VAL   A CA   1 
ATOM   1066 C C    A VAL   A 1 49  ? 20.612 4.053   3.452   0.86 8.70  ?  49  VAL   A C    1 
ATOM   1067 C C    B VAL   A 1 49  ? 20.935 4.035   3.404   0.14 8.89  ?  49  VAL   A C    1 
ATOM   1068 O O    A VAL   A 1 49  ? 20.822 4.465   4.599   0.86 9.12  ?  49  VAL   A O    1 
ATOM   1069 O O    B VAL   A 1 49  ? 21.152 4.468   4.542   0.14 8.44  ?  49  VAL   A O    1 
ATOM   1070 C CB   A VAL   A 1 49  ? 19.393 1.848   3.107   0.86 10.47 ?  49  VAL   A CB   1 
ATOM   1071 C CB   B VAL   A 1 49  ? 19.894 1.756   3.040   0.14 9.62  ?  49  VAL   A CB   1 
ATOM   1072 C CG1  A VAL   A 1 49  ? 20.155 1.377   4.342   0.86 11.35 ?  49  VAL   A CG1  1 
ATOM   1073 C CG1  B VAL   A 1 49  ? 20.786 1.328   4.196   0.14 9.26  ?  49  VAL   A CG1  1 
ATOM   1074 C CG2  A VAL   A 1 49  ? 18.011 1.215   3.041   0.86 12.53 ?  49  VAL   A CG2  1 
ATOM   1075 C CG2  B VAL   A 1 49  ? 18.591 0.995   3.109   0.14 9.85  ?  49  VAL   A CG2  1 
ATOM   1076 H H    A VAL   A 1 49  ? 18.685 3.202   1.215   0.86 11.39 ?  49  VAL   A H    1 
ATOM   1077 H H    B VAL   A 1 49  ? 19.014 3.149   1.207   0.14 12.04 ?  49  VAL   A H    1 
ATOM   1078 H HA   A VAL   A 1 49  ? 18.634 3.635   3.761   0.86 11.51 ?  49  VAL   A HA   1 
ATOM   1079 H HA   B VAL   A 1 49  ? 19.021 3.453   3.788   0.14 11.55 ?  49  VAL   A HA   1 
ATOM   1080 H HB   A VAL   A 1 49  ? 19.889 1.554   2.326   0.86 12.57 ?  49  VAL   A HB   1 
ATOM   1081 H HB   B VAL   A 1 49  ? 20.336 1.517   2.210   0.14 11.55 ?  49  VAL   A HB   1 
ATOM   1082 H HG11 A VAL   A 1 49  ? 19.969 0.436   4.486   0.86 13.63 ?  49  VAL   A HG11 1 
ATOM   1083 H HG11 B VAL   A 1 49  ? 20.687 0.372   4.336   0.14 11.12 ?  49  VAL   A HG11 1 
ATOM   1084 H HG12 A VAL   A 1 49  ? 21.100 1.513   4.204   0.86 13.63 ?  49  VAL   A HG12 1 
ATOM   1085 H HG12 B VAL   A 1 49  ? 21.710 1.531   3.979   0.14 11.12 ?  49  VAL   A HG12 1 
ATOM   1086 H HG13 A VAL   A 1 49  ? 19.849 1.891   5.109   0.86 13.63 ?  49  VAL   A HG13 1 
ATOM   1087 H HG13 B VAL   A 1 49  ? 20.517 1.804   4.996   0.14 11.12 ?  49  VAL   A HG13 1 
ATOM   1088 H HG21 A VAL   A 1 49  ? 18.106 0.247   3.054   0.86 15.05 ?  49  VAL   A HG21 1 
ATOM   1089 H HG21 B VAL   A 1 49  ? 18.773 0.041   3.056   0.14 11.83 ?  49  VAL   A HG21 1 
ATOM   1090 H HG22 A VAL   A 1 49  ? 17.495 1.505   3.807   0.86 15.05 ?  49  VAL   A HG22 1 
ATOM   1091 H HG22 B VAL   A 1 49  ? 18.147 1.201   3.947   0.14 11.83 ?  49  VAL   A HG22 1 
ATOM   1092 H HG23 A VAL   A 1 49  ? 17.576 1.492   2.221   0.86 15.05 ?  49  VAL   A HG23 1 
ATOM   1093 H HG23 B VAL   A 1 49  ? 18.046 1.270   2.365   0.14 11.83 ?  49  VAL   A HG23 1 
ATOM   1094 N N    A ALA   A 1 50  ? 21.540 4.135   2.495   0.86 8.12  ?  50  ALA   A N    1 
ATOM   1095 N N    B ALA   A 1 50  ? 21.810 4.195   2.409   0.14 8.85  ?  50  ALA   A N    1 
ATOM   1096 C CA   A ALA   A 1 50  ? 22.862 4.680   2.797   0.86 8.06  ?  50  ALA   A CA   1 
ATOM   1097 C CA   B ALA   A 1 50  ? 23.094 4.844   2.651   0.14 8.98  ?  50  ALA   A CA   1 
ATOM   1098 C C    A ALA   A 1 50  ? 22.772 6.134   3.235   0.86 8.11  ?  50  ALA   A C    1 
ATOM   1099 C C    B ALA   A 1 50  ? 22.895 6.276   3.129   0.14 8.97  ?  50  ALA   A C    1 
ATOM   1100 O O    A ALA   A 1 50  ? 23.417 6.544   4.209   0.86 8.64  ?  50  ALA   A O    1 
ATOM   1101 O O    B ALA   A 1 50  ? 23.521 6.712   4.102   0.14 8.89  ?  50  ALA   A O    1 
ATOM   1102 C CB   A ALA   A 1 50  ? 23.776 4.551   1.579   0.86 8.18  ?  50  ALA   A CB   1 
ATOM   1103 C CB   B ALA   A 1 50  ? 23.946 4.798   1.382   0.14 9.01  ?  50  ALA   A CB   1 
ATOM   1104 H H    A ALA   A 1 50  ? 21.427 3.886   1.675   0.86 9.75  ?  50  ALA   A H    1 
ATOM   1105 H H    B ALA   A 1 50  ? 21.681 3.949   1.596   0.14 10.62 ?  50  ALA   A H    1 
ATOM   1106 H HA   A ALA   A 1 50  ? 23.251 4.180   3.522   0.86 9.68  ?  50  ALA   A HA   1 
ATOM   1107 H HA   B ALA   A 1 50  ? 23.569 4.365   3.345   0.14 10.78 ?  50  ALA   A HA   1 
ATOM   1108 H HB1  A ALA   A 1 50  ? 24.646 4.922   1.799   0.86 9.83  ?  50  ALA   A HB1  1 
ATOM   1109 H HB1  B ALA   A 1 50  ? 24.820 5.175   1.572   0.14 10.83 ?  50  ALA   A HB1  1 
ATOM   1110 H HB2  A ALA   A 1 50  ? 23.863 3.615   1.347   0.86 9.83  ?  50  ALA   A HB2  1 
ATOM   1111 H HB2  B ALA   A 1 50  ? 24.043 3.873   1.101   0.14 10.83 ?  50  ALA   A HB2  1 
ATOM   1112 H HB3  A ALA   A 1 50  ? 23.388 5.043   0.836   0.86 9.83  ?  50  ALA   A HB3  1 
ATOM   1113 H HB3  B ALA   A 1 50  ? 23.508 5.309   0.683   0.14 10.83 ?  50  ALA   A HB3  1 
ATOM   1114 N N    A GLY   A 1 51  ? 21.999 6.939   2.507   0.86 8.56  ?  51  GLY   A N    1 
ATOM   1115 N N    B GLY   A 1 51  ? 22.014 7.022   2.462   0.14 9.12  ?  51  GLY   A N    1 
ATOM   1116 C CA   A GLY   A 1 51  ? 21.867 8.331   2.890   0.86 9.17  ?  51  GLY   A CA   1 
ATOM   1117 C CA   B GLY   A 1 51  ? 21.757 8.388   2.884   0.14 9.33  ?  51  GLY   A CA   1 
ATOM   1118 C C    A GLY   A 1 51  ? 21.272 8.479   4.274   0.86 9.00  ?  51  GLY   A C    1 
ATOM   1119 C C    B GLY   A 1 51  ? 21.132 8.460   4.263   0.14 9.41  ?  51  GLY   A C    1 
ATOM   1120 O O    A GLY   A 1 51  ? 21.678 9.357   5.041   0.86 9.43  ?  51  GLY   A O    1 
ATOM   1121 O O    B GLY   A 1 51  ? 21.434 9.365   5.046   0.14 9.52  ?  51  GLY   A O    1 
ATOM   1122 H H    A GLY   A 1 51  ? 21.556 6.711   1.803   0.86 10.28 ?  51  GLY   A H    1 
ATOM   1123 H H    B GLY   A 1 51  ? 21.561 6.763   1.779   0.14 10.96 ?  51  GLY   A H    1 
ATOM   1124 H HA2  A GLY   A 1 51  ? 22.738 8.755   2.883   0.86 11.01 ?  51  GLY   A HA2  1 
ATOM   1125 H HA2  B GLY   A 1 51  ? 22.590 8.885   2.897   0.14 11.20 ?  51  GLY   A HA2  1 
ATOM   1126 H HA3  A GLY   A 1 51  ? 21.292 8.792   2.258   0.86 11.01 ?  51  GLY   A HA3  1 
ATOM   1127 H HA3  B GLY   A 1 51  ? 21.155 8.813   2.253   0.14 11.20 ?  51  GLY   A HA3  1 
ATOM   1128 N N    A ALA   A 1 52  ? 20.306 7.618   4.614   0.86 9.00  ?  52  ALA   A N    1 
ATOM   1129 N N    B ALA   A 1 52  ? 20.254 7.507   4.581   0.14 9.42  ?  52  ALA   A N    1 
ATOM   1130 C CA   A ALA   A 1 52  ? 19.671 7.677   5.926   0.86 9.65  ?  52  ALA   A CA   1 
ATOM   1131 C CA   B ALA   A 1 52  ? 19.612 7.497   5.890   0.14 9.46  ?  52  ALA   A CA   1 
ATOM   1132 C C    A ALA   A 1 52  ? 20.631 7.245   7.033   0.86 9.09  ?  52  ALA   A C    1 
ATOM   1133 C C    B ALA   A 1 52  ? 20.616 7.177   6.991   0.14 9.23  ?  52  ALA   A C    1 
ATOM   1134 O O    A ALA   A 1 52  ? 20.719 7.899   8.078   0.86 9.75  ?  52  ALA   A O    1 
ATOM   1135 O O    B ALA   A 1 52  ? 20.660 7.859   8.022   0.14 9.32  ?  52  ALA   A O    1 
ATOM   1136 C CB   A ALA   A 1 52  ? 18.403 6.820   5.929   0.86 10.85 ?  52  ALA   A CB   1 
ATOM   1137 C CB   B ALA   A 1 52  ? 18.460 6.492   5.899   0.14 9.64  ?  52  ALA   A CB   1 
ATOM   1138 H H    A ALA   A 1 52  ? 20.012 6.985   4.103   0.86 10.81 ?  52  ALA   A H    1 
ATOM   1139 H H    B ALA   A 1 52  ? 20.018 6.864   4.061   0.14 11.31 ?  52  ALA   A H    1 
ATOM   1140 H HA   A ALA   A 1 52  ? 19.411 8.587   6.103   0.86 11.59 ?  52  ALA   A HA   1 
ATOM   1141 H HA   B ALA   A 1 52  ? 19.244 8.376   6.067   0.14 11.36 ?  52  ALA   A HA   1 
ATOM   1142 H HB1  A ALA   A 1 52  ? 17.989 6.869   6.807   0.86 13.02 ?  52  ALA   A HB1  1 
ATOM   1143 H HB1  B ALA   A 1 52  ? 18.044 6.497   6.775   0.14 11.58 ?  52  ALA   A HB1  1 
ATOM   1144 H HB2  A ALA   A 1 52  ? 17.788 7.160   5.258   0.86 13.02 ?  52  ALA   A HB2  1 
ATOM   1145 H HB2  B ALA   A 1 52  ? 17.813 6.749   5.224   0.14 11.58 ?  52  ALA   A HB2  1 
ATOM   1146 H HB3  A ALA   A 1 52  ? 18.634 5.899   5.727   0.86 13.02 ?  52  ALA   A HB3  1 
ATOM   1147 H HB3  B ALA   A 1 52  ? 18.810 5.609   5.704   0.14 11.58 ?  52  ALA   A HB3  1 
ATOM   1148 N N    A LEU   A 1 53  ? 21.348 6.134   6.836   0.86 8.89  ?  53  LEU   A N    1 
ATOM   1149 N N    B LEU   A 1 53  ? 21.429 6.137   6.794   0.14 8.98  ?  53  LEU   A N    1 
ATOM   1150 C CA   A LEU   A 1 53  ? 22.321 5.710   7.843   0.86 9.12  ?  53  LEU   A CA   1 
ATOM   1151 C CA   B LEU   A 1 53  ? 22.421 5.776   7.803   0.14 8.77  ?  53  LEU   A CA   1 
ATOM   1152 C C    A LEU   A 1 53  ? 23.387 6.778   8.038   0.86 8.77  ?  53  LEU   A C    1 
ATOM   1153 C C    B LEU   A 1 53  ? 23.429 6.903   8.002   0.14 8.39  ?  53  LEU   A C    1 
ATOM   1154 O O    A LEU   A 1 53  ? 23.745 7.116   9.173   0.86 9.72  ?  53  LEU   A O    1 
ATOM   1155 O O    B LEU   A 1 53  ? 23.689 7.328   9.134   0.14 8.24  ?  53  LEU   A O    1 
ATOM   1156 C CB   A LEU   A 1 53  ? 22.972 4.376   7.453   0.86 9.46  ?  53  LEU   A CB   1 
ATOM   1157 C CB   B LEU   A 1 53  ? 23.131 4.476   7.410   0.14 8.79  ?  53  LEU   A CB   1 
ATOM   1158 C CG   A LEU   A 1 53  ? 22.091 3.124   7.515   0.86 10.21 ?  53  LEU   A CG   1 
ATOM   1159 C CG   B LEU   A 1 53  ? 22.316 3.178   7.384   0.14 9.10  ?  53  LEU   A CG   1 
ATOM   1160 C CD1  A LEU   A 1 53  ? 22.798 1.940   6.870   0.86 10.88 ?  53  LEU   A CD1  1 
ATOM   1161 C CD1  B LEU   A 1 53  ? 23.208 2.000   6.996   0.14 8.80  ?  53  LEU   A CD1  1 
ATOM   1162 C CD2  A LEU   A 1 53  ? 21.702 2.779   8.944   0.86 11.72 ?  53  LEU   A CD2  1 
ATOM   1163 C CD2  B LEU   A 1 53  ? 21.633 2.918   8.720   0.14 9.70  ?  53  LEU   A CD2  1 
ATOM   1164 H H    A LEU   A 1 53  ? 21.299 5.618   6.142   0.86 10.68 ?  53  LEU   A H    1 
ATOM   1165 H H    B LEU   A 1 53  ? 21.425 5.634   6.096   0.14 10.79 ?  53  LEU   A H    1 
ATOM   1166 H HA   A LEU   A 1 53  ? 21.865 5.583   8.688   0.86 10.96 ?  53  LEU   A HA   1 
ATOM   1167 H HA   B LEU   A 1 53  ? 21.970 5.626   8.647   0.14 10.53 ?  53  LEU   A HA   1 
ATOM   1168 H HB2  A LEU   A 1 53  ? 23.298 4.451   6.543   0.86 11.36 ?  53  LEU   A HB2  1 
ATOM   1169 H HB2  B LEU   A 1 53  ? 23.495 4.592   6.520   0.14 10.56 ?  53  LEU   A HB2  1 
ATOM   1170 H HB3  A LEU   A 1 53  ? 23.724 4.221   8.048   0.86 11.36 ?  53  LEU   A HB3  1 
ATOM   1171 H HB3  B LEU   A 1 53  ? 23.859 4.335   8.034   0.14 10.56 ?  53  LEU   A HB3  1 
ATOM   1172 H HG   A LEU   A 1 53  ? 21.278 3.287   7.012   0.86 12.26 ?  53  LEU   A HG   1 
ATOM   1173 H HG   B LEU   A 1 53  ? 21.626 3.254   6.709   0.14 10.92 ?  53  LEU   A HG   1 
ATOM   1174 H HD11 A LEU   A 1 53  ? 22.219 1.161   6.922   0.86 13.07 ?  53  LEU   A HD11 1 
ATOM   1175 H HD11 B LEU   A 1 53  ? 22.675 1.188   6.985   0.14 10.57 ?  53  LEU   A HD11 1 
ATOM   1176 H HD12 A LEU   A 1 53  ? 22.987 2.149   5.943   0.86 13.07 ?  53  LEU   A HD12 1 
ATOM   1177 H HD12 B LEU   A 1 53  ? 23.581 2.161   6.115   0.14 10.57 ?  53  LEU   A HD12 1 
ATOM   1178 H HD13 A LEU   A 1 53  ? 23.624 1.768   7.348   0.86 13.07 ?  53  LEU   A HD13 1 
ATOM   1179 H HD13 B LEU   A 1 53  ? 23.923 1.916   7.647   0.14 10.57 ?  53  LEU   A HD13 1 
ATOM   1180 H HD21 A LEU   A 1 53  ? 21.172 1.965   8.940   0.86 14.07 ?  53  LEU   A HD21 1 
ATOM   1181 H HD21 B LEU   A 1 53  ? 21.214 2.042   8.697   0.14 11.65 ?  53  LEU   A HD21 1 
ATOM   1182 H HD22 A LEU   A 1 53  ? 22.504 2.649   9.469   0.86 14.07 ?  53  LEU   A HD22 1 
ATOM   1183 H HD22 B LEU   A 1 53  ? 22.297 2.947   9.427   0.14 11.65 ?  53  LEU   A HD22 1 
ATOM   1184 H HD23 A LEU   A 1 53  ? 21.178 3.509   9.312   0.86 14.07 ?  53  LEU   A HD23 1 
ATOM   1185 H HD23 B LEU   A 1 53  ? 20.960 3.601   8.869   0.14 11.65 ?  53  LEU   A HD23 1 
ATOM   1186 N N    A ASN   A 1 54  ? 23.895 7.337   6.942   0.86 8.55  ?  54  ASN   A N    1 
ATOM   1187 N N    B ASN   A 1 54  ? 24.000 7.411   6.907   0.14 8.50  ?  54  ASN   A N    1 
ATOM   1188 C CA   A ASN   A 1 54  ? 24.951 8.332   7.075   0.86 8.46  ?  54  ASN   A CA   1 
ATOM   1189 C CA   B ASN   A 1 54  ? 25.031 8.439   7.024   0.14 8.64  ?  54  ASN   A CA   1 
ATOM   1190 C C    A ASN   A 1 54  ? 24.450 9.580   7.805   0.86 8.79  ?  54  ASN   A C    1 
ATOM   1191 C C    B ASN   A 1 54  ? 24.499 9.683   7.724   0.14 8.90  ?  54  ASN   A C    1 
ATOM   1192 O O    A ASN   A 1 54  ? 25.139 10.116  8.686   0.86 9.09  ?  54  ASN   A O    1 
ATOM   1193 O O    B ASN   A 1 54  ? 25.218 10.319  8.504   0.14 9.00  ?  54  ASN   A O    1 
ATOM   1194 C CB   A ASN   A 1 54  ? 25.517 8.693   5.711   0.86 8.71  ?  54  ASN   A CB   1 
ATOM   1195 C CB   B ASN   A 1 54  ? 25.589 8.795   5.647   0.14 8.77  ?  54  ASN   A CB   1 
ATOM   1196 C CG   A ASN   A 1 54  ? 26.541 9.793   5.818   0.86 8.63  ?  54  ASN   A CG   1 
ATOM   1197 C CG   B ASN   A 1 54  ? 26.549 9.968   5.699   0.14 9.01  ?  54  ASN   A CG   1 
ATOM   1198 O OD1  A ASN   A 1 54  ? 27.535 9.651   6.536   0.86 8.76  ?  54  ASN   A OD1  1 
ATOM   1199 O OD1  B ASN   A 1 54  ? 27.643 9.862   6.254   0.14 9.40  ?  54  ASN   A OD1  1 
ATOM   1200 N ND2  A ASN   A 1 54  ? 26.283 10.919  5.157   0.86 9.59  ?  54  ASN   A ND2  1 
ATOM   1201 N ND2  B ASN   A 1 54  ? 26.143 11.097  5.124   0.14 9.01  ?  54  ASN   A ND2  1 
ATOM   1202 H H    A ASN   A 1 54  ? 23.644 7.162   6.137   0.86 10.27 ?  54  ASN   A H    1 
ATOM   1203 H H    B ASN   A 1 54  ? 23.808 7.182   6.102   0.14 10.20 ?  54  ASN   A H    1 
ATOM   1204 H HA   A ASN   A 1 54  ? 25.665 7.949   7.599   0.86 10.16 ?  54  ASN   A HA   1 
ATOM   1205 H HA   B ASN   A 1 54  ? 25.759 8.091   7.559   0.14 10.37 ?  54  ASN   A HA   1 
ATOM   1206 H HB2  A ASN   A 1 54  ? 25.948 7.903   5.327   0.86 10.46 ?  54  ASN   A HB2  1 
ATOM   1207 H HB2  B ASN   A 1 54  ? 26.070 8.030   5.294   0.14 10.54 ?  54  ASN   A HB2  1 
ATOM   1208 H HB3  A ASN   A 1 54  ? 24.799 8.987   5.128   0.86 10.46 ?  54  ASN   A HB3  1 
ATOM   1209 H HB3  B ASN   A 1 54  ? 24.856 9.029   5.058   0.14 10.54 ?  54  ASN   A HB3  1 
ATOM   1210 H HD21 A ASN   A 1 54  ? 26.839 11.571  5.194   0.86 11.52 ?  54  ASN   A HD21 1 
ATOM   1211 H HD21 B ASN   A 1 54  ? 26.652 11.791  5.131   0.14 10.82 ?  54  ASN   A HD21 1 
ATOM   1212 H HD22 A ASN   A 1 54  ? 25.571 10.984  4.679   0.86 11.52 ?  54  ASN   A HD22 1 
ATOM   1213 H HD22 B ASN   A 1 54  ? 25.373 11.133  4.744   0.14 10.82 ?  54  ASN   A HD22 1 
ATOM   1214 N N    . LYS   A 1 55  ? 23.242 10.048  7.460   1.00 9.29  ?  55  LYS   A N    1 
ATOM   1215 C CA   . LYS   A 1 55  ? 22.664 11.204  8.133   1.00 9.62  ?  55  LYS   A CA   1 
ATOM   1216 C C    . LYS   A 1 55  ? 22.574 10.962  9.634   1.00 10.05 ?  55  LYS   A C    1 
ATOM   1217 O O    . LYS   A 1 55  ? 22.858 11.859  10.436  1.00 10.67 ?  55  LYS   A O    1 
ATOM   1218 C CB   . LYS   A 1 55  ? 21.292 11.509  7.525   1.00 10.42 ?  55  LYS   A CB   1 
ATOM   1219 C CG   . LYS   A 1 55  ? 20.557 12.678  8.154   1.00 11.46 ?  55  LYS   A CG   1 
ATOM   1220 C CD   . LYS   A 1 55  ? 19.223 12.923  7.445   1.00 12.29 ?  55  LYS   A CD   1 
ATOM   1221 C CE   . LYS   A 1 55  ? 18.426 14.051  8.077   1.00 14.22 ?  55  LYS   A CE   1 
ATOM   1222 N NZ   . LYS   A 1 55  ? 17.079 14.196  7.448   1.00 15.10 ?  55  LYS   A NZ   1 
ATOM   1223 H H    A LYS   A 1 55  ? 22.740 9.707   6.845   0.86 11.16 ?  55  LYS   A H    1 
ATOM   1224 H H    B LYS   A 1 55  ? 22.711 9.643   6.911   0.14 11.16 ?  55  LYS   A H    1 
ATOM   1225 H HA   . LYS   A 1 55  ? 23.233 11.973  7.984   1.00 11.55 ?  55  LYS   A HA   1 
ATOM   1226 H HB2  . LYS   A 1 55  ? 21.407 11.713  6.584   1.00 12.51 ?  55  LYS   A HB2  1 
ATOM   1227 H HB3  . LYS   A 1 55  ? 20.729 10.724  7.620   1.00 12.51 ?  55  LYS   A HB3  1 
ATOM   1228 H HG2  . LYS   A 1 55  ? 20.371 12.476  9.087   1.00 13.76 ?  55  LYS   A HG2  1 
ATOM   1229 H HG3  . LYS   A 1 55  ? 21.096 13.476  8.081   1.00 13.76 ?  55  LYS   A HG3  1 
ATOM   1230 H HD2  . LYS   A 1 55  ? 19.399 13.154  6.520   1.00 14.76 ?  55  LYS   A HD2  1 
ATOM   1231 H HD3  . LYS   A 1 55  ? 18.689 12.112  7.488   1.00 14.76 ?  55  LYS   A HD3  1 
ATOM   1232 H HE2  . LYS   A 1 55  ? 18.303 13.864  9.022   1.00 17.07 ?  55  LYS   A HE2  1 
ATOM   1233 H HE3  . LYS   A 1 55  ? 18.907 14.884  7.961   1.00 17.07 ?  55  LYS   A HE3  1 
ATOM   1234 H HZ1  . LYS   A 1 55  ? 16.555 14.697  7.966   1.00 18.13 ?  55  LYS   A HZ1  1 
ATOM   1235 H HZ2  . LYS   A 1 55  ? 17.152 14.583  6.652   1.00 18.13 ?  55  LYS   A HZ2  1 
ATOM   1236 H HZ3  . LYS   A 1 55  ? 16.700 13.395  7.349   1.00 18.13 ?  55  LYS   A HZ3  1 
ATOM   1237 N N    . ALA   A 1 56  ? 22.193 9.744   10.033  1.00 10.04 ?  56  ALA   A N    1 
ATOM   1238 C CA   . ALA   A 1 56  ? 22.082 9.412   11.447  1.00 10.98 ?  56  ALA   A CA   1 
ATOM   1239 C C    . ALA   A 1 56  ? 23.425 9.451   12.167  1.00 10.67 ?  56  ALA   A C    1 
ATOM   1240 O O    . ALA   A 1 56  ? 23.453 9.650   13.385  1.00 12.35 ?  56  ALA   A O    1 
ATOM   1241 C CB   . ALA   A 1 56  ? 21.419 8.040   11.608  1.00 12.03 ?  56  ALA   A CB   1 
ATOM   1242 H H    . ALA   A 1 56  ? 21.995 9.100   9.497   1.00 12.06 ?  56  ALA   A H    1 
ATOM   1243 H HA   . ALA   A 1 56  ? 21.505 10.059  11.871  1.00 13.18 ?  56  ALA   A HA   1 
ATOM   1244 H HB1  . ALA   A 1 56  ? 21.335 7.838   12.555  1.00 14.44 ?  56  ALA   A HB1  1 
ATOM   1245 H HB2  . ALA   A 1 56  ? 20.539 8.062   11.197  1.00 14.44 ?  56  ALA   A HB2  1 
ATOM   1246 H HB3  . ALA   A 1 56  ? 21.967 7.366   11.175  1.00 14.44 ?  56  ALA   A HB3  1 
ATOM   1247 N N    . THR   A 1 57  ? 24.535 9.271   11.444  1.00 9.87  ?  57  THR   A N    1 
ATOM   1248 C CA   . THR   A 1 57  ? 25.879 9.394   12.014  1.00 10.20 ?  57  THR   A CA   1 
ATOM   1249 C C    . THR   A 1 57  ? 26.430 10.814  11.945  1.00 10.42 ?  57  THR   A C    1 
ATOM   1250 O O    . THR   A 1 57  ? 27.611 11.024  12.248  1.00 11.04 ?  57  THR   A O    1 
ATOM   1251 C CB   . THR   A 1 57  ? 26.891 8.447   11.336  1.00 9.99  ?  57  THR   A CB   1 
ATOM   1252 O OG1  . THR   A 1 57  ? 27.272 8.947   10.041  1.00 9.70  ?  57  THR   A OG1  1 
ATOM   1253 C CG2  . THR   A 1 57  ? 26.359 7.021   11.240  1.00 10.08 ?  57  THR   A CG2  1 
ATOM   1254 H H    . THR   A 1 57  ? 24.534 9.069   10.602  1.00 11.86 ?  57  THR   A H    1 
ATOM   1255 H HA   . THR   A 1 57  ? 25.833 9.136   12.949  1.00 12.25 ?  57  THR   A HA   1 
ATOM   1256 H HB   . THR   A 1 57  ? 27.687 8.407   11.892  1.00 11.99 ?  57  THR   A HB   1 
ATOM   1257 H HG1  . THR   A 1 57  ? 26.594 9.006   9.551   1.00 11.65 ?  57  THR   A HG1  1 
ATOM   1258 H HG21 . THR   A 1 57  ? 27.031 6.436   10.854  1.00 12.11 ?  57  THR   A HG21 1 
ATOM   1259 H HG22 . THR   A 1 57  ? 26.127 6.689   12.123  1.00 12.11 ?  57  THR   A HG22 1 
ATOM   1260 H HG23 . THR   A 1 57  ? 25.566 6.996   10.681  1.00 12.11 ?  57  THR   A HG23 1 
ATOM   1261 N N    . ASN   A 1 58  ? 25.613 11.787  11.545  1.00 10.67 ?  58  ASN   A N    1 
ATOM   1262 C CA   . ASN   A 1 58  ? 26.071 13.169  11.445  1.00 11.62 ?  58  ASN   A CA   1 
ATOM   1263 C C    . ASN   A 1 58  ? 27.218 13.293  10.437  1.00 10.61 ?  58  ASN   A C    1 
ATOM   1264 O O    . ASN   A 1 58  ? 28.121 14.120  10.600  1.00 11.22 ?  58  ASN   A O    1 
ATOM   1265 C CB   . ASN   A 1 58  ? 26.455 13.704  12.839  1.00 14.56 ?  58  ASN   A CB   1 
ATOM   1266 C CG   . ASN   A 1 58  ? 26.853 15.166  12.840  1.00 17.85 ?  58  ASN   A CG   1 
ATOM   1267 O OD1  . ASN   A 1 58  ? 26.228 15.985  12.182  1.00 19.05 ?  58  ASN   A OD1  1 
ATOM   1268 N ND2  . ASN   A 1 58  ? 27.890 15.501  13.605  1.00 19.31 ?  58  ASN   A ND2  1 
ATOM   1269 H H    . ASN   A 1 58  ? 24.791 11.662  11.318  1.00 12.81 ?  58  ASN   A H    1 
ATOM   1270 H HA   . ASN   A 1 58  ? 25.334 13.703  11.117  1.00 13.95 ?  58  ASN   A HA   1 
ATOM   1271 H HB2  . ASN   A 1 58  ? 25.689 13.594  13.432  1.00 17.48 ?  58  ASN   A HB2  1 
ATOM   1272 H HB3  . ASN   A 1 58  ? 27.204 13.195  13.178  1.00 17.48 ?  58  ASN   A HB3  1 
ATOM   1273 H HD21 . ASN   A 1 58  ? 28.141 16.322  13.643  1.00 23.18 ?  58  ASN   A HD21 1 
ATOM   1274 H HD22 . ASN   A 1 58  ? 28.297 14.900  14.058  1.00 23.18 ?  58  ASN   A HD22 1 
ATOM   1275 N N    . ASN   A 1 59  ? 27.190 12.476  9.379   1.00 9.71  ?  59  ASN   A N    1 
ATOM   1276 C CA   . ASN   A 1 59  ? 28.166 12.460  8.282   1.00 9.62  ?  59  ASN   A CA   1 
ATOM   1277 C C    . ASN   A 1 59  ? 29.488 11.784  8.662   1.00 9.52  ?  59  ASN   A C    1 
ATOM   1278 O O    . ASN   A 1 59  ? 30.401 11.740  7.830   1.00 9.83  ?  59  ASN   A O    1 
ATOM   1279 C CB   . ASN   A 1 59  ? 28.441 13.849  7.679   1.00 10.06 ?  59  ASN   A CB   1 
ATOM   1280 C CG   . ASN   A 1 59  ? 28.796 13.786  6.212   1.00 10.14 ?  59  ASN   A CG   1 
ATOM   1281 O OD1  . ASN   A 1 59  ? 28.084 13.169  5.416   1.00 10.57 ?  59  ASN   A OD1  1 
ATOM   1282 N ND2  . ASN   A 1 59  ? 29.882 14.450  5.834   1.00 10.93 ?  59  ASN   A ND2  1 
ATOM   1283 H H    . ASN   A 1 59  ? 26.570 11.887  9.262   1.00 11.66 ?  59  ASN   A H    1 
ATOM   1284 H HA   . ASN   A 1 59  ? 27.783 11.928  7.567   1.00 11.55 ?  59  ASN   A HA   1 
ATOM   1285 H HB2  . ASN   A 1 59  ? 27.647 14.400  7.765   1.00 12.09 ?  59  ASN   A HB2  1 
ATOM   1286 H HB3  . ASN   A 1 59  ? 29.184 14.260  8.146   1.00 12.09 ?  59  ASN   A HB3  1 
ATOM   1287 H HD21 . ASN   A 1 59  ? 30.128 14.452  5.010   1.00 13.13 ?  59  ASN   A HD21 1 
ATOM   1288 H HD22 . ASN   A 1 59  ? 30.357 14.877  6.419   1.00 13.13 ?  59  ASN   A HD22 1 
ATOM   1289 N N    . ALA   A 1 60  ? 29.618 11.230  9.867   1.00 9.60  ?  60  ALA   A N    1 
ATOM   1290 C CA   . ALA   A 1 60  ? 30.854 10.538  10.222  1.00 9.71  ?  60  ALA   A CA   1 
ATOM   1291 C C    . ALA   A 1 60  ? 31.081 9.307   9.354   1.00 9.44  ?  60  ALA   A C    1 
ATOM   1292 O O    . ALA   A 1 60  ? 32.227 8.989   9.019   1.00 10.02 ?  60  ALA   A O    1 
ATOM   1293 C CB   . ALA   A 1 60  ? 30.853 10.168  11.704  1.00 10.73 ?  60  ALA   A CB   1 
ATOM   1294 H H    . ALA   A 1 60  ? 29.018 11.236  10.482  1.00 11.53 ?  60  ALA   A H    1 
ATOM   1295 H HA   . ALA   A 1 60  ? 31.598 11.144  10.069  1.00 11.66 ?  60  ALA   A HA   1 
ATOM   1296 H HB1  . ALA   A 1 60  ? 31.685 9.715   11.915  1.00 12.88 ?  60  ALA   A HB1  1 
ATOM   1297 H HB2  . ALA   A 1 60  ? 30.778 10.981  12.230  1.00 12.88 ?  60  ALA   A HB2  1 
ATOM   1298 H HB3  . ALA   A 1 60  ? 30.102 9.585   11.882  1.00 12.88 ?  60  ALA   A HB3  1 
ATOM   1299 N N    . MET   A 1 61  ? 30.009 8.610   8.968   1.00 9.36  ?  61  MET   A N    1 
ATOM   1300 C CA   . MET   A 1 61  ? 30.150 7.477   8.059   1.00 9.13  ?  61  MET   A CA   1 
ATOM   1301 C C    . MET   A 1 61  ? 30.779 7.911   6.733   1.00 8.84  ?  61  MET   A C    1 
ATOM   1302 O O    . MET   A 1 61  ? 31.667 7.232   6.207   1.00 9.25  ?  61  MET   A O    1 
ATOM   1303 C CB   . MET   A 1 61  ? 28.783 6.816   7.848   1.00 9.16  ?  61  MET   A CB   1 
ATOM   1304 C CG   . MET   A 1 61  ? 28.792 5.654   6.860   1.00 9.65  ?  61  MET   A CG   1 
ATOM   1305 S SD   . MET   A 1 61  ? 27.164 4.922   6.640   1.00 10.67 ?  61  MET   A SD   1 
ATOM   1306 C CE   . MET   A 1 61  ? 27.006 4.010   8.178   1.00 12.09 ?  61  MET   A CE   1 
ATOM   1307 H H    . MET   A 1 61  ? 29.203 8.778   9.211   1.00 11.24 ?  61  MET   A H    1 
ATOM   1308 H HA   . MET   A 1 61  ? 30.729 6.821   8.473   1.00 10.97 ?  61  MET   A HA   1 
ATOM   1309 H HB2  . MET   A 1 61  ? 28.473 6.474   8.702   1.00 11.00 ?  61  MET   A HB2  1 
ATOM   1310 H HB3  . MET   A 1 61  ? 28.164 7.482   7.517   1.00 11.00 ?  61  MET   A HB3  1 
ATOM   1311 H HG2  . MET   A 1 61  ? 29.091 5.967   5.994   1.00 11.59 ?  61  MET   A HG2  1 
ATOM   1312 H HG3  . MET   A 1 61  ? 29.384 4.959   7.185   1.00 11.59 ?  61  MET   A HG3  1 
ATOM   1313 H HE1  . MET   A 1 61  ? 26.160 3.530   8.180   1.00 14.52 ?  61  MET   A HE1  1 
ATOM   1314 H HE2  . MET   A 1 61  ? 27.741 3.381   8.248   1.00 14.52 ?  61  MET   A HE2  1 
ATOM   1315 H HE3  . MET   A 1 61  ? 27.031 4.632   8.922   1.00 14.52 ?  61  MET   A HE3  1 
ATOM   1316 N N    . GLN   A 1 62  ? 30.329 9.044   6.182   1.00 8.87  ?  62  GLN   A N    1 
ATOM   1317 C CA   . GLN   A 1 62  ? 30.882 9.529   4.921   1.00 9.09  ?  62  GLN   A CA   1 
ATOM   1318 C C    . GLN   A 1 62  ? 32.351 9.905   5.061   1.00 9.31  ?  62  GLN   A C    1 
ATOM   1319 O O    . GLN   A 1 62  ? 33.158 9.606   4.175   1.00 9.90  ?  62  GLN   A O    1 
ATOM   1320 C CB   . GLN   A 1 62  ? 30.070 10.713  4.394   1.00 9.37  ?  62  GLN   A CB   1 
ATOM   1321 C CG   . GLN   A 1 62  ? 30.437 11.085  2.971   1.00 9.38  ?  62  GLN   A CG   1 
ATOM   1322 C CD   . GLN   A 1 62  ? 30.106 9.963   2.019   1.00 9.49  ?  62  GLN   A CD   1 
ATOM   1323 O OE1  . GLN   A 1 62  ? 28.930 9.654   1.819   1.00 10.16 ?  62  GLN   A OE1  1 
ATOM   1324 N NE2  . GLN   A 1 62  ? 31.121 9.294   1.487   1.00 10.07 ?  62  GLN   A NE2  1 
ATOM   1325 H H    . GLN   A 1 62  ? 29.709 9.537   6.518   1.00 10.65 ?  62  GLN   A H    1 
ATOM   1326 H HA   . GLN   A 1 62  ? 30.828 8.811   4.272   1.00 10.92 ?  62  GLN   A HA   1 
ATOM   1327 H HB2  . GLN   A 1 62  ? 29.129 10.483  4.411   1.00 11.26 ?  62  GLN   A HB2  1 
ATOM   1328 H HB3  . GLN   A 1 62  ? 30.235 11.484  4.959   1.00 11.26 ?  62  GLN   A HB3  1 
ATOM   1329 H HG2  . GLN   A 1 62  ? 29.930 11.866  2.704   1.00 11.26 ?  62  GLN   A HG2  1 
ATOM   1330 H HG3  . GLN   A 1 62  ? 31.388 11.263  2.916   1.00 11.26 ?  62  GLN   A HG3  1 
ATOM   1331 H HE21 . GLN   A 1 62  ? 31.932 9.527   1.666   1.00 12.09 ?  62  GLN   A HE21 1 
ATOM   1332 H HE22 . GLN   A 1 62  ? 30.974 8.640   0.948   1.00 12.09 ?  62  GLN   A HE22 1 
ATOM   1333 N N    . VAL   A 1 63  ? 32.717 10.580  6.155   1.00 9.66  ?  63  VAL   A N    1 
ATOM   1334 C CA   . VAL   A 1 63  ? 34.110 10.976  6.360   1.00 10.78 ?  63  VAL   A CA   1 
ATOM   1335 C C    . VAL   A 1 63  ? 35.010 9.742   6.407   1.00 10.13 ?  63  VAL   A C    1 
ATOM   1336 O O    . VAL   A 1 63  ? 36.064 9.685   5.755   1.00 10.62 ?  63  VAL   A O    1 
ATOM   1337 C CB   . VAL   A 1 63  ? 34.229 11.847  7.624   1.00 12.06 ?  63  VAL   A CB   1 
ATOM   1338 C CG1  . VAL   A 1 63  ? 35.679 12.093  7.978   1.00 13.89 ?  63  VAL   A CG1  1 
ATOM   1339 C CG2  . VAL   A 1 63  ? 33.499 13.172  7.418   1.00 12.62 ?  63  VAL   A CG2  1 
ATOM   1340 H H    . VAL   A 1 63  ? 32.178 10.814  6.791   1.00 11.60 ?  63  VAL   A H    1 
ATOM   1341 H HA   . VAL   A 1 63  ? 34.384 11.513  5.608   1.00 12.95 ?  63  VAL   A HA   1 
ATOM   1342 H HB   . VAL   A 1 63  ? 33.813 11.386  8.371   1.00 14.48 ?  63  VAL   A HB   1 
ATOM   1343 H HG11 . VAL   A 1 63  ? 35.727 12.821  8.614   1.00 16.68 ?  63  VAL   A HG11 1 
ATOM   1344 H HG12 . VAL   A 1 63  ? 36.052 11.287  8.366   1.00 16.68 ?  63  VAL   A HG12 1 
ATOM   1345 H HG13 . VAL   A 1 63  ? 36.162 12.328  7.169   1.00 16.68 ?  63  VAL   A HG13 1 
ATOM   1346 H HG21 . VAL   A 1 63  ? 33.593 13.715  8.220   1.00 15.15 ?  63  VAL   A HG21 1 
ATOM   1347 H HG22 . VAL   A 1 63  ? 33.885 13.636  6.660   1.00 15.15 ?  63  VAL   A HG22 1 
ATOM   1348 H HG23 . VAL   A 1 63  ? 32.557 12.996  7.253   1.00 15.15 ?  63  VAL   A HG23 1 
ATOM   1349 N N    . GLU   A 1 64  ? 34.597 8.729   7.172   1.00 9.98  ?  64  GLU   A N    1 
ATOM   1350 C CA   . GLU   A 1 64  ? 35.363 7.491   7.258   1.00 9.97  ?  64  GLU   A CA   1 
ATOM   1351 C C    . GLU   A 1 64  ? 35.445 6.806   5.899   1.00 9.65  ?  64  GLU   A C    1 
ATOM   1352 O O    . GLU   A 1 64  ? 36.493 6.259   5.518   1.00 10.06 ?  64  GLU   A O    1 
ATOM   1353 C CB   . GLU   A 1 64  ? 34.684 6.578   8.279   1.00 10.67 ?  64  GLU   A CB   1 
ATOM   1354 C CG   . GLU   A 1 64  ? 35.346 5.237   8.449   1.00 11.20 ?  64  GLU   A CG   1 
ATOM   1355 C CD   . GLU   A 1 64  ? 34.465 4.236   9.173   1.00 11.76 ?  64  GLU   A CD   1 
ATOM   1356 O OE1  . GLU   A 1 64  ? 33.221 4.329   9.048   1.00 12.50 ?  64  GLU   A OE1  1 
ATOM   1357 O OE2  . GLU   A 1 64  ? 35.024 3.336   9.848   1.00 12.42 -1 64  GLU   A OE2  1 
ATOM   1358 H H    . GLU   A 1 64  ? 33.874 8.731   7.637   1.00 11.98 ?  64  GLU   A H    1 
ATOM   1359 H HA   . GLU   A 1 64  ? 36.262 7.687   7.564   1.00 11.98 ?  64  GLU   A HA   1 
ATOM   1360 H HB2  . GLU   A 1 64  ? 34.695 7.026   9.145   1.00 12.81 ?  64  GLU   A HB2  1 
ATOM   1361 H HB3  . GLU   A 1 64  ? 33.769 6.432   8.002   1.00 12.81 ?  64  GLU   A HB3  1 
ATOM   1362 H HG2  . GLU   A 1 64  ? 35.564 4.864   7.578   1.00 13.45 ?  64  GLU   A HG2  1 
ATOM   1363 H HG3  . GLU   A 1 64  ? 36.161 5.347   8.967   1.00 13.45 ?  64  GLU   A HG3  1 
ATOM   1364 N N    . SER   A 1 65  ? 34.323 6.802   5.173   1.00 9.35  ?  65  SER   A N    1 
ATOM   1365 C CA   . SER   A 1 65  ? 34.264 6.151   3.868   1.00 9.33  ?  65  SER   A CA   1 
ATOM   1366 C C    . SER   A 1 65  ? 35.179 6.827   2.858   1.00 9.67  ?  65  SER   A C    1 
ATOM   1367 O O    . SER   A 1 65  ? 35.815 6.153   2.040   1.00 10.26 ?  65  SER   A O    1 
ATOM   1368 C CB   . SER   A 1 65  ? 32.826 6.156   3.346   1.00 9.27  ?  65  SER   A CB   1 
ATOM   1369 O OG   . SER   A 1 65  ? 31.982 5.336   4.140   1.00 9.87  ?  65  SER   A OG   1 
ATOM   1370 H H    . SER   A 1 65  ? 33.587 7.168   5.414   1.00 11.23 ?  65  SER   A H    1 
ATOM   1371 H HA   . SER   A 1 65  ? 34.551 5.230   3.956   1.00 11.21 ?  65  SER   A HA   1 
ATOM   1372 H HB2  . SER   A 1 65  ? 32.490 7.063   3.360   1.00 11.13 ?  65  SER   A HB2  1 
ATOM   1373 H HB3  . SER   A 1 65  ? 32.825 5.818   2.436   1.00 11.13 ?  65  SER   A HB3  1 
ATOM   1374 H HG   . SER   A 1 65  ? 31.976 5.621   4.934   1.00 11.85 ?  65  SER   A HG   1 
ATOM   1375 N N    . ASP   A 1 66  ? 35.249 8.161   2.887   1.00 9.73  ?  66  ASP   A N    1 
ATOM   1376 C CA   . ASP   A 1 66  ? 36.102 8.868   1.940   1.00 10.68 ?  66  ASP   A CA   1 
ATOM   1377 C C    . ASP   A 1 66  ? 37.568 8.507   2.161   1.00 10.84 ?  66  ASP   A C    1 
ATOM   1378 O O    . ASP   A 1 66  ? 38.328 8.339   1.200   1.00 11.50 ?  66  ASP   A O    1 
ATOM   1379 C CB   . ASP   A 1 66  ? 35.885 10.376  2.061   1.00 11.72 ?  66  ASP   A CB   1 
ATOM   1380 C CG   . ASP   A 1 66  ? 34.551 10.841  1.462   1.00 13.49 ?  66  ASP   A CG   1 
ATOM   1381 O OD1  . ASP   A 1 66  ? 33.833 10.039  0.825   1.00 13.47 ?  66  ASP   A OD1  1 
ATOM   1382 O OD2  . ASP   A 1 66  ? 34.237 12.036  1.623   1.00 16.53 -1 66  ASP   A OD2  1 
ATOM   1383 H H    . ASP   A 1 66  ? 34.812 8.672   3.432   1.00 11.69 ?  66  ASP   A H    1 
ATOM   1384 H HA   . ASP   A 1 66  ? 35.858 8.602   1.041   1.00 12.82 ?  66  ASP   A HA   1 
ATOM   1385 H HB2  . ASP   A 1 66  ? 35.885 10.622  3.000   1.00 14.07 ?  66  ASP   A HB2  1 
ATOM   1386 H HB3  . ASP   A 1 66  ? 36.603 10.836  1.599   1.00 14.07 ?  66  ASP   A HB3  1 
ATOM   1387 N N    . ASP   A 1 67  ? 37.981 8.367   3.421   1.00 10.93 ?  67  ASP   A N    1 
ATOM   1388 C CA   . ASP   A 1 67  ? 39.339 7.918   3.706   1.00 11.71 ?  67  ASP   A CA   1 
ATOM   1389 C C    . ASP   A 1 67  ? 39.560 6.484   3.226   1.00 11.47 ?  67  ASP   A C    1 
ATOM   1390 O O    . ASP   A 1 67  ? 40.621 6.164   2.679   1.00 12.19 ?  67  ASP   A O    1 
ATOM   1391 C CB   . ASP   A 1 67  ? 39.625 8.048   5.200   1.00 13.24 ?  67  ASP   A CB   1 
ATOM   1392 C CG   . ASP   A 1 67  ? 40.925 7.380   5.605   1.00 14.48 ?  67  ASP   A CG   1 
ATOM   1393 O OD1  . ASP   A 1 67  ? 42.000 8.003   5.450   1.00 17.02 ?  67  ASP   A OD1  1 
ATOM   1394 O OD2  . ASP   A 1 67  ? 40.861 6.218   6.068   1.00 14.10 -1 67  ASP   A OD2  1 
ATOM   1395 H H    . ASP   A 1 67  ? 37.498 8.520   4.114   1.00 13.12 ?  67  ASP   A H    1 
ATOM   1396 H HA   . ASP   A 1 67  ? 39.960 8.485   3.230   1.00 14.07 ?  67  ASP   A HA   1 
ATOM   1397 H HB2  . ASP   A 1 67  ? 39.685 8.986   5.424   1.00 15.90 ?  67  ASP   A HB2  1 
ATOM   1398 H HB3  . ASP   A 1 67  ? 38.901 7.629   5.696   1.00 15.90 ?  67  ASP   A HB3  1 
ATOM   1399 N N    A TYR   A 1 68  ? 38.567 5.606   3.421   0.86 10.59 ?  68  TYR   A N    1 
ATOM   1400 N N    B TYR   A 1 68  ? 38.569 5.605   3.419   0.14 11.12 ?  68  TYR   A N    1 
ATOM   1401 C CA   A TYR   A 1 68  ? 38.682 4.227   2.943   0.86 11.10 ?  68  TYR   A CA   1 
ATOM   1402 C CA   B TYR   A 1 68  ? 38.700 4.233   2.931   0.14 11.09 ?  68  TYR   A CA   1 
ATOM   1403 C C    A TYR   A 1 68  ? 38.911 4.182   1.434   0.86 10.61 ?  68  TYR   A C    1 
ATOM   1404 C C    B TYR   A 1 68  ? 38.937 4.210   1.426   0.14 10.62 ?  68  TYR   A C    1 
ATOM   1405 O O    A TYR   A 1 68  ? 39.778 3.443   0.948   0.86 10.99 ?  68  TYR   A O    1 
ATOM   1406 O O    B TYR   A 1 68  ? 39.845 3.527   0.937   0.14 10.61 ?  68  TYR   A O    1 
ATOM   1407 C CB   A TYR   A 1 68  ? 37.434 3.403   3.331   0.86 11.78 ?  68  TYR   A CB   1 
ATOM   1408 C CB   B TYR   A 1 68  ? 37.461 3.404   3.289   0.14 11.57 ?  68  TYR   A CB   1 
ATOM   1409 C CG   A TYR   A 1 68  ? 37.458 2.015   2.699   0.86 13.22 ?  68  TYR   A CG   1 
ATOM   1410 C CG   B TYR   A 1 68  ? 37.464 2.032   2.634   0.14 12.09 ?  68  TYR   A CG   1 
ATOM   1411 C CD1  A TYR   A 1 68  ? 37.004 1.821   1.395   0.86 14.62 ?  68  TYR   A CD1  1 
ATOM   1412 C CD1  B TYR   A 1 68  ? 36.897 1.838   1.378   0.14 12.25 ?  68  TYR   A CD1  1 
ATOM   1413 C CD2  A TYR   A 1 68  ? 38.002 0.926   3.364   0.86 14.77 ?  68  TYR   A CD2  1 
ATOM   1414 C CD2  B TYR   A 1 68  ? 38.054 0.940   3.258   0.14 12.45 ?  68  TYR   A CD2  1 
ATOM   1415 C CE1  A TYR   A 1 68  ? 37.076 0.596   0.779   0.86 15.75 ?  68  TYR   A CE1  1 
ATOM   1416 C CE1  B TYR   A 1 68  ? 36.910 0.599   0.768   0.14 12.37 ?  68  TYR   A CE1  1 
ATOM   1417 C CE2  A TYR   A 1 68  ? 38.066 -0.329  2.752   0.86 15.45 ?  68  TYR   A CE2  1 
ATOM   1418 C CE2  B TYR   A 1 68  ? 38.068 -0.308  2.655   0.14 12.41 ?  68  TYR   A CE2  1 
ATOM   1419 C CZ   A TYR   A 1 68  ? 37.610 -0.470  1.462   0.86 16.29 ?  68  TYR   A CZ   1 
ATOM   1420 C CZ   B TYR   A 1 68  ? 37.497 -0.468  1.410   0.14 12.47 ?  68  TYR   A CZ   1 
ATOM   1421 O OH   A TYR   A 1 68  ? 37.699 -1.688  0.848   0.86 17.69 ?  68  TYR   A OH   1 
ATOM   1422 O OH   B TYR   A 1 68  ? 37.514 -1.704  0.808   0.14 12.74 ?  68  TYR   A OH   1 
ATOM   1423 H H    A TYR   A 1 68  ? 37.822 5.780   3.820   0.86 12.71 ?  68  TYR   A H    1 
ATOM   1424 H H    B TYR   A 1 68  ? 37.826 5.771   3.824   0.14 13.36 ?  68  TYR   A H    1 
ATOM   1425 H HA   A TYR   A 1 68  ? 39.449 3.817   3.365   0.86 13.32 ?  68  TYR   A HA   1 
ATOM   1426 H HA   B TYR   A 1 68  ? 39.463 3.820   3.358   0.14 13.32 ?  68  TYR   A HA   1 
ATOM   1427 H HB2  A TYR   A 1 68  ? 37.417 3.288   4.292   0.86 14.14 ?  68  TYR   A HB2  1 
ATOM   1428 H HB2  B TYR   A 1 68  ? 37.434 3.273   4.251   0.14 13.90 ?  68  TYR   A HB2  1 
ATOM   1429 H HB3  A TYR   A 1 68  ? 36.639 3.858   3.026   0.86 14.14 ?  68  TYR   A HB3  1 
ATOM   1430 H HB3  B TYR   A 1 68  ? 36.665 3.873   2.996   0.14 13.90 ?  68  TYR   A HB3  1 
ATOM   1431 H HD1  A TYR   A 1 68  ? 36.655 2.548   0.923   0.86 17.55 ?  68  TYR   A HD1  1 
ATOM   1432 H HD1  B TYR   A 1 68  ? 36.501 2.555   0.939   0.14 14.71 ?  68  TYR   A HD1  1 
ATOM   1433 H HD2  A TYR   A 1 68  ? 38.334 1.031   4.220   0.86 17.74 ?  68  TYR   A HD2  1 
ATOM   1434 H HD2  B TYR   A 1 68  ? 38.441 1.047   4.096   0.14 14.95 ?  68  TYR   A HD2  1 
ATOM   1435 H HE1  A TYR   A 1 68  ? 36.753 0.492   -0.093  0.86 18.91 ?  68  TYR   A HE1  1 
ATOM   1436 H HE1  B TYR   A 1 68  ? 36.525 0.483   -0.071  0.14 14.86 ?  68  TYR   A HE1  1 
ATOM   1437 H HE2  A TYR   A 1 68  ? 38.435 -1.056  3.194   0.86 18.54 ?  68  TYR   A HE2  1 
ATOM   1438 H HE2  B TYR   A 1 68  ? 38.466 -1.032  3.084   0.14 14.90 ?  68  TYR   A HE2  1 
ATOM   1439 H HH   A TYR   A 1 68  ? 38.022 -2.256  1.377   0.86 21.23 ?  68  TYR   A HH   1 
ATOM   1440 H HH   B TYR   A 1 68  ? 37.901 -2.263  1.307   0.14 15.30 ?  68  TYR   A HH   1 
ATOM   1441 N N    . ILE   A 1 69  ? 38.120 4.947   0.671   1.00 10.41 ?  69  ILE   A N    1 
ATOM   1442 C CA   . ILE   A 1 69  ? 38.249 4.943   -0.784  1.00 10.53 ?  69  ILE   A CA   1 
ATOM   1443 C C    . ILE   A 1 69  ? 39.578 5.556   -1.218  1.00 10.31 ?  69  ILE   A C    1 
ATOM   1444 O O    . ILE   A 1 69  ? 40.224 5.067   -2.150  1.00 10.75 ?  69  ILE   A O    1 
ATOM   1445 C CB   . ILE   A 1 69  ? 37.050 5.657   -1.439  1.00 11.47 ?  69  ILE   A CB   1 
ATOM   1446 C CG1  . ILE   A 1 69  ? 35.734 4.929   -1.152  1.00 12.04 ?  69  ILE   A CG1  1 
ATOM   1447 C CG2  . ILE   A 1 69  ? 37.280 5.848   -2.944  1.00 13.01 ?  69  ILE   A CG2  1 
ATOM   1448 C CD1  . ILE   A 1 69  ? 35.559 3.627   -1.907  1.00 12.57 ?  69  ILE   A CD1  1 
ATOM   1449 H H    A ILE   A 1 69  ? 37.509 5.471   0.971   0.86 12.50 ?  69  ILE   A H    1 
ATOM   1450 H H    B ILE   A 1 69  ? 37.494 5.452   0.972   0.14 12.50 ?  69  ILE   A H    1 
ATOM   1451 H HA   . ILE   A 1 69  ? 38.242 4.022   -1.091  1.00 12.64 ?  69  ILE   A HA   1 
ATOM   1452 H HB   . ILE   A 1 69  ? 36.987 6.537   -1.040  1.00 13.77 ?  69  ILE   A HB   1 
ATOM   1453 H HG12 . ILE   A 1 69  ? 35.695 4.730   -0.203  1.00 14.45 ?  69  ILE   A HG12 1 
ATOM   1454 H HG13 . ILE   A 1 69  ? 35.001 5.515   -1.393  1.00 14.45 ?  69  ILE   A HG13 1 
ATOM   1455 H HG21 . ILE   A 1 69  ? 36.433 6.060   -3.367  1.00 15.62 ?  69  ILE   A HG21 1 
ATOM   1456 H HG22 . ILE   A 1 69  ? 37.904 6.585   -3.079  1.00 15.62 ?  69  ILE   A HG22 1 
ATOM   1457 H HG23 . ILE   A 1 69  ? 37.643 5.034   -3.318  1.00 15.62 ?  69  ILE   A HG23 1 
ATOM   1458 H HD11 . ILE   A 1 69  ? 34.745 3.199   -1.596  1.00 15.09 ?  69  ILE   A HD11 1 
ATOM   1459 H HD12 . ILE   A 1 69  ? 35.489 3.819   -2.854  1.00 15.09 ?  69  ILE   A HD12 1 
ATOM   1460 H HD13 . ILE   A 1 69  ? 36.320 3.056   -1.735  1.00 15.09 ?  69  ILE   A HD13 1 
ATOM   1461 N N    . ALA   A 1 70  ? 39.998 6.640   -0.566  1.00 10.58 ?  70  ALA   A N    1 
ATOM   1462 C CA   . ALA   A 1 70  ? 41.274 7.244   -0.932  1.00 11.44 ?  70  ALA   A CA   1 
ATOM   1463 C C    . ALA   A 1 70  ? 42.422 6.255   -0.766  1.00 11.51 ?  70  ALA   A C    1 
ATOM   1464 O O    . ALA   A 1 70  ? 43.374 6.269   -1.550  1.00 13.49 ?  70  ALA   A O    1 
ATOM   1465 C CB   . ALA   A 1 70  ? 41.524 8.497   -0.095  1.00 12.00 ?  70  ALA   A CB   1 
ATOM   1466 H H    . ALA   A 1 70  ? 39.575 7.032   0.071   1.00 12.70 ?  70  ALA   A H    1 
ATOM   1467 H HA   . ALA   A 1 70  ? 41.239 7.513   -1.863  1.00 13.74 ?  70  ALA   A HA   1 
ATOM   1468 H HB1  . ALA   A 1 70  ? 42.381 8.880   -0.355  1.00 14.41 ?  70  ALA   A HB1  1 
ATOM   1469 H HB2  . ALA   A 1 70  ? 40.816 9.134   -0.255  1.00 14.41 ?  70  ALA   A HB2  1 
ATOM   1470 H HB3  . ALA   A 1 70  ? 41.549 8.249   0.843   1.00 14.41 ?  70  ALA   A HB3  1 
ATOM   1471 N N    . THR   A 1 71  ? 42.335 5.367   0.223   1.00 11.26 ?  71  THR   A N    1 
ATOM   1472 C CA   . THR   A 1 71  ? 43.391 4.389   0.464   1.00 12.70 ?  71  THR   A CA   1 
ATOM   1473 C C    . THR   A 1 71  ? 43.276 3.167   -0.439  1.00 12.57 ?  71  THR   A C    1 
ATOM   1474 O O    . THR   A 1 71  ? 44.292 2.673   -0.950  1.00 14.54 ?  71  THR   A O    1 
ATOM   1475 C CB   . THR   A 1 71  ? 43.334 3.939   1.921   1.00 14.31 ?  71  THR   A CB   1 
ATOM   1476 O OG1  . THR   A 1 71  ? 43.613 5.058   2.769   1.00 15.47 ?  71  THR   A OG1  1 
ATOM   1477 C CG2  . THR   A 1 71  ? 44.329 2.808   2.192   1.00 15.61 ?  71  THR   A CG2  1 
ATOM   1478 H H    . THR   A 1 71  ? 41.667 5.299   0.758   1.00 13.53 ?  71  THR   A H    1 
ATOM   1479 H HA   . THR   A 1 71  ? 44.252 4.796   0.299   1.00 15.25 ?  71  THR   A HA   1 
ATOM   1480 H HB   . THR   A 1 71  ? 42.444 3.602   2.115   1.00 17.18 ?  71  THR   A HB   1 
ATOM   1481 H HG1  . THR   A 1 71  ? 43.589 4.812   3.571   1.00 18.57 ?  71  THR   A HG1  1 
ATOM   1482 H HG21 . THR   A 1 71  ? 44.486 2.727   3.146   1.00 18.74 ?  71  THR   A HG21 1 
ATOM   1483 H HG22 . THR   A 1 71  ? 43.984 1.962   1.861   1.00 18.74 ?  71  THR   A HG22 1 
ATOM   1484 H HG23 . THR   A 1 71  ? 45.176 2.995   1.753   1.00 18.74 ?  71  THR   A HG23 1 
ATOM   1485 N N    . ASN   A 1 72  ? 42.054 2.652   -0.623  1.00 11.73 ?  72  ASN   A N    1 
ATOM   1486 C CA   . ASN   A 1 72  ? 41.830 1.326   -1.187  1.00 12.25 ?  72  ASN   A CA   1 
ATOM   1487 C C    . ASN   A 1 72  ? 41.195 1.320   -2.566  1.00 12.35 ?  72  ASN   A C    1 
ATOM   1488 O O    . ASN   A 1 72  ? 41.202 0.269   -3.221  1.00 13.56 ?  72  ASN   A O    1 
ATOM   1489 C CB   . ASN   A 1 72  ? 40.944 0.507   -0.241  1.00 12.65 ?  72  ASN   A CB   1 
ATOM   1490 C CG   . ASN   A 1 72  ? 41.567 0.352   1.118   1.00 13.40 ?  72  ASN   A CG   1 
ATOM   1491 O OD1  . ASN   A 1 72  ? 41.107 0.946   2.093   1.00 15.06 ?  72  ASN   A OD1  1 
ATOM   1492 N ND2  . ASN   A 1 72  ? 42.627 -0.426  1.193   1.00 14.45 ?  72  ASN   A ND2  1 
ATOM   1493 H H    . ASN   A 1 72  ? 41.321 3.065   -0.425  1.00 14.09 ?  72  ASN   A H    1 
ATOM   1494 H HA   . ASN   A 1 72  ? 42.676 0.870   -1.259  1.00 14.71 ?  72  ASN   A HA   1 
ATOM   1495 H HB2  . ASN   A 1 72  ? 40.087 0.952   -0.132  1.00 15.19 ?  72  ASN   A HB2  1 
ATOM   1496 H HB3  . ASN   A 1 72  ? 40.810 -0.381  -0.613  1.00 15.19 ?  72  ASN   A HB3  1 
ATOM   1497 H HD21 . ASN   A 1 72  ? 43.024 -0.540  1.950   1.00 17.35 ?  72  ASN   A HD21 1 
ATOM   1498 H HD22 . ASN   A 1 72  ? 42.926 -0.815  0.489   1.00 17.35 ?  72  ASN   A HD22 1 
ATOM   1499 N N    . GLY   A 1 73  ? 40.642 2.437   -3.020  1.00 11.89 ?  73  GLY   A N    1 
ATOM   1500 C CA   . GLY   A 1 73  ? 39.899 2.457   -4.255  1.00 11.75 ?  73  GLY   A CA   1 
ATOM   1501 C C    . GLY   A 1 73  ? 38.504 1.880   -4.086  1.00 11.15 ?  73  GLY   A C    1 
ATOM   1502 O O    . GLY   A 1 73  ? 38.124 1.413   -3.007  1.00 11.69 ?  73  GLY   A O    1 
ATOM   1503 H H    . GLY   A 1 73  ? 40.681 3.203   -2.624  1.00 14.27 ?  73  GLY   A H    1 
ATOM   1504 H HA2  . GLY   A 1 73  ? 39.821 3.371   -4.571  1.00 14.11 ?  73  GLY   A HA2  1 
ATOM   1505 H HA3  . GLY   A 1 73  ? 40.371 1.938   -4.927  1.00 14.11 ?  73  GLY   A HA3  1 
ATOM   1506 N N    . PRO   A 1 74  ? 37.723 1.899   -5.165  1.00 11.37 ?  74  PRO   A N    1 
ATOM   1507 C CA   . PRO   A 1 74  ? 36.326 1.461   -5.085  1.00 11.44 ?  74  PRO   A CA   1 
ATOM   1508 C C    . PRO   A 1 74  ? 36.183 -0.023  -4.772  1.00 10.82 ?  74  PRO   A C    1 
ATOM   1509 O O    . PRO   A 1 74  ? 37.044 -0.855  -5.073  1.00 11.78 ?  74  PRO   A O    1 
ATOM   1510 C CB   . PRO   A 1 74  ? 35.777 1.768   -6.485  1.00 13.12 ?  74  PRO   A CB   1 
ATOM   1511 C CG   . PRO   A 1 74  ? 36.725 2.768   -7.077  1.00 15.40 ?  74  PRO   A CG   1 
ATOM   1512 C CD   . PRO   A 1 74  ? 38.066 2.428   -6.497  1.00 13.12 ?  74  PRO   A CD   1 
ATOM   1513 H HA   . PRO   A 1 74  ? 35.841 1.985   -4.427  1.00 13.73 ?  74  PRO   A HA   1 
ATOM   1514 H HB2  . PRO   A 1 74  ? 35.759 0.957   -7.015  1.00 15.75 ?  74  PRO   A HB2  1 
ATOM   1515 H HB3  . PRO   A 1 74  ? 34.885 2.149   -6.411  1.00 15.75 ?  74  PRO   A HB3  1 
ATOM   1516 H HG2  . PRO   A 1 74  ? 36.740 2.678   -8.043  1.00 18.49 ?  74  PRO   A HG2  1 
ATOM   1517 H HG3  . PRO   A 1 74  ? 36.462 3.665   -6.821  1.00 18.49 ?  74  PRO   A HG3  1 
ATOM   1518 H HD2  . PRO   A 1 74  ? 38.508 1.748   -7.031  1.00 15.75 ?  74  PRO   A HD2  1 
ATOM   1519 H HD3  . PRO   A 1 74  ? 38.611 3.230   -6.424  1.00 15.75 ?  74  PRO   A HD3  1 
ATOM   1520 N N    . LEU   A 1 75  ? 35.042 -0.348  -4.175  1.00 10.17 ?  75  LEU   A N    1 
ATOM   1521 C CA   . LEU   A 1 75  ? 34.635 -1.734  -4.023  1.00 10.10 ?  75  LEU   A CA   1 
ATOM   1522 C C    . LEU   A 1 75  ? 34.237 -2.308  -5.379  1.00 10.50 ?  75  LEU   A C    1 
ATOM   1523 O O    . LEU   A 1 75  ? 34.125 -1.593  -6.379  1.00 12.24 ?  75  LEU   A O    1 
ATOM   1524 C CB   . LEU   A 1 75  ? 33.451 -1.853  -3.058  1.00 10.10 ?  75  LEU   A CB   1 
ATOM   1525 C CG   . LEU   A 1 75  ? 33.694 -1.450  -1.604  1.00 11.80 ?  75  LEU   A CG   1 
ATOM   1526 C CD1  . LEU   A 1 75  ? 32.416 -1.611  -0.780  1.00 13.58 ?  75  LEU   A CD1  1 
ATOM   1527 C CD2  . LEU   A 1 75  ? 34.828 -2.217  -0.981  1.00 15.06 ?  75  LEU   A CD2  1 
ATOM   1528 H H    . LEU   A 1 75  ? 34.479 0.223   -3.858  1.00 12.21 ?  75  LEU   A H    1 
ATOM   1529 H HA   . LEU   A 1 75  ? 35.373 -2.248  -3.680  1.00 12.12 ?  75  LEU   A HA   1 
ATOM   1530 H HB2  . LEU   A 1 75  ? 32.730 -1.296  -3.393  1.00 12.13 ?  75  LEU   A HB2  1 
ATOM   1531 H HB3  . LEU   A 1 75  ? 33.160 -2.779  -3.057  1.00 12.13 ?  75  LEU   A HB3  1 
ATOM   1532 H HG   . LEU   A 1 75  ? 33.941 -0.514  -1.586  1.00 14.17 ?  75  LEU   A HG   1 
ATOM   1533 H HD11 . LEU   A 1 75  ? 32.600 -1.345  0.136   1.00 16.30 ?  75  LEU   A HD11 1 
ATOM   1534 H HD12 . LEU   A 1 75  ? 31.729 -1.037  -1.157  1.00 16.30 ?  75  LEU   A HD12 1 
ATOM   1535 H HD13 . LEU   A 1 75  ? 32.134 -2.534  -0.809  1.00 16.30 ?  75  LEU   A HD13 1 
ATOM   1536 H HD21 . LEU   A 1 75  ? 34.888 -1.987  -0.042  1.00 18.08 ?  75  LEU   A HD21 1 
ATOM   1537 H HD22 . LEU   A 1 75  ? 34.660 -3.169  -1.079  1.00 18.08 ?  75  LEU   A HD22 1 
ATOM   1538 H HD23 . LEU   A 1 75  ? 35.658 -1.983  -1.431  1.00 18.08 ?  75  LEU   A HD23 1 
ATOM   1539 N N    . LYS   A 1 76  ? 34.050 -3.628  -5.400  1.00 11.10 ?  76  LYS   A N    1 
ATOM   1540 C CA   . LYS   A 1 76  ? 33.441 -4.342  -6.517  1.00 11.68 ?  76  LYS   A CA   1 
ATOM   1541 C C    . LYS   A 1 76  ? 31.928 -4.426  -6.313  1.00 10.37 ?  76  LYS   A C    1 
ATOM   1542 O O    . LYS   A 1 76  ? 31.456 -4.565  -5.188  1.00 10.25 ?  76  LYS   A O    1 
ATOM   1543 C CB   . LYS   A 1 76  ? 33.983 -5.783  -6.584  1.00 13.36 ?  76  LYS   A CB   1 
ATOM   1544 C CG   . LYS   A 1 76  ? 35.496 -5.894  -6.781  1.00 15.08 ?  76  LYS   A CG   1 
ATOM   1545 C CD   . LYS   A 1 76  ? 36.023 -7.304  -6.583  1.00 16.59 ?  76  LYS   A CD   1 
ATOM   1546 C CE   . LYS   A 1 76  ? 37.518 -7.368  -6.812  1.00 19.06 ?  76  LYS   A CE   1 
ATOM   1547 N NZ   . LYS   A 1 76  ? 38.042 -8.734  -6.607  1.00 20.21 ?  76  LYS   A NZ   1 
ATOM   1548 H H    . LYS   A 1 76  ? 34.279 -4.147  -4.754  1.00 13.33 ?  76  LYS   A H    1 
ATOM   1549 H HA   . LYS   A 1 76  ? 33.629 -3.892  -7.356  1.00 14.03 ?  76  LYS   A HA   1 
ATOM   1550 H HB2  . LYS   A 1 76  ? 33.763 -6.235  -5.757  1.00 16.05 ?  76  LYS   A HB2  1 
ATOM   1551 H HB3  . LYS   A 1 76  ? 33.559 -6.239  -7.329  1.00 16.05 ?  76  LYS   A HB3  1 
ATOM   1552 H HG2  . LYS   A 1 76  ? 35.719 -5.614  -7.685  1.00 18.10 ?  76  LYS   A HG2  1 
ATOM   1553 H HG3  . LYS   A 1 76  ? 35.941 -5.315  -6.140  1.00 18.10 ?  76  LYS   A HG3  1 
ATOM   1554 H HD2  . LYS   A 1 76  ? 35.838 -7.590  -5.674  1.00 19.92 ?  76  LYS   A HD2  1 
ATOM   1555 H HD3  . LYS   A 1 76  ? 35.590 -7.899  -7.217  1.00 19.92 ?  76  LYS   A HD3  1 
ATOM   1556 H HE2  . LYS   A 1 76  ? 37.712 -7.098  -7.722  1.00 22.88 ?  76  LYS   A HE2  1 
ATOM   1557 H HE3  . LYS   A 1 76  ? 37.960 -6.774  -6.184  1.00 22.88 ?  76  LYS   A HE3  1 
ATOM   1558 H HZ1  . LYS   A 1 76  ? 38.919 -8.751  -6.746  1.00 24.26 ?  76  LYS   A HZ1  1 
ATOM   1559 H HZ2  . LYS   A 1 76  ? 37.875 -9.006  -5.775  1.00 24.26 ?  76  LYS   A HZ2  1 
ATOM   1560 H HZ3  . LYS   A 1 76  ? 37.649 -9.300  -7.175  1.00 24.26 ?  76  LYS   A HZ3  1 
ATOM   1561 N N    . VAL   A 1 77  ? 31.165 -4.403  -7.413  1.00 10.54 ?  77  VAL   A N    1 
ATOM   1562 C CA   . VAL   A 1 77  ? 29.758 -4.790  -7.317  1.00 10.54 ?  77  VAL   A CA   1 
ATOM   1563 C C    . VAL   A 1 77  ? 29.700 -6.246  -6.878  1.00 9.61  ?  77  VAL   A C    1 
ATOM   1564 O O    . VAL   A 1 77  ? 30.366 -7.110  -7.461  1.00 10.23 ?  77  VAL   A O    1 
ATOM   1565 C CB   . VAL   A 1 77  ? 29.017 -4.565  -8.645  1.00 11.76 ?  77  VAL   A CB   1 
ATOM   1566 C CG1  . VAL   A 1 77  ? 27.566 -5.020  -8.524  1.00 12.35 ?  77  VAL   A CG1  1 
ATOM   1567 C CG2  . VAL   A 1 77  ? 29.084 -3.100  -9.055  1.00 13.48 ?  77  VAL   A CG2  1 
ATOM   1568 H H    . VAL   A 1 77  ? 31.435 -4.166  -8.192  1.00 12.65 ?  77  VAL   A H    1 
ATOM   1569 H HA   . VAL   A 1 77  ? 29.330 -4.250  -6.634  1.00 12.66 ?  77  VAL   A HA   1 
ATOM   1570 H HB   . VAL   A 1 77  ? 29.449 -5.091  -9.337  1.00 14.13 ?  77  VAL   A HB   1 
ATOM   1571 H HG11 . VAL   A 1 77  ? 27.080 -4.720  -9.305  1.00 14.83 ?  77  VAL   A HG11 1 
ATOM   1572 H HG12 . VAL   A 1 77  ? 27.540 -5.988  -8.469  1.00 14.83 ?  77  VAL   A HG12 1 
ATOM   1573 H HG13 . VAL   A 1 77  ? 27.181 -4.631  -7.723  1.00 14.83 ?  77  VAL   A HG13 1 
ATOM   1574 H HG21 . VAL   A 1 77  ? 28.577 -2.984  -9.871  1.00 16.18 ?  77  VAL   A HG21 1 
ATOM   1575 H HG22 . VAL   A 1 77  ? 28.702 -2.561  -8.345  1.00 16.18 ?  77  VAL   A HG22 1 
ATOM   1576 H HG23 . VAL   A 1 77  ? 30.010 -2.854  -9.198  1.00 16.18 ?  77  VAL   A HG23 1 
ATOM   1577 N N    . GLY   A 1 78  ? 28.919 -6.523  -5.830  1.00 9.77  ?  78  GLY   A N    1 
ATOM   1578 C CA   . GLY   A 1 78  ? 28.910 -7.812  -5.175  1.00 10.02 ?  78  GLY   A CA   1 
ATOM   1579 C C    . GLY   A 1 78  ? 29.836 -7.906  -3.982  1.00 9.40  ?  78  GLY   A C    1 
ATOM   1580 O O    . GLY   A 1 78  ? 29.784 -8.909  -3.261  1.00 10.12 ?  78  GLY   A O    1 
ATOM   1581 H H    . GLY   A 1 78  ? 28.365 -5.954  -5.482  1.00 11.73 ?  78  GLY   A H    1 
ATOM   1582 H HA2  . GLY   A 1 78  ? 28.011 -8.008  -4.878  1.00 12.04 ?  78  GLY   A HA2  1 
ATOM   1583 H HA3  . GLY   A 1 78  ? 29.172 -8.489  -5.819  1.00 12.04 ?  78  GLY   A HA3  1 
ATOM   1584 N N    . GLY   A 1 79  ? 30.690 -6.905  -3.765  1.00 9.55  ?  79  GLY   A N    1 
ATOM   1585 C CA   . GLY   A 1 79  ? 31.661 -6.922  -2.695  1.00 9.88  ?  79  GLY   A CA   1 
ATOM   1586 C C    . GLY   A 1 79  ? 31.217 -6.126  -1.476  1.00 9.25  ?  79  GLY   A C    1 
ATOM   1587 O O    . GLY   A 1 79  ? 30.099 -5.616  -1.390  1.00 9.71  ?  79  GLY   A O    1 
ATOM   1588 H H    . GLY   A 1 79  ? 30.725 -6.192  -4.244  1.00 11.46 ?  79  GLY   A H    1 
ATOM   1589 H HA2  . GLY   A 1 79  ? 31.819 -7.846  -2.422  1.00 11.86 ?  79  GLY   A HA2  1 
ATOM   1590 H HA3  . GLY   A 1 79  ? 32.499 -6.558  -3.014  1.00 11.86 ?  79  GLY   A HA3  1 
ATOM   1591 N N    . SER   A 1 80  ? 32.133 -6.039  -0.511  1.00 9.99  ?  80  SER   A N    1 
ATOM   1592 C CA   . SER   A 1 80  ? 31.825 -5.408  0.763   1.00 9.50  ?  80  SER   A CA   1 
ATOM   1593 C C    . SER   A 1 80  ? 33.103 -4.960  1.455   1.00 9.54  ?  80  SER   A C    1 
ATOM   1594 O O    . SER   A 1 80  ? 34.215 -5.381  1.110   1.00 10.84 ?  80  SER   A O    1 
ATOM   1595 C CB   . SER   A 1 80  ? 31.069 -6.371  1.685   1.00 10.36 ?  80  SER   A CB   1 
ATOM   1596 O OG   . SER   A 1 80  ? 31.908 -7.422  2.147   1.00 12.24 ?  80  SER   A OG   1 
ATOM   1597 H H    . SER   A 1 80  ? 32.943 -6.323  -0.578  1.00 11.99 ?  80  SER   A H    1 
ATOM   1598 H HA   . SER   A 1 80  ? 31.271 -4.629  0.595   1.00 11.40 ?  80  SER   A HA   1 
ATOM   1599 H HB2  . SER   A 1 80  ? 30.736 -5.877  2.447   1.00 12.44 ?  80  SER   A HB2  1 
ATOM   1600 H HB3  . SER   A 1 80  ? 30.327 -6.757  1.190   1.00 12.44 ?  80  SER   A HB3  1 
ATOM   1601 H HG   . SER   A 1 80  ? 32.206 -7.857  1.488   1.00 14.70 ?  80  SER   A HG   1 
ATOM   1602 N N    . CYS   A 1 81  ? 32.917 -4.113  2.466   1.00 9.15  ?  81  CYS   A N    1 
ATOM   1603 C CA   . CYS   A 1 81  ? 33.972 -3.829  3.427   1.00 9.27  ?  81  CYS   A CA   1 
ATOM   1604 C C    . CYS   A 1 81  ? 33.339 -3.593  4.788   1.00 9.05  ?  81  CYS   A C    1 
ATOM   1605 O O    . CYS   A 1 81  ? 32.175 -3.203  4.885   1.00 10.12 ?  81  CYS   A O    1 
ATOM   1606 C CB   . CYS   A 1 81  ? 34.840 -2.640  3.006   1.00 10.10 ?  81  CYS   A CB   1 
ATOM   1607 S SG   . CYS   A 1 81  ? 33.952 -1.060  3.030   1.00 10.35 ?  81  CYS   A SG   1 
ATOM   1608 H H    . CYS   A 1 81  ? 32.177 -3.688  2.619   1.00 10.98 ?  81  CYS   A H    1 
ATOM   1609 H HA   . CYS   A 1 81  ? 34.544 -4.605  3.492   1.00 11.13 ?  81  CYS   A HA   1 
ATOM   1610 H HB2  . CYS   A 1 81  ? 35.593 -2.575  3.614   1.00 12.13 ?  81  CYS   A HB2  1 
ATOM   1611 H HB3  . CYS   A 1 81  ? 35.162 -2.795  2.101   1.00 12.13 ?  81  CYS   A HB3  1 
ATOM   1612 H HG   . CYS   A 1 81  ? 34.705 -0.184  2.687   1.00 12.42 ?  81  CYS   A HG   1 
ATOM   1613 N N    . VAL   A 1 82  ? 34.115 -3.851  5.834   1.00 9.45  ?  82  VAL   A N    1 
ATOM   1614 C CA   . VAL   A 1 82  ? 33.693 -3.619  7.209   1.00 9.77  ?  82  VAL   A CA   1 
ATOM   1615 C C    . VAL   A 1 82  ? 34.303 -2.309  7.684   1.00 9.92  ?  82  VAL   A C    1 
ATOM   1616 O O    . VAL   A 1 82  ? 35.530 -2.140  7.664   1.00 10.98 ?  82  VAL   A O    1 
ATOM   1617 C CB   . VAL   A 1 82  ? 34.124 -4.764  8.138   1.00 11.35 ?  82  VAL   A CB   1 
ATOM   1618 C CG1  . VAL   A 1 82  ? 33.678 -4.466  9.563   1.00 12.84 ?  82  VAL   A CG1  1 
ATOM   1619 C CG2  . VAL   A 1 82  ? 33.571 -6.095  7.666   1.00 12.34 ?  82  VAL   A CG2  1 
ATOM   1620 H H    . VAL   A 1 82  ? 34.916 -4.169  5.768   1.00 11.35 ?  82  VAL   A H    1 
ATOM   1621 H HA   . VAL   A 1 82  ? 32.729 -3.542  7.242   1.00 11.73 ?  82  VAL   A HA   1 
ATOM   1622 H HB   . VAL   A 1 82  ? 35.092 -4.824  8.137   1.00 13.63 ?  82  VAL   A HB   1 
ATOM   1623 H HG11 . VAL   A 1 82  ? 33.745 -5.276  10.091  1.00 15.41 ?  82  VAL   A HG11 1 
ATOM   1624 H HG12 . VAL   A 1 82  ? 34.250 -3.778  9.941   1.00 15.41 ?  82  VAL   A HG12 1 
ATOM   1625 H HG13 . VAL   A 1 82  ? 32.757 -4.158  9.548   1.00 15.41 ?  82  VAL   A HG13 1 
ATOM   1626 H HG21 . VAL   A 1 82  ? 33.836 -6.787  8.292   1.00 14.81 ?  82  VAL   A HG21 1 
ATOM   1627 H HG22 . VAL   A 1 82  ? 32.605 -6.038  7.623   1.00 14.81 ?  82  VAL   A HG22 1 
ATOM   1628 H HG23 . VAL   A 1 82  ? 33.931 -6.291  6.786   1.00 14.81 ?  82  VAL   A HG23 1 
ATOM   1629 N N    . LEU   A 1 83  ? 33.453 -1.388  8.123   1.00 9.48  ?  83  LEU   A N    1 
ATOM   1630 C CA   . LEU   A 1 83  ? 33.875 -0.121  8.705   1.00 9.74  ?  83  LEU   A CA   1 
ATOM   1631 C C    . LEU   A 1 83  ? 33.169 0.051   10.047  1.00 9.69  ?  83  LEU   A C    1 
ATOM   1632 O O    . LEU   A 1 83  ? 32.453 -0.841  10.517  1.00 10.16 ?  83  LEU   A O    1 
ATOM   1633 C CB   . LEU   A 1 83  ? 33.618 1.044   7.733   1.00 10.24 ?  83  LEU   A CB   1 
ATOM   1634 C CG   . LEU   A 1 83  ? 34.509 1.044   6.482   1.00 10.99 ?  83  LEU   A CG   1 
ATOM   1635 C CD1  . LEU   A 1 83  ? 34.065 2.093   5.486   1.00 11.53 ?  83  LEU   A CD1  1 
ATOM   1636 C CD2  . LEU   A 1 83  ? 35.984 1.244   6.852   1.00 11.92 ?  83  LEU   A CD2  1 
ATOM   1637 H H    . LEU   A 1 83  ? 32.597 -1.480  8.086   1.00 11.39 ?  83  LEU   A H    1 
ATOM   1638 H HA   . LEU   A 1 83  ? 34.827 -0.155  8.872   1.00 11.69 ?  83  LEU   A HA   1 
ATOM   1639 H HB2  . LEU   A 1 83  ? 32.695 1.006   7.432   1.00 12.29 ?  83  LEU   A HB2  1 
ATOM   1640 H HB3  . LEU   A 1 83  ? 33.770 1.881   8.200   1.00 12.29 ?  83  LEU   A HB3  1 
ATOM   1641 H HG   . LEU   A 1 83  ? 34.435 0.178   6.054   1.00 13.19 ?  83  LEU   A HG   1 
ATOM   1642 H HD11 . LEU   A 1 83  ? 34.650 2.054   4.711   1.00 13.85 ?  83  LEU   A HD11 1 
ATOM   1643 H HD12 . LEU   A 1 83  ? 33.152 1.904   5.221   1.00 13.85 ?  83  LEU   A HD12 1 
ATOM   1644 H HD13 . LEU   A 1 83  ? 34.121 2.965   5.901   1.00 13.85 ?  83  LEU   A HD13 1 
ATOM   1645 H HD21 . LEU   A 1 83  ? 36.495 1.400   6.040   1.00 14.31 ?  83  LEU   A HD21 1 
ATOM   1646 H HD22 . LEU   A 1 83  ? 36.063 2.012   7.441   1.00 14.31 ?  83  LEU   A HD22 1 
ATOM   1647 H HD23 . LEU   A 1 83  ? 36.314 0.449   7.300   1.00 14.31 ?  83  LEU   A HD23 1 
ATOM   1648 N N    . SER   A 1 84  ? 33.391 1.197   10.684  1.00 10.17 ?  84  SER   A N    1 
ATOM   1649 C CA   . SER   A 1 84  ? 32.755 1.454   11.965  1.00 10.55 ?  84  SER   A CA   1 
ATOM   1650 C C    . SER   A 1 84  ? 31.235 1.526   11.827  1.00 10.33 ?  84  SER   A C    1 
ATOM   1651 O O    . SER   A 1 84  ? 30.700 1.992   10.821  1.00 10.78 ?  84  SER   A O    1 
ATOM   1652 C CB   . SER   A 1 84  ? 33.248 2.779   12.534  1.00 11.46 ?  84  SER   A CB   1 
ATOM   1653 O OG   . SER   A 1 84  ? 32.619 3.052   13.772  1.00 12.48 ?  84  SER   A OG   1 
ATOM   1654 H H    . SER   A 1 84  ? 33.897 1.838   10.385  1.00 12.21 ?  84  SER   A H    1 
ATOM   1655 H HA   . SER   A 1 84  ? 32.984 0.747   12.578  1.00 12.67 ?  84  SER   A HA   1 
ATOM   1656 H HB2  . SER   A 1 84  ? 34.210 2.733   12.662  1.00 13.76 ?  84  SER   A HB2  1 
ATOM   1657 H HB3  . SER   A 1 84  ? 33.036 3.494   11.906  1.00 13.76 ?  84  SER   A HB3  1 
ATOM   1658 H HG   . SER   A 1 84  ? 32.897 3.779   14.080  1.00 14.98 ?  84  SER   A HG   1 
ATOM   1659 N N    . GLY   A 1 85  ? 30.536 1.101   12.875  1.00 10.97 ?  85  GLY   A N    1 
ATOM   1660 C CA   . GLY   A 1 85  ? 29.114 1.339   12.971  1.00 11.73 ?  85  GLY   A CA   1 
ATOM   1661 C C    . GLY   A 1 85  ? 28.746 2.645   13.630  1.00 10.97 ?  85  GLY   A C    1 
ATOM   1662 O O    . GLY   A 1 85  ? 27.556 2.953   13.752  1.00 11.57 ?  85  GLY   A O    1 
ATOM   1663 H H    . GLY   A 1 85  ? 30.875 0.663   13.534  1.00 13.17 ?  85  GLY   A H    1 
ATOM   1664 H HA2  . GLY   A 1 85  ? 28.736 1.332   12.079  1.00 14.09 ?  85  GLY   A HA2  1 
ATOM   1665 H HA3  . GLY   A 1 85  ? 28.713 0.625   13.478  1.00 14.09 ?  85  GLY   A HA3  1 
ATOM   1666 N N    . HIS   A 1 86  ? 29.729 3.427   14.067  1.00 10.52 ?  86  HIS   A N    1 
ATOM   1667 C CA   . HIS   A 1 86  ? 29.491 4.758   14.643  1.00 11.21 ?  86  HIS   A CA   1 
ATOM   1668 C C    . HIS   A 1 86  ? 28.506 4.622   15.798  1.00 12.20 ?  86  HIS   A C    1 
ATOM   1669 O O    . HIS   A 1 86  ? 28.687 3.738   16.652  1.00 13.03 ?  86  HIS   A O    1 
ATOM   1670 C CB   . HIS   A 1 86  ? 29.099 5.745   13.548  1.00 11.32 ?  86  HIS   A CB   1 
ATOM   1671 C CG   . HIS   A 1 86  ? 30.142 5.856   12.498  1.00 11.54 ?  86  HIS   A CG   1 
ATOM   1672 N ND1  . HIS   A 1 86  ? 31.234 6.685   12.631  1.00 12.76 ?  86  HIS   A ND1  1 
ATOM   1673 C CD2  . HIS   A 1 86  ? 30.320 5.173   11.345  1.00 11.52 ?  86  HIS   A CD2  1 
ATOM   1674 C CE1  . HIS   A 1 86  ? 32.021 6.532   11.582  1.00 12.54 ?  86  HIS   A CE1  1 
ATOM   1675 N NE2  . HIS   A 1 86  ? 31.493 5.617   10.790  1.00 11.85 ?  86  HIS   A NE2  1 
ATOM   1676 H H    . HIS   A 1 86  ? 30.560 3.211   14.056  1.00 12.63 ?  86  HIS   A H    1 
ATOM   1677 H HA   . HIS   A 1 86  ? 30.324 5.080   15.025  1.00 13.46 ?  86  HIS   A HA   1 
ATOM   1678 H HB2  . HIS   A 1 86  ? 28.276 5.450   13.131  1.00 13.60 ?  86  HIS   A HB2  1 
ATOM   1679 H HB3  . HIS   A 1 86  ? 28.972 6.628   13.942  1.00 13.60 ?  86  HIS   A HB3  1 
ATOM   1680 H HD2  . HIS   A 1 86  ? 29.755 4.522   10.996  1.00 13.83 ?  86  HIS   A HD2  1 
ATOM   1681 H HE1  . HIS   A 1 86  ? 32.812 6.997   11.419  1.00 15.06 ?  86  HIS   A HE1  1 
ATOM   1682 H HE2  . HIS   A 1 86  ? 31.824 5.350   10.041  1.00 14.22 ?  86  HIS   A HE2  1 
ATOM   1683 N N    . ASN   A 1 87  ? 27.490 5.470   15.875  1.00 12.71 ?  87  ASN   A N    1 
ATOM   1684 C CA   . ASN   A 1 87  ? 26.493 5.449   16.929  1.00 13.89 ?  87  ASN   A CA   1 
ATOM   1685 C C    . ASN   A 1 87  ? 25.372 4.453   16.667  1.00 14.86 ?  87  ASN   A C    1 
ATOM   1686 O O    . ASN   A 1 87  ? 24.425 4.397   17.457  1.00 17.53 ?  87  ASN   A O    1 
ATOM   1687 C CB   . ASN   A 1 87  ? 25.902 6.855   17.101  1.00 14.64 ?  87  ASN   A CB   1 
ATOM   1688 C CG   . ASN   A 1 87  ? 25.380 7.440   15.793  1.00 15.37 ?  87  ASN   A CG   1 
ATOM   1689 O OD1  . ASN   A 1 87  ? 25.999 7.311   14.740  1.00 16.32 ?  87  ASN   A OD1  1 
ATOM   1690 N ND2  . ASN   A 1 87  ? 24.239 8.101   15.865  1.00 16.51 ?  87  ASN   A ND2  1 
ATOM   1691 H H    . ASN   A 1 87  ? 27.351 6.090   15.305  1.00 15.27 ?  87  ASN   A H    1 
ATOM   1692 H HA   . ASN   A 1 87  ? 26.915 5.199   17.768  1.00 16.67 ?  87  ASN   A HA   1 
ATOM   1693 H HB2  . ASN   A 1 87  ? 25.160 6.808   17.735  1.00 17.58 ?  87  ASN   A HB2  1 
ATOM   1694 H HB3  . ASN   A 1 87  ? 26.588 7.443   17.449  1.00 17.58 ?  87  ASN   A HB3  1 
ATOM   1695 H HD21 . ASN   A 1 87  ? 23.904 8.453   15.159  1.00 19.82 ?  87  ASN   A HD21 1 
ATOM   1696 H HD22 . ASN   A 1 87  ? 23.830 8.182   16.622  1.00 19.82 ?  87  ASN   A HD22 1 
ATOM   1697 N N    . LEU   A 1 88  ? 25.458 3.660   15.602  1.00 14.12 ?  88  LEU   A N    1 
ATOM   1698 C CA   . LEU   A 1 88  ? 24.362 2.786   15.201  1.00 14.31 ?  88  LEU   A CA   1 
ATOM   1699 C C    . LEU   A 1 88  ? 24.586 1.314   15.523  1.00 13.90 ?  88  LEU   A C    1 
ATOM   1700 O O    . LEU   A 1 88  ? 23.611 0.581   15.715  1.00 15.36 ?  88  LEU   A O    1 
ATOM   1701 C CB   . LEU   A 1 88  ? 24.120 2.923   13.697  1.00 15.17 ?  88  LEU   A CB   1 
ATOM   1702 C CG   . LEU   A 1 88  ? 23.817 4.340   13.205  1.00 17.06 ?  88  LEU   A CG   1 
ATOM   1703 C CD1  . LEU   A 1 88  ? 23.616 4.353   11.701  1.00 17.45 ?  88  LEU   A CD1  1 
ATOM   1704 C CD2  . LEU   A 1 88  ? 22.595 4.913   13.912  1.00 18.84 ?  88  LEU   A CD2  1 
ATOM   1705 H H    . LEU   A 1 88  ? 26.150 3.614   15.094  1.00 16.95 ?  88  LEU   A H    1 
ATOM   1706 H HA   . LEU   A 1 88  ? 23.558 3.065   15.660  1.00 17.18 ?  88  LEU   A HA   1 
ATOM   1707 H HB2  . LEU   A 1 88  ? 24.908 2.618   13.224  1.00 18.22 ?  88  LEU   A HB2  1 
ATOM   1708 H HB3  . LEU   A 1 88  ? 23.361 2.370   13.456  1.00 18.22 ?  88  LEU   A HB3  1 
ATOM   1709 H HG   . LEU   A 1 88  ? 24.574 4.912   13.403  1.00 20.48 ?  88  LEU   A HG   1 
ATOM   1710 H HD11 . LEU   A 1 88  ? 23.461 5.267   11.407  1.00 20.95 ?  88  LEU   A HD11 1 
ATOM   1711 H HD12 . LEU   A 1 88  ? 24.410 4.000   11.269  1.00 20.95 ?  88  LEU   A HD12 1 
ATOM   1712 H HD13 . LEU   A 1 88  ? 22.847 3.803   11.479  1.00 20.95 ?  88  LEU   A HD13 1 
ATOM   1713 H HD21 . LEU   A 1 88  ? 22.345 5.746   13.483  1.00 22.62 ?  88  LEU   A HD21 1 
ATOM   1714 H HD22 . LEU   A 1 88  ? 21.869 4.276   13.849  1.00 22.62 ?  88  LEU   A HD22 1 
ATOM   1715 H HD23 . LEU   A 1 88  ? 22.819 5.073   14.842  1.00 22.62 ?  88  LEU   A HD23 1 
ATOM   1716 N N    . ALA   A 1 89  ? 25.840 0.873   15.574  1.00 12.42 ?  89  ALA   A N    1 
ATOM   1717 C CA   . ALA   A 1 89  ? 26.193 -0.538  15.659  1.00 12.33 ?  89  ALA   A CA   1 
ATOM   1718 C C    . ALA   A 1 89  ? 27.679 -0.597  15.970  1.00 12.73 ?  89  ALA   A C    1 
ATOM   1719 O O    . ALA   A 1 89  ? 28.383 0.407   15.859  1.00 13.68 ?  89  ALA   A O    1 
ATOM   1720 C CB   . ALA   A 1 89  ? 25.910 -1.247  14.334  1.00 12.40 ?  89  ALA   A CB   1 
ATOM   1721 H H    . ALA   A 1 89  ? 26.528 1.395   15.555  1.00 14.91 ?  89  ALA   A H    1 
ATOM   1722 H HA   . ALA   A 1 89  ? 25.695 -0.964  16.374  1.00 14.80 ?  89  ALA   A HA   1 
ATOM   1723 H HB1  . ALA   A 1 89  ? 26.175 -2.178  14.414  1.00 14.89 ?  89  ALA   A HB1  1 
ATOM   1724 H HB2  . ALA   A 1 89  ? 24.960 -1.191  14.141  1.00 14.89 ?  89  ALA   A HB2  1 
ATOM   1725 H HB3  . ALA   A 1 89  ? 26.418 -0.819  13.631  1.00 14.89 ?  89  ALA   A HB3  1 
ATOM   1726 N N    . LYS   A 1 90  ? 28.170 -1.779  16.341  1.00 13.51 ?  90  LYS   A N    1 
ATOM   1727 C CA   . LYS   A 1 90  ? 29.617 -1.919  16.482  1.00 14.10 ?  90  LYS   A CA   1 
ATOM   1728 C C    . LYS   A 1 90  ? 30.304 -1.719  15.135  1.00 12.94 ?  90  LYS   A C    1 
ATOM   1729 O O    . LYS   A 1 90  ? 31.239 -0.913  15.006  1.00 14.12 ?  90  LYS   A O    1 
ATOM   1730 C CB   . LYS   A 1 90  ? 29.966 -3.279  17.089  1.00 16.52 ?  90  LYS   A CB   1 
ATOM   1731 C CG   . LYS   A 1 90  ? 31.444 -3.422  17.422  1.00 20.41 ?  90  LYS   A CG   1 
ATOM   1732 C CD   . LYS   A 1 90  ? 31.700 -4.666  18.258  1.00 24.36 ?  90  LYS   A CD   1 
ATOM   1733 C CE   . LYS   A 1 90  ? 33.108 -4.681  18.834  1.00 27.28 ?  90  LYS   A CE   1 
ATOM   1734 N NZ   . LYS   A 1 90  ? 34.140 -5.035  17.822  1.00 29.17 ?  90  LYS   A NZ   1 
ATOM   1735 H H    . LYS   A 1 90  ? 27.707 -2.479  16.511  1.00 16.22 ?  90  LYS   A H    1 
ATOM   1736 H HA   . LYS   A 1 90  ? 29.942 -1.232  17.081  1.00 16.93 ?  90  LYS   A HA   1 
ATOM   1737 H HB2  . LYS   A 1 90  ? 29.461 -3.393  17.912  1.00 19.83 ?  90  LYS   A HB2  1 
ATOM   1738 H HB3  . LYS   A 1 90  ? 29.730 -3.977  16.460  1.00 19.83 ?  90  LYS   A HB3  1 
ATOM   1739 H HG2  . LYS   A 1 90  ? 31.952 -3.498  16.600  1.00 24.51 ?  90  LYS   A HG2  1 
ATOM   1740 H HG3  . LYS   A 1 90  ? 31.736 -2.649  17.930  1.00 24.51 ?  90  LYS   A HG3  1 
ATOM   1741 H HD2  . LYS   A 1 90  ? 31.070 -4.693  18.996  1.00 29.24 ?  90  LYS   A HD2  1 
ATOM   1742 H HD3  . LYS   A 1 90  ? 31.593 -5.454  17.700  1.00 29.24 ?  90  LYS   A HD3  1 
ATOM   1743 H HE2  . LYS   A 1 90  ? 33.317 -3.798  19.179  1.00 32.75 ?  90  LYS   A HE2  1 
ATOM   1744 H HE3  . LYS   A 1 90  ? 33.151 -5.334  19.549  1.00 32.75 ?  90  LYS   A HE3  1 
ATOM   1745 H HZ1  . LYS   A 1 90  ? 34.947 -5.034  18.199  1.00 35.01 ?  90  LYS   A HZ1  1 
ATOM   1746 H HZ2  . LYS   A 1 90  ? 33.976 -5.845  17.492  1.00 35.01 ?  90  LYS   A HZ2  1 
ATOM   1747 H HZ3  . LYS   A 1 90  ? 34.130 -4.443  17.158  1.00 35.01 ?  90  LYS   A HZ3  1 
ATOM   1748 N N    . HIS   A 1 91  ? 29.822 -2.425  14.112  1.00 11.33 ?  91  HIS   A N    1 
ATOM   1749 C CA   . HIS   A 1 91  ? 30.381 -2.400  12.774  1.00 10.88 ?  91  HIS   A CA   1 
ATOM   1750 C C    . HIS   A 1 91  ? 29.280 -2.121  11.766  1.00 9.94  ?  91  HIS   A C    1 
ATOM   1751 O O    . HIS   A 1 91  ? 28.118 -2.496  11.967  1.00 10.29 ?  91  HIS   A O    1 
ATOM   1752 C CB   . HIS   A 1 91  ? 30.974 -3.770  12.397  1.00 12.85 ?  91  HIS   A CB   1 
ATOM   1753 C CG   . HIS   A 1 91  ? 31.964 -4.302  13.385  1.00 17.39 ?  91  HIS   A CG   1 
ATOM   1754 N ND1  . HIS   A 1 91  ? 33.247 -3.812  13.490  1.00 19.61 ?  91  HIS   A ND1  1 
ATOM   1755 C CD2  . HIS   A 1 91  ? 31.864 -5.294  14.302  1.00 19.33 ?  91  HIS   A CD2  1 
ATOM   1756 C CE1  . HIS   A 1 91  ? 33.895 -4.476  14.432  1.00 20.52 ?  91  HIS   A CE1  1 
ATOM   1757 N NE2  . HIS   A 1 91  ? 33.077 -5.381  14.941  1.00 20.74 ?  91  HIS   A NE2  1 
ATOM   1758 H H    . HIS   A 1 91  ? 29.147 -2.963  14.182  1.00 13.61 ?  91  HIS   A H    1 
ATOM   1759 H HA   . HIS   A 1 91  ? 31.069 -1.726  12.702  1.00 13.07 ?  91  HIS   A HA   1 
ATOM   1760 H HB2  . HIS   A 1 91  ? 30.254 -4.419  12.329  1.00 15.42 ?  91  HIS   A HB2  1 
ATOM   1761 H HB3  . HIS   A 1 91  ? 31.425 -3.695  11.541  1.00 15.42 ?  91  HIS   A HB3  1 
ATOM   1762 H HD1  . HIS   A 1 91  ? 33.577 -3.176  13.013  1.00 23.55 ?  91  HIS   A HD1  1 
ATOM   1763 H HD2  . HIS   A 1 91  ? 31.117 -5.818  14.469  1.00 23.20 ?  91  HIS   A HD2  1 
ATOM   1764 H HE1  . HIS   A 1 91  ? 34.777 -4.325  14.692  1.00 24.63 ?  91  HIS   A HE1  1 
ATOM   1765 N N    . CYS   A 1 92  ? 29.674 -1.515  10.648  1.00 9.63  ?  92  CYS   A N    1 
ATOM   1766 C CA   . CYS   A 1 92  ? 28.828 -1.434  9.465   1.00 9.23  ?  92  CYS   A CA   1 
ATOM   1767 C C    . CYS   A 1 92  ? 29.469 -2.252  8.352   1.00 8.96  ?  92  CYS   A C    1 
ATOM   1768 O O    . CYS   A 1 92  ? 30.624 -2.000  7.975   1.00 9.61  ?  92  CYS   A O    1 
ATOM   1769 C CB   . CYS   A 1 92  ? 28.618 0.013   9.013   1.00 10.06 ?  92  CYS   A CB   1 
ATOM   1770 S SG   . CYS   A 1 92  ? 27.586 0.129   7.518   1.00 9.55  ?  92  CYS   A SG   1 
ATOM   1771 H H    . CYS   A 1 92  ? 30.439 -1.130  10.553  1.00 11.57 ?  92  CYS   A H    1 
ATOM   1772 H HA   . CYS   A 1 92  ? 27.962 -1.817  9.670   1.00 11.09 ?  92  CYS   A HA   1 
ATOM   1773 H HB2  . CYS   A 1 92  ? 28.173 0.506   9.722   1.00 12.08 ?  92  CYS   A HB2  1 
ATOM   1774 H HB3  . CYS   A 1 92  ? 29.475 0.413   8.814   1.00 12.08 ?  92  CYS   A HB3  1 
ATOM   1775 H HG   . CYS   A 1 92  ? 27.448 1.283   7.227   1.00 11.47 ?  92  CYS   A HG   1 
ATOM   1776 N N    . LEU   A 1 93  ? 28.727 -3.238  7.849   1.00 8.74  ?  93  LEU   A N    1 
ATOM   1777 C CA   . LEU   A 1 93  ? 29.112 -3.994  6.664   1.00 8.46  ?  93  LEU   A CA   1 
ATOM   1778 C C    . LEU   A 1 93  ? 28.509 -3.287  5.455   1.00 7.94  ?  93  LEU   A C    1 
ATOM   1779 O O    . LEU   A 1 93  ? 27.293 -3.346  5.229   1.00 8.23  ?  93  LEU   A O    1 
ATOM   1780 C CB   . LEU   A 1 93  ? 28.621 -5.436  6.773   1.00 8.86  ?  93  LEU   A CB   1 
ATOM   1781 C CG   . LEU   A 1 93  ? 29.005 -6.332  5.595   1.00 9.16  ?  93  LEU   A CG   1 
ATOM   1782 C CD1  . LEU   A 1 93  ? 30.513 -6.580  5.589   1.00 10.34 ?  93  LEU   A CD1  1 
ATOM   1783 C CD2  . LEU   A 1 93  ? 28.231 -7.653  5.619   1.00 10.00 ?  93  LEU   A CD2  1 
ATOM   1784 H H    . LEU   A 1 93  ? 27.975 -3.490  8.190   1.00 10.50 ?  93  LEU   A H    1 
ATOM   1785 H HA   . LEU   A 1 93  ? 30.076 -3.995  6.583   1.00 10.16 ?  93  LEU   A HA   1 
ATOM   1786 H HB2  . LEU   A 1 93  ? 28.994 -5.830  7.580   1.00 10.64 ?  93  LEU   A HB2  1 
ATOM   1787 H HB3  . LEU   A 1 93  ? 27.653 -5.432  6.835   1.00 10.64 ?  93  LEU   A HB3  1 
ATOM   1788 H HG   . LEU   A 1 93  ? 28.786 -5.879  4.774   1.00 11.00 ?  93  LEU   A HG   1 
ATOM   1789 H HD11 . LEU   A 1 93  ? 30.735 -7.212  4.891   1.00 12.41 ?  93  LEU   A HD11 1 
ATOM   1790 H HD12 . LEU   A 1 93  ? 30.978 -5.741  5.437   1.00 12.41 ?  93  LEU   A HD12 1 
ATOM   1791 H HD13 . LEU   A 1 93  ? 30.783 -6.944  6.456   1.00 12.41 ?  93  LEU   A HD13 1 
ATOM   1792 H HD21 . LEU   A 1 93  ? 28.511 -8.192  4.858   1.00 12.01 ?  93  LEU   A HD21 1 
ATOM   1793 H HD22 . LEU   A 1 93  ? 28.430 -8.124  6.443   1.00 12.01 ?  93  LEU   A HD22 1 
ATOM   1794 H HD23 . LEU   A 1 93  ? 27.285 -7.465  5.561   1.00 12.01 ?  93  LEU   A HD23 1 
ATOM   1795 N N    . HIS   A 1 94  ? 29.354 -2.591  4.697   1.00 8.03  ?  94  HIS   A N    1 
ATOM   1796 C CA   . HIS   A 1 94  ? 28.929 -1.915  3.475   1.00 8.19  ?  94  HIS   A CA   1 
ATOM   1797 C C    . HIS   A 1 94  ? 28.926 -2.946  2.359   1.00 7.94  ?  94  HIS   A C    1 
ATOM   1798 O O    . HIS   A 1 94  ? 29.990 -3.455  1.998   1.00 9.46  ?  94  HIS   A O    1 
ATOM   1799 C CB   . HIS   A 1 94  ? 29.889 -0.777  3.142   1.00 8.32  ?  94  HIS   A CB   1 
ATOM   1800 C CG   . HIS   A 1 94  ? 29.883 0.320   4.155   1.00 8.36  ?  94  HIS   A CG   1 
ATOM   1801 N ND1  . HIS   A 1 94  ? 29.004 1.382   4.101   1.00 8.55  ?  94  HIS   A ND1  1 
ATOM   1802 C CD2  . HIS   A 1 94  ? 30.626 0.487   5.273   1.00 8.89  ?  94  HIS   A CD2  1 
ATOM   1803 C CE1  . HIS   A 1 94  ? 29.227 2.163   5.144   1.00 8.77  ?  94  HIS   A CE1  1 
ATOM   1804 N NE2  . HIS   A 1 94  ? 30.204 1.644   5.869   1.00 9.29  ?  94  HIS   A NE2  1 
ATOM   1805 H H    . HIS   A 1 94  ? 30.195 -2.490  4.873   1.00 9.65  ?  94  HIS   A H    1 
ATOM   1806 H HA   . HIS   A 1 94  ? 28.031 -1.570  3.585   1.00 9.83  ?  94  HIS   A HA   1 
ATOM   1807 H HB2  . HIS   A 1 94  ? 30.782 -1.130  3.084   1.00 9.99  ?  94  HIS   A HB2  1 
ATOM   1808 H HB3  . HIS   A 1 94  ? 29.621 -0.396  2.288   1.00 9.99  ?  94  HIS   A HB3  1 
ATOM   1809 H HD2  . HIS   A 1 94  ? 31.299 -0.073  5.575   1.00 10.67 ?  94  HIS   A HD2  1 
ATOM   1810 H HE1  . HIS   A 1 94  ? 28.763 2.948   5.336   1.00 10.53 ?  94  HIS   A HE1  1 
ATOM   1811 H HE2  . HIS   A 1 94  ? 30.519 1.985   6.591   1.00 11.16 ?  94  HIS   A HE2  1 
ATOM   1812 N N    . VAL   A 1 95  ? 27.748 -3.272  1.818   1.00 7.59  ?  95  VAL   A N    1 
ATOM   1813 C CA   . VAL   A 1 95  ? 27.605 -4.300  0.790   1.00 8.03  ?  95  VAL   A CA   1 
ATOM   1814 C C    . VAL   A 1 95  ? 27.057 -3.655  -0.469  1.00 7.70  ?  95  VAL   A C    1 
ATOM   1815 O O    . VAL   A 1 95  ? 26.052 -2.936  -0.410  1.00 8.49  ?  95  VAL   A O    1 
ATOM   1816 C CB   . VAL   A 1 95  ? 26.678 -5.443  1.245   1.00 8.61  ?  95  VAL   A CB   1 
ATOM   1817 C CG1  . VAL   A 1 95  ? 26.565 -6.486  0.144   1.00 9.54  ?  95  VAL   A CG1  1 
ATOM   1818 C CG2  . VAL   A 1 95  ? 27.187 -6.059  2.532   1.00 9.10  ?  95  VAL   A CG2  1 
ATOM   1819 H H    . VAL   A 1 95  ? 27.001 -2.898  2.034   1.00 9.12  ?  95  VAL   A H    1 
ATOM   1820 H HA   . VAL   A 1 95  ? 28.471 -4.677  0.586   1.00 9.65  ?  95  VAL   A HA   1 
ATOM   1821 H HB   . VAL   A 1 95  ? 25.791 -5.092  1.413   1.00 10.34 ?  95  VAL   A HB   1 
ATOM   1822 H HG11 . VAL   A 1 95  ? 26.163 -7.296  0.510   1.00 11.46 ?  95  VAL   A HG11 1 
ATOM   1823 H HG12 . VAL   A 1 95  ? 26.010 -6.145  -0.573  1.00 11.46 ?  95  VAL   A HG12 1 
ATOM   1824 H HG13 . VAL   A 1 95  ? 27.452 -6.695  -0.194  1.00 11.46 ?  95  VAL   A HG13 1 
ATOM   1825 H HG21 . VAL   A 1 95  ? 26.637 -6.826  2.759   1.00 10.93 ?  95  VAL   A HG21 1 
ATOM   1826 H HG22 . VAL   A 1 95  ? 28.109 -6.342  2.405   1.00 10.93 ?  95  VAL   A HG22 1 
ATOM   1827 H HG23 . VAL   A 1 95  ? 27.140 -5.398  3.239   1.00 10.93 ?  95  VAL   A HG23 1 
ATOM   1828 N N    A VAL   A 1 96  ? 27.673 -3.948  -1.614  0.86 8.03  ?  96  VAL   A N    1 
ATOM   1829 N N    B VAL   A 1 96  ? 27.726 -3.895  -1.593  0.14 8.34  ?  96  VAL   A N    1 
ATOM   1830 C CA   A VAL   A 1 96  ? 27.250 -3.385  -2.893  0.86 8.33  ?  96  VAL   A CA   1 
ATOM   1831 C CA   B VAL   A 1 96  ? 27.389 -3.277  -2.869  0.14 9.10  ?  96  VAL   A CA   1 
ATOM   1832 C C    A VAL   A 1 96  ? 26.428 -4.429  -3.643  0.86 8.30  ?  96  VAL   A C    1 
ATOM   1833 C C    B VAL   A 1 96  ? 26.592 -4.295  -3.675  0.14 9.40  ?  96  VAL   A C    1 
ATOM   1834 O O    A VAL   A 1 96  ? 26.975 -5.365  -4.236  0.86 9.37  ?  96  VAL   A O    1 
ATOM   1835 O O    B VAL   A 1 96  ? 27.151 -5.246  -4.228  0.14 9.74  ?  96  VAL   A O    1 
ATOM   1836 C CB   A VAL   A 1 96  ? 28.432 -2.910  -3.737  0.86 8.68  ?  96  VAL   A CB   1 
ATOM   1837 C CB   B VAL   A 1 96  ? 28.640 -2.818  -3.620  0.14 9.77  ?  96  VAL   A CB   1 
ATOM   1838 C CG1  A VAL   A 1 96  ? 27.915 -2.265  -5.007  0.86 8.83  ?  96  VAL   A CG1  1 
ATOM   1839 C CG1  B VAL   A 1 96  ? 28.256 -2.175  -4.944  0.14 10.27 ?  96  VAL   A CG1  1 
ATOM   1840 C CG2  A VAL   A 1 96  ? 29.308 -1.950  -2.948  0.86 9.35  ?  96  VAL   A CG2  1 
ATOM   1841 C CG2  B VAL   A 1 96  ? 29.444 -1.853  -2.767  0.14 9.94  ?  96  VAL   A CG2  1 
ATOM   1842 H H    A VAL   A 1 96  ? 28.354 -4.473  -1.677  0.86 9.65  ?  96  VAL   A H    1 
ATOM   1843 H H    B VAL   A 1 96  ? 28.404 -4.424  -1.639  0.14 10.02 ?  96  VAL   A H    1 
ATOM   1844 H HA   A VAL   A 1 96  ? 26.680 -2.620  -2.729  0.86 10.01 ?  96  VAL   A HA   1 
ATOM   1845 H HA   B VAL   A 1 96  ? 26.827 -2.504  -2.714  0.14 10.93 ?  96  VAL   A HA   1 
ATOM   1846 H HB   A VAL   A 1 96  ? 28.974 -3.674  -3.986  0.86 10.43 ?  96  VAL   A HB   1 
ATOM   1847 H HB   B VAL   A 1 96  ? 29.199 -3.588  -3.811  0.14 11.74 ?  96  VAL   A HB   1 
ATOM   1848 H HG11 A VAL   A 1 96  ? 28.655 -1.797  -5.434  0.86 10.61 ?  96  VAL   A HG11 1 
ATOM   1849 H HG11 B VAL   A 1 96  ? 29.049 -1.787  -5.346  0.14 12.33 ?  96  VAL   A HG11 1 
ATOM   1850 H HG12 A VAL   A 1 96  ? 27.576 -2.951  -5.594  0.86 10.61 ?  96  VAL   A HG12 1 
ATOM   1851 H HG12 B VAL   A 1 96  ? 27.886 -2.851  -5.532  0.14 12.33 ?  96  VAL   A HG12 1 
ATOM   1852 H HG13 A VAL   A 1 96  ? 27.219 -1.635  -4.776  0.86 10.61 ?  96  VAL   A HG13 1 
ATOM   1853 H HG13 B VAL   A 1 96  ? 27.597 -1.483  -4.778  0.14 12.33 ?  96  VAL   A HG13 1 
ATOM   1854 H HG21 A VAL   A 1 96  ? 30.001 -1.604  -3.526  0.86 11.23 ?  96  VAL   A HG21 1 
ATOM   1855 H HG21 B VAL   A 1 96  ? 30.189 -1.518  -3.288  0.14 11.94 ?  96  VAL   A HG21 1 
ATOM   1856 H HG22 A VAL   A 1 96  ? 28.755 -1.220  -2.618  0.86 11.23 ?  96  VAL   A HG22 1 
ATOM   1857 H HG22 B VAL   A 1 96  ? 28.868 -1.119  -2.500  0.14 11.94 ?  96  VAL   A HG22 1 
ATOM   1858 H HG23 A VAL   A 1 96  ? 29.703 -2.424  -2.199  0.86 11.23 ?  96  VAL   A HG23 1 
ATOM   1859 H HG23 B VAL   A 1 96  ? 29.769 -2.322  -1.984  0.14 11.94 ?  96  VAL   A HG23 1 
ATOM   1860 N N    A GLY   A 1 97  ? 25.108 -4.273  -3.647  0.86 8.68  ?  97  GLY   A N    1 
ATOM   1861 N N    B GLY   A 1 97  ? 25.280 -4.094  -3.748  0.14 9.83  ?  97  GLY   A N    1 
ATOM   1862 C CA   A GLY   A 1 97  ? 24.281 -5.023  -4.560  0.86 9.17  ?  97  GLY   A CA   1 
ATOM   1863 C CA   B GLY   A 1 97  ? 24.443 -4.882  -4.617  0.14 10.17 ?  97  GLY   A CA   1 
ATOM   1864 C C    A GLY   A 1 97  ? 24.292 -4.371  -5.930  0.86 9.14  ?  97  GLY   A C    1 
ATOM   1865 C C    B GLY   A 1 97  ? 24.320 -4.231  -5.979  0.14 10.48 ?  97  GLY   A C    1 
ATOM   1866 O O    A GLY   A 1 97  ? 24.603 -3.182  -6.068  0.86 10.17 ?  97  GLY   A O    1 
ATOM   1867 O O    B GLY   A 1 97  ? 24.499 -3.017  -6.128  0.14 10.45 ?  97  GLY   A O    1 
ATOM   1868 H H    A GLY   A 1 97  ? 24.671 -3.737  -3.128  0.86 10.43 ?  97  GLY   A H    1 
ATOM   1869 H H    B GLY   A 1 97  ? 24.854 -3.500  -3.294  0.14 11.80 ?  97  GLY   A H    1 
ATOM   1870 H HA2  A GLY   A 1 97  ? 24.621 -5.930  -4.634  0.86 11.01 ?  97  GLY   A HA2  1 
ATOM   1871 H HA2  B GLY   A 1 97  ? 24.824 -5.771  -4.712  0.14 12.22 ?  97  GLY   A HA2  1 
ATOM   1872 H HA3  A GLY   A 1 97  ? 23.367 -5.061  -4.228  0.86 11.01 ?  97  GLY   A HA3  1 
ATOM   1873 H HA3  B GLY   A 1 97  ? 23.556 -4.963  -4.237  0.14 12.22 ?  97  GLY   A HA3  1 
ATOM   1874 N N    A PRO   A 1 98  ? 23.946 -5.123  -6.972  0.86 9.52  ?  98  PRO   A N    1 
ATOM   1875 N N    B PRO   A 1 98  ? 24.010 -5.022  -7.003  0.14 10.89 ?  98  PRO   A N    1 
ATOM   1876 C CA   A PRO   A 1 98  ? 23.833 -4.512  -8.302  0.86 10.62 ?  98  PRO   A CA   1 
ATOM   1877 C CA   B PRO   A 1 98  ? 23.871 -4.452  -8.347  0.14 11.42 ?  98  PRO   A CA   1 
ATOM   1878 C C    A PRO   A 1 98  ? 22.722 -3.468  -8.341  0.86 10.39 ?  98  PRO   A C    1 
ATOM   1879 C C    B PRO   A 1 98  ? 22.742 -3.437  -8.412  0.14 11.88 ?  98  PRO   A C    1 
ATOM   1880 O O    A PRO   A 1 98  ? 21.642 -3.654  -7.773  0.86 10.69 ?  98  PRO   A O    1 
ATOM   1881 O O    B PRO   A 1 98  ? 21.729 -3.548  -7.717  0.14 11.80 ?  98  PRO   A O    1 
ATOM   1882 C CB   A PRO   A 1 98  ? 23.518 -5.707  -9.213  0.86 11.06 ?  98  PRO   A CB   1 
ATOM   1883 C CB   B PRO   A 1 98  ? 23.571 -5.674  -9.223  0.14 11.46 ?  98  PRO   A CB   1 
ATOM   1884 C CG   A PRO   A 1 98  ? 22.879 -6.716  -8.307  0.86 11.11 ?  98  PRO   A CG   1 
ATOM   1885 C CG   B PRO   A 1 98  ? 23.025 -6.694  -8.278  0.14 11.39 ?  98  PRO   A CG   1 
ATOM   1886 C CD   A PRO   A 1 98  ? 23.603 -6.557  -6.990  0.86 9.94  ?  98  PRO   A CD   1 
ATOM   1887 C CD   B PRO   A 1 98  ? 23.771 -6.474  -6.997  0.14 11.06 ?  98  PRO   A CD   1 
ATOM   1888 H HA   A PRO   A 1 98  ? 24.677 -4.112  -8.563  0.86 12.75 ?  98  PRO   A HA   1 
ATOM   1889 H HA   B PRO   A 1 98  ? 24.698 -4.035  -8.630  0.14 13.71 ?  98  PRO   A HA   1 
ATOM   1890 H HB2  A PRO   A 1 98  ? 22.900 -5.430  -9.910  0.86 13.28 ?  98  PRO   A HB2  1 
ATOM   1891 H HB2  B PRO   A 1 98  ? 22.914 -5.439  -9.897  0.14 13.76 ?  98  PRO   A HB2  1 
ATOM   1892 H HB3  A PRO   A 1 98  ? 24.337 -6.054  -9.596  0.86 13.28 ?  98  PRO   A HB3  1 
ATOM   1893 H HB3  B PRO   A 1 98  ? 24.391 -5.987  -9.633  0.14 13.76 ?  98  PRO   A HB3  1 
ATOM   1894 H HG2  A PRO   A 1 98  ? 21.937 -6.516  -8.208  0.86 13.34 ?  98  PRO   A HG2  1 
ATOM   1895 H HG2  B PRO   A 1 98  ? 22.074 -6.544  -8.151  0.14 13.68 ?  98  PRO   A HG2  1 
ATOM   1896 H HG3  A PRO   A 1 98  ? 23.010 -7.605  -8.667  0.86 13.34 ?  98  PRO   A HG3  1 
ATOM   1897 H HG3  B PRO   A 1 98  ? 23.191 -7.582  -8.625  0.14 13.68 ?  98  PRO   A HG3  1 
ATOM   1898 H HD2  A PRO   A 1 98  ? 23.010 -6.780  -6.252  0.86 11.93 ?  98  PRO   A HD2  1 
ATOM   1899 H HD2  B PRO   A 1 98  ? 23.226 -6.729  -6.237  0.14 13.28 ?  98  PRO   A HD2  1 
ATOM   1900 H HD3  A PRO   A 1 98  ? 24.407 -7.099  -6.976  0.86 11.93 ?  98  PRO   A HD3  1 
ATOM   1901 H HD3  B PRO   A 1 98  ? 24.616 -6.950  -7.008  0.14 13.28 ?  98  PRO   A HD3  1 
ATOM   1902 N N    A ASN   A 1 99  ? 22.998 -2.358  -9.029  0.86 11.46 ?  99  ASN   A N    1 
ATOM   1903 N N    B ASN   A 1 99  ? 22.932 -2.438  -9.266  0.14 12.56 ?  99  ASN   A N    1 
ATOM   1904 C CA   A ASN   A 1 99  ? 22.024 -1.290  -9.241  0.86 12.77 ?  99  ASN   A CA   1 
ATOM   1905 C CA   B ASN   A 1 99  ? 21.952 -1.385  -9.485  0.14 13.50 ?  99  ASN   A CA   1 
ATOM   1906 C C    A ASN   A 1 99  ? 21.468 -1.446  -10.654 0.86 13.71 ?  99  ASN   A C    1 
ATOM   1907 C C    B ASN   A 1 99  ? 21.248 -1.654  -10.809 0.14 14.20 ?  99  ASN   A C    1 
ATOM   1908 O O    A ASN   A 1 99  ? 22.160 -1.172  -11.641 0.86 15.02 ?  99  ASN   A O    1 
ATOM   1909 O O    B ASN   A 1 99  ? 21.893 -1.696  -11.863 0.14 13.81 ?  99  ASN   A O    1 
ATOM   1910 C CB   A ASN   A 1 99  ? 22.669 0.082   -9.034  0.86 13.04 ?  99  ASN   A CB   1 
ATOM   1911 C CB   B ASN   A 1 99  ? 22.644 -0.022  -9.505  0.14 14.14 ?  99  ASN   A CB   1 
ATOM   1912 C CG   A ASN   A 1 99  ? 21.651 1.230   -9.033  0.86 13.55 ?  99  ASN   A CG   1 
ATOM   1913 C CG   B ASN   A 1 99  ? 21.667 1.137   -9.423  0.14 14.70 ?  99  ASN   A CG   1 
ATOM   1914 O OD1  A ASN   A 1 99  ? 20.649 1.188   -9.747  0.86 14.61 ?  99  ASN   A OD1  1 
ATOM   1915 O OD1  B ASN   A 1 99  ? 20.524 1.039   -9.872  0.14 14.90 ?  99  ASN   A OD1  1 
ATOM   1916 N ND2  A ASN   A 1 99  ? 21.921 2.263   -8.237  0.86 14.01 ?  99  ASN   A ND2  1 
ATOM   1917 N ND2  B ASN   A 1 99  ? 22.118 2.249   -8.844  0.14 14.90 ?  99  ASN   A ND2  1 
ATOM   1918 H H    A ASN   A 1 99  ? 23.765 -2.195  -9.378  0.86 13.77 ?  99  ASN   A H    1 
ATOM   1919 H H    B ASN   A 1 99  ? 23.644 -2.344  -9.740  0.14 15.08 ?  99  ASN   A H    1 
ATOM   1920 H HA   A ASN   A 1 99  ? 21.297 -1.385  -8.595  0.86 15.33 ?  99  ASN   A HA   1 
ATOM   1921 H HA   B ASN   A 1 99  ? 21.295 -1.387  -8.773  0.14 16.21 ?  99  ASN   A HA   1 
ATOM   1922 H HB2  A ASN   A 1 99  ? 23.135 0.093   -8.182  0.86 15.66 ?  99  ASN   A HB2  1 
ATOM   1923 H HB2  B ASN   A 1 99  ? 23.239 0.041   -8.745  0.14 16.98 ?  99  ASN   A HB2  1 
ATOM   1924 H HB3  A ASN   A 1 99  ? 23.300 0.239   -9.755  0.86 15.66 ?  99  ASN   A HB3  1 
ATOM   1925 H HB3  B ASN   A 1 99  ? 23.153 0.064   -10.321 0.14 16.98 ?  99  ASN   A HB3  1 
ATOM   1926 H HD21 A ASN   A 1 99  ? 21.381 2.930   -8.207  0.86 16.82 ?  99  ASN   A HD21 1 
ATOM   1927 H HD21 B ASN   A 1 99  ? 21.608 2.938   -8.769  0.14 17.89 ?  99  ASN   A HD21 1 
ATOM   1928 H HD22 A ASN   A 1 99  ? 22.632 2.259   -7.757  0.86 16.82 ?  99  ASN   A HD22 1 
ATOM   1929 H HD22 B ASN   A 1 99  ? 22.925 2.279   -8.540  0.14 17.89 ?  99  ASN   A HD22 1 
ATOM   1930 N N    A VAL   A 1 100 ? 20.218 -1.906  -10.738 0.86 14.11 ?  100 VAL   A N    1 
ATOM   1931 N N    B VAL   A 1 100 ? 19.931 -1.863  -10.748 0.14 15.50 ?  100 VAL   A N    1 
ATOM   1932 C CA   A VAL   A 1 100 ? 19.575 -2.120  -12.028 0.86 16.23 ?  100 VAL   A CA   1 
ATOM   1933 C CA   B VAL   A 1 100 ? 19.155 -2.074  -11.966 0.14 16.89 ?  100 VAL   A CA   1 
ATOM   1934 C C    A VAL   A 1 100 ? 19.469 -0.815  -12.805 0.86 16.44 ?  100 VAL   A C    1 
ATOM   1935 C C    B VAL   A 1 100 ? 19.076 -0.793  -12.785 0.14 18.15 ?  100 VAL   A C    1 
ATOM   1936 O O    A VAL   A 1 100 ? 19.521 -0.814  -14.041 0.86 17.84 ?  100 VAL   A O    1 
ATOM   1937 O O    B VAL   A 1 100 ? 19.049 -0.838  -14.021 0.14 18.38 ?  100 VAL   A O    1 
ATOM   1938 C CB   A VAL   A 1 100 ? 18.205 -2.798  -11.819 0.86 18.11 ?  100 VAL   A CB   1 
ATOM   1939 C CB   B VAL   A 1 100 ? 17.762 -2.632  -11.618 0.14 16.88 ?  100 VAL   A CB   1 
ATOM   1940 C CG1  A VAL   A 1 100 ? 17.499 -3.015  -13.149 0.86 18.99 ?  100 VAL   A CG1  1 
ATOM   1941 C CG1  B VAL   A 1 100 ? 16.875 -2.693  -12.853 0.14 16.92 ?  100 VAL   A CG1  1 
ATOM   1942 C CG2  A VAL   A 1 100 ? 18.382 -4.118  -11.085 0.86 19.02 ?  100 VAL   A CG2  1 
ATOM   1943 C CG2  B VAL   A 1 100 ? 17.888 -4.002  -10.977 0.14 16.89 ?  100 VAL   A CG2  1 
ATOM   1944 H H    A VAL   A 1 100 ? 19.720 -2.108  -10.053 0.86 16.94 ?  100 VAL   A H    1 
ATOM   1945 H H    B VAL   A 1 100 ? 19.474 -1.895  -10.021 0.14 18.60 ?  100 VAL   A H    1 
ATOM   1946 H HA   A VAL   A 1 100 ? 20.123 -2.724  -12.544 0.86 19.49 ?  100 VAL   A HA   1 
ATOM   1947 H HA   B VAL   A 1 100 ? 19.604 -2.738  -12.505 0.14 20.28 ?  100 VAL   A HA   1 
ATOM   1948 H HB   A VAL   A 1 100 ? 17.645 -2.224  -11.275 0.86 21.74 ?  100 VAL   A HB   1 
ATOM   1949 H HB   B VAL   A 1 100 ? 17.342 -2.044  -10.982 0.14 20.27 ?  100 VAL   A HB   1 
ATOM   1950 H HG11 A VAL   A 1 100 ? 16.723 -3.580  -13.004 0.86 22.79 ?  100 VAL   A HG11 1 
ATOM   1951 H HG11 B VAL   A 1 100 ? 16.101 -3.244  -12.654 0.14 20.32 ?  100 VAL   A HG11 1 
ATOM   1952 H HG12 A VAL   A 1 100 ? 17.221 -2.158  -13.506 0.86 22.79 ?  100 VAL   A HG12 1 
ATOM   1953 H HG12 B VAL   A 1 100 ? 16.588 -1.796  -13.085 0.14 20.32 ?  100 VAL   A HG12 1 
ATOM   1954 H HG13 A VAL   A 1 100 ? 18.111 -3.449  -13.764 0.86 22.79 ?  100 VAL   A HG13 1 
ATOM   1955 H HG13 B VAL   A 1 100 ? 17.380 -3.083  -13.581 0.14 20.32 ?  100 VAL   A HG13 1 
ATOM   1956 H HG21 A VAL   A 1 100 ? 17.535 -4.588  -11.072 0.86 22.83 ?  100 VAL   A HG21 1 
ATOM   1957 H HG21 B VAL   A 1 100 ? 17.001 -4.345  -10.786 0.14 20.27 ?  100 VAL   A HG21 1 
ATOM   1958 H HG22 A VAL   A 1 100 ? 19.049 -4.649  -11.548 0.86 22.83 ?  100 VAL   A HG22 1 
ATOM   1959 H HG22 B VAL   A 1 100 ? 18.347 -4.593  -11.593 0.14 20.27 ?  100 VAL   A HG22 1 
ATOM   1960 H HG23 A VAL   A 1 100 ? 18.675 -3.938  -10.178 0.86 22.83 ?  100 VAL   A HG23 1 
ATOM   1961 H HG23 B VAL   A 1 100 ? 18.395 -3.920  -10.154 0.14 20.27 ?  100 VAL   A HG23 1 
ATOM   1962 N N    A ASN   A 1 101 ? 19.339 0.313   -12.111 0.86 18.13 ?  101 ASN   A N    1 
ATOM   1963 N N    B ASN   A 1 101 ? 19.036 0.365   -12.123 0.14 19.32 ?  101 ASN   A N    1 
ATOM   1964 C CA   A ASN   A 1 101 ? 19.298 1.592   -12.811 0.86 20.19 ?  101 ASN   A CA   1 
ATOM   1965 C CA   B ASN   A 1 101 ? 19.010 1.633   -12.841 0.14 20.51 ?  101 ASN   A CA   1 
ATOM   1966 C C    A ASN   A 1 101 ? 20.661 2.009   -13.369 0.86 21.98 ?  101 ASN   A C    1 
ATOM   1967 C C    B ASN   A 1 101 ? 20.359 1.968   -13.461 0.14 21.55 ?  101 ASN   A C    1 
ATOM   1968 O O    A ASN   A 1 101 ? 20.747 3.051   -14.034 0.86 23.88 ?  101 ASN   A O    1 
ATOM   1969 O O    B ASN   A 1 101 ? 20.426 2.831   -14.343 0.14 21.69 ?  101 ASN   A O    1 
ATOM   1970 C CB   A ASN   A 1 101 ? 18.675 2.649   -11.897 0.86 20.16 ?  101 ASN   A CB   1 
ATOM   1971 C CB   B ASN   A 1 101 ? 18.530 2.738   -11.903 0.14 20.72 ?  101 ASN   A CB   1 
ATOM   1972 C CG   A ASN   A 1 101 ? 17.305 2.222   -11.382 0.86 19.81 ?  101 ASN   A CG   1 
ATOM   1973 C CG   B ASN   A 1 101 ? 17.228 2.378   -11.220 0.14 20.82 ?  101 ASN   A CG   1 
ATOM   1974 O OD1  A ASN   A 1 101 ? 16.474 1.714   -12.141 0.86 20.45 ?  101 ASN   A OD1  1 
ATOM   1975 O OD1  B ASN   A 1 101 ? 16.288 1.916   -11.866 0.14 20.94 ?  101 ASN   A OD1  1 
ATOM   1976 N ND2  A ASN   A 1 101 ? 17.072 2.404   -10.089 0.86 19.42 ?  101 ASN   A ND2  1 
ATOM   1977 N ND2  B ASN   A 1 101 ? 17.175 2.557   -9.905  0.14 20.84 ?  101 ASN   A ND2  1 
ATOM   1978 H H    A ASN   A 1 101 ? 19.274 0.365   -11.252 0.86 21.76 ?  101 ASN   A H    1 
ATOM   1979 H H    B ASN   A 1 101 ? 19.016 0.440   -11.267 0.14 23.19 ?  101 ASN   A H    1 
ATOM   1980 H HA   A ASN   A 1 101 ? 18.711 1.493   -13.570 0.86 24.23 ?  101 ASN   A HA   1 
ATOM   1981 H HA   B ASN   A 1 101 ? 18.369 1.566   -13.564 0.14 24.62 ?  101 ASN   A HA   1 
ATOM   1982 H HB2  A ASN   A 1 101 ? 19.252 2.799   -11.136 0.86 24.20 ?  101 ASN   A HB2  1 
ATOM   1983 H HB2  B ASN   A 1 101 ? 19.197 2.892   -11.218 0.14 24.87 ?  101 ASN   A HB2  1 
ATOM   1984 H HB3  A ASN   A 1 101 ? 18.564 3.474   -12.401 0.86 24.20 ?  101 ASN   A HB3  1 
ATOM   1985 H HB3  B ASN   A 1 101 ? 18.387 3.552   -12.417 0.14 24.87 ?  101 ASN   A HB3  1 
ATOM   1986 H HD21 A ASN   A 1 101 ? 16.314 2.177   -9.755  0.86 23.31 ?  101 ASN   A HD21 1 
ATOM   1987 H HD21 B ASN   A 1 101 ? 16.456 2.364   -9.474  0.14 25.01 ?  101 ASN   A HD21 1 
ATOM   1988 H HD22 A ASN   A 1 101 ? 17.674 2.763   -9.591  0.86 23.31 ?  101 ASN   A HD22 1 
ATOM   1989 H HD22 B ASN   A 1 101 ? 17.856 2.870   -9.487  0.14 25.01 ?  101 ASN   A HD22 1 
ATOM   1990 N N    A LYS   A 1 102 ? 21.708 1.209   -13.136 0.86 23.54 ?  102 LYS   A N    1 
ATOM   1991 N N    B LYS   A 1 102 ? 21.429 1.306   -13.022 0.14 22.43 ?  102 LYS   A N    1 
ATOM   1992 C CA   A LYS   A 1 102 ? 22.997 1.356   -13.802 0.86 25.01 ?  102 LYS   A CA   1 
ATOM   1993 C CA   B LYS   A 1 102 ? 22.708 1.342   -13.715 0.14 23.12 ?  102 LYS   A CA   1 
ATOM   1994 C C    A LYS   A 1 102 ? 23.281 0.226   -14.784 0.86 24.97 ?  102 LYS   A C    1 
ATOM   1995 C C    B LYS   A 1 102 ? 22.848 0.228   -14.742 0.14 23.16 ?  102 LYS   A C    1 
ATOM   1996 O O    A LYS   A 1 102 ? 24.378 0.177   -15.348 0.86 25.59 ?  102 LYS   A O    1 
ATOM   1997 O O    B LYS   A 1 102 ? 23.845 0.200   -15.471 0.14 23.32 ?  102 LYS   A O    1 
ATOM   1998 C CB   A LYS   A 1 102 ? 24.132 1.412   -12.769 0.86 26.57 ?  102 LYS   A CB   1 
ATOM   1999 C CB   B LYS   A 1 102 ? 23.866 1.239   -12.715 0.14 23.64 ?  102 LYS   A CB   1 
ATOM   2000 C CG   A LYS   A 1 102 ? 24.036 2.555   -11.773 0.86 27.86 ?  102 LYS   A CG   1 
ATOM   2001 C CG   B LYS   A 1 102 ? 24.057 2.458   -11.824 0.14 24.05 ?  102 LYS   A CG   1 
ATOM   2002 C CD   A LYS   A 1 102 ? 25.181 2.505   -10.766 0.86 29.09 ?  102 LYS   A CD   1 
ATOM   2003 C CD   B LYS   A 1 102 ? 25.221 2.245   -10.863 0.14 24.41 ?  102 LYS   A CD   1 
ATOM   2004 C CE   A LYS   A 1 102 ? 25.107 3.662   -9.778  0.86 30.15 ?  102 LYS   A CE   1 
ATOM   2005 C CE   B LYS   A 1 102 ? 25.446 3.452   -9.967  0.14 24.70 ?  102 LYS   A CE   1 
ATOM   2006 N NZ   A LYS   A 1 102 ? 26.177 3.583   -8.739  0.86 30.75 ?  102 LYS   A NZ   1 
ATOM   2007 N NZ   B LYS   A 1 102 ? 26.532 3.209   -8.973  0.14 24.83 ?  102 LYS   A NZ   1 
ATOM   2008 H H    A LYS   A 1 102 ? 21.692 0.549   -12.580 0.86 28.25 ?  102 LYS   A H    1 
ATOM   2009 H H    B LYS   A 1 102 ? 21.433 0.822   -12.313 0.14 26.93 ?  102 LYS   A H    1 
ATOM   2010 H HA   A LYS   A 1 102 ? 23.001 2.191   -14.292 0.86 30.02 ?  102 LYS   A HA   1 
ATOM   2011 H HA   B LYS   A 1 102 ? 22.796 2.183   -14.180 0.14 27.75 ?  102 LYS   A HA   1 
ATOM   2012 H HB2  A LYS   A 1 102 ? 24.135 0.584   -12.263 0.86 31.89 ?  102 LYS   A HB2  1 
ATOM   2013 H HB2  B LYS   A 1 102 ? 23.728 0.463   -12.154 0.14 28.38 ?  102 LYS   A HB2  1 
ATOM   2014 H HB3  A LYS   A 1 102 ? 24.976 1.507   -13.241 0.86 31.89 ?  102 LYS   A HB3  1 
ATOM   2015 H HB3  B LYS   A 1 102 ? 24.687 1.126   -13.210 0.14 28.38 ?  102 LYS   A HB3  1 
ATOM   2016 H HG2  A LYS   A 1 102 ? 24.084 3.399   -12.249 0.86 33.44 ?  102 LYS   A HG2  1 
ATOM   2017 H HG2  B LYS   A 1 102 ? 24.256 3.232   -12.378 0.14 28.87 ?  102 LYS   A HG2  1 
ATOM   2018 H HG3  A LYS   A 1 102 ? 23.199 2.487   -11.288 0.86 33.44 ?  102 LYS   A HG3  1 
ATOM   2019 H HG3  B LYS   A 1 102 ? 23.254 2.614   -11.304 0.14 28.87 ?  102 LYS   A HG3  1 
ATOM   2020 H HD2  A LYS   A 1 102 ? 25.132 1.674   -10.267 0.86 34.91 ?  102 LYS   A HD2  1 
ATOM   2021 H HD2  B LYS   A 1 102 ? 25.030 1.480   -10.298 0.14 29.30 ?  102 LYS   A HD2  1 
ATOM   2022 H HD3  A LYS   A 1 102 ? 26.026 2.562   -11.240 0.86 34.91 ?  102 LYS   A HD3  1 
ATOM   2023 H HD3  B LYS   A 1 102 ? 26.032 2.091   -11.373 0.14 29.30 ?  102 LYS   A HD3  1 
ATOM   2024 H HE2  A LYS   A 1 102 ? 25.213 4.498   -10.259 0.86 36.19 ?  102 LYS   A HE2  1 
ATOM   2025 H HE2  B LYS   A 1 102 ? 25.700 4.212   -10.513 0.14 29.65 ?  102 LYS   A HE2  1 
ATOM   2026 H HE3  A LYS   A 1 102 ? 24.246 3.642   -9.330  0.86 36.19 ?  102 LYS   A HE3  1 
ATOM   2027 H HE3  B LYS   A 1 102 ? 24.629 3.646   -9.482  0.14 29.65 ?  102 LYS   A HE3  1 
ATOM   2028 H HZ1  A LYS   A 1 102 ? 26.107 4.270   -8.178  0.86 36.91 ?  102 LYS   A HZ1  1 
ATOM   2029 H HZ1  B LYS   A 1 102 ? 26.643 3.929   -8.462  0.14 29.81 ?  102 LYS   A HZ1  1 
ATOM   2030 H HZ2  A LYS   A 1 102 ? 26.097 2.824   -8.279  0.86 36.91 ?  102 LYS   A HZ2  1 
ATOM   2031 H HZ2  B LYS   A 1 102 ? 26.321 2.517   -8.455  0.14 29.81 ?  102 LYS   A HZ2  1 
ATOM   2032 H HZ3  A LYS   A 1 102 ? 26.978 3.603   -9.125  0.86 36.91 ?  102 LYS   A HZ3  1 
ATOM   2033 H HZ3  B LYS   A 1 102 ? 27.296 3.032   -9.394  0.14 29.81 ?  102 LYS   A HZ3  1 
ATOM   2034 N N    A GLY   A 1 103 ? 22.341 -0.695  -14.986 0.86 24.94 ?  103 GLY   A N    1 
ATOM   2035 N N    B GLY   A 1 103 ? 21.883 -0.687  -14.818 0.14 23.04 ?  103 GLY   A N    1 
ATOM   2036 C CA   A GLY   A 1 103 ? 22.549 -1.800  -15.904 0.86 24.55 ?  103 GLY   A CA   1 
ATOM   2037 C CA   B GLY   A 1 103 ? 21.973 -1.796  -15.743 0.14 22.77 ?  103 GLY   A CA   1 
ATOM   2038 C C    A GLY   A 1 103 ? 23.362 -2.954  -15.359 0.86 24.20 ?  103 GLY   A C    1 
ATOM   2039 C C    B GLY   A 1 103 ? 22.868 -2.925  -15.289 0.14 22.55 ?  103 GLY   A C    1 
ATOM   2040 O O    A GLY   A 1 103 ? 23.883 -3.752  -16.143 0.86 25.24 ?  103 GLY   A O    1 
ATOM   2041 O O    B GLY   A 1 103 ? 23.221 -3.781  -16.108 0.14 22.57 ?  103 GLY   A O    1 
ATOM   2042 H H    A GLY   A 1 103 ? 21.575 -0.702  -14.601 0.86 29.93 ?  103 GLY   A H    1 
ATOM   2043 H H    B GLY   A 1 103 ? 21.167 -0.685  -14.336 0.14 27.65 ?  103 GLY   A H    1 
ATOM   2044 H HA2  A GLY   A 1 103 ? 21.687 -2.149  -16.176 0.86 29.47 ?  103 GLY   A HA2  1 
ATOM   2045 H HA2  B GLY   A 1 103 ? 21.088 -2.160  -15.891 0.14 27.33 ?  103 GLY   A HA2  1 
ATOM   2046 H HA3  A GLY   A 1 103 ? 23.000 -1.467  -16.699 0.86 29.47 ?  103 GLY   A HA3  1 
ATOM   2047 H HA3  B GLY   A 1 103 ? 22.311 -1.469  -16.592 0.14 27.33 ?  103 GLY   A HA3  1 
ATOM   2048 N N    A GLU   A 1 104 ? 23.477 -3.082  -14.043 0.86 22.28 ?  104 GLU   A N    1 
ATOM   2049 N N    B GLU   A 1 104 ? 23.240 -2.959  -14.014 0.14 22.33 ?  104 GLU   A N    1 
ATOM   2050 C CA   A GLU   A 1 104 ? 24.364 -4.075  -13.457 0.86 20.87 ?  104 GLU   A CA   1 
ATOM   2051 C CA   B GLU   A 1 104 ? 24.184 -3.952  -13.528 0.14 22.07 ?  104 GLU   A CA   1 
ATOM   2052 C C    A GLU   A 1 104 ? 23.685 -5.440  -13.351 0.86 20.99 ?  104 GLU   A C    1 
ATOM   2053 C C    B GLU   A 1 104 ? 23.516 -5.315  -13.372 0.14 22.38 ?  104 GLU   A C    1 
ATOM   2054 O O    A GLU   A 1 104 ? 22.466 -5.548  -13.186 0.86 22.01 ?  104 GLU   A O    1 
ATOM   2055 O O    B GLU   A 1 104 ? 22.306 -5.423  -13.154 0.14 22.37 ?  104 GLU   A O    1 
ATOM   2056 C CB   A GLU   A 1 104 ? 24.886 -3.578  -12.104 0.86 19.61 ?  104 GLU   A CB   1 
ATOM   2057 C CB   B GLU   A 1 104 ? 24.801 -3.491  -12.208 0.14 21.60 ?  104 GLU   A CB   1 
ATOM   2058 C CG   A GLU   A 1 104 ? 25.823 -2.373  -12.279 0.86 19.37 ?  104 GLU   A CG   1 
ATOM   2059 C CG   B GLU   A 1 104 ? 25.705 -2.273  -12.370 0.14 21.35 ?  104 GLU   A CG   1 
ATOM   2060 C CD   A GLU   A 1 104 ? 26.162 -1.604  -11.012 0.86 18.43 ?  104 GLU   A CD   1 
ATOM   2061 C CD   B GLU   A 1 104 ? 26.092 -1.640  -11.047 0.14 21.07 ?  104 GLU   A CD   1 
ATOM   2062 O OE1  A GLU   A 1 104 ? 25.573 -1.867  -9.941  0.86 17.22 ?  104 GLU   A OE1  1 
ATOM   2063 O OE1  B GLU   A 1 104 ? 25.587 -2.087  -9.996  0.14 20.94 ?  104 GLU   A OE1  1 
ATOM   2064 O OE2  A GLU   A 1 104 ? 27.034 -0.708  -11.113 0.86 19.23 -1 104 GLU   A OE2  1 
ATOM   2065 O OE2  B GLU   A 1 104 ? 26.902 -0.689  -11.060 0.14 21.09 -1 104 GLU   A OE2  1 
ATOM   2066 H H    A GLU   A 1 104 ? 23.051 -2.606  -13.473 0.86 26.74 ?  104 GLU   A H    1 
ATOM   2067 H H    B GLU   A 1 104 ? 22.959 -2.411  -13.411 0.14 26.80 ?  104 GLU   A H    1 
ATOM   2068 H HA   A GLU   A 1 104 ? 25.132 -4.179  -14.039 0.86 25.05 ?  104 GLU   A HA   1 
ATOM   2069 H HA   B GLU   A 1 104 ? 24.899 -4.045  -14.173 0.14 26.49 ?  104 GLU   A HA   1 
ATOM   2070 H HB2  A GLU   A 1 104 ? 24.137 -3.308  -11.551 0.86 23.54 ?  104 GLU   A HB2  1 
ATOM   2071 H HB2  B GLU   A 1 104 ? 24.092 -3.254  -11.590 0.14 25.93 ?  104 GLU   A HB2  1 
ATOM   2072 H HB3  A GLU   A 1 104 ? 25.383 -4.292  -11.673 0.86 23.54 ?  104 GLU   A HB3  1 
ATOM   2073 H HB3  B GLU   A 1 104 ? 25.336 -4.211  -11.838 0.14 25.93 ?  104 GLU   A HB3  1 
ATOM   2074 H HG2  A GLU   A 1 104 ? 26.658 -2.686  -12.656 0.86 23.25 ?  104 GLU   A HG2  1 
ATOM   2075 H HG2  B GLU   A 1 104 ? 26.522 -2.543  -12.821 0.14 25.63 ?  104 GLU   A HG2  1 
ATOM   2076 H HG3  A GLU   A 1 104 ? 25.404 -1.745  -12.885 0.86 23.25 ?  104 GLU   A HG3  1 
ATOM   2077 H HG3  B GLU   A 1 104 ? 25.243 -1.605  -12.902 0.14 25.63 ?  104 GLU   A HG3  1 
ATOM   2078 N N    A ASP   A 1 105 ? 24.502 -6.486  -13.451 0.86 21.96 ?  105 ASP   A N    1 
ATOM   2079 N N    B ASP   A 1 105 ? 24.330 -6.361  -13.489 0.14 22.80 ?  105 ASP   A N    1 
ATOM   2080 C CA   A ASP   A 1 105 ? 24.014 -7.855  -13.580 0.86 23.20 ?  105 ASP   A CA   1 
ATOM   2081 C CA   B ASP   A 1 105 ? 23.830 -7.729  -13.525 0.14 23.28 ?  105 ASP   A CA   1 
ATOM   2082 C C    A ASP   A 1 105 ? 23.328 -8.301  -12.293 0.86 20.92 ?  105 ASP   A C    1 
ATOM   2083 C C    B ASP   A 1 105 ? 23.192 -8.091  -12.189 0.14 22.77 ?  105 ASP   A C    1 
ATOM   2084 O O    A ASP   A 1 105 ? 23.960 -8.366  -11.237 0.86 18.78 ?  105 ASP   A O    1 
ATOM   2085 O O    B ASP   A 1 105 ? 23.846 -8.027  -11.143 0.14 22.68 ?  105 ASP   A O    1 
ATOM   2086 C CB   A ASP   A 1 105 ? 25.201 -8.763  -13.897 0.86 26.74 ?  105 ASP   A CB   1 
ATOM   2087 C CB   B ASP   A 1 105 ? 24.984 -8.680  -13.834 0.14 24.19 ?  105 ASP   A CB   1 
ATOM   2088 C CG   A ASP   A 1 105 ? 24.788 -10.192 -14.159 0.86 29.95 ?  105 ASP   A CG   1 
ATOM   2089 C CG   B ASP   A 1 105 ? 24.569 -10.133 -13.778 0.14 24.95 ?  105 ASP   A CG   1 
ATOM   2090 O OD1  A ASP   A 1 105 ? 23.572 -10.443 -14.267 0.86 30.58 ?  105 ASP   A OD1  1 
ATOM   2091 O OD1  B ASP   A 1 105 ? 23.372 -10.413 -13.994 0.14 25.22 ?  105 ASP   A OD1  1 
ATOM   2092 O OD2  A ASP   A 1 105 ? 25.684 -11.060 -14.261 0.86 31.79 -1 105 ASP   A OD2  1 
ATOM   2093 O OD2  B ASP   A 1 105 ? 25.434 -10.993 -13.509 0.14 25.26 -1 105 ASP   A OD2  1 
ATOM   2094 H H    A ASP   A 1 105 ? 25.363 -6.426  -13.445 0.86 26.36 ?  105 ASP   A H    1 
ATOM   2095 H H    B ASP   A 1 105 ? 25.183 -6.301  -13.541 0.14 27.37 ?  105 ASP   A H    1 
ATOM   2096 H HA   A ASP   A 1 105 ? 23.379 -7.909  -14.306 0.86 27.85 ?  105 ASP   A HA   1 
ATOM   2097 H HA   B ASP   A 1 105 ? 23.162 -7.818  -14.220 0.14 27.94 ?  105 ASP   A HA   1 
ATOM   2098 H HB2  A ASP   A 1 105 ? 25.652 -8.430  -14.692 0.86 32.10 ?  105 ASP   A HB2  1 
ATOM   2099 H HB2  B ASP   A 1 105 ? 25.310 -8.501  -14.731 0.14 29.03 ?  105 ASP   A HB2  1 
ATOM   2100 H HB3  A ASP   A 1 105 ? 25.816 -8.760  -13.147 0.86 32.10 ?  105 ASP   A HB3  1 
ATOM   2101 H HB3  B ASP   A 1 105 ? 25.696 -8.535  -13.189 0.14 29.03 ?  105 ASP   A HB3  1 
ATOM   2102 N N    A ILE   A 1 106 ? 22.039 -8.635  -12.384 0.86 21.08 ?  106 ILE   A N    1 
ATOM   2103 N N    B ILE   A 1 106 ? 21.914 -8.476  -12.225 0.14 22.33 ?  106 ILE   A N    1 
ATOM   2104 C CA   A ILE   A 1 106 ? 21.289 -9.034  -11.200 0.86 20.64 ?  106 ILE   A CA   1 
ATOM   2105 C CA   B ILE   A 1 106 ? 21.222 -8.854  -10.999 0.14 21.77 ?  106 ILE   A CA   1 
ATOM   2106 C C    A ILE   A 1 106 ? 21.828 -10.320 -10.599 0.86 19.73 ?  106 ILE   A C    1 
ATOM   2107 C C    B ILE   A 1 106 ? 21.720 -10.184 -10.448 0.14 21.28 ?  106 ILE   A C    1 
ATOM   2108 O O    A ILE   A 1 106 ? 21.611 -10.578 -9.412  0.86 18.95 ?  106 ILE   A O    1 
ATOM   2109 O O    B ILE   A 1 106 ? 21.496 -10.479 -9.268  0.14 21.11 ?  106 ILE   A O    1 
ATOM   2110 C CB   A ILE   A 1 106 ? 19.777 -9.124  -11.517 0.86 22.22 ?  106 ILE   A CB   1 
ATOM   2111 C CB   B ILE   A 1 106 ? 19.692 -8.845  -11.200 0.14 21.78 ?  106 ILE   A CB   1 
ATOM   2112 C CG1  A ILE   A 1 106 ? 18.952 -9.217  -10.231 0.86 22.97 ?  106 ILE   A CG1  1 
ATOM   2113 C CG1  B ILE   A 1 106 ? 18.968 -8.771  -9.851  0.14 21.71 ?  106 ILE   A CG1  1 
ATOM   2114 C CG2  A ILE   A 1 106 ? 19.482 -10.314 -12.413 0.86 22.92 ?  106 ILE   A CG2  1 
ATOM   2115 C CG2  B ILE   A 1 106 ? 19.241 -10.082 -11.962 0.14 21.89 ?  106 ILE   A CG2  1 
ATOM   2116 C CD1  A ILE   A 1 106 ? 19.077 -8.004  -9.337  0.86 23.39 ?  106 ILE   A CD1  1 
ATOM   2117 C CD1  B ILE   A 1 106 ? 19.377 -7.588  -8.997  0.14 21.66 ?  106 ILE   A CD1  1 
ATOM   2118 H H    A ILE   A 1 106 ? 21.591 -8.636  -13.110 0.86 25.30 ?  106 ILE   A H    1 
ATOM   2119 H H    B ILE   A 1 106 ? 21.430 -8.507  -12.933 0.14 26.80 ?  106 ILE   A H    1 
ATOM   2120 H HA   A ILE   A 1 106 ? 21.405 -8.354  -10.528 0.86 24.78 ?  106 ILE   A HA   1 
ATOM   2121 H HA   B ILE   A 1 106 ? 21.435 -8.186  -10.337 0.14 26.14 ?  106 ILE   A HA   1 
ATOM   2122 H HB   A ILE   A 1 106 ? 19.520 -8.318  -11.988 0.86 26.67 ?  106 ILE   A HB   1 
ATOM   2123 H HB   B ILE   A 1 106 ? 19.451 -8.062  -11.718 0.14 26.15 ?  106 ILE   A HB   1 
ATOM   2124 H HG12 A ILE   A 1 106 ? 18.017 -9.312  -10.468 0.86 27.58 ?  106 ILE   A HG12 1 
ATOM   2125 H HG12 B ILE   A 1 106 ? 18.013 -8.701  -10.010 0.14 26.06 ?  106 ILE   A HG12 1 
ATOM   2126 H HG13 A ILE   A 1 106 ? 19.243 -9.990  -9.724  0.86 27.58 ?  106 ILE   A HG13 1 
ATOM   2127 H HG13 B ILE   A 1 106 ? 19.157 -9.578  -9.348  0.14 26.06 ?  106 ILE   A HG13 1 
ATOM   2128 H HG21 A ILE   A 1 106 ? 18.576 -10.233 -12.751 0.86 27.51 ?  106 ILE   A HG21 1 
ATOM   2129 H HG21 B ILE   A 1 106 ? 18.338 -9.941  -12.288 0.14 26.28 ?  106 ILE   A HG21 1 
ATOM   2130 H HG22 A ILE   A 1 106 ? 20.111 -10.315 -13.149 0.86 27.51 ?  106 ILE   A HG22 1 
ATOM   2131 H HG22 B ILE   A 1 106 ? 19.843 -10.227 -12.708 0.14 26.28 ?  106 ILE   A HG22 1 
ATOM   2132 H HG23 A ILE   A 1 106 ? 19.571 -11.129 -11.897 0.86 27.51 ?  106 ILE   A HG23 1 
ATOM   2133 H HG23 B ILE   A 1 106 ? 19.260 -10.848 -11.367 0.14 26.28 ?  106 ILE   A HG23 1 
ATOM   2134 H HD11 A ILE   A 1 106 ? 18.360 -8.018  -8.686  0.86 28.07 ?  106 ILE   A HD11 1 
ATOM   2135 H HD11 B ILE   A 1 106 ? 18.676 -7.407  -8.356  0.14 26.00 ?  106 ILE   A HD11 1 
ATOM   2136 H HD12 A ILE   A 1 106 ? 19.935 -8.032  -8.882  0.86 28.07 ?  106 ILE   A HD12 1 
ATOM   2137 H HD12 B ILE   A 1 106 ? 20.202 -7.805  -8.533  0.14 26.00 ?  106 ILE   A HD12 1 
ATOM   2138 H HD13 A ILE   A 1 106 ? 19.016 -7.203  -9.881  0.86 28.07 ?  106 ILE   A HD13 1 
ATOM   2139 H HD13 B ILE   A 1 106 ? 19.511 -6.817  -9.572  0.14 26.00 ?  106 ILE   A HD13 1 
ATOM   2140 N N    A GLN   A 1 107 ? 22.524 -11.143 -11.396 0.86 20.16 ?  107 GLN   A N    1 
ATOM   2141 N N    B GLN   A 1 107 ? 22.396 -11.000 -11.262 0.14 21.12 ?  107 GLN   A N    1 
ATOM   2142 C CA   A GLN   A 1 107 ? 23.151 -12.350 -10.864 0.86 22.23 ?  107 GLN   A CA   1 
ATOM   2143 C CA   B GLN   A 1 107 ? 22.960 -12.241 -10.742 0.14 20.89 ?  107 GLN   A CA   1 
ATOM   2144 C C    A GLN   A 1 107 ? 24.122 -12.014 -9.742  0.86 20.23 ?  107 GLN   A C    1 
ATOM   2145 C C    B GLN   A 1 107 ? 24.047 -11.977 -9.709  0.14 18.83 ?  107 GLN   A C    1 
ATOM   2146 O O    A GLN   A 1 107 ? 24.367 -12.845 -8.859  0.86 21.98 ?  107 GLN   A O    1 
ATOM   2147 O O    B GLN   A 1 107 ? 24.319 -12.846 -8.873  0.14 19.29 ?  107 GLN   A O    1 
ATOM   2148 C CB   A GLN   A 1 107 ? 23.877 -13.102 -11.984 0.86 26.39 ?  107 GLN   A CB   1 
ATOM   2149 C CB   B GLN   A 1 107 ? 23.501 -13.114 -11.878 0.14 22.66 ?  107 GLN   A CB   1 
ATOM   2150 C CG   A GLN   A 1 107 ? 23.026 -13.339 -13.226 0.86 30.91 ?  107 GLN   A CG   1 
ATOM   2151 C CG   B GLN   A 1 107 ? 22.537 -13.304 -13.044 0.14 24.37 ?  107 GLN   A CG   1 
ATOM   2152 C CD   A GLN   A 1 107 ? 21.750 -14.097 -12.924 0.86 34.36 ?  107 GLN   A CD   1 
ATOM   2153 C CD   B GLN   A 1 107 ? 21.127 -13.645 -12.606 0.14 25.70 ?  107 GLN   A CD   1 
ATOM   2154 O OE1  A GLN   A 1 107 ? 21.775 -15.148 -12.282 0.86 35.61 ?  107 GLN   A OE1  1 
ATOM   2155 O OE1  B GLN   A 1 107 ? 20.921 -14.438 -11.688 0.14 26.17 ?  107 GLN   A OE1  1 
ATOM   2156 N NE2  A GLN   A 1 107 ? 20.622 -13.562 -13.378 0.86 35.51 ?  107 GLN   A NE2  1 
ATOM   2157 N NE2  B GLN   A 1 107 ? 20.143 -13.039 -13.265 0.14 26.08 ?  107 GLN   A NE2  1 
ATOM   2158 H H    A GLN   A 1 107 ? 22.649 -11.024 -12.234 0.86 24.20 ?  107 GLN   A H    1 
ATOM   2159 H H    B GLN   A 1 107 ? 22.540 -10.859 -12.099 0.14 25.36 ?  107 GLN   A H    1 
ATOM   2160 H HA   A GLN   A 1 107 ? 22.475 -12.942 -10.505 0.86 26.68 ?  107 GLN   A HA   1 
ATOM   2161 H HA   B GLN   A 1 107 ? 22.257 -12.737 -10.301 0.14 25.08 ?  107 GLN   A HA   1 
ATOM   2162 H HB2  A GLN   A 1 107 ? 24.659 -12.593 -12.255 0.86 31.68 ?  107 GLN   A HB2  1 
ATOM   2163 H HB2  B GLN   A 1 107 ? 24.309 -12.708 -12.227 0.14 27.21 ?  107 GLN   A HB2  1 
ATOM   2164 H HB3  A GLN   A 1 107 ? 24.157 -13.974 -11.655 0.86 31.68 ?  107 GLN   A HB3  1 
ATOM   2165 H HB3  B GLN   A 1 107 ? 23.706 -13.993 -11.521 0.14 27.21 ?  107 GLN   A HB3  1 
ATOM   2166 H HG2  A GLN   A 1 107 ? 22.782 -12.484 -13.614 0.86 37.10 ?  107 GLN   A HG2  1 
ATOM   2167 H HG2  B GLN   A 1 107 ? 22.495 -12.487 -13.560 0.14 29.25 ?  107 GLN   A HG2  1 
ATOM   2168 H HG3  A GLN   A 1 107 ? 23.541 -13.853 -13.867 0.86 37.10 ?  107 GLN   A HG3  1 
ATOM   2169 H HG3  B GLN   A 1 107 ? 22.859 -14.029 -13.602 0.14 29.25 ?  107 GLN   A HG3  1 
ATOM   2170 H HE21 A GLN   A 1 107 ? 20.642 -12.826 -13.821 0.86 42.62 ?  107 GLN   A HE21 1 
ATOM   2171 H HE21 B GLN   A 1 107 ? 20.328 -12.489 -13.901 0.14 31.30 ?  107 GLN   A HE21 1 
ATOM   2172 H HE22 A GLN   A 1 107 ? 19.873 -13.956 -13.230 0.86 42.62 ?  107 GLN   A HE22 1 
ATOM   2173 H HE22 B GLN   A 1 107 ? 19.323 -13.197 -13.059 0.14 31.30 ?  107 GLN   A HE22 1 
ATOM   2174 N N    . LEU   A 1 108 ? 24.669 -10.795 -9.744  1.00 16.40 ?  108 LEU   A N    1 
ATOM   2175 C CA   . LEU   A 1 108 ? 25.603 -10.395 -8.704  1.00 13.80 ?  108 LEU   A CA   1 
ATOM   2176 C C    . LEU   A 1 108 ? 24.922 -10.240 -7.356  1.00 11.98 ?  108 LEU   A C    1 
ATOM   2177 O O    . LEU   A 1 108 ? 25.614 -10.097 -6.347  1.00 12.23 ?  108 LEU   A O    1 
ATOM   2178 C CB   . LEU   A 1 108 ? 26.314 -9.097  -9.105  1.00 13.21 ?  108 LEU   A CB   1 
ATOM   2179 C CG   . LEU   A 1 108 ? 27.321 -9.280  -10.241 1.00 14.95 ?  108 LEU   A CG   1 
ATOM   2180 C CD1  . LEU   A 1 108 ? 27.777 -7.939  -10.793 1.00 15.65 ?  108 LEU   A CD1  1 
ATOM   2181 C CD2  . LEU   A 1 108 ? 28.526 -10.090 -9.769  1.00 16.88 ?  108 LEU   A CD2  1 
ATOM   2182 H H    A LEU   A 1 108 ? 24.513 -10.193 -10.333 0.86 19.69 ?  108 LEU   A H    1 
ATOM   2183 H H    B LEU   A 1 108 ? 24.569 -10.216 -10.368 0.14 19.69 ?  108 LEU   A H    1 
ATOM   2184 H HA   . LEU   A 1 108 ? 26.277 -11.083 -8.604  1.00 16.56 ?  108 LEU   A HA   1 
ATOM   2185 H HB2  . LEU   A 1 108 ? 25.649 -8.455  -9.401  1.00 15.86 ?  108 LEU   A HB2  1 
ATOM   2186 H HB3  . LEU   A 1 108 ? 26.790 -8.749  -8.339  1.00 15.86 ?  108 LEU   A HB3  1 
ATOM   2187 H HG   . LEU   A 1 108 ? 26.899 -9.770  -10.965 1.00 17.95 ?  108 LEU   A HG   1 
ATOM   2188 H HD11 . LEU   A 1 108 ? 28.371 -8.091  -11.547 1.00 18.79 ?  108 LEU   A HD11 1 
ATOM   2189 H HD12 . LEU   A 1 108 ? 27.001 -7.434  -11.081 1.00 18.79 ?  108 LEU   A HD12 1 
ATOM   2190 H HD13 . LEU   A 1 108 ? 28.248 -7.454  -10.097 1.00 18.79 ?  108 LEU   A HD13 1 
ATOM   2191 H HD21 . LEU   A 1 108 ? 29.222 -10.039 -10.441 1.00 20.27 ?  108 LEU   A HD21 1 
ATOM   2192 H HD22 . LEU   A 1 108 ? 28.844 -9.717  -8.932  1.00 20.27 ?  108 LEU   A HD22 1 
ATOM   2193 H HD23 . LEU   A 1 108 ? 28.255 -11.012 -9.640  1.00 20.27 ?  108 LEU   A HD23 1 
ATOM   2194 N N    . LEU   A 1 109 ? 23.590 -10.291 -7.306  1.00 11.41 ?  109 LEU   A N    1 
ATOM   2195 C CA   . LEU   A 1 109 ? 22.905 -10.175 -6.027  1.00 10.83 ?  109 LEU   A CA   1 
ATOM   2196 C C    . LEU   A 1 109 ? 23.261 -11.331 -5.097  1.00 9.85  ?  109 LEU   A C    1 
ATOM   2197 O O    . LEU   A 1 109 ? 23.401 -11.136 -3.883  1.00 10.37 ?  109 LEU   A O    1 
ATOM   2198 C CB   . LEU   A 1 109 ? 21.399 -10.089 -6.264  1.00 11.41 ?  109 LEU   A CB   1 
ATOM   2199 C CG   . LEU   A 1 109 ? 20.521 -9.802  -5.053  1.00 11.61 ?  109 LEU   A CG   1 
ATOM   2200 C CD1  . LEU   A 1 109 ? 20.971 -8.535  -4.343  1.00 12.25 ?  109 LEU   A CD1  1 
ATOM   2201 C CD2  . LEU   A 1 109 ? 19.068 -9.683  -5.476  1.00 12.52 ?  109 LEU   A CD2  1 
ATOM   2202 H H    . LEU   A 1 109 ? 23.070 -10.393 -7.982  1.00 13.70 ?  109 LEU   A H    1 
ATOM   2203 H HA   . LEU   A 1 109 ? 23.188 -9.352  -5.599  1.00 13.00 ?  109 LEU   A HA   1 
ATOM   2204 H HB2  . LEU   A 1 109 ? 21.236 -9.378  -6.905  1.00 13.71 ?  109 LEU   A HB2  1 
ATOM   2205 H HB3  . LEU   A 1 109 ? 21.102 -10.930 -6.635  1.00 13.71 ?  109 LEU   A HB3  1 
ATOM   2206 H HG   . LEU   A 1 109 ? 20.592 -10.536 -4.425  1.00 13.94 ?  109 LEU   A HG   1 
ATOM   2207 H HD11 . LEU   A 1 109 ? 20.304 -8.277  -3.690  1.00 14.71 ?  109 LEU   A HD11 1 
ATOM   2208 H HD12 . LEU   A 1 109 ? 21.820 -8.700  -3.901  1.00 14.71 ?  109 LEU   A HD12 1 
ATOM   2209 H HD13 . LEU   A 1 109 ? 21.078 -7.823  -5.000  1.00 14.71 ?  109 LEU   A HD13 1 
ATOM   2210 H HD21 . LEU   A 1 109 ? 18.535 -9.403  -4.712  1.00 15.03 ?  109 LEU   A HD21 1 
ATOM   2211 H HD22 . LEU   A 1 109 ? 18.993 -9.026  -6.185  1.00 15.03 ?  109 LEU   A HD22 1 
ATOM   2212 H HD23 . LEU   A 1 109 ? 18.757 -10.547 -5.793  1.00 15.03 ?  109 LEU   A HD23 1 
ATOM   2213 N N    . LYS   A 1 110 ? 23.420 -12.543 -5.641  1.00 9.81  ?  110 LYS   A N    1 
ATOM   2214 C CA   . LYS   A 1 110 ? 23.802 -13.668 -4.791  1.00 9.66  ?  110 LYS   A CA   1 
ATOM   2215 C C    . LYS   A 1 110 ? 25.187 -13.443 -4.189  1.00 9.25  ?  110 LYS   A C    1 
ATOM   2216 O O    . LYS   A 1 110 ? 25.393 -13.645 -2.989  1.00 9.50  ?  110 LYS   A O    1 
ATOM   2217 C CB   . LYS   A 1 110 ? 23.716 -14.988 -5.564  1.00 10.33 ?  110 LYS   A CB   1 
ATOM   2218 C CG   . LYS   A 1 110 ? 23.941 -16.212 -4.667  1.00 10.48 ?  110 LYS   A CG   1 
ATOM   2219 C CD   . LYS   A 1 110 ? 23.698 -17.531 -5.378  1.00 11.09 ?  110 LYS   A CD   1 
ATOM   2220 C CE   . LYS   A 1 110 ? 23.799 -18.719 -4.426  1.00 12.05 ?  110 LYS   A CE   1 
ATOM   2221 N NZ   . LYS   A 1 110 ? 22.623 -18.844 -3.519  1.00 12.49 ?  110 LYS   A NZ   1 
ATOM   2222 H H    . LYS   A 1 110 ? 23.307 -12.733 -6.472  1.00 11.79 ?  110 LYS   A H    1 
ATOM   2223 H HA   . LYS   A 1 110 ? 23.167 -13.723 -4.057  1.00 11.61 ?  110 LYS   A HA   1 
ATOM   2224 H HB2  . LYS   A 1 110 ? 22.834 -15.067 -5.962  1.00 12.40 ?  110 LYS   A HB2  1 
ATOM   2225 H HB3  . LYS   A 1 110 ? 24.394 -14.991 -6.256  1.00 12.40 ?  110 LYS   A HB3  1 
ATOM   2226 H HG2  . LYS   A 1 110 ? 24.861 -16.205 -4.355  1.00 12.59 ?  110 LYS   A HG2  1 
ATOM   2227 H HG3  . LYS   A 1 110 ? 23.338 -16.162 -3.911  1.00 12.59 ?  110 LYS   A HG3  1 
ATOM   2228 H HD2  . LYS   A 1 110 ? 22.810 -17.528 -5.762  1.00 13.32 ?  110 LYS   A HD2  1 
ATOM   2229 H HD3  . LYS   A 1 110 ? 24.365 -17.646 -6.074  1.00 13.32 ?  110 LYS   A HD3  1 
ATOM   2230 H HE2  . LYS   A 1 110 ? 23.864 -19.534 -4.945  1.00 14.47 ?  110 LYS   A HE2  1 
ATOM   2231 H HE3  . LYS   A 1 110 ? 24.592 -18.614 -3.874  1.00 14.47 ?  110 LYS   A HE3  1 
ATOM   2232 H HZ1  . LYS   A 1 110 ? 22.726 -19.544 -2.984  1.00 15.00 ?  110 LYS   A HZ1  1 
ATOM   2233 H HZ2  . LYS   A 1 110 ? 22.546 -18.107 -3.023  1.00 15.00 ?  110 LYS   A HZ2  1 
ATOM   2234 H HZ3  . LYS   A 1 110 ? 21.882 -18.947 -3.999  1.00 15.00 ?  110 LYS   A HZ3  1 
ATOM   2235 N N    . SER   A 1 111 ? 26.143 -13.006 -5.012  1.00 9.40  ?  111 SER   A N    1 
ATOM   2236 C CA   . SER   A 1 111 ? 27.477 -12.693 -4.506  1.00 9.77  ?  111 SER   A CA   1 
ATOM   2237 C C    . SER   A 1 111 ? 27.413 -11.651 -3.392  1.00 9.33  ?  111 SER   A C    1 
ATOM   2238 O O    . SER   A 1 111 ? 28.115 -11.763 -2.380  1.00 9.83  ?  111 SER   A O    1 
ATOM   2239 C CB   . SER   A 1 111 ? 28.361 -12.199 -5.652  1.00 10.90 ?  111 SER   A CB   1 
ATOM   2240 O OG   . SER   A 1 111 ? 28.475 -13.194 -6.658  1.00 13.34 ?  111 SER   A OG   1 
ATOM   2241 H H    . SER   A 1 111 ? 26.042 -12.882 -5.856  1.00 11.29 ?  111 SER   A H    1 
ATOM   2242 H HA   . SER   A 1 111 ? 27.875 -13.495 -4.142  1.00 11.73 ?  111 SER   A HA   1 
ATOM   2243 H HB2  . SER   A 1 111 ? 27.962 -11.403 -6.041  1.00 13.09 ?  111 SER   A HB2  1 
ATOM   2244 H HB3  . SER   A 1 111 ? 29.242 -11.990 -5.305  1.00 13.09 ?  111 SER   A HB3  1 
ATOM   2245 H HG   . SER   A 1 111 ? 28.973 -12.907 -7.282  1.00 16.02 ?  111 SER   A HG   1 
ATOM   2246 N N    . ALA   A 1 112 ? 26.569 -10.632 -3.564  1.00 9.39  ?  112 ALA   A N    1 
ATOM   2247 C CA   . ALA   A 1 112 ? 26.428 -9.597  -2.541  1.00 9.29  ?  112 ALA   A CA   1 
ATOM   2248 C C    . ALA   A 1 112 ? 25.953 -10.196 -1.220  1.00 9.12  ?  112 ALA   A C    1 
ATOM   2249 O O    . ALA   A 1 112 ? 26.511 -9.904  -0.153  1.00 9.29  ?  112 ALA   A O    1 
ATOM   2250 C CB   . ALA   A 1 112 ? 25.474 -8.508  -3.032  1.00 9.82  ?  112 ALA   A CB   1 
ATOM   2251 H H    . ALA   A 1 112 ? 26.073 -10.512 -4.254  1.00 11.28 ?  112 ALA   A H    1 
ATOM   2252 H HA   . ALA   A 1 112 ? 27.289 -9.182  -2.383  1.00 11.16 ?  112 ALA   A HA   1 
ATOM   2253 H HB1  . ALA   A 1 112 ? 25.395 -7.818  -2.346  1.00 11.79 ?  112 ALA   A HB1  1 
ATOM   2254 H HB2  . ALA   A 1 112 ? 25.825 -8.117  -3.846  1.00 11.79 ?  112 ALA   A HB2  1 
ATOM   2255 H HB3  . ALA   A 1 112 ? 24.601 -8.897  -3.200  1.00 11.79 ?  112 ALA   A HB3  1 
ATOM   2256 N N    . TYR   A 1 113 ? 24.922 -11.049 -1.268  1.00 9.10  ?  113 TYR   A N    1 
ATOM   2257 C CA   . TYR   A 1 113 ? 24.419 -11.660 -0.040  1.00 8.88  ?  113 TYR   A CA   1 
ATOM   2258 C C    . TYR   A 1 113 ? 25.431 -12.607 0.601   1.00 8.51  ?  113 TYR   A C    1 
ATOM   2259 O O    . TYR   A 1 113 ? 25.398 -12.797 1.820   1.00 9.13  ?  113 TYR   A O    1 
ATOM   2260 C CB   . TYR   A 1 113 ? 23.099 -12.391 -0.302  1.00 9.23  ?  113 TYR   A CB   1 
ATOM   2261 C CG   . TYR   A 1 113 ? 21.879 -11.507 -0.197  1.00 9.20  ?  113 TYR   A CG   1 
ATOM   2262 C CD1  . TYR   A 1 113 ? 21.524 -10.926 1.016   1.00 9.57  ?  113 TYR   A CD1  1 
ATOM   2263 C CD2  . TYR   A 1 113 ? 21.069 -11.260 -1.300  1.00 9.63  ?  113 TYR   A CD2  1 
ATOM   2264 C CE1  . TYR   A 1 113 ? 20.395 -10.136 1.134   1.00 9.80  ?  113 TYR   A CE1  1 
ATOM   2265 C CE2  . TYR   A 1 113 ? 19.918 -10.469 -1.188  1.00 9.74  ?  113 TYR   A CE2  1 
ATOM   2266 C CZ   . TYR   A 1 113 ? 19.596 -9.906  0.028   1.00 9.68  ?  113 TYR   A CZ   1 
ATOM   2267 O OH   . TYR   A 1 113 ? 18.468 -9.118  0.179   1.00 10.29 ?  113 TYR   A OH   1 
ATOM   2268 H H    . TYR   A 1 113 ? 24.507 -11.284 -1.984  1.00 10.93 ?  113 TYR   A H    1 
ATOM   2269 H HA   . TYR   A 1 113 ? 24.243 -10.953 0.599   1.00 10.67 ?  113 TYR   A HA   1 
ATOM   2270 H HB2  . TYR   A 1 113 ? 23.116 -12.755 -1.198  1.00 11.08 ?  113 TYR   A HB2  1 
ATOM   2271 H HB3  . TYR   A 1 113 ? 23.003 -13.101 0.347   1.00 11.08 ?  113 TYR   A HB3  1 
ATOM   2272 H HD1  . TYR   A 1 113 ? 22.052 -11.077 1.767   1.00 11.49 ?  113 TYR   A HD1  1 
ATOM   2273 H HD2  . TYR   A 1 113 ? 21.279 -11.645 -2.116  1.00 11.57 ?  113 TYR   A HD2  1 
ATOM   2274 H HE1  . TYR   A 1 113 ? 20.175 -9.756  1.956   1.00 11.77 ?  113 TYR   A HE1  1 
ATOM   2275 H HE2  . TYR   A 1 113 ? 19.377 -10.309 -1.930  1.00 11.70 ?  113 TYR   A HE2  1 
ATOM   2276 H HH   . TYR   A 1 113 ? 18.068 -9.055  -0.561  1.00 12.35 ?  113 TYR   A HH   1 
ATOM   2277 N N    . GLU   A 1 114 ? 26.327 -13.216 -0.186  1.00 8.92  ?  114 GLU   A N    1 
ATOM   2278 C CA   . GLU   A 1 114 ? 27.315 -14.118 0.405   1.00 8.81  ?  114 GLU   A CA   1 
ATOM   2279 C C    . GLU   A 1 114 ? 28.171 -13.410 1.454   1.00 8.78  ?  114 GLU   A C    1 
ATOM   2280 O O    . GLU   A 1 114 ? 28.655 -14.050 2.398   1.00 9.11  ?  114 GLU   A O    1 
ATOM   2281 C CB   . GLU   A 1 114 ? 28.179 -14.759 -0.689  1.00 8.99  ?  114 GLU   A CB   1 
ATOM   2282 C CG   . GLU   A 1 114 ? 27.414 -15.808 -1.475  1.00 9.31  ?  114 GLU   A CG   1 
ATOM   2283 C CD   . GLU   A 1 114 ? 28.117 -16.342 -2.720  1.00 10.01 ?  114 GLU   A CD   1 
ATOM   2284 O OE1  . GLU   A 1 114 ? 29.066 -15.710 -3.229  1.00 10.24 ?  114 GLU   A OE1  1 
ATOM   2285 O OE2  . GLU   A 1 114 ? 27.672 -17.408 -3.206  1.00 10.96 -1 114 GLU   A OE2  1 
ATOM   2286 H H    . GLU   A 1 114 ? 26.382 -13.118 -1.045  1.00 10.71 ?  114 GLU   A H    1 
ATOM   2287 H HA   . GLU   A 1 114 ? 26.842 -14.833 0.846   1.00 10.59 ?  114 GLU   A HA   1 
ATOM   2288 H HB2  . GLU   A 1 114 ? 28.472 -14.074 -1.317  1.00 10.79 ?  114 GLU   A HB2  1 
ATOM   2289 H HB3  . GLU   A 1 114 ? 28.946 -15.189 -0.286  1.00 10.79 ?  114 GLU   A HB3  1 
ATOM   2290 H HG2  . GLU   A 1 114 ? 27.246 -16.568 -0.898  1.00 11.18 ?  114 GLU   A HG2  1 
ATOM   2291 H HG3  . GLU   A 1 114 ? 26.567 -15.429 -1.764  1.00 11.18 ?  114 GLU   A HG3  1 
ATOM   2292 N N    . ASN   A 1 115 ? 28.352 -12.089 1.328   1.00 8.93  ?  115 ASN   A N    1 
ATOM   2293 C CA   . ASN   A 1 115 ? 29.123 -11.365 2.333   1.00 8.89  ?  115 ASN   A CA   1 
ATOM   2294 C C    . ASN   A 1 115 ? 28.510 -11.505 3.721   1.00 8.79  ?  115 ASN   A C    1 
ATOM   2295 O O    . ASN   A 1 115 ? 29.224 -11.431 4.726   1.00 9.16  ?  115 ASN   A O    1 
ATOM   2296 C CB   . ASN   A 1 115 ? 29.225 -9.884  1.959   1.00 9.29  ?  115 ASN   A CB   1 
ATOM   2297 C CG   . ASN   A 1 115 ? 30.015 -9.657  0.695   1.00 10.40 ?  115 ASN   A CG   1 
ATOM   2298 O OD1  . ASN   A 1 115 ? 31.231 -9.760  0.698   1.00 13.69 ?  115 ASN   A OD1  1 
ATOM   2299 N ND2  . ASN   A 1 115 ? 29.329 -9.355  -0.391  1.00 9.95  ?  115 ASN   A ND2  1 
ATOM   2300 H H    . ASN   A 1 115 ? 28.043 -11.603 0.686   1.00 10.72 ?  115 ASN   A H    1 
ATOM   2301 H HA   . ASN   A 1 115 ? 30.016 -11.731 2.367   1.00 10.68 ?  115 ASN   A HA   1 
ATOM   2302 H HB2  . ASN   A 1 115 ? 28.331 -9.530  1.833   1.00 11.15 ?  115 ASN   A HB2  1 
ATOM   2303 H HB3  . ASN   A 1 115 ? 29.668 -9.412  2.683   1.00 11.15 ?  115 ASN   A HB3  1 
ATOM   2304 H HD21 . ASN   A 1 115 ? 29.736 -9.212  -1.130  1.00 11.95 ?  115 ASN   A HD21 1 
ATOM   2305 H HD22 . ASN   A 1 115 ? 28.467 -9.303  -0.355  1.00 11.95 ?  115 ASN   A HD22 1 
ATOM   2306 N N    . PHE   A 1 116 ? 27.184 -11.669 3.801   1.00 8.65  ?  116 PHE   A N    1 
ATOM   2307 C CA   . PHE   A 1 116 ? 26.537 -11.779 5.105   1.00 8.88  ?  116 PHE   A CA   1 
ATOM   2308 C C    . PHE   A 1 116 ? 27.020 -13.014 5.869   1.00 9.03  ?  116 PHE   A C    1 
ATOM   2309 O O    . PHE   A 1 116 ? 26.951 -13.034 7.096   1.00 9.55  ?  116 PHE   A O    1 
ATOM   2310 C CB   . PHE   A 1 116 ? 25.006 -11.905 4.975   1.00 9.03  ?  116 PHE   A CB   1 
ATOM   2311 C CG   . PHE   A 1 116 ? 24.248 -10.654 4.529   1.00 8.77  ?  116 PHE   A CG   1 
ATOM   2312 C CD1  . PHE   A 1 116 ? 24.816 -9.623  3.789   1.00 8.96  ?  116 PHE   A CD1  1 
ATOM   2313 C CD2  . PHE   A 1 116 ? 22.893 -10.559 4.850   1.00 9.68  ?  116 PHE   A CD2  1 
ATOM   2314 C CE1  . PHE   A 1 116 ? 24.045 -8.537  3.386   1.00 9.32  ?  116 PHE   A CE1  1 
ATOM   2315 C CE2  . PHE   A 1 116 ? 22.123 -9.483  4.454   1.00 9.62  ?  116 PHE   A CE2  1 
ATOM   2316 C CZ   . PHE   A 1 116 ? 22.690 -8.466  3.723   1.00 9.15  ?  116 PHE   A CZ   1 
ATOM   2317 H H    . PHE   A 1 116 ? 26.645 -11.711 3.124   1.00 10.39 ?  116 PHE   A H    1 
ATOM   2318 H HA   . PHE   A 1 116 ? 26.734 -10.991 5.630   1.00 10.66 ?  116 PHE   A HA   1 
ATOM   2319 H HB2  . PHE   A 1 116 ? 24.817 -12.605 4.327   1.00 10.84 ?  116 PHE   A HB2  1 
ATOM   2320 H HB3  . PHE   A 1 116 ? 24.654 -12.167 5.839   1.00 10.84 ?  116 PHE   A HB3  1 
ATOM   2321 H HD1  . PHE   A 1 116 ? 25.712 -9.675  3.550   1.00 10.76 ?  116 PHE   A HD1  1 
ATOM   2322 H HD2  . PHE   A 1 116 ? 22.496 -11.251 5.335   1.00 11.63 ?  116 PHE   A HD2  1 
ATOM   2323 H HE1  . PHE   A 1 116 ? 24.437 -7.854  2.892   1.00 11.19 ?  116 PHE   A HE1  1 
ATOM   2324 H HE2  . PHE   A 1 116 ? 21.226 -9.450  4.687   1.00 11.56 ?  116 PHE   A HE2  1 
ATOM   2325 H HZ   . PHE   A 1 116 ? 22.183 -7.736  3.462   1.00 10.99 ?  116 PHE   A HZ   1 
ATOM   2326 N N    . ASN   A 1 117 ? 27.456 -14.066 5.161   1.00 8.98  ?  117 ASN   A N    1 
ATOM   2327 C CA   . ASN   A 1 117 ? 27.834 -15.317 5.821   1.00 9.22  ?  117 ASN   A CA   1 
ATOM   2328 C C    . ASN   A 1 117 ? 29.101 -15.192 6.649   1.00 9.84  ?  117 ASN   A C    1 
ATOM   2329 O O    . ASN   A 1 117 ? 29.411 -16.110 7.418   1.00 10.52 ?  117 ASN   A O    1 
ATOM   2330 C CB   . ASN   A 1 117 ? 27.939 -16.438 4.790   1.00 9.48  ?  117 ASN   A CB   1 
ATOM   2331 C CG   . ASN   A 1 117 ? 26.577 -16.818 4.262   1.00 9.47  ?  117 ASN   A CG   1 
ATOM   2332 O OD1  . ASN   A 1 117 ? 25.611 -16.862 5.028   1.00 10.38 ?  117 ASN   A OD1  1 
ATOM   2333 N ND2  . ASN   A 1 117 ? 26.476 -17.070 2.969   1.00 9.54  ?  117 ASN   A ND2  1 
ATOM   2334 H H    . ASN   A 1 117 ? 27.524 -14.081 4.303   1.00 10.79 ?  117 ASN   A H    1 
ATOM   2335 H HA   . ASN   A 1 117 ? 27.122 -15.556 6.429   1.00 11.07 ?  117 ASN   A HA   1 
ATOM   2336 H HB2  . ASN   A 1 117 ? 28.488 -16.143 4.045   1.00 11.38 ?  117 ASN   A HB2  1 
ATOM   2337 H HB3  . ASN   A 1 117 ? 28.333 -17.220 5.208   1.00 11.38 ?  117 ASN   A HB3  1 
ATOM   2338 H HD21 . ASN   A 1 117 ? 25.717 -17.286 2.627   1.00 11.46 ?  117 ASN   A HD21 1 
ATOM   2339 H HD22 . ASN   A 1 117 ? 27.173 -17.020 2.462   1.00 11.46 ?  117 ASN   A HD22 1 
ATOM   2340 N N    . GLN   A 1 118 ? 29.826 -14.079 6.524   1.00 9.87  ?  118 GLN   A N    1 
ATOM   2341 C CA   . GLN   A 1 118 ? 31.010 -13.836 7.338   1.00 10.31 ?  118 GLN   A CA   1 
ATOM   2342 C C    . GLN   A 1 118 ? 30.677 -13.261 8.708   1.00 10.17 ?  118 GLN   A C    1 
ATOM   2343 O O    . GLN   A 1 118 ? 31.596 -12.965 9.479   1.00 11.88 ?  118 GLN   A O    1 
ATOM   2344 C CB   . GLN   A 1 118 ? 31.987 -12.923 6.592   1.00 10.71 ?  118 GLN   A CB   1 
ATOM   2345 C CG   . GLN   A 1 118 ? 32.470 -13.510 5.264   1.00 10.71 ?  118 GLN   A CG   1 
ATOM   2346 C CD   . GLN   A 1 118 ? 33.287 -14.780 5.439   1.00 10.75 ?  118 GLN   A CD   1 
ATOM   2347 O OE1  . GLN   A 1 118 ? 34.145 -14.858 6.327   1.00 11.60 ?  118 GLN   A OE1  1 
ATOM   2348 N NE2  . GLN   A 1 118 ? 33.026 -15.779 4.594   1.00 11.09 ?  118 GLN   A NE2  1 
ATOM   2349 H H    . GLN   A 1 118 ? 29.643 -13.437 5.975   1.00 11.85 ?  118 GLN   A H    1 
ATOM   2350 H HA   . GLN   A 1 118 ? 31.453 -14.684 7.481   1.00 12.38 ?  118 GLN   A HA   1 
ATOM   2351 H HB2  . GLN   A 1 118 ? 31.551 -12.079 6.405   1.00 12.86 ?  118 GLN   A HB2  1 
ATOM   2352 H HB3  . GLN   A 1 118 ? 32.766 -12.776 7.152   1.00 12.86 ?  118 GLN   A HB3  1 
ATOM   2353 H HG2  . GLN   A 1 118 ? 31.701 -13.715 4.709   1.00 12.87 ?  118 GLN   A HG2  1 
ATOM   2354 H HG3  . GLN   A 1 118 ? 33.032 -12.854 4.815   1.00 12.87 ?  118 GLN   A HG3  1 
ATOM   2355 H HE21 . GLN   A 1 118 ? 32.418 -15.687 3.985   1.00 13.32 ?  118 GLN   A HE21 1 
ATOM   2356 H HE22 . GLN   A 1 118 ? 33.459 -16.520 4.650   1.00 13.32 ?  118 GLN   A HE22 1 
ATOM   2357 N N    . HIS   A 1 119 ? 29.392 -13.120 9.036   1.00 9.88  ?  119 HIS   A N    1 
ATOM   2358 C CA   . HIS   A 1 119 ? 28.943 -12.508 10.283  1.00 10.47 ?  119 HIS   A CA   1 
ATOM   2359 C C    . HIS   A 1 119 ? 27.811 -13.339 10.861  1.00 10.56 ?  119 HIS   A C    1 
ATOM   2360 O O    . HIS   A 1 119 ? 26.861 -13.668 10.149  1.00 11.05 ?  119 HIS   A O    1 
ATOM   2361 C CB   . HIS   A 1 119 ? 28.475 -11.075 10.013  1.00 10.95 ?  119 HIS   A CB   1 
ATOM   2362 C CG   . HIS   A 1 119 ? 29.546 -10.261 9.388   1.00 12.32 ?  119 HIS   A CG   1 
ATOM   2363 N ND1  . HIS   A 1 119 ? 30.532 -9.658  10.133  1.00 14.58 ?  119 HIS   A ND1  1 
ATOM   2364 C CD2  . HIS   A 1 119 ? 29.870 -10.065 8.090   1.00 13.71 ?  119 HIS   A CD2  1 
ATOM   2365 C CE1  . HIS   A 1 119 ? 31.389 -9.073  9.315   1.00 15.19 ?  119 HIS   A CE1  1 
ATOM   2366 N NE2  . HIS   A 1 119 ? 31.021 -9.318  8.071   1.00 15.46 ?  119 HIS   A NE2  1 
ATOM   2367 H H    . HIS   A 1 119 ? 28.741 -13.384 8.538   1.00 11.87 ?  119 HIS   A H    1 
ATOM   2368 H HA   . HIS   A 1 119 ? 29.675 -12.487 10.921  1.00 12.57 ?  119 HIS   A HA   1 
ATOM   2369 H HB2  . HIS   A 1 119 ? 27.714 -11.099 9.413   1.00 13.15 ?  119 HIS   A HB2  1 
ATOM   2370 H HB3  . HIS   A 1 119 ? 28.228 -10.661 10.855  1.00 13.15 ?  119 HIS   A HB3  1 
ATOM   2371 H HD2  . HIS   A 1 119 ? 29.399 -10.380 7.347   1.00 16.46 ?  119 HIS   A HD2  1 
ATOM   2372 H HE1  . HIS   A 1 119 ? 32.129 -8.570  9.565   1.00 18.24 ?  119 HIS   A HE1  1 
ATOM   2373 H HE2  . HIS   A 1 119 ? 31.412 -9.024  7.360   1.00 18.56 ?  119 HIS   A HE2  1 
ATOM   2374 N N    . GLU   A 1 120 ? 27.906 -13.662 12.151  1.00 11.08 ?  120 GLU   A N    1 
ATOM   2375 C CA   . GLU   A 1 120 ? 26.954 -14.601 12.741  1.00 12.57 ?  120 GLU   A CA   1 
ATOM   2376 C C    . GLU   A 1 120 ? 25.539 -14.032 12.826  1.00 11.13 ?  120 GLU   A C    1 
ATOM   2377 O O    . GLU   A 1 120 ? 24.563 -14.793 12.715  1.00 11.58 ?  120 GLU   A O    1 
ATOM   2378 C CB   . GLU   A 1 120 ? 27.442 -15.046 14.121  1.00 17.03 ?  120 GLU   A CB   1 
ATOM   2379 C CG   . GLU   A 1 120 ? 28.628 -15.993 14.076  1.00 24.43 ?  120 GLU   A CG   1 
ATOM   2380 C CD   . GLU   A 1 120 ? 28.843 -16.709 15.394  1.00 31.59 ?  120 GLU   A CD   1 
ATOM   2381 O OE1  . GLU   A 1 120 ? 28.484 -16.140 16.447  1.00 33.85 ?  120 GLU   A OE1  1 
ATOM   2382 O OE2  . GLU   A 1 120 ? 29.360 -17.846 15.376  1.00 36.05 -1 120 GLU   A OE2  1 
ATOM   2383 H H    . GLU   A 1 120 ? 28.505 -13.362 12.696  1.00 13.30 ?  120 GLU   A H    1 
ATOM   2384 H HA   . GLU   A 1 120 ? 26.920 -15.390 12.185  1.00 15.09 ?  120 GLU   A HA   1 
ATOM   2385 H HB2  . GLU   A 1 120 ? 27.713 -14.266 14.631  1.00 20.45 ?  120 GLU   A HB2  1 
ATOM   2386 H HB3  . GLU   A 1 120 ? 26.721 -15.504 14.579  1.00 20.45 ?  120 GLU   A HB3  1 
ATOM   2387 H HG2  . GLU   A 1 120 ? 28.477 -16.666 13.394  1.00 29.33 ?  120 GLU   A HG2  1 
ATOM   2388 H HG3  . GLU   A 1 120 ? 29.435 -15.492 13.876  1.00 29.33 ?  120 GLU   A HG3  1 
ATOM   2389 N N    . VAL   A 1 121 ? 25.411 -12.723 13.059  1.00 10.72 ?  121 VAL   A N    1 
ATOM   2390 C CA   . VAL   A 1 121 ? 24.123 -12.054 13.208  1.00 11.09 ?  121 VAL   A CA   1 
ATOM   2391 C C    . VAL   A 1 121 ? 24.230 -10.670 12.574  1.00 10.19 ?  121 VAL   A C    1 
ATOM   2392 O O    . VAL   A 1 121 ? 25.203 -9.947  12.810  1.00 11.10 ?  121 VAL   A O    1 
ATOM   2393 C CB   . VAL   A 1 121 ? 23.717 -11.913 14.693  1.00 13.73 ?  121 VAL   A CB   1 
ATOM   2394 C CG1  . VAL   A 1 121 ? 22.352 -11.241 14.815  1.00 14.58 ?  121 VAL   A CG1  1 
ATOM   2395 C CG2  . VAL   A 1 121 ? 23.712 -13.249 15.406  1.00 16.21 ?  121 VAL   A CG2  1 
ATOM   2396 H H    . VAL   A 1 121 ? 26.082 -12.189 13.147  1.00 12.87 ?  121 VAL   A H    1 
ATOM   2397 H HA   . VAL   A 1 121 ? 23.440 -12.561 12.745  1.00 13.31 ?  121 VAL   A HA   1 
ATOM   2398 H HB   . VAL   A 1 121 ? 24.361 -11.344 15.139  1.00 16.48 ?  121 VAL   A HB   1 
ATOM   2399 H HG11 . VAL   A 1 121 ? 22.046 -11.314 15.734  1.00 17.51 ?  121 VAL   A HG11 1 
ATOM   2400 H HG12 . VAL   A 1 121 ? 22.434 -10.305 14.571  1.00 17.51 ?  121 VAL   A HG12 1 
ATOM   2401 H HG13 . VAL   A 1 121 ? 21.725 -11.685 14.224  1.00 17.51 ?  121 VAL   A HG13 1 
ATOM   2402 H HG21 . VAL   A 1 121 ? 23.386 -13.124 16.316  1.00 19.46 ?  121 VAL   A HG21 1 
ATOM   2403 H HG22 . VAL   A 1 121 ? 23.121 -13.861 14.934  1.00 19.46 ?  121 VAL   A HG22 1 
ATOM   2404 H HG23 . VAL   A 1 121 ? 24.610 -13.606 15.426  1.00 19.46 ?  121 VAL   A HG23 1 
ATOM   2405 N N    . LEU   A 1 122 ? 23.211 -10.279 11.800  1.00 9.99  ?  122 LEU   A N    1 
ATOM   2406 C CA   . LEU   A 1 122 ? 23.205 -8.979  11.128  1.00 10.01 ?  122 LEU   A CA   1 
ATOM   2407 C C    . LEU   A 1 122 ? 21.806 -8.388  11.110  1.00 9.61  ?  122 LEU   A C    1 
ATOM   2408 O O    . LEU   A 1 122 ? 20.819 -9.112  10.978  1.00 10.82 ?  122 LEU   A O    1 
ATOM   2409 C CB   . LEU   A 1 122 ? 23.606 -9.070  9.644   1.00 11.58 ?  122 LEU   A CB   1 
ATOM   2410 C CG   . LEU   A 1 122 ? 24.811 -9.919  9.260   1.00 11.25 ?  122 LEU   A CG   1 
ATOM   2411 C CD1  . LEU   A 1 122 ? 24.422 -11.370 9.038   1.00 12.21 ?  122 LEU   A CD1  1 
ATOM   2412 C CD2  . LEU   A 1 122 ? 25.464 -9.341  8.017   1.00 10.86 ?  122 LEU   A CD2  1 
ATOM   2413 H H    . LEU   A 1 122 ? 22.509 -10.751 11.641  1.00 12.00 ?  122 LEU   A H    1 
ATOM   2414 H HA   . LEU   A 1 122 ? 23.806 -8.364  11.578  1.00 12.02 ?  122 LEU   A HA   1 
ATOM   2415 H HB2  . LEU   A 1 122 ? 22.857 -9.424  9.152   1.00 13.90 ?  122 LEU   A HB2  1 
ATOM   2416 H HB3  . LEU   A 1 122 ? 23.795 -8.169  9.332   1.00 13.90 ?  122 LEU   A HB3  1 
ATOM   2417 H HG   . LEU   A 1 122 ? 25.473 -9.887  9.972   1.00 13.51 ?  122 LEU   A HG   1 
ATOM   2418 H HD11 . LEU   A 1 122 ? 25.203 -11.870 8.752   1.00 14.66 ?  122 LEU   A HD11 1 
ATOM   2419 H HD12 . LEU   A 1 122 ? 24.085 -11.733 9.872   1.00 14.66 ?  122 LEU   A HD12 1 
ATOM   2420 H HD13 . LEU   A 1 122 ? 23.735 -11.410 8.356   1.00 14.66 ?  122 LEU   A HD13 1 
ATOM   2421 H HD21 . LEU   A 1 122 ? 26.204 -9.911  7.746   1.00 13.04 ?  122 LEU   A HD21 1 
ATOM   2422 H HD22 . LEU   A 1 122 ? 24.806 -9.298  7.304   1.00 13.04 ?  122 LEU   A HD22 1 
ATOM   2423 H HD23 . LEU   A 1 122 ? 25.795 -8.448  8.212   1.00 13.04 ?  122 LEU   A HD23 1 
ATOM   2424 N N    . LEU   A 1 123 ? 21.746 -7.055  11.197  1.00 9.37  ?  123 LEU   A N    1 
ATOM   2425 C CA   . LEU   A 1 123 ? 20.570 -6.258  10.848  1.00 9.30  ?  123 LEU   A CA   1 
ATOM   2426 C C    . LEU   A 1 123 ? 20.802 -5.713  9.445   1.00 8.94  ?  123 LEU   A C    1 
ATOM   2427 O O    . LEU   A 1 123 ? 21.850 -5.116  9.194   1.00 9.53  ?  123 LEU   A O    1 
ATOM   2428 C CB   . LEU   A 1 123 ? 20.452 -5.092  11.830  1.00 9.79  ?  123 LEU   A CB   1 
ATOM   2429 C CG   . LEU   A 1 123 ? 19.400 -4.028  11.510  1.00 10.62 ?  123 LEU   A CG   1 
ATOM   2430 C CD1  . LEU   A 1 123 ? 17.997 -4.618  11.515  1.00 11.50 ?  123 LEU   A CD1  1 
ATOM   2431 C CD2  . LEU   A 1 123 ? 19.496 -2.865  12.493  1.00 11.11 ?  123 LEU   A CD2  1 
ATOM   2432 H H    . LEU   A 1 123 ? 22.404 -6.569  11.467  1.00 11.25 ?  123 LEU   A H    1 
ATOM   2433 H HA   . LEU   A 1 123 ? 19.759 -6.798  10.868  1.00 11.17 ?  123 LEU   A HA   1 
ATOM   2434 H HB2  . LEU   A 1 123 ? 20.231 -5.452  12.705  1.00 11.76 ?  123 LEU   A HB2  1 
ATOM   2435 H HB3  . LEU   A 1 123 ? 21.305 -4.642  11.873  1.00 11.76 ?  123 LEU   A HB3  1 
ATOM   2436 H HG   . LEU   A 1 123 ? 19.561 -3.672  10.622  1.00 12.76 ?  123 LEU   A HG   1 
ATOM   2437 H HD11 . LEU   A 1 123 ? 17.352 -3.915  11.350  1.00 13.81 ?  123 LEU   A HD11 1 
ATOM   2438 H HD12 . LEU   A 1 123 ? 17.935 -5.294  10.818  1.00 13.81 ?  123 LEU   A HD12 1 
ATOM   2439 H HD13 . LEU   A 1 123 ? 17.829 -5.026  12.381  1.00 13.81 ?  123 LEU   A HD13 1 
ATOM   2440 H HD21 . LEU   A 1 123 ? 18.820 -2.208  12.271  1.00 13.34 ?  123 LEU   A HD21 1 
ATOM   2441 H HD22 . LEU   A 1 123 ? 19.346 -3.205  13.391  1.00 13.34 ?  123 LEU   A HD22 1 
ATOM   2442 H HD23 . LEU   A 1 123 ? 20.378 -2.475  12.428  1.00 13.34 ?  123 LEU   A HD23 1 
ATOM   2443 N N    A ALA   A 1 124 ? 19.832 -5.885  8.546   0.86 8.79  ?  124 ALA   A N    1 
ATOM   2444 N N    B ALA   A 1 124 ? 19.859 -5.931  8.529   0.14 9.15  ?  124 ALA   A N    1 
ATOM   2445 C CA   A ALA   A 1 124 ? 20.097 -5.584  7.146   0.86 8.97  ?  124 ALA   A CA   1 
ATOM   2446 C CA   B ALA   A 1 124 ? 20.143 -5.644  7.128   0.14 9.51  ?  124 ALA   A CA   1 
ATOM   2447 C C    A ALA   A 1 124 ? 18.844 -5.108  6.425   0.86 8.81  ?  124 ALA   A C    1 
ATOM   2448 C C    B ALA   A 1 124 ? 18.879 -5.238  6.388   0.14 9.57  ?  124 ALA   A C    1 
ATOM   2449 O O    A ALA   A 1 124 ? 17.718 -5.481  6.790   0.86 9.43  ?  124 ALA   A O    1 
ATOM   2450 O O    B ALA   A 1 124 ? 17.775 -5.627  6.784   0.14 9.49  ?  124 ALA   A O    1 
ATOM   2451 C CB   A ALA   A 1 124 ? 20.649 -6.807  6.409   0.86 9.16  ?  124 ALA   A CB   1 
ATOM   2452 C CB   B ALA   A 1 124 ? 20.758 -6.866  6.430   0.14 9.74  ?  124 ALA   A CB   1 
ATOM   2453 H H    A ALA   A 1 124 ? 19.039 -6.175  8.712   0.86 10.55 ?  124 ALA   A H    1 
ATOM   2454 H H    B ALA   A 1 124 ? 19.066 -6.226  8.685   0.14 10.99 ?  124 ALA   A H    1 
ATOM   2455 H HA   A ALA   A 1 124 ? 20.770 -4.886  7.110   0.86 10.77 ?  124 ALA   A HA   1 
ATOM   2456 H HA   B ALA   A 1 124 ? 20.785 -4.917  7.079   0.14 11.43 ?  124 ALA   A HA   1 
ATOM   2457 H HB1  A ALA   A 1 124 ? 20.822 -6.573  5.481   0.86 11.00 ?  124 ALA   A HB1  1 
ATOM   2458 H HB1  B ALA   A 1 124 ? 20.939 -6.644  5.502   0.14 11.70 ?  124 ALA   A HB1  1 
ATOM   2459 H HB2  A ALA   A 1 124 ? 21.486 -7.085  6.830   0.86 11.00 ?  124 ALA   A HB2  1 
ATOM   2460 H HB2  B ALA   A 1 124 ? 21.585 -7.107  6.878   0.14 11.70 ?  124 ALA   A HB2  1 
ATOM   2461 H HB3  A ALA   A 1 124 ? 20.007 -7.528  6.454   0.86 11.00 ?  124 ALA   A HB3  1 
ATOM   2462 H HB3  B ALA   A 1 124 ? 20.130 -7.604  6.476   0.14 11.70 ?  124 ALA   A HB3  1 
ATOM   2463 N N    A PRO   A 1 125 ? 19.021 -4.340  5.349   0.86 8.92  ?  125 PRO   A N    1 
ATOM   2464 N N    B PRO   A 1 125 ? 19.010 -4.455  5.307   0.14 9.72  ?  125 PRO   A N    1 
ATOM   2465 C CA   A PRO   A 1 125 ? 17.962 -4.097  4.375   0.86 9.28  ?  125 PRO   A CA   1 
ATOM   2466 C CA   B PRO   A 1 125 ? 17.880 -4.247  4.395   0.14 9.90  ?  125 PRO   A CA   1 
ATOM   2467 C C    A PRO   A 1 125 ? 18.023 -5.171  3.293   0.86 9.22  ?  125 PRO   A C    1 
ATOM   2468 C C    B PRO   A 1 125 ? 17.928 -5.223  3.229   0.14 9.88  ?  125 PRO   A C    1 
ATOM   2469 O O    A PRO   A 1 125 ? 18.999 -5.912  3.173   0.86 9.79  ?  125 PRO   A O    1 
ATOM   2470 O O    B PRO   A 1 125 ? 18.870 -6.013  3.117   0.14 10.01 ?  125 PRO   A O    1 
ATOM   2471 C CB   A PRO   A 1 125 ? 18.393 -2.750  3.787   0.86 9.46  ?  125 PRO   A CB   1 
ATOM   2472 C CB   B PRO   A 1 125 ? 18.094 -2.806  3.920   0.14 9.90  ?  125 PRO   A CB   1 
ATOM   2473 C CG   A PRO   A 1 125 ? 19.909 -2.898  3.694   0.86 9.38  ?  125 PRO   A CG   1 
ATOM   2474 C CG   B PRO   A 1 125 ? 19.588 -2.677  3.878   0.14 10.04 ?  125 PRO   A CG   1 
ATOM   2475 C CD   A PRO   A 1 125 ? 20.296 -3.724  4.919   0.86 9.18  ?  125 PRO   A CD   1 
ATOM   2476 C CD   B PRO   A 1 125 ? 20.129 -3.545  5.000   0.14 9.89  ?  125 PRO   A CD   1 
ATOM   2477 H HA   A PRO   A 1 125 ? 17.083 -4.048  4.786   0.86 11.14 ?  125 PRO   A HA   1 
ATOM   2478 H HA   B PRO   A 1 125 ? 17.031 -4.322  4.857   0.14 11.89 ?  125 PRO   A HA   1 
ATOM   2479 H HB2  A PRO   A 1 125 ? 17.994 -2.626  2.911   0.86 11.36 ?  125 PRO   A HB2  1 
ATOM   2480 H HB2  B PRO   A 1 125 ? 17.708 -2.681  3.038   0.14 11.88 ?  125 PRO   A HB2  1 
ATOM   2481 H HB3  A PRO   A 1 125 ? 18.144 -2.030  4.390   0.86 11.36 ?  125 PRO   A HB3  1 
ATOM   2482 H HB3  B PRO   A 1 125 ? 17.711 -2.183  4.559   0.14 11.88 ?  125 PRO   A HB3  1 
ATOM   2483 H HG2  A PRO   A 1 125 ? 20.140 -3.366  2.876   0.86 11.27 ?  125 PRO   A HG2  1 
ATOM   2484 H HG2  B PRO   A 1 125 ? 19.914 -2.992  3.020   0.14 12.06 ?  125 PRO   A HG2  1 
ATOM   2485 H HG3  A PRO   A 1 125 ? 20.324 -2.024  3.721   0.86 11.27 ?  125 PRO   A HG3  1 
ATOM   2486 H HG3  B PRO   A 1 125 ? 19.838 -1.751  4.016   0.14 12.06 ?  125 PRO   A HG3  1 
ATOM   2487 H HD2  A PRO   A 1 125 ? 20.945 -4.405  4.674   0.86 11.02 ?  125 PRO   A HD2  1 
ATOM   2488 H HD2  B PRO   A 1 125 ? 20.901 -4.049  4.697   0.14 11.88 ?  125 PRO   A HD2  1 
ATOM   2489 H HD3  A PRO   A 1 125 ? 20.644 -3.144  5.618   0.86 11.02 ?  125 PRO   A HD3  1 
ATOM   2490 H HD3  B PRO   A 1 125 ? 20.343 -3.001  5.775   0.14 11.88 ?  125 PRO   A HD3  1 
ATOM   2491 N N    A LEU   A 1 126 ? 16.968 -5.223  2.485   0.86 9.44  ?  126 LEU   A N    1 
ATOM   2492 N N    B LEU   A 1 126 ? 16.927 -5.176  2.353   0.14 9.92  ?  126 LEU   A N    1 
ATOM   2493 C CA   A LEU   A 1 126 ? 16.992 -6.052  1.286   0.86 9.79  ?  126 LEU   A CA   1 
ATOM   2494 C CA   B LEU   A 1 126 ? 16.909 -6.018  1.160   0.14 9.73  ?  126 LEU   A CA   1 
ATOM   2495 C C    A LEU   A 1 126 ? 17.928 -5.446  0.244   0.86 9.55  ?  126 LEU   A C    1 
ATOM   2496 C C    B LEU   A 1 126 ? 17.789 -5.376  0.094   0.14 9.03  ?  126 LEU   A C    1 
ATOM   2497 O O    A LEU   A 1 126 ? 17.728 -4.315  -0.215  0.86 10.22 ?  126 LEU   A O    1 
ATOM   2498 O O    B LEU   A 1 126 ? 17.421 -4.355  -0.498  0.14 9.17  ?  126 LEU   A O    1 
ATOM   2499 C CB   A LEU   A 1 126 ? 15.589 -6.202  0.710   0.86 10.67 ?  126 LEU   A CB   1 
ATOM   2500 C CB   B LEU   A 1 126 ? 15.478 -6.198  0.661   0.14 10.15 ?  126 LEU   A CB   1 
ATOM   2501 C CG   A LEU   A 1 126 ? 14.676 -7.138  1.492   0.86 12.02 ?  126 LEU   A CG   1 
ATOM   2502 C CG   B LEU   A 1 126 ? 14.616 -7.182  1.454   0.14 10.62 ?  126 LEU   A CG   1 
ATOM   2503 C CD1  A LEU   A 1 126 ? 13.242 -6.972  1.018   0.86 13.31 ?  126 LEU   A CD1  1 
ATOM   2504 C CD1  B LEU   A 1 126 ? 13.216 -7.248  0.868   0.14 11.00 ?  126 LEU   A CD1  1 
ATOM   2505 C CD2  A LEU   A 1 126 ? 15.129 -8.597  1.346   0.86 11.99 ?  126 LEU   A CD2  1 
ATOM   2506 C CD2  B LEU   A 1 126 ? 15.250 -8.566  1.473   0.14 10.59 ?  126 LEU   A CD2  1 
ATOM   2507 H H    A LEU   A 1 126 ? 16.232 -4.787  2.604   0.86 11.34 ?  126 LEU   A H    1 
ATOM   2508 H H    B LEU   A 1 126 ? 16.242 -4.663  2.429   0.14 11.92 ?  126 LEU   A H    1 
ATOM   2509 H HA   A LEU   A 1 126 ? 17.322 -6.929  1.515   0.86 11.76 ?  126 LEU   A HA   1 
ATOM   2510 H HA   B LEU   A 1 126 ? 17.278 -6.887  1.374   0.14 11.68 ?  126 LEU   A HA   1 
ATOM   2511 H HB2  A LEU   A 1 126 ? 15.163 -5.330  0.692   0.86 12.81 ?  126 LEU   A HB2  1 
ATOM   2512 H HB2  B LEU   A 1 126 ? 15.033 -5.336  0.692   0.14 12.19 ?  126 LEU   A HB2  1 
ATOM   2513 H HB3  A LEU   A 1 126 ? 15.658 -6.549  -0.192  0.86 12.81 ?  126 LEU   A HB3  1 
ATOM   2514 H HB3  B LEU   A 1 126 ? 15.509 -6.514  -0.254  0.14 12.19 ?  126 LEU   A HB3  1 
ATOM   2515 H HG   A LEU   A 1 126 ? 14.708 -6.906  2.432   0.86 14.44 ?  126 LEU   A HG   1 
ATOM   2516 H HG   B LEU   A 1 126 ? 14.541 -6.873  2.370   0.14 12.75 ?  126 LEU   A HG   1 
ATOM   2517 H HD11 A LEU   A 1 126 ? 12.674 -7.580  1.515   0.86 15.98 ?  126 LEU   A HD11 1 
ATOM   2518 H HD11 B LEU   A 1 126 ? 12.686 -7.870  1.390   0.14 13.21 ?  126 LEU   A HD11 1 
ATOM   2519 H HD12 A LEU   A 1 126 ? 12.966 -6.056  1.170   0.86 15.98 ?  126 LEU   A HD12 1 
ATOM   2520 H HD12 B LEU   A 1 126 ? 12.819 -6.364  0.902   0.14 13.21 ?  126 LEU   A HD12 1 
ATOM   2521 H HD13 A LEU   A 1 126 ? 13.200 -7.179  0.070   0.86 15.98 ?  126 LEU   A HD13 1 
ATOM   2522 H HD13 B LEU   A 1 126 ? 13.274 -7.551  -0.051  0.14 13.21 ?  126 LEU   A HD13 1 
ATOM   2523 H HD21 A LEU   A 1 126 ? 14.465 -9.179  1.740   0.86 14.39 ?  126 LEU   A HD21 1 
ATOM   2524 H HD21 B LEU   A 1 126 ? 14.586 -9.214  1.751   0.14 12.71 ?  126 LEU   A HD21 1 
ATOM   2525 H HD22 A LEU   A 1 126 ? 15.235 -8.802  0.402   0.86 14.39 ?  126 LEU   A HD22 1 
ATOM   2526 H HD22 B LEU   A 1 126 ? 15.568 -8.778  0.581   0.14 12.71 ?  126 LEU   A HD22 1 
ATOM   2527 H HD23 A LEU   A 1 126 ? 15.981 -8.709  1.802   0.86 14.39 ?  126 LEU   A HD23 1 
ATOM   2528 H HD23 B LEU   A 1 126 ? 15.994 -8.564  2.097   0.14 12.71 ?  126 LEU   A HD23 1 
ATOM   2529 N N    A LEU   A 1 127 ? 18.946 -6.207  -0.141  0.86 9.95  ?  127 LEU   A N    1 
ATOM   2530 N N    B LEU   A 1 127 ? 18.946 -5.982  -0.157  0.14 8.47  ?  127 LEU   A N    1 
ATOM   2531 C CA   A LEU   A 1 127 ? 19.928 -5.716  -1.093  0.86 9.51  ?  127 LEU   A CA   1 
ATOM   2532 C CA   B LEU   A 1 127 ? 19.923 -5.396  -1.063  0.14 8.24  ?  127 LEU   A CA   1 
ATOM   2533 C C    A LEU   A 1 127 ? 19.295 -5.495  -2.458  0.86 8.92  ?  127 LEU   A C    1 
ATOM   2534 C C    B LEU   A 1 127 ? 19.380 -5.327  -2.487  0.14 8.21  ?  127 LEU   A C    1 
ATOM   2535 O O    A LEU   A 1 127 ? 18.447 -6.267  -2.915  0.86 9.65  ?  127 LEU   A O    1 
ATOM   2536 O O    B LEU   A 1 127 ? 18.607 -6.181  -2.930  0.14 8.06  ?  127 LEU   A O    1 
ATOM   2537 C CB   A LEU   A 1 127 ? 21.098 -6.694  -1.209  0.86 9.67  ?  127 LEU   A CB   1 
ATOM   2538 C CB   B LEU   A 1 127 ? 21.213 -6.217  -1.033  0.14 8.53  ?  127 LEU   A CB   1 
ATOM   2539 C CG   A LEU   A 1 127 ? 21.915 -6.935  0.060   0.86 9.99  ?  127 LEU   A CG   1 
ATOM   2540 C CG   B LEU   A 1 127 ? 21.911 -6.299  0.327   0.14 8.86  ?  127 LEU   A CG   1 
ATOM   2541 C CD1  A LEU   A 1 127 ? 23.031 -7.913  -0.226  0.86 10.36 ?  127 LEU   A CD1  1 
ATOM   2542 C CD1  B LEU   A 1 127 ? 23.115 -7.220  0.244   0.14 9.04  ?  127 LEU   A CD1  1 
ATOM   2543 C CD2  A LEU   A 1 127 ? 22.487 -5.643  0.597   0.86 10.81 ?  127 LEU   A CD2  1 
ATOM   2544 C CD2  B LEU   A 1 127 ? 22.320 -4.913  0.815   0.14 9.10  ?  127 LEU   A CD2  1 
ATOM   2545 H H    A LEU   A 1 127 ? 19.087 -7.011  0.139   0.86 11.95 ?  127 LEU   A H    1 
ATOM   2546 H H    B LEU   A 1 127 ? 19.192 -6.731  0.189   0.14 10.17 ?  127 LEU   A H    1 
ATOM   2547 H HA   A LEU   A 1 127 ? 20.271 -4.870  -0.781  0.86 11.42 ?  127 LEU   A HA   1 
ATOM   2548 H HA   B LEU   A 1 127 ? 20.128 -4.495  -0.773  0.14 9.90  ?  127 LEU   A HA   1 
ATOM   2549 H HB2  A LEU   A 1 127 ? 20.750 -7.555  -1.492  0.86 11.61 ?  127 LEU   A HB2  1 
ATOM   2550 H HB2  B LEU   A 1 127 ? 21.009 -7.125  -1.307  0.14 10.25 ?  127 LEU   A HB2  1 
ATOM   2551 H HB3  A LEU   A 1 127 ? 21.708 -6.358  -1.881  0.86 11.61 ?  127 LEU   A HB3  1 
ATOM   2552 H HB3  B LEU   A 1 127 ? 21.843 -5.824  -1.656  0.14 10.25 ?  127 LEU   A HB3  1 
ATOM   2553 H HG   A LEU   A 1 127 ? 21.340 -7.320  0.743   0.86 12.00 ?  127 LEU   A HG   1 
ATOM   2554 H HG   B LEU   A 1 127 ? 21.296 -6.675  0.977   0.14 10.64 ?  127 LEU   A HG   1 
ATOM   2555 H HD11 A LEU   A 1 127 ? 23.531 -8.072  0.594   0.86 12.44 ?  127 LEU   A HD11 1 
ATOM   2556 H HD11 B LEU   A 1 127 ? 23.651 -7.109  1.044   0.14 10.85 ?  127 LEU   A HD11 1 
ATOM   2557 H HD12 A LEU   A 1 127 ? 22.653 -8.747  -0.545  0.86 12.44 ?  127 LEU   A HD12 1 
ATOM   2558 H HD12 B LEU   A 1 127 ? 22.806 -8.137  0.176   0.14 10.85 ?  127 LEU   A HD12 1 
ATOM   2559 H HD13 A LEU   A 1 127 ? 23.618 -7.536  -0.899  0.86 12.44 ?  127 LEU   A HD13 1 
ATOM   2560 H HD13 B LEU   A 1 127 ? 23.636 -6.985  -0.538  0.14 10.85 ?  127 LEU   A HD13 1 
ATOM   2561 H HD21 A LEU   A 1 127 ? 23.106 -5.844  1.315   0.86 12.98 ?  127 LEU   A HD21 1 
ATOM   2562 H HD21 B LEU   A 1 127 ? 22.862 -5.007  1.615   0.14 10.93 ?  127 LEU   A HD21 1 
ATOM   2563 H HD22 A LEU   A 1 127 ? 22.956 -5.185  -0.122  0.86 12.98 ?  127 LEU   A HD22 1 
ATOM   2564 H HD22 B LEU   A 1 127 ? 22.830 -4.473  0.119   0.14 10.93 ?  127 LEU   A HD22 1 
ATOM   2565 H HD23 A LEU   A 1 127 ? 21.766 -5.085  0.925   0.86 12.98 ?  127 LEU   A HD23 1 
ATOM   2566 H HD23 B LEU   A 1 127 ? 21.521 -4.402  1.016   0.14 10.93 ?  127 LEU   A HD23 1 
ATOM   2567 N N    A SER   A 1 128 ? 19.736 -4.429  -3.112  0.86 9.10  ?  128 SER   A N    1 
ATOM   2568 N N    B SER   A 1 128 ? 19.795 -4.277  -3.197  0.14 8.34  ?  128 SER   A N    1 
ATOM   2569 C CA   A SER   A 1 128 ? 19.306 -4.010  -4.440  0.86 9.43  ?  128 SER   A CA   1 
ATOM   2570 C CA   B SER   A 1 128 ? 19.465 -4.047  -4.602  0.14 8.36  ?  128 SER   A CA   1 
ATOM   2571 C C    A SER   A 1 128 ? 17.853 -3.552  -4.502  0.86 9.69  ?  128 SER   A C    1 
ATOM   2572 C C    B SER   A 1 128 ? 18.029 -3.576  -4.806  0.14 8.22  ?  128 SER   A C    1 
ATOM   2573 O O    A SER   A 1 128 ? 17.368 -3.243  -5.589  0.86 10.98 ?  128 SER   A O    1 
ATOM   2574 O O    B SER   A 1 128 ? 17.651 -3.213  -5.925  0.14 8.22  ?  128 SER   A O    1 
ATOM   2575 C CB   A SER   A 1 128 ? 19.630 -5.037  -5.534  0.86 9.61  ?  128 SER   A CB   1 
ATOM   2576 C CB   B SER   A 1 128 ? 19.785 -5.262  -5.482  0.14 8.37  ?  128 SER   A CB   1 
ATOM   2577 O OG   A SER   A 1 128 ? 21.037 -5.249  -5.609  0.86 10.36 ?  128 SER   A OG   1 
ATOM   2578 O OG   B SER   A 1 128 ? 21.178 -5.327  -5.743  0.14 8.63  ?  128 SER   A OG   1 
ATOM   2579 H H    A SER   A 1 128 ? 20.339 -3.903  -2.786  0.86 10.93 ?  128 SER   A H    1 
ATOM   2580 H H    B SER   A 1 128 ? 20.283 -3.653  -2.864  0.14 10.02 ?  128 SER   A H    1 
ATOM   2581 H HA   A SER   A 1 128 ? 19.835 -3.232  -4.661  0.86 11.32 ?  128 SER   A HA   1 
ATOM   2582 H HA   B SER   A 1 128 ? 20.034 -3.333  -4.912  0.14 10.04 ?  128 SER   A HA   1 
ATOM   2583 H HB2  A SER   A 1 128 ? 19.192 -5.876  -5.330  0.86 11.54 ?  128 SER   A HB2  1 
ATOM   2584 H HB2  B SER   A 1 128 ? 19.505 -6.078  -5.046  0.14 10.05 ?  128 SER   A HB2  1 
ATOM   2585 H HB3  A SER   A 1 128 ? 19.309 -4.698  -6.391  0.86 11.54 ?  128 SER   A HB3  1 
ATOM   2586 H HB3  B SER   A 1 128 ? 19.317 -5.164  -6.328  0.14 10.05 ?  128 SER   A HB3  1 
ATOM   2587 H HG   A SER   A 1 128 ? 21.428 -4.531  -5.804  0.86 12.45 ?  128 SER   A HG   1 
ATOM   2588 H HG   B SER   A 1 128 ? 21.427 -4.620  -6.126  0.14 10.36 ?  128 SER   A HG   1 
ATOM   2589 N N    A ALA   A 1 129 ? 17.163 -3.455  -3.364  0.86 10.12 ?  129 ALA   A N    1 
ATOM   2590 N N    B ALA   A 1 129 ? 17.233 -3.556  -3.740  0.14 8.74  ?  129 ALA   A N    1 
ATOM   2591 C CA   A ALA   A 1 129 ? 15.798 -2.947  -3.338  0.86 10.38 ?  129 ALA   A CA   1 
ATOM   2592 C CA   B ALA   A 1 129 ? 15.880 -3.024  -3.812  0.14 9.10  ?  129 ALA   A CA   1 
ATOM   2593 C C    A ALA   A 1 129 ? 15.809 -1.417  -3.356  0.86 9.90  ?  129 ALA   A C    1 
ATOM   2594 C C    B ALA   A 1 129 ? 15.922 -1.504  -3.634  0.14 9.38  ?  129 ALA   A C    1 
ATOM   2595 O O    A ALA   A 1 129 ? 16.852 -0.767  -3.495  0.86 10.03 ?  129 ALA   A O    1 
ATOM   2596 O O    B ALA   A 1 129 ? 16.990 -0.889  -3.570  0.14 9.55  ?  129 ALA   A O    1 
ATOM   2597 C CB   A ALA   A 1 129 ? 15.034 -3.518  -2.144  0.86 11.62 ?  129 ALA   A CB   1 
ATOM   2598 C CB   B ALA   A 1 129 ? 14.982 -3.728  -2.798  0.14 9.06  ?  129 ALA   A CB   1 
ATOM   2599 H H    A ALA   A 1 129 ? 17.473 -3.678  -2.587  0.86 12.16 ?  129 ALA   A H    1 
ATOM   2600 H H    B ALA   A 1 129 ? 17.454 -3.846  -2.960  0.14 10.50 ?  129 ALA   A H    1 
ATOM   2601 H HA   A ALA   A 1 129 ? 15.349 -3.252  -4.140  0.86 12.46 ?  129 ALA   A HA   1 
ATOM   2602 H HA   B ALA   A 1 129 ? 15.525 -3.211  -4.692  0.14 10.93 ?  129 ALA   A HA   1 
ATOM   2603 H HB1  A ALA   A 1 129 ? 14.124 -3.177  -2.161  0.86 13.96 ?  129 ALA   A HB1  1 
ATOM   2604 H HB1  B ALA   A 1 129 ? 14.097 -3.333  -2.832  0.14 10.89 ?  129 ALA   A HB1  1 
ATOM   2605 H HB2  A ALA   A 1 129 ? 15.022 -4.487  -2.207  0.86 13.96 ?  129 ALA   A HB2  1 
ATOM   2606 H HB2  B ALA   A 1 129 ? 14.933 -4.670  -3.023  0.14 10.89 ?  129 ALA   A HB2  1 
ATOM   2607 H HB3  A ALA   A 1 129 ? 15.474 -3.245  -1.325  0.86 13.96 ?  129 ALA   A HB3  1 
ATOM   2608 H HB3  B ALA   A 1 129 ? 15.359 -3.619  -1.912  0.14 10.89 ?  129 ALA   A HB3  1 
ATOM   2609 N N    A GLY   A 1 130 ? 14.626 -0.824  -3.229  0.86 11.01 ?  130 GLY   A N    1 
ATOM   2610 N N    B GLY   A 1 130 ? 14.751 -0.878  -3.563  0.14 9.69  ?  130 GLY   A N    1 
ATOM   2611 C CA   A GLY   A 1 130 ? 14.538 0.625   -3.216  0.86 11.81 ?  130 GLY   A CA   1 
ATOM   2612 C CA   B GLY   A 1 130 ? 14.707 0.566   -3.392  0.14 9.92  ?  130 GLY   A CA   1 
ATOM   2613 C C    A GLY   A 1 130 ? 15.134 1.227   -4.470  0.86 11.17 ?  130 GLY   A C    1 
ATOM   2614 C C    B GLY   A 1 130 ? 15.222 1.268   -4.633  0.14 10.07 ?  130 GLY   A C    1 
ATOM   2615 O O    A GLY   A 1 130 ? 14.891 0.758   -5.587  0.86 11.47 ?  130 GLY   A O    1 
ATOM   2616 O O    B GLY   A 1 130 ? 14.847 0.932   -5.762  0.14 10.15 ?  130 GLY   A O    1 
ATOM   2617 H H    A GLY   A 1 130 ? 13.874 -1.236  -3.150  0.86 13.23 ?  130 GLY   A H    1 
ATOM   2618 H H    B GLY   A 1 130 ? 13.982 -1.258  -3.614  0.14 11.64 ?  130 GLY   A H    1 
ATOM   2619 H HA2  A GLY   A 1 130 ? 13.605 0.889   -3.150  0.86 14.18 ?  130 GLY   A HA2  1 
ATOM   2620 H HA2  B GLY   A 1 130 ? 13.793 0.849   -3.216  0.14 11.92 ?  130 GLY   A HA2  1 
ATOM   2621 H HA3  A GLY   A 1 130 ? 15.014 0.971   -2.450  0.86 14.18 ?  130 GLY   A HA3  1 
ATOM   2622 H HA3  B GLY   A 1 130 ? 15.261 0.825   -2.641  0.14 11.92 ?  130 GLY   A HA3  1 
ATOM   2623 N N    A ILE   A 1 131 ? 15.933 2.284   -4.284  0.86 10.83 ?  131 ILE   A N    1 
ATOM   2624 N N    B ILE   A 1 131 ? 16.104 2.252   -4.431  0.14 10.21 ?  131 ILE   A N    1 
ATOM   2625 C CA   A ILE   A 1 131 ? 16.490 3.030   -5.409  0.86 10.79 ?  131 ILE   A CA   1 
ATOM   2626 C CA   B ILE   A 1 131 ? 16.639 3.027   -5.547  0.14 10.36 ?  131 ILE   A CA   1 
ATOM   2627 C C    A ILE   A 1 131 ? 17.502 2.241   -6.229  0.86 10.44 ?  131 ILE   A C    1 
ATOM   2628 C C    B ILE   A 1 131 ? 17.591 2.230   -6.424  0.14 10.27 ?  131 ILE   A C    1 
ATOM   2629 O O    A ILE   A 1 131 ? 17.924 2.727   -7.285  0.86 11.51 ?  131 ILE   A O    1 
ATOM   2630 O O    B ILE   A 1 131 ? 17.960 2.705   -7.504  0.14 10.54 ?  131 ILE   A O    1 
ATOM   2631 C CB   A ILE   A 1 131 ? 17.056 4.405   -4.986  0.86 11.68 ?  131 ILE   A CB   1 
ATOM   2632 C CB   B ILE   A 1 131 ? 17.314 4.335   -5.080  0.14 10.75 ?  131 ILE   A CB   1 
ATOM   2633 C CG1  A ILE   A 1 131 ? 18.328 4.257   -4.140  0.86 12.84 ?  131 ILE   A CG1  1 
ATOM   2634 C CG1  B ILE   A 1 131 ? 18.504 4.040   -4.160  0.14 10.99 ?  131 ILE   A CG1  1 
ATOM   2635 C CG2  A ILE   A 1 131 ? 15.989 5.219   -4.255  0.86 12.55 ?  131 ILE   A CG2  1 
ATOM   2636 C CG2  B ILE   A 1 131 ? 16.303 5.239   -4.390  0.14 10.86 ?  131 ILE   A CG2  1 
ATOM   2637 C CD1  A ILE   A 1 131 ? 18.983 5.587   -3.773  0.86 14.53 ?  131 ILE   A CD1  1 
ATOM   2638 C CD1  B ILE   A 1 131 ? 19.198 5.284   -3.639  0.14 11.24 ?  131 ILE   A CD1  1 
ATOM   2639 H H    A ILE   A 1 131 ? 16.151 2.590   -3.511  0.86 13.01 ?  131 ILE   A H    1 
ATOM   2640 H H    B ILE   A 1 131 ? 16.404 2.483   -3.661  0.14 12.26 ?  131 ILE   A H    1 
ATOM   2641 H HA   A ILE   A 1 131 ? 15.761 3.224   -6.008  0.86 12.96 ?  131 ILE   A HA   1 
ATOM   2642 H HA   B ILE   A 1 131 ? 15.899 3.284   -6.110  0.14 12.44 ?  131 ILE   A HA   1 
ATOM   2643 H HB   A ILE   A 1 131 ? 17.295 4.887   -5.791  0.86 14.03 ?  131 ILE   A HB   1 
ATOM   2644 H HB   B ILE   A 1 131 ? 17.647 4.800   -5.863  0.14 12.91 ?  131 ILE   A HB   1 
ATOM   2645 H HG12 A ILE   A 1 131 ? 18.107 3.800   -3.314  0.86 15.42 ?  131 ILE   A HG12 1 
ATOM   2646 H HG12 B ILE   A 1 131 ? 18.194 3.533   -3.396  0.14 13.19 ?  131 ILE   A HG12 1 
ATOM   2647 H HG13 A ILE   A 1 131 ? 18.983 3.741   -4.636  0.86 15.42 ?  131 ILE   A HG13 1 
ATOM   2648 H HG13 B ILE   A 1 131 ? 19.160 3.525   -4.653  0.14 13.19 ?  131 ILE   A HG13 1 
ATOM   2649 H HG21 A ILE   A 1 131 ? 16.308 6.130   -4.137  0.86 15.07 ?  131 ILE   A HG21 1 
ATOM   2650 H HG21 B ILE   A 1 131 ? 16.690 6.123   -4.280  0.14 13.04 ?  131 ILE   A HG21 1 
ATOM   2651 H HG22 A ILE   A 1 131 ? 15.178 5.222   -4.787  0.86 15.07 ?  131 ILE   A HG22 1 
ATOM   2652 H HG22 B ILE   A 1 131 ? 15.506 5.296   -4.939  0.14 13.04 ?  131 ILE   A HG22 1 
ATOM   2653 H HG23 A ILE   A 1 131 ? 15.816 4.815   -3.391  0.86 15.07 ?  131 ILE   A HG23 1 
ATOM   2654 H HG23 B ILE   A 1 131 ? 16.082 4.863   -3.524  0.14 13.04 ?  131 ILE   A HG23 1 
ATOM   2655 H HD11 A ILE   A 1 131 ? 19.834 5.413   -3.336  0.86 17.45 ?  131 ILE   A HD11 1 
ATOM   2656 H HD11 B ILE   A 1 131 ? 20.021 5.025   -3.196  0.14 13.50 ?  131 ILE   A HD11 1 
ATOM   2657 H HD12 A ILE   A 1 131 ? 19.128 6.104   -4.580  0.86 17.45 ?  131 ILE   A HD12 1 
ATOM   2658 H HD12 B ILE   A 1 131 ? 19.395 5.873   -4.385  0.14 13.50 ?  131 ILE   A HD12 1 
ATOM   2659 H HD13 A ILE   A 1 131 ? 18.399 6.074   -3.169  0.86 17.45 ?  131 ILE   A HD13 1 
ATOM   2660 H HD13 B ILE   A 1 131 ? 18.613 5.736   -3.009  0.14 13.50 ?  131 ILE   A HD13 1 
ATOM   2661 N N    A PHE   A 1 132 ? 17.906 1.039   -5.787  0.86 9.98  ?  132 PHE   A N    1 
ATOM   2662 N N    B PHE   A 1 132 ? 17.999 1.033   -5.997  0.14 10.06 ?  132 PHE   A N    1 
ATOM   2663 C CA   A PHE   A 1 132 ? 18.747 0.179   -6.617  0.86 10.20 ?  132 PHE   A CA   1 
ATOM   2664 C CA   B PHE   A 1 132 ? 18.874 0.210   -6.822  0.14 10.12 ?  132 PHE   A CA   1 
ATOM   2665 C C    A PHE   A 1 132 ? 17.950 -0.581  -7.679  0.86 10.72 ?  132 PHE   A C    1 
ATOM   2666 C C    B PHE   A 1 132 ? 18.120 -0.549  -7.910  0.14 10.56 ?  132 PHE   A C    1 
ATOM   2667 O O    A PHE   A 1 132 ? 18.554 -1.234  -8.535  0.86 11.59 ?  132 PHE   A O    1 
ATOM   2668 O O    B PHE   A 1 132 ? 18.757 -1.064  -8.836  0.14 10.82 ?  132 PHE   A O    1 
ATOM   2669 C CB   A PHE   A 1 132 ? 19.562 -0.801  -5.760  0.86 10.11 ?  132 PHE   A CB   1 
ATOM   2670 C CB   B PHE   A 1 132 ? 19.703 -0.741  -5.952  0.14 9.85  ?  132 PHE   A CB   1 
ATOM   2671 C CG   A PHE   A 1 132 ? 20.798 -0.196  -5.106  0.86 9.90  ?  132 PHE   A CG   1 
ATOM   2672 C CG   B PHE   A 1 132 ? 20.904 -0.088  -5.312  0.14 10.03 ?  132 PHE   A CG   1 
ATOM   2673 C CD1  A PHE   A 1 132 ? 20.693 0.831   -4.181  0.86 10.98 ?  132 PHE   A CD1  1 
ATOM   2674 C CD1  B PHE   A 1 132 ? 20.753 0.990   -4.454  0.14 10.29 ?  132 PHE   A CD1  1 
ATOM   2675 C CD2  A PHE   A 1 132 ? 22.059 -0.704  -5.379  0.86 10.86 ?  132 PHE   A CD2  1 
ATOM   2676 C CD2  B PHE   A 1 132 ? 22.183 -0.559  -5.565  0.14 10.45 ?  132 PHE   A CD2  1 
ATOM   2677 C CE1  A PHE   A 1 132 ? 21.826 1.359   -3.569  0.86 10.90 ?  132 PHE   A CE1  1 
ATOM   2678 C CE1  B PHE   A 1 132 ? 21.854 1.589   -3.865  0.14 10.59 ?  132 PHE   A CE1  1 
ATOM   2679 C CE2  A PHE   A 1 132 ? 23.191 -0.184  -4.768  0.86 11.11 ?  132 PHE   A CE2  1 
ATOM   2680 C CE2  B PHE   A 1 132 ? 23.287 0.035   -4.978  0.14 10.74 ?  132 PHE   A CE2  1 
ATOM   2681 C CZ   A PHE   A 1 132 ? 23.072 0.850   -3.864  0.86 11.06 ?  132 PHE   A CZ   1 
ATOM   2682 C CZ   B PHE   A 1 132 ? 23.121 1.109   -4.127  0.14 10.72 ?  132 PHE   A CZ   1 
ATOM   2683 H H    A PHE   A 1 132 ? 17.704 0.704   -5.014  0.86 11.99 ?  132 PHE   A H    1 
ATOM   2684 H H    B PHE   A 1 132 ? 17.782 0.680   -5.240  0.14 12.08 ?  132 PHE   A H    1 
ATOM   2685 H HA   A PHE   A 1 132 ? 19.380 0.744   -7.078  0.86 12.25 ?  132 PHE   A HA   1 
ATOM   2686 H HA   B PHE   A 1 132 ? 19.499 0.800   -7.265  0.14 12.15 ?  132 PHE   A HA   1 
ATOM   2687 H HB2  A PHE   A 1 132 ? 18.991 -1.139  -5.049  0.86 12.14 ?  132 PHE   A HB2  1 
ATOM   2688 H HB2  B PHE   A 1 132 ? 19.143 -1.085  -5.241  0.14 11.83 ?  132 PHE   A HB2  1 
ATOM   2689 H HB3  A PHE   A 1 132 ? 19.851 -1.539  -6.321  0.86 12.14 ?  132 PHE   A HB3  1 
ATOM   2690 H HB3  B PHE   A 1 132 ? 20.024 -1.471  -6.504  0.14 11.83 ?  132 PHE   A HB3  1 
ATOM   2691 H HD1  A PHE   A 1 132 ? 19.856 1.177   -3.974  0.86 13.19 ?  132 PHE   A HD1  1 
ATOM   2692 H HD1  B PHE   A 1 132 ? 19.902 1.319   -4.274  0.14 12.36 ?  132 PHE   A HD1  1 
ATOM   2693 H HD2  A PHE   A 1 132 ? 22.150 -1.405  -5.993  0.86 13.04 ?  132 PHE   A HD2  1 
ATOM   2694 H HD2  B PHE   A 1 132 ? 22.301 -1.283  -6.137  0.14 12.54 ?  132 PHE   A HD2  1 
ATOM   2695 H HE1  A PHE   A 1 132 ? 21.740 2.056   -2.960  0.86 13.09 ?  132 PHE   A HE1  1 
ATOM   2696 H HE1  B PHE   A 1 132 ? 21.740 2.313   -3.292  0.14 12.71 ?  132 PHE   A HE1  1 
ATOM   2697 H HE2  A PHE   A 1 132 ? 24.030 -0.527  -4.979  0.86 13.34 ?  132 PHE   A HE2  1 
ATOM   2698 H HE2  B PHE   A 1 132 ? 24.139 -0.290  -5.156  0.14 12.89 ?  132 PHE   A HE2  1 
ATOM   2699 H HZ   A PHE   A 1 132 ? 23.829 1.207   -3.461  0.86 13.28 ?  132 PHE   A HZ   1 
ATOM   2700 H HZ   B PHE   A 1 132 ? 23.862 1.509   -3.732  0.14 12.87 ?  132 PHE   A HZ   1 
ATOM   2701 N N    A GLY   A 1 133 ? 16.618 -0.535  -7.642  0.86 10.89 ?  133 GLY   A N    1 
ATOM   2702 N N    B GLY   A 1 133 ? 16.792 -0.636  -7.823  0.14 10.44 ?  133 GLY   A N    1 
ATOM   2703 C CA   A GLY   A 1 133 ? 15.809 -0.904  -8.788  0.86 11.81 ?  133 GLY   A CA   1 
ATOM   2704 C CA   B GLY   A 1 133 ? 15.961 -1.012  -8.946  0.14 10.42 ?  133 GLY   A CA   1 
ATOM   2705 C C    A GLY   A 1 133 ? 15.473 -2.369  -8.976  0.86 12.12 ?  133 GLY   A C    1 
ATOM   2706 C C    B GLY   A 1 133 ? 15.426 -2.432  -8.942  0.14 10.33 ?  133 GLY   A C    1 
ATOM   2707 O O    A GLY   A 1 133 ? 14.811 -2.699  -9.972  0.86 13.70 ?  133 GLY   A O    1 
ATOM   2708 O O    B GLY   A 1 133 ? 14.503 -2.722  -9.714  0.14 10.75 ?  133 GLY   A O    1 
ATOM   2709 H H    A GLY   A 1 133 ? 16.159 -0.297  -6.956  0.86 13.08 ?  133 GLY   A H    1 
ATOM   2710 H H    B GLY   A 1 133 ? 16.346 -0.477  -7.107  0.14 12.54 ?  133 GLY   A H    1 
ATOM   2711 H HA2  A GLY   A 1 133 ? 14.965 -0.434  -8.735  0.86 14.19 ?  133 GLY   A HA2  1 
ATOM   2712 H HA2  B GLY   A 1 133 ? 15.192 -0.433  -8.956  0.14 12.51 ?  133 GLY   A HA2  1 
ATOM   2713 H HA3  A GLY   A 1 133 ? 16.261 -0.611  -9.595  0.86 14.19 ?  133 GLY   A HA3  1 
ATOM   2714 H HA3  B GLY   A 1 133 ? 16.447 -0.845  -9.767  0.14 12.51 ?  133 GLY   A HA3  1 
ATOM   2715 N N    A ALA   A 1 134 ? 15.902 -3.261  -8.086  0.86 11.57 ?  134 ALA   A N    1 
ATOM   2716 N N    B ALA   A 1 134 ? 15.955 -3.320  -8.103  0.14 10.02 ?  134 ALA   A N    1 
ATOM   2717 C CA   A ALA   A 1 134 ? 15.559 -4.666  -8.242  0.86 12.47 ?  134 ALA   A CA   1 
ATOM   2718 C CA   B ALA   A 1 134 ? 15.521 -4.708  -8.143  0.14 9.88  ?  134 ALA   A CA   1 
ATOM   2719 C C    A ALA   A 1 134 ? 14.192 -4.953  -7.621  0.86 12.60 ?  134 ALA   A C    1 
ATOM   2720 C C    B ALA   A 1 134 ? 14.207 -4.893  -7.387  0.14 9.57  ?  134 ALA   A C    1 
ATOM   2721 O O    A ALA   A 1 134 ? 13.638 -4.155  -6.861  0.86 13.59 ?  134 ALA   A O    1 
ATOM   2722 O O    B ALA   A 1 134 ? 13.837 -4.101  -6.516  0.14 9.39  ?  134 ALA   A O    1 
ATOM   2723 C CB   A ALA   A 1 134 ? 16.634 -5.567  -7.633  0.86 13.80 ?  134 ALA   A CB   1 
ATOM   2724 C CB   B ALA   A 1 134 ? 16.588 -5.631  -7.555  0.14 10.20 ?  134 ALA   A CB   1 
ATOM   2725 H H    A ALA   A 1 134 ? 16.403 -3.081  -7.397  0.86 13.89 ?  134 ALA   A H    1 
ATOM   2726 H H    B ALA   A 1 134 ? 16.556 -3.147  -7.512  0.14 12.03 ?  134 ALA   A H    1 
ATOM   2727 H HA   A ALA   A 1 134 ? 15.513 -4.871  -9.189  0.86 14.97 ?  134 ALA   A HA   1 
ATOM   2728 H HA   B ALA   A 1 134 ? 15.375 -4.968  -9.065  0.14 11.87 ?  134 ALA   A HA   1 
ATOM   2729 H HB1  A ALA   A 1 134 ? 16.384 -6.493  -7.772  0.86 16.57 ?  134 ALA   A HB1  1 
ATOM   2730 H HB1  B ALA   A 1 134 ? 16.278 -6.549  -7.616  0.14 12.25 ?  134 ALA   A HB1  1 
ATOM   2731 H HB2  A ALA   A 1 134 ? 17.487 -5.388  -8.068  0.86 16.57 ?  134 ALA   A HB2  1 
ATOM   2732 H HB2  B ALA   A 1 134 ? 17.407 -5.525  -8.062  0.14 12.25 ?  134 ALA   A HB2  1 
ATOM   2733 H HB3  A ALA   A 1 134 ? 16.706 -5.380  -6.685  0.86 16.57 ?  134 ALA   A HB3  1 
ATOM   2734 H HB3  B ALA   A 1 134 ? 16.737 -5.392  -6.628  0.14 12.25 ?  134 ALA   A HB3  1 
ATOM   2735 N N    A ASP   A 1 135 ? 13.647 -6.112  -7.969  0.86 13.61 ?  135 ASP   A N    1 
ATOM   2736 N N    B ASP   A 1 135 ? 13.505 -5.964  -7.738  0.14 9.79  ?  135 ASP   A N    1 
ATOM   2737 C CA   A ASP   A 1 135 ? 12.390 -6.584  -7.392  0.86 14.61 ?  135 ASP   A CA   1 
ATOM   2738 C CA   B ASP   A 1 135 ? 12.254 -6.315  -7.080  0.14 9.83  ?  135 ASP   A CA   1 
ATOM   2739 C C    A ASP   A 1 135 ? 12.646 -7.046  -5.962  0.86 14.00 ?  135 ASP   A C    1 
ATOM   2740 C C    B ASP   A 1 135 ? 12.548 -6.811  -5.669  0.14 9.57  ?  135 ASP   A C    1 
ATOM   2741 O O    A ASP   A 1 135 ? 13.418 -7.993  -5.759  0.86 13.81 ?  135 ASP   A O    1 
ATOM   2742 O O    B ASP   A 1 135 ? 13.281 -7.797  -5.511  0.14 9.50  ?  135 ASP   A O    1 
ATOM   2743 C CB   A ASP   A 1 135 ? 11.885 -7.753  -8.240  0.86 16.98 ?  135 ASP   A CB   1 
ATOM   2744 C CB   B ASP   A 1 135 ? 11.569 -7.419  -7.878  0.14 9.83  ?  135 ASP   A CB   1 
ATOM   2745 C CG   A ASP   A 1 135 ? 10.600 -8.386  -7.702  0.86 19.52 ?  135 ASP   A CG   1 
ATOM   2746 C CG   B ASP   A 1 135 ? 10.154 -7.691  -7.407  0.14 10.02 ?  135 ASP   A CG   1 
ATOM   2747 O OD1  A ASP   A 1 135 ? 10.083 -7.945  -6.656  0.86 20.02 ?  135 ASP   A OD1  1 
ATOM   2748 O OD1  B ASP   A 1 135 ? 9.817  -7.303  -6.266  0.14 10.14 ?  135 ASP   A OD1  1 
ATOM   2749 O OD2  A ASP   A 1 135 ? 10.103 -9.337  -8.346  0.86 22.06 -1 135 ASP   A OD2  1 
ATOM   2750 O OD2  B ASP   A 1 135 ? 9.381  -8.300  -8.177  0.14 10.16 -1 135 ASP   A OD2  1 
ATOM   2751 H H    A ASP   A 1 135 ? 13.985 -6.645  -8.548  0.86 16.34 ?  135 ASP   A H    1 
ATOM   2752 H H    B ASP   A 1 135 ? 13.727 -6.506  -8.364  0.14 11.76 ?  135 ASP   A H    1 
ATOM   2753 H HA   A ASP   A 1 135 ? 11.731 -5.865  -7.409  0.86 17.54 ?  135 ASP   A HA   1 
ATOM   2754 H HA   B ASP   A 1 135 ? 11.664 -5.542  -7.056  0.14 11.81 ?  135 ASP   A HA   1 
ATOM   2755 H HB2  A ASP   A 1 135 ? 11.707 -7.430  -9.134  0.86 20.38 ?  135 ASP   A HB2  1 
ATOM   2756 H HB2  B ASP   A 1 135 ? 11.541 -7.163  -8.814  0.14 11.80 ?  135 ASP   A HB2  1 
ATOM   2757 H HB3  A ASP   A 1 135 ? 12.573 -8.433  -8.258  0.86 20.38 ?  135 ASP   A HB3  1 
ATOM   2758 H HB3  B ASP   A 1 135 ? 12.074 -8.241  -7.776  0.14 11.80 ?  135 ASP   A HB3  1 
ATOM   2759 N N    A PRO   A 1 136 ? 12.048 -6.412  -4.949  0.86 14.17 ?  136 PRO   A N    1 
ATOM   2760 N N    B PRO   A 1 136 ? 12.013 -6.173  -4.624  0.14 9.51  ?  136 PRO   A N    1 
ATOM   2761 C CA   A PRO   A 1 136 ? 12.317 -6.832  -3.562  0.86 14.11 ?  136 PRO   A CA   1 
ATOM   2762 C CA   B PRO   A 1 136 ? 12.285 -6.655  -3.259  0.14 9.73  ?  136 PRO   A CA   1 
ATOM   2763 C C    A PRO   A 1 136 ? 11.883 -8.256  -3.253  0.86 13.15 ?  136 PRO   A C    1 
ATOM   2764 C C    B PRO   A 1 136 ? 11.870 -8.099  -3.016  0.14 9.91  ?  136 PRO   A C    1 
ATOM   2765 O O    A PRO   A 1 136 ? 12.477 -8.903  -2.381  0.86 12.69 ?  136 PRO   A O    1 
ATOM   2766 O O    B PRO   A 1 136 ? 12.469 -8.769  -2.165  0.14 9.43  ?  136 PRO   A O    1 
ATOM   2767 C CB   A PRO   A 1 136 ? 11.547 -5.797  -2.726  0.86 15.30 ?  136 PRO   A CB   1 
ATOM   2768 C CB   B PRO   A 1 136 ? 11.506 -5.668  -2.373  0.14 9.87  ?  136 PRO   A CB   1 
ATOM   2769 C CG   A PRO   A 1 136 ? 10.485 -5.278  -3.648  0.86 16.71 ?  136 PRO   A CG   1 
ATOM   2770 C CG   B PRO   A 1 136 ? 10.526 -5.001  -3.295  0.14 10.13 ?  136 PRO   A CG   1 
ATOM   2771 C CD   A PRO   A 1 136 ? 11.095 -5.290  -5.016  0.86 15.40 ?  136 PRO   A CD   1 
ATOM   2772 C CD   B PRO   A 1 136 ? 11.201 -4.946  -4.622  0.14 9.62  ?  136 PRO   A CD   1 
ATOM   2773 H HA   A PRO   A 1 136 ? 13.265 -6.740  -3.366  0.86 16.94 ?  136 PRO   A HA   1 
ATOM   2774 H HA   B PRO   A 1 136 ? 13.229 -6.566  -3.063  0.14 11.69 ?  136 PRO   A HA   1 
ATOM   2775 H HB2  A PRO   A 1 136 ? 11.150 -6.227  -1.953  0.86 18.37 ?  136 PRO   A HB2  1 
ATOM   2776 H HB2  B PRO   A 1 136 ? 11.041 -6.149  -1.672  0.14 11.86 ?  136 PRO   A HB2  1 
ATOM   2777 H HB3  A PRO   A 1 136 ? 12.145 -5.082  -2.452  0.86 18.37 ?  136 PRO   A HB3  1 
ATOM   2778 H HB3  B PRO   A 1 136 ? 12.116 -5.014  -1.995  0.14 11.86 ?  136 PRO   A HB3  1 
ATOM   2779 H HG2  A PRO   A 1 136 ? 9.712  -5.859  -3.615  0.86 20.06 ?  136 PRO   A HG2  1 
ATOM   2780 H HG2  B PRO   A 1 136 ? 9.716  -5.532  -3.353  0.14 12.16 ?  136 PRO   A HG2  1 
ATOM   2781 H HG3  A PRO   A 1 136 ? 10.245 -4.372  -3.393  0.86 20.06 ?  136 PRO   A HG3  1 
ATOM   2782 H HG3  B PRO   A 1 136 ? 10.329 -4.107  -2.979  0.14 12.16 ?  136 PRO   A HG3  1 
ATOM   2783 H HD2  A PRO   A 1 136 ? 10.410 -5.467  -5.686  0.86 18.49 ?  136 PRO   A HD2  1 
ATOM   2784 H HD2  B PRO   A 1 136 ? 10.540 -4.966  -5.335  0.14 11.56 ?  136 PRO   A HD2  1 
ATOM   2785 H HD3  A PRO   A 1 136 ? 11.554 -4.454  -5.195  0.86 18.49 ?  136 PRO   A HD3  1 
ATOM   2786 H HD3  B PRO   A 1 136 ? 11.771 -4.162  -4.688  0.14 11.56 ?  136 PRO   A HD3  1 
ATOM   2787 N N    A ILE   A 1 137 ? 10.846 -8.764  -3.923  0.86 13.57 ?  137 ILE   A N    1 
ATOM   2788 N N    B ILE   A 1 137 ? 10.859 -8.599  -3.729  0.14 10.85 ?  137 ILE   A N    1 
ATOM   2789 C CA   A ILE   A 1 137 ? 10.461 -10.161 -3.730  0.86 14.22 ?  137 ILE   A CA   1 
ATOM   2790 C CA   B ILE   A 1 137 ? 10.451 -9.992  -3.563  0.14 11.61 ?  137 ILE   A CA   1 
ATOM   2791 C C    A ILE   A 1 137 ? 11.605 -11.076 -4.147  0.86 13.33 ?  137 ILE   A C    1 
ATOM   2792 C C    B ILE   A 1 137 ? 11.558 -10.931 -4.028  0.14 11.76 ?  137 ILE   A C    1 
ATOM   2793 O O    A ILE   A 1 137 ? 11.919 -12.064 -3.469  0.86 13.46 ?  137 ILE   A O    1 
ATOM   2794 O O    B ILE   A 1 137 ? 11.852 -11.940 -3.374  0.14 11.82 ?  137 ILE   A O    1 
ATOM   2795 C CB   A ILE   A 1 137 ? 9.160  -10.473 -4.497  0.86 15.69 ?  137 ILE   A CB   1 
ATOM   2796 C CB   B ILE   A 1 137 ? 9.122  -10.247 -4.299  0.14 12.17 ?  137 ILE   A CB   1 
ATOM   2797 C CG1  A ILE   A 1 137 ? 7.989  -9.646  -3.949  0.86 17.80 ?  137 ILE   A CG1  1 
ATOM   2798 C CG1  B ILE   A 1 137 ? 7.981  -9.484  -3.619  0.14 12.59 ?  137 ILE   A CG1  1 
ATOM   2799 C CG2  A ILE   A 1 137 ? 8.850  -11.964 -4.424  0.86 16.22 ?  137 ILE   A CG2  1 
ATOM   2800 C CG2  B ILE   A 1 137 ? 8.812  -11.739 -4.355  0.14 12.48 ?  137 ILE   A CG2  1 
ATOM   2801 C CD1  A ILE   A 1 137 ? 6.708  -9.807  -4.733  0.86 19.24 ?  137 ILE   A CD1  1 
ATOM   2802 C CD1  B ILE   A 1 137 ? 6.837  -9.147  -4.545  0.14 12.75 ?  137 ILE   A CD1  1 
ATOM   2803 H H    A ILE   A 1 137 ? 10.363 -8.324  -4.479  0.86 16.29 ?  137 ILE   A H    1 
ATOM   2804 H H    B ILE   A 1 137 ? 10.399 -8.156  -4.304  0.14 13.03 ?  137 ILE   A H    1 
ATOM   2805 H HA   A ILE   A 1 137 ? 10.294 -10.309 -2.787  0.86 17.08 ?  137 ILE   A HA   1 
ATOM   2806 H HA   B ILE   A 1 137 ? 10.298 -10.160 -2.621  0.14 13.94 ?  137 ILE   A HA   1 
ATOM   2807 H HB   A ILE   A 1 137 ? 9.292  -10.230 -5.426  0.86 18.84 ?  137 ILE   A HB   1 
ATOM   2808 H HB   B ILE   A 1 137 ? 9.206  -9.921  -5.206  0.14 14.61 ?  137 ILE   A HB   1 
ATOM   2809 H HG12 A ILE   A 1 137 ? 7.819  -9.915  -3.033  0.86 21.37 ?  137 ILE   A HG12 1 
ATOM   2810 H HG12 B ILE   A 1 137 ? 7.625  -10.026 -2.897  0.14 15.12 ?  137 ILE   A HG12 1 
ATOM   2811 H HG13 A ILE   A 1 137 ? 8.235  -8.704  -3.971  0.86 21.37 ?  137 ILE   A HG13 1 
ATOM   2812 H HG13 B ILE   A 1 137 ? 8.326  -8.650  -3.262  0.14 15.12 ?  137 ILE   A HG13 1 
ATOM   2813 H HG21 A ILE   A 1 137 ? 7.943  -12.123 -4.723  0.86 19.47 ?  137 ILE   A HG21 1 
ATOM   2814 H HG21 B ILE   A 1 137 ? 7.874  -11.859 -4.574  0.14 14.99 ?  137 ILE   A HG21 1 
ATOM   2815 H HG22 A ILE   A 1 137 ? 9.470  -12.438 -4.994  0.86 19.47 ?  137 ILE   A HG22 1 
ATOM   2816 H HG22 B ILE   A 1 137 ? 9.364  -12.152 -5.039  0.14 14.99 ?  137 ILE   A HG22 1 
ATOM   2817 H HG23 A ILE   A 1 137 ? 8.948  -12.254 -3.506  0.86 19.47 ?  137 ILE   A HG23 1 
ATOM   2818 H HG23 B ILE   A 1 137 ? 9.001  -12.135 -3.491  0.14 14.99 ?  137 ILE   A HG23 1 
ATOM   2819 H HD11 A ILE   A 1 137 ? 6.007  -10.109 -4.135  0.86 23.09 ?  137 ILE   A HD11 1 
ATOM   2820 H HD11 B ILE   A 1 137 ? 6.333  -8.416  -4.158  0.14 15.31 ?  137 ILE   A HD11 1 
ATOM   2821 H HD12 A ILE   A 1 137 ? 6.478  -8.951  -5.118  0.86 23.09 ?  137 ILE   A HD12 1 
ATOM   2822 H HD12 B ILE   A 1 137 ? 7.194  -8.881  -5.408  0.14 15.31 ?  137 ILE   A HD12 1 
ATOM   2823 H HD13 A ILE   A 1 137 ? 6.843  -10.454 -5.443  0.86 23.09 ?  137 ILE   A HD13 1 
ATOM   2824 H HD13 B ILE   A 1 137 ? 6.270  -9.928  -4.650  0.14 15.31 ?  137 ILE   A HD13 1 
ATOM   2825 N N    A HIS   A 1 138 ? 12.246 -10.753 -5.272  0.86 13.34 ?  138 HIS   A N    1 
ATOM   2826 N N    B HIS   A 1 138 ? 12.188 -10.616 -5.161  0.14 12.05 ?  138 HIS   A N    1 
ATOM   2827 C CA   A HIS   A 1 138 ? 13.413 -11.508 -5.709  0.86 12.91 ?  138 HIS   A CA   1 
ATOM   2828 C CA   B HIS   A 1 138 ? 13.298 -11.429 -5.651  0.14 12.14 ?  138 HIS   A CA   1 
ATOM   2829 C C    A HIS   A 1 138 ? 14.563 -11.368 -4.719  0.86 11.87 ?  138 HIS   A C    1 
ATOM   2830 C C    B HIS   A 1 138 ? 14.495 -11.353 -4.710  0.14 11.78 ?  138 HIS   A C    1 
ATOM   2831 O O    A HIS   A 1 138 ? 15.241 -12.354 -4.399  0.86 12.32 ?  138 HIS   A O    1 
ATOM   2832 O O    B HIS   A 1 138 ? 15.139 -12.370 -4.428  0.14 11.90 ?  138 HIS   A O    1 
ATOM   2833 C CB   A HIS   A 1 138 ? 13.828 -11.054 -7.107  0.86 13.52 ?  138 HIS   A CB   1 
ATOM   2834 C CB   B HIS   A 1 138 ? 13.683 -10.967 -7.057  0.14 12.46 ?  138 HIS   A CB   1 
ATOM   2835 C CG   A HIS   A 1 138 ? 15.090 -11.696 -7.589  0.86 14.23 ?  138 HIS   A CG   1 
ATOM   2836 C CG   B HIS   A 1 138 ? 14.959 -11.565 -7.562  0.14 12.83 ?  138 HIS   A CG   1 
ATOM   2837 N ND1  A HIS   A 1 138 ? 15.190 -13.048 -7.839  0.86 15.83 ?  138 HIS   A ND1  1 
ATOM   2838 N ND1  B HIS   A 1 138 ? 15.104 -12.914 -7.805  0.14 13.25 ?  138 HIS   A ND1  1 
ATOM   2839 C CD2  A HIS   A 1 138 ? 16.310 -11.172 -7.846  0.86 14.38 ?  138 HIS   A CD2  1 
ATOM   2840 C CD2  B HIS   A 1 138 ? 16.149 -10.997 -7.871  0.14 12.95 ?  138 HIS   A CD2  1 
ATOM   2841 C CE1  A HIS   A 1 138 ? 16.418 -13.326 -8.241  0.86 15.92 ?  138 HIS   A CE1  1 
ATOM   2842 C CE1  B HIS   A 1 138 ? 16.329 -13.151 -8.241  0.14 13.26 ?  138 HIS   A CE1  1 
ATOM   2843 N NE2  A HIS   A 1 138 ? 17.117 -12.206 -8.255  0.86 15.09 ?  138 HIS   A NE2  1 
ATOM   2844 N NE2  B HIS   A 1 138 ? 16.983 -12.004 -8.290  0.14 13.13 ?  138 HIS   A NE2  1 
ATOM   2845 H H    A HIS   A 1 138 ? 12.022 -10.100 -5.794  0.86 16.02 ?  138 HIS   A H    1 
ATOM   2846 H H    B HIS   A 1 138 ? 11.990 -9.941  -5.658  0.14 14.47 ?  138 HIS   A H    1 
ATOM   2847 H HA   A HIS   A 1 138 ? 13.169 -12.442 -5.761  0.86 15.50 ?  138 HIS   A HA   1 
ATOM   2848 H HA   B HIS   A 1 138 ? 13.014 -12.353 -5.705  0.14 14.57 ?  138 HIS   A HA   1 
ATOM   2849 H HB2  A HIS   A 1 138 ? 13.119 -11.281 -7.735  0.86 16.23 ?  138 HIS   A HB2  1 
ATOM   2850 H HB2  B HIS   A 1 138 ? 12.974 -11.216 -7.673  0.14 14.96 ?  138 HIS   A HB2  1 
ATOM   2851 H HB3  A HIS   A 1 138 ? 13.962 -10.094 -7.102  0.86 16.23 ?  138 HIS   A HB3  1 
ATOM   2852 H HB3  B HIS   A 1 138 ? 13.788 -10.003 -7.053  0.14 14.96 ?  138 HIS   A HB3  1 
ATOM   2853 H HD1  A HIS   A 1 138 ? 14.552 -13.618 -7.752  0.86 19.01 ?  138 HIS   A HD1  1 
ATOM   2854 H HD1  B HIS   A 1 138 ? 14.493 -13.508 -7.691  0.14 15.90 ?  138 HIS   A HD1  1 
ATOM   2855 H HD2  A HIS   A 1 138 ? 16.550 -10.277 -7.767  0.86 17.26 ?  138 HIS   A HD2  1 
ATOM   2856 H HD2  B HIS   A 1 138 ? 16.359 -10.092 -7.810  0.14 15.55 ?  138 HIS   A HD2  1 
ATOM   2857 H HE1  A HIS   A 1 138 ? 16.736 -14.166 -8.474  0.86 19.11 ?  138 HIS   A HE1  1 
ATOM   2858 H HE1  B HIS   A 1 138 ? 16.671 -13.983 -8.474  0.14 15.93 ?  138 HIS   A HE1  1 
ATOM   2859 N N    . SER   A 1 139 ? 14.802 -10.153 -4.217  1.00 11.51 ?  139 SER   A N    1 
ATOM   2860 C CA   . SER   A 1 139 ? 15.893 -9.979  -3.269  1.00 10.94 ?  139 SER   A CA   1 
ATOM   2861 C C    . SER   A 1 139 ? 15.684 -10.828 -2.020  1.00 10.61 ?  139 SER   A C    1 
ATOM   2862 O O    . SER   A 1 139 ? 16.638 -11.426 -1.509  1.00 10.68 ?  139 SER   A O    1 
ATOM   2863 C CB   . SER   A 1 139 ? 16.039 -8.505  -2.910  1.00 11.24 ?  139 SER   A CB   1 
ATOM   2864 O OG   . SER   A 1 139 ? 17.136 -8.348  -2.030  1.00 11.38 ?  139 SER   A OG   1 
ATOM   2865 H H    A SER   A 1 139 ? 14.356 -9.439  -4.402  0.86 13.82 ?  139 SER   A H    1 
ATOM   2866 H H    B SER   A 1 139 ? 14.384 -9.425  -4.415  0.14 13.82 ?  139 SER   A H    1 
ATOM   2867 H HA   . SER   A 1 139 ? 16.718 -10.261 -3.687  1.00 13.14 ?  139 SER   A HA   1 
ATOM   2868 H HB2  . SER   A 1 139 ? 16.199 -7.984  -3.717  1.00 13.49 ?  139 SER   A HB2  1 
ATOM   2869 H HB3  . SER   A 1 139 ? 15.233 -8.191  -2.468  1.00 13.49 ?  139 SER   A HB3  1 
ATOM   2870 H HG   . SER   A 1 139 ? 17.236 -7.538  -1.825  1.00 13.66 ?  139 SER   A HG   1 
ATOM   2871 N N    . LEU   A 1 140 ? 14.449 -10.892 -1.515  1.00 10.73 ?  140 LEU   A N    1 
ATOM   2872 C CA   . LEU   A 1 140 ? 14.180 -11.718 -0.342  1.00 10.68 ?  140 LEU   A CA   1 
ATOM   2873 C C    . LEU   A 1 140 ? 14.438 -13.192 -0.640  1.00 10.59 ?  140 LEU   A C    1 
ATOM   2874 O O    . LEU   A 1 140 ? 14.992 -13.918 0.195   1.00 11.23 ?  140 LEU   A O    1 
ATOM   2875 C CB   . LEU   A 1 140 ? 12.747 -11.488 0.139   1.00 11.24 ?  140 LEU   A CB   1 
ATOM   2876 C CG   . LEU   A 1 140 ? 12.293 -12.359 1.306   1.00 11.75 ?  140 LEU   A CG   1 
ATOM   2877 C CD1  . LEU   A 1 140 ? 13.205 -12.189 2.511   1.00 11.74 ?  140 LEU   A CD1  1 
ATOM   2878 C CD2  . LEU   A 1 140 ? 10.842 -12.040 1.677   1.00 12.91 ?  140 LEU   A CD2  1 
ATOM   2879 H H    . LEU   A 1 140 ? 13.765 -10.470 -1.823  1.00 12.88 ?  140 LEU   A H    1 
ATOM   2880 H HA   . LEU   A 1 140 ? 14.777 -11.451 0.375   1.00 12.83 ?  140 LEU   A HA   1 
ATOM   2881 H HB2  . LEU   A 1 140 ? 12.659 -10.565 0.420   1.00 13.50 ?  140 LEU   A HB2  1 
ATOM   2882 H HB3  . LEU   A 1 140 ? 12.144 -11.660 -0.601  1.00 13.50 ?  140 LEU   A HB3  1 
ATOM   2883 H HG   . LEU   A 1 140 ? 12.320 -13.292 1.035   1.00 14.11 ?  140 LEU   A HG   1 
ATOM   2884 H HD11 . LEU   A 1 140 ? 12.827 -12.670 3.264   1.00 14.09 ?  140 LEU   A HD11 1 
ATOM   2885 H HD12 . LEU   A 1 140 ? 14.079 -12.556 2.294   1.00 14.09 ?  140 LEU   A HD12 1 
ATOM   2886 H HD13 . LEU   A 1 140 ? 13.282 -11.249 2.719   1.00 14.09 ?  140 LEU   A HD13 1 
ATOM   2887 H HD21 . LEU   A 1 140 ? 10.574 -12.611 2.420   1.00 15.50 ?  140 LEU   A HD21 1 
ATOM   2888 H HD22 . LEU   A 1 140 ? 10.778 -11.111 1.937   1.00 15.50 ?  140 LEU   A HD22 1 
ATOM   2889 H HD23 . LEU   A 1 140 ? 10.272 -12.214 0.911   1.00 15.50 ?  140 LEU   A HD23 1 
ATOM   2890 N N    . ARG   A 1 141 ? 14.040 -13.651 -1.828  1.00 11.28 ?  141 ARG   A N    1 
ATOM   2891 C CA   . ARG   A 1 141 ? 14.273 -15.040 -2.213  1.00 12.19 ?  141 ARG   A CA   1 
ATOM   2892 C C    . ARG   A 1 141 ? 15.766 -15.354 -2.242  1.00 11.21 ?  141 ARG   A C    1 
ATOM   2893 O O    . ARG   A 1 141 ? 16.216 -16.371 -1.697  1.00 11.33 ?  141 ARG   A O    1 
ATOM   2894 C CB   . ARG   A 1 141 ? 13.640 -15.269 -3.587  1.00 14.20 ?  141 ARG   A CB   1 
ATOM   2895 C CG   . ARG   A 1 141 ? 13.619 -16.696 -4.063  1.00 17.14 ?  141 ARG   A CG   1 
ATOM   2896 C CD   . ARG   A 1 141 ? 12.592 -17.484 -3.307  1.00 19.02 ?  141 ARG   A CD   1 
ATOM   2897 N NE   . ARG   A 1 141 ? 13.215 -18.271 -2.257  1.00 19.61 ?  141 ARG   A NE   1 
ATOM   2898 C CZ   . ARG   A 1 141 ? 12.541 -18.872 -1.286  1.00 20.34 ?  141 ARG   A CZ   1 
ATOM   2899 N NH1  . ARG   A 1 141 ? 11.242 -18.682 -1.126  1.00 20.60 ?  141 ARG   A NH1  1 
ATOM   2900 N NH2  . ARG   A 1 141 ? 13.187 -19.679 -0.452  1.00 20.81 ?  141 ARG   A NH2  1 
ATOM   2901 H H    . ARG   A 1 141 ? 13.635 -13.179 -2.421  1.00 13.55 ?  141 ARG   A H    1 
ATOM   2902 H HA   . ARG   A 1 141 ? 13.849 -15.629 -1.574  1.00 14.64 ?  141 ARG   A HA   1 
ATOM   2903 H HB2  . ARG   A 1 141 ? 12.725 -14.947 -3.561  1.00 17.05 ?  141 ARG   A HB2  1 
ATOM   2904 H HB3  . ARG   A 1 141 ? 14.140 -14.751 -4.239  1.00 17.05 ?  141 ARG   A HB3  1 
ATOM   2905 H HG2  . ARG   A 1 141 ? 13.392 -16.718 -5.007  1.00 20.58 ?  141 ARG   A HG2  1 
ATOM   2906 H HG3  . ARG   A 1 141 ? 14.490 -17.101 -3.918  1.00 20.58 ?  141 ARG   A HG3  1 
ATOM   2907 H HD2  . ARG   A 1 141 ? 11.959 -16.878 -2.891  1.00 22.83 ?  141 ARG   A HD2  1 
ATOM   2908 H HD3  . ARG   A 1 141 ? 12.132 -18.082 -3.918  1.00 22.83 ?  141 ARG   A HD3  1 
ATOM   2909 H HE   . ARG   A 1 141 ? 14.050 -18.455 -2.334  1.00 23.54 ?  141 ARG   A HE   1 
ATOM   2910 H HH11 . ARG   A 1 141 ? 10.806 -18.176 -1.668  1.00 24.73 ?  141 ARG   A HH11 1 
ATOM   2911 H HH12 . ARG   A 1 141 ? 10.823 -19.083 -0.488  1.00 24.73 ?  141 ARG   A HH12 1 
ATOM   2912 H HH21 . ARG   A 1 141 ? 14.034 -19.807 -0.544  1.00 24.98 ?  141 ARG   A HH21 1 
ATOM   2913 H HH22 . ARG   A 1 141 ? 12.764 -20.066 0.191   1.00 24.98 ?  141 ARG   A HH22 1 
ATOM   2914 N N    . VAL   A 1 142 ? 16.557 -14.481 -2.871  1.00 10.86 ?  142 VAL   A N    1 
ATOM   2915 C CA   . VAL   A 1 142 ? 18.003 -14.696 -2.912  1.00 10.85 ?  142 VAL   A CA   1 
ATOM   2916 C C    . VAL   A 1 142 ? 18.587 -14.683 -1.504  1.00 10.05 ?  142 VAL   A C    1 
ATOM   2917 O O    . VAL   A 1 142 ? 19.450 -15.503 -1.167  1.00 10.50 ?  142 VAL   A O    1 
ATOM   2918 C CB   . VAL   A 1 142 ? 18.694 -13.673 -3.835  1.00 11.13 ?  142 VAL   A CB   1 
ATOM   2919 C CG1  . VAL   A 1 142 ? 20.206 -13.882 -3.810  1.00 10.87 ?  142 VAL   A CG1  1 
ATOM   2920 C CG2  . VAL   A 1 142 ? 18.179 -13.800 -5.260  1.00 12.33 ?  142 VAL   A CG2  1 
ATOM   2921 H H    . VAL   A 1 142 ? 16.293 -13.760 -3.269  1.00 13.04 ?  142 VAL   A H    1 
ATOM   2922 H HA   . VAL   A 1 142 ? 18.172 -15.568 -3.287  1.00 13.03 ?  142 VAL   A HA   1 
ATOM   2923 H HB   . VAL   A 1 142 ? 18.513 -12.768 -3.520  1.00 13.36 ?  142 VAL   A HB   1 
ATOM   2924 H HG11 . VAL   A 1 142 ? 20.608 -13.386 -4.541  1.00 13.05 ?  142 VAL   A HG11 1 
ATOM   2925 H HG12 . VAL   A 1 142 ? 20.562 -13.557 -2.963  1.00 13.05 ?  142 VAL   A HG12 1 
ATOM   2926 H HG13 . VAL   A 1 142 ? 20.395 -14.826 -3.906  1.00 13.05 ?  142 VAL   A HG13 1 
ATOM   2927 H HG21 . VAL   A 1 142 ? 18.650 -13.164 -5.823  1.00 14.80 ?  142 VAL   A HG21 1 
ATOM   2928 H HG22 . VAL   A 1 142 ? 18.351 -14.703 -5.570  1.00 14.80 ?  142 VAL   A HG22 1 
ATOM   2929 H HG23 . VAL   A 1 142 ? 17.233 -13.617 -5.268  1.00 14.80 ?  142 VAL   A HG23 1 
ATOM   2930 N N    . CYS   A 1 143 ? 18.119 -13.767 -0.657  1.00 10.24 ?  143 CYS   A N    1 
ATOM   2931 C CA   . CYS   A 1 143 ? 18.586 -13.726 0.724   1.00 10.32 ?  143 CYS   A CA   1 
ATOM   2932 C C    . CYS   A 1 143 ? 18.368 -15.072 1.407   1.00 9.87  ?  143 CYS   A C    1 
ATOM   2933 O O    . CYS   A 1 143 ? 19.294 -15.658 1.977   1.00 10.15 ?  143 CYS   A O    1 
ATOM   2934 C CB   . CYS   A 1 143 ? 17.846 -12.626 1.478   1.00 10.50 ?  143 CYS   A CB   1 
ATOM   2935 S SG   . CYS   A 1 143 ? 18.358 -12.443 3.205   1.00 11.03 ?  143 CYS   A SG   1 
ATOM   2936 H H    . CYS   A 1 143 ? 17.538 -13.167 -0.856  1.00 12.30 ?  143 CYS   A H    1 
ATOM   2937 H HA   . CYS   A 1 143 ? 19.532 -13.531 0.740   1.00 12.39 ?  143 CYS   A HA   1 
ATOM   2938 H HB2  . CYS   A 1 143 ? 18.004 -11.778 1.030   1.00 12.60 ?  143 CYS   A HB2  1 
ATOM   2939 H HB3  . CYS   A 1 143 ? 16.899 -12.823 1.473   1.00 12.60 ?  143 CYS   A HB3  1 
ATOM   2940 H HG   . CYS   A 1 143 ? 17.761 -11.523 3.690   1.00 13.25 ?  143 CYS   A HG   1 
ATOM   2941 N N    . VAL   A 1 144 ? 17.137 -15.576 1.359   1.00 10.49 ?  144 VAL   A N    1 
ATOM   2942 C CA   . VAL   A 1 144 ? 16.809 -16.813 2.062   1.00 11.68 ?  144 VAL   A CA   1 
ATOM   2943 C C    . VAL   A 1 144 ? 17.619 -17.982 1.522   1.00 11.19 ?  144 VAL   A C    1 
ATOM   2944 O O    . VAL   A 1 144 ? 17.992 -18.893 2.272   1.00 11.88 ?  144 VAL   A O    1 
ATOM   2945 C CB   . VAL   A 1 144 ? 15.292 -17.057 1.965   1.00 14.75 ?  144 VAL   A CB   1 
ATOM   2946 C CG1  . VAL   A 1 144 ? 14.941 -18.487 2.316   1.00 16.28 ?  144 VAL   A CG1  1 
ATOM   2947 C CG2  . VAL   A 1 144 ? 14.551 -16.058 2.849   1.00 14.64 ?  144 VAL   A CG2  1 
ATOM   2948 H H    . VAL   A 1 144 ? 16.475 -15.220 0.934   1.00 12.59 ?  144 VAL   A H    1 
ATOM   2949 H HA   . VAL   A 1 144 ? 17.024 -16.706 2.997   1.00 14.03 ?  144 VAL   A HA   1 
ATOM   2950 H HB   . VAL   A 1 144 ? 15.004 -16.900 1.048   1.00 17.71 ?  144 VAL   A HB   1 
ATOM   2951 H HG11 . VAL   A 1 144 ? 13.987 -18.542 2.508   1.00 19.54 ?  144 VAL   A HG11 1 
ATOM   2952 H HG12 . VAL   A 1 144 ? 15.154 -19.065 1.567   1.00 19.54 ?  144 VAL   A HG12 1 
ATOM   2953 H HG13 . VAL   A 1 144 ? 15.445 -18.754 3.099   1.00 19.54 ?  144 VAL   A HG13 1 
ATOM   2954 H HG21 . VAL   A 1 144 ? 13.599 -16.251 2.825   1.00 17.57 ?  144 VAL   A HG21 1 
ATOM   2955 H HG22 . VAL   A 1 144 ? 14.879 -16.134 3.757   1.00 17.57 ?  144 VAL   A HG22 1 
ATOM   2956 H HG23 . VAL   A 1 144 ? 14.710 -15.158 2.515   1.00 17.57 ?  144 VAL   A HG23 1 
ATOM   2957 N N    . ASP   A 1 145 ? 17.879 -17.994 0.217   1.00 11.41 ?  145 ASP   A N    1 
ATOM   2958 C CA   . ASP   A 1 145 ? 18.585 -19.100 -0.421  1.00 11.92 ?  145 ASP   A CA   1 
ATOM   2959 C C    . ASP   A 1 145 ? 20.107 -18.954 -0.394  1.00 11.68 ?  145 ASP   A C    1 
ATOM   2960 O O    . ASP   A 1 145 ? 20.807 -19.846 -0.886  1.00 14.27 ?  145 ASP   A O    1 
ATOM   2961 C CB   . ASP   A 1 145 ? 18.126 -19.244 -1.873  1.00 13.39 ?  145 ASP   A CB   1 
ATOM   2962 C CG   . ASP   A 1 145 ? 16.661 -19.642 -1.990  1.00 15.24 ?  145 ASP   A CG   1 
ATOM   2963 O OD1  . ASP   A 1 145 ? 16.104 -20.192 -1.014  1.00 15.85 ?  145 ASP   A OD1  1 
ATOM   2964 O OD2  . ASP   A 1 145 ? 16.067 -19.420 -3.067  1.00 16.67 -1 145 ASP   A OD2  1 
ATOM   2965 H H    . ASP   A 1 145 ? 17.645 -17.365 -0.329  1.00 13.70 ?  145 ASP   A H    1 
ATOM   2966 H HA   . ASP   A 1 145 ? 18.356 -19.917 0.046   1.00 14.32 ?  145 ASP   A HA   1 
ATOM   2967 H HB2  . ASP   A 1 145 ? 18.247 -18.402 -2.331  1.00 16.08 ?  145 ASP   A HB2  1 
ATOM   2968 H HB3  . ASP   A 1 145 ? 18.650 -19.940 -2.298  1.00 16.08 ?  145 ASP   A HB3  1 
ATOM   2969 N N    . THR   A 1 146 ? 20.635 -17.864 0.151   1.00 10.35 ?  146 THR   A N    1 
ATOM   2970 C CA   . THR   A 1 146 ? 22.075 -17.609 0.158   1.00 9.78  ?  146 THR   A CA   1 
ATOM   2971 C C    . THR   A 1 146 ? 22.642 -17.425 1.555   1.00 9.61  ?  146 THR   A C    1 
ATOM   2972 O O    . THR   A 1 146 ? 23.722 -17.948 1.856   1.00 10.68 ?  146 THR   A O    1 
ATOM   2973 C CB   . THR   A 1 146 ? 22.394 -16.352 -0.682  1.00 9.76  ?  146 THR   A CB   1 
ATOM   2974 O OG1  . THR   A 1 146 ? 21.854 -16.507 -1.995  1.00 10.50 ?  146 THR   A OG1  1 
ATOM   2975 C CG2  . THR   A 1 146 ? 23.900 -16.119 -0.783  1.00 10.58 ?  146 THR   A CG2  1 
ATOM   2976 H H    . THR   A 1 146 ? 20.172 -17.237 0.525   1.00 12.43 ?  146 THR   A H    1 
ATOM   2977 H HA   . THR   A 1 146 ? 22.529 -18.358 -0.250  1.00 11.75 ?  146 THR   A HA   1 
ATOM   2978 H HB   . THR   A 1 146 ? 21.999 -15.572 -0.267  1.00 11.72 ?  146 THR   A HB   1 
ATOM   2979 H HG1  . THR   A 1 146 ? 21.015 -16.582 -1.956  1.00 12.61 ?  146 THR   A HG1  1 
ATOM   2980 H HG21 . THR   A 1 146 ? 24.087 -15.447 -1.457  1.00 12.70 ?  146 THR   A HG21 1 
ATOM   2981 H HG22 . THR   A 1 146 ? 24.246 -15.816 0.069   1.00 12.70 ?  146 THR   A HG22 1 
ATOM   2982 H HG23 . THR   A 1 146 ? 24.345 -16.945 -1.031  1.00 12.70 ?  146 THR   A HG23 1 
ATOM   2983 N N    . VAL   A 1 147 ? 21.962 -16.658 2.399   1.00 9.58  ?  147 VAL   A N    1 
ATOM   2984 C CA   . VAL   A 1 147 ? 22.459 -16.363 3.734   1.00 9.76  ?  147 VAL   A CA   1 
ATOM   2985 C C    . VAL   A 1 147 ? 22.135 -17.531 4.650   1.00 9.91  ?  147 VAL   A C    1 
ATOM   2986 O O    . VAL   A 1 147 ? 20.989 -18.000 4.705   1.00 10.51 ?  147 VAL   A O    1 
ATOM   2987 C CB   . VAL   A 1 147 ? 21.845 -15.057 4.260   1.00 10.08 ?  147 VAL   A CB   1 
ATOM   2988 C CG1  . VAL   A 1 147 ? 22.388 -14.743 5.639   1.00 11.17 ?  147 VAL   A CG1  1 
ATOM   2989 C CG2  . VAL   A 1 147 ? 22.098 -13.909 3.288   1.00 10.15 ?  147 VAL   A CG2  1 
ATOM   2990 H H    . VAL   A 1 147 ? 21.198 -16.300 2.225   1.00 11.50 ?  147 VAL   A H    1 
ATOM   2991 H HA   . VAL   A 1 147 ? 23.424 -16.255 3.697   1.00 11.72 ?  147 VAL   A HA   1 
ATOM   2992 H HB   . VAL   A 1 147 ? 20.890 -15.168 4.339   1.00 12.11 ?  147 VAL   A HB   1 
ATOM   2993 H HG11 . VAL   A 1 147 ? 22.142 -13.838 5.879   1.00 13.41 ?  147 VAL   A HG11 1 
ATOM   2994 H HG12 . VAL   A 1 147 ? 22.010 -15.369 6.278   1.00 13.41 ?  147 VAL   A HG12 1 
ATOM   2995 H HG13 . VAL   A 1 147 ? 23.356 -14.830 5.627   1.00 13.41 ?  147 VAL   A HG13 1 
ATOM   2996 H HG21 . VAL   A 1 147 ? 21.776 -13.082 3.685   1.00 12.19 ?  147 VAL   A HG21 1 
ATOM   2997 H HG22 . VAL   A 1 147 ? 23.051 -13.840 3.117   1.00 12.19 ?  147 VAL   A HG22 1 
ATOM   2998 H HG23 . VAL   A 1 147 ? 21.625 -14.083 2.461   1.00 12.19 ?  147 VAL   A HG23 1 
ATOM   2999 N N    . ARG   A 1 148 ? 23.161 -18.011 5.355   1.00 9.97  ?  148 ARG   A N    1 
ATOM   3000 C CA   . ARG   A 1 148 ? 23.034 -19.090 6.321   1.00 10.35 ?  148 ARG   A CA   1 
ATOM   3001 C C    . ARG   A 1 148 ? 23.181 -18.618 7.757   1.00 10.72 ?  148 ARG   A C    1 
ATOM   3002 O O    . ARG   A 1 148 ? 22.790 -19.346 8.676   1.00 12.01 ?  148 ARG   A O    1 
ATOM   3003 C CB   . ARG   A 1 148 ? 24.070 -20.185 6.029   1.00 10.98 ?  148 ARG   A CB   1 
ATOM   3004 C CG   . ARG   A 1 148 ? 23.889 -20.824 4.660   1.00 11.99 ?  148 ARG   A CG   1 
ATOM   3005 C CD   . ARG   A 1 148 ? 24.970 -21.856 4.348   1.00 13.05 ?  148 ARG   A CD   1 
ATOM   3006 N NE   . ARG   A 1 148 ? 26.307 -21.273 4.356   1.00 12.80 ?  148 ARG   A NE   1 
ATOM   3007 C CZ   . ARG   A 1 148 ? 26.805 -20.528 3.378   1.00 12.05 ?  148 ARG   A CZ   1 
ATOM   3008 N NH1  . ARG   A 1 148 ? 26.117 -20.287 2.274   1.00 12.63 ?  148 ARG   A NH1  1 
ATOM   3009 N NH2  . ARG   A 1 148 ? 28.026 -20.006 3.511   1.00 12.45 ?  148 ARG   A NH2  1 
ATOM   3010 H H    . ARG   A 1 148 ? 23.972 -17.717 5.273   1.00 11.97 ?  148 ARG   A H    1 
ATOM   3011 H HA   . ARG   A 1 148 ? 22.157 -19.483 6.225   1.00 12.42 ?  148 ARG   A HA   1 
ATOM   3012 H HB2  . ARG   A 1 148 ? 24.958 -19.807 6.066   1.00 13.18 ?  148 ARG   A HB2  1 
ATOM   3013 H HB3  . ARG   A 1 148 ? 23.978 -20.889 6.695   1.00 13.18 ?  148 ARG   A HB3  1 
ATOM   3014 H HG2  . ARG   A 1 148 ? 23.026 -21.267 4.631   1.00 14.39 ?  148 ARG   A HG2  1 
ATOM   3015 H HG3  . ARG   A 1 148 ? 23.928 -20.128 3.984   1.00 14.39 ?  148 ARG   A HG3  1 
ATOM   3016 H HD2  . ARG   A 1 148 ? 24.944 -22.556 5.018   1.00 15.67 ?  148 ARG   A HD2  1 
ATOM   3017 H HD3  . ARG   A 1 148 ? 24.807 -22.231 3.467   1.00 15.67 ?  148 ARG   A HD3  1 
ATOM   3018 H HE   . ARG   A 1 148 ? 26.807 -21.419 5.038   1.00 15.36 ?  148 ARG   A HE   1 
ATOM   3019 H HH11 . ARG   A 1 148 ? 25.329 -20.613 2.172   1.00 15.16 ?  148 ARG   A HH11 1 
ATOM   3020 H HH12 . ARG   A 1 148 ? 26.460 -19.797 1.650   1.00 15.16 ?  148 ARG   A HH12 1 
ATOM   3021 H HH21 . ARG   A 1 148 ? 28.478 -20.152 4.224   1.00 14.95 ?  148 ARG   A HH21 1 
ATOM   3022 H HH22 . ARG   A 1 148 ? 28.356 -19.518 2.882   1.00 14.95 ?  148 ARG   A HH22 1 
ATOM   3023 N N    . THR   A 1 149 ? 23.732 -17.428 7.967   1.00 10.33 ?  149 THR   A N    1 
ATOM   3024 C CA   . THR   A 1 149 ? 23.819 -16.830 9.286   1.00 10.54 ?  149 THR   A CA   1 
ATOM   3025 C C    . THR   A 1 149 ? 22.494 -16.134 9.610   1.00 10.21 ?  149 THR   A C    1 
ATOM   3026 O O    . THR   A 1 149 ? 21.541 -16.143 8.821   1.00 10.86 ?  149 THR   A O    1 
ATOM   3027 C CB   . THR   A 1 149 ? 25.020 -15.894 9.338   1.00 11.00 ?  149 THR   A CB   1 
ATOM   3028 O OG1  . THR   A 1 149 ? 24.878 -14.956 8.274   1.00 11.13 ?  149 THR   A OG1  1 
ATOM   3029 C CG2  . THR   A 1 149 ? 26.338 -16.683 9.183   1.00 11.84 ?  149 THR   A CG2  1 
ATOM   3030 H H    . THR   A 1 149 ? 24.073 -16.937 7.344   1.00 12.41 ?  149 THR   A H    1 
ATOM   3031 H HA   . THR   A 1 149 ? 23.955 -17.535 9.938   1.00 12.66 ?  149 THR   A HA   1 
ATOM   3032 H HB   . THR   A 1 149 ? 25.029 -15.431 10.188  1.00 13.21 ?  149 THR   A HB   1 
ATOM   3033 H HG1  . THR   A 1 149 ? 25.529 -14.422 8.274   1.00 13.37 ?  149 THR   A HG1  1 
ATOM   3034 H HG21 . THR   A 1 149 ? 27.095 -16.079 9.234   1.00 14.22 ?  149 THR   A HG21 1 
ATOM   3035 H HG22 . THR   A 1 149 ? 26.417 -17.347 9.888   1.00 14.22 ?  149 THR   A HG22 1 
ATOM   3036 H HG23 . THR   A 1 149 ? 26.358 -17.138 8.324   1.00 14.22 ?  149 THR   A HG23 1 
ATOM   3037 N N    . ASN   A 1 150 ? 22.391 -15.580 10.809  1.00 10.54 ?  150 ASN   A N    1 
ATOM   3038 C CA   . ASN   A 1 150 ? 21.111 -15.088 11.316  1.00 10.85 ?  150 ASN   A CA   1 
ATOM   3039 C C    . ASN   A 1 150 ? 20.914 -13.645 10.876  1.00 10.38 ?  150 ASN   A C    1 
ATOM   3040 O O    . ASN   A 1 150 ? 21.646 -12.748 11.313  1.00 12.26 ?  150 ASN   A O    1 
ATOM   3041 C CB   . ASN   A 1 150 ? 21.080 -15.215 12.832  1.00 12.99 ?  150 ASN   A CB   1 
ATOM   3042 C CG   . ASN   A 1 150 ? 20.936 -16.649 13.282  1.00 17.95 ?  150 ASN   A CG   1 
ATOM   3043 O OD1  . ASN   A 1 150 ? 20.334 -17.468 12.589  1.00 19.63 ?  150 ASN   A OD1  1 
ATOM   3044 N ND2  . ASN   A 1 150 ? 21.508 -16.969 14.437  1.00 20.57 ?  150 ASN   A ND2  1 
ATOM   3045 H H    . ASN   A 1 150 ? 23.052 -15.473 11.350  1.00 12.66 ?  150 ASN   A H    1 
ATOM   3046 H HA   . ASN   A 1 150 ? 20.393 -15.625 10.948  1.00 13.03 ?  150 ASN   A HA   1 
ATOM   3047 H HB2  . ASN   A 1 150 ? 21.908 -14.866 13.199  1.00 15.59 ?  150 ASN   A HB2  1 
ATOM   3048 H HB3  . ASN   A 1 150 ? 20.325 -14.717 13.177  1.00 15.59 ?  150 ASN   A HB3  1 
ATOM   3049 H HD21 . ASN   A 1 150 ? 21.457 -17.777 14.736  1.00 24.69 ?  150 ASN   A HD21 1 
ATOM   3050 H HD22 . ASN   A 1 150 ? 21.924 -16.371 14.895  1.00 24.69 ?  150 ASN   A HD22 1 
ATOM   3051 N N    . VAL   A 1 151 ? 19.923 -13.414 10.021  1.00 10.08 ?  151 VAL   A N    1 
ATOM   3052 C CA   . VAL   A 1 151 ? 19.702 -12.098 9.439   1.00 10.20 ?  151 VAL   A CA   1 
ATOM   3053 C C    . VAL   A 1 151 ? 18.318 -11.583 9.820   1.00 10.15 ?  151 VAL   A C    1 
ATOM   3054 O O    . VAL   A 1 151 ? 17.311 -12.296 9.690   1.00 11.27 ?  151 VAL   A O    1 
ATOM   3055 C CB   . VAL   A 1 151 ? 19.979 -12.072 7.920   1.00 11.65 ?  151 VAL   A CB   1 
ATOM   3056 C CG1  . VAL   A 1 151 ? 19.154 -13.095 7.171   1.00 12.91 ?  151 VAL   A CG1  1 
ATOM   3057 C CG2  . VAL   A 1 151 ? 19.770 -10.670 7.355   1.00 12.26 ?  151 VAL   A CG2  1 
ATOM   3058 H H    . VAL   A 1 151 ? 19.368 -14.014 9.750   1.00 12.11 ?  151 VAL   A H    1 
ATOM   3059 H HA   . VAL   A 1 151 ? 20.345 -11.491 9.832   1.00 12.25 ?  151 VAL   A HA   1 
ATOM   3060 H HB   . VAL   A 1 151 ? 20.914 -12.298 7.771   1.00 13.99 ?  151 VAL   A HB   1 
ATOM   3061 H HG11 . VAL   A 1 151 ? 19.338 -13.030 6.220   1.00 15.50 ?  151 VAL   A HG11 1 
ATOM   3062 H HG12 . VAL   A 1 151 ? 19.384 -13.986 7.488   1.00 15.50 ?  151 VAL   A HG12 1 
ATOM   3063 H HG13 . VAL   A 1 151 ? 18.210 -12.925 7.334   1.00 15.50 ?  151 VAL   A HG13 1 
ATOM   3064 H HG21 . VAL   A 1 151 ? 20.088 -10.646 6.438   1.00 14.73 ?  151 VAL   A HG21 1 
ATOM   3065 H HG22 . VAL   A 1 151 ? 18.823 -10.458 7.380   1.00 14.73 ?  151 VAL   A HG22 1 
ATOM   3066 H HG23 . VAL   A 1 151 ? 20.267 -10.036 7.893   1.00 14.73 ?  151 VAL   A HG23 1 
ATOM   3067 N N    . TYR   A 1 152 ? 18.308 -10.335 10.303  1.00 9.94  ?  152 TYR   A N    1 
ATOM   3068 C CA   . TYR   A 1 152 ? 17.122 -9.597  10.703  1.00 10.02 ?  152 TYR   A CA   1 
ATOM   3069 C C    . TYR   A 1 152 ? 16.928 -8.492  9.673   1.00 9.70  ?  152 TYR   A C    1 
ATOM   3070 O O    . TYR   A 1 152 ? 17.711 -7.536  9.618   1.00 10.17 ?  152 TYR   A O    1 
ATOM   3071 C CB   . TYR   A 1 152 ? 17.309 -9.059  12.122  1.00 10.16 ?  152 TYR   A CB   1 
ATOM   3072 C CG   . TYR   A 1 152 ? 17.284 -10.199 13.113  1.00 10.86 ?  152 TYR   A CG   1 
ATOM   3073 C CD1  . TYR   A 1 152 ? 18.423 -10.946 13.388  1.00 12.04 ?  152 TYR   A CD1  1 
ATOM   3074 C CD2  . TYR   A 1 152 ? 16.100 -10.571 13.731  1.00 11.13 ?  152 TYR   A CD2  1 
ATOM   3075 C CE1  . TYR   A 1 152 ? 18.389 -12.022 14.257  1.00 12.94 ?  152 TYR   A CE1  1 
ATOM   3076 C CE2  . TYR   A 1 152 ? 16.052 -11.653 14.604  1.00 12.21 ?  152 TYR   A CE2  1 
ATOM   3077 C CZ   . TYR   A 1 152 ? 17.200 -12.375 14.860  1.00 12.86 ?  152 TYR   A CZ   1 
ATOM   3078 O OH   . TYR   A 1 152 ? 17.160 -13.455 15.722  1.00 14.91 ?  152 TYR   A OH   1 
ATOM   3079 H H    . TYR   A 1 152 ? 19.032 -9.866  10.396  1.00 11.94 ?  152 TYR   A H    1 
ATOM   3080 H HA   . TYR   A 1 152 ? 16.354 -10.186 10.686  1.00 12.03 ?  152 TYR   A HA   1 
ATOM   3081 H HB2  . TYR   A 1 152 ? 18.162 -8.617  12.197  1.00 12.20 ?  152 TYR   A HB2  1 
ATOM   3082 H HB3  . TYR   A 1 152 ? 16.583 -8.454  12.338  1.00 12.20 ?  152 TYR   A HB3  1 
ATOM   3083 H HD1  . TYR   A 1 152 ? 19.221 -10.721 12.973  1.00 14.46 ?  152 TYR   A HD1  1 
ATOM   3084 H HD2  . TYR   A 1 152 ? 15.317 -10.099 13.553  1.00 13.37 ?  152 TYR   A HD2  1 
ATOM   3085 H HE1  . TYR   A 1 152 ? 19.164 -12.505 14.435  1.00 15.53 ?  152 TYR   A HE1  1 
ATOM   3086 H HE2  . TYR   A 1 152 ? 15.250 -11.883 15.018  1.00 14.66 ?  152 TYR   A HE2  1 
ATOM   3087 H HH   . TYR   A 1 152 ? 16.377 -13.540 16.033  1.00 17.90 ?  152 TYR   A HH   1 
ATOM   3088 N N    . LEU   A 1 153 ? 15.905 -8.653  8.836   1.00 9.91  ?  153 LEU   A N    1 
ATOM   3089 C CA   . LEU   A 1 153 ? 15.631 -7.742  7.733   1.00 10.31 ?  153 LEU   A CA   1 
ATOM   3090 C C    . LEU   A 1 153 ? 14.643 -6.668  8.158   1.00 10.82 ?  153 LEU   A C    1 
ATOM   3091 O O    . LEU   A 1 153 ? 13.551 -6.971  8.656   1.00 11.91 ?  153 LEU   A O    1 
ATOM   3092 C CB   . LEU   A 1 153 ? 15.054 -8.503  6.542   1.00 10.47 ?  153 LEU   A CB   1 
ATOM   3093 C CG   . LEU   A 1 153 ? 15.979 -9.524  5.874   1.00 10.54 ?  153 LEU   A CG   1 
ATOM   3094 C CD1  . LEU   A 1 153 ? 15.187 -10.411 4.933   1.00 11.30 ?  153 LEU   A CD1  1 
ATOM   3095 C CD2  . LEU   A 1 153 ? 17.104 -8.833  5.125   1.00 11.08 ?  153 LEU   A CD2  1 
ATOM   3096 H H    . LEU   A 1 153 ? 15.341 -9.303  8.896   1.00 11.90 ?  153 LEU   A H    1 
ATOM   3097 H HA   . LEU   A 1 153 ? 16.460 -7.326  7.466   1.00 12.38 ?  153 LEU   A HA   1 
ATOM   3098 H HB2  . LEU   A 1 153 ? 14.264 -8.977  6.840   1.00 12.58 ?  153 LEU   A HB2  1 
ATOM   3099 H HB3  . LEU   A 1 153 ? 14.805 -7.851  5.867   1.00 12.58 ?  153 LEU   A HB3  1 
ATOM   3100 H HG   . LEU   A 1 153 ? 16.379 -10.084 6.561   1.00 12.65 ?  153 LEU   A HG   1 
ATOM   3101 H HD11 . LEU   A 1 153 ? 15.768 -11.112 4.600   1.00 13.57 ?  153 LEU   A HD11 1 
ATOM   3102 H HD12 . LEU   A 1 153 ? 14.446 -10.797 5.421   1.00 13.57 ?  153 LEU   A HD12 1 
ATOM   3103 H HD13 . LEU   A 1 153 ? 14.860 -9.871  4.198   1.00 13.57 ?  153 LEU   A HD13 1 
ATOM   3104 H HD21 . LEU   A 1 153 ? 17.670 -9.511  4.722   1.00 13.31 ?  153 LEU   A HD21 1 
ATOM   3105 H HD22 . LEU   A 1 153 ? 16.721 -8.270  4.439   1.00 13.31 ?  153 LEU   A HD22 1 
ATOM   3106 H HD23 . LEU   A 1 153 ? 17.619 -8.301  5.749   1.00 13.31 ?  153 LEU   A HD23 1 
ATOM   3107 N N    . ALA   A 1 154 ? 15.019 -5.415  7.920   1.00 10.82 ?  154 ALA   A N    1 
ATOM   3108 C CA   . ALA   A 1 154 ? 14.172 -4.262  8.182   1.00 11.87 ?  154 ALA   A CA   1 
ATOM   3109 C C    . ALA   A 1 154 ? 13.646 -3.728  6.859   1.00 11.89 ?  154 ALA   A C    1 
ATOM   3110 O O    . ALA   A 1 154 ? 14.431 -3.401  5.957   1.00 12.58 ?  154 ALA   A O    1 
ATOM   3111 C CB   . ALA   A 1 154 ? 14.949 -3.156  8.897   1.00 12.44 ?  154 ALA   A CB   1 
ATOM   3112 H H    . ALA   A 1 154 ? 15.788 -5.201  7.588   1.00 13.00 ?  154 ALA   A H    1 
ATOM   3113 H HA   . ALA   A 1 154 ? 13.425 -4.520  8.743   1.00 14.25 ?  154 ALA   A HA   1 
ATOM   3114 H HB1  . ALA   A 1 154 ? 14.361 -2.401  9.058   1.00 14.94 ?  154 ALA   A HB1  1 
ATOM   3115 H HB2  . ALA   A 1 154 ? 15.292 -3.493  9.740   1.00 14.94 ?  154 ALA   A HB2  1 
ATOM   3116 H HB3  . ALA   A 1 154 ? 15.694 -2.874  8.333   1.00 14.94 ?  154 ALA   A HB3  1 
ATOM   3117 N N    A VAL   A 1 155 ? 12.324 -3.669  6.724   0.86 12.57 ?  155 VAL   A N    1 
ATOM   3118 N N    B VAL   A 1 155 ? 12.327 -3.559  6.801   0.14 12.21 ?  155 VAL   A N    1 
ATOM   3119 C CA   A VAL   A 1 155 ? 11.666 -3.182  5.514   0.86 13.54 ?  155 VAL   A CA   1 
ATOM   3120 C CA   B VAL   A 1 155 ? 11.623 -2.989  5.661   0.14 12.61 ?  155 VAL   A CA   1 
ATOM   3121 C C    A VAL   A 1 155 ? 10.916 -1.907  5.874   0.86 15.54 ?  155 VAL   A C    1 
ATOM   3122 C C    B VAL   A 1 155 ? 11.032 -1.653  6.092   0.14 13.44 ?  155 VAL   A C    1 
ATOM   3123 O O    A VAL   A 1 155 ? 9.970  -1.948  6.668   0.86 15.42 ?  155 VAL   A O    1 
ATOM   3124 O O    B VAL   A 1 155 ? 10.289 -1.583  7.078   0.14 13.49 ?  155 VAL   A O    1 
ATOM   3125 C CB   A VAL   A 1 155 ? 10.720 -4.238  4.917   0.86 13.47 ?  155 VAL   A CB   1 
ATOM   3126 C CB   B VAL   A 1 155 ? 10.522 -3.942  5.167   0.14 12.49 ?  155 VAL   A CB   1 
ATOM   3127 C CG1  A VAL   A 1 155 ? 9.993  -3.678  3.709   0.86 14.52 ?  155 VAL   A CG1  1 
ATOM   3128 C CG1  B VAL   A 1 155 ? 9.819  -3.353  3.961   0.14 12.59 ?  155 VAL   A CG1  1 
ATOM   3129 C CG2  A VAL   A 1 155 ? 11.497 -5.497  4.536   0.86 14.16 ?  155 VAL   A CG2  1 
ATOM   3130 C CG2  B VAL   A 1 155 ? 11.112 -5.309  4.848   0.14 12.49 ?  155 VAL   A CG2  1 
ATOM   3131 H H    A VAL   A 1 155 ? 11.770 -3.916  7.339   0.86 15.09 ?  155 VAL   A H    1 
ATOM   3132 H H    B VAL   A 1 155 ? 11.799 -3.770  7.449   0.14 14.66 ?  155 VAL   A H    1 
ATOM   3133 H HA   A VAL   A 1 155 ? 12.338 -2.964  4.851   0.86 16.26 ?  155 VAL   A HA   1 
ATOM   3134 H HA   B VAL   A 1 155 ? 12.248 -2.836  4.938   0.14 15.14 ?  155 VAL   A HA   1 
ATOM   3135 H HB   A VAL   A 1 155 ? 10.058 -4.484  5.587   0.86 16.18 ?  155 VAL   A HB   1 
ATOM   3136 H HB   B VAL   A 1 155 ? 9.867  -4.057  5.874   0.14 14.99 ?  155 VAL   A HB   1 
ATOM   3137 H HG11 A VAL   A 1 155 ? 9.562  -4.403  3.234   0.86 17.44 ?  155 VAL   A HG11 1 
ATOM   3138 H HG11 B VAL   A 1 155 ? 9.245  -4.030  3.573   0.14 15.11 ?  155 VAL   A HG11 1 
ATOM   3139 H HG12 A VAL   A 1 155 ? 9.324  -3.036  4.006   0.86 17.44 ?  155 VAL   A HG12 1 
ATOM   3140 H HG12 B VAL   A 1 155 ? 9.289  -2.592  4.244   0.14 15.11 ?  155 VAL   A HG12 1 
ATOM   3141 H HG13 A VAL   A 1 155 ? 10.634 -3.237  3.129   0.86 17.44 ?  155 VAL   A HG13 1 
ATOM   3142 H HG13 B VAL   A 1 155 ? 10.486 -3.073  3.315   0.14 15.11 ?  155 VAL   A HG13 1 
ATOM   3143 H HG21 A VAL   A 1 155 ? 10.887 -6.135  4.139   0.86 17.00 ?  155 VAL   A HG21 1 
ATOM   3144 H HG21 B VAL   A 1 155 ? 10.422 -5.866  4.458   0.14 15.00 ?  155 VAL   A HG21 1 
ATOM   3145 H HG22 A VAL   A 1 155 ? 12.187 -5.255  3.897   0.86 17.00 ?  155 VAL   A HG22 1 
ATOM   3146 H HG22 B VAL   A 1 155 ? 11.843 -5.198  4.220   0.14 15.00 ?  155 VAL   A HG22 1 
ATOM   3147 H HG23 A VAL   A 1 155 ? 11.902 -5.874  5.332   0.86 17.00 ?  155 VAL   A HG23 1 
ATOM   3148 H HG23 B VAL   A 1 155 ? 11.440 -5.713  5.668   0.14 15.00 ?  155 VAL   A HG23 1 
ATOM   3149 N N    A PHE   A 1 156 ? 11.341 -0.777  5.293   0.86 17.37 ?  156 PHE   A N    1 
ATOM   3150 N N    B PHE   A 1 156 ? 11.357 -0.596  5.345   0.14 14.09 ?  156 PHE   A N    1 
ATOM   3151 C CA   A PHE   A 1 156 ? 10.787 0.530   5.658   0.86 19.20 ?  156 PHE   A CA   1 
ATOM   3152 C CA   B PHE   A 1 156 ? 10.926 0.751   5.710   0.14 14.94 ?  156 PHE   A CA   1 
ATOM   3153 C C    A PHE   A 1 156 ? 9.312  0.657   5.286   0.86 19.31 ?  156 PHE   A C    1 
ATOM   3154 C C    B PHE   A 1 156 ? 9.424  0.930   5.522   0.14 14.78 ?  156 PHE   A C    1 
ATOM   3155 O O    A PHE   A 1 156 ? 8.510  1.176   6.073   0.86 20.58 ?  156 PHE   A O    1 
ATOM   3156 O O    B PHE   A 1 156 ? 8.756  1.538   6.366   0.14 15.00 ?  156 PHE   A O    1 
ATOM   3157 C CB   A PHE   A 1 156 ? 11.602 1.625   4.966   0.86 20.27 ?  156 PHE   A CB   1 
ATOM   3158 C CB   B PHE   A 1 156 ? 11.697 1.761   4.860   0.14 15.78 ?  156 PHE   A CB   1 
ATOM   3159 C CG   A PHE   A 1 156 ? 11.146 3.022   5.280   0.86 22.11 ?  156 PHE   A CG   1 
ATOM   3160 C CG   B PHE   A 1 156 ? 11.460 3.199   5.234   0.14 16.49 ?  156 PHE   A CG   1 
ATOM   3161 C CD1  A PHE   A 1 156 ? 11.123 3.474   6.587   0.86 23.10 ?  156 PHE   A CD1  1 
ATOM   3162 C CD1  B PHE   A 1 156 ? 11.857 3.686   6.469   0.14 16.74 ?  156 PHE   A CD1  1 
ATOM   3163 C CD2  A PHE   A 1 156 ? 10.769 3.890   4.265   0.86 22.80 ?  156 PHE   A CD2  1 
ATOM   3164 C CD2  B PHE   A 1 156 ? 10.875 4.074   4.332   0.14 16.74 ?  156 PHE   A CD2  1 
ATOM   3165 C CE1  A PHE   A 1 156 ? 10.715 4.762   6.881   0.86 24.02 ?  156 PHE   A CE1  1 
ATOM   3166 C CE1  B PHE   A 1 156 ? 11.651 5.013   6.806   0.14 16.83 ?  156 PHE   A CE1  1 
ATOM   3167 C CE2  A PHE   A 1 156 ? 10.360 5.182   4.551   0.86 23.92 ?  156 PHE   A CE2  1 
ATOM   3168 C CE2  B PHE   A 1 156 ? 10.670 5.402   4.662   0.14 16.87 ?  156 PHE   A CE2  1 
ATOM   3169 C CZ   A PHE   A 1 156 ? 10.337 5.620   5.861   0.86 24.22 ?  156 PHE   A CZ   1 
ATOM   3170 C CZ   B PHE   A 1 156 ? 11.057 5.871   5.900   0.14 16.86 ?  156 PHE   A CZ   1 
ATOM   3171 H H    A PHE   A 1 156 ? 11.955 -0.743  4.692   0.86 20.85 ?  156 PHE   A H    1 
ATOM   3172 H H    B PHE   A 1 156 ? 11.825 -0.636  4.629   0.14 16.91 ?  156 PHE   A H    1 
ATOM   3173 H HA   A PHE   A 1 156 ? 10.871 0.654   6.615   0.86 23.05 ?  156 PHE   A HA   1 
ATOM   3174 H HA   B PHE   A 1 156 ? 11.134 0.913   6.643   0.14 17.94 ?  156 PHE   A HA   1 
ATOM   3175 H HB2  A PHE   A 1 156 ? 12.529 1.549   5.245   0.86 24.33 ?  156 PHE   A HB2  1 
ATOM   3176 H HB2  B PHE   A 1 156 ? 12.645 1.585   4.956   0.14 18.95 ?  156 PHE   A HB2  1 
ATOM   3177 H HB3  A PHE   A 1 156 ? 11.539 1.503   4.006   0.86 24.33 ?  156 PHE   A HB3  1 
ATOM   3178 H HB3  B PHE   A 1 156 ? 11.435 1.651   3.933   0.14 18.95 ?  156 PHE   A HB3  1 
ATOM   3179 H HD1  A PHE   A 1 156 ? 11.379 2.904   7.275   0.86 27.73 ?  156 PHE   A HD1  1 
ATOM   3180 H HD1  B PHE   A 1 156 ? 12.254 3.111   7.083   0.14 20.10 ?  156 PHE   A HD1  1 
ATOM   3181 H HD2  A PHE   A 1 156 ? 10.786 3.597   3.382   0.86 27.36 ?  156 PHE   A HD2  1 
ATOM   3182 H HD2  B PHE   A 1 156 ? 10.611 3.761   3.497   0.14 20.09 ?  156 PHE   A HD2  1 
ATOM   3183 H HE1  A PHE   A 1 156 ? 10.699 5.057   7.763   0.86 28.83 ?  156 PHE   A HE1  1 
ATOM   3184 H HE1  B PHE   A 1 156 ? 11.915 5.326   7.640   0.14 20.20 ?  156 PHE   A HE1  1 
ATOM   3185 H HE2  A PHE   A 1 156 ? 10.105 5.752   3.862   0.86 28.72 ?  156 PHE   A HE2  1 
ATOM   3186 H HE2  B PHE   A 1 156 ? 10.270 5.976   4.049   0.14 20.25 ?  156 PHE   A HE2  1 
ATOM   3187 H HZ   A PHE   A 1 156 ? 10.059 6.486   6.056   0.86 29.07 ?  156 PHE   A HZ   1 
ATOM   3188 H HZ   B PHE   A 1 156 ? 10.921 6.763   6.125   0.14 20.25 ?  156 PHE   A HZ   1 
ATOM   3189 N N    A ASP   A 1 157 ? 8.941  0.200   4.097   0.86 18.83 ?  157 ASP   A N    1 
ATOM   3190 N N    B ASP   A 1 157 ? 8.876  0.407   4.429   0.14 14.43 ?  157 ASP   A N    1 
ATOM   3191 C CA   A ASP   A 1 157 ? 7.613  0.438   3.544   0.86 19.55 ?  157 ASP   A CA   1 
ATOM   3192 C CA   B ASP   A 1 157 ? 7.492  0.649   4.045   0.14 14.60 ?  157 ASP   A CA   1 
ATOM   3193 C C    A ASP   A 1 157 ? 6.637  -0.630  4.035   0.86 19.31 ?  157 ASP   A C    1 
ATOM   3194 C C    B ASP   A 1 157 ? 6.594  -0.477  4.544   0.14 15.00 ?  157 ASP   A C    1 
ATOM   3195 O O    A ASP   A 1 157 ? 6.833  -1.820  3.767   0.86 18.06 ?  157 ASP   A O    1 
ATOM   3196 O O    B ASP   A 1 157 ? 6.947  -1.656  4.449   0.14 14.92 ?  157 ASP   A O    1 
ATOM   3197 C CB   A ASP   A 1 157 ? 7.702  0.412   2.022   0.86 20.81 ?  157 ASP   A CB   1 
ATOM   3198 C CB   B ASP   A 1 157 ? 7.388  0.753   2.523   0.14 14.41 ?  157 ASP   A CB   1 
ATOM   3199 C CG   A ASP   A 1 157 ? 6.446  0.930   1.365   0.86 22.66 ?  157 ASP   A CG   1 
ATOM   3200 C CG   B ASP   A 1 157 ? 6.015  1.178   2.064   0.14 14.18 ?  157 ASP   A CG   1 
ATOM   3201 O OD1  A ASP   A 1 157 ? 6.215  2.153   1.413   0.86 24.82 ?  157 ASP   A OD1  1 
ATOM   3202 O OD1  B ASP   A 1 157 ? 5.607  2.319   2.363   0.14 13.82 ?  157 ASP   A OD1  1 
ATOM   3203 O OD2  A ASP   A 1 157 ? 5.674  0.115   0.819   0.86 22.84 -1 157 ASP   A OD2  1 
ATOM   3204 O OD2  B ASP   A 1 157 ? 5.344  0.364   1.401   0.14 14.14 -1 157 ASP   A OD2  1 
ATOM   3205 H H    A ASP   A 1 157 ? 9.452  -0.268  3.583   0.86 22.60 ?  157 ASP   A H    1 
ATOM   3206 H H    B ASP   A 1 157 ? 9.296  -0.103  3.880   0.14 17.33 ?  157 ASP   A H    1 
ATOM   3207 H HA   A ASP   A 1 157 ? 7.293  1.307   3.825   0.86 23.47 ?  157 ASP   A HA   1 
ATOM   3208 H HA   B ASP   A 1 157 ? 7.185  1.484   4.431   0.14 17.53 ?  157 ASP   A HA   1 
ATOM   3209 H HB2  A ASP   A 1 157 ? 8.465  0.949   1.744   0.86 24.98 ?  157 ASP   A HB2  1 
ATOM   3210 H HB2  B ASP   A 1 157 ? 8.035  1.401   2.203   0.14 17.30 ?  157 ASP   A HB2  1 
ATOM   3211 H HB3  A ASP   A 1 157 ? 7.831  -0.505  1.728   0.86 24.98 ?  157 ASP   A HB3  1 
ATOM   3212 H HB3  B ASP   A 1 157 ? 7.566  -0.116  2.130   0.14 17.30 ?  157 ASP   A HB3  1 
ATOM   3213 N N    A LYS   A 1 158 ? 5.582  -0.204  4.745   0.86 20.61 ?  158 LYS   A N    1 
ATOM   3214 N N    B LYS   A 1 158 ? 5.423  -0.103  5.073   0.14 15.59 ?  158 LYS   A N    1 
ATOM   3215 C CA   A LYS   A 1 158 ? 4.618  -1.155  5.298   0.86 21.53 ?  158 LYS   A CA   1 
ATOM   3216 C CA   B LYS   A 1 158 ? 4.484  -1.103  5.575   0.14 16.33 ?  158 LYS   A CA   1 
ATOM   3217 C C    A LYS   A 1 158 ? 3.910  -1.931  4.192   0.86 21.06 ?  158 LYS   A C    1 
ATOM   3218 C C    B LYS   A 1 158 ? 3.804  -1.850  4.433   0.14 16.15 ?  158 LYS   A C    1 
ATOM   3219 O O    A LYS   A 1 158 ? 3.740  -3.155  4.288   0.86 20.92 ?  158 LYS   A O    1 
ATOM   3220 O O    B LYS   A 1 158 ? 3.595  -3.067  4.517   0.14 16.27 ?  158 LYS   A O    1 
ATOM   3221 C CB   A LYS   A 1 158 ? 3.609  -0.418  6.185   0.86 22.66 ?  158 LYS   A CB   1 
ATOM   3222 C CB   B LYS   A 1 158 ? 3.447  -0.439  6.484   0.14 17.21 ?  158 LYS   A CB   1 
ATOM   3223 C CG   A LYS   A 1 158 ? 2.413  -1.260  6.638   0.86 23.87 ?  158 LYS   A CG   1 
ATOM   3224 C CG   B LYS   A 1 158 ? 2.284  -1.340  6.894   0.14 17.95 ?  158 LYS   A CG   1 
ATOM   3225 C CD   A LYS   A 1 158 ? 2.827  -2.492  7.443   0.86 25.07 ?  158 LYS   A CD   1 
ATOM   3226 C CD   B LYS   A 1 158 ? 2.753  -2.581  7.641   0.14 18.62 ?  158 LYS   A CD   1 
ATOM   3227 C CE   A LYS   A 1 158 ? 1.600  -3.211  8.002   0.86 26.13 ?  158 LYS   A CE   1 
ATOM   3228 C CE   B LYS   A 1 158 ? 1.572  -3.418  8.109   0.14 19.19 ?  158 LYS   A CE   1 
ATOM   3229 N NZ   A LYS   A 1 158 ? 1.917  -4.554  8.569   0.86 26.72 ?  158 LYS   A NZ   1 
ATOM   3230 N NZ   B LYS   A 1 158 ? 1.995  -4.728  8.676   0.14 19.46 ?  158 LYS   A NZ   1 
ATOM   3231 H H    A LYS   A 1 158 ? 5.419  0.620   4.921   0.86 24.74 ?  158 LYS   A H    1 
ATOM   3232 H H    B LYS   A 1 158 ? 5.157  0.712   5.152   0.14 18.72 ?  158 LYS   A H    1 
ATOM   3233 H HA   A LYS   A 1 158 ? 5.093  -1.789  5.860   0.86 25.85 ?  158 LYS   A HA   1 
ATOM   3234 H HA   B LYS   A 1 158 ? 4.972  -1.749  6.107   0.14 19.60 ?  158 LYS   A HA   1 
ATOM   3235 H HB2  A LYS   A 1 158 ? 4.067  -0.106  6.985   0.86 27.20 ?  158 LYS   A HB2  1 
ATOM   3236 H HB2  B LYS   A 1 158 ? 3.890  -0.147  7.298   0.14 20.66 ?  158 LYS   A HB2  1 
ATOM   3237 H HB3  A LYS   A 1 158 ? 3.265  0.346   5.694   0.86 27.20 ?  158 LYS   A HB3  1 
ATOM   3238 H HB3  B LYS   A 1 158 ? 3.075  0.329   6.024   0.14 20.66 ?  158 LYS   A HB3  1 
ATOM   3239 H HG2  A LYS   A 1 158 ? 1.845  -0.712  7.201   0.86 28.65 ?  158 LYS   A HG2  1 
ATOM   3240 H HG2  B LYS   A 1 158 ? 1.694  -0.843  7.482   0.14 21.55 ?  158 LYS   A HG2  1 
ATOM   3241 H HG3  A LYS   A 1 158 ? 1.915  -1.555  5.860   0.86 28.65 ?  158 LYS   A HG3  1 
ATOM   3242 H HG3  B LYS   A 1 158 ? 1.797  -1.625  6.104   0.14 21.55 ?  158 LYS   A HG3  1 
ATOM   3243 H HD2  A LYS   A 1 158 ? 3.307  -3.105  6.866   0.86 30.10 ?  158 LYS   A HD2  1 
ATOM   3244 H HD2  B LYS   A 1 158 ? 3.298  -3.125  7.052   0.14 22.35 ?  158 LYS   A HD2  1 
ATOM   3245 H HD3  A LYS   A 1 158 ? 3.387  -2.215  8.185   0.86 30.10 ?  158 LYS   A HD3  1 
ATOM   3246 H HD3  B LYS   A 1 158 ? 3.264  -2.311  8.420   0.14 22.35 ?  158 LYS   A HD3  1 
ATOM   3247 H HE2  A LYS   A 1 158 ? 1.211  -2.670  8.707   0.86 31.36 ?  158 LYS   A HE2  1 
ATOM   3248 H HE2  B LYS   A 1 158 ? 1.092  -2.932  8.799   0.14 23.04 ?  158 LYS   A HE2  1 
ATOM   3249 H HE3  A LYS   A 1 158 ? 0.956  -3.332  7.287   0.86 31.36 ?  158 LYS   A HE3  1 
ATOM   3250 H HE3  B LYS   A 1 158 ? 0.985  -3.589  7.356   0.14 23.04 ?  158 LYS   A HE3  1 
ATOM   3251 H HZ1  A LYS   A 1 158 ? 1.176  -4.934  8.881   0.86 32.07 ?  158 LYS   A HZ1  1 
ATOM   3252 H HZ1  B LYS   A 1 158 ? 1.282  -5.190  8.939   0.14 23.37 ?  158 LYS   A HZ1  1 
ATOM   3253 H HZ2  A LYS   A 1 158 ? 2.265  -5.075  7.936   0.86 32.07 ?  158 LYS   A HZ2  1 
ATOM   3254 H HZ2  B LYS   A 1 158 ? 2.433  -5.198  8.060   0.14 23.37 ?  158 LYS   A HZ2  1 
ATOM   3255 H HZ3  A LYS   A 1 158 ? 2.504  -4.474  9.232   0.86 32.07 ?  158 LYS   A HZ3  1 
ATOM   3256 H HZ3  B LYS   A 1 158 ? 2.529  -4.598  9.376   0.14 23.37 ?  158 LYS   A HZ3  1 
ATOM   3257 N N    A ASN   A 1 159 ? 3.481  -1.238  3.137   0.86 21.80 ?  159 ASN   A N    1 
ATOM   3258 N N    B ASN   A 1 159 ? 3.443  -1.140  3.362   0.14 15.73 ?  159 ASN   A N    1 
ATOM   3259 C CA   A ASN   A 1 159 ? 2.832  -1.932  2.032   0.86 22.36 ?  159 ASN   A CA   1 
ATOM   3260 C CA   B ASN   A 1 159 ? 2.808  -1.792  2.220   0.14 15.28 ?  159 ASN   A CA   1 
ATOM   3261 C C    A ASN   A 1 159 ? 3.743  -3.003  1.441   0.86 20.99 ?  159 ASN   A C    1 
ATOM   3262 C C    B ASN   A 1 159 ? 3.696  -2.899  1.666   0.14 15.25 ?  159 ASN   A C    1 
ATOM   3263 O O    A ASN   A 1 159 ? 3.307  -4.132  1.184   0.86 20.83 ?  159 ASN   A O    1 
ATOM   3264 O O    B ASN   A 1 159 ? 3.230  -4.015  1.408   0.14 15.18 ?  159 ASN   A O    1 
ATOM   3265 C CB   A ASN   A 1 159 ? 2.384  -0.922  0.974   0.86 24.70 ?  159 ASN   A CB   1 
ATOM   3266 C CB   B ASN   A 1 159 ? 2.494  -0.760  1.135   0.14 14.95 ?  159 ASN   A CB   1 
ATOM   3267 C CG   A ASN   A 1 159 ? 1.167  -0.134  1.408   0.86 27.21 ?  159 ASN   A CG   1 
ATOM   3268 C CG   B ASN   A 1 159 ? 1.811  -1.371  -0.076  0.14 14.79 ?  159 ASN   A CG   1 
ATOM   3269 O OD1  A ASN   A 1 159 ? 0.286  -0.668  2.079   0.86 28.20 ?  159 ASN   A OD1  1 
ATOM   3270 O OD1  B ASN   A 1 159 ? 2.450  -2.022  -0.902  0.14 14.70 ?  159 ASN   A OD1  1 
ATOM   3271 N ND2  A ASN   A 1 159 ? 1.108  1.141   1.031   0.86 28.33 ?  159 ASN   A ND2  1 
ATOM   3272 N ND2  B ASN   A 1 159 ? 0.507  -1.149  -0.195  0.14 15.02 ?  159 ASN   A ND2  1 
ATOM   3273 H H    A ASN   A 1 159 ? 3.560  -0.386  3.044   0.86 26.17 ?  159 ASN   A H    1 
ATOM   3274 H H    B ASN   A 1 159 ? 3.552  -0.294  3.274   0.14 18.88 ?  159 ASN   A H    1 
ATOM   3275 H HA   A ASN   A 1 159 ? 2.041  -2.374  2.372   0.86 26.84 ?  159 ASN   A HA   1 
ATOM   3276 H HA   B ASN   A 1 159 ? 1.974  -2.194  2.506   0.14 18.35 ?  159 ASN   A HA   1 
ATOM   3277 H HB2  A ASN   A 1 159 ? 3.100  -0.291  0.808   0.86 29.65 ?  159 ASN   A HB2  1 
ATOM   3278 H HB2  B ASN   A 1 159 ? 1.903  -0.086  1.504   0.14 17.95 ?  159 ASN   A HB2  1 
ATOM   3279 H HB3  A ASN   A 1 159 ? 2.160  -1.396  0.159   0.86 29.65 ?  159 ASN   A HB3  1 
ATOM   3280 H HB3  B ASN   A 1 159 ? 3.319  -0.352  0.834   0.14 17.95 ?  159 ASN   A HB3  1 
ATOM   3281 H HD21 A ASN   A 1 159 ? 0.435  1.629   1.252   0.86 34.01 ?  159 ASN   A HD21 1 
ATOM   3282 H HD21 B ASN   A 1 159 ? 0.074  -1.473  -0.865  0.14 18.04 ?  159 ASN   A HD21 1 
ATOM   3283 H HD22 A ASN   A 1 159 ? 1.749  1.479   0.569   0.86 34.01 ?  159 ASN   A HD22 1 
ATOM   3284 H HD22 B ASN   A 1 159 ? 0.094  -0.687  0.400   0.14 18.04 ?  159 ASN   A HD22 1 
ATOM   3285 N N    A LEU   A 1 160 ? 5.021  -2.676  1.242   0.86 19.49 ?  160 LEU   A N    1 
ATOM   3286 N N    B LEU   A 1 160 ? 4.985  -2.608  1.482   0.14 15.10 ?  160 LEU   A N    1 
ATOM   3287 C CA   A LEU   A 1 160 ? 5.955  -3.664  0.711   0.86 18.59 ?  160 LEU   A CA   1 
ATOM   3288 C CA   B LEU   A 1 160 ? 5.896  -3.615  0.952   0.14 14.91 ?  160 LEU   A CA   1 
ATOM   3289 C C    A LEU   A 1 160 ? 6.156  -4.813  1.688   0.86 17.53 ?  160 LEU   A C    1 
ATOM   3290 C C    B LEU   A 1 160 ? 6.095  -4.759  1.939   0.14 14.60 ?  160 LEU   A C    1 
ATOM   3291 O O    A LEU   A 1 160 ? 6.177  -5.983  1.285   0.86 17.71 ?  160 LEU   A O    1 
ATOM   3292 O O    B LEU   A 1 160 ? 6.200  -5.922  1.535   0.14 14.54 ?  160 LEU   A O    1 
ATOM   3293 C CB   A LEU   A 1 160 ? 7.292  -3.005  0.375   0.86 18.48 ?  160 LEU   A CB   1 
ATOM   3294 C CB   B LEU   A 1 160 ? 7.237  -2.974  0.592   0.14 15.01 ?  160 LEU   A CB   1 
ATOM   3295 C CG   A LEU   A 1 160 ? 8.374  -3.993  -0.064  0.86 18.65 ?  160 LEU   A CG   1 
ATOM   3296 C CG   B LEU   A 1 160 ? 8.315  -3.959  0.136   0.14 15.10 ?  160 LEU   A CG   1 
ATOM   3297 C CD1  A LEU   A 1 160 ? 7.922  -4.757  -1.293  0.86 19.13 ?  160 LEU   A CD1  1 
ATOM   3298 C CD1  B LEU   A 1 160 ? 7.831  -4.749  -1.071  0.14 15.16 ?  160 LEU   A CD1  1 
ATOM   3299 C CD2  A LEU   A 1 160 ? 9.689  -3.288  -0.323  0.86 18.87 ?  160 LEU   A CD2  1 
ATOM   3300 C CD2  B LEU   A 1 160 ? 9.619  -3.239  -0.169  0.14 15.14 ?  160 LEU   A CD2  1 
ATOM   3301 H H    A LEU   A 1 160 ? 5.368  -1.902  1.409   0.86 23.40 ?  160 LEU   A H    1 
ATOM   3302 H H    B LEU   A 1 160 ? 5.349  -1.848  1.652   0.14 18.13 ?  160 LEU   A H    1 
ATOM   3303 H HA   A LEU   A 1 160 ? 5.588  -4.027  -0.103  0.86 22.31 ?  160 LEU   A HA   1 
ATOM   3304 H HA   B LEU   A 1 160 ? 5.516  -3.983  0.141   0.14 17.90 ?  160 LEU   A HA   1 
ATOM   3305 H HB2  A LEU   A 1 160 ? 7.157  -2.365  -0.346  0.86 22.19 ?  160 LEU   A HB2  1 
ATOM   3306 H HB2  B LEU   A 1 160 ? 7.094  -2.342  -0.132  0.14 18.02 ?  160 LEU   A HB2  1 
ATOM   3307 H HB3  A LEU   A 1 160 ? 7.620  -2.546  1.163   0.86 22.19 ?  160 LEU   A HB3  1 
ATOM   3308 H HB3  B LEU   A 1 160 ? 7.578  -2.507  1.369   0.14 18.02 ?  160 LEU   A HB3  1 
ATOM   3309 H HG   A LEU   A 1 160 ? 8.526  -4.634  0.645   0.86 22.39 ?  160 LEU   A HG   1 
ATOM   3310 H HG   B LEU   A 1 160 ? 8.494  -4.589  0.850   0.14 18.13 ?  160 LEU   A HG   1 
ATOM   3311 H HD11 A LEU   A 1 160 ? 8.661  -5.289  -1.618  0.86 22.96 ?  160 LEU   A HD11 1 
ATOM   3312 H HD11 B LEU   A 1 160 ? 8.560  -5.294  -1.401  0.14 18.20 ?  160 LEU   A HD11 1 
ATOM   3313 H HD12 A LEU   A 1 160 ? 7.180  -5.335  -1.051  0.86 22.96 ?  160 LEU   A HD12 1 
ATOM   3314 H HD12 B LEU   A 1 160 ? 7.091  -5.316  -0.802  0.14 18.20 ?  160 LEU   A HD12 1 
ATOM   3315 H HD13 A LEU   A 1 160 ? 7.641  -4.124  -1.972  0.86 22.96 ?  160 LEU   A HD13 1 
ATOM   3316 H HD13 B LEU   A 1 160 ? 7.541  -4.128  -1.758  0.14 18.20 ?  160 LEU   A HD13 1 
ATOM   3317 H HD21 A LEU   A 1 160 ? 10.349 -3.944  -0.596  0.86 22.66 ?  160 LEU   A HD21 1 
ATOM   3318 H HD21 B LEU   A 1 160 ? 10.280 -3.890  -0.453  0.14 18.18 ?  160 LEU   A HD21 1 
ATOM   3319 H HD22 A LEU   A 1 160 ? 9.563  -2.633  -1.027  0.86 22.66 ?  160 LEU   A HD22 1 
ATOM   3320 H HD22 B LEU   A 1 160 ? 9.465  -2.593  -0.876  0.14 18.18 ?  160 LEU   A HD22 1 
ATOM   3321 H HD23 A LEU   A 1 160 ? 9.977  -2.848  0.492   0.86 22.66 ?  160 LEU   A HD23 1 
ATOM   3322 H HD23 B LEU   A 1 160 ? 9.924  -2.786  0.633   0.14 18.18 ?  160 LEU   A HD23 1 
ATOM   3323 N N    A TYR   A 1 161 ? 6.319  -4.501  2.974   0.86 16.64 ?  161 TYR   A N    1 
ATOM   3324 N N    B TYR   A 1 161 ? 6.155  -4.449  3.236   0.14 14.48 ?  161 TYR   A N    1 
ATOM   3325 C CA   A TYR   A 1 161 ? 6.464  -5.553  3.973   0.86 16.33 ?  161 TYR   A CA   1 
ATOM   3326 C CA   B TYR   A 1 161 ? 6.366  -5.495  4.232   0.14 14.49 ?  161 TYR   A CA   1 
ATOM   3327 C C    A TYR   A 1 161 ? 5.315  -6.555  3.889   0.86 16.48 ?  161 TYR   A C    1 
ATOM   3328 C C    B TYR   A 1 161 ? 5.272  -6.555  4.169   0.14 14.97 ?  161 TYR   A C    1 
ATOM   3329 O O    A TYR   A 1 161 ? 5.528  -7.772  3.867   0.86 15.99 ?  161 TYR   A O    1 
ATOM   3330 O O    B TYR   A 1 161 ? 5.547  -7.750  4.323   0.14 14.73 ?  161 TYR   A O    1 
ATOM   3331 C CB   A TYR   A 1 161 ? 6.542  -4.933  5.368   0.86 16.63 ?  161 TYR   A CB   1 
ATOM   3332 C CB   B TYR   A 1 161 ? 6.447  -4.883  5.631   0.14 14.25 ?  161 TYR   A CB   1 
ATOM   3333 C CG   A TYR   A 1 161 ? 6.450  -5.965  6.456   0.86 16.11 ?  161 TYR   A CG   1 
ATOM   3334 C CG   B TYR   A 1 161 ? 6.409  -5.912  6.736   0.14 13.95 ?  161 TYR   A CG   1 
ATOM   3335 C CD1  A TYR   A 1 161 ? 7.580  -6.640  6.895   0.86 15.88 ?  161 TYR   A CD1  1 
ATOM   3336 C CD1  B TYR   A 1 161 ? 7.532  -6.666  7.050   0.14 13.87 ?  161 TYR   A CD1  1 
ATOM   3337 C CD2  A TYR   A 1 161 ? 5.226  -6.282  7.032   0.86 15.94 ?  161 TYR   A CD2  1 
ATOM   3338 C CD2  B TYR   A 1 161 ? 5.248  -6.131  7.464   0.14 13.80 ?  161 TYR   A CD2  1 
ATOM   3339 C CE1  A TYR   A 1 161 ? 7.495  -7.601  7.882   0.86 16.14 ?  161 TYR   A CE1  1 
ATOM   3340 C CE1  B TYR   A 1 161 ? 7.498  -7.611  8.057   0.14 13.89 ?  161 TYR   A CE1  1 
ATOM   3341 C CE2  A TYR   A 1 161 ? 5.129  -7.239  8.017   0.86 15.76 ?  161 TYR   A CE2  1 
ATOM   3342 C CE2  B TYR   A 1 161 ? 5.204  -7.073  8.474   0.14 13.86 ?  161 TYR   A CE2  1 
ATOM   3343 C CZ   A TYR   A 1 161 ? 6.266  -7.903  8.438   0.86 16.13 ?  161 TYR   A CZ   1 
ATOM   3344 C CZ   B TYR   A 1 161 ? 6.332  -7.811  8.766   0.14 14.04 ?  161 TYR   A CZ   1 
ATOM   3345 O OH   A TYR   A 1 161 ? 6.189  -8.867  9.423   0.86 17.08 ?  161 TYR   A OH   1 
ATOM   3346 O OH   B TYR   A 1 161 ? 6.294  -8.751  9.772   0.14 14.37 ?  161 TYR   A OH   1 
ATOM   3347 H H    A TYR   A 1 161 ? 6.346  -3.702  3.291   0.86 19.97 ?  161 TYR   A H    1 
ATOM   3348 H H    B TYR   A 1 161 ? 6.082  -3.655  3.557   0.14 17.39 ?  161 TYR   A H    1 
ATOM   3349 H HA   A TYR   A 1 161 ? 7.294  -6.031  3.815   0.86 19.61 ?  161 TYR   A HA   1 
ATOM   3350 H HA   B TYR   A 1 161 ? 7.212  -5.932  4.052   0.14 17.39 ?  161 TYR   A HA   1 
ATOM   3351 H HB2  A TYR   A 1 161 ? 7.389  -4.473  5.467   0.86 19.96 ?  161 TYR   A HB2  1 
ATOM   3352 H HB2  B TYR   A 1 161 ? 7.280  -4.391  5.712   0.14 17.11 ?  161 TYR   A HB2  1 
ATOM   3353 H HB3  A TYR   A 1 161 ? 5.807  -4.313  5.483   0.86 19.96 ?  161 TYR   A HB3  1 
ATOM   3354 H HB3  B TYR   A 1 161 ? 5.697  -4.283  5.757   0.14 17.11 ?  161 TYR   A HB3  1 
ATOM   3355 H HD1  A TYR   A 1 161 ? 8.404  -6.445  6.519   0.86 19.06 ?  161 TYR   A HD1  1 
ATOM   3356 H HD1  B TYR   A 1 161 ? 8.319  -6.535  6.572   0.14 16.65 ?  161 TYR   A HD1  1 
ATOM   3357 H HD2  A TYR   A 1 161 ? 4.455  -5.847  6.749   0.86 19.14 ?  161 TYR   A HD2  1 
ATOM   3358 H HD2  B TYR   A 1 161 ? 4.485  -5.636  7.269   0.14 16.57 ?  161 TYR   A HD2  1 
ATOM   3359 H HE1  A TYR   A 1 161 ? 8.258  -8.050  8.170   0.86 19.37 ?  161 TYR   A HE1  1 
ATOM   3360 H HE1  B TYR   A 1 161 ? 8.257  -8.110  8.255   0.14 16.68 ?  161 TYR   A HE1  1 
ATOM   3361 H HE2  A TYR   A 1 161 ? 4.297  -7.446  8.396   0.86 18.92 ?  161 TYR   A HE2  1 
ATOM   3362 H HE2  B TYR   A 1 161 ? 4.418  -7.209  8.953   0.14 16.65 ?  161 TYR   A HE2  1 
ATOM   3363 H HH   A TYR   A 1 161 ? 5.383  -8.958  9.679   0.86 20.51 ?  161 TYR   A HH   1 
ATOM   3364 H HH   B TYR   A 1 161 ? 5.527  -8.769  10.118  0.14 17.26 ?  161 TYR   A HH   1 
ATOM   3365 N N    A ASP   A 1 162 ? 4.082  -6.055  3.842   0.86 17.23 ?  162 ASP   A N    1 
ATOM   3366 N N    B ASP   A 1 162 ? 4.023  -6.140  3.942   0.14 15.81 ?  162 ASP   A N    1 
ATOM   3367 C CA   A ASP   A 1 162 ? 2.929  -6.950  3.783   0.86 18.09 ?  162 ASP   A CA   1 
ATOM   3368 C CA   B ASP   A 1 162 ? 2.929  -7.106  3.886   0.14 16.63 ?  162 ASP   A CA   1 
ATOM   3369 C C    A ASP   A 1 162 ? 2.961  -7.800  2.519   0.86 18.05 ?  162 ASP   A C    1 
ATOM   3370 C C    B ASP   A 1 162 ? 2.980  -7.948  2.617   0.14 17.09 ?  162 ASP   A C    1 
ATOM   3371 O O    A ASP   A 1 162 ? 2.623  -8.991  2.551   0.86 18.74 ?  162 ASP   A O    1 
ATOM   3372 O O    B ASP   A 1 162 ? 2.583  -9.118  2.638   0.14 17.02 ?  162 ASP   A O    1 
ATOM   3373 C CB   A ASP   A 1 162 ? 1.628  -6.146  3.856   0.86 19.18 ?  162 ASP   A CB   1 
ATOM   3374 C CB   B ASP   A 1 162 ? 1.581  -6.392  3.999   0.14 16.99 ?  162 ASP   A CB   1 
ATOM   3375 C CG   A ASP   A 1 162 ? 1.332  -5.614  5.247   0.86 20.88 ?  162 ASP   A CG   1 
ATOM   3376 C CG   B ASP   A 1 162 ? 1.374  -5.749  5.355   0.14 17.47 ?  162 ASP   A CG   1 
ATOM   3377 O OD1  A ASP   A 1 162 ? 1.986  -6.037  6.218   0.86 22.04 ?  162 ASP   A OD1  1 
ATOM   3378 O OD1  B ASP   A 1 162 ? 2.053  -6.157  6.320   0.14 17.75 ?  162 ASP   A OD1  1 
ATOM   3379 O OD2  A ASP   A 1 162 ? 0.416  -4.769  5.368   0.86 22.29 -1 162 ASP   A OD2  1 
ATOM   3380 O OD2  B ASP   A 1 162 ? 0.524  -4.839  5.457   0.14 17.81 -1 162 ASP   A OD2  1 
ATOM   3381 H H    A ASP   A 1 162 ? 3.889  -5.221  3.844   0.86 20.69 ?  162 ASP   A H    1 
ATOM   3382 H H    B ASP   A 1 162 ? 3.788  -5.322  3.823   0.14 18.99 ?  162 ASP   A H    1 
ATOM   3383 H HA   A ASP   A 1 162 ? 2.953  -7.555  4.538   0.86 21.72 ?  162 ASP   A HA   1 
ATOM   3384 H HA   B ASP   A 1 162 ? 3.007  -7.710  4.639   0.14 19.96 ?  162 ASP   A HA   1 
ATOM   3385 H HB2  A ASP   A 1 162 ? 1.693  -5.388  3.260   0.86 23.03 ?  162 ASP   A HB2  1 
ATOM   3386 H HB2  B ASP   A 1 162 ? 1.532  -5.695  3.328   0.14 20.40 ?  162 ASP   A HB2  1 
ATOM   3387 H HB3  A ASP   A 1 162 ? 0.890  -6.717  3.598   0.86 23.03 ?  162 ASP   A HB3  1 
ATOM   3388 H HB3  B ASP   A 1 162 ? 0.868  -7.037  3.861   0.14 20.40 ?  162 ASP   A HB3  1 
ATOM   3389 N N    A LYS   A 1 163 ? 3.368  -7.207  1.393   0.86 19.08 ?  163 LYS   A N    1 
ATOM   3390 N N    B LYS   A 1 163 ? 3.461  -7.379  1.509   0.14 17.72 ?  163 LYS   A N    1 
ATOM   3391 C CA   A LYS   A 1 163 ? 3.463  -7.975  0.156   0.86 19.54 ?  163 LYS   A CA   1 
ATOM   3392 C CA   B LYS   A 1 163 ? 3.529  -8.138  0.265   0.14 18.29 ?  163 LYS   A CA   1 
ATOM   3393 C C    A LYS   A 1 163 ? 4.557  -9.032  0.245   0.86 18.61 ?  163 LYS   A C    1 
ATOM   3394 C C    B LYS   A 1 163 ? 4.642  -9.180  0.314   0.14 17.50 ?  163 LYS   A C    1 
ATOM   3395 O O    A LYS   A 1 163 ? 4.397  -10.140 -0.278  0.86 19.39 ?  163 LYS   A O    1 
ATOM   3396 O O    B LYS   A 1 163 ? 4.482  -10.291 -0.204  0.14 17.76 ?  163 LYS   A O    1 
ATOM   3397 C CB   A LYS   A 1 163 ? 3.707  -7.047  -1.034  0.86 21.95 ?  163 LYS   A CB   1 
ATOM   3398 C CB   B LYS   A 1 163 ? 3.722  -7.187  -0.917  0.14 19.71 ?  163 LYS   A CB   1 
ATOM   3399 C CG   A LYS   A 1 163 ? 3.773  -7.773  -2.373  0.86 24.79 ?  163 LYS   A CG   1 
ATOM   3400 C CG   B LYS   A 1 163 ? 3.711  -7.873  -2.273  0.14 21.04 ?  163 LYS   A CG   1 
ATOM   3401 C CD   A LYS   A 1 163 ? 4.129  -6.825  -3.506  0.86 27.45 ?  163 LYS   A CD   1 
ATOM   3402 C CD   B LYS   A 1 163 ? 3.706  -6.859  -3.406  0.14 22.15 ?  163 LYS   A CD   1 
ATOM   3403 C CE   A LYS   A 1 163 ? 4.015  -7.512  -4.858  0.86 29.40 ?  163 LYS   A CE   1 
ATOM   3404 C CE   B LYS   A 1 163 ? 3.618  -7.543  -4.761  0.14 22.97 ?  163 LYS   A CE   1 
ATOM   3405 N NZ   A LYS   A 1 163 ? 4.623  -6.705  -5.953  0.86 30.32 ?  163 LYS   A NZ   1 
ATOM   3406 N NZ   B LYS   A 1 163 ? 3.714  -6.572  -5.885  0.14 23.36 ?  163 LYS   A NZ   1 
ATOM   3407 H H    A LYS   A 1 163 ? 3.587  -6.372  1.320   0.86 22.91 ?  163 LYS   A H    1 
ATOM   3408 H H    B LYS   A 1 163 ? 3.746  -6.569  1.453   0.14 21.27 ?  163 LYS   A H    1 
ATOM   3409 H HA   A LYS   A 1 163 ? 2.617  -8.425  0.007   0.86 23.45 ?  163 LYS   A HA   1 
ATOM   3410 H HA   B LYS   A 1 163 ? 2.690  -8.604  0.134   0.14 21.96 ?  163 LYS   A HA   1 
ATOM   3411 H HB2  A LYS   A 1 163 ? 2.980  -6.400  -1.088  0.86 26.35 ?  163 LYS   A HB2  1 
ATOM   3412 H HB2  B LYS   A 1 163 ? 3.005  -6.533  -0.913  0.14 23.66 ?  163 LYS   A HB2  1 
ATOM   3413 H HB3  A LYS   A 1 163 ? 4.546  -6.582  -0.909  0.86 26.35 ?  163 LYS   A HB3  1 
ATOM   3414 H HB3  B LYS   A 1 163 ? 4.576  -6.738  -0.822  0.14 23.66 ?  163 LYS   A HB3  1 
ATOM   3415 H HG2  A LYS   A 1 163 ? 4.452  -8.462  -2.336  0.86 29.76 ?  163 LYS   A HG2  1 
ATOM   3416 H HG2  B LYS   A 1 163 ? 4.505  -8.423  -2.362  0.14 25.26 ?  163 LYS   A HG2  1 
ATOM   3417 H HG3  A LYS   A 1 163 ? 2.906  -8.167  -2.568  0.86 29.76 ?  163 LYS   A HG3  1 
ATOM   3418 H HG3  B LYS   A 1 163 ? 2.913  -8.419  -2.351  0.14 25.26 ?  163 LYS   A HG3  1 
ATOM   3419 H HD2  A LYS   A 1 163 ? 3.518  -6.071  -3.498  0.86 32.95 ?  163 LYS   A HD2  1 
ATOM   3420 H HD2  B LYS   A 1 163 ? 2.937  -6.274  -3.310  0.14 26.59 ?  163 LYS   A HD2  1 
ATOM   3421 H HD3  A LYS   A 1 163 ? 5.042  -6.520  -3.394  0.86 32.95 ?  163 LYS   A HD3  1 
ATOM   3422 H HD3  B LYS   A 1 163 ? 4.526  -6.341  -3.377  0.14 26.59 ?  163 LYS   A HD3  1 
ATOM   3423 H HE2  A LYS   A 1 163 ? 4.462  -8.371  -4.821  0.86 35.29 ?  163 LYS   A HE2  1 
ATOM   3424 H HE2  B LYS   A 1 163 ? 4.339  -8.184  -4.849  0.14 27.57 ?  163 LYS   A HE2  1 
ATOM   3425 H HE3  A LYS   A 1 163 ? 3.079  -7.639  -5.069  0.86 35.29 ?  163 LYS   A HE3  1 
ATOM   3426 H HE3  B LYS   A 1 163 ? 2.765  -7.996  -4.828  0.14 27.57 ?  163 LYS   A HE3  1 
ATOM   3427 H HZ1  A LYS   A 1 163 ? 4.542  -7.133  -6.729  0.86 36.39 ?  163 LYS   A HZ1  1 
ATOM   3428 H HZ1  B LYS   A 1 163 ? 3.661  -7.003  -6.662  0.14 28.04 ?  163 LYS   A HZ1  1 
ATOM   3429 H HZ2  A LYS   A 1 163 ? 4.211  -5.918  -6.013  0.86 36.39 ?  163 LYS   A HZ2  1 
ATOM   3430 H HZ2  B LYS   A 1 163 ? 3.049  -5.983  -5.834  0.14 28.04 ?  163 LYS   A HZ2  1 
ATOM   3431 H HZ3  A LYS   A 1 163 ? 5.486  -6.566  -5.787  0.86 36.39 ?  163 LYS   A HZ3  1 
ATOM   3432 H HZ3  B LYS   A 1 163 ? 4.490  -6.138  -5.847  0.14 28.04 ?  163 LYS   A HZ3  1 
ATOM   3433 N N    A LEU   A 1 164 ? 5.680  -8.703  0.891   0.86 16.84 ?  164 LEU   A N    1 
ATOM   3434 N N    B LEU   A 1 164 ? 5.774  -8.840  0.934   0.14 16.42 ?  164 LEU   A N    1 
ATOM   3435 C CA   A LEU   A 1 164 ? 6.772  -9.666  1.028   0.86 16.06 ?  164 LEU   A CA   1 
ATOM   3436 C CA   B LEU   A 1 164 ? 6.868  -9.798  1.059   0.14 15.47 ?  164 LEU   A CA   1 
ATOM   3437 C C    A LEU   A 1 164 ? 6.353  -10.860 1.875   0.86 16.00 ?  164 LEU   A C    1 
ATOM   3438 C C    B LEU   A 1 164 ? 6.449  -11.002 1.891   0.14 14.93 ?  164 LEU   A C    1 
ATOM   3439 O O    A LEU   A 1 164 ? 6.650  -12.011 1.530   0.86 16.25 ?  164 LEU   A O    1 
ATOM   3440 O O    B LEU   A 1 164 ? 6.844  -12.138 1.601   0.14 14.79 ?  164 LEU   A O    1 
ATOM   3441 C CB   A LEU   A 1 164 ? 7.982  -8.980  1.653   0.86 15.35 ?  164 LEU   A CB   1 
ATOM   3442 C CB   B LEU   A 1 164 ? 8.082  -9.115  1.690   0.14 15.14 ?  164 LEU   A CB   1 
ATOM   3443 C CG   A LEU   A 1 164 ? 8.749  -8.027  0.736   0.86 15.58 ?  164 LEU   A CG   1 
ATOM   3444 C CG   B LEU   A 1 164 ? 8.748  -8.010  0.868   0.14 15.00 ?  164 LEU   A CG   1 
ATOM   3445 C CD1  A LEU   A 1 164 ? 9.664  -7.133  1.556   0.86 15.46 ?  164 LEU   A CD1  1 
ATOM   3446 C CD1  B LEU   A 1 164 ? 9.665  -7.166  1.741   0.14 14.92 ?  164 LEU   A CD1  1 
ATOM   3447 C CD2  A LEU   A 1 164 ? 9.540  -8.783  -0.326  0.86 16.18 ?  164 LEU   A CD2  1 
ATOM   3448 C CD2  B LEU   A 1 164 ? 9.520  -8.609  -0.293  0.14 15.01 ?  164 LEU   A CD2  1 
ATOM   3449 H H    A LEU   A 1 164 ? 5.828  -7.934  1.254   0.86 20.22 ?  164 LEU   A H    1 
ATOM   3450 H H    B LEU   A 1 164 ? 5.929  -8.073  1.286   0.14 19.71 ?  164 LEU   A H    1 
ATOM   3451 H HA   A LEU   A 1 164 ? 7.019  -9.985  0.149   0.86 19.29 ?  164 LEU   A HA   1 
ATOM   3452 H HA   B LEU   A 1 164 ? 7.120  -10.116 0.180   0.14 18.58 ?  164 LEU   A HA   1 
ATOM   3453 H HB2  A LEU   A 1 164 ? 7.683  -8.462  2.418   0.86 18.42 ?  164 LEU   A HB2  1 
ATOM   3454 H HB2  B LEU   A 1 164 ? 7.805  -8.719  2.530   0.14 18.18 ?  164 LEU   A HB2  1 
ATOM   3455 H HB3  A LEU   A 1 164 ? 8.602  -9.661  1.944   0.86 18.42 ?  164 LEU   A HB3  1 
ATOM   3456 H HB3  B LEU   A 1 164 ? 8.756  -9.790  1.860   0.14 18.18 ?  164 LEU   A HB3  1 
ATOM   3457 H HG   A LEU   A 1 164 ? 8.116  -7.453  0.279   0.86 18.70 ?  164 LEU   A HG   1 
ATOM   3458 H HG   B LEU   A 1 164 ? 8.063  -7.428  0.505   0.14 18.01 ?  164 LEU   A HG   1 
ATOM   3459 H HD11 A LEU   A 1 164 ? 10.152 -6.540  0.959   0.86 18.56 ?  164 LEU   A HD11 1 
ATOM   3460 H HD11 B LEU   A 1 164 ? 10.077 -6.478  1.194   0.14 17.91 ?  164 LEU   A HD11 1 
ATOM   3461 H HD12 A LEU   A 1 164 ? 9.130  -6.608  2.173   0.86 18.56 ?  164 LEU   A HD12 1 
ATOM   3462 H HD12 B LEU   A 1 164 ? 9.141  -6.756  2.447   0.14 17.91 ?  164 LEU   A HD12 1 
ATOM   3463 H HD13 A LEU   A 1 164 ? 10.291 -7.685  2.052   0.86 18.56 ?  164 LEU   A HD13 1 
ATOM   3464 H HD13 B LEU   A 1 164 ? 10.350 -7.736  2.125   0.14 17.91 ?  164 LEU   A HD13 1 
ATOM   3465 H HD21 A LEU   A 1 164 ? 10.053 -8.146  -0.853  0.86 19.42 ?  164 LEU   A HD21 1 
ATOM   3466 H HD21 B LEU   A 1 164 ? 9.939  -7.894  -0.796  0.14 18.02 ?  164 LEU   A HD21 1 
ATOM   3467 H HD22 A LEU   A 1 164 ? 10.141 -9.408  0.109   0.86 19.42 ?  164 LEU   A HD22 1 
ATOM   3468 H HD22 B LEU   A 1 164 ? 10.199 -9.209  0.055   0.14 18.02 ?  164 LEU   A HD22 1 
ATOM   3469 H HD23 A LEU   A 1 164 ? 8.923  -9.261  -0.900  0.86 19.42 ?  164 LEU   A HD23 1 
ATOM   3470 H HD23 B LEU   A 1 164 ? 8.906  -9.098  -0.862  0.14 18.02 ?  164 LEU   A HD23 1 
ATOM   3471 N N    A VAL   A 1 165 ? 5.676  -10.601 2.993   0.86 15.78 ?  165 VAL   A N    1 
ATOM   3472 N N    B VAL   A 1 165 ? 5.651  -10.772 2.935   0.14 14.59 ?  165 VAL   A N    1 
ATOM   3473 C CA   A VAL   A 1 165 ? 5.201  -11.685 3.847   0.86 15.60 ?  165 VAL   A CA   1 
ATOM   3474 C CA   B VAL   A 1 165 ? 5.190  -11.871 3.777   0.14 14.26 ?  165 VAL   A CA   1 
ATOM   3475 C C    A VAL   A 1 165 ? 4.164  -12.525 3.110   0.86 15.47 ?  165 VAL   A C    1 
ATOM   3476 C C    B VAL   A 1 165 ? 4.158  -12.713 3.036   0.14 14.15 ?  165 VAL   A C    1 
ATOM   3477 O O    A VAL   A 1 165 ? 4.258  -13.758 3.053   0.86 15.37 ?  165 VAL   A O    1 
ATOM   3478 O O    B VAL   A 1 165 ? 4.240  -13.946 3.012   0.14 13.91 ?  165 VAL   A O    1 
ATOM   3479 C CB   A VAL   A 1 165 ? 4.639  -11.112 5.161   0.86 16.25 ?  165 VAL   A CB   1 
ATOM   3480 C CB   B VAL   A 1 165 ? 4.636  -11.324 5.106   0.14 14.15 ?  165 VAL   A CB   1 
ATOM   3481 C CG1  A VAL   A 1 165 ? 3.899  -12.185 5.949   0.86 16.40 ?  165 VAL   A CG1  1 
ATOM   3482 C CG1  B VAL   A 1 165 ? 4.012  -12.443 5.926   0.14 14.11 ?  165 VAL   A CG1  1 
ATOM   3483 C CG2  A VAL   A 1 165 ? 5.753  -10.487 5.994   0.86 16.89 ?  165 VAL   A CG2  1 
ATOM   3484 C CG2  B VAL   A 1 165 ? 5.737  -10.623 5.893   0.14 14.26 ?  165 VAL   A CG2  1 
ATOM   3485 H H    A VAL   A 1 165 ? 5.488  -9.812  3.284   0.86 18.95 ?  165 VAL   A H    1 
ATOM   3486 H H    B VAL   A 1 165 ? 5.369  -9.996  3.175   0.14 17.52 ?  165 VAL   A H    1 
ATOM   3487 H HA   A VAL   A 1 165 ? 5.948  -12.261 4.073   0.86 18.73 ?  165 VAL   A HA   1 
ATOM   3488 H HA   B VAL   A 1 165 ? 5.945  -12.442 3.989   0.14 17.12 ?  165 VAL   A HA   1 
ATOM   3489 H HB   A VAL   A 1 165 ? 4.005  -10.409 4.950   0.86 19.51 ?  165 VAL   A HB   1 
ATOM   3490 H HB   B VAL   A 1 165 ? 3.945  -10.671 4.916   0.14 16.99 ?  165 VAL   A HB   1 
ATOM   3491 H HG11 A VAL   A 1 165 ? 3.798  -11.885 6.867   0.86 19.69 ?  165 VAL   A HG11 1 
ATOM   3492 H HG11 B VAL   A 1 165 ? 3.898  -12.137 6.839   0.14 16.94 ?  165 VAL   A HG11 1 
ATOM   3493 H HG12 A VAL   A 1 165 ? 3.024  -12.321 5.551   0.86 19.69 ?  165 VAL   A HG12 1 
ATOM   3494 H HG12 B VAL   A 1 165 ? 3.150  -12.672 5.544   0.14 16.94 ?  165 VAL   A HG12 1 
ATOM   3495 H HG13 A VAL   A 1 165 ? 4.411  -13.005 5.923   0.86 19.69 ?  165 VAL   A HG13 1 
ATOM   3496 H HG13 B VAL   A 1 165 ? 4.601  -13.213 5.906   0.14 16.94 ?  165 VAL   A HG13 1 
ATOM   3497 H HG21 A VAL   A 1 165 ? 5.379  -10.137 6.819   0.86 20.28 ?  165 VAL   A HG21 1 
ATOM   3498 H HG21 B VAL   A 1 165 ? 5.361  -10.266 6.713   0.14 17.13 ?  165 VAL   A HG21 1 
ATOM   3499 H HG22 A VAL   A 1 165 ? 6.420  -11.161 6.194   0.86 20.28 ?  165 VAL   A HG22 1 
ATOM   3500 H HG22 B VAL   A 1 165 ? 6.434  -11.264 6.101   0.14 17.13 ?  165 VAL   A HG22 1 
ATOM   3501 H HG23 A VAL   A 1 165 ? 6.161  -9.762  5.488   0.86 20.28 ?  165 VAL   A HG23 1 
ATOM   3502 H HG23 B VAL   A 1 165 ? 6.100  -9.902  5.355   0.14 17.13 ?  165 VAL   A HG23 1 
ATOM   3503 N N    A SER   A 1 166 ? 3.158  -11.865 2.529   0.86 16.18 ?  166 SER   A N    1 
ATOM   3504 N N    B SER   A 1 166 ? 3.177  -12.058 2.409   0.14 14.53 ?  166 SER   A N    1 
ATOM   3505 C CA   A SER   A 1 166 ? 2.027  -12.594 1.962   0.86 17.10 ?  166 SER   A CA   1 
ATOM   3506 C CA   B SER   A 1 166 ? 2.071  -12.784 1.793   0.14 14.97 ?  166 SER   A CA   1 
ATOM   3507 C C    A SER   A 1 166 ? 2.426  -13.424 0.752   0.86 17.69 ?  166 SER   A C    1 
ATOM   3508 C C    B SER   A 1 166 ? 2.539  -13.684 0.656   0.14 15.49 ?  166 SER   A C    1 
ATOM   3509 O O    A SER   A 1 166 ? 1.758  -14.420 0.442   0.86 19.93 ?  166 SER   A O    1 
ATOM   3510 O O    B SER   A 1 166 ? 1.946  -14.744 0.423   0.14 15.88 ?  166 SER   A O    1 
ATOM   3511 C CB   A SER   A 1 166 ? 0.908  -11.627 1.574   0.86 18.76 ?  166 SER   A CB   1 
ATOM   3512 C CB   B SER   A 1 166 ? 1.009  -11.802 1.292   0.14 14.97 ?  166 SER   A CB   1 
ATOM   3513 O OG   A SER   A 1 166 ? 0.309  -11.039 2.715   0.86 21.03 ?  166 SER   A OG   1 
ATOM   3514 O OG   B SER   A 1 166 ? 0.155  -11.387 2.343   0.14 15.02 ?  166 SER   A OG   1 
ATOM   3515 H H    A SER   A 1 166 ? 3.105  -11.012 2.460   0.86 19.42 ?  166 SER   A H    1 
ATOM   3516 H H    B SER   A 1 166 ? 3.135  -11.205 2.328   0.14 17.45 ?  166 SER   A H    1 
ATOM   3517 H HA   A SER   A 1 166 ? 1.674  -13.201 2.631   0.86 20.53 ?  166 SER   A HA   1 
ATOM   3518 H HA   B SER   A 1 166 ? 1.658  -13.348 2.460   0.14 17.97 ?  166 SER   A HA   1 
ATOM   3519 H HB2  A SER   A 1 166 ? 1.275  -10.934 1.003   0.86 22.53 ?  166 SER   A HB2  1 
ATOM   3520 H HB2  B SER   A 1 166 ? 1.449  -11.020 0.925   0.14 17.98 ?  166 SER   A HB2  1 
ATOM   3521 H HB3  A SER   A 1 166 ? 0.220  -12.118 1.096   0.86 22.53 ?  166 SER   A HB3  1 
ATOM   3522 H HB3  B SER   A 1 166 ? 0.476  -12.234 0.608   0.14 17.98 ?  166 SER   A HB3  1 
ATOM   3523 H HG   A SER   A 1 166 ? -0.284 -10.495 2.479   0.86 25.25 ?  166 SER   A HG   1 
ATOM   3524 H HG   B SER   A 1 166 ? 0.600  -11.013 2.949   0.14 18.03 ?  166 SER   A HG   1 
ATOM   3525 N N    A SER   A 1 167 ? 3.489  -13.031 0.050   0.86 17.25 ?  167 SER   A N    1 
ATOM   3526 N N    B SER   A 1 167 ? 3.597  -13.292 -0.053  0.14 15.68 ?  167 SER   A N    1 
ATOM   3527 C CA   A SER   A 1 167 ? 3.939  -13.741 -1.138  0.86 18.21 ?  167 SER   A CA   1 
ATOM   3528 C CA   B SER   A 1 167 ? 4.048  -14.003 -1.241  0.14 16.12 ?  167 SER   A CA   1 
ATOM   3529 C C    A SER   A 1 167 ? 5.085  -14.708 -0.861  0.86 17.72 ?  167 SER   A C    1 
ATOM   3530 C C    B SER   A 1 167 ? 5.274  -14.870 -0.981  0.14 16.41 ?  167 SER   A C    1 
ATOM   3531 O O    A SER   A 1 167 ? 5.564  -15.356 -1.796  0.86 18.82 ?  167 SER   A O    1 
ATOM   3532 O O    B SER   A 1 167 ? 5.944  -15.283 -1.934  0.14 16.41 ?  167 SER   A O    1 
ATOM   3533 C CB   A SER   A 1 167 ? 4.345  -12.743 -2.235  0.86 19.29 ?  167 SER   A CB   1 
ATOM   3534 C CB   B SER   A 1 167 ? 4.328  -13.021 -2.378  0.14 16.27 ?  167 SER   A CB   1 
ATOM   3535 O OG   A SER   A 1 167 ? 5.422  -11.914 -1.816  0.86 19.33 ?  167 SER   A OG   1 
ATOM   3536 O OG   B SER   A 1 167 ? 5.429  -12.183 -2.071  0.14 16.24 ?  167 SER   A OG   1 
ATOM   3537 H H    A SER   A 1 167 ? 3.970  -12.340 0.247   0.86 20.71 ?  167 SER   A H    1 
ATOM   3538 H H    B SER   A 1 167 ? 4.082  -12.612 0.146   0.14 18.83 ?  167 SER   A H    1 
ATOM   3539 H HA   A SER   A 1 167 ? 3.196  -14.256 -1.482  0.86 21.86 ?  167 SER   A HA   1 
ATOM   3540 H HA   B SER   A 1 167 ? 3.332  -14.580 -1.538  0.14 19.36 ?  167 SER   A HA   1 
ATOM   3541 H HB2  A SER   A 1 167 ? 4.622  -13.239 -3.022  0.86 23.16 ?  167 SER   A HB2  1 
ATOM   3542 H HB2  B SER   A 1 167 ? 4.529  -13.525 -3.183  0.14 19.53 ?  167 SER   A HB2  1 
ATOM   3543 H HB3  A SER   A 1 167 ? 3.576  -12.187 -2.456  0.86 23.16 ?  167 SER   A HB3  1 
ATOM   3544 H HB3  B SER   A 1 167 ? 3.541  -12.473 -2.520  0.14 19.53 ?  167 SER   A HB3  1 
ATOM   3545 H HG   A SER   A 1 167 ? 5.185  -11.461 -1.145  0.86 23.20 ?  167 SER   A HG   1 
ATOM   3546 H HG   B SER   A 1 167 ? 5.266  -11.740 -1.376  0.14 19.50 ?  167 SER   A HG   1 
ATOM   3547 N N    A PHE   A 1 168 ? 5.518  -14.841 0.390   0.86 16.76 ?  168 PHE   A N    1 
ATOM   3548 N N    B PHE   A 1 168 ? 5.584  -15.158 0.281   0.14 16.83 ?  168 PHE   A N    1 
ATOM   3549 C CA   A PHE   A 1 168 ? 6.705  -15.638 0.677   0.86 16.83 ?  168 PHE   A CA   1 
ATOM   3550 C CA   B PHE   A 1 168 ? 6.764  -15.944 0.608   0.14 17.44 ?  168 PHE   A CA   1 
ATOM   3551 C C    A PHE   A 1 168 ? 6.402  -17.124 0.566   0.86 18.78 ?  168 PHE   A C    1 
ATOM   3552 C C    B PHE   A 1 168 ? 6.431  -17.429 0.636   0.14 18.90 ?  168 PHE   A C    1 
ATOM   3553 O O    A PHE   A 1 168 ? 5.463  -17.630 1.191   0.86 20.21 ?  168 PHE   A O    1 
ATOM   3554 O O    B PHE   A 1 168 ? 5.376  -17.836 1.131   0.14 19.26 ?  168 PHE   A O    1 
ATOM   3555 C CB   A PHE   A 1 168 ? 7.234  -15.349 2.075   0.86 15.71 ?  168 PHE   A CB   1 
ATOM   3556 C CB   B PHE   A 1 168 ? 7.350  -15.530 1.958   0.14 16.83 ?  168 PHE   A CB   1 
ATOM   3557 C CG   A PHE   A 1 168 ? 8.496  -16.093 2.381   0.86 15.04 ?  168 PHE   A CG   1 
ATOM   3558 C CG   B PHE   A 1 168 ? 8.591  -16.291 2.329   0.14 16.28 ?  168 PHE   A CG   1 
ATOM   3559 C CD1  A PHE   A 1 168 ? 9.677  -15.718 1.774   0.86 15.68 ?  168 PHE   A CD1  1 
ATOM   3560 C CD1  B PHE   A 1 168 ? 9.810  -15.970 1.756   0.14 16.22 ?  168 PHE   A CD1  1 
ATOM   3561 C CD2  A PHE   A 1 168 ? 8.509  -17.185 3.236   0.86 14.72 ?  168 PHE   A CD2  1 
ATOM   3562 C CD2  B PHE   A 1 168 ? 8.538  -17.337 3.236   0.14 15.96 ?  168 PHE   A CD2  1 
ATOM   3563 C CE1  A PHE   A 1 168 ? 10.851 -16.397 2.027   0.86 15.37 ?  168 PHE   A CE1  1 
ATOM   3564 C CE1  B PHE   A 1 168 ? 10.953 -16.671 2.086   0.14 16.10 ?  168 PHE   A CE1  1 
ATOM   3565 C CE2  A PHE   A 1 168 ? 9.691  -17.866 3.494   0.86 14.83 ?  168 PHE   A CE2  1 
ATOM   3566 C CE2  B PHE   A 1 168 ? 9.681  -18.041 3.571   0.14 15.91 ?  168 PHE   A CE2  1 
ATOM   3567 C CZ   A PHE   A 1 168 ? 10.858 -17.470 2.885   0.86 15.14 ?  168 PHE   A CZ   1 
ATOM   3568 C CZ   B PHE   A 1 168 ? 10.889 -17.707 2.995   0.14 16.01 ?  168 PHE   A CZ   1 
ATOM   3569 H H    A PHE   A 1 168 ? 5.148  -14.481 1.080   0.86 20.12 ?  168 PHE   A H    1 
ATOM   3570 H H    B PHE   A 1 168 ? 5.127  -14.908 0.965   0.14 20.21 ?  168 PHE   A H    1 
ATOM   3571 H HA   A PHE   A 1 168 ? 7.397  -15.416 0.035   0.86 20.20 ?  168 PHE   A HA   1 
ATOM   3572 H HA   B PHE   A 1 168 ? 7.439  -15.802 -0.070  0.14 20.94 ?  168 PHE   A HA   1 
ATOM   3573 H HB2  A PHE   A 1 168 ? 7.420  -14.399 2.151   0.86 18.86 ?  168 PHE   A HB2  1 
ATOM   3574 H HB2  B PHE   A 1 168 ? 7.578  -14.588 1.923   0.14 20.21 ?  168 PHE   A HB2  1 
ATOM   3575 H HB3  A PHE   A 1 168 ? 6.565  -15.610 2.725   0.86 18.86 ?  168 PHE   A HB3  1 
ATOM   3576 H HB3  B PHE   A 1 168 ? 6.688  -15.684 2.650   0.14 20.21 ?  168 PHE   A HB3  1 
ATOM   3577 H HD1  A PHE   A 1 168 ? 9.688  -14.992 1.193   0.86 18.83 ?  168 PHE   A HD1  1 
ATOM   3578 H HD1  B PHE   A 1 168 ? 9.860  -15.272 1.143   0.14 19.48 ?  168 PHE   A HD1  1 
ATOM   3579 H HD2  A PHE   A 1 168 ? 7.719  -17.455 3.648   0.86 17.68 ?  168 PHE   A HD2  1 
ATOM   3580 H HD2  B PHE   A 1 168 ? 7.727  -17.566 3.627   0.14 19.16 ?  168 PHE   A HD2  1 
ATOM   3581 H HE1  A PHE   A 1 168 ? 11.647 -16.129 1.620   0.86 18.45 ?  168 PHE   A HE1  1 
ATOM   3582 H HE1  B PHE   A 1 168 ? 11.767 -16.443 1.697   0.14 19.33 ?  168 PHE   A HE1  1 
ATOM   3583 H HE2  A PHE   A 1 168 ? 9.685  -18.595 4.075   0.86 17.81 ?  168 PHE   A HE2  1 
ATOM   3584 H HE2  B PHE   A 1 168 ? 9.634  -18.740 4.183   0.14 19.10 ?  168 PHE   A HE2  1 
ATOM   3585 H HZ   A PHE   A 1 168 ? 11.650 -17.929 3.060   0.86 18.18 ?  168 PHE   A HZ   1 
ATOM   3586 H HZ   B PHE   A 1 168 ? 11.659 -18.180 3.218   0.14 19.22 ?  168 PHE   A HZ   1 
ATOM   3587 N N    A LEU   A 1 169 ? 7.223  -17.828 -0.208  0.86 21.76 ?  169 LEU   A N    1 
ATOM   3588 N N    B LEU   A 1 169 ? 7.346  -18.232 0.104   0.14 20.34 ?  169 LEU   A N    1 
ATOM   3589 C CA   A LEU   A 1 169 ? 7.052  -19.260 -0.370  0.86 26.29 ?  169 LEU   A CA   1 
ATOM   3590 C CA   B LEU   A 1 169 ? 7.195  -19.678 0.088   0.14 22.06 ?  169 LEU   A CA   1 
ATOM   3591 C C    A LEU   A 1 169 ? 7.932  -19.998 0.630   0.86 27.60 ?  169 LEU   A C    1 
ATOM   3592 C C    B LEU   A 1 169 ? 8.556  -20.314 0.362   0.14 22.61 ?  169 LEU   A C    1 
ATOM   3593 O O    A LEU   A 1 169 ? 7.447  -20.457 1.665   0.86 28.32 ?  169 LEU   A O    1 
ATOM   3594 O O    B LEU   A 1 169 ? 8.754  -20.996 1.369   0.14 22.78 ?  169 LEU   A O    1 
ATOM   3595 C CB   A LEU   A 1 169 ? 7.378  -19.682 -1.806  0.86 28.82 ?  169 LEU   A CB   1 
ATOM   3596 C CB   B LEU   A 1 169 ? 6.642  -20.139 -1.264  0.14 23.07 ?  169 LEU   A CB   1 
ATOM   3597 C CG   A LEU   A 1 169 ? 7.064  -21.136 -2.166  0.86 30.74 ?  169 LEU   A CG   1 
ATOM   3598 C CG   B LEU   A 1 169 ? 7.029  -21.541 -1.748  0.14 23.93 ?  169 LEU   A CG   1 
ATOM   3599 C CD1  A LEU   A 1 169 ? 5.644  -21.497 -1.758  0.86 31.45 ?  169 LEU   A CD1  1 
ATOM   3600 C CD1  B LEU   A 1 169 ? 5.801  -22.340 -2.132  0.14 24.22 ?  169 LEU   A CD1  1 
ATOM   3601 C CD2  A LEU   A 1 169 ? 7.266  -21.376 -3.656  0.86 31.28 ?  169 LEU   A CD2  1 
ATOM   3602 C CD2  B LEU   A 1 169 ? 7.993  -21.434 -2.921  0.14 24.21 ?  169 LEU   A CD2  1 
ATOM   3603 O OXT  A LEU   A 1 169 ? 9.140  -20.137 0.441   0.86 27.44 -1 169 LEU   A OXT  1 
ATOM   3604 O OXT  B LEU   A 1 169 ? 9.491  -20.157 -0.422  0.14 22.82 -1 169 LEU   A OXT  1 
ATOM   3605 H H    A LEU   A 1 169 ? 7.881  -17.495 -0.651  0.86 26.12 ?  169 LEU   A H    1 
ATOM   3606 H H    B LEU   A 1 169 ? 8.077  -17.959 -0.258  0.14 24.42 ?  169 LEU   A H    1 
ATOM   3607 H HA   A LEU   A 1 169 ? 6.133  -19.491 -0.181  0.86 31.55 ?  169 LEU   A HA   1 
ATOM   3608 H HA   B LEU   A 1 169 ? 6.565  -19.945 0.777   0.14 26.48 ?  169 LEU   A HA   1 
ATOM   3609 H HB2  A LEU   A 1 169 ? 6.868  -19.120 -2.412  0.86 34.59 ?  169 LEU   A HB2  1 
ATOM   3610 H HB2  B LEU   A 1 169 ? 5.672  -20.113 -1.216  0.14 27.70 ?  169 LEU   A HB2  1 
ATOM   3611 H HB3  A LEU   A 1 169 ? 8.325  -19.545 -1.961  0.86 34.59 ?  169 LEU   A HB3  1 
ATOM   3612 H HB3  B LEU   A 1 169 ? 6.942  -19.509 -1.939  0.14 27.70 ?  169 LEU   A HB3  1 
ATOM   3613 H HG   A LEU   A 1 169 ? 7.672  -21.721 -1.685  0.86 36.89 ?  169 LEU   A HG   1 
ATOM   3614 H HG   B LEU   A 1 169 ? 7.473  -22.034 -1.042  0.14 28.72 ?  169 LEU   A HG   1 
ATOM   3615 H HD11 A LEU   A 1 169 ? 5.392  -22.326 -2.191  0.86 37.75 ?  169 LEU   A HD11 1 
ATOM   3616 H HD11 B LEU   A 1 169 ? 6.083  -23.215 -2.440  0.14 29.07 ?  169 LEU   A HD11 1 
ATOM   3617 H HD12 A LEU   A 1 169 ? 5.609  -21.604 -0.794  0.86 37.75 ?  169 LEU   A HD12 1 
ATOM   3618 H HD12 B LEU   A 1 169 ? 5.230  -22.430 -1.353  0.14 29.07 ?  169 LEU   A HD12 1 
ATOM   3619 H HD13 A LEU   A 1 169 ? 5.046  -20.784 -2.034  0.86 37.75 ?  169 LEU   A HD13 1 
ATOM   3620 H HD13 B LEU   A 1 169 ? 5.330  -21.873 -2.837  0.14 29.07 ?  169 LEU   A HD13 1 
ATOM   3621 H HD21 A LEU   A 1 169 ? 7.069  -22.305 -3.856  0.86 37.54 ?  169 LEU   A HD21 1 
ATOM   3622 H HD21 B LEU   A 1 169 ? 8.251  -22.327 -3.196  0.14 29.07 ?  169 LEU   A HD21 1 
ATOM   3623 H HD22 A LEU   A 1 169 ? 6.666  -20.796 -4.152  0.86 37.54 ?  169 LEU   A HD22 1 
ATOM   3624 H HD22 B LEU   A 1 169 ? 7.548  -20.977 -3.653  0.14 29.07 ?  169 LEU   A HD22 1 
ATOM   3625 H HD23 A LEU   A 1 169 ? 8.186  -21.175 -3.886  0.86 37.54 ?  169 LEU   A HD23 1 
ATOM   3626 H HD23 B LEU   A 1 169 ? 8.777  -20.932 -2.646  0.14 29.07 ?  169 LEU   A HD23 1 
ATOM   3627 N N    A SER   B 1 1   ? 50.808 -9.221  -23.834 0.86 26.45 ?  1   SER   B N    1 
ATOM   3628 N N    B SER   B 1 1   ? 50.825 -9.236  -23.886 0.14 26.27 ?  1   SER   B N    1 
ATOM   3629 C CA   A SER   B 1 1   ? 51.257 -10.277 -22.908 0.86 25.97 ?  1   SER   B CA   1 
ATOM   3630 C CA   B SER   B 1 1   ? 51.277 -10.209 -22.869 0.14 26.20 ?  1   SER   B CA   1 
ATOM   3631 C C    A SER   B 1 1   ? 50.150 -11.291 -22.645 0.86 24.45 ?  1   SER   B C    1 
ATOM   3632 C C    B SER   B 1 1   ? 50.197 -11.255 -22.622 0.14 26.00 ?  1   SER   B C    1 
ATOM   3633 O O    A SER   B 1 1   ? 48.965 -11.091 -22.973 0.86 23.82 ?  1   SER   B O    1 
ATOM   3634 O O    B SER   B 1 1   ? 49.062 -11.115 -23.080 0.14 25.92 ?  1   SER   B O    1 
ATOM   3635 C CB   A SER   B 1 1   ? 51.733 -9.678  -21.585 0.86 26.81 ?  1   SER   B CB   1 
ATOM   3636 C CB   B SER   B 1 1   ? 51.634 -9.496  -21.568 0.14 26.28 ?  1   SER   B CB   1 
ATOM   3637 O OG   A SER   B 1 1   ? 50.635 -9.438  -20.725 0.86 28.78 ?  1   SER   B OG   1 
ATOM   3638 O OG   B SER   B 1 1   ? 50.558 -9.560  -20.650 0.14 26.55 ?  1   SER   B OG   1 
ATOM   3639 H H1   A SER   B 1 1   ? 50.677 -9.579  -24.635 0.86 31.74 ?  1   SER   B H1   1 
ATOM   3640 H H1   B SER   B 1 1   ? 51.533 -8.800  -24.199 0.14 31.53 ?  1   SER   B H1   1 
ATOM   3641 H H2   A SER   B 1 1   ? 50.054 -8.873  -23.527 0.86 31.74 ?  1   SER   B H2   1 
ATOM   3642 H H2   B SER   B 1 1   ? 50.424 -9.673  -24.546 0.14 31.53 ?  1   SER   B H2   1 
ATOM   3643 H H3   A SER   B 1 1   ? 51.436 -8.595  -23.881 0.86 31.74 ?  1   SER   B H3   1 
ATOM   3644 H H3   B SER   B 1 1   ? 50.260 -8.666  -23.511 0.14 31.53 ?  1   SER   B H3   1 
ATOM   3645 H HA   A SER   B 1 1   ? 52.007 -10.737 -23.315 0.86 31.18 ?  1   SER   B HA   1 
ATOM   3646 H HA   B SER   B 1 1   ? 52.064 -10.656 -23.203 0.14 31.45 ?  1   SER   B HA   1 
ATOM   3647 H HB2  A SER   B 1 1   ? 52.340 -10.304 -21.159 0.86 32.18 ?  1   SER   B HB2  1 
ATOM   3648 H HB2  B SER   B 1 1   ? 52.417 -9.923  -21.188 0.14 31.55 ?  1   SER   B HB2  1 
ATOM   3649 H HB3  A SER   B 1 1   ? 52.190 -8.840  -21.760 0.86 32.18 ?  1   SER   B HB3  1 
ATOM   3650 H HB3  B SER   B 1 1   ? 51.826 -8.564  -21.762 0.14 31.55 ?  1   SER   B HB3  1 
ATOM   3651 H HG   A SER   B 1 1   ? 50.862 -8.895  -20.126 0.86 34.55 ?  1   SER   B HG   1 
ATOM   3652 H HG   B SER   B 1 1   ? 50.605 -8.917  -20.115 0.14 31.87 ?  1   SER   B HG   1 
ATOM   3653 N N    A MET   B 1 2   ? 50.570 -12.390 -22.031 0.86 24.35 ?  2   MET   B N    1 
ATOM   3654 N N    B MET   B 1 2   ? 50.561 -12.299 -21.884 0.14 25.82 ?  2   MET   B N    1 
ATOM   3655 C CA   A MET   B 1 2   ? 49.747 -13.578 -21.857 0.86 24.55 ?  2   MET   B CA   1 
ATOM   3656 C CA   B MET   B 1 2   ? 49.737 -13.492 -21.731 0.14 25.51 ?  2   MET   B CA   1 
ATOM   3657 C C    A MET   B 1 2   ? 49.517 -13.762 -20.365 0.86 22.10 ?  2   MET   B C    1 
ATOM   3658 C C    B MET   B 1 2   ? 49.474 -13.716 -20.248 0.14 23.43 ?  2   MET   B C    1 
ATOM   3659 O O    A MET   B 1 2   ? 50.459 -14.057 -19.622 0.86 22.46 ?  2   MET   B O    1 
ATOM   3660 O O    B MET   B 1 2   ? 50.372 -14.135 -19.510 0.14 23.58 ?  2   MET   B O    1 
ATOM   3661 C CB   A MET   B 1 2   ? 50.478 -14.780 -22.448 0.86 28.75 ?  2   MET   B CB   1 
ATOM   3662 C CB   B MET   B 1 2   ? 50.466 -14.687 -22.336 0.14 27.34 ?  2   MET   B CB   1 
ATOM   3663 C CG   A MET   B 1 2   ? 49.620 -15.999 -22.732 0.86 32.43 ?  2   MET   B CG   1 
ATOM   3664 C CG   B MET   B 1 2   ? 49.581 -15.854 -22.729 0.14 28.95 ?  2   MET   B CG   1 
ATOM   3665 S SD   A MET   B 1 2   ? 50.501 -17.213 -23.732 0.86 35.67 ?  2   MET   B SD   1 
ATOM   3666 S SD   B MET   B 1 2   ? 50.473 -17.031 -23.759 0.14 30.28 ?  2   MET   B SD   1 
ATOM   3667 C CE   A MET   B 1 2   ? 51.118 -16.155 -25.035 0.86 35.78 ?  2   MET   B CE   1 
ATOM   3668 C CE   B MET   B 1 2   ? 51.273 -15.912 -24.905 0.14 30.62 ?  2   MET   B CE   1 
ATOM   3669 H H    A MET   B 1 2   ? 51.357 -12.483 -21.692 0.86 29.22 ?  2   MET   B H    1 
ATOM   3670 H H    B MET   B 1 2   ? 51.307 -12.343 -21.460 0.14 30.99 ?  2   MET   B H    1 
ATOM   3671 H HA   A MET   B 1 2   ? 48.899 -13.476 -22.313 0.86 29.46 ?  2   MET   B HA   1 
ATOM   3672 H HA   B MET   B 1 2   ? 48.898 -13.377 -22.205 0.14 30.62 ?  2   MET   B HA   1 
ATOM   3673 H HB2  A MET   B 1 2   ? 50.878 -14.485 -23.275 0.86 34.51 ?  2   MET   B HB2  1 
ATOM   3674 H HB2  B MET   B 1 2   ? 50.928 -14.358 -23.119 0.14 32.82 ?  2   MET   B HB2  1 
ATOM   3675 H HB3  A MET   B 1 2   ? 51.171 -15.066 -21.837 0.86 34.51 ?  2   MET   B HB3  1 
ATOM   3676 H HB3  B MET   B 1 2   ? 51.111 -15.028 -21.702 0.14 32.82 ?  2   MET   B HB3  1 
ATOM   3677 H HG2  A MET   B 1 2   ? 49.375 -16.416 -21.890 0.86 38.92 ?  2   MET   B HG2  1 
ATOM   3678 H HG2  B MET   B 1 2   ? 49.283 -16.313 -21.928 0.14 34.75 ?  2   MET   B HG2  1 
ATOM   3679 H HG3  A MET   B 1 2   ? 48.828 -15.740 -23.224 0.86 38.92 ?  2   MET   B HG3  1 
ATOM   3680 H HG3  B MET   B 1 2   ? 48.819 -15.536 -23.231 0.14 34.75 ?  2   MET   B HG3  1 
ATOM   3681 H HE1  A MET   B 1 2   ? 51.291 -16.693 -25.814 0.86 42.94 ?  2   MET   B HE1  1 
ATOM   3682 H HE1  B MET   B 1 2   ? 51.501 -16.394 -25.703 0.14 36.75 ?  2   MET   B HE1  1 
ATOM   3683 H HE2  A MET   B 1 2   ? 50.439 -15.488 -25.231 0.86 42.94 ?  2   MET   B HE2  1 
ATOM   3684 H HE2  B MET   B 1 2   ? 50.661 -15.185 -25.116 0.14 36.75 ?  2   MET   B HE2  1 
ATOM   3685 H HE3  A MET   B 1 2   ? 51.934 -15.715 -24.742 0.86 42.94 ?  2   MET   B HE3  1 
ATOM   3686 H HE3  B MET   B 1 2   ? 52.077 -15.554 -24.487 0.14 36.75 ?  2   MET   B HE3  1 
ATOM   3687 N N    A VAL   B 1 3   ? 48.277 -13.558 -19.925 0.86 19.82 ?  3   VAL   B N    1 
ATOM   3688 N N    B VAL   B 1 3   ? 48.248 -13.434 -19.815 0.14 21.21 ?  3   VAL   B N    1 
ATOM   3689 C CA   A VAL   B 1 3   ? 47.864 -13.825 -18.553 0.86 18.59 ?  3   VAL   B CA   1 
ATOM   3690 C CA   B VAL   B 1 3   ? 47.810 -13.725 -18.456 0.14 19.08 ?  3   VAL   B CA   1 
ATOM   3691 C C    A VAL   B 1 3   ? 46.637 -14.729 -18.590 0.86 16.76 ?  3   VAL   B C    1 
ATOM   3692 C C    B VAL   B 1 3   ? 46.578 -14.616 -18.518 0.14 16.97 ?  3   VAL   B C    1 
ATOM   3693 O O    A VAL   B 1 3   ? 45.901 -14.780 -19.577 0.86 17.20 ?  3   VAL   B O    1 
ATOM   3694 O O    B VAL   B 1 3   ? 45.776 -14.539 -19.454 0.14 16.78 ?  3   VAL   B O    1 
ATOM   3695 C CB   A VAL   B 1 3   ? 47.575 -12.528 -17.761 0.86 20.20 ?  3   VAL   B CB   1 
ATOM   3696 C CB   B VAL   B 1 3   ? 47.523 -12.449 -17.633 0.14 19.22 ?  3   VAL   B CB   1 
ATOM   3697 C CG1  A VAL   B 1 3   ? 48.846 -11.679 -17.643 0.86 20.77 ?  3   VAL   B CG1  1 
ATOM   3698 C CG1  B VAL   B 1 3   ? 48.783 -11.608 -17.494 0.14 19.27 ?  3   VAL   B CG1  1 
ATOM   3699 C CG2  A VAL   B 1 3   ? 46.451 -11.735 -18.414 0.86 20.96 ?  3   VAL   B CG2  1 
ATOM   3700 C CG2  B VAL   B 1 3   ? 46.396 -11.644 -18.264 0.14 19.30 ?  3   VAL   B CG2  1 
ATOM   3701 H H    A VAL   B 1 3   ? 47.640 -13.254 -20.415 0.86 23.79 ?  3   VAL   B H    1 
ATOM   3702 H H    B VAL   B 1 3   ? 47.646 -13.060 -20.303 0.14 25.46 ?  3   VAL   B H    1 
ATOM   3703 H HA   A VAL   B 1 3   ? 48.570 -14.300 -18.088 0.86 22.32 ?  3   VAL   B HA   1 
ATOM   3704 H HA   B VAL   B 1 3   ? 48.512 -14.216 -18.003 0.14 22.91 ?  3   VAL   B HA   1 
ATOM   3705 H HB   A VAL   B 1 3   ? 47.295 -12.756 -16.862 0.86 24.25 ?  3   VAL   B HB   1 
ATOM   3706 H HB   B VAL   B 1 3   ? 47.240 -12.712 -16.743 0.14 23.07 ?  3   VAL   B HB   1 
ATOM   3707 H HG11 A VAL   B 1 3   ? 48.647 -10.875 -17.137 0.86 24.94 ?  3   VAL   B HG11 1 
ATOM   3708 H HG11 B VAL   B 1 3   ? 48.581 -10.824 -16.959 0.14 23.14 ?  3   VAL   B HG11 1 
ATOM   3709 H HG12 A VAL   B 1 3   ? 49.529 -12.196 -17.187 0.86 24.94 ?  3   VAL   B HG12 1 
ATOM   3710 H HG12 B VAL   B 1 3   ? 49.469 -12.138 -17.058 0.14 23.14 ?  3   VAL   B HG12 1 
ATOM   3711 H HG13 A VAL   B 1 3   ? 49.151 -11.441 -18.533 0.86 24.94 ?  3   VAL   B HG13 1 
ATOM   3712 H HG13 B VAL   B 1 3   ? 49.082 -11.339 -18.376 0.14 23.14 ?  3   VAL   B HG13 1 
ATOM   3713 H HG21 A VAL   B 1 3   ? 46.381 -10.870 -17.980 0.86 25.16 ?  3   VAL   B HG21 1 
ATOM   3714 H HG21 B VAL   B 1 3   ? 46.323 -10.793 -17.805 0.14 23.17 ?  3   VAL   B HG21 1 
ATOM   3715 H HG22 A VAL   B 1 3   ? 46.653 -11.617 -19.355 0.86 25.16 ?  3   VAL   B HG22 1 
ATOM   3716 H HG22 B VAL   B 1 3   ? 46.599 -11.497 -19.201 0.14 23.17 ?  3   VAL   B HG22 1 
ATOM   3717 H HG23 A VAL   B 1 3   ? 45.621 -12.224 -18.310 0.86 25.16 ?  3   VAL   B HG23 1 
ATOM   3718 H HG23 B VAL   B 1 3   ? 45.565 -12.137 -18.178 0.14 23.17 ?  3   VAL   B HG23 1 
ATOM   3719 N N    . ASN   B 1 4   ? 46.431 -15.465 -17.502 1.00 15.19 ?  4   ASN   B N    1 
ATOM   3720 C CA   . ASN   B 1 4   ? 45.301 -16.392 -17.409 1.00 13.94 ?  4   ASN   B CA   1 
ATOM   3721 C C    . ASN   B 1 4   ? 45.257 -17.350 -18.599 1.00 14.05 ?  4   ASN   B C    1 
ATOM   3722 O O    . ASN   B 1 4   ? 44.196 -17.627 -19.159 1.00 15.43 ?  4   ASN   B O    1 
ATOM   3723 C CB   . ASN   B 1 4   ? 43.971 -15.650 -17.246 1.00 13.30 ?  4   ASN   B CB   1 
ATOM   3724 C CG   . ASN   B 1 4   ? 43.926 -14.829 -15.981 1.00 12.69 ?  4   ASN   B CG   1 
ATOM   3725 O OD1  . ASN   B 1 4   ? 44.226 -15.330 -14.902 1.00 12.31 ?  4   ASN   B OD1  1 
ATOM   3726 N ND2  . ASN   B 1 4   ? 43.576 -13.556 -16.105 1.00 13.62 ?  4   ASN   B ND2  1 
ATOM   3727 H H    A ASN   B 1 4   ? 46.934 -15.458 -16.805 0.86 18.24 ?  4   ASN   B H    1 
ATOM   3728 H H    B ASN   B 1 4   ? 46.975 -15.519 -16.839 0.14 18.24 ?  4   ASN   B H    1 
ATOM   3729 H HA   . ASN   B 1 4   ? 45.426 -16.931 -16.614 1.00 16.74 ?  4   ASN   B HA   1 
ATOM   3730 H HB2  . ASN   B 1 4   ? 43.845 -15.052 -17.998 1.00 15.97 ?  4   ASN   B HB2  1 
ATOM   3731 H HB3  . ASN   B 1 4   ? 43.250 -16.299 -17.211 1.00 15.97 ?  4   ASN   B HB3  1 
ATOM   3732 H HD21 . ASN   B 1 4   ? 43.544 -13.049 -15.410 1.00 16.36 ?  4   ASN   B HD21 1 
ATOM   3733 H HD22 . ASN   B 1 4   ? 43.377 -13.236 -16.878 1.00 16.36 ?  4   ASN   B HD22 1 
ATOM   3734 N N    . SER   B 1 5   ? 46.422 -17.864 -18.991 1.00 15.00 ?  5   SER   B N    1 
ATOM   3735 C CA   . SER   B 1 5   ? 46.518 -18.787 -20.125 1.00 17.71 ?  5   SER   B CA   1 
ATOM   3736 C C    . SER   B 1 5   ? 46.528 -20.225 -19.613 1.00 18.88 ?  5   SER   B C    1 
ATOM   3737 O O    . SER   B 1 5   ? 47.545 -20.913 -19.602 1.00 21.45 ?  5   SER   B O    1 
ATOM   3738 C CB   . SER   B 1 5   ? 47.756 -18.480 -20.962 1.00 19.64 ?  5   SER   B CB   1 
ATOM   3739 O OG   . SER   B 1 5   ? 48.941 -18.709 -20.218 1.00 22.24 ?  5   SER   B OG   1 
ATOM   3740 H H    . SER   B 1 5   ? 47.182 -17.682 -18.622 1.00 18.01 ?  5   SER   B H    1 
ATOM   3741 H HA   . SER   B 1 5   ? 45.739 -18.675 -20.690 1.00 21.26 ?  5   SER   B HA   1 
ATOM   3742 H HB2  . SER   B 1 5   ? 47.754 -19.048 -21.750 1.00 23.57 ?  5   SER   B HB2  1 
ATOM   3743 H HB3  . SER   B 1 5   ? 47.715 -17.551 -21.227 1.00 23.57 ?  5   SER   B HB3  1 
ATOM   3744 H HG   . SER   B 1 5   ? 49.005 -19.524 -20.026 1.00 26.70 ?  5   SER   B HG   1 
ATOM   3745 N N    . PHE   B 1 6   ? 45.354 -20.665 -19.178 1.00 18.47 ?  6   PHE   B N    1 
ATOM   3746 C CA   . PHE   B 1 6   ? 45.184 -22.017 -18.667 1.00 17.96 ?  6   PHE   B CA   1 
ATOM   3747 C C    . PHE   B 1 6   ? 45.132 -23.003 -19.825 1.00 20.98 ?  6   PHE   B C    1 
ATOM   3748 O O    . PHE   B 1 6   ? 44.480 -22.749 -20.841 1.00 23.04 ?  6   PHE   B O    1 
ATOM   3749 C CB   . PHE   B 1 6   ? 43.895 -22.102 -17.850 1.00 16.30 ?  6   PHE   B CB   1 
ATOM   3750 C CG   . PHE   B 1 6   ? 43.899 -21.228 -16.623 1.00 14.56 ?  6   PHE   B CG   1 
ATOM   3751 C CD1  . PHE   B 1 6   ? 44.410 -21.704 -15.433 1.00 13.64 ?  6   PHE   B CD1  1 
ATOM   3752 C CD2  . PHE   B 1 6   ? 43.394 -19.934 -16.662 1.00 14.20 ?  6   PHE   B CD2  1 
ATOM   3753 C CE1  . PHE   B 1 6   ? 44.412 -20.911 -14.294 1.00 13.29 ?  6   PHE   B CE1  1 
ATOM   3754 C CE2  . PHE   B 1 6   ? 43.403 -19.132 -15.531 1.00 14.62 ?  6   PHE   B CE2  1 
ATOM   3755 C CZ   . PHE   B 1 6   ? 43.916 -19.616 -14.348 1.00 13.56 ?  6   PHE   B CZ   1 
ATOM   3756 H H    . PHE   B 1 6   ? 44.635 -20.197 -19.171 1.00 22.18 ?  6   PHE   B H    1 
ATOM   3757 H HA   . PHE   B 1 6   ? 45.930 -22.252 -18.095 1.00 21.57 ?  6   PHE   B HA   1 
ATOM   3758 H HB2  . PHE   B 1 6   ? 43.149 -21.828 -18.406 1.00 19.57 ?  6   PHE   B HB2  1 
ATOM   3759 H HB3  . PHE   B 1 6   ? 43.765 -23.021 -17.559 1.00 19.57 ?  6   PHE   B HB3  1 
ATOM   3760 H HD1  . PHE   B 1 6   ? 44.752 -22.569 -15.387 1.00 16.38 ?  6   PHE   B HD1  1 
ATOM   3761 H HD2  . PHE   B 1 6   ? 43.049 -19.606 -17.461 1.00 17.05 ?  6   PHE   B HD2  1 
ATOM   3762 H HE1  . PHE   B 1 6   ? 44.768 -21.236 -13.495 1.00 15.96 ?  6   PHE   B HE1  1 
ATOM   3763 H HE2  . PHE   B 1 6   ? 43.062 -18.266 -15.571 1.00 17.56 ?  6   PHE   B HE2  1 
ATOM   3764 H HZ   . PHE   B 1 6   ? 43.921 -19.082 -13.587 1.00 16.28 ?  6   PHE   B HZ   1 
ATOM   3765 N N    A SER   B 1 7   ? 45.821 -24.134 -19.668 0.86 21.14 ?  7   SER   B N    1 
ATOM   3766 N N    B SER   B 1 7   ? 45.833 -24.125 -19.667 0.14 21.65 ?  7   SER   B N    1 
ATOM   3767 C CA   A SER   B 1 7   ? 45.901 -25.137 -20.721 0.86 22.71 ?  7   SER   B CA   1 
ATOM   3768 C CA   B SER   B 1 7   ? 45.953 -25.126 -20.716 0.14 22.33 ?  7   SER   B CA   1 
ATOM   3769 C C    A SER   B 1 7   ? 45.864 -26.536 -20.120 0.86 21.96 ?  7   SER   B C    1 
ATOM   3770 C C    B SER   B 1 7   ? 45.915 -26.518 -20.107 0.14 21.98 ?  7   SER   B C    1 
ATOM   3771 O O    A SER   B 1 7   ? 46.438 -26.784 -19.056 0.86 23.09 ?  7   SER   B O    1 
ATOM   3772 O O    B SER   B 1 7   ? 46.497 -26.759 -19.046 0.14 22.26 ?  7   SER   B O    1 
ATOM   3773 C CB   A SER   B 1 7   ? 47.181 -24.961 -21.550 0.86 25.16 ?  7   SER   B CB   1 
ATOM   3774 C CB   B SER   B 1 7   ? 47.265 -24.950 -21.492 0.14 23.19 ?  7   SER   B CB   1 
ATOM   3775 O OG   A SER   B 1 7   ? 47.153 -25.771 -22.710 0.86 27.32 ?  7   SER   B OG   1 
ATOM   3776 O OG   B SER   B 1 7   ? 47.446 -25.996 -22.431 0.14 23.75 ?  7   SER   B OG   1 
ATOM   3777 H H    A SER   B 1 7   ? 46.253 -24.343 -18.953 0.86 25.38 ?  7   SER   B H    1 
ATOM   3778 H H    B SER   B 1 7   ? 46.258 -24.330 -18.945 0.14 25.99 ?  7   SER   B H    1 
ATOM   3779 H HA   A SER   B 1 7   ? 45.140 -25.046 -21.313 0.86 27.27 ?  7   SER   B HA   1 
ATOM   3780 H HA   B SER   B 1 7   ? 45.214 -25.041 -21.336 0.14 26.80 ?  7   SER   B HA   1 
ATOM   3781 H HB2  A SER   B 1 7   ? 47.255 -24.031 -21.818 0.86 30.20 ?  7   SER   B HB2  1 
ATOM   3782 H HB2  B SER   B 1 7   ? 47.239 -24.103 -21.964 0.14 27.83 ?  7   SER   B HB2  1 
ATOM   3783 H HB3  A SER   B 1 7   ? 47.945 -25.209 -21.006 0.86 30.20 ?  7   SER   B HB3  1 
ATOM   3784 H HB3  B SER   B 1 7   ? 48.006 -24.958 -20.866 0.14 27.83 ?  7   SER   B HB3  1 
ATOM   3785 H HG   A SER   B 1 7   ? 47.861 -25.666 -23.151 0.86 32.79 ?  7   SER   B HG   1 
ATOM   3786 H HG   B SER   B 1 7   ? 48.167 -25.885 -22.848 0.14 28.51 ?  7   SER   B HG   1 
ATOM   3787 N N    A GLY   B 1 8   ? 45.187 -27.449 -20.814 0.86 21.65 ?  8   GLY   B N    1 
ATOM   3788 N N    B GLY   B 1 8   ? 45.225 -27.431 -20.787 0.14 21.40 ?  8   GLY   B N    1 
ATOM   3789 C CA   A GLY   B 1 8   ? 45.167 -28.839 -20.409 0.86 21.18 ?  8   GLY   B CA   1 
ATOM   3790 C CA   B GLY   B 1 8   ? 45.198 -28.818 -20.374 0.14 20.64 ?  8   GLY   B CA   1 
ATOM   3791 C C    A GLY   B 1 8   ? 44.201 -29.171 -19.299 0.86 20.06 ?  8   GLY   B C    1 
ATOM   3792 C C    B GLY   B 1 8   ? 44.236 -29.141 -19.256 0.14 19.64 ?  8   GLY   B C    1 
ATOM   3793 O O    A GLY   B 1 8   ? 44.326 -30.238 -18.687 0.86 21.21 ?  8   GLY   B O    1 
ATOM   3794 O O    B GLY   B 1 8   ? 44.404 -30.169 -18.593 0.14 19.89 ?  8   GLY   B O    1 
ATOM   3795 H H    A GLY   B 1 8   ? 44.732 -27.279 -21.522 0.86 25.99 ?  8   GLY   B H    1 
ATOM   3796 H H    B GLY   B 1 8   ? 44.764 -27.266 -21.494 0.14 25.69 ?  8   GLY   B H    1 
ATOM   3797 H HA2  A GLY   B 1 8   ? 44.940 -29.383 -21.180 0.86 25.42 ?  8   GLY   B HA2  1 
ATOM   3798 H HA2  B GLY   B 1 8   ? 44.966 -29.368 -21.139 0.14 24.78 ?  8   GLY   B HA2  1 
ATOM   3799 H HA3  A GLY   B 1 8   ? 46.053 -29.093 -20.113 0.86 25.42 ?  8   GLY   B HA3  1 
ATOM   3800 H HA3  B GLY   B 1 8   ? 46.083 -29.075 -20.078 0.14 24.78 ?  8   GLY   B HA3  1 
ATOM   3801 N N    . TYR   B 1 9   ? 43.230 -28.304 -19.024 1.00 18.49 ?  9   TYR   B N    1 
ATOM   3802 C CA   . TYR   B 1 9   ? 42.250 -28.570 -17.985 1.00 16.50 ?  9   TYR   B CA   1 
ATOM   3803 C C    . TYR   B 1 9   ? 41.072 -29.357 -18.534 1.00 15.83 ?  9   TYR   B C    1 
ATOM   3804 O O    . TYR   B 1 9   ? 40.690 -29.223 -19.700 1.00 18.04 ?  9   TYR   B O    1 
ATOM   3805 C CB   . TYR   B 1 9   ? 41.742 -27.275 -17.356 1.00 16.34 ?  9   TYR   B CB   1 
ATOM   3806 C CG   . TYR   B 1 9   ? 42.755 -26.644 -16.431 1.00 15.82 ?  9   TYR   B CG   1 
ATOM   3807 C CD1  . TYR   B 1 9   ? 43.868 -25.988 -16.940 1.00 16.60 ?  9   TYR   B CD1  1 
ATOM   3808 C CD2  . TYR   B 1 9   ? 42.617 -26.724 -15.053 1.00 15.02 ?  9   TYR   B CD2  1 
ATOM   3809 C CE1  . TYR   B 1 9   ? 44.809 -25.428 -16.103 1.00 16.99 ?  9   TYR   B CE1  1 
ATOM   3810 C CE2  . TYR   B 1 9   ? 43.552 -26.168 -14.209 1.00 15.80 ?  9   TYR   B CE2  1 
ATOM   3811 C CZ   . TYR   B 1 9   ? 44.647 -25.517 -14.741 1.00 16.91 ?  9   TYR   B CZ   1 
ATOM   3812 O OH   . TYR   B 1 9   ? 45.586 -24.968 -13.908 1.00 17.88 ?  9   TYR   B OH   1 
ATOM   3813 H H    A TYR   B 1 9   ? 43.112 -27.559 -19.436 0.86 22.20 ?  9   TYR   B H    1 
ATOM   3814 H H    B TYR   B 1 9   ? 43.089 -27.579 -19.464 0.14 22.20 ?  9   TYR   B H    1 
ATOM   3815 H HA   . TYR   B 1 9   ? 42.660 -29.097 -17.284 1.00 19.81 ?  9   TYR   B HA   1 
ATOM   3816 H HB2  . TYR   B 1 9   ? 41.533 -26.633 -18.054 1.00 19.62 ?  9   TYR   B HB2  1 
ATOM   3817 H HB3  . TYR   B 1 9   ? 40.953 -27.474 -16.835 1.00 19.62 ?  9   TYR   B HB3  1 
ATOM   3818 H HD1  . TYR   B 1 9   ? 43.982 -25.931 -17.861 1.00 19.93 ?  9   TYR   B HD1  1 
ATOM   3819 H HD2  . TYR   B 1 9   ? 41.878 -27.169 -14.695 1.00 18.04 ?  9   TYR   B HD2  1 
ATOM   3820 H HE1  . TYR   B 1 9   ? 45.547 -24.994 -16.457 1.00 20.39 ?  9   TYR   B HE1  1 
ATOM   3821 H HE2  . TYR   B 1 9   ? 43.438 -26.234 -13.286 1.00 18.97 ?  9   TYR   B HE2  1 
ATOM   3822 H HH   . TYR   B 1 9   ? 46.188 -24.608 -14.360 1.00 21.47 ?  9   TYR   B HH   1 
ATOM   3823 N N    . LEU   B 1 10  ? 40.510 -30.193 -17.673 1.00 14.17 ?  10  LEU   B N    1 
ATOM   3824 C CA   . LEU   B 1 10  ? 39.300 -30.941 -17.964 1.00 14.20 ?  10  LEU   B CA   1 
ATOM   3825 C C    . LEU   B 1 10  ? 38.110 -30.178 -17.396 1.00 13.44 ?  10  LEU   B C    1 
ATOM   3826 O O    . LEU   B 1 10  ? 38.125 -29.768 -16.232 1.00 13.39 ?  10  LEU   B O    1 
ATOM   3827 C CB   . LEU   B 1 10  ? 39.397 -32.324 -17.321 1.00 15.26 ?  10  LEU   B CB   1 
ATOM   3828 C CG   . LEU   B 1 10  ? 38.227 -33.254 -17.605 1.00 17.08 ?  10  LEU   B CG   1 
ATOM   3829 C CD1  . LEU   B 1 10  ? 38.257 -33.728 -19.052 1.00 18.73 ?  10  LEU   B CD1  1 
ATOM   3830 C CD2  . LEU   B 1 10  ? 38.241 -34.426 -16.645 1.00 18.44 ?  10  LEU   B CD2  1 
ATOM   3831 H H    . LEU   B 1 10  ? 40.822 -30.348 -16.882 1.00 17.01 ?  10  LEU   B H    1 
ATOM   3832 H HA   . LEU   B 1 10  ? 39.189 -31.043 -18.919 1.00 17.05 ?  10  LEU   B HA   1 
ATOM   3833 H HB2  . LEU   B 1 10  ? 40.201 -32.763 -17.645 1.00 18.32 ?  10  LEU   B HB2  1 
ATOM   3834 H HB3  . LEU   B 1 10  ? 39.456 -32.218 -16.357 1.00 18.32 ?  10  LEU   B HB3  1 
ATOM   3835 H HG   . LEU   B 1 10  ? 37.397 -32.773 -17.467 1.00 20.51 ?  10  LEU   B HG   1 
ATOM   3836 H HD11 . LEU   B 1 10  ? 37.531 -34.355 -19.193 1.00 22.49 ?  10  LEU   B HD11 1 
ATOM   3837 H HD12 . LEU   B 1 10  ? 38.148 -32.960 -19.635 1.00 22.49 ?  10  LEU   B HD12 1 
ATOM   3838 H HD13 . LEU   B 1 10  ? 39.107 -34.159 -19.225 1.00 22.49 ?  10  LEU   B HD13 1 
ATOM   3839 H HD21 . LEU   B 1 10  ? 37.493 -35.008 -16.850 1.00 22.14 ?  10  LEU   B HD21 1 
ATOM   3840 H HD22 . LEU   B 1 10  ? 39.075 -34.906 -16.749 1.00 22.14 ?  10  LEU   B HD22 1 
ATOM   3841 H HD23 . LEU   B 1 10  ? 38.160 -34.089 -15.739 1.00 22.14 ?  10  LEU   B HD23 1 
ATOM   3842 N N    . LYS   B 1 11  ? 37.079 -30.000 -18.211 1.00 14.48 ?  11  LYS   B N    1 
ATOM   3843 C CA   . LYS   B 1 11  ? 35.893 -29.267 -17.795 1.00 16.12 ?  11  LYS   B CA   1 
ATOM   3844 C C    . LYS   B 1 11  ? 34.980 -30.183 -16.987 1.00 15.47 ?  11  LYS   B C    1 
ATOM   3845 O O    . LYS   B 1 11  ? 34.555 -31.234 -17.480 1.00 17.58 ?  11  LYS   B O    1 
ATOM   3846 C CB   . LYS   B 1 11  ? 35.175 -28.749 -19.038 1.00 19.30 ?  11  LYS   B CB   1 
ATOM   3847 C CG   . LYS   B 1 11  ? 34.019 -27.806 -18.775 1.00 22.43 ?  11  LYS   B CG   1 
ATOM   3848 C CD   . LYS   B 1 11  ? 33.317 -27.452 -20.080 1.00 25.21 ?  11  LYS   B CD   1 
ATOM   3849 C CE   . LYS   B 1 11  ? 32.247 -26.398 -19.875 1.00 27.37 ?  11  LYS   B CE   1 
ATOM   3850 N NZ   . LYS   B 1 11  ? 32.831 -25.073 -19.542 1.00 28.70 ?  11  LYS   B NZ   1 
ATOM   3851 H H    . LYS   B 1 11  ? 37.037 -30.306 -19.013 1.00 17.38 ?  11  LYS   B H    1 
ATOM   3852 H HA   . LYS   B 1 11  ? 36.150 -28.512 -17.243 1.00 19.35 ?  11  LYS   B HA   1 
ATOM   3853 H HB2  . LYS   B 1 11  ? 35.817 -28.274 -19.588 1.00 23.17 ?  11  LYS   B HB2  1 
ATOM   3854 H HB3  . LYS   B 1 11  ? 34.825 -29.507 -19.530 1.00 23.17 ?  11  LYS   B HB3  1 
ATOM   3855 H HG2  . LYS   B 1 11  ? 33.376 -28.235 -18.189 1.00 26.92 ?  11  LYS   B HG2  1 
ATOM   3856 H HG3  . LYS   B 1 11  ? 34.351 -26.988 -18.375 1.00 26.92 ?  11  LYS   B HG3  1 
ATOM   3857 H HD2  . LYS   B 1 11  ? 33.970 -27.106 -20.710 1.00 30.26 ?  11  LYS   B HD2  1 
ATOM   3858 H HD3  . LYS   B 1 11  ? 32.896 -28.249 -20.443 1.00 30.26 ?  11  LYS   B HD3  1 
ATOM   3859 H HE2  . LYS   B 1 11  ? 31.729 -26.306 -20.690 1.00 32.86 ?  11  LYS   B HE2  1 
ATOM   3860 H HE3  . LYS   B 1 11  ? 31.671 -26.670 -19.143 1.00 32.86 ?  11  LYS   B HE3  1 
ATOM   3861 H HZ1  . LYS   B 1 11  ? 32.187 -24.461 -19.492 1.00 34.45 ?  11  LYS   B HZ1  1 
ATOM   3862 H HZ2  . LYS   B 1 11  ? 33.253 -25.114 -18.760 1.00 34.45 ?  11  LYS   B HZ2  1 
ATOM   3863 H HZ3  . LYS   B 1 11  ? 33.411 -24.830 -20.172 1.00 34.45 ?  11  LYS   B HZ3  1 
ATOM   3864 N N    . LEU   B 1 12  ? 34.662 -29.780 -15.757 1.00 14.29 ?  12  LEU   B N    1 
ATOM   3865 C CA   . LEU   B 1 12  ? 33.704 -30.498 -14.922 1.00 14.31 ?  12  LEU   B CA   1 
ATOM   3866 C C    . LEU   B 1 12  ? 32.307 -29.900 -15.014 1.00 14.51 ?  12  LEU   B C    1 
ATOM   3867 O O    . LEU   B 1 12  ? 31.321 -30.621 -15.178 1.00 15.29 ?  12  LEU   B O    1 
ATOM   3868 C CB   . LEU   B 1 12  ? 34.169 -30.513 -13.461 1.00 13.74 ?  12  LEU   B CB   1 
ATOM   3869 C CG   . LEU   B 1 12  ? 35.507 -31.200 -13.185 1.00 13.99 ?  12  LEU   B CG   1 
ATOM   3870 C CD1  . LEU   B 1 12  ? 35.836 -31.148 -11.700 1.00 14.28 ?  12  LEU   B CD1  1 
ATOM   3871 C CD2  . LEU   B 1 12  ? 35.510 -32.634 -13.694 1.00 14.85 ?  12  LEU   B CD2  1 
ATOM   3872 H H    . LEU   B 1 12  ? 34.982 -29.070 -15.383 1.00 17.16 ?  12  LEU   B H    1 
ATOM   3873 H HA   . LEU   B 1 12  ? 33.650 -31.413 -15.230 1.00 17.18 ?  12  LEU   B HA   1 
ATOM   3874 H HB2  . LEU   B 1 12  ? 34.246 -29.594 -13.160 1.00 16.50 ?  12  LEU   B HB2  1 
ATOM   3875 H HB3  . LEU   B 1 12  ? 33.494 -30.969 -12.936 1.00 16.50 ?  12  LEU   B HB3  1 
ATOM   3876 H HG   . LEU   B 1 12  ? 36.207 -30.720 -13.657 1.00 16.80 ?  12  LEU   B HG   1 
ATOM   3877 H HD11 . LEU   B 1 12  ? 36.690 -31.589 -11.549 1.00 17.14 ?  12  LEU   B HD11 1 
ATOM   3878 H HD12 . LEU   B 1 12  ? 35.890 -30.223 -11.419 1.00 17.14 ?  12  LEU   B HD12 1 
ATOM   3879 H HD13 . LEU   B 1 12  ? 35.139 -31.606 -11.205 1.00 17.14 ?  12  LEU   B HD13 1 
ATOM   3880 H HD21 . LEU   B 1 12  ? 36.312 -33.079 -13.379 1.00 17.83 ?  12  LEU   B HD21 1 
ATOM   3881 H HD22 . LEU   B 1 12  ? 34.723 -33.089 -13.360 1.00 17.83 ?  12  LEU   B HD22 1 
ATOM   3882 H HD23 . LEU   B 1 12  ? 35.499 -32.623 -14.666 1.00 17.83 ?  12  LEU   B HD23 1 
ATOM   3883 N N    . THR   B 1 13  ? 32.214 -28.581 -14.902 1.00 14.36 ?  13  THR   B N    1 
ATOM   3884 C CA   . THR   B 1 13  ? 30.982 -27.835 -15.096 1.00 14.30 ?  13  THR   B CA   1 
ATOM   3885 C C    . THR   B 1 13  ? 31.303 -26.622 -15.965 1.00 15.56 ?  13  THR   B C    1 
ATOM   3886 O O    . THR   B 1 13  ? 32.444 -26.415 -16.391 1.00 16.44 ?  13  THR   B O    1 
ATOM   3887 C CB   . THR   B 1 13  ? 30.387 -27.377 -13.761 1.00 13.97 ?  13  THR   B CB   1 
ATOM   3888 O OG1  . THR   B 1 13  ? 31.229 -26.355 -13.211 1.00 13.74 ?  13  THR   B OG1  1 
ATOM   3889 C CG2  . THR   B 1 13  ? 30.276 -28.536 -12.772 1.00 14.72 ?  13  THR   B CG2  1 
ATOM   3890 H H    . THR   B 1 13  ? 32.880 -28.076 -14.700 1.00 17.25 ?  13  THR   B H    1 
ATOM   3891 H HA   . THR   B 1 13  ? 30.327 -28.389 -15.550 1.00 17.17 ?  13  THR   B HA   1 
ATOM   3892 H HB   . THR   B 1 13  ? 29.496 -27.013 -13.908 1.00 16.78 ?  13  THR   B HB   1 
ATOM   3893 H HG1  . THR   B 1 13  ? 30.912 -25.593 -13.387 1.00 16.49 ?  13  THR   B HG1  1 
ATOM   3894 H HG21 . THR   B 1 13  ? 29.780 -28.257 -11.985 1.00 17.67 ?  13  THR   B HG21 1 
ATOM   3895 H HG22 . THR   B 1 13  ? 29.813 -29.281 -13.186 1.00 17.67 ?  13  THR   B HG22 1 
ATOM   3896 H HG23 . THR   B 1 13  ? 31.160 -28.826 -12.499 1.00 17.67 ?  13  THR   B HG23 1 
ATOM   3897 N N    A ASP   B 1 14  ? 30.283 -25.798 -16.209 0.86 16.74 ?  14  ASP   B N    1 
ATOM   3898 N N    B ASP   B 1 14  ? 30.287 -25.790 -16.204 0.14 16.40 ?  14  ASP   B N    1 
ATOM   3899 C CA   A ASP   B 1 14  ? 30.473 -24.624 -17.053 0.86 18.38 ?  14  ASP   B CA   1 
ATOM   3900 C CA   B ASP   B 1 14  ? 30.473 -24.623 -17.059 0.14 17.24 ?  14  ASP   B CA   1 
ATOM   3901 C C    A ASP   B 1 14  ? 31.566 -23.704 -16.522 0.86 16.61 ?  14  ASP   B C    1 
ATOM   3902 C C    B ASP   B 1 14  ? 31.492 -23.638 -16.501 0.14 15.78 ?  14  ASP   B C    1 
ATOM   3903 O O    A ASP   B 1 14  ? 32.185 -22.973 -17.303 0.86 18.04 ?  14  ASP   B O    1 
ATOM   3904 O O    B ASP   B 1 14  ? 31.975 -22.782 -17.250 0.14 16.07 ?  14  ASP   B O    1 
ATOM   3905 C CB   A ASP   B 1 14  ? 29.157 -23.859 -17.190 0.86 22.19 ?  14  ASP   B CB   1 
ATOM   3906 C CB   B ASP   B 1 14  ? 29.142 -23.904 -17.285 0.14 19.37 ?  14  ASP   B CB   1 
ATOM   3907 C CG   A ASP   B 1 14  ? 28.202 -24.512 -18.165 0.86 26.33 ?  14  ASP   B CG   1 
ATOM   3908 C CG   B ASP   B 1 14  ? 28.253 -24.625 -18.282 0.14 21.19 ?  14  ASP   B CG   1 
ATOM   3909 O OD1  A ASP   B 1 14  ? 28.606 -25.474 -18.854 0.86 27.97 ?  14  ASP   B OD1  1 
ATOM   3910 O OD1  B ASP   B 1 14  ? 28.793 -25.345 -19.148 0.14 21.80 ?  14  ASP   B OD1  1 
ATOM   3911 O OD2  A ASP   B 1 14  ? 27.041 -24.060 -18.240 0.86 27.97 -1 14  ASP   B OD2  1 
ATOM   3912 O OD2  B ASP   B 1 14  ? 27.017 -24.472 -18.202 0.14 21.82 -1 14  ASP   B OD2  1 
ATOM   3913 H H    A ASP   B 1 14  ? 29.489 -25.890 -15.894 0.86 20.10 ?  14  ASP   B H    1 
ATOM   3914 H H    B ASP   B 1 14  ? 29.493 -25.877 -15.886 0.14 19.69 ?  14  ASP   B H    1 
ATOM   3915 H HA   A ASP   B 1 14  ? 30.743 -24.911 -17.936 0.86 22.07 ?  14  ASP   B HA   1 
ATOM   3916 H HA   B ASP   B 1 14  ? 30.797 -24.922 -17.921 0.14 20.70 ?  14  ASP   B HA   1 
ATOM   3917 H HB2  A ASP   B 1 14  ? 28.711 -23.825 -16.330 0.86 26.63 ?  14  ASP   B HB2  1 
ATOM   3918 H HB2  B ASP   B 1 14  ? 28.663 -23.853 -16.444 0.14 23.26 ?  14  ASP   B HB2  1 
ATOM   3919 H HB3  A ASP   B 1 14  ? 29.337 -22.960 -17.507 0.86 26.63 ?  14  ASP   B HB3  1 
ATOM   3920 H HB3  B ASP   B 1 14  ? 29.321 -23.007 -17.618 0.14 23.26 ?  14  ASP   B HB3  1 
ATOM   3921 N N    . ASN   B 1 15  ? 31.819 -23.722 -15.209 1.00 14.05 ?  15  ASN   B N    1 
ATOM   3922 C CA   . ASN   B 1 15  ? 32.779 -22.801 -14.607 1.00 12.49 ?  15  ASN   B CA   1 
ATOM   3923 C C    . ASN   B 1 15  ? 33.872 -23.454 -13.770 1.00 11.56 ?  15  ASN   B C    1 
ATOM   3924 O O    . ASN   B 1 15  ? 34.698 -22.722 -13.218 1.00 12.31 ?  15  ASN   B O    1 
ATOM   3925 C CB   . ASN   B 1 15  ? 32.060 -21.750 -13.747 1.00 12.46 ?  15  ASN   B CB   1 
ATOM   3926 C CG   . ASN   B 1 15  ? 31.436 -22.352 -12.509 1.00 12.39 ?  15  ASN   B CG   1 
ATOM   3927 O OD1  . ASN   B 1 15  ? 30.492 -23.144 -12.597 1.00 14.07 ?  15  ASN   B OD1  1 
ATOM   3928 N ND2  . ASN   B 1 15  ? 31.961 -22.001 -11.348 1.00 12.09 ?  15  ASN   B ND2  1 
ATOM   3929 H H    A ASN   B 1 15  ? 31.447 -24.261 -14.648 0.86 16.87 ?  15  ASN   B H    1 
ATOM   3930 H H    B ASN   B 1 15  ? 31.482 -24.292 -14.657 0.14 16.87 ?  15  ASN   B H    1 
ATOM   3931 H HA   . ASN   B 1 15  ? 33.222 -22.320 -15.316 1.00 14.99 ?  15  ASN   B HA   1 
ATOM   3932 H HB2  . ASN   B 1 15  ? 32.704 -21.074 -13.468 1.00 14.96 ?  15  ASN   B HB2  1 
ATOM   3933 H HB3  . ASN   B 1 15  ? 31.356 -21.332 -14.271 1.00 14.96 ?  15  ASN   B HB3  1 
ATOM   3934 H HD21 . ASN   B 1 15  ? 31.637 -22.312 -10.615 1.00 14.52 ?  15  ASN   B HD21 1 
ATOM   3935 H HD22 . ASN   B 1 15  ? 32.622 -21.447 -11.321 1.00 14.52 ?  15  ASN   B HD22 1 
ATOM   3936 N N    . VAL   B 1 16  ? 33.907 -24.782 -13.651 1.00 11.27 ?  16  VAL   B N    1 
ATOM   3937 C CA   . VAL   B 1 16  ? 34.904 -25.473 -12.836 1.00 11.01 ?  16  VAL   B CA   1 
ATOM   3938 C C    . VAL   B 1 16  ? 35.704 -26.411 -13.726 1.00 11.16 ?  16  VAL   B C    1 
ATOM   3939 O O    . VAL   B 1 16  ? 35.129 -27.279 -14.401 1.00 12.32 ?  16  VAL   B O    1 
ATOM   3940 C CB   . VAL   B 1 16  ? 34.268 -26.245 -11.665 1.00 11.65 ?  16  VAL   B CB   1 
ATOM   3941 C CG1  . VAL   B 1 16  ? 35.343 -26.968 -10.860 1.00 11.82 ?  16  VAL   B CG1  1 
ATOM   3942 C CG2  . VAL   B 1 16  ? 33.453 -25.306 -10.783 1.00 12.45 ?  16  VAL   B CG2  1 
ATOM   3943 H H    . VAL   B 1 16  ? 33.352 -25.313 -14.038 1.00 13.53 ?  16  VAL   B H    1 
ATOM   3944 H HA   . VAL   B 1 16  ? 35.516 -24.817 -12.461 1.00 13.22 ?  16  VAL   B HA   1 
ATOM   3945 H HB   . VAL   B 1 16  ? 33.666 -26.915 -12.028 1.00 13.99 ?  16  VAL   B HB   1 
ATOM   3946 H HG11 . VAL   B 1 16  ? 34.952 -27.268 -10.024 1.00 14.20 ?  16  VAL   B HG11 1 
ATOM   3947 H HG12 . VAL   B 1 16  ? 35.665 -27.725 -11.366 1.00 14.20 ?  16  VAL   B HG12 1 
ATOM   3948 H HG13 . VAL   B 1 16  ? 36.067 -26.348 -10.680 1.00 14.20 ?  16  VAL   B HG13 1 
ATOM   3949 H HG21 . VAL   B 1 16  ? 33.099 -25.809 -10.033 1.00 14.95 ?  16  VAL   B HG21 1 
ATOM   3950 H HG22 . VAL   B 1 16  ? 34.024 -24.593 -10.467 1.00 14.95 ?  16  VAL   B HG22 1 
ATOM   3951 H HG23 . VAL   B 1 16  ? 32.720 -24.938 -11.307 1.00 14.95 ?  16  VAL   B HG23 1 
ATOM   3952 N N    . TYR   B 1 17  ? 37.030 -26.246 -13.694 1.00 11.54 ?  17  TYR   B N    1 
ATOM   3953 C CA   . TYR   B 1 17  ? 37.980 -26.994 -14.502 1.00 11.86 ?  17  TYR   B CA   1 
ATOM   3954 C C    . TYR   B 1 17  ? 39.023 -27.612 -13.582 1.00 11.30 ?  17  TYR   B C    1 
ATOM   3955 O O    . TYR   B 1 17  ? 39.296 -27.080 -12.502 1.00 11.64 ?  17  TYR   B O    1 
ATOM   3956 C CB   . TYR   B 1 17  ? 38.692 -26.054 -15.478 1.00 13.40 ?  17  TYR   B CB   1 
ATOM   3957 C CG   . TYR   B 1 17  ? 37.770 -25.288 -16.390 1.00 15.75 ?  17  TYR   B CG   1 
ATOM   3958 C CD1  . TYR   B 1 17  ? 37.157 -24.110 -15.974 1.00 16.36 ?  17  TYR   B CD1  1 
ATOM   3959 C CD2  . TYR   B 1 17  ? 37.512 -25.743 -17.673 1.00 17.53 ?  17  TYR   B CD2  1 
ATOM   3960 C CE1  . TYR   B 1 17  ? 36.307 -23.410 -16.815 1.00 17.58 ?  17  TYR   B CE1  1 
ATOM   3961 C CE2  . TYR   B 1 17  ? 36.669 -25.050 -18.523 1.00 18.85 ?  17  TYR   B CE2  1 
ATOM   3962 C CZ   . TYR   B 1 17  ? 36.068 -23.889 -18.087 1.00 19.04 ?  17  TYR   B CZ   1 
ATOM   3963 O OH   . TYR   B 1 17  ? 35.230 -23.198 -18.928 1.00 20.95 ?  17  TYR   B OH   1 
ATOM   3964 H H    . TYR   B 1 17  ? 37.425 -25.670 -13.181 1.00 13.85 ?  17  TYR   B H    1 
ATOM   3965 H HA   . TYR   B 1 17  ? 37.527 -27.698 -14.998 1.00 14.24 ?  17  TYR   B HA   1 
ATOM   3966 H HB2  . TYR   B 1 17  ? 39.212 -25.413 -14.971 1.00 16.09 ?  17  TYR   B HB2  1 
ATOM   3967 H HB3  . TYR   B 1 17  ? 39.278 -26.582 -16.039 1.00 16.09 ?  17  TYR   B HB3  1 
ATOM   3968 H HD1  . TYR   B 1 17  ? 37.318 -23.788 -15.118 1.00 19.64 ?  17  TYR   B HD1  1 
ATOM   3969 H HD2  . TYR   B 1 17  ? 37.910 -26.528 -17.970 1.00 21.04 ?  17  TYR   B HD2  1 
ATOM   3970 H HE1  . TYR   B 1 17  ? 35.901 -22.621 -16.526 1.00 21.11 ?  17  TYR   B HE1  1 
ATOM   3971 H HE2  . TYR   B 1 17  ? 36.498 -25.370 -19.382 1.00 22.63 ?  17  TYR   B HE2  1 
ATOM   3972 H HH   . TYR   B 1 17  ? 35.164 -23.589 -19.668 1.00 25.15 ?  17  TYR   B HH   1 
ATOM   3973 N N    . ILE   B 1 18  ? 39.644 -28.714 -14.016 1.00 11.30 ?  18  ILE   B N    1 
ATOM   3974 C CA   . ILE   B 1 18  ? 40.575 -29.439 -13.153 1.00 11.08 ?  18  ILE   B CA   1 
ATOM   3975 C C    . ILE   B 1 18  ? 41.744 -29.986 -13.966 1.00 11.39 ?  18  ILE   B C    1 
ATOM   3976 O O    . ILE   B 1 18  ? 41.588 -30.393 -15.122 1.00 12.48 ?  18  ILE   B O    1 
ATOM   3977 C CB   . ILE   B 1 18  ? 39.825 -30.536 -12.359 1.00 11.58 ?  18  ILE   B CB   1 
ATOM   3978 C CG1  . ILE   B 1 18  ? 40.668 -31.079 -11.203 1.00 12.10 ?  18  ILE   B CG1  1 
ATOM   3979 C CG2  . ILE   B 1 18  ? 39.333 -31.649 -13.288 1.00 11.97 ?  18  ILE   B CG2  1 
ATOM   3980 C CD1  . ILE   B 1 18  ? 39.831 -31.868 -10.198 1.00 13.91 ?  18  ILE   B CD1  1 
ATOM   3981 H H    . ILE   B 1 18  ? 39.549 -29.060 -14.799 1.00 13.57 ?  18  ILE   B H    1 
ATOM   3982 H HA   . ILE   B 1 18  ? 40.938 -28.823 -12.500 1.00 13.30 ?  18  ILE   B HA   1 
ATOM   3983 H HB   . ILE   B 1 18  ? 39.036 -30.132 -11.968 1.00 13.90 ?  18  ILE   B HB   1 
ATOM   3984 H HG12 . ILE   B 1 18  ? 41.352 -31.667 -11.551 1.00 14.53 ?  18  ILE   B HG12 1 
ATOM   3985 H HG13 . ILE   B 1 18  ? 41.073 -30.332 -10.732 1.00 14.53 ?  18  ILE   B HG13 1 
ATOM   3986 H HG21 . ILE   B 1 18  ? 38.736 -32.235 -12.793 1.00 14.38 ?  18  ILE   B HG21 1 
ATOM   3987 H HG22 . ILE   B 1 18  ? 38.861 -31.250 -14.032 1.00 14.38 ?  18  ILE   B HG22 1 
ATOM   3988 H HG23 . ILE   B 1 18  ? 40.096 -32.154 -13.610 1.00 14.38 ?  18  ILE   B HG23 1 
ATOM   3989 H HD11 . ILE   B 1 18  ? 40.396 -32.141 -9.460  1.00 16.71 ?  18  ILE   B HD11 1 
ATOM   3990 H HD12 . ILE   B 1 18  ? 39.111 -31.303 -9.872  1.00 16.71 ?  18  ILE   B HD12 1 
ATOM   3991 H HD13 . ILE   B 1 18  ? 39.461 -32.649 -10.640 1.00 16.71 ?  18  ILE   B HD13 1 
ATOM   3992 N N    . LYS   B 1 19  ? 42.924 -30.012 -13.342 1.00 11.69 ?  19  LYS   B N    1 
ATOM   3993 C CA   . LYS   B 1 19  ? 44.137 -30.493 -13.991 1.00 12.18 ?  19  LYS   B CA   1 
ATOM   3994 C C    . LYS   B 1 19  ? 45.029 -31.170 -12.961 1.00 11.96 ?  19  LYS   B C    1 
ATOM   3995 O O    . LYS   B 1 19  ? 45.111 -30.727 -11.814 1.00 11.94 ?  19  LYS   B O    1 
ATOM   3996 C CB   . LYS   B 1 19  ? 44.913 -29.332 -14.635 1.00 13.65 ?  19  LYS   B CB   1 
ATOM   3997 C CG   . LYS   B 1 19  ? 46.158 -29.732 -15.413 1.00 15.17 ?  19  LYS   B CG   1 
ATOM   3998 C CD   . LYS   B 1 19  ? 46.872 -28.499 -15.954 1.00 16.76 ?  19  LYS   B CD   1 
ATOM   3999 C CE   . LYS   B 1 19  ? 48.031 -28.870 -16.858 1.00 18.67 ?  19  LYS   B CE   1 
ATOM   4000 N NZ   . LYS   B 1 19  ? 48.775 -27.673 -17.336 1.00 19.96 ?  19  LYS   B NZ   1 
ATOM   4001 H H    . LYS   B 1 19  ? 43.040 -29.756 -12.524 1.00 14.03 ?  19  LYS   B H    1 
ATOM   4002 H HA   . LYS   B 1 19  ? 43.905 -31.139 -14.676 1.00 14.63 ?  19  LYS   B HA   1 
ATOM   4003 H HB2  . LYS   B 1 19  ? 44.315 -28.875 -15.247 1.00 16.39 ?  19  LYS   B HB2  1 
ATOM   4004 H HB3  . LYS   B 1 19  ? 45.183 -28.720 -13.930 1.00 16.39 ?  19  LYS   B HB3  1 
ATOM   4005 H HG2  . LYS   B 1 19  ? 46.763 -30.209 -14.825 1.00 18.21 ?  19  LYS   B HG2  1 
ATOM   4006 H HG3  . LYS   B 1 19  ? 45.897 -30.294 -16.160 1.00 18.21 ?  19  LYS   B HG3  1 
ATOM   4007 H HD2  . LYS   B 1 19  ? 46.242 -27.965 -16.464 1.00 20.12 ?  19  LYS   B HD2  1 
ATOM   4008 H HD3  . LYS   B 1 19  ? 47.219 -27.982 -15.208 1.00 20.12 ?  19  LYS   B HD3  1 
ATOM   4009 H HE2  . LYS   B 1 19  ? 48.646 -29.438 -16.369 1.00 22.41 ?  19  LYS   B HE2  1 
ATOM   4010 H HE3  . LYS   B 1 19  ? 47.686 -29.344 -17.633 1.00 22.41 ?  19  LYS   B HE3  1 
ATOM   4011 H HZ1  . LYS   B 1 19  ? 49.405 -27.920 -17.914 1.00 23.96 ?  19  LYS   B HZ1  1 
ATOM   4012 H HZ2  . LYS   B 1 19  ? 48.218 -27.109 -17.739 1.00 23.96 ?  19  LYS   B HZ2  1 
ATOM   4013 H HZ3  . LYS   B 1 19  ? 49.159 -27.261 -16.648 1.00 23.96 ?  19  LYS   B HZ3  1 
ATOM   4014 N N    . ASN   B 1 20  ? 45.720 -32.223 -13.390 1.00 12.87 ?  20  ASN   B N    1 
ATOM   4015 C CA   . ASN   B 1 20  ? 46.758 -32.849 -12.578 1.00 13.77 ?  20  ASN   B CA   1 
ATOM   4016 C C    . ASN   B 1 20  ? 48.025 -32.025 -12.771 1.00 14.26 ?  20  ASN   B C    1 
ATOM   4017 O O    . ASN   B 1 20  ? 48.683 -32.111 -13.813 1.00 16.21 ?  20  ASN   B O    1 
ATOM   4018 C CB   . ASN   B 1 20  ? 46.941 -34.298 -13.020 1.00 14.88 ?  20  ASN   B CB   1 
ATOM   4019 C CG   . ASN   B 1 20  ? 48.090 -35.003 -12.323 1.00 16.32 ?  20  ASN   B CG   1 
ATOM   4020 O OD1  . ASN   B 1 20  ? 48.757 -35.851 -12.921 1.00 18.74 ?  20  ASN   B OD1  1 
ATOM   4021 N ND2  . ASN   B 1 20  ? 48.320 -34.675 -11.062 1.00 15.84 ?  20  ASN   B ND2  1 
ATOM   4022 H H    . ASN   B 1 20  ? 45.605 -32.595 -14.156 1.00 15.46 ?  20  ASN   B H    1 
ATOM   4023 H HA   . ASN   B 1 20  ? 46.492 -32.833 -11.643 1.00 16.53 ?  20  ASN   B HA   1 
ATOM   4024 H HB2  . ASN   B 1 20  ? 46.130 -34.792 -12.825 1.00 17.86 ?  20  ASN   B HB2  1 
ATOM   4025 H HB3  . ASN   B 1 20  ? 47.116 -34.311 -13.973 1.00 17.86 ?  20  ASN   B HB3  1 
ATOM   4026 H HD21 . ASN   B 1 20  ? 48.964 -35.043 -10.631 1.00 19.02 ?  20  ASN   B HD21 1 
ATOM   4027 H HD22 . ASN   B 1 20  ? 47.829 -34.081 -10.667 1.00 19.02 ?  20  ASN   B HD22 1 
ATOM   4028 N N    . ALA   B 1 21  ? 48.364 -31.210 -11.771 1.00 14.10 ?  21  ALA   B N    1 
ATOM   4029 C CA   . ALA   B 1 21  ? 49.465 -30.268 -11.913 1.00 14.88 ?  21  ALA   B CA   1 
ATOM   4030 C C    . ALA   B 1 21  ? 49.923 -29.782 -10.546 1.00 14.06 ?  21  ALA   B C    1 
ATOM   4031 O O    . ALA   B 1 21  ? 49.174 -29.811 -9.567  1.00 14.18 ?  21  ALA   B O    1 
ATOM   4032 C CB   . ALA   B 1 21  ? 49.061 -29.075 -12.783 1.00 16.32 ?  21  ALA   B CB   1 
ATOM   4033 H H    . ALA   B 1 21  ? 47.970 -31.184 -11.001 1.00 16.92 ?  21  ALA   B H    1 
ATOM   4034 H HA   . ALA   B 1 21  ? 50.207 -30.718 -12.339 1.00 17.87 ?  21  ALA   B HA   1 
ATOM   4035 H HB1  . ALA   B 1 21  ? 49.839 -28.522 -12.927 1.00 19.60 ?  21  ALA   B HB1  1 
ATOM   4036 H HB2  . ALA   B 1 21  ? 48.726 -29.410 -13.630 1.00 19.60 ?  21  ALA   B HB2  1 
ATOM   4037 H HB3  . ALA   B 1 21  ? 48.365 -28.574 -12.328 1.00 19.60 ?  21  ALA   B HB3  1 
ATOM   4038 N N    . ASP   B 1 22  ? 51.179 -29.336 -10.515 1.00 13.91 ?  22  ASP   B N    1 
ATOM   4039 C CA   . ASP   B 1 22  ? 51.782 -28.644 -9.382  1.00 13.36 ?  22  ASP   B CA   1 
ATOM   4040 C C    . ASP   B 1 22  ? 51.379 -27.173 -9.470  1.00 12.33 ?  22  ASP   B C    1 
ATOM   4041 O O    . ASP   B 1 22  ? 51.702 -26.503 -10.454 1.00 12.66 ?  22  ASP   B O    1 
ATOM   4042 C CB   . ASP   B 1 22  ? 53.298 -28.814 -9.527  1.00 14.79 ?  22  ASP   B CB   1 
ATOM   4043 C CG   . ASP   B 1 22  ? 54.114 -28.059 -8.484  1.00 16.68 ?  22  ASP   B CG   1 
ATOM   4044 O OD1  . ASP   B 1 22  ? 53.726 -26.953 -8.068  1.00 17.17 ?  22  ASP   B OD1  1 
ATOM   4045 O OD2  . ASP   B 1 22  ? 55.193 -28.572 -8.105  1.00 19.03 -1 22  ASP   B OD2  1 
ATOM   4046 H H    . ASP   B 1 22  ? 51.729 -29.433 -11.175 1.00 16.70 ?  22  ASP   B H    1 
ATOM   4047 H HA   . ASP   B 1 22  ? 51.485 -29.028 -8.541  1.00 16.04 ?  22  ASP   B HA   1 
ATOM   4048 H HB2  . ASP   B 1 22  ? 53.523 -29.750 -9.451  1.00 17.76 ?  22  ASP   B HB2  1 
ATOM   4049 H HB3  . ASP   B 1 22  ? 53.568 -28.478 -10.398 1.00 17.76 ?  22  ASP   B HB3  1 
ATOM   4050 N N    . ILE   B 1 23  ? 50.661 -26.678 -8.456  1.00 11.80 ?  23  ILE   B N    1 
ATOM   4051 C CA   . ILE   B 1 23  ? 50.069 -25.340 -8.531  1.00 11.47 ?  23  ILE   B CA   1 
ATOM   4052 C C    . ILE   B 1 23  ? 51.123 -24.248 -8.669  1.00 11.14 ?  23  ILE   B C    1 
ATOM   4053 O O    . ILE   B 1 23  ? 50.852 -23.203 -9.271  1.00 11.08 ?  23  ILE   B O    1 
ATOM   4054 C CB   . ILE   B 1 23  ? 49.120 -25.099 -7.338  1.00 12.03 ?  23  ILE   B CB   1 
ATOM   4055 C CG1  . ILE   B 1 23  ? 48.284 -23.833 -7.543  1.00 12.59 ?  23  ILE   B CG1  1 
ATOM   4056 C CG2  . ILE   B 1 23  ? 49.885 -25.054 -6.029  1.00 12.94 ?  23  ILE   B CG2  1 
ATOM   4057 C CD1  . ILE   B 1 23  ? 47.171 -23.675 -6.529  1.00 13.23 ?  23  ILE   B CD1  1 
ATOM   4058 H H    . ILE   B 1 23  ? 50.511 -27.096 -7.719  1.00 14.17 ?  23  ILE   B H    1 
ATOM   4059 H HA   . ILE   B 1 23  ? 49.526 -25.305 -9.331  1.00 13.78 ?  23  ILE   B HA   1 
ATOM   4060 H HB   . ILE   B 1 23  ? 48.507 -25.850 -7.297  1.00 14.44 ?  23  ILE   B HB   1 
ATOM   4061 H HG12 . ILE   B 1 23  ? 48.865 -23.057 -7.471  1.00 15.12 ?  23  ILE   B HG12 1 
ATOM   4062 H HG13 . ILE   B 1 23  ? 47.883 -23.859 -8.428  1.00 15.12 ?  23  ILE   B HG13 1 
ATOM   4063 H HG21 . ILE   B 1 23  ? 49.253 -25.058 -5.293  1.00 15.54 ?  23  ILE   B HG21 1 
ATOM   4064 H HG22 . ILE   B 1 23  ? 50.460 -25.834 -5.973  1.00 15.54 ?  23  ILE   B HG22 1 
ATOM   4065 H HG23 . ILE   B 1 23  ? 50.421 -24.247 -6.002  1.00 15.54 ?  23  ILE   B HG23 1 
ATOM   4066 H HD11 . ILE   B 1 23  ? 46.630 -22.911 -6.773  1.00 15.88 ?  23  ILE   B HD11 1 
ATOM   4067 H HD12 . ILE   B 1 23  ? 46.629 -24.482 -6.537  1.00 15.88 ?  23  ILE   B HD12 1 
ATOM   4068 H HD13 . ILE   B 1 23  ? 47.560 -23.546 -5.653  1.00 15.88 ?  23  ILE   B HD13 1 
ATOM   4069 N N    . VAL   B 1 24  ? 52.317 -24.448 -8.103  1.00 11.60 ?  24  VAL   B N    1 
ATOM   4070 C CA   . VAL   B 1 24  ? 53.393 -23.471 -8.271  1.00 12.01 ?  24  VAL   B CA   1 
ATOM   4071 C C    . VAL   B 1 24  ? 53.842 -23.422 -9.725  1.00 11.99 ?  24  VAL   B C    1 
ATOM   4072 O O    . VAL   B 1 24  ? 53.984 -22.344 -10.319 1.00 12.74 ?  24  VAL   B O    1 
ATOM   4073 C CB   . VAL   B 1 24  ? 54.574 -23.792 -7.332  1.00 13.14 ?  24  VAL   B CB   1 
ATOM   4074 C CG1  . VAL   B 1 24  ? 55.787 -22.924 -7.666  1.00 13.83 ?  24  VAL   B CG1  1 
ATOM   4075 C CG2  . VAL   B 1 24  ? 54.168 -23.603 -5.889  1.00 14.28 ?  24  VAL   B CG2  1 
ATOM   4076 H H    . VAL   B 1 24  ? 52.526 -25.131 -7.624  1.00 13.93 ?  24  VAL   B H    1 
ATOM   4077 H HA   . VAL   B 1 24  ? 53.060 -22.594 -8.035  1.00 14.43 ?  24  VAL   B HA   1 
ATOM   4078 H HB   . VAL   B 1 24  ? 54.831 -24.721 -7.447  1.00 15.78 ?  24  VAL   B HB   1 
ATOM   4079 H HG11 . VAL   B 1 24  ? 56.382 -22.909 -6.899  1.00 16.61 ?  24  VAL   B HG11 1 
ATOM   4080 H HG12 . VAL   B 1 24  ? 56.245 -23.307 -8.430  1.00 16.61 ?  24  VAL   B HG12 1 
ATOM   4081 H HG13 . VAL   B 1 24  ? 55.486 -22.027 -7.869  1.00 16.61 ?  24  VAL   B HG13 1 
ATOM   4082 H HG21 . VAL   B 1 24  ? 54.892 -23.892 -5.314  1.00 17.14 ?  24  VAL   B HG21 1 
ATOM   4083 H HG22 . VAL   B 1 24  ? 53.978 -22.664 -5.737  1.00 17.14 ?  24  VAL   B HG22 1 
ATOM   4084 H HG23 . VAL   B 1 24  ? 53.374 -24.134 -5.712  1.00 17.14 ?  24  VAL   B HG23 1 
ATOM   4085 N N    . GLU   B 1 25  ? 54.100 -24.593 -10.313 1.00 12.85 ?  25  GLU   B N    1 
ATOM   4086 C CA   . GLU   B 1 25  ? 54.496 -24.634 -11.715 1.00 14.17 ?  25  GLU   B CA   1 
ATOM   4087 C C    . GLU   B 1 25  ? 53.398 -24.076 -12.606 1.00 13.03 ?  25  GLU   B C    1 
ATOM   4088 O O    . GLU   B 1 25  ? 53.673 -23.361 -13.578 1.00 14.04 ?  25  GLU   B O    1 
ATOM   4089 C CB   . GLU   B 1 25  ? 54.872 -26.063 -12.108 1.00 17.48 ?  25  GLU   B CB   1 
ATOM   4090 C CG   . GLU   B 1 25  ? 56.160 -26.527 -11.452 1.00 22.85 ?  25  GLU   B CG   1 
ATOM   4091 C CD   . GLU   B 1 25  ? 57.281 -25.503 -11.559 1.00 27.70 ?  25  GLU   B CD   1 
ATOM   4092 O OE1  . GLU   B 1 25  ? 57.660 -25.148 -12.696 1.00 29.51 ?  25  GLU   B OE1  1 
ATOM   4093 O OE2  . GLU   B 1 25  ? 57.769 -25.033 -10.506 1.00 29.40 -1 25  GLU   B OE2  1 
ATOM   4094 H H    . GLU   B 1 25  ? 54.045 -25.364 -9.929  1.00 15.42 ?  25  GLU   B H    1 
ATOM   4095 H HA   . GLU   B 1 25  ? 55.261 -24.062 -11.836 1.00 17.01 ?  25  GLU   B HA   1 
ATOM   4096 H HB2  . GLU   B 1 25  ? 54.163 -26.670 -11.830 1.00 20.99 ?  25  GLU   B HB2  1 
ATOM   4097 H HB3  . GLU   B 1 25  ? 54.987 -26.111 -13.069 1.00 20.99 ?  25  GLU   B HB3  1 
ATOM   4098 H HG2  . GLU   B 1 25  ? 56.003 -26.680 -10.512 1.00 27.42 ?  25  GLU   B HG2  1 
ATOM   4099 H HG3  . GLU   B 1 25  ? 56.459 -27.343 -11.884 1.00 27.42 ?  25  GLU   B HG3  1 
ATOM   4100 N N    . GLU   B 1 26  ? 52.143 -24.379 -12.277 1.00 12.51 ?  26  GLU   B N    1 
ATOM   4101 C CA   . GLU   B 1 26  ? 51.023 -23.846 -13.044 1.00 12.96 ?  26  GLU   B CA   1 
ATOM   4102 C C    . GLU   B 1 26  ? 50.978 -22.327 -12.956 1.00 12.50 ?  26  GLU   B C    1 
ATOM   4103 O O    . GLU   B 1 26  ? 50.775 -21.645 -13.966 1.00 13.77 ?  26  GLU   B O    1 
ATOM   4104 C CB   . GLU   B 1 26  ? 49.705 -24.427 -12.530 1.00 14.58 ?  26  GLU   B CB   1 
ATOM   4105 C CG   . GLU   B 1 26  ? 49.319 -25.744 -13.146 1.00 17.99 ?  26  GLU   B CG   1 
ATOM   4106 C CD   . GLU   B 1 26  ? 49.080 -25.649 -14.646 1.00 19.85 ?  26  GLU   B CD   1 
ATOM   4107 O OE1  . GLU   B 1 26  ? 48.135 -24.956 -15.082 1.00 19.80 ?  26  GLU   B OE1  1 
ATOM   4108 O OE2  . GLU   B 1 26  ? 49.841 -26.283 -15.389 1.00 21.65 -1 26  GLU   B OE2  1 
ATOM   4109 H H    . GLU   B 1 26  ? 51.909 -24.887 -11.616 1.00 15.02 ?  26  GLU   B H    1 
ATOM   4110 H HA   . GLU   B 1 26  ? 51.126 -24.091 -13.975 1.00 15.57 ?  26  GLU   B HA   1 
ATOM   4111 H HB2  . GLU   B 1 26  ? 49.775 -24.561 -11.573 1.00 17.50 ?  26  GLU   B HB2  1 
ATOM   4112 H HB3  . GLU   B 1 26  ? 48.992 -23.795 -12.720 1.00 17.50 ?  26  GLU   B HB3  1 
ATOM   4113 H HG2  . GLU   B 1 26  ? 50.036 -26.373 -12.992 1.00 21.59 ?  26  GLU   B HG2  1 
ATOM   4114 H HG3  . GLU   B 1 26  ? 48.499 -26.057 -12.735 1.00 21.59 ?  26  GLU   B HG3  1 
ATOM   4115 N N    . ALA   B 1 27  ? 51.122 -21.782 -11.746 1.00 11.76 ?  27  ALA   B N    1 
ATOM   4116 C CA   . ALA   B 1 27  ? 51.084 -20.330 -11.587 1.00 12.21 ?  27  ALA   B CA   1 
ATOM   4117 C C    . ALA   B 1 27  ? 52.153 -19.659 -12.436 1.00 13.04 ?  27  ALA   B C    1 
ATOM   4118 O O    . ALA   B 1 27  ? 51.890 -18.653 -13.112 1.00 13.62 ?  27  ALA   B O    1 
ATOM   4119 C CB   . ALA   B 1 27  ? 51.236 -19.957 -10.113 1.00 12.59 ?  27  ALA   B CB   1 
ATOM   4120 H H    . ALA   B 1 27  ? 51.237 -22.225 -11.014 1.00 14.12 ?  27  ALA   B H    1 
ATOM   4121 H HA   . ALA   B 1 27  ? 50.226 -20.005 -11.885 1.00 14.67 ?  27  ALA   B HA   1 
ATOM   4122 H HB1  . ALA   B 1 27  ? 51.203 -18.994 -10.026 1.00 15.11 ?  27  ALA   B HB1  1 
ATOM   4123 H HB2  . ALA   B 1 27  ? 50.504 -20.358 -9.611  1.00 15.11 ?  27  ALA   B HB2  1 
ATOM   4124 H HB3  . ALA   B 1 27  ? 52.082 -20.295 -9.783  1.00 15.11 ?  27  ALA   B HB3  1 
ATOM   4125 N N    . LYS   B 1 28  ? 53.368 -20.205 -12.419 1.00 14.35 ?  28  LYS   B N    1 
ATOM   4126 C CA   . LYS   B 1 28  ? 54.446 -19.589 -13.183 1.00 16.47 ?  28  LYS   B CA   1 
ATOM   4127 C C    . LYS   B 1 28  ? 54.186 -19.659 -14.682 1.00 17.48 ?  28  LYS   B C    1 
ATOM   4128 O O    . LYS   B 1 28  ? 54.608 -18.763 -15.424 1.00 18.52 ?  28  LYS   B O    1 
ATOM   4129 C CB   . LYS   B 1 28  ? 55.795 -20.201 -12.800 1.00 19.01 ?  28  LYS   B CB   1 
ATOM   4130 C CG   . LYS   B 1 28  ? 56.199 -19.881 -11.364 1.00 21.92 ?  28  LYS   B CG   1 
ATOM   4131 C CD   . LYS   B 1 28  ? 57.622 -20.303 -11.036 1.00 25.88 ?  28  LYS   B CD   1 
ATOM   4132 C CE   . LYS   B 1 28  ? 57.706 -21.778 -10.715 1.00 28.84 ?  28  LYS   B CE   1 
ATOM   4133 N NZ   . LYS   B 1 28  ? 59.045 -22.148 -10.174 1.00 29.83 ?  28  LYS   B NZ   1 
ATOM   4134 H H    . LYS   B 1 28  ? 53.598 -20.908 -11.975 1.00 17.23 ?  28  LYS   B H    1 
ATOM   4135 H HA   . LYS   B 1 28  ? 54.488 -18.650 -12.946 1.00 19.78 ?  28  LYS   B HA   1 
ATOM   4136 H HB2  . LYS   B 1 28  ? 55.747 -21.163 -12.888 1.00 22.83 ?  28  LYS   B HB2  1 
ATOM   4137 H HB3  . LYS   B 1 28  ? 56.483 -19.846 -13.387 1.00 22.83 ?  28  LYS   B HB3  1 
ATOM   4138 H HG2  . LYS   B 1 28  ? 56.129 -18.923 -11.225 1.00 26.32 ?  28  LYS   B HG2  1 
ATOM   4139 H HG3  . LYS   B 1 28  ? 55.600 -20.346 -10.760 1.00 26.32 ?  28  LYS   B HG3  1 
ATOM   4140 H HD2  . LYS   B 1 28  ? 58.191 -20.123 -11.801 1.00 31.07 ?  28  LYS   B HD2  1 
ATOM   4141 H HD3  . LYS   B 1 28  ? 57.931 -19.802 -10.264 1.00 31.07 ?  28  LYS   B HD3  1 
ATOM   4142 H HE2  . LYS   B 1 28  ? 57.037 -21.998 -10.047 1.00 34.62 ?  28  LYS   B HE2  1 
ATOM   4143 H HE3  . LYS   B 1 28  ? 57.552 -22.292 -11.523 1.00 34.62 ?  28  LYS   B HE3  1 
ATOM   4144 H HZ1  . LYS   B 1 28  ? 59.070 -23.019 -9.991  1.00 35.80 ?  28  LYS   B HZ1  1 
ATOM   4145 H HZ2  . LYS   B 1 28  ? 59.677 -21.959 -10.771 1.00 35.80 ?  28  LYS   B HZ2  1 
ATOM   4146 H HZ3  . LYS   B 1 28  ? 59.207 -21.692 -9.426  1.00 35.80 ?  28  LYS   B HZ3  1 
ATOM   4147 N N    A LYS   B 1 29  ? 53.489 -20.701 -15.143 0.86 18.20 ?  29  LYS   B N    1 
ATOM   4148 N N    B LYS   B 1 29  ? 53.462 -20.678 -15.142 0.14 18.76 ?  29  LYS   B N    1 
ATOM   4149 C CA   A LYS   B 1 29  ? 53.201 -20.842 -16.567 0.86 20.29 ?  29  LYS   B CA   1 
ATOM   4150 C CA   B LYS   B 1 29  ? 53.201 -20.819 -16.570 0.14 20.17 ?  29  LYS   B CA   1 
ATOM   4151 C C    A LYS   B 1 29  ? 51.961 -20.057 -16.989 0.86 19.35 ?  29  LYS   B C    1 
ATOM   4152 C C    B LYS   B 1 29  ? 51.940 -20.083 -17.010 0.14 19.19 ?  29  LYS   B C    1 
ATOM   4153 O O    A LYS   B 1 29  ? 51.974 -19.395 -18.033 0.86 20.71 ?  29  LYS   B O    1 
ATOM   4154 O O    B LYS   B 1 29  ? 51.924 -19.470 -18.084 0.14 19.50 ?  29  LYS   B O    1 
ATOM   4155 C CB   A LYS   B 1 29  ? 53.037 -22.320 -16.924 0.86 24.20 ?  29  LYS   B CB   1 
ATOM   4156 C CB   B LYS   B 1 29  ? 53.098 -22.301 -16.941 0.14 22.66 ?  29  LYS   B CB   1 
ATOM   4157 C CG   A LYS   B 1 29  ? 52.834 -22.573 -18.409 0.86 27.74 ?  29  LYS   B CG   1 
ATOM   4158 C CG   B LYS   B 1 29  ? 52.891 -22.554 -18.427 0.14 24.90 ?  29  LYS   B CG   1 
ATOM   4159 C CD   A LYS   B 1 29  ? 53.064 -24.035 -18.762 0.86 30.58 ?  29  LYS   B CD   1 
ATOM   4160 C CD   B LYS   B 1 29  ? 53.131 -24.015 -18.788 0.14 26.68 ?  29  LYS   B CD   1 
ATOM   4161 C CE   A LYS   B 1 29  ? 51.952 -24.926 -18.237 0.86 32.55 ?  29  LYS   B CE   1 
ATOM   4162 C CE   B LYS   B 1 29  ? 52.077 -24.932 -18.186 0.14 27.91 ?  29  LYS   B CE   1 
ATOM   4163 N NZ   A LYS   B 1 29  ? 52.171 -26.353 -18.613 0.86 33.66 ?  29  LYS   B NZ   1 
ATOM   4164 N NZ   B LYS   B 1 29  ? 52.319 -26.359 -18.542 0.14 28.62 ?  29  LYS   B NZ   1 
ATOM   4165 H H    A LYS   B 1 29  ? 53.177 -21.335 -14.648 0.86 21.85 ?  29  LYS   B H    1 
ATOM   4166 H H    B LYS   B 1 29  ? 53.107 -21.290 -14.647 0.14 22.52 ?  29  LYS   B H    1 
ATOM   4167 H HA   A LYS   B 1 29  ? 53.950 -20.497 -17.068 0.86 24.36 ?  29  LYS   B HA   1 
ATOM   4168 H HA   B LYS   B 1 29  ? 53.947 -20.445 -17.056 0.14 24.21 ?  29  LYS   B HA   1 
ATOM   4169 H HB2  A LYS   B 1 29  ? 53.838 -22.796 -16.651 0.86 29.05 ?  29  LYS   B HB2  1 
ATOM   4170 H HB2  B LYS   B 1 29  ? 53.920 -22.741 -16.677 0.14 27.20 ?  29  LYS   B HB2  1 
ATOM   4171 H HB3  A LYS   B 1 29  ? 52.268 -22.675 -16.455 0.86 29.05 ?  29  LYS   B HB3  1 
ATOM   4172 H HB3  B LYS   B 1 29  ? 52.349 -22.689 -16.466 0.14 27.20 ?  29  LYS   B HB3  1 
ATOM   4173 H HG2  A LYS   B 1 29  ? 51.923 -22.342 -18.651 0.86 33.30 ?  29  LYS   B HG2  1 
ATOM   4174 H HG2  B LYS   B 1 29  ? 51.978 -22.328 -18.664 0.14 29.89 ?  29  LYS   B HG2  1 
ATOM   4175 H HG3  A LYS   B 1 29  ? 53.463 -22.035 -18.915 0.86 33.30 ?  29  LYS   B HG3  1 
ATOM   4176 H HG3  B LYS   B 1 29  ? 53.513 -22.009 -18.934 0.14 29.89 ?  29  LYS   B HG3  1 
ATOM   4177 H HD2  A LYS   B 1 29  ? 53.099 -24.130 -19.726 0.86 36.70 ?  29  LYS   B HD2  1 
ATOM   4178 H HD2  B LYS   B 1 29  ? 53.102 -24.114 -19.753 0.14 32.02 ?  29  LYS   B HD2  1 
ATOM   4179 H HD3  A LYS   B 1 29  ? 53.900 -24.332 -18.367 0.86 36.70 ?  29  LYS   B HD3  1 
ATOM   4180 H HD3  B LYS   B 1 29  ? 53.998 -24.290 -18.450 0.14 32.02 ?  29  LYS   B HD3  1 
ATOM   4181 H HE2  A LYS   B 1 29  ? 51.922 -24.868 -17.269 0.86 39.07 ?  29  LYS   B HE2  1 
ATOM   4182 H HE2  B LYS   B 1 29  ? 52.098 -24.855 -17.219 0.14 33.50 ?  29  LYS   B HE2  1 
ATOM   4183 H HE3  A LYS   B 1 29  ? 51.106 -24.638 -18.616 0.86 39.07 ?  29  LYS   B HE3  1 
ATOM   4184 H HE3  B LYS   B 1 29  ? 51.203 -24.679 -18.523 0.14 33.50 ?  29  LYS   B HE3  1 
ATOM   4185 H HZ1  A LYS   B 1 29  ? 51.508 -26.856 -18.297 0.86 40.40 ?  29  LYS   B HZ1  1 
ATOM   4186 H HZ1  B LYS   B 1 29  ? 51.690 -26.874 -18.179 0.14 34.35 ?  29  LYS   B HZ1  1 
ATOM   4187 H HZ2  A LYS   B 1 29  ? 52.198 -26.433 -19.499 0.86 40.40 ?  29  LYS   B HZ2  1 
ATOM   4188 H HZ2  B LYS   B 1 29  ? 52.300 -26.459 -19.426 0.14 34.35 ?  29  LYS   B HZ2  1 
ATOM   4189 H HZ3  A LYS   B 1 29  ? 52.941 -26.642 -18.273 0.86 40.40 ?  29  LYS   B HZ3  1 
ATOM   4190 H HZ3  B LYS   B 1 29  ? 53.115 -26.617 -18.239 0.14 34.35 ?  29  LYS   B HZ3  1 
ATOM   4191 N N    . VAL   B 1 30  ? 50.883 -20.137 -16.200 1.00 18.09 ?  30  VAL   B N    1 
ATOM   4192 C CA   . VAL   B 1 30  ? 49.600 -19.528 -16.573 1.00 18.09 ?  30  VAL   B CA   1 
ATOM   4193 C C    . VAL   B 1 30  ? 49.600 -18.012 -16.407 1.00 17.34 ?  30  VAL   B C    1 
ATOM   4194 O O    . VAL   B 1 30  ? 48.857 -17.303 -17.104 1.00 18.51 ?  30  VAL   B O    1 
ATOM   4195 C CB   . VAL   B 1 30  ? 48.492 -20.162 -15.708 1.00 19.19 ?  30  VAL   B CB   1 
ATOM   4196 C CG1  . VAL   B 1 30  ? 47.205 -19.348 -15.775 1.00 18.94 ?  30  VAL   B CG1  1 
ATOM   4197 C CG2  . VAL   B 1 30  ? 48.243 -21.612 -16.119 1.00 19.83 ?  30  VAL   B CG2  1 
ATOM   4198 H H    A VAL   B 1 30  ? 50.863 -20.551 -15.439 0.86 21.72 ?  30  VAL   B H    1 
ATOM   4199 H H    B VAL   B 1 30  ? 50.869 -20.546 -15.436 0.14 21.72 ?  30  VAL   B H    1 
ATOM   4200 H HA   . VAL   B 1 30  ? 49.405 -19.750 -17.498 1.00 21.72 ?  30  VAL   B HA   1 
ATOM   4201 H HB   . VAL   B 1 30  ? 48.781 -20.174 -14.781 1.00 23.03 ?  30  VAL   B HB   1 
ATOM   4202 H HG11 . VAL   B 1 30  ? 46.463 -19.928 -15.545 1.00 22.74 ?  30  VAL   B HG11 1 
ATOM   4203 H HG12 . VAL   B 1 30  ? 47.259 -18.618 -15.142 1.00 22.74 ?  30  VAL   B HG12 1 
ATOM   4204 H HG13 . VAL   B 1 30  ? 47.090 -19.016 -16.674 1.00 22.74 ?  30  VAL   B HG13 1 
ATOM   4205 H HG21 . VAL   B 1 30  ? 47.545 -21.991 -15.555 1.00 23.80 ?  30  VAL   B HG21 1 
ATOM   4206 H HG22 . VAL   B 1 30  ? 47.957 -21.634 -17.047 1.00 23.80 ?  30  VAL   B HG22 1 
ATOM   4207 H HG23 . VAL   B 1 30  ? 49.061 -22.118 -16.012 1.00 23.80 ?  30  VAL   B HG23 1 
ATOM   4208 N N    . LYS   B 1 31  ? 50.378 -17.505 -15.463 1.00 17.24 ?  31  LYS   B N    1 
ATOM   4209 C CA   . LYS   B 1 31  ? 50.386 -16.094 -15.100 1.00 17.63 ?  31  LYS   B CA   1 
ATOM   4210 C C    . LYS   B 1 31  ? 48.977 -15.642 -14.715 1.00 15.42 ?  31  LYS   B C    1 
ATOM   4211 O O    . LYS   B 1 31  ? 48.420 -14.725 -15.337 1.00 16.64 ?  31  LYS   B O    1 
ATOM   4212 C CB   . LYS   B 1 31  ? 51.003 -15.261 -16.230 1.00 20.84 ?  31  LYS   B CB   1 
ATOM   4213 C CG   . LYS   B 1 31  ? 52.401 -15.743 -16.626 1.00 23.85 ?  31  LYS   B CG   1 
ATOM   4214 C CD   . LYS   B 1 31  ? 52.974 -14.969 -17.795 1.00 26.84 ?  31  LYS   B CD   1 
ATOM   4215 C CE   . LYS   B 1 31  ? 54.442 -15.295 -17.986 1.00 29.16 ?  31  LYS   B CE   1 
ATOM   4216 N NZ   . LYS   B 1 31  ? 55.241 -14.953 -16.776 1.00 30.12 ?  31  LYS   B NZ   1 
ATOM   4217 H H    . LYS   B 1 31  ? 50.923 -17.988 -15.007 1.00 20.70 ?  31  LYS   B H    1 
ATOM   4218 H HA   . LYS   B 1 31  ? 50.944 -16.000 -14.326 1.00 21.16 ?  31  LYS   B HA   1 
ATOM   4219 H HB2  . LYS   B 1 31  ? 50.432 -15.312 -17.013 1.00 25.01 ?  31  LYS   B HB2  1 
ATOM   4220 H HB3  . LYS   B 1 31  ? 51.074 -14.344 -15.927 1.00 25.01 ?  31  LYS   B HB3  1 
ATOM   4221 H HG2  . LYS   B 1 31  ? 52.991 -15.638 -15.865 1.00 28.63 ?  31  LYS   B HG2  1 
ATOM   4222 H HG3  . LYS   B 1 31  ? 52.352 -16.681 -16.879 1.00 28.63 ?  31  LYS   B HG3  1 
ATOM   4223 H HD2  . LYS   B 1 31  ? 52.495 -15.214 -18.603 1.00 32.21 ?  31  LYS   B HD2  1 
ATOM   4224 H HD3  . LYS   B 1 31  ? 52.886 -14.021 -17.622 1.00 32.21 ?  31  LYS   B HD3  1 
ATOM   4225 H HE2  . LYS   B 1 31  ? 54.539 -16.247 -18.154 1.00 35.00 ?  31  LYS   B HE2  1 
ATOM   4226 H HE3  . LYS   B 1 31  ? 54.787 -14.785 -18.733 1.00 35.00 ?  31  LYS   B HE3  1 
ATOM   4227 H HZ1  . LYS   B 1 31  ? 56.110 -15.012 -16.959 1.00 36.15 ?  31  LYS   B HZ1  1 
ATOM   4228 H HZ2  . LYS   B 1 31  ? 55.056 -14.122 -16.515 1.00 36.15 ?  31  LYS   B HZ2  1 
ATOM   4229 H HZ3  . LYS   B 1 31  ? 55.048 -15.513 -16.111 1.00 36.15 ?  31  LYS   B HZ3  1 
ATOM   4230 N N    . PRO   B 1 32  ? 48.372 -16.258 -13.690 1.00 12.95 ?  32  PRO   B N    1 
ATOM   4231 C CA   . PRO   B 1 32  ? 46.988 -15.917 -13.337 1.00 11.76 ?  32  PRO   B CA   1 
ATOM   4232 C C    . PRO   B 1 32  ? 46.894 -14.570 -12.638 1.00 11.95 ?  32  PRO   B C    1 
ATOM   4233 O O    . PRO   B 1 32  ? 47.814 -14.136 -11.936 1.00 13.27 ?  32  PRO   B O    1 
ATOM   4234 C CB   . PRO   B 1 32  ? 46.593 -17.043 -12.374 1.00 12.17 ?  32  PRO   B CB   1 
ATOM   4235 C CG   . PRO   B 1 32  ? 47.890 -17.380 -11.690 1.00 12.60 ?  32  PRO   B CG   1 
ATOM   4236 C CD   . PRO   B 1 32  ? 48.943 -17.253 -12.759 1.00 12.69 ?  32  PRO   B CD   1 
ATOM   4237 H HA   . PRO   B 1 32  ? 46.408 -15.936 -14.121 1.00 14.13 ?  32  PRO   B HA   1 
ATOM   4238 H HB2  . PRO   B 1 32  ? 45.936 -16.723 -11.735 1.00 14.61 ?  32  PRO   B HB2  1 
ATOM   4239 H HB3  . PRO   B 1 32  ? 46.255 -17.807 -12.868 1.00 14.61 ?  32  PRO   B HB3  1 
ATOM   4240 H HG2  . PRO   B 1 32  ? 48.051 -16.748 -10.970 1.00 15.13 ?  32  PRO   B HG2  1 
ATOM   4241 H HG3  . PRO   B 1 32  ? 47.855 -18.287 -11.347 1.00 15.13 ?  32  PRO   B HG3  1 
ATOM   4242 H HD2  . PRO   B 1 32  ? 49.766 -16.918 -12.377 1.00 15.24 ?  32  PRO   B HD2  1 
ATOM   4243 H HD3  . PRO   B 1 32  ? 49.069 -18.102 -13.204 1.00 15.24 ?  32  PRO   B HD3  1 
ATOM   4244 N N    . THR   B 1 33  ? 45.740 -13.922 -12.814 1.00 11.33 ?  33  THR   B N    1 
ATOM   4245 C CA   . THR   B 1 33  ? 45.432 -12.745 -12.009 1.00 11.72 ?  33  THR   B CA   1 
ATOM   4246 C C    . THR   B 1 33  ? 45.382 -13.096 -10.528 1.00 11.26 ?  33  THR   B C    1 
ATOM   4247 O O    . THR   B 1 33  ? 45.842 -12.311 -9.685  1.00 12.40 ?  33  THR   B O    1 
ATOM   4248 C CB   . THR   B 1 33  ? 44.111 -12.119 -12.463 1.00 12.26 ?  33  THR   B CB   1 
ATOM   4249 O OG1  . THR   B 1 33  ? 44.163 -11.850 -13.867 1.00 12.47 ?  33  THR   B OG1  1 
ATOM   4250 C CG2  . THR   B 1 33  ? 43.833 -10.826 -11.705 1.00 13.46 ?  33  THR   B CG2  1 
ATOM   4251 H H    . THR   B 1 33  ? 45.122 -14.150 -13.377 1.00 13.60 ?  33  THR   B H    1 
ATOM   4252 H HA   . THR   B 1 33  ? 46.130 -12.092 -12.137 1.00 14.08 ?  33  THR   B HA   1 
ATOM   4253 H HB   . THR   B 1 33  ? 43.381 -12.738 -12.283 1.00 14.72 ?  33  THR   B HB   1 
ATOM   4254 H HG1  . THR   B 1 33  ? 43.434 -11.494 -14.118 1.00 14.98 ?  33  THR   B HG1  1 
ATOM   4255 H HG21 . THR   B 1 33  ? 43.076 -10.367 -12.100 1.00 16.17 ?  33  THR   B HG21 1 
ATOM   4256 H HG22 . THR   B 1 33  ? 43.633 -11.020 -10.776 1.00 16.17 ?  33  THR   B HG22 1 
ATOM   4257 H HG23 . THR   B 1 33  ? 44.610 -10.247 -11.748 1.00 16.17 ?  33  THR   B HG23 1 
ATOM   4258 N N    . VAL   B 1 34  ? 44.838 -14.270 -10.190 1.00 10.69 ?  34  VAL   B N    1 
ATOM   4259 C CA   . VAL   B 1 34  ? 44.652 -14.673 -8.801  1.00 10.05 ?  34  VAL   B CA   1 
ATOM   4260 C C    . VAL   B 1 34  ? 45.088 -16.120 -8.638  1.00 9.21  ?  34  VAL   B C    1 
ATOM   4261 O O    . VAL   B 1 34  ? 44.574 -17.008 -9.328  1.00 9.99  ?  34  VAL   B O    1 
ATOM   4262 C CB   . VAL   B 1 34  ? 43.183 -14.536 -8.349  1.00 11.32 ?  34  VAL   B CB   1 
ATOM   4263 C CG1  . VAL   B 1 34  ? 43.025 -14.989 -6.903  1.00 11.80 ?  34  VAL   B CG1  1 
ATOM   4264 C CG2  . VAL   B 1 34  ? 42.679 -13.111 -8.531  1.00 12.27 ?  34  VAL   B CG2  1 
ATOM   4265 H H    . VAL   B 1 34  ? 44.578 -14.862 -10.759 1.00 12.84 ?  34  VAL   B H    1 
ATOM   4266 H HA   . VAL   B 1 34  ? 45.205 -14.117 -8.225  1.00 12.06 ?  34  VAL   B HA   1 
ATOM   4267 H HB   . VAL   B 1 34  ? 42.635 -15.113 -8.902  1.00 13.59 ?  34  VAL   B HB   1 
ATOM   4268 H HG11 . VAL   B 1 34  ? 42.166 -14.683 -6.568  1.00 14.16 ?  34  VAL   B HG11 1 
ATOM   4269 H HG12 . VAL   B 1 34  ? 43.061 -15.960 -6.866  1.00 14.16 ?  34  VAL   B HG12 1 
ATOM   4270 H HG13 . VAL   B 1 34  ? 43.739 -14.610 -6.369  1.00 14.16 ?  34  VAL   B HG13 1 
ATOM   4271 H HG21 . VAL   B 1 34  ? 41.764 -13.056 -8.214  1.00 14.73 ?  34  VAL   B HG21 1 
ATOM   4272 H HG22 . VAL   B 1 34  ? 43.243 -12.508 -8.021  1.00 14.73 ?  34  VAL   B HG22 1 
ATOM   4273 H HG23 . VAL   B 1 34  ? 42.717 -12.880 -9.474  1.00 14.73 ?  34  VAL   B HG23 1 
ATOM   4274 N N    . VAL   B 1 35  ? 45.999 -16.363 -7.698  1.00 9.15  ?  35  VAL   B N    1 
ATOM   4275 C CA   . VAL   B 1 35  ? 46.245 -17.704 -7.179  1.00 8.80  ?  35  VAL   B CA   1 
ATOM   4276 C C    . VAL   B 1 35  ? 45.705 -17.764 -5.757  1.00 8.91  ?  35  VAL   B C    1 
ATOM   4277 O O    . VAL   B 1 35  ? 45.923 -16.841 -4.962  1.00 9.04  ?  35  VAL   B O    1 
ATOM   4278 C CB   . VAL   B 1 35  ? 47.731 -18.119 -7.258  1.00 9.32  ?  35  VAL   B CB   1 
ATOM   4279 C CG1  . VAL   B 1 35  ? 48.620 -17.279 -6.334  1.00 10.07 ?  35  VAL   B CG1  1 
ATOM   4280 C CG2  . VAL   B 1 35  ? 47.885 -19.617 -6.957  1.00 9.94  ?  35  VAL   B CG2  1 
ATOM   4281 H H    . VAL   B 1 35  ? 46.498 -15.758 -7.341  1.00 10.98 ?  35  VAL   B H    1 
ATOM   4282 H HA   . VAL   B 1 35  ? 45.736 -18.338 -7.711  1.00 10.57 ?  35  VAL   B HA   1 
ATOM   4283 H HB   . VAL   B 1 35  ? 48.040 -17.979 -8.167  1.00 11.19 ?  35  VAL   B HB   1 
ATOM   4284 H HG11 . VAL   B 1 35  ? 49.545 -17.493 -6.510  1.00 12.09 ?  35  VAL   B HG11 1 
ATOM   4285 H HG12 . VAL   B 1 35  ? 48.450 -16.343 -6.506  1.00 12.09 ?  35  VAL   B HG12 1 
ATOM   4286 H HG13 . VAL   B 1 35  ? 48.399 -17.492 -5.411  1.00 12.09 ?  35  VAL   B HG13 1 
ATOM   4287 H HG21 . VAL   B 1 35  ? 48.814 -19.871 -7.052  1.00 11.94 ?  35  VAL   B HG21 1 
ATOM   4288 H HG22 . VAL   B 1 35  ? 47.585 -19.793 -6.048  1.00 11.94 ?  35  VAL   B HG22 1 
ATOM   4289 H HG23 . VAL   B 1 35  ? 47.338 -20.128 -7.582  1.00 11.94 ?  35  VAL   B HG23 1 
ATOM   4290 N N    . VAL   B 1 36  ? 44.994 -18.848 -5.442  1.00 8.60  ?  36  VAL   B N    1 
ATOM   4291 C CA   . VAL   B 1 36  ? 44.446 -19.062 -4.110  1.00 8.53  ?  36  VAL   B CA   1 
ATOM   4292 C C    . VAL   B 1 36  ? 45.455 -19.824 -3.263  1.00 8.19  ?  36  VAL   B C    1 
ATOM   4293 O O    . VAL   B 1 36  ? 45.994 -20.854 -3.690  1.00 9.24  ?  36  VAL   B O    1 
ATOM   4294 C CB   . VAL   B 1 36  ? 43.112 -19.825 -4.191  1.00 8.76  ?  36  VAL   B CB   1 
ATOM   4295 C CG1  . VAL   B 1 36  ? 42.610 -20.193 -2.799  1.00 9.61  ?  36  VAL   B CG1  1 
ATOM   4296 C CG2  . VAL   B 1 36  ? 42.080 -18.991 -4.943  1.00 9.36  ?  36  VAL   B CG2  1 
ATOM   4297 H H    . VAL   B 1 36  ? 44.821 -19.488 -5.995  1.00 10.33 ?  36  VAL   B H    1 
ATOM   4298 H HA   . VAL   B 1 36  ? 44.281 -18.203 -3.693  1.00 10.25 ?  36  VAL   B HA   1 
ATOM   4299 H HB   . VAL   B 1 36  ? 43.250 -20.645 -4.688  1.00 10.52 ?  36  VAL   B HB   1 
ATOM   4300 H HG11 . VAL   B 1 36  ? 41.673 -20.428 -2.859  1.00 11.55 ?  36  VAL   B HG11 1 
ATOM   4301 H HG12 . VAL   B 1 36  ? 43.122 -20.942 -2.466  1.00 11.55 ?  36  VAL   B HG12 1 
ATOM   4302 H HG13 . VAL   B 1 36  ? 42.720 -19.424 -2.215  1.00 11.55 ?  36  VAL   B HG13 1 
ATOM   4303 H HG21 . VAL   B 1 36  ? 41.240 -19.468 -4.964  1.00 11.24 ?  36  VAL   B HG21 1 
ATOM   4304 H HG22 . VAL   B 1 36  ? 41.971 -18.139 -4.492  1.00 11.24 ?  36  VAL   B HG22 1 
ATOM   4305 H HG23 . VAL   B 1 36  ? 42.397 -18.839 -5.852  1.00 11.24 ?  36  VAL   B HG23 1 
ATOM   4306 N N    . ASN   B 1 37  ? 45.683 -19.333 -2.044  1.00 8.44  ?  37  ASN   B N    1 
ATOM   4307 C CA   . ASN   B 1 37  ? 46.440 -20.057 -1.037  1.00 8.87  ?  37  ASN   B CA   1 
ATOM   4308 C C    . ASN   B 1 37  ? 45.492 -20.730 -0.051  1.00 8.80  ?  37  ASN   B C    1 
ATOM   4309 O O    . ASN   B 1 37  ? 44.484 -20.149 0.365   1.00 9.38  ?  37  ASN   B O    1 
ATOM   4310 C CB   . ASN   B 1 37  ? 47.367 -19.110 -0.276  1.00 8.91  ?  37  ASN   B CB   1 
ATOM   4311 C CG   . ASN   B 1 37  ? 48.215 -19.827 0.741   1.00 9.15  ?  37  ASN   B CG   1 
ATOM   4312 O OD1  . ASN   B 1 37  ? 48.570 -20.996 0.559   1.00 9.76  ?  37  ASN   B OD1  1 
ATOM   4313 N ND2  . ASN   B 1 37  ? 48.562 -19.133 1.813   1.00 9.42  ?  37  ASN   B ND2  1 
ATOM   4314 H H    . ASN   B 1 37  ? 45.394 -18.568 -1.770  1.00 10.13 ?  37  ASN   B H    1 
ATOM   4315 H HA   . ASN   B 1 37  ? 46.975 -20.748 -1.463  1.00 10.65 ?  37  ASN   B HA   1 
ATOM   4316 H HB2  . ASN   B 1 37  ? 47.960 -18.682 -0.910  1.00 10.70 ?  37  ASN   B HB2  1 
ATOM   4317 H HB3  . ASN   B 1 37  ? 46.834 -18.453 0.189   1.00 10.70 ?  37  ASN   B HB3  1 
ATOM   4318 H HD21 . ASN   B 1 37  ? 49.045 -19.503 2.423   1.00 11.32 ?  37  ASN   B HD21 1 
ATOM   4319 H HD22 . ASN   B 1 37  ? 48.296 -18.330 1.908   1.00 11.32 ?  37  ASN   B HD22 1 
ATOM   4320 N N    . ALA   B 1 38  ? 45.843 -21.961 0.331   1.00 8.96  ?  38  ALA   B N    1 
ATOM   4321 C CA   . ALA   B 1 38  ? 45.180 -22.709 1.399   1.00 9.22  ?  38  ALA   B CA   1 
ATOM   4322 C C    . ALA   B 1 38  ? 45.767 -22.231 2.727   1.00 9.15  ?  38  ALA   B C    1 
ATOM   4323 O O    . ALA   B 1 38  ? 46.673 -22.839 3.306   1.00 9.96  ?  38  ALA   B O    1 
ATOM   4324 C CB   . ALA   B 1 38  ? 45.389 -24.203 1.197   1.00 10.51 ?  38  ALA   B CB   1 
ATOM   4325 H H    . ALA   B 1 38  ? 46.501 -22.396 -0.017  1.00 10.77 ?  38  ALA   B H    1 
ATOM   4326 H HA   . ALA   B 1 38  ? 44.227 -22.519 1.391   1.00 11.07 ?  38  ALA   B HA   1 
ATOM   4327 H HB1  . ALA   B 1 38  ? 44.935 -24.685 1.915   1.00 12.62 ?  38  ALA   B HB1  1 
ATOM   4328 H HB2  . ALA   B 1 38  ? 45.008 -24.463 0.343   1.00 12.62 ?  38  ALA   B HB2  1 
ATOM   4329 H HB3  . ALA   B 1 38  ? 46.333 -24.399 1.217   1.00 12.62 ?  38  ALA   B HB3  1 
ATOM   4330 N N    . ALA   B 1 39  ? 45.251 -21.093 3.196   1.00 9.11  ?  39  ALA   B N    1 
ATOM   4331 C CA   . ALA   B 1 39  ? 45.801 -20.367 4.331   1.00 9.39  ?  39  ALA   B CA   1 
ATOM   4332 C C    . ALA   B 1 39  ? 45.182 -20.822 5.652   1.00 9.34  ?  39  ALA   B C    1 
ATOM   4333 O O    . ALA   B 1 39  ? 44.156 -21.503 5.700   1.00 10.19 ?  39  ALA   B O    1 
ATOM   4334 C CB   . ALA   B 1 39  ? 45.562 -18.867 4.142   1.00 10.11 ?  39  ALA   B CB   1 
ATOM   4335 H H    . ALA   B 1 39  ? 44.558 -20.714 2.854   1.00 10.94 ?  39  ALA   B H    1 
ATOM   4336 H HA   . ALA   B 1 39  ? 46.751 -20.523 4.376   1.00 11.28 ?  39  ALA   B HA   1 
ATOM   4337 H HB1  . ALA   B 1 39  ? 45.932 -18.392 4.904   1.00 12.14 ?  39  ALA   B HB1  1 
ATOM   4338 H HB2  . ALA   B 1 39  ? 46.006 -18.578 3.328   1.00 12.14 ?  39  ALA   B HB2  1 
ATOM   4339 H HB3  . ALA   B 1 39  ? 44.611 -18.699 4.078   1.00 12.14 ?  39  ALA   B HB3  1 
ATOM   4340 N N    . ASN   B 1 40  ? 45.819 -20.396 6.739   1.00 10.26 ?  40  ASN   B N    1 
ATOM   4341 C CA   . ASN   B 1 40  ? 45.257 -20.452 8.079   1.00 10.81 ?  40  ASN   B CA   1 
ATOM   4342 C C    . ASN   B 1 40  ? 45.082 -19.026 8.608   1.00 10.40 ?  40  ASN   B C    1 
ATOM   4343 O O    . ASN   B 1 40  ? 45.499 -18.046 7.981   1.00 10.63 ?  40  ASN   B O    1 
ATOM   4344 C CB   . ASN   B 1 40  ? 46.104 -21.334 9.016   1.00 11.81 ?  40  ASN   B CB   1 
ATOM   4345 C CG   . ASN   B 1 40  ? 47.561 -20.934 9.045   1.00 12.76 ?  40  ASN   B CG   1 
ATOM   4346 O OD1  . ASN   B 1 40  ? 47.884 -19.755 9.118   1.00 14.62 ?  40  ASN   B OD1  1 
ATOM   4347 N ND2  . ASN   B 1 40  ? 48.451 -21.914 9.003   1.00 12.79 ?  40  ASN   B ND2  1 
ATOM   4348 H H    . ASN   B 1 40  ? 46.610 -20.064 6.718   1.00 12.32 ?  40  ASN   B H    1 
ATOM   4349 H HA   . ASN   B 1 40  ? 44.376 -20.850 8.033   1.00 12.98 ?  40  ASN   B HA   1 
ATOM   4350 H HB2  . ASN   B 1 40  ? 45.759 -21.260 9.921   1.00 14.18 ?  40  ASN   B HB2  1 
ATOM   4351 H HB3  . ASN   B 1 40  ? 46.052 -22.255 8.717   1.00 14.18 ?  40  ASN   B HB3  1 
ATOM   4352 H HD21 . ASN   B 1 40  ? 49.294 -21.738 9.016   1.00 15.36 ?  40  ASN   B HD21 1 
ATOM   4353 H HD22 . ASN   B 1 40  ? 48.188 -22.734 8.954   1.00 15.36 ?  40  ASN   B HD22 1 
ATOM   4354 N N    . VAL   B 1 41  ? 44.424 -18.901 9.763   1.00 10.91 ?  41  VAL   B N    1 
ATOM   4355 C CA   . VAL   B 1 41  ? 43.969 -17.581 10.210  1.00 11.45 ?  41  VAL   B CA   1 
ATOM   4356 C C    . VAL   B 1 41  ? 45.121 -16.636 10.525  1.00 11.50 ?  41  VAL   B C    1 
ATOM   4357 O O    . VAL   B 1 41  ? 44.944 -15.415 10.462  1.00 11.86 ?  41  VAL   B O    1 
ATOM   4358 C CB   . VAL   B 1 41  ? 42.979 -17.658 11.390  1.00 12.90 ?  41  VAL   B CB   1 
ATOM   4359 C CG1  . VAL   B 1 41  ? 41.679 -18.328 10.965  1.00 13.43 ?  41  VAL   B CG1  1 
ATOM   4360 C CG2  . VAL   B 1 41  ? 43.603 -18.359 12.587  1.00 13.95 ?  41  VAL   B CG2  1 
ATOM   4361 H H    . VAL   B 1 41  ? 44.238 -19.544 10.295  1.00 13.10 ?  41  VAL   B H    1 
ATOM   4362 H HA   . VAL   B 1 41  ? 43.483 -17.178 9.476   1.00 13.75 ?  41  VAL   B HA   1 
ATOM   4363 H HB   . VAL   B 1 41  ? 42.760 -16.755 11.667  1.00 15.49 ?  41  VAL   B HB   1 
ATOM   4364 H HG11 . VAL   B 1 41  ? 41.062 -18.326 11.715  1.00 16.12 ?  41  VAL   B HG11 1 
ATOM   4365 H HG12 . VAL   B 1 41  ? 41.297 -17.834 10.222  1.00 16.12 ?  41  VAL   B HG12 1 
ATOM   4366 H HG13 . VAL   B 1 41  ? 41.867 -19.240 10.694  1.00 16.12 ?  41  VAL   B HG13 1 
ATOM   4367 H HG21 . VAL   B 1 41  ? 42.958 -18.382 13.310  1.00 16.74 ?  41  VAL   B HG21 1 
ATOM   4368 H HG22 . VAL   B 1 41  ? 43.844 -19.266 12.333  1.00 16.74 ?  41  VAL   B HG22 1 
ATOM   4369 H HG23 . VAL   B 1 41  ? 44.394 -17.872 12.863  1.00 16.74 ?  41  VAL   B HG23 1 
ATOM   4370 N N    . TYR   B 1 42  ? 46.291 -17.154 10.901  1.00 11.57 ?  42  TYR   B N    1 
ATOM   4371 C CA   . TYR   B 1 42  ? 47.445 -16.306 11.172  1.00 12.64 ?  42  TYR   B CA   1 
ATOM   4372 C C    . TYR   B 1 42  ? 48.410 -16.230 9.994   1.00 11.53 ?  42  TYR   B C    1 
ATOM   4373 O O    . TYR   B 1 42  ? 49.498 -15.657 10.131  1.00 12.41 ?  42  TYR   B O    1 
ATOM   4374 C CB   . TYR   B 1 42  ? 48.148 -16.708 12.476  1.00 14.84 ?  42  TYR   B CB   1 
ATOM   4375 C CG   . TYR   B 1 42  ? 47.534 -16.039 13.704  1.00 15.08 ?  42  TYR   B CG   1 
ATOM   4376 C CD1  . TYR   B 1 42  ? 47.760 -14.691 13.970  1.00 14.45 ?  42  TYR   B CD1  1 
ATOM   4377 C CD2  . TYR   B 1 42  ? 46.726 -16.746 14.579  1.00 17.13 ?  42  TYR   B CD2  1 
ATOM   4378 C CE1  . TYR   B 1 42  ? 47.200 -14.069 15.073  1.00 15.56 ?  42  TYR   B CE1  1 
ATOM   4379 C CE2  . TYR   B 1 42  ? 46.164 -16.133 15.687  1.00 17.53 ?  42  TYR   B CE2  1 
ATOM   4380 C CZ   . TYR   B 1 42  ? 46.400 -14.793 15.929  1.00 17.30 ?  42  TYR   B CZ   1 
ATOM   4381 O OH   . TYR   B 1 42  ? 45.847 -14.184 17.033  1.00 20.02 ?  42  TYR   B OH   1 
ATOM   4382 H H    . TYR   B 1 42  ? 46.438 -17.999 10.995  1.00 13.89 ?  42  TYR   B H    1 
ATOM   4383 H HA   . TYR   B 1 42  ? 47.116 -15.406 11.307  1.00 15.17 ?  42  TYR   B HA   1 
ATOM   4384 H HB2  . TYR   B 1 42  ? 48.076 -17.666 12.590  1.00 17.82 ?  42  TYR   B HB2  1 
ATOM   4385 H HB3  . TYR   B 1 42  ? 49.079 -16.445 12.423  1.00 17.82 ?  42  TYR   B HB3  1 
ATOM   4386 H HD1  . TYR   B 1 42  ? 48.301 -14.197 13.386  1.00 17.35 ?  42  TYR   B HD1  1 
ATOM   4387 H HD2  . TYR   B 1 42  ? 46.558 -17.648 14.414  1.00 20.57 ?  42  TYR   B HD2  1 
ATOM   4388 H HE1  . TYR   B 1 42  ? 47.370 -13.170 15.236  1.00 18.69 ?  42  TYR   B HE1  1 
ATOM   4389 H HE2  . TYR   B 1 42  ? 45.627 -16.625 16.263  1.00 21.04 ?  42  TYR   B HE2  1 
ATOM   4390 H HH   . TYR   B 1 42  ? 46.083 -13.382 17.058  1.00 24.04 ?  42  TYR   B HH   1 
ATOM   4391 N N    . LEU   B 1 43  ? 48.014 -16.743 8.830   1.00 10.78 ?  43  LEU   B N    1 
ATOM   4392 C CA   . LEU   B 1 43  ? 48.827 -16.664 7.620   1.00 10.63 ?  43  LEU   B CA   1 
ATOM   4393 C C    . LEU   B 1 43  ? 50.242 -17.173 7.875   1.00 11.09 ?  43  LEU   B C    1 
ATOM   4394 O O    . LEU   B 1 43  ? 51.223 -16.570 7.438   1.00 11.65 ?  43  LEU   B O    1 
ATOM   4395 C CB   . LEU   B 1 43  ? 48.842 -15.252 7.031   1.00 10.57 ?  43  LEU   B CB   1 
ATOM   4396 C CG   . LEU   B 1 43  ? 47.481 -14.647 6.657   1.00 10.72 ?  43  LEU   B CG   1 
ATOM   4397 C CD1  . LEU   B 1 43  ? 47.688 -13.246 6.085   1.00 12.12 ?  43  LEU   B CD1  1 
ATOM   4398 C CD2  . LEU   B 1 43  ? 46.726 -15.533 5.674   1.00 11.00 ?  43  LEU   B CD2  1 
ATOM   4399 H H    . LEU   B 1 43  ? 47.270 -17.163 8.714   1.00 12.94 ?  43  LEU   B H    1 
ATOM   4400 H HA   . LEU   B 1 43  ? 48.429 -17.246 6.951   1.00 12.76 ?  43  LEU   B HA   1 
ATOM   4401 H HB2  . LEU   B 1 43  ? 49.252 -14.658 7.678   1.00 12.70 ?  43  LEU   B HB2  1 
ATOM   4402 H HB3  . LEU   B 1 43  ? 49.378 -15.268 6.224   1.00 12.70 ?  43  LEU   B HB3  1 
ATOM   4403 H HG   . LEU   B 1 43  ? 46.943 -14.563 7.459   1.00 12.88 ?  43  LEU   B HG   1 
ATOM   4404 H HD11 . LEU   B 1 43  ? 46.825 -12.868 5.852   1.00 14.56 ?  43  LEU   B HD11 1 
ATOM   4405 H HD12 . LEU   B 1 43  ? 48.119 -12.690 6.757   1.00 14.56 ?  43  LEU   B HD12 1 
ATOM   4406 H HD13 . LEU   B 1 43  ? 48.248 -13.303 5.296   1.00 14.56 ?  43  LEU   B HD13 1 
ATOM   4407 H HD21 . LEU   B 1 43  ? 45.926 -15.066 5.381   1.00 13.21 ?  43  LEU   B HD21 1 
ATOM   4408 H HD22 . LEU   B 1 43  ? 47.297 -15.718 4.913   1.00 13.21 ?  43  LEU   B HD22 1 
ATOM   4409 H HD23 . LEU   B 1 43  ? 46.482 -16.359 6.117   1.00 13.21 ?  43  LEU   B HD23 1 
ATOM   4410 N N    . LYS   B 1 44  ? 50.345 -18.298 8.587   1.00 10.80 ?  44  LYS   B N    1 
ATOM   4411 C CA   . LYS   B 1 44  ? 51.613 -18.978 8.816   1.00 11.43 ?  44  LYS   B CA   1 
ATOM   4412 C C    . LYS   B 1 44  ? 51.726 -20.089 7.780   1.00 10.98 ?  44  LYS   B C    1 
ATOM   4413 O O    . LYS   B 1 44  ? 51.022 -21.103 7.859   1.00 11.97 ?  44  LYS   B O    1 
ATOM   4414 C CB   . LYS   B 1 44  ? 51.686 -19.496 10.250  1.00 12.85 ?  44  LYS   B CB   1 
ATOM   4415 C CG   . LYS   B 1 44  ? 51.854 -18.386 11.280  1.00 15.62 ?  44  LYS   B CG   1 
ATOM   4416 C CD   . LYS   B 1 44  ? 53.075 -17.527 10.944  1.00 18.17 ?  44  LYS   B CD   1 
ATOM   4417 C CE   . LYS   B 1 44  ? 53.437 -16.559 12.042  1.00 20.62 ?  44  LYS   B CE   1 
ATOM   4418 N NZ   . LYS   B 1 44  ? 54.669 -15.796 11.708  1.00 22.22 ?  44  LYS   B NZ   1 
ATOM   4419 H H    . LYS   B 1 44  ? 49.674 -18.687 8.958   1.00 12.97 ?  44  LYS   B H    1 
ATOM   4420 H HA   . LYS   B 1 44  ? 52.341 -18.359 8.653   1.00 13.72 ?  44  LYS   B HA   1 
ATOM   4421 H HB2  . LYS   B 1 44  ? 50.862 -19.969 10.452  1.00 15.43 ?  44  LYS   B HB2  1 
ATOM   4422 H HB3  . LYS   B 1 44  ? 52.440 -20.096 10.327  1.00 15.43 ?  44  LYS   B HB3  1 
ATOM   4423 H HG2  . LYS   B 1 44  ? 51.068 -17.822 11.281  1.00 18.75 ?  44  LYS   B HG2  1 
ATOM   4424 H HG3  . LYS   B 1 44  ? 51.990 -18.784 12.157  1.00 18.75 ?  44  LYS   B HG3  1 
ATOM   4425 H HD2  . LYS   B 1 44  ? 53.835 -18.114 10.778  1.00 21.81 ?  44  LYS   B HD2  1 
ATOM   4426 H HD3  . LYS   B 1 44  ? 52.882 -17.007 10.148  1.00 21.81 ?  44  LYS   B HD3  1 
ATOM   4427 H HE2  . LYS   B 1 44  ? 52.711 -15.928 12.154  1.00 24.76 ?  44  LYS   B HE2  1 
ATOM   4428 H HE3  . LYS   B 1 44  ? 53.592 -17.050 12.861  1.00 24.76 ?  44  LYS   B HE3  1 
ATOM   4429 H HZ1  . LYS   B 1 44  ? 54.862 -15.230 12.366  1.00 26.67 ?  44  LYS   B HZ1  1 
ATOM   4430 H HZ2  . LYS   B 1 44  ? 55.353 -16.353 11.594  1.00 26.67 ?  44  LYS   B HZ2  1 
ATOM   4431 H HZ3  . LYS   B 1 44  ? 54.547 -15.333 10.955  1.00 26.67 ?  44  LYS   B HZ3  1 
ATOM   4432 N N    . HIS   B 1 45  ? 52.583 -19.870 6.786   1.00 10.50 ?  45  HIS   B N    1 
ATOM   4433 C CA   . HIS   B 1 45  ? 52.604 -20.697 5.582   1.00 11.05 ?  45  HIS   B CA   1 
ATOM   4434 C C    . HIS   B 1 45  ? 53.620 -21.822 5.742   1.00 13.34 ?  45  HIS   B C    1 
ATOM   4435 O O    . HIS   B 1 45  ? 54.682 -21.838 5.127   1.00 15.30 ?  45  HIS   B O    1 
ATOM   4436 C CB   . HIS   B 1 45  ? 52.916 -19.841 4.367   1.00 10.82 ?  45  HIS   B CB   1 
ATOM   4437 C CG   . HIS   B 1 45  ? 52.044 -18.637 4.260   1.00 10.62 ?  45  HIS   B CG   1 
ATOM   4438 N ND1  . HIS   B 1 45  ? 50.666 -18.714 4.234   1.00 11.03 ?  45  HIS   B ND1  1 
ATOM   4439 C CD2  . HIS   B 1 45  ? 52.362 -17.324 4.190   1.00 11.48 ?  45  HIS   B CD2  1 
ATOM   4440 C CE1  . HIS   B 1 45  ? 50.179 -17.490 4.138   1.00 10.67 ?  45  HIS   B CE1  1 
ATOM   4441 N NE2  . HIS   B 1 45  ? 51.184 -16.629 4.108   1.00 11.10 ?  45  HIS   B NE2  1 
ATOM   4442 H H    . HIS   B 1 45  ? 53.163 -19.235 6.778   1.00 12.61 ?  45  HIS   B H    1 
ATOM   4443 H HA   . HIS   B 1 45  ? 51.729 -21.096 5.451   1.00 13.26 ?  45  HIS   B HA   1 
ATOM   4444 H HB2  . HIS   B 1 45  ? 53.837 -19.546 4.416   1.00 12.99 ?  45  HIS   B HB2  1 
ATOM   4445 H HB3  . HIS   B 1 45  ? 52.788 -20.380 3.563   1.00 12.99 ?  45  HIS   B HB3  1 
ATOM   4446 H HD2  . HIS   B 1 45  ? 53.218 -16.963 4.191   1.00 13.79 ?  45  HIS   B HD2  1 
ATOM   4447 H HE1  . HIS   B 1 45  ? 49.276 -17.272 4.090   1.00 12.81 ?  45  HIS   B HE1  1 
ATOM   4448 H HE2  . HIS   B 1 45  ? 51.108 -15.777 4.053   1.00 13.33 ?  45  HIS   B HE2  1 
ATOM   4449 N N    A GLY   B 1 46  ? 53.255 -22.794 6.573   0.86 13.90 ?  46  GLY   B N    1 
ATOM   4450 N N    B GLY   B 1 46  ? 53.262 -22.781 6.591   0.14 14.08 ?  46  GLY   B N    1 
ATOM   4451 C CA   A GLY   B 1 46  ? 54.180 -23.853 6.932   0.86 15.50 ?  46  GLY   B CA   1 
ATOM   4452 C CA   B GLY   B 1 46  ? 54.173 -23.853 6.939   0.14 14.93 ?  46  GLY   B CA   1 
ATOM   4453 C C    A GLY   B 1 46  ? 54.229 -25.044 5.997   0.86 16.96 ?  46  GLY   B C    1 
ATOM   4454 C C    B GLY   B 1 46  ? 54.214 -24.996 5.944   0.14 15.74 ?  46  GLY   B C    1 
ATOM   4455 O O    A GLY   B 1 46  ? 55.300 -25.425 5.514   0.86 20.26 ?  46  GLY   B O    1 
ATOM   4456 O O    B GLY   B 1 46  ? 55.262 -25.274 5.353   0.14 16.23 ?  46  GLY   B O    1 
ATOM   4457 H H    A GLY   B 1 46  ? 52.481 -22.848 6.955   0.86 16.68 ?  46  GLY   B H    1 
ATOM   4458 H H    B GLY   B 1 46  ? 52.495 -22.826 6.984   0.14 16.90 ?  46  GLY   B H    1 
ATOM   4459 H HA2  A GLY   B 1 46  ? 55.072 -23.480 6.987   0.86 18.61 ?  46  GLY   B HA2  1 
ATOM   4460 H HA2  B GLY   B 1 46  ? 55.068 -23.489 7.016   0.14 17.93 ?  46  GLY   B HA2  1 
ATOM   4461 H HA3  A GLY   B 1 46  ? 53.942 -24.190 7.810   0.86 18.61 ?  46  GLY   B HA3  1 
ATOM   4462 H HA3  B GLY   B 1 46  ? 53.920 -24.211 7.805   0.14 17.93 ?  46  GLY   B HA3  1 
ATOM   4463 N N    . GLY   B 1 47  ? 53.078 -25.662 5.740   1.00 16.17 ?  47  GLY   B N    1 
ATOM   4464 C CA   . GLY   B 1 47  ? 53.031 -26.921 5.025   1.00 13.87 ?  47  GLY   B CA   1 
ATOM   4465 C C    . GLY   B 1 47  ? 52.105 -26.897 3.825   1.00 12.05 ?  47  GLY   B C    1 
ATOM   4466 O O    . GLY   B 1 47  ? 51.454 -25.892 3.532   1.00 12.14 ?  47  GLY   B O    1 
ATOM   4467 H H    A GLY   B 1 47  ? 52.309 -25.380 6.000   0.86 19.42 ?  47  GLY   B H    1 
ATOM   4468 H H    B GLY   B 1 47  ? 52.310 -25.396 6.020   0.14 19.42 ?  47  GLY   B H    1 
ATOM   4469 H HA2  . GLY   B 1 47  ? 53.922 -27.156 4.716   1.00 16.65 ?  47  GLY   B HA2  1 
ATOM   4470 H HA3  . GLY   B 1 47  ? 52.734 -27.620 5.632   1.00 16.65 ?  47  GLY   B HA3  1 
ATOM   4471 N N    . GLY   B 1 48  ? 52.066 -28.032 3.130   1.00 11.33 ?  48  GLY   B N    1 
ATOM   4472 C CA   . GLY   B 1 48  ? 51.140 -28.180 2.023   1.00 11.26 ?  48  GLY   B CA   1 
ATOM   4473 C C    . GLY   B 1 48  ? 51.273 -27.067 1.009   1.00 10.61 ?  48  GLY   B C    1 
ATOM   4474 O O    . GLY   B 1 48  ? 52.376 -26.605 0.690   1.00 11.09 ?  48  GLY   B O    1 
ATOM   4475 H H    . GLY   B 1 48  ? 52.574 -28.709 3.268   1.00 13.60 ?  48  GLY   B H    1 
ATOM   4476 H HA2  . GLY   B 1 48  ? 51.302 -29.028 1.579   1.00 13.52 ?  48  GLY   B HA2  1 
ATOM   4477 H HA3  . GLY   B 1 48  ? 50.232 -28.179 2.362   1.00 13.52 ?  48  GLY   B HA3  1 
ATOM   4478 N N    . VAL   B 1 49  ? 50.123 -26.635 0.487   1.00 10.71 ?  49  VAL   B N    1 
ATOM   4479 C CA   . VAL   B 1 49  ? 50.098 -25.607 -0.550  1.00 10.80 ?  49  VAL   B CA   1 
ATOM   4480 C C    . VAL   B 1 49  ? 50.755 -24.321 -0.060  1.00 10.06 ?  49  VAL   B C    1 
ATOM   4481 O O    . VAL   B 1 49  ? 51.540 -23.699 -0.784  1.00 10.63 ?  49  VAL   B O    1 
ATOM   4482 C CB   . VAL   B 1 49  ? 48.654 -25.364 -1.032  1.00 12.05 ?  49  VAL   B CB   1 
ATOM   4483 C CG1  . VAL   B 1 49  ? 48.580 -24.114 -1.905  1.00 11.88 ?  49  VAL   B CG1  1 
ATOM   4484 C CG2  . VAL   B 1 49  ? 48.120 -26.580 -1.781  1.00 13.46 ?  49  VAL   B CG2  1 
ATOM   4485 H H    . VAL   B 1 49  ? 49.342 -26.922 0.711   1.00 12.87 ?  49  VAL   B H    1 
ATOM   4486 H HA   . VAL   B 1 49  ? 50.605 -25.919 -1.314  1.00 12.97 ?  49  VAL   B HA   1 
ATOM   4487 H HB   . VAL   B 1 49  ? 48.084 -25.218 -0.263  1.00 14.47 ?  49  VAL   B HB   1 
ATOM   4488 H HG11 . VAL   B 1 49  ? 47.751 -24.130 -2.412  1.00 14.26 ?  49  VAL   B HG11 1 
ATOM   4489 H HG12 . VAL   B 1 49  ? 48.600 -23.326 -1.338  1.00 14.26 ?  49  VAL   B HG12 1 
ATOM   4490 H HG13 . VAL   B 1 49  ? 49.335 -24.105 -2.513  1.00 14.26 ?  49  VAL   B HG13 1 
ATOM   4491 H HG21 . VAL   B 1 49  ? 47.214 -26.400 -2.072  1.00 16.16 ?  49  VAL   B HG21 1 
ATOM   4492 H HG22 . VAL   B 1 49  ? 48.688 -26.749 -2.551  1.00 16.16 ?  49  VAL   B HG22 1 
ATOM   4493 H HG23 . VAL   B 1 49  ? 48.134 -27.344 -1.186  1.00 16.16 ?  49  VAL   B HG23 1 
ATOM   4494 N N    . ALA   B 1 50  ? 50.413 -23.876 1.155   1.00 9.76  ?  50  ALA   B N    1 
ATOM   4495 C CA   . ALA   B 1 50  ? 50.935 -22.596 1.632   1.00 9.77  ?  50  ALA   B CA   1 
ATOM   4496 C C    . ALA   B 1 50  ? 52.456 -22.623 1.736   1.00 9.88  ?  50  ALA   B C    1 
ATOM   4497 O O    . ALA   B 1 50  ? 53.135 -21.653 1.366   1.00 10.12 ?  50  ALA   B O    1 
ATOM   4498 C CB   . ALA   B 1 50  ? 50.305 -22.234 2.976   1.00 10.06 ?  50  ALA   B CB   1 
ATOM   4499 H H    . ALA   B 1 50  ? 49.900 -24.288 1.709   1.00 11.73 ?  50  ALA   B H    1 
ATOM   4500 H HA   . ALA   B 1 50  ? 50.702 -21.906 1.000   1.00 11.74 ?  50  ALA   B HA   1 
ATOM   4501 H HB1  . ALA   B 1 50  ? 50.662 -21.380 3.276   1.00 12.08 ?  50  ALA   B HB1  1 
ATOM   4502 H HB2  . ALA   B 1 50  ? 49.342 -22.164 2.865   1.00 12.08 ?  50  ALA   B HB2  1 
ATOM   4503 H HB3  . ALA   B 1 50  ? 50.512 -22.923 3.626   1.00 12.08 ?  50  ALA   B HB3  1 
ATOM   4504 N N    . GLY   B 1 51  ? 53.011 -23.719 2.247   1.00 10.45 ?  51  GLY   B N    1 
ATOM   4505 C CA   . GLY   B 1 51  ? 54.456 -23.822 2.318   1.00 11.19 ?  51  GLY   B CA   1 
ATOM   4506 C C    . GLY   B 1 51  ? 55.106 -23.769 0.951   1.00 11.02 ?  51  GLY   B C    1 
ATOM   4507 O O    . GLY   B 1 51  ? 56.144 -23.128 0.769   1.00 11.88 ?  51  GLY   B O    1 
ATOM   4508 H H    . GLY   B 1 51  ? 52.585 -24.404 2.547   1.00 12.55 ?  51  GLY   B H    1 
ATOM   4509 H HA2  . GLY   B 1 51  ? 54.807 -23.089 2.852   1.00 13.43 ?  51  GLY   B HA2  1 
ATOM   4510 H HA3  . GLY   B 1 51  ? 54.704 -24.656 2.745   1.00 13.43 ?  51  GLY   B HA3  1 
ATOM   4511 N N    . ALA   B 1 52  ? 54.499 -24.428 -0.033  1.00 10.78 ?  52  ALA   B N    1 
ATOM   4512 C CA   . ALA   B 1 52  ? 55.052 -24.432 -1.381  1.00 11.34 ?  52  ALA   B CA   1 
ATOM   4513 C C    . ALA   B 1 52  ? 54.976 -23.053 -2.027  1.00 10.65 ?  52  ALA   B C    1 
ATOM   4514 O O    . ALA   B 1 52  ? 55.940 -22.604 -2.666  1.00 11.11 ?  52  ALA   B O    1 
ATOM   4515 C CB   . ALA   B 1 52  ? 54.334 -25.468 -2.239  1.00 12.10 ?  52  ALA   B CB   1 
ATOM   4516 H H    . ALA   B 1 52  ? 53.765 -24.872 0.054   1.00 12.95 ?  52  ALA   B H    1 
ATOM   4517 H HA   . ALA   B 1 52  ? 55.986 -24.683 -1.330  1.00 13.61 ?  52  ALA   B HA   1 
ATOM   4518 H HB1  . ALA   B 1 52  ? 54.719 -25.456 -3.131  1.00 14.53 ?  52  ALA   B HB1  1 
ATOM   4519 H HB2  . ALA   B 1 52  ? 54.453 -26.343 -1.840  1.00 14.53 ?  52  ALA   B HB2  1 
ATOM   4520 H HB3  . ALA   B 1 52  ? 53.393 -25.245 -2.282  1.00 14.53 ?  52  ALA   B HB3  1 
ATOM   4521 N N    . LEU   B 1 53  ? 53.830 -22.379 -1.904  1.00 10.05 ?  53  LEU   B N    1 
ATOM   4522 C CA   . LEU   B 1 53  ? 53.714 -21.043 -2.474  1.00 10.39 ?  53  LEU   B CA   1 
ATOM   4523 C C    . LEU   B 1 53  ? 54.718 -20.102 -1.827  1.00 10.43 ?  53  LEU   B C    1 
ATOM   4524 O O    . LEU   B 1 53  ? 55.418 -19.350 -2.513  1.00 11.13 ?  53  LEU   B O    1 
ATOM   4525 C CB   . LEU   B 1 53  ? 52.288 -20.510 -2.297  1.00 10.95 ?  53  LEU   B CB   1 
ATOM   4526 C CG   . LEU   B 1 53  ? 51.166 -21.226 -3.057  1.00 11.29 ?  53  LEU   B CG   1 
ATOM   4527 C CD1  . LEU   B 1 53  ? 49.811 -20.635 -2.702  1.00 12.64 ?  53  LEU   B CD1  1 
ATOM   4528 C CD2  . LEU   B 1 53  ? 51.387 -21.180 -4.564  1.00 12.80 ?  53  LEU   B CD2  1 
ATOM   4529 H H    . LEU   B 1 53  ? 53.125 -22.665 -1.505  1.00 12.06 ?  53  LEU   B H    1 
ATOM   4530 H HA   . LEU   B 1 53  ? 53.906 -21.082 -3.426  1.00 12.48 ?  53  LEU   B HA   1 
ATOM   4531 H HB2  . LEU   B 1 53  ? 52.065 -20.557 -1.355  1.00 13.15 ?  53  LEU   B HB2  1 
ATOM   4532 H HB3  . LEU   B 1 53  ? 52.273 -19.585 -2.584  1.00 13.15 ?  53  LEU   B HB3  1 
ATOM   4533 H HG   . LEU   B 1 53  ? 51.151 -22.160 -2.788  1.00 13.55 ?  53  LEU   B HG   1 
ATOM   4534 H HD11 . LEU   B 1 53  ? 49.119 -21.110 -3.193  1.00 15.17 ?  53  LEU   B HD11 1 
ATOM   4535 H HD12 . LEU   B 1 53  ? 49.661 -20.736 -1.747  1.00 15.17 ?  53  LEU   B HD12 1 
ATOM   4536 H HD13 . LEU   B 1 53  ? 49.801 -19.697 -2.942  1.00 15.17 ?  53  LEU   B HD13 1 
ATOM   4537 H HD21 . LEU   B 1 53  ? 50.648 -21.623 -5.009  1.00 15.37 ?  53  LEU   B HD21 1 
ATOM   4538 H HD22 . LEU   B 1 53  ? 51.434 -20.254 -4.847  1.00 15.37 ?  53  LEU   B HD22 1 
ATOM   4539 H HD23 . LEU   B 1 53  ? 52.218 -21.634 -4.775  1.00 15.37 ?  53  LEU   B HD23 1 
ATOM   4540 N N    . ASN   B 1 54  ? 54.813 -20.138 -0.498  1.00 10.20 ?  54  ASN   B N    1 
ATOM   4541 C CA   . ASN   B 1 54  ? 55.723 -19.224 0.175   1.00 10.97 ?  54  ASN   B CA   1 
ATOM   4542 C C    . ASN   B 1 54  ? 57.167 -19.493 -0.228  1.00 10.94 ?  54  ASN   B C    1 
ATOM   4543 O O    . ASN   B 1 54  ? 57.937 -18.553 -0.464  1.00 11.60 ?  54  ASN   B O    1 
ATOM   4544 C CB   . ASN   B 1 54  ? 55.565 -19.310 1.688   1.00 11.51 ?  54  ASN   B CB   1 
ATOM   4545 C CG   . ASN   B 1 54  ? 56.544 -18.401 2.403   1.00 11.66 ?  54  ASN   B CG   1 
ATOM   4546 O OD1  . ASN   B 1 54  ? 56.560 -17.185 2.168   1.00 11.65 ?  54  ASN   B OD1  1 
ATOM   4547 N ND2  . ASN   B 1 54  ? 57.387 -18.983 3.249   1.00 13.07 ?  54  ASN   B ND2  1 
ATOM   4548 H H    . ASN   B 1 54  ? 54.377 -20.670 0.017   1.00 12.25 ?  54  ASN   B H    1 
ATOM   4549 H HA   . ASN   B 1 54  ? 55.506 -18.318 -0.094  1.00 13.17 ?  54  ASN   B HA   1 
ATOM   4550 H HB2  . ASN   B 1 54  ? 54.662 -19.036 1.927   1.00 13.82 ?  54  ASN   B HB2  1 
ATOM   4551 H HB3  . ASN   B 1 54  ? 55.724 -20.221 1.974   1.00 13.82 ?  54  ASN   B HB3  1 
ATOM   4552 H HD21 . ASN   B 1 54  ? 57.965 -18.511 3.674   1.00 15.69 ?  54  ASN   B HD21 1 
ATOM   4553 H HD22 . ASN   B 1 54  ? 57.353 -19.835 3.376   1.00 15.69 ?  54  ASN   B HD22 1 
ATOM   4554 N N    . LYS   B 1 55  ? 57.555 -20.769 -0.302  1.00 11.69 ?  55  LYS   B N    1 
ATOM   4555 C CA   . LYS   B 1 55  ? 58.912 -21.105 -0.720  1.00 12.49 ?  55  LYS   B CA   1 
ATOM   4556 C C    . LYS   B 1 55  ? 59.211 -20.561 -2.112  1.00 12.28 ?  55  LYS   B C    1 
ATOM   4557 O O    . LYS   B 1 55  ? 60.309 -20.048 -2.362  1.00 12.68 ?  55  LYS   B O    1 
ATOM   4558 C CB   . LYS   B 1 55  ? 59.106 -22.621 -0.670  1.00 13.45 ?  55  LYS   B CB   1 
ATOM   4559 C CG   . LYS   B 1 55  ? 60.503 -23.073 -1.044  1.00 17.24 ?  55  LYS   B CG   1 
ATOM   4560 C CD   . LYS   B 1 55  ? 60.670 -24.577 -0.905  1.00 20.48 ?  55  LYS   B CD   1 
ATOM   4561 C CE   . LYS   B 1 55  ? 60.565 -25.024 0.549   1.00 23.43 ?  55  LYS   B CE   1 
ATOM   4562 N NZ   . LYS   B 1 55  ? 61.022 -26.419 0.744   1.00 24.92 ?  55  LYS   B NZ   1 
ATOM   4563 H H    . LYS   B 1 55  ? 57.058 -21.442 -0.112  1.00 14.04 ?  55  LYS   B H    1 
ATOM   4564 H HA   . LYS   B 1 55  ? 59.541 -20.703 -0.101  1.00 15.00 ?  55  LYS   B HA   1 
ATOM   4565 H HB2  . LYS   B 1 55  ? 58.925 -22.923 0.235   1.00 16.15 ?  55  LYS   B HB2  1 
ATOM   4566 H HB3  . LYS   B 1 55  ? 58.485 -23.037 -1.285  1.00 16.15 ?  55  LYS   B HB3  1 
ATOM   4567 H HG2  . LYS   B 1 55  ? 60.681 -22.837 -1.968  1.00 20.70 ?  55  LYS   B HG2  1 
ATOM   4568 H HG3  . LYS   B 1 55  ? 61.148 -22.643 -0.459  1.00 20.70 ?  55  LYS   B HG3  1 
ATOM   4569 H HD2  . LYS   B 1 55  ? 59.976 -25.027 -1.411  1.00 24.59 ?  55  LYS   B HD2  1 
ATOM   4570 H HD3  . LYS   B 1 55  ? 61.547 -24.836 -1.235  1.00 24.59 ?  55  LYS   B HD3  1 
ATOM   4571 H HE2  . LYS   B 1 55  ? 61.113 -24.436 1.098   1.00 28.12 ?  55  LYS   B HE2  1 
ATOM   4572 H HE3  . LYS   B 1 55  ? 59.635 -24.961 0.829   1.00 28.12 ?  55  LYS   B HE3  1 
ATOM   4573 H HZ1  . LYS   B 1 55  ? 60.919 -26.653 1.596   1.00 29.92 ?  55  LYS   B HZ1  1 
ATOM   4574 H HZ2  . LYS   B 1 55  ? 60.542 -26.966 0.232   1.00 29.92 ?  55  LYS   B HZ2  1 
ATOM   4575 H HZ3  . LYS   B 1 55  ? 61.879 -26.489 0.523   1.00 29.92 ?  55  LYS   B HZ3  1 
ATOM   4576 N N    . ALA   B 1 56  ? 58.240 -20.640 -3.028  1.00 11.98 ?  56  ALA   B N    1 
ATOM   4577 C CA   . ALA   B 1 56  ? 58.463 -20.134 -4.378  1.00 12.63 ?  56  ALA   B CA   1 
ATOM   4578 C C    . ALA   B 1 56  ? 58.735 -18.638 -4.374  1.00 12.24 ?  56  ALA   B C    1 
ATOM   4579 O O    . ALA   B 1 56  ? 59.457 -18.133 -5.247  1.00 13.31 ?  56  ALA   B O    1 
ATOM   4580 C CB   . ALA   B 1 56  ? 57.270 -20.462 -5.275  1.00 13.77 ?  56  ALA   B CB   1 
ATOM   4581 H H    . ALA   B 1 56  ? 57.454 -20.970 -2.891  1.00 14.39 ?  56  ALA   B H    1 
ATOM   4582 H HA   . ALA   B 1 56  ? 59.244 -20.570 -4.746  1.00 15.16 ?  56  ALA   B HA   1 
ATOM   4583 H HB1  . ALA   B 1 56  ? 57.447 -20.122 -6.168  1.00 16.54 ?  56  ALA   B HB1  1 
ATOM   4584 H HB2  . ALA   B 1 56  ? 57.159 -21.425 -5.305  1.00 16.54 ?  56  ALA   B HB2  1 
ATOM   4585 H HB3  . ALA   B 1 56  ? 56.476 -20.045 -4.912  1.00 16.54 ?  56  ALA   B HB3  1 
ATOM   4586 N N    . THR   B 1 57  ? 58.172 -17.913 -3.403  1.00 12.08 ?  57  THR   B N    1 
ATOM   4587 C CA   . THR   B 1 57  ? 58.404 -16.478 -3.269  1.00 12.17 ?  57  THR   B CA   1 
ATOM   4588 C C    . THR   B 1 57  ? 59.651 -16.152 -2.455  1.00 13.07 ?  57  THR   B C    1 
ATOM   4589 O O    . THR   B 1 57  ? 59.884 -14.977 -2.143  1.00 13.43 ?  57  THR   B O    1 
ATOM   4590 C CB   . THR   B 1 57  ? 57.200 -15.759 -2.632  1.00 11.71 ?  57  THR   B CB   1 
ATOM   4591 O OG1  . THR   B 1 57  ? 57.184 -15.970 -1.211  1.00 11.62 ?  57  THR   B OG1  1 
ATOM   4592 C CG2  . THR   B 1 57  ? 55.879 -16.197 -3.262  1.00 11.85 ?  57  THR   B CG2  1 
ATOM   4593 H H    . THR   B 1 57  ? 57.636 -18.232 -2.807  1.00 14.50 ?  57  THR   B H    1 
ATOM   4594 H HA   . THR   B 1 57  ? 58.524 -16.105 -4.155  1.00 14.61 ?  57  THR   B HA   1 
ATOM   4595 H HB   . THR   B 1 57  ? 57.287 -14.809 -2.800  1.00 14.06 ?  57  THR   B HB   1 
ATOM   4596 H HG1  . THR   B 1 57  ? 57.117 -16.792 -1.046  1.00 13.96 ?  57  THR   B HG1  1 
ATOM   4597 H HG21 . THR   B 1 57  ? 55.150 -15.657 -2.927  1.00 14.23 ?  57  THR   B HG21 1 
ATOM   4598 H HG22 . THR   B 1 57  ? 55.922 -16.111 -4.227  1.00 14.23 ?  57  THR   B HG22 1 
ATOM   4599 H HG23 . THR   B 1 57  ? 55.700 -17.130 -3.045  1.00 14.23 ?  57  THR   B HG23 1 
ATOM   4600 N N    . ASN   B 1 58  ? 60.449 -17.155 -2.095  1.00 13.77 ?  58  ASN   B N    1 
ATOM   4601 C CA   . ASN   B 1 58  ? 61.651 -16.935 -1.294  1.00 16.47 ?  58  ASN   B CA   1 
ATOM   4602 C C    . ASN   B 1 58  ? 61.310 -16.229 0.020   1.00 14.35 ?  58  ASN   B C    1 
ATOM   4603 O O    . ASN   B 1 58  ? 62.042 -15.354 0.489   1.00 15.05 ?  58  ASN   B O    1 
ATOM   4604 C CB   . ASN   B 1 58  ? 62.724 -16.176 -2.079  1.00 24.32 ?  58  ASN   B CB   1 
ATOM   4605 C CG   . ASN   B 1 58  ? 64.090 -16.259 -1.426  1.00 32.46 ?  58  ASN   B CG   1 
ATOM   4606 O OD1  . ASN   B 1 58  ? 64.409 -17.238 -0.752  1.00 35.88 ?  58  ASN   B OD1  1 
ATOM   4607 N ND2  . ASN   B 1 58  ? 64.903 -15.227 -1.621  1.00 36.04 ?  58  ASN   B ND2  1 
ATOM   4608 H H    . ASN   B 1 58  ? 60.314 -17.984 -2.299  1.00 16.54 ?  58  ASN   B H    1 
ATOM   4609 H HA   . ASN   B 1 58  ? 62.025 -17.802 -1.069  1.00 19.78 ?  58  ASN   B HA   1 
ATOM   4610 H HB2  . ASN   B 1 58  ? 62.794 -16.556 -2.972  1.00 29.19 ?  58  ASN   B HB2  1 
ATOM   4611 H HB3  . ASN   B 1 58  ? 62.477 -15.241 -2.136  1.00 29.19 ?  58  ASN   B HB3  1 
ATOM   4612 H HD21 . ASN   B 1 58  ? 65.690 -15.226 -1.273  1.00 43.25 ?  58  ASN   B HD21 1 
ATOM   4613 H HD22 . ASN   B 1 58  ? 64.644 -14.559 -2.097  1.00 43.25 ?  58  ASN   B HD22 1 
ATOM   4614 N N    . ASN   B 1 59  ? 60.187 -16.623 0.621   1.00 13.20 ?  59  ASN   B N    1 
ATOM   4615 C CA   . ASN   B 1 59  ? 59.706 -16.158 1.921   1.00 13.21 ?  59  ASN   B CA   1 
ATOM   4616 C C    . ASN   B 1 59  ? 59.105 -14.752 1.871   1.00 12.40 ?  59  ASN   B C    1 
ATOM   4617 O O    . ASN   B 1 59  ? 58.673 -14.249 2.919   1.00 12.71 ?  59  ASN   B O    1 
ATOM   4618 C CB   . ASN   B 1 59  ? 60.775 -16.220 3.025   1.00 14.31 ?  59  ASN   B CB   1 
ATOM   4619 C CG   . ASN   B 1 59  ? 60.183 -16.406 4.400   1.00 15.44 ?  59  ASN   B CG   1 
ATOM   4620 O OD1  . ASN   B 1 59  ? 59.357 -17.294 4.616   1.00 15.81 ?  59  ASN   B OD1  1 
ATOM   4621 N ND2  . ASN   B 1 59  ? 60.597 -15.568 5.342   1.00 16.27 ?  59  ASN   B ND2  1 
ATOM   4622 H H    . ASN   B 1 59  ? 59.653 -17.199 0.270   1.00 15.85 ?  59  ASN   B H    1 
ATOM   4623 H HA   . ASN   B 1 59  ? 58.995 -16.756 2.197   1.00 15.86 ?  59  ASN   B HA   1 
ATOM   4624 H HB2  . ASN   B 1 59  ? 61.366 -16.972 2.858   1.00 17.18 ?  59  ASN   B HB2  1 
ATOM   4625 H HB3  . ASN   B 1 59  ? 61.279 -15.395 3.033   1.00 17.18 ?  59  ASN   B HB3  1 
ATOM   4626 H HD21 . ASN   B 1 59  ? 60.284 -15.630 6.143   1.00 19.54 ?  59  ASN   B HD21 1 
ATOM   4627 H HD22 . ASN   B 1 59  ? 61.169 -14.957 5.152   1.00 19.54 ?  59  ASN   B HD22 1 
ATOM   4628 N N    . ALA   B 1 60  ? 59.045 -14.103 0.705   1.00 12.30 ?  60  ALA   B N    1 
ATOM   4629 C CA   . ALA   B 1 60  ? 58.449 -12.770 0.644   1.00 12.53 ?  60  ALA   B CA   1 
ATOM   4630 C C    . ALA   B 1 60  ? 56.978 -12.796 1.038   1.00 11.68 ?  60  ALA   B C    1 
ATOM   4631 O O    . ALA   B 1 60  ? 56.475 -11.844 1.650   1.00 12.09 ?  60  ALA   B O    1 
ATOM   4632 C CB   . ALA   B 1 60  ? 58.623 -12.177 -0.755  1.00 13.26 ?  60  ALA   B CB   1 
ATOM   4633 H H    . ALA   B 1 60  ? 59.337 -14.408 -0.040  1.00 14.77 ?  60  ALA   B H    1 
ATOM   4634 H HA   . ALA   B 1 60  ? 58.910 -12.194 1.270   1.00 15.05 ?  60  ALA   B HA   1 
ATOM   4635 H HB1  . ALA   B 1 60  ? 58.223 -11.295 -0.774  1.00 15.93 ?  60  ALA   B HB1  1 
ATOM   4636 H HB2  . ALA   B 1 60  ? 59.572 -12.115 -0.955  1.00 15.93 ?  60  ALA   B HB2  1 
ATOM   4637 H HB3  . ALA   B 1 60  ? 58.188 -12.755 -1.401  1.00 15.93 ?  60  ALA   B HB3  1 
ATOM   4638 N N    . MET   B 1 61  ? 56.274 -13.873 0.697   1.00 11.22 ?  61  MET   B N    1 
ATOM   4639 C CA   . MET   B 1 61  ? 54.878 -13.997 1.096   1.00 11.18 ?  61  MET   B CA   1 
ATOM   4640 C C    . MET   B 1 61  ? 54.743 -14.018 2.619   1.00 10.99 ?  61  MET   B C    1 
ATOM   4641 O O    . MET   B 1 61  ? 53.851 -13.370 3.177   1.00 10.93 ?  61  MET   B O    1 
ATOM   4642 C CB   . MET   B 1 61  ? 54.295 -15.260 0.458   1.00 10.74 ?  61  MET   B CB   1 
ATOM   4643 C CG   . MET   B 1 61  ? 52.850 -15.557 0.869   1.00 10.68 ?  61  MET   B CG   1 
ATOM   4644 S SD   . MET   B 1 61  ? 52.213 -17.064 0.115   1.00 11.57 ?  61  MET   B SD   1 
ATOM   4645 C CE   . MET   B 1 61  ? 51.967 -16.507 -1.570  1.00 12.84 ?  61  MET   B CE   1 
ATOM   4646 H H    . MET   B 1 61  ? 56.578 -14.540 0.240   1.00 13.47 ?  61  MET   B H    1 
ATOM   4647 H HA   . MET   B 1 61  ? 54.386 -13.241 0.742   1.00 13.43 ?  61  MET   B HA   1 
ATOM   4648 H HB2  . MET   B 1 61  ? 54.307 -15.163 -0.510  1.00 12.90 ?  61  MET   B HB2  1 
ATOM   4649 H HB3  . MET   B 1 61  ? 54.834 -16.024 0.714   1.00 12.90 ?  61  MET   B HB3  1 
ATOM   4650 H HG2  . MET   B 1 61  ? 52.806 -15.669 1.832   1.00 12.83 ?  61  MET   B HG2  1 
ATOM   4651 H HG3  . MET   B 1 61  ? 52.281 -14.821 0.594   1.00 12.83 ?  61  MET   B HG3  1 
ATOM   4652 H HE1  . MET   B 1 61  ? 51.595 -17.237 -2.093  1.00 15.41 ?  61  MET   B HE1  1 
ATOM   4653 H HE2  . MET   B 1 61  ? 51.354 -15.757 -1.568  1.00 15.41 ?  61  MET   B HE2  1 
ATOM   4654 H HE3  . MET   B 1 61  ? 52.821 -16.238 -1.942  1.00 15.41 ?  61  MET   B HE3  1 
ATOM   4655 N N    . GLN   B 1 62  ? 55.626 -14.741 3.314   1.00 10.99 ?  62  GLN   B N    1 
ATOM   4656 C CA   . GLN   B 1 62  ? 55.527 -14.804 4.771   1.00 11.16 ?  62  GLN   B CA   1 
ATOM   4657 C C    . GLN   B 1 62  ? 55.806 -13.450 5.410   1.00 11.44 ?  62  GLN   B C    1 
ATOM   4658 O O    . GLN   B 1 62  ? 55.127 -13.057 6.365   1.00 11.87 ?  62  GLN   B O    1 
ATOM   4659 C CB   . GLN   B 1 62  ? 56.479 -15.861 5.329   1.00 11.42 ?  62  GLN   B CB   1 
ATOM   4660 C CG   . GLN   B 1 62  ? 56.262 -16.139 6.807   1.00 11.62 ?  62  GLN   B CG   1 
ATOM   4661 C CD   . GLN   B 1 62  ? 54.890 -16.723 7.050   1.00 11.53 ?  62  GLN   B CD   1 
ATOM   4662 O OE1  . GLN   B 1 62  ? 54.638 -17.874 6.704   1.00 11.82 ?  62  GLN   B OE1  1 
ATOM   4663 N NE2  . GLN   B 1 62  ? 53.980 -15.930 7.604   1.00 11.94 ?  62  GLN   B NE2  1 
ATOM   4664 H H    . GLN   B 1 62  ? 56.268 -15.199 2.967   1.00 13.19 ?  62  GLN   B H    1 
ATOM   4665 H HA   . GLN   B 1 62  ? 54.623 -15.064 5.004   1.00 13.40 ?  62  GLN   B HA   1 
ATOM   4666 H HB2  . GLN   B 1 62  ? 56.354 -16.692 4.844   1.00 13.71 ?  62  GLN   B HB2  1 
ATOM   4667 H HB3  . GLN   B 1 62  ? 57.395 -15.551 5.214   1.00 13.71 ?  62  GLN   B HB3  1 
ATOM   4668 H HG2  . GLN   B 1 62  ? 56.925 -16.777 7.111   1.00 13.95 ?  62  GLN   B HG2  1 
ATOM   4669 H HG3  . GLN   B 1 62  ? 56.336 -15.311 7.304   1.00 13.95 ?  62  GLN   B HG3  1 
ATOM   4670 H HE21 . GLN   B 1 62  ? 54.189 -15.126 7.822   1.00 14.34 ?  62  GLN   B HE21 1 
ATOM   4671 H HE22 . GLN   B 1 62  ? 53.188 -16.226 7.751   1.00 14.34 ?  62  GLN   B HE22 1 
ATOM   4672 N N    . VAL   B 1 63  ? 56.813 -12.730 4.916   1.00 12.16 ?  63  VAL   B N    1 
ATOM   4673 C CA   . VAL   B 1 63  ? 57.122 -11.419 5.482   1.00 12.91 ?  63  VAL   B CA   1 
ATOM   4674 C C    . VAL   B 1 63  ? 55.932 -10.480 5.310   1.00 12.32 ?  63  VAL   B C    1 
ATOM   4675 O O    . VAL   B 1 63  ? 55.526 -9.779  6.246   1.00 13.13 ?  63  VAL   B O    1 
ATOM   4676 C CB   . VAL   B 1 63  ? 58.410 -10.857 4.856   1.00 14.39 ?  63  VAL   B CB   1 
ATOM   4677 C CG1  . VAL   B 1 63  ? 58.646 -9.422  5.317   1.00 15.05 ?  63  VAL   B CG1  1 
ATOM   4678 C CG2  . VAL   B 1 63  ? 59.593 -11.732 5.234   1.00 15.20 ?  63  VAL   B CG2  1 
ATOM   4679 H H    . VAL   B 1 63  ? 57.322 -12.973 4.263   1.00 14.60 ?  63  VAL   B H    1 
ATOM   4680 H HA   . VAL   B 1 63  ? 57.280 -11.525 6.431   1.00 15.50 ?  63  VAL   B HA   1 
ATOM   4681 H HB   . VAL   B 1 63  ? 58.329 -10.856 3.891   1.00 17.28 ?  63  VAL   B HB   1 
ATOM   4682 H HG11 . VAL   B 1 63  ? 59.560 -9.171  5.114   1.00 18.07 ?  63  VAL   B HG11 1 
ATOM   4683 H HG12 . VAL   B 1 63  ? 58.031 -8.832  4.854   1.00 18.07 ?  63  VAL   B HG12 1 
ATOM   4684 H HG13 . VAL   B 1 63  ? 58.497 -9.370  6.276   1.00 18.07 ?  63  VAL   B HG13 1 
ATOM   4685 H HG21 . VAL   B 1 63  ? 60.402 -11.352 4.855   1.00 18.25 ?  63  VAL   B HG21 1 
ATOM   4686 H HG22 . VAL   B 1 63  ? 59.666 -11.762 6.203   1.00 18.25 ?  63  VAL   B HG22 1 
ATOM   4687 H HG23 . VAL   B 1 63  ? 59.451 -12.624 4.886   1.00 18.25 ?  63  VAL   B HG23 1 
ATOM   4688 N N    . GLU   B 1 64  ? 55.357 -10.458 4.104   1.00 12.16 ?  64  GLU   B N    1 
ATOM   4689 C CA   . GLU   B 1 64  ? 54.184 -9.624  3.840   1.00 11.57 ?  64  GLU   B CA   1 
ATOM   4690 C C    . GLU   B 1 64  ? 53.009 -10.031 4.722   1.00 11.08 ?  64  GLU   B C    1 
ATOM   4691 O O    . GLU   B 1 64  ? 52.268 -9.176  5.233   1.00 11.99 ?  64  GLU   B O    1 
ATOM   4692 C CB   . GLU   B 1 64  ? 53.815 -9.765  2.363   1.00 11.97 ?  64  GLU   B CB   1 
ATOM   4693 C CG   . GLU   B 1 64  ? 52.556 -9.027  1.937   1.00 12.18 ?  64  GLU   B CG   1 
ATOM   4694 C CD   . GLU   B 1 64  ? 52.014 -9.513  0.597   1.00 13.02 ?  64  GLU   B CD   1 
ATOM   4695 O OE1  . GLU   B 1 64  ? 52.197 -10.715 0.262   1.00 13.67 ?  64  GLU   B OE1  1 
ATOM   4696 O OE2  . GLU   B 1 64  ? 51.382 -8.695  -0.117  1.00 13.73 -1 64  GLU   B OE2  1 
ATOM   4697 H H    . GLU   B 1 64  ? 55.633 -10.914 3.425   1.00 14.60 ?  64  GLU   B H    1 
ATOM   4698 H HA   . GLU   B 1 64  ? 54.403 -8.696  4.017   1.00 13.89 ?  64  GLU   B HA   1 
ATOM   4699 H HB2  . GLU   B 1 64  ? 54.547 -9.417  1.825   1.00 14.37 ?  64  GLU   B HB2  1 
ATOM   4700 H HB3  . GLU   B 1 64  ? 53.687 -10.703 2.166   1.00 14.37 ?  64  GLU   B HB3  1 
ATOM   4701 H HG2  . GLU   B 1 64  ? 51.858 -9.157  2.602   1.00 14.62 ?  64  GLU   B HG2  1 
ATOM   4702 H HG3  . GLU   B 1 64  ? 52.754 -8.082  1.852   1.00 14.62 ?  64  GLU   B HG3  1 
ATOM   4703 N N    . SER   B 1 65  ? 52.825 -11.339 4.898   1.00 11.22 ?  65  SER   B N    1 
ATOM   4704 C CA   . SER   B 1 65  ? 51.724 -11.855 5.701   1.00 11.29 ?  65  SER   B CA   1 
ATOM   4705 C C    . SER   B 1 65  ? 51.867 -11.463 7.166   1.00 11.19 ?  65  SER   B C    1 
ATOM   4706 O O    . SER   B 1 65  ? 50.875 -11.094 7.813   1.00 11.74 ?  65  SER   B O    1 
ATOM   4707 C CB   . SER   B 1 65  ? 51.657 -13.374 5.567   1.00 11.48 ?  65  SER   B CB   1 
ATOM   4708 O OG   . SER   B 1 65  ? 51.288 -13.772 4.252   1.00 11.61 ?  65  SER   B OG   1 
ATOM   4709 H H    . SER   B 1 65  ? 53.333 -11.955 4.567   1.00 13.48 ?  65  SER   B H    1 
ATOM   4710 H HA   . SER   B 1 65  ? 50.890 -11.486 5.369   1.00 13.56 ?  65  SER   B HA   1 
ATOM   4711 H HB2  . SER   B 1 65  ? 52.527 -13.745 5.772   1.00 13.79 ?  65  SER   B HB2  1 
ATOM   4712 H HB3  . SER   B 1 65  ? 50.997 -13.713 6.192   1.00 13.79 ?  65  SER   B HB3  1 
ATOM   4713 H HG   . SER   B 1 65  ? 51.851 -13.477 3.695   1.00 13.94 ?  65  SER   B HG   1 
ATOM   4714 N N    . ASP   B 1 66  ? 53.079 -11.561 7.719   1.00 11.67 ?  66  ASP   B N    1 
ATOM   4715 C CA   . ASP   B 1 66  ? 53.279 -11.177 9.115   1.00 12.30 ?  66  ASP   B CA   1 
ATOM   4716 C C    . ASP   B 1 66  ? 52.958 -9.703  9.327   1.00 12.38 ?  66  ASP   B C    1 
ATOM   4717 O O    . ASP   B 1 66  ? 52.382 -9.321  10.353  1.00 12.67 ?  66  ASP   B O    1 
ATOM   4718 C CB   . ASP   B 1 66  ? 54.715 -11.479 9.549   1.00 13.81 ?  66  ASP   B CB   1 
ATOM   4719 C CG   . ASP   B 1 66  ? 54.989 -12.963 9.695   1.00 15.53 ?  66  ASP   B CG   1 
ATOM   4720 O OD1  . ASP   B 1 66  ? 54.046 -13.778 9.616   1.00 15.91 ?  66  ASP   B OD1  1 
ATOM   4721 O OD2  . ASP   B 1 66  ? 56.167 -13.317 9.900   1.00 18.15 -1 66  ASP   B OD2  1 
ATOM   4722 H H    . ASP   B 1 66  ? 53.782 -11.845 7.318   1.00 14.01 ?  66  ASP   B H    1 
ATOM   4723 H HA   . ASP   B 1 66  ? 52.685 -11.690 9.678   1.00 14.77 ?  66  ASP   B HA   1 
ATOM   4724 H HB2  . ASP   B 1 66  ? 55.331 -11.130 8.885   1.00 16.58 ?  66  ASP   B HB2  1 
ATOM   4725 H HB3  . ASP   B 1 66  ? 54.885 -11.056 10.408  1.00 16.58 ?  66  ASP   B HB3  1 
ATOM   4726 N N    . ASP   B 1 67  ? 53.329 -8.851  8.371   1.00 12.01 ?  67  ASP   B N    1 
ATOM   4727 C CA   . ASP   B 1 67  ? 52.977 -7.439  8.473   1.00 12.54 ?  67  ASP   B CA   1 
ATOM   4728 C C    . ASP   B 1 67  ? 51.464 -7.236  8.395   1.00 12.41 ?  67  ASP   B C    1 
ATOM   4729 O O    . ASP   B 1 67  ? 50.899 -6.430  9.143   1.00 13.18 ?  67  ASP   B O    1 
ATOM   4730 C CB   . ASP   B 1 67  ? 53.686 -6.654  7.379   1.00 14.04 ?  67  ASP   B CB   1 
ATOM   4731 C CG   . ASP   B 1 67  ? 53.272 -5.210  7.361   1.00 15.28 ?  67  ASP   B CG   1 
ATOM   4732 O OD1  . ASP   B 1 67  ? 53.770 -4.422  8.195   1.00 16.08 ?  67  ASP   B OD1  1 
ATOM   4733 O OD2  . ASP   B 1 67  ? 52.419 -4.877  6.523   1.00 16.49 -1 67  ASP   B OD2  1 
ATOM   4734 H H    . ASP   B 1 67  ? 53.785 -9.061  7.670   1.00 14.43 ?  67  ASP   B H    1 
ATOM   4735 H HA   . ASP   B 1 67  ? 53.286 -7.099  9.326   1.00 15.06 ?  67  ASP   B HA   1 
ATOM   4736 H HB2  . ASP   B 1 67  ? 54.643 -6.675  7.529   1.00 16.86 ?  67  ASP   B HB2  1 
ATOM   4737 H HB3  . ASP   B 1 67  ? 53.479 -7.048  6.513   1.00 16.86 ?  67  ASP   B HB3  1 
ATOM   4738 N N    . TYR   B 1 68  ? 50.786 -7.965  7.504   1.00 12.11 ?  68  TYR   B N    1 
ATOM   4739 C CA   . TYR   B 1 68  ? 49.327 -7.889  7.439   1.00 12.84 ?  68  TYR   B CA   1 
ATOM   4740 C C    . TYR   B 1 68  ? 48.694 -8.239  8.783   1.00 12.37 ?  68  TYR   B C    1 
ATOM   4741 O O    . TYR   B 1 68  ? 47.766 -7.561  9.239   1.00 12.95 ?  68  TYR   B O    1 
ATOM   4742 C CB   . TYR   B 1 68  ? 48.793 -8.816  6.340   1.00 13.86 ?  68  TYR   B CB   1 
ATOM   4743 C CG   . TYR   B 1 68  ? 47.285 -8.969  6.392   1.00 14.60 ?  68  TYR   B CG   1 
ATOM   4744 C CD1  . TYR   B 1 68  ? 46.691 -9.926  7.209   1.00 15.37 ?  68  TYR   B CD1  1 
ATOM   4745 C CD2  . TYR   B 1 68  ? 46.460 -8.127  5.669   1.00 15.55 ?  68  TYR   B CD2  1 
ATOM   4746 C CE1  . TYR   B 1 68  ? 45.323 -10.048 7.292   1.00 16.32 ?  68  TYR   B CE1  1 
ATOM   4747 C CE2  . TYR   B 1 68  ? 45.079 -8.251  5.737   1.00 16.03 ?  68  TYR   B CE2  1 
ATOM   4748 C CZ   . TYR   B 1 68  ? 44.526 -9.207  6.555   1.00 16.27 ?  68  TYR   B CZ   1 
ATOM   4749 O OH   . TYR   B 1 68  ? 43.157 -9.320  6.638   1.00 17.17 ?  68  TYR   B OH   1 
ATOM   4750 H H    . TYR   B 1 68  ? 51.143 -8.512  6.943   1.00 14.54 ?  68  TYR   B H    1 
ATOM   4751 H HA   . TYR   B 1 68  ? 49.075 -6.982  7.221   1.00 15.42 ?  68  TYR   B HA   1 
ATOM   4752 H HB2  . TYR   B 1 68  ? 49.025 -8.444  5.479   1.00 16.64 ?  68  TYR   B HB2  1 
ATOM   4753 H HB3  . TYR   B 1 68  ? 49.188 -9.693  6.448   1.00 16.64 ?  68  TYR   B HB3  1 
ATOM   4754 H HD1  . TYR   B 1 68  ? 47.226 -10.499 7.713   1.00 18.45 ?  68  TYR   B HD1  1 
ATOM   4755 H HD2  . TYR   B 1 68  ? 46.838 -7.474  5.132   1.00 18.67 ?  68  TYR   B HD2  1 
ATOM   4756 H HE1  . TYR   B 1 68  ? 44.937 -10.706 7.830   1.00 19.59 ?  68  TYR   B HE1  1 
ATOM   4757 H HE2  . TYR   B 1 68  ? 44.534 -7.682  5.247   1.00 19.24 ?  68  TYR   B HE2  1 
ATOM   4758 H HH   . TYR   B 1 68  ? 42.781 -8.765  6.125   1.00 20.61 ?  68  TYR   B HH   1 
ATOM   4759 N N    . ILE   B 1 69  ? 49.175 -9.305  9.425   1.00 12.22 ?  69  ILE   B N    1 
ATOM   4760 C CA   . ILE   B 1 69  ? 48.617 -9.736  10.703  1.00 12.79 ?  69  ILE   B CA   1 
ATOM   4761 C C    . ILE   B 1 69  ? 48.876 -8.696  11.785  1.00 12.48 ?  69  ILE   B C    1 
ATOM   4762 O O    . ILE   B 1 69  ? 48.008 -8.423  12.619  1.00 13.01 ?  69  ILE   B O    1 
ATOM   4763 C CB   . ILE   B 1 69  ? 49.187 -11.116 11.088  1.00 13.91 ?  69  ILE   B CB   1 
ATOM   4764 C CG1  . ILE   B 1 69  ? 48.655 -12.207 10.154  1.00 13.92 ?  69  ILE   B CG1  1 
ATOM   4765 C CG2  . ILE   B 1 69  ? 48.902 -11.436 12.551  1.00 15.04 ?  69  ILE   B CG2  1 
ATOM   4766 C CD1  . ILE   B 1 69  ? 47.185 -12.520 10.321  1.00 14.14 ?  69  ILE   B CD1  1 
ATOM   4767 H H    . ILE   B 1 69  ? 49.826 -9.790  9.148   1.00 14.67 ?  69  ILE   B H    1 
ATOM   4768 H HA   . ILE   B 1 69  ? 47.656 -9.825  10.609  1.00 15.36 ?  69  ILE   B HA   1 
ATOM   4769 H HB   . ILE   B 1 69  ? 50.150 -11.073 10.980  1.00 16.70 ?  69  ILE   B HB   1 
ATOM   4770 H HG12 . ILE   B 1 69  ? 48.793 -11.918 9.237   1.00 16.71 ?  69  ILE   B HG12 1 
ATOM   4771 H HG13 . ILE   B 1 69  ? 49.153 -13.020 10.318  1.00 16.71 ?  69  ILE   B HG13 1 
ATOM   4772 H HG21 . ILE   B 1 69  ? 49.038 -12.387 12.691  1.00 18.05 ?  69  ILE   B HG21 1 
ATOM   4773 H HG22 . ILE   B 1 69  ? 49.510 -10.932 13.113  1.00 18.05 ?  69  ILE   B HG22 1 
ATOM   4774 H HG23 . ILE   B 1 69  ? 47.984 -11.201 12.753  1.00 18.05 ?  69  ILE   B HG23 1 
ATOM   4775 H HD11 . ILE   B 1 69  ? 46.943 -13.218 9.696   1.00 16.98 ?  69  ILE   B HD11 1 
ATOM   4776 H HD12 . ILE   B 1 69  ? 47.026 -12.822 11.230  1.00 16.98 ?  69  ILE   B HD12 1 
ATOM   4777 H HD13 . ILE   B 1 69  ? 46.665 -11.722 10.143  1.00 16.98 ?  69  ILE   B HD13 1 
ATOM   4778 N N    . ALA   B 1 70  ? 50.069 -8.104  11.801  1.00 12.38 ?  70  ALA   B N    1 
ATOM   4779 C CA   . ALA   B 1 70  ? 50.354 -7.075  12.793  1.00 12.50 ?  70  ALA   B CA   1 
ATOM   4780 C C    . ALA   B 1 70  ? 49.366 -5.920  12.678  1.00 12.36 ?  70  ALA   B C    1 
ATOM   4781 O O    . ALA   B 1 70  ? 48.931 -5.365  13.691  1.00 12.83 ?  70  ALA   B O    1 
ATOM   4782 C CB   . ALA   B 1 70  ? 51.794 -6.585  12.634  1.00 13.28 ?  70  ALA   B CB   1 
ATOM   4783 H H    . ALA   B 1 70  ? 50.708 -8.282  11.267  1.00 14.87 ?  70  ALA   B H    1 
ATOM   4784 H HA   . ALA   B 1 70  ? 50.266 -7.456  13.684  1.00 15.01 ?  70  ALA   B HA   1 
ATOM   4785 H HB1  . ALA   B 1 70  ? 51.977 -5.914  13.310  1.00 15.95 ?  70  ALA   B HB1  1 
ATOM   4786 H HB2  . ALA   B 1 70  ? 52.397 -7.338  12.747  1.00 15.95 ?  70  ALA   B HB2  1 
ATOM   4787 H HB3  . ALA   B 1 70  ? 51.902 -6.205  11.749  1.00 15.95 ?  70  ALA   B HB3  1 
ATOM   4788 N N    . THR   B 1 71  ? 48.989 -5.552  11.454  1.00 12.95 ?  71  THR   B N    1 
ATOM   4789 C CA   . THR   B 1 71  ? 48.097 -4.415  11.251  1.00 14.10 ?  71  THR   B CA   1 
ATOM   4790 C C    . THR   B 1 71  ? 46.629 -4.781  11.452  1.00 14.48 ?  71  THR   B C    1 
ATOM   4791 O O    . THR   B 1 71  ? 45.852 -3.962  11.960  1.00 15.93 ?  71  THR   B O    1 
ATOM   4792 C CB   . THR   B 1 71  ? 48.318 -3.842  9.849   1.00 16.16 ?  71  THR   B CB   1 
ATOM   4793 O OG1  . THR   B 1 71  ? 49.648 -3.321  9.753   1.00 18.18 ?  71  THR   B OG1  1 
ATOM   4794 C CG2  . THR   B 1 71  ? 47.311 -2.736  9.535   1.00 17.30 ?  71  THR   B CG2  1 
ATOM   4795 H H    . THR   B 1 71  ? 49.236 -5.940  10.732  1.00 15.55 ?  71  THR   B H    1 
ATOM   4796 H HA   . THR   B 1 71  ? 48.316 -3.720  11.891  1.00 16.93 ?  71  THR   B HA   1 
ATOM   4797 H HB   . THR   B 1 71  ? 48.206 -4.545  9.191   1.00 19.40 ?  71  THR   B HB   1 
ATOM   4798 H HG1  . THR   B 1 71  ? 49.777 -2.996  8.985   1.00 21.82 ?  71  THR   B HG1  1 
ATOM   4799 H HG21 . THR   B 1 71  ? 47.613 -2.219  8.769   1.00 20.77 ?  71  THR   B HG21 1 
ATOM   4800 H HG22 . THR   B 1 71  ? 46.444 -3.117  9.333   1.00 20.77 ?  71  THR   B HG22 1 
ATOM   4801 H HG23 . THR   B 1 71  ? 47.225 -2.139  10.297  1.00 20.77 ?  71  THR   B HG23 1 
ATOM   4802 N N    . ASN   B 1 72  ? 46.228 -5.994  11.056  1.00 14.19 ?  72  ASN   B N    1 
ATOM   4803 C CA   . ASN   B 1 72  ? 44.821 -6.344  10.926  1.00 14.74 ?  72  ASN   B CA   1 
ATOM   4804 C C    . ASN   B 1 72  ? 44.344 -7.449  11.859  1.00 15.02 ?  72  ASN   B C    1 
ATOM   4805 O O    . ASN   B 1 72  ? 43.129 -7.612  12.019  1.00 16.13 ?  72  ASN   B O    1 
ATOM   4806 C CB   . ASN   B 1 72  ? 44.515 -6.759  9.477   1.00 15.66 ?  72  ASN   B CB   1 
ATOM   4807 C CG   . ASN   B 1 72  ? 44.793 -5.649  8.496   1.00 16.93 ?  72  ASN   B CG   1 
ATOM   4808 O OD1  . ASN   B 1 72  ? 45.807 -5.657  7.793   1.00 18.02 ?  72  ASN   B OD1  1 
ATOM   4809 N ND2  . ASN   B 1 72  ? 43.912 -4.665  8.466   1.00 18.26 ?  72  ASN   B ND2  1 
ATOM   4810 H H    . ASN   B 1 72  ? 46.766 -6.636  10.846  1.00 17.04 ?  72  ASN   B H    1 
ATOM   4811 H HA   . ASN   B 1 72  ? 44.293 -5.557  11.114  1.00 17.69 ?  72  ASN   B HA   1 
ATOM   4812 H HB2  . ASN   B 1 72  ? 45.072 -7.517  9.236   1.00 18.80 ?  72  ASN   B HB2  1 
ATOM   4813 H HB3  . ASN   B 1 72  ? 43.578 -6.998  9.405   1.00 18.80 ?  72  ASN   B HB3  1 
ATOM   4814 H HD21 . ASN   B 1 72  ? 44.017 -4.002  7.925   1.00 21.92 ?  72  ASN   B HD21 1 
ATOM   4815 H HD22 . ASN   B 1 72  ? 43.215 -4.691  8.974   1.00 21.92 ?  72  ASN   B HD22 1 
ATOM   4816 N N    . GLY   B 1 73  ? 45.244 -8.202  12.479  1.00 14.62 ?  73  GLY   B N    1 
ATOM   4817 C CA   . GLY   B 1 73  ? 44.847 -9.347  13.261  1.00 13.90 ?  73  GLY   B CA   1 
ATOM   4818 C C    . GLY   B 1 73  ? 44.488 -10.529 12.386  1.00 12.79 ?  73  GLY   B C    1 
ATOM   4819 O O    . GLY   B 1 73  ? 44.478 -10.446 11.154  1.00 12.89 ?  73  GLY   B O    1 
ATOM   4820 H H    . GLY   B 1 73  ? 46.094 -8.067  12.457  1.00 17.55 ?  73  GLY   B H    1 
ATOM   4821 H HA2  . GLY   B 1 73  ? 45.574 -9.605  13.849  1.00 16.69 ?  73  GLY   B HA2  1 
ATOM   4822 H HA3  . GLY   B 1 73  ? 44.076 -9.118  13.804  1.00 16.69 ?  73  GLY   B HA3  1 
ATOM   4823 N N    . PRO   B 1 74  ? 44.181 -11.656 13.019  1.00 12.98 ?  74  PRO   B N    1 
ATOM   4824 C CA   . PRO   B 1 74  ? 43.931 -12.885 12.267  1.00 12.93 ?  74  PRO   B CA   1 
ATOM   4825 C C    . PRO   B 1 74  ? 42.625 -12.833 11.483  1.00 12.17 ?  74  PRO   B C    1 
ATOM   4826 O O    . PRO   B 1 74  ? 41.680 -12.103 11.806  1.00 13.21 ?  74  PRO   B O    1 
ATOM   4827 C CB   . PRO   B 1 74  ? 43.868 -13.956 13.363  1.00 13.85 ?  74  PRO   B CB   1 
ATOM   4828 C CG   . PRO   B 1 74  ? 43.430 -13.220 14.580  1.00 15.17 ?  74  PRO   B CG   1 
ATOM   4829 C CD   . PRO   B 1 74  ? 44.081 -11.867 14.472  1.00 14.60 ?  74  PRO   B CD   1 
ATOM   4830 H HA   . PRO   B 1 74  ? 44.675 -13.071 11.663  1.00 15.53 ?  74  PRO   B HA   1 
ATOM   4831 H HB2  . PRO   B 1 74  ? 43.222 -14.634 13.114  1.00 16.63 ?  74  PRO   B HB2  1 
ATOM   4832 H HB3  . PRO   B 1 74  ? 44.748 -14.345 13.488  1.00 16.63 ?  74  PRO   B HB3  1 
ATOM   4833 H HG2  . PRO   B 1 74  ? 42.465 -13.139 14.580  1.00 18.21 ?  74  PRO   B HG2  1 
ATOM   4834 H HG3  . PRO   B 1 74  ? 43.740 -13.688 15.369  1.00 18.21 ?  74  PRO   B HG3  1 
ATOM   4835 H HD2  . PRO   B 1 74  ? 43.515 -11.187 14.878  1.00 17.53 ?  74  PRO   B HD2  1 
ATOM   4836 H HD3  . PRO   B 1 74  ? 44.963 -11.879 14.873  1.00 17.53 ?  74  PRO   B HD3  1 
ATOM   4837 N N    . LEU   B 1 75  ? 42.596 -13.647 10.429  1.00 11.26 ?  75  LEU   B N    1 
ATOM   4838 C CA   . LEU   B 1 75  ? 41.384 -13.872 9.663   1.00 11.45 ?  75  LEU   B CA   1 
ATOM   4839 C C    . LEU   B 1 75  ? 40.418 -14.739 10.469  1.00 11.77 ?  75  LEU   B C    1 
ATOM   4840 O O    . LEU   B 1 75  ? 40.760 -15.279 11.522  1.00 12.83 ?  75  LEU   B O    1 
ATOM   4841 C CB   . LEU   B 1 75  ? 41.716 -14.582 8.349   1.00 11.61 ?  75  LEU   B CB   1 
ATOM   4842 C CG   . LEU   B 1 75  ? 42.575 -13.835 7.321   1.00 13.46 ?  75  LEU   B CG   1 
ATOM   4843 C CD1  . LEU   B 1 75  ? 42.732 -14.664 6.048   1.00 14.70 ?  75  LEU   B CD1  1 
ATOM   4844 C CD2  . LEU   B 1 75  ? 42.023 -12.469 6.996   1.00 16.40 ?  75  LEU   B CD2  1 
ATOM   4845 H H    . LEU   B 1 75  ? 43.275 -14.092 10.135  1.00 13.53 ?  75  LEU   B H    1 
ATOM   4846 H HA   . LEU   B 1 75  ? 40.955 -13.025 9.464   1.00 13.75 ?  75  LEU   B HA   1 
ATOM   4847 H HB2  . LEU   B 1 75  ? 42.183 -15.405 8.564   1.00 13.94 ?  75  LEU   B HB2  1 
ATOM   4848 H HB3  . LEU   B 1 75  ? 40.878 -14.803 7.908   1.00 13.94 ?  75  LEU   B HB3  1 
ATOM   4849 H HG   . LEU   B 1 75  ? 43.461 -13.715 7.692   1.00 16.17 ?  75  LEU   B HG   1 
ATOM   4850 H HD11 . LEU   B 1 75  ? 43.282 -14.173 5.414   1.00 17.65 ?  75  LEU   B HD11 1 
ATOM   4851 H HD12 . LEU   B 1 75  ? 43.159 -15.509 6.266   1.00 17.65 ?  75  LEU   B HD12 1 
ATOM   4852 H HD13 . LEU   B 1 75  ? 41.856 -14.828 5.663   1.00 17.65 ?  75  LEU   B HD13 1 
ATOM   4853 H HD21 . LEU   B 1 75  ? 42.550 -12.076 6.284   1.00 19.69 ?  75  LEU   B HD21 1 
ATOM   4854 H HD22 . LEU   B 1 75  ? 41.100 -12.562 6.714   1.00 19.69 ?  75  LEU   B HD22 1 
ATOM   4855 H HD23 . LEU   B 1 75  ? 42.073 -11.915 7.791   1.00 19.69 ?  75  LEU   B HD23 1 
ATOM   4856 N N    . LYS   B 1 76  ? 39.191 -14.856 9.958   1.00 12.71 ?  76  LYS   B N    1 
ATOM   4857 C CA   . LYS   B 1 76  ? 38.208 -15.823 10.434  1.00 13.95 ?  76  LYS   B CA   1 
ATOM   4858 C C    . LYS   B 1 76  ? 38.287 -17.087 9.579   1.00 12.18 ?  76  LYS   B C    1 
ATOM   4859 O O    . LYS   B 1 76  ? 38.550 -17.014 8.379   1.00 11.91 ?  76  LYS   B O    1 
ATOM   4860 C CB   . LYS   B 1 76  ? 36.786 -15.254 10.276  1.00 17.24 ?  76  LYS   B CB   1 
ATOM   4861 C CG   . LYS   B 1 76  ? 36.521 -13.856 10.858  1.00 19.47 ?  76  LYS   B CG   1 
ATOM   4862 C CD   . LYS   B 1 76  ? 35.108 -13.337 10.519  1.00 21.12 ?  76  LYS   B CD   1 
ATOM   4863 C CE   . LYS   B 1 76  ? 34.836 -11.987 11.164  1.00 22.98 ?  76  LYS   B CE   1 
ATOM   4864 N NZ   . LYS   B 1 76  ? 33.564 -11.372 10.689  1.00 23.71 ?  76  LYS   B NZ   1 
ATOM   4865 H H    . LYS   B 1 76  ? 38.896 -14.367 9.318   1.00 15.26 ?  76  LYS   B H    1 
ATOM   4866 H HA   . LYS   B 1 76  ? 38.365 -16.049 11.366  1.00 16.74 ?  76  LYS   B HA   1 
ATOM   4867 H HB2  . LYS   B 1 76  ? 36.585 -15.210 9.327   1.00 20.70 ?  76  LYS   B HB2  1 
ATOM   4868 H HB3  . LYS   B 1 76  ? 36.166 -15.863 10.705  1.00 20.70 ?  76  LYS   B HB3  1 
ATOM   4869 H HG2  . LYS   B 1 76  ? 36.606 -13.892 11.823  1.00 23.38 ?  76  LYS   B HG2  1 
ATOM   4870 H HG3  . LYS   B 1 76  ? 37.167 -13.231 10.490  1.00 23.38 ?  76  LYS   B HG3  1 
ATOM   4871 H HD2  . LYS   B 1 76  ? 35.025 -13.235 9.557   1.00 25.35 ?  76  LYS   B HD2  1 
ATOM   4872 H HD3  . LYS   B 1 76  ? 34.448 -13.969 10.846  1.00 25.35 ?  76  LYS   B HD3  1 
ATOM   4873 H HE2  . LYS   B 1 76  ? 34.773 -12.103 12.126  1.00 27.58 ?  76  LYS   B HE2  1 
ATOM   4874 H HE3  . LYS   B 1 76  ? 35.562 -11.381 10.950  1.00 27.58 ?  76  LYS   B HE3  1 
ATOM   4875 H HZ1  . LYS   B 1 76  ? 33.438 -10.585 11.088  1.00 28.46 ?  76  LYS   B HZ1  1 
ATOM   4876 H HZ2  . LYS   B 1 76  ? 33.596 -11.247 9.808   1.00 28.46 ?  76  LYS   B HZ2  1 
ATOM   4877 H HZ3  . LYS   B 1 76  ? 32.877 -11.905 10.880  1.00 28.46 ?  76  LYS   B HZ3  1 
ATOM   4878 N N    . VAL   B 1 77  ? 38.027 -18.251 10.190  1.00 12.25 ?  77  VAL   B N    1 
ATOM   4879 C CA   . VAL   B 1 77  ? 37.812 -19.454 9.388   1.00 12.27 ?  77  VAL   B CA   1 
ATOM   4880 C C    . VAL   B 1 77  ? 36.621 -19.212 8.473   1.00 11.17 ?  77  VAL   B C    1 
ATOM   4881 O O    . VAL   B 1 77  ? 35.559 -18.750 8.915   1.00 11.69 ?  77  VAL   B O    1 
ATOM   4882 C CB   . VAL   B 1 77  ? 37.626 -20.696 10.273  1.00 13.17 ?  77  VAL   B CB   1 
ATOM   4883 C CG1  . VAL   B 1 77  ? 37.346 -21.909 9.404   1.00 14.12 ?  77  VAL   B CG1  1 
ATOM   4884 C CG2  . VAL   B 1 77  ? 38.864 -20.935 11.131  1.00 14.74 ?  77  VAL   B CG2  1 
ATOM   4885 H H    . VAL   B 1 77  ? 37.975 -18.362 11.038  1.00 14.71 ?  77  VAL   B H    1 
ATOM   4886 H HA   . VAL   B 1 77  ? 38.588 -19.598 8.827   1.00 14.73 ?  77  VAL   B HA   1 
ATOM   4887 H HB   . VAL   B 1 77  ? 36.867 -20.554 10.864  1.00 15.81 ?  77  VAL   B HB   1 
ATOM   4888 H HG11 . VAL   B 1 77  ? 37.413 -22.706 9.952   1.00 16.95 ?  77  VAL   B HG11 1 
ATOM   4889 H HG12 . VAL   B 1 77  ? 36.448 -21.838 9.038   1.00 16.95 ?  77  VAL   B HG12 1 
ATOM   4890 H HG13 . VAL   B 1 77  ? 37.995 -21.941 8.688   1.00 16.95 ?  77  VAL   B HG13 1 
ATOM   4891 H HG21 . VAL   B 1 77  ? 38.727 -21.737 11.654  1.00 17.70 ?  77  VAL   B HG21 1 
ATOM   4892 H HG22 . VAL   B 1 77  ? 39.630 -21.038 10.550  1.00 17.70 ?  77  VAL   B HG22 1 
ATOM   4893 H HG23 . VAL   B 1 77  ? 38.991 -20.172 11.718  1.00 17.70 ?  77  VAL   B HG23 1 
ATOM   4894 N N    . GLY   B 1 78  ? 36.807 -19.485 7.183   1.00 11.00 ?  78  GLY   B N    1 
ATOM   4895 C CA   . GLY   B 1 78  ? 35.838 -19.158 6.167   1.00 10.72 ?  78  GLY   B CA   1 
ATOM   4896 C C    . GLY   B 1 78  ? 36.082 -17.835 5.477   1.00 10.32 ?  78  GLY   B C    1 
ATOM   4897 O O    . GLY   B 1 78  ? 35.400 -17.539 4.487   1.00 10.99 ?  78  GLY   B O    1 
ATOM   4898 H H    . GLY   B 1 78  ? 37.511 -19.868 6.874   1.00 13.21 ?  78  GLY   B H    1 
ATOM   4899 H HA2  . GLY   B 1 78  ? 35.838 -19.852 5.493   1.00 12.87 ?  78  GLY   B HA2  1 
ATOM   4900 H HA3  . GLY   B 1 78  ? 34.955 -19.122 6.567   1.00 12.87 ?  78  GLY   B HA3  1 
ATOM   4901 N N    . GLY   B 1 79  ? 37.026 -17.032 5.973   1.00 10.55 ?  79  GLY   B N    1 
ATOM   4902 C CA   . GLY   B 1 79  ? 37.326 -15.734 5.409   1.00 10.52 ?  79  GLY   B CA   1 
ATOM   4903 C C    . GLY   B 1 79  ? 38.562 -15.741 4.515   1.00 10.05 ?  79  GLY   B C    1 
ATOM   4904 O O    . GLY   B 1 79  ? 39.178 -16.774 4.255   1.00 10.42 ?  79  GLY   B O    1 
ATOM   4905 H H    . GLY   B 1 79  ? 37.520 -17.229 6.646   1.00 12.67 ?  79  GLY   B H    1 
ATOM   4906 H HA2  . GLY   B 1 79  ? 36.574 -15.426 4.878   1.00 12.63 ?  79  GLY   B HA2  1 
ATOM   4907 H HA3  . GLY   B 1 79  ? 37.476 -15.097 6.124   1.00 12.63 ?  79  GLY   B HA3  1 
ATOM   4908 N N    . SER   B 1 80  ? 38.922 -14.541 4.046   1.00 10.43 ?  80  SER   B N    1 
ATOM   4909 C CA   . SER   B 1 80  ? 40.030 -14.399 3.110   1.00 10.10 ?  80  SER   B CA   1 
ATOM   4910 C C    . SER   B 1 80  ? 40.610 -12.991 3.179   1.00 10.16 ?  80  SER   B C    1 
ATOM   4911 O O    . SER   B 1 80  ? 39.991 -12.062 3.703   1.00 11.40 ?  80  SER   B O    1 
ATOM   4912 C CB   . SER   B 1 80  ? 39.586 -14.677 1.671   1.00 10.73 ?  80  SER   B CB   1 
ATOM   4913 O OG   . SER   B 1 80  ? 38.742 -13.650 1.171   1.00 11.71 ?  80  SER   B OG   1 
ATOM   4914 H H    . SER   B 1 80  ? 38.544 -13.799 4.257   1.00 12.53 ?  80  SER   B H    1 
ATOM   4915 H HA   . SER   B 1 80  ? 40.725 -15.028 3.349   1.00 12.13 ?  80  SER   B HA   1 
ATOM   4916 H HB2  . SER   B 1 80  ? 40.370 -14.741 1.103   1.00 12.89 ?  80  SER   B HB2  1 
ATOM   4917 H HB3  . SER   B 1 80  ? 39.100 -15.520 1.651   1.00 12.89 ?  80  SER   B HB3  1 
ATOM   4918 H HG   . SER   B 1 80  ? 38.056 -13.592 1.652   1.00 14.06 ?  80  SER   B HG   1 
ATOM   4919 N N    . CYS   B 1 81  ? 41.800 -12.840 2.599   1.00 9.89  ?  81  CYS   B N    1 
ATOM   4920 C CA   . CYS   B 1 81  ? 42.339 -11.525 2.291   1.00 10.21 ?  81  CYS   B CA   1 
ATOM   4921 C C    . CYS   B 1 81  ? 43.112 -11.602 0.984   1.00 9.50  ?  81  CYS   B C    1 
ATOM   4922 O O    . CYS   B 1 81  ? 43.630 -12.661 0.611   1.00 10.48 ?  81  CYS   B O    1 
ATOM   4923 C CB   . CYS   B 1 81  ? 43.232 -10.970 3.412   1.00 11.00 ?  81  CYS   B CB   1 
ATOM   4924 S SG   . CYS   B 1 81  ? 44.750 -11.907 3.666   1.00 11.25 ?  81  CYS   B SG   1 
ATOM   4925 H H    . CYS   B 1 81  ? 42.317 -13.491 2.366   1.00 11.88 ?  81  CYS   B H    1 
ATOM   4926 H HA   . CYS   B 1 81  ? 41.603 -10.906 2.161   1.00 12.27 ?  81  CYS   B HA   1 
ATOM   4927 H HB2  . CYS   B 1 81  ? 43.479 -10.060 3.193   1.00 13.21 ?  81  CYS   B HB2  1 
ATOM   4928 H HB3  . CYS   B 1 81  ? 42.729 -10.985 4.241   1.00 13.21 ?  81  CYS   B HB3  1 
ATOM   4929 H HG   . CYS   B 1 81  ? 45.377 -11.409 4.561   1.00 13.51 ?  81  CYS   B HG   1 
ATOM   4930 N N    . VAL   B 1 82  ? 43.210 -10.459 0.309   1.00 9.89  ?  82  VAL   B N    1 
ATOM   4931 C CA   . VAL   B 1 82  ? 43.974 -10.325 -0.928  1.00 10.15 ?  82  VAL   B CA   1 
ATOM   4932 C C    . VAL   B 1 82  ? 45.315 -9.683  -0.606  1.00 10.37 ?  82  VAL   B C    1 
ATOM   4933 O O    . VAL   B 1 82  ? 45.366 -8.566  -0.068  1.00 11.50 ?  82  VAL   B O    1 
ATOM   4934 C CB   . VAL   B 1 82  ? 43.226 -9.480  -1.969  1.00 11.32 ?  82  VAL   B CB   1 
ATOM   4935 C CG1  . VAL   B 1 82  ? 44.085 -9.303  -3.220  1.00 12.52 ?  82  VAL   B CG1  1 
ATOM   4936 C CG2  . VAL   B 1 82  ? 41.880 -10.093 -2.307  1.00 12.03 ?  82  VAL   B CG2  1 
ATOM   4937 H H    . VAL   B 1 82  ? 42.827 -9.726  0.551   1.00 11.88 ?  82  VAL   B H    1 
ATOM   4938 H HA   . VAL   B 1 82  ? 44.133 -11.201 -1.311  1.00 12.19 ?  82  VAL   B HA   1 
ATOM   4939 H HB   . VAL   B 1 82  ? 43.062 -8.596  -1.599  1.00 13.60 ?  82  VAL   B HB   1 
ATOM   4940 H HG11 . VAL   B 1 82  ? 43.524 -8.997  -3.950  1.00 15.03 ?  82  VAL   B HG11 1 
ATOM   4941 H HG12 . VAL   B 1 82  ? 44.776 -8.640  -3.041  1.00 15.03 ?  82  VAL   B HG12 1 
ATOM   4942 H HG13 . VAL   B 1 82  ? 44.491 -10.151 -3.447  1.00 15.03 ?  82  VAL   B HG13 1 
ATOM   4943 H HG21 . VAL   B 1 82  ? 41.445 -9.554  -2.990  1.00 14.45 ?  82  VAL   B HG21 1 
ATOM   4944 H HG22 . VAL   B 1 82  ? 42.016 -10.994 -2.637  1.00 14.45 ?  82  VAL   B HG22 1 
ATOM   4945 H HG23 . VAL   B 1 82  ? 41.331 -10.112 -1.507  1.00 14.45 ?  82  VAL   B HG23 1 
ATOM   4946 N N    . LEU   B 1 83  ? 46.397 -10.367 -0.973  1.00 10.19 ?  83  LEU   B N    1 
ATOM   4947 C CA   . LEU   B 1 83  ? 47.750 -9.848  -0.847  1.00 9.97  ?  83  LEU   B CA   1 
ATOM   4948 C C    . LEU   B 1 83  ? 48.457 -9.971  -2.197  1.00 10.23 ?  83  LEU   B C    1 
ATOM   4949 O O    . LEU   B 1 83  ? 47.859 -10.388 -3.197  1.00 10.24 ?  83  LEU   B O    1 
ATOM   4950 C CB   . LEU   B 1 83  ? 48.501 -10.525 0.308   1.00 10.68 ?  83  LEU   B CB   1 
ATOM   4951 C CG   . LEU   B 1 83  ? 47.979 -10.168 1.705   1.00 11.96 ?  83  LEU   B CG   1 
ATOM   4952 C CD1  . LEU   B 1 83  ? 48.603 -11.038 2.780   1.00 12.44 ?  83  LEU   B CD1  1 
ATOM   4953 C CD2  . LEU   B 1 83  ? 48.197 -8.688  2.036   1.00 13.13 ?  83  LEU   B CD2  1 
ATOM   4954 H H    . LEU   B 1 83  ? 46.366 -11.163 -1.304  1.00 12.24 ?  83  LEU   B H    1 
ATOM   4955 H HA   . LEU   B 1 83  ? 47.694 -8.906  -0.642  1.00 11.97 ?  83  LEU   B HA   1 
ATOM   4956 H HB2  . LEU   B 1 83  ? 48.437 -11.483 0.210   1.00 12.82 ?  83  LEU   B HB2  1 
ATOM   4957 H HB3  . LEU   B 1 83  ? 49.434 -10.253 0.272   1.00 12.82 ?  83  LEU   B HB3  1 
ATOM   4958 H HG   . LEU   B 1 83  ? 47.024 -10.327 1.723   1.00 14.37 ?  83  LEU   B HG   1 
ATOM   4959 H HD11 . LEU   B 1 83  ? 48.237 -10.788 3.645   1.00 14.94 ?  83  LEU   B HD11 1 
ATOM   4960 H HD12 . LEU   B 1 83  ? 48.391 -11.969 2.593   1.00 14.94 ?  83  LEU   B HD12 1 
ATOM   4961 H HD13 . LEU   B 1 83  ? 49.562 -10.911 2.778   1.00 14.94 ?  83  LEU   B HD13 1 
ATOM   4962 H HD21 . LEU   B 1 83  ? 47.985 -8.539  2.971   1.00 15.76 ?  83  LEU   B HD21 1 
ATOM   4963 H HD22 . LEU   B 1 83  ? 49.123 -8.460  1.865   1.00 15.76 ?  83  LEU   B HD22 1 
ATOM   4964 H HD23 . LEU   B 1 83  ? 47.615 -8.151  1.476   1.00 15.76 ?  83  LEU   B HD23 1 
ATOM   4965 N N    . SER   B 1 84  ? 49.734 -9.599  -2.240  1.00 10.99 ?  84  SER   B N    1 
ATOM   4966 C CA   . SER   B 1 84  ? 50.473 -9.696  -3.488  1.00 11.46 ?  84  SER   B CA   1 
ATOM   4967 C C    . SER   B 1 84  ? 50.620 -11.148 -3.930  1.00 10.70 ?  84  SER   B C    1 
ATOM   4968 O O    . SER   B 1 84  ? 50.735 -12.062 -3.117  1.00 10.59 ?  84  SER   B O    1 
ATOM   4969 C CB   . SER   B 1 84  ? 51.868 -9.098  -3.326  1.00 13.42 ?  84  SER   B CB   1 
ATOM   4970 O OG   . SER   B 1 84  ? 52.625 -9.298  -4.503  1.00 15.12 ?  84  SER   B OG   1 
ATOM   4971 H H    . SER   B 1 84  ? 50.185 -9.289  -1.572  1.00 13.20 ?  84  SER   B H    1 
ATOM   4972 H HA   . SER   B 1 84  ? 50.004 -9.209  -4.182  1.00 13.77 ?  84  SER   B HA   1 
ATOM   4973 H HB2  . SER   B 1 84  ? 51.785 -8.143  -3.154  1.00 16.12 ?  84  SER   B HB2  1 
ATOM   4974 H HB3  . SER   B 1 84  ? 52.318 -9.530  -2.587  1.00 16.12 ?  84  SER   B HB3  1 
ATOM   4975 H HG   . SER   B 1 84  ? 53.389 -8.954  -4.418  1.00 18.15 ?  84  SER   B HG   1 
ATOM   4976 N N    . GLY   B 1 85  ? 50.679 -11.347 -5.242  1.00 11.79 ?  85  GLY   B N    1 
ATOM   4977 C CA   . GLY   B 1 85  ? 51.026 -12.630 -5.808  1.00 12.35 ?  85  GLY   B CA   1 
ATOM   4978 C C    . GLY   B 1 85  ? 52.499 -12.834 -6.098  1.00 11.62 ?  85  GLY   B C    1 
ATOM   4979 O O    . GLY   B 1 85  ? 52.868 -13.910 -6.571  1.00 11.84 ?  85  GLY   B O    1 
ATOM   4980 H H    . GLY   B 1 85  ? 50.536 -10.740 -5.828  1.00 14.16 ?  85  GLY   B H    1 
ATOM   4981 H HA2  . GLY   B 1 85  ? 50.748 -13.329 -5.196  1.00 14.82 ?  85  GLY   B HA2  1 
ATOM   4982 H HA3  . GLY   B 1 85  ? 50.550 -12.747 -6.637  1.00 14.82 ?  85  GLY   B HA3  1 
ATOM   4983 N N    . HIS   B 1 86  ? 53.355 -11.847 -5.848  1.00 11.19 ?  86  HIS   B N    1 
ATOM   4984 C CA   . HIS   B 1 86  ? 54.815 -12.025 -5.933  1.00 11.44 ?  86  HIS   B CA   1 
ATOM   4985 C C    . HIS   B 1 86  ? 55.181 -12.526 -7.329  1.00 11.62 ?  86  HIS   B C    1 
ATOM   4986 O O    . HIS   B 1 86  ? 54.799 -11.899 -8.330  1.00 12.23 ?  86  HIS   B O    1 
ATOM   4987 C CB   . HIS   B 1 86  ? 55.289 -12.890 -4.766  1.00 11.35 ?  86  HIS   B CB   1 
ATOM   4988 C CG   . HIS   B 1 86  ? 54.985 -12.292 -3.434  1.00 11.76 ?  86  HIS   B CG   1 
ATOM   4989 N ND1  . HIS   B 1 86  ? 55.804 -11.361 -2.834  1.00 13.15 ?  86  HIS   B ND1  1 
ATOM   4990 C CD2  . HIS   B 1 86  ? 53.919 -12.446 -2.613  1.00 12.09 ?  86  HIS   B CD2  1 
ATOM   4991 C CE1  . HIS   B 1 86  ? 55.259 -10.975 -1.695  1.00 13.19 ?  86  HIS   B CE1  1 
ATOM   4992 N NE2  . HIS   B 1 86  ? 54.116 -11.619 -1.536  1.00 12.52 ?  86  HIS   B NE2  1 
ATOM   4993 H H    . HIS   B 1 86  ? 53.121 -11.053 -5.631  1.00 13.43 ?  86  HIS   B H    1 
ATOM   4994 H HA   . HIS   B 1 86  ? 55.233 -11.157 -5.826  1.00 13.73 ?  86  HIS   B HA   1 
ATOM   4995 H HB2  . HIS   B 1 86  ? 54.855 -13.753 -4.814  1.00 13.63 ?  86  HIS   B HB2  1 
ATOM   4996 H HB3  . HIS   B 1 86  ? 56.254 -13.001 -4.826  1.00 13.63 ?  86  HIS   B HB3  1 
ATOM   4997 H HD2  . HIS   B 1 86  ? 53.188 -13.006 -2.754  1.00 14.51 ?  86  HIS   B HD2  1 
ATOM   4998 H HE1  . HIS   B 1 86  ? 55.630 -10.369 -1.096  1.00 15.83 ?  86  HIS   B HE1  1 
ATOM   4999 H HE2  . HIS   B 1 86  ? 53.590 -11.545 -0.860  1.00 15.03 ?  86  HIS   B HE2  1 
ATOM   5000 N N    . ASN   B 1 87  ? 55.941 -13.611 -7.450  1.00 11.76 ?  87  ASN   B N    1 
ATOM   5001 C CA   . ASN   B 1 87  ? 56.340 -14.175 -8.731  1.00 12.29 ?  87  ASN   B CA   1 
ATOM   5002 C C    . ASN   B 1 87  ? 55.361 -15.223 -9.236  1.00 11.87 ?  87  ASN   B C    1 
ATOM   5003 O O    . ASN   B 1 87  ? 55.676 -15.935 -10.194 1.00 13.62 ?  87  ASN   B O    1 
ATOM   5004 C CB   . ASN   B 1 87  ? 57.739 -14.795 -8.618  1.00 14.17 ?  87  ASN   B CB   1 
ATOM   5005 C CG   . ASN   B 1 87  ? 57.802 -15.920 -7.588  1.00 15.22 ?  87  ASN   B CG   1 
ATOM   5006 O OD1  . ASN   B 1 87  ? 57.163 -15.857 -6.533  1.00 14.27 ?  87  ASN   B OD1  1 
ATOM   5007 N ND2  . ASN   B 1 87  ? 58.553 -16.971 -7.907  1.00 17.22 ?  87  ASN   B ND2  1 
ATOM   5008 H H    . ASN   B 1 87  ? 56.249 -14.058 -6.779  1.00 14.12 ?  87  ASN   B H    1 
ATOM   5009 H HA   . ASN   B 1 87  ? 56.377 -13.464 -9.387  1.00 14.76 ?  87  ASN   B HA   1 
ATOM   5010 H HB2  . ASN   B 1 87  ? 57.989 -15.161 -9.483  1.00 17.02 ?  87  ASN   B HB2  1 
ATOM   5011 H HB3  . ASN   B 1 87  ? 58.366 -14.106 -8.354  1.00 17.02 ?  87  ASN   B HB3  1 
ATOM   5012 H HD21 . ASN   B 1 87  ? 58.618 -17.628 -7.361  1.00 20.68 ?  87  ASN   B HD21 1 
ATOM   5013 H HD22 . ASN   B 1 87  ? 58.976 -16.985 -8.656  1.00 20.68 ?  87  ASN   B HD22 1 
ATOM   5014 N N    . LEU   B 1 88  ? 54.183 -15.324 -8.623  1.00 11.26 ?  88  LEU   B N    1 
ATOM   5015 C CA   . LEU   B 1 88  ? 53.208 -16.358 -8.952  1.00 11.28 ?  88  LEU   B CA   1 
ATOM   5016 C C    . LEU   B 1 88  ? 51.973 -15.841 -9.670  1.00 10.85 ?  88  LEU   B C    1 
ATOM   5017 O O    . LEU   B 1 88  ? 51.367 -16.591 -10.444 1.00 12.65 ?  88  LEU   B O    1 
ATOM   5018 C CB   . LEU   B 1 88  ? 52.736 -17.048 -7.667  1.00 12.19 ?  88  LEU   B CB   1 
ATOM   5019 C CG   . LEU   B 1 88  ? 53.856 -17.686 -6.853  1.00 14.40 ?  88  LEU   B CG   1 
ATOM   5020 C CD1  . LEU   B 1 88  ? 53.351 -18.026 -5.460  1.00 15.97 ?  88  LEU   B CD1  1 
ATOM   5021 C CD2  . LEU   B 1 88  ? 54.373 -18.923 -7.561  1.00 17.46 ?  88  LEU   B CD2  1 
ATOM   5022 H H    . LEU   B 1 88  ? 53.920 -14.799 -7.992  1.00 13.52 ?  88  LEU   B H    1 
ATOM   5023 H HA   . LEU   B 1 88  ? 53.625 -17.025 -9.512  1.00 13.54 ?  88  LEU   B HA   1 
ATOM   5024 H HB2  . LEU   B 1 88  ? 52.296 -16.393 -7.101  1.00 14.64 ?  88  LEU   B HB2  1 
ATOM   5025 H HB3  . LEU   B 1 88  ? 52.108 -17.750 -7.902  1.00 14.64 ?  88  LEU   B HB3  1 
ATOM   5026 H HG   . LEU   B 1 88  ? 54.586 -17.054 -6.763  1.00 17.29 ?  88  LEU   B HG   1 
ATOM   5027 H HD11 . LEU   B 1 88  ? 53.979 -18.631 -5.037  1.00 19.17 ?  88  LEU   B HD11 1 
ATOM   5028 H HD12 . LEU   B 1 88  ? 53.278 -17.208 -4.942  1.00 19.17 ?  88  LEU   B HD12 1 
ATOM   5029 H HD13 . LEU   B 1 88  ? 52.482 -18.448 -5.536  1.00 19.17 ?  88  LEU   B HD13 1 
ATOM   5030 H HD21 . LEU   B 1 88  ? 55.041 -19.347 -7.002  1.00 20.96 ?  88  LEU   B HD21 1 
ATOM   5031 H HD22 . LEU   B 1 88  ? 53.634 -19.530 -7.715  1.00 20.96 ?  88  LEU   B HD22 1 
ATOM   5032 H HD23 . LEU   B 1 88  ? 54.768 -18.659 -8.407  1.00 20.96 ?  88  LEU   B HD23 1 
ATOM   5033 N N    . ALA   B 1 89  ? 51.563 -14.606 -9.403  1.00 10.59 ?  89  ALA   B N    1 
ATOM   5034 C CA   . ALA   B 1 89  ? 50.268 -14.115 -9.849  1.00 10.11 ?  89  ALA   B CA   1 
ATOM   5035 C C    . ALA   B 1 89  ? 50.233 -12.623 -9.576  1.00 10.33 ?  89  ALA   B C    1 
ATOM   5036 O O    . ALA   B 1 89  ? 51.076 -12.095 -8.849  1.00 11.39 ?  89  ALA   B O    1 
ATOM   5037 C CB   . ALA   B 1 89  ? 49.133 -14.799 -9.084  1.00 10.45 ?  89  ALA   B CB   1 
ATOM   5038 H H    . ALA   B 1 89  ? 52.013 -14.029 -8.945  1.00 12.72 ?  89  ALA   B H    1 
ATOM   5039 H HA   . ALA   B 1 89  ? 50.154 -14.275 -10.796 1.00 12.14 ?  89  ALA   B HA   1 
ATOM   5040 H HB1  . ALA   B 1 89  ? 48.282 -14.468 -9.417  1.00 12.55 ?  89  ALA   B HB1  1 
ATOM   5041 H HB2  . ALA   B 1 89  ? 49.189 -15.759 -9.228  1.00 12.55 ?  89  ALA   B HB2  1 
ATOM   5042 H HB3  . ALA   B 1 89  ? 49.220 -14.601 -8.141  1.00 12.55 ?  89  ALA   B HB3  1 
ATOM   5043 N N    . LYS   B 1 90  ? 49.229 -11.941 -10.130 1.00 11.19 ?  90  LYS   B N    1 
ATOM   5044 C CA   . LYS   B 1 90  ? 49.031 -10.553 -9.729  1.00 11.75 ?  90  LYS   B CA   1 
ATOM   5045 C C    . LYS   B 1 90  ? 48.714 -10.477 -8.240  1.00 11.58 ?  90  LYS   B C    1 
ATOM   5046 O O    . LYS   B 1 90  ? 49.341 -9.709  -7.493  1.00 13.29 ?  90  LYS   B O    1 
ATOM   5047 C CB   . LYS   B 1 90  ? 47.948 -9.896  -10.586 1.00 13.11 ?  90  LYS   B CB   1 
ATOM   5048 C CG   . LYS   B 1 90  ? 47.655 -8.450  -10.228 1.00 14.02 ?  90  LYS   B CG   1 
ATOM   5049 C CD   . LYS   B 1 90  ? 48.858 -7.545  -10.355 1.00 16.87 ?  90  LYS   B CD   1 
ATOM   5050 C CE   . LYS   B 1 90  ? 48.438 -6.107  -10.139 1.00 19.10 ?  90  LYS   B CE   1 
ATOM   5051 N NZ   . LYS   B 1 90  ? 49.611 -5.207  -10.023 1.00 19.43 ?  90  LYS   B NZ   1 
ATOM   5052 H H    . LYS   B 1 90  ? 48.668 -12.251 -10.705 1.00 13.44 ?  90  LYS   B H    1 
ATOM   5053 H HA   . LYS   B 1 90  ? 49.857 -10.074 -9.877  1.00 14.10 ?  90  LYS   B HA   1 
ATOM   5054 H HB2  . LYS   B 1 90  ? 48.238 -9.915  -11.515 1.00 15.74 ?  90  LYS   B HB2  1 
ATOM   5055 H HB3  . LYS   B 1 90  ? 47.126 -10.399 -10.493 1.00 15.74 ?  90  LYS   B HB3  1 
ATOM   5056 H HG2  . LYS   B 1 90  ? 46.965 -8.114  -10.821 1.00 16.83 ?  90  LYS   B HG2  1 
ATOM   5057 H HG3  . LYS   B 1 90  ? 47.344 -8.410  -9.308  1.00 16.83 ?  90  LYS   B HG3  1 
ATOM   5058 H HD2  . LYS   B 1 90  ? 49.515 -7.779  -9.680  1.00 20.25 ?  90  LYS   B HD2  1 
ATOM   5059 H HD3  . LYS   B 1 90  ? 49.236 -7.629  -11.243 1.00 20.25 ?  90  LYS   B HD3  1 
ATOM   5060 H HE2  . LYS   B 1 90  ? 47.906 -5.806  -10.895 1.00 22.93 ?  90  LYS   B HE2  1 
ATOM   5061 H HE3  . LYS   B 1 90  ? 47.925 -6.034  -9.320  1.00 22.93 ?  90  LYS   B HE3  1 
ATOM   5062 H HZ1  . LYS   B 1 90  ? 49.347 -4.364  -9.899  1.00 23.33 ?  90  LYS   B HZ1  1 
ATOM   5063 H HZ2  . LYS   B 1 90  ? 50.120 -5.451  -9.334  1.00 23.33 ?  90  LYS   B HZ2  1 
ATOM   5064 H HZ3  . LYS   B 1 90  ? 50.103 -5.243  -10.768 1.00 23.33 ?  90  LYS   B HZ3  1 
ATOM   5065 N N    . HIS   B 1 91  ? 47.764 -11.298 -7.788  1.00 10.14 ?  91  HIS   B N    1 
ATOM   5066 C CA   . HIS   B 1 91  ? 47.311 -11.326 -6.410  1.00 9.96  ?  91  HIS   B CA   1 
ATOM   5067 C C    . HIS   B 1 91  ? 47.318 -12.757 -5.896  1.00 9.48  ?  91  HIS   B C    1 
ATOM   5068 O O    . HIS   B 1 91  ? 47.079 -13.711 -6.649  1.00 10.09 ?  91  HIS   B O    1 
ATOM   5069 C CB   . HIS   B 1 91  ? 45.860 -10.847 -6.285  1.00 11.67 ?  91  HIS   B CB   1 
ATOM   5070 C CG   . HIS   B 1 91  ? 45.632 -9.452  -6.759  1.00 15.40 ?  91  HIS   B CG   1 
ATOM   5071 N ND1  . HIS   B 1 91  ? 46.192 -8.355  -6.141  1.00 17.97 ?  91  HIS   B ND1  1 
ATOM   5072 C CD2  . HIS   B 1 91  ? 44.874 -8.969  -7.768  1.00 17.98 ?  91  HIS   B CD2  1 
ATOM   5073 C CE1  . HIS   B 1 91  ? 45.804 -7.254  -6.762  1.00 18.98 ?  91  HIS   B CE1  1 
ATOM   5074 N NE2  . HIS   B 1 91  ? 44.999 -7.600  -7.751  1.00 19.18 ?  91  HIS   B NE2  1 
ATOM   5075 H H    . HIS   B 1 91  ? 47.354 -11.866 -8.285  1.00 12.18 ?  91  HIS   B H    1 
ATOM   5076 H HA   . HIS   B 1 91  ? 47.887 -10.770 -5.849  1.00 11.96 ?  91  HIS   B HA   1 
ATOM   5077 H HB2  . HIS   B 1 91  ? 45.293 -11.431 -6.806  1.00 14.02 ?  91  HIS   B HB2  1 
ATOM   5078 H HB3  . HIS   B 1 91  ? 45.598 -10.886 -5.347  1.00 14.02 ?  91  HIS   B HB3  1 
ATOM   5079 H HD1  . HIS   B 1 91  ? 46.716 -8.380  -5.454  1.00 21.57 ?  91  HIS   B HD1  1 
ATOM   5080 H HD2  . HIS   B 1 91  ? 44.372 -9.462  -8.369  1.00 21.59 ?  91  HIS   B HD2  1 
ATOM   5081 H HE1  . HIS   B 1 91  ? 46.054 -6.383  -6.534  1.00 22.79 ?  91  HIS   B HE1  1 
ATOM   5082 N N    . CYS   B 1 92  ? 47.511 -12.891 -4.590  1.00 9.41  ?  92  CYS   B N    1 
ATOM   5083 C CA   . CYS   B 1 92  ? 47.226 -14.129 -3.880  1.00 9.03  ?  92  CYS   B CA   1 
ATOM   5084 C C    . CYS   B 1 92  ? 46.008 -13.905 -2.992  1.00 8.78  ?  92  CYS   B C    1 
ATOM   5085 O O    . CYS   B 1 92  ? 46.004 -13.007 -2.139  1.00 9.82  ?  92  CYS   B O    1 
ATOM   5086 C CB   . CYS   B 1 92  ? 48.412 -14.587 -3.035  1.00 9.64  ?  92  CYS   B CB   1 
ATOM   5087 S SG   . CYS   B 1 92  ? 48.057 -16.129 -2.138  1.00 9.88  ?  92  CYS   B SG   1 
ATOM   5088 H H    . CYS   B 1 92  ? 47.819 -12.264 -4.079  1.00 11.31 ?  92  CYS   B H    1 
ATOM   5089 H HA   . CYS   B 1 92  ? 47.025 -14.825 -4.527  1.00 10.84 ?  92  CYS   B HA   1 
ATOM   5090 H HB2  . CYS   B 1 92  ? 49.174 -14.735 -3.610  1.00 11.58 ?  92  CYS   B HB2  1 
ATOM   5091 H HB3  . CYS   B 1 92  ? 48.612 -13.899 -2.380  1.00 11.58 ?  92  CYS   B HB3  1 
ATOM   5092 H HG   . CYS   B 1 92  ? 49.033 -16.441 -1.517  1.00 11.86 ?  92  CYS   B HG   1 
ATOM   5093 N N    . LEU   B 1 93  ? 44.972 -14.716 -3.211  1.00 8.70  ?  93  LEU   B N    1 
ATOM   5094 C CA   . LEU   B 1 93  ? 43.796 -14.734 -2.352  1.00 8.99  ?  93  LEU   B CA   1 
ATOM   5095 C C    . LEU   B 1 93  ? 44.026 -15.806 -1.291  1.00 8.38  ?  93  LEU   B C    1 
ATOM   5096 O O    . LEU   B 1 93  ? 43.981 -17.011 -1.588  1.00 8.80  ?  93  LEU   B O    1 
ATOM   5097 C CB   . LEU   B 1 93  ? 42.534 -15.026 -3.160  1.00 9.27  ?  93  LEU   B CB   1 
ATOM   5098 C CG   . LEU   B 1 93  ? 41.235 -15.058 -2.354  1.00 9.89  ?  93  LEU   B CG   1 
ATOM   5099 C CD1  . LEU   B 1 93  ? 40.879 -13.661 -1.861  1.00 10.10 ?  93  LEU   B CD1  1 
ATOM   5100 C CD2  . LEU   B 1 93  ? 40.116 -15.650 -3.183  1.00 10.09 ?  93  LEU   B CD2  1 
ATOM   5101 H H    . LEU   B 1 93  ? 44.930 -15.288 -3.861  1.00 10.45 ?  93  LEU   B H    1 
ATOM   5102 H HA   . LEU   B 1 93  ? 43.702 -13.875 -1.914  1.00 10.80 ?  93  LEU   B HA   1 
ATOM   5103 H HB2  . LEU   B 1 93  ? 42.441 -14.333 -3.836  1.00 11.13 ?  93  LEU   B HB2  1 
ATOM   5104 H HB3  . LEU   B 1 93  ? 42.633 -15.886 -3.586  1.00 11.13 ?  93  LEU   B HB3  1 
ATOM   5105 H HG   . LEU   B 1 93  ? 41.361 -15.616 -1.574  1.00 11.87 ?  93  LEU   B HG   1 
ATOM   5106 H HD11 . LEU   B 1 93  ? 40.025 -13.693 -1.408  1.00 12.13 ?  93  LEU   B HD11 1 
ATOM   5107 H HD12 . LEU   B 1 93  ? 41.569 -13.352 -1.251  1.00 12.13 ?  93  LEU   B HD12 1 
ATOM   5108 H HD13 . LEU   B 1 93  ? 40.825 -13.061 -2.625  1.00 12.13 ?  93  LEU   B HD13 1 
ATOM   5109 H HD21 . LEU   B 1 93  ? 39.300 -15.657 -2.657  1.00 12.11 ?  93  LEU   B HD21 1 
ATOM   5110 H HD22 . LEU   B 1 93  ? 39.989 -15.112 -3.980  1.00 12.11 ?  93  LEU   B HD22 1 
ATOM   5111 H HD23 . LEU   B 1 93  ? 40.354 -16.557 -3.432  1.00 12.11 ?  93  LEU   B HD23 1 
ATOM   5112 N N    . HIS   B 1 94  ? 44.302 -15.372 -0.065  1.00 8.34  ?  94  HIS   B N    1 
ATOM   5113 C CA   . HIS   B 1 94  ? 44.521 -16.280 1.055   1.00 8.61  ?  94  HIS   B CA   1 
ATOM   5114 C C    . HIS   B 1 94  ? 43.159 -16.641 1.630   1.00 8.86  ?  94  HIS   B C    1 
ATOM   5115 O O    . HIS   B 1 94  ? 42.483 -15.771 2.181   1.00 10.42 ?  94  HIS   B O    1 
ATOM   5116 C CB   . HIS   B 1 94  ? 45.393 -15.603 2.113   1.00 8.85  ?  94  HIS   B CB   1 
ATOM   5117 C CG   . HIS   B 1 94  ? 46.779 -15.302 1.643   1.00 9.04  ?  94  HIS   B CG   1 
ATOM   5118 N ND1  . HIS   B 1 94  ? 47.810 -16.213 1.730   1.00 9.29  ?  94  HIS   B ND1  1 
ATOM   5119 C CD2  . HIS   B 1 94  ? 47.284 -14.192 1.050   1.00 9.42  ?  94  HIS   B CD2  1 
ATOM   5120 C CE1  . HIS   B 1 94  ? 48.900 -15.660 1.223   1.00 9.68  ?  94  HIS   B CE1  1 
ATOM   5121 N NE2  . HIS   B 1 94  ? 48.609 -14.437 0.803   1.00 9.80  ?  94  HIS   B NE2  1 
ATOM   5122 H H    . HIS   B 1 94  ? 44.367 -14.537 0.147   1.00 10.02 ?  94  HIS   B H    1 
ATOM   5123 H HA   . HIS   B 1 94  ? 44.959 -17.086 0.746   1.00 10.34 ?  94  HIS   B HA   1 
ATOM   5124 H HB2  . HIS   B 1 94  ? 44.978 -14.767 2.370   1.00 10.63 ?  94  HIS   B HB2  1 
ATOM   5125 H HB3  . HIS   B 1 94  ? 45.461 -16.191 2.880   1.00 10.63 ?  94  HIS   B HB3  1 
ATOM   5126 H HD2  . HIS   B 1 94  ? 46.825 -13.412 0.849   1.00 11.31 ?  94  HIS   B HD2  1 
ATOM   5127 H HE1  . HIS   B 1 94  ? 49.736 -16.072 1.167   1.00 11.62 ?  94  HIS   B HE1  1 
ATOM   5128 H HE2  . HIS   B 1 94  ? 49.165 -13.895 0.434   1.00 11.77 ?  94  HIS   B HE2  1 
ATOM   5129 N N    . VAL   B 1 95  ? 42.734 -17.897 1.477   1.00 8.66  ?  95  VAL   B N    1 
ATOM   5130 C CA   . VAL   B 1 95  ? 41.410 -18.344 1.913   1.00 8.91  ?  95  VAL   B CA   1 
ATOM   5131 C C    . VAL   B 1 95  ? 41.581 -19.385 3.008   1.00 9.24  ?  95  VAL   B C    1 
ATOM   5132 O O    . VAL   B 1 95  ? 42.350 -20.338 2.845   1.00 9.41  ?  95  VAL   B O    1 
ATOM   5133 C CB   . VAL   B 1 95  ? 40.591 -18.942 0.754   1.00 9.19  ?  95  VAL   B CB   1 
ATOM   5134 C CG1  . VAL   B 1 95  ? 39.213 -19.383 1.238   1.00 10.23 ?  95  VAL   B CG1  1 
ATOM   5135 C CG2  . VAL   B 1 95  ? 40.474 -17.959 -0.387  1.00 9.51  ?  95  VAL   B CG2  1 
ATOM   5136 H H    . VAL   B 1 95  ? 43.195 -18.520 1.107   1.00 10.40 ?  95  VAL   B H    1 
ATOM   5137 H HA   . VAL   B 1 95  ? 40.913 -17.595 2.280   1.00 10.70 ?  95  VAL   B HA   1 
ATOM   5138 H HB   . VAL   B 1 95  ? 41.045 -19.725 0.419   1.00 11.04 ?  95  VAL   B HB   1 
ATOM   5139 H HG11 . VAL   B 1 95  ? 38.651 -19.578 0.466   1.00 12.28 ?  95  VAL   B HG11 1 
ATOM   5140 H HG12 . VAL   B 1 95  ? 39.304 -20.184 1.780   1.00 12.28 ?  95  VAL   B HG12 1 
ATOM   5141 H HG13 . VAL   B 1 95  ? 38.812 -18.672 1.761   1.00 12.28 ?  95  VAL   B HG13 1 
ATOM   5142 H HG21 . VAL   B 1 95  ? 39.896 -18.335 -1.069  1.00 11.42 ?  95  VAL   B HG21 1 
ATOM   5143 H HG22 . VAL   B 1 95  ? 40.096 -17.131 -0.051  1.00 11.42 ?  95  VAL   B HG22 1 
ATOM   5144 H HG23 . VAL   B 1 95  ? 41.357 -17.798 -0.750  1.00 11.42 ?  95  VAL   B HG23 1 
ATOM   5145 N N    . VAL   B 1 96  ? 40.843 -19.224 4.103   1.00 9.59  ?  96  VAL   B N    1 
ATOM   5146 C CA   . VAL   B 1 96  ? 40.923 -20.143 5.238   1.00 9.79  ?  96  VAL   B CA   1 
ATOM   5147 C C    . VAL   B 1 96  ? 39.736 -21.102 5.189   1.00 9.85  ?  96  VAL   B C    1 
ATOM   5148 O O    . VAL   B 1 96  ? 38.615 -20.748 5.565   1.00 10.67 ?  96  VAL   B O    1 
ATOM   5149 C CB   . VAL   B 1 96  ? 40.974 -19.397 6.573   1.00 10.64 ?  96  VAL   B CB   1 
ATOM   5150 C CG1  . VAL   B 1 96  ? 41.153 -20.388 7.713   1.00 11.23 ?  96  VAL   B CG1  1 
ATOM   5151 C CG2  . VAL   B 1 96  ? 42.096 -18.368 6.581   1.00 11.36 ?  96  VAL   B CG2  1 
ATOM   5152 H H    . VAL   B 1 96  ? 40.277 -18.588 4.215   1.00 11.51 ?  96  VAL   B H    1 
ATOM   5153 H HA   . VAL   B 1 96  ? 41.738 -20.668 5.163   1.00 11.76 ?  96  VAL   B HA   1 
ATOM   5154 H HB   . VAL   B 1 96  ? 40.134 -18.930 6.710   1.00 12.78 ?  96  VAL   B HB   1 
ATOM   5155 H HG11 . VAL   B 1 96  ? 41.339 -19.895 8.532   1.00 13.49 ?  96  VAL   B HG11 1 
ATOM   5156 H HG12 . VAL   B 1 96  ? 40.340 -20.903 7.821   1.00 13.49 ?  96  VAL   B HG12 1 
ATOM   5157 H HG13 . VAL   B 1 96  ? 41.897 -20.974 7.510   1.00 13.49 ?  96  VAL   B HG13 1 
ATOM   5158 H HG21 . VAL   B 1 96  ? 42.150 -17.958 7.461   1.00 13.64 ?  96  VAL   B HG21 1 
ATOM   5159 H HG22 . VAL   B 1 96  ? 42.935 -18.807 6.371   1.00 13.64 ?  96  VAL   B HG22 1 
ATOM   5160 H HG23 . VAL   B 1 96  ? 41.907 -17.684 5.915   1.00 13.64 ?  96  VAL   B HG23 1 
ATOM   5161 N N    . GLY   B 1 97  ? 39.977 -22.336 4.757   1.00 10.17 ?  97  GLY   B N    1 
ATOM   5162 C CA   . GLY   B 1 97  ? 39.003 -23.393 4.919   1.00 10.51 ?  97  GLY   B CA   1 
ATOM   5163 C C    . GLY   B 1 97  ? 39.112 -24.003 6.300   1.00 11.02 ?  97  GLY   B C    1 
ATOM   5164 O O    . GLY   B 1 97  ? 40.149 -23.884 6.963   1.00 11.46 ?  97  GLY   B O    1 
ATOM   5165 H H    . GLY   B 1 97  ? 40.709 -22.581 4.365   1.00 12.21 ?  97  GLY   B H    1 
ATOM   5166 H HA2  . GLY   B 1 97  ? 38.112 -23.025 4.795   1.00 12.62 ?  97  GLY   B HA2  1 
ATOM   5167 H HA3  . GLY   B 1 97  ? 39.151 -24.079 4.249   1.00 12.62 ?  97  GLY   B HA3  1 
ATOM   5168 N N    . PRO   B 1 98  ? 38.061 -24.688 6.756   1.00 11.46 ?  98  PRO   B N    1 
ATOM   5169 C CA   . PRO   B 1 98  ? 38.148 -25.387 8.041   1.00 12.38 ?  98  PRO   B CA   1 
ATOM   5170 C C    . PRO   B 1 98  ? 39.175 -26.506 8.000   1.00 12.11 ?  98  PRO   B C    1 
ATOM   5171 O O    . PRO   B 1 98  ? 39.287 -27.239 7.016   1.00 12.17 ?  98  PRO   B O    1 
ATOM   5172 C CB   . PRO   B 1 98  ? 36.732 -25.938 8.240   1.00 12.54 ?  98  PRO   B CB   1 
ATOM   5173 C CG   . PRO   B 1 98  ? 36.180 -26.063 6.860   1.00 11.88 ?  98  PRO   B CG   1 
ATOM   5174 C CD   . PRO   B 1 98  ? 36.749 -24.881 6.113   1.00 11.27 ?  98  PRO   B CD   1 
ATOM   5175 H HA   . PRO   B 1 98  ? 38.365 -24.766 8.749   1.00 14.86 ?  98  PRO   B HA   1 
ATOM   5176 H HB2  . PRO   B 1 98  ? 36.778 -26.808 8.668   1.00 15.06 ?  98  PRO   B HB2  1 
ATOM   5177 H HB3  . PRO   B 1 98  ? 36.210 -25.318 8.763   1.00 15.06 ?  98  PRO   B HB3  1 
ATOM   5178 H HG2  . PRO   B 1 98  ? 36.477 -26.898 6.463   1.00 14.27 ?  98  PRO   B HG2  1 
ATOM   5179 H HG3  . PRO   B 1 98  ? 35.215 -26.018 6.891   1.00 14.27 ?  98  PRO   B HG3  1 
ATOM   5180 H HD2  . PRO   B 1 98  ? 36.856 -25.096 5.168   1.00 13.53 ?  98  PRO   B HD2  1 
ATOM   5181 H HD3  . PRO   B 1 98  ? 36.197 -24.096 6.237   1.00 13.53 ?  98  PRO   B HD3  1 
ATOM   5182 N N    A ASN   B 1 99  ? 39.923 -26.631 9.088   0.86 12.68 ?  99  ASN   B N    1 
ATOM   5183 N N    B ASN   B 1 99  ? 39.915 -26.638 9.098   0.14 13.56 ?  99  ASN   B N    1 
ATOM   5184 C CA   A ASN   B 1 99  ? 40.900 -27.699 9.252   0.86 12.92 ?  99  ASN   B CA   1 
ATOM   5185 C CA   B ASN   B 1 99  ? 40.897 -27.705 9.272   0.14 14.98 ?  99  ASN   B CA   1 
ATOM   5186 C C    A ASN   B 1 99  ? 40.269 -28.779 10.128  0.86 13.99 ?  99  ASN   B C    1 
ATOM   5187 C C    B ASN   B 1 99  ? 40.243 -28.804 10.103  0.14 16.25 ?  99  ASN   B C    1 
ATOM   5188 O O    A ASN   B 1 99  ? 40.169 -28.625 11.347  0.86 15.05 ?  99  ASN   B O    1 
ATOM   5189 O O    B ASN   B 1 99  ? 40.108 -28.680 11.323  0.14 16.37 ?  99  ASN   B O    1 
ATOM   5190 C CB   A ASN   B 1 99  ? 42.176 -27.141 9.865   0.86 13.57 ?  99  ASN   B CB   1 
ATOM   5191 C CB   B ASN   B 1 99  ? 42.152 -27.164 9.947   0.14 15.28 ?  99  ASN   B CB   1 
ATOM   5192 C CG   A ASN   B 1 99  ? 43.297 -28.158 9.887   0.86 14.69 ?  99  ASN   B CG   1 
ATOM   5193 C CG   B ASN   B 1 99  ? 43.301 -28.152 9.922   0.14 15.55 ?  99  ASN   B CG   1 
ATOM   5194 O OD1  A ASN   B 1 99  ? 43.055 -29.350 10.054  0.86 15.81 ?  99  ASN   B OD1  1 
ATOM   5195 O OD1  B ASN   B 1 99  ? 43.099 -29.358 10.058  0.14 15.76 ?  99  ASN   B OD1  1 
ATOM   5196 N ND2  A ASN   B 1 99  ? 44.528 -27.693 9.704   0.86 15.52 ?  99  ASN   B ND2  1 
ATOM   5197 N ND2  B ASN   B 1 99  ? 44.515 -27.644 9.740   0.14 15.72 ?  99  ASN   B ND2  1 
ATOM   5198 H H    A ASN   B 1 99  ? 39.883 -26.093 9.761   0.86 15.22 ?  99  ASN   B H    1 
ATOM   5199 H H    B ASN   B 1 99  ? 39.865 -26.104 9.772   0.14 16.28 ?  99  ASN   B H    1 
ATOM   5200 H HA   A ASN   B 1 99  ? 41.112 -28.085 8.390   0.86 15.51 ?  99  ASN   B HA   1 
ATOM   5201 H HA   B ASN   B 1 99  ? 41.139 -28.072 8.409   0.14 17.99 ?  99  ASN   B HA   1 
ATOM   5202 H HB2  A ASN   B 1 99  ? 42.470 -26.377 9.350   0.86 16.30 ?  99  ASN   B HB2  1 
ATOM   5203 H HB2  B ASN   B 1 99  ? 42.436 -26.359 9.488   0.14 18.34 ?  99  ASN   B HB2  1 
ATOM   5204 H HB3  A ASN   B 1 99  ? 41.995 -26.873 10.783  0.86 16.30 ?  99  ASN   B HB3  1 
ATOM   5205 H HB3  B ASN   B 1 99  ? 41.949 -26.962 10.875  0.14 18.34 ?  99  ASN   B HB3  1 
ATOM   5206 H HD21 A ASN   B 1 99  ? 45.199 -28.228 9.709   0.86 18.63 ?  99  ASN   B HD21 1 
ATOM   5207 H HD21 B ASN   B 1 99  ? 45.201 -28.162 9.717   0.14 18.88 ?  99  ASN   B HD21 1 
ATOM   5208 H HD22 A ASN   B 1 99  ? 44.654 -26.848 9.587   0.86 18.63 ?  99  ASN   B HD22 1 
ATOM   5209 H HD22 B ASN   B 1 99  ? 44.615 -26.794 9.646   0.14 18.88 ?  99  ASN   B HD22 1 
ATOM   5210 N N    A VAL   B 1 100 ? 39.812 -29.861 9.491   0.86 15.84 ?  100 VAL   B N    1 
ATOM   5211 N N    B VAL   B 1 100 ? 39.830 -29.883 9.434   0.14 17.64 ?  100 VAL   B N    1 
ATOM   5212 C CA   A VAL   B 1 100 ? 39.194 -30.965 10.225  0.86 18.92 ?  100 VAL   B CA   1 
ATOM   5213 C CA   B VAL   B 1 100 ? 39.182 -30.990 10.133  0.14 19.18 ?  100 VAL   B CA   1 
ATOM   5214 C C    A VAL   B 1 100 ? 40.191 -31.631 11.165  0.86 19.79 ?  100 VAL   B C    1 
ATOM   5215 C C    B VAL   B 1 100 ? 40.145 -31.665 11.101  0.14 20.12 ?  100 VAL   B C    1 
ATOM   5216 O O    A VAL   B 1 100 ? 39.806 -32.152 12.220  0.86 20.40 ?  100 VAL   B O    1 
ATOM   5217 O O    B VAL   B 1 100 ? 39.730 -32.168 12.152  0.14 20.22 ?  100 VAL   B O    1 
ATOM   5218 C CB   A VAL   B 1 100 ? 38.567 -31.974 9.242   0.86 22.10 ?  100 VAL   B CB   1 
ATOM   5219 C CB   B VAL   B 1 100 ? 38.573 -31.980 9.120   0.14 19.93 ?  100 VAL   B CB   1 
ATOM   5220 C CG1  A VAL   B 1 100 ? 38.100 -33.223 9.979   0.86 23.12 ?  100 VAL   B CG1  1 
ATOM   5221 C CG1  B VAL   B 1 100 ? 38.041 -33.218 9.828   0.14 20.25 ?  100 VAL   B CG1  1 
ATOM   5222 C CG2  A VAL   B 1 100 ? 37.410 -31.333 8.494   0.86 22.93 ?  100 VAL   B CG2  1 
ATOM   5223 C CG2  B VAL   B 1 100 ? 37.464 -31.304 8.327   0.14 20.13 ?  100 VAL   B CG2  1 
ATOM   5224 H H    A VAL   B 1 100 ? 39.835 -29.969 8.639   0.86 19.02 ?  100 VAL   B H    1 
ATOM   5225 H H    B VAL   B 1 100 ? 39.907 -29.992 8.586   0.14 21.18 ?  100 VAL   B H    1 
ATOM   5226 H HA   A VAL   B 1 100 ? 38.475 -30.609 10.770  0.86 22.71 ?  100 VAL   B HA   1 
ATOM   5227 H HA   B VAL   B 1 100 ? 38.450 -30.633 10.656  0.14 23.03 ?  100 VAL   B HA   1 
ATOM   5228 H HB   A VAL   B 1 100 ? 39.236 -32.246 8.595   0.86 26.53 ?  100 VAL   B HB   1 
ATOM   5229 H HB   B VAL   B 1 100 ? 39.261 -32.262 8.497   0.14 23.93 ?  100 VAL   B HB   1 
ATOM   5230 H HG11 A VAL   B 1 100 ? 37.507 -33.729 9.400   0.86 27.75 ?  100 VAL   B HG11 1 
ATOM   5231 H HG11 B VAL   B 1 100 ? 37.477 -33.713 9.213   0.14 24.31 ?  100 VAL   B HG11 1 
ATOM   5232 H HG12 A VAL   B 1 100 ? 38.869 -33.767 10.214  0.86 27.75 ?  100 VAL   B HG12 1 
ATOM   5233 H HG12 B VAL   B 1 100 ? 38.787 -33.771 10.107  0.14 24.31 ?  100 VAL   B HG12 1 
ATOM   5234 H HG13 A VAL   B 1 100 ? 37.625 -32.959 10.784  0.86 27.75 ?  100 VAL   B HG13 1 
ATOM   5235 H HG13 B VAL   B 1 100 ? 37.523 -32.942 10.600  0.14 24.31 ?  100 VAL   B HG13 1 
ATOM   5236 H HG21 A VAL   B 1 100 ? 37.028 -31.987 7.886   0.86 27.52 ?  100 VAL   B HG21 1 
ATOM   5237 H HG21 B VAL   B 1 100 ? 37.081 -31.946 7.709   0.14 24.17 ?  100 VAL   B HG21 1 
ATOM   5238 H HG22 A VAL   B 1 100 ? 36.739 -31.050 9.137   0.86 27.52 ?  100 VAL   B HG22 1 
ATOM   5239 H HG22 B VAL   B 1 100 ? 36.781 -30.992 8.943   0.14 24.17 ?  100 VAL   B HG22 1 
ATOM   5240 H HG23 A VAL   B 1 100 ? 37.739 -30.571 7.999   0.86 27.52 ?  100 VAL   B HG23 1 
ATOM   5241 H HG23 B VAL   B 1 100 ? 37.836 -30.554 7.839   0.14 24.17 ?  100 VAL   B HG23 1 
ATOM   5242 N N    A ASN   B 1 101 ? 41.476 -31.654 10.796  0.86 20.54 ?  101 ASN   B N    1 
ATOM   5243 N N    B ASN   B 1 101 ? 41.439 -31.696 10.769  0.14 21.07 ?  101 ASN   B N    1 
ATOM   5244 C CA   A ASN   B 1 101 ? 42.500 -32.198 11.687  0.86 22.56 ?  101 ASN   B CA   1 
ATOM   5245 C CA   B ASN   B 1 101 ? 42.434 -32.235 11.691  0.14 22.25 ?  101 ASN   B CA   1 
ATOM   5246 C C    A ASN   B 1 101 ? 42.672 -31.365 12.951  0.86 23.74 ?  101 ASN   B C    1 
ATOM   5247 C C    B ASN   B 1 101 ? 42.562 -31.401 12.960  0.14 23.34 ?  101 ASN   B C    1 
ATOM   5248 O O    A ASN   B 1 101 ? 43.258 -31.853 13.925  0.86 25.09 ?  101 ASN   B O    1 
ATOM   5249 O O    B ASN   B 1 101 ? 43.127 -31.885 13.947  0.14 23.53 ?  101 ASN   B O    1 
ATOM   5250 C CB   A ASN   B 1 101 ? 43.835 -32.335 10.945  0.86 22.99 ?  101 ASN   B CB   1 
ATOM   5251 C CB   B ASN   B 1 101 ? 43.790 -32.371 10.993  0.14 22.30 ?  101 ASN   B CB   1 
ATOM   5252 C CG   A ASN   B 1 101 ? 43.816 -33.450 9.914   0.86 22.92 ?  101 ASN   B CG   1 
ATOM   5253 C CG   B ASN   B 1 101 ? 43.787 -33.446 9.922   0.14 22.32 ?  101 ASN   B CG   1 
ATOM   5254 O OD1  A ASN   B 1 101 ? 43.142 -34.461 10.095  0.86 24.08 ?  101 ASN   B OD1  1 
ATOM   5255 O OD1  B ASN   B 1 101 ? 43.102 -34.461 10.048  0.14 22.50 ?  101 ASN   B OD1  1 
ATOM   5256 N ND2  A ASN   B 1 101 ? 44.553 -33.267 8.826   0.86 22.79 ?  101 ASN   B ND2  1 
ATOM   5257 N ND2  B ASN   B 1 101 ? 44.552 -33.227 8.859   0.14 22.20 ?  101 ASN   B ND2  1 
ATOM   5258 H H    A ASN   B 1 101 ? 41.773 -31.380 10.036  0.86 24.66 ?  101 ASN   B H    1 
ATOM   5259 H H    B ASN   B 1 101 ? 41.759 -31.427 10.019  0.14 25.29 ?  101 ASN   B H    1 
ATOM   5260 H HA   A ASN   B 1 101 ? 42.232 -33.080 11.968  0.86 27.08 ?  101 ASN   B HA   1 
ATOM   5261 H HA   B ASN   B 1 101 ? 42.159 -33.122 11.962  0.14 26.71 ?  101 ASN   B HA   1 
ATOM   5262 H HB2  A ASN   B 1 101 ? 44.037 -31.506 10.482  0.86 27.59 ?  101 ASN   B HB2  1 
ATOM   5263 H HB2  B ASN   B 1 101 ? 44.021 -31.530 10.569  0.14 26.77 ?  101 ASN   B HB2  1 
ATOM   5264 H HB3  A ASN   B 1 101 ? 44.538 -32.532 11.586  0.86 27.59 ?  101 ASN   B HB3  1 
ATOM   5265 H HB3  B ASN   B 1 101 ? 44.466 -32.606 11.649  0.14 26.77 ?  101 ASN   B HB3  1 
ATOM   5266 H HD21 A ASN   B 1 101 ? 44.574 -33.873 8.214   0.86 27.36 ?  101 ASN   B HD21 1 
ATOM   5267 H HD21 B ASN   B 1 101 ? 44.583 -33.808 8.225   0.14 26.65 ?  101 ASN   B HD21 1 
ATOM   5268 H HD22 A ASN   B 1 101 ? 45.010 -32.545 8.729   0.86 27.36 ?  101 ASN   B HD22 1 
ATOM   5269 H HD22 B ASN   B 1 101 ? 45.016 -32.506 8.804   0.14 26.65 ?  101 ASN   B HD22 1 
ATOM   5270 N N    A LYS   B 1 102 ? 42.180 -30.124 12.950  0.86 24.88 ?  102 LYS   B N    1 
ATOM   5271 N N    B LYS   B 1 102 ? 42.054 -30.170 12.959  0.14 24.27 ?  102 LYS   B N    1 
ATOM   5272 C CA   A LYS   B 1 102 ? 42.171 -29.266 14.128  0.86 27.01 ?  102 LYS   B CA   1 
ATOM   5273 C CA   B LYS   B 1 102 ? 42.002 -29.338 14.154  0.14 25.26 ?  102 LYS   B CA   1 
ATOM   5274 C C    A LYS   B 1 102 ? 40.800 -29.207 14.790  0.86 26.66 ?  102 LYS   B C    1 
ATOM   5275 C C    B LYS   B 1 102 ? 40.627 -29.334 14.808  0.14 24.95 ?  102 LYS   B C    1 
ATOM   5276 O O    A LYS   B 1 102 ? 40.600 -28.404 15.707  0.86 27.35 ?  102 LYS   B O    1 
ATOM   5277 O O    B LYS   B 1 102 ? 40.424 -28.609 15.786  0.14 25.00 ?  102 LYS   B O    1 
ATOM   5278 C CB   A LYS   B 1 102 ? 42.603 -27.842 13.761  0.86 29.96 ?  102 LYS   B CB   1 
ATOM   5279 C CB   B LYS   B 1 102 ? 42.407 -27.897 13.822  0.14 26.57 ?  102 LYS   B CB   1 
ATOM   5280 C CG   A LYS   B 1 102 ? 44.072 -27.662 13.408  0.86 32.67 ?  102 LYS   B CG   1 
ATOM   5281 C CG   B LYS   B 1 102 ? 43.864 -27.714 13.430  0.14 27.76 ?  102 LYS   B CG   1 
ATOM   5282 C CD   A LYS   B 1 102 ? 44.341 -26.208 13.032  0.86 35.04 ?  102 LYS   B CD   1 
ATOM   5283 C CD   B LYS   B 1 102 ? 44.129 -26.270 13.028  0.14 28.79 ?  102 LYS   B CD   1 
ATOM   5284 C CE   A LYS   B 1 102 ? 45.810 -25.938 12.749  0.86 36.93 ?  102 LYS   B CE   1 
ATOM   5285 C CE   B LYS   B 1 102 ? 45.593 -26.030 12.701  0.14 29.59 ?  102 LYS   B CE   1 
ATOM   5286 N NZ   A LYS   B 1 102 ? 46.033 -24.514 12.355  0.86 38.05 ?  102 LYS   B NZ   1 
ATOM   5287 N NZ   B LYS   B 1 102 ? 45.823 -24.633 12.234  0.14 30.03 ?  102 LYS   B NZ   1 
ATOM   5288 H H    A LYS   B 1 102 ? 41.827 -29.745 12.255  0.86 29.86 ?  102 LYS   B H    1 
ATOM   5289 H H    B LYS   B 1 102 ? 41.726 -29.788 12.263  0.14 29.13 ?  102 LYS   B H    1 
ATOM   5290 H HA   A LYS   B 1 102 ? 42.813 -29.611 14.767  0.86 32.42 ?  102 LYS   B HA   1 
ATOM   5291 H HA   B LYS   B 1 102 ? 42.634 -29.678 14.803  0.14 30.32 ?  102 LYS   B HA   1 
ATOM   5292 H HB2  A LYS   B 1 102 ? 42.085 -27.549 12.997  0.86 35.96 ?  102 LYS   B HB2  1 
ATOM   5293 H HB2  B LYS   B 1 102 ? 41.865 -27.584 13.082  0.14 31.89 ?  102 LYS   B HB2  1 
ATOM   5294 H HB3  A LYS   B 1 102 ? 42.417 -27.261 14.518  0.86 35.96 ?  102 LYS   B HB3  1 
ATOM   5295 H HB3  B LYS   B 1 102 ? 42.245 -27.343 14.602  0.14 31.89 ?  102 LYS   B HB3  1 
ATOM   5296 H HG2  A LYS   B 1 102 ? 44.624 -27.887 14.174  0.86 39.22 ?  102 LYS   B HG2  1 
ATOM   5297 H HG2  B LYS   B 1 102 ? 44.433 -27.932 14.185  0.14 33.32 ?  102 LYS   B HG2  1 
ATOM   5298 H HG3  A LYS   B 1 102 ? 44.297 -28.222 12.649  0.86 39.22 ?  102 LYS   B HG3  1 
ATOM   5299 H HG3  B LYS   B 1 102 ? 44.071 -28.286 12.674  0.14 33.32 ?  102 LYS   B HG3  1 
ATOM   5300 H HD2  A LYS   B 1 102 ? 43.836 -25.988 12.233  0.86 42.06 ?  102 LYS   B HD2  1 
ATOM   5301 H HD2  B LYS   B 1 102 ? 43.604 -26.057 12.240  0.14 34.56 ?  102 LYS   B HD2  1 
ATOM   5302 H HD3  A LYS   B 1 102 ? 44.066 -25.634 13.765  0.86 42.06 ?  102 LYS   B HD3  1 
ATOM   5303 H HD3  B LYS   B 1 102 ? 43.883 -25.685 13.762  0.14 34.56 ?  102 LYS   B HD3  1 
ATOM   5304 H HE2  A LYS   B 1 102 ? 46.330 -26.117 13.548  0.86 44.32 ?  102 LYS   B HE2  1 
ATOM   5305 H HE2  B LYS   B 1 102 ? 46.128 -26.177 13.497  0.14 35.51 ?  102 LYS   B HE2  1 
ATOM   5306 H HE3  A LYS   B 1 102 ? 46.107 -26.505 12.020  0.86 44.32 ?  102 LYS   B HE3  1 
ATOM   5307 H HE3  B LYS   B 1 102 ? 45.867 -26.636 11.995  0.14 35.51 ?  102 LYS   B HE3  1 
ATOM   5308 H HZ1  A LYS   B 1 102 ? 46.897 -24.374 12.193  0.86 45.67 ?  102 LYS   B HZ1  1 
ATOM   5309 H HZ1  B LYS   B 1 102 ? 46.685 -24.513 12.048  0.14 36.05 ?  102 LYS   B HZ1  1 
ATOM   5310 H HZ2  A LYS   B 1 102 ? 45.567 -24.325 11.620  0.86 45.67 ?  102 LYS   B HZ2  1 
ATOM   5311 H HZ2  B LYS   B 1 102 ? 45.344 -24.475 11.501  0.14 36.05 ?  102 LYS   B HZ2  1 
ATOM   5312 H HZ3  A LYS   B 1 102 ? 45.770 -23.972 13.011  0.86 45.67 ?  102 LYS   B HZ3  1 
ATOM   5313 H HZ3  B LYS   B 1 102 ? 45.581 -24.057 12.868  0.14 36.05 ?  102 LYS   B HZ3  1 
ATOM   5314 N N    A GLY   B 1 103 ? 39.846 -30.014 14.332  0.86 25.58 ?  103 GLY   B N    1 
ATOM   5315 N N    B GLY   B 1 103 ? 39.681 -30.118 14.296  0.14 24.58 ?  103 GLY   B N    1 
ATOM   5316 C CA   A GLY   B 1 103 ? 38.524 -30.044 14.927  0.86 25.51 ?  103 GLY   B CA   1 
ATOM   5317 C CA   B GLY   B 1 103 ? 38.351 -30.153 14.865  0.14 24.25 ?  103 GLY   B CA   1 
ATOM   5318 C C    A GLY   B 1 103 ? 37.563 -28.991 14.420  0.86 24.54 ?  103 GLY   B C    1 
ATOM   5319 C C    B GLY   B 1 103 ? 37.439 -29.031 14.427  0.14 23.79 ?  103 GLY   B C    1 
ATOM   5320 O O    A GLY   B 1 103 ? 36.459 -28.868 14.966  0.86 25.50 ?  103 GLY   B O    1 
ATOM   5321 O O    B GLY   B 1 103 ? 36.396 -28.820 15.057  0.14 23.94 ?  103 GLY   B O    1 
ATOM   5322 H H    A GLY   B 1 103 ? 39.947 -30.553 13.670  0.86 30.70 ?  103 GLY   B H    1 
ATOM   5323 H H    B GLY   B 1 103 ? 39.790 -30.638 13.616  0.14 29.51 ?  103 GLY   B H    1 
ATOM   5324 H HA2  A GLY   B 1 103 ? 38.131 -30.913 14.760  0.86 30.62 ?  103 GLY   B HA2  1 
ATOM   5325 H HA2  B GLY   B 1 103 ? 37.927 -30.989 14.626  0.14 29.11 ?  103 GLY   B HA2  1 
ATOM   5326 H HA3  A GLY   B 1 103 ? 38.617 -29.941 15.890  0.86 30.62 ?  103 GLY   B HA3  1 
ATOM   5327 H HA3  B GLY   B 1 103 ? 38.424 -30.117 15.833  0.14 29.11 ?  103 GLY   B HA3  1 
ATOM   5328 N N    A GLU   B 1 104 ? 37.937 -28.234 13.393  0.86 22.84 ?  104 GLU   B N    1 
ATOM   5329 N N    B GLU   B 1 104 ? 37.792 -28.308 13.369  0.14 23.11 ?  104 GLU   B N    1 
ATOM   5330 C CA   A GLU   B 1 104 ? 37.099 -27.143 12.922  0.86 21.09 ?  104 GLU   B CA   1 
ATOM   5331 C CA   B GLU   B 1 104 ? 36.982 -27.191 12.912  0.14 22.46 ?  104 GLU   B CA   1 
ATOM   5332 C C    A GLU   B 1 104 ? 35.927 -27.676 12.098  0.86 21.71 ?  104 GLU   B C    1 
ATOM   5333 C C    B GLU   B 1 104 ? 35.827 -27.684 12.046  0.14 22.50 ?  104 GLU   B C    1 
ATOM   5334 O O    A GLU   B 1 104 ? 35.981 -28.761 11.511  0.86 23.10 ?  104 GLU   B O    1 
ATOM   5335 O O    B GLU   B 1 104 ? 35.929 -28.700 11.351  0.14 22.56 ?  104 GLU   B O    1 
ATOM   5336 C CB   A GLU   B 1 104 ? 37.943 -26.139 12.138  0.86 19.64 ?  104 GLU   B CB   1 
ATOM   5337 C CB   B GLU   B 1 104 ? 37.849 -26.193 12.145  0.14 21.90 ?  104 GLU   B CB   1 
ATOM   5338 C CG   A GLU   B 1 104 ? 39.040 -25.536 13.002  0.86 18.73 ?  104 GLU   B CG   1 
ATOM   5339 C CG   B GLU   B 1 104 ? 38.947 -25.581 13.006  0.14 21.45 ?  104 GLU   B CG   1 
ATOM   5340 C CD   A GLU   B 1 104 ? 39.997 -24.647 12.252  0.86 17.81 ?  104 GLU   B CD   1 
ATOM   5341 C CD   B GLU   B 1 104 ? 39.889 -24.690 12.222  0.14 21.14 ?  104 GLU   B CD   1 
ATOM   5342 O OE1  A GLU   B 1 104 ? 39.998 -24.643 11.002  0.86 16.27 ?  104 GLU   B OE1  1 
ATOM   5343 O OE1  B GLU   B 1 104 ? 39.812 -24.681 10.976  0.14 20.96 ?  104 GLU   B OE1  1 
ATOM   5344 O OE2  A GLU   B 1 104 ? 40.763 -23.947 12.942  0.86 18.70 -1 104 GLU   B OE2  1 
ATOM   5345 O OE2  B GLU   B 1 104 ? 40.710 -23.996 12.858  0.14 21.18 -1 104 GLU   B OE2  1 
ATOM   5346 H H    A GLU   B 1 104 ? 38.678 -28.329 12.963  0.86 27.42 ?  104 GLU   B H    1 
ATOM   5347 H H    B GLU   B 1 104 ? 38.501 -28.446 12.901  0.14 27.74 ?  104 GLU   B H    1 
ATOM   5348 H HA   A GLU   B 1 104 ? 36.739 -26.679 13.698  0.86 25.31 ?  104 GLU   B HA   1 
ATOM   5349 H HA   B GLU   B 1 104 ? 36.609 -26.734 13.680  0.14 26.96 ?  104 GLU   B HA   1 
ATOM   5350 H HB2  A GLU   B 1 104 ? 38.360 -26.587 11.389  0.86 23.58 ?  104 GLU   B HB2  1 
ATOM   5351 H HB2  B GLU   B 1 104 ? 38.271 -26.647 11.399  0.14 26.29 ?  104 GLU   B HB2  1 
ATOM   5352 H HB3  A GLU   B 1 104 ? 37.373 -25.419 11.828  0.86 23.58 ?  104 GLU   B HB3  1 
ATOM   5353 H HB3  B GLU   B 1 104 ? 37.287 -25.471 11.820  0.14 26.29 ?  104 GLU   B HB3  1 
ATOM   5354 H HG2  A GLU   B 1 104 ? 38.639 -24.996 13.701  0.86 22.48 ?  104 GLU   B HG2  1 
ATOM   5355 H HG2  B GLU   B 1 104 ? 38.538 -25.044 13.704  0.14 25.75 ?  104 GLU   B HG2  1 
ATOM   5356 H HG3  A GLU   B 1 104 ? 39.569 -26.245 13.397  0.86 22.48 ?  104 GLU   B HG3  1 
ATOM   5357 H HG3  B GLU   B 1 104 ? 39.470 -26.295 13.406  0.14 25.75 ?  104 GLU   B HG3  1 
ATOM   5358 N N    A ASP   B 1 105 ? 34.856 -26.886 12.063  0.86 22.04 ?  105 ASP   B N    1 
ATOM   5359 N N    B ASP   B 1 105 ? 34.720 -26.948 12.098  0.14 22.60 ?  105 ASP   B N    1 
ATOM   5360 C CA   A ASP   B 1 105 ? 33.574 -27.340 11.536  0.86 22.73 ?  105 ASP   B CA   1 
ATOM   5361 C CA   B ASP   B 1 105 ? 33.471 -27.407 11.501  0.14 22.86 ?  105 ASP   B CA   1 
ATOM   5362 C C    A ASP   B 1 105 ? 33.604 -27.375 10.010  0.86 20.79 ?  105 ASP   B C    1 
ATOM   5363 C C    B ASP   B 1 105 ? 33.581 -27.423 9.981   0.14 22.28 ?  105 ASP   B C    1 
ATOM   5364 O O    A ASP   B 1 105 ? 33.732 -26.334 9.355   0.86 19.94 ?  105 ASP   B O    1 
ATOM   5365 O O    B ASP   B 1 105 ? 33.815 -26.385 9.353   0.14 22.04 ?  105 ASP   B O    1 
ATOM   5366 C CB   A ASP   B 1 105 ? 32.463 -26.418 12.036  0.86 25.69 ?  105 ASP   B CB   1 
ATOM   5367 C CB   B ASP   B 1 105 ? 32.324 -26.504 11.948  0.14 23.66 ?  105 ASP   B CB   1 
ATOM   5368 C CG   A ASP   B 1 105 ? 31.073 -26.907 11.653  0.86 28.20 ?  105 ASP   B CG   1 
ATOM   5369 C CG   B ASP   B 1 105 ? 30.962 -27.103 11.649  0.14 24.38 ?  105 ASP   B CG   1 
ATOM   5370 O OD1  A ASP   B 1 105 ? 30.965 -27.926 10.936  0.86 28.72 ?  105 ASP   B OD1  1 
ATOM   5371 O OD1  B ASP   B 1 105 ? 30.901 -28.104 10.904  0.14 24.57 ?  105 ASP   B OD1  1 
ATOM   5372 O OD2  A ASP   B 1 105 ? 30.081 -26.279 12.084  0.86 29.88 -1 105 ASP   B OD2  1 
ATOM   5373 O OD2  B ASP   B 1 105 ? 29.952 -26.581 12.166  0.14 24.68 -1 105 ASP   B OD2  1 
ATOM   5374 H H    A ASP   B 1 105 ? 34.858 -26.070 12.334  0.86 26.46 ?  105 ASP   B H    1 
ATOM   5375 H H    B ASP   B 1 105 ? 34.668 -26.177 12.472  0.14 27.12 ?  105 ASP   B H    1 
ATOM   5376 H HA   A ASP   B 1 105 ? 33.400 -28.236 11.860  0.86 27.28 ?  105 ASP   B HA   1 
ATOM   5377 H HA   B ASP   B 1 105 ? 33.283 -28.309 11.801  0.14 27.44 ?  105 ASP   B HA   1 
ATOM   5378 H HB2  A ASP   B 1 105 ? 32.515 -26.365 13.006  0.86 30.84 ?  105 ASP   B HB2  1 
ATOM   5379 H HB2  B ASP   B 1 105 ? 32.390 -26.361 12.907  0.14 28.40 ?  105 ASP   B HB2  1 
ATOM   5380 H HB3  A ASP   B 1 105 ? 32.598 -25.534 11.654  0.86 30.84 ?  105 ASP   B HB3  1 
ATOM   5381 H HB3  B ASP   B 1 105 ? 32.388 -25.655 11.483  0.14 28.40 ?  105 ASP   B HB3  1 
ATOM   5382 N N    A ILE   B 1 106 ? 33.469 -28.578 9.444   0.86 20.45 ?  106 ILE   B N    1 
ATOM   5383 N N    B ILE   B 1 106 ? 33.402 -28.608 9.392   0.14 21.99 ?  106 ILE   B N    1 
ATOM   5384 C CA   A ILE   B 1 106 ? 33.462 -28.751 7.995   0.86 19.99 ?  106 ILE   B CA   1 
ATOM   5385 C CA   B ILE   B 1 106 ? 33.431 -28.757 7.942   0.14 21.74 ?  106 ILE   B CA   1 
ATOM   5386 C C    A ILE   B 1 106 ? 32.360 -27.928 7.331   0.86 19.10 ?  106 ILE   B C    1 
ATOM   5387 C C    B ILE   B 1 106 ? 32.342 -27.931 7.270   0.14 21.44 ?  106 ILE   B C    1 
ATOM   5388 O O    A ILE   B 1 106 ? 32.455 -27.605 6.140   0.86 18.05 ?  106 ILE   B O    1 
ATOM   5389 O O    B ILE   B 1 106 ? 32.440 -27.629 6.076   0.14 21.27 ?  106 ILE   B O    1 
ATOM   5390 C CB   A ILE   B 1 106 ? 33.360 -30.258 7.667   0.86 21.39 ?  106 ILE   B CB   1 
ATOM   5391 C CB   B ILE   B 1 106 ? 33.331 -30.256 7.576   0.14 21.89 ?  106 ILE   B CB   1 
ATOM   5392 C CG1  A ILE   B 1 106 ? 33.609 -30.514 6.180   0.86 21.88 ?  106 ILE   B CG1  1 
ATOM   5393 C CG1  B ILE   B 1 106 ? 33.602 -30.479 6.085   0.14 21.90 ?  106 ILE   B CG1  1 
ATOM   5394 C CG2  A ILE   B 1 106 ? 32.006 -30.813 8.095   0.86 22.39 ?  106 ILE   B CG2  1 
ATOM   5395 C CG2  B ILE   B 1 106 ? 31.965 -30.813 7.958   0.14 22.07 ?  106 ILE   B CG2  1 
ATOM   5396 C CD1  A ILE   B 1 106 ? 34.977 -30.074 5.713   0.86 22.30 ?  106 ILE   B CD1  1 
ATOM   5397 C CD1  B ILE   B 1 106 ? 34.977 -30.030 5.642   0.14 21.94 ?  106 ILE   B CD1  1 
ATOM   5398 H H    A ILE   B 1 106 ? 33.396 -29.306 9.888   0.86 24.55 ?  106 ILE   B H    1 
ATOM   5399 H H    B ILE   B 1 106 ? 33.271 -29.342 9.816   0.14 26.40 ?  106 ILE   B H    1 
ATOM   5400 H HA   A ILE   B 1 106 ? 34.313 -28.434 7.653   0.86 24.00 ?  106 ILE   B HA   1 
ATOM   5401 H HA   B ILE   B 1 106 ? 34.282 -28.430 7.620   0.14 26.10 ?  106 ILE   B HA   1 
ATOM   5402 H HB   A ILE   B 1 106 ? 34.046 -30.727 8.172   0.86 25.68 ?  106 ILE   B HB   1 
ATOM   5403 H HB   B ILE   B 1 106 ? 34.005 -30.738 8.080   0.14 26.28 ?  106 ILE   B HB   1 
ATOM   5404 H HG12 A ILE   B 1 106 ? 33.532 -31.468 6.011   0.86 26.27 ?  106 ILE   B HG12 1 
ATOM   5405 H HG12 B ILE   B 1 106 ? 33.528 -31.429 5.894   0.14 26.29 ?  106 ILE   B HG12 1 
ATOM   5406 H HG13 A ILE   B 1 106 ? 32.948 -30.034 5.663   0.86 26.27 ?  106 ILE   B HG13 1 
ATOM   5407 H HG13 B ILE   B 1 106 ? 32.947 -29.990 5.567   0.14 26.29 ?  106 ILE   B HG13 1 
ATOM   5408 H HG21 A ILE   B 1 106 ? 32.014 -31.778 7.996   0.86 26.87 ?  106 ILE   B HG21 1 
ATOM   5409 H HG21 B ILE   B 1 106 ? 31.978 -31.777 7.853   0.14 26.50 ?  106 ILE   B HG21 1 
ATOM   5410 H HG22 A ILE   B 1 106 ? 31.848 -30.580 9.025   0.86 26.87 ?  106 ILE   B HG22 1 
ATOM   5411 H HG22 B ILE   B 1 106 ? 31.779 -30.584 8.882   0.14 26.50 ?  106 ILE   B HG22 1 
ATOM   5412 H HG23 A ILE   B 1 106 ? 31.314 -30.428 7.537   0.86 26.87 ?  106 ILE   B HG23 1 
ATOM   5413 H HG23 B ILE   B 1 106 ? 31.291 -30.427 7.378   0.14 26.50 ?  106 ILE   B HG23 1 
ATOM   5414 H HD11 A ILE   B 1 106 ? 35.162 -30.482 4.854   0.86 26.76 ?  106 ILE   B HD11 1 
ATOM   5415 H HD11 B ILE   B 1 106 ? 35.165 -30.409 4.770   0.14 26.34 ?  106 ILE   B HD11 1 
ATOM   5416 H HD12 A ILE   B 1 106 ? 34.989 -29.108 5.631   0.86 26.76 ?  106 ILE   B HD12 1 
ATOM   5417 H HD12 B ILE   B 1 106 ? 34.992 -29.062 5.592   0.14 26.34 ?  106 ILE   B HD12 1 
ATOM   5418 H HD13 A ILE   B 1 106 ? 35.640 -30.359 6.364   0.86 26.76 ?  106 ILE   B HD13 1 
ATOM   5419 H HD13 B ILE   B 1 106 ? 35.632 -30.341 6.286   0.14 26.34 ?  106 ILE   B HD13 1 
ATOM   5420 N N    A GLN   B 1 107 ? 31.320 -27.559 8.079   0.86 20.11 ?  107 GLN   B N    1 
ATOM   5421 N N    B GLN   B 1 107 ? 31.299 -27.553 8.013   0.14 21.39 ?  107 GLN   B N    1 
ATOM   5422 C CA   A GLN   B 1 107 ? 30.244 -26.749 7.516   0.86 20.89 ?  107 GLN   B CA   1 
ATOM   5423 C CA   B GLN   B 1 107 ? 30.229 -26.735 7.452   0.14 21.28 ?  107 GLN   B CA   1 
ATOM   5424 C C    A GLN   B 1 107 ? 30.737 -25.402 6.994   0.86 19.03 ?  107 GLN   B C    1 
ATOM   5425 C C    B GLN   B 1 107 ? 30.725 -25.369 6.989   0.14 19.05 ?  107 GLN   B C    1 
ATOM   5426 O O    A GLN   B 1 107 ? 30.101 -24.824 6.107   0.86 20.31 ?  107 GLN   B O    1 
ATOM   5427 O O    B GLN   B 1 107 ? 30.069 -24.737 6.155   0.14 19.30 ?  107 GLN   B O    1 
ATOM   5428 C CB   A GLN   B 1 107 ? 29.156 -26.553 8.574   0.86 24.54 ?  107 GLN   B CB   1 
ATOM   5429 C CB   B GLN   B 1 107 ? 29.113 -26.574 8.488   0.14 23.40 ?  107 GLN   B CB   1 
ATOM   5430 C CG   A GLN   B 1 107 ? 27.826 -26.050 8.036   0.86 28.50 ?  107 GLN   B CG   1 
ATOM   5431 C CG   B GLN   B 1 107 ? 27.789 -26.066 7.929   0.14 25.38 ?  107 GLN   B CG   1 
ATOM   5432 C CD   A GLN   B 1 107 ? 27.767 -24.538 7.924   0.86 31.45 ?  107 GLN   B CD   1 
ATOM   5433 C CD   B GLN   B 1 107 ? 27.683 -24.553 7.939   0.14 26.92 ?  107 GLN   B CD   1 
ATOM   5434 O OE1  A GLN   B 1 107 ? 28.615 -23.826 8.467   0.86 32.60 ?  107 GLN   B OE1  1 
ATOM   5435 O OE1  B GLN   B 1 107 ? 28.530 -23.861 8.506   0.14 27.51 ?  107 GLN   B OE1  1 
ATOM   5436 N NE2  A GLN   B 1 107 ? 26.757 -24.037 7.217   0.86 32.48 ?  107 GLN   B NE2  1 
ATOM   5437 N NE2  B GLN   B 1 107 ? 26.635 -24.030 7.313   0.14 27.41 ?  107 GLN   B NE2  1 
ATOM   5438 H H    A GLN   B 1 107 ? 31.222 -27.759 8.905   0.86 24.14 ?  107 GLN   B H    1 
ATOM   5439 H H    B GLN   B 1 107 ? 31.185 -27.764 8.837   0.14 25.67 ?  107 GLN   B H    1 
ATOM   5440 H HA   A GLN   B 1 107 ? 29.854 -27.234 6.773   0.86 25.08 ?  107 GLN   B HA   1 
ATOM   5441 H HA   B GLN   B 1 107 ? 29.853 -27.194 6.684   0.14 25.54 ?  107 GLN   B HA   1 
ATOM   5442 H HB2  A GLN   B 1 107 ? 28.992 -27.404 9.007   0.86 29.46 ?  107 GLN   B HB2  1 
ATOM   5443 H HB2  B GLN   B 1 107 ? 28.943 -27.436 8.895   0.14 28.09 ?  107 GLN   B HB2  1 
ATOM   5444 H HB3  A GLN   B 1 107 ? 29.473 -25.912 9.229   0.86 29.46 ?  107 GLN   B HB3  1 
ATOM   5445 H HB3  B GLN   B 1 107 ? 29.407 -25.948 9.168   0.14 28.09 ?  107 GLN   B HB3  1 
ATOM   5446 H HG2  A GLN   B 1 107 ? 27.680 -26.420 7.152   0.86 34.21 ?  107 GLN   B HG2  1 
ATOM   5447 H HG2  B GLN   B 1 107 ? 27.697 -26.365 7.011   0.14 30.46 ?  107 GLN   B HG2  1 
ATOM   5448 H HG3  A GLN   B 1 107 ? 27.115 -26.339 8.635   0.86 34.21 ?  107 GLN   B HG3  1 
ATOM   5449 H HG3  B GLN   B 1 107 ? 27.062 -26.424 8.467   0.14 30.46 ?  107 GLN   B HG3  1 
ATOM   5450 H HE21 A GLN   B 1 107 ? 26.184 -24.564 6.848   0.86 38.98 ?  107 GLN   B HE21 1 
ATOM   5451 H HE21 B GLN   B 1 107 ? 26.064 -24.545 6.927   0.14 32.91 ?  107 GLN   B HE21 1 
ATOM   5452 H HE22 A GLN   B 1 107 ? 26.674 -23.186 7.127   0.86 38.98 ?  107 GLN   B HE22 1 
ATOM   5453 H HE22 B GLN   B 1 107 ? 26.527 -23.178 7.293   0.14 32.91 ?  107 GLN   B HE22 1 
ATOM   5454 N N    . LEU   B 1 108 ? 31.864 -24.900 7.503   1.00 16.68 ?  108 LEU   B N    1 
ATOM   5455 C CA   . LEU   B 1 108 ? 32.420 -23.610 7.091   1.00 14.85 ?  108 LEU   B CA   1 
ATOM   5456 C C    . LEU   B 1 108 ? 33.069 -23.643 5.715   1.00 13.09 ?  108 LEU   B C    1 
ATOM   5457 O O    . LEU   B 1 108 ? 33.497 -22.591 5.218   1.00 13.18 ?  108 LEU   B O    1 
ATOM   5458 C CB   . LEU   B 1 108 ? 33.432 -23.131 8.129   1.00 15.39 ?  108 LEU   B CB   1 
ATOM   5459 C CG   . LEU   B 1 108 ? 32.816 -22.690 9.454   1.00 16.78 ?  108 LEU   B CG   1 
ATOM   5460 C CD1  . LEU   B 1 108 ? 33.864 -22.606 10.548  1.00 16.81 ?  108 LEU   B CD1  1 
ATOM   5461 C CD2  . LEU   B 1 108 ? 32.120 -21.349 9.283   1.00 18.64 ?  108 LEU   B CD2  1 
ATOM   5462 H H    A LEU   B 1 108 ? 32.330 -25.297 8.106   0.86 20.03 ?  108 LEU   B H    1 
ATOM   5463 H H    B LEU   B 1 108 ? 32.329 -25.310 8.097   0.14 20.03 ?  108 LEU   B H    1 
ATOM   5464 H HA   . LEU   B 1 108 ? 31.700 -22.964 7.058   1.00 17.83 ?  108 LEU   B HA   1 
ATOM   5465 H HB2  . LEU   B 1 108 ? 34.046 -23.856 8.320   1.00 18.47 ?  108 LEU   B HB2  1 
ATOM   5466 H HB3  . LEU   B 1 108 ? 33.915 -22.377 7.764   1.00 18.47 ?  108 LEU   B HB3  1 
ATOM   5467 H HG   . LEU   B 1 108 ? 32.148 -23.339 9.730   1.00 20.14 ?  108 LEU   B HG   1 
ATOM   5468 H HD11 . LEU   B 1 108 ? 33.432 -22.359 11.384  1.00 20.19 ?  108 LEU   B HD11 1 
ATOM   5469 H HD12 . LEU   B 1 108 ? 34.295 -23.468 10.643  1.00 20.19 ?  108 LEU   B HD12 1 
ATOM   5470 H HD13 . LEU   B 1 108 ? 34.519 -21.932 10.308  1.00 20.19 ?  108 LEU   B HD13 1 
ATOM   5471 H HD21 . LEU   B 1 108 ? 31.822 -21.035 10.151  1.00 22.37 ?  108 LEU   B HD21 1 
ATOM   5472 H HD22 . LEU   B 1 108 ? 32.747 -20.717 8.899   1.00 22.37 ?  108 LEU   B HD22 1 
ATOM   5473 H HD23 . LEU   B 1 108 ? 31.359 -21.461 8.692   1.00 22.37 ?  108 LEU   B HD23 1 
ATOM   5474 N N    . LEU   B 1 109 ? 33.139 -24.815 5.089   1.00 12.19 ?  109 LEU   B N    1 
ATOM   5475 C CA   . LEU   B 1 109 ? 33.765 -24.922 3.780   1.00 11.65 ?  109 LEU   B CA   1 
ATOM   5476 C C    . LEU   B 1 109 ? 33.002 -24.131 2.723   1.00 10.89 ?  109 LEU   B C    1 
ATOM   5477 O O    . LEU   B 1 109 ? 33.619 -23.535 1.833   1.00 10.89 ?  109 LEU   B O    1 
ATOM   5478 C CB   . LEU   B 1 109 ? 33.882 -26.394 3.396   1.00 11.77 ?  109 LEU   B CB   1 
ATOM   5479 C CG   . LEU   B 1 109 ? 34.663 -26.721 2.124   1.00 11.57 ?  109 LEU   B CG   1 
ATOM   5480 C CD1  . LEU   B 1 109 ? 36.048 -26.087 2.134   1.00 11.94 ?  109 LEU   B CD1  1 
ATOM   5481 C CD2  . LEU   B 1 109 ? 34.764 -28.233 1.962   1.00 12.55 ?  109 LEU   B CD2  1 
ATOM   5482 H H    . LEU   B 1 109 ? 32.834 -25.557 5.397   1.00 14.64 ?  109 LEU   B H    1 
ATOM   5483 H HA   . LEU   B 1 109 ? 34.657 -24.556 3.831   1.00 13.98 ?  109 LEU   B HA   1 
ATOM   5484 H HB2  . LEU   B 1 109 ? 34.325 -26.862 4.122   1.00 14.14 ?  109 LEU   B HB2  1 
ATOM   5485 H HB3  . LEU   B 1 109 ? 32.990 -26.755 3.283   1.00 14.14 ?  109 LEU   B HB3  1 
ATOM   5486 H HG   . LEU   B 1 109 ? 34.176 -26.377 1.355   1.00 13.89 ?  109 LEU   B HG   1 
ATOM   5487 H HD11 . LEU   B 1 109 ? 36.562 -26.440 1.391   1.00 14.34 ?  109 LEU   B HD11 1 
ATOM   5488 H HD12 . LEU   B 1 109 ? 35.955 -25.129 2.050   1.00 14.34 ?  109 LEU   B HD12 1 
ATOM   5489 H HD13 . LEU   B 1 109 ? 36.485 -26.311 2.972   1.00 14.34 ?  109 LEU   B HD13 1 
ATOM   5490 H HD21 . LEU   B 1 109 ? 35.335 -28.431 1.202   1.00 15.06 ?  109 LEU   B HD21 1 
ATOM   5491 H HD22 . LEU   B 1 109 ? 35.144 -28.610 2.769   1.00 15.06 ?  109 LEU   B HD22 1 
ATOM   5492 H HD23 . LEU   B 1 109 ? 33.876 -28.597 1.811   1.00 15.06 ?  109 LEU   B HD23 1 
ATOM   5493 N N    . LYS   B 1 110 ? 31.666 -24.099 2.801   1.00 10.76 ?  110 LYS   B N    1 
ATOM   5494 C CA   . LYS   B 1 110 ? 30.910 -23.336 1.813   1.00 10.65 ?  110 LYS   B CA   1 
ATOM   5495 C C    . LYS   B 1 110 ? 31.247 -21.846 1.905   1.00 10.38 ?  110 LYS   B C    1 
ATOM   5496 O O    . LYS   B 1 110 ? 31.497 -21.191 0.890   1.00 10.11 ?  110 LYS   B O    1 
ATOM   5497 C CB   . LYS   B 1 110 ? 29.407 -23.584 1.961   1.00 11.37 ?  110 LYS   B CB   1 
ATOM   5498 C CG   . LYS   B 1 110 ? 28.603 -22.957 0.828   1.00 11.74 ?  110 LYS   B CG   1 
ATOM   5499 C CD   . LYS   B 1 110 ? 27.142 -23.391 0.852   1.00 12.20 ?  110 LYS   B CD   1 
ATOM   5500 C CE   . LYS   B 1 110 ? 26.362 -22.862 -0.353  1.00 12.75 ?  110 LYS   B CE   1 
ATOM   5501 N NZ   . LYS   B 1 110 ? 26.696 -23.563 -1.626  1.00 13.03 ?  110 LYS   B NZ   1 
ATOM   5502 H H    . LYS   B 1 110 ? 31.192 -24.505 3.391   1.00 12.92 ?  110 LYS   B H    1 
ATOM   5503 H HA   . LYS   B 1 110 ? 31.168 -23.641 0.926   1.00 12.79 ?  110 LYS   B HA   1 
ATOM   5504 H HB2  . LYS   B 1 110 ? 29.240 -24.542 1.951   1.00 13.66 ?  110 LYS   B HB2  1 
ATOM   5505 H HB3  . LYS   B 1 110 ? 29.102 -23.201 2.795   1.00 13.66 ?  110 LYS   B HB3  1 
ATOM   5506 H HG2  . LYS   B 1 110 ? 28.624 -21.990 0.914   1.00 14.09 ?  110 LYS   B HG2  1 
ATOM   5507 H HG3  . LYS   B 1 110 ? 28.977 -23.225 -0.025  1.00 14.09 ?  110 LYS   B HG3  1 
ATOM   5508 H HD2  . LYS   B 1 110 ? 27.096 -24.364 0.841   1.00 14.65 ?  110 LYS   B HD2  1 
ATOM   5509 H HD3  . LYS   B 1 110 ? 26.718 -23.053 1.660   1.00 14.65 ?  110 LYS   B HD3  1 
ATOM   5510 H HE2  . LYS   B 1 110 ? 25.412 -22.982 -0.190  1.00 15.31 ?  110 LYS   B HE2  1 
ATOM   5511 H HE3  . LYS   B 1 110 ? 26.563 -21.924 -0.467  1.00 15.31 ?  110 LYS   B HE3  1 
ATOM   5512 H HZ1  . LYS   B 1 110 ? 26.221 -23.223 -2.294  1.00 15.64 ?  110 LYS   B HZ1  1 
ATOM   5513 H HZ2  . LYS   B 1 110 ? 27.563 -23.467 -1.805  1.00 15.64 ?  110 LYS   B HZ2  1 
ATOM   5514 H HZ3  . LYS   B 1 110 ? 26.513 -24.433 -1.552  1.00 15.64 ?  110 LYS   B HZ3  1 
ATOM   5515 N N    . SER   B 1 111 ? 31.271 -21.297 3.123   1.00 10.64 ?  111 SER   B N    1 
ATOM   5516 C CA   . SER   B 1 111 ? 31.661 -19.899 3.300   1.00 10.58 ?  111 SER   B CA   1 
ATOM   5517 C C    . SER   B 1 111 ? 33.044 -19.638 2.716   1.00 9.99  ?  111 SER   B C    1 
ATOM   5518 O O    . SER   B 1 111 ? 33.274 -18.604 2.078   1.00 10.39 ?  111 SER   B O    1 
ATOM   5519 C CB   . SER   B 1 111 ? 31.642 -19.544 4.784   1.00 11.97 ?  111 SER   B CB   1 
ATOM   5520 O OG   . SER   B 1 111 ? 30.328 -19.564 5.293   1.00 13.90 ?  111 SER   B OG   1 
ATOM   5521 H H    . SER   B 1 111 ? 31.072 -21.714 3.850   1.00 12.78 ?  111 SER   B H    1 
ATOM   5522 H HA   . SER   B 1 111 ? 31.025 -19.333 2.840   1.00 12.71 ?  111 SER   B HA   1 
ATOM   5523 H HB2  . SER   B 1 111 ? 32.177 -20.187 5.272   1.00 14.37 ?  111 SER   B HB2  1 
ATOM   5524 H HB3  . SER   B 1 111 ? 31.997 -18.653 4.901   1.00 14.37 ?  111 SER   B HB3  1 
ATOM   5525 H HG   . SER   B 1 111 ? 30.324 -19.377 6.117   1.00 16.69 ?  111 SER   B HG   1 
ATOM   5526 N N    . ALA   B 1 112 ? 33.983 -20.557 2.939   1.00 10.18 ?  112 ALA   B N    1 
ATOM   5527 C CA   . ALA   B 1 112 ? 35.326 -20.390 2.391   1.00 10.23 ?  112 ALA   B CA   1 
ATOM   5528 C C    . ALA   B 1 112 ? 35.288 -20.286 0.869   1.00 9.61  ?  112 ALA   B C    1 
ATOM   5529 O O    . ALA   B 1 112 ? 35.918 -19.398 0.282   1.00 9.89  ?  112 ALA   B O    1 
ATOM   5530 C CB   . ALA   B 1 112 ? 36.232 -21.536 2.849   1.00 10.73 ?  112 ALA   B CB   1 
ATOM   5531 H H    . ALA   B 1 112 ? 33.872 -21.276 3.404   1.00 12.22 ?  112 ALA   B H    1 
ATOM   5532 H HA   . ALA   B 1 112 ? 35.700 -19.565 2.737   1.00 12.29 ?  112 ALA   B HA   1 
ATOM   5533 H HB1  . ALA   B 1 112 ? 37.121 -21.397 2.484   1.00 12.88 ?  112 ALA   B HB1  1 
ATOM   5534 H HB2  . ALA   B 1 112 ? 36.273 -21.537 3.820   1.00 12.88 ?  112 ALA   B HB2  1 
ATOM   5535 H HB3  . ALA   B 1 112 ? 35.869 -22.374 2.532   1.00 12.88 ?  112 ALA   B HB3  1 
ATOM   5536 N N    . TYR   B 1 113 ? 34.560 -21.190 0.206   1.00 9.72  ?  113 TYR   B N    1 
ATOM   5537 C CA   . TYR   B 1 113 ? 34.481 -21.132 -1.249  1.00 9.23  ?  113 TYR   B CA   1 
ATOM   5538 C C    . TYR   B 1 113 ? 33.779 -19.876 -1.759  1.00 9.05  ?  113 TYR   B C    1 
ATOM   5539 O O    . TYR   B 1 113 ? 34.056 -19.440 -2.877  1.00 9.20  ?  113 TYR   B O    1 
ATOM   5540 C CB   . TYR   B 1 113 ? 33.812 -22.391 -1.804  1.00 9.57  ?  113 TYR   B CB   1 
ATOM   5541 C CG   . TYR   B 1 113 ? 34.769 -23.541 -2.065  1.00 9.78  ?  113 TYR   B CG   1 
ATOM   5542 C CD1  . TYR   B 1 113 ? 35.764 -23.433 -3.031  1.00 10.36 ?  113 TYR   B CD1  1 
ATOM   5543 C CD2  . TYR   B 1 113 ? 34.671 -24.740 -1.361  1.00 10.08 ?  113 TYR   B CD2  1 
ATOM   5544 C CE1  . TYR   B 1 113 ? 36.639 -24.474 -3.284  1.00 10.51 ?  113 TYR   B CE1  1 
ATOM   5545 C CE2  . TYR   B 1 113 ? 35.541 -25.792 -1.612  1.00 10.35 ?  113 TYR   B CE2  1 
ATOM   5546 C CZ   . TYR   B 1 113 ? 36.523 -25.656 -2.575  1.00 10.39 ?  113 TYR   B CZ   1 
ATOM   5547 O OH   . TYR   B 1 113 ? 37.400 -26.674 -2.855  1.00 10.93 ?  113 TYR   B OH   1 
ATOM   5548 H H    . TYR   B 1 113 ? 34.108 -21.825 0.571   1.00 11.67 ?  113 TYR   B H    1 
ATOM   5549 H HA   . TYR   B 1 113 ? 35.383 -21.112 -1.594  1.00 11.09 ?  113 TYR   B HA   1 
ATOM   5550 H HB2  . TYR   B 1 113 ? 33.148 -22.705 -1.166  1.00 11.50 ?  113 TYR   B HB2  1 
ATOM   5551 H HB3  . TYR   B 1 113 ? 33.375 -22.172 -2.642  1.00 11.50 ?  113 TYR   B HB3  1 
ATOM   5552 H HD1  . TYR   B 1 113 ? 35.844 -22.640 -3.515  1.00 12.44 ?  113 TYR   B HD1  1 
ATOM   5553 H HD2  . TYR   B 1 113 ? 34.004 -24.836 -0.724  1.00 12.11 ?  113 TYR   B HD2  1 
ATOM   5554 H HE1  . TYR   B 1 113 ? 37.298 -24.380 -3.940  1.00 12.63 ?  113 TYR   B HE1  1 
ATOM   5555 H HE2  . TYR   B 1 113 ? 35.455 -26.585 -1.143  1.00 12.43 ?  113 TYR   B HE2  1 
ATOM   5556 H HH   . TYR   B 1 113 ? 37.192 -27.352 -2.405  1.00 13.13 ?  113 TYR   B HH   1 
ATOM   5557 N N    . GLU   B 1 114 ? 32.850 -19.305 -0.985  1.00 9.18  ?  114 GLU   B N    1 
ATOM   5558 C CA   . GLU   B 1 114 ? 32.164 -18.099 -1.438  1.00 9.02  ?  114 GLU   B CA   1 
ATOM   5559 C C    . GLU   B 1 114 ? 33.143 -16.973 -1.730  1.00 8.94  ?  114 GLU   B C    1 
ATOM   5560 O O    . GLU   B 1 114 ? 32.859 -16.111 -2.566  1.00 9.50  ?  114 GLU   B O    1 
ATOM   5561 C CB   . GLU   B 1 114 ? 31.099 -17.671 -0.424  1.00 9.48  ?  114 GLU   B CB   1 
ATOM   5562 C CG   . GLU   B 1 114 ? 29.889 -18.596 -0.476  1.00 9.87  ?  114 GLU   B CG   1 
ATOM   5563 C CD   . GLU   B 1 114 ? 28.871 -18.407 0.638   1.00 9.87  ?  114 GLU   B CD   1 
ATOM   5564 O OE1  . GLU   B 1 114 ? 29.166 -17.791 1.687   1.00 10.50 ?  114 GLU   B OE1  1 
ATOM   5565 O OE2  . GLU   B 1 114 ? 27.745 -18.934 0.470   1.00 10.83 -1 114 GLU   B OE2  1 
ATOM   5566 H H    . GLU   B 1 114 ? 32.595 -19.602 -0.216  1.00 11.02 ?  114 GLU   B H    1 
ATOM   5567 H HA   . GLU   B 1 114 ? 31.706 -18.299 -2.265  1.00 10.84 ?  114 GLU   B HA   1 
ATOM   5568 H HB2  . GLU   B 1 114 ? 31.470 -17.711 0.474   1.00 11.39 ?  114 GLU   B HB2  1 
ATOM   5569 H HB3  . GLU   B 1 114 ? 30.799 -16.775 -0.626  1.00 11.39 ?  114 GLU   B HB3  1 
ATOM   5570 H HG2  . GLU   B 1 114 ? 29.433 -18.464 -1.319  1.00 11.85 ?  114 GLU   B HG2  1 
ATOM   5571 H HG3  . GLU   B 1 114 ? 30.205 -19.520 -0.426  1.00 11.85 ?  114 GLU   B HG3  1 
ATOM   5572 N N    . ASN   B 1 115 ? 34.309 -16.968 -1.076  1.00 9.12  ?  115 ASN   B N    1 
ATOM   5573 C CA   . ASN   B 1 115 ? 35.298 -15.933 -1.368  1.00 9.44  ?  115 ASN   B CA   1 
ATOM   5574 C C    . ASN   B 1 115 ? 35.712 -15.948 -2.833  1.00 8.91  ?  115 ASN   B C    1 
ATOM   5575 O O    . ASN   B 1 115 ? 36.100 -14.903 -3.379  1.00 9.56  ?  115 ASN   B O    1 
ATOM   5576 C CB   . ASN   B 1 115 ? 36.543 -16.114 -0.490  1.00 9.84  ?  115 ASN   B CB   1 
ATOM   5577 C CG   . ASN   B 1 115 ? 36.280 -15.850 0.975   1.00 10.33 ?  115 ASN   B CG   1 
ATOM   5578 O OD1  . ASN   B 1 115 ? 36.281 -14.703 1.419   1.00 12.46 ?  115 ASN   B OD1  1 
ATOM   5579 N ND2  . ASN   B 1 115 ? 36.113 -16.918 1.749   1.00 10.42 ?  115 ASN   B ND2  1 
ATOM   5580 H H    . ASN   B 1 115 ? 34.545 -17.533 -0.466  1.00 10.96 ?  115 ASN   B H    1 
ATOM   5581 H HA   . ASN   B 1 115 ? 34.920 -15.063 -1.166  1.00 11.34 ?  115 ASN   B HA   1 
ATOM   5582 H HB2  . ASN   B 1 115 ? 36.863 -17.027 -0.578  1.00 11.81 ?  115 ASN   B HB2  1 
ATOM   5583 H HB3  . ASN   B 1 115 ? 37.230 -15.495 -0.782  1.00 11.81 ?  115 ASN   B HB3  1 
ATOM   5584 H HD21 . ASN   B 1 115 ? 35.971 -16.821 2.593   1.00 12.51 ?  115 ASN   B HD21 1 
ATOM   5585 H HD22 . ASN   B 1 115 ? 36.136 -17.708 1.408   1.00 12.51 ?  115 ASN   B HD22 1 
ATOM   5586 N N    . PHE   B 1 116 ? 35.685 -17.124 -3.475  1.00 8.70  ?  116 PHE   B N    1 
ATOM   5587 C CA   . PHE   B 1 116 ? 36.115 -17.213 -4.866  1.00 9.09  ?  116 PHE   B CA   1 
ATOM   5588 C C    . PHE   B 1 116 ? 35.217 -16.385 -5.776  1.00 8.86  ?  116 PHE   B C    1 
ATOM   5589 O O    . PHE   B 1 116 ? 35.655 -15.952 -6.848  1.00 9.28  ?  116 PHE   B O    1 
ATOM   5590 C CB   . PHE   B 1 116 ? 36.089 -18.661 -5.390  1.00 8.94  ?  116 PHE   B CB   1 
ATOM   5591 C CG   . PHE   B 1 116 ? 37.162 -19.613 -4.837  1.00 8.93  ?  116 PHE   B CG   1 
ATOM   5592 C CD1  . PHE   B 1 116 ? 37.815 -19.424 -3.628  1.00 9.96  ?  116 PHE   B CD1  1 
ATOM   5593 C CD2  . PHE   B 1 116 ? 37.465 -20.748 -5.578  1.00 9.36  ?  116 PHE   B CD2  1 
ATOM   5594 C CE1  . PHE   B 1 116 ? 38.743 -20.361 -3.172  1.00 9.87  ?  116 PHE   B CE1  1 
ATOM   5595 C CE2  . PHE   B 1 116 ? 38.388 -21.686 -5.135  1.00 9.54  ?  116 PHE   B CE2  1 
ATOM   5596 C CZ   . PHE   B 1 116 ? 39.033 -21.491 -3.935  1.00 9.63  ?  116 PHE   B CZ   1 
ATOM   5597 H H    . PHE   B 1 116 ? 35.423 -17.870 -3.129  1.00 10.44 ?  116 PHE   B H    1 
ATOM   5598 H HA   . PHE   B 1 116 ? 37.020 -16.879 -4.945  1.00 10.92 ?  116 PHE   B HA   1 
ATOM   5599 H HB2  . PHE   B 1 116 ? 35.221 -19.044 -5.176  1.00 10.74 ?  116 PHE   B HB2  1 
ATOM   5600 H HB3  . PHE   B 1 116 ? 36.194 -18.634 -6.355  1.00 10.74 ?  116 PHE   B HB3  1 
ATOM   5601 H HD1  . PHE   B 1 116 ? 37.616 -18.674 -3.109  1.00 11.96 ?  116 PHE   B HD1  1 
ATOM   5602 H HD2  . PHE   B 1 116 ? 37.025 -20.894 -6.385  1.00 11.24 ?  116 PHE   B HD2  1 
ATOM   5603 H HE1  . PHE   B 1 116 ? 39.185 -20.220 -2.365  1.00 11.86 ?  116 PHE   B HE1  1 
ATOM   5604 H HE2  . PHE   B 1 116 ? 38.584 -22.435 -5.651  1.00 11.46 ?  116 PHE   B HE2  1 
ATOM   5605 H HZ   . PHE   B 1 116 ? 39.668 -22.101 -3.636  1.00 11.57 ?  116 PHE   B HZ   1 
ATOM   5606 N N    . ASN   B 1 117 ? 33.950 -16.178 -5.388  1.00 9.16  ?  117 ASN   B N    1 
ATOM   5607 C CA   . ASN   B 1 117 ? 33.002 -15.480 -6.256  1.00 9.39  ?  117 ASN   B CA   1 
ATOM   5608 C C    . ASN   B 1 117 ? 33.311 -13.997 -6.406  1.00 9.55  ?  117 ASN   B C    1 
ATOM   5609 O O    . ASN   B 1 117 ? 32.713 -13.338 -7.261  1.00 10.60 ?  117 ASN   B O    1 
ATOM   5610 C CB   . ASN   B 1 117 ? 31.575 -15.707 -5.770  1.00 9.74  ?  117 ASN   B CB   1 
ATOM   5611 C CG   . ASN   B 1 117 ? 31.129 -17.118 -6.018  1.00 9.69  ?  117 ASN   B CG   1 
ATOM   5612 O OD1  . ASN   B 1 117 ? 31.481 -17.707 -7.039  1.00 10.57 ?  117 ASN   B OD1  1 
ATOM   5613 N ND2  . ASN   B 1 117 ? 30.392 -17.687 -5.079  1.00 9.94  ?  117 ASN   B ND2  1 
ATOM   5614 H H    . ASN   B 1 117 ? 33.624 -16.424 -4.628  1.00 11.00 ?  117 ASN   B H    1 
ATOM   5615 H HA   . ASN   B 1 117 ? 33.069 -15.875 -7.136  1.00 11.28 ?  117 ASN   B HA   1 
ATOM   5616 H HB2  . ASN   B 1 117 ? 31.531 -15.536 -4.814  1.00 11.70 ?  117 ASN   B HB2  1 
ATOM   5617 H HB3  . ASN   B 1 117 ? 30.981 -15.102 -6.243  1.00 11.70 ?  117 ASN   B HB3  1 
ATOM   5618 H HD21 . ASN   B 1 117 ? 30.113 -18.490 -5.179  1.00 11.93 ?  117 ASN   B HD21 1 
ATOM   5619 H HD22 . ASN   B 1 117 ? 30.173 -17.236 -4.377  1.00 11.93 ?  117 ASN   B HD22 1 
ATOM   5620 N N    . GLN   B 1 118 ? 34.245 -13.469 -5.622  1.00 9.45  ?  118 GLN   B N    1 
ATOM   5621 C CA   . GLN   B 1 118 ? 34.677 -12.082 -5.759  1.00 10.07 ?  118 GLN   B CA   1 
ATOM   5622 C C    . GLN   B 1 118 ? 35.743 -11.891 -6.835  1.00 10.38 ?  118 GLN   B C    1 
ATOM   5623 O O    . GLN   B 1 118 ? 36.217 -10.764 -7.014  1.00 11.68 ?  118 GLN   B O    1 
ATOM   5624 C CB   . GLN   B 1 118 ? 35.159 -11.551 -4.406  1.00 10.63 ?  118 GLN   B CB   1 
ATOM   5625 C CG   . GLN   B 1 118 ? 34.077 -11.584 -3.333  1.00 10.83 ?  118 GLN   B CG   1 
ATOM   5626 C CD   . GLN   B 1 118 ? 32.899 -10.684 -3.663  1.00 10.63 ?  118 GLN   B CD   1 
ATOM   5627 O OE1  . GLN   B 1 118 ? 33.083 -9.541  -4.103  1.00 11.36 ?  118 GLN   B OE1  1 
ATOM   5628 N NE2  . GLN   B 1 118 ? 31.685 -11.181 -3.451  1.00 11.15 ?  118 GLN   B NE2  1 
ATOM   5629 H H    . GLN   B 1 118 ? 34.659 -13.896 -4.996  1.00 11.34 ?  118 GLN   B H    1 
ATOM   5630 H HA   . GLN   B 1 118 ? 33.911 -11.551 -6.023  1.00 12.09 ?  118 GLN   B HA   1 
ATOM   5631 H HB2  . GLN   B 1 118 ? 35.904 -12.087 -4.099  1.00 12.77 ?  118 GLN   B HB2  1 
ATOM   5632 H HB3  . GLN   B 1 118 ? 35.441 -10.624 -4.512  1.00 12.77 ?  118 GLN   B HB3  1 
ATOM   5633 H HG2  . GLN   B 1 118 ? 33.750 -12.492 -3.246  1.00 13.00 ?  118 GLN   B HG2  1 
ATOM   5634 H HG3  . GLN   B 1 118 ? 34.460 -11.286 -2.492  1.00 13.00 ?  118 GLN   B HG3  1 
ATOM   5635 H HE21 . GLN   B 1 118 ? 31.600 -11.982 -3.141  1.00 13.39 ?  118 GLN   B HE21 1 
ATOM   5636 H HE22 . GLN   B 1 118 ? 30.996 -10.707 -3.620  1.00 13.39 ?  118 GLN   B HE22 1 
ATOM   5637 N N    . HIS   B 1 119 ? 36.102 -12.949 -7.567  1.00 9.50  ?  119 HIS   B N    1 
ATOM   5638 C CA   . HIS   B 1 119 ? 37.145 -12.904 -8.586  1.00 10.05 ?  119 HIS   B CA   1 
ATOM   5639 C C    . HIS   B 1 119 ? 36.661 -13.644 -9.820  1.00 10.09 ?  119 HIS   B C    1 
ATOM   5640 O O    . HIS   B 1 119 ? 36.161 -14.763 -9.712  1.00 10.63 ?  119 HIS   B O    1 
ATOM   5641 C CB   . HIS   B 1 119 ? 38.429 -13.535 -8.038  1.00 10.67 ?  119 HIS   B CB   1 
ATOM   5642 C CG   . HIS   B 1 119 ? 38.922 -12.824 -6.824  1.00 11.88 ?  119 HIS   B CG   1 
ATOM   5643 N ND1  . HIS   B 1 119 ? 39.704 -11.692 -6.898  1.00 13.66 ?  119 HIS   B ND1  1 
ATOM   5644 C CD2  . HIS   B 1 119 ? 38.645 -13.008 -5.514  1.00 13.26 ?  119 HIS   B CD2  1 
ATOM   5645 C CE1  . HIS   B 1 119 ? 39.922 -11.235 -5.678  1.00 14.55 ?  119 HIS   B CE1  1 
ATOM   5646 N NE2  . HIS   B 1 119 ? 39.289 -12.015 -4.821  1.00 14.75 ?  119 HIS   B NE2  1 
ATOM   5647 H H    . HIS   B 1 119 ? 35.733 -13.727 -7.495  1.00 11.41 ?  119 HIS   B H    1 
ATOM   5648 H HA   . HIS   B 1 119 ? 37.322 -11.982 -8.830  1.00 12.07 ?  119 HIS   B HA   1 
ATOM   5649 H HB2  . HIS   B 1 119 ? 38.251 -14.455 -7.803  1.00 12.82 ?  119 HIS   B HB2  1 
ATOM   5650 H HB3  . HIS   B 1 119 ? 39.116 -13.485 -8.722  1.00 12.82 ?  119 HIS   B HB3  1 
ATOM   5651 H HD2  . HIS   B 1 119 ? 38.127 -13.690 -5.152  1.00 15.92 ?  119 HIS   B HD2  1 
ATOM   5652 H HE1  . HIS   B 1 119 ? 40.448 -10.501 -5.459  1.00 17.47 ?  119 HIS   B HE1  1 
ATOM   5653 H HE2  . HIS   B 1 119 ? 39.304 -11.930 -3.966  1.00 17.71 ?  119 HIS   B HE2  1 
ATOM   5654 N N    A GLU   B 1 120 ? 36.810 -13.025 -10.992 0.86 10.22 ?  120 GLU   B N    1 
ATOM   5655 N N    B GLU   B 1 120 ? 36.813 -13.028 -10.995 0.14 11.48 ?  120 GLU   B N    1 
ATOM   5656 C CA   A GLU   B 1 120 ? 36.218 -13.608 -12.193 0.86 11.52 ?  120 GLU   B CA   1 
ATOM   5657 C CA   B GLU   B 1 120 ? 36.219 -13.605 -12.199 0.14 12.95 ?  120 GLU   B CA   1 
ATOM   5658 C C    A GLU   B 1 120 ? 36.894 -14.907 -12.610 0.86 10.43 ?  120 GLU   B C    1 
ATOM   5659 C C    B GLU   B 1 120 ? 36.903 -14.901 -12.626 0.14 11.56 ?  120 GLU   B C    1 
ATOM   5660 O O    A GLU   B 1 120 ? 36.231 -15.780 -13.184 0.86 10.70 ?  120 GLU   B O    1 
ATOM   5661 O O    B GLU   B 1 120 ? 36.253 -15.773 -13.214 0.14 11.56 ?  120 GLU   B O    1 
ATOM   5662 C CB   A GLU   B 1 120 ? 36.216 -12.600 -13.340 0.86 15.01 ?  120 GLU   B CB   1 
ATOM   5663 C CB   B GLU   B 1 120 ? 36.215 -12.585 -13.337 0.14 15.88 ?  120 GLU   B CB   1 
ATOM   5664 C CG   A GLU   B 1 120 ? 35.251 -11.450 -13.112 0.86 20.36 ?  120 GLU   B CG   1 
ATOM   5665 C CG   B GLU   B 1 120 ? 35.233 -11.445 -13.119 0.14 18.77 ?  120 GLU   B CG   1 
ATOM   5666 C CD   A GLU   B 1 120 ? 35.100 -10.541 -14.315 0.86 25.50 ?  120 GLU   B CD   1 
ATOM   5667 C CD   B GLU   B 1 120 ? 35.032 -10.598 -14.360 0.14 21.23 ?  120 GLU   B CD   1 
ATOM   5668 O OE1  A GLU   B 1 120 ? 36.117 -10.257 -14.981 0.86 27.51 ?  120 GLU   B OE1  1 
ATOM   5669 O OE1  B GLU   B 1 120 ? 36.040 -10.181 -14.968 0.14 22.20 ?  120 GLU   B OE1  1 
ATOM   5670 O OE2  A GLU   B 1 120 ? 33.960 -10.110 -14.587 0.86 28.16 -1 120 GLU   B OE2  1 
ATOM   5671 O OE2  B GLU   B 1 120 ? 33.864 -10.357 -14.730 0.14 22.23 -1 120 GLU   B OE2  1 
ATOM   5672 H H    A GLU   B 1 120 ? 37.235 -12.289 -11.118 0.86 12.27 ?  120 GLU   B H    1 
ATOM   5673 H H    B GLU   B 1 120 ? 37.242 -12.294 -11.118 0.14 13.78 ?  120 GLU   B H    1 
ATOM   5674 H HA   A GLU   B 1 120 ? 35.294 -13.821 -12.001 0.86 13.83 ?  120 GLU   B HA   1 
ATOM   5675 H HA   B GLU   B 1 120 ? 35.295 -13.821 -12.007 0.14 15.54 ?  120 GLU   B HA   1 
ATOM   5676 H HB2  A GLU   B 1 120 ? 37.104 -12.228 -13.438 0.86 18.02 ?  120 GLU   B HB2  1 
ATOM   5677 H HB2  B GLU   B 1 120 ? 37.101 -12.201 -13.421 0.14 19.07 ?  120 GLU   B HB2  1 
ATOM   5678 H HB3  A GLU   B 1 120 ? 35.951 -13.051 -14.157 0.86 18.02 ?  120 GLU   B HB3  1 
ATOM   5679 H HB3  B GLU   B 1 120 ? 35.970 -13.034 -14.162 0.14 19.07 ?  120 GLU   B HB3  1 
ATOM   5680 H HG2  A GLU   B 1 120 ? 34.372 -11.808 -12.916 0.86 24.44 ?  120 GLU   B HG2  1 
ATOM   5681 H HG2  B GLU   B 1 120 ? 34.372 -11.814 -12.865 0.14 22.53 ?  120 GLU   B HG2  1 
ATOM   5682 H HG3  A GLU   B 1 120 ? 35.566 -10.918 -12.365 0.86 24.44 ?  120 GLU   B HG3  1 
ATOM   5683 H HG3  B GLU   B 1 120 ? 35.568 -10.870 -12.413 0.14 22.53 ?  120 GLU   B HG3  1 
ATOM   5684 N N    . VAL   B 1 121 ? 38.196 -15.047 -12.349 1.00 10.33 ?  121 VAL   B N    1 
ATOM   5685 C CA   . VAL   B 1 121 ? 38.945 -16.254 -12.698 1.00 10.27 ?  121 VAL   B CA   1 
ATOM   5686 C C    . VAL   B 1 121 ? 40.058 -16.455 -11.675 1.00 9.81  ?  121 VAL   B C    1 
ATOM   5687 O O    . VAL   B 1 121 ? 40.733 -15.496 -11.281 1.00 10.40 ?  121 VAL   B O    1 
ATOM   5688 C CB   . VAL   B 1 121 ? 39.462 -16.212 -14.157 1.00 12.07 ?  121 VAL   B CB   1 
ATOM   5689 C CG1  . VAL   B 1 121 ? 40.331 -14.985 -14.416 1.00 13.23 ?  121 VAL   B CG1  1 
ATOM   5690 C CG2  . VAL   B 1 121 ? 40.205 -17.493 -14.503 1.00 13.41 ?  121 VAL   B CG2  1 
ATOM   5691 H H    A VAL   B 1 121 ? 38.675 -14.445 -11.966 0.86 12.40 ?  121 VAL   B H    1 
ATOM   5692 H H    B VAL   B 1 121 ? 38.673 -14.449 -11.956 0.14 12.40 ?  121 VAL   B H    1 
ATOM   5693 H HA   . VAL   B 1 121 ? 38.342 -17.010 -12.631 1.00 12.34 ?  121 VAL   B HA   1 
ATOM   5694 H HB   . VAL   B 1 121 ? 38.696 -16.154 -14.754 1.00 14.50 ?  121 VAL   B HB   1 
ATOM   5695 H HG11 . VAL   B 1 121 ? 40.632 -14.998 -15.339 1.00 15.89 ?  121 VAL   B HG11 1 
ATOM   5696 H HG12 . VAL   B 1 121 ? 39.804 -14.184 -14.254 1.00 15.89 ?  121 VAL   B HG12 1 
ATOM   5697 H HG13 . VAL   B 1 121 ? 41.093 -15.005 -13.819 1.00 15.89 ?  121 VAL   B HG13 1 
ATOM   5698 H HG21 . VAL   B 1 121 ? 40.403 -17.494 -15.455 1.00 16.10 ?  121 VAL   B HG21 1 
ATOM   5699 H HG22 . VAL   B 1 121 ? 41.033 -17.524 -13.998 1.00 16.10 ?  121 VAL   B HG22 1 
ATOM   5700 H HG23 . VAL   B 1 121 ? 39.649 -18.252 -14.281 1.00 16.10 ?  121 VAL   B HG23 1 
ATOM   5701 N N    . LEU   B 1 122 ? 40.251 -17.708 -11.246 1.00 9.42  ?  122 LEU   B N    1 
ATOM   5702 C CA   . LEU   B 1 122 ? 41.234 -18.054 -10.222 1.00 9.27  ?  122 LEU   B CA   1 
ATOM   5703 C C    . LEU   B 1 122 ? 41.890 -19.385 -10.548 1.00 9.11  ?  122 LEU   B C    1 
ATOM   5704 O O    . LEU   B 1 122 ? 41.232 -20.307 -11.045 1.00 10.14 ?  122 LEU   B O    1 
ATOM   5705 C CB   . LEU   B 1 122 ? 40.582 -18.287 -8.847  1.00 10.98 ?  122 LEU   B CB   1 
ATOM   5706 C CG   . LEU   B 1 122 ? 39.549 -17.265 -8.357  1.00 10.87 ?  122 LEU   B CG   1 
ATOM   5707 C CD1  . LEU   B 1 122 ? 38.148 -17.628 -8.824  1.00 12.10 ?  122 LEU   B CD1  1 
ATOM   5708 C CD2  . LEU   B 1 122 ? 39.600 -17.164 -6.844  1.00 10.75 ?  122 LEU   B CD2  1 
ATOM   5709 H H    . LEU   B 1 122 ? 39.812 -18.387 -11.537 1.00 11.32 ?  122 LEU   B H    1 
ATOM   5710 H HA   . LEU   B 1 122 ? 41.909 -17.355 -10.148 1.00 11.13 ?  122 LEU   B HA   1 
ATOM   5711 H HB2  . LEU   B 1 122 ? 40.140 -19.146 -8.872  1.00 13.19 ?  122 LEU   B HB2  1 
ATOM   5712 H HB3  . LEU   B 1 122 ? 41.289 -18.310 -8.184  1.00 13.19 ?  122 LEU   B HB3  1 
ATOM   5713 H HG   . LEU   B 1 122 ? 39.766 -16.393 -8.719  1.00 13.06 ?  122 LEU   B HG   1 
ATOM   5714 H HD11 . LEU   B 1 122 ? 37.520 -16.983 -8.464  1.00 14.52 ?  122 LEU   B HD11 1 
ATOM   5715 H HD12 . LEU   B 1 122 ? 38.126 -17.610 -9.792  1.00 14.52 ?  122 LEU   B HD12 1 
ATOM   5716 H HD13 . LEU   B 1 122 ? 37.931 -18.517 -8.503  1.00 14.52 ?  122 LEU   B HD13 1 
ATOM   5717 H HD21 . LEU   B 1 122 ? 38.921 -16.545 -6.540  1.00 12.91 ?  122 LEU   B HD21 1 
ATOM   5718 H HD22 . LEU   B 1 122 ? 39.446 -18.042 -6.460  1.00 12.91 ?  122 LEU   B HD22 1 
ATOM   5719 H HD23 . LEU   B 1 122 ? 40.481 -16.842 -6.579  1.00 12.91 ?  122 LEU   B HD23 1 
ATOM   5720 N N    . LEU   B 1 123 ? 43.177 -19.489 -10.193 1.00 9.01  ?  123 LEU   B N    1 
ATOM   5721 C CA   . LEU   B 1 123 ? 43.894 -20.757 -10.066 1.00 9.15  ?  123 LEU   B CA   1 
ATOM   5722 C C    . LEU   B 1 123 ? 43.865 -21.153 -8.594  1.00 8.92  ?  123 LEU   B C    1 
ATOM   5723 O O    . LEU   B 1 123 ? 44.214 -20.333 -7.739  1.00 9.46  ?  123 LEU   B O    1 
ATOM   5724 C CB   . LEU   B 1 123 ? 45.347 -20.571 -10.519 1.00 9.74  ?  123 LEU   B CB   1 
ATOM   5725 C CG   . LEU   B 1 123 ? 46.294 -21.751 -10.290 1.00 10.24 ?  123 LEU   B CG   1 
ATOM   5726 C CD1  . LEU   B 1 123 ? 45.865 -22.981 -11.081 1.00 10.67 ?  123 LEU   B CD1  1 
ATOM   5727 C CD2  . LEU   B 1 123 ? 47.721 -21.362 -10.650 1.00 10.86 ?  123 LEU   B CD2  1 
ATOM   5728 H H    . LEU   B 1 123 ? 43.674 -18.810 -10.002 1.00 10.82 ?  123 LEU   B H    1 
ATOM   5729 H HA   . LEU   B 1 123 ? 43.465 -21.448 -10.601 1.00 10.99 ?  123 LEU   B HA   1 
ATOM   5730 H HB2  . LEU   B 1 123 ? 45.343 -20.389 -11.472 1.00 11.70 ?  123 LEU   B HB2  1 
ATOM   5731 H HB3  . LEU   B 1 123 ? 45.715 -19.814 -10.046 1.00 11.70 ?  123 LEU   B HB3  1 
ATOM   5732 H HG   . LEU   B 1 123 ? 46.287 -21.992 -9.352  1.00 12.30 ?  123 LEU   B HG   1 
ATOM   5733 H HD11 . LEU   B 1 123 ? 46.505 -23.693 -10.930 1.00 12.82 ?  123 LEU   B HD11 1 
ATOM   5734 H HD12 . LEU   B 1 123 ? 44.985 -23.256 -10.778 1.00 12.82 ?  123 LEU   B HD12 1 
ATOM   5735 H HD13 . LEU   B 1 123 ? 45.836 -22.754 -12.023 1.00 12.82 ?  123 LEU   B HD13 1 
ATOM   5736 H HD21 . LEU   B 1 123 ? 48.304 -22.123 -10.498 1.00 13.04 ?  123 LEU   B HD21 1 
ATOM   5737 H HD22 . LEU   B 1 123 ? 47.750 -21.102 -11.583 1.00 13.04 ?  123 LEU   B HD22 1 
ATOM   5738 H HD23 . LEU   B 1 123 ? 47.992 -20.619 -10.088 1.00 13.04 ?  123 LEU   B HD23 1 
ATOM   5739 N N    . ALA   B 1 124 ? 43.438 -22.383 -8.287  1.00 8.77  ?  124 ALA   B N    1 
ATOM   5740 C CA   . ALA   B 1 124 ? 43.182 -22.713 -6.892  1.00 8.92  ?  124 ALA   B CA   1 
ATOM   5741 C C    . ALA   B 1 124 ? 43.450 -24.174 -6.570  1.00 9.03  ?  124 ALA   B C    1 
ATOM   5742 O O    . ALA   B 1 124 ? 43.324 -25.043 -7.445  1.00 9.40  ?  124 ALA   B O    1 
ATOM   5743 C CB   . ALA   B 1 124 ? 41.722 -22.401 -6.523  1.00 9.50  ?  124 ALA   B CB   1 
ATOM   5744 H H    . ALA   B 1 124 ? 43.288 -23.026 -8.844  1.00 10.54 ?  124 ALA   B H    1 
ATOM   5745 H HA   . ALA   B 1 124 ? 43.748 -22.157 -6.338  1.00 10.71 ?  124 ALA   B HA   1 
ATOM   5746 H HB1  . ALA   B 1 124 ? 41.570 -22.620 -5.590  1.00 11.41 ?  124 ALA   B HB1  1 
ATOM   5747 H HB2  . ALA   B 1 124 ? 41.552 -21.452 -6.666  1.00 11.41 ?  124 ALA   B HB2  1 
ATOM   5748 H HB3  . ALA   B 1 124 ? 41.130 -22.926 -7.085  1.00 11.41 ?  124 ALA   B HB3  1 
ATOM   5749 N N    . PRO   B 1 125 ? 43.748 -24.474 -5.309  1.00 9.16  ?  125 PRO   B N    1 
ATOM   5750 C CA   . PRO   B 1 125 ? 43.689 -25.840 -4.793  1.00 9.82  ?  125 PRO   B CA   1 
ATOM   5751 C C    . PRO   B 1 125 ? 42.287 -26.118 -4.252  1.00 9.78  ?  125 PRO   B C    1 
ATOM   5752 O O    . PRO   B 1 125 ? 41.487 -25.203 -4.041  1.00 10.31 ?  125 PRO   B O    1 
ATOM   5753 C CB   . PRO   B 1 125 ? 44.672 -25.766 -3.622  1.00 10.92 ?  125 PRO   B CB   1 
ATOM   5754 C CG   . PRO   B 1 125 ? 44.413 -24.382 -3.042  1.00 10.94 ?  125 PRO   B CG   1 
ATOM   5755 C CD   . PRO   B 1 125 ? 44.072 -23.509 -4.240  1.00 9.86  ?  125 PRO   B CD   1 
ATOM   5756 H HA   . PRO   B 1 125 ? 43.960 -26.506 -5.446  1.00 11.79 ?  125 PRO   B HA   1 
ATOM   5757 H HB2  . PRO   B 1 125 ? 44.470 -26.457 -2.971  1.00 13.11 ?  125 PRO   B HB2  1 
ATOM   5758 H HB3  . PRO   B 1 125 ? 45.582 -25.844 -3.945  1.00 13.11 ?  125 PRO   B HB3  1 
ATOM   5759 H HG2  . PRO   B 1 125 ? 43.667 -24.413 -2.421  1.00 13.13 ?  125 PRO   B HG2  1 
ATOM   5760 H HG3  . PRO   B 1 125 ? 45.214 -24.055 -2.594  1.00 13.13 ?  125 PRO   B HG3  1 
ATOM   5761 H HD2  . PRO   B 1 125 ? 43.309 -22.945 -4.050  1.00 11.84 ?  125 PRO   B HD2  1 
ATOM   5762 H HD3  . PRO   B 1 125 ? 44.847 -22.972 -4.499  1.00 11.84 ?  125 PRO   B HD3  1 
ATOM   5763 N N    . LEU   B 1 126 ? 42.017 -27.403 -3.983  1.00 10.36 ?  126 LEU   B N    1 
ATOM   5764 C CA   . LEU   B 1 126 ? 40.796 -27.769 -3.273  1.00 10.77 ?  126 LEU   B CA   1 
ATOM   5765 C C    . LEU   B 1 126 ? 40.911 -27.370 -1.807  1.00 10.86 ?  126 LEU   B C    1 
ATOM   5766 O O    . LEU   B 1 126 ? 41.803 -27.829 -1.087  1.00 12.55 ?  126 LEU   B O    1 
ATOM   5767 C CB   . LEU   B 1 126 ? 40.536 -29.264 -3.395  1.00 11.98 ?  126 LEU   B CB   1 
ATOM   5768 C CG   . LEU   B 1 126 ? 39.996 -29.734 -4.747  1.00 12.71 ?  126 LEU   B CG   1 
ATOM   5769 C CD1  . LEU   B 1 126 ? 40.049 -31.248 -4.845  1.00 14.61 ?  126 LEU   B CD1  1 
ATOM   5770 C CD2  . LEU   B 1 126 ? 38.578 -29.244 -4.979  1.00 13.00 ?  126 LEU   B CD2  1 
ATOM   5771 H H    . LEU   B 1 126 ? 42.525 -28.066 -4.184  1.00 12.45 ?  126 LEU   B H    1 
ATOM   5772 H HA   . LEU   B 1 126 ? 40.046 -27.293 -3.664  1.00 12.94 ?  126 LEU   B HA   1 
ATOM   5773 H HB2  . LEU   B 1 126 ? 41.366 -29.734 -3.238  1.00 14.38 ?  126 LEU   B HB2  1 
ATOM   5774 H HB3  . LEU   B 1 126 ? 39.884 -29.518 -2.724  1.00 14.38 ?  126 LEU   B HB3  1 
ATOM   5775 H HG   . LEU   B 1 126 ? 40.555 -29.378 -5.455  1.00 15.26 ?  126 LEU   B HG   1 
ATOM   5776 H HD11 . LEU   B 1 126 ? 39.701 -31.526 -5.709  1.00 17.54 ?  126 LEU   B HD11 1 
ATOM   5777 H HD12 . LEU   B 1 126 ? 40.966 -31.543 -4.749  1.00 17.54 ?  126 LEU   B HD12 1 
ATOM   5778 H HD13 . LEU   B 1 126 ? 39.503 -31.631 -4.136  1.00 17.54 ?  126 LEU   B HD13 1 
ATOM   5779 H HD21 . LEU   B 1 126 ? 38.226 -29.652 -5.786  1.00 15.61 ?  126 LEU   B HD21 1 
ATOM   5780 H HD22 . LEU   B 1 126 ? 38.029 -29.489 -4.218  1.00 15.61 ?  126 LEU   B HD22 1 
ATOM   5781 H HD23 . LEU   B 1 126 ? 38.591 -28.277 -5.079  1.00 15.61 ?  126 LEU   B HD23 1 
ATOM   5782 N N    . LEU   B 1 127 ? 39.982 -26.541 -1.353  1.00 10.47 ?  127 LEU   B N    1 
ATOM   5783 C CA   . LEU   B 1 127 ? 40.030 -26.049 0.013   1.00 10.87 ?  127 LEU   B CA   1 
ATOM   5784 C C    . LEU   B 1 127 ? 39.761 -27.174 1.006   1.00 10.52 ?  127 LEU   B C    1 
ATOM   5785 O O    . LEU   B 1 127 ? 38.946 -28.074 0.772   1.00 10.68 ?  127 LEU   B O    1 
ATOM   5786 C CB   . LEU   B 1 127 ? 39.006 -24.931 0.217   1.00 11.32 ?  127 LEU   B CB   1 
ATOM   5787 C CG   . LEU   B 1 127 ? 39.178 -23.657 -0.615  1.00 11.79 ?  127 LEU   B CG   1 
ATOM   5788 C CD1  . LEU   B 1 127 ? 38.047 -22.701 -0.269  1.00 12.04 ?  127 LEU   B CD1  1 
ATOM   5789 C CD2  . LEU   B 1 127 ? 40.533 -23.014 -0.385  1.00 12.73 ?  127 LEU   B CD2  1 
ATOM   5790 H H    . LEU   B 1 127 ? 39.304 -26.247 -1.812  1.00 12.57 ?  127 LEU   B H    1 
ATOM   5791 H HA   . LEU   B 1 127 ? 40.911 -25.687 0.189   1.00 13.05 ?  127 LEU   B HA   1 
ATOM   5792 H HB2  . LEU   B 1 127 ? 38.124 -25.286 0.015   1.00 13.59 ?  127 LEU   B HB2  1 
ATOM   5793 H HB3  . LEU   B 1 127 ? 39.030 -24.663 1.150   1.00 13.59 ?  127 LEU   B HB3  1 
ATOM   5794 H HG   . LEU   B 1 127 ? 39.090 -23.876 -1.554  1.00 14.16 ?  127 LEU   B HG   1 
ATOM   5795 H HD11 . LEU   B 1 127 ? 38.142 -21.888 -0.791  1.00 14.45 ?  127 LEU   B HD11 1 
ATOM   5796 H HD12 . LEU   B 1 127 ? 37.192 -23.120 -0.470  1.00 14.45 ?  127 LEU   B HD12 1 
ATOM   5797 H HD13 . LEU   B 1 127 ? 38.087 -22.487 0.680   1.00 14.45 ?  127 LEU   B HD13 1 
ATOM   5798 H HD21 . LEU   B 1 127 ? 40.560 -22.163 -0.849  1.00 15.29 ?  127 LEU   B HD21 1 
ATOM   5799 H HD22 . LEU   B 1 127 ? 40.655 -22.876 0.568   1.00 15.29 ?  127 LEU   B HD22 1 
ATOM   5800 H HD23 . LEU   B 1 127 ? 41.216 -23.605 -0.728  1.00 15.29 ?  127 LEU   B HD23 1 
ATOM   5801 N N    . SER   B 1 128 ? 40.446 -27.092 2.138   1.00 10.62 ?  128 SER   B N    1 
ATOM   5802 C CA   . SER   B 1 128 ? 40.343 -28.010 3.265   1.00 11.18 ?  128 SER   B CA   1 
ATOM   5803 C C    . SER   B 1 128 ? 40.839 -29.417 2.941   1.00 12.06 ?  128 SER   B C    1 
ATOM   5804 O O    . SER   B 1 128 ? 40.745 -30.301 3.793   1.00 13.31 ?  128 SER   B O    1 
ATOM   5805 C CB   . SER   B 1 128 ? 38.947 -28.025 3.908   1.00 11.55 ?  128 SER   B CB   1 
ATOM   5806 O OG   . SER   B 1 128 ? 38.625 -26.752 4.459   1.00 11.89 ?  128 SER   B OG   1 
ATOM   5807 H H    . SER   B 1 128 ? 41.017 -26.464 2.288   1.00 12.75 ?  128 SER   B H    1 
ATOM   5808 H HA   . SER   B 1 128 ? 40.940 -27.667 3.950   1.00 13.43 ?  128 SER   B HA   1 
ATOM   5809 H HB2  . SER   B 1 128 ? 38.289 -28.261 3.239   1.00 13.87 ?  128 SER   B HB2  1 
ATOM   5810 H HB3  . SER   B 1 128 ? 38.939 -28.696 4.623   1.00 13.87 ?  128 SER   B HB3  1 
ATOM   5811 H HG   . SER   B 1 128 ? 39.193 -26.553 5.050   1.00 14.28 ?  128 SER   B HG   1 
ATOM   5812 N N    . ALA   B 1 129 ? 41.414 -29.637 1.759   1.00 12.83 ?  129 ALA   B N    1 
ATOM   5813 C CA   . ALA   B 1 129 ? 41.953 -30.938 1.406   1.00 13.85 ?  129 ALA   B CA   1 
ATOM   5814 C C    . ALA   B 1 129 ? 43.344 -31.112 2.002   1.00 12.86 ?  129 ALA   B C    1 
ATOM   5815 O O    . ALA   B 1 129 ? 43.907 -30.204 2.629   1.00 12.98 ?  129 ALA   B O    1 
ATOM   5816 C CB   . ALA   B 1 129 ? 41.997 -31.103 -0.110  1.00 15.53 ?  129 ALA   B CB   1 
ATOM   5817 H H    . ALA   B 1 129 ? 41.503 -29.043 1.145   1.00 15.40 ?  129 ALA   B H    1 
ATOM   5818 H HA   . ALA   B 1 129 ? 41.383 -31.627 1.774   1.00 16.63 ?  129 ALA   B HA   1 
ATOM   5819 H HB1  . ALA   B 1 129 ? 42.354 -31.981 -0.320  1.00 18.65 ?  129 ALA   B HB1  1 
ATOM   5820 H HB2  . ALA   B 1 129 ? 41.098 -31.019 -0.460  1.00 18.65 ?  129 ALA   B HB2  1 
ATOM   5821 H HB3  . ALA   B 1 129 ? 42.568 -30.416 -0.487  1.00 18.65 ?  129 ALA   B HB3  1 
ATOM   5822 N N    . GLY   B 1 130 ? 43.897 -32.305 1.804   1.00 13.19 ?  130 GLY   B N    1 
ATOM   5823 C CA   . GLY   B 1 130 ? 45.287 -32.541 2.149   1.00 14.03 ?  130 GLY   B CA   1 
ATOM   5824 C C    . GLY   B 1 130 ? 45.506 -32.441 3.641   1.00 13.68 ?  130 GLY   B C    1 
ATOM   5825 O O    . GLY   B 1 130 ? 44.811 -33.084 4.442   1.00 14.61 ?  130 GLY   B O    1 
ATOM   5826 H H    . GLY   B 1 130 ? 43.493 -32.984 1.465   1.00 15.84 ?  130 GLY   B H    1 
ATOM   5827 H HA2  . GLY   B 1 130 ? 45.552 -33.430 1.854   1.00 16.84 ?  130 GLY   B HA2  1 
ATOM   5828 H HA3  . GLY   B 1 130 ? 45.854 -31.891 1.702   1.00 16.84 ?  130 GLY   B HA3  1 
ATOM   5829 N N    . ILE   B 1 131 ? 46.474 -31.602 4.026   1.00 13.67 ?  131 ILE   B N    1 
ATOM   5830 C CA   . ILE   B 1 131 ? 46.822 -31.460 5.433   1.00 14.32 ?  131 ILE   B CA   1 
ATOM   5831 C C    . ILE   B 1 131 ? 45.698 -30.865 6.266   1.00 13.78 ?  131 ILE   B C    1 
ATOM   5832 O O    . ILE   B 1 131 ? 45.776 -30.922 7.498   1.00 15.27 ?  131 ILE   B O    1 
ATOM   5833 C CB   . ILE   B 1 131 ? 48.141 -30.680 5.637   1.00 16.32 ?  131 ILE   B CB   1 
ATOM   5834 C CG1  . ILE   B 1 131 ? 47.980 -29.203 5.252   1.00 17.08 ?  131 ILE   B CG1  1 
ATOM   5835 C CG2  . ILE   B 1 131 ? 49.272 -31.331 4.842   1.00 17.66 ?  131 ILE   B CG2  1 
ATOM   5836 C CD1  . ILE   B 1 131 ? 49.202 -28.352 5.560   1.00 18.16 ?  131 ILE   B CD1  1 
ATOM   5837 H H    . ILE   B 1 131 ? 46.938 -31.111 3.492   1.00 16.42 ?  131 ILE   B H    1 
ATOM   5838 H HA   . ILE   B 1 131 ? 46.973 -32.350 5.781   1.00 17.20 ?  131 ILE   B HA   1 
ATOM   5839 H HB   . ILE   B 1 131 ? 48.369 -30.725 6.578   1.00 19.59 ?  131 ILE   B HB   1 
ATOM   5840 H HG12 . ILE   B 1 131 ? 47.809 -29.147 4.300   1.00 20.51 ?  131 ILE   B HG12 1 
ATOM   5841 H HG13 . ILE   B 1 131 ? 47.232 -28.826 5.742   1.00 20.51 ?  131 ILE   B HG13 1 
ATOM   5842 H HG21 . ILE   B 1 131 ? 50.113 -30.930 5.109   1.00 21.20 ?  131 ILE   B HG21 1 
ATOM   5843 H HG22 . ILE   B 1 131 ? 49.281 -32.280 5.031   1.00 21.20 ?  131 ILE   B HG22 1 
ATOM   5844 H HG23 . ILE   B 1 131 ? 49.116 -31.181 3.897   1.00 21.20 ?  131 ILE   B HG23 1 
ATOM   5845 H HD11 . ILE   B 1 131 ? 48.986 -27.421 5.386   1.00 21.80 ?  131 ILE   B HD11 1 
ATOM   5846 H HD12 . ILE   B 1 131 ? 49.439 -28.466 6.493   1.00 21.80 ?  131 ILE   B HD12 1 
ATOM   5847 H HD13 . ILE   B 1 131 ? 49.935 -28.634 4.993   1.00 21.80 ?  131 ILE   B HD13 1 
ATOM   5848 N N    . PHE   B 1 132 ? 44.663 -30.300 5.633   1.00 12.66 ?  132 PHE   B N    1 
ATOM   5849 C CA   . PHE   B 1 132 ? 43.497 -29.799 6.357   1.00 12.73 ?  132 PHE   B CA   1 
ATOM   5850 C C    . PHE   B 1 132 ? 42.471 -30.890 6.668   1.00 13.75 ?  132 PHE   B C    1 
ATOM   5851 O O    . PHE   B 1 132 ? 41.551 -30.645 7.453   1.00 15.51 ?  132 PHE   B O    1 
ATOM   5852 C CB   . PHE   B 1 132 ? 42.827 -28.656 5.576   1.00 12.03 ?  132 PHE   B CB   1 
ATOM   5853 C CG   . PHE   B 1 132 ? 43.529 -27.316 5.695   1.00 12.27 ?  132 PHE   B CG   1 
ATOM   5854 C CD1  . PHE   B 1 132 ? 44.816 -27.123 5.209   1.00 13.60 ?  132 PHE   B CD1  1 
ATOM   5855 C CD2  . PHE   B 1 132 ? 42.863 -26.225 6.237   1.00 11.89 ?  132 PHE   B CD2  1 
ATOM   5856 C CE1  . PHE   B 1 132 ? 45.435 -25.880 5.306   1.00 13.91 ?  132 PHE   B CE1  1 
ATOM   5857 C CE2  . PHE   B 1 132 ? 43.473 -24.978 6.330   1.00 12.30 ?  132 PHE   B CE2  1 
ATOM   5858 C CZ   . PHE   B 1 132 ? 44.759 -24.808 5.863   1.00 13.50 ?  132 PHE   B CZ   1 
ATOM   5859 H H    . PHE   B 1 132 ? 44.616 -30.196 4.780   1.00 15.20 ?  132 PHE   B H    1 
ATOM   5860 H HA   . PHE   B 1 132 ? 43.801 -29.428 7.199   1.00 15.29 ?  132 PHE   B HA   1 
ATOM   5861 H HB2  . PHE   B 1 132 ? 42.817 -28.893 4.638   1.00 14.45 ?  132 PHE   B HB2  1 
ATOM   5862 H HB3  . PHE   B 1 132 ? 41.923 -28.545 5.902   1.00 14.45 ?  132 PHE   B HB3  1 
ATOM   5863 H HD1  . PHE   B 1 132 ? 45.279 -27.839 4.837   1.00 16.32 ?  132 PHE   B HD1  1 
ATOM   5864 H HD2  . PHE   B 1 132 ? 41.994 -26.334 6.554   1.00 14.27 ?  132 PHE   B HD2  1 
ATOM   5865 H HE1  . PHE   B 1 132 ? 46.304 -25.768 4.991   1.00 16.71 ?  132 PHE   B HE1  1 
ATOM   5866 H HE2  . PHE   B 1 132 ? 43.015 -24.260 6.709   1.00 14.77 ?  132 PHE   B HE2  1 
ATOM   5867 H HZ   . PHE   B 1 132 ? 45.174 -23.974 5.929   1.00 16.21 ?  132 PHE   B HZ   1 
ATOM   5868 N N    . GLY   B 1 133 ? 42.590 -32.083 6.075   1.00 13.40 ?  133 GLY   B N    1 
ATOM   5869 C CA   . GLY   B 1 133 ? 41.883 -33.257 6.559   1.00 14.33 ?  133 GLY   B CA   1 
ATOM   5870 C C    . GLY   B 1 133 ? 40.490 -33.521 6.017   1.00 14.46 ?  133 GLY   B C    1 
ATOM   5871 O O    . GLY   B 1 133 ? 39.895 -34.536 6.392   1.00 16.48 ?  133 GLY   B O    1 
ATOM   5872 H H    . GLY   B 1 133 ? 43.088 -32.232 5.388   1.00 16.08 ?  133 GLY   B H    1 
ATOM   5873 H HA2  . GLY   B 1 133 ? 42.421 -34.037 6.359   1.00 17.21 ?  133 GLY   B HA2  1 
ATOM   5874 H HA3  . GLY   B 1 133 ? 41.814 -33.190 7.525   1.00 17.21 ?  133 GLY   B HA3  1 
ATOM   5875 N N    . ALA   B 1 134 ? 39.937 -32.660 5.169   1.00 13.91 ?  134 ALA   B N    1 
ATOM   5876 C CA   . ALA   B 1 134 ? 38.606 -32.926 4.640   1.00 14.06 ?  134 ALA   B CA   1 
ATOM   5877 C C    . ALA   B 1 134 ? 38.678 -33.918 3.482   1.00 14.04 ?  134 ALA   B C    1 
ATOM   5878 O O    . ALA   B 1 134 ? 39.725 -34.110 2.861   1.00 15.34 ?  134 ALA   B O    1 
ATOM   5879 C CB   . ALA   B 1 134 ? 37.935 -31.631 4.179   1.00 14.89 ?  134 ALA   B CB   1 
ATOM   5880 H H    . ALA   B 1 134 ? 40.303 -31.929 4.892   1.00 16.70 ?  134 ALA   B H    1 
ATOM   5881 H HA   . ALA   B 1 134 ? 38.060 -33.314 5.343   1.00 16.88 ?  134 ALA   B HA   1 
ATOM   5882 H HB1  . ALA   B 1 134 ? 37.048 -31.840 3.848   1.00 17.87 ?  134 ALA   B HB1  1 
ATOM   5883 H HB2  . ALA   B 1 134 ? 37.874 -31.023 4.932   1.00 17.87 ?  134 ALA   B HB2  1 
ATOM   5884 H HB3  . ALA   B 1 134 ? 38.469 -31.236 3.474   1.00 17.87 ?  134 ALA   B HB3  1 
ATOM   5885 N N    . ASP   B 1 135 ? 37.545 -34.552 3.201   1.00 14.05 ?  135 ASP   B N    1 
ATOM   5886 C CA   . ASP   B 1 135 ? 37.446 -35.447 2.055   1.00 14.69 ?  135 ASP   B CA   1 
ATOM   5887 C C    . ASP   B 1 135 ? 37.547 -34.617 0.781   1.00 13.53 ?  135 ASP   B C    1 
ATOM   5888 O O    . ASP   B 1 135 ? 36.696 -33.746 0.556   1.00 13.54 ?  135 ASP   B O    1 
ATOM   5889 C CB   . ASP   B 1 135 ? 36.100 -36.176 2.118   1.00 16.45 ?  135 ASP   B CB   1 
ATOM   5890 C CG   . ASP   B 1 135 ? 35.894 -37.160 0.974   1.00 18.22 ?  135 ASP   B CG   1 
ATOM   5891 O OD1  . ASP   B 1 135 ? 36.755 -37.226 0.071   1.00 17.93 ?  135 ASP   B OD1  1 
ATOM   5892 O OD2  . ASP   B 1 135 ? 34.868 -37.882 0.991   1.00 21.27 -1 135 ASP   B OD2  1 
ATOM   5893 H H    . ASP   B 1 135 ? 36.820 -34.481 3.660   1.00 16.87 ?  135 ASP   B H    1 
ATOM   5894 H HA   . ASP   B 1 135 ? 38.163 -36.104 2.091   1.00 17.64 ?  135 ASP   B HA   1 
ATOM   5895 H HB2  . ASP   B 1 135 ? 36.053 -36.672 2.949   1.00 19.75 ?  135 ASP   B HB2  1 
ATOM   5896 H HB3  . ASP   B 1 135 ? 35.392 -35.517 2.081   1.00 19.75 ?  135 ASP   B HB3  1 
ATOM   5897 N N    . PRO   B 1 136 ? 38.556 -34.831 -0.068  1.00 13.64 ?  136 PRO   B N    1 
ATOM   5898 C CA   . PRO   B 1 136 ? 38.664 -33.998 -1.278  1.00 13.09 ?  136 PRO   B CA   1 
ATOM   5899 C C    . PRO   B 1 136 ? 37.483 -34.148 -2.214  1.00 12.60 ?  136 PRO   B C    1 
ATOM   5900 O O    . PRO   B 1 136 ? 37.157 -33.200 -2.942  1.00 12.10 ?  136 PRO   B O    1 
ATOM   5901 C CB   . PRO   B 1 136 ? 39.976 -34.470 -1.919  1.00 14.42 ?  136 PRO   B CB   1 
ATOM   5902 C CG   . PRO   B 1 136 ? 40.170 -35.862 -1.390  1.00 15.34 ?  136 PRO   B CG   1 
ATOM   5903 C CD   . PRO   B 1 136 ? 39.628 -35.835 0.011   1.00 14.79 ?  136 PRO   B CD   1 
ATOM   5904 H HA   . PRO   B 1 136 ? 38.754 -33.063 -1.034  1.00 15.72 ?  136 PRO   B HA   1 
ATOM   5905 H HB2  . PRO   B 1 136 ? 39.887 -34.482 -2.885  1.00 17.32 ?  136 PRO   B HB2  1 
ATOM   5906 H HB3  . PRO   B 1 136 ? 40.704 -33.894 -1.645  1.00 17.32 ?  136 PRO   B HB3  1 
ATOM   5907 H HG2  . PRO   B 1 136 ? 39.678 -36.495 -1.935  1.00 18.42 ?  136 PRO   B HG2  1 
ATOM   5908 H HG3  . PRO   B 1 136 ? 41.117 -36.081 -1.383  1.00 18.42 ?  136 PRO   B HG3  1 
ATOM   5909 H HD2  . PRO   B 1 136 ? 39.258 -36.701 0.251   1.00 17.76 ?  136 PRO   B HD2  1 
ATOM   5910 H HD3  . PRO   B 1 136 ? 40.313 -35.556 0.642   1.00 17.76 ?  136 PRO   B HD3  1 
ATOM   5911 N N    . ILE   B 1 137 ? 36.825 -35.312 -2.217  1.00 12.86 ?  137 ILE   B N    1 
ATOM   5912 C CA   . ILE   B 1 137 ? 35.608 -35.479 -3.010  1.00 13.19 ?  137 ILE   B CA   1 
ATOM   5913 C C    . ILE   B 1 137 ? 34.535 -34.510 -2.534  1.00 12.79 ?  137 ILE   B C    1 
ATOM   5914 O O    . ILE   B 1 137 ? 33.820 -33.897 -3.339  1.00 12.64 ?  137 ILE   B O    1 
ATOM   5915 C CB   . ILE   B 1 137 ? 35.137 -36.946 -2.958  1.00 15.22 ?  137 ILE   B CB   1 
ATOM   5916 C CG1  . ILE   B 1 137 ? 36.125 -37.839 -3.710  1.00 17.72 ?  137 ILE   B CG1  1 
ATOM   5917 C CG2  . ILE   B 1 137 ? 33.735 -37.086 -3.542  1.00 15.65 ?  137 ILE   B CG2  1 
ATOM   5918 C CD1  . ILE   B 1 137 ? 35.818 -39.319 -3.612  1.00 20.14 ?  137 ILE   B CD1  1 
ATOM   5919 H H    . ILE   B 1 137 ? 37.057 -36.011 -1.779  1.00 15.44 ?  137 ILE   B H    1 
ATOM   5920 H HA   . ILE   B 1 137 ? 35.801 -35.266 -3.936  1.00 15.84 ?  137 ILE   B HA   1 
ATOM   5921 H HB   . ILE   B 1 137 ? 35.109 -37.228 -2.034  1.00 18.27 ?  137 ILE   B HB   1 
ATOM   5922 H HG12 . ILE   B 1 137 ? 36.113 -37.596 -4.650  1.00 21.27 ?  137 ILE   B HG12 1 
ATOM   5923 H HG13 . ILE   B 1 137 ? 37.011 -37.695 -3.345  1.00 21.27 ?  137 ILE   B HG13 1 
ATOM   5924 H HG21 . ILE   B 1 137 ? 33.501 -38.027 -3.600  1.00 18.78 ?  137 ILE   B HG21 1 
ATOM   5925 H HG22 . ILE   B 1 137 ? 33.099 -36.637 -2.966  1.00 18.78 ?  137 ILE   B HG22 1 
ATOM   5926 H HG23 . ILE   B 1 137 ? 33.719 -36.692 -4.428  1.00 18.78 ?  137 ILE   B HG23 1 
ATOM   5927 H HD11 . ILE   B 1 137 ? 36.538 -39.807 -4.035  1.00 24.18 ?  137 ILE   B HD11 1 
ATOM   5928 H HD12 . ILE   B 1 137 ? 35.749 -39.568 -2.677  1.00 24.18 ?  137 ILE   B HD12 1 
ATOM   5929 H HD13 . ILE   B 1 137 ? 34.984 -39.508 -4.069  1.00 24.18 ?  137 ILE   B HD13 1 
ATOM   5930 N N    A HIS   B 1 138 ? 34.401 -34.361 -1.219  0.86 13.07 ?  138 HIS   B N    1 
ATOM   5931 N N    B HIS   B 1 138 ? 34.414 -34.342 -1.215  0.14 12.75 ?  138 HIS   B N    1 
ATOM   5932 C CA   A HIS   B 1 138 ? 33.449 -33.397 -0.686  0.86 13.46 ?  138 HIS   B CA   1 
ATOM   5933 C CA   B HIS   B 1 138 ? 33.443 -33.393 -0.681  0.14 12.80 ?  138 HIS   B CA   1 
ATOM   5934 C C    A HIS   B 1 138 ? 33.866 -31.964 -1.005  0.86 12.64 ?  138 HIS   B C    1 
ATOM   5935 C C    B HIS   B 1 138 ? 33.857 -31.953 -0.965  0.14 12.42 ?  138 HIS   B C    1 
ATOM   5936 O O    A HIS   B 1 138 ? 33.020 -31.125 -1.329  0.86 13.13 ?  138 HIS   B O    1 
ATOM   5937 O O    B HIS   B 1 138 ? 33.002 -31.099 -1.225  0.14 12.55 ?  138 HIS   B O    1 
ATOM   5938 C CB   A HIS   B 1 138 ? 33.313 -33.584 0.818   0.86 14.83 ?  138 HIS   B CB   1 
ATOM   5939 C CB   B HIS   B 1 138 ? 33.260 -33.609 0.820   0.14 13.28 ?  138 HIS   B CB   1 
ATOM   5940 C CG   A HIS   B 1 138 ? 32.385 -32.600 1.453   0.86 15.99 ?  138 HIS   B CG   1 
ATOM   5941 C CG   B HIS   B 1 138 ? 32.329 -32.625 1.456   0.14 13.70 ?  138 HIS   B CG   1 
ATOM   5942 N ND1  A HIS   B 1 138 ? 31.044 -32.533 1.138   0.86 17.15 ?  138 HIS   B ND1  1 
ATOM   5943 N ND1  B HIS   B 1 138 ? 30.989 -32.556 1.138   0.14 14.02 ?  138 HIS   B ND1  1 
ATOM   5944 C CD2  A HIS   B 1 138 ? 32.607 -31.623 2.363   0.86 16.56 ?  138 HIS   B CD2  1 
ATOM   5945 C CD2  B HIS   B 1 138 ? 32.545 -31.661 2.381   0.14 13.89 ?  138 HIS   B CD2  1 
ATOM   5946 C CE1  A HIS   B 1 138 ? 30.478 -31.567 1.839   0.86 17.02 ?  138 HIS   B CE1  1 
ATOM   5947 C CE1  B HIS   B 1 138 ? 30.419 -31.596 1.846   0.14 14.05 ?  138 HIS   B CE1  1 
ATOM   5948 N NE2  A HIS   B 1 138 ? 31.404 -31.001 2.592   0.86 16.78 ?  138 HIS   B NE2  1 
ATOM   5949 N NE2  B HIS   B 1 138 ? 31.342 -31.038 2.608   0.14 13.99 ?  138 HIS   B NE2  1 
ATOM   5950 H H    A HIS   B 1 138 ? 34.846 -34.795 -0.628  0.86 15.69 ?  138 HIS   B H    1 
ATOM   5951 H H    B HIS   B 1 138 ? 34.875 -34.760 -0.623  0.14 15.31 ?  138 HIS   B H    1 
ATOM   5952 H HA   A HIS   B 1 138 ? 32.581 -33.556 -1.090  0.86 16.16 ?  138 HIS   B HA   1 
ATOM   5953 H HA   B HIS   B 1 138 ? 32.586 -33.549 -1.108  0.14 15.37 ?  138 HIS   B HA   1 
ATOM   5954 H HB2  A HIS   B 1 138 ? 32.964 -34.472 0.994   0.86 17.80 ?  138 HIS   B HB2  1 
ATOM   5955 H HB2  B HIS   B 1 138 ? 32.899 -34.497 0.969   0.14 15.95 ?  138 HIS   B HB2  1 
ATOM   5956 H HB3  A HIS   B 1 138 ? 34.181 -33.479 1.230   0.86 17.80 ?  138 HIS   B HB3  1 
ATOM   5957 H HB3  B HIS   B 1 138 ? 34.122 -33.527 1.257   0.14 15.95 ?  138 HIS   B HB3  1 
ATOM   5958 H HD1  A HIS   B 1 138 ? 30.638 -33.046 0.578   0.86 20.59 ?  138 HIS   B HD1  1 
ATOM   5959 H HD1  B HIS   B 1 138 ? 30.585 -33.061 0.571   0.14 16.84 ?  138 HIS   B HD1  1 
ATOM   5960 H HD2  A HIS   B 1 138 ? 33.415 -31.419 2.768   0.86 19.88 ?  138 HIS   B HD2  1 
ATOM   5961 H HD2  B HIS   B 1 138 ? 33.355 -31.459 2.791   0.14 16.68 ?  138 HIS   B HD2  1 
ATOM   5962 H HE1  A HIS   B 1 138 ? 29.576 -31.331 1.810   0.86 20.43 ?  138 HIS   B HE1  1 
ATOM   5963 H HE1  B HIS   B 1 138 ? 29.521 -31.355 1.813   0.14 16.87 ?  138 HIS   B HE1  1 
ATOM   5964 N N    . SER   B 1 139 ? 35.158 -31.658 -0.915  1.00 12.10 ?  139 SER   B N    1 
ATOM   5965 C CA   . SER   B 1 139 ? 35.603 -30.309 -1.233  1.00 11.67 ?  139 SER   B CA   1 
ATOM   5966 C C    . SER   B 1 139 ? 35.262 -29.954 -2.673  1.00 10.74 ?  139 SER   B C    1 
ATOM   5967 O O    . SER   B 1 139 ? 34.813 -28.838 -2.950  1.00 10.99 ?  139 SER   B O    1 
ATOM   5968 C CB   . SER   B 1 139 ? 37.100 -30.171 -0.967  1.00 11.88 ?  139 SER   B CB   1 
ATOM   5969 O OG   . SER   B 1 139 ? 37.510 -28.842 -1.242  1.00 12.20 ?  139 SER   B OG   1 
ATOM   5970 H H    A SER   B 1 139 ? 35.778 -32.205 -0.685  0.86 14.53 ?  139 SER   B H    1 
ATOM   5971 H H    B SER   B 1 139 ? 35.782 -32.212 -0.713  0.14 14.53 ?  139 SER   B H    1 
ATOM   5972 H HA   . SER   B 1 139 ? 35.137 -29.687 -0.660  1.00 14.02 ?  139 SER   B HA   1 
ATOM   5973 H HB2  . SER   B 1 139 ? 37.279 -30.366 -0.034  1.00 14.27 ?  139 SER   B HB2  1 
ATOM   5974 H HB3  . SER   B 1 139 ? 37.590 -30.779 -1.540  1.00 14.27 ?  139 SER   B HB3  1 
ATOM   5975 H HG   . SER   B 1 139 ? 37.128 -28.304 -0.720  1.00 14.65 ?  139 SER   B HG   1 
ATOM   5976 N N    . LEU   B 1 140 ? 35.451 -30.893 -3.600  1.00 10.67 ?  140 LEU   B N    1 
ATOM   5977 C CA   . LEU   B 1 140 ? 35.093 -30.640 -4.990  1.00 10.76 ?  140 LEU   B CA   1 
ATOM   5978 C C    . LEU   B 1 140 ? 33.590 -30.416 -5.128  1.00 11.01 ?  140 LEU   B C    1 
ATOM   5979 O O    . LEU   B 1 140 ? 33.151 -29.533 -5.870  1.00 10.91 ?  140 LEU   B O    1 
ATOM   5980 C CB   . LEU   B 1 140 ? 35.570 -31.799 -5.872  1.00 11.04 ?  140 LEU   B CB   1 
ATOM   5981 C CG   . LEU   B 1 140 ? 35.198 -31.690 -7.345  1.00 11.01 ?  140 LEU   B CG   1 
ATOM   5982 C CD1  . LEU   B 1 140 ? 35.758 -30.409 -7.958  1.00 11.55 ?  140 LEU   B CD1  1 
ATOM   5983 C CD2  . LEU   B 1 140 ? 35.672 -32.917 -8.105  1.00 11.87 ?  140 LEU   B CD2  1 
ATOM   5984 H H    . LEU   B 1 140 ? 35.783 -31.673 -3.451  1.00 12.82 ?  140 LEU   B H    1 
ATOM   5985 H HA   . LEU   B 1 140 ? 35.546 -29.834 -5.287  1.00 12.92 ?  140 LEU   B HA   1 
ATOM   5986 H HB2  . LEU   B 1 140 ? 36.542 -31.845 -5.821  1.00 13.26 ?  140 LEU   B HB2  1 
ATOM   5987 H HB3  . LEU   B 1 140 ? 35.190 -32.621 -5.537  1.00 13.26 ?  140 LEU   B HB3  1 
ATOM   5988 H HG   . LEU   B 1 140 ? 34.233 -31.644 -7.419  1.00 13.22 ?  140 LEU   B HG   1 
ATOM   5989 H HD11 . LEU   B 1 140 ? 35.607 -30.427 -8.916  1.00 13.87 ?  140 LEU   B HD11 1 
ATOM   5990 H HD12 . LEU   B 1 140 ? 35.303 -29.642 -7.569  1.00 13.87 ?  140 LEU   B HD12 1 
ATOM   5991 H HD13 . LEU   B 1 140 ? 36.708 -30.357 -7.773  1.00 13.87 ?  140 LEU   B HD13 1 
ATOM   5992 H HD21 . LEU   B 1 140 ? 35.417 -32.817 -9.037  1.00 14.25 ?  140 LEU   B HD21 1 
ATOM   5993 H HD22 . LEU   B 1 140 ? 36.630 -32.983 -8.024  1.00 14.25 ?  140 LEU   B HD22 1 
ATOM   5994 H HD23 . LEU   B 1 140 ? 35.242 -33.696 -7.724  1.00 14.25 ?  140 LEU   B HD23 1 
ATOM   5995 N N    . ARG   B 1 141 ? 32.788 -31.199 -4.401  1.00 11.05 ?  141 ARG   B N    1 
ATOM   5996 C CA   . ARG   B 1 141 ? 31.337 -31.029 -4.399  1.00 12.07 ?  141 ARG   B CA   1 
ATOM   5997 C C    . ARG   B 1 141 ? 30.954 -29.618 -3.965  1.00 11.30 ?  141 ARG   B C    1 
ATOM   5998 O O    . ARG   B 1 141 ? 30.149 -28.938 -4.619  1.00 11.67 ?  141 ARG   B O    1 
ATOM   5999 C CB   . ARG   B 1 141 ? 30.748 -32.058 -3.426  1.00 14.10 ?  141 ARG   B CB   1 
ATOM   6000 C CG   . ARG   B 1 141 ? 29.283 -31.932 -3.093  1.00 16.70 ?  141 ARG   B CG   1 
ATOM   6001 C CD   . ARG   B 1 141 ? 28.473 -32.569 -4.153  1.00 18.60 ?  141 ARG   B CD   1 
ATOM   6002 N NE   . ARG   B 1 141 ? 28.217 -31.660 -5.259  1.00 19.08 ?  141 ARG   B NE   1 
ATOM   6003 C CZ   . ARG   B 1 141 ? 28.228 -32.009 -6.537  1.00 18.58 ?  141 ARG   B CZ   1 
ATOM   6004 N NH1  . ARG   B 1 141 ? 28.668 -33.194 -6.929  1.00 18.76 ?  141 ARG   B NH1  1 
ATOM   6005 N NH2  . ARG   B 1 141 ? 27.793 -31.142 -7.447  1.00 19.03 ?  141 ARG   B NH2  1 
ATOM   6006 H H    . ARG   B 1 141 ? 33.069 -31.837 -3.896  1.00 13.27 ?  141 ARG   B H    1 
ATOM   6007 H HA   . ARG   B 1 141 ? 30.986 -31.195 -5.285  1.00 14.49 ?  141 ARG   B HA   1 
ATOM   6008 H HB2  . ARG   B 1 141 ? 30.891 -32.944 -3.802  1.00 16.93 ?  141 ARG   B HB2  1 
ATOM   6009 H HB3  . ARG   B 1 141 ? 31.235 -31.997 -2.591  1.00 16.93 ?  141 ARG   B HB3  1 
ATOM   6010 H HG2  . ARG   B 1 141 ? 29.110 -32.378 -2.252  1.00 20.05 ?  141 ARG   B HG2  1 
ATOM   6011 H HG3  . ARG   B 1 141 ? 29.033 -30.992 -3.029  1.00 20.05 ?  141 ARG   B HG3  1 
ATOM   6012 H HD2  . ARG   B 1 141 ? 28.946 -33.352 -4.487  1.00 22.33 ?  141 ARG   B HD2  1 
ATOM   6013 H HD3  . ARG   B 1 141 ? 27.626 -32.841 -3.777  1.00 22.33 ?  141 ARG   B HD3  1 
ATOM   6014 H HE   . ARG   B 1 141 ? 28.028 -30.843 -5.066  1.00 22.90 ?  141 ARG   B HE   1 
ATOM   6015 H HH11 . ARG   B 1 141 ? 28.941 -33.771 -6.354  1.00 22.52 ?  141 ARG   B HH11 1 
ATOM   6016 H HH12 . ARG   B 1 141 ? 28.674 -33.390 -7.764  1.00 22.52 ?  141 ARG   B HH12 1 
ATOM   6017 H HH21 . ARG   B 1 141 ? 27.516 -30.362 -7.205  1.00 22.85 ?  141 ARG   B HH21 1 
ATOM   6018 H HH22 . ARG   B 1 141 ? 27.819 -31.345 -8.283  1.00 22.85 ?  141 ARG   B HH22 1 
ATOM   6019 N N    . VAL   B 1 142 ? 31.496 -29.180 -2.833  1.00 11.08 ?  142 VAL   B N    1 
ATOM   6020 C CA   . VAL   B 1 142 ? 31.167 -27.847 -2.345  1.00 11.06 ?  142 VAL   B CA   1 
ATOM   6021 C C    . VAL   B 1 142 ? 31.641 -26.786 -3.332  1.00 11.09 ?  142 VAL   B C    1 
ATOM   6022 O O    . VAL   B 1 142 ? 30.943 -25.796 -3.579  1.00 11.36 ?  142 VAL   B O    1 
ATOM   6023 C CB   . VAL   B 1 142 ? 31.715 -27.621 -0.922  1.00 11.74 ?  142 VAL   B CB   1 
ATOM   6024 C CG1  . VAL   B 1 142 ? 31.394 -26.190 -0.444  1.00 11.80 ?  142 VAL   B CG1  1 
ATOM   6025 C CG2  . VAL   B 1 142 ? 31.142 -28.641 0.047   1.00 12.50 ?  142 VAL   B CG2  1 
ATOM   6026 H H    . VAL   B 1 142 ? 32.046 -29.621 -2.341  1.00 13.30 ?  142 VAL   B H    1 
ATOM   6027 H HA   . VAL   B 1 142 ? 30.208 -27.771 -2.290  1.00 13.29 ?  142 VAL   B HA   1 
ATOM   6028 H HB   . VAL   B 1 142 ? 32.682 -27.718 -0.929  1.00 14.09 ?  142 VAL   B HB   1 
ATOM   6029 H HG11 . VAL   B 1 142 ? 31.584 -26.127 0.504   1.00 14.16 ?  142 VAL   B HG11 1 
ATOM   6030 H HG12 . VAL   B 1 142 ? 31.947 -25.560 -0.934  1.00 14.16 ?  142 VAL   B HG12 1 
ATOM   6031 H HG13 . VAL   B 1 142 ? 30.457 -26.009 -0.608  1.00 14.16 ?  142 VAL   B HG13 1 
ATOM   6032 H HG21 . VAL   B 1 142 ? 31.498 -28.464 0.932   1.00 15.01 ?  142 VAL   B HG21 1 
ATOM   6033 H HG22 . VAL   B 1 142 ? 30.178 -28.555 0.052   1.00 15.01 ?  142 VAL   B HG22 1 
ATOM   6034 H HG23 . VAL   B 1 142 ? 31.400 -29.525 -0.245  1.00 15.01 ?  142 VAL   B HG23 1 
ATOM   6035 N N    . CYS   B 1 143 ? 32.822 -26.981 -3.925  1.00 10.49 ?  143 CYS   B N    1 
ATOM   6036 C CA   . CYS   B 1 143 ? 33.316 -26.039 -4.924  1.00 10.58 ?  143 CYS   B CA   1 
ATOM   6037 C C    . CYS   B 1 143 ? 32.315 -25.882 -6.063  1.00 10.52 ?  143 CYS   B C    1 
ATOM   6038 O O    . CYS   B 1 143 ? 31.908 -24.768 -6.409  1.00 10.97 ?  143 CYS   B O    1 
ATOM   6039 C CB   . CYS   B 1 143 ? 34.673 -26.519 -5.455  1.00 11.14 ?  143 CYS   B CB   1 
ATOM   6040 S SG   . CYS   B 1 143 ? 35.427 -25.414 -6.663  1.00 11.48 ?  143 CYS   B SG   1 
ATOM   6041 H H    . CYS   B 1 143 ? 33.349 -27.643 -3.769  1.00 12.59 ?  143 CYS   B H    1 
ATOM   6042 H HA   . CYS   B 1 143 ? 33.446 -25.170 -4.510  1.00 12.70 ?  143 CYS   B HA   1 
ATOM   6043 H HB2  . CYS   B 1 143 ? 35.289 -26.610 -4.713  1.00 13.38 ?  143 CYS   B HB2  1 
ATOM   6044 H HB3  . CYS   B 1 143 ? 34.549 -27.380 -5.881  1.00 13.38 ?  143 CYS   B HB3  1 
ATOM   6045 H HG   . CYS   B 1 143 ? 36.494 -25.852 -6.990  1.00 13.78 ?  143 CYS   B HG   1 
ATOM   6046 N N    . VAL   B 1 144 ? 31.903 -26.999 -6.660  1.00 10.81 ?  144 VAL   B N    1 
ATOM   6047 C CA   . VAL   B 1 144 ? 31.000 -26.934 -7.803  1.00 11.80 ?  144 VAL   B CA   1 
ATOM   6048 C C    . VAL   B 1 144 ? 29.663 -26.325 -7.423  1.00 11.79 ?  144 VAL   B C    1 
ATOM   6049 O O    . VAL   B 1 144 ? 29.045 -25.615 -8.227  1.00 13.17 ?  144 VAL   B O    1 
ATOM   6050 C CB   . VAL   B 1 144 ? 30.852 -28.345 -8.391  1.00 14.57 ?  144 VAL   B CB   1 
ATOM   6051 C CG1  . VAL   B 1 144 ? 29.589 -28.472 -9.238  1.00 17.03 ?  144 VAL   B CG1  1 
ATOM   6052 C CG2  . VAL   B 1 144 ? 32.106 -28.715 -9.179  1.00 14.53 ?  144 VAL   B CG2  1 
ATOM   6053 H H    . VAL   B 1 144 ? 32.140 -27.794 -6.433  1.00 12.98 ?  144 VAL   B H    1 
ATOM   6054 H HA   . VAL   B 1 144 ? 31.392 -26.373 -8.488  1.00 14.17 ?  144 VAL   B HA   1 
ATOM   6055 H HB   . VAL   B 1 144 ? 30.777 -28.980 -7.660  1.00 17.49 ?  144 VAL   B HB   1 
ATOM   6056 H HG11 . VAL   B 1 144 ? 29.677 -29.254 -9.809  1.00 20.44 ?  144 VAL   B HG11 1 
ATOM   6057 H HG12 . VAL   B 1 144 ? 28.829 -28.578 -8.650  1.00 20.44 ?  144 VAL   B HG12 1 
ATOM   6058 H HG13 . VAL   B 1 144 ? 29.495 -27.678 -9.781  1.00 20.44 ?  144 VAL   B HG13 1 
ATOM   6059 H HG21 . VAL   B 1 144 ? 32.004 -29.612 -9.536  1.00 17.44 ?  144 VAL   B HG21 1 
ATOM   6060 H HG22 . VAL   B 1 144 ? 32.219 -28.082 -9.906  1.00 17.44 ?  144 VAL   B HG22 1 
ATOM   6061 H HG23 . VAL   B 1 144 ? 32.873 -28.679 -8.587  1.00 17.44 ?  144 VAL   B HG23 1 
ATOM   6062 N N    . ASP   B 1 145 ? 29.198 -26.576 -6.202  1.00 11.79 ?  145 ASP   B N    1 
ATOM   6063 C CA   . ASP   B 1 145 ? 27.888 -26.110 -5.773  1.00 12.38 ?  145 ASP   B CA   1 
ATOM   6064 C C    . ASP   B 1 145 ? 27.911 -24.684 -5.227  1.00 12.03 ?  145 ASP   B C    1 
ATOM   6065 O O    . ASP   B 1 145 ? 26.846 -24.142 -4.908  1.00 14.20 ?  145 ASP   B O    1 
ATOM   6066 C CB   . ASP   B 1 145 ? 27.312 -27.035 -4.691  1.00 13.89 ?  145 ASP   B CB   1 
ATOM   6067 C CG   . ASP   B 1 145 ? 26.942 -28.413 -5.208  1.00 15.56 ?  145 ASP   B CG   1 
ATOM   6068 O OD1  . ASP   B 1 145 ? 26.842 -28.605 -6.438  1.00 16.11 ?  145 ASP   B OD1  1 
ATOM   6069 O OD2  . ASP   B 1 145 ? 26.750 -29.308 -4.361  1.00 18.37 -1 145 ASP   B OD2  1 
ATOM   6070 H H    . ASP   B 1 145 ? 29.632 -27.002 -5.597  1.00 14.16 ?  145 ASP   B H    1 
ATOM   6071 H HA   . ASP   B 1 145 ? 27.287 -26.113 -6.533  1.00 14.87 ?  145 ASP   B HA   1 
ATOM   6072 H HB2  . ASP   B 1 145 ? 27.969 -27.156 -3.999  1.00 16.68 ?  145 ASP   B HB2  1 
ATOM   6073 H HB3  . ASP   B 1 145 ? 26.509 -26.628 -4.330  1.00 16.68 ?  145 ASP   B HB3  1 
ATOM   6074 N N    . THR   B 1 146 ? 29.088 -24.074 -5.094  1.00 10.71 ?  146 THR   B N    1 
ATOM   6075 C CA   . THR   B 1 146 ? 29.226 -22.751 -4.485  1.00 10.51 ?  146 THR   B CA   1 
ATOM   6076 C C    . THR   B 1 146 ? 29.862 -21.717 -5.400  1.00 10.34 ?  146 THR   B C    1 
ATOM   6077 O O    . THR   B 1 146 ? 29.408 -20.557 -5.440  1.00 10.77 ?  146 THR   B O    1 
ATOM   6078 C CB   . THR   B 1 146 ? 30.055 -22.860 -3.194  1.00 10.98 ?  146 THR   B CB   1 
ATOM   6079 O OG1  . THR   B 1 146 ? 29.483 -23.854 -2.334  1.00 11.19 ?  146 THR   B OG1  1 
ATOM   6080 C CG2  . THR   B 1 146 ? 30.122 -21.523 -2.471  1.00 11.27 ?  146 THR   B CG2  1 
ATOM   6081 H H    . THR   B 1 146 ? 29.841 -24.414 -5.349  1.00 12.86 ?  146 THR   B H    1 
ATOM   6082 H HA   . THR   B 1 146 ? 28.352 -22.424 -4.244  1.00 12.62 ?  146 THR   B HA   1 
ATOM   6083 H HB   . THR   B 1 146 ? 30.963 -23.116 -3.419  1.00 13.18 ?  146 THR   B HB   1 
ATOM   6084 H HG1  . THR   B 1 146 ? 29.517 -24.611 -2.716  1.00 13.43 ?  146 THR   B HG1  1 
ATOM   6085 H HG21 . THR   B 1 146 ? 30.478 -21.648 -1.578  1.00 13.54 ?  146 THR   B HG21 1 
ATOM   6086 H HG22 . THR   B 1 146 ? 30.701 -20.910 -2.955  1.00 13.54 ?  146 THR   B HG22 1 
ATOM   6087 H HG23 . THR   B 1 146 ? 29.236 -21.136 -2.406  1.00 13.54 ?  146 THR   B HG23 1 
ATOM   6088 N N    . VAL   B 1 147 ? 30.922 -22.093 -6.106  1.00 10.43 ?  147 VAL   B N    1 
ATOM   6089 C CA   . VAL   B 1 147 ? 31.647 -21.148 -6.939  1.00 10.16 ?  147 VAL   B CA   1 
ATOM   6090 C C    . VAL   B 1 147 ? 30.918 -21.015 -8.263  1.00 10.24 ?  147 VAL   B C    1 
ATOM   6091 O O    . VAL   B 1 147 ? 30.552 -22.017 -8.892  1.00 11.12 ?  147 VAL   B O    1 
ATOM   6092 C CB   . VAL   B 1 147 ? 33.100 -21.604 -7.143  1.00 10.40 ?  147 VAL   B CB   1 
ATOM   6093 C CG1  . VAL   B 1 147 ? 33.868 -20.584 -7.963  1.00 10.83 ?  147 VAL   B CG1  1 
ATOM   6094 C CG2  . VAL   B 1 147 ? 33.773 -21.822 -5.800  1.00 10.81 ?  147 VAL   B CG2  1 
ATOM   6095 H H    . VAL   B 1 147 ? 31.246 -22.893 -6.120  1.00 12.53 ?  147 VAL   B H    1 
ATOM   6096 H HA   . VAL   B 1 147 ? 31.663 -20.282 -6.509  1.00 12.21 ?  147 VAL   B HA   1 
ATOM   6097 H HB   . VAL   B 1 147 ? 33.114 -22.448 -7.624  1.00 12.49 ?  147 VAL   B HB   1 
ATOM   6098 H HG11 . VAL   B 1 147 ? 34.813 -20.814 -7.951  1.00 13.01 ?  147 VAL   B HG11 1 
ATOM   6099 H HG12 . VAL   B 1 147 ? 33.540 -20.597 -8.875  1.00 13.01 ?  147 VAL   B HG12 1 
ATOM   6100 H HG13 . VAL   B 1 147 ? 33.740 -19.706 -7.573  1.00 13.01 ?  147 VAL   B HG13 1 
ATOM   6101 H HG21 . VAL   B 1 147 ? 34.717 -22.007 -5.941  1.00 12.98 ?  147 VAL   B HG21 1 
ATOM   6102 H HG22 . VAL   B 1 147 ? 33.673 -21.020 -5.264  1.00 12.98 ?  147 VAL   B HG22 1 
ATOM   6103 H HG23 . VAL   B 1 147 ? 33.354 -22.573 -5.353  1.00 12.98 ?  147 VAL   B HG23 1 
ATOM   6104 N N    . ARG   B 1 148 ? 30.707 -19.768 -8.681  1.00 10.42 ?  148 ARG   B N    1 
ATOM   6105 C CA   . ARG   B 1 148 ? 30.080 -19.442 -9.951  1.00 10.46 ?  148 ARG   B CA   1 
ATOM   6106 C C    . ARG   B 1 148 ? 31.034 -18.767 -10.926 1.00 10.66 ?  148 ARG   B C    1 
ATOM   6107 O O    . ARG   B 1 148 ? 30.755 -18.758 -12.128 1.00 12.04 ?  148 ARG   B O    1 
ATOM   6108 C CB   . ARG   B 1 148 ? 28.845 -18.556 -9.722  1.00 11.24 ?  148 ARG   B CB   1 
ATOM   6109 C CG   . ARG   B 1 148 ? 27.763 -19.254 -8.912  1.00 11.82 ?  148 ARG   B CG   1 
ATOM   6110 C CD   . ARG   B 1 148 ? 26.566 -18.360 -8.606  1.00 12.81 ?  148 ARG   B CD   1 
ATOM   6111 N NE   . ARG   B 1 148 ? 26.959 -17.163 -7.872  1.00 12.40 ?  148 ARG   B NE   1 
ATOM   6112 C CZ   . ARG   B 1 148 ? 27.258 -17.134 -6.579  1.00 11.57 ?  148 ARG   B CZ   1 
ATOM   6113 N NH1  . ARG   B 1 148 ? 27.177 -18.217 -5.823  1.00 11.75 ?  148 ARG   B NH1  1 
ATOM   6114 N NH2  . ARG   B 1 148 ? 27.653 -15.987 -6.029  1.00 11.71 ?  148 ARG   B NH2  1 
ATOM   6115 H H    . ARG   B 1 148 ? 30.931 -19.072 -8.221  1.00 12.51 ?  148 ARG   B H    1 
ATOM   6116 H HA   . ARG   B 1 148 ? 29.780 -20.264 -10.361 1.00 12.56 ?  148 ARG   B HA   1 
ATOM   6117 H HB2  . ARG   B 1 148 ? 29.113 -17.756 -9.240  1.00 13.50 ?  148 ARG   B HB2  1 
ATOM   6118 H HB3  . ARG   B 1 148 ? 28.469 -18.314 -10.582 1.00 13.50 ?  148 ARG   B HB3  1 
ATOM   6119 H HG2  . ARG   B 1 148 ? 27.441 -20.020 -9.412  1.00 14.19 ?  148 ARG   B HG2  1 
ATOM   6120 H HG3  . ARG   B 1 148 ? 28.139 -19.546 -8.067  1.00 14.19 ?  148 ARG   B HG3  1 
ATOM   6121 H HD2  . ARG   B 1 148 ? 26.153 -18.080 -9.437  1.00 15.38 ?  148 ARG   B HD2  1 
ATOM   6122 H HD3  . ARG   B 1 148 ? 25.927 -18.852 -8.064  1.00 15.38 ?  148 ARG   B HD3  1 
ATOM   6123 H HE   . ARG   B 1 148 ? 27.004 -16.424 -8.307  1.00 14.89 ?  148 ARG   B HE   1 
ATOM   6124 H HH11 . ARG   B 1 148 ? 26.919 -18.966 -6.159  1.00 14.11 ?  148 ARG   B HH11 1 
ATOM   6125 H HH12 . ARG   B 1 148 ? 27.370 -18.174 -4.982  1.00 14.11 ?  148 ARG   B HH12 1 
ATOM   6126 H HH21 . ARG   B 1 148 ? 27.712 -15.278 -6.510  1.00 14.06 ?  148 ARG   B HH21 1 
ATOM   6127 H HH22 . ARG   B 1 148 ? 27.849 -15.955 -5.192  1.00 14.06 ?  148 ARG   B HH22 1 
ATOM   6128 N N    . THR   B 1 149 ? 32.141 -18.211 -10.440 1.00 10.67 ?  149 THR   B N    1 
ATOM   6129 C CA   . THR   B 1 149 ? 33.182 -17.658 -11.289 1.00 10.69 ?  149 THR   B CA   1 
ATOM   6130 C C    . THR   B 1 149 ? 34.077 -18.796 -11.787 1.00 10.22 ?  149 THR   B C    1 
ATOM   6131 O O    . THR   B 1 149 ? 33.890 -19.966 -11.442 1.00 10.85 ?  149 THR   B O    1 
ATOM   6132 C CB   . THR   B 1 149 ? 33.952 -16.600 -10.510 1.00 10.77 ?  149 THR   B CB   1 
ATOM   6133 O OG1  . THR   B 1 149 ? 34.399 -17.194 -9.289  1.00 10.78 ?  149 THR   B OG1  1 
ATOM   6134 C CG2  . THR   B 1 149 ? 33.066 -15.389 -10.224 1.00 11.47 ?  149 THR   B CG2  1 
ATOM   6135 H H    . THR   B 1 149 ? 32.310 -18.137 -9.599  1.00 12.81 ?  149 THR   B H    1 
ATOM   6136 H HA   . THR   B 1 149 ? 32.774 -17.231 -12.059 1.00 12.83 ?  149 THR   B HA   1 
ATOM   6137 H HB   . THR   B 1 149 ? 34.719 -16.316 -11.030 1.00 12.93 ?  149 THR   B HB   1 
ATOM   6138 H HG1  . THR   B 1 149 ? 34.820 -16.619 -8.835  1.00 12.94 ?  149 THR   B HG1  1 
ATOM   6139 H HG21 . THR   B 1 149 ? 33.574 -14.715 -9.743  1.00 13.77 ?  149 THR   B HG21 1 
ATOM   6140 H HG22 . THR   B 1 149 ? 32.752 -15.001 -11.060 1.00 13.77 ?  149 THR   B HG22 1 
ATOM   6141 H HG23 . THR   B 1 149 ? 32.302 -15.649 -9.693  1.00 13.77 ?  149 THR   B HG23 1 
ATOM   6142 N N    . ASN   B 1 150 ? 35.038 -18.473 -12.640 1.00 10.44 ?  150 ASN   B N    1 
ATOM   6143 C CA   . ASN   B 1 150 ? 35.805 -19.498 -13.337 1.00 10.93 ?  150 ASN   B CA   1 
ATOM   6144 C C    . ASN   B 1 150 ? 36.968 -19.948 -12.466 1.00 10.66 ?  150 ASN   B C    1 
ATOM   6145 O O    . ASN   B 1 150 ? 37.889 -19.172 -12.194 1.00 11.44 ?  150 ASN   B O    1 
ATOM   6146 C CB   . ASN   B 1 150 ? 36.279 -18.973 -14.683 1.00 12.10 ?  150 ASN   B CB   1 
ATOM   6147 C CG   . ASN   B 1 150 ? 35.134 -18.749 -15.626 1.00 14.62 ?  150 ASN   B CG   1 
ATOM   6148 O OD1  . ASN   B 1 150 ? 34.252 -19.591 -15.737 1.00 15.99 ?  150 ASN   B OD1  1 
ATOM   6149 N ND2  . ASN   B 1 150 ? 35.113 -17.601 -16.283 1.00 16.45 ?  150 ASN   B ND2  1 
ATOM   6150 H H    . ASN   B 1 150 ? 35.274 -17.661 -12.833 1.00 12.53 ?  150 ASN   B H    1 
ATOM   6151 H HA   . ASN   B 1 150 ? 35.228 -20.264 -13.500 1.00 13.13 ?  150 ASN   B HA   1 
ATOM   6152 H HB2  . ASN   B 1 150 ? 36.730 -18.125 -14.555 1.00 14.53 ?  150 ASN   B HB2  1 
ATOM   6153 H HB3  . ASN   B 1 150 ? 36.880 -19.618 -15.085 1.00 14.53 ?  150 ASN   B HB3  1 
ATOM   6154 H HD21 . ASN   B 1 150 ? 34.476 -17.430 -16.837 1.00 19.75 ?  150 ASN   B HD21 1 
ATOM   6155 H HD22 . ASN   B 1 150 ? 35.747 -17.030 -16.171 1.00 19.75 ?  150 ASN   B HD22 1 
ATOM   6156 N N    . VAL   B 1 151 ? 36.937 -21.203 -12.034 1.00 10.24 ?  151 VAL   B N    1 
ATOM   6157 C CA   . VAL   B 1 151 ? 37.957 -21.733 -11.145 1.00 10.26 ?  151 VAL   B CA   1 
ATOM   6158 C C    . VAL   B 1 151 ? 38.670 -22.901 -11.815 1.00 9.87  ?  151 VAL   B C    1 
ATOM   6159 O O    . VAL   B 1 151 ? 38.037 -23.839 -12.320 1.00 10.93 ?  151 VAL   B O    1 
ATOM   6160 C CB   . VAL   B 1 151 ? 37.403 -22.061 -9.744  1.00 11.69 ?  151 VAL   B CB   1 
ATOM   6161 C CG1  . VAL   B 1 151 ? 36.234 -23.047 -9.817  1.00 12.73 ?  151 VAL   B CG1  1 
ATOM   6162 C CG2  . VAL   B 1 151 ? 38.516 -22.560 -8.835  1.00 12.42 ?  151 VAL   B CG2  1 
ATOM   6163 H H    . VAL   B 1 151 ? 36.321 -21.769 -12.245 1.00 12.30 ?  151 VAL   B H    1 
ATOM   6164 H HA   . VAL   B 1 151 ? 38.622 -21.035 -11.020 1.00 12.32 ?  151 VAL   B HA   1 
ATOM   6165 H HB   . VAL   B 1 151 ? 37.064 -21.240 -9.354  1.00 14.04 ?  151 VAL   B HB   1 
ATOM   6166 H HG11 . VAL   B 1 151 ? 35.926 -23.241 -8.919  1.00 15.28 ?  151 VAL   B HG11 1 
ATOM   6167 H HG12 . VAL   B 1 151 ? 35.513 -22.648 -10.333 1.00 15.28 ?  151 VAL   B HG12 1 
ATOM   6168 H HG13 . VAL   B 1 151 ? 36.531 -23.864 -10.249 1.00 15.28 ?  151 VAL   B HG13 1 
ATOM   6169 H HG21 . VAL   B 1 151 ? 38.174 -22.628 -7.930  1.00 14.91 ?  151 VAL   B HG21 1 
ATOM   6170 H HG22 . VAL   B 1 151 ? 38.812 -23.431 -9.143  1.00 14.91 ?  151 VAL   B HG22 1 
ATOM   6171 H HG23 . VAL   B 1 151 ? 39.255 -21.931 -8.862  1.00 14.91 ?  151 VAL   B HG23 1 
ATOM   6172 N N    . TYR   B 1 152 ? 40.000 -22.804 -11.830 1.00 9.69  ?  152 TYR   B N    1 
ATOM   6173 C CA   . TYR   B 1 152 ? 40.910 -23.780 -12.411 1.00 9.92  ?  152 TYR   B CA   1 
ATOM   6174 C C    . TYR   B 1 152 ? 41.632 -24.459 -11.251 1.00 9.43  ?  152 TYR   B C    1 
ATOM   6175 O O    . TYR   B 1 152 ? 42.466 -23.841 -10.585 1.00 9.89  ?  152 TYR   B O    1 
ATOM   6176 C CB   . TYR   B 1 152 ? 41.876 -23.067 -13.363 1.00 10.62 ?  152 TYR   B CB   1 
ATOM   6177 C CG   . TYR   B 1 152 ? 41.191 -22.610 -14.629 1.00 10.99 ?  152 TYR   B CG   1 
ATOM   6178 C CD1  . TYR   B 1 152 ? 40.511 -21.398 -14.691 1.00 11.80 ?  152 TYR   B CD1  1 
ATOM   6179 C CD2  . TYR   B 1 152 ? 41.210 -23.408 -15.762 1.00 11.91 ?  152 TYR   B CD2  1 
ATOM   6180 C CE1  . TYR   B 1 152 ? 39.866 -21.004 -15.848 1.00 12.90 ?  152 TYR   B CE1  1 
ATOM   6181 C CE2  . TYR   B 1 152 ? 40.573 -23.026 -16.918 1.00 13.01 ?  152 TYR   B CE2  1 
ATOM   6182 C CZ   . TYR   B 1 152 ? 39.904 -21.821 -16.963 1.00 13.39 ?  152 TYR   B CZ   1 
ATOM   6183 O OH   . TYR   B 1 152 ? 39.271 -21.451 -18.125 1.00 15.61 ?  152 TYR   B OH   1 
ATOM   6184 H H    . TYR   B 1 152 ? 40.425 -22.136 -11.483 1.00 11.64 ?  152 TYR   B H    1 
ATOM   6185 H HA   . TYR   B 1 152 ? 40.407 -24.449 -12.908 1.00 11.91 ?  152 TYR   B HA   1 
ATOM   6186 H HB2  . TYR   B 1 152 ? 42.239 -22.290 -12.914 1.00 12.76 ?  152 TYR   B HB2  1 
ATOM   6187 H HB3  . TYR   B 1 152 ? 42.591 -23.678 -13.603 1.00 12.76 ?  152 TYR   B HB3  1 
ATOM   6188 H HD1  . TYR   B 1 152 ? 40.481 -20.851 -13.938 1.00 14.16 ?  152 TYR   B HD1  1 
ATOM   6189 H HD2  . TYR   B 1 152 ? 41.656 -24.229 -15.735 1.00 14.30 ?  152 TYR   B HD2  1 
ATOM   6190 H HE1  . TYR   B 1 152 ? 39.419 -20.191 -15.879 1.00 15.49 ?  152 TYR   B HE1  1 
ATOM   6191 H HE2  . TYR   B 1 152 ? 40.600 -23.574 -17.669 1.00 15.62 ?  152 TYR   B HE2  1 
ATOM   6192 H HH   . TYR   B 1 152 ? 38.911 -20.700 -18.020 1.00 18.74 ?  152 TYR   B HH   1 
ATOM   6193 N N    . LEU   B 1 153 ? 41.271 -25.718 -10.990 1.00 9.60  ?  153 LEU   B N    1 
ATOM   6194 C CA   . LEU   B 1 153 ? 41.770 -26.470 -9.847  1.00 9.43  ?  153 LEU   B CA   1 
ATOM   6195 C C    . LEU   B 1 153 ? 43.000 -27.275 -10.234 1.00 9.79  ?  153 LEU   B C    1 
ATOM   6196 O O    . LEU   B 1 153 ? 42.984 -28.000 -11.231 1.00 10.97 ?  153 LEU   B O    1 
ATOM   6197 C CB   . LEU   B 1 153 ? 40.687 -27.424 -9.340  1.00 9.99  ?  153 LEU   B CB   1 
ATOM   6198 C CG   . LEU   B 1 153 ? 39.427 -26.778 -8.769  1.00 10.82 ?  153 LEU   B CG   1 
ATOM   6199 C CD1  . LEU   B 1 153 ? 38.338 -27.824 -8.606  1.00 11.45 ?  153 LEU   B CD1  1 
ATOM   6200 C CD2  . LEU   B 1 153 ? 39.727 -26.116 -7.433  1.00 11.42 ?  153 LEU   B CD2  1 
ATOM   6201 H H    . LEU   B 1 153 ? 40.709 -26.165 -11.472 1.00 11.53 ?  153 LEU   B H    1 
ATOM   6202 H HA   . LEU   B 1 153 ? 41.996 -25.858 -9.133  1.00 11.32 ?  153 LEU   B HA   1 
ATOM   6203 H HB2  . LEU   B 1 153 ? 40.404 -27.990 -10.078 1.00 12.00 ?  153 LEU   B HB2  1 
ATOM   6204 H HB3  . LEU   B 1 153 ? 41.066 -27.978 -8.640  1.00 12.00 ?  153 LEU   B HB3  1 
ATOM   6205 H HG   . LEU   B 1 153 ? 39.105 -26.093 -9.377  1.00 12.99 ?  153 LEU   B HG   1 
ATOM   6206 H HD11 . LEU   B 1 153 ? 37.535 -27.390 -8.272  1.00 13.75 ?  153 LEU   B HD11 1 
ATOM   6207 H HD12 . LEU   B 1 153 ? 38.164 -28.227 -9.465  1.00 13.75 ?  153 LEU   B HD12 1 
ATOM   6208 H HD13 . LEU   B 1 153 ? 38.640 -28.491 -7.973  1.00 13.75 ?  153 LEU   B HD13 1 
ATOM   6209 H HD21 . LEU   B 1 153 ? 38.910 -25.752 -7.064  1.00 13.71 ?  153 LEU   B HD21 1 
ATOM   6210 H HD22 . LEU   B 1 153 ? 40.099 -26.780 -6.829  1.00 13.71 ?  153 LEU   B HD22 1 
ATOM   6211 H HD23 . LEU   B 1 153 ? 40.374 -25.403 -7.572  1.00 13.71 ?  153 LEU   B HD23 1 
ATOM   6212 N N    . ALA   B 1 154 ? 44.053 -27.165 -9.427  1.00 10.05 ?  154 ALA   B N    1 
ATOM   6213 C CA   . ALA   B 1 154 ? 45.283 -27.920 -9.612  1.00 10.79 ?  154 ALA   B CA   1 
ATOM   6214 C C    . ALA   B 1 154 ? 45.351 -28.998 -8.538  1.00 11.28 ?  154 ALA   B C    1 
ATOM   6215 O O    . ALA   B 1 154 ? 45.261 -28.702 -7.339  1.00 12.67 ?  154 ALA   B O    1 
ATOM   6216 C CB   . ALA   B 1 154 ? 46.506 -27.005 -9.543  1.00 12.12 ?  154 ALA   B CB   1 
ATOM   6217 H H    . ALA   B 1 154 ? 44.071 -26.640 -8.741  1.00 12.07 ?  154 ALA   B H    1 
ATOM   6218 H HA   . ALA   B 1 154 ? 45.274 -28.349 -10.478 1.00 12.96 ?  154 ALA   B HA   1 
ATOM   6219 H HB1  . ALA   B 1 154 ? 47.308 -27.535 -9.667  1.00 14.55 ?  154 ALA   B HB1  1 
ATOM   6220 H HB2  . ALA   B 1 154 ? 46.440 -26.334 -10.241 1.00 14.55 ?  154 ALA   B HB2  1 
ATOM   6221 H HB3  . ALA   B 1 154 ? 46.530 -26.571 -8.672  1.00 14.55 ?  154 ALA   B HB3  1 
ATOM   6222 N N    . VAL   B 1 155 ? 45.483 -30.244 -8.971  1.00 10.57 ?  155 VAL   B N    1 
ATOM   6223 C CA   . VAL   B 1 155 ? 45.587 -31.392 -8.078  1.00 10.61 ?  155 VAL   B CA   1 
ATOM   6224 C C    . VAL   B 1 155 ? 46.930 -32.060 -8.349  1.00 10.78 ?  155 VAL   B C    1 
ATOM   6225 O O    . VAL   B 1 155 ? 47.173 -32.555 -9.458  1.00 12.32 ?  155 VAL   B O    1 
ATOM   6226 C CB   . VAL   B 1 155 ? 44.433 -32.388 -8.288  1.00 12.14 ?  155 VAL   B CB   1 
ATOM   6227 C CG1  . VAL   B 1 155 ? 44.610 -33.600 -7.383  1.00 12.26 ?  155 VAL   B CG1  1 
ATOM   6228 C CG2  . VAL   B 1 155 ? 43.089 -31.711 -8.032  1.00 13.38 ?  155 VAL   B CG2  1 
ATOM   6229 H H    . VAL   B 1 155 ? 45.523 -30.460 -9.803  1.00 12.69 ?  155 VAL   B H    1 
ATOM   6230 H HA   . VAL   B 1 155 ? 45.571 -31.096 -7.155  1.00 12.74 ?  155 VAL   B HA   1 
ATOM   6231 H HB   . VAL   B 1 155 ? 44.445 -32.699 -9.207  1.00 14.58 ?  155 VAL   B HB   1 
ATOM   6232 H HG11 . VAL   B 1 155 ? 43.785 -34.107 -7.364  1.00 14.72 ?  155 VAL   B HG11 1 
ATOM   6233 H HG12 . VAL   B 1 155 ? 45.329 -34.158 -7.731  1.00 14.72 ?  155 VAL   B HG12 1 
ATOM   6234 H HG13 . VAL   B 1 155 ? 44.834 -33.299 -6.488  1.00 14.72 ?  155 VAL   B HG13 1 
ATOM   6235 H HG21 . VAL   B 1 155 ? 42.382 -32.367 -8.138  1.00 16.06 ?  155 VAL   B HG21 1 
ATOM   6236 H HG22 . VAL   B 1 155 ? 43.082 -31.360 -7.127  1.00 16.06 ?  155 VAL   B HG22 1 
ATOM   6237 H HG23 . VAL   B 1 155 ? 42.973 -30.992 -8.669  1.00 16.06 ?  155 VAL   B HG23 1 
ATOM   6238 N N    . PHE   B 1 156 ? 47.795 -32.098 -7.329  1.00 11.05 ?  156 PHE   B N    1 
ATOM   6239 C CA   . PHE   B 1 156 ? 49.175 -32.553 -7.518  1.00 12.13 ?  156 PHE   B CA   1 
ATOM   6240 C C    . PHE   B 1 156 ? 49.277 -34.052 -7.806  1.00 12.73 ?  156 PHE   B C    1 
ATOM   6241 O O    . PHE   B 1 156 ? 50.021 -34.470 -8.703  1.00 14.66 ?  156 PHE   B O    1 
ATOM   6242 C CB   . PHE   B 1 156 ? 49.997 -32.183 -6.285  1.00 12.55 ?  156 PHE   B CB   1 
ATOM   6243 C CG   . PHE   B 1 156 ? 51.422 -32.646 -6.340  1.00 13.33 ?  156 PHE   B CG   1 
ATOM   6244 C CD1  . PHE   B 1 156 ? 52.311 -32.085 -7.235  1.00 15.27 ?  156 PHE   B CD1  1 
ATOM   6245 C CD2  . PHE   B 1 156 ? 51.875 -33.627 -5.484  1.00 13.40 ?  156 PHE   B CD2  1 
ATOM   6246 C CE1  . PHE   B 1 156 ? 53.631 -32.491 -7.285  1.00 16.12 ?  156 PHE   B CE1  1 
ATOM   6247 C CE2  . PHE   B 1 156 ? 53.197 -34.042 -5.530  1.00 14.80 ?  156 PHE   B CE2  1 
ATOM   6248 C CZ   . PHE   B 1 156 ? 54.069 -33.472 -6.434  1.00 15.56 ?  156 PHE   B CZ   1 
ATOM   6249 H H    . PHE   B 1 156 ? 47.607 -31.868 -6.520  1.00 13.27 ?  156 PHE   B H    1 
ATOM   6250 H HA   . PHE   B 1 156 ? 49.554 -32.079 -8.272  1.00 14.56 ?  156 PHE   B HA   1 
ATOM   6251 H HB2  . PHE   B 1 156 ? 50.007 -31.219 -6.191  1.00 15.07 ?  156 PHE   B HB2  1 
ATOM   6252 H HB3  . PHE   B 1 156 ? 49.589 -32.586 -5.501  1.00 15.07 ?  156 PHE   B HB3  1 
ATOM   6253 H HD1  . PHE   B 1 156 ? 52.018 -31.413 -7.811  1.00 18.33 ?  156 PHE   B HD1  1 
ATOM   6254 H HD2  . PHE   B 1 156 ? 51.287 -34.017 -4.875  1.00 16.09 ?  156 PHE   B HD2  1 
ATOM   6255 H HE1  . PHE   B 1 156 ? 54.214 -32.098 -7.898  1.00 19.35 ?  156 PHE   B HE1  1 
ATOM   6256 H HE2  . PHE   B 1 156 ? 53.490 -34.712 -4.955  1.00 17.76 ?  156 PHE   B HE2  1 
ATOM   6257 H HZ   . PHE   B 1 156 ? 54.954 -33.751 -6.468  1.00 18.68 ?  156 PHE   B HZ   1 
ATOM   6258 N N    . ASP   B 1 157 ? 48.595 -34.877 -7.023  1.00 13.24 ?  157 ASP   B N    1 
ATOM   6259 C CA   . ASP   B 1 157 ? 48.748 -36.324 -7.117  1.00 14.50 ?  157 ASP   B CA   1 
ATOM   6260 C C    . ASP   B 1 157 ? 47.839 -36.868 -8.213  1.00 14.27 ?  157 ASP   B C    1 
ATOM   6261 O O    . ASP   B 1 157 ? 46.611 -36.751 -8.117  1.00 13.66 ?  157 ASP   B O    1 
ATOM   6262 C CB   . ASP   B 1 157 ? 48.375 -36.937 -5.775  1.00 16.11 ?  157 ASP   B CB   1 
ATOM   6263 C CG   . ASP   B 1 157 ? 48.531 -38.444 -5.749  1.00 17.66 ?  157 ASP   B CG   1 
ATOM   6264 O OD1  . ASP   B 1 157 ? 48.872 -39.055 -6.790  1.00 18.22 ?  157 ASP   B OD1  1 
ATOM   6265 O OD2  . ASP   B 1 157 ? 48.331 -39.022 -4.662  1.00 19.87 -1 157 ASP   B OD2  1 
ATOM   6266 H H    . ASP   B 1 157 ? 48.040 -34.624 -6.426  1.00 15.89 ?  157 ASP   B H    1 
ATOM   6267 H HA   . ASP   B 1 157 ? 49.671 -36.553 -7.325  1.00 17.41 ?  157 ASP   B HA   1 
ATOM   6268 H HB2  . ASP   B 1 157 ? 48.938 -36.556 -5.089  1.00 19.34 ?  157 ASP   B HB2  1 
ATOM   6269 H HB3  . ASP   B 1 157 ? 47.441 -36.733 -5.588  1.00 19.34 ?  157 ASP   B HB3  1 
ATOM   6270 N N    . LYS   B 1 158 ? 48.439 -37.483 -9.240  1.00 15.23 ?  158 LYS   B N    1 
ATOM   6271 C CA   . LYS   B 1 158 ? 47.666 -38.094 -10.324 1.00 16.19 ?  158 LYS   B CA   1 
ATOM   6272 C C    . LYS   B 1 158 ? 46.607 -39.062 -9.798  1.00 15.74 ?  158 LYS   B C    1 
ATOM   6273 O O    . LYS   B 1 158 ? 45.508 -39.156 -10.356 1.00 16.07 ?  158 LYS   B O    1 
ATOM   6274 C CB   . LYS   B 1 158 ? 48.618 -38.812 -11.291 1.00 17.73 ?  158 LYS   B CB   1 
ATOM   6275 C CG   . LYS   B 1 158 ? 47.948 -39.701 -12.333 1.00 19.60 ?  158 LYS   B CG   1 
ATOM   6276 C CD   . LYS   B 1 158 ? 47.091 -38.912 -13.300 1.00 21.79 ?  158 LYS   B CD   1 
ATOM   6277 C CE   . LYS   B 1 158 ? 46.488 -39.818 -14.362 1.00 23.39 ?  158 LYS   B CE   1 
ATOM   6278 N NZ   . LYS   B 1 158 ? 45.451 -39.117 -15.174 1.00 23.46 ?  158 LYS   B NZ   1 
ATOM   6279 H H    . LYS   B 1 158 ? 49.296 -37.561 -9.333  1.00 18.28 ?  158 LYS   B H    1 
ATOM   6280 H HA   . LYS   B 1 158 ? 47.217 -37.398 -10.825 1.00 19.44 ?  158 LYS   B HA   1 
ATOM   6281 H HB2  . LYS   B 1 158 ? 49.133 -38.143 -11.778 1.00 21.29 ?  158 LYS   B HB2  1 
ATOM   6282 H HB3  . LYS   B 1 158 ? 49.224 -39.370 -10.779 1.00 21.29 ?  158 LYS   B HB3  1 
ATOM   6283 H HG2  . LYS   B 1 158 ? 48.638 -40.154 -12.848 1.00 23.53 ?  158 LYS   B HG2  1 
ATOM   6284 H HG3  . LYS   B 1 158 ? 47.390 -40.363 -11.893 1.00 23.53 ?  158 LYS   B HG3  1 
ATOM   6285 H HD2  . LYS   B 1 158 ? 46.369 -38.485 -12.815 1.00 26.16 ?  158 LYS   B HD2  1 
ATOM   6286 H HD3  . LYS   B 1 158 ? 47.640 -38.247 -13.745 1.00 26.16 ?  158 LYS   B HD3  1 
ATOM   6287 H HE2  . LYS   B 1 158 ? 47.186 -40.120 -14.962 1.00 28.07 ?  158 LYS   B HE2  1 
ATOM   6288 H HE3  . LYS   B 1 158 ? 46.067 -40.581 -13.931 1.00 28.07 ?  158 LYS   B HE3  1 
ATOM   6289 H HZ1  . LYS   B 1 158 ? 45.114 -39.670 -15.784 1.00 28.16 ?  158 LYS   B HZ1  1 
ATOM   6290 H HZ2  . LYS   B 1 158 ? 44.791 -38.832 -14.647 1.00 28.16 ?  158 LYS   B HZ2  1 
ATOM   6291 H HZ3  . LYS   B 1 158 ? 45.812 -38.416 -15.587 1.00 28.16 ?  158 LYS   B HZ3  1 
ATOM   6292 N N    . ASN   B 1 159 ? 46.926 -39.819 -8.748  1.00 16.04 ?  159 ASN   B N    1 
ATOM   6293 C CA   . ASN   B 1 159 ? 45.970 -40.804 -8.251  1.00 16.67 ?  159 ASN   B CA   1 
ATOM   6294 C C    . ASN   B 1 159 ? 44.765 -40.135 -7.588  1.00 15.82 ?  159 ASN   B C    1 
ATOM   6295 O O    . ASN   B 1 159 ? 43.632 -40.621 -7.718  1.00 15.91 ?  159 ASN   B O    1 
ATOM   6296 C CB   . ASN   B 1 159 ? 46.665 -41.784 -7.314  1.00 18.35 ?  159 ASN   B CB   1 
ATOM   6297 C CG   . ASN   B 1 159 ? 47.708 -42.614 -8.025  1.00 20.37 ?  159 ASN   B CG   1 
ATOM   6298 O OD1  . ASN   B 1 159 ? 47.462 -43.134 -9.117  1.00 21.33 ?  159 ASN   B OD1  1 
ATOM   6299 N ND2  . ASN   B 1 159 ? 48.882 -42.739 -7.420  1.00 21.14 ?  159 ASN   B ND2  1 
ATOM   6300 H H    . ASN   B 1 159 ? 47.668 -39.776 -8.319  1.00 19.25 ?  159 ASN   B H    1 
ATOM   6301 H HA   . ASN   B 1 159 ? 45.636 -41.307 -9.010  1.00 20.02 ?  159 ASN   B HA   1 
ATOM   6302 H HB2  . ASN   B 1 159 ? 47.106 -41.295 -6.608  1.00 22.03 ?  159 ASN   B HB2  1 
ATOM   6303 H HB3  . ASN   B 1 159 ? 46.005 -42.390 -6.947  1.00 22.03 ?  159 ASN   B HB3  1 
ATOM   6304 H HD21 . ASN   B 1 159 ? 49.511 -43.206 -7.785  1.00 25.38 ?  159 ASN   B HD21 1 
ATOM   6305 H HD22 . ASN   B 1 159 ? 49.014 -42.372 -6.656  1.00 25.38 ?  159 ASN   B HD22 1 
ATOM   6306 N N    . LEU   B 1 160 ? 44.976 -39.007 -6.896  1.00 14.86 ?  160 LEU   B N    1 
ATOM   6307 C CA   . LEU   B 1 160 ? 43.841 -38.270 -6.352  1.00 13.63 ?  160 LEU   B CA   1 
ATOM   6308 C C    . LEU   B 1 160 ? 43.056 -37.602 -7.467  1.00 13.17 ?  160 LEU   B C    1 
ATOM   6309 O O    . LEU   B 1 160 ? 41.819 -37.612 -7.459  1.00 12.67 ?  160 LEU   B O    1 
ATOM   6310 C CB   . LEU   B 1 160 ? 44.299 -37.241 -5.320  1.00 13.28 ?  160 LEU   B CB   1 
ATOM   6311 C CG   . LEU   B 1 160 ? 43.171 -36.352 -4.770  1.00 13.26 ?  160 LEU   B CG   1 
ATOM   6312 C CD1  . LEU   B 1 160 ? 42.045 -37.177 -4.157  1.00 13.71 ?  160 LEU   B CD1  1 
ATOM   6313 C CD2  . LEU   B 1 160 ? 43.716 -35.362 -3.753  1.00 13.81 ?  160 LEU   B CD2  1 
ATOM   6314 H H    . LEU   B 1 160 ? 45.751 -38.654 -6.741  1.00 17.84 ?  160 LEU   B H    1 
ATOM   6315 H HA   . LEU   B 1 160 ? 43.254 -38.896 -5.911  1.00 16.37 ?  160 LEU   B HA   1 
ATOM   6316 H HB2  . LEU   B 1 160 ? 44.702 -37.710 -4.569  1.00 15.95 ?  160 LEU   B HB2  1 
ATOM   6317 H HB3  . LEU   B 1 160 ? 44.964 -36.659 -5.729  1.00 15.95 ?  160 LEU   B HB3  1 
ATOM   6318 H HG   . LEU   B 1 160 ? 42.799 -35.838 -5.500  1.00 15.92 ?  160 LEU   B HG   1 
ATOM   6319 H HD11 . LEU   B 1 160 ? 41.410 -36.577 -3.741  1.00 16.47 ?  160 LEU   B HD11 1 
ATOM   6320 H HD12 . LEU   B 1 160 ? 41.612 -37.689 -4.857  1.00 16.47 ?  160 LEU   B HD12 1 
ATOM   6321 H HD13 . LEU   B 1 160 ? 42.421 -37.777 -3.491  1.00 16.47 ?  160 LEU   B HD13 1 
ATOM   6322 H HD21 . LEU   B 1 160 ? 42.990 -34.798 -3.443  1.00 16.59 ?  160 LEU   B HD21 1 
ATOM   6323 H HD22 . LEU   B 1 160 ? 44.096 -35.851 -3.006  1.00 16.59 ?  160 LEU   B HD22 1 
ATOM   6324 H HD23 . LEU   B 1 160 ? 44.401 -34.817 -4.174  1.00 16.59 ?  160 LEU   B HD23 1 
ATOM   6325 N N    . TYR   B 1 161 ? 43.758 -37.026 -8.444  1.00 13.28 ?  161 TYR   B N    1 
ATOM   6326 C CA   . TYR   B 1 161 ? 43.086 -36.465 -9.610  1.00 13.06 ?  161 TYR   B CA   1 
ATOM   6327 C C    . TYR   B 1 161 ? 42.146 -37.488 -10.236 1.00 12.97 ?  161 TYR   B C    1 
ATOM   6328 O O    . TYR   B 1 161 ? 40.977 -37.191 -10.507 1.00 12.75 ?  161 TYR   B O    1 
ATOM   6329 C CB   . TYR   B 1 161 ? 44.132 -35.985 -10.622 1.00 13.70 ?  161 TYR   B CB   1 
ATOM   6330 C CG   . TYR   B 1 161 ? 43.560 -35.517 -11.935 1.00 14.21 ?  161 TYR   B CG   1 
ATOM   6331 C CD1  . TYR   B 1 161 ? 43.156 -34.200 -12.102 1.00 14.08 ?  161 TYR   B CD1  1 
ATOM   6332 C CD2  . TYR   B 1 161 ? 43.407 -36.389 -13.006 1.00 15.06 ?  161 TYR   B CD2  1 
ATOM   6333 C CE1  . TYR   B 1 161 ? 42.623 -33.766 -13.290 1.00 15.15 ?  161 TYR   B CE1  1 
ATOM   6334 C CE2  . TYR   B 1 161 ? 42.872 -35.962 -14.199 1.00 15.96 ?  161 TYR   B CE2  1 
ATOM   6335 C CZ   . TYR   B 1 161 ? 42.483 -34.649 -14.337 1.00 15.85 ?  161 TYR   B CZ   1 
ATOM   6336 O OH   . TYR   B 1 161 ? 41.950 -34.201 -15.518 1.00 17.63 ?  161 TYR   B OH   1 
ATOM   6337 H H    . TYR   B 1 161 ? 44.614 -36.961 -8.464  1.00 15.95 ?  161 TYR   B H    1 
ATOM   6338 H HA   . TYR   B 1 161 ? 42.557 -35.703 -9.340  1.00 15.68 ?  161 TYR   B HA   1 
ATOM   6339 H HB2  . TYR   B 1 161 ? 44.624 -35.241 -10.234 1.00 16.45 ?  161 TYR   B HB2  1 
ATOM   6340 H HB3  . TYR   B 1 161 ? 44.745 -36.712 -10.815 1.00 16.45 ?  161 TYR   B HB3  1 
ATOM   6341 H HD1  . TYR   B 1 161 ? 43.252 -33.593 -11.398 1.00 16.90 ?  161 TYR   B HD1  1 
ATOM   6342 H HD2  . TYR   B 1 161 ? 43.667 -37.274 -12.918 1.00 18.09 ?  161 TYR   B HD2  1 
ATOM   6343 H HE1  . TYR   B 1 161 ? 42.364 -32.872 -13.383 1.00 18.19 ?  161 TYR   B HE1  1 
ATOM   6344 H HE2  . TYR   B 1 161 ? 42.776 -36.549 -14.910 1.00 19.17 ?  161 TYR   B HE2  1 
ATOM   6345 H HH   . TYR   B 1 161 ? 41.918 -34.832 -16.071 1.00 21.17 ?  161 TYR   B HH   1 
ATOM   6346 N N    . ASP   B 1 162 ? 42.645 -38.709 -10.461 1.00 13.58 ?  162 ASP   B N    1 
ATOM   6347 C CA   . ASP   B 1 162 ? 41.825 -39.749 -11.078 1.00 14.34 ?  162 ASP   B CA   1 
ATOM   6348 C C    . ASP   B 1 162 ? 40.610 -40.085 -10.220 1.00 13.86 ?  162 ASP   B C    1 
ATOM   6349 O O    . ASP   B 1 162 ? 39.512 -40.299 -10.746 1.00 14.14 ?  162 ASP   B O    1 
ATOM   6350 C CB   . ASP   B 1 162 ? 42.659 -41.010 -11.333 1.00 16.26 ?  162 ASP   B CB   1 
ATOM   6351 C CG   . ASP   B 1 162 ? 43.654 -40.845 -12.470 1.00 17.41 ?  162 ASP   B CG   1 
ATOM   6352 O OD1  . ASP   B 1 162 ? 43.512 -39.901 -13.275 1.00 17.66 ?  162 ASP   B OD1  1 
ATOM   6353 O OD2  . ASP   B 1 162 ? 44.572 -41.687 -12.572 1.00 19.27 -1 162 ASP   B OD2  1 
ATOM   6354 H H    . ASP   B 1 162 ? 43.444 -38.958 -10.263 1.00 16.31 ?  162 ASP   B H    1 
ATOM   6355 H HA   . ASP   B 1 162 ? 41.503 -39.428 -11.932 1.00 17.21 ?  162 ASP   B HA   1 
ATOM   6356 H HB2  . ASP   B 1 162 ? 43.161 -41.222 -10.530 1.00 19.52 ?  162 ASP   B HB2  1 
ATOM   6357 H HB3  . ASP   B 1 162 ? 42.066 -41.739 -11.560 1.00 19.52 ?  162 ASP   B HB3  1 
ATOM   6358 N N    A LYS   B 1 163 ? 40.788 -40.159 -8.901  0.86 13.28 ?  163 LYS   B N    1 
ATOM   6359 N N    B LYS   B 1 163 ? 40.784 -40.142 -8.897  0.14 14.60 ?  163 LYS   B N    1 
ATOM   6360 C CA   A LYS   B 1 163 ? 39.661 -40.439 -8.019  0.86 13.57 ?  163 LYS   B CA   1 
ATOM   6361 C CA   B LYS   B 1 163 ? 39.653 -40.444 -8.024  0.14 15.57 ?  163 LYS   B CA   1 
ATOM   6362 C C    A LYS   B 1 163 ? 38.616 -39.334 -8.095  0.86 12.71 ?  163 LYS   B C    1 
ATOM   6363 C C    B LYS   B 1 163 ? 38.615 -39.329 -8.059  0.14 13.72 ?  163 LYS   B C    1 
ATOM   6364 O O    A LYS   B 1 163 ? 37.408 -39.607 -8.130  0.86 13.73 ?  163 LYS   B O    1 
ATOM   6365 O O    B LYS   B 1 163 ? 37.407 -39.593 -8.018  0.14 13.79 ?  163 LYS   B O    1 
ATOM   6366 C CB   A LYS   B 1 163 ? 40.144 -40.617 -6.582  0.86 16.01 ?  163 LYS   B CB   1 
ATOM   6367 C CB   B LYS   B 1 163 ? 40.140 -40.674 -6.593  0.14 18.48 ?  163 LYS   B CB   1 
ATOM   6368 C CG   A LYS   B 1 163 ? 39.049 -41.123 -5.663  0.86 20.63 ?  163 LYS   B CG   1 
ATOM   6369 C CG   B LYS   B 1 163 ? 39.048 -41.162 -5.659  0.14 21.26 ?  163 LYS   B CG   1 
ATOM   6370 C CD   A LYS   B 1 163 ? 39.478 -41.195 -4.211  0.86 24.60 ?  163 LYS   B CD   1 
ATOM   6371 C CD   B LYS   B 1 163 ? 39.537 -41.327 -4.234  0.14 23.99 ?  163 LYS   B CD   1 
ATOM   6372 C CE   A LYS   B 1 163 ? 38.402 -41.886 -3.385  0.86 27.25 ?  163 LYS   B CE   1 
ATOM   6373 C CE   B LYS   B 1 163 ? 38.487 -42.034 -3.392  0.14 26.13 ?  163 LYS   B CE   1 
ATOM   6374 N NZ   A LYS   B 1 163 ? 38.454 -41.521 -1.942  0.86 28.96 ?  163 LYS   B NZ   1 
ATOM   6375 N NZ   B LYS   B 1 163 ? 38.511 -41.598 -1.970  0.14 26.79 ?  163 LYS   B NZ   1 
ATOM   6376 H H    A LYS   B 1 163 ? 41.543 -40.049 -8.500  0.86 15.94 ?  163 LYS   B H    1 
ATOM   6377 H H    B LYS   B 1 163 ? 41.531 -40.017 -8.490  0.14 17.53 ?  163 LYS   B H    1 
ATOM   6378 H HA   A LYS   B 1 163 ? 39.244 -41.266 -8.300  0.86 16.29 ?  163 LYS   B HA   1 
ATOM   6379 H HA   B LYS   B 1 163 ? 39.227 -41.259 -8.329  0.14 18.70 ?  163 LYS   B HA   1 
ATOM   6380 H HB2  A LYS   B 1 163 ? 40.870 -41.263 -6.569  0.86 19.22 ?  163 LYS   B HB2  1 
ATOM   6381 H HB2  B LYS   B 1 163 ? 40.842 -41.344 -6.603  0.14 22.18 ?  163 LYS   B HB2  1 
ATOM   6382 H HB3  A LYS   B 1 163 ? 40.453 -39.765 -6.241  0.86 19.22 ?  163 LYS   B HB3  1 
ATOM   6383 H HB3  B LYS   B 1 163 ? 40.484 -39.840 -6.238  0.14 22.18 ?  163 LYS   B HB3  1 
ATOM   6384 H HG2  A LYS   B 1 163 ? 38.286 -40.528 -5.717  0.86 24.76 ?  163 LYS   B HG2  1 
ATOM   6385 H HG2  B LYS   B 1 163 ? 38.323 -40.517 -5.652  0.14 25.52 ?  163 LYS   B HG2  1 
ATOM   6386 H HG3  A LYS   B 1 163 ? 38.791 -42.018 -5.942  0.86 24.76 ?  163 LYS   B HG3  1 
ATOM   6387 H HG3  B LYS   B 1 163 ? 38.726 -42.022 -5.969  0.14 25.52 ?  163 LYS   B HG3  1 
ATOM   6388 H HD2  A LYS   B 1 163 ? 40.299 -41.708 -4.139  0.86 29.53 ?  163 LYS   B HD2  1 
ATOM   6389 H HD2  B LYS   B 1 163 ? 40.347 -41.862 -4.230  0.14 28.80 ?  163 LYS   B HD2  1 
ATOM   6390 H HD3  A LYS   B 1 163 ? 39.606 -40.298 -3.865  0.86 29.53 ?  163 LYS   B HD3  1 
ATOM   6391 H HD3  B LYS   B 1 163 ? 39.706 -40.454 -3.845  0.14 28.80 ?  163 LYS   B HD3  1 
ATOM   6392 H HE2  A LYS   B 1 163 ? 37.528 -41.647 -3.731  0.86 32.71 ?  163 LYS   B HE2  1 
ATOM   6393 H HE2  B LYS   B 1 163 ? 37.608 -41.841 -3.755  0.14 31.36 ?  163 LYS   B HE2  1 
ATOM   6394 H HE3  A LYS   B 1 163 ? 38.527 -42.845 -3.452  0.86 32.71 ?  163 LYS   B HE3  1 
ATOM   6395 H HE3  B LYS   B 1 163 ? 38.653 -42.990 -3.418  0.14 31.36 ?  163 LYS   B HE3  1 
ATOM   6396 H HZ1  A LYS   B 1 163 ? 37.808 -41.945 -1.499  0.86 34.76 ?  163 LYS   B HZ1  1 
ATOM   6397 H HZ1  B LYS   B 1 163 ? 37.884 -42.031 -1.510  0.14 32.15 ?  163 LYS   B HZ1  1 
ATOM   6398 H HZ2  A LYS   B 1 163 ? 39.241 -41.752 -1.599  0.86 34.76 ?  163 LYS   B HZ2  1 
ATOM   6399 H HZ2  B LYS   B 1 163 ? 39.306 -41.772 -1.612  0.14 32.15 ?  163 LYS   B HZ2  1 
ATOM   6400 H HZ3  A LYS   B 1 163 ? 38.342 -40.643 -1.847  0.86 34.76 ?  163 LYS   B HZ3  1 
ATOM   6401 H HZ3  B LYS   B 1 163 ? 38.354 -40.723 -1.919  0.14 32.15 ?  163 LYS   B HZ3  1 
ATOM   6402 N N    . LEU   B 1 164 ? 39.069 -38.078 -8.135  1.00 12.03 ?  164 LEU   B N    1 
ATOM   6403 C CA   . LEU   B 1 164 ? 38.154 -36.942 -8.183  1.00 11.71 ?  164 LEU   B CA   1 
ATOM   6404 C C    . LEU   B 1 164 ? 37.375 -36.914 -9.492  1.00 11.88 ?  164 LEU   B C    1 
ATOM   6405 O O    . LEU   B 1 164 ? 36.153 -36.718 -9.495  1.00 12.98 ?  164 LEU   B O    1 
ATOM   6406 C CB   . LEU   B 1 164 ? 38.949 -35.644 -8.015  1.00 11.23 ?  164 LEU   B CB   1 
ATOM   6407 C CG   . LEU   B 1 164 ? 39.473 -35.353 -6.614  1.00 12.18 ?  164 LEU   B CG   1 
ATOM   6408 C CD1  . LEU   B 1 164 ? 40.570 -34.305 -6.676  1.00 12.28 ?  164 LEU   B CD1  1 
ATOM   6409 C CD2  . LEU   B 1 164 ? 38.351 -34.896 -5.704  1.00 13.95 ?  164 LEU   B CD2  1 
ATOM   6410 H H    A LEU   B 1 164 ? 39.902 -37.858 -8.138  0.86 14.45 ?  164 LEU   B H    1 
ATOM   6411 H H    B LEU   B 1 164 ? 39.902 -37.861 -8.165  0.14 14.45 ?  164 LEU   B H    1 
ATOM   6412 H HA   . LEU   B 1 164 ? 37.521 -37.006 -7.457  1.00 14.06 ?  164 LEU   B HA   1 
ATOM   6413 H HB2  . LEU   B 1 164 ? 39.718 -35.679 -8.610  1.00 13.48 ?  164 LEU   B HB2  1 
ATOM   6414 H HB3  . LEU   B 1 164 ? 38.382 -34.902 -8.272  1.00 13.48 ?  164 LEU   B HB3  1 
ATOM   6415 H HG   . LEU   B 1 164 ? 39.859 -36.157 -6.244  1.00 14.63 ?  164 LEU   B HG   1 
ATOM   6416 H HD11 . LEU   B 1 164 ? 40.887 -34.120 -5.777  1.00 14.74 ?  164 LEU   B HD11 1 
ATOM   6417 H HD12 . LEU   B 1 164 ? 41.306 -34.642 -7.217  1.00 14.74 ?  164 LEU   B HD12 1 
ATOM   6418 H HD13 . LEU   B 1 164 ? 40.219 -33.492 -7.075  1.00 14.74 ?  164 LEU   B HD13 1 
ATOM   6419 H HD21 . LEU   B 1 164 ? 38.718 -34.678 -4.833  1.00 16.75 ?  164 LEU   B HD21 1 
ATOM   6420 H HD22 . LEU   B 1 164 ? 37.928 -34.112 -6.089  1.00 16.75 ?  164 LEU   B HD22 1 
ATOM   6421 H HD23 . LEU   B 1 164 ? 37.705 -35.614 -5.621  1.00 16.75 ?  164 LEU   B HD23 1 
ATOM   6422 N N    . VAL   B 1 165 ? 38.067 -37.080 -10.620 1.00 13.01 ?  165 VAL   B N    1 
ATOM   6423 C CA   . VAL   B 1 165 ? 37.407 -37.020 -11.921 1.00 13.81 ?  165 VAL   B CA   1 
ATOM   6424 C C    . VAL   B 1 165 ? 36.488 -38.222 -12.106 1.00 15.26 ?  165 VAL   B C    1 
ATOM   6425 O O    . VAL   B 1 165 ? 35.329 -38.087 -12.515 1.00 16.03 ?  165 VAL   B O    1 
ATOM   6426 C CB   . VAL   B 1 165 ? 38.451 -36.926 -13.050 1.00 14.61 ?  165 VAL   B CB   1 
ATOM   6427 C CG1  . VAL   B 1 165 ? 37.780 -37.014 -14.406 1.00 15.69 ?  165 VAL   B CG1  1 
ATOM   6428 C CG2  . VAL   B 1 165 ? 39.255 -35.645 -12.930 1.00 14.81 ?  165 VAL   B CG2  1 
ATOM   6429 H H    . VAL   B 1 165 ? 38.917 -37.215 -10.658 1.00 15.62 ?  165 VAL   B H    1 
ATOM   6430 H HA   . VAL   B 1 165 ? 36.862 -36.218 -11.961 1.00 16.59 ?  165 VAL   B HA   1 
ATOM   6431 H HB   . VAL   B 1 165 ? 39.069 -37.669 -12.971 1.00 17.54 ?  165 VAL   B HB   1 
ATOM   6432 H HG11 . VAL   B 1 165 ? 38.406 -36.724 -15.085 1.00 18.83 ?  165 VAL   B HG11 1 
ATOM   6433 H HG12 . VAL   B 1 165 ? 37.521 -37.935 -14.568 1.00 18.83 ?  165 VAL   B HG12 1 
ATOM   6434 H HG13 . VAL   B 1 165 ? 36.999 -36.443 -14.406 1.00 18.83 ?  165 VAL   B HG13 1 
ATOM   6435 H HG21 . VAL   B 1 165 ? 39.886 -35.595 -13.667 1.00 17.78 ?  165 VAL   B HG21 1 
ATOM   6436 H HG22 . VAL   B 1 165 ? 38.651 -34.886 -12.963 1.00 17.78 ?  165 VAL   B HG22 1 
ATOM   6437 H HG23 . VAL   B 1 165 ? 39.735 -35.648 -12.086 1.00 17.78 ?  165 VAL   B HG23 1 
ATOM   6438 N N    . SER   B 1 166 ? 36.997 -39.418 -11.800 1.00 15.99 ?  166 SER   B N    1 
ATOM   6439 C CA   . SER   B 1 166 ? 36.241 -40.630 -12.079 1.00 17.18 ?  166 SER   B CA   1 
ATOM   6440 C C    . SER   B 1 166 ? 34.980 -40.716 -11.232 1.00 17.50 ?  166 SER   B C    1 
ATOM   6441 O O    . SER   B 1 166 ? 34.008 -41.337 -11.660 1.00 19.06 ?  166 SER   B O    1 
ATOM   6442 C CB   . SER   B 1 166 ? 37.106 -41.883 -11.902 1.00 18.22 ?  166 SER   B CB   1 
ATOM   6443 O OG   . SER   B 1 166 ? 37.478 -42.087 -10.551 1.00 18.55 ?  166 SER   B OG   1 
ATOM   6444 H H    . SER   B 1 166 ? 37.771 -39.547 -11.444 1.00 19.20 ?  166 SER   B H    1 
ATOM   6445 H HA   . SER   B 1 166 ? 35.963 -40.605 -13.007 1.00 20.62 ?  166 SER   B HA   1 
ATOM   6446 H HB2  . SER   B 1 166 ? 36.598 -42.653 -12.205 1.00 21.88 ?  166 SER   B HB2  1 
ATOM   6447 H HB3  . SER   B 1 166 ? 37.905 -41.788 -12.445 1.00 21.88 ?  166 SER   B HB3  1 
ATOM   6448 H HG   . SER   B 1 166 ? 37.933 -41.431 -10.282 1.00 22.27 ?  166 SER   B HG   1 
ATOM   6449 N N    . SER   B 1 167 ? 34.960 -40.106 -10.047 1.00 16.58 ?  167 SER   B N    1 
ATOM   6450 C CA   . SER   B 1 167 ? 33.804 -40.170 -9.161  1.00 15.99 ?  167 SER   B CA   1 
ATOM   6451 C C    . SER   B 1 167 ? 32.882 -38.954 -9.265  1.00 15.83 ?  167 SER   B C    1 
ATOM   6452 O O    . SER   B 1 167 ? 31.809 -38.950 -8.650  1.00 15.94 ?  167 SER   B O    1 
ATOM   6453 C CB   . SER   B 1 167 ? 34.252 -40.352 -7.705  1.00 15.81 ?  167 SER   B CB   1 
ATOM   6454 O OG   . SER   B 1 167 ? 34.916 -39.195 -7.218  1.00 15.44 ?  167 SER   B OG   1 
ATOM   6455 H H    . SER   B 1 167 ? 35.611 -39.641 -9.737  1.00 19.90 ?  167 SER   B H    1 
ATOM   6456 H HA   . SER   B 1 167 ? 33.279 -40.950 -9.402  1.00 19.20 ?  167 SER   B HA   1 
ATOM   6457 H HB2  . SER   B 1 167 ? 33.469 -40.524 -7.157  1.00 18.98 ?  167 SER   B HB2  1 
ATOM   6458 H HB3  . SER   B 1 167 ? 34.855 -41.115 -7.659  1.00 18.98 ?  167 SER   B HB3  1 
ATOM   6459 H HG   . SER   B 1 167 ? 35.601 -39.048 -7.684  1.00 18.54 ?  167 SER   B HG   1 
ATOM   6460 N N    . PHE   B 1 168 ? 33.259 -37.925 -10.027 1.00 15.65 ?  168 PHE   B N    1 
ATOM   6461 C CA   . PHE   B 1 168 ? 32.432 -36.720 -10.086 1.00 15.29 ?  168 PHE   B CA   1 
ATOM   6462 C C    . PHE   B 1 168 ? 31.106 -36.975 -10.798 1.00 13.50 ?  168 PHE   B C    1 
ATOM   6463 O O    . PHE   B 1 168 ? 30.078 -36.365 -10.454 1.00 14.23 ?  168 PHE   B O    1 
ATOM   6464 C CB   . PHE   B 1 168 ? 33.194 -35.594 -10.781 1.00 15.78 ?  168 PHE   B CB   1 
ATOM   6465 C CG   . PHE   B 1 168 ? 32.406 -34.330 -10.888 1.00 15.88 ?  168 PHE   B CG   1 
ATOM   6466 C CD1  . PHE   B 1 168 ? 32.113 -33.592 -9.752  1.00 17.07 ?  168 PHE   B CD1  1 
ATOM   6467 C CD2  . PHE   B 1 168 ? 31.931 -33.891 -12.108 1.00 15.51 ?  168 PHE   B CD2  1 
ATOM   6468 C CE1  . PHE   B 1 168 ? 31.368 -32.433 -9.830  1.00 18.04 ?  168 PHE   B CE1  1 
ATOM   6469 C CE2  . PHE   B 1 168 ? 31.190 -32.720 -12.198 1.00 16.45 ?  168 PHE   B CE2  1 
ATOM   6470 C CZ   . PHE   B 1 168 ? 30.908 -31.992 -11.056 1.00 17.12 ?  168 PHE   B CZ   1 
ATOM   6471 H H    . PHE   B 1 168 ? 33.975 -37.898 -10.501 1.00 18.79 ?  168 PHE   B H    1 
ATOM   6472 H HA   . PHE   B 1 168 ? 32.230 -36.432 -9.186  1.00 18.35 ?  168 PHE   B HA   1 
ATOM   6473 H HB2  . PHE   B 1 168 ? 33.997 -35.397 -10.271 1.00 18.95 ?  168 PHE   B HB2  1 
ATOM   6474 H HB3  . PHE   B 1 168 ? 33.429 -35.872 -11.677 1.00 18.95 ?  168 PHE   B HB3  1 
ATOM   6475 H HD1  . PHE   B 1 168 ? 32.418 -33.885 -8.924  1.00 20.50 ?  168 PHE   B HD1  1 
ATOM   6476 H HD2  . PHE   B 1 168 ? 32.118 -34.376 -12.878 1.00 18.62 ?  168 PHE   B HD2  1 
ATOM   6477 H HE1  . PHE   B 1 168 ? 31.181 -31.944 -9.061  1.00 21.66 ?  168 PHE   B HE1  1 
ATOM   6478 H HE2  . PHE   B 1 168 ? 30.876 -32.429 -13.027 1.00 19.75 ?  168 PHE   B HE2  1 
ATOM   6479 H HZ   . PHE   B 1 168 ? 30.406 -31.210 -11.117 1.00 20.55 ?  168 PHE   B HZ   1 
ATOM   6480 N N    . LEU   B 1 169 ? 31.116 -37.875 -11.779 1.00 14.18 ?  169 LEU   B N    1 
ATOM   6481 C CA   . LEU   B 1 169 ? 29.932 -38.173 -12.573 1.00 16.67 ?  169 LEU   B CA   1 
ATOM   6482 C C    . LEU   B 1 169 ? 29.943 -39.606 -13.095 1.00 19.37 ?  169 LEU   B C    1 
ATOM   6483 O O    . LEU   B 1 169 ? 29.037 -40.033 -13.814 1.00 22.04 ?  169 LEU   B O    1 
ATOM   6484 C CB   . LEU   B 1 169 ? 29.840 -37.198 -13.747 1.00 18.42 ?  169 LEU   B CB   1 
ATOM   6485 C CG   . LEU   B 1 169 ? 28.557 -36.372 -13.845 1.00 21.54 ?  169 LEU   B CG   1 
ATOM   6486 C CD1  . LEU   B 1 169 ? 28.523 -35.634 -15.170 1.00 22.81 ?  169 LEU   B CD1  1 
ATOM   6487 C CD2  . LEU   B 1 169 ? 27.325 -37.244 -13.680 1.00 21.88 ?  169 LEU   B CD2  1 
ATOM   6488 O OXT  . LEU   B 1 169 ? 30.867 -40.365 -12.815 1.00 20.01 -1 169 LEU   B OXT  1 
ATOM   6489 H H    . LEU   B 1 169 ? 31.815 -38.330 -12.017 1.00 17.02 ?  169 LEU   B H    1 
ATOM   6490 H HA   . LEU   B 1 169 ? 29.153 -38.059 -12.013 1.00 20.01 ?  169 LEU   B HA   1 
ATOM   6491 H HB2  . LEU   B 1 169 ? 30.579 -36.571 -13.685 1.00 22.11 ?  169 LEU   B HB2  1 
ATOM   6492 H HB3  . LEU   B 1 169 ? 29.917 -37.703 -14.571 1.00 22.11 ?  169 LEU   B HB3  1 
ATOM   6493 H HG   . LEU   B 1 169 ? 28.553 -35.709 -13.136 1.00 25.85 ?  169 LEU   B HG   1 
ATOM   6494 H HD11 . LEU   B 1 169 ? 27.714 -35.101 -15.213 1.00 27.38 ?  169 LEU   B HD11 1 
ATOM   6495 H HD12 . LEU   B 1 169 ? 29.302 -35.061 -15.231 1.00 27.38 ?  169 LEU   B HD12 1 
ATOM   6496 H HD13 . LEU   B 1 169 ? 28.532 -36.283 -15.890 1.00 27.38 ?  169 LEU   B HD13 1 
ATOM   6497 H HD21 . LEU   B 1 169 ? 26.558 -36.784 -14.051 1.00 26.27 ?  169 LEU   B HD21 1 
ATOM   6498 H HD22 . LEU   B 1 169 ? 27.468 -38.083 -14.147 1.00 26.27 ?  169 LEU   B HD22 1 
ATOM   6499 H HD23 . LEU   B 1 169 ? 27.187 -37.412 -12.736 1.00 26.27 ?  169 LEU   B HD23 1 
HETATM 6500 C C3   B A1A5B C 2 .   ? 14.698 -0.971  1.663   0.14 13.58 ?  201 A1A5B A C3   1 
HETATM 6501 C C6   B A1A5B C 2 .   ? 16.602 -0.059  0.639   0.14 13.50 ?  201 A1A5B A C6   1 
HETATM 6502 C C9   B A1A5B C 2 .   ? 15.167 3.840   5.849   0.14 14.62 ?  201 A1A5B A C9   1 
HETATM 6503 C C12  B A1A5B C 2 .   ? 15.329 5.688   4.284   0.14 14.23 ?  201 A1A5B A C12  1 
HETATM 6504 C C1   B A1A5B C 2 .   ? 15.766 2.476   2.297   0.14 13.84 ?  201 A1A5B A C1   1 
HETATM 6505 C C10  B A1A5B C 2 .   ? 15.156 5.216   5.566   0.14 14.40 ?  201 A1A5B A C10  1 
HETATM 6506 C C11  B A1A5B C 2 .   ? 14.942 7.406   5.595   0.14 14.32 ?  201 A1A5B A C11  1 
HETATM 6507 C C13  B A1A5B C 2 .   ? 15.531 4.817   3.204   0.14 14.19 ?  201 A1A5B A C13  1 
HETATM 6508 C C2   B A1A5B C 2 .   ? 15.570 0.083   1.621   0.14 13.68 ?  201 A1A5B A C2   1 
HETATM 6509 C C4   B A1A5B C 2 .   ? 13.505 -1.248  2.493   0.14 13.24 ?  201 A1A5B A C4   1 
HETATM 6510 C C5   B A1A5B C 2 .   ? 16.502 -1.227  -0.063  0.14 13.49 ?  201 A1A5B A C5   1 
HETATM 6511 C C7   B A1A5B C 2 .   ? 15.543 3.422   3.446   0.14 14.07 ?  201 A1A5B A C7   1 
HETATM 6512 C C8   B A1A5B C 2 .   ? 15.370 2.943   4.776   0.14 14.31 ?  201 A1A5B A C8   1 
HETATM 6513 N N1   B A1A5B C 2 .   ? 15.439 1.188   2.507   0.14 13.76 ?  201 A1A5B A N1   1 
HETATM 6514 O O1   B A1A5B C 2 .   ? 16.229 2.912   1.242   0.14 13.82 ?  201 A1A5B A O1   1 
HETATM 6515 O O2   B A1A5B C 2 .   ? 13.353 -0.596  3.548   0.14 12.71 ?  201 A1A5B A O2   1 
HETATM 6516 O O3   B A1A5B C 2 .   ? 14.982 6.264   6.410   0.14 14.39 ?  201 A1A5B A O3   1 
HETATM 6517 O O4   B A1A5B C 2 .   ? 15.272 7.044   4.279   0.14 14.11 ?  201 A1A5B A O4   1 
HETATM 6518 O O5   B A1A5B C 2 .   ? 12.689 -2.107  2.101   0.14 13.59 ?  201 A1A5B A O5   1 
HETATM 6519 S S1   B A1A5B C 2 .   ? 15.142 -2.174  0.470   0.14 13.56 ?  201 A1A5B A S1   1 
HETATM 6520 H H3   B A1A5B C 2 .   ? 17.374 0.671   0.470   0.14 16.21 ?  201 A1A5B A H3   1 
HETATM 6521 H H5   B A1A5B C 2 .   ? 15.028 3.476   6.855   0.14 17.56 ?  201 A1A5B A H5   1 
HETATM 6522 H H7   B A1A5B C 2 .   ? 13.939 7.836   5.614   0.14 17.19 ?  201 A1A5B A H7   1 
HETATM 6523 H H6   B A1A5B C 2 .   ? 15.650 8.148   5.964   0.14 17.19 ?  201 A1A5B A H6   1 
HETATM 6524 H H8   B A1A5B C 2 .   ? 15.668 5.219   2.215   0.14 17.04 ?  201 A1A5B A H8   1 
HETATM 6525 H H2   B A1A5B C 2 .   ? 17.138 -1.586  -0.856  0.14 16.19 ?  201 A1A5B A H2   1 
HETATM 6526 H H4   B A1A5B C 2 .   ? 15.381 1.879   4.979   0.14 17.18 ?  201 A1A5B A H4   1 
HETATM 6527 H H1   B A1A5B C 2 .   ? 15.078 0.950   3.424   0.14 16.52 ?  201 A1A5B A H1   1 
HETATM 6528 O O    . HOH   D 3 .   ? 26.855 11.394  1.683   1.00 14.67 ?  301 HOH   A O    1 
HETATM 6529 O O    . HOH   D 3 .   ? 6.975  -8.179  12.008  1.00 19.34 ?  302 HOH   A O    1 
HETATM 6530 O O    . HOH   D 3 .   ? 7.614  -6.334  -6.455  1.00 38.38 ?  303 HOH   A O    1 
HETATM 6531 O O    . HOH   D 3 .   ? 4.715  3.967   0.769   1.00 23.36 ?  304 HOH   A O    1 
HETATM 6532 O O    . HOH   D 3 .   ? 34.460 -1.929  12.489  1.00 37.05 ?  305 HOH   A O    1 
HETATM 6533 O O    . HOH   D 3 .   ? 10.579 -22.260 -1.142  1.00 43.13 ?  306 HOH   A O    1 
HETATM 6534 O O    . HOH   D 3 .   ? 11.136 1.558   12.990  1.00 22.28 ?  307 HOH   A O    1 
HETATM 6535 O O    . HOH   D 3 .   ? 14.894 -4.694  20.601  1.00 38.49 ?  308 HOH   A O    1 
HETATM 6536 O O    . HOH   D 3 .   ? 28.307 -6.413  19.596  1.00 40.80 ?  309 HOH   A O    1 
HETATM 6537 O O    . HOH   D 3 .   ? 28.900 0.458   -9.742  1.00 19.18 ?  310 HOH   A O    1 
HETATM 6538 O O    . HOH   D 3 .   ? 26.960 4.157   -0.632  1.00 11.40 ?  311 HOH   A O    1 
HETATM 6539 O O    . HOH   D 3 .   ? 42.490 10.555  5.228   1.00 18.86 ?  312 HOH   A O    1 
HETATM 6540 O O    . HOH   D 3 .   ? 34.020 -0.989  -8.915  1.00 26.10 ?  313 HOH   A O    1 
HETATM 6541 O O    . HOH   D 3 .   ? 17.134 -18.096 15.228  1.00 21.46 ?  314 HOH   A O    1 
HETATM 6542 O O    . HOH   D 3 .   ? 28.183 -0.119  -13.388 1.00 31.18 ?  315 HOH   A O    1 
HETATM 6543 O O    . HOH   D 3 .   ? 8.116  -21.500 3.979   1.00 41.06 ?  316 HOH   A O    1 
HETATM 6544 O O    . HOH   D 3 .   ? 15.211 -12.273 18.780  1.00 25.29 ?  317 HOH   A O    1 
HETATM 6545 O O    . HOH   D 3 .   ? 36.197 -5.096  -0.594  1.00 25.79 ?  318 HOH   A O    1 
HETATM 6546 O O    . HOH   D 3 .   ? 19.794 -12.483 -9.033  1.00 23.57 ?  319 HOH   A O    1 
HETATM 6547 O O    . HOH   D 3 .   ? 21.256 -2.401  -2.050  1.00 15.20 ?  320 HOH   A O    1 
HETATM 6548 O O    . HOH   D 3 .   ? 30.252 -13.294 -8.611  1.00 17.10 ?  321 HOH   A O    1 
HETATM 6549 O O    . HOH   D 3 .   ? 9.192  -10.211 19.427  1.00 37.40 ?  322 HOH   A O    1 
HETATM 6550 O O    . HOH   D 3 .   ? 14.802 -14.077 16.756  1.00 17.96 ?  323 HOH   A O    1 
HETATM 6551 O O    . HOH   D 3 .   ? 7.989  -12.634 -0.745  1.00 19.02 ?  324 HOH   A O    1 
HETATM 6552 O O    . HOH   D 3 .   ? 26.486 -19.368 -1.851  1.00 12.24 ?  325 HOH   A O    1 
HETATM 6553 O O    . HOH   D 3 .   ? 14.161 -4.561  -11.767 1.00 26.61 ?  326 HOH   A O    1 
HETATM 6554 O O    . HOH   D 3 .   ? 31.015 -18.218 7.728   1.00 18.95 ?  327 HOH   A O    1 
HETATM 6555 O O    . HOH   D 3 .   ? 12.267 0.278   15.039  1.00 30.43 ?  328 HOH   A O    1 
HETATM 6556 O O    B HOH   D 3 .   ? 10.351 -0.445  2.372   0.14 12.89 ?  329 HOH   A O    1 
HETATM 6557 O O    . HOH   D 3 .   ? 27.274 13.747  2.927   1.00 25.36 ?  330 HOH   A O    1 
HETATM 6558 O O    . HOH   D 3 .   ? 37.618 2.721   10.144  1.00 26.97 ?  331 HOH   A O    1 
HETATM 6559 O O    . HOH   D 3 .   ? 17.169 -17.912 -4.993  1.00 24.13 ?  332 HOH   A O    1 
HETATM 6560 O O    A HOH   D 3 .   ? 17.518 -1.737  0.512   0.86 15.03 ?  333 HOH   A O    1 
HETATM 6561 O O    . HOH   D 3 .   ? 18.829 -22.031 6.870   1.00 28.19 ?  334 HOH   A O    1 
HETATM 6562 O O    . HOH   D 3 .   ? 3.625  -9.486  9.983   1.00 30.88 ?  335 HOH   A O    1 
HETATM 6563 O O    . HOH   D 3 .   ? 22.524 5.247   19.174  1.00 40.95 ?  336 HOH   A O    1 
HETATM 6564 O O    . HOH   D 3 .   ? 38.338 10.060  7.166   1.00 29.26 ?  337 HOH   A O    1 
HETATM 6565 O O    . HOH   D 3 .   ? 20.610 -19.713 -5.106  1.00 26.71 ?  338 HOH   A O    1 
HETATM 6566 O O    . HOH   D 3 .   ? 0.718  -4.566  0.508   1.00 28.43 ?  339 HOH   A O    1 
HETATM 6567 O O    B HOH   D 3 .   ? 14.330 -4.333  3.411   0.14 11.85 ?  340 HOH   A O    1 
HETATM 6568 O O    . HOH   D 3 .   ? 38.614 4.954   6.930   1.00 14.68 ?  341 HOH   A O    1 
HETATM 6569 O O    . HOH   D 3 .   ? 37.499 11.865  4.959   1.00 28.16 ?  342 HOH   A O    1 
HETATM 6570 O O    . HOH   D 3 .   ? 31.748 8.194   14.847  1.00 22.52 ?  343 HOH   A O    1 
HETATM 6571 O O    . HOH   D 3 .   ? 35.801 -12.732 6.770   1.00 14.22 ?  344 HOH   A O    1 
HETATM 6572 O O    . HOH   D 3 .   ? 27.921 0.860   -7.161  1.00 12.31 ?  345 HOH   A O    1 
HETATM 6573 O O    B HOH   D 3 .   ? 19.173 -0.528  -1.965  0.14 12.68 ?  346 HOH   A O    1 
HETATM 6574 O O    . HOH   D 3 .   ? 18.722 -19.444 13.574  1.00 31.14 ?  347 HOH   A O    1 
HETATM 6575 O O    . HOH   D 3 .   ? 22.361 -19.294 11.376  1.00 30.56 ?  348 HOH   A O    1 
HETATM 6576 O O    . HOH   D 3 .   ? 42.619 4.279   5.266   1.00 27.59 ?  349 HOH   A O    1 
HETATM 6577 O O    . HOH   D 3 .   ? 33.681 -7.184  4.220   1.00 14.53 ?  350 HOH   A O    1 
HETATM 6578 O O    . HOH   D 3 .   ? 44.353 7.052   6.480   1.00 24.59 ?  351 HOH   A O    1 
HETATM 6579 O O    . HOH   D 3 .   ? -0.635 -8.486  2.398   1.00 39.09 ?  352 HOH   A O    1 
HETATM 6580 O O    . HOH   D 3 .   ? 11.638 -10.827 -10.064 1.00 35.83 ?  353 HOH   A O    1 
HETATM 6581 O O    . HOH   D 3 .   ? 37.293 -2.823  9.653   1.00 36.90 ?  354 HOH   A O    1 
HETATM 6582 O O    . HOH   D 3 .   ? 24.022 -2.088  -2.053  1.00 8.93  ?  355 HOH   A O    1 
HETATM 6583 O O    . HOH   D 3 .   ? 39.783 -0.979  -5.248  1.00 18.82 ?  356 HOH   A O    1 
HETATM 6584 O O    . HOH   D 3 .   ? 31.076 -13.963 -2.548  1.00 11.56 ?  357 HOH   A O    1 
HETATM 6585 O O    B HOH   D 3 .   ? 15.677 -1.026  5.321   0.14 12.83 ?  358 HOH   A O    1 
HETATM 6586 O O    . HOH   D 3 .   ? 13.270 -1.402  -6.498  1.00 14.90 ?  359 HOH   A O    1 
HETATM 6587 O O    . HOH   D 3 .   ? 21.984 -21.974 8.450   1.00 24.71 ?  360 HOH   A O    1 
HETATM 6588 O O    . HOH   D 3 .   ? 5.199  2.624   5.449   1.00 31.81 ?  361 HOH   A O    1 
HETATM 6589 O O    . HOH   D 3 .   ? 24.048 3.977   -4.836  1.00 22.47 ?  362 HOH   A O    1 
HETATM 6590 O O    . HOH   D 3 .   ? 22.783 12.538  1.701   1.00 12.94 ?  363 HOH   A O    1 
HETATM 6591 O O    . HOH   D 3 .   ? 15.285 3.932   17.935  1.00 33.89 ?  364 HOH   A O    1 
HETATM 6592 O O    . HOH   D 3 .   ? 15.594 11.938  8.051   1.00 25.17 ?  365 HOH   A O    1 
HETATM 6593 O O    . HOH   D 3 .   ? 16.489 -22.058 0.996   1.00 25.37 ?  366 HOH   A O    1 
HETATM 6594 O O    . HOH   D 3 .   ? 31.812 -9.334  -6.663  1.00 19.34 ?  367 HOH   A O    1 
HETATM 6595 O O    . HOH   D 3 .   ? 30.866 3.073   8.275   1.00 10.75 ?  368 HOH   A O    1 
HETATM 6596 O O    . HOH   D 3 .   ? 43.923 8.432   -3.195  1.00 22.26 ?  369 HOH   A O    1 
HETATM 6597 O O    . HOH   D 3 .   ? 14.321 -21.259 -4.193  1.00 27.73 ?  370 HOH   A O    1 
HETATM 6598 O O    . HOH   D 3 .   ? 9.820  -21.394 5.784   1.00 16.03 ?  371 HOH   A O    1 
HETATM 6599 O O    . HOH   D 3 .   ? 27.586 -10.694 14.022  1.00 14.40 ?  372 HOH   A O    1 
HETATM 6600 O O    . HOH   D 3 .   ? 18.598 9.416   9.044   1.00 18.43 ?  373 HOH   A O    1 
HETATM 6601 O O    . HOH   D 3 .   ? 31.686 -7.291  -9.902  1.00 19.25 ?  374 HOH   A O    1 
HETATM 6602 O O    . HOH   D 3 .   ? 17.027 -19.337 4.917   1.00 12.68 ?  375 HOH   A O    1 
HETATM 6603 O O    . HOH   D 3 .   ? 14.296 0.577   6.901   1.00 17.61 ?  376 HOH   A O    1 
HETATM 6604 O O    . HOH   D 3 .   ? 18.619 -2.388  -16.299 1.00 40.46 ?  377 HOH   A O    1 
HETATM 6605 O O    . HOH   D 3 .   ? 24.382 -7.859  14.469  1.00 15.04 ?  378 HOH   A O    1 
HETATM 6606 O O    . HOH   D 3 .   ? 13.491 -15.217 -7.391  1.00 25.49 ?  379 HOH   A O    1 
HETATM 6607 O O    . HOH   D 3 .   ? 24.438 3.579   -1.815  1.00 13.15 ?  380 HOH   A O    1 
HETATM 6608 O O    . HOH   D 3 .   ? 8.953  -12.133 17.279  1.00 42.67 ?  381 HOH   A O    1 
HETATM 6609 O O    . HOH   D 3 .   ? 14.073 -5.025  17.691  1.00 20.98 ?  382 HOH   A O    1 
HETATM 6610 O O    . HOH   D 3 .   ? 25.691 -0.793  -7.352  1.00 13.37 ?  383 HOH   A O    1 
HETATM 6611 O O    . HOH   D 3 .   ? 20.088 4.533   -7.538  1.00 16.40 ?  384 HOH   A O    1 
HETATM 6612 O O    . HOH   D 3 .   ? 24.606 2.003   -7.033  1.00 16.87 ?  385 HOH   A O    1 
HETATM 6613 O O    . HOH   D 3 .   ? 24.781 -17.595 12.711  1.00 21.55 ?  386 HOH   A O    1 
HETATM 6614 O O    A HOH   D 3 .   ? 14.665 -3.685  3.170   0.86 14.99 ?  387 HOH   A O    1 
HETATM 6615 O O    . HOH   D 3 .   ? -0.463 -3.135  3.256   1.00 36.48 ?  388 HOH   A O    1 
HETATM 6616 O O    . HOH   D 3 .   ? 43.398 7.869   2.630   1.00 21.51 ?  389 HOH   A O    1 
HETATM 6617 O O    . HOH   D 3 .   ? 21.279 10.289  15.071  1.00 31.91 ?  390 HOH   A O    1 
HETATM 6618 O O    . HOH   D 3 .   ? 37.610 -1.989  5.744   1.00 25.26 ?  391 HOH   A O    1 
HETATM 6619 O O    . HOH   D 3 .   ? 23.497 11.364  4.139   1.00 10.68 ?  392 HOH   A O    1 
HETATM 6620 O O    . HOH   D 3 .   ? 6.533  -5.614  11.326  1.00 18.90 ?  393 HOH   A O    1 
HETATM 6621 O O    . HOH   D 3 .   ? 28.480 -10.621 -14.013 1.00 40.95 ?  394 HOH   A O    1 
HETATM 6622 O O    . HOH   D 3 .   ? 6.768  -3.468  13.138  1.00 29.61 ?  395 HOH   A O    1 
HETATM 6623 O O    . HOH   D 3 .   ? 20.587 -20.059 2.785   1.00 15.11 ?  396 HOH   A O    1 
HETATM 6624 O O    . HOH   D 3 .   ? 22.712 -12.014 21.875  1.00 34.24 ?  397 HOH   A O    1 
HETATM 6625 O O    . HOH   D 3 .   ? 27.375 2.269   18.715  1.00 27.00 ?  398 HOH   A O    1 
HETATM 6626 O O    . HOH   D 3 .   ? 27.246 -5.925  -13.997 1.00 33.18 ?  399 HOH   A O    1 
HETATM 6627 O O    . HOH   D 3 .   ? 32.822 -9.282  5.855   1.00 18.67 ?  400 HOH   A O    1 
HETATM 6628 O O    . HOH   D 3 .   ? 21.740 -13.825 -8.114  1.00 32.10 ?  401 HOH   A O    1 
HETATM 6629 O O    A HOH   D 3 .   ? 15.835 -0.982  5.347   0.86 21.83 ?  402 HOH   A O    1 
HETATM 6630 O O    . HOH   D 3 .   ? 14.418 -24.745 11.627  1.00 29.20 ?  403 HOH   A O    1 
HETATM 6631 O O    . HOH   D 3 .   ? 30.797 1.793   16.699  1.00 18.47 ?  404 HOH   A O    1 
HETATM 6632 O O    . HOH   D 3 .   ? 21.378 3.173   -0.339  1.00 11.26 ?  405 HOH   A O    1 
HETATM 6633 O O    . HOH   D 3 .   ? 15.121 -8.075  -9.464  1.00 19.55 ?  406 HOH   A O    1 
HETATM 6634 O O    A HOH   D 3 .   ? 18.974 -0.686  -1.557  0.86 10.07 ?  407 HOH   A O    1 
HETATM 6635 O O    . HOH   D 3 .   ? 15.228 -21.668 14.240  1.00 15.04 ?  408 HOH   A O    1 
HETATM 6636 O O    . HOH   D 3 .   ? 23.958 -15.696 -9.206  1.00 27.37 ?  409 HOH   A O    1 
HETATM 6637 O O    . HOH   D 3 .   ? 41.685 1.532   4.869   1.00 34.78 ?  410 HOH   A O    1 
HETATM 6638 O O    . HOH   D 3 .   ? 14.075 -23.129 7.456   1.00 15.18 ?  411 HOH   A O    1 
HETATM 6639 O O    . HOH   D 3 .   ? 16.292 16.654  8.776   1.00 22.69 ?  412 HOH   A O    1 
HETATM 6640 O O    . HOH   D 3 .   ? 27.226 -3.272  19.320  1.00 31.30 ?  413 HOH   A O    1 
HETATM 6641 O O    . HOH   D 3 .   ? 38.136 -1.356  -2.017  1.00 17.40 ?  414 HOH   A O    1 
HETATM 6642 O O    . HOH   D 3 .   ? 32.615 -4.234  -9.937  1.00 24.47 ?  415 HOH   A O    1 
HETATM 6643 O O    . HOH   D 3 .   ? 23.942 -20.322 -1.378  1.00 13.77 ?  416 HOH   A O    1 
HETATM 6644 O O    . HOH   D 3 .   ? 30.174 -10.167 12.984  1.00 18.56 ?  417 HOH   A O    1 
HETATM 6645 O O    . HOH   D 3 .   ? 10.399 -13.729 -1.579  1.00 15.31 ?  418 HOH   A O    1 
HETATM 6646 O O    . HOH   D 3 .   ? 35.051 -5.217  -3.162  1.00 16.82 ?  419 HOH   A O    1 
HETATM 6647 O O    . HOH   D 3 .   ? 18.458 4.870   -15.075 1.00 43.04 ?  420 HOH   A O    1 
HETATM 6648 O O    B HOH   D 3 .   ? 16.792 2.840   -1.634  0.14 11.80 ?  421 HOH   A O    1 
HETATM 6649 O O    . HOH   D 3 .   ? 30.434 -13.015 13.487  1.00 16.94 ?  422 HOH   A O    1 
HETATM 6650 O O    . HOH   D 3 .   ? 30.918 6.282   -12.339 1.00 29.56 ?  423 HOH   A O    1 
HETATM 6651 O O    . HOH   D 3 .   ? 22.759 8.118   18.397  1.00 38.25 ?  424 HOH   A O    1 
HETATM 6652 O O    . HOH   D 3 .   ? 36.768 -5.013  5.362   1.00 22.61 ?  425 HOH   A O    1 
HETATM 6653 O O    A HOH   D 3 .   ? 16.044 6.924   3.088   0.86 13.39 ?  426 HOH   A O    1 
HETATM 6654 O O    . HOH   D 3 .   ? 40.939 -8.234  -6.721  1.00 36.08 ?  427 HOH   A O    1 
HETATM 6655 O O    . HOH   D 3 .   ? 44.992 -0.651  2.937   1.00 36.98 ?  428 HOH   A O    1 
HETATM 6656 O O    . HOH   D 3 .   ? 32.640 -10.694 3.131   1.00 26.11 ?  429 HOH   A O    1 
HETATM 6657 O O    . HOH   D 3 .   ? 16.194 -14.240 20.406  1.00 34.45 ?  430 HOH   A O    1 
HETATM 6658 O O    . HOH   D 3 .   ? 14.482 -0.492  -11.963 1.00 26.31 ?  431 HOH   A O    1 
HETATM 6659 O O    . HOH   D 3 .   ? 20.641 -17.902 24.822  1.00 43.44 ?  432 HOH   A O    1 
HETATM 6660 O O    . HOH   D 3 .   ? 15.923 2.075   24.901  1.00 47.51 ?  433 HOH   A O    1 
HETATM 6661 O O    . HOH   D 3 .   ? 11.767 -10.790 17.126  1.00 19.02 ?  434 HOH   A O    1 
HETATM 6662 O O    A HOH   D 3 .   ? 16.274 2.930   -1.354  0.86 14.46 ?  435 HOH   A O    1 
HETATM 6663 O O    . HOH   D 3 .   ? 21.343 -9.342  21.365  1.00 36.95 ?  436 HOH   A O    1 
HETATM 6664 O O    A HOH   D 3 .   ? 11.093 -0.409  2.025   0.86 23.10 ?  437 HOH   A O    1 
HETATM 6665 O O    . HOH   D 3 .   ? -1.388 -4.996  7.828   1.00 32.67 ?  438 HOH   A O    1 
HETATM 6666 O O    . HOH   D 3 .   ? 23.676 -8.112  17.102  1.00 19.79 ?  439 HOH   A O    1 
HETATM 6667 O O    . HOH   D 3 .   ? 23.312 -21.006 1.294   1.00 15.16 ?  440 HOH   A O    1 
HETATM 6668 O O    A HOH   D 3 .   ? 18.881 2.014   -0.675  0.86 10.90 ?  441 HOH   A O    1 
HETATM 6669 O O    . HOH   D 3 .   ? 23.221 7.609   -3.087  1.00 22.45 ?  442 HOH   A O    1 
HETATM 6670 O O    . HOH   D 3 .   ? 34.438 -8.084  -0.603  1.00 25.27 ?  443 HOH   A O    1 
HETATM 6671 O O    . HOH   D 3 .   ? 30.625 14.790  2.851   1.00 17.08 ?  444 HOH   A O    1 
HETATM 6672 O O    . HOH   D 3 .   ? 9.451  -16.287 -1.932  1.00 37.36 ?  445 HOH   A O    1 
HETATM 6673 O O    . HOH   D 3 .   ? 21.644 -14.722 18.143  1.00 40.62 ?  446 HOH   A O    1 
HETATM 6674 O O    . HOH   D 3 .   ? 31.350 -12.783 -0.030  1.00 17.26 ?  447 HOH   A O    1 
HETATM 6675 O O    . HOH   D 3 .   ? 19.520 -11.102 24.223  1.00 49.26 ?  448 HOH   A O    1 
HETATM 6676 O O    . HOH   D 3 .   ? 37.734 -8.825  -3.494  1.00 23.80 ?  449 HOH   A O    1 
HETATM 6677 O O    . HOH   D 3 .   ? 29.911 -16.084 10.527  1.00 32.70 ?  450 HOH   A O    1 
HETATM 6678 O O    . HOH   D 3 .   ? 18.469 -16.196 16.559  1.00 30.84 ?  451 HOH   A O    1 
HETATM 6679 O O    B HOH   D 3 .   ? 19.260 1.889   -0.828  0.14 13.83 ?  452 HOH   A O    1 
HETATM 6680 O O    . HOH   D 3 .   ? 25.457 8.267   -4.716  1.00 20.22 ?  453 HOH   A O    1 
HETATM 6681 O O    . HOH   D 3 .   ? 27.787 7.057   -6.305  1.00 32.22 ?  454 HOH   A O    1 
HETATM 6682 O O    A HOH   D 3 .   ? 14.057 -0.371  3.545   0.86 16.46 ?  455 HOH   A O    1 
HETATM 6683 O O    . HOH   D 3 .   ? 29.715 -1.962  -12.784 1.00 40.83 ?  456 HOH   A O    1 
HETATM 6684 O O    . HOH   D 3 .   ? 32.515 -15.981 10.770  1.00 35.33 ?  457 HOH   A O    1 
HETATM 6685 O O    . HOH   D 3 .   ? 19.890 -17.351 -5.059  1.00 23.20 ?  458 HOH   A O    1 
HETATM 6686 O O    . HOH   D 3 .   ? 23.208 -22.368 -3.317  1.00 33.22 ?  459 HOH   A O    1 
HETATM 6687 O O    . HOH   D 3 .   ? 24.643 14.529  7.929   1.00 31.75 ?  460 HOH   A O    1 
HETATM 6688 O O    . HOH   D 3 .   ? 24.963 5.599   20.826  1.00 47.32 ?  461 HOH   A O    1 
HETATM 6689 O O    . HOH   D 3 .   ? 26.906 11.635  -1.244  1.00 24.63 ?  462 HOH   A O    1 
HETATM 6690 O O    . HOH   D 3 .   ? 23.557 13.715  5.542   1.00 17.02 ?  463 HOH   A O    1 
HETATM 6691 O O    . HOH   D 3 .   ? 39.639 -7.068  -3.694  1.00 44.05 ?  464 HOH   A O    1 
HETATM 6692 O O    . HOH   D 3 .   ? 27.511 -11.420 16.529  1.00 33.87 ?  465 HOH   A O    1 
HETATM 6693 O O    . HOH   D 3 .   ? 15.712 -21.520 3.707   1.00 19.39 ?  466 HOH   A O    1 
HETATM 6694 O O    . HOH   D 3 .   ? 21.962 5.248   -5.803  1.00 24.77 ?  467 HOH   A O    1 
HETATM 6695 O O    . HOH   D 3 .   ? 18.748 10.762  11.434  1.00 28.72 ?  468 HOH   A O    1 
HETATM 6696 O O    . HOH   D 3 .   ? 12.048 -13.445 16.452  1.00 36.72 ?  469 HOH   A O    1 
HETATM 6697 O O    . HOH   D 3 .   ? 25.834 10.817  -3.654  1.00 21.86 ?  470 HOH   A O    1 
HETATM 6698 O O    . HOH   D 3 .   ? 12.387 1.561   17.489  1.00 38.33 ?  471 HOH   A O    1 
HETATM 6699 O O    . HOH   D 3 .   ? 11.011 -14.990 -6.065  1.00 31.93 ?  472 HOH   A O    1 
HETATM 6700 O O    . HOH   D 3 .   ? 35.193 7.407   12.284  1.00 44.36 ?  473 HOH   A O    1 
HETATM 6701 O O    . HOH   D 3 .   ? 14.036 -10.303 -10.784 1.00 29.76 ?  474 HOH   A O    1 
HETATM 6702 O O    . HOH   D 3 .   ? 28.935 8.957   17.500  1.00 35.31 ?  475 HOH   A O    1 
HETATM 6703 O O    . HOH   D 3 .   ? 40.965 -3.970  -0.348  1.00 37.34 ?  476 HOH   A O    1 
HETATM 6704 O O    . HOH   D 3 .   ? 17.396 -18.771 19.867  1.00 42.84 ?  477 HOH   A O    1 
HETATM 6705 O O    . HOH   D 3 .   ? 15.678 -17.088 -6.949  1.00 28.75 ?  478 HOH   A O    1 
HETATM 6706 O O    . HOH   D 3 .   ? 30.903 0.646   19.186  1.00 36.35 ?  479 HOH   A O    1 
HETATM 6707 O O    . HOH   D 3 .   ? 18.056 -16.260 -8.710  1.00 36.86 ?  480 HOH   A O    1 
HETATM 6708 O O    . HOH   D 3 .   ? 16.792 -20.633 16.264  1.00 24.13 ?  481 HOH   A O    1 
HETATM 6709 O O    . HOH   D 3 .   ? 23.163 11.838  -4.044  1.00 16.69 ?  482 HOH   A O    1 
HETATM 6710 O O    . HOH   D 3 .   ? 41.711 9.235   -4.174  1.00 29.03 ?  483 HOH   A O    1 
HETATM 6711 O O    . HOH   D 3 .   ? 44.528 10.457  -1.620  1.00 27.73 ?  484 HOH   A O    1 
HETATM 6712 O O    . HOH   D 3 .   ? 18.498 -23.201 1.936   1.00 38.13 ?  485 HOH   A O    1 
HETATM 6713 O O    . HOH   D 3 .   ? 23.399 -12.950 19.393  1.00 37.72 ?  486 HOH   A O    1 
HETATM 6714 O O    . HOH   D 3 .   ? 28.534 -4.636  -12.337 1.00 30.98 ?  487 HOH   A O    1 
HETATM 6715 O O    . HOH   D 3 .   ? 19.983 -22.362 4.123   1.00 23.23 ?  488 HOH   A O    1 
HETATM 6716 O O    . HOH   D 3 .   ? 31.420 -0.595  -10.602 1.00 24.64 ?  489 HOH   A O    1 
HETATM 6717 O O    . HOH   D 3 .   ? 40.575 -0.202  -7.812  1.00 34.16 ?  490 HOH   A O    1 
HETATM 6718 O O    . HOH   D 3 .   ? 15.947 -6.736  -11.703 1.00 36.08 ?  491 HOH   A O    1 
HETATM 6719 O O    . HOH   D 3 .   ? 39.207 2.361   7.600   1.00 29.34 ?  492 HOH   A O    1 
HETATM 6720 O O    . HOH   D 3 .   ? 28.656 -7.852  -15.250 1.00 41.58 ?  493 HOH   A O    1 
HETATM 6721 O O    . HOH   D 3 .   ? 14.112 -25.417 8.950   1.00 24.80 ?  494 HOH   A O    1 
HETATM 6722 O O    . HOH   D 3 .   ? 30.701 -5.809  -11.849 1.00 41.85 ?  495 HOH   A O    1 
HETATM 6723 O O    . HOH   D 3 .   ? 16.145 -23.402 5.722   1.00 24.18 ?  496 HOH   A O    1 
HETATM 6724 O O    . HOH   D 3 .   ? 8.222  -3.041  -5.579  1.00 36.36 ?  497 HOH   A O    1 
HETATM 6725 O O    . HOH   D 3 .   ? 30.774 5.830   -14.668 1.00 35.45 ?  498 HOH   A O    1 
HETATM 6726 O O    . HOH   D 3 .   ? 20.480 -16.079 -7.381  1.00 25.92 ?  499 HOH   A O    1 
HETATM 6727 O O    . HOH   D 3 .   ? 37.405 -6.668  7.491   1.00 22.93 ?  500 HOH   A O    1 
HETATM 6728 O O    . HOH   D 3 .   ? 23.123 -23.798 1.707   1.00 25.98 ?  501 HOH   A O    1 
HETATM 6729 O O    . HOH   D 3 .   ? 28.998 14.430  0.989   1.00 41.60 ?  502 HOH   A O    1 
HETATM 6730 O O    . HOH   D 3 .   ? 39.589 -0.029  6.568   1.00 28.43 ?  503 HOH   A O    1 
HETATM 6731 O O    . HOH   D 3 .   ? 38.145 13.817  6.751   1.00 45.94 ?  504 HOH   A O    1 
HETATM 6732 O O    . HOH   D 3 .   ? 36.555 -6.489  10.150  1.00 39.09 ?  505 HOH   A O    1 
HETATM 6733 O O    . HOH   D 3 .   ? 17.411 -6.599  -14.062 1.00 32.91 ?  506 HOH   A O    1 
HETATM 6734 O O    . HOH   D 3 .   ? 21.989 -24.142 4.387   1.00 22.88 ?  507 HOH   A O    1 
HETATM 6735 O O    A HOH   D 3 .   ? 14.882 8.615   4.995   0.86 34.23 ?  508 HOH   A O    1 
HETATM 6736 O O    . HOH   D 3 .   ? 24.097 8.984   -7.217  1.00 30.38 ?  509 HOH   A O    1 
HETATM 6737 O O    . HOH   D 3 .   ? 16.415 -21.166 18.867  1.00 29.22 ?  510 HOH   A O    1 
HETATM 6738 O O    . HOH   D 3 .   ? 16.018 -12.248 27.575  1.00 38.81 ?  511 HOH   A O    1 
HETATM 6739 O O    . HOH   D 3 .   ? 14.650 -22.842 19.943  1.00 30.31 ?  512 HOH   A O    1 
HETATM 6740 O O    . HOH   E 3 .   ? 29.813 -22.437 5.389   1.00 17.67 ?  201 HOH   B O    1 
HETATM 6741 O O    . HOH   E 3 .   ? 48.200 -6.920  15.557  1.00 31.18 ?  202 HOH   B O    1 
HETATM 6742 O O    . HOH   E 3 .   ? 27.841 -41.768 -15.240 1.00 33.12 ?  203 HOH   B O    1 
HETATM 6743 O O    . HOH   E 3 .   ? 47.410 -7.488  -4.063  1.00 38.34 ?  204 HOH   B O    1 
HETATM 6744 O O    . HOH   E 3 .   ? 49.357 -22.727 -19.828 1.00 44.24 ?  205 HOH   B O    1 
HETATM 6745 O O    . HOH   E 3 .   ? 41.417 -7.804  5.489   1.00 36.09 ?  206 HOH   B O    1 
HETATM 6746 O O    . HOH   E 3 .   ? 59.188 -18.806 6.706   1.00 34.46 ?  207 HOH   B O    1 
HETATM 6747 O O    . HOH   E 3 .   ? 41.872 -35.937 -17.436 1.00 27.94 ?  208 HOH   B O    1 
HETATM 6748 O O    . HOH   E 3 .   ? 37.908 -39.532 -0.348  1.00 40.80 ?  209 HOH   B O    1 
HETATM 6749 O O    . HOH   E 3 .   ? 27.746 -29.193 -1.932  1.00 32.56 ?  210 HOH   B O    1 
HETATM 6750 O O    . HOH   E 3 .   ? 55.523 -16.507 -14.432 1.00 35.55 ?  211 HOH   B O    1 
HETATM 6751 O O    . HOH   E 3 .   ? 54.470 -9.348  -8.888  1.00 17.35 ?  212 HOH   B O    1 
HETATM 6752 O O    . HOH   E 3 .   ? 58.303 -12.906 8.413   1.00 36.92 ?  213 HOH   B O    1 
HETATM 6753 O O    . HOH   E 3 .   ? 56.401 -19.750 7.289   1.00 33.22 ?  214 HOH   B O    1 
HETATM 6754 O O    . HOH   E 3 .   ? 29.746 -34.237 -0.496  1.00 30.72 ?  215 HOH   B O    1 
HETATM 6755 O O    . HOH   E 3 .   ? 50.749 -6.135  0.194   1.00 26.82 ?  216 HOH   B O    1 
HETATM 6756 O O    . HOH   E 3 .   ? 50.300 -3.398  7.138   1.00 34.30 ?  217 HOH   B O    1 
HETATM 6757 O O    . HOH   E 3 .   ? 57.777 -24.470 4.956   1.00 31.54 ?  218 HOH   B O    1 
HETATM 6758 O O    . HOH   E 3 .   ? 30.234 -41.066 -8.236  1.00 14.53 ?  219 HOH   B O    1 
HETATM 6759 O O    . HOH   E 3 .   ? 45.211 -34.949 6.855   1.00 36.30 ?  220 HOH   B O    1 
HETATM 6760 O O    . HOH   E 3 .   ? 39.383 -10.941 6.058   1.00 26.44 ?  221 HOH   B O    1 
HETATM 6761 O O    . HOH   E 3 .   ? 56.764 -30.725 -7.831  1.00 38.07 ?  222 HOH   B O    1 
HETATM 6762 O O    . HOH   E 3 .   ? 35.975 -43.238 -8.640  1.00 25.31 ?  223 HOH   B O    1 
HETATM 6763 O O    . HOH   E 3 .   ? 37.185 -19.751 -18.117 1.00 34.31 ?  224 HOH   B O    1 
HETATM 6764 O O    . HOH   E 3 .   ? 57.431 -16.199 -12.218 1.00 17.66 ?  225 HOH   B O    1 
HETATM 6765 O O    . HOH   E 3 .   ? 52.944 -13.390 -20.446 1.00 34.58 ?  226 HOH   B O    1 
HETATM 6766 O O    . HOH   E 3 .   ? 44.477 -7.259  2.127   1.00 31.05 ?  227 HOH   B O    1 
HETATM 6767 O O    . HOH   E 3 .   ? 40.625 -16.089 14.105  1.00 25.10 ?  228 HOH   B O    1 
HETATM 6768 O O    . HOH   E 3 .   ? 41.385 -9.687  13.025  1.00 20.36 ?  229 HOH   B O    1 
HETATM 6769 O O    . HOH   E 3 .   ? 41.516 -39.166 -14.974 1.00 19.50 ?  230 HOH   B O    1 
HETATM 6770 O O    . HOH   E 3 .   ? 57.230 -26.818 -7.671  1.00 39.44 ?  231 HOH   B O    1 
HETATM 6771 O O    . HOH   E 3 .   ? 29.888 -26.365 3.870   1.00 24.57 ?  232 HOH   B O    1 
HETATM 6772 O O    . HOH   E 3 .   ? 34.571 -36.397 -7.298  1.00 14.91 ?  233 HOH   B O    1 
HETATM 6773 O O    . HOH   E 3 .   ? 30.846 -28.824 4.193   1.00 20.80 ?  234 HOH   B O    1 
HETATM 6774 O O    . HOH   E 3 .   ? 28.407 -19.700 -13.188 1.00 22.57 ?  235 HOH   B O    1 
HETATM 6775 O O    . HOH   E 3 .   ? 42.662 -22.906 3.773   1.00 10.05 ?  236 HOH   B O    1 
HETATM 6776 O O    . HOH   E 3 .   ? 44.537 -27.861 -0.806  1.00 21.08 ?  237 HOH   B O    1 
HETATM 6777 O O    . HOH   E 3 .   ? 39.492 -11.159 0.276   1.00 15.35 ?  238 HOH   B O    1 
HETATM 6778 O O    . HOH   E 3 .   ? 50.748 -12.979 -0.521  1.00 11.09 ?  239 HOH   B O    1 
HETATM 6779 O O    . HOH   E 3 .   ? 51.713 -6.522  4.428   1.00 18.59 ?  240 HOH   B O    1 
HETATM 6780 O O    . HOH   E 3 .   ? 32.912 -43.856 -11.421 1.00 17.54 ?  241 HOH   B O    1 
HETATM 6781 O O    . HOH   E 3 .   ? 51.604 -13.925 10.889  1.00 28.30 ?  242 HOH   B O    1 
HETATM 6782 O O    . HOH   E 3 .   ? 35.137 -7.992  -3.106  1.00 16.93 ?  243 HOH   B O    1 
HETATM 6783 O O    . HOH   E 3 .   ? 42.597 -25.412 2.561   1.00 13.69 ?  244 HOH   B O    1 
HETATM 6784 O O    . HOH   E 3 .   ? 25.450 -26.018 -1.385  1.00 28.91 ?  245 HOH   B O    1 
HETATM 6785 O O    . HOH   E 3 .   ? 48.532 -36.468 -15.609 1.00 41.72 ?  246 HOH   B O    1 
HETATM 6786 O O    . HOH   E 3 .   ? 45.066 -43.534 -10.564 1.00 27.37 ?  247 HOH   B O    1 
HETATM 6787 O O    . HOH   E 3 .   ? 43.254 -32.386 -17.161 1.00 19.77 ?  248 HOH   B O    1 
HETATM 6788 O O    . HOH   E 3 .   ? 57.635 -24.429 -3.900  1.00 20.54 ?  249 HOH   B O    1 
HETATM 6789 O O    . HOH   E 3 .   ? 38.951 -12.110 12.335  1.00 29.39 ?  250 HOH   B O    1 
HETATM 6790 O O    . HOH   E 3 .   ? 43.148 -43.294 -8.325  1.00 26.78 ?  251 HOH   B O    1 
HETATM 6791 O O    . HOH   E 3 .   ? 41.887 -23.574 9.258   1.00 14.26 ?  252 HOH   B O    1 
HETATM 6792 O O    . HOH   E 3 .   ? 30.887 -15.785 2.567   1.00 11.58 ?  253 HOH   B O    1 
HETATM 6793 O O    . HOH   E 3 .   ? 29.742 -25.243 -10.925 1.00 14.09 ?  254 HOH   B O    1 
HETATM 6794 O O    . HOH   E 3 .   ? 40.322 -12.756 -11.593 1.00 13.20 ?  255 HOH   B O    1 
HETATM 6795 O O    . HOH   E 3 .   ? 58.150 -10.599 -4.135  1.00 19.97 ?  256 HOH   B O    1 
HETATM 6796 O O    . HOH   E 3 .   ? 46.414 -1.591  13.318  1.00 27.85 ?  257 HOH   B O    1 
HETATM 6797 O O    . HOH   E 3 .   ? 51.048 -39.947 -8.301  1.00 27.07 ?  258 HOH   B O    1 
HETATM 6798 O O    . HOH   E 3 .   ? 57.086 -12.141 12.269  1.00 36.50 ?  259 HOH   B O    1 
HETATM 6799 O O    . HOH   E 3 .   ? 33.533 -17.053 7.988   1.00 17.43 ?  260 HOH   B O    1 
HETATM 6800 O O    . HOH   E 3 .   ? 57.525 -9.257  1.405   1.00 18.47 ?  261 HOH   B O    1 
HETATM 6801 O O    . HOH   E 3 .   ? 34.881 -24.698 13.816  1.00 26.20 ?  262 HOH   B O    1 
HETATM 6802 O O    . HOH   E 3 .   ? 48.111 -24.455 -17.843 1.00 26.60 ?  263 HOH   B O    1 
HETATM 6803 O O    . HOH   E 3 .   ? 42.211 -10.190 -15.016 1.00 29.65 ?  264 HOH   B O    1 
HETATM 6804 O O    . HOH   E 3 .   ? 31.835 -17.979 -14.601 1.00 28.63 ?  265 HOH   B O    1 
HETATM 6805 O O    . HOH   E 3 .   ? 43.623 -15.406 18.240  1.00 29.59 ?  266 HOH   B O    1 
HETATM 6806 O O    . HOH   E 3 .   ? 49.819 -0.567  10.288  1.00 30.44 ?  267 HOH   B O    1 
HETATM 6807 O O    . HOH   E 3 .   ? 48.028 -22.816 5.769   1.00 14.94 ?  268 HOH   B O    1 
HETATM 6808 O O    . HOH   E 3 .   ? 27.153 -31.843 -10.097 1.00 18.77 ?  269 HOH   B O    1 
HETATM 6809 O O    . HOH   E 3 .   ? 28.291 -34.372 -9.582  1.00 18.62 ?  270 HOH   B O    1 
HETATM 6810 O O    . HOH   E 3 .   ? 34.188 -18.594 11.369  1.00 19.72 ?  271 HOH   B O    1 
HETATM 6811 O O    . HOH   E 3 .   ? 38.459 -11.082 -2.296  1.00 17.49 ?  272 HOH   B O    1 
HETATM 6812 O O    . HOH   E 3 .   ? 49.380 -28.706 -6.978  1.00 13.68 ?  273 HOH   B O    1 
HETATM 6813 O O    . HOH   E 3 .   ? 56.990 -8.695  8.407   1.00 19.16 ?  274 HOH   B O    1 
HETATM 6814 O O    . HOH   E 3 .   ? 43.387 -15.822 -12.223 1.00 12.49 ?  275 HOH   B O    1 
HETATM 6815 O O    . HOH   E 3 .   ? 56.228 -23.436 -14.809 1.00 23.87 ?  276 HOH   B O    1 
HETATM 6816 O O    . HOH   E 3 .   ? 41.199 -5.584  11.551  1.00 41.23 ?  277 HOH   B O    1 
HETATM 6817 O O    . HOH   E 3 .   ? 28.527 -30.952 -14.802 1.00 27.58 ?  278 HOH   B O    1 
HETATM 6818 O O    . HOH   E 3 .   ? 27.977 -22.912 -8.094  1.00 14.79 ?  279 HOH   B O    1 
HETATM 6819 O O    . HOH   E 3 .   ? 42.343 -9.939  9.343   1.00 19.28 ?  280 HOH   B O    1 
HETATM 6820 O O    . HOH   E 3 .   ? 34.933 -33.398 -19.290 1.00 25.91 ?  281 HOH   B O    1 
HETATM 6821 O O    . HOH   E 3 .   ? 34.476 -12.795 2.535   1.00 23.85 ?  282 HOH   B O    1 
HETATM 6822 O O    . HOH   E 3 .   ? 37.375 -35.699 7.072   1.00 29.89 ?  283 HOH   B O    1 
HETATM 6823 O O    . HOH   E 3 .   ? 30.710 -42.271 -10.690 1.00 26.46 ?  284 HOH   B O    1 
HETATM 6824 O O    . HOH   E 3 .   ? 46.640 -31.288 -4.837  1.00 17.60 ?  285 HOH   B O    1 
HETATM 6825 O O    . HOH   E 3 .   ? 48.443 -25.078 3.041   1.00 11.54 ?  286 HOH   B O    1 
HETATM 6826 O O    . HOH   E 3 .   ? 48.740 -20.073 5.879   1.00 12.62 ?  287 HOH   B O    1 
HETATM 6827 O O    . HOH   E 3 .   ? 41.242 -24.486 15.726  1.00 39.27 ?  288 HOH   B O    1 
HETATM 6828 O O    . HOH   E 3 .   ? 51.284 -37.622 -9.650  1.00 22.32 ?  289 HOH   B O    1 
HETATM 6829 O O    . HOH   E 3 .   ? 52.569 -10.476 12.985  1.00 21.34 ?  290 HOH   B O    1 
HETATM 6830 O O    . HOH   E 3 .   ? 46.894 -29.565 9.782   1.00 29.91 ?  291 HOH   B O    1 
HETATM 6831 O O    . HOH   E 3 .   ? 33.512 -15.328 -14.039 1.00 18.64 ?  292 HOH   B O    1 
HETATM 6832 O O    . HOH   E 3 .   ? 59.791 -15.459 8.111   1.00 29.07 ?  293 HOH   B O    1 
HETATM 6833 O O    . HOH   E 3 .   ? 36.833 -12.777 -1.562  1.00 24.04 ?  294 HOH   B O    1 
HETATM 6834 O O    . HOH   E 3 .   ? 45.431 -33.420 -16.008 1.00 19.42 ?  295 HOH   B O    1 
HETATM 6835 O O    . HOH   E 3 .   ? 27.587 -26.742 -15.739 1.00 31.13 ?  296 HOH   B O    1 
HETATM 6836 O O    . HOH   E 3 .   ? 40.238 -10.824 -9.611  1.00 15.02 ?  297 HOH   B O    1 
HETATM 6837 O O    . HOH   E 3 .   ? 35.084 -33.612 4.412   1.00 24.56 ?  298 HOH   B O    1 
HETATM 6838 O O    . HOH   E 3 .   ? 42.667 -12.321 -18.568 1.00 27.60 ?  299 HOH   B O    1 
HETATM 6839 O O    . HOH   E 3 .   ? 44.647 -27.494 1.897   1.00 13.90 ?  300 HOH   B O    1 
HETATM 6840 O O    . HOH   E 3 .   ? 38.343 -9.381  -13.336 1.00 24.78 ?  301 HOH   B O    1 
HETATM 6841 O O    . HOH   E 3 .   ? 42.432 -34.733 3.714   1.00 25.61 ?  302 HOH   B O    1 
HETATM 6842 O O    . HOH   E 3 .   ? 52.679 -35.645 -8.637  1.00 25.77 ?  303 HOH   B O    1 
HETATM 6843 O O    . HOH   E 3 .   ? 42.860 -20.334 -20.857 1.00 35.68 ?  304 HOH   B O    1 
HETATM 6844 O O    . HOH   E 3 .   ? 47.114 -34.003 -4.675  1.00 14.82 ?  305 HOH   B O    1 
HETATM 6845 O O    . HOH   E 3 .   ? 53.210 -16.072 -12.786 1.00 27.45 ?  306 HOH   B O    1 
HETATM 6846 O O    . HOH   E 3 .   ? 50.084 -24.616 5.772   1.00 30.27 ?  307 HOH   B O    1 
HETATM 6847 O O    . HOH   E 3 .   ? 52.628 -29.242 -13.052 1.00 21.80 ?  308 HOH   B O    1 
HETATM 6848 O O    . HOH   E 3 .   ? 57.716 -22.115 3.016   1.00 22.51 ?  309 HOH   B O    1 
HETATM 6849 O O    . HOH   E 3 .   ? 25.965 -21.511 -3.581  1.00 14.09 ?  310 HOH   B O    1 
HETATM 6850 O O    . HOH   E 3 .   ? 44.063 -29.394 -4.754  1.00 21.65 ?  311 HOH   B O    1 
HETATM 6851 O O    . HOH   E 3 .   ? 45.952 -40.407 -3.634  1.00 26.78 ?  312 HOH   B O    1 
HETATM 6852 O O    . HOH   E 3 .   ? 32.825 -34.620 -6.009  1.00 14.18 ?  313 HOH   B O    1 
HETATM 6853 O O    . HOH   E 3 .   ? 48.227 -32.651 -16.671 1.00 40.59 ?  314 HOH   B O    1 
HETATM 6854 O O    . HOH   E 3 .   ? 62.895 -20.164 -0.957  1.00 37.50 ?  315 HOH   B O    1 
HETATM 6855 O O    . HOH   E 3 .   ? 37.559 -18.287 13.103  1.00 24.12 ?  316 HOH   B O    1 
HETATM 6856 O O    . HOH   E 3 .   ? 41.717 -8.127  1.329   1.00 23.20 ?  317 HOH   B O    1 
HETATM 6857 O O    . HOH   E 3 .   ? 37.834 -10.262 -10.809 1.00 15.03 ?  318 HOH   B O    1 
HETATM 6858 O O    . HOH   E 3 .   ? 53.510 -30.228 4.475   1.00 17.64 ?  319 HOH   B O    1 
HETATM 6859 O O    . HOH   E 3 .   ? 43.233 -21.482 10.614  1.00 13.98 ?  320 HOH   B O    1 
HETATM 6860 O O    . HOH   E 3 .   ? 59.977 -17.146 -10.505 1.00 30.95 ?  321 HOH   B O    1 
HETATM 6861 O O    . HOH   E 3 .   ? 44.589 -24.674 9.535   1.00 17.52 ?  322 HOH   B O    1 
HETATM 6862 O O    . HOH   E 3 .   ? 62.693 -13.567 4.652   1.00 25.72 ?  323 HOH   B O    1 
HETATM 6863 O O    . HOH   E 3 .   ? 39.456 -23.455 -20.323 1.00 32.51 ?  324 HOH   B O    1 
HETATM 6864 O O    . HOH   E 3 .   ? 38.364 -12.846 7.907   1.00 16.61 ?  325 HOH   B O    1 
HETATM 6865 O O    . HOH   E 3 .   ? 26.338 -21.049 -6.342  1.00 14.37 ?  326 HOH   B O    1 
HETATM 6866 O O    . HOH   E 3 .   ? 37.245 -30.631 -21.141 1.00 27.93 ?  327 HOH   B O    1 
HETATM 6867 O O    . HOH   E 3 .   ? 27.998 -14.822 -9.460  1.00 29.30 ?  328 HOH   B O    1 
HETATM 6868 O O    . HOH   E 3 .   ? 36.718 -12.467 4.219   1.00 16.89 ?  329 HOH   B O    1 
HETATM 6869 O O    . HOH   E 3 .   ? 33.622 -31.154 11.044  1.00 33.88 ?  330 HOH   B O    1 
HETATM 6870 O O    . HOH   E 3 .   ? 51.480 -32.928 -10.889 1.00 34.62 ?  331 HOH   B O    1 
HETATM 6871 O O    . HOH   E 3 .   ? 47.173 -24.533 8.105   1.00 23.93 ?  332 HOH   B O    1 
HETATM 6872 O O    . HOH   E 3 .   ? 45.846 -36.274 -16.205 1.00 29.92 ?  333 HOH   B O    1 
HETATM 6873 O O    . HOH   E 3 .   ? 44.273 -1.772  7.565   1.00 41.44 ?  334 HOH   B O    1 
HETATM 6874 O O    . HOH   E 3 .   ? 51.717 -5.917  -7.920  1.00 46.29 ?  335 HOH   B O    1 
HETATM 6875 O O    . HOH   E 3 .   ? 48.608 -11.874 -13.890 1.00 24.98 ?  336 HOH   B O    1 
HETATM 6876 O O    . HOH   E 3 .   ? 47.513 -27.480 1.919   1.00 12.93 ?  337 HOH   B O    1 
HETATM 6877 O O    . HOH   E 3 .   ? 43.139 -34.720 0.021   1.00 18.63 ?  338 HOH   B O    1 
HETATM 6878 O O    . HOH   E 3 .   ? 42.847 -43.505 -14.465 1.00 45.52 ?  339 HOH   B O    1 
HETATM 6879 O O    . HOH   E 3 .   ? 53.694 -12.504 -22.386 1.00 34.31 ?  340 HOH   B O    1 
HETATM 6880 O O    . HOH   E 3 .   ? 46.852 -19.937 12.286  1.00 31.31 ?  341 HOH   B O    1 
HETATM 6881 O O    . HOH   E 3 .   ? 36.985 -15.062 -16.528 1.00 35.33 ?  342 HOH   B O    1 
HETATM 6882 O O    . HOH   E 3 .   ? 28.898 -42.938 -12.475 1.00 35.20 ?  343 HOH   B O    1 
HETATM 6883 O O    . HOH   E 3 .   ? 39.783 -44.295 -11.304 1.00 36.16 ?  344 HOH   B O    1 
HETATM 6884 O O    . HOH   E 3 .   ? 37.160 -45.303 -9.868  1.00 36.70 ?  345 HOH   B O    1 
HETATM 6885 O O    . HOH   E 3 .   ? 33.001 -14.709 0.973   1.00 16.17 ?  346 HOH   B O    1 
HETATM 6886 O O    . HOH   E 3 .   ? 27.755 -26.638 -0.701  1.00 27.67 ?  347 HOH   B O    1 
HETATM 6887 O O    . HOH   E 3 .   ? 40.439 -43.514 -9.187  1.00 26.49 ?  348 HOH   B O    1 
HETATM 6888 O O    . HOH   E 3 .   ? 33.717 -9.347  -8.836  1.00 29.27 ?  349 HOH   B O    1 
HETATM 6889 O O    . HOH   E 3 .   ? 62.502 -20.144 -4.963  1.00 41.66 ?  350 HOH   B O    1 
HETATM 6890 O O    . HOH   E 3 .   ? 38.490 -12.316 -16.290 1.00 35.79 ?  351 HOH   B O    1 
HETATM 6891 O O    . HOH   E 3 .   ? 38.591 -22.355 15.044  1.00 37.94 ?  352 HOH   B O    1 
HETATM 6892 O O    . HOH   E 3 .   ? 36.032 -8.649  -9.702  1.00 33.04 ?  353 HOH   B O    1 
HETATM 6893 O O    . HOH   E 3 .   ? 44.192 -37.377 -17.861 1.00 31.76 ?  354 HOH   B O    1 
HETATM 6894 O O    . HOH   E 3 .   ? 55.663 -8.316  10.856  1.00 24.86 ?  355 HOH   B O    1 
HETATM 6895 O O    . HOH   E 3 .   ? 23.207 -23.735 6.706   1.00 30.69 ?  356 HOH   B O    1 
HETATM 6896 O O    . HOH   E 3 .   ? 56.567 -7.299  3.092   1.00 27.17 ?  357 HOH   B O    1 
HETATM 6897 O O    . HOH   E 3 .   ? 61.505 -19.860 1.607   1.00 29.82 ?  358 HOH   B O    1 
HETATM 6898 O O    . HOH   E 3 .   ? 34.746 -10.328 7.336   1.00 22.85 ?  359 HOH   B O    1 
HETATM 6899 O O    . HOH   E 3 .   ? 43.116 -12.713 -21.287 1.00 38.50 ?  360 HOH   B O    1 
HETATM 6900 O O    . HOH   E 3 .   ? 34.209 -7.779  11.397  1.00 39.23 ?  361 HOH   B O    1 
HETATM 6901 O O    . HOH   E 3 .   ? 40.254 -8.852  9.877   1.00 37.23 ?  362 HOH   B O    1 
HETATM 6902 O O    . HOH   E 3 .   ? 27.146 -26.017 -11.506 1.00 29.70 ?  363 HOH   B O    1 
HETATM 6903 O O    . HOH   E 3 .   ? 57.005 -21.548 -16.492 1.00 38.45 ?  364 HOH   B O    1 
HETATM 6904 O O    . HOH   E 3 .   ? 59.006 -10.555 9.110   1.00 35.71 ?  365 HOH   B O    1 
HETATM 6905 O O    . HOH   E 3 .   ? 32.463 -23.664 14.067  1.00 36.59 ?  366 HOH   B O    1 
HETATM 6906 O O    . HOH   E 3 .   ? 54.250 -5.767  2.973   1.00 35.68 ?  367 HOH   B O    1 
HETATM 6907 O O    . HOH   E 3 .   ? 36.202 -8.749  8.976   1.00 36.51 ?  368 HOH   B O    1 
HETATM 6908 O O    . HOH   E 3 .   ? 39.885 -7.110  7.769   1.00 41.97 ?  369 HOH   B O    1 
HETATM 6909 O O    . HOH   E 3 .   ? 39.944 -11.431 -14.029 1.00 26.16 ?  370 HOH   B O    1 
HETATM 6910 O O    . HOH   E 3 .   ? 52.105 -12.975 13.267  1.00 32.58 ?  371 HOH   B O    1 
HETATM 6911 O O    . HOH   E 3 .   ? 56.080 -7.844  -0.604  1.00 34.44 ?  372 HOH   B O    1 
HETATM 6912 O O    . HOH   E 3 .   ? 41.761 -10.018 -17.462 1.00 49.74 ?  373 HOH   B O    1 
HETATM 6913 O O    . HOH   E 3 .   ? 48.462 -26.525 8.718   1.00 36.06 ?  374 HOH   B O    1 
HETATM 6914 O O    . HOH   E 3 .   ? 38.104 -10.690 10.033  1.00 27.56 ?  375 HOH   B O    1 
HETATM 6915 O O    . HOH   E 3 .   ? 63.028 -12.365 6.882   1.00 36.28 ?  376 HOH   B O    1 
HETATM 6916 O O    . HOH   E 3 .   ? 44.103 -5.631  -3.505  1.00 42.63 ?  377 HOH   B O    1 
HETATM 6917 O O    . HOH   E 3 .   ? 41.843 -6.827  -4.869  1.00 45.94 ?  378 HOH   B O    1 
HETATM 6918 O O    . HOH   E 3 .   ? 36.512 -22.803 13.270  1.00 22.50 ?  379 HOH   B O    1 
HETATM 6919 O O    . HOH   E 3 .   ? 40.109 -7.682  3.222   1.00 33.23 ?  380 HOH   B O    1 
HETATM 6920 O O    . HOH   E 3 .   ? 42.678 -17.123 -23.295 1.00 41.07 ?  381 HOH   B O    1 
HETATM 6921 O O    . HOH   E 3 .   ? 52.861 -29.930 7.081   1.00 22.11 ?  382 HOH   B O    1 
HETATM 6922 O O    . HOH   E 3 .   ? 60.497 -22.247 2.710   1.00 40.40 ?  383 HOH   B O    1 
HETATM 6923 O O    . HOH   E 3 .   ? 39.771 -14.126 15.746  1.00 48.95 ?  384 HOH   B O    1 
HETATM 6924 O O    . HOH   E 3 .   ? 40.977 -9.872  15.745  1.00 43.68 ?  385 HOH   B O    1 
HETATM 6925 O O    . HOH   E 3 .   ? 35.347 -20.314 13.301  1.00 25.01 ?  386 HOH   B O    1 
HETATM 6926 O O    . HOH   E 3 .   ? 46.865 -5.369  2.899   1.00 37.52 ?  387 HOH   B O    1 
HETATM 6927 O O    . HOH   E 3 .   ? 35.368 -33.738 7.187   1.00 38.77 ?  388 HOH   B O    1 
HETATM 6928 O O    . HOH   E 3 .   ? 23.916 -20.851 -7.752  1.00 24.22 ?  389 HOH   B O    1 
HETATM 6929 O O    . HOH   E 3 .   ? 25.786 -18.915 -12.048 1.00 34.47 ?  390 HOH   B O    1 
HETATM 6930 O O    . HOH   E 3 .   ? 44.176 -31.759 -3.918  1.00 29.99 ?  391 HOH   B O    1 
HETATM 6931 O O    . HOH   E 3 .   ? 40.733 -6.629  -0.921  1.00 23.25 ?  392 HOH   B O    1 
HETATM 6932 O O    . HOH   E 3 .   ? 27.975 -27.162 2.167   1.00 29.91 ?  393 HOH   B O    1 
HETATM 6933 O O    . HOH   E 3 .   ? 26.640 -28.008 -13.558 1.00 30.90 ?  394 HOH   B O    1 
HETATM 6934 O O    . HOH   E 3 .   ? 24.611 -20.656 -10.492 1.00 34.38 ?  395 HOH   B O    1 
HETATM 6935 O O    . HOH   E 3 .   ? 34.440 -33.479 9.562   1.00 30.54 ?  396 HOH   B O    1 
HETATM 6936 O O    . HOH   E 3 .   ? 45.840 -20.314 15.123  1.00 47.60 ?  397 HOH   B O    1 
HETATM 6937 O O    . HOH   E 3 .   ? 26.896 -30.682 -12.778 1.00 25.93 ?  398 HOH   B O    1 
HETATM 6938 O O    . HOH   E 3 .   ? 50.677 -30.834 8.646   1.00 25.81 ?  399 HOH   B O    1 
HETATM 6939 O O    . HOH   E 3 .   ? 57.748 -6.506  -2.440  1.00 34.96 ?  400 HOH   B O    1 
HETATM 6940 O O    . HOH   E 3 .   ? 40.864 -11.814 -22.419 1.00 40.23 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.5050 0.4932 0.5579 0.0028  -0.0243 0.0868  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5026 0.4991 0.5439 -0.0028 -0.0152 0.0475  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5031 0.4917 0.5496 0.0005  -0.0228 0.0846  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5002 0.4968 0.5377 -0.0039 -0.0158 0.0495  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.4892 0.4827 0.5124 -0.0053 -0.0249 0.0831  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.4887 0.4865 0.5083 -0.0080 -0.0202 0.0620  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.4901 0.4831 0.5152 -0.0020 -0.0269 0.0870  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.4916 0.4890 0.5160 -0.0065 -0.0205 0.0614  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.5134 0.4978 0.5704 0.0030  -0.0179 0.0837  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5068 0.5028 0.5542 -0.0017 -0.0122 0.0407  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.5173 0.5001 0.5761 0.0038  -0.0162 0.0831  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5090 0.5048 0.5592 -0.0010 -0.0109 0.0374  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.5168 0.5000 0.5758 0.0036  -0.0161 0.0854  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5090 0.5048 0.5593 -0.0010 -0.0109 0.0379  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.4710 0.4711 0.4632 -0.0144 -0.0244 0.0767  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.4337 0.4433 0.3657 -0.0305 -0.0256 0.0823  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.3943 0.4190 0.3030 -0.0454 -0.0124 0.0584  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.3938 0.4177 0.2885 -0.0462 -0.0126 0.0687  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.4339 0.4383 0.3286 -0.0309 -0.0385 0.1067  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.4333 0.4309 0.2931 -0.0315 -0.0504 0.1323  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.4331 0.4248 0.2823 -0.0331 -0.0498 0.1418  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.4320 0.4290 0.2868 -0.0301 -0.0546 0.1436  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.3547 0.3911 0.2540 -0.0574 -0.0023 0.0258  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3184 0.3706 0.2197 -0.0648 0.0067  -0.0101 5   SER   A CA  
48   C C   . SER   A 5   ? 0.2806 0.3320 0.1938 -0.0495 0.0153  -0.0373 5   SER   A C   
49   O O   . SER   A 5   ? 0.2848 0.3381 0.2086 -0.0323 0.0247  -0.0580 5   SER   A O   
50   C CB  . SER   A 5   ? 0.3238 0.3865 0.2264 -0.0790 0.0160  -0.0117 5   SER   A CB  
51   O OG  . SER   A 5   ? 0.3306 0.3885 0.2296 -0.0843 0.0277  -0.0053 5   SER   A OG  
57   N N   . PHE   A 6   ? 0.2373 0.2875 0.1575 -0.0525 0.0206  -0.0342 6   PHE   A N   
58   C CA  . PHE   A 6   ? 0.2116 0.2495 0.1474 -0.0517 0.0300  -0.0101 6   PHE   A CA  
59   C C   . PHE   A 6   ? 0.2084 0.2490 0.1732 -0.0564 0.0485  -0.0057 6   PHE   A C   
60   O O   . PHE   A 6   ? 0.2171 0.2635 0.2061 -0.0597 0.0480  0.0087  6   PHE   A O   
61   C CB  . PHE   A 6   ? 0.1997 0.2172 0.1438 -0.0377 0.0284  0.0013  6   PHE   A CB  
62   C CG  . PHE   A 6   ? 0.1934 0.1972 0.1385 -0.0296 0.0293  0.0110  6   PHE   A CG  
63   C CD1 . PHE   A 6   ? 0.1913 0.1945 0.1552 -0.0222 0.0217  0.0228  6   PHE   A CD1 
64   C CD2 . PHE   A 6   ? 0.2018 0.1977 0.1720 -0.0144 0.0347  0.0089  6   PHE   A CD2 
65   C CE1 . PHE   A 6   ? 0.1939 0.1919 0.1595 -0.0230 0.0258  0.0295  6   PHE   A CE1 
66   C CE2 . PHE   A 6   ? 0.2046 0.1958 0.1825 -0.0087 0.0313  -0.0013 6   PHE   A CE2 
67   C CZ  . PHE   A 6   ? 0.2005 0.1947 0.1777 -0.0201 0.0268  0.0081  6   PHE   A CZ  
77   N N   . SER   A 7   ? 0.2039 0.2418 0.1833 -0.0500 0.0662  -0.0090 7   SER   A N   
78   C CA  . SER   A 7   ? 0.2094 0.2506 0.2170 -0.0401 0.0704  -0.0177 7   SER   A CA  
79   C C   . SER   A 7   ? 0.1971 0.2119 0.2228 -0.0407 0.0737  -0.0073 7   SER   A C   
80   O O   . SER   A 7   ? 0.2081 0.2025 0.2318 -0.0468 0.0719  -0.0024 7   SER   A O   
81   C CB  . SER   A 7   ? 0.2312 0.2933 0.2526 -0.0284 0.0728  -0.0268 7   SER   A CB  
82   O OG  . SER   A 7   ? 0.2527 0.3099 0.2958 -0.0204 0.0738  -0.0333 7   SER   A OG  
88   N N   . GLY   A 8   ? 0.1848 0.2006 0.2316 -0.0397 0.0688  -0.0093 8   GLY   A N   
89   C CA  . GLY   A 8   ? 0.1770 0.1903 0.2411 -0.0256 0.0646  -0.0118 8   GLY   A CA  
90   C C   . GLY   A 8   ? 0.1614 0.1815 0.2247 -0.0189 0.0549  -0.0060 8   GLY   A C   
91   O O   . GLY   A 8   ? 0.1647 0.1886 0.2584 -0.0015 0.0389  -0.0205 8   GLY   A O   
95   N N   . TYR   A 9   ? 0.1466 0.1686 0.1985 -0.0193 0.0423  0.0071  9   TYR   A N   
96   C CA  . TYR   A 9   ? 0.1421 0.1575 0.1743 -0.0208 0.0332  0.0105  9   TYR   A CA  
97   C C   . TYR   A 9   ? 0.1441 0.1489 0.1809 -0.0201 0.0311  0.0311  9   TYR   A C   
98   O O   . TYR   A 9   ? 0.1765 0.1722 0.1974 -0.0364 0.0287  0.0307  9   TYR   A O   
99   C CB  . TYR   A 9   ? 0.1358 0.1643 0.1787 -0.0140 0.0272  0.0060  9   TYR   A CB  
100  C CG  . TYR   A 9   ? 0.1335 0.1698 0.1694 -0.0015 0.0320  -0.0024 9   TYR   A CG  
101  C CD1 . TYR   A 9   ? 0.1331 0.1790 0.1896 -0.0155 0.0389  -0.0019 9   TYR   A CD1 
102  C CD2 . TYR   A 9   ? 0.1327 0.1598 0.1737 0.0025  0.0267  0.0117  9   TYR   A CD2 
103  C CE1 . TYR   A 9   ? 0.1391 0.1809 0.1909 -0.0176 0.0415  -0.0084 9   TYR   A CE1 
104  C CE2 . TYR   A 9   ? 0.1311 0.1709 0.1858 0.0012  0.0358  0.0022  9   TYR   A CE2 
105  C CZ  . TYR   A 9   ? 0.1367 0.1774 0.1953 -0.0184 0.0453  0.0016  9   TYR   A CZ  
106  O OH  . TYR   A 9   ? 0.1491 0.1914 0.2123 -0.0308 0.0472  -0.0068 9   TYR   A OH  
116  N N   . LEU   A 10  ? 0.1294 0.1383 0.1827 -0.0132 0.0227  0.0311  10  LEU   A N   
117  C CA  . LEU   A 10  ? 0.1287 0.1413 0.1810 -0.0172 0.0184  0.0430  10  LEU   A CA  
118  C C   . LEU   A 10  ? 0.1254 0.1336 0.1626 -0.0200 0.0117  0.0391  10  LEU   A C   
119  O O   . LEU   A 10  ? 0.1344 0.1294 0.1835 -0.0175 0.0310  0.0408  10  LEU   A O   
120  C CB  . LEU   A 10  ? 0.1307 0.1553 0.2169 -0.0254 -0.0053 0.0589  10  LEU   A CB  
121  C CG  . LEU   A 10  ? 0.1738 0.1857 0.2616 -0.0328 -0.0404 0.0733  10  LEU   A CG  
122  C CD1 . LEU   A 10  ? 0.2094 0.2350 0.3266 -0.0435 -0.0138 0.0245  10  LEU   A CD1 
123  C CD2 . LEU   A 10  ? 0.2233 0.2226 0.3068 -0.0253 -0.0237 0.0410  10  LEU   A CD2 
135  N N   . LYS   A 11  ? 0.1237 0.1377 0.1539 -0.0189 0.0134  0.0394  11  LYS   A N   
136  C CA  . LYS   A 11  ? 0.1269 0.1344 0.1535 -0.0257 0.0048  0.0360  11  LYS   A CA  
137  C C   . LYS   A 11  ? 0.1295 0.1423 0.1524 -0.0313 0.0105  0.0345  11  LYS   A C   
138  O O   . LYS   A 11  ? 0.1413 0.1804 0.1762 -0.0599 0.0185  0.0100  11  LYS   A O   
139  C CB  . LYS   A 11  ? 0.1398 0.1275 0.1556 -0.0237 0.0030  0.0279  11  LYS   A CB  
140  C CG  . LYS   A 11  ? 0.1457 0.1262 0.1516 -0.0207 0.0148  0.0268  11  LYS   A CG  
141  C CD  . LYS   A 11  ? 0.1617 0.1343 0.1542 -0.0141 0.0141  0.0243  11  LYS   A CD  
142  C CE  . LYS   A 11  ? 0.1699 0.1268 0.1544 -0.0143 0.0088  0.0316  11  LYS   A CE  
143  N NZ  . LYS   A 11  ? 0.1670 0.1254 0.1558 -0.0063 -0.0074 0.0263  11  LYS   A NZ  
157  N N   . LEU   A 12  ? 0.1159 0.1383 0.1405 -0.0252 0.0043  0.0291  12  LEU   A N   
158  C CA  . LEU   A 12  ? 0.1156 0.1488 0.1442 -0.0211 0.0028  0.0403  12  LEU   A CA  
159  C C   . LEU   A 12  ? 0.1220 0.1406 0.1375 -0.0252 0.0064  0.0351  12  LEU   A C   
160  O O   . LEU   A 12  ? 0.1296 0.1472 0.1456 -0.0262 0.0016  0.0246  12  LEU   A O   
161  C CB  . LEU   A 12  ? 0.1266 0.1542 0.1635 -0.0226 -0.0053 0.0475  12  LEU   A CB  
162  C CG  . LEU   A 12  ? 0.1333 0.1643 0.1768 -0.0160 0.0042  0.0570  12  LEU   A CG  
163  C CD1 . LEU   A 12  ? 0.1476 0.1706 0.1874 -0.0068 0.0165  0.0616  12  LEU   A CD1 
164  C CD2 . LEU   A 12  ? 0.1355 0.1715 0.2004 -0.0089 -0.0004 0.0444  12  LEU   A CD2 
176  N N   . THR   A 13  ? 0.1173 0.1390 0.1490 -0.0240 0.0044  0.0282  13  THR   A N   
177  C CA  . THR   A 13  ? 0.1303 0.1364 0.1546 -0.0218 0.0069  0.0263  13  THR   A CA  
178  C C   . THR   A 13  ? 0.1279 0.1314 0.1516 -0.0239 0.0028  0.0292  13  THR   A C   
179  O O   . THR   A 13  ? 0.1313 0.1350 0.1544 -0.0154 0.0010  0.0272  13  THR   A O   
180  C CB  . THR   A 13  ? 0.1375 0.1490 0.1531 -0.0204 0.0160  0.0254  13  THR   A CB  
181  O OG1 . THR   A 13  ? 0.1320 0.1474 0.1595 -0.0254 0.0041  0.0262  13  THR   A OG1 
182  C CG2 . THR   A 13  ? 0.1424 0.1702 0.1748 -0.0211 0.0224  0.0201  13  THR   A CG2 
190  N N   . ASP   A 14  ? 0.1307 0.1341 0.1639 -0.0207 0.0062  0.0269  14  ASP   A N   
191  C CA  . ASP   A 14  ? 0.1334 0.1326 0.1648 -0.0163 0.0035  0.0341  14  ASP   A CA  
192  C C   . ASP   A 14  ? 0.1277 0.1374 0.1546 -0.0147 -0.0027 0.0359  14  ASP   A C   
193  O O   . ASP   A 14  ? 0.1498 0.1531 0.1758 -0.0344 -0.0113 0.0423  14  ASP   A O   
194  C CB  . ASP   A 14  ? 0.1582 0.1460 0.2125 -0.0187 0.0077  0.0364  14  ASP   A CB  
195  C CG  . ASP   A 14  ? 0.1791 0.1980 0.2886 -0.0133 0.0074  0.0382  14  ASP   A CG  
196  O OD1 . ASP   A 14  ? 0.1976 0.2127 0.2999 0.0001  -0.0053 0.0473  14  ASP   A OD1 
197  O OD2 . ASP   A 14  ? 0.2006 0.2429 0.3386 -0.0132 0.0020  0.0239  14  ASP   A OD2 
202  N N   . ASN   A 15  ? 0.1235 0.1278 0.1546 -0.0179 0.0045  0.0366  15  ASN   A N   
203  C CA  . ASN   A 15  ? 0.1216 0.1273 0.1611 -0.0167 -0.0009 0.0280  15  ASN   A CA  
204  C C   . ASN   A 15  ? 0.1187 0.1238 0.1813 -0.0143 0.0001  0.0285  15  ASN   A C   
205  O O   . ASN   A 15  ? 0.1191 0.1302 0.2360 -0.0135 -0.0202 0.0253  15  ASN   A O   
206  C CB  . ASN   A 15  ? 0.1187 0.1256 0.1710 -0.0128 -0.0016 0.0235  15  ASN   A CB  
207  C CG  . ASN   A 15  ? 0.1196 0.1298 0.1674 -0.0072 0.0033  0.0168  15  ASN   A CG  
208  O OD1 . ASN   A 15  ? 0.1384 0.1376 0.1810 -0.0238 0.0080  0.0157  15  ASN   A OD1 
209  N ND2 . ASN   A 15  ? 0.1202 0.1428 0.1647 -0.0137 0.0133  0.0125  15  ASN   A ND2 
216  N N   . VAL   A 16  ? 0.1182 0.1214 0.1656 -0.0128 0.0006  0.0300  16  VAL   A N   
217  C CA  . VAL   A 16  ? 0.1186 0.1261 0.1572 -0.0088 0.0073  0.0308  16  VAL   A CA  
218  C C   . VAL   A 16  ? 0.1187 0.1256 0.1445 -0.0121 0.0026  0.0332  16  VAL   A C   
219  O O   . VAL   A 16  ? 0.1105 0.1226 0.1570 -0.0176 0.0104  0.0206  16  VAL   A O   
220  C CB  . VAL   A 16  ? 0.1312 0.1398 0.1698 0.0031  0.0229  0.0388  16  VAL   A CB  
221  C CG1 . VAL   A 16  ? 0.1408 0.1501 0.1692 0.0111  0.0222  0.0483  16  VAL   A CG1 
222  C CG2 . VAL   A 16  ? 0.1431 0.1519 0.1823 0.0090  0.0381  0.0419  16  VAL   A CG2 
232  N N   A TYR   A 17  ? 0.1177 0.1201 0.1512 -0.0089 0.0118  0.0279  17  TYR   A N   
233  N N   B TYR   A 17  ? 0.1204 0.1249 0.1430 -0.0131 0.0065  0.0305  17  TYR   A N   
234  C CA  A TYR   A 17  ? 0.1195 0.1202 0.1476 -0.0095 0.0074  0.0322  17  TYR   A CA  
235  C CA  B TYR   A 17  ? 0.1226 0.1254 0.1428 -0.0142 0.0079  0.0292  17  TYR   A CA  
236  C C   A TYR   A 17  ? 0.1212 0.1191 0.1601 -0.0120 0.0114  0.0319  17  TYR   A C   
237  C C   B TYR   A 17  ? 0.1219 0.1239 0.1539 -0.0122 0.0135  0.0334  17  TYR   A C   
238  O O   A TYR   A 17  ? 0.1126 0.1226 0.1787 -0.0116 0.0193  0.0415  17  TYR   A O   
239  O O   B TYR   A 17  ? 0.1205 0.1242 0.1560 -0.0118 0.0153  0.0347  17  TYR   A O   
240  C CB  A TYR   A 17  ? 0.1310 0.1269 0.1502 -0.0085 0.0120  0.0295  17  TYR   A CB  
241  C CB  B TYR   A 17  ? 0.1267 0.1279 0.1365 -0.0186 0.0059  0.0243  17  TYR   A CB  
242  C CG  A TYR   A 17  ? 0.1430 0.1368 0.1446 -0.0152 0.0052  0.0210  17  TYR   A CG  
243  C CG  B TYR   A 17  ? 0.1301 0.1299 0.1295 -0.0235 0.0005  0.0190  17  TYR   A CG  
244  C CD1 A TYR   A 17  ? 0.1497 0.1489 0.1534 -0.0045 -0.0010 0.0243  17  TYR   A CD1 
245  C CD1 B TYR   A 17  ? 0.1298 0.1322 0.1248 -0.0238 -0.0001 0.0201  17  TYR   A CD1 
246  C CD2 A TYR   A 17  ? 0.1484 0.1403 0.1438 -0.0197 0.0029  0.0217  17  TYR   A CD2 
247  C CD2 B TYR   A 17  ? 0.1320 0.1297 0.1256 -0.0286 -0.0030 0.0187  17  TYR   A CD2 
248  C CE1 A TYR   A 17  ? 0.1597 0.1473 0.1616 -0.0058 -0.0063 0.0196  17  TYR   A CE1 
249  C CE1 B TYR   A 17  ? 0.1273 0.1295 0.1232 -0.0268 -0.0048 0.0201  17  TYR   A CE1 
250  C CE2 A TYR   A 17  ? 0.1628 0.1406 0.1538 -0.0237 0.0015  0.0126  17  TYR   A CE2 
251  C CE2 B TYR   A 17  ? 0.1327 0.1278 0.1230 -0.0310 -0.0063 0.0180  17  TYR   A CE2 
252  C CZ  A TYR   A 17  ? 0.1689 0.1369 0.1557 -0.0137 -0.0121 0.0256  17  TYR   A CZ  
253  C CZ  B TYR   A 17  ? 0.1316 0.1252 0.1201 -0.0317 -0.0088 0.0239  17  TYR   A CZ  
254  O OH  A TYR   A 17  ? 0.1835 0.1436 0.1639 -0.0045 -0.0083 0.0290  17  TYR   A OH  
255  O OH  B TYR   A 17  ? 0.1354 0.1221 0.1179 -0.0318 -0.0172 0.0294  17  TYR   A OH  
274  N N   . ILE   A 18  ? 0.1222 0.1236 0.1649 -0.0096 0.0192  0.0397  18  ILE   A N   
275  C CA  . ILE   A 18  ? 0.1149 0.1269 0.1766 -0.0087 0.0223  0.0379  18  ILE   A CA  
276  C C   . ILE   A 18  ? 0.1230 0.1326 0.1856 -0.0121 0.0185  0.0378  18  ILE   A C   
277  O O   . ILE   A 18  ? 0.1240 0.1411 0.1866 -0.0152 0.0334  0.0392  18  ILE   A O   
278  C CB  . ILE   A 18  ? 0.1322 0.1354 0.1695 -0.0035 0.0135  0.0555  18  ILE   A CB  
279  C CG1 . ILE   A 18  ? 0.1515 0.1467 0.1808 -0.0013 0.0011  0.0628  18  ILE   A CG1 
280  C CG2 . ILE   A 18  ? 0.1373 0.1445 0.1905 -0.0080 0.0075  0.0503  18  ILE   A CG2 
281  C CD1 . ILE   A 18  ? 0.1791 0.1663 0.2119 0.0003  -0.0090 0.0635  18  ILE   A CD1 
294  N N   A LYS   A 19  ? 0.1197 0.1308 0.2099 -0.0066 0.0395  0.0359  19  LYS   A N   
295  N N   B LYS   A 19  ? 0.1362 0.1429 0.1823 -0.0076 0.0194  0.0272  19  LYS   A N   
296  C CA  A LYS   A 19  ? 0.1320 0.1388 0.2464 0.0011  0.0472  0.0432  19  LYS   A CA  
297  C CA  B LYS   A 19  ? 0.1528 0.1543 0.1835 -0.0025 0.0191  0.0185  19  LYS   A CA  
298  C C   A LYS   A 19  ? 0.1285 0.1318 0.2616 0.0079  0.0464  0.0517  19  LYS   A C   
299  C C   B LYS   A 19  ? 0.1595 0.1575 0.1760 -0.0013 0.0150  0.0157  19  LYS   A C   
300  O O   A LYS   A 19  ? 0.1241 0.1316 0.2593 0.0046  0.0301  0.0540  19  LYS   A O   
301  O O   B LYS   A 19  ? 0.1602 0.1576 0.1675 0.0007  0.0155  0.0136  19  LYS   A O   
302  C CB  A LYS   A 19  ? 0.1442 0.1525 0.2575 0.0019  0.0553  0.0337  19  LYS   A CB  
303  C CB  B LYS   A 19  ? 0.1620 0.1617 0.1907 0.0007  0.0227  0.0112  19  LYS   A CB  
304  C CG  A LYS   A 19  ? 0.1783 0.1733 0.2739 0.0076  0.0541  0.0190  19  LYS   A CG  
305  C CG  B LYS   A 19  ? 0.1723 0.1687 0.2024 0.0040  0.0237  0.0047  19  LYS   A CG  
306  C CD  A LYS   A 19  ? 0.2071 0.1977 0.2755 0.0059  0.0591  0.0195  19  LYS   A CD  
307  C CD  B LYS   A 19  ? 0.1810 0.1763 0.2113 0.0062  0.0250  -0.0003 19  LYS   A CD  
308  C CE  A LYS   A 19  ? 0.2272 0.2077 0.2805 -0.0003 0.0544  0.0150  19  LYS   A CE  
309  C CE  B LYS   A 19  ? 0.1852 0.1803 0.2172 0.0054  0.0280  -0.0043 19  LYS   A CE  
310  N NZ  A LYS   A 19  ? 0.2403 0.2101 0.2761 -0.0161 0.0582  0.0091  19  LYS   A NZ  
311  N NZ  B LYS   A 19  ? 0.1873 0.1819 0.2182 0.0037  0.0311  -0.0102 19  LYS   A NZ  
338  N N   A ASN   A 20  ? 0.1343 0.1358 0.2934 0.0102  0.0482  0.0487  20  ASN   A N   
339  N N   B ASN   A 20  ? 0.1665 0.1616 0.1800 -0.0033 0.0098  0.0133  20  ASN   A N   
340  C CA  A ASN   A 20  ? 0.1472 0.1552 0.3113 0.0323  0.0562  0.0486  20  ASN   A CA  
341  C CA  B ASN   A 20  ? 0.1736 0.1675 0.1824 -0.0035 0.0060  0.0080  20  ASN   A CA  
342  C C   A ASN   A 20  ? 0.1724 0.1506 0.3036 0.0218  0.0633  0.0394  20  ASN   A C   
343  C C   B ASN   A 20  ? 0.1812 0.1713 0.1814 -0.0023 0.0026  0.0049  20  ASN   A C   
344  O O   A ASN   A 20  ? 0.1974 0.1687 0.3176 -0.0011 0.0649  0.0340  20  ASN   A O   
345  O O   B ASN   A 20  ? 0.1857 0.1741 0.1865 -0.0050 0.0055  0.0052  20  ASN   A O   
346  C CB  A ASN   A 20  ? 0.1535 0.1813 0.3394 0.0463  0.0575  0.0640  20  ASN   A CB  
347  C CB  B ASN   A 20  ? 0.1743 0.1698 0.1865 -0.0052 0.0058  0.0067  20  ASN   A CB  
348  C CG  A ASN   A 20  ? 0.1693 0.1924 0.3692 0.0568  0.0546  0.0819  20  ASN   A CG  
349  C CG  B ASN   A 20  ? 0.1757 0.1700 0.1906 -0.0082 0.0041  0.0012  20  ASN   A CG  
350  O OD1 A ASN   A 20  ? 0.1966 0.2044 0.3926 0.0656  0.0602  0.0746  20  ASN   A OD1 
351  O OD1 B ASN   A 20  ? 0.1776 0.1720 0.1966 -0.0093 -0.0010 -0.0024 20  ASN   A OD1 
352  N ND2 A ASN   A 20  ? 0.1761 0.1981 0.3852 0.0503  0.0454  0.0887  20  ASN   A ND2 
353  N ND2 B ASN   A 20  ? 0.1758 0.1695 0.1883 -0.0092 0.0050  0.0000  20  ASN   A ND2 
366  N N   A ALA   A 21  ? 0.1768 0.1493 0.2965 0.0168  0.0586  0.0270  21  ALA   A N   
367  N N   B ALA   A 21  ? 0.1852 0.1742 0.1822 -0.0007 -0.0044 0.0004  21  ALA   A N   
368  C CA  A ALA   A 21  ? 0.1774 0.1528 0.2875 0.0100  0.0626  0.0219  21  ALA   A CA  
369  C CA  B ALA   A 21  ? 0.1888 0.1781 0.1858 0.0013  -0.0067 -0.0027 21  ALA   A CA  
370  C C   A ALA   A 21  ? 0.1656 0.1514 0.2703 0.0081  0.0608  0.0181  21  ALA   A C   
371  C C   B ALA   A 21  ? 0.1875 0.1794 0.1855 0.0072  -0.0094 -0.0023 21  ALA   A C   
372  O O   A ALA   A 21  ? 0.1714 0.1626 0.2673 0.0069  0.0475  0.0089  21  ALA   A O   
373  O O   B ALA   A 21  ? 0.1893 0.1829 0.1834 0.0100  -0.0101 0.0025  21  ALA   A O   
374  C CB  A ALA   A 21  ? 0.1997 0.1674 0.3038 0.0009  0.0467  0.0327  21  ALA   A CB  
375  C CB  B ALA   A 21  ? 0.1937 0.1808 0.1912 -0.0006 -0.0088 -0.0034 21  ALA   A CB  
386  N N   A ASP   A 22  ? 0.1652 0.1521 0.2676 -0.0001 0.0601  0.0178  22  ASP   A N   
387  N N   B ASP   A 22  ? 0.1857 0.1794 0.1897 0.0082  -0.0112 -0.0058 22  ASP   A N   
388  C CA  A ASP   A 22  ? 0.1658 0.1617 0.2611 -0.0011 0.0520  0.0164  22  ASP   A CA  
389  C CA  B ASP   A 22  ? 0.1837 0.1807 0.1914 0.0095  -0.0087 -0.0062 22  ASP   A CA  
390  C C   A ASP   A 22  ? 0.1568 0.1733 0.2236 -0.0045 0.0531  0.0185  22  ASP   A C   
391  C C   B ASP   A 22  ? 0.1807 0.1835 0.1751 0.0058  -0.0071 -0.0049 22  ASP   A C   
392  O O   A ASP   A 22  ? 0.1666 0.1981 0.2266 -0.0069 0.0622  0.0265  22  ASP   A O   
393  O O   B ASP   A 22  ? 0.1808 0.1883 0.1707 0.0047  -0.0049 -0.0046 22  ASP   A O   
394  C CB  A ASP   A 22  ? 0.1907 0.1707 0.3160 -0.0034 0.0391  0.0118  22  ASP   A CB  
395  C CB  B ASP   A 22  ? 0.1855 0.1795 0.2080 0.0127  -0.0060 -0.0063 22  ASP   A CB  
396  C CG  A ASP   A 22  ? 0.2136 0.1831 0.3802 -0.0095 0.0223  0.0218  22  ASP   A CG  
397  C CG  B ASP   A 22  ? 0.1847 0.1774 0.2218 0.0148  -0.0043 -0.0077 22  ASP   A CG  
398  O OD1 A ASP   A 22  ? 0.2075 0.1865 0.3954 -0.0237 0.0197  0.0442  22  ASP   A OD1 
399  O OD1 B ASP   A 22  ? 0.1815 0.1741 0.2232 0.0146  -0.0010 -0.0101 22  ASP   A OD1 
400  O OD2 A ASP   A 22  ? 0.2423 0.1960 0.4197 -0.0054 0.0194  0.0079  22  ASP   A OD2 
401  O OD2 B ASP   A 22  ? 0.1884 0.1791 0.2301 0.0156  -0.0027 -0.0111 22  ASP   A OD2 
410  N N   A ILE   A 23  ? 0.1536 0.1701 0.2081 -0.0040 0.0492  0.0139  23  ILE   A N   
411  N N   B ILE   A 23  ? 0.1791 0.1827 0.1658 0.0029  -0.0053 -0.0032 23  ILE   A N   
412  C CA  A ILE   A 23  ? 0.1532 0.1623 0.1874 -0.0084 0.0415  0.0242  23  ILE   A CA  
413  C CA  B ILE   A 23  ? 0.1766 0.1796 0.1584 0.0006  -0.0000 -0.0028 23  ILE   A CA  
414  C C   A ILE   A 23  ? 0.1537 0.1770 0.1787 -0.0137 0.0556  0.0116  23  ILE   A C   
415  C C   B ILE   A 23  ? 0.1770 0.1834 0.1600 -0.0007 0.0032  -0.0069 23  ILE   A C   
416  O O   A ILE   A 23  ? 0.1620 0.1806 0.1810 -0.0062 0.0506  0.0026  23  ILE   A O   
417  O O   B ILE   A 23  ? 0.1777 0.1848 0.1598 0.0014  0.0031  -0.0060 23  ILE   A O   
418  C CB  A ILE   A 23  ? 0.1551 0.1549 0.1630 -0.0057 0.0324  0.0222  23  ILE   A CB  
419  C CB  B ILE   A 23  ? 0.1750 0.1751 0.1529 -0.0001 0.0029  0.0010  23  ILE   A CB  
420  C CG1 A ILE   A 23  ? 0.1616 0.1577 0.1524 -0.0036 0.0268  0.0137  23  ILE   A CG1 
421  C CG1 B ILE   A 23  ? 0.1753 0.1722 0.1460 -0.0001 0.0066  0.0025  23  ILE   A CG1 
422  C CG2 A ILE   A 23  ? 0.1597 0.1536 0.1717 -0.0037 0.0343  0.0223  23  ILE   A CG2 
423  C CG2 B ILE   A 23  ? 0.1745 0.1744 0.1545 0.0008  0.0026  0.0050  23  ILE   A CG2 
424  C CD1 A ILE   A 23  ? 0.1637 0.1567 0.1541 -0.0053 0.0150  0.0062  23  ILE   A CD1 
425  C CD1 B ILE   A 23  ? 0.1746 0.1707 0.1411 -0.0011 0.0080  0.0032  23  ILE   A CD1 
448  N N   A VAL   A 24  ? 0.1693 0.1835 0.1937 -0.0226 0.0580  0.0081  24  VAL   A N   
449  N N   B VAL   A 24  ? 0.1797 0.1861 0.1661 -0.0040 0.0072  -0.0126 24  VAL   A N   
450  C CA  A VAL   A 24  ? 0.1854 0.1934 0.2183 -0.0263 0.0548  0.0017  24  VAL   A CA  
451  C CA  B VAL   A 24  ? 0.1829 0.1897 0.1736 -0.0084 0.0089  -0.0195 24  VAL   A CA  
452  C C   A VAL   A 24  ? 0.1954 0.2017 0.2221 -0.0275 0.0619  -0.0070 24  VAL   A C   
453  C C   B VAL   A 24  ? 0.1908 0.1996 0.1843 -0.0116 0.0099  -0.0190 24  VAL   A C   
454  O O   A VAL   A 24  ? 0.2042 0.1957 0.2228 -0.0160 0.0583  -0.0108 24  VAL   A O   
455  O O   B VAL   A 24  ? 0.1909 0.1988 0.1815 -0.0104 0.0076  -0.0220 24  VAL   A O   
456  C CB  A VAL   A 24  ? 0.1951 0.2007 0.2429 -0.0301 0.0542  0.0083  24  VAL   A CB  
457  C CB  B VAL   A 24  ? 0.1795 0.1854 0.1711 -0.0092 0.0115  -0.0256 24  VAL   A CB  
458  C CG1 A VAL   A 24  ? 0.2051 0.2068 0.2562 -0.0316 0.0484  0.0039  24  VAL   A CG1 
459  C CG1 B VAL   A 24  ? 0.1792 0.1848 0.1703 -0.0093 0.0136  -0.0281 24  VAL   A CG1 
460  C CG2 A VAL   A 24  ? 0.2061 0.2146 0.2534 -0.0275 0.0620  0.0156  24  VAL   A CG2 
461  C CG2 B VAL   A 24  ? 0.1792 0.1854 0.1718 -0.0101 0.0122  -0.0259 24  VAL   A CG2 
480  N N   A GLU   A 25  ? 0.2036 0.2328 0.2337 -0.0257 0.0780  -0.0142 25  GLU   A N   
481  N N   B GLU   A 25  ? 0.2009 0.2135 0.2001 -0.0130 0.0154  -0.0143 25  GLU   A N   
482  C CA  A GLU   A 25  ? 0.2236 0.2625 0.2436 -0.0215 0.0961  -0.0165 25  GLU   A CA  
483  C CA  B GLU   A 25  ? 0.2129 0.2271 0.2163 -0.0142 0.0218  -0.0094 25  GLU   A CA  
484  C C   A GLU   A 25  ? 0.2179 0.2630 0.2159 -0.0352 0.0986  -0.0139 25  GLU   A C   
485  C C   B GLU   A 25  ? 0.2163 0.2345 0.2042 -0.0155 0.0224  -0.0103 25  GLU   A C   
486  O O   A GLU   A 25  ? 0.2266 0.2712 0.2246 -0.0368 0.0983  -0.0134 25  GLU   A O   
487  O O   B GLU   A 25  ? 0.2166 0.2352 0.2002 -0.0151 0.0255  -0.0100 25  GLU   A O   
488  C CB  A GLU   A 25  ? 0.2467 0.2877 0.2868 -0.0091 0.1064  -0.0164 25  GLU   A CB  
489  C CB  B GLU   A 25  ? 0.2210 0.2316 0.2441 -0.0148 0.0264  -0.0034 25  GLU   A CB  
490  C CG  A GLU   A 25  ? 0.2742 0.3128 0.3426 -0.0057 0.0942  -0.0121 25  GLU   A CG  
491  C CG  B GLU   A 25  ? 0.2286 0.2366 0.2708 -0.0171 0.0267  0.0023  25  GLU   A CG  
492  C CD  A GLU   A 25  ? 0.2941 0.3367 0.3838 -0.0058 0.0908  -0.0059 25  GLU   A CD  
493  C CD  B GLU   A 25  ? 0.2338 0.2408 0.2916 -0.0204 0.0269  0.0060  25  GLU   A CD  
494  O OE1 A GLU   A 25  ? 0.3022 0.3467 0.3953 -0.0034 0.0799  -0.0101 25  GLU   A OE1 
495  O OE1 B GLU   A 25  ? 0.2346 0.2433 0.2978 -0.0209 0.0270  0.0073  25  GLU   A OE1 
496  O OE2 A GLU   A 25  ? 0.3023 0.3440 0.4081 -0.0053 0.0898  -0.0091 25  GLU   A OE2 
497  O OE2 B GLU   A 25  ? 0.2369 0.2397 0.2964 -0.0225 0.0290  0.0076  25  GLU   A OE2 
510  N N   A GLU   A 26  ? 0.2040 0.2517 0.2097 -0.0514 0.0978  -0.0154 26  GLU   A N   
511  N N   B GLU   A 26  ? 0.2193 0.2397 0.1992 -0.0177 0.0188  -0.0128 26  GLU   A N   
512  C CA  A GLU   A 26  ? 0.2121 0.2395 0.1968 -0.0680 0.0841  -0.0087 26  GLU   A CA  
513  C CA  B GLU   A 26  ? 0.2247 0.2442 0.1970 -0.0194 0.0150  -0.0137 26  GLU   A CA  
514  C C   A GLU   A 26  ? 0.2031 0.2210 0.1696 -0.0627 0.0694  -0.0130 26  GLU   A C   
515  C C   B GLU   A 26  ? 0.2306 0.2447 0.1836 -0.0185 0.0136  -0.0139 26  GLU   A C   
516  O O   A GLU   A 26  ? 0.2095 0.2216 0.1671 -0.0674 0.0686  -0.0108 26  GLU   A O   
517  O O   B GLU   A 26  ? 0.2295 0.2428 0.1795 -0.0180 0.0129  -0.0146 26  GLU   A O   
518  C CB  A GLU   A 26  ? 0.2410 0.2340 0.2398 -0.0841 0.0665  0.0039  26  GLU   A CB  
519  C CB  B GLU   A 26  ? 0.2256 0.2480 0.2146 -0.0213 0.0124  -0.0141 26  GLU   A CB  
520  C CG  A GLU   A 26  ? 0.2705 0.2389 0.2930 -0.0870 0.0696  -0.0026 26  GLU   A CG  
521  C CG  B GLU   A 26  ? 0.2270 0.2508 0.2388 -0.0217 0.0090  -0.0155 26  GLU   A CG  
522  C CD  A GLU   A 26  ? 0.2854 0.2345 0.3163 -0.1008 0.0965  -0.0050 26  GLU   A CD  
523  C CD  B GLU   A 26  ? 0.2269 0.2529 0.2576 -0.0234 0.0079  -0.0183 26  GLU   A CD  
524  O OE1 A GLU   A 26  ? 0.2783 0.2669 0.3128 -0.0804 0.1288  -0.0588 26  GLU   A OE1 
525  O OE1 B GLU   A 26  ? 0.2253 0.2597 0.2558 -0.0203 0.0116  -0.0242 26  GLU   A OE1 
526  O OE2 A GLU   A 26  ? 0.3079 0.2344 0.3201 -0.0943 0.0970  0.0132  26  GLU   A OE2 
527  O OE2 B GLU   A 26  ? 0.2281 0.2508 0.2682 -0.0260 0.0019  -0.0218 26  GLU   A OE2 
540  N N   A ALA   A 27  ? 0.1827 0.1965 0.1494 -0.0602 0.0608  -0.0119 27  ALA   A N   
541  N N   B ALA   A 27  ? 0.2375 0.2475 0.1804 -0.0192 0.0130  -0.0132 27  ALA   A N   
542  C CA  A ALA   A 27  ? 0.1902 0.1900 0.1384 -0.0519 0.0566  -0.0136 27  ALA   A CA  
543  C CA  B ALA   A 27  ? 0.2467 0.2526 0.1814 -0.0198 0.0145  -0.0128 27  ALA   A CA  
544  C C   A ALA   A 27  ? 0.2203 0.1957 0.1487 -0.0549 0.0602  -0.0274 27  ALA   A C   
545  C C   B ALA   A 27  ? 0.2590 0.2603 0.1897 -0.0226 0.0188  -0.0135 27  ALA   A C   
546  O O   A ALA   A 27  ? 0.2280 0.1930 0.1512 -0.0575 0.0510  -0.0245 27  ALA   A O   
547  O O   B ALA   A 27  ? 0.2587 0.2602 0.1872 -0.0216 0.0138  -0.0118 27  ALA   A O   
548  C CB  A ALA   A 27  ? 0.1763 0.1844 0.1474 -0.0476 0.0477  -0.0165 27  ALA   A CB  
549  C CB  B ALA   A 27  ? 0.2450 0.2514 0.1796 -0.0190 0.0137  -0.0122 27  ALA   A CB  
560  N N   A LYS   A 28  ? 0.2565 0.2181 0.1703 -0.0480 0.0563  -0.0556 28  LYS   A N   
561  N N   B LYS   A 28  ? 0.2733 0.2694 0.2042 -0.0266 0.0285  -0.0180 28  LYS   A N   
562  C CA  A LYS   A 28  ? 0.2967 0.2515 0.2144 -0.0419 0.0517  -0.0695 28  LYS   A CA  
563  C CA  B LYS   A 28  ? 0.2882 0.2794 0.2203 -0.0309 0.0395  -0.0226 28  LYS   A CA  
564  C C   A LYS   A 28  ? 0.3110 0.2783 0.1969 -0.0444 0.0582  -0.0624 28  LYS   A C   
565  C C   B LYS   A 28  ? 0.3006 0.2872 0.2036 -0.0384 0.0570  -0.0320 28  LYS   A C   
566  O O   A LYS   A 28  ? 0.3223 0.2923 0.2365 -0.0447 0.0417  -0.0519 28  LYS   A O   
567  O O   B LYS   A 28  ? 0.3024 0.2886 0.2112 -0.0380 0.0545  -0.0287 28  LYS   A O   
568  C CB  A LYS   A 28  ? 0.3171 0.2639 0.2637 -0.0323 0.0473  -0.0864 28  LYS   A CB  
569  C CB  B LYS   A 28  ? 0.2901 0.2817 0.2480 -0.0277 0.0343  -0.0180 28  LYS   A CB  
570  C CG  A LYS   A 28  ? 0.3327 0.2776 0.3130 -0.0252 0.0431  -0.0905 28  LYS   A CG  
571  C CG  B LYS   A 28  ? 0.2917 0.2840 0.2726 -0.0249 0.0300  -0.0140 28  LYS   A CG  
572  C CD  A LYS   A 28  ? 0.3466 0.2986 0.3764 -0.0187 0.0370  -0.0811 28  LYS   A CD  
573  C CD  B LYS   A 28  ? 0.2933 0.2868 0.2942 -0.0228 0.0262  -0.0098 28  LYS   A CD  
574  C CE  A LYS   A 28  ? 0.3569 0.3123 0.4228 -0.0159 0.0322  -0.0748 28  LYS   A CE  
575  C CE  B LYS   A 28  ? 0.2941 0.2879 0.3086 -0.0221 0.0234  -0.0074 28  LYS   A CE  
576  N NZ  A LYS   A 28  ? 0.3643 0.3206 0.4513 -0.0121 0.0309  -0.0688 28  LYS   A NZ  
577  N NZ  B LYS   A 28  ? 0.2945 0.2888 0.3170 -0.0217 0.0219  -0.0060 28  LYS   A NZ  
604  N N   . LYS   A 29  ? 0.3104 0.2933 0.1834 -0.0464 0.0766  -0.0436 29  LYS   A N   
605  C CA  . LYS   A 29  ? 0.3289 0.3232 0.1995 -0.0536 0.0954  -0.0265 29  LYS   A CA  
606  C C   . LYS   A 29  ? 0.3231 0.3143 0.1584 -0.0596 0.0923  -0.0251 29  LYS   A C   
607  O O   . LYS   A 29  ? 0.3342 0.3261 0.1712 -0.0509 0.0832  -0.0286 29  LYS   A O   
608  C CB  . LYS   A 29  ? 0.3477 0.3601 0.2628 -0.0535 0.1181  -0.0130 29  LYS   A CB  
609  C CG  . LYS   A 29  ? 0.3677 0.3875 0.3429 -0.0538 0.1264  -0.0070 29  LYS   A CG  
610  C CD  . LYS   A 29  ? 0.3875 0.4099 0.4215 -0.0526 0.1259  -0.0094 29  LYS   A CD  
611  C CE  . LYS   A 29  ? 0.4018 0.4283 0.4755 -0.0511 0.1278  -0.0112 29  LYS   A CE  
612  N NZ  . LYS   A 29  ? 0.4086 0.4380 0.5071 -0.0503 0.1288  -0.0131 29  LYS   A NZ  
627  N N   . VAL   A 30  ? 0.3057 0.2934 0.1469 -0.0715 0.0916  -0.0181 30  VAL   A N   
628  C CA  . VAL   A 30  ? 0.2962 0.2734 0.1447 -0.0807 0.0658  -0.0047 30  VAL   A CA  
629  C C   . VAL   A 30  ? 0.2935 0.2589 0.1199 -0.0782 0.0452  0.0095  30  VAL   A C   
630  O O   . VAL   A 30  ? 0.3019 0.2659 0.1174 -0.0827 0.0329  0.0169  30  VAL   A O   
631  C CB  . VAL   A 30  ? 0.2919 0.2678 0.1781 -0.0931 0.0481  0.0004  30  VAL   A CB  
632  C CG1 . VAL   A 30  ? 0.2969 0.2664 0.1919 -0.0933 0.0300  0.0009  30  VAL   A CG1 
633  C CG2 . VAL   A 30  ? 0.2925 0.2749 0.2118 -0.0926 0.0498  0.0016  30  VAL   A CG2 
643  N N   A LYS   A 31  ? 0.2786 0.2407 0.0988 -0.0761 0.0416  -0.0061 31  LYS   A N   
644  N N   B LYS   A 31  ? 0.2920 0.2536 0.1437 -0.0725 0.0360  0.0054  31  LYS   A N   
645  C CA  A LYS   A 31  ? 0.2899 0.2421 0.1004 -0.0725 0.0186  -0.0141 31  LYS   A CA  
646  C CA  B LYS   A 31  ? 0.2914 0.2499 0.1694 -0.0655 0.0233  0.0031  31  LYS   A CA  
647  C C   A LYS   A 31  ? 0.2765 0.2258 0.0878 -0.0630 0.0157  0.0161  31  LYS   A C   
648  C C   B LYS   A 31  ? 0.2749 0.2315 0.1298 -0.0620 0.0189  0.0082  31  LYS   A C   
649  O O   A LYS   A 31  ? 0.2818 0.2376 0.1108 -0.0604 0.0060  0.0285  31  LYS   A O   
650  O O   B LYS   A 31  ? 0.2775 0.2356 0.1362 -0.0617 0.0180  0.0109  31  LYS   A O   
651  C CB  A LYS   A 31  ? 0.3214 0.2639 0.1899 -0.0688 -0.0002 -0.0368 31  LYS   A CB  
652  C CB  B LYS   A 31  ? 0.3075 0.2638 0.2356 -0.0612 0.0155  -0.0024 31  LYS   A CB  
653  C CG  A LYS   A 31  ? 0.3614 0.2916 0.3239 -0.0566 -0.0173 -0.0473 31  LYS   A CG  
654  C CG  B LYS   A 31  ? 0.3220 0.2768 0.3005 -0.0547 0.0076  -0.0071 31  LYS   A CG  
655  C CD  A LYS   A 31  ? 0.3904 0.3131 0.4293 -0.0479 -0.0325 -0.0541 31  LYS   A CD  
656  C CD  B LYS   A 31  ? 0.3334 0.2871 0.3510 -0.0498 0.0001  -0.0114 31  LYS   A CD  
657  C CE  A LYS   A 31  ? 0.4078 0.3310 0.4915 -0.0421 -0.0463 -0.0627 31  LYS   A CE  
658  C CE  B LYS   A 31  ? 0.3406 0.2939 0.3842 -0.0465 -0.0051 -0.0146 31  LYS   A CE  
659  N NZ  A LYS   A 31  ? 0.4153 0.3399 0.5245 -0.0402 -0.0538 -0.0662 31  LYS   A NZ  
660  N NZ  B LYS   A 31  ? 0.3440 0.2972 0.4016 -0.0451 -0.0080 -0.0158 31  LYS   A NZ  
687  N N   . PRO   A 32  ? 0.2554 0.2108 0.0839 -0.0581 0.0162  0.0108  32  PRO   A N   
688  C CA  . PRO   A 32  ? 0.2429 0.1941 0.1061 -0.0520 0.0017  0.0124  32  PRO   A CA  
689  C C   . PRO   A 32  ? 0.2350 0.1929 0.1076 -0.0410 -0.0133 0.0193  32  PRO   A C   
690  O O   . PRO   A 32  ? 0.2265 0.1875 0.1227 -0.0452 -0.0235 0.0246  32  PRO   A O   
691  C CB  . PRO   A 32  ? 0.2364 0.2021 0.1200 -0.0528 0.0012  0.0080  32  PRO   A CB  
692  C CG  . PRO   A 32  ? 0.2303 0.2052 0.0858 -0.0490 0.0023  0.0114  32  PRO   A CG  
693  C CD  . PRO   A 32  ? 0.2375 0.2026 0.0776 -0.0512 0.0119  0.0089  32  PRO   A CD  
701  N N   . THR   A 33  ? 0.2417 0.1913 0.1144 -0.0370 -0.0103 0.0241  33  THR   A N   
702  C CA  . THR   A 33  ? 0.2361 0.1916 0.1229 -0.0248 -0.0206 0.0311  33  THR   A CA  
703  C C   . THR   A 33  ? 0.2038 0.1752 0.1090 -0.0246 -0.0216 0.0251  33  THR   A C   
704  O O   . THR   A 33  ? 0.1963 0.1822 0.1235 -0.0232 -0.0398 0.0246  33  THR   A O   
705  C CB  . THR   A 33  ? 0.2637 0.2108 0.1372 -0.0130 -0.0340 0.0509  33  THR   A CB  
706  O OG1 . THR   A 33  ? 0.2876 0.2218 0.1693 -0.0076 -0.0235 0.0649  33  THR   A OG1 
707  C CG2 . THR   A 33  ? 0.2669 0.2217 0.1657 -0.0039 -0.0421 0.0521  33  THR   A CG2 
715  N N   . VAL   A 34  ? 0.1814 0.1624 0.1007 -0.0245 -0.0165 0.0242  34  VAL   A N   
716  C CA  . VAL   A 34  ? 0.1641 0.1481 0.0929 -0.0199 -0.0036 0.0212  34  VAL   A CA  
717  C C   . VAL   A 34  ? 0.1521 0.1439 0.0859 -0.0181 0.0021  0.0116  34  VAL   A C   
718  O O   . VAL   A 34  ? 0.1567 0.1420 0.1127 -0.0289 -0.0004 0.0187  34  VAL   A O   
719  C CB  . VAL   A 34  ? 0.1721 0.1448 0.1105 -0.0180 -0.0022 0.0118  34  VAL   A CB  
720  C CG1 . VAL   A 34  ? 0.1754 0.1463 0.1209 -0.0167 0.0081  0.0085  34  VAL   A CG1 
721  C CG2 . VAL   A 34  ? 0.1780 0.1559 0.1366 -0.0068 -0.0182 0.0091  34  VAL   A CG2 
731  N N   . VAL   A 35  ? 0.1387 0.1362 0.0907 -0.0242 -0.0030 0.0080  35  VAL   A N   
732  C CA  . VAL   A 35  ? 0.1270 0.1350 0.0906 -0.0216 0.0004  0.0084  35  VAL   A CA  
733  C C   . VAL   A 35  ? 0.1141 0.1214 0.0910 -0.0189 0.0022  0.0110  35  VAL   A C   
734  O O   . VAL   A 35  ? 0.1200 0.1359 0.0965 -0.0213 0.0067  0.0024  35  VAL   A O   
735  C CB  . VAL   A 35  ? 0.1388 0.1429 0.0951 -0.0131 0.0143  -0.0002 35  VAL   A CB  
736  C CG1 . VAL   A 35  ? 0.1455 0.1440 0.1152 -0.0073 0.0038  -0.0124 35  VAL   A CG1 
737  C CG2 . VAL   A 35  ? 0.1390 0.1416 0.1176 -0.0108 0.0211  -0.0061 35  VAL   A CG2 
747  N N   . VAL   A 36  ? 0.1063 0.1294 0.0807 -0.0147 0.0084  0.0110  36  VAL   A N   
748  C CA  . VAL   A 36  ? 0.1056 0.1152 0.0893 -0.0084 0.0087  0.0026  36  VAL   A CA  
749  C C   . VAL   A 36  ? 0.1043 0.1103 0.0912 -0.0084 0.0060  0.0061  36  VAL   A C   
750  O O   . VAL   A 36  ? 0.1130 0.1112 0.1135 -0.0027 0.0185  0.0078  36  VAL   A O   
751  C CB  . VAL   A 36  ? 0.1066 0.1053 0.1048 -0.0098 0.0029  0.0079  36  VAL   A CB  
752  C CG1 . VAL   A 36  ? 0.1134 0.1104 0.1103 -0.0148 0.0100  0.0021  36  VAL   A CG1 
753  C CG2 . VAL   A 36  ? 0.1168 0.1039 0.1206 -0.0039 -0.0021 0.0106  36  VAL   A CG2 
763  N N   . ASN   A 37  ? 0.0992 0.1072 0.0965 -0.0036 0.0033  0.0101  37  ASN   A N   
764  C CA  . ASN   A 37  ? 0.1052 0.1037 0.0835 0.0043  0.0075  0.0142  37  ASN   A CA  
765  C C   . ASN   A 37  ? 0.1059 0.1008 0.0940 -0.0014 0.0140  0.0156  37  ASN   A C   
766  O O   . ASN   A 37  ? 0.1122 0.1134 0.0916 0.0056  0.0062  0.0075  37  ASN   A O   
767  C CB  . ASN   A 37  ? 0.1058 0.1068 0.1023 0.0012  0.0008  0.0056  37  ASN   A CB  
768  C CG  . ASN   A 37  ? 0.1060 0.1048 0.1118 0.0023  0.0014  0.0081  37  ASN   A CG  
769  O OD1 . ASN   A 37  ? 0.1088 0.1092 0.1265 0.0012  0.0037  0.0126  37  ASN   A OD1 
770  N ND2 . ASN   A 37  ? 0.1092 0.1079 0.1144 -0.0019 -0.0002 0.0195  37  ASN   A ND2 
777  N N   A ALA   A 38  ? 0.1052 0.1105 0.1024 0.0027  0.0066  0.0011  38  ALA   A N   
778  N N   B ALA   A 38  ? 0.1070 0.1072 0.0985 -0.0014 0.0070  0.0102  38  ALA   A N   
779  C CA  A ALA   A 38  ? 0.1092 0.1165 0.1018 0.0009  -0.0019 0.0013  38  ALA   A CA  
780  C CA  B ALA   A 38  ? 0.1091 0.1132 0.1040 -0.0019 0.0003  0.0064  38  ALA   A CA  
781  C C   A ALA   A 38  ? 0.1091 0.1184 0.0940 0.0072  -0.0071 0.0015  38  ALA   A C   
782  C C   B ALA   A 38  ? 0.1066 0.1145 0.1006 0.0017  -0.0037 0.0049  38  ALA   A C   
783  O O   A ALA   A 38  ? 0.1092 0.1183 0.1117 0.0090  -0.0064 0.0031  38  ALA   A O   
784  O O   B ALA   A 38  ? 0.1031 0.1176 0.1020 0.0005  -0.0098 0.0099  38  ALA   A O   
785  C CB  A ALA   A 38  ? 0.1176 0.1463 0.1199 -0.0121 -0.0032 0.0049  38  ALA   A CB  
786  C CB  B ALA   A 38  ? 0.1132 0.1199 0.1144 -0.0056 -0.0043 0.0008  38  ALA   A CB  
797  N N   . ALA   A 39  ? 0.1091 0.1127 0.1033 0.0053  0.0021  0.0033  39  ALA   A N   
798  C CA  . ALA   A 39  ? 0.1148 0.1110 0.1052 0.0005  0.0056  0.0010  39  ALA   A CA  
799  C C   . ALA   A 39  ? 0.1163 0.1088 0.0989 0.0037  0.0065  0.0049  39  ALA   A C   
800  O O   . ALA   A 39  ? 0.1263 0.1125 0.0981 -0.0019 0.0059  0.0010  39  ALA   A O   
801  C CB  . ALA   A 39  ? 0.1145 0.1305 0.1198 0.0008  -0.0047 0.0034  39  ALA   A CB  
808  N N   A ASN   A 40  ? 0.1248 0.1180 0.1095 -0.0031 0.0197  0.0008  40  ASN   A N   
809  N N   B ASN   A 40  ? 0.1194 0.1093 0.1044 0.0025  0.0055  0.0047  40  ASN   A N   
810  C CA  A ASN   A 40  ? 0.1334 0.1127 0.1144 0.0016  0.0120  0.0023  40  ASN   A CA  
811  C CA  B ASN   A 40  ? 0.1224 0.1079 0.1069 0.0036  0.0013  0.0080  40  ASN   A CA  
812  C C   A ASN   A 40  ? 0.1355 0.1044 0.0930 -0.0043 0.0273  0.0123  40  ASN   A C   
813  C C   B ASN   A 40  ? 0.1305 0.1108 0.1096 0.0065  0.0090  0.0136  40  ASN   A C   
814  O O   A ASN   A 40  ? 0.1285 0.1052 0.0995 -0.0055 0.0240  0.0097  40  ASN   A O   
815  O O   B ASN   A 40  ? 0.1293 0.1085 0.1098 0.0089  0.0118  0.0108  40  ASN   A O   
816  C CB  A ASN   A 40  ? 0.1440 0.1202 0.1265 0.0051  -0.0025 0.0028  40  ASN   A CB  
817  C CB  B ASN   A 40  ? 0.1191 0.1040 0.1041 0.0008  -0.0079 0.0074  40  ASN   A CB  
818  C CG  A ASN   A 40  ? 0.1468 0.1202 0.1390 0.0043  -0.0022 0.0065  40  ASN   A CG  
819  C CG  B ASN   A 40  ? 0.1152 0.0996 0.1059 -0.0030 -0.0107 0.0084  40  ASN   A CG  
820  O OD1 A ASN   A 40  ? 0.1498 0.1183 0.1558 -0.0006 0.0071  0.0045  40  ASN   A OD1 
821  O OD1 B ASN   A 40  ? 0.1106 0.0961 0.0895 -0.0064 -0.0048 0.0171  40  ASN   A OD1 
822  N ND2 A ASN   A 40  ? 0.1520 0.1343 0.1675 0.0109  -0.0043 -0.0050 40  ASN   A ND2 
823  N ND2 B ASN   A 40  ? 0.1144 0.1017 0.1201 -0.0031 -0.0124 0.0017  40  ASN   A ND2 
836  N N   A VAL   A 41  ? 0.1437 0.0998 0.1038 -0.0016 0.0273  0.0146  41  VAL   A N   
837  N N   B VAL   A 41  ? 0.1390 0.1161 0.1135 0.0067  0.0098  0.0218  41  VAL   A N   
838  C CA  A VAL   A 41  ? 0.1421 0.1099 0.1160 -0.0012 0.0340  0.0101  41  VAL   A CA  
839  C CA  B VAL   A 41  ? 0.1448 0.1218 0.1096 0.0067  0.0163  0.0277  41  VAL   A CA  
840  C C   A VAL   A 41  ? 0.1353 0.1126 0.1222 0.0016  0.0352  0.0107  41  VAL   A C   
841  C C   B VAL   A 41  ? 0.1495 0.1306 0.1167 0.0083  0.0152  0.0249  41  VAL   A C   
842  O O   A VAL   A 41  ? 0.1371 0.1054 0.1477 0.0027  0.0300  -0.0019 41  VAL   A O   
843  O O   B VAL   A 41  ? 0.1524 0.1312 0.1189 0.0083  0.0131  0.0224  41  VAL   A O   
844  C CB  A VAL   A 41  ? 0.1559 0.1194 0.1121 -0.0023 0.0417  0.0102  41  VAL   A CB  
845  C CB  B VAL   A 41  ? 0.1469 0.1200 0.1048 0.0049  0.0253  0.0345  41  VAL   A CB  
846  C CG1 A VAL   A 41  ? 0.1684 0.1260 0.1158 0.0021  0.0377  0.0041  41  VAL   A CG1 
847  C CG1 B VAL   A 41  ? 0.1503 0.1209 0.0998 0.0021  0.0349  0.0355  41  VAL   A CG1 
848  C CG2 A VAL   A 41  ? 0.1703 0.1313 0.1178 -0.0060 0.0370  0.0108  41  VAL   A CG2 
849  C CG2 B VAL   A 41  ? 0.1468 0.1211 0.1091 0.0056  0.0216  0.0377  41  VAL   A CG2 
868  N N   A TYR   A 42  ? 0.1245 0.1076 0.1330 -0.0026 0.0302  0.0232  42  TYR   A N   
869  N N   B TYR   A 42  ? 0.1502 0.1352 0.1200 0.0085  0.0136  0.0248  42  TYR   A N   
870  C CA  A TYR   A 42  ? 0.1235 0.1064 0.1420 -0.0074 0.0344  0.0187  42  TYR   A CA  
871  C CA  B TYR   A 42  ? 0.1516 0.1424 0.1280 0.0058  0.0135  0.0155  42  TYR   A CA  
872  C C   A TYR   A 42  ? 0.1139 0.1025 0.1427 -0.0033 0.0223  0.0187  42  TYR   A C   
873  C C   B TYR   A 42  ? 0.1490 0.1411 0.1153 0.0050  0.0106  0.0198  42  TYR   A C   
874  O O   A TYR   A 42  ? 0.1204 0.1055 0.1593 -0.0099 0.0192  0.0051  42  TYR   A O   
875  O O   B TYR   A 42  ? 0.1496 0.1416 0.1157 0.0024  0.0123  0.0189  42  TYR   A O   
876  C CB  A TYR   A 42  ? 0.1485 0.1136 0.1429 -0.0058 0.0384  0.0306  42  TYR   A CB  
877  C CB  B TYR   A 42  ? 0.1579 0.1513 0.1492 0.0037  0.0153  0.0069  42  TYR   A CB  
878  C CG  A TYR   A 42  ? 0.1689 0.1288 0.1516 -0.0124 0.0309  0.0351  42  TYR   A CG  
879  C CG  B TYR   A 42  ? 0.1647 0.1604 0.1664 -0.0004 0.0169  -0.0001 42  TYR   A CG  
880  C CD1 A TYR   A 42  ? 0.1773 0.1425 0.1525 -0.0149 0.0369  0.0256  42  TYR   A CD1 
881  C CD1 B TYR   A 42  ? 0.1692 0.1659 0.1783 -0.0010 0.0156  -0.0064 42  TYR   A CD1 
882  C CD2 A TYR   A 42  ? 0.1764 0.1544 0.1658 -0.0093 0.0322  0.0294  42  TYR   A CD2 
883  C CD2 B TYR   A 42  ? 0.1676 0.1671 0.1765 -0.0012 0.0178  -0.0030 42  TYR   A CD2 
884  C CE1 A TYR   A 42  ? 0.1840 0.1560 0.1451 -0.0197 0.0439  0.0288  42  TYR   A CE1 
885  C CE1 B TYR   A 42  ? 0.1723 0.1714 0.1869 -0.0028 0.0156  -0.0075 42  TYR   A CE1 
886  C CE2 A TYR   A 42  ? 0.1908 0.1675 0.1732 -0.0227 0.0258  0.0319  42  TYR   A CE2 
887  C CE2 B TYR   A 42  ? 0.1708 0.1727 0.1855 -0.0042 0.0178  -0.0049 42  TYR   A CE2 
888  C CZ  A TYR   A 42  ? 0.1963 0.1706 0.1500 -0.0235 0.0370  0.0343  42  TYR   A CZ  
889  C CZ  B TYR   A 42  ? 0.1733 0.1748 0.1889 -0.0042 0.0170  -0.0071 42  TYR   A CZ  
890  O OH  A TYR   A 42  ? 0.2033 0.1970 0.1736 -0.0380 0.0346  0.0268  42  TYR   A OH  
891  O OH  B TYR   A 42  ? 0.1773 0.1804 0.1964 -0.0053 0.0155  -0.0078 42  TYR   A OH  
910  N N   A LEU   A 43  ? 0.1126 0.1025 0.1308 -0.0035 0.0129  0.0112  43  LEU   A N   
911  N N   B LEU   A 43  ? 0.1457 0.1406 0.1123 0.0075  0.0035  0.0172  43  LEU   A N   
912  C CA  A LEU   A 43  ? 0.1053 0.1014 0.1255 -0.0032 0.0146  0.0073  43  LEU   A CA  
913  C CA  B LEU   A 43  ? 0.1446 0.1398 0.1119 0.0083  0.0007  0.0125  43  LEU   A CA  
914  C C   A LEU   A 43  ? 0.1088 0.1034 0.1324 -0.0014 0.0076  -0.0000 43  LEU   A C   
915  C C   B LEU   A 43  ? 0.1474 0.1419 0.1145 0.0113  -0.0002 0.0043  43  LEU   A C   
916  O O   A LEU   A 43  ? 0.1293 0.1087 0.1466 0.0013  -0.0015 0.0052  43  LEU   A O   
917  O O   B LEU   A 43  ? 0.1499 0.1428 0.1098 0.0135  -0.0069 -0.0003 43  LEU   A O   
918  C CB  A LEU   A 43  ? 0.1130 0.1024 0.1249 -0.0051 0.0144  0.0039  43  LEU   A CB  
919  C CB  B LEU   A 43  ? 0.1428 0.1346 0.1090 0.0087  -0.0038 0.0177  43  LEU   A CB  
920  C CG  A LEU   A 43  ? 0.1203 0.1063 0.1247 -0.0006 0.0077  0.0066  43  LEU   A CG  
921  C CG  B LEU   A 43  ? 0.1400 0.1310 0.1025 0.0105  -0.0098 0.0178  43  LEU   A CG  
922  C CD1 A LEU   A 43  ? 0.1286 0.1166 0.1367 -0.0021 0.0087  0.0063  43  LEU   A CD1 
923  C CD1 B LEU   A 43  ? 0.1400 0.1301 0.0983 0.0127  -0.0127 0.0181  43  LEU   A CD1 
924  C CD2 A LEU   A 43  ? 0.1340 0.1128 0.1316 -0.0049 0.0079  0.0095  43  LEU   A CD2 
925  C CD2 B LEU   A 43  ? 0.1411 0.1295 0.0967 0.0105  -0.0090 0.0225  43  LEU   A CD2 
948  N N   A LYS   A 44  ? 0.1145 0.1058 0.1249 -0.0017 0.0082  0.0083  44  LYS   A N   
949  N N   B LYS   A 44  ? 0.1496 0.1452 0.1249 0.0130  0.0017  0.0031  44  LYS   A N   
950  C CA  A LYS   A 44  ? 0.1232 0.1037 0.1312 -0.0025 0.0149  0.0148  44  LYS   A CA  
951  C CA  B LYS   A 44  ? 0.1552 0.1487 0.1392 0.0146  0.0023  0.0015  44  LYS   A CA  
952  C C   A LYS   A 44  ? 0.1165 0.1025 0.1225 0.0020  0.0062  0.0104  44  LYS   A C   
953  C C   B LYS   A 44  ? 0.1491 0.1418 0.1258 0.0163  -0.0028 -0.0052 44  LYS   A C   
954  O O   A LYS   A 44  ? 0.1206 0.1186 0.1314 0.0003  0.0047  -0.0011 44  LYS   A O   
955  O O   B LYS   A 44  ? 0.1505 0.1396 0.1217 0.0180  -0.0062 -0.0117 44  LYS   A O   
956  C CB  A LYS   A 44  ? 0.1512 0.1171 0.1734 0.0009  0.0288  0.0307  44  LYS   A CB  
957  C CB  B LYS   A 44  ? 0.1675 0.1615 0.1715 0.0148  0.0084  0.0036  44  LYS   A CB  
958  C CG  A LYS   A 44  ? 0.1817 0.1455 0.2410 -0.0107 0.0577  0.0437  44  LYS   A CG  
959  C CG  B LYS   A 44  ? 0.1791 0.1714 0.2061 0.0143  0.0164  0.0015  44  LYS   A CG  
960  C CD  A LYS   A 44  ? 0.2249 0.2028 0.3653 -0.0121 0.0424  0.0251  44  LYS   A CD  
961  C CD  B LYS   A 44  ? 0.1901 0.1821 0.2436 0.0149  0.0156  -0.0018 44  LYS   A CD  
962  C CE  A LYS   A 44  ? 0.2446 0.2324 0.4438 -0.0115 0.0361  0.0197  44  LYS   A CE  
963  C CE  B LYS   A 44  ? 0.1946 0.1862 0.2681 0.0165  0.0144  -0.0049 44  LYS   A CE  
964  N NZ  A LYS   A 44  ? 0.2508 0.2478 0.4823 -0.0102 0.0368  0.0190  44  LYS   A NZ  
965  N NZ  B LYS   A 44  ? 0.1942 0.1851 0.2798 0.0183  0.0140  -0.0077 44  LYS   A NZ  
992  N N   A HIS   A 45  ? 0.1097 0.1015 0.1214 0.0011  0.0026  0.0122  45  HIS   A N   
993  N N   B HIS   A 45  ? 0.1440 0.1396 0.1236 0.0140  -0.0061 -0.0029 45  HIS   A N   
994  C CA  A HIS   A 45  ? 0.1088 0.1050 0.1192 0.0012  -0.0028 0.0110  45  HIS   A CA  
995  C CA  B HIS   A 45  ? 0.1395 0.1370 0.1224 0.0114  -0.0098 -0.0001 45  HIS   A CA  
996  C C   A HIS   A 45  ? 0.1109 0.1214 0.1300 0.0034  0.0026  0.0114  45  HIS   A C   
997  C C   B HIS   A 45  ? 0.1407 0.1401 0.1332 0.0118  -0.0063 0.0068  45  HIS   A C   
998  O O   A HIS   A 45  ? 0.1249 0.1240 0.1516 0.0146  -0.0042 -0.0066 45  HIS   A O   
999  O O   B HIS   A 45  ? 0.1409 0.1387 0.1425 0.0102  -0.0093 0.0068  45  HIS   A O   
1000 C CB  A HIS   A 45  ? 0.1073 0.1021 0.1253 0.0050  -0.0003 -0.0015 45  HIS   A CB  
1001 C CB  B HIS   A 45  ? 0.1331 0.1325 0.1144 0.0134  -0.0131 -0.0057 45  HIS   A CB  
1002 C CG  A HIS   A 45  ? 0.1095 0.1010 0.1027 -0.0065 0.0082  0.0010  45  HIS   A CG  
1003 C CG  B HIS   A 45  ? 0.1263 0.1278 0.1020 0.0125  -0.0081 -0.0095 45  HIS   A CG  
1004 N ND1 A HIS   A 45  ? 0.1050 0.1038 0.1200 -0.0051 0.0085  0.0062  45  HIS   A ND1 
1005 N ND1 B HIS   A 45  ? 0.1231 0.1264 0.1057 0.0140  -0.0093 -0.0054 45  HIS   A ND1 
1006 C CD2 A HIS   A 45  ? 0.1093 0.1059 0.1187 -0.0100 -0.0012 0.0095  45  HIS   A CD2 
1007 C CD2 B HIS   A 45  ? 0.1217 0.1213 0.0877 0.0099  -0.0067 -0.0171 45  HIS   A CD2 
1008 C CE1 A HIS   A 45  ? 0.1038 0.1058 0.1136 -0.0066 0.0031  0.0156  45  HIS   A CE1 
1009 C CE1 B HIS   A 45  ? 0.1179 0.1175 0.0840 0.0095  -0.0122 -0.0171 45  HIS   A CE1 
1010 N NE2 A HIS   A 45  ? 0.1047 0.1124 0.1173 -0.0029 0.0008  0.0094  45  HIS   A NE2 
1011 N NE2 B HIS   A 45  ? 0.1166 0.1178 0.0718 0.0074  -0.0119 -0.0265 45  HIS   A NE2 
1026 N N   A GLY   A 46  ? 0.1205 0.1343 0.1510 0.0142  -0.0110 0.0172  46  GLY   A N   
1027 N N   B GLY   A 46  ? 0.1432 0.1426 0.1364 0.0153  -0.0057 0.0140  46  GLY   A N   
1028 C CA  A GLY   A 46  ? 0.1317 0.1370 0.1697 0.0177  -0.0092 0.0233  46  GLY   A CA  
1029 C CA  B GLY   A 46  ? 0.1434 0.1416 0.1385 0.0153  -0.0049 0.0177  46  GLY   A CA  
1030 C C   A GLY   A 46  ? 0.1342 0.1326 0.1609 0.0273  -0.0169 0.0280  46  GLY   A C   
1031 C C   B GLY   A 46  ? 0.1413 0.1378 0.1365 0.0186  -0.0064 0.0170  46  GLY   A C   
1032 O O   A GLY   A 46  ? 0.1396 0.1413 0.1918 0.0266  -0.0265 0.0146  46  GLY   A O   
1033 O O   B GLY   A 46  ? 0.1422 0.1407 0.1320 0.0157  0.0001  0.0111  46  GLY   A O   
1040 N N   . GLY   A 47  ? 0.1405 0.1341 0.1492 0.0231  -0.0152 0.0216  47  GLY   A N   
1041 C CA  . GLY   A 47  ? 0.1450 0.1359 0.1577 0.0183  -0.0346 0.0169  47  GLY   A CA  
1042 C C   . GLY   A 47  ? 0.1403 0.1275 0.1377 0.0197  -0.0384 -0.0043 47  GLY   A C   
1043 O O   . GLY   A 47  ? 0.1393 0.1278 0.1406 0.0254  -0.0322 0.0053  47  GLY   A O   
1048 N N   A GLY   A 48  ? 0.1411 0.1309 0.1513 0.0180  -0.0443 -0.0058 48  GLY   A N   
1049 N N   B GLY   A 48  ? 0.1393 0.1305 0.1369 0.0153  -0.0277 -0.0062 48  GLY   A N   
1050 C CA  A GLY   A 48  ? 0.1395 0.1229 0.1648 0.0087  -0.0388 -0.0134 48  GLY   A CA  
1051 C CA  B GLY   A 48  ? 0.1368 0.1307 0.1332 0.0096  -0.0176 -0.0073 48  GLY   A CA  
1052 C C   A GLY   A 48  ? 0.1203 0.1174 0.1500 0.0048  -0.0166 -0.0094 48  GLY   A C   
1053 C C   B GLY   A 48  ? 0.1310 0.1311 0.1266 0.0042  -0.0055 -0.0038 48  GLY   A C   
1054 O O   A GLY   A 48  ? 0.1325 0.1148 0.1609 0.0085  -0.0207 -0.0123 48  GLY   A O   
1055 O O   B GLY   A 48  ? 0.1338 0.1337 0.1233 0.0022  -0.0087 -0.0052 48  GLY   A O   
1062 N N   A VAL   A 49  ? 0.1059 0.1103 0.1440 -0.0006 -0.0052 -0.0068 49  VAL   A N   
1063 N N   B VAL   A 49  ? 0.1246 0.1291 0.1273 0.0018  0.0033  -0.0000 49  VAL   A N   
1064 C CA  A VAL   A 49  ? 0.1171 0.1111 0.1359 -0.0067 0.0135  -0.0057 49  VAL   A CA  
1065 C CA  B VAL   A 49  ? 0.1182 0.1269 0.1204 0.0032  0.0106  0.0062  49  VAL   A CA  
1066 C C   A VAL   A 49  ? 0.1114 0.1039 0.1151 -0.0002 0.0071  -0.0019 49  VAL   A C   
1067 C C   B VAL   A 49  ? 0.1165 0.1208 0.1006 0.0030  0.0145  0.0045  49  VAL   A C   
1068 O O   A VAL   A 49  ? 0.1140 0.1086 0.1240 -0.0085 0.0146  -0.0056 49  VAL   A O   
1069 O O   B VAL   A 49  ? 0.1185 0.1187 0.0835 0.0082  0.0201  0.0027  49  VAL   A O   
1070 C CB  A VAL   A 49  ? 0.1410 0.1124 0.1445 -0.0164 0.0108  -0.0008 49  VAL   A CB  
1071 C CB  B VAL   A 49  ? 0.1133 0.1259 0.1264 0.0071  0.0074  0.0132  49  VAL   A CB  
1072 C CG1 A VAL   A 49  ? 0.1575 0.1158 0.1580 -0.0097 0.0131  0.0042  49  VAL   A CG1 
1073 C CG1 B VAL   A 49  ? 0.1077 0.1234 0.1209 0.0132  0.0027  0.0183  49  VAL   A CG1 
1074 C CG2 A VAL   A 49  ? 0.1535 0.1305 0.1921 -0.0315 0.0067  -0.0066 49  VAL   A CG2 
1075 C CG2 B VAL   A 49  ? 0.1138 0.1276 0.1328 0.0075  0.0073  0.0129  49  VAL   A CG2 
1094 N N   A ALA   A 50  ? 0.1069 0.0990 0.1025 -0.0009 -0.0031 0.0035  50  ALA   A N   
1095 N N   B ALA   A 50  ? 0.1158 0.1173 0.1030 0.0029  0.0142  0.0008  50  ALA   A N   
1096 C CA  A ALA   A 50  ? 0.1011 0.1009 0.1044 -0.0044 -0.0004 0.0125  50  ALA   A CA  
1097 C CA  B ALA   A 50  ? 0.1182 0.1150 0.1079 -0.0020 0.0091  0.0029  50  ALA   A CA  
1098 C C   A ALA   A 50  ? 0.0988 0.1043 0.1049 -0.0046 0.0009  -0.0018 50  ALA   A C   
1099 C C   B ALA   A 50  ? 0.1196 0.1117 0.1095 -0.0022 0.0002  0.0022  50  ALA   A C   
1100 O O   A ALA   A 50  ? 0.1068 0.1071 0.1145 0.0019  -0.0028 0.0015  50  ALA   A O   
1101 O O   B ALA   A 50  ? 0.1193 0.1077 0.1108 -0.0016 -0.0050 0.0082  50  ALA   A O   
1102 C CB  A ALA   A 50  ? 0.1027 0.0993 0.1090 -0.0025 -0.0009 0.0066  50  ALA   A CB  
1103 C CB  B ALA   A 50  ? 0.1200 0.1128 0.1097 -0.0051 0.0203  -0.0002 50  ALA   A CB  
1114 N N   A GLY   A 51  ? 0.1060 0.0982 0.1211 0.0033  -0.0155 -0.0012 51  GLY   A N   
1115 N N   B GLY   A 51  ? 0.1210 0.1119 0.1137 -0.0011 -0.0057 -0.0011 51  GLY   A N   
1116 C CA  A GLY   A 51  ? 0.1180 0.0995 0.1308 0.0100  -0.0145 -0.0027 51  GLY   A CA  
1117 C CA  B GLY   A 51  ? 0.1235 0.1127 0.1182 -0.0010 -0.0053 -0.0054 51  GLY   A CA  
1118 C C   A GLY   A 51  ? 0.1037 0.1081 0.1303 0.0056  -0.0126 -0.0077 51  GLY   A C   
1119 C C   B GLY   A 51  ? 0.1209 0.1146 0.1222 -0.0002 -0.0053 -0.0090 51  GLY   A C   
1120 O O   A GLY   A 51  ? 0.1066 0.1084 0.1431 0.0000  -0.0091 -0.0081 51  GLY   A O   
1121 O O   B GLY   A 51  ? 0.1238 0.1161 0.1218 0.0003  -0.0074 -0.0144 51  GLY   A O   
1128 N N   A ALA   A 52  ? 0.1079 0.1147 0.1194 0.0028  -0.0030 -0.0205 52  ALA   A N   
1129 N N   B ALA   A 52  ? 0.1173 0.1155 0.1251 0.0006  -0.0023 -0.0066 52  ALA   A N   
1130 C CA  A ALA   A 52  ? 0.1062 0.1237 0.1369 -0.0012 -0.0036 -0.0194 52  ALA   A CA  
1131 C CA  B ALA   A 52  ? 0.1142 0.1164 0.1289 0.0013  -0.0006 -0.0096 52  ALA   A CA  
1132 C C   A ALA   A 52  ? 0.1052 0.1244 0.1158 -0.0117 0.0047  -0.0140 52  ALA   A C   
1133 C C   B ALA   A 52  ? 0.1121 0.1166 0.1219 -0.0014 -0.0005 -0.0071 52  ALA   A C   
1134 O O   A ALA   A 52  ? 0.1195 0.1303 0.1209 -0.0080 0.0060  -0.0206 52  ALA   A O   
1135 O O   B ALA   A 52  ? 0.1147 0.1169 0.1227 -0.0002 0.0008  -0.0059 52  ALA   A O   
1136 C CB  A ALA   A 52  ? 0.1215 0.1391 0.1515 -0.0064 -0.0033 -0.0199 52  ALA   A CB  
1137 C CB  B ALA   A 52  ? 0.1135 0.1195 0.1333 0.0015  -0.0003 -0.0139 52  ALA   A CB  
1148 N N   A LEU   A 53  ? 0.1067 0.1173 0.1140 -0.0057 0.0054  -0.0097 53  LEU   A N   
1149 N N   B LEU   A 53  ? 0.1101 0.1149 0.1164 -0.0011 -0.0046 -0.0084 53  LEU   A N   
1150 C CA  A LEU   A 53  ? 0.1168 0.1201 0.1098 -0.0057 0.0074  -0.0000 53  LEU   A CA  
1151 C CA  B LEU   A 53  ? 0.1104 0.1155 0.1072 -0.0009 -0.0105 -0.0097 53  LEU   A CA  
1152 C C   A LEU   A 53  ? 0.1116 0.1193 0.1021 0.0044  0.0007  0.0007  53  LEU   A C   
1153 C C   B LEU   A 53  ? 0.1080 0.1127 0.0979 0.0019  -0.0098 -0.0062 53  LEU   A C   
1154 O O   A LEU   A 53  ? 0.1294 0.1313 0.1084 -0.0103 0.0004  0.0027  53  LEU   A O   
1155 O O   B LEU   A 53  ? 0.1133 0.1082 0.0915 0.0014  -0.0111 -0.0126 53  LEU   A O   
1156 C CB  A LEU   A 53  ? 0.1259 0.1223 0.1112 -0.0039 0.0132  0.0020  53  LEU   A CB  
1157 C CB  B LEU   A 53  ? 0.1104 0.1178 0.1058 -0.0052 -0.0163 -0.0138 53  LEU   A CB  
1158 C CG  A LEU   A 53  ? 0.1477 0.1237 0.1165 -0.0100 0.0135  0.0096  53  LEU   A CG  
1159 C CG  B LEU   A 53  ? 0.1158 0.1204 0.1094 -0.0095 -0.0203 -0.0174 53  LEU   A CG  
1160 C CD1 A LEU   A 53  ? 0.1513 0.1300 0.1322 -0.0069 0.0109  0.0087  53  LEU   A CD1 
1161 C CD1 B LEU   A 53  ? 0.1138 0.1206 0.1000 -0.0091 -0.0286 -0.0243 53  LEU   A CD1 
1162 C CD2 A LEU   A 53  ? 0.1771 0.1330 0.1351 -0.0218 0.0188  0.0116  53  LEU   A CD2 
1163 C CD2 B LEU   A 53  ? 0.1243 0.1225 0.1218 -0.0152 -0.0152 -0.0192 53  LEU   A CD2 
1186 N N   A ASN   A 54  ? 0.1098 0.1150 0.1001 0.0008  -0.0001 0.0012  54  ASN   A N   
1187 N N   B ASN   A 54  ? 0.1050 0.1160 0.1018 0.0047  -0.0052 0.0000  54  ASN   A N   
1188 C CA  A ASN   A 54  ? 0.1009 0.1124 0.1080 -0.0001 -0.0066 -0.0066 54  ASN   A CA  
1189 C CA  B ASN   A 54  ? 0.1022 0.1188 0.1071 0.0044  -0.0033 0.0034  54  ASN   A CA  
1190 C C   A ASN   A 54  ? 0.1100 0.1194 0.1044 -0.0058 0.0016  -0.0029 54  ASN   A C   
1191 C C   B ASN   A 54  ? 0.1058 0.1181 0.1140 0.0010  -0.0027 0.0006  54  ASN   A C   
1192 O O   A ASN   A 54  ? 0.1124 0.1206 0.1126 -0.0067 -0.0021 -0.0111 54  ASN   A O   
1193 O O   B ASN   A 54  ? 0.1060 0.1176 0.1184 0.0012  -0.0058 0.0054  54  ASN   A O   
1194 C CB  A ASN   A 54  ? 0.0995 0.1133 0.1180 -0.0077 -0.0045 -0.0088 54  ASN   A CB  
1195 C CB  B ASN   A 54  ? 0.1034 0.1212 0.1087 0.0100  -0.0004 0.0099  54  ASN   A CB  
1196 C CG  A ASN   A 54  ? 0.1053 0.1119 0.1109 -0.0009 -0.0066 -0.0046 54  ASN   A CG  
1197 C CG  B ASN   A 54  ? 0.1050 0.1220 0.1154 0.0164  -0.0005 0.0144  54  ASN   A CG  
1198 O OD1 A ASN   A 54  ? 0.1059 0.1118 0.1153 -0.0041 -0.0111 0.0019  54  ASN   A OD1 
1199 O OD1 B ASN   A 54  ? 0.1074 0.1254 0.1243 0.0169  -0.0008 0.0210  54  ASN   A OD1 
1200 N ND2 A ASN   A 54  ? 0.1029 0.1194 0.1422 -0.0063 -0.0196 0.0010  54  ASN   A ND2 
1201 N ND2 B ASN   A 54  ? 0.1040 0.1200 0.1183 0.0203  -0.0028 0.0135  54  ASN   A ND2 
1214 N N   . LYS   A 55  ? 0.1088 0.1177 0.1264 -0.0000 -0.0052 -0.0121 55  LYS   A N   
1215 C CA  . LYS   A 55  ? 0.1154 0.1211 0.1288 0.0034  -0.0066 -0.0170 55  LYS   A CA  
1216 C C   . LYS   A 55  ? 0.1151 0.1344 0.1325 0.0009  0.0022  -0.0193 55  LYS   A C   
1217 O O   . LYS   A 55  ? 0.1283 0.1435 0.1336 0.0032  -0.0029 -0.0305 55  LYS   A O   
1218 C CB  . LYS   A 55  ? 0.1276 0.1272 0.1412 0.0103  -0.0089 -0.0186 55  LYS   A CB  
1219 C CG  . LYS   A 55  ? 0.1310 0.1494 0.1551 0.0174  -0.0089 -0.0226 55  LYS   A CG  
1220 C CD  . LYS   A 55  ? 0.1387 0.1696 0.1587 0.0245  0.0034  -0.0218 55  LYS   A CD  
1221 C CE  . LYS   A 55  ? 0.1573 0.2003 0.1826 0.0323  -0.0149 -0.0243 55  LYS   A CE  
1222 N NZ  . LYS   A 55  ? 0.1607 0.2135 0.1994 0.0352  -0.0122 -0.0192 55  LYS   A NZ  
1237 N N   . ALA   A 56  ? 0.1174 0.1425 0.1216 -0.0075 0.0043  -0.0231 56  ALA   A N   
1238 C CA  . ALA   A 56  ? 0.1311 0.1552 0.1308 -0.0070 0.0108  -0.0158 56  ALA   A CA  
1239 C C   . ALA   A 56  ? 0.1371 0.1605 0.1077 -0.0068 0.0080  -0.0251 56  ALA   A C   
1240 O O   . ALA   A 56  ? 0.1440 0.1946 0.1305 0.0065  0.0109  -0.0215 56  ALA   A O   
1241 C CB  . ALA   A 56  ? 0.1460 0.1747 0.1362 -0.0162 0.0133  -0.0051 56  ALA   A CB  
1247 N N   . THR   A 57  ? 0.1241 0.1387 0.1124 -0.0035 0.0038  -0.0137 57  THR   A N   
1248 C CA  . THR   A 57  ? 0.1268 0.1412 0.1196 -0.0025 -0.0028 -0.0169 57  THR   A CA  
1249 C C   . THR   A 57  ? 0.1250 0.1471 0.1236 -0.0029 -0.0041 -0.0264 57  THR   A C   
1250 O O   . THR   A 57  ? 0.1271 0.1525 0.1399 -0.0039 -0.0115 -0.0316 57  THR   A O   
1251 C CB  . THR   A 57  ? 0.1237 0.1401 0.1157 -0.0018 -0.0021 -0.0101 57  THR   A CB  
1252 O OG1 . THR   A 57  ? 0.1140 0.1355 0.1190 0.0009  -0.0040 -0.0098 57  THR   A OG1 
1253 C CG2 . THR   A 57  ? 0.1322 0.1433 0.1075 -0.0033 0.0001  -0.0103 57  THR   A CG2 
1261 N N   . ASN   A 58  ? 0.1247 0.1437 0.1370 -0.0036 0.0022  -0.0323 58  ASN   A N   
1262 C CA  . ASN   A 58  ? 0.1496 0.1376 0.1542 -0.0066 0.0087  -0.0385 58  ASN   A CA  
1263 C C   . ASN   A 58  ? 0.1319 0.1274 0.1440 -0.0001 -0.0080 -0.0234 58  ASN   A C   
1264 O O   . ASN   A 58  ? 0.1315 0.1360 0.1590 -0.0114 -0.0069 -0.0309 58  ASN   A O   
1265 C CB  . ASN   A 58  ? 0.1956 0.1590 0.1987 -0.0200 0.0245  -0.0578 58  ASN   A CB  
1266 C CG  . ASN   A 58  ? 0.2386 0.1808 0.2590 -0.0152 0.0290  -0.0543 58  ASN   A CG  
1267 O OD1 . ASN   A 58  ? 0.2561 0.1777 0.2900 0.0145  0.0560  -0.0471 58  ASN   A OD1 
1268 N ND2 . ASN   A 58  ? 0.2553 0.1938 0.2845 -0.0207 0.0160  -0.0496 58  ASN   A ND2 
1275 N N   . ASN   A 59  ? 0.1151 0.1222 0.1314 -0.0048 -0.0150 -0.0148 59  ASN   A N   
1276 C CA  . ASN   A 59  ? 0.1155 0.1120 0.1380 -0.0053 -0.0072 -0.0128 59  ASN   A CA  
1277 C C   . ASN   A 59  ? 0.1125 0.1154 0.1336 -0.0039 -0.0087 -0.0126 59  ASN   A C   
1278 O O   . ASN   A 59  ? 0.1140 0.1199 0.1395 -0.0045 -0.0018 -0.0041 59  ASN   A O   
1279 C CB  . ASN   A 59  ? 0.1161 0.1131 0.1532 -0.0002 -0.0171 -0.0155 59  ASN   A CB  
1280 C CG  . ASN   A 59  ? 0.1199 0.1173 0.1481 -0.0005 -0.0240 -0.0052 59  ASN   A CG  
1281 O OD1 . ASN   A 59  ? 0.1330 0.1284 0.1402 -0.0096 -0.0284 0.0051  59  ASN   A OD1 
1282 N ND2 . ASN   A 59  ? 0.1310 0.1214 0.1630 -0.0104 -0.0163 -0.0029 59  ASN   A ND2 
1289 N N   . ALA   A 60  ? 0.1108 0.1200 0.1341 0.0013  -0.0081 -0.0117 60  ALA   A N   
1290 C CA  . ALA   A 60  ? 0.1092 0.1233 0.1363 0.0011  -0.0118 -0.0108 60  ALA   A CA  
1291 C C   . ALA   A 60  ? 0.1144 0.1128 0.1313 0.0012  -0.0054 -0.0039 60  ALA   A C   
1292 O O   . ALA   A 60  ? 0.1103 0.1195 0.1510 -0.0028 -0.0086 -0.0070 60  ALA   A O   
1293 C CB  . ALA   A 60  ? 0.1270 0.1372 0.1433 -0.0001 -0.0207 -0.0191 60  ALA   A CB  
1299 N N   . MET   A 61  ? 0.1105 0.1121 0.1329 -0.0054 -0.0063 -0.0059 61  MET   A N   
1300 C CA  . MET   A 61  ? 0.1086 0.1122 0.1262 -0.0033 -0.0041 -0.0038 61  MET   A CA  
1301 C C   . MET   A 61  ? 0.1015 0.1050 0.1292 -0.0070 -0.0061 -0.0040 61  MET   A C   
1302 O O   . MET   A 61  ? 0.1110 0.1054 0.1352 -0.0008 0.0042  -0.0016 61  MET   A O   
1303 C CB  . MET   A 61  ? 0.1122 0.1116 0.1242 -0.0043 -0.0051 -0.0053 61  MET   A CB  
1304 C CG  . MET   A 61  ? 0.1141 0.1233 0.1292 0.0022  -0.0017 -0.0099 61  MET   A CG  
1305 S SD  . MET   A 61  ? 0.1201 0.1200 0.1653 -0.0085 -0.0009 -0.0212 61  MET   A SD  
1306 C CE  . MET   A 61  ? 0.1399 0.1356 0.1840 -0.0155 0.0157  -0.0159 61  MET   A CE  
1316 N N   . GLN   A 62  ? 0.1048 0.1075 0.1246 -0.0035 -0.0048 -0.0065 62  GLN   A N   
1317 C CA  . GLN   A 62  ? 0.1111 0.1041 0.1304 -0.0034 0.0037  -0.0032 62  GLN   A CA  
1318 C C   . GLN   A 62  ? 0.1101 0.0989 0.1446 -0.0022 0.0055  -0.0002 62  GLN   A C   
1319 O O   . GLN   A 62  ? 0.1124 0.1199 0.1439 -0.0030 0.0060  -0.0030 62  GLN   A O   
1320 C CB  . GLN   A 62  ? 0.1125 0.1033 0.1404 -0.0035 -0.0034 -0.0048 62  GLN   A CB  
1321 C CG  . GLN   A 62  ? 0.1118 0.1031 0.1415 -0.0041 -0.0050 0.0090  62  GLN   A CG  
1322 C CD  . GLN   A 62  ? 0.1207 0.1055 0.1345 -0.0044 0.0067  0.0109  62  GLN   A CD  
1323 O OE1 . GLN   A 62  ? 0.1257 0.1203 0.1401 -0.0049 0.0019  -0.0011 62  GLN   A OE1 
1324 N NE2 . GLN   A 62  ? 0.1300 0.1108 0.1417 0.0009  0.0001  -0.0076 62  GLN   A NE2 
1333 N N   . VAL   A 63  ? 0.1069 0.1086 0.1515 -0.0059 0.0040  -0.0161 63  VAL   A N   
1334 C CA  . VAL   A 63  ? 0.1125 0.1198 0.1773 -0.0148 -0.0015 -0.0228 63  VAL   A CA  
1335 C C   . VAL   A 63  ? 0.1038 0.1185 0.1625 -0.0119 -0.0107 -0.0197 63  VAL   A C   
1336 O O   . VAL   A 63  ? 0.1055 0.1221 0.1758 -0.0132 0.0006  -0.0182 63  VAL   A O   
1337 C CB  . VAL   A 63  ? 0.1196 0.1372 0.2015 -0.0135 -0.0021 -0.0440 63  VAL   A CB  
1338 C CG1 . VAL   A 63  ? 0.1372 0.1557 0.2351 -0.0164 -0.0060 -0.0667 63  VAL   A CG1 
1339 C CG2 . VAL   A 63  ? 0.1355 0.1222 0.2218 -0.0141 0.0112  -0.0406 63  VAL   A CG2 
1349 N N   . GLU   A 64  ? 0.1067 0.1250 0.1474 -0.0016 -0.0025 -0.0170 64  GLU   A N   
1350 C CA  . GLU   A 64  ? 0.1050 0.1248 0.1491 -0.0053 -0.0056 -0.0048 64  GLU   A CA  
1351 C C   . GLU   A 64  ? 0.1036 0.1194 0.1438 -0.0058 0.0006  -0.0032 64  GLU   A C   
1352 O O   . GLU   A 64  ? 0.1095 0.1253 0.1475 0.0024  0.0004  -0.0048 64  GLU   A O   
1353 C CB  . GLU   A 64  ? 0.1176 0.1343 0.1534 -0.0039 0.0000  -0.0105 64  GLU   A CB  
1354 C CG  . GLU   A 64  ? 0.1267 0.1355 0.1635 -0.0085 0.0087  -0.0094 64  GLU   A CG  
1355 C CD  . GLU   A 64  ? 0.1401 0.1432 0.1636 -0.0149 0.0089  -0.0149 64  GLU   A CD  
1356 O OE1 . GLU   A 64  ? 0.1356 0.1548 0.1845 -0.0233 0.0169  -0.0135 64  GLU   A OE1 
1357 O OE2 . GLU   A 64  ? 0.1604 0.1453 0.1662 -0.0254 0.0010  -0.0045 64  GLU   A OE2 
1364 N N   . SER   A 65  ? 0.1038 0.1170 0.1346 0.0014  0.0036  -0.0065 65  SER   A N   
1365 C CA  . SER   A 65  ? 0.1085 0.1107 0.1354 -0.0028 -0.0013 -0.0054 65  SER   A CA  
1366 C C   . SER   A 65  ? 0.1096 0.1181 0.1396 -0.0043 -0.0002 -0.0036 65  SER   A C   
1367 O O   . SER   A 65  ? 0.1171 0.1204 0.1522 0.0012  0.0095  -0.0096 65  SER   A O   
1368 C CB  . SER   A 65  ? 0.1077 0.1112 0.1333 -0.0076 0.0064  -0.0004 65  SER   A CB  
1369 O OG  . SER   A 65  ? 0.1040 0.1201 0.1508 -0.0060 -0.0082 0.0042  65  SER   A OG  
1375 N N   . ASP   A 66  ? 0.1078 0.1154 0.1466 -0.0051 0.0117  0.0012  66  ASP   A N   
1376 C CA  . ASP   A 66  ? 0.1204 0.1258 0.1596 -0.0029 0.0068  0.0105  66  ASP   A CA  
1377 C C   . ASP   A 66  ? 0.1205 0.1235 0.1680 -0.0035 0.0171  0.0141  66  ASP   A C   
1378 O O   . ASP   A 66  ? 0.1275 0.1343 0.1751 -0.0020 0.0260  0.0191  66  ASP   A O   
1379 C CB  . ASP   A 66  ? 0.1287 0.1331 0.1833 0.0051  0.0111  0.0213  66  ASP   A CB  
1380 C CG  . ASP   A 66  ? 0.1512 0.1467 0.2148 0.0079  0.0035  0.0333  66  ASP   A CG  
1381 O OD1 . ASP   A 66  ? 0.1494 0.1742 0.1884 -0.0046 -0.0023 0.0385  66  ASP   A OD1 
1382 O OD2 . ASP   A 66  ? 0.1709 0.1557 0.3016 0.0283  -0.0182 0.0153  66  ASP   A OD2 
1387 N N   . ASP   A 67  ? 0.1086 0.1232 0.1836 -0.0016 0.0120  0.0120  67  ASP   A N   
1388 C CA  . ASP   A 67  ? 0.1149 0.1372 0.1931 -0.0022 0.0024  0.0214  67  ASP   A CA  
1389 C C   . ASP   A 67  ? 0.1167 0.1373 0.1817 0.0000  0.0126  0.0185  67  ASP   A C   
1390 O O   . ASP   A 67  ? 0.1135 0.1445 0.2050 0.0032  0.0322  0.0316  67  ASP   A O   
1391 C CB  . ASP   A 67  ? 0.1230 0.1504 0.2296 -0.0061 -0.0190 0.0229  67  ASP   A CB  
1392 C CG  . ASP   A 67  ? 0.1241 0.1639 0.2622 -0.0059 -0.0329 0.0278  67  ASP   A CG  
1393 O OD1 . ASP   A 67  ? 0.1263 0.1765 0.3440 -0.0123 -0.0381 0.0396  67  ASP   A OD1 
1394 O OD2 . ASP   A 67  ? 0.1240 0.1696 0.2422 0.0033  -0.0225 0.0207  67  ASP   A OD2 
1399 N N   A TYR   A 68  ? 0.1143 0.1229 0.1650 0.0023  0.0190  0.0196  68  TYR   A N   
1400 N N   B TYR   A 68  ? 0.1206 0.1332 0.1689 0.0015  0.0127  0.0185  68  TYR   A N   
1401 C CA  A TYR   A 68  ? 0.1246 0.1235 0.1735 0.0009  0.0293  0.0176  68  TYR   A CA  
1402 C CA  B TYR   A 68  ? 0.1269 0.1317 0.1628 0.0029  0.0128  0.0176  68  TYR   A CA  
1403 C C   A TYR   A 68  ? 0.1175 0.1203 0.1655 0.0011  0.0280  0.0177  68  TYR   A C   
1404 C C   B TYR   A 68  ? 0.1202 0.1234 0.1601 0.0023  0.0190  0.0152  68  TYR   A C   
1405 O O   A TYR   A 68  ? 0.1233 0.1245 0.1698 0.0081  0.0330  0.0196  68  TYR   A O   
1406 O O   B TYR   A 68  ? 0.1209 0.1246 0.1576 0.0048  0.0208  0.0143  68  TYR   A O   
1407 C CB  A TYR   A 68  ? 0.1297 0.1221 0.1957 0.0128  0.0513  0.0180  68  TYR   A CB  
1408 C CB  B TYR   A 68  ? 0.1380 0.1380 0.1637 0.0073  0.0069  0.0206  68  TYR   A CB  
1409 C CG  A TYR   A 68  ? 0.1306 0.1398 0.2318 0.0079  0.0706  0.0260  68  TYR   A CG  
1410 C CG  B TYR   A 68  ? 0.1478 0.1463 0.1652 0.0099  -0.0004 0.0244  68  TYR   A CG  
1411 C CD1 A TYR   A 68  ? 0.1411 0.1525 0.2618 -0.0221 0.0579  -0.0091 68  TYR   A CD1 
1412 C CD1 B TYR   A 68  ? 0.1527 0.1512 0.1616 0.0076  -0.0052 0.0224  68  TYR   A CD1 
1413 C CD2 A TYR   A 68  ? 0.1560 0.1401 0.2651 0.0136  0.0711  0.0331  68  TYR   A CD2 
1414 C CD2 B TYR   A 68  ? 0.1561 0.1481 0.1689 0.0132  -0.0081 0.0278  68  TYR   A CD2 
1415 C CE1 A TYR   A 68  ? 0.1442 0.1588 0.2955 -0.0238 0.0588  -0.0234 68  TYR   A CE1 
1416 C CE1 B TYR   A 68  ? 0.1568 0.1527 0.1606 0.0108  -0.0119 0.0277  68  TYR   A CE1 
1417 C CE2 A TYR   A 68  ? 0.1523 0.1444 0.2902 0.0057  0.0780  0.0122  68  TYR   A CE2 
1418 C CE2 B TYR   A 68  ? 0.1585 0.1507 0.1623 0.0161  -0.0136 0.0304  68  TYR   A CE2 
1419 C CZ  A TYR   A 68  ? 0.1532 0.1518 0.3140 -0.0185 0.0633  -0.0209 68  TYR   A CZ  
1420 C CZ  B TYR   A 68  ? 0.1618 0.1528 0.1594 0.0150  -0.0172 0.0333  68  TYR   A CZ  
1421 O OH  A TYR   A 68  ? 0.1759 0.1503 0.3459 -0.0155 0.0353  -0.0495 68  TYR   A OH  
1422 O OH  B TYR   A 68  ? 0.1719 0.1522 0.1600 0.0201  -0.0289 0.0401  68  TYR   A OH  
1441 N N   . ILE   A 69  ? 0.1148 0.1144 0.1663 0.0017  0.0241  0.0143  69  ILE   A N   
1442 C CA  . ILE   A 69  ? 0.1220 0.1203 0.1577 0.0024  0.0182  0.0051  69  ILE   A CA  
1443 C C   . ILE   A 69  ? 0.1222 0.1218 0.1479 0.0044  0.0197  0.0172  69  ILE   A C   
1444 O O   . ILE   A 69  ? 0.1334 0.1318 0.1430 -0.0012 0.0243  0.0178  69  ILE   A O   
1445 C CB  . ILE   A 69  ? 0.1303 0.1435 0.1619 0.0040  0.0180  -0.0052 69  ILE   A CB  
1446 C CG1 . ILE   A 69  ? 0.1302 0.1576 0.1696 0.0059  0.0222  -0.0181 69  ILE   A CG1 
1447 C CG2 . ILE   A 69  ? 0.1496 0.1658 0.1789 0.0135  0.0014  -0.0139 69  ILE   A CG2 
1448 C CD1 . ILE   A 69  ? 0.1282 0.1682 0.1813 -0.0023 0.0193  -0.0160 69  ILE   A CD1 
1461 N N   . ALA   A 70  ? 0.1271 0.1219 0.1528 -0.0061 0.0220  0.0093  70  ALA   A N   
1462 C CA  . ALA   A 70  ? 0.1328 0.1297 0.1721 -0.0141 0.0237  0.0212  70  ALA   A CA  
1463 C C   . ALA   A 70  ? 0.1278 0.1478 0.1618 -0.0108 0.0274  0.0187  70  ALA   A C   
1464 O O   . ALA   A 70  ? 0.1446 0.1825 0.1854 0.0032  0.0444  0.0299  70  ALA   A O   
1465 C CB  . ALA   A 70  ? 0.1338 0.1253 0.1970 -0.0231 0.0181  0.0115  70  ALA   A CB  
1471 N N   . THR   A 71  ? 0.1234 0.1472 0.1573 -0.0047 0.0173  0.0218  71  THR   A N   
1472 C CA  . THR   A 71  ? 0.1344 0.1606 0.1876 0.0052  0.0221  0.0229  71  THR   A CA  
1473 C C   . THR   A 71  ? 0.1248 0.1570 0.1959 0.0096  0.0340  0.0231  71  THR   A C   
1474 O O   . THR   A 71  ? 0.1304 0.1786 0.2433 0.0102  0.0423  -0.0003 71  THR   A O   
1475 C CB  . THR   A 71  ? 0.1550 0.1795 0.2091 0.0148  -0.0074 0.0232  71  THR   A CB  
1476 O OG1 . THR   A 71  ? 0.1753 0.2000 0.2123 0.0102  -0.0246 0.0163  71  THR   A OG1 
1477 C CG2 . THR   A 71  ? 0.1659 0.1919 0.2351 0.0217  -0.0129 0.0283  71  THR   A CG2 
1485 N N   . ASN   A 72  ? 0.1305 0.1414 0.1740 0.0099  0.0286  0.0170  72  ASN   A N   
1486 C CA  . ASN   A 72  ? 0.1386 0.1398 0.1871 0.0170  0.0369  0.0208  72  ASN   A CA  
1487 C C   . ASN   A 72  ? 0.1447 0.1399 0.1846 0.0148  0.0483  0.0091  72  ASN   A C   
1488 O O   . ASN   A 72  ? 0.1595 0.1401 0.2157 0.0180  0.0472  -0.0022 72  ASN   A O   
1489 C CB  . ASN   A 72  ? 0.1467 0.1455 0.1885 0.0129  0.0375  0.0169  72  ASN   A CB  
1490 C CG  . ASN   A 72  ? 0.1671 0.1558 0.1863 0.0261  0.0329  0.0219  72  ASN   A CG  
1491 O OD1 . ASN   A 72  ? 0.1894 0.1845 0.1982 0.0216  0.0392  0.0209  72  ASN   A OD1 
1492 N ND2 . ASN   A 72  ? 0.1839 0.1646 0.2007 0.0458  0.0137  0.0108  72  ASN   A ND2 
1499 N N   . GLY   A 73  ? 0.1499 0.1378 0.1639 0.0083  0.0430  0.0119  73  GLY   A N   
1500 C CA  . GLY   A 73  ? 0.1520 0.1364 0.1583 -0.0039 0.0380  0.0070  73  GLY   A CA  
1501 C C   . GLY   A 73  ? 0.1519 0.1314 0.1402 0.0014  0.0538  0.0139  73  GLY   A C   
1502 O O   . GLY   A 73  ? 0.1491 0.1397 0.1554 0.0080  0.0396  0.0244  73  GLY   A O   
1506 N N   . PRO   A 74  ? 0.1595 0.1282 0.1445 -0.0102 0.0477  0.0120  74  PRO   A N   
1507 C CA  . PRO   A 74  ? 0.1547 0.1266 0.1532 -0.0038 0.0418  0.0168  74  PRO   A CA  
1508 C C   . PRO   A 74  ? 0.1433 0.1176 0.1502 0.0005  0.0274  0.0028  74  PRO   A C   
1509 O O   . PRO   A 74  ? 0.1540 0.1191 0.1745 0.0023  0.0337  -0.0036 74  PRO   A O   
1510 C CB  . PRO   A 74  ? 0.1689 0.1512 0.1782 -0.0004 0.0439  0.0292  74  PRO   A CB  
1511 C CG  . PRO   A 74  ? 0.1922 0.1813 0.2117 -0.0159 0.0359  0.0170  74  PRO   A CG  
1512 C CD  . PRO   A 74  ? 0.1787 0.1596 0.1600 -0.0202 0.0348  0.0070  74  PRO   A CD  
1520 N N   . LEU   A 75  ? 0.1370 0.1094 0.1399 0.0004  0.0242  0.0091  75  LEU   A N   
1521 C CA  . LEU   A 75  ? 0.1473 0.1053 0.1309 -0.0003 0.0131  0.0019  75  LEU   A CA  
1522 C C   . LEU   A 75  ? 0.1585 0.1164 0.1241 0.0013  0.0159  0.0076  75  LEU   A C   
1523 O O   . LEU   A 75  ? 0.1965 0.1377 0.1309 0.0056  0.0092  0.0052  75  LEU   A O   
1524 C CB  . LEU   A 75  ? 0.1532 0.1171 0.1134 -0.0111 0.0065  0.0093  75  LEU   A CB  
1525 C CG  . LEU   A 75  ? 0.1702 0.1442 0.1342 -0.0408 0.0048  0.0107  75  LEU   A CG  
1526 C CD1 . LEU   A 75  ? 0.1826 0.1908 0.1425 -0.0382 0.0029  -0.0039 75  LEU   A CD1 
1527 C CD2 . LEU   A 75  ? 0.1959 0.1924 0.1839 -0.0191 0.0145  0.0149  75  LEU   A CD2 
1539 N N   . LYS   A 76  ? 0.1600 0.1235 0.1382 -0.0086 0.0133  -0.0046 76  LYS   A N   
1540 C CA  . LYS   A 76  ? 0.1565 0.1445 0.1429 -0.0079 0.0147  -0.0140 76  LYS   A CA  
1541 C C   . LYS   A 76  ? 0.1520 0.1233 0.1189 -0.0040 0.0170  -0.0000 76  LYS   A C   
1542 O O   . LYS   A 76  ? 0.1520 0.1210 0.1166 -0.0026 0.0180  0.0040  76  LYS   A O   
1543 C CB  . LYS   A 76  ? 0.1552 0.1684 0.1842 0.0054  0.0159  -0.0394 76  LYS   A CB  
1544 C CG  . LYS   A 76  ? 0.1648 0.1610 0.2470 0.0079  0.0156  -0.0402 76  LYS   A CG  
1545 C CD  . LYS   A 76  ? 0.1684 0.1605 0.3014 0.0111  0.0010  -0.0481 76  LYS   A CD  
1546 C CE  . LYS   A 76  ? 0.1789 0.1851 0.3600 0.0052  0.0090  -0.0589 76  LYS   A CE  
1547 N NZ  . LYS   A 76  ? 0.1779 0.1875 0.4024 -0.0074 0.0043  -0.0688 76  LYS   A NZ  
1561 N N   . VAL   A 77  ? 0.1587 0.1242 0.1175 -0.0006 0.0237  0.0089  77  VAL   A N   
1562 C CA  . VAL   A 77  ? 0.1551 0.1272 0.1182 0.0087  0.0231  0.0124  77  VAL   A CA  
1563 C C   . VAL   A 77  ? 0.1403 0.1298 0.0950 0.0094  0.0148  0.0020  77  VAL   A C   
1564 O O   . VAL   A 77  ? 0.1512 0.1330 0.1046 0.0168  0.0252  -0.0062 77  VAL   A O   
1565 C CB  . VAL   A 77  ? 0.1734 0.1474 0.1262 0.0111  0.0132  0.0165  77  VAL   A CB  
1566 C CG1 . VAL   A 77  ? 0.1636 0.1603 0.1453 0.0167  0.0028  0.0036  77  VAL   A CG1 
1567 C CG2 . VAL   A 77  ? 0.2002 0.1592 0.1527 0.0047  -0.0014 0.0244  77  VAL   A CG2 
1577 N N   . GLY   A 78  ? 0.1446 0.1264 0.1002 0.0088  0.0165  0.0036  78  GLY   A N   
1578 C CA  . GLY   A 78  ? 0.1384 0.1214 0.1211 0.0040  0.0202  0.0096  78  GLY   A CA  
1579 C C   . GLY   A 78  ? 0.1306 0.1145 0.1120 0.0031  0.0232  0.0044  78  GLY   A C   
1580 O O   . GLY   A 78  ? 0.1328 0.1267 0.1250 0.0044  0.0207  0.0198  78  GLY   A O   
1584 N N   . GLY   A 79  ? 0.1303 0.1181 0.1143 0.0037  0.0185  0.0080  79  GLY   A N   
1585 C CA  . GLY   A 79  ? 0.1250 0.1189 0.1314 0.0020  0.0176  0.0051  79  GLY   A CA  
1586 C C   . GLY   A 79  ? 0.1206 0.1114 0.1194 0.0030  0.0131  -0.0010 79  GLY   A C   
1587 O O   . GLY   A 79  ? 0.1249 0.1204 0.1237 0.0209  0.0141  0.0023  79  GLY   A O   
1591 N N   . SER   A 80  ? 0.1144 0.1272 0.1378 0.0022  0.0183  -0.0094 80  SER   A N   
1592 C CA  . SER   A 80  ? 0.1139 0.1198 0.1271 -0.0009 0.0081  -0.0028 80  SER   A CA  
1593 C C   . SER   A 80  ? 0.1135 0.1185 0.1306 0.0007  0.0036  0.0060  80  SER   A C   
1594 O O   . SER   A 80  ? 0.1084 0.1395 0.1639 0.0099  0.0096  -0.0102 80  SER   A O   
1595 C CB  . SER   A 80  ? 0.1263 0.1197 0.1477 -0.0055 0.0037  -0.0020 80  SER   A CB  
1596 O OG  . SER   A 80  ? 0.1530 0.1229 0.1892 0.0049  -0.0064 0.0106  80  SER   A OG  
1602 N N   . CYS   A 81  ? 0.1054 0.1125 0.1296 0.0019  -0.0010 0.0026  81  CYS   A N   
1603 C CA  . CYS   A 81  ? 0.1036 0.1190 0.1295 -0.0032 -0.0056 0.0105  81  CYS   A CA  
1604 C C   . CYS   A 81  ? 0.1026 0.1122 0.1289 -0.0043 0.0000  0.0167  81  CYS   A C   
1605 O O   . CYS   A 81  ? 0.1063 0.1424 0.1357 0.0011  -0.0006 0.0227  81  CYS   A O   
1606 C CB  . CYS   A 81  ? 0.1171 0.1289 0.1378 -0.0093 0.0029  0.0118  81  CYS   A CB  
1607 S SG  . CYS   A 81  ? 0.1308 0.1194 0.1429 -0.0134 0.0033  0.0069  81  CYS   A SG  
1613 N N   . VAL   A 82  ? 0.1072 0.1245 0.1276 0.0011  -0.0105 0.0070  82  VAL   A N   
1614 C CA  . VAL   A 82  ? 0.1182 0.1285 0.1245 0.0040  -0.0089 0.0179  82  VAL   A CA  
1615 C C   . VAL   A 82  ? 0.1147 0.1331 0.1290 0.0033  -0.0063 0.0164  82  VAL   A C   
1616 O O   . VAL   A 82  ? 0.1128 0.1464 0.1578 0.0026  -0.0057 -0.0070 82  VAL   A O   
1617 C CB  . VAL   A 82  ? 0.1521 0.1399 0.1394 0.0053  -0.0038 0.0162  82  VAL   A CB  
1618 C CG1 . VAL   A 82  ? 0.1737 0.1589 0.1552 0.0118  0.0067  0.0161  82  VAL   A CG1 
1619 C CG2 . VAL   A 82  ? 0.1563 0.1435 0.1690 0.0013  -0.0105 0.0228  82  VAL   A CG2 
1629 N N   . LEU   A 83  ? 0.1117 0.1274 0.1211 -0.0073 -0.0053 0.0059  83  LEU   A N   
1630 C CA  . LEU   A 83  ? 0.1130 0.1328 0.1241 -0.0075 -0.0066 0.0044  83  LEU   A CA  
1631 C C   . LEU   A 83  ? 0.1201 0.1320 0.1163 -0.0077 -0.0158 0.0060  83  LEU   A C   
1632 O O   . LEU   A 83  ? 0.1304 0.1324 0.1233 -0.0111 -0.0045 0.0057  83  LEU   A O   
1633 C CB  . LEU   A 83  ? 0.1270 0.1372 0.1248 -0.0086 -0.0079 0.0073  83  LEU   A CB  
1634 C CG  . LEU   A 83  ? 0.1433 0.1488 0.1253 -0.0106 0.0057  0.0017  83  LEU   A CG  
1635 C CD1 . LEU   A 83  ? 0.1563 0.1498 0.1321 -0.0219 0.0042  0.0170  83  LEU   A CD1 
1636 C CD2 . LEU   A 83  ? 0.1412 0.1659 0.1459 -0.0113 0.0147  0.0081  83  LEU   A CD2 
1648 N N   . SER   A 84  ? 0.1332 0.1358 0.1174 -0.0113 -0.0090 0.0085  84  SER   A N   
1649 C CA  . SER   A 84  ? 0.1396 0.1427 0.1184 -0.0060 -0.0093 -0.0004 84  SER   A CA  
1650 C C   . SER   A 84  ? 0.1475 0.1333 0.1117 -0.0144 -0.0013 0.0016  84  SER   A C   
1651 O O   . SER   A 84  ? 0.1408 0.1535 0.1152 -0.0139 -0.0062 -0.0032 84  SER   A O   
1652 C CB  . SER   A 84  ? 0.1451 0.1690 0.1211 -0.0083 -0.0043 -0.0082 84  SER   A CB  
1653 O OG  . SER   A 84  ? 0.1553 0.1878 0.1309 -0.0043 -0.0190 -0.0202 84  SER   A OG  
1659 N N   . GLY   A 85  ? 0.1616 0.1417 0.1134 -0.0169 0.0110  -0.0064 85  GLY   A N   
1660 C CA  . GLY   A 85  ? 0.1679 0.1550 0.1230 -0.0221 0.0143  -0.0115 85  GLY   A CA  
1661 C C   . GLY   A 85  ? 0.1569 0.1625 0.0975 -0.0155 0.0078  -0.0067 85  GLY   A C   
1662 O O   . GLY   A 85  ? 0.1537 0.1740 0.1119 -0.0206 0.0121  -0.0119 85  GLY   A O   
1666 N N   . HIS   A 86  ? 0.1584 0.1466 0.0947 -0.0128 0.0007  -0.0030 86  HIS   A N   
1667 C CA  . HIS   A 86  ? 0.1717 0.1579 0.0963 -0.0179 -0.0009 -0.0073 86  HIS   A CA  
1668 C C   . HIS   A 86  ? 0.1891 0.1690 0.1056 -0.0138 -0.0053 -0.0074 86  HIS   A C   
1669 O O   . HIS   A 86  ? 0.1972 0.1886 0.1094 -0.0077 0.0057  -0.0023 86  HIS   A O   
1670 C CB  . HIS   A 86  ? 0.1682 0.1503 0.1117 -0.0099 0.0095  -0.0074 86  HIS   A CB  
1671 C CG  . HIS   A 86  ? 0.1683 0.1487 0.1215 -0.0016 0.0078  0.0003  86  HIS   A CG  
1672 N ND1 . HIS   A 86  ? 0.1721 0.1557 0.1571 -0.0131 0.0094  0.0049  86  HIS   A ND1 
1673 C CD2 . HIS   A 86  ? 0.1686 0.1451 0.1240 0.0033  0.0079  0.0092  86  HIS   A CD2 
1674 C CE1 . HIS   A 86  ? 0.1707 0.1533 0.1526 -0.0086 0.0236  0.0113  86  HIS   A CE1 
1675 N NE2 . HIS   A 86  ? 0.1689 0.1441 0.1371 0.0078  0.0225  0.0226  86  HIS   A NE2 
1683 N N   . ASN   A 87  ? 0.1947 0.1740 0.1144 -0.0105 0.0129  -0.0134 87  ASN   A N   
1684 C CA  . ASN   A 87  ? 0.2137 0.1874 0.1265 -0.0049 0.0403  -0.0131 87  ASN   A CA  
1685 C C   . ASN   A 87  ? 0.2138 0.2006 0.1504 -0.0077 0.0581  0.0026  87  ASN   A C   
1686 O O   . ASN   A 87  ? 0.2397 0.2232 0.2031 -0.0155 0.0839  -0.0002 87  ASN   A O   
1687 C CB  . ASN   A 87  ? 0.2295 0.1962 0.1305 0.0067  0.0416  -0.0163 87  ASN   A CB  
1688 C CG  . ASN   A 87  ? 0.2400 0.2064 0.1375 0.0180  0.0473  -0.0080 87  ASN   A CG  
1689 O OD1 . ASN   A 87  ? 0.2564 0.2063 0.1572 0.0355  0.0456  0.0043  87  ASN   A OD1 
1690 N ND2 . ASN   A 87  ? 0.2427 0.2306 0.1540 0.0203  0.0487  -0.0042 87  ASN   A ND2 
1697 N N   . LEU   A 88  ? 0.1885 0.1983 0.1497 -0.0173 0.0334  0.0130  88  LEU   A N   
1698 C CA  . LEU   A 88  ? 0.1800 0.1970 0.1666 -0.0285 0.0242  0.0299  88  LEU   A CA  
1699 C C   . LEU   A 88  ? 0.1796 0.1961 0.1524 -0.0268 0.0217  0.0291  88  LEU   A C   
1700 O O   . LEU   A 88  ? 0.1847 0.2076 0.1913 -0.0315 0.0218  0.0516  88  LEU   A O   
1701 C CB  . LEU   A 88  ? 0.1835 0.2074 0.1856 -0.0428 -0.0093 0.0419  88  LEU   A CB  
1702 C CG  . LEU   A 88  ? 0.2037 0.2230 0.2215 -0.0434 -0.0244 0.0425  88  LEU   A CG  
1703 C CD1 . LEU   A 88  ? 0.2203 0.2294 0.2134 -0.0417 -0.0271 0.0281  88  LEU   A CD1 
1704 C CD2 . LEU   A 88  ? 0.2176 0.2353 0.2630 -0.0360 -0.0218 0.0363  88  LEU   A CD2 
1716 N N   . ALA   A 89  ? 0.1774 0.1764 0.1179 -0.0257 0.0196  0.0073  89  ALA   A N   
1717 C CA  . ALA   A 89  ? 0.1871 0.1769 0.1043 -0.0240 0.0065  0.0075  89  ALA   A CA  
1718 C C   . ALA   A 89  ? 0.1921 0.1815 0.1101 -0.0183 -0.0102 0.0015  89  ALA   A C   
1719 O O   . ALA   A 89  ? 0.1890 0.1838 0.1468 -0.0211 -0.0188 -0.0187 89  ALA   A O   
1720 C CB  . ALA   A 89  ? 0.1811 0.1836 0.1067 -0.0254 0.0010  0.0110  89  ALA   A CB  
1726 N N   . LYS   A 90  ? 0.2029 0.1956 0.1147 -0.0215 -0.0286 0.0094  90  LYS   A N   
1727 C CA  . LYS   A 90  ? 0.2097 0.2051 0.1210 -0.0209 -0.0397 0.0069  90  LYS   A CA  
1728 C C   . LYS   A 90  ? 0.1811 0.1870 0.1235 -0.0198 -0.0291 0.0017  90  LYS   A C   
1729 O O   . LYS   A 90  ? 0.1857 0.2074 0.1435 -0.0239 -0.0298 -0.0093 90  LYS   A O   
1730 C CB  . LYS   A 90  ? 0.2418 0.2376 0.1483 -0.0118 -0.0500 0.0219  90  LYS   A CB  
1731 C CG  . LYS   A 90  ? 0.2658 0.2669 0.2429 -0.0085 -0.0501 0.0304  90  LYS   A CG  
1732 C CD  . LYS   A 90  ? 0.2939 0.2927 0.3389 -0.0069 -0.0373 0.0359  90  LYS   A CD  
1733 C CE  . LYS   A 90  ? 0.3152 0.3140 0.4074 -0.0067 -0.0259 0.0354  90  LYS   A CE  
1734 N NZ  . LYS   A 90  ? 0.3275 0.3263 0.4545 -0.0069 -0.0175 0.0291  90  LYS   A NZ  
1748 N N   . HIS   A 91  ? 0.1654 0.1637 0.1015 -0.0157 -0.0269 0.0083  91  HIS   A N   
1749 C CA  . HIS   A 91  ? 0.1512 0.1490 0.1133 -0.0119 -0.0249 0.0080  91  HIS   A CA  
1750 C C   . HIS   A 91  ? 0.1393 0.1378 0.1004 -0.0165 -0.0104 0.0073  91  HIS   A C   
1751 O O   . HIS   A 91  ? 0.1424 0.1497 0.0988 -0.0173 -0.0053 0.0093  91  HIS   A O   
1752 C CB  . HIS   A 91  ? 0.1650 0.1743 0.1487 0.0096  -0.0405 0.0013  91  HIS   A CB  
1753 C CG  . HIS   A 91  ? 0.2066 0.2246 0.2294 0.0184  -0.0708 -0.0005 91  HIS   A CG  
1754 N ND1 . HIS   A 91  ? 0.2168 0.2540 0.2744 0.0198  -0.0771 -0.0169 91  HIS   A ND1 
1755 C CD2 . HIS   A 91  ? 0.2309 0.2435 0.2600 0.0279  -0.0786 0.0114  91  HIS   A CD2 
1756 C CE1 . HIS   A 91  ? 0.2263 0.2613 0.2920 0.0262  -0.0787 -0.0083 91  HIS   A CE1 
1757 N NE2 . HIS   A 91  ? 0.2408 0.2578 0.2896 0.0322  -0.0782 0.0018  91  HIS   A NE2 
1765 N N   . CYS   A 92  ? 0.1269 0.1303 0.1088 -0.0158 -0.0057 0.0066  92  CYS   A N   
1766 C CA  . CYS   A 92  ? 0.1180 0.1278 0.1050 -0.0121 -0.0013 0.0008  92  CYS   A CA  
1767 C C   . CYS   A 92  ? 0.1133 0.1275 0.0995 -0.0103 0.0008  0.0074  92  CYS   A C   
1768 O O   . CYS   A 92  ? 0.1150 0.1341 0.1159 -0.0154 -0.0002 0.0013  92  CYS   A O   
1769 C CB  . CYS   A 92  ? 0.1265 0.1327 0.1230 -0.0041 -0.0075 0.0061  92  CYS   A CB  
1770 S SG  . CYS   A 92  ? 0.1259 0.1225 0.1146 -0.0076 -0.0025 0.0054  92  CYS   A SG  
1776 N N   . LEU   A 93  ? 0.1119 0.1152 0.1050 -0.0095 0.0069  0.0128  93  LEU   A N   
1777 C CA  . LEU   A 93  ? 0.1091 0.1144 0.0977 -0.0038 0.0064  0.0049  93  LEU   A CA  
1778 C C   . LEU   A 93  ? 0.1017 0.1011 0.0988 -0.0010 0.0047  0.0019  93  LEU   A C   
1779 O O   . LEU   A 93  ? 0.1012 0.1156 0.0958 -0.0022 0.0010  0.0061  93  LEU   A O   
1780 C CB  . LEU   A 93  ? 0.1150 0.1107 0.1109 -0.0016 -0.0009 0.0170  93  LEU   A CB  
1781 C CG  . LEU   A 93  ? 0.1208 0.1121 0.1150 0.0005  0.0006  0.0173  93  LEU   A CG  
1782 C CD1 . LEU   A 93  ? 0.1272 0.1205 0.1450 0.0025  0.0169  0.0056  93  LEU   A CD1 
1783 C CD2 . LEU   A 93  ? 0.1336 0.1175 0.1287 -0.0048 0.0032  0.0054  93  LEU   A CD2 
1795 N N   . HIS   A 94  ? 0.1002 0.1046 0.1004 -0.0028 0.0038  0.0051  94  HIS   A N   
1796 C CA  . HIS   A 94  ? 0.1013 0.1071 0.1026 -0.0029 0.0024  0.0105  94  HIS   A CA  
1797 C C   . HIS   A 94  ? 0.0999 0.1014 0.1006 -0.0040 0.0009  0.0070  94  HIS   A C   
1798 O O   . HIS   A 94  ? 0.1030 0.1260 0.1304 0.0024  0.0021  -0.0122 94  HIS   A O   
1799 C CB  . HIS   A 94  ? 0.1047 0.1010 0.1102 -0.0005 0.0010  0.0095  94  HIS   A CB  
1800 C CG  . HIS   A 94  ? 0.1049 0.1063 0.1063 -0.0043 -0.0015 0.0092  94  HIS   A CG  
1801 N ND1 . HIS   A 94  ? 0.1048 0.1049 0.1150 -0.0028 -0.0012 0.0094  94  HIS   A ND1 
1802 C CD2 . HIS   A 94  ? 0.1123 0.1171 0.1083 -0.0004 -0.0093 0.0019  94  HIS   A CD2 
1803 C CE1 . HIS   A 94  ? 0.1127 0.1048 0.1157 -0.0049 -0.0091 0.0009  94  HIS   A CE1 
1804 N NE2 . HIS   A 94  ? 0.1205 0.1108 0.1218 -0.0055 -0.0075 0.0023  94  HIS   A NE2 
1812 N N   . VAL   A 95  ? 0.0987 0.0980 0.0917 -0.0048 0.0076  0.0018  95  VAL   A N   
1813 C CA  . VAL   A 95  ? 0.1053 0.1006 0.0993 -0.0047 0.0080  0.0084  95  VAL   A CA  
1814 C C   . VAL   A 95  ? 0.1031 0.1025 0.0870 -0.0081 0.0013  0.0017  95  VAL   A C   
1815 O O   . VAL   A 95  ? 0.1157 0.1146 0.0925 0.0074  0.0038  0.0024  95  VAL   A O   
1816 C CB  . VAL   A 95  ? 0.1098 0.1075 0.1098 -0.0069 -0.0024 0.0012  95  VAL   A CB  
1817 C CG1 . VAL   A 95  ? 0.1287 0.1108 0.1232 -0.0105 0.0041  -0.0061 95  VAL   A CG1 
1818 C CG2 . VAL   A 95  ? 0.1140 0.1087 0.1231 -0.0116 0.0053  0.0113  95  VAL   A CG2 
1828 N N   A VAL   A 96  ? 0.1099 0.1050 0.0903 -0.0013 0.0060  0.0065  96  VAL   A N   
1829 N N   B VAL   A 96  ? 0.1116 0.1106 0.0946 -0.0046 0.0044  0.0024  96  VAL   A N   
1830 C CA  A VAL   A 96  ? 0.1171 0.1026 0.0969 0.0002  0.0101  0.0122  96  VAL   A CA  
1831 C CA  B VAL   A 96  ? 0.1216 0.1183 0.1057 -0.0028 0.0036  0.0014  96  VAL   A CA  
1832 C C   A VAL   A 96  ? 0.1192 0.1090 0.0873 0.0028  0.0157  0.0112  96  VAL   A C   
1833 C C   B VAL   A 96  ? 0.1233 0.1244 0.1092 0.0009  0.0054  0.0034  96  VAL   A C   
1834 O O   A VAL   A 96  ? 0.1224 0.1196 0.1141 -0.0017 0.0124  -0.0073 96  VAL   A O   
1835 O O   B VAL   A 96  ? 0.1268 0.1265 0.1169 0.0030  0.0089  0.0029  96  VAL   A O   
1836 C CB  A VAL   A 96  ? 0.1175 0.1105 0.1018 -0.0042 0.0220  0.0065  96  VAL   A CB  
1837 C CB  B VAL   A 96  ? 0.1297 0.1222 0.1193 -0.0023 0.0056  -0.0006 96  VAL   A CB  
1838 C CG1 A VAL   A 96  ? 0.1222 0.1182 0.0952 -0.0037 0.0116  0.0083  96  VAL   A CG1 
1839 C CG1 B VAL   A 96  ? 0.1369 0.1248 0.1286 -0.0020 0.0041  -0.0023 96  VAL   A CG1 
1840 C CG2 A VAL   A 96  ? 0.1287 0.1150 0.1117 -0.0118 0.0202  0.0125  96  VAL   A CG2 
1841 C CG2 B VAL   A 96  ? 0.1306 0.1229 0.1241 -0.0035 0.0018  -0.0018 96  VAL   A CG2 
1860 N N   A GLY   A 97  ? 0.1187 0.1098 0.1013 -0.0052 0.0131  0.0055  97  GLY   A N   
1861 N N   B GLY   A 97  ? 0.1272 0.1307 0.1155 0.0036  -0.0010 0.0004  97  GLY   A N   
1862 C CA  A GLY   A 97  ? 0.1276 0.1170 0.1038 -0.0050 0.0057  0.0060  97  GLY   A CA  
1863 C CA  B GLY   A 97  ? 0.1314 0.1365 0.1187 0.0055  -0.0003 -0.0004 97  GLY   A CA  
1864 C C   A GLY   A 97  ? 0.1327 0.1326 0.0819 -0.0048 0.0060  0.0031  97  GLY   A C   
1865 C C   B GLY   A 97  ? 0.1373 0.1434 0.1177 0.0065  -0.0033 -0.0011 97  GLY   A C   
1866 O O   A GLY   A 97  ? 0.1424 0.1396 0.1044 -0.0047 0.0065  0.0174  97  GLY   A O   
1867 O O   B GLY   A 97  ? 0.1384 0.1440 0.1148 0.0071  -0.0072 0.0008  97  GLY   A O   
1874 N N   A PRO   A 98  ? 0.1380 0.1428 0.0808 0.0011  -0.0011 0.0164  98  PRO   A N   
1875 N N   B PRO   A 98  ? 0.1439 0.1484 0.1213 0.0076  -0.0049 0.0013  98  PRO   A N   
1876 C CA  A PRO   A 98  ? 0.1512 0.1614 0.0908 0.0040  0.0067  0.0062  98  PRO   A CA  
1877 C CA  B PRO   A 98  ? 0.1526 0.1545 0.1268 0.0078  -0.0039 0.0033  98  PRO   A CA  
1878 C C   A PRO   A 98  ? 0.1503 0.1675 0.0769 -0.0075 0.0045  0.0220  98  PRO   A C   
1879 C C   B PRO   A 98  ? 0.1627 0.1590 0.1296 0.0039  -0.0048 0.0086  98  PRO   A C   
1880 O O   A PRO   A 98  ? 0.1455 0.1535 0.1071 -0.0066 0.0006  0.0226  98  PRO   A O   
1881 O O   B PRO   A 98  ? 0.1620 0.1570 0.1292 0.0040  -0.0029 0.0078  98  PRO   A O   
1882 C CB  A PRO   A 98  ? 0.1626 0.1732 0.0844 0.0085  -0.0038 -0.0078 98  PRO   A CB  
1883 C CB  B PRO   A 98  ? 0.1522 0.1565 0.1268 0.0099  -0.0048 -0.0010 98  PRO   A CB  
1884 C CG  A PRO   A 98  ? 0.1578 0.1614 0.1028 0.0070  -0.0097 -0.0122 98  PRO   A CG  
1885 C CG  B PRO   A 98  ? 0.1503 0.1539 0.1286 0.0100  -0.0061 -0.0041 98  PRO   A CG  
1886 C CD  A PRO   A 98  ? 0.1450 0.1434 0.0891 0.0014  -0.0051 0.0057  98  PRO   A CD  
1887 C CD  B PRO   A 98  ? 0.1457 0.1498 0.1246 0.0086  -0.0069 -0.0021 98  PRO   A CD  
1902 N N   A ASN   A 99  ? 0.1564 0.1901 0.0891 -0.0041 0.0036  0.0401  99  ASN   A N   
1903 N N   B ASN   A 99  ? 0.1738 0.1655 0.1380 0.0029  -0.0078 0.0151  99  ASN   A N   
1904 C CA  A ASN   A 99  ? 0.1725 0.2043 0.1082 -0.0057 0.0029  0.0607  99  ASN   A CA  
1905 C CA  B ASN   A 99  ? 0.1864 0.1720 0.1547 0.0003  -0.0123 0.0171  99  ASN   A CA  
1906 C C   A ASN   A 99  ? 0.1814 0.2449 0.0945 -0.0132 0.0080  0.0592  99  ASN   A C   
1907 C C   B ASN   A 99  ? 0.1990 0.1814 0.1591 -0.0044 -0.0117 0.0104  99  ASN   A C   
1908 O O   A ASN   A 99  ? 0.1908 0.2729 0.1072 -0.0077 0.0045  0.0586  99  ASN   A O   
1909 O O   B ASN   A 99  ? 0.1968 0.1750 0.1530 -0.0083 -0.0152 0.0043  99  ASN   A O   
1910 C CB  A ASN   A 99  ? 0.1776 0.1942 0.1236 -0.0066 -0.0097 0.0636  99  ASN   A CB  
1911 C CB  B ASN   A 99  ? 0.1874 0.1727 0.1771 0.0006  -0.0173 0.0237  99  ASN   A CB  
1912 C CG  A ASN   A 99  ? 0.1816 0.1875 0.1456 -0.0091 -0.0188 0.0460  99  ASN   A CG  
1913 C CG  B ASN   A 99  ? 0.1884 0.1722 0.1979 0.0010  -0.0197 0.0307  99  ASN   A CG  
1914 O OD1 A ASN   A 99  ? 0.1953 0.1972 0.1625 -0.0029 -0.0308 0.0340  99  ASN   A OD1 
1915 O OD1 B ASN   A 99  ? 0.1907 0.1729 0.2024 0.0031  -0.0208 0.0318  99  ASN   A OD1 
1916 N ND2 A ASN   A 99  ? 0.1827 0.1861 0.1633 -0.0048 -0.0170 0.0481  99  ASN   A ND2 
1917 N ND2 B ASN   A 99  ? 0.1882 0.1718 0.2062 0.0013  -0.0192 0.0317  99  ASN   A ND2 
1930 N N   A VAL   A 100 ? 0.1938 0.2526 0.0896 -0.0240 -0.0157 0.0469  100 VAL   A N   
1931 N N   B VAL   A 100 ? 0.2132 0.1980 0.1776 -0.0052 -0.0096 0.0075  100 VAL   A N   
1932 C CA  A VAL   A 100 ? 0.2185 0.2818 0.1165 -0.0345 -0.0253 0.0400  100 VAL   A CA  
1933 C CA  B VAL   A 100 ? 0.2266 0.2162 0.1989 -0.0054 -0.0057 0.0057  100 VAL   A CA  
1934 C C   A VAL   A 100 ? 0.2276 0.2921 0.1048 -0.0379 -0.0311 0.0633  100 VAL   A C   
1935 C C   B VAL   A 100 ? 0.2400 0.2354 0.2143 -0.0040 -0.0072 0.0121  100 VAL   A C   
1936 O O   A VAL   A 100 ? 0.2390 0.3158 0.1231 -0.0374 -0.0128 0.0618  100 VAL   A O   
1937 O O   B VAL   A 100 ? 0.2412 0.2387 0.2183 -0.0012 -0.0061 0.0133  100 VAL   A O   
1938 C CB  A VAL   A 100 ? 0.2426 0.2831 0.1623 -0.0409 -0.0284 0.0315  100 VAL   A CB  
1939 C CB  B VAL   A 100 ? 0.2256 0.2138 0.2020 -0.0067 -0.0031 0.0006  100 VAL   A CB  
1940 C CG1 A VAL   A 100 ? 0.2463 0.2907 0.1845 -0.0444 -0.0262 0.0297  100 VAL   A CG1 
1941 C CG1 B VAL   A 100 ? 0.2256 0.2137 0.2038 -0.0058 -0.0018 -0.0011 100 VAL   A CG1 
1942 C CG2 A VAL   A 100 ? 0.2552 0.2865 0.1808 -0.0453 -0.0200 0.0193  100 VAL   A CG2 
1943 C CG2 B VAL   A 100 ? 0.2247 0.2129 0.2040 -0.0082 -0.0029 -0.0033 100 VAL   A CG2 
1962 N N   A ASN   A 101 ? 0.2433 0.3056 0.1399 -0.0419 -0.0355 0.0954  101 ASN   A N   
1963 N N   B ASN   A 101 ? 0.2520 0.2517 0.2302 -0.0050 -0.0091 0.0170  101 ASN   A N   
1964 C CA  A ASN   A 101 ? 0.2744 0.3154 0.1772 -0.0481 -0.0397 0.1167  101 ASN   A CA  
1965 C CA  B ASN   A 101 ? 0.2647 0.2684 0.2461 -0.0065 -0.0140 0.0219  101 ASN   A CA  
1966 C C   A ASN   A 101 ? 0.2974 0.3382 0.1996 -0.0519 -0.0044 0.1396  101 ASN   A C   
1967 C C   B ASN   A 101 ? 0.2744 0.2830 0.2614 -0.0079 -0.0142 0.0284  101 ASN   A C   
1968 O O   A ASN   A 101 ? 0.3166 0.3478 0.2429 -0.0568 -0.0068 0.1417  101 ASN   A O   
1969 O O   B ASN   A 101 ? 0.2764 0.2848 0.2630 -0.0090 -0.0172 0.0316  101 ASN   A O   
1970 C CB  A ASN   A 101 ? 0.2841 0.3020 0.1800 -0.0394 -0.0728 0.1021  101 ASN   A CB  
1971 C CB  B ASN   A 101 ? 0.2676 0.2707 0.2488 -0.0066 -0.0170 0.0176  101 ASN   A CB  
1972 C CG  A ASN   A 101 ? 0.2909 0.2922 0.1696 -0.0349 -0.0947 0.0600  101 ASN   A CG  
1973 C CG  B ASN   A 101 ? 0.2694 0.2725 0.2492 -0.0065 -0.0190 0.0126  101 ASN   A CG  
1974 O OD1 A ASN   A 101 ? 0.2934 0.2997 0.1839 -0.0253 -0.0860 0.0102  101 ASN   A OD1 
1975 O OD1 B ASN   A 101 ? 0.2692 0.2747 0.2518 -0.0045 -0.0189 0.0081  101 ASN   A OD1 
1976 N ND2 A ASN   A 101 ? 0.2968 0.2766 0.1645 -0.0468 -0.0915 0.0597  101 ASN   A ND2 
1977 N ND2 B ASN   A 101 ? 0.2711 0.2726 0.2480 -0.0076 -0.0201 0.0140  101 ASN   A ND2 
1990 N N   A LYS   A 102 ? 0.3037 0.3727 0.2178 -0.0655 0.0189  0.1439  102 LYS   A N   
1991 N N   B LYS   A 102 ? 0.2811 0.2948 0.2765 -0.0082 -0.0115 0.0278  102 LYS   A N   
1992 C CA  A LYS   A 102 ? 0.3158 0.4009 0.2335 -0.0650 0.0292  0.1283  102 LYS   A CA  
1993 C CA  B LYS   A 102 ? 0.2867 0.3041 0.2875 -0.0074 -0.0087 0.0254  102 LYS   A CA  
1994 C C   A LYS   A 102 ? 0.3227 0.4221 0.2040 -0.0519 0.0340  0.1226  102 LYS   A C   
1995 C C   B LYS   A 102 ? 0.2882 0.3094 0.2825 -0.0064 -0.0055 0.0240  102 LYS   A C   
1996 O O   A LYS   A 102 ? 0.3254 0.4377 0.2090 -0.0479 0.0389  0.1128  102 LYS   A O   
1997 O O   B LYS   A 102 ? 0.2885 0.3120 0.2856 -0.0059 -0.0053 0.0236  102 LYS   A O   
1998 C CB  A LYS   A 102 ? 0.3269 0.4089 0.2737 -0.0737 0.0217  0.1110  102 LYS   A CB  
1999 C CB  B LYS   A 102 ? 0.2898 0.3077 0.3007 -0.0074 -0.0078 0.0238  102 LYS   A CB  
2000 C CG  A LYS   A 102 ? 0.3372 0.4146 0.3067 -0.0792 0.0103  0.0896  102 LYS   A CG  
2001 C CG  B LYS   A 102 ? 0.2922 0.3104 0.3112 -0.0076 -0.0080 0.0216  102 LYS   A CG  
2002 C CD  A LYS   A 102 ? 0.3499 0.4210 0.3341 -0.0799 -0.0032 0.0645  102 LYS   A CD  
2003 C CD  B LYS   A 102 ? 0.2948 0.3132 0.3195 -0.0076 -0.0081 0.0185  102 LYS   A CD  
2004 C CE  A LYS   A 102 ? 0.3619 0.4268 0.3571 -0.0781 -0.0142 0.0459  102 LYS   A CE  
2005 C CE  B LYS   A 102 ? 0.2971 0.3156 0.3259 -0.0071 -0.0084 0.0167  102 LYS   A CE  
2006 N NZ  A LYS   A 102 ? 0.3701 0.4291 0.3693 -0.0798 -0.0178 0.0333  102 LYS   A NZ  
2007 N NZ  B LYS   A 102 ? 0.2982 0.3168 0.3286 -0.0072 -0.0078 0.0152  102 LYS   A NZ  
2034 N N   A GLY   A 103 ? 0.3232 0.4323 0.1921 -0.0380 0.0231  0.0912  103 GLY   A N   
2035 N N   B GLY   A 103 ? 0.2880 0.3113 0.2760 -0.0051 -0.0048 0.0199  103 GLY   A N   
2036 C CA  A GLY   A 103 ? 0.3252 0.4345 0.1732 -0.0271 0.0196  0.0715  103 GLY   A CA  
2037 C CA  B GLY   A 103 ? 0.2864 0.3115 0.2670 -0.0047 -0.0026 0.0166  103 GLY   A CA  
2038 C C   A GLY   A 103 ? 0.3205 0.4333 0.1657 -0.0216 0.0246  0.0476  103 GLY   A C   
2039 C C   B GLY   A 103 ? 0.2850 0.3122 0.2596 -0.0045 -0.0014 0.0118  103 GLY   A C   
2040 O O   A GLY   A 103 ? 0.3292 0.4442 0.1856 -0.0173 0.0241  0.0298  103 GLY   A O   
2041 O O   B GLY   A 103 ? 0.2841 0.3129 0.2605 -0.0050 0.0002  0.0114  103 GLY   A O   
2048 N N   A GLU   A 104 ? 0.3039 0.4184 0.1240 -0.0229 0.0269  0.0348  104 GLU   A N   
2049 N N   B GLU   A 104 ? 0.2846 0.3120 0.2517 -0.0038 -0.0020 0.0067  104 GLU   A N   
2050 C CA  A GLU   A 104 ? 0.2826 0.4026 0.1077 -0.0317 0.0237  0.0187  104 GLU   A CA  
2051 C CA  B GLU   A 104 ? 0.2832 0.3111 0.2443 -0.0041 -0.0025 0.0010  104 GLU   A CA  
2052 C C   A GLU   A 104 ? 0.2811 0.4069 0.1097 -0.0358 0.0310  -0.0004 104 GLU   A C   
2053 C C   B GLU   A 104 ? 0.2857 0.3146 0.2499 -0.0060 0.0002  -0.0055 104 GLU   A C   
2054 O O   A GLU   A 104 ? 0.2749 0.4063 0.1551 -0.0396 0.0188  -0.0076 104 GLU   A O   
2055 O O   B GLU   A 104 ? 0.2852 0.3154 0.2495 -0.0070 -0.0003 -0.0068 104 GLU   A O   
2056 C CB  A GLU   A 104 ? 0.2591 0.3751 0.1109 -0.0351 0.0303  0.0404  104 GLU   A CB  
2057 C CB  B GLU   A 104 ? 0.2793 0.3068 0.2346 -0.0027 -0.0053 0.0044  104 GLU   A CB  
2058 C CG  A GLU   A 104 ? 0.2448 0.3628 0.1284 -0.0372 0.0251  0.0519  104 GLU   A CG  
2059 C CG  B GLU   A 104 ? 0.2769 0.3029 0.2315 -0.0008 -0.0074 0.0073  104 GLU   A CG  
2060 C CD  A GLU   A 104 ? 0.2256 0.3462 0.1284 -0.0382 0.0234  0.0680  104 GLU   A CD  
2061 C CD  B GLU   A 104 ? 0.2742 0.2989 0.2276 0.0008  -0.0087 0.0100  104 GLU   A CD  
2062 O OE1 A GLU   A 104 ? 0.2083 0.3341 0.1120 -0.0345 0.0151  0.0653  104 GLU   A OE1 
2063 O OE1 B GLU   A 104 ? 0.2730 0.2974 0.2251 0.0018  -0.0097 0.0121  104 GLU   A OE1 
2064 O OE2 A GLU   A 104 ? 0.2361 0.3455 0.1490 -0.0433 0.0226  0.0830  104 GLU   A OE2 
2065 O OE2 B GLU   A 104 ? 0.2748 0.2979 0.2286 0.0008  -0.0094 0.0100  104 GLU   A OE2 
2078 N N   A ASP   A 105 ? 0.2876 0.4181 0.1288 -0.0374 0.0398  -0.0218 105 ASP   A N   
2079 N N   B ASP   A 105 ? 0.2885 0.3174 0.2605 -0.0070 0.0035  -0.0109 105 ASP   A N   
2080 C CA  A ASP   A 105 ? 0.2885 0.4211 0.1719 -0.0351 0.0408  -0.0490 105 ASP   A CA  
2081 C CA  B ASP   A 105 ? 0.2913 0.3190 0.2742 -0.0082 0.0052  -0.0168 105 ASP   A CA  
2082 C C   A ASP   A 105 ? 0.2510 0.4038 0.1400 -0.0419 0.0201  -0.0578 105 ASP   A C   
2083 C C   B ASP   A 105 ? 0.2853 0.3152 0.2645 -0.0109 0.0047  -0.0183 105 ASP   A C   
2084 O O   A ASP   A 105 ? 0.2243 0.3695 0.1195 -0.0388 0.0080  -0.0733 105 ASP   A O   
2085 O O   B ASP   A 105 ? 0.2844 0.3157 0.2615 -0.0103 0.0029  -0.0184 105 ASP   A O   
2086 C CB  A ASP   A 105 ? 0.3215 0.4456 0.2490 -0.0287 0.0599  -0.0610 105 ASP   A CB  
2087 C CB  B ASP   A 105 ? 0.2985 0.3230 0.2976 -0.0066 0.0069  -0.0217 105 ASP   A CB  
2088 C CG  A ASP   A 105 ? 0.3502 0.4635 0.3243 -0.0206 0.0630  -0.0745 105 ASP   A CG  
2089 C CG  B ASP   A 105 ? 0.3045 0.3263 0.3171 -0.0052 0.0069  -0.0270 105 ASP   A CG  
2090 O OD1 A ASP   A 105 ? 0.3577 0.4695 0.3349 -0.0201 0.0629  -0.0892 105 ASP   A OD1 
2091 O OD1 B ASP   A 105 ? 0.3075 0.3274 0.3232 -0.0047 0.0067  -0.0309 105 ASP   A OD1 
2092 O OD2 A ASP   A 105 ? 0.3646 0.4721 0.3711 -0.0192 0.0674  -0.0679 105 ASP   A OD2 
2093 O OD2 B ASP   A 105 ? 0.3066 0.3278 0.3253 -0.0052 0.0071  -0.0283 105 ASP   A OD2 
2102 N N   A ILE   A 106 ? 0.2408 0.3977 0.1624 -0.0452 -0.0065 -0.0508 106 ILE   A N   
2103 N N   B ILE   A 106 ? 0.2801 0.3094 0.2588 -0.0146 0.0042  -0.0204 106 ILE   A N   
2104 C CA  A ILE   A 106 ? 0.2151 0.3841 0.1852 -0.0561 -0.0315 -0.0615 106 ILE   A CA  
2105 C CA  B ILE   A 106 ? 0.2724 0.3012 0.2537 -0.0182 0.0053  -0.0252 106 ILE   A CA  
2106 C C   A ILE   A 106 ? 0.1946 0.3532 0.2020 -0.0691 -0.0288 -0.0838 106 ILE   A C   
2107 C C   B ILE   A 106 ? 0.2632 0.2889 0.2566 -0.0227 0.0091  -0.0340 106 ILE   A C   
2108 O O   A ILE   A 106 ? 0.1740 0.3390 0.2071 -0.0694 -0.0133 -0.0930 106 ILE   A O   
2109 O O   B ILE   A 106 ? 0.2623 0.2861 0.2536 -0.0217 0.0106  -0.0374 106 ILE   A O   
2110 C CB  A ILE   A 106 ? 0.2173 0.3970 0.2298 -0.0464 -0.0478 -0.0349 106 ILE   A CB  
2111 C CB  B ILE   A 106 ? 0.2735 0.3035 0.2507 -0.0167 0.0041  -0.0220 106 ILE   A CB  
2112 C CG1 A ILE   A 106 ? 0.2134 0.3977 0.2618 -0.0360 -0.0519 -0.0136 106 ILE   A CG1 
2113 C CG1 B ILE   A 106 ? 0.2726 0.3020 0.2501 -0.0162 0.0029  -0.0200 106 ILE   A CG1 
2114 C CG2 A ILE   A 106 ? 0.2210 0.4029 0.2470 -0.0467 -0.0532 -0.0350 106 ILE   A CG2 
2115 C CG2 B ILE   A 106 ? 0.2748 0.3054 0.2517 -0.0164 0.0041  -0.0206 106 ILE   A CG2 
2116 C CD1 A ILE   A 106 ? 0.2147 0.3949 0.2790 -0.0298 -0.0398 -0.0037 106 ILE   A CD1 
2117 C CD1 B ILE   A 106 ? 0.2722 0.3005 0.2503 -0.0158 0.0026  -0.0176 106 ILE   A CD1 
2140 N N   A GLN   A 107 ? 0.2099 0.3360 0.2202 -0.0718 -0.0220 -0.1020 107 GLN   A N   
2141 N N   B GLN   A 107 ? 0.2554 0.2795 0.2678 -0.0279 0.0137  -0.0392 107 GLN   A N   
2142 C CA  A GLN   A 107 ? 0.2358 0.3150 0.2938 -0.0564 0.0129  -0.1072 107 GLN   A CA  
2143 C CA  B GLN   A 107 ? 0.2458 0.2680 0.2800 -0.0311 0.0194  -0.0466 107 GLN   A CA  
2144 C C   A GLN   A 107 ? 0.2158 0.2645 0.2884 -0.0500 0.0307  -0.0735 107 GLN   A C   
2145 C C   B GLN   A 107 ? 0.2183 0.2439 0.2533 -0.0397 0.0278  -0.0557 107 GLN   A C   
2146 O O   A GLN   A 107 ? 0.2260 0.2553 0.3536 -0.0420 0.0419  -0.0607 107 GLN   A O   
2147 O O   B GLN   A 107 ? 0.2219 0.2438 0.2671 -0.0377 0.0315  -0.0511 107 GLN   A O   
2148 C CB  A GLN   A 107 ? 0.2745 0.3442 0.3841 -0.0570 0.0133  -0.1197 107 GLN   A CB  
2149 C CB  B GLN   A 107 ? 0.2621 0.2791 0.3200 -0.0272 0.0142  -0.0407 107 GLN   A CB  
2150 C CG  A GLN   A 107 ? 0.3139 0.3778 0.4826 -0.0541 0.0119  -0.1177 107 GLN   A CG  
2151 C CG  B GLN   A 107 ? 0.2758 0.2892 0.3608 -0.0237 0.0099  -0.0345 107 GLN   A CG  
2152 C CD  A GLN   A 107 ? 0.3430 0.4012 0.5613 -0.0521 0.0158  -0.1102 107 GLN   A CD  
2153 C CD  B GLN   A 107 ? 0.2864 0.2964 0.3936 -0.0198 0.0065  -0.0282 107 GLN   A CD  
2154 O OE1 A GLN   A 107 ? 0.3531 0.4075 0.5925 -0.0514 0.0188  -0.1088 107 GLN   A OE1 
2155 O OE1 B GLN   A 107 ? 0.2898 0.2985 0.4061 -0.0190 0.0064  -0.0250 107 GLN   A OE1 
2156 N NE2 A GLN   A 107 ? 0.3524 0.4109 0.5859 -0.0533 0.0156  -0.1100 107 GLN   A NE2 
2157 N NE2 B GLN   A 107 ? 0.2896 0.2981 0.4031 -0.0182 0.0057  -0.0269 107 GLN   A NE2 
2174 N N   . LEU   A 108 ? 0.1880 0.2187 0.2163 -0.0484 0.0332  -0.0732 108 LEU   A N   
2175 C CA  . LEU   A 108 ? 0.1645 0.1739 0.1858 -0.0172 0.0302  -0.0241 108 LEU   A CA  
2176 C C   . LEU   A 108 ? 0.1419 0.1387 0.1744 -0.0029 0.0173  0.0124  108 LEU   A C   
2177 O O   . LEU   A 108 ? 0.1346 0.1405 0.1895 0.0001  0.0176  0.0182  108 LEU   A O   
2178 C CB  . LEU   A 108 ? 0.1679 0.1822 0.1519 -0.0210 0.0334  -0.0183 108 LEU   A CB  
2179 C CG  . LEU   A 108 ? 0.1866 0.2064 0.1750 -0.0208 0.0418  -0.0198 108 LEU   A CG  
2180 C CD1 . LEU   A 108 ? 0.2124 0.2136 0.1686 -0.0318 0.0460  -0.0186 108 LEU   A CD1 
2181 C CD2 . LEU   A 108 ? 0.1875 0.2321 0.2219 -0.0087 0.0414  -0.0064 108 LEU   A CD2 
2194 N N   . LEU   A 109 ? 0.1307 0.1358 0.1669 0.0014  0.0141  0.0257  109 LEU   A N   
2195 C CA  . LEU   A 109 ? 0.1290 0.1311 0.1513 -0.0001 0.0087  0.0215  109 LEU   A CA  
2196 C C   . LEU   A 109 ? 0.1234 0.1231 0.1277 -0.0055 -0.0013 0.0131  109 LEU   A C   
2197 O O   . LEU   A 109 ? 0.1322 0.1131 0.1487 -0.0028 -0.0104 0.0020  109 LEU   A O   
2198 C CB  . LEU   A 109 ? 0.1328 0.1414 0.1595 0.0033  -0.0004 0.0368  109 LEU   A CB  
2199 C CG  . LEU   A 109 ? 0.1311 0.1411 0.1690 0.0028  0.0043  0.0371  109 LEU   A CG  
2200 C CD1 . LEU   A 109 ? 0.1350 0.1331 0.1974 0.0033  0.0116  0.0152  109 LEU   A CD1 
2201 C CD2 . LEU   A 109 ? 0.1285 0.1625 0.1847 0.0009  0.0009  0.0387  109 LEU   A CD2 
2213 N N   . LYS   A 110 ? 0.1212 0.1214 0.1303 -0.0043 0.0029  0.0051  110 LYS   A N   
2214 C CA  . LYS   A 110 ? 0.1165 0.1138 0.1368 -0.0048 0.0016  0.0101  110 LYS   A CA  
2215 C C   . LYS   A 110 ? 0.1229 0.1053 0.1231 -0.0021 0.0001  -0.0004 110 LYS   A C   
2216 O O   . LYS   A 110 ? 0.1210 0.1114 0.1287 -0.0061 0.0024  -0.0011 110 LYS   A O   
2217 C CB  . LYS   A 110 ? 0.1262 0.1196 0.1466 -0.0034 -0.0044 -0.0021 110 LYS   A CB  
2218 C CG  . LYS   A 110 ? 0.1294 0.1184 0.1505 -0.0046 0.0008  -0.0067 110 LYS   A CG  
2219 C CD  . LYS   A 110 ? 0.1375 0.1226 0.1613 -0.0042 -0.0054 -0.0070 110 LYS   A CD  
2220 C CE  . LYS   A 110 ? 0.1461 0.1269 0.1850 -0.0054 0.0094  -0.0146 110 LYS   A CE  
2221 N NZ  . LYS   A 110 ? 0.1493 0.1322 0.1932 -0.0115 0.0169  -0.0048 110 LYS   A NZ  
2235 N N   . SER   A 111 ? 0.1201 0.1150 0.1220 -0.0032 0.0018  0.0032  111 SER   A N   
2236 C CA  . SER   A 111 ? 0.1201 0.1209 0.1302 -0.0022 0.0063  0.0035  111 SER   A CA  
2237 C C   . SER   A 111 ? 0.1105 0.1159 0.1283 -0.0063 0.0089  0.0079  111 SER   A C   
2238 O O   . SER   A 111 ? 0.1223 0.1066 0.1446 -0.0028 0.0052  0.0055  111 SER   A O   
2239 C CB  . SER   A 111 ? 0.1352 0.1378 0.1411 -0.0076 0.0199  -0.0098 111 SER   A CB  
2240 O OG  . SER   A 111 ? 0.1853 0.1630 0.1585 -0.0040 0.0281  -0.0144 111 SER   A OG  
2246 N N   . ALA   A 112 ? 0.1109 0.1063 0.1395 0.0022  0.0107  0.0065  112 ALA   A N   
2247 C CA  . ALA   A 112 ? 0.1160 0.1043 0.1328 0.0008  0.0157  0.0011  112 ALA   A CA  
2248 C C   . ALA   A 112 ? 0.1147 0.0999 0.1317 -0.0009 0.0093  -0.0013 112 ALA   A C   
2249 O O   . ALA   A 112 ? 0.1167 0.1041 0.1321 -0.0102 0.0094  0.0003  112 ALA   A O   
2250 C CB  . ALA   A 112 ? 0.1285 0.1071 0.1373 -0.0030 0.0130  0.0015  112 ALA   A CB  
2256 N N   . TYR   A 113 ? 0.1049 0.1028 0.1380 -0.0013 0.0097  0.0058  113 TYR   A N   
2257 C CA  . TYR   A 113 ? 0.1057 0.0991 0.1329 -0.0006 0.0109  0.0077  113 TYR   A CA  
2258 C C   . TYR   A 113 ? 0.1045 0.0969 0.1220 -0.0072 0.0035  -0.0002 113 TYR   A C   
2259 O O   . TYR   A 113 ? 0.1079 0.1061 0.1330 -0.0029 0.0085  -0.0011 113 TYR   A O   
2260 C CB  . TYR   A 113 ? 0.1099 0.1091 0.1316 -0.0038 -0.0014 0.0121  113 TYR   A CB  
2261 C CG  . TYR   A 113 ? 0.1067 0.1079 0.1350 -0.0072 0.0040  0.0169  113 TYR   A CG  
2262 C CD1 . TYR   A 113 ? 0.1122 0.1177 0.1336 -0.0013 0.0088  0.0213  113 TYR   A CD1 
2263 C CD2 . TYR   A 113 ? 0.1098 0.1193 0.1370 -0.0079 -0.0010 0.0154  113 TYR   A CD2 
2264 C CE1 . TYR   A 113 ? 0.1153 0.1253 0.1317 -0.0015 0.0067  0.0268  113 TYR   A CE1 
2265 C CE2 . TYR   A 113 ? 0.1124 0.1237 0.1341 -0.0110 -0.0043 0.0209  113 TYR   A CE2 
2266 C CZ  . TYR   A 113 ? 0.1118 0.1240 0.1319 0.0027  0.0086  0.0273  113 TYR   A CZ  
2267 O OH  . TYR   A 113 ? 0.1119 0.1301 0.1489 0.0115  0.0083  0.0317  113 TYR   A OH  
2277 N N   . GLU   A 114 ? 0.1041 0.1044 0.1302 -0.0066 0.0038  0.0016  114 GLU   A N   
2278 C CA  . GLU   A 114 ? 0.1021 0.0993 0.1335 0.0042  0.0055  0.0131  114 GLU   A CA  
2279 C C   . GLU   A 114 ? 0.1005 0.1028 0.1302 0.0046  0.0133  0.0054  114 GLU   A C   
2280 O O   . GLU   A 114 ? 0.1119 0.1030 0.1311 0.0020  0.0039  0.0006  114 GLU   A O   
2281 C CB  . GLU   A 114 ? 0.1084 0.1026 0.1305 -0.0045 0.0028  0.0063  114 GLU   A CB  
2282 C CG  . GLU   A 114 ? 0.1165 0.1058 0.1314 0.0046  0.0040  -0.0012 114 GLU   A CG  
2283 C CD  . GLU   A 114 ? 0.1260 0.1072 0.1469 -0.0028 0.0022  0.0011  114 GLU   A CD  
2284 O OE1 . GLU   A 114 ? 0.1309 0.1104 0.1477 -0.0065 0.0149  -0.0086 114 GLU   A OE1 
2285 O OE2 . GLU   A 114 ? 0.1403 0.1149 0.1612 -0.0083 0.0114  -0.0131 114 GLU   A OE2 
2292 N N   . ASN   A 115 ? 0.1047 0.1060 0.1285 -0.0006 0.0086  0.0001  115 ASN   A N   
2293 C CA  . ASN   A 115 ? 0.1027 0.1089 0.1262 -0.0043 0.0075  0.0009  115 ASN   A CA  
2294 C C   . ASN   A 115 ? 0.1039 0.1068 0.1233 -0.0080 0.0018  -0.0021 115 ASN   A C   
2295 O O   . ASN   A 115 ? 0.1106 0.1192 0.1182 -0.0076 0.0061  0.0075  115 ASN   A O   
2296 C CB  . ASN   A 115 ? 0.1128 0.1133 0.1267 -0.0098 0.0078  0.0024  115 ASN   A CB  
2297 C CG  . ASN   A 115 ? 0.1149 0.1424 0.1379 -0.0123 0.0112  0.0112  115 ASN   A CG  
2298 O OD1 . ASN   A 115 ? 0.1200 0.2351 0.1651 -0.0146 0.0195  0.0264  115 ASN   A OD1 
2299 N ND2 . ASN   A 115 ? 0.1164 0.1267 0.1351 -0.0095 0.0226  0.0112  115 ASN   A ND2 
2306 N N   . PHE   A 116 ? 0.1040 0.1068 0.1179 -0.0022 0.0088  0.0057  116 PHE   A N   
2307 C CA  . PHE   A 116 ? 0.1039 0.1133 0.1202 -0.0015 0.0071  0.0111  116 PHE   A CA  
2308 C C   . PHE   A 116 ? 0.1060 0.1196 0.1175 -0.0062 0.0114  0.0096  116 PHE   A C   
2309 O O   . PHE   A 116 ? 0.1123 0.1243 0.1263 0.0020  0.0097  0.0134  116 PHE   A O   
2310 C CB  . PHE   A 116 ? 0.1083 0.1058 0.1289 -0.0011 0.0137  0.0096  116 PHE   A CB  
2311 C CG  . PHE   A 116 ? 0.1049 0.1067 0.1217 -0.0068 0.0103  0.0045  116 PHE   A CG  
2312 C CD1 . PHE   A 116 ? 0.1085 0.1071 0.1248 -0.0054 0.0151  0.0047  116 PHE   A CD1 
2313 C CD2 . PHE   A 116 ? 0.1137 0.1195 0.1345 -0.0029 0.0144  0.0103  116 PHE   A CD2 
2314 C CE1 . PHE   A 116 ? 0.1150 0.1027 0.1362 -0.0081 0.0048  0.0050  116 PHE   A CE1 
2315 C CE2 . PHE   A 116 ? 0.1106 0.1144 0.1407 -0.0003 0.0106  0.0071  116 PHE   A CE2 
2316 C CZ  . PHE   A 116 ? 0.1161 0.1023 0.1292 0.0007  0.0046  0.0111  116 PHE   A CZ  
2326 N N   . ASN   A 117 ? 0.1061 0.1135 0.1217 -0.0012 0.0108  0.0105  117 ASN   A N   
2327 C CA  . ASN   A 117 ? 0.1104 0.1086 0.1312 -0.0008 0.0087  0.0140  117 ASN   A CA  
2328 C C   . ASN   A 117 ? 0.1121 0.1186 0.1431 0.0023  0.0078  0.0131  117 ASN   A C   
2329 O O   . ASN   A 117 ? 0.1181 0.1259 0.1558 -0.0010 -0.0076 0.0256  117 ASN   A O   
2330 C CB  . ASN   A 117 ? 0.1102 0.1089 0.1411 0.0010  0.0070  0.0170  117 ASN   A CB  
2331 C CG  . ASN   A 117 ? 0.1108 0.1123 0.1367 -0.0005 0.0082  0.0238  117 ASN   A CG  
2332 O OD1 . ASN   A 117 ? 0.1151 0.1376 0.1418 -0.0094 0.0123  0.0169  117 ASN   A OD1 
2333 N ND2 . ASN   A 117 ? 0.1061 0.1184 0.1381 0.0008  0.0092  0.0206  117 ASN   A ND2 
2340 N N   . GLN   A 118 ? 0.1080 0.1162 0.1508 -0.0041 -0.0041 0.0164  118 GLN   A N   
2341 C CA  . GLN   A 118 ? 0.1151 0.1257 0.1508 -0.0044 -0.0017 0.0083  118 GLN   A CA  
2342 C C   . GLN   A 118 ? 0.1130 0.1323 0.1411 -0.0025 -0.0064 0.0115  118 GLN   A C   
2343 O O   . GLN   A 118 ? 0.1147 0.1662 0.1706 0.0044  -0.0124 -0.0036 118 GLN   A O   
2344 C CB  . GLN   A 118 ? 0.1080 0.1346 0.1644 -0.0001 -0.0016 0.0149  118 GLN   A CB  
2345 C CG  . GLN   A 118 ? 0.1086 0.1367 0.1618 -0.0008 0.0074  0.0179  118 GLN   A CG  
2346 C CD  . GLN   A 118 ? 0.1096 0.1378 0.1611 -0.0006 0.0064  0.0129  118 GLN   A CD  
2347 O OE1 . GLN   A 118 ? 0.1193 0.1500 0.1714 0.0105  -0.0065 0.0032  118 GLN   A OE1 
2348 N NE2 . GLN   A 118 ? 0.1260 0.1277 0.1679 0.0040  -0.0001 0.0131  118 GLN   A NE2 
2357 N N   . HIS   A 119 ? 0.1179 0.1291 0.1285 -0.0022 -0.0046 0.0137  119 HIS   A N   
2358 C CA  . HIS   A 119 ? 0.1252 0.1353 0.1373 -0.0024 -0.0027 0.0182  119 HIS   A CA  
2359 C C   . HIS   A 119 ? 0.1345 0.1394 0.1271 -0.0059 0.0013  0.0126  119 HIS   A C   
2360 O O   . HIS   A 119 ? 0.1380 0.1510 0.1311 -0.0240 -0.0016 0.0193  119 HIS   A O   
2361 C CB  . HIS   A 119 ? 0.1287 0.1336 0.1536 -0.0004 0.0172  0.0183  119 HIS   A CB  
2362 C CG  . HIS   A 119 ? 0.1350 0.1310 0.2023 0.0034  0.0201  0.0350  119 HIS   A CG  
2363 N ND1 . HIS   A 119 ? 0.1429 0.1519 0.2591 -0.0063 0.0167  0.0194  119 HIS   A ND1 
2364 C CD2 . HIS   A 119 ? 0.1485 0.1454 0.2271 0.0184  0.0359  0.0469  119 HIS   A CD2 
2365 C CE1 . HIS   A 119 ? 0.1413 0.1541 0.2818 -0.0124 0.0290  0.0399  119 HIS   A CE1 
2366 N NE2 . HIS   A 119 ? 0.1592 0.1541 0.2739 0.0086  0.0491  0.0559  119 HIS   A NE2 
2374 N N   . GLU   A 120 ? 0.1421 0.1530 0.1257 -0.0016 0.0009  0.0294  120 GLU   A N   
2375 C CA  . GLU   A 120 ? 0.1600 0.1737 0.1438 0.0121  0.0005  0.0500  120 GLU   A CA  
2376 C C   . GLU   A 120 ? 0.1452 0.1573 0.1204 -0.0038 -0.0060 0.0453  120 GLU   A C   
2377 O O   . GLU   A 120 ? 0.1469 0.1572 0.1357 -0.0070 -0.0027 0.0412  120 GLU   A O   
2378 C CB  . GLU   A 120 ? 0.2102 0.2441 0.1928 0.0356  -0.0086 0.1109  120 GLU   A CB  
2379 C CG  . GLU   A 120 ? 0.2979 0.3234 0.3071 0.0517  -0.0086 0.1249  120 GLU   A CG  
2380 C CD  . GLU   A 120 ? 0.3757 0.3866 0.4379 0.0628  0.0066  0.1137  120 GLU   A CD  
2381 O OE1 . GLU   A 120 ? 0.4033 0.4081 0.4747 0.0634  0.0094  0.1079  120 GLU   A OE1 
2382 O OE2 . GLU   A 120 ? 0.4382 0.4382 0.4932 0.0683  0.0140  0.1131  120 GLU   A OE2 
2389 N N   . VAL   A 121 ? 0.1378 0.1552 0.1144 -0.0045 0.0019  0.0377  121 VAL   A N   
2390 C CA  . VAL   A 121 ? 0.1445 0.1664 0.1103 -0.0055 0.0103  0.0337  121 VAL   A CA  
2391 C C   . VAL   A 121 ? 0.1363 0.1485 0.1023 -0.0127 0.0040  0.0215  121 VAL   A C   
2392 O O   . VAL   A 121 ? 0.1408 0.1573 0.1236 -0.0205 -0.0093 0.0181  121 VAL   A O   
2393 C CB  . VAL   A 121 ? 0.1822 0.2023 0.1370 0.0081  0.0255  0.0435  121 VAL   A CB  
2394 C CG1 . VAL   A 121 ? 0.1895 0.2183 0.1462 0.0143  0.0367  0.0462  121 VAL   A CG1 
2395 C CG2 . VAL   A 121 ? 0.2082 0.2185 0.1892 0.0026  0.0250  0.0352  121 VAL   A CG2 
2405 N N   . LEU   A 122 ? 0.1289 0.1357 0.1150 -0.0100 0.0055  0.0235  122 LEU   A N   
2406 C CA  . LEU   A 122 ? 0.1339 0.1279 0.1183 -0.0138 0.0238  0.0182  122 LEU   A CA  
2407 C C   . LEU   A 122 ? 0.1278 0.1264 0.1108 -0.0181 0.0076  0.0106  122 LEU   A C   
2408 O O   . LEU   A 122 ? 0.1281 0.1346 0.1483 -0.0219 0.0064  0.0181  122 LEU   A O   
2409 C CB  . LEU   A 122 ? 0.1492 0.1390 0.1515 -0.0068 0.0116  0.0267  122 LEU   A CB  
2410 C CG  . LEU   A 122 ? 0.1518 0.1410 0.1348 -0.0070 0.0204  0.0145  122 LEU   A CG  
2411 C CD1 . LEU   A 122 ? 0.1758 0.1404 0.1475 -0.0137 0.0176  0.0212  122 LEU   A CD1 
2412 C CD2 . LEU   A 122 ? 0.1451 0.1362 0.1314 -0.0032 0.0241  0.0172  122 LEU   A CD2 
2424 N N   . LEU   A 123 ? 0.1204 0.1270 0.1085 -0.0144 0.0086  0.0142  123 LEU   A N   
2425 C CA  . LEU   A 123 ? 0.1235 0.1228 0.1071 -0.0116 0.0136  0.0144  123 LEU   A CA  
2426 C C   . LEU   A 123 ? 0.1187 0.1217 0.0993 -0.0111 0.0126  0.0164  123 LEU   A C   
2427 O O   . LEU   A 123 ? 0.1184 0.1398 0.1037 -0.0231 0.0083  0.0188  123 LEU   A O   
2428 C CB  . LEU   A 123 ? 0.1272 0.1327 0.1123 -0.0122 0.0173  0.0163  123 LEU   A CB  
2429 C CG  . LEU   A 123 ? 0.1336 0.1421 0.1279 -0.0144 0.0257  0.0092  123 LEU   A CG  
2430 C CD1 . LEU   A 123 ? 0.1393 0.1449 0.1527 -0.0009 0.0174  -0.0020 123 LEU   A CD1 
2431 C CD2 . LEU   A 123 ? 0.1462 0.1464 0.1297 -0.0081 0.0202  -0.0025 123 LEU   A CD2 
2443 N N   A ALA   A 124 ? 0.1173 0.1173 0.0992 -0.0156 0.0107  0.0145  124 ALA   A N   
2444 N N   B ALA   A 124 ? 0.1237 0.1228 0.1012 -0.0118 0.0090  0.0157  124 ALA   A N   
2445 C CA  A ALA   A 124 ? 0.1095 0.1215 0.1098 -0.0096 0.0089  0.0147  124 ALA   A CA  
2446 C CA  B ALA   A 124 ? 0.1268 0.1268 0.1079 -0.0115 0.0055  0.0170  124 ALA   A CA  
2447 C C   A ALA   A 124 ? 0.1076 0.1140 0.1130 -0.0112 0.0116  0.0113  124 ALA   A C   
2448 C C   B ALA   A 124 ? 0.1263 0.1261 0.1113 -0.0067 0.0013  0.0166  124 ALA   A C   
2449 O O   A ALA   A 124 ? 0.1098 0.1213 0.1272 -0.0104 0.0180  0.0228  124 ALA   A O   
2450 O O   B ALA   A 124 ? 0.1249 0.1233 0.1122 -0.0025 -0.0000 0.0228  124 ALA   A O   
2451 C CB  A ALA   A 124 ? 0.1057 0.1242 0.1181 -0.0123 0.0048  0.0208  124 ALA   A CB  
2452 C CB  B ALA   A 124 ? 0.1304 0.1287 0.1109 -0.0160 0.0076  0.0177  124 ALA   A CB  
2463 N N   A PRO   A 125 ? 0.1068 0.1119 0.1202 -0.0089 0.0084  0.0270  125 PRO   A N   
2464 N N   B PRO   A 125 ? 0.1266 0.1290 0.1138 -0.0029 -0.0020 0.0112  125 PRO   A N   
2465 C CA  A PRO   A 125 ? 0.1119 0.1185 0.1221 -0.0067 0.0047  0.0250  125 PRO   A CA  
2466 C CA  B PRO   A 125 ? 0.1272 0.1318 0.1172 -0.0001 -0.0030 0.0084  125 PRO   A CA  
2467 C C   A PRO   A 125 ? 0.1092 0.1230 0.1181 -0.0098 0.0060  0.0245  125 PRO   A C   
2468 C C   B PRO   A 125 ? 0.1231 0.1305 0.1217 -0.0028 0.0009  0.0092  125 PRO   A C   
2469 O O   A PRO   A 125 ? 0.1158 0.1245 0.1318 0.0005  -0.0033 0.0183  125 PRO   A O   
2470 O O   B PRO   A 125 ? 0.1243 0.1305 0.1254 -0.0021 0.0035  0.0103  125 PRO   A O   
2471 C CB  A PRO   A 125 ? 0.1211 0.1152 0.1229 -0.0110 0.0159  0.0287  125 PRO   A CB  
2472 C CB  B PRO   A 125 ? 0.1300 0.1338 0.1122 -0.0005 -0.0012 0.0057  125 PRO   A CB  
2473 C CG  A PRO   A 125 ? 0.1166 0.1098 0.1301 -0.0079 0.0217  0.0211  125 PRO   A CG  
2474 C CG  B PRO   A 125 ? 0.1323 0.1333 0.1159 -0.0018 -0.0024 0.0058  125 PRO   A CG  
2475 C CD  A PRO   A 125 ? 0.1118 0.1136 0.1233 -0.0113 0.0160  0.0247  125 PRO   A CD  
2476 C CD  B PRO   A 125 ? 0.1295 0.1320 0.1144 -0.0025 -0.0021 0.0085  125 PRO   A CD  
2491 N N   A LEU   A 126 ? 0.1114 0.1395 0.1078 -0.0034 0.0035  0.0252  126 LEU   A N   
2492 N N   B LEU   A 126 ? 0.1205 0.1324 0.1242 -0.0034 0.0013  0.0092  126 LEU   A N   
2493 C CA  A LEU   A 126 ? 0.1148 0.1362 0.1209 -0.0117 0.0029  0.0244  126 LEU   A CA  
2494 C CA  B LEU   A 126 ? 0.1176 0.1299 0.1220 -0.0052 0.0012  0.0134  126 LEU   A CA  
2495 C C   A LEU   A 126 ? 0.1174 0.1255 0.1201 -0.0040 -0.0018 0.0223  126 LEU   A C   
2496 C C   B LEU   A 126 ? 0.1096 0.1232 0.1101 -0.0048 -0.0024 0.0174  126 LEU   A C   
2497 O O   A LEU   A 126 ? 0.1231 0.1236 0.1415 0.0049  0.0103  0.0218  126 LEU   A O   
2498 O O   B LEU   A 126 ? 0.1094 0.1240 0.1151 -0.0055 -0.0072 0.0190  126 LEU   A O   
2499 C CB  A LEU   A 126 ? 0.1187 0.1515 0.1353 -0.0167 -0.0007 0.0247  126 LEU   A CB  
2500 C CB  B LEU   A 126 ? 0.1211 0.1356 0.1289 -0.0050 0.0020  0.0114  126 LEU   A CB  
2501 C CG  A LEU   A 126 ? 0.1206 0.1759 0.1603 -0.0220 0.0064  0.0227  126 LEU   A CG  
2502 C CG  B LEU   A 126 ? 0.1246 0.1420 0.1367 -0.0038 0.0046  0.0115  126 LEU   A CG  
2503 C CD1 A LEU   A 126 ? 0.1192 0.1896 0.1970 -0.0286 0.0034  0.0168  126 LEU   A CD1 
2504 C CD1 B LEU   A 126 ? 0.1246 0.1449 0.1486 -0.0044 0.0041  0.0124  126 LEU   A CD1 
2505 C CD2 A LEU   A 126 ? 0.1263 0.1668 0.1623 -0.0311 -0.0004 0.0305  126 LEU   A CD2 
2506 C CD2 B LEU   A 126 ? 0.1272 0.1402 0.1349 -0.0048 0.0036  0.0119  126 LEU   A CD2 
2529 N N   A LEU   A 127 ? 0.1192 0.1263 0.1325 0.0035  0.0027  0.0282  127 LEU   A N   
2530 N N   B LEU   A 127 ? 0.1037 0.1182 0.0998 -0.0025 0.0005  0.0210  127 LEU   A N   
2531 C CA  A LEU   A 127 ? 0.1135 0.1256 0.1224 -0.0015 -0.0059 0.0189  127 LEU   A CA  
2532 C CA  B LEU   A 127 ? 0.0972 0.1177 0.0981 -0.0014 -0.0013 0.0209  127 LEU   A CA  
2533 C C   A LEU   A 127 ? 0.1128 0.1147 0.1114 -0.0028 -0.0009 0.0147  127 LEU   A C   
2534 C C   B LEU   A 127 ? 0.0960 0.1158 0.1003 -0.0034 -0.0021 0.0162  127 LEU   A C   
2535 O O   A LEU   A 127 ? 0.1240 0.1177 0.1248 -0.0091 -0.0026 0.0176  127 LEU   A O   
2536 O O   B LEU   A 127 ? 0.0964 0.1135 0.0964 -0.0061 0.0025  0.0278  127 LEU   A O   
2537 C CB  A LEU   A 127 ? 0.1175 0.1302 0.1196 0.0025  0.0033  0.0134  127 LEU   A CB  
2538 C CB  B LEU   A 127 ? 0.0974 0.1222 0.1045 0.0012  -0.0062 0.0147  127 LEU   A CB  
2539 C CG  A LEU   A 127 ? 0.1242 0.1324 0.1230 0.0109  -0.0058 0.0172  127 LEU   A CG  
2540 C CG  B LEU   A 127 ? 0.1011 0.1263 0.1093 0.0076  -0.0129 0.0094  127 LEU   A CG  
2541 C CD1 A LEU   A 127 ? 0.1283 0.1341 0.1310 0.0072  -0.0080 0.0202  127 LEU   A CD1 
2542 C CD1 B LEU   A 127 ? 0.1021 0.1259 0.1154 0.0111  -0.0081 0.0081  127 LEU   A CD1 
2543 C CD2 A LEU   A 127 ? 0.1369 0.1348 0.1391 0.0152  -0.0170 0.0121  127 LEU   A CD2 
2544 C CD2 B LEU   A 127 ? 0.1062 0.1304 0.1093 0.0107  -0.0202 0.0001  127 LEU   A CD2 
2567 N N   A SER   A 128 ? 0.1194 0.1171 0.1093 -0.0046 -0.0052 0.0129  128 SER   A N   
2568 N N   B SER   A 128 ? 0.0970 0.1151 0.1049 -0.0054 -0.0095 0.0091  128 SER   A N   
2569 C CA  A SER   A 128 ? 0.1292 0.1204 0.1086 -0.0050 -0.0031 0.0220  128 SER   A CA  
2570 C CA  B SER   A 128 ? 0.0994 0.1128 0.1053 -0.0044 -0.0175 0.0054  128 SER   A CA  
2571 C C   A SER   A 128 ? 0.1321 0.1225 0.1137 0.0019  -0.0087 0.0195  128 SER   A C   
2572 C C   B SER   A 128 ? 0.1014 0.1066 0.1042 -0.0044 -0.0198 0.0154  128 SER   A C   
2573 O O   A SER   A 128 ? 0.1451 0.1433 0.1288 0.0022  -0.0140 0.0105  128 SER   A O   
2574 O O   B SER   A 128 ? 0.0975 0.1029 0.1118 -0.0010 -0.0265 0.0183  128 SER   A O   
2575 C CB  A SER   A 128 ? 0.1269 0.1291 0.1092 -0.0038 -0.0003 0.0175  128 SER   A CB  
2576 C CB  B SER   A 128 ? 0.0991 0.1166 0.1022 -0.0044 -0.0208 -0.0045 128 SER   A CB  
2577 O OG  A SER   A 128 ? 0.1348 0.1386 0.1204 0.0001  0.0049  0.0181  128 SER   A OG  
2578 O OG  B SER   A 128 ? 0.0984 0.1220 0.1075 -0.0053 -0.0196 -0.0077 128 SER   A OG  
2589 N N   A ALA   A 129 ? 0.1220 0.1288 0.1338 -0.0010 -0.0003 0.0256  129 ALA   A N   
2590 N N   B ALA   A 129 ? 0.1066 0.1112 0.1142 -0.0047 -0.0165 0.0174  129 ALA   A N   
2591 C CA  A ALA   A 129 ? 0.1229 0.1319 0.1395 0.0014  -0.0014 0.0225  129 ALA   A CA  
2592 C CA  B ALA   A 129 ? 0.1144 0.1141 0.1173 -0.0030 -0.0113 0.0150  129 ALA   A CA  
2593 C C   A ALA   A 129 ? 0.1277 0.1261 0.1224 -0.0039 -0.0073 0.0190  129 ALA   A C   
2594 C C   B ALA   A 129 ? 0.1214 0.1157 0.1195 -0.0001 -0.0109 0.0101  129 ALA   A C   
2595 O O   A ALA   A 129 ? 0.1324 0.1289 0.1199 -0.0084 -0.0087 0.0202  129 ALA   A O   
2596 O O   B ALA   A 129 ? 0.1225 0.1188 0.1216 -0.0030 -0.0089 0.0120  129 ALA   A O   
2597 C CB  A ALA   A 129 ? 0.1245 0.1517 0.1654 0.0118  0.0066  0.0360  129 ALA   A CB  
2598 C CB  B ALA   A 129 ? 0.1131 0.1196 0.1116 -0.0037 -0.0107 0.0132  129 ALA   A CB  
2609 N N   A GLY   A 130 ? 0.1303 0.1277 0.1605 0.0020  0.0121  0.0034  130 GLY   A N   
2610 N N   B GLY   A 130 ? 0.1265 0.1174 0.1243 0.0057  -0.0124 0.0057  130 GLY   A N   
2611 C CA  A GLY   A 130 ? 0.1444 0.1301 0.1742 0.0035  0.0149  -0.0001 130 GLY   A CA  
2612 C CA  B GLY   A 130 ? 0.1317 0.1203 0.1251 0.0064  -0.0111 0.0049  130 GLY   A CA  
2613 C C   A GLY   A 130 ? 0.1452 0.1224 0.1567 0.0105  0.0013  -0.0001 130 GLY   A C   
2614 C C   B GLY   A 130 ? 0.1362 0.1217 0.1246 0.0056  -0.0186 0.0064  130 GLY   A C   
2615 O O   A GLY   A 130 ? 0.1551 0.1214 0.1592 0.0047  -0.0183 -0.0018 130 GLY   A O   
2616 O O   B GLY   A 130 ? 0.1418 0.1222 0.1217 0.0044  -0.0244 0.0077  130 GLY   A O   
2623 N N   A ILE   A 131 ? 0.1516 0.1235 0.1364 -0.0005 -0.0033 0.0087  131 ILE   A N   
2624 N N   B ILE   A 131 ? 0.1383 0.1238 0.1258 0.0021  -0.0184 0.0093  131 ILE   A N   
2625 C CA  A ILE   A 131 ? 0.1617 0.1233 0.1250 -0.0070 -0.0136 0.0041  131 ILE   A CA  
2626 C CA  B ILE   A 131 ? 0.1408 0.1242 0.1285 0.0004  -0.0220 0.0109  131 ILE   A CA  
2627 C C   A ILE   A 131 ? 0.1551 0.1252 0.1164 -0.0114 -0.0209 0.0144  131 ILE   A C   
2628 C C   B ILE   A 131 ? 0.1374 0.1245 0.1282 -0.0018 -0.0196 0.0163  131 ILE   A C   
2629 O O   A ILE   A 131 ? 0.1677 0.1306 0.1390 -0.0040 -0.0157 0.0179  131 ILE   A O   
2630 O O   B ILE   A 131 ? 0.1409 0.1248 0.1349 -0.0002 -0.0183 0.0173  131 ILE   A O   
2631 C CB  A ILE   A 131 ? 0.1793 0.1296 0.1349 -0.0184 -0.0192 -0.0061 131 ILE   A CB  
2632 C CB  B ILE   A 131 ? 0.1474 0.1265 0.1347 -0.0010 -0.0269 0.0038  131 ILE   A CB  
2633 C CG1 A ILE   A 131 ? 0.1943 0.1575 0.1360 -0.0248 -0.0222 -0.0040 131 ILE   A CG1 
2634 C CG1 B ILE   A 131 ? 0.1515 0.1311 0.1349 -0.0011 -0.0306 0.0050  131 ILE   A CG1 
2635 C CG2 A ILE   A 131 ? 0.1930 0.1220 0.1620 -0.0102 -0.0137 -0.0159 131 ILE   A CG2 
2636 C CG2 B ILE   A 131 ? 0.1491 0.1264 0.1369 -0.0027 -0.0237 -0.0028 131 ILE   A CG2 
2637 C CD1 A ILE   A 131 ? 0.2034 0.1753 0.1735 -0.0272 -0.0261 -0.0108 131 ILE   A CD1 
2638 C CD1 B ILE   A 131 ? 0.1545 0.1333 0.1393 -0.0012 -0.0303 0.0024  131 ILE   A CD1 
2661 N N   A PHE   A 132 ? 0.1452 0.1233 0.1108 0.0002  -0.0142 0.0120  132 PHE   A N   
2662 N N   B PHE   A 132 ? 0.1336 0.1250 0.1235 -0.0015 -0.0159 0.0157  132 PHE   A N   
2663 C CA  A PHE   A 132 ? 0.1492 0.1321 0.1063 0.0000  -0.0022 0.0125  132 PHE   A CA  
2664 C CA  B PHE   A 132 ? 0.1334 0.1268 0.1243 -0.0058 -0.0155 0.0143  132 PHE   A CA  
2665 C C   A PHE   A 132 ? 0.1551 0.1522 0.0999 0.0041  0.0045  0.0135  132 PHE   A C   
2666 C C   B PHE   A 132 ? 0.1353 0.1315 0.1344 -0.0082 -0.0174 0.0154  132 PHE   A C   
2667 O O   A PHE   A 132 ? 0.1623 0.1668 0.1111 -0.0000 0.0029  0.0137  132 PHE   A O   
2668 O O   B PHE   A 132 ? 0.1389 0.1382 0.1340 -0.0121 -0.0204 0.0234  132 PHE   A O   
2669 C CB  A PHE   A 132 ? 0.1503 0.1245 0.1093 -0.0001 -0.0058 0.0161  132 PHE   A CB  
2670 C CB  B PHE   A 132 ? 0.1319 0.1259 0.1163 -0.0080 -0.0127 0.0148  132 PHE   A CB  
2671 C CG  A PHE   A 132 ? 0.1511 0.1247 0.1005 0.0031  -0.0110 0.0134  132 PHE   A CG  
2672 C CG  B PHE   A 132 ? 0.1335 0.1276 0.1200 -0.0080 -0.0141 0.0061  132 PHE   A CG  
2673 C CD1 A PHE   A 132 ? 0.1568 0.1353 0.1251 0.0101  -0.0098 0.0042  132 PHE   A CD1 
2674 C CD1 B PHE   A 132 ? 0.1357 0.1315 0.1239 -0.0063 -0.0143 -0.0003 132 PHE   A CD1 
2675 C CD2 A PHE   A 132 ? 0.1544 0.1361 0.1222 0.0104  -0.0055 -0.0016 132 PHE   A CD2 
2676 C CD2 B PHE   A 132 ? 0.1339 0.1308 0.1322 -0.0065 -0.0161 -0.0016 132 PHE   A CD2 
2677 C CE1 A PHE   A 132 ? 0.1585 0.1363 0.1192 0.0109  -0.0183 -0.0064 132 PHE   A CE1 
2678 C CE1 B PHE   A 132 ? 0.1369 0.1341 0.1313 -0.0073 -0.0142 -0.0061 132 PHE   A CE1 
2679 C CE2 A PHE   A 132 ? 0.1531 0.1431 0.1260 0.0170  -0.0130 -0.0017 132 PHE   A CE2 
2680 C CE2 B PHE   A 132 ? 0.1341 0.1348 0.1390 -0.0058 -0.0157 -0.0051 132 PHE   A CE2 
2681 C CZ  A PHE   A 132 ? 0.1520 0.1375 0.1306 0.0072  -0.0214 0.0050  132 PHE   A CZ  
2682 C CZ  B PHE   A 132 ? 0.1352 0.1357 0.1365 -0.0080 -0.0151 -0.0067 132 PHE   A CZ  
2701 N N   A GLY   A 133 ? 0.1603 0.1509 0.1025 0.0037  -0.0216 0.0121  133 GLY   A N   
2702 N N   B GLY   A 133 ? 0.1333 0.1285 0.1350 -0.0085 -0.0160 0.0103  133 GLY   A N   
2703 C CA  A GLY   A 133 ? 0.1706 0.1611 0.1171 0.0001  -0.0332 0.0026  133 GLY   A CA  
2704 C CA  B GLY   A 133 ? 0.1311 0.1275 0.1372 -0.0074 -0.0118 0.0071  133 GLY   A CA  
2705 C C   A GLY   A 133 ? 0.1736 0.1724 0.1146 -0.0038 -0.0378 -0.0006 133 GLY   A C   
2706 C C   B GLY   A 133 ? 0.1273 0.1281 0.1370 -0.0066 -0.0056 0.0025  133 GLY   A C   
2707 O O   A GLY   A 133 ? 0.1943 0.1902 0.1362 -0.0078 -0.0480 -0.0075 133 GLY   A O   
2708 O O   B GLY   A 133 ? 0.1288 0.1344 0.1454 -0.0086 -0.0036 0.0007  133 GLY   A O   
2715 N N   A ALA   A 134 ? 0.1666 0.1610 0.1119 -0.0117 -0.0310 -0.0010 134 ALA   A N   
2716 N N   B ALA   A 134 ? 0.1256 0.1203 0.1347 -0.0071 -0.0035 0.0002  134 ALA   A N   
2717 C CA  A ALA   A 134 ? 0.1622 0.1645 0.1471 -0.0104 -0.0298 -0.0024 134 ALA   A CA  
2718 C CA  B ALA   A 134 ? 0.1233 0.1157 0.1365 -0.0060 -0.0042 -0.0058 134 ALA   A CA  
2719 C C   A ALA   A 134 ? 0.1665 0.1713 0.1410 -0.0091 -0.0282 0.0144  134 ALA   A C   
2720 C C   B ALA   A 134 ? 0.1239 0.1157 0.1242 -0.0037 -0.0068 -0.0125 134 ALA   A C   
2721 O O   A ALA   A 134 ? 0.1759 0.1786 0.1620 -0.0041 -0.0028 0.0165  134 ALA   A O   
2722 O O   B ALA   A 134 ? 0.1204 0.1169 0.1196 -0.0042 0.0014  -0.0189 134 ALA   A O   
2723 C CB  A ALA   A 134 ? 0.1696 0.1623 0.1924 -0.0083 -0.0277 -0.0066 134 ALA   A CB  
2724 C CB  B ALA   A 134 ? 0.1241 0.1131 0.1503 -0.0063 -0.0036 -0.0050 134 ALA   A CB  
2735 N N   A ASP   A 135 ? 0.1736 0.1778 0.1656 -0.0202 -0.0331 0.0231  135 ASP   A N   
2736 N N   B ASP   A 135 ? 0.1309 0.1170 0.1241 -0.0059 -0.0152 -0.0090 135 ASP   A N   
2737 C CA  A ASP   A 135 ? 0.1715 0.1871 0.1966 -0.0240 -0.0471 0.0369  135 ASP   A CA  
2738 C CA  B ASP   A 135 ? 0.1322 0.1186 0.1227 -0.0071 -0.0212 -0.0003 135 ASP   A CA  
2739 C C   A ASP   A 135 ? 0.1573 0.1777 0.1969 -0.0182 -0.0348 0.0480  135 ASP   A C   
2740 C C   B ASP   A 135 ? 0.1270 0.1147 0.1220 -0.0041 -0.0151 -0.0001 135 ASP   A C   
2741 O O   A ASP   A 135 ? 0.1573 0.1684 0.1989 -0.0198 -0.0348 0.0448  135 ASP   A O   
2742 O O   B ASP   A 135 ? 0.1261 0.1118 0.1232 -0.0063 -0.0147 0.0024  135 ASP   A O   
2743 C CB  A ASP   A 135 ? 0.1936 0.2140 0.2375 -0.0422 -0.0681 0.0229  135 ASP   A CB  
2744 C CB  B ASP   A 135 ? 0.1358 0.1233 0.1142 -0.0092 -0.0324 -0.0011 135 ASP   A CB  
2745 C CG  A ASP   A 135 ? 0.2121 0.2436 0.2861 -0.0553 -0.0783 0.0144  135 ASP   A CG  
2746 C CG  B ASP   A 135 ? 0.1375 0.1280 0.1152 -0.0082 -0.0411 -0.0035 135 ASP   A CG  
2747 O OD1 A ASP   A 135 ? 0.2090 0.2547 0.2969 -0.0527 -0.0800 0.0373  135 ASP   A OD1 
2748 O OD1 B ASP   A 135 ? 0.1376 0.1264 0.1213 -0.0083 -0.0415 -0.0044 135 ASP   A OD1 
2749 O OD2 A ASP   A 135 ? 0.2416 0.2629 0.3338 -0.0589 -0.0589 0.0087  135 ASP   A OD2 
2750 O OD2 B ASP   A 135 ? 0.1376 0.1335 0.1150 -0.0081 -0.0499 -0.0087 135 ASP   A OD2 
2759 N N   A PRO   A 136 ? 0.1472 0.1822 0.2089 -0.0026 -0.0178 0.0632  136 PRO   A N   
2760 N N   B PRO   A 136 ? 0.1246 0.1149 0.1217 0.0023  -0.0072 -0.0006 136 PRO   A N   
2761 C CA  A PRO   A 136 ? 0.1404 0.1852 0.2103 -0.0047 -0.0082 0.0575  136 PRO   A CA  
2762 C CA  B PRO   A 136 ? 0.1258 0.1226 0.1213 0.0009  -0.0044 -0.0030 136 PRO   A CA  
2763 C C   A PRO   A 136 ? 0.1173 0.1783 0.2039 -0.0050 -0.0053 0.0512  136 PRO   A C   
2764 C C   B PRO   A 136 ? 0.1267 0.1304 0.1196 -0.0016 -0.0057 -0.0043 136 PRO   A C   
2765 O O   A PRO   A 136 ? 0.1146 0.1707 0.1968 -0.0061 -0.0016 0.0469  136 PRO   A O   
2766 O O   B PRO   A 136 ? 0.1265 0.1277 0.1041 0.0017  0.0011  -0.0078 136 PRO   A O   
2767 C CB  A PRO   A 136 ? 0.1595 0.1889 0.2331 0.0014  -0.0015 0.0618  136 PRO   A CB  
2768 C CB  B PRO   A 136 ? 0.1279 0.1203 0.1270 0.0035  -0.0057 -0.0050 136 PRO   A CB  
2769 C CG  A PRO   A 136 ? 0.1746 0.1997 0.2604 0.0061  -0.0022 0.0560  136 PRO   A CG  
2770 C CG  B PRO   A 136 ? 0.1314 0.1185 0.1349 0.0056  -0.0030 -0.0057 136 PRO   A CG  
2771 C CD  A PRO   A 136 ? 0.1608 0.1891 0.2352 0.0087  -0.0035 0.0720  136 PRO   A CD  
2772 C CD  B PRO   A 136 ? 0.1265 0.1133 0.1258 0.0050  -0.0030 0.0025  136 PRO   A CD  
2787 N N   A ILE   A 137 ? 0.1196 0.1803 0.2155 -0.0046 -0.0201 0.0540  137 ILE   A N   
2788 N N   B ILE   A 137 ? 0.1327 0.1390 0.1407 -0.0055 -0.0120 -0.0014 137 ILE   A N   
2789 C CA  A ILE   A 137 ? 0.1230 0.1888 0.2286 -0.0187 -0.0353 0.0511  137 ILE   A CA  
2790 C CA  B ILE   A 137 ? 0.1378 0.1482 0.1551 -0.0085 -0.0146 0.0000  137 ILE   A CA  
2791 C C   A ILE   A 137 ? 0.1225 0.1828 0.2011 -0.0218 -0.0359 0.0494  137 ILE   A C   
2792 C C   B ILE   A 137 ? 0.1393 0.1545 0.1529 -0.0102 -0.0117 0.0073  137 ILE   A C   
2793 O O   A ILE   A 137 ? 0.1302 0.1811 0.2001 -0.0242 -0.0203 0.0458  137 ILE   A O   
2794 O O   B ILE   A 137 ? 0.1404 0.1565 0.1522 -0.0106 -0.0077 0.0079  137 ILE   A O   
2795 C CB  A ILE   A 137 ? 0.1279 0.2096 0.2587 -0.0200 -0.0489 0.0482  137 ILE   A CB  
2796 C CB  B ILE   A 137 ? 0.1412 0.1507 0.1704 -0.0079 -0.0183 -0.0036 137 ILE   A CB  
2797 C CG1 A ILE   A 137 ? 0.1404 0.2325 0.3036 -0.0121 -0.0509 0.0416  137 ILE   A CG1 
2798 C CG1 B ILE   A 137 ? 0.1432 0.1517 0.1835 -0.0091 -0.0214 -0.0064 137 ILE   A CG1 
2799 C CG2 A ILE   A 137 ? 0.1395 0.2118 0.2649 -0.0296 -0.0495 0.0481  137 ILE   A CG2 
2800 C CG2 B ILE   A 137 ? 0.1447 0.1530 0.1765 -0.0073 -0.0195 -0.0036 137 ILE   A CG2 
2801 C CD1 A ILE   A 137 ? 0.1556 0.2462 0.3291 -0.0073 -0.0486 0.0410  137 ILE   A CD1 
2802 C CD1 B ILE   A 137 ? 0.1440 0.1508 0.1897 -0.0116 -0.0277 -0.0093 137 ILE   A CD1 
2825 N N   A HIS   A 138 ? 0.1268 0.1884 0.1916 -0.0201 -0.0274 0.0439  138 HIS   A N   
2826 N N   B HIS   A 138 ? 0.1403 0.1603 0.1572 -0.0104 -0.0090 0.0118  138 HIS   A N   
2827 C CA  A HIS   A 138 ? 0.1312 0.1903 0.1691 -0.0195 -0.0252 0.0338  138 HIS   A CA  
2828 C CA  B HIS   A 138 ? 0.1401 0.1630 0.1582 -0.0102 -0.0080 0.0159  138 HIS   A CA  
2829 C C   A HIS   A 138 ? 0.1230 0.1773 0.1507 -0.0125 -0.0144 0.0377  138 HIS   A C   
2830 C C   B HIS   A 138 ? 0.1312 0.1628 0.1535 -0.0104 -0.0087 0.0274  138 HIS   A C   
2831 O O   A HIS   A 138 ? 0.1337 0.1756 0.1588 -0.0122 -0.0130 0.0239  138 HIS   A O   
2832 O O   B HIS   A 138 ? 0.1346 0.1628 0.1547 -0.0105 -0.0073 0.0239  138 HIS   A O   
2833 C CB  A HIS   A 138 ? 0.1489 0.2028 0.1621 -0.0210 -0.0294 0.0215  138 HIS   A CB  
2834 C CB  B HIS   A 138 ? 0.1462 0.1653 0.1619 -0.0071 -0.0049 0.0068  138 HIS   A CB  
2835 C CG  A HIS   A 138 ? 0.1689 0.2128 0.1588 -0.0202 -0.0267 0.0088  138 HIS   A CG  
2836 C CG  B HIS   A 138 ? 0.1529 0.1676 0.1669 -0.0051 -0.0033 -0.0017 138 HIS   A CG  
2837 N ND1 A HIS   A 138 ? 0.1831 0.2282 0.1903 -0.0251 -0.0270 -0.0028 138 HIS   A ND1 
2838 N ND1 B HIS   A 138 ? 0.1569 0.1709 0.1755 -0.0045 -0.0044 -0.0059 138 HIS   A ND1 
2839 C CD2 A HIS   A 138 ? 0.1720 0.2164 0.1578 -0.0113 -0.0202 0.0112  138 HIS   A CD2 
2840 C CD2 B HIS   A 138 ? 0.1550 0.1679 0.1691 -0.0030 0.0000  -0.0045 138 HIS   A CD2 
2841 C CE1 A HIS   A 138 ? 0.1880 0.2335 0.1833 -0.0143 -0.0259 -0.0059 138 HIS   A CE1 
2842 C CE1 B HIS   A 138 ? 0.1579 0.1715 0.1746 -0.0016 -0.0033 -0.0078 138 HIS   A CE1 
2843 N NE2 A HIS   A 138 ? 0.1825 0.2298 0.1612 -0.0091 -0.0184 0.0002  138 HIS   A NE2 
2844 N NE2 B HIS   A 138 ? 0.1577 0.1707 0.1704 -0.0014 -0.0003 -0.0078 138 HIS   A NE2 
2859 N N   . SER   A 139 ? 0.1221 0.1617 0.1535 -0.0109 -0.0138 0.0393  139 SER   A N   
2860 C CA  . SER   A 139 ? 0.1154 0.1493 0.1510 -0.0115 -0.0111 0.0410  139 SER   A CA  
2861 C C   . SER   A 139 ? 0.1135 0.1401 0.1496 -0.0084 0.0012  0.0243  139 SER   A C   
2862 O O   . SER   A 139 ? 0.1077 0.1373 0.1610 -0.0098 -0.0011 0.0338  139 SER   A O   
2863 C CB  . SER   A 139 ? 0.1168 0.1503 0.1600 -0.0177 -0.0129 0.0418  139 SER   A CB  
2864 O OG  . SER   A 139 ? 0.1219 0.1475 0.1629 -0.0184 -0.0147 0.0463  139 SER   A OG  
2871 N N   . LEU   A 140 ? 0.1084 0.1458 0.1534 -0.0079 -0.0007 0.0368  140 LEU   A N   
2872 C CA  . LEU   A 140 ? 0.1030 0.1445 0.1584 -0.0074 -0.0004 0.0407  140 LEU   A CA  
2873 C C   . LEU   A 140 ? 0.1021 0.1455 0.1548 -0.0138 -0.0067 0.0343  140 LEU   A C   
2874 O O   . LEU   A 140 ? 0.1120 0.1476 0.1670 -0.0046 -0.0084 0.0316  140 LEU   A O   
2875 C CB  . LEU   A 140 ? 0.1064 0.1540 0.1669 -0.0076 -0.0019 0.0400  140 LEU   A CB  
2876 C CG  . LEU   A 140 ? 0.1107 0.1674 0.1683 -0.0178 0.0041  0.0480  140 LEU   A CG  
2877 C CD1 . LEU   A 140 ? 0.1174 0.1704 0.1582 -0.0132 0.0026  0.0471  140 LEU   A CD1 
2878 C CD2 . LEU   A 140 ? 0.1149 0.1859 0.1898 -0.0162 0.0094  0.0575  140 LEU   A CD2 
2890 N N   . ARG   A 141 ? 0.1097 0.1513 0.1677 -0.0138 -0.0051 0.0334  141 ARG   A N   
2891 C CA  . ARG   A 141 ? 0.1200 0.1640 0.1791 -0.0235 -0.0128 0.0115  141 ARG   A CA  
2892 C C   . ARG   A 141 ? 0.1214 0.1472 0.1574 -0.0180 -0.0134 0.0195  141 ARG   A C   
2893 O O   . ARG   A 141 ? 0.1215 0.1449 0.1642 -0.0175 -0.0023 0.0134  141 ARG   A O   
2894 C CB  . ARG   A 141 ? 0.1355 0.1859 0.2182 -0.0269 -0.0251 -0.0069 141 ARG   A CB  
2895 C CG  . ARG   A 141 ? 0.1699 0.2195 0.2620 -0.0215 -0.0194 -0.0206 141 ARG   A CG  
2896 C CD  . ARG   A 141 ? 0.1940 0.2372 0.2915 -0.0292 -0.0119 -0.0244 141 ARG   A CD  
2897 N NE  . ARG   A 141 ? 0.1884 0.2523 0.3045 -0.0348 -0.0238 -0.0215 141 ARG   A NE  
2898 C CZ  . ARG   A 141 ? 0.1892 0.2663 0.3174 -0.0482 -0.0115 -0.0108 141 ARG   A CZ  
2899 N NH1 . ARG   A 141 ? 0.1868 0.2735 0.3225 -0.0541 0.0024  -0.0215 141 ARG   A NH1 
2900 N NH2 . ARG   A 141 ? 0.1910 0.2740 0.3255 -0.0445 -0.0178 0.0046  141 ARG   A NH2 
2914 N N   . VAL   A 142 ? 0.1133 0.1446 0.1547 -0.0121 -0.0112 0.0129  142 VAL   A N   
2915 C CA  . VAL   A 142 ? 0.1215 0.1398 0.1508 -0.0133 0.0028  0.0141  142 VAL   A CA  
2916 C C   . VAL   A 142 ? 0.1067 0.1324 0.1427 -0.0158 0.0051  0.0132  142 VAL   A C   
2917 O O   . VAL   A 142 ? 0.1117 0.1390 0.1484 0.0001  0.0047  0.0115  142 VAL   A O   
2918 C CB  . VAL   A 142 ? 0.1292 0.1498 0.1438 -0.0115 0.0056  0.0171  142 VAL   A CB  
2919 C CG1 . VAL   A 142 ? 0.1273 0.1444 0.1412 -0.0120 0.0091  0.0138  142 VAL   A CG1 
2920 C CG2 . VAL   A 142 ? 0.1443 0.1650 0.1590 -0.0054 -0.0013 0.0193  142 VAL   A CG2 
2930 N N   . CYS   A 143 ? 0.1074 0.1350 0.1468 -0.0125 0.0017  0.0176  143 CYS   A N   
2931 C CA  . CYS   A 143 ? 0.1086 0.1299 0.1535 -0.0134 0.0042  0.0176  143 CYS   A CA  
2932 C C   . CYS   A 143 ? 0.1066 0.1248 0.1436 -0.0077 0.0008  0.0175  143 CYS   A C   
2933 O O   . CYS   A 143 ? 0.1093 0.1276 0.1489 -0.0054 0.0045  0.0222  143 CYS   A O   
2934 C CB  . CYS   A 143 ? 0.1170 0.1316 0.1502 -0.0044 0.0105  0.0191  143 CYS   A CB  
2935 S SG  . CYS   A 143 ? 0.1343 0.1389 0.1459 0.0034  0.0100  0.0132  143 CYS   A SG  
2941 N N   . VAL   A 144 ? 0.1077 0.1318 0.1589 -0.0066 0.0031  0.0271  144 VAL   A N   
2942 C CA  . VAL   A 144 ? 0.1107 0.1370 0.1962 -0.0127 0.0123  0.0265  144 VAL   A CA  
2943 C C   . VAL   A 144 ? 0.1144 0.1283 0.1824 -0.0186 -0.0058 0.0175  144 VAL   A C   
2944 O O   . VAL   A 144 ? 0.1294 0.1363 0.1856 -0.0048 -0.0069 0.0227  144 VAL   A O   
2945 C CB  . VAL   A 144 ? 0.1394 0.1603 0.2608 -0.0042 0.0274  0.0290  144 VAL   A CB  
2946 C CG1 . VAL   A 144 ? 0.1500 0.1791 0.2894 -0.0103 0.0108  0.0327  144 VAL   A CG1 
2947 C CG2 . VAL   A 144 ? 0.1249 0.1652 0.2660 -0.0036 0.0348  0.0425  144 VAL   A CG2 
2957 N N   . ASP   A 145 ? 0.1200 0.1332 0.1803 -0.0137 0.0000  0.0098  145 ASP   A N   
2958 C CA  . ASP   A 145 ? 0.1329 0.1331 0.1870 -0.0208 -0.0069 0.0041  145 ASP   A CA  
2959 C C   . ASP   A 145 ? 0.1332 0.1283 0.1822 -0.0127 0.0003  -0.0065 145 ASP   A C   
2960 O O   . ASP   A 145 ? 0.1512 0.1463 0.2447 -0.0156 -0.0023 -0.0394 145 ASP   A O   
2961 C CB  . ASP   A 145 ? 0.1483 0.1581 0.2025 -0.0241 -0.0185 0.0037  145 ASP   A CB  
2962 C CG  . ASP   A 145 ? 0.1648 0.1891 0.2250 -0.0413 -0.0308 0.0105  145 ASP   A CG  
2963 O OD1 . ASP   A 145 ? 0.1568 0.2011 0.2441 -0.0497 -0.0197 0.0105  145 ASP   A OD1 
2964 O OD2 . ASP   A 145 ? 0.1841 0.2155 0.2338 -0.0477 -0.0430 0.0141  145 ASP   A OD2 
2969 N N   . THR   A 146 ? 0.1192 0.1209 0.1531 -0.0109 0.0032  0.0037  146 THR   A N   
2970 C CA  . THR   A 146 ? 0.1113 0.1195 0.1409 -0.0027 0.0002  -0.0005 146 THR   A CA  
2971 C C   . THR   A 146 ? 0.1078 0.1154 0.1421 0.0009  0.0062  0.0098  146 THR   A C   
2972 O O   . THR   A 146 ? 0.1234 0.1266 0.1556 0.0034  0.0048  0.0061  146 THR   A O   
2973 C CB  . THR   A 146 ? 0.1134 0.1259 0.1315 -0.0054 0.0031  0.0084  146 THR   A CB  
2974 O OG1 . THR   A 146 ? 0.1139 0.1398 0.1453 -0.0024 0.0002  0.0057  146 THR   A OG1 
2975 C CG2 . THR   A 146 ? 0.1186 0.1301 0.1531 -0.0074 0.0094  0.0084  146 THR   A CG2 
2983 N N   . VAL   A 147 ? 0.1033 0.1172 0.1433 -0.0013 0.0052  0.0135  147 VAL   A N   
2984 C CA  . VAL   A 147 ? 0.1124 0.1207 0.1378 -0.0085 0.0146  0.0107  147 VAL   A CA  
2985 C C   . VAL   A 147 ? 0.1151 0.1161 0.1454 -0.0102 0.0113  0.0151  147 VAL   A C   
2986 O O   . VAL   A 147 ? 0.1154 0.1226 0.1613 -0.0159 0.0065  0.0134  147 VAL   A O   
2987 C CB  . VAL   A 147 ? 0.1208 0.1230 0.1392 -0.0112 0.0164  0.0154  147 VAL   A CB  
2988 C CG1 . VAL   A 147 ? 0.1523 0.1352 0.1368 -0.0106 0.0130  0.0220  147 VAL   A CG1 
2989 C CG2 . VAL   A 147 ? 0.1285 0.1205 0.1367 -0.0139 0.0037  0.0155  147 VAL   A CG2 
2999 N N   . ARG   A 148 ? 0.1161 0.1148 0.1479 -0.0097 0.0115  0.0217  148 ARG   A N   
3000 C CA  . ARG   A 148 ? 0.1188 0.1164 0.1579 -0.0055 0.0065  0.0272  148 ARG   A CA  
3001 C C   . ARG   A 148 ? 0.1295 0.1216 0.1562 -0.0096 0.0132  0.0376  148 ARG   A C   
3002 O O   . ARG   A 148 ? 0.1576 0.1334 0.1654 -0.0191 0.0156  0.0324  148 ARG   A O   
3003 C CB  . ARG   A 148 ? 0.1248 0.1202 0.1722 -0.0091 0.0151  0.0218  148 ARG   A CB  
3004 C CG  . ARG   A 148 ? 0.1438 0.1191 0.1925 -0.0086 0.0272  0.0106  148 ARG   A CG  
3005 C CD  . ARG   A 148 ? 0.1610 0.1194 0.2154 -0.0080 0.0325  0.0262  148 ARG   A CD  
3006 N NE  . ARG   A 148 ? 0.1529 0.1281 0.2052 0.0050  0.0374  0.0309  148 ARG   A NE  
3007 C CZ  . ARG   A 148 ? 0.1487 0.1201 0.1889 0.0040  0.0379  0.0250  148 ARG   A CZ  
3008 N NH1 . ARG   A 148 ? 0.1572 0.1346 0.1879 -0.0062 0.0386  0.0118  148 ARG   A NH1 
3009 N NH2 . ARG   A 148 ? 0.1465 0.1377 0.1888 0.0134  0.0386  0.0326  148 ARG   A NH2 
3023 N N   . THR   A 149 ? 0.1258 0.1247 0.1422 -0.0170 0.0000  0.0249  149 THR   A N   
3024 C CA  . THR   A 149 ? 0.1298 0.1306 0.1401 -0.0103 0.0012  0.0289  149 THR   A CA  
3025 C C   . THR   A 149 ? 0.1264 0.1274 0.1341 -0.0174 0.0044  0.0388  149 THR   A C   
3026 O O   . THR   A 149 ? 0.1252 0.1406 0.1470 -0.0157 0.0047  0.0275  149 THR   A O   
3027 C CB  . THR   A 149 ? 0.1309 0.1462 0.1410 -0.0107 0.0084  0.0226  149 THR   A CB  
3028 O OG1 . THR   A 149 ? 0.1331 0.1376 0.1523 -0.0182 0.0042  0.0157  149 THR   A OG1 
3029 C CG2 . THR   A 149 ? 0.1295 0.1568 0.1637 -0.0030 -0.0011 0.0237  149 THR   A CG2 
3037 N N   . ASN   A 150 ? 0.1279 0.1288 0.1439 -0.0049 -0.0013 0.0320  150 ASN   A N   
3038 C CA  . ASN   A 150 ? 0.1377 0.1361 0.1384 -0.0075 0.0118  0.0276  150 ASN   A CA  
3039 C C   . ASN   A 150 ? 0.1223 0.1293 0.1428 -0.0112 0.0057  0.0298  150 ASN   A C   
3040 O O   . ASN   A 150 ? 0.1332 0.1401 0.1925 -0.0086 -0.0157 0.0228  150 ASN   A O   
3041 C CB  . ASN   A 150 ? 0.1749 0.1631 0.1555 -0.0121 0.0346  0.0395  150 ASN   A CB  
3042 C CG  . ASN   A 150 ? 0.2349 0.2021 0.2451 -0.0094 0.0101  0.0512  150 ASN   A CG  
3043 O OD1 . ASN   A 150 ? 0.2559 0.2154 0.2745 -0.0160 0.0069  0.0671  150 ASN   A OD1 
3044 N ND2 . ASN   A 150 ? 0.2676 0.2235 0.2903 0.0015  -0.0035 0.0562  150 ASN   A ND2 
3051 N N   . VAL   A 151 ? 0.1256 0.1243 0.1333 -0.0113 0.0038  0.0270  151 VAL   A N   
3052 C CA  . VAL   A 151 ? 0.1310 0.1227 0.1339 -0.0139 0.0074  0.0246  151 VAL   A CA  
3053 C C   . VAL   A 151 ? 0.1207 0.1207 0.1444 -0.0221 0.0112  0.0272  151 VAL   A C   
3054 O O   . VAL   A 151 ? 0.1286 0.1263 0.1734 -0.0174 0.0069  0.0228  151 VAL   A O   
3055 C CB  . VAL   A 151 ? 0.1597 0.1398 0.1430 0.0052  0.0154  0.0252  151 VAL   A CB  
3056 C CG1 . VAL   A 151 ? 0.1548 0.1651 0.1706 -0.0048 0.0013  0.0243  151 VAL   A CG1 
3057 C CG2 . VAL   A 151 ? 0.1736 0.1415 0.1510 0.0047  0.0263  0.0224  151 VAL   A CG2 
3067 N N   . TYR   A 152 ? 0.1174 0.1233 0.1371 -0.0165 0.0150  0.0224  152 TYR   A N   
3068 C CA  . TYR   A 152 ? 0.1178 0.1269 0.1360 -0.0158 0.0157  0.0229  152 TYR   A CA  
3069 C C   . TYR   A 152 ? 0.1148 0.1244 0.1294 -0.0149 0.0172  0.0242  152 TYR   A C   
3070 O O   . TYR   A 152 ? 0.1236 0.1226 0.1403 -0.0260 0.0133  0.0243  152 TYR   A O   
3071 C CB  . TYR   A 152 ? 0.1295 0.1246 0.1320 -0.0089 0.0191  0.0149  152 TYR   A CB  
3072 C CG  . TYR   A 152 ? 0.1445 0.1410 0.1270 -0.0131 0.0286  0.0212  152 TYR   A CG  
3073 C CD1 . TYR   A 152 ? 0.1528 0.1626 0.1421 0.0020  0.0229  0.0331  152 TYR   A CD1 
3074 C CD2 . TYR   A 152 ? 0.1495 0.1480 0.1255 -0.0249 0.0207  0.0219  152 TYR   A CD2 
3075 C CE1 . TYR   A 152 ? 0.1737 0.1701 0.1477 0.0034  0.0060  0.0397  152 TYR   A CE1 
3076 C CE2 . TYR   A 152 ? 0.1699 0.1642 0.1299 -0.0284 0.0212  0.0309  152 TYR   A CE2 
3077 C CZ  . TYR   A 152 ? 0.1872 0.1657 0.1357 -0.0161 0.0086  0.0404  152 TYR   A CZ  
3078 O OH  . TYR   A 152 ? 0.2176 0.1899 0.1589 -0.0098 0.0110  0.0546  152 TYR   A OH  
3088 N N   . LEU   A 153 ? 0.1146 0.1241 0.1377 -0.0182 0.0167  0.0320  153 LEU   A N   
3089 C CA  . LEU   A 153 ? 0.1143 0.1197 0.1577 -0.0053 0.0167  0.0318  153 LEU   A CA  
3090 C C   . LEU   A 153 ? 0.1197 0.1297 0.1617 -0.0109 0.0279  0.0333  153 LEU   A C   
3091 O O   . LEU   A 153 ? 0.1246 0.1351 0.1928 -0.0088 0.0364  0.0304  153 LEU   A O   
3092 C CB  . LEU   A 153 ? 0.1080 0.1286 0.1612 -0.0087 0.0084  0.0354  153 LEU   A CB  
3093 C CG  . LEU   A 153 ? 0.1143 0.1376 0.1484 -0.0112 0.0149  0.0274  153 LEU   A CG  
3094 C CD1 . LEU   A 153 ? 0.1252 0.1404 0.1638 -0.0127 0.0030  0.0295  153 LEU   A CD1 
3095 C CD2 . LEU   A 153 ? 0.1274 0.1422 0.1515 -0.0091 0.0243  0.0129  153 LEU   A CD2 
3107 N N   . ALA   A 154 ? 0.1131 0.1269 0.1713 -0.0062 0.0228  0.0368  154 ALA   A N   
3108 C CA  . ALA   A 154 ? 0.1273 0.1332 0.1905 -0.0003 0.0287  0.0321  154 ALA   A CA  
3109 C C   . ALA   A 154 ? 0.1311 0.1289 0.1918 0.0018  0.0221  0.0487  154 ALA   A C   
3110 O O   . ALA   A 154 ? 0.1370 0.1473 0.1938 -0.0003 0.0211  0.0486  154 ALA   A O   
3111 C CB  . ALA   A 154 ? 0.1425 0.1329 0.1973 0.0069  0.0076  0.0231  154 ALA   A CB  
3117 N N   A VAL   A 155 ? 0.1312 0.1339 0.2126 0.0086  0.0219  0.0565  155 VAL   A N   
3118 N N   B VAL   A 155 ? 0.1394 0.1433 0.1811 -0.0015 0.0121  0.0441  155 VAL   A N   
3119 C CA  A VAL   A 155 ? 0.1358 0.1404 0.2384 0.0083  0.0162  0.0692  155 VAL   A CA  
3120 C CA  B VAL   A 155 ? 0.1490 0.1567 0.1734 -0.0049 0.0029  0.0379  155 VAL   A CA  
3121 C C   A VAL   A 155 ? 0.1547 0.1465 0.2892 0.0125  0.0097  0.0803  155 VAL   A C   
3122 C C   B VAL   A 155 ? 0.1626 0.1654 0.1827 -0.0045 -0.0007 0.0331  155 VAL   A C   
3123 O O   A VAL   A 155 ? 0.1528 0.1488 0.2843 0.0209  0.0193  0.0653  155 VAL   A O   
3124 O O   B VAL   A 155 ? 0.1633 0.1676 0.1818 -0.0044 -0.0015 0.0308  155 VAL   A O   
3125 C CB  A VAL   A 155 ? 0.1380 0.1502 0.2237 0.0130  0.0116  0.0622  155 VAL   A CB  
3126 C CB  B VAL   A 155 ? 0.1473 0.1615 0.1657 -0.0080 -0.0024 0.0374  155 VAL   A CB  
3127 C CG1 A VAL   A 155 ? 0.1530 0.1602 0.2386 0.0146  -0.0038 0.0683  155 VAL   A CG1 
3128 C CG1 B VAL   A 155 ? 0.1504 0.1646 0.1632 -0.0070 -0.0032 0.0366  155 VAL   A CG1 
3129 C CG2 A VAL   A 155 ? 0.1558 0.1613 0.2207 0.0252  0.0051  0.0524  155 VAL   A CG2 
3130 C CG2 B VAL   A 155 ? 0.1440 0.1638 0.1669 -0.0103 -0.0035 0.0363  155 VAL   A CG2 
3149 N N   A PHE   A 156 ? 0.1750 0.1539 0.3309 0.0110  0.0030  0.1000  156 PHE   A N   
3150 N N   B PHE   A 156 ? 0.1730 0.1707 0.1915 -0.0018 -0.0038 0.0295  156 PHE   A N   
3151 C CA  A PHE   A 156 ? 0.1905 0.1608 0.3783 0.0190  0.0013  0.0987  156 PHE   A CA  
3152 C CA  B PHE   A 156 ? 0.1821 0.1767 0.2089 0.0011  -0.0067 0.0231  156 PHE   A CA  
3153 C C   A PHE   A 156 ? 0.1830 0.1650 0.3858 0.0291  0.0126  0.1040  156 PHE   A C   
3154 C C   B PHE   A 156 ? 0.1811 0.1786 0.2017 0.0019  -0.0043 0.0190  156 PHE   A C   
3155 O O   A PHE   A 156 ? 0.1959 0.1722 0.4137 0.0319  0.0200  0.0734  156 PHE   A O   
3156 O O   B PHE   A 156 ? 0.1838 0.1788 0.2072 0.0006  -0.0068 0.0127  156 PHE   A O   
3157 C CB  A PHE   A 156 ? 0.2135 0.1636 0.3928 0.0108  -0.0099 0.1145  156 PHE   A CB  
3158 C CB  B PHE   A 156 ? 0.1888 0.1801 0.2307 0.0018  -0.0116 0.0232  156 PHE   A CB  
3159 C CG  A PHE   A 156 ? 0.2459 0.1776 0.4166 0.0204  -0.0225 0.1023  156 PHE   A CG  
3160 C CG  B PHE   A 156 ? 0.1959 0.1816 0.2489 0.0039  -0.0170 0.0202  156 PHE   A CG  
3161 C CD1 A PHE   A 156 ? 0.2602 0.1927 0.4250 0.0258  -0.0185 0.0856  156 PHE   A CD1 
3162 C CD1 B PHE   A 156 ? 0.1974 0.1814 0.2573 0.0049  -0.0208 0.0172  156 PHE   A CD1 
3163 C CD2 A PHE   A 156 ? 0.2636 0.1834 0.4192 0.0244  -0.0262 0.1159  156 PHE   A CD2 
3164 C CD2 B PHE   A 156 ? 0.1977 0.1823 0.2559 0.0033  -0.0178 0.0201  156 PHE   A CD2 
3165 C CE1 A PHE   A 156 ? 0.2757 0.1988 0.4382 0.0245  -0.0141 0.0771  156 PHE   A CE1 
3166 C CE1 B PHE   A 156 ? 0.1969 0.1816 0.2608 0.0051  -0.0235 0.0154  156 PHE   A CE1 
3167 C CE2 A PHE   A 156 ? 0.2794 0.1971 0.4325 0.0300  -0.0234 0.0926  156 PHE   A CE2 
3168 C CE2 B PHE   A 156 ? 0.1990 0.1824 0.2596 0.0031  -0.0192 0.0183  156 PHE   A CE2 
3169 C CZ  A PHE   A 156 ? 0.2794 0.2005 0.4402 0.0329  -0.0190 0.0724  156 PHE   A CZ  
3170 C CZ  B PHE   A 156 ? 0.1977 0.1817 0.2613 0.0033  -0.0220 0.0162  156 PHE   A CZ  
3189 N N   A ASP   A 157 ? 0.1805 0.1725 0.3625 0.0251  0.0145  0.1224  157 ASP   A N   
3190 N N   B ASP   A 157 ? 0.1794 0.1788 0.1900 0.0032  0.0016  0.0179  157 ASP   A N   
3191 C CA  A ASP   A 157 ? 0.1902 0.1925 0.3603 0.0226  0.0093  0.1266  157 ASP   A CA  
3192 C CA  B ASP   A 157 ? 0.1792 0.1813 0.1942 0.0039  0.0092  0.0192  157 ASP   A CA  
3193 C C   A ASP   A 157 ? 0.1782 0.1996 0.3558 0.0294  0.0193  0.1263  157 ASP   A C   
3194 C C   B ASP   A 157 ? 0.1797 0.1879 0.2023 0.0045  0.0146  0.0167  157 ASP   A C   
3195 O O   A ASP   A 157 ? 0.1687 0.1892 0.3284 0.0221  0.0208  0.1348  157 ASP   A O   
3196 O O   B ASP   A 157 ? 0.1810 0.1882 0.1978 0.0049  0.0178  0.0138  157 ASP   A O   
3197 C CB  A ASP   A 157 ? 0.2118 0.2065 0.3724 0.0220  -0.0004 0.1222  157 ASP   A CB  
3198 C CB  B ASP   A 157 ? 0.1779 0.1779 0.1917 0.0042  0.0108  0.0211  157 ASP   A CB  
3199 C CG  A ASP   A 157 ? 0.2438 0.2169 0.4003 0.0278  -0.0183 0.1187  157 ASP   A CG  
3200 C CG  B ASP   A 157 ? 0.1758 0.1763 0.1869 0.0044  0.0128  0.0240  157 ASP   A CG  
3201 O OD1 A ASP   A 157 ? 0.2801 0.2273 0.4356 0.0262  -0.0367 0.1030  157 ASP   A OD1 
3202 O OD1 B ASP   A 157 ? 0.1715 0.1755 0.1782 0.0019  0.0141  0.0369  157 ASP   A OD1 
3203 O OD2 A ASP   A 157 ? 0.2332 0.2175 0.4172 0.0282  -0.0146 0.1198  157 ASP   A OD2 
3204 O OD2 B ASP   A 157 ? 0.1750 0.1722 0.1901 0.0074  0.0116  0.0172  157 ASP   A OD2 
3213 N N   A LYS   A 158 ? 0.1852 0.2168 0.3812 0.0412  0.0291  0.1232  158 LYS   A N   
3214 N N   B LYS   A 158 ? 0.1817 0.1937 0.2171 0.0027  0.0167  0.0206  158 LYS   A N   
3215 C CA  A LYS   A 158 ? 0.1870 0.2411 0.3900 0.0474  0.0454  0.1218  158 LYS   A CA  
3216 C CA  B LYS   A 158 ? 0.1856 0.2005 0.2343 0.0006  0.0145  0.0250  158 LYS   A CA  
3217 C C   A LYS   A 158 ? 0.1709 0.2495 0.3798 0.0520  0.0469  0.1434  158 LYS   A C   
3218 C C   B LYS   A 158 ? 0.1838 0.2008 0.2290 -0.0011 0.0065  0.0291  158 LYS   A C   
3219 O O   A LYS   A 158 ? 0.1664 0.2467 0.3816 0.0462  0.0543  0.1511  158 LYS   A O   
3220 O O   B LYS   A 158 ? 0.1846 0.2023 0.2313 -0.0038 0.0084  0.0309  158 LYS   A O   
3221 C CB  A LYS   A 158 ? 0.2026 0.2555 0.4028 0.0499  0.0666  0.1118  158 LYS   A CB  
3222 C CB  B LYS   A 158 ? 0.1924 0.2066 0.2548 0.0019  0.0189  0.0251  158 LYS   A CB  
3223 C CG  A LYS   A 158 ? 0.2135 0.2724 0.4210 0.0516  0.0865  0.1052  158 LYS   A CG  
3224 C CG  B LYS   A 158 ? 0.1983 0.2117 0.2721 0.0023  0.0218  0.0256  158 LYS   A CG  
3225 C CD  A LYS   A 158 ? 0.2246 0.2900 0.4380 0.0469  0.1049  0.1077  158 LYS   A CD  
3226 C CD  B LYS   A 158 ? 0.2042 0.2166 0.2867 0.0021  0.0240  0.0268  158 LYS   A CD  
3227 C CE  A LYS   A 158 ? 0.2314 0.3033 0.4580 0.0388  0.1187  0.1130  158 LYS   A CE  
3228 C CE  B LYS   A 158 ? 0.2085 0.2208 0.2999 0.0022  0.0251  0.0279  158 LYS   A CE  
3229 N NZ  A LYS   A 158 ? 0.2368 0.3098 0.4686 0.0305  0.1258  0.1189  158 LYS   A NZ  
3230 N NZ  B LYS   A 158 ? 0.2108 0.2229 0.3058 0.0015  0.0251  0.0293  158 LYS   A NZ  
3257 N N   A ASN   A 159 ? 0.1707 0.2697 0.3880 0.0553  0.0271  0.1454  159 ASN   A N   
3258 N N   B ASN   A 159 ? 0.1804 0.1991 0.2181 -0.0004 -0.0037 0.0278  159 ASN   A N   
3259 C CA  A ASN   A 159 ? 0.1716 0.2882 0.3897 0.0548  0.0071  0.1548  159 ASN   A CA  
3260 C CA  B ASN   A 159 ? 0.1778 0.1976 0.2052 -0.0004 -0.0118 0.0275  159 ASN   A CA  
3261 C C   A ASN   A 159 ? 0.1529 0.2863 0.3584 0.0375  0.0115  0.1515  159 ASN   A C   
3262 C C   B ASN   A 159 ? 0.1782 0.1987 0.2023 -0.0008 -0.0039 0.0260  159 ASN   A C   
3263 O O   A ASN   A 159 ? 0.1396 0.2994 0.3525 0.0369  0.0061  0.1377  159 ASN   A O   
3264 O O   B ASN   A 159 ? 0.1777 0.1989 0.2003 -0.0004 -0.0048 0.0219  159 ASN   A O   
3265 C CB  A ASN   A 159 ? 0.1990 0.3071 0.4324 0.0557  0.0046  0.1620  159 ASN   A CB  
3266 C CB  B ASN   A 159 ? 0.1758 0.1958 0.1965 -0.0018 -0.0232 0.0306  159 ASN   A CB  
3267 C CG  A ASN   A 159 ? 0.2283 0.3249 0.4806 0.0472  0.0116  0.1574  159 ASN   A CG  
3268 C CG  B ASN   A 159 ? 0.1729 0.1953 0.1936 -0.0024 -0.0287 0.0342  159 ASN   A CG  
3269 O OD1 A ASN   A 159 ? 0.2389 0.3328 0.4997 0.0412  0.0231  0.1545  159 ASN   A OD1 
3270 O OD1 B ASN   A 159 ? 0.1733 0.1944 0.1908 -0.0027 -0.0347 0.0431  159 ASN   A OD1 
3271 N ND2 A ASN   A 159 ? 0.2427 0.3321 0.5017 0.0428  0.0118  0.1526  159 ASN   A ND2 
3272 N ND2 B ASN   A 159 ? 0.1730 0.1971 0.2008 0.0010  -0.0246 0.0298  159 ASN   A ND2 
3285 N N   A LEU   A 160 ? 0.1428 0.2668 0.3311 0.0261  -0.0012 0.1542  160 LEU   A N   
3286 N N   B LEU   A 160 ? 0.1766 0.1978 0.1994 -0.0008 0.0001  0.0252  160 LEU   A N   
3287 C CA  A LEU   A 160 ? 0.1416 0.2520 0.3127 0.0104  0.0046  0.1407  160 LEU   A CA  
3288 C CA  B LEU   A 160 ? 0.1754 0.1968 0.1941 -0.0025 0.0033  0.0226  160 LEU   A CA  
3289 C C   A LEU   A 160 ? 0.1270 0.2391 0.3002 0.0004  0.0131  0.1281  160 LEU   A C   
3290 C C   B LEU   A 160 ? 0.1727 0.1963 0.1859 -0.0014 0.0045  0.0188  160 LEU   A C   
3291 O O   A LEU   A 160 ? 0.1232 0.2503 0.2995 -0.0065 0.0032  0.1147  160 LEU   A O   
3292 O O   B LEU   A 160 ? 0.1716 0.1981 0.1829 -0.0026 0.0024  0.0168  160 LEU   A O   
3293 C CB  A LEU   A 160 ? 0.1533 0.2542 0.2947 -0.0003 0.0038  0.1383  160 LEU   A CB  
3294 C CB  B LEU   A 160 ? 0.1769 0.1970 0.1965 -0.0051 0.0043  0.0239  160 LEU   A CB  
3295 C CG  A LEU   A 160 ? 0.1608 0.2572 0.2907 -0.0141 0.0180  0.1220  160 LEU   A CG  
3296 C CG  B LEU   A 160 ? 0.1775 0.1966 0.1996 -0.0084 0.0072  0.0216  160 LEU   A CG  
3297 C CD1 A LEU   A 160 ? 0.1715 0.2647 0.2905 -0.0125 0.0213  0.1082  160 LEU   A CD1 
3298 C CD1 B LEU   A 160 ? 0.1793 0.1973 0.1994 -0.0080 0.0074  0.0197  160 LEU   A CD1 
3299 C CD2 A LEU   A 160 ? 0.1617 0.2588 0.2967 -0.0219 0.0236  0.1077  160 LEU   A CD2 
3300 C CD2 B LEU   A 160 ? 0.1767 0.1967 0.2019 -0.0103 0.0086  0.0203  160 LEU   A CD2 
3323 N N   A TYR   A 161 ? 0.1236 0.2138 0.2947 0.0079  0.0207  0.1206  161 TYR   A N   
3324 N N   B TYR   A 161 ? 0.1731 0.1939 0.1832 0.0016  0.0062  0.0139  161 TYR   A N   
3325 C CA  A TYR   A 161 ? 0.1269 0.2010 0.2928 0.0099  0.0232  0.1177  161 TYR   A CA  
3326 C CA  B TYR   A 161 ? 0.1743 0.1941 0.1820 0.0026  0.0083  0.0130  161 TYR   A CA  
3327 C C   A TYR   A 161 ? 0.1214 0.2103 0.2943 0.0112  0.0165  0.1116  161 TYR   A C   
3328 C C   B TYR   A 161 ? 0.1804 0.2008 0.1878 0.0012  0.0090  0.0163  161 TYR   A C   
3329 O O   A TYR   A 161 ? 0.1163 0.2105 0.2807 0.0093  0.0199  0.1085  161 TYR   A O   
3330 O O   B TYR   A 161 ? 0.1791 0.1999 0.1805 -0.0002 0.0109  0.0133  161 TYR   A O   
3331 C CB  A TYR   A 161 ? 0.1425 0.1883 0.3010 0.0104  0.0228  0.1017  161 TYR   A CB  
3332 C CB  B TYR   A 161 ? 0.1718 0.1885 0.1812 0.0048  0.0079  0.0080  161 TYR   A CB  
3333 C CG  A TYR   A 161 ? 0.1386 0.1824 0.2911 0.0087  0.0240  0.0802  161 TYR   A CG  
3334 C CG  B TYR   A 161 ? 0.1681 0.1842 0.1777 0.0060  0.0068  0.0059  161 TYR   A CG  
3335 C CD1 A TYR   A 161 ? 0.1333 0.1771 0.2928 0.0039  0.0171  0.0742  161 TYR   A CD1 
3336 C CD1 B TYR   A 161 ? 0.1661 0.1824 0.1783 0.0058  0.0064  0.0061  161 TYR   A CD1 
3337 C CD2 A TYR   A 161 ? 0.1387 0.1889 0.2781 0.0111  0.0217  0.0689  161 TYR   A CD2 
3338 C CD2 B TYR   A 161 ? 0.1664 0.1833 0.1747 0.0069  0.0063  0.0060  161 TYR   A CD2 
3339 C CE1 A TYR   A 161 ? 0.1431 0.1758 0.2942 0.0045  0.0111  0.0699  161 TYR   A CE1 
3340 C CE1 B TYR   A 161 ? 0.1664 0.1822 0.1791 0.0061  0.0073  0.0085  161 TYR   A CE1 
3341 C CE2 A TYR   A 161 ? 0.1456 0.1824 0.2707 0.0058  0.0171  0.0725  161 TYR   A CE2 
3342 C CE2 B TYR   A 161 ? 0.1670 0.1827 0.1771 0.0066  0.0070  0.0092  161 TYR   A CE2 
3343 C CZ  A TYR   A 161 ? 0.1546 0.1756 0.2826 0.0017  0.0076  0.0790  161 TYR   A CZ  
3344 C CZ  B TYR   A 161 ? 0.1679 0.1834 0.1820 0.0066  0.0072  0.0121  161 TYR   A CZ  
3345 O OH  A TYR   A 161 ? 0.1690 0.1869 0.2931 -0.0063 -0.0023 0.0852  161 TYR   A OH  
3346 O OH  B TYR   A 161 ? 0.1696 0.1872 0.1893 0.0070  0.0045  0.0167  161 TYR   A OH  
3365 N N   A ASP   A 162 ? 0.1194 0.2241 0.3111 0.0091  0.0209  0.1126  162 ASP   A N   
3366 N N   B ASP   A 162 ? 0.1881 0.2086 0.2042 0.0014  0.0080  0.0203  162 ASP   A N   
3367 C CA  A ASP   A 162 ? 0.1177 0.2457 0.3241 0.0038  0.0274  0.1159  162 ASP   A CA  
3368 C CA  B ASP   A 162 ? 0.1955 0.2171 0.2192 0.0000  0.0075  0.0258  162 ASP   A CA  
3369 C C   A ASP   A 162 ? 0.1115 0.2595 0.3149 -0.0045 0.0235  0.1178  162 ASP   A C   
3370 C C   B ASP   A 162 ? 0.1995 0.2247 0.2252 -0.0032 0.0054  0.0272  162 ASP   A C   
3371 O O   A ASP   A 162 ? 0.1191 0.2575 0.3356 -0.0094 0.0274  0.1088  162 ASP   A O   
3372 O O   B ASP   A 162 ? 0.1992 0.2234 0.2242 -0.0054 0.0058  0.0268  162 ASP   A O   
3373 C CB  A ASP   A 162 ? 0.1258 0.2550 0.3482 0.0087  0.0393  0.1085  162 ASP   A CB  
3374 C CB  B ASP   A 162 ? 0.1988 0.2183 0.2284 0.0033  0.0086  0.0276  162 ASP   A CB  
3375 C CG  A ASP   A 162 ? 0.1437 0.2738 0.3758 0.0157  0.0503  0.0932  162 ASP   A CG  
3376 C CG  B ASP   A 162 ? 0.2029 0.2206 0.2402 0.0067  0.0073  0.0272  162 ASP   A CG  
3377 O OD1 A ASP   A 162 ? 0.1618 0.2860 0.3898 0.0043  0.0496  0.0883  162 ASP   A OD1 
3378 O OD1 B ASP   A 162 ? 0.2057 0.2229 0.2456 0.0056  0.0081  0.0257  162 ASP   A OD1 
3379 O OD2 A ASP   A 162 ? 0.1618 0.2844 0.4006 0.0364  0.0493  0.0752  162 ASP   A OD2 
3380 O OD2 B ASP   A 162 ? 0.2063 0.2226 0.2478 0.0110  0.0059  0.0261  162 ASP   A OD2 
3389 N N   A LYS   A 163 ? 0.1278 0.2819 0.3153 -0.0048 0.0047  0.1141  163 LYS   A N   
3390 N N   B LYS   A 163 ? 0.2057 0.2328 0.2347 -0.0039 0.0013  0.0280  163 LYS   A N   
3391 C CA  A LYS   A 163 ? 0.1393 0.2994 0.3036 -0.0062 -0.0095 0.1148  163 LYS   A CA  
3392 C CA  B LYS   A 163 ? 0.2114 0.2396 0.2439 -0.0045 -0.0013 0.0269  163 LYS   A CA  
3393 C C   A LYS   A 163 ? 0.1296 0.2912 0.2865 -0.0106 0.0035  0.1134  163 LYS   A C   
3394 C C   B LYS   A 163 ? 0.2048 0.2340 0.2262 -0.0040 0.0008  0.0270  163 LYS   A C   
3395 O O   A LYS   A 163 ? 0.1247 0.3058 0.3062 -0.0199 0.0058  0.0910  163 LYS   A O   
3396 O O   B LYS   A 163 ? 0.2066 0.2396 0.2286 -0.0067 0.0018  0.0242  163 LYS   A O   
3397 C CB  A LYS   A 163 ? 0.1768 0.3251 0.3320 0.0065  -0.0306 0.1069  163 LYS   A CB  
3398 C CB  B LYS   A 163 ? 0.2246 0.2508 0.2736 -0.0042 -0.0044 0.0237  163 LYS   A CB  
3399 C CG  A LYS   A 163 ? 0.2184 0.3469 0.3767 0.0087  -0.0235 0.0979  163 LYS   A CG  
3400 C CG  B LYS   A 163 ? 0.2363 0.2604 0.3029 -0.0051 -0.0045 0.0198  163 LYS   A CG  
3401 C CD  A LYS   A 163 ? 0.2569 0.3640 0.4220 0.0093  -0.0211 0.0871  163 LYS   A CD  
3402 C CD  B LYS   A 163 ? 0.2450 0.2682 0.3285 -0.0056 -0.0055 0.0151  163 LYS   A CD  
3403 C CE  A LYS   A 163 ? 0.2833 0.3764 0.4574 0.0081  -0.0168 0.0791  163 LYS   A CE  
3404 C CE  B LYS   A 163 ? 0.2504 0.2743 0.3479 -0.0059 -0.0066 0.0110  163 LYS   A CE  
3405 N NZ  A LYS   A 163 ? 0.2887 0.3846 0.4788 0.0075  -0.0155 0.0759  163 LYS   A NZ  
3406 N NZ  B LYS   A 163 ? 0.2529 0.2772 0.3572 -0.0056 -0.0073 0.0093  163 LYS   A NZ  
3433 N N   A LEU   A 164 ? 0.1118 0.2637 0.2643 -0.0178 0.0019  0.1087  164 LEU   A N   
3434 N N   B LEU   A 164 ? 0.1944 0.2208 0.2085 -0.0027 0.0008  0.0262  164 LEU   A N   
3435 C CA  A LEU   A 164 ? 0.1147 0.2411 0.2545 -0.0269 0.0089  0.0962  164 LEU   A CA  
3436 C CA  B LEU   A 164 ? 0.1860 0.2081 0.1937 -0.0009 0.0040  0.0244  164 LEU   A CA  
3437 C C   A LEU   A 164 ? 0.1219 0.2360 0.2499 -0.0237 0.0156  0.0881  164 LEU   A C   
3438 C C   B LEU   A 164 ? 0.1803 0.2005 0.1866 0.0025  0.0078  0.0245  164 LEU   A C   
3439 O O   A LEU   A 164 ? 0.1361 0.2441 0.2373 -0.0334 0.0379  0.0697  164 LEU   A O   
3440 O O   B LEU   A 164 ? 0.1794 0.2006 0.1818 0.0028  0.0109  0.0228  164 LEU   A O   
3441 C CB  A LEU   A 164 ? 0.1166 0.2294 0.2371 -0.0248 0.0126  0.0918  164 LEU   A CB  
3442 C CB  B LEU   A 164 ? 0.1847 0.2035 0.1871 -0.0024 0.0049  0.0222  164 LEU   A CB  
3443 C CG  A LEU   A 164 ? 0.1272 0.2267 0.2379 -0.0214 0.0045  0.0763  164 LEU   A CG  
3444 C CG  B LEU   A 164 ? 0.1846 0.2004 0.1848 -0.0029 0.0056  0.0196  164 LEU   A CG  
3445 C CD1 A LEU   A 164 ? 0.1233 0.2226 0.2414 -0.0134 -0.0013 0.0666  164 LEU   A CD1 
3446 C CD1 B LEU   A 164 ? 0.1833 0.1990 0.1846 -0.0028 0.0059  0.0178  164 LEU   A CD1 
3447 C CD2 A LEU   A 164 ? 0.1430 0.2315 0.2402 -0.0256 0.0220  0.0695  164 LEU   A CD2 
3448 C CD2 B LEU   A 164 ? 0.1864 0.1997 0.1843 -0.0037 0.0086  0.0182  164 LEU   A CD2 
3471 N N   A VAL   A 165 ? 0.1211 0.2249 0.2538 -0.0265 0.0194  0.0864  165 VAL   A N   
3472 N N   B VAL   A 165 ? 0.1762 0.1936 0.1845 0.0045  0.0105  0.0222  165 VAL   A N   
3473 C CA  A VAL   A 165 ? 0.1275 0.2182 0.2470 -0.0244 0.0258  0.0904  165 VAL   A CA  
3474 C CA  B VAL   A 165 ? 0.1727 0.1883 0.1808 0.0058  0.0122  0.0208  165 VAL   A CA  
3475 C C   A VAL   A 165 ? 0.1207 0.2274 0.2399 -0.0162 0.0263  0.0916  165 VAL   A C   
3476 C C   B VAL   A 165 ? 0.1703 0.1902 0.1772 0.0076  0.0085  0.0211  165 VAL   A C   
3477 O O   A VAL   A 165 ? 0.1243 0.2272 0.2323 -0.0164 0.0234  0.0850  165 VAL   A O   
3478 O O   B VAL   A 165 ? 0.1686 0.1875 0.1723 0.0094  0.0073  0.0194  165 VAL   A O   
3479 C CB  A VAL   A 165 ? 0.1515 0.2099 0.2562 -0.0270 0.0262  0.0739  165 VAL   A CB  
3480 C CB  B VAL   A 165 ? 0.1735 0.1822 0.1822 0.0047  0.0143  0.0176  165 VAL   A CB  
3481 C CG1 A VAL   A 165 ? 0.1550 0.2067 0.2614 -0.0240 0.0331  0.0636  165 VAL   A CG1 
3482 C CG1 B VAL   A 165 ? 0.1733 0.1802 0.1825 0.0044  0.0166  0.0164  165 VAL   A CG1 
3483 C CG2 A VAL   A 165 ? 0.1669 0.2113 0.2634 -0.0279 0.0251  0.0710  165 VAL   A CG2 
3484 C CG2 B VAL   A 165 ? 0.1753 0.1815 0.1852 0.0030  0.0143  0.0184  165 VAL   A CG2 
3503 N N   A SER   A 166 ? 0.1096 0.2416 0.2635 -0.0142 0.0264  0.0864  166 SER   A N   
3504 N N   B SER   A 166 ? 0.1708 0.1965 0.1849 0.0048  0.0064  0.0214  166 SER   A N   
3505 C CA  A SER   A 166 ? 0.1090 0.2666 0.2741 -0.0178 0.0233  0.0738  166 SER   A CA  
3506 C CA  B SER   A 166 ? 0.1716 0.2050 0.1920 0.0019  0.0046  0.0186  166 SER   A CA  
3507 C C   A SER   A 166 ? 0.1186 0.2937 0.2600 -0.0191 0.0102  0.0669  166 SER   A C   
3508 C C   B SER   A 166 ? 0.1739 0.2147 0.1999 0.0004  0.0044  0.0153  166 SER   A C   
3509 O O   A SER   A 166 ? 0.1456 0.3107 0.3011 -0.0295 0.0191  0.0354  166 SER   A O   
3510 O O   B SER   A 166 ? 0.1744 0.2167 0.2124 -0.0005 0.0047  0.0101  166 SER   A O   
3511 C CB  A SER   A 166 ? 0.1273 0.2763 0.3093 -0.0092 0.0153  0.0581  166 SER   A CB  
3512 C CB  B SER   A 166 ? 0.1727 0.2051 0.1910 0.0010  0.0035  0.0174  166 SER   A CB  
3513 O OG  A SER   A 166 ? 0.1716 0.2853 0.3423 -0.0140 0.0083  0.0533  166 SER   A OG  
3514 O OG  B SER   A 166 ? 0.1753 0.2051 0.1903 -0.0014 0.0021  0.0173  166 SER   A OG  
3525 N N   A SER   A 167 ? 0.1256 0.3043 0.2255 -0.0042 -0.0050 0.0733  167 SER   A N   
3526 N N   B SER   A 167 ? 0.1785 0.2213 0.1961 0.0003  0.0040  0.0142  167 SER   A N   
3527 C CA  A SER   A 167 ? 0.1498 0.3205 0.2215 0.0018  -0.0113 0.0605  167 SER   A CA  
3528 C CA  B SER   A 167 ? 0.1872 0.2297 0.1957 0.0035  0.0042  0.0118  167 SER   A CA  
3529 C C   A SER   A 167 ? 0.1491 0.3210 0.2031 0.0098  -0.0028 0.0509  167 SER   A C   
3530 C C   B SER   A 167 ? 0.1930 0.2338 0.1966 0.0052  0.0011  0.0092  167 SER   A C   
3531 O O   A SER   A 167 ? 0.1654 0.3283 0.2216 0.0120  -0.0110 0.0485  167 SER   A O   
3532 O O   B SER   A 167 ? 0.1926 0.2351 0.1958 0.0045  0.0004  0.0123  167 SER   A O   
3533 C CB  A SER   A 167 ? 0.1669 0.3322 0.2340 0.0039  -0.0052 0.0688  167 SER   A CB  
3534 C CB  B SER   A 167 ? 0.1892 0.2333 0.1956 0.0050  0.0110  0.0142  167 SER   A CB  
3535 O OG  A SER   A 167 ? 0.1668 0.3373 0.2304 -0.0010 0.0154  0.0773  167 SER   A OG  
3536 O OG  B SER   A 167 ? 0.1890 0.2360 0.1922 0.0052  0.0202  0.0173  167 SER   A OG  
3547 N N   A PHE   A 168 ? 0.1390 0.3118 0.1861 0.0171  0.0037  0.0385  168 PHE   A N   
3548 N N   B PHE   A 168 ? 0.2011 0.2369 0.2015 0.0062  0.0001  0.0033  168 PHE   A N   
3549 C CA  A PHE   A 168 ? 0.1411 0.3033 0.1950 0.0105  0.0151  0.0296  168 PHE   A CA  
3550 C CA  B PHE   A 168 ? 0.2114 0.2390 0.2123 0.0060  0.0012  -0.0016 168 PHE   A CA  
3551 C C   A PHE   A 168 ? 0.1582 0.3268 0.2284 -0.0031 0.0495  0.0008  168 PHE   A C   
3552 C C   B PHE   A 168 ? 0.2243 0.2527 0.2413 0.0052  0.0074  -0.0057 168 PHE   A C   
3553 O O   A PHE   A 168 ? 0.1661 0.3287 0.2731 -0.0168 0.0591  0.0009  168 PHE   A O   
3554 O O   B PHE   A 168 ? 0.2264 0.2549 0.2505 0.0034  0.0116  -0.0054 168 PHE   A O   
3555 C CB  A PHE   A 168 ? 0.1410 0.2752 0.1806 0.0122  -0.0016 0.0324  168 PHE   A CB  
3556 C CB  B PHE   A 168 ? 0.2107 0.2289 0.2000 0.0039  -0.0036 -0.0024 168 PHE   A CB  
3557 C CG  A PHE   A 168 ? 0.1410 0.2530 0.1775 -0.0001 -0.0070 0.0411  168 PHE   A CG  
3558 C CG  B PHE   A 168 ? 0.2091 0.2201 0.1894 0.0020  -0.0064 -0.0027 168 PHE   A CG  
3559 C CD1 A PHE   A 168 ? 0.1449 0.2534 0.1974 -0.0095 -0.0119 0.0572  168 PHE   A CD1 
3560 C CD1 B PHE   A 168 ? 0.2090 0.2182 0.1893 0.0019  -0.0075 -0.0004 168 PHE   A CD1 
3561 C CD2 A PHE   A 168 ? 0.1452 0.2409 0.1734 -0.0045 -0.0007 0.0337  168 PHE   A CD2 
3562 C CD2 B PHE   A 168 ? 0.2077 0.2157 0.1830 0.0016  -0.0068 -0.0039 168 PHE   A CD2 
3563 C CE1 A PHE   A 168 ? 0.1336 0.2516 0.1987 -0.0130 -0.0100 0.0589  168 PHE   A CE1 
3564 C CE1 B PHE   A 168 ? 0.2075 0.2171 0.1870 0.0014  -0.0073 -0.0007 168 PHE   A CE1 
3565 C CE2 A PHE   A 168 ? 0.1473 0.2353 0.1810 -0.0069 0.0046  0.0460  168 PHE   A CE2 
3566 C CE2 B PHE   A 168 ? 0.2075 0.2146 0.1824 0.0014  -0.0069 -0.0035 168 PHE   A CE2 
3567 C CZ  A PHE   A 168 ? 0.1401 0.2421 0.1931 -0.0089 -0.0053 0.0533  168 PHE   A CZ  
3568 C CZ  B PHE   A 168 ? 0.2074 0.2157 0.1851 0.0015  -0.0072 -0.0018 168 PHE   A CZ  
3587 N N   A LEU   A 169 ? 0.1997 0.3504 0.2768 -0.0113 0.0592  -0.0214 169 LEU   A N   
3588 N N   B LEU   A 169 ? 0.2376 0.2651 0.2702 0.0063  0.0093  -0.0091 169 LEU   A N   
3589 C CA  A LEU   A 169 ? 0.2582 0.3771 0.3635 -0.0080 0.0388  -0.0303 169 LEU   A CA  
3590 C CA  B LEU   A 169 ? 0.2537 0.2774 0.3069 0.0079  0.0078  -0.0122 169 LEU   A CA  
3591 C C   A LEU   A 169 ? 0.2643 0.3814 0.4029 -0.0082 0.0394  -0.0194 169 LEU   A C   
3592 C C   B LEU   A 169 ? 0.2598 0.2814 0.3180 0.0091  0.0074  -0.0092 169 LEU   A C   
3593 O O   A LEU   A 169 ? 0.2743 0.3835 0.4181 -0.0061 0.0346  -0.0198 169 LEU   A O   
3594 O O   B LEU   A 169 ? 0.2609 0.2822 0.3226 0.0100  0.0053  -0.0073 169 LEU   A O   
3595 C CB  A LEU   A 169 ? 0.2961 0.3965 0.4024 -0.0078 0.0222  -0.0415 169 LEU   A CB  
3596 C CB  B LEU   A 169 ? 0.2615 0.2841 0.3311 0.0097  0.0064  -0.0168 169 LEU   A CB  
3597 C CG  A LEU   A 169 ? 0.3258 0.4103 0.4318 -0.0102 0.0051  -0.0539 169 LEU   A CG  
3598 C CG  B LEU   A 169 ? 0.2681 0.2897 0.3514 0.0122  0.0065  -0.0193 169 LEU   A CG  
3599 C CD1 A LEU   A 169 ? 0.3367 0.4143 0.4440 -0.0108 -0.0024 -0.0561 169 LEU   A CD1 
3600 C CD1 B LEU   A 169 ? 0.2702 0.2909 0.3590 0.0133  0.0058  -0.0214 169 LEU   A CD1 
3601 C CD2 A LEU   A 169 ? 0.3341 0.4157 0.4386 -0.0125 0.0017  -0.0572 169 LEU   A CD2 
3602 C CD2 B LEU   A 169 ? 0.2700 0.2918 0.3582 0.0130  0.0073  -0.0192 169 LEU   A CD2 
3603 O OXT A LEU   A 169 ? 0.2506 0.3829 0.4090 -0.0093 0.0497  -0.0137 169 LEU   A OXT 
3604 O OXT B LEU   A 169 ? 0.2624 0.2825 0.3221 0.0089  0.0072  -0.0094 169 LEU   A OXT 
3627 N N   A SER   B 1   ? 0.3273 0.3346 0.3430 -0.1212 -0.0773 0.0696  1   SER   B N   
3628 N N   B SER   B 1   ? 0.3359 0.3362 0.3262 -0.0299 -0.0174 0.0131  1   SER   B N   
3629 C CA  A SER   B 1   ? 0.3130 0.3360 0.3379 -0.1258 -0.0859 0.0641  1   SER   B CA  
3630 C CA  B SER   B 1   ? 0.3337 0.3356 0.3264 -0.0299 -0.0174 0.0128  1   SER   B CA  
3631 C C   A SER   B 1   ? 0.2789 0.3381 0.3119 -0.1264 -0.0967 0.0852  1   SER   B C   
3632 C C   B SER   B 1   ? 0.3276 0.3337 0.3267 -0.0291 -0.0189 0.0173  1   SER   B C   
3633 O O   A SER   B 1   ? 0.2894 0.3370 0.2787 -0.1156 -0.0954 0.0900  1   SER   B O   
3634 O O   B SER   B 1   ? 0.3294 0.3341 0.3212 -0.0283 -0.0195 0.0168  1   SER   B O   
3635 C CB  A SER   B 1   ? 0.3260 0.3335 0.3592 -0.1265 -0.0731 0.0387  1   SER   B CB  
3636 C CB  B SER   B 1   ? 0.3358 0.3358 0.3270 -0.0301 -0.0142 0.0077  1   SER   B CB  
3637 O OG  A SER   B 1   ? 0.3466 0.3445 0.4025 -0.1170 -0.0585 0.0271  1   SER   B OG  
3638 O OG  B SER   B 1   ? 0.3382 0.3372 0.3333 -0.0301 -0.0123 0.0049  1   SER   B OG  
3653 N N   A MET   B 2   ? 0.2529 0.3426 0.3295 -0.1179 -0.0901 0.1178  2   MET   B N   
3654 N N   B MET   B 2   ? 0.3196 0.3304 0.3310 -0.0283 -0.0186 0.0240  2   MET   B N   
3655 C CA  A MET   B 2   ? 0.2394 0.3425 0.3507 -0.0911 -0.0898 0.1292  2   MET   B CA  
3656 C CA  B MET   B 2   ? 0.3099 0.3248 0.3346 -0.0264 -0.0176 0.0291  2   MET   B CA  
3657 C C   A MET   B 2   ? 0.2073 0.3116 0.3207 -0.0714 -0.0902 0.1507  2   MET   B C   
3658 C C   B MET   B 2   ? 0.2876 0.3044 0.2983 -0.0276 -0.0180 0.0355  2   MET   B C   
3659 O O   A MET   B 2   ? 0.1977 0.3238 0.3320 -0.0567 -0.0908 0.1521  2   MET   B O   
3660 O O   B MET   B 2   ? 0.2898 0.3073 0.2990 -0.0265 -0.0154 0.0338  2   MET   B O   
3661 C CB  A MET   B 2   ? 0.2762 0.3810 0.4353 -0.0685 -0.0771 0.1051  2   MET   B CB  
3662 C CB  B MET   B 2   ? 0.3223 0.3388 0.3777 -0.0224 -0.0166 0.0271  2   MET   B CB  
3663 C CG  A MET   B 2   ? 0.3073 0.4173 0.5075 -0.0485 -0.0653 0.0921  2   MET   B CG  
3664 C CG  B MET   B 2   ? 0.3328 0.3508 0.4165 -0.0190 -0.0158 0.0266  2   MET   B CG  
3665 S SD  A MET   B 2   ? 0.3338 0.4472 0.5744 -0.0313 -0.0543 0.0786  2   MET   B SD  
3666 S SD  B MET   B 2   ? 0.3412 0.3606 0.4486 -0.0158 -0.0154 0.0264  2   MET   B SD  
3667 C CE  A MET   B 2   ? 0.3337 0.4503 0.5754 -0.0308 -0.0505 0.0772  2   MET   B CE  
3668 C CE  B MET   B 2   ? 0.3427 0.3630 0.4577 -0.0156 -0.0147 0.0253  2   MET   B CE  
3687 N N   A VAL   B 3   ? 0.1884 0.2685 0.2960 -0.0746 -0.0808 0.1523  3   VAL   B N   
3688 N N   B VAL   B 3   ? 0.2621 0.2798 0.2640 -0.0306 -0.0216 0.0432  3   VAL   B N   
3689 C CA  A VAL   B 3   ? 0.1885 0.2300 0.2878 -0.0639 -0.0650 0.1316  3   VAL   B CA  
3690 C CA  B VAL   B 3   ? 0.2362 0.2544 0.2344 -0.0329 -0.0264 0.0503  3   VAL   B CA  
3691 C C   A VAL   B 3   ? 0.1767 0.2223 0.2379 -0.0529 -0.0600 0.1112  3   VAL   B C   
3692 C C   B VAL   B 3   ? 0.2058 0.2292 0.2099 -0.0371 -0.0374 0.0637  3   VAL   B C   
3693 O O   A VAL   B 3   ? 0.1780 0.2360 0.2395 -0.0540 -0.0655 0.1170  3   VAL   B O   
3694 O O   B VAL   B 3   ? 0.2060 0.2319 0.1998 -0.0337 -0.0356 0.0618  3   VAL   B O   
3695 C CB  A VAL   B 3   ? 0.2119 0.2209 0.3346 -0.0567 -0.0534 0.1125  3   VAL   B CB  
3696 C CB  B VAL   B 3   ? 0.2411 0.2552 0.2338 -0.0316 -0.0213 0.0442  3   VAL   B CB  
3697 C CG1 A VAL   B 3   ? 0.2221 0.2146 0.3525 -0.0570 -0.0534 0.1047  3   VAL   B CG1 
3698 C CG1 B VAL   B 3   ? 0.2430 0.2554 0.2339 -0.0318 -0.0197 0.0415  3   VAL   B CG1 
3699 C CG2 A VAL   B 3   ? 0.2164 0.2269 0.3532 -0.0496 -0.0483 0.1118  3   VAL   B CG2 
3700 C CG2 B VAL   B 3   ? 0.2429 0.2563 0.2342 -0.0305 -0.0198 0.0432  3   VAL   B CG2 
3719 N N   . ASN   B 4   ? 0.1772 0.2014 0.1986 -0.0452 -0.0521 0.0809  4   ASN   B N   
3720 C CA  . ASN   B 4   ? 0.1723 0.1905 0.1668 -0.0490 -0.0385 0.0403  4   ASN   B CA  
3721 C C   . ASN   B 4   ? 0.1822 0.2013 0.1505 -0.0539 -0.0216 0.0247  4   ASN   B C   
3722 O O   . ASN   B 4   ? 0.1868 0.2152 0.1843 -0.0533 -0.0165 0.0063  4   ASN   B O   
3723 C CB  . ASN   B 4   ? 0.1697 0.1830 0.1526 -0.0410 -0.0432 0.0330  4   ASN   B CB  
3724 C CG  . ASN   B 4   ? 0.1686 0.1694 0.1441 -0.0407 -0.0368 0.0228  4   ASN   B CG  
3725 O OD1 . ASN   B 4   ? 0.1658 0.1586 0.1432 -0.0350 -0.0371 0.0214  4   ASN   B OD1 
3726 N ND2 . ASN   B 4   ? 0.1850 0.1769 0.1557 -0.0195 -0.0257 0.0164  4   ASN   B ND2 
3734 N N   . SER   B 5   ? 0.2010 0.2154 0.1536 -0.0490 0.0028  0.0279  5   SER   B N   
3735 C CA  . SER   B 5   ? 0.2290 0.2453 0.1984 -0.0339 0.0232  0.0293  5   SER   B CA  
3736 C C   . SER   B 5   ? 0.2380 0.2509 0.2286 -0.0474 0.0465  0.0318  5   SER   B C   
3737 O O   . SER   B 5   ? 0.2484 0.2558 0.3107 -0.0444 0.0605  0.0361  5   SER   B O   
3738 C CB  . SER   B 5   ? 0.2418 0.2684 0.2358 -0.0266 0.0262  0.0405  5   SER   B CB  
3739 O OG  . SER   B 5   ? 0.2595 0.2944 0.2913 -0.0198 0.0221  0.0410  5   SER   B OG  
3745 N N   . PHE   B 6   ? 0.2500 0.2638 0.1881 -0.0515 0.0509  0.0311  6   PHE   B N   
3746 C CA  . PHE   B 6   ? 0.2572 0.2614 0.1640 -0.0667 0.0481  0.0152  6   PHE   B CA  
3747 C C   . PHE   B 6   ? 0.3043 0.2849 0.2078 -0.0669 0.0616  -0.0101 6   PHE   B C   
3748 O O   . PHE   B 6   ? 0.3186 0.3137 0.2431 -0.0579 0.0378  -0.0256 6   PHE   B O   
3749 C CB  . PHE   B 6   ? 0.2252 0.2412 0.1530 -0.0639 0.0251  0.0117  6   PHE   B CB  
3750 C CG  . PHE   B 6   ? 0.1927 0.2125 0.1481 -0.0608 0.0144  0.0071  6   PHE   B CG  
3751 C CD1 . PHE   B 6   ? 0.1945 0.1879 0.1358 -0.0546 -0.0013 0.0027  6   PHE   B CD1 
3752 C CD2 . PHE   B 6   ? 0.1744 0.2156 0.1496 -0.0479 0.0140  0.0285  6   PHE   B CD2 
3753 C CE1 . PHE   B 6   ? 0.1861 0.1723 0.1465 -0.0427 -0.0054 -0.0035 6   PHE   B CE1 
3754 C CE2 . PHE   B 6   ? 0.1771 0.2002 0.1784 -0.0342 0.0136  0.0240  6   PHE   B CE2 
3755 C CZ  . PHE   B 6   ? 0.1767 0.1783 0.1601 -0.0365 0.0128  0.0012  6   PHE   B CZ  
3765 N N   A SER   B 7   ? 0.3293 0.2689 0.2052 -0.0829 0.0931  -0.0321 7   SER   B N   
3766 N N   B SER   B 7   ? 0.3099 0.2781 0.2346 -0.0672 0.0596  -0.0108 7   SER   B N   
3767 C CA  A SER   B 7   ? 0.3542 0.2699 0.2389 -0.0820 0.1116  -0.0392 7   SER   B CA  
3768 C CA  B SER   B 7   ? 0.3148 0.2731 0.2605 -0.0637 0.0570  -0.0104 7   SER   B CA  
3769 C C   A SER   B 7   ? 0.3481 0.2580 0.2282 -0.0817 0.1218  -0.0479 7   SER   B C   
3770 C C   B SER   B 7   ? 0.3131 0.2622 0.2600 -0.0626 0.0577  -0.0143 7   SER   B C   
3771 O O   A SER   B 7   ? 0.3518 0.2631 0.2622 -0.0801 0.1176  -0.0440 7   SER   B O   
3772 O O   B SER   B 7   ? 0.3143 0.2645 0.2672 -0.0614 0.0548  -0.0120 7   SER   B O   
3773 C CB  A SER   B 7   ? 0.3766 0.2818 0.2976 -0.0792 0.1209  -0.0395 7   SER   B CB  
3774 C CB  B SER   B 7   ? 0.3195 0.2778 0.2836 -0.0604 0.0545  -0.0079 7   SER   B CB  
3775 O OG  A SER   B 7   ? 0.3912 0.2986 0.3482 -0.0765 0.1204  -0.0379 7   SER   B OG  
3776 O OG  B SER   B 7   ? 0.3222 0.2819 0.2982 -0.0578 0.0517  -0.0065 7   SER   B OG  
3787 N N   A GLY   B 8   ? 0.3430 0.2453 0.2344 -0.0728 0.1186  -0.0553 8   GLY   B N   
3788 N N   B GLY   B 8   ? 0.3105 0.2485 0.2541 -0.0615 0.0617  -0.0211 8   GLY   B N   
3789 C CA  A GLY   B 8   ? 0.3301 0.2311 0.2434 -0.0679 0.1144  -0.0611 8   GLY   B CA  
3790 C CA  B GLY   B 8   ? 0.3062 0.2338 0.2444 -0.0613 0.0681  -0.0288 8   GLY   B CA  
3791 C C   A GLY   B 8   ? 0.3111 0.2140 0.2371 -0.0658 0.1129  -0.0487 8   GLY   B C   
3792 C C   B GLY   B 8   ? 0.3000 0.2174 0.2290 -0.0619 0.0782  -0.0353 8   GLY   B C   
3793 O O   A GLY   B 8   ? 0.3178 0.2193 0.2690 -0.0558 0.1175  -0.0502 8   GLY   B O   
3794 O O   B GLY   B 8   ? 0.3019 0.2196 0.2345 -0.0595 0.0769  -0.0361 8   GLY   B O   
3801 N N   . TYR   B 9   ? 0.2934 0.1998 0.2093 -0.0620 0.0889  -0.0426 9   TYR   B N   
3802 C CA  . TYR   B 9   ? 0.2703 0.1765 0.1801 -0.0459 0.0652  -0.0291 9   TYR   B CA  
3803 C C   . TYR   B 9   ? 0.2609 0.1828 0.1576 -0.0394 0.0327  -0.0191 9   TYR   B C   
3804 O O   . TYR   B 9   ? 0.2770 0.2123 0.1960 -0.0411 0.0274  -0.0042 9   TYR   B O   
3805 C CB  . TYR   B 9   ? 0.2678 0.1619 0.1912 -0.0377 0.0656  -0.0243 9   TYR   B CB  
3806 C CG  . TYR   B 9   ? 0.2614 0.1444 0.1954 -0.0420 0.0688  -0.0339 9   TYR   B CG  
3807 C CD1 . TYR   B 9   ? 0.2684 0.1471 0.2153 -0.0565 0.0696  -0.0304 9   TYR   B CD1 
3808 C CD2 . TYR   B 9   ? 0.2446 0.1351 0.1910 -0.0350 0.0713  -0.0352 9   TYR   B CD2 
3809 C CE1 . TYR   B 9   ? 0.2627 0.1552 0.2274 -0.0664 0.0727  -0.0409 9   TYR   B CE1 
3810 C CE2 . TYR   B 9   ? 0.2489 0.1382 0.2133 -0.0376 0.0663  -0.0402 9   TYR   B CE2 
3811 C CZ  . TYR   B 9   ? 0.2557 0.1542 0.2328 -0.0552 0.0709  -0.0541 9   TYR   B CZ  
3812 O OH  . TYR   B 9   ? 0.2558 0.1731 0.2505 -0.0698 0.0662  -0.0684 9   TYR   B OH  
3823 N N   . LEU   B 10  ? 0.2367 0.1579 0.1436 -0.0318 0.0100  -0.0193 10  LEU   B N   
3824 C CA  . LEU   B 10  ? 0.2325 0.1567 0.1504 -0.0387 -0.0097 -0.0258 10  LEU   B CA  
3825 C C   . LEU   B 10  ? 0.2119 0.1544 0.1442 -0.0403 -0.0180 -0.0253 10  LEU   B C   
3826 O O   . LEU   B 10  ? 0.2021 0.1557 0.1511 -0.0302 -0.0110 -0.0241 10  LEU   B O   
3827 C CB  . LEU   B 10  ? 0.2477 0.1598 0.1723 -0.0425 -0.0248 -0.0225 10  LEU   B CB  
3828 C CG  . LEU   B 10  ? 0.2670 0.1715 0.2105 -0.0404 -0.0439 -0.0122 10  LEU   B CG  
3829 C CD1 . LEU   B 10  ? 0.2776 0.1908 0.2433 -0.0417 -0.0417 -0.0125 10  LEU   B CD1 
3830 C CD2 . LEU   B 10  ? 0.2818 0.1769 0.2419 -0.0402 -0.0353 0.0004  10  LEU   B CD2 
3842 N N   . LYS   B 11  ? 0.2202 0.1772 0.1526 -0.0314 -0.0244 -0.0215 11  LYS   B N   
3843 C CA  . LYS   B 11  ? 0.2347 0.2059 0.1719 -0.0205 -0.0420 -0.0200 11  LYS   B CA  
3844 C C   . LYS   B 11  ? 0.2235 0.1926 0.1719 -0.0428 -0.0411 -0.0358 11  LYS   B C   
3845 O O   . LYS   B 11  ? 0.2413 0.2137 0.2129 -0.0532 -0.0366 -0.0674 11  LYS   B O   
3846 C CB  . LYS   B 11  ? 0.2633 0.2492 0.2210 0.0071  -0.0445 -0.0043 11  LYS   B CB  
3847 C CG  . LYS   B 11  ? 0.2913 0.2794 0.2813 0.0215  -0.0418 -0.0008 11  LYS   B CG  
3848 C CD  . LYS   B 11  ? 0.3122 0.3033 0.3421 0.0295  -0.0398 -0.0049 11  LYS   B CD  
3849 C CE  . LYS   B 11  ? 0.3288 0.3213 0.3899 0.0289  -0.0376 -0.0081 11  LYS   B CE  
3850 N NZ  . LYS   B 11  ? 0.3389 0.3325 0.4191 0.0266  -0.0357 -0.0079 11  LYS   B NZ  
3864 N N   . LEU   B 12  ? 0.1976 0.1665 0.1790 -0.0385 -0.0242 -0.0359 12  LEU   B N   
3865 C CA  . LEU   B 12  ? 0.1949 0.1517 0.1971 -0.0389 -0.0230 -0.0294 12  LEU   B CA  
3866 C C   . LEU   B 12  ? 0.1871 0.1559 0.2082 -0.0417 -0.0354 -0.0289 12  LEU   B C   
3867 O O   . LEU   B 12  ? 0.1881 0.1601 0.2327 -0.0545 -0.0408 -0.0231 12  LEU   B O   
3868 C CB  . LEU   B 12  ? 0.1954 0.1319 0.1949 -0.0323 -0.0157 -0.0282 12  LEU   B CB  
3869 C CG  . LEU   B 12  ? 0.1955 0.1350 0.2012 -0.0314 -0.0146 -0.0233 12  LEU   B CG  
3870 C CD1 . LEU   B 12  ? 0.2072 0.1393 0.1960 -0.0191 -0.0095 -0.0146 12  LEU   B CD1 
3871 C CD2 . LEU   B 12  ? 0.2015 0.1394 0.2235 -0.0284 -0.0141 -0.0343 12  LEU   B CD2 
3883 N N   . THR   B 13  ? 0.1796 0.1580 0.2082 -0.0402 -0.0344 -0.0395 13  THR   B N   
3884 C CA  . THR   B 13  ? 0.1794 0.1642 0.1996 -0.0445 -0.0378 -0.0250 13  THR   B CA  
3885 C C   . THR   B 13  ? 0.2085 0.1773 0.2054 -0.0509 -0.0512 -0.0208 13  THR   B C   
3886 O O   . THR   B 13  ? 0.2181 0.1767 0.2300 -0.0520 -0.0181 -0.0212 13  THR   B O   
3887 C CB  . THR   B 13  ? 0.1657 0.1657 0.1996 -0.0444 -0.0362 -0.0175 13  THR   B CB  
3888 O OG1 . THR   B 13  ? 0.1617 0.1605 0.1997 -0.0341 -0.0209 -0.0182 13  THR   B OG1 
3889 C CG2 . THR   B 13  ? 0.1778 0.1744 0.2070 -0.0387 -0.0231 -0.0086 13  THR   B CG2 
3897 N N   A ASP   B 14  ? 0.2266 0.1877 0.2217 -0.0509 -0.0868 -0.0125 14  ASP   B N   
3898 N N   B ASP   B 14  ? 0.2154 0.1826 0.2253 -0.0485 -0.0535 -0.0144 14  ASP   B N   
3899 C CA  A ASP   B 14  ? 0.2390 0.2092 0.2502 -0.0499 -0.1020 0.0076  14  ASP   B CA  
3900 C CA  B ASP   B 14  ? 0.2203 0.1898 0.2450 -0.0466 -0.0549 -0.0065 14  ASP   B CA  
3901 C C   A ASP   B 14  ? 0.2277 0.1927 0.2109 -0.0542 -0.0734 0.0114  14  ASP   B C   
3902 C C   B ASP   B 14  ? 0.2075 0.1776 0.2145 -0.0458 -0.0565 -0.0008 14  ASP   B C   
3903 O O   A ASP   B 14  ? 0.2543 0.2160 0.2150 -0.0594 -0.0724 0.0232  14  ASP   B O   
3904 O O   B ASP   B 14  ? 0.2125 0.1825 0.2157 -0.0460 -0.0587 0.0002  14  ASP   B O   
3905 C CB  A ASP   B 14  ? 0.2631 0.2485 0.3314 -0.0376 -0.1210 0.0127  14  ASP   B CB  
3906 C CB  B ASP   B 14  ? 0.2360 0.2078 0.2923 -0.0436 -0.0522 -0.0069 14  ASP   B CB  
3907 C CG  A ASP   B 14  ? 0.2945 0.2863 0.4197 -0.0267 -0.1165 0.0067  14  ASP   B CG  
3908 C CG  B ASP   B 14  ? 0.2502 0.2232 0.3316 -0.0410 -0.0472 -0.0089 14  ASP   B CG  
3909 O OD1 A ASP   B 14  ? 0.3156 0.3043 0.4427 -0.0267 -0.1105 -0.0085 14  ASP   B OD1 
3910 O OD1 B ASP   B 14  ? 0.2552 0.2306 0.3427 -0.0409 -0.0438 -0.0112 14  ASP   B OD1 
3911 O OD2 A ASP   B 14  ? 0.2992 0.3027 0.4608 -0.0248 -0.1172 0.0105  14  ASP   B OD2 
3912 O OD2 B ASP   B 14  ? 0.2549 0.2281 0.3462 -0.0415 -0.0478 -0.0090 14  ASP   B OD2 
3921 N N   . ASN   B 15  ? 0.1883 0.1618 0.1838 -0.0413 -0.0582 0.0044  15  ASN   B N   
3922 C CA  . ASN   B 15  ? 0.1558 0.1414 0.1772 -0.0277 -0.0291 -0.0005 15  ASN   B CA  
3923 C C   . ASN   B 15  ? 0.1379 0.1327 0.1685 -0.0180 -0.0247 -0.0084 15  ASN   B C   
3924 O O   . ASN   B 15  ? 0.1424 0.1294 0.1958 -0.0159 -0.0394 -0.0166 15  ASN   B O   
3925 C CB  . ASN   B 15  ? 0.1487 0.1379 0.1869 -0.0108 -0.0328 -0.0003 15  ASN   B CB  
3926 C CG  . ASN   B 15  ? 0.1442 0.1397 0.1867 -0.0148 -0.0129 -0.0048 15  ASN   B CG  
3927 O OD1 . ASN   B 15  ? 0.1538 0.1678 0.2131 -0.0357 -0.0207 0.0064  15  ASN   B OD1 
3928 N ND2 . ASN   B 15  ? 0.1449 0.1285 0.1860 -0.0087 0.0079  -0.0158 15  ASN   B ND2 
3936 N N   . VAL   B 16  ? 0.1385 0.1242 0.1654 -0.0205 -0.0350 -0.0100 16  VAL   B N   
3937 C CA  . VAL   B 16  ? 0.1388 0.1241 0.1553 -0.0208 -0.0227 -0.0241 16  VAL   B CA  
3938 C C   . VAL   B 16  ? 0.1424 0.1300 0.1516 -0.0272 -0.0232 -0.0168 16  VAL   B C   
3939 O O   . VAL   B 16  ? 0.1458 0.1458 0.1764 -0.0250 -0.0175 -0.0312 16  VAL   B O   
3940 C CB  . VAL   B 16  ? 0.1527 0.1253 0.1647 -0.0126 -0.0120 -0.0203 16  VAL   B CB  
3941 C CG1 . VAL   B 16  ? 0.1612 0.1290 0.1590 0.0027  -0.0103 -0.0157 16  VAL   B CG1 
3942 C CG2 . VAL   B 16  ? 0.1543 0.1383 0.1804 -0.0067 -0.0069 -0.0146 16  VAL   B CG2 
3952 N N   . TYR   B 17  ? 0.1480 0.1400 0.1504 -0.0259 -0.0154 -0.0179 17  TYR   B N   
3953 C CA  . TYR   B 17  ? 0.1543 0.1491 0.1473 -0.0253 -0.0139 -0.0059 17  TYR   B CA  
3954 C C   . TYR   B 17  ? 0.1473 0.1302 0.1518 -0.0277 -0.0135 -0.0105 17  TYR   B C   
3955 O O   . TYR   B 17  ? 0.1470 0.1344 0.1608 -0.0197 -0.0236 -0.0321 17  TYR   B O   
3956 C CB  . TYR   B 17  ? 0.1743 0.1780 0.1568 -0.0111 -0.0143 0.0217  17  TYR   B CB  
3957 C CG  . TYR   B 17  ? 0.2039 0.2097 0.1851 -0.0062 -0.0227 0.0161  17  TYR   B CG  
3958 C CD1 . TYR   B 17  ? 0.2198 0.2142 0.1875 -0.0028 -0.0266 0.0238  17  TYR   B CD1 
3959 C CD2 . TYR   B 17  ? 0.2269 0.2348 0.2043 0.0013  -0.0282 0.0078  17  TYR   B CD2 
3960 C CE1 . TYR   B 17  ? 0.2393 0.2337 0.1951 0.0046  -0.0333 0.0160  17  TYR   B CE1 
3961 C CE2 . TYR   B 17  ? 0.2454 0.2507 0.2200 0.0074  -0.0376 0.0082  17  TYR   B CE2 
3962 C CZ  . TYR   B 17  ? 0.2540 0.2552 0.2144 0.0113  -0.0461 0.0147  17  TYR   B CZ  
3963 O OH  . TYR   B 17  ? 0.2722 0.2798 0.2442 0.0201  -0.0549 0.0167  17  TYR   B OH  
3973 N N   . ILE   B 18  ? 0.1579 0.1295 0.1419 -0.0209 -0.0093 -0.0221 18  ILE   B N   
3974 C CA  . ILE   B 18  ? 0.1608 0.1231 0.1371 -0.0219 -0.0100 -0.0187 18  ILE   B CA  
3975 C C   . ILE   B 18  ? 0.1716 0.1286 0.1326 -0.0262 -0.0101 -0.0254 18  ILE   B C   
3976 O O   . ILE   B 18  ? 0.1897 0.1420 0.1426 -0.0228 0.0092  -0.0310 18  ILE   B O   
3977 C CB  . ILE   B 18  ? 0.1658 0.1262 0.1478 -0.0323 -0.0045 -0.0094 18  ILE   B CB  
3978 C CG1 . ILE   B 18  ? 0.1668 0.1347 0.1584 -0.0311 -0.0046 -0.0017 18  ILE   B CG1 
3979 C CG2 . ILE   B 18  ? 0.1669 0.1320 0.1559 -0.0331 -0.0024 -0.0090 18  ILE   B CG2 
3980 C CD1 . ILE   B 18  ? 0.1741 0.1657 0.1889 -0.0331 -0.0136 0.0153  18  ILE   B CD1 
3992 N N   . LYS   B 19  ? 0.1720 0.1306 0.1414 -0.0128 0.0141  -0.0279 19  LYS   B N   
3993 C CA  . LYS   B 19  ? 0.1729 0.1370 0.1531 -0.0159 0.0168  -0.0303 19  LYS   B CA  
3994 C C   . LYS   B 19  ? 0.1582 0.1369 0.1592 -0.0163 0.0200  -0.0351 19  LYS   B C   
3995 O O   . LYS   B 19  ? 0.1561 0.1396 0.1580 -0.0072 0.0128  -0.0335 19  LYS   B O   
3996 C CB  . LYS   B 19  ? 0.1947 0.1532 0.1708 -0.0181 0.0298  -0.0137 19  LYS   B CB  
3997 C CG  . LYS   B 19  ? 0.2138 0.1739 0.1886 -0.0237 0.0389  -0.0174 19  LYS   B CG  
3998 C CD  . LYS   B 19  ? 0.2344 0.2035 0.1989 -0.0340 0.0437  -0.0107 19  LYS   B CD  
3999 C CE  . LYS   B 19  ? 0.2568 0.2291 0.2235 -0.0373 0.0467  -0.0096 19  LYS   B CE  
4000 N NZ  . LYS   B 19  ? 0.2717 0.2453 0.2412 -0.0445 0.0505  -0.0042 19  LYS   B NZ  
4014 N N   . ASN   B 20  ? 0.1598 0.1430 0.1864 -0.0098 0.0270  -0.0450 20  ASN   B N   
4015 C CA  . ASN   B 20  ? 0.1588 0.1540 0.2103 -0.0013 0.0264  -0.0522 20  ASN   B CA  
4016 C C   . ASN   B 20  ? 0.1552 0.1727 0.2141 -0.0073 0.0352  -0.0625 20  ASN   B C   
4017 O O   . ASN   B 20  ? 0.1732 0.2087 0.2338 -0.0262 0.0386  -0.0658 20  ASN   B O   
4018 C CB  . ASN   B 20  ? 0.1821 0.1556 0.2276 0.0106  0.0232  -0.0495 20  ASN   B CB  
4019 C CG  . ASN   B 20  ? 0.2072 0.1624 0.2506 0.0348  0.0145  -0.0555 20  ASN   B CG  
4020 O OD1 . ASN   B 20  ? 0.2357 0.1914 0.2847 0.0508  0.0140  -0.0653 20  ASN   B OD1 
4021 N ND2 . ASN   B 20  ? 0.2047 0.1614 0.2359 0.0311  0.0026  -0.0550 20  ASN   B ND2 
4028 N N   . ALA   B 21  ? 0.1603 0.1605 0.2147 -0.0156 0.0343  -0.0498 21  ALA   B N   
4029 C CA  . ALA   B 21  ? 0.1691 0.1634 0.2331 -0.0232 0.0257  -0.0347 21  ALA   B CA  
4030 C C   . ALA   B 21  ? 0.1679 0.1431 0.2233 -0.0173 0.0302  -0.0253 21  ALA   B C   
4031 O O   . ALA   B 21  ? 0.1698 0.1400 0.2290 -0.0278 0.0307  -0.0248 21  ALA   B O   
4032 C CB  . ALA   B 21  ? 0.1839 0.1887 0.2476 -0.0398 0.0217  -0.0140 21  ALA   B CB  
4038 N N   . ASP   B 22  ? 0.1623 0.1393 0.2269 -0.0155 0.0204  -0.0202 22  ASP   B N   
4039 C CA  . ASP   B 22  ? 0.1576 0.1327 0.2172 -0.0080 0.0178  -0.0174 22  ASP   B CA  
4040 C C   . ASP   B 22  ? 0.1543 0.1326 0.1818 -0.0136 0.0134  -0.0074 22  ASP   B C   
4041 O O   . ASP   B 22  ? 0.1615 0.1337 0.1858 -0.0086 0.0123  -0.0036 22  ASP   B O   
4042 C CB  . ASP   B 22  ? 0.1645 0.1397 0.2578 -0.0061 0.0154  -0.0020 22  ASP   B CB  
4043 C CG  . ASP   B 22  ? 0.1760 0.1597 0.2982 -0.0004 -0.0145 -0.0050 22  ASP   B CG  
4044 O OD1 . ASP   B 22  ? 0.1916 0.1623 0.2983 0.0064  -0.0314 -0.0119 22  ASP   B OD1 
4045 O OD2 . ASP   B 22  ? 0.1869 0.1920 0.3441 0.0100  -0.0322 -0.0164 22  ASP   B OD2 
4050 N N   . ILE   B 23  ? 0.1589 0.1242 0.1652 -0.0092 0.0032  0.0103  23  ILE   B N   
4051 C CA  . ILE   B 23  ? 0.1460 0.1295 0.1605 -0.0055 -0.0006 0.0061  23  ILE   B CA  
4052 C C   . ILE   B 23  ? 0.1393 0.1289 0.1550 -0.0011 -0.0043 -0.0002 23  ILE   B C   
4053 O O   . ILE   B 23  ? 0.1373 0.1308 0.1530 -0.0048 -0.0000 0.0057  23  ILE   B O   
4054 C CB  . ILE   B 23  ? 0.1466 0.1341 0.1764 -0.0155 -0.0016 0.0139  23  ILE   B CB  
4055 C CG1 . ILE   B 23  ? 0.1511 0.1439 0.1834 -0.0139 0.0076  0.0247  23  ILE   B CG1 
4056 C CG2 . ILE   B 23  ? 0.1553 0.1529 0.1834 -0.0139 -0.0101 0.0113  23  ILE   B CG2 
4057 C CD1 . ILE   B 23  ? 0.1583 0.1589 0.1854 -0.0093 0.0131  0.0188  23  ILE   B CD1 
4069 N N   . VAL   B 24  ? 0.1437 0.1291 0.1682 -0.0012 -0.0066 -0.0028 24  VAL   B N   
4070 C CA  . VAL   B 24  ? 0.1408 0.1313 0.1844 -0.0028 -0.0121 -0.0083 24  VAL   B CA  
4071 C C   . VAL   B 24  ? 0.1367 0.1340 0.1848 -0.0114 -0.0063 0.0025  24  VAL   B C   
4072 O O   . VAL   B 24  ? 0.1365 0.1414 0.2062 -0.0134 -0.0058 0.0159  24  VAL   B O   
4073 C CB  . VAL   B 24  ? 0.1515 0.1508 0.1970 0.0073  -0.0206 -0.0047 24  VAL   B CB  
4074 C CG1 . VAL   B 24  ? 0.1523 0.1533 0.2199 -0.0002 -0.0156 -0.0079 24  VAL   B CG1 
4075 C CG2 . VAL   B 24  ? 0.1626 0.1786 0.2013 0.0140  -0.0146 -0.0111 24  VAL   B CG2 
4085 N N   . GLU   B 25  ? 0.1586 0.1446 0.1849 -0.0072 0.0000  0.0028  25  GLU   B N   
4086 C CA  . GLU   B 25  ? 0.1669 0.1677 0.2037 0.0034  0.0149  -0.0015 25  GLU   B CA  
4087 C C   . GLU   B 25  ? 0.1624 0.1537 0.1791 -0.0032 0.0174  0.0074  25  GLU   B C   
4088 O O   . GLU   B 25  ? 0.1685 0.1749 0.1900 -0.0037 0.0207  0.0192  25  GLU   B O   
4089 C CB  . GLU   B 25  ? 0.1987 0.2068 0.2588 0.0217  0.0294  -0.0091 25  GLU   B CB  
4090 C CG  . GLU   B 25  ? 0.2411 0.2675 0.3594 0.0296  0.0248  -0.0165 25  GLU   B CG  
4091 C CD  . GLU   B 25  ? 0.2810 0.3216 0.4500 0.0268  0.0206  -0.0245 25  GLU   B CD  
4092 O OE1 . GLU   B 25  ? 0.2956 0.3420 0.4839 0.0295  0.0254  -0.0241 25  GLU   B OE1 
4093 O OE2 . GLU   B 25  ? 0.2944 0.3368 0.4857 0.0258  0.0148  -0.0336 25  GLU   B OE2 
4100 N N   . GLU   B 26  ? 0.1651 0.1467 0.1635 -0.0177 0.0065  0.0042  26  GLU   B N   
4101 C CA  . GLU   B 26  ? 0.1635 0.1601 0.1690 -0.0296 -0.0037 0.0061  26  GLU   B CA  
4102 C C   . GLU   B 26  ? 0.1448 0.1569 0.1733 -0.0214 0.0016  0.0225  26  GLU   B C   
4103 O O   . GLU   B 26  ? 0.1676 0.1790 0.1765 -0.0185 0.0027  0.0361  26  GLU   B O   
4104 C CB  . GLU   B 26  ? 0.1907 0.1799 0.1833 -0.0440 -0.0066 0.0111  26  GLU   B CB  
4105 C CG  . GLU   B 26  ? 0.2306 0.2120 0.2409 -0.0477 0.0012  -0.0037 26  GLU   B CG  
4106 C CD  . GLU   B 26  ? 0.2576 0.2349 0.2615 -0.0647 0.0146  -0.0314 26  GLU   B CD  
4107 O OE1 . GLU   B 26  ? 0.2767 0.2192 0.2563 -0.0772 0.0545  -0.0311 26  GLU   B OE1 
4108 O OE2 . GLU   B 26  ? 0.2559 0.2744 0.2922 -0.0576 0.0125  -0.0165 26  GLU   B OE2 
4115 N N   . ALA   B 27  ? 0.1285 0.1440 0.1743 -0.0148 0.0066  0.0195  27  ALA   B N   
4116 C CA  . ALA   B 27  ? 0.1353 0.1395 0.1893 -0.0102 0.0032  0.0298  27  ALA   B CA  
4117 C C   . ALA   B 27  ? 0.1409 0.1474 0.2069 -0.0086 0.0143  0.0394  27  ALA   B C   
4118 O O   . ALA   B 27  ? 0.1517 0.1541 0.2118 0.0011  0.0195  0.0451  27  ALA   B O   
4119 C CB  . ALA   B 27  ? 0.1538 0.1290 0.1954 -0.0144 -0.0031 0.0161  27  ALA   B CB  
4125 N N   . LYS   B 28  ? 0.1353 0.1688 0.2411 -0.0161 0.0186  0.0563  28  LYS   B N   
4126 C CA  . LYS   B 28  ? 0.1556 0.2059 0.2644 -0.0054 0.0433  0.0821  28  LYS   B CA  
4127 C C   . LYS   B 28  ? 0.1844 0.2307 0.2492 0.0091  0.0604  0.0722  28  LYS   B C   
4128 O O   . LYS   B 28  ? 0.2085 0.2324 0.2630 0.0012  0.0612  0.0754  28  LYS   B O   
4129 C CB  . LYS   B 28  ? 0.1732 0.2395 0.3097 0.0021  0.0656  0.1008  28  LYS   B CB  
4130 C CG  . LYS   B 28  ? 0.2030 0.2792 0.3508 0.0132  0.0659  0.1142  28  LYS   B CG  
4131 C CD  . LYS   B 28  ? 0.2494 0.3323 0.4016 0.0198  0.0845  0.1149  28  LYS   B CD  
4132 C CE  . LYS   B 28  ? 0.2842 0.3683 0.4435 0.0285  0.0929  0.1147  28  LYS   B CE  
4133 N NZ  . LYS   B 28  ? 0.2949 0.3754 0.4630 0.0353  0.0946  0.1186  28  LYS   B NZ  
4147 N N   A LYS   B 29  ? 0.1974 0.2476 0.2465 0.0331  0.0600  0.0536  29  LYS   B N   
4148 N N   B LYS   B 29  ? 0.2034 0.2506 0.2587 0.0139  0.0534  0.0638  29  LYS   B N   
4149 C CA  A LYS   B 29  ? 0.2332 0.2714 0.2664 0.0327  0.0613  0.0477  29  LYS   B CA  
4150 C CA  B LYS   B 29  ? 0.2236 0.2705 0.2722 0.0163  0.0476  0.0578  29  LYS   B CA  
4151 C C   A LYS   B 29  ? 0.2285 0.2766 0.2299 0.0306  0.0556  0.0664  29  LYS   B C   
4152 C C   B LYS   B 29  ? 0.2176 0.2697 0.2418 0.0198  0.0485  0.0651  29  LYS   B C   
4153 O O   A LYS   B 29  ? 0.2446 0.2992 0.2432 0.0293  0.0472  0.0713  29  LYS   B O   
4154 O O   B LYS   B 29  ? 0.2227 0.2755 0.2426 0.0198  0.0466  0.0666  29  LYS   B O   
4155 C CB  A LYS   B 29  ? 0.2810 0.2980 0.3404 0.0256  0.0508  0.0319  29  LYS   B CB  
4156 C CB  B LYS   B 29  ? 0.2504 0.2911 0.3196 0.0143  0.0372  0.0450  29  LYS   B CB  
4157 C CG  A LYS   B 29  ? 0.3182 0.3197 0.4160 0.0166  0.0460  0.0278  29  LYS   B CG  
4158 C CG  B LYS   B 29  ? 0.2731 0.3078 0.3653 0.0120  0.0298  0.0356  29  LYS   B CG  
4159 C CD  A LYS   B 29  ? 0.3508 0.3343 0.4767 0.0082  0.0480  0.0217  29  LYS   B CD  
4160 C CD  B LYS   B 29  ? 0.2911 0.3204 0.4022 0.0101  0.0250  0.0272  29  LYS   B CD  
4161 C CE  A LYS   B 29  ? 0.3743 0.3435 0.5191 0.0014  0.0509  0.0176  29  LYS   B CE  
4162 C CE  B LYS   B 29  ? 0.3032 0.3289 0.4283 0.0084  0.0221  0.0212  29  LYS   B CE  
4163 N NZ  A LYS   B 29  ? 0.3818 0.3497 0.5474 -0.0016 0.0512  0.0145  29  LYS   B NZ  
4164 N NZ  B LYS   B 29  ? 0.3094 0.3337 0.4443 0.0078  0.0203  0.0181  29  LYS   B NZ  
4191 N N   . VAL   B 30  ? 0.2056 0.2630 0.2189 0.0209  0.0486  0.0698  30  VAL   B N   
4192 C CA  . VAL   B 30  ? 0.1908 0.2540 0.2426 0.0107  0.0187  0.0756  30  VAL   B CA  
4193 C C   . VAL   B 30  ? 0.1665 0.2479 0.2444 0.0074  0.0278  0.0962  30  VAL   B C   
4194 O O   . VAL   B 30  ? 0.1817 0.2673 0.2542 0.0177  0.0263  0.1110  30  VAL   B O   
4195 C CB  . VAL   B 30  ? 0.2008 0.2492 0.2791 -0.0036 -0.0127 0.0636  30  VAL   B CB  
4196 C CG1 . VAL   B 30  ? 0.1982 0.2529 0.2686 -0.0074 -0.0139 0.0588  30  VAL   B CG1 
4197 C CG2 . VAL   B 30  ? 0.2062 0.2469 0.3003 -0.0105 -0.0219 0.0503  30  VAL   B CG2 
4208 N N   . LYS   B 31  ? 0.1549 0.2148 0.2855 -0.0130 0.0197  0.0998  31  LYS   B N   
4209 C CA  . LYS   B 31  ? 0.1469 0.2033 0.3196 -0.0316 0.0124  0.1046  31  LYS   B CA  
4210 C C   . LYS   B 31  ? 0.1398 0.1658 0.2802 -0.0275 -0.0175 0.0843  31  LYS   B C   
4211 O O   . LYS   B 31  ? 0.1517 0.1808 0.2999 -0.0199 -0.0125 0.1015  31  LYS   B O   
4212 C CB  . LYS   B 31  ? 0.1686 0.2469 0.3762 -0.0327 0.0305  0.1161  31  LYS   B CB  
4213 C CG  . LYS   B 31  ? 0.2002 0.2955 0.4105 -0.0319 0.0433  0.1131  31  LYS   B CG  
4214 C CD  . LYS   B 31  ? 0.2390 0.3408 0.4399 -0.0274 0.0400  0.1022  31  LYS   B CD  
4215 C CE  . LYS   B 31  ? 0.2692 0.3674 0.4712 -0.0247 0.0281  0.0893  31  LYS   B CE  
4216 N NZ  . LYS   B 31  ? 0.2747 0.3821 0.4875 -0.0209 0.0175  0.0777  31  LYS   B NZ  
4230 N N   . PRO   B 32  ? 0.1458 0.1398 0.2065 -0.0239 -0.0352 0.0428  32  PRO   B N   
4231 C CA  . PRO   B 32  ? 0.1532 0.1339 0.1599 -0.0266 -0.0362 0.0261  32  PRO   B CA  
4232 C C   . PRO   B 32  ? 0.1662 0.1240 0.1639 -0.0303 -0.0427 0.0314  32  PRO   B C   
4233 O O   . PRO   B 32  ? 0.1796 0.1286 0.1959 -0.0319 -0.0641 0.0299  32  PRO   B O   
4234 C CB  . PRO   B 32  ? 0.1693 0.1357 0.1573 -0.0265 -0.0251 0.0122  32  PRO   B CB  
4235 C CG  . PRO   B 32  ? 0.1851 0.1291 0.1645 -0.0213 -0.0378 0.0149  32  PRO   B CG  
4236 C CD  . PRO   B 32  ? 0.1687 0.1299 0.1837 -0.0159 -0.0484 0.0304  32  PRO   B CD  
4244 N N   . THR   B 33  ? 0.1658 0.1213 0.1433 -0.0218 -0.0407 0.0194  33  THR   B N   
4245 C CA  . THR   B 33  ? 0.1720 0.1296 0.1438 -0.0249 -0.0363 0.0241  33  THR   B CA  
4246 C C   . THR   B 33  ? 0.1735 0.1195 0.1347 -0.0230 -0.0366 0.0143  33  THR   B C   
4247 O O   . THR   B 33  ? 0.1972 0.1232 0.1508 -0.0351 -0.0468 0.0117  33  THR   B O   
4248 C CB  . THR   B 33  ? 0.1811 0.1352 0.1495 -0.0083 -0.0443 0.0272  33  THR   B CB  
4249 O OG1 . THR   B 33  ? 0.1713 0.1466 0.1559 -0.0144 -0.0380 0.0358  33  THR   B OG1 
4250 C CG2 . THR   B 33  ? 0.2044 0.1397 0.1675 0.0011  -0.0481 0.0227  33  THR   B CG2 
4258 N N   . VAL   B 34  ? 0.1618 0.1152 0.1293 -0.0271 -0.0345 0.0096  34  VAL   B N   
4259 C CA  . VAL   B 34  ? 0.1482 0.1116 0.1219 -0.0162 -0.0279 0.0074  34  VAL   B CA  
4260 C C   . VAL   B 34  ? 0.1320 0.1082 0.1097 -0.0196 -0.0147 0.0049  34  VAL   B C   
4261 O O   . VAL   B 34  ? 0.1530 0.1098 0.1165 -0.0205 -0.0257 0.0030  34  VAL   B O   
4262 C CB  . VAL   B 34  ? 0.1515 0.1242 0.1543 -0.0048 -0.0296 -0.0006 34  VAL   B CB  
4263 C CG1 . VAL   B 34  ? 0.1538 0.1347 0.1597 -0.0016 -0.0169 -0.0061 34  VAL   B CG1 
4264 C CG2 . VAL   B 34  ? 0.1593 0.1306 0.1762 -0.0049 -0.0247 -0.0029 34  VAL   B CG2 
4274 N N   . VAL   B 35  ? 0.1278 0.1074 0.1122 -0.0182 -0.0025 0.0022  35  VAL   B N   
4275 C CA  . VAL   B 35  ? 0.1215 0.1061 0.1068 -0.0148 -0.0022 0.0057  35  VAL   B CA  
4276 C C   . VAL   B 35  ? 0.1149 0.1040 0.1197 -0.0123 -0.0042 0.0057  35  VAL   B C   
4277 O O   . VAL   B 35  ? 0.1215 0.1046 0.1174 -0.0194 -0.0008 -0.0069 35  VAL   B O   
4278 C CB  . VAL   B 35  ? 0.1247 0.1217 0.1077 -0.0157 0.0026  0.0090  35  VAL   B CB  
4279 C CG1 . VAL   B 35  ? 0.1169 0.1356 0.1300 -0.0218 0.0017  -0.0006 35  VAL   B CG1 
4280 C CG2 . VAL   B 35  ? 0.1230 0.1263 0.1284 -0.0029 0.0058  0.0027  35  VAL   B CG2 
4290 N N   . VAL   B 36  ? 0.1166 0.1058 0.1042 -0.0156 -0.0082 0.0017  36  VAL   B N   
4291 C CA  . VAL   B 36  ? 0.1157 0.1013 0.1072 -0.0088 -0.0069 0.0021  36  VAL   B CA  
4292 C C   . VAL   B 36  ? 0.1099 0.0997 0.1013 -0.0097 0.0014  -0.0015 36  VAL   B C   
4293 O O   . VAL   B 36  ? 0.1191 0.1137 0.1185 -0.0058 -0.0010 -0.0095 36  VAL   B O   
4294 C CB  . VAL   B 36  ? 0.1152 0.1048 0.1127 -0.0131 -0.0040 -0.0005 36  VAL   B CB  
4295 C CG1 . VAL   B 36  ? 0.1160 0.1173 0.1320 -0.0184 -0.0038 0.0022  36  VAL   B CG1 
4296 C CG2 . VAL   B 36  ? 0.1209 0.1114 0.1233 -0.0099 -0.0115 0.0093  36  VAL   B CG2 
4306 N N   . ASN   B 37  ? 0.1141 0.1071 0.0993 0.0015  -0.0027 0.0015  37  ASN   B N   
4307 C CA  . ASN   B 37  ? 0.1166 0.1068 0.1136 0.0051  -0.0054 0.0054  37  ASN   B CA  
4308 C C   . ASN   B 37  ? 0.1175 0.1078 0.1089 0.0078  -0.0060 -0.0013 37  ASN   B C   
4309 O O   . ASN   B 37  ? 0.1272 0.1159 0.1131 0.0068  0.0002  0.0035  37  ASN   B O   
4310 C CB  . ASN   B 37  ? 0.1187 0.1147 0.1050 0.0032  -0.0083 0.0009  37  ASN   B CB  
4311 C CG  . ASN   B 37  ? 0.1178 0.1137 0.1162 0.0016  -0.0090 -0.0004 37  ASN   B CG  
4312 O OD1 . ASN   B 37  ? 0.1268 0.1216 0.1225 0.0113  -0.0124 -0.0021 37  ASN   B OD1 
4313 N ND2 . ASN   B 37  ? 0.1263 0.1132 0.1185 0.0029  -0.0164 0.0051  37  ASN   B ND2 
4320 N N   . ALA   B 38  ? 0.1216 0.1085 0.1105 0.0084  0.0006  -0.0037 38  ALA   B N   
4321 C CA  . ALA   B 38  ? 0.1297 0.1103 0.1103 -0.0009 0.0059  0.0079  38  ALA   B CA  
4322 C C   . ALA   B 38  ? 0.1228 0.1130 0.1117 0.0043  0.0047  0.0012  38  ALA   B C   
4323 O O   . ALA   B 38  ? 0.1282 0.1200 0.1301 0.0085  0.0010  0.0038  38  ALA   B O   
4324 C CB  . ALA   B 38  ? 0.1567 0.1172 0.1253 -0.0092 0.0091  0.0097  38  ALA   B CB  
4330 N N   . ALA   B 39  ? 0.1222 0.1166 0.1072 0.0090  -0.0043 0.0035  39  ALA   B N   
4331 C CA  . ALA   B 39  ? 0.1312 0.1185 0.1072 0.0034  -0.0060 0.0015  39  ALA   B CA  
4332 C C   . ALA   B 39  ? 0.1318 0.1243 0.0989 0.0036  0.0010  -0.0015 39  ALA   B C   
4333 O O   . ALA   B 39  ? 0.1369 0.1291 0.1211 -0.0004 0.0005  0.0073  39  ALA   B O   
4334 C CB  . ALA   B 39  ? 0.1366 0.1211 0.1264 -0.0053 0.0037  -0.0021 39  ALA   B CB  
4340 N N   . ASN   B 40  ? 0.1378 0.1470 0.1050 -0.0097 0.0036  -0.0108 40  ASN   B N   
4341 C CA  . ASN   B 40  ? 0.1428 0.1551 0.1128 -0.0050 -0.0091 -0.0097 40  ASN   B CA  
4342 C C   . ASN   B 40  ? 0.1424 0.1591 0.0935 0.0041  -0.0092 -0.0062 40  ASN   B C   
4343 O O   . ASN   B 40  ? 0.1428 0.1500 0.1112 0.0064  -0.0127 -0.0044 40  ASN   B O   
4344 C CB  . ASN   B 40  ? 0.1578 0.1553 0.1357 0.0027  -0.0115 0.0062  40  ASN   B CB  
4345 C CG  . ASN   B 40  ? 0.1595 0.1577 0.1676 0.0040  -0.0199 0.0064  40  ASN   B CG  
4346 O OD1 . ASN   B 40  ? 0.1517 0.1563 0.2476 0.0048  -0.0329 0.0093  40  ASN   B OD1 
4347 N ND2 . ASN   B 40  ? 0.1621 0.1593 0.1648 0.0029  -0.0133 0.0080  40  ASN   B ND2 
4354 N N   . VAL   B 41  ? 0.1503 0.1633 0.1009 0.0077  -0.0001 -0.0027 41  VAL   B N   
4355 C CA  . VAL   B 41  ? 0.1560 0.1695 0.1095 0.0162  -0.0006 -0.0149 41  VAL   B CA  
4356 C C   . VAL   B 41  ? 0.1561 0.1717 0.1094 0.0174  -0.0041 -0.0177 41  VAL   B C   
4357 O O   . VAL   B 41  ? 0.1582 0.1706 0.1220 0.0110  -0.0118 -0.0242 41  VAL   B O   
4358 C CB  . VAL   B 41  ? 0.1740 0.1860 0.1300 0.0023  0.0137  -0.0278 41  VAL   B CB  
4359 C CG1 . VAL   B 41  ? 0.1713 0.1929 0.1459 -0.0021 0.0187  -0.0276 41  VAL   B CG1 
4360 C CG2 . VAL   B 41  ? 0.1859 0.2044 0.1396 -0.0025 0.0187  -0.0286 41  VAL   B CG2 
4370 N N   . TYR   B 42  ? 0.1580 0.1677 0.1140 0.0150  -0.0202 -0.0054 42  TYR   B N   
4371 C CA  . TYR   B 42  ? 0.1659 0.1792 0.1350 0.0130  -0.0264 -0.0172 42  TYR   B CA  
4372 C C   . TYR   B 42  ? 0.1502 0.1543 0.1334 0.0183  -0.0203 -0.0197 42  TYR   B C   
4373 O O   . TYR   B 42  ? 0.1574 0.1636 0.1507 0.0104  -0.0249 -0.0278 42  TYR   B O   
4374 C CB  . TYR   B 42  ? 0.1936 0.2144 0.1558 0.0078  -0.0333 -0.0056 42  TYR   B CB  
4375 C CG  . TYR   B 42  ? 0.1985 0.2317 0.1427 0.0008  -0.0344 0.0070  42  TYR   B CG  
4376 C CD1 . TYR   B 42  ? 0.1976 0.2346 0.1169 -0.0042 -0.0208 -0.0097 42  TYR   B CD1 
4377 C CD2 . TYR   B 42  ? 0.2163 0.2453 0.1892 -0.0041 -0.0125 0.0111  42  TYR   B CD2 
4378 C CE1 . TYR   B 42  ? 0.2113 0.2542 0.1259 -0.0007 -0.0127 -0.0032 42  TYR   B CE1 
4379 C CE2 . TYR   B 42  ? 0.2226 0.2595 0.1838 0.0000  0.0058  0.0217  42  TYR   B CE2 
4380 C CZ  . TYR   B 42  ? 0.2309 0.2689 0.1574 0.0104  0.0103  0.0098  42  TYR   B CZ  
4381 O OH  . TYR   B 42  ? 0.2627 0.2874 0.2108 0.0232  0.0280  0.0165  42  TYR   B OH  
4391 N N   . LEU   B 43  ? 0.1445 0.1404 0.1245 0.0090  -0.0160 -0.0168 43  LEU   B N   
4392 C CA  . LEU   B 43  ? 0.1413 0.1372 0.1252 0.0039  -0.0143 -0.0050 43  LEU   B CA  
4393 C C   . LEU   B 43  ? 0.1500 0.1459 0.1254 0.0022  -0.0157 -0.0070 43  LEU   B C   
4394 O O   . LEU   B 43  ? 0.1440 0.1481 0.1505 0.0071  -0.0166 0.0042  43  LEU   B O   
4395 C CB  . LEU   B 43  ? 0.1434 0.1318 0.1265 0.0048  -0.0209 -0.0092 43  LEU   B CB  
4396 C CG  . LEU   B 43  ? 0.1458 0.1299 0.1317 0.0039  -0.0219 -0.0123 43  LEU   B CG  
4397 C CD1 . LEU   B 43  ? 0.1551 0.1351 0.1705 0.0044  -0.0338 -0.0089 43  LEU   B CD1 
4398 C CD2 . LEU   B 43  ? 0.1444 0.1304 0.1433 -0.0032 -0.0214 -0.0129 43  LEU   B CD2 
4410 N N   . LYS   B 44  ? 0.1432 0.1442 0.1230 0.0100  -0.0097 -0.0083 44  LYS   B N   
4411 C CA  . LYS   B 44  ? 0.1540 0.1505 0.1298 0.0080  -0.0129 0.0058  44  LYS   B CA  
4412 C C   . LYS   B 44  ? 0.1449 0.1410 0.1313 0.0117  -0.0110 -0.0001 44  LYS   B C   
4413 O O   . LYS   B 44  ? 0.1624 0.1374 0.1552 0.0018  -0.0052 -0.0041 44  LYS   B O   
4414 C CB  . LYS   B 44  ? 0.1806 0.1722 0.1355 0.0166  -0.0174 0.0070  44  LYS   B CB  
4415 C CG  . LYS   B 44  ? 0.2196 0.1978 0.1760 0.0122  -0.0378 0.0003  44  LYS   B CG  
4416 C CD  . LYS   B 44  ? 0.2500 0.2186 0.2217 -0.0024 -0.0494 -0.0016 44  LYS   B CD  
4417 C CE  . LYS   B 44  ? 0.2794 0.2433 0.2610 -0.0088 -0.0511 0.0054  44  LYS   B CE  
4418 N NZ  . LYS   B 44  ? 0.2938 0.2566 0.2938 -0.0071 -0.0514 0.0133  44  LYS   B NZ  
4432 N N   . HIS   B 45  ? 0.1419 0.1408 0.1162 0.0060  -0.0122 0.0010  45  HIS   B N   
4433 C CA  . HIS   B 45  ? 0.1488 0.1403 0.1305 0.0116  -0.0079 -0.0046 45  HIS   B CA  
4434 C C   . HIS   B 45  ? 0.1776 0.1597 0.1697 0.0168  -0.0173 -0.0112 45  HIS   B C   
4435 O O   . HIS   B 45  ? 0.1840 0.1879 0.2093 0.0436  0.0068  -0.0028 45  HIS   B O   
4436 C CB  . HIS   B 45  ? 0.1383 0.1421 0.1307 0.0000  -0.0068 -0.0027 45  HIS   B CB  
4437 C CG  . HIS   B 45  ? 0.1416 0.1392 0.1226 -0.0054 -0.0063 0.0034  45  HIS   B CG  
4438 N ND1 . HIS   B 45  ? 0.1450 0.1360 0.1381 0.0020  -0.0130 -0.0067 45  HIS   B ND1 
4439 C CD2 . HIS   B 45  ? 0.1512 0.1402 0.1449 -0.0093 -0.0118 0.0035  45  HIS   B CD2 
4440 C CE1 . HIS   B 45  ? 0.1524 0.1307 0.1221 -0.0009 -0.0219 -0.0068 45  HIS   B CE1 
4441 N NE2 . HIS   B 45  ? 0.1568 0.1343 0.1308 0.0003  -0.0201 -0.0045 45  HIS   B NE2 
4449 N N   A GLY   B 46  ? 0.1893 0.1498 0.1889 0.0186  -0.0366 -0.0034 46  GLY   B N   
4450 N N   B GLY   B 46  ? 0.1834 0.1666 0.1848 0.0165  -0.0219 -0.0059 46  GLY   B N   
4451 C CA  A GLY   B 46  ? 0.1980 0.1626 0.2284 0.0205  -0.0474 -0.0033 46  GLY   B CA  
4452 C CA  B GLY   B 46  ? 0.1882 0.1758 0.2033 0.0157  -0.0256 -0.0021 46  GLY   B CA  
4453 C C   A GLY   B 46  ? 0.1935 0.1821 0.2686 0.0277  -0.0433 -0.0042 46  GLY   B C   
4454 C C   B GLY   B 46  ? 0.1902 0.1852 0.2227 0.0158  -0.0263 0.0007  46  GLY   B C   
4455 O O   A GLY   B 46  ? 0.2049 0.2098 0.3549 0.0306  -0.0208 -0.0270 46  GLY   B O   
4456 O O   B GLY   B 46  ? 0.1934 0.1916 0.2318 0.0172  -0.0262 0.0067  46  GLY   B O   
4463 N N   . GLY   B 47  ? 0.1894 0.1903 0.2348 0.0127  -0.0199 -0.0047 47  GLY   B N   
4464 C CA  . GLY   B 47  ? 0.1756 0.1607 0.1906 0.0056  -0.0139 -0.0018 47  GLY   B CA  
4465 C C   . GLY   B 47  ? 0.1563 0.1382 0.1634 0.0082  0.0009  0.0060  47  GLY   B C   
4466 O O   . GLY   B 47  ? 0.1695 0.1286 0.1632 0.0050  -0.0050 0.0101  47  GLY   B O   
4471 N N   . GLY   B 48  ? 0.1403 0.1310 0.1590 0.0070  -0.0085 0.0167  48  GLY   B N   
4472 C CA  . GLY   B 48  ? 0.1415 0.1268 0.1597 0.0025  -0.0024 0.0106  48  GLY   B CA  
4473 C C   . GLY   B 48  ? 0.1364 0.1206 0.1462 0.0008  0.0058  0.0041  48  GLY   B C   
4474 O O   . GLY   B 48  ? 0.1345 0.1278 0.1592 0.0057  -0.0028 0.0045  48  GLY   B O   
4478 N N   . VAL   B 49  ? 0.1394 0.1274 0.1402 0.0113  0.0010  0.0056  49  VAL   B N   
4479 C CA  . VAL   B 49  ? 0.1416 0.1349 0.1339 0.0108  -0.0114 -0.0067 49  VAL   B CA  
4480 C C   . VAL   B 49  ? 0.1332 0.1291 0.1199 0.0144  -0.0022 0.0043  49  VAL   B C   
4481 O O   . VAL   B 49  ? 0.1370 0.1372 0.1298 0.0067  -0.0022 0.0077  49  VAL   B O   
4482 C CB  . VAL   B 49  ? 0.1420 0.1538 0.1622 0.0051  -0.0208 -0.0002 49  VAL   B CB  
4483 C CG1 . VAL   B 49  ? 0.1402 0.1607 0.1504 0.0043  -0.0199 0.0029  49  VAL   B CG1 
4484 C CG2 . VAL   B 49  ? 0.1614 0.1637 0.1862 -0.0028 -0.0376 -0.0011 49  VAL   B CG2 
4494 N N   . ALA   B 50  ? 0.1266 0.1215 0.1229 0.0070  -0.0018 0.0056  50  ALA   B N   
4495 C CA  . ALA   B 50  ? 0.1244 0.1190 0.1279 0.0094  -0.0073 0.0080  50  ALA   B CA  
4496 C C   . ALA   B 50  ? 0.1259 0.1253 0.1242 0.0122  -0.0020 0.0075  50  ALA   B C   
4497 O O   . ALA   B 50  ? 0.1287 0.1276 0.1283 0.0072  -0.0015 0.0008  50  ALA   B O   
4498 C CB  . ALA   B 50  ? 0.1253 0.1148 0.1422 0.0003  0.0032  0.0035  50  ALA   B CB  
4504 N N   . GLY   B 51  ? 0.1252 0.1348 0.1369 0.0124  -0.0122 0.0049  51  GLY   B N   
4505 C CA  . GLY   B 51  ? 0.1326 0.1379 0.1545 0.0180  -0.0148 0.0129  51  GLY   B CA  
4506 C C   . GLY   B 51  ? 0.1302 0.1318 0.1568 0.0190  -0.0070 0.0120  51  GLY   B C   
4507 O O   . GLY   B 51  ? 0.1343 0.1452 0.1721 0.0095  -0.0083 0.0042  51  GLY   B O   
4511 N N   . ALA   B 52  ? 0.1278 0.1256 0.1564 0.0180  0.0006  0.0158  52  ALA   B N   
4512 C CA  . ALA   B 52  ? 0.1351 0.1390 0.1567 0.0205  0.0021  0.0004  52  ALA   B CA  
4513 C C   . ALA   B 52  ? 0.1312 0.1350 0.1382 0.0128  0.0026  0.0062  52  ALA   B C   
4514 O O   . ALA   B 52  ? 0.1342 0.1425 0.1454 0.0146  0.0085  0.0006  52  ALA   B O   
4515 C CB  . ALA   B 52  ? 0.1560 0.1453 0.1584 0.0067  0.0142  0.0015  52  ALA   B CB  
4521 N N   . LEU   B 53  ? 0.1225 0.1306 0.1287 0.0173  0.0033  0.0090  53  LEU   B N   
4522 C CA  . LEU   B 53  ? 0.1233 0.1379 0.1336 0.0139  0.0010  0.0112  53  LEU   B CA  
4523 C C   . LEU   B 53  ? 0.1291 0.1289 0.1381 0.0137  0.0046  0.0149  53  LEU   B C   
4524 O O   . LEU   B 53  ? 0.1337 0.1420 0.1474 0.0040  0.0067  0.0198  53  LEU   B O   
4525 C CB  . LEU   B 53  ? 0.1276 0.1486 0.1398 0.0085  0.0018  0.0176  53  LEU   B CB  
4526 C CG  . LEU   B 53  ? 0.1271 0.1566 0.1452 0.0060  0.0007  0.0226  53  LEU   B CG  
4527 C CD1 . LEU   B 53  ? 0.1309 0.1811 0.1682 0.0158  -0.0052 0.0057  53  LEU   B CD1 
4528 C CD2 . LEU   B 53  ? 0.1405 0.1819 0.1640 -0.0083 -0.0080 -0.0132 53  LEU   B CD2 
4540 N N   . ASN   B 54  ? 0.1272 0.1257 0.1348 0.0062  -0.0003 0.0085  54  ASN   B N   
4541 C CA  . ASN   B 54  ? 0.1315 0.1345 0.1508 0.0045  -0.0036 0.0082  54  ASN   B CA  
4542 C C   . ASN   B 54  ? 0.1281 0.1350 0.1524 0.0059  -0.0006 0.0174  54  ASN   B C   
4543 O O   . ASN   B 54  ? 0.1327 0.1414 0.1668 0.0007  0.0041  0.0053  54  ASN   B O   
4544 C CB  . ASN   B 54  ? 0.1342 0.1436 0.1596 0.0063  0.0048  0.0075  54  ASN   B CB  
4545 C CG  . ASN   B 54  ? 0.1346 0.1557 0.1528 0.0057  -0.0042 0.0022  54  ASN   B CG  
4546 O OD1 . ASN   B 54  ? 0.1300 0.1543 0.1582 0.0003  -0.0077 -0.0077 54  ASN   B OD1 
4547 N ND2 . ASN   B 54  ? 0.1427 0.1744 0.1794 0.0003  -0.0286 0.0131  54  ASN   B ND2 
4554 N N   . LYS   B 55  ? 0.1296 0.1442 0.1704 0.0144  0.0012  0.0080  55  LYS   B N   
4555 C CA  . LYS   B 55  ? 0.1362 0.1584 0.1801 0.0198  -0.0003 0.0104  55  LYS   B CA  
4556 C C   . LYS   B 55  ? 0.1283 0.1584 0.1800 0.0138  0.0060  0.0041  55  LYS   B C   
4557 O O   . LYS   B 55  ? 0.1227 0.1691 0.1901 0.0111  0.0081  -0.0031 55  LYS   B O   
4558 C CB  . LYS   B 55  ? 0.1465 0.1703 0.1944 0.0303  0.0047  0.0235  55  LYS   B CB  
4559 C CG  . LYS   B 55  ? 0.1822 0.1964 0.2765 0.0375  0.0248  0.0290  55  LYS   B CG  
4560 C CD  . LYS   B 55  ? 0.2163 0.2165 0.3455 0.0475  0.0501  0.0273  55  LYS   B CD  
4561 C CE  . LYS   B 55  ? 0.2457 0.2364 0.4081 0.0515  0.0551  0.0291  55  LYS   B CE  
4562 N NZ  . LYS   B 55  ? 0.2576 0.2480 0.4414 0.0497  0.0452  0.0313  55  LYS   B NZ  
4576 N N   . ALA   B 56  ? 0.1253 0.1652 0.1647 0.0121  0.0049  -0.0045 56  ALA   B N   
4577 C CA  . ALA   B 56  ? 0.1411 0.1753 0.1634 0.0081  0.0061  -0.0042 56  ALA   B CA  
4578 C C   . ALA   B 56  ? 0.1421 0.1675 0.1554 0.0080  0.0126  0.0064  56  ALA   B C   
4579 O O   . ALA   B 56  ? 0.1529 0.1814 0.1714 0.0128  0.0277  0.0151  56  ALA   B O   
4580 C CB  . ALA   B 56  ? 0.1544 0.1989 0.1700 -0.0040 -0.0000 -0.0032 56  ALA   B CB  
4586 N N   . THR   B 57  ? 0.1378 0.1561 0.1650 0.0097  0.0136  0.0137  57  THR   B N   
4587 C CA  . THR   B 57  ? 0.1392 0.1556 0.1676 0.0054  0.0191  0.0189  57  THR   B CA  
4588 C C   . THR   B 57  ? 0.1422 0.1676 0.1869 0.0016  0.0225  0.0178  57  THR   B C   
4589 O O   . THR   B 57  ? 0.1463 0.1692 0.1949 -0.0143 0.0210  0.0179  57  THR   B O   
4590 C CB  . THR   B 57  ? 0.1420 0.1455 0.1573 0.0021  0.0152  0.0208  57  THR   B CB  
4591 O OG1 . THR   B 57  ? 0.1424 0.1412 0.1581 0.0029  0.0145  0.0088  57  THR   B OG1 
4592 C CG2 . THR   B 57  ? 0.1392 0.1568 0.1544 0.0003  0.0169  0.0186  57  THR   B CG2 
4600 N N   . ASN   B 58  ? 0.1267 0.1877 0.2090 -0.0105 0.0075  0.0058  58  ASN   B N   
4601 C CA  . ASN   B 58  ? 0.1488 0.2310 0.2461 -0.0147 0.0303  0.0065  58  ASN   B CA  
4602 C C   . ASN   B 58  ? 0.1273 0.2065 0.2113 -0.0102 0.0014  0.0079  58  ASN   B C   
4603 O O   . ASN   B 58  ? 0.1341 0.2146 0.2233 -0.0149 0.0009  0.0066  58  ASN   B O   
4604 C CB  . ASN   B 58  ? 0.2451 0.3114 0.3677 -0.0277 0.0599  0.0134  58  ASN   B CB  
4605 C CG  . ASN   B 58  ? 0.3441 0.3787 0.5107 -0.0315 0.0700  0.0307  58  ASN   B CG  
4606 O OD1 . ASN   B 58  ? 0.4014 0.4014 0.5607 -0.0322 0.0713  0.0363  58  ASN   B OD1 
4607 N ND2 . ASN   B 58  ? 0.4046 0.4046 0.5601 -0.0337 0.0726  0.0344  58  ASN   B ND2 
4614 N N   . ASN   B 59  ? 0.1227 0.1862 0.1926 -0.0094 -0.0035 0.0171  59  ASN   B N   
4615 C CA  . ASN   B 59  ? 0.1284 0.1877 0.1859 -0.0088 -0.0056 0.0213  59  ASN   B CA  
4616 C C   . ASN   B 59  ? 0.1203 0.1811 0.1696 -0.0109 -0.0066 0.0098  59  ASN   B C   
4617 O O   . ASN   B 59  ? 0.1324 0.1811 0.1695 -0.0139 -0.0125 0.0019  59  ASN   B O   
4618 C CB  . ASN   B 59  ? 0.1392 0.2068 0.1978 -0.0013 -0.0225 0.0225  59  ASN   B CB  
4619 C CG  . ASN   B 59  ? 0.1504 0.2219 0.2142 0.0022  -0.0348 0.0145  59  ASN   B CG  
4620 O OD1 . ASN   B 59  ? 0.1571 0.2276 0.2160 0.0022  -0.0240 0.0232  59  ASN   B OD1 
4621 N ND2 . ASN   B 59  ? 0.1598 0.2317 0.2267 -0.0066 -0.0338 0.0104  59  ASN   B ND2 
4628 N N   . ALA   B 60  ? 0.1256 0.1669 0.1749 -0.0086 -0.0032 0.0043  60  ALA   B N   
4629 C CA  . ALA   B 60  ? 0.1369 0.1579 0.1814 -0.0176 0.0012  0.0084  60  ALA   B CA  
4630 C C   . ALA   B 60  ? 0.1359 0.1464 0.1614 -0.0115 -0.0067 0.0101  60  ALA   B C   
4631 O O   . ALA   B 60  ? 0.1396 0.1499 0.1698 -0.0126 -0.0039 -0.0017 60  ALA   B O   
4632 C CB  . ALA   B 60  ? 0.1488 0.1579 0.1973 -0.0132 0.0083  0.0098  60  ALA   B CB  
4638 N N   . MET   B 61  ? 0.1227 0.1398 0.1637 -0.0079 -0.0042 0.0098  61  MET   B N   
4639 C CA  . MET   B 61  ? 0.1234 0.1367 0.1647 -0.0054 -0.0085 0.0018  61  MET   B CA  
4640 C C   . MET   B 61  ? 0.1308 0.1303 0.1566 -0.0078 -0.0087 0.0054  61  MET   B C   
4641 O O   . MET   B 61  ? 0.1375 0.1338 0.1441 -0.0017 -0.0070 -0.0025 61  MET   B O   
4642 C CB  . MET   B 61  ? 0.1215 0.1418 0.1448 0.0025  -0.0087 -0.0031 61  MET   B CB  
4643 C CG  . MET   B 61  ? 0.1290 0.1417 0.1352 0.0030  -0.0063 -0.0035 61  MET   B CG  
4644 S SD  . MET   B 61  ? 0.1268 0.1420 0.1710 -0.0012 -0.0023 -0.0098 61  MET   B SD  
4645 C CE  . MET   B 61  ? 0.1350 0.1613 0.1914 -0.0010 -0.0006 -0.0128 61  MET   B CE  
4655 N N   . GLN   B 62  ? 0.1320 0.1382 0.1472 -0.0024 -0.0078 0.0057  62  GLN   B N   
4656 C CA  . GLN   B 62  ? 0.1303 0.1424 0.1514 -0.0020 -0.0097 0.0014  62  GLN   B CA  
4657 C C   . GLN   B 62  ? 0.1323 0.1484 0.1540 -0.0074 -0.0180 -0.0068 62  GLN   B C   
4658 O O   . GLN   B 62  ? 0.1455 0.1488 0.1567 -0.0010 -0.0227 -0.0178 62  GLN   B O   
4659 C CB  . GLN   B 62  ? 0.1369 0.1482 0.1488 -0.0018 -0.0131 0.0062  62  GLN   B CB  
4660 C CG  . GLN   B 62  ? 0.1308 0.1538 0.1569 0.0021  -0.0228 0.0021  62  GLN   B CG  
4661 C CD  . GLN   B 62  ? 0.1375 0.1500 0.1508 0.0039  -0.0246 0.0069  62  GLN   B CD  
4662 O OE1 . GLN   B 62  ? 0.1417 0.1461 0.1612 -0.0014 -0.0222 -0.0067 62  GLN   B OE1 
4663 N NE2 . GLN   B 62  ? 0.1369 0.1577 0.1592 -0.0011 -0.0247 -0.0065 62  GLN   B NE2 
4672 N N   . VAL   B 63  ? 0.1357 0.1550 0.1712 -0.0114 -0.0162 -0.0064 63  VAL   B N   
4673 C CA  . VAL   B 63  ? 0.1459 0.1533 0.1912 -0.0176 -0.0235 -0.0098 63  VAL   B CA  
4674 C C   . VAL   B 63  ? 0.1473 0.1420 0.1786 -0.0176 -0.0264 -0.0151 63  VAL   B C   
4675 O O   . VAL   B 63  ? 0.1571 0.1414 0.2004 -0.0092 -0.0381 -0.0158 63  VAL   B O   
4676 C CB  . VAL   B 63  ? 0.1531 0.1674 0.2265 -0.0228 -0.0213 -0.0071 63  VAL   B CB  
4677 C CG1 . VAL   B 63  ? 0.1616 0.1729 0.2373 -0.0289 -0.0167 -0.0060 63  VAL   B CG1 
4678 C CG2 . VAL   B 63  ? 0.1494 0.1809 0.2473 -0.0182 -0.0251 -0.0098 63  VAL   B CG2 
4688 N N   . GLU   B 64  ? 0.1495 0.1353 0.1774 -0.0080 -0.0181 -0.0112 64  GLU   B N   
4689 C CA  . GLU   B 64  ? 0.1486 0.1266 0.1643 -0.0098 -0.0241 -0.0149 64  GLU   B CA  
4690 C C   . GLU   B 64  ? 0.1438 0.1269 0.1503 -0.0073 -0.0193 -0.0174 64  GLU   B C   
4691 O O   . GLU   B 64  ? 0.1536 0.1431 0.1591 -0.0081 -0.0174 -0.0148 64  GLU   B O   
4692 C CB  . GLU   B 64  ? 0.1492 0.1394 0.1662 -0.0136 -0.0186 -0.0073 64  GLU   B CB  
4693 C CG  . GLU   B 64  ? 0.1509 0.1462 0.1656 -0.0218 -0.0214 -0.0164 64  GLU   B CG  
4694 C CD  . GLU   B 64  ? 0.1581 0.1603 0.1763 -0.0316 -0.0299 -0.0161 64  GLU   B CD  
4695 O OE1 . GLU   B 64  ? 0.1579 0.1785 0.1832 -0.0346 -0.0212 -0.0302 64  GLU   B OE1 
4696 O OE2 . GLU   B 64  ? 0.1733 0.1743 0.1741 -0.0297 -0.0433 -0.0163 64  GLU   B OE2 
4703 N N   . SER   B 65  ? 0.1402 0.1263 0.1599 -0.0090 -0.0093 -0.0161 65  SER   B N   
4704 C CA  . SER   B 65  ? 0.1404 0.1260 0.1626 -0.0050 -0.0141 -0.0171 65  SER   B CA  
4705 C C   . SER   B 65  ? 0.1407 0.1341 0.1505 -0.0005 -0.0197 -0.0201 65  SER   B C   
4706 O O   . SER   B 65  ? 0.1498 0.1392 0.1570 -0.0023 -0.0185 -0.0270 65  SER   B O   
4707 C CB  . SER   B 65  ? 0.1420 0.1368 0.1575 -0.0087 -0.0110 -0.0157 65  SER   B CB  
4708 O OG  . SER   B 65  ? 0.1463 0.1365 0.1583 -0.0077 -0.0117 -0.0237 65  SER   B OG  
4714 N N   . ASP   B 66  ? 0.1466 0.1394 0.1575 0.0001  -0.0221 -0.0208 66  ASP   B N   
4715 C CA  . ASP   B 66  ? 0.1579 0.1474 0.1623 0.0041  -0.0286 -0.0215 66  ASP   B CA  
4716 C C   . ASP   B 66  ? 0.1607 0.1528 0.1567 -0.0029 -0.0234 -0.0224 66  ASP   B C   
4717 O O   . ASP   B 66  ? 0.1631 0.1541 0.1642 0.0058  -0.0279 -0.0300 66  ASP   B O   
4718 C CB  . ASP   B 66  ? 0.1791 0.1641 0.1815 0.0166  -0.0412 -0.0264 66  ASP   B CB  
4719 C CG  . ASP   B 66  ? 0.2051 0.1800 0.2051 0.0247  -0.0547 -0.0093 66  ASP   B CG  
4720 O OD1 . ASP   B 66  ? 0.2266 0.1780 0.2000 0.0120  -0.0490 -0.0086 66  ASP   B OD1 
4721 O OD2 . ASP   B 66  ? 0.2207 0.2041 0.2649 0.0394  -0.0521 -0.0114 66  ASP   B OD2 
4726 N N   . ASP   B 67  ? 0.1607 0.1458 0.1499 -0.0080 -0.0216 -0.0172 67  ASP   B N   
4727 C CA  . ASP   B 67  ? 0.1731 0.1431 0.1603 -0.0120 -0.0215 -0.0158 67  ASP   B CA  
4728 C C   . ASP   B 67  ? 0.1659 0.1389 0.1667 0.0005  -0.0199 -0.0178 67  ASP   B C   
4729 O O   . ASP   B 67  ? 0.1741 0.1437 0.1828 -0.0011 -0.0156 -0.0236 67  ASP   B O   
4730 C CB  . ASP   B 67  ? 0.2004 0.1543 0.1789 -0.0154 -0.0343 -0.0153 67  ASP   B CB  
4731 C CG  . ASP   B 67  ? 0.2342 0.1625 0.1838 -0.0097 -0.0582 -0.0159 67  ASP   B CG  
4732 O OD1 . ASP   B 67  ? 0.2544 0.1660 0.1905 -0.0160 -0.0620 -0.0043 67  ASP   B OD1 
4733 O OD2 . ASP   B 67  ? 0.2509 0.1700 0.2055 0.0015  -0.0704 -0.0132 67  ASP   B OD2 
4738 N N   . TYR   B 68  ? 0.1601 0.1450 0.1550 0.0023  -0.0310 -0.0256 68  TYR   B N   
4739 C CA  . TYR   B 68  ? 0.1618 0.1568 0.1693 0.0052  -0.0375 -0.0366 68  TYR   B CA  
4740 C C   . TYR   B 68  ? 0.1538 0.1549 0.1613 0.0050  -0.0347 -0.0417 68  TYR   B C   
4741 O O   . TYR   B 68  ? 0.1521 0.1632 0.1768 0.0056  -0.0302 -0.0533 68  TYR   B O   
4742 C CB  . TYR   B 68  ? 0.1658 0.1798 0.1808 0.0104  -0.0397 -0.0439 68  TYR   B CB  
4743 C CG  . TYR   B 68  ? 0.1758 0.1926 0.1861 0.0154  -0.0357 -0.0674 68  TYR   B CG  
4744 C CD1 . TYR   B 68  ? 0.1756 0.1948 0.2137 -0.0036 -0.0369 -0.0769 68  TYR   B CD1 
4745 C CD2 . TYR   B 68  ? 0.1789 0.2087 0.2032 0.0235  -0.0400 -0.0577 68  TYR   B CD2 
4746 C CE1 . TYR   B 68  ? 0.1802 0.2083 0.2316 -0.0025 -0.0357 -0.0708 68  TYR   B CE1 
4747 C CE2 . TYR   B 68  ? 0.1860 0.2108 0.2121 0.0189  -0.0310 -0.0654 68  TYR   B CE2 
4748 C CZ  . TYR   B 68  ? 0.1783 0.2125 0.2273 0.0038  -0.0346 -0.0717 68  TYR   B CZ  
4749 O OH  . TYR   B 68  ? 0.1750 0.2323 0.2451 0.0022  -0.0371 -0.0584 68  TYR   B OH  
4759 N N   . ILE   B 69  ? 0.1539 0.1446 0.1656 0.0036  -0.0327 -0.0352 69  ILE   B N   
4760 C CA  . ILE   B 69  ? 0.1625 0.1499 0.1738 -0.0029 -0.0243 -0.0407 69  ILE   B CA  
4761 C C   . ILE   B 69  ? 0.1635 0.1483 0.1623 0.0091  -0.0349 -0.0338 69  ILE   B C   
4762 O O   . ILE   B 69  ? 0.1670 0.1619 0.1654 0.0087  -0.0242 -0.0411 69  ILE   B O   
4763 C CB  . ILE   B 69  ? 0.1690 0.1570 0.2024 -0.0054 -0.0046 -0.0336 69  ILE   B CB  
4764 C CG1 . ILE   B 69  ? 0.1693 0.1532 0.2064 -0.0065 0.0030  -0.0417 69  ILE   B CG1 
4765 C CG2 . ILE   B 69  ? 0.1823 0.1658 0.2233 -0.0031 -0.0018 -0.0303 69  ILE   B CG2 
4766 C CD1 . ILE   B 69  ? 0.1625 0.1595 0.2154 -0.0136 0.0007  -0.0399 69  ILE   B CD1 
4778 N N   . ALA   B 70  ? 0.1603 0.1474 0.1628 0.0089  -0.0383 -0.0290 70  ALA   B N   
4779 C CA  . ALA   B 70  ? 0.1661 0.1518 0.1572 0.0053  -0.0397 -0.0240 70  ALA   B CA  
4780 C C   . ALA   B 70  ? 0.1677 0.1494 0.1526 -0.0008 -0.0462 -0.0341 70  ALA   B C   
4781 O O   . ALA   B 70  ? 0.1764 0.1536 0.1576 0.0032  -0.0414 -0.0404 70  ALA   B O   
4782 C CB  . ALA   B 70  ? 0.1652 0.1678 0.1716 -0.0002 -0.0438 -0.0242 70  ALA   B CB  
4788 N N   . THR   B 71  ? 0.1720 0.1527 0.1674 0.0023  -0.0512 -0.0364 71  THR   B N   
4789 C CA  . THR   B 71  ? 0.1867 0.1577 0.1915 0.0085  -0.0659 -0.0349 71  THR   B CA  
4790 C C   . THR   B 71  ? 0.1808 0.1614 0.2082 0.0260  -0.0609 -0.0515 71  THR   B C   
4791 O O   . THR   B 71  ? 0.1922 0.1703 0.2428 0.0246  -0.0559 -0.0741 71  THR   B O   
4792 C CB  . THR   B 71  ? 0.2126 0.1821 0.2192 -0.0034 -0.0779 -0.0162 71  THR   B CB  
4793 O OG1 . THR   B 71  ? 0.2251 0.2096 0.2560 -0.0176 -0.0738 0.0081  71  THR   B OG1 
4794 C CG2 . THR   B 71  ? 0.2307 0.1857 0.2408 0.0042  -0.0741 0.0034  71  THR   B CG2 
4802 N N   . ASN   B 72  ? 0.1684 0.1622 0.2087 0.0161  -0.0549 -0.0696 72  ASN   B N   
4803 C CA  . ASN   B 72  ? 0.1688 0.1795 0.2116 0.0184  -0.0475 -0.0740 72  ASN   B CA  
4804 C C   . ASN   B 72  ? 0.1676 0.1901 0.2131 0.0034  -0.0253 -0.0790 72  ASN   B C   
4805 O O   . ASN   B 72  ? 0.1678 0.2077 0.2375 0.0077  -0.0105 -0.0742 72  ASN   B O   
4806 C CB  . ASN   B 72  ? 0.1771 0.1967 0.2212 0.0170  -0.0606 -0.0678 72  ASN   B CB  
4807 C CG  . ASN   B 72  ? 0.1911 0.2122 0.2398 0.0308  -0.0649 -0.0409 72  ASN   B CG  
4808 O OD1 . ASN   B 72  ? 0.2147 0.2299 0.2402 0.0164  -0.0494 -0.0487 72  ASN   B OD1 
4809 N ND2 . ASN   B 72  ? 0.2031 0.2133 0.2775 0.0484  -0.0494 -0.0063 72  ASN   B ND2 
4816 N N   . GLY   B 73  ? 0.1694 0.1945 0.1917 0.0017  -0.0258 -0.0702 73  GLY   B N   
4817 C CA  . GLY   B 73  ? 0.1639 0.1987 0.1656 -0.0014 -0.0240 -0.0576 73  GLY   B CA  
4818 C C   . GLY   B 73  ? 0.1594 0.1967 0.1300 0.0049  -0.0194 -0.0534 73  GLY   B C   
4819 O O   . GLY   B 73  ? 0.1580 0.1841 0.1474 0.0080  -0.0184 -0.0435 73  GLY   B O   
4823 N N   . PRO   B 74  ? 0.1628 0.2050 0.1252 0.0050  -0.0239 -0.0412 74  PRO   B N   
4824 C CA  . PRO   B 74  ? 0.1564 0.2038 0.1313 0.0090  -0.0219 -0.0286 74  PRO   B CA  
4825 C C   . PRO   B 74  ? 0.1439 0.1892 0.1294 0.0098  -0.0210 -0.0286 74  PRO   B C   
4826 O O   . PRO   B 74  ? 0.1476 0.1887 0.1655 0.0126  -0.0183 -0.0392 74  PRO   B O   
4827 C CB  . PRO   B 74  ? 0.1751 0.2215 0.1295 0.0091  -0.0211 -0.0242 74  PRO   B CB  
4828 C CG  . PRO   B 74  ? 0.1913 0.2297 0.1552 0.0056  -0.0134 -0.0276 74  PRO   B CG  
4829 C CD  . PRO   B 74  ? 0.1868 0.2229 0.1451 0.0058  -0.0140 -0.0389 74  PRO   B CD  
4837 N N   . LEU   B 75  ? 0.1385 0.1771 0.1123 0.0092  -0.0219 -0.0250 75  LEU   B N   
4838 C CA  . LEU   B 75  ? 0.1416 0.1729 0.1206 0.0028  -0.0186 -0.0164 75  LEU   B CA  
4839 C C   . LEU   B 75  ? 0.1441 0.1794 0.1237 0.0068  -0.0137 -0.0133 75  LEU   B C   
4840 O O   . LEU   B 75  ? 0.1621 0.1919 0.1335 0.0019  -0.0088 -0.0045 75  LEU   B O   
4841 C CB  . LEU   B 75  ? 0.1493 0.1743 0.1176 -0.0048 -0.0238 -0.0019 75  LEU   B CB  
4842 C CG  . LEU   B 75  ? 0.1839 0.1911 0.1366 -0.0313 -0.0113 -0.0077 75  LEU   B CG  
4843 C CD1 . LEU   B 75  ? 0.2186 0.2028 0.1371 -0.0395 0.0075  -0.0121 75  LEU   B CD1 
4844 C CD2 . LEU   B 75  ? 0.2124 0.2087 0.2020 -0.0269 0.0016  0.0004  75  LEU   B CD2 
4856 N N   . LYS   B 76  ? 0.1427 0.2010 0.1391 -0.0012 -0.0072 -0.0120 76  LYS   B N   
4857 C CA  . LYS   B 76  ? 0.1545 0.2104 0.1650 -0.0065 0.0127  -0.0193 76  LYS   B CA  
4858 C C   . LYS   B 76  ? 0.1452 0.1905 0.1273 0.0037  0.0006  0.0004  76  LYS   B C   
4859 O O   . LYS   B 76  ? 0.1480 0.1746 0.1298 0.0035  -0.0007 0.0029  76  LYS   B O   
4860 C CB  . LYS   B 76  ? 0.1734 0.2231 0.2586 -0.0081 0.0412  -0.0528 76  LYS   B CB  
4861 C CG  . LYS   B 76  ? 0.1839 0.2385 0.3175 0.0044  0.0321  -0.0672 76  LYS   B CG  
4862 C CD  . LYS   B 76  ? 0.1825 0.2501 0.3698 0.0121  0.0170  -0.0862 76  LYS   B CD  
4863 C CE  . LYS   B 76  ? 0.1903 0.2652 0.4174 0.0170  0.0031  -0.1008 76  LYS   B CE  
4864 N NZ  . LYS   B 76  ? 0.1915 0.2706 0.4386 0.0135  -0.0191 -0.1211 76  LYS   B NZ  
4878 N N   . VAL   B 77  ? 0.1553 0.1963 0.1137 0.0198  0.0019  0.0063  77  VAL   B N   
4879 C CA  . VAL   B 77  ? 0.1559 0.1826 0.1278 0.0210  0.0154  0.0210  77  VAL   B CA  
4880 C C   . VAL   B 77  ? 0.1447 0.1636 0.1161 0.0240  0.0066  0.0166  77  VAL   B C   
4881 O O   . VAL   B 77  ? 0.1463 0.1657 0.1322 0.0279  0.0194  0.0133  77  VAL   B O   
4882 C CB  . VAL   B 77  ? 0.1634 0.1891 0.1479 0.0230  0.0228  0.0395  77  VAL   B CB  
4883 C CG1 . VAL   B 77  ? 0.1707 0.1767 0.1891 0.0138  0.0268  0.0499  77  VAL   B CG1 
4884 C CG2 . VAL   B 77  ? 0.1792 0.2111 0.1699 0.0240  0.0129  0.0467  77  VAL   B CG2 
4894 N N   . GLY   B 78  ? 0.1460 0.1565 0.1154 0.0162  0.0083  0.0134  78  GLY   B N   
4895 C CA  . GLY   B 78  ? 0.1365 0.1498 0.1210 0.0119  0.0182  0.0054  78  GLY   B CA  
4896 C C   . GLY   B 78  ? 0.1310 0.1454 0.1159 0.0106  0.0118  0.0027  78  GLY   B C   
4897 O O   . GLY   B 78  ? 0.1386 0.1478 0.1313 0.0168  0.0088  0.0076  78  GLY   B O   
4901 N N   . GLY   B 79  ? 0.1282 0.1532 0.1193 0.0125  0.0157  0.0054  79  GLY   B N   
4902 C CA  . GLY   B 79  ? 0.1308 0.1453 0.1235 0.0102  0.0127  -0.0051 79  GLY   B CA  
4903 C C   . GLY   B 79  ? 0.1286 0.1306 0.1226 0.0136  0.0056  -0.0069 79  GLY   B C   
4904 O O   . GLY   B 79  ? 0.1335 0.1328 0.1295 0.0131  0.0151  0.0049  79  GLY   B O   
4908 N N   . SER   B 80  ? 0.1294 0.1260 0.1408 0.0078  0.0126  -0.0078 80  SER   B N   
4909 C CA  . SER   B 80  ? 0.1260 0.1229 0.1349 0.0075  0.0038  -0.0057 80  SER   B CA  
4910 C C   . SER   B 80  ? 0.1247 0.1282 0.1332 0.0111  -0.0081 -0.0078 80  SER   B C   
4911 O O   . SER   B 80  ? 0.1381 0.1312 0.1640 0.0106  0.0024  -0.0146 80  SER   B O   
4912 C CB  . SER   B 80  ? 0.1287 0.1292 0.1500 -0.0038 -0.0019 -0.0050 80  SER   B CB  
4913 O OG  . SER   B 80  ? 0.1362 0.1437 0.1651 0.0011  -0.0154 0.0068  80  SER   B OG  
4919 N N   . CYS   B 81  ? 0.1236 0.1132 0.1392 0.0021  -0.0023 -0.0130 81  CYS   B N   
4920 C CA  . CYS   B 81  ? 0.1299 0.1120 0.1462 0.0036  -0.0073 -0.0122 81  CYS   B CA  
4921 C C   . CYS   B 81  ? 0.1258 0.1089 0.1264 0.0033  -0.0151 -0.0113 81  CYS   B C   
4922 O O   . CYS   B 81  ? 0.1518 0.1137 0.1329 0.0094  -0.0043 -0.0137 81  CYS   B O   
4923 C CB  . CYS   B 81  ? 0.1471 0.1268 0.1441 -0.0066 -0.0119 -0.0089 81  CYS   B CB  
4924 S SG  . CYS   B 81  ? 0.1471 0.1437 0.1368 -0.0035 -0.0260 -0.0147 81  CYS   B SG  
4930 N N   . VAL   B 82  ? 0.1323 0.1095 0.1339 0.0031  -0.0108 -0.0133 82  VAL   B N   
4931 C CA  . VAL   B 82  ? 0.1361 0.1114 0.1383 -0.0030 -0.0095 -0.0082 82  VAL   B CA  
4932 C C   . VAL   B 82  ? 0.1423 0.1068 0.1449 0.0023  -0.0101 -0.0076 82  VAL   B C   
4933 O O   . VAL   B 82  ? 0.1482 0.1101 0.1787 0.0011  -0.0067 -0.0231 82  VAL   B O   
4934 C CB  . VAL   B 82  ? 0.1433 0.1372 0.1498 -0.0006 -0.0141 0.0027  82  VAL   B CB  
4935 C CG1 . VAL   B 82  ? 0.1599 0.1585 0.1573 0.0028  -0.0094 0.0131  82  VAL   B CG1 
4936 C CG2 . VAL   B 82  ? 0.1505 0.1483 0.1584 -0.0030 -0.0257 0.0054  82  VAL   B CG2 
4946 N N   . LEU   B 83  ? 0.1327 0.1064 0.1482 -0.0109 -0.0177 -0.0075 83  LEU   B N   
4947 C CA  . LEU   B 83  ? 0.1299 0.1091 0.1399 -0.0108 -0.0182 -0.0048 83  LEU   B CA  
4948 C C   . LEU   B 83  ? 0.1316 0.1107 0.1466 -0.0135 -0.0163 -0.0017 83  LEU   B C   
4949 O O   . LEU   B 83  ? 0.1361 0.1185 0.1344 -0.0149 -0.0144 0.0038  83  LEU   B O   
4950 C CB  . LEU   B 83  ? 0.1367 0.1240 0.1449 -0.0130 -0.0225 -0.0160 83  LEU   B CB  
4951 C CG  . LEU   B 83  ? 0.1513 0.1490 0.1543 -0.0129 -0.0089 -0.0199 83  LEU   B CG  
4952 C CD1 . LEU   B 83  ? 0.1644 0.1590 0.1494 -0.0056 -0.0216 -0.0045 83  LEU   B CD1 
4953 C CD2 . LEU   B 83  ? 0.1683 0.1593 0.1711 -0.0048 0.0001  -0.0296 83  LEU   B CD2 
4965 N N   . SER   B 84  ? 0.1355 0.1225 0.1596 -0.0157 -0.0105 0.0030  84  SER   B N   
4966 C CA  . SER   B 84  ? 0.1410 0.1407 0.1539 -0.0225 -0.0125 0.0130  84  SER   B CA  
4967 C C   . SER   B 84  ? 0.1305 0.1594 0.1167 -0.0135 -0.0145 0.0161  84  SER   B C   
4968 O O   . SER   B 84  ? 0.1410 0.1436 0.1179 -0.0140 -0.0098 0.0026  84  SER   B O   
4969 C CB  . SER   B 84  ? 0.1614 0.1456 0.2030 -0.0232 0.0141  0.0132  84  SER   B CB  
4970 O OG  . SER   B 84  ? 0.1664 0.1574 0.2507 -0.0310 0.0206  0.0220  84  SER   B OG  
4976 N N   . GLY   B 85  ? 0.1338 0.1834 0.1310 -0.0194 -0.0113 0.0162  85  GLY   B N   
4977 C CA  . GLY   B 85  ? 0.1351 0.1914 0.1426 -0.0307 0.0031  -0.0101 85  GLY   B CA  
4978 C C   . GLY   B 85  ? 0.1335 0.1683 0.1396 -0.0392 -0.0029 0.0040  85  GLY   B C   
4979 O O   . GLY   B 85  ? 0.1454 0.1717 0.1327 -0.0536 0.0125  -0.0065 85  GLY   B O   
4983 N N   . HIS   B 86  ? 0.1347 0.1476 0.1429 -0.0289 -0.0180 0.0159  86  HIS   B N   
4984 C CA  . HIS   B 86  ? 0.1321 0.1470 0.1555 -0.0337 -0.0163 0.0196  86  HIS   B CA  
4985 C C   . HIS   B 86  ? 0.1321 0.1606 0.1487 -0.0412 -0.0099 0.0397  86  HIS   B C   
4986 O O   . HIS   B 86  ? 0.1467 0.1672 0.1507 -0.0324 -0.0016 0.0348  86  HIS   B O   
4987 C CB  . HIS   B 86  ? 0.1397 0.1433 0.1483 -0.0164 -0.0201 0.0098  86  HIS   B CB  
4988 C CG  . HIS   B 86  ? 0.1462 0.1523 0.1484 -0.0103 -0.0199 0.0112  86  HIS   B CG  
4989 N ND1 . HIS   B 86  ? 0.1628 0.1740 0.1629 -0.0213 -0.0265 0.0005  86  HIS   B ND1 
4990 C CD2 . HIS   B 86  ? 0.1457 0.1612 0.1522 -0.0101 -0.0211 0.0125  86  HIS   B CD2 
4991 C CE1 . HIS   B 86  ? 0.1677 0.1783 0.1551 -0.0138 -0.0131 -0.0117 86  HIS   B CE1 
4992 N NE2 . HIS   B 86  ? 0.1603 0.1700 0.1453 0.0009  -0.0145 -0.0022 86  HIS   B NE2 
5000 N N   . ASN   B 87  ? 0.1383 0.1641 0.1444 -0.0344 -0.0042 0.0385  87  ASN   B N   
5001 C CA  . ASN   B 87  ? 0.1382 0.1818 0.1472 -0.0288 0.0166  0.0277  87  ASN   B CA  
5002 C C   . ASN   B 87  ? 0.1540 0.1679 0.1292 -0.0267 0.0263  0.0235  87  ASN   B C   
5003 O O   . ASN   B 87  ? 0.1755 0.1763 0.1656 -0.0254 0.0432  0.0152  87  ASN   B O   
5004 C CB  . ASN   B 87  ? 0.1439 0.2171 0.1775 -0.0252 0.0224  0.0164  87  ASN   B CB  
5005 C CG  . ASN   B 87  ? 0.1509 0.2342 0.1931 0.0053  0.0282  0.0311  87  ASN   B CG  
5006 O OD1 . ASN   B 87  ? 0.1420 0.2152 0.1852 0.0107  0.0379  0.0482  87  ASN   B OD1 
5007 N ND2 . ASN   B 87  ? 0.1855 0.2466 0.2223 0.0045  0.0302  0.0273  87  ASN   B ND2 
5014 N N   . LEU   B 88  ? 0.1457 0.1587 0.1234 -0.0302 0.0163  0.0120  88  LEU   B N   
5015 C CA  . LEU   B 88  ? 0.1499 0.1500 0.1285 -0.0268 0.0040  0.0020  88  LEU   B CA  
5016 C C   . LEU   B 88  ? 0.1511 0.1378 0.1235 -0.0294 -0.0003 0.0045  88  LEU   B C   
5017 O O   . LEU   B 88  ? 0.1746 0.1466 0.1595 -0.0195 -0.0258 -0.0033 88  LEU   B O   
5018 C CB  . LEU   B 88  ? 0.1584 0.1530 0.1520 -0.0318 -0.0070 0.0174  88  LEU   B CB  
5019 C CG  . LEU   B 88  ? 0.1933 0.1824 0.1716 -0.0309 -0.0281 0.0452  88  LEU   B CG  
5020 C CD1 . LEU   B 88  ? 0.2044 0.2151 0.1871 -0.0403 -0.0181 0.0545  88  LEU   B CD1 
5021 C CD2 . LEU   B 88  ? 0.2283 0.2082 0.2267 0.0071  -0.0536 0.0264  88  LEU   B CD2 
5033 N N   . ALA   B 89  ? 0.1419 0.1357 0.1250 -0.0303 0.0145  0.0048  89  ALA   B N   
5034 C CA  . ALA   B 89  ? 0.1430 0.1321 0.1090 -0.0304 0.0028  0.0069  89  ALA   B CA  
5035 C C   . ALA   B 89  ? 0.1489 0.1353 0.1081 -0.0366 0.0132  0.0088  89  ALA   B C   
5036 O O   . ALA   B 89  ? 0.1362 0.1460 0.1507 -0.0350 0.0111  -0.0238 89  ALA   B O   
5037 C CB  . ALA   B 89  ? 0.1346 0.1298 0.1327 -0.0341 0.0064  0.0157  89  ALA   B CB  
5043 N N   . LYS   B 90  ? 0.1779 0.1291 0.1182 -0.0371 -0.0044 0.0087  90  LYS   B N   
5044 C CA  . LYS   B 90  ? 0.1966 0.1214 0.1282 -0.0352 -0.0045 0.0054  90  LYS   B CA  
5045 C C   . LYS   B 90  ? 0.1875 0.1124 0.1401 -0.0422 -0.0056 -0.0057 90  LYS   B C   
5046 O O   . LYS   B 90  ? 0.2018 0.1386 0.1644 -0.0590 0.0041  -0.0055 90  LYS   B O   
5047 C CB  . LYS   B 90  ? 0.2173 0.1286 0.1523 -0.0274 0.0043  0.0161  90  LYS   B CB  
5048 C CG  . LYS   B 90  ? 0.2229 0.1439 0.1658 -0.0117 0.0310  0.0192  90  LYS   B CG  
5049 C CD  . LYS   B 90  ? 0.2505 0.1733 0.2170 -0.0107 0.0449  0.0024  90  LYS   B CD  
5050 C CE  . LYS   B 90  ? 0.2643 0.1932 0.2681 -0.0183 0.0512  -0.0068 90  LYS   B CE  
5051 N NZ  . LYS   B 90  ? 0.2689 0.1924 0.2769 -0.0309 0.0559  -0.0085 90  LYS   B NZ  
5065 N N   . HIS   B 91  ? 0.1568 0.1093 0.1192 -0.0262 -0.0173 -0.0027 91  HIS   B N   
5066 C CA  . HIS   B 91  ? 0.1444 0.1136 0.1205 -0.0186 -0.0073 -0.0039 91  HIS   B CA  
5067 C C   . HIS   B 91  ? 0.1321 0.1162 0.1120 -0.0251 -0.0089 0.0017  91  HIS   B C   
5068 O O   . HIS   B 91  ? 0.1511 0.1197 0.1125 -0.0213 -0.0162 -0.0008 91  HIS   B O   
5069 C CB  . HIS   B 91  ? 0.1654 0.1166 0.1616 -0.0032 -0.0007 0.0090  91  HIS   B CB  
5070 C CG  . HIS   B 91  ? 0.2089 0.1371 0.2391 0.0068  0.0276  0.0271  91  HIS   B CG  
5071 N ND1 . HIS   B 91  ? 0.2407 0.1480 0.2940 0.0043  0.0363  0.0125  91  HIS   B ND1 
5072 C CD2 . HIS   B 91  ? 0.2283 0.1664 0.2886 0.0220  0.0130  0.0597  91  HIS   B CD2 
5073 C CE1 . HIS   B 91  ? 0.2466 0.1597 0.3150 0.0244  0.0334  0.0294  91  HIS   B CE1 
5074 N NE2 . HIS   B 91  ? 0.2379 0.1754 0.3154 0.0379  0.0259  0.0678  91  HIS   B NE2 
5082 N N   . CYS   B 92  ? 0.1275 0.1146 0.1156 -0.0235 -0.0159 -0.0005 92  CYS   B N   
5083 C CA  . CYS   B 92  ? 0.1223 0.1102 0.1105 -0.0150 -0.0096 0.0016  92  CYS   B CA  
5084 C C   . CYS   B 92  ? 0.1222 0.1044 0.1071 -0.0068 -0.0088 0.0026  92  CYS   B C   
5085 O O   . CYS   B 92  ? 0.1270 0.1136 0.1324 -0.0126 -0.0030 -0.0089 92  CYS   B O   
5086 C CB  . CYS   B 92  ? 0.1254 0.1200 0.1211 -0.0100 -0.0027 0.0042  92  CYS   B CB  
5087 S SG  . CYS   B 92  ? 0.1264 0.1223 0.1266 -0.0084 -0.0109 0.0050  92  CYS   B SG  
5093 N N   . LEU   B 93  ? 0.1146 0.1136 0.1025 -0.0096 -0.0006 -0.0054 93  LEU   B N   
5094 C CA  . LEU   B 93  ? 0.1196 0.1109 0.1112 -0.0019 -0.0049 -0.0021 93  LEU   B CA  
5095 C C   . LEU   B 93  ? 0.1096 0.1066 0.1021 0.0002  -0.0043 0.0013  93  LEU   B C   
5096 O O   . LEU   B 93  ? 0.1184 0.1091 0.1067 -0.0034 -0.0028 -0.0007 93  LEU   B O   
5097 C CB  . LEU   B 93  ? 0.1176 0.1111 0.1234 -0.0013 -0.0040 -0.0014 93  LEU   B CB  
5098 C CG  . LEU   B 93  ? 0.1171 0.1234 0.1351 0.0009  -0.0002 0.0050  93  LEU   B CG  
5099 C CD1 . LEU   B 93  ? 0.1232 0.1317 0.1290 0.0067  -0.0032 -0.0090 93  LEU   B CD1 
5100 C CD2 . LEU   B 93  ? 0.1149 0.1275 0.1409 -0.0028 -0.0027 -0.0035 93  LEU   B CD2 
5112 N N   . HIS   B 94  ? 0.1136 0.1012 0.1021 -0.0007 -0.0083 -0.0007 94  HIS   B N   
5113 C CA  . HIS   B 94  ? 0.1149 0.1016 0.1106 0.0013  -0.0015 -0.0009 94  HIS   B CA  
5114 C C   . HIS   B 94  ? 0.1079 0.1063 0.1224 0.0008  -0.0004 -0.0009 94  HIS   B C   
5115 O O   . HIS   B 94  ? 0.1194 0.1200 0.1566 -0.0012 0.0183  -0.0121 94  HIS   B O   
5116 C CB  . HIS   B 94  ? 0.1156 0.1114 0.1094 0.0015  -0.0056 0.0002  94  HIS   B CB  
5117 C CG  . HIS   B 94  ? 0.1193 0.1055 0.1185 -0.0041 -0.0194 -0.0004 94  HIS   B CG  
5118 N ND1 . HIS   B 94  ? 0.1263 0.1083 0.1184 -0.0051 -0.0194 -0.0047 94  HIS   B ND1 
5119 C CD2 . HIS   B 94  ? 0.1258 0.1124 0.1197 0.0005  -0.0176 0.0021  94  HIS   B CD2 
5120 C CE1 . HIS   B 94  ? 0.1280 0.1164 0.1232 -0.0098 -0.0204 -0.0014 94  HIS   B CE1 
5121 N NE2 . HIS   B 94  ? 0.1247 0.1210 0.1265 -0.0136 -0.0121 0.0006  94  HIS   B NE2 
5129 N N   . VAL   B 95  ? 0.1074 0.1034 0.1181 0.0000  0.0025  -0.0020 95  VAL   B N   
5130 C CA  . VAL   B 95  ? 0.1102 0.1101 0.1181 0.0043  0.0015  0.0020  95  VAL   B CA  
5131 C C   . VAL   B 95  ? 0.1169 0.1160 0.1180 0.0018  0.0067  -0.0042 95  VAL   B C   
5132 O O   . VAL   B 95  ? 0.1182 0.1134 0.1261 0.0044  0.0071  0.0042  95  VAL   B O   
5133 C CB  . VAL   B 95  ? 0.1177 0.1137 0.1177 -0.0002 -0.0022 -0.0028 95  VAL   B CB  
5134 C CG1 . VAL   B 95  ? 0.1262 0.1299 0.1325 -0.0130 -0.0099 0.0080  95  VAL   B CG1 
5135 C CG2 . VAL   B 95  ? 0.1264 0.1124 0.1225 0.0001  -0.0089 -0.0045 95  VAL   B CG2 
5145 N N   . VAL   B 96  ? 0.1241 0.1222 0.1180 0.0102  0.0077  0.0056  96  VAL   B N   
5146 C CA  . VAL   B 96  ? 0.1304 0.1277 0.1138 0.0102  -0.0002 0.0110  96  VAL   B CA  
5147 C C   . VAL   B 96  ? 0.1305 0.1326 0.1113 0.0089  0.0100  0.0067  96  VAL   B C   
5148 O O   . VAL   B 96  ? 0.1290 0.1382 0.1382 0.0069  0.0143  -0.0014 96  VAL   B O   
5149 C CB  . VAL   B 96  ? 0.1379 0.1458 0.1206 0.0067  0.0003  -0.0022 96  VAL   B CB  
5150 C CG1 . VAL   B 96  ? 0.1386 0.1591 0.1290 0.0091  0.0046  -0.0031 96  VAL   B CG1 
5151 C CG2 . VAL   B 96  ? 0.1532 0.1534 0.1251 0.0068  0.0060  -0.0144 96  VAL   B CG2 
5161 N N   . GLY   B 97  ? 0.1363 0.1340 0.1162 0.0048  0.0050  0.0091  97  GLY   B N   
5162 C CA  . GLY   B 97  ? 0.1450 0.1330 0.1213 0.0007  0.0086  0.0117  97  GLY   B CA  
5163 C C   . GLY   B 97  ? 0.1582 0.1432 0.1171 0.0101  -0.0003 0.0123  97  GLY   B C   
5164 O O   . GLY   B 97  ? 0.1626 0.1530 0.1198 0.0029  -0.0005 0.0105  97  GLY   B O   
5168 N N   . PRO   B 98  ? 0.1658 0.1463 0.1232 0.0082  0.0172  0.0211  98  PRO   B N   
5169 C CA  . PRO   B 98  ? 0.1733 0.1566 0.1403 0.0096  0.0224  0.0153  98  PRO   B CA  
5170 C C   . PRO   B 98  ? 0.1822 0.1624 0.1158 0.0180  0.0223  0.0284  98  PRO   B C   
5171 O O   . PRO   B 98  ? 0.1759 0.1541 0.1323 0.0228  0.0266  0.0254  98  PRO   B O   
5172 C CB  . PRO   B 98  ? 0.1599 0.1577 0.1589 0.0050  0.0322  0.0200  98  PRO   B CB  
5173 C CG  . PRO   B 98  ? 0.1556 0.1526 0.1434 0.0046  0.0194  0.0215  98  PRO   B CG  
5174 C CD  . PRO   B 98  ? 0.1456 0.1471 0.1354 0.0094  0.0119  0.0206  98  PRO   B CD  
5182 N N   A ASN   B 99  ? 0.1917 0.1686 0.1213 0.0321  0.0215  0.0204  99  ASN   B N   
5183 N N   B ASN   B 99  ? 0.1952 0.1790 0.1411 0.0142  0.0157  0.0197  99  ASN   B N   
5184 C CA  A ASN   B 99  ? 0.2023 0.1721 0.1164 0.0372  0.0139  0.0305  99  ASN   B CA  
5185 C CA  B ASN   B 99  ? 0.2075 0.1947 0.1670 0.0096  0.0092  0.0145  99  ASN   B CA  
5186 C C   A ASN   B 99  ? 0.2173 0.1900 0.1241 0.0299  0.0296  0.0379  99  ASN   B C   
5187 C C   B ASN   B 99  ? 0.2204 0.2105 0.1866 0.0045  0.0071  0.0124  99  ASN   B C   
5188 O O   A ASN   B 99  ? 0.2357 0.1966 0.1397 0.0239  0.0235  0.0338  99  ASN   B O   
5189 O O   B ASN   B 99  ? 0.2230 0.2115 0.1875 0.0024  0.0058  0.0118  99  ASN   B O   
5190 C CB  A ASN   B 99  ? 0.2119 0.1687 0.1351 0.0371  0.0096  0.0298  99  ASN   B CB  
5191 C CB  B ASN   B 99  ? 0.2085 0.1955 0.1764 0.0096  0.0078  0.0118  99  ASN   B CB  
5192 C CG  A ASN   B 99  ? 0.2172 0.1773 0.1635 0.0314  -0.0084 0.0336  99  ASN   B CG  
5193 C CG  B ASN   B 99  ? 0.2102 0.1975 0.1830 0.0098  0.0043  0.0103  99  ASN   B CG  
5194 O OD1 A ASN   B 99  ? 0.2227 0.1793 0.1987 0.0348  -0.0175 0.0301  99  ASN   B OD1 
5195 O OD1 B ASN   B 99  ? 0.2118 0.1981 0.1889 0.0113  0.0021  0.0097  99  ASN   B OD1 
5196 N ND2 A ASN   B 99  ? 0.2176 0.1841 0.1879 0.0305  -0.0252 0.0267  99  ASN   B ND2 
5197 N ND2 B ASN   B 99  ? 0.2107 0.1987 0.1880 0.0095  0.0010  0.0090  99  ASN   B ND2 
5210 N N   A VAL   B 100 ? 0.2357 0.2058 0.1604 0.0149  0.0319  0.0583  100 VAL   B N   
5211 N N   B VAL   B 100 ? 0.2334 0.2263 0.2106 0.0013  0.0047  0.0119  100 VAL   B N   
5212 C CA  A VAL   B 100 ? 0.2719 0.2245 0.2225 0.0073  0.0386  0.0716  100 VAL   B CA  
5213 C CA  B VAL   B 100 ? 0.2496 0.2425 0.2367 -0.0005 0.0040  0.0109  100 VAL   B CA  
5214 C C   A VAL   B 100 ? 0.3011 0.2283 0.2227 0.0189  0.0384  0.0936  100 VAL   B C   
5215 C C   B VAL   B 100 ? 0.2645 0.2555 0.2445 0.0014  0.0039  0.0106  100 VAL   B C   
5216 O O   A VAL   B 100 ? 0.3089 0.2378 0.2284 0.0172  0.0494  0.0903  100 VAL   B O   
5217 O O   B VAL   B 100 ? 0.2657 0.2564 0.2463 0.0008  0.0052  0.0101  100 VAL   B O   
5218 C CB  A VAL   B 100 ? 0.2847 0.2469 0.3081 -0.0126 0.0309  0.0700  100 VAL   B CB  
5219 C CB  B VAL   B 100 ? 0.2519 0.2468 0.2587 -0.0042 0.0027  0.0125  100 VAL   B CB  
5220 C CG1 A VAL   B 100 ? 0.2908 0.2531 0.3344 -0.0153 0.0328  0.0706  100 VAL   B CG1 
5221 C CG1 B VAL   B 100 ? 0.2539 0.2485 0.2670 -0.0048 0.0035  0.0137  100 VAL   B CG1 
5222 C CG2 A VAL   B 100 ? 0.2872 0.2537 0.3303 -0.0185 0.0314  0.0735  100 VAL   B CG2 
5223 C CG2 B VAL   B 100 ? 0.2516 0.2477 0.2657 -0.0053 0.0027  0.0136  100 VAL   B CG2 
5242 N N   A ASN   B 101 ? 0.3258 0.2333 0.2212 0.0315  0.0251  0.1051  101 ASN   B N   
5243 N N   B ASN   B 101 ? 0.2787 0.2686 0.2533 0.0035  0.0025  0.0106  101 ASN   B N   
5244 C CA  A ASN   B 101 ? 0.3600 0.2504 0.2467 0.0425  0.0005  0.1136  101 ASN   B CA  
5245 C CA  B ASN   B 101 ? 0.2946 0.2828 0.2680 0.0057  0.0011  0.0124  101 ASN   B CA  
5246 C C   A ASN   B 101 ? 0.3918 0.2817 0.2285 0.0489  -0.0174 0.1213  101 ASN   B C   
5247 C C   B ASN   B 101 ? 0.3092 0.2969 0.2807 0.0058  -0.0006 0.0124  101 ASN   B C   
5248 O O   A ASN   B 101 ? 0.3970 0.2998 0.2567 0.0544  -0.0298 0.0999  101 ASN   B O   
5249 O O   B ASN   B 101 ? 0.3109 0.2994 0.2838 0.0070  -0.0024 0.0121  101 ASN   B O   
5250 C CB  A ASN   B 101 ? 0.3627 0.2425 0.2681 0.0385  0.0059  0.1129  101 ASN   B CB  
5251 C CB  B ASN   B 101 ? 0.2956 0.2831 0.2687 0.0065  0.0022  0.0134  101 ASN   B CB  
5252 C CG  A ASN   B 101 ? 0.3639 0.2348 0.2722 0.0337  0.0141  0.1189  101 ASN   B CG  
5253 C CG  B ASN   B 101 ? 0.2963 0.2831 0.2687 0.0066  0.0038  0.0148  101 ASN   B CG  
5254 O OD1 A ASN   B 101 ? 0.3706 0.2395 0.3047 0.0226  0.0353  0.1111  101 ASN   B OD1 
5255 O OD1 B ASN   B 101 ? 0.2976 0.2840 0.2734 0.0063  0.0063  0.0147  101 ASN   B OD1 
5256 N ND2 A ASN   B 101 ? 0.3603 0.2372 0.2686 0.0322  0.0108  0.1028  101 ASN   B ND2 
5257 N ND2 B ASN   B 101 ? 0.2954 0.2829 0.2653 0.0062  0.0032  0.0145  101 ASN   B ND2 
5270 N N   A LYS   B 102 ? 0.4160 0.3040 0.2253 0.0426  -0.0097 0.1126  102 LYS   B N   
5271 N N   B LYS   B 102 ? 0.3208 0.3080 0.2934 0.0045  0.0013  0.0096  102 LYS   B N   
5272 C CA  A LYS   B 102 ? 0.4400 0.3358 0.2503 0.0322  0.0115  0.0898  102 LYS   B CA  
5273 C CA  B LYS   B 102 ? 0.3312 0.3188 0.3098 0.0030  0.0054  0.0074  102 LYS   B CA  
5274 C C   A LYS   B 102 ? 0.4399 0.3403 0.2329 0.0353  0.0333  0.0909  102 LYS   B C   
5275 C C   B LYS   B 102 ? 0.3301 0.3167 0.3013 0.0041  0.0088  0.0090  102 LYS   B C   
5276 O O   A LYS   B 102 ? 0.4497 0.3462 0.2433 0.0373  0.0279  0.0758  102 LYS   B O   
5277 O O   B LYS   B 102 ? 0.3322 0.3178 0.3001 0.0045  0.0089  0.0075  102 LYS   B O   
5278 C CB  A LYS   B 102 ? 0.4621 0.3602 0.3162 0.0195  0.0198  0.0569  102 LYS   B CB  
5279 C CB  B LYS   B 102 ? 0.3418 0.3305 0.3372 0.0007  0.0067  0.0031  102 LYS   B CB  
5280 C CG  A LYS   B 102 ? 0.4780 0.3811 0.3824 0.0114  0.0280  0.0251  102 LYS   B CG  
5281 C CG  B LYS   B 102 ? 0.3507 0.3405 0.3635 -0.0007 0.0081  -0.0014 102 LYS   B CG  
5282 C CD  A LYS   B 102 ? 0.4909 0.3978 0.4427 0.0051  0.0364  0.0014  102 LYS   B CD  
5283 C CD  B LYS   B 102 ? 0.3584 0.3488 0.3868 -0.0019 0.0092  -0.0045 102 LYS   B CD  
5284 C CE  A LYS   B 102 ? 0.5021 0.4101 0.4909 -0.0002 0.0423  -0.0159 102 LYS   B CE  
5285 C CE  B LYS   B 102 ? 0.3641 0.3550 0.4050 -0.0029 0.0104  -0.0069 102 LYS   B CE  
5286 N NZ  A LYS   B 102 ? 0.5091 0.4178 0.5187 -0.0036 0.0448  -0.0251 102 LYS   B NZ  
5287 N NZ  B LYS   B 102 ? 0.3673 0.3587 0.4152 -0.0034 0.0110  -0.0080 102 LYS   B NZ  
5314 N N   A GLY   B 103 ? 0.4264 0.3347 0.2108 0.0354  0.0638  0.1083  103 GLY   B N   
5315 N N   B GLY   B 103 ? 0.3254 0.3126 0.2960 0.0047  0.0120  0.0122  103 GLY   B N   
5316 C CA  A GLY   B 103 ? 0.4134 0.3327 0.2232 0.0354  0.0870  0.0951  103 GLY   B CA  
5317 C CA  B GLY   B 103 ? 0.3208 0.3084 0.2924 0.0049  0.0141  0.0121  103 GLY   B CA  
5318 C C   A GLY   B 103 ? 0.3964 0.3231 0.2129 0.0300  0.1074  0.0813  103 GLY   B C   
5319 C C   B GLY   B 103 ? 0.3153 0.3029 0.2856 0.0039  0.0157  0.0101  103 GLY   B C   
5320 O O   A GLY   B 103 ? 0.4028 0.3327 0.2335 0.0283  0.1060  0.0782  103 GLY   B O   
5321 O O   B GLY   B 103 ? 0.3163 0.3043 0.2888 0.0046  0.0158  0.0106  103 GLY   B O   
5328 N N   A GLU   B 104 ? 0.3719 0.3007 0.1954 0.0259  0.1103  0.0622  104 GLU   B N   
5329 N N   B GLU   B 104 ? 0.3085 0.2954 0.2742 0.0014  0.0140  0.0064  104 GLU   B N   
5330 C CA  A GLU   B 104 ? 0.3478 0.2822 0.1713 0.0216  0.1061  0.0424  104 GLU   B CA  
5331 C CA  B GLU   B 104 ? 0.3022 0.2889 0.2623 -0.0013 0.0119  0.0033  104 GLU   B CA  
5332 C C   A GLU   B 104 ? 0.3511 0.2806 0.1933 0.0110  0.1232  0.0289  104 GLU   B C   
5333 C C   B GLU   B 104 ? 0.3015 0.2886 0.2647 -0.0040 0.0164  0.0008  104 GLU   B C   
5334 O O   A GLU   B 104 ? 0.3560 0.2829 0.2388 0.0087  0.1145  0.0137  104 GLU   B O   
5335 O O   B GLU   B 104 ? 0.3022 0.2887 0.2664 -0.0046 0.0167  -0.0014 104 GLU   B O   
5336 C CB  A GLU   B 104 ? 0.3260 0.2636 0.1569 0.0262  0.0744  0.0251  104 GLU   B CB  
5337 C CB  B GLU   B 104 ? 0.2979 0.2831 0.2510 -0.0019 0.0055  0.0021  104 GLU   B CB  
5338 C CG  A GLU   B 104 ? 0.3092 0.2509 0.1515 0.0273  0.0347  0.0003  104 GLU   B CG  
5339 C CG  B GLU   B 104 ? 0.2949 0.2787 0.2414 -0.0028 -0.0004 -0.0001 104 GLU   B CG  
5340 C CD  A GLU   B 104 ? 0.2928 0.2351 0.1487 0.0256  0.0032  0.0007  104 GLU   B CD  
5341 C CD  B GLU   B 104 ? 0.2926 0.2750 0.2356 -0.0044 -0.0044 -0.0002 104 GLU   B CD  
5342 O OE1 A GLU   B 104 ? 0.2673 0.2129 0.1379 0.0314  0.0131  0.0088  104 GLU   B OE1 
5343 O OE1 B GLU   B 104 ? 0.2908 0.2725 0.2332 -0.0051 -0.0040 0.0008  104 GLU   B OE1 
5344 O OE2 A GLU   B 104 ? 0.3011 0.2488 0.1608 0.0137  -0.0287 -0.0078 104 GLU   B OE2 
5345 O OE2 B GLU   B 104 ? 0.2928 0.2754 0.2366 -0.0056 -0.0082 -0.0021 104 GLU   B OE2 
5358 N N   A ASP   B 105 ? 0.3489 0.2834 0.2052 -0.0044 0.1355  0.0331  105 ASP   B N   
5359 N N   B ASP   B 105 ? 0.3002 0.2894 0.2688 -0.0066 0.0199  0.0009  105 ASP   B N   
5360 C CA  A ASP   B 105 ? 0.3502 0.2851 0.2283 -0.0200 0.1530  0.0269  105 ASP   B CA  
5361 C CA  B ASP   B 105 ? 0.3001 0.2908 0.2777 -0.0087 0.0227  -0.0002 105 ASP   B CA  
5362 C C   A ASP   B 105 ? 0.3337 0.2490 0.2072 -0.0327 0.1397  0.0167  105 ASP   B C   
5363 C C   B ASP   B 105 ? 0.2964 0.2869 0.2634 -0.0085 0.0227  -0.0033 105 ASP   B C   
5364 O O   A ASP   B 105 ? 0.3192 0.2323 0.2062 -0.0369 0.1323  0.0128  105 ASP   B O   
5365 O O   B ASP   B 105 ? 0.2952 0.2856 0.2566 -0.0087 0.0222  -0.0046 105 ASP   B O   
5366 C CB  A ASP   B 105 ? 0.3638 0.3176 0.2947 -0.0133 0.1705  0.0115  105 ASP   B CB  
5367 C CB  B ASP   B 105 ? 0.3032 0.2952 0.3006 -0.0098 0.0265  0.0003  105 ASP   B CB  
5368 C CG  A ASP   B 105 ? 0.3740 0.3409 0.3565 -0.0106 0.1918  0.0003  105 ASP   B CG  
5369 C CG  B ASP   B 105 ? 0.3057 0.2984 0.3222 -0.0112 0.0298  0.0012  105 ASP   B CG  
5370 O OD1 A ASP   B 105 ? 0.3770 0.3489 0.3654 -0.0194 0.1981  0.0085  105 ASP   B OD1 
5371 O OD1 B ASP   B 105 ? 0.3056 0.2990 0.3288 -0.0133 0.0306  0.0025  105 ASP   B OD1 
5372 O OD2 A ASP   B 105 ? 0.3796 0.3533 0.4024 -0.0044 0.1875  -0.0130 105 ASP   B OD2 
5373 O OD2 B ASP   B 105 ? 0.3069 0.3003 0.3304 -0.0116 0.0310  0.0019  105 ASP   B OD2 
5382 N N   A ILE   B 106 ? 0.3282 0.2301 0.2190 -0.0377 0.1237  0.0132  106 ILE   B N   
5383 N N   B ILE   B 106 ? 0.2933 0.2843 0.2579 -0.0075 0.0219  -0.0045 106 ILE   B N   
5384 C CA  A ILE   B 106 ? 0.3088 0.2118 0.2392 -0.0486 0.1280  0.0023  106 ILE   B CA  
5385 C CA  B ILE   B 106 ? 0.2882 0.2816 0.2563 -0.0067 0.0235  -0.0061 106 ILE   B CA  
5386 C C   A ILE   B 106 ? 0.2768 0.2152 0.2338 -0.0481 0.1229  -0.0214 106 ILE   B C   
5387 C C   B ILE   B 106 ? 0.2787 0.2798 0.2560 -0.0058 0.0260  -0.0105 106 ILE   B C   
5388 O O   A ILE   B 106 ? 0.2653 0.1979 0.2226 -0.0510 0.1089  -0.0344 106 ILE   B O   
5389 O O   B ILE   B 106 ? 0.2781 0.2786 0.2516 -0.0059 0.0229  -0.0108 106 ILE   B O   
5390 C CB  A ILE   B 106 ? 0.3297 0.2064 0.2767 -0.0489 0.1191  0.0095  106 ILE   B CB  
5391 C CB  B ILE   B 106 ? 0.2924 0.2814 0.2579 -0.0065 0.0229  -0.0034 106 ILE   B CB  
5392 C CG1 A ILE   B 106 ? 0.3391 0.2061 0.2862 -0.0348 0.1109  0.0050  106 ILE   B CG1 
5393 C CG1 B ILE   B 106 ? 0.2934 0.2807 0.2580 -0.0049 0.0217  -0.0023 106 ILE   B CG1 
5394 C CG2 A ILE   B 106 ? 0.3372 0.2109 0.3025 -0.0581 0.1200  0.0171  106 ILE   B CG2 
5395 C CG2 B ILE   B 106 ? 0.2945 0.2826 0.2617 -0.0071 0.0234  -0.0025 106 ILE   B CG2 
5396 C CD1 A ILE   B 106 ? 0.3431 0.2108 0.2933 -0.0231 0.1096  0.0086  106 ILE   B CD1 
5397 C CD1 B ILE   B 106 ? 0.2939 0.2808 0.2590 -0.0034 0.0215  -0.0009 106 ILE   B CD1 
5420 N N   A GLN   B 107 ? 0.2637 0.2420 0.2583 -0.0440 0.1124  -0.0292 107 GLN   B N   
5421 N N   B GLN   B 107 ? 0.2694 0.2787 0.2644 -0.0057 0.0298  -0.0144 107 GLN   B N   
5422 C CA  A GLN   B 107 ? 0.2486 0.2635 0.2816 -0.0381 0.1059  -0.0273 107 GLN   B CA  
5423 C CA  B GLN   B 107 ? 0.2592 0.2759 0.2734 -0.0051 0.0342  -0.0168 107 GLN   B CA  
5424 C C   A GLN   B 107 ? 0.2205 0.2492 0.2535 -0.0182 0.0669  -0.0328 107 GLN   B C   
5425 C C   B GLN   B 107 ? 0.2304 0.2553 0.2380 -0.0034 0.0398  -0.0235 107 GLN   B C   
5426 O O   A GLN   B 107 ? 0.2196 0.2543 0.2979 -0.0060 0.0419  -0.0411 107 GLN   B O   
5427 O O   B GLN   B 107 ? 0.2321 0.2577 0.2436 -0.0029 0.0358  -0.0259 107 GLN   B O   
5428 C CB  A GLN   B 107 ? 0.2767 0.2999 0.3558 -0.0389 0.1059  -0.0172 107 GLN   B CB  
5429 C CB  B GLN   B 107 ? 0.2772 0.2922 0.3199 -0.0046 0.0303  -0.0125 107 GLN   B CB  
5430 C CG  A GLN   B 107 ? 0.3116 0.3367 0.4348 -0.0301 0.0757  -0.0111 107 GLN   B CG  
5431 C CG  B GLN   B 107 ? 0.2934 0.3066 0.3642 -0.0029 0.0237  -0.0085 107 GLN   B CG  
5432 C CD  A GLN   B 107 ? 0.3358 0.3634 0.4956 -0.0257 0.0554  -0.0036 107 GLN   B CD  
5433 C CD  B GLN   B 107 ? 0.3055 0.3176 0.3997 -0.0018 0.0188  -0.0048 107 GLN   B CD  
5434 O OE1 A GLN   B 107 ? 0.3461 0.3743 0.5182 -0.0199 0.0564  -0.0048 107 GLN   B OE1 
5435 O OE1 B GLN   B 107 ? 0.3105 0.3226 0.4122 -0.0009 0.0191  -0.0042 107 GLN   B OE1 
5436 N NE2 A GLN   B 107 ? 0.3451 0.3719 0.5170 -0.0227 0.0425  0.0050  107 GLN   B NE2 
5437 N NE2 B GLN   B 107 ? 0.3094 0.3202 0.4120 -0.0011 0.0164  -0.0022 107 GLN   B NE2 
5454 N N   . LEU   B 108 ? 0.1994 0.2313 0.2031 -0.0015 0.0502  -0.0284 108 LEU   B N   
5455 C CA  . LEU   B 108 ? 0.1859 0.2032 0.1751 0.0212  0.0317  -0.0117 108 LEU   B CA  
5456 C C   . LEU   B 108 ? 0.1664 0.1654 0.1654 0.0223  0.0211  0.0096  108 LEU   B C   
5457 O O   . LEU   B 108 ? 0.1757 0.1509 0.1744 0.0232  0.0115  0.0052  108 LEU   B O   
5458 C CB  . LEU   B 108 ? 0.1997 0.2205 0.1644 0.0227  0.0364  -0.0099 108 LEU   B CB  
5459 C CG  . LEU   B 108 ? 0.2215 0.2484 0.1676 0.0240  0.0357  -0.0253 108 LEU   B CG  
5460 C CD1 . LEU   B 108 ? 0.2279 0.2620 0.1490 0.0122  0.0367  -0.0223 108 LEU   B CD1 
5461 C CD2 . LEU   B 108 ? 0.2421 0.2607 0.2053 0.0316  0.0259  -0.0336 108 LEU   B CD2 
5474 N N   . LEU   B 109 ? 0.1587 0.1471 0.1575 0.0177  0.0251  0.0149  109 LEU   B N   
5475 C CA  . LEU   B 109 ? 0.1468 0.1270 0.1686 0.0139  0.0205  0.0168  109 LEU   B CA  
5476 C C   . LEU   B 109 ? 0.1359 0.1153 0.1626 0.0057  0.0227  0.0127  109 LEU   B C   
5477 O O   . LEU   B 109 ? 0.1303 0.1178 0.1658 0.0068  0.0199  0.0227  109 LEU   B O   
5478 C CB  . LEU   B 109 ? 0.1528 0.1228 0.1717 0.0134  0.0205  0.0239  109 LEU   B CB  
5479 C CG  . LEU   B 109 ? 0.1502 0.1230 0.1664 0.0092  0.0111  0.0123  109 LEU   B CG  
5480 C CD1 . LEU   B 109 ? 0.1526 0.1335 0.1675 0.0160  0.0204  0.0084  109 LEU   B CD1 
5481 C CD2 . LEU   B 109 ? 0.1606 0.1336 0.1825 0.0088  0.0136  0.0063  109 LEU   B CD2 
5493 N N   . LYS   B 110 ? 0.1303 0.1175 0.1610 0.0036  0.0228  0.0182  110 LYS   B N   
5494 C CA  . LYS   B 110 ? 0.1283 0.1154 0.1611 -0.0004 0.0165  0.0136  110 LYS   B CA  
5495 C C   . LYS   B 110 ? 0.1275 0.1196 0.1474 0.0048  0.0181  0.0076  110 LYS   B C   
5496 O O   . LYS   B 110 ? 0.1230 0.1170 0.1443 -0.0024 0.0105  0.0031  110 LYS   B O   
5497 C CB  . LYS   B 110 ? 0.1316 0.1174 0.1832 -0.0044 0.0185  0.0014  110 LYS   B CB  
5498 C CG  . LYS   B 110 ? 0.1293 0.1213 0.1953 -0.0078 0.0111  0.0106  110 LYS   B CG  
5499 C CD  . LYS   B 110 ? 0.1353 0.1247 0.2036 -0.0048 0.0076  0.0014  110 LYS   B CD  
5500 C CE  . LYS   B 110 ? 0.1315 0.1379 0.2149 -0.0041 0.0073  -0.0002 110 LYS   B CE  
5501 N NZ  . LYS   B 110 ? 0.1346 0.1545 0.2059 0.0032  0.0042  -0.0149 110 LYS   B NZ  
5515 N N   . SER   B 111 ? 0.1332 0.1224 0.1487 -0.0007 0.0218  0.0091  111 SER   B N   
5516 C CA  . SER   B 111 ? 0.1362 0.1256 0.1402 0.0003  0.0131  0.0082  111 SER   B CA  
5517 C C   . SER   B 111 ? 0.1322 0.1220 0.1252 0.0015  0.0001  0.0030  111 SER   B C   
5518 O O   . SER   B 111 ? 0.1275 0.1255 0.1417 -0.0017 -0.0001 0.0082  111 SER   B O   
5519 C CB  . SER   B 111 ? 0.1514 0.1456 0.1578 0.0023  0.0208  0.0167  111 SER   B CB  
5520 O OG  . SER   B 111 ? 0.1696 0.1890 0.1695 -0.0012 0.0336  0.0061  111 SER   B OG  
5526 N N   . ALA   B 112 ? 0.1196 0.1255 0.1416 0.0065  0.0088  0.0131  112 ALA   B N   
5527 C CA  . ALA   B 112 ? 0.1203 0.1249 0.1435 0.0045  0.0040  0.0034  112 ALA   B CA  
5528 C C   . ALA   B 112 ? 0.1086 0.1147 0.1420 0.0029  0.0043  0.0048  112 ALA   B C   
5529 O O   . ALA   B 112 ? 0.1104 0.1182 0.1472 -0.0012 0.0035  -0.0034 112 ALA   B O   
5530 C CB  . ALA   B 112 ? 0.1266 0.1282 0.1528 0.0126  0.0004  0.0077  112 ALA   B CB  
5536 N N   . TYR   B 113 ? 0.1098 0.1074 0.1520 -0.0007 0.0072  0.0064  113 TYR   B N   
5537 C CA  . TYR   B 113 ? 0.1072 0.1064 0.1372 -0.0026 0.0053  0.0015  113 TYR   B CA  
5538 C C   . TYR   B 113 ? 0.1052 0.1001 0.1385 -0.0001 0.0031  0.0019  113 TYR   B C   
5539 O O   . TYR   B 113 ? 0.1128 0.1056 0.1310 -0.0017 0.0042  -0.0022 113 TYR   B O   
5540 C CB  . TYR   B 113 ? 0.1115 0.1098 0.1425 -0.0017 0.0122  0.0067  113 TYR   B CB  
5541 C CG  . TYR   B 113 ? 0.1158 0.1088 0.1469 -0.0055 0.0081  0.0024  113 TYR   B CG  
5542 C CD1 . TYR   B 113 ? 0.1204 0.1088 0.1645 -0.0020 0.0126  0.0100  113 TYR   B CD1 
5543 C CD2 . TYR   B 113 ? 0.1262 0.1029 0.1539 -0.0023 0.0066  0.0043  113 TYR   B CD2 
5544 C CE1 . TYR   B 113 ? 0.1217 0.1174 0.1604 -0.0007 0.0134  0.0043  113 TYR   B CE1 
5545 C CE2 . TYR   B 113 ? 0.1294 0.1006 0.1632 0.0039  0.0068  0.0113  113 TYR   B CE2 
5546 C CZ  . TYR   B 113 ? 0.1187 0.1114 0.1645 0.0057  0.0026  0.0010  113 TYR   B CZ  
5547 O OH  . TYR   B 113 ? 0.1260 0.1124 0.1769 0.0123  0.0108  0.0030  113 TYR   B OH  
5557 N N   . GLU   B 114 ? 0.1077 0.0997 0.1413 0.0008  0.0072  0.0061  114 GLU   B N   
5558 C CA  . GLU   B 114 ? 0.1051 0.1039 0.1339 0.0009  0.0037  -0.0048 114 GLU   B CA  
5559 C C   . GLU   B 114 ? 0.1037 0.1036 0.1322 0.0053  0.0081  -0.0063 114 GLU   B C   
5560 O O   . GLU   B 114 ? 0.1078 0.1056 0.1475 0.0043  0.0061  0.0028  114 GLU   B O   
5561 C CB  . GLU   B 114 ? 0.1096 0.1112 0.1394 0.0017  0.0050  0.0006  114 GLU   B CB  
5562 C CG  . GLU   B 114 ? 0.1167 0.1158 0.1424 0.0005  0.0110  -0.0010 114 GLU   B CG  
5563 C CD  . GLU   B 114 ? 0.1122 0.1187 0.1439 -0.0028 0.0051  0.0027  114 GLU   B CD  
5564 O OE1 . GLU   B 114 ? 0.1145 0.1323 0.1520 -0.0031 0.0153  0.0029  114 GLU   B OE1 
5565 O OE2 . GLU   B 114 ? 0.1162 0.1311 0.1640 -0.0133 0.0117  0.0020  114 GLU   B OE2 
5572 N N   . ASN   B 115 ? 0.1120 0.1007 0.1340 0.0007  0.0024  -0.0001 115 ASN   B N   
5573 C CA  . ASN   B 115 ? 0.1142 0.1051 0.1393 -0.0009 0.0051  0.0007  115 ASN   B CA  
5574 C C   . ASN   B 115 ? 0.1075 0.1035 0.1275 -0.0081 0.0059  -0.0027 115 ASN   B C   
5575 O O   . ASN   B 115 ? 0.1147 0.1118 0.1368 -0.0059 0.0001  -0.0008 115 ASN   B O   
5576 C CB  . ASN   B 115 ? 0.1225 0.1183 0.1329 -0.0069 0.0019  0.0001  115 ASN   B CB  
5577 C CG  . ASN   B 115 ? 0.1362 0.1237 0.1326 0.0026  -0.0014 -0.0051 115 ASN   B CG  
5578 O OD1 . ASN   B 115 ? 0.1795 0.1400 0.1539 0.0006  0.0070  -0.0199 115 ASN   B OD1 
5579 N ND2 . ASN   B 115 ? 0.1323 0.1333 0.1303 -0.0003 -0.0002 -0.0009 115 ASN   B ND2 
5586 N N   . PHE   B 116 ? 0.1078 0.1044 0.1183 -0.0017 0.0024  0.0023  116 PHE   B N   
5587 C CA  . PHE   B 116 ? 0.1147 0.1069 0.1239 -0.0061 0.0003  -0.0017 116 PHE   B CA  
5588 C C   . PHE   B 116 ? 0.1165 0.0964 0.1238 -0.0037 0.0012  0.0048  116 PHE   B C   
5589 O O   . PHE   B 116 ? 0.1161 0.1060 0.1305 0.0014  -0.0008 -0.0004 116 PHE   B O   
5590 C CB  . PHE   B 116 ? 0.1088 0.1038 0.1273 -0.0039 -0.0076 0.0019  116 PHE   B CB  
5591 C CG  . PHE   B 116 ? 0.1067 0.1067 0.1259 -0.0016 0.0027  -0.0046 116 PHE   B CG  
5592 C CD1 . PHE   B 116 ? 0.1152 0.1118 0.1515 -0.0004 -0.0002 -0.0077 116 PHE   B CD1 
5593 C CD2 . PHE   B 116 ? 0.1115 0.1138 0.1304 0.0032  -0.0003 -0.0092 116 PHE   B CD2 
5594 C CE1 . PHE   B 116 ? 0.1149 0.1163 0.1439 0.0007  -0.0090 -0.0040 116 PHE   B CE1 
5595 C CE2 . PHE   B 116 ? 0.1140 0.1118 0.1368 0.0058  0.0045  -0.0021 116 PHE   B CE2 
5596 C CZ  . PHE   B 116 ? 0.1051 0.1165 0.1445 -0.0000 -0.0074 0.0006  116 PHE   B CZ  
5606 N N   . ASN   B 117 ? 0.1111 0.1022 0.1346 -0.0001 -0.0015 0.0018  117 ASN   B N   
5607 C CA  . ASN   B 117 ? 0.1163 0.1070 0.1336 0.0014  -0.0002 -0.0028 117 ASN   B CA  
5608 C C   . ASN   B 117 ? 0.1185 0.1009 0.1435 0.0021  0.0015  -0.0001 117 ASN   B C   
5609 O O   . ASN   B 117 ? 0.1270 0.1119 0.1641 0.0001  -0.0194 0.0030  117 ASN   B O   
5610 C CB  . ASN   B 117 ? 0.1167 0.1124 0.1410 0.0031  -0.0015 -0.0032 117 ASN   B CB  
5611 C CG  . ASN   B 117 ? 0.1153 0.1072 0.1457 0.0037  -0.0022 -0.0086 117 ASN   B CG  
5612 O OD1 . ASN   B 117 ? 0.1387 0.1127 0.1502 -0.0090 0.0082  -0.0103 117 ASN   B OD1 
5613 N ND2 . ASN   B 117 ? 0.1207 0.1133 0.1435 0.0019  0.0059  -0.0023 117 ASN   B ND2 
5620 N N   . GLN   B 118 ? 0.1201 0.0998 0.1390 -0.0048 -0.0120 -0.0019 118 GLN   B N   
5621 C CA  . GLN   B 118 ? 0.1246 0.1062 0.1519 0.0030  -0.0085 -0.0020 118 GLN   B CA  
5622 C C   . GLN   B 118 ? 0.1299 0.1070 0.1576 0.0003  -0.0036 -0.0063 118 GLN   B C   
5623 O O   . GLN   B 118 ? 0.1468 0.1033 0.1936 -0.0085 0.0085  -0.0024 118 GLN   B O   
5624 C CB  . GLN   B 118 ? 0.1320 0.1086 0.1633 0.0044  -0.0119 -0.0057 118 GLN   B CB  
5625 C CG  . GLN   B 118 ? 0.1394 0.1105 0.1615 0.0070  -0.0064 -0.0131 118 GLN   B CG  
5626 C CD  . GLN   B 118 ? 0.1441 0.1043 0.1556 0.0044  -0.0035 -0.0181 118 GLN   B CD  
5627 O OE1 . GLN   B 118 ? 0.1518 0.1078 0.1723 0.0047  0.0081  -0.0017 118 GLN   B OE1 
5628 N NE2 . GLN   B 118 ? 0.1491 0.1084 0.1663 0.0053  -0.0136 -0.0069 118 GLN   B NE2 
5637 N N   . HIS   B 119 ? 0.1287 0.1062 0.1260 -0.0026 -0.0039 0.0004  119 HIS   B N   
5638 C CA  . HIS   B 119 ? 0.1359 0.1150 0.1310 0.0002  -0.0090 0.0015  119 HIS   B CA  
5639 C C   . HIS   B 119 ? 0.1358 0.1157 0.1320 -0.0020 -0.0109 0.0009  119 HIS   B C   
5640 O O   . HIS   B 119 ? 0.1428 0.1168 0.1442 -0.0215 -0.0063 0.0039  119 HIS   B O   
5641 C CB  . HIS   B 119 ? 0.1348 0.1251 0.1457 0.0028  -0.0129 -0.0055 119 HIS   B CB  
5642 C CG  . HIS   B 119 ? 0.1412 0.1501 0.1601 0.0120  -0.0301 -0.0224 119 HIS   B CG  
5643 N ND1 . HIS   B 119 ? 0.1598 0.1686 0.1906 0.0068  -0.0362 -0.0406 119 HIS   B ND1 
5644 C CD2 . HIS   B 119 ? 0.1607 0.1703 0.1730 0.0381  -0.0400 -0.0285 119 HIS   B CD2 
5645 C CE1 . HIS   B 119 ? 0.1789 0.1767 0.1973 0.0201  -0.0404 -0.0536 119 HIS   B CE1 
5646 N NE2 . HIS   B 119 ? 0.1803 0.1939 0.1861 0.0328  -0.0399 -0.0446 119 HIS   B NE2 
5654 N N   A GLU   B 120 ? 0.1464 0.1139 0.1279 -0.0061 -0.0196 0.0079  120 GLU   B N   
5655 N N   B GLU   B 120 ? 0.1527 0.1300 0.1535 -0.0060 -0.0103 0.0028  120 GLU   B N   
5656 C CA  A GLU   B 120 ? 0.1723 0.1302 0.1352 0.0014  -0.0325 0.0141  120 GLU   B CA  
5657 C CA  B GLU   B 120 ? 0.1697 0.1451 0.1771 -0.0076 -0.0110 0.0057  120 GLU   B CA  
5658 C C   A GLU   B 120 ? 0.1531 0.1212 0.1219 -0.0079 -0.0183 0.0175  120 GLU   B C   
5659 C C   B GLU   B 120 ? 0.1587 0.1316 0.1491 -0.0107 -0.0083 0.0113  120 GLU   B C   
5660 O O   A GLU   B 120 ? 0.1523 0.1322 0.1220 -0.0125 -0.0192 0.0061  120 GLU   B O   
5661 O O   B GLU   B 120 ? 0.1597 0.1342 0.1453 -0.0118 -0.0084 0.0107  120 GLU   B O   
5662 C CB  A GLU   B 120 ? 0.2262 0.1506 0.1934 0.0194  -0.0556 0.0267  120 GLU   B CB  
5663 C CB  B GLU   B 120 ? 0.1979 0.1709 0.2347 -0.0057 -0.0135 0.0044  120 GLU   B CB  
5664 C CG  A GLU   B 120 ? 0.2712 0.2085 0.2938 0.0280  -0.0773 0.0434  120 GLU   B CG  
5665 C CG  B GLU   B 120 ? 0.2221 0.1982 0.2927 -0.0054 -0.0158 0.0061  120 GLU   B CG  
5666 C CD  A GLU   B 120 ? 0.3102 0.2604 0.3982 0.0211  -0.0781 0.0606  120 GLU   B CD  
5667 C CD  B GLU   B 120 ? 0.2418 0.2215 0.3434 -0.0081 -0.0158 0.0095  120 GLU   B CD  
5668 O OE1 A GLU   B 120 ? 0.3298 0.2782 0.4373 0.0102  -0.0703 0.0719  120 GLU   B OE1 
5669 O OE1 B GLU   B 120 ? 0.2496 0.2314 0.3623 -0.0103 -0.0141 0.0118  120 GLU   B OE1 
5670 O OE2 A GLU   B 120 ? 0.3309 0.2864 0.4528 0.0189  -0.0762 0.0543  120 GLU   B OE2 
5671 O OE2 B GLU   B 120 ? 0.2505 0.2301 0.3641 -0.0098 -0.0158 0.0088  120 GLU   B OE2 
5684 N N   . VAL   B 121 ? 0.1480 0.1158 0.1286 -0.0126 -0.0058 0.0156  121 VAL   B N   
5685 C CA  . VAL   B 121 ? 0.1434 0.1279 0.1189 -0.0094 -0.0132 0.0089  121 VAL   B CA  
5686 C C   . VAL   B 121 ? 0.1348 0.1237 0.1144 -0.0178 -0.0072 0.0065  121 VAL   B C   
5687 O O   . VAL   B 121 ? 0.1413 0.1195 0.1345 -0.0221 -0.0138 -0.0002 121 VAL   B O   
5688 C CB  . VAL   B 121 ? 0.1641 0.1638 0.1307 0.0042  -0.0151 0.0155  121 VAL   B CB  
5689 C CG1 . VAL   B 121 ? 0.1714 0.1739 0.1575 -0.0049 -0.0037 0.0103  121 VAL   B CG1 
5690 C CG2 . VAL   B 121 ? 0.1895 0.1870 0.1330 0.0111  -0.0071 0.0033  121 VAL   B CG2 
5701 N N   . LEU   B 122 ? 0.1272 0.1151 0.1158 -0.0112 -0.0141 0.0049  122 LEU   B N   
5702 C CA  . LEU   B 122 ? 0.1213 0.1234 0.1075 -0.0108 -0.0040 0.0006  122 LEU   B CA  
5703 C C   . LEU   B 122 ? 0.1209 0.1102 0.1149 -0.0176 -0.0090 0.0010  122 LEU   B C   
5704 O O   . LEU   B 122 ? 0.1342 0.1120 0.1391 -0.0211 -0.0184 -0.0042 122 LEU   B O   
5705 C CB  . LEU   B 122 ? 0.1410 0.1335 0.1428 -0.0008 -0.0126 0.0073  122 LEU   B CB  
5706 C CG  . LEU   B 122 ? 0.1369 0.1365 0.1397 -0.0118 -0.0042 0.0087  122 LEU   B CG  
5707 C CD1 . LEU   B 122 ? 0.1432 0.1592 0.1572 -0.0158 -0.0070 0.0053  122 LEU   B CD1 
5708 C CD2 . LEU   B 122 ? 0.1391 0.1399 0.1293 -0.0054 -0.0029 -0.0046 122 LEU   B CD2 
5720 N N   . LEU   B 123 ? 0.1243 0.1061 0.1118 -0.0178 -0.0011 0.0014  123 LEU   B N   
5721 C CA  . LEU   B 123 ? 0.1273 0.1065 0.1138 -0.0177 -0.0093 -0.0008 123 LEU   B CA  
5722 C C   . LEU   B 123 ? 0.1214 0.1036 0.1140 -0.0191 -0.0093 -0.0042 123 LEU   B C   
5723 O O   . LEU   B 123 ? 0.1350 0.1090 0.1156 -0.0272 -0.0082 0.0004  123 LEU   B O   
5724 C CB  . LEU   B 123 ? 0.1335 0.1121 0.1247 -0.0150 -0.0054 -0.0046 123 LEU   B CB  
5725 C CG  . LEU   B 123 ? 0.1321 0.1173 0.1398 -0.0093 0.0012  0.0062  123 LEU   B CG  
5726 C CD1 . LEU   B 123 ? 0.1401 0.1178 0.1476 -0.0139 0.0058  -0.0101 123 LEU   B CD1 
5727 C CD2 . LEU   B 123 ? 0.1356 0.1181 0.1588 -0.0110 0.0088  0.0147  123 LEU   B CD2 
5739 N N   . ALA   B 124 ? 0.1198 0.1028 0.1107 -0.0184 -0.0010 -0.0051 124 ALA   B N   
5740 C CA  . ALA   B 124 ? 0.1114 0.1050 0.1223 -0.0121 -0.0004 -0.0090 124 ALA   B CA  
5741 C C   . ALA   B 124 ? 0.1122 0.1046 0.1262 -0.0121 -0.0053 -0.0072 124 ALA   B C   
5742 O O   . ALA   B 124 ? 0.1262 0.1072 0.1236 -0.0103 -0.0033 0.0001  124 ALA   B O   
5743 C CB  . ALA   B 124 ? 0.1282 0.1099 0.1229 -0.0042 0.0067  -0.0029 124 ALA   B CB  
5749 N N   . PRO   B 125 ? 0.1237 0.1079 0.1164 -0.0141 -0.0115 0.0071  125 PRO   B N   
5750 C CA  . PRO   B 125 ? 0.1304 0.1095 0.1332 -0.0104 -0.0099 0.0108  125 PRO   B CA  
5751 C C   . PRO   B 125 ? 0.1264 0.1060 0.1391 -0.0132 -0.0064 0.0028  125 PRO   B C   
5752 O O   . PRO   B 125 ? 0.1288 0.1045 0.1582 -0.0073 -0.0021 0.0059  125 PRO   B O   
5753 C CB  . PRO   B 125 ? 0.1359 0.1336 0.1453 -0.0162 -0.0162 0.0212  125 PRO   B CB  
5754 C CG  . PRO   B 125 ? 0.1426 0.1400 0.1330 -0.0288 -0.0147 0.0068  125 PRO   B CG  
5755 C CD  . PRO   B 125 ? 0.1349 0.1215 0.1181 -0.0265 -0.0093 0.0038  125 PRO   B CD  
5763 N N   . LEU   B 126 ? 0.1305 0.1015 0.1618 -0.0124 0.0104  0.0036  126 LEU   B N   
5764 C CA  . LEU   B 126 ? 0.1387 0.1083 0.1624 -0.0107 0.0181  0.0023  126 LEU   B CA  
5765 C C   . LEU   B 126 ? 0.1290 0.1195 0.1640 0.0016  0.0174  0.0058  126 LEU   B C   
5766 O O   . LEU   B 126 ? 0.1512 0.1447 0.1809 0.0247  -0.0018 -0.0102 126 LEU   B O   
5767 C CB  . LEU   B 126 ? 0.1525 0.1146 0.1880 -0.0154 0.0258  -0.0035 126 LEU   B CB  
5768 C CG  . LEU   B 126 ? 0.1667 0.1227 0.1936 -0.0233 0.0290  -0.0152 126 LEU   B CG  
5769 C CD1 . LEU   B 126 ? 0.1783 0.1353 0.2416 -0.0231 0.0246  -0.0227 126 LEU   B CD1 
5770 C CD2 . LEU   B 126 ? 0.1669 0.1367 0.1906 -0.0289 0.0183  -0.0104 126 LEU   B CD2 
5782 N N   . LEU   B 127 ? 0.1265 0.1092 0.1621 0.0006  0.0141  0.0035  127 LEU   B N   
5783 C CA  . LEU   B 127 ? 0.1306 0.1188 0.1634 -0.0043 0.0216  0.0083  127 LEU   B CA  
5784 C C   . LEU   B 127 ? 0.1285 0.1155 0.1558 -0.0019 0.0152  0.0087  127 LEU   B C   
5785 O O   . LEU   B 127 ? 0.1307 0.1236 0.1514 -0.0140 0.0015  0.0134  127 LEU   B O   
5786 C CB  . LEU   B 127 ? 0.1439 0.1214 0.1648 0.0004  0.0175  0.0161  127 LEU   B CB  
5787 C CG  . LEU   B 127 ? 0.1543 0.1210 0.1729 -0.0005 0.0133  0.0121  127 LEU   B CG  
5788 C CD1 . LEU   B 127 ? 0.1554 0.1233 0.1787 0.0028  0.0069  0.0051  127 LEU   B CD1 
5789 C CD2 . LEU   B 127 ? 0.1575 0.1299 0.1964 -0.0065 0.0150  0.0174  127 LEU   B CD2 
5801 N N   . SER   B 128 ? 0.1372 0.1157 0.1506 -0.0019 0.0038  0.0052  128 SER   B N   
5802 C CA  . SER   B 128 ? 0.1439 0.1257 0.1554 0.0081  -0.0044 0.0129  128 SER   B CA  
5803 C C   . SER   B 128 ? 0.1565 0.1286 0.1733 0.0086  -0.0190 0.0141  128 SER   B C   
5804 O O   . SER   B 128 ? 0.1694 0.1327 0.2036 0.0046  -0.0096 0.0255  128 SER   B O   
5805 C CB  . SER   B 128 ? 0.1563 0.1285 0.1540 0.0095  0.0026  0.0223  128 SER   B CB  
5806 O OG  . SER   B 128 ? 0.1641 0.1391 0.1487 0.0114  0.0097  0.0180  128 SER   B OG  
5812 N N   . ALA   B 129 ? 0.1639 0.1328 0.1907 0.0293  -0.0159 -0.0030 129 ALA   B N   
5813 C CA  . ALA   B 129 ? 0.1755 0.1433 0.2076 0.0270  -0.0137 -0.0118 129 ALA   B CA  
5814 C C   . ALA   B 129 ? 0.1644 0.1321 0.1921 0.0218  0.0035  -0.0009 129 ALA   B C   
5815 O O   . ALA   B 129 ? 0.1569 0.1403 0.1958 0.0179  -0.0014 0.0139  129 ALA   B O   
5816 C CB  . ALA   B 129 ? 0.1954 0.1655 0.2291 0.0286  -0.0078 -0.0205 129 ALA   B CB  
5822 N N   . GLY   B 130 ? 0.1661 0.1286 0.2066 0.0240  0.0109  -0.0035 130 GLY   B N   
5823 C CA  . GLY   B 130 ? 0.1720 0.1392 0.2219 0.0250  0.0257  -0.0066 130 GLY   B CA  
5824 C C   . GLY   B 130 ? 0.1703 0.1356 0.2138 0.0168  0.0118  0.0057  130 GLY   B C   
5825 O O   . GLY   B 130 ? 0.1921 0.1465 0.2164 0.0155  0.0119  0.0132  130 GLY   B O   
5829 N N   . ILE   B 131 ? 0.1588 0.1488 0.2119 0.0325  0.0108  0.0080  131 ILE   B N   
5830 C CA  . ILE   B 131 ? 0.1726 0.1652 0.2063 0.0318  -0.0084 0.0202  131 ILE   B CA  
5831 C C   . ILE   B 131 ? 0.1882 0.1571 0.1782 0.0190  -0.0118 0.0243  131 ILE   B C   
5832 O O   . ILE   B 131 ? 0.2154 0.1745 0.1904 0.0223  -0.0234 0.0216  131 ILE   B O   
5833 C CB  . ILE   B 131 ? 0.1777 0.2055 0.2368 0.0288  -0.0168 0.0247  131 ILE   B CB  
5834 C CG1 . ILE   B 131 ? 0.1830 0.2230 0.2432 0.0084  -0.0104 0.0203  131 ILE   B CG1 
5835 C CG2 . ILE   B 131 ? 0.1789 0.2257 0.2662 0.0287  -0.0132 0.0152  131 ILE   B CG2 
5836 C CD1 . ILE   B 131 ? 0.1933 0.2404 0.2562 -0.0119 -0.0097 0.0242  131 ILE   B CD1 
5848 N N   . PHE   B 132 ? 0.1723 0.1397 0.1690 0.0111  0.0014  0.0214  132 PHE   B N   
5849 C CA  . PHE   B 132 ? 0.1804 0.1432 0.1601 0.0071  0.0190  0.0091  132 PHE   B CA  
5850 C C   . PHE   B 132 ? 0.1971 0.1581 0.1672 0.0049  0.0224  0.0155  132 PHE   B C   
5851 O O   . PHE   B 132 ? 0.2164 0.1786 0.1943 0.0019  0.0390  0.0166  132 PHE   B O   
5852 C CB  . PHE   B 132 ? 0.1644 0.1429 0.1499 0.0113  0.0106  0.0111  132 PHE   B CB  
5853 C CG  . PHE   B 132 ? 0.1620 0.1463 0.1578 0.0165  0.0165  0.0114  132 PHE   B CG  
5854 C CD1 . PHE   B 132 ? 0.1703 0.1510 0.1953 0.0113  0.0274  0.0113  132 PHE   B CD1 
5855 C CD2 . PHE   B 132 ? 0.1622 0.1456 0.1439 0.0199  0.0122  0.0181  132 PHE   B CD2 
5856 C CE1 . PHE   B 132 ? 0.1724 0.1532 0.2031 0.0119  0.0240  0.0131  132 PHE   B CE1 
5857 C CE2 . PHE   B 132 ? 0.1691 0.1500 0.1483 0.0178  0.0088  0.0088  132 PHE   B CE2 
5858 C CZ  . PHE   B 132 ? 0.1735 0.1520 0.1875 0.0101  0.0004  0.0215  132 PHE   B CZ  
5868 N N   . GLY   B 133 ? 0.1950 0.1484 0.1656 0.0032  0.0146  0.0295  133 GLY   B N   
5869 C CA  . GLY   B 133 ? 0.2046 0.1617 0.1782 -0.0132 0.0076  0.0321  133 GLY   B CA  
5870 C C   . GLY   B 133 ? 0.2062 0.1656 0.1777 -0.0226 0.0174  0.0286  133 GLY   B C   
5871 O O   . GLY   B 133 ? 0.2233 0.1801 0.2229 -0.0352 0.0169  0.0445  133 GLY   B O   
5875 N N   . ALA   B 134 ? 0.1924 0.1648 0.1712 -0.0228 0.0148  0.0123  134 ALA   B N   
5876 C CA  . ALA   B 134 ? 0.1861 0.1598 0.1883 -0.0161 0.0236  0.0006  134 ALA   B CA  
5877 C C   . ALA   B 134 ? 0.1929 0.1548 0.1857 -0.0068 0.0179  0.0102  134 ALA   B C   
5878 O O   . ALA   B 134 ? 0.1986 0.1748 0.2094 0.0017  0.0190  0.0034  134 ALA   B O   
5879 C CB  . ALA   B 134 ? 0.1856 0.1604 0.2196 -0.0058 0.0187  -0.0089 134 ALA   B CB  
5885 N N   . ASP   B 135 ? 0.2052 0.1496 0.1793 -0.0135 0.0042  0.0177  135 ASP   B N   
5886 C CA  . ASP   B 135 ? 0.2169 0.1432 0.1982 -0.0133 -0.0089 0.0213  135 ASP   B CA  
5887 C C   . ASP   B 135 ? 0.1998 0.1353 0.1792 -0.0026 -0.0004 0.0162  135 ASP   B C   
5888 O O   . ASP   B 135 ? 0.1942 0.1314 0.1889 -0.0023 -0.0003 0.0209  135 ASP   B O   
5889 C CB  . ASP   B 135 ? 0.2431 0.1508 0.2310 -0.0297 0.0001  0.0270  135 ASP   B CB  
5890 C CG  . ASP   B 135 ? 0.2668 0.1536 0.2721 -0.0477 0.0035  0.0182  135 ASP   B CG  
5891 O OD1 . ASP   B 135 ? 0.2761 0.1416 0.2635 -0.0347 -0.0023 0.0137  135 ASP   B OD1 
5892 O OD2 . ASP   B 135 ? 0.2888 0.1895 0.3298 -0.0597 0.0027  0.0017  135 ASP   B OD2 
5897 N N   . PRO   B 136 ? 0.1951 0.1355 0.1875 0.0134  -0.0058 0.0093  136 PRO   B N   
5898 C CA  . PRO   B 136 ? 0.1758 0.1330 0.1887 0.0107  -0.0033 0.0016  136 PRO   B CA  
5899 C C   . PRO   B 136 ? 0.1601 0.1231 0.1956 0.0149  -0.0022 -0.0024 136 PRO   B C   
5900 O O   . PRO   B 136 ? 0.1473 0.1192 0.1934 0.0141  -0.0003 0.0012  136 PRO   B O   
5901 C CB  . PRO   B 136 ? 0.1841 0.1558 0.2081 0.0218  -0.0140 -0.0046 136 PRO   B CB  
5902 C CG  . PRO   B 136 ? 0.1994 0.1613 0.2222 0.0253  -0.0163 -0.0088 136 PRO   B CG  
5903 C CD  . PRO   B 136 ? 0.1992 0.1483 0.2144 0.0326  -0.0055 0.0042  136 PRO   B CD  
5911 N N   . ILE   B 137 ? 0.1719 0.1184 0.1983 0.0129  -0.0091 0.0048  137 ILE   B N   
5912 C CA  . ILE   B 137 ? 0.1810 0.1119 0.2082 -0.0061 -0.0017 0.0020  137 ILE   B CA  
5913 C C   . ILE   B 137 ? 0.1739 0.1161 0.1962 -0.0081 0.0084  0.0127  137 ILE   B C   
5914 O O   . ILE   B 137 ? 0.1609 0.1193 0.2001 -0.0152 0.0070  0.0068  137 ILE   B O   
5915 C CB  . ILE   B 137 ? 0.2091 0.1202 0.2490 -0.0021 -0.0052 0.0001  137 ILE   B CB  
5916 C CG1 . ILE   B 137 ? 0.2380 0.1345 0.3006 0.0026  0.0026  -0.0150 137 ILE   B CG1 
5917 C CG2 . ILE   B 137 ? 0.2118 0.1248 0.2578 -0.0241 -0.0054 -0.0013 137 ILE   B CG2 
5918 C CD1 . ILE   B 137 ? 0.2639 0.1591 0.3424 0.0176  -0.0033 0.0009  137 ILE   B CD1 
5930 N N   A HIS   B 138 ? 0.1797 0.1171 0.1998 -0.0032 0.0164  0.0172  138 HIS   B N   
5931 N N   B HIS   B 138 ? 0.1749 0.1193 0.1903 -0.0040 0.0120  0.0100  138 HIS   B N   
5932 C CA  A HIS   B 138 ? 0.1837 0.1239 0.2038 0.0004  0.0293  0.0176  138 HIS   B CA  
5933 C CA  B HIS   B 138 ? 0.1748 0.1243 0.1875 -0.0006 0.0155  0.0065  138 HIS   B CA  
5934 C C   A HIS   B 138 ? 0.1660 0.1255 0.1886 0.0027  0.0290  0.0166  138 HIS   B C   
5935 C C   B HIS   B 138 ? 0.1678 0.1209 0.1831 0.0019  0.0192  0.0052  138 HIS   B C   
5936 O O   A HIS   B 138 ? 0.1605 0.1291 0.2094 0.0055  0.0271  0.0303  138 HIS   B O   
5937 O O   B HIS   B 138 ? 0.1675 0.1220 0.1875 0.0021  0.0192  0.0055  138 HIS   B O   
5938 C CB  A HIS   B 138 ? 0.2057 0.1368 0.2208 -0.0004 0.0434  0.0112  138 HIS   B CB  
5939 C CB  B HIS   B 138 ? 0.1817 0.1331 0.1899 0.0001  0.0133  0.0037  138 HIS   B CB  
5940 C CG  A HIS   B 138 ? 0.2209 0.1598 0.2267 -0.0058 0.0621  0.0246  138 HIS   B CG  
5941 C CG  B HIS   B 138 ? 0.1864 0.1429 0.1911 -0.0008 0.0127  0.0041  138 HIS   B CG  
5942 N ND1 A HIS   B 138 ? 0.2261 0.1779 0.2476 -0.0014 0.0722  0.0169  138 HIS   B ND1 
5943 N ND1 B HIS   B 138 ? 0.1882 0.1490 0.1957 0.0004  0.0142  0.0020  138 HIS   B ND1 
5944 C CD2 A HIS   B 138 ? 0.2330 0.1663 0.2298 -0.0062 0.0689  0.0170  138 HIS   B CD2 
5945 C CD2 B HIS   B 138 ? 0.1895 0.1462 0.1920 -0.0008 0.0134  0.0011  138 HIS   B CD2 
5946 C CE1 A HIS   B 138 ? 0.2314 0.1724 0.2429 -0.0024 0.0752  0.0219  138 HIS   B CE1 
5947 C CE1 B HIS   B 138 ? 0.1900 0.1488 0.1952 0.0004  0.0150  0.0025  138 HIS   B CE1 
5948 N NE2 A HIS   B 138 ? 0.2388 0.1622 0.2364 0.0005  0.0736  0.0128  138 HIS   B NE2 
5949 N NE2 B HIS   B 138 ? 0.1914 0.1463 0.1937 0.0005  0.0143  -0.0004 138 HIS   B NE2 
5964 N N   . SER   B 139 ? 0.1625 0.1151 0.1822 0.0053  0.0203  0.0037  139 SER   B N   
5965 C CA  . SER   B 139 ? 0.1560 0.1091 0.1785 -0.0025 0.0165  -0.0046 139 SER   B CA  
5966 C C   . SER   B 139 ? 0.1336 0.1061 0.1685 -0.0009 0.0131  -0.0050 139 SER   B C   
5967 O O   . SER   B 139 ? 0.1360 0.1084 0.1732 0.0030  0.0021  -0.0014 139 SER   B O   
5968 C CB  . SER   B 139 ? 0.1640 0.1078 0.1796 0.0032  0.0045  0.0032  139 SER   B CB  
5969 O OG  . SER   B 139 ? 0.1733 0.1117 0.1786 0.0003  -0.0091 0.0005  139 SER   B OG  
5976 N N   . LEU   B 140 ? 0.1335 0.1030 0.1690 -0.0038 0.0105  -0.0102 140 LEU   B N   
5977 C CA  . LEU   B 140 ? 0.1285 0.1084 0.1720 0.0014  0.0099  -0.0023 140 LEU   B CA  
5978 C C   . LEU   B 140 ? 0.1306 0.1045 0.1835 -0.0027 0.0033  -0.0049 140 LEU   B C   
5979 O O   . LEU   B 140 ? 0.1298 0.1051 0.1798 -0.0005 -0.0013 -0.0040 140 LEU   B O   
5980 C CB  . LEU   B 140 ? 0.1296 0.1069 0.1830 -0.0050 0.0132  -0.0075 140 LEU   B CB  
5981 C CG  . LEU   B 140 ? 0.1388 0.1095 0.1701 -0.0103 0.0060  0.0022  140 LEU   B CG  
5982 C CD1 . LEU   B 140 ? 0.1479 0.1177 0.1734 -0.0132 0.0031  -0.0057 140 LEU   B CD1 
5983 C CD2 . LEU   B 140 ? 0.1554 0.1204 0.1751 -0.0085 0.0014  -0.0111 140 LEU   B CD2 
5995 N N   . ARG   B 141 ? 0.1211 0.1068 0.1920 -0.0062 0.0057  -0.0082 141 ARG   B N   
5996 C CA  . ARG   B 141 ? 0.1265 0.1117 0.2203 -0.0163 0.0206  -0.0076 141 ARG   B CA  
5997 C C   . ARG   B 141 ? 0.1224 0.1063 0.2005 -0.0116 0.0138  -0.0049 141 ARG   B C   
5998 O O   . ARG   B 141 ? 0.1292 0.1106 0.2038 -0.0088 0.0034  -0.0135 141 ARG   B O   
5999 C CB  . ARG   B 141 ? 0.1440 0.1256 0.2663 -0.0209 0.0289  -0.0059 141 ARG   B CB  
6000 C CG  . ARG   B 141 ? 0.1786 0.1560 0.2999 -0.0207 0.0355  0.0037  141 ARG   B CG  
6001 C CD  . ARG   B 141 ? 0.2191 0.1773 0.3104 -0.0139 0.0226  -0.0088 141 ARG   B CD  
6002 N NE  . ARG   B 141 ? 0.2391 0.1759 0.3098 -0.0334 0.0330  -0.0085 141 ARG   B NE  
6003 C CZ  . ARG   B 141 ? 0.2481 0.1530 0.3049 -0.0285 0.0488  -0.0233 141 ARG   B CZ  
6004 N NH1 . ARG   B 141 ? 0.2594 0.1483 0.3051 -0.0276 0.0506  -0.0289 141 ARG   B NH1 
6005 N NH2 . ARG   B 141 ? 0.2540 0.1595 0.3097 -0.0137 0.0352  -0.0180 141 ARG   B NH2 
6019 N N   . VAL   B 142 ? 0.1307 0.1018 0.1885 -0.0020 0.0126  -0.0085 142 VAL   B N   
6020 C CA  . VAL   B 142 ? 0.1256 0.1123 0.1825 -0.0037 0.0150  -0.0049 142 VAL   B CA  
6021 C C   . VAL   B 142 ? 0.1251 0.1102 0.1859 0.0017  0.0106  -0.0138 142 VAL   B C   
6022 O O   . VAL   B 142 ? 0.1300 0.1078 0.1937 0.0039  0.0139  -0.0063 142 VAL   B O   
6023 C CB  . VAL   B 142 ? 0.1364 0.1205 0.1890 0.0012  0.0237  0.0033  142 VAL   B CB  
6024 C CG1 . VAL   B 142 ? 0.1393 0.1134 0.1955 0.0115  0.0199  -0.0070 142 VAL   B CG1 
6025 C CG2 . VAL   B 142 ? 0.1539 0.1217 0.1994 -0.0061 0.0227  0.0043  142 VAL   B CG2 
6035 N N   . CYS   B 143 ? 0.1226 0.1028 0.1730 0.0010  0.0077  0.0020  143 CYS   B N   
6036 C CA  . CYS   B 143 ? 0.1197 0.1042 0.1780 -0.0023 0.0061  -0.0018 143 CYS   B CA  
6037 C C   . CYS   B 143 ? 0.1169 0.1082 0.1747 -0.0036 0.0103  -0.0059 143 CYS   B C   
6038 O O   . CYS   B 143 ? 0.1204 0.1094 0.1870 -0.0027 -0.0006 -0.0041 143 CYS   B O   
6039 C CB  . CYS   B 143 ? 0.1229 0.1167 0.1838 -0.0021 0.0019  -0.0024 143 CYS   B CB  
6040 S SG  . CYS   B 143 ? 0.1268 0.1299 0.1794 -0.0023 0.0105  -0.0003 143 CYS   B SG  
6046 N N   . VAL   B 144 ? 0.1196 0.1112 0.1798 -0.0033 0.0073  -0.0108 144 VAL   B N   
6047 C CA  . VAL   B 144 ? 0.1267 0.1163 0.2055 -0.0116 -0.0038 -0.0225 144 VAL   B CA  
6048 C C   . VAL   B 144 ? 0.1236 0.1183 0.2061 -0.0093 -0.0063 -0.0059 144 VAL   B C   
6049 O O   . VAL   B 144 ? 0.1389 0.1364 0.2253 0.0065  -0.0001 0.0062  144 VAL   B O   
6050 C CB  . VAL   B 144 ? 0.1476 0.1349 0.2710 -0.0099 -0.0117 -0.0247 144 VAL   B CB  
6051 C CG1 . VAL   B 144 ? 0.1730 0.1698 0.3041 -0.0034 -0.0238 -0.0212 144 VAL   B CG1 
6052 C CG2 . VAL   B 144 ? 0.1578 0.1342 0.2599 0.0050  -0.0200 -0.0327 144 VAL   B CG2 
6062 N N   . ASP   B 145 ? 0.1280 0.1081 0.2120 -0.0039 -0.0006 -0.0102 145 ASP   B N   
6063 C CA  . ASP   B 145 ? 0.1259 0.1187 0.2259 -0.0024 0.0075  -0.0140 145 ASP   B CA  
6064 C C   . ASP   B 145 ? 0.1178 0.1176 0.2216 -0.0003 0.0129  -0.0093 145 ASP   B C   
6065 O O   . ASP   B 145 ? 0.1221 0.1352 0.2821 -0.0074 0.0133  -0.0329 145 ASP   B O   
6066 C CB  . ASP   B 145 ? 0.1409 0.1306 0.2563 -0.0130 0.0215  -0.0083 145 ASP   B CB  
6067 C CG  . ASP   B 145 ? 0.1576 0.1332 0.3004 -0.0246 0.0285  -0.0011 145 ASP   B CG  
6068 O OD1 . ASP   B 145 ? 0.1619 0.1352 0.3151 -0.0194 0.0043  -0.0157 145 ASP   B OD1 
6069 O OD2 . ASP   B 145 ? 0.1903 0.1514 0.3563 -0.0273 0.0434  0.0088  145 ASP   B OD2 
6074 N N   . THR   B 146 ? 0.1123 0.1153 0.1792 -0.0061 0.0059  -0.0060 146 THR   B N   
6075 C CA  . THR   B 146 ? 0.1192 0.1141 0.1661 -0.0060 0.0063  -0.0080 146 THR   B CA  
6076 C C   . THR   B 146 ? 0.1201 0.1076 0.1653 -0.0026 0.0025  -0.0028 146 THR   B C   
6077 O O   . THR   B 146 ? 0.1255 0.1133 0.1703 0.0003  0.0059  -0.0027 146 THR   B O   
6078 C CB  . THR   B 146 ? 0.1242 0.1121 0.1808 -0.0029 0.0164  -0.0003 146 THR   B CB  
6079 O OG1 . THR   B 146 ? 0.1315 0.1093 0.1843 -0.0018 0.0146  0.0038  146 THR   B OG1 
6080 C CG2 . THR   B 146 ? 0.1370 0.1150 0.1764 0.0010  0.0127  -0.0053 146 THR   B CG2 
6088 N N   . VAL   B 147 ? 0.1224 0.1148 0.1591 -0.0020 0.0107  0.0002  147 VAL   B N   
6089 C CA  . VAL   B 147 ? 0.1241 0.1073 0.1548 -0.0093 0.0007  -0.0047 147 VAL   B CA  
6090 C C   . VAL   B 147 ? 0.1155 0.1103 0.1632 -0.0160 -0.0008 -0.0069 147 VAL   B C   
6091 O O   . VAL   B 147 ? 0.1320 0.1209 0.1695 -0.0201 -0.0174 -0.0129 147 VAL   B O   
6092 C CB  . VAL   B 147 ? 0.1262 0.1226 0.1463 -0.0084 -0.0039 -0.0008 147 VAL   B CB  
6093 C CG1 . VAL   B 147 ? 0.1259 0.1355 0.1501 -0.0122 -0.0076 0.0029  147 VAL   B CG1 
6094 C CG2 . VAL   B 147 ? 0.1305 0.1241 0.1560 -0.0128 -0.0029 0.0024  147 VAL   B CG2 
6104 N N   . ARG   B 148 ? 0.1205 0.1140 0.1614 -0.0071 -0.0116 -0.0141 148 ARG   B N   
6105 C CA  . ARG   B 148 ? 0.1243 0.1197 0.1533 -0.0061 -0.0172 -0.0113 148 ARG   B CA  
6106 C C   . ARG   B 148 ? 0.1327 0.1258 0.1465 -0.0066 -0.0200 -0.0066 148 ARG   B C   
6107 O O   . ARG   B 148 ? 0.1527 0.1538 0.1512 -0.0200 -0.0242 -0.0023 148 ARG   B O   
6108 C CB  . ARG   B 148 ? 0.1330 0.1287 0.1655 -0.0046 -0.0178 -0.0159 148 ARG   B CB  
6109 C CG  . ARG   B 148 ? 0.1320 0.1440 0.1731 -0.0090 -0.0155 -0.0306 148 ARG   B CG  
6110 C CD  . ARG   B 148 ? 0.1408 0.1566 0.1892 0.0098  -0.0183 -0.0322 148 ARG   B CD  
6111 N NE  . ARG   B 148 ? 0.1430 0.1510 0.1771 0.0243  -0.0212 -0.0326 148 ARG   B NE  
6112 C CZ  . ARG   B 148 ? 0.1391 0.1445 0.1560 0.0181  -0.0153 -0.0206 148 ARG   B CZ  
6113 N NH1 . ARG   B 148 ? 0.1335 0.1527 0.1602 -0.0037 0.0001  -0.0135 148 ARG   B NH1 
6114 N NH2 . ARG   B 148 ? 0.1608 0.1302 0.1539 0.0156  -0.0143 -0.0084 148 ARG   B NH2 
6128 N N   . THR   B 149 ? 0.1350 0.1212 0.1491 -0.0104 -0.0189 -0.0009 149 THR   B N   
6129 C CA  . THR   B 149 ? 0.1349 0.1261 0.1451 -0.0115 -0.0162 0.0070  149 THR   B CA  
6130 C C   . THR   B 149 ? 0.1370 0.1197 0.1316 -0.0135 -0.0185 0.0008  149 THR   B C   
6131 O O   . THR   B 149 ? 0.1398 0.1204 0.1520 -0.0169 -0.0038 -0.0026 149 THR   B O   
6132 C CB  . THR   B 149 ? 0.1392 0.1227 0.1472 -0.0145 -0.0152 0.0013  149 THR   B CB  
6133 O OG1 . THR   B 149 ? 0.1436 0.1251 0.1408 -0.0212 -0.0169 -0.0044 149 THR   B OG1 
6134 C CG2 . THR   B 149 ? 0.1389 0.1250 0.1719 -0.0056 -0.0081 0.0001  149 THR   B CG2 
6142 N N   . ASN   B 150 ? 0.1414 0.1181 0.1370 -0.0099 -0.0201 -0.0022 150 ASN   B N   
6143 C CA  . ASN   B 150 ? 0.1459 0.1298 0.1397 -0.0114 -0.0161 -0.0109 150 ASN   B CA  
6144 C C   . ASN   B 150 ? 0.1347 0.1253 0.1451 -0.0098 -0.0162 -0.0037 150 ASN   B C   
6145 O O   . ASN   B 150 ? 0.1436 0.1223 0.1688 -0.0188 -0.0365 -0.0014 150 ASN   B O   
6146 C CB  . ASN   B 150 ? 0.1593 0.1632 0.1374 -0.0118 -0.0227 0.0013  150 ASN   B CB  
6147 C CG  . ASN   B 150 ? 0.1835 0.2067 0.1653 -0.0093 -0.0219 0.0194  150 ASN   B CG  
6148 O OD1 . ASN   B 150 ? 0.1939 0.2242 0.1894 -0.0235 -0.0465 0.0091  150 ASN   B OD1 
6149 N ND2 . ASN   B 150 ? 0.1954 0.2269 0.2026 0.0051  -0.0295 0.0557  150 ASN   B ND2 
6156 N N   . VAL   B 151 ? 0.1270 0.1228 0.1392 -0.0132 -0.0150 -0.0016 151 VAL   B N   
6157 C CA  . VAL   B 151 ? 0.1258 0.1249 0.1391 -0.0152 -0.0116 -0.0010 151 VAL   B CA  
6158 C C   . VAL   B 151 ? 0.1271 0.1123 0.1356 -0.0204 -0.0095 -0.0069 151 VAL   B C   
6159 O O   . VAL   B 151 ? 0.1352 0.1226 0.1575 -0.0199 -0.0091 -0.0141 151 VAL   B O   
6160 C CB  . VAL   B 151 ? 0.1449 0.1421 0.1571 -0.0002 -0.0070 -0.0094 151 VAL   B CB  
6161 C CG1 . VAL   B 151 ? 0.1606 0.1419 0.1811 -0.0094 0.0066  -0.0162 151 VAL   B CG1 
6162 C CG2 . VAL   B 151 ? 0.1599 0.1581 0.1538 0.0124  -0.0069 0.0036  151 VAL   B CG2 
6172 N N   . TYR   B 152 ? 0.1284 0.1060 0.1339 -0.0183 -0.0093 -0.0053 152 TYR   B N   
6173 C CA  . TYR   B 152 ? 0.1306 0.1176 0.1288 -0.0218 -0.0037 -0.0125 152 TYR   B CA  
6174 C C   . TYR   B 152 ? 0.1261 0.1120 0.1202 -0.0161 -0.0044 -0.0088 152 TYR   B C   
6175 O O   . TYR   B 152 ? 0.1327 0.1171 0.1260 -0.0232 -0.0077 -0.0062 152 TYR   B O   
6176 C CB  . TYR   B 152 ? 0.1413 0.1287 0.1337 -0.0180 -0.0042 -0.0013 152 TYR   B CB  
6177 C CG  . TYR   B 152 ? 0.1564 0.1358 0.1253 -0.0246 -0.0090 0.0053  152 TYR   B CG  
6178 C CD1 . TYR   B 152 ? 0.1645 0.1492 0.1345 -0.0128 -0.0151 0.0079  152 TYR   B CD1 
6179 C CD2 . TYR   B 152 ? 0.1727 0.1514 0.1282 -0.0223 -0.0055 0.0019  152 TYR   B CD2 
6180 C CE1 . TYR   B 152 ? 0.1834 0.1621 0.1446 -0.0106 -0.0197 0.0203  152 TYR   B CE1 
6181 C CE2 . TYR   B 152 ? 0.1847 0.1723 0.1374 -0.0241 -0.0071 -0.0014 152 TYR   B CE2 
6182 C CZ  . TYR   B 152 ? 0.1921 0.1838 0.1330 -0.0190 -0.0286 0.0196  152 TYR   B CZ  
6183 O OH  . TYR   B 152 ? 0.2153 0.2182 0.1594 -0.0102 -0.0349 0.0178  152 TYR   B OH  
6193 N N   . LEU   B 153 ? 0.1251 0.1104 0.1292 -0.0247 -0.0062 -0.0087 153 LEU   B N   
6194 C CA  . LEU   B 153 ? 0.1291 0.1066 0.1224 -0.0158 -0.0025 -0.0105 153 LEU   B CA  
6195 C C   . LEU   B 153 ? 0.1318 0.1042 0.1360 -0.0185 -0.0041 -0.0087 153 LEU   B C   
6196 O O   . LEU   B 153 ? 0.1376 0.1275 0.1518 -0.0080 -0.0056 -0.0309 153 LEU   B O   
6197 C CB  . LEU   B 153 ? 0.1334 0.1050 0.1411 -0.0140 0.0028  -0.0078 153 LEU   B CB  
6198 C CG  . LEU   B 153 ? 0.1334 0.1184 0.1593 -0.0170 0.0002  -0.0027 153 LEU   B CG  
6199 C CD1 . LEU   B 153 ? 0.1403 0.1357 0.1593 -0.0268 0.0049  -0.0020 153 LEU   B CD1 
6200 C CD2 . LEU   B 153 ? 0.1380 0.1315 0.1643 -0.0230 0.0136  -0.0083 153 LEU   B CD2 
6212 N N   . ALA   B 154 ? 0.1333 0.1067 0.1418 -0.0052 -0.0116 -0.0089 154 ALA   B N   
6213 C CA  . ALA   B 154 ? 0.1394 0.1193 0.1513 0.0050  -0.0146 -0.0175 154 ALA   B CA  
6214 C C   . ALA   B 154 ? 0.1504 0.1210 0.1571 0.0050  -0.0252 -0.0276 154 ALA   B C   
6215 O O   . ALA   B 154 ? 0.1777 0.1237 0.1800 0.0065  -0.0108 -0.0132 154 ALA   B O   
6216 C CB  . ALA   B 154 ? 0.1363 0.1388 0.1853 -0.0014 -0.0118 -0.0224 154 ALA   B CB  
6222 N N   . VAL   B 155 ? 0.1231 0.1104 0.1680 -0.0005 -0.0062 -0.0174 155 VAL   B N   
6223 C CA  . VAL   B 155 ? 0.1195 0.1126 0.1712 0.0009  -0.0116 -0.0026 155 VAL   B CA  
6224 C C   . VAL   B 155 ? 0.1224 0.1130 0.1743 0.0007  -0.0077 -0.0112 155 VAL   B C   
6225 O O   . VAL   B 155 ? 0.1407 0.1300 0.1972 0.0103  -0.0078 -0.0296 155 VAL   B O   
6226 C CB  . VAL   B 155 ? 0.1251 0.1287 0.2076 -0.0044 -0.0160 0.0074  155 VAL   B CB  
6227 C CG1 . VAL   B 155 ? 0.1306 0.1211 0.2141 -0.0121 -0.0153 0.0012  155 VAL   B CG1 
6228 C CG2 . VAL   B 155 ? 0.1214 0.1432 0.2436 -0.0045 -0.0120 0.0312  155 VAL   B CG2 
6238 N N   . PHE   B 156 ? 0.1165 0.1252 0.1782 0.0064  -0.0055 -0.0100 156 PHE   B N   
6239 C CA  . PHE   B 156 ? 0.1178 0.1336 0.2093 0.0051  -0.0073 -0.0076 156 PHE   B CA  
6240 C C   . PHE   B 156 ? 0.1153 0.1364 0.2320 0.0131  -0.0150 -0.0287 156 PHE   B C   
6241 O O   . PHE   B 156 ? 0.1373 0.1609 0.2590 0.0242  -0.0025 -0.0270 156 PHE   B O   
6242 C CB  . PHE   B 156 ? 0.1252 0.1279 0.2237 -0.0027 -0.0149 -0.0078 156 PHE   B CB  
6243 C CG  . PHE   B 156 ? 0.1291 0.1358 0.2417 -0.0039 -0.0172 0.0084  156 PHE   B CG  
6244 C CD1 . PHE   B 156 ? 0.1340 0.1654 0.2808 -0.0005 -0.0095 0.0472  156 PHE   B CD1 
6245 C CD2 . PHE   B 156 ? 0.1370 0.1411 0.2310 0.0075  -0.0237 0.0174  156 PHE   B CD2 
6246 C CE1 . PHE   B 156 ? 0.1335 0.1812 0.2977 0.0029  -0.0098 0.0492  156 PHE   B CE1 
6247 C CE2 . PHE   B 156 ? 0.1414 0.1623 0.2585 0.0111  -0.0234 0.0231  156 PHE   B CE2 
6248 C CZ  . PHE   B 156 ? 0.1307 0.1765 0.2839 0.0123  -0.0232 0.0357  156 PHE   B CZ  
6258 N N   . ASP   B 157 ? 0.1205 0.1289 0.2536 0.0107  -0.0192 -0.0214 157 ASP   B N   
6259 C CA  . ASP   B 157 ? 0.1323 0.1326 0.2861 0.0067  -0.0248 -0.0284 157 ASP   B CA  
6260 C C   . ASP   B 157 ? 0.1303 0.1229 0.2889 0.0105  -0.0225 -0.0391 157 ASP   B C   
6261 O O   . ASP   B 157 ? 0.1261 0.1296 0.2633 0.0039  -0.0163 -0.0331 157 ASP   B O   
6262 C CB  . ASP   B 157 ? 0.1576 0.1467 0.3079 0.0041  -0.0397 -0.0073 157 ASP   B CB  
6263 C CG  . ASP   B 157 ? 0.1861 0.1596 0.3252 -0.0021 -0.0264 -0.0041 157 ASP   B CG  
6264 O OD1 . ASP   B 157 ? 0.1916 0.1583 0.3423 0.0034  -0.0267 -0.0098 157 ASP   B OD1 
6265 O OD2 . ASP   B 157 ? 0.2203 0.1835 0.3513 -0.0071 -0.0039 0.0073  157 ASP   B OD2 
6270 N N   . LYS   B 158 ? 0.1303 0.1469 0.3013 0.0111  -0.0118 -0.0566 158 LYS   B N   
6271 C CA  . LYS   B 158 ? 0.1410 0.1605 0.3139 0.0109  -0.0036 -0.0612 158 LYS   B CA  
6272 C C   . LYS   B 158 ? 0.1436 0.1476 0.3070 0.0118  -0.0119 -0.0637 158 LYS   B C   
6273 O O   . LYS   B 158 ? 0.1535 0.1467 0.3103 0.0003  -0.0131 -0.0679 158 LYS   B O   
6274 C CB  . LYS   B 158 ? 0.1630 0.1903 0.3205 0.0102  0.0116  -0.0794 158 LYS   B CB  
6275 C CG  . LYS   B 158 ? 0.1931 0.2235 0.3282 0.0133  0.0220  -0.0852 158 LYS   B CG  
6276 C CD  . LYS   B 158 ? 0.2192 0.2635 0.3452 0.0076  0.0253  -0.0797 158 LYS   B CD  
6277 C CE  . LYS   B 158 ? 0.2383 0.2881 0.3622 0.0105  0.0254  -0.0743 158 LYS   B CE  
6278 N NZ  . LYS   B 158 ? 0.2376 0.2942 0.3594 0.0083  0.0281  -0.0748 158 LYS   B NZ  
6292 N N   . ASN   B 159 ? 0.1479 0.1410 0.3204 0.0094  -0.0179 -0.0457 159 ASN   B N   
6293 C CA  . ASN   B 159 ? 0.1624 0.1385 0.3326 0.0201  -0.0271 -0.0398 159 ASN   B CA  
6294 C C   . ASN   B 159 ? 0.1521 0.1305 0.3184 0.0122  -0.0360 -0.0258 159 ASN   B C   
6295 O O   . ASN   B 159 ? 0.1545 0.1229 0.3271 -0.0014 -0.0309 -0.0273 159 ASN   B O   
6296 C CB  . ASN   B 159 ? 0.1840 0.1526 0.3608 0.0265  -0.0327 -0.0329 159 ASN   B CB  
6297 C CG  . ASN   B 159 ? 0.2089 0.1725 0.3925 0.0296  -0.0352 -0.0481 159 ASN   B CG  
6298 O OD1 . ASN   B 159 ? 0.2191 0.1879 0.4036 0.0305  -0.0380 -0.0633 159 ASN   B OD1 
6299 N ND2 . ASN   B 159 ? 0.2142 0.1810 0.4080 0.0369  -0.0340 -0.0440 159 ASN   B ND2 
6306 N N   . LEU   B 160 ? 0.1401 0.1304 0.2939 0.0064  -0.0371 -0.0255 160 LEU   B N   
6307 C CA  . LEU   B 160 ? 0.1350 0.1284 0.2546 0.0097  -0.0287 -0.0147 160 LEU   B CA  
6308 C C   . LEU   B 160 ? 0.1287 0.1222 0.2493 0.0017  -0.0174 -0.0294 160 LEU   B C   
6309 O O   . LEU   B 160 ? 0.1248 0.1269 0.2299 -0.0017 -0.0247 -0.0188 160 LEU   B O   
6310 C CB  . LEU   B 160 ? 0.1349 0.1378 0.2321 0.0058  -0.0252 -0.0038 160 LEU   B CB  
6311 C CG  . LEU   B 160 ? 0.1420 0.1499 0.2121 0.0123  -0.0240 -0.0011 160 LEU   B CG  
6312 C CD1 . LEU   B 160 ? 0.1552 0.1620 0.2038 0.0006  -0.0174 -0.0073 160 LEU   B CD1 
6313 C CD2 . LEU   B 160 ? 0.1425 0.1573 0.2251 0.0200  -0.0287 -0.0151 160 LEU   B CD2 
6325 N N   . TYR   B 161 ? 0.1202 0.1302 0.2542 -0.0008 -0.0059 -0.0315 161 TYR   B N   
6326 C CA  . TYR   B 161 ? 0.1265 0.1268 0.2429 -0.0067 0.0102  -0.0412 161 TYR   B CA  
6327 C C   . TYR   B 161 ? 0.1342 0.1289 0.2298 -0.0051 0.0120  -0.0330 161 TYR   B C   
6328 O O   . TYR   B 161 ? 0.1357 0.1314 0.2172 -0.0087 -0.0046 -0.0315 161 TYR   B O   
6329 C CB  . TYR   B 161 ? 0.1387 0.1342 0.2477 -0.0127 0.0219  -0.0401 161 TYR   B CB  
6330 C CG  . TYR   B 161 ? 0.1608 0.1393 0.2397 -0.0154 0.0339  -0.0460 161 TYR   B CG  
6331 C CD1 . TYR   B 161 ? 0.1650 0.1369 0.2329 -0.0294 0.0319  -0.0431 161 TYR   B CD1 
6332 C CD2 . TYR   B 161 ? 0.1853 0.1490 0.2381 -0.0191 0.0283  -0.0475 161 TYR   B CD2 
6333 C CE1 . TYR   B 161 ? 0.1805 0.1499 0.2452 -0.0293 0.0246  -0.0380 161 TYR   B CE1 
6334 C CE2 . TYR   B 161 ? 0.2014 0.1602 0.2450 -0.0226 0.0251  -0.0366 161 TYR   B CE2 
6335 C CZ  . TYR   B 161 ? 0.1943 0.1634 0.2445 -0.0314 0.0218  -0.0242 161 TYR   B CZ  
6336 O OH  . TYR   B 161 ? 0.2213 0.1877 0.2609 -0.0344 0.0189  -0.0163 161 TYR   B OH  
6346 N N   . ASP   B 162 ? 0.1363 0.1272 0.2525 -0.0028 -0.0019 -0.0414 162 ASP   B N   
6347 C CA  . ASP   B 162 ? 0.1540 0.1347 0.2561 -0.0035 -0.0066 -0.0439 162 ASP   B CA  
6348 C C   . ASP   B 162 ? 0.1497 0.1272 0.2498 -0.0086 -0.0065 -0.0430 162 ASP   B C   
6349 O O   . ASP   B 162 ? 0.1563 0.1335 0.2473 -0.0131 -0.0145 -0.0391 162 ASP   B O   
6350 C CB  . ASP   B 162 ? 0.1747 0.1516 0.2913 0.0042  -0.0099 -0.0644 162 ASP   B CB  
6351 C CG  . ASP   B 162 ? 0.1757 0.1775 0.3085 0.0147  -0.0058 -0.0781 162 ASP   B CG  
6352 O OD1 . ASP   B 162 ? 0.1698 0.1995 0.3019 0.0125  0.0080  -0.0761 162 ASP   B OD1 
6353 O OD2 . ASP   B 162 ? 0.1907 0.1971 0.3445 0.0287  0.0043  -0.0766 162 ASP   B OD2 
6358 N N   A LYS   B 163 ? 0.1458 0.1137 0.2451 -0.0078 -0.0168 -0.0256 163 LYS   B N   
6359 N N   B LYS   B 163 ? 0.1609 0.1432 0.2507 -0.0091 -0.0096 -0.0306 163 LYS   B N   
6360 C CA  A LYS   B 163 ? 0.1546 0.1177 0.2432 -0.0140 -0.0199 -0.0071 163 LYS   B CA  
6361 C CA  B LYS   B 163 ? 0.1741 0.1619 0.2556 -0.0097 -0.0101 -0.0186 163 LYS   B CA  
6362 C C   A LYS   B 163 ? 0.1354 0.1161 0.2315 -0.0203 -0.0177 -0.0095 163 LYS   B C   
6363 C C   B LYS   B 163 ? 0.1489 0.1414 0.2309 -0.0115 -0.0113 -0.0128 163 LYS   B C   
6364 O O   A LYS   B 163 ? 0.1355 0.1268 0.2595 -0.0193 -0.0169 -0.0080 163 LYS   B O   
6365 O O   B LYS   B 163 ? 0.1484 0.1429 0.2326 -0.0109 -0.0114 -0.0117 163 LYS   B O   
6366 C CB  A LYS   B 163 ? 0.1876 0.1439 0.2766 -0.0103 -0.0193 0.0114  163 LYS   B CB  
6367 C CB  B LYS   B 163 ? 0.2098 0.2001 0.2922 -0.0087 -0.0092 -0.0137 163 LYS   B CB  
6368 C CG  A LYS   B 163 ? 0.2484 0.2049 0.3306 -0.0155 -0.0112 0.0152  163 LYS   B CG  
6369 C CG  B LYS   B 163 ? 0.2412 0.2341 0.3324 -0.0085 -0.0075 -0.0105 163 LYS   B CG  
6370 C CD  A LYS   B 163 ? 0.3015 0.2509 0.3823 -0.0241 -0.0123 0.0047  163 LYS   B CD  
6371 C CD  B LYS   B 163 ? 0.2735 0.2681 0.3700 -0.0090 -0.0074 -0.0091 163 LYS   B CD  
6372 C CE  A LYS   B 163 ? 0.3339 0.2841 0.4172 -0.0328 -0.0103 0.0011  163 LYS   B CE  
6373 C CE  B LYS   B 163 ? 0.2993 0.2948 0.3987 -0.0099 -0.0067 -0.0079 163 LYS   B CE  
6374 N NZ  A LYS   B 163 ? 0.3514 0.3032 0.4456 -0.0371 -0.0097 -0.0032 163 LYS   B NZ  
6375 N NZ  B LYS   B 163 ? 0.3032 0.2982 0.4164 -0.0103 -0.0061 -0.0079 163 LYS   B NZ  
6402 N N   . LEU   B 164 ? 0.1253 0.1201 0.2119 -0.0122 -0.0110 -0.0072 164 LEU   B N   
6403 C CA  . LEU   B 164 ? 0.1248 0.1185 0.2017 -0.0083 -0.0190 -0.0061 164 LEU   B CA  
6404 C C   . LEU   B 164 ? 0.1238 0.1209 0.2069 -0.0084 -0.0269 -0.0073 164 LEU   B C   
6405 O O   . LEU   B 164 ? 0.1292 0.1384 0.2254 -0.0085 -0.0250 -0.0057 164 LEU   B O   
6406 C CB  . LEU   B 164 ? 0.1217 0.1156 0.1893 -0.0045 -0.0205 -0.0053 164 LEU   B CB  
6407 C CG  . LEU   B 164 ? 0.1314 0.1342 0.1972 -0.0100 -0.0126 -0.0037 164 LEU   B CG  
6408 C CD1 . LEU   B 164 ? 0.1353 0.1292 0.2019 -0.0099 -0.0218 -0.0105 164 LEU   B CD1 
6409 C CD2 . LEU   B 164 ? 0.1483 0.1675 0.2142 -0.0097 -0.0010 -0.0237 164 LEU   B CD2 
6422 N N   . VAL   B 165 ? 0.1484 0.1273 0.2188 -0.0124 -0.0217 -0.0185 165 VAL   B N   
6423 C CA  . VAL   B 165 ? 0.1731 0.1395 0.2123 -0.0174 -0.0327 -0.0177 165 VAL   B CA  
6424 C C   . VAL   B 165 ? 0.1964 0.1489 0.2344 -0.0267 -0.0586 -0.0126 165 VAL   B C   
6425 O O   . VAL   B 165 ? 0.2097 0.1590 0.2404 -0.0312 -0.0631 -0.0074 165 VAL   B O   
6426 C CB  . VAL   B 165 ? 0.1921 0.1548 0.2083 -0.0096 -0.0074 -0.0189 165 VAL   B CB  
6427 C CG1 . VAL   B 165 ? 0.2095 0.1590 0.2275 -0.0149 -0.0009 -0.0173 165 VAL   B CG1 
6428 C CG2 . VAL   B 165 ? 0.1823 0.1624 0.2180 -0.0105 0.0023  -0.0112 165 VAL   B CG2 
6438 N N   . SER   B 166 ? 0.2066 0.1382 0.2627 -0.0283 -0.0668 -0.0289 166 SER   B N   
6439 C CA  . SER   B 166 ? 0.2076 0.1362 0.3089 -0.0365 -0.0621 -0.0332 166 SER   B CA  
6440 C C   . SER   B 166 ? 0.1969 0.1432 0.3247 -0.0347 -0.0637 -0.0135 166 SER   B C   
6441 O O   . SER   B 166 ? 0.2007 0.1660 0.3574 -0.0458 -0.0775 -0.0265 166 SER   B O   
6442 C CB  . SER   B 166 ? 0.2117 0.1435 0.3372 -0.0282 -0.0564 -0.0382 166 SER   B CB  
6443 O OG  . SER   B 166 ? 0.2034 0.1404 0.3610 -0.0235 -0.0587 -0.0172 166 SER   B OG  
6449 N N   . SER   B 167 ? 0.1806 0.1446 0.3046 -0.0293 -0.0581 0.0112  167 SER   B N   
6450 C CA  . SER   B 167 ? 0.1724 0.1483 0.2868 -0.0353 -0.0357 0.0216  167 SER   B CA  
6451 C C   . SER   B 167 ? 0.1691 0.1538 0.2786 -0.0432 -0.0401 0.0342  167 SER   B C   
6452 O O   . SER   B 167 ? 0.1775 0.1676 0.2604 -0.0436 -0.0345 0.0334  167 SER   B O   
6453 C CB  . SER   B 167 ? 0.1662 0.1604 0.2741 -0.0331 -0.0114 0.0257  167 SER   B CB  
6454 O OG  . SER   B 167 ? 0.1599 0.1707 0.2561 -0.0201 -0.0069 0.0275  167 SER   B OG  
6460 N N   . PHE   B 168 ? 0.1674 0.1465 0.2807 -0.0332 -0.0315 0.0409  168 PHE   B N   
6461 C CA  . PHE   B 168 ? 0.1722 0.1449 0.2637 -0.0366 -0.0251 0.0233  168 PHE   B CA  
6462 C C   . PHE   B 168 ? 0.1506 0.1373 0.2249 -0.0182 -0.0045 0.0107  168 PHE   B C   
6463 O O   . PHE   B 168 ? 0.1757 0.1347 0.2304 0.0038  -0.0092 -0.0052 168 PHE   B O   
6464 C CB  . PHE   B 168 ? 0.1856 0.1495 0.2645 -0.0408 -0.0395 0.0413  168 PHE   B CB  
6465 C CG  . PHE   B 168 ? 0.2093 0.1353 0.2588 -0.0466 -0.0444 0.0195  168 PHE   B CG  
6466 C CD1 . PHE   B 168 ? 0.2444 0.1364 0.2679 -0.0398 -0.0508 0.0137  168 PHE   B CD1 
6467 C CD2 . PHE   B 168 ? 0.1965 0.1372 0.2555 -0.0396 -0.0442 0.0235  168 PHE   B CD2 
6468 C CE1 . PHE   B 168 ? 0.2577 0.1529 0.2750 -0.0218 -0.0441 0.0138  168 PHE   B CE1 
6469 C CE2 . PHE   B 168 ? 0.2201 0.1461 0.2589 -0.0243 -0.0543 0.0158  168 PHE   B CE2 
6470 C CZ  . PHE   B 168 ? 0.2416 0.1420 0.2669 -0.0148 -0.0534 0.0263  168 PHE   B CZ  
6480 N N   . LEU   B 169 ? 0.1525 0.1590 0.2272 -0.0004 0.0021  -0.0038 169 LEU   B N   
6481 C CA  . LEU   B 169 ? 0.1765 0.1862 0.2707 -0.0135 -0.0010 -0.0164 169 LEU   B CA  
6482 C C   . LEU   B 169 ? 0.1988 0.2080 0.3290 0.0014  -0.0037 -0.0464 169 LEU   B C   
6483 O O   . LEU   B 169 ? 0.2218 0.2313 0.3845 -0.0025 -0.0044 -0.0699 169 LEU   B O   
6484 C CB  . LEU   B 169 ? 0.1963 0.2205 0.2830 -0.0165 -0.0114 0.0062  169 LEU   B CB  
6485 C CG  . LEU   B 169 ? 0.2332 0.2554 0.3298 -0.0048 -0.0152 0.0099  169 LEU   B CG  
6486 C CD1 . LEU   B 169 ? 0.2468 0.2759 0.3442 -0.0006 -0.0203 0.0232  169 LEU   B CD1 
6487 C CD2 . LEU   B 169 ? 0.2317 0.2615 0.3382 0.0066  -0.0029 -0.0035 169 LEU   B CD2 
6488 O OXT . LEU   B 169 ? 0.2130 0.2229 0.3246 0.0268  0.0046  -0.0470 169 LEU   B OXT 
6500 C C3  B A1A5B C .   ? 0.1794 0.1671 0.1693 0.0363  0.0030  0.0076  201 A1A5B A C3  
6501 C C6  B A1A5B C .   ? 0.1780 0.1707 0.1642 0.0258  0.0087  0.0074  201 A1A5B A C6  
6502 C C9  B A1A5B C .   ? 0.1889 0.1841 0.1826 0.0181  0.0324  0.0011  201 A1A5B A C9  
6503 C C12 B A1A5B C .   ? 0.1822 0.1802 0.1781 0.0214  0.0312  -0.0003 201 A1A5B A C12 
6504 C C1  B A1A5B C .   ? 0.1820 0.1744 0.1693 0.0218  0.0254  0.0119  201 A1A5B A C1  
6505 C C10 B A1A5B C .   ? 0.1861 0.1826 0.1785 0.0168  0.0335  0.0007  201 A1A5B A C10 
6506 C C11 B A1A5B C .   ? 0.1852 0.1792 0.1796 0.0204  0.0355  0.0012  201 A1A5B A C11 
6507 C C13 B A1A5B C .   ? 0.1811 0.1800 0.1781 0.0252  0.0312  0.0011  201 A1A5B A C13 
6508 C C2  B A1A5B C .   ? 0.1793 0.1724 0.1682 0.0312  0.0107  0.0089  201 A1A5B A C2  
6509 C C4  B A1A5B C .   ? 0.1781 0.1646 0.1604 0.0431  0.0016  0.0176  201 A1A5B A C4  
6510 C C5  B A1A5B C .   ? 0.1786 0.1685 0.1653 0.0247  0.0071  0.0025  201 A1A5B A C5  
6511 C C7  B A1A5B C .   ? 0.1809 0.1785 0.1750 0.0235  0.0303  0.0052  201 A1A5B A C7  
6512 C C8  B A1A5B C .   ? 0.1836 0.1805 0.1796 0.0217  0.0320  0.0052  201 A1A5B A C8  
6513 N N1  B A1A5B C .   ? 0.1822 0.1727 0.1680 0.0241  0.0202  0.0152  201 A1A5B A N1  
6514 O O1  B A1A5B C .   ? 0.1826 0.1720 0.1706 0.0207  0.0227  0.0159  201 A1A5B A O1  
6515 O O2  B A1A5B C .   ? 0.1780 0.1648 0.1403 0.0497  0.0088  0.0285  201 A1A5B A O2  
6516 O O3  B A1A5B C .   ? 0.1864 0.1806 0.1799 0.0193  0.0364  0.0009  201 A1A5B A O3  
6517 O O4  B A1A5B C .   ? 0.1816 0.1779 0.1766 0.0201  0.0317  -0.0023 201 A1A5B A O4  
6518 O O5  B A1A5B C .   ? 0.1707 0.1651 0.1806 0.0394  -0.0005 0.0196  201 A1A5B A O5  
6519 S S1  B A1A5B C .   ? 0.1781 0.1652 0.1719 0.0230  0.0046  -0.0035 201 A1A5B A S1  
6528 O O   . HOH   D .   ? 0.1938 0.1530 0.2107 0.0223  -0.0204 -0.0055 301 HOH   A O   
6529 O O   . HOH   D .   ? 0.2166 0.2172 0.3012 -0.0325 0.0319  0.0690  302 HOH   A O   
6530 O O   . HOH   D .   ? 0.2690 0.6552 0.5340 0.0131  -0.0709 0.1549  303 HOH   A O   
6531 O O   . HOH   D .   ? 0.3782 0.1817 0.3278 -0.0138 -0.0515 0.0549  304 HOH   A O   
6532 O O   . HOH   D .   ? 0.6033 0.4561 0.3484 0.2046  -0.1105 0.0531  305 HOH   A O   
6533 O O   . HOH   D .   ? 0.6114 0.5239 0.5034 -0.0130 0.0242  0.0333  306 HOH   A O   
6534 O O   . HOH   D .   ? 0.2567 0.2763 0.3135 0.0045  0.1040  -0.0210 307 HOH   A O   
6535 O O   . HOH   D .   ? 0.3757 0.6481 0.4388 -0.1240 0.0906  0.0160  308 HOH   A O   
6536 O O   . HOH   D .   ? 0.7348 0.4842 0.3313 0.0019  -0.0105 0.1025  309 HOH   A O   
6537 O O   . HOH   D .   ? 0.3047 0.2693 0.1546 -0.0162 0.0428  0.0469  310 HOH   A O   
6538 O O   . HOH   D .   ? 0.1681 0.1244 0.1405 -0.0212 0.0095  -0.0026 311 HOH   A O   
6539 O O   . HOH   D .   ? 0.1926 0.1774 0.3468 -0.0426 -0.0009 -0.0212 312 HOH   A O   
6540 O O   . HOH   D .   ? 0.3084 0.4321 0.2513 -0.0100 0.0624  0.0611  313 HOH   A O   
6541 O O   . HOH   D .   ? 0.2392 0.1979 0.3784 -0.0182 -0.0843 0.0838  314 HOH   A O   
6542 O O   . HOH   D .   ? 0.4361 0.4917 0.2567 -0.0750 0.1400  0.1016  315 HOH   A O   
6543 O O   . HOH   D .   ? 0.7039 0.3505 0.5057 -0.0709 -0.1295 0.0483  316 HOH   A O   
6544 O O   . HOH   D .   ? 0.3776 0.2306 0.3528 -0.0440 0.0704  0.0042  317 HOH   A O   
6545 O O   . HOH   D .   ? 0.3221 0.3043 0.3536 -0.0853 0.1485  -0.0402 318 HOH   A O   
6546 O O   . HOH   D .   ? 0.1735 0.3254 0.3968 -0.0297 0.0220  -0.1388 319 HOH   A O   
6547 O O   . HOH   D .   ? 0.1329 0.1661 0.2785 0.0115  -0.0429 -0.0714 320 HOH   A O   
6548 O O   . HOH   D .   ? 0.1549 0.2497 0.2451 0.0211  -0.0222 -0.0136 321 HOH   A O   
6549 O O   . HOH   D .   ? 0.5705 0.4562 0.3944 -0.1319 0.1589  0.1133  322 HOH   A O   
6550 O O   . HOH   D .   ? 0.2512 0.2289 0.2025 -0.0564 0.0318  0.0257  323 HOH   A O   
6551 O O   . HOH   D .   ? 0.1265 0.3520 0.2442 -0.0096 0.0113  0.0800  324 HOH   A O   
6552 O O   . HOH   D .   ? 0.1446 0.1406 0.1799 -0.0195 0.0069  0.0005  325 HOH   A O   
6553 O O   . HOH   D .   ? 0.3787 0.3427 0.2896 -0.0145 -0.0774 -0.0720 326 HOH   A O   
6554 O O   . HOH   D .   ? 0.2677 0.2269 0.2254 0.0732  0.0294  0.0390  327 HOH   A O   
6555 O O   . HOH   D .   ? 0.4202 0.2945 0.4414 0.0082  0.1255  -0.0487 328 HOH   A O   
6556 O O   B HOH   D .   ? 0.1923 0.1531 0.1442 0.0023  -0.0042 0.0381  329 HOH   A O   
6557 O O   . HOH   D .   ? 0.3238 0.2139 0.4259 0.0064  -0.1362 0.0883  330 HOH   A O   
6558 O O   . HOH   D .   ? 0.2280 0.4458 0.3509 0.0575  -0.0336 0.1446  331 HOH   A O   
6559 O O   . HOH   D .   ? 0.2591 0.4123 0.2453 -0.0405 0.0378  0.0171  332 HOH   A O   
6560 O O   A HOH   D .   ? 0.2886 0.1337 0.1487 0.0304  0.0233  0.0217  333 HOH   A O   
6561 O O   . HOH   D .   ? 0.4831 0.1672 0.4206 0.0449  0.0453  0.0146  334 HOH   A O   
6562 O O   . HOH   D .   ? 0.2432 0.3856 0.5447 -0.0058 0.1001  0.2072  335 HOH   A O   
6563 O O   . HOH   D .   ? 0.5721 0.4896 0.4943 0.1022  0.2070  -0.1140 336 HOH   A O   
6564 O O   . HOH   D .   ? 0.3431 0.3832 0.3853 -0.0677 -0.1472 -0.1140 337 HOH   A O   
6565 O O   . HOH   D .   ? 0.3038 0.4018 0.3093 -0.1374 -0.0885 -0.0246 338 HOH   A O   
6566 O O   . HOH   D .   ? 0.2046 0.4755 0.4004 -0.0181 -0.0633 0.0951  339 HOH   A O   
6567 O O   B HOH   D .   ? 0.1033 0.2010 0.1459 -0.0255 0.0185  0.0006  340 HOH   A O   
6568 O O   . HOH   D .   ? 0.1385 0.2191 0.2001 0.0125  -0.0085 0.0472  341 HOH   A O   
6569 O O   . HOH   D .   ? 0.4085 0.2682 0.3933 -0.1504 0.1135  -0.0390 342 HOH   A O   
6570 O O   . HOH   D .   ? 0.3140 0.3261 0.2155 -0.0798 -0.0184 -0.0708 343 HOH   A O   
6571 O O   . HOH   D .   ? 0.1369 0.1676 0.2357 0.0125  -0.0209 -0.0018 344 HOH   A O   
6572 O O   . HOH   D .   ? 0.1866 0.1535 0.1277 -0.0024 0.0172  0.0078  345 HOH   A O   
6573 O O   B HOH   D .   ? 0.1881 0.1641 0.1294 0.0331  -0.0128 0.0647  346 HOH   A O   
6574 O O   . HOH   D .   ? 0.4508 0.3872 0.3451 -0.1885 -0.0968 0.1708  347 HOH   A O   
6575 O O   . HOH   D .   ? 0.4948 0.3997 0.2666 0.0413  0.0649  0.1474  348 HOH   A O   
6576 O O   . HOH   D .   ? 0.3203 0.4240 0.3041 0.1706  0.0519  0.0541  349 HOH   A O   
6577 O O   . HOH   D .   ? 0.1820 0.1717 0.1983 -0.0308 0.0153  0.0131  350 HOH   A O   
6578 O O   . HOH   D .   ? 0.2336 0.3354 0.3653 0.0807  -0.0649 -0.0213 351 HOH   A O   
6579 O O   . HOH   D .   ? 0.5564 0.3637 0.5652 -0.0029 -0.1120 0.0352  352 HOH   A O   
6580 O O   . HOH   D .   ? 0.4859 0.4905 0.3852 -0.1047 -0.1122 -0.0466 353 HOH   A O   
6581 O O   . HOH   D .   ? 0.3364 0.5947 0.4708 -0.0385 -0.1468 0.0668  354 HOH   A O   
6582 O O   . HOH   D .   ? 0.1195 0.1160 0.1039 0.0006  0.0075  0.0052  355 HOH   A O   
6583 O O   . HOH   D .   ? 0.1752 0.2006 0.3393 0.0248  0.0851  -0.0205 356 HOH   A O   
6584 O O   . HOH   D .   ? 0.1438 0.1184 0.1773 -0.0045 0.0154  -0.0098 357 HOH   A O   
6585 O O   B HOH   D .   ? 0.0955 0.1555 0.2367 -0.0175 0.0310  -0.0002 358 HOH   A O   
6586 O O   . HOH   D .   ? 0.1795 0.1577 0.2288 -0.0040 -0.0469 -0.0107 359 HOH   A O   
6587 O O   . HOH   D .   ? 0.3482 0.2039 0.3867 -0.1034 0.0936  0.0150  360 HOH   A O   
6588 O O   . HOH   D .   ? 0.3573 0.2477 0.6038 0.0637  0.0951  0.0082  361 HOH   A O   
6589 O O   . HOH   D .   ? 0.2189 0.2074 0.4274 0.0384  -0.0790 -0.0693 362 HOH   A O   
6590 O O   . HOH   D .   ? 0.1575 0.1502 0.1841 0.0106  -0.0191 0.0235  363 HOH   A O   
6591 O O   . HOH   D .   ? 0.4691 0.4437 0.3747 0.1607  0.1470  -0.0694 364 HOH   A O   
6592 O O   . HOH   D .   ? 0.2644 0.3592 0.3328 0.0972  0.0820  0.0612  365 HOH   A O   
6593 O O   . HOH   D .   ? 0.3203 0.2213 0.4225 -0.0763 -0.0548 0.0322  366 HOH   A O   
6594 O O   . HOH   D .   ? 0.3796 0.1972 0.1582 0.1184  0.0218  0.0025  367 HOH   A O   
6595 O O   . HOH   D .   ? 0.1344 0.1364 0.1375 -0.0024 -0.0136 -0.0033 368 HOH   A O   
6596 O O   . HOH   D .   ? 0.2288 0.3744 0.2425 0.0235  0.0450  0.1413  369 HOH   A O   
6597 O O   . HOH   D .   ? 0.2539 0.3002 0.4997 -0.0480 -0.0974 -0.0953 370 HOH   A O   
6598 O O   . HOH   D .   ? 0.2323 0.1717 0.2049 -0.0353 -0.0017 -0.0094 371 HOH   A O   
6599 O O   . HOH   D .   ? 0.1798 0.1924 0.1749 -0.0162 -0.0408 0.0169  372 HOH   A O   
6600 O O   . HOH   D .   ? 0.1855 0.2124 0.3023 0.0329  0.0767  -0.0351 373 HOH   A O   
6601 O O   . HOH   D .   ? 0.2705 0.2750 0.1859 0.0355  0.0850  0.0123  374 HOH   A O   
6602 O O   . HOH   D .   ? 0.1507 0.1499 0.1813 -0.0143 0.0087  0.0196  375 HOH   A O   
6603 O O   . HOH   D .   ? 0.1872 0.2288 0.2533 0.0270  0.0248  0.0288  376 HOH   A O   
6604 O O   . HOH   D .   ? 0.6066 0.5593 0.3713 -0.0902 0.0729  0.2117  377 HOH   A O   
6605 O O   . HOH   D .   ? 0.2389 0.1652 0.1673 -0.0446 0.0224  0.0088  378 HOH   A O   
6606 O O   . HOH   D .   ? 0.3460 0.2747 0.3477 -0.1043 -0.0308 -0.0038 379 HOH   A O   
6607 O O   . HOH   D .   ? 0.1842 0.1687 0.1469 0.0060  0.0026  0.0113  380 HOH   A O   
6608 O O   . HOH   D .   ? 0.6473 0.4328 0.5410 -0.0525 0.0501  0.1248  381 HOH   A O   
6609 O O   . HOH   D .   ? 0.2331 0.2214 0.3425 -0.0465 0.0875  -0.0023 382 HOH   A O   
6610 O O   . HOH   D .   ? 0.1598 0.2031 0.1451 -0.0030 0.0114  0.0522  383 HOH   A O   
6611 O O   . HOH   D .   ? 0.2002 0.2133 0.2096 0.0203  0.0035  0.0524  384 HOH   A O   
6612 O O   . HOH   D .   ? 0.2089 0.1929 0.2391 0.0107  -0.0473 0.0264  385 HOH   A O   
6613 O O   . HOH   D .   ? 0.2915 0.2052 0.3220 -0.0042 -0.0380 0.0649  386 HOH   A O   
6614 O O   A HOH   D .   ? 0.1373 0.2214 0.2110 0.0343  0.0394  0.0665  387 HOH   A O   
6615 O O   . HOH   D .   ? 0.2637 0.5259 0.5967 0.1029  0.0549  0.0852  388 HOH   A O   
6616 O O   . HOH   D .   ? 0.1972 0.3377 0.2823 -0.0297 -0.0203 0.0563  389 HOH   A O   
6617 O O   . HOH   D .   ? 0.2831 0.5324 0.3971 0.0735  0.0833  -0.1419 390 HOH   A O   
6618 O O   . HOH   D .   ? 0.2405 0.4030 0.3165 -0.0390 0.0911  -0.0945 391 HOH   A O   
6619 O O   . HOH   D .   ? 0.1193 0.1315 0.1548 0.0010  -0.0149 0.0071  392 HOH   A O   
6620 O O   . HOH   D .   ? 0.1468 0.2331 0.3382 -0.0020 0.0544  0.0654  393 HOH   A O   
6621 O O   . HOH   D .   ? 0.5835 0.5979 0.3743 0.1495  -0.0986 -0.0686 394 HOH   A O   
6622 O O   . HOH   D .   ? 0.3132 0.3199 0.4919 0.0177  0.1268  -0.0275 395 HOH   A O   
6623 O O   . HOH   D .   ? 0.2022 0.1504 0.2213 0.0039  -0.0346 -0.0061 396 HOH   A O   
6624 O O   . HOH   D .   ? 0.4507 0.4100 0.4402 -0.0764 -0.0348 0.0679  397 HOH   A O   
6625 O O   . HOH   D .   ? 0.4862 0.3556 0.1840 0.0273  0.1050  0.0692  398 HOH   A O   
6626 O O   . HOH   D .   ? 0.3103 0.5622 0.3883 -0.0540 0.0314  0.1206  399 HOH   A O   
6627 O O   . HOH   D .   ? 0.1803 0.1778 0.3513 0.0457  0.1158  0.0989  400 HOH   A O   
6628 O O   . HOH   D .   ? 0.3034 0.5058 0.4104 -0.0311 -0.0443 0.1218  401 HOH   A O   
6629 O O   A HOH   D .   ? 0.2437 0.1824 0.4034 -0.0266 0.0851  -0.0071 402 HOH   A O   
6630 O O   . HOH   D .   ? 0.3982 0.3140 0.3975 0.0168  0.1562  -0.0602 403 HOH   A O   
6631 O O   . HOH   D .   ? 0.2667 0.2336 0.2012 -0.0451 -0.0773 0.0155  404 HOH   A O   
6632 O O   . HOH   D .   ? 0.1237 0.1557 0.1485 0.0048  -0.0135 -0.0239 405 HOH   A O   
6633 O O   . HOH   D .   ? 0.2364 0.2477 0.2585 0.0064  -0.0267 -0.0548 406 HOH   A O   
6634 O O   A HOH   D .   ? 0.1277 0.1292 0.1257 -0.0063 -0.0147 0.0055  407 HOH   A O   
6635 O O   . HOH   D .   ? 0.1666 0.1882 0.2165 -0.0032 -0.0055 0.0630  408 HOH   A O   
6636 O O   . HOH   D .   ? 0.4803 0.2745 0.2852 0.0790  -0.0824 -0.0585 409 HOH   A O   
6637 O O   . HOH   D .   ? 0.4279 0.5948 0.2988 -0.0927 -0.0370 0.1286  410 HOH   A O   
6638 O O   . HOH   D .   ? 0.2165 0.1490 0.2112 -0.0044 0.0052  0.0077  411 HOH   A O   
6639 O O   . HOH   D .   ? 0.2727 0.3225 0.2668 0.1033  -0.0357 -0.0757 412 HOH   A O   
6640 O O   . HOH   D .   ? 0.4600 0.4362 0.2932 -0.0328 -0.1270 0.0402  413 HOH   A O   
6641 O O   . HOH   D .   ? 0.2348 0.2082 0.2180 -0.0595 -0.0024 0.0598  414 HOH   A O   
6642 O O   . HOH   D .   ? 0.2625 0.5054 0.1619 -0.0795 0.0595  -0.0133 415 HOH   A O   
6643 O O   . HOH   D .   ? 0.1388 0.1585 0.2260 0.0005  0.0027  0.0160  416 HOH   A O   
6644 O O   . HOH   D .   ? 0.1713 0.2330 0.3010 -0.0122 -0.0278 -0.0001 417 HOH   A O   
6645 O O   . HOH   D .   ? 0.1460 0.1839 0.2517 -0.0192 -0.0102 0.0483  418 HOH   A O   
6646 O O   . HOH   D .   ? 0.3206 0.1194 0.1989 0.0020  -0.0664 0.0044  419 HOH   A O   
6647 O O   . HOH   D .   ? 0.6614 0.6202 0.3536 0.2048  -0.1156 0.1354  420 HOH   A O   
6648 O O   B HOH   D .   ? 0.1473 0.1795 0.1216 -0.0363 0.0611  0.0378  421 HOH   A O   
6649 O O   . HOH   D .   ? 0.1945 0.2443 0.2048 0.0059  -0.0562 0.0244  422 HOH   A O   
6650 O O   . HOH   D .   ? 0.5203 0.2918 0.3112 -0.1061 0.0626  0.0721  423 HOH   A O   
6651 O O   . HOH   D .   ? 0.4930 0.6142 0.3460 0.0709  0.2134  -0.0973 424 HOH   A O   
6652 O O   . HOH   D .   ? 0.2148 0.4249 0.2194 0.1606  -0.0022 -0.0034 425 HOH   A O   
6653 O O   A HOH   D .   ? 0.1533 0.1464 0.2090 0.0195  -0.0265 0.0261  426 HOH   A O   
6654 O O   . HOH   D .   ? 0.3443 0.3597 0.6668 -0.0215 0.1374  -0.0488 427 HOH   A O   
6655 O O   . HOH   D .   ? 0.6371 0.3279 0.4400 0.1821  -0.0509 0.1096  428 HOH   A O   
6656 O O   . HOH   D .   ? 0.3816 0.2088 0.4018 -0.0579 -0.1798 0.0786  429 HOH   A O   
6657 O O   . HOH   D .   ? 0.4872 0.3734 0.4484 -0.1137 -0.0933 -0.1164 430 HOH   A O   
6658 O O   . HOH   D .   ? 0.3905 0.3485 0.2609 0.0610  -0.1348 0.0045  431 HOH   A O   
6659 O O   . HOH   D .   ? 0.5651 0.6095 0.4760 0.0545  -0.1192 0.0335  432 HOH   A O   
6660 O O   . HOH   D .   ? 0.5625 0.6922 0.5504 0.1140  -0.0090 0.0108  433 HOH   A O   
6661 O O   . HOH   D .   ? 0.2694 0.2146 0.2388 0.0055  -0.0180 0.0079  434 HOH   A O   
6662 O O   A HOH   D .   ? 0.2009 0.1393 0.2093 0.0282  -0.0839 -0.0421 435 HOH   A O   
6663 O O   . HOH   D .   ? 0.4074 0.4686 0.5280 -0.1515 0.0427  -0.0546 436 HOH   A O   
6664 O O   A HOH   D .   ? 0.2823 0.2261 0.3695 0.0182  0.0751  0.1318  437 HOH   A O   
6665 O O   . HOH   D .   ? 0.3565 0.4306 0.4543 -0.0499 0.0245  0.1728  438 HOH   A O   
6666 O O   . HOH   D .   ? 0.3681 0.2385 0.1453 -0.0950 0.0462  0.0393  439 HOH   A O   
6667 O O   . HOH   D .   ? 0.2275 0.1441 0.2043 0.0028  0.0096  0.0066  440 HOH   A O   
6668 O O   A HOH   D .   ? 0.1656 0.1156 0.1329 -0.0002 -0.0075 -0.0142 441 HOH   A O   
6669 O O   . HOH   D .   ? 0.2415 0.2166 0.3950 0.0062  0.0540  -0.0359 442 HOH   A O   
6670 O O   . HOH   D .   ? 0.3599 0.3165 0.2838 0.1966  -0.0466 -0.0555 443 HOH   A O   
6671 O O   . HOH   D .   ? 0.2314 0.1952 0.2224 0.0229  0.0366  0.0190  444 HOH   A O   
6672 O O   . HOH   D .   ? 0.4693 0.3809 0.5691 0.1008  0.0819  -0.0866 445 HOH   A O   
6673 O O   . HOH   D .   ? 0.4282 0.4731 0.6420 0.0460  -0.1438 0.1341  446 HOH   A O   
6674 O O   . HOH   D .   ? 0.2025 0.2378 0.2156 0.0078  -0.0141 -0.0477 447 HOH   A O   
6675 O O   . HOH   D .   ? 0.6556 0.7091 0.5071 -0.0195 0.0611  -0.0768 448 HOH   A O   
6676 O O   . HOH   D .   ? 0.1638 0.2162 0.5242 -0.0263 -0.0846 0.0654  449 HOH   A O   
6677 O O   . HOH   D .   ? 0.5714 0.2661 0.4051 0.0372  -0.0213 0.1166  450 HOH   A O   
6678 O O   . HOH   D .   ? 0.3908 0.3474 0.4337 -0.0922 -0.1027 -0.1050 451 HOH   A O   
6679 O O   B HOH   D .   ? 0.1583 0.2465 0.1207 0.0437  -0.0155 0.0509  452 HOH   A O   
6680 O O   . HOH   D .   ? 0.2174 0.2354 0.3155 0.0279  -0.0134 0.0298  453 HOH   A O   
6681 O O   . HOH   D .   ? 0.4262 0.4116 0.3862 0.0121  -0.0358 0.1253  454 HOH   A O   
6682 O O   A HOH   D .   ? 0.1596 0.1775 0.2884 0.0022  0.0258  0.0805  455 HOH   A O   
6683 O O   . HOH   D .   ? 0.6014 0.5178 0.4323 -0.0293 0.1179  0.0733  456 HOH   A O   
6684 O O   . HOH   D .   ? 0.4774 0.3825 0.4825 0.0422  -0.0304 0.0596  457 HOH   A O   
6685 O O   . HOH   D .   ? 0.3326 0.2642 0.2847 -0.0788 0.0207  -0.0476 458 HOH   A O   
6686 O O   . HOH   D .   ? 0.2569 0.4976 0.5078 -0.1252 0.0609  -0.1763 459 HOH   A O   
6687 O O   . HOH   D .   ? 0.3153 0.4460 0.4449 0.1101  -0.0745 0.1049  460 HOH   A O   
6688 O O   . HOH   D .   ? 0.6342 0.7273 0.4365 0.0379  -0.1159 -0.0365 461 HOH   A O   
6689 O O   . HOH   D .   ? 0.2463 0.3506 0.3388 -0.0336 -0.0357 0.0175  462 HOH   A O   
6690 O O   . HOH   D .   ? 0.2549 0.1645 0.2274 0.0347  -0.0869 -0.0343 463 HOH   A O   
6691 O O   . HOH   D .   ? 0.6012 0.3492 0.7235 0.1036  0.0676  0.2222  464 HOH   A O   
6692 O O   . HOH   D .   ? 0.3842 0.5433 0.3593 -0.1187 -0.0875 0.1768  465 HOH   A O   
6693 O O   . HOH   D .   ? 0.2281 0.2297 0.2787 -0.0712 0.0343  -0.0299 466 HOH   A O   
6694 O O   . HOH   D .   ? 0.2791 0.2223 0.4399 0.0645  -0.1417 -0.0439 467 HOH   A O   
6695 O O   . HOH   D .   ? 0.2831 0.3742 0.4341 0.0736  0.0155  -0.1643 468 HOH   A O   
6696 O O   . HOH   D .   ? 0.5712 0.3693 0.4548 0.1917  0.2743  0.1263  469 HOH   A O   
6697 O O   . HOH   D .   ? 0.2269 0.2259 0.3779 0.0045  0.0470  -0.0069 470 HOH   A O   
6698 O O   . HOH   D .   ? 0.5606 0.4862 0.4097 0.0507  0.1066  0.0651  471 HOH   A O   
6699 O O   . HOH   D .   ? 0.3754 0.5201 0.3177 0.0311  -0.0316 -0.0426 472 HOH   A O   
6700 O O   . HOH   D .   ? 0.5306 0.5747 0.5801 -0.1493 -0.0934 0.1000  473 HOH   A O   
6701 O O   . HOH   D .   ? 0.4439 0.3619 0.3248 -0.0842 -0.0806 -0.0241 474 HOH   A O   
6702 O O   . HOH   D .   ? 0.4391 0.4156 0.4868 -0.1927 -0.0365 -0.0375 475 HOH   A O   
6703 O O   . HOH   D .   ? 0.6010 0.4696 0.3482 -0.0301 0.0784  -0.1383 476 HOH   A O   
6704 O O   . HOH   D .   ? 0.6031 0.4444 0.5802 -0.1124 0.0253  -0.0374 477 HOH   A O   
6705 O O   . HOH   D .   ? 0.4221 0.4316 0.2386 -0.0535 0.0073  0.0118  478 HOH   A O   
6706 O O   . HOH   D .   ? 0.7449 0.3504 0.2860 -0.0515 -0.0889 -0.0098 479 HOH   A O   
6707 O O   . HOH   D .   ? 0.4540 0.5535 0.3929 0.1085  -0.1102 -0.0772 480 HOH   A O   
6708 O O   . HOH   D .   ? 0.3611 0.2367 0.3191 -0.0654 -0.1202 0.0465  481 HOH   A O   
6709 O O   . HOH   D .   ? 0.2210 0.1875 0.2256 0.0093  0.0098  0.0052  482 HOH   A O   
6710 O O   . HOH   D .   ? 0.3024 0.4800 0.3207 0.1355  0.1075  0.1983  483 HOH   A O   
6711 O O   . HOH   D .   ? 0.2212 0.4186 0.4139 0.0006  0.0608  0.1100  484 HOH   A O   
6712 O O   . HOH   D .   ? 0.4847 0.4591 0.5052 -0.0718 -0.1205 0.0459  485 HOH   A O   
6713 O O   . HOH   D .   ? 0.4452 0.5959 0.3921 0.0245  0.0984  0.1070  486 HOH   A O   
6714 O O   . HOH   D .   ? 0.4646 0.3664 0.3460 -0.0104 0.1225  0.0063  487 HOH   A O   
6715 O O   . HOH   D .   ? 0.2551 0.1911 0.4364 0.0015  0.0407  0.0716  488 HOH   A O   
6716 O O   . HOH   D .   ? 0.3822 0.3269 0.2272 -0.0361 0.1256  -0.0155 489 HOH   A O   
6717 O O   . HOH   D .   ? 0.5232 0.3102 0.4643 -0.0708 0.2183  0.0269  490 HOH   A O   
6718 O O   . HOH   D .   ? 0.4677 0.5220 0.3813 -0.0365 -0.0712 -0.0468 491 HOH   A O   
6719 O O   . HOH   D .   ? 0.2297 0.2601 0.6251 -0.0160 -0.1273 0.0552  492 HOH   A O   
6720 O O   . HOH   D .   ? 0.4883 0.5228 0.5687 0.0908  0.0660  -0.1200 493 HOH   A O   
6721 O O   . HOH   D .   ? 0.3166 0.2596 0.3660 -0.0813 0.0124  0.0690  494 HOH   A O   
6722 O O   . HOH   D .   ? 0.3854 0.7554 0.4494 -0.1112 0.0159  0.2630  495 HOH   A O   
6723 O O   . HOH   D .   ? 0.2315 0.2969 0.3905 0.0016  0.0825  -0.0505 496 HOH   A O   
6724 O O   . HOH   D .   ? 0.4751 0.4746 0.4318 0.0861  -0.1241 0.0420  497 HOH   A O   
6725 O O   . HOH   D .   ? 0.6338 0.2597 0.4534 -0.0411 -0.0240 0.0743  498 HOH   A O   
6726 O O   . HOH   D .   ? 0.3053 0.4200 0.2598 -0.0325 -0.0133 -0.0649 499 HOH   A O   
6727 O O   . HOH   D .   ? 0.2341 0.2891 0.3479 0.0365  -0.0561 0.0408  500 HOH   A O   
6728 O O   . HOH   D .   ? 0.4108 0.2137 0.3626 -0.1163 0.0255  0.0010  501 HOH   A O   
6729 O O   . HOH   D .   ? 0.5290 0.5931 0.4586 0.1265  -0.0551 0.0378  502 HOH   A O   
6730 O O   . HOH   D .   ? 0.2822 0.4311 0.3671 0.0789  0.0168  0.0481  503 HOH   A O   
6731 O O   . HOH   D .   ? 0.6377 0.5146 0.5932 0.0743  0.0186  -0.0130 504 HOH   A O   
6732 O O   . HOH   D .   ? 0.4340 0.6105 0.4406 0.2690  -0.0217 0.0721  505 HOH   A O   
6733 O O   . HOH   D .   ? 0.3768 0.4661 0.4074 0.0149  -0.0482 -0.1355 506 HOH   A O   
6734 O O   . HOH   D .   ? 0.2673 0.2140 0.3881 0.0124  0.0396  0.0520  507 HOH   A O   
6735 O O   A HOH   D .   ? 0.3349 0.6463 0.3192 0.0709  0.1215  -0.0493 508 HOH   A O   
6736 O O   . HOH   D .   ? 0.2349 0.5973 0.3221 0.0302  0.0369  0.0094  509 HOH   A O   
6737 O O   . HOH   D .   ? 0.3369 0.4260 0.3471 0.0836  -0.0489 0.0735  510 HOH   A O   
6738 O O   . HOH   D .   ? 0.4430 0.5432 0.4886 -0.0936 -0.0801 -0.0101 511 HOH   A O   
6739 O O   . HOH   D .   ? 0.3179 0.3547 0.4791 -0.0651 -0.0994 0.2141  512 HOH   A O   
6740 O O   . HOH   E .   ? 0.2104 0.2107 0.2503 0.0341  0.0580  0.0279  201 HOH   B O   
6741 O O   . HOH   E .   ? 0.5016 0.4559 0.2273 0.0338  -0.0742 -0.1142 202 HOH   B O   
6742 O O   . HOH   E .   ? 0.2858 0.5066 0.4659 -0.0031 0.1473  -0.1835 203 HOH   B O   
6743 O O   . HOH   E .   ? 0.4904 0.3853 0.5809 0.0546  -0.1039 0.2393  204 HOH   B O   
6744 O O   . HOH   E .   ? 0.5958 0.5716 0.5136 0.1983  0.0349  0.0327  205 HOH   B O   
6745 O O   . HOH   E .   ? 0.4265 0.5313 0.4135 0.2569  -0.1053 -0.0076 206 HOH   B O   
6746 O O   . HOH   E .   ? 0.3228 0.6508 0.3357 0.0844  0.0294  0.1871  207 HOH   B O   
6747 O O   . HOH   E .   ? 0.4572 0.2848 0.3197 -0.0365 -0.0142 -0.1061 208 HOH   B O   
6748 O O   . HOH   E .   ? 0.6293 0.3899 0.5312 0.0786  0.1909  -0.0334 209 HOH   B O   
6749 O O   . HOH   E .   ? 0.3420 0.3773 0.5179 -0.0547 0.0594  -0.0511 210 HOH   B O   
6750 O O   . HOH   E .   ? 0.6278 0.3112 0.4118 -0.1985 0.0924  0.0375  211 HOH   B O   
6751 O O   . HOH   E .   ? 0.1881 0.2093 0.2618 0.0127  0.0182  -0.0198 212 HOH   B O   
6752 O O   . HOH   E .   ? 0.5627 0.4702 0.3698 -0.0659 -0.1001 0.1231  213 HOH   B O   
6753 O O   . HOH   E .   ? 0.2730 0.2886 0.7007 0.0761  -0.1162 0.0266  214 HOH   B O   
6754 O O   . HOH   E .   ? 0.3331 0.4078 0.4262 -0.1480 0.0399  0.0736  215 HOH   B O   
6755 O O   . HOH   E .   ? 0.4625 0.1832 0.3731 0.0165  -0.1039 -0.0005 216 HOH   B O   
6756 O O   . HOH   E .   ? 0.3913 0.4921 0.4197 0.2257  -0.0635 0.0255  217 HOH   B O   
6757 O O   . HOH   E .   ? 0.2957 0.5497 0.3531 0.1413  0.0335  -0.0678 218 HOH   B O   
6758 O O   . HOH   E .   ? 0.1475 0.1663 0.2382 -0.0172 0.0029  -0.0015 219 HOH   B O   
6759 O O   . HOH   E .   ? 0.5098 0.5842 0.2851 0.0759  -0.0620 -0.0156 220 HOH   B O   
6760 O O   . HOH   E .   ? 0.2349 0.4125 0.3574 -0.0655 0.0369  -0.0827 221 HOH   B O   
6761 O O   . HOH   E .   ? 0.4565 0.4780 0.5120 -0.0446 -0.0098 0.0469  222 HOH   B O   
6762 O O   . HOH   E .   ? 0.2590 0.2545 0.4482 -0.0057 0.0505  0.0296  223 HOH   B O   
6763 O O   . HOH   E .   ? 0.3361 0.6217 0.3460 0.1989  -0.0080 -0.0523 224 HOH   B O   
6764 O O   . HOH   E .   ? 0.2485 0.1687 0.2538 -0.0378 0.1056  0.0008  225 HOH   B O   
6765 O O   . HOH   E .   ? 0.3753 0.4228 0.5158 -0.1105 -0.0158 -0.1556 226 HOH   B O   
6766 O O   . HOH   E .   ? 0.3328 0.4540 0.3931 0.0218  0.0745  -0.1575 227 HOH   B O   
6767 O O   . HOH   E .   ? 0.3772 0.3621 0.2144 0.0736  0.0840  0.0698  228 HOH   B O   
6768 O O   . HOH   E .   ? 0.2513 0.2188 0.3035 0.0336  0.0268  -0.0875 229 HOH   B O   
6769 O O   . HOH   E .   ? 0.2105 0.2067 0.3237 -0.0354 -0.0273 -0.0477 230 HOH   B O   
6770 O O   . HOH   E .   ? 0.4540 0.4271 0.6175 0.0153  -0.1502 -0.0931 231 HOH   B O   
6771 O O   . HOH   E .   ? 0.2926 0.1977 0.4434 0.0151  0.1637  0.0813  232 HOH   B O   
6772 O O   . HOH   E .   ? 0.1549 0.1805 0.2312 -0.0119 0.0070  -0.0091 233 HOH   B O   
6773 O O   . HOH   E .   ? 0.2870 0.2074 0.2960 0.0057  0.0848  -0.0020 234 HOH   B O   
6774 O O   . HOH   E .   ? 0.2005 0.3880 0.2693 -0.0400 -0.0484 -0.0733 235 HOH   B O   
6775 O O   . HOH   E .   ? 0.1291 0.1195 0.1331 -0.0000 -0.0039 0.0026  236 HOH   B O   
6776 O O   . HOH   E .   ? 0.1753 0.4137 0.2120 -0.0522 -0.0137 0.0653  237 HOH   B O   
6777 O O   . HOH   E .   ? 0.2142 0.1835 0.1855 -0.0255 -0.0378 -0.0086 238 HOH   B O   
6778 O O   . HOH   E .   ? 0.1383 0.1321 0.1508 -0.0105 -0.0060 0.0029  239 HOH   B O   
6779 O O   . HOH   E .   ? 0.3498 0.1676 0.1889 0.0115  -0.0486 -0.0022 240 HOH   B O   
6780 O O   . HOH   E .   ? 0.2024 0.2025 0.2616 -0.0494 0.0139  -0.0272 241 HOH   B O   
6781 O O   . HOH   E .   ? 0.2534 0.4624 0.3595 -0.0977 -0.0265 -0.0938 242 HOH   B O   
6782 O O   . HOH   E .   ? 0.2005 0.1203 0.3225 0.0165  -0.0604 -0.0260 243 HOH   B O   
6783 O O   . HOH   E .   ? 0.1468 0.1372 0.2362 -0.0117 0.0125  -0.0178 244 HOH   B O   
6784 O O   . HOH   E .   ? 0.4285 0.2905 0.3793 -0.2032 0.0286  -0.0136 245 HOH   B O   
6785 O O   . HOH   E .   ? 0.5805 0.4332 0.5714 0.1516  -0.0211 -0.0827 246 HOH   B O   
6786 O O   . HOH   E .   ? 0.3855 0.2615 0.3929 0.1110  -0.0513 -0.0934 247 HOH   B O   
6787 O O   . HOH   E .   ? 0.2770 0.2110 0.2632 -0.0278 0.0151  -0.0447 248 HOH   B O   
6788 O O   . HOH   E .   ? 0.2671 0.2257 0.2877 0.0910  0.0983  0.0150  249 HOH   B O   
6789 O O   . HOH   E .   ? 0.2672 0.3982 0.4513 0.0648  0.0589  -0.0868 250 HOH   B O   
6790 O O   . HOH   E .   ? 0.2950 0.1591 0.5634 -0.0039 -0.1421 -0.0224 251 HOH   B O   
6791 O O   . HOH   E .   ? 0.1986 0.1934 0.1499 0.0074  -0.0053 -0.0009 252 HOH   B O   
6792 O O   . HOH   E .   ? 0.1279 0.1431 0.1690 -0.0023 0.0067  0.0016  253 HOH   B O   
6793 O O   . HOH   E .   ? 0.1523 0.1520 0.2310 -0.0118 -0.0192 0.0028  254 HOH   B O   
6794 O O   . HOH   E .   ? 0.1913 0.1267 0.1835 -0.0209 -0.0251 0.0231  255 HOH   B O   
6795 O O   . HOH   E .   ? 0.2145 0.3142 0.2301 -0.0527 0.0245  0.0751  256 HOH   B O   
6796 O O   . HOH   E .   ? 0.3378 0.3215 0.3988 0.0658  -0.1053 -0.1704 257 HOH   B O   
6797 O O   . HOH   E .   ? 0.2452 0.3160 0.4674 0.0930  -0.0607 -0.0745 258 HOH   B O   
6798 O O   . HOH   E .   ? 0.3834 0.5016 0.5017 -0.0017 -0.1089 0.0238  259 HOH   B O   
6799 O O   . HOH   E .   ? 0.1678 0.2500 0.2444 0.0470  0.0416  0.0978  260 HOH   B O   
6800 O O   . HOH   E .   ? 0.2375 0.1859 0.2783 -0.0584 0.0049  -0.0074 261 HOH   B O   
6801 O O   . HOH   E .   ? 0.4882 0.2878 0.2194 0.0597  0.0970  -0.0098 262 HOH   B O   
6802 O O   . HOH   E .   ? 0.3768 0.3060 0.3277 -0.0507 0.0713  -0.0705 263 HOH   B O   
6803 O O   . HOH   E .   ? 0.3157 0.5454 0.2655 0.1889  -0.0730 -0.0406 264 HOH   B O   
6804 O O   . HOH   E .   ? 0.2735 0.4932 0.3212 -0.0387 -0.0795 0.1076  265 HOH   B O   
6805 O O   . HOH   E .   ? 0.4308 0.4594 0.2339 0.1204  -0.0522 -0.0022 266 HOH   B O   
6806 O O   . HOH   E .   ? 0.3646 0.3840 0.4081 -0.0310 -0.1003 -0.0975 267 HOH   B O   
6807 O O   . HOH   E .   ? 0.2063 0.1976 0.1637 0.0155  -0.0063 0.0104  268 HOH   B O   
6808 O O   . HOH   E .   ? 0.2136 0.1850 0.3146 -0.0029 -0.0544 -0.0463 269 HOH   B O   
6809 O O   . HOH   E .   ? 0.1586 0.1311 0.4177 -0.0065 -0.0159 -0.0025 270 HOH   B O   
6810 O O   . HOH   E .   ? 0.2653 0.3169 0.1671 0.0485  0.0444  0.0085  271 HOH   B O   
6811 O O   . HOH   E .   ? 0.2246 0.2069 0.2331 0.0834  -0.0826 -0.0676 272 HOH   B O   
6812 O O   . HOH   E .   ? 0.1866 0.1375 0.1959 -0.0229 -0.0124 0.0104  273 HOH   B O   
6813 O O   . HOH   E .   ? 0.2370 0.2422 0.2488 -0.0424 -0.0650 -0.0400 274 HOH   B O   
6814 O O   . HOH   E .   ? 0.1686 0.1690 0.1371 -0.0364 -0.0277 0.0012  275 HOH   B O   
6815 O O   . HOH   E .   ? 0.2271 0.3519 0.3279 0.0339  0.0852  0.0197  276 HOH   B O   
6816 O O   . HOH   E .   ? 0.2655 0.5970 0.7040 0.1391  -0.0394 -0.1018 277 HOH   B O   
6817 O O   . HOH   E .   ? 0.1892 0.4163 0.4423 -0.0461 -0.0380 -0.1536 278 HOH   B O   
6818 O O   . HOH   E .   ? 0.1444 0.1467 0.2708 -0.0136 0.0092  0.0019  279 HOH   B O   
6819 O O   . HOH   E .   ? 0.2493 0.2690 0.2142 -0.0286 -0.0817 0.0035  280 HOH   B O   
6820 O O   . HOH   E .   ? 0.2542 0.2927 0.4375 -0.0195 0.0270  -0.1519 281 HOH   B O   
6821 O O   . HOH   E .   ? 0.2343 0.3718 0.3002 -0.0742 0.0816  -0.1492 282 HOH   B O   
6822 O O   . HOH   E .   ? 0.4028 0.2660 0.4668 -0.0857 0.0080  0.0957  283 HOH   B O   
6823 O O   . HOH   E .   ? 0.3855 0.3744 0.2454 0.0712  -0.0206 -0.1310 284 HOH   B O   
6824 O O   . HOH   E .   ? 0.2215 0.2434 0.2038 0.0799  -0.0262 -0.0132 285 HOH   B O   
6825 O O   . HOH   E .   ? 0.1439 0.1417 0.1527 0.0039  0.0046  -0.0009 286 HOH   B O   
6826 O O   . HOH   E .   ? 0.1444 0.2049 0.1303 -0.0164 -0.0142 -0.0022 287 HOH   B O   
6827 O O   . HOH   E .   ? 0.6198 0.4426 0.4295 -0.1135 -0.0104 0.0597  288 HOH   B O   
6828 O O   . HOH   E .   ? 0.1460 0.2637 0.4382 -0.0019 -0.0007 -0.1037 289 HOH   B O   
6829 O O   . HOH   E .   ? 0.3410 0.2710 0.1989 0.0697  -0.0683 -0.0268 290 HOH   B O   
6830 O O   . HOH   E .   ? 0.3667 0.3532 0.4167 0.1335  -0.1031 -0.0967 291 HOH   B O   
6831 O O   . HOH   E .   ? 0.2185 0.2403 0.2493 0.0201  -0.0640 0.0252  292 HOH   B O   
6832 O O   . HOH   E .   ? 0.2293 0.6171 0.2583 0.0407  0.0018  -0.0364 293 HOH   B O   
6833 O O   . HOH   E .   ? 0.3528 0.1920 0.3686 -0.0695 -0.1997 0.0378  294 HOH   B O   
6834 O O   . HOH   E .   ? 0.2544 0.2497 0.2337 0.0084  -0.0032 -0.1013 295 HOH   B O   
6835 O O   . HOH   E .   ? 0.2344 0.4555 0.4928 -0.0990 -0.1142 0.1216  296 HOH   B O   
6836 O O   . HOH   E .   ? 0.1888 0.1508 0.2309 -0.0143 -0.0218 -0.0091 297 HOH   B O   
6837 O O   . HOH   E .   ? 0.2617 0.2779 0.3936 -0.0773 0.1154  -0.0712 298 HOH   B O   
6838 O O   . HOH   E .   ? 0.4500 0.3760 0.2227 0.1115  -0.0766 0.0520  299 HOH   B O   
6839 O O   . HOH   E .   ? 0.1691 0.1441 0.2150 0.0086  -0.0013 0.0077  300 HOH   B O   
6840 O O   . HOH   E .   ? 0.4521 0.2295 0.2601 0.0519  0.0374  0.0861  301 HOH   B O   
6841 O O   . HOH   E .   ? 0.2372 0.1946 0.5413 0.0019  0.0718  0.0095  302 HOH   B O   
6842 O O   . HOH   E .   ? 0.1889 0.2322 0.5579 0.0379  -0.0418 -0.0836 303 HOH   B O   
6843 O O   . HOH   E .   ? 0.4938 0.6134 0.2486 -0.0184 -0.0277 0.1222  304 HOH   B O   
6844 O O   . HOH   E .   ? 0.1475 0.1765 0.2390 0.0175  -0.0133 0.0066  305 HOH   B O   
6845 O O   . HOH   E .   ? 0.5177 0.2790 0.2464 -0.1952 0.0845  -0.0197 306 HOH   B O   
6846 O O   . HOH   E .   ? 0.5303 0.3512 0.2684 0.2412  0.0977  0.0758  307 HOH   B O   
6847 O O   . HOH   E .   ? 0.2467 0.2937 0.2880 -0.0469 0.0688  -0.0686 308 HOH   B O   
6848 O O   . HOH   E .   ? 0.2088 0.2805 0.3659 -0.0155 -0.0756 0.0712  309 HOH   B O   
6849 O O   . HOH   E .   ? 0.1602 0.1380 0.2373 0.0079  -0.0012 -0.0064 310 HOH   B O   
6850 O O   . HOH   E .   ? 0.3312 0.1681 0.3232 0.0709  0.1389  0.0447  311 HOH   B O   
6851 O O   . HOH   E .   ? 0.2955 0.2413 0.4806 -0.0221 -0.0704 0.1007  312 HOH   B O   
6852 O O   . HOH   E .   ? 0.1503 0.1794 0.2093 -0.0241 -0.0047 0.0063  313 HOH   B O   
6853 O O   . HOH   E .   ? 0.6483 0.4382 0.4558 0.2020  0.0702  0.0197  314 HOH   B O   
6854 O O   . HOH   E .   ? 0.4153 0.3887 0.6207 0.1053  -0.0250 0.0603  315 HOH   B O   
6855 O O   . HOH   E .   ? 0.3701 0.3994 0.1467 -0.0287 0.0230  0.0159  316 HOH   B O   
6856 O O   . HOH   E .   ? 0.3830 0.2268 0.2717 0.1517  0.1010  0.0365  317 HOH   B O   
6857 O O   . HOH   E .   ? 0.2122 0.1360 0.2227 -0.0107 -0.0068 0.0227  318 HOH   B O   
6858 O O   . HOH   E .   ? 0.2060 0.1369 0.3275 0.0223  -0.1135 0.0033  319 HOH   B O   
6859 O O   . HOH   E .   ? 0.1872 0.1913 0.1527 -0.0046 0.0179  0.0143  320 HOH   B O   
6860 O O   . HOH   E .   ? 0.3886 0.2997 0.4877 0.0904  0.2071  0.1699  321 HOH   B O   
6861 O O   . HOH   E .   ? 0.2328 0.2061 0.2268 0.0115  -0.0319 0.0320  322 HOH   B O   
6862 O O   . HOH   E .   ? 0.2199 0.2990 0.4583 -0.0180 -0.0348 0.0084  323 HOH   B O   
6863 O O   . HOH   E .   ? 0.4586 0.4917 0.2849 -0.0219 -0.0982 0.0521  324 HOH   B O   
6864 O O   . HOH   E .   ? 0.1555 0.2597 0.2159 -0.0148 -0.0271 0.0545  325 HOH   B O   
6865 O O   . HOH   E .   ? 0.1529 0.1542 0.2389 -0.0123 -0.0021 -0.0178 326 HOH   B O   
6866 O O   . HOH   E .   ? 0.4156 0.4297 0.2159 0.0662  -0.0250 -0.0583 327 HOH   B O   
6867 O O   . HOH   E .   ? 0.7008 0.1767 0.2358 -0.0165 -0.0265 0.0061  328 HOH   B O   
6868 O O   . HOH   E .   ? 0.1747 0.1926 0.2746 0.0350  0.0324  0.0177  329 HOH   B O   
6869 O O   . HOH   E .   ? 0.6648 0.3098 0.3127 -0.0604 0.0919  0.1023  330 HOH   B O   
6870 O O   . HOH   E .   ? 0.2722 0.3497 0.6933 -0.0300 -0.0594 0.2064  331 HOH   B O   
6871 O O   . HOH   E .   ? 0.2410 0.1747 0.4936 0.0047  0.0137  -0.0010 332 HOH   B O   
6872 O O   . HOH   E .   ? 0.4575 0.3103 0.3688 0.0577  0.0033  -0.1410 333 HOH   B O   
6873 O O   . HOH   E .   ? 0.5367 0.4803 0.5576 0.0197  -0.0929 0.2210  334 HOH   B O   
6874 O O   . HOH   E .   ? 0.6295 0.5960 0.5334 0.2717  0.0589  -0.0011 335 HOH   B O   
6875 O O   . HOH   E .   ? 0.2140 0.2210 0.5142 -0.0440 0.0122  0.1328  336 HOH   B O   
6876 O O   . HOH   E .   ? 0.1565 0.1283 0.2066 0.0057  -0.0233 0.0025  337 HOH   B O   
6877 O O   . HOH   E .   ? 0.1605 0.2598 0.2877 0.0141  -0.0056 -0.0613 338 HOH   B O   
6878 O O   . HOH   E .   ? 0.6057 0.5572 0.5667 -0.0693 -0.0885 -0.1128 339 HOH   B O   
6879 O O   . HOH   E .   ? 0.1957 0.6106 0.4974 -0.0340 0.0324  -0.0678 340 HOH   B O   
6880 O O   . HOH   E .   ? 0.4990 0.3909 0.2999 0.1344  -0.1237 -0.0863 341 HOH   B O   
6881 O O   . HOH   E .   ? 0.4337 0.6281 0.2806 0.0397  0.0122  0.0684  342 HOH   B O   
6882 O O   . HOH   E .   ? 0.1878 0.5764 0.5731 0.0345  -0.0587 0.0444  343 HOH   B O   
6883 O O   . HOH   E .   ? 0.4017 0.4708 0.5012 -0.0174 -0.0933 0.0718  344 HOH   B O   
6884 O O   . HOH   E .   ? 0.4566 0.5584 0.3794 -0.0663 -0.1161 -0.0660 345 HOH   B O   
6885 O O   . HOH   E .   ? 0.1973 0.1846 0.2325 -0.0108 0.0439  -0.0160 346 HOH   B O   
6886 O O   . HOH   E .   ? 0.2003 0.3804 0.4706 0.0258  0.0350  0.0135  347 HOH   B O   
6887 O O   . HOH   E .   ? 0.2661 0.2240 0.5165 -0.0041 -0.0964 -0.0730 348 HOH   B O   
6888 O O   . HOH   E .   ? 0.2478 0.5417 0.3225 0.1684  -0.0599 -0.1427 349 HOH   B O   
6889 O O   . HOH   E .   ? 0.4381 0.5589 0.5858 0.0519  0.0126  -0.0898 350 HOH   B O   
6890 O O   . HOH   E .   ? 0.5260 0.5814 0.2523 0.0084  -0.0533 0.0841  351 HOH   B O   
6891 O O   . HOH   E .   ? 0.5087 0.5369 0.3958 -0.1341 0.0617  0.0886  352 HOH   B O   
6892 O O   . HOH   E .   ? 0.4793 0.3667 0.4093 0.1197  0.1173  -0.0406 353 HOH   B O   
6893 O O   . HOH   E .   ? 0.3483 0.4272 0.4311 -0.1808 -0.0085 0.0231  354 HOH   B O   
6894 O O   . HOH   E .   ? 0.3592 0.2239 0.3617 -0.0791 0.0018  -0.0986 355 HOH   B O   
6895 O O   . HOH   E .   ? 0.4169 0.2403 0.5087 -0.0747 0.1637  0.0190  356 HOH   B O   
6896 O O   . HOH   E .   ? 0.3578 0.2677 0.4070 -0.0811 -0.0101 -0.0655 357 HOH   B O   
6897 O O   . HOH   E .   ? 0.3870 0.3096 0.4362 0.0525  -0.1789 -0.0012 358 HOH   B O   
6898 O O   . HOH   E .   ? 0.2920 0.1795 0.3967 0.0490  -0.1180 -0.0619 359 HOH   B O   
6899 O O   . HOH   E .   ? 0.4285 0.5272 0.5071 -0.1010 -0.0324 -0.0195 360 HOH   B O   
6900 O O   . HOH   E .   ? 0.4137 0.5302 0.5465 0.1608  -0.1249 0.1784  361 HOH   B O   
6901 O O   . HOH   E .   ? 0.4209 0.6798 0.3140 0.2298  0.0201  0.0892  362 HOH   B O   
6902 O O   . HOH   E .   ? 0.2058 0.3152 0.6075 -0.0680 -0.0641 -0.0646 363 HOH   B O   
6903 O O   . HOH   E .   ? 0.4713 0.3908 0.5988 -0.0123 0.0771  0.1021  364 HOH   B O   
6904 O O   . HOH   E .   ? 0.5744 0.4582 0.3241 0.0786  -0.1340 0.0279  365 HOH   B O   
6905 O O   . HOH   E .   ? 0.5688 0.3983 0.4231 0.0741  0.1192  0.0575  366 HOH   B O   
6906 O O   . HOH   E .   ? 0.4985 0.3073 0.5497 -0.1177 -0.0573 0.0082  367 HOH   B O   
6907 O O   . HOH   E .   ? 0.5034 0.3990 0.4849 0.1456  -0.1363 0.0213  368 HOH   B O   
6908 O O   . HOH   E .   ? 0.4465 0.5588 0.5895 0.2562  0.0937  0.1040  369 HOH   B O   
6909 O O   . HOH   E .   ? 0.5042 0.1957 0.2940 0.0098  0.0185  0.0346  370 HOH   B O   
6910 O O   . HOH   E .   ? 0.4478 0.3342 0.4557 0.0309  -0.1627 -0.0282 371 HOH   B O   
6911 O O   . HOH   E .   ? 0.6355 0.3829 0.2902 -0.1203 -0.0932 -0.0563 372 HOH   B O   
6912 O O   . HOH   E .   ? 0.7136 0.6946 0.4817 0.2024  -0.1426 0.1143  373 HOH   B O   
6913 O O   . HOH   E .   ? 0.4191 0.5064 0.4447 -0.0451 -0.0666 -0.1122 374 HOH   B O   
6914 O O   . HOH   E .   ? 0.2363 0.3948 0.4160 0.0441  -0.0828 -0.0541 375 HOH   B O   
6915 O O   . HOH   E .   ? 0.4355 0.4710 0.4719 -0.0855 -0.0873 0.0669  376 HOH   B O   
6916 O O   . HOH   E .   ? 0.7003 0.3587 0.5609 -0.1001 -0.0139 -0.0133 377 HOH   B O   
6917 O O   . HOH   E .   ? 0.4784 0.6759 0.5910 0.1996  0.1000  0.2842  378 HOH   B O   
6918 O O   . HOH   E .   ? 0.2858 0.3734 0.1957 0.0617  0.0218  -0.0021 379 HOH   B O   
6919 O O   . HOH   E .   ? 0.3279 0.5219 0.4126 0.1158  -0.0157 0.0169  380 HOH   B O   
6920 O O   . HOH   E .   ? 0.5017 0.6614 0.3973 -0.1350 0.0792  -0.1410 381 HOH   B O   
6921 O O   . HOH   E .   ? 0.2957 0.2377 0.3066 0.0013  0.0047  0.0567  382 HOH   B O   
6922 O O   . HOH   E .   ? 0.3030 0.7238 0.5082 0.0878  0.1628  0.1439  383 HOH   B O   
6923 O O   . HOH   E .   ? 0.5553 0.6957 0.6088 -0.0180 0.2152  0.1232  384 HOH   B O   
6924 O O   . HOH   E .   ? 0.6434 0.6008 0.4154 0.2400  0.0448  0.0698  385 HOH   B O   
6925 O O   . HOH   E .   ? 0.3835 0.3200 0.2467 0.0270  0.0126  -0.0147 386 HOH   B O   
6926 O O   . HOH   E .   ? 0.6520 0.3419 0.4316 0.0819  0.0149  -0.1209 387 HOH   B O   
6927 O O   . HOH   E .   ? 0.5064 0.4542 0.5127 -0.0731 -0.0046 -0.0111 388 HOH   B O   
6928 O O   . HOH   E .   ? 0.2036 0.4131 0.3034 -0.0700 -0.0663 -0.0176 389 HOH   B O   
6929 O O   . HOH   E .   ? 0.4969 0.4384 0.3742 -0.0395 -0.0832 -0.0220 390 HOH   B O   
6930 O O   . HOH   E .   ? 0.4529 0.3745 0.3120 -0.0545 0.0075  0.0474  391 HOH   B O   
6931 O O   . HOH   E .   ? 0.3781 0.1976 0.3077 0.0806  -0.0388 0.0182  392 HOH   B O   
6932 O O   . HOH   E .   ? 0.4525 0.2134 0.4706 -0.0697 0.0671  0.0266  393 HOH   B O   
6933 O O   . HOH   E .   ? 0.2430 0.3900 0.5410 -0.1376 -0.0579 0.0103  394 HOH   B O   
6934 O O   . HOH   E .   ? 0.4458 0.5386 0.3220 0.1593  -0.0394 -0.0743 395 HOH   B O   
6935 O O   . HOH   E .   ? 0.4066 0.3594 0.3945 0.0074  0.1005  0.0679  396 HOH   B O   
6936 O O   . HOH   E .   ? 0.5465 0.5973 0.6649 0.1788  0.0005  0.2276  397 HOH   B O   
6937 O O   . HOH   E .   ? 0.1978 0.3198 0.4677 -0.0608 -0.0772 -0.0110 398 HOH   B O   
6938 O O   . HOH   E .   ? 0.2976 0.3622 0.3209 0.0569  0.0101  -0.0542 399 HOH   B O   
6939 O O   . HOH   E .   ? 0.6161 0.4001 0.3122 -0.1826 0.0586  0.1080  400 HOH   B O   
6940 O O   . HOH   E .   ? 0.5944 0.5725 0.3617 0.1709  -0.0407 0.0675  401 HOH   B O   
# 
